data_2IKC
# 
_entry.id   2IKC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2IKC         
RCSB  RCSB039678   
WWPDB D_1000039678 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2GJ1 'Crystal structure of Bovine lactoperoxidase at 2.3A resolution'   unspecified 
PDB 2GJM 'Crystal structure of Buffalo lactoperoxidase at 2.75A resolution' unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2IKC 
_pdbx_database_status.recvd_initial_deposition_date   2006-10-02 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Sheikh, I.A.' 1 
'Singh, N.'    2 
'Singh, A.K.'  3 
'Sharma, S.'   4 
'Singh, T.P.'  5 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structure of sheep lactoperoxidase at 3.25 A resolution reveals the binding sites for formate' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Sheikh, I.A.' 1 
primary 'Singh, N.'    2 
primary 'Singh, A.K.'  3 
primary 'Sharma, S.'   4 
primary 'Singh, T.P.'  5 
# 
_cell.entry_id           2IKC 
_cell.length_a           59.080 
_cell.length_b           72.590 
_cell.length_c           84.470 
_cell.angle_alpha        85.20 
_cell.angle_beta         84.07 
_cell.angle_gamma        75.41 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2IKC 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat 'milk lactoperoxidase'            67696.172 2   1.11.1.7 ? 'residues 1-595' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE            221.208   14  ?        ? ?                ? 
3 non-polymer man ALPHA-D-MANNOSE                   180.156   2   ?        ? ?                ? 
4 non-polymer syn 'CALCIUM ION'                     40.078    2   ?        ? ?                ? 
5 non-polymer syn 'CARBONATE ION'                   60.009    2   ?        ? ?                ? 
6 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ?        ? ?                ? 
7 non-polymer syn 'FORMIC ACID'                     46.025    6   ?        ? ?                ? 
8 water       nat water                             18.015    148 ?        ? ?                ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Peroxidase, Airway lactoperoxidase' 
# 
_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       
;SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSN
KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF
FRAGFVCPTPPYQSLARDQINSVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNMKPSPCEFI
NTTARVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEKLYQEARKILGAFIQIITFRDYLPIVLGSE
MQKWIPRYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPRGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL
AKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKL
LDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT
KVPLHAFQANNYPHDFVDCSAIDKLDLSPWASREN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSN
KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF
FRAGFVCPTPPYQSLARDQINSVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNMKPSPCEFI
NTTARVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEKLYQEARKILGAFIQIITFRDYLPIVLGSE
MQKWIPRYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPRGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLL
AKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKL
LDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHIT
KVPLHAFQANNYPHDFVDCSAIDKLDLSPWASREN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
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   TRP n 
1 3   GLU n 
1 4   VAL n 
1 5   GLY n 
1 6   CYS n 
1 7   GLY n 
1 8   ALA n 
1 9   PRO n 
1 10  VAL n 
1 11  PRO n 
1 12  LEU n 
1 13  VAL n 
1 14  LYS n 
1 15  CYS n 
1 16  ASP n 
1 17  GLU n 
1 18  ASN n 
1 19  SER n 
1 20  PRO n 
1 21  TYR n 
1 22  ARG n 
1 23  THR n 
1 24  ILE n 
1 25  THR n 
1 26  GLY n 
1 27  ASP n 
1 28  CYS n 
1 29  ASN n 
1 30  ASN n 
1 31  ARG n 
1 32  ARG n 
1 33  SER n 
1 34  PRO n 
1 35  ALA n 
1 36  LEU n 
1 37  GLY n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  ARG n 
1 42  ALA n 
1 43  LEU n 
1 44  ALA n 
1 45  ARG n 
1 46  TRP n 
1 47  LEU n 
1 48  PRO n 
1 49  ALA n 
1 50  GLU n 
1 51  TYR n 
1 52  GLU n 
1 53  ASP n 
1 54  GLY n 
1 55  LEU n 
1 56  ALA n 
1 57  VAL n 
1 58  PRO n 
1 59  PHE n 
1 60  GLY n 
1 61  TRP n 
1 62  THR n 
1 63  GLN n 
1 64  ARG n 
1 65  LYS n 
1 66  THR n 
1 67  ARG n 
1 68  ASN n 
1 69  GLY n 
1 70  PHE n 
1 71  ARG n 
1 72  VAL n 
1 73  PRO n 
1 74  LEU n 
1 75  ALA n 
1 76  ARG n 
1 77  GLU n 
1 78  VAL n 
1 79  SER n 
1 80  ASN n 
1 81  LYS n 
1 82  ILE n 
1 83  VAL n 
1 84  GLY n 
1 85  TYR n 
1 86  LEU n 
1 87  ASP n 
1 88  GLU n 
1 89  GLU n 
1 90  GLY n 
1 91  VAL n 
1 92  LEU n 
1 93  ASP n 
1 94  GLN n 
1 95  ASN n 
1 96  ARG n 
1 97  SER n 
1 98  LEU n 
1 99  LEU n 
1 100 PHE n 
1 101 MET n 
1 102 GLN n 
1 103 TRP n 
1 104 GLY n 
1 105 GLN n 
1 106 ILE n 
1 107 VAL n 
1 108 ASP n 
1 109 HIS n 
1 110 ASP n 
1 111 LEU n 
1 112 ASP n 
1 113 PHE n 
1 114 ALA n 
1 115 PRO n 
1 116 GLU n 
1 117 THR n 
1 118 GLU n 
1 119 LEU n 
1 120 GLY n 
1 121 SER n 
1 122 SER n 
1 123 GLU n 
1 124 HIS n 
1 125 SER n 
1 126 LYS n 
1 127 VAL n 
1 128 GLN n 
1 129 CYS n 
1 130 GLU n 
1 131 GLU n 
1 132 TYR n 
1 133 CYS n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 ASP n 
1 138 ASN n 
1 139 CYS n 
1 140 PHE n 
1 141 PRO n 
1 142 ILE n 
1 143 MET n 
1 144 PHE n 
1 145 PRO n 
1 146 LYS n 
1 147 ASN n 
1 148 ASP n 
1 149 PRO n 
1 150 LYS n 
1 151 LEU n 
1 152 LYS n 
1 153 THR n 
1 154 GLN n 
1 155 GLY n 
1 156 LYS n 
1 157 CYS n 
1 158 MET n 
1 159 PRO n 
1 160 PHE n 
1 161 PHE n 
1 162 ARG n 
1 163 ALA n 
1 164 GLY n 
1 165 PHE n 
1 166 VAL n 
1 167 CYS n 
1 168 PRO n 
1 169 THR n 
1 170 PRO n 
1 171 PRO n 
1 172 TYR n 
1 173 GLN n 
1 174 SER n 
1 175 LEU n 
1 176 ALA n 
1 177 ARG n 
1 178 ASP n 
1 179 GLN n 
1 180 ILE n 
1 181 ASN n 
1 182 SER n 
1 183 VAL n 
1 184 THR n 
1 185 SER n 
1 186 PHE n 
1 187 LEU n 
1 188 ASP n 
1 189 ALA n 
1 190 SER n 
1 191 LEU n 
1 192 VAL n 
1 193 TYR n 
1 194 GLY n 
1 195 SER n 
1 196 GLU n 
1 197 PRO n 
1 198 SER n 
1 199 LEU n 
1 200 ALA n 
1 201 SER n 
1 202 ARG n 
1 203 LEU n 
1 204 ARG n 
1 205 ASN n 
1 206 LEU n 
1 207 SER n 
1 208 SER n 
1 209 PRO n 
1 210 LEU n 
1 211 GLY n 
1 212 LEU n 
1 213 MET n 
1 214 ALA n 
1 215 VAL n 
1 216 ASN n 
1 217 GLN n 
1 218 GLU n 
1 219 ALA n 
1 220 TRP n 
1 221 ASP n 
1 222 HIS n 
1 223 GLY n 
1 224 LEU n 
1 225 ALA n 
1 226 TYR n 
1 227 PRO n 
1 228 PRO n 
1 229 PHE n 
1 230 ASN n 
1 231 ASN n 
1 232 MET n 
1 233 LYS n 
1 234 PRO n 
1 235 SER n 
1 236 PRO n 
1 237 CYS n 
1 238 GLU n 
1 239 PHE n 
1 240 ILE n 
1 241 ASN n 
1 242 THR n 
1 243 THR n 
1 244 ALA n 
1 245 ARG n 
1 246 VAL n 
1 247 PRO n 
1 248 CYS n 
1 249 PHE n 
1 250 GLN n 
1 251 ALA n 
1 252 GLY n 
1 253 ASP n 
1 254 SER n 
1 255 ARG n 
1 256 ALA n 
1 257 SER n 
1 258 GLU n 
1 259 GLN n 
1 260 ILE n 
1 261 LEU n 
1 262 LEU n 
1 263 ALA n 
1 264 THR n 
1 265 VAL n 
1 266 HIS n 
1 267 THR n 
1 268 LEU n 
1 269 LEU n 
1 270 LEU n 
1 271 ARG n 
1 272 GLU n 
1 273 HIS n 
1 274 ASN n 
1 275 ARG n 
1 276 LEU n 
1 277 ALA n 
1 278 ARG n 
1 279 GLU n 
1 280 LEU n 
1 281 LYS n 
1 282 ARG n 
1 283 LEU n 
1 284 ASN n 
1 285 PRO n 
1 286 HIS n 
1 287 TRP n 
1 288 ASP n 
1 289 GLY n 
1 290 GLU n 
1 291 LYS n 
1 292 LEU n 
1 293 TYR n 
1 294 GLN n 
1 295 GLU n 
1 296 ALA n 
1 297 ARG n 
1 298 LYS n 
1 299 ILE n 
1 300 LEU n 
1 301 GLY n 
1 302 ALA n 
1 303 PHE n 
1 304 ILE n 
1 305 GLN n 
1 306 ILE n 
1 307 ILE n 
1 308 THR n 
1 309 PHE n 
1 310 ARG n 
1 311 ASP n 
1 312 TYR n 
1 313 LEU n 
1 314 PRO n 
1 315 ILE n 
1 316 VAL n 
1 317 LEU n 
1 318 GLY n 
1 319 SER n 
1 320 GLU n 
1 321 MET n 
1 322 GLN n 
1 323 LYS n 
1 324 TRP n 
1 325 ILE n 
1 326 PRO n 
1 327 ARG n 
1 328 TYR n 
1 329 GLN n 
1 330 GLY n 
1 331 TYR n 
1 332 ASN n 
1 333 ASN n 
1 334 SER n 
1 335 VAL n 
1 336 ASP n 
1 337 PRO n 
1 338 ARG n 
1 339 ILE n 
1 340 SER n 
1 341 ASN n 
1 342 VAL n 
1 343 PHE n 
1 344 THR n 
1 345 PHE n 
1 346 ALA n 
1 347 PHE n 
1 348 ARG n 
1 349 PHE n 
1 350 GLY n 
1 351 HIS n 
1 352 MET n 
1 353 GLU n 
1 354 VAL n 
1 355 PRO n 
1 356 SER n 
1 357 THR n 
1 358 VAL n 
1 359 SER n 
1 360 ARG n 
1 361 LEU n 
1 362 ASP n 
1 363 GLU n 
1 364 ASN n 
1 365 TYR n 
1 366 GLN n 
1 367 PRO n 
1 368 ARG n 
1 369 GLY n 
1 370 PRO n 
1 371 GLU n 
1 372 ALA n 
1 373 GLU n 
1 374 LEU n 
1 375 PRO n 
1 376 LEU n 
1 377 HIS n 
1 378 THR n 
1 379 LEU n 
1 380 PHE n 
1 381 PHE n 
1 382 ASN n 
1 383 THR n 
1 384 TRP n 
1 385 ARG n 
1 386 ILE n 
1 387 ILE n 
1 388 LYS n 
1 389 ASP n 
1 390 GLY n 
1 391 GLY n 
1 392 ILE n 
1 393 ASP n 
1 394 PRO n 
1 395 LEU n 
1 396 VAL n 
1 397 ARG n 
1 398 GLY n 
1 399 LEU n 
1 400 LEU n 
1 401 ALA n 
1 402 LYS n 
1 403 LYS n 
1 404 SER n 
1 405 LYS n 
1 406 LEU n 
1 407 MET n 
1 408 ASN n 
1 409 GLN n 
1 410 ASN n 
1 411 LYS n 
1 412 MET n 
1 413 VAL n 
1 414 THR n 
1 415 SER n 
1 416 GLU n 
1 417 LEU n 
1 418 ARG n 
1 419 ASN n 
1 420 LYS n 
1 421 LEU n 
1 422 PHE n 
1 423 GLN n 
1 424 PRO n 
1 425 THR n 
1 426 HIS n 
1 427 LYS n 
1 428 ILE n 
1 429 HIS n 
1 430 GLY n 
1 431 PHE n 
1 432 ASP n 
1 433 LEU n 
1 434 ALA n 
1 435 ALA n 
1 436 ILE n 
1 437 ASN n 
1 438 LEU n 
1 439 GLN n 
1 440 ARG n 
1 441 CYS n 
1 442 ARG n 
1 443 ASP n 
1 444 HIS n 
1 445 GLY n 
1 446 MET n 
1 447 PRO n 
1 448 GLY n 
1 449 TYR n 
1 450 ASN n 
1 451 SER n 
1 452 TRP n 
1 453 ARG n 
1 454 GLY n 
1 455 PHE n 
1 456 CYS n 
1 457 GLY n 
1 458 LEU n 
1 459 SER n 
1 460 GLN n 
1 461 PRO n 
1 462 LYS n 
1 463 THR n 
1 464 LEU n 
1 465 LYS n 
1 466 GLY n 
1 467 LEU n 
1 468 GLN n 
1 469 ALA n 
1 470 VAL n 
1 471 LEU n 
1 472 LYS n 
1 473 ASN n 
1 474 LYS n 
1 475 ILE n 
1 476 LEU n 
1 477 ALA n 
1 478 LYS n 
1 479 LYS n 
1 480 LEU n 
1 481 LEU n 
1 482 ASP n 
1 483 LEU n 
1 484 TYR n 
1 485 LYS n 
1 486 THR n 
1 487 PRO n 
1 488 ASP n 
1 489 ASN n 
1 490 ILE n 
1 491 ASP n 
1 492 ILE n 
1 493 TRP n 
1 494 ILE n 
1 495 GLY n 
1 496 GLY n 
1 497 ASN n 
1 498 ALA n 
1 499 GLU n 
1 500 PRO n 
1 501 MET n 
1 502 VAL n 
1 503 GLU n 
1 504 ARG n 
1 505 GLY n 
1 506 ARG n 
1 507 VAL n 
1 508 GLY n 
1 509 PRO n 
1 510 LEU n 
1 511 LEU n 
1 512 ALA n 
1 513 CYS n 
1 514 LEU n 
1 515 LEU n 
1 516 GLY n 
1 517 ARG n 
1 518 GLN n 
1 519 PHE n 
1 520 GLN n 
1 521 GLN n 
1 522 ILE n 
1 523 ARG n 
1 524 ASP n 
1 525 GLY n 
1 526 ASP n 
1 527 ARG n 
1 528 PHE n 
1 529 TRP n 
1 530 TRP n 
1 531 GLU n 
1 532 ASN n 
1 533 PRO n 
1 534 GLY n 
1 535 VAL n 
1 536 PHE n 
1 537 THR n 
1 538 GLU n 
1 539 LYS n 
1 540 GLN n 
1 541 ARG n 
1 542 ASP n 
1 543 SER n 
1 544 LEU n 
1 545 GLN n 
1 546 LYS n 
1 547 VAL n 
1 548 SER n 
1 549 PHE n 
1 550 SER n 
1 551 ARG n 
1 552 LEU n 
1 553 ILE n 
1 554 CYS n 
1 555 ASP n 
1 556 ASN n 
1 557 THR n 
1 558 HIS n 
1 559 ILE n 
1 560 THR n 
1 561 LYS n 
1 562 VAL n 
1 563 PRO n 
1 564 LEU n 
1 565 HIS n 
1 566 ALA n 
1 567 PHE n 
1 568 GLN n 
1 569 ALA n 
1 570 ASN n 
1 571 ASN n 
1 572 TYR n 
1 573 PRO n 
1 574 HIS n 
1 575 ASP n 
1 576 PHE n 
1 577 VAL n 
1 578 ASP n 
1 579 CYS n 
1 580 SER n 
1 581 ALA n 
1 582 ILE n 
1 583 ASP n 
1 584 LYS n 
1 585 LEU n 
1 586 ASP n 
1 587 LEU n 
1 588 SER n 
1 589 PRO n 
1 590 TRP n 
1 591 ALA n 
1 592 SER n 
1 593 ARG n 
1 594 GLU n 
1 595 ASN n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                sheep 
_entity_src_nat.pdbx_organism_scientific   'Ovis aries' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      9940 
_entity_src_nat.genus                      Ovis 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9MZY2_SHEEP 
_struct_ref.pdbx_db_accession          Q9MZY2 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_align_begin           118 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
# 
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 2IKC A 1 ? 595 ? Q9MZY2 118 ? 712 ? 1 595 
2 1 2IKC B 1 ? 595 ? Q9MZY2 118 ? 712 ? 1 595 
# 
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 
CA  non-polymer         . 'CALCIUM ION'                     ?    'Ca 2'             40.078  
CO3 non-polymer         . 'CARBONATE ION'                   ?    'C O3 -2'          60.009  
CYS 'L-peptide linking' y CYSTEINE                          ?    'C3 H7 N O2 S'     121.158 
FMT non-polymer         . 'FORMIC ACID'                     ?    'C H2 O2'          46.025  
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
MAN D-saccharide        . ALPHA-D-MANNOSE                   ?    'C6 H12 O6'        180.156 
MET 'L-peptide linking' y METHIONINE                        ?    'C5 H11 N O2 S'    149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE            ?    'C8 H15 N O6'      221.208 
PHE 'L-peptide linking' y PHENYLALANINE                     ?    'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                           ?    'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?    'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
_exptl.entry_id          2IKC 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.57 
_exptl_crystal.density_percent_sol   52.13 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           295 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.pdbx_collection_date   2006-09-20 
_diffrn_detector.details                Mirror 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    graphite 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54132 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU300' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.54132 
# 
_reflns.entry_id                     2IKC 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             19.97 
_reflns.d_resolution_high            3.25 
_reflns.number_obs                   20388 
_reflns.number_all                   20423 
_reflns.percent_possible_obs         96.5 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        37.9 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             3.25 
_reflns_shell.d_res_low              3.31 
_reflns_shell.percent_possible_all   96.5 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2IKC 
_refine.ls_number_reflns_obs                     20328 
_refine.ls_number_reflns_all                     20423 
_refine.pdbx_ls_sigma_I                          0 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               30133.34 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.97 
_refine.ls_d_res_high                            3.25 
_refine.ls_percent_reflns_obs                    96.4 
_refine.ls_R_factor_obs                          0.187 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.187 
_refine.ls_R_factor_R_free                       0.23 
_refine.ls_R_factor_R_free_error                 0.009 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 2.9 
_refine.ls_number_reflns_R_free                  600 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               11.0 
_refine.aniso_B[1][1]                            7.33 
_refine.aniso_B[2][2]                            -4.54 
_refine.aniso_B[3][3]                            -2.79 
_refine.aniso_B[1][2]                            9.48 
_refine.aniso_B[1][3]                            2.13 
_refine.aniso_B[2][3]                            -1.60 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.366155 
_refine.solvent_model_param_bsol                 72.4964 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      2GJ1 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2IKC 
_refine_analyze.Luzzati_coordinate_error_obs    0.29 
_refine_analyze.Luzzati_sigma_a_obs             0.37 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.37 
_refine_analyze.Luzzati_sigma_a_free            0.54 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        9528 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         332 
_refine_hist.number_atoms_solvent             148 
_refine_hist.number_atoms_total               10008 
_refine_hist.d_res_high                       3.25 
_refine_hist.d_res_low                        19.97 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.013 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             2.2   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      24.3  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.26  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.28  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.17  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             1.80  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            3.00  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       3.25 
_refine_ls_shell.d_res_low                        3.45 
_refine_ls_shell.number_reflns_R_work             3293 
_refine_ls_shell.R_factor_R_work                  0.237 
_refine_ls_shell.percent_reflns_obs               96.2 
_refine_ls_shell.R_factor_R_free                  0.308 
_refine_ls_shell.R_factor_R_free_error            0.032 
_refine_ls_shell.percent_reflns_R_free            2.7 
_refine_ls_shell.number_reflns_R_free             91 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param  protein.top      'X-RAY DIFFRACTION' 
2 ion.param          ion.top          'X-RAY DIFFRACTION' 
3 water_rep.param    water.top        'X-RAY DIFFRACTION' 
4 all.param          all.top          'X-RAY DIFFRACTION' 
5 carbohydrate.param carbohydrate.top 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2IKC 
_struct.title                     
'Crystal structure of sheep lactoperoxidase at 3.25 A resolution reveals the binding sites for formate' 
_struct.pdbx_descriptor           'Milk lactoperoxidase (E.C.1.11.1.7)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2IKC 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'Peroxidase, Formate, Heme, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 2 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 2 ? 
K  N N 4 ? 
L  N N 5 ? 
M  N N 6 ? 
N  N N 7 ? 
O  N N 7 ? 
P  N N 7 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 2 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 2 ? 
Y  N N 4 ? 
Z  N N 5 ? 
AA N N 6 ? 
BA N N 7 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 8 ? 
FA N N 8 ? 
# 
_struct_biol.id   1 
# 
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  1  LEU A 74  ? ILE A 82  ? LEU A 74  ILE A 82  1 ? 9  
HELX_P HELX_P2  2  LEU A 98  ? ASP A 112 ? LEU A 98  ASP A 112 1 ? 15 
HELX_P HELX_P3  3  ASP A 148 ? GLN A 154 ? ASP A 148 GLN A 154 1 ? 7  
HELX_P HELX_P4  4  ALA A 189 ? GLY A 194 ? ALA A 189 GLY A 194 1 ? 6  
HELX_P HELX_P5  5  GLU A 196 ? LEU A 203 ? GLU A 196 LEU A 203 1 ? 8  
HELX_P HELX_P6  6  SER A 235 ? ASN A 241 ? SER A 235 ASN A 241 1 ? 7  
HELX_P HELX_P7  7  ASP A 253 ? GLU A 258 ? ASP A 253 GLU A 258 5 ? 6  
HELX_P HELX_P8  8  GLN A 259 ? ASN A 284 ? GLN A 259 ASN A 284 1 ? 26 
HELX_P HELX_P9  9  ASP A 288 ? ASP A 311 ? ASP A 288 ASP A 311 1 ? 24 
HELX_P HELX_P10 10 LEU A 313 ? GLY A 318 ? LEU A 313 GLY A 318 1 ? 6  
HELX_P HELX_P11 11 GLU A 320 ? ILE A 325 ? GLU A 320 ILE A 325 1 ? 6  
HELX_P HELX_P12 12 VAL A 342 ? PHE A 347 ? VAL A 342 PHE A 347 1 ? 6  
HELX_P HELX_P13 13 ARG A 348 ? GLU A 353 ? ARG A 348 GLU A 353 5 ? 6  
HELX_P HELX_P14 14 HIS A 377 ? PHE A 380 ? HIS A 377 PHE A 380 5 ? 4  
HELX_P HELX_P15 15 THR A 383 ? LYS A 388 ? THR A 383 LYS A 388 1 ? 6  
HELX_P HELX_P16 16 ILE A 392 ? LYS A 402 ? ILE A 392 LYS A 402 1 ? 11 
HELX_P HELX_P17 17 THR A 414 ? ASN A 419 ? THR A 414 ASN A 419 1 ? 6  
HELX_P HELX_P18 18 ASP A 432 ? HIS A 444 ? ASP A 432 HIS A 444 1 ? 13 
HELX_P HELX_P19 19 TYR A 449 ? CYS A 456 ? TYR A 449 CYS A 456 1 ? 8  
HELX_P HELX_P20 20 THR A 463 ? LYS A 472 ? THR A 463 LYS A 472 1 ? 10 
HELX_P HELX_P21 21 ASN A 473 ? LYS A 485 ? ASN A 473 LYS A 485 1 ? 13 
HELX_P HELX_P22 22 THR A 486 ? ILE A 490 ? THR A 486 ILE A 490 5 ? 5  
HELX_P HELX_P23 23 ASP A 491 ? GLU A 499 ? ASP A 491 GLU A 499 1 ? 9  
HELX_P HELX_P24 24 GLY A 508 ? GLY A 525 ? GLY A 508 GLY A 525 1 ? 18 
HELX_P HELX_P25 25 THR A 537 ? GLN A 545 ? THR A 537 GLN A 545 1 ? 9  
HELX_P HELX_P26 26 SER A 548 ? ASN A 556 ? SER A 548 ASN A 556 1 ? 9  
HELX_P HELX_P27 27 SER A 580 ? ILE A 582 ? SER A 580 ILE A 582 5 ? 3  
HELX_P HELX_P28 28 LEU A 587 ? ALA A 591 ? LEU A 587 ALA A 591 5 ? 5  
HELX_P HELX_P29 29 LEU B 74  ? VAL B 83  ? LEU B 74  VAL B 83  1 ? 10 
HELX_P HELX_P30 30 LEU B 98  ? ASP B 112 ? LEU B 98  ASP B 112 1 ? 15 
HELX_P HELX_P31 31 HIS B 124 ? GLU B 131 ? HIS B 124 GLU B 131 1 ? 8  
HELX_P HELX_P32 32 PRO B 149 ? GLN B 154 ? PRO B 149 GLN B 154 1 ? 6  
HELX_P HELX_P33 33 ALA B 189 ? GLY B 194 ? ALA B 189 GLY B 194 1 ? 6  
HELX_P HELX_P34 34 GLU B 196 ? LEU B 203 ? GLU B 196 LEU B 203 1 ? 8  
HELX_P HELX_P35 35 SER B 235 ? ILE B 240 ? SER B 235 ILE B 240 1 ? 6  
HELX_P HELX_P36 36 GLN B 259 ? ASN B 284 ? GLN B 259 ASN B 284 1 ? 26 
HELX_P HELX_P37 37 ASP B 288 ? ASP B 311 ? ASP B 288 ASP B 311 1 ? 24 
HELX_P HELX_P38 38 LEU B 313 ? GLY B 318 ? LEU B 313 GLY B 318 1 ? 6  
HELX_P HELX_P39 39 GLU B 320 ? ILE B 325 ? GLU B 320 ILE B 325 1 ? 6  
HELX_P HELX_P40 40 VAL B 342 ? PHE B 347 ? VAL B 342 PHE B 347 1 ? 6  
HELX_P HELX_P41 41 ARG B 348 ? VAL B 354 ? ARG B 348 VAL B 354 5 ? 7  
HELX_P HELX_P42 42 HIS B 377 ? PHE B 380 ? HIS B 377 PHE B 380 5 ? 4  
HELX_P HELX_P43 43 THR B 383 ? LYS B 388 ? THR B 383 LYS B 388 1 ? 6  
HELX_P HELX_P44 44 ILE B 392 ? LYS B 402 ? ILE B 392 LYS B 402 1 ? 11 
HELX_P HELX_P45 45 THR B 414 ? ASN B 419 ? THR B 414 ASN B 419 1 ? 6  
HELX_P HELX_P46 46 ASP B 432 ? GLY B 445 ? ASP B 432 GLY B 445 1 ? 14 
HELX_P HELX_P47 47 GLY B 448 ? GLY B 457 ? GLY B 448 GLY B 457 1 ? 10 
HELX_P HELX_P48 48 THR B 463 ? LYS B 472 ? THR B 463 LYS B 472 1 ? 10 
HELX_P HELX_P49 49 ASN B 473 ? LYS B 485 ? ASN B 473 LYS B 485 1 ? 13 
HELX_P HELX_P50 50 THR B 486 ? ILE B 490 ? THR B 486 ILE B 490 5 ? 5  
HELX_P HELX_P51 51 ASP B 491 ? GLU B 499 ? ASP B 491 GLU B 499 1 ? 9  
HELX_P HELX_P52 52 GLY B 508 ? GLY B 525 ? GLY B 508 GLY B 525 1 ? 18 
HELX_P HELX_P53 53 THR B 537 ? GLN B 545 ? THR B 537 GLN B 545 1 ? 9  
HELX_P HELX_P54 54 SER B 548 ? THR B 557 ? SER B 548 THR B 557 1 ? 10 
HELX_P HELX_P55 55 SER B 580 ? ILE B 582 ? SER B 580 ILE B 582 5 ? 3  
HELX_P HELX_P56 56 LEU B 587 ? ALA B 591 ? LEU B 587 ALA B 591 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 6   SG  ? ? ? 1_555 A CYS 167 SG  ? ? A CYS 6   A CYS 167  1_555 ? ? ? ? ? ? ? 2.226 ? 
disulf2  disulf ? ? A  CYS 15  SG  ? ? ? 1_555 A CYS 28  SG  ? ? A CYS 15  A CYS 28   1_555 ? ? ? ? ? ? ? 2.245 ? 
disulf3  disulf ? ? A  CYS 129 SG  ? ? ? 1_555 A CYS 139 SG  ? ? A CYS 129 A CYS 139  1_555 ? ? ? ? ? ? ? 1.874 ? 
disulf4  disulf ? ? A  CYS 133 SG  ? ? ? 1_555 A CYS 157 SG  ? ? A CYS 133 A CYS 157  1_555 ? ? ? ? ? ? ? 1.983 ? 
disulf5  disulf ? ? A  CYS 237 SG  ? ? ? 1_555 A CYS 248 SG  ? ? A CYS 237 A CYS 248  1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf6  disulf ? ? A  CYS 456 SG  ? ? ? 1_555 A CYS 513 SG  ? ? A CYS 456 A CYS 513  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf7  disulf ? ? A  CYS 554 SG  ? ? ? 1_555 A CYS 579 SG  ? ? A CYS 554 A CYS 579  1_555 ? ? ? ? ? ? ? 2.025 ? 
disulf8  disulf ? ? B  CYS 6   SG  ? ? ? 1_555 B CYS 167 SG  ? ? B CYS 6   B CYS 167  1_555 ? ? ? ? ? ? ? 2.089 ? 
disulf9  disulf ? ? B  CYS 15  SG  ? ? ? 1_555 B CYS 28  SG  ? ? B CYS 15  B CYS 28   1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf10 disulf ? ? B  CYS 129 SG  ? ? ? 1_555 B CYS 139 SG  ? ? B CYS 129 B CYS 139  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf11 disulf ? ? B  CYS 133 SG  ? ? ? 1_555 B CYS 157 SG  ? ? B CYS 133 B CYS 157  1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf12 disulf ? ? B  CYS 237 SG  ? ? ? 1_555 B CYS 248 SG  ? ? B CYS 237 B CYS 248  1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf13 disulf ? ? B  CYS 456 SG  ? ? ? 1_555 B CYS 513 SG  ? ? B CYS 456 B CYS 513  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf14 disulf ? ? B  CYS 554 SG  ? ? ? 1_555 B CYS 579 SG  ? ? B CYS 554 B CYS 579  1_555 ? ? ? ? ? ? ? 2.012 ? 
metalc1  metalc ? ? M  HEM .   FE  ? ? ? 1_555 A HIS 351 NE2 ? ? A HEM 605 A HIS 351  1_555 ? ? ? ? ? ? ? 2.174 ? 
covale1  covale ? ? M  HEM .   CMD ? ? ? 1_555 A ASP 108 OD2 ? ? A HEM 605 A ASP 108  1_555 ? ? ? ? ? ? ? 1.806 ? 
covale2  covale ? ? M  HEM .   CMB ? ? ? 1_555 A GLU 258 OE2 ? ? A HEM 605 A GLU 258  1_555 ? ? ? ? ? ? ? 1.511 ? 
metalc2  metalc ? ? AA HEM .   FE  ? ? ? 1_555 B HIS 351 NE2 ? ? B HEM 605 B HIS 351  1_555 ? ? ? ? ? ? ? 2.350 ? 
covale3  covale ? ? AA HEM .   CMD ? ? ? 1_555 B ASP 108 OD2 ? ? B HEM 605 B ASP 108  1_555 ? ? ? ? ? ? ? 1.516 ? 
covale4  covale ? ? AA HEM .   CMB ? ? ? 1_555 B GLU 258 OE2 ? ? B HEM 605 B GLU 258  1_555 ? ? ? ? ? ? ? 1.574 ? 
covale5  covale ? ? A  ASN 95  ND2 ? ? ? 1_555 C NAG .   C1  ? ? A ASN 95  A NAG 596  1_555 ? ? ? ? ? ? ? 1.390 ? 
covale6  covale ? ? A  ASN 205 ND2 ? ? ? 1_555 E NAG .   C1  ? ? A ASN 205 A NAG 598  1_555 ? ? ? ? ? ? ? 1.452 ? 
covale7  covale ? ? A  ASN 241 ND2 ? ? ? 1_555 G NAG .   C1  ? ? A ASN 241 A NAG 600  1_555 ? ? ? ? ? ? ? 1.448 ? 
covale8  covale ? ? A  ASN 332 ND2 ? ? ? 1_555 J NAG .   C1  ? ? A ASN 332 A NAG 603  1_555 ? ? ? ? ? ? ? 1.447 ? 
covale9  covale ? ? B  ASN 95  ND2 ? ? ? 1_555 Q NAG .   C1  ? ? B ASN 95  B NAG 596  1_555 ? ? ? ? ? ? ? 1.457 ? 
covale10 covale ? ? B  ASN 205 ND2 ? ? ? 1_555 S NAG .   C1  ? ? B ASN 205 B NAG 598  1_555 ? ? ? ? ? ? ? 1.513 ? 
covale11 covale ? ? B  ASN 241 ND2 ? ? ? 1_555 U NAG .   C1  ? ? B ASN 241 B NAG 600  1_555 ? ? ? ? ? ? ? 1.439 ? 
covale12 covale ? ? B  ASN 332 ND2 ? ? ? 1_555 X NAG .   C1  ? ? B ASN 332 B NAG 603  1_555 ? ? ? ? ? ? ? 1.436 ? 
covale13 covale ? ? C  NAG .   O4  ? ? ? 1_555 D NAG .   C1  ? ? A NAG 596 A NAG 597  1_555 ? ? ? ? ? ? ? 1.396 ? 
covale14 covale ? ? E  NAG .   O4  ? ? ? 1_555 F NAG .   C1  ? ? A NAG 598 A NAG 599  1_555 ? ? ? ? ? ? ? 1.397 ? 
covale15 covale ? ? G  NAG .   O4  ? ? ? 1_555 H NAG .   C1  ? ? A NAG 600 A NAG 601  1_555 ? ? ? ? ? ? ? 1.386 ? 
covale16 covale ? ? H  NAG .   O4  ? ? ? 1_555 I MAN .   C1  ? ? A NAG 601 A MAN 602  1_555 ? ? ? ? ? ? ? 1.403 ? 
covale17 covale ? ? Q  NAG .   O4  ? ? ? 1_555 R NAG .   C1  ? ? B NAG 596 B NAG 597  1_555 ? ? ? ? ? ? ? 1.389 ? 
covale18 covale ? ? S  NAG .   O4  ? ? ? 1_555 T NAG .   C1  ? ? B NAG 598 B NAG 599  1_555 ? ? ? ? ? ? ? 1.398 ? 
covale19 covale ? ? U  NAG .   O4  ? ? ? 1_555 V NAG .   C1  ? ? B NAG 600 B NAG 601  1_555 ? ? ? ? ? ? ? 1.395 ? 
covale20 covale ? ? V  NAG .   O4  ? ? ? 1_555 W MAN .   C1  ? ? B NAG 601 B MAN 602  1_555 ? ? ? ? ? ? ? 1.465 ? 
metalc3  metalc ? ? A  ASP 110 O   ? ? ? 1_555 K CA  .   CA  ? ? A ASP 110 A CA  1001 1_555 ? ? ? ? ? ? ? 2.555 ? 
metalc4  metalc ? ? A  ASP 110 OD1 ? ? ? 1_555 K CA  .   CA  ? ? A ASP 110 A CA  1001 1_555 ? ? ? ? ? ? ? 2.446 ? 
metalc5  metalc ? ? A  THR 184 O   ? ? ? 1_555 K CA  .   CA  ? ? A THR 184 A CA  1001 1_555 ? ? ? ? ? ? ? 2.588 ? 
metalc6  metalc ? ? A  THR 184 OG1 ? ? ? 1_555 K CA  .   CA  ? ? A THR 184 A CA  1001 1_555 ? ? ? ? ? ? ? 2.487 ? 
metalc7  metalc ? ? A  PHE 186 O   ? ? ? 1_555 K CA  .   CA  ? ? A PHE 186 A CA  1001 1_555 ? ? ? ? ? ? ? 2.561 ? 
metalc8  metalc ? ? A  ASP 188 OD1 ? ? ? 1_555 K CA  .   CA  ? ? A ASP 188 A CA  1001 1_555 ? ? ? ? ? ? ? 2.348 ? 
metalc9  metalc ? ? A  SER 190 OG  ? ? ? 1_555 K CA  .   CA  ? ? A SER 190 A CA  1001 1_555 ? ? ? ? ? ? ? 2.830 ? 
metalc10 metalc ? ? B  ASP 110 O   ? ? ? 1_555 Y CA  .   CA  ? ? B ASP 110 B CA  1002 1_555 ? ? ? ? ? ? ? 2.576 ? 
metalc11 metalc ? ? B  ASP 110 OD1 ? ? ? 1_555 Y CA  .   CA  ? ? B ASP 110 B CA  1002 1_555 ? ? ? ? ? ? ? 2.313 ? 
metalc12 metalc ? ? B  THR 184 O   ? ? ? 1_555 Y CA  .   CA  ? ? B THR 184 B CA  1002 1_555 ? ? ? ? ? ? ? 2.451 ? 
metalc13 metalc ? ? B  THR 184 OG1 ? ? ? 1_555 Y CA  .   CA  ? ? B THR 184 B CA  1002 1_555 ? ? ? ? ? ? ? 2.516 ? 
metalc14 metalc ? ? B  PHE 186 O   ? ? ? 1_555 Y CA  .   CA  ? ? B PHE 186 B CA  1002 1_555 ? ? ? ? ? ? ? 2.499 ? 
metalc15 metalc ? ? B  ASP 188 OD1 ? ? ? 1_555 Y CA  .   CA  ? ? B ASP 188 B CA  1002 1_555 ? ? ? ? ? ? ? 2.488 ? 
metalc16 metalc ? ? B  SER 190 OG  ? ? ? 1_555 Y CA  .   CA  ? ? B SER 190 B CA  1002 1_555 ? ? ? ? ? ? ? 2.706 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           572 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            572 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    573 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     573 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.20 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 2 ? 
C ? 2 ? 
D ? 2 ? 
E ? 2 ? 
F ? 2 ? 
G ? 2 ? 
H ? 2 ? 
I ? 2 ? 
J ? 2 ? 
K ? 2 ? 
L ? 2 ? 
M ? 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 
A 1 2 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
G 1 2 ? anti-parallel 
H 1 2 ? anti-parallel 
I 1 2 ? anti-parallel 
J 1 2 ? anti-parallel 
K 1 2 ? anti-parallel 
L 1 2 ? anti-parallel 
M 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 
A 1 LEU A 92  ? SER A 97  ? LEU A 92  SER A 97  
A 2 LYS A 403 ? LYS A 405 ? LYS A 403 LYS A 405 
B 1 ILE A 142 ? MET A 143 ? ILE A 142 MET A 143 
B 2 CYS A 157 ? MET A 158 ? CYS A 157 MET A 158 
C 1 ARG A 204 ? ASN A 205 ? ARG A 204 ASN A 205 
C 2 LEU A 212 ? MET A 213 ? LEU A 212 MET A 213 
D 1 THR A 357 ? VAL A 358 ? THR A 357 VAL A 358 
D 2 LEU A 374 ? PRO A 375 ? LEU A 374 PRO A 375 
E 1 LEU A 361 ? ASP A 362 ? LEU A 361 ASP A 362 
E 2 GLN A 366 ? PRO A 367 ? GLN A 366 PRO A 367 
F 1 LYS A 561 ? VAL A 562 ? LYS A 561 VAL A 562 
F 2 VAL A 577 ? ASP A 578 ? VAL A 577 ASP A 578 
G 1 ARG B 41  ? ALA B 42  ? ARG B 41  ALA B 42  
G 2 ILE B 180 ? ASN B 181 ? ILE B 180 ASN B 181 
H 1 LEU B 92  ? SER B 97  ? LEU B 92  SER B 97  
H 2 LYS B 403 ? LYS B 405 ? LYS B 403 LYS B 405 
I 1 ILE B 142 ? MET B 143 ? ILE B 142 MET B 143 
I 2 CYS B 157 ? MET B 158 ? CYS B 157 MET B 158 
J 1 ARG B 204 ? ASN B 205 ? ARG B 204 ASN B 205 
J 2 LEU B 212 ? MET B 213 ? LEU B 212 MET B 213 
K 1 THR B 357 ? SER B 359 ? THR B 357 SER B 359 
K 2 GLU B 373 ? PRO B 375 ? GLU B 373 PRO B 375 
L 1 LEU B 361 ? ASP B 362 ? LEU B 361 ASP B 362 
L 2 GLN B 366 ? PRO B 367 ? GLN B 366 PRO B 367 
M 1 LYS B 561 ? PRO B 563 ? LYS B 561 PRO B 563 
M 2 PHE B 576 ? ASP B 578 ? PHE B 576 ASP B 578 
# 
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 
A 1 2 N ARG A 96  ? N ARG A 96  O SER A 404 ? O SER A 404 
B 1 2 N ILE A 142 ? N ILE A 142 O MET A 158 ? O MET A 158 
C 1 2 N ASN A 205 ? N ASN A 205 O LEU A 212 ? O LEU A 212 
D 1 2 N VAL A 358 ? N VAL A 358 O LEU A 374 ? O LEU A 374 
E 1 2 N ASP A 362 ? N ASP A 362 O GLN A 366 ? O GLN A 366 
F 1 2 N VAL A 562 ? N VAL A 562 O VAL A 577 ? O VAL A 577 
G 1 2 N ARG B 41  ? N ARG B 41  O ASN B 181 ? O ASN B 181 
H 1 2 N ARG B 96  ? N ARG B 96  O SER B 404 ? O SER B 404 
I 1 2 N ILE B 142 ? N ILE B 142 O MET B 158 ? O MET B 158 
J 1 2 N ASN B 205 ? N ASN B 205 O LEU B 212 ? O LEU B 212 
K 1 2 N VAL B 358 ? N VAL B 358 O LEU B 374 ? O LEU B 374 
L 1 2 N ASP B 362 ? N ASP B 362 O GLN B 366 ? O GLN B 366 
M 1 2 N VAL B 562 ? N VAL B 562 O VAL B 577 ? O VAL B 577 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG A 596'  
AC2 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 597'  
AC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG A 598'  
AC4 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 599'  
AC5 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG A 600'  
AC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 601'  
AC7 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE MAN A 602'  
AC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 603'  
AC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B 596'  
BC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 597'  
BC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG B 598'  
BC3 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG B 599'  
BC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE NAG B 600'  
BC5 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG B 601'  
BC6 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE MAN B 602'  
BC7 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG B 603'  
BC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CA A 1001'  
BC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CA B 1002'  
CC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CO3 A 2001' 
CC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CO3 B 2002' 
CC3 Software ? ? ? ? 17 'BINDING SITE FOR RESIDUE HEM A 605'  
CC4 Software ? ? ? ? 21 'BINDING SITE FOR RESIDUE HEM B 605'  
CC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE FMT A 3001' 
CC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE FMT A 3002' 
CC7 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE FMT A 3003' 
CC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE FMT B 3004' 
CC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE FMT B 3005' 
DC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE FMT B 3006' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 5  ASN A  95  ? ASN A 95   . ? 1_555 ? 
2   AC1 5  ARG A  96  ? ARG A 96   . ? 1_555 ? 
3   AC1 5  ARG A  504 ? ARG A 504  . ? 1_555 ? 
4   AC1 5  NAG D  .   ? NAG A 597  . ? 1_555 ? 
5   AC1 5  CO3 L  .   ? CO3 A 2001 . ? 1_555 ? 
6   AC2 2  ARG A  504 ? ARG A 504  . ? 1_555 ? 
7   AC2 2  NAG C  .   ? NAG A 596  . ? 1_555 ? 
8   AC3 7  ASN A  205 ? ASN A 205  . ? 1_555 ? 
9   AC3 7  SER A  208 ? SER A 208  . ? 1_555 ? 
10  AC3 7  LEU A  210 ? LEU A 210  . ? 1_555 ? 
11  AC3 7  VAL A  215 ? VAL A 215  . ? 1_555 ? 
12  AC3 7  GLN A  217 ? GLN A 217  . ? 1_555 ? 
13  AC3 7  NAG F  .   ? NAG A 599  . ? 1_555 ? 
14  AC3 7  HOH EA .   ? HOH A 3023 . ? 1_555 ? 
15  AC4 1  NAG E  .   ? NAG A 598  . ? 1_555 ? 
16  AC5 6  ASN A  241 ? ASN A 241  . ? 1_555 ? 
17  AC5 6  ALA A  244 ? ALA A 244  . ? 1_555 ? 
18  AC5 6  TRP A  384 ? TRP A 384  . ? 1_555 ? 
19  AC5 6  NAG H  .   ? NAG A 601  . ? 1_555 ? 
20  AC5 6  PHE B  70  ? PHE B 70   . ? 1_545 ? 
21  AC5 6  LYS B  485 ? LYS B 485  . ? 1_545 ? 
22  AC6 3  NAG G  .   ? NAG A 600  . ? 1_555 ? 
23  AC6 3  MAN I  .   ? MAN A 602  . ? 1_555 ? 
24  AC6 3  LYS B  485 ? LYS B 485  . ? 1_545 ? 
25  AC7 1  NAG H  .   ? NAG A 601  . ? 1_555 ? 
26  AC8 3  ASN A  332 ? ASN A 332  . ? 1_555 ? 
27  AC8 3  VAL A  335 ? VAL A 335  . ? 1_555 ? 
28  AC8 3  HOH EA .   ? HOH A 3054 . ? 1_555 ? 
29  AC9 5  ASN B  95  ? ASN B 95   . ? 1_555 ? 
30  AC9 5  ARG B  504 ? ARG B 504  . ? 1_555 ? 
31  AC9 5  GLN B  568 ? GLN B 568  . ? 1_555 ? 
32  AC9 5  NAG R  .   ? NAG B 597  . ? 1_555 ? 
33  AC9 5  CO3 Z  .   ? CO3 B 2002 . ? 1_555 ? 
34  BC1 4  ARG B  504 ? ARG B 504  . ? 1_555 ? 
35  BC1 4  HIS B  565 ? HIS B 565  . ? 1_555 ? 
36  BC1 4  GLN B  568 ? GLN B 568  . ? 1_555 ? 
37  BC1 4  NAG Q  .   ? NAG B 596  . ? 1_555 ? 
38  BC2 6  LEU A  206 ? LEU A 206  . ? 1_556 ? 
39  BC2 6  ASN B  205 ? ASN B 205  . ? 1_555 ? 
40  BC2 6  VAL B  215 ? VAL B 215  . ? 1_555 ? 
41  BC2 6  GLN B  217 ? GLN B 217  . ? 1_555 ? 
42  BC2 6  NAG T  .   ? NAG B 599  . ? 1_555 ? 
43  BC2 6  HOH FA .   ? HOH B 3014 . ? 1_555 ? 
44  BC3 1  NAG S  .   ? NAG B 598  . ? 1_555 ? 
45  BC4 7  PHE A  70  ? PHE A 70   . ? 1_655 ? 
46  BC4 7  LYS A  485 ? LYS A 485  . ? 1_655 ? 
47  BC4 7  ASN B  241 ? ASN B 241  . ? 1_555 ? 
48  BC4 7  ALA B  244 ? ALA B 244  . ? 1_555 ? 
49  BC4 7  TRP B  384 ? TRP B 384  . ? 1_555 ? 
50  BC4 7  LYS B  388 ? LYS B 388  . ? 1_555 ? 
51  BC4 7  NAG V  .   ? NAG B 601  . ? 1_555 ? 
52  BC5 2  NAG U  .   ? NAG B 600  . ? 1_555 ? 
53  BC5 2  MAN W  .   ? MAN B 602  . ? 1_555 ? 
54  BC6 2  PRO B  370 ? PRO B 370  . ? 1_555 ? 
55  BC6 2  NAG V  .   ? NAG B 601  . ? 1_555 ? 
56  BC7 2  ASN B  332 ? ASN B 332  . ? 1_555 ? 
57  BC7 2  ASP B  524 ? ASP B 524  . ? 1_555 ? 
58  BC8 5  ASP A  110 ? ASP A 110  . ? 1_555 ? 
59  BC8 5  THR A  184 ? THR A 184  . ? 1_555 ? 
60  BC8 5  PHE A  186 ? PHE A 186  . ? 1_555 ? 
61  BC8 5  ASP A  188 ? ASP A 188  . ? 1_555 ? 
62  BC8 5  SER A  190 ? SER A 190  . ? 1_555 ? 
63  BC9 5  ASP B  110 ? ASP B 110  . ? 1_555 ? 
64  BC9 5  THR B  184 ? THR B 184  . ? 1_555 ? 
65  BC9 5  PHE B  186 ? PHE B 186  . ? 1_555 ? 
66  BC9 5  ASP B  188 ? ASP B 188  . ? 1_555 ? 
67  BC9 5  SER B  190 ? SER B 190  . ? 1_555 ? 
68  CC1 4  ASN A  95  ? ASN A 95   . ? 1_555 ? 
69  CC1 4  ARG A  504 ? ARG A 504  . ? 1_555 ? 
70  CC1 4  ARG A  506 ? ARG A 506  . ? 1_555 ? 
71  CC1 4  NAG C  .   ? NAG A 596  . ? 1_555 ? 
72  CC2 5  ASN B  95  ? ASN B 95   . ? 1_555 ? 
73  CC2 5  ARG B  96  ? ARG B 96   . ? 1_555 ? 
74  CC2 5  ARG B  504 ? ARG B 504  . ? 1_555 ? 
75  CC2 5  ARG B  506 ? ARG B 506  . ? 1_555 ? 
76  CC2 5  NAG Q  .   ? NAG B 596  . ? 1_555 ? 
77  CC3 17 MET A  101 ? MET A 101  . ? 1_555 ? 
78  CC3 17 GLY A  104 ? GLY A 104  . ? 1_555 ? 
79  CC3 17 GLN A  105 ? GLN A 105  . ? 1_555 ? 
80  CC3 17 ASP A  108 ? ASP A 108  . ? 1_555 ? 
81  CC3 17 ASP A  112 ? ASP A 112  . ? 1_555 ? 
82  CC3 17 ALA A  114 ? ALA A 114  . ? 1_555 ? 
83  CC3 17 GLU A  258 ? GLU A 258  . ? 1_555 ? 
84  CC3 17 THR A  344 ? THR A 344  . ? 1_555 ? 
85  CC3 17 PHE A  347 ? PHE A 347  . ? 1_555 ? 
86  CC3 17 ARG A  348 ? ARG A 348  . ? 1_555 ? 
87  CC3 17 GLY A  350 ? GLY A 350  . ? 1_555 ? 
88  CC3 17 HIS A  351 ? HIS A 351  . ? 1_555 ? 
89  CC3 17 VAL A  354 ? VAL A 354  . ? 1_555 ? 
90  CC3 17 PHE A  380 ? PHE A 380  . ? 1_555 ? 
91  CC3 17 ILE A  436 ? ILE A 436  . ? 1_555 ? 
92  CC3 17 ARG A  440 ? ARG A 440  . ? 1_555 ? 
93  CC3 17 FMT P  .   ? FMT A 3003 . ? 1_555 ? 
94  CC4 21 MET B  101 ? MET B 101  . ? 1_555 ? 
95  CC4 21 GLY B  104 ? GLY B 104  . ? 1_555 ? 
96  CC4 21 GLN B  105 ? GLN B 105  . ? 1_555 ? 
97  CC4 21 ASP B  108 ? ASP B 108  . ? 1_555 ? 
98  CC4 21 ASP B  112 ? ASP B 112  . ? 1_555 ? 
99  CC4 21 PHE B  113 ? PHE B 113  . ? 1_555 ? 
100 CC4 21 ALA B  114 ? ALA B 114  . ? 1_555 ? 
101 CC4 21 GLU B  116 ? GLU B 116  . ? 1_555 ? 
102 CC4 21 ARG B  255 ? ARG B 255  . ? 1_555 ? 
103 CC4 21 GLU B  258 ? GLU B 258  . ? 1_555 ? 
104 CC4 21 THR B  344 ? THR B 344  . ? 1_555 ? 
105 CC4 21 PHE B  347 ? PHE B 347  . ? 1_555 ? 
106 CC4 21 ARG B  348 ? ARG B 348  . ? 1_555 ? 
107 CC4 21 HIS B  351 ? HIS B 351  . ? 1_555 ? 
108 CC4 21 VAL B  354 ? VAL B 354  . ? 1_555 ? 
109 CC4 21 PHE B  380 ? PHE B 380  . ? 1_555 ? 
110 CC4 21 LEU B  417 ? LEU B 417  . ? 1_555 ? 
111 CC4 21 GLN B  423 ? GLN B 423  . ? 1_555 ? 
112 CC4 21 ARG B  440 ? ARG B 440  . ? 1_555 ? 
113 CC4 21 FMT DA .   ? FMT B 3006 . ? 1_555 ? 
114 CC4 21 HOH FA .   ? HOH B 3027 . ? 1_555 ? 
115 CC5 3  ARG A  397 ? ARG A 397  . ? 1_555 ? 
116 CC5 3  ILE A  559 ? ILE A 559  . ? 1_555 ? 
117 CC5 3  THR A  560 ? THR A 560  . ? 1_555 ? 
118 CC6 5  TRP A  46  ? TRP A 46   . ? 1_555 ? 
119 CC6 5  LEU A  47  ? LEU A 47   . ? 1_555 ? 
120 CC6 5  ASN A  341 ? ASN A 341  . ? 1_555 ? 
121 CC6 5  VAL A  342 ? VAL A 342  . ? 1_555 ? 
122 CC6 5  TRP A  452 ? TRP A 452  . ? 1_555 ? 
123 CC7 3  HIS A  109 ? HIS A 109  . ? 1_555 ? 
124 CC7 3  ARG A  255 ? ARG A 255  . ? 1_555 ? 
125 CC7 3  HEM M  .   ? HEM A 605  . ? 1_555 ? 
126 CC8 3  GLU B  363 ? GLU B 363  . ? 1_555 ? 
127 CC8 3  TYR B  365 ? TYR B 365  . ? 1_555 ? 
128 CC8 3  THR B  560 ? THR B 560  . ? 1_555 ? 
129 CC9 8  ALA B  44  ? ALA B 44   . ? 1_555 ? 
130 CC9 8  ARG B  45  ? ARG B 45   . ? 1_555 ? 
131 CC9 8  TRP B  46  ? TRP B 46   . ? 1_555 ? 
132 CC9 8  LEU B  47  ? LEU B 47   . ? 1_555 ? 
133 CC9 8  SER B  340 ? SER B 340  . ? 1_555 ? 
134 CC9 8  ASN B  341 ? ASN B 341  . ? 1_555 ? 
135 CC9 8  VAL B  342 ? VAL B 342  . ? 1_555 ? 
136 CC9 8  TRP B  452 ? TRP B 452  . ? 1_555 ? 
137 DC1 4  GLN B  105 ? GLN B 105  . ? 1_555 ? 
138 DC1 4  HIS B  109 ? HIS B 109  . ? 1_555 ? 
139 DC1 4  ARG B  255 ? ARG B 255  . ? 1_555 ? 
140 DC1 4  HEM AA .   ? HEM B 605  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2IKC 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2IKC 
_atom_sites.fract_transf_matrix[1][1]   0.016926 
_atom_sites.fract_transf_matrix[1][2]   -0.004406 
_atom_sites.fract_transf_matrix[1][3]   -0.001497 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014235 
_atom_sites.fract_transf_matrix[2][3]   -0.000854 
_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]   0.011924 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . SER A  1 1   ? -12.027 27.698  4.401   1.00 78.23 ? 1    SER A N   1 
ATOM   2     C  CA  . SER A  1 1   ? -10.656 28.084  4.574   1.00 78.46 ? 1    SER A CA  1 
ATOM   3     C  C   . SER A  1 1   ? -9.969  28.258  3.239   1.00 79.15 ? 1    SER A C   1 
ATOM   4     O  O   . SER A  1 1   ? -9.547  27.331  2.553   1.00 78.63 ? 1    SER A O   1 
ATOM   5     C  CB  . SER A  1 1   ? -9.847  27.113  5.414   1.00 78.43 ? 1    SER A CB  1 
ATOM   6     O  OG  . SER A  1 1   ? -9.788  27.545  6.766   1.00 77.89 ? 1    SER A OG  1 
ATOM   7     N  N   . TRP A  1 2   ? -9.866  29.486  2.937   1.00 80.27 ? 2    TRP A N   1 
ATOM   8     C  CA  . TRP A  1 2   ? -9.167  29.928  1.775   1.00 80.85 ? 2    TRP A CA  1 
ATOM   9     C  C   . TRP A  1 2   ? -8.141  30.928  2.378   1.00 81.17 ? 2    TRP A C   1 
ATOM   10    O  O   . TRP A  1 2   ? -8.512  32.063  2.707   1.00 80.09 ? 2    TRP A O   1 
ATOM   11    C  CB  . TRP A  1 2   ? -10.119 30.557  0.745   1.00 82.94 ? 2    TRP A CB  1 
ATOM   12    C  CG  . TRP A  1 2   ? -10.654 29.697  -0.373  1.00 84.86 ? 2    TRP A CG  1 
ATOM   13    C  CD1 . TRP A  1 2   ? -10.283 28.442  -0.783  1.00 85.04 ? 2    TRP A CD1 1 
ATOM   14    C  CD2 . TRP A  1 2   ? -11.690 30.121  -1.280  1.00 85.35 ? 2    TRP A CD2 1 
ATOM   15    N  NE1 . TRP A  1 2   ? -11.016 28.065  -1.888  1.00 85.38 ? 2    TRP A NE1 1 
ATOM   16    C  CE2 . TRP A  1 2   ? -11.885 29.075  -2.213  1.00 85.68 ? 2    TRP A CE2 1 
ATOM   17    C  CE3 . TRP A  1 2   ? -12.467 31.285  -1.396  1.00 85.69 ? 2    TRP A CE3 1 
ATOM   18    C  CZ2 . TRP A  1 2   ? -12.828 29.158  -3.251  1.00 85.62 ? 2    TRP A CZ2 1 
ATOM   19    C  CZ3 . TRP A  1 2   ? -13.405 31.366  -2.430  1.00 85.85 ? 2    TRP A CZ3 1 
ATOM   20    C  CH2 . TRP A  1 2   ? -13.575 30.307  -3.343  1.00 85.81 ? 2    TRP A CH2 1 
ATOM   21    N  N   . GLU A  1 3   ? -6.875  30.492  2.529   1.00 81.40 ? 3    GLU A N   1 
ATOM   22    C  CA  . GLU A  1 3   ? -5.784  31.230  3.152   1.00 81.49 ? 3    GLU A CA  1 
ATOM   23    C  C   . GLU A  1 3   ? -4.399  30.702  2.822   1.00 81.19 ? 3    GLU A C   1 
ATOM   24    O  O   . GLU A  1 3   ? -4.241  29.641  2.236   1.00 81.00 ? 3    GLU A O   1 
ATOM   25    C  CB  . GLU A  1 3   ? -5.862  31.125  4.692   1.00 82.90 ? 3    GLU A CB  1 
ATOM   26    C  CG  . GLU A  1 3   ? -6.228  32.429  5.433   1.00 84.96 ? 3    GLU A CG  1 
ATOM   27    C  CD  . GLU A  1 3   ? -5.117  33.004  6.336   1.00 86.01 ? 3    GLU A CD  1 
ATOM   28    O  OE1 . GLU A  1 3   ? -4.764  32.354  7.335   1.00 86.47 ? 3    GLU A OE1 1 
ATOM   29    O  OE2 . GLU A  1 3   ? -4.617  34.108  6.027   1.00 86.80 ? 3    GLU A OE2 1 
ATOM   30    N  N   . VAL A  1 4   ? -3.387  31.454  3.236   1.00 80.37 ? 4    VAL A N   1 
ATOM   31    C  CA  . VAL A  1 4   ? -1.951  31.227  2.967   1.00 79.76 ? 4    VAL A CA  1 
ATOM   32    C  C   . VAL A  1 4   ? -1.203  30.145  3.756   1.00 79.47 ? 4    VAL A C   1 
ATOM   33    O  O   . VAL A  1 4   ? -1.693  29.632  4.767   1.00 79.86 ? 4    VAL A O   1 
ATOM   34    C  CB  . VAL A  1 4   ? -1.188  32.540  3.231   1.00 79.64 ? 4    VAL A CB  1 
ATOM   35    C  CG1 . VAL A  1 4   ? -0.450  32.977  1.969   1.00 78.81 ? 4    VAL A CG1 1 
ATOM   36    C  CG2 . VAL A  1 4   ? -2.143  33.641  3.700   1.00 78.97 ? 4    VAL A CG2 1 
ATOM   37    N  N   . GLY A  1 5   ? 0.059   29.852  3.316   1.00 78.86 ? 5    GLY A N   1 
ATOM   38    C  CA  . GLY A  1 5   ? 0.885   28.816  4.028   1.00 76.87 ? 5    GLY A CA  1 
ATOM   39    C  C   . GLY A  1 5   ? 2.372   28.664  3.625   1.00 75.00 ? 5    GLY A C   1 
ATOM   40    O  O   . GLY A  1 5   ? 2.802   29.171  2.589   1.00 75.70 ? 5    GLY A O   1 
ATOM   41    N  N   . CYS A  1 6   ? 3.194   27.934  4.470   1.00 72.57 ? 6    CYS A N   1 
ATOM   42    C  CA  . CYS A  1 6   ? 4.618   27.630  4.300   1.00 70.54 ? 6    CYS A CA  1 
ATOM   43    C  C   . CYS A  1 6   ? 4.880   27.081  2.914   1.00 70.73 ? 6    CYS A C   1 
ATOM   44    O  O   . CYS A  1 6   ? 4.445   25.996  2.539   1.00 71.30 ? 6    CYS A O   1 
ATOM   45    C  CB  . CYS A  1 6   ? 5.092   26.611  5.344   1.00 66.62 ? 6    CYS A CB  1 
ATOM   46    S  SG  . CYS A  1 6   ? 4.679   27.046  7.065   1.00 61.30 ? 6    CYS A SG  1 
ATOM   47    N  N   . GLY A  1 7   ? 5.614   27.863  2.170   1.00 70.58 ? 7    GLY A N   1 
ATOM   48    C  CA  . GLY A  1 7   ? 6.020   27.447  0.865   1.00 70.11 ? 7    GLY A CA  1 
ATOM   49    C  C   . GLY A  1 7   ? 7.474   27.016  1.011   1.00 69.33 ? 7    GLY A C   1 
ATOM   50    O  O   . GLY A  1 7   ? 8.394   27.800  0.804   1.00 69.86 ? 7    GLY A O   1 
ATOM   51    N  N   . ALA A  1 8   ? 7.664   25.709  1.358   1.00 68.25 ? 8    ALA A N   1 
ATOM   52    C  CA  . ALA A  1 8   ? 8.976   25.033  1.575   1.00 67.17 ? 8    ALA A CA  1 
ATOM   53    C  C   . ALA A  1 8   ? 9.580   24.382  0.292   1.00 66.50 ? 8    ALA A C   1 
ATOM   54    O  O   . ALA A  1 8   ? 8.971   24.474  -0.764  1.00 65.94 ? 8    ALA A O   1 
ATOM   55    C  CB  . ALA A  1 8   ? 8.837   23.977  2.660   1.00 66.43 ? 8    ALA A CB  1 
ATOM   56    N  N   . PRO A  1 9   ? 10.789  23.708  0.385   1.00 65.66 ? 9    PRO A N   1 
ATOM   57    C  CA  . PRO A  1 9   ? 11.506  23.180  -0.921  1.00 64.50 ? 9    PRO A CA  1 
ATOM   58    C  C   . PRO A  1 9   ? 10.804  22.365  -1.984  1.00 62.95 ? 9    PRO A C   1 
ATOM   59    O  O   . PRO A  1 9   ? 10.802  21.131  -1.871  1.00 63.67 ? 9    PRO A O   1 
ATOM   60    C  CB  . PRO A  1 9   ? 12.707  22.474  -0.389  1.00 64.67 ? 9    PRO A CB  1 
ATOM   61    C  CG  . PRO A  1 9   ? 13.096  23.389  0.717   1.00 64.97 ? 9    PRO A CG  1 
ATOM   62    C  CD  . PRO A  1 9   ? 11.907  24.162  1.233   1.00 65.10 ? 9    PRO A CD  1 
ATOM   63    N  N   . VAL A  1 10  ? 10.221  22.940  -3.026  1.00 59.57 ? 10   VAL A N   1 
ATOM   64    C  CA  . VAL A  1 10  ? 9.556   21.997  -3.930  1.00 55.56 ? 10   VAL A CA  1 
ATOM   65    C  C   . VAL A  1 10  ? 10.023  22.146  -5.363  1.00 54.62 ? 10   VAL A C   1 
ATOM   66    O  O   . VAL A  1 10  ? 10.128  23.285  -5.845  1.00 54.93 ? 10   VAL A O   1 
ATOM   67    C  CB  . VAL A  1 10  ? 8.034   22.181  -3.946  1.00 55.32 ? 10   VAL A CB  1 
ATOM   68    C  CG1 . VAL A  1 10  ? 7.411   21.519  -2.725  1.00 54.65 ? 10   VAL A CG1 1 
ATOM   69    C  CG2 . VAL A  1 10  ? 7.665   23.658  -4.019  1.00 55.20 ? 10   VAL A CG2 1 
ATOM   70    N  N   . PRO A  1 11  ? 10.297  21.037  -6.068  1.00 53.30 ? 11   PRO A N   1 
ATOM   71    C  CA  . PRO A  1 11  ? 10.728  21.224  -7.445  1.00 51.04 ? 11   PRO A CA  1 
ATOM   72    C  C   . PRO A  1 11  ? 9.682   22.051  -8.166  1.00 49.80 ? 11   PRO A C   1 
ATOM   73    O  O   . PRO A  1 11  ? 8.501   21.692  -8.223  1.00 50.46 ? 11   PRO A O   1 
ATOM   74    C  CB  . PRO A  1 11  ? 10.823  19.798  -7.959  1.00 50.88 ? 11   PRO A CB  1 
ATOM   75    C  CG  . PRO A  1 11  ? 11.358  19.094  -6.761  1.00 52.01 ? 11   PRO A CG  1 
ATOM   76    C  CD  . PRO A  1 11  ? 10.337  19.608  -5.725  1.00 52.86 ? 11   PRO A CD  1 
ATOM   77    N  N   . LEU A  1 12  ? 10.130  23.169  -8.711  1.00 48.78 ? 12   LEU A N   1 
ATOM   78    C  CA  . LEU A  1 12  ? 9.252   24.082  -9.410  1.00 48.43 ? 12   LEU A CA  1 
ATOM   79    C  C   . LEU A  1 12  ? 9.351   23.832  -10.906 1.00 47.75 ? 12   LEU A C   1 
ATOM   80    O  O   . LEU A  1 12  ? 10.454  23.653  -11.430 1.00 48.56 ? 12   LEU A O   1 
ATOM   81    C  CB  . LEU A  1 12  ? 9.662   25.514  -9.048  1.00 48.21 ? 12   LEU A CB  1 
ATOM   82    C  CG  . LEU A  1 12  ? 8.667   26.639  -9.333  1.00 48.06 ? 12   LEU A CG  1 
ATOM   83    C  CD1 . LEU A  1 12  ? 7.916   27.027  -8.076  1.00 46.88 ? 12   LEU A CD1 1 
ATOM   84    C  CD2 . LEU A  1 12  ? 9.386   27.832  -9.917  1.00 47.22 ? 12   LEU A CD2 1 
ATOM   85    N  N   . VAL A  1 13  ? 8.200   23.834  -11.622 1.00 45.18 ? 13   VAL A N   1 
ATOM   86    C  CA  . VAL A  1 13  ? 8.183   23.662  -13.073 1.00 43.92 ? 13   VAL A CA  1 
ATOM   87    C  C   . VAL A  1 13  ? 7.112   24.490  -13.745 1.00 43.19 ? 13   VAL A C   1 
ATOM   88    O  O   . VAL A  1 13  ? 6.171   24.977  -13.127 1.00 43.98 ? 13   VAL A O   1 
ATOM   89    C  CB  . VAL A  1 13  ? 7.955   22.216  -13.475 1.00 44.94 ? 13   VAL A CB  1 
ATOM   90    C  CG1 . VAL A  1 13  ? 9.264   21.462  -13.509 1.00 45.39 ? 13   VAL A CG1 1 
ATOM   91    C  CG2 . VAL A  1 13  ? 6.962   21.553  -12.527 1.00 45.45 ? 13   VAL A CG2 1 
ATOM   92    N  N   . LYS A  1 14  ? 7.266   24.595  -15.037 1.00 42.03 ? 14   LYS A N   1 
ATOM   93    C  CA  . LYS A  1 14  ? 6.388   25.371  -15.866 1.00 39.16 ? 14   LYS A CA  1 
ATOM   94    C  C   . LYS A  1 14  ? 5.455   24.442  -16.608 1.00 36.95 ? 14   LYS A C   1 
ATOM   95    O  O   . LYS A  1 14  ? 5.890   23.521  -17.302 1.00 36.92 ? 14   LYS A O   1 
ATOM   96    C  CB  . LYS A  1 14  ? 7.245   26.197  -16.828 1.00 40.75 ? 14   LYS A CB  1 
ATOM   97    C  CG  . LYS A  1 14  ? 6.542   27.337  -17.534 1.00 44.18 ? 14   LYS A CG  1 
ATOM   98    C  CD  . LYS A  1 14  ? 7.326   28.635  -17.455 1.00 45.82 ? 14   LYS A CD  1 
ATOM   99    C  CE  . LYS A  1 14  ? 7.522   29.086  -16.017 1.00 46.25 ? 14   LYS A CE  1 
ATOM   100   N  NZ  . LYS A  1 14  ? 8.109   30.453  -15.944 1.00 46.55 ? 14   LYS A NZ  1 
ATOM   101   N  N   . CYS A  1 15  ? 4.165   24.704  -16.464 1.00 34.21 ? 15   CYS A N   1 
ATOM   102   C  CA  . CYS A  1 15  ? 3.171   23.896  -17.130 1.00 30.81 ? 15   CYS A CA  1 
ATOM   103   C  C   . CYS A  1 15  ? 3.172   24.176  -18.615 1.00 31.17 ? 15   CYS A C   1 
ATOM   104   O  O   . CYS A  1 15  ? 2.878   25.293  -19.071 1.00 30.51 ? 15   CYS A O   1 
ATOM   105   C  CB  . CYS A  1 15  ? 1.796   24.157  -16.527 1.00 25.51 ? 15   CYS A CB  1 
ATOM   106   S  SG  . CYS A  1 15  ? 1.795   23.750  -14.756 1.00 16.93 ? 15   CYS A SG  1 
ATOM   107   N  N   . ASP A  1 16  ? 3.542   23.142  -19.359 1.00 32.84 ? 16   ASP A N   1 
ATOM   108   C  CA  . ASP A  1 16  ? 3.579   23.218  -20.799 1.00 34.40 ? 16   ASP A CA  1 
ATOM   109   C  C   . ASP A  1 16  ? 2.136   23.622  -21.099 1.00 34.36 ? 16   ASP A C   1 
ATOM   110   O  O   . ASP A  1 16  ? 1.881   24.707  -21.627 1.00 34.28 ? 16   ASP A O   1 
ATOM   111   C  CB  . ASP A  1 16  ? 3.945   21.839  -21.371 1.00 35.17 ? 16   ASP A CB  1 
ATOM   112   C  CG  . ASP A  1 16  ? 4.410   21.908  -22.808 1.00 36.16 ? 16   ASP A CG  1 
ATOM   113   O  OD1 . ASP A  1 16  ? 3.597   22.319  -23.659 1.00 37.63 ? 16   ASP A OD1 1 
ATOM   114   O  OD2 . ASP A  1 16  ? 5.580   21.561  -23.089 1.00 36.85 ? 16   ASP A OD2 1 
ATOM   115   N  N   . GLU A  1 17  ? 1.202   22.758  -20.705 1.00 34.04 ? 17   GLU A N   1 
ATOM   116   C  CA  . GLU A  1 17  ? -0.247  22.991  -20.839 1.00 33.39 ? 17   GLU A CA  1 
ATOM   117   C  C   . GLU A  1 17  ? -0.980  22.346  -22.004 1.00 32.46 ? 17   GLU A C   1 
ATOM   118   O  O   . GLU A  1 17  ? -2.205  22.432  -22.076 1.00 31.09 ? 17   GLU A O   1 
ATOM   119   C  CB  . GLU A  1 17  ? -0.572  24.495  -20.833 1.00 34.50 ? 17   GLU A CB  1 
ATOM   120   C  CG  . GLU A  1 17  ? -2.072  24.817  -20.683 1.00 37.10 ? 17   GLU A CG  1 
ATOM   121   C  CD  . GLU A  1 17  ? -2.570  24.644  -19.258 1.00 37.51 ? 17   GLU A CD  1 
ATOM   122   O  OE1 . GLU A  1 17  ? -3.782  24.831  -19.024 1.00 38.24 ? 17   GLU A OE1 1 
ATOM   123   O  OE2 . GLU A  1 17  ? -1.745  24.330  -18.374 1.00 38.22 ? 17   GLU A OE2 1 
ATOM   124   N  N   . ASN A  1 18  ? -0.258  21.714  -22.918 1.00 31.35 ? 18   ASN A N   1 
ATOM   125   C  CA  . ASN A  1 18  ? -0.920  21.079  -24.042 1.00 30.05 ? 18   ASN A CA  1 
ATOM   126   C  C   . ASN A  1 18  ? -0.217  19.800  -24.413 1.00 27.48 ? 18   ASN A C   1 
ATOM   127   O  O   . ASN A  1 18  ? -0.302  19.320  -25.540 1.00 27.78 ? 18   ASN A O   1 
ATOM   128   C  CB  . ASN A  1 18  ? -0.990  22.023  -25.240 1.00 34.17 ? 18   ASN A CB  1 
ATOM   129   C  CG  . ASN A  1 18  ? -2.071  23.088  -25.079 1.00 37.82 ? 18   ASN A CG  1 
ATOM   130   O  OD1 . ASN A  1 18  ? -1.833  24.149  -24.501 1.00 38.55 ? 18   ASN A OD1 1 
ATOM   131   N  ND2 . ASN A  1 18  ? -3.282  22.788  -25.563 1.00 40.35 ? 18   ASN A ND2 1 
ATOM   132   N  N   . SER A  1 19  ? 0.476   19.263  -23.418 1.00 24.14 ? 19   SER A N   1 
ATOM   133   C  CA  . SER A  1 19  ? 1.214   18.022  -23.530 1.00 20.15 ? 19   SER A CA  1 
ATOM   134   C  C   . SER A  1 19  ? 0.230   16.912  -23.204 1.00 16.61 ? 19   SER A C   1 
ATOM   135   O  O   . SER A  1 19  ? -0.424  16.942  -22.167 1.00 16.19 ? 19   SER A O   1 
ATOM   136   C  CB  . SER A  1 19  ? 2.355   18.014  -22.515 1.00 20.02 ? 19   SER A CB  1 
ATOM   137   O  OG  . SER A  1 19  ? 2.738   16.695  -22.170 1.00 19.64 ? 19   SER A OG  1 
ATOM   138   N  N   . PRO A  1 20  ? 0.096   15.924  -24.090 1.00 13.88 ? 20   PRO A N   1 
ATOM   139   C  CA  . PRO A  1 20  ? -0.846  14.843  -23.792 1.00 13.53 ? 20   PRO A CA  1 
ATOM   140   C  C   . PRO A  1 20  ? -0.287  13.947  -22.685 1.00 11.69 ? 20   PRO A C   1 
ATOM   141   O  O   . PRO A  1 20  ? -0.885  12.920  -22.339 1.00 12.40 ? 20   PRO A O   1 
ATOM   142   C  CB  . PRO A  1 20  ? -0.950  14.088  -25.123 1.00 13.51 ? 20   PRO A CB  1 
ATOM   143   C  CG  . PRO A  1 20  ? -0.464  15.079  -26.154 1.00 14.74 ? 20   PRO A CG  1 
ATOM   144   C  CD  . PRO A  1 20  ? 0.650   15.794  -25.446 1.00 14.09 ? 20   PRO A CD  1 
ATOM   145   N  N   . TYR A  1 21  ? 0.852   14.341  -22.120 1.00 7.53  ? 21   TYR A N   1 
ATOM   146   C  CA  . TYR A  1 21  ? 1.489   13.519  -21.110 1.00 4.22  ? 21   TYR A CA  1 
ATOM   147   C  C   . TYR A  1 21  ? 1.547   14.069  -19.713 1.00 3.14  ? 21   TYR A C   1 
ATOM   148   O  O   . TYR A  1 21  ? 1.772   15.259  -19.518 1.00 2.42  ? 21   TYR A O   1 
ATOM   149   C  CB  . TYR A  1 21  ? 2.887   13.162  -21.596 1.00 3.05  ? 21   TYR A CB  1 
ATOM   150   C  CG  . TYR A  1 21  ? 2.821   12.517  -22.952 1.00 3.31  ? 21   TYR A CG  1 
ATOM   151   C  CD1 . TYR A  1 21  ? 1.751   11.688  -23.273 1.00 5.07  ? 21   TYR A CD1 1 
ATOM   152   C  CD2 . TYR A  1 21  ? 3.800   12.734  -23.916 1.00 2.14  ? 21   TYR A CD2 1 
ATOM   153   C  CE1 . TYR A  1 21  ? 1.645   11.089  -24.510 1.00 6.35  ? 21   TYR A CE1 1 
ATOM   154   C  CE2 . TYR A  1 21  ? 3.708   12.132  -25.174 1.00 4.03  ? 21   TYR A CE2 1 
ATOM   155   C  CZ  . TYR A  1 21  ? 2.620   11.305  -25.461 1.00 5.62  ? 21   TYR A CZ  1 
ATOM   156   O  OH  . TYR A  1 21  ? 2.482   10.663  -26.679 1.00 5.85  ? 21   TYR A OH  1 
ATOM   157   N  N   . ARG A  1 22  ? 1.321   13.184  -18.742 1.00 3.35  ? 22   ARG A N   1 
ATOM   158   C  CA  . ARG A  1 22  ? 1.372   13.548  -17.327 1.00 3.62  ? 22   ARG A CA  1 
ATOM   159   C  C   . ARG A  1 22  ? 2.786   14.030  -17.002 1.00 3.65  ? 22   ARG A C   1 
ATOM   160   O  O   . ARG A  1 22  ? 3.759   13.595  -17.623 1.00 4.22  ? 22   ARG A O   1 
ATOM   161   C  CB  . ARG A  1 22  ? 1.122   12.331  -16.422 1.00 3.14  ? 22   ARG A CB  1 
ATOM   162   C  CG  . ARG A  1 22  ? -0.293  11.812  -16.236 1.00 2.95  ? 22   ARG A CG  1 
ATOM   163   C  CD  . ARG A  1 22  ? -0.226  10.618  -15.260 1.00 2.91  ? 22   ARG A CD  1 
ATOM   164   N  NE  . ARG A  1 22  ? -1.505  9.942   -15.038 1.00 2.47  ? 22   ARG A NE  1 
ATOM   165   C  CZ  . ARG A  1 22  ? -2.454  10.365  -14.206 1.00 2.00  ? 22   ARG A CZ  1 
ATOM   166   N  NH1 . ARG A  1 22  ? -2.281  11.471  -13.496 1.00 2.00  ? 22   ARG A NH1 1 
ATOM   167   N  NH2 . ARG A  1 22  ? -3.582  9.685   -14.093 1.00 2.00  ? 22   ARG A NH2 1 
ATOM   168   N  N   . THR A  1 23  ? 2.939   14.979  -16.055 1.00 3.70  ? 23   THR A N   1 
ATOM   169   C  CA  . THR A  1 23  ? 4.322   15.265  -15.725 1.00 3.75  ? 23   THR A CA  1 
ATOM   170   C  C   . THR A  1 23  ? 4.725   14.212  -14.769 1.00 5.61  ? 23   THR A C   1 
ATOM   171   O  O   . THR A  1 23  ? 3.908   13.673  -14.035 1.00 5.29  ? 23   THR A O   1 
ATOM   172   C  CB  . THR A  1 23  ? 4.606   16.635  -14.997 1.00 5.96  ? 23   THR A CB  1 
ATOM   173   O  OG1 . THR A  1 23  ? 4.017   16.579  -13.691 1.00 6.69  ? 23   THR A OG1 1 
ATOM   174   C  CG2 . THR A  1 23  ? 4.019   17.788  -15.777 1.00 6.68  ? 23   THR A CG2 1 
ATOM   175   N  N   . ILE A  1 24  ? 5.992   13.887  -14.777 1.00 5.34  ? 24   ILE A N   1 
ATOM   176   C  CA  . ILE A  1 24  ? 6.353   13.071  -13.455 1.00 5.19  ? 24   ILE A CA  1 
ATOM   177   C  C   . ILE A  1 24  ? 6.187   13.440  -11.990 1.00 5.83  ? 24   ILE A C   1 
ATOM   178   O  O   . ILE A  1 24  ? 5.974   12.584  -11.128 1.00 6.58  ? 24   ILE A O   1 
ATOM   179   C  CB  . ILE A  1 24  ? 7.826   12.734  -13.795 1.00 5.03  ? 24   ILE A CB  1 
ATOM   180   C  CG1 . ILE A  1 24  ? 7.902   11.291  -14.290 1.00 4.90  ? 24   ILE A CG1 1 
ATOM   181   C  CG2 . ILE A  1 24  ? 8.732   12.943  -12.583 1.00 6.52  ? 24   ILE A CG2 1 
ATOM   182   C  CD1 . ILE A  1 24  ? 9.102   11.009  -15.156 1.00 4.03  ? 24   ILE A CD1 1 
ATOM   183   N  N   . THR A  1 25  ? 6.262   14.740  -11.739 1.00 5.97  ? 25   THR A N   1 
ATOM   184   C  CA  . THR A  1 25  ? 6.133   15.313  -10.409 1.00 6.01  ? 25   THR A CA  1 
ATOM   185   C  C   . THR A  1 25  ? 4.681   15.355  -9.950  1.00 6.15  ? 25   THR A C   1 
ATOM   186   O  O   . THR A  1 25  ? 4.392   15.561  -8.769  1.00 5.33  ? 25   THR A O   1 
ATOM   187   C  CB  . THR A  1 25  ? 6.689   16.749  -10.406 1.00 7.65  ? 25   THR A CB  1 
ATOM   188   O  OG1 . THR A  1 25  ? 7.974   16.764  -9.769  1.00 9.01  ? 25   THR A OG1 1 
ATOM   189   C  CG2 . THR A  1 25  ? 5.726   17.710  -9.704  1.00 8.39  ? 25   THR A CG2 1 
ATOM   190   N  N   . GLY A  1 26  ? 3.766   15.166  -10.890 1.00 6.56  ? 26   GLY A N   1 
ATOM   191   C  CA  . GLY A  1 26  ? 2.361   15.215  -10.543 1.00 6.12  ? 26   GLY A CA  1 
ATOM   192   C  C   . GLY A  1 26  ? 1.845   16.628  -10.733 1.00 5.76  ? 26   GLY A C   1 
ATOM   193   O  O   . GLY A  1 26  ? 0.630   16.846  -10.780 1.00 6.34  ? 26   GLY A O   1 
ATOM   194   N  N   . ASP A  1 27  ? 2.735   17.618  -10.865 1.00 4.10  ? 27   ASP A N   1 
ATOM   195   C  CA  . ASP A  1 27  ? 2.366   18.982  -11.109 1.00 2.80  ? 27   ASP A CA  1 
ATOM   196   C  C   . ASP A  1 27  ? 1.662   19.221  -12.435 1.00 2.93  ? 27   ASP A C   1 
ATOM   197   O  O   . ASP A  1 27  ? 1.828   18.495  -13.425 1.00 3.13  ? 27   ASP A O   1 
ATOM   198   C  CB  . ASP A  1 27  ? 3.621   19.878  -11.192 1.00 2.91  ? 27   ASP A CB  1 
ATOM   199   C  CG  . ASP A  1 27  ? 4.123   20.439  -9.875  1.00 3.07  ? 27   ASP A CG  1 
ATOM   200   O  OD1 . ASP A  1 27  ? 3.271   20.752  -9.015  1.00 3.83  ? 27   ASP A OD1 1 
ATOM   201   O  OD2 . ASP A  1 27  ? 5.349   20.557  -9.710  1.00 3.38  ? 27   ASP A OD2 1 
ATOM   202   N  N   . CYS A  1 28  ? 0.859   20.286  -12.436 1.00 2.77  ? 28   CYS A N   1 
ATOM   203   C  CA  . CYS A  1 28  ? 0.211   20.742  -13.637 1.00 3.14  ? 28   CYS A CA  1 
ATOM   204   C  C   . CYS A  1 28  ? -1.041  19.952  -13.986 1.00 2.91  ? 28   CYS A C   1 
ATOM   205   O  O   . CYS A  1 28  ? -1.700  20.284  -14.970 1.00 3.07  ? 28   CYS A O   1 
ATOM   206   C  CB  . CYS A  1 28  ? 1.207   20.708  -14.794 1.00 5.20  ? 28   CYS A CB  1 
ATOM   207   S  SG  . CYS A  1 28  ? 2.705   21.712  -14.514 1.00 12.38 ? 28   CYS A SG  1 
ATOM   208   N  N   . ASN A  1 29  ? -1.388  18.918  -13.230 1.00 2.97  ? 29   ASN A N   1 
ATOM   209   C  CA  . ASN A  1 29  ? -2.598  18.169  -13.581 1.00 3.87  ? 29   ASN A CA  1 
ATOM   210   C  C   . ASN A  1 29  ? -3.758  19.154  -13.589 1.00 2.91  ? 29   ASN A C   1 
ATOM   211   O  O   . ASN A  1 29  ? -4.495  19.292  -14.574 1.00 2.00  ? 29   ASN A O   1 
ATOM   212   C  CB  . ASN A  1 29  ? -2.868  17.049  -12.564 1.00 3.73  ? 29   ASN A CB  1 
ATOM   213   C  CG  . ASN A  1 29  ? -4.289  16.501  -12.656 1.00 4.13  ? 29   ASN A CG  1 
ATOM   214   O  OD1 . ASN A  1 29  ? -5.268  17.222  -12.414 1.00 4.94  ? 29   ASN A OD1 1 
ATOM   215   N  ND2 . ASN A  1 29  ? -4.410  15.224  -13.004 1.00 2.18  ? 29   ASN A ND2 1 
ATOM   216   N  N   . ASN A  1 30  ? -3.890  19.847  -12.464 1.00 5.26  ? 30   ASN A N   1 
ATOM   217   C  CA  . ASN A  1 30  ? -4.929  20.836  -12.280 1.00 5.43  ? 30   ASN A CA  1 
ATOM   218   C  C   . ASN A  1 30  ? -4.487  22.152  -12.868 1.00 7.11  ? 30   ASN A C   1 
ATOM   219   O  O   . ASN A  1 30  ? -3.426  22.686  -12.518 1.00 6.20  ? 30   ASN A O   1 
ATOM   220   C  CB  . ASN A  1 30  ? -5.222  21.052  -10.809 1.00 4.71  ? 30   ASN A CB  1 
ATOM   221   C  CG  . ASN A  1 30  ? -6.327  22.050  -10.597 1.00 4.16  ? 30   ASN A CG  1 
ATOM   222   O  OD1 . ASN A  1 30  ? -6.414  23.044  -11.316 1.00 2.16  ? 30   ASN A OD1 1 
ATOM   223   N  ND2 . ASN A  1 30  ? -7.182  21.800  -9.604  1.00 4.67  ? 30   ASN A ND2 1 
ATOM   224   N  N   . ARG A  1 31  ? -5.336  22.674  -13.744 1.00 9.58  ? 31   ARG A N   1 
ATOM   225   C  CA  . ARG A  1 31  ? -5.092  23.927  -14.432 1.00 10.92 ? 31   ARG A CA  1 
ATOM   226   C  C   . ARG A  1 31  ? -5.158  25.153  -13.510 1.00 12.11 ? 31   ARG A C   1 
ATOM   227   O  O   . ARG A  1 31  ? -4.169  25.881  -13.361 1.00 11.67 ? 31   ARG A O   1 
ATOM   228   C  CB  . ARG A  1 31  ? -6.086  24.046  -15.592 1.00 13.58 ? 31   ARG A CB  1 
ATOM   229   C  CG  . ARG A  1 31  ? -5.410  23.845  -16.936 1.00 19.21 ? 31   ARG A CG  1 
ATOM   230   C  CD  . ARG A  1 31  ? -6.166  22.970  -17.940 1.00 21.98 ? 31   ARG A CD  1 
ATOM   231   N  NE  . ARG A  1 31  ? -5.324  22.784  -19.129 1.00 27.10 ? 31   ARG A NE  1 
ATOM   232   C  CZ  . ARG A  1 31  ? -5.658  22.095  -20.218 1.00 29.09 ? 31   ARG A CZ  1 
ATOM   233   N  NH1 . ARG A  1 31  ? -6.842  21.502  -20.295 1.00 30.94 ? 31   ARG A NH1 1 
ATOM   234   N  NH2 . ARG A  1 31  ? -4.799  21.996  -21.234 1.00 29.56 ? 31   ARG A NH2 1 
ATOM   235   N  N   . ARG A  1 32  ? -6.305  25.379  -12.877 1.00 11.19 ? 32   ARG A N   1 
ATOM   236   C  CA  . ARG A  1 32  ? -6.428  26.529  -12.001 1.00 10.19 ? 32   ARG A CA  1 
ATOM   237   C  C   . ARG A  1 32  ? -5.447  26.523  -10.803 1.00 8.35  ? 32   ARG A C   1 
ATOM   238   O  O   . ARG A  1 32  ? -4.977  27.601  -10.413 1.00 7.75  ? 32   ARG A O   1 
ATOM   239   C  CB  . ARG A  1 32  ? -7.859  26.652  -11.499 1.00 16.19 ? 32   ARG A CB  1 
ATOM   240   C  CG  . ARG A  1 32  ? -8.572  27.884  -12.061 1.00 24.15 ? 32   ARG A CG  1 
ATOM   241   C  CD  . ARG A  1 32  ? -10.032 27.919  -11.644 1.00 28.89 ? 32   ARG A CD  1 
ATOM   242   N  NE  . ARG A  1 32  ? -10.904 28.391  -12.712 1.00 36.74 ? 32   ARG A NE  1 
ATOM   243   C  CZ  . ARG A  1 32  ? -11.545 29.554  -12.689 1.00 39.30 ? 32   ARG A CZ  1 
ATOM   244   N  NH1 . ARG A  1 32  ? -11.406 30.374  -11.649 1.00 42.26 ? 32   ARG A NH1 1 
ATOM   245   N  NH2 . ARG A  1 32  ? -12.326 29.912  -13.689 1.00 42.71 ? 32   ARG A NH2 1 
ATOM   246   N  N   . SER A  1 33  ? -5.164  25.379  -10.215 1.00 7.35  ? 33   SER A N   1 
ATOM   247   C  CA  . SER A  1 33  ? -4.245  25.192  -9.105  1.00 7.80  ? 33   SER A CA  1 
ATOM   248   C  C   . SER A  1 33  ? -3.291  24.075  -9.591  1.00 8.44  ? 33   SER A C   1 
ATOM   249   O  O   . SER A  1 33  ? -3.684  22.903  -9.654  1.00 8.68  ? 33   SER A O   1 
ATOM   250   C  CB  . SER A  1 33  ? -4.931  24.740  -7.810  1.00 6.92  ? 33   SER A CB  1 
ATOM   251   O  OG  . SER A  1 33  ? -4.064  24.859  -6.689  1.00 6.24  ? 33   SER A OG  1 
ATOM   252   N  N   . PRO A  1 34  ? -2.048  24.428  -9.950  1.00 6.92  ? 34   PRO A N   1 
ATOM   253   C  CA  . PRO A  1 34  ? -1.015  23.440  -10.412 1.00 4.25  ? 34   PRO A CA  1 
ATOM   254   C  C   . PRO A  1 34  ? -0.631  22.318  -9.436  1.00 5.47  ? 34   PRO A C   1 
ATOM   255   O  O   . PRO A  1 34  ? -0.874  21.128  -9.681  1.00 7.28  ? 34   PRO A O   1 
ATOM   256   C  CB  . PRO A  1 34  ? 0.147   24.283  -10.824 1.00 4.61  ? 34   PRO A CB  1 
ATOM   257   C  CG  . PRO A  1 34  ? -0.542  25.446  -11.436 1.00 6.56  ? 34   PRO A CG  1 
ATOM   258   C  CD  . PRO A  1 34  ? -1.929  25.574  -10.863 1.00 5.75  ? 34   PRO A CD  1 
ATOM   259   N  N   . ALA A  1 35  ? -0.025  22.753  -8.319  1.00 4.12  ? 35   ALA A N   1 
ATOM   260   C  CA  . ALA A  1 35  ? 0.458   21.850  -7.270  1.00 2.93  ? 35   ALA A CA  1 
ATOM   261   C  C   . ALA A  1 35  ? -0.497  20.773  -6.855  1.00 2.00  ? 35   ALA A C   1 
ATOM   262   O  O   . ALA A  1 35  ? -0.088  19.662  -6.516  1.00 2.00  ? 35   ALA A O   1 
ATOM   263   C  CB  . ALA A  1 35  ? 0.904   22.668  -6.058  1.00 2.44  ? 35   ALA A CB  1 
ATOM   264   N  N   . LEU A  1 36  ? -1.739  21.085  -6.863  1.00 2.04  ? 36   LEU A N   1 
ATOM   265   C  CA  . LEU A  1 36  ? -2.714  20.146  -6.418  1.00 2.00  ? 36   LEU A CA  1 
ATOM   266   C  C   . LEU A  1 36  ? -2.491  18.720  -6.826  1.00 2.50  ? 36   LEU A C   1 
ATOM   267   O  O   . LEU A  1 36  ? -2.605  18.370  -7.989  1.00 2.00  ? 36   LEU A O   1 
ATOM   268   C  CB  . LEU A  1 36  ? -4.055  20.611  -6.870  1.00 2.00  ? 36   LEU A CB  1 
ATOM   269   C  CG  . LEU A  1 36  ? -5.122  20.439  -5.797  1.00 2.00  ? 36   LEU A CG  1 
ATOM   270   C  CD1 . LEU A  1 36  ? -4.637  21.026  -4.472  1.00 2.23  ? 36   LEU A CD1 1 
ATOM   271   C  CD2 . LEU A  1 36  ? -6.433  21.068  -6.245  1.00 3.51  ? 36   LEU A CD2 1 
ATOM   272   N  N   . GLY A  1 37  ? -2.186  17.917  -5.844  1.00 3.30  ? 37   GLY A N   1 
ATOM   273   C  CA  . GLY A  1 37  ? -1.972  16.522  -6.120  1.00 2.81  ? 37   GLY A CA  1 
ATOM   274   C  C   . GLY A  1 37  ? -0.512  16.210  -6.386  1.00 2.38  ? 37   GLY A C   1 
ATOM   275   O  O   . GLY A  1 37  ? -0.169  15.049  -6.663  1.00 2.37  ? 37   GLY A O   1 
ATOM   276   N  N   . ALA A  1 38  ? 0.354   17.246  -6.306  1.00 2.00  ? 38   ALA A N   1 
ATOM   277   C  CA  . ALA A  1 38  ? 1.780   17.030  -6.500  1.00 2.02  ? 38   ALA A CA  1 
ATOM   278   C  C   . ALA A  1 38  ? 2.435   16.335  -5.326  1.00 2.00  ? 38   ALA A C   1 
ATOM   279   O  O   . ALA A  1 38  ? 1.901   16.314  -4.217  1.00 2.15  ? 38   ALA A O   1 
ATOM   280   C  CB  . ALA A  1 38  ? 2.486   18.352  -6.761  1.00 2.00  ? 38   ALA A CB  1 
ATOM   281   N  N   . ALA A  1 39  ? 3.606   15.773  -5.592  1.00 2.00  ? 39   ALA A N   1 
ATOM   282   C  CA  . ALA A  1 39  ? 4.370   15.086  -4.578  1.00 2.00  ? 39   ALA A CA  1 
ATOM   283   C  C   . ALA A  1 39  ? 5.175   16.094  -3.788  1.00 2.30  ? 39   ALA A C   1 
ATOM   284   O  O   . ALA A  1 39  ? 5.536   17.150  -4.294  1.00 2.82  ? 39   ALA A O   1 
ATOM   285   C  CB  . ALA A  1 39  ? 5.288   14.097  -5.215  1.00 2.00  ? 39   ALA A CB  1 
ATOM   286   N  N   . ASN A  1 40  ? 5.447   15.746  -2.537  1.00 3.33  ? 40   ASN A N   1 
ATOM   287   C  CA  . ASN A  1 40  ? 6.247   16.569  -1.588  1.00 3.11  ? 40   ASN A CA  1 
ATOM   288   C  C   . ASN A  1 40  ? 5.521   17.763  -1.059  1.00 4.16  ? 40   ASN A C   1 
ATOM   289   O  O   . ASN A  1 40  ? 6.098   18.797  -0.734  1.00 4.91  ? 40   ASN A O   1 
ATOM   290   C  CB  . ASN A  1 40  ? 7.557   17.013  -2.262  1.00 3.64  ? 40   ASN A CB  1 
ATOM   291   C  CG  . ASN A  1 40  ? 8.493   15.832  -2.327  1.00 6.41  ? 40   ASN A CG  1 
ATOM   292   O  OD1 . ASN A  1 40  ? 8.983   15.372  -1.294  1.00 7.60  ? 40   ASN A OD1 1 
ATOM   293   N  ND2 . ASN A  1 40  ? 8.751   15.330  -3.533  1.00 7.16  ? 40   ASN A ND2 1 
ATOM   294   N  N   . ARG A  1 41  ? 4.241   17.590  -0.976  1.00 3.79  ? 41   ARG A N   1 
ATOM   295   C  CA  . ARG A  1 41  ? 3.352   18.616  -0.444  1.00 2.90  ? 41   ARG A CA  1 
ATOM   296   C  C   . ARG A  1 41  ? 2.789   17.990  0.780   1.00 5.14  ? 41   ARG A C   1 
ATOM   297   O  O   . ARG A  1 41  ? 2.933   16.776  0.922   1.00 6.31  ? 41   ARG A O   1 
ATOM   298   C  CB  . ARG A  1 41  ? 2.153   18.909  -1.338  1.00 2.43  ? 41   ARG A CB  1 
ATOM   299   C  CG  . ARG A  1 41  ? 2.507   19.501  -2.679  1.00 3.19  ? 41   ARG A CG  1 
ATOM   300   C  CD  . ARG A  1 41  ? 3.635   20.487  -2.557  1.00 2.00  ? 41   ARG A CD  1 
ATOM   301   N  NE  . ARG A  1 41  ? 3.995   20.978  -3.877  1.00 2.00  ? 41   ARG A NE  1 
ATOM   302   C  CZ  . ARG A  1 41  ? 4.028   22.256  -4.229  1.00 2.02  ? 41   ARG A CZ  1 
ATOM   303   N  NH1 . ARG A  1 41  ? 3.715   23.189  -3.328  1.00 2.00  ? 41   ARG A NH1 1 
ATOM   304   N  NH2 . ARG A  1 41  ? 4.355   22.599  -5.463  1.00 3.90  ? 41   ARG A NH2 1 
ATOM   305   N  N   . ALA A  1 42  ? 2.175   18.670  1.644   1.00 2.70  ? 42   ALA A N   1 
ATOM   306   C  CA  . ALA A  1 42  ? 1.835   17.792  2.724   1.00 2.00  ? 42   ALA A CA  1 
ATOM   307   C  C   . ALA A  1 42  ? 0.361   17.564  2.968   1.00 2.00  ? 42   ALA A C   1 
ATOM   308   O  O   . ALA A  1 42  ? -0.378  18.417  3.424   1.00 2.00  ? 42   ALA A O   1 
ATOM   309   C  CB  . ALA A  1 42  ? 2.469   18.307  4.010   1.00 3.46  ? 42   ALA A CB  1 
ATOM   310   N  N   . LEU A  1 43  ? -0.006  16.350  2.623   1.00 2.12  ? 43   LEU A N   1 
ATOM   311   C  CA  . LEU A  1 43  ? -1.279  15.642  2.853   1.00 2.00  ? 43   LEU A CA  1 
ATOM   312   C  C   . LEU A  1 43  ? -2.552  16.394  3.140   1.00 2.50  ? 43   LEU A C   1 
ATOM   313   O  O   . LEU A  1 43  ? -2.739  16.888  4.264   1.00 2.76  ? 43   LEU A O   1 
ATOM   314   C  CB  . LEU A  1 43  ? -1.167  14.799  4.116   1.00 2.00  ? 43   LEU A CB  1 
ATOM   315   C  CG  . LEU A  1 43  ? -0.379  13.497  4.091   1.00 2.00  ? 43   LEU A CG  1 
ATOM   316   C  CD1 . LEU A  1 43  ? 0.048   13.101  5.509   1.00 2.00  ? 43   LEU A CD1 1 
ATOM   317   C  CD2 . LEU A  1 43  ? -1.195  12.393  3.450   1.00 2.00  ? 43   LEU A CD2 1 
ATOM   318   N  N   . ALA A  1 44  ? -3.447  16.509  2.175   1.00 2.02  ? 44   ALA A N   1 
ATOM   319   C  CA  . ALA A  1 44  ? -4.862  16.896  2.654   1.00 2.37  ? 44   ALA A CA  1 
ATOM   320   C  C   . ALA A  1 44  ? -5.412  16.492  4.064   1.00 4.50  ? 44   ALA A C   1 
ATOM   321   O  O   . ALA A  1 44  ? -5.302  15.326  4.457   1.00 5.64  ? 44   ALA A O   1 
ATOM   322   C  CB  . ALA A  1 44  ? -5.911  16.549  1.598   1.00 2.00  ? 44   ALA A CB  1 
ATOM   323   N  N   . ARG A  1 45  ? -6.017  17.438  4.841   1.00 3.32  ? 45   ARG A N   1 
ATOM   324   C  CA  . ARG A  1 45  ? -6.567  17.215  6.176   1.00 2.00  ? 45   ARG A CA  1 
ATOM   325   C  C   . ARG A  1 45  ? -8.108  17.298  6.106   1.00 2.00  ? 45   ARG A C   1 
ATOM   326   O  O   . ARG A  1 45  ? -8.630  18.269  5.563   1.00 3.41  ? 45   ARG A O   1 
ATOM   327   C  CB  . ARG A  1 45  ? -6.072  18.244  7.213   1.00 2.00  ? 45   ARG A CB  1 
ATOM   328   C  CG  . ARG A  1 45  ? -4.680  17.980  7.738   1.00 3.23  ? 45   ARG A CG  1 
ATOM   329   C  CD  . ARG A  1 45  ? -4.633  17.165  9.029   1.00 3.32  ? 45   ARG A CD  1 
ATOM   330   N  NE  . ARG A  1 45  ? -3.247  17.089  9.507   1.00 3.49  ? 45   ARG A NE  1 
ATOM   331   C  CZ  . ARG A  1 45  ? -2.826  16.422  10.571  1.00 2.76  ? 45   ARG A CZ  1 
ATOM   332   N  NH1 . ARG A  1 45  ? -3.690  15.735  11.308  1.00 2.35  ? 45   ARG A NH1 1 
ATOM   333   N  NH2 . ARG A  1 45  ? -1.543  16.453  10.897  1.00 2.19  ? 45   ARG A NH2 1 
ATOM   334   N  N   . TRP A  1 46  ? -8.827  16.300  6.628   1.00 2.49  ? 46   TRP A N   1 
ATOM   335   C  CA  . TRP A  1 46  ? -10.275 16.377  6.561   1.00 3.28  ? 46   TRP A CA  1 
ATOM   336   C  C   . TRP A  1 46  ? -10.859 16.828  7.902   1.00 3.80  ? 46   TRP A C   1 
ATOM   337   O  O   . TRP A  1 46  ? -12.024 17.227  7.979   1.00 5.21  ? 46   TRP A O   1 
ATOM   338   C  CB  . TRP A  1 46  ? -10.871 15.037  6.101   1.00 2.70  ? 46   TRP A CB  1 
ATOM   339   C  CG  . TRP A  1 46  ? -10.529 14.686  4.665   1.00 2.10  ? 46   TRP A CG  1 
ATOM   340   C  CD1 . TRP A  1 46  ? -9.926  15.496  3.744   1.00 2.06  ? 46   TRP A CD1 1 
ATOM   341   C  CD2 . TRP A  1 46  ? -10.746 13.427  4.006   1.00 2.18  ? 46   TRP A CD2 1 
ATOM   342   N  NE1 . TRP A  1 46  ? -9.748  14.820  2.558   1.00 2.02  ? 46   TRP A NE1 1 
ATOM   343   C  CE2 . TRP A  1 46  ? -10.242 13.551  2.692   1.00 2.00  ? 46   TRP A CE2 1 
ATOM   344   C  CE3 . TRP A  1 46  ? -11.312 12.207  4.402   1.00 2.00  ? 46   TRP A CE3 1 
ATOM   345   C  CZ2 . TRP A  1 46  ? -10.285 12.504  1.773   1.00 2.00  ? 46   TRP A CZ2 1 
ATOM   346   C  CZ3 . TRP A  1 46  ? -11.354 11.163  3.483   1.00 2.00  ? 46   TRP A CZ3 1 
ATOM   347   C  CH2 . TRP A  1 46  ? -10.842 11.321  2.185   1.00 2.00  ? 46   TRP A CH2 1 
ATOM   348   N  N   . LEU A  1 47  ? -10.038 16.745  8.949   1.00 2.70  ? 47   LEU A N   1 
ATOM   349   C  CA  . LEU A  1 47  ? -10.444 17.153  10.282  1.00 2.00  ? 47   LEU A CA  1 
ATOM   350   C  C   . LEU A  1 47  ? -9.270  17.866  10.966  1.00 2.81  ? 47   LEU A C   1 
ATOM   351   O  O   . LEU A  1 47  ? -8.130  17.828  10.475  1.00 4.38  ? 47   LEU A O   1 
ATOM   352   C  CB  . LEU A  1 47  ? -10.942 15.957  11.088  1.00 2.00  ? 47   LEU A CB  1 
ATOM   353   C  CG  . LEU A  1 47  ? -12.374 15.524  10.792  1.00 2.00  ? 47   LEU A CG  1 
ATOM   354   C  CD1 . LEU A  1 47  ? -12.811 14.438  11.774  1.00 2.00  ? 47   LEU A CD1 1 
ATOM   355   C  CD2 . LEU A  1 47  ? -13.314 16.726  10.833  1.00 2.00  ? 47   LEU A CD2 1 
ATOM   356   N  N   . PRO A  1 48  ? -9.568  18.532  12.102  1.00 2.00  ? 48   PRO A N   1 
ATOM   357   C  CA  . PRO A  1 48  ? -8.538  19.339  12.859  1.00 2.00  ? 48   PRO A CA  1 
ATOM   358   C  C   . PRO A  1 48  ? -7.374  18.568  13.315  1.00 2.00  ? 48   PRO A C   1 
ATOM   359   O  O   . PRO A  1 48  ? -7.561  17.417  13.694  1.00 2.00  ? 48   PRO A O   1 
ATOM   360   C  CB  . PRO A  1 48  ? -9.293  19.966  13.989  1.00 3.36  ? 48   PRO A CB  1 
ATOM   361   C  CG  . PRO A  1 48  ? -10.559 20.313  13.291  1.00 4.25  ? 48   PRO A CG  1 
ATOM   362   C  CD  . PRO A  1 48  ? -10.740 19.393  12.123  1.00 3.14  ? 48   PRO A CD  1 
ATOM   363   N  N   . ALA A  1 49  ? -6.172  19.071  13.302  1.00 2.08  ? 49   ALA A N   1 
ATOM   364   C  CA  . ALA A  1 49  ? -5.180  18.203  13.895  1.00 2.00  ? 49   ALA A CA  1 
ATOM   365   C  C   . ALA A  1 49  ? -5.415  18.157  15.411  1.00 2.49  ? 49   ALA A C   1 
ATOM   366   O  O   . ALA A  1 49  ? -5.618  19.188  16.050  1.00 2.43  ? 49   ALA A O   1 
ATOM   367   C  CB  . ALA A  1 49  ? -3.772  18.687  13.616  1.00 2.00  ? 49   ALA A CB  1 
ATOM   368   N  N   . GLU A  1 50  ? -5.352  16.949  15.955  1.00 3.40  ? 50   GLU A N   1 
ATOM   369   C  CA  . GLU A  1 50  ? -5.408  16.775  17.381  1.00 3.51  ? 50   GLU A CA  1 
ATOM   370   C  C   . GLU A  1 50  ? -3.987  16.409  17.802  1.00 4.16  ? 50   GLU A C   1 
ATOM   371   O  O   . GLU A  1 50  ? -3.418  15.419  17.346  1.00 4.22  ? 50   GLU A O   1 
ATOM   372   C  CB  . GLU A  1 50  ? -6.529  15.803  17.751  1.00 2.00  ? 50   GLU A CB  1 
ATOM   373   C  CG  . GLU A  1 50  ? -7.895  16.318  17.353  1.00 2.92  ? 50   GLU A CG  1 
ATOM   374   C  CD  . GLU A  1 50  ? -9.061  15.681  18.101  1.00 3.62  ? 50   GLU A CD  1 
ATOM   375   O  OE1 . GLU A  1 50  ? -8.831  14.688  18.819  1.00 2.17  ? 50   GLU A OE1 1 
ATOM   376   O  OE2 . GLU A  1 50  ? -10.184 16.190  17.963  1.00 2.61  ? 50   GLU A OE2 1 
ATOM   377   N  N   . TYR A  1 51  ? -3.456  17.252  18.650  1.00 5.29  ? 51   TYR A N   1 
ATOM   378   C  CA  . TYR A  1 51  ? -2.155  17.044  19.271  1.00 5.38  ? 51   TYR A CA  1 
ATOM   379   C  C   . TYR A  1 51  ? -2.346  17.389  20.739  1.00 5.94  ? 51   TYR A C   1 
ATOM   380   O  O   . TYR A  1 51  ? -3.324  18.038  21.108  1.00 4.14  ? 51   TYR A O   1 
ATOM   381   C  CB  . TYR A  1 51  ? -1.055  17.921  18.695  1.00 5.81  ? 51   TYR A CB  1 
ATOM   382   C  CG  . TYR A  1 51  ? -0.518  17.478  17.353  1.00 6.13  ? 51   TYR A CG  1 
ATOM   383   C  CD1 . TYR A  1 51  ? 0.123   16.258  17.204  1.00 6.83  ? 51   TYR A CD1 1 
ATOM   384   C  CD2 . TYR A  1 51  ? -0.658  18.310  16.238  1.00 6.90  ? 51   TYR A CD2 1 
ATOM   385   C  CE1 . TYR A  1 51  ? 0.623   15.878  15.971  1.00 8.26  ? 51   TYR A CE1 1 
ATOM   386   C  CE2 . TYR A  1 51  ? -0.134  17.943  15.003  1.00 6.20  ? 51   TYR A CE2 1 
ATOM   387   C  CZ  . TYR A  1 51  ? 0.507   16.729  14.876  1.00 6.93  ? 51   TYR A CZ  1 
ATOM   388   O  OH  . TYR A  1 51  ? 1.047   16.370  13.664  1.00 8.77  ? 51   TYR A OH  1 
ATOM   389   N  N   . GLU A  1 52  ? -1.395  16.962  21.564  1.00 8.39  ? 52   GLU A N   1 
ATOM   390   C  CA  . GLU A  1 52  ? -1.441  17.191  23.005  1.00 10.11 ? 52   GLU A CA  1 
ATOM   391   C  C   . GLU A  1 52  ? -1.247  18.658  23.387  1.00 10.30 ? 52   GLU A C   1 
ATOM   392   O  O   . GLU A  1 52  ? -1.859  19.133  24.350  1.00 11.33 ? 52   GLU A O   1 
ATOM   393   C  CB  . GLU A  1 52  ? -0.382  16.339  23.697  1.00 12.34 ? 52   GLU A CB  1 
ATOM   394   C  CG  . GLU A  1 52  ? -0.506  16.289  25.201  1.00 16.35 ? 52   GLU A CG  1 
ATOM   395   C  CD  . GLU A  1 52  ? 0.734   15.717  25.849  1.00 18.30 ? 52   GLU A CD  1 
ATOM   396   O  OE1 . GLU A  1 52  ? 1.705   16.483  26.050  1.00 18.90 ? 52   GLU A OE1 1 
ATOM   397   O  OE2 . GLU A  1 52  ? 0.741   14.500  26.140  1.00 20.18 ? 52   GLU A OE2 1 
ATOM   398   N  N   . ASP A  1 53  ? -0.386  19.364  22.654  1.00 9.17  ? 53   ASP A N   1 
ATOM   399   C  CA  . ASP A  1 53  ? -0.152  20.785  22.912  1.00 8.05  ? 53   ASP A CA  1 
ATOM   400   C  C   . ASP A  1 53  ? -0.804  21.566  21.780  1.00 6.61  ? 53   ASP A C   1 
ATOM   401   O  O   . ASP A  1 53  ? -0.393  22.683  21.447  1.00 5.14  ? 53   ASP A O   1 
ATOM   402   C  CB  . ASP A  1 53  ? 1.350   21.102  22.986  1.00 9.16  ? 53   ASP A CB  1 
ATOM   403   C  CG  . ASP A  1 53  ? 2.021   21.136  21.617  1.00 11.09 ? 53   ASP A CG  1 
ATOM   404   O  OD1 . ASP A  1 53  ? 1.516   20.474  20.689  1.00 12.65 ? 53   ASP A OD1 1 
ATOM   405   O  OD2 . ASP A  1 53  ? 3.036   21.840  21.470  1.00 11.50 ? 53   ASP A OD2 1 
ATOM   406   N  N   . GLY A  1 54  ? -1.831  20.982  21.195  1.00 6.71  ? 54   GLY A N   1 
ATOM   407   C  CA  . GLY A  1 54  ? -2.594  21.606  20.139  1.00 7.60  ? 54   GLY A CA  1 
ATOM   408   C  C   . GLY A  1 54  ? -1.783  21.969  18.906  1.00 7.45  ? 54   GLY A C   1 
ATOM   409   O  O   . GLY A  1 54  ? -2.293  22.641  18.015  1.00 8.92  ? 54   GLY A O   1 
ATOM   410   N  N   . LEU A  1 55  ? -0.533  21.523  18.833  1.00 7.65  ? 55   LEU A N   1 
ATOM   411   C  CA  . LEU A  1 55  ? 0.313   21.853  17.686  1.00 7.00  ? 55   LEU A CA  1 
ATOM   412   C  C   . LEU A  1 55  ? 1.228   20.734  17.193  1.00 6.58  ? 55   LEU A C   1 
ATOM   413   O  O   . LEU A  1 55  ? 1.305   20.502  15.987  1.00 7.48  ? 55   LEU A O   1 
ATOM   414   C  CB  . LEU A  1 55  ? 1.175   23.076  18.037  1.00 5.38  ? 55   LEU A CB  1 
ATOM   415   C  CG  . LEU A  1 55  ? 0.444   24.382  18.291  1.00 3.28  ? 55   LEU A CG  1 
ATOM   416   C  CD1 . LEU A  1 55  ? 1.369   25.407  18.923  1.00 2.00  ? 55   LEU A CD1 1 
ATOM   417   C  CD2 . LEU A  1 55  ? -0.138  24.920  16.997  1.00 3.31  ? 55   LEU A CD2 1 
ATOM   418   N  N   . ALA A  1 56  ? 1.902   20.016  18.095  1.00 5.51  ? 56   ALA A N   1 
ATOM   419   C  CA  . ALA A  1 56  ? 2.818   18.993  17.600  1.00 4.55  ? 56   ALA A CA  1 
ATOM   420   C  C   . ALA A  1 56  ? 3.256   17.850  18.548  1.00 4.97  ? 56   ALA A C   1 
ATOM   421   O  O   . ALA A  1 56  ? 3.806   16.864  18.051  1.00 7.43  ? 56   ALA A O   1 
ATOM   422   C  CB  . ALA A  1 56  ? 4.047   19.681  17.051  1.00 4.62  ? 56   ALA A CB  1 
ATOM   423   N  N   . VAL A  1 57  ? 3.036   17.895  19.859  1.00 5.01  ? 57   VAL A N   1 
ATOM   424   C  CA  . VAL A  1 57  ? 3.474   16.722  20.633  1.00 4.57  ? 57   VAL A CA  1 
ATOM   425   C  C   . VAL A  1 57  ? 2.370   15.667  20.643  1.00 3.04  ? 57   VAL A C   1 
ATOM   426   O  O   . VAL A  1 57  ? 1.242   15.899  21.051  1.00 3.26  ? 57   VAL A O   1 
ATOM   427   C  CB  . VAL A  1 57  ? 3.934   17.052  22.084  1.00 4.57  ? 57   VAL A CB  1 
ATOM   428   C  CG1 . VAL A  1 57  ? 5.077   18.044  22.076  1.00 4.75  ? 57   VAL A CG1 1 
ATOM   429   C  CG2 . VAL A  1 57  ? 2.778   17.598  22.917  1.00 5.87  ? 57   VAL A CG2 1 
ATOM   430   N  N   . PRO A  1 58  ? 2.781   14.456  20.185  1.00 3.57  ? 58   PRO A N   1 
ATOM   431   C  CA  . PRO A  1 58  ? 1.872   13.308  20.138  1.00 3.62  ? 58   PRO A CA  1 
ATOM   432   C  C   . PRO A  1 58  ? 1.069   13.003  21.390  1.00 2.46  ? 58   PRO A C   1 
ATOM   433   O  O   . PRO A  1 58  ? 1.610   13.179  22.479  1.00 4.20  ? 58   PRO A O   1 
ATOM   434   C  CB  . PRO A  1 58  ? 2.761   12.215  19.583  1.00 4.18  ? 58   PRO A CB  1 
ATOM   435   C  CG  . PRO A  1 58  ? 3.572   12.971  18.577  1.00 4.02  ? 58   PRO A CG  1 
ATOM   436   C  CD  . PRO A  1 58  ? 3.665   14.397  19.010  1.00 2.47  ? 58   PRO A CD  1 
ATOM   437   N  N   . PHE A  1 59  ? -0.181  12.554  21.306  1.00 2.08  ? 59   PHE A N   1 
ATOM   438   C  CA  . PHE A  1 59  ? -0.857  12.195  22.546  1.00 3.79  ? 59   PHE A CA  1 
ATOM   439   C  C   . PHE A  1 59  ? -0.225  10.951  23.135  1.00 4.84  ? 59   PHE A C   1 
ATOM   440   O  O   . PHE A  1 59  ? -0.274  9.873   22.547  1.00 6.39  ? 59   PHE A O   1 
ATOM   441   C  CB  . PHE A  1 59  ? -2.349  11.938  22.334  1.00 2.18  ? 59   PHE A CB  1 
ATOM   442   C  CG  . PHE A  1 59  ? -3.202  13.140  22.570  1.00 2.00  ? 59   PHE A CG  1 
ATOM   443   C  CD1 . PHE A  1 59  ? -3.843  13.765  21.519  1.00 2.10  ? 59   PHE A CD1 1 
ATOM   444   C  CD2 . PHE A  1 59  ? -3.342  13.668  23.845  1.00 2.82  ? 59   PHE A CD2 1 
ATOM   445   C  CE1 . PHE A  1 59  ? -4.611  14.900  21.734  1.00 2.02  ? 59   PHE A CE1 1 
ATOM   446   C  CE2 . PHE A  1 59  ? -4.111  14.807  24.066  1.00 2.00  ? 59   PHE A CE2 1 
ATOM   447   C  CZ  . PHE A  1 59  ? -4.743  15.420  23.010  1.00 2.00  ? 59   PHE A CZ  1 
ATOM   448   N  N   . GLY A  1 60  ? 0.377   11.100  24.303  1.00 6.07  ? 60   GLY A N   1 
ATOM   449   C  CA  . GLY A  1 60  ? 0.987   9.955   24.935  1.00 7.23  ? 60   GLY A CA  1 
ATOM   450   C  C   . GLY A  1 60  ? 2.483   10.085  24.981  1.00 8.66  ? 60   GLY A C   1 
ATOM   451   O  O   . GLY A  1 60  ? 3.181   9.087   25.126  1.00 11.83 ? 60   GLY A O   1 
ATOM   452   N  N   . TRP A  1 61  ? 2.977   11.312  24.861  1.00 8.55  ? 61   TRP A N   1 
ATOM   453   C  CA  . TRP A  1 61  ? 4.410   11.533  24.898  1.00 10.45 ? 61   TRP A CA  1 
ATOM   454   C  C   . TRP A  1 61  ? 4.815   12.239  26.166  1.00 11.26 ? 61   TRP A C   1 
ATOM   455   O  O   . TRP A  1 61  ? 5.871   11.990  26.743  1.00 10.92 ? 61   TRP A O   1 
ATOM   456   C  CB  . TRP A  1 61  ? 4.846   12.349  23.687  1.00 10.68 ? 61   TRP A CB  1 
ATOM   457   C  CG  . TRP A  1 61  ? 5.931   13.393  23.908  1.00 10.21 ? 61   TRP A CG  1 
ATOM   458   C  CD1 . TRP A  1 61  ? 5.949   14.424  24.802  1.00 10.84 ? 61   TRP A CD1 1 
ATOM   459   C  CD2 . TRP A  1 61  ? 7.145   13.500  23.150  1.00 9.73  ? 61   TRP A CD2 1 
ATOM   460   N  NE1 . TRP A  1 61  ? 7.090   15.169  24.646  1.00 11.92 ? 61   TRP A NE1 1 
ATOM   461   C  CE2 . TRP A  1 61  ? 7.843   14.627  23.639  1.00 10.14 ? 61   TRP A CE2 1 
ATOM   462   C  CE3 . TRP A  1 61  ? 7.707   12.757  22.105  1.00 8.85  ? 61   TRP A CE3 1 
ATOM   463   C  CZ2 . TRP A  1 61  ? 9.075   15.033  23.119  1.00 10.02 ? 61   TRP A CZ2 1 
ATOM   464   C  CZ3 . TRP A  1 61  ? 8.934   13.160  21.586  1.00 10.35 ? 61   TRP A CZ3 1 
ATOM   465   C  CH2 . TRP A  1 61  ? 9.604   14.291  22.096  1.00 10.58 ? 61   TRP A CH2 1 
ATOM   466   N  N   . THR A  1 62  ? 3.976   13.163  26.592  1.00 13.44 ? 62   THR A N   1 
ATOM   467   C  CA  . THR A  1 62  ? 4.221   13.794  27.847  1.00 16.82 ? 62   THR A CA  1 
ATOM   468   C  C   . THR A  1 62  ? 3.569   12.775  28.802  1.00 18.07 ? 62   THR A C   1 
ATOM   469   O  O   . THR A  1 62  ? 2.369   12.500  28.703  1.00 15.62 ? 62   THR A O   1 
ATOM   470   C  CB  . THR A  1 62  ? 3.666   15.239  27.936  1.00 17.26 ? 62   THR A CB  1 
ATOM   471   O  OG1 . THR A  1 62  ? 4.338   16.048  26.967  1.00 19.06 ? 62   THR A OG1 1 
ATOM   472   C  CG2 . THR A  1 62  ? 3.874   15.826  29.325  1.00 18.31 ? 62   THR A CG2 1 
ATOM   473   N  N   . GLN A  1 63  ? 4.348   12.205  29.734  1.00 21.33 ? 63   GLN A N   1 
ATOM   474   C  CA  . GLN A  1 63  ? 3.938   11.174  30.708  1.00 24.65 ? 63   GLN A CA  1 
ATOM   475   C  C   . GLN A  1 63  ? 2.987   11.631  31.807  1.00 26.23 ? 63   GLN A C   1 
ATOM   476   O  O   . GLN A  1 63  ? 2.982   11.025  32.875  1.00 26.67 ? 63   GLN A O   1 
ATOM   477   C  CB  . GLN A  1 63  ? 5.200   10.596  31.388  1.00 27.90 ? 63   GLN A CB  1 
ATOM   478   C  CG  . GLN A  1 63  ? 6.229   9.988   30.439  1.00 32.62 ? 63   GLN A CG  1 
ATOM   479   C  CD  . GLN A  1 63  ? 5.906   8.556   30.046  1.00 34.49 ? 63   GLN A CD  1 
ATOM   480   O  OE1 . GLN A  1 63  ? 4.871   8.294   29.433  1.00 36.07 ? 63   GLN A OE1 1 
ATOM   481   N  NE2 . GLN A  1 63  ? 6.649   7.497   30.283  1.00 34.82 ? 63   GLN A NE2 1 
ATOM   482   N  N   . ARG A  1 64  ? 2.185   12.666  31.582  1.00 27.48 ? 64   ARG A N   1 
ATOM   483   C  CA  . ARG A  1 64  ? 1.272   13.077  32.663  1.00 28.72 ? 64   ARG A CA  1 
ATOM   484   C  C   . ARG A  1 64  ? 0.032   13.873  32.197  1.00 27.27 ? 64   ARG A C   1 
ATOM   485   O  O   . ARG A  1 64  ? -0.955  13.946  32.938  1.00 25.98 ? 64   ARG A O   1 
ATOM   486   C  CB  . ARG A  1 64  ? 2.029   13.859  33.723  1.00 32.93 ? 64   ARG A CB  1 
ATOM   487   C  CG  . ARG A  1 64  ? 2.890   15.001  33.194  1.00 38.70 ? 64   ARG A CG  1 
ATOM   488   C  CD  . ARG A  1 64  ? 2.080   16.254  32.972  1.00 43.37 ? 64   ARG A CD  1 
ATOM   489   N  NE  . ARG A  1 64  ? 2.886   17.477  32.980  1.00 47.46 ? 64   ARG A NE  1 
ATOM   490   C  CZ  . ARG A  1 64  ? 2.401   18.696  32.754  1.00 48.58 ? 64   ARG A CZ  1 
ATOM   491   N  NH1 . ARG A  1 64  ? 1.102   18.869  32.526  1.00 50.17 ? 64   ARG A NH1 1 
ATOM   492   N  NH2 . ARG A  1 64  ? 3.214   19.746  32.758  1.00 49.20 ? 64   ARG A NH2 1 
ATOM   493   N  N   . LYS A  1 65  ? 0.079   14.472  31.009  1.00 26.30 ? 65   LYS A N   1 
ATOM   494   C  CA  . LYS A  1 65  ? -1.116  15.131  30.454  1.00 24.25 ? 65   LYS A CA  1 
ATOM   495   C  C   . LYS A  1 65  ? -2.016  13.993  29.965  1.00 20.83 ? 65   LYS A C   1 
ATOM   496   O  O   . LYS A  1 65  ? -1.527  12.889  29.724  1.00 21.03 ? 65   LYS A O   1 
ATOM   497   C  CB  . LYS A  1 65  ? -0.761  16.066  29.272  1.00 27.21 ? 65   LYS A CB  1 
ATOM   498   C  CG  . LYS A  1 65  ? 0.184   17.225  29.603  1.00 31.37 ? 65   LYS A CG  1 
ATOM   499   C  CD  . LYS A  1 65  ? 0.456   18.061  28.361  1.00 35.60 ? 65   LYS A CD  1 
ATOM   500   C  CE  . LYS A  1 65  ? 1.358   19.255  28.651  1.00 37.79 ? 65   LYS A CE  1 
ATOM   501   N  NZ  . LYS A  1 65  ? 1.364   20.241  27.530  1.00 39.60 ? 65   LYS A NZ  1 
ATOM   502   N  N   . THR A  1 66  ? -3.311  14.235  29.815  1.00 15.98 ? 66   THR A N   1 
ATOM   503   C  CA  . THR A  1 66  ? -4.195  13.161  29.371  1.00 12.62 ? 66   THR A CA  1 
ATOM   504   C  C   . THR A  1 66  ? -4.842  13.489  28.048  1.00 11.35 ? 66   THR A C   1 
ATOM   505   O  O   . THR A  1 66  ? -4.533  14.499  27.415  1.00 12.00 ? 66   THR A O   1 
ATOM   506   C  CB  . THR A  1 66  ? -5.307  12.893  30.433  1.00 12.63 ? 66   THR A CB  1 
ATOM   507   O  OG1 . THR A  1 66  ? -6.356  13.865  30.280  1.00 11.79 ? 66   THR A OG1 1 
ATOM   508   C  CG2 . THR A  1 66  ? -4.725  12.963  31.836  1.00 11.70 ? 66   THR A CG2 1 
ATOM   509   N  N   . ARG A  1 67  ? -5.764  12.652  27.670  1.00 9.02  ? 67   ARG A N   1 
ATOM   510   C  CA  . ARG A  1 67  ? -6.603  12.867  26.536  1.00 6.88  ? 67   ARG A CA  1 
ATOM   511   C  C   . ARG A  1 67  ? -7.976  12.797  27.148  1.00 6.71  ? 67   ARG A C   1 
ATOM   512   O  O   . ARG A  1 67  ? -8.297  11.778  27.759  1.00 5.59  ? 67   ARG A O   1 
ATOM   513   C  CB  . ARG A  1 67  ? -6.409  11.786  25.456  1.00 6.45  ? 67   ARG A CB  1 
ATOM   514   C  CG  . ARG A  1 67  ? -6.974  12.139  24.103  1.00 5.17  ? 67   ARG A CG  1 
ATOM   515   C  CD  . ARG A  1 67  ? -6.846  10.943  23.163  1.00 5.27  ? 67   ARG A CD  1 
ATOM   516   N  NE  . ARG A  1 67  ? -7.431  11.172  21.848  1.00 4.49  ? 67   ARG A NE  1 
ATOM   517   C  CZ  . ARG A  1 67  ? -6.723  11.308  20.729  1.00 3.93  ? 67   ARG A CZ  1 
ATOM   518   N  NH1 . ARG A  1 67  ? -5.397  11.236  20.756  1.00 2.00  ? 67   ARG A NH1 1 
ATOM   519   N  NH2 . ARG A  1 67  ? -7.347  11.512  19.576  1.00 4.46  ? 67   ARG A NH2 1 
ATOM   520   N  N   . ASN A  1 68  ? -8.798  13.800  27.019  1.00 5.74  ? 68   ASN A N   1 
ATOM   521   C  CA  . ASN A  1 68  ? -10.146 13.675  27.568  1.00 5.23  ? 68   ASN A CA  1 
ATOM   522   C  C   . ASN A  1 68  ? -10.247 13.164  29.013  1.00 4.73  ? 68   ASN A C   1 
ATOM   523   O  O   . ASN A  1 68  ? -11.266 12.614  29.435  1.00 3.85  ? 68   ASN A O   1 
ATOM   524   C  CB  . ASN A  1 68  ? -10.951 12.738  26.646  1.00 5.41  ? 68   ASN A CB  1 
ATOM   525   C  CG  . ASN A  1 68  ? -11.035 13.287  25.248  1.00 6.19  ? 68   ASN A CG  1 
ATOM   526   O  OD1 . ASN A  1 68  ? -11.426 14.440  25.049  1.00 5.77  ? 68   ASN A OD1 1 
ATOM   527   N  ND2 . ASN A  1 68  ? -10.666 12.471  24.265  1.00 7.00  ? 68   ASN A ND2 1 
ATOM   528   N  N   . GLY A  1 69  ? -9.180  13.358  29.769  1.00 4.49  ? 69   GLY A N   1 
ATOM   529   C  CA  . GLY A  1 69  ? -9.173  13.001  31.164  1.00 6.58  ? 69   GLY A CA  1 
ATOM   530   C  C   . GLY A  1 69  ? -8.632  11.616  31.442  1.00 8.07  ? 69   GLY A C   1 
ATOM   531   O  O   . GLY A  1 69  ? -8.718  11.126  32.573  1.00 8.15  ? 69   GLY A O   1 
ATOM   532   N  N   . PHE A  1 70  ? -8.067  10.978  30.424  1.00 8.73  ? 70   PHE A N   1 
ATOM   533   C  CA  . PHE A  1 70  ? -7.536  9.639   30.607  1.00 8.85  ? 70   PHE A CA  1 
ATOM   534   C  C   . PHE A  1 70  ? -6.168  9.437   29.988  1.00 9.00  ? 70   PHE A C   1 
ATOM   535   O  O   . PHE A  1 70  ? -5.839  10.032  28.966  1.00 9.14  ? 70   PHE A O   1 
ATOM   536   C  CB  . PHE A  1 70  ? -8.517  8.609   30.045  1.00 9.82  ? 70   PHE A CB  1 
ATOM   537   C  CG  . PHE A  1 70  ? -9.826  8.555   30.784  1.00 11.16 ? 70   PHE A CG  1 
ATOM   538   C  CD1 . PHE A  1 70  ? -11.032 8.693   30.097  1.00 11.84 ? 70   PHE A CD1 1 
ATOM   539   C  CD2 . PHE A  1 70  ? -9.854  8.369   32.167  1.00 11.56 ? 70   PHE A CD2 1 
ATOM   540   C  CE1 . PHE A  1 70  ? -12.250 8.650   30.770  1.00 12.46 ? 70   PHE A CE1 1 
ATOM   541   C  CE2 . PHE A  1 70  ? -11.059 8.323   32.855  1.00 12.59 ? 70   PHE A CE2 1 
ATOM   542   C  CZ  . PHE A  1 70  ? -12.266 8.464   32.153  1.00 14.35 ? 70   PHE A CZ  1 
ATOM   543   N  N   . ARG A  1 71  ? -5.379  8.589   30.637  1.00 9.24  ? 71   ARG A N   1 
ATOM   544   C  CA  . ARG A  1 71  ? -4.033  8.201   30.173  1.00 9.41  ? 71   ARG A CA  1 
ATOM   545   C  C   . ARG A  1 71  ? -4.120  7.389   28.879  1.00 7.09  ? 71   ARG A C   1 
ATOM   546   O  O   . ARG A  1 71  ? -4.960  6.498   28.774  1.00 6.87  ? 71   ARG A O   1 
ATOM   547   C  CB  . ARG A  1 71  ? -3.359  7.327   31.248  1.00 14.60 ? 71   ARG A CB  1 
ATOM   548   C  CG  . ARG A  1 71  ? -2.043  7.860   31.763  1.00 22.08 ? 71   ARG A CG  1 
ATOM   549   C  CD  . ARG A  1 71  ? -2.102  8.103   33.251  1.00 26.54 ? 71   ARG A CD  1 
ATOM   550   N  NE  . ARG A  1 71  ? -1.466  9.371   33.590  1.00 31.37 ? 71   ARG A NE  1 
ATOM   551   C  CZ  . ARG A  1 71  ? -0.157  9.551   33.723  1.00 33.03 ? 71   ARG A CZ  1 
ATOM   552   N  NH1 . ARG A  1 71  ? 0.682   8.536   33.550  1.00 35.49 ? 71   ARG A NH1 1 
ATOM   553   N  NH2 . ARG A  1 71  ? 0.311   10.751  34.033  1.00 34.47 ? 71   ARG A NH2 1 
ATOM   554   N  N   . VAL A  1 72  ? -3.271  7.667   27.861  1.00 4.12  ? 72   VAL A N   1 
ATOM   555   C  CA  . VAL A  1 72  ? -3.344  6.894   26.580  1.00 3.95  ? 72   VAL A CA  1 
ATOM   556   C  C   . VAL A  1 72  ? -2.477  5.630   26.672  1.00 3.18  ? 72   VAL A C   1 
ATOM   557   O  O   . VAL A  1 72  ? -1.338  5.661   27.145  1.00 2.00  ? 72   VAL A O   1 
ATOM   558   C  CB  . VAL A  1 72  ? -2.928  7.708   25.365  1.00 2.00  ? 72   VAL A CB  1 
ATOM   559   C  CG1 . VAL A  1 72  ? -3.145  9.200   25.617  1.00 2.00  ? 72   VAL A CG1 1 
ATOM   560   C  CG2 . VAL A  1 72  ? -1.475  7.442   24.996  1.00 3.52  ? 72   VAL A CG2 1 
ATOM   561   N  N   . PRO A  1 73  ? -3.030  4.521   26.203  1.00 2.00  ? 73   PRO A N   1 
ATOM   562   C  CA  . PRO A  1 73  ? -2.346  3.192   26.307  1.00 2.00  ? 73   PRO A CA  1 
ATOM   563   C  C   . PRO A  1 73  ? -1.007  3.073   25.648  1.00 2.53  ? 73   PRO A C   1 
ATOM   564   O  O   . PRO A  1 73  ? -0.808  3.627   24.567  1.00 2.00  ? 73   PRO A O   1 
ATOM   565   C  CB  . PRO A  1 73  ? -3.369  2.224   25.758  1.00 2.98  ? 73   PRO A CB  1 
ATOM   566   C  CG  . PRO A  1 73  ? -4.612  2.793   26.333  1.00 2.97  ? 73   PRO A CG  1 
ATOM   567   C  CD  . PRO A  1 73  ? -4.404  4.244   26.607  1.00 2.41  ? 73   PRO A CD  1 
ATOM   568   N  N   . LEU A  1 74  ? -0.069  2.385   26.244  1.00 4.87  ? 74   LEU A N   1 
ATOM   569   C  CA  . LEU A  1 74  ? 1.167   2.276   25.519  1.00 3.64  ? 74   LEU A CA  1 
ATOM   570   C  C   . LEU A  1 74  ? 0.930   1.665   24.129  1.00 2.41  ? 74   LEU A C   1 
ATOM   571   O  O   . LEU A  1 74  ? 0.114   0.756   23.978  1.00 2.00  ? 74   LEU A O   1 
ATOM   572   C  CB  . LEU A  1 74  ? 2.184   1.448   26.274  1.00 3.92  ? 74   LEU A CB  1 
ATOM   573   C  CG  . LEU A  1 74  ? 2.560   1.984   27.634  1.00 3.95  ? 74   LEU A CG  1 
ATOM   574   C  CD1 . LEU A  1 74  ? 3.640   1.125   28.285  1.00 4.67  ? 74   LEU A CD1 1 
ATOM   575   C  CD2 . LEU A  1 74  ? 3.030   3.424   27.539  1.00 4.39  ? 74   LEU A CD2 1 
ATOM   576   N  N   . ALA A  1 75  ? 1.645   2.171   23.134  1.00 2.19  ? 75   ALA A N   1 
ATOM   577   C  CA  . ALA A  1 75  ? 1.481   1.657   21.786  1.00 2.56  ? 75   ALA A CA  1 
ATOM   578   C  C   . ALA A  1 75  ? 1.510   0.131   21.815  1.00 2.00  ? 75   ALA A C   1 
ATOM   579   O  O   . ALA A  1 75  ? 0.535   -0.516  21.411  1.00 2.00  ? 75   ALA A O   1 
ATOM   580   C  CB  . ALA A  1 75  ? 2.575   2.206   20.878  1.00 2.00  ? 75   ALA A CB  1 
ATOM   581   N  N   . ARG A  1 76  ? 2.617   -0.430  22.302  1.00 2.02  ? 76   ARG A N   1 
ATOM   582   C  CA  . ARG A  1 76  ? 2.812   -1.882  22.388  1.00 3.45  ? 76   ARG A CA  1 
ATOM   583   C  C   . ARG A  1 76  ? 1.782   -2.646  23.227  1.00 4.52  ? 76   ARG A C   1 
ATOM   584   O  O   . ARG A  1 76  ? 1.381   -3.754  22.872  1.00 4.18  ? 76   ARG A O   1 
ATOM   585   C  CB  . ARG A  1 76  ? 4.214   -2.183  22.899  1.00 2.08  ? 76   ARG A CB  1 
ATOM   586   C  CG  . ARG A  1 76  ? 4.444   -3.643  23.306  1.00 2.00  ? 76   ARG A CG  1 
ATOM   587   C  CD  . ARG A  1 76  ? 4.623   -4.561  22.090  1.00 5.01  ? 76   ARG A CD  1 
ATOM   588   N  NE  . ARG A  1 76  ? 5.307   -5.816  22.435  1.00 5.14  ? 76   ARG A NE  1 
ATOM   589   C  CZ  . ARG A  1 76  ? 5.613   -6.783  21.568  1.00 3.88  ? 76   ARG A CZ  1 
ATOM   590   N  NH1 . ARG A  1 76  ? 5.304   -6.671  20.282  1.00 2.07  ? 76   ARG A NH1 1 
ATOM   591   N  NH2 . ARG A  1 76  ? 6.239   -7.868  21.990  1.00 4.48  ? 76   ARG A NH2 1 
ATOM   592   N  N   . GLU A  1 77  ? 1.356   -2.075  24.342  1.00 3.89  ? 77   GLU A N   1 
ATOM   593   C  CA  . GLU A  1 77  ? 0.402   -2.771  25.180  1.00 4.30  ? 77   GLU A CA  1 
ATOM   594   C  C   . GLU A  1 77  ? -0.867  -3.182  24.418  1.00 3.92  ? 77   GLU A C   1 
ATOM   595   O  O   . GLU A  1 77  ? -1.390  -4.271  24.658  1.00 2.00  ? 77   GLU A O   1 
ATOM   596   C  CB  . GLU A  1 77  ? 0.077   -1.905  26.400  1.00 9.19  ? 77   GLU A CB  1 
ATOM   597   C  CG  . GLU A  1 77  ? -0.954  -2.492  27.353  1.00 16.66 ? 77   GLU A CG  1 
ATOM   598   C  CD  . GLU A  1 77  ? -0.982  -1.767  28.702  1.00 21.05 ? 77   GLU A CD  1 
ATOM   599   O  OE1 . GLU A  1 77  ? -0.732  -0.541  28.737  1.00 24.10 ? 77   GLU A OE1 1 
ATOM   600   O  OE2 . GLU A  1 77  ? -1.268  -2.423  29.725  1.00 22.24 ? 77   GLU A OE2 1 
ATOM   601   N  N   . VAL A  1 78  ? -1.349  -2.330  23.518  1.00 3.24  ? 78   VAL A N   1 
ATOM   602   C  CA  . VAL A  1 78  ? -2.559  -2.640  22.748  1.00 2.86  ? 78   VAL A CA  1 
ATOM   603   C  C   . VAL A  1 78  ? -2.314  -3.873  21.891  1.00 4.13  ? 78   VAL A C   1 
ATOM   604   O  O   . VAL A  1 78  ? -3.149  -4.778  21.795  1.00 4.63  ? 78   VAL A O   1 
ATOM   605   C  CB  . VAL A  1 78  ? -2.953  -1.451  21.837  1.00 2.00  ? 78   VAL A CB  1 
ATOM   606   C  CG1 . VAL A  1 78  ? -4.019  -1.868  20.830  1.00 2.00  ? 78   VAL A CG1 1 
ATOM   607   C  CG2 . VAL A  1 78  ? -3.463  -0.281  22.662  1.00 2.00  ? 78   VAL A CG2 1 
ATOM   608   N  N   . SER A  1 79  ? -1.141  -3.888  21.279  1.00 2.82  ? 79   SER A N   1 
ATOM   609   C  CA  . SER A  1 79  ? -0.711  -4.971  20.423  1.00 3.06  ? 79   SER A CA  1 
ATOM   610   C  C   . SER A  1 79  ? -0.738  -6.314  21.188  1.00 5.57  ? 79   SER A C   1 
ATOM   611   O  O   . SER A  1 79  ? -1.275  -7.306  20.683  1.00 6.23  ? 79   SER A O   1 
ATOM   612   C  CB  . SER A  1 79  ? 0.701   -4.707  19.907  1.00 2.00  ? 79   SER A CB  1 
ATOM   613   O  OG  . SER A  1 79  ? 0.875   -5.240  18.601  1.00 2.00  ? 79   SER A OG  1 
ATOM   614   N  N   . ASN A  1 80  ? -0.190  -6.358  22.403  1.00 2.63  ? 80   ASN A N   1 
ATOM   615   C  CA  . ASN A  1 80  ? -0.179  -7.615  23.148  1.00 2.00  ? 80   ASN A CA  1 
ATOM   616   C  C   . ASN A  1 80  ? -1.573  -8.054  23.538  1.00 3.13  ? 80   ASN A C   1 
ATOM   617   O  O   . ASN A  1 80  ? -1.964  -9.202  23.329  1.00 3.29  ? 80   ASN A O   1 
ATOM   618   C  CB  . ASN A  1 80  ? 0.642   -7.507  24.433  1.00 2.06  ? 80   ASN A CB  1 
ATOM   619   C  CG  . ASN A  1 80  ? 2.047   -7.029  24.190  1.00 2.51  ? 80   ASN A CG  1 
ATOM   620   O  OD1 . ASN A  1 80  ? 2.561   -7.110  23.078  1.00 2.95  ? 80   ASN A OD1 1 
ATOM   621   N  ND2 . ASN A  1 80  ? 2.691   -6.536  25.242  1.00 3.09  ? 80   ASN A ND2 1 
ATOM   622   N  N   . LYS A  1 81  ? -2.320  -7.130  24.121  1.00 2.95  ? 81   LYS A N   1 
ATOM   623   C  CA  . LYS A  1 81  ? -3.659  -7.438  24.576  1.00 2.98  ? 81   LYS A CA  1 
ATOM   624   C  C   . LYS A  1 81  ? -4.658  -7.748  23.481  1.00 3.56  ? 81   LYS A C   1 
ATOM   625   O  O   . LYS A  1 81  ? -5.471  -8.660  23.614  1.00 5.58  ? 81   LYS A O   1 
ATOM   626   C  CB  . LYS A  1 81  ? -4.209  -6.290  25.424  1.00 3.35  ? 81   LYS A CB  1 
ATOM   627   C  CG  . LYS A  1 81  ? -4.110  -6.526  26.920  1.00 5.07  ? 81   LYS A CG  1 
ATOM   628   C  CD  . LYS A  1 81  ? -2.672  -6.439  27.392  1.00 8.57  ? 81   LYS A CD  1 
ATOM   629   C  CE  . LYS A  1 81  ? -2.594  -6.396  28.918  1.00 13.40 ? 81   LYS A CE  1 
ATOM   630   N  NZ  . LYS A  1 81  ? -2.999  -5.064  29.446  1.00 14.69 ? 81   LYS A NZ  1 
ATOM   631   N  N   . ILE A  1 82  ? -4.584  -6.986  22.361  1.00 3.04  ? 82   ILE A N   1 
ATOM   632   C  CA  . ILE A  1 82  ? -5.632  -7.148  21.328  1.00 2.24  ? 82   ILE A CA  1 
ATOM   633   C  C   . ILE A  1 82  ? -5.224  -7.691  19.960  1.00 2.00  ? 82   ILE A C   1 
ATOM   634   O  O   . ILE A  1 82  ? -5.752  -8.718  19.526  1.00 2.00  ? 82   ILE A O   1 
ATOM   635   C  CB  . ILE A  1 82  ? -6.297  -5.809  21.075  1.00 2.00  ? 82   ILE A CB  1 
ATOM   636   C  CG1 . ILE A  1 82  ? -6.777  -5.214  22.401  1.00 2.00  ? 82   ILE A CG1 1 
ATOM   637   C  CG2 . ILE A  1 82  ? -7.466  -5.960  20.122  1.00 2.00  ? 82   ILE A CG2 1 
ATOM   638   C  CD1 . ILE A  1 82  ? -6.475  -3.743  22.559  1.00 2.06  ? 82   ILE A CD1 1 
ATOM   639   N  N   . VAL A  1 83  ? -4.302  -7.004  19.313  1.00 2.44  ? 83   VAL A N   1 
ATOM   640   C  CA  . VAL A  1 83  ? -3.919  -7.286  17.916  1.00 2.26  ? 83   VAL A CA  1 
ATOM   641   C  C   . VAL A  1 83  ? -3.351  -8.660  17.543  1.00 3.71  ? 83   VAL A C   1 
ATOM   642   O  O   . VAL A  1 83  ? -3.517  -9.115  16.410  1.00 2.35  ? 83   VAL A O   1 
ATOM   643   C  CB  . VAL A  1 83  ? -2.942  -6.210  17.415  1.00 2.00  ? 83   VAL A CB  1 
ATOM   644   C  CG1 . VAL A  1 83  ? -2.465  -6.519  16.009  1.00 2.61  ? 83   VAL A CG1 1 
ATOM   645   C  CG2 . VAL A  1 83  ? -3.583  -4.837  17.475  1.00 2.00  ? 83   VAL A CG2 1 
ATOM   646   N  N   . GLY A  1 84  ? -2.707  -9.355  18.481  1.00 3.45  ? 84   GLY A N   1 
ATOM   647   C  CA  . GLY A  1 84  ? -2.035  -10.612 18.179  1.00 3.40  ? 84   GLY A CA  1 
ATOM   648   C  C   . GLY A  1 84  ? -2.781  -11.914 18.497  1.00 2.00  ? 84   GLY A C   1 
ATOM   649   O  O   . GLY A  1 84  ? -3.800  -11.944 19.185  1.00 2.00  ? 84   GLY A O   1 
ATOM   650   N  N   . TYR A  1 85  ? -2.206  -12.999 17.983  1.00 2.00  ? 85   TYR A N   1 
ATOM   651   C  CA  . TYR A  1 85  ? -2.726  -14.344 18.166  1.00 2.00  ? 85   TYR A CA  1 
ATOM   652   C  C   . TYR A  1 85  ? -1.593  -15.372 17.963  1.00 3.39  ? 85   TYR A C   1 
ATOM   653   O  O   . TYR A  1 85  ? -0.541  -15.009 17.442  1.00 4.05  ? 85   TYR A O   1 
ATOM   654   C  CB  . TYR A  1 85  ? -3.844  -14.640 17.162  1.00 2.00  ? 85   TYR A CB  1 
ATOM   655   C  CG  . TYR A  1 85  ? -3.460  -14.557 15.708  1.00 2.12  ? 85   TYR A CG  1 
ATOM   656   C  CD1 . TYR A  1 85  ? -3.237  -15.728 14.983  1.00 2.52  ? 85   TYR A CD1 1 
ATOM   657   C  CD2 . TYR A  1 85  ? -3.320  -13.339 15.035  1.00 2.69  ? 85   TYR A CD2 1 
ATOM   658   C  CE1 . TYR A  1 85  ? -2.895  -15.687 13.613  1.00 3.09  ? 85   TYR A CE1 1 
ATOM   659   C  CE2 . TYR A  1 85  ? -3.006  -13.287 13.667  1.00 2.90  ? 85   TYR A CE2 1 
ATOM   660   C  CZ  . TYR A  1 85  ? -2.802  -14.463 12.962  1.00 2.08  ? 85   TYR A CZ  1 
ATOM   661   O  OH  . TYR A  1 85  ? -2.524  -14.411 11.607  1.00 2.00  ? 85   TYR A OH  1 
ATOM   662   N  N   . LEU A  1 86  ? -1.771  -16.659 18.394  1.00 4.74  ? 86   LEU A N   1 
ATOM   663   C  CA  . LEU A  1 86  ? -0.701  -17.694 18.331  1.00 3.35  ? 86   LEU A CA  1 
ATOM   664   C  C   . LEU A  1 86  ? -1.012  -18.880 17.462  1.00 2.03  ? 86   LEU A C   1 
ATOM   665   O  O   . LEU A  1 86  ? -0.117  -19.679 17.168  1.00 2.00  ? 86   LEU A O   1 
ATOM   666   C  CB  . LEU A  1 86  ? -0.472  -18.430 19.650  1.00 3.41  ? 86   LEU A CB  1 
ATOM   667   C  CG  . LEU A  1 86  ? -0.086  -17.684 20.899  1.00 3.65  ? 86   LEU A CG  1 
ATOM   668   C  CD1 . LEU A  1 86  ? -0.244  -18.590 22.107  1.00 2.74  ? 86   LEU A CD1 1 
ATOM   669   C  CD2 . LEU A  1 86  ? 1.343   -17.147 20.806  1.00 4.27  ? 86   LEU A CD2 1 
ATOM   670   N  N   . ASP A  1 87  ? -2.241  -19.036 17.063  1.00 2.00  ? 87   ASP A N   1 
ATOM   671   C  CA  . ASP A  1 87  ? -2.574  -20.103 16.125  1.00 2.45  ? 87   ASP A CA  1 
ATOM   672   C  C   . ASP A  1 87  ? -2.804  -19.390 14.792  1.00 3.48  ? 87   ASP A C   1 
ATOM   673   O  O   . ASP A  1 87  ? -3.531  -18.399 14.738  1.00 2.00  ? 87   ASP A O   1 
ATOM   674   C  CB  . ASP A  1 87  ? -3.841  -20.856 16.579  1.00 3.65  ? 87   ASP A CB  1 
ATOM   675   C  CG  . ASP A  1 87  ? -4.301  -22.076 15.753  1.00 6.43  ? 87   ASP A CG  1 
ATOM   676   O  OD1 . ASP A  1 87  ? -3.481  -22.656 15.021  1.00 5.44  ? 87   ASP A OD1 1 
ATOM   677   O  OD2 . ASP A  1 87  ? -5.489  -22.426 15.863  1.00 7.33  ? 87   ASP A OD2 1 
ATOM   678   N  N   . GLU A  1 88  ? -2.194  -19.913 13.741  1.00 3.75  ? 88   GLU A N   1 
ATOM   679   C  CA  . GLU A  1 88  ? -2.386  -19.318 12.426  1.00 2.47  ? 88   GLU A CA  1 
ATOM   680   C  C   . GLU A  1 88  ? -3.259  -20.266 11.667  1.00 2.11  ? 88   GLU A C   1 
ATOM   681   O  O   . GLU A  1 88  ? -3.156  -20.358 10.453  1.00 2.00  ? 88   GLU A O   1 
ATOM   682   C  CB  . GLU A  1 88  ? -1.062  -19.216 11.650  1.00 3.86  ? 88   GLU A CB  1 
ATOM   683   C  CG  . GLU A  1 88  ? -0.137  -18.162 12.185  1.00 7.62  ? 88   GLU A CG  1 
ATOM   684   C  CD  . GLU A  1 88  ? -0.454  -16.820 11.579  1.00 10.69 ? 88   GLU A CD  1 
ATOM   685   O  OE1 . GLU A  1 88  ? -0.985  -16.774 10.454  1.00 11.76 ? 88   GLU A OE1 1 
ATOM   686   O  OE2 . GLU A  1 88  ? -0.184  -15.792 12.235  1.00 13.26 ? 88   GLU A OE2 1 
ATOM   687   N  N   . GLU A  1 89  ? -4.120  -20.997 12.356  1.00 3.20  ? 89   GLU A N   1 
ATOM   688   C  CA  . GLU A  1 89  ? -4.929  -21.984 11.669  1.00 3.26  ? 89   GLU A CA  1 
ATOM   689   C  C   . GLU A  1 89  ? -6.376  -21.619 11.447  1.00 3.34  ? 89   GLU A C   1 
ATOM   690   O  O   . GLU A  1 89  ? -7.094  -21.237 12.378  1.00 4.34  ? 89   GLU A O   1 
ATOM   691   C  CB  . GLU A  1 89  ? -4.840  -23.281 12.460  1.00 4.29  ? 89   GLU A CB  1 
ATOM   692   C  CG  . GLU A  1 89  ? -5.386  -24.466 11.725  1.00 10.54 ? 89   GLU A CG  1 
ATOM   693   C  CD  . GLU A  1 89  ? -4.943  -25.712 12.439  1.00 15.88 ? 89   GLU A CD  1 
ATOM   694   O  OE1 . GLU A  1 89  ? -3.716  -26.015 12.404  1.00 19.03 ? 89   GLU A OE1 1 
ATOM   695   O  OE2 . GLU A  1 89  ? -5.807  -26.401 13.027  1.00 20.25 ? 89   GLU A OE2 1 
ATOM   696   N  N   . GLY A  1 90  ? -6.799  -21.728 10.196  1.00 3.46  ? 90   GLY A N   1 
ATOM   697   C  CA  . GLY A  1 90  ? -8.169  -21.412 9.852   1.00 4.16  ? 90   GLY A CA  1 
ATOM   698   C  C   . GLY A  1 90  ? -8.319  -19.929 9.629   1.00 4.71  ? 90   GLY A C   1 
ATOM   699   O  O   . GLY A  1 90  ? -9.424  -19.431 9.422   1.00 7.40  ? 90   GLY A O   1 
ATOM   700   N  N   . VAL A  1 91  ? -7.192  -19.228 9.668   1.00 4.17  ? 91   VAL A N   1 
ATOM   701   C  CA  . VAL A  1 91  ? -7.152  -17.779 9.481   1.00 3.80  ? 91   VAL A CA  1 
ATOM   702   C  C   . VAL A  1 91  ? -7.186  -17.359 8.000   1.00 4.84  ? 91   VAL A C   1 
ATOM   703   O  O   . VAL A  1 91  ? -7.122  -16.162 7.686   1.00 4.38  ? 91   VAL A O   1 
ATOM   704   C  CB  . VAL A  1 91  ? -5.868  -17.213 10.109  1.00 2.00  ? 91   VAL A CB  1 
ATOM   705   C  CG1 . VAL A  1 91  ? -4.641  -17.841 9.472   1.00 2.27  ? 91   VAL A CG1 1 
ATOM   706   C  CG2 . VAL A  1 91  ? -5.833  -15.704 9.979   1.00 2.00  ? 91   VAL A CG2 1 
ATOM   707   N  N   . LEU A  1 92  ? -7.287  -18.337 7.095   1.00 4.33  ? 92   LEU A N   1 
ATOM   708   C  CA  . LEU A  1 92  ? -7.257  -18.046 5.665   1.00 2.39  ? 92   LEU A CA  1 
ATOM   709   C  C   . LEU A  1 92  ? -8.579  -17.656 5.061   1.00 2.36  ? 92   LEU A C   1 
ATOM   710   O  O   . LEU A  1 92  ? -9.612  -18.246 5.355   1.00 3.38  ? 92   LEU A O   1 
ATOM   711   C  CB  . LEU A  1 92  ? -6.682  -19.247 4.907   1.00 2.26  ? 92   LEU A CB  1 
ATOM   712   C  CG  . LEU A  1 92  ? -5.158  -19.317 4.900   1.00 2.00  ? 92   LEU A CG  1 
ATOM   713   C  CD1 . LEU A  1 92  ? -4.654  -19.919 3.596   1.00 2.68  ? 92   LEU A CD1 1 
ATOM   714   C  CD2 . LEU A  1 92  ? -4.546  -17.938 5.122   1.00 2.00  ? 92   LEU A CD2 1 
ATOM   715   N  N   . ASP A  1 93  ? -8.527  -16.649 4.230   1.00 2.00  ? 93   ASP A N   1 
ATOM   716   C  CA  . ASP A  1 93  ? -9.714  -16.142 3.530   1.00 2.53  ? 93   ASP A CA  1 
ATOM   717   C  C   . ASP A  1 93  ? -10.060 -17.122 2.419   1.00 3.77  ? 93   ASP A C   1 
ATOM   718   O  O   . ASP A  1 93  ? -9.372  -17.191 1.404   1.00 3.63  ? 93   ASP A O   1 
ATOM   719   C  CB  . ASP A  1 93  ? -9.422  -14.753 2.963   1.00 2.15  ? 93   ASP A CB  1 
ATOM   720   C  CG  . ASP A  1 93  ? -10.638 -14.105 2.354   1.00 2.00  ? 93   ASP A CG  1 
ATOM   721   O  OD1 . ASP A  1 93  ? -11.223 -14.693 1.421   1.00 2.00  ? 93   ASP A OD1 1 
ATOM   722   O  OD2 . ASP A  1 93  ? -11.002 -13.001 2.810   1.00 2.00  ? 93   ASP A OD2 1 
ATOM   723   N  N   . GLN A  1 94  ? -11.134 -17.878 2.608   1.00 4.68  ? 94   GLN A N   1 
ATOM   724   C  CA  . GLN A  1 94  ? -11.522 -18.913 1.628   1.00 6.00  ? 94   GLN A CA  1 
ATOM   725   C  C   . GLN A  1 94  ? -11.730 -18.409 0.202   1.00 6.39  ? 94   GLN A C   1 
ATOM   726   O  O   . GLN A  1 94  ? -11.622 -19.193 -0.740  1.00 6.78  ? 94   GLN A O   1 
ATOM   727   C  CB  . GLN A  1 94  ? -12.775 -19.632 2.098   1.00 7.54  ? 94   GLN A CB  1 
ATOM   728   C  CG  . GLN A  1 94  ? -12.490 -20.712 3.135   1.00 10.12 ? 94   GLN A CG  1 
ATOM   729   C  CD  . GLN A  1 94  ? -11.208 -21.472 2.840   1.00 12.14 ? 94   GLN A CD  1 
ATOM   730   O  OE1 . GLN A  1 94  ? -11.060 -22.062 1.765   1.00 12.75 ? 94   GLN A OE1 1 
ATOM   731   N  NE2 . GLN A  1 94  ? -10.167 -21.605 3.654   1.00 12.33 ? 94   GLN A NE2 1 
ATOM   732   N  N   . ASN A  1 95  ? -12.040 -17.137 0.026   1.00 6.63  ? 95   ASN A N   1 
ATOM   733   C  CA  . ASN A  1 95  ? -12.329 -16.644 -1.314  1.00 7.20  ? 95   ASN A CA  1 
ATOM   734   C  C   . ASN A  1 95  ? -11.579 -15.389 -1.761  1.00 5.75  ? 95   ASN A C   1 
ATOM   735   O  O   . ASN A  1 95  ? -12.173 -14.419 -2.258  1.00 5.15  ? 95   ASN A O   1 
ATOM   736   C  CB  . ASN A  1 95  ? -13.819 -16.418 -1.406  1.00 11.57 ? 95   ASN A CB  1 
ATOM   737   C  CG  . ASN A  1 95  ? -14.224 -16.117 -2.814  1.00 18.38 ? 95   ASN A CG  1 
ATOM   738   O  OD1 . ASN A  1 95  ? -13.550 -16.498 -3.784  1.00 15.50 ? 95   ASN A OD1 1 
ATOM   739   N  ND2 . ASN A  1 95  ? -15.350 -15.426 -2.954  1.00 28.95 ? 95   ASN A ND2 1 
ATOM   740   N  N   . ARG A  1 96  ? -10.261 -15.409 -1.575  1.00 4.65  ? 96   ARG A N   1 
ATOM   741   C  CA  . ARG A  1 96  ? -9.371  -14.303 -1.939  1.00 3.29  ? 96   ARG A CA  1 
ATOM   742   C  C   . ARG A  1 96  ? -7.906  -14.772 -2.099  1.00 2.87  ? 96   ARG A C   1 
ATOM   743   O  O   . ARG A  1 96  ? -7.278  -15.205 -1.131  1.00 2.00  ? 96   ARG A O   1 
ATOM   744   C  CB  . ARG A  1 96  ? -9.434  -13.217 -0.862  1.00 2.28  ? 96   ARG A CB  1 
ATOM   745   C  CG  . ARG A  1 96  ? -10.745 -12.452 -0.781  1.00 2.00  ? 96   ARG A CG  1 
ATOM   746   C  CD  . ARG A  1 96  ? -10.992 -11.671 -2.058  1.00 2.74  ? 96   ARG A CD  1 
ATOM   747   N  NE  . ARG A  1 96  ? -11.831 -10.486 -1.861  1.00 3.57  ? 96   ARG A NE  1 
ATOM   748   C  CZ  . ARG A  1 96  ? -13.155 -10.454 -1.992  1.00 3.40  ? 96   ARG A CZ  1 
ATOM   749   N  NH1 . ARG A  1 96  ? -13.830 -11.546 -2.325  1.00 2.79  ? 96   ARG A NH1 1 
ATOM   750   N  NH2 . ARG A  1 96  ? -13.808 -9.317  -1.794  1.00 3.88  ? 96   ARG A NH2 1 
ATOM   751   N  N   . SER A  1 97  ? -7.368  -14.677 -3.314  1.00 2.00  ? 97   SER A N   1 
ATOM   752   C  CA  . SER A  1 97  ? -5.986  -15.080 -3.585  1.00 2.00  ? 97   SER A CA  1 
ATOM   753   C  C   . SER A  1 97  ? -4.977  -14.203 -2.848  1.00 2.00  ? 97   SER A C   1 
ATOM   754   O  O   . SER A  1 97  ? -5.289  -13.076 -2.484  1.00 2.00  ? 97   SER A O   1 
ATOM   755   C  CB  . SER A  1 97  ? -5.702  -15.010 -5.091  1.00 2.14  ? 97   SER A CB  1 
ATOM   756   O  OG  . SER A  1 97  ? -5.976  -13.713 -5.585  1.00 2.00  ? 97   SER A OG  1 
ATOM   757   N  N   . LEU A  1 98  ? -3.765  -14.709 -2.633  1.00 2.06  ? 98   LEU A N   1 
ATOM   758   C  CA  . LEU A  1 98  ? -2.738  -13.926 -1.942  1.00 2.00  ? 98   LEU A CA  1 
ATOM   759   C  C   . LEU A  1 98  ? -2.475  -12.643 -2.736  1.00 2.00  ? 98   LEU A C   1 
ATOM   760   O  O   . LEU A  1 98  ? -2.032  -11.638 -2.178  1.00 2.00  ? 98   LEU A O   1 
ATOM   761   C  CB  . LEU A  1 98  ? -1.442  -14.767 -1.811  1.00 2.00  ? 98   LEU A CB  1 
ATOM   762   C  CG  . LEU A  1 98  ? -0.416  -14.378 -0.731  1.00 2.00  ? 98   LEU A CG  1 
ATOM   763   C  CD1 . LEU A  1 98  ? 0.971   -14.236 -1.352  1.00 2.00  ? 98   LEU A CD1 1 
ATOM   764   C  CD2 . LEU A  1 98  ? -0.840  -13.090 -0.026  1.00 2.00  ? 98   LEU A CD2 1 
ATOM   765   N  N   . LEU A  1 99  ? -2.767  -12.694 -4.039  1.00 2.00  ? 99   LEU A N   1 
ATOM   766   C  CA  . LEU A  1 99  ? -2.598  -11.564 -4.957  1.00 2.00  ? 99   LEU A CA  1 
ATOM   767   C  C   . LEU A  1 99  ? -3.414  -10.354 -4.520  1.00 2.91  ? 99   LEU A C   1 
ATOM   768   O  O   . LEU A  1 99  ? -2.937  -9.212  -4.552  1.00 3.04  ? 99   LEU A O   1 
ATOM   769   C  CB  . LEU A  1 99  ? -3.008  -11.951 -6.361  1.00 2.00  ? 99   LEU A CB  1 
ATOM   770   C  CG  . LEU A  1 99  ? -3.014  -10.772 -7.329  1.00 2.00  ? 99   LEU A CG  1 
ATOM   771   C  CD1 . LEU A  1 99  ? -1.605  -10.305 -7.623  1.00 2.15  ? 99   LEU A CD1 1 
ATOM   772   C  CD2 . LEU A  1 99  ? -3.736  -11.133 -8.610  1.00 2.47  ? 99   LEU A CD2 1 
ATOM   773   N  N   . PHE A  1 100 ? -4.659  -10.622 -4.113  1.00 2.20  ? 100  PHE A N   1 
ATOM   774   C  CA  . PHE A  1 100 ? -5.536  -9.599  -3.558  1.00 2.00  ? 100  PHE A CA  1 
ATOM   775   C  C   . PHE A  1 100 ? -4.719  -8.740  -2.611  1.00 2.58  ? 100  PHE A C   1 
ATOM   776   O  O   . PHE A  1 100 ? -4.546  -7.550  -2.838  1.00 3.96  ? 100  PHE A O   1 
ATOM   777   C  CB  . PHE A  1 100 ? -6.708  -10.245 -2.837  1.00 2.00  ? 100  PHE A CB  1 
ATOM   778   C  CG  . PHE A  1 100 ? -7.656  -9.331  -2.132  1.00 2.67  ? 100  PHE A CG  1 
ATOM   779   C  CD1 . PHE A  1 100 ? -8.179  -8.233  -2.813  1.00 3.49  ? 100  PHE A CD1 1 
ATOM   780   C  CD2 . PHE A  1 100 ? -8.043  -9.573  -0.823  1.00 3.28  ? 100  PHE A CD2 1 
ATOM   781   C  CE1 . PHE A  1 100 ? -9.078  -7.383  -2.204  1.00 4.49  ? 100  PHE A CE1 1 
ATOM   782   C  CE2 . PHE A  1 100 ? -8.972  -8.735  -0.195  1.00 4.94  ? 100  PHE A CE2 1 
ATOM   783   C  CZ  . PHE A  1 100 ? -9.495  -7.634  -0.890  1.00 6.38  ? 100  PHE A CZ  1 
ATOM   784   N  N   . MET A  1 101 ? -4.227  -9.376  -1.557  1.00 3.32  ? 101  MET A N   1 
ATOM   785   C  CA  . MET A  1 101 ? -3.410  -8.716  -0.554  1.00 2.09  ? 101  MET A CA  1 
ATOM   786   C  C   . MET A  1 101 ? -2.327  -7.893  -1.239  1.00 2.00  ? 101  MET A C   1 
ATOM   787   O  O   . MET A  1 101 ? -2.127  -6.718  -0.900  1.00 2.47  ? 101  MET A O   1 
ATOM   788   C  CB  . MET A  1 101 ? -2.794  -9.775  0.368   1.00 2.00  ? 101  MET A CB  1 
ATOM   789   C  CG  . MET A  1 101 ? -1.938  -9.196  1.490   1.00 2.00  ? 101  MET A CG  1 
ATOM   790   S  SD  . MET A  1 101 ? -0.382  -8.524  0.877   1.00 2.00  ? 101  MET A SD  1 
ATOM   791   C  CE  . MET A  1 101 ? 0.561   -10.018 0.610   1.00 2.00  ? 101  MET A CE  1 
ATOM   792   N  N   . GLN A  1 102 ? -1.652  -8.515  -2.197  1.00 2.00  ? 102  GLN A N   1 
ATOM   793   C  CA  . GLN A  1 102 ? -0.525  -7.861  -2.884  1.00 2.00  ? 102  GLN A CA  1 
ATOM   794   C  C   . GLN A  1 102 ? -0.897  -6.660  -3.756  1.00 2.00  ? 102  GLN A C   1 
ATOM   795   O  O   . GLN A  1 102 ? -0.120  -5.710  -3.809  1.00 2.42  ? 102  GLN A O   1 
ATOM   796   C  CB  . GLN A  1 102 ? 0.233   -8.890  -3.699  1.00 2.00  ? 102  GLN A CB  1 
ATOM   797   C  CG  . GLN A  1 102 ? 1.650   -8.419  -4.030  1.00 2.35  ? 102  GLN A CG  1 
ATOM   798   C  CD  . GLN A  1 102 ? 2.498   -8.101  -2.794  1.00 2.00  ? 102  GLN A CD  1 
ATOM   799   O  OE1 . GLN A  1 102 ? 2.833   -8.999  -2.010  1.00 2.02  ? 102  GLN A OE1 1 
ATOM   800   N  NE2 . GLN A  1 102 ? 2.934   -6.900  -2.435  1.00 2.00  ? 102  GLN A NE2 1 
ATOM   801   N  N   . TRP A  1 103 ? -2.036  -6.682  -4.445  1.00 2.57  ? 103  TRP A N   1 
ATOM   802   C  CA  . TRP A  1 103 ? -2.379  -5.536  -5.293  1.00 2.96  ? 103  TRP A CA  1 
ATOM   803   C  C   . TRP A  1 103 ? -2.731  -4.356  -4.409  1.00 2.45  ? 103  TRP A C   1 
ATOM   804   O  O   . TRP A  1 103 ? -2.551  -3.208  -4.785  1.00 3.89  ? 103  TRP A O   1 
ATOM   805   C  CB  . TRP A  1 103 ? -3.514  -5.871  -6.279  1.00 2.00  ? 103  TRP A CB  1 
ATOM   806   C  CG  . TRP A  1 103 ? -3.720  -4.792  -7.318  1.00 2.00  ? 103  TRP A CG  1 
ATOM   807   C  CD1 . TRP A  1 103 ? -4.784  -3.975  -7.476  1.00 3.47  ? 103  TRP A CD1 1 
ATOM   808   C  CD2 . TRP A  1 103 ? -2.778  -4.423  -8.340  1.00 2.18  ? 103  TRP A CD2 1 
ATOM   809   N  NE1 . TRP A  1 103 ? -4.577  -3.110  -8.524  1.00 4.16  ? 103  TRP A NE1 1 
ATOM   810   C  CE2 . TRP A  1 103 ? -3.352  -3.365  -9.075  1.00 2.56  ? 103  TRP A CE2 1 
ATOM   811   C  CE3 . TRP A  1 103 ? -1.507  -4.883  -8.707  1.00 2.62  ? 103  TRP A CE3 1 
ATOM   812   C  CZ2 . TRP A  1 103 ? -2.704  -2.757  -10.151 1.00 2.00  ? 103  TRP A CZ2 1 
ATOM   813   C  CZ3 . TRP A  1 103 ? -0.863  -4.277  -9.777  1.00 2.00  ? 103  TRP A CZ3 1 
ATOM   814   C  CH2 . TRP A  1 103 ? -1.466  -3.225  -10.485 1.00 2.00  ? 103  TRP A CH2 1 
ATOM   815   N  N   . GLY A  1 104 ? -3.247  -4.641  -3.220  1.00 2.00  ? 104  GLY A N   1 
ATOM   816   C  CA  . GLY A  1 104 ? -3.595  -3.566  -2.318  1.00 2.00  ? 104  GLY A CA  1 
ATOM   817   C  C   . GLY A  1 104 ? -2.373  -2.758  -1.935  1.00 2.00  ? 104  GLY A C   1 
ATOM   818   O  O   . GLY A  1 104 ? -2.430  -1.535  -1.828  1.00 2.73  ? 104  GLY A O   1 
ATOM   819   N  N   . GLN A  1 105 ? -1.256  -3.443  -1.739  1.00 2.00  ? 105  GLN A N   1 
ATOM   820   C  CA  . GLN A  1 105 ? -0.033  -2.773  -1.342  1.00 2.00  ? 105  GLN A CA  1 
ATOM   821   C  C   . GLN A  1 105 ? 0.574   -1.970  -2.472  1.00 2.00  ? 105  GLN A C   1 
ATOM   822   O  O   . GLN A  1 105 ? 1.358   -1.056  -2.236  1.00 2.00  ? 105  GLN A O   1 
ATOM   823   C  CB  . GLN A  1 105 ? 0.986   -3.788  -0.832  1.00 2.00  ? 105  GLN A CB  1 
ATOM   824   C  CG  . GLN A  1 105 ? 2.322   -3.168  -0.515  1.00 2.00  ? 105  GLN A CG  1 
ATOM   825   C  CD  . GLN A  1 105 ? 3.279   -4.129  0.148   1.00 2.00  ? 105  GLN A CD  1 
ATOM   826   O  OE1 . GLN A  1 105 ? 3.598   -5.194  -0.389  1.00 2.00  ? 105  GLN A OE1 1 
ATOM   827   N  NE2 . GLN A  1 105 ? 3.876   -3.971  1.330   1.00 2.76  ? 105  GLN A NE2 1 
ATOM   828   N  N   . ILE A  1 106 ? 0.227   -2.313  -3.703  1.00 2.00  ? 106  ILE A N   1 
ATOM   829   C  CA  . ILE A  1 106 ? 0.767   -1.590  -4.841  1.00 2.00  ? 106  ILE A CA  1 
ATOM   830   C  C   . ILE A  1 106 ? -0.010  -0.291  -5.058  1.00 2.53  ? 106  ILE A C   1 
ATOM   831   O  O   . ILE A  1 106 ? 0.574   0.764   -5.259  1.00 3.20  ? 106  ILE A O   1 
ATOM   832   C  CB  . ILE A  1 106 ? 0.699   -2.451  -6.124  1.00 2.00  ? 106  ILE A CB  1 
ATOM   833   C  CG1 . ILE A  1 106 ? 1.685   -3.625  -6.053  1.00 2.00  ? 106  ILE A CG1 1 
ATOM   834   C  CG2 . ILE A  1 106 ? 0.991   -1.607  -7.357  1.00 2.00  ? 106  ILE A CG2 1 
ATOM   835   C  CD1 . ILE A  1 106 ? 2.795   -3.559  -7.082  1.00 2.00  ? 106  ILE A CD1 1 
ATOM   836   N  N   . VAL A  1 107 ? -1.328  -0.407  -5.034  1.00 2.00  ? 107  VAL A N   1 
ATOM   837   C  CA  . VAL A  1 107 ? -2.171  0.746   -5.137  1.00 2.00  ? 107  VAL A CA  1 
ATOM   838   C  C   . VAL A  1 107 ? -1.842  1.746   -4.051  1.00 2.00  ? 107  VAL A C   1 
ATOM   839   O  O   . VAL A  1 107 ? -1.823  2.946   -4.313  1.00 2.26  ? 107  VAL A O   1 
ATOM   840   C  CB  . VAL A  1 107 ? -3.669  0.363   -5.062  1.00 2.14  ? 107  VAL A CB  1 
ATOM   841   C  CG1 . VAL A  1 107 ? -4.547  1.591   -5.236  1.00 2.00  ? 107  VAL A CG1 1 
ATOM   842   C  CG2 . VAL A  1 107 ? -4.004  -0.670  -6.112  1.00 3.06  ? 107  VAL A CG2 1 
ATOM   843   N  N   . ASP A  1 108 ? -1.569  1.267   -2.787  1.00 2.00  ? 108  ASP A N   1 
ATOM   844   C  CA  . ASP A  1 108 ? -1.214  2.159   -1.625  1.00 2.00  ? 108  ASP A CA  1 
ATOM   845   C  C   . ASP A  1 108 ? 0.097   2.893   -1.880  1.00 2.00  ? 108  ASP A C   1 
ATOM   846   O  O   . ASP A  1 108 ? 0.163   4.109   -1.713  1.00 2.00  ? 108  ASP A O   1 
ATOM   847   C  CB  . ASP A  1 108 ? -1.069  1.404   -0.286  1.00 3.53  ? 108  ASP A CB  1 
ATOM   848   C  CG  . ASP A  1 108 ? -0.521  2.247   0.872   1.00 4.12  ? 108  ASP A CG  1 
ATOM   849   O  OD1 . ASP A  1 108 ? 0.702   2.467   0.919   1.00 2.00  ? 108  ASP A OD1 1 
ATOM   850   O  OD2 . ASP A  1 108 ? -1.318  2.686   1.715   1.00 7.85  ? 108  ASP A OD2 1 
ATOM   851   N  N   . HIS A  1 109 ? 1.146   2.172   -2.275  1.00 2.44  ? 109  HIS A N   1 
ATOM   852   C  CA  . HIS A  1 109 ? 2.474   2.754   -2.511  1.00 2.00  ? 109  HIS A CA  1 
ATOM   853   C  C   . HIS A  1 109 ? 2.483   3.763   -3.661  1.00 2.00  ? 109  HIS A C   1 
ATOM   854   O  O   . HIS A  1 109 ? 3.368   4.636   -3.694  1.00 2.13  ? 109  HIS A O   1 
ATOM   855   C  CB  . HIS A  1 109 ? 3.474   1.649   -2.783  1.00 3.47  ? 109  HIS A CB  1 
ATOM   856   C  CG  . HIS A  1 109 ? 4.041   1.022   -1.498  1.00 2.66  ? 109  HIS A CG  1 
ATOM   857   N  ND1 . HIS A  1 109 ? 4.781   -0.140  -1.510  1.00 2.10  ? 109  HIS A ND1 1 
ATOM   858   C  CD2 . HIS A  1 109 ? 3.985   1.415   -0.203  1.00 2.34  ? 109  HIS A CD2 1 
ATOM   859   C  CE1 . HIS A  1 109 ? 5.157   -0.435  -0.281  1.00 2.00  ? 109  HIS A CE1 1 
ATOM   860   N  NE2 . HIS A  1 109 ? 4.686   0.495   0.531   1.00 2.00  ? 109  HIS A NE2 1 
ATOM   861   N  N   . ASP A  1 110 ? 1.512   3.689   -4.651  1.00 2.00  ? 110  ASP A N   1 
ATOM   862   C  CA  . ASP A  1 110 ? 1.364   4.597   -5.802  1.00 2.00  ? 110  ASP A CA  1 
ATOM   863   C  C   . ASP A  1 110 ? 0.787   5.898   -5.267  1.00 2.00  ? 110  ASP A C   1 
ATOM   864   O  O   . ASP A  1 110 ? 0.977   6.961   -5.859  1.00 2.00  ? 110  ASP A O   1 
ATOM   865   C  CB  . ASP A  1 110 ? 0.414   3.984   -6.862  1.00 2.00  ? 110  ASP A CB  1 
ATOM   866   C  CG  . ASP A  1 110 ? 0.420   4.687   -8.201  1.00 2.58  ? 110  ASP A CG  1 
ATOM   867   O  OD1 . ASP A  1 110 ? 0.498   5.928   -8.250  1.00 2.00  ? 110  ASP A OD1 1 
ATOM   868   O  OD2 . ASP A  1 110 ? 0.356   3.987   -9.243  1.00 2.58  ? 110  ASP A OD2 1 
ATOM   869   N  N   . LEU A  1 111 ? 0.063   5.815   -4.125  1.00 2.94  ? 111  LEU A N   1 
ATOM   870   C  CA  . LEU A  1 111 ? -0.625  6.971   -3.574  1.00 2.00  ? 111  LEU A CA  1 
ATOM   871   C  C   . LEU A  1 111 ? 0.033   7.715   -2.427  1.00 2.00  ? 111  LEU A C   1 
ATOM   872   O  O   . LEU A  1 111 ? -0.234  8.915   -2.277  1.00 2.00  ? 111  LEU A O   1 
ATOM   873   C  CB  . LEU A  1 111 ? -2.061  6.570   -3.202  1.00 2.00  ? 111  LEU A CB  1 
ATOM   874   C  CG  . LEU A  1 111 ? -2.895  5.987   -4.333  1.00 2.00  ? 111  LEU A CG  1 
ATOM   875   C  CD1 . LEU A  1 111 ? -4.137  5.327   -3.777  1.00 2.00  ? 111  LEU A CD1 1 
ATOM   876   C  CD2 . LEU A  1 111 ? -3.263  7.054   -5.356  1.00 2.00  ? 111  LEU A CD2 1 
ATOM   877   N  N   . ASP A  1 112 ? 0.841   7.113   -1.548  1.00 2.00  ? 112  ASP A N   1 
ATOM   878   C  CA  . ASP A  1 112 ? 1.289   7.899   -0.402  1.00 2.72  ? 112  ASP A CA  1 
ATOM   879   C  C   . ASP A  1 112 ? 2.596   7.381   0.268   1.00 2.19  ? 112  ASP A C   1 
ATOM   880   O  O   . ASP A  1 112 ? 2.761   6.179   0.522   1.00 2.00  ? 112  ASP A O   1 
ATOM   881   C  CB  . ASP A  1 112 ? 0.074   8.035   0.675   1.00 2.46  ? 112  ASP A CB  1 
ATOM   882   C  CG  . ASP A  1 112 ? -0.701  6.828   1.308   1.00 2.00  ? 112  ASP A CG  1 
ATOM   883   O  OD1 . ASP A  1 112 ? -1.439  6.141   0.569   1.00 2.00  ? 112  ASP A OD1 1 
ATOM   884   O  OD2 . ASP A  1 112 ? -0.540  6.581   2.518   1.00 2.00  ? 112  ASP A OD2 1 
ATOM   885   N  N   . PHE A  1 113 ? 3.560   8.353   0.560   1.00 2.00  ? 113  PHE A N   1 
ATOM   886   C  CA  . PHE A  1 113 ? 4.778   8.119   1.350   1.00 2.51  ? 113  PHE A CA  1 
ATOM   887   C  C   . PHE A  1 113 ? 5.021   9.299   2.318   1.00 2.00  ? 113  PHE A C   1 
ATOM   888   O  O   . PHE A  1 113 ? 5.305   10.393  1.863   1.00 2.00  ? 113  PHE A O   1 
ATOM   889   C  CB  . PHE A  1 113 ? 6.033   7.989   0.487   1.00 2.59  ? 113  PHE A CB  1 
ATOM   890   C  CG  . PHE A  1 113 ? 7.184   7.258   1.180   1.00 2.84  ? 113  PHE A CG  1 
ATOM   891   C  CD1 . PHE A  1 113 ? 7.047   6.784   2.486   1.00 2.00  ? 113  PHE A CD1 1 
ATOM   892   C  CD2 . PHE A  1 113 ? 8.389   7.058   0.519   1.00 3.48  ? 113  PHE A CD2 1 
ATOM   893   C  CE1 . PHE A  1 113 ? 8.084   6.121   3.109   1.00 2.00  ? 113  PHE A CE1 1 
ATOM   894   C  CE2 . PHE A  1 113 ? 9.431   6.363   1.139   1.00 4.39  ? 113  PHE A CE2 1 
ATOM   895   C  CZ  . PHE A  1 113 ? 9.276   5.893   2.433   1.00 2.91  ? 113  PHE A CZ  1 
ATOM   896   N  N   . ALA A  1 114 ? 4.896   9.104   3.647   1.00 2.00  ? 114  ALA A N   1 
ATOM   897   C  CA  . ALA A  1 114 ? 5.282   10.097  4.638   1.00 2.00  ? 114  ALA A CA  1 
ATOM   898   C  C   . ALA A  1 114 ? 6.656   9.590   5.113   1.00 3.79  ? 114  ALA A C   1 
ATOM   899   O  O   . ALA A  1 114 ? 6.759   8.574   5.780   1.00 3.65  ? 114  ALA A O   1 
ATOM   900   C  CB  . ALA A  1 114 ? 4.260   10.213  5.767   1.00 2.00  ? 114  ALA A CB  1 
ATOM   901   N  N   . PRO A  1 115 ? 7.711   10.342  4.682   1.00 4.91  ? 115  PRO A N   1 
ATOM   902   C  CA  . PRO A  1 115 ? 9.074   9.990   5.055   1.00 7.29  ? 115  PRO A CA  1 
ATOM   903   C  C   . PRO A  1 115 ? 9.341   9.993   6.514   1.00 11.61 ? 115  PRO A C   1 
ATOM   904   O  O   . PRO A  1 115 ? 9.157   11.045  7.134   1.00 11.39 ? 115  PRO A O   1 
ATOM   905   C  CB  . PRO A  1 115 ? 9.934   11.004  4.375   1.00 6.95  ? 115  PRO A CB  1 
ATOM   906   C  CG  . PRO A  1 115 ? 9.261   11.089  3.049   1.00 5.33  ? 115  PRO A CG  1 
ATOM   907   C  CD  . PRO A  1 115 ? 7.840   10.668  3.262   1.00 5.32  ? 115  PRO A CD  1 
ATOM   908   N  N   . GLU A  1 116 ? 9.769   8.929   7.185   1.00 17.12 ? 116  GLU A N   1 
ATOM   909   C  CA  . GLU A  1 116 ? 10.090  9.420   8.524   1.00 21.91 ? 116  GLU A CA  1 
ATOM   910   C  C   . GLU A  1 116 ? 11.386  10.292  8.345   1.00 25.09 ? 116  GLU A C   1 
ATOM   911   O  O   . GLU A  1 116 ? 12.097  10.236  7.334   1.00 24.49 ? 116  GLU A O   1 
ATOM   912   C  CB  . GLU A  1 116 ? 10.125  8.315   9.547   1.00 20.97 ? 116  GLU A CB  1 
ATOM   913   C  CG  . GLU A  1 116 ? 10.022  6.937   8.982   1.00 22.31 ? 116  GLU A CG  1 
ATOM   914   C  CD  . GLU A  1 116 ? 11.187  6.220   9.581   1.00 22.99 ? 116  GLU A CD  1 
ATOM   915   O  OE1 . GLU A  1 116 ? 12.286  6.267   9.006   1.00 23.60 ? 116  GLU A OE1 1 
ATOM   916   O  OE2 . GLU A  1 116 ? 11.020  5.611   10.663  1.00 22.77 ? 116  GLU A OE2 1 
ATOM   917   N  N   . THR A  1 117 ? 11.607  11.104  9.411   1.00 29.01 ? 117  THR A N   1 
ATOM   918   C  CA  . THR A  1 117 ? 12.548  12.211  9.543   1.00 32.56 ? 117  THR A CA  1 
ATOM   919   C  C   . THR A  1 117 ? 13.997  12.052  9.322   1.00 36.34 ? 117  THR A C   1 
ATOM   920   O  O   . THR A  1 117 ? 14.497  11.936  8.215   1.00 37.24 ? 117  THR A O   1 
ATOM   921   C  CB  . THR A  1 117 ? 12.535  12.785  10.963  1.00 31.54 ? 117  THR A CB  1 
ATOM   922   O  OG1 . THR A  1 117 ? 11.965  11.825  11.855  1.00 31.20 ? 117  THR A OG1 1 
ATOM   923   C  CG2 . THR A  1 117 ? 11.735  14.069  11.009  1.00 31.90 ? 117  THR A CG2 1 
ATOM   924   N  N   . GLU A  1 118 ? 14.642  12.063  10.389  1.00 41.56 ? 118  GLU A N   1 
ATOM   925   C  CA  . GLU A  1 118 ? 15.967  12.206  10.195  1.00 46.34 ? 118  GLU A CA  1 
ATOM   926   C  C   . GLU A  1 118 ? 16.835  11.013  10.028  1.00 47.53 ? 118  GLU A C   1 
ATOM   927   O  O   . GLU A  1 118 ? 16.545  9.860   10.323  1.00 47.12 ? 118  GLU A O   1 
ATOM   928   C  CB  . GLU A  1 118 ? 16.521  13.095  11.307  1.00 49.07 ? 118  GLU A CB  1 
ATOM   929   C  CG  . GLU A  1 118 ? 17.347  14.226  10.712  1.00 51.16 ? 118  GLU A CG  1 
ATOM   930   C  CD  . GLU A  1 118 ? 16.606  15.556  10.661  1.00 52.17 ? 118  GLU A CD  1 
ATOM   931   O  OE1 . GLU A  1 118 ? 15.600  15.676  9.930   1.00 52.45 ? 118  GLU A OE1 1 
ATOM   932   O  OE2 . GLU A  1 118 ? 17.053  16.477  11.359  1.00 52.33 ? 118  GLU A OE2 1 
ATOM   933   N  N   . LEU A  1 119 ? 17.928  11.448  9.510   1.00 49.81 ? 119  LEU A N   1 
ATOM   934   C  CA  . LEU A  1 119 ? 19.059  10.614  9.289   1.00 51.66 ? 119  LEU A CA  1 
ATOM   935   C  C   . LEU A  1 119 ? 20.091  11.153  10.259  1.00 52.73 ? 119  LEU A C   1 
ATOM   936   O  O   . LEU A  1 119 ? 20.150  10.778  11.443  1.00 52.76 ? 119  LEU A O   1 
ATOM   937   C  CB  . LEU A  1 119 ? 19.568  10.688  7.829   1.00 50.98 ? 119  LEU A CB  1 
ATOM   938   C  CG  . LEU A  1 119 ? 19.244  11.923  6.955   1.00 51.16 ? 119  LEU A CG  1 
ATOM   939   C  CD1 . LEU A  1 119 ? 17.763  12.003  6.653   1.00 51.59 ? 119  LEU A CD1 1 
ATOM   940   C  CD2 . LEU A  1 119 ? 19.719  13.193  7.634   1.00 50.46 ? 119  LEU A CD2 1 
ATOM   941   N  N   . GLY A  1 120 ? 20.879  12.050  9.712   1.00 53.92 ? 120  GLY A N   1 
ATOM   942   C  CA  . GLY A  1 120 ? 21.897  12.708  10.406  1.00 55.12 ? 120  GLY A CA  1 
ATOM   943   C  C   . GLY A  1 120 ? 23.077  12.827  9.488   1.00 55.49 ? 120  GLY A C   1 
ATOM   944   O  O   . GLY A  1 120 ? 23.508  13.919  9.111   1.00 55.92 ? 120  GLY A O   1 
ATOM   945   N  N   . SER A  1 121 ? 23.613  11.619  9.089   1.00 55.64 ? 121  SER A N   1 
ATOM   946   C  CA  . SER A  1 121 ? 24.858  11.495  8.288   1.00 55.91 ? 121  SER A CA  1 
ATOM   947   C  C   . SER A  1 121 ? 25.927  11.596  9.273   1.00 55.48 ? 121  SER A C   1 
ATOM   948   O  O   . SER A  1 121 ? 26.482  12.642  9.598   1.00 55.22 ? 121  SER A O   1 
ATOM   949   C  CB  . SER A  1 121 ? 25.061  12.632  7.284   1.00 55.95 ? 121  SER A CB  1 
ATOM   950   O  OG  . SER A  1 121 ? 23.950  12.754  6.412   1.00 55.38 ? 121  SER A OG  1 
ATOM   951   N  N   . SER A  1 122 ? 26.235  10.426  9.780   1.00 55.52 ? 122  SER A N   1 
ATOM   952   C  CA  . SER A  1 122 ? 27.162  10.241  10.868  1.00 56.58 ? 122  SER A CA  1 
ATOM   953   C  C   . SER A  1 122 ? 26.567  10.964  12.072  1.00 55.54 ? 122  SER A C   1 
ATOM   954   O  O   . SER A  1 122 ? 26.873  12.113  12.375  1.00 54.85 ? 122  SER A O   1 
ATOM   955   C  CB  . SER A  1 122 ? 28.583  10.762  10.533  1.00 57.76 ? 122  SER A CB  1 
ATOM   956   O  OG  . SER A  1 122 ? 29.563  10.058  11.285  1.00 58.85 ? 122  SER A OG  1 
ATOM   957   N  N   . GLU A  1 123 ? 25.681  10.229  12.773  1.00 53.67 ? 123  GLU A N   1 
ATOM   958   C  CA  . GLU A  1 123 ? 24.992  10.795  13.893  1.00 51.79 ? 123  GLU A CA  1 
ATOM   959   C  C   . GLU A  1 123 ? 25.099  10.036  15.224  1.00 51.18 ? 123  GLU A C   1 
ATOM   960   O  O   . GLU A  1 123 ? 25.139  8.807   15.289  1.00 49.57 ? 123  GLU A O   1 
ATOM   961   C  CB  . GLU A  1 123 ? 23.538  10.991  13.456  1.00 51.71 ? 123  GLU A CB  1 
ATOM   962   C  CG  . GLU A  1 123 ? 22.678  11.723  14.460  1.00 52.14 ? 123  GLU A CG  1 
ATOM   963   C  CD  . GLU A  1 123 ? 22.633  13.220  14.233  1.00 52.56 ? 123  GLU A CD  1 
ATOM   964   O  OE1 . GLU A  1 123 ? 21.986  13.643  13.256  1.00 53.06 ? 123  GLU A OE1 1 
ATOM   965   O  OE2 . GLU A  1 123 ? 23.232  13.969  15.045  1.00 52.28 ? 123  GLU A OE2 1 
ATOM   966   N  N   . HIS A  1 124 ? 25.185  10.827  16.283  1.00 50.82 ? 124  HIS A N   1 
ATOM   967   C  CA  . HIS A  1 124 ? 25.268  10.336  17.646  1.00 50.15 ? 124  HIS A CA  1 
ATOM   968   C  C   . HIS A  1 124 ? 23.896  10.259  18.209  1.00 48.02 ? 124  HIS A C   1 
ATOM   969   O  O   . HIS A  1 124 ? 23.707  9.865   19.359  1.00 47.19 ? 124  HIS A O   1 
ATOM   970   C  CB  . HIS A  1 124 ? 26.051  11.329  18.487  1.00 54.00 ? 124  HIS A CB  1 
ATOM   971   C  CG  . HIS A  1 124 ? 27.415  10.834  18.981  1.00 57.13 ? 124  HIS A CG  1 
ATOM   972   N  ND1 . HIS A  1 124 ? 28.593  11.193  18.370  1.00 58.15 ? 124  HIS A ND1 1 
ATOM   973   C  CD2 . HIS A  1 124 ? 27.756  10.039  20.024  1.00 58.14 ? 124  HIS A CD2 1 
ATOM   974   C  CE1 . HIS A  1 124 ? 29.607  10.650  19.016  1.00 59.11 ? 124  HIS A CE1 1 
ATOM   975   N  NE2 . HIS A  1 124 ? 29.127  9.946   20.026  1.00 59.29 ? 124  HIS A NE2 1 
ATOM   976   N  N   . SER A  1 125 ? 22.911  10.645  17.403  1.00 45.73 ? 125  SER A N   1 
ATOM   977   C  CA  . SER A  1 125 ? 21.535  10.673  17.876  1.00 43.81 ? 125  SER A CA  1 
ATOM   978   C  C   . SER A  1 125 ? 20.660  9.482   17.503  1.00 42.05 ? 125  SER A C   1 
ATOM   979   O  O   . SER A  1 125 ? 19.622  9.264   18.126  1.00 43.23 ? 125  SER A O   1 
ATOM   980   C  CB  . SER A  1 125 ? 20.856  11.972  17.419  1.00 43.56 ? 125  SER A CB  1 
ATOM   981   O  OG  . SER A  1 125 ? 20.398  11.879  16.083  1.00 42.15 ? 125  SER A OG  1 
ATOM   982   N  N   . LYS A  1 126 ? 21.048  8.725   16.484  1.00 38.72 ? 126  LYS A N   1 
ATOM   983   C  CA  . LYS A  1 126 ? 20.300  7.509   16.142  1.00 34.57 ? 126  LYS A CA  1 
ATOM   984   C  C   . LYS A  1 126 ? 20.626  6.537   17.262  1.00 33.74 ? 126  LYS A C   1 
ATOM   985   O  O   . LYS A  1 126 ? 19.845  5.656   17.624  1.00 32.82 ? 126  LYS A O   1 
ATOM   986   C  CB  . LYS A  1 126 ? 20.751  6.908   14.821  1.00 31.90 ? 126  LYS A CB  1 
ATOM   987   C  CG  . LYS A  1 126 ? 20.877  7.884   13.669  1.00 29.25 ? 126  LYS A CG  1 
ATOM   988   C  CD  . LYS A  1 126 ? 21.311  7.174   12.394  1.00 27.81 ? 126  LYS A CD  1 
ATOM   989   C  CE  . LYS A  1 126 ? 21.619  8.160   11.280  1.00 26.56 ? 126  LYS A CE  1 
ATOM   990   N  NZ  . LYS A  1 126 ? 22.868  8.925   11.550  1.00 25.08 ? 126  LYS A NZ  1 
ATOM   991   N  N   . VAL A  1 127 ? 21.814  6.742   17.809  1.00 34.12 ? 127  VAL A N   1 
ATOM   992   C  CA  . VAL A  1 127 ? 22.337  5.933   18.882  1.00 35.33 ? 127  VAL A CA  1 
ATOM   993   C  C   . VAL A  1 127 ? 21.635  6.181   20.224  1.00 34.61 ? 127  VAL A C   1 
ATOM   994   O  O   . VAL A  1 127 ? 21.546  5.272   21.044  1.00 34.75 ? 127  VAL A O   1 
ATOM   995   C  CB  . VAL A  1 127 ? 23.846  6.198   19.053  1.00 36.03 ? 127  VAL A CB  1 
ATOM   996   C  CG1 . VAL A  1 127 ? 24.507  5.059   19.831  1.00 37.02 ? 127  VAL A CG1 1 
ATOM   997   C  CG2 . VAL A  1 127 ? 24.511  6.369   17.686  1.00 36.11 ? 127  VAL A CG2 1 
ATOM   998   N  N   . GLN A  1 128 ? 21.124  7.393   20.475  1.00 33.73 ? 128  GLN A N   1 
ATOM   999   C  CA  . GLN A  1 128 ? 20.481  7.732   21.753  1.00 32.01 ? 128  GLN A CA  1 
ATOM   1000  C  C   . GLN A  1 128 ? 19.035  7.267   21.863  1.00 30.83 ? 128  GLN A C   1 
ATOM   1001  O  O   . GLN A  1 128 ? 18.391  7.417   22.901  1.00 30.46 ? 128  GLN A O   1 
ATOM   1002  C  CB  . GLN A  1 128 ? 20.573  9.247   21.987  1.00 33.87 ? 128  GLN A CB  1 
ATOM   1003  C  CG  . GLN A  1 128 ? 20.418  9.679   23.432  1.00 35.14 ? 128  GLN A CG  1 
ATOM   1004  C  CD  . GLN A  1 128 ? 20.876  11.113  23.676  1.00 36.00 ? 128  GLN A CD  1 
ATOM   1005  O  OE1 . GLN A  1 128 ? 20.052  12.030  23.742  1.00 35.71 ? 128  GLN A OE1 1 
ATOM   1006  N  NE2 . GLN A  1 128 ? 22.137  11.513  23.833  1.00 35.39 ? 128  GLN A NE2 1 
ATOM   1007  N  N   . CYS A  1 129 ? 18.504  6.714   20.782  1.00 29.02 ? 129  CYS A N   1 
ATOM   1008  C  CA  . CYS A  1 129 ? 17.122  6.252   20.706  1.00 27.15 ? 129  CYS A CA  1 
ATOM   1009  C  C   . CYS A  1 129 ? 17.032  4.702   20.633  1.00 27.50 ? 129  CYS A C   1 
ATOM   1010  O  O   . CYS A  1 129 ? 16.003  4.099   20.993  1.00 27.99 ? 129  CYS A O   1 
ATOM   1011  C  CB  . CYS A  1 129 ? 16.455  6.865   19.471  1.00 23.78 ? 129  CYS A CB  1 
ATOM   1012  S  SG  . CYS A  1 129 ? 14.643  7.033   19.605  1.00 20.08 ? 129  CYS A SG  1 
ATOM   1013  N  N   . GLU A  1 130 ? 18.115  4.079   20.162  1.00 27.25 ? 130  GLU A N   1 
ATOM   1014  C  CA  . GLU A  1 130 ? 18.207  2.622   20.033  1.00 28.02 ? 130  GLU A CA  1 
ATOM   1015  C  C   . GLU A  1 130 ? 19.138  2.036   21.117  1.00 29.25 ? 130  GLU A C   1 
ATOM   1016  O  O   . GLU A  1 130 ? 19.733  0.973   20.922  1.00 31.08 ? 130  GLU A O   1 
ATOM   1017  C  CB  . GLU A  1 130 ? 18.713  2.253   18.644  1.00 29.13 ? 130  GLU A CB  1 
ATOM   1018  C  CG  . GLU A  1 130 ? 18.676  0.762   18.325  1.00 30.87 ? 130  GLU A CG  1 
ATOM   1019  C  CD  . GLU A  1 130 ? 19.042  0.436   16.884  1.00 31.83 ? 130  GLU A CD  1 
ATOM   1020  O  OE1 . GLU A  1 130 ? 18.877  -0.743  16.494  1.00 31.84 ? 130  GLU A OE1 1 
ATOM   1021  O  OE2 . GLU A  1 130 ? 19.490  1.344   16.142  1.00 31.58 ? 130  GLU A OE2 1 
ATOM   1022  N  N   . GLU A  1 131 ? 19.263  2.717   22.258  1.00 27.94 ? 131  GLU A N   1 
ATOM   1023  C  CA  . GLU A  1 131 ? 20.145  2.245   23.329  1.00 25.75 ? 131  GLU A CA  1 
ATOM   1024  C  C   . GLU A  1 131 ? 19.646  2.621   24.714  1.00 25.58 ? 131  GLU A C   1 
ATOM   1025  O  O   . GLU A  1 131 ? 19.586  1.782   25.611  1.00 25.18 ? 131  GLU A O   1 
ATOM   1026  C  CB  . GLU A  1 131 ? 21.552  2.822   23.148  1.00 27.69 ? 131  GLU A CB  1 
ATOM   1027  C  CG  . GLU A  1 131 ? 22.221  2.490   21.816  1.00 30.67 ? 131  GLU A CG  1 
ATOM   1028  C  CD  . GLU A  1 131 ? 22.979  1.171   21.837  1.00 31.82 ? 131  GLU A CD  1 
ATOM   1029  O  OE1 . GLU A  1 131 ? 22.379  0.135   22.209  1.00 32.69 ? 131  GLU A OE1 1 
ATOM   1030  O  OE2 . GLU A  1 131 ? 24.178  1.176   21.474  1.00 32.09 ? 131  GLU A OE2 1 
ATOM   1031  N  N   . TYR A  1 132 ? 19.295  3.891   24.888  1.00 25.37 ? 132  TYR A N   1 
ATOM   1032  C  CA  . TYR A  1 132 ? 18.821  4.387   26.179  1.00 24.23 ? 132  TYR A CA  1 
ATOM   1033  C  C   . TYR A  1 132 ? 17.329  4.707   26.137  1.00 23.07 ? 132  TYR A C   1 
ATOM   1034  O  O   . TYR A  1 132 ? 16.721  5.035   27.165  1.00 22.73 ? 132  TYR A O   1 
ATOM   1035  C  CB  . TYR A  1 132 ? 19.624  5.628   26.578  1.00 25.67 ? 132  TYR A CB  1 
ATOM   1036  C  CG  . TYR A  1 132 ? 21.044  5.598   26.050  1.00 28.47 ? 132  TYR A CG  1 
ATOM   1037  C  CD1 . TYR A  1 132 ? 21.302  5.810   24.691  1.00 29.76 ? 132  TYR A CD1 1 
ATOM   1038  C  CD2 . TYR A  1 132 ? 22.129  5.332   26.892  1.00 28.65 ? 132  TYR A CD2 1 
ATOM   1039  C  CE1 . TYR A  1 132 ? 22.597  5.759   24.178  1.00 30.34 ? 132  TYR A CE1 1 
ATOM   1040  C  CE2 . TYR A  1 132 ? 23.437  5.277   26.385  1.00 29.77 ? 132  TYR A CE2 1 
ATOM   1041  C  CZ  . TYR A  1 132 ? 23.655  5.493   25.024  1.00 30.13 ? 132  TYR A CZ  1 
ATOM   1042  O  OH  . TYR A  1 132 ? 24.921  5.450   24.521  1.00 30.89 ? 132  TYR A OH  1 
ATOM   1043  N  N   . CYS A  1 133 ? 16.745  4.605   24.942  1.00 20.48 ? 133  CYS A N   1 
ATOM   1044  C  CA  . CYS A  1 133 ? 15.322  4.856   24.766  1.00 17.42 ? 133  CYS A CA  1 
ATOM   1045  C  C   . CYS A  1 133 ? 14.907  6.149   25.452  1.00 17.49 ? 133  CYS A C   1 
ATOM   1046  O  O   . CYS A  1 133 ? 14.013  6.165   26.307  1.00 16.04 ? 133  CYS A O   1 
ATOM   1047  C  CB  . CYS A  1 133 ? 14.498  3.697   25.322  1.00 15.90 ? 133  CYS A CB  1 
ATOM   1048  S  SG  . CYS A  1 133 ? 14.825  2.091   24.529  1.00 12.40 ? 133  CYS A SG  1 
ATOM   1049  N  N   . ILE A  1 134 ? 15.566  7.235   25.073  1.00 16.99 ? 134  ILE A N   1 
ATOM   1050  C  CA  . ILE A  1 134 ? 15.264  8.518   25.665  1.00 16.44 ? 134  ILE A CA  1 
ATOM   1051  C  C   . ILE A  1 134 ? 14.450  9.353   24.692  1.00 15.87 ? 134  ILE A C   1 
ATOM   1052  O  O   . ILE A  1 134 ? 14.832  9.562   23.537  1.00 14.03 ? 134  ILE A O   1 
ATOM   1053  C  CB  . ILE A  1 134 ? 16.560  9.268   26.056  1.00 17.71 ? 134  ILE A CB  1 
ATOM   1054  C  CG1 . ILE A  1 134 ? 17.564  8.328   26.718  1.00 19.00 ? 134  ILE A CG1 1 
ATOM   1055  C  CG2 . ILE A  1 134 ? 16.250  10.447  26.968  1.00 18.22 ? 134  ILE A CG2 1 
ATOM   1056  C  CD1 . ILE A  1 134 ? 18.142  8.853   28.013  1.00 19.42 ? 134  ILE A CD1 1 
ATOM   1057  N  N   . GLN A  1 135 ? 13.311  9.802   25.180  1.00 16.47 ? 135  GLN A N   1 
ATOM   1058  C  CA  . GLN A  1 135 ? 12.393  10.678  24.452  1.00 15.80 ? 135  GLN A CA  1 
ATOM   1059  C  C   . GLN A  1 135 ? 13.123  11.978  24.090  1.00 14.81 ? 135  GLN A C   1 
ATOM   1060  O  O   . GLN A  1 135 ? 13.888  12.508  24.896  1.00 14.08 ? 135  GLN A O   1 
ATOM   1061  C  CB  . GLN A  1 135 ? 11.186  11.032  25.324  1.00 18.34 ? 135  GLN A CB  1 
ATOM   1062  C  CG  . GLN A  1 135 ? 9.900   11.232  24.563  1.00 21.42 ? 135  GLN A CG  1 
ATOM   1063  C  CD  . GLN A  1 135 ? 8.903   10.129  24.843  1.00 24.08 ? 135  GLN A CD  1 
ATOM   1064  O  OE1 . GLN A  1 135 ? 7.696   10.315  24.689  1.00 26.41 ? 135  GLN A OE1 1 
ATOM   1065  N  NE2 . GLN A  1 135 ? 9.185   8.903   25.255  1.00 26.07 ? 135  GLN A NE2 1 
ATOM   1066  N  N   . GLY A  1 136 ? 12.885  12.536  22.887  1.00 14.35 ? 136  GLY A N   1 
ATOM   1067  C  CA  . GLY A  1 136 ? 13.531  13.769  22.516  1.00 14.57 ? 136  GLY A CA  1 
ATOM   1068  C  C   . GLY A  1 136 ? 13.330  14.266  21.077  1.00 14.49 ? 136  GLY A C   1 
ATOM   1069  O  O   . GLY A  1 136 ? 14.018  13.820  20.156  1.00 14.01 ? 136  GLY A O   1 
ATOM   1070  N  N   . ASP A  1 137 ? 12.401  15.205  20.865  1.00 14.77 ? 137  ASP A N   1 
ATOM   1071  C  CA  . ASP A  1 137 ? 12.155  15.938  19.559  1.00 15.90 ? 137  ASP A CA  1 
ATOM   1072  C  C   . ASP A  1 137 ? 12.143  15.225  18.197  1.00 14.24 ? 137  ASP A C   1 
ATOM   1073  O  O   . ASP A  1 137 ? 11.499  15.695  17.272  1.00 14.31 ? 137  ASP A O   1 
ATOM   1074  C  CB  . ASP A  1 137 ? 13.249  17.016  19.388  1.00 19.06 ? 137  ASP A CB  1 
ATOM   1075  C  CG  . ASP A  1 137 ? 14.257  16.707  18.256  1.00 21.20 ? 137  ASP A CG  1 
ATOM   1076  O  OD1 . ASP A  1 137 ? 14.603  15.531  18.076  1.00 21.65 ? 137  ASP A OD1 1 
ATOM   1077  O  OD2 . ASP A  1 137 ? 14.675  17.662  17.582  1.00 21.74 ? 137  ASP A OD2 1 
ATOM   1078  N  N   . ASN A  1 138 ? 12.832  14.102  18.072  1.00 10.84 ? 138  ASN A N   1 
ATOM   1079  C  CA  . ASN A  1 138 ? 12.724  13.435  16.784  1.00 9.53  ? 138  ASN A CA  1 
ATOM   1080  C  C   . ASN A  1 138 ? 12.575  11.982  17.029  1.00 6.80  ? 138  ASN A C   1 
ATOM   1081  O  O   . ASN A  1 138 ? 12.213  11.193  16.143  1.00 5.46  ? 138  ASN A O   1 
ATOM   1082  C  CB  . ASN A  1 138 ? 13.896  13.762  15.840  1.00 12.26 ? 138  ASN A CB  1 
ATOM   1083  C  CG  . ASN A  1 138 ? 13.434  14.418  14.542  1.00 16.49 ? 138  ASN A CG  1 
ATOM   1084  O  OD1 . ASN A  1 138 ? 13.305  13.764  13.505  1.00 16.23 ? 138  ASN A OD1 1 
ATOM   1085  N  ND2 . ASN A  1 138 ? 13.203  15.730  14.601  1.00 17.02 ? 138  ASN A ND2 1 
ATOM   1086  N  N   . CYS A  1 139 ? 12.861  11.644  18.257  1.00 5.59  ? 139  CYS A N   1 
ATOM   1087  C  CA  . CYS A  1 139 ? 12.780  10.282  18.674  1.00 4.92  ? 139  CYS A CA  1 
ATOM   1088  C  C   . CYS A  1 139 ? 11.642  10.137  19.693  1.00 3.36  ? 139  CYS A C   1 
ATOM   1089  O  O   . CYS A  1 139 ? 11.714  10.652  20.803  1.00 3.14  ? 139  CYS A O   1 
ATOM   1090  C  CB  . CYS A  1 139 ? 14.141  9.824   19.233  1.00 8.98  ? 139  CYS A CB  1 
ATOM   1091  S  SG  . CYS A  1 139 ? 14.022  8.542   20.526  1.00 15.52 ? 139  CYS A SG  1 
ATOM   1092  N  N   . PHE A  1 140 ? 10.620  9.416   19.316  1.00 3.62  ? 140  PHE A N   1 
ATOM   1093  C  CA  . PHE A  1 140 ? 9.432   9.142   20.144  1.00 3.67  ? 140  PHE A CA  1 
ATOM   1094  C  C   . PHE A  1 140 ? 9.370   7.596   20.250  1.00 5.32  ? 140  PHE A C   1 
ATOM   1095  O  O   . PHE A  1 140 ? 8.839   6.923   19.375  1.00 7.17  ? 140  PHE A O   1 
ATOM   1096  C  CB  . PHE A  1 140 ? 8.236   9.806   19.515  1.00 2.53  ? 140  PHE A CB  1 
ATOM   1097  C  CG  . PHE A  1 140 ? 6.935   9.389   20.096  1.00 3.16  ? 140  PHE A CG  1 
ATOM   1098  C  CD1 . PHE A  1 140 ? 6.783   9.244   21.471  1.00 3.08  ? 140  PHE A CD1 1 
ATOM   1099  C  CD2 . PHE A  1 140 ? 5.851   9.129   19.263  1.00 2.68  ? 140  PHE A CD2 1 
ATOM   1100  C  CE1 . PHE A  1 140 ? 5.571   8.849   22.009  1.00 2.44  ? 140  PHE A CE1 1 
ATOM   1101  C  CE2 . PHE A  1 140 ? 4.635   8.736   19.790  1.00 2.75  ? 140  PHE A CE2 1 
ATOM   1102  C  CZ  . PHE A  1 140 ? 4.493   8.594   21.170  1.00 2.63  ? 140  PHE A CZ  1 
ATOM   1103  N  N   . PRO A  1 141 ? 9.985   7.062   21.344  1.00 5.91  ? 141  PRO A N   1 
ATOM   1104  C  CA  . PRO A  1 141 ? 10.085  5.584   21.582  1.00 2.71  ? 141  PRO A CA  1 
ATOM   1105  C  C   . PRO A  1 141 ? 8.863   4.800   21.706  1.00 2.76  ? 141  PRO A C   1 
ATOM   1106  O  O   . PRO A  1 141 ? 7.801   5.339   22.040  1.00 2.00  ? 141  PRO A O   1 
ATOM   1107  C  CB  . PRO A  1 141 ? 10.914  5.469   22.820  1.00 3.07  ? 141  PRO A CB  1 
ATOM   1108  C  CG  . PRO A  1 141 ? 11.929  6.562   22.613  1.00 3.95  ? 141  PRO A CG  1 
ATOM   1109  C  CD  . PRO A  1 141 ? 11.323  7.583   21.683  1.00 4.96  ? 141  PRO A CD  1 
ATOM   1110  N  N   . ILE A  1 142 ? 8.972   3.514   21.479  1.00 3.50  ? 142  ILE A N   1 
ATOM   1111  C  CA  . ILE A  1 142 ? 7.844   2.733   21.815  1.00 3.10  ? 142  ILE A CA  1 
ATOM   1112  C  C   . ILE A  1 142 ? 8.300   1.934   23.005  1.00 3.83  ? 142  ILE A C   1 
ATOM   1113  O  O   . ILE A  1 142 ? 9.209   1.092   22.908  1.00 2.52  ? 142  ILE A O   1 
ATOM   1114  C  CB  . ILE A  1 142 ? 7.394   1.763   20.741  1.00 2.39  ? 142  ILE A CB  1 
ATOM   1115  C  CG1 . ILE A  1 142 ? 7.099   2.507   19.438  1.00 2.90  ? 142  ILE A CG1 1 
ATOM   1116  C  CG2 . ILE A  1 142 ? 6.175   0.990   21.198  1.00 2.00  ? 142  ILE A CG2 1 
ATOM   1117  C  CD1 . ILE A  1 142 ? 6.560   1.633   18.325  1.00 3.76  ? 142  ILE A CD1 1 
ATOM   1118  N  N   . MET A  1 143 ? 7.681   2.188   24.155  1.00 6.06  ? 143  MET A N   1 
ATOM   1119  C  CA  . MET A  1 143 ? 8.065   1.503   25.380  1.00 8.04  ? 143  MET A CA  1 
ATOM   1120  C  C   . MET A  1 143 ? 7.439   0.118   25.502  1.00 8.11  ? 143  MET A C   1 
ATOM   1121  O  O   . MET A  1 143 ? 6.349   -0.127  24.994  1.00 7.05  ? 143  MET A O   1 
ATOM   1122  C  CB  . MET A  1 143 ? 7.662   2.359   26.587  1.00 11.12 ? 143  MET A CB  1 
ATOM   1123  C  CG  . MET A  1 143 ? 8.797   2.669   27.555  1.00 15.03 ? 143  MET A CG  1 
ATOM   1124  S  SD  . MET A  1 143 ? 10.175  3.506   26.755  1.00 18.64 ? 143  MET A SD  1 
ATOM   1125  C  CE  . MET A  1 143 ? 10.651  4.668   28.033  1.00 19.38 ? 143  MET A CE  1 
ATOM   1126  N  N   . PHE A  1 144 ? 8.146   -0.786  26.173  1.00 9.23  ? 144  PHE A N   1 
ATOM   1127  C  CA  . PHE A  1 144 ? 7.656   -2.113  26.434  1.00 10.59 ? 144  PHE A CA  1 
ATOM   1128  C  C   . PHE A  1 144 ? 6.917   -2.142  27.788  1.00 11.43 ? 144  PHE A C   1 
ATOM   1129  O  O   . PHE A  1 144 ? 7.443   -1.697  28.807  1.00 12.89 ? 144  PHE A O   1 
ATOM   1130  C  CB  . PHE A  1 144 ? 8.812   -3.139  26.524  1.00 12.03 ? 144  PHE A CB  1 
ATOM   1131  C  CG  . PHE A  1 144 ? 9.533   -3.400  25.242  1.00 13.89 ? 144  PHE A CG  1 
ATOM   1132  C  CD1 . PHE A  1 144 ? 10.907  -3.588  25.238  1.00 14.62 ? 144  PHE A CD1 1 
ATOM   1133  C  CD2 . PHE A  1 144 ? 8.843   -3.472  24.040  1.00 15.35 ? 144  PHE A CD2 1 
ATOM   1134  C  CE1 . PHE A  1 144 ? 11.588  -3.841  24.056  1.00 16.66 ? 144  PHE A CE1 1 
ATOM   1135  C  CE2 . PHE A  1 144 ? 9.512   -3.726  22.848  1.00 17.21 ? 144  PHE A CE2 1 
ATOM   1136  C  CZ  . PHE A  1 144 ? 10.889  -3.910  22.855  1.00 17.71 ? 144  PHE A CZ  1 
ATOM   1137  N  N   . PRO A  1 145 ? 5.717   -2.668  27.767  1.00 12.54 ? 145  PRO A N   1 
ATOM   1138  C  CA  . PRO A  1 145 ? 4.944   -2.853  28.999  1.00 15.33 ? 145  PRO A CA  1 
ATOM   1139  C  C   . PRO A  1 145 ? 5.679   -3.760  29.975  1.00 16.36 ? 145  PRO A C   1 
ATOM   1140  O  O   . PRO A  1 145 ? 6.729   -4.304  29.641  1.00 17.90 ? 145  PRO A O   1 
ATOM   1141  C  CB  . PRO A  1 145 ? 3.585   -3.293  28.477  1.00 13.96 ? 145  PRO A CB  1 
ATOM   1142  C  CG  . PRO A  1 145 ? 3.448   -2.469  27.234  1.00 13.49 ? 145  PRO A CG  1 
ATOM   1143  C  CD  . PRO A  1 145 ? 4.808   -2.092  26.771  1.00 12.69 ? 145  PRO A CD  1 
ATOM   1144  N  N   . LYS A  1 146 ? 5.121   -3.922  31.154  1.00 17.40 ? 146  LYS A N   1 
ATOM   1145  C  CA  . LYS A  1 146 ? 5.670   -4.839  32.145  1.00 18.84 ? 146  LYS A CA  1 
ATOM   1146  C  C   . LYS A  1 146 ? 5.309   -6.268  31.724  1.00 17.65 ? 146  LYS A C   1 
ATOM   1147  O  O   . LYS A  1 146 ? 4.296   -6.467  31.048  1.00 15.09 ? 146  LYS A O   1 
ATOM   1148  C  CB  . LYS A  1 146 ? 5.132   -4.544  33.544  1.00 20.72 ? 146  LYS A CB  1 
ATOM   1149  C  CG  . LYS A  1 146 ? 4.951   -5.773  34.428  1.00 22.40 ? 146  LYS A CG  1 
ATOM   1150  C  CD  . LYS A  1 146 ? 4.054   -5.497  35.617  1.00 24.81 ? 146  LYS A CD  1 
ATOM   1151  C  CE  . LYS A  1 146 ? 3.640   -6.799  36.281  1.00 26.02 ? 146  LYS A CE  1 
ATOM   1152  N  NZ  . LYS A  1 146 ? 2.602   -6.582  37.340  1.00 27.45 ? 146  LYS A NZ  1 
ATOM   1153  N  N   . ASN A  1 147 ? 6.117   -7.233  32.106  1.00 17.37 ? 147  ASN A N   1 
ATOM   1154  C  CA  . ASN A  1 147 ? 5.802   -8.620  31.820  1.00 18.19 ? 147  ASN A CA  1 
ATOM   1155  C  C   . ASN A  1 147 ? 5.626   -8.942  30.347  1.00 16.11 ? 147  ASN A C   1 
ATOM   1156  O  O   . ASN A  1 147 ? 4.780   -9.766  29.985  1.00 16.37 ? 147  ASN A O   1 
ATOM   1157  C  CB  . ASN A  1 147 ? 4.569   -9.032  32.613  1.00 21.26 ? 147  ASN A CB  1 
ATOM   1158  C  CG  . ASN A  1 147 ? 4.915   -9.455  34.030  1.00 23.29 ? 147  ASN A CG  1 
ATOM   1159  O  OD1 . ASN A  1 147 ? 4.051   -9.486  34.902  1.00 23.36 ? 147  ASN A OD1 1 
ATOM   1160  N  ND2 . ASN A  1 147 ? 6.197   -9.768  34.257  1.00 23.13 ? 147  ASN A ND2 1 
ATOM   1161  N  N   . ASP A  1 148 ? 6.456   -8.292  29.501  1.00 12.32 ? 148  ASP A N   1 
ATOM   1162  C  CA  . ASP A  1 148 ? 6.427   -8.455  28.027  1.00 7.15  ? 148  ASP A CA  1 
ATOM   1163  C  C   . ASP A  1 148 ? 7.718   -9.160  27.491  1.00 5.76  ? 148  ASP A C   1 
ATOM   1164  O  O   . ASP A  1 148 ? 8.827   -8.838  27.930  1.00 6.15  ? 148  ASP A O   1 
ATOM   1165  C  CB  . ASP A  1 148 ? 6.247   -7.121  27.344  1.00 7.55  ? 148  ASP A CB  1 
ATOM   1166  C  CG  . ASP A  1 148 ? 6.415   -7.280  25.839  1.00 6.98  ? 148  ASP A CG  1 
ATOM   1167  O  OD1 . ASP A  1 148 ? 7.446   -7.806  25.385  1.00 6.93  ? 148  ASP A OD1 1 
ATOM   1168  O  OD2 . ASP A  1 148 ? 5.489   -6.866  25.100  1.00 4.15  ? 148  ASP A OD2 1 
ATOM   1169  N  N   . PRO A  1 149 ? 7.577   -10.130 26.542  1.00 4.00  ? 149  PRO A N   1 
ATOM   1170  C  CA  . PRO A  1 149 ? 8.772   -11.002 26.147  1.00 3.31  ? 149  PRO A CA  1 
ATOM   1171  C  C   . PRO A  1 149 ? 9.992   -10.297 25.715  1.00 2.77  ? 149  PRO A C   1 
ATOM   1172  O  O   . PRO A  1 149 ? 11.112  -10.610 26.094  1.00 5.15  ? 149  PRO A O   1 
ATOM   1173  C  CB  . PRO A  1 149 ? 8.252   -11.932 25.076  1.00 2.27  ? 149  PRO A CB  1 
ATOM   1174  C  CG  . PRO A  1 149 ? 6.908   -12.241 25.625  1.00 3.58  ? 149  PRO A CG  1 
ATOM   1175  C  CD  . PRO A  1 149 ? 6.473   -11.110 26.535  1.00 3.40  ? 149  PRO A CD  1 
ATOM   1176  N  N   . LYS A  1 150 ? 9.687   -9.316  24.901  1.00 2.00  ? 150  LYS A N   1 
ATOM   1177  C  CA  . LYS A  1 150 ? 10.693  -8.506  24.275  1.00 2.98  ? 150  LYS A CA  1 
ATOM   1178  C  C   . LYS A  1 150 ? 11.624  -7.872  25.274  1.00 2.01  ? 150  LYS A C   1 
ATOM   1179  O  O   . LYS A  1 150 ? 12.732  -7.497  24.934  1.00 2.00  ? 150  LYS A O   1 
ATOM   1180  C  CB  . LYS A  1 150 ? 10.037  -7.451  23.371  1.00 3.41  ? 150  LYS A CB  1 
ATOM   1181  C  CG  . LYS A  1 150 ? 9.180   -8.042  22.267  1.00 4.59  ? 150  LYS A CG  1 
ATOM   1182  C  CD  . LYS A  1 150 ? 9.626   -7.576  20.894  1.00 4.71  ? 150  LYS A CD  1 
ATOM   1183  C  CE  . LYS A  1 150 ? 9.002   -8.424  19.806  1.00 3.90  ? 150  LYS A CE  1 
ATOM   1184  N  NZ  . LYS A  1 150 ? 9.417   -9.849  19.905  1.00 4.73  ? 150  LYS A NZ  1 
ATOM   1185  N  N   . LEU A  1 151 ? 11.164  -7.755  26.496  1.00 2.50  ? 151  LEU A N   1 
ATOM   1186  C  CA  . LEU A  1 151 ? 11.960  -7.182  27.601  1.00 2.00  ? 151  LEU A CA  1 
ATOM   1187  C  C   . LEU A  1 151 ? 13.196  -8.021  27.907  1.00 2.83  ? 151  LEU A C   1 
ATOM   1188  O  O   . LEU A  1 151 ? 14.329  -7.526  27.912  1.00 2.00  ? 151  LEU A O   1 
ATOM   1189  C  CB  . LEU A  1 151 ? 11.095  -7.118  28.861  1.00 2.00  ? 151  LEU A CB  1 
ATOM   1190  C  CG  . LEU A  1 151 ? 11.045  -5.786  29.628  1.00 2.00  ? 151  LEU A CG  1 
ATOM   1191  C  CD1 . LEU A  1 151 ? 9.604   -5.343  29.866  1.00 2.85  ? 151  LEU A CD1 1 
ATOM   1192  C  CD2 . LEU A  1 151 ? 11.799  -5.907  30.940  1.00 3.85  ? 151  LEU A CD2 1 
ATOM   1193  N  N   . LYS A  1 152 ? 12.967  -9.302  28.163  1.00 3.30  ? 152  LYS A N   1 
ATOM   1194  C  CA  . LYS A  1 152 ? 14.055  -10.213 28.466  1.00 3.10  ? 152  LYS A CA  1 
ATOM   1195  C  C   . LYS A  1 152 ? 15.053  -10.261 27.309  1.00 5.32  ? 152  LYS A C   1 
ATOM   1196  O  O   . LYS A  1 152 ? 16.265  -10.420 27.544  1.00 5.50  ? 152  LYS A O   1 
ATOM   1197  C  CB  . LYS A  1 152 ? 13.495  -11.608 28.816  1.00 2.42  ? 152  LYS A CB  1 
ATOM   1198  C  CG  . LYS A  1 152 ? 12.305  -11.580 29.753  1.00 3.52  ? 152  LYS A CG  1 
ATOM   1199  C  CD  . LYS A  1 152 ? 11.981  -12.960 30.326  1.00 3.46  ? 152  LYS A CD  1 
ATOM   1200  C  CE  . LYS A  1 152 ? 11.012  -12.862 31.495  1.00 3.71  ? 152  LYS A CE  1 
ATOM   1201  N  NZ  . LYS A  1 152 ? 10.399  -14.176 31.828  1.00 4.09  ? 152  LYS A NZ  1 
ATOM   1202  N  N   . THR A  1 153 ? 14.491  -10.156 26.069  1.00 4.99  ? 153  THR A N   1 
ATOM   1203  C  CA  . THR A  1 153 ? 15.231  -10.366 24.795  1.00 3.05  ? 153  THR A CA  1 
ATOM   1204  C  C   . THR A  1 153 ? 15.742  -9.199  23.949  1.00 4.45  ? 153  THR A C   1 
ATOM   1205  O  O   . THR A  1 153 ? 16.778  -9.362  23.319  1.00 4.64  ? 153  THR A O   1 
ATOM   1206  C  CB  . THR A  1 153 ? 14.357  -11.281 23.908  1.00 2.00  ? 153  THR A CB  1 
ATOM   1207  O  OG1 . THR A  1 153 ? 14.197  -12.536 24.561  1.00 2.00  ? 153  THR A OG1 1 
ATOM   1208  C  CG2 . THR A  1 153 ? 15.000  -11.482 22.552  1.00 2.35  ? 153  THR A CG2 1 
ATOM   1209  N  N   . GLN A  1 154 ? 15.087  -8.072  23.912  1.00 4.79  ? 154  GLN A N   1 
ATOM   1210  C  CA  . GLN A  1 154 ? 15.597  -7.077  22.967  1.00 4.28  ? 154  GLN A CA  1 
ATOM   1211  C  C   . GLN A  1 154 ? 16.001  -5.904  23.793  1.00 3.43  ? 154  GLN A C   1 
ATOM   1212  O  O   . GLN A  1 154 ? 17.064  -5.327  23.622  1.00 2.83  ? 154  GLN A O   1 
ATOM   1213  C  CB  . GLN A  1 154 ? 14.569  -6.657  21.948  1.00 4.27  ? 154  GLN A CB  1 
ATOM   1214  C  CG  . GLN A  1 154 ? 14.739  -7.253  20.581  1.00 2.00  ? 154  GLN A CG  1 
ATOM   1215  C  CD  . GLN A  1 154 ? 13.479  -7.053  19.781  1.00 2.00  ? 154  GLN A CD  1 
ATOM   1216  O  OE1 . GLN A  1 154 ? 12.462  -7.707  20.009  1.00 2.00  ? 154  GLN A OE1 1 
ATOM   1217  N  NE2 . GLN A  1 154 ? 13.321  -6.188  18.780  1.00 2.39  ? 154  GLN A NE2 1 
ATOM   1218  N  N   . GLY A  1 155 ? 15.124  -5.550  24.718  1.00 3.15  ? 155  GLY A N   1 
ATOM   1219  C  CA  . GLY A  1 155 ? 15.492  -4.406  25.527  1.00 5.18  ? 155  GLY A CA  1 
ATOM   1220  C  C   . GLY A  1 155 ? 14.371  -3.672  26.270  1.00 8.16  ? 155  GLY A C   1 
ATOM   1221  O  O   . GLY A  1 155 ? 13.475  -4.269  26.841  1.00 8.13  ? 155  GLY A O   1 
ATOM   1222  N  N   . LYS A  1 156 ? 14.471  -2.349  26.229  1.00 9.97  ? 156  LYS A N   1 
ATOM   1223  C  CA  . LYS A  1 156 ? 13.535  -1.478  26.921  1.00 11.09 ? 156  LYS A CA  1 
ATOM   1224  C  C   . LYS A  1 156 ? 12.467  -0.915  26.001  1.00 11.36 ? 156  LYS A C   1 
ATOM   1225  O  O   . LYS A  1 156 ? 11.326  -0.708  26.409  1.00 11.47 ? 156  LYS A O   1 
ATOM   1226  C  CB  . LYS A  1 156 ? 14.304  -0.320  27.563  1.00 12.85 ? 156  LYS A CB  1 
ATOM   1227  C  CG  . LYS A  1 156 ? 14.158  -0.230  29.073  1.00 16.07 ? 156  LYS A CG  1 
ATOM   1228  C  CD  . LYS A  1 156 ? 15.121  0.794   29.670  1.00 19.00 ? 156  LYS A CD  1 
ATOM   1229  C  CE  . LYS A  1 156 ? 14.977  0.856   31.185  1.00 20.60 ? 156  LYS A CE  1 
ATOM   1230  N  NZ  . LYS A  1 156 ? 14.932  -0.498  31.798  1.00 22.74 ? 156  LYS A NZ  1 
ATOM   1231  N  N   . CYS A  1 157 ? 12.836  -0.686  24.779  1.00 9.27  ? 157  CYS A N   1 
ATOM   1232  C  CA  . CYS A  1 157 ? 11.944  -0.128  23.815  1.00 7.89  ? 157  CYS A CA  1 
ATOM   1233  C  C   . CYS A  1 157 ? 12.482  -0.356  22.414  1.00 9.17  ? 157  CYS A C   1 
ATOM   1234  O  O   . CYS A  1 157 ? 13.641  -0.774  22.243  1.00 10.42 ? 157  CYS A O   1 
ATOM   1235  C  CB  . CYS A  1 157 ? 11.828  1.369   24.026  1.00 8.79  ? 157  CYS A CB  1 
ATOM   1236  S  SG  . CYS A  1 157 ? 13.236  2.319   23.364  1.00 9.13  ? 157  CYS A SG  1 
ATOM   1237  N  N   . MET A  1 158 ? 11.640  -0.079  21.433  1.00 8.05  ? 158  MET A N   1 
ATOM   1238  C  CA  . MET A  1 158 ? 12.094  -0.188  20.063  1.00 5.37  ? 158  MET A CA  1 
ATOM   1239  C  C   . MET A  1 158 ? 12.005  1.172   19.383  1.00 4.67  ? 158  MET A C   1 
ATOM   1240  O  O   . MET A  1 158 ? 11.043  1.903   19.529  1.00 3.27  ? 158  MET A O   1 
ATOM   1241  C  CB  . MET A  1 158 ? 11.294  -1.211  19.296  1.00 5.41  ? 158  MET A CB  1 
ATOM   1242  C  CG  . MET A  1 158 ? 9.817   -1.091  19.526  1.00 4.75  ? 158  MET A CG  1 
ATOM   1243  S  SD  . MET A  1 158 ? 8.897   -2.374  18.670  1.00 7.14  ? 158  MET A SD  1 
ATOM   1244  C  CE  . MET A  1 158 ? 9.248   -3.789  19.707  1.00 5.28  ? 158  MET A CE  1 
ATOM   1245  N  N   . PRO A  1 159 ? 13.070  1.471   18.610  1.00 3.10  ? 159  PRO A N   1 
ATOM   1246  C  CA  . PRO A  1 159 ? 13.169  2.815   17.919  1.00 3.50  ? 159  PRO A CA  1 
ATOM   1247  C  C   . PRO A  1 159 ? 11.951  3.298   17.152  1.00 4.40  ? 159  PRO A C   1 
ATOM   1248  O  O   . PRO A  1 159 ? 11.205  2.498   16.572  1.00 4.70  ? 159  PRO A O   1 
ATOM   1249  C  CB  . PRO A  1 159 ? 14.470  2.716   17.155  1.00 3.96  ? 159  PRO A CB  1 
ATOM   1250  C  CG  . PRO A  1 159 ? 15.317  1.970   18.135  1.00 4.72  ? 159  PRO A CG  1 
ATOM   1251  C  CD  . PRO A  1 159 ? 14.447  1.110   19.010  1.00 4.05  ? 159  PRO A CD  1 
ATOM   1252  N  N   . PHE A  1 160 ? 11.728  4.590   17.128  1.00 4.55  ? 160  PHE A N   1 
ATOM   1253  C  CA  . PHE A  1 160 ? 10.612  5.130   16.378  1.00 4.64  ? 160  PHE A CA  1 
ATOM   1254  C  C   . PHE A  1 160 ? 10.813  6.620   16.224  1.00 5.09  ? 160  PHE A C   1 
ATOM   1255  O  O   . PHE A  1 160 ? 10.830  7.361   17.208  1.00 4.33  ? 160  PHE A O   1 
ATOM   1256  C  CB  . PHE A  1 160 ? 9.280   4.857   17.087  1.00 4.55  ? 160  PHE A CB  1 
ATOM   1257  C  CG  . PHE A  1 160 ? 8.111   5.347   16.273  1.00 3.53  ? 160  PHE A CG  1 
ATOM   1258  C  CD1 . PHE A  1 160 ? 7.794   6.697   16.252  1.00 3.03  ? 160  PHE A CD1 1 
ATOM   1259  C  CD2 . PHE A  1 160 ? 7.356   4.463   15.517  1.00 2.32  ? 160  PHE A CD2 1 
ATOM   1260  C  CE1 . PHE A  1 160 ? 6.744   7.161   15.491  1.00 4.54  ? 160  PHE A CE1 1 
ATOM   1261  C  CE2 . PHE A  1 160 ? 6.307   4.911   14.754  1.00 3.84  ? 160  PHE A CE2 1 
ATOM   1262  C  CZ  . PHE A  1 160 ? 5.995   6.268   14.737  1.00 4.97  ? 160  PHE A CZ  1 
ATOM   1263  N  N   . PHE A  1 161 ? 10.963  7.047   14.976  1.00 7.01  ? 161  PHE A N   1 
ATOM   1264  C  CA  . PHE A  1 161 ? 11.171  8.454   14.661  1.00 8.25  ? 161  PHE A CA  1 
ATOM   1265  C  C   . PHE A  1 161 ? 9.942   9.058   14.002  1.00 8.09  ? 161  PHE A C   1 
ATOM   1266  O  O   . PHE A  1 161 ? 9.435   8.533   13.016  1.00 8.63  ? 161  PHE A O   1 
ATOM   1267  C  CB  . PHE A  1 161 ? 12.358  8.613   13.720  1.00 9.25  ? 161  PHE A CB  1 
ATOM   1268  C  CG  . PHE A  1 161 ? 13.656  8.176   14.306  1.00 9.67  ? 161  PHE A CG  1 
ATOM   1269  C  CD1 . PHE A  1 161 ? 13.878  6.843   14.625  1.00 10.72 ? 161  PHE A CD1 1 
ATOM   1270  C  CD2 . PHE A  1 161 ? 14.656  9.101   14.550  1.00 10.32 ? 161  PHE A CD2 1 
ATOM   1271  C  CE1 . PHE A  1 161 ? 15.083  6.438   15.180  1.00 10.80 ? 161  PHE A CE1 1 
ATOM   1272  C  CE2 . PHE A  1 161 ? 15.863  8.709   15.105  1.00 11.22 ? 161  PHE A CE2 1 
ATOM   1273  C  CZ  . PHE A  1 161 ? 16.078  7.376   15.421  1.00 11.61 ? 161  PHE A CZ  1 
ATOM   1274  N  N   . ARG A  1 162 ? 9.479   10.176  14.540  1.00 8.35  ? 162  ARG A N   1 
ATOM   1275  C  CA  . ARG A  1 162 ? 8.306   10.850  14.003  1.00 8.53  ? 162  ARG A CA  1 
ATOM   1276  C  C   . ARG A  1 162 ? 8.483   11.114  12.519  1.00 6.84  ? 162  ARG A C   1 
ATOM   1277  O  O   . ARG A  1 162 ? 9.610   11.200  12.041  1.00 6.30  ? 162  ARG A O   1 
ATOM   1278  C  CB  . ARG A  1 162 ? 8.072   12.153  14.744  1.00 7.61  ? 162  ARG A CB  1 
ATOM   1279  C  CG  . ARG A  1 162 ? 8.439   12.059  16.200  1.00 5.53  ? 162  ARG A CG  1 
ATOM   1280  C  CD  . ARG A  1 162 ? 8.007   13.319  16.910  1.00 5.46  ? 162  ARG A CD  1 
ATOM   1281  N  NE  . ARG A  1 162 ? 6.693   13.766  16.489  1.00 5.04  ? 162  ARG A NE  1 
ATOM   1282  C  CZ  . ARG A  1 162 ? 6.203   14.972  16.816  1.00 5.24  ? 162  ARG A CZ  1 
ATOM   1283  N  NH1 . ARG A  1 162 ? 6.928   15.820  17.536  1.00 5.93  ? 162  ARG A NH1 1 
ATOM   1284  N  NH2 . ARG A  1 162 ? 4.983   15.316  16.408  1.00 6.21  ? 162  ARG A NH2 1 
ATOM   1285  N  N   . ALA A  1 163 ? 7.373   11.254  11.798  1.00 6.28  ? 163  ALA A N   1 
ATOM   1286  C  CA  . ALA A  1 163 ? 7.434   11.473  10.355  1.00 5.95  ? 163  ALA A CA  1 
ATOM   1287  C  C   . ALA A  1 163 ? 7.564   12.926  9.930   1.00 5.74  ? 163  ALA A C   1 
ATOM   1288  O  O   . ALA A  1 163 ? 7.071   13.829  10.608  1.00 5.55  ? 163  ALA A O   1 
ATOM   1289  C  CB  . ALA A  1 163 ? 6.225   10.845  9.690   1.00 6.98  ? 163  ALA A CB  1 
ATOM   1290  N  N   . GLY A  1 164 ? 8.205   13.127  8.789   1.00 5.31  ? 164  GLY A N   1 
ATOM   1291  C  CA  . GLY A  1 164 ? 8.504   14.426  8.253   1.00 6.41  ? 164  GLY A CA  1 
ATOM   1292  C  C   . GLY A  1 164 ? 7.323   15.382  8.114   1.00 7.72  ? 164  GLY A C   1 
ATOM   1293  O  O   . GLY A  1 164 ? 6.225   15.020  7.709   1.00 7.58  ? 164  GLY A O   1 
ATOM   1294  N  N   . PHE A  1 165 ? 7.645   16.635  8.472   1.00 9.10  ? 165  PHE A N   1 
ATOM   1295  C  CA  . PHE A  1 165 ? 6.741   17.770  8.398   1.00 11.64 ? 165  PHE A CA  1 
ATOM   1296  C  C   . PHE A  1 165 ? 7.410   18.885  7.597   1.00 14.88 ? 165  PHE A C   1 
ATOM   1297  O  O   . PHE A  1 165 ? 8.618   19.081  7.536   1.00 15.33 ? 165  PHE A O   1 
ATOM   1298  C  CB  . PHE A  1 165 ? 6.260   18.227  9.757   1.00 11.87 ? 165  PHE A CB  1 
ATOM   1299  C  CG  . PHE A  1 165 ? 7.454   18.518  10.569  1.00 12.89 ? 165  PHE A CG  1 
ATOM   1300  C  CD1 . PHE A  1 165 ? 8.207   17.475  11.115  1.00 13.50 ? 165  PHE A CD1 1 
ATOM   1301  C  CD2 . PHE A  1 165 ? 7.868   19.832  10.758  1.00 12.24 ? 165  PHE A CD2 1 
ATOM   1302  C  CE1 . PHE A  1 165 ? 9.346   17.739  11.839  1.00 13.55 ? 165  PHE A CE1 1 
ATOM   1303  C  CE2 . PHE A  1 165 ? 9.003   20.109  11.480  1.00 12.44 ? 165  PHE A CE2 1 
ATOM   1304  C  CZ  . PHE A  1 165 ? 9.744   19.064  12.024  1.00 13.90 ? 165  PHE A CZ  1 
ATOM   1305  N  N   . VAL A  1 166 ? 6.453   19.583  6.997   1.00 17.69 ? 166  VAL A N   1 
ATOM   1306  C  CA  . VAL A  1 166 ? 6.447   20.635  5.969   1.00 21.39 ? 166  VAL A CA  1 
ATOM   1307  C  C   . VAL A  1 166 ? 7.008   21.999  5.983   1.00 26.49 ? 166  VAL A C   1 
ATOM   1308  O  O   . VAL A  1 166 ? 6.658   22.711  5.033   1.00 25.99 ? 166  VAL A O   1 
ATOM   1309  C  CB  . VAL A  1 166 ? 4.991   20.944  5.583   1.00 20.08 ? 166  VAL A CB  1 
ATOM   1310  C  CG1 . VAL A  1 166 ? 4.359   19.772  4.852   1.00 19.42 ? 166  VAL A CG1 1 
ATOM   1311  C  CG2 . VAL A  1 166 ? 4.163   21.284  6.813   1.00 21.41 ? 166  VAL A CG2 1 
ATOM   1312  N  N   . CYS A  1 167 ? 7.762   22.522  6.843   1.00 33.14 ? 167  CYS A N   1 
ATOM   1313  C  CA  . CYS A  1 167 ? 8.252   23.827  6.397   1.00 38.51 ? 167  CYS A CA  1 
ATOM   1314  C  C   . CYS A  1 167 ? 9.730   23.533  6.391   1.00 38.60 ? 167  CYS A C   1 
ATOM   1315  O  O   . CYS A  1 167 ? 10.510  23.731  5.449   1.00 39.84 ? 167  CYS A O   1 
ATOM   1316  C  CB  . CYS A  1 167 ? 7.773   24.968  7.286   1.00 45.40 ? 167  CYS A CB  1 
ATOM   1317  S  SG  . CYS A  1 167 ? 5.971   25.243  7.257   1.00 55.95 ? 167  CYS A SG  1 
ATOM   1318  N  N   . PRO A  1 168 ? 10.007  23.038  7.597   1.00 38.32 ? 168  PRO A N   1 
ATOM   1319  C  CA  . PRO A  1 168 ? 11.340  22.438  7.999   1.00 38.08 ? 168  PRO A CA  1 
ATOM   1320  C  C   . PRO A  1 168 ? 11.744  21.066  7.397   1.00 40.32 ? 168  PRO A C   1 
ATOM   1321  O  O   . PRO A  1 168 ? 11.520  20.740  6.236   1.00 38.44 ? 168  PRO A O   1 
ATOM   1322  C  CB  . PRO A  1 168 ? 11.266  22.520  9.519   1.00 37.46 ? 168  PRO A CB  1 
ATOM   1323  C  CG  . PRO A  1 168 ? 10.557  23.785  9.768   1.00 38.21 ? 168  PRO A CG  1 
ATOM   1324  C  CD  . PRO A  1 168 ? 9.738   24.132  8.571   1.00 37.81 ? 168  PRO A CD  1 
ATOM   1325  N  N   . THR A  1 169 ? 12.354  20.309  8.320   1.00 42.83 ? 169  THR A N   1 
ATOM   1326  C  CA  . THR A  1 169 ? 12.854  18.973  8.386   1.00 46.43 ? 169  THR A CA  1 
ATOM   1327  C  C   . THR A  1 169 ? 13.299  19.038  9.910   1.00 48.82 ? 169  THR A C   1 
ATOM   1328  O  O   . THR A  1 169 ? 12.741  18.353  10.770  1.00 50.45 ? 169  THR A O   1 
ATOM   1329  C  CB  . THR A  1 169 ? 13.946  18.613  7.335   1.00 48.50 ? 169  THR A CB  1 
ATOM   1330  O  OG1 . THR A  1 169 ? 14.023  19.640  6.346   1.00 50.05 ? 169  THR A OG1 1 
ATOM   1331  C  CG2 . THR A  1 169 ? 13.609  17.278  6.664   1.00 49.13 ? 169  THR A CG2 1 
ATOM   1332  N  N   . PRO A  1 170 ? 14.364  19.851  10.132  1.00 50.53 ? 170  PRO A N   1 
ATOM   1333  C  CA  . PRO A  1 170 ? 14.838  20.190  11.490  1.00 50.91 ? 170  PRO A CA  1 
ATOM   1334  C  C   . PRO A  1 170 ? 13.736  20.765  12.354  1.00 51.40 ? 170  PRO A C   1 
ATOM   1335  O  O   . PRO A  1 170 ? 12.554  20.724  12.009  1.00 50.51 ? 170  PRO A O   1 
ATOM   1336  C  CB  . PRO A  1 170 ? 16.098  20.989  11.256  1.00 50.77 ? 170  PRO A CB  1 
ATOM   1337  C  CG  . PRO A  1 170 ? 16.661  20.269  10.078  1.00 49.82 ? 170  PRO A CG  1 
ATOM   1338  C  CD  . PRO A  1 170 ? 15.544  19.596  9.328   1.00 49.53 ? 170  PRO A CD  1 
ATOM   1339  N  N   . PRO A  1 171 ? 14.180  21.346  13.475  1.00 52.57 ? 171  PRO A N   1 
ATOM   1340  C  CA  . PRO A  1 171 ? 13.314  21.878  14.635  1.00 53.34 ? 171  PRO A CA  1 
ATOM   1341  C  C   . PRO A  1 171 ? 12.204  23.043  14.868  1.00 54.05 ? 171  PRO A C   1 
ATOM   1342  O  O   . PRO A  1 171 ? 12.503  23.660  15.883  1.00 52.71 ? 171  PRO A O   1 
ATOM   1343  C  CB  . PRO A  1 171 ? 14.382  22.108  15.676  1.00 53.57 ? 171  PRO A CB  1 
ATOM   1344  C  CG  . PRO A  1 171 ? 15.354  20.998  15.485  1.00 53.20 ? 171  PRO A CG  1 
ATOM   1345  C  CD  . PRO A  1 171 ? 15.255  20.534  14.055  1.00 52.80 ? 171  PRO A CD  1 
ATOM   1346  N  N   . TYR A  1 172 ? 11.028  23.557  14.317  1.00 55.88 ? 172  TYR A N   1 
ATOM   1347  C  CA  . TYR A  1 172 ? 10.510  24.836  15.092  1.00 57.00 ? 172  TYR A CA  1 
ATOM   1348  C  C   . TYR A  1 172 ? 8.981   25.195  15.456  1.00 55.72 ? 172  TYR A C   1 
ATOM   1349  O  O   . TYR A  1 172 ? 8.489   24.718  16.478  1.00 55.54 ? 172  TYR A O   1 
ATOM   1350  C  CB  . TYR A  1 172 ? 10.759  26.179  14.367  1.00 61.89 ? 172  TYR A CB  1 
ATOM   1351  C  CG  . TYR A  1 172 ? 11.996  27.040  14.171  1.00 66.36 ? 172  TYR A CG  1 
ATOM   1352  C  CD1 . TYR A  1 172 ? 13.207  27.031  14.867  1.00 67.34 ? 172  TYR A CD1 1 
ATOM   1353  C  CD2 . TYR A  1 172 ? 11.828  27.973  13.170  1.00 67.67 ? 172  TYR A CD2 1 
ATOM   1354  C  CE1 . TYR A  1 172 ? 14.238  27.850  14.452  1.00 69.16 ? 172  TYR A CE1 1 
ATOM   1355  C  CE2 . TYR A  1 172 ? 12.861  28.806  12.757  1.00 69.14 ? 172  TYR A CE2 1 
ATOM   1356  C  CZ  . TYR A  1 172 ? 14.056  28.720  13.377  1.00 69.43 ? 172  TYR A CZ  1 
ATOM   1357  O  OH  . TYR A  1 172 ? 15.116  29.481  12.926  1.00 70.32 ? 172  TYR A OH  1 
ATOM   1358  N  N   . GLN A  1 173 ? 8.144   26.058  14.685  1.00 52.73 ? 173  GLN A N   1 
ATOM   1359  C  CA  . GLN A  1 173 ? 6.837   26.614  15.352  1.00 49.61 ? 173  GLN A CA  1 
ATOM   1360  C  C   . GLN A  1 173 ? 5.330   26.846  14.765  1.00 46.43 ? 173  GLN A C   1 
ATOM   1361  O  O   . GLN A  1 173 ? 4.762   25.990  14.088  1.00 46.00 ? 173  GLN A O   1 
ATOM   1362  C  CB  . GLN A  1 173 ? 7.313   27.950  15.922  1.00 50.11 ? 173  GLN A CB  1 
ATOM   1363  C  CG  . GLN A  1 173 ? 8.592   28.454  15.234  1.00 50.76 ? 173  GLN A CG  1 
ATOM   1364  C  CD  . GLN A  1 173 ? 9.304   29.599  15.946  1.00 51.64 ? 173  GLN A CD  1 
ATOM   1365  O  OE1 . GLN A  1 173 ? 9.595   29.525  17.146  1.00 51.82 ? 173  GLN A OE1 1 
ATOM   1366  N  NE2 . GLN A  1 173 ? 9.682   30.755  15.395  1.00 51.11 ? 173  GLN A NE2 1 
ATOM   1367  N  N   . SER A  1 174 ? 4.760   28.073  15.135  1.00 42.94 ? 174  SER A N   1 
ATOM   1368  C  CA  . SER A  1 174 ? 3.419   28.658  14.943  1.00 38.46 ? 174  SER A CA  1 
ATOM   1369  C  C   . SER A  1 174 ? 2.207   27.706  14.461  1.00 34.47 ? 174  SER A C   1 
ATOM   1370  O  O   . SER A  1 174 ? 1.209   27.750  15.180  1.00 33.16 ? 174  SER A O   1 
ATOM   1371  C  CB  . SER A  1 174 ? 3.666   29.963  14.176  1.00 39.12 ? 174  SER A CB  1 
ATOM   1372  O  OG  . SER A  1 174 ? 2.935   29.993  12.963  1.00 39.92 ? 174  SER A OG  1 
ATOM   1373  N  N   . LEU A  1 175 ? 2.172   26.879  13.359  1.00 28.92 ? 175  LEU A N   1 
ATOM   1374  C  CA  . LEU A  1 175 ? 0.898   26.192  12.957  1.00 21.71 ? 175  LEU A CA  1 
ATOM   1375  C  C   . LEU A  1 175 ? 0.751   24.641  13.078  1.00 17.66 ? 175  LEU A C   1 
ATOM   1376  O  O   . LEU A  1 175 ? 1.749   23.910  12.988  1.00 17.36 ? 175  LEU A O   1 
ATOM   1377  C  CB  . LEU A  1 175 ? 0.608   26.562  11.496  1.00 20.57 ? 175  LEU A CB  1 
ATOM   1378  C  CG  . LEU A  1 175 ? -0.877  26.620  11.092  1.00 19.97 ? 175  LEU A CG  1 
ATOM   1379  C  CD1 . LEU A  1 175 ? -1.014  27.267  9.719   1.00 18.80 ? 175  LEU A CD1 1 
ATOM   1380  C  CD2 . LEU A  1 175 ? -1.504  25.221  11.112  1.00 17.90 ? 175  LEU A CD2 1 
ATOM   1381  N  N   . ALA A  1 176 ? -0.481  24.175  13.286  1.00 12.89 ? 176  ALA A N   1 
ATOM   1382  C  CA  . ALA A  1 176 ? -0.725  22.780  13.449  1.00 8.97  ? 176  ALA A CA  1 
ATOM   1383  C  C   . ALA A  1 176 ? 0.081   22.047  12.406  1.00 6.31  ? 176  ALA A C   1 
ATOM   1384  O  O   . ALA A  1 176 ? -0.067  22.267  11.211  1.00 4.19  ? 176  ALA A O   1 
ATOM   1385  C  CB  . ALA A  1 176 ? -2.211  22.451  13.303  1.00 9.22  ? 176  ALA A CB  1 
ATOM   1386  N  N   . ARG A  1 177 ? 0.928   21.170  12.887  1.00 2.59  ? 177  ARG A N   1 
ATOM   1387  C  CA  . ARG A  1 177 ? 1.843   20.313  12.126  1.00 2.00  ? 177  ARG A CA  1 
ATOM   1388  C  C   . ARG A  1 177 ? 1.216   19.352  11.110  1.00 2.00  ? 177  ARG A C   1 
ATOM   1389  O  O   . ARG A  1 177 ? 0.226   18.678  11.423  1.00 2.41  ? 177  ARG A O   1 
ATOM   1390  C  CB  . ARG A  1 177 ? 2.659   19.502  13.143  1.00 2.78  ? 177  ARG A CB  1 
ATOM   1391  C  CG  . ARG A  1 177 ? 3.607   18.475  12.558  1.00 2.00  ? 177  ARG A CG  1 
ATOM   1392  C  CD  . ARG A  1 177 ? 5.035   18.834  12.904  1.00 2.04  ? 177  ARG A CD  1 
ATOM   1393  N  NE  . ARG A  1 177 ? 5.801   17.769  13.535  1.00 2.18  ? 177  ARG A NE  1 
ATOM   1394  C  CZ  . ARG A  1 177 ? 7.000   17.951  14.083  1.00 4.00  ? 177  ARG A CZ  1 
ATOM   1395  N  NH1 . ARG A  1 177 ? 7.560   19.158  14.075  1.00 3.44  ? 177  ARG A NH1 1 
ATOM   1396  N  NH2 . ARG A  1 177 ? 7.642   16.932  14.640  1.00 4.80  ? 177  ARG A NH2 1 
ATOM   1397  N  N   . ASP A  1 178 ? 1.782   19.306  9.903   1.00 2.00  ? 178  ASP A N   1 
ATOM   1398  C  CA  . ASP A  1 178 ? 1.293   18.406  8.848   1.00 2.61  ? 178  ASP A CA  1 
ATOM   1399  C  C   . ASP A  1 178 ? 2.442   17.606  8.191   1.00 2.92  ? 178  ASP A C   1 
ATOM   1400  O  O   . ASP A  1 178 ? 3.553   18.122  8.012   1.00 2.11  ? 178  ASP A O   1 
ATOM   1401  C  CB  . ASP A  1 178 ? 0.499   19.225  7.809   1.00 2.75  ? 178  ASP A CB  1 
ATOM   1402  C  CG  . ASP A  1 178 ? -0.919  19.573  8.247   1.00 4.23  ? 178  ASP A CG  1 
ATOM   1403  O  OD1 . ASP A  1 178 ? -1.627  18.681  8.766   1.00 2.27  ? 178  ASP A OD1 1 
ATOM   1404  O  OD2 . ASP A  1 178 ? -1.327  20.752  8.057   1.00 2.35  ? 178  ASP A OD2 1 
ATOM   1405  N  N   . GLN A  1 179 ? 2.174   16.344  7.848   1.00 2.00  ? 179  GLN A N   1 
ATOM   1406  C  CA  . GLN A  1 179 ? 3.186   15.487  7.236   1.00 2.00  ? 179  GLN A CA  1 
ATOM   1407  C  C   . GLN A  1 179 ? 3.174   15.495  5.709   1.00 2.93  ? 179  GLN A C   1 
ATOM   1408  O  O   . GLN A  1 179 ? 2.139   15.743  5.072   1.00 3.54  ? 179  GLN A O   1 
ATOM   1409  C  CB  . GLN A  1 179 ? 3.035   14.047  7.747   1.00 2.09  ? 179  GLN A CB  1 
ATOM   1410  C  CG  . GLN A  1 179 ? 3.418   13.899  9.224   1.00 2.62  ? 179  GLN A CG  1 
ATOM   1411  C  CD  . GLN A  1 179 ? 2.315   14.349  10.157  1.00 3.15  ? 179  GLN A CD  1 
ATOM   1412  O  OE1 . GLN A  1 179 ? 1.306   14.876  9.712   1.00 4.28  ? 179  GLN A OE1 1 
ATOM   1413  N  NE2 . GLN A  1 179 ? 2.291   14.236  11.490  1.00 4.59  ? 179  GLN A NE2 1 
ATOM   1414  N  N   . ILE A  1 180 ? 4.346   15.229  5.137   1.00 2.16  ? 180  ILE A N   1 
ATOM   1415  C  CA  . ILE A  1 180 ? 4.542   15.288  3.703   1.00 2.14  ? 180  ILE A CA  1 
ATOM   1416  C  C   . ILE A  1 180 ? 4.276   14.003  2.942   1.00 2.26  ? 180  ILE A C   1 
ATOM   1417  O  O   . ILE A  1 180 ? 4.648   12.926  3.406   1.00 5.05  ? 180  ILE A O   1 
ATOM   1418  C  CB  . ILE A  1 180 ? 5.984   15.686  3.408   1.00 2.31  ? 180  ILE A CB  1 
ATOM   1419  C  CG1 . ILE A  1 180 ? 6.353   16.896  4.258   1.00 2.00  ? 180  ILE A CG1 1 
ATOM   1420  C  CG2 . ILE A  1 180 ? 6.167   15.993  1.918   1.00 4.16  ? 180  ILE A CG2 1 
ATOM   1421  C  CD1 . ILE A  1 180 ? 7.750   17.422  4.019   1.00 2.00  ? 180  ILE A CD1 1 
ATOM   1422  N  N   . ASN A  1 181 ? 3.642   14.128  1.796   1.00 2.02  ? 181  ASN A N   1 
ATOM   1423  C  CA  . ASN A  1 181 ? 3.438   13.015  0.889   1.00 2.00  ? 181  ASN A CA  1 
ATOM   1424  C  C   . ASN A  1 181 ? 4.499   13.192  -0.185  1.00 2.00  ? 181  ASN A C   1 
ATOM   1425  O  O   . ASN A  1 181 ? 4.465   14.148  -0.963  1.00 2.00  ? 181  ASN A O   1 
ATOM   1426  C  CB  . ASN A  1 181 ? 2.048   13.040  0.250   1.00 2.00  ? 181  ASN A CB  1 
ATOM   1427  C  CG  . ASN A  1 181 ? 1.714   11.788  -0.553  1.00 2.00  ? 181  ASN A CG  1 
ATOM   1428  O  OD1 . ASN A  1 181 ? 2.476   10.828  -0.575  1.00 2.39  ? 181  ASN A OD1 1 
ATOM   1429  N  ND2 . ASN A  1 181 ? 0.561   11.796  -1.208  1.00 2.00  ? 181  ASN A ND2 1 
ATOM   1430  N  N   . SER A  1 182 ? 5.443   12.265  -0.254  1.00 2.33  ? 182  SER A N   1 
ATOM   1431  C  CA  . SER A  1 182 ? 6.502   12.332  -1.238  1.00 2.27  ? 182  SER A CA  1 
ATOM   1432  C  C   . SER A  1 182 ? 6.206   11.624  -2.572  1.00 2.00  ? 182  SER A C   1 
ATOM   1433  O  O   . SER A  1 182 ? 7.139   11.384  -3.346  1.00 2.00  ? 182  SER A O   1 
ATOM   1434  C  CB  . SER A  1 182 ? 7.798   11.789  -0.627  1.00 3.69  ? 182  SER A CB  1 
ATOM   1435  O  OG  . SER A  1 182 ? 7.657   10.425  -0.266  1.00 5.34  ? 182  SER A OG  1 
ATOM   1436  N  N   . VAL A  1 183 ? 4.943   11.305  -2.832  1.00 2.00  ? 183  VAL A N   1 
ATOM   1437  C  CA  . VAL A  1 183 ? 4.569   10.610  -4.052  1.00 2.00  ? 183  VAL A CA  1 
ATOM   1438  C  C   . VAL A  1 183 ? 3.324   11.300  -4.655  1.00 3.70  ? 183  VAL A C   1 
ATOM   1439  O  O   . VAL A  1 183 ? 2.535   11.900  -3.916  1.00 3.84  ? 183  VAL A O   1 
ATOM   1440  C  CB  . VAL A  1 183 ? 4.271   9.126   -3.798  1.00 2.00  ? 183  VAL A CB  1 
ATOM   1441  C  CG1 . VAL A  1 183 ? 5.378   8.498   -2.955  1.00 2.00  ? 183  VAL A CG1 1 
ATOM   1442  C  CG2 . VAL A  1 183 ? 2.926   8.971   -3.118  1.00 2.14  ? 183  VAL A CG2 1 
ATOM   1443  N  N   . THR A  1 184 ? 3.147   11.230  -5.968  1.00 3.02  ? 184  THR A N   1 
ATOM   1444  C  CA  . THR A  1 184 ? 1.999   11.873  -6.584  1.00 2.50  ? 184  THR A CA  1 
ATOM   1445  C  C   . THR A  1 184 ? 0.702   11.219  -6.146  1.00 2.05  ? 184  THR A C   1 
ATOM   1446  O  O   . THR A  1 184 ? 0.600   10.001  -6.106  1.00 2.00  ? 184  THR A O   1 
ATOM   1447  C  CB  . THR A  1 184 ? 2.092   11.833  -8.113  1.00 3.67  ? 184  THR A CB  1 
ATOM   1448  O  OG1 . THR A  1 184 ? 2.097   10.478  -8.561  1.00 2.98  ? 184  THR A OG1 1 
ATOM   1449  C  CG2 . THR A  1 184 ? 3.352   12.537  -8.579  1.00 4.10  ? 184  THR A CG2 1 
ATOM   1450  N  N   . SER A  1 185 ? -0.286  12.051  -5.858  1.00 2.75  ? 185  SER A N   1 
ATOM   1451  C  CA  . SER A  1 185 ? -1.594  11.594  -5.367  1.00 2.28  ? 185  SER A CA  1 
ATOM   1452  C  C   . SER A  1 185 ? -2.512  10.917  -6.377  1.00 2.93  ? 185  SER A C   1 
ATOM   1453  O  O   . SER A  1 185 ? -3.513  10.328  -5.985  1.00 3.28  ? 185  SER A O   1 
ATOM   1454  C  CB  . SER A  1 185 ? -2.350  12.757  -4.745  1.00 2.31  ? 185  SER A CB  1 
ATOM   1455  O  OG  . SER A  1 185 ? -1.732  13.167  -3.539  1.00 5.58  ? 185  SER A OG  1 
ATOM   1456  N  N   . PHE A  1 186 ? -2.194  10.997  -7.663  1.00 2.04  ? 186  PHE A N   1 
ATOM   1457  C  CA  . PHE A  1 186 ? -3.033  10.373  -8.684  1.00 2.00  ? 186  PHE A CA  1 
ATOM   1458  C  C   . PHE A  1 186 ? -2.600  8.937   -8.942  1.00 2.00  ? 186  PHE A C   1 
ATOM   1459  O  O   . PHE A  1 186 ? -1.441  8.613   -8.757  1.00 2.15  ? 186  PHE A O   1 
ATOM   1460  C  CB  . PHE A  1 186 ? -2.915  11.157  -9.983  1.00 2.45  ? 186  PHE A CB  1 
ATOM   1461  C  CG  . PHE A  1 186 ? -3.165  12.616  -9.826  1.00 2.00  ? 186  PHE A CG  1 
ATOM   1462  C  CD1 . PHE A  1 186 ? -4.461  13.115  -9.826  1.00 2.04  ? 186  PHE A CD1 1 
ATOM   1463  C  CD2 . PHE A  1 186 ? -2.108  13.492  -9.662  1.00 2.00  ? 186  PHE A CD2 1 
ATOM   1464  C  CE1 . PHE A  1 186 ? -4.699  14.471  -9.663  1.00 2.00  ? 186  PHE A CE1 1 
ATOM   1465  C  CE2 . PHE A  1 186 ? -2.333  14.845  -9.499  1.00 3.09  ? 186  PHE A CE2 1 
ATOM   1466  C  CZ  . PHE A  1 186 ? -3.634  15.339  -9.499  1.00 2.34  ? 186  PHE A CZ  1 
ATOM   1467  N  N   . LEU A  1 187 ? -3.518  8.077   -9.376  1.00 2.00  ? 187  LEU A N   1 
ATOM   1468  C  CA  . LEU A  1 187 ? -3.158  6.687   -9.676  1.00 2.24  ? 187  LEU A CA  1 
ATOM   1469  C  C   . LEU A  1 187 ? -2.475  6.658   -11.044 1.00 2.00  ? 187  LEU A C   1 
ATOM   1470  O  O   . LEU A  1 187 ? -3.083  6.271   -12.041 1.00 2.00  ? 187  LEU A O   1 
ATOM   1471  C  CB  . LEU A  1 187 ? -4.404  5.797   -9.710  1.00 2.40  ? 187  LEU A CB  1 
ATOM   1472  C  CG  . LEU A  1 187 ? -4.363  4.546   -8.826  1.00 2.17  ? 187  LEU A CG  1 
ATOM   1473  C  CD1 . LEU A  1 187 ? -5.533  3.626   -9.157  1.00 2.84  ? 187  LEU A CD1 1 
ATOM   1474  C  CD2 . LEU A  1 187 ? -3.053  3.822   -9.048  1.00 3.55  ? 187  LEU A CD2 1 
ATOM   1475  N  N   . ASP A  1 188 ? -1.202  7.044   -11.074 1.00 2.00  ? 188  ASP A N   1 
ATOM   1476  C  CA  . ASP A  1 188 ? -0.450  7.125   -12.320 1.00 2.00  ? 188  ASP A CA  1 
ATOM   1477  C  C   . ASP A  1 188 ? 0.794   6.244   -12.448 1.00 2.00  ? 188  ASP A C   1 
ATOM   1478  O  O   . ASP A  1 188 ? 1.712   6.591   -13.189 1.00 2.06  ? 188  ASP A O   1 
ATOM   1479  C  CB  . ASP A  1 188 ? -0.054  8.597   -12.529 1.00 2.00  ? 188  ASP A CB  1 
ATOM   1480  C  CG  . ASP A  1 188 ? 0.648   9.190   -11.327 1.00 2.00  ? 188  ASP A CG  1 
ATOM   1481  O  OD1 . ASP A  1 188 ? 0.929   8.439   -10.371 1.00 2.00  ? 188  ASP A OD1 1 
ATOM   1482  O  OD2 . ASP A  1 188 ? 0.901   10.416  -11.334 1.00 2.22  ? 188  ASP A OD2 1 
ATOM   1483  N  N   . ALA A  1 189 ? 0.836   5.125   -11.733 1.00 2.77  ? 189  ALA A N   1 
ATOM   1484  C  CA  . ALA A  1 189 ? 1.979   4.209   -11.793 1.00 2.00  ? 189  ALA A CA  1 
ATOM   1485  C  C   . ALA A  1 189 ? 3.299   4.925   -11.683 1.00 2.00  ? 189  ALA A C   1 
ATOM   1486  O  O   . ALA A  1 189 ? 4.116   4.874   -12.584 1.00 2.00  ? 189  ALA A O   1 
ATOM   1487  C  CB  . ALA A  1 189 ? 1.947   3.404   -13.078 1.00 2.00  ? 189  ALA A CB  1 
ATOM   1488  N  N   . SER A  1 190 ? 3.500   5.554   -10.563 1.00 2.00  ? 190  SER A N   1 
ATOM   1489  C  CA  . SER A  1 190 ? 4.736   6.288   -10.337 1.00 2.21  ? 190  SER A CA  1 
ATOM   1490  C  C   . SER A  1 190 ? 5.596   5.602   -9.315  1.00 2.00  ? 190  SER A C   1 
ATOM   1491  O  O   . SER A  1 190 ? 6.639   6.109   -8.906  1.00 2.00  ? 190  SER A O   1 
ATOM   1492  C  CB  . SER A  1 190 ? 4.407   7.733   -9.920  1.00 2.89  ? 190  SER A CB  1 
ATOM   1493  O  OG  . SER A  1 190 ? 3.689   7.757   -8.693  1.00 3.43  ? 190  SER A OG  1 
ATOM   1494  N  N   . LEU A  1 191 ? 5.156   4.405   -8.934  1.00 2.70  ? 191  LEU A N   1 
ATOM   1495  C  CA  . LEU A  1 191 ? 5.950   3.536   -8.111  1.00 2.35  ? 191  LEU A CA  1 
ATOM   1496  C  C   . LEU A  1 191 ? 6.974   2.963   -9.089  1.00 3.05  ? 191  LEU A C   1 
ATOM   1497  O  O   . LEU A  1 191 ? 8.013   2.436   -8.689  1.00 2.27  ? 191  LEU A O   1 
ATOM   1498  C  CB  . LEU A  1 191 ? 5.119   2.404   -7.466  1.00 2.00  ? 191  LEU A CB  1 
ATOM   1499  C  CG  . LEU A  1 191 ? 4.418   1.375   -8.396  1.00 2.00  ? 191  LEU A CG  1 
ATOM   1500  C  CD1 . LEU A  1 191 ? 3.884   0.199   -7.601  1.00 2.00  ? 191  LEU A CD1 1 
ATOM   1501  C  CD2 . LEU A  1 191 ? 3.285   2.048   -9.165  1.00 2.00  ? 191  LEU A CD2 1 
ATOM   1502  N  N   . VAL A  1 192 ? 6.663   3.088   -10.379 1.00 3.37  ? 192  VAL A N   1 
ATOM   1503  C  CA  . VAL A  1 192 ? 7.519   2.596   -11.447 1.00 2.38  ? 192  VAL A CA  1 
ATOM   1504  C  C   . VAL A  1 192 ? 8.408   3.686   -12.016 1.00 3.89  ? 192  VAL A C   1 
ATOM   1505  O  O   . VAL A  1 192 ? 9.629   3.573   -11.967 1.00 7.01  ? 192  VAL A O   1 
ATOM   1506  C  CB  . VAL A  1 192 ? 6.700   2.028   -12.610 1.00 2.00  ? 192  VAL A CB  1 
ATOM   1507  C  CG1 . VAL A  1 192 ? 7.602   1.768   -13.797 1.00 2.00  ? 192  VAL A CG1 1 
ATOM   1508  C  CG2 . VAL A  1 192 ? 6.011   0.748   -12.183 1.00 2.00  ? 192  VAL A CG2 1 
ATOM   1509  N  N   . TYR A  1 193 ? 7.798   4.742   -12.549 1.00 2.88  ? 193  TYR A N   1 
ATOM   1510  C  CA  . TYR A  1 193 ? 8.546   5.836   -13.167 1.00 2.00  ? 193  TYR A CA  1 
ATOM   1511  C  C   . TYR A  1 193 ? 9.174   6.852   -12.224 1.00 2.00  ? 193  TYR A C   1 
ATOM   1512  O  O   . TYR A  1 193 ? 9.936   7.710   -12.662 1.00 2.00  ? 193  TYR A O   1 
ATOM   1513  C  CB  . TYR A  1 193 ? 7.640   6.535   -14.174 1.00 2.00  ? 193  TYR A CB  1 
ATOM   1514  C  CG  . TYR A  1 193 ? 7.103   5.546   -15.156 1.00 2.00  ? 193  TYR A CG  1 
ATOM   1515  C  CD1 . TYR A  1 193 ? 7.925   5.014   -16.144 1.00 2.07  ? 193  TYR A CD1 1 
ATOM   1516  C  CD2 . TYR A  1 193 ? 5.813   5.040   -15.026 1.00 2.08  ? 193  TYR A CD2 1 
ATOM   1517  C  CE1 . TYR A  1 193 ? 7.479   3.996   -16.976 1.00 2.70  ? 193  TYR A CE1 1 
ATOM   1518  C  CE2 . TYR A  1 193 ? 5.353   4.023   -15.849 1.00 2.00  ? 193  TYR A CE2 1 
ATOM   1519  C  CZ  . TYR A  1 193 ? 6.192   3.507   -16.817 1.00 2.03  ? 193  TYR A CZ  1 
ATOM   1520  O  OH  . TYR A  1 193 ? 5.746   2.496   -17.618 1.00 3.81  ? 193  TYR A OH  1 
ATOM   1521  N  N   . GLY A  1 194 ? 8.858   6.749   -10.936 1.00 2.68  ? 194  GLY A N   1 
ATOM   1522  C  CA  . GLY A  1 194 ? 9.401   7.668   -9.945  1.00 2.61  ? 194  GLY A CA  1 
ATOM   1523  C  C   . GLY A  1 194 ? 8.644   8.980   -9.783  1.00 2.75  ? 194  GLY A C   1 
ATOM   1524  O  O   . GLY A  1 194 ? 7.761   9.304   -10.582 1.00 2.46  ? 194  GLY A O   1 
ATOM   1525  N  N   . SER A  1 195 ? 8.989   9.734   -8.738  1.00 3.98  ? 195  SER A N   1 
ATOM   1526  C  CA  . SER A  1 195 ? 8.364   11.036  -8.454  1.00 4.18  ? 195  SER A CA  1 
ATOM   1527  C  C   . SER A  1 195 ? 9.346   12.208  -8.503  1.00 4.98  ? 195  SER A C   1 
ATOM   1528  O  O   . SER A  1 195 ? 9.069   13.274  -7.964  1.00 3.22  ? 195  SER A O   1 
ATOM   1529  C  CB  . SER A  1 195 ? 7.708   11.037  -7.072  1.00 3.11  ? 195  SER A CB  1 
ATOM   1530  O  OG  . SER A  1 195 ? 6.448   10.395  -7.082  1.00 5.87  ? 195  SER A OG  1 
ATOM   1531  N  N   . GLU A  1 196 ? 10.494  12.022  -9.137  1.00 7.78  ? 196  GLU A N   1 
ATOM   1532  C  CA  . GLU A  1 196 ? 11.468  13.105  -9.206  1.00 10.03 ? 196  GLU A CA  1 
ATOM   1533  C  C   . GLU A  1 196 ? 12.062  13.233  -10.593 1.00 8.65  ? 196  GLU A C   1 
ATOM   1534  O  O   . GLU A  1 196 ? 12.516  12.249  -11.175 1.00 8.04  ? 196  GLU A O   1 
ATOM   1535  C  CB  . GLU A  1 196 ? 12.608  12.871  -8.218  1.00 15.53 ? 196  GLU A CB  1 
ATOM   1536  C  CG  . GLU A  1 196 ? 12.191  12.662  -6.770  1.00 21.71 ? 196  GLU A CG  1 
ATOM   1537  C  CD  . GLU A  1 196 ? 13.383  12.287  -5.897  1.00 24.30 ? 196  GLU A CD  1 
ATOM   1538  O  OE1 . GLU A  1 196 ? 14.426  12.975  -6.000  1.00 26.36 ? 196  GLU A OE1 1 
ATOM   1539  O  OE2 . GLU A  1 196 ? 13.281  11.311  -5.115  1.00 26.34 ? 196  GLU A OE2 1 
ATOM   1540  N  N   . PRO A  1 197 ? 12.161  14.461  -11.064 1.00 7.40  ? 197  PRO A N   1 
ATOM   1541  C  CA  . PRO A  1 197 ? 12.742  14.704  -12.396 1.00 6.72  ? 197  PRO A CA  1 
ATOM   1542  C  C   . PRO A  1 197 ? 14.000  13.921  -12.625 1.00 5.63  ? 197  PRO A C   1 
ATOM   1543  O  O   . PRO A  1 197 ? 14.132  13.168  -13.594 1.00 6.23  ? 197  PRO A O   1 
ATOM   1544  C  CB  . PRO A  1 197 ? 12.756  16.212  -12.492 1.00 7.36  ? 197  PRO A CB  1 
ATOM   1545  C  CG  . PRO A  1 197 ? 11.450  16.529  -11.845 1.00 6.66  ? 197  PRO A CG  1 
ATOM   1546  C  CD  . PRO A  1 197 ? 11.104  15.450  -10.861 1.00 6.87  ? 197  PRO A CD  1 
ATOM   1547  N  N   . SER A  1 198 ? 14.910  14.106  -11.693 1.00 4.47  ? 198  SER A N   1 
ATOM   1548  C  CA  . SER A  1 198 ? 16.229  13.499  -11.651 1.00 5.31  ? 198  SER A CA  1 
ATOM   1549  C  C   . SER A  1 198 ? 16.291  11.972  -11.509 1.00 5.71  ? 198  SER A C   1 
ATOM   1550  O  O   . SER A  1 198 ? 17.134  11.335  -12.157 1.00 6.02  ? 198  SER A O   1 
ATOM   1551  C  CB  . SER A  1 198 ? 16.999  14.115  -10.494 1.00 6.91  ? 198  SER A CB  1 
ATOM   1552  O  OG  . SER A  1 198 ? 16.264  14.015  -9.281  1.00 11.41 ? 198  SER A OG  1 
ATOM   1553  N  N   . LEU A  1 199 ? 15.468  11.388  -10.667 1.00 4.44  ? 199  LEU A N   1 
ATOM   1554  C  CA  . LEU A  1 199 ? 15.459  9.951   -10.560 1.00 3.70  ? 199  LEU A CA  1 
ATOM   1555  C  C   . LEU A  1 199 ? 14.736  9.422   -11.761 1.00 3.24  ? 199  LEU A C   1 
ATOM   1556  O  O   . LEU A  1 199 ? 15.179  8.493   -12.423 1.00 3.66  ? 199  LEU A O   1 
ATOM   1557  C  CB  . LEU A  1 199 ? 14.771  9.504   -9.274  1.00 3.19  ? 199  LEU A CB  1 
ATOM   1558  C  CG  . LEU A  1 199 ? 14.263  8.086   -9.244  1.00 2.37  ? 199  LEU A CG  1 
ATOM   1559  C  CD1 . LEU A  1 199 ? 15.316  7.105   -9.742  1.00 3.00  ? 199  LEU A CD1 1 
ATOM   1560  C  CD2 . LEU A  1 199 ? 13.810  7.701   -7.839  1.00 2.39  ? 199  LEU A CD2 1 
ATOM   1561  N  N   . ALA A  1 200 ? 13.597  10.038  -12.038 1.00 3.60  ? 200  ALA A N   1 
ATOM   1562  C  CA  . ALA A  1 200 ? 12.754  9.641   -13.150 1.00 4.95  ? 200  ALA A CA  1 
ATOM   1563  C  C   . ALA A  1 200 ? 13.583  9.302   -14.406 1.00 6.08  ? 200  ALA A C   1 
ATOM   1564  O  O   . ALA A  1 200 ? 13.266  8.367   -15.143 1.00 6.95  ? 200  ALA A O   1 
ATOM   1565  C  CB  . ALA A  1 200 ? 11.748  10.742  -13.476 1.00 5.24  ? 200  ALA A CB  1 
ATOM   1566  N  N   . SER A  1 201 ? 14.650  10.106  -14.645 1.00 7.63  ? 201  SER A N   1 
ATOM   1567  C  CA  . SER A  1 201 ? 15.534  9.945   -15.822 1.00 8.14  ? 201  SER A CA  1 
ATOM   1568  C  C   . SER A  1 201 ? 16.498  8.745   -15.685 1.00 9.67  ? 201  SER A C   1 
ATOM   1569  O  O   . SER A  1 201 ? 16.549  7.886   -16.556 1.00 10.28 ? 201  SER A O   1 
ATOM   1570  C  CB  . SER A  1 201 ? 16.296  11.237  -16.097 1.00 7.83  ? 201  SER A CB  1 
ATOM   1571  O  OG  . SER A  1 201 ? 17.457  11.316  -15.291 1.00 6.62  ? 201  SER A OG  1 
ATOM   1572  N  N   . ARG A  1 202 ? 17.246  8.738   -14.580 1.00 10.69 ? 202  ARG A N   1 
ATOM   1573  C  CA  . ARG A  1 202 ? 18.251  7.727   -14.215 1.00 11.56 ? 202  ARG A CA  1 
ATOM   1574  C  C   . ARG A  1 202 ? 17.661  6.288   -14.261 1.00 9.03  ? 202  ARG A C   1 
ATOM   1575  O  O   . ARG A  1 202 ? 18.369  5.301   -14.496 1.00 9.13  ? 202  ARG A O   1 
ATOM   1576  C  CB  . ARG A  1 202 ? 18.851  8.105   -12.841 1.00 15.18 ? 202  ARG A CB  1 
ATOM   1577  C  CG  . ARG A  1 202 ? 19.331  6.951   -11.980 1.00 22.31 ? 202  ARG A CG  1 
ATOM   1578  C  CD  . ARG A  1 202 ? 20.467  7.400   -11.066 1.00 26.93 ? 202  ARG A CD  1 
ATOM   1579  N  NE  . ARG A  1 202 ? 20.234  7.073   -9.659  1.00 31.34 ? 202  ARG A NE  1 
ATOM   1580  C  CZ  . ARG A  1 202 ? 20.586  5.931   -9.069  1.00 33.37 ? 202  ARG A CZ  1 
ATOM   1581  N  NH1 . ARG A  1 202 ? 21.204  4.970   -9.752  1.00 34.70 ? 202  ARG A NH1 1 
ATOM   1582  N  NH2 . ARG A  1 202 ? 20.309  5.745   -7.784  1.00 34.57 ? 202  ARG A NH2 1 
ATOM   1583  N  N   . LEU A  1 203 ? 16.363  6.207   -14.012 1.00 7.00  ? 203  LEU A N   1 
ATOM   1584  C  CA  . LEU A  1 203 ? 15.648  4.945   -13.990 1.00 6.87  ? 203  LEU A CA  1 
ATOM   1585  C  C   . LEU A  1 203 ? 15.414  4.350   -15.371 1.00 7.56  ? 203  LEU A C   1 
ATOM   1586  O  O   . LEU A  1 203 ? 14.956  3.224   -15.499 1.00 7.25  ? 203  LEU A O   1 
ATOM   1587  C  CB  . LEU A  1 203 ? 14.327  5.182   -13.263 1.00 5.57  ? 203  LEU A CB  1 
ATOM   1588  C  CG  . LEU A  1 203 ? 13.824  4.183   -12.220 1.00 4.40  ? 203  LEU A CG  1 
ATOM   1589  C  CD1 . LEU A  1 203 ? 14.979  3.535   -11.489 1.00 4.14  ? 203  LEU A CD1 1 
ATOM   1590  C  CD2 . LEU A  1 203 ? 12.877  4.857   -11.251 1.00 3.13  ? 203  LEU A CD2 1 
ATOM   1591  N  N   . ARG A  1 204 ? 15.730  5.147   -16.392 1.00 7.92  ? 204  ARG A N   1 
ATOM   1592  C  CA  . ARG A  1 204 ? 15.571  4.774   -17.799 1.00 9.34  ? 204  ARG A CA  1 
ATOM   1593  C  C   . ARG A  1 204 ? 16.896  4.499   -18.517 1.00 11.03 ? 204  ARG A C   1 
ATOM   1594  O  O   . ARG A  1 204 ? 17.959  5.018   -18.136 1.00 9.15  ? 204  ARG A O   1 
ATOM   1595  C  CB  . ARG A  1 204 ? 14.871  5.905   -18.558 1.00 9.54  ? 204  ARG A CB  1 
ATOM   1596  C  CG  . ARG A  1 204 ? 13.737  6.576   -17.800 1.00 10.91 ? 204  ARG A CG  1 
ATOM   1597  C  CD  . ARG A  1 204 ? 13.350  7.939   -18.409 1.00 11.59 ? 204  ARG A CD  1 
ATOM   1598  N  NE  . ARG A  1 204 ? 13.383  7.952   -19.875 1.00 11.97 ? 204  ARG A NE  1 
ATOM   1599  C  CZ  . ARG A  1 204 ? 12.905  8.935   -20.635 1.00 10.99 ? 204  ARG A CZ  1 
ATOM   1600  N  NH1 . ARG A  1 204 ? 12.340  10.002  -20.089 1.00 12.67 ? 204  ARG A NH1 1 
ATOM   1601  N  NH2 . ARG A  1 204 ? 13.010  8.857   -21.951 1.00 11.35 ? 204  ARG A NH2 1 
ATOM   1602  N  N   . ASN A  1 205 ? 16.800  3.684   -19.573 1.00 12.68 ? 205  ASN A N   1 
ATOM   1603  C  CA  . ASN A  1 205 ? 17.927  3.326   -20.441 1.00 13.73 ? 205  ASN A CA  1 
ATOM   1604  C  C   . ASN A  1 205 ? 17.863  4.352   -21.578 1.00 13.18 ? 205  ASN A C   1 
ATOM   1605  O  O   . ASN A  1 205 ? 17.164  4.145   -22.581 1.00 12.60 ? 205  ASN A O   1 
ATOM   1606  C  CB  . ASN A  1 205 ? 17.752  1.895   -20.993 1.00 18.19 ? 205  ASN A CB  1 
ATOM   1607  C  CG  . ASN A  1 205 ? 18.871  1.471   -21.949 1.00 22.34 ? 205  ASN A CG  1 
ATOM   1608  O  OD1 . ASN A  1 205 ? 19.690  2.287   -22.353 1.00 21.02 ? 205  ASN A OD1 1 
ATOM   1609  N  ND2 . ASN A  1 205 ? 18.868  0.192   -22.317 1.00 28.02 ? 205  ASN A ND2 1 
ATOM   1610  N  N   . LEU A  1 206 ? 18.613  5.465   -21.407 1.00 10.97 ? 206  LEU A N   1 
ATOM   1611  C  CA  . LEU A  1 206 ? 18.667  6.510   -22.400 1.00 7.65  ? 206  LEU A CA  1 
ATOM   1612  C  C   . LEU A  1 206 ? 19.785  6.235   -23.462 1.00 8.11  ? 206  LEU A C   1 
ATOM   1613  O  O   . LEU A  1 206 ? 19.940  7.007   -24.417 1.00 9.18  ? 206  LEU A O   1 
ATOM   1614  C  CB  . LEU A  1 206 ? 18.801  7.869   -21.676 1.00 5.45  ? 206  LEU A CB  1 
ATOM   1615  C  CG  . LEU A  1 206 ? 17.685  8.305   -20.682 1.00 3.11  ? 206  LEU A CG  1 
ATOM   1616  C  CD1 . LEU A  1 206 ? 18.003  9.674   -20.087 1.00 2.05  ? 206  LEU A CD1 1 
ATOM   1617  C  CD2 . LEU A  1 206 ? 16.326  8.306   -21.367 1.00 2.00  ? 206  LEU A CD2 1 
ATOM   1618  N  N   . SER A  1 207 ? 20.568  5.133   -23.244 1.00 6.55  ? 207  SER A N   1 
ATOM   1619  C  CA  . SER A  1 207 ? 21.682  4.689   -24.130 1.00 4.46  ? 207  SER A CA  1 
ATOM   1620  C  C   . SER A  1 207 ? 21.121  4.045   -25.404 1.00 5.33  ? 207  SER A C   1 
ATOM   1621  O  O   . SER A  1 207 ? 21.836  3.423   -26.178 1.00 5.09  ? 207  SER A O   1 
ATOM   1622  C  CB  . SER A  1 207 ? 22.592  3.707   -23.375 1.00 4.90  ? 207  SER A CB  1 
ATOM   1623  O  OG  . SER A  1 207 ? 22.277  3.690   -21.994 1.00 5.02  ? 207  SER A OG  1 
ATOM   1624  N  N   . SER A  1 208 ? 19.789  4.221   -25.636 1.00 6.47  ? 208  SER A N   1 
ATOM   1625  C  CA  . SER A  1 208 ? 19.040  3.657   -26.791 1.00 7.66  ? 208  SER A CA  1 
ATOM   1626  C  C   . SER A  1 208 ? 17.756  4.475   -27.148 1.00 9.29  ? 208  SER A C   1 
ATOM   1627  O  O   . SER A  1 208 ? 17.310  5.353   -26.407 1.00 12.40 ? 208  SER A O   1 
ATOM   1628  C  CB  . SER A  1 208 ? 18.705  2.194   -26.531 1.00 7.34  ? 208  SER A CB  1 
ATOM   1629  O  OG  . SER A  1 208 ? 17.310  1.969   -26.625 1.00 6.89  ? 208  SER A OG  1 
ATOM   1630  N  N   . PRO A  1 209 ? 17.239  4.227   -28.355 1.00 8.97  ? 209  PRO A N   1 
ATOM   1631  C  CA  . PRO A  1 209 ? 16.161  5.024   -29.027 1.00 8.15  ? 209  PRO A CA  1 
ATOM   1632  C  C   . PRO A  1 209 ? 14.888  4.584   -28.567 1.00 7.44  ? 209  PRO A C   1 
ATOM   1633  O  O   . PRO A  1 209 ? 13.829  5.219   -28.591 1.00 6.76  ? 209  PRO A O   1 
ATOM   1634  C  CB  . PRO A  1 209 ? 16.212  4.643   -30.472 1.00 8.44  ? 209  PRO A CB  1 
ATOM   1635  C  CG  . PRO A  1 209 ? 17.653  4.560   -30.704 1.00 8.76  ? 209  PRO A CG  1 
ATOM   1636  C  CD  . PRO A  1 209 ? 18.298  4.338   -29.368 1.00 8.84  ? 209  PRO A CD  1 
ATOM   1637  N  N   . LEU A  1 210 ? 15.097  3.376   -28.122 1.00 6.77  ? 210  LEU A N   1 
ATOM   1638  C  CA  . LEU A  1 210 ? 13.930  2.521   -27.994 1.00 6.09  ? 210  LEU A CA  1 
ATOM   1639  C  C   . LEU A  1 210 ? 12.988  2.935   -26.872 1.00 4.81  ? 210  LEU A C   1 
ATOM   1640  O  O   . LEU A  1 210 ? 11.889  2.398   -26.748 1.00 4.45  ? 210  LEU A O   1 
ATOM   1641  C  CB  . LEU A  1 210 ? 14.403  1.079   -27.826 1.00 7.93  ? 210  LEU A CB  1 
ATOM   1642  C  CG  . LEU A  1 210 ? 15.238  0.683   -29.058 1.00 10.00 ? 210  LEU A CG  1 
ATOM   1643  C  CD1 . LEU A  1 210 ? 16.372  -0.272  -28.686 1.00 9.87  ? 210  LEU A CD1 1 
ATOM   1644  C  CD2 . LEU A  1 210 ? 14.307  0.080   -30.110 1.00 10.22 ? 210  LEU A CD2 1 
ATOM   1645  N  N   . GLY A  1 211 ? 13.419  3.906   -26.070 1.00 5.03  ? 211  GLY A N   1 
ATOM   1646  C  CA  . GLY A  1 211 ? 12.604  4.394   -24.967 1.00 4.08  ? 211  GLY A CA  1 
ATOM   1647  C  C   . GLY A  1 211 ? 12.212  3.295   -24.001 1.00 3.07  ? 211  GLY A C   1 
ATOM   1648  O  O   . GLY A  1 211 ? 11.065  2.861   -23.973 1.00 2.48  ? 211  GLY A O   1 
ATOM   1649  N  N   . LEU A  1 212 ? 13.168  2.841   -23.202 1.00 2.69  ? 212  LEU A N   1 
ATOM   1650  C  CA  . LEU A  1 212 ? 12.898  1.774   -22.260 1.00 2.50  ? 212  LEU A CA  1 
ATOM   1651  C  C   . LEU A  1 212 ? 13.411  2.159   -20.884 1.00 3.75  ? 212  LEU A C   1 
ATOM   1652  O  O   . LEU A  1 212 ? 14.177  3.125   -20.746 1.00 4.96  ? 212  LEU A O   1 
ATOM   1653  C  CB  . LEU A  1 212 ? 13.607  0.487   -22.704 1.00 2.71  ? 212  LEU A CB  1 
ATOM   1654  C  CG  . LEU A  1 212 ? 13.847  0.169   -24.189 1.00 2.00  ? 212  LEU A CG  1 
ATOM   1655  C  CD1 . LEU A  1 212 ? 14.564  -1.167  -24.306 1.00 2.00  ? 212  LEU A CD1 1 
ATOM   1656  C  CD2 . LEU A  1 212 ? 12.538  0.116   -24.949 1.00 2.00  ? 212  LEU A CD2 1 
ATOM   1657  N  N   . MET A  1 213 ? 12.974  1.407   -19.871 1.00 4.08  ? 213  MET A N   1 
ATOM   1658  C  CA  . MET A  1 213 ? 13.431  1.609   -18.497 1.00 2.52  ? 213  MET A CA  1 
ATOM   1659  C  C   . MET A  1 213 ? 14.695  0.766   -18.445 1.00 2.49  ? 213  MET A C   1 
ATOM   1660  O  O   . MET A  1 213 ? 14.768  -0.292  -19.076 1.00 2.70  ? 213  MET A O   1 
ATOM   1661  C  CB  . MET A  1 213 ? 12.431  1.061   -17.474 1.00 2.42  ? 213  MET A CB  1 
ATOM   1662  C  CG  . MET A  1 213 ? 11.094  1.772   -17.410 1.00 2.00  ? 213  MET A CG  1 
ATOM   1663  S  SD  . MET A  1 213 ? 11.243  3.516   -16.991 1.00 2.00  ? 213  MET A SD  1 
ATOM   1664  C  CE  . MET A  1 213 ? 11.311  3.435   -15.239 1.00 2.00  ? 213  MET A CE  1 
ATOM   1665  N  N   . ALA A  1 214 ? 15.689  1.217   -17.699 1.00 2.00  ? 214  ALA A N   1 
ATOM   1666  C  CA  . ALA A  1 214 ? 16.939  0.480   -17.626 1.00 2.00  ? 214  ALA A CA  1 
ATOM   1667  C  C   . ALA A  1 214 ? 16.826  -0.802  -16.811 1.00 2.00  ? 214  ALA A C   1 
ATOM   1668  O  O   . ALA A  1 214 ? 16.255  -0.792  -15.724 1.00 2.40  ? 214  ALA A O   1 
ATOM   1669  C  CB  . ALA A  1 214 ? 18.014  1.376   -17.041 1.00 3.41  ? 214  ALA A CB  1 
ATOM   1670  N  N   . VAL A  1 215 ? 17.372  -1.903  -17.333 1.00 2.63  ? 215  VAL A N   1 
ATOM   1671  C  CA  . VAL A  1 215 ? 17.341  -3.180  -16.611 1.00 2.40  ? 215  VAL A CA  1 
ATOM   1672  C  C   . VAL A  1 215 ? 18.697  -3.600  -16.031 1.00 2.30  ? 215  VAL A C   1 
ATOM   1673  O  O   . VAL A  1 215 ? 19.739  -3.006  -16.313 1.00 2.00  ? 215  VAL A O   1 
ATOM   1674  C  CB  . VAL A  1 215 ? 16.829  -4.341  -17.492 1.00 2.00  ? 215  VAL A CB  1 
ATOM   1675  C  CG1 . VAL A  1 215 ? 15.551  -3.942  -18.179 1.00 2.00  ? 215  VAL A CG1 1 
ATOM   1676  C  CG2 . VAL A  1 215 ? 17.883  -4.749  -18.483 1.00 2.39  ? 215  VAL A CG2 1 
ATOM   1677  N  N   . ASN A  1 216 ? 18.663  -4.645  -15.216 1.00 3.53  ? 216  ASN A N   1 
ATOM   1678  C  CA  . ASN A  1 216 ? 19.862  -5.163  -14.570 1.00 4.58  ? 216  ASN A CA  1 
ATOM   1679  C  C   . ASN A  1 216 ? 20.773  -5.880  -15.559 1.00 4.12  ? 216  ASN A C   1 
ATOM   1680  O  O   . ASN A  1 216 ? 20.329  -6.749  -16.310 1.00 2.17  ? 216  ASN A O   1 
ATOM   1681  C  CB  . ASN A  1 216 ? 19.471  -6.113  -13.437 1.00 4.05  ? 216  ASN A CB  1 
ATOM   1682  C  CG  . ASN A  1 216 ? 20.604  -6.359  -12.474 1.00 3.98  ? 216  ASN A CG  1 
ATOM   1683  O  OD1 . ASN A  1 216 ? 21.605  -6.980  -12.823 1.00 4.40  ? 216  ASN A OD1 1 
ATOM   1684  N  ND2 . ASN A  1 216 ? 20.458  -5.861  -11.251 1.00 5.19  ? 216  ASN A ND2 1 
ATOM   1685  N  N   . GLN A  1 217 ? 22.052  -5.510  -15.542 1.00 6.08  ? 217  GLN A N   1 
ATOM   1686  C  CA  . GLN A  1 217 ? 23.041  -6.099  -16.441 1.00 6.81  ? 217  GLN A CA  1 
ATOM   1687  C  C   . GLN A  1 217 ? 23.816  -7.259  -15.831 1.00 8.82  ? 217  GLN A C   1 
ATOM   1688  O  O   . GLN A  1 217 ? 24.560  -7.934  -16.538 1.00 8.37  ? 217  GLN A O   1 
ATOM   1689  C  CB  . GLN A  1 217 ? 24.049  -5.041  -16.912 1.00 6.93  ? 217  GLN A CB  1 
ATOM   1690  C  CG  . GLN A  1 217 ? 23.460  -3.915  -17.747 1.00 4.03  ? 217  GLN A CG  1 
ATOM   1691  C  CD  . GLN A  1 217 ? 22.519  -4.427  -18.809 1.00 4.49  ? 217  GLN A CD  1 
ATOM   1692  O  OE1 . GLN A  1 217 ? 22.912  -5.200  -19.690 1.00 5.54  ? 217  GLN A OE1 1 
ATOM   1693  N  NE2 . GLN A  1 217 ? 21.260  -4.010  -18.729 1.00 3.36  ? 217  GLN A NE2 1 
ATOM   1694  N  N   . GLU A  1 218 ? 23.658  -7.488  -14.528 1.00 10.91 ? 218  GLU A N   1 
ATOM   1695  C  CA  . GLU A  1 218 ? 24.366  -8.584  -13.865 1.00 11.69 ? 218  GLU A CA  1 
ATOM   1696  C  C   . GLU A  1 218 ? 23.584  -9.884  -13.716 1.00 11.18 ? 218  GLU A C   1 
ATOM   1697  O  O   . GLU A  1 218 ? 24.180  -10.930 -13.475 1.00 12.45 ? 218  GLU A O   1 
ATOM   1698  C  CB  . GLU A  1 218 ? 24.856  -8.164  -12.475 1.00 14.49 ? 218  GLU A CB  1 
ATOM   1699  C  CG  . GLU A  1 218 ? 26.171  -7.416  -12.485 1.00 20.47 ? 218  GLU A CG  1 
ATOM   1700  C  CD  . GLU A  1 218 ? 25.994  -5.925  -12.663 1.00 23.41 ? 218  GLU A CD  1 
ATOM   1701  O  OE1 . GLU A  1 218 ? 25.680  -5.249  -11.654 1.00 24.75 ? 218  GLU A OE1 1 
ATOM   1702  O  OE2 . GLU A  1 218 ? 26.163  -5.437  -13.808 1.00 25.37 ? 218  GLU A OE2 1 
ATOM   1703  N  N   . ALA A  1 219 ? 22.264  -9.837  -13.854 1.00 10.61 ? 219  ALA A N   1 
ATOM   1704  C  CA  . ALA A  1 219 ? 21.473  -11.048 -13.693 1.00 9.82  ? 219  ALA A CA  1 
ATOM   1705  C  C   . ALA A  1 219 ? 20.162  -11.029 -14.451 1.00 10.62 ? 219  ALA A C   1 
ATOM   1706  O  O   . ALA A  1 219 ? 19.464  -10.024 -14.471 1.00 11.06 ? 219  ALA A O   1 
ATOM   1707  C  CB  . ALA A  1 219 ? 21.210  -11.284 -12.224 1.00 8.24  ? 219  ALA A CB  1 
ATOM   1708  N  N   . TRP A  1 220 ? 19.831  -12.150 -15.072 1.00 12.85 ? 220  TRP A N   1 
ATOM   1709  C  CA  . TRP A  1 220 ? 18.589  -12.256 -15.819 1.00 16.15 ? 220  TRP A CA  1 
ATOM   1710  C  C   . TRP A  1 220 ? 17.748  -13.416 -15.307 1.00 15.76 ? 220  TRP A C   1 
ATOM   1711  O  O   . TRP A  1 220 ? 18.230  -14.234 -14.523 1.00 16.13 ? 220  TRP A O   1 
ATOM   1712  C  CB  . TRP A  1 220 ? 18.884  -12.429 -17.309 1.00 23.14 ? 220  TRP A CB  1 
ATOM   1713  C  CG  . TRP A  1 220 ? 19.141  -11.125 -18.006 1.00 28.97 ? 220  TRP A CG  1 
ATOM   1714  C  CD1 . TRP A  1 220 ? 20.191  -10.269 -17.801 1.00 30.15 ? 220  TRP A CD1 1 
ATOM   1715  C  CD2 . TRP A  1 220 ? 18.272  -10.474 -18.942 1.00 30.61 ? 220  TRP A CD2 1 
ATOM   1716  N  NE1 . TRP A  1 220 ? 20.022  -9.125  -18.545 1.00 32.35 ? 220  TRP A NE1 1 
ATOM   1717  C  CE2 . TRP A  1 220 ? 18.850  -9.226  -19.256 1.00 32.40 ? 220  TRP A CE2 1 
ATOM   1718  C  CE3 . TRP A  1 220 ? 17.051  -10.826 -19.542 1.00 31.87 ? 220  TRP A CE3 1 
ATOM   1719  C  CZ2 . TRP A  1 220 ? 18.253  -8.320  -20.149 1.00 32.94 ? 220  TRP A CZ2 1 
ATOM   1720  C  CZ3 . TRP A  1 220 ? 16.455  -9.925  -20.427 1.00 33.03 ? 220  TRP A CZ3 1 
ATOM   1721  C  CH2 . TRP A  1 220 ? 17.059  -8.689  -20.722 1.00 32.46 ? 220  TRP A CH2 1 
ATOM   1722  N  N   . ASP A  1 221 ? 16.490  -13.485 -15.734 1.00 13.70 ? 221  ASP A N   1 
ATOM   1723  C  CA  . ASP A  1 221 ? 15.614  -14.562 -15.295 1.00 12.58 ? 221  ASP A CA  1 
ATOM   1724  C  C   . ASP A  1 221 ? 15.028  -15.293 -16.493 1.00 12.41 ? 221  ASP A C   1 
ATOM   1725  O  O   . ASP A  1 221 ? 14.009  -14.893 -17.055 1.00 10.73 ? 221  ASP A O   1 
ATOM   1726  C  CB  . ASP A  1 221 ? 14.503  -14.012 -14.395 1.00 12.93 ? 221  ASP A CB  1 
ATOM   1727  C  CG  . ASP A  1 221 ? 13.421  -15.038 -14.116 1.00 14.94 ? 221  ASP A CG  1 
ATOM   1728  O  OD1 . ASP A  1 221 ? 13.738  -16.250 -14.164 1.00 14.90 ? 221  ASP A OD1 1 
ATOM   1729  O  OD2 . ASP A  1 221 ? 12.264  -14.636 -13.839 1.00 15.01 ? 221  ASP A OD2 1 
ATOM   1730  N  N   . HIS A  1 222 ? 15.697  -16.380 -16.866 1.00 13.33 ? 222  HIS A N   1 
ATOM   1731  C  CA  . HIS A  1 222 ? 15.303  -17.201 -18.001 1.00 12.88 ? 222  HIS A CA  1 
ATOM   1732  C  C   . HIS A  1 222 ? 15.078  -16.295 -19.199 1.00 10.90 ? 222  HIS A C   1 
ATOM   1733  O  O   . HIS A  1 222 ? 14.008  -16.283 -19.804 1.00 9.85  ? 222  HIS A O   1 
ATOM   1734  C  CB  . HIS A  1 222 ? 14.038  -18.010 -17.674 1.00 17.95 ? 222  HIS A CB  1 
ATOM   1735  C  CG  . HIS A  1 222 ? 14.269  -19.116 -16.685 1.00 21.80 ? 222  HIS A CG  1 
ATOM   1736  N  ND1 . HIS A  1 222 ? 13.624  -19.181 -15.468 1.00 22.82 ? 222  HIS A ND1 1 
ATOM   1737  C  CD2 . HIS A  1 222 ? 15.095  -20.192 -16.725 1.00 23.12 ? 222  HIS A CD2 1 
ATOM   1738  C  CE1 . HIS A  1 222 ? 14.041  -20.242 -14.801 1.00 23.90 ? 222  HIS A CE1 1 
ATOM   1739  N  NE2 . HIS A  1 222 ? 14.937  -20.873 -15.544 1.00 24.03 ? 222  HIS A NE2 1 
ATOM   1740  N  N   . GLY A  1 223 ? 16.114  -15.527 -19.522 1.00 10.03 ? 223  GLY A N   1 
ATOM   1741  C  CA  . GLY A  1 223 ? 16.062  -14.607 -20.648 1.00 9.37  ? 223  GLY A CA  1 
ATOM   1742  C  C   . GLY A  1 223 ? 15.063  -13.482 -20.459 1.00 8.19  ? 223  GLY A C   1 
ATOM   1743  O  O   . GLY A  1 223 ? 14.473  -12.992 -21.428 1.00 9.14  ? 223  GLY A O   1 
ATOM   1744  N  N   . LEU A  1 224 ? 14.881  -13.064 -19.208 1.00 6.85  ? 224  LEU A N   1 
ATOM   1745  C  CA  . LEU A  1 224 ? 13.935  -12.008 -18.888 1.00 4.74  ? 224  LEU A CA  1 
ATOM   1746  C  C   . LEU A  1 224 ? 14.509  -10.992 -17.937 1.00 3.18  ? 224  LEU A C   1 
ATOM   1747  O  O   . LEU A  1 224 ? 15.439  -11.284 -17.190 1.00 3.06  ? 224  LEU A O   1 
ATOM   1748  C  CB  . LEU A  1 224 ? 12.660  -12.612 -18.312 1.00 2.81  ? 224  LEU A CB  1 
ATOM   1749  C  CG  . LEU A  1 224 ? 11.805  -13.182 -19.435 1.00 2.00  ? 224  LEU A CG  1 
ATOM   1750  C  CD1 . LEU A  1 224 ? 10.723  -14.077 -18.910 1.00 2.00  ? 224  LEU A CD1 1 
ATOM   1751  C  CD2 . LEU A  1 224 ? 11.223  -12.029 -20.199 1.00 2.00  ? 224  LEU A CD2 1 
ATOM   1752  N  N   . ALA A  1 225 ? 13.924  -9.799  -17.981 1.00 3.96  ? 225  ALA A N   1 
ATOM   1753  C  CA  . ALA A  1 225 ? 14.343  -8.650  -17.184 1.00 3.35  ? 225  ALA A CA  1 
ATOM   1754  C  C   . ALA A  1 225 ? 14.147  -8.698  -15.679 1.00 2.00  ? 225  ALA A C   1 
ATOM   1755  O  O   . ALA A  1 225 ? 13.291  -9.403  -15.157 1.00 2.00  ? 225  ALA A O   1 
ATOM   1756  C  CB  . ALA A  1 225 ? 13.676  -7.390  -17.731 1.00 3.93  ? 225  ALA A CB  1 
ATOM   1757  N  N   . TYR A  1 226 ? 14.961  -7.895  -15.008 1.00 2.00  ? 226  TYR A N   1 
ATOM   1758  C  CA  . TYR A  1 226 ? 14.964  -7.729  -13.564 1.00 2.27  ? 226  TYR A CA  1 
ATOM   1759  C  C   . TYR A  1 226 ? 15.226  -6.243  -13.376 1.00 2.00  ? 226  TYR A C   1 
ATOM   1760  O  O   . TYR A  1 226 ? 15.777  -5.589  -14.256 1.00 2.00  ? 226  TYR A O   1 
ATOM   1761  C  CB  . TYR A  1 226 ? 16.156  -8.446  -12.940 1.00 3.00  ? 226  TYR A CB  1 
ATOM   1762  C  CG  . TYR A  1 226 ? 15.939  -9.818  -12.359 1.00 4.86  ? 226  TYR A CG  1 
ATOM   1763  C  CD1 . TYR A  1 226 ? 17.004  -10.501 -11.777 1.00 6.12  ? 226  TYR A CD1 1 
ATOM   1764  C  CD2 . TYR A  1 226 ? 14.696  -10.439 -12.381 1.00 6.22  ? 226  TYR A CD2 1 
ATOM   1765  C  CE1 . TYR A  1 226 ? 16.843  -11.763 -11.234 1.00 7.39  ? 226  TYR A CE1 1 
ATOM   1766  C  CE2 . TYR A  1 226 ? 14.522  -11.719 -11.832 1.00 6.82  ? 226  TYR A CE2 1 
ATOM   1767  C  CZ  . TYR A  1 226 ? 15.606  -12.370 -11.263 1.00 7.66  ? 226  TYR A CZ  1 
ATOM   1768  O  OH  . TYR A  1 226 ? 15.471  -13.633 -10.730 1.00 10.23 ? 226  TYR A OH  1 
ATOM   1769  N  N   . PRO A  1 227 ? 14.806  -5.673  -12.250 1.00 2.00  ? 227  PRO A N   1 
ATOM   1770  C  CA  . PRO A  1 227 ? 15.140  -4.254  -12.166 1.00 2.00  ? 227  PRO A CA  1 
ATOM   1771  C  C   . PRO A  1 227 ? 16.636  -4.180  -11.800 1.00 2.55  ? 227  PRO A C   1 
ATOM   1772  O  O   . PRO A  1 227 ? 17.235  -5.189  -11.412 1.00 2.00  ? 227  PRO A O   1 
ATOM   1773  C  CB  . PRO A  1 227 ? 14.213  -3.742  -11.061 1.00 2.26  ? 227  PRO A CB  1 
ATOM   1774  C  CG  . PRO A  1 227 ? 13.887  -4.968  -10.260 1.00 2.00  ? 227  PRO A CG  1 
ATOM   1775  C  CD  . PRO A  1 227 ? 13.743  -6.031  -11.299 1.00 2.32  ? 227  PRO A CD  1 
ATOM   1776  N  N   . PRO A  1 228 ? 17.261  -3.000  -11.942 1.00 2.00  ? 228  PRO A N   1 
ATOM   1777  C  CA  . PRO A  1 228 ? 18.682  -2.819  -11.626 1.00 2.00  ? 228  PRO A CA  1 
ATOM   1778  C  C   . PRO A  1 228 ? 18.890  -2.679  -10.135 1.00 2.59  ? 228  PRO A C   1 
ATOM   1779  O  O   . PRO A  1 228 ? 18.029  -2.144  -9.442  1.00 4.52  ? 228  PRO A O   1 
ATOM   1780  C  CB  . PRO A  1 228 ? 19.039  -1.523  -12.342 1.00 2.82  ? 228  PRO A CB  1 
ATOM   1781  C  CG  . PRO A  1 228 ? 17.943  -1.357  -13.371 1.00 2.48  ? 228  PRO A CG  1 
ATOM   1782  C  CD  . PRO A  1 228 ? 16.736  -1.808  -12.620 1.00 2.00  ? 228  PRO A CD  1 
ATOM   1783  N  N   . PHE A  1 229 ? 20.037  -3.137  -9.645  1.00 3.69  ? 229  PHE A N   1 
ATOM   1784  C  CA  . PHE A  1 229 ? 20.338  -3.051  -8.220  1.00 4.76  ? 229  PHE A CA  1 
ATOM   1785  C  C   . PHE A  1 229 ? 20.543  -1.613  -7.810  1.00 6.38  ? 229  PHE A C   1 
ATOM   1786  O  O   . PHE A  1 229 ? 20.796  -0.763  -8.646  1.00 7.43  ? 229  PHE A O   1 
ATOM   1787  C  CB  . PHE A  1 229 ? 21.599  -3.837  -7.895  1.00 3.55  ? 229  PHE A CB  1 
ATOM   1788  C  CG  . PHE A  1 229 ? 21.509  -5.286  -8.243  1.00 3.12  ? 229  PHE A CG  1 
ATOM   1789  C  CD1 . PHE A  1 229 ? 20.484  -6.067  -7.731  1.00 2.84  ? 229  PHE A CD1 1 
ATOM   1790  C  CD2 . PHE A  1 229 ? 22.452  -5.874  -9.076  1.00 2.89  ? 229  PHE A CD2 1 
ATOM   1791  C  CE1 . PHE A  1 229 ? 20.398  -7.407  -8.045  1.00 3.44  ? 229  PHE A CE1 1 
ATOM   1792  C  CE2 . PHE A  1 229 ? 22.373  -7.220  -9.396  1.00 2.85  ? 229  PHE A CE2 1 
ATOM   1793  C  CZ  . PHE A  1 229 ? 21.344  -7.989  -8.881  1.00 2.95  ? 229  PHE A CZ  1 
ATOM   1794  N  N   . ASN A  1 230 ? 20.445  -1.350  -6.517  1.00 9.71  ? 230  ASN A N   1 
ATOM   1795  C  CA  . ASN A  1 230 ? 20.624  -0.010  -5.978  1.00 14.23 ? 230  ASN A CA  1 
ATOM   1796  C  C   . ASN A  1 230 ? 22.054  0.171   -5.433  1.00 18.44 ? 230  ASN A C   1 
ATOM   1797  O  O   . ASN A  1 230 ? 22.569  -0.690  -4.720  1.00 18.63 ? 230  ASN A O   1 
ATOM   1798  C  CB  . ASN A  1 230 ? 19.583  0.208   -4.878  1.00 16.20 ? 230  ASN A CB  1 
ATOM   1799  C  CG  . ASN A  1 230 ? 19.856  1.429   -4.037  1.00 17.43 ? 230  ASN A CG  1 
ATOM   1800  O  OD1 . ASN A  1 230 ? 19.802  2.560   -4.515  1.00 19.17 ? 230  ASN A OD1 1 
ATOM   1801  N  ND2 . ASN A  1 230 ? 20.143  1.206   -2.763  1.00 19.39 ? 230  ASN A ND2 1 
ATOM   1802  N  N   . ASN A  1 231 ? 22.689  1.287   -5.786  1.00 23.03 ? 231  ASN A N   1 
ATOM   1803  C  CA  . ASN A  1 231 ? 24.061  1.617   -5.361  1.00 26.19 ? 231  ASN A CA  1 
ATOM   1804  C  C   . ASN A  1 231 ? 24.314  1.492   -3.865  1.00 27.18 ? 231  ASN A C   1 
ATOM   1805  O  O   . ASN A  1 231 ? 25.156  0.705   -3.414  1.00 25.71 ? 231  ASN A O   1 
ATOM   1806  C  CB  . ASN A  1 231 ? 24.400  3.056   -5.772  1.00 29.28 ? 231  ASN A CB  1 
ATOM   1807  C  CG  . ASN A  1 231 ? 25.193  3.127   -7.058  1.00 32.70 ? 231  ASN A CG  1 
ATOM   1808  O  OD1 . ASN A  1 231 ? 25.291  2.141   -7.796  1.00 33.88 ? 231  ASN A OD1 1 
ATOM   1809  N  ND2 . ASN A  1 231 ? 25.763  4.301   -7.341  1.00 32.99 ? 231  ASN A ND2 1 
ATOM   1810  N  N   . MET A  1 232 ? 23.587  2.334   -3.134  1.00 28.81 ? 232  MET A N   1 
ATOM   1811  C  CA  . MET A  1 232 ? 23.600  2.461   -1.677  1.00 30.02 ? 232  MET A CA  1 
ATOM   1812  C  C   . MET A  1 232 ? 24.379  1.466   -0.831  1.00 29.67 ? 232  MET A C   1 
ATOM   1813  O  O   . MET A  1 232 ? 23.956  0.320   -0.659  1.00 29.44 ? 232  MET A O   1 
ATOM   1814  C  CB  . MET A  1 232 ? 22.149  2.499   -1.178  1.00 33.37 ? 232  MET A CB  1 
ATOM   1815  C  CG  . MET A  1 232 ? 21.950  2.450   0.348   1.00 37.38 ? 232  MET A CG  1 
ATOM   1816  S  SD  . MET A  1 232 ? 20.171  2.356   0.808   1.00 42.06 ? 232  MET A SD  1 
ATOM   1817  C  CE  . MET A  1 232 ? 20.248  1.897   2.574   1.00 39.18 ? 232  MET A CE  1 
ATOM   1818  N  N   . LYS A  1 233 ? 25.519  1.897   -0.300  1.00 28.34 ? 233  LYS A N   1 
ATOM   1819  C  CA  . LYS A  1 233 ? 26.238  1.013   0.588   1.00 27.66 ? 233  LYS A CA  1 
ATOM   1820  C  C   . LYS A  1 233 ? 25.502  1.213   1.923   1.00 26.82 ? 233  LYS A C   1 
ATOM   1821  O  O   . LYS A  1 233 ? 25.049  2.321   2.233   1.00 24.15 ? 233  LYS A O   1 
ATOM   1822  C  CB  . LYS A  1 233 ? 27.737  1.306   0.574   1.00 29.34 ? 233  LYS A CB  1 
ATOM   1823  C  CG  . LYS A  1 233 ? 28.441  0.368   -0.432  1.00 32.37 ? 233  LYS A CG  1 
ATOM   1824  C  CD  . LYS A  1 233 ? 27.417  -0.603  -1.080  1.00 33.47 ? 233  LYS A CD  1 
ATOM   1825  C  CE  . LYS A  1 233 ? 27.934  -1.252  -2.353  1.00 35.41 ? 233  LYS A CE  1 
ATOM   1826  N  NZ  . LYS A  1 233 ? 29.070  -2.177  -2.096  1.00 36.32 ? 233  LYS A NZ  1 
ATOM   1827  N  N   . PRO A  1 234 ? 25.443  0.159   2.752   1.00 26.20 ? 234  PRO A N   1 
ATOM   1828  C  CA  . PRO A  1 234 ? 24.836  -0.152  4.033   1.00 24.19 ? 234  PRO A CA  1 
ATOM   1829  C  C   . PRO A  1 234 ? 23.415  -0.397  3.582   1.00 22.94 ? 234  PRO A C   1 
ATOM   1830  O  O   . PRO A  1 234 ? 22.449  0.216   4.032   1.00 25.09 ? 234  PRO A O   1 
ATOM   1831  C  CB  . PRO A  1 234 ? 25.111  1.100   4.819   1.00 24.03 ? 234  PRO A CB  1 
ATOM   1832  C  CG  . PRO A  1 234 ? 26.630  1.248   4.500   1.00 25.51 ? 234  PRO A CG  1 
ATOM   1833  C  CD  . PRO A  1 234 ? 26.839  0.447   3.138   1.00 26.04 ? 234  PRO A CD  1 
ATOM   1834  N  N   . SER A  1 235 ? 23.369  -1.303  2.610   1.00 19.65 ? 235  SER A N   1 
ATOM   1835  C  CA  . SER A  1 235 ? 22.168  -1.784  1.962   1.00 17.06 ? 235  SER A CA  1 
ATOM   1836  C  C   . SER A  1 235 ? 21.568  -2.840  2.897   1.00 15.22 ? 235  SER A C   1 
ATOM   1837  O  O   . SER A  1 235 ? 22.302  -3.581  3.553   1.00 15.92 ? 235  SER A O   1 
ATOM   1838  C  CB  . SER A  1 235 ? 22.571  -2.398  0.608   1.00 16.29 ? 235  SER A CB  1 
ATOM   1839  O  OG  . SER A  1 235 ? 21.504  -3.070  -0.041  1.00 15.86 ? 235  SER A OG  1 
ATOM   1840  N  N   . PRO A  1 236 ? 20.230  -2.902  2.996   1.00 12.04 ? 236  PRO A N   1 
ATOM   1841  C  CA  . PRO A  1 236 ? 19.599  -3.893  3.872   1.00 11.63 ? 236  PRO A CA  1 
ATOM   1842  C  C   . PRO A  1 236 ? 19.572  -5.257  3.208   1.00 11.74 ? 236  PRO A C   1 
ATOM   1843  O  O   . PRO A  1 236 ? 19.720  -6.288  3.867   1.00 11.97 ? 236  PRO A O   1 
ATOM   1844  C  CB  . PRO A  1 236 ? 18.184  -3.349  4.066   1.00 10.69 ? 236  PRO A CB  1 
ATOM   1845  C  CG  . PRO A  1 236 ? 18.308  -1.899  3.747   1.00 11.68 ? 236  PRO A CG  1 
ATOM   1846  C  CD  . PRO A  1 236 ? 19.246  -1.897  2.577   1.00 12.00 ? 236  PRO A CD  1 
ATOM   1847  N  N   . CYS A  1 237 ? 19.381  -5.240  1.891   1.00 12.04 ? 237  CYS A N   1 
ATOM   1848  C  CA  . CYS A  1 237 ? 19.304  -6.459  1.088   1.00 10.41 ? 237  CYS A CA  1 
ATOM   1849  C  C   . CYS A  1 237 ? 20.525  -7.351  1.238   1.00 8.65  ? 237  CYS A C   1 
ATOM   1850  O  O   . CYS A  1 237 ? 20.388  -8.565  1.311   1.00 7.96  ? 237  CYS A O   1 
ATOM   1851  C  CB  . CYS A  1 237 ? 19.054  -6.105  -0.392  1.00 8.93  ? 237  CYS A CB  1 
ATOM   1852  S  SG  . CYS A  1 237 ? 17.383  -5.405  -0.674  1.00 7.92  ? 237  CYS A SG  1 
ATOM   1853  N  N   . GLU A  1 238 ? 21.707  -6.743  1.305   1.00 8.21  ? 238  GLU A N   1 
ATOM   1854  C  CA  . GLU A  1 238 ? 22.959  -7.480  1.461   1.00 8.81  ? 238  GLU A CA  1 
ATOM   1855  C  C   . GLU A  1 238 ? 23.119  -8.009  2.891   1.00 9.85  ? 238  GLU A C   1 
ATOM   1856  O  O   . GLU A  1 238 ? 23.572  -9.142  3.099   1.00 8.68  ? 238  GLU A O   1 
ATOM   1857  C  CB  . GLU A  1 238 ? 24.164  -6.582  1.128   1.00 10.10 ? 238  GLU A CB  1 
ATOM   1858  C  CG  . GLU A  1 238 ? 24.307  -6.168  -0.347  1.00 13.51 ? 238  GLU A CG  1 
ATOM   1859  C  CD  . GLU A  1 238 ? 25.543  -5.286  -0.614  1.00 14.70 ? 238  GLU A CD  1 
ATOM   1860  O  OE1 . GLU A  1 238 ? 25.647  -4.720  -1.727  1.00 15.31 ? 238  GLU A OE1 1 
ATOM   1861  O  OE2 . GLU A  1 238 ? 26.411  -5.159  0.282   1.00 14.86 ? 238  GLU A OE2 1 
ATOM   1862  N  N   . PHE A  1 239 ? 22.748  -7.186  3.873   1.00 9.61  ? 239  PHE A N   1 
ATOM   1863  C  CA  . PHE A  1 239 ? 22.866  -7.561  5.283   1.00 8.92  ? 239  PHE A CA  1 
ATOM   1864  C  C   . PHE A  1 239 ? 22.168  -8.875  5.583   1.00 9.05  ? 239  PHE A C   1 
ATOM   1865  O  O   . PHE A  1 239 ? 22.699  -9.713  6.313   1.00 7.45  ? 239  PHE A O   1 
ATOM   1866  C  CB  . PHE A  1 239 ? 22.292  -6.466  6.185   1.00 10.84 ? 239  PHE A CB  1 
ATOM   1867  C  CG  . PHE A  1 239 ? 22.518  -6.707  7.663   1.00 13.06 ? 239  PHE A CG  1 
ATOM   1868  C  CD1 . PHE A  1 239 ? 23.802  -6.908  8.162   1.00 14.37 ? 239  PHE A CD1 1 
ATOM   1869  C  CD2 . PHE A  1 239 ? 21.447  -6.698  8.561   1.00 13.57 ? 239  PHE A CD2 1 
ATOM   1870  C  CE1 . PHE A  1 239 ? 24.016  -7.092  9.530   1.00 15.39 ? 239  PHE A CE1 1 
ATOM   1871  C  CE2 . PHE A  1 239 ? 21.648  -6.881  9.930   1.00 12.86 ? 239  PHE A CE2 1 
ATOM   1872  C  CZ  . PHE A  1 239 ? 22.931  -7.077  10.416  1.00 15.23 ? 239  PHE A CZ  1 
ATOM   1873  N  N   . ILE A  1 240 ? 20.974  -9.051  5.025   1.00 9.91  ? 240  ILE A N   1 
ATOM   1874  C  CA  . ILE A  1 240 ? 20.226  -10.279 5.245   1.00 11.16 ? 240  ILE A CA  1 
ATOM   1875  C  C   . ILE A  1 240 ? 21.188  -11.430 5.114   1.00 12.14 ? 240  ILE A C   1 
ATOM   1876  O  O   . ILE A  1 240 ? 21.475  -12.127 6.087   1.00 14.07 ? 240  ILE A O   1 
ATOM   1877  C  CB  . ILE A  1 240 ? 19.078  -10.451 4.225   1.00 9.88  ? 240  ILE A CB  1 
ATOM   1878  C  CG1 . ILE A  1 240 ? 17.895  -9.587  4.653   1.00 9.89  ? 240  ILE A CG1 1 
ATOM   1879  C  CG2 . ILE A  1 240 ? 18.648  -11.923 4.139   1.00 10.17 ? 240  ILE A CG2 1 
ATOM   1880  C  CD1 . ILE A  1 240 ? 17.501  -9.794  6.111   1.00 9.83  ? 240  ILE A CD1 1 
ATOM   1881  N  N   . ASN A  1 241 ? 21.695  -11.623 3.906   1.00 13.58 ? 241  ASN A N   1 
ATOM   1882  C  CA  . ASN A  1 241 ? 22.645  -12.686 3.673   1.00 15.11 ? 241  ASN A CA  1 
ATOM   1883  C  C   . ASN A  1 241 ? 23.906  -12.157 3.018   1.00 16.03 ? 241  ASN A C   1 
ATOM   1884  O  O   . ASN A  1 241 ? 23.931  -11.856 1.819   1.00 15.55 ? 241  ASN A O   1 
ATOM   1885  C  CB  . ASN A  1 241 ? 22.046  -13.775 2.803   1.00 16.03 ? 241  ASN A CB  1 
ATOM   1886  C  CG  . ASN A  1 241 ? 23.000  -14.914 2.599   1.00 18.79 ? 241  ASN A CG  1 
ATOM   1887  O  OD1 . ASN A  1 241 ? 24.066  -14.750 2.014   1.00 16.92 ? 241  ASN A OD1 1 
ATOM   1888  N  ND2 . ASN A  1 241 ? 22.623  -16.075 3.108   1.00 24.76 ? 241  ASN A ND2 1 
ATOM   1889  N  N   . THR A  1 242 ? 24.952  -12.043 3.831   1.00 17.15 ? 242  THR A N   1 
ATOM   1890  C  CA  . THR A  1 242 ? 26.249  -11.563 3.381   1.00 17.28 ? 242  THR A CA  1 
ATOM   1891  C  C   . THR A  1 242 ? 26.904  -12.533 2.389   1.00 17.46 ? 242  THR A C   1 
ATOM   1892  O  O   . THR A  1 242 ? 27.580  -12.106 1.454   1.00 18.94 ? 242  THR A O   1 
ATOM   1893  C  CB  . THR A  1 242 ? 27.186  -11.344 4.586   1.00 16.30 ? 242  THR A CB  1 
ATOM   1894  O  OG1 . THR A  1 242 ? 27.189  -12.519 5.410   1.00 14.28 ? 242  THR A OG1 1 
ATOM   1895  C  CG2 . THR A  1 242 ? 26.716  -10.151 5.407   1.00 15.58 ? 242  THR A CG2 1 
ATOM   1896  N  N   . THR A  1 243 ? 26.703  -13.833 2.582   1.00 17.01 ? 243  THR A N   1 
ATOM   1897  C  CA  . THR A  1 243 ? 27.290  -14.817 1.674   1.00 16.50 ? 243  THR A CA  1 
ATOM   1898  C  C   . THR A  1 243 ? 26.817  -14.560 0.244   1.00 14.88 ? 243  THR A C   1 
ATOM   1899  O  O   . THR A  1 243 ? 27.623  -14.464 -0.684  1.00 13.52 ? 243  THR A O   1 
ATOM   1900  C  CB  . THR A  1 243 ? 26.899  -16.264 2.055   1.00 17.46 ? 243  THR A CB  1 
ATOM   1901  O  OG1 . THR A  1 243 ? 27.373  -16.567 3.374   1.00 18.09 ? 243  THR A OG1 1 
ATOM   1902  C  CG2 . THR A  1 243 ? 27.502  -17.252 1.063   1.00 17.40 ? 243  THR A CG2 1 
ATOM   1903  N  N   . ALA A  1 244 ? 25.502  -14.458 0.076   1.00 13.92 ? 244  ALA A N   1 
ATOM   1904  C  CA  . ALA A  1 244 ? 24.916  -14.210 -1.235  1.00 12.88 ? 244  ALA A CA  1 
ATOM   1905  C  C   . ALA A  1 244 ? 25.344  -12.833 -1.694  1.00 12.12 ? 244  ALA A C   1 
ATOM   1906  O  O   . ALA A  1 244 ? 25.846  -12.669 -2.799  1.00 12.22 ? 244  ALA A O   1 
ATOM   1907  C  CB  . ALA A  1 244 ? 23.397  -14.292 -1.164  1.00 12.28 ? 244  ALA A CB  1 
ATOM   1908  N  N   . ARG A  1 245 ? 25.131  -11.841 -0.842  1.00 12.68 ? 245  ARG A N   1 
ATOM   1909  C  CA  . ARG A  1 245 ? 25.527  -10.478 -1.169  1.00 13.73 ? 245  ARG A CA  1 
ATOM   1910  C  C   . ARG A  1 245 ? 24.790  -9.976  -2.411  1.00 10.45 ? 245  ARG A C   1 
ATOM   1911  O  O   . ARG A  1 245 ? 25.396  -9.703  -3.448  1.00 7.43  ? 245  ARG A O   1 
ATOM   1912  C  CB  . ARG A  1 245 ? 27.043  -10.446 -1.385  1.00 19.20 ? 245  ARG A CB  1 
ATOM   1913  C  CG  . ARG A  1 245 ? 27.727  -9.145  -1.010  1.00 27.21 ? 245  ARG A CG  1 
ATOM   1914  C  CD  . ARG A  1 245 ? 29.144  -9.424  -0.497  1.00 33.28 ? 245  ARG A CD  1 
ATOM   1915  N  NE  . ARG A  1 245 ? 29.215  -9.426  0.967   1.00 39.85 ? 245  ARG A NE  1 
ATOM   1916  C  CZ  . ARG A  1 245 ? 29.727  -10.415 1.698   1.00 42.53 ? 245  ARG A CZ  1 
ATOM   1917  N  NH1 . ARG A  1 245 ? 30.217  -11.502 1.110   1.00 43.74 ? 245  ARG A NH1 1 
ATOM   1918  N  NH2 . ARG A  1 245 ? 29.753  -10.314 3.025   1.00 45.66 ? 245  ARG A NH2 1 
ATOM   1919  N  N   . VAL A  1 246 ? 23.471  -9.873  -2.293  1.00 8.12  ? 246  VAL A N   1 
ATOM   1920  C  CA  . VAL A  1 246 ? 22.640  -9.402  -3.392  1.00 5.88  ? 246  VAL A CA  1 
ATOM   1921  C  C   . VAL A  1 246 ? 21.933  -8.118  -2.968  1.00 5.37  ? 246  VAL A C   1 
ATOM   1922  O  O   . VAL A  1 246 ? 21.105  -8.115  -2.054  1.00 6.14  ? 246  VAL A O   1 
ATOM   1923  C  CB  . VAL A  1 246 ? 21.589  -10.458 -3.803  1.00 5.23  ? 246  VAL A CB  1 
ATOM   1924  C  CG1 . VAL A  1 246 ? 20.766  -9.941  -4.980  1.00 5.00  ? 246  VAL A CG1 1 
ATOM   1925  C  CG2 . VAL A  1 246 ? 22.282  -11.763 -4.170  1.00 3.36  ? 246  VAL A CG2 1 
ATOM   1926  N  N   . PRO A  1 247 ? 22.250  -7.006  -3.638  1.00 4.64  ? 247  PRO A N   1 
ATOM   1927  C  CA  . PRO A  1 247 ? 21.667  -5.696  -3.345  1.00 5.33  ? 247  PRO A CA  1 
ATOM   1928  C  C   . PRO A  1 247 ? 20.171  -5.528  -3.630  1.00 5.38  ? 247  PRO A C   1 
ATOM   1929  O  O   . PRO A  1 247 ? 19.536  -6.355  -4.301  1.00 4.89  ? 247  PRO A O   1 
ATOM   1930  C  CB  . PRO A  1 247 ? 22.527  -4.751  -4.180  1.00 5.33  ? 247  PRO A CB  1 
ATOM   1931  C  CG  . PRO A  1 247 ? 22.839  -5.595  -5.382  1.00 4.92  ? 247  PRO A CG  1 
ATOM   1932  C  CD  . PRO A  1 247 ? 23.182  -6.927  -4.774  1.00 3.97  ? 247  PRO A CD  1 
ATOM   1933  N  N   . CYS A  1 248 ? 19.628  -4.438  -3.093  1.00 4.70  ? 248  CYS A N   1 
ATOM   1934  C  CA  . CYS A  1 248 ? 18.230  -4.086  -3.263  1.00 3.30  ? 248  CYS A CA  1 
ATOM   1935  C  C   . CYS A  1 248 ? 17.953  -3.667  -4.702  1.00 3.47  ? 248  CYS A C   1 
ATOM   1936  O  O   . CYS A  1 248 ? 18.835  -3.179  -5.411  1.00 2.38  ? 248  CYS A O   1 
ATOM   1937  C  CB  . CYS A  1 248 ? 17.871  -2.932  -2.332  1.00 4.72  ? 248  CYS A CB  1 
ATOM   1938  S  SG  . CYS A  1 248 ? 17.649  -3.399  -0.593  1.00 4.31  ? 248  CYS A SG  1 
ATOM   1939  N  N   . PHE A  1 249 ? 16.720  -3.857  -5.139  1.00 2.53  ? 249  PHE A N   1 
ATOM   1940  C  CA  . PHE A  1 249 ? 16.380  -3.471  -6.485  1.00 2.00  ? 249  PHE A CA  1 
ATOM   1941  C  C   . PHE A  1 249 ? 16.111  -1.996  -6.524  1.00 2.32  ? 249  PHE A C   1 
ATOM   1942  O  O   . PHE A  1 249 ? 15.642  -1.417  -5.552  1.00 4.73  ? 249  PHE A O   1 
ATOM   1943  C  CB  . PHE A  1 249 ? 15.152  -4.222  -6.964  1.00 2.00  ? 249  PHE A CB  1 
ATOM   1944  C  CG  . PHE A  1 249 ? 15.461  -5.562  -7.524  1.00 2.00  ? 249  PHE A CG  1 
ATOM   1945  C  CD1 . PHE A  1 249 ? 16.696  -5.804  -8.111  1.00 2.00  ? 249  PHE A CD1 1 
ATOM   1946  C  CD2 . PHE A  1 249 ? 14.508  -6.569  -7.518  1.00 2.01  ? 249  PHE A CD2 1 
ATOM   1947  C  CE1 . PHE A  1 249 ? 16.975  -7.025  -8.685  1.00 2.65  ? 249  PHE A CE1 1 
ATOM   1948  C  CE2 . PHE A  1 249 ? 14.776  -7.794  -8.090  1.00 2.00  ? 249  PHE A CE2 1 
ATOM   1949  C  CZ  . PHE A  1 249 ? 16.014  -8.025  -8.676  1.00 2.81  ? 249  PHE A CZ  1 
ATOM   1950  N  N   . GLN A  1 250 ? 16.419  -1.381  -7.650  1.00 2.00  ? 250  GLN A N   1 
ATOM   1951  C  CA  . GLN A  1 250 ? 16.173  0.032   -7.797  1.00 2.52  ? 250  GLN A CA  1 
ATOM   1952  C  C   . GLN A  1 250 ? 14.892  0.205   -8.582  1.00 3.41  ? 250  GLN A C   1 
ATOM   1953  O  O   . GLN A  1 250 ? 14.806  -0.234  -9.723  1.00 4.91  ? 250  GLN A O   1 
ATOM   1954  C  CB  . GLN A  1 250 ? 17.315  0.683   -8.544  1.00 2.00  ? 250  GLN A CB  1 
ATOM   1955  C  CG  . GLN A  1 250 ? 17.007  2.086   -8.932  1.00 4.18  ? 250  GLN A CG  1 
ATOM   1956  C  CD  . GLN A  1 250 ? 18.204  2.972   -8.789  1.00 6.09  ? 250  GLN A CD  1 
ATOM   1957  O  OE1 . GLN A  1 250 ? 19.153  2.893   -9.577  1.00 7.44  ? 250  GLN A OE1 1 
ATOM   1958  N  NE2 . GLN A  1 250 ? 18.184  3.821   -7.762  1.00 6.73  ? 250  GLN A NE2 1 
ATOM   1959  N  N   . ALA A  1 251 ? 13.892  0.841   -7.989  1.00 2.55  ? 251  ALA A N   1 
ATOM   1960  C  CA  . ALA A  1 251 ? 12.637  1.031   -8.698  1.00 2.00  ? 251  ALA A CA  1 
ATOM   1961  C  C   . ALA A  1 251 ? 12.111  2.448   -8.539  1.00 2.40  ? 251  ALA A C   1 
ATOM   1962  O  O   . ALA A  1 251 ? 12.704  3.261   -7.833  1.00 2.03  ? 251  ALA A O   1 
ATOM   1963  C  CB  . ALA A  1 251 ? 11.613  0.029   -8.198  1.00 2.48  ? 251  ALA A CB  1 
ATOM   1964  N  N   . GLY A  1 252 ? 10.989  2.735   -9.193  1.00 2.77  ? 252  GLY A N   1 
ATOM   1965  C  CA  . GLY A  1 252 ? 10.395  4.060   -9.113  1.00 2.44  ? 252  GLY A CA  1 
ATOM   1966  C  C   . GLY A  1 252 ? 9.969   4.514   -7.723  1.00 3.70  ? 252  GLY A C   1 
ATOM   1967  O  O   . GLY A  1 252 ? 9.628   5.686   -7.541  1.00 5.59  ? 252  GLY A O   1 
ATOM   1968  N  N   . ASP A  1 253 ? 9.982   3.599   -6.751  1.00 3.25  ? 253  ASP A N   1 
ATOM   1969  C  CA  . ASP A  1 253 ? 9.599   3.898   -5.364  1.00 3.29  ? 253  ASP A CA  1 
ATOM   1970  C  C   . ASP A  1 253 ? 10.483  3.161   -4.358  1.00 3.36  ? 253  ASP A C   1 
ATOM   1971  O  O   . ASP A  1 253 ? 10.699  1.961   -4.479  1.00 3.63  ? 253  ASP A O   1 
ATOM   1972  C  CB  . ASP A  1 253 ? 8.144   3.491   -5.111  1.00 5.53  ? 253  ASP A CB  1 
ATOM   1973  C  CG  . ASP A  1 253 ? 7.747   3.597   -3.629  1.00 7.89  ? 253  ASP A CG  1 
ATOM   1974  O  OD1 . ASP A  1 253 ? 7.621   4.743   -3.123  1.00 6.58  ? 253  ASP A OD1 1 
ATOM   1975  O  OD2 . ASP A  1 253 ? 7.568   2.535   -2.976  1.00 7.39  ? 253  ASP A OD2 1 
ATOM   1976  N  N   . SER A  1 254 ? 10.968  3.871   -3.347  1.00 3.79  ? 254  SER A N   1 
ATOM   1977  C  CA  . SER A  1 254 ? 11.848  3.262   -2.330  1.00 4.08  ? 254  SER A CA  1 
ATOM   1978  C  C   . SER A  1 254 ? 11.432  1.855   -1.881  1.00 4.71  ? 254  SER A C   1 
ATOM   1979  O  O   . SER A  1 254 ? 12.147  0.898   -2.161  1.00 8.34  ? 254  SER A O   1 
ATOM   1980  C  CB  . SER A  1 254 ? 11.887  4.141   -1.078  1.00 4.17  ? 254  SER A CB  1 
ATOM   1981  O  OG  . SER A  1 254 ? 12.479  5.392   -1.359  1.00 8.38  ? 254  SER A OG  1 
ATOM   1982  N  N   . ARG A  1 255 ? 10.271  1.715   -1.231  1.00 3.52  ? 255  ARG A N   1 
ATOM   1983  C  CA  . ARG A  1 255 ? 9.873   0.409   -0.665  1.00 2.54  ? 255  ARG A CA  1 
ATOM   1984  C  C   . ARG A  1 255 ? 9.880   -0.831  -1.594  1.00 2.45  ? 255  ARG A C   1 
ATOM   1985  O  O   . ARG A  1 255 ? 9.777   -1.974  -1.119  1.00 2.00  ? 255  ARG A O   1 
ATOM   1986  C  CB  . ARG A  1 255 ? 8.541   0.539   0.068   1.00 2.50  ? 255  ARG A CB  1 
ATOM   1987  C  CG  . ARG A  1 255 ? 8.335   1.805   0.867   1.00 2.00  ? 255  ARG A CG  1 
ATOM   1988  C  CD  . ARG A  1 255 ? 7.500   2.751   0.018   1.00 3.19  ? 255  ARG A CD  1 
ATOM   1989  N  NE  . ARG A  1 255 ? 6.596   3.557   0.837   1.00 2.46  ? 255  ARG A NE  1 
ATOM   1990  C  CZ  . ARG A  1 255 ? 5.555   4.179   0.324   1.00 2.00  ? 255  ARG A CZ  1 
ATOM   1991  N  NH1 . ARG A  1 255 ? 5.283   4.060   -0.974  1.00 2.00  ? 255  ARG A NH1 1 
ATOM   1992  N  NH2 . ARG A  1 255 ? 4.785   4.924   1.104   1.00 2.00  ? 255  ARG A NH2 1 
ATOM   1993  N  N   . ALA A  1 256 ? 10.010  -0.608  -2.864  1.00 2.08  ? 256  ALA A N   1 
ATOM   1994  C  CA  . ALA A  1 256 ? 10.032  -1.690  -3.849  1.00 2.00  ? 256  ALA A CA  1 
ATOM   1995  C  C   . ALA A  1 256 ? 10.534  -3.053  -3.375  1.00 2.00  ? 256  ALA A C   1 
ATOM   1996  O  O   . ALA A  1 256 ? 10.061  -4.077  -3.850  1.00 2.00  ? 256  ALA A O   1 
ATOM   1997  C  CB  . ALA A  1 256 ? 10.854  -1.231  -5.044  1.00 2.00  ? 256  ALA A CB  1 
ATOM   1998  N  N   . SER A  1 257 ? 11.477  -3.100  -2.446  1.00 2.47  ? 257  SER A N   1 
ATOM   1999  C  CA  . SER A  1 257 ? 11.972  -4.415  -2.022  1.00 3.90  ? 257  SER A CA  1 
ATOM   2000  C  C   . SER A  1 257 ? 11.788  -4.772  -0.503  1.00 2.02  ? 257  SER A C   1 
ATOM   2001  O  O   . SER A  1 257 ? 12.640  -5.430  0.089   1.00 2.00  ? 257  SER A O   1 
ATOM   2002  C  CB  . SER A  1 257 ? 13.435  -4.578  -2.430  1.00 4.05  ? 257  SER A CB  1 
ATOM   2003  O  OG  . SER A  1 257 ? 14.082  -3.319  -2.510  1.00 7.04  ? 257  SER A OG  1 
ATOM   2004  N  N   . GLU A  1 258 ? 10.678  -4.345  0.131   1.00 2.74  ? 258  GLU A N   1 
ATOM   2005  C  CA  . GLU A  1 258 ? 10.463  -4.696  1.579   1.00 2.00  ? 258  GLU A CA  1 
ATOM   2006  C  C   . GLU A  1 258 ? 10.128  -6.185  1.656   1.00 2.00  ? 258  GLU A C   1 
ATOM   2007  O  O   . GLU A  1 258 ? 10.309  -6.788  2.712   1.00 2.15  ? 258  GLU A O   1 
ATOM   2008  C  CB  . GLU A  1 258 ? 9.306   -3.910  2.270   1.00 2.00  ? 258  GLU A CB  1 
ATOM   2009  C  CG  . GLU A  1 258 ? 8.996   -4.358  3.721   1.00 2.40  ? 258  GLU A CG  1 
ATOM   2010  C  CD  . GLU A  1 258 ? 7.517   -4.761  3.986   1.00 2.00  ? 258  GLU A CD  1 
ATOM   2011  O  OE1 . GLU A  1 258 ? 6.724   -4.672  3.026   1.00 2.00  ? 258  GLU A OE1 1 
ATOM   2012  O  OE2 . GLU A  1 258 ? 7.197   -5.151  5.115   1.00 2.14  ? 258  GLU A OE2 1 
ATOM   2013  N  N   . GLN A  1 259 ? 9.637   -6.762  0.592   1.00 2.00  ? 259  GLN A N   1 
ATOM   2014  C  CA  . GLN A  1 259 ? 9.334   -8.174  0.681   1.00 2.00  ? 259  GLN A CA  1 
ATOM   2015  C  C   . GLN A  1 259 ? 9.275   -8.851  -0.679  1.00 3.25  ? 259  GLN A C   1 
ATOM   2016  O  O   . GLN A  1 259 ? 8.876   -8.273  -1.699  1.00 2.87  ? 259  GLN A O   1 
ATOM   2017  C  CB  . GLN A  1 259 ? 8.090   -8.369  1.524   1.00 2.00  ? 259  GLN A CB  1 
ATOM   2018  C  CG  . GLN A  1 259 ? 6.853   -7.635  1.036   1.00 2.00  ? 259  GLN A CG  1 
ATOM   2019  C  CD  . GLN A  1 259 ? 5.987   -8.554  0.215   1.00 2.28  ? 259  GLN A CD  1 
ATOM   2020  O  OE1 . GLN A  1 259 ? 6.197   -9.764  0.208   1.00 2.85  ? 259  GLN A OE1 1 
ATOM   2021  N  NE2 . GLN A  1 259 ? 4.963   -8.193  -0.555  1.00 2.00  ? 259  GLN A NE2 1 
ATOM   2022  N  N   . ILE A  1 260 ? 9.729   -10.100 -0.698  1.00 2.38  ? 260  ILE A N   1 
ATOM   2023  C  CA  . ILE A  1 260 ? 9.877   -10.822 -1.931  1.00 2.26  ? 260  ILE A CA  1 
ATOM   2024  C  C   . ILE A  1 260 ? 8.684   -10.676 -2.818  1.00 2.00  ? 260  ILE A C   1 
ATOM   2025  O  O   . ILE A  1 260 ? 8.800   -10.533 -4.036  1.00 2.10  ? 260  ILE A O   1 
ATOM   2026  C  CB  . ILE A  1 260 ? 10.119  -12.320 -1.741  1.00 2.00  ? 260  ILE A CB  1 
ATOM   2027  C  CG1 . ILE A  1 260 ? 10.658  -12.926 -3.042  1.00 2.00  ? 260  ILE A CG1 1 
ATOM   2028  C  CG2 . ILE A  1 260 ? 8.834   -13.044 -1.335  1.00 2.49  ? 260  ILE A CG2 1 
ATOM   2029  C  CD1 . ILE A  1 260 ? 12.129  -13.282 -2.991  1.00 2.00  ? 260  ILE A CD1 1 
ATOM   2030  N  N   . LEU A  1 261 ? 7.498   -10.714 -2.246  1.00 2.00  ? 261  LEU A N   1 
ATOM   2031  C  CA  . LEU A  1 261 ? 6.284   -10.617 -3.017  1.00 2.00  ? 261  LEU A CA  1 
ATOM   2032  C  C   . LEU A  1 261 ? 6.040   -9.264  -3.684  1.00 2.00  ? 261  LEU A C   1 
ATOM   2033  O  O   . LEU A  1 261 ? 5.527   -9.215  -4.797  1.00 2.43  ? 261  LEU A O   1 
ATOM   2034  C  CB  . LEU A  1 261 ? 5.103   -10.950 -2.115  1.00 2.00  ? 261  LEU A CB  1 
ATOM   2035  C  CG  . LEU A  1 261 ? 4.430   -12.301 -2.337  1.00 2.00  ? 261  LEU A CG  1 
ATOM   2036  C  CD1 . LEU A  1 261 ? 5.115   -13.053 -3.462  1.00 2.00  ? 261  LEU A CD1 1 
ATOM   2037  C  CD2 . LEU A  1 261 ? 4.442   -13.118 -1.047  1.00 2.00  ? 261  LEU A CD2 1 
ATOM   2038  N  N   . LEU A  1 262 ? 6.387   -8.170  -3.015  1.00 2.00  ? 262  LEU A N   1 
ATOM   2039  C  CA  . LEU A  1 262 ? 6.195   -6.841  -3.594  1.00 2.00  ? 262  LEU A CA  1 
ATOM   2040  C  C   . LEU A  1 262 ? 7.217   -6.591  -4.695  1.00 2.00  ? 262  LEU A C   1 
ATOM   2041  O  O   . LEU A  1 262 ? 6.872   -6.141  -5.794  1.00 2.00  ? 262  LEU A O   1 
ATOM   2042  C  CB  . LEU A  1 262 ? 6.334   -5.750  -2.526  1.00 2.00  ? 262  LEU A CB  1 
ATOM   2043  C  CG  . LEU A  1 262 ? 6.438   -4.319  -3.074  1.00 2.00  ? 262  LEU A CG  1 
ATOM   2044  C  CD1 . LEU A  1 262 ? 5.272   -4.037  -4.009  1.00 2.00  ? 262  LEU A CD1 1 
ATOM   2045  C  CD2 . LEU A  1 262 ? 6.459   -3.322  -1.932  1.00 2.00  ? 262  LEU A CD2 1 
ATOM   2046  N  N   . ALA A  1 263 ? 8.479   -6.882  -4.387  1.00 2.00  ? 263  ALA A N   1 
ATOM   2047  C  CA  . ALA A  1 263 ? 9.557   -6.702  -5.346  1.00 2.00  ? 263  ALA A CA  1 
ATOM   2048  C  C   . ALA A  1 263 ? 9.230   -7.497  -6.602  1.00 2.00  ? 263  ALA A C   1 
ATOM   2049  O  O   . ALA A  1 263 ? 9.688   -7.167  -7.692  1.00 2.00  ? 263  ALA A O   1 
ATOM   2050  C  CB  . ALA A  1 263 ? 10.872  -7.173  -4.749  1.00 2.00  ? 263  ALA A CB  1 
ATOM   2051  N  N   . THR A  1 264 ? 8.427   -8.543  -6.437  1.00 2.03  ? 264  THR A N   1 
ATOM   2052  C  CA  . THR A  1 264 ? 8.019   -9.389  -7.546  1.00 2.00  ? 264  THR A CA  1 
ATOM   2053  C  C   . THR A  1 264 ? 7.099   -8.652  -8.515  1.00 2.21  ? 264  THR A C   1 
ATOM   2054  O  O   . THR A  1 264 ? 7.449   -8.447  -9.680  1.00 2.93  ? 264  THR A O   1 
ATOM   2055  C  CB  . THR A  1 264 ? 7.346   -10.648 -7.016  1.00 2.00  ? 264  THR A CB  1 
ATOM   2056  O  OG1 . THR A  1 264 ? 8.345   -11.458 -6.398  1.00 2.00  ? 264  THR A OG1 1 
ATOM   2057  C  CG2 . THR A  1 264 ? 6.688   -11.434 -8.118  1.00 2.00  ? 264  THR A CG2 1 
ATOM   2058  N  N   . VAL A  1 265 ? 5.928   -8.234  -8.056  1.00 2.00  ? 265  VAL A N   1 
ATOM   2059  C  CA  . VAL A  1 265 ? 5.043   -7.518  -8.958  1.00 2.00  ? 265  VAL A CA  1 
ATOM   2060  C  C   . VAL A  1 265 ? 5.742   -6.271  -9.496  1.00 2.00  ? 265  VAL A C   1 
ATOM   2061  O  O   . VAL A  1 265 ? 5.388   -5.744  -10.555 1.00 2.00  ? 265  VAL A O   1 
ATOM   2062  C  CB  . VAL A  1 265 ? 3.744   -7.113  -8.261  1.00 2.00  ? 265  VAL A CB  1 
ATOM   2063  C  CG1 . VAL A  1 265 ? 2.870   -6.329  -9.214  1.00 2.00  ? 265  VAL A CG1 1 
ATOM   2064  C  CG2 . VAL A  1 265 ? 3.013   -8.347  -7.795  1.00 2.00  ? 265  VAL A CG2 1 
ATOM   2065  N  N   . HIS A  1 266 ? 6.753   -5.804  -8.775  1.00 2.19  ? 266  HIS A N   1 
ATOM   2066  C  CA  . HIS A  1 266 ? 7.469   -4.615  -9.210  1.00 3.02  ? 266  HIS A CA  1 
ATOM   2067  C  C   . HIS A  1 266 ? 8.228   -4.841  -10.494 1.00 3.45  ? 266  HIS A C   1 
ATOM   2068  O  O   . HIS A  1 266 ? 8.588   -3.887  -11.195 1.00 3.66  ? 266  HIS A O   1 
ATOM   2069  C  CB  . HIS A  1 266 ? 8.423   -4.148  -8.131  1.00 2.00  ? 266  HIS A CB  1 
ATOM   2070  C  CG  . HIS A  1 266 ? 8.103   -2.787  -7.615  1.00 2.00  ? 266  HIS A CG  1 
ATOM   2071  N  ND1 . HIS A  1 266 ? 8.366   -1.642  -8.333  1.00 2.00  ? 266  HIS A ND1 1 
ATOM   2072  C  CD2 . HIS A  1 266 ? 7.509   -2.387  -6.466  1.00 2.00  ? 266  HIS A CD2 1 
ATOM   2073  C  CE1 . HIS A  1 266 ? 7.950   -0.595  -7.645  1.00 2.28  ? 266  HIS A CE1 1 
ATOM   2074  N  NE2 . HIS A  1 266 ? 7.426   -1.020  -6.508  1.00 2.00  ? 266  HIS A NE2 1 
ATOM   2075  N  N   . THR A  1 267 ? 8.465   -6.116  -10.789 1.00 3.40  ? 267  THR A N   1 
ATOM   2076  C  CA  . THR A  1 267 ? 9.175   -6.526  -11.990 1.00 3.55  ? 267  THR A CA  1 
ATOM   2077  C  C   . THR A  1 267 ? 8.165   -6.748  -13.111 1.00 3.22  ? 267  THR A C   1 
ATOM   2078  O  O   . THR A  1 267 ? 8.381   -6.297  -14.237 1.00 3.63  ? 267  THR A O   1 
ATOM   2079  C  CB  . THR A  1 267 ? 9.975   -7.809  -11.733 1.00 2.00  ? 267  THR A CB  1 
ATOM   2080  O  OG1 . THR A  1 267 ? 10.815  -7.599  -10.598 1.00 2.65  ? 267  THR A OG1 1 
ATOM   2081  C  CG2 . THR A  1 267 ? 10.848  -8.166  -12.931 1.00 2.00  ? 267  THR A CG2 1 
ATOM   2082  N  N   . LEU A  1 268 ? 7.063   -7.435  -12.822 1.00 2.00  ? 268  LEU A N   1 
ATOM   2083  C  CA  . LEU A  1 268 ? 6.063   -7.623  -13.862 1.00 2.38  ? 268  LEU A CA  1 
ATOM   2084  C  C   . LEU A  1 268 ? 5.727   -6.253  -14.441 1.00 2.89  ? 268  LEU A C   1 
ATOM   2085  O  O   . LEU A  1 268 ? 5.542   -6.091  -15.646 1.00 2.00  ? 268  LEU A O   1 
ATOM   2086  C  CB  . LEU A  1 268 ? 4.804   -8.270  -13.298 1.00 3.69  ? 268  LEU A CB  1 
ATOM   2087  C  CG  . LEU A  1 268 ? 4.713   -9.784  -13.437 1.00 4.50  ? 268  LEU A CG  1 
ATOM   2088  C  CD1 . LEU A  1 268 ? 5.975   -10.462 -12.912 1.00 5.42  ? 268  LEU A CD1 1 
ATOM   2089  C  CD2 . LEU A  1 268 ? 3.488   -10.240 -12.678 1.00 6.12  ? 268  LEU A CD2 1 
ATOM   2090  N  N   . LEU A  1 269 ? 5.659   -5.259  -13.571 1.00 2.04  ? 269  LEU A N   1 
ATOM   2091  C  CA  . LEU A  1 269 ? 5.372   -3.917  -14.022 1.00 2.46  ? 269  LEU A CA  1 
ATOM   2092  C  C   . LEU A  1 269 ? 6.487   -3.448  -14.958 1.00 3.33  ? 269  LEU A C   1 
ATOM   2093  O  O   . LEU A  1 269 ? 6.246   -3.103  -16.127 1.00 2.00  ? 269  LEU A O   1 
ATOM   2094  C  CB  . LEU A  1 269 ? 5.272   -3.000  -12.813 1.00 2.19  ? 269  LEU A CB  1 
ATOM   2095  C  CG  . LEU A  1 269 ? 3.869   -2.462  -12.551 1.00 2.82  ? 269  LEU A CG  1 
ATOM   2096  C  CD1 . LEU A  1 269 ? 2.773   -3.530  -12.777 1.00 2.00  ? 269  LEU A CD1 1 
ATOM   2097  C  CD2 . LEU A  1 269 ? 3.857   -1.951  -11.128 1.00 2.23  ? 269  LEU A CD2 1 
ATOM   2098  N  N   . LEU A  1 270 ? 7.710   -3.450  -14.432 1.00 2.55  ? 270  LEU A N   1 
ATOM   2099  C  CA  . LEU A  1 270 ? 8.873   -3.031  -15.192 1.00 2.68  ? 270  LEU A CA  1 
ATOM   2100  C  C   . LEU A  1 270 ? 8.935   -3.726  -16.544 1.00 3.21  ? 270  LEU A C   1 
ATOM   2101  O  O   . LEU A  1 270 ? 9.286   -3.120  -17.552 1.00 4.58  ? 270  LEU A O   1 
ATOM   2102  C  CB  . LEU A  1 270 ? 10.148  -3.342  -14.420 1.00 2.02  ? 270  LEU A CB  1 
ATOM   2103  C  CG  . LEU A  1 270 ? 11.415  -2.922  -15.153 1.00 2.00  ? 270  LEU A CG  1 
ATOM   2104  C  CD1 . LEU A  1 270 ? 11.477  -1.413  -15.194 1.00 2.00  ? 270  LEU A CD1 1 
ATOM   2105  C  CD2 . LEU A  1 270 ? 12.626  -3.484  -14.455 1.00 2.65  ? 270  LEU A CD2 1 
ATOM   2106  N  N   . ARG A  1 271 ? 8.600   -5.007  -16.566 1.00 3.11  ? 271  ARG A N   1 
ATOM   2107  C  CA  . ARG A  1 271 ? 8.629   -5.752  -17.810 1.00 2.91  ? 271  ARG A CA  1 
ATOM   2108  C  C   . ARG A  1 271 ? 7.511   -5.319  -18.738 1.00 2.89  ? 271  ARG A C   1 
ATOM   2109  O  O   . ARG A  1 271 ? 7.686   -5.275  -19.957 1.00 2.65  ? 271  ARG A O   1 
ATOM   2110  C  CB  . ARG A  1 271 ? 8.510   -7.240  -17.529 1.00 2.19  ? 271  ARG A CB  1 
ATOM   2111  C  CG  . ARG A  1 271 ? 9.665   -7.777  -16.731 1.00 2.00  ? 271  ARG A CG  1 
ATOM   2112  C  CD  . ARG A  1 271 ? 9.534   -9.252  -16.595 1.00 2.00  ? 271  ARG A CD  1 
ATOM   2113  N  NE  . ARG A  1 271 ? 10.668  -9.828  -15.897 1.00 2.00  ? 271  ARG A NE  1 
ATOM   2114  C  CZ  . ARG A  1 271 ? 10.769  -11.119 -15.621 1.00 2.12  ? 271  ARG A CZ  1 
ATOM   2115  N  NH1 . ARG A  1 271 ? 9.802   -11.951 -15.986 1.00 3.06  ? 271  ARG A NH1 1 
ATOM   2116  N  NH2 . ARG A  1 271 ? 11.830  -11.581 -14.989 1.00 3.05  ? 271  ARG A NH2 1 
ATOM   2117  N  N   . GLU A  1 272 ? 6.361   -4.995  -18.156 1.00 3.60  ? 272  GLU A N   1 
ATOM   2118  C  CA  . GLU A  1 272 ? 5.204   -4.566  -18.934 1.00 3.07  ? 272  GLU A CA  1 
ATOM   2119  C  C   . GLU A  1 272 ? 5.565   -3.396  -19.821 1.00 2.09  ? 272  GLU A C   1 
ATOM   2120  O  O   . GLU A  1 272 ? 5.199   -3.360  -20.993 1.00 2.00  ? 272  GLU A O   1 
ATOM   2121  C  CB  . GLU A  1 272 ? 4.051   -4.180  -18.002 1.00 2.44  ? 272  GLU A CB  1 
ATOM   2122  C  CG  . GLU A  1 272 ? 2.742   -3.877  -18.702 1.00 2.00  ? 272  GLU A CG  1 
ATOM   2123  C  CD  . GLU A  1 272 ? 2.475   -4.804  -19.866 1.00 3.76  ? 272  GLU A CD  1 
ATOM   2124  O  OE1 . GLU A  1 272 ? 3.241   -5.770  -20.051 1.00 2.65  ? 272  GLU A OE1 1 
ATOM   2125  O  OE2 . GLU A  1 272 ? 1.494   -4.569  -20.605 1.00 6.19  ? 272  GLU A OE2 1 
ATOM   2126  N  N   . HIS A  1 273 ? 6.296   -2.446  -19.245 1.00 2.73  ? 273  HIS A N   1 
ATOM   2127  C  CA  . HIS A  1 273 ? 6.725   -1.256  -19.964 1.00 3.30  ? 273  HIS A CA  1 
ATOM   2128  C  C   . HIS A  1 273 ? 7.611   -1.581  -21.159 1.00 4.48  ? 273  HIS A C   1 
ATOM   2129  O  O   . HIS A  1 273 ? 7.239   -1.294  -22.297 1.00 7.71  ? 273  HIS A O   1 
ATOM   2130  C  CB  . HIS A  1 273 ? 7.471   -0.322  -19.030 1.00 2.00  ? 273  HIS A CB  1 
ATOM   2131  C  CG  . HIS A  1 273 ? 8.068   0.861   -19.718 1.00 2.00  ? 273  HIS A CG  1 
ATOM   2132  N  ND1 . HIS A  1 273 ? 7.595   2.142   -19.541 1.00 2.00  ? 273  HIS A ND1 1 
ATOM   2133  C  CD2 . HIS A  1 273 ? 9.117   0.963   -20.566 1.00 2.41  ? 273  HIS A CD2 1 
ATOM   2134  C  CE1 . HIS A  1 273 ? 8.328   2.984   -20.246 1.00 2.00  ? 273  HIS A CE1 1 
ATOM   2135  N  NE2 . HIS A  1 273 ? 9.259   2.293   -20.878 1.00 2.19  ? 273  HIS A NE2 1 
ATOM   2136  N  N   . ASN A  1 274 ? 8.783   -2.162  -20.913 1.00 3.39  ? 274  ASN A N   1 
ATOM   2137  C  CA  . ASN A  1 274 ? 9.685   -2.506  -22.012 1.00 2.00  ? 274  ASN A CA  1 
ATOM   2138  C  C   . ASN A  1 274 ? 8.963   -3.211  -23.147 1.00 2.00  ? 274  ASN A C   1 
ATOM   2139  O  O   . ASN A  1 274 ? 9.328   -3.069  -24.305 1.00 2.00  ? 274  ASN A O   1 
ATOM   2140  C  CB  . ASN A  1 274 ? 10.811  -3.417  -21.541 1.00 2.00  ? 274  ASN A CB  1 
ATOM   2141  C  CG  . ASN A  1 274 ? 11.789  -2.714  -20.644 1.00 2.13  ? 274  ASN A CG  1 
ATOM   2142  O  OD1 . ASN A  1 274 ? 11.858  -1.484  -20.614 1.00 2.00  ? 274  ASN A OD1 1 
ATOM   2143  N  ND2 . ASN A  1 274 ? 12.573  -3.495  -19.913 1.00 3.68  ? 274  ASN A ND2 1 
ATOM   2144  N  N   . ARG A  1 275 ? 7.946   -3.987  -22.812 1.00 2.00  ? 275  ARG A N   1 
ATOM   2145  C  CA  . ARG A  1 275 ? 7.206   -4.706  -23.827 1.00 2.00  ? 275  ARG A CA  1 
ATOM   2146  C  C   . ARG A  1 275 ? 6.513   -3.682  -24.703 1.00 2.00  ? 275  ARG A C   1 
ATOM   2147  O  O   . ARG A  1 275 ? 6.757   -3.611  -25.896 1.00 2.00  ? 275  ARG A O   1 
ATOM   2148  C  CB  . ARG A  1 275 ? 6.177   -5.610  -23.164 1.00 2.00  ? 275  ARG A CB  1 
ATOM   2149  C  CG  . ARG A  1 275 ? 5.696   -6.754  -24.012 1.00 2.00  ? 275  ARG A CG  1 
ATOM   2150  C  CD  . ARG A  1 275 ? 4.427   -7.325  -23.414 1.00 4.54  ? 275  ARG A CD  1 
ATOM   2151  N  NE  . ARG A  1 275 ? 3.264   -6.925  -24.196 1.00 6.59  ? 275  ARG A NE  1 
ATOM   2152  C  CZ  . ARG A  1 275 ? 2.064   -6.658  -23.691 1.00 6.80  ? 275  ARG A CZ  1 
ATOM   2153  N  NH1 . ARG A  1 275 ? 1.846   -6.740  -22.388 1.00 7.45  ? 275  ARG A NH1 1 
ATOM   2154  N  NH2 . ARG A  1 275 ? 1.077   -6.314  -24.503 1.00 8.03  ? 275  ARG A NH2 1 
ATOM   2155  N  N   . LEU A  1 276 ? 5.655   -2.879  -24.083 1.00 2.21  ? 276  LEU A N   1 
ATOM   2156  C  CA  . LEU A  1 276 ? 4.890   -1.846  -24.769 1.00 2.00  ? 276  LEU A CA  1 
ATOM   2157  C  C   . LEU A  1 276 ? 5.762   -0.963  -25.637 1.00 2.00  ? 276  LEU A C   1 
ATOM   2158  O  O   . LEU A  1 276 ? 5.466   -0.770  -26.808 1.00 2.75  ? 276  LEU A O   1 
ATOM   2159  C  CB  . LEU A  1 276 ? 4.143   -1.000  -23.741 1.00 2.00  ? 276  LEU A CB  1 
ATOM   2160  C  CG  . LEU A  1 276 ? 2.816   -1.508  -23.168 1.00 2.00  ? 276  LEU A CG  1 
ATOM   2161  C  CD1 . LEU A  1 276 ? 2.814   -3.014  -23.061 1.00 2.60  ? 276  LEU A CD1 1 
ATOM   2162  C  CD2 . LEU A  1 276 ? 2.593   -0.867  -21.811 1.00 2.00  ? 276  LEU A CD2 1 
ATOM   2163  N  N   . ALA A  1 277 ? 6.828   -0.418  -25.066 1.00 2.00  ? 277  ALA A N   1 
ATOM   2164  C  CA  . ALA A  1 277 ? 7.737   0.427   -25.826 1.00 2.00  ? 277  ALA A CA  1 
ATOM   2165  C  C   . ALA A  1 277 ? 8.217   -0.344  -27.060 1.00 2.89  ? 277  ALA A C   1 
ATOM   2166  O  O   . ALA A  1 277 ? 8.118   0.124   -28.192 1.00 3.09  ? 277  ALA A O   1 
ATOM   2167  C  CB  . ALA A  1 277 ? 8.920   0.815   -24.966 1.00 2.00  ? 277  ALA A CB  1 
ATOM   2168  N  N   . ARG A  1 278 ? 8.732   -1.541  -26.831 1.00 4.29  ? 278  ARG A N   1 
ATOM   2169  C  CA  . ARG A  1 278 ? 9.220   -2.372  -27.920 1.00 4.67  ? 278  ARG A CA  1 
ATOM   2170  C  C   . ARG A  1 278 ? 8.094   -2.532  -28.930 1.00 3.78  ? 278  ARG A C   1 
ATOM   2171  O  O   . ARG A  1 278 ? 8.217   -2.129  -30.081 1.00 2.43  ? 278  ARG A O   1 
ATOM   2172  C  CB  . ARG A  1 278 ? 9.656   -3.735  -27.371 1.00 5.73  ? 278  ARG A CB  1 
ATOM   2173  C  CG  . ARG A  1 278 ? 10.902  -4.270  -28.023 1.00 7.61  ? 278  ARG A CG  1 
ATOM   2174  C  CD  . ARG A  1 278 ? 11.453  -5.452  -27.273 1.00 10.29 ? 278  ARG A CD  1 
ATOM   2175  N  NE  . ARG A  1 278 ? 12.084  -5.082  -26.009 1.00 13.32 ? 278  ARG A NE  1 
ATOM   2176  C  CZ  . ARG A  1 278 ? 11.608  -5.415  -24.812 1.00 15.59 ? 278  ARG A CZ  1 
ATOM   2177  N  NH1 . ARG A  1 278 ? 10.486  -6.117  -24.713 1.00 16.71 ? 278  ARG A NH1 1 
ATOM   2178  N  NH2 . ARG A  1 278 ? 12.273  -5.085  -23.711 1.00 16.67 ? 278  ARG A NH2 1 
ATOM   2179  N  N   . GLU A  1 279 ? 6.994   -3.112  -28.471 1.00 5.50  ? 279  GLU A N   1 
ATOM   2180  C  CA  . GLU A  1 279 ? 5.816   -3.338  -29.290 1.00 7.11  ? 279  GLU A CA  1 
ATOM   2181  C  C   . GLU A  1 279 ? 5.414   -2.114  -30.100 1.00 9.59  ? 279  GLU A C   1 
ATOM   2182  O  O   . GLU A  1 279 ? 5.243   -2.199  -31.316 1.00 11.85 ? 279  GLU A O   1 
ATOM   2183  C  CB  . GLU A  1 279 ? 4.644   -3.714  -28.410 1.00 9.84  ? 279  GLU A CB  1 
ATOM   2184  C  CG  . GLU A  1 279 ? 3.386   -3.933  -29.191 1.00 14.47 ? 279  GLU A CG  1 
ATOM   2185  C  CD  . GLU A  1 279 ? 3.325   -5.322  -29.773 1.00 17.45 ? 279  GLU A CD  1 
ATOM   2186  O  OE1 . GLU A  1 279 ? 4.329   -5.747  -30.387 1.00 19.07 ? 279  GLU A OE1 1 
ATOM   2187  O  OE2 . GLU A  1 279 ? 2.272   -5.986  -29.610 1.00 20.35 ? 279  GLU A OE2 1 
ATOM   2188  N  N   . LEU A  1 280 ? 5.229   -0.987  -29.415 1.00 8.95  ? 280  LEU A N   1 
ATOM   2189  C  CA  . LEU A  1 280 ? 4.845   0.261   -30.073 1.00 8.44  ? 280  LEU A CA  1 
ATOM   2190  C  C   . LEU A  1 280 ? 5.844   0.617   -31.162 1.00 9.61  ? 280  LEU A C   1 
ATOM   2191  O  O   . LEU A  1 280 ? 5.459   1.042   -32.246 1.00 10.09 ? 280  LEU A O   1 
ATOM   2192  C  CB  . LEU A  1 280 ? 4.790   1.415   -29.069 1.00 6.74  ? 280  LEU A CB  1 
ATOM   2193  C  CG  . LEU A  1 280 ? 3.791   1.333   -27.917 1.00 6.15  ? 280  LEU A CG  1 
ATOM   2194  C  CD1 . LEU A  1 280 ? 4.275   2.238   -26.802 1.00 4.44  ? 280  LEU A CD1 1 
ATOM   2195  C  CD2 . LEU A  1 280 ? 2.388   1.710   -28.386 1.00 4.94  ? 280  LEU A CD2 1 
ATOM   2196  N  N   . LYS A  1 281 ? 7.130   0.442   -30.876 1.00 10.16 ? 281  LYS A N   1 
ATOM   2197  C  CA  . LYS A  1 281 ? 8.158   0.768   -31.854 1.00 11.17 ? 281  LYS A CA  1 
ATOM   2198  C  C   . LYS A  1 281 ? 7.965   0.119   -33.219 1.00 12.45 ? 281  LYS A C   1 
ATOM   2199  O  O   . LYS A  1 281 ? 8.153   0.779   -34.234 1.00 11.52 ? 281  LYS A O   1 
ATOM   2200  C  CB  . LYS A  1 281 ? 9.538   0.398   -31.325 1.00 12.20 ? 281  LYS A CB  1 
ATOM   2201  C  CG  . LYS A  1 281 ? 10.631  0.460   -32.386 1.00 11.92 ? 281  LYS A CG  1 
ATOM   2202  C  CD  . LYS A  1 281 ? 10.905  1.879   -32.818 1.00 12.04 ? 281  LYS A CD  1 
ATOM   2203  C  CE  . LYS A  1 281 ? 12.209  1.974   -33.584 1.00 11.72 ? 281  LYS A CE  1 
ATOM   2204  N  NZ  . LYS A  1 281 ? 12.621  3.399   -33.729 1.00 12.62 ? 281  LYS A NZ  1 
ATOM   2205  N  N   . ARG A  1 282 ? 7.605   -1.164  -33.265 1.00 16.06 ? 282  ARG A N   1 
ATOM   2206  C  CA  . ARG A  1 282 ? 7.427   -1.800  -34.568 1.00 19.60 ? 282  ARG A CA  1 
ATOM   2207  C  C   . ARG A  1 282 ? 6.159   -1.372  -35.273 1.00 19.42 ? 282  ARG A C   1 
ATOM   2208  O  O   . ARG A  1 282 ? 6.140   -1.275  -36.501 1.00 20.53 ? 282  ARG A O   1 
ATOM   2209  C  CB  . ARG A  1 282 ? 7.499   -3.333  -34.490 1.00 22.85 ? 282  ARG A CB  1 
ATOM   2210  C  CG  . ARG A  1 282 ? 6.580   -4.055  -33.526 1.00 28.27 ? 282  ARG A CG  1 
ATOM   2211  C  CD  . ARG A  1 282 ? 6.901   -5.556  -33.625 1.00 33.41 ? 282  ARG A CD  1 
ATOM   2212  N  NE  . ARG A  1 282 ? 6.542   -6.324  -32.434 1.00 38.99 ? 282  ARG A NE  1 
ATOM   2213  C  CZ  . ARG A  1 282 ? 7.128   -7.467  -32.078 1.00 40.79 ? 282  ARG A CZ  1 
ATOM   2214  N  NH1 . ARG A  1 282 ? 8.104   -7.974  -32.824 1.00 42.61 ? 282  ARG A NH1 1 
ATOM   2215  N  NH2 . ARG A  1 282 ? 6.744   -8.098  -30.972 1.00 42.16 ? 282  ARG A NH2 1 
ATOM   2216  N  N   . LEU A  1 283 ? 5.100   -1.109  -34.514 1.00 18.77 ? 283  LEU A N   1 
ATOM   2217  C  CA  . LEU A  1 283 ? 3.866   -0.647  -35.137 1.00 16.94 ? 283  LEU A CA  1 
ATOM   2218  C  C   . LEU A  1 283 ? 4.032   0.810   -35.558 1.00 15.58 ? 283  LEU A C   1 
ATOM   2219  O  O   . LEU A  1 283 ? 3.358   1.279   -36.470 1.00 15.76 ? 283  LEU A O   1 
ATOM   2220  C  CB  . LEU A  1 283 ? 2.676   -0.772  -34.187 1.00 17.55 ? 283  LEU A CB  1 
ATOM   2221  C  CG  . LEU A  1 283 ? 1.675   -1.874  -34.562 1.00 19.93 ? 283  LEU A CG  1 
ATOM   2222  C  CD1 . LEU A  1 283 ? 0.347   -1.592  -33.870 1.00 20.36 ? 283  LEU A CD1 1 
ATOM   2223  C  CD2 . LEU A  1 283 ? 1.462   -1.923  -36.082 1.00 20.30 ? 283  LEU A CD2 1 
ATOM   2224  N  N   . ASN A  1 284 ? 4.942   1.513   -34.889 1.00 13.91 ? 284  ASN A N   1 
ATOM   2225  C  CA  . ASN A  1 284 ? 5.225   2.917   -35.177 1.00 12.04 ? 284  ASN A CA  1 
ATOM   2226  C  C   . ASN A  1 284 ? 6.730   3.119   -35.310 1.00 11.02 ? 284  ASN A C   1 
ATOM   2227  O  O   . ASN A  1 284 ? 7.367   3.752   -34.467 1.00 11.31 ? 284  ASN A O   1 
ATOM   2228  C  CB  . ASN A  1 284 ? 4.686   3.813   -34.058 1.00 12.72 ? 284  ASN A CB  1 
ATOM   2229  C  CG  . ASN A  1 284 ? 3.178   3.980   -34.113 1.00 13.31 ? 284  ASN A CG  1 
ATOM   2230  O  OD1 . ASN A  1 284 ? 2.434   3.008   -34.274 1.00 14.76 ? 284  ASN A OD1 1 
ATOM   2231  N  ND2 . ASN A  1 284 ? 2.717   5.217   -33.968 1.00 13.09 ? 284  ASN A ND2 1 
ATOM   2232  N  N   . PRO A  1 285 ? 7.316   2.580   -36.384 1.00 10.94 ? 285  PRO A N   1 
ATOM   2233  C  CA  . PRO A  1 285 ? 8.747   2.650   -36.708 1.00 12.63 ? 285  PRO A CA  1 
ATOM   2234  C  C   . PRO A  1 285 ? 9.464   4.004   -36.524 1.00 11.51 ? 285  PRO A C   1 
ATOM   2235  O  O   . PRO A  1 285 ? 10.594  4.069   -36.031 1.00 10.27 ? 285  PRO A O   1 
ATOM   2236  C  CB  . PRO A  1 285 ? 8.779   2.167   -38.158 1.00 12.03 ? 285  PRO A CB  1 
ATOM   2237  C  CG  . PRO A  1 285 ? 7.704   1.117   -38.165 1.00 11.81 ? 285  PRO A CG  1 
ATOM   2238  C  CD  . PRO A  1 285 ? 6.586   1.789   -37.394 1.00 11.13 ? 285  PRO A CD  1 
ATOM   2239  N  N   . HIS A  1 286 ? 8.794   5.081   -36.905 1.00 12.54 ? 286  HIS A N   1 
ATOM   2240  C  CA  . HIS A  1 286 ? 9.411   6.414   -36.868 1.00 13.77 ? 286  HIS A CA  1 
ATOM   2241  C  C   . HIS A  1 286 ? 9.222   7.180   -35.536 1.00 14.16 ? 286  HIS A C   1 
ATOM   2242  O  O   . HIS A  1 286 ? 9.603   8.352   -35.455 1.00 15.88 ? 286  HIS A O   1 
ATOM   2243  C  CB  . HIS A  1 286 ? 8.832   7.273   -37.986 1.00 14.30 ? 286  HIS A CB  1 
ATOM   2244  C  CG  . HIS A  1 286 ? 7.290   7.400   -37.787 1.00 15.49 ? 286  HIS A CG  1 
ATOM   2245  N  ND1 . HIS A  1 286 ? 6.439   6.328   -37.956 1.00 15.89 ? 286  HIS A ND1 1 
ATOM   2246  C  CD2 . HIS A  1 286 ? 6.512   8.447   -37.424 1.00 16.49 ? 286  HIS A CD2 1 
ATOM   2247  C  CE1 . HIS A  1 286 ? 5.200   6.710   -37.704 1.00 17.41 ? 286  HIS A CE1 1 
ATOM   2248  N  NE2 . HIS A  1 286 ? 5.216   7.991   -37.378 1.00 18.07 ? 286  HIS A NE2 1 
ATOM   2249  N  N   . TRP A  1 287 ? 8.654   6.574   -34.493 1.00 13.74 ? 287  TRP A N   1 
ATOM   2250  C  CA  . TRP A  1 287 ? 8.455   7.304   -33.226 1.00 12.49 ? 287  TRP A CA  1 
ATOM   2251  C  C   . TRP A  1 287 ? 9.765   7.593   -32.527 1.00 11.64 ? 287  TRP A C   1 
ATOM   2252  O  O   . TRP A  1 287 ? 10.841  7.162   -32.954 1.00 12.55 ? 287  TRP A O   1 
ATOM   2253  C  CB  . TRP A  1 287 ? 7.514   6.589   -32.270 1.00 10.41 ? 287  TRP A CB  1 
ATOM   2254  C  CG  . TRP A  1 287 ? 6.104   7.052   -32.452 1.00 10.08 ? 287  TRP A CG  1 
ATOM   2255  C  CD1 . TRP A  1 287 ? 5.636   7.924   -33.390 1.00 11.10 ? 287  TRP A CD1 1 
ATOM   2256  C  CD2 . TRP A  1 287 ? 4.956   6.637   -31.689 1.00 10.51 ? 287  TRP A CD2 1 
ATOM   2257  N  NE1 . TRP A  1 287 ? 4.275   8.081   -33.264 1.00 11.54 ? 287  TRP A NE1 1 
ATOM   2258  C  CE2 . TRP A  1 287 ? 3.832   7.303   -32.229 1.00 10.69 ? 287  TRP A CE2 1 
ATOM   2259  C  CE3 . TRP A  1 287 ? 4.768   5.770   -30.606 1.00 10.71 ? 287  TRP A CE3 1 
ATOM   2260  C  CZ2 . TRP A  1 287 ? 2.538   7.130   -31.724 1.00 10.58 ? 287  TRP A CZ2 1 
ATOM   2261  C  CZ3 . TRP A  1 287 ? 3.476   5.597   -30.103 1.00 10.39 ? 287  TRP A CZ3 1 
ATOM   2262  C  CH2 . TRP A  1 287 ? 2.382   6.276   -30.664 1.00 11.10 ? 287  TRP A CH2 1 
ATOM   2263  N  N   . ASP A  1 288 ? 9.686   8.313   -31.433 1.00 11.43 ? 288  ASP A N   1 
ATOM   2264  C  CA  . ASP A  1 288 ? 10.875  8.762   -30.743 1.00 11.27 ? 288  ASP A CA  1 
ATOM   2265  C  C   . ASP A  1 288 ? 11.236  7.945   -29.523 1.00 9.71  ? 288  ASP A C   1 
ATOM   2266  O  O   . ASP A  1 288 ? 10.362  7.331   -28.902 1.00 7.87  ? 288  ASP A O   1 
ATOM   2267  C  CB  . ASP A  1 288 ? 10.661  10.215  -30.318 1.00 14.62 ? 288  ASP A CB  1 
ATOM   2268  C  CG  . ASP A  1 288 ? 11.941  10.979  -30.281 1.00 17.66 ? 288  ASP A CG  1 
ATOM   2269  O  OD1 . ASP A  1 288 ? 12.985  10.429  -30.663 1.00 18.94 ? 288  ASP A OD1 1 
ATOM   2270  O  OD2 . ASP A  1 288 ? 11.898  12.155  -29.858 1.00 18.82 ? 288  ASP A OD2 1 
ATOM   2271  N  N   . GLY A  1 289 ? 12.506  7.939   -29.178 1.00 9.78  ? 289  GLY A N   1 
ATOM   2272  C  CA  . GLY A  1 289 ? 12.919  7.183   -28.031 1.00 10.55 ? 289  GLY A CA  1 
ATOM   2273  C  C   . GLY A  1 289 ? 12.047  7.662   -26.917 1.00 11.43 ? 289  GLY A C   1 
ATOM   2274  O  O   . GLY A  1 289 ? 11.517  6.925   -26.078 1.00 13.61 ? 289  GLY A O   1 
ATOM   2275  N  N   . GLU A  1 290 ? 11.939  9.010   -26.960 1.00 10.58 ? 290  GLU A N   1 
ATOM   2276  C  CA  . GLU A  1 290 ? 11.121  9.718   -25.987 1.00 8.99  ? 290  GLU A CA  1 
ATOM   2277  C  C   . GLU A  1 290 ? 9.633   9.495   -26.191 1.00 7.58  ? 290  GLU A C   1 
ATOM   2278  O  O   . GLU A  1 290 ? 8.965   9.206   -25.193 1.00 7.91  ? 290  GLU A O   1 
ATOM   2279  C  CB  . GLU A  1 290 ? 11.477  11.225  -25.826 1.00 10.21 ? 290  GLU A CB  1 
ATOM   2280  C  CG  . GLU A  1 290 ? 10.462  12.080  -25.005 1.00 12.52 ? 290  GLU A CG  1 
ATOM   2281  C  CD  . GLU A  1 290 ? 10.645  12.195  -23.472 1.00 13.62 ? 290  GLU A CD  1 
ATOM   2282  O  OE1 . GLU A  1 290 ? 11.220  11.268  -22.868 1.00 15.61 ? 290  GLU A OE1 1 
ATOM   2283  O  OE2 . GLU A  1 290 ? 10.199  13.219  -22.897 1.00 15.67 ? 290  GLU A OE2 1 
ATOM   2284  N  N   . LYS A  1 291 ? 9.096   9.598   -27.407 1.00 5.49  ? 291  LYS A N   1 
ATOM   2285  C  CA  . LYS A  1 291 ? 7.651   9.329   -27.635 1.00 4.04  ? 291  LYS A CA  1 
ATOM   2286  C  C   . LYS A  1 291 ? 7.311   7.928   -27.091 1.00 3.57  ? 291  LYS A C   1 
ATOM   2287  O  O   . LYS A  1 291 ? 6.206   7.708   -26.560 1.00 2.00  ? 291  LYS A O   1 
ATOM   2288  C  CB  . LYS A  1 291 ? 7.339   9.403   -29.136 1.00 2.59  ? 291  LYS A CB  1 
ATOM   2289  C  CG  . LYS A  1 291 ? 5.851   9.427   -29.450 1.00 2.00  ? 291  LYS A CG  1 
ATOM   2290  C  CD  . LYS A  1 291 ? 5.246   10.737  -29.013 1.00 2.25  ? 291  LYS A CD  1 
ATOM   2291  C  CE  . LYS A  1 291 ? 3.894   10.927  -29.663 1.00 4.21  ? 291  LYS A CE  1 
ATOM   2292  N  NZ  . LYS A  1 291 ? 2.955   9.827   -29.307 1.00 6.53  ? 291  LYS A NZ  1 
ATOM   2293  N  N   . LEU A  1 292 ? 8.242   6.990   -27.252 1.00 3.78  ? 292  LEU A N   1 
ATOM   2294  C  CA  . LEU A  1 292 ? 8.035   5.606   -26.771 1.00 4.32  ? 292  LEU A CA  1 
ATOM   2295  C  C   . LEU A  1 292 ? 7.636   5.632   -25.281 1.00 5.89  ? 292  LEU A C   1 
ATOM   2296  O  O   . LEU A  1 292 ? 6.571   5.096   -24.945 1.00 7.64  ? 292  LEU A O   1 
ATOM   2297  C  CB  . LEU A  1 292 ? 9.244   4.720   -27.136 1.00 3.57  ? 292  LEU A CB  1 
ATOM   2298  C  CG  . LEU A  1 292 ? 9.207   4.074   -28.558 1.00 3.20  ? 292  LEU A CG  1 
ATOM   2299  C  CD1 . LEU A  1 292 ? 8.168   4.755   -29.447 1.00 2.00  ? 292  LEU A CD1 1 
ATOM   2300  C  CD2 . LEU A  1 292 ? 10.585  4.127   -29.211 1.00 3.43  ? 292  LEU A CD2 1 
ATOM   2301  N  N   . TYR A  1 293 ? 8.438   6.251   -24.359 1.00 4.29  ? 293  TYR A N   1 
ATOM   2302  C  CA  . TYR A  1 293 ? 8.062   6.407   -22.920 1.00 3.64  ? 293  TYR A CA  1 
ATOM   2303  C  C   . TYR A  1 293 ? 6.865   7.348   -22.921 1.00 4.18  ? 293  TYR A C   1 
ATOM   2304  O  O   . TYR A  1 293 ? 6.675   8.112   -23.864 1.00 5.79  ? 293  TYR A O   1 
ATOM   2305  C  CB  . TYR A  1 293 ? 9.319   6.901   -22.131 1.00 3.74  ? 293  TYR A CB  1 
ATOM   2306  C  CG  . TYR A  1 293 ? 9.285   7.440   -20.697 1.00 4.42  ? 293  TYR A CG  1 
ATOM   2307  C  CD1 . TYR A  1 293 ? 9.543   6.607   -19.616 1.00 5.54  ? 293  TYR A CD1 1 
ATOM   2308  C  CD2 . TYR A  1 293 ? 9.068   8.799   -20.420 1.00 6.83  ? 293  TYR A CD2 1 
ATOM   2309  C  CE1 . TYR A  1 293 ? 9.594   7.076   -18.323 1.00 7.27  ? 293  TYR A CE1 1 
ATOM   2310  C  CE2 . TYR A  1 293 ? 9.145   9.285   -19.127 1.00 8.59  ? 293  TYR A CE2 1 
ATOM   2311  C  CZ  . TYR A  1 293 ? 9.410   8.433   -18.068 1.00 8.41  ? 293  TYR A CZ  1 
ATOM   2312  O  OH  . TYR A  1 293 ? 9.499   8.938   -16.790 1.00 10.73 ? 293  TYR A OH  1 
ATOM   2313  N  N   . GLN A  1 294 ? 6.062   7.283   -21.930 1.00 4.46  ? 294  GLN A N   1 
ATOM   2314  C  CA  . GLN A  1 294 ? 4.810   8.048   -21.858 1.00 4.17  ? 294  GLN A CA  1 
ATOM   2315  C  C   . GLN A  1 294 ? 3.742   7.734   -22.944 1.00 4.99  ? 294  GLN A C   1 
ATOM   2316  O  O   . GLN A  1 294 ? 2.595   8.160   -22.774 1.00 4.95  ? 294  GLN A O   1 
ATOM   2317  C  CB  . GLN A  1 294 ? 5.015   9.601   -21.727 1.00 3.57  ? 294  GLN A CB  1 
ATOM   2318  C  CG  . GLN A  1 294 ? 6.392   10.183  -22.064 1.00 4.08  ? 294  GLN A CG  1 
ATOM   2319  C  CD  . GLN A  1 294 ? 6.900   11.243  -21.103 1.00 3.24  ? 294  GLN A CD  1 
ATOM   2320  O  OE1 . GLN A  1 294 ? 6.202   11.652  -20.166 1.00 5.69  ? 294  GLN A OE1 1 
ATOM   2321  N  NE2 . GLN A  1 294 ? 8.075   11.829  -21.155 1.00 3.02  ? 294  GLN A NE2 1 
ATOM   2322  N  N   . GLU A  1 295 ? 4.010   7.005   -24.064 1.00 3.69  ? 295  GLU A N   1 
ATOM   2323  C  CA  . GLU A  1 295 ? 2.907   6.528   -24.840 1.00 2.10  ? 295  GLU A CA  1 
ATOM   2324  C  C   . GLU A  1 295 ? 2.667   5.191   -24.203 1.00 2.00  ? 295  GLU A C   1 
ATOM   2325  O  O   . GLU A  1 295 ? 1.556   4.676   -24.130 1.00 3.56  ? 295  GLU A O   1 
ATOM   2326  C  CB  . GLU A  1 295 ? 3.249   6.422   -26.325 1.00 2.49  ? 295  GLU A CB  1 
ATOM   2327  C  CG  . GLU A  1 295 ? 2.648   7.511   -27.190 1.00 4.03  ? 295  GLU A CG  1 
ATOM   2328  C  CD  . GLU A  1 295 ? 1.130   7.498   -27.167 1.00 5.97  ? 295  GLU A CD  1 
ATOM   2329  O  OE1 . GLU A  1 295 ? 0.549   6.474   -26.733 1.00 7.20  ? 295  GLU A OE1 1 
ATOM   2330  O  OE2 . GLU A  1 295 ? 0.518   8.497   -27.597 1.00 5.15  ? 295  GLU A OE2 1 
ATOM   2331  N  N   . ALA A  1 296 ? 3.793   4.667   -23.741 1.00 2.00  ? 296  ALA A N   1 
ATOM   2332  C  CA  . ALA A  1 296 ? 3.697   3.390   -23.046 1.00 2.00  ? 296  ALA A CA  1 
ATOM   2333  C  C   . ALA A  1 296 ? 3.303   3.707   -21.617 1.00 2.81  ? 296  ALA A C   1 
ATOM   2334  O  O   . ALA A  1 296 ? 2.341   3.145   -21.088 1.00 4.62  ? 296  ALA A O   1 
ATOM   2335  C  CB  . ALA A  1 296 ? 5.031   2.685   -23.062 1.00 2.00  ? 296  ALA A CB  1 
ATOM   2336  N  N   . ARG A  1 297 ? 4.064   4.609   -20.998 1.00 2.75  ? 297  ARG A N   1 
ATOM   2337  C  CA  . ARG A  1 297 ? 3.793   5.042   -19.632 1.00 2.00  ? 297  ARG A CA  1 
ATOM   2338  C  C   . ARG A  1 297 ? 2.323   5.447   -19.491 1.00 3.62  ? 297  ARG A C   1 
ATOM   2339  O  O   . ARG A  1 297 ? 1.751   5.379   -18.395 1.00 4.49  ? 297  ARG A O   1 
ATOM   2340  C  CB  . ARG A  1 297 ? 4.695   6.221   -19.259 1.00 2.00  ? 297  ARG A CB  1 
ATOM   2341  C  CG  . ARG A  1 297 ? 4.267   6.995   -18.011 1.00 2.00  ? 297  ARG A CG  1 
ATOM   2342  C  CD  . ARG A  1 297 ? 5.460   7.727   -17.403 1.00 2.15  ? 297  ARG A CD  1 
ATOM   2343  N  NE  . ARG A  1 297 ? 5.110   8.627   -16.306 1.00 2.31  ? 297  ARG A NE  1 
ATOM   2344  C  CZ  . ARG A  1 297 ? 4.741   9.894   -16.467 1.00 2.32  ? 297  ARG A CZ  1 
ATOM   2345  N  NH1 . ARG A  1 297 ? 4.670   10.416  -17.682 1.00 3.22  ? 297  ARG A NH1 1 
ATOM   2346  N  NH2 . ARG A  1 297 ? 4.465   10.648  -15.413 1.00 2.00  ? 297  ARG A NH2 1 
ATOM   2347  N  N   . LYS A  1 298 ? 1.704   5.869   -20.591 1.00 2.00  ? 298  LYS A N   1 
ATOM   2348  C  CA  . LYS A  1 298 ? 0.306   6.241   -20.515 1.00 2.00  ? 298  LYS A CA  1 
ATOM   2349  C  C   . LYS A  1 298 ? -0.465  4.933   -20.475 1.00 2.15  ? 298  LYS A C   1 
ATOM   2350  O  O   . LYS A  1 298 ? -1.301  4.715   -19.596 1.00 2.78  ? 298  LYS A O   1 
ATOM   2351  C  CB  . LYS A  1 298 ? -0.108  7.087   -21.723 1.00 3.39  ? 298  LYS A CB  1 
ATOM   2352  C  CG  . LYS A  1 298 ? -1.372  7.935   -21.476 1.00 3.49  ? 298  LYS A CG  1 
ATOM   2353  C  CD  . LYS A  1 298 ? -1.290  9.294   -22.161 1.00 2.00  ? 298  LYS A CD  1 
ATOM   2354  C  CE  . LYS A  1 298 ? -2.274  9.401   -23.289 1.00 2.00  ? 298  LYS A CE  1 
ATOM   2355  N  NZ  . LYS A  1 298 ? -1.560  9.963   -24.456 1.00 4.52  ? 298  LYS A NZ  1 
ATOM   2356  N  N   . ILE A  1 299 ? -0.153  4.056   -21.422 1.00 2.00  ? 299  ILE A N   1 
ATOM   2357  C  CA  . ILE A  1 299 ? -0.794  2.749   -21.505 1.00 2.83  ? 299  ILE A CA  1 
ATOM   2358  C  C   . ILE A  1 299 ? -0.728  2.038   -20.144 1.00 2.31  ? 299  ILE A C   1 
ATOM   2359  O  O   . ILE A  1 299 ? -1.695  1.401   -19.713 1.00 2.00  ? 299  ILE A O   1 
ATOM   2360  C  CB  . ILE A  1 299 ? -0.105  1.853   -22.612 1.00 2.16  ? 299  ILE A CB  1 
ATOM   2361  C  CG1 . ILE A  1 299 ? -0.601  2.253   -24.007 1.00 2.08  ? 299  ILE A CG1 1 
ATOM   2362  C  CG2 . ILE A  1 299 ? -0.393  0.373   -22.376 1.00 2.82  ? 299  ILE A CG2 1 
ATOM   2363  C  CD1 . ILE A  1 299 ? -0.005  1.423   -25.144 1.00 2.00  ? 299  ILE A CD1 1 
ATOM   2364  N  N   . LEU A  1 300 ? 0.400   2.176   -19.455 1.00 2.00  ? 300  LEU A N   1 
ATOM   2365  C  CA  . LEU A  1 300 ? 0.580   1.503   -18.182 1.00 2.00  ? 300  LEU A CA  1 
ATOM   2366  C  C   . LEU A  1 300 ? -0.258  2.052   -17.031 1.00 2.89  ? 300  LEU A C   1 
ATOM   2367  O  O   . LEU A  1 300 ? -0.911  1.284   -16.325 1.00 3.17  ? 300  LEU A O   1 
ATOM   2368  C  CB  . LEU A  1 300 ? 2.066   1.486   -17.812 1.00 2.00  ? 300  LEU A CB  1 
ATOM   2369  C  CG  . LEU A  1 300 ? 2.479   0.624   -16.611 1.00 2.00  ? 300  LEU A CG  1 
ATOM   2370  C  CD1 . LEU A  1 300 ? 1.876   -0.767  -16.706 1.00 2.00  ? 300  LEU A CD1 1 
ATOM   2371  C  CD2 . LEU A  1 300 ? 3.987   0.541   -16.554 1.00 2.00  ? 300  LEU A CD2 1 
ATOM   2372  N  N   . GLY A  1 301 ? -0.247  3.366   -16.830 1.00 2.87  ? 301  GLY A N   1 
ATOM   2373  C  CA  . GLY A  1 301 ? -1.039  3.931   -15.748 1.00 2.00  ? 301  GLY A CA  1 
ATOM   2374  C  C   . GLY A  1 301 ? -2.477  3.494   -15.917 1.00 2.00  ? 301  GLY A C   1 
ATOM   2375  O  O   . GLY A  1 301 ? -3.088  2.942   -15.007 1.00 2.00  ? 301  GLY A O   1 
ATOM   2376  N  N   . ALA A  1 302 ? -3.007  3.735   -17.112 1.00 2.07  ? 302  ALA A N   1 
ATOM   2377  C  CA  . ALA A  1 302 ? -4.377  3.360   -17.453 1.00 2.73  ? 302  ALA A CA  1 
ATOM   2378  C  C   . ALA A  1 302 ? -4.641  1.916   -17.051 1.00 2.10  ? 302  ALA A C   1 
ATOM   2379  O  O   . ALA A  1 302 ? -5.757  1.547   -16.684 1.00 2.00  ? 302  ALA A O   1 
ATOM   2380  C  CB  . ALA A  1 302 ? -4.607  3.525   -18.951 1.00 2.00  ? 302  ALA A CB  1 
ATOM   2381  N  N   . PHE A  1 303 ? -3.609  1.092   -17.137 1.00 2.00  ? 303  PHE A N   1 
ATOM   2382  C  CA  . PHE A  1 303 ? -3.763  -0.292  -16.763 1.00 2.26  ? 303  PHE A CA  1 
ATOM   2383  C  C   . PHE A  1 303 ? -4.017  -0.360  -15.258 1.00 3.81  ? 303  PHE A C   1 
ATOM   2384  O  O   . PHE A  1 303 ? -4.999  -0.965  -14.822 1.00 4.97  ? 303  PHE A O   1 
ATOM   2385  C  CB  . PHE A  1 303 ? -2.512  -1.088  -17.132 1.00 2.00  ? 303  PHE A CB  1 
ATOM   2386  C  CG  . PHE A  1 303 ? -2.502  -2.476  -16.571 1.00 2.00  ? 303  PHE A CG  1 
ATOM   2387  C  CD1 . PHE A  1 303 ? -3.418  -3.423  -17.002 1.00 2.00  ? 303  PHE A CD1 1 
ATOM   2388  C  CD2 . PHE A  1 303 ? -1.607  -2.822  -15.571 1.00 2.00  ? 303  PHE A CD2 1 
ATOM   2389  C  CE1 . PHE A  1 303 ? -3.443  -4.697  -16.440 1.00 2.19  ? 303  PHE A CE1 1 
ATOM   2390  C  CE2 . PHE A  1 303 ? -1.627  -4.089  -15.006 1.00 2.00  ? 303  PHE A CE2 1 
ATOM   2391  C  CZ  . PHE A  1 303 ? -2.547  -5.028  -15.441 1.00 2.00  ? 303  PHE A CZ  1 
ATOM   2392  N  N   . ILE A  1 304 ? -3.148  0.271   -14.467 1.00 3.47  ? 304  ILE A N   1 
ATOM   2393  C  CA  . ILE A  1 304 ? -3.303  0.255   -13.011 1.00 2.60  ? 304  ILE A CA  1 
ATOM   2394  C  C   . ILE A  1 304 ? -4.726  0.680   -12.662 1.00 4.38  ? 304  ILE A C   1 
ATOM   2395  O  O   . ILE A  1 304 ? -5.497  -0.093  -12.082 1.00 5.51  ? 304  ILE A O   1 
ATOM   2396  C  CB  . ILE A  1 304 ? -2.346  1.238   -12.300 1.00 2.84  ? 304  ILE A CB  1 
ATOM   2397  C  CG1 . ILE A  1 304 ? -0.928  1.125   -12.865 1.00 2.36  ? 304  ILE A CG1 1 
ATOM   2398  C  CG2 . ILE A  1 304 ? -2.339  0.943   -10.808 1.00 2.00  ? 304  ILE A CG2 1 
ATOM   2399  C  CD1 . ILE A  1 304 ? -0.163  -0.081  -12.386 1.00 2.35  ? 304  ILE A CD1 1 
ATOM   2400  N  N   . GLN A  1 305 ? -5.066  1.913   -13.023 1.00 3.57  ? 305  GLN A N   1 
ATOM   2401  C  CA  . GLN A  1 305 ? -6.389  2.442   -12.755 1.00 2.00  ? 305  GLN A CA  1 
ATOM   2402  C  C   . GLN A  1 305 ? -7.490  1.416   -12.975 1.00 2.00  ? 305  GLN A C   1 
ATOM   2403  O  O   . GLN A  1 305 ? -8.317  1.187   -12.093 1.00 2.39  ? 305  GLN A O   1 
ATOM   2404  C  CB  . GLN A  1 305 ? -6.635  3.679   -13.616 1.00 2.00  ? 305  GLN A CB  1 
ATOM   2405  C  CG  . GLN A  1 305 ? -5.954  4.909   -13.048 1.00 3.88  ? 305  GLN A CG  1 
ATOM   2406  C  CD  . GLN A  1 305 ? -6.139  6.154   -13.891 1.00 3.24  ? 305  GLN A CD  1 
ATOM   2407  O  OE1 . GLN A  1 305 ? -6.981  6.199   -14.786 1.00 3.40  ? 305  GLN A OE1 1 
ATOM   2408  N  NE2 . GLN A  1 305 ? -5.353  7.183   -13.594 1.00 2.56  ? 305  GLN A NE2 1 
ATOM   2409  N  N   . ILE A  1 306 ? -7.495  0.769   -14.134 1.00 2.46  ? 306  ILE A N   1 
ATOM   2410  C  CA  . ILE A  1 306 ? -8.544  -0.203  -14.403 1.00 3.35  ? 306  ILE A CA  1 
ATOM   2411  C  C   . ILE A  1 306 ? -8.615  -1.335  -13.403 1.00 2.31  ? 306  ILE A C   1 
ATOM   2412  O  O   . ILE A  1 306 ? -9.626  -1.506  -12.726 1.00 3.28  ? 306  ILE A O   1 
ATOM   2413  C  CB  . ILE A  1 306 ? -8.419  -0.806  -15.792 1.00 2.00  ? 306  ILE A CB  1 
ATOM   2414  C  CG1 . ILE A  1 306 ? -8.636  0.284   -16.831 1.00 2.00  ? 306  ILE A CG1 1 
ATOM   2415  C  CG2 . ILE A  1 306 ? -9.460  -1.892  -15.970 1.00 2.00  ? 306  ILE A CG2 1 
ATOM   2416  C  CD1 . ILE A  1 306 ? -8.724  -0.230  -18.220 1.00 2.00  ? 306  ILE A CD1 1 
ATOM   2417  N  N   . ILE A  1 307 ? -7.547  -2.111  -13.317 1.00 2.00  ? 307  ILE A N   1 
ATOM   2418  C  CA  . ILE A  1 307 ? -7.508  -3.230  -12.396 1.00 2.00  ? 307  ILE A CA  1 
ATOM   2419  C  C   . ILE A  1 307 ? -7.960  -2.802  -11.001 1.00 2.45  ? 307  ILE A C   1 
ATOM   2420  O  O   . ILE A  1 307 ? -8.698  -3.525  -10.323 1.00 2.69  ? 307  ILE A O   1 
ATOM   2421  C  CB  . ILE A  1 307 ? -6.093  -3.805  -12.343 1.00 2.00  ? 307  ILE A CB  1 
ATOM   2422  C  CG1 . ILE A  1 307 ? -5.638  -4.118  -13.768 1.00 2.30  ? 307  ILE A CG1 1 
ATOM   2423  C  CG2 . ILE A  1 307 ? -6.058  -5.064  -11.480 1.00 2.12  ? 307  ILE A CG2 1 
ATOM   2424  C  CD1 . ILE A  1 307 ? -6.578  -5.066  -14.511 1.00 2.00  ? 307  ILE A CD1 1 
ATOM   2425  N  N   . THR A  1 308 ? -7.535  -1.610  -10.592 1.00 2.00  ? 308  THR A N   1 
ATOM   2426  C  CA  . THR A  1 308 ? -7.883  -1.076  -9.283  1.00 2.56  ? 308  THR A CA  1 
ATOM   2427  C  C   . THR A  1 308 ? -9.371  -0.733  -9.101  1.00 3.31  ? 308  THR A C   1 
ATOM   2428  O  O   . THR A  1 308 ? -9.954  -1.040  -8.060  1.00 4.05  ? 308  THR A O   1 
ATOM   2429  C  CB  . THR A  1 308 ? -7.022  0.168   -8.966  1.00 2.22  ? 308  THR A CB  1 
ATOM   2430  O  OG1 . THR A  1 308 ? -5.673  -0.244  -8.727  1.00 2.00  ? 308  THR A OG1 1 
ATOM   2431  C  CG2 . THR A  1 308 ? -7.546  0.901   -7.742  1.00 2.00  ? 308  THR A CG2 1 
ATOM   2432  N  N   . PHE A  1 309 ? -10.000 -0.114  -10.094 1.00 2.57  ? 309  PHE A N   1 
ATOM   2433  C  CA  . PHE A  1 309 ? -11.405 0.296   -9.900  1.00 2.00  ? 309  PHE A CA  1 
ATOM   2434  C  C   . PHE A  1 309 ? -12.332 -0.758  -10.393 1.00 2.00  ? 309  PHE A C   1 
ATOM   2435  O  O   . PHE A  1 309 ? -13.494 -0.869  -9.987  1.00 2.00  ? 309  PHE A O   1 
ATOM   2436  C  CB  . PHE A  1 309 ? -11.686 1.617   -10.579 1.00 2.00  ? 309  PHE A CB  1 
ATOM   2437  C  CG  . PHE A  1 309 ? -11.210 2.755   -9.765  1.00 2.12  ? 309  PHE A CG  1 
ATOM   2438  C  CD1 . PHE A  1 309 ? -9.864  3.103   -9.734  1.00 3.10  ? 309  PHE A CD1 1 
ATOM   2439  C  CD2 . PHE A  1 309 ? -12.108 3.498   -9.012  1.00 2.00  ? 309  PHE A CD2 1 
ATOM   2440  C  CE1 . PHE A  1 309 ? -9.420  4.174   -8.967  1.00 2.00  ? 309  PHE A CE1 1 
ATOM   2441  C  CE2 . PHE A  1 309 ? -11.680 4.563   -8.243  1.00 2.00  ? 309  PHE A CE2 1 
ATOM   2442  C  CZ  . PHE A  1 309 ? -10.331 4.905   -8.220  1.00 2.78  ? 309  PHE A CZ  1 
ATOM   2443  N  N   . ARG A  1 310 ? -11.800 -1.571  -11.272 1.00 2.93  ? 310  ARG A N   1 
ATOM   2444  C  CA  . ARG A  1 310 ? -12.625 -2.586  -11.833 1.00 2.10  ? 310  ARG A CA  1 
ATOM   2445  C  C   . ARG A  1 310 ? -12.526 -3.981  -11.198 1.00 2.50  ? 310  ARG A C   1 
ATOM   2446  O  O   . ARG A  1 310 ? -13.562 -4.669  -11.213 1.00 2.05  ? 310  ARG A O   1 
ATOM   2447  C  CB  . ARG A  1 310 ? -12.374 -2.739  -13.307 1.00 2.00  ? 310  ARG A CB  1 
ATOM   2448  C  CG  . ARG A  1 310 ? -13.298 -3.826  -13.844 1.00 2.00  ? 310  ARG A CG  1 
ATOM   2449  C  CD  . ARG A  1 310 ? -12.862 -4.345  -15.201 1.00 2.00  ? 310  ARG A CD  1 
ATOM   2450  N  NE  . ARG A  1 310 ? -11.743 -5.278  -15.130 1.00 2.22  ? 310  ARG A NE  1 
ATOM   2451  C  CZ  . ARG A  1 310 ? -11.038 -5.708  -16.177 1.00 2.00  ? 310  ARG A CZ  1 
ATOM   2452  N  NH1 . ARG A  1 310 ? -11.348 -5.294  -17.406 1.00 2.00  ? 310  ARG A NH1 1 
ATOM   2453  N  NH2 . ARG A  1 310 ? -10.040 -6.554  -15.985 1.00 2.00  ? 310  ARG A NH2 1 
ATOM   2454  N  N   . ASP A  1 311 ? -11.443 -4.463  -10.677 1.00 2.49  ? 311  ASP A N   1 
ATOM   2455  C  CA  . ASP A  1 311 ? -11.613 -5.839  -10.181 1.00 2.60  ? 311  ASP A CA  1 
ATOM   2456  C  C   . ASP A  1 311 ? -11.330 -5.808  -8.712  1.00 2.00  ? 311  ASP A C   1 
ATOM   2457  O  O   . ASP A  1 311 ? -11.677 -6.706  -7.953  1.00 2.00  ? 311  ASP A O   1 
ATOM   2458  C  CB  . ASP A  1 311 ? -10.631 -6.795  -10.822 1.00 3.94  ? 311  ASP A CB  1 
ATOM   2459  C  CG  . ASP A  1 311 ? -10.808 -6.792  -12.324 1.00 5.81  ? 311  ASP A CG  1 
ATOM   2460  O  OD1 . ASP A  1 311 ? -11.951 -7.005  -12.779 1.00 7.61  ? 311  ASP A OD1 1 
ATOM   2461  O  OD2 . ASP A  1 311 ? -9.809  -6.591  -13.045 1.00 5.36  ? 311  ASP A OD2 1 
ATOM   2462  N  N   . TYR A  1 312 ? -10.668 -4.733  -8.368  1.00 2.00  ? 312  TYR A N   1 
ATOM   2463  C  CA  . TYR A  1 312 ? -10.171 -4.611  -7.032  1.00 2.00  ? 312  TYR A CA  1 
ATOM   2464  C  C   . TYR A  1 312 ? -10.958 -3.847  -6.023  1.00 2.00  ? 312  TYR A C   1 
ATOM   2465  O  O   . TYR A  1 312 ? -11.118 -4.291  -4.897  1.00 2.00  ? 312  TYR A O   1 
ATOM   2466  C  CB  . TYR A  1 312 ? -8.818  -3.977  -7.090  1.00 2.33  ? 312  TYR A CB  1 
ATOM   2467  C  CG  . TYR A  1 312 ? -8.384  -3.674  -5.684  1.00 3.19  ? 312  TYR A CG  1 
ATOM   2468  C  CD1 . TYR A  1 312 ? -7.989  -4.699  -4.842  1.00 3.53  ? 312  TYR A CD1 1 
ATOM   2469  C  CD2 . TYR A  1 312 ? -8.365  -2.370  -5.211  1.00 3.43  ? 312  TYR A CD2 1 
ATOM   2470  C  CE1 . TYR A  1 312 ? -7.561  -4.405  -3.569  1.00 3.67  ? 312  TYR A CE1 1 
ATOM   2471  C  CE2 . TYR A  1 312 ? -7.937  -2.065  -3.934  1.00 4.27  ? 312  TYR A CE2 1 
ATOM   2472  C  CZ  . TYR A  1 312 ? -7.521  -3.107  -3.120  1.00 3.98  ? 312  TYR A CZ  1 
ATOM   2473  O  OH  . TYR A  1 312 ? -7.070  -2.826  -1.849  1.00 6.14  ? 312  TYR A OH  1 
ATOM   2474  N  N   . LEU A  1 313 ? -11.456 -2.692  -6.418  1.00 2.53  ? 313  LEU A N   1 
ATOM   2475  C  CA  . LEU A  1 313 ? -12.165 -1.951  -5.410  1.00 2.00  ? 313  LEU A CA  1 
ATOM   2476  C  C   . LEU A  1 313 ? -13.515 -2.530  -5.153  1.00 2.00  ? 313  LEU A C   1 
ATOM   2477  O  O   . LEU A  1 313 ? -14.007 -2.527  -4.024  1.00 2.00  ? 313  LEU A O   1 
ATOM   2478  C  CB  . LEU A  1 313 ? -12.253 -0.480  -5.796  1.00 2.00  ? 313  LEU A CB  1 
ATOM   2479  C  CG  . LEU A  1 313 ? -11.009 0.358   -5.469  1.00 2.00  ? 313  LEU A CG  1 
ATOM   2480  C  CD1 . LEU A  1 313 ? -11.124 1.765   -6.037  1.00 2.00  ? 313  LEU A CD1 1 
ATOM   2481  C  CD2 . LEU A  1 313 ? -10.801 0.416   -3.962  1.00 2.00  ? 313  LEU A CD2 1 
ATOM   2482  N  N   . PRO A  1 314 ? -14.156 -3.042  -6.206  1.00 2.00  ? 314  PRO A N   1 
ATOM   2483  C  CA  . PRO A  1 314 ? -15.498 -3.607  -6.072  1.00 2.00  ? 314  PRO A CA  1 
ATOM   2484  C  C   . PRO A  1 314 ? -15.545 -4.719  -5.034  1.00 2.00  ? 314  PRO A C   1 
ATOM   2485  O  O   . PRO A  1 314 ? -16.610 -5.031  -4.502  1.00 2.00  ? 314  PRO A O   1 
ATOM   2486  C  CB  . PRO A  1 314 ? -15.794 -4.114  -7.469  1.00 2.00  ? 314  PRO A CB  1 
ATOM   2487  C  CG  . PRO A  1 314 ? -15.125 -3.100  -8.314  1.00 2.00  ? 314  PRO A CG  1 
ATOM   2488  C  CD  . PRO A  1 314 ? -13.799 -2.898  -7.626  1.00 2.21  ? 314  PRO A CD  1 
ATOM   2489  N  N   . ILE A  1 315 ? -14.398 -5.329  -4.745  1.00 2.30  ? 315  ILE A N   1 
ATOM   2490  C  CA  . ILE A  1 315 ? -14.382 -6.396  -3.744  1.00 3.03  ? 315  ILE A CA  1 
ATOM   2491  C  C   . ILE A  1 315 ? -13.770 -6.025  -2.396  1.00 2.76  ? 315  ILE A C   1 
ATOM   2492  O  O   . ILE A  1 315 ? -13.700 -6.860  -1.503  1.00 3.93  ? 315  ILE A O   1 
ATOM   2493  C  CB  . ILE A  1 315 ? -13.704 -7.705  -4.260  1.00 2.70  ? 315  ILE A CB  1 
ATOM   2494  C  CG1 . ILE A  1 315 ? -12.222 -7.484  -4.582  1.00 2.79  ? 315  ILE A CG1 1 
ATOM   2495  C  CG2 . ILE A  1 315 ? -14.464 -8.220  -5.464  1.00 3.13  ? 315  ILE A CG2 1 
ATOM   2496  C  CD1 . ILE A  1 315 ? -11.530 -8.725  -5.159  1.00 2.00  ? 315  ILE A CD1 1 
ATOM   2497  N  N   . VAL A  1 316 ? -13.313 -4.789  -2.244  1.00 2.00  ? 316  VAL A N   1 
ATOM   2498  C  CA  . VAL A  1 316 ? -12.788 -4.369  -0.954  1.00 2.00  ? 316  VAL A CA  1 
ATOM   2499  C  C   . VAL A  1 316 ? -13.977 -3.737  -0.249  1.00 3.29  ? 316  VAL A C   1 
ATOM   2500  O  O   . VAL A  1 316 ? -14.244 -4.014  0.924   1.00 2.98  ? 316  VAL A O   1 
ATOM   2501  C  CB  . VAL A  1 316 ? -11.703 -3.293  -1.066  1.00 2.00  ? 316  VAL A CB  1 
ATOM   2502  C  CG1 . VAL A  1 316 ? -11.346 -2.776  0.323   1.00 2.00  ? 316  VAL A CG1 1 
ATOM   2503  C  CG2 . VAL A  1 316 ? -10.490 -3.856  -1.755  1.00 2.89  ? 316  VAL A CG2 1 
ATOM   2504  N  N   . LEU A  1 317 ? -14.693 -2.891  -0.992  1.00 2.12  ? 317  LEU A N   1 
ATOM   2505  C  CA  . LEU A  1 317 ? -15.854 -2.177  -0.474  1.00 2.00  ? 317  LEU A CA  1 
ATOM   2506  C  C   . LEU A  1 317 ? -17.142 -2.994  -0.445  1.00 3.48  ? 317  LEU A C   1 
ATOM   2507  O  O   . LEU A  1 317 ? -17.958 -2.846  0.468   1.00 2.85  ? 317  LEU A O   1 
ATOM   2508  C  CB  . LEU A  1 317 ? -16.083 -0.907  -1.288  1.00 2.00  ? 317  LEU A CB  1 
ATOM   2509  C  CG  . LEU A  1 317 ? -15.328 0.363   -0.907  1.00 2.00  ? 317  LEU A CG  1 
ATOM   2510  C  CD1 . LEU A  1 317 ? -14.343 0.083   0.203   1.00 2.69  ? 317  LEU A CD1 1 
ATOM   2511  C  CD2 . LEU A  1 317 ? -14.624 0.915   -2.134  1.00 2.00  ? 317  LEU A CD2 1 
ATOM   2512  N  N   . GLY A  1 318 ? -17.328 -3.850  -1.444  1.00 2.93  ? 318  GLY A N   1 
ATOM   2513  C  CA  . GLY A  1 318 ? -18.536 -4.653  -1.493  1.00 2.24  ? 318  GLY A CA  1 
ATOM   2514  C  C   . GLY A  1 318 ? -19.788 -3.824  -1.708  1.00 3.21  ? 318  GLY A C   1 
ATOM   2515  O  O   . GLY A  1 318 ? -19.847 -2.964  -2.582  1.00 3.91  ? 318  GLY A O   1 
ATOM   2516  N  N   . SER A  1 319 ? -20.801 -4.064  -0.898  1.00 3.22  ? 319  SER A N   1 
ATOM   2517  C  CA  . SER A  1 319 ? -22.049 -3.347  -1.051  1.00 5.50  ? 319  SER A CA  1 
ATOM   2518  C  C   . SER A  1 319 ? -22.017 -1.865  -0.676  1.00 6.53  ? 319  SER A C   1 
ATOM   2519  O  O   . SER A  1 319 ? -23.071 -1.245  -0.548  1.00 7.92  ? 319  SER A O   1 
ATOM   2520  C  CB  . SER A  1 319 ? -23.130 -4.065  -0.246  1.00 7.47  ? 319  SER A CB  1 
ATOM   2521  O  OG  . SER A  1 319 ? -22.652 -4.390  1.053   1.00 10.31 ? 319  SER A OG  1 
ATOM   2522  N  N   . GLU A  1 320 ? -20.829 -1.291  -0.504  1.00 5.62  ? 320  GLU A N   1 
ATOM   2523  C  CA  . GLU A  1 320 ? -20.725 0.126   -0.144  1.00 6.53  ? 320  GLU A CA  1 
ATOM   2524  C  C   . GLU A  1 320 ? -20.028 0.935   -1.238  1.00 7.30  ? 320  GLU A C   1 
ATOM   2525  O  O   . GLU A  1 320 ? -19.677 2.104   -1.048  1.00 6.40  ? 320  GLU A O   1 
ATOM   2526  C  CB  . GLU A  1 320 ? -19.949 0.287   1.162   1.00 7.38  ? 320  GLU A CB  1 
ATOM   2527  C  CG  . GLU A  1 320 ? -20.554 -0.419  2.352   1.00 7.62  ? 320  GLU A CG  1 
ATOM   2528  C  CD  . GLU A  1 320 ? -21.593 0.413   3.061   1.00 8.11  ? 320  GLU A CD  1 
ATOM   2529  O  OE1 . GLU A  1 320 ? -21.302 1.596   3.340   1.00 8.88  ? 320  GLU A OE1 1 
ATOM   2530  O  OE2 . GLU A  1 320 ? -22.689 -0.119  3.348   1.00 8.37  ? 320  GLU A OE2 1 
ATOM   2531  N  N   . MET A  1 321 ? -19.829 0.298   -2.383  1.00 8.56  ? 321  MET A N   1 
ATOM   2532  C  CA  . MET A  1 321 ? -19.170 0.936   -3.513  1.00 10.54 ? 321  MET A CA  1 
ATOM   2533  C  C   . MET A  1 321 ? -20.084 1.896   -4.273  1.00 13.52 ? 321  MET A C   1 
ATOM   2534  O  O   . MET A  1 321 ? -19.664 2.986   -4.654  1.00 13.89 ? 321  MET A O   1 
ATOM   2535  C  CB  . MET A  1 321 ? -18.636 -0.132  -4.462  1.00 8.01  ? 321  MET A CB  1 
ATOM   2536  C  CG  . MET A  1 321 ? -18.100 0.412   -5.750  1.00 6.17  ? 321  MET A CG  1 
ATOM   2537  S  SD  . MET A  1 321 ? -16.506 -0.300  -6.115  1.00 6.27  ? 321  MET A SD  1 
ATOM   2538  C  CE  . MET A  1 321 ? -15.649 1.129   -6.754  1.00 5.76  ? 321  MET A CE  1 
ATOM   2539  N  N   . GLN A  1 322 ? -21.330 1.499   -4.503  1.00 16.51 ? 322  GLN A N   1 
ATOM   2540  C  CA  . GLN A  1 322 ? -22.255 2.375   -5.210  1.00 18.36 ? 322  GLN A CA  1 
ATOM   2541  C  C   . GLN A  1 322 ? -22.531 3.615   -4.356  1.00 17.29 ? 322  GLN A C   1 
ATOM   2542  O  O   . GLN A  1 322 ? -22.636 4.731   -4.867  1.00 16.07 ? 322  GLN A O   1 
ATOM   2543  C  CB  . GLN A  1 322 ? -23.557 1.631   -5.504  1.00 23.15 ? 322  GLN A CB  1 
ATOM   2544  C  CG  . GLN A  1 322 ? -23.382 0.416   -6.405  1.00 29.19 ? 322  GLN A CG  1 
ATOM   2545  C  CD  . GLN A  1 322 ? -24.678 -0.356  -6.589  1.00 32.29 ? 322  GLN A CD  1 
ATOM   2546  O  OE1 . GLN A  1 322 ? -25.282 -0.818  -5.616  1.00 34.43 ? 322  GLN A OE1 1 
ATOM   2547  N  NE2 . GLN A  1 322 ? -25.112 -0.499  -7.838  1.00 33.81 ? 322  GLN A NE2 1 
ATOM   2548  N  N   . LYS A  1 323 ? -22.625 3.392   -3.048  1.00 15.60 ? 323  LYS A N   1 
ATOM   2549  C  CA  . LYS A  1 323 ? -22.884 4.428   -2.053  1.00 14.03 ? 323  LYS A CA  1 
ATOM   2550  C  C   . LYS A  1 323 ? -21.832 5.552   -2.034  1.00 14.34 ? 323  LYS A C   1 
ATOM   2551  O  O   . LYS A  1 323 ? -22.164 6.715   -1.784  1.00 15.12 ? 323  LYS A O   1 
ATOM   2552  C  CB  . LYS A  1 323 ? -22.961 3.763   -0.674  1.00 14.07 ? 323  LYS A CB  1 
ATOM   2553  C  CG  . LYS A  1 323 ? -23.303 4.676   0.492   1.00 16.44 ? 323  LYS A CG  1 
ATOM   2554  C  CD  . LYS A  1 323 ? -23.287 3.890   1.809   1.00 17.57 ? 323  LYS A CD  1 
ATOM   2555  C  CE  . LYS A  1 323 ? -23.956 4.654   2.958   1.00 19.18 ? 323  LYS A CE  1 
ATOM   2556  N  NZ  . LYS A  1 323 ? -23.279 5.948   3.297   1.00 19.77 ? 323  LYS A NZ  1 
ATOM   2557  N  N   . TRP A  1 324 ? -20.573 5.204   -2.300  1.00 12.72 ? 324  TRP A N   1 
ATOM   2558  C  CA  . TRP A  1 324 ? -19.479 6.176   -2.289  1.00 9.80  ? 324  TRP A CA  1 
ATOM   2559  C  C   . TRP A  1 324 ? -18.882 6.489   -3.657  1.00 9.79  ? 324  TRP A C   1 
ATOM   2560  O  O   . TRP A  1 324 ? -18.544 7.634   -3.965  1.00 9.16  ? 324  TRP A O   1 
ATOM   2561  C  CB  . TRP A  1 324 ? -18.361 5.669   -1.389  1.00 9.95  ? 324  TRP A CB  1 
ATOM   2562  C  CG  . TRP A  1 324 ? -18.775 5.524   0.008   1.00 11.37 ? 324  TRP A CG  1 
ATOM   2563  C  CD1 . TRP A  1 324 ? -18.833 4.370   0.732   1.00 12.31 ? 324  TRP A CD1 1 
ATOM   2564  C  CD2 . TRP A  1 324 ? -19.210 6.572   0.879   1.00 12.07 ? 324  TRP A CD2 1 
ATOM   2565  N  NE1 . TRP A  1 324 ? -19.280 4.633   2.009   1.00 13.39 ? 324  TRP A NE1 1 
ATOM   2566  C  CE2 . TRP A  1 324 ? -19.519 5.979   2.124   1.00 12.52 ? 324  TRP A CE2 1 
ATOM   2567  C  CE3 . TRP A  1 324 ? -19.369 7.957   0.729   1.00 11.41 ? 324  TRP A CE3 1 
ATOM   2568  C  CZ2 . TRP A  1 324 ? -19.981 6.726   3.214   1.00 11.59 ? 324  TRP A CZ2 1 
ATOM   2569  C  CZ3 . TRP A  1 324 ? -19.827 8.697   1.814   1.00 10.32 ? 324  TRP A CZ3 1 
ATOM   2570  C  CH2 . TRP A  1 324 ? -20.127 8.079   3.038   1.00 10.51 ? 324  TRP A CH2 1 
ATOM   2571  N  N   . ILE A  1 325 ? -18.732 5.456   -4.468  1.00 8.63  ? 325  ILE A N   1 
ATOM   2572  C  CA  . ILE A  1 325 ? -18.151 5.613   -5.786  1.00 7.66  ? 325  ILE A CA  1 
ATOM   2573  C  C   . ILE A  1 325 ? -19.222 5.425   -6.864  1.00 8.85  ? 325  ILE A C   1 
ATOM   2574  O  O   . ILE A  1 325 ? -19.444 4.316   -7.359  1.00 11.14 ? 325  ILE A O   1 
ATOM   2575  C  CB  . ILE A  1 325 ? -16.974 4.603   -5.978  1.00 5.46  ? 325  ILE A CB  1 
ATOM   2576  C  CG1 . ILE A  1 325 ? -15.829 4.952   -5.019  1.00 3.99  ? 325  ILE A CG1 1 
ATOM   2577  C  CG2 . ILE A  1 325 ? -16.481 4.618   -7.406  1.00 4.60  ? 325  ILE A CG2 1 
ATOM   2578  C  CD1 . ILE A  1 325 ? -14.694 3.949   -5.012  1.00 2.70  ? 325  ILE A CD1 1 
ATOM   2579  N  N   . PRO A  1 326 ? -19.925 6.513   -7.215  1.00 8.03  ? 326  PRO A N   1 
ATOM   2580  C  CA  . PRO A  1 326 ? -20.968 6.468   -8.241  1.00 6.92  ? 326  PRO A CA  1 
ATOM   2581  C  C   . PRO A  1 326 ? -20.249 6.296   -9.581  1.00 6.55  ? 326  PRO A C   1 
ATOM   2582  O  O   . PRO A  1 326 ? -19.026 6.299   -9.622  1.00 5.42  ? 326  PRO A O   1 
ATOM   2583  C  CB  . PRO A  1 326 ? -21.627 7.841   -8.120  1.00 7.72  ? 326  PRO A CB  1 
ATOM   2584  C  CG  . PRO A  1 326 ? -21.284 8.296   -6.715  1.00 7.07  ? 326  PRO A CG  1 
ATOM   2585  C  CD  . PRO A  1 326 ? -19.873 7.841   -6.581  1.00 7.16  ? 326  PRO A CD  1 
ATOM   2586  N  N   . ARG A  1 327 ? -20.998 6.173   -10.670 1.00 7.82  ? 327  ARG A N   1 
ATOM   2587  C  CA  . ARG A  1 327 ? -20.405 5.997   -11.997 1.00 11.26 ? 327  ARG A CA  1 
ATOM   2588  C  C   . ARG A  1 327 ? -19.780 7.319   -12.501 1.00 10.67 ? 327  ARG A C   1 
ATOM   2589  O  O   . ARG A  1 327 ? -20.364 8.390   -12.324 1.00 11.89 ? 327  ARG A O   1 
ATOM   2590  C  CB  . ARG A  1 327 ? -21.491 5.474   -12.959 1.00 15.61 ? 327  ARG A CB  1 
ATOM   2591  C  CG  . ARG A  1 327 ? -22.177 4.118   -12.514 1.00 23.88 ? 327  ARG A CG  1 
ATOM   2592  C  CD  . ARG A  1 327 ? -23.097 4.250   -11.253 1.00 28.70 ? 327  ARG A CD  1 
ATOM   2593  N  NE  . ARG A  1 327 ? -23.516 2.986   -10.604 1.00 33.02 ? 327  ARG A NE  1 
ATOM   2594  C  CZ  . ARG A  1 327 ? -24.396 2.104   -11.089 1.00 34.29 ? 327  ARG A CZ  1 
ATOM   2595  N  NH1 . ARG A  1 327 ? -24.986 2.303   -12.261 1.00 35.26 ? 327  ARG A NH1 1 
ATOM   2596  N  NH2 . ARG A  1 327 ? -24.709 1.025   -10.380 1.00 36.12 ? 327  ARG A NH2 1 
ATOM   2597  N  N   . TYR A  1 328 ? -18.595 7.257   -13.111 1.00 10.08 ? 328  TYR A N   1 
ATOM   2598  C  CA  . TYR A  1 328 ? -17.911 8.467   -13.592 1.00 9.31  ? 328  TYR A CA  1 
ATOM   2599  C  C   . TYR A  1 328 ? -18.765 9.299   -14.547 1.00 10.34 ? 328  TYR A C   1 
ATOM   2600  O  O   . TYR A  1 328 ? -19.302 8.794   -15.548 1.00 9.12  ? 328  TYR A O   1 
ATOM   2601  C  CB  . TYR A  1 328 ? -16.586 8.084   -14.269 1.00 8.37  ? 328  TYR A CB  1 
ATOM   2602  C  CG  . TYR A  1 328 ? -15.668 9.213   -14.691 1.00 6.15  ? 328  TYR A CG  1 
ATOM   2603  C  CD1 . TYR A  1 328 ? -15.025 10.015  -13.751 1.00 6.72  ? 328  TYR A CD1 1 
ATOM   2604  C  CD2 . TYR A  1 328 ? -15.339 9.382   -16.031 1.00 6.14  ? 328  TYR A CD2 1 
ATOM   2605  C  CE1 . TYR A  1 328 ? -14.060 10.948  -14.142 1.00 6.82  ? 328  TYR A CE1 1 
ATOM   2606  C  CE2 . TYR A  1 328 ? -14.384 10.297  -16.431 1.00 5.86  ? 328  TYR A CE2 1 
ATOM   2607  C  CZ  . TYR A  1 328 ? -13.743 11.072  -15.487 1.00 6.34  ? 328  TYR A CZ  1 
ATOM   2608  O  OH  . TYR A  1 328 ? -12.744 11.921  -15.890 1.00 5.15  ? 328  TYR A OH  1 
ATOM   2609  N  N   . GLN A  1 329 ? -18.901 10.578  -14.210 1.00 8.59  ? 329  GLN A N   1 
ATOM   2610  C  CA  . GLN A  1 329 ? -19.667 11.506  -15.020 1.00 7.52  ? 329  GLN A CA  1 
ATOM   2611  C  C   . GLN A  1 329 ? -18.700 12.552  -15.588 1.00 5.74  ? 329  GLN A C   1 
ATOM   2612  O  O   . GLN A  1 329 ? -19.112 13.653  -15.944 1.00 6.61  ? 329  GLN A O   1 
ATOM   2613  C  CB  . GLN A  1 329 ? -20.773 12.175  -14.185 1.00 11.72 ? 329  GLN A CB  1 
ATOM   2614  C  CG  . GLN A  1 329 ? -21.892 11.244  -13.669 1.00 17.35 ? 329  GLN A CG  1 
ATOM   2615  C  CD  . GLN A  1 329 ? -23.119 11.154  -14.592 1.00 20.30 ? 329  GLN A CD  1 
ATOM   2616  O  OE1 . GLN A  1 329 ? -23.121 10.474  -15.626 1.00 22.32 ? 329  GLN A OE1 1 
ATOM   2617  N  NE2 . GLN A  1 329 ? -24.180 11.856  -14.212 1.00 21.96 ? 329  GLN A NE2 1 
ATOM   2618  N  N   . GLY A  1 330 ? -17.412 12.207  -15.656 1.00 2.65  ? 330  GLY A N   1 
ATOM   2619  C  CA  . GLY A  1 330 ? -16.415 13.112  -16.216 1.00 2.00  ? 330  GLY A CA  1 
ATOM   2620  C  C   . GLY A  1 330 ? -15.628 13.968  -15.239 1.00 2.00  ? 330  GLY A C   1 
ATOM   2621  O  O   . GLY A  1 330 ? -16.002 14.097  -14.078 1.00 2.01  ? 330  GLY A O   1 
ATOM   2622  N  N   . TYR A  1 331 ? -14.546 14.578  -15.711 1.00 2.14  ? 331  TYR A N   1 
ATOM   2623  C  CA  . TYR A  1 331 ? -13.704 15.416  -14.859 1.00 2.37  ? 331  TYR A CA  1 
ATOM   2624  C  C   . TYR A  1 331 ? -14.406 16.565  -14.123 1.00 3.34  ? 331  TYR A C   1 
ATOM   2625  O  O   . TYR A  1 331 ? -14.954 17.481  -14.746 1.00 2.45  ? 331  TYR A O   1 
ATOM   2626  C  CB  . TYR A  1 331 ? -12.542 15.967  -15.694 1.00 3.82  ? 331  TYR A CB  1 
ATOM   2627  C  CG  . TYR A  1 331 ? -11.566 16.877  -14.970 1.00 5.77  ? 331  TYR A CG  1 
ATOM   2628  C  CD1 . TYR A  1 331 ? -11.113 16.588  -13.686 1.00 6.75  ? 331  TYR A CD1 1 
ATOM   2629  C  CD2 . TYR A  1 331 ? -11.024 17.990  -15.615 1.00 7.54  ? 331  TYR A CD2 1 
ATOM   2630  C  CE1 . TYR A  1 331 ? -10.137 17.387  -13.071 1.00 7.78  ? 331  TYR A CE1 1 
ATOM   2631  C  CE2 . TYR A  1 331 ? -10.051 18.785  -15.008 1.00 6.63  ? 331  TYR A CE2 1 
ATOM   2632  C  CZ  . TYR A  1 331 ? -9.611  18.479  -13.749 1.00 6.09  ? 331  TYR A CZ  1 
ATOM   2633  O  OH  . TYR A  1 331 ? -8.617  19.246  -13.199 1.00 6.81  ? 331  TYR A OH  1 
ATOM   2634  N  N   . ASN A  1 332 ? -14.384 16.499  -12.792 1.00 4.38  ? 332  ASN A N   1 
ATOM   2635  C  CA  . ASN A  1 332 ? -14.966 17.523  -11.921 1.00 7.42  ? 332  ASN A CA  1 
ATOM   2636  C  C   . ASN A  1 332 ? -13.747 18.303  -11.403 1.00 6.74  ? 332  ASN A C   1 
ATOM   2637  O  O   . ASN A  1 332 ? -13.223 17.992  -10.341 1.00 6.83  ? 332  ASN A O   1 
ATOM   2638  C  CB  . ASN A  1 332 ? -15.712 16.865  -10.744 1.00 12.11 ? 332  ASN A CB  1 
ATOM   2639  C  CG  . ASN A  1 332 ? -16.453 17.875  -9.873  1.00 19.49 ? 332  ASN A CG  1 
ATOM   2640  O  OD1 . ASN A  1 332 ? -15.956 18.960  -9.610  1.00 16.70 ? 332  ASN A OD1 1 
ATOM   2641  N  ND2 . ASN A  1 332 ? -17.649 17.518  -9.419  1.00 30.80 ? 332  ASN A ND2 1 
ATOM   2642  N  N   . ASN A  1 333 ? -13.292 19.306  -12.154 1.00 6.36  ? 333  ASN A N   1 
ATOM   2643  C  CA  . ASN A  1 333 ? -12.105 20.081  -11.769 1.00 6.66  ? 333  ASN A CA  1 
ATOM   2644  C  C   . ASN A  1 333 ? -12.190 20.751  -10.406 1.00 6.43  ? 333  ASN A C   1 
ATOM   2645  O  O   . ASN A  1 333 ? -11.178 21.197  -9.860  1.00 6.40  ? 333  ASN A O   1 
ATOM   2646  C  CB  . ASN A  1 333 ? -11.785 21.151  -12.823 1.00 7.26  ? 333  ASN A CB  1 
ATOM   2647  C  CG  . ASN A  1 333 ? -12.611 22.421  -12.647 1.00 7.05  ? 333  ASN A CG  1 
ATOM   2648  O  OD1 . ASN A  1 333 ? -12.371 23.214  -11.733 1.00 6.39  ? 333  ASN A OD1 1 
ATOM   2649  N  ND2 . ASN A  1 333 ? -13.590 22.616  -13.525 1.00 7.48  ? 333  ASN A ND2 1 
ATOM   2650  N  N   . SER A  1 334 ? -13.387 20.840  -9.853  1.00 5.25  ? 334  SER A N   1 
ATOM   2651  C  CA  . SER A  1 334 ? -13.518 21.462  -8.551  1.00 6.54  ? 334  SER A CA  1 
ATOM   2652  C  C   . SER A  1 334 ? -13.327 20.467  -7.409  1.00 5.31  ? 334  SER A C   1 
ATOM   2653  O  O   . SER A  1 334 ? -13.783 20.713  -6.297  1.00 7.63  ? 334  SER A O   1 
ATOM   2654  C  CB  . SER A  1 334 ? -14.886 22.148  -8.417  1.00 7.62  ? 334  SER A CB  1 
ATOM   2655  O  OG  . SER A  1 334 ? -14.882 23.442  -9.006  1.00 8.52  ? 334  SER A OG  1 
ATOM   2656  N  N   . VAL A  1 335 ? -12.636 19.361  -7.664  1.00 3.93  ? 335  VAL A N   1 
ATOM   2657  C  CA  . VAL A  1 335 ? -12.430 18.347  -6.627  1.00 2.06  ? 335  VAL A CA  1 
ATOM   2658  C  C   . VAL A  1 335 ? -10.972 18.145  -6.165  1.00 2.00  ? 335  VAL A C   1 
ATOM   2659  O  O   . VAL A  1 335 ? -10.091 17.848  -6.967  1.00 2.00  ? 335  VAL A O   1 
ATOM   2660  C  CB  . VAL A  1 335 ? -13.001 16.993  -7.101  1.00 2.00  ? 335  VAL A CB  1 
ATOM   2661  C  CG1 . VAL A  1 335 ? -12.963 15.984  -5.981  1.00 2.00  ? 335  VAL A CG1 1 
ATOM   2662  C  CG2 . VAL A  1 335 ? -14.422 17.180  -7.590  1.00 2.00  ? 335  VAL A CG2 1 
ATOM   2663  N  N   . ASP A  1 336 ? -10.731 18.297  -4.864  1.00 2.00  ? 336  ASP A N   1 
ATOM   2664  C  CA  . ASP A  1 336 ? -9.393  18.125  -4.277  1.00 2.74  ? 336  ASP A CA  1 
ATOM   2665  C  C   . ASP A  1 336 ? -8.898  16.672  -4.468  1.00 2.53  ? 336  ASP A C   1 
ATOM   2666  O  O   . ASP A  1 336 ? -9.378  15.748  -3.806  1.00 2.14  ? 336  ASP A O   1 
ATOM   2667  C  CB  . ASP A  1 336 ? -9.450  18.492  -2.778  1.00 3.25  ? 336  ASP A CB  1 
ATOM   2668  C  CG  . ASP A  1 336 ? -8.069  18.568  -2.126  1.00 4.04  ? 336  ASP A CG  1 
ATOM   2669  O  OD1 . ASP A  1 336 ? -7.397  17.522  -2.027  1.00 6.00  ? 336  ASP A OD1 1 
ATOM   2670  O  OD2 . ASP A  1 336 ? -7.652  19.670  -1.707  1.00 4.10  ? 336  ASP A OD2 1 
ATOM   2671  N  N   . PRO A  1 337 ? -7.916  16.456  -5.364  1.00 2.00  ? 337  PRO A N   1 
ATOM   2672  C  CA  . PRO A  1 337 ? -7.370  15.123  -5.643  1.00 2.00  ? 337  PRO A CA  1 
ATOM   2673  C  C   . PRO A  1 337 ? -6.298  14.624  -4.678  1.00 3.32  ? 337  PRO A C   1 
ATOM   2674  O  O   . PRO A  1 337 ? -5.802  13.505  -4.833  1.00 3.14  ? 337  PRO A O   1 
ATOM   2675  C  CB  . PRO A  1 337 ? -6.801  15.291  -7.036  1.00 2.00  ? 337  PRO A CB  1 
ATOM   2676  C  CG  . PRO A  1 337 ? -6.145  16.614  -6.892  1.00 2.00  ? 337  PRO A CG  1 
ATOM   2677  C  CD  . PRO A  1 337 ? -7.238  17.455  -6.207  1.00 2.00  ? 337  PRO A CD  1 
ATOM   2678  N  N   . ARG A  1 338 ? -5.933  15.448  -3.699  1.00 3.03  ? 338  ARG A N   1 
ATOM   2679  C  CA  . ARG A  1 338 ? -4.902  15.089  -2.723  1.00 2.00  ? 338  ARG A CA  1 
ATOM   2680  C  C   . ARG A  1 338 ? -5.284  13.996  -1.756  1.00 2.00  ? 338  ARG A C   1 
ATOM   2681  O  O   . ARG A  1 338 ? -6.453  13.837  -1.416  1.00 2.00  ? 338  ARG A O   1 
ATOM   2682  C  CB  . ARG A  1 338 ? -4.521  16.294  -1.896  1.00 2.00  ? 338  ARG A CB  1 
ATOM   2683  C  CG  . ARG A  1 338 ? -3.798  17.365  -2.649  1.00 2.67  ? 338  ARG A CG  1 
ATOM   2684  C  CD  . ARG A  1 338 ? -3.579  18.506  -1.701  1.00 2.41  ? 338  ARG A CD  1 
ATOM   2685  N  NE  . ARG A  1 338 ? -4.837  18.858  -1.062  1.00 2.00  ? 338  ARG A NE  1 
ATOM   2686  C  CZ  . ARG A  1 338 ? -4.943  19.788  -0.132  1.00 2.00  ? 338  ARG A CZ  1 
ATOM   2687  N  NH1 . ARG A  1 338 ? -3.855  20.440  0.252   1.00 2.91  ? 338  ARG A NH1 1 
ATOM   2688  N  NH2 . ARG A  1 338 ? -6.123  20.068  0.405   1.00 2.04  ? 338  ARG A NH2 1 
ATOM   2689  N  N   . ILE A  1 339 ? -4.281  13.264  -1.287  1.00 2.00  ? 339  ILE A N   1 
ATOM   2690  C  CA  . ILE A  1 339 ? -4.520  12.193  -0.330  1.00 3.75  ? 339  ILE A CA  1 
ATOM   2691  C  C   . ILE A  1 339 ? -4.642  12.794  1.071   1.00 2.53  ? 339  ILE A C   1 
ATOM   2692  O  O   . ILE A  1 339 ? -3.801  13.589  1.485   1.00 3.61  ? 339  ILE A O   1 
ATOM   2693  C  CB  . ILE A  1 339 ? -3.372  11.158  -0.334  1.00 2.20  ? 339  ILE A CB  1 
ATOM   2694  C  CG1 . ILE A  1 339 ? -3.207  10.549  -1.732  1.00 2.24  ? 339  ILE A CG1 1 
ATOM   2695  C  CG2 . ILE A  1 339 ? -3.675  10.057  0.665   1.00 2.07  ? 339  ILE A CG2 1 
ATOM   2696  C  CD1 . ILE A  1 339 ? -4.462  9.870   -2.279  1.00 2.00  ? 339  ILE A CD1 1 
ATOM   2697  N  N   . SER A  1 340 ? -5.700  12.427  1.788   1.00 2.00  ? 340  SER A N   1 
ATOM   2698  C  CA  . SER A  1 340 ? -5.921  12.935  3.135   1.00 2.00  ? 340  SER A CA  1 
ATOM   2699  C  C   . SER A  1 340 ? -4.972  12.198  4.033   1.00 2.00  ? 340  SER A C   1 
ATOM   2700  O  O   . SER A  1 340 ? -4.396  11.191  3.628   1.00 2.41  ? 340  SER A O   1 
ATOM   2701  C  CB  . SER A  1 340 ? -7.342  12.658  3.598   1.00 2.00  ? 340  SER A CB  1 
ATOM   2702  O  OG  . SER A  1 340 ? -7.533  11.275  3.826   1.00 2.00  ? 340  SER A OG  1 
ATOM   2703  N  N   . ASN A  1 341 ? -4.818  12.676  5.259   1.00 2.00  ? 341  ASN A N   1 
ATOM   2704  C  CA  . ASN A  1 341 ? -3.899  12.027  6.168   1.00 2.00  ? 341  ASN A CA  1 
ATOM   2705  C  C   . ASN A  1 341 ? -4.470  10.703  6.595   1.00 2.00  ? 341  ASN A C   1 
ATOM   2706  O  O   . ASN A  1 341 ? -3.820  9.667   6.474   1.00 2.57  ? 341  ASN A O   1 
ATOM   2707  C  CB  . ASN A  1 341 ? -3.654  12.882  7.399   1.00 2.00  ? 341  ASN A CB  1 
ATOM   2708  C  CG  . ASN A  1 341 ? -2.354  12.540  8.081   1.00 2.00  ? 341  ASN A CG  1 
ATOM   2709  O  OD1 . ASN A  1 341 ? -2.073  11.376  8.356   1.00 2.01  ? 341  ASN A OD1 1 
ATOM   2710  N  ND2 . ASN A  1 341 ? -1.548  13.555  8.359   1.00 2.00  ? 341  ASN A ND2 1 
ATOM   2711  N  N   . VAL A  1 342 ? -5.703  10.740  7.080   1.00 2.50  ? 342  VAL A N   1 
ATOM   2712  C  CA  . VAL A  1 342 ? -6.364  9.536   7.553   1.00 2.00  ? 342  VAL A CA  1 
ATOM   2713  C  C   . VAL A  1 342 ? -6.355  8.392   6.544   1.00 2.12  ? 342  VAL A C   1 
ATOM   2714  O  O   . VAL A  1 342 ? -6.314  7.231   6.937   1.00 3.32  ? 342  VAL A O   1 
ATOM   2715  C  CB  . VAL A  1 342 ? -7.804  9.819   7.935   1.00 2.00  ? 342  VAL A CB  1 
ATOM   2716  C  CG1 . VAL A  1 342 ? -8.628  9.995   6.681   1.00 3.87  ? 342  VAL A CG1 1 
ATOM   2717  C  CG2 . VAL A  1 342 ? -8.338  8.699   8.797   1.00 2.00  ? 342  VAL A CG2 1 
ATOM   2718  N  N   . PHE A  1 343 ? -6.397  8.703   5.252   1.00 2.00  ? 343  PHE A N   1 
ATOM   2719  C  CA  . PHE A  1 343 ? -6.387  7.644   4.251   1.00 2.00  ? 343  PHE A CA  1 
ATOM   2720  C  C   . PHE A  1 343 ? -5.187  6.755   4.492   1.00 2.00  ? 343  PHE A C   1 
ATOM   2721  O  O   . PHE A  1 343 ? -5.280  5.528   4.385   1.00 2.00  ? 343  PHE A O   1 
ATOM   2722  C  CB  . PHE A  1 343 ? -6.293  8.211   2.838   1.00 2.00  ? 343  PHE A CB  1 
ATOM   2723  C  CG  . PHE A  1 343 ? -6.418  7.170   1.759   1.00 2.00  ? 343  PHE A CG  1 
ATOM   2724  C  CD1 . PHE A  1 343 ? -7.570  6.402   1.651   1.00 2.00  ? 343  PHE A CD1 1 
ATOM   2725  C  CD2 . PHE A  1 343 ? -5.389  6.959   0.850   1.00 2.00  ? 343  PHE A CD2 1 
ATOM   2726  C  CE1 . PHE A  1 343 ? -7.696  5.438   0.650   1.00 2.00  ? 343  PHE A CE1 1 
ATOM   2727  C  CE2 . PHE A  1 343 ? -5.507  5.995   -0.155  1.00 2.00  ? 343  PHE A CE2 1 
ATOM   2728  C  CZ  . PHE A  1 343 ? -6.664  5.235   -0.254  1.00 2.00  ? 343  PHE A CZ  1 
ATOM   2729  N  N   . THR A  1 344 ? -4.066  7.383   4.841   1.00 2.00  ? 344  THR A N   1 
ATOM   2730  C  CA  . THR A  1 344 ? -2.830  6.646   5.070   1.00 2.12  ? 344  THR A CA  1 
ATOM   2731  C  C   . THR A  1 344 ? -2.859  5.747   6.305   1.00 2.00  ? 344  THR A C   1 
ATOM   2732  O  O   . THR A  1 344 ? -1.887  5.065   6.609   1.00 2.00  ? 344  THR A O   1 
ATOM   2733  C  CB  . THR A  1 344 ? -1.585  7.589   5.132   1.00 2.10  ? 344  THR A CB  1 
ATOM   2734  O  OG1 . THR A  1 344 ? -1.387  8.044   6.470   1.00 4.20  ? 344  THR A OG1 1 
ATOM   2735  C  CG2 . THR A  1 344 ? -1.765  8.794   4.218   1.00 2.00  ? 344  THR A CG2 1 
ATOM   2736  N  N   . PHE A  1 345 ? -3.972  5.741   7.023   1.00 2.01  ? 345  PHE A N   1 
ATOM   2737  C  CA  . PHE A  1 345 ? -4.089  4.862   8.182   1.00 3.04  ? 345  PHE A CA  1 
ATOM   2738  C  C   . PHE A  1 345 ? -5.300  3.962   7.938   1.00 2.00  ? 345  PHE A C   1 
ATOM   2739  O  O   . PHE A  1 345 ? -5.418  2.870   8.525   1.00 2.00  ? 345  PHE A O   1 
ATOM   2740  C  CB  . PHE A  1 345 ? -4.253  5.660   9.486   1.00 2.00  ? 345  PHE A CB  1 
ATOM   2741  C  CG  . PHE A  1 345 ? -3.041  6.464   9.865   1.00 2.00  ? 345  PHE A CG  1 
ATOM   2742  C  CD1 . PHE A  1 345 ? -2.910  7.788   9.459   1.00 2.00  ? 345  PHE A CD1 1 
ATOM   2743  C  CD2 . PHE A  1 345 ? -2.022  5.898   10.621  1.00 2.00  ? 345  PHE A CD2 1 
ATOM   2744  C  CE1 . PHE A  1 345 ? -1.778  8.544   9.802   1.00 2.00  ? 345  PHE A CE1 1 
ATOM   2745  C  CE2 . PHE A  1 345 ? -0.884  6.641   10.971  1.00 2.00  ? 345  PHE A CE2 1 
ATOM   2746  C  CZ  . PHE A  1 345 ? -0.766  7.968   10.558  1.00 2.00  ? 345  PHE A CZ  1 
ATOM   2747  N  N   . ALA A  1 346 ? -6.189  4.427   7.074   1.00 2.00  ? 346  ALA A N   1 
ATOM   2748  C  CA  . ALA A  1 346 ? -7.373  3.668   6.746   1.00 2.00  ? 346  ALA A CA  1 
ATOM   2749  C  C   . ALA A  1 346 ? -6.964  2.570   5.803   1.00 2.36  ? 346  ALA A C   1 
ATOM   2750  O  O   . ALA A  1 346 ? -7.499  1.466   5.854   1.00 2.93  ? 346  ALA A O   1 
ATOM   2751  C  CB  . ALA A  1 346 ? -8.398  4.551   6.076   1.00 2.00  ? 346  ALA A CB  1 
ATOM   2752  N  N   . PHE A  1 347 ? -6.000  2.865   4.942   1.00 2.00  ? 347  PHE A N   1 
ATOM   2753  C  CA  . PHE A  1 347 ? -5.587  1.864   3.977   1.00 2.00  ? 347  PHE A CA  1 
ATOM   2754  C  C   . PHE A  1 347 ? -4.781  0.731   4.608   1.00 2.00  ? 347  PHE A C   1 
ATOM   2755  O  O   . PHE A  1 347 ? -4.700  -0.360  4.051   1.00 2.27  ? 347  PHE A O   1 
ATOM   2756  C  CB  . PHE A  1 347 ? -4.807  2.515   2.826   1.00 2.00  ? 347  PHE A CB  1 
ATOM   2757  C  CG  . PHE A  1 347 ? -5.013  1.841   1.486   1.00 2.00  ? 347  PHE A CG  1 
ATOM   2758  C  CD1 . PHE A  1 347 ? -5.618  0.591   1.396   1.00 2.30  ? 347  PHE A CD1 1 
ATOM   2759  C  CD2 . PHE A  1 347 ? -4.542  2.425   0.327   1.00 2.00  ? 347  PHE A CD2 1 
ATOM   2760  C  CE1 . PHE A  1 347 ? -5.741  -0.066  0.169   1.00 2.00  ? 347  PHE A CE1 1 
ATOM   2761  C  CE2 . PHE A  1 347 ? -4.659  1.777   -0.898  1.00 2.00  ? 347  PHE A CE2 1 
ATOM   2762  C  CZ  . PHE A  1 347 ? -5.258  0.529   -0.977  1.00 2.00  ? 347  PHE A CZ  1 
ATOM   2763  N  N   . ARG A  1 348 ? -4.207  0.959   5.781   1.00 2.00  ? 348  ARG A N   1 
ATOM   2764  C  CA  . ARG A  1 348 ? -3.428  -0.097  6.410   1.00 2.00  ? 348  ARG A CA  1 
ATOM   2765  C  C   . ARG A  1 348 ? -4.260  -1.303  6.844   1.00 2.00  ? 348  ARG A C   1 
ATOM   2766  O  O   . ARG A  1 348 ? -3.750  -2.215  7.493   1.00 2.00  ? 348  ARG A O   1 
ATOM   2767  C  CB  . ARG A  1 348 ? -2.673  0.458   7.602   1.00 2.00  ? 348  ARG A CB  1 
ATOM   2768  C  CG  . ARG A  1 348 ? -1.892  1.684   7.266   1.00 2.00  ? 348  ARG A CG  1 
ATOM   2769  C  CD  . ARG A  1 348 ? -1.012  2.055   8.412   1.00 2.00  ? 348  ARG A CD  1 
ATOM   2770  N  NE  . ARG A  1 348 ? -0.310  3.302   8.161   1.00 2.00  ? 348  ARG A NE  1 
ATOM   2771  C  CZ  . ARG A  1 348 ? 0.786   3.667   8.811   1.00 2.04  ? 348  ARG A CZ  1 
ATOM   2772  N  NH1 . ARG A  1 348 ? 1.295   2.871   9.747   1.00 2.00  ? 348  ARG A NH1 1 
ATOM   2773  N  NH2 . ARG A  1 348 ? 1.375   4.821   8.523   1.00 2.00  ? 348  ARG A NH2 1 
ATOM   2774  N  N   . PHE A  1 349 ? -5.540  -1.312  6.491   1.00 2.00  ? 349  PHE A N   1 
ATOM   2775  C  CA  . PHE A  1 349 ? -6.386  -2.433  6.857   1.00 2.00  ? 349  PHE A CA  1 
ATOM   2776  C  C   . PHE A  1 349 ? -5.724  -3.673  6.270   1.00 2.06  ? 349  PHE A C   1 
ATOM   2777  O  O   . PHE A  1 349 ? -5.814  -4.775  6.815   1.00 2.84  ? 349  PHE A O   1 
ATOM   2778  C  CB  . PHE A  1 349 ? -7.797  -2.241  6.289   1.00 2.00  ? 349  PHE A CB  1 
ATOM   2779  C  CG  . PHE A  1 349 ? -7.871  -2.301  4.782   1.00 2.00  ? 349  PHE A CG  1 
ATOM   2780  C  CD1 . PHE A  1 349 ? -7.923  -3.525  4.119   1.00 2.00  ? 349  PHE A CD1 1 
ATOM   2781  C  CD2 . PHE A  1 349 ? -7.897  -1.135  4.029   1.00 2.00  ? 349  PHE A CD2 1 
ATOM   2782  C  CE1 . PHE A  1 349 ? -8.000  -3.585  2.738   1.00 2.00  ? 349  PHE A CE1 1 
ATOM   2783  C  CE2 . PHE A  1 349 ? -7.973  -1.186  2.647   1.00 2.00  ? 349  PHE A CE2 1 
ATOM   2784  C  CZ  . PHE A  1 349 ? -8.024  -2.413  2.000   1.00 2.00  ? 349  PHE A CZ  1 
ATOM   2785  N  N   . GLY A  1 350 ? -5.032  -3.466  5.159   1.00 2.00  ? 350  GLY A N   1 
ATOM   2786  C  CA  . GLY A  1 350 ? -4.356  -4.557  4.493   1.00 2.00  ? 350  GLY A CA  1 
ATOM   2787  C  C   . GLY A  1 350 ? -3.254  -5.204  5.303   1.00 2.33  ? 350  GLY A C   1 
ATOM   2788  O  O   . GLY A  1 350 ? -2.792  -6.278  4.930   1.00 3.14  ? 350  GLY A O   1 
ATOM   2789  N  N   . HIS A  1 351 ? -2.819  -4.572  6.394   1.00 3.98  ? 351  HIS A N   1 
ATOM   2790  C  CA  . HIS A  1 351 ? -1.756  -5.151  7.223   1.00 2.00  ? 351  HIS A CA  1 
ATOM   2791  C  C   . HIS A  1 351 ? -2.276  -6.398  7.883   1.00 2.00  ? 351  HIS A C   1 
ATOM   2792  O  O   . HIS A  1 351 ? -1.506  -7.225  8.360   1.00 2.00  ? 351  HIS A O   1 
ATOM   2793  C  CB  . HIS A  1 351 ? -1.293  -4.177  8.308   1.00 2.00  ? 351  HIS A CB  1 
ATOM   2794  C  CG  . HIS A  1 351 ? -0.237  -3.222  7.853   1.00 2.00  ? 351  HIS A CG  1 
ATOM   2795  N  ND1 . HIS A  1 351 ? 0.106   -2.095  8.569   1.00 2.09  ? 351  HIS A ND1 1 
ATOM   2796  C  CD2 . HIS A  1 351 ? 0.557   -3.227  6.756   1.00 2.00  ? 351  HIS A CD2 1 
ATOM   2797  C  CE1 . HIS A  1 351 ? 1.064   -1.447  7.931   1.00 2.92  ? 351  HIS A CE1 1 
ATOM   2798  N  NE2 . HIS A  1 351 ? 1.357   -2.113  6.829   1.00 2.00  ? 351  HIS A NE2 1 
ATOM   2799  N  N   . MET A  1 352 ? -3.598  -6.521  7.892   1.00 2.00  ? 352  MET A N   1 
ATOM   2800  C  CA  . MET A  1 352 ? -4.266  -7.654  8.502   1.00 2.00  ? 352  MET A CA  1 
ATOM   2801  C  C   . MET A  1 352 ? -4.735  -8.679  7.479   1.00 2.00  ? 352  MET A C   1 
ATOM   2802  O  O   . MET A  1 352 ? -5.635  -9.474  7.747   1.00 2.00  ? 352  MET A O   1 
ATOM   2803  C  CB  . MET A  1 352 ? -5.437  -7.149  9.341   1.00 3.36  ? 352  MET A CB  1 
ATOM   2804  C  CG  . MET A  1 352 ? -4.992  -6.233  10.475  1.00 2.66  ? 352  MET A CG  1 
ATOM   2805  S  SD  . MET A  1 352 ? -6.296  -5.947  11.675  1.00 5.70  ? 352  MET A SD  1 
ATOM   2806  C  CE  . MET A  1 352 ? -5.727  -4.399  12.464  1.00 3.00  ? 352  MET A CE  1 
ATOM   2807  N  N   . GLU A  1 353 ? -4.105  -8.657  6.308   1.00 2.16  ? 353  GLU A N   1 
ATOM   2808  C  CA  . GLU A  1 353 ? -4.432  -9.582  5.231   1.00 2.00  ? 353  GLU A CA  1 
ATOM   2809  C  C   . GLU A  1 353 ? -3.189  -10.333 4.813   1.00 2.00  ? 353  GLU A C   1 
ATOM   2810  O  O   . GLU A  1 353 ? -3.193  -11.071 3.840   1.00 2.00  ? 353  GLU A O   1 
ATOM   2811  C  CB  . GLU A  1 353 ? -5.006  -8.831  4.035   1.00 2.00  ? 353  GLU A CB  1 
ATOM   2812  C  CG  . GLU A  1 353 ? -6.274  -8.096  4.358   1.00 2.00  ? 353  GLU A CG  1 
ATOM   2813  C  CD  . GLU A  1 353 ? -6.901  -7.496  3.145   1.00 2.00  ? 353  GLU A CD  1 
ATOM   2814  O  OE1 . GLU A  1 353 ? -6.148  -7.062  2.262   1.00 2.41  ? 353  GLU A OE1 1 
ATOM   2815  O  OE2 . GLU A  1 353 ? -8.140  -7.442  3.073   1.00 2.00  ? 353  GLU A OE2 1 
ATOM   2816  N  N   . VAL A  1 354 ? -2.120  -10.129 5.565   1.00 2.00  ? 354  VAL A N   1 
ATOM   2817  C  CA  . VAL A  1 354 ? -0.860  -10.795 5.305   1.00 2.00  ? 354  VAL A CA  1 
ATOM   2818  C  C   . VAL A  1 354 ? -0.793  -12.115 6.059   1.00 2.36  ? 354  VAL A C   1 
ATOM   2819  O  O   . VAL A  1 354 ? -0.723  -12.123 7.290   1.00 2.00  ? 354  VAL A O   1 
ATOM   2820  C  CB  . VAL A  1 354 ? 0.297   -9.980  5.798   1.00 2.00  ? 354  VAL A CB  1 
ATOM   2821  C  CG1 . VAL A  1 354 ? 1.569   -10.674 5.403   1.00 3.07  ? 354  VAL A CG1 1 
ATOM   2822  C  CG2 . VAL A  1 354 ? 0.195   -8.564  5.287   1.00 2.00  ? 354  VAL A CG2 1 
ATOM   2823  N  N   . PRO A  1 355 ? -0.775  -13.244 5.332   1.00 2.00  ? 355  PRO A N   1 
ATOM   2824  C  CA  . PRO A  1 355 ? -0.715  -14.597 5.888   1.00 2.00  ? 355  PRO A CA  1 
ATOM   2825  C  C   . PRO A  1 355 ? 0.661   -14.891 6.486   1.00 2.90  ? 355  PRO A C   1 
ATOM   2826  O  O   . PRO A  1 355 ? 1.655   -14.264 6.110   1.00 3.20  ? 355  PRO A O   1 
ATOM   2827  C  CB  . PRO A  1 355 ? -1.020  -15.457 4.683   1.00 2.00  ? 355  PRO A CB  1 
ATOM   2828  C  CG  . PRO A  1 355 ? -0.287  -14.731 3.615   1.00 2.00  ? 355  PRO A CG  1 
ATOM   2829  C  CD  . PRO A  1 355 ? -0.660  -13.288 3.866   1.00 2.00  ? 355  PRO A CD  1 
ATOM   2830  N  N   . SER A  1 356 ? 0.720   -15.856 7.401   1.00 3.04  ? 356  SER A N   1 
ATOM   2831  C  CA  . SER A  1 356 ? 1.967   -16.209 8.085   1.00 2.00  ? 356  SER A CA  1 
ATOM   2832  C  C   . SER A  1 356 ? 3.161   -16.625 7.230   1.00 2.02  ? 356  SER A C   1 
ATOM   2833  O  O   . SER A  1 356 ? 4.304   -16.366 7.609   1.00 2.32  ? 356  SER A O   1 
ATOM   2834  C  CB  . SER A  1 356 ? 1.711   -17.329 9.086   1.00 2.10  ? 356  SER A CB  1 
ATOM   2835  O  OG  . SER A  1 356 ? 1.526   -18.567 8.419   1.00 2.71  ? 356  SER A OG  1 
ATOM   2836  N  N   . THR A  1 357 ? 2.909   -17.268 6.092   1.00 2.00  ? 357  THR A N   1 
ATOM   2837  C  CA  . THR A  1 357 ? 3.997   -17.745 5.245   1.00 2.00  ? 357  THR A CA  1 
ATOM   2838  C  C   . THR A  1 357 ? 3.872   -17.338 3.788   1.00 2.00  ? 357  THR A C   1 
ATOM   2839  O  O   . THR A  1 357 ? 2.816   -16.900 3.352   1.00 3.40  ? 357  THR A O   1 
ATOM   2840  C  CB  . THR A  1 357 ? 4.045   -19.260 5.241   1.00 2.13  ? 357  THR A CB  1 
ATOM   2841  O  OG1 . THR A  1 357 ? 3.062   -19.749 4.318   1.00 5.01  ? 357  THR A OG1 1 
ATOM   2842  C  CG2 . THR A  1 357 ? 3.726   -19.805 6.615   1.00 2.81  ? 357  THR A CG2 1 
ATOM   2843  N  N   . VAL A  1 358 ? 4.960   -17.523 3.040   1.00 2.51  ? 358  VAL A N   1 
ATOM   2844  C  CA  . VAL A  1 358 ? 5.020   -17.226 1.604   1.00 2.00  ? 358  VAL A CA  1 
ATOM   2845  C  C   . VAL A  1 358 ? 5.513   -18.486 0.879   1.00 2.00  ? 358  VAL A C   1 
ATOM   2846  O  O   . VAL A  1 358 ? 6.579   -19.009 1.196   1.00 2.00  ? 358  VAL A O   1 
ATOM   2847  C  CB  . VAL A  1 358 ? 5.982   -16.045 1.311   1.00 2.00  ? 358  VAL A CB  1 
ATOM   2848  C  CG1 . VAL A  1 358 ? 6.481   -16.120 -0.114  1.00 2.00  ? 358  VAL A CG1 1 
ATOM   2849  C  CG2 . VAL A  1 358 ? 5.265   -14.716 1.534   1.00 2.00  ? 358  VAL A CG2 1 
ATOM   2850  N  N   . SER A  1 359 ? 4.737   -18.958 -0.097  1.00 3.42  ? 359  SER A N   1 
ATOM   2851  C  CA  . SER A  1 359 ? 5.054   -20.181 -0.852  1.00 3.26  ? 359  SER A CA  1 
ATOM   2852  C  C   . SER A  1 359 ? 5.738   -20.028 -2.207  1.00 3.74  ? 359  SER A C   1 
ATOM   2853  O  O   . SER A  1 359 ? 5.793   -18.938 -2.775  1.00 6.42  ? 359  SER A O   1 
ATOM   2854  C  CB  . SER A  1 359 ? 3.779   -20.999 -1.072  1.00 3.93  ? 359  SER A CB  1 
ATOM   2855  O  OG  . SER A  1 359 ? 3.777   -22.165 -0.271  1.00 6.39  ? 359  SER A OG  1 
ATOM   2856  N  N   . ARG A  1 360 ? 6.237   -21.154 -2.719  1.00 3.51  ? 360  ARG A N   1 
ATOM   2857  C  CA  . ARG A  1 360 ? 6.918   -21.239 -4.018  1.00 3.08  ? 360  ARG A CA  1 
ATOM   2858  C  C   . ARG A  1 360 ? 6.462   -22.513 -4.744  1.00 3.87  ? 360  ARG A C   1 
ATOM   2859  O  O   . ARG A  1 360 ? 6.685   -23.621 -4.260  1.00 3.70  ? 360  ARG A O   1 
ATOM   2860  C  CB  . ARG A  1 360 ? 8.442   -21.272 -3.823  1.00 2.06  ? 360  ARG A CB  1 
ATOM   2861  C  CG  . ARG A  1 360 ? 9.156   -19.956 -4.115  1.00 2.00  ? 360  ARG A CG  1 
ATOM   2862  C  CD  . ARG A  1 360 ? 9.732   -19.296 -2.865  1.00 2.00  ? 360  ARG A CD  1 
ATOM   2863  N  NE  . ARG A  1 360 ? 11.068  -19.773 -2.500  1.00 2.01  ? 360  ARG A NE  1 
ATOM   2864  C  CZ  . ARG A  1 360 ? 11.350  -21.005 -2.085  1.00 2.00  ? 360  ARG A CZ  1 
ATOM   2865  N  NH1 . ARG A  1 360 ? 10.390  -21.911 -1.977  1.00 2.00  ? 360  ARG A NH1 1 
ATOM   2866  N  NH2 . ARG A  1 360 ? 12.596  -21.326 -1.763  1.00 2.00  ? 360  ARG A NH2 1 
ATOM   2867  N  N   . LEU A  1 361 ? 5.853   -22.367 -5.917  1.00 3.68  ? 361  LEU A N   1 
ATOM   2868  C  CA  . LEU A  1 361 ? 5.352   -23.531 -6.634  1.00 3.76  ? 361  LEU A CA  1 
ATOM   2869  C  C   . LEU A  1 361 ? 6.026   -23.881 -7.911  1.00 6.60  ? 361  LEU A C   1 
ATOM   2870  O  O   . LEU A  1 361 ? 6.469   -23.028 -8.699  1.00 5.60  ? 361  LEU A O   1 
ATOM   2871  C  CB  . LEU A  1 361 ? 3.865   -23.354 -6.921  1.00 4.35  ? 361  LEU A CB  1 
ATOM   2872  C  CG  . LEU A  1 361 ? 2.935   -22.869 -5.814  1.00 3.61  ? 361  LEU A CG  1 
ATOM   2873  C  CD1 . LEU A  1 361 ? 1.532   -22.658 -6.346  1.00 2.27  ? 361  LEU A CD1 1 
ATOM   2874  C  CD2 . LEU A  1 361 ? 2.930   -23.837 -4.643  1.00 4.62  ? 361  LEU A CD2 1 
ATOM   2875  N  N   . ASP A  1 362 ? 6.093   -25.164 -8.113  1.00 8.88  ? 362  ASP A N   1 
ATOM   2876  C  CA  . ASP A  1 362 ? 6.697   -25.885 -9.263  1.00 8.80  ? 362  ASP A CA  1 
ATOM   2877  C  C   . ASP A  1 362 ? 5.787   -25.871 -10.519 1.00 7.18  ? 362  ASP A C   1 
ATOM   2878  O  O   . ASP A  1 362 ? 4.558   -25.826 -10.336 1.00 2.77  ? 362  ASP A O   1 
ATOM   2879  C  CB  . ASP A  1 362 ? 6.929   -27.321 -8.842  1.00 14.36 ? 362  ASP A CB  1 
ATOM   2880  C  CG  . ASP A  1 362 ? 7.248   -28.216 -10.020 1.00 19.20 ? 362  ASP A CG  1 
ATOM   2881  O  OD1 . ASP A  1 362 ? 7.761   -27.697 -11.041 1.00 20.85 ? 362  ASP A OD1 1 
ATOM   2882  O  OD2 . ASP A  1 362 ? 6.984   -29.419 -9.924  1.00 21.47 ? 362  ASP A OD2 1 
ATOM   2883  N  N   . GLU A  1 363 ? 6.219   -25.907 -11.783 1.00 8.80  ? 363  GLU A N   1 
ATOM   2884  C  CA  . GLU A  1 363 ? 5.228   -25.680 -12.881 1.00 10.83 ? 363  GLU A CA  1 
ATOM   2885  C  C   . GLU A  1 363 ? 3.910   -26.487 -12.851 1.00 10.54 ? 363  GLU A C   1 
ATOM   2886  O  O   . GLU A  1 363 ? 3.106   -26.324 -13.755 1.00 10.55 ? 363  GLU A O   1 
ATOM   2887  C  CB  . GLU A  1 363 ? 5.883   -25.929 -14.224 1.00 13.06 ? 363  GLU A CB  1 
ATOM   2888  C  CG  . GLU A  1 363 ? 7.105   -26.799 -14.123 1.00 19.10 ? 363  GLU A CG  1 
ATOM   2889  C  CD  . GLU A  1 363 ? 8.375   -26.059 -14.505 1.00 22.04 ? 363  GLU A CD  1 
ATOM   2890  O  OE1 . GLU A  1 363 ? 9.362   -26.146 -13.758 1.00 24.57 ? 363  GLU A OE1 1 
ATOM   2891  O  OE2 . GLU A  1 363 ? 8.379   -25.404 -15.560 1.00 22.91 ? 363  GLU A OE2 1 
ATOM   2892  N  N   . ASN A  1 364 ? 3.653   -27.344 -11.876 1.00 9.01  ? 364  ASN A N   1 
ATOM   2893  C  CA  . ASN A  1 364 ? 2.408   -28.087 -11.860 1.00 8.89  ? 364  ASN A CA  1 
ATOM   2894  C  C   . ASN A  1 364 ? 1.674   -27.537 -10.641 1.00 9.95  ? 364  ASN A C   1 
ATOM   2895  O  O   . ASN A  1 364 ? 0.702   -28.118 -10.150 1.00 8.75  ? 364  ASN A O   1 
ATOM   2896  C  CB  . ASN A  1 364 ? 2.696   -29.572 -11.700 1.00 9.60  ? 364  ASN A CB  1 
ATOM   2897  C  CG  . ASN A  1 364 ? 3.089   -30.223 -13.000 1.00 8.25  ? 364  ASN A CG  1 
ATOM   2898  O  OD1 . ASN A  1 364 ? 3.691   -31.295 -13.012 1.00 7.85  ? 364  ASN A OD1 1 
ATOM   2899  N  ND2 . ASN A  1 364 ? 2.735   -29.585 -14.109 1.00 8.89  ? 364  ASN A ND2 1 
ATOM   2900  N  N   . TYR A  1 365 ? 2.161   -26.387 -10.176 1.00 10.05 ? 365  TYR A N   1 
ATOM   2901  C  CA  . TYR A  1 365 ? 1.627   -25.726 -9.001  1.00 9.12  ? 365  TYR A CA  1 
ATOM   2902  C  C   . TYR A  1 365 ? 1.679   -26.711 -7.851  1.00 11.30 ? 365  TYR A C   1 
ATOM   2903  O  O   . TYR A  1 365 ? 0.702   -26.926 -7.132  1.00 13.26 ? 365  TYR A O   1 
ATOM   2904  C  CB  . TYR A  1 365 ? 0.209   -25.255 -9.250  1.00 7.97  ? 365  TYR A CB  1 
ATOM   2905  C  CG  . TYR A  1 365 ? 0.149   -24.027 -10.119 1.00 7.15  ? 365  TYR A CG  1 
ATOM   2906  C  CD1 . TYR A  1 365 ? 0.111   -22.749 -9.564  1.00 5.90  ? 365  TYR A CD1 1 
ATOM   2907  C  CD2 . TYR A  1 365 ? 0.106   -24.142 -11.500 1.00 6.96  ? 365  TYR A CD2 1 
ATOM   2908  C  CE1 . TYR A  1 365 ? 0.022   -21.619 -10.374 1.00 3.63  ? 365  TYR A CE1 1 
ATOM   2909  C  CE2 . TYR A  1 365 ? 0.018   -23.023 -12.311 1.00 5.52  ? 365  TYR A CE2 1 
ATOM   2910  C  CZ  . TYR A  1 365 ? -0.027  -21.769 -11.748 1.00 4.02  ? 365  TYR A CZ  1 
ATOM   2911  O  OH  . TYR A  1 365 ? -0.146  -20.683 -12.583 1.00 2.60  ? 365  TYR A OH  1 
ATOM   2912  N  N   . GLN A  1 366 ? 2.847   -27.325 -7.715  1.00 11.37 ? 366  GLN A N   1 
ATOM   2913  C  CA  . GLN A  1 366 ? 3.129   -28.283 -6.665  1.00 10.59 ? 366  GLN A CA  1 
ATOM   2914  C  C   . GLN A  1 366 ? 4.227   -27.612 -5.855  1.00 10.27 ? 366  GLN A C   1 
ATOM   2915  O  O   . GLN A  1 366 ? 5.028   -26.869 -6.409  1.00 10.11 ? 366  GLN A O   1 
ATOM   2916  C  CB  . GLN A  1 366 ? 3.638   -29.583 -7.286  1.00 13.70 ? 366  GLN A CB  1 
ATOM   2917  C  CG  . GLN A  1 366 ? 2.594   -30.316 -8.114  1.00 15.56 ? 366  GLN A CG  1 
ATOM   2918  C  CD  . GLN A  1 366 ? 1.399   -30.739 -7.274  1.00 18.07 ? 366  GLN A CD  1 
ATOM   2919  O  OE1 . GLN A  1 366 ? 0.694   -29.898 -6.708  1.00 18.69 ? 366  GLN A OE1 1 
ATOM   2920  N  NE2 . GLN A  1 366 ? 1.172   -32.047 -7.178  1.00 19.34 ? 366  GLN A NE2 1 
ATOM   2921  N  N   . PRO A  1 367 ? 4.274   -27.837 -4.532  1.00 10.56 ? 367  PRO A N   1 
ATOM   2922  C  CA  . PRO A  1 367 ? 5.343   -27.178 -3.769  1.00 9.96  ? 367  PRO A CA  1 
ATOM   2923  C  C   . PRO A  1 367 ? 6.676   -27.500 -4.431  1.00 9.72  ? 367  PRO A C   1 
ATOM   2924  O  O   . PRO A  1 367 ? 7.045   -28.665 -4.529  1.00 10.65 ? 367  PRO A O   1 
ATOM   2925  C  CB  . PRO A  1 367 ? 5.221   -27.810 -2.385  1.00 8.83  ? 367  PRO A CB  1 
ATOM   2926  C  CG  . PRO A  1 367 ? 3.768   -28.129 -2.285  1.00 9.08  ? 367  PRO A CG  1 
ATOM   2927  C  CD  . PRO A  1 367 ? 3.453   -28.691 -3.658  1.00 10.06 ? 367  PRO A CD  1 
ATOM   2928  N  N   . ARG A  1 368 ? 7.406   -26.496 -4.897  1.00 9.53  ? 368  ARG A N   1 
ATOM   2929  C  CA  . ARG A  1 368 ? 8.657   -26.829 -5.549  1.00 11.02 ? 368  ARG A CA  1 
ATOM   2930  C  C   . ARG A  1 368 ? 9.907   -26.707 -4.689  1.00 11.62 ? 368  ARG A C   1 
ATOM   2931  O  O   . ARG A  1 368 ? 10.419  -25.612 -4.422  1.00 10.09 ? 368  ARG A O   1 
ATOM   2932  C  CB  . ARG A  1 368 ? 8.829   -26.032 -6.855  1.00 10.78 ? 368  ARG A CB  1 
ATOM   2933  C  CG  . ARG A  1 368 ? 9.558   -24.709 -6.731  1.00 11.38 ? 368  ARG A CG  1 
ATOM   2934  C  CD  . ARG A  1 368 ? 10.010  -24.180 -8.092  1.00 11.71 ? 368  ARG A CD  1 
ATOM   2935  N  NE  . ARG A  1 368 ? 11.465  -24.090 -8.262  1.00 11.54 ? 368  ARG A NE  1 
ATOM   2936  C  CZ  . ARG A  1 368 ? 12.338  -23.782 -7.299  1.00 12.85 ? 368  ARG A CZ  1 
ATOM   2937  N  NH1 . ARG A  1 368 ? 11.934  -23.539 -6.055  1.00 11.81 ? 368  ARG A NH1 1 
ATOM   2938  N  NH2 . ARG A  1 368 ? 13.630  -23.684 -7.590  1.00 12.20 ? 368  ARG A NH2 1 
ATOM   2939  N  N   . GLY A  1 369 ? 10.396  -27.853 -4.241  1.00 12.34 ? 369  GLY A N   1 
ATOM   2940  C  CA  . GLY A  1 369 ? 11.610  -27.825 -3.465  1.00 15.37 ? 369  GLY A CA  1 
ATOM   2941  C  C   . GLY A  1 369 ? 11.554  -28.315 -2.042  1.00 16.46 ? 369  GLY A C   1 
ATOM   2942  O  O   . GLY A  1 369 ? 10.479  -28.507 -1.474  1.00 16.74 ? 369  GLY A O   1 
ATOM   2943  N  N   . PRO A  1 370 ? 12.739  -28.516 -1.444  1.00 17.41 ? 370  PRO A N   1 
ATOM   2944  C  CA  . PRO A  1 370 ? 12.981  -28.985 -0.076  1.00 17.02 ? 370  PRO A CA  1 
ATOM   2945  C  C   . PRO A  1 370 ? 12.547  -27.931 0.943   1.00 18.06 ? 370  PRO A C   1 
ATOM   2946  O  O   . PRO A  1 370 ? 12.292  -28.236 2.114   1.00 17.37 ? 370  PRO A O   1 
ATOM   2947  C  CB  . PRO A  1 370 ? 14.488  -29.191 -0.063  1.00 17.48 ? 370  PRO A CB  1 
ATOM   2948  C  CG  . PRO A  1 370 ? 14.967  -28.044 -0.944  1.00 16.50 ? 370  PRO A CG  1 
ATOM   2949  C  CD  . PRO A  1 370 ? 14.013  -28.155 -2.104  1.00 16.58 ? 370  PRO A CD  1 
ATOM   2950  N  N   . GLU A  1 371 ? 12.480  -26.686 0.478   1.00 18.42 ? 371  GLU A N   1 
ATOM   2951  C  CA  . GLU A  1 371 ? 12.100  -25.561 1.319   1.00 17.74 ? 371  GLU A CA  1 
ATOM   2952  C  C   . GLU A  1 371 ? 11.207  -24.614 0.512   1.00 15.88 ? 371  GLU A C   1 
ATOM   2953  O  O   . GLU A  1 371 ? 11.573  -23.468 0.233   1.00 15.35 ? 371  GLU A O   1 
ATOM   2954  C  CB  . GLU A  1 371 ? 13.362  -24.833 1.807   1.00 19.38 ? 371  GLU A CB  1 
ATOM   2955  C  CG  . GLU A  1 371 ? 14.505  -25.777 2.199   1.00 22.22 ? 371  GLU A CG  1 
ATOM   2956  C  CD  . GLU A  1 371 ? 15.715  -25.048 2.761   1.00 23.88 ? 371  GLU A CD  1 
ATOM   2957  O  OE1 . GLU A  1 371 ? 16.097  -23.998 2.199   1.00 24.47 ? 371  GLU A OE1 1 
ATOM   2958  O  OE2 . GLU A  1 371 ? 16.294  -25.535 3.760   1.00 25.52 ? 371  GLU A OE2 1 
ATOM   2959  N  N   . ALA A  1 372 ? 10.032  -25.115 0.141   1.00 13.48 ? 372  ALA A N   1 
ATOM   2960  C  CA  . ALA A  1 372 ? 9.065   -24.348 -0.631  1.00 12.17 ? 372  ALA A CA  1 
ATOM   2961  C  C   . ALA A  1 372 ? 8.340   -23.282 0.194   1.00 11.62 ? 372  ALA A C   1 
ATOM   2962  O  O   . ALA A  1 372 ? 8.256   -22.127 -0.229  1.00 12.99 ? 372  ALA A O   1 
ATOM   2963  C  CB  . ALA A  1 372 ? 8.052   -25.286 -1.255  1.00 13.18 ? 372  ALA A CB  1 
ATOM   2964  N  N   . GLU A  1 373 ? 7.804   -23.673 1.353   1.00 8.23  ? 373  GLU A N   1 
ATOM   2965  C  CA  . GLU A  1 373 ? 7.087   -22.743 2.228   1.00 5.33  ? 373  GLU A CA  1 
ATOM   2966  C  C   . GLU A  1 373 ? 8.058   -22.041 3.138   1.00 4.02  ? 373  GLU A C   1 
ATOM   2967  O  O   . GLU A  1 373 ? 8.645   -22.660 4.014   1.00 5.46  ? 373  GLU A O   1 
ATOM   2968  C  CB  . GLU A  1 373 ? 6.079   -23.468 3.099   1.00 5.79  ? 373  GLU A CB  1 
ATOM   2969  C  CG  . GLU A  1 373 ? 4.653   -23.236 2.707   1.00 10.05 ? 373  GLU A CG  1 
ATOM   2970  C  CD  . GLU A  1 373 ? 3.717   -23.378 3.888   1.00 12.30 ? 373  GLU A CD  1 
ATOM   2971  O  OE1 . GLU A  1 373 ? 3.648   -22.437 4.711   1.00 12.73 ? 373  GLU A OE1 1 
ATOM   2972  O  OE2 . GLU A  1 373 ? 3.060   -24.435 4.002   1.00 14.87 ? 373  GLU A OE2 1 
ATOM   2973  N  N   . LEU A  1 374 ? 8.213   -20.742 2.952   1.00 2.60  ? 374  LEU A N   1 
ATOM   2974  C  CA  . LEU A  1 374 ? 9.147   -19.994 3.766   1.00 2.00  ? 374  LEU A CA  1 
ATOM   2975  C  C   . LEU A  1 374 ? 8.438   -19.061 4.750   1.00 2.00  ? 374  LEU A C   1 
ATOM   2976  O  O   . LEU A  1 374 ? 7.523   -18.326 4.371   1.00 2.39  ? 374  LEU A O   1 
ATOM   2977  C  CB  . LEU A  1 374 ? 10.082  -19.195 2.846   1.00 2.12  ? 374  LEU A CB  1 
ATOM   2978  C  CG  . LEU A  1 374 ? 11.044  -19.966 1.931   1.00 2.00  ? 374  LEU A CG  1 
ATOM   2979  C  CD1 . LEU A  1 374 ? 11.622  -19.054 0.860   1.00 2.00  ? 374  LEU A CD1 1 
ATOM   2980  C  CD2 . LEU A  1 374 ? 12.152  -20.553 2.768   1.00 2.43  ? 374  LEU A CD2 1 
ATOM   2981  N  N   . PRO A  1 375 ? 8.831   -19.101 6.039   1.00 2.00  ? 375  PRO A N   1 
ATOM   2982  C  CA  . PRO A  1 375 ? 8.179   -18.212 6.999   1.00 2.25  ? 375  PRO A CA  1 
ATOM   2983  C  C   . PRO A  1 375 ? 8.415   -16.786 6.516   1.00 2.85  ? 375  PRO A C   1 
ATOM   2984  O  O   . PRO A  1 375 ? 9.539   -16.408 6.166   1.00 2.00  ? 375  PRO A O   1 
ATOM   2985  C  CB  . PRO A  1 375 ? 8.897   -18.529 8.313   1.00 2.00  ? 375  PRO A CB  1 
ATOM   2986  C  CG  . PRO A  1 375 ? 10.253  -18.945 7.867   1.00 2.00  ? 375  PRO A CG  1 
ATOM   2987  C  CD  . PRO A  1 375 ? 9.929   -19.838 6.686   1.00 2.51  ? 375  PRO A CD  1 
ATOM   2988  N  N   . LEU A  1 376 ? 7.345   -16.002 6.488   1.00 2.70  ? 376  LEU A N   1 
ATOM   2989  C  CA  . LEU A  1 376 ? 7.433   -14.642 6.003   1.00 2.00  ? 376  LEU A CA  1 
ATOM   2990  C  C   . LEU A  1 376 ? 8.585   -13.806 6.548   1.00 2.07  ? 376  LEU A C   1 
ATOM   2991  O  O   . LEU A  1 376 ? 9.372   -13.242 5.790   1.00 2.73  ? 376  LEU A O   1 
ATOM   2992  C  CB  . LEU A  1 376 ? 6.148   -13.869 6.317   1.00 3.38  ? 376  LEU A CB  1 
ATOM   2993  C  CG  . LEU A  1 376 ? 5.782   -12.714 5.365   1.00 3.54  ? 376  LEU A CG  1 
ATOM   2994  C  CD1 . LEU A  1 376 ? 4.919   -11.685 6.075   1.00 2.00  ? 376  LEU A CD1 1 
ATOM   2995  C  CD2 . LEU A  1 376 ? 7.051   -12.076 4.808   1.00 2.00  ? 376  LEU A CD2 1 
ATOM   2996  N  N   . HIS A  1 377 ? 8.653   -13.752 7.862   1.00 2.63  ? 377  HIS A N   1 
ATOM   2997  C  CA  . HIS A  1 377 ? 9.648   -12.927 8.535   1.00 2.56  ? 377  HIS A CA  1 
ATOM   2998  C  C   . HIS A  1 377 ? 11.082  -12.989 7.970   1.00 2.00  ? 377  HIS A C   1 
ATOM   2999  O  O   . HIS A  1 377 ? 11.822  -12.012 8.117   1.00 2.00  ? 377  HIS A O   1 
ATOM   3000  C  CB  . HIS A  1 377 ? 9.611   -13.310 9.989   1.00 2.00  ? 377  HIS A CB  1 
ATOM   3001  C  CG  . HIS A  1 377 ? 10.708  -14.299 10.407  1.00 2.00  ? 377  HIS A CG  1 
ATOM   3002  N  ND1 . HIS A  1 377 ? 10.594  -15.667 10.237  1.00 2.00  ? 377  HIS A ND1 1 
ATOM   3003  C  CD2 . HIS A  1 377 ? 11.905  -14.053 10.958  1.00 2.00  ? 377  HIS A CD2 1 
ATOM   3004  C  CE1 . HIS A  1 377 ? 11.722  -16.222 10.657  1.00 2.00  ? 377  HIS A CE1 1 
ATOM   3005  N  NE2 . HIS A  1 377 ? 12.516  -15.266 11.100  1.00 2.00  ? 377  HIS A NE2 1 
ATOM   3006  N  N   . THR A  1 378 ? 11.464  -14.106 7.311   1.00 2.00  ? 378  THR A N   1 
ATOM   3007  C  CA  . THR A  1 378 ? 12.807  -14.215 6.682   1.00 2.00  ? 378  THR A CA  1 
ATOM   3008  C  C   . THR A  1 378 ? 12.762  -13.767 5.233   1.00 2.34  ? 378  THR A C   1 
ATOM   3009  O  O   . THR A  1 378 ? 13.588  -14.169 4.418   1.00 2.97  ? 378  THR A O   1 
ATOM   3010  C  CB  . THR A  1 378 ? 13.325  -15.647 6.732   1.00 2.00  ? 378  THR A CB  1 
ATOM   3011  O  OG1 . THR A  1 378 ? 12.617  -16.450 5.779   1.00 2.00  ? 378  THR A OG1 1 
ATOM   3012  C  CG2 . THR A  1 378 ? 13.151  -16.212 8.143   1.00 2.00  ? 378  THR A CG2 1 
ATOM   3013  N  N   . LEU A  1 379 ? 11.795  -12.921 4.917   1.00 2.00  ? 379  LEU A N   1 
ATOM   3014  C  CA  . LEU A  1 379 ? 11.644  -12.451 3.557   1.00 2.03  ? 379  LEU A CA  1 
ATOM   3015  C  C   . LEU A  1 379 ? 11.592  -10.940 3.429   1.00 2.65  ? 379  LEU A C   1 
ATOM   3016  O  O   . LEU A  1 379 ? 11.613  -10.426 2.316   1.00 3.63  ? 379  LEU A O   1 
ATOM   3017  C  CB  . LEU A  1 379 ? 10.393  -13.064 2.925   1.00 2.00  ? 379  LEU A CB  1 
ATOM   3018  C  CG  . LEU A  1 379 ? 10.484  -14.529 2.507   1.00 2.00  ? 379  LEU A CG  1 
ATOM   3019  C  CD1 . LEU A  1 379 ? 9.096   -15.083 2.288   1.00 2.00  ? 379  LEU A CD1 1 
ATOM   3020  C  CD2 . LEU A  1 379 ? 11.308  -14.651 1.249   1.00 2.00  ? 379  LEU A CD2 1 
ATOM   3021  N  N   . PHE A  1 380 ? 11.508  -10.210 4.536   1.00 2.00  ? 380  PHE A N   1 
ATOM   3022  C  CA  . PHE A  1 380 ? 11.497  -8.760  4.392   1.00 2.00  ? 380  PHE A CA  1 
ATOM   3023  C  C   . PHE A  1 380 ? 12.868  -8.400  3.828   1.00 2.33  ? 380  PHE A C   1 
ATOM   3024  O  O   . PHE A  1 380 ? 13.894  -8.901  4.289   1.00 2.92  ? 380  PHE A O   1 
ATOM   3025  C  CB  . PHE A  1 380 ? 11.294  -8.044  5.731   1.00 2.00  ? 380  PHE A CB  1 
ATOM   3026  C  CG  . PHE A  1 380 ? 10.088  -8.496  6.475   1.00 2.00  ? 380  PHE A CG  1 
ATOM   3027  C  CD1 . PHE A  1 380 ? 8.834   -8.416  5.904   1.00 2.00  ? 380  PHE A CD1 1 
ATOM   3028  C  CD2 . PHE A  1 380 ? 10.212  -9.051  7.736   1.00 2.64  ? 380  PHE A CD2 1 
ATOM   3029  C  CE1 . PHE A  1 380 ? 7.716   -8.892  6.581   1.00 2.00  ? 380  PHE A CE1 1 
ATOM   3030  C  CE2 . PHE A  1 380 ? 9.106   -9.526  8.416   1.00 2.00  ? 380  PHE A CE2 1 
ATOM   3031  C  CZ  . PHE A  1 380 ? 7.853   -9.448  7.835   1.00 2.00  ? 380  PHE A CZ  1 
ATOM   3032  N  N   . PHE A  1 381 ? 12.881  -7.554  2.810   1.00 2.20  ? 381  PHE A N   1 
ATOM   3033  C  CA  . PHE A  1 381 ? 14.125  -7.129  2.195   1.00 3.14  ? 381  PHE A CA  1 
ATOM   3034  C  C   . PHE A  1 381 ? 14.948  -8.248  1.566   1.00 2.03  ? 381  PHE A C   1 
ATOM   3035  O  O   . PHE A  1 381 ? 16.161  -8.115  1.414   1.00 2.04  ? 381  PHE A O   1 
ATOM   3036  C  CB  . PHE A  1 381 ? 14.958  -6.371  3.226   1.00 2.08  ? 381  PHE A CB  1 
ATOM   3037  C  CG  . PHE A  1 381 ? 14.392  -5.029  3.572   1.00 3.60  ? 381  PHE A CG  1 
ATOM   3038  C  CD1 . PHE A  1 381 ? 14.405  -3.998  2.636   1.00 4.90  ? 381  PHE A CD1 1 
ATOM   3039  C  CD2 . PHE A  1 381 ? 13.835  -4.791  4.820   1.00 4.19  ? 381  PHE A CD2 1 
ATOM   3040  C  CE1 . PHE A  1 381 ? 13.876  -2.745  2.936   1.00 4.41  ? 381  PHE A CE1 1 
ATOM   3041  C  CE2 . PHE A  1 381 ? 13.301  -3.539  5.132   1.00 5.14  ? 381  PHE A CE2 1 
ATOM   3042  C  CZ  . PHE A  1 381 ? 13.324  -2.516  4.185   1.00 4.98  ? 381  PHE A CZ  1 
ATOM   3043  N  N   . ASN A  1 382 ? 14.294  -9.338  1.173   1.00 2.43  ? 382  ASN A N   1 
ATOM   3044  C  CA  . ASN A  1 382 ? 15.011  -10.451 0.555   1.00 3.02  ? 382  ASN A CA  1 
ATOM   3045  C  C   . ASN A  1 382 ? 15.056  -10.338 -0.970  1.00 3.81  ? 382  ASN A C   1 
ATOM   3046  O  O   . ASN A  1 382 ? 14.048  -10.066 -1.613  1.00 5.31  ? 382  ASN A O   1 
ATOM   3047  C  CB  . ASN A  1 382 ? 14.382  -11.778 0.959   1.00 2.00  ? 382  ASN A CB  1 
ATOM   3048  C  CG  . ASN A  1 382 ? 15.345  -12.927 0.828   1.00 2.00  ? 382  ASN A CG  1 
ATOM   3049  O  OD1 . ASN A  1 382 ? 15.648  -13.377 -0.273  1.00 3.19  ? 382  ASN A OD1 1 
ATOM   3050  N  ND2 . ASN A  1 382 ? 15.856  -13.399 1.958   1.00 2.68  ? 382  ASN A ND2 1 
ATOM   3051  N  N   . THR A  1 383 ? 16.233  -10.556 -1.542  1.00 3.11  ? 383  THR A N   1 
ATOM   3052  C  CA  . THR A  1 383 ? 16.418  -10.456 -2.979  1.00 2.00  ? 383  THR A CA  1 
ATOM   3053  C  C   . THR A  1 383 ? 17.060  -11.702 -3.571  1.00 2.90  ? 383  THR A C   1 
ATOM   3054  O  O   . THR A  1 383 ? 16.712  -12.128 -4.684  1.00 2.00  ? 383  THR A O   1 
ATOM   3055  C  CB  . THR A  1 383 ? 17.309  -9.260  -3.314  1.00 2.00  ? 383  THR A CB  1 
ATOM   3056  O  OG1 . THR A  1 383 ? 18.341  -9.157  -2.323  1.00 2.94  ? 383  THR A OG1 1 
ATOM   3057  C  CG2 . THR A  1 383 ? 16.503  -7.979  -3.351  1.00 2.00  ? 383  THR A CG2 1 
ATOM   3058  N  N   . TRP A  1 384 ? 18.002  -12.286 -2.832  1.00 3.02  ? 384  TRP A N   1 
ATOM   3059  C  CA  . TRP A  1 384 ? 18.685  -13.466 -3.332  1.00 2.44  ? 384  TRP A CA  1 
ATOM   3060  C  C   . TRP A  1 384 ? 17.733  -14.609 -3.585  1.00 2.35  ? 384  TRP A C   1 
ATOM   3061  O  O   . TRP A  1 384 ? 17.857  -15.298 -4.599  1.00 3.39  ? 384  TRP A O   1 
ATOM   3062  C  CB  . TRP A  1 384 ? 19.796  -13.909 -2.392  1.00 2.63  ? 384  TRP A CB  1 
ATOM   3063  C  CG  . TRP A  1 384 ? 19.370  -14.289 -1.039  1.00 2.81  ? 384  TRP A CG  1 
ATOM   3064  C  CD1 . TRP A  1 384 ? 19.187  -13.459 0.025   1.00 4.28  ? 384  TRP A CD1 1 
ATOM   3065  C  CD2 . TRP A  1 384 ? 19.184  -15.617 -0.552  1.00 2.43  ? 384  TRP A CD2 1 
ATOM   3066  N  NE1 . TRP A  1 384 ? 18.910  -14.192 1.156   1.00 3.69  ? 384  TRP A NE1 1 
ATOM   3067  C  CE2 . TRP A  1 384 ? 18.902  -15.521 0.825   1.00 2.77  ? 384  TRP A CE2 1 
ATOM   3068  C  CE3 . TRP A  1 384 ? 19.232  -16.881 -1.145  1.00 2.21  ? 384  TRP A CE3 1 
ATOM   3069  C  CZ2 . TRP A  1 384 ? 18.674  -16.640 1.618   1.00 3.09  ? 384  TRP A CZ2 1 
ATOM   3070  C  CZ3 . TRP A  1 384 ? 19.006  -17.992 -0.359  1.00 2.26  ? 384  TRP A CZ3 1 
ATOM   3071  C  CH2 . TRP A  1 384 ? 18.729  -17.865 1.010   1.00 3.34  ? 384  TRP A CH2 1 
ATOM   3072  N  N   . ARG A  1 385 ? 16.780  -14.816 -2.680  1.00 2.05  ? 385  ARG A N   1 
ATOM   3073  C  CA  . ARG A  1 385 ? 15.800  -15.880 -2.882  1.00 3.31  ? 385  ARG A CA  1 
ATOM   3074  C  C   . ARG A  1 385 ? 15.117  -15.730 -4.246  1.00 3.00  ? 385  ARG A C   1 
ATOM   3075  O  O   . ARG A  1 385 ? 14.407  -16.635 -4.690  1.00 2.19  ? 385  ARG A O   1 
ATOM   3076  C  CB  . ARG A  1 385 ? 14.747  -15.877 -1.774  1.00 2.00  ? 385  ARG A CB  1 
ATOM   3077  C  CG  . ARG A  1 385 ? 15.197  -16.554 -0.507  1.00 2.00  ? 385  ARG A CG  1 
ATOM   3078  C  CD  . ARG A  1 385 ? 15.442  -18.039 -0.730  1.00 3.01  ? 385  ARG A CD  1 
ATOM   3079  N  NE  . ARG A  1 385 ? 15.569  -18.747 0.543   1.00 3.91  ? 385  ARG A NE  1 
ATOM   3080  C  CZ  . ARG A  1 385 ? 15.786  -20.052 0.666   1.00 3.34  ? 385  ARG A CZ  1 
ATOM   3081  N  NH1 . ARG A  1 385 ? 15.907  -20.820 -0.413  1.00 3.59  ? 385  ARG A NH1 1 
ATOM   3082  N  NH2 . ARG A  1 385 ? 15.887  -20.586 1.876   1.00 2.40  ? 385  ARG A NH2 1 
ATOM   3083  N  N   . ILE A  1 386 ? 15.323  -14.587 -4.901  1.00 2.64  ? 386  ILE A N   1 
ATOM   3084  C  CA  . ILE A  1 386 ? 14.753  -14.364 -6.227  1.00 3.01  ? 386  ILE A CA  1 
ATOM   3085  C  C   . ILE A  1 386 ? 15.820  -14.610 -7.273  1.00 2.94  ? 386  ILE A C   1 
ATOM   3086  O  O   . ILE A  1 386 ? 15.788  -15.588 -8.024  1.00 2.00  ? 386  ILE A O   1 
ATOM   3087  C  CB  . ILE A  1 386 ? 14.318  -12.914 -6.487  1.00 2.00  ? 386  ILE A CB  1 
ATOM   3088  C  CG1 . ILE A  1 386 ? 13.138  -12.510 -5.619  1.00 3.39  ? 386  ILE A CG1 1 
ATOM   3089  C  CG2 . ILE A  1 386 ? 13.896  -12.783 -7.934  1.00 2.00  ? 386  ILE A CG2 1 
ATOM   3090  C  CD1 . ILE A  1 386 ? 12.662  -11.076 -5.893  1.00 2.00  ? 386  ILE A CD1 1 
ATOM   3091  N  N   . ILE A  1 387 ? 16.751  -13.665 -7.318  1.00 4.10  ? 387  ILE A N   1 
ATOM   3092  C  CA  . ILE A  1 387 ? 17.839  -13.692 -8.271  1.00 5.18  ? 387  ILE A CA  1 
ATOM   3093  C  C   . ILE A  1 387 ? 18.574  -15.001 -8.210  1.00 3.79  ? 387  ILE A C   1 
ATOM   3094  O  O   . ILE A  1 387 ? 18.884  -15.569 -9.251  1.00 4.71  ? 387  ILE A O   1 
ATOM   3095  C  CB  . ILE A  1 387 ? 18.819  -12.511 -8.024  1.00 4.99  ? 387  ILE A CB  1 
ATOM   3096  C  CG1 . ILE A  1 387 ? 18.215  -11.228 -8.604  1.00 3.99  ? 387  ILE A CG1 1 
ATOM   3097  C  CG2 . ILE A  1 387 ? 20.179  -12.793 -8.659  1.00 3.19  ? 387  ILE A CG2 1 
ATOM   3098  C  CD1 . ILE A  1 387 ? 18.616  -9.981  -7.891  1.00 4.49  ? 387  ILE A CD1 1 
ATOM   3099  N  N   . LYS A  1 388 ? 18.821  -15.493 -6.995  1.00 4.01  ? 388  LYS A N   1 
ATOM   3100  C  CA  . LYS A  1 388 ? 19.554  -16.742 -6.817  1.00 3.16  ? 388  LYS A CA  1 
ATOM   3101  C  C   . LYS A  1 388 ? 18.776  -18.018 -6.543  1.00 2.00  ? 388  LYS A C   1 
ATOM   3102  O  O   . LYS A  1 388 ? 19.230  -19.089 -6.908  1.00 2.93  ? 388  LYS A O   1 
ATOM   3103  C  CB  . LYS A  1 388 ? 20.636  -16.569 -5.748  1.00 2.32  ? 388  LYS A CB  1 
ATOM   3104  C  CG  . LYS A  1 388 ? 21.899  -15.946 -6.311  1.00 3.83  ? 388  LYS A CG  1 
ATOM   3105  C  CD  . LYS A  1 388 ? 22.993  -15.819 -5.277  1.00 7.99  ? 388  LYS A CD  1 
ATOM   3106  C  CE  . LYS A  1 388 ? 24.333  -15.477 -5.935  1.00 11.53 ? 388  LYS A CE  1 
ATOM   3107  N  NZ  . LYS A  1 388 ? 24.864  -16.593 -6.800  1.00 14.57 ? 388  LYS A NZ  1 
ATOM   3108  N  N   . ASP A  1 389 ? 17.610  -17.943 -5.923  1.00 2.00  ? 389  ASP A N   1 
ATOM   3109  C  CA  . ASP A  1 389 ? 16.905  -19.186 -5.673  1.00 3.32  ? 389  ASP A CA  1 
ATOM   3110  C  C   . ASP A  1 389 ? 15.617  -19.437 -6.462  1.00 4.42  ? 389  ASP A C   1 
ATOM   3111  O  O   . ASP A  1 389 ? 14.563  -19.635 -5.861  1.00 5.49  ? 389  ASP A O   1 
ATOM   3112  C  CB  . ASP A  1 389 ? 16.629  -19.335 -4.172  1.00 5.05  ? 389  ASP A CB  1 
ATOM   3113  C  CG  . ASP A  1 389 ? 16.012  -20.693 -3.818  1.00 7.73  ? 389  ASP A CG  1 
ATOM   3114  O  OD1 . ASP A  1 389 ? 16.555  -21.738 -4.243  1.00 7.55  ? 389  ASP A OD1 1 
ATOM   3115  O  OD2 . ASP A  1 389 ? 14.984  -20.717 -3.105  1.00 8.43  ? 389  ASP A OD2 1 
ATOM   3116  N  N   . GLY A  1 390 ? 15.680  -19.429 -7.796  1.00 3.89  ? 390  GLY A N   1 
ATOM   3117  C  CA  . GLY A  1 390 ? 14.476  -19.725 -8.565  1.00 2.92  ? 390  GLY A CA  1 
ATOM   3118  C  C   . GLY A  1 390 ? 13.890  -18.800 -9.626  1.00 2.80  ? 390  GLY A C   1 
ATOM   3119  O  O   . GLY A  1 390 ? 13.474  -19.270 -10.684 1.00 2.46  ? 390  GLY A O   1 
ATOM   3120  N  N   . GLY A  1 391 ? 13.838  -17.499 -9.356  1.00 3.92  ? 391  GLY A N   1 
ATOM   3121  C  CA  . GLY A  1 391 ? 13.247  -16.564 -10.306 1.00 5.34  ? 391  GLY A CA  1 
ATOM   3122  C  C   . GLY A  1 391 ? 11.957  -16.011 -9.713  1.00 5.36  ? 391  GLY A C   1 
ATOM   3123  O  O   . GLY A  1 391 ? 11.764  -16.140 -8.509  1.00 8.51  ? 391  GLY A O   1 
ATOM   3124  N  N   . ILE A  1 392 ? 11.081  -15.399 -10.516 1.00 4.26  ? 392  ILE A N   1 
ATOM   3125  C  CA  . ILE A  1 392 ? 9.818   -14.856 -9.991  1.00 3.90  ? 392  ILE A CA  1 
ATOM   3126  C  C   . ILE A  1 392 ? 8.685   -15.779 -10.427 1.00 2.28  ? 392  ILE A C   1 
ATOM   3127  O  O   . ILE A  1 392 ? 7.579   -15.736 -9.886  1.00 2.23  ? 392  ILE A O   1 
ATOM   3128  C  CB  . ILE A  1 392 ? 9.518   -13.396 -10.508 1.00 2.01  ? 392  ILE A CB  1 
ATOM   3129  C  CG1 . ILE A  1 392 ? 8.783   -13.452 -11.861 1.00 2.00  ? 392  ILE A CG1 1 
ATOM   3130  C  CG2 . ILE A  1 392 ? 10.812  -12.580 -10.559 1.00 2.00  ? 392  ILE A CG2 1 
ATOM   3131  C  CD1 . ILE A  1 392 ? 8.934   -12.219 -12.744 1.00 2.00  ? 392  ILE A CD1 1 
ATOM   3132  N  N   . ASP A  1 393 ? 8.956   -16.620 -11.415 1.00 2.00  ? 393  ASP A N   1 
ATOM   3133  C  CA  . ASP A  1 393 ? 7.933   -17.548 -11.881 1.00 3.51  ? 393  ASP A CA  1 
ATOM   3134  C  C   . ASP A  1 393 ? 7.351   -18.355 -10.752 1.00 4.62  ? 393  ASP A C   1 
ATOM   3135  O  O   . ASP A  1 393 ? 6.132   -18.407 -10.598 1.00 7.29  ? 393  ASP A O   1 
ATOM   3136  C  CB  . ASP A  1 393 ? 8.477   -18.466 -12.960 1.00 4.68  ? 393  ASP A CB  1 
ATOM   3137  C  CG  . ASP A  1 393 ? 8.298   -17.870 -14.325 1.00 6.13  ? 393  ASP A CG  1 
ATOM   3138  O  OD1 . ASP A  1 393 ? 8.275   -16.617 -14.382 1.00 6.17  ? 393  ASP A OD1 1 
ATOM   3139  O  OD2 . ASP A  1 393 ? 8.186   -18.602 -15.332 1.00 5.86  ? 393  ASP A OD2 1 
ATOM   3140  N  N   . PRO A  1 394 ? 8.200   -18.989 -9.933  1.00 4.68  ? 394  PRO A N   1 
ATOM   3141  C  CA  . PRO A  1 394 ? 7.689   -19.784 -8.820  1.00 2.76  ? 394  PRO A CA  1 
ATOM   3142  C  C   . PRO A  1 394 ? 6.820   -18.900 -7.900  1.00 2.50  ? 394  PRO A C   1 
ATOM   3143  O  O   . PRO A  1 394 ? 5.757   -19.318 -7.475  1.00 2.58  ? 394  PRO A O   1 
ATOM   3144  C  CB  . PRO A  1 394 ? 8.975   -20.313 -8.150  1.00 2.13  ? 394  PRO A CB  1 
ATOM   3145  C  CG  . PRO A  1 394 ? 9.971   -20.321 -9.295  1.00 2.94  ? 394  PRO A CG  1 
ATOM   3146  C  CD  . PRO A  1 394 ? 9.668   -18.989 -9.918  1.00 4.04  ? 394  PRO A CD  1 
ATOM   3147  N  N   . LEU A  1 395 ? 7.249   -17.666 -7.640  1.00 2.00  ? 395  LEU A N   1 
ATOM   3148  C  CA  . LEU A  1 395 ? 6.493   -16.768 -6.778  1.00 2.62  ? 395  LEU A CA  1 
ATOM   3149  C  C   . LEU A  1 395 ? 5.123   -16.363 -7.341  1.00 6.23  ? 395  LEU A C   1 
ATOM   3150  O  O   . LEU A  1 395 ? 4.130   -16.358 -6.608  1.00 6.36  ? 395  LEU A O   1 
ATOM   3151  C  CB  . LEU A  1 395 ? 7.334   -15.514 -6.454  1.00 2.43  ? 395  LEU A CB  1 
ATOM   3152  C  CG  . LEU A  1 395 ? 8.703   -15.744 -5.784  1.00 2.00  ? 395  LEU A CG  1 
ATOM   3153  C  CD1 . LEU A  1 395 ? 9.552   -14.468 -5.756  1.00 2.00  ? 395  LEU A CD1 1 
ATOM   3154  C  CD2 . LEU A  1 395 ? 8.478   -16.234 -4.369  1.00 2.00  ? 395  LEU A CD2 1 
ATOM   3155  N  N   . VAL A  1 396 ? 5.067   -16.025 -8.629  1.00 3.93  ? 396  VAL A N   1 
ATOM   3156  C  CA  . VAL A  1 396 ? 3.819   -15.613 -9.275  1.00 2.17  ? 396  VAL A CA  1 
ATOM   3157  C  C   . VAL A  1 396 ? 2.818   -16.751 -9.303  1.00 2.00  ? 396  VAL A C   1 
ATOM   3158  O  O   . VAL A  1 396 ? 1.621   -16.524 -9.328  1.00 2.83  ? 396  VAL A O   1 
ATOM   3159  C  CB  . VAL A  1 396 ? 4.063   -15.104 -10.717 1.00 2.00  ? 396  VAL A CB  1 
ATOM   3160  C  CG1 . VAL A  1 396 ? 2.762   -14.910 -11.432 1.00 2.00  ? 396  VAL A CG1 1 
ATOM   3161  C  CG2 . VAL A  1 396 ? 4.836   -13.790 -10.678 1.00 2.00  ? 396  VAL A CG2 1 
ATOM   3162  N  N   . ARG A  1 397 ? 3.285   -17.986 -9.294  1.00 2.00  ? 397  ARG A N   1 
ATOM   3163  C  CA  . ARG A  1 397 ? 2.326   -19.070 -9.271  1.00 2.00  ? 397  ARG A CA  1 
ATOM   3164  C  C   . ARG A  1 397 ? 1.846   -19.080 -7.835  1.00 2.00  ? 397  ARG A C   1 
ATOM   3165  O  O   . ARG A  1 397 ? 0.757   -19.542 -7.526  1.00 3.90  ? 397  ARG A O   1 
ATOM   3166  C  CB  . ARG A  1 397 ? 2.975   -20.410 -9.631  1.00 3.76  ? 397  ARG A CB  1 
ATOM   3167  C  CG  . ARG A  1 397 ? 3.583   -20.451 -11.027 1.00 5.79  ? 397  ARG A CG  1 
ATOM   3168  C  CD  . ARG A  1 397 ? 3.668   -21.872 -11.564 1.00 7.12  ? 397  ARG A CD  1 
ATOM   3169  N  NE  . ARG A  1 397 ? 4.433   -21.910 -12.805 1.00 9.60  ? 397  ARG A NE  1 
ATOM   3170  C  CZ  . ARG A  1 397 ? 5.760   -21.972 -12.860 1.00 10.76 ? 397  ARG A CZ  1 
ATOM   3171  N  NH1 . ARG A  1 397 ? 6.475   -22.012 -11.738 1.00 11.03 ? 397  ARG A NH1 1 
ATOM   3172  N  NH2 . ARG A  1 397 ? 6.374   -21.983 -14.039 1.00 11.07 ? 397  ARG A NH2 1 
ATOM   3173  N  N   . GLY A  1 398 ? 2.666   -18.536 -6.950  1.00 2.00  ? 398  GLY A N   1 
ATOM   3174  C  CA  . GLY A  1 398 ? 2.283   -18.492 -5.555  1.00 2.00  ? 398  GLY A CA  1 
ATOM   3175  C  C   . GLY A  1 398 ? 1.062   -17.618 -5.373  1.00 2.21  ? 398  GLY A C   1 
ATOM   3176  O  O   . GLY A  1 398 ? 0.018   -18.072 -4.888  1.00 2.30  ? 398  GLY A O   1 
ATOM   3177  N  N   . LEU A  1 399 ? 1.207   -16.358 -5.782  1.00 2.32  ? 399  LEU A N   1 
ATOM   3178  C  CA  . LEU A  1 399 ? 0.151   -15.352 -5.696  1.00 2.00  ? 399  LEU A CA  1 
ATOM   3179  C  C   . LEU A  1 399 ? -1.177  -15.804 -6.329  1.00 2.16  ? 399  LEU A C   1 
ATOM   3180  O  O   . LEU A  1 399 ? -2.242  -15.647 -5.725  1.00 2.00  ? 399  LEU A O   1 
ATOM   3181  C  CB  . LEU A  1 399 ? 0.630   -14.042 -6.344  1.00 2.00  ? 399  LEU A CB  1 
ATOM   3182  C  CG  . LEU A  1 399 ? 1.663   -13.157 -5.630  1.00 2.00  ? 399  LEU A CG  1 
ATOM   3183  C  CD1 . LEU A  1 399 ? 2.410   -12.315 -6.650  1.00 2.00  ? 399  LEU A CD1 1 
ATOM   3184  C  CD2 . LEU A  1 399 ? 0.975   -12.266 -4.609  1.00 2.00  ? 399  LEU A CD2 1 
ATOM   3185  N  N   . LEU A  1 400 ? -1.129  -16.376 -7.529  1.00 2.00  ? 400  LEU A N   1 
ATOM   3186  C  CA  . LEU A  1 400 ? -2.359  -16.821 -8.175  1.00 2.00  ? 400  LEU A CA  1 
ATOM   3187  C  C   . LEU A  1 400 ? -3.047  -17.998 -7.479  1.00 2.00  ? 400  LEU A C   1 
ATOM   3188  O  O   . LEU A  1 400 ? -4.274  -18.065 -7.457  1.00 2.00  ? 400  LEU A O   1 
ATOM   3189  C  CB  . LEU A  1 400 ? -2.109  -17.182 -9.647  1.00 2.00  ? 400  LEU A CB  1 
ATOM   3190  C  CG  . LEU A  1 400 ? -1.923  -16.074 -10.694 1.00 2.00  ? 400  LEU A CG  1 
ATOM   3191  C  CD1 . LEU A  1 400 ? -2.040  -16.680 -12.095 1.00 2.18  ? 400  LEU A CD1 1 
ATOM   3192  C  CD2 . LEU A  1 400 ? -2.983  -14.990 -10.507 1.00 2.00  ? 400  LEU A CD2 1 
ATOM   3193  N  N   . ALA A  1 401 ? -2.264  -18.904 -6.893  1.00 2.00  ? 401  ALA A N   1 
ATOM   3194  C  CA  . ALA A  1 401 ? -2.815  -20.102 -6.248  1.00 2.00  ? 401  ALA A CA  1 
ATOM   3195  C  C   . ALA A  1 401 ? -3.003  -20.093 -4.734  1.00 3.28  ? 401  ALA A C   1 
ATOM   3196  O  O   . ALA A  1 401 ? -3.794  -20.867 -4.205  1.00 4.70  ? 401  ALA A O   1 
ATOM   3197  C  CB  . ALA A  1 401 ? -1.989  -21.305 -6.629  1.00 2.02  ? 401  ALA A CB  1 
ATOM   3198  N  N   . LYS A  1 402 ? -2.285  -19.245 -4.020  1.00 2.38  ? 402  LYS A N   1 
ATOM   3199  C  CA  . LYS A  1 402 ? -2.460  -19.212 -2.584  1.00 2.00  ? 402  LYS A CA  1 
ATOM   3200  C  C   . LYS A  1 402 ? -3.523  -18.211 -2.172  1.00 2.00  ? 402  LYS A C   1 
ATOM   3201  O  O   . LYS A  1 402 ? -4.033  -17.469 -3.003  1.00 2.00  ? 402  LYS A O   1 
ATOM   3202  C  CB  . LYS A  1 402 ? -1.137  -18.893 -1.920  1.00 2.00  ? 402  LYS A CB  1 
ATOM   3203  C  CG  . LYS A  1 402 ? -0.157  -20.020 -2.052  1.00 2.00  ? 402  LYS A CG  1 
ATOM   3204  C  CD  . LYS A  1 402 ? -0.747  -21.275 -1.461  1.00 2.38  ? 402  LYS A CD  1 
ATOM   3205  C  CE  . LYS A  1 402 ? 0.257   -22.398 -1.469  1.00 2.53  ? 402  LYS A CE  1 
ATOM   3206  N  NZ  . LYS A  1 402 ? -0.328  -23.593 -0.807  1.00 5.39  ? 402  LYS A NZ  1 
ATOM   3207  N  N   . LYS A  1 403 ? -3.853  -18.198 -0.884  1.00 2.00  ? 403  LYS A N   1 
ATOM   3208  C  CA  . LYS A  1 403 ? -4.876  -17.300 -0.344  1.00 2.00  ? 403  LYS A CA  1 
ATOM   3209  C  C   . LYS A  1 403 ? -4.343  -16.260 0.638   1.00 2.00  ? 403  LYS A C   1 
ATOM   3210  O  O   . LYS A  1 403 ? -3.330  -16.477 1.307   1.00 2.00  ? 403  LYS A O   1 
ATOM   3211  C  CB  . LYS A  1 403 ? -5.964  -18.098 0.380   1.00 2.00  ? 403  LYS A CB  1 
ATOM   3212  C  CG  . LYS A  1 403 ? -6.933  -18.884 -0.483  1.00 2.00  ? 403  LYS A CG  1 
ATOM   3213  C  CD  . LYS A  1 403 ? -7.808  -19.766 0.401   1.00 2.70  ? 403  LYS A CD  1 
ATOM   3214  C  CE  . LYS A  1 403 ? -8.732  -20.644 -0.411  1.00 4.17  ? 403  LYS A CE  1 
ATOM   3215  N  NZ  . LYS A  1 403 ? -7.958  -21.412 -1.430  1.00 8.49  ? 403  LYS A NZ  1 
ATOM   3216  N  N   . SER A  1 404 ? -5.064  -15.144 0.729   1.00 2.00  ? 404  SER A N   1 
ATOM   3217  C  CA  . SER A  1 404 ? -4.728  -14.041 1.626   1.00 2.52  ? 404  SER A CA  1 
ATOM   3218  C  C   . SER A  1 404 ? -5.122  -14.422 3.036   1.00 2.49  ? 404  SER A C   1 
ATOM   3219  O  O   . SER A  1 404 ? -5.483  -15.565 3.313   1.00 3.08  ? 404  SER A O   1 
ATOM   3220  C  CB  . SER A  1 404 ? -5.507  -12.777 1.256   1.00 2.83  ? 404  SER A CB  1 
ATOM   3221  O  OG  . SER A  1 404 ? -5.193  -12.312 -0.041  1.00 6.98  ? 404  SER A OG  1 
ATOM   3222  N  N   . LYS A  1 405 ? -5.072  -13.442 3.926   1.00 2.00  ? 405  LYS A N   1 
ATOM   3223  C  CA  . LYS A  1 405 ? -5.436  -13.671 5.307   1.00 2.00  ? 405  LYS A CA  1 
ATOM   3224  C  C   . LYS A  1 405 ? -6.741  -12.952 5.571   1.00 2.45  ? 405  LYS A C   1 
ATOM   3225  O  O   . LYS A  1 405 ? -6.861  -11.754 5.315   1.00 2.60  ? 405  LYS A O   1 
ATOM   3226  C  CB  . LYS A  1 405 ? -4.364  -13.122 6.236   1.00 2.03  ? 405  LYS A CB  1 
ATOM   3227  C  CG  . LYS A  1 405 ? -4.089  -14.036 7.395   1.00 3.56  ? 405  LYS A CG  1 
ATOM   3228  C  CD  . LYS A  1 405 ? -3.698  -13.279 8.636   1.00 2.00  ? 405  LYS A CD  1 
ATOM   3229  C  CE  . LYS A  1 405 ? -4.898  -12.591 9.214   1.00 2.00  ? 405  LYS A CE  1 
ATOM   3230  N  NZ  . LYS A  1 405 ? -4.712  -12.455 10.669  1.00 2.21  ? 405  LYS A NZ  1 
ATOM   3231  N  N   . LEU A  1 406 ? -7.727  -13.677 6.076   1.00 2.00  ? 406  LEU A N   1 
ATOM   3232  C  CA  . LEU A  1 406 ? -9.000  -13.047 6.355   1.00 2.00  ? 406  LEU A CA  1 
ATOM   3233  C  C   . LEU A  1 406 ? -8.882  -12.208 7.611   1.00 3.22  ? 406  LEU A C   1 
ATOM   3234  O  O   . LEU A  1 406 ? -8.234  -12.615 8.578   1.00 2.12  ? 406  LEU A O   1 
ATOM   3235  C  CB  . LEU A  1 406 ? -10.095 -14.095 6.537   1.00 2.00  ? 406  LEU A CB  1 
ATOM   3236  C  CG  . LEU A  1 406 ? -11.469 -13.545 6.909   1.00 2.00  ? 406  LEU A CG  1 
ATOM   3237  C  CD1 . LEU A  1 406 ? -11.806 -12.360 6.029   1.00 2.98  ? 406  LEU A CD1 1 
ATOM   3238  C  CD2 . LEU A  1 406 ? -12.495 -14.636 6.749   1.00 2.00  ? 406  LEU A CD2 1 
ATOM   3239  N  N   . MET A  1 407 ? -9.473  -11.019 7.585   1.00 3.71  ? 407  MET A N   1 
ATOM   3240  C  CA  . MET A  1 407 ? -9.453  -10.174 8.760   1.00 2.88  ? 407  MET A CA  1 
ATOM   3241  C  C   . MET A  1 407 ? -10.414 -10.919 9.669   1.00 3.61  ? 407  MET A C   1 
ATOM   3242  O  O   . MET A  1 407 ? -11.485 -11.338 9.231   1.00 4.03  ? 407  MET A O   1 
ATOM   3243  C  CB  . MET A  1 407 ? -9.995  -8.789  8.444   1.00 5.60  ? 407  MET A CB  1 
ATOM   3244  C  CG  . MET A  1 407 ? -9.698  -7.766  9.520   1.00 8.07  ? 407  MET A CG  1 
ATOM   3245  S  SD  . MET A  1 407 ? -10.120 -8.361  11.175  1.00 12.23 ? 407  MET A SD  1 
ATOM   3246  C  CE  . MET A  1 407 ? -11.925 -8.044  11.247  1.00 10.12 ? 407  MET A CE  1 
ATOM   3247  N  N   . ASN A  1 408 ? -10.021 -11.097 10.923  1.00 4.21  ? 408  ASN A N   1 
ATOM   3248  C  CA  . ASN A  1 408 ? -10.823 -11.827 11.899  1.00 3.75  ? 408  ASN A CA  1 
ATOM   3249  C  C   . ASN A  1 408 ? -10.724 -11.123 13.256  1.00 4.19  ? 408  ASN A C   1 
ATOM   3250  O  O   . ASN A  1 408 ? -9.675  -11.164 13.894  1.00 3.69  ? 408  ASN A O   1 
ATOM   3251  C  CB  . ASN A  1 408 ? -10.272 -13.254 11.993  1.00 6.28  ? 408  ASN A CB  1 
ATOM   3252  C  CG  . ASN A  1 408 ? -11.185 -14.198 12.746  1.00 9.55  ? 408  ASN A CG  1 
ATOM   3253  O  OD1 . ASN A  1 408 ? -11.360 -14.087 13.967  1.00 10.65 ? 408  ASN A OD1 1 
ATOM   3254  N  ND2 . ASN A  1 408 ? -11.771 -15.146 12.018  1.00 10.00 ? 408  ASN A ND2 1 
ATOM   3255  N  N   . GLN A  1 409 ? -11.807 -10.475 13.684  1.00 3.53  ? 409  GLN A N   1 
ATOM   3256  C  CA  . GLN A  1 409 ? -11.850 -9.745  14.961  1.00 4.15  ? 409  GLN A CA  1 
ATOM   3257  C  C   . GLN A  1 409 ? -11.019 -10.324 16.090  1.00 4.97  ? 409  GLN A C   1 
ATOM   3258  O  O   . GLN A  1 409 ? -10.729 -9.644  17.068  1.00 3.20  ? 409  GLN A O   1 
ATOM   3259  C  CB  . GLN A  1 409 ? -13.288 -9.645  15.467  1.00 4.67  ? 409  GLN A CB  1 
ATOM   3260  C  CG  . GLN A  1 409 ? -13.987 -8.373  15.076  1.00 8.54  ? 409  GLN A CG  1 
ATOM   3261  C  CD  . GLN A  1 409 ? -15.461 -8.385  15.418  1.00 9.94  ? 409  GLN A CD  1 
ATOM   3262  O  OE1 . GLN A  1 409 ? -16.220 -9.231  14.933  1.00 11.72 ? 409  GLN A OE1 1 
ATOM   3263  N  NE2 . GLN A  1 409 ? -15.879 -7.442  16.253  1.00 12.11 ? 409  GLN A NE2 1 
ATOM   3264  N  N   . ASN A  1 410 ? -10.542 -11.551 15.942  1.00 6.80  ? 410  ASN A N   1 
ATOM   3265  C  CA  . ASN A  1 410 ? -9.745  -12.319 16.967  1.00 8.25  ? 410  ASN A CA  1 
ATOM   3266  C  C   . ASN A  1 410 ? -8.229  -12.558 16.682  1.00 7.87  ? 410  ASN A C   1 
ATOM   3267  O  O   . ASN A  1 410 ? -7.440  -12.645 17.610  1.00 6.83  ? 410  ASN A O   1 
ATOM   3268  C  CB  . ASN A  1 410 ? -10.536 -13.596 17.183  1.00 12.44 ? 410  ASN A CB  1 
ATOM   3269  C  CG  . ASN A  1 410 ? -10.233 -14.211 18.518  1.00 16.58 ? 410  ASN A CG  1 
ATOM   3270  O  OD1 . ASN A  1 410 ? -9.091  -14.557 18.795  1.00 18.01 ? 410  ASN A OD1 1 
ATOM   3271  N  ND2 . ASN A  1 410 ? -11.263 -14.358 19.354  1.00 17.95 ? 410  ASN A ND2 1 
ATOM   3272  N  N   . LYS A  1 411 ? -7.870  -12.679 15.429  1.00 7.53  ? 411  LYS A N   1 
ATOM   3273  C  CA  . LYS A  1 411 ? -6.523  -12.816 14.955  1.00 4.24  ? 411  LYS A CA  1 
ATOM   3274  C  C   . LYS A  1 411 ? -6.335  -11.610 14.049  1.00 2.32  ? 411  LYS A C   1 
ATOM   3275  O  O   . LYS A  1 411 ? -6.757  -11.621 12.902  1.00 2.00  ? 411  LYS A O   1 
ATOM   3276  C  CB  . LYS A  1 411 ? -6.289  -14.172 14.268  1.00 2.97  ? 411  LYS A CB  1 
ATOM   3277  C  CG  . LYS A  1 411 ? -6.703  -15.390 15.104  1.00 2.59  ? 411  LYS A CG  1 
ATOM   3278  C  CD  . LYS A  1 411 ? -6.553  -16.654 14.271  1.00 3.70  ? 411  LYS A CD  1 
ATOM   3279  C  CE  . LYS A  1 411 ? -6.884  -17.906 15.078  1.00 2.85  ? 411  LYS A CE  1 
ATOM   3280  N  NZ  . LYS A  1 411 ? -8.350  -18.192 15.075  1.00 3.33  ? 411  LYS A NZ  1 
ATOM   3281  N  N   . MET A  1 412 ? -5.687  -10.577 14.554  1.00 2.50  ? 412  MET A N   1 
ATOM   3282  C  CA  . MET A  1 412 ? -5.575  -9.404  13.733  1.00 2.97  ? 412  MET A CA  1 
ATOM   3283  C  C   . MET A  1 412 ? -4.334  -9.382  12.808  1.00 4.09  ? 412  MET A C   1 
ATOM   3284  O  O   . MET A  1 412 ? -4.451  -9.375  11.578  1.00 3.17  ? 412  MET A O   1 
ATOM   3285  C  CB  . MET A  1 412 ? -5.671  -8.161  14.603  1.00 2.14  ? 412  MET A CB  1 
ATOM   3286  C  CG  . MET A  1 412 ? -7.086  -7.572  14.648  1.00 2.00  ? 412  MET A CG  1 
ATOM   3287  S  SD  . MET A  1 412 ? -7.384  -6.476  16.053  1.00 2.46  ? 412  MET A SD  1 
ATOM   3288  C  CE  . MET A  1 412 ? -9.068  -6.914  16.460  1.00 2.00  ? 412  MET A CE  1 
ATOM   3289  N  N   . VAL A  1 413 ? -3.160  -9.375  13.431  1.00 4.62  ? 413  VAL A N   1 
ATOM   3290  C  CA  . VAL A  1 413 ? -1.914  -9.313  12.671  1.00 3.03  ? 413  VAL A CA  1 
ATOM   3291  C  C   . VAL A  1 413 ? -0.914  -10.441 12.983  1.00 4.31  ? 413  VAL A C   1 
ATOM   3292  O  O   . VAL A  1 413 ? -0.580  -10.670 14.147  1.00 6.79  ? 413  VAL A O   1 
ATOM   3293  C  CB  . VAL A  1 413 ? -1.231  -7.946  12.909  1.00 2.00  ? 413  VAL A CB  1 
ATOM   3294  C  CG1 . VAL A  1 413 ? 0.126   -7.926  12.269  1.00 2.00  ? 413  VAL A CG1 1 
ATOM   3295  C  CG2 . VAL A  1 413 ? -2.115  -6.829  12.366  1.00 2.00  ? 413  VAL A CG2 1 
ATOM   3296  N  N   . THR A  1 414 ? -0.440  -11.126 11.936  1.00 4.54  ? 414  THR A N   1 
ATOM   3297  C  CA  . THR A  1 414 ? 0.539   -12.227 12.038  1.00 3.32  ? 414  THR A CA  1 
ATOM   3298  C  C   . THR A  1 414 ? 1.702   -11.877 12.929  1.00 2.00  ? 414  THR A C   1 
ATOM   3299  O  O   . THR A  1 414 ? 2.146   -10.731 12.975  1.00 2.00  ? 414  THR A O   1 
ATOM   3300  C  CB  . THR A  1 414 ? 1.227   -12.551 10.720  1.00 3.13  ? 414  THR A CB  1 
ATOM   3301  O  OG1 . THR A  1 414 ? 0.321   -12.375 9.627   1.00 5.29  ? 414  THR A OG1 1 
ATOM   3302  C  CG2 . THR A  1 414 ? 1.757   -13.971 10.759  1.00 2.00  ? 414  THR A CG2 1 
ATOM   3303  N  N   . SER A  1 415 ? 2.242   -12.891 13.582  1.00 2.00  ? 415  SER A N   1 
ATOM   3304  C  CA  . SER A  1 415 ? 3.359   -12.693 14.481  1.00 2.00  ? 415  SER A CA  1 
ATOM   3305  C  C   . SER A  1 415 ? 4.624   -12.425 13.702  1.00 2.00  ? 415  SER A C   1 
ATOM   3306  O  O   . SER A  1 415 ? 5.610   -11.938 14.246  1.00 2.00  ? 415  SER A O   1 
ATOM   3307  C  CB  . SER A  1 415 ? 3.522   -13.922 15.351  1.00 2.75  ? 415  SER A CB  1 
ATOM   3308  O  OG  . SER A  1 415 ? 2.266   -14.247 15.922  1.00 3.84  ? 415  SER A OG  1 
ATOM   3309  N  N   . GLU A  1 416 ? 4.592   -12.781 12.419  1.00 2.00  ? 416  GLU A N   1 
ATOM   3310  C  CA  . GLU A  1 416 ? 5.746   -12.512 11.575  1.00 2.00  ? 416  GLU A CA  1 
ATOM   3311  C  C   . GLU A  1 416 ? 5.832   -11.004 11.380  1.00 2.00  ? 416  GLU A C   1 
ATOM   3312  O  O   . GLU A  1 416 ? 6.871   -10.491 10.987  1.00 2.09  ? 416  GLU A O   1 
ATOM   3313  C  CB  . GLU A  1 416 ? 5.661   -13.258 10.219  1.00 2.70  ? 416  GLU A CB  1 
ATOM   3314  C  CG  . GLU A  1 416 ? 5.366   -14.761 10.335  1.00 3.43  ? 416  GLU A CG  1 
ATOM   3315  C  CD  . GLU A  1 416 ? 6.469   -15.590 11.018  1.00 3.58  ? 416  GLU A CD  1 
ATOM   3316  O  OE1 . GLU A  1 416 ? 6.131   -16.679 11.523  1.00 2.00  ? 416  GLU A OE1 1 
ATOM   3317  O  OE2 . GLU A  1 416 ? 7.646   -15.161 11.031  1.00 3.15  ? 416  GLU A OE2 1 
ATOM   3318  N  N   . LEU A  1 417 ? 4.738   -10.298 11.670  1.00 2.00  ? 417  LEU A N   1 
ATOM   3319  C  CA  . LEU A  1 417 ? 4.700   -8.838  11.537  1.00 2.00  ? 417  LEU A CA  1 
ATOM   3320  C  C   . LEU A  1 417 ? 4.610   -8.113  12.870  1.00 2.11  ? 417  LEU A C   1 
ATOM   3321  O  O   . LEU A  1 417 ? 5.056   -6.974  12.996  1.00 2.00  ? 417  LEU A O   1 
ATOM   3322  C  CB  . LEU A  1 417 ? 3.525   -8.394  10.666  1.00 2.00  ? 417  LEU A CB  1 
ATOM   3323  C  CG  . LEU A  1 417 ? 3.820   -8.270  9.175   1.00 2.00  ? 417  LEU A CG  1 
ATOM   3324  C  CD1 . LEU A  1 417 ? 2.597   -7.768  8.437   1.00 2.00  ? 417  LEU A CD1 1 
ATOM   3325  C  CD2 . LEU A  1 417 ? 4.979   -7.323  8.986   1.00 2.00  ? 417  LEU A CD2 1 
ATOM   3326  N  N   . ARG A  1 418 ? 4.025   -8.766  13.865  1.00 4.02  ? 418  ARG A N   1 
ATOM   3327  C  CA  . ARG A  1 418 ? 3.890   -8.155  15.179  1.00 2.78  ? 418  ARG A CA  1 
ATOM   3328  C  C   . ARG A  1 418 ? 5.189   -8.211  15.998  1.00 3.11  ? 418  ARG A C   1 
ATOM   3329  O  O   . ARG A  1 418 ? 5.565   -7.222  16.619  1.00 2.59  ? 418  ARG A O   1 
ATOM   3330  C  CB  . ARG A  1 418 ? 2.755   -8.828  15.951  1.00 3.77  ? 418  ARG A CB  1 
ATOM   3331  C  CG  . ARG A  1 418 ? 2.178   -7.963  17.044  1.00 6.63  ? 418  ARG A CG  1 
ATOM   3332  C  CD  . ARG A  1 418 ? 0.925   -8.590  17.610  1.00 9.22  ? 418  ARG A CD  1 
ATOM   3333  N  NE  . ARG A  1 418 ? 1.264   -9.731  18.445  1.00 13.73 ? 418  ARG A NE  1 
ATOM   3334  C  CZ  . ARG A  1 418 ? 1.870   -9.620  19.622  1.00 14.59 ? 418  ARG A CZ  1 
ATOM   3335  N  NH1 . ARG A  1 418 ? 2.181   -8.414  20.081  1.00 16.16 ? 418  ARG A NH1 1 
ATOM   3336  N  NH2 . ARG A  1 418 ? 2.184   -10.706 20.326  1.00 14.83 ? 418  ARG A NH2 1 
ATOM   3337  N  N   . ASN A  1 419 ? 5.885   -9.350  15.977  1.00 2.95  ? 419  ASN A N   1 
ATOM   3338  C  CA  . ASN A  1 419 ? 7.123   -9.519  16.743  1.00 2.00  ? 419  ASN A CA  1 
ATOM   3339  C  C   . ASN A  1 419 ? 8.435   -9.551  15.975  1.00 2.26  ? 419  ASN A C   1 
ATOM   3340  O  O   . ASN A  1 419 ? 9.465   -9.090  16.480  1.00 2.00  ? 419  ASN A O   1 
ATOM   3341  C  CB  . ASN A  1 419 ? 7.056   -10.803 17.545  1.00 3.34  ? 419  ASN A CB  1 
ATOM   3342  C  CG  . ASN A  1 419 ? 5.939   -10.801 18.538  1.00 5.71  ? 419  ASN A CG  1 
ATOM   3343  O  OD1 . ASN A  1 419 ? 5.823   -9.881  19.359  1.00 5.46  ? 419  ASN A OD1 1 
ATOM   3344  N  ND2 . ASN A  1 419 ? 5.099   -11.838 18.484  1.00 6.56  ? 419  ASN A ND2 1 
ATOM   3345  N  N   . LYS A  1 420 ? 8.392   -10.114 14.768  1.00 2.80  ? 420  LYS A N   1 
ATOM   3346  C  CA  . LYS A  1 420 ? 9.570   -10.281 13.923  1.00 2.00  ? 420  LYS A CA  1 
ATOM   3347  C  C   . LYS A  1 420 ? 9.656   -9.378  12.688  1.00 2.00  ? 420  LYS A C   1 
ATOM   3348  O  O   . LYS A  1 420 ? 10.076  -9.842  11.635  1.00 3.08  ? 420  LYS A O   1 
ATOM   3349  C  CB  . LYS A  1 420 ? 9.636   -11.733 13.455  1.00 2.00  ? 420  LYS A CB  1 
ATOM   3350  C  CG  . LYS A  1 420 ? 8.842   -12.708 14.304  1.00 2.00  ? 420  LYS A CG  1 
ATOM   3351  C  CD  . LYS A  1 420 ? 9.747   -13.599 15.127  1.00 2.00  ? 420  LYS A CD  1 
ATOM   3352  C  CE  . LYS A  1 420 ? 9.688   -15.031 14.604  1.00 2.81  ? 420  LYS A CE  1 
ATOM   3353  N  NZ  . LYS A  1 420 ? 10.698  -15.944 15.241  1.00 5.39  ? 420  LYS A NZ  1 
ATOM   3354  N  N   . LEU A  1 421 ? 9.278   -8.105  12.791  1.00 3.32  ? 421  LEU A N   1 
ATOM   3355  C  CA  . LEU A  1 421 ? 9.348   -7.211  11.622  1.00 3.88  ? 421  LEU A CA  1 
ATOM   3356  C  C   . LEU A  1 421 ? 10.726  -6.617  11.409  1.00 3.44  ? 421  LEU A C   1 
ATOM   3357  O  O   . LEU A  1 421 ? 11.323  -6.093  12.342  1.00 4.70  ? 421  LEU A O   1 
ATOM   3358  C  CB  . LEU A  1 421 ? 8.354   -6.045  11.735  1.00 2.23  ? 421  LEU A CB  1 
ATOM   3359  C  CG  . LEU A  1 421 ? 8.594   -4.934  10.698  1.00 2.00  ? 421  LEU A CG  1 
ATOM   3360  C  CD1 . LEU A  1 421 ? 8.349   -5.481  9.314   1.00 2.00  ? 421  LEU A CD1 1 
ATOM   3361  C  CD2 . LEU A  1 421 ? 7.697   -3.737  10.960  1.00 2.96  ? 421  LEU A CD2 1 
ATOM   3362  N  N   . PHE A  1 422 ? 11.226  -6.675  10.180  1.00 3.21  ? 422  PHE A N   1 
ATOM   3363  C  CA  . PHE A  1 422 ? 12.531  -6.091  9.905   1.00 4.10  ? 422  PHE A CA  1 
ATOM   3364  C  C   . PHE A  1 422 ? 12.434  -4.659  9.374   1.00 5.82  ? 422  PHE A C   1 
ATOM   3365  O  O   . PHE A  1 422 ? 11.617  -4.360  8.491   1.00 7.36  ? 422  PHE A O   1 
ATOM   3366  C  CB  . PHE A  1 422 ? 13.295  -6.919  8.880   1.00 3.76  ? 422  PHE A CB  1 
ATOM   3367  C  CG  . PHE A  1 422 ? 14.758  -6.559  8.782   1.00 3.22  ? 422  PHE A CG  1 
ATOM   3368  C  CD1 . PHE A  1 422 ? 15.594  -6.719  9.874   1.00 2.08  ? 422  PHE A CD1 1 
ATOM   3369  C  CD2 . PHE A  1 422 ? 15.301  -6.091  7.599   1.00 2.55  ? 422  PHE A CD2 1 
ATOM   3370  C  CE1 . PHE A  1 422 ? 16.937  -6.426  9.785   1.00 2.00  ? 422  PHE A CE1 1 
ATOM   3371  C  CE2 . PHE A  1 422 ? 16.656  -5.795  7.510   1.00 2.00  ? 422  PHE A CE2 1 
ATOM   3372  C  CZ  . PHE A  1 422 ? 17.469  -5.964  8.603   1.00 2.00  ? 422  PHE A CZ  1 
ATOM   3373  N  N   . GLN A  1 423 ? 13.269  -3.775  9.913   1.00 4.60  ? 423  GLN A N   1 
ATOM   3374  C  CA  . GLN A  1 423 ? 13.298  -2.394  9.448   1.00 5.36  ? 423  GLN A CA  1 
ATOM   3375  C  C   . GLN A  1 423 ? 14.640  -2.231  8.742   1.00 5.60  ? 423  GLN A C   1 
ATOM   3376  O  O   . GLN A  1 423 ? 15.654  -2.760  9.207   1.00 6.58  ? 423  GLN A O   1 
ATOM   3377  C  CB  . GLN A  1 423 ? 13.164  -1.422  10.624  1.00 4.57  ? 423  GLN A CB  1 
ATOM   3378  C  CG  . GLN A  1 423 ? 11.778  -1.423  11.252  1.00 5.20  ? 423  GLN A CG  1 
ATOM   3379  C  CD  . GLN A  1 423 ? 10.740  -0.676  10.429  1.00 6.50  ? 423  GLN A CD  1 
ATOM   3380  O  OE1 . GLN A  1 423 ? 10.659  -0.825  9.205   1.00 8.40  ? 423  GLN A OE1 1 
ATOM   3381  N  NE2 . GLN A  1 423 ? 9.927   0.126   11.108  1.00 7.67  ? 423  GLN A NE2 1 
ATOM   3382  N  N   . PRO A  1 424 ? 14.665  -1.512  7.602   1.00 4.91  ? 424  PRO A N   1 
ATOM   3383  C  CA  . PRO A  1 424 ? 15.917  -1.319  6.857   1.00 4.61  ? 424  PRO A CA  1 
ATOM   3384  C  C   . PRO A  1 424 ? 17.013  -0.625  7.659   1.00 4.60  ? 424  PRO A C   1 
ATOM   3385  O  O   . PRO A  1 424 ? 18.176  -1.015  7.620   1.00 3.91  ? 424  PRO A O   1 
ATOM   3386  C  CB  . PRO A  1 424 ? 15.468  -0.524  5.629   1.00 3.44  ? 424  PRO A CB  1 
ATOM   3387  C  CG  . PRO A  1 424 ? 14.306  0.271   6.142   1.00 3.78  ? 424  PRO A CG  1 
ATOM   3388  C  CD  . PRO A  1 424 ? 13.567  -0.723  7.008   1.00 4.63  ? 424  PRO A CD  1 
ATOM   3389  N  N   . THR A  1 425 ? 16.626  0.397   8.399   1.00 5.52  ? 425  THR A N   1 
ATOM   3390  C  CA  . THR A  1 425 ? 17.559  1.149   9.216   1.00 9.38  ? 425  THR A CA  1 
ATOM   3391  C  C   . THR A  1 425 ? 18.415  0.254   10.115  1.00 10.50 ? 425  THR A C   1 
ATOM   3392  O  O   . THR A  1 425 ? 19.641  0.207   10.003  1.00 10.21 ? 425  THR A O   1 
ATOM   3393  C  CB  . THR A  1 425 ? 16.799  2.114   10.150  1.00 10.54 ? 425  THR A CB  1 
ATOM   3394  O  OG1 . THR A  1 425 ? 15.730  2.740   9.428   1.00 13.44 ? 425  THR A OG1 1 
ATOM   3395  C  CG2 . THR A  1 425 ? 17.745  3.172   10.688  1.00 10.85 ? 425  THR A CG2 1 
ATOM   3396  N  N   . HIS A  1 426 ? 17.768  -0.468  10.998  1.00 11.42 ? 426  HIS A N   1 
ATOM   3397  C  CA  . HIS A  1 426 ? 18.409  -1.305  12.000  1.00 11.68 ? 426  HIS A CA  1 
ATOM   3398  C  C   . HIS A  1 426 ? 18.675  -2.742  11.665  1.00 12.00 ? 426  HIS A C   1 
ATOM   3399  O  O   . HIS A  1 426 ? 18.321  -3.233  10.606  1.00 11.91 ? 426  HIS A O   1 
ATOM   3400  C  CB  . HIS A  1 426 ? 17.517  -1.358  13.250  1.00 11.80 ? 426  HIS A CB  1 
ATOM   3401  C  CG  . HIS A  1 426 ? 16.935  0.009   13.579  1.00 11.97 ? 426  HIS A CG  1 
ATOM   3402  N  ND1 . HIS A  1 426 ? 17.322  0.723   14.700  1.00 11.76 ? 426  HIS A ND1 1 
ATOM   3403  C  CD2 . HIS A  1 426 ? 16.044  0.774   12.936  1.00 11.75 ? 426  HIS A CD2 1 
ATOM   3404  C  CE1 . HIS A  1 426 ? 16.715  1.880   14.729  1.00 12.52 ? 426  HIS A CE1 1 
ATOM   3405  N  NE2 . HIS A  1 426 ? 15.936  1.931   13.669  1.00 11.94 ? 426  HIS A NE2 1 
ATOM   3406  N  N   . LYS A  1 427 ? 19.327  -3.419  12.652  1.00 13.13 ? 427  LYS A N   1 
ATOM   3407  C  CA  . LYS A  1 427 ? 19.832  -4.797  12.546  1.00 12.75 ? 427  LYS A CA  1 
ATOM   3408  C  C   . LYS A  1 427 ? 18.910  -5.979  12.902  1.00 11.02 ? 427  LYS A C   1 
ATOM   3409  O  O   . LYS A  1 427 ? 18.645  -6.845  12.066  1.00 12.12 ? 427  LYS A O   1 
ATOM   3410  C  CB  . LYS A  1 427 ? 21.117  -4.897  13.392  1.00 14.51 ? 427  LYS A CB  1 
ATOM   3411  C  CG  . LYS A  1 427 ? 22.269  -4.028  12.921  1.00 17.32 ? 427  LYS A CG  1 
ATOM   3412  C  CD  . LYS A  1 427 ? 23.456  -4.093  13.864  1.00 18.91 ? 427  LYS A CD  1 
ATOM   3413  C  CE  . LYS A  1 427 ? 24.501  -3.032  13.542  1.00 19.36 ? 427  LYS A CE  1 
ATOM   3414  N  NZ  . LYS A  1 427 ? 23.898  -1.664  13.475  1.00 19.90 ? 427  LYS A NZ  1 
ATOM   3415  N  N   . ILE A  1 428 ? 18.420  -6.035  14.134  1.00 9.54  ? 428  ILE A N   1 
ATOM   3416  C  CA  . ILE A  1 428 ? 17.610  -7.183  14.530  1.00 9.09  ? 428  ILE A CA  1 
ATOM   3417  C  C   . ILE A  1 428 ? 16.277  -7.291  13.793  1.00 7.46  ? 428  ILE A C   1 
ATOM   3418  O  O   . ILE A  1 428 ? 15.809  -6.356  13.155  1.00 7.14  ? 428  ILE A O   1 
ATOM   3419  C  CB  . ILE A  1 428 ? 17.389  -7.225  16.055  1.00 9.62  ? 428  ILE A CB  1 
ATOM   3420  C  CG1 . ILE A  1 428 ? 16.129  -6.459  16.462  1.00 9.47  ? 428  ILE A CG1 1 
ATOM   3421  C  CG2 . ILE A  1 428 ? 18.609  -6.657  16.768  1.00 9.77  ? 428  ILE A CG2 1 
ATOM   3422  C  CD1 . ILE A  1 428 ? 16.220  -4.970  16.226  1.00 11.45 ? 428  ILE A CD1 1 
ATOM   3423  N  N   . HIS A  1 429 ? 15.662  -8.464  13.907  1.00 7.46  ? 429  HIS A N   1 
ATOM   3424  C  CA  . HIS A  1 429 ? 14.377  -8.794  13.279  1.00 7.60  ? 429  HIS A CA  1 
ATOM   3425  C  C   . HIS A  1 429 ? 13.248  -8.789  14.325  1.00 8.95  ? 429  HIS A C   1 
ATOM   3426  O  O   . HIS A  1 429 ? 12.413  -9.705  14.327  1.00 9.56  ? 429  HIS A O   1 
ATOM   3427  C  CB  . HIS A  1 429 ? 14.436  -10.217 12.699  1.00 6.23  ? 429  HIS A CB  1 
ATOM   3428  C  CG  . HIS A  1 429 ? 14.815  -10.294 11.254  1.00 4.24  ? 429  HIS A CG  1 
ATOM   3429  N  ND1 . HIS A  1 429 ? 16.042  -9.885  10.777  1.00 3.17  ? 429  HIS A ND1 1 
ATOM   3430  C  CD2 . HIS A  1 429 ? 14.128  -10.761 10.183  1.00 2.61  ? 429  HIS A CD2 1 
ATOM   3431  C  CE1 . HIS A  1 429 ? 16.091  -10.093 9.473   1.00 4.36  ? 429  HIS A CE1 1 
ATOM   3432  N  NE2 . HIS A  1 429 ? 14.942  -10.623 9.088   1.00 2.75  ? 429  HIS A NE2 1 
ATOM   3433  N  N   . GLY A  1 430 ? 13.194  -7.789  15.203  1.00 7.88  ? 430  GLY A N   1 
ATOM   3434  C  CA  . GLY A  1 430 ? 12.160  -7.823  16.226  1.00 6.44  ? 430  GLY A CA  1 
ATOM   3435  C  C   . GLY A  1 430 ? 11.275  -6.618  16.453  1.00 5.90  ? 430  GLY A C   1 
ATOM   3436  O  O   . GLY A  1 430 ? 10.989  -6.271  17.596  1.00 6.18  ? 430  GLY A O   1 
ATOM   3437  N  N   . PHE A  1 431 ? 10.820  -5.983  15.383  1.00 5.05  ? 431  PHE A N   1 
ATOM   3438  C  CA  . PHE A  1 431 ? 9.956   -4.830  15.541  1.00 4.66  ? 431  PHE A CA  1 
ATOM   3439  C  C   . PHE A  1 431 ? 8.486   -5.213  15.521  1.00 5.64  ? 431  PHE A C   1 
ATOM   3440  O  O   . PHE A  1 431 ? 8.150   -6.395  15.444  1.00 5.38  ? 431  PHE A O   1 
ATOM   3441  C  CB  . PHE A  1 431 ? 10.252  -3.803  14.460  1.00 3.25  ? 431  PHE A CB  1 
ATOM   3442  C  CG  . PHE A  1 431 ? 11.366  -2.871  14.817  1.00 2.65  ? 431  PHE A CG  1 
ATOM   3443  C  CD1 . PHE A  1 431 ? 12.646  -3.049  14.307  1.00 2.00  ? 431  PHE A CD1 1 
ATOM   3444  C  CD2 . PHE A  1 431 ? 11.131  -1.810  15.679  1.00 2.97  ? 431  PHE A CD2 1 
ATOM   3445  C  CE1 . PHE A  1 431 ? 13.676  -2.182  14.648  1.00 2.00  ? 431  PHE A CE1 1 
ATOM   3446  C  CE2 . PHE A  1 431 ? 12.150  -0.937  16.029  1.00 3.78  ? 431  PHE A CE2 1 
ATOM   3447  C  CZ  . PHE A  1 431 ? 13.427  -1.122  15.512  1.00 3.58  ? 431  PHE A CZ  1 
ATOM   3448  N  N   . ASP A  1 432 ? 7.608   -4.217  15.604  1.00 7.05  ? 432  ASP A N   1 
ATOM   3449  C  CA  . ASP A  1 432 ? 6.171   -4.482  15.596  1.00 6.61  ? 432  ASP A CA  1 
ATOM   3450  C  C   . ASP A  1 432 ? 5.333   -3.527  14.746  1.00 5.39  ? 432  ASP A C   1 
ATOM   3451  O  O   . ASP A  1 432 ? 4.990   -2.430  15.192  1.00 5.30  ? 432  ASP A O   1 
ATOM   3452  C  CB  . ASP A  1 432 ? 5.620   -4.462  17.017  1.00 7.63  ? 432  ASP A CB  1 
ATOM   3453  C  CG  . ASP A  1 432 ? 4.114   -4.647  17.048  1.00 9.69  ? 432  ASP A CG  1 
ATOM   3454  O  OD1 . ASP A  1 432 ? 3.508   -4.762  15.955  1.00 8.73  ? 432  ASP A OD1 1 
ATOM   3455  O  OD2 . ASP A  1 432 ? 3.535   -4.677  18.160  1.00 11.92 ? 432  ASP A OD2 1 
ATOM   3456  N  N   . LEU A  1 433 ? 4.965   -3.968  13.546  1.00 4.52  ? 433  LEU A N   1 
ATOM   3457  C  CA  . LEU A  1 433 ? 4.163   -3.144  12.649  1.00 4.38  ? 433  LEU A CA  1 
ATOM   3458  C  C   . LEU A  1 433 ? 2.931   -2.586  13.345  1.00 2.00  ? 433  LEU A C   1 
ATOM   3459  O  O   . LEU A  1 433 ? 2.626   -1.406  13.209  1.00 2.00  ? 433  LEU A O   1 
ATOM   3460  C  CB  . LEU A  1 433 ? 3.735   -3.939  11.412  1.00 2.25  ? 433  LEU A CB  1 
ATOM   3461  C  CG  . LEU A  1 433 ? 2.963   -3.112  10.386  1.00 2.00  ? 433  LEU A CG  1 
ATOM   3462  C  CD1 . LEU A  1 433 ? 3.658   -1.773  10.166  1.00 2.00  ? 433  LEU A CD1 1 
ATOM   3463  C  CD2 . LEU A  1 433 ? 2.859   -3.895  9.097   1.00 2.00  ? 433  LEU A CD2 1 
ATOM   3464  N  N   . ALA A  1 434 ? 2.230   -3.434  14.092  1.00 2.00  ? 434  ALA A N   1 
ATOM   3465  C  CA  . ALA A  1 434 ? 1.035   -3.000  14.805  1.00 2.69  ? 434  ALA A CA  1 
ATOM   3466  C  C   . ALA A  1 434 ? 1.361   -1.809  15.707  1.00 5.02  ? 434  ALA A C   1 
ATOM   3467  O  O   . ALA A  1 434 ? 0.717   -0.758  15.618  1.00 6.01  ? 434  ALA A O   1 
ATOM   3468  C  CB  . ALA A  1 434 ? 0.464   -4.147  15.634  1.00 2.00  ? 434  ALA A CB  1 
ATOM   3469  N  N   . ALA A  1 435 ? 2.362   -1.963  16.569  1.00 2.76  ? 435  ALA A N   1 
ATOM   3470  C  CA  . ALA A  1 435 ? 2.745   -0.879  17.464  1.00 2.21  ? 435  ALA A CA  1 
ATOM   3471  C  C   . ALA A  1 435 ? 3.233   0.329   16.683  1.00 2.83  ? 435  ALA A C   1 
ATOM   3472  O  O   . ALA A  1 435 ? 2.992   1.459   17.084  1.00 4.06  ? 435  ALA A O   1 
ATOM   3473  C  CB  . ALA A  1 435 ? 3.818   -1.339  18.429  1.00 2.54  ? 435  ALA A CB  1 
ATOM   3474  N  N   . ILE A  1 436 ? 3.933   0.111   15.576  1.00 2.00  ? 436  ILE A N   1 
ATOM   3475  C  CA  . ILE A  1 436 ? 4.381   1.255   14.803  1.00 2.00  ? 436  ILE A CA  1 
ATOM   3476  C  C   . ILE A  1 436 ? 3.115   2.025   14.420  1.00 2.00  ? 436  ILE A C   1 
ATOM   3477  O  O   . ILE A  1 436 ? 3.010   3.224   14.644  1.00 2.89  ? 436  ILE A O   1 
ATOM   3478  C  CB  . ILE A  1 436 ? 5.058   0.860   13.489  1.00 2.00  ? 436  ILE A CB  1 
ATOM   3479  C  CG1 . ILE A  1 436 ? 5.948   -0.371  13.673  1.00 2.63  ? 436  ILE A CG1 1 
ATOM   3480  C  CG2 . ILE A  1 436 ? 5.849   2.045   12.970  1.00 2.00  ? 436  ILE A CG2 1 
ATOM   3481  C  CD1 . ILE A  1 436 ? 7.327   -0.089  14.203  1.00 3.69  ? 436  ILE A CD1 1 
ATOM   3482  N  N   . ASN A  1 437 ? 2.146   1.314   13.851  1.00 2.08  ? 437  ASN A N   1 
ATOM   3483  C  CA  . ASN A  1 437 ? 0.894   1.921   13.408  1.00 2.39  ? 437  ASN A CA  1 
ATOM   3484  C  C   . ASN A  1 437 ? 0.203   2.774   14.451  1.00 2.00  ? 437  ASN A C   1 
ATOM   3485  O  O   . ASN A  1 437 ? -0.155  3.921   14.196  1.00 2.00  ? 437  ASN A O   1 
ATOM   3486  C  CB  . ASN A  1 437 ? -0.083  0.845   12.944  1.00 3.39  ? 437  ASN A CB  1 
ATOM   3487  C  CG  . ASN A  1 437 ? 0.442   0.051   11.780  1.00 4.07  ? 437  ASN A CG  1 
ATOM   3488  O  OD1 . ASN A  1 437 ? 0.819   0.607   10.743  1.00 2.00  ? 437  ASN A OD1 1 
ATOM   3489  N  ND2 . ASN A  1 437 ? 0.468   -1.266  11.939  1.00 6.87  ? 437  ASN A ND2 1 
ATOM   3490  N  N   . LEU A  1 438 ? -0.016  2.200   15.621  1.00 2.00  ? 438  LEU A N   1 
ATOM   3491  C  CA  . LEU A  1 438 ? -0.674  2.938   16.669  1.00 2.10  ? 438  LEU A CA  1 
ATOM   3492  C  C   . LEU A  1 438 ? 0.173   4.142   17.053  1.00 2.00  ? 438  LEU A C   1 
ATOM   3493  O  O   . LEU A  1 438 ? -0.331  5.257   17.115  1.00 3.62  ? 438  LEU A O   1 
ATOM   3494  C  CB  . LEU A  1 438 ? -0.930  2.034   17.880  1.00 3.23  ? 438  LEU A CB  1 
ATOM   3495  C  CG  . LEU A  1 438 ? -2.015  0.961   17.678  1.00 4.78  ? 438  LEU A CG  1 
ATOM   3496  C  CD1 . LEU A  1 438 ? -2.181  0.170   18.968  1.00 3.16  ? 438  LEU A CD1 1 
ATOM   3497  C  CD2 . LEU A  1 438 ? -3.350  1.608   17.267  1.00 3.10  ? 438  LEU A CD2 1 
ATOM   3498  N  N   . GLN A  1 439 ? 1.461   3.939   17.295  1.00 2.07  ? 439  GLN A N   1 
ATOM   3499  C  CA  . GLN A  1 439 ? 2.310   5.063   17.666  1.00 2.48  ? 439  GLN A CA  1 
ATOM   3500  C  C   . GLN A  1 439 ? 2.168   6.119   16.574  1.00 2.00  ? 439  GLN A C   1 
ATOM   3501  O  O   . GLN A  1 439 ? 1.866   7.283   16.842  1.00 3.17  ? 439  GLN A O   1 
ATOM   3502  C  CB  . GLN A  1 439 ? 3.777   4.626   17.782  1.00 3.53  ? 439  GLN A CB  1 
ATOM   3503  C  CG  . GLN A  1 439 ? 4.688   5.677   18.420  1.00 6.85  ? 439  GLN A CG  1 
ATOM   3504  C  CD  . GLN A  1 439 ? 4.609   5.696   19.953  1.00 9.04  ? 439  GLN A CD  1 
ATOM   3505  O  OE1 . GLN A  1 439 ? 3.530   5.563   20.546  1.00 8.31  ? 439  GLN A OE1 1 
ATOM   3506  N  NE2 . GLN A  1 439 ? 5.760   5.882   20.597  1.00 10.44 ? 439  GLN A NE2 1 
ATOM   3507  N  N   . ARG A  1 440 ? 2.356   5.681   15.338  1.00 2.00  ? 440  ARG A N   1 
ATOM   3508  C  CA  . ARG A  1 440 ? 2.275   6.534   14.166  1.00 2.38  ? 440  ARG A CA  1 
ATOM   3509  C  C   . ARG A  1 440 ? 0.992   7.386   14.012  1.00 3.73  ? 440  ARG A C   1 
ATOM   3510  O  O   . ARG A  1 440 ? 1.002   8.396   13.301  1.00 4.27  ? 440  ARG A O   1 
ATOM   3511  C  CB  . ARG A  1 440 ? 2.473   5.663   12.929  1.00 2.84  ? 440  ARG A CB  1 
ATOM   3512  C  CG  . ARG A  1 440 ? 2.498   6.393   11.595  1.00 4.29  ? 440  ARG A CG  1 
ATOM   3513  C  CD  . ARG A  1 440 ? 3.751   7.190   11.432  1.00 5.09  ? 440  ARG A CD  1 
ATOM   3514  N  NE  . ARG A  1 440 ? 4.868   6.413   10.950  1.00 5.13  ? 440  ARG A NE  1 
ATOM   3515  C  CZ  . ARG A  1 440 ? 6.116   6.756   11.199  1.00 6.40  ? 440  ARG A CZ  1 
ATOM   3516  N  NH1 . ARG A  1 440 ? 6.365   7.822   11.924  1.00 7.16  ? 440  ARG A NH1 1 
ATOM   3517  N  NH2 . ARG A  1 440 ? 7.106   6.030   10.714  1.00 4.80  ? 440  ARG A NH2 1 
ATOM   3518  N  N   . CYS A  1 441 ? -0.111  6.989   14.648  1.00 3.86  ? 441  CYS A N   1 
ATOM   3519  C  CA  . CYS A  1 441 ? -1.349  7.772   14.549  1.00 2.00  ? 441  CYS A CA  1 
ATOM   3520  C  C   . CYS A  1 441 ? -1.195  9.005   15.407  1.00 2.00  ? 441  CYS A C   1 
ATOM   3521  O  O   . CYS A  1 441 ? -1.492  10.121  14.990  1.00 2.32  ? 441  CYS A O   1 
ATOM   3522  C  CB  . CYS A  1 441 ? -2.551  6.999   15.077  1.00 2.00  ? 441  CYS A CB  1 
ATOM   3523  S  SG  . CYS A  1 441 ? -3.050  5.596   14.115  1.00 2.00  ? 441  CYS A SG  1 
ATOM   3524  N  N   . ARG A  1 442 ? -0.737  8.780   16.628  1.00 2.00  ? 442  ARG A N   1 
ATOM   3525  C  CA  . ARG A  1 442 ? -0.547  9.856   17.571  1.00 2.00  ? 442  ARG A CA  1 
ATOM   3526  C  C   . ARG A  1 442 ? 0.479   10.843  17.031  1.00 2.42  ? 442  ARG A C   1 
ATOM   3527  O  O   . ARG A  1 442 ? 0.393   12.035  17.314  1.00 2.95  ? 442  ARG A O   1 
ATOM   3528  C  CB  . ARG A  1 442 ? -0.140  9.257   18.912  1.00 2.00  ? 442  ARG A CB  1 
ATOM   3529  C  CG  . ARG A  1 442 ? -1.210  8.294   19.409  1.00 2.00  ? 442  ARG A CG  1 
ATOM   3530  C  CD  . ARG A  1 442 ? -0.695  7.310   20.428  1.00 2.40  ? 442  ARG A CD  1 
ATOM   3531  N  NE  . ARG A  1 442 ? -1.691  6.285   20.723  1.00 2.00  ? 442  ARG A NE  1 
ATOM   3532  C  CZ  . ARG A  1 442 ? -1.586  5.416   21.718  1.00 2.00  ? 442  ARG A CZ  1 
ATOM   3533  N  NH1 . ARG A  1 442 ? -0.532  5.443   22.520  1.00 2.00  ? 442  ARG A NH1 1 
ATOM   3534  N  NH2 . ARG A  1 442 ? -2.540  4.527   21.917  1.00 2.00  ? 442  ARG A NH2 1 
ATOM   3535  N  N   . ASP A  1 443 ? 1.424   10.353  16.227  1.00 2.10  ? 443  ASP A N   1 
ATOM   3536  C  CA  . ASP A  1 443 ? 2.465   11.197  15.611  1.00 2.95  ? 443  ASP A CA  1 
ATOM   3537  C  C   . ASP A  1 443 ? 1.843   12.082  14.512  1.00 2.86  ? 443  ASP A C   1 
ATOM   3538  O  O   . ASP A  1 443 ? 2.162   13.270  14.382  1.00 2.00  ? 443  ASP A O   1 
ATOM   3539  C  CB  . ASP A  1 443 ? 3.587   10.295  15.032  1.00 2.43  ? 443  ASP A CB  1 
ATOM   3540  C  CG  . ASP A  1 443 ? 4.687   11.075  14.276  1.00 2.30  ? 443  ASP A CG  1 
ATOM   3541  O  OD1 . ASP A  1 443 ? 5.072   12.190  14.702  1.00 2.00  ? 443  ASP A OD1 1 
ATOM   3542  O  OD2 . ASP A  1 443 ? 5.189   10.541  13.256  1.00 2.00  ? 443  ASP A OD2 1 
ATOM   3543  N  N   . HIS A  1 444 ? 0.934   11.491  13.746  1.00 2.00  ? 444  HIS A N   1 
ATOM   3544  C  CA  . HIS A  1 444 ? 0.261   12.181  12.660  1.00 2.00  ? 444  HIS A CA  1 
ATOM   3545  C  C   . HIS A  1 444 ? -0.896  13.058  13.099  1.00 2.00  ? 444  HIS A C   1 
ATOM   3546  O  O   . HIS A  1 444 ? -1.618  13.597  12.268  1.00 2.00  ? 444  HIS A O   1 
ATOM   3547  C  CB  . HIS A  1 444 ? -0.262  11.129  11.675  1.00 2.35  ? 444  HIS A CB  1 
ATOM   3548  C  CG  . HIS A  1 444 ? 0.731   10.924  10.530  1.00 2.46  ? 444  HIS A CG  1 
ATOM   3549  N  ND1 . HIS A  1 444 ? 0.643   11.583  9.324   1.00 2.72  ? 444  HIS A ND1 1 
ATOM   3550  C  CD2 . HIS A  1 444 ? 1.840   10.152  10.460  1.00 2.69  ? 444  HIS A CD2 1 
ATOM   3551  C  CE1 . HIS A  1 444 ? 1.658   11.228  8.557   1.00 4.05  ? 444  HIS A CE1 1 
ATOM   3552  N  NE2 . HIS A  1 444 ? 2.400   10.361  9.223   1.00 4.37  ? 444  HIS A NE2 1 
ATOM   3553  N  N   . GLY A  1 445 ? -1.089  13.158  14.433  1.00 2.19  ? 445  GLY A N   1 
ATOM   3554  C  CA  . GLY A  1 445 ? -2.162  13.974  15.021  1.00 2.37  ? 445  GLY A CA  1 
ATOM   3555  C  C   . GLY A  1 445 ? -3.584  13.477  14.728  1.00 2.00  ? 445  GLY A C   1 
ATOM   3556  O  O   . GLY A  1 445 ? -4.527  14.253  14.723  1.00 2.00  ? 445  GLY A O   1 
ATOM   3557  N  N   . MET A  1 446 ? -3.755  12.161  14.471  1.00 2.00  ? 446  MET A N   1 
ATOM   3558  C  CA  . MET A  1 446 ? -5.061  11.535  14.156  1.00 2.00  ? 446  MET A CA  1 
ATOM   3559  C  C   . MET A  1 446 ? -6.159  11.785  15.178  1.00 3.59  ? 446  MET A C   1 
ATOM   3560  O  O   . MET A  1 446 ? -6.035  11.401  16.348  1.00 5.26  ? 446  MET A O   1 
ATOM   3561  C  CB  . MET A  1 446 ? -4.897  10.028  14.041  1.00 2.00  ? 446  MET A CB  1 
ATOM   3562  C  CG  . MET A  1 446 ? -4.306  9.576   12.719  1.00 2.34  ? 446  MET A CG  1 
ATOM   3563  S  SD  . MET A  1 446 ? -5.192  10.264  11.315  1.00 2.00  ? 446  MET A SD  1 
ATOM   3564  C  CE  . MET A  1 446 ? -4.158  11.683  10.936  1.00 2.38  ? 446  MET A CE  1 
ATOM   3565  N  N   . PRO A  1 447 ? -7.251  12.444  14.755  1.00 3.40  ? 447  PRO A N   1 
ATOM   3566  C  CA  . PRO A  1 447 ? -8.403  12.653  15.661  1.00 2.00  ? 447  PRO A CA  1 
ATOM   3567  C  C   . PRO A  1 447 ? -8.811  11.334  16.208  1.00 2.00  ? 447  PRO A C   1 
ATOM   3568  O  O   . PRO A  1 447 ? -8.583  10.314  15.549  1.00 2.00  ? 447  PRO A O   1 
ATOM   3569  C  CB  . PRO A  1 447 ? -9.398  13.377  14.802  1.00 2.00  ? 447  PRO A CB  1 
ATOM   3570  C  CG  . PRO A  1 447 ? -8.486  14.296  14.034  1.00 2.00  ? 447  PRO A CG  1 
ATOM   3571  C  CD  . PRO A  1 447 ? -7.124  13.657  13.966  1.00 2.63  ? 447  PRO A CD  1 
ATOM   3572  N  N   . GLY A  1 448 ? -9.412  11.251  17.388  1.00 2.00  ? 448  GLY A N   1 
ATOM   3573  C  CA  . GLY A  1 448 ? -9.905  9.959   17.856  1.00 2.00  ? 448  GLY A CA  1 
ATOM   3574  C  C   . GLY A  1 448 ? -10.856 9.167   16.966  1.00 2.00  ? 448  GLY A C   1 
ATOM   3575  O  O   . GLY A  1 448 ? -11.241 9.599   15.891  1.00 3.60  ? 448  GLY A O   1 
ATOM   3576  N  N   . TYR A  1 449 ? -11.246 7.993   17.433  1.00 2.00  ? 449  TYR A N   1 
ATOM   3577  C  CA  . TYR A  1 449 ? -12.148 7.124   16.690  1.00 2.00  ? 449  TYR A CA  1 
ATOM   3578  C  C   . TYR A  1 449 ? -13.563 7.668   16.474  1.00 2.43  ? 449  TYR A C   1 
ATOM   3579  O  O   . TYR A  1 449 ? -14.076 7.627   15.364  1.00 2.00  ? 449  TYR A O   1 
ATOM   3580  C  CB  . TYR A  1 449 ? -12.226 5.785   17.410  1.00 2.93  ? 449  TYR A CB  1 
ATOM   3581  C  CG  . TYR A  1 449 ? -13.332 4.856   16.971  1.00 2.37  ? 449  TYR A CG  1 
ATOM   3582  C  CD1 . TYR A  1 449 ? -13.214 4.086   15.815  1.00 2.81  ? 449  TYR A CD1 1 
ATOM   3583  C  CD2 . TYR A  1 449 ? -14.464 4.685   17.762  1.00 2.37  ? 449  TYR A CD2 1 
ATOM   3584  C  CE1 . TYR A  1 449 ? -14.191 3.158   15.468  1.00 2.00  ? 449  TYR A CE1 1 
ATOM   3585  C  CE2 . TYR A  1 449 ? -15.442 3.765   17.422  1.00 2.00  ? 449  TYR A CE2 1 
ATOM   3586  C  CZ  . TYR A  1 449 ? -15.297 3.005   16.282  1.00 2.00  ? 449  TYR A CZ  1 
ATOM   3587  O  OH  . TYR A  1 449 ? -16.252 2.072   15.977  1.00 3.13  ? 449  TYR A OH  1 
ATOM   3588  N  N   . ASN A  1 450 ? -14.206 8.154   17.531  1.00 4.17  ? 450  ASN A N   1 
ATOM   3589  C  CA  . ASN A  1 450 ? -15.561 8.674   17.398  1.00 3.94  ? 450  ASN A CA  1 
ATOM   3590  C  C   . ASN A  1 450 ? -15.609 9.861   16.478  1.00 3.31  ? 450  ASN A C   1 
ATOM   3591  O  O   . ASN A  1 450 ? -16.530 9.993   15.673  1.00 4.30  ? 450  ASN A O   1 
ATOM   3592  C  CB  . ASN A  1 450 ? -16.127 9.095   18.747  1.00 6.06  ? 450  ASN A CB  1 
ATOM   3593  C  CG  . ASN A  1 450 ? -16.631 7.925   19.551  1.00 8.40  ? 450  ASN A CG  1 
ATOM   3594  O  OD1 . ASN A  1 450 ? -17.409 7.101   19.059  1.00 9.30  ? 450  ASN A OD1 1 
ATOM   3595  N  ND2 . ASN A  1 450 ? -16.203 7.848   20.804  1.00 10.66 ? 450  ASN A ND2 1 
ATOM   3596  N  N   . SER A  1 451 ? -14.615 10.732  16.607  1.00 2.91  ? 451  SER A N   1 
ATOM   3597  C  CA  . SER A  1 451 ? -14.553 11.927  15.786  1.00 3.02  ? 451  SER A CA  1 
ATOM   3598  C  C   . SER A  1 451 ? -14.589 11.580  14.294  1.00 4.41  ? 451  SER A C   1 
ATOM   3599  O  O   . SER A  1 451 ? -14.746 12.459  13.442  1.00 5.07  ? 451  SER A O   1 
ATOM   3600  C  CB  . SER A  1 451 ? -13.301 12.722  16.123  1.00 2.00  ? 451  SER A CB  1 
ATOM   3601  O  OG  . SER A  1 451 ? -13.601 14.102  16.105  1.00 5.72  ? 451  SER A OG  1 
ATOM   3602  N  N   . TRP A  1 452 ? -14.444 10.293  13.985  1.00 4.05  ? 452  TRP A N   1 
ATOM   3603  C  CA  . TRP A  1 452 ? -14.495 9.819   12.611  1.00 2.00  ? 452  TRP A CA  1 
ATOM   3604  C  C   . TRP A  1 452 ? -15.823 9.136   12.339  1.00 2.55  ? 452  TRP A C   1 
ATOM   3605  O  O   . TRP A  1 452 ? -16.368 9.285   11.256  1.00 4.50  ? 452  TRP A O   1 
ATOM   3606  C  CB  . TRP A  1 452 ? -13.354 8.858   12.322  1.00 2.00  ? 452  TRP A CB  1 
ATOM   3607  C  CG  . TRP A  1 452 ? -12.021 9.532   12.298  1.00 2.94  ? 452  TRP A CG  1 
ATOM   3608  C  CD1 . TRP A  1 452 ? -10.998 9.367   13.186  1.00 2.10  ? 452  TRP A CD1 1 
ATOM   3609  C  CD2 . TRP A  1 452 ? -11.565 10.491  11.338  1.00 3.47  ? 452  TRP A CD2 1 
ATOM   3610  N  NE1 . TRP A  1 452 ? -9.930  10.161  12.841  1.00 2.02  ? 452  TRP A NE1 1 
ATOM   3611  C  CE2 . TRP A  1 452 ? -10.251 10.861  11.709  1.00 2.35  ? 452  TRP A CE2 1 
ATOM   3612  C  CE3 . TRP A  1 452 ? -12.138 11.074  10.199  1.00 2.00  ? 452  TRP A CE3 1 
ATOM   3613  C  CZ2 . TRP A  1 452 ? -9.503  11.786  10.986  1.00 2.00  ? 452  TRP A CZ2 1 
ATOM   3614  C  CZ3 . TRP A  1 452 ? -11.395 11.992  9.484   1.00 2.00  ? 452  TRP A CZ3 1 
ATOM   3615  C  CH2 . TRP A  1 452 ? -10.089 12.338  9.880   1.00 2.00  ? 452  TRP A CH2 1 
ATOM   3616  N  N   . ARG A  1 453 ? -16.351 8.376   13.296  1.00 2.76  ? 453  ARG A N   1 
ATOM   3617  C  CA  . ARG A  1 453 ? -17.652 7.741   13.074  1.00 2.61  ? 453  ARG A CA  1 
ATOM   3618  C  C   . ARG A  1 453 ? -18.617 8.874   12.737  1.00 2.92  ? 453  ARG A C   1 
ATOM   3619  O  O   . ARG A  1 453 ? -19.494 8.742   11.875  1.00 2.00  ? 453  ARG A O   1 
ATOM   3620  C  CB  . ARG A  1 453 ? -18.152 7.026   14.335  1.00 2.00  ? 453  ARG A CB  1 
ATOM   3621  C  CG  . ARG A  1 453 ? -17.477 5.700   14.640  1.00 2.31  ? 453  ARG A CG  1 
ATOM   3622  C  CD  . ARG A  1 453 ? -18.117 4.532   13.890  1.00 2.71  ? 453  ARG A CD  1 
ATOM   3623  N  NE  . ARG A  1 453 ? -19.521 4.333   14.256  1.00 4.01  ? 453  ARG A NE  1 
ATOM   3624  C  CZ  . ARG A  1 453 ? -20.243 3.264   13.921  1.00 4.13  ? 453  ARG A CZ  1 
ATOM   3625  N  NH1 . ARG A  1 453 ? -19.692 2.292   13.208  1.00 4.26  ? 453  ARG A NH1 1 
ATOM   3626  N  NH2 . ARG A  1 453 ? -21.513 3.161   14.300  1.00 3.75  ? 453  ARG A NH2 1 
ATOM   3627  N  N   . GLY A  1 454 ? -18.430 9.996   13.428  1.00 2.25  ? 454  GLY A N   1 
ATOM   3628  C  CA  . GLY A  1 454 ? -19.278 11.150  13.214  1.00 3.39  ? 454  GLY A CA  1 
ATOM   3629  C  C   . GLY A  1 454 ? -19.060 11.742  11.839  1.00 4.44  ? 454  GLY A C   1 
ATOM   3630  O  O   . GLY A  1 454 ? -20.023 12.006  11.113  1.00 3.66  ? 454  GLY A O   1 
ATOM   3631  N  N   . PHE A  1 455 ? -17.791 11.947  11.485  1.00 4.72  ? 455  PHE A N   1 
ATOM   3632  C  CA  . PHE A  1 455 ? -17.432 12.512  10.188  1.00 2.27  ? 455  PHE A CA  1 
ATOM   3633  C  C   . PHE A  1 455 ? -18.089 11.763  9.039   1.00 2.00  ? 455  PHE A C   1 
ATOM   3634  O  O   . PHE A  1 455 ? -18.396 12.361  8.017   1.00 2.75  ? 455  PHE A O   1 
ATOM   3635  C  CB  . PHE A  1 455 ? -15.917 12.496  9.977   1.00 2.73  ? 455  PHE A CB  1 
ATOM   3636  C  CG  . PHE A  1 455 ? -15.504 12.808  8.559   1.00 3.54  ? 455  PHE A CG  1 
ATOM   3637  C  CD1 . PHE A  1 455 ? -15.552 14.114  8.074   1.00 3.18  ? 455  PHE A CD1 1 
ATOM   3638  C  CD2 . PHE A  1 455 ? -15.105 11.788  7.695   1.00 2.18  ? 455  PHE A CD2 1 
ATOM   3639  C  CE1 . PHE A  1 455 ? -15.210 14.396  6.754   1.00 2.80  ? 455  PHE A CE1 1 
ATOM   3640  C  CE2 . PHE A  1 455 ? -14.762 12.061  6.375   1.00 2.00  ? 455  PHE A CE2 1 
ATOM   3641  C  CZ  . PHE A  1 455 ? -14.815 13.363  5.905   1.00 2.00  ? 455  PHE A CZ  1 
ATOM   3642  N  N   . CYS A  1 456 ? -18.287 10.458  9.193   1.00 2.00  ? 456  CYS A N   1 
ATOM   3643  C  CA  . CYS A  1 456 ? -18.926 9.673   8.144   1.00 2.15  ? 456  CYS A CA  1 
ATOM   3644  C  C   . CYS A  1 456 ? -20.421 9.574   8.416   1.00 2.27  ? 456  CYS A C   1 
ATOM   3645  O  O   . CYS A  1 456 ? -21.155 8.923   7.674   1.00 2.00  ? 456  CYS A O   1 
ATOM   3646  C  CB  . CYS A  1 456 ? -18.319 8.275   8.069   1.00 2.36  ? 456  CYS A CB  1 
ATOM   3647  S  SG  . CYS A  1 456 ? -16.600 8.195   7.465   1.00 2.00  ? 456  CYS A SG  1 
ATOM   3648  N  N   . GLY A  1 457 ? -20.856 10.220  9.495   1.00 2.47  ? 457  GLY A N   1 
ATOM   3649  C  CA  . GLY A  1 457 ? -22.262 10.221  9.854   1.00 2.74  ? 457  GLY A CA  1 
ATOM   3650  C  C   . GLY A  1 457 ? -22.798 8.893   10.348  1.00 3.35  ? 457  GLY A C   1 
ATOM   3651  O  O   . GLY A  1 457 ? -23.723 8.322   9.751   1.00 2.13  ? 457  GLY A O   1 
ATOM   3652  N  N   . LEU A  1 458 ? -22.149 8.398   11.436  1.00 3.26  ? 458  LEU A N   1 
ATOM   3653  C  CA  . LEU A  1 458 ? -22.511 7.137   12.129  1.00 3.12  ? 458  LEU A CA  1 
ATOM   3654  C  C   . LEU A  1 458 ? -22.445 7.331   13.642  1.00 4.28  ? 458  LEU A C   1 
ATOM   3655  O  O   . LEU A  1 458 ? -21.724 8.155   14.175  1.00 3.06  ? 458  LEU A O   1 
ATOM   3656  C  CB  . LEU A  1 458 ? -21.628 5.919   11.750  1.00 2.00  ? 458  LEU A CB  1 
ATOM   3657  C  CG  . LEU A  1 458 ? -20.807 5.871   10.446  1.00 2.00  ? 458  LEU A CG  1 
ATOM   3658  C  CD1 . LEU A  1 458 ? -19.937 4.619   10.420  1.00 2.00  ? 458  LEU A CD1 1 
ATOM   3659  C  CD2 . LEU A  1 458 ? -21.705 5.924   9.231   1.00 2.51  ? 458  LEU A CD2 1 
ATOM   3660  N  N   . SER A  1 459 ? -23.301 6.466   14.263  1.00 5.40  ? 459  SER A N   1 
ATOM   3661  C  CA  . SER A  1 459 ? -23.485 6.340   15.683  1.00 6.20  ? 459  SER A CA  1 
ATOM   3662  C  C   . SER A  1 459 ? -22.143 6.454   16.369  1.00 7.14  ? 459  SER A C   1 
ATOM   3663  O  O   . SER A  1 459 ? -21.125 5.875   15.985  1.00 8.53  ? 459  SER A O   1 
ATOM   3664  C  CB  . SER A  1 459 ? -24.180 5.031   16.054  1.00 6.25  ? 459  SER A CB  1 
ATOM   3665  O  OG  . SER A  1 459 ? -24.549 5.019   17.425  1.00 10.08 ? 459  SER A OG  1 
ATOM   3666  N  N   . GLN A  1 460 ? -22.224 7.252   17.376  1.00 7.61  ? 460  GLN A N   1 
ATOM   3667  C  CA  . GLN A  1 460 ? -21.104 7.444   18.191  1.00 8.54  ? 460  GLN A CA  1 
ATOM   3668  C  C   . GLN A  1 460 ? -21.452 6.735   19.505  1.00 7.79  ? 460  GLN A C   1 
ATOM   3669  O  O   . GLN A  1 460 ? -22.354 7.158   20.235  1.00 9.39  ? 460  GLN A O   1 
ATOM   3670  C  CB  . GLN A  1 460 ? -20.753 8.954   18.242  1.00 8.47  ? 460  GLN A CB  1 
ATOM   3671  C  CG  . GLN A  1 460 ? -20.661 9.669   16.864  1.00 8.11  ? 460  GLN A CG  1 
ATOM   3672  C  CD  . GLN A  1 460 ? -20.191 11.124  16.904  1.00 8.80  ? 460  GLN A CD  1 
ATOM   3673  O  OE1 . GLN A  1 460 ? -19.025 11.410  17.222  1.00 8.11  ? 460  GLN A OE1 1 
ATOM   3674  N  NE2 . GLN A  1 460 ? -20.914 12.203  16.613  1.00 8.48  ? 460  GLN A NE2 1 
ATOM   3675  N  N   . PRO A  1 461 ? -20.727 5.619   19.783  1.00 6.15  ? 461  PRO A N   1 
ATOM   3676  C  CA  . PRO A  1 461 ? -20.842 4.948   21.081  1.00 9.31  ? 461  PRO A CA  1 
ATOM   3677  C  C   . PRO A  1 461 ? -20.055 5.566   22.236  1.00 8.78  ? 461  PRO A C   1 
ATOM   3678  O  O   . PRO A  1 461 ? -18.861 5.849   22.106  1.00 7.91  ? 461  PRO A O   1 
ATOM   3679  C  CB  . PRO A  1 461 ? -20.382 3.527   20.770  1.00 8.22  ? 461  PRO A CB  1 
ATOM   3680  C  CG  . PRO A  1 461 ? -19.332 3.763   19.738  1.00 8.24  ? 461  PRO A CG  1 
ATOM   3681  C  CD  . PRO A  1 461 ? -20.022 4.756   18.821  1.00 7.22  ? 461  PRO A CD  1 
ATOM   3682  N  N   . LYS A  1 462 ? -20.742 5.750   23.367  1.00 8.46  ? 462  LYS A N   1 
ATOM   3683  C  CA  . LYS A  1 462 ? -20.147 6.318   24.573  1.00 7.88  ? 462  LYS A CA  1 
ATOM   3684  C  C   . LYS A  1 462 ? -19.964 5.265   25.663  1.00 8.46  ? 462  LYS A C   1 
ATOM   3685  O  O   . LYS A  1 462 ? -18.975 5.280   26.392  1.00 8.35  ? 462  LYS A O   1 
ATOM   3686  C  CB  . LYS A  1 462 ? -21.020 7.453   25.103  1.00 6.67  ? 462  LYS A CB  1 
ATOM   3687  C  CG  . LYS A  1 462 ? -20.847 8.758   24.355  1.00 7.73  ? 462  LYS A CG  1 
ATOM   3688  C  CD  . LYS A  1 462 ? -19.478 9.346   24.665  1.00 8.88  ? 462  LYS A CD  1 
ATOM   3689  C  CE  . LYS A  1 462 ? -19.236 10.675  23.959  1.00 8.41  ? 462  LYS A CE  1 
ATOM   3690  N  NZ  . LYS A  1 462 ? -17.905 11.220  24.346  1.00 4.68  ? 462  LYS A NZ  1 
ATOM   3691  N  N   . THR A  1 463 ? -20.912 4.341   25.767  1.00 8.46  ? 463  THR A N   1 
ATOM   3692  C  CA  . THR A  1 463 ? -20.827 3.306   26.789  1.00 7.25  ? 463  THR A CA  1 
ATOM   3693  C  C   . THR A  1 463 ? -20.257 2.023   26.251  1.00 9.17  ? 463  THR A C   1 
ATOM   3694  O  O   . THR A  1 463 ? -20.091 1.859   25.044  1.00 10.95 ? 463  THR A O   1 
ATOM   3695  C  CB  . THR A  1 463 ? -22.185 2.928   27.321  1.00 7.58  ? 463  THR A CB  1 
ATOM   3696  O  OG1 . THR A  1 463 ? -22.910 2.258   26.283  1.00 6.17  ? 463  THR A OG1 1 
ATOM   3697  C  CG2 . THR A  1 463 ? -22.941 4.163   27.772  1.00 9.31  ? 463  THR A CG2 1 
ATOM   3698  N  N   . LEU A  1 464 ? -19.992 1.105   27.175  1.00 9.45  ? 464  LEU A N   1 
ATOM   3699  C  CA  . LEU A  1 464 ? -19.467 -0.216  26.861  1.00 8.56  ? 464  LEU A CA  1 
ATOM   3700  C  C   . LEU A  1 464 ? -20.602 -0.958  26.176  1.00 8.06  ? 464  LEU A C   1 
ATOM   3701  O  O   . LEU A  1 464 ? -20.390 -1.691  25.222  1.00 8.02  ? 464  LEU A O   1 
ATOM   3702  C  CB  . LEU A  1 464 ? -19.037 -0.922  28.159  1.00 9.27  ? 464  LEU A CB  1 
ATOM   3703  C  CG  . LEU A  1 464 ? -18.592 -2.393  28.297  1.00 9.40  ? 464  LEU A CG  1 
ATOM   3704  C  CD1 . LEU A  1 464 ? -19.776 -3.236  28.747  1.00 8.90  ? 464  LEU A CD1 1 
ATOM   3705  C  CD2 . LEU A  1 464 ? -17.982 -2.919  27.007  1.00 8.07  ? 464  LEU A CD2 1 
ATOM   3706  N  N   . LYS A  1 465 ? -21.820 -0.755  26.652  1.00 10.22 ? 465  LYS A N   1 
ATOM   3707  C  CA  . LYS A  1 465 ? -22.950 -1.417  26.017  1.00 13.75 ? 465  LYS A CA  1 
ATOM   3708  C  C   . LYS A  1 465 ? -23.050 -0.767  24.646  1.00 10.32 ? 465  LYS A C   1 
ATOM   3709  O  O   . LYS A  1 465 ? -23.632 -1.323  23.718  1.00 8.67  ? 465  LYS A O   1 
ATOM   3710  C  CB  . LYS A  1 465 ? -24.251 -1.197  26.824  1.00 19.21 ? 465  LYS A CB  1 
ATOM   3711  C  CG  . LYS A  1 465 ? -25.469 -2.040  26.366  1.00 23.44 ? 465  LYS A CG  1 
ATOM   3712  C  CD  . LYS A  1 465 ? -26.626 -1.976  27.384  1.00 26.34 ? 465  LYS A CD  1 
ATOM   3713  C  CE  . LYS A  1 465 ? -27.784 -2.947  27.042  1.00 28.94 ? 465  LYS A CE  1 
ATOM   3714  N  NZ  . LYS A  1 465 ? -27.738 -4.290  27.735  1.00 29.09 ? 465  LYS A NZ  1 
ATOM   3715  N  N   . GLY A  1 466 ? -22.460 0.417   24.531  1.00 9.67  ? 466  GLY A N   1 
ATOM   3716  C  CA  . GLY A  1 466 ? -22.488 1.133   23.270  1.00 9.06  ? 466  GLY A CA  1 
ATOM   3717  C  C   . GLY A  1 466 ? -21.530 0.550   22.252  1.00 7.85  ? 466  GLY A C   1 
ATOM   3718  O  O   . GLY A  1 466 ? -21.910 0.240   21.120  1.00 7.60  ? 466  GLY A O   1 
ATOM   3719  N  N   . LEU A  1 467 ? -20.280 0.388   22.665  1.00 6.47  ? 467  LEU A N   1 
ATOM   3720  C  CA  . LEU A  1 467 ? -19.265 -0.146  21.781  1.00 6.22  ? 467  LEU A CA  1 
ATOM   3721  C  C   . LEU A  1 467 ? -19.478 -1.612  21.401  1.00 8.27  ? 467  LEU A C   1 
ATOM   3722  O  O   . LEU A  1 467 ? -18.879 -2.090  20.435  1.00 9.33  ? 467  LEU A O   1 
ATOM   3723  C  CB  . LEU A  1 467 ? -17.887 0.018   22.409  1.00 3.54  ? 467  LEU A CB  1 
ATOM   3724  C  CG  . LEU A  1 467 ? -16.779 -0.084  21.367  1.00 2.20  ? 467  LEU A CG  1 
ATOM   3725  C  CD1 . LEU A  1 467 ? -16.834 1.132   20.445  1.00 2.00  ? 467  LEU A CD1 1 
ATOM   3726  C  CD2 . LEU A  1 467 ? -15.439 -0.174  22.059  1.00 2.01  ? 467  LEU A CD2 1 
ATOM   3727  N  N   . GLN A  1 468 ? -20.327 -2.320  22.144  1.00 8.09  ? 468  GLN A N   1 
ATOM   3728  C  CA  . GLN A  1 468 ? -20.590 -3.736  21.859  1.00 8.11  ? 468  GLN A CA  1 
ATOM   3729  C  C   . GLN A  1 468 ? -21.574 -3.930  20.708  1.00 6.75  ? 468  GLN A C   1 
ATOM   3730  O  O   . GLN A  1 468 ? -21.448 -4.864  19.918  1.00 2.01  ? 468  GLN A O   1 
ATOM   3731  C  CB  . GLN A  1 468 ? -21.144 -4.437  23.098  1.00 10.80 ? 468  GLN A CB  1 
ATOM   3732  C  CG  . GLN A  1 468 ? -20.259 -4.357  24.319  1.00 14.01 ? 468  GLN A CG  1 
ATOM   3733  C  CD  . GLN A  1 468 ? -20.931 -4.937  25.547  1.00 15.87 ? 468  GLN A CD  1 
ATOM   3734  O  OE1 . GLN A  1 468 ? -20.428 -4.806  26.661  1.00 18.16 ? 468  GLN A OE1 1 
ATOM   3735  N  NE2 . GLN A  1 468 ? -22.074 -5.588  25.348  1.00 16.68 ? 468  GLN A NE2 1 
ATOM   3736  N  N   . ALA A  1 469 ? -22.556 -3.041  20.634  1.00 7.02  ? 469  ALA A N   1 
ATOM   3737  C  CA  . ALA A  1 469 ? -23.578 -3.088  19.596  1.00 8.19  ? 469  ALA A CA  1 
ATOM   3738  C  C   . ALA A  1 469 ? -22.970 -2.912  18.207  1.00 9.12  ? 469  ALA A C   1 
ATOM   3739  O  O   . ALA A  1 469 ? -23.453 -3.494  17.228  1.00 10.31 ? 469  ALA A O   1 
ATOM   3740  C  CB  . ALA A  1 469 ? -24.616 -2.000  19.850  1.00 7.42  ? 469  ALA A CB  1 
ATOM   3741  N  N   . VAL A  1 470 ? -21.914 -2.104  18.126  1.00 8.89  ? 470  VAL A N   1 
ATOM   3742  C  CA  . VAL A  1 470 ? -21.236 -1.836  16.858  1.00 8.29  ? 470  VAL A CA  1 
ATOM   3743  C  C   . VAL A  1 470 ? -20.253 -2.938  16.468  1.00 7.23  ? 470  VAL A C   1 
ATOM   3744  O  O   . VAL A  1 470 ? -20.304 -3.469  15.357  1.00 5.60  ? 470  VAL A O   1 
ATOM   3745  C  CB  . VAL A  1 470 ? -20.474 -0.487  16.916  1.00 8.54  ? 470  VAL A CB  1 
ATOM   3746  C  CG1 . VAL A  1 470 ? -19.509 -0.368  15.744  1.00 6.40  ? 470  VAL A CG1 1 
ATOM   3747  C  CG2 . VAL A  1 470 ? -21.466 0.663   16.882  1.00 8.28  ? 470  VAL A CG2 1 
ATOM   3748  N  N   . LEU A  1 471 ? -19.355 -3.267  17.391  1.00 7.19  ? 471  LEU A N   1 
ATOM   3749  C  CA  . LEU A  1 471 ? -18.352 -4.296  17.157  1.00 7.64  ? 471  LEU A CA  1 
ATOM   3750  C  C   . LEU A  1 471 ? -18.983 -5.685  17.070  1.00 8.63  ? 471  LEU A C   1 
ATOM   3751  O  O   . LEU A  1 471 ? -18.392 -6.613  16.511  1.00 9.00  ? 471  LEU A O   1 
ATOM   3752  C  CB  . LEU A  1 471 ? -17.292 -4.235  18.270  1.00 4.29  ? 471  LEU A CB  1 
ATOM   3753  C  CG  . LEU A  1 471 ? -16.101 -3.285  18.046  1.00 2.33  ? 471  LEU A CG  1 
ATOM   3754  C  CD1 . LEU A  1 471 ? -16.414 -2.279  16.963  1.00 2.92  ? 471  LEU A CD1 1 
ATOM   3755  C  CD2 . LEU A  1 471 ? -15.750 -2.577  19.328  1.00 2.00  ? 471  LEU A CD2 1 
ATOM   3756  N  N   . LYS A  1 472 ? -20.200 -5.811  17.594  1.00 10.26 ? 472  LYS A N   1 
ATOM   3757  C  CA  . LYS A  1 472 ? -20.914 -7.086  17.595  1.00 11.49 ? 472  LYS A CA  1 
ATOM   3758  C  C   . LYS A  1 472 ? -20.072 -8.127  18.326  1.00 12.25 ? 472  LYS A C   1 
ATOM   3759  O  O   . LYS A  1 472 ? -20.115 -9.316  18.013  1.00 12.34 ? 472  LYS A O   1 
ATOM   3760  C  CB  . LYS A  1 472 ? -21.191 -7.559  16.162  1.00 11.92 ? 472  LYS A CB  1 
ATOM   3761  C  CG  . LYS A  1 472 ? -22.665 -7.696  15.834  1.00 12.69 ? 472  LYS A CG  1 
ATOM   3762  C  CD  . LYS A  1 472 ? -23.306 -6.334  15.646  1.00 16.04 ? 472  LYS A CD  1 
ATOM   3763  C  CE  . LYS A  1 472 ? -24.831 -6.396  15.772  1.00 19.48 ? 472  LYS A CE  1 
ATOM   3764  N  NZ  . LYS A  1 472 ? -25.475 -7.445  14.916  1.00 20.21 ? 472  LYS A NZ  1 
ATOM   3765  N  N   . ASN A  1 473 ? -19.309 -7.664  19.310  1.00 12.50 ? 473  ASN A N   1 
ATOM   3766  C  CA  . ASN A  1 473 ? -18.439 -8.537  20.084  1.00 13.78 ? 473  ASN A CA  1 
ATOM   3767  C  C   . ASN A  1 473 ? -18.243 -7.954  21.488  1.00 15.80 ? 473  ASN A C   1 
ATOM   3768  O  O   . ASN A  1 473 ? -17.534 -6.963  21.655  1.00 16.21 ? 473  ASN A O   1 
ATOM   3769  C  CB  . ASN A  1 473 ? -17.094 -8.653  19.368  1.00 14.23 ? 473  ASN A CB  1 
ATOM   3770  C  CG  . ASN A  1 473 ? -16.150 -9.598  20.063  1.00 15.54 ? 473  ASN A CG  1 
ATOM   3771  O  OD1 . ASN A  1 473 ? -15.853 -9.438  21.250  1.00 15.92 ? 473  ASN A OD1 1 
ATOM   3772  N  ND2 . ASN A  1 473 ? -15.669 -10.595 19.328  1.00 15.67 ? 473  ASN A ND2 1 
ATOM   3773  N  N   . LYS A  1 474 ? -18.856 -8.566  22.499  1.00 17.16 ? 474  LYS A N   1 
ATOM   3774  C  CA  . LYS A  1 474 ? -18.742 -8.042  23.862  1.00 18.48 ? 474  LYS A CA  1 
ATOM   3775  C  C   . LYS A  1 474 ? -17.286 -7.995  24.338  1.00 18.75 ? 474  LYS A C   1 
ATOM   3776  O  O   . LYS A  1 474 ? -16.697 -6.919  24.493  1.00 18.60 ? 474  LYS A O   1 
ATOM   3777  C  CB  . LYS A  1 474 ? -19.556 -8.896  24.846  1.00 22.54 ? 474  LYS A CB  1 
ATOM   3778  C  CG  . LYS A  1 474 ? -21.008 -9.214  24.456  1.00 27.25 ? 474  LYS A CG  1 
ATOM   3779  C  CD  . LYS A  1 474 ? -21.547 -10.337 25.369  1.00 30.59 ? 474  LYS A CD  1 
ATOM   3780  C  CE  . LYS A  1 474 ? -22.818 -11.014 24.833  1.00 32.88 ? 474  LYS A CE  1 
ATOM   3781  N  NZ  . LYS A  1 474 ? -23.019 -12.386 25.435  1.00 34.45 ? 474  LYS A NZ  1 
ATOM   3782  N  N   . ILE A  1 475 ? -16.718 -9.173  24.575  1.00 16.92 ? 475  ILE A N   1 
ATOM   3783  C  CA  . ILE A  1 475 ? -15.346 -9.302  25.041  1.00 14.08 ? 475  ILE A CA  1 
ATOM   3784  C  C   . ILE A  1 475 ? -14.397 -8.277  24.423  1.00 13.32 ? 475  ILE A C   1 
ATOM   3785  O  O   . ILE A  1 475 ? -13.629 -7.637  25.142  1.00 13.63 ? 475  ILE A O   1 
ATOM   3786  C  CB  . ILE A  1 475 ? -14.822 -10.720 24.768  1.00 14.63 ? 475  ILE A CB  1 
ATOM   3787  C  CG1 . ILE A  1 475 ? -13.296 -10.720 24.723  1.00 15.55 ? 475  ILE A CG1 1 
ATOM   3788  C  CG2 . ILE A  1 475 ? -15.411 -11.240 23.483  1.00 15.22 ? 475  ILE A CG2 1 
ATOM   3789  C  CD1 . ILE A  1 475 ? -12.653 -10.273 26.015  1.00 17.27 ? 475  ILE A CD1 1 
ATOM   3790  N  N   . LEU A  1 476 ? -14.444 -8.116  23.102  1.00 11.61 ? 476  LEU A N   1 
ATOM   3791  C  CA  . LEU A  1 476 ? -13.562 -7.151  22.443  1.00 9.88  ? 476  LEU A CA  1 
ATOM   3792  C  C   . LEU A  1 476 ? -13.828 -5.749  22.961  1.00 8.09  ? 476  LEU A C   1 
ATOM   3793  O  O   . LEU A  1 476 ? -12.921 -5.080  23.465  1.00 8.71  ? 476  LEU A O   1 
ATOM   3794  C  CB  . LEU A  1 476 ? -13.747 -7.175  20.922  1.00 8.20  ? 476  LEU A CB  1 
ATOM   3795  C  CG  . LEU A  1 476 ? -12.861 -6.206  20.125  1.00 7.45  ? 476  LEU A CG  1 
ATOM   3796  C  CD1 . LEU A  1 476 ? -11.459 -6.138  20.713  1.00 6.10  ? 476  LEU A CD1 1 
ATOM   3797  C  CD2 . LEU A  1 476 ? -12.809 -6.668  18.680  1.00 7.53  ? 476  LEU A CD2 1 
ATOM   3798  N  N   . ALA A  1 477 ? -15.077 -5.315  22.843  1.00 5.86  ? 477  ALA A N   1 
ATOM   3799  C  CA  . ALA A  1 477 ? -15.467 -3.992  23.305  1.00 5.89  ? 477  ALA A CA  1 
ATOM   3800  C  C   . ALA A  1 477 ? -14.889 -3.743  24.698  1.00 4.95  ? 477  ALA A C   1 
ATOM   3801  O  O   . ALA A  1 477 ? -14.499 -2.612  25.033  1.00 2.00  ? 477  ALA A O   1 
ATOM   3802  C  CB  . ALA A  1 477 ? -17.000 -3.869  23.325  1.00 4.31  ? 477  ALA A CB  1 
ATOM   3803  N  N   . LYS A  1 478 ? -14.809 -4.807  25.497  1.00 3.74  ? 478  LYS A N   1 
ATOM   3804  C  CA  . LYS A  1 478 ? -14.284 -4.677  26.851  1.00 5.55  ? 478  LYS A CA  1 
ATOM   3805  C  C   . LYS A  1 478 ? -12.769 -4.533  26.896  1.00 5.19  ? 478  LYS A C   1 
ATOM   3806  O  O   . LYS A  1 478 ? -12.251 -3.624  27.543  1.00 6.39  ? 478  LYS A O   1 
ATOM   3807  C  CB  . LYS A  1 478 ? -14.691 -5.864  27.726  1.00 6.14  ? 478  LYS A CB  1 
ATOM   3808  C  CG  . LYS A  1 478 ? -14.550 -5.568  29.225  1.00 8.16  ? 478  LYS A CG  1 
ATOM   3809  C  CD  . LYS A  1 478 ? -14.481 -6.841  30.068  1.00 10.33 ? 478  LYS A CD  1 
ATOM   3810  C  CE  . LYS A  1 478 ? -13.048 -7.121  30.545  1.00 10.87 ? 478  LYS A CE  1 
ATOM   3811  N  NZ  . LYS A  1 478 ? -12.601 -8.527  30.310  1.00 8.84  ? 478  LYS A NZ  1 
ATOM   3812  N  N   . LYS A  1 479 ? -12.062 -5.439  26.228  1.00 4.47  ? 479  LYS A N   1 
ATOM   3813  C  CA  . LYS A  1 479 ? -10.603 -5.403  26.200  1.00 3.78  ? 479  LYS A CA  1 
ATOM   3814  C  C   . LYS A  1 479 ? -10.194 -4.038  25.706  1.00 3.03  ? 479  LYS A C   1 
ATOM   3815  O  O   . LYS A  1 479 ? -9.256  -3.416  26.205  1.00 2.00  ? 479  LYS A O   1 
ATOM   3816  C  CB  . LYS A  1 479 ? -10.062 -6.460  25.231  1.00 5.13  ? 479  LYS A CB  1 
ATOM   3817  C  CG  . LYS A  1 479 ? -10.089 -7.899  25.748  1.00 6.88  ? 479  LYS A CG  1 
ATOM   3818  C  CD  . LYS A  1 479 ? -9.871  -8.906  24.611  1.00 8.56  ? 479  LYS A CD  1 
ATOM   3819  C  CE  . LYS A  1 479 ? -9.366  -10.264 25.121  1.00 9.11  ? 479  LYS A CE  1 
ATOM   3820  N  NZ  . LYS A  1 479 ? -9.261  -11.310 24.049  1.00 7.99  ? 479  LYS A NZ  1 
ATOM   3821  N  N   . LEU A  1 480 ? -10.938 -3.575  24.717  1.00 2.00  ? 480  LEU A N   1 
ATOM   3822  C  CA  . LEU A  1 480 ? -10.664 -2.298  24.100  1.00 2.91  ? 480  LEU A CA  1 
ATOM   3823  C  C   . LEU A  1 480 ? -10.638 -1.120  25.059  1.00 4.77  ? 480  LEU A C   1 
ATOM   3824  O  O   . LEU A  1 480 ? -9.689  -0.334  25.032  1.00 3.96  ? 480  LEU A O   1 
ATOM   3825  C  CB  . LEU A  1 480 ? -11.672 -2.043  22.981  1.00 3.63  ? 480  LEU A CB  1 
ATOM   3826  C  CG  . LEU A  1 480 ? -11.128 -1.397  21.703  1.00 2.72  ? 480  LEU A CG  1 
ATOM   3827  C  CD1 . LEU A  1 480 ? -9.597  -1.421  21.687  1.00 2.15  ? 480  LEU A CD1 1 
ATOM   3828  C  CD2 . LEU A  1 480 ? -11.695 -2.150  20.509  1.00 2.00  ? 480  LEU A CD2 1 
ATOM   3829  N  N   . LEU A  1 481 ? -11.660 -0.981  25.905  1.00 5.35  ? 481  LEU A N   1 
ATOM   3830  C  CA  . LEU A  1 481 ? -11.676 0.153   26.835  1.00 5.95  ? 481  LEU A CA  1 
ATOM   3831  C  C   . LEU A  1 481 ? -11.226 -0.123  28.265  1.00 5.93  ? 481  LEU A C   1 
ATOM   3832  O  O   . LEU A  1 481 ? -11.202 0.764   29.116  1.00 4.21  ? 481  LEU A O   1 
ATOM   3833  C  CB  . LEU A  1 481 ? -13.034 0.850   26.813  1.00 6.16  ? 481  LEU A CB  1 
ATOM   3834  C  CG  . LEU A  1 481 ? -14.321 0.057   26.925  1.00 6.17  ? 481  LEU A CG  1 
ATOM   3835  C  CD1 . LEU A  1 481 ? -14.655 -0.157  28.384  1.00 7.30  ? 481  LEU A CD1 1 
ATOM   3836  C  CD2 . LEU A  1 481 ? -15.428 0.850   26.242  1.00 7.79  ? 481  LEU A CD2 1 
ATOM   3837  N  N   . ASP A  1 482 ? -10.871 -1.362  28.539  1.00 6.34  ? 482  ASP A N   1 
ATOM   3838  C  CA  . ASP A  1 482 ? -10.329 -1.655  29.839  1.00 7.56  ? 482  ASP A CA  1 
ATOM   3839  C  C   . ASP A  1 482 ? -8.998  -0.954  29.662  1.00 8.18  ? 482  ASP A C   1 
ATOM   3840  O  O   . ASP A  1 482 ? -8.258  -0.715  30.614  1.00 8.96  ? 482  ASP A O   1 
ATOM   3841  C  CB  . ASP A  1 482 ? -10.072 -3.142  29.973  1.00 11.88 ? 482  ASP A CB  1 
ATOM   3842  C  CG  . ASP A  1 482 ? -11.042 -3.806  30.880  1.00 14.61 ? 482  ASP A CG  1 
ATOM   3843  O  OD1 . ASP A  1 482 ? -12.209 -3.361  30.905  1.00 16.88 ? 482  ASP A OD1 1 
ATOM   3844  O  OD2 . ASP A  1 482 ? -10.640 -4.774  31.559  1.00 17.44 ? 482  ASP A OD2 1 
ATOM   3845  N  N   . LEU A  1 483 ? -8.715  -0.636  28.400  1.00 7.81  ? 483  LEU A N   1 
ATOM   3846  C  CA  . LEU A  1 483 ? -7.467  -0.002  27.985  1.00 6.61  ? 483  LEU A CA  1 
ATOM   3847  C  C   . LEU A  1 483 ? -7.541  1.469   27.607  1.00 5.56  ? 483  LEU A C   1 
ATOM   3848  O  O   . LEU A  1 483 ? -6.658  2.259   27.958  1.00 4.46  ? 483  LEU A O   1 
ATOM   3849  C  CB  . LEU A  1 483 ? -6.903  -0.765  26.797  1.00 5.17  ? 483  LEU A CB  1 
ATOM   3850  C  CG  . LEU A  1 483 ? -5.803  -1.755  27.109  1.00 4.18  ? 483  LEU A CG  1 
ATOM   3851  C  CD1 . LEU A  1 483 ? -5.791  -2.801  26.024  1.00 5.60  ? 483  LEU A CD1 1 
ATOM   3852  C  CD2 . LEU A  1 483 ? -4.473  -1.028  27.210  1.00 4.37  ? 483  LEU A CD2 1 
ATOM   3853  N  N   . TYR A  1 484 ? -8.585  1.811   26.859  1.00 5.10  ? 484  TYR A N   1 
ATOM   3854  C  CA  . TYR A  1 484 ? -8.803  3.165   26.378  1.00 3.91  ? 484  TYR A CA  1 
ATOM   3855  C  C   . TYR A  1 484 ? -9.726  3.940   27.298  1.00 2.69  ? 484  TYR A C   1 
ATOM   3856  O  O   . TYR A  1 484 ? -9.776  5.164   27.259  1.00 2.00  ? 484  TYR A O   1 
ATOM   3857  C  CB  . TYR A  1 484 ? -9.362  3.106   24.952  1.00 4.37  ? 484  TYR A CB  1 
ATOM   3858  C  CG  . TYR A  1 484 ? -8.281  2.926   23.893  1.00 3.88  ? 484  TYR A CG  1 
ATOM   3859  C  CD1 . TYR A  1 484 ? -7.383  3.958   23.617  1.00 2.62  ? 484  TYR A CD1 1 
ATOM   3860  C  CD2 . TYR A  1 484 ? -8.157  1.735   23.167  1.00 2.99  ? 484  TYR A CD2 1 
ATOM   3861  C  CE1 . TYR A  1 484 ? -6.402  3.820   22.656  1.00 2.00  ? 484  TYR A CE1 1 
ATOM   3862  C  CE2 . TYR A  1 484 ? -7.169  1.590   22.196  1.00 2.00  ? 484  TYR A CE2 1 
ATOM   3863  C  CZ  . TYR A  1 484 ? -6.296  2.643   21.949  1.00 2.00  ? 484  TYR A CZ  1 
ATOM   3864  O  OH  . TYR A  1 484 ? -5.311  2.541   20.997  1.00 2.00  ? 484  TYR A OH  1 
ATOM   3865  N  N   . LYS A  1 485 ? -10.447 3.205   28.133  1.00 4.39  ? 485  LYS A N   1 
ATOM   3866  C  CA  . LYS A  1 485 ? -11.364 3.783   29.110  1.00 4.45  ? 485  LYS A CA  1 
ATOM   3867  C  C   . LYS A  1 485 ? -12.545 4.525   28.497  1.00 4.72  ? 485  LYS A C   1 
ATOM   3868  O  O   . LYS A  1 485 ? -13.567 4.702   29.163  1.00 4.07  ? 485  LYS A O   1 
ATOM   3869  C  CB  . LYS A  1 485 ? -10.600 4.710   30.059  1.00 5.78  ? 485  LYS A CB  1 
ATOM   3870  C  CG  . LYS A  1 485 ? -9.264  4.140   30.548  1.00 7.86  ? 485  LYS A CG  1 
ATOM   3871  C  CD  . LYS A  1 485 ? -9.409  2.889   31.426  1.00 8.42  ? 485  LYS A CD  1 
ATOM   3872  C  CE  . LYS A  1 485 ? -8.027  2.255   31.688  1.00 9.13  ? 485  LYS A CE  1 
ATOM   3873  N  NZ  . LYS A  1 485 ? -7.938  1.366   32.899  1.00 7.04  ? 485  LYS A NZ  1 
ATOM   3874  N  N   . THR A  1 486 ? -12.405 4.964   27.243  1.00 4.24  ? 486  THR A N   1 
ATOM   3875  C  CA  . THR A  1 486 ? -13.489 5.660   26.535  1.00 2.86  ? 486  THR A CA  1 
ATOM   3876  C  C   . THR A  1 486 ? -13.408 5.559   25.020  1.00 3.23  ? 486  THR A C   1 
ATOM   3877  O  O   . THR A  1 486 ? -12.337 5.668   24.426  1.00 3.60  ? 486  THR A O   1 
ATOM   3878  C  CB  . THR A  1 486 ? -13.565 7.166   26.858  1.00 2.24  ? 486  THR A CB  1 
ATOM   3879  O  OG1 . THR A  1 486 ? -14.738 7.709   26.243  1.00 2.00  ? 486  THR A OG1 1 
ATOM   3880  C  CG2 . THR A  1 486 ? -12.358 7.909   26.298  1.00 2.16  ? 486  THR A CG2 1 
ATOM   3881  N  N   . PRO A  1 487 ? -14.556 5.352   24.372  1.00 3.29  ? 487  PRO A N   1 
ATOM   3882  C  CA  . PRO A  1 487 ? -14.609 5.242   22.918  1.00 2.82  ? 487  PRO A CA  1 
ATOM   3883  C  C   . PRO A  1 487 ? -13.915 6.414   22.249  1.00 4.20  ? 487  PRO A C   1 
ATOM   3884  O  O   . PRO A  1 487 ? -13.340 6.262   21.169  1.00 4.04  ? 487  PRO A O   1 
ATOM   3885  C  CB  . PRO A  1 487 ? -16.105 5.225   22.635  1.00 3.93  ? 487  PRO A CB  1 
ATOM   3886  C  CG  . PRO A  1 487 ? -16.634 4.461   23.796  1.00 4.97  ? 487  PRO A CG  1 
ATOM   3887  C  CD  . PRO A  1 487 ? -15.870 5.060   24.967  1.00 4.70  ? 487  PRO A CD  1 
ATOM   3888  N  N   . ASP A  1 488 ? -13.967 7.580   22.890  1.00 2.95  ? 488  ASP A N   1 
ATOM   3889  C  CA  . ASP A  1 488 ? -13.346 8.772   22.321  1.00 4.65  ? 488  ASP A CA  1 
ATOM   3890  C  C   . ASP A  1 488 ? -11.833 8.612   22.095  1.00 4.05  ? 488  ASP A C   1 
ATOM   3891  O  O   . ASP A  1 488 ? -11.278 9.172   21.150  1.00 2.47  ? 488  ASP A O   1 
ATOM   3892  C  CB  . ASP A  1 488 ? -13.589 10.011  23.214  1.00 7.00  ? 488  ASP A CB  1 
ATOM   3893  C  CG  . ASP A  1 488 ? -15.074 10.386  23.351  1.00 8.91  ? 488  ASP A CG  1 
ATOM   3894  O  OD1 . ASP A  1 488 ? -15.853 10.164  22.392  1.00 7.65  ? 488  ASP A OD1 1 
ATOM   3895  O  OD2 . ASP A  1 488 ? -15.448 10.929  24.424  1.00 8.95  ? 488  ASP A OD2 1 
ATOM   3896  N  N   . ASN A  1 489 ? -11.164 7.835   22.938  1.00 3.33  ? 489  ASN A N   1 
ATOM   3897  C  CA  . ASN A  1 489 ? -9.722  7.691   22.790  1.00 3.23  ? 489  ASN A CA  1 
ATOM   3898  C  C   . ASN A  1 489 ? -9.150  6.545   21.961  1.00 3.23  ? 489  ASN A C   1 
ATOM   3899  O  O   . ASN A  1 489 ? -7.936  6.494   21.761  1.00 4.38  ? 489  ASN A O   1 
ATOM   3900  C  CB  . ASN A  1 489 ? -9.065  7.707   24.170  1.00 3.67  ? 489  ASN A CB  1 
ATOM   3901  C  CG  . ASN A  1 489 ? -9.237  9.040   24.873  1.00 3.85  ? 489  ASN A CG  1 
ATOM   3902  O  OD1 . ASN A  1 489 ? -9.351  10.086  24.226  1.00 5.05  ? 489  ASN A OD1 1 
ATOM   3903  N  ND2 . ASN A  1 489 ? -9.243  9.014   26.197  1.00 4.27  ? 489  ASN A ND2 1 
ATOM   3904  N  N   . ILE A  1 490 ? -9.997  5.635   21.479  1.00 3.33  ? 490  ILE A N   1 
ATOM   3905  C  CA  . ILE A  1 490 ? -9.528  4.519   20.645  1.00 2.08  ? 490  ILE A CA  1 
ATOM   3906  C  C   . ILE A  1 490 ? -8.813  5.079   19.410  1.00 2.00  ? 490  ILE A C   1 
ATOM   3907  O  O   . ILE A  1 490 ? -9.353  5.940   18.709  1.00 2.00  ? 490  ILE A O   1 
ATOM   3908  C  CB  . ILE A  1 490 ? -10.716 3.621   20.169  1.00 2.00  ? 490  ILE A CB  1 
ATOM   3909  C  CG1 . ILE A  1 490 ? -10.831 2.381   21.048  1.00 2.00  ? 490  ILE A CG1 1 
ATOM   3910  C  CG2 . ILE A  1 490 ? -10.519 3.188   18.730  1.00 2.00  ? 490  ILE A CG2 1 
ATOM   3911  C  CD1 . ILE A  1 490 ? -12.175 2.223   21.675  1.00 2.00  ? 490  ILE A CD1 1 
ATOM   3912  N  N   . ASP A  1 491 ? -7.600  4.596   19.153  1.00 2.00  ? 491  ASP A N   1 
ATOM   3913  C  CA  . ASP A  1 491 ? -6.831  5.047   17.992  1.00 2.31  ? 491  ASP A CA  1 
ATOM   3914  C  C   . ASP A  1 491 ? -7.566  4.633   16.713  1.00 2.00  ? 491  ASP A C   1 
ATOM   3915  O  O   . ASP A  1 491 ? -8.020  3.498   16.585  1.00 2.00  ? 491  ASP A O   1 
ATOM   3916  C  CB  . ASP A  1 491 ? -5.414  4.449   18.026  1.00 2.54  ? 491  ASP A CB  1 
ATOM   3917  C  CG  . ASP A  1 491 ? -4.495  5.160   19.020  1.00 2.00  ? 491  ASP A CG  1 
ATOM   3918  O  OD1 . ASP A  1 491 ? -4.347  6.399   18.924  1.00 2.00  ? 491  ASP A OD1 1 
ATOM   3919  O  OD2 . ASP A  1 491 ? -3.913  4.478   19.889  1.00 2.00  ? 491  ASP A OD2 1 
ATOM   3920  N  N   . ILE A  1 492 ? -7.674  5.543   15.757  1.00 2.00  ? 492  ILE A N   1 
ATOM   3921  C  CA  . ILE A  1 492 ? -8.412  5.231   14.544  1.00 2.00  ? 492  ILE A CA  1 
ATOM   3922  C  C   . ILE A  1 492 ? -8.092  3.856   13.953  1.00 2.42  ? 492  ILE A C   1 
ATOM   3923  O  O   . ILE A  1 492 ? -8.957  2.979   13.935  1.00 2.96  ? 492  ILE A O   1 
ATOM   3924  C  CB  . ILE A  1 492 ? -8.248  6.380   13.484  1.00 2.56  ? 492  ILE A CB  1 
ATOM   3925  C  CG1 . ILE A  1 492 ? -9.581  6.622   12.756  1.00 2.00  ? 492  ILE A CG1 1 
ATOM   3926  C  CG2 . ILE A  1 492 ? -7.119  6.076   12.516  1.00 2.76  ? 492  ILE A CG2 1 
ATOM   3927  C  CD1 . ILE A  1 492 ? -10.000 5.557   11.780  1.00 3.24  ? 492  ILE A CD1 1 
ATOM   3928  N  N   . TRP A  1 493 ? -6.856  3.653   13.509  1.00 2.00  ? 493  TRP A N   1 
ATOM   3929  C  CA  . TRP A  1 493 ? -6.443  2.386   12.908  1.00 2.07  ? 493  TRP A CA  1 
ATOM   3930  C  C   . TRP A  1 493 ? -7.115  1.132   13.481  1.00 2.00  ? 493  TRP A C   1 
ATOM   3931  O  O   . TRP A  1 493 ? -7.776  0.383   12.763  1.00 2.33  ? 493  TRP A O   1 
ATOM   3932  C  CB  . TRP A  1 493 ? -4.928  2.231   13.021  1.00 2.00  ? 493  TRP A CB  1 
ATOM   3933  C  CG  . TRP A  1 493 ? -4.423  1.029   12.310  1.00 2.00  ? 493  TRP A CG  1 
ATOM   3934  C  CD1 . TRP A  1 493 ? -4.440  0.806   10.966  1.00 2.00  ? 493  TRP A CD1 1 
ATOM   3935  C  CD2 . TRP A  1 493 ? -3.844  -0.135  12.903  1.00 2.49  ? 493  TRP A CD2 1 
ATOM   3936  N  NE1 . TRP A  1 493 ? -3.910  -0.425  10.683  1.00 2.00  ? 493  TRP A NE1 1 
ATOM   3937  C  CE2 . TRP A  1 493 ? -3.537  -1.026  11.855  1.00 2.00  ? 493  TRP A CE2 1 
ATOM   3938  C  CE3 . TRP A  1 493 ? -3.558  -0.516  14.224  1.00 2.82  ? 493  TRP A CE3 1 
ATOM   3939  C  CZ2 . TRP A  1 493 ? -2.956  -2.272  12.082  1.00 2.00  ? 493  TRP A CZ2 1 
ATOM   3940  C  CZ3 . TRP A  1 493 ? -2.979  -1.760  14.450  1.00 2.18  ? 493  TRP A CZ3 1 
ATOM   3941  C  CH2 . TRP A  1 493 ? -2.686  -2.622  13.382  1.00 2.16  ? 493  TRP A CH2 1 
ATOM   3942  N  N   . ILE A  1 494 ? -6.940  0.906   14.776  1.00 2.00  ? 494  ILE A N   1 
ATOM   3943  C  CA  . ILE A  1 494 ? -7.512  -0.260  15.425  1.00 2.00  ? 494  ILE A CA  1 
ATOM   3944  C  C   . ILE A  1 494 ? -9.026  -0.176  15.490  1.00 2.61  ? 494  ILE A C   1 
ATOM   3945  O  O   . ILE A  1 494 ? -9.724  -1.080  15.031  1.00 2.51  ? 494  ILE A O   1 
ATOM   3946  C  CB  . ILE A  1 494 ? -6.931  -0.426  16.840  1.00 2.00  ? 494  ILE A CB  1 
ATOM   3947  C  CG1 . ILE A  1 494 ? -7.620  -1.583  17.559  1.00 3.12  ? 494  ILE A CG1 1 
ATOM   3948  C  CG2 . ILE A  1 494 ? -7.068  0.865   17.610  1.00 2.00  ? 494  ILE A CG2 1 
ATOM   3949  C  CD1 . ILE A  1 494 ? -6.986  -1.926  18.893  1.00 2.32  ? 494  ILE A CD1 1 
ATOM   3950  N  N   . GLY A  1 495 ? -9.531  0.914   16.058  1.00 3.00  ? 495  GLY A N   1 
ATOM   3951  C  CA  . GLY A  1 495 ? -10.968 1.093   16.160  1.00 2.63  ? 495  GLY A CA  1 
ATOM   3952  C  C   . GLY A  1 495 ? -11.638 0.880   14.818  1.00 2.05  ? 495  GLY A C   1 
ATOM   3953  O  O   . GLY A  1 495 ? -12.679 0.234   14.719  1.00 2.00  ? 495  GLY A O   1 
ATOM   3954  N  N   . GLY A  1 496 ? -11.038 1.432   13.773  1.00 2.00  ? 496  GLY A N   1 
ATOM   3955  C  CA  . GLY A  1 496 ? -11.605 1.259   12.458  1.00 2.00  ? 496  GLY A CA  1 
ATOM   3956  C  C   . GLY A  1 496 ? -11.554 -0.216  12.135  1.00 2.22  ? 496  GLY A C   1 
ATOM   3957  O  O   . GLY A  1 496 ? -12.572 -0.840  11.839  1.00 2.88  ? 496  GLY A O   1 
ATOM   3958  N  N   . ASN A  1 497 ? -10.359 -0.786  12.226  1.00 2.03  ? 497  ASN A N   1 
ATOM   3959  C  CA  . ASN A  1 497 ? -10.171 -2.191  11.914  1.00 2.00  ? 497  ASN A CA  1 
ATOM   3960  C  C   . ASN A  1 497 ? -10.907 -3.148  12.804  1.00 2.03  ? 497  ASN A C   1 
ATOM   3961  O  O   . ASN A  1 497 ? -10.962 -4.346  12.534  1.00 2.00  ? 497  ASN A O   1 
ATOM   3962  C  CB  . ASN A  1 497 ? -8.697  -2.529  11.922  1.00 2.00  ? 497  ASN A CB  1 
ATOM   3963  C  CG  . ASN A  1 497 ? -8.039  -2.138  10.645  1.00 2.47  ? 497  ASN A CG  1 
ATOM   3964  O  OD1 . ASN A  1 497 ? -7.263  -1.182  10.592  1.00 4.75  ? 497  ASN A OD1 1 
ATOM   3965  N  ND2 . ASN A  1 497 ? -8.370  -2.858  9.579   1.00 3.12  ? 497  ASN A ND2 1 
ATOM   3966  N  N   . ALA A  1 498 ? -11.488 -2.625  13.867  1.00 2.40  ? 498  ALA A N   1 
ATOM   3967  C  CA  . ALA A  1 498 ? -12.207 -3.484  14.774  1.00 2.19  ? 498  ALA A CA  1 
ATOM   3968  C  C   . ALA A  1 498 ? -13.627 -3.783  14.292  1.00 2.70  ? 498  ALA A C   1 
ATOM   3969  O  O   . ALA A  1 498 ? -14.105 -4.897  14.468  1.00 2.88  ? 498  ALA A O   1 
ATOM   3970  C  CB  . ALA A  1 498 ? -12.227 -2.864  16.166  1.00 2.00  ? 498  ALA A CB  1 
ATOM   3971  N  N   . GLU A  1 499 ? -14.298 -2.815  13.670  1.00 2.00  ? 499  GLU A N   1 
ATOM   3972  C  CA  . GLU A  1 499 ? -15.675 -3.038  13.220  1.00 2.00  ? 499  GLU A CA  1 
ATOM   3973  C  C   . GLU A  1 499 ? -15.812 -4.219  12.253  1.00 2.40  ? 499  GLU A C   1 
ATOM   3974  O  O   . GLU A  1 499 ? -15.026 -4.351  11.312  1.00 2.00  ? 499  GLU A O   1 
ATOM   3975  C  CB  . GLU A  1 499 ? -16.221 -1.779  12.555  1.00 2.00  ? 499  GLU A CB  1 
ATOM   3976  C  CG  . GLU A  1 499 ? -15.823 -0.486  13.239  1.00 2.26  ? 499  GLU A CG  1 
ATOM   3977  C  CD  . GLU A  1 499 ? -16.549 0.721   12.659  1.00 3.60  ? 499  GLU A CD  1 
ATOM   3978  O  OE1 . GLU A  1 499 ? -16.782 0.751   11.426  1.00 3.30  ? 499  GLU A OE1 1 
ATOM   3979  O  OE2 . GLU A  1 499 ? -16.878 1.645   13.437  1.00 3.79  ? 499  GLU A OE2 1 
ATOM   3980  N  N   . PRO A  1 500 ? -16.818 -5.094  12.478  1.00 2.55  ? 500  PRO A N   1 
ATOM   3981  C  CA  . PRO A  1 500 ? -17.082 -6.276  11.642  1.00 2.00  ? 500  PRO A CA  1 
ATOM   3982  C  C   . PRO A  1 500 ? -17.389 -5.917  10.190  1.00 2.61  ? 500  PRO A C   1 
ATOM   3983  O  O   . PRO A  1 500 ? -18.097 -4.949  9.926   1.00 3.52  ? 500  PRO A O   1 
ATOM   3984  C  CB  . PRO A  1 500 ? -18.256 -6.948  12.352  1.00 2.00  ? 500  PRO A CB  1 
ATOM   3985  C  CG  . PRO A  1 500 ? -18.938 -5.814  13.040  1.00 2.00  ? 500  PRO A CG  1 
ATOM   3986  C  CD  . PRO A  1 500 ? -17.790 -5.017  13.583  1.00 2.00  ? 500  PRO A CD  1 
ATOM   3987  N  N   . MET A  1 501 ? -16.868 -6.714  9.259   1.00 3.71  ? 501  MET A N   1 
ATOM   3988  C  CA  . MET A  1 501 ? -17.020 -6.476  7.819   1.00 3.27  ? 501  MET A CA  1 
ATOM   3989  C  C   . MET A  1 501 ? -18.397 -6.288  7.208   1.00 2.27  ? 501  MET A C   1 
ATOM   3990  O  O   . MET A  1 501 ? -19.394 -6.855  7.647   1.00 2.00  ? 501  MET A O   1 
ATOM   3991  C  CB  . MET A  1 501 ? -16.280 -7.562  7.043   1.00 5.10  ? 501  MET A CB  1 
ATOM   3992  C  CG  . MET A  1 501 ? -14.774 -7.426  7.172   1.00 8.97  ? 501  MET A CG  1 
ATOM   3993  S  SD  . MET A  1 501 ? -13.871 -8.997  7.185   1.00 15.50 ? 501  MET A SD  1 
ATOM   3994  C  CE  . MET A  1 501 ? -12.621 -8.697  5.874   1.00 13.35 ? 501  MET A CE  1 
ATOM   3995  N  N   . VAL A  1 502 ? -18.422 -5.474  6.163   1.00 3.20  ? 502  VAL A N   1 
ATOM   3996  C  CA  . VAL A  1 502 ? -19.645 -5.178  5.443   1.00 5.01  ? 502  VAL A CA  1 
ATOM   3997  C  C   . VAL A  1 502 ? -19.935 -6.319  4.474   1.00 5.81  ? 502  VAL A C   1 
ATOM   3998  O  O   . VAL A  1 502 ? -19.097 -7.207  4.286   1.00 5.77  ? 502  VAL A O   1 
ATOM   3999  C  CB  . VAL A  1 502 ? -19.515 -3.845  4.662   1.00 2.00  ? 502  VAL A CB  1 
ATOM   4000  C  CG1 . VAL A  1 502 ? -19.128 -2.726  5.612   1.00 2.00  ? 502  VAL A CG1 1 
ATOM   4001  C  CG2 . VAL A  1 502 ? -18.488 -3.977  3.557   1.00 2.00  ? 502  VAL A CG2 1 
ATOM   4002  N  N   . GLU A  1 503 ? -21.121 -6.286  3.866   1.00 8.72  ? 503  GLU A N   1 
ATOM   4003  C  CA  . GLU A  1 503 ? -21.544 -7.317  2.918   1.00 10.66 ? 503  GLU A CA  1 
ATOM   4004  C  C   . GLU A  1 503 ? -20.600 -7.367  1.713   1.00 9.50  ? 503  GLU A C   1 
ATOM   4005  O  O   . GLU A  1 503 ? -20.148 -6.335  1.219   1.00 7.17  ? 503  GLU A O   1 
ATOM   4006  C  CB  . GLU A  1 503 ? -22.981 -7.049  2.447   1.00 14.66 ? 503  GLU A CB  1 
ATOM   4007  C  CG  . GLU A  1 503 ? -23.780 -8.308  2.078   1.00 20.69 ? 503  GLU A CG  1 
ATOM   4008  C  CD  . GLU A  1 503 ? -24.960 -8.021  1.137   1.00 24.69 ? 503  GLU A CD  1 
ATOM   4009  O  OE1 . GLU A  1 503 ? -25.725 -7.061  1.396   1.00 26.76 ? 503  GLU A OE1 1 
ATOM   4010  O  OE2 . GLU A  1 503 ? -25.126 -8.763  0.138   1.00 26.47 ? 503  GLU A OE2 1 
ATOM   4011  N  N   . ARG A  1 504 ? -20.285 -8.587  1.294   1.00 9.08  ? 504  ARG A N   1 
ATOM   4012  C  CA  . ARG A  1 504 ? -19.430 -8.874  0.167   1.00 9.13  ? 504  ARG A CA  1 
ATOM   4013  C  C   . ARG A  1 504 ? -18.195 -7.996  -0.032  1.00 8.37  ? 504  ARG A C   1 
ATOM   4014  O  O   . ARG A  1 504 ? -17.682 -7.870  -1.133  1.00 7.97  ? 504  ARG A O   1 
ATOM   4015  C  CB  . ARG A  1 504 ? -20.319 -8.854  -1.080  1.00 13.17 ? 504  ARG A CB  1 
ATOM   4016  C  CG  . ARG A  1 504 ? -21.000 -10.167 -1.390  1.00 23.19 ? 504  ARG A CG  1 
ATOM   4017  C  CD  . ARG A  1 504 ? -20.318 -10.736 -2.604  1.00 29.95 ? 504  ARG A CD  1 
ATOM   4018  N  NE  . ARG A  1 504 ? -21.156 -11.609 -3.399  1.00 37.48 ? 504  ARG A NE  1 
ATOM   4019  C  CZ  . ARG A  1 504 ? -21.276 -12.918 -3.167  1.00 41.73 ? 504  ARG A CZ  1 
ATOM   4020  N  NH1 . ARG A  1 504 ? -20.636 -13.489 -2.145  1.00 43.49 ? 504  ARG A NH1 1 
ATOM   4021  N  NH2 . ARG A  1 504 ? -22.031 -13.668 -3.967  1.00 44.87 ? 504  ARG A NH2 1 
ATOM   4022  N  N   . GLY A  1 505 ? -17.738 -7.386  1.063   1.00 6.65  ? 505  GLY A N   1 
ATOM   4023  C  CA  . GLY A  1 505 ? -16.554 -6.538  1.022   1.00 4.89  ? 505  GLY A CA  1 
ATOM   4024  C  C   . GLY A  1 505 ? -15.542 -6.989  2.062   1.00 4.92  ? 505  GLY A C   1 
ATOM   4025  O  O   . GLY A  1 505 ? -15.714 -8.044  2.668   1.00 5.99  ? 505  GLY A O   1 
ATOM   4026  N  N   . ARG A  1 506 ? -14.493 -6.211  2.297   1.00 3.81  ? 506  ARG A N   1 
ATOM   4027  C  CA  . ARG A  1 506 ? -13.510 -6.633  3.282   1.00 2.00  ? 506  ARG A CA  1 
ATOM   4028  C  C   . ARG A  1 506 ? -13.156 -5.601  4.330   1.00 2.00  ? 506  ARG A C   1 
ATOM   4029  O  O   . ARG A  1 506 ? -12.126 -5.721  4.991   1.00 2.00  ? 506  ARG A O   1 
ATOM   4030  C  CB  . ARG A  1 506 ? -12.245 -7.122  2.586   1.00 2.04  ? 506  ARG A CB  1 
ATOM   4031  C  CG  . ARG A  1 506 ? -12.447 -8.408  1.817   1.00 2.71  ? 506  ARG A CG  1 
ATOM   4032  C  CD  . ARG A  1 506 ? -13.077 -9.462  2.707   1.00 4.96  ? 506  ARG A CD  1 
ATOM   4033  N  NE  . ARG A  1 506 ? -12.829 -10.816 2.219   1.00 7.68  ? 506  ARG A NE  1 
ATOM   4034  C  CZ  . ARG A  1 506 ? -13.761 -11.637 1.741   1.00 7.87  ? 506  ARG A CZ  1 
ATOM   4035  N  NH1 . ARG A  1 506 ? -15.027 -11.257 1.680   1.00 8.21  ? 506  ARG A NH1 1 
ATOM   4036  N  NH2 . ARG A  1 506 ? -13.425 -12.848 1.320   1.00 9.30  ? 506  ARG A NH2 1 
ATOM   4037  N  N   . VAL A  1 507 ? -14.006 -4.590  4.489   1.00 2.00  ? 507  VAL A N   1 
ATOM   4038  C  CA  . VAL A  1 507 ? -13.772 -3.568  5.499   1.00 2.00  ? 507  VAL A CA  1 
ATOM   4039  C  C   . VAL A  1 507 ? -15.077 -3.161  6.174   1.00 2.00  ? 507  VAL A C   1 
ATOM   4040  O  O   . VAL A  1 507 ? -16.155 -3.344  5.620   1.00 2.00  ? 507  VAL A O   1 
ATOM   4041  C  CB  . VAL A  1 507 ? -13.113 -2.333  4.900   1.00 2.00  ? 507  VAL A CB  1 
ATOM   4042  C  CG1 . VAL A  1 507 ? -12.069 -2.760  3.895   1.00 2.00  ? 507  VAL A CG1 1 
ATOM   4043  C  CG2 . VAL A  1 507 ? -14.154 -1.436  4.270   1.00 2.00  ? 507  VAL A CG2 1 
ATOM   4044  N  N   . GLY A  1 508 ? -14.969 -2.605  7.374   1.00 2.00  ? 508  GLY A N   1 
ATOM   4045  C  CA  . GLY A  1 508 ? -16.149 -2.205  8.116   1.00 2.27  ? 508  GLY A CA  1 
ATOM   4046  C  C   . GLY A  1 508 ? -16.811 -0.949  7.598   1.00 2.50  ? 508  GLY A C   1 
ATOM   4047  O  O   . GLY A  1 508 ? -16.262 -0.284  6.715   1.00 2.13  ? 508  GLY A O   1 
ATOM   4048  N  N   . PRO A  1 509 ? -17.997 -0.592  8.132   1.00 2.54  ? 509  PRO A N   1 
ATOM   4049  C  CA  . PRO A  1 509 ? -18.701 0.608   7.687   1.00 2.00  ? 509  PRO A CA  1 
ATOM   4050  C  C   . PRO A  1 509 ? -17.841 1.870   7.721   1.00 2.00  ? 509  PRO A C   1 
ATOM   4051  O  O   . PRO A  1 509 ? -17.917 2.677   6.803   1.00 2.00  ? 509  PRO A O   1 
ATOM   4052  C  CB  . PRO A  1 509 ? -19.911 0.665   8.626   1.00 2.00  ? 509  PRO A CB  1 
ATOM   4053  C  CG  . PRO A  1 509 ? -19.465 -0.070  9.835   1.00 2.00  ? 509  PRO A CG  1 
ATOM   4054  C  CD  . PRO A  1 509 ? -18.732 -1.230  9.238   1.00 2.00  ? 509  PRO A CD  1 
ATOM   4055  N  N   . LEU A  1 510 ? -17.020 2.038   8.759   1.00 2.00  ? 510  LEU A N   1 
ATOM   4056  C  CA  . LEU A  1 510 ? -16.163 3.217   8.848   1.00 2.00  ? 510  LEU A CA  1 
ATOM   4057  C  C   . LEU A  1 510 ? -15.172 3.261   7.689   1.00 3.25  ? 510  LEU A C   1 
ATOM   4058  O  O   . LEU A  1 510 ? -15.275 4.130   6.827   1.00 4.02  ? 510  LEU A O   1 
ATOM   4059  C  CB  . LEU A  1 510 ? -15.387 3.247   10.161  1.00 2.50  ? 510  LEU A CB  1 
ATOM   4060  C  CG  . LEU A  1 510 ? -14.641 4.572   10.395  1.00 3.53  ? 510  LEU A CG  1 
ATOM   4061  C  CD1 . LEU A  1 510 ? -15.657 5.676   10.625  1.00 3.37  ? 510  LEU A CD1 1 
ATOM   4062  C  CD2 . LEU A  1 510 ? -13.709 4.478   11.597  1.00 3.45  ? 510  LEU A CD2 1 
ATOM   4063  N  N   . LEU A  1 511 ? -14.213 2.334   7.663   1.00 3.26  ? 511  LEU A N   1 
ATOM   4064  C  CA  . LEU A  1 511 ? -13.220 2.296   6.583   1.00 2.00  ? 511  LEU A CA  1 
ATOM   4065  C  C   . LEU A  1 511 ? -13.877 2.392   5.220   1.00 2.00  ? 511  LEU A C   1 
ATOM   4066  O  O   . LEU A  1 511 ? -13.367 3.055   4.325   1.00 2.00  ? 511  LEU A O   1 
ATOM   4067  C  CB  . LEU A  1 511 ? -12.382 1.011   6.630   1.00 2.00  ? 511  LEU A CB  1 
ATOM   4068  C  CG  . LEU A  1 511 ? -11.168 0.938   7.568   1.00 2.00  ? 511  LEU A CG  1 
ATOM   4069  C  CD1 . LEU A  1 511 ? -10.334 2.200   7.408   1.00 2.00  ? 511  LEU A CD1 1 
ATOM   4070  C  CD2 . LEU A  1 511 ? -11.612 0.780   9.012   1.00 2.00  ? 511  LEU A CD2 1 
ATOM   4071  N  N   . ALA A  1 512 ? -15.008 1.720   5.062   1.00 2.00  ? 512  ALA A N   1 
ATOM   4072  C  CA  . ALA A  1 512 ? -15.717 1.751   3.796   1.00 2.00  ? 512  ALA A CA  1 
ATOM   4073  C  C   . ALA A  1 512 ? -15.895 3.200   3.364   1.00 2.02  ? 512  ALA A C   1 
ATOM   4074  O  O   . ALA A  1 512 ? -15.712 3.544   2.198   1.00 2.58  ? 512  ALA A O   1 
ATOM   4075  C  CB  . ALA A  1 512 ? -17.070 1.073   3.937   1.00 2.00  ? 512  ALA A CB  1 
ATOM   4076  N  N   . CYS A  1 513 ? -16.245 4.047   4.320   1.00 2.00  ? 513  CYS A N   1 
ATOM   4077  C  CA  . CYS A  1 513 ? -16.453 5.461   4.060   1.00 2.00  ? 513  CYS A CA  1 
ATOM   4078  C  C   . CYS A  1 513 ? -15.164 6.128   3.601   1.00 2.00  ? 513  CYS A C   1 
ATOM   4079  O  O   . CYS A  1 513 ? -15.049 6.531   2.443   1.00 2.00  ? 513  CYS A O   1 
ATOM   4080  C  CB  . CYS A  1 513 ? -16.976 6.125   5.332   1.00 2.00  ? 513  CYS A CB  1 
ATOM   4081  S  SG  . CYS A  1 513 ? -16.807 7.932   5.462   1.00 2.00  ? 513  CYS A SG  1 
ATOM   4082  N  N   . LEU A  1 514 ? -14.207 6.224   4.525   1.00 3.57  ? 514  LEU A N   1 
ATOM   4083  C  CA  . LEU A  1 514 ? -12.892 6.830   4.306   1.00 2.00  ? 514  LEU A CA  1 
ATOM   4084  C  C   . LEU A  1 514 ? -12.293 6.432   2.970   1.00 2.00  ? 514  LEU A C   1 
ATOM   4085  O  O   . LEU A  1 514 ? -11.921 7.279   2.159   1.00 2.00  ? 514  LEU A O   1 
ATOM   4086  C  CB  . LEU A  1 514 ? -11.954 6.431   5.426   1.00 2.00  ? 514  LEU A CB  1 
ATOM   4087  C  CG  . LEU A  1 514 ? -12.483 6.677   6.830   1.00 2.00  ? 514  LEU A CG  1 
ATOM   4088  C  CD1 . LEU A  1 514 ? -11.818 5.742   7.818   1.00 2.00  ? 514  LEU A CD1 1 
ATOM   4089  C  CD2 . LEU A  1 514 ? -12.267 8.121   7.253   1.00 2.00  ? 514  LEU A CD2 1 
ATOM   4090  N  N   . LEU A  1 515 ? -12.218 5.131   2.753   1.00 2.00  ? 515  LEU A N   1 
ATOM   4091  C  CA  . LEU A  1 515 ? -11.647 4.601   1.508   1.00 2.00  ? 515  LEU A CA  1 
ATOM   4092  C  C   . LEU A  1 515 ? -12.489 4.854   0.302   1.00 2.00  ? 515  LEU A C   1 
ATOM   4093  O  O   . LEU A  1 515 ? -11.966 4.967   -0.809  1.00 2.18  ? 515  LEU A O   1 
ATOM   4094  C  CB  . LEU A  1 515 ? -11.562 3.106   1.503   1.00 2.67  ? 515  LEU A CB  1 
ATOM   4095  C  CG  . LEU A  1 515 ? -10.696 2.477   2.563   1.00 2.00  ? 515  LEU A CG  1 
ATOM   4096  C  CD1 . LEU A  1 515 ? -10.542 0.975   2.323   1.00 2.00  ? 515  LEU A CD1 1 
ATOM   4097  C  CD2 . LEU A  1 515 ? -9.328  3.131   2.595   1.00 2.00  ? 515  LEU A CD2 1 
ATOM   4098  N  N   . GLY A  1 516 ? -13.779 4.916   0.456   1.00 2.00  ? 516  GLY A N   1 
ATOM   4099  C  CA  . GLY A  1 516 ? -14.635 5.140   -0.684  1.00 2.20  ? 516  GLY A CA  1 
ATOM   4100  C  C   . GLY A  1 516 ? -14.474 6.581   -1.145  1.00 2.00  ? 516  GLY A C   1 
ATOM   4101  O  O   . GLY A  1 516 ? -14.304 6.857   -2.344  1.00 2.11  ? 516  GLY A O   1 
ATOM   4102  N  N   . ARG A  1 517 ? -14.550 7.465   -0.191  1.00 2.00  ? 517  ARG A N   1 
ATOM   4103  C  CA  . ARG A  1 517 ? -14.430 8.885   -0.472  1.00 3.16  ? 517  ARG A CA  1 
ATOM   4104  C  C   . ARG A  1 517 ? -13.111 9.227   -1.141  1.00 2.69  ? 517  ARG A C   1 
ATOM   4105  O  O   . ARG A  1 517 ? -13.091 9.934   -2.147  1.00 3.48  ? 517  ARG A O   1 
ATOM   4106  C  CB  . ARG A  1 517 ? -14.551 9.710   0.809   1.00 6.91  ? 517  ARG A CB  1 
ATOM   4107  C  CG  . ARG A  1 517 ? -15.925 9.670   1.474   1.00 11.12 ? 517  ARG A CG  1 
ATOM   4108  C  CD  . ARG A  1 517 ? -16.148 10.918  2.321   1.00 12.41 ? 517  ARG A CD  1 
ATOM   4109  N  NE  . ARG A  1 517 ? -17.401 10.867  3.068   1.00 15.90 ? 517  ARG A NE  1 
ATOM   4110  C  CZ  . ARG A  1 517 ? -17.911 11.901  3.731   1.00 16.86 ? 517  ARG A CZ  1 
ATOM   4111  N  NH1 . ARG A  1 517 ? -17.271 13.064  3.731   1.00 18.42 ? 517  ARG A NH1 1 
ATOM   4112  N  NH2 . ARG A  1 517 ? -19.055 11.776  4.397   1.00 17.48 ? 517  ARG A NH2 1 
ATOM   4113  N  N   . GLN A  1 518 ? -12.011 8.731   -0.578  1.00 3.21  ? 518  GLN A N   1 
ATOM   4114  C  CA  . GLN A  1 518 ? -10.681 9.012   -1.119  1.00 2.10  ? 518  GLN A CA  1 
ATOM   4115  C  C   . GLN A  1 518 ? -10.530 8.572   -2.555  1.00 2.00  ? 518  GLN A C   1 
ATOM   4116  O  O   . GLN A  1 518 ? -10.123 9.348   -3.410  1.00 2.00  ? 518  GLN A O   1 
ATOM   4117  C  CB  . GLN A  1 518 ? -9.592  8.328   -0.291  1.00 2.16  ? 518  GLN A CB  1 
ATOM   4118  C  CG  . GLN A  1 518 ? -8.180  8.699   -0.715  1.00 2.00  ? 518  GLN A CG  1 
ATOM   4119  C  CD  . GLN A  1 518 ? -7.829  10.131  -0.377  1.00 2.00  ? 518  GLN A CD  1 
ATOM   4120  O  OE1 . GLN A  1 518 ? -7.241  10.409  0.662   1.00 2.00  ? 518  GLN A OE1 1 
ATOM   4121  N  NE2 . GLN A  1 518 ? -8.203  11.051  -1.251  1.00 2.48  ? 518  GLN A NE2 1 
ATOM   4122  N  N   . PHE A  1 519 ? -10.862 7.321   -2.823  1.00 2.00  ? 519  PHE A N   1 
ATOM   4123  C  CA  . PHE A  1 519 ? -10.712 6.815   -4.167  1.00 2.00  ? 519  PHE A CA  1 
ATOM   4124  C  C   . PHE A  1 519 ? -11.539 7.524   -5.206  1.00 2.00  ? 519  PHE A C   1 
ATOM   4125  O  O   . PHE A  1 519 ? -11.052 7.822   -6.297  1.00 2.67  ? 519  PHE A O   1 
ATOM   4126  C  CB  . PHE A  1 519 ? -10.988 5.326   -4.190  1.00 2.58  ? 519  PHE A CB  1 
ATOM   4127  C  CG  . PHE A  1 519 ? -9.791  4.510   -3.838  1.00 2.61  ? 519  PHE A CG  1 
ATOM   4128  C  CD1 . PHE A  1 519 ? -8.668  4.538   -4.652  1.00 2.00  ? 519  PHE A CD1 1 
ATOM   4129  C  CD2 . PHE A  1 519 ? -9.772  3.737   -2.683  1.00 2.22  ? 519  PHE A CD2 1 
ATOM   4130  C  CE1 . PHE A  1 519 ? -7.543  3.810   -4.326  1.00 2.00  ? 519  PHE A CE1 1 
ATOM   4131  C  CE2 . PHE A  1 519 ? -8.650  3.005   -2.348  1.00 3.27  ? 519  PHE A CE2 1 
ATOM   4132  C  CZ  . PHE A  1 519 ? -7.527  3.040   -3.174  1.00 2.50  ? 519  PHE A CZ  1 
ATOM   4133  N  N   . GLN A  1 520 ? -12.793 7.792   -4.881  1.00 2.73  ? 520  GLN A N   1 
ATOM   4134  C  CA  . GLN A  1 520 ? -13.651 8.497   -5.817  1.00 3.69  ? 520  GLN A CA  1 
ATOM   4135  C  C   . GLN A  1 520 ? -12.952 9.794   -6.220  1.00 4.20  ? 520  GLN A C   1 
ATOM   4136  O  O   . GLN A  1 520 ? -12.841 10.125  -7.403  1.00 5.07  ? 520  GLN A O   1 
ATOM   4137  C  CB  . GLN A  1 520 ? -14.982 8.815   -5.150  1.00 3.79  ? 520  GLN A CB  1 
ATOM   4138  C  CG  . GLN A  1 520 ? -15.469 10.210  -5.408  1.00 4.96  ? 520  GLN A CG  1 
ATOM   4139  C  CD  . GLN A  1 520 ? -16.440 10.656  -4.354  1.00 7.91  ? 520  GLN A CD  1 
ATOM   4140  O  OE1 . GLN A  1 520 ? -16.775 11.833  -4.268  1.00 10.37 ? 520  GLN A OE1 1 
ATOM   4141  N  NE2 . GLN A  1 520 ? -16.904 9.714   -3.533  1.00 8.27  ? 520  GLN A NE2 1 
ATOM   4142  N  N   . GLN A  1 521 ? -12.458 10.504  -5.214  1.00 3.49  ? 521  GLN A N   1 
ATOM   4143  C  CA  . GLN A  1 521 ? -11.774 11.777  -5.395  1.00 2.83  ? 521  GLN A CA  1 
ATOM   4144  C  C   . GLN A  1 521 ? -10.557 11.849  -6.311  1.00 2.55  ? 521  GLN A C   1 
ATOM   4145  O  O   . GLN A  1 521 ? -10.450 12.784  -7.099  1.00 2.44  ? 521  GLN A O   1 
ATOM   4146  C  CB  . GLN A  1 521 ? -11.376 12.321  -4.040  1.00 4.06  ? 521  GLN A CB  1 
ATOM   4147  C  CG  . GLN A  1 521 ? -11.939 13.669  -3.777  1.00 7.35  ? 521  GLN A CG  1 
ATOM   4148  C  CD  . GLN A  1 521 ? -11.942 13.983  -2.312  1.00 9.56  ? 521  GLN A CD  1 
ATOM   4149  O  OE1 . GLN A  1 521 ? -10.912 14.356  -1.741  1.00 12.36 ? 521  GLN A OE1 1 
ATOM   4150  N  NE2 . GLN A  1 521 ? -13.100 13.813  -1.676  1.00 9.85  ? 521  GLN A NE2 1 
ATOM   4151  N  N   . ILE A  1 522 ? -9.629  10.896  -6.192  1.00 3.27  ? 522  ILE A N   1 
ATOM   4152  C  CA  . ILE A  1 522 ? -8.422  10.896  -7.028  1.00 2.40  ? 522  ILE A CA  1 
ATOM   4153  C  C   . ILE A  1 522 ? -8.787  10.485  -8.452  1.00 2.00  ? 522  ILE A C   1 
ATOM   4154  O  O   . ILE A  1 522 ? -7.986  10.598  -9.384  1.00 2.00  ? 522  ILE A O   1 
ATOM   4155  C  CB  . ILE A  1 522 ? -7.326  9.938   -6.468  1.00 2.00  ? 522  ILE A CB  1 
ATOM   4156  C  CG1 . ILE A  1 522 ? -7.698  8.480   -6.714  1.00 2.33  ? 522  ILE A CG1 1 
ATOM   4157  C  CG2 . ILE A  1 522 ? -7.161  10.142  -4.975  1.00 2.99  ? 522  ILE A CG2 1 
ATOM   4158  C  CD1 . ILE A  1 522 ? -6.745  7.778   -7.659  1.00 3.60  ? 522  ILE A CD1 1 
ATOM   4159  N  N   . ARG A  1 523 ? -10.020 10.019  -8.600  1.00 2.16  ? 523  ARG A N   1 
ATOM   4160  C  CA  . ARG A  1 523 ? -10.539 9.599   -9.880  1.00 2.88  ? 523  ARG A CA  1 
ATOM   4161  C  C   . ARG A  1 523 ? -11.356 10.723  -10.519 1.00 4.27  ? 523  ARG A C   1 
ATOM   4162  O  O   . ARG A  1 523 ? -11.356 10.873  -11.736 1.00 7.40  ? 523  ARG A O   1 
ATOM   4163  C  CB  . ARG A  1 523 ? -11.391 8.346   -9.694  1.00 2.00  ? 523  ARG A CB  1 
ATOM   4164  C  CG  . ARG A  1 523 ? -12.275 7.982   -10.882 1.00 2.07  ? 523  ARG A CG  1 
ATOM   4165  C  CD  . ARG A  1 523 ? -13.699 8.496   -10.680 1.00 2.87  ? 523  ARG A CD  1 
ATOM   4166  N  NE  . ARG A  1 523 ? -14.700 7.482   -11.001 1.00 2.00  ? 523  ARG A NE  1 
ATOM   4167  C  CZ  . ARG A  1 523 ? -15.968 7.527   -10.606 1.00 2.00  ? 523  ARG A CZ  1 
ATOM   4168  N  NH1 . ARG A  1 523 ? -16.414 8.540   -9.868  1.00 2.00  ? 523  ARG A NH1 1 
ATOM   4169  N  NH2 . ARG A  1 523 ? -16.788 6.543   -10.940 1.00 2.00  ? 523  ARG A NH2 1 
ATOM   4170  N  N   . ASP A  1 524 ? -12.047 11.525  -9.716  1.00 3.48  ? 524  ASP A N   1 
ATOM   4171  C  CA  . ASP A  1 524 ? -12.836 12.607  -10.293 1.00 2.00  ? 524  ASP A CA  1 
ATOM   4172  C  C   . ASP A  1 524 ? -12.059 13.908  -10.475 1.00 2.00  ? 524  ASP A C   1 
ATOM   4173  O  O   . ASP A  1 524 ? -12.514 14.813  -11.173 1.00 2.00  ? 524  ASP A O   1 
ATOM   4174  C  CB  . ASP A  1 524 ? -14.092 12.867  -9.453  1.00 2.00  ? 524  ASP A CB  1 
ATOM   4175  C  CG  . ASP A  1 524 ? -15.118 11.758  -9.589  1.00 2.00  ? 524  ASP A CG  1 
ATOM   4176  O  OD1 . ASP A  1 524 ? -15.092 11.087  -10.630 1.00 2.22  ? 524  ASP A OD1 1 
ATOM   4177  O  OD2 . ASP A  1 524 ? -15.956 11.556  -8.682  1.00 2.00  ? 524  ASP A OD2 1 
ATOM   4178  N  N   . GLY A  1 525 ? -10.884 14.001  -9.864  1.00 2.00  ? 525  GLY A N   1 
ATOM   4179  C  CA  . GLY A  1 525 ? -10.104 15.221  -9.978  1.00 2.00  ? 525  GLY A CA  1 
ATOM   4180  C  C   . GLY A  1 525 ? -8.835  15.082  -10.796 1.00 2.68  ? 525  GLY A C   1 
ATOM   4181  O  O   . GLY A  1 525 ? -8.063  16.039  -10.932 1.00 2.63  ? 525  GLY A O   1 
ATOM   4182  N  N   . ASP A  1 526 ? -8.622  13.894  -11.351 1.00 2.92  ? 526  ASP A N   1 
ATOM   4183  C  CA  . ASP A  1 526 ? -7.432  13.630  -12.146 1.00 2.41  ? 526  ASP A CA  1 
ATOM   4184  C  C   . ASP A  1 526 ? -7.725  13.897  -13.607 1.00 2.00  ? 526  ASP A C   1 
ATOM   4185  O  O   . ASP A  1 526 ? -8.364  13.092  -14.273 1.00 2.00  ? 526  ASP A O   1 
ATOM   4186  C  CB  . ASP A  1 526 ? -6.986  12.181  -11.940 1.00 3.69  ? 526  ASP A CB  1 
ATOM   4187  C  CG  . ASP A  1 526 ? -5.823  11.804  -12.820 1.00 4.94  ? 526  ASP A CG  1 
ATOM   4188  O  OD1 . ASP A  1 526 ? -4.847  12.577  -12.872 1.00 7.27  ? 526  ASP A OD1 1 
ATOM   4189  O  OD2 . ASP A  1 526 ? -5.882  10.735  -13.458 1.00 5.49  ? 526  ASP A OD2 1 
ATOM   4190  N  N   . ARG A  1 527 ? -7.247  15.034  -14.097 1.00 2.00  ? 527  ARG A N   1 
ATOM   4191  C  CA  . ARG A  1 527 ? -7.477  15.445  -15.483 1.00 3.24  ? 527  ARG A CA  1 
ATOM   4192  C  C   . ARG A  1 527 ? -7.110  14.382  -16.493 1.00 2.09  ? 527  ARG A C   1 
ATOM   4193  O  O   . ARG A  1 527 ? -7.598  14.405  -17.625 1.00 2.00  ? 527  ARG A O   1 
ATOM   4194  C  CB  . ARG A  1 527 ? -6.695  16.728  -15.802 1.00 2.98  ? 527  ARG A CB  1 
ATOM   4195  C  CG  . ARG A  1 527 ? -6.904  17.269  -17.211 1.00 2.00  ? 527  ARG A CG  1 
ATOM   4196  C  CD  . ARG A  1 527 ? -6.432  18.710  -17.289 1.00 2.00  ? 527  ARG A CD  1 
ATOM   4197  N  NE  . ARG A  1 527 ? -4.980  18.818  -17.213 1.00 2.00  ? 527  ARG A NE  1 
ATOM   4198  C  CZ  . ARG A  1 527 ? -4.179  18.723  -18.267 1.00 2.00  ? 527  ARG A CZ  1 
ATOM   4199  N  NH1 . ARG A  1 527 ? -4.697  18.523  -19.467 1.00 2.00  ? 527  ARG A NH1 1 
ATOM   4200  N  NH2 . ARG A  1 527 ? -2.864  18.822  -18.127 1.00 2.00  ? 527  ARG A NH2 1 
ATOM   4201  N  N   . PHE A  1 528 ? -6.255  13.449  -16.082 1.00 2.19  ? 528  PHE A N   1 
ATOM   4202  C  CA  . PHE A  1 528 ? -5.809  12.389  -16.981 1.00 3.68  ? 528  PHE A CA  1 
ATOM   4203  C  C   . PHE A  1 528 ? -6.463  11.027  -16.794 1.00 2.82  ? 528  PHE A C   1 
ATOM   4204  O  O   . PHE A  1 528 ? -6.079  10.065  -17.467 1.00 2.00  ? 528  PHE A O   1 
ATOM   4205  C  CB  . PHE A  1 528 ? -4.288  12.227  -16.908 1.00 2.85  ? 528  PHE A CB  1 
ATOM   4206  C  CG  . PHE A  1 528 ? -3.528  13.361  -17.533 1.00 2.00  ? 528  PHE A CG  1 
ATOM   4207  C  CD1 . PHE A  1 528 ? -3.210  14.492  -16.797 1.00 3.37  ? 528  PHE A CD1 1 
ATOM   4208  C  CD2 . PHE A  1 528 ? -3.141  13.301  -18.864 1.00 2.00  ? 528  PHE A CD2 1 
ATOM   4209  C  CE1 . PHE A  1 528 ? -2.515  15.547  -17.381 1.00 4.17  ? 528  PHE A CE1 1 
ATOM   4210  C  CE2 . PHE A  1 528 ? -2.448  14.349  -19.456 1.00 2.59  ? 528  PHE A CE2 1 
ATOM   4211  C  CZ  . PHE A  1 528 ? -2.133  15.473  -18.716 1.00 3.55  ? 528  PHE A CZ  1 
ATOM   4212  N  N   . TRP A  1 529 ? -7.435  10.936  -15.887 1.00 2.28  ? 529  TRP A N   1 
ATOM   4213  C  CA  . TRP A  1 529 ? -8.137  9.674   -15.682 1.00 2.50  ? 529  TRP A CA  1 
ATOM   4214  C  C   . TRP A  1 529 ? -8.483  9.193   -17.094 1.00 2.78  ? 529  TRP A C   1 
ATOM   4215  O  O   . TRP A  1 529 ? -8.874  9.990   -17.939 1.00 3.79  ? 529  TRP A O   1 
ATOM   4216  C  CB  . TRP A  1 529 ? -9.399  9.897   -14.850 1.00 2.00  ? 529  TRP A CB  1 
ATOM   4217  C  CG  . TRP A  1 529 ? -10.129 8.638   -14.569 1.00 2.00  ? 529  TRP A CG  1 
ATOM   4218  C  CD1 . TRP A  1 529 ? -11.182 8.131   -15.267 1.00 2.93  ? 529  TRP A CD1 1 
ATOM   4219  C  CD2 . TRP A  1 529 ? -9.812  7.670   -13.563 1.00 2.00  ? 529  TRP A CD2 1 
ATOM   4220  N  NE1 . TRP A  1 529 ? -11.544 6.904   -14.764 1.00 3.24  ? 529  TRP A NE1 1 
ATOM   4221  C  CE2 . TRP A  1 529 ? -10.717 6.597   -13.715 1.00 2.17  ? 529  TRP A CE2 1 
ATOM   4222  C  CE3 . TRP A  1 529 ? -8.850  7.603   -12.548 1.00 2.11  ? 529  TRP A CE3 1 
ATOM   4223  C  CZ2 . TRP A  1 529 ? -10.688 5.468   -12.890 1.00 2.00  ? 529  TRP A CZ2 1 
ATOM   4224  C  CZ3 . TRP A  1 529 ? -8.823  6.477   -11.727 1.00 2.00  ? 529  TRP A CZ3 1 
ATOM   4225  C  CH2 . TRP A  1 529 ? -9.736  5.429   -11.905 1.00 2.00  ? 529  TRP A CH2 1 
ATOM   4226  N  N   . TRP A  1 530 ? -8.364  7.903   -17.363 1.00 3.29  ? 530  TRP A N   1 
ATOM   4227  C  CA  . TRP A  1 530 ? -8.581  7.392   -18.742 1.00 4.42  ? 530  TRP A CA  1 
ATOM   4228  C  C   . TRP A  1 530 ? -9.988  7.554   -19.311 1.00 3.47  ? 530  TRP A C   1 
ATOM   4229  O  O   . TRP A  1 530 ? -10.124 7.948   -20.475 1.00 2.90  ? 530  TRP A O   1 
ATOM   4230  C  CB  . TRP A  1 530 ? -8.137  5.922   -18.788 1.00 3.51  ? 530  TRP A CB  1 
ATOM   4231  C  CG  . TRP A  1 530 ? -9.055  5.032   -18.011 1.00 2.37  ? 530  TRP A CG  1 
ATOM   4232  C  CD1 . TRP A  1 530 ? -9.142  4.942   -16.658 1.00 2.86  ? 530  TRP A CD1 1 
ATOM   4233  C  CD2 . TRP A  1 530 ? -10.024 4.130   -18.540 1.00 2.30  ? 530  TRP A CD2 1 
ATOM   4234  N  NE1 . TRP A  1 530 ? -10.113 4.034   -16.306 1.00 2.79  ? 530  TRP A NE1 1 
ATOM   4235  C  CE2 . TRP A  1 530 ? -10.671 3.523   -17.446 1.00 2.00  ? 530  TRP A CE2 1 
ATOM   4236  C  CE3 . TRP A  1 530 ? -10.413 3.778   -19.836 1.00 2.20  ? 530  TRP A CE3 1 
ATOM   4237  C  CZ2 . TRP A  1 530 ? -11.683 2.583   -17.604 1.00 2.00  ? 530  TRP A CZ2 1 
ATOM   4238  C  CZ3 . TRP A  1 530 ? -11.421 2.842   -19.994 1.00 2.71  ? 530  TRP A CZ3 1 
ATOM   4239  C  CH2 . TRP A  1 530 ? -12.046 2.255   -18.882 1.00 2.29  ? 530  TRP A CH2 1 
ATOM   4240  N  N   . GLU A  1 531 ? -11.028 7.242   -18.543 1.00 4.04  ? 531  GLU A N   1 
ATOM   4241  C  CA  . GLU A  1 531 ? -12.361 7.331   -19.118 1.00 4.87  ? 531  GLU A CA  1 
ATOM   4242  C  C   . GLU A  1 531 ? -12.643 8.734   -19.621 1.00 4.64  ? 531  GLU A C   1 
ATOM   4243  O  O   . GLU A  1 531 ? -13.549 8.941   -20.447 1.00 5.89  ? 531  GLU A O   1 
ATOM   4244  C  CB  . GLU A  1 531 ? -13.395 6.825   -18.128 1.00 5.81  ? 531  GLU A CB  1 
ATOM   4245  C  CG  . GLU A  1 531 ? -13.744 5.355   -18.302 1.00 8.42  ? 531  GLU A CG  1 
ATOM   4246  C  CD  . GLU A  1 531 ? -14.711 4.861   -17.259 1.00 12.02 ? 531  GLU A CD  1 
ATOM   4247  O  OE1 . GLU A  1 531 ? -14.504 5.164   -16.064 1.00 13.51 ? 531  GLU A OE1 1 
ATOM   4248  O  OE2 . GLU A  1 531 ? -15.697 4.177   -17.620 1.00 13.97 ? 531  GLU A OE2 1 
ATOM   4249  N  N   . ASN A  1 532 ? -11.865 9.685   -19.125 1.00 4.12  ? 532  ASN A N   1 
ATOM   4250  C  CA  . ASN A  1 532 ? -12.012 11.088  -19.488 1.00 3.62  ? 532  ASN A CA  1 
ATOM   4251  C  C   . ASN A  1 532 ? -11.752 11.324  -20.947 1.00 4.08  ? 532  ASN A C   1 
ATOM   4252  O  O   . ASN A  1 532 ? -10.764 10.799  -21.490 1.00 4.73  ? 532  ASN A O   1 
ATOM   4253  C  CB  . ASN A  1 532 ? -11.051 11.917  -18.656 1.00 4.46  ? 532  ASN A CB  1 
ATOM   4254  C  CG  . ASN A  1 532 ? -11.320 13.376  -18.769 1.00 6.15  ? 532  ASN A CG  1 
ATOM   4255  O  OD1 . ASN A  1 532 ? -12.454 13.820  -18.580 1.00 8.22  ? 532  ASN A OD1 1 
ATOM   4256  N  ND2 . ASN A  1 532 ? -10.283 14.148  -19.074 1.00 7.24  ? 532  ASN A ND2 1 
ATOM   4257  N  N   . PRO A  1 533 ? -12.581 12.109  -21.636 1.00 3.93  ? 533  PRO A N   1 
ATOM   4258  C  CA  . PRO A  1 533 ? -12.395 12.349  -23.070 1.00 4.35  ? 533  PRO A CA  1 
ATOM   4259  C  C   . PRO A  1 533 ? -11.149 13.172  -23.368 1.00 6.24  ? 533  PRO A C   1 
ATOM   4260  O  O   . PRO A  1 533 ? -10.802 14.080  -22.616 1.00 7.84  ? 533  PRO A O   1 
ATOM   4261  C  CB  . PRO A  1 533 ? -13.680 13.063  -23.462 1.00 3.27  ? 533  PRO A CB  1 
ATOM   4262  C  CG  . PRO A  1 533 ? -14.684 12.506  -22.468 1.00 2.94  ? 533  PRO A CG  1 
ATOM   4263  C  CD  . PRO A  1 533 ? -13.903 12.580  -21.194 1.00 2.74  ? 533  PRO A CD  1 
ATOM   4264  N  N   . GLY A  1 534 ? -10.477 12.853  -24.469 1.00 7.19  ? 534  GLY A N   1 
ATOM   4265  C  CA  . GLY A  1 534 ? -9.273  13.579  -24.828 1.00 8.66  ? 534  GLY A CA  1 
ATOM   4266  C  C   . GLY A  1 534 ? -8.043  12.780  -24.443 1.00 10.60 ? 534  GLY A C   1 
ATOM   4267  O  O   . GLY A  1 534 ? -7.087  12.676  -25.223 1.00 12.90 ? 534  GLY A O   1 
ATOM   4268  N  N   . VAL A  1 535 ? -8.074  12.199  -23.246 1.00 8.53  ? 535  VAL A N   1 
ATOM   4269  C  CA  . VAL A  1 535 ? -6.962  11.406  -22.742 1.00 7.74  ? 535  VAL A CA  1 
ATOM   4270  C  C   . VAL A  1 535 ? -6.612  10.232  -23.660 1.00 7.13  ? 535  VAL A C   1 
ATOM   4271  O  O   . VAL A  1 535 ? -5.455  10.074  -24.052 1.00 6.66  ? 535  VAL A O   1 
ATOM   4272  C  CB  . VAL A  1 535 ? -7.280  10.912  -21.326 1.00 8.76  ? 535  VAL A CB  1 
ATOM   4273  C  CG1 . VAL A  1 535 ? -6.247  9.904   -20.868 1.00 10.66 ? 535  VAL A CG1 1 
ATOM   4274  C  CG2 . VAL A  1 535 ? -7.289  12.095  -20.376 1.00 8.48  ? 535  VAL A CG2 1 
ATOM   4275  N  N   . PHE A  1 536 ? -7.601  9.403   -23.979 1.00 6.21  ? 536  PHE A N   1 
ATOM   4276  C  CA  . PHE A  1 536 ? -7.410  8.269   -24.891 1.00 6.60  ? 536  PHE A CA  1 
ATOM   4277  C  C   . PHE A  1 536 ? -8.569  8.333   -25.870 1.00 7.54  ? 536  PHE A C   1 
ATOM   4278  O  O   . PHE A  1 536 ? -9.623  8.874   -25.535 1.00 9.05  ? 536  PHE A O   1 
ATOM   4279  C  CB  . PHE A  1 536 ? -7.457  6.921   -24.161 1.00 5.79  ? 536  PHE A CB  1 
ATOM   4280  C  CG  . PHE A  1 536 ? -6.173  6.546   -23.474 1.00 4.74  ? 536  PHE A CG  1 
ATOM   4281  C  CD1 . PHE A  1 536 ? -6.037  6.678   -22.099 1.00 3.22  ? 536  PHE A CD1 1 
ATOM   4282  C  CD2 . PHE A  1 536 ? -5.094  6.073   -24.207 1.00 5.41  ? 536  PHE A CD2 1 
ATOM   4283  C  CE1 . PHE A  1 536 ? -4.846  6.347   -21.466 1.00 3.23  ? 536  PHE A CE1 1 
ATOM   4284  C  CE2 . PHE A  1 536 ? -3.896  5.741   -23.578 1.00 5.59  ? 536  PHE A CE2 1 
ATOM   4285  C  CZ  . PHE A  1 536 ? -3.776  5.880   -22.206 1.00 3.40  ? 536  PHE A CZ  1 
ATOM   4286  N  N   . THR A  1 537 ? -8.393  7.778   -27.066 1.00 6.65  ? 537  THR A N   1 
ATOM   4287  C  CA  . THR A  1 537 ? -9.453  7.811   -28.076 1.00 6.35  ? 537  THR A CA  1 
ATOM   4288  C  C   . THR A  1 537 ? -10.561 6.780   -27.834 1.00 8.99  ? 537  THR A C   1 
ATOM   4289  O  O   . THR A  1 537 ? -10.389 5.847   -27.046 1.00 9.60  ? 537  THR A O   1 
ATOM   4290  C  CB  . THR A  1 537 ? -8.898  7.542   -29.445 1.00 5.36  ? 537  THR A CB  1 
ATOM   4291  O  OG1 . THR A  1 537 ? -8.727  6.129   -29.599 1.00 7.70  ? 537  THR A OG1 1 
ATOM   4292  C  CG2 . THR A  1 537 ? -7.563  8.227   -29.609 1.00 4.55  ? 537  THR A CG2 1 
ATOM   4293  N  N   . GLU A  1 538 ? -11.688 6.955   -28.531 1.00 10.48 ? 538  GLU A N   1 
ATOM   4294  C  CA  . GLU A  1 538 ? -12.846 6.064   -28.410 1.00 11.34 ? 538  GLU A CA  1 
ATOM   4295  C  C   . GLU A  1 538 ? -12.368 4.648   -28.647 1.00 11.21 ? 538  GLU A C   1 
ATOM   4296  O  O   . GLU A  1 538 ? -12.678 3.732   -27.880 1.00 10.31 ? 538  GLU A O   1 
ATOM   4297  C  CB  . GLU A  1 538 ? -13.931 6.411   -29.453 1.00 14.52 ? 538  GLU A CB  1 
ATOM   4298  C  CG  . GLU A  1 538 ? -15.344 5.852   -29.137 1.00 19.36 ? 538  GLU A CG  1 
ATOM   4299  C  CD  . GLU A  1 538 ? -15.993 5.070   -30.296 1.00 21.66 ? 538  GLU A CD  1 
ATOM   4300  O  OE1 . GLU A  1 538 ? -16.309 3.875   -30.095 1.00 22.75 ? 538  GLU A OE1 1 
ATOM   4301  O  OE2 . GLU A  1 538 ? -16.198 5.639   -31.395 1.00 22.38 ? 538  GLU A OE2 1 
ATOM   4302  N  N   . LYS A  1 539 ? -11.608 4.468   -29.720 1.00 10.65 ? 539  LYS A N   1 
ATOM   4303  C  CA  . LYS A  1 539 ? -11.096 3.146   -30.035 1.00 11.79 ? 539  LYS A CA  1 
ATOM   4304  C  C   . LYS A  1 539 ? -10.064 2.715   -28.996 1.00 10.77 ? 539  LYS A C   1 
ATOM   4305  O  O   . LYS A  1 539 ? -10.162 1.615   -28.445 1.00 10.93 ? 539  LYS A O   1 
ATOM   4306  C  CB  . LYS A  1 539 ? -10.504 3.117   -31.455 1.00 13.45 ? 539  LYS A CB  1 
ATOM   4307  C  CG  . LYS A  1 539 ? -11.513 2.693   -32.536 1.00 16.37 ? 539  LYS A CG  1 
ATOM   4308  C  CD  . LYS A  1 539 ? -11.038 3.045   -33.944 1.00 19.35 ? 539  LYS A CD  1 
ATOM   4309  C  CE  . LYS A  1 539 ? -9.644  2.483   -34.224 1.00 22.24 ? 539  LYS A CE  1 
ATOM   4310  N  NZ  . LYS A  1 539 ? -9.124  2.768   -35.607 1.00 22.37 ? 539  LYS A NZ  1 
ATOM   4311  N  N   . GLN A  1 540 ? -9.096  3.581   -28.706 1.00 8.16  ? 540  GLN A N   1 
ATOM   4312  C  CA  . GLN A  1 540 ? -8.064  3.251   -27.728 1.00 7.27  ? 540  GLN A CA  1 
ATOM   4313  C  C   . GLN A  1 540 ? -8.649  2.694   -26.438 1.00 8.12  ? 540  GLN A C   1 
ATOM   4314  O  O   . GLN A  1 540 ? -8.128  1.730   -25.885 1.00 7.87  ? 540  GLN A O   1 
ATOM   4315  C  CB  . GLN A  1 540 ? -7.213  4.477   -27.415 1.00 6.59  ? 540  GLN A CB  1 
ATOM   4316  C  CG  . GLN A  1 540 ? -6.366  4.931   -28.581 1.00 6.64  ? 540  GLN A CG  1 
ATOM   4317  C  CD  . GLN A  1 540 ? -5.444  6.063   -28.209 1.00 6.45  ? 540  GLN A CD  1 
ATOM   4318  O  OE1 . GLN A  1 540 ? -5.759  6.871   -27.335 1.00 7.17  ? 540  GLN A OE1 1 
ATOM   4319  N  NE2 . GLN A  1 540 ? -4.304  6.142   -28.884 1.00 5.63  ? 540  GLN A NE2 1 
ATOM   4320  N  N   . ARG A  1 541 ? -9.727  3.307   -25.960 1.00 8.96  ? 541  ARG A N   1 
ATOM   4321  C  CA  . ARG A  1 541 ? -10.392 2.862   -24.740 1.00 9.86  ? 541  ARG A CA  1 
ATOM   4322  C  C   . ARG A  1 541 ? -10.937 1.440   -24.922 1.00 11.52 ? 541  ARG A C   1 
ATOM   4323  O  O   . ARG A  1 541 ? -10.588 0.514   -24.180 1.00 9.16  ? 541  ARG A O   1 
ATOM   4324  C  CB  . ARG A  1 541 ? -11.559 3.806   -24.389 1.00 11.59 ? 541  ARG A CB  1 
ATOM   4325  C  CG  . ARG A  1 541 ? -11.173 5.256   -24.082 1.00 12.65 ? 541  ARG A CG  1 
ATOM   4326  C  CD  . ARG A  1 541 ? -12.313 6.013   -23.377 1.00 13.64 ? 541  ARG A CD  1 
ATOM   4327  N  NE  . ARG A  1 541 ? -13.385 6.454   -24.276 1.00 15.13 ? 541  ARG A NE  1 
ATOM   4328  C  CZ  . ARG A  1 541 ? -13.295 7.489   -25.113 1.00 14.67 ? 541  ARG A CZ  1 
ATOM   4329  N  NH1 . ARG A  1 541 ? -12.177 8.202   -25.175 1.00 14.57 ? 541  ARG A NH1 1 
ATOM   4330  N  NH2 . ARG A  1 541 ? -14.327 7.818   -25.884 1.00 13.35 ? 541  ARG A NH2 1 
ATOM   4331  N  N   . ASP A  1 542 ? -11.804 1.286   -25.919 1.00 12.83 ? 542  ASP A N   1 
ATOM   4332  C  CA  . ASP A  1 542 ? -12.424 0.002   -26.223 1.00 13.90 ? 542  ASP A CA  1 
ATOM   4333  C  C   . ASP A  1 542 ? -11.463 -1.176  -26.151 1.00 13.82 ? 542  ASP A C   1 
ATOM   4334  O  O   . ASP A  1 542 ? -11.881 -2.314  -25.945 1.00 14.63 ? 542  ASP A O   1 
ATOM   4335  C  CB  . ASP A  1 542 ? -13.066 0.056   -27.609 1.00 15.97 ? 542  ASP A CB  1 
ATOM   4336  C  CG  . ASP A  1 542 ? -14.557 0.266   -27.541 1.00 18.35 ? 542  ASP A CG  1 
ATOM   4337  O  OD1 . ASP A  1 542 ? -15.261 -0.667  -27.083 1.00 18.72 ? 542  ASP A OD1 1 
ATOM   4338  O  OD2 . ASP A  1 542 ? -15.019 1.362   -27.934 1.00 18.77 ? 542  ASP A OD2 1 
ATOM   4339  N  N   . SER A  1 543 ? -10.177 -0.889  -26.321 1.00 12.50 ? 543  SER A N   1 
ATOM   4340  C  CA  . SER A  1 543 ? -9.137  -1.903  -26.294 1.00 10.55 ? 543  SER A CA  1 
ATOM   4341  C  C   . SER A  1 543 ? -8.501  -2.024  -24.912 1.00 8.85  ? 543  SER A C   1 
ATOM   4342  O  O   . SER A  1 543 ? -7.893  -3.046  -24.590 1.00 8.03  ? 543  SER A O   1 
ATOM   4343  C  CB  . SER A  1 543 ? -8.071  -1.560  -27.340 1.00 11.68 ? 543  SER A CB  1 
ATOM   4344  O  OG  . SER A  1 543 ? -6.918  -2.369  -27.182 1.00 15.71 ? 543  SER A OG  1 
ATOM   4345  N  N   . LEU A  1 544 ? -8.634  -0.975  -24.104 1.00 8.00  ? 544  LEU A N   1 
ATOM   4346  C  CA  . LEU A  1 544 ? -8.082  -0.968  -22.750 1.00 7.53  ? 544  LEU A CA  1 
ATOM   4347  C  C   . LEU A  1 544 ? -9.076  -1.622  -21.809 1.00 9.60  ? 544  LEU A C   1 
ATOM   4348  O  O   . LEU A  1 544 ? -8.716  -2.072  -20.719 1.00 9.55  ? 544  LEU A O   1 
ATOM   4349  C  CB  . LEU A  1 544 ? -7.788  0.461   -22.284 1.00 4.50  ? 544  LEU A CB  1 
ATOM   4350  C  CG  . LEU A  1 544 ? -6.392  0.971   -22.642 1.00 4.18  ? 544  LEU A CG  1 
ATOM   4351  C  CD1 . LEU A  1 544 ? -6.363  2.496   -22.718 1.00 3.46  ? 544  LEU A CD1 1 
ATOM   4352  C  CD2 . LEU A  1 544 ? -5.413  0.443   -21.613 1.00 2.90  ? 544  LEU A CD2 1 
ATOM   4353  N  N   . GLN A  1 545 ? -10.331 -1.683  -22.244 1.00 10.22 ? 545  GLN A N   1 
ATOM   4354  C  CA  . GLN A  1 545 ? -11.378 -2.299  -21.441 1.00 10.69 ? 545  GLN A CA  1 
ATOM   4355  C  C   . GLN A  1 545 ? -11.132 -3.783  -21.239 1.00 9.68  ? 545  GLN A C   1 
ATOM   4356  O  O   . GLN A  1 545 ? -11.909 -4.448  -20.560 1.00 9.02  ? 545  GLN A O   1 
ATOM   4357  C  CB  . GLN A  1 545 ? -12.737 -2.116  -22.112 1.00 15.54 ? 545  GLN A CB  1 
ATOM   4358  C  CG  . GLN A  1 545 ? -13.513 -0.914  -21.632 1.00 22.18 ? 545  GLN A CG  1 
ATOM   4359  C  CD  . GLN A  1 545 ? -14.575 -0.485  -22.627 1.00 25.84 ? 545  GLN A CD  1 
ATOM   4360  O  OE1 . GLN A  1 545 ? -15.544 0.191   -22.268 1.00 27.84 ? 545  GLN A OE1 1 
ATOM   4361  N  NE2 . GLN A  1 545 ? -14.390 -0.863  -23.895 1.00 27.71 ? 545  GLN A NE2 1 
ATOM   4362  N  N   . LYS A  1 546 ? -10.055 -4.306  -21.817 1.00 7.03  ? 546  LYS A N   1 
ATOM   4363  C  CA  . LYS A  1 546 ? -9.783  -5.726  -21.696 1.00 4.67  ? 546  LYS A CA  1 
ATOM   4364  C  C   . LYS A  1 546 ? -8.485  -6.104  -21.015 1.00 3.13  ? 546  LYS A C   1 
ATOM   4365  O  O   . LYS A  1 546 ? -8.153  -7.281  -20.948 1.00 3.21  ? 546  LYS A O   1 
ATOM   4366  C  CB  . LYS A  1 546 ? -9.837  -6.397  -23.066 1.00 6.63  ? 546  LYS A CB  1 
ATOM   4367  C  CG  . LYS A  1 546 ? -11.169 -6.283  -23.804 1.00 7.80  ? 546  LYS A CG  1 
ATOM   4368  C  CD  . LYS A  1 546 ? -11.047 -6.980  -25.162 1.00 8.65  ? 546  LYS A CD  1 
ATOM   4369  C  CE  . LYS A  1 546 ? -12.023 -6.432  -26.187 1.00 8.59  ? 546  LYS A CE  1 
ATOM   4370  N  NZ  . LYS A  1 546 ? -11.737 -6.976  -27.546 1.00 8.14  ? 546  LYS A NZ  1 
ATOM   4371  N  N   . VAL A  1 547 ? -7.731  -5.130  -20.530 1.00 2.01  ? 547  VAL A N   1 
ATOM   4372  C  CA  . VAL A  1 547 ? -6.508  -5.470  -19.812 1.00 3.35  ? 547  VAL A CA  1 
ATOM   4373  C  C   . VAL A  1 547 ? -6.940  -6.340  -18.623 1.00 3.21  ? 547  VAL A C   1 
ATOM   4374  O  O   . VAL A  1 547 ? -8.054  -6.172  -18.113 1.00 4.59  ? 547  VAL A O   1 
ATOM   4375  C  CB  . VAL A  1 547 ? -5.828  -4.215  -19.250 1.00 2.07  ? 547  VAL A CB  1 
ATOM   4376  C  CG1 . VAL A  1 547 ? -5.178  -3.425  -20.365 1.00 2.01  ? 547  VAL A CG1 1 
ATOM   4377  C  CG2 . VAL A  1 547 ? -6.859  -3.360  -18.535 1.00 2.00  ? 547  VAL A CG2 1 
ATOM   4378  N  N   . SER A  1 548 ? -6.088  -7.275  -18.198 1.00 3.11  ? 548  SER A N   1 
ATOM   4379  C  CA  . SER A  1 548 ? -6.393  -8.133  -17.036 1.00 4.92  ? 548  SER A CA  1 
ATOM   4380  C  C   . SER A  1 548 ? -5.088  -8.483  -16.338 1.00 3.29  ? 548  SER A C   1 
ATOM   4381  O  O   . SER A  1 548 ? -4.038  -8.524  -16.984 1.00 4.73  ? 548  SER A O   1 
ATOM   4382  C  CB  . SER A  1 548 ? -7.114  -9.425  -17.451 1.00 2.78  ? 548  SER A CB  1 
ATOM   4383  O  OG  . SER A  1 548 ? -6.262  -10.282 -18.180 1.00 2.00  ? 548  SER A OG  1 
ATOM   4384  N  N   . PHE A  1 549 ? -5.127  -8.731  -15.032 1.00 2.30  ? 549  PHE A N   1 
ATOM   4385  C  CA  . PHE A  1 549 ? -3.875  -9.051  -14.375 1.00 3.34  ? 549  PHE A CA  1 
ATOM   4386  C  C   . PHE A  1 549 ? -3.396  -10.435 -14.809 1.00 2.22  ? 549  PHE A C   1 
ATOM   4387  O  O   . PHE A  1 549 ? -2.205  -10.744 -14.720 1.00 2.77  ? 549  PHE A O   1 
ATOM   4388  C  CB  . PHE A  1 549 ? -3.979  -8.967  -12.848 1.00 2.00  ? 549  PHE A CB  1 
ATOM   4389  C  CG  . PHE A  1 549 ? -2.651  -9.066  -12.172 1.00 2.00  ? 549  PHE A CG  1 
ATOM   4390  C  CD1 . PHE A  1 549 ? -1.724  -8.040  -12.284 1.00 2.00  ? 549  PHE A CD1 1 
ATOM   4391  C  CD2 . PHE A  1 549 ? -2.280  -10.225 -11.517 1.00 2.00  ? 549  PHE A CD2 1 
ATOM   4392  C  CE1 . PHE A  1 549 ? -0.442  -8.170  -11.758 1.00 2.00  ? 549  PHE A CE1 1 
ATOM   4393  C  CE2 . PHE A  1 549 ? -1.006  -10.365 -10.991 1.00 2.18  ? 549  PHE A CE2 1 
ATOM   4394  C  CZ  . PHE A  1 549 ? -0.084  -9.330  -11.115 1.00 2.00  ? 549  PHE A CZ  1 
ATOM   4395  N  N   . SER A  1 550 ? -4.319  -11.254 -15.309 1.00 2.00  ? 550  SER A N   1 
ATOM   4396  C  CA  . SER A  1 550 ? -3.967  -12.591 -15.777 1.00 2.00  ? 550  SER A CA  1 
ATOM   4397  C  C   . SER A  1 550 ? -3.123  -12.446 -17.039 1.00 2.00  ? 550  SER A C   1 
ATOM   4398  O  O   . SER A  1 550 ? -2.123  -13.138 -17.210 1.00 2.72  ? 550  SER A O   1 
ATOM   4399  C  CB  . SER A  1 550 ? -5.221  -13.406 -16.104 1.00 2.00  ? 550  SER A CB  1 
ATOM   4400  O  OG  . SER A  1 550 ? -6.260  -13.142 -15.183 1.00 2.00  ? 550  SER A OG  1 
ATOM   4401  N  N   . ARG A  1 551 ? -3.558  -11.541 -17.926 1.00 2.00  ? 551  ARG A N   1 
ATOM   4402  C  CA  . ARG A  1 551 ? -2.756  -11.330 -19.161 1.00 2.41  ? 551  ARG A CA  1 
ATOM   4403  C  C   . ARG A  1 551 ? -1.400  -10.805 -18.819 1.00 3.52  ? 551  ARG A C   1 
ATOM   4404  O  O   . ARG A  1 551 ? -0.409  -11.253 -19.397 1.00 3.41  ? 551  ARG A O   1 
ATOM   4405  C  CB  . ARG A  1 551 ? -3.388  -10.366 -20.165 1.00 3.44  ? 551  ARG A CB  1 
ATOM   4406  C  CG  . ARG A  1 551 ? -2.577  -10.283 -21.445 1.00 5.71  ? 551  ARG A CG  1 
ATOM   4407  C  CD  . ARG A  1 551 ? -2.971  -11.364 -22.471 1.00 6.05  ? 551  ARG A CD  1 
ATOM   4408  N  NE  . ARG A  1 551 ? -1.893  -12.297 -22.815 1.00 7.85  ? 551  ARG A NE  1 
ATOM   4409  C  CZ  . ARG A  1 551 ? -1.995  -13.389 -23.569 1.00 8.69  ? 551  ARG A CZ  1 
ATOM   4410  N  NH1 . ARG A  1 551 ? -3.167  -13.715 -24.105 1.00 9.19  ? 551  ARG A NH1 1 
ATOM   4411  N  NH2 . ARG A  1 551 ? -0.936  -14.161 -23.787 1.00 7.59  ? 551  ARG A NH2 1 
ATOM   4412  N  N   . LEU A  1 552 ? -1.327  -9.862  -17.880 1.00 2.15  ? 552  LEU A N   1 
ATOM   4413  C  CA  . LEU A  1 552 ? -0.038  -9.319  -17.476 1.00 2.00  ? 552  LEU A CA  1 
ATOM   4414  C  C   . LEU A  1 552 ? 0.889   -10.499 -17.232 1.00 2.00  ? 552  LEU A C   1 
ATOM   4415  O  O   . LEU A  1 552 ? 1.962   -10.596 -17.832 1.00 2.00  ? 552  LEU A O   1 
ATOM   4416  C  CB  . LEU A  1 552 ? -0.158  -8.505  -16.187 1.00 2.00  ? 552  LEU A CB  1 
ATOM   4417  C  CG  . LEU A  1 552 ? 1.179   -7.911  -15.722 1.00 2.00  ? 552  LEU A CG  1 
ATOM   4418  C  CD1 . LEU A  1 552 ? 1.670   -6.923  -16.768 1.00 2.00  ? 552  LEU A CD1 1 
ATOM   4419  C  CD2 . LEU A  1 552 ? 1.023   -7.222  -14.387 1.00 2.00  ? 552  LEU A CD2 1 
ATOM   4420  N  N   . ILE A  1 553 ? 0.451   -11.395 -16.349 1.00 2.52  ? 553  ILE A N   1 
ATOM   4421  C  CA  . ILE A  1 553 ? 1.206   -12.598 -16.000 1.00 2.00  ? 553  ILE A CA  1 
ATOM   4422  C  C   . ILE A  1 553 ? 1.704   -13.308 -17.253 1.00 2.00  ? 553  ILE A C   1 
ATOM   4423  O  O   . ILE A  1 553 ? 2.882   -13.647 -17.353 1.00 2.00  ? 553  ILE A O   1 
ATOM   4424  C  CB  . ILE A  1 553 ? 0.343   -13.627 -15.233 1.00 2.00  ? 553  ILE A CB  1 
ATOM   4425  C  CG1 . ILE A  1 553 ? -0.177  -13.047 -13.912 1.00 2.00  ? 553  ILE A CG1 1 
ATOM   4426  C  CG2 . ILE A  1 553 ? 1.152   -14.884 -15.012 1.00 2.61  ? 553  ILE A CG2 1 
ATOM   4427  C  CD1 . ILE A  1 553 ? 0.889   -12.625 -12.962 1.00 2.00  ? 553  ILE A CD1 1 
ATOM   4428  N  N   . CYS A  1 554 ? 0.794   -13.531 -18.198 1.00 2.00  ? 554  CYS A N   1 
ATOM   4429  C  CA  . CYS A  1 554 ? 1.118   -14.220 -19.440 1.00 2.00  ? 554  CYS A CA  1 
ATOM   4430  C  C   . CYS A  1 554 ? 2.205   -13.565 -20.302 1.00 2.63  ? 554  CYS A C   1 
ATOM   4431  O  O   . CYS A  1 554 ? 3.298   -14.109 -20.440 1.00 3.05  ? 554  CYS A O   1 
ATOM   4432  C  CB  . CYS A  1 554 ? -0.145  -14.400 -20.278 1.00 2.34  ? 554  CYS A CB  1 
ATOM   4433  S  SG  . CYS A  1 554 ? -1.447  -15.428 -19.527 1.00 2.12  ? 554  CYS A SG  1 
ATOM   4434  N  N   . ASP A  1 555 ? 1.915   -12.407 -20.887 1.00 2.55  ? 555  ASP A N   1 
ATOM   4435  C  CA  . ASP A  1 555 ? 2.896   -11.737 -21.742 1.00 2.31  ? 555  ASP A CA  1 
ATOM   4436  C  C   . ASP A  1 555 ? 4.284   -11.551 -21.094 1.00 3.72  ? 555  ASP A C   1 
ATOM   4437  O  O   . ASP A  1 555 ? 5.276   -11.369 -21.805 1.00 5.21  ? 555  ASP A O   1 
ATOM   4438  C  CB  . ASP A  1 555 ? 2.386   -10.349 -22.198 1.00 2.00  ? 555  ASP A CB  1 
ATOM   4439  C  CG  . ASP A  1 555 ? 1.061   -10.405 -22.959 1.00 2.00  ? 555  ASP A CG  1 
ATOM   4440  O  OD1 . ASP A  1 555 ? 0.805   -11.397 -23.673 1.00 2.35  ? 555  ASP A OD1 1 
ATOM   4441  O  OD2 . ASP A  1 555 ? 0.277   -9.433  -22.859 1.00 2.00  ? 555  ASP A OD2 1 
ATOM   4442  N  N   . ASN A  1 556 ? 4.406   -11.642 -19.765 1.00 2.85  ? 556  ASN A N   1 
ATOM   4443  C  CA  . ASN A  1 556 ? 5.693   -11.341 -19.137 1.00 2.57  ? 556  ASN A CA  1 
ATOM   4444  C  C   . ASN A  1 556 ? 6.320   -12.431 -18.234 1.00 2.86  ? 556  ASN A C   1 
ATOM   4445  O  O   . ASN A  1 556 ? 7.072   -12.128 -17.307 1.00 2.00  ? 556  ASN A O   1 
ATOM   4446  C  CB  . ASN A  1 556 ? 5.578   -10.080 -18.304 1.00 3.15  ? 556  ASN A CB  1 
ATOM   4447  C  CG  . ASN A  1 556 ? 5.630   -8.861  -19.182 1.00 3.22  ? 556  ASN A CG  1 
ATOM   4448  O  OD1 . ASN A  1 556 ? 6.607   -8.645  -19.900 1.00 5.55  ? 556  ASN A OD1 1 
ATOM   4449  N  ND2 . ASN A  1 556 ? 4.579   -8.057  -19.143 1.00 2.85  ? 556  ASN A ND2 1 
ATOM   4450  N  N   . THR A  1 557 ? 6.016   -13.692 -18.525 1.00 4.12  ? 557  THR A N   1 
ATOM   4451  C  CA  . THR A  1 557 ? 6.542   -14.847 -17.745 1.00 6.39  ? 557  THR A CA  1 
ATOM   4452  C  C   . THR A  1 557 ? 6.384   -16.104 -18.558 1.00 5.83  ? 557  THR A C   1 
ATOM   4453  O  O   . THR A  1 557 ? 5.826   -16.091 -19.654 1.00 6.70  ? 557  THR A O   1 
ATOM   4454  C  CB  . THR A  1 557 ? 5.768   -15.005 -16.426 1.00 6.71  ? 557  THR A CB  1 
ATOM   4455  O  OG1 . THR A  1 557 ? 4.467   -15.528 -16.705 1.00 6.85  ? 557  THR A OG1 1 
ATOM   4456  C  CG2 . THR A  1 557 ? 5.645   -13.649 -15.727 1.00 7.35  ? 557  THR A CG2 1 
ATOM   4457  N  N   . HIS A  1 558 ? 6.822   -17.203 -18.018 1.00 5.69  ? 558  HIS A N   1 
ATOM   4458  C  CA  . HIS A  1 558 ? 6.741   -18.439 -18.757 1.00 5.46  ? 558  HIS A CA  1 
ATOM   4459  C  C   . HIS A  1 558 ? 5.670   -19.373 -18.217 1.00 4.48  ? 558  HIS A C   1 
ATOM   4460  O  O   . HIS A  1 558 ? 5.777   -20.605 -18.264 1.00 2.08  ? 558  HIS A O   1 
ATOM   4461  C  CB  . HIS A  1 558 ? 8.102   -19.090 -18.741 1.00 6.24  ? 558  HIS A CB  1 
ATOM   4462  C  CG  . HIS A  1 558 ? 9.110   -18.326 -19.640 1.00 5.78  ? 558  HIS A CG  1 
ATOM   4463  N  ND1 . HIS A  1 558 ? 10.466  -18.574 -19.590 1.00 6.25  ? 558  HIS A ND1 1 
ATOM   4464  C  CD2 . HIS A  1 558 ? 8.914   -17.372 -20.581 1.00 5.37  ? 558  HIS A CD2 1 
ATOM   4465  C  CE1 . HIS A  1 558 ? 11.062  -17.804 -20.484 1.00 6.60  ? 558  HIS A CE1 1 
ATOM   4466  N  NE2 . HIS A  1 558 ? 10.143  -17.066 -21.080 1.00 5.89  ? 558  HIS A NE2 1 
ATOM   4467  N  N   . ILE A  1 559 ? 4.623   -18.737 -17.687 1.00 3.41  ? 559  ILE A N   1 
ATOM   4468  C  CA  . ILE A  1 559 ? 3.465   -19.412 -17.118 1.00 2.25  ? 559  ILE A CA  1 
ATOM   4469  C  C   . ILE A  1 559 ? 2.406   -19.455 -18.208 1.00 2.00  ? 559  ILE A C   1 
ATOM   4470  O  O   . ILE A  1 559 ? 2.132   -18.444 -18.859 1.00 2.00  ? 559  ILE A O   1 
ATOM   4471  C  CB  . ILE A  1 559 ? 2.928   -18.649 -15.890 1.00 2.00  ? 559  ILE A CB  1 
ATOM   4472  C  CG1 . ILE A  1 559 ? 4.095   -18.294 -14.957 1.00 2.09  ? 559  ILE A CG1 1 
ATOM   4473  C  CG2 . ILE A  1 559 ? 1.919   -19.513 -15.153 1.00 2.00  ? 559  ILE A CG2 1 
ATOM   4474  C  CD1 . ILE A  1 559 ? 3.721   -17.531 -13.710 1.00 2.00  ? 559  ILE A CD1 1 
ATOM   4475  N  N   . THR A  1 560 ? 1.828   -20.632 -18.418 1.00 2.00  ? 560  THR A N   1 
ATOM   4476  C  CA  . THR A  1 560 ? 0.829   -20.808 -19.462 1.00 2.80  ? 560  THR A CA  1 
ATOM   4477  C  C   . THR A  1 560 ? -0.573  -21.105 -18.958 1.00 3.09  ? 560  THR A C   1 
ATOM   4478  O  O   . THR A  1 560 ? -1.521  -21.138 -19.738 1.00 2.55  ? 560  THR A O   1 
ATOM   4479  C  CB  . THR A  1 560 ? 1.218   -21.944 -20.399 1.00 2.34  ? 560  THR A CB  1 
ATOM   4480  O  OG1 . THR A  1 560 ? 1.126   -23.187 -19.693 1.00 4.80  ? 560  THR A OG1 1 
ATOM   4481  C  CG2 . THR A  1 560 ? 2.634   -21.756 -20.888 1.00 3.38  ? 560  THR A CG2 1 
ATOM   4482  N  N   . LYS A  1 561 ? -0.711  -21.349 -17.665 1.00 3.79  ? 561  LYS A N   1 
ATOM   4483  C  CA  . LYS A  1 561 ? -2.027  -21.627 -17.118 1.00 4.67  ? 561  LYS A CA  1 
ATOM   4484  C  C   . LYS A  1 561 ? -2.304  -20.572 -16.043 1.00 4.35  ? 561  LYS A C   1 
ATOM   4485  O  O   . LYS A  1 561 ? -1.590  -20.481 -15.035 1.00 2.38  ? 561  LYS A O   1 
ATOM   4486  C  CB  . LYS A  1 561 ? -2.070  -23.040 -16.523 1.00 7.38  ? 561  LYS A CB  1 
ATOM   4487  C  CG  . LYS A  1 561 ? -1.524  -24.147 -17.437 1.00 10.77 ? 561  LYS A CG  1 
ATOM   4488  C  CD  . LYS A  1 561 ? -2.557  -24.673 -18.429 1.00 13.99 ? 561  LYS A CD  1 
ATOM   4489  C  CE  . LYS A  1 561 ? -1.965  -25.788 -19.300 1.00 15.48 ? 561  LYS A CE  1 
ATOM   4490  N  NZ  . LYS A  1 561 ? -2.945  -26.887 -19.588 1.00 17.67 ? 561  LYS A NZ  1 
ATOM   4491  N  N   . VAL A  1 562 ? -3.331  -19.760 -16.291 1.00 3.66  ? 562  VAL A N   1 
ATOM   4492  C  CA  . VAL A  1 562 ? -3.746  -18.690 -15.386 1.00 4.17  ? 562  VAL A CA  1 
ATOM   4493  C  C   . VAL A  1 562 ? -5.276  -18.568 -15.388 1.00 4.77  ? 562  VAL A C   1 
ATOM   4494  O  O   . VAL A  1 562 ? -5.923  -18.766 -16.420 1.00 4.19  ? 562  VAL A O   1 
ATOM   4495  C  CB  . VAL A  1 562 ? -3.144  -17.337 -15.812 1.00 4.09  ? 562  VAL A CB  1 
ATOM   4496  C  CG1 . VAL A  1 562 ? -1.625  -17.404 -15.765 1.00 2.00  ? 562  VAL A CG1 1 
ATOM   4497  C  CG2 . VAL A  1 562 ? -3.632  -16.971 -17.215 1.00 4.62  ? 562  VAL A CG2 1 
ATOM   4498  N  N   . PRO A  1 563 ? -5.865  -18.210 -14.238 1.00 2.47  ? 563  PRO A N   1 
ATOM   4499  C  CA  . PRO A  1 563 ? -7.309  -18.054 -14.045 1.00 3.64  ? 563  PRO A CA  1 
ATOM   4500  C  C   . PRO A  1 563 ? -7.848  -16.765 -14.633 1.00 5.17  ? 563  PRO A C   1 
ATOM   4501  O  O   . PRO A  1 563 ? -7.103  -15.798 -14.796 1.00 7.08  ? 563  PRO A O   1 
ATOM   4502  C  CB  . PRO A  1 563 ? -7.466  -18.073 -12.521 1.00 5.02  ? 563  PRO A CB  1 
ATOM   4503  C  CG  . PRO A  1 563 ? -6.065  -18.443 -11.983 1.00 5.39  ? 563  PRO A CG  1 
ATOM   4504  C  CD  . PRO A  1 563 ? -5.156  -17.853 -13.005 1.00 4.07  ? 563  PRO A CD  1 
ATOM   4505  N  N   . LEU A  1 564 ? -9.146  -16.749 -14.932 1.00 3.25  ? 564  LEU A N   1 
ATOM   4506  C  CA  . LEU A  1 564 ? -9.779  -15.566 -15.493 1.00 2.21  ? 564  LEU A CA  1 
ATOM   4507  C  C   . LEU A  1 564 ? -9.862  -14.512 -14.410 1.00 2.00  ? 564  LEU A C   1 
ATOM   4508  O  O   . LEU A  1 564 ? -9.617  -13.337 -14.647 1.00 3.14  ? 564  LEU A O   1 
ATOM   4509  C  CB  . LEU A  1 564 ? -11.206 -15.861 -15.984 1.00 2.00  ? 564  LEU A CB  1 
ATOM   4510  C  CG  . LEU A  1 564 ? -11.626 -16.984 -16.954 1.00 2.20  ? 564  LEU A CG  1 
ATOM   4511  C  CD1 . LEU A  1 564 ? -10.530 -17.248 -17.973 1.00 2.00  ? 564  LEU A CD1 1 
ATOM   4512  C  CD2 . LEU A  1 564 ? -11.952 -18.254 -16.171 1.00 2.00  ? 564  LEU A CD2 1 
ATOM   4513  N  N   . HIS A  1 565 ? -10.188 -14.940 -13.204 1.00 2.00  ? 565  HIS A N   1 
ATOM   4514  C  CA  . HIS A  1 565 ? -10.341 -13.995 -12.109 1.00 3.26  ? 565  HIS A CA  1 
ATOM   4515  C  C   . HIS A  1 565 ? -9.246  -14.094 -11.041 1.00 3.73  ? 565  HIS A C   1 
ATOM   4516  O  O   . HIS A  1 565 ? -9.465  -14.595 -9.930  1.00 3.45  ? 565  HIS A O   1 
ATOM   4517  C  CB  . HIS A  1 565 ? -11.738 -14.196 -11.533 1.00 3.98  ? 565  HIS A CB  1 
ATOM   4518  C  CG  . HIS A  1 565 ? -12.797 -14.262 -12.589 1.00 3.18  ? 565  HIS A CG  1 
ATOM   4519  N  ND1 . HIS A  1 565 ? -13.475 -13.148 -13.035 1.00 2.68  ? 565  HIS A ND1 1 
ATOM   4520  C  CD2 . HIS A  1 565 ? -13.230 -15.294 -13.352 1.00 2.98  ? 565  HIS A CD2 1 
ATOM   4521  C  CE1 . HIS A  1 565 ? -14.279 -13.491 -14.027 1.00 3.14  ? 565  HIS A CE1 1 
ATOM   4522  N  NE2 . HIS A  1 565 ? -14.149 -14.788 -14.240 1.00 3.11  ? 565  HIS A NE2 1 
ATOM   4523  N  N   . ALA A  1 566 ? -8.072  -13.576 -11.406 1.00 3.33  ? 566  ALA A N   1 
ATOM   4524  C  CA  . ALA A  1 566 ? -6.876  -13.580 -10.570 1.00 2.00  ? 566  ALA A CA  1 
ATOM   4525  C  C   . ALA A  1 566 ? -7.027  -13.014 -9.175  1.00 2.26  ? 566  ALA A C   1 
ATOM   4526  O  O   . ALA A  1 566 ? -6.088  -13.067 -8.389  1.00 2.38  ? 566  ALA A O   1 
ATOM   4527  C  CB  . ALA A  1 566 ? -5.757  -12.850 -11.279 1.00 2.00  ? 566  ALA A CB  1 
ATOM   4528  N  N   . PHE A  1 567 ? -8.184  -12.473 -8.836  1.00 3.05  ? 567  PHE A N   1 
ATOM   4529  C  CA  . PHE A  1 567 ? -8.287  -11.925 -7.499  1.00 5.42  ? 567  PHE A CA  1 
ATOM   4530  C  C   . PHE A  1 567 ? -8.953  -12.800 -6.447  1.00 5.90  ? 567  PHE A C   1 
ATOM   4531  O  O   . PHE A  1 567 ? -8.648  -12.683 -5.264  1.00 5.73  ? 567  PHE A O   1 
ATOM   4532  C  CB  . PHE A  1 567 ? -8.935  -10.538 -7.542  1.00 4.14  ? 567  PHE A CB  1 
ATOM   4533  C  CG  . PHE A  1 567 ? -7.968  -9.435  -7.900  1.00 3.86  ? 567  PHE A CG  1 
ATOM   4534  C  CD1 . PHE A  1 567 ? -6.776  -9.288  -7.205  1.00 4.11  ? 567  PHE A CD1 1 
ATOM   4535  C  CD2 . PHE A  1 567 ? -8.255  -8.534  -8.914  1.00 4.60  ? 567  PHE A CD2 1 
ATOM   4536  C  CE1 . PHE A  1 567 ? -5.885  -8.257  -7.512  1.00 5.02  ? 567  PHE A CE1 1 
ATOM   4537  C  CE2 . PHE A  1 567 ? -7.366  -7.498  -9.226  1.00 4.87  ? 567  PHE A CE2 1 
ATOM   4538  C  CZ  . PHE A  1 567 ? -6.182  -7.362  -8.523  1.00 3.96  ? 567  PHE A CZ  1 
ATOM   4539  N  N   . GLN A  1 568 ? -9.838  -13.696 -6.855  1.00 7.46  ? 568  GLN A N   1 
ATOM   4540  C  CA  . GLN A  1 568 ? -10.505 -14.543 -5.873  1.00 9.18  ? 568  GLN A CA  1 
ATOM   4541  C  C   . GLN A  1 568 ? -9.772  -15.855 -5.646  1.00 9.37  ? 568  GLN A C   1 
ATOM   4542  O  O   . GLN A  1 568 ? -8.603  -15.980 -5.995  1.00 10.19 ? 568  GLN A O   1 
ATOM   4543  C  CB  . GLN A  1 568 ? -11.922 -14.815 -6.333  1.00 10.09 ? 568  GLN A CB  1 
ATOM   4544  C  CG  . GLN A  1 568 ? -11.986 -15.173 -7.781  1.00 13.51 ? 568  GLN A CG  1 
ATOM   4545  C  CD  . GLN A  1 568 ? -13.395 -15.176 -8.268  1.00 15.68 ? 568  GLN A CD  1 
ATOM   4546  O  OE1 . GLN A  1 568 ? -14.160 -14.260 -7.962  1.00 16.45 ? 568  GLN A OE1 1 
ATOM   4547  N  NE2 . GLN A  1 568 ? -13.760 -16.199 -9.036  1.00 17.11 ? 568  GLN A NE2 1 
ATOM   4548  N  N   . ALA A  1 569 ? -10.447 -16.825 -5.039  1.00 10.51 ? 569  ALA A N   1 
ATOM   4549  C  CA  . ALA A  1 569 ? -9.833  -18.128 -4.811  1.00 11.48 ? 569  ALA A CA  1 
ATOM   4550  C  C   . ALA A  1 569 ? -9.829  -18.871 -6.152  1.00 13.37 ? 569  ALA A C   1 
ATOM   4551  O  O   . ALA A  1 569 ? -10.745 -18.714 -6.966  1.00 14.77 ? 569  ALA A O   1 
ATOM   4552  C  CB  . ALA A  1 569 ? -10.623 -18.916 -3.772  1.00 11.50 ? 569  ALA A CB  1 
ATOM   4553  N  N   . ASN A  1 570 ? -8.799  -19.675 -6.383  1.00 12.19 ? 570  ASN A N   1 
ATOM   4554  C  CA  . ASN A  1 570 ? -8.680  -20.417 -7.630  1.00 10.31 ? 570  ASN A CA  1 
ATOM   4555  C  C   . ASN A  1 570 ? -7.855  -21.665 -7.385  1.00 12.21 ? 570  ASN A C   1 
ATOM   4556  O  O   . ASN A  1 570 ? -6.648  -21.575 -7.146  1.00 12.05 ? 570  ASN A O   1 
ATOM   4557  C  CB  . ASN A  1 570 ? -7.972  -19.568 -8.685  1.00 10.79 ? 570  ASN A CB  1 
ATOM   4558  C  CG  . ASN A  1 570 ? -8.807  -18.407 -9.163  1.00 10.48 ? 570  ASN A CG  1 
ATOM   4559  O  OD1 . ASN A  1 570 ? -8.343  -17.263 -9.186  1.00 9.83  ? 570  ASN A OD1 1 
ATOM   4560  N  ND2 . ASN A  1 570 ? -10.042 -18.692 -9.567  1.00 10.28 ? 570  ASN A ND2 1 
ATOM   4561  N  N   . ASN A  1 571 ? -8.496  -22.826 -7.446  1.00 13.58 ? 571  ASN A N   1 
ATOM   4562  C  CA  . ASN A  1 571 ? -7.792  -24.081 -7.228  1.00 14.83 ? 571  ASN A CA  1 
ATOM   4563  C  C   . ASN A  1 571 ? -7.243  -24.642 -8.520  1.00 15.33 ? 571  ASN A C   1 
ATOM   4564  O  O   . ASN A  1 571 ? -7.897  -24.579 -9.560  1.00 16.61 ? 571  ASN A O   1 
ATOM   4565  C  CB  . ASN A  1 571 ? -8.717  -25.103 -6.583  1.00 17.30 ? 571  ASN A CB  1 
ATOM   4566  C  CG  . ASN A  1 571 ? -9.080  -24.728 -5.169  1.00 20.36 ? 571  ASN A CG  1 
ATOM   4567  O  OD1 . ASN A  1 571 ? -8.212  -24.647 -4.293  1.00 21.85 ? 571  ASN A OD1 1 
ATOM   4568  N  ND2 . ASN A  1 571 ? -10.365 -24.481 -4.933  1.00 21.13 ? 571  ASN A ND2 1 
ATOM   4569  N  N   . TYR A  1 572 ? -6.029  -25.173 -8.455  1.00 14.38 ? 572  TYR A N   1 
ATOM   4570  C  CA  . TYR A  1 572 ? -5.409  -25.761 -9.627  1.00 13.11 ? 572  TYR A CA  1 
ATOM   4571  C  C   . TYR A  1 572 ? -5.905  -27.203 -9.693  1.00 12.72 ? 572  TYR A C   1 
ATOM   4572  O  O   . TYR A  1 572 ? -5.979  -27.883 -8.673  1.00 14.06 ? 572  TYR A O   1 
ATOM   4573  C  CB  . TYR A  1 572 ? -3.891  -25.737 -9.495  1.00 12.41 ? 572  TYR A CB  1 
ATOM   4574  C  CG  . TYR A  1 572 ? -3.175  -26.245 -10.721 1.00 12.06 ? 572  TYR A CG  1 
ATOM   4575  C  CD1 . TYR A  1 572 ? -2.951  -25.414 -11.823 1.00 11.94 ? 572  TYR A CD1 1 
ATOM   4576  C  CD2 . TYR A  1 572 ? -2.747  -27.567 -10.794 1.00 11.98 ? 572  TYR A CD2 1 
ATOM   4577  C  CE1 . TYR A  1 572 ? -2.315  -25.892 -12.969 1.00 12.43 ? 572  TYR A CE1 1 
ATOM   4578  C  CE2 . TYR A  1 572 ? -2.113  -28.056 -11.931 1.00 13.39 ? 572  TYR A CE2 1 
ATOM   4579  C  CZ  . TYR A  1 572 ? -1.899  -27.217 -13.018 1.00 13.18 ? 572  TYR A CZ  1 
ATOM   4580  O  OH  . TYR A  1 572 ? -1.270  -27.707 -14.145 1.00 12.83 ? 572  TYR A OH  1 
ATOM   4581  N  N   . PRO A  1 573 ? -6.223  -27.698 -10.898 1.00 11.82 ? 573  PRO A N   1 
ATOM   4582  C  CA  . PRO A  1 573 ? -6.135  -26.981 -12.169 1.00 11.35 ? 573  PRO A CA  1 
ATOM   4583  C  C   . PRO A  1 573 ? -7.478  -26.568 -12.759 1.00 11.76 ? 573  PRO A C   1 
ATOM   4584  O  O   . PRO A  1 573 ? -7.513  -25.991 -13.842 1.00 10.84 ? 573  PRO A O   1 
ATOM   4585  C  CB  . PRO A  1 573 ? -5.450  -27.992 -13.052 1.00 11.34 ? 573  PRO A CB  1 
ATOM   4586  C  CG  . PRO A  1 573 ? -6.215  -29.243 -12.666 1.00 12.42 ? 573  PRO A CG  1 
ATOM   4587  C  CD  . PRO A  1 573 ? -6.376  -29.143 -11.143 1.00 11.85 ? 573  PRO A CD  1 
ATOM   4588  N  N   . HIS A  1 574 ? -8.579  -26.863 -12.073 1.00 12.89 ? 574  HIS A N   1 
ATOM   4589  C  CA  . HIS A  1 574 ? -9.887  -26.505 -12.615 1.00 12.34 ? 574  HIS A CA  1 
ATOM   4590  C  C   . HIS A  1 574 ? -10.094 -25.032 -12.887 1.00 10.94 ? 574  HIS A C   1 
ATOM   4591  O  O   . HIS A  1 574 ? -10.725 -24.678 -13.875 1.00 11.63 ? 574  HIS A O   1 
ATOM   4592  C  CB  . HIS A  1 574 ? -11.037 -26.964 -11.719 1.00 18.88 ? 574  HIS A CB  1 
ATOM   4593  C  CG  . HIS A  1 574 ? -12.350 -26.326 -12.072 1.00 25.04 ? 574  HIS A CG  1 
ATOM   4594  N  ND1 . HIS A  1 574 ? -12.918 -26.437 -13.326 1.00 27.94 ? 574  HIS A ND1 1 
ATOM   4595  C  CD2 . HIS A  1 574 ? -13.176 -25.524 -11.356 1.00 27.16 ? 574  HIS A CD2 1 
ATOM   4596  C  CE1 . HIS A  1 574 ? -14.034 -25.728 -13.367 1.00 29.15 ? 574  HIS A CE1 1 
ATOM   4597  N  NE2 . HIS A  1 574 ? -14.213 -25.164 -12.185 1.00 29.04 ? 574  HIS A NE2 1 
ATOM   4598  N  N   . ASP A  1 575 ? -9.594  -24.158 -12.029 1.00 7.77  ? 575  ASP A N   1 
ATOM   4599  C  CA  . ASP A  1 575 ? -9.824  -22.750 -12.284 1.00 6.40  ? 575  ASP A CA  1 
ATOM   4600  C  C   . ASP A  1 575 ? -8.801  -22.115 -13.195 1.00 5.11  ? 575  ASP A C   1 
ATOM   4601  O  O   . ASP A  1 575 ? -8.920  -20.941 -13.537 1.00 4.67  ? 575  ASP A O   1 
ATOM   4602  C  CB  . ASP A  1 575 ? -9.899  -21.982 -10.976 1.00 8.06  ? 575  ASP A CB  1 
ATOM   4603  C  CG  . ASP A  1 575 ? -10.841 -22.625 -9.996  1.00 9.56  ? 575  ASP A CG  1 
ATOM   4604  O  OD1 . ASP A  1 575 ? -11.935 -23.058 -10.419 1.00 10.54 ? 575  ASP A OD1 1 
ATOM   4605  O  OD2 . ASP A  1 575 ? -10.488 -22.697 -8.802  1.00 10.42 ? 575  ASP A OD2 1 
ATOM   4606  N  N   . PHE A  1 576 ? -7.805  -22.893 -13.601 1.00 3.85  ? 576  PHE A N   1 
ATOM   4607  C  CA  . PHE A  1 576 ? -6.766  -22.382 -14.481 1.00 2.70  ? 576  PHE A CA  1 
ATOM   4608  C  C   . PHE A  1 576 ? -7.015  -22.797 -15.925 1.00 4.08  ? 576  PHE A C   1 
ATOM   4609  O  O   . PHE A  1 576 ? -7.453  -23.916 -16.191 1.00 5.21  ? 576  PHE A O   1 
ATOM   4610  C  CB  . PHE A  1 576 ? -5.397  -22.878 -14.009 1.00 2.91  ? 576  PHE A CB  1 
ATOM   4611  C  CG  . PHE A  1 576 ? -4.957  -22.274 -12.700 1.00 4.62  ? 576  PHE A CG  1 
ATOM   4612  C  CD1 . PHE A  1 576 ? -5.823  -22.232 -11.608 1.00 2.28  ? 576  PHE A CD1 1 
ATOM   4613  C  CD2 . PHE A  1 576 ? -3.677  -21.739 -12.558 1.00 4.81  ? 576  PHE A CD2 1 
ATOM   4614  C  CE1 . PHE A  1 576 ? -5.424  -21.670 -10.408 1.00 2.00  ? 576  PHE A CE1 1 
ATOM   4615  C  CE2 . PHE A  1 576 ? -3.270  -21.172 -11.352 1.00 3.48  ? 576  PHE A CE2 1 
ATOM   4616  C  CZ  . PHE A  1 576 ? -4.145  -21.138 -10.280 1.00 2.00  ? 576  PHE A CZ  1 
ATOM   4617  N  N   . VAL A  1 577 ? -6.762  -21.874 -16.849 1.00 4.43  ? 577  VAL A N   1 
ATOM   4618  C  CA  . VAL A  1 577 ? -6.931  -22.120 -18.277 1.00 2.41  ? 577  VAL A CA  1 
ATOM   4619  C  C   . VAL A  1 577 ? -5.643  -21.685 -18.944 1.00 4.20  ? 577  VAL A C   1 
ATOM   4620  O  O   . VAL A  1 577 ? -4.792  -21.070 -18.299 1.00 3.49  ? 577  VAL A O   1 
ATOM   4621  C  CB  . VAL A  1 577 ? -8.081  -21.297 -18.878 1.00 3.38  ? 577  VAL A CB  1 
ATOM   4622  C  CG1 . VAL A  1 577 ? -9.394  -21.706 -18.245 1.00 4.96  ? 577  VAL A CG1 1 
ATOM   4623  C  CG2 . VAL A  1 577 ? -7.819  -19.817 -18.674 1.00 3.98  ? 577  VAL A CG2 1 
ATOM   4624  N  N   . ASP A  1 578 ? -5.503  -21.994 -20.233 1.00 5.61  ? 578  ASP A N   1 
ATOM   4625  C  CA  . ASP A  1 578 ? -4.296  -21.639 -20.977 1.00 3.96  ? 578  ASP A CA  1 
ATOM   4626  C  C   . ASP A  1 578 ? -4.300  -20.170 -21.335 1.00 2.61  ? 578  ASP A C   1 
ATOM   4627  O  O   . ASP A  1 578 ? -5.336  -19.624 -21.685 1.00 2.00  ? 578  ASP A O   1 
ATOM   4628  C  CB  . ASP A  1 578 ? -4.183  -22.466 -22.256 1.00 5.76  ? 578  ASP A CB  1 
ATOM   4629  C  CG  . ASP A  1 578 ? -2.754  -22.543 -22.769 1.00 9.33  ? 578  ASP A CG  1 
ATOM   4630  O  OD1 . ASP A  1 578 ? -1.898  -23.176 -22.084 1.00 8.77  ? 578  ASP A OD1 1 
ATOM   4631  O  OD2 . ASP A  1 578 ? -2.491  -21.960 -23.849 1.00 9.68  ? 578  ASP A OD2 1 
ATOM   4632  N  N   . CYS A  1 579 ? -3.134  -19.537 -21.255 1.00 2.00  ? 579  CYS A N   1 
ATOM   4633  C  CA  . CYS A  1 579 ? -3.028  -18.119 -21.557 1.00 2.30  ? 579  CYS A CA  1 
ATOM   4634  C  C   . CYS A  1 579 ? -3.663  -17.772 -22.885 1.00 5.49  ? 579  CYS A C   1 
ATOM   4635  O  O   . CYS A  1 579 ? -3.938  -16.595 -23.153 1.00 6.15  ? 579  CYS A O   1 
ATOM   4636  C  CB  . CYS A  1 579 ? -1.576  -17.671 -21.568 1.00 3.02  ? 579  CYS A CB  1 
ATOM   4637  S  SG  . CYS A  1 579 ? -0.867  -17.326 -19.928 1.00 5.30  ? 579  CYS A SG  1 
ATOM   4638  N  N   . SER A  1 580 ? -3.893  -18.792 -23.714 1.00 4.29  ? 580  SER A N   1 
ATOM   4639  C  CA  . SER A  1 580 ? -4.515  -18.611 -25.028 1.00 2.54  ? 580  SER A CA  1 
ATOM   4640  C  C   . SER A  1 580 ? -6.032  -18.440 -24.891 1.00 2.01  ? 580  SER A C   1 
ATOM   4641  O  O   . SER A  1 580 ? -6.726  -18.108 -25.850 1.00 2.00  ? 580  SER A O   1 
ATOM   4642  C  CB  . SER A  1 580 ? -4.218  -19.821 -25.911 1.00 2.87  ? 580  SER A CB  1 
ATOM   4643  O  OG  . SER A  1 580 ? -4.705  -21.008 -25.307 1.00 2.00  ? 580  SER A OG  1 
ATOM   4644  N  N   . ALA A  1 581 ? -6.533  -18.671 -23.683 1.00 2.58  ? 581  ALA A N   1 
ATOM   4645  C  CA  . ALA A  1 581 ? -7.954  -18.557 -23.399 1.00 4.35  ? 581  ALA A CA  1 
ATOM   4646  C  C   . ALA A  1 581 ? -8.327  -17.151 -22.951 1.00 5.59  ? 581  ALA A C   1 
ATOM   4647  O  O   . ALA A  1 581 ? -9.508  -16.818 -22.862 1.00 7.75  ? 581  ALA A O   1 
ATOM   4648  C  CB  . ALA A  1 581 ? -8.348  -19.559 -22.321 1.00 2.64  ? 581  ALA A CB  1 
ATOM   4649  N  N   . ILE A  1 582 ? -7.328  -16.324 -22.663 1.00 5.52  ? 582  ILE A N   1 
ATOM   4650  C  CA  . ILE A  1 582 ? -7.603  -14.963 -22.224 1.00 5.72  ? 582  ILE A CA  1 
ATOM   4651  C  C   . ILE A  1 582 ? -7.114  -13.907 -23.219 1.00 8.90  ? 582  ILE A C   1 
ATOM   4652  O  O   . ILE A  1 582 ? -6.035  -14.035 -23.815 1.00 8.32  ? 582  ILE A O   1 
ATOM   4653  C  CB  . ILE A  1 582 ? -6.999  -14.703 -20.833 1.00 4.00  ? 582  ILE A CB  1 
ATOM   4654  C  CG1 . ILE A  1 582 ? -5.947  -13.604 -20.902 1.00 4.53  ? 582  ILE A CG1 1 
ATOM   4655  C  CG2 . ILE A  1 582 ? -6.375  -15.960 -20.303 1.00 5.50  ? 582  ILE A CG2 1 
ATOM   4656  C  CD1 . ILE A  1 582 ? -5.357  -13.272 -19.564 1.00 5.53  ? 582  ILE A CD1 1 
ATOM   4657  N  N   . ASP A  1 583 ? -7.931  -12.865 -23.371 1.00 8.45  ? 583  ASP A N   1 
ATOM   4658  C  CA  . ASP A  1 583 ? -7.696  -11.750 -24.288 1.00 8.75  ? 583  ASP A CA  1 
ATOM   4659  C  C   . ASP A  1 583 ? -6.297  -11.136 -24.300 1.00 9.87  ? 583  ASP A C   1 
ATOM   4660  O  O   . ASP A  1 583 ? -5.501  -11.392 -23.401 1.00 7.56  ? 583  ASP A O   1 
ATOM   4661  C  CB  . ASP A  1 583 ? -8.749  -10.693 -24.019 1.00 12.28 ? 583  ASP A CB  1 
ATOM   4662  C  CG  . ASP A  1 583 ? -10.145 -11.281 -24.004 1.00 14.99 ? 583  ASP A CG  1 
ATOM   4663  O  OD1 . ASP A  1 583 ? -10.421 -12.107 -23.100 1.00 16.05 ? 583  ASP A OD1 1 
ATOM   4664  O  OD2 . ASP A  1 583 ? -10.951 -10.932 -24.900 1.00 14.17 ? 583  ASP A OD2 1 
ATOM   4665  N  N   . LYS A  1 584 ? -6.019  -10.298 -25.305 1.00 10.73 ? 584  LYS A N   1 
ATOM   4666  C  CA  . LYS A  1 584 ? -4.681  -9.712  -25.483 1.00 10.46 ? 584  LYS A CA  1 
ATOM   4667  C  C   . LYS A  1 584 ? -4.380  -8.207  -25.538 1.00 8.41  ? 584  LYS A C   1 
ATOM   4668  O  O   . LYS A  1 584 ? -3.206  -7.851  -25.636 1.00 10.23 ? 584  LYS A O   1 
ATOM   4669  C  CB  . LYS A  1 584 ? -4.029  -10.332 -26.733 1.00 11.66 ? 584  LYS A CB  1 
ATOM   4670  C  CG  . LYS A  1 584 ? -3.374  -11.692 -26.520 1.00 14.61 ? 584  LYS A CG  1 
ATOM   4671  C  CD  . LYS A  1 584 ? -2.985  -12.371 -27.852 1.00 17.17 ? 584  LYS A CD  1 
ATOM   4672  C  CE  . LYS A  1 584 ? -1.881  -11.634 -28.633 1.00 18.86 ? 584  LYS A CE  1 
ATOM   4673  N  NZ  . LYS A  1 584 ? -0.530  -11.660 -27.983 1.00 20.30 ? 584  LYS A NZ  1 
ATOM   4674  N  N   . LEU A  1 585 ? -5.363  -7.318  -25.484 1.00 4.72  ? 585  LEU A N   1 
ATOM   4675  C  CA  . LEU A  1 585 ? -5.019  -5.888  -25.577 1.00 4.65  ? 585  LEU A CA  1 
ATOM   4676  C  C   . LEU A  1 585 ? -4.407  -5.579  -26.944 1.00 2.81  ? 585  LEU A C   1 
ATOM   4677  O  O   . LEU A  1 585 ? -3.186  -5.594  -27.106 1.00 3.02  ? 585  LEU A O   1 
ATOM   4678  C  CB  . LEU A  1 585 ? -3.985  -5.468  -24.508 1.00 2.56  ? 585  LEU A CB  1 
ATOM   4679  C  CG  . LEU A  1 585 ? -3.341  -4.085  -24.756 1.00 2.00  ? 585  LEU A CG  1 
ATOM   4680  C  CD1 . LEU A  1 585 ? -4.378  -3.008  -24.528 1.00 2.00  ? 585  LEU A CD1 1 
ATOM   4681  C  CD2 . LEU A  1 585 ? -2.155  -3.846  -23.856 1.00 2.00  ? 585  LEU A CD2 1 
ATOM   4682  N  N   . ASP A  1 586 ? -5.244  -5.289  -27.924 1.00 2.00  ? 586  ASP A N   1 
ATOM   4683  C  CA  . ASP A  1 586 ? -4.737  -4.978  -29.243 1.00 3.25  ? 586  ASP A CA  1 
ATOM   4684  C  C   . ASP A  1 586 ? -4.231  -3.537  -29.291 1.00 2.00  ? 586  ASP A C   1 
ATOM   4685  O  O   . ASP A  1 586 ? -4.968  -2.606  -29.005 1.00 2.00  ? 586  ASP A O   1 
ATOM   4686  C  CB  . ASP A  1 586 ? -5.846  -5.224  -30.268 1.00 4.60  ? 586  ASP A CB  1 
ATOM   4687  C  CG  . ASP A  1 586 ? -5.587  -4.545  -31.585 1.00 6.11  ? 586  ASP A CG  1 
ATOM   4688  O  OD1 . ASP A  1 586 ? -4.402  -4.376  -31.946 1.00 7.60  ? 586  ASP A OD1 1 
ATOM   4689  O  OD2 . ASP A  1 586 ? -6.577  -4.192  -32.263 1.00 7.04  ? 586  ASP A OD2 1 
ATOM   4690  N  N   . LEU A  1 587 ? -2.961  -3.354  -29.632 1.00 2.00  ? 587  LEU A N   1 
ATOM   4691  C  CA  . LEU A  1 587 ? -2.402  -2.009  -29.706 1.00 3.70  ? 587  LEU A CA  1 
ATOM   4692  C  C   . LEU A  1 587 ? -2.517  -1.408  -31.112 1.00 4.15  ? 587  LEU A C   1 
ATOM   4693  O  O   . LEU A  1 587 ? -1.974  -0.331  -31.386 1.00 4.42  ? 587  LEU A O   1 
ATOM   4694  C  CB  . LEU A  1 587 ? -0.931  -2.010  -29.268 1.00 3.23  ? 587  LEU A CB  1 
ATOM   4695  C  CG  . LEU A  1 587 ? -0.626  -2.364  -27.807 1.00 5.17  ? 587  LEU A CG  1 
ATOM   4696  C  CD1 . LEU A  1 587 ? 0.862   -2.230  -27.560 1.00 6.88  ? 587  LEU A CD1 1 
ATOM   4697  C  CD2 . LEU A  1 587 ? -1.382  -1.444  -26.860 1.00 6.02  ? 587  LEU A CD2 1 
ATOM   4698  N  N   . SER A  1 588 ? -3.240  -2.089  -31.998 1.00 3.73  ? 588  SER A N   1 
ATOM   4699  C  CA  . SER A  1 588 ? -3.401  -1.609  -33.370 1.00 3.80  ? 588  SER A CA  1 
ATOM   4700  C  C   . SER A  1 588 ? -3.968  -0.192  -33.437 1.00 2.47  ? 588  SER A C   1 
ATOM   4701  O  O   . SER A  1 588 ? -3.636  0.579   -34.335 1.00 2.45  ? 588  SER A O   1 
ATOM   4702  C  CB  . SER A  1 588 ? -4.294  -2.561  -34.179 1.00 2.94  ? 588  SER A CB  1 
ATOM   4703  O  OG  . SER A  1 588 ? -5.664  -2.398  -33.860 1.00 3.01  ? 588  SER A OG  1 
ATOM   4704  N  N   . PRO A  1 589 ? -4.835  0.169   -32.487 1.00 3.07  ? 589  PRO A N   1 
ATOM   4705  C  CA  . PRO A  1 589 ? -5.400  1.513   -32.513 1.00 4.51  ? 589  PRO A CA  1 
ATOM   4706  C  C   . PRO A  1 589 ? -4.397  2.580   -32.090 1.00 6.30  ? 589  PRO A C   1 
ATOM   4707  O  O   . PRO A  1 589 ? -4.702  3.767   -32.143 1.00 7.46  ? 589  PRO A O   1 
ATOM   4708  C  CB  . PRO A  1 589 ? -6.577  1.404   -31.556 1.00 4.48  ? 589  PRO A CB  1 
ATOM   4709  C  CG  . PRO A  1 589 ? -6.056  0.454   -30.534 1.00 4.72  ? 589  PRO A CG  1 
ATOM   4710  C  CD  . PRO A  1 589 ? -5.422  -0.617  -31.391 1.00 3.62  ? 589  PRO A CD  1 
ATOM   4711  N  N   . TRP A  1 590 ? -3.211  2.179   -31.643 1.00 7.18  ? 590  TRP A N   1 
ATOM   4712  C  CA  . TRP A  1 590 ? -2.209  3.182   -31.277 1.00 9.79  ? 590  TRP A CA  1 
ATOM   4713  C  C   . TRP A  1 590 ? -1.348  3.466   -32.517 1.00 13.15 ? 590  TRP A C   1 
ATOM   4714  O  O   . TRP A  1 590 ? -0.415  4.273   -32.474 1.00 12.56 ? 590  TRP A O   1 
ATOM   4715  C  CB  . TRP A  1 590 ? -1.327  2.701   -30.115 1.00 6.93  ? 590  TRP A CB  1 
ATOM   4716  C  CG  . TRP A  1 590 ? -1.826  3.071   -28.728 1.00 4.65  ? 590  TRP A CG  1 
ATOM   4717  C  CD1 . TRP A  1 590 ? -1.378  4.096   -27.928 1.00 3.88  ? 590  TRP A CD1 1 
ATOM   4718  C  CD2 . TRP A  1 590 ? -2.836  2.391   -27.973 1.00 3.15  ? 590  TRP A CD2 1 
ATOM   4719  N  NE1 . TRP A  1 590 ? -2.049  4.085   -26.721 1.00 2.57  ? 590  TRP A NE1 1 
ATOM   4720  C  CE2 . TRP A  1 590 ? -2.948  3.050   -26.727 1.00 2.45  ? 590  TRP A CE2 1 
ATOM   4721  C  CE3 . TRP A  1 590 ? -3.658  1.286   -28.230 1.00 2.00  ? 590  TRP A CE3 1 
ATOM   4722  C  CZ2 . TRP A  1 590 ? -3.848  2.637   -25.746 1.00 2.46  ? 590  TRP A CZ2 1 
ATOM   4723  C  CZ3 . TRP A  1 590 ? -4.551  0.876   -27.253 1.00 2.00  ? 590  TRP A CZ3 1 
ATOM   4724  C  CH2 . TRP A  1 590 ? -4.639  1.549   -26.028 1.00 2.00  ? 590  TRP A CH2 1 
ATOM   4725  N  N   . ALA A  1 591 ? -1.689  2.799   -33.620 1.00 16.68 ? 591  ALA A N   1 
ATOM   4726  C  CA  . ALA A  1 591 ? -0.986  2.936   -34.894 1.00 20.64 ? 591  ALA A CA  1 
ATOM   4727  C  C   . ALA A  1 591 ? -1.238  4.281   -35.565 1.00 25.11 ? 591  ALA A C   1 
ATOM   4728  O  O   . ALA A  1 591 ? -2.338  4.543   -36.059 1.00 26.09 ? 591  ALA A O   1 
ATOM   4729  C  CB  . ALA A  1 591 ? -1.404  1.819   -35.828 1.00 19.48 ? 591  ALA A CB  1 
ATOM   4730  N  N   . SER A  1 592 ? -0.212  5.125   -35.589 1.00 30.18 ? 592  SER A N   1 
ATOM   4731  C  CA  . SER A  1 592 ? -0.306  6.444   -36.206 1.00 34.71 ? 592  SER A CA  1 
ATOM   4732  C  C   . SER A  1 592 ? 0.140   6.253   -37.650 1.00 38.86 ? 592  SER A C   1 
ATOM   4733  O  O   . SER A  1 592 ? 1.026   5.437   -37.919 1.00 39.31 ? 592  SER A O   1 
ATOM   4734  C  CB  . SER A  1 592 ? 0.624   7.430   -35.485 1.00 34.42 ? 592  SER A CB  1 
ATOM   4735  O  OG  . SER A  1 592 ? 0.078   8.738   -35.435 1.00 33.31 ? 592  SER A OG  1 
ATOM   4736  N  N   . ARG A  1 593 ? -0.477  6.993   -38.571 1.00 44.46 ? 593  ARG A N   1 
ATOM   4737  C  CA  . ARG A  1 593 ? -0.152  6.892   -39.995 1.00 49.50 ? 593  ARG A CA  1 
ATOM   4738  C  C   . ARG A  1 593 ? 0.008   8.247   -40.712 1.00 52.72 ? 593  ARG A C   1 
ATOM   4739  O  O   . ARG A  1 593 ? -0.962  8.976   -40.953 1.00 52.33 ? 593  ARG A O   1 
ATOM   4740  C  CB  . ARG A  1 593 ? -1.199  6.007   -40.690 1.00 50.16 ? 593  ARG A CB  1 
ATOM   4741  C  CG  . ARG A  1 593 ? -0.992  4.518   -40.387 1.00 52.49 ? 593  ARG A CG  1 
ATOM   4742  C  CD  . ARG A  1 593 ? -2.261  3.690   -40.530 1.00 54.20 ? 593  ARG A CD  1 
ATOM   4743  N  NE  . ARG A  1 593 ? -2.778  3.689   -41.894 1.00 56.99 ? 593  ARG A NE  1 
ATOM   4744  C  CZ  . ARG A  1 593 ? -3.925  3.120   -42.259 1.00 58.37 ? 593  ARG A CZ  1 
ATOM   4745  N  NH1 . ARG A  1 593 ? -4.681  2.499   -41.358 1.00 58.63 ? 593  ARG A NH1 1 
ATOM   4746  N  NH2 . ARG A  1 593 ? -4.321  3.177   -43.526 1.00 58.57 ? 593  ARG A NH2 1 
ATOM   4747  N  N   . GLU A  1 594 ? 1.268   8.543   -41.037 1.00 56.49 ? 594  GLU A N   1 
ATOM   4748  C  CA  . GLU A  1 594 ? 1.753   9.762   -41.707 1.00 59.50 ? 594  GLU A CA  1 
ATOM   4749  C  C   . GLU A  1 594 ? 0.859   10.969  -42.033 1.00 60.97 ? 594  GLU A C   1 
ATOM   4750  O  O   . GLU A  1 594 ? 0.685   11.870  -41.203 1.00 60.98 ? 594  GLU A O   1 
ATOM   4751  C  CB  . GLU A  1 594 ? 2.518   9.375   -42.990 1.00 60.87 ? 594  GLU A CB  1 
ATOM   4752  C  CG  . GLU A  1 594 ? 3.573   8.300   -42.777 1.00 62.45 ? 594  GLU A CG  1 
ATOM   4753  C  CD  . GLU A  1 594 ? 4.129   8.315   -41.362 1.00 63.52 ? 594  GLU A CD  1 
ATOM   4754  O  OE1 . GLU A  1 594 ? 4.833   9.287   -41.002 1.00 63.87 ? 594  GLU A OE1 1 
ATOM   4755  O  OE2 . GLU A  1 594 ? 3.845   7.357   -40.608 1.00 63.16 ? 594  GLU A OE2 1 
ATOM   4756  N  N   . ASN A  1 595 ? 0.324   10.985  -43.253 1.00 61.86 ? 595  ASN A N   1 
ATOM   4757  C  CA  . ASN A  1 595 ? -0.488  12.088  -43.766 1.00 62.60 ? 595  ASN A CA  1 
ATOM   4758  C  C   . ASN A  1 595 ? -1.958  12.161  -43.350 1.00 63.11 ? 595  ASN A C   1 
ATOM   4759  O  O   . ASN A  1 595 ? -2.630  13.129  -43.782 1.00 63.13 ? 595  ASN A O   1 
ATOM   4760  C  CB  . ASN A  1 595 ? -0.376  12.086  -45.291 1.00 62.82 ? 595  ASN A CB  1 
ATOM   4761  C  CG  . ASN A  1 595 ? 1.070   12.138  -45.762 1.00 63.34 ? 595  ASN A CG  1 
ATOM   4762  O  OD1 . ASN A  1 595 ? 1.641   13.215  -45.937 1.00 63.54 ? 595  ASN A OD1 1 
ATOM   4763  N  ND2 . ASN A  1 595 ? 1.677   10.967  -45.945 1.00 62.79 ? 595  ASN A ND2 1 
ATOM   4764  O  OXT . ASN A  1 595 ? -2.420  11.269  -42.605 1.00 63.13 ? 595  ASN A OXT 1 
ATOM   4765  N  N   . SER B  1 1   ? 12.305  59.387  28.808  1.00 78.30 ? 1    SER B N   1 
ATOM   4766  C  CA  . SER B  1 1   ? 11.285  58.372  29.192  1.00 78.51 ? 1    SER B CA  1 
ATOM   4767  C  C   . SER B  1 1   ? 11.924  57.078  29.711  1.00 78.35 ? 1    SER B C   1 
ATOM   4768  O  O   . SER B  1 1   ? 13.155  56.917  29.681  1.00 78.25 ? 1    SER B O   1 
ATOM   4769  C  CB  . SER B  1 1   ? 10.380  58.071  27.985  1.00 78.50 ? 1    SER B CB  1 
ATOM   4770  O  OG  . SER B  1 1   ? 9.550   56.940  28.204  1.00 77.44 ? 1    SER B OG  1 
ATOM   4771  N  N   . TRP B  1 2   ? 11.054  56.185  30.190  1.00 78.46 ? 2    TRP B N   1 
ATOM   4772  C  CA  . TRP B  1 2   ? 11.389  54.865  30.743  1.00 79.03 ? 2    TRP B CA  1 
ATOM   4773  C  C   . TRP B  1 2   ? 10.655  53.762  29.963  1.00 79.01 ? 2    TRP B C   1 
ATOM   4774  O  O   . TRP B  1 2   ? 9.626   53.260  30.432  1.00 79.04 ? 2    TRP B O   1 
ATOM   4775  C  CB  . TRP B  1 2   ? 10.935  54.757  32.205  1.00 77.64 ? 2    TRP B CB  1 
ATOM   4776  C  CG  . TRP B  1 2   ? 11.976  54.995  33.244  1.00 76.86 ? 2    TRP B CG  1 
ATOM   4777  C  CD1 . TRP B  1 2   ? 12.719  54.056  33.907  1.00 76.35 ? 2    TRP B CD1 1 
ATOM   4778  C  CD2 . TRP B  1 2   ? 12.373  56.259  33.765  1.00 76.82 ? 2    TRP B CD2 1 
ATOM   4779  N  NE1 . TRP B  1 2   ? 13.553  54.661  34.814  1.00 76.17 ? 2    TRP B NE1 1 
ATOM   4780  C  CE2 . TRP B  1 2   ? 13.362  56.016  34.746  1.00 76.50 ? 2    TRP B CE2 1 
ATOM   4781  C  CE3 . TRP B  1 2   ? 11.989  57.582  33.498  1.00 76.32 ? 2    TRP B CE3 1 
ATOM   4782  C  CZ2 . TRP B  1 2   ? 13.972  57.049  35.462  1.00 76.17 ? 2    TRP B CZ2 1 
ATOM   4783  C  CZ3 . TRP B  1 2   ? 12.595  58.609  34.211  1.00 75.80 ? 2    TRP B CZ3 1 
ATOM   4784  C  CH2 . TRP B  1 2   ? 13.576  58.336  35.182  1.00 75.77 ? 2    TRP B CH2 1 
ATOM   4785  N  N   . GLU B  1 3   ? 11.157  53.396  28.783  1.00 78.60 ? 3    GLU B N   1 
ATOM   4786  C  CA  . GLU B  1 3   ? 10.552  52.315  28.000  1.00 78.04 ? 3    GLU B CA  1 
ATOM   4787  C  C   . GLU B  1 3   ? 11.109  51.060  28.635  1.00 78.48 ? 3    GLU B C   1 
ATOM   4788  O  O   . GLU B  1 3   ? 11.479  50.121  27.925  1.00 78.77 ? 3    GLU B O   1 
ATOM   4789  C  CB  . GLU B  1 3   ? 11.019  52.332  26.545  1.00 78.09 ? 3    GLU B CB  1 
ATOM   4790  C  CG  . GLU B  1 3   ? 10.104  51.568  25.592  1.00 77.61 ? 3    GLU B CG  1 
ATOM   4791  C  CD  . GLU B  1 3   ? 10.845  50.633  24.636  1.00 77.50 ? 3    GLU B CD  1 
ATOM   4792  O  OE1 . GLU B  1 3   ? 11.065  49.458  25.000  1.00 77.45 ? 3    GLU B OE1 1 
ATOM   4793  O  OE2 . GLU B  1 3   ? 11.207  51.070  23.523  1.00 77.04 ? 3    GLU B OE2 1 
ATOM   4794  N  N   . VAL B  1 4   ? 11.220  51.072  29.966  1.00 78.34 ? 4    VAL B N   1 
ATOM   4795  C  CA  . VAL B  1 4   ? 11.750  49.938  30.709  1.00 77.36 ? 4    VAL B CA  1 
ATOM   4796  C  C   . VAL B  1 4   ? 10.995  48.677  30.286  1.00 77.11 ? 4    VAL B C   1 
ATOM   4797  O  O   . VAL B  1 4   ? 10.145  48.161  31.008  1.00 76.46 ? 4    VAL B O   1 
ATOM   4798  C  CB  . VAL B  1 4   ? 11.612  50.168  32.225  1.00 77.18 ? 4    VAL B CB  1 
ATOM   4799  C  CG1 . VAL B  1 4   ? 12.396  51.385  32.609  1.00 77.00 ? 4    VAL B CG1 1 
ATOM   4800  C  CG2 . VAL B  1 4   ? 10.147  50.329  32.614  1.00 77.63 ? 4    VAL B CG2 1 
ATOM   4801  N  N   . GLY B  1 5   ? 11.370  48.140  29.152  1.00 76.92 ? 5    GLY B N   1 
ATOM   4802  C  CA  . GLY B  1 5   ? 10.812  46.970  28.589  1.00 75.97 ? 5    GLY B CA  1 
ATOM   4803  C  C   . GLY B  1 5   ? 10.175  45.874  29.473  1.00 74.83 ? 5    GLY B C   1 
ATOM   4804  O  O   . GLY B  1 5   ? 8.944   45.863  29.657  1.00 75.33 ? 5    GLY B O   1 
ATOM   4805  N  N   . CYS B  1 6   ? 10.976  44.871  29.987  1.00 72.65 ? 6    CYS B N   1 
ATOM   4806  C  CA  . CYS B  1 6   ? 10.451  43.683  30.745  1.00 70.63 ? 6    CYS B CA  1 
ATOM   4807  C  C   . CYS B  1 6   ? 11.148  43.383  32.110  1.00 71.42 ? 6    CYS B C   1 
ATOM   4808  O  O   . CYS B  1 6   ? 12.186  44.003  32.394  1.00 72.11 ? 6    CYS B O   1 
ATOM   4809  C  CB  . CYS B  1 6   ? 10.474  42.434  29.844  1.00 66.25 ? 6    CYS B CB  1 
ATOM   4810  S  SG  . CYS B  1 6   ? 12.144  41.844  29.416  1.00 60.04 ? 6    CYS B SG  1 
ATOM   4811  N  N   . GLY B  1 7   ? 10.656  42.451  32.997  1.00 72.03 ? 7    GLY B N   1 
ATOM   4812  C  CA  . GLY B  1 7   ? 11.157  42.428  34.402  1.00 72.28 ? 7    GLY B CA  1 
ATOM   4813  C  C   . GLY B  1 7   ? 12.226  41.546  35.087  1.00 71.94 ? 7    GLY B C   1 
ATOM   4814  O  O   . GLY B  1 7   ? 13.380  41.972  35.242  1.00 71.67 ? 7    GLY B O   1 
ATOM   4815  N  N   . ALA B  1 8   ? 11.857  40.315  35.498  1.00 71.48 ? 8    ALA B N   1 
ATOM   4816  C  CA  . ALA B  1 8   ? 12.767  39.522  36.337  1.00 70.17 ? 8    ALA B CA  1 
ATOM   4817  C  C   . ALA B  1 8   ? 12.222  38.365  37.162  1.00 69.10 ? 8    ALA B C   1 
ATOM   4818  O  O   . ALA B  1 8   ? 11.091  38.453  37.665  1.00 68.99 ? 8    ALA B O   1 
ATOM   4819  C  CB  . ALA B  1 8   ? 13.532  40.442  37.369  1.00 69.52 ? 8    ALA B CB  1 
ATOM   4820  N  N   . PRO B  1 9   ? 13.032  37.265  37.232  1.00 68.25 ? 9    PRO B N   1 
ATOM   4821  C  CA  . PRO B  1 9   ? 12.499  36.203  38.075  1.00 67.25 ? 9    PRO B CA  1 
ATOM   4822  C  C   . PRO B  1 9   ? 12.747  36.804  39.538  1.00 65.47 ? 9    PRO B C   1 
ATOM   4823  O  O   . PRO B  1 9   ? 11.850  37.431  40.171  1.00 65.82 ? 9    PRO B O   1 
ATOM   4824  C  CB  . PRO B  1 9   ? 13.411  35.001  37.829  1.00 67.63 ? 9    PRO B CB  1 
ATOM   4825  C  CG  . PRO B  1 9   ? 14.833  35.622  37.466  1.00 68.10 ? 9    PRO B CG  1 
ATOM   4826  C  CD  . PRO B  1 9   ? 14.488  37.141  37.039  1.00 68.16 ? 9    PRO B CD  1 
ATOM   4827  N  N   . VAL B  1 10  ? 13.991  36.604  40.016  1.00 62.56 ? 10   VAL B N   1 
ATOM   4828  C  CA  . VAL B  1 10  ? 14.613  37.110  41.258  1.00 58.30 ? 10   VAL B CA  1 
ATOM   4829  C  C   . VAL B  1 10  ? 14.092  36.679  42.631  1.00 56.30 ? 10   VAL B C   1 
ATOM   4830  O  O   . VAL B  1 10  ? 12.941  36.955  42.998  1.00 56.96 ? 10   VAL B O   1 
ATOM   4831  C  CB  . VAL B  1 10  ? 14.604  38.654  41.291  1.00 57.78 ? 10   VAL B CB  1 
ATOM   4832  C  CG1 . VAL B  1 10  ? 14.728  39.194  39.871  1.00 56.40 ? 10   VAL B CG1 1 
ATOM   4833  C  CG2 . VAL B  1 10  ? 13.355  39.186  41.984  1.00 56.88 ? 10   VAL B CG2 1 
ATOM   4834  N  N   . PRO B  1 11  ? 14.980  36.008  43.363  1.00 54.33 ? 11   PRO B N   1 
ATOM   4835  C  CA  . PRO B  1 11  ? 14.662  35.784  44.790  1.00 52.19 ? 11   PRO B CA  1 
ATOM   4836  C  C   . PRO B  1 11  ? 14.329  37.099  45.453  1.00 50.84 ? 11   PRO B C   1 
ATOM   4837  O  O   . PRO B  1 11  ? 15.241  37.910  45.670  1.00 50.43 ? 11   PRO B O   1 
ATOM   4838  C  CB  . PRO B  1 11  ? 15.872  35.058  45.305  1.00 51.73 ? 11   PRO B CB  1 
ATOM   4839  C  CG  . PRO B  1 11  ? 16.139  34.157  44.121  1.00 52.65 ? 11   PRO B CG  1 
ATOM   4840  C  CD  . PRO B  1 11  ? 15.565  34.756  42.875  1.00 53.90 ? 11   PRO B CD  1 
ATOM   4841  N  N   . LEU B  1 12  ? 13.095  37.382  45.805  1.00 49.91 ? 12   LEU B N   1 
ATOM   4842  C  CA  . LEU B  1 12  ? 12.755  38.636  46.457  1.00 49.46 ? 12   LEU B CA  1 
ATOM   4843  C  C   . LEU B  1 12  ? 12.936  38.659  47.986  1.00 49.03 ? 12   LEU B C   1 
ATOM   4844  O  O   . LEU B  1 12  ? 12.079  38.179  48.732  1.00 49.83 ? 12   LEU B O   1 
ATOM   4845  C  CB  . LEU B  1 12  ? 11.312  38.998  46.076  1.00 49.00 ? 12   LEU B CB  1 
ATOM   4846  C  CG  . LEU B  1 12  ? 10.616  40.215  46.681  1.00 48.89 ? 12   LEU B CG  1 
ATOM   4847  C  CD1 . LEU B  1 12  ? 9.906   40.982  45.575  1.00 48.49 ? 12   LEU B CD1 1 
ATOM   4848  C  CD2 . LEU B  1 12  ? 9.629   39.761  47.752  1.00 47.92 ? 12   LEU B CD2 1 
ATOM   4849  N  N   . VAL B  1 13  ? 14.057  39.220  48.446  1.00 48.24 ? 13   VAL B N   1 
ATOM   4850  C  CA  . VAL B  1 13  ? 14.336  39.340  49.883  1.00 48.38 ? 13   VAL B CA  1 
ATOM   4851  C  C   . VAL B  1 13  ? 13.856  40.697  50.393  1.00 48.73 ? 13   VAL B C   1 
ATOM   4852  O  O   . VAL B  1 13  ? 13.741  41.661  49.623  1.00 49.34 ? 13   VAL B O   1 
ATOM   4853  C  CB  . VAL B  1 13  ? 15.845  39.230  50.216  1.00 48.01 ? 13   VAL B CB  1 
ATOM   4854  C  CG1 . VAL B  1 13  ? 16.203  37.799  50.577  1.00 48.52 ? 13   VAL B CG1 1 
ATOM   4855  C  CG2 . VAL B  1 13  ? 16.699  39.707  49.040  1.00 48.36 ? 13   VAL B CG2 1 
ATOM   4856  N  N   . LYS B  1 14  ? 13.595  40.766  51.697  1.00 47.15 ? 14   LYS B N   1 
ATOM   4857  C  CA  . LYS B  1 14  ? 13.106  41.986  52.328  1.00 44.57 ? 14   LYS B CA  1 
ATOM   4858  C  C   . LYS B  1 14  ? 14.118  42.645  53.245  1.00 42.03 ? 14   LYS B C   1 
ATOM   4859  O  O   . LYS B  1 14  ? 13.764  43.553  54.000  1.00 43.50 ? 14   LYS B O   1 
ATOM   4860  C  CB  . LYS B  1 14  ? 11.824  41.658  53.119  1.00 46.03 ? 14   LYS B CB  1 
ATOM   4861  C  CG  . LYS B  1 14  ? 12.042  40.615  54.208  1.00 46.69 ? 14   LYS B CG  1 
ATOM   4862  C  CD  . LYS B  1 14  ? 11.052  40.812  55.352  1.00 48.04 ? 14   LYS B CD  1 
ATOM   4863  C  CE  . LYS B  1 14  ? 10.654  39.475  55.969  1.00 48.39 ? 14   LYS B CE  1 
ATOM   4864  N  NZ  . LYS B  1 14  ? 9.870   38.632  55.014  1.00 48.13 ? 14   LYS B NZ  1 
ATOM   4865  N  N   . CYS B  1 15  ? 15.366  42.194  53.168  1.00 37.96 ? 15   CYS B N   1 
ATOM   4866  C  CA  . CYS B  1 15  ? 16.422  42.708  54.032  1.00 35.08 ? 15   CYS B CA  1 
ATOM   4867  C  C   . CYS B  1 15  ? 16.184  42.295  55.452  1.00 35.94 ? 15   CYS B C   1 
ATOM   4868  O  O   . CYS B  1 15  ? 15.159  41.699  55.744  1.00 36.77 ? 15   CYS B O   1 
ATOM   4869  C  CB  . CYS B  1 15  ? 16.512  44.222  53.870  1.00 29.72 ? 15   CYS B CB  1 
ATOM   4870  S  SG  . CYS B  1 15  ? 16.917  44.776  52.184  1.00 19.82 ? 15   CYS B SG  1 
ATOM   4871  N  N   . ASP B  1 16  ? 17.076  42.576  56.354  1.00 36.36 ? 16   ASP B N   1 
ATOM   4872  C  CA  . ASP B  1 16  ? 16.734  42.408  57.737  1.00 36.76 ? 16   ASP B CA  1 
ATOM   4873  C  C   . ASP B  1 16  ? 16.503  43.859  58.100  1.00 36.98 ? 16   ASP B C   1 
ATOM   4874  O  O   . ASP B  1 16  ? 15.384  44.379  58.083  1.00 37.77 ? 16   ASP B O   1 
ATOM   4875  C  CB  . ASP B  1 16  ? 17.806  41.836  58.671  1.00 37.54 ? 16   ASP B CB  1 
ATOM   4876  C  CG  . ASP B  1 16  ? 17.732  42.397  60.093  1.00 37.47 ? 16   ASP B CG  1 
ATOM   4877  O  OD1 . ASP B  1 16  ? 16.628  42.739  60.540  1.00 37.17 ? 16   ASP B OD1 1 
ATOM   4878  O  OD2 . ASP B  1 16  ? 18.797  42.498  60.733  1.00 37.35 ? 16   ASP B OD2 1 
ATOM   4879  N  N   . GLU B  1 17  ? 17.604  44.503  58.421  1.00 36.33 ? 17   GLU B N   1 
ATOM   4880  C  CA  . GLU B  1 17  ? 17.627  45.897  58.710  1.00 36.36 ? 17   GLU B CA  1 
ATOM   4881  C  C   . GLU B  1 17  ? 18.895  46.293  59.435  1.00 34.33 ? 17   GLU B C   1 
ATOM   4882  O  O   . GLU B  1 17  ? 19.804  46.883  58.852  1.00 35.18 ? 17   GLU B O   1 
ATOM   4883  C  CB  . GLU B  1 17  ? 16.418  46.313  59.547  1.00 38.31 ? 17   GLU B CB  1 
ATOM   4884  C  CG  . GLU B  1 17  ? 16.203  47.811  59.547  1.00 43.44 ? 17   GLU B CG  1 
ATOM   4885  C  CD  . GLU B  1 17  ? 16.753  48.474  58.282  1.00 45.73 ? 17   GLU B CD  1 
ATOM   4886  O  OE1 . GLU B  1 17  ? 17.984  48.710  58.223  1.00 46.80 ? 17   GLU B OE1 1 
ATOM   4887  O  OE2 . GLU B  1 17  ? 15.961  48.743  57.347  1.00 46.91 ? 17   GLU B OE2 1 
ATOM   4888  N  N   . ASN B  1 18  ? 18.949  45.962  60.715  1.00 31.13 ? 18   ASN B N   1 
ATOM   4889  C  CA  . ASN B  1 18  ? 20.107  46.286  61.528  1.00 28.95 ? 18   ASN B CA  1 
ATOM   4890  C  C   . ASN B  1 18  ? 21.219  45.227  61.499  1.00 25.91 ? 18   ASN B C   1 
ATOM   4891  O  O   . ASN B  1 18  ? 22.355  45.526  61.856  1.00 26.74 ? 18   ASN B O   1 
ATOM   4892  C  CB  . ASN B  1 18  ? 19.658  46.515  62.977  1.00 31.35 ? 18   ASN B CB  1 
ATOM   4893  C  CG  . ASN B  1 18  ? 19.602  47.987  63.349  1.00 32.58 ? 18   ASN B CG  1 
ATOM   4894  O  OD1 . ASN B  1 18  ? 18.805  48.393  64.199  1.00 32.25 ? 18   ASN B OD1 1 
ATOM   4895  N  ND2 . ASN B  1 18  ? 20.464  48.791  62.730  1.00 32.71 ? 18   ASN B ND2 1 
ATOM   4896  N  N   . SER B  1 19  ? 20.908  44.007  61.064  1.00 21.35 ? 19   SER B N   1 
ATOM   4897  C  CA  . SER B  1 19  ? 21.893  42.919  61.046  1.00 16.10 ? 19   SER B CA  1 
ATOM   4898  C  C   . SER B  1 19  ? 23.324  43.250  60.647  1.00 11.80 ? 19   SER B C   1 
ATOM   4899  O  O   . SER B  1 19  ? 23.569  43.944  59.668  1.00 10.30 ? 19   SER B O   1 
ATOM   4900  C  CB  . SER B  1 19  ? 21.417  41.770  60.160  1.00 16.74 ? 19   SER B CB  1 
ATOM   4901  O  OG  . SER B  1 19  ? 22.396  40.742  60.132  1.00 17.28 ? 19   SER B OG  1 
ATOM   4902  N  N   . PRO B  1 20  ? 24.294  42.746  61.418  1.00 10.11 ? 20   PRO B N   1 
ATOM   4903  C  CA  . PRO B  1 20  ? 25.720  42.966  61.160  1.00 10.25 ? 20   PRO B CA  1 
ATOM   4904  C  C   . PRO B  1 20  ? 26.237  41.977  60.116  1.00 9.57  ? 20   PRO B C   1 
ATOM   4905  O  O   . PRO B  1 20  ? 27.454  41.822  59.968  1.00 10.06 ? 20   PRO B O   1 
ATOM   4906  C  CB  . PRO B  1 20  ? 26.381  42.695  62.519  1.00 10.37 ? 20   PRO B CB  1 
ATOM   4907  C  CG  . PRO B  1 20  ? 25.273  42.850  63.515  1.00 11.56 ? 20   PRO B CG  1 
ATOM   4908  C  CD  . PRO B  1 20  ? 24.090  42.251  62.789  1.00 11.57 ? 20   PRO B CD  1 
ATOM   4909  N  N   . TYR B  1 21  ? 25.326  41.314  59.399  1.00 6.92  ? 21   TYR B N   1 
ATOM   4910  C  CA  . TYR B  1 21  ? 25.729  40.309  58.417  1.00 3.51  ? 21   TYR B CA  1 
ATOM   4911  C  C   . TYR B  1 21  ? 25.275  40.488  56.966  1.00 2.78  ? 21   TYR B C   1 
ATOM   4912  O  O   . TYR B  1 21  ? 24.239  41.088  56.698  1.00 4.09  ? 21   TYR B O   1 
ATOM   4913  C  CB  . TYR B  1 21  ? 25.306  38.936  58.938  1.00 2.35  ? 21   TYR B CB  1 
ATOM   4914  C  CG  . TYR B  1 21  ? 25.911  38.621  60.293  1.00 2.43  ? 21   TYR B CG  1 
ATOM   4915  C  CD1 . TYR B  1 21  ? 27.287  38.692  60.491  1.00 2.96  ? 21   TYR B CD1 1 
ATOM   4916  C  CD2 . TYR B  1 21  ? 25.114  38.274  61.379  1.00 2.71  ? 21   TYR B CD2 1 
ATOM   4917  C  CE1 . TYR B  1 21  ? 27.857  38.429  61.729  1.00 2.30  ? 21   TYR B CE1 1 
ATOM   4918  C  CE2 . TYR B  1 21  ? 25.676  38.008  62.630  1.00 2.46  ? 21   TYR B CE2 1 
ATOM   4919  C  CZ  . TYR B  1 21  ? 27.054  38.086  62.794  1.00 2.50  ? 21   TYR B CZ  1 
ATOM   4920  O  OH  . TYR B  1 21  ? 27.645  37.806  64.009  1.00 2.75  ? 21   TYR B OH  1 
ATOM   4921  N  N   . ARG B  1 22  ? 26.077  39.959  56.040  1.00 2.87  ? 22   ARG B N   1 
ATOM   4922  C  CA  . ARG B  1 22  ? 25.812  40.020  54.592  1.00 3.56  ? 22   ARG B CA  1 
ATOM   4923  C  C   . ARG B  1 22  ? 24.740  39.014  54.157  1.00 2.62  ? 22   ARG B C   1 
ATOM   4924  O  O   . ARG B  1 22  ? 24.732  37.880  54.636  1.00 3.04  ? 22   ARG B O   1 
ATOM   4925  C  CB  . ARG B  1 22  ? 27.081  39.672  53.791  1.00 3.47  ? 22   ARG B CB  1 
ATOM   4926  C  CG  . ARG B  1 22  ? 28.173  40.734  53.658  1.00 3.07  ? 22   ARG B CG  1 
ATOM   4927  C  CD  . ARG B  1 22  ? 29.320  40.190  52.784  1.00 2.00  ? 22   ARG B CD  1 
ATOM   4928  N  NE  . ARG B  1 22  ? 30.407  41.147  52.565  1.00 2.05  ? 22   ARG B NE  1 
ATOM   4929  C  CZ  . ARG B  1 22  ? 30.338  42.193  51.747  1.00 2.00  ? 22   ARG B CZ  1 
ATOM   4930  N  NH1 . ARG B  1 22  ? 29.233  42.422  51.059  1.00 2.00  ? 22   ARG B NH1 1 
ATOM   4931  N  NH2 . ARG B  1 22  ? 31.368  43.017  51.625  1.00 2.00  ? 22   ARG B NH2 1 
ATOM   4932  N  N   . THR B  1 23  ? 23.856  39.403  53.240  1.00 2.00  ? 23   THR B N   1 
ATOM   4933  C  CA  . THR B  1 23  ? 22.849  38.455  52.770  1.00 2.20  ? 23   THR B CA  1 
ATOM   4934  C  C   . THR B  1 23  ? 23.538  37.621  51.704  1.00 2.79  ? 23   THR B C   1 
ATOM   4935  O  O   . THR B  1 23  ? 24.566  38.022  51.169  1.00 2.56  ? 23   THR B O   1 
ATOM   4936  C  CB  . THR B  1 23  ? 21.653  39.125  52.094  1.00 2.00  ? 23   THR B CB  1 
ATOM   4937  O  OG1 . THR B  1 23  ? 21.974  39.400  50.725  1.00 2.00  ? 23   THR B OG1 1 
ATOM   4938  C  CG2 . THR B  1 23  ? 21.306  40.411  52.786  1.00 3.46  ? 23   THR B CG2 1 
ATOM   4939  N  N   . ILE B  1 24  ? 22.968  36.464  51.394  1.00 4.17  ? 24   ILE B N   1 
ATOM   4940  C  CA  . ILE B  1 24  ? 23.532  35.581  50.378  1.00 2.17  ? 24   ILE B CA  1 
ATOM   4941  C  C   . ILE B  1 24  ? 23.305  36.184  48.994  1.00 2.62  ? 24   ILE B C   1 
ATOM   4942  O  O   . ILE B  1 24  ? 24.252  36.437  48.255  1.00 2.59  ? 24   ILE B O   1 
ATOM   4943  C  CB  . ILE B  1 24  ? 22.879  34.181  50.452  1.00 2.30  ? 24   ILE B CB  1 
ATOM   4944  C  CG1 . ILE B  1 24  ? 23.386  33.440  51.696  1.00 2.29  ? 24   ILE B CG1 1 
ATOM   4945  C  CG2 . ILE B  1 24  ? 23.149  33.402  49.175  1.00 2.00  ? 24   ILE B CG2 1 
ATOM   4946  C  CD1 . ILE B  1 24  ? 24.882  33.207  51.716  1.00 2.00  ? 24   ILE B CD1 1 
ATOM   4947  N  N   . THR B  1 25  ? 22.035  36.404  48.662  1.00 3.13  ? 25   THR B N   1 
ATOM   4948  C  CA  . THR B  1 25  ? 21.620  36.991  47.394  1.00 2.25  ? 25   THR B CA  1 
ATOM   4949  C  C   . THR B  1 25  ? 22.433  38.247  47.076  1.00 3.30  ? 25   THR B C   1 
ATOM   4950  O  O   . THR B  1 25  ? 22.702  38.552  45.915  1.00 2.32  ? 25   THR B O   1 
ATOM   4951  C  CB  . THR B  1 25  ? 20.124  37.349  47.451  1.00 3.45  ? 25   THR B CB  1 
ATOM   4952  O  OG1 . THR B  1 25  ? 19.793  38.247  46.383  1.00 6.19  ? 25   THR B OG1 1 
ATOM   4953  C  CG2 . THR B  1 25  ? 19.793  37.997  48.784  1.00 2.69  ? 25   THR B CG2 1 
ATOM   4954  N  N   . GLY B  1 26  ? 22.822  38.982  48.110  1.00 3.58  ? 26   GLY B N   1 
ATOM   4955  C  CA  . GLY B  1 26  ? 23.618  40.178  47.884  1.00 4.41  ? 26   GLY B CA  1 
ATOM   4956  C  C   . GLY B  1 26  ? 22.860  41.468  48.116  1.00 4.29  ? 26   GLY B C   1 
ATOM   4957  O  O   . GLY B  1 26  ? 23.437  42.557  48.109  1.00 4.14  ? 26   GLY B O   1 
ATOM   4958  N  N   . ASP B  1 27  ? 21.558  41.330  48.330  1.00 3.31  ? 27   ASP B N   1 
ATOM   4959  C  CA  . ASP B  1 27  ? 20.685  42.462  48.570  1.00 2.50  ? 27   ASP B CA  1 
ATOM   4960  C  C   . ASP B  1 27  ? 21.005  43.228  49.840  1.00 2.07  ? 27   ASP B C   1 
ATOM   4961  O  O   . ASP B  1 27  ? 21.808  42.801  50.668  1.00 2.00  ? 27   ASP B O   1 
ATOM   4962  C  CB  . ASP B  1 27  ? 19.237  41.983  48.653  1.00 2.52  ? 27   ASP B CB  1 
ATOM   4963  C  CG  . ASP B  1 27  ? 18.631  41.720  47.294  1.00 4.30  ? 27   ASP B CG  1 
ATOM   4964  O  OD1 . ASP B  1 27  ? 18.446  42.705  46.544  1.00 6.08  ? 27   ASP B OD1 1 
ATOM   4965  O  OD2 . ASP B  1 27  ? 18.342  40.542  46.972  1.00 3.32  ? 27   ASP B OD2 1 
ATOM   4966  N  N   . CYS B  1 28  ? 20.366  44.387  49.950  1.00 4.90  ? 28   CYS B N   1 
ATOM   4967  C  CA  . CYS B  1 28  ? 20.442  45.256  51.114  1.00 5.31  ? 28   CYS B CA  1 
ATOM   4968  C  C   . CYS B  1 28  ? 21.742  45.914  51.458  1.00 3.08  ? 28   CYS B C   1 
ATOM   4969  O  O   . CYS B  1 28  ? 21.800  46.699  52.399  1.00 2.00  ? 28   CYS B O   1 
ATOM   4970  C  CB  . CYS B  1 28  ? 19.936  44.479  52.311  1.00 11.07 ? 28   CYS B CB  1 
ATOM   4971  S  SG  . CYS B  1 28  ? 18.484  43.513  51.804  1.00 20.36 ? 28   CYS B SG  1 
ATOM   4972  N  N   . ASN B  1 29  ? 22.790  45.601  50.716  1.00 3.49  ? 29   ASN B N   1 
ATOM   4973  C  CA  . ASN B  1 29  ? 24.067  46.235  50.990  1.00 4.72  ? 29   ASN B CA  1 
ATOM   4974  C  C   . ASN B  1 29  ? 23.765  47.736  50.938  1.00 2.95  ? 29   ASN B C   1 
ATOM   4975  O  O   . ASN B  1 29  ? 24.346  48.544  51.666  1.00 3.00  ? 29   ASN B O   1 
ATOM   4976  C  CB  . ASN B  1 29  ? 25.091  45.822  49.919  1.00 3.38  ? 29   ASN B CB  1 
ATOM   4977  C  CG  . ASN B  1 29  ? 26.439  46.483  50.109  1.00 3.37  ? 29   ASN B CG  1 
ATOM   4978  O  OD1 . ASN B  1 29  ? 26.562  47.698  49.993  1.00 6.23  ? 29   ASN B OD1 1 
ATOM   4979  N  ND2 . ASN B  1 29  ? 27.457  45.689  50.398  1.00 2.00  ? 29   ASN B ND2 1 
ATOM   4980  N  N   . ASN B  1 30  ? 22.792  48.080  50.101  1.00 3.60  ? 30   ASN B N   1 
ATOM   4981  C  CA  . ASN B  1 30  ? 22.384  49.460  49.912  1.00 2.97  ? 30   ASN B CA  1 
ATOM   4982  C  C   . ASN B  1 30  ? 20.975  49.772  50.443  1.00 4.06  ? 30   ASN B C   1 
ATOM   4983  O  O   . ASN B  1 30  ? 19.988  49.137  50.063  1.00 3.76  ? 30   ASN B O   1 
ATOM   4984  C  CB  . ASN B  1 30  ? 22.464  49.790  48.433  1.00 2.53  ? 30   ASN B CB  1 
ATOM   4985  C  CG  . ASN B  1 30  ? 22.166  51.222  48.155  1.00 2.56  ? 30   ASN B CG  1 
ATOM   4986  O  OD1 . ASN B  1 30  ? 21.124  51.732  48.558  1.00 5.28  ? 30   ASN B OD1 1 
ATOM   4987  N  ND2 . ASN B  1 30  ? 23.076  51.894  47.460  1.00 2.00  ? 30   ASN B ND2 1 
ATOM   4988  N  N   . ARG B  1 31  ? 20.891  50.775  51.310  1.00 4.81  ? 31   ARG B N   1 
ATOM   4989  C  CA  . ARG B  1 31  ? 19.623  51.163  51.902  1.00 5.10  ? 31   ARG B CA  1 
ATOM   4990  C  C   . ARG B  1 31  ? 18.661  51.875  50.936  1.00 7.94  ? 31   ARG B C   1 
ATOM   4991  O  O   . ARG B  1 31  ? 17.464  51.574  50.932  1.00 8.35  ? 31   ARG B O   1 
ATOM   4992  C  CB  . ARG B  1 31  ? 19.886  52.005  53.166  1.00 5.71  ? 31   ARG B CB  1 
ATOM   4993  C  CG  . ARG B  1 31  ? 20.346  51.151  54.363  1.00 5.68  ? 31   ARG B CG  1 
ATOM   4994  C  CD  . ARG B  1 31  ? 20.810  51.935  55.605  1.00 5.31  ? 31   ARG B CD  1 
ATOM   4995  N  NE  . ARG B  1 31  ? 20.867  51.052  56.780  1.00 7.89  ? 31   ARG B NE  1 
ATOM   4996  C  CZ  . ARG B  1 31  ? 21.841  51.043  57.693  1.00 9.01  ? 31   ARG B CZ  1 
ATOM   4997  N  NH1 . ARG B  1 31  ? 22.869  51.876  57.584  1.00 9.95  ? 31   ARG B NH1 1 
ATOM   4998  N  NH2 . ARG B  1 31  ? 21.796  50.189  58.715  1.00 7.08  ? 31   ARG B NH2 1 
ATOM   4999  N  N   . ARG B  1 32  ? 19.151  52.798  50.106  1.00 8.93  ? 32   ARG B N   1 
ATOM   5000  C  CA  . ARG B  1 32  ? 18.244  53.478  49.177  1.00 9.56  ? 32   ARG B CA  1 
ATOM   5001  C  C   . ARG B  1 32  ? 17.841  52.633  47.973  1.00 8.63  ? 32   ARG B C   1 
ATOM   5002  O  O   . ARG B  1 32  ? 16.761  52.815  47.419  1.00 9.57  ? 32   ARG B O   1 
ATOM   5003  C  CB  . ARG B  1 32  ? 18.820  54.821  48.702  1.00 12.74 ? 32   ARG B CB  1 
ATOM   5004  C  CG  . ARG B  1 32  ? 18.238  56.010  49.492  1.00 18.80 ? 32   ARG B CG  1 
ATOM   5005  C  CD  . ARG B  1 32  ? 18.406  57.381  48.812  1.00 20.99 ? 32   ARG B CD  1 
ATOM   5006  N  NE  . ARG B  1 32  ? 19.361  58.254  49.502  1.00 23.27 ? 32   ARG B NE  1 
ATOM   5007  C  CZ  . ARG B  1 32  ? 20.635  58.397  49.147  1.00 24.17 ? 32   ARG B CZ  1 
ATOM   5008  N  NH1 . ARG B  1 32  ? 21.120  57.727  48.105  1.00 24.57 ? 32   ARG B NH1 1 
ATOM   5009  N  NH2 . ARG B  1 32  ? 21.426  59.212  49.830  1.00 25.47 ? 32   ARG B NH2 1 
ATOM   5010  N  N   . SER B  1 33  ? 18.702  51.707  47.575  1.00 7.43  ? 33   SER B N   1 
ATOM   5011  C  CA  . SER B  1 33  ? 18.419  50.832  46.447  1.00 6.88  ? 33   SER B CA  1 
ATOM   5012  C  C   . SER B  1 33  ? 18.980  49.474  46.825  1.00 6.82  ? 33   SER B C   1 
ATOM   5013  O  O   . SER B  1 33  ? 20.165  49.207  46.649  1.00 7.43  ? 33   SER B O   1 
ATOM   5014  C  CB  . SER B  1 33  ? 19.100  51.355  45.189  1.00 6.76  ? 33   SER B CB  1 
ATOM   5015  O  OG  . SER B  1 33  ? 18.198  51.349  44.099  1.00 9.11  ? 33   SER B OG  1 
ATOM   5016  N  N   . PRO B  1 34  ? 18.126  48.599  47.363  1.00 6.37  ? 34   PRO B N   1 
ATOM   5017  C  CA  . PRO B  1 34  ? 18.423  47.232  47.820  1.00 5.82  ? 34   PRO B CA  1 
ATOM   5018  C  C   . PRO B  1 34  ? 19.056  46.297  46.790  1.00 5.71  ? 34   PRO B C   1 
ATOM   5019  O  O   . PRO B  1 34  ? 20.230  45.946  46.905  1.00 6.02  ? 34   PRO B O   1 
ATOM   5020  C  CB  . PRO B  1 34  ? 17.065  46.726  48.296  1.00 7.03  ? 34   PRO B CB  1 
ATOM   5021  C  CG  . PRO B  1 34  ? 16.338  48.012  48.683  1.00 8.63  ? 34   PRO B CG  1 
ATOM   5022  C  CD  . PRO B  1 34  ? 16.702  48.918  47.547  1.00 6.83  ? 34   PRO B CD  1 
ATOM   5023  N  N   . ALA B  1 35  ? 18.271  45.891  45.796  1.00 3.68  ? 35   ALA B N   1 
ATOM   5024  C  CA  . ALA B  1 35  ? 18.738  44.994  44.739  1.00 3.31  ? 35   ALA B CA  1 
ATOM   5025  C  C   . ALA B  1 35  ? 19.965  45.501  43.984  1.00 4.39  ? 35   ALA B C   1 
ATOM   5026  O  O   . ALA B  1 35  ? 20.469  44.822  43.085  1.00 5.13  ? 35   ALA B O   1 
ATOM   5027  C  CB  . ALA B  1 35  ? 17.617  44.740  43.754  1.00 2.54  ? 35   ALA B CB  1 
ATOM   5028  N  N   . LEU B  1 36  ? 20.439  46.691  44.332  1.00 4.37  ? 36   LEU B N   1 
ATOM   5029  C  CA  . LEU B  1 36  ? 21.604  47.262  43.669  1.00 2.39  ? 36   LEU B CA  1 
ATOM   5030  C  C   . LEU B  1 36  ? 22.866  46.525  44.063  1.00 3.09  ? 36   LEU B C   1 
ATOM   5031  O  O   . LEU B  1 36  ? 23.380  46.704  45.168  1.00 2.00  ? 36   LEU B O   1 
ATOM   5032  C  CB  . LEU B  1 36  ? 21.772  48.731  44.039  1.00 3.56  ? 36   LEU B CB  1 
ATOM   5033  C  CG  . LEU B  1 36  ? 22.988  49.394  43.395  1.00 3.46  ? 36   LEU B CG  1 
ATOM   5034  C  CD1 . LEU B  1 36  ? 22.556  50.103  42.113  1.00 3.75  ? 36   LEU B CD1 1 
ATOM   5035  C  CD2 . LEU B  1 36  ? 23.610  50.378  44.370  1.00 3.10  ? 36   LEU B CD2 1 
ATOM   5036  N  N   . GLY B  1 37  ? 23.361  45.693  43.153  1.00 5.54  ? 37   GLY B N   1 
ATOM   5037  C  CA  . GLY B  1 37  ? 24.583  44.956  43.417  1.00 4.26  ? 37   GLY B CA  1 
ATOM   5038  C  C   . GLY B  1 37  ? 24.395  43.486  43.720  1.00 4.30  ? 37   GLY B C   1 
ATOM   5039  O  O   . GLY B  1 37  ? 25.377  42.779  43.954  1.00 5.17  ? 37   GLY B O   1 
ATOM   5040  N  N   . ALA B  1 38  ? 23.150  43.015  43.710  1.00 4.26  ? 38   ALA B N   1 
ATOM   5041  C  CA  . ALA B  1 38  ? 22.879  41.612  44.001  1.00 3.55  ? 38   ALA B CA  1 
ATOM   5042  C  C   . ALA B  1 38  ? 22.988  40.729  42.765  1.00 2.91  ? 38   ALA B C   1 
ATOM   5043  O  O   . ALA B  1 38  ? 23.048  41.214  41.639  1.00 2.89  ? 38   ALA B O   1 
ATOM   5044  C  CB  . ALA B  1 38  ? 21.503  41.466  44.628  1.00 3.79  ? 38   ALA B CB  1 
ATOM   5045  N  N   . ALA B  1 39  ? 23.014  39.423  42.994  1.00 3.55  ? 39   ALA B N   1 
ATOM   5046  C  CA  . ALA B  1 39  ? 23.120  38.455  41.918  1.00 2.00  ? 39   ALA B CA  1 
ATOM   5047  C  C   . ALA B  1 39  ? 21.845  38.349  41.094  1.00 2.23  ? 39   ALA B C   1 
ATOM   5048  O  O   . ALA B  1 39  ? 20.748  38.635  41.572  1.00 2.40  ? 39   ALA B O   1 
ATOM   5049  C  CB  . ALA B  1 39  ? 23.483  37.096  42.484  1.00 2.00  ? 39   ALA B CB  1 
ATOM   5050  N  N   . ASN B  1 40  ? 22.021  37.921  39.848  1.00 4.01  ? 40   ASN B N   1 
ATOM   5051  C  CA  . ASN B  1 40  ? 20.943  37.744  38.880  1.00 4.64  ? 40   ASN B CA  1 
ATOM   5052  C  C   . ASN B  1 40  ? 20.326  39.016  38.339  1.00 4.29  ? 40   ASN B C   1 
ATOM   5053  O  O   . ASN B  1 40  ? 19.129  39.049  38.068  1.00 5.00  ? 40   ASN B O   1 
ATOM   5054  C  CB  . ASN B  1 40  ? 19.835  36.863  39.445  1.00 5.69  ? 40   ASN B CB  1 
ATOM   5055  C  CG  . ASN B  1 40  ? 20.289  35.446  39.664  1.00 7.46  ? 40   ASN B CG  1 
ATOM   5056  O  OD1 . ASN B  1 40  ? 20.724  34.768  38.732  1.00 7.37  ? 40   ASN B OD1 1 
ATOM   5057  N  ND2 . ASN B  1 40  ? 20.194  34.985  40.905  1.00 10.69 ? 40   ASN B ND2 1 
ATOM   5058  N  N   . ARG B  1 41  ? 21.135  40.061  38.197  1.00 4.34  ? 41   ARG B N   1 
ATOM   5059  C  CA  . ARG B  1 41  ? 20.660  41.315  37.626  1.00 4.92  ? 41   ARG B CA  1 
ATOM   5060  C  C   . ARG B  1 41  ? 21.613  41.633  36.473  1.00 5.20  ? 41   ARG B C   1 
ATOM   5061  O  O   . ARG B  1 41  ? 22.791  41.282  36.518  1.00 6.61  ? 41   ARG B O   1 
ATOM   5062  C  CB  . ARG B  1 41  ? 20.703  42.438  38.651  1.00 5.73  ? 41   ARG B CB  1 
ATOM   5063  C  CG  . ARG B  1 41  ? 20.053  42.101  39.968  1.00 10.37 ? 41   ARG B CG  1 
ATOM   5064  C  CD  . ARG B  1 41  ? 18.552  41.961  39.855  1.00 11.78 ? 41   ARG B CD  1 
ATOM   5065  N  NE  . ARG B  1 41  ? 17.985  41.657  41.163  1.00 14.39 ? 41   ARG B NE  1 
ATOM   5066  C  CZ  . ARG B  1 41  ? 16.978  42.323  41.716  1.00 16.06 ? 41   ARG B CZ  1 
ATOM   5067  N  NH1 . ARG B  1 41  ? 16.417  43.338  41.069  1.00 16.39 ? 41   ARG B NH1 1 
ATOM   5068  N  NH2 . ARG B  1 41  ? 16.538  41.980  42.922  1.00 17.76 ? 41   ARG B NH2 1 
ATOM   5069  N  N   . ALA B  1 42  ? 21.107  42.289  35.438  1.00 4.30  ? 42   ALA B N   1 
ATOM   5070  C  CA  . ALA B  1 42  ? 21.929  42.625  34.290  1.00 2.38  ? 42   ALA B CA  1 
ATOM   5071  C  C   . ALA B  1 42  ? 23.219  43.322  34.665  1.00 2.00  ? 42   ALA B C   1 
ATOM   5072  O  O   . ALA B  1 42  ? 23.248  44.137  35.578  1.00 2.00  ? 42   ALA B O   1 
ATOM   5073  C  CB  . ALA B  1 42  ? 21.153  43.504  33.351  1.00 3.41  ? 42   ALA B CB  1 
ATOM   5074  N  N   . LEU B  1 43  ? 24.283  42.991  33.944  1.00 2.00  ? 43   LEU B N   1 
ATOM   5075  C  CA  . LEU B  1 43  ? 25.585  43.615  34.141  1.00 2.00  ? 43   LEU B CA  1 
ATOM   5076  C  C   . LEU B  1 43  ? 25.363  45.090  33.792  1.00 2.06  ? 43   LEU B C   1 
ATOM   5077  O  O   . LEU B  1 43  ? 24.473  45.413  33.004  1.00 3.73  ? 43   LEU B O   1 
ATOM   5078  C  CB  . LEU B  1 43  ? 26.605  43.009  33.168  1.00 2.08  ? 43   LEU B CB  1 
ATOM   5079  C  CG  . LEU B  1 43  ? 26.871  41.501  33.167  1.00 2.00  ? 43   LEU B CG  1 
ATOM   5080  C  CD1 . LEU B  1 43  ? 27.290  41.046  31.790  1.00 2.00  ? 43   LEU B CD1 1 
ATOM   5081  C  CD2 . LEU B  1 43  ? 27.942  41.179  34.175  1.00 2.00  ? 43   LEU B CD2 1 
ATOM   5082  N  N   . ALA B  1 44  ? 26.155  45.989  34.364  1.00 2.38  ? 44   ALA B N   1 
ATOM   5083  C  CA  . ALA B  1 44  ? 25.985  47.412  34.068  1.00 2.99  ? 44   ALA B CA  1 
ATOM   5084  C  C   . ALA B  1 44  ? 26.724  47.816  32.796  1.00 2.72  ? 44   ALA B C   1 
ATOM   5085  O  O   . ALA B  1 44  ? 27.653  47.139  32.362  1.00 3.12  ? 44   ALA B O   1 
ATOM   5086  C  CB  . ALA B  1 44  ? 26.466  48.254  35.243  1.00 3.76  ? 44   ALA B CB  1 
ATOM   5087  N  N   . ARG B  1 45  ? 26.317  48.928  32.205  1.00 2.00  ? 45   ARG B N   1 
ATOM   5088  C  CA  . ARG B  1 45  ? 26.948  49.386  30.982  1.00 2.00  ? 45   ARG B CA  1 
ATOM   5089  C  C   . ARG B  1 45  ? 27.572  50.740  31.171  1.00 2.00  ? 45   ARG B C   1 
ATOM   5090  O  O   . ARG B  1 45  ? 26.870  51.691  31.481  1.00 4.21  ? 45   ARG B O   1 
ATOM   5091  C  CB  . ARG B  1 45  ? 25.912  49.513  29.885  1.00 2.00  ? 45   ARG B CB  1 
ATOM   5092  C  CG  . ARG B  1 45  ? 25.239  48.239  29.513  1.00 2.49  ? 45   ARG B CG  1 
ATOM   5093  C  CD  . ARG B  1 45  ? 25.861  47.686  28.268  1.00 2.12  ? 45   ARG B CD  1 
ATOM   5094  N  NE  . ARG B  1 45  ? 25.170  46.481  27.846  1.00 2.94  ? 45   ARG B NE  1 
ATOM   5095  C  CZ  . ARG B  1 45  ? 25.585  45.707  26.857  1.00 2.42  ? 45   ARG B CZ  1 
ATOM   5096  N  NH1 . ARG B  1 45  ? 26.689  46.021  26.195  1.00 2.00  ? 45   ARG B NH1 1 
ATOM   5097  N  NH2 . ARG B  1 45  ? 24.896  44.624  26.535  1.00 3.40  ? 45   ARG B NH2 1 
ATOM   5098  N  N   . TRP B  1 46  ? 28.878  50.853  30.988  1.00 2.00  ? 46   TRP B N   1 
ATOM   5099  C  CA  . TRP B  1 46  ? 29.484  52.163  31.125  1.00 2.00  ? 46   TRP B CA  1 
ATOM   5100  C  C   . TRP B  1 46  ? 29.307  52.877  29.794  1.00 2.00  ? 46   TRP B C   1 
ATOM   5101  O  O   . TRP B  1 46  ? 29.219  54.100  29.753  1.00 3.14  ? 46   TRP B O   1 
ATOM   5102  C  CB  . TRP B  1 46  ? 30.962  52.059  31.481  1.00 2.11  ? 46   TRP B CB  1 
ATOM   5103  C  CG  . TRP B  1 46  ? 31.220  51.509  32.851  1.00 2.00  ? 46   TRP B CG  1 
ATOM   5104  C  CD1 . TRP B  1 46  ? 30.316  51.356  33.864  1.00 2.00  ? 46   TRP B CD1 1 
ATOM   5105  C  CD2 . TRP B  1 46  ? 32.483  51.092  33.375  1.00 2.31  ? 46   TRP B CD2 1 
ATOM   5106  N  NE1 . TRP B  1 46  ? 30.942  50.873  34.992  1.00 2.00  ? 46   TRP B NE1 1 
ATOM   5107  C  CE2 . TRP B  1 46  ? 32.273  50.704  34.718  1.00 2.00  ? 46   TRP B CE2 1 
ATOM   5108  C  CE3 . TRP B  1 46  ? 33.778  51.013  32.840  1.00 2.00  ? 46   TRP B CE3 1 
ATOM   5109  C  CZ2 . TRP B  1 46  ? 33.305  50.243  35.533  1.00 2.14  ? 46   TRP B CZ2 1 
ATOM   5110  C  CZ3 . TRP B  1 46  ? 34.808  50.554  33.652  1.00 2.00  ? 46   TRP B CZ3 1 
ATOM   5111  C  CH2 . TRP B  1 46  ? 34.564  50.175  34.986  1.00 2.39  ? 46   TRP B CH2 1 
ATOM   5112  N  N   . LEU B  1 47  ? 29.248  52.108  28.707  1.00 2.00  ? 47   LEU B N   1 
ATOM   5113  C  CA  . LEU B  1 47  ? 29.043  52.668  27.366  1.00 2.00  ? 47   LEU B CA  1 
ATOM   5114  C  C   . LEU B  1 47  ? 27.928  51.927  26.612  1.00 2.00  ? 47   LEU B C   1 
ATOM   5115  O  O   . LEU B  1 47  ? 27.842  50.703  26.659  1.00 2.00  ? 47   LEU B O   1 
ATOM   5116  C  CB  . LEU B  1 47  ? 30.340  52.633  26.549  1.00 2.00  ? 47   LEU B CB  1 
ATOM   5117  C  CG  . LEU B  1 47  ? 31.391  53.717  26.792  1.00 2.00  ? 47   LEU B CG  1 
ATOM   5118  C  CD1 . LEU B  1 47  ? 32.458  53.626  25.727  1.00 2.00  ? 47   LEU B CD1 1 
ATOM   5119  C  CD2 . LEU B  1 47  ? 30.754  55.078  26.742  1.00 2.00  ? 47   LEU B CD2 1 
ATOM   5120  N  N   . PRO B  1 48  ? 27.066  52.666  25.899  1.00 2.00  ? 48   PRO B N   1 
ATOM   5121  C  CA  . PRO B  1 48  ? 25.954  52.089  25.143  1.00 2.00  ? 48   PRO B CA  1 
ATOM   5122  C  C   . PRO B  1 48  ? 26.327  50.874  24.325  1.00 2.00  ? 48   PRO B C   1 
ATOM   5123  O  O   . PRO B  1 48  ? 27.367  50.843  23.669  1.00 2.52  ? 48   PRO B O   1 
ATOM   5124  C  CB  . PRO B  1 48  ? 25.490  53.249  24.278  1.00 2.40  ? 48   PRO B CB  1 
ATOM   5125  C  CG  . PRO B  1 48  ? 25.761  54.424  25.150  1.00 2.77  ? 48   PRO B CG  1 
ATOM   5126  C  CD  . PRO B  1 48  ? 27.151  54.112  25.650  1.00 2.72  ? 48   PRO B CD  1 
ATOM   5127  N  N   . ALA B  1 49  ? 25.446  49.881  24.370  1.00 2.00  ? 49   ALA B N   1 
ATOM   5128  C  CA  . ALA B  1 49  ? 25.626  48.622  23.670  1.00 2.00  ? 49   ALA B CA  1 
ATOM   5129  C  C   . ALA B  1 49  ? 25.772  48.797  22.177  1.00 2.00  ? 49   ALA B C   1 
ATOM   5130  O  O   . ALA B  1 49  ? 25.120  49.636  21.569  1.00 2.28  ? 49   ALA B O   1 
ATOM   5131  C  CB  . ALA B  1 49  ? 24.458  47.708  23.963  1.00 2.00  ? 49   ALA B CB  1 
ATOM   5132  N  N   . GLU B  1 50  ? 26.628  47.991  21.577  1.00 2.00  ? 50   GLU B N   1 
ATOM   5133  C  CA  . GLU B  1 50  ? 26.816  48.091  20.150  1.00 2.00  ? 50   GLU B CA  1 
ATOM   5134  C  C   . GLU B  1 50  ? 26.536  46.786  19.430  1.00 2.00  ? 50   GLU B C   1 
ATOM   5135  O  O   . GLU B  1 50  ? 27.399  45.932  19.325  1.00 3.51  ? 50   GLU B O   1 
ATOM   5136  C  CB  . GLU B  1 50  ? 28.227  48.594  19.840  1.00 2.00  ? 50   GLU B CB  1 
ATOM   5137  C  CG  . GLU B  1 50  ? 28.430  50.051  20.239  1.00 2.00  ? 50   GLU B CG  1 
ATOM   5138  C  CD  . GLU B  1 50  ? 29.666  50.658  19.619  1.00 2.11  ? 50   GLU B CD  1 
ATOM   5139  O  OE1 . GLU B  1 50  ? 30.271  49.998  18.744  1.00 3.07  ? 50   GLU B OE1 1 
ATOM   5140  O  OE2 . GLU B  1 50  ? 30.022  51.797  19.998  1.00 2.02  ? 50   GLU B OE2 1 
ATOM   5141  N  N   . TYR B  1 51  ? 25.303  46.633  18.959  1.00 3.25  ? 51   TYR B N   1 
ATOM   5142  C  CA  . TYR B  1 51  ? 24.894  45.449  18.210  1.00 2.33  ? 51   TYR B CA  1 
ATOM   5143  C  C   . TYR B  1 51  ? 24.660  45.851  16.754  1.00 2.00  ? 51   TYR B C   1 
ATOM   5144  O  O   . TYR B  1 51  ? 24.446  47.023  16.452  1.00 2.00  ? 51   TYR B O   1 
ATOM   5145  C  CB  . TYR B  1 51  ? 23.594  44.862  18.764  1.00 2.00  ? 51   TYR B CB  1 
ATOM   5146  C  CG  . TYR B  1 51  ? 23.709  44.218  20.111  1.00 2.00  ? 51   TYR B CG  1 
ATOM   5147  C  CD1 . TYR B  1 51  ? 24.591  43.171  20.324  1.00 2.00  ? 51   TYR B CD1 1 
ATOM   5148  C  CD2 . TYR B  1 51  ? 22.921  44.647  21.173  1.00 2.00  ? 51   TYR B CD2 1 
ATOM   5149  C  CE1 . TYR B  1 51  ? 24.692  42.557  21.571  1.00 2.61  ? 51   TYR B CE1 1 
ATOM   5150  C  CE2 . TYR B  1 51  ? 23.008  44.046  22.425  1.00 2.13  ? 51   TYR B CE2 1 
ATOM   5151  C  CZ  . TYR B  1 51  ? 23.898  43.000  22.617  1.00 2.52  ? 51   TYR B CZ  1 
ATOM   5152  O  OH  . TYR B  1 51  ? 24.004  42.399  23.850  1.00 3.89  ? 51   TYR B OH  1 
ATOM   5153  N  N   . GLU B  1 52  ? 24.688  44.860  15.867  1.00 3.99  ? 52   GLU B N   1 
ATOM   5154  C  CA  . GLU B  1 52  ? 24.485  45.053  14.433  1.00 4.77  ? 52   GLU B CA  1 
ATOM   5155  C  C   . GLU B  1 52  ? 23.138  45.699  14.099  1.00 5.19  ? 52   GLU B C   1 
ATOM   5156  O  O   . GLU B  1 52  ? 23.089  46.686  13.352  1.00 6.07  ? 52   GLU B O   1 
ATOM   5157  C  CB  . GLU B  1 52  ? 24.628  43.706  13.727  1.00 5.49  ? 52   GLU B CB  1 
ATOM   5158  C  CG  . GLU B  1 52  ? 23.843  43.556  12.450  1.00 9.32  ? 52   GLU B CG  1 
ATOM   5159  C  CD  . GLU B  1 52  ? 24.143  42.242  11.754  1.00 11.87 ? 52   GLU B CD  1 
ATOM   5160  O  OE1 . GLU B  1 52  ? 23.298  41.783  10.952  1.00 13.40 ? 52   GLU B OE1 1 
ATOM   5161  O  OE2 . GLU B  1 52  ? 25.231  41.673  12.002  1.00 13.10 ? 52   GLU B OE2 1 
ATOM   5162  N  N   . ASP B  1 53  ? 22.051  45.140  14.632  1.00 4.79  ? 53   ASP B N   1 
ATOM   5163  C  CA  . ASP B  1 53  ? 20.723  45.707  14.404  1.00 3.43  ? 53   ASP B CA  1 
ATOM   5164  C  C   . ASP B  1 53  ? 20.527  46.765  15.478  1.00 3.05  ? 53   ASP B C   1 
ATOM   5165  O  O   . ASP B  1 53  ? 19.405  47.108  15.838  1.00 3.87  ? 53   ASP B O   1 
ATOM   5166  C  CB  . ASP B  1 53  ? 19.622  44.629  14.490  1.00 3.49  ? 53   ASP B CB  1 
ATOM   5167  C  CG  . ASP B  1 53  ? 19.524  43.977  15.866  1.00 2.58  ? 53   ASP B CG  1 
ATOM   5168  O  OD1 . ASP B  1 53  ? 20.421  44.207  16.699  1.00 2.00  ? 53   ASP B OD1 1 
ATOM   5169  O  OD2 . ASP B  1 53  ? 18.553  43.219  16.108  1.00 2.00  ? 53   ASP B OD2 1 
ATOM   5170  N  N   . GLY B  1 54  ? 21.654  47.265  15.983  1.00 3.39  ? 54   GLY B N   1 
ATOM   5171  C  CA  . GLY B  1 54  ? 21.656  48.284  17.017  1.00 2.39  ? 54   GLY B CA  1 
ATOM   5172  C  C   . GLY B  1 54  ? 20.919  47.858  18.273  1.00 2.48  ? 54   GLY B C   1 
ATOM   5173  O  O   . GLY B  1 54  ? 21.065  48.478  19.324  1.00 2.28  ? 54   GLY B O   1 
ATOM   5174  N  N   . LEU B  1 55  ? 20.162  46.770  18.176  1.00 2.00  ? 55   LEU B N   1 
ATOM   5175  C  CA  . LEU B  1 55  ? 19.358  46.296  19.293  1.00 3.25  ? 55   LEU B CA  1 
ATOM   5176  C  C   . LEU B  1 55  ? 19.791  44.992  20.012  1.00 5.06  ? 55   LEU B C   1 
ATOM   5177  O  O   . LEU B  1 55  ? 19.855  44.956  21.249  1.00 4.03  ? 55   LEU B O   1 
ATOM   5178  C  CB  . LEU B  1 55  ? 17.917  46.171  18.797  1.00 3.08  ? 55   LEU B CB  1 
ATOM   5179  C  CG  . LEU B  1 55  ? 16.784  46.256  19.806  1.00 3.05  ? 55   LEU B CG  1 
ATOM   5180  C  CD1 . LEU B  1 55  ? 16.880  47.571  20.562  1.00 2.00  ? 55   LEU B CD1 1 
ATOM   5181  C  CD2 . LEU B  1 55  ? 15.456  46.134  19.068  1.00 2.00  ? 55   LEU B CD2 1 
ATOM   5182  N  N   . ALA B  1 56  ? 20.080  43.928  19.261  1.00 4.14  ? 56   ALA B N   1 
ATOM   5183  C  CA  . ALA B  1 56  ? 20.470  42.672  19.894  1.00 3.07  ? 56   ALA B CA  1 
ATOM   5184  C  C   . ALA B  1 56  ? 21.295  41.625  19.104  1.00 3.89  ? 56   ALA B C   1 
ATOM   5185  O  O   . ALA B  1 56  ? 21.751  40.654  19.711  1.00 3.12  ? 56   ALA B O   1 
ATOM   5186  C  CB  . ALA B  1 56  ? 19.220  42.007  20.474  1.00 2.86  ? 56   ALA B CB  1 
ATOM   5187  N  N   . VAL B  1 57  ? 21.488  41.776  17.788  1.00 3.27  ? 57   VAL B N   1 
ATOM   5188  C  CA  . VAL B  1 57  ? 22.281  40.769  17.060  1.00 2.53  ? 57   VAL B CA  1 
ATOM   5189  C  C   . VAL B  1 57  ? 23.728  41.207  16.993  1.00 2.00  ? 57   VAL B C   1 
ATOM   5190  O  O   . VAL B  1 57  ? 24.024  42.352  16.669  1.00 2.00  ? 57   VAL B O   1 
ATOM   5191  C  CB  . VAL B  1 57  ? 21.772  40.484  15.619  1.00 3.10  ? 57   VAL B CB  1 
ATOM   5192  C  CG1 . VAL B  1 57  ? 20.356  40.977  15.462  1.00 4.91  ? 57   VAL B CG1 1 
ATOM   5193  C  CG2 . VAL B  1 57  ? 22.705  41.093  14.585  1.00 3.83  ? 57   VAL B CG2 1 
ATOM   5194  N  N   . PRO B  1 58  ? 24.649  40.281  17.285  1.00 2.00  ? 58   PRO B N   1 
ATOM   5195  C  CA  . PRO B  1 58  ? 26.107  40.446  17.315  1.00 3.51  ? 58   PRO B CA  1 
ATOM   5196  C  C   . PRO B  1 58  ? 26.775  40.782  15.999  1.00 3.42  ? 58   PRO B C   1 
ATOM   5197  O  O   . PRO B  1 58  ? 26.300  40.395  14.939  1.00 5.48  ? 58   PRO B O   1 
ATOM   5198  C  CB  . PRO B  1 58  ? 26.597  39.100  17.860  1.00 2.24  ? 58   PRO B CB  1 
ATOM   5199  C  CG  . PRO B  1 58  ? 25.366  38.488  18.498  1.00 2.00  ? 58   PRO B CG  1 
ATOM   5200  C  CD  . PRO B  1 58  ? 24.294  38.881  17.549  1.00 2.00  ? 58   PRO B CD  1 
ATOM   5201  N  N   . PHE B  1 59  ? 27.887  41.501  16.058  1.00 3.74  ? 59   PHE B N   1 
ATOM   5202  C  CA  . PHE B  1 59  ? 28.587  41.805  14.826  1.00 6.16  ? 59   PHE B CA  1 
ATOM   5203  C  C   . PHE B  1 59  ? 29.298  40.564  14.308  1.00 7.63  ? 59   PHE B C   1 
ATOM   5204  O  O   . PHE B  1 59  ? 30.151  39.998  14.984  1.00 9.49  ? 59   PHE B O   1 
ATOM   5205  C  CB  . PHE B  1 59  ? 29.593  42.927  15.034  1.00 4.75  ? 59   PHE B CB  1 
ATOM   5206  C  CG  . PHE B  1 59  ? 29.025  44.279  14.774  1.00 3.61  ? 59   PHE B CG  1 
ATOM   5207  C  CD1 . PHE B  1 59  ? 28.753  45.142  15.814  1.00 3.79  ? 59   PHE B CD1 1 
ATOM   5208  C  CD2 . PHE B  1 59  ? 28.717  44.672  13.479  1.00 3.32  ? 59   PHE B CD2 1 
ATOM   5209  C  CE1 . PHE B  1 59  ? 28.177  46.382  15.569  1.00 3.99  ? 59   PHE B CE1 1 
ATOM   5210  C  CE2 . PHE B  1 59  ? 28.142  45.907  13.226  1.00 2.83  ? 59   PHE B CE2 1 
ATOM   5211  C  CZ  . PHE B  1 59  ? 27.872  46.761  14.270  1.00 3.32  ? 59   PHE B CZ  1 
ATOM   5212  N  N   . GLY B  1 60  ? 28.947  40.143  13.102  1.00 9.40  ? 60   GLY B N   1 
ATOM   5213  C  CA  . GLY B  1 60  ? 29.570  38.966  12.533  1.00 11.71 ? 60   GLY B CA  1 
ATOM   5214  C  C   . GLY B  1 60  ? 28.497  37.916  12.407  1.00 13.56 ? 60   GLY B C   1 
ATOM   5215  O  O   . GLY B  1 60  ? 28.768  36.724  12.265  1.00 15.59 ? 60   GLY B O   1 
ATOM   5216  N  N   . TRP B  1 61  ? 27.257  38.381  12.452  1.00 14.43 ? 61   TRP B N   1 
ATOM   5217  C  CA  . TRP B  1 61  ? 26.107  37.504  12.363  1.00 17.16 ? 61   TRP B CA  1 
ATOM   5218  C  C   . TRP B  1 61  ? 25.567  37.347  10.957  1.00 19.82 ? 61   TRP B C   1 
ATOM   5219  O  O   . TRP B  1 61  ? 25.533  36.240  10.420  1.00 22.10 ? 61   TRP B O   1 
ATOM   5220  C  CB  . TRP B  1 61  ? 25.001  38.036  13.245  1.00 13.80 ? 61   TRP B CB  1 
ATOM   5221  C  CG  . TRP B  1 61  ? 23.854  37.130  13.332  1.00 10.44 ? 61   TRP B CG  1 
ATOM   5222  C  CD1 . TRP B  1 61  ? 22.725  37.152  12.572  1.00 10.66 ? 61   TRP B CD1 1 
ATOM   5223  C  CD2 . TRP B  1 61  ? 23.681  36.092  14.288  1.00 9.04  ? 61   TRP B CD2 1 
ATOM   5224  N  NE1 . TRP B  1 61  ? 21.844  36.192  13.009  1.00 9.40  ? 61   TRP B NE1 1 
ATOM   5225  C  CE2 . TRP B  1 61  ? 22.409  35.528  14.064  1.00 8.23  ? 61   TRP B CE2 1 
ATOM   5226  C  CE3 . TRP B  1 61  ? 24.478  35.585  15.320  1.00 7.55  ? 61   TRP B CE3 1 
ATOM   5227  C  CZ2 . TRP B  1 61  ? 21.913  34.487  14.834  1.00 8.71  ? 61   TRP B CZ2 1 
ATOM   5228  C  CZ3 . TRP B  1 61  ? 23.991  34.552  16.084  1.00 7.60  ? 61   TRP B CZ3 1 
ATOM   5229  C  CH2 . TRP B  1 61  ? 22.716  34.011  15.840  1.00 9.65  ? 61   TRP B CH2 1 
ATOM   5230  N  N   . THR B  1 62  ? 25.108  38.453  10.379  1.00 22.20 ? 62   THR B N   1 
ATOM   5231  C  CA  . THR B  1 62  ? 24.575  38.425  9.029   1.00 24.63 ? 62   THR B CA  1 
ATOM   5232  C  C   . THR B  1 62  ? 25.657  38.871  8.074   1.00 26.74 ? 62   THR B C   1 
ATOM   5233  O  O   . THR B  1 62  ? 25.627  39.982  7.559   1.00 26.64 ? 62   THR B O   1 
ATOM   5234  C  CB  . THR B  1 62  ? 23.346  39.338  8.874   1.00 24.92 ? 62   THR B CB  1 
ATOM   5235  O  OG1 . THR B  1 62  ? 22.272  38.815  9.663   1.00 25.97 ? 62   THR B OG1 1 
ATOM   5236  C  CG2 . THR B  1 62  ? 22.900  39.399  7.414   1.00 25.64 ? 62   THR B CG2 1 
ATOM   5237  N  N   . GLN B  1 63  ? 26.626  37.984  7.877   1.00 29.35 ? 63   GLN B N   1 
ATOM   5238  C  CA  . GLN B  1 63  ? 27.765  38.187  6.979   1.00 30.48 ? 63   GLN B CA  1 
ATOM   5239  C  C   . GLN B  1 63  ? 27.658  39.437  6.114   1.00 29.50 ? 63   GLN B C   1 
ATOM   5240  O  O   . GLN B  1 63  ? 28.500  40.332  6.156   1.00 27.13 ? 63   GLN B O   1 
ATOM   5241  C  CB  . GLN B  1 63  ? 27.869  36.985  6.049   1.00 33.51 ? 63   GLN B CB  1 
ATOM   5242  C  CG  . GLN B  1 63  ? 27.597  35.664  6.726   1.00 38.69 ? 63   GLN B CG  1 
ATOM   5243  C  CD  . GLN B  1 63  ? 27.233  34.573  5.739   1.00 41.57 ? 63   GLN B CD  1 
ATOM   5244  O  OE1 . GLN B  1 63  ? 27.067  33.410  6.116   1.00 44.20 ? 63   GLN B OE1 1 
ATOM   5245  N  NE2 . GLN B  1 63  ? 27.100  34.942  4.465   1.00 43.09 ? 63   GLN B NE2 1 
ATOM   5246  N  N   . ARG B  1 64  ? 26.600  39.436  5.312   1.00 29.55 ? 64   ARG B N   1 
ATOM   5247  C  CA  . ARG B  1 64  ? 26.246  40.485  4.364   1.00 28.28 ? 64   ARG B CA  1 
ATOM   5248  C  C   . ARG B  1 64  ? 25.952  41.899  4.959   1.00 26.41 ? 64   ARG B C   1 
ATOM   5249  O  O   . ARG B  1 64  ? 25.208  42.708  4.385   1.00 26.04 ? 64   ARG B O   1 
ATOM   5250  C  CB  . ARG B  1 64  ? 25.096  39.913  3.499   1.00 30.13 ? 64   ARG B CB  1 
ATOM   5251  C  CG  . ARG B  1 64  ? 23.898  40.789  3.216   1.00 34.68 ? 64   ARG B CG  1 
ATOM   5252  C  CD  . ARG B  1 64  ? 22.920  40.781  4.369   1.00 37.22 ? 64   ARG B CD  1 
ATOM   5253  N  NE  . ARG B  1 64  ? 21.815  41.706  4.138   1.00 41.26 ? 64   ARG B NE  1 
ATOM   5254  C  CZ  . ARG B  1 64  ? 20.632  41.621  4.739   1.00 42.64 ? 64   ARG B CZ  1 
ATOM   5255  N  NH1 . ARG B  1 64  ? 20.396  40.646  5.611   1.00 43.95 ? 64   ARG B NH1 1 
ATOM   5256  N  NH2 . ARG B  1 64  ? 19.681  42.509  4.471   1.00 44.01 ? 64   ARG B NH2 1 
ATOM   5257  N  N   . LYS B  1 65  ? 26.590  42.183  6.097   1.00 22.96 ? 65   LYS B N   1 
ATOM   5258  C  CA  . LYS B  1 65  ? 26.491  43.460  6.815   1.00 18.72 ? 65   LYS B CA  1 
ATOM   5259  C  C   . LYS B  1 65  ? 27.893  43.717  7.380   1.00 16.23 ? 65   LYS B C   1 
ATOM   5260  O  O   . LYS B  1 65  ? 28.617  42.767  7.684   1.00 17.49 ? 65   LYS B O   1 
ATOM   5261  C  CB  . LYS B  1 65  ? 25.491  43.349  7.973   1.00 18.42 ? 65   LYS B CB  1 
ATOM   5262  C  CG  . LYS B  1 65  ? 24.195  42.593  7.640   1.00 19.75 ? 65   LYS B CG  1 
ATOM   5263  C  CD  . LYS B  1 65  ? 23.050  43.495  7.150   1.00 19.08 ? 65   LYS B CD  1 
ATOM   5264  C  CE  . LYS B  1 65  ? 22.694  44.545  8.193   1.00 18.08 ? 65   LYS B CE  1 
ATOM   5265  N  NZ  . LYS B  1 65  ? 21.485  45.315  7.812   1.00 16.49 ? 65   LYS B NZ  1 
ATOM   5266  N  N   . THR B  1 66  ? 28.287  44.945  7.545   1.00 11.58 ? 66   THR B N   1 
ATOM   5267  C  CA  . THR B  1 66  ? 29.612  45.194  8.080   1.00 7.07  ? 66   THR B CA  1 
ATOM   5268  C  C   . THR B  1 66  ? 29.607  45.962  9.361   1.00 5.88  ? 66   THR B C   1 
ATOM   5269  O  O   . THR B  1 66  ? 28.631  46.624  9.711   1.00 4.69  ? 66   THR B O   1 
ATOM   5270  C  CB  . THR B  1 66  ? 30.403  46.171  7.147   1.00 6.51  ? 66   THR B CB  1 
ATOM   5271  O  OG1 . THR B  1 66  ? 29.597  47.315  6.895   1.00 4.28  ? 66   THR B OG1 1 
ATOM   5272  C  CG2 . THR B  1 66  ? 30.759  45.488  5.843   1.00 7.23  ? 66   THR B CG2 1 
ATOM   5273  N  N   . ARG B  1 67  ? 30.741  45.852  10.056  1.00 4.96  ? 67   ARG B N   1 
ATOM   5274  C  CA  . ARG B  1 67  ? 30.713  47.468  10.907  1.00 6.20  ? 67   ARG B CA  1 
ATOM   5275  C  C   . ARG B  1 67  ? 31.673  48.563  10.482  1.00 6.08  ? 67   ARG B C   1 
ATOM   5276  O  O   . ARG B  1 67  ? 32.856  48.303  10.267  1.00 5.69  ? 67   ARG B O   1 
ATOM   5277  C  CB  . ARG B  1 67  ? 31.373  46.604  11.989  1.00 6.19  ? 67   ARG B CB  1 
ATOM   5278  C  CG  . ARG B  1 67  ? 31.328  47.209  13.397  1.00 5.68  ? 67   ARG B CG  1 
ATOM   5279  C  CD  . ARG B  1 67  ? 32.536  46.797  14.218  1.00 7.37  ? 67   ARG B CD  1 
ATOM   5280  N  NE  . ARG B  1 67  ? 32.407  47.129  15.637  1.00 9.58  ? 67   ARG B NE  1 
ATOM   5281  C  CZ  . ARG B  1 67  ? 32.171  46.235  16.593  1.00 8.63  ? 67   ARG B CZ  1 
ATOM   5282  N  NH1 . ARG B  1 67  ? 32.043  44.953  16.286  1.00 8.40  ? 67   ARG B NH1 1 
ATOM   5283  N  NH2 . ARG B  1 67  ? 32.051  46.622  17.854  1.00 8.36  ? 67   ARG B NH2 1 
ATOM   5284  N  N   . ASN B  1 68  ? 31.168  49.781  10.342  1.00 4.94  ? 68   ASN B N   1 
ATOM   5285  C  CA  . ASN B  1 68  ? 32.010  50.884  9.906   1.00 4.68  ? 68   ASN B CA  1 
ATOM   5286  C  C   . ASN B  1 68  ? 32.515  50.624  8.485   1.00 4.17  ? 68   ASN B C   1 
ATOM   5287  O  O   . ASN B  1 68  ? 33.567  51.116  8.065   1.00 2.22  ? 68   ASN B O   1 
ATOM   5288  C  CB  . ASN B  1 68  ? 33.160  51.083  10.888  1.00 5.53  ? 68   ASN B CB  1 
ATOM   5289  C  CG  . ASN B  1 68  ? 32.660  51.359  12.296  1.00 8.05  ? 68   ASN B CG  1 
ATOM   5290  O  OD1 . ASN B  1 68  ? 31.698  52.110  12.481  1.00 9.01  ? 68   ASN B OD1 1 
ATOM   5291  N  ND2 . ASN B  1 68  ? 33.306  50.760  13.294  1.00 9.29  ? 68   ASN B ND2 1 
ATOM   5292  N  N   . GLY B  1 69  ? 31.728  49.838  7.755   1.00 4.05  ? 69   GLY B N   1 
ATOM   5293  C  CA  . GLY B  1 69  ? 32.038  49.523  6.374   1.00 4.63  ? 69   GLY B CA  1 
ATOM   5294  C  C   . GLY B  1 69  ? 33.035  48.418  6.115   1.00 4.98  ? 69   GLY B C   1 
ATOM   5295  O  O   . GLY B  1 69  ? 33.696  48.427  5.075   1.00 5.45  ? 69   GLY B O   1 
ATOM   5296  N  N   . PHE B  1 70  ? 33.139  47.462  7.036   1.00 5.86  ? 70   PHE B N   1 
ATOM   5297  C  CA  . PHE B  1 70  ? 34.082  46.348  6.886   1.00 6.22  ? 70   PHE B CA  1 
ATOM   5298  C  C   . PHE B  1 70  ? 33.556  45.023  7.420   1.00 6.52  ? 70   PHE B C   1 
ATOM   5299  O  O   . PHE B  1 70  ? 32.644  44.998  8.241   1.00 5.95  ? 70   PHE B O   1 
ATOM   5300  C  CB  . PHE B  1 70  ? 35.395  46.674  7.599   1.00 6.24  ? 70   PHE B CB  1 
ATOM   5301  C  CG  . PHE B  1 70  ? 36.144  47.817  6.992   1.00 6.97  ? 70   PHE B CG  1 
ATOM   5302  C  CD1 . PHE B  1 70  ? 36.155  49.068  7.599   1.00 7.60  ? 70   PHE B CD1 1 
ATOM   5303  C  CD2 . PHE B  1 70  ? 36.828  47.644  5.793   1.00 8.18  ? 70   PHE B CD2 1 
ATOM   5304  C  CE1 . PHE B  1 70  ? 36.841  50.139  7.018   1.00 9.31  ? 70   PHE B CE1 1 
ATOM   5305  C  CE2 . PHE B  1 70  ? 37.514  48.701  5.201   1.00 9.26  ? 70   PHE B CE2 1 
ATOM   5306  C  CZ  . PHE B  1 70  ? 37.521  49.954  5.815   1.00 9.37  ? 70   PHE B CZ  1 
ATOM   5307  N  N   . ARG B  1 71  ? 34.136  43.921  6.955   1.00 8.58  ? 71   ARG B N   1 
ATOM   5308  C  CA  . ARG B  1 71  ? 33.727  42.599  7.425   1.00 11.89 ? 71   ARG B CA  1 
ATOM   5309  C  C   . ARG B  1 71  ? 34.550  42.236  8.662   1.00 11.08 ? 71   ARG B C   1 
ATOM   5310  O  O   . ARG B  1 71  ? 35.787  42.237  8.630   1.00 11.53 ? 71   ARG B O   1 
ATOM   5311  C  CB  . ARG B  1 71  ? 33.955  41.509  6.360   1.00 18.62 ? 71   ARG B CB  1 
ATOM   5312  C  CG  . ARG B  1 71  ? 33.419  41.807  4.950   1.00 27.97 ? 71   ARG B CG  1 
ATOM   5313  C  CD  . ARG B  1 71  ? 33.396  40.544  4.072   1.00 33.51 ? 71   ARG B CD  1 
ATOM   5314  N  NE  . ARG B  1 71  ? 32.129  39.813  4.194   1.00 42.51 ? 71   ARG B NE  1 
ATOM   5315  C  CZ  . ARG B  1 71  ? 31.941  38.537  3.848   1.00 45.44 ? 71   ARG B CZ  1 
ATOM   5316  N  NH1 . ARG B  1 71  ? 32.940  37.813  3.353   1.00 48.34 ? 71   ARG B NH1 1 
ATOM   5317  N  NH2 . ARG B  1 71  ? 30.740  37.984  3.987   1.00 48.24 ? 71   ARG B NH2 1 
ATOM   5318  N  N   . VAL B  1 72  ? 33.863  41.937  9.757   1.00 7.99  ? 72   VAL B N   1 
ATOM   5319  C  CA  . VAL B  1 72  ? 34.542  41.553  10.984  1.00 5.27  ? 72   VAL B CA  1 
ATOM   5320  C  C   . VAL B  1 72  ? 35.206  40.196  10.763  1.00 4.06  ? 72   VAL B C   1 
ATOM   5321  O  O   . VAL B  1 72  ? 34.570  39.239  10.306  1.00 2.00  ? 72   VAL B O   1 
ATOM   5322  C  CB  . VAL B  1 72  ? 33.551  41.452  12.140  1.00 3.52  ? 72   VAL B CB  1 
ATOM   5323  C  CG1 . VAL B  1 72  ? 33.218  42.830  12.642  1.00 2.52  ? 72   VAL B CG1 1 
ATOM   5324  C  CG2 . VAL B  1 72  ? 32.283  40.759  11.663  1.00 3.49  ? 72   VAL B CG2 1 
ATOM   5325  N  N   . PRO B  1 73  ? 36.504  40.100  11.076  1.00 2.00  ? 73   PRO B N   1 
ATOM   5326  C  CA  . PRO B  1 73  ? 37.242  38.853  10.904  1.00 2.00  ? 73   PRO B CA  1 
ATOM   5327  C  C   . PRO B  1 73  ? 36.669  37.731  11.757  1.00 2.00  ? 73   PRO B C   1 
ATOM   5328  O  O   . PRO B  1 73  ? 36.199  37.962  12.871  1.00 2.00  ? 73   PRO B O   1 
ATOM   5329  C  CB  . PRO B  1 73  ? 38.655  39.240  11.322  1.00 2.00  ? 73   PRO B CB  1 
ATOM   5330  C  CG  . PRO B  1 73  ? 38.412  40.241  12.390  1.00 2.08  ? 73   PRO B CG  1 
ATOM   5331  C  CD  . PRO B  1 73  ? 37.326  41.099  11.779  1.00 2.34  ? 73   PRO B CD  1 
ATOM   5332  N  N   . LEU B  1 74  ? 36.695  36.516  11.222  1.00 2.00  ? 74   LEU B N   1 
ATOM   5333  C  CA  . LEU B  1 74  ? 36.196  35.374  11.963  1.00 2.00  ? 74   LEU B CA  1 
ATOM   5334  C  C   . LEU B  1 74  ? 36.921  35.333  13.292  1.00 2.00  ? 74   LEU B C   1 
ATOM   5335  O  O   . LEU B  1 74  ? 38.077  35.738  13.387  1.00 2.00  ? 74   LEU B O   1 
ATOM   5336  C  CB  . LEU B  1 74  ? 36.493  34.083  11.223  1.00 2.00  ? 74   LEU B CB  1 
ATOM   5337  C  CG  . LEU B  1 74  ? 35.763  33.694  9.945   1.00 2.00  ? 74   LEU B CG  1 
ATOM   5338  C  CD1 . LEU B  1 74  ? 36.183  32.264  9.642   1.00 3.18  ? 74   LEU B CD1 1 
ATOM   5339  C  CD2 . LEU B  1 74  ? 34.243  33.761  10.095  1.00 2.00  ? 74   LEU B CD2 1 
ATOM   5340  N  N   . ALA B  1 75  ? 36.251  34.835  14.319  1.00 2.00  ? 75   ALA B N   1 
ATOM   5341  C  CA  . ALA B  1 75  ? 36.875  34.747  15.632  1.00 2.60  ? 75   ALA B CA  1 
ATOM   5342  C  C   . ALA B  1 75  ? 38.154  33.899  15.595  1.00 2.00  ? 75   ALA B C   1 
ATOM   5343  O  O   . ALA B  1 75  ? 39.227  34.364  15.974  1.00 2.00  ? 75   ALA B O   1 
ATOM   5344  C  CB  . ALA B  1 75  ? 35.884  34.162  16.635  1.00 2.00  ? 75   ALA B CB  1 
ATOM   5345  N  N   . ARG B  1 76  ? 38.017  32.662  15.120  1.00 2.46  ? 76   ARG B N   1 
ATOM   5346  C  CA  . ARG B  1 76  ? 39.110  31.687  15.024  1.00 3.21  ? 76   ARG B CA  1 
ATOM   5347  C  C   . ARG B  1 76  ? 40.344  32.137  14.227  1.00 2.41  ? 76   ARG B C   1 
ATOM   5348  O  O   . ARG B  1 76  ? 41.451  31.644  14.463  1.00 2.00  ? 76   ARG B O   1 
ATOM   5349  C  CB  . ARG B  1 76  ? 38.551  30.373  14.448  1.00 2.30  ? 76   ARG B CB  1 
ATOM   5350  C  CG  . ARG B  1 76  ? 39.557  29.258  14.181  1.00 2.00  ? 76   ARG B CG  1 
ATOM   5351  C  CD  . ARG B  1 76  ? 40.166  28.619  15.434  1.00 2.00  ? 76   ARG B CD  1 
ATOM   5352  N  NE  . ARG B  1 76  ? 41.107  27.561  15.043  1.00 2.38  ? 76   ARG B NE  1 
ATOM   5353  C  CZ  . ARG B  1 76  ? 41.911  26.879  15.861  1.00 2.00  ? 76   ARG B CZ  1 
ATOM   5354  N  NH1 . ARG B  1 76  ? 41.927  27.106  17.163  1.00 2.00  ? 76   ARG B NH1 1 
ATOM   5355  N  NH2 . ARG B  1 76  ? 42.724  25.966  15.363  1.00 2.00  ? 76   ARG B NH2 1 
ATOM   5356  N  N   . GLU B  1 77  ? 40.166  33.062  13.286  1.00 2.22  ? 77   GLU B N   1 
ATOM   5357  C  CA  . GLU B  1 77  ? 41.304  33.541  12.505  1.00 3.14  ? 77   GLU B CA  1 
ATOM   5358  C  C   . GLU B  1 77  ? 42.140  34.501  13.346  1.00 3.98  ? 77   GLU B C   1 
ATOM   5359  O  O   . GLU B  1 77  ? 43.374  34.440  13.336  1.00 3.88  ? 77   GLU B O   1 
ATOM   5360  C  CB  . GLU B  1 77  ? 40.845  34.240  11.218  1.00 3.29  ? 77   GLU B CB  1 
ATOM   5361  C  CG  . GLU B  1 77  ? 42.003  34.753  10.359  1.00 3.17  ? 77   GLU B CG  1 
ATOM   5362  C  CD  . GLU B  1 77  ? 41.644  34.919  8.885   1.00 5.45  ? 77   GLU B CD  1 
ATOM   5363  O  OE1 . GLU B  1 77  ? 40.543  34.485  8.464   1.00 7.02  ? 77   GLU B OE1 1 
ATOM   5364  O  OE2 . GLU B  1 77  ? 42.478  35.477  8.137   1.00 4.93  ? 77   GLU B OE2 1 
ATOM   5365  N  N   . VAL B  1 78  ? 41.464  35.386  14.076  1.00 3.38  ? 78   VAL B N   1 
ATOM   5366  C  CA  . VAL B  1 78  ? 42.148  36.342  14.936  1.00 3.18  ? 78   VAL B CA  1 
ATOM   5367  C  C   . VAL B  1 78  ? 43.084  35.557  15.859  1.00 2.35  ? 78   VAL B C   1 
ATOM   5368  O  O   . VAL B  1 78  ? 44.226  35.953  16.099  1.00 2.59  ? 78   VAL B O   1 
ATOM   5369  C  CB  . VAL B  1 78  ? 41.130  37.144  15.767  1.00 2.16  ? 78   VAL B CB  1 
ATOM   5370  C  CG1 . VAL B  1 78  ? 41.848  38.106  16.701  1.00 2.00  ? 78   VAL B CG1 1 
ATOM   5371  C  CG2 . VAL B  1 78  ? 40.198  37.896  14.829  1.00 2.00  ? 78   VAL B CG2 1 
ATOM   5372  N  N   . SER B  1 79  ? 42.590  34.424  16.345  1.00 2.04  ? 79   SER B N   1 
ATOM   5373  C  CA  . SER B  1 79  ? 43.350  33.550  17.228  1.00 2.63  ? 79   SER B CA  1 
ATOM   5374  C  C   . SER B  1 79  ? 44.623  33.020  16.561  1.00 2.45  ? 79   SER B C   1 
ATOM   5375  O  O   . SER B  1 79  ? 45.723  33.197  17.092  1.00 2.52  ? 79   SER B O   1 
ATOM   5376  C  CB  . SER B  1 79  ? 42.464  32.374  17.669  1.00 3.02  ? 79   SER B CB  1 
ATOM   5377  O  OG  . SER B  1 79  ? 43.128  31.514  18.580  1.00 2.00  ? 79   SER B OG  1 
ATOM   5378  N  N   . ASN B  1 80  ? 44.466  32.379  15.401  1.00 2.30  ? 80   ASN B N   1 
ATOM   5379  C  CA  . ASN B  1 80  ? 45.595  31.797  14.664  1.00 3.07  ? 80   ASN B CA  1 
ATOM   5380  C  C   . ASN B  1 80  ? 46.610  32.807  14.137  1.00 2.43  ? 80   ASN B C   1 
ATOM   5381  O  O   . ASN B  1 80  ? 47.814  32.693  14.373  1.00 2.00  ? 80   ASN B O   1 
ATOM   5382  C  CB  . ASN B  1 80  ? 45.105  30.981  13.461  1.00 2.79  ? 80   ASN B CB  1 
ATOM   5383  C  CG  . ASN B  1 80  ? 44.048  29.969  13.823  1.00 2.29  ? 80   ASN B CG  1 
ATOM   5384  O  OD1 . ASN B  1 80  ? 43.967  29.514  14.962  1.00 3.33  ? 80   ASN B OD1 1 
ATOM   5385  N  ND2 . ASN B  1 80  ? 43.237  29.592  12.840  1.00 2.01  ? 80   ASN B ND2 1 
ATOM   5386  N  N   . LYS B  1 81  ? 46.116  33.783  13.393  1.00 2.60  ? 81   LYS B N   1 
ATOM   5387  C  CA  . LYS B  1 81  ? 46.986  34.778  12.808  1.00 4.25  ? 81   LYS B CA  1 
ATOM   5388  C  C   . LYS B  1 81  ? 47.711  35.608  13.846  1.00 5.14  ? 81   LYS B C   1 
ATOM   5389  O  O   . LYS B  1 81  ? 48.831  36.056  13.602  1.00 6.79  ? 81   LYS B O   1 
ATOM   5390  C  CB  . LYS B  1 81  ? 46.179  35.702  11.896  1.00 5.76  ? 81   LYS B CB  1 
ATOM   5391  C  CG  . LYS B  1 81  ? 45.565  35.021  10.689  1.00 7.61  ? 81   LYS B CG  1 
ATOM   5392  C  CD  . LYS B  1 81  ? 46.532  35.014  9.525   1.00 11.23 ? 81   LYS B CD  1 
ATOM   5393  C  CE  . LYS B  1 81  ? 46.015  34.168  8.359   1.00 13.72 ? 81   LYS B CE  1 
ATOM   5394  N  NZ  . LYS B  1 81  ? 44.737  34.685  7.789   1.00 13.83 ? 81   LYS B NZ  1 
ATOM   5395  N  N   . ILE B  1 82  ? 47.099  35.798  15.012  1.00 4.61  ? 82   ILE B N   1 
ATOM   5396  C  CA  . ILE B  1 82  ? 47.719  36.649  16.028  1.00 4.50  ? 82   ILE B CA  1 
ATOM   5397  C  C   . ILE B  1 82  ? 47.915  36.145  17.453  1.00 2.13  ? 82   ILE B C   1 
ATOM   5398  O  O   . ILE B  1 82  ? 48.892  36.518  18.095  1.00 2.00  ? 82   ILE B O   1 
ATOM   5399  C  CB  . ILE B  1 82  ? 46.966  37.996  16.101  1.00 2.49  ? 82   ILE B CB  1 
ATOM   5400  C  CG1 . ILE B  1 82  ? 46.997  38.657  14.719  1.00 2.00  ? 82   ILE B CG1 1 
ATOM   5401  C  CG2 . ILE B  1 82  ? 47.592  38.894  17.154  1.00 2.00  ? 82   ILE B CG2 1 
ATOM   5402  C  CD1 . ILE B  1 82  ? 46.159  39.885  14.598  1.00 2.74  ? 82   ILE B CD1 1 
ATOM   5403  N  N   . VAL B  1 83  ? 47.015  35.297  17.941  1.00 2.00  ? 83   VAL B N   1 
ATOM   5404  C  CA  . VAL B  1 83  ? 47.097  34.807  19.315  1.00 2.00  ? 83   VAL B CA  1 
ATOM   5405  C  C   . VAL B  1 83  ? 48.040  33.634  19.638  1.00 2.57  ? 83   VAL B C   1 
ATOM   5406  O  O   . VAL B  1 83  ? 48.711  33.644  20.677  1.00 2.00  ? 83   VAL B O   1 
ATOM   5407  C  CB  . VAL B  1 83  ? 45.679  34.470  19.833  1.00 2.00  ? 83   VAL B CB  1 
ATOM   5408  C  CG1 . VAL B  1 83  ? 45.726  34.054  21.301  1.00 2.00  ? 83   VAL B CG1 1 
ATOM   5409  C  CG2 . VAL B  1 83  ? 44.782  35.676  19.666  1.00 2.00  ? 83   VAL B CG2 1 
ATOM   5410  N  N   . GLY B  1 84  ? 48.099  32.638  18.762  1.00 2.00  ? 84   GLY B N   1 
ATOM   5411  C  CA  . GLY B  1 84  ? 48.945  31.481  19.015  1.00 2.00  ? 84   GLY B CA  1 
ATOM   5412  C  C   . GLY B  1 84  ? 50.455  31.656  18.952  1.00 2.00  ? 84   GLY B C   1 
ATOM   5413  O  O   . GLY B  1 84  ? 50.957  32.688  18.508  1.00 2.00  ? 84   GLY B O   1 
ATOM   5414  N  N   . TYR B  1 85  ? 51.166  30.622  19.413  1.00 3.30  ? 85   TYR B N   1 
ATOM   5415  C  CA  . TYR B  1 85  ? 52.635  30.561  19.437  1.00 2.00  ? 85   TYR B CA  1 
ATOM   5416  C  C   . TYR B  1 85  ? 53.071  29.121  19.736  1.00 2.00  ? 85   TYR B C   1 
ATOM   5417  O  O   . TYR B  1 85  ? 52.467  28.450  20.573  1.00 2.00  ? 85   TYR B O   1 
ATOM   5418  C  CB  . TYR B  1 85  ? 53.194  31.515  20.498  1.00 2.77  ? 85   TYR B CB  1 
ATOM   5419  C  CG  . TYR B  1 85  ? 52.988  31.076  21.931  1.00 3.09  ? 85   TYR B CG  1 
ATOM   5420  C  CD1 . TYR B  1 85  ? 53.857  30.164  22.533  1.00 3.67  ? 85   TYR B CD1 1 
ATOM   5421  C  CD2 . TYR B  1 85  ? 51.929  31.578  22.693  1.00 2.37  ? 85   TYR B CD2 1 
ATOM   5422  C  CE1 . TYR B  1 85  ? 53.677  29.764  23.862  1.00 3.81  ? 85   TYR B CE1 1 
ATOM   5423  C  CE2 . TYR B  1 85  ? 51.738  31.185  24.021  1.00 2.02  ? 85   TYR B CE2 1 
ATOM   5424  C  CZ  . TYR B  1 85  ? 52.616  30.277  24.599  1.00 2.79  ? 85   TYR B CZ  1 
ATOM   5425  O  OH  . TYR B  1 85  ? 52.445  29.874  25.904  1.00 2.00  ? 85   TYR B OH  1 
ATOM   5426  N  N   . LEU B  1 86  ? 54.126  28.654  19.070  1.00 3.50  ? 86   LEU B N   1 
ATOM   5427  C  CA  . LEU B  1 86  ? 54.601  27.273  19.236  1.00 3.45  ? 86   LEU B CA  1 
ATOM   5428  C  C   . LEU B  1 86  ? 55.638  26.963  20.303  1.00 2.00  ? 86   LEU B C   1 
ATOM   5429  O  O   . LEU B  1 86  ? 55.505  25.982  21.013  1.00 2.00  ? 86   LEU B O   1 
ATOM   5430  C  CB  . LEU B  1 86  ? 55.139  26.733  17.896  1.00 3.20  ? 86   LEU B CB  1 
ATOM   5431  C  CG  . LEU B  1 86  ? 54.198  25.958  16.962  1.00 3.70  ? 86   LEU B CG  1 
ATOM   5432  C  CD1 . LEU B  1 86  ? 54.799  25.828  15.567  1.00 3.38  ? 86   LEU B CD1 1 
ATOM   5433  C  CD2 . LEU B  1 86  ? 53.939  24.591  17.550  1.00 4.07  ? 86   LEU B CD2 1 
ATOM   5434  N  N   . ASP B  1 87  ? 56.667  27.787  20.417  1.00 2.00  ? 87   ASP B N   1 
ATOM   5435  C  CA  . ASP B  1 87  ? 57.751  27.527  21.359  1.00 2.29  ? 87   ASP B CA  1 
ATOM   5436  C  C   . ASP B  1 87  ? 57.599  28.078  22.778  1.00 3.87  ? 87   ASP B C   1 
ATOM   5437  O  O   . ASP B  1 87  ? 57.683  29.286  22.979  1.00 4.82  ? 87   ASP B O   1 
ATOM   5438  C  CB  . ASP B  1 87  ? 59.048  28.047  20.742  1.00 3.32  ? 87   ASP B CB  1 
ATOM   5439  C  CG  . ASP B  1 87  ? 60.239  27.839  21.634  1.00 5.70  ? 87   ASP B CG  1 
ATOM   5440  O  OD1 . ASP B  1 87  ? 60.275  26.798  22.323  1.00 7.86  ? 87   ASP B OD1 1 
ATOM   5441  O  OD2 . ASP B  1 87  ? 61.144  28.705  21.637  1.00 6.18  ? 87   ASP B OD2 1 
ATOM   5442  N  N   . GLU B  1 88  ? 57.411  27.200  23.767  1.00 3.06  ? 88   GLU B N   1 
ATOM   5443  C  CA  . GLU B  1 88  ? 57.250  27.643  25.163  1.00 2.00  ? 88   GLU B CA  1 
ATOM   5444  C  C   . GLU B  1 88  ? 58.559  28.095  25.813  1.00 2.82  ? 88   GLU B C   1 
ATOM   5445  O  O   . GLU B  1 88  ? 58.573  28.523  26.970  1.00 2.00  ? 88   GLU B O   1 
ATOM   5446  C  CB  . GLU B  1 88  ? 56.664  26.525  26.033  1.00 2.00  ? 88   GLU B CB  1 
ATOM   5447  C  CG  . GLU B  1 88  ? 55.240  26.097  25.728  1.00 4.95  ? 88   GLU B CG  1 
ATOM   5448  C  CD  . GLU B  1 88  ? 54.204  27.165  26.036  1.00 6.36  ? 88   GLU B CD  1 
ATOM   5449  O  OE1 . GLU B  1 88  ? 54.365  27.898  27.039  1.00 6.80  ? 88   GLU B OE1 1 
ATOM   5450  O  OE2 . GLU B  1 88  ? 53.212  27.251  25.281  1.00 7.79  ? 88   GLU B OE2 1 
ATOM   5451  N  N   . GLU B  1 89  ? 59.662  27.994  25.082  1.00 4.57  ? 89   GLU B N   1 
ATOM   5452  C  CA  . GLU B  1 89  ? 60.941  28.371  25.645  1.00 5.61  ? 89   GLU B CA  1 
ATOM   5453  C  C   . GLU B  1 89  ? 60.958  29.734  26.292  1.00 4.22  ? 89   GLU B C   1 
ATOM   5454  O  O   . GLU B  1 89  ? 60.599  30.733  25.678  1.00 3.29  ? 89   GLU B O   1 
ATOM   5455  C  CB  . GLU B  1 89  ? 62.034  28.320  24.593  1.00 12.41 ? 89   GLU B CB  1 
ATOM   5456  C  CG  . GLU B  1 89  ? 63.347  28.929  25.074  1.00 22.69 ? 89   GLU B CG  1 
ATOM   5457  C  CD  . GLU B  1 89  ? 64.470  28.785  24.056  1.00 26.65 ? 89   GLU B CD  1 
ATOM   5458  O  OE1 . GLU B  1 89  ? 65.020  27.664  23.912  1.00 29.82 ? 89   GLU B OE1 1 
ATOM   5459  O  OE2 . GLU B  1 89  ? 64.795  29.791  23.385  1.00 29.63 ? 89   GLU B OE2 1 
ATOM   5460  N  N   . GLY B  1 90  ? 61.399  29.747  27.545  1.00 5.28  ? 90   GLY B N   1 
ATOM   5461  C  CA  . GLY B  1 90  ? 61.514  30.973  28.318  1.00 5.45  ? 90   GLY B CA  1 
ATOM   5462  C  C   . GLY B  1 90  ? 60.406  31.976  28.098  1.00 4.99  ? 90   GLY B C   1 
ATOM   5463  O  O   . GLY B  1 90  ? 60.649  33.149  27.796  1.00 5.79  ? 90   GLY B O   1 
ATOM   5464  N  N   . VAL B  1 91  ? 59.180  31.507  28.262  1.00 3.84  ? 91   VAL B N   1 
ATOM   5465  C  CA  . VAL B  1 91  ? 58.019  32.348  28.087  1.00 2.13  ? 91   VAL B CA  1 
ATOM   5466  C  C   . VAL B  1 91  ? 57.362  32.553  29.441  1.00 2.00  ? 91   VAL B C   1 
ATOM   5467  O  O   . VAL B  1 91  ? 56.150  32.719  29.521  1.00 2.90  ? 91   VAL B O   1 
ATOM   5468  C  CB  . VAL B  1 91  ? 57.013  31.659  27.197  1.00 2.00  ? 91   VAL B CB  1 
ATOM   5469  C  CG1 . VAL B  1 91  ? 56.480  30.426  27.916  1.00 2.69  ? 91   VAL B CG1 1 
ATOM   5470  C  CG2 . VAL B  1 91  ? 55.890  32.607  26.848  1.00 2.75  ? 91   VAL B CG2 1 
ATOM   5471  N  N   . LEU B  1 92  ? 58.148  32.547  30.511  1.00 2.00  ? 92   LEU B N   1 
ATOM   5472  C  CA  . LEU B  1 92  ? 57.561  32.680  31.842  1.00 2.74  ? 92   LEU B CA  1 
ATOM   5473  C  C   . LEU B  1 92  ? 57.892  33.941  32.615  1.00 3.56  ? 92   LEU B C   1 
ATOM   5474  O  O   . LEU B  1 92  ? 59.050  34.363  32.688  1.00 2.47  ? 92   LEU B O   1 
ATOM   5475  C  CB  . LEU B  1 92  ? 57.925  31.464  32.706  1.00 2.01  ? 92   LEU B CB  1 
ATOM   5476  C  CG  . LEU B  1 92  ? 57.255  30.108  32.449  1.00 2.00  ? 92   LEU B CG  1 
ATOM   5477  C  CD1 . LEU B  1 92  ? 57.384  29.707  30.995  1.00 2.00  ? 92   LEU B CD1 1 
ATOM   5478  C  CD2 . LEU B  1 92  ? 57.904  29.060  33.334  1.00 2.00  ? 92   LEU B CD2 1 
ATOM   5479  N  N   . ASP B  1 93  ? 56.847  34.534  33.193  1.00 4.85  ? 93   ASP B N   1 
ATOM   5480  C  CA  . ASP B  1 93  ? 56.968  35.743  34.002  1.00 5.16  ? 93   ASP B CA  1 
ATOM   5481  C  C   . ASP B  1 93  ? 57.986  35.310  35.023  1.00 5.43  ? 93   ASP B C   1 
ATOM   5482  O  O   . ASP B  1 93  ? 57.931  34.178  35.490  1.00 6.94  ? 93   ASP B O   1 
ATOM   5483  C  CB  . ASP B  1 93  ? 55.636  36.059  34.686  1.00 6.64  ? 93   ASP B CB  1 
ATOM   5484  C  CG  . ASP B  1 93  ? 55.634  37.414  35.378  1.00 7.95  ? 93   ASP B CG  1 
ATOM   5485  O  OD1 . ASP B  1 93  ? 56.601  37.694  36.126  1.00 7.12  ? 93   ASP B OD1 1 
ATOM   5486  O  OD2 . ASP B  1 93  ? 54.658  38.185  35.181  1.00 5.16  ? 93   ASP B OD2 1 
ATOM   5487  N  N   . GLN B  1 94  ? 58.907  36.188  35.385  1.00 5.11  ? 94   GLN B N   1 
ATOM   5488  C  CA  . GLN B  1 94  ? 59.936  35.772  36.314  1.00 5.12  ? 94   GLN B CA  1 
ATOM   5489  C  C   . GLN B  1 94  ? 59.923  36.349  37.710  1.00 4.78  ? 94   GLN B C   1 
ATOM   5490  O  O   . GLN B  1 94  ? 60.832  36.085  38.492  1.00 4.15  ? 94   GLN B O   1 
ATOM   5491  C  CB  . GLN B  1 94  ? 61.290  36.011  35.689  1.00 7.64  ? 94   GLN B CB  1 
ATOM   5492  C  CG  . GLN B  1 94  ? 62.303  35.010  36.121  1.00 13.35 ? 94   GLN B CG  1 
ATOM   5493  C  CD  . GLN B  1 94  ? 63.216  34.665  34.984  1.00 16.89 ? 94   GLN B CD  1 
ATOM   5494  O  OE1 . GLN B  1 94  ? 63.797  35.561  34.355  1.00 19.79 ? 94   GLN B OE1 1 
ATOM   5495  N  NE2 . GLN B  1 94  ? 63.350  33.366  34.694  1.00 18.16 ? 94   GLN B NE2 1 
ATOM   5496  N  N   . ASN B  1 95  ? 58.914  37.150  38.017  1.00 5.84  ? 95   ASN B N   1 
ATOM   5497  C  CA  . ASN B  1 95  ? 58.787  37.713  39.351  1.00 5.43  ? 95   ASN B CA  1 
ATOM   5498  C  C   . ASN B  1 95  ? 57.312  37.575  39.695  1.00 4.41  ? 95   ASN B C   1 
ATOM   5499  O  O   . ASN B  1 95  ? 56.685  38.514  40.167  1.00 3.21  ? 95   ASN B O   1 
ATOM   5500  C  CB  . ASN B  1 95  ? 59.236  39.184  39.386  1.00 10.02 ? 95   ASN B CB  1 
ATOM   5501  C  CG  . ASN B  1 95  ? 59.391  39.700  40.805  1.00 17.52 ? 95   ASN B CG  1 
ATOM   5502  O  OD1 . ASN B  1 95  ? 59.632  38.907  41.714  1.00 14.75 ? 95   ASN B OD1 1 
ATOM   5503  N  ND2 . ASN B  1 95  ? 59.267  41.014  41.005  1.00 28.64 ? 95   ASN B ND2 1 
ATOM   5504  N  N   . ARG B  1 96  ? 56.773  36.383  39.432  1.00 4.88  ? 96   ARG B N   1 
ATOM   5505  C  CA  . ARG B  1 96  ? 55.365  36.051  39.679  1.00 4.46  ? 96   ARG B CA  1 
ATOM   5506  C  C   . ARG B  1 96  ? 55.129  34.536  39.874  1.00 6.18  ? 96   ARG B C   1 
ATOM   5507  O  O   . ARG B  1 96  ? 55.320  33.738  38.950  1.00 7.03  ? 96   ARG B O   1 
ATOM   5508  C  CB  . ARG B  1 96  ? 54.511  36.542  38.506  1.00 2.18  ? 96   ARG B CB  1 
ATOM   5509  C  CG  . ARG B  1 96  ? 54.510  38.043  38.308  1.00 2.00  ? 96   ARG B CG  1 
ATOM   5510  C  CD  . ARG B  1 96  ? 53.942  38.718  39.535  1.00 2.65  ? 96   ARG B CD  1 
ATOM   5511  N  NE  . ARG B  1 96  ? 53.561  40.114  39.324  1.00 3.42  ? 96   ARG B NE  1 
ATOM   5512  C  CZ  . ARG B  1 96  ? 54.370  41.162  39.456  1.00 2.64  ? 96   ARG B CZ  1 
ATOM   5513  N  NH1 . ARG B  1 96  ? 55.641  41.001  39.800  1.00 2.00  ? 96   ARG B NH1 1 
ATOM   5514  N  NH2 . ARG B  1 96  ? 53.892  42.384  39.258  1.00 3.40  ? 96   ARG B NH2 1 
ATOM   5515  N  N   . SER B  1 97  ? 54.707  34.142  41.071  1.00 3.70  ? 97   SER B N   1 
ATOM   5516  C  CA  . SER B  1 97  ? 54.442  32.736  41.350  1.00 2.84  ? 97   SER B CA  1 
ATOM   5517  C  C   . SER B  1 97  ? 53.240  32.310  40.539  1.00 2.00  ? 97   SER B C   1 
ATOM   5518  O  O   . SER B  1 97  ? 52.535  33.151  40.000  1.00 2.00  ? 97   SER B O   1 
ATOM   5519  C  CB  . SER B  1 97  ? 54.119  32.538  42.830  1.00 3.87  ? 97   SER B CB  1 
ATOM   5520  O  OG  . SER B  1 97  ? 52.892  33.172  43.168  1.00 2.90  ? 97   SER B OG  1 
ATOM   5521  N  N   . LEU B  1 98  ? 53.005  31.005  40.463  1.00 2.00  ? 98   LEU B N   1 
ATOM   5522  C  CA  . LEU B  1 98  ? 51.857  30.478  39.740  1.00 2.00  ? 98   LEU B CA  1 
ATOM   5523  C  C   . LEU B  1 98  ? 50.650  30.945  40.522  1.00 2.00  ? 98   LEU B C   1 
ATOM   5524  O  O   . LEU B  1 98  ? 49.568  31.083  39.982  1.00 2.00  ? 98   LEU B O   1 
ATOM   5525  C  CB  . LEU B  1 98  ? 51.872  28.949  39.715  1.00 2.00  ? 98   LEU B CB  1 
ATOM   5526  C  CG  . LEU B  1 98  ? 51.171  28.209  38.566  1.00 2.00  ? 98   LEU B CG  1 
ATOM   5527  C  CD1 . LEU B  1 98  ? 50.356  27.077  39.142  1.00 2.00  ? 98   LEU B CD1 1 
ATOM   5528  C  CD2 . LEU B  1 98  ? 50.280  29.140  37.767  1.00 2.00  ? 98   LEU B CD2 1 
ATOM   5529  N  N   . LEU B  1 99  ? 50.846  31.186  41.809  1.00 2.00  ? 99   LEU B N   1 
ATOM   5530  C  CA  . LEU B  1 99  ? 49.771  31.663  42.668  1.00 2.00  ? 99   LEU B CA  1 
ATOM   5531  C  C   . LEU B  1 99  ? 49.186  32.980  42.160  1.00 2.29  ? 99   LEU B C   1 
ATOM   5532  O  O   . LEU B  1 99  ? 48.013  33.270  42.382  1.00 2.00  ? 99   LEU B O   1 
ATOM   5533  C  CB  . LEU B  1 99  ? 50.300  31.870  44.074  1.00 2.00  ? 99   LEU B CB  1 
ATOM   5534  C  CG  . LEU B  1 99  ? 49.296  32.454  45.051  1.00 2.00  ? 99   LEU B CG  1 
ATOM   5535  C  CD1 . LEU B  1 99  ? 48.005  31.678  44.996  1.00 2.00  ? 99   LEU B CD1 1 
ATOM   5536  C  CD2 . LEU B  1 99  ? 49.886  32.403  46.436  1.00 2.83  ? 99   LEU B CD2 1 
ATOM   5537  N  N   . PHE B  1 100 ? 50.033  33.757  41.482  1.00 2.65  ? 100  PHE B N   1 
ATOM   5538  C  CA  . PHE B  1 100 ? 49.697  35.056  40.906  1.00 2.00  ? 100  PHE B CA  1 
ATOM   5539  C  C   . PHE B  1 100 ? 48.567  34.997  39.894  1.00 3.01  ? 100  PHE B C   1 
ATOM   5540  O  O   . PHE B  1 100 ? 47.867  35.988  39.690  1.00 5.33  ? 100  PHE B O   1 
ATOM   5541  C  CB  . PHE B  1 100 ? 50.942  35.671  40.248  1.00 2.00  ? 100  PHE B CB  1 
ATOM   5542  C  CG  . PHE B  1 100 ? 50.686  36.977  39.525  1.00 2.00  ? 100  PHE B CG  1 
ATOM   5543  C  CD1 . PHE B  1 100 ? 50.046  38.040  40.162  1.00 2.00  ? 100  PHE B CD1 1 
ATOM   5544  C  CD2 . PHE B  1 100 ? 51.098  37.148  38.202  1.00 2.33  ? 100  PHE B CD2 1 
ATOM   5545  C  CE1 . PHE B  1 100 ? 49.819  39.251  39.489  1.00 2.00  ? 100  PHE B CE1 1 
ATOM   5546  C  CE2 . PHE B  1 100 ? 50.874  38.357  37.526  1.00 2.00  ? 100  PHE B CE2 1 
ATOM   5547  C  CZ  . PHE B  1 100 ? 50.237  39.404  38.170  1.00 2.00  ? 100  PHE B CZ  1 
ATOM   5548  N  N   . MET B  1 101 ? 48.401  33.866  39.217  1.00 2.83  ? 101  MET B N   1 
ATOM   5549  C  CA  . MET B  1 101 ? 47.299  33.788  38.280  1.00 2.00  ? 101  MET B CA  1 
ATOM   5550  C  C   . MET B  1 101 ? 46.187  32.960  38.875  1.00 2.37  ? 101  MET B C   1 
ATOM   5551  O  O   . MET B  1 101 ? 45.067  33.034  38.399  1.00 5.88  ? 101  MET B O   1 
ATOM   5552  C  CB  . MET B  1 101 ? 47.718  33.240  36.902  1.00 2.00  ? 101  MET B CB  1 
ATOM   5553  C  CG  . MET B  1 101 ? 48.108  31.773  36.792  1.00 2.00  ? 101  MET B CG  1 
ATOM   5554  S  SD  . MET B  1 101 ? 46.702  30.643  36.869  1.00 2.05  ? 101  MET B SD  1 
ATOM   5555  C  CE  . MET B  1 101 ? 45.586  31.450  35.820  1.00 2.00  ? 101  MET B CE  1 
ATOM   5556  N  N   . GLN B  1 102 ? 46.457  32.191  39.926  1.00 2.00  ? 102  GLN B N   1 
ATOM   5557  C  CA  . GLN B  1 102 ? 45.376  31.413  40.501  1.00 2.00  ? 102  GLN B CA  1 
ATOM   5558  C  C   . GLN B  1 102 ? 44.491  32.312  41.352  1.00 2.32  ? 102  GLN B C   1 
ATOM   5559  O  O   . GLN B  1 102 ? 43.264  32.182  41.330  1.00 2.98  ? 102  GLN B O   1 
ATOM   5560  C  CB  . GLN B  1 102 ? 45.891  30.248  41.335  1.00 2.00  ? 102  GLN B CB  1 
ATOM   5561  C  CG  . GLN B  1 102 ? 44.869  29.144  41.407  1.00 2.00  ? 102  GLN B CG  1 
ATOM   5562  C  CD  . GLN B  1 102 ? 44.202  28.907  40.062  1.00 2.00  ? 102  GLN B CD  1 
ATOM   5563  O  OE1 . GLN B  1 102 ? 44.730  28.222  39.196  1.00 3.23  ? 102  GLN B OE1 1 
ATOM   5564  N  NE2 . GLN B  1 102 ? 43.034  29.500  39.869  1.00 2.00  ? 102  GLN B NE2 1 
ATOM   5565  N  N   . TRP B  1 103 ? 45.097  33.240  42.088  1.00 2.00  ? 103  TRP B N   1 
ATOM   5566  C  CA  . TRP B  1 103 ? 44.307  34.144  42.912  1.00 3.42  ? 103  TRP B CA  1 
ATOM   5567  C  C   . TRP B  1 103 ? 43.514  35.066  42.004  1.00 3.51  ? 103  TRP B C   1 
ATOM   5568  O  O   . TRP B  1 103 ? 42.503  35.647  42.403  1.00 4.39  ? 103  TRP B O   1 
ATOM   5569  C  CB  . TRP B  1 103 ? 45.191  34.991  43.837  1.00 2.65  ? 103  TRP B CB  1 
ATOM   5570  C  CG  . TRP B  1 103 ? 44.367  35.794  44.753  1.00 2.00  ? 103  TRP B CG  1 
ATOM   5571  C  CD1 . TRP B  1 103 ? 44.083  37.117  44.660  1.00 2.00  ? 103  TRP B CD1 1 
ATOM   5572  C  CD2 . TRP B  1 103 ? 43.608  35.294  45.842  1.00 2.00  ? 103  TRP B CD2 1 
ATOM   5573  N  NE1 . TRP B  1 103 ? 43.184  37.477  45.626  1.00 2.00  ? 103  TRP B NE1 1 
ATOM   5574  C  CE2 . TRP B  1 103 ? 42.875  36.370  46.369  1.00 2.00  ? 103  TRP B CE2 1 
ATOM   5575  C  CE3 . TRP B  1 103 ? 43.474  34.031  46.426  1.00 2.00  ? 103  TRP B CE3 1 
ATOM   5576  C  CZ2 . TRP B  1 103 ? 42.017  36.224  47.456  1.00 2.00  ? 103  TRP B CZ2 1 
ATOM   5577  C  CZ3 . TRP B  1 103 ? 42.625  33.884  47.503  1.00 2.08  ? 103  TRP B CZ3 1 
ATOM   5578  C  CH2 . TRP B  1 103 ? 41.906  34.974  48.010  1.00 2.08  ? 103  TRP B CH2 1 
ATOM   5579  N  N   . GLY B  1 104 ? 43.988  35.213  40.779  1.00 2.00  ? 104  GLY B N   1 
ATOM   5580  C  CA  . GLY B  1 104 ? 43.286  36.078  39.865  1.00 2.00  ? 104  GLY B CA  1 
ATOM   5581  C  C   . GLY B  1 104 ? 41.960  35.442  39.542  1.00 2.00  ? 104  GLY B C   1 
ATOM   5582  O  O   . GLY B  1 104 ? 40.904  35.972  39.868  1.00 2.11  ? 104  GLY B O   1 
ATOM   5583  N  N   . GLN B  1 105 ? 42.025  34.276  38.916  1.00 2.00  ? 105  GLN B N   1 
ATOM   5584  C  CA  . GLN B  1 105 ? 40.834  33.546  38.518  1.00 2.01  ? 105  GLN B CA  1 
ATOM   5585  C  C   . GLN B  1 105 ? 39.811  33.401  39.626  1.00 2.00  ? 105  GLN B C   1 
ATOM   5586  O  O   . GLN B  1 105 ? 38.634  33.169  39.360  1.00 2.00  ? 105  GLN B O   1 
ATOM   5587  C  CB  . GLN B  1 105 ? 41.205  32.155  38.019  1.00 3.00  ? 105  GLN B CB  1 
ATOM   5588  C  CG  . GLN B  1 105 ? 40.000  31.394  37.532  1.00 3.74  ? 105  GLN B CG  1 
ATOM   5589  C  CD  . GLN B  1 105 ? 40.344  30.022  37.050  1.00 4.20  ? 105  GLN B CD  1 
ATOM   5590  O  OE1 . GLN B  1 105 ? 40.948  29.226  37.770  1.00 6.25  ? 105  GLN B OE1 1 
ATOM   5591  N  NE2 . GLN B  1 105 ? 39.957  29.713  35.820  1.00 3.42  ? 105  GLN B NE2 1 
ATOM   5592  N  N   . ILE B  1 106 ? 40.272  33.517  40.866  1.00 2.15  ? 106  ILE B N   1 
ATOM   5593  C  CA  . ILE B  1 106 ? 39.406  33.402  42.035  1.00 2.00  ? 106  ILE B CA  1 
ATOM   5594  C  C   . ILE B  1 106 ? 38.637  34.693  42.351  1.00 2.62  ? 106  ILE B C   1 
ATOM   5595  O  O   . ILE B  1 106 ? 37.408  34.671  42.505  1.00 2.13  ? 106  ILE B O   1 
ATOM   5596  C  CB  . ILE B  1 106 ? 40.220  32.976  43.278  1.00 2.00  ? 106  ILE B CB  1 
ATOM   5597  C  CG1 . ILE B  1 106 ? 40.470  31.465  43.245  1.00 2.00  ? 106  ILE B CG1 1 
ATOM   5598  C  CG2 . ILE B  1 106 ? 39.507  33.411  44.540  1.00 2.00  ? 106  ILE B CG2 1 
ATOM   5599  C  CD1 . ILE B  1 106 ? 41.315  30.953  44.396  1.00 2.00  ? 106  ILE B CD1 1 
ATOM   5600  N  N   . VAL B  1 107 ? 39.351  35.811  42.457  1.00 2.00  ? 107  VAL B N   1 
ATOM   5601  C  CA  . VAL B  1 107 ? 38.691  37.099  42.651  1.00 2.00  ? 107  VAL B CA  1 
ATOM   5602  C  C   . VAL B  1 107 ? 37.684  37.388  41.493  1.00 2.00  ? 107  VAL B C   1 
ATOM   5603  O  O   . VAL B  1 107 ? 36.591  37.913  41.723  1.00 3.50  ? 107  VAL B O   1 
ATOM   5604  C  CB  . VAL B  1 107 ? 39.775  38.212  42.711  1.00 2.00  ? 107  VAL B CB  1 
ATOM   5605  C  CG1 . VAL B  1 107 ? 39.118  39.578  42.807  1.00 2.00  ? 107  VAL B CG1 1 
ATOM   5606  C  CG2 . VAL B  1 107 ? 40.717  37.995  43.891  1.00 2.41  ? 107  VAL B CG2 1 
ATOM   5607  N  N   . ASP B  1 108 ? 38.075  37.039  40.189  1.00 2.00  ? 108  ASP B N   1 
ATOM   5608  C  CA  . ASP B  1 108 ? 37.227  37.203  38.927  1.00 2.00  ? 108  ASP B CA  1 
ATOM   5609  C  C   . ASP B  1 108 ? 35.920  36.508  39.240  1.00 2.00  ? 108  ASP B C   1 
ATOM   5610  O  O   . ASP B  1 108 ? 34.841  37.054  39.079  1.00 2.00  ? 108  ASP B O   1 
ATOM   5611  C  CB  . ASP B  1 108 ? 37.777  36.516  37.607  1.00 2.81  ? 108  ASP B CB  1 
ATOM   5612  C  CG  . ASP B  1 108 ? 36.871  36.474  36.334  1.00 2.17  ? 108  ASP B CG  1 
ATOM   5613  O  OD1 . ASP B  1 108 ? 35.885  35.704  36.316  1.00 2.00  ? 108  ASP B OD1 1 
ATOM   5614  O  OD2 . ASP B  1 108 ? 37.170  37.213  35.374  1.00 3.97  ? 108  ASP B OD2 1 
ATOM   5615  N  N   . HIS B  1 109 ? 36.085  35.229  39.686  1.00 3.73  ? 109  HIS B N   1 
ATOM   5616  C  CA  . HIS B  1 109 ? 34.968  34.323  40.010  1.00 3.49  ? 109  HIS B CA  1 
ATOM   5617  C  C   . HIS B  1 109 ? 34.074  34.773  41.141  1.00 2.79  ? 109  HIS B C   1 
ATOM   5618  O  O   . HIS B  1 109 ? 32.893  34.421  41.187  1.00 2.29  ? 109  HIS B O   1 
ATOM   5619  C  CB  . HIS B  1 109 ? 35.473  32.932  40.301  1.00 4.15  ? 109  HIS B CB  1 
ATOM   5620  C  CG  . HIS B  1 109 ? 35.809  32.142  39.023  1.00 3.43  ? 109  HIS B CG  1 
ATOM   5621  N  ND1 . HIS B  1 109 ? 35.850  30.767  38.984  1.00 4.35  ? 109  HIS B ND1 1 
ATOM   5622  C  CD2 . HIS B  1 109 ? 36.133  32.561  37.776  1.00 3.58  ? 109  HIS B CD2 1 
ATOM   5623  C  CE1 . HIS B  1 109 ? 36.184  30.369  37.771  1.00 3.82  ? 109  HIS B CE1 1 
ATOM   5624  N  NE2 . HIS B  1 109 ? 36.362  31.440  37.017  1.00 2.35  ? 109  HIS B NE2 1 
ATOM   5625  N  N   . ASP B  1 110 ? 34.631  35.538  42.068  1.00 2.00  ? 110  ASP B N   1 
ATOM   5626  C  CA  . ASP B  1 110 ? 33.806  36.041  43.142  1.00 2.57  ? 110  ASP B CA  1 
ATOM   5627  C  C   . ASP B  1 110 ? 32.991  37.212  42.599  1.00 2.00  ? 110  ASP B C   1 
ATOM   5628  O  O   . ASP B  1 110 ? 31.886  37.488  43.082  1.00 2.00  ? 110  ASP B O   1 
ATOM   5629  C  CB  . ASP B  1 110 ? 34.660  36.496  44.318  1.00 4.61  ? 110  ASP B CB  1 
ATOM   5630  C  CG  . ASP B  1 110 ? 33.763  37.023  45.419  1.00 5.71  ? 110  ASP B CG  1 
ATOM   5631  O  OD1 . ASP B  1 110 ? 33.000  37.967  45.153  1.00 7.95  ? 110  ASP B OD1 1 
ATOM   5632  O  OD2 . ASP B  1 110 ? 33.834  36.505  46.545  1.00 7.87  ? 110  ASP B OD2 1 
ATOM   5633  N  N   . LEU B  1 111 ? 33.522  37.912  41.601  1.00 2.21  ? 111  LEU B N   1 
ATOM   5634  C  CA  . LEU B  1 111 ? 32.827  39.058  41.034  1.00 2.00  ? 111  LEU B CA  1 
ATOM   5635  C  C   . LEU B  1 111 ? 31.819  38.818  39.886  1.00 2.00  ? 111  LEU B C   1 
ATOM   5636  O  O   . LEU B  1 111 ? 30.764  39.446  39.892  1.00 2.76  ? 111  LEU B O   1 
ATOM   5637  C  CB  . LEU B  1 111 ? 33.856  40.123  40.638  1.00 2.00  ? 111  LEU B CB  1 
ATOM   5638  C  CG  . LEU B  1 111 ? 34.825  40.524  41.761  1.00 2.00  ? 111  LEU B CG  1 
ATOM   5639  C  CD1 . LEU B  1 111 ? 35.742  41.630  41.283  1.00 2.00  ? 111  LEU B CD1 1 
ATOM   5640  C  CD2 . LEU B  1 111 ? 34.052  40.980  42.976  1.00 2.00  ? 111  LEU B CD2 1 
ATOM   5641  N  N   . ASP B  1 112 ? 32.088  37.936  38.915  1.00 2.00  ? 112  ASP B N   1 
ATOM   5642  C  CA  . ASP B  1 112 ? 31.090  37.751  37.840  1.00 3.30  ? 112  ASP B CA  1 
ATOM   5643  C  C   . ASP B  1 112 ? 30.872  36.385  37.177  1.00 2.97  ? 112  ASP B C   1 
ATOM   5644  O  O   . ASP B  1 112 ? 31.712  35.499  37.239  1.00 2.36  ? 112  ASP B O   1 
ATOM   5645  C  CB  . ASP B  1 112 ? 31.301  38.795  36.730  1.00 2.32  ? 112  ASP B CB  1 
ATOM   5646  C  CG  . ASP B  1 112 ? 32.706  38.786  36.161  1.00 2.00  ? 112  ASP B CG  1 
ATOM   5647  O  OD1 . ASP B  1 112 ? 33.636  39.176  36.889  1.00 2.23  ? 112  ASP B OD1 1 
ATOM   5648  O  OD2 . ASP B  1 112 ? 32.884  38.392  34.990  1.00 2.00  ? 112  ASP B OD2 1 
ATOM   5649  N  N   . PHE B  1 113 ? 29.715  36.234  36.533  1.00 4.45  ? 113  PHE B N   1 
ATOM   5650  C  CA  . PHE B  1 113 ? 29.374  34.993  35.848  1.00 6.47  ? 113  PHE B CA  1 
ATOM   5651  C  C   . PHE B  1 113 ? 28.129  35.149  34.984  1.00 7.39  ? 113  PHE B C   1 
ATOM   5652  O  O   . PHE B  1 113 ? 27.010  35.239  35.496  1.00 6.78  ? 113  PHE B O   1 
ATOM   5653  C  CB  . PHE B  1 113 ? 29.140  33.859  36.861  1.00 5.38  ? 113  PHE B CB  1 
ATOM   5654  C  CG  . PHE B  1 113 ? 28.813  32.507  36.231  1.00 5.42  ? 113  PHE B CG  1 
ATOM   5655  C  CD1 . PHE B  1 113 ? 29.431  32.097  35.048  1.00 4.13  ? 113  PHE B CD1 1 
ATOM   5656  C  CD2 . PHE B  1 113 ? 27.976  31.607  36.889  1.00 5.00  ? 113  PHE B CD2 1 
ATOM   5657  C  CE1 . PHE B  1 113 ? 29.228  30.815  34.545  1.00 3.00  ? 113  PHE B CE1 1 
ATOM   5658  C  CE2 . PHE B  1 113 ? 27.770  30.328  36.393  1.00 4.42  ? 113  PHE B CE2 1 
ATOM   5659  C  CZ  . PHE B  1 113 ? 28.400  29.929  35.220  1.00 3.32  ? 113  PHE B CZ  1 
ATOM   5660  N  N   . ALA B  1 114 ? 28.321  35.172  33.671  1.00 7.55  ? 114  ALA B N   1 
ATOM   5661  C  CA  . ALA B  1 114 ? 27.185  35.295  32.782  1.00 8.99  ? 114  ALA B CA  1 
ATOM   5662  C  C   . ALA B  1 114 ? 26.848  33.902  32.236  1.00 10.42 ? 114  ALA B C   1 
ATOM   5663  O  O   . ALA B  1 114 ? 27.515  33.383  31.325  1.00 10.27 ? 114  ALA B O   1 
ATOM   5664  C  CB  . ALA B  1 114 ? 27.507  36.281  31.656  1.00 8.23  ? 114  ALA B CB  1 
ATOM   5665  N  N   . PRO B  1 115 ? 25.803  33.275  32.790  1.00 11.95 ? 115  PRO B N   1 
ATOM   5666  C  CA  . PRO B  1 115 ? 25.355  31.944  32.400  1.00 14.14 ? 115  PRO B CA  1 
ATOM   5667  C  C   . PRO B  1 115 ? 25.182  31.780  30.914  1.00 18.01 ? 115  PRO B C   1 
ATOM   5668  O  O   . PRO B  1 115 ? 24.713  32.683  30.225  1.00 18.71 ? 115  PRO B O   1 
ATOM   5669  C  CB  . PRO B  1 115 ? 24.025  31.805  33.119  1.00 14.01 ? 115  PRO B CB  1 
ATOM   5670  C  CG  . PRO B  1 115 ? 24.244  32.642  34.332  1.00 14.60 ? 115  PRO B CG  1 
ATOM   5671  C  CD  . PRO B  1 115 ? 24.781  33.868  33.650  1.00 13.15 ? 115  PRO B CD  1 
ATOM   5672  N  N   . GLU B  1 116 ? 25.570  30.617  30.423  1.00 21.77 ? 116  GLU B N   1 
ATOM   5673  C  CA  . GLU B  1 116 ? 25.393  30.336  29.019  1.00 25.65 ? 116  GLU B CA  1 
ATOM   5674  C  C   . GLU B  1 116 ? 23.913  29.961  28.997  1.00 27.66 ? 116  GLU B C   1 
ATOM   5675  O  O   . GLU B  1 116 ? 23.341  29.627  30.042  1.00 27.56 ? 116  GLU B O   1 
ATOM   5676  C  CB  . GLU B  1 116 ? 26.265  29.154  28.587  1.00 26.28 ? 116  GLU B CB  1 
ATOM   5677  C  CG  . GLU B  1 116 ? 26.937  29.354  27.229  1.00 26.86 ? 116  GLU B CG  1 
ATOM   5678  C  CD  . GLU B  1 116 ? 28.144  28.453  27.015  1.00 27.35 ? 116  GLU B CD  1 
ATOM   5679  O  OE1 . GLU B  1 116 ? 27.990  27.213  27.037  1.00 28.18 ? 116  GLU B OE1 1 
ATOM   5680  O  OE2 . GLU B  1 116 ? 29.253  28.993  26.818  1.00 27.55 ? 116  GLU B OE2 1 
ATOM   5681  N  N   . THR B  1 117 ? 23.286  30.048  27.833  1.00 29.59 ? 117  THR B N   1 
ATOM   5682  C  CA  . THR B  1 117 ? 21.911  29.674  27.704  1.00 32.45 ? 117  THR B CA  1 
ATOM   5683  C  C   . THR B  1 117 ? 21.797  28.298  27.101  1.00 37.16 ? 117  THR B C   1 
ATOM   5684  O  O   . THR B  1 117 ? 22.351  28.041  26.023  1.00 37.81 ? 117  THR B O   1 
ATOM   5685  C  CB  . THR B  1 117 ? 21.198  30.564  26.687  1.00 31.27 ? 117  THR B CB  1 
ATOM   5686  O  OG1 . THR B  1 117 ? 21.892  30.499  25.430  1.00 31.03 ? 117  THR B OG1 1 
ATOM   5687  C  CG2 . THR B  1 117 ? 21.162  31.996  27.192  1.00 31.78 ? 117  THR B CG2 1 
ATOM   5688  N  N   . GLU B  1 118 ? 21.123  27.508  27.818  1.00 42.80 ? 118  GLU B N   1 
ATOM   5689  C  CA  . GLU B  1 118 ? 20.848  26.183  27.489  1.00 46.63 ? 118  GLU B CA  1 
ATOM   5690  C  C   . GLU B  1 118 ? 19.487  26.033  28.021  1.00 50.78 ? 118  GLU B C   1 
ATOM   5691  O  O   . GLU B  1 118 ? 19.317  25.962  29.230  1.00 50.78 ? 118  GLU B O   1 
ATOM   5692  C  CB  . GLU B  1 118 ? 21.648  25.195  28.299  1.00 45.95 ? 118  GLU B CB  1 
ATOM   5693  C  CG  . GLU B  1 118 ? 21.711  23.813  27.777  1.00 46.02 ? 118  GLU B CG  1 
ATOM   5694  C  CD  . GLU B  1 118 ? 23.126  23.395  27.938  1.00 47.97 ? 118  GLU B CD  1 
ATOM   5695  O  OE1 . GLU B  1 118 ? 23.441  22.579  28.826  1.00 48.93 ? 118  GLU B OE1 1 
ATOM   5696  O  OE2 . GLU B  1 118 ? 23.975  23.883  27.144  1.00 47.79 ? 118  GLU B OE2 1 
ATOM   5697  N  N   . LEU B  1 119 ? 18.545  26.029  27.178  1.00 53.75 ? 119  LEU B N   1 
ATOM   5698  C  CA  . LEU B  1 119 ? 17.309  25.569  27.681  1.00 55.67 ? 119  LEU B CA  1 
ATOM   5699  C  C   . LEU B  1 119 ? 17.544  24.197  27.143  1.00 58.16 ? 119  LEU B C   1 
ATOM   5700  O  O   . LEU B  1 119 ? 18.467  24.091  26.327  1.00 57.74 ? 119  LEU B O   1 
ATOM   5701  C  CB  . LEU B  1 119 ? 16.092  26.203  27.055  1.00 55.54 ? 119  LEU B CB  1 
ATOM   5702  C  CG  . LEU B  1 119 ? 16.230  27.688  26.707  1.00 56.00 ? 119  LEU B CG  1 
ATOM   5703  C  CD1 . LEU B  1 119 ? 17.335  28.319  27.529  1.00 55.42 ? 119  LEU B CD1 1 
ATOM   5704  C  CD2 . LEU B  1 119 ? 16.497  27.872  25.231  1.00 56.41 ? 119  LEU B CD2 1 
ATOM   5705  N  N   . GLY B  1 120 ? 16.854  23.132  27.440  1.00 60.54 ? 120  GLY B N   1 
ATOM   5706  C  CA  . GLY B  1 120 ? 17.423  21.967  26.831  1.00 63.66 ? 120  GLY B CA  1 
ATOM   5707  C  C   . GLY B  1 120 ? 18.333  21.324  27.856  1.00 65.08 ? 120  GLY B C   1 
ATOM   5708  O  O   . GLY B  1 120 ? 19.381  21.834  28.250  1.00 65.09 ? 120  GLY B O   1 
ATOM   5709  N  N   . SER B  1 121 ? 17.761  20.149  28.230  1.00 65.77 ? 121  SER B N   1 
ATOM   5710  C  CA  . SER B  1 121 ? 18.218  19.120  29.204  1.00 66.96 ? 121  SER B CA  1 
ATOM   5711  C  C   . SER B  1 121 ? 17.677  17.641  28.948  1.00 67.61 ? 121  SER B C   1 
ATOM   5712  O  O   . SER B  1 121 ? 17.719  16.780  29.840  1.00 68.05 ? 121  SER B O   1 
ATOM   5713  C  CB  . SER B  1 121 ? 17.845  19.559  30.612  1.00 66.71 ? 121  SER B CB  1 
ATOM   5714  O  OG  . SER B  1 121 ? 17.969  18.490  31.538  1.00 66.31 ? 121  SER B OG  1 
ATOM   5715  N  N   . SER B  1 122 ? 17.197  17.413  27.760  1.00 67.87 ? 122  SER B N   1 
ATOM   5716  C  CA  . SER B  1 122 ? 16.744  16.232  27.092  1.00 68.12 ? 122  SER B CA  1 
ATOM   5717  C  C   . SER B  1 122 ? 17.312  16.727  25.625  1.00 67.81 ? 122  SER B C   1 
ATOM   5718  O  O   . SER B  1 122 ? 18.222  16.060  25.104  1.00 68.14 ? 122  SER B O   1 
ATOM   5719  C  CB  . SER B  1 122 ? 15.260  15.856  27.380  1.00 68.64 ? 122  SER B CB  1 
ATOM   5720  O  OG  . SER B  1 122 ? 15.150  15.152  28.608  1.00 69.46 ? 122  SER B OG  1 
ATOM   5721  N  N   . GLU B  1 123 ? 16.814  17.860  24.952  1.00 66.61 ? 123  GLU B N   1 
ATOM   5722  C  CA  . GLU B  1 123 ? 17.098  18.599  23.597  1.00 64.45 ? 123  GLU B CA  1 
ATOM   5723  C  C   . GLU B  1 123 ? 18.062  18.103  22.454  1.00 62.46 ? 123  GLU B C   1 
ATOM   5724  O  O   . GLU B  1 123 ? 19.107  17.501  22.687  1.00 62.19 ? 123  GLU B O   1 
ATOM   5725  C  CB  . GLU B  1 123 ? 17.477  20.042  23.933  1.00 65.37 ? 123  GLU B CB  1 
ATOM   5726  C  CG  . GLU B  1 123 ? 17.599  20.921  22.702  1.00 65.72 ? 123  GLU B CG  1 
ATOM   5727  C  CD  . GLU B  1 123 ? 16.753  22.180  22.846  1.00 66.50 ? 123  GLU B CD  1 
ATOM   5728  O  OE1 . GLU B  1 123 ? 15.773  22.139  23.609  1.00 66.65 ? 123  GLU B OE1 1 
ATOM   5729  O  OE2 . GLU B  1 123 ? 17.084  23.203  22.205  1.00 67.21 ? 123  GLU B OE2 1 
ATOM   5730  N  N   . HIS B  1 124 ? 17.675  18.435  21.185  1.00 59.54 ? 124  HIS B N   1 
ATOM   5731  C  CA  . HIS B  1 124 ? 18.401  18.162  19.916  1.00 57.71 ? 124  HIS B CA  1 
ATOM   5732  C  C   . HIS B  1 124 ? 18.692  19.490  19.165  1.00 55.92 ? 124  HIS B C   1 
ATOM   5733  O  O   . HIS B  1 124 ? 19.505  19.486  18.242  1.00 56.03 ? 124  HIS B O   1 
ATOM   5734  C  CB  . HIS B  1 124 ? 17.595  17.282  18.981  1.00 57.10 ? 124  HIS B CB  1 
ATOM   5735  C  CG  . HIS B  1 124 ? 18.113  15.991  18.236  1.00 55.94 ? 124  HIS B CG  1 
ATOM   5736  N  ND1 . HIS B  1 124 ? 17.169  15.278  17.550  1.00 54.62 ? 124  HIS B ND1 1 
ATOM   5737  C  CD2 . HIS B  1 124 ? 19.272  15.298  18.068  1.00 55.29 ? 124  HIS B CD2 1 
ATOM   5738  C  CE1 . HIS B  1 124 ? 17.694  14.213  16.989  1.00 54.32 ? 124  HIS B CE1 1 
ATOM   5739  N  NE2 . HIS B  1 124 ? 18.975  14.195  17.294  1.00 54.90 ? 124  HIS B NE2 1 
ATOM   5740  N  N   . SER B  1 125 ? 18.065  20.649  19.531  1.00 52.98 ? 125  SER B N   1 
ATOM   5741  C  CA  . SER B  1 125 ? 18.462  21.964  18.999  1.00 50.84 ? 125  SER B CA  1 
ATOM   5742  C  C   . SER B  1 125 ? 19.858  22.193  19.570  1.00 49.25 ? 125  SER B C   1 
ATOM   5743  O  O   . SER B  1 125 ? 20.665  22.943  19.019  1.00 49.56 ? 125  SER B O   1 
ATOM   5744  C  CB  . SER B  1 125 ? 17.516  23.094  19.454  1.00 50.96 ? 125  SER B CB  1 
ATOM   5745  O  OG  . SER B  1 125 ? 16.256  22.995  18.800  1.00 50.76 ? 125  SER B OG  1 
ATOM   5746  N  N   . LYS B  1 126 ? 20.082  21.526  20.695  1.00 46.06 ? 126  LYS B N   1 
ATOM   5747  C  CA  . LYS B  1 126 ? 21.362  21.536  21.380  1.00 42.86 ? 126  LYS B CA  1 
ATOM   5748  C  C   . LYS B  1 126 ? 22.319  20.888  20.380  1.00 42.52 ? 126  LYS B C   1 
ATOM   5749  O  O   . LYS B  1 126 ? 23.506  21.201  20.331  1.00 42.16 ? 126  LYS B O   1 
ATOM   5750  C  CB  . LYS B  1 126 ? 21.243  20.672  22.633  1.00 41.15 ? 126  LYS B CB  1 
ATOM   5751  C  CG  . LYS B  1 126 ? 22.352  20.802  23.652  1.00 39.63 ? 126  LYS B CG  1 
ATOM   5752  C  CD  . LYS B  1 126 ? 22.067  19.882  24.843  1.00 38.42 ? 126  LYS B CD  1 
ATOM   5753  C  CE  . LYS B  1 126 ? 20.710  20.187  25.468  1.00 37.15 ? 126  LYS B CE  1 
ATOM   5754  N  NZ  . LYS B  1 126 ? 20.297  19.163  26.458  1.00 35.68 ? 126  LYS B NZ  1 
ATOM   5755  N  N   . VAL B  1 127 ? 21.764  19.997  19.563  1.00 42.46 ? 127  VAL B N   1 
ATOM   5756  C  CA  . VAL B  1 127 ? 22.518  19.254  18.559  1.00 42.13 ? 127  VAL B CA  1 
ATOM   5757  C  C   . VAL B  1 127 ? 22.549  19.864  17.155  1.00 42.02 ? 127  VAL B C   1 
ATOM   5758  O  O   . VAL B  1 127 ? 23.460  19.564  16.374  1.00 40.91 ? 127  VAL B O   1 
ATOM   5759  C  CB  . VAL B  1 127 ? 21.991  17.806  18.462  1.00 42.00 ? 127  VAL B CB  1 
ATOM   5760  C  CG1 . VAL B  1 127 ? 22.738  17.041  17.379  1.00 42.51 ? 127  VAL B CG1 1 
ATOM   5761  C  CG2 . VAL B  1 127 ? 22.151  17.115  19.811  1.00 42.62 ? 127  VAL B CG2 1 
ATOM   5762  N  N   . GLN B  1 128 ? 21.568  20.701  16.814  1.00 42.07 ? 128  GLN B N   1 
ATOM   5763  C  CA  . GLN B  1 128 ? 21.586  21.312  15.487  1.00 41.38 ? 128  GLN B CA  1 
ATOM   5764  C  C   . GLN B  1 128 ? 22.771  22.268  15.438  1.00 38.75 ? 128  GLN B C   1 
ATOM   5765  O  O   . GLN B  1 128 ? 23.179  22.721  14.366  1.00 37.75 ? 128  GLN B O   1 
ATOM   5766  C  CB  . GLN B  1 128 ? 20.283  22.069  15.158  1.00 45.12 ? 128  GLN B CB  1 
ATOM   5767  C  CG  . GLN B  1 128 ? 20.372  22.770  13.783  1.00 52.09 ? 128  GLN B CG  1 
ATOM   5768  C  CD  . GLN B  1 128 ? 19.039  23.220  13.160  1.00 55.22 ? 128  GLN B CD  1 
ATOM   5769  O  OE1 . GLN B  1 128 ? 19.029  23.826  12.079  1.00 57.40 ? 128  GLN B OE1 1 
ATOM   5770  N  NE2 . GLN B  1 128 ? 17.922  22.922  13.824  1.00 57.60 ? 128  GLN B NE2 1 
ATOM   5771  N  N   . CYS B  1 129 ? 23.333  22.559  16.609  1.00 34.60 ? 129  CYS B N   1 
ATOM   5772  C  CA  . CYS B  1 129 ? 24.486  23.444  16.685  1.00 30.68 ? 129  CYS B CA  1 
ATOM   5773  C  C   . CYS B  1 129 ? 25.789  22.633  16.756  1.00 30.59 ? 129  CYS B C   1 
ATOM   5774  O  O   . CYS B  1 129 ? 26.712  22.893  15.986  1.00 32.79 ? 129  CYS B O   1 
ATOM   5775  C  CB  . CYS B  1 129 ? 24.363  24.383  17.886  1.00 27.08 ? 129  CYS B CB  1 
ATOM   5776  S  SG  . CYS B  1 129 ? 25.323  25.938  17.790  1.00 22.08 ? 129  CYS B SG  1 
ATOM   5777  N  N   . GLU B  1 130 ? 25.889  21.643  17.640  1.00 27.37 ? 130  GLU B N   1 
ATOM   5778  C  CA  . GLU B  1 130 ? 27.140  20.899  17.677  1.00 24.21 ? 130  GLU B CA  1 
ATOM   5779  C  C   . GLU B  1 130 ? 27.354  20.101  16.381  1.00 24.79 ? 130  GLU B C   1 
ATOM   5780  O  O   . GLU B  1 130 ? 28.490  19.979  15.929  1.00 25.36 ? 130  GLU B O   1 
ATOM   5781  C  CB  . GLU B  1 130 ? 27.223  19.953  18.902  1.00 23.21 ? 130  GLU B CB  1 
ATOM   5782  C  CG  . GLU B  1 130 ? 28.687  19.514  19.251  1.00 21.29 ? 130  GLU B CG  1 
ATOM   5783  C  CD  . GLU B  1 130 ? 28.811  18.450  20.360  1.00 19.55 ? 130  GLU B CD  1 
ATOM   5784  O  OE1 . GLU B  1 130 ? 29.950  18.199  20.824  1.00 15.99 ? 130  GLU B OE1 1 
ATOM   5785  O  OE2 . GLU B  1 130 ? 27.786  17.865  20.766  1.00 19.09 ? 130  GLU B OE2 1 
ATOM   5786  N  N   . GLU B  1 131 ? 26.284  19.603  15.752  1.00 24.25 ? 131  GLU B N   1 
ATOM   5787  C  CA  . GLU B  1 131 ? 26.444  18.775  14.539  1.00 24.55 ? 131  GLU B CA  1 
ATOM   5788  C  C   . GLU B  1 131 ? 26.275  19.381  13.129  1.00 22.89 ? 131  GLU B C   1 
ATOM   5789  O  O   . GLU B  1 131 ? 26.791  18.822  12.159  1.00 22.07 ? 131  GLU B O   1 
ATOM   5790  C  CB  . GLU B  1 131 ? 25.533  17.532  14.619  1.00 27.11 ? 131  GLU B CB  1 
ATOM   5791  C  CG  . GLU B  1 131 ? 25.669  16.631  15.873  1.00 29.72 ? 131  GLU B CG  1 
ATOM   5792  C  CD  . GLU B  1 131 ? 26.935  15.772  15.905  1.00 30.67 ? 131  GLU B CD  1 
ATOM   5793  O  OE1 . GLU B  1 131 ? 27.307  15.205  14.854  1.00 30.91 ? 131  GLU B OE1 1 
ATOM   5794  O  OE2 . GLU B  1 131 ? 27.545  15.648  16.993  1.00 31.76 ? 131  GLU B OE2 1 
ATOM   5795  N  N   . TYR B  1 132 ? 25.558  20.493  12.993  1.00 21.73 ? 132  TYR B N   1 
ATOM   5796  C  CA  . TYR B  1 132 ? 25.355  21.081  11.662  1.00 19.80 ? 132  TYR B CA  1 
ATOM   5797  C  C   . TYR B  1 132 ? 25.919  22.491  11.466  1.00 18.32 ? 132  TYR B C   1 
ATOM   5798  O  O   . TYR B  1 132 ? 25.992  22.995  10.339  1.00 17.42 ? 132  TYR B O   1 
ATOM   5799  C  CB  . TYR B  1 132 ? 23.865  21.081  11.307  1.00 21.08 ? 132  TYR B CB  1 
ATOM   5800  C  CG  . TYR B  1 132 ? 23.267  19.701  11.199  1.00 22.21 ? 132  TYR B CG  1 
ATOM   5801  C  CD1 . TYR B  1 132 ? 22.489  19.174  12.228  1.00 23.63 ? 132  TYR B CD1 1 
ATOM   5802  C  CD2 . TYR B  1 132 ? 23.499  18.909  10.079  1.00 23.11 ? 132  TYR B CD2 1 
ATOM   5803  C  CE1 . TYR B  1 132 ? 21.955  17.888  12.145  1.00 24.37 ? 132  TYR B CE1 1 
ATOM   5804  C  CE2 . TYR B  1 132 ? 22.972  17.621  9.985   1.00 24.08 ? 132  TYR B CE2 1 
ATOM   5805  C  CZ  . TYR B  1 132 ? 22.202  17.119  11.023  1.00 23.95 ? 132  TYR B CZ  1 
ATOM   5806  O  OH  . TYR B  1 132 ? 21.685  15.849  10.950  1.00 24.53 ? 132  TYR B OH  1 
ATOM   5807  N  N   . CYS B  1 133 ? 26.320  23.121  12.562  1.00 15.51 ? 133  CYS B N   1 
ATOM   5808  C  CA  . CYS B  1 133 ? 26.878  24.463  12.508  1.00 13.52 ? 133  CYS B CA  1 
ATOM   5809  C  C   . CYS B  1 133 ? 25.966  25.433  11.761  1.00 14.35 ? 133  CYS B C   1 
ATOM   5810  O  O   . CYS B  1 133 ? 26.368  26.075  10.786  1.00 15.46 ? 133  CYS B O   1 
ATOM   5811  C  CB  . CYS B  1 133 ? 28.268  24.435  11.861  1.00 11.56 ? 133  CYS B CB  1 
ATOM   5812  S  SG  . CYS B  1 133 ? 29.501  23.445  12.768  1.00 7.17  ? 133  CYS B SG  1 
ATOM   5813  N  N   . ILE B  1 134 ? 24.731  25.533  12.236  1.00 14.20 ? 134  ILE B N   1 
ATOM   5814  C  CA  . ILE B  1 134 ? 23.746  26.426  11.648  1.00 12.94 ? 134  ILE B CA  1 
ATOM   5815  C  C   . ILE B  1 134 ? 23.371  27.525  12.648  1.00 13.89 ? 134  ILE B C   1 
ATOM   5816  O  O   . ILE B  1 134 ? 22.848  27.250  13.730  1.00 12.44 ? 134  ILE B O   1 
ATOM   5817  C  CB  . ILE B  1 134 ? 22.468  25.643  11.241  1.00 11.73 ? 134  ILE B CB  1 
ATOM   5818  C  CG1 . ILE B  1 134 ? 22.592  25.167  9.797   1.00 9.58  ? 134  ILE B CG1 1 
ATOM   5819  C  CG2 . ILE B  1 134 ? 21.230  26.496  11.450  1.00 12.38 ? 134  ILE B CG2 1 
ATOM   5820  C  CD1 . ILE B  1 134 ? 22.952  23.724  9.676   1.00 8.50  ? 134  ILE B CD1 1 
ATOM   5821  N  N   . GLN B  1 135 ? 23.652  28.705  12.174  1.00 15.17 ? 135  GLN B N   1 
ATOM   5822  C  CA  . GLN B  1 135 ? 23.308  29.882  12.891  1.00 16.49 ? 135  GLN B CA  1 
ATOM   5823  C  C   . GLN B  1 135 ? 21.830  30.052  12.813  1.00 16.39 ? 135  GLN B C   1 
ATOM   5824  O  O   . GLN B  1 135 ? 21.210  29.907  11.767  1.00 16.55 ? 135  GLN B O   1 
ATOM   5825  C  CB  . GLN B  1 135 ? 23.941  31.118  12.245  1.00 17.89 ? 135  GLN B CB  1 
ATOM   5826  C  CG  . GLN B  1 135 ? 24.286  32.291  13.110  1.00 20.98 ? 135  GLN B CG  1 
ATOM   5827  C  CD  . GLN B  1 135 ? 25.278  33.109  12.293  1.00 24.20 ? 135  GLN B CD  1 
ATOM   5828  O  OE1 . GLN B  1 135 ? 26.490  32.840  12.302  1.00 26.80 ? 135  GLN B OE1 1 
ATOM   5829  N  NE2 . GLN B  1 135 ? 24.990  34.145  11.531  1.00 23.97 ? 135  GLN B NE2 1 
ATOM   5830  N  N   . GLY B  1 136 ? 21.264  30.420  13.955  1.00 15.86 ? 136  GLY B N   1 
ATOM   5831  C  CA  . GLY B  1 136 ? 19.839  30.644  14.150  1.00 17.04 ? 136  GLY B CA  1 
ATOM   5832  C  C   . GLY B  1 136 ? 19.490  30.490  15.663  1.00 18.74 ? 136  GLY B C   1 
ATOM   5833  O  O   . GLY B  1 136 ? 19.883  29.498  16.269  1.00 20.30 ? 136  GLY B O   1 
ATOM   5834  N  N   . ASP B  1 137 ? 18.747  31.435  16.252  1.00 18.20 ? 137  ASP B N   1 
ATOM   5835  C  CA  . ASP B  1 137 ? 18.435  31.489  17.723  1.00 18.57 ? 137  ASP B CA  1 
ATOM   5836  C  C   . ASP B  1 137 ? 19.719  31.584  18.564  1.00 17.63 ? 137  ASP B C   1 
ATOM   5837  O  O   . ASP B  1 137 ? 20.679  32.246  18.167  1.00 15.35 ? 137  ASP B O   1 
ATOM   5838  C  CB  . ASP B  1 137 ? 17.616  30.267  18.216  1.00 21.21 ? 137  ASP B CB  1 
ATOM   5839  C  CG  . ASP B  1 137 ? 16.222  30.622  18.749  1.00 24.36 ? 137  ASP B CG  1 
ATOM   5840  O  OD1 . ASP B  1 137 ? 15.421  31.212  17.989  1.00 26.51 ? 137  ASP B OD1 1 
ATOM   5841  O  OD2 . ASP B  1 137 ? 15.940  30.322  19.925  1.00 26.17 ? 137  ASP B OD2 1 
ATOM   5842  N  N   . ASN B  1 138 ? 19.753  30.948  19.707  1.00 17.11 ? 138  ASN B N   1 
ATOM   5843  C  CA  . ASN B  1 138 ? 20.865  31.052  20.632  1.00 15.35 ? 138  ASN B CA  1 
ATOM   5844  C  C   . ASN B  1 138 ? 22.218  30.446  20.164  1.00 14.38 ? 138  ASN B C   1 
ATOM   5845  O  O   . ASN B  1 138 ? 23.232  30.612  20.816  1.00 14.14 ? 138  ASN B O   1 
ATOM   5846  C  CB  . ASN B  1 138 ? 20.439  30.404  21.941  1.00 16.19 ? 138  ASN B CB  1 
ATOM   5847  C  CG  . ASN B  1 138 ? 19.517  31.310  22.707  1.00 17.94 ? 138  ASN B CG  1 
ATOM   5848  O  OD1 . ASN B  1 138 ? 19.953  32.331  23.250  1.00 18.70 ? 138  ASN B OD1 1 
ATOM   5849  N  ND2 . ASN B  1 138 ? 18.235  30.957  22.766  1.00 17.51 ? 138  ASN B ND2 1 
ATOM   5850  N  N   . CYS B  1 139 ? 22.194  29.747  19.032  1.00 12.34 ? 139  CYS B N   1 
ATOM   5851  C  CA  . CYS B  1 139 ? 23.383  29.120  18.463  1.00 11.96 ? 139  CYS B CA  1 
ATOM   5852  C  C   . CYS B  1 139 ? 24.102  30.144  17.596  1.00 9.95  ? 139  CYS B C   1 
ATOM   5853  O  O   . CYS B  1 139 ? 23.545  30.651  16.618  1.00 10.22 ? 139  CYS B O   1 
ATOM   5854  C  CB  . CYS B  1 139 ? 22.977  27.907  17.620  1.00 15.63 ? 139  CYS B CB  1 
ATOM   5855  S  SG  . CYS B  1 139 ? 24.248  27.134  16.544  1.00 21.45 ? 139  CYS B SG  1 
ATOM   5856  N  N   . PHE B  1 140 ? 25.341  30.448  17.962  1.00 5.44  ? 140  PHE B N   1 
ATOM   5857  C  CA  . PHE B  1 140 ? 26.133  31.418  17.228  1.00 2.49  ? 140  PHE B CA  1 
ATOM   5858  C  C   . PHE B  1 140 ? 27.533  30.856  17.010  1.00 3.11  ? 140  PHE B C   1 
ATOM   5859  O  O   . PHE B  1 140 ? 28.512  31.362  17.544  1.00 2.99  ? 140  PHE B O   1 
ATOM   5860  C  CB  . PHE B  1 140 ? 26.173  32.715  18.020  1.00 2.10  ? 140  PHE B CB  1 
ATOM   5861  C  CG  . PHE B  1 140 ? 27.012  33.787  17.402  1.00 2.67  ? 140  PHE B CG  1 
ATOM   5862  C  CD1 . PHE B  1 140 ? 27.279  33.797  16.044  1.00 2.75  ? 140  PHE B CD1 1 
ATOM   5863  C  CD2 . PHE B  1 140 ? 27.509  34.818  18.185  1.00 2.83  ? 140  PHE B CD2 1 
ATOM   5864  C  CE1 . PHE B  1 140 ? 28.028  34.819  15.479  1.00 2.34  ? 140  PHE B CE1 1 
ATOM   5865  C  CE2 . PHE B  1 140 ? 28.254  35.840  17.628  1.00 3.06  ? 140  PHE B CE2 1 
ATOM   5866  C  CZ  . PHE B  1 140 ? 28.514  35.841  16.271  1.00 2.68  ? 140  PHE B CZ  1 
ATOM   5867  N  N   . PRO B  1 141 ? 27.634  29.792  16.201  1.00 4.12  ? 141  PRO B N   1 
ATOM   5868  C  CA  . PRO B  1 141 ? 28.843  29.055  15.825  1.00 2.95  ? 141  PRO B CA  1 
ATOM   5869  C  C   . PRO B  1 141 ? 30.097  29.863  15.514  1.00 3.52  ? 141  PRO B C   1 
ATOM   5870  O  O   . PRO B  1 141 ? 30.026  30.957  14.950  1.00 3.56  ? 141  PRO B O   1 
ATOM   5871  C  CB  . PRO B  1 141 ? 28.386  28.260  14.606  1.00 3.70  ? 141  PRO B CB  1 
ATOM   5872  C  CG  . PRO B  1 141 ? 26.980  27.948  14.927  1.00 3.21  ? 141  PRO B CG  1 
ATOM   5873  C  CD  . PRO B  1 141 ? 26.473  29.269  15.454  1.00 5.04  ? 141  PRO B CD  1 
ATOM   5874  N  N   . ILE B  1 142 ? 31.244  29.290  15.877  1.00 3.46  ? 142  ILE B N   1 
ATOM   5875  C  CA  . ILE B  1 142 ? 32.546  29.894  15.611  1.00 4.21  ? 142  ILE B CA  1 
ATOM   5876  C  C   . ILE B  1 142 ? 33.124  29.155  14.400  1.00 5.88  ? 142  ILE B C   1 
ATOM   5877  O  O   . ILE B  1 142 ? 33.718  28.087  14.540  1.00 6.56  ? 142  ILE B O   1 
ATOM   5878  C  CB  . ILE B  1 142 ? 33.515  29.724  16.801  1.00 2.00  ? 142  ILE B CB  1 
ATOM   5879  C  CG1 . ILE B  1 142 ? 32.975  30.456  18.032  1.00 2.10  ? 142  ILE B CG1 1 
ATOM   5880  C  CG2 . ILE B  1 142 ? 34.875  30.270  16.429  1.00 2.00  ? 142  ILE B CG2 1 
ATOM   5881  C  CD1 . ILE B  1 142 ? 33.888  30.392  19.241  1.00 2.00  ? 142  ILE B CD1 1 
ATOM   5882  N  N   . MET B  1 143 ? 32.932  29.720  13.212  1.00 5.82  ? 143  MET B N   1 
ATOM   5883  C  CA  . MET B  1 143 ? 33.415  29.116  11.973  1.00 6.28  ? 143  MET B CA  1 
ATOM   5884  C  C   . MET B  1 143 ? 34.944  29.070  11.895  1.00 8.27  ? 143  MET B C   1 
ATOM   5885  O  O   . MET B  1 143 ? 35.630  29.804  12.614  1.00 8.25  ? 143  MET B O   1 
ATOM   5886  C  CB  . MET B  1 143 ? 32.869  29.911  10.785  1.00 7.37  ? 143  MET B CB  1 
ATOM   5887  C  CG  . MET B  1 143 ? 32.090  29.091  9.780   1.00 8.71  ? 143  MET B CG  1 
ATOM   5888  S  SD  . MET B  1 143 ? 30.762  28.149  10.548  1.00 8.31  ? 143  MET B SD  1 
ATOM   5889  C  CE  . MET B  1 143 ? 29.559  29.439  10.830  1.00 12.64 ? 143  MET B CE  1 
ATOM   5890  N  N   . PHE B  1 144 ? 35.468  28.207  11.020  1.00 8.61  ? 144  PHE B N   1 
ATOM   5891  C  CA  . PHE B  1 144 ? 36.923  28.065  10.809  1.00 7.70  ? 144  PHE B CA  1 
ATOM   5892  C  C   . PHE B  1 144 ? 37.341  28.708  9.483   1.00 6.61  ? 144  PHE B C   1 
ATOM   5893  O  O   . PHE B  1 144 ? 36.584  28.702  8.514   1.00 8.37  ? 144  PHE B O   1 
ATOM   5894  C  CB  . PHE B  1 144 ? 37.359  26.586  10.704  1.00 7.46  ? 144  PHE B CB  1 
ATOM   5895  C  CG  . PHE B  1 144 ? 37.116  25.751  11.944  1.00 8.34  ? 144  PHE B CG  1 
ATOM   5896  C  CD1 . PHE B  1 144 ? 37.569  26.162  13.195  1.00 8.69  ? 144  PHE B CD1 1 
ATOM   5897  C  CD2 . PHE B  1 144 ? 36.491  24.510  11.840  1.00 7.12  ? 144  PHE B CD2 1 
ATOM   5898  C  CE1 . PHE B  1 144 ? 37.402  25.341  14.318  1.00 7.86  ? 144  PHE B CE1 1 
ATOM   5899  C  CE2 . PHE B  1 144 ? 36.325  23.695  12.949  1.00 5.97  ? 144  PHE B CE2 1 
ATOM   5900  C  CZ  . PHE B  1 144 ? 36.781  24.109  14.190  1.00 6.32  ? 144  PHE B CZ  1 
ATOM   5901  N  N   . PRO B  1 145 ? 38.546  29.284  9.428   1.00 5.80  ? 145  PRO B N   1 
ATOM   5902  C  CA  . PRO B  1 145 ? 39.009  29.892  8.177   1.00 7.28  ? 145  PRO B CA  1 
ATOM   5903  C  C   . PRO B  1 145 ? 39.610  28.757  7.322   1.00 9.47  ? 145  PRO B C   1 
ATOM   5904  O  O   . PRO B  1 145 ? 39.612  27.601  7.750   1.00 9.40  ? 145  PRO B O   1 
ATOM   5905  C  CB  . PRO B  1 145 ? 40.064  30.883  8.653   1.00 6.62  ? 145  PRO B CB  1 
ATOM   5906  C  CG  . PRO B  1 145 ? 40.635  30.197  9.857   1.00 5.28  ? 145  PRO B CG  1 
ATOM   5907  C  CD  . PRO B  1 145 ? 39.385  29.716  10.558  1.00 4.87  ? 145  PRO B CD  1 
ATOM   5908  N  N   . LYS B  1 146 ? 40.111  29.064  6.127   1.00 12.54 ? 146  LYS B N   1 
ATOM   5909  C  CA  . LYS B  1 146 ? 40.716  28.026  5.274   1.00 15.11 ? 146  LYS B CA  1 
ATOM   5910  C  C   . LYS B  1 146 ? 41.939  27.408  5.949   1.00 15.64 ? 146  LYS B C   1 
ATOM   5911  O  O   . LYS B  1 146 ? 42.510  27.978  6.880   1.00 15.71 ? 146  LYS B O   1 
ATOM   5912  C  CB  . LYS B  1 146 ? 41.190  28.600  3.933   1.00 17.18 ? 146  LYS B CB  1 
ATOM   5913  C  CG  . LYS B  1 146 ? 40.118  29.091  2.982   1.00 21.56 ? 146  LYS B CG  1 
ATOM   5914  C  CD  . LYS B  1 146 ? 40.763  29.644  1.700   1.00 24.94 ? 146  LYS B CD  1 
ATOM   5915  C  CE  . LYS B  1 146 ? 41.686  28.616  1.030   1.00 26.54 ? 146  LYS B CE  1 
ATOM   5916  N  NZ  . LYS B  1 146 ? 42.330  29.134  -0.217  1.00 28.48 ? 146  LYS B NZ  1 
ATOM   5917  N  N   . ASN B  1 147 ? 42.350  26.250  5.453   1.00 15.17 ? 147  ASN B N   1 
ATOM   5918  C  CA  . ASN B  1 147 ? 43.526  25.565  5.979   1.00 14.98 ? 147  ASN B CA  1 
ATOM   5919  C  C   . ASN B  1 147 ? 43.757  25.704  7.490   1.00 11.71 ? 147  ASN B C   1 
ATOM   5920  O  O   . ASN B  1 147 ? 44.864  26.028  7.931   1.00 9.83  ? 147  ASN B O   1 
ATOM   5921  C  CB  . ASN B  1 147 ? 44.772  26.033  5.218   1.00 19.53 ? 147  ASN B CB  1 
ATOM   5922  C  CG  . ASN B  1 147 ? 44.679  25.767  3.714   1.00 23.04 ? 147  ASN B CG  1 
ATOM   5923  O  OD1 . ASN B  1 147 ? 43.752  26.235  3.049   1.00 26.04 ? 147  ASN B OD1 1 
ATOM   5924  N  ND2 . ASN B  1 147 ? 45.640  25.015  3.176   1.00 23.68 ? 147  ASN B ND2 1 
ATOM   5925  N  N   . ASP B  1 148 ? 42.699  25.483  8.271   1.00 8.37  ? 148  ASP B N   1 
ATOM   5926  C  CA  . ASP B  1 148 ? 42.789  25.511  9.732   1.00 4.66  ? 148  ASP B CA  1 
ATOM   5927  C  C   . ASP B  1 148 ? 42.883  24.035  10.058  1.00 2.69  ? 148  ASP B C   1 
ATOM   5928  O  O   . ASP B  1 148 ? 41.943  23.277  9.835   1.00 2.00  ? 148  ASP B O   1 
ATOM   5929  C  CB  . ASP B  1 148 ? 41.527  26.096  10.381  1.00 3.43  ? 148  ASP B CB  1 
ATOM   5930  C  CG  . ASP B  1 148 ? 41.611  26.130  11.913  1.00 2.48  ? 148  ASP B CG  1 
ATOM   5931  O  OD1 . ASP B  1 148 ? 41.836  25.068  12.533  1.00 3.42  ? 148  ASP B OD1 1 
ATOM   5932  O  OD2 . ASP B  1 148 ? 41.450  27.220  12.499  1.00 2.00  ? 148  ASP B OD2 1 
ATOM   5933  N  N   . PRO B  1 149 ? 43.997  23.632  10.697  1.00 2.00  ? 149  PRO B N   1 
ATOM   5934  C  CA  . PRO B  1 149 ? 44.185  22.222  11.021  1.00 2.00  ? 149  PRO B CA  1 
ATOM   5935  C  C   . PRO B  1 149 ? 42.949  21.544  11.587  1.00 2.51  ? 149  PRO B C   1 
ATOM   5936  O  O   . PRO B  1 149 ? 42.649  20.400  11.271  1.00 3.50  ? 149  PRO B O   1 
ATOM   5937  C  CB  . PRO B  1 149 ? 45.471  22.229  11.798  1.00 2.30  ? 149  PRO B CB  1 
ATOM   5938  C  CG  . PRO B  1 149 ? 46.243  23.290  11.050  1.00 2.65  ? 149  PRO B CG  1 
ATOM   5939  C  CD  . PRO B  1 149 ? 45.282  24.249  10.428  1.00 2.02  ? 149  PRO B CD  1 
ATOM   5940  N  N   . LYS B  1 150 ? 42.215  22.268  12.450  1.00 2.04  ? 150  LYS B N   1 
ATOM   5941  C  CA  . LYS B  1 150 ? 41.027  21.673  13.060  1.00 2.00  ? 150  LYS B CA  1 
ATOM   5942  C  C   . LYS B  1 150 ? 40.117  21.067  11.950  1.00 2.12  ? 150  LYS B C   1 
ATOM   5943  O  O   . LYS B  1 150 ? 39.421  20.065  12.186  1.00 2.99  ? 150  LYS B O   1 
ATOM   5944  C  CB  . LYS B  1 150 ? 40.305  22.693  13.949  1.00 2.00  ? 150  LYS B CB  1 
ATOM   5945  C  CG  . LYS B  1 150 ? 40.348  22.373  15.445  1.00 2.96  ? 150  LYS B CG  1 
ATOM   5946  C  CD  . LYS B  1 150 ? 40.836  23.538  16.304  1.00 3.23  ? 150  LYS B CD  1 
ATOM   5947  C  CE  . LYS B  1 150 ? 41.036  23.114  17.757  1.00 2.00  ? 150  LYS B CE  1 
ATOM   5948  N  NZ  . LYS B  1 150 ? 41.853  21.869  17.867  1.00 2.00  ? 150  LYS B NZ  1 
ATOM   5949  N  N   . LEU B  1 151 ? 40.115  21.622  10.762  1.00 2.00  ? 151  LEU B N   1 
ATOM   5950  C  CA  . LEU B  1 151 ? 39.216  21.177  9.699   1.00 2.26  ? 151  LEU B CA  1 
ATOM   5951  C  C   . LEU B  1 151 ? 39.220  19.697  9.335   1.00 3.85  ? 151  LEU B C   1 
ATOM   5952  O  O   . LEU B  1 151 ? 38.169  19.089  9.117   1.00 3.40  ? 151  LEU B O   1 
ATOM   5953  C  CB  . LEU B  1 151 ? 39.498  21.990  8.434   1.00 2.00  ? 151  LEU B CB  1 
ATOM   5954  C  CG  . LEU B  1 151 ? 38.719  23.291  8.241   1.00 2.76  ? 151  LEU B CG  1 
ATOM   5955  C  CD1 . LEU B  1 151 ? 39.268  24.085  7.065   1.00 2.94  ? 151  LEU B CD1 1 
ATOM   5956  C  CD2 . LEU B  1 151 ? 37.236  23.002  8.055   1.00 2.25  ? 151  LEU B CD2 1 
ATOM   5957  N  N   . LYS B  1 152 ? 40.419  19.131  9.283   1.00 4.05  ? 152  LYS B N   1 
ATOM   5958  C  CA  . LYS B  1 152 ? 40.591  17.731  8.953   1.00 5.89  ? 152  LYS B CA  1 
ATOM   5959  C  C   . LYS B  1 152 ? 40.282  16.887  10.195  1.00 8.69  ? 152  LYS B C   1 
ATOM   5960  O  O   . LYS B  1 152 ? 40.119  15.664  10.102  1.00 10.63 ? 152  LYS B O   1 
ATOM   5961  C  CB  . LYS B  1 152 ? 42.033  17.491  8.501   1.00 3.57  ? 152  LYS B CB  1 
ATOM   5962  C  CG  . LYS B  1 152 ? 42.492  18.414  7.383   1.00 2.86  ? 152  LYS B CG  1 
ATOM   5963  C  CD  . LYS B  1 152 ? 43.994  18.338  7.212   1.00 2.20  ? 152  LYS B CD  1 
ATOM   5964  C  CE  . LYS B  1 152 ? 44.509  19.317  6.184   1.00 2.00  ? 152  LYS B CE  1 
ATOM   5965  N  NZ  . LYS B  1 152 ? 45.990  19.215  6.136   1.00 2.19  ? 152  LYS B NZ  1 
ATOM   5966  N  N   . THR B  1 153 ? 40.143  17.570  11.352  1.00 6.63  ? 153  THR B N   1 
ATOM   5967  C  CA  . THR B  1 153 ? 39.924  16.779  12.587  1.00 5.31  ? 153  THR B CA  1 
ATOM   5968  C  C   . THR B  1 153 ? 38.574  16.903  13.288  1.00 7.59  ? 153  THR B C   1 
ATOM   5969  O  O   . THR B  1 153 ? 37.886  15.894  13.438  1.00 8.59  ? 153  THR B O   1 
ATOM   5970  C  CB  . THR B  1 153 ? 41.010  17.135  13.608  1.00 3.06  ? 153  THR B CB  1 
ATOM   5971  O  OG1 . THR B  1 153 ? 42.214  16.443  13.258  1.00 3.89  ? 153  THR B OG1 1 
ATOM   5972  C  CG2 . THR B  1 153 ? 40.588  16.738  15.019  1.00 3.30  ? 153  THR B CG2 1 
ATOM   5973  N  N   . GLN B  1 154 ? 38.159  18.093  13.668  1.00 7.33  ? 154  GLN B N   1 
ATOM   5974  C  CA  . GLN B  1 154 ? 36.910  18.159  14.403  1.00 8.06  ? 154  GLN B CA  1 
ATOM   5975  C  C   . GLN B  1 154 ? 35.634  18.521  13.679  1.00 9.88  ? 154  GLN B C   1 
ATOM   5976  O  O   . GLN B  1 154 ? 34.553  18.170  14.169  1.00 10.41 ? 154  GLN B O   1 
ATOM   5977  C  CB  . GLN B  1 154 ? 37.012  19.222  15.505  1.00 5.78  ? 154  GLN B CB  1 
ATOM   5978  C  CG  . GLN B  1 154 ? 38.132  19.087  16.507  1.00 4.45  ? 154  GLN B CG  1 
ATOM   5979  C  CD  . GLN B  1 154 ? 38.311  20.372  17.316  1.00 4.61  ? 154  GLN B CD  1 
ATOM   5980  O  OE1 . GLN B  1 154 ? 39.433  20.819  17.525  1.00 4.04  ? 154  GLN B OE1 1 
ATOM   5981  N  NE2 . GLN B  1 154 ? 37.356  21.118  17.850  1.00 6.02  ? 154  GLN B NE2 1 
ATOM   5982  N  N   . GLY B  1 155 ? 35.664  19.206  12.567  1.00 9.85  ? 155  GLY B N   1 
ATOM   5983  C  CA  . GLY B  1 155 ? 34.383  19.506  11.964  1.00 10.10 ? 155  GLY B CA  1 
ATOM   5984  C  C   . GLY B  1 155 ? 34.474  20.766  11.159  1.00 9.58  ? 155  GLY B C   1 
ATOM   5985  O  O   . GLY B  1 155 ? 35.532  21.112  10.635  1.00 9.05  ? 155  GLY B O   1 
ATOM   5986  N  N   . LYS B  1 156 ? 33.361  21.487  11.064  1.00 8.31  ? 156  LYS B N   1 
ATOM   5987  C  CA  . LYS B  1 156 ? 33.327  22.723  10.296  1.00 7.65  ? 156  LYS B CA  1 
ATOM   5988  C  C   . LYS B  1 156 ? 33.283  23.912  11.248  1.00 5.92  ? 156  LYS B C   1 
ATOM   5989  O  O   . LYS B  1 156 ? 33.451  25.058  10.834  1.00 5.93  ? 156  LYS B O   1 
ATOM   5990  C  CB  . LYS B  1 156 ? 32.104  22.737  9.365   1.00 7.41  ? 156  LYS B CB  1 
ATOM   5991  C  CG  . LYS B  1 156 ? 32.452  22.954  7.896   1.00 7.75  ? 156  LYS B CG  1 
ATOM   5992  C  CD  . LYS B  1 156 ? 31.295  22.592  6.969   1.00 8.89  ? 156  LYS B CD  1 
ATOM   5993  C  CE  . LYS B  1 156 ? 31.761  22.577  5.517   1.00 9.95  ? 156  LYS B CE  1 
ATOM   5994  N  NZ  . LYS B  1 156 ? 32.927  21.653  5.312   1.00 9.15  ? 156  LYS B NZ  1 
ATOM   5995  N  N   . CYS B  1 157 ? 33.082  23.642  12.531  1.00 3.99  ? 157  CYS B N   1 
ATOM   5996  C  CA  . CYS B  1 157 ? 33.001  24.731  13.483  1.00 4.38  ? 157  CYS B CA  1 
ATOM   5997  C  C   . CYS B  1 157 ? 33.024  24.249  14.924  1.00 5.69  ? 157  CYS B C   1 
ATOM   5998  O  O   . CYS B  1 157 ? 33.079  23.046  15.198  1.00 7.03  ? 157  CYS B O   1 
ATOM   5999  C  CB  . CYS B  1 157 ? 31.709  25.495  13.262  1.00 4.56  ? 157  CYS B CB  1 
ATOM   6000  S  SG  . CYS B  1 157 ? 30.298  24.730  14.119  1.00 5.16  ? 157  CYS B SG  1 
ATOM   6001  N  N   . MET B  1 158 ? 32.964  25.205  15.847  1.00 5.77  ? 158  MET B N   1 
ATOM   6002  C  CA  . MET B  1 158 ? 32.960  24.884  17.263  1.00 3.96  ? 158  MET B CA  1 
ATOM   6003  C  C   . MET B  1 158 ? 31.657  25.339  17.866  1.00 2.00  ? 158  MET B C   1 
ATOM   6004  O  O   . MET B  1 158 ? 31.349  26.524  17.868  1.00 2.02  ? 158  MET B O   1 
ATOM   6005  C  CB  . MET B  1 158 ? 34.081  25.604  18.007  1.00 4.70  ? 158  MET B CB  1 
ATOM   6006  C  CG  . MET B  1 158 ? 35.465  25.423  17.443  1.00 5.10  ? 158  MET B CG  1 
ATOM   6007  S  SD  . MET B  1 158 ? 36.558  26.466  18.414  1.00 10.65 ? 158  MET B SD  1 
ATOM   6008  C  CE  . MET B  1 158 ? 37.754  25.305  18.978  1.00 7.71  ? 158  MET B CE  1 
ATOM   6009  N  N   . PRO B  1 159 ? 30.855  24.401  18.360  1.00 2.00  ? 159  PRO B N   1 
ATOM   6010  C  CA  . PRO B  1 159 ? 29.595  24.824  18.964  1.00 2.00  ? 159  PRO B CA  1 
ATOM   6011  C  C   . PRO B  1 159 ? 29.842  25.989  19.933  1.00 2.30  ? 159  PRO B C   1 
ATOM   6012  O  O   . PRO B  1 159 ? 30.858  26.033  20.625  1.00 2.24  ? 159  PRO B O   1 
ATOM   6013  C  CB  . PRO B  1 159 ? 29.097  23.551  19.666  1.00 2.08  ? 159  PRO B CB  1 
ATOM   6014  C  CG  . PRO B  1 159 ? 30.311  22.596  19.656  1.00 2.30  ? 159  PRO B CG  1 
ATOM   6015  C  CD  . PRO B  1 159 ? 30.979  22.937  18.360  1.00 2.01  ? 159  PRO B CD  1 
ATOM   6016  N  N   . PHE B  1 160 ? 28.912  26.939  19.957  1.00 3.40  ? 160  PHE B N   1 
ATOM   6017  C  CA  . PHE B  1 160 ? 29.007  28.122  20.813  1.00 2.52  ? 160  PHE B CA  1 
ATOM   6018  C  C   . PHE B  1 160 ? 27.616  28.739  20.989  1.00 3.65  ? 160  PHE B C   1 
ATOM   6019  O  O   . PHE B  1 160 ? 26.887  28.924  20.015  1.00 5.18  ? 160  PHE B O   1 
ATOM   6020  C  CB  . PHE B  1 160 ? 29.952  29.134  20.168  1.00 2.00  ? 160  PHE B CB  1 
ATOM   6021  C  CG  . PHE B  1 160 ? 30.062  30.426  20.911  1.00 2.00  ? 160  PHE B CG  1 
ATOM   6022  C  CD1 . PHE B  1 160 ? 29.007  31.321  20.941  1.00 2.55  ? 160  PHE B CD1 1 
ATOM   6023  C  CD2 . PHE B  1 160 ? 31.234  30.758  21.569  1.00 2.85  ? 160  PHE B CD2 1 
ATOM   6024  C  CE1 . PHE B  1 160 ? 29.122  32.530  21.614  1.00 3.85  ? 160  PHE B CE1 1 
ATOM   6025  C  CE2 . PHE B  1 160 ? 31.360  31.964  22.245  1.00 3.17  ? 160  PHE B CE2 1 
ATOM   6026  C  CZ  . PHE B  1 160 ? 30.302  32.852  22.268  1.00 3.36  ? 160  PHE B CZ  1 
ATOM   6027  N  N   . PHE B  1 161 ? 27.248  29.068  22.222  1.00 2.83  ? 161  PHE B N   1 
ATOM   6028  C  CA  . PHE B  1 161 ? 25.935  29.650  22.478  1.00 2.70  ? 161  PHE B CA  1 
ATOM   6029  C  C   . PHE B  1 161 ? 25.971  31.049  23.076  1.00 2.51  ? 161  PHE B C   1 
ATOM   6030  O  O   . PHE B  1 161 ? 26.970  31.450  23.667  1.00 3.27  ? 161  PHE B O   1 
ATOM   6031  C  CB  . PHE B  1 161 ? 25.141  28.754  23.410  1.00 4.43  ? 161  PHE B CB  1 
ATOM   6032  C  CG  . PHE B  1 161 ? 24.694  27.479  22.787  1.00 5.33  ? 161  PHE B CG  1 
ATOM   6033  C  CD1 . PHE B  1 161 ? 25.550  26.389  22.706  1.00 6.88  ? 161  PHE B CD1 1 
ATOM   6034  C  CD2 . PHE B  1 161 ? 23.398  27.356  22.307  1.00 6.52  ? 161  PHE B CD2 1 
ATOM   6035  C  CE1 . PHE B  1 161 ? 25.117  25.185  22.159  1.00 7.46  ? 161  PHE B CE1 1 
ATOM   6036  C  CE2 . PHE B  1 161 ? 22.953  26.164  21.757  1.00 7.36  ? 161  PHE B CE2 1 
ATOM   6037  C  CZ  . PHE B  1 161 ? 23.811  25.073  21.684  1.00 7.57  ? 161  PHE B CZ  1 
ATOM   6038  N  N   . ARG B  1 162 ? 24.865  31.781  22.949  1.00 2.00  ? 162  ARG B N   1 
ATOM   6039  C  CA  . ARG B  1 162 ? 24.798  33.140  23.478  1.00 2.50  ? 162  ARG B CA  1 
ATOM   6040  C  C   . ARG B  1 162 ? 24.528  33.196  24.965  1.00 2.00  ? 162  ARG B C   1 
ATOM   6041  O  O   . ARG B  1 162 ? 23.781  32.385  25.504  1.00 2.21  ? 162  ARG B O   1 
ATOM   6042  C  CB  . ARG B  1 162 ? 23.728  33.946  22.753  1.00 2.87  ? 162  ARG B CB  1 
ATOM   6043  C  CG  . ARG B  1 162 ? 23.995  34.121  21.277  1.00 4.77  ? 162  ARG B CG  1 
ATOM   6044  C  CD  . ARG B  1 162 ? 23.068  35.161  20.666  1.00 6.48  ? 162  ARG B CD  1 
ATOM   6045  N  NE  . ARG B  1 162 ? 23.488  36.530  20.952  1.00 7.56  ? 162  ARG B NE  1 
ATOM   6046  C  CZ  . ARG B  1 162 ? 22.874  37.602  20.468  1.00 8.03  ? 162  ARG B CZ  1 
ATOM   6047  N  NH1 . ARG B  1 162 ? 21.816  37.450  19.686  1.00 9.57  ? 162  ARG B NH1 1 
ATOM   6048  N  NH2 . ARG B  1 162 ? 23.325  38.819  20.745  1.00 8.84  ? 162  ARG B NH2 1 
ATOM   6049  N  N   . ALA B  1 163 ? 25.131  34.178  25.621  1.00 2.00  ? 163  ALA B N   1 
ATOM   6050  C  CA  . ALA B  1 163 ? 24.968  34.356  27.062  1.00 3.10  ? 163  ALA B CA  1 
ATOM   6051  C  C   . ALA B  1 163 ? 23.580  34.864  27.436  1.00 2.00  ? 163  ALA B C   1 
ATOM   6052  O  O   . ALA B  1 163 ? 23.087  35.820  26.851  1.00 2.63  ? 163  ALA B O   1 
ATOM   6053  C  CB  . ALA B  1 163 ? 26.024  35.325  27.581  1.00 4.02  ? 163  ALA B CB  1 
ATOM   6054  N  N   . GLY B  1 164 ? 22.962  34.239  28.428  1.00 2.00  ? 164  GLY B N   1 
ATOM   6055  C  CA  . GLY B  1 164 ? 21.636  34.665  28.848  1.00 4.06  ? 164  GLY B CA  1 
ATOM   6056  C  C   . GLY B  1 164 ? 21.491  36.160  29.066  1.00 5.78  ? 164  GLY B C   1 
ATOM   6057  O  O   . GLY B  1 164 ? 22.440  36.822  29.497  1.00 6.81  ? 164  GLY B O   1 
ATOM   6058  N  N   . PHE B  1 165 ? 20.304  36.690  28.771  1.00 5.50  ? 165  PHE B N   1 
ATOM   6059  C  CA  . PHE B  1 165 ? 20.029  38.112  28.928  1.00 5.47  ? 165  PHE B CA  1 
ATOM   6060  C  C   . PHE B  1 165 ? 18.966  38.322  29.972  1.00 7.31  ? 165  PHE B C   1 
ATOM   6061  O  O   . PHE B  1 165 ? 18.356  37.366  30.442  1.00 6.89  ? 165  PHE B O   1 
ATOM   6062  C  CB  . PHE B  1 165 ? 19.573  38.744  27.604  1.00 6.32  ? 165  PHE B CB  1 
ATOM   6063  C  CG  . PHE B  1 165 ? 18.849  37.798  26.672  1.00 6.57  ? 165  PHE B CG  1 
ATOM   6064  C  CD1 . PHE B  1 165 ? 19.536  36.776  26.021  1.00 7.24  ? 165  PHE B CD1 1 
ATOM   6065  C  CD2 . PHE B  1 165 ? 17.486  37.950  26.418  1.00 6.00  ? 165  PHE B CD2 1 
ATOM   6066  C  CE1 . PHE B  1 165 ? 18.880  35.923  25.130  1.00 7.36  ? 165  PHE B CE1 1 
ATOM   6067  C  CE2 . PHE B  1 165 ? 16.824  37.102  25.529  1.00 5.80  ? 165  PHE B CE2 1 
ATOM   6068  C  CZ  . PHE B  1 165 ? 17.522  36.089  24.885  1.00 6.17  ? 165  PHE B CZ  1 
ATOM   6069  N  N   . VAL B  1 166 ? 18.731  39.571  30.349  1.00 10.80 ? 166  VAL B N   1 
ATOM   6070  C  CA  . VAL B  1 166 ? 17.715  39.800  31.352  1.00 16.03 ? 166  VAL B CA  1 
ATOM   6071  C  C   . VAL B  1 166 ? 16.387  39.343  30.826  1.00 22.66 ? 166  VAL B C   1 
ATOM   6072  O  O   . VAL B  1 166 ? 16.230  39.104  29.625  1.00 23.21 ? 166  VAL B O   1 
ATOM   6073  C  CB  . VAL B  1 166 ? 17.561  41.277  31.768  1.00 14.29 ? 166  VAL B CB  1 
ATOM   6074  C  CG1 . VAL B  1 166 ? 18.837  41.769  32.356  1.00 13.64 ? 166  VAL B CG1 1 
ATOM   6075  C  CG2 . VAL B  1 166 ? 17.121  42.128  30.592  1.00 14.74 ? 166  VAL B CG2 1 
ATOM   6076  N  N   . CYS B  1 167 ? 15.436  39.224  31.747  1.00 31.24 ? 167  CYS B N   1 
ATOM   6077  C  CA  . CYS B  1 167 ? 14.084  38.787  31.424  1.00 37.09 ? 167  CYS B CA  1 
ATOM   6078  C  C   . CYS B  1 167 ? 14.269  37.281  31.083  1.00 40.39 ? 167  CYS B C   1 
ATOM   6079  O  O   . CYS B  1 167 ? 15.137  36.604  31.688  1.00 38.94 ? 167  CYS B O   1 
ATOM   6080  C  CB  . CYS B  1 167 ? 13.554  39.689  30.255  1.00 41.88 ? 167  CYS B CB  1 
ATOM   6081  S  SG  . CYS B  1 167 ? 13.926  41.506  30.452  1.00 52.85 ? 167  CYS B SG  1 
ATOM   6082  N  N   . PRO B  1 168 ? 13.475  36.714  30.151  1.00 40.66 ? 168  PRO B N   1 
ATOM   6083  C  CA  . PRO B  1 168 ? 13.792  35.289  29.952  1.00 42.88 ? 168  PRO B CA  1 
ATOM   6084  C  C   . PRO B  1 168 ? 15.182  34.852  29.426  1.00 45.51 ? 168  PRO B C   1 
ATOM   6085  O  O   . PRO B  1 168 ? 16.168  34.856  30.152  1.00 45.55 ? 168  PRO B O   1 
ATOM   6086  C  CB  . PRO B  1 168 ? 12.674  34.820  29.008  1.00 42.46 ? 168  PRO B CB  1 
ATOM   6087  C  CG  . PRO B  1 168 ? 11.516  35.657  29.403  1.00 42.23 ? 168  PRO B CG  1 
ATOM   6088  C  CD  . PRO B  1 168 ? 12.210  37.033  29.463  1.00 40.39 ? 168  PRO B CD  1 
ATOM   6089  N  N   . THR B  1 169 ? 15.200  34.426  28.162  1.00 49.28 ? 169  THR B N   1 
ATOM   6090  C  CA  . THR B  1 169 ? 16.367  33.964  27.384  1.00 52.94 ? 169  THR B CA  1 
ATOM   6091  C  C   . THR B  1 169 ? 15.764  33.428  26.082  1.00 56.20 ? 169  THR B C   1 
ATOM   6092  O  O   . THR B  1 169 ? 16.353  33.588  25.003  1.00 56.20 ? 169  THR B O   1 
ATOM   6093  C  CB  . THR B  1 169 ? 17.195  32.866  28.095  1.00 52.70 ? 169  THR B CB  1 
ATOM   6094  O  OG1 . THR B  1 169 ? 16.412  32.236  29.110  1.00 53.64 ? 169  THR B OG1 1 
ATOM   6095  C  CG2 . THR B  1 169 ? 18.452  33.471  28.705  1.00 52.42 ? 169  THR B CG2 1 
ATOM   6096  N  N   . PRO B  1 170 ? 14.569  32.792  26.168  1.00 59.51 ? 170  PRO B N   1 
ATOM   6097  C  CA  . PRO B  1 170 ? 13.839  32.238  25.016  1.00 61.57 ? 170  PRO B CA  1 
ATOM   6098  C  C   . PRO B  1 170 ? 13.456  33.398  24.062  1.00 63.13 ? 170  PRO B C   1 
ATOM   6099  O  O   . PRO B  1 170 ? 13.978  34.504  24.215  1.00 63.50 ? 170  PRO B O   1 
ATOM   6100  C  CB  . PRO B  1 170 ? 12.637  31.553  25.687  1.00 61.27 ? 170  PRO B CB  1 
ATOM   6101  C  CG  . PRO B  1 170 ? 13.282  30.972  26.912  1.00 61.13 ? 170  PRO B CG  1 
ATOM   6102  C  CD  . PRO B  1 170 ? 14.035  32.205  27.411  1.00 59.74 ? 170  PRO B CD  1 
ATOM   6103  N  N   . PRO B  1 171 ? 12.384  33.217  23.179  1.00 64.34 ? 171  PRO B N   1 
ATOM   6104  C  CA  . PRO B  1 171 ? 11.998  34.185  22.047  1.00 65.49 ? 171  PRO B CA  1 
ATOM   6105  C  C   . PRO B  1 171 ? 12.073  35.757  22.150  1.00 66.33 ? 171  PRO B C   1 
ATOM   6106  O  O   . PRO B  1 171 ? 11.183  36.467  21.681  1.00 67.23 ? 171  PRO B O   1 
ATOM   6107  C  CB  . PRO B  1 171 ? 10.703  33.602  21.562  1.00 65.22 ? 171  PRO B CB  1 
ATOM   6108  C  CG  . PRO B  1 171 ? 10.960  32.112  21.687  1.00 65.20 ? 171  PRO B CG  1 
ATOM   6109  C  CD  . PRO B  1 171 ? 11.912  31.882  22.824  1.00 64.46 ? 171  PRO B CD  1 
ATOM   6110  N  N   . TYR B  1 172 ? 13.199  36.245  22.749  1.00 66.32 ? 172  TYR B N   1 
ATOM   6111  C  CA  . TYR B  1 172 ? 13.861  37.606  23.040  1.00 66.16 ? 172  TYR B CA  1 
ATOM   6112  C  C   . TYR B  1 172 ? 13.459  38.925  22.292  1.00 65.25 ? 172  TYR B C   1 
ATOM   6113  O  O   . TYR B  1 172 ? 13.173  38.818  21.103  1.00 65.51 ? 172  TYR B O   1 
ATOM   6114  C  CB  . TYR B  1 172 ? 15.301  37.411  22.624  1.00 68.86 ? 172  TYR B CB  1 
ATOM   6115  C  CG  . TYR B  1 172 ? 15.481  36.649  21.322  1.00 71.15 ? 172  TYR B CG  1 
ATOM   6116  C  CD1 . TYR B  1 172 ? 15.072  35.296  21.211  1.00 71.95 ? 172  TYR B CD1 1 
ATOM   6117  C  CD2 . TYR B  1 172 ? 16.038  37.241  20.198  1.00 71.82 ? 172  TYR B CD2 1 
ATOM   6118  C  CE1 . TYR B  1 172 ? 15.270  34.574  20.028  1.00 72.94 ? 172  TYR B CE1 1 
ATOM   6119  C  CE2 . TYR B  1 172 ? 16.251  36.511  19.034  1.00 72.95 ? 172  TYR B CE2 1 
ATOM   6120  C  CZ  . TYR B  1 172 ? 15.872  35.195  18.958  1.00 73.10 ? 172  TYR B CZ  1 
ATOM   6121  O  OH  . TYR B  1 172 ? 16.096  34.504  17.798  1.00 73.49 ? 172  TYR B OH  1 
ATOM   6122  N  N   . GLN B  1 173 ? 13.398  40.158  22.880  1.00 62.60 ? 173  GLN B N   1 
ATOM   6123  C  CA  . GLN B  1 173 ? 12.895  41.323  22.049  1.00 59.52 ? 173  GLN B CA  1 
ATOM   6124  C  C   . GLN B  1 173 ? 13.328  42.752  22.440  1.00 57.35 ? 173  GLN B C   1 
ATOM   6125  O  O   . GLN B  1 173 ? 14.485  43.032  22.689  1.00 56.17 ? 173  GLN B O   1 
ATOM   6126  C  CB  . GLN B  1 173 ? 11.362  41.261  22.042  1.00 59.33 ? 173  GLN B CB  1 
ATOM   6127  C  CG  . GLN B  1 173 ? 10.708  41.745  23.325  1.00 59.45 ? 173  GLN B CG  1 
ATOM   6128  C  CD  . GLN B  1 173 ? 9.279   41.245  23.416  1.00 60.01 ? 173  GLN B CD  1 
ATOM   6129  O  OE1 . GLN B  1 173 ? 8.352   41.917  22.970  1.00 59.89 ? 173  GLN B OE1 1 
ATOM   6130  N  NE2 . GLN B  1 173 ? 8.870   40.092  23.946  1.00 60.27 ? 173  GLN B NE2 1 
ATOM   6131  N  N   . SER B  1 174 ? 12.312  43.626  22.466  1.00 54.88 ? 174  SER B N   1 
ATOM   6132  C  CA  . SER B  1 174 ? 12.269  45.062  22.866  1.00 52.53 ? 174  SER B CA  1 
ATOM   6133  C  C   . SER B  1 174 ? 13.410  46.113  22.948  1.00 50.20 ? 174  SER B C   1 
ATOM   6134  O  O   . SER B  1 174 ? 13.569  46.907  22.010  1.00 50.86 ? 174  SER B O   1 
ATOM   6135  C  CB  . SER B  1 174 ? 11.446  45.171  24.157  1.00 53.01 ? 174  SER B CB  1 
ATOM   6136  O  OG  . SER B  1 174 ? 10.144  44.642  23.953  1.00 53.34 ? 174  SER B OG  1 
ATOM   6137  N  N   . LEU B  1 175 ? 14.146  46.173  24.066  1.00 45.22 ? 175  LEU B N   1 
ATOM   6138  C  CA  . LEU B  1 175 ? 15.229  47.161  24.240  1.00 39.16 ? 175  LEU B CA  1 
ATOM   6139  C  C   . LEU B  1 175 ? 16.625  46.565  24.014  1.00 35.53 ? 175  LEU B C   1 
ATOM   6140  O  O   . LEU B  1 175 ? 16.752  45.362  23.785  1.00 36.11 ? 175  LEU B O   1 
ATOM   6141  C  CB  . LEU B  1 175 ? 15.164  47.779  25.640  1.00 38.39 ? 175  LEU B CB  1 
ATOM   6142  C  CG  . LEU B  1 175 ? 15.778  49.179  25.756  1.00 38.05 ? 175  LEU B CG  1 
ATOM   6143  C  CD1 . LEU B  1 175 ? 14.651  50.169  26.018  1.00 37.95 ? 175  LEU B CD1 1 
ATOM   6144  C  CD2 . LEU B  1 175 ? 16.824  49.242  26.872  1.00 37.02 ? 175  LEU B CD2 1 
ATOM   6145  N  N   . ALA B  1 176 ? 17.662  47.408  24.076  1.00 29.94 ? 176  ALA B N   1 
ATOM   6146  C  CA  . ALA B  1 176 ? 19.057  46.977  23.875  1.00 23.85 ? 176  ALA B CA  1 
ATOM   6147  C  C   . ALA B  1 176 ? 19.465  45.915  24.900  1.00 19.49 ? 176  ALA B C   1 
ATOM   6148  O  O   . ALA B  1 176 ? 19.411  46.152  26.107  1.00 18.29 ? 176  ALA B O   1 
ATOM   6149  C  CB  . ALA B  1 176 ? 19.990  48.181  23.964  1.00 24.51 ? 176  ALA B CB  1 
ATOM   6150  N  N   . ARG B  1 177 ? 19.909  44.762  24.405  1.00 14.98 ? 177  ARG B N   1 
ATOM   6151  C  CA  . ARG B  1 177 ? 20.268  43.626  25.257  1.00 11.86 ? 177  ARG B CA  1 
ATOM   6152  C  C   . ARG B  1 177 ? 21.309  43.791  26.356  1.00 9.43  ? 177  ARG B C   1 
ATOM   6153  O  O   . ARG B  1 177 ? 22.391  44.336  26.152  1.00 7.15  ? 177  ARG B O   1 
ATOM   6154  C  CB  . ARG B  1 177 ? 20.673  42.432  24.392  1.00 12.14 ? 177  ARG B CB  1 
ATOM   6155  C  CG  . ARG B  1 177 ? 20.655  41.110  25.145  1.00 10.59 ? 177  ARG B CG  1 
ATOM   6156  C  CD  . ARG B  1 177 ? 19.674  40.152  24.508  1.00 10.18 ? 177  ARG B CD  1 
ATOM   6157  N  NE  . ARG B  1 177 ? 20.333  39.147  23.684  1.00 11.11 ? 177  ARG B NE  1 
ATOM   6158  C  CZ  . ARG B  1 177 ? 19.681  38.285  22.908  1.00 12.98 ? 177  ARG B CZ  1 
ATOM   6159  N  NH1 . ARG B  1 177 ? 18.353  38.323  22.855  1.00 13.45 ? 177  ARG B NH1 1 
ATOM   6160  N  NH2 . ARG B  1 177 ? 20.347  37.378  22.200  1.00 12.18 ? 177  ARG B NH2 1 
ATOM   6161  N  N   . ASP B  1 178 ? 20.966  43.276  27.530  1.00 7.14  ? 178  ASP B N   1 
ATOM   6162  C  CA  . ASP B  1 178 ? 21.852  43.336  28.675  1.00 6.90  ? 178  ASP B CA  1 
ATOM   6163  C  C   . ASP B  1 178 ? 21.883  41.948  29.287  1.00 6.23  ? 178  ASP B C   1 
ATOM   6164  O  O   . ASP B  1 178 ? 20.843  41.410  29.650  1.00 6.00  ? 178  ASP B O   1 
ATOM   6165  C  CB  . ASP B  1 178 ? 21.350  44.380  29.687  1.00 7.96  ? 178  ASP B CB  1 
ATOM   6166  C  CG  . ASP B  1 178 ? 21.518  45.817  29.180  1.00 9.78  ? 178  ASP B CG  1 
ATOM   6167  O  OD1 . ASP B  1 178 ? 22.664  46.188  28.822  1.00 8.49  ? 178  ASP B OD1 1 
ATOM   6168  O  OD2 . ASP B  1 178 ? 20.512  46.571  29.142  1.00 8.94  ? 178  ASP B OD2 1 
ATOM   6169  N  N   . GLN B  1 179 ? 23.074  41.361  29.373  1.00 5.31  ? 179  GLN B N   1 
ATOM   6170  C  CA  . GLN B  1 179 ? 23.227  40.025  29.931  1.00 4.02  ? 179  GLN B CA  1 
ATOM   6171  C  C   . GLN B  1 179 ? 23.390  40.048  31.429  1.00 4.56  ? 179  GLN B C   1 
ATOM   6172  O  O   . GLN B  1 179 ? 23.883  41.020  31.997  1.00 3.71  ? 179  GLN B O   1 
ATOM   6173  C  CB  . GLN B  1 179 ? 24.416  39.307  29.311  1.00 4.60  ? 179  GLN B CB  1 
ATOM   6174  C  CG  . GLN B  1 179 ? 25.404  40.226  28.652  1.00 6.13  ? 179  GLN B CG  1 
ATOM   6175  C  CD  . GLN B  1 179 ? 25.045  40.528  27.214  1.00 5.37  ? 179  GLN B CD  1 
ATOM   6176  O  OE1 . GLN B  1 179 ? 24.619  39.642  26.472  1.00 5.76  ? 179  GLN B OE1 1 
ATOM   6177  N  NE2 . GLN B  1 179 ? 25.233  41.776  26.806  1.00 5.46  ? 179  GLN B NE2 1 
ATOM   6178  N  N   . ILE B  1 180 ? 22.992  38.937  32.043  1.00 4.28  ? 180  ILE B N   1 
ATOM   6179  C  CA  . ILE B  1 180 ? 23.003  38.741  33.488  1.00 3.20  ? 180  ILE B CA  1 
ATOM   6180  C  C   . ILE B  1 180 ? 24.314  38.360  34.171  1.00 3.96  ? 180  ILE B C   1 
ATOM   6181  O  O   . ILE B  1 180 ? 25.171  37.716  33.578  1.00 4.74  ? 180  ILE B O   1 
ATOM   6182  C  CB  . ILE B  1 180 ? 21.969  37.665  33.867  1.00 3.76  ? 180  ILE B CB  1 
ATOM   6183  C  CG1 . ILE B  1 180 ? 20.558  38.173  33.587  1.00 4.69  ? 180  ILE B CG1 1 
ATOM   6184  C  CG2 . ILE B  1 180 ? 22.103  37.293  35.335  1.00 5.86  ? 180  ILE B CG2 1 
ATOM   6185  C  CD1 . ILE B  1 180 ? 19.467  37.195  34.027  1.00 5.45  ? 180  ILE B CD1 1 
ATOM   6186  N  N   . ASN B  1 181 ? 24.431  38.769  35.436  1.00 3.52  ? 181  ASN B N   1 
ATOM   6187  C  CA  . ASN B  1 181 ? 25.565  38.466  36.327  1.00 3.42  ? 181  ASN B CA  1 
ATOM   6188  C  C   . ASN B  1 181 ? 24.908  37.618  37.448  1.00 2.00  ? 181  ASN B C   1 
ATOM   6189  O  O   . ASN B  1 181 ? 24.235  38.155  38.326  1.00 2.00  ? 181  ASN B O   1 
ATOM   6190  C  CB  . ASN B  1 181 ? 26.147  39.781  36.882  1.00 2.89  ? 181  ASN B CB  1 
ATOM   6191  C  CG  . ASN B  1 181 ? 27.238  39.570  37.927  1.00 2.16  ? 181  ASN B CG  1 
ATOM   6192  O  OD1 . ASN B  1 181 ? 27.576  38.446  38.284  1.00 2.66  ? 181  ASN B OD1 1 
ATOM   6193  N  ND2 . ASN B  1 181 ? 27.786  40.670  38.425  1.00 2.50  ? 181  ASN B ND2 1 
ATOM   6194  N  N   . SER B  1 182 ? 25.092  36.298  37.404  1.00 2.00  ? 182  SER B N   1 
ATOM   6195  C  CA  . SER B  1 182 ? 24.426  35.405  38.374  1.00 3.55  ? 182  SER B CA  1 
ATOM   6196  C  C   . SER B  1 182 ? 25.102  35.343  39.751  1.00 2.74  ? 182  SER B C   1 
ATOM   6197  O  O   . SER B  1 182 ? 24.690  34.584  40.619  1.00 2.00  ? 182  SER B O   1 
ATOM   6198  C  CB  . SER B  1 182 ? 24.340  33.988  37.790  1.00 5.07  ? 182  SER B CB  1 
ATOM   6199  O  OG  . SER B  1 182 ? 25.598  33.343  37.825  1.00 7.37  ? 182  SER B OG  1 
ATOM   6200  N  N   . VAL B  1 183 ? 26.145  36.172  39.947  1.00 2.00  ? 183  VAL B N   1 
ATOM   6201  C  CA  . VAL B  1 183 ? 26.895  36.269  41.196  1.00 2.73  ? 183  VAL B CA  1 
ATOM   6202  C  C   . VAL B  1 183 ? 26.906  37.724  41.705  1.00 4.17  ? 183  VAL B C   1 
ATOM   6203  O  O   . VAL B  1 183 ? 26.392  38.625  41.044  1.00 4.79  ? 183  VAL B O   1 
ATOM   6204  C  CB  . VAL B  1 183 ? 28.332  35.805  41.077  1.00 2.00  ? 183  VAL B CB  1 
ATOM   6205  C  CG1 . VAL B  1 183 ? 28.404  34.310  40.844  1.00 2.40  ? 183  VAL B CG1 1 
ATOM   6206  C  CG2 . VAL B  1 183 ? 29.032  36.548  39.959  1.00 2.14  ? 183  VAL B CG2 1 
ATOM   6207  N  N   . THR B  1 184 ? 27.526  37.955  42.865  1.00 3.00  ? 184  THR B N   1 
ATOM   6208  C  CA  . THR B  1 184 ? 27.498  39.269  43.494  1.00 2.85  ? 184  THR B CA  1 
ATOM   6209  C  C   . THR B  1 184 ? 28.746  40.079  43.327  1.00 2.78  ? 184  THR B C   1 
ATOM   6210  O  O   . THR B  1 184 ? 29.869  39.598  43.457  1.00 2.08  ? 184  THR B O   1 
ATOM   6211  C  CB  . THR B  1 184 ? 27.147  39.148  44.956  1.00 3.09  ? 184  THR B CB  1 
ATOM   6212  O  OG1 . THR B  1 184 ? 28.299  38.774  45.717  1.00 2.00  ? 184  THR B OG1 1 
ATOM   6213  C  CG2 . THR B  1 184 ? 26.062  38.096  45.149  1.00 3.18  ? 184  THR B CG2 1 
ATOM   6214  N  N   . SER B  1 185 ? 28.459  41.343  43.026  1.00 3.47  ? 185  SER B N   1 
ATOM   6215  C  CA  . SER B  1 185 ? 29.543  42.240  42.746  1.00 4.56  ? 185  SER B CA  1 
ATOM   6216  C  C   . SER B  1 185 ? 30.458  42.528  43.924  1.00 3.49  ? 185  SER B C   1 
ATOM   6217  O  O   . SER B  1 185 ? 31.418  43.293  43.785  1.00 4.64  ? 185  SER B O   1 
ATOM   6218  C  CB  . SER B  1 185 ? 28.960  43.558  42.218  1.00 6.10  ? 185  SER B CB  1 
ATOM   6219  O  OG  . SER B  1 185 ? 27.680  43.348  41.634  1.00 10.68 ? 185  SER B OG  1 
ATOM   6220  N  N   . PHE B  1 186 ? 30.227  41.956  45.074  1.00 3.52  ? 186  PHE B N   1 
ATOM   6221  C  CA  . PHE B  1 186 ? 31.083  42.290  46.209  1.00 2.16  ? 186  PHE B CA  1 
ATOM   6222  C  C   . PHE B  1 186 ? 32.153  41.239  46.526  1.00 2.18  ? 186  PHE B C   1 
ATOM   6223  O  O   . PHE B  1 186 ? 31.901  40.022  46.428  1.00 3.03  ? 186  PHE B O   1 
ATOM   6224  C  CB  . PHE B  1 186 ? 30.200  42.452  47.474  1.00 2.00  ? 186  PHE B CB  1 
ATOM   6225  C  CG  . PHE B  1 186 ? 29.059  43.408  47.323  1.00 2.00  ? 186  PHE B CG  1 
ATOM   6226  C  CD1 . PHE B  1 186 ? 29.303  44.763  47.505  1.00 2.00  ? 186  PHE B CD1 1 
ATOM   6227  C  CD2 . PHE B  1 186 ? 27.763  43.007  47.022  1.00 2.00  ? 186  PHE B CD2 1 
ATOM   6228  C  CE1 . PHE B  1 186 ? 28.269  45.697  47.386  1.00 2.00  ? 186  PHE B CE1 1 
ATOM   6229  C  CE2 . PHE B  1 186 ? 26.730  43.937  46.903  1.00 2.00  ? 186  PHE B CE2 1 
ATOM   6230  C  CZ  . PHE B  1 186 ? 26.985  45.278  47.085  1.00 2.00  ? 186  PHE B CZ  1 
ATOM   6231  N  N   . LEU B  1 187 ? 33.343  41.706  46.918  1.00 2.03  ? 187  LEU B N   1 
ATOM   6232  C  CA  . LEU B  1 187 ? 34.362  40.731  47.303  1.00 2.00  ? 187  LEU B CA  1 
ATOM   6233  C  C   . LEU B  1 187 ? 33.876  40.094  48.609  1.00 2.00  ? 187  LEU B C   1 
ATOM   6234  O  O   . LEU B  1 187 ? 34.468  40.309  49.657  1.00 2.05  ? 187  LEU B O   1 
ATOM   6235  C  CB  . LEU B  1 187 ? 35.695  41.413  47.561  1.00 2.00  ? 187  LEU B CB  1 
ATOM   6236  C  CG  . LEU B  1 187 ? 36.779  40.938  46.616  1.00 2.00  ? 187  LEU B CG  1 
ATOM   6237  C  CD1 . LEU B  1 187 ? 38.153  41.369  47.124  1.00 2.00  ? 187  LEU B CD1 1 
ATOM   6238  C  CD2 . LEU B  1 187 ? 36.686  39.427  46.510  1.00 2.00  ? 187  LEU B CD2 1 
ATOM   6239  N  N   . ASP B  1 188 ? 32.807  39.310  48.557  1.00 2.00  ? 188  ASP B N   1 
ATOM   6240  C  CA  . ASP B  1 188 ? 32.246  38.716  49.773  1.00 2.00  ? 188  ASP B CA  1 
ATOM   6241  C  C   . ASP B  1 188 ? 32.357  37.200  49.835  1.00 2.07  ? 188  ASP B C   1 
ATOM   6242  O  O   . ASP B  1 188 ? 31.512  36.532  50.447  1.00 2.31  ? 188  ASP B O   1 
ATOM   6243  C  CB  . ASP B  1 188 ? 30.780  39.084  49.849  1.00 3.08  ? 188  ASP B CB  1 
ATOM   6244  C  CG  . ASP B  1 188 ? 30.052  38.670  48.607  1.00 4.11  ? 188  ASP B CG  1 
ATOM   6245  O  OD1 . ASP B  1 188 ? 30.745  38.079  47.751  1.00 3.51  ? 188  ASP B OD1 1 
ATOM   6246  O  OD2 . ASP B  1 188 ? 28.835  38.919  48.476  1.00 4.12  ? 188  ASP B OD2 1 
ATOM   6247  N  N   . ALA B  1 189 ? 33.374  36.657  49.182  1.00 2.53  ? 189  ALA B N   1 
ATOM   6248  C  CA  . ALA B  1 189 ? 33.598  35.217  49.186  1.00 2.00  ? 189  ALA B CA  1 
ATOM   6249  C  C   . ALA B  1 189 ? 32.328  34.467  48.861  1.00 2.00  ? 189  ALA B C   1 
ATOM   6250  O  O   . ALA B  1 189 ? 32.005  33.460  49.475  1.00 2.45  ? 189  ALA B O   1 
ATOM   6251  C  CB  . ALA B  1 189 ? 34.114  34.791  50.533  1.00 2.00  ? 189  ALA B CB  1 
ATOM   6252  N  N   . SER B  1 190 ? 31.591  34.978  47.894  1.00 2.17  ? 190  SER B N   1 
ATOM   6253  C  CA  . SER B  1 190 ? 30.362  34.329  47.508  1.00 3.12  ? 190  SER B CA  1 
ATOM   6254  C  C   . SER B  1 190 ? 30.702  33.110  46.638  1.00 2.60  ? 190  SER B C   1 
ATOM   6255  O  O   . SER B  1 190 ? 29.814  32.499  46.042  1.00 3.74  ? 190  SER B O   1 
ATOM   6256  C  CB  . SER B  1 190 ? 29.500  35.302  46.722  1.00 3.54  ? 190  SER B CB  1 
ATOM   6257  O  OG  . SER B  1 190 ? 30.066  35.541  45.445  1.00 5.10  ? 190  SER B OG  1 
ATOM   6258  N  N   . LEU B  1 191 ? 31.980  32.763  46.529  1.00 2.58  ? 191  LEU B N   1 
ATOM   6259  C  CA  . LEU B  1 191 ? 32.341  31.595  45.724  1.00 3.85  ? 191  LEU B CA  1 
ATOM   6260  C  C   . LEU B  1 191 ? 32.448  30.433  46.685  1.00 5.45  ? 191  LEU B C   1 
ATOM   6261  O  O   . LEU B  1 191 ? 32.410  29.262  46.287  1.00 7.96  ? 191  LEU B O   1 
ATOM   6262  C  CB  . LEU B  1 191 ? 33.685  31.790  45.008  1.00 2.67  ? 191  LEU B CB  1 
ATOM   6263  C  CG  . LEU B  1 191 ? 35.018  31.938  45.747  1.00 2.15  ? 191  LEU B CG  1 
ATOM   6264  C  CD1 . LEU B  1 191 ? 36.112  32.199  44.713  1.00 3.58  ? 191  LEU B CD1 1 
ATOM   6265  C  CD2 . LEU B  1 191 ? 34.950  33.093  46.729  1.00 2.00  ? 191  LEU B CD2 1 
ATOM   6266  N  N   . VAL B  1 192 ? 32.578  30.784  47.960  1.00 3.68  ? 192  VAL B N   1 
ATOM   6267  C  CA  . VAL B  1 192 ? 32.709  29.818  49.022  1.00 2.00  ? 192  VAL B CA  1 
ATOM   6268  C  C   . VAL B  1 192 ? 31.361  29.526  49.642  1.00 2.21  ? 192  VAL B C   1 
ATOM   6269  O  O   . VAL B  1 192 ? 31.141  28.427  50.127  1.00 4.01  ? 192  VAL B O   1 
ATOM   6270  C  CB  . VAL B  1 192 ? 33.641  30.348  50.112  1.00 2.00  ? 192  VAL B CB  1 
ATOM   6271  C  CG1 . VAL B  1 192 ? 33.484  29.525  51.368  1.00 2.00  ? 192  VAL B CG1 1 
ATOM   6272  C  CG2 . VAL B  1 192 ? 35.082  30.317  49.626  1.00 2.44  ? 192  VAL B CG2 1 
ATOM   6273  N  N   . TYR B  1 193 ? 30.456  30.499  49.621  1.00 2.54  ? 193  TYR B N   1 
ATOM   6274  C  CA  . TYR B  1 193 ? 29.138  30.317  50.235  1.00 2.00  ? 193  TYR B CA  1 
ATOM   6275  C  C   . TYR B  1 193 ? 27.936  30.290  49.290  1.00 2.14  ? 193  TYR B C   1 
ATOM   6276  O  O   . TYR B  1 193 ? 26.850  29.860  49.679  1.00 2.00  ? 193  TYR B O   1 
ATOM   6277  C  CB  . TYR B  1 193 ? 28.927  31.396  51.290  1.00 2.00  ? 193  TYR B CB  1 
ATOM   6278  C  CG  . TYR B  1 193 ? 30.004  31.395  52.336  1.00 2.00  ? 193  TYR B CG  1 
ATOM   6279  C  CD1 . TYR B  1 193 ? 30.056  30.396  53.303  1.00 2.00  ? 193  TYR B CD1 1 
ATOM   6280  C  CD2 . TYR B  1 193 ? 31.000  32.366  52.334  1.00 2.00  ? 193  TYR B CD2 1 
ATOM   6281  C  CE1 . TYR B  1 193 ? 31.078  30.363  54.242  1.00 2.05  ? 193  TYR B CE1 1 
ATOM   6282  C  CE2 . TYR B  1 193 ? 32.027  32.342  53.269  1.00 2.00  ? 193  TYR B CE2 1 
ATOM   6283  C  CZ  . TYR B  1 193 ? 32.058  31.340  54.218  1.00 2.00  ? 193  TYR B CZ  1 
ATOM   6284  O  OH  . TYR B  1 193 ? 33.062  31.318  55.150  1.00 2.00  ? 193  TYR B OH  1 
ATOM   6285  N  N   . GLY B  1 194 ? 28.124  30.773  48.064  1.00 3.29  ? 194  GLY B N   1 
ATOM   6286  C  CA  . GLY B  1 194 ? 27.048  30.770  47.084  1.00 4.48  ? 194  GLY B CA  1 
ATOM   6287  C  C   . GLY B  1 194 ? 26.338  32.094  46.867  1.00 5.66  ? 194  GLY B C   1 
ATOM   6288  O  O   . GLY B  1 194 ? 26.606  33.069  47.579  1.00 5.48  ? 194  GLY B O   1 
ATOM   6289  N  N   . SER B  1 195 ? 25.432  32.127  45.883  1.00 6.80  ? 195  SER B N   1 
ATOM   6290  C  CA  . SER B  1 195 ? 24.666  33.333  45.569  1.00 7.74  ? 195  SER B CA  1 
ATOM   6291  C  C   . SER B  1 195 ? 23.139  33.190  45.633  1.00 9.84  ? 195  SER B C   1 
ATOM   6292  O  O   . SER B  1 195 ? 22.422  34.187  45.517  1.00 11.41 ? 195  SER B O   1 
ATOM   6293  C  CB  . SER B  1 195 ? 25.080  33.889  44.206  1.00 7.43  ? 195  SER B CB  1 
ATOM   6294  O  OG  . SER B  1 195 ? 26.382  34.451  44.269  1.00 6.82  ? 195  SER B OG  1 
ATOM   6295  N  N   . GLU B  1 196 ? 22.638  31.966  45.798  1.00 11.57 ? 196  GLU B N   1 
ATOM   6296  C  CA  . GLU B  1 196 ? 21.193  31.745  45.944  1.00 13.38 ? 196  GLU B CA  1 
ATOM   6297  C  C   . GLU B  1 196 ? 20.947  30.885  47.189  1.00 13.02 ? 196  GLU B C   1 
ATOM   6298  O  O   . GLU B  1 196 ? 21.333  29.714  47.231  1.00 13.04 ? 196  GLU B O   1 
ATOM   6299  C  CB  . GLU B  1 196 ? 20.588  31.070  44.711  1.00 15.94 ? 196  GLU B CB  1 
ATOM   6300  C  CG  . GLU B  1 196 ? 21.298  29.818  44.251  1.00 20.63 ? 196  GLU B CG  1 
ATOM   6301  C  CD  . GLU B  1 196 ? 20.394  28.920  43.427  1.00 22.44 ? 196  GLU B CD  1 
ATOM   6302  O  OE1 . GLU B  1 196 ? 19.477  28.321  44.029  1.00 23.54 ? 196  GLU B OE1 1 
ATOM   6303  O  OE2 . GLU B  1 196 ? 20.593  28.818  42.189  1.00 22.56 ? 196  GLU B OE2 1 
ATOM   6304  N  N   . PRO B  1 197 ? 20.290  31.461  48.216  1.00 11.41 ? 197  PRO B N   1 
ATOM   6305  C  CA  . PRO B  1 197 ? 19.958  30.825  49.502  1.00 9.54  ? 197  PRO B CA  1 
ATOM   6306  C  C   . PRO B  1 197 ? 19.717  29.326  49.376  1.00 9.70  ? 197  PRO B C   1 
ATOM   6307  O  O   . PRO B  1 197 ? 20.160  28.526  50.195  1.00 8.29  ? 197  PRO B O   1 
ATOM   6308  C  CB  . PRO B  1 197 ? 18.703  31.567  49.932  1.00 10.61 ? 197  PRO B CB  1 
ATOM   6309  C  CG  . PRO B  1 197 ? 18.938  32.929  49.406  1.00 11.51 ? 197  PRO B CG  1 
ATOM   6310  C  CD  . PRO B  1 197 ? 19.477  32.674  48.020  1.00 10.50 ? 197  PRO B CD  1 
ATOM   6311  N  N   . SER B  1 198 ? 18.986  28.969  48.338  1.00 10.10 ? 198  SER B N   1 
ATOM   6312  C  CA  . SER B  1 198 ? 18.681  27.592  48.043  1.00 10.29 ? 198  SER B CA  1 
ATOM   6313  C  C   . SER B  1 198 ? 19.963  26.765  48.189  1.00 12.77 ? 198  SER B C   1 
ATOM   6314  O  O   . SER B  1 198 ? 20.023  25.801  48.963  1.00 12.52 ? 198  SER B O   1 
ATOM   6315  C  CB  . SER B  1 198 ? 18.163  27.532  46.609  1.00 12.45 ? 198  SER B CB  1 
ATOM   6316  O  OG  . SER B  1 198 ? 18.156  28.845  46.043  1.00 13.63 ? 198  SER B OG  1 
ATOM   6317  N  N   . LEU B  1 199 ? 21.000  27.164  47.458  1.00 12.71 ? 199  LEU B N   1 
ATOM   6318  C  CA  . LEU B  1 199 ? 22.264  26.444  47.486  1.00 12.02 ? 199  LEU B CA  1 
ATOM   6319  C  C   . LEU B  1 199 ? 23.176  26.746  48.661  1.00 11.08 ? 199  LEU B C   1 
ATOM   6320  O  O   . LEU B  1 199 ? 24.059  25.950  48.973  1.00 12.20 ? 199  LEU B O   1 
ATOM   6321  C  CB  . LEU B  1 199 ? 23.040  26.693  46.197  1.00 12.53 ? 199  LEU B CB  1 
ATOM   6322  C  CG  . LEU B  1 199 ? 24.438  26.064  46.157  1.00 13.11 ? 199  LEU B CG  1 
ATOM   6323  C  CD1 . LEU B  1 199 ? 24.353  24.536  46.271  1.00 13.05 ? 199  LEU B CD1 1 
ATOM   6324  C  CD2 . LEU B  1 199 ? 25.118  26.467  44.861  1.00 14.12 ? 199  LEU B CD2 1 
ATOM   6325  N  N   . ALA B  1 200 ? 22.982  27.885  49.312  1.00 10.09 ? 200  ALA B N   1 
ATOM   6326  C  CA  . ALA B  1 200 ? 23.842  28.238  50.435  1.00 9.57  ? 200  ALA B CA  1 
ATOM   6327  C  C   . ALA B  1 200 ? 23.611  27.341  51.637  1.00 9.78  ? 200  ALA B C   1 
ATOM   6328  O  O   . ALA B  1 200 ? 24.464  27.259  52.524  1.00 10.73 ? 200  ALA B O   1 
ATOM   6329  C  CB  . ALA B  1 200 ? 23.638  29.687  50.825  1.00 10.22 ? 200  ALA B CB  1 
ATOM   6330  N  N   . SER B  1 201 ? 22.463  26.671  51.678  1.00 9.31  ? 201  SER B N   1 
ATOM   6331  C  CA  . SER B  1 201 ? 22.185  25.787  52.800  1.00 9.83  ? 201  SER B CA  1 
ATOM   6332  C  C   . SER B  1 201 ? 22.626  24.368  52.448  1.00 11.26 ? 201  SER B C   1 
ATOM   6333  O  O   . SER B  1 201 ? 23.025  23.601  53.331  1.00 11.57 ? 201  SER B O   1 
ATOM   6334  C  CB  . SER B  1 201 ? 20.697  25.823  53.174  1.00 7.92  ? 201  SER B CB  1 
ATOM   6335  O  OG  . SER B  1 201 ? 19.976  24.769  52.570  1.00 9.37  ? 201  SER B OG  1 
ATOM   6336  N  N   . ARG B  1 202 ? 22.568  24.016  51.163  1.00 10.71 ? 202  ARG B N   1 
ATOM   6337  C  CA  . ARG B  1 202 ? 23.003  22.684  50.745  1.00 11.71 ? 202  ARG B CA  1 
ATOM   6338  C  C   . ARG B  1 202 ? 24.459  22.509  51.151  1.00 10.20 ? 202  ARG B C   1 
ATOM   6339  O  O   . ARG B  1 202 ? 24.910  21.396  51.449  1.00 9.22  ? 202  ARG B O   1 
ATOM   6340  C  CB  . ARG B  1 202 ? 22.893  22.516  49.226  1.00 16.73 ? 202  ARG B CB  1 
ATOM   6341  C  CG  . ARG B  1 202 ? 21.508  22.173  48.689  1.00 24.79 ? 202  ARG B CG  1 
ATOM   6342  C  CD  . ARG B  1 202 ? 21.505  22.123  47.153  1.00 29.30 ? 202  ARG B CD  1 
ATOM   6343  N  NE  . ARG B  1 202 ? 22.556  21.254  46.620  1.00 35.40 ? 202  ARG B NE  1 
ATOM   6344  C  CZ  . ARG B  1 202 ? 22.621  19.938  46.823  1.00 37.80 ? 202  ARG B CZ  1 
ATOM   6345  N  NH1 . ARG B  1 202 ? 21.689  19.331  47.550  1.00 39.18 ? 202  ARG B NH1 1 
ATOM   6346  N  NH2 . ARG B  1 202 ? 23.614  19.223  46.297  1.00 39.09 ? 202  ARG B NH2 1 
ATOM   6347  N  N   . LEU B  1 203 ? 25.184  23.635  51.158  1.00 7.91  ? 203  LEU B N   1 
ATOM   6348  C  CA  . LEU B  1 203 ? 26.611  23.581  51.456  1.00 6.89  ? 203  LEU B CA  1 
ATOM   6349  C  C   . LEU B  1 203 ? 26.929  23.347  52.950  1.00 7.89  ? 203  LEU B C   1 
ATOM   6350  O  O   . LEU B  1 203 ? 28.087  23.253  53.342  1.00 8.59  ? 203  LEU B O   1 
ATOM   6351  C  CB  . LEU B  1 203 ? 27.287  24.885  50.892  1.00 5.96  ? 203  LEU B CB  1 
ATOM   6352  C  CG  . LEU B  1 203 ? 27.789  24.941  49.411  1.00 5.94  ? 203  LEU B CG  1 
ATOM   6353  C  CD1 . LEU B  1 203 ? 26.826  24.207  48.496  1.00 4.68  ? 203  LEU B CD1 1 
ATOM   6354  C  CD2 . LEU B  1 203 ? 27.952  26.390  48.966  1.00 3.69  ? 203  LEU B CD2 1 
ATOM   6355  N  N   . ARG B  1 204 ? 25.884  23.253  53.754  1.00 8.67  ? 204  ARG B N   1 
ATOM   6356  C  CA  . ARG B  1 204 ? 26.056  23.287  55.221  1.00 8.35  ? 204  ARG B CA  1 
ATOM   6357  C  C   . ARG B  1 204 ? 25.873  22.042  56.099  1.00 8.36  ? 204  ARG B C   1 
ATOM   6358  O  O   . ARG B  1 204 ? 24.861  21.341  55.998  1.00 9.12  ? 204  ARG B O   1 
ATOM   6359  C  CB  . ARG B  1 204 ? 25.072  24.340  55.707  1.00 6.55  ? 204  ARG B CB  1 
ATOM   6360  C  CG  . ARG B  1 204 ? 25.640  25.437  56.572  1.00 6.47  ? 204  ARG B CG  1 
ATOM   6361  C  CD  . ARG B  1 204 ? 24.658  26.576  56.592  1.00 4.07  ? 204  ARG B CD  1 
ATOM   6362  N  NE  . ARG B  1 204 ? 24.667  27.299  57.849  1.00 2.53  ? 204  ARG B NE  1 
ATOM   6363  C  CZ  . ARG B  1 204 ? 23.764  28.207  58.186  1.00 2.73  ? 204  ARG B CZ  1 
ATOM   6364  N  NH1 . ARG B  1 204 ? 22.774  28.506  57.356  1.00 4.78  ? 204  ARG B NH1 1 
ATOM   6365  N  NH2 . ARG B  1 204 ? 23.848  28.813  59.358  1.00 3.66  ? 204  ARG B NH2 1 
ATOM   6366  N  N   . ASN B  1 205 ? 26.882  21.774  56.938  1.00 8.14  ? 205  ASN B N   1 
ATOM   6367  C  CA  . ASN B  1 205 ? 26.755  20.766  57.954  1.00 8.77  ? 205  ASN B CA  1 
ATOM   6368  C  C   . ASN B  1 205 ? 25.699  21.432  58.847  1.00 9.55  ? 205  ASN B C   1 
ATOM   6369  O  O   . ASN B  1 205 ? 26.044  22.309  59.654  1.00 11.01 ? 205  ASN B O   1 
ATOM   6370  C  CB  . ASN B  1 205 ? 28.098  20.498  58.688  1.00 11.28 ? 205  ASN B CB  1 
ATOM   6371  C  CG  . ASN B  1 205 ? 28.143  19.240  59.499  1.00 15.60 ? 205  ASN B CG  1 
ATOM   6372  O  OD1 . ASN B  1 205 ? 27.120  18.855  60.072  1.00 12.67 ? 205  ASN B OD1 1 
ATOM   6373  N  ND2 . ASN B  1 205 ? 29.295  18.594  59.567  1.00 22.08 ? 205  ASN B ND2 1 
ATOM   6374  N  N   . LEU B  1 206 ? 24.415  21.044  58.721  1.00 7.78  ? 206  LEU B N   1 
ATOM   6375  C  CA  . LEU B  1 206 ? 23.378  21.645  59.577  1.00 5.28  ? 206  LEU B CA  1 
ATOM   6376  C  C   . LEU B  1 206 ? 22.728  20.626  60.492  1.00 7.30  ? 206  LEU B C   1 
ATOM   6377  O  O   . LEU B  1 206 ? 21.527  20.705  60.789  1.00 8.31  ? 206  LEU B O   1 
ATOM   6378  C  CB  . LEU B  1 206 ? 22.251  22.250  58.734  1.00 4.26  ? 206  LEU B CB  1 
ATOM   6379  C  CG  . LEU B  1 206 ? 22.484  23.556  57.981  1.00 3.79  ? 206  LEU B CG  1 
ATOM   6380  C  CD1 . LEU B  1 206 ? 21.269  23.910  57.151  1.00 2.00  ? 206  LEU B CD1 1 
ATOM   6381  C  CD2 . LEU B  1 206 ? 22.832  24.679  58.948  1.00 2.43  ? 206  LEU B CD2 1 
ATOM   6382  N  N   . SER B  1 207 ? 23.517  19.643  60.931  1.00 6.59  ? 207  SER B N   1 
ATOM   6383  C  CA  . SER B  1 207 ? 23.056  18.597  61.841  1.00 4.55  ? 207  SER B CA  1 
ATOM   6384  C  C   . SER B  1 207 ? 23.890  18.694  63.107  1.00 5.78  ? 207  SER B C   1 
ATOM   6385  O  O   . SER B  1 207 ? 23.538  18.159  64.154  1.00 7.53  ? 207  SER B O   1 
ATOM   6386  C  CB  . SER B  1 207 ? 23.205  17.235  61.186  1.00 2.45  ? 207  SER B CB  1 
ATOM   6387  O  OG  . SER B  1 207 ? 24.274  17.269  60.269  1.00 2.00  ? 207  SER B OG  1 
ATOM   6388  N  N   . SER B  1 208 ? 25.017  19.377  62.997  1.00 6.49  ? 208  SER B N   1 
ATOM   6389  C  CA  . SER B  1 208 ? 25.866  19.607  64.152  1.00 8.62  ? 208  SER B CA  1 
ATOM   6390  C  C   . SER B  1 208 ? 25.532  21.063  64.458  1.00 10.25 ? 208  SER B C   1 
ATOM   6391  O  O   . SER B  1 208 ? 25.528  21.895  63.551  1.00 12.39 ? 208  SER B O   1 
ATOM   6392  C  CB  . SER B  1 208 ? 27.347  19.454  63.776  1.00 8.25  ? 208  SER B CB  1 
ATOM   6393  O  OG  . SER B  1 208 ? 27.697  20.274  62.666  1.00 8.76  ? 208  SER B OG  1 
ATOM   6394  N  N   . PRO B  1 209 ? 25.206  21.393  65.718  1.00 9.47  ? 209  PRO B N   1 
ATOM   6395  C  CA  . PRO B  1 209 ? 24.887  22.797  65.994  1.00 9.50  ? 209  PRO B CA  1 
ATOM   6396  C  C   . PRO B  1 209 ? 26.134  23.630  66.273  1.00 8.08  ? 209  PRO B C   1 
ATOM   6397  O  O   . PRO B  1 209 ? 26.240  24.263  67.320  1.00 7.20  ? 209  PRO B O   1 
ATOM   6398  C  CB  . PRO B  1 209 ? 23.967  22.703  67.204  1.00 8.43  ? 209  PRO B CB  1 
ATOM   6399  C  CG  . PRO B  1 209 ? 24.596  21.610  67.973  1.00 11.28 ? 209  PRO B CG  1 
ATOM   6400  C  CD  . PRO B  1 209 ? 24.930  20.558  66.899  1.00 11.09 ? 209  PRO B CD  1 
ATOM   6401  N  N   . LEU B  1 210 ? 27.069  23.629  65.328  1.00 7.99  ? 210  LEU B N   1 
ATOM   6402  C  CA  . LEU B  1 210 ? 28.306  24.378  65.488  1.00 9.48  ? 210  LEU B CA  1 
ATOM   6403  C  C   . LEU B  1 210 ? 28.808  25.029  64.182  1.00 9.99  ? 210  LEU B C   1 
ATOM   6404  O  O   . LEU B  1 210 ? 30.019  25.080  63.925  1.00 9.54  ? 210  LEU B O   1 
ATOM   6405  C  CB  . LEU B  1 210 ? 29.376  23.457  66.082  1.00 10.83 ? 210  LEU B CB  1 
ATOM   6406  C  CG  . LEU B  1 210 ? 29.661  22.159  65.324  1.00 12.66 ? 210  LEU B CG  1 
ATOM   6407  C  CD1 . LEU B  1 210 ? 31.146  22.098  65.029  1.00 14.26 ? 210  LEU B CD1 1 
ATOM   6408  C  CD2 . LEU B  1 210 ? 29.227  20.941  66.131  1.00 13.00 ? 210  LEU B CD2 1 
ATOM   6409  N  N   . GLY B  1 211 ? 27.855  25.525  63.382  1.00 9.85  ? 211  GLY B N   1 
ATOM   6410  C  CA  . GLY B  1 211 ? 28.124  26.197  62.111  1.00 7.23  ? 211  GLY B CA  1 
ATOM   6411  C  C   . GLY B  1 211 ? 29.305  25.737  61.273  1.00 6.33  ? 211  GLY B C   1 
ATOM   6412  O  O   . GLY B  1 211 ? 30.397  26.262  61.418  1.00 6.40  ? 211  GLY B O   1 
ATOM   6413  N  N   . LEU B  1 212 ? 29.100  24.777  60.379  1.00 5.90  ? 212  LEU B N   1 
ATOM   6414  C  CA  . LEU B  1 212 ? 30.201  24.280  59.554  1.00 5.39  ? 212  LEU B CA  1 
ATOM   6415  C  C   . LEU B  1 212 ? 29.777  24.083  58.111  1.00 5.45  ? 212  LEU B C   1 
ATOM   6416  O  O   . LEU B  1 212 ? 28.583  23.951  57.808  1.00 6.90  ? 212  LEU B O   1 
ATOM   6417  C  CB  . LEU B  1 212 ? 30.719  22.932  60.074  1.00 3.44  ? 212  LEU B CB  1 
ATOM   6418  C  CG  . LEU B  1 212 ? 31.560  22.735  61.334  1.00 2.00  ? 212  LEU B CG  1 
ATOM   6419  C  CD1 . LEU B  1 212 ? 31.863  21.252  61.458  1.00 2.57  ? 212  LEU B CD1 1 
ATOM   6420  C  CD2 . LEU B  1 212 ? 32.860  23.503  61.255  1.00 2.00  ? 212  LEU B CD2 1 
ATOM   6421  N  N   . MET B  1 213 ? 30.762  24.045  57.221  1.00 4.09  ? 213  MET B N   1 
ATOM   6422  C  CA  . MET B  1 213 ? 30.478  23.837  55.814  1.00 3.75  ? 213  MET B CA  1 
ATOM   6423  C  C   . MET B  1 213 ? 30.397  22.346  55.557  1.00 3.08  ? 213  MET B C   1 
ATOM   6424  O  O   . MET B  1 213 ? 31.144  21.557  56.141  1.00 2.24  ? 213  MET B O   1 
ATOM   6425  C  CB  . MET B  1 213 ? 31.574  24.443  54.941  1.00 2.77  ? 213  MET B CB  1 
ATOM   6426  C  CG  . MET B  1 213 ? 31.599  25.944  54.947  1.00 2.00  ? 213  MET B CG  1 
ATOM   6427  S  SD  . MET B  1 213 ? 29.985  26.551  54.544  1.00 2.00  ? 213  MET B SD  1 
ATOM   6428  C  CE  . MET B  1 213 ? 29.950  26.268  52.801  1.00 2.45  ? 213  MET B CE  1 
ATOM   6429  N  N   . ALA B  1 214 ? 29.478  21.957  54.691  1.00 2.00  ? 214  ALA B N   1 
ATOM   6430  C  CA  . ALA B  1 214 ? 29.345  20.554  54.375  1.00 2.03  ? 214  ALA B CA  1 
ATOM   6431  C  C   . ALA B  1 214 ? 30.657  20.104  53.735  1.00 2.00  ? 214  ALA B C   1 
ATOM   6432  O  O   . ALA B  1 214 ? 31.227  20.844  52.940  1.00 2.31  ? 214  ALA B O   1 
ATOM   6433  C  CB  . ALA B  1 214 ? 28.188  20.361  53.411  1.00 2.00  ? 214  ALA B CB  1 
ATOM   6434  N  N   . VAL B  1 215 ? 31.148  18.917  54.094  1.00 2.00  ? 215  VAL B N   1 
ATOM   6435  C  CA  . VAL B  1 215 ? 32.382  18.389  53.499  1.00 2.53  ? 215  VAL B CA  1 
ATOM   6436  C  C   . VAL B  1 215 ? 32.231  16.927  53.032  1.00 4.11  ? 215  VAL B C   1 
ATOM   6437  O  O   . VAL B  1 215 ? 31.271  16.238  53.385  1.00 4.19  ? 215  VAL B O   1 
ATOM   6438  C  CB  . VAL B  1 215 ? 33.566  18.488  54.475  1.00 2.00  ? 215  VAL B CB  1 
ATOM   6439  C  CG1 . VAL B  1 215 ? 33.387  19.694  55.355  1.00 2.00  ? 215  VAL B CG1 1 
ATOM   6440  C  CG2 . VAL B  1 215 ? 33.696  17.219  55.287  1.00 2.83  ? 215  VAL B CG2 1 
ATOM   6441  N  N   . ASN B  1 216 ? 33.177  16.453  52.232  1.00 4.18  ? 216  ASN B N   1 
ATOM   6442  C  CA  . ASN B  1 216 ? 33.109  15.088  51.727  1.00 4.97  ? 216  ASN B CA  1 
ATOM   6443  C  C   . ASN B  1 216 ? 33.253  14.070  52.860  1.00 7.12  ? 216  ASN B C   1 
ATOM   6444  O  O   . ASN B  1 216 ? 34.083  14.232  53.762  1.00 4.94  ? 216  ASN B O   1 
ATOM   6445  C  CB  . ASN B  1 216 ? 34.209  14.859  50.683  1.00 4.82  ? 216  ASN B CB  1 
ATOM   6446  C  CG  . ASN B  1 216 ? 33.849  13.784  49.673  1.00 5.15  ? 216  ASN B CG  1 
ATOM   6447  O  OD1 . ASN B  1 216 ? 34.665  13.414  48.827  1.00 4.95  ? 216  ASN B OD1 1 
ATOM   6448  N  ND2 . ASN B  1 216 ? 32.621  13.285  49.749  1.00 5.70  ? 216  ASN B ND2 1 
ATOM   6449  N  N   . GLN B  1 217 ? 32.421  13.031  52.808  1.00 10.03 ? 217  GLN B N   1 
ATOM   6450  C  CA  . GLN B  1 217 ? 32.444  11.951  53.788  1.00 12.49 ? 217  GLN B CA  1 
ATOM   6451  C  C   . GLN B  1 217 ? 33.081  10.704  53.174  1.00 13.11 ? 217  GLN B C   1 
ATOM   6452  O  O   . GLN B  1 217 ? 33.333  9.732   53.878  1.00 13.96 ? 217  GLN B O   1 
ATOM   6453  C  CB  . GLN B  1 217 ? 31.024  11.596  54.250  1.00 16.58 ? 217  GLN B CB  1 
ATOM   6454  C  CG  . GLN B  1 217 ? 30.406  12.530  55.284  1.00 23.00 ? 217  GLN B CG  1 
ATOM   6455  C  CD  . GLN B  1 217 ? 31.280  12.700  56.516  1.00 26.75 ? 217  GLN B CD  1 
ATOM   6456  O  OE1 . GLN B  1 217 ? 31.783  13.794  56.784  1.00 30.09 ? 217  GLN B OE1 1 
ATOM   6457  N  NE2 . GLN B  1 217 ? 31.471  11.618  57.271  1.00 29.09 ? 217  GLN B NE2 1 
ATOM   6458  N  N   . GLU B  1 218 ? 33.346  10.736  51.867  1.00 13.62 ? 218  GLU B N   1 
ATOM   6459  C  CA  . GLU B  1 218 ? 33.934  9.594   51.159  1.00 12.81 ? 218  GLU B CA  1 
ATOM   6460  C  C   . GLU B  1 218 ? 35.369  9.754   50.669  1.00 11.41 ? 218  GLU B C   1 
ATOM   6461  O  O   . GLU B  1 218 ? 35.922  8.822   50.104  1.00 12.28 ? 218  GLU B O   1 
ATOM   6462  C  CB  . GLU B  1 218 ? 33.121  9.247   49.916  1.00 15.77 ? 218  GLU B CB  1 
ATOM   6463  C  CG  . GLU B  1 218 ? 31.627  9.198   50.058  1.00 20.36 ? 218  GLU B CG  1 
ATOM   6464  C  CD  . GLU B  1 218 ? 30.962  9.061   48.696  1.00 21.95 ? 218  GLU B CD  1 
ATOM   6465  O  OE1 . GLU B  1 218 ? 31.701  8.980   47.689  1.00 23.10 ? 218  GLU B OE1 1 
ATOM   6466  O  OE2 . GLU B  1 218 ? 29.713  9.035   48.629  1.00 23.77 ? 218  GLU B OE2 1 
ATOM   6467  N  N   . ALA B  1 219 ? 35.974  10.919  50.835  1.00 10.94 ? 219  ALA B N   1 
ATOM   6468  C  CA  . ALA B  1 219 ? 37.339  11.099  50.347  1.00 10.94 ? 219  ALA B CA  1 
ATOM   6469  C  C   . ALA B  1 219 ? 38.154  11.889  51.359  1.00 12.45 ? 219  ALA B C   1 
ATOM   6470  O  O   . ALA B  1 219 ? 37.626  12.772  52.020  1.00 12.88 ? 219  ALA B O   1 
ATOM   6471  C  CB  . ALA B  1 219 ? 37.305  11.832  49.004  1.00 11.12 ? 219  ALA B CB  1 
ATOM   6472  N  N   . TRP B  1 220 ? 39.439  11.579  51.499  1.00 15.00 ? 220  TRP B N   1 
ATOM   6473  C  CA  . TRP B  1 220 ? 40.253  12.322  52.459  1.00 16.81 ? 220  TRP B CA  1 
ATOM   6474  C  C   . TRP B  1 220 ? 41.642  12.718  52.008  1.00 17.63 ? 220  TRP B C   1 
ATOM   6475  O  O   . TRP B  1 220 ? 42.138  12.240  50.975  1.00 17.20 ? 220  TRP B O   1 
ATOM   6476  C  CB  . TRP B  1 220 ? 40.372  11.555  53.768  1.00 24.92 ? 220  TRP B CB  1 
ATOM   6477  C  CG  . TRP B  1 220 ? 39.058  11.133  54.263  1.00 32.76 ? 220  TRP B CG  1 
ATOM   6478  C  CD1 . TRP B  1 220 ? 38.443  9.938   54.030  1.00 34.84 ? 220  TRP B CD1 1 
ATOM   6479  C  CD2 . TRP B  1 220 ? 38.119  11.943  54.965  1.00 34.11 ? 220  TRP B CD2 1 
ATOM   6480  N  NE1 . TRP B  1 220 ? 37.166  9.954   54.538  1.00 37.17 ? 220  TRP B NE1 1 
ATOM   6481  C  CE2 . TRP B  1 220 ? 36.939  11.179  55.117  1.00 37.04 ? 220  TRP B CE2 1 
ATOM   6482  C  CE3 . TRP B  1 220 ? 38.153  13.246  55.481  1.00 37.60 ? 220  TRP B CE3 1 
ATOM   6483  C  CZ2 . TRP B  1 220 ? 35.798  11.676  55.760  1.00 38.83 ? 220  TRP B CZ2 1 
ATOM   6484  C  CZ3 . TRP B  1 220 ? 37.016  13.740  56.124  1.00 39.45 ? 220  TRP B CZ3 1 
ATOM   6485  C  CH2 . TRP B  1 220 ? 35.860  12.956  56.252  1.00 39.95 ? 220  TRP B CH2 1 
ATOM   6486  N  N   . ASP B  1 221 ? 42.264  13.581  52.817  1.00 15.20 ? 221  ASP B N   1 
ATOM   6487  C  CA  . ASP B  1 221 ? 43.606  14.097  52.556  1.00 15.64 ? 221  ASP B CA  1 
ATOM   6488  C  C   . ASP B  1 221 ? 44.415  14.243  53.838  1.00 16.19 ? 221  ASP B C   1 
ATOM   6489  O  O   . ASP B  1 221 ? 44.580  15.358  54.342  1.00 16.37 ? 221  ASP B O   1 
ATOM   6490  C  CB  . ASP B  1 221 ? 43.521  15.464  51.862  1.00 17.51 ? 221  ASP B CB  1 
ATOM   6491  C  CG  . ASP B  1 221 ? 44.890  15.992  51.439  1.00 20.93 ? 221  ASP B CG  1 
ATOM   6492  O  OD1 . ASP B  1 221 ? 45.788  15.152  51.208  1.00 22.93 ? 221  ASP B OD1 1 
ATOM   6493  O  OD2 . ASP B  1 221 ? 45.068  17.229  51.318  1.00 21.55 ? 221  ASP B OD2 1 
ATOM   6494  N  N   . HIS B  1 222 ? 44.930  13.127  54.356  1.00 16.46 ? 222  HIS B N   1 
ATOM   6495  C  CA  . HIS B  1 222 ? 45.718  13.135  55.595  1.00 17.40 ? 222  HIS B CA  1 
ATOM   6496  C  C   . HIS B  1 222 ? 44.883  13.633  56.787  1.00 16.31 ? 222  HIS B C   1 
ATOM   6497  O  O   . HIS B  1 222 ? 45.392  14.334  57.665  1.00 16.10 ? 222  HIS B O   1 
ATOM   6498  C  CB  . HIS B  1 222 ? 46.948  14.046  55.451  1.00 22.05 ? 222  HIS B CB  1 
ATOM   6499  C  CG  . HIS B  1 222 ? 47.970  13.558  54.470  1.00 25.98 ? 222  HIS B CG  1 
ATOM   6500  N  ND1 . HIS B  1 222 ? 49.036  14.335  54.065  1.00 26.81 ? 222  HIS B ND1 1 
ATOM   6501  C  CD2 . HIS B  1 222 ? 48.101  12.373  53.824  1.00 27.28 ? 222  HIS B CD2 1 
ATOM   6502  C  CE1 . HIS B  1 222 ? 49.777  13.651  53.211  1.00 28.17 ? 222  HIS B CE1 1 
ATOM   6503  N  NE2 . HIS B  1 222 ? 49.233  12.457  53.048  1.00 28.62 ? 222  HIS B NE2 1 
ATOM   6504  N  N   . GLY B  1 223 ? 43.607  13.277  56.830  1.00 13.96 ? 223  GLY B N   1 
ATOM   6505  C  CA  . GLY B  1 223 ? 42.780  13.749  57.924  1.00 11.16 ? 223  GLY B CA  1 
ATOM   6506  C  C   . GLY B  1 223 ? 42.359  15.188  57.682  1.00 9.83  ? 223  GLY B C   1 
ATOM   6507  O  O   . GLY B  1 223 ? 42.016  15.923  58.613  1.00 11.87 ? 223  GLY B O   1 
ATOM   6508  N  N   . LEU B  1 224 ? 42.411  15.600  56.422  1.00 6.69  ? 224  LEU B N   1 
ATOM   6509  C  CA  . LEU B  1 224 ? 42.008  16.943  56.035  1.00 4.53  ? 224  LEU B CA  1 
ATOM   6510  C  C   . LEU B  1 224 ? 40.945  16.720  54.982  1.00 2.02  ? 224  LEU B C   1 
ATOM   6511  O  O   . LEU B  1 224 ? 40.975  15.706  54.289  1.00 2.00  ? 224  LEU B O   1 
ATOM   6512  C  CB  . LEU B  1 224 ? 43.205  17.743  55.504  1.00 3.33  ? 224  LEU B CB  1 
ATOM   6513  C  CG  . LEU B  1 224 ? 44.199  18.157  56.603  1.00 2.00  ? 224  LEU B CG  1 
ATOM   6514  C  CD1 . LEU B  1 224 ? 45.304  19.029  56.060  1.00 2.00  ? 224  LEU B CD1 1 
ATOM   6515  C  CD2 . LEU B  1 224 ? 43.447  18.913  57.672  1.00 2.00  ? 224  LEU B CD2 1 
ATOM   6516  N  N   . ALA B  1 225 ? 40.011  17.660  54.867  1.00 2.00  ? 225  ALA B N   1 
ATOM   6517  C  CA  . ALA B  1 225 ? 38.882  17.510  53.954  1.00 2.00  ? 225  ALA B CA  1 
ATOM   6518  C  C   . ALA B  1 225 ? 38.920  18.106  52.563  1.00 2.00  ? 225  ALA B C   1 
ATOM   6519  O  O   . ALA B  1 225 ? 39.725  18.981  52.240  1.00 2.13  ? 225  ALA B O   1 
ATOM   6520  C  CB  . ALA B  1 225 ? 37.614  17.984  54.648  1.00 3.28  ? 225  ALA B CB  1 
ATOM   6521  N  N   . TYR B  1 226 ? 38.002  17.603  51.749  1.00 2.00  ? 226  TYR B N   1 
ATOM   6522  C  CA  . TYR B  1 226 ? 37.821  18.040  50.377  1.00 2.00  ? 226  TYR B CA  1 
ATOM   6523  C  C   . TYR B  1 226 ? 36.383  18.532  50.327  1.00 2.00  ? 226  TYR B C   1 
ATOM   6524  O  O   . TYR B  1 226 ? 35.588  18.222  51.204  1.00 2.00  ? 226  TYR B O   1 
ATOM   6525  C  CB  . TYR B  1 226 ? 37.921  16.861  49.405  1.00 3.47  ? 226  TYR B CB  1 
ATOM   6526  C  CG  . TYR B  1 226 ? 39.264  16.176  49.246  1.00 2.67  ? 226  TYR B CG  1 
ATOM   6527  C  CD1 . TYR B  1 226 ? 39.366  14.797  49.376  1.00 2.00  ? 226  TYR B CD1 1 
ATOM   6528  C  CD2 . TYR B  1 226 ? 40.394  16.878  48.837  1.00 2.00  ? 226  TYR B CD2 1 
ATOM   6529  C  CE1 . TYR B  1 226 ? 40.542  14.132  49.093  1.00 2.75  ? 226  TYR B CE1 1 
ATOM   6530  C  CE2 . TYR B  1 226 ? 41.584  16.215  48.551  1.00 2.83  ? 226  TYR B CE2 1 
ATOM   6531  C  CZ  . TYR B  1 226 ? 41.646  14.838  48.677  1.00 3.05  ? 226  TYR B CZ  1 
ATOM   6532  O  OH  . TYR B  1 226 ? 42.795  14.145  48.355  1.00 4.43  ? 226  TYR B OH  1 
ATOM   6533  N  N   . PRO B  1 227 ? 36.030  19.314  49.309  1.00 2.11  ? 227  PRO B N   1 
ATOM   6534  C  CA  . PRO B  1 227 ? 34.635  19.763  49.271  1.00 2.92  ? 227  PRO B CA  1 
ATOM   6535  C  C   . PRO B  1 227 ? 33.737  18.547  48.993  1.00 3.13  ? 227  PRO B C   1 
ATOM   6536  O  O   . PRO B  1 227 ? 34.229  17.497  48.577  1.00 5.55  ? 227  PRO B O   1 
ATOM   6537  C  CB  . PRO B  1 227 ? 34.634  20.759  48.118  1.00 2.90  ? 227  PRO B CB  1 
ATOM   6538  C  CG  . PRO B  1 227 ? 36.018  21.359  48.211  1.00 3.58  ? 227  PRO B CG  1 
ATOM   6539  C  CD  . PRO B  1 227 ? 36.883  20.144  48.441  1.00 2.48  ? 227  PRO B CD  1 
ATOM   6540  N  N   . PRO B  1 228 ? 32.419  18.664  49.229  1.00 2.08  ? 228  PRO B N   1 
ATOM   6541  C  CA  . PRO B  1 228 ? 31.509  17.543  48.980  1.00 2.00  ? 228  PRO B CA  1 
ATOM   6542  C  C   . PRO B  1 228 ? 31.395  17.304  47.495  1.00 2.00  ? 228  PRO B C   1 
ATOM   6543  O  O   . PRO B  1 228 ? 31.422  18.254  46.716  1.00 2.15  ? 228  PRO B O   1 
ATOM   6544  C  CB  . PRO B  1 228 ? 30.186  18.031  49.545  1.00 2.00  ? 228  PRO B CB  1 
ATOM   6545  C  CG  . PRO B  1 228 ? 30.595  19.000  50.589  1.00 2.69  ? 228  PRO B CG  1 
ATOM   6546  C  CD  . PRO B  1 228 ? 31.711  19.752  49.917  1.00 2.46  ? 228  PRO B CD  1 
ATOM   6547  N  N   . PHE B  1 229 ? 31.267  16.042  47.102  1.00 2.47  ? 229  PHE B N   1 
ATOM   6548  C  CA  . PHE B  1 229 ? 31.134  15.711  45.695  1.00 3.57  ? 229  PHE B CA  1 
ATOM   6549  C  C   . PHE B  1 229 ? 29.831  16.256  45.206  1.00 5.66  ? 229  PHE B C   1 
ATOM   6550  O  O   . PHE B  1 229 ? 28.855  16.280  45.942  1.00 5.04  ? 229  PHE B O   1 
ATOM   6551  C  CB  . PHE B  1 229 ? 31.130  14.214  45.473  1.00 2.39  ? 229  PHE B CB  1 
ATOM   6552  C  CG  . PHE B  1 229 ? 32.481  13.604  45.500  1.00 3.14  ? 229  PHE B CG  1 
ATOM   6553  C  CD1 . PHE B  1 229 ? 33.558  14.253  44.907  1.00 2.71  ? 229  PHE B CD1 1 
ATOM   6554  C  CD2 . PHE B  1 229 ? 32.674  12.350  46.068  1.00 3.91  ? 229  PHE B CD2 1 
ATOM   6555  C  CE1 . PHE B  1 229 ? 34.814  13.660  44.873  1.00 4.14  ? 229  PHE B CE1 1 
ATOM   6556  C  CE2 . PHE B  1 229 ? 33.920  11.745  46.043  1.00 4.46  ? 229  PHE B CE2 1 
ATOM   6557  C  CZ  . PHE B  1 229 ? 35.000  12.401  45.441  1.00 3.97  ? 229  PHE B CZ  1 
ATOM   6558  N  N   . ASN B  1 230 ? 29.805  16.687  43.957  1.00 10.32 ? 230  ASN B N   1 
ATOM   6559  C  CA  . ASN B  1 230 ? 28.582  17.232  43.416  1.00 15.81 ? 230  ASN B CA  1 
ATOM   6560  C  C   . ASN B  1 230 ? 27.613  16.114  43.093  1.00 21.12 ? 230  ASN B C   1 
ATOM   6561  O  O   . ASN B  1 230 ? 28.006  15.016  42.702  1.00 21.52 ? 230  ASN B O   1 
ATOM   6562  C  CB  . ASN B  1 230 ? 28.860  18.053  42.173  1.00 16.39 ? 230  ASN B CB  1 
ATOM   6563  C  CG  . ASN B  1 230 ? 27.604  18.571  41.548  1.00 16.02 ? 230  ASN B CG  1 
ATOM   6564  O  OD1 . ASN B  1 230 ? 26.745  19.116  42.232  1.00 16.63 ? 230  ASN B OD1 1 
ATOM   6565  N  ND2 . ASN B  1 230 ? 27.483  18.408  40.241  1.00 18.63 ? 230  ASN B ND2 1 
ATOM   6566  N  N   . ASN B  1 231 ? 26.334  16.411  43.260  1.00 26.21 ? 231  ASN B N   1 
ATOM   6567  C  CA  . ASN B  1 231 ? 25.278  15.438  43.023  1.00 29.72 ? 231  ASN B CA  1 
ATOM   6568  C  C   . ASN B  1 231 ? 25.130  14.989  41.572  1.00 30.46 ? 231  ASN B C   1 
ATOM   6569  O  O   . ASN B  1 231 ? 25.748  14.018  41.140  1.00 29.89 ? 231  ASN B O   1 
ATOM   6570  C  CB  . ASN B  1 231 ? 23.948  16.022  43.497  1.00 33.88 ? 231  ASN B CB  1 
ATOM   6571  C  CG  . ASN B  1 231 ? 23.549  15.538  44.871  1.00 37.10 ? 231  ASN B CG  1 
ATOM   6572  O  OD1 . ASN B  1 231 ? 24.398  15.138  45.671  1.00 38.51 ? 231  ASN B OD1 1 
ATOM   6573  N  ND2 . ASN B  1 231 ? 22.245  15.585  45.161  1.00 37.95 ? 231  ASN B ND2 1 
ATOM   6574  N  N   . MET B  1 232 ? 24.278  15.730  40.874  1.00 32.26 ? 232  MET B N   1 
ATOM   6575  C  CA  . MET B  1 232 ? 23.912  15.521  39.494  1.00 33.33 ? 232  MET B CA  1 
ATOM   6576  C  C   . MET B  1 232 ? 24.753  14.585  38.650  1.00 32.23 ? 232  MET B C   1 
ATOM   6577  O  O   . MET B  1 232 ? 25.966  14.760  38.519  1.00 29.43 ? 232  MET B O   1 
ATOM   6578  C  CB  . MET B  1 232 ? 23.827  16.869  38.754  1.00 37.15 ? 232  MET B CB  1 
ATOM   6579  C  CG  . MET B  1 232 ? 22.552  17.064  37.950  1.00 41.59 ? 232  MET B CG  1 
ATOM   6580  S  SD  . MET B  1 232 ? 21.654  18.564  38.508  1.00 48.29 ? 232  MET B SD  1 
ATOM   6581  C  CE  . MET B  1 232 ? 19.907  17.961  38.584  1.00 47.18 ? 232  MET B CE  1 
ATOM   6582  N  N   . LYS B  1 233 ? 24.101  13.579  38.092  1.00 32.39 ? 233  LYS B N   1 
ATOM   6583  C  CA  . LYS B  1 233 ? 24.772  12.691  37.162  1.00 30.82 ? 233  LYS B CA  1 
ATOM   6584  C  C   . LYS B  1 233 ? 24.498  13.326  35.793  1.00 29.89 ? 233  LYS B C   1 
ATOM   6585  O  O   . LYS B  1 233 ? 23.481  14.026  35.658  1.00 31.14 ? 233  LYS B O   1 
ATOM   6586  C  CB  . LYS B  1 233 ? 24.186  11.263  37.278  1.00 31.84 ? 233  LYS B CB  1 
ATOM   6587  C  CG  . LYS B  1 233 ? 24.797  10.467  38.440  1.00 34.54 ? 233  LYS B CG  1 
ATOM   6588  C  CD  . LYS B  1 233 ? 26.267  10.110  38.115  1.00 35.25 ? 233  LYS B CD  1 
ATOM   6589  C  CE  . LYS B  1 233 ? 26.968  9.360   39.276  1.00 37.02 ? 233  LYS B CE  1 
ATOM   6590  N  NZ  . LYS B  1 233 ? 27.788  8.170   38.817  1.00 36.53 ? 233  LYS B NZ  1 
ATOM   6591  N  N   . PRO B  1 234 ? 25.471  13.266  34.851  1.00 26.96 ? 234  PRO B N   1 
ATOM   6592  C  CA  . PRO B  1 234 ? 26.279  13.412  33.665  1.00 24.24 ? 234  PRO B CA  1 
ATOM   6593  C  C   . PRO B  1 234 ? 27.203  14.553  33.894  1.00 22.65 ? 234  PRO B C   1 
ATOM   6594  O  O   . PRO B  1 234 ? 27.137  15.599  33.259  1.00 24.01 ? 234  PRO B O   1 
ATOM   6595  C  CB  . PRO B  1 234 ? 25.201  13.722  32.620  1.00 24.39 ? 234  PRO B CB  1 
ATOM   6596  C  CG  . PRO B  1 234 ? 24.168  12.714  32.958  1.00 26.94 ? 234  PRO B CG  1 
ATOM   6597  C  CD  . PRO B  1 234 ? 24.570  12.227  34.414  1.00 27.57 ? 234  PRO B CD  1 
ATOM   6598  N  N   . SER B  1 235 ? 28.005  14.362  34.917  1.00 18.93 ? 235  SER B N   1 
ATOM   6599  C  CA  . SER B  1 235 ? 28.987  15.356  35.311  1.00 14.81 ? 235  SER B CA  1 
ATOM   6600  C  C   . SER B  1 235 ? 30.190  15.075  34.443  1.00 13.14 ? 235  SER B C   1 
ATOM   6601  O  O   . SER B  1 235 ? 30.439  13.940  34.074  1.00 13.72 ? 235  SER B O   1 
ATOM   6602  C  CB  . SER B  1 235 ? 29.371  15.205  36.782  1.00 13.89 ? 235  SER B CB  1 
ATOM   6603  O  OG  . SER B  1 235 ? 30.267  14.129  36.907  1.00 11.64 ? 235  SER B OG  1 
ATOM   6604  N  N   . PRO B  1 236 ? 30.965  16.112  34.110  1.00 11.18 ? 236  PRO B N   1 
ATOM   6605  C  CA  . PRO B  1 236 ? 32.118  15.813  33.266  1.00 8.34  ? 236  PRO B CA  1 
ATOM   6606  C  C   . PRO B  1 236 ? 33.345  15.289  34.002  1.00 7.67  ? 236  PRO B C   1 
ATOM   6607  O  O   . PRO B  1 236 ? 34.079  14.482  33.450  1.00 7.68  ? 236  PRO B O   1 
ATOM   6608  C  CB  . PRO B  1 236 ? 32.362  17.136  32.547  1.00 10.38 ? 236  PRO B CB  1 
ATOM   6609  C  CG  . PRO B  1 236 ? 31.990  18.141  33.583  1.00 9.74  ? 236  PRO B CG  1 
ATOM   6610  C  CD  . PRO B  1 236 ? 30.728  17.567  34.196  1.00 10.57 ? 236  PRO B CD  1 
ATOM   6611  N  N   . CYS B  1 237 ? 33.578  15.716  35.241  1.00 6.83  ? 237  CYS B N   1 
ATOM   6612  C  CA  . CYS B  1 237 ? 34.758  15.225  35.968  1.00 7.01  ? 237  CYS B CA  1 
ATOM   6613  C  C   . CYS B  1 237 ? 34.833  13.705  36.005  1.00 8.35  ? 237  CYS B C   1 
ATOM   6614  O  O   . CYS B  1 237 ? 35.885  13.145  36.320  1.00 8.11  ? 237  CYS B O   1 
ATOM   6615  C  CB  . CYS B  1 237 ? 34.799  15.754  37.404  1.00 7.21  ? 237  CYS B CB  1 
ATOM   6616  S  SG  . CYS B  1 237 ? 34.801  17.561  37.473  1.00 4.98  ? 237  CYS B SG  1 
ATOM   6617  N  N   . GLU B  1 238 ? 33.714  13.043  35.712  1.00 9.32  ? 238  GLU B N   1 
ATOM   6618  C  CA  . GLU B  1 238 ? 33.665  11.583  35.684  1.00 10.35 ? 238  GLU B CA  1 
ATOM   6619  C  C   . GLU B  1 238 ? 34.138  11.099  34.315  1.00 12.17 ? 238  GLU B C   1 
ATOM   6620  O  O   . GLU B  1 238 ? 34.959  10.182  34.207  1.00 11.79 ? 238  GLU B O   1 
ATOM   6621  C  CB  . GLU B  1 238 ? 32.239  11.078  35.892  1.00 11.52 ? 238  GLU B CB  1 
ATOM   6622  C  CG  . GLU B  1 238 ? 31.666  11.245  37.280  1.00 14.85 ? 238  GLU B CG  1 
ATOM   6623  C  CD  . GLU B  1 238 ? 30.482  10.307  37.513  1.00 16.35 ? 238  GLU B CD  1 
ATOM   6624  O  OE1 . GLU B  1 238 ? 29.858  10.367  38.598  1.00 18.43 ? 238  GLU B OE1 1 
ATOM   6625  O  OE2 . GLU B  1 238 ? 30.180  9.500   36.604  1.00 17.59 ? 238  GLU B OE2 1 
ATOM   6626  N  N   . PHE B  1 239 ? 33.588  11.722  33.276  1.00 12.08 ? 239  PHE B N   1 
ATOM   6627  C  CA  . PHE B  1 239 ? 33.902  11.399  31.890  1.00 12.31 ? 239  PHE B CA  1 
ATOM   6628  C  C   . PHE B  1 239 ? 35.410  11.301  31.667  1.00 13.17 ? 239  PHE B C   1 
ATOM   6629  O  O   . PHE B  1 239 ? 35.904  10.263  31.219  1.00 14.21 ? 239  PHE B O   1 
ATOM   6630  C  CB  . PHE B  1 239 ? 33.314  12.470  30.975  1.00 14.62 ? 239  PHE B CB  1 
ATOM   6631  C  CG  . PHE B  1 239 ? 33.260  12.082  29.522  1.00 16.76 ? 239  PHE B CG  1 
ATOM   6632  C  CD1 . PHE B  1 239 ? 32.671  10.884  29.126  1.00 18.16 ? 239  PHE B CD1 1 
ATOM   6633  C  CD2 . PHE B  1 239 ? 33.716  12.962  28.539  1.00 17.16 ? 239  PHE B CD2 1 
ATOM   6634  C  CE1 . PHE B  1 239 ? 32.530  10.575  27.765  1.00 20.21 ? 239  PHE B CE1 1 
ATOM   6635  C  CE2 . PHE B  1 239 ? 33.581  12.668  27.178  1.00 17.03 ? 239  PHE B CE2 1 
ATOM   6636  C  CZ  . PHE B  1 239 ? 32.985  11.476  26.787  1.00 19.11 ? 239  PHE B CZ  1 
ATOM   6637  N  N   . ILE B  1 240 ? 36.129  12.376  32.001  1.00 11.26 ? 240  ILE B N   1 
ATOM   6638  C  CA  . ILE B  1 240 ? 37.578  12.441  31.823  1.00 9.90  ? 240  ILE B CA  1 
ATOM   6639  C  C   . ILE B  1 240 ? 38.293  11.098  32.041  1.00 9.60  ? 240  ILE B C   1 
ATOM   6640  O  O   . ILE B  1 240 ? 39.006  10.651  31.141  1.00 10.69 ? 240  ILE B O   1 
ATOM   6641  C  CB  . ILE B  1 240 ? 38.201  13.562  32.685  1.00 7.97  ? 240  ILE B CB  1 
ATOM   6642  C  CG1 . ILE B  1 240 ? 37.764  14.934  32.149  1.00 8.54  ? 240  ILE B CG1 1 
ATOM   6643  C  CG2 . ILE B  1 240 ? 39.711  13.491  32.615  1.00 10.38 ? 240  ILE B CG2 1 
ATOM   6644  C  CD1 . ILE B  1 240 ? 38.040  15.137  30.672  1.00 5.84  ? 240  ILE B CD1 1 
ATOM   6645  N  N   . ASN B  1 241 ? 38.143  10.471  33.211  1.00 8.42  ? 241  ASN B N   1 
ATOM   6646  C  CA  . ASN B  1 241 ? 38.720  9.130   33.453  1.00 7.86  ? 241  ASN B CA  1 
ATOM   6647  C  C   . ASN B  1 241 ? 37.521  8.301   33.854  1.00 8.63  ? 241  ASN B C   1 
ATOM   6648  O  O   . ASN B  1 241 ? 37.108  8.300   35.012  1.00 7.08  ? 241  ASN B O   1 
ATOM   6649  C  CB  . ASN B  1 241 ? 39.748  9.063   34.598  1.00 10.14 ? 241  ASN B CB  1 
ATOM   6650  C  CG  . ASN B  1 241 ? 40.298  7.631   34.828  1.00 13.38 ? 241  ASN B CG  1 
ATOM   6651  O  OD1 . ASN B  1 241 ? 39.581  6.697   35.156  1.00 9.12  ? 241  ASN B OD1 1 
ATOM   6652  N  ND2 . ASN B  1 241 ? 41.597  7.480   34.612  1.00 21.92 ? 241  ASN B ND2 1 
ATOM   6653  N  N   . THR B  1 242 ? 36.939  7.631   32.872  1.00 10.18 ? 242  THR B N   1 
ATOM   6654  C  CA  . THR B  1 242 ? 35.777  6.788   33.097  1.00 11.66 ? 242  THR B CA  1 
ATOM   6655  C  C   . THR B  1 242 ? 36.006  5.771   34.210  1.00 12.84 ? 242  THR B C   1 
ATOM   6656  O  O   . THR B  1 242 ? 35.119  5.504   35.018  1.00 13.01 ? 242  THR B O   1 
ATOM   6657  C  CB  . THR B  1 242 ? 35.427  6.023   31.829  1.00 12.18 ? 242  THR B CB  1 
ATOM   6658  O  OG1 . THR B  1 242 ? 36.346  6.394   30.786  1.00 11.42 ? 242  THR B OG1 1 
ATOM   6659  C  CG2 . THR B  1 242 ? 33.996  6.332   31.413  1.00 13.45 ? 242  THR B CG2 1 
ATOM   6660  N  N   . THR B  1 243 ? 37.206  5.207   34.244  1.00 14.30 ? 243  THR B N   1 
ATOM   6661  C  CA  . THR B  1 243 ? 37.553  4.203   35.243  1.00 14.04 ? 243  THR B CA  1 
ATOM   6662  C  C   . THR B  1 243 ? 37.500  4.746   36.666  1.00 14.52 ? 243  THR B C   1 
ATOM   6663  O  O   . THR B  1 243 ? 36.716  4.273   37.488  1.00 14.08 ? 243  THR B O   1 
ATOM   6664  C  CB  . THR B  1 243 ? 38.966  3.628   34.976  1.00 14.36 ? 243  THR B CB  1 
ATOM   6665  O  OG1 . THR B  1 243 ? 38.942  2.835   33.784  1.00 12.11 ? 243  THR B OG1 1 
ATOM   6666  C  CG2 . THR B  1 243 ? 39.429  2.779   36.146  1.00 14.57 ? 243  THR B CG2 1 
ATOM   6667  N  N   . ALA B  1 244 ? 38.346  5.737   36.937  1.00 15.50 ? 244  ALA B N   1 
ATOM   6668  C  CA  . ALA B  1 244 ? 38.445  6.375   38.247  1.00 15.31 ? 244  ALA B CA  1 
ATOM   6669  C  C   . ALA B  1 244 ? 37.086  6.674   38.865  1.00 15.75 ? 244  ALA B C   1 
ATOM   6670  O  O   . ALA B  1 244 ? 36.876  6.418   40.050  1.00 14.49 ? 244  ALA B O   1 
ATOM   6671  C  CB  . ALA B  1 244 ? 39.266  7.661   38.135  1.00 14.96 ? 244  ALA B CB  1 
ATOM   6672  N  N   . ARG B  1 245 ? 36.174  7.225   38.066  1.00 17.43 ? 245  ARG B N   1 
ATOM   6673  C  CA  . ARG B  1 245 ? 34.821  7.552   38.527  1.00 18.86 ? 245  ARG B CA  1 
ATOM   6674  C  C   . ARG B  1 245 ? 34.726  8.480   39.746  1.00 17.85 ? 245  ARG B C   1 
ATOM   6675  O  O   . ARG B  1 245 ? 33.982  8.196   40.692  1.00 17.30 ? 245  ARG B O   1 
ATOM   6676  C  CB  . ARG B  1 245 ? 34.053  6.265   38.833  1.00 23.52 ? 245  ARG B CB  1 
ATOM   6677  C  CG  . ARG B  1 245 ? 33.607  5.495   37.612  1.00 29.63 ? 245  ARG B CG  1 
ATOM   6678  C  CD  . ARG B  1 245 ? 33.290  4.061   37.993  1.00 34.61 ? 245  ARG B CD  1 
ATOM   6679  N  NE  . ARG B  1 245 ? 32.329  3.985   39.089  1.00 39.41 ? 245  ARG B NE  1 
ATOM   6680  C  CZ  . ARG B  1 245 ? 32.526  3.289   40.204  1.00 41.46 ? 245  ARG B CZ  1 
ATOM   6681  N  NH1 . ARG B  1 245 ? 33.657  2.607   40.373  1.00 42.88 ? 245  ARG B NH1 1 
ATOM   6682  N  NH2 . ARG B  1 245 ? 31.588  3.268   41.145  1.00 42.68 ? 245  ARG B NH2 1 
ATOM   6683  N  N   . VAL B  1 246 ? 35.480  9.576   39.723  1.00 15.42 ? 246  VAL B N   1 
ATOM   6684  C  CA  . VAL B  1 246 ? 35.457  10.555  40.809  1.00 13.39 ? 246  VAL B CA  1 
ATOM   6685  C  C   . VAL B  1 246 ? 34.882  11.838  40.220  1.00 13.02 ? 246  VAL B C   1 
ATOM   6686  O  O   . VAL B  1 246 ? 35.475  12.439  39.324  1.00 15.14 ? 246  VAL B O   1 
ATOM   6687  C  CB  . VAL B  1 246 ? 36.873  10.880  41.351  1.00 12.47 ? 246  VAL B CB  1 
ATOM   6688  C  CG1 . VAL B  1 246 ? 36.846  10.897  42.871  1.00 12.82 ? 246  VAL B CG1 1 
ATOM   6689  C  CG2 . VAL B  1 246 ? 37.887  9.885   40.830  1.00 10.52 ? 246  VAL B CG2 1 
ATOM   6690  N  N   . PRO B  1 247 ? 33.719  12.277  40.712  1.00 10.26 ? 247  PRO B N   1 
ATOM   6691  C  CA  . PRO B  1 247 ? 33.113  13.498  40.186  1.00 10.13 ? 247  PRO B CA  1 
ATOM   6692  C  C   . PRO B  1 247 ? 33.732  14.812  40.664  1.00 9.28  ? 247  PRO B C   1 
ATOM   6693  O  O   . PRO B  1 247 ? 34.703  14.837  41.426  1.00 9.04  ? 247  PRO B O   1 
ATOM   6694  C  CB  . PRO B  1 247 ? 31.665  13.365  40.626  1.00 9.92  ? 247  PRO B CB  1 
ATOM   6695  C  CG  . PRO B  1 247 ? 31.813  12.729  41.961  1.00 10.47 ? 247  PRO B CG  1 
ATOM   6696  C  CD  . PRO B  1 247 ? 32.822  11.632  41.683  1.00 10.42 ? 247  PRO B CD  1 
ATOM   6697  N  N   . CYS B  1 248 ? 33.131  15.901  40.197  1.00 7.79  ? 248  CYS B N   1 
ATOM   6698  C  CA  . CYS B  1 248 ? 33.549  17.248  40.522  1.00 5.48  ? 248  CYS B CA  1 
ATOM   6699  C  C   . CYS B  1 248 ? 33.202  17.609  41.942  1.00 5.88  ? 248  CYS B C   1 
ATOM   6700  O  O   . CYS B  1 248 ? 32.327  17.014  42.559  1.00 4.92  ? 248  CYS B O   1 
ATOM   6701  C  CB  . CYS B  1 248 ? 32.827  18.254  39.648  1.00 6.28  ? 248  CYS B CB  1 
ATOM   6702  S  SG  . CYS B  1 248 ? 32.861  17.967  37.863  1.00 7.80  ? 248  CYS B SG  1 
ATOM   6703  N  N   . PHE B  1 249 ? 33.878  18.624  42.441  1.00 6.40  ? 249  PHE B N   1 
ATOM   6704  C  CA  . PHE B  1 249 ? 33.618  19.109  43.770  1.00 6.76  ? 249  PHE B CA  1 
ATOM   6705  C  C   . PHE B  1 249 ? 32.486  20.089  43.617  1.00 7.20  ? 249  PHE B C   1 
ATOM   6706  O  O   . PHE B  1 249 ? 32.268  20.627  42.533  1.00 6.73  ? 249  PHE B O   1 
ATOM   6707  C  CB  . PHE B  1 249 ? 34.838  19.834  44.315  1.00 8.87  ? 249  PHE B CB  1 
ATOM   6708  C  CG  . PHE B  1 249 ? 35.971  18.924  44.679  1.00 10.17 ? 249  PHE B CG  1 
ATOM   6709  C  CD1 . PHE B  1 249 ? 35.730  17.737  45.360  1.00 10.80 ? 249  PHE B CD1 1 
ATOM   6710  C  CD2 . PHE B  1 249 ? 37.282  19.293  44.417  1.00 10.66 ? 249  PHE B CD2 1 
ATOM   6711  C  CE1 . PHE B  1 249 ? 36.777  16.939  45.780  1.00 11.44 ? 249  PHE B CE1 1 
ATOM   6712  C  CE2 . PHE B  1 249 ? 38.339  18.502  44.835  1.00 11.37 ? 249  PHE B CE2 1 
ATOM   6713  C  CZ  . PHE B  1 249 ? 38.087  17.323  45.520  1.00 12.14 ? 249  PHE B CZ  1 
ATOM   6714  N  N   . GLN B  1 250 ? 31.755  20.322  44.694  1.00 8.91  ? 250  GLN B N   1 
ATOM   6715  C  CA  . GLN B  1 250 ? 30.665  21.273  44.624  1.00 10.27 ? 250  GLN B CA  1 
ATOM   6716  C  C   . GLN B  1 250 ? 30.931  22.404  45.594  1.00 10.69 ? 250  GLN B C   1 
ATOM   6717  O  O   . GLN B  1 250 ? 31.179  22.183  46.782  1.00 11.31 ? 250  GLN B O   1 
ATOM   6718  C  CB  . GLN B  1 250 ? 29.344  20.581  44.929  1.00 12.22 ? 250  GLN B CB  1 
ATOM   6719  C  CG  . GLN B  1 250 ? 28.145  21.237  44.284  1.00 18.24 ? 250  GLN B CG  1 
ATOM   6720  C  CD  . GLN B  1 250 ? 26.887  20.931  45.054  1.00 21.38 ? 250  GLN B CD  1 
ATOM   6721  O  OE1 . GLN B  1 250 ? 26.768  19.889  45.697  1.00 22.80 ? 250  GLN B OE1 1 
ATOM   6722  N  NE2 . GLN B  1 250 ? 25.799  21.700  45.114  1.00 24.26 ? 250  GLN B NE2 1 
ATOM   6723  N  N   . ALA B  1 251 ? 30.849  23.624  45.079  1.00 9.32  ? 251  ALA B N   1 
ATOM   6724  C  CA  . ALA B  1 251 ? 31.141  24.816  45.902  1.00 7.92  ? 251  ALA B CA  1 
ATOM   6725  C  C   . ALA B  1 251 ? 30.230  25.956  45.525  1.00 7.32  ? 251  ALA B C   1 
ATOM   6726  O  O   . ALA B  1 251 ? 29.568  25.939  44.483  1.00 6.67  ? 251  ALA B O   1 
ATOM   6727  C  CB  . ALA B  1 251 ? 32.596  25.220  45.762  1.00 7.54  ? 251  ALA B CB  1 
ATOM   6728  N  N   . GLY B  1 252 ? 30.192  26.948  46.400  1.00 6.35  ? 252  GLY B N   1 
ATOM   6729  C  CA  . GLY B  1 252 ? 29.349  28.121  46.223  1.00 5.71  ? 252  GLY B CA  1 
ATOM   6730  C  C   . GLY B  1 252 ? 29.282  28.543  44.754  1.00 4.12  ? 252  GLY B C   1 
ATOM   6731  O  O   . GLY B  1 252 ? 28.292  29.091  44.298  1.00 5.64  ? 252  GLY B O   1 
ATOM   6732  N  N   . ASP B  1 253 ? 30.344  28.284  44.005  1.00 3.32  ? 253  ASP B N   1 
ATOM   6733  C  CA  . ASP B  1 253 ? 30.393  28.653  42.597  1.00 2.91  ? 253  ASP B CA  1 
ATOM   6734  C  C   . ASP B  1 253 ? 30.404  27.373  41.764  1.00 2.99  ? 253  ASP B C   1 
ATOM   6735  O  O   . ASP B  1 253 ? 30.881  26.332  42.225  1.00 2.93  ? 253  ASP B O   1 
ATOM   6736  C  CB  . ASP B  1 253 ? 31.649  29.472  42.311  1.00 3.08  ? 253  ASP B CB  1 
ATOM   6737  C  CG  . ASP B  1 253 ? 31.758  29.882  40.856  1.00 2.99  ? 253  ASP B CG  1 
ATOM   6738  O  OD1 . ASP B  1 253 ? 31.187  30.929  40.480  1.00 2.00  ? 253  ASP B OD1 1 
ATOM   6739  O  OD2 . ASP B  1 253 ? 32.412  29.142  40.088  1.00 3.53  ? 253  ASP B OD2 1 
ATOM   6740  N  N   . SER B  1 254 ? 29.893  27.446  40.538  1.00 2.22  ? 254  SER B N   1 
ATOM   6741  C  CA  . SER B  1 254 ? 29.836  26.263  39.688  1.00 3.20  ? 254  SER B CA  1 
ATOM   6742  C  C   . SER B  1 254 ? 31.019  26.040  38.746  1.00 2.68  ? 254  SER B C   1 
ATOM   6743  O  O   . SER B  1 254 ? 31.012  25.091  37.969  1.00 3.92  ? 254  SER B O   1 
ATOM   6744  C  CB  . SER B  1 254 ? 28.531  26.249  38.874  1.00 2.61  ? 254  SER B CB  1 
ATOM   6745  O  OG  . SER B  1 254 ? 28.512  27.253  37.870  1.00 2.00  ? 254  SER B OG  1 
ATOM   6746  N  N   . ARG B  1 255 ? 32.034  26.886  38.789  1.00 2.00  ? 255  ARG B N   1 
ATOM   6747  C  CA  . ARG B  1 255 ? 33.157  26.642  37.900  1.00 2.00  ? 255  ARG B CA  1 
ATOM   6748  C  C   . ARG B  1 255 ? 34.318  26.054  38.662  1.00 3.30  ? 255  ARG B C   1 
ATOM   6749  O  O   . ARG B  1 255 ? 35.387  25.813  38.104  1.00 2.00  ? 255  ARG B O   1 
ATOM   6750  C  CB  . ARG B  1 255 ? 33.653  27.924  37.233  1.00 2.00  ? 255  ARG B CB  1 
ATOM   6751  C  CG  . ARG B  1 255 ? 32.614  28.564  36.351  1.00 2.11  ? 255  ARG B CG  1 
ATOM   6752  C  CD  . ARG B  1 255 ? 31.890  29.641  37.129  1.00 3.12  ? 255  ARG B CD  1 
ATOM   6753  N  NE  . ARG B  1 255 ? 32.119  30.935  36.531  1.00 2.36  ? 255  ARG B NE  1 
ATOM   6754  C  CZ  . ARG B  1 255 ? 32.251  32.069  37.207  1.00 2.84  ? 255  ARG B CZ  1 
ATOM   6755  N  NH1 . ARG B  1 255 ? 32.218  32.071  38.535  1.00 2.00  ? 255  ARG B NH1 1 
ATOM   6756  N  NH2 . ARG B  1 255 ? 32.425  33.205  36.549  1.00 4.59  ? 255  ARG B NH2 1 
ATOM   6757  N  N   . ALA B  1 256 ? 34.097  25.847  39.976  1.00 4.78  ? 256  ALA B N   1 
ATOM   6758  C  CA  . ALA B  1 256 ? 35.136  25.327  40.845  1.00 2.00  ? 256  ALA B CA  1 
ATOM   6759  C  C   . ALA B  1 256 ? 36.018  24.228  40.232  1.00 2.00  ? 256  ALA B C   1 
ATOM   6760  O  O   . ALA B  1 256 ? 37.180  24.127  40.605  1.00 3.74  ? 256  ALA B O   1 
ATOM   6761  C  CB  . ALA B  1 256 ? 34.506  24.796  42.124  1.00 2.00  ? 256  ALA B CB  1 
ATOM   6762  N  N   . SER B  1 257 ? 35.522  23.395  39.312  1.00 2.17  ? 257  SER B N   1 
ATOM   6763  C  CA  . SER B  1 257 ? 36.361  22.255  38.856  1.00 2.00  ? 257  SER B CA  1 
ATOM   6764  C  C   . SER B  1 257 ? 37.078  22.476  37.533  1.00 2.65  ? 257  SER B C   1 
ATOM   6765  O  O   . SER B  1 257 ? 37.940  21.677  37.172  1.00 2.56  ? 257  SER B O   1 
ATOM   6766  C  CB  . SER B  1 257 ? 35.497  20.990  38.731  1.00 2.00  ? 257  SER B CB  1 
ATOM   6767  O  OG  . SER B  1 257 ? 35.313  20.356  39.980  1.00 2.00  ? 257  SER B OG  1 
ATOM   6768  N  N   . GLU B  1 258 ? 36.737  23.560  36.804  1.00 3.89  ? 258  GLU B N   1 
ATOM   6769  C  CA  . GLU B  1 258 ? 37.384  23.732  35.497  1.00 2.00  ? 258  GLU B CA  1 
ATOM   6770  C  C   . GLU B  1 258 ? 38.784  23.135  35.531  1.00 2.00  ? 258  GLU B C   1 
ATOM   6771  O  O   . GLU B  1 258 ? 39.077  22.256  34.720  1.00 2.70  ? 258  GLU B O   1 
ATOM   6772  C  CB  . GLU B  1 258 ? 37.483  25.207  35.017  1.00 2.57  ? 258  GLU B CB  1 
ATOM   6773  C  CG  . GLU B  1 258 ? 37.875  25.354  33.537  1.00 2.66  ? 258  GLU B CG  1 
ATOM   6774  C  CD  . GLU B  1 258 ? 39.130  26.217  33.279  1.00 2.55  ? 258  GLU B CD  1 
ATOM   6775  O  OE1 . GLU B  1 258 ? 39.704  26.715  34.260  1.00 2.00  ? 258  GLU B OE1 1 
ATOM   6776  O  OE2 . GLU B  1 258 ? 39.510  26.387  32.094  1.00 4.75  ? 258  GLU B OE2 1 
ATOM   6777  N  N   . GLN B  1 259 ? 39.668  23.582  36.458  1.00 2.00  ? 259  GLN B N   1 
ATOM   6778  C  CA  . GLN B  1 259 ? 41.035  23.047  36.444  1.00 2.00  ? 259  GLN B CA  1 
ATOM   6779  C  C   . GLN B  1 259 ? 41.530  22.745  37.862  1.00 3.42  ? 259  GLN B C   1 
ATOM   6780  O  O   . GLN B  1 259 ? 41.331  23.536  38.802  1.00 3.12  ? 259  GLN B O   1 
ATOM   6781  C  CB  . GLN B  1 259 ? 41.964  23.994  35.703  1.00 2.00  ? 259  GLN B CB  1 
ATOM   6782  C  CG  . GLN B  1 259 ? 41.904  25.410  36.187  1.00 2.00  ? 259  GLN B CG  1 
ATOM   6783  C  CD  . GLN B  1 259 ? 43.032  25.688  37.144  1.00 2.00  ? 259  GLN B CD  1 
ATOM   6784  O  OE1 . GLN B  1 259 ? 43.813  24.787  37.464  1.00 2.00  ? 259  GLN B OE1 1 
ATOM   6785  N  NE2 . GLN B  1 259 ? 43.308  26.856  37.713  1.00 2.00  ? 259  GLN B NE2 1 
ATOM   6786  N  N   . ILE B  1 260 ? 42.176  21.589  37.987  1.00 3.96  ? 260  ILE B N   1 
ATOM   6787  C  CA  . ILE B  1 260 ? 42.695  21.050  39.237  1.00 2.11  ? 260  ILE B CA  1 
ATOM   6788  C  C   . ILE B  1 260 ? 43.319  22.035  40.212  1.00 2.00  ? 260  ILE B C   1 
ATOM   6789  O  O   . ILE B  1 260 ? 43.272  21.822  41.422  1.00 2.00  ? 260  ILE B O   1 
ATOM   6790  C  CB  . ILE B  1 260 ? 43.693  19.911  38.934  1.00 2.00  ? 260  ILE B CB  1 
ATOM   6791  C  CG1 . ILE B  1 260 ? 44.038  19.159  40.212  1.00 2.00  ? 260  ILE B CG1 1 
ATOM   6792  C  CG2 . ILE B  1 260 ? 44.944  20.467  38.288  1.00 2.00  ? 260  ILE B CG2 1 
ATOM   6793  C  CD1 . ILE B  1 260 ? 44.792  17.875  39.960  1.00 2.00  ? 260  ILE B CD1 1 
ATOM   6794  N  N   . LEU B  1 261 ? 43.904  23.111  39.704  1.00 2.00  ? 261  LEU B N   1 
ATOM   6795  C  CA  . LEU B  1 261 ? 44.509  24.088  40.594  1.00 2.00  ? 261  LEU B CA  1 
ATOM   6796  C  C   . LEU B  1 261 ? 43.464  25.034  41.160  1.00 2.22  ? 261  LEU B C   1 
ATOM   6797  O  O   . LEU B  1 261 ? 43.648  25.609  42.232  1.00 2.00  ? 261  LEU B O   1 
ATOM   6798  C  CB  . LEU B  1 261 ? 45.591  24.873  39.867  1.00 2.00  ? 261  LEU B CB  1 
ATOM   6799  C  CG  . LEU B  1 261 ? 47.035  24.583  40.287  1.00 2.25  ? 261  LEU B CG  1 
ATOM   6800  C  CD1 . LEU B  1 261 ? 47.118  23.403  41.250  1.00 2.00  ? 261  LEU B CD1 1 
ATOM   6801  C  CD2 . LEU B  1 261 ? 47.847  24.322  39.030  1.00 2.00  ? 261  LEU B CD2 1 
ATOM   6802  N  N   . LEU B  1 262 ? 42.361  25.196  40.441  1.00 2.45  ? 262  LEU B N   1 
ATOM   6803  C  CA  . LEU B  1 262 ? 41.292  26.056  40.914  1.00 2.00  ? 262  LEU B CA  1 
ATOM   6804  C  C   . LEU B  1 262 ? 40.654  25.324  42.086  1.00 2.00  ? 262  LEU B C   1 
ATOM   6805  O  O   . LEU B  1 262 ? 40.495  25.884  43.167  1.00 2.00  ? 262  LEU B O   1 
ATOM   6806  C  CB  . LEU B  1 262 ? 40.265  26.283  39.810  1.00 2.00  ? 262  LEU B CB  1 
ATOM   6807  C  CG  . LEU B  1 262 ? 39.163  27.265  40.186  1.00 2.00  ? 262  LEU B CG  1 
ATOM   6808  C  CD1 . LEU B  1 262 ? 39.785  28.581  40.611  1.00 3.52  ? 262  LEU B CD1 1 
ATOM   6809  C  CD2 . LEU B  1 262 ? 38.235  27.467  39.011  1.00 2.00  ? 262  LEU B CD2 1 
ATOM   6810  N  N   . ALA B  1 263 ? 40.315  24.058  41.855  1.00 2.41  ? 263  ALA B N   1 
ATOM   6811  C  CA  . ALA B  1 263 ? 39.706  23.200  42.868  1.00 2.00  ? 263  ALA B CA  1 
ATOM   6812  C  C   . ALA B  1 263 ? 40.548  23.209  44.135  1.00 4.41  ? 263  ALA B C   1 
ATOM   6813  O  O   . ALA B  1 263 ? 40.027  23.176  45.252  1.00 4.98  ? 263  ALA B O   1 
ATOM   6814  C  CB  . ALA B  1 263 ? 39.596  21.780  42.344  1.00 2.00  ? 263  ALA B CB  1 
ATOM   6815  N  N   . THR B  1 264 ? 41.860  23.255  43.958  1.00 3.38  ? 264  THR B N   1 
ATOM   6816  C  CA  . THR B  1 264 ? 42.745  23.248  45.097  1.00 2.00  ? 264  THR B CA  1 
ATOM   6817  C  C   . THR B  1 264 ? 42.520  24.428  46.029  1.00 2.00  ? 264  THR B C   1 
ATOM   6818  O  O   . THR B  1 264 ? 42.326  24.228  47.223  1.00 2.71  ? 264  THR B O   1 
ATOM   6819  C  CB  . THR B  1 264 ? 44.203  23.195  44.644  1.00 2.00  ? 264  THR B CB  1 
ATOM   6820  O  OG1 . THR B  1 264 ? 44.405  21.997  43.885  1.00 2.00  ? 264  THR B OG1 1 
ATOM   6821  C  CG2 . THR B  1 264 ? 45.141  23.193  45.841  1.00 2.00  ? 264  THR B CG2 1 
ATOM   6822  N  N   . VAL B  1 265 ? 42.511  25.651  45.514  1.00 2.00  ? 265  VAL B N   1 
ATOM   6823  C  CA  . VAL B  1 265 ? 42.322  26.780  46.420  1.00 2.00  ? 265  VAL B CA  1 
ATOM   6824  C  C   . VAL B  1 265 ? 40.919  26.831  46.991  1.00 2.00  ? 265  VAL B C   1 
ATOM   6825  O  O   . VAL B  1 265 ? 40.683  27.445  48.031  1.00 2.00  ? 265  VAL B O   1 
ATOM   6826  C  CB  . VAL B  1 265 ? 42.605  28.120  45.754  1.00 2.00  ? 265  VAL B CB  1 
ATOM   6827  C  CG1 . VAL B  1 265 ? 43.195  29.072  46.783  1.00 2.00  ? 265  VAL B CG1 1 
ATOM   6828  C  CG2 . VAL B  1 265 ? 43.538  27.936  44.589  1.00 2.12  ? 265  VAL B CG2 1 
ATOM   6829  N  N   . HIS B  1 266 ? 39.988  26.190  46.298  1.00 2.00  ? 266  HIS B N   1 
ATOM   6830  C  CA  . HIS B  1 266 ? 38.601  26.143  46.744  1.00 2.00  ? 266  HIS B CA  1 
ATOM   6831  C  C   . HIS B  1 266 ? 38.581  25.308  48.012  1.00 3.06  ? 266  HIS B C   1 
ATOM   6832  O  O   . HIS B  1 266 ? 37.691  25.443  48.861  1.00 2.22  ? 266  HIS B O   1 
ATOM   6833  C  CB  . HIS B  1 266 ? 37.731  25.475  45.682  1.00 2.35  ? 266  HIS B CB  1 
ATOM   6834  C  CG  . HIS B  1 266 ? 36.861  26.423  44.918  1.00 2.00  ? 266  HIS B CG  1 
ATOM   6835  N  ND1 . HIS B  1 266 ? 35.797  27.079  45.493  1.00 2.00  ? 266  HIS B ND1 1 
ATOM   6836  C  CD2 . HIS B  1 266 ? 36.879  26.800  43.618  1.00 2.75  ? 266  HIS B CD2 1 
ATOM   6837  C  CE1 . HIS B  1 266 ? 35.191  27.816  44.578  1.00 3.11  ? 266  HIS B CE1 1 
ATOM   6838  N  NE2 . HIS B  1 266 ? 35.828  27.664  43.431  1.00 2.41  ? 266  HIS B NE2 1 
ATOM   6839  N  N   . THR B  1 267 ? 39.576  24.434  48.117  1.00 3.26  ? 267  THR B N   1 
ATOM   6840  C  CA  . THR B  1 267 ? 39.723  23.559  49.263  1.00 2.18  ? 267  THR B CA  1 
ATOM   6841  C  C   . THR B  1 267 ? 40.331  24.315  50.446  1.00 2.29  ? 267  THR B C   1 
ATOM   6842  O  O   . THR B  1 267 ? 39.927  24.105  51.589  1.00 3.33  ? 267  THR B O   1 
ATOM   6843  C  CB  . THR B  1 267 ? 40.565  22.337  48.876  1.00 2.61  ? 267  THR B CB  1 
ATOM   6844  O  OG1 . THR B  1 267 ? 39.768  21.484  48.045  1.00 2.00  ? 267  THR B OG1 1 
ATOM   6845  C  CG2 . THR B  1 267 ? 41.026  21.566  50.103  1.00 3.14  ? 267  THR B CG2 1 
ATOM   6846  N  N   . LEU B  1 268 ? 41.284  25.204  50.183  1.00 2.00  ? 268  LEU B N   1 
ATOM   6847  C  CA  . LEU B  1 268 ? 41.872  25.991  51.264  1.00 2.05  ? 268  LEU B CA  1 
ATOM   6848  C  C   . LEU B  1 268 ? 40.807  26.916  51.879  1.00 3.27  ? 268  LEU B C   1 
ATOM   6849  O  O   . LEU B  1 268 ? 40.671  27.001  53.104  1.00 2.00  ? 268  LEU B O   1 
ATOM   6850  C  CB  . LEU B  1 268 ? 43.050  26.811  50.741  1.00 2.00  ? 268  LEU B CB  1 
ATOM   6851  C  CG  . LEU B  1 268 ? 44.412  26.111  50.756  1.00 2.11  ? 268  LEU B CG  1 
ATOM   6852  C  CD1 . LEU B  1 268 ? 44.250  24.634  50.439  1.00 2.92  ? 268  LEU B CD1 1 
ATOM   6853  C  CD2 . LEU B  1 268 ? 45.339  26.787  49.750  1.00 2.22  ? 268  LEU B CD2 1 
ATOM   6854  N  N   . LEU B  1 269 ? 40.041  27.594  51.030  1.00 3.23  ? 269  LEU B N   1 
ATOM   6855  C  CA  . LEU B  1 269 ? 38.999  28.478  51.522  1.00 2.00  ? 269  LEU B CA  1 
ATOM   6856  C  C   . LEU B  1 269 ? 37.950  27.696  52.297  1.00 3.91  ? 269  LEU B C   1 
ATOM   6857  O  O   . LEU B  1 269 ? 37.510  28.130  53.360  1.00 5.39  ? 269  LEU B O   1 
ATOM   6858  C  CB  . LEU B  1 269 ? 38.361  29.237  50.363  1.00 2.00  ? 269  LEU B CB  1 
ATOM   6859  C  CG  . LEU B  1 269 ? 39.414  30.052  49.613  1.00 2.07  ? 269  LEU B CG  1 
ATOM   6860  C  CD1 . LEU B  1 269 ? 38.727  31.067  48.712  1.00 2.00  ? 269  LEU B CD1 1 
ATOM   6861  C  CD2 . LEU B  1 269 ? 40.338  30.770  50.608  1.00 2.00  ? 269  LEU B CD2 1 
ATOM   6862  N  N   . LEU B  1 270 ? 37.554  26.539  51.775  1.00 3.67  ? 270  LEU B N   1 
ATOM   6863  C  CA  . LEU B  1 270 ? 36.574  25.712  52.466  1.00 2.00  ? 270  LEU B CA  1 
ATOM   6864  C  C   . LEU B  1 270 ? 37.171  25.312  53.792  1.00 2.00  ? 270  LEU B C   1 
ATOM   6865  O  O   . LEU B  1 270 ? 36.516  25.373  54.822  1.00 2.00  ? 270  LEU B O   1 
ATOM   6866  C  CB  . LEU B  1 270 ? 36.248  24.454  51.670  1.00 2.00  ? 270  LEU B CB  1 
ATOM   6867  C  CG  . LEU B  1 270 ? 35.306  23.502  52.399  1.00 2.00  ? 270  LEU B CG  1 
ATOM   6868  C  CD1 . LEU B  1 270 ? 34.130  24.288  52.906  1.00 2.00  ? 270  LEU B CD1 1 
ATOM   6869  C  CD2 . LEU B  1 270 ? 34.845  22.397  51.478  1.00 2.00  ? 270  LEU B CD2 1 
ATOM   6870  N  N   . ARG B  1 271 ? 38.433  24.913  53.765  1.00 2.00  ? 271  ARG B N   1 
ATOM   6871  C  CA  . ARG B  1 271 ? 39.105  24.517  54.986  1.00 2.00  ? 271  ARG B CA  1 
ATOM   6872  C  C   . ARG B  1 271 ? 39.219  25.647  56.015  1.00 2.00  ? 271  ARG B C   1 
ATOM   6873  O  O   . ARG B  1 271 ? 38.981  25.421  57.198  1.00 2.03  ? 271  ARG B O   1 
ATOM   6874  C  CB  . ARG B  1 271 ? 40.497  23.955  54.665  1.00 2.00  ? 271  ARG B CB  1 
ATOM   6875  C  CG  . ARG B  1 271 ? 40.452  22.602  53.978  1.00 2.00  ? 271  ARG B CG  1 
ATOM   6876  C  CD  . ARG B  1 271 ? 41.821  21.988  53.777  1.00 2.00  ? 271  ARG B CD  1 
ATOM   6877  N  NE  . ARG B  1 271 ? 41.698  20.740  53.033  1.00 2.00  ? 271  ARG B NE  1 
ATOM   6878  C  CZ  . ARG B  1 271 ? 42.715  19.961  52.677  1.00 2.00  ? 271  ARG B CZ  1 
ATOM   6879  N  NH1 . ARG B  1 271 ? 43.960  20.285  52.994  1.00 2.00  ? 271  ARG B NH1 1 
ATOM   6880  N  NH2 . ARG B  1 271 ? 42.481  18.852  51.994  1.00 2.05  ? 271  ARG B NH2 1 
ATOM   6881  N  N   . GLU B  1 272 ? 39.568  26.859  55.581  1.00 2.14  ? 272  GLU B N   1 
ATOM   6882  C  CA  . GLU B  1 272 ? 39.719  27.976  56.524  1.00 2.10  ? 272  GLU B CA  1 
ATOM   6883  C  C   . GLU B  1 272 ? 38.427  28.315  57.249  1.00 2.00  ? 272  GLU B C   1 
ATOM   6884  O  O   . GLU B  1 272 ? 38.446  28.865  58.355  1.00 2.00  ? 272  GLU B O   1 
ATOM   6885  C  CB  . GLU B  1 272 ? 40.249  29.230  55.817  1.00 2.80  ? 272  GLU B CB  1 
ATOM   6886  C  CG  . GLU B  1 272 ? 40.551  30.425  56.747  1.00 4.61  ? 272  GLU B CG  1 
ATOM   6887  C  CD  . GLU B  1 272 ? 41.440  30.071  57.942  1.00 5.61  ? 272  GLU B CD  1 
ATOM   6888  O  OE1 . GLU B  1 272 ? 42.004  28.957  57.966  1.00 8.29  ? 272  GLU B OE1 1 
ATOM   6889  O  OE2 . GLU B  1 272 ? 41.584  30.914  58.859  1.00 6.76  ? 272  GLU B OE2 1 
ATOM   6890  N  N   . HIS B  1 273 ? 37.301  27.998  56.622  1.00 2.02  ? 273  HIS B N   1 
ATOM   6891  C  CA  . HIS B  1 273 ? 36.023  28.260  57.250  1.00 2.09  ? 273  HIS B CA  1 
ATOM   6892  C  C   . HIS B  1 273 ? 35.985  27.451  58.531  1.00 3.16  ? 273  HIS B C   1 
ATOM   6893  O  O   . HIS B  1 273 ? 35.830  27.992  59.624  1.00 3.41  ? 273  HIS B O   1 
ATOM   6894  C  CB  . HIS B  1 273 ? 34.882  27.818  56.362  1.00 2.00  ? 273  HIS B CB  1 
ATOM   6895  C  CG  . HIS B  1 273 ? 33.543  28.030  56.984  1.00 3.46  ? 273  HIS B CG  1 
ATOM   6896  N  ND1 . HIS B  1 273 ? 32.814  29.184  56.799  1.00 3.66  ? 273  HIS B ND1 1 
ATOM   6897  C  CD2 . HIS B  1 273 ? 32.828  27.264  57.842  1.00 4.28  ? 273  HIS B CD2 1 
ATOM   6898  C  CE1 . HIS B  1 273 ? 31.706  29.118  57.516  1.00 5.03  ? 273  HIS B CE1 1 
ATOM   6899  N  NE2 . HIS B  1 273 ? 31.690  27.964  58.159  1.00 3.92  ? 273  HIS B NE2 1 
ATOM   6900  N  N   . ASN B  1 274 ? 36.146  26.143  58.403  1.00 2.00  ? 274  ASN B N   1 
ATOM   6901  C  CA  . ASN B  1 274 ? 36.126  25.315  59.585  1.00 2.00  ? 274  ASN B CA  1 
ATOM   6902  C  C   . ASN B  1 274 ? 37.158  25.663  60.664  1.00 2.00  ? 274  ASN B C   1 
ATOM   6903  O  O   . ASN B  1 274 ? 36.755  25.811  61.800  1.00 3.58  ? 274  ASN B O   1 
ATOM   6904  C  CB  . ASN B  1 274 ? 36.171  23.850  59.181  1.00 2.11  ? 274  ASN B CB  1 
ATOM   6905  C  CG  . ASN B  1 274 ? 34.977  23.460  58.317  1.00 2.00  ? 274  ASN B CG  1 
ATOM   6906  O  OD1 . ASN B  1 274 ? 33.865  23.936  58.525  1.00 2.00  ? 274  ASN B OD1 1 
ATOM   6907  N  ND2 . ASN B  1 274 ? 35.204  22.589  57.356  1.00 2.00  ? 274  ASN B ND2 1 
ATOM   6908  N  N   . ARG B  1 275 ? 38.458  25.819  60.375  1.00 2.00  ? 275  ARG B N   1 
ATOM   6909  C  CA  . ARG B  1 275 ? 39.375  26.181  61.481  1.00 2.41  ? 275  ARG B CA  1 
ATOM   6910  C  C   . ARG B  1 275 ? 38.749  27.359  62.254  1.00 2.00  ? 275  ARG B C   1 
ATOM   6911  O  O   . ARG B  1 275 ? 38.776  27.398  63.482  1.00 2.00  ? 275  ARG B O   1 
ATOM   6912  C  CB  . ARG B  1 275 ? 40.807  26.632  61.019  1.00 2.89  ? 275  ARG B CB  1 
ATOM   6913  C  CG  . ARG B  1 275 ? 41.219  27.971  61.741  1.00 5.49  ? 275  ARG B CG  1 
ATOM   6914  C  CD  . ARG B  1 275 ? 42.662  28.568  61.689  1.00 4.92  ? 275  ARG B CD  1 
ATOM   6915  N  NE  . ARG B  1 275 ? 42.629  29.741  62.584  1.00 12.11 ? 275  ARG B NE  1 
ATOM   6916  C  CZ  . ARG B  1 275 ? 43.661  30.488  63.005  1.00 13.66 ? 275  ARG B CZ  1 
ATOM   6917  N  NH1 . ARG B  1 275 ? 44.924  30.246  62.630  1.00 14.04 ? 275  ARG B NH1 1 
ATOM   6918  N  NH2 . ARG B  1 275 ? 43.412  31.484  63.855  1.00 14.50 ? 275  ARG B NH2 1 
ATOM   6919  N  N   . LEU B  1 276 ? 38.184  28.312  61.516  1.00 2.00  ? 276  LEU B N   1 
ATOM   6920  C  CA  . LEU B  1 276 ? 37.612  29.514  62.114  1.00 2.10  ? 276  LEU B CA  1 
ATOM   6921  C  C   . LEU B  1 276 ? 36.366  29.329  62.953  1.00 2.00  ? 276  LEU B C   1 
ATOM   6922  O  O   . LEU B  1 276 ? 36.230  29.955  64.002  1.00 2.00  ? 276  LEU B O   1 
ATOM   6923  C  CB  . LEU B  1 276 ? 37.358  30.567  61.026  1.00 2.29  ? 276  LEU B CB  1 
ATOM   6924  C  CG  . LEU B  1 276 ? 38.366  31.723  60.972  1.00 2.16  ? 276  LEU B CG  1 
ATOM   6925  C  CD1 . LEU B  1 276 ? 39.802  31.212  61.006  1.00 2.00  ? 276  LEU B CD1 1 
ATOM   6926  C  CD2 . LEU B  1 276 ? 38.109  32.520  59.716  1.00 2.00  ? 276  LEU B CD2 1 
ATOM   6927  N  N   . ALA B  1 277 ? 35.458  28.484  62.484  1.00 2.29  ? 277  ALA B N   1 
ATOM   6928  C  CA  . ALA B  1 277 ? 34.223  28.207  63.199  1.00 2.93  ? 277  ALA B CA  1 
ATOM   6929  C  C   . ALA B  1 277 ? 34.555  27.448  64.471  1.00 5.29  ? 277  ALA B C   1 
ATOM   6930  O  O   . ALA B  1 277 ? 34.178  27.861  65.563  1.00 7.31  ? 277  ALA B O   1 
ATOM   6931  C  CB  . ALA B  1 277 ? 33.319  27.388  62.346  1.00 2.38  ? 277  ALA B CB  1 
ATOM   6932  N  N   . ARG B  1 278 ? 35.265  26.335  64.324  1.00 8.29  ? 278  ARG B N   1 
ATOM   6933  C  CA  . ARG B  1 278 ? 35.666  25.519  65.469  1.00 10.53 ? 278  ARG B CA  1 
ATOM   6934  C  C   . ARG B  1 278 ? 36.328  26.405  66.510  1.00 10.57 ? 278  ARG B C   1 
ATOM   6935  O  O   . ARG B  1 278 ? 35.949  26.408  67.684  1.00 9.97  ? 278  ARG B O   1 
ATOM   6936  C  CB  . ARG B  1 278 ? 36.644  24.432  65.026  1.00 13.47 ? 278  ARG B CB  1 
ATOM   6937  C  CG  . ARG B  1 278 ? 36.095  23.023  65.152  1.00 19.32 ? 278  ARG B CG  1 
ATOM   6938  C  CD  . ARG B  1 278 ? 36.963  22.061  64.372  1.00 23.82 ? 278  ARG B CD  1 
ATOM   6939  N  NE  . ARG B  1 278 ? 36.325  21.534  63.167  1.00 28.66 ? 278  ARG B NE  1 
ATOM   6940  C  CZ  . ARG B  1 278 ? 36.958  21.369  62.006  1.00 31.17 ? 278  ARG B CZ  1 
ATOM   6941  N  NH1 . ARG B  1 278 ? 38.238  21.702  61.892  1.00 32.30 ? 278  ARG B NH1 1 
ATOM   6942  N  NH2 . ARG B  1 278 ? 36.328  20.841  60.961  1.00 33.14 ? 278  ARG B NH2 1 
ATOM   6943  N  N   . GLU B  1 279 ? 37.321  27.157  66.059  1.00 11.85 ? 279  GLU B N   1 
ATOM   6944  C  CA  . GLU B  1 279 ? 38.043  28.073  66.916  1.00 12.49 ? 279  GLU B CA  1 
ATOM   6945  C  C   . GLU B  1 279 ? 37.047  28.952  67.656  1.00 12.25 ? 279  GLU B C   1 
ATOM   6946  O  O   . GLU B  1 279 ? 36.922  28.865  68.870  1.00 14.35 ? 279  GLU B O   1 
ATOM   6947  C  CB  . GLU B  1 279 ? 38.964  28.953  66.080  1.00 16.00 ? 279  GLU B CB  1 
ATOM   6948  C  CG  . GLU B  1 279 ? 40.071  29.569  66.881  1.00 19.57 ? 279  GLU B CG  1 
ATOM   6949  C  CD  . GLU B  1 279 ? 40.872  28.511  67.600  1.00 22.00 ? 279  GLU B CD  1 
ATOM   6950  O  OE1 . GLU B  1 279 ? 41.409  27.610  66.912  1.00 23.80 ? 279  GLU B OE1 1 
ATOM   6951  O  OE2 . GLU B  1 279 ? 40.955  28.576  68.847  1.00 23.02 ? 279  GLU B OE2 1 
ATOM   6952  N  N   . LEU B  1 280 ? 36.325  29.794  66.925  1.00 11.28 ? 280  LEU B N   1 
ATOM   6953  C  CA  . LEU B  1 280 ? 35.358  30.684  67.561  1.00 10.15 ? 280  LEU B CA  1 
ATOM   6954  C  C   . LEU B  1 280 ? 34.469  29.957  68.570  1.00 9.83  ? 280  LEU B C   1 
ATOM   6955  O  O   . LEU B  1 280 ? 34.268  30.443  69.684  1.00 9.43  ? 280  LEU B O   1 
ATOM   6956  C  CB  . LEU B  1 280 ? 34.504  31.394  66.505  1.00 6.58  ? 280  LEU B CB  1 
ATOM   6957  C  CG  . LEU B  1 280 ? 35.285  32.280  65.534  1.00 3.26  ? 280  LEU B CG  1 
ATOM   6958  C  CD1 . LEU B  1 280 ? 34.290  33.012  64.689  1.00 3.08  ? 280  LEU B CD1 1 
ATOM   6959  C  CD2 . LEU B  1 280 ? 36.181  33.265  66.260  1.00 2.00  ? 280  LEU B CD2 1 
ATOM   6960  N  N   . LYS B  1 281 ? 33.952  28.792  68.186  1.00 10.05 ? 281  LYS B N   1 
ATOM   6961  C  CA  . LYS B  1 281 ? 33.105  28.002  69.075  1.00 10.76 ? 281  LYS B CA  1 
ATOM   6962  C  C   . LYS B  1 281 ? 33.785  27.776  70.429  1.00 11.73 ? 281  LYS B C   1 
ATOM   6963  O  O   . LYS B  1 281 ? 33.175  27.968  71.479  1.00 11.53 ? 281  LYS B O   1 
ATOM   6964  C  CB  . LYS B  1 281 ? 32.781  26.648  68.433  1.00 9.00  ? 281  LYS B CB  1 
ATOM   6965  C  CG  . LYS B  1 281 ? 32.820  25.468  69.403  1.00 8.40  ? 281  LYS B CG  1 
ATOM   6966  C  CD  . LYS B  1 281 ? 31.710  25.517  70.440  1.00 6.22  ? 281  LYS B CD  1 
ATOM   6967  C  CE  . LYS B  1 281 ? 30.394  25.031  69.866  1.00 6.03  ? 281  LYS B CE  1 
ATOM   6968  N  NZ  . LYS B  1 281 ? 29.351  24.947  70.926  1.00 5.60  ? 281  LYS B NZ  1 
ATOM   6969  N  N   . ARG B  1 282 ? 35.048  27.368  70.399  1.00 12.08 ? 282  ARG B N   1 
ATOM   6970  C  CA  . ARG B  1 282 ? 35.784  27.101  71.627  1.00 13.58 ? 282  ARG B CA  1 
ATOM   6971  C  C   . ARG B  1 282 ? 35.959  28.343  72.485  1.00 12.09 ? 282  ARG B C   1 
ATOM   6972  O  O   . ARG B  1 282 ? 36.013  28.262  73.718  1.00 11.39 ? 282  ARG B O   1 
ATOM   6973  C  CB  . ARG B  1 282 ? 37.173  26.548  71.308  1.00 18.64 ? 282  ARG B CB  1 
ATOM   6974  C  CG  . ARG B  1 282 ? 38.212  27.623  70.995  1.00 24.92 ? 282  ARG B CG  1 
ATOM   6975  C  CD  . ARG B  1 282 ? 39.608  27.091  71.205  1.00 28.80 ? 282  ARG B CD  1 
ATOM   6976  N  NE  . ARG B  1 282 ? 39.784  25.812  70.530  1.00 34.18 ? 282  ARG B NE  1 
ATOM   6977  C  CZ  . ARG B  1 282 ? 40.781  24.976  70.790  1.00 37.09 ? 282  ARG B CZ  1 
ATOM   6978  N  NH1 . ARG B  1 282 ? 41.682  25.297  71.713  1.00 39.79 ? 282  ARG B NH1 1 
ATOM   6979  N  NH2 . ARG B  1 282 ? 40.875  23.826  70.132  1.00 38.31 ? 282  ARG B NH2 1 
ATOM   6980  N  N   . LEU B  1 283 ? 36.072  29.487  71.818  1.00 10.43 ? 283  LEU B N   1 
ATOM   6981  C  CA  . LEU B  1 283 ? 36.274  30.759  72.493  1.00 9.06  ? 283  LEU B CA  1 
ATOM   6982  C  C   . LEU B  1 283 ? 34.974  31.355  72.972  1.00 8.59  ? 283  LEU B C   1 
ATOM   6983  O  O   . LEU B  1 283 ? 34.912  31.944  74.042  1.00 7.66  ? 283  LEU B O   1 
ATOM   6984  C  CB  . LEU B  1 283 ? 36.958  31.747  71.559  1.00 7.23  ? 283  LEU B CB  1 
ATOM   6985  C  CG  . LEU B  1 283 ? 38.340  32.184  72.032  1.00 6.75  ? 283  LEU B CG  1 
ATOM   6986  C  CD1 . LEU B  1 283 ? 38.848  33.272  71.114  1.00 7.30  ? 283  LEU B CD1 1 
ATOM   6987  C  CD2 . LEU B  1 283 ? 38.271  32.683  73.469  1.00 5.73  ? 283  LEU B CD2 1 
ATOM   6988  N  N   . ASN B  1 284 ? 33.942  31.216  72.154  1.00 10.08 ? 284  ASN B N   1 
ATOM   6989  C  CA  . ASN B  1 284 ? 32.614  31.726  72.477  1.00 12.57 ? 284  ASN B CA  1 
ATOM   6990  C  C   . ASN B  1 284 ? 31.705  30.488  72.525  1.00 12.30 ? 284  ASN B C   1 
ATOM   6991  O  O   . ASN B  1 284 ? 30.867  30.272  71.643  1.00 12.75 ? 284  ASN B O   1 
ATOM   6992  C  CB  . ASN B  1 284 ? 32.154  32.710  71.386  1.00 13.37 ? 284  ASN B CB  1 
ATOM   6993  C  CG  . ASN B  1 284 ? 33.050  33.953  71.286  1.00 14.93 ? 284  ASN B CG  1 
ATOM   6994  O  OD1 . ASN B  1 284 ? 34.270  33.882  71.467  1.00 14.70 ? 284  ASN B OD1 1 
ATOM   6995  N  ND2 . ASN B  1 284 ? 32.441  35.093  70.976  1.00 15.16 ? 284  ASN B ND2 1 
ATOM   6996  N  N   . PRO B  1 285 ? 31.864  29.661  73.571  1.00 10.31 ? 285  PRO B N   1 
ATOM   6997  C  CA  . PRO B  1 285 ? 31.102  28.429  73.783  1.00 10.18 ? 285  PRO B CA  1 
ATOM   6998  C  C   . PRO B  1 285 ? 29.597  28.587  73.666  1.00 10.88 ? 285  PRO B C   1 
ATOM   6999  O  O   . PRO B  1 285 ? 28.929  27.781  73.020  1.00 10.05 ? 285  PRO B O   1 
ATOM   7000  C  CB  . PRO B  1 285 ? 31.531  27.997  75.181  1.00 9.69  ? 285  PRO B CB  1 
ATOM   7001  C  CG  . PRO B  1 285 ? 32.907  28.572  75.311  1.00 9.81  ? 285  PRO B CG  1 
ATOM   7002  C  CD  . PRO B  1 285 ? 32.706  29.945  74.743  1.00 10.01 ? 285  PRO B CD  1 
ATOM   7003  N  N   . HIS B  1 286 ? 29.063  29.629  74.289  1.00 12.10 ? 286  HIS B N   1 
ATOM   7004  C  CA  . HIS B  1 286 ? 27.623  29.870  74.259  1.00 13.40 ? 286  HIS B CA  1 
ATOM   7005  C  C   . HIS B  1 286 ? 27.096  30.240  72.872  1.00 12.56 ? 286  HIS B C   1 
ATOM   7006  O  O   . HIS B  1 286 ? 25.882  30.206  72.641  1.00 12.94 ? 286  HIS B O   1 
ATOM   7007  C  CB  . HIS B  1 286 ? 27.264  30.986  75.231  1.00 17.12 ? 286  HIS B CB  1 
ATOM   7008  C  CG  . HIS B  1 286 ? 28.054  32.228  75.004  1.00 20.63 ? 286  HIS B CG  1 
ATOM   7009  N  ND1 . HIS B  1 286 ? 29.394  32.316  75.314  1.00 22.16 ? 286  HIS B ND1 1 
ATOM   7010  C  CD2 . HIS B  1 286 ? 27.725  33.395  74.403  1.00 22.29 ? 286  HIS B CD2 1 
ATOM   7011  C  CE1 . HIS B  1 286 ? 29.858  33.485  74.910  1.00 24.81 ? 286  HIS B CE1 1 
ATOM   7012  N  NE2 . HIS B  1 286 ? 28.866  34.159  74.353  1.00 24.97 ? 286  HIS B NE2 1 
ATOM   7013  N  N   . TRP B  1 287 ? 27.988  30.598  71.951  1.00 9.52  ? 287  TRP B N   1 
ATOM   7014  C  CA  . TRP B  1 287 ? 27.538  30.970  70.618  1.00 7.02  ? 287  TRP B CA  1 
ATOM   7015  C  C   . TRP B  1 287 ? 26.813  29.858  69.889  1.00 6.95  ? 287  TRP B C   1 
ATOM   7016  O  O   . TRP B  1 287 ? 27.188  28.694  69.959  1.00 7.77  ? 287  TRP B O   1 
ATOM   7017  C  CB  . TRP B  1 287 ? 28.701  31.486  69.784  1.00 6.51  ? 287  TRP B CB  1 
ATOM   7018  C  CG  . TRP B  1 287 ? 28.837  32.953  69.918  1.00 7.46  ? 287  TRP B CG  1 
ATOM   7019  C  CD1 . TRP B  1 287 ? 28.117  33.756  70.747  1.00 8.65  ? 287  TRP B CD1 1 
ATOM   7020  C  CD2 . TRP B  1 287 ? 29.718  33.814  69.188  1.00 7.43  ? 287  TRP B CD2 1 
ATOM   7021  N  NE1 . TRP B  1 287 ? 28.487  35.066  70.579  1.00 10.10 ? 287  TRP B NE1 1 
ATOM   7022  C  CE2 . TRP B  1 287 ? 29.469  35.131  69.627  1.00 7.93  ? 287  TRP B CE2 1 
ATOM   7023  C  CE3 . TRP B  1 287 ? 30.691  33.603  68.205  1.00 5.99  ? 287  TRP B CE3 1 
ATOM   7024  C  CZ2 . TRP B  1 287 ? 30.160  36.235  69.118  1.00 7.25  ? 287  TRP B CZ2 1 
ATOM   7025  C  CZ3 . TRP B  1 287 ? 31.376  34.698  67.700  1.00 5.39  ? 287  TRP B CZ3 1 
ATOM   7026  C  CH2 . TRP B  1 287 ? 31.105  35.998  68.158  1.00 6.09  ? 287  TRP B CH2 1 
ATOM   7027  N  N   . ASP B  1 288 ? 25.758  30.236  69.189  1.00 5.42  ? 288  ASP B N   1 
ATOM   7028  C  CA  . ASP B  1 288 ? 24.945  29.290  68.459  1.00 4.83  ? 288  ASP B CA  1 
ATOM   7029  C  C   . ASP B  1 288 ? 25.361  29.148  66.989  1.00 3.83  ? 288  ASP B C   1 
ATOM   7030  O  O   . ASP B  1 288 ? 25.879  30.085  66.379  1.00 2.00  ? 288  ASP B O   1 
ATOM   7031  C  CB  . ASP B  1 288 ? 23.489  29.728  68.589  1.00 9.57  ? 288  ASP B CB  1 
ATOM   7032  C  CG  . ASP B  1 288 ? 22.729  29.624  67.292  1.00 13.38 ? 288  ASP B CG  1 
ATOM   7033  O  OD1 . ASP B  1 288 ? 22.531  28.475  66.817  1.00 15.55 ? 288  ASP B OD1 1 
ATOM   7034  O  OD2 . ASP B  1 288 ? 22.333  30.693  66.757  1.00 12.08 ? 288  ASP B OD2 1 
ATOM   7035  N  N   . GLY B  1 289 ? 25.119  27.960  66.436  1.00 3.17  ? 289  GLY B N   1 
ATOM   7036  C  CA  . GLY B  1 289 ? 25.466  27.649  65.054  1.00 2.81  ? 289  GLY B CA  1 
ATOM   7037  C  C   . GLY B  1 289 ? 25.423  28.778  64.041  1.00 2.25  ? 289  GLY B C   1 
ATOM   7038  O  O   . GLY B  1 289 ? 26.452  29.162  63.486  1.00 2.00  ? 289  GLY B O   1 
ATOM   7039  N  N   . GLU B  1 290 ? 24.222  29.285  63.787  1.00 2.26  ? 290  GLU B N   1 
ATOM   7040  C  CA  . GLU B  1 290 ? 24.000  30.379  62.853  1.00 2.00  ? 290  GLU B CA  1 
ATOM   7041  C  C   . GLU B  1 290 ? 24.969  31.523  63.125  1.00 2.00  ? 290  GLU B C   1 
ATOM   7042  O  O   . GLU B  1 290 ? 25.521  32.117  62.201  1.00 2.00  ? 290  GLU B O   1 
ATOM   7043  C  CB  . GLU B  1 290 ? 22.580  30.891  63.014  1.00 2.00  ? 290  GLU B CB  1 
ATOM   7044  C  CG  . GLU B  1 290 ? 22.159  31.883  61.970  1.00 3.12  ? 290  GLU B CG  1 
ATOM   7045  C  CD  . GLU B  1 290 ? 22.037  31.241  60.616  1.00 5.32  ? 290  GLU B CD  1 
ATOM   7046  O  OE1 . GLU B  1 290 ? 21.637  30.055  60.568  1.00 6.59  ? 290  GLU B OE1 1 
ATOM   7047  O  OE2 . GLU B  1 290 ? 22.326  31.917  59.603  1.00 7.99  ? 290  GLU B OE2 1 
ATOM   7048  N  N   . LYS B  1 291 ? 25.158  31.837  64.402  1.00 2.34  ? 291  LYS B N   1 
ATOM   7049  C  CA  . LYS B  1 291 ? 26.061  32.909  64.806  1.00 2.88  ? 291  LYS B CA  1 
ATOM   7050  C  C   . LYS B  1 291 ? 27.474  32.560  64.354  1.00 4.85  ? 291  LYS B C   1 
ATOM   7051  O  O   . LYS B  1 291 ? 28.183  33.411  63.810  1.00 6.31  ? 291  LYS B O   1 
ATOM   7052  C  CB  . LYS B  1 291 ? 26.012  33.081  66.326  1.00 3.04  ? 291  LYS B CB  1 
ATOM   7053  C  CG  . LYS B  1 291 ? 27.047  34.018  66.922  1.00 2.00  ? 291  LYS B CG  1 
ATOM   7054  C  CD  . LYS B  1 291 ? 26.701  35.477  66.723  1.00 2.00  ? 291  LYS B CD  1 
ATOM   7055  C  CE  . LYS B  1 291 ? 26.799  36.209  68.061  1.00 2.98  ? 291  LYS B CE  1 
ATOM   7056  N  NZ  . LYS B  1 291 ? 27.366  37.586  67.937  1.00 2.21  ? 291  LYS B NZ  1 
ATOM   7057  N  N   . LEU B  1 292 ? 27.882  31.307  64.573  1.00 5.85  ? 292  LEU B N   1 
ATOM   7058  C  CA  . LEU B  1 292 ? 29.220  30.856  64.158  1.00 5.74  ? 292  LEU B CA  1 
ATOM   7059  C  C   . LEU B  1 292 ? 29.394  30.973  62.631  1.00 5.33  ? 292  LEU B C   1 
ATOM   7060  O  O   . LEU B  1 292 ? 30.330  31.618  62.152  1.00 3.29  ? 292  LEU B O   1 
ATOM   7061  C  CB  . LEU B  1 292 ? 29.477  29.395  64.593  1.00 4.19  ? 292  LEU B CB  1 
ATOM   7062  C  CG  . LEU B  1 292 ? 29.777  29.032  66.056  1.00 2.00  ? 292  LEU B CG  1 
ATOM   7063  C  CD1 . LEU B  1 292 ? 30.945  29.855  66.594  1.00 2.00  ? 292  LEU B CD1 1 
ATOM   7064  C  CD2 . LEU B  1 292 ? 28.541  29.263  66.885  1.00 3.06  ? 292  LEU B CD2 1 
ATOM   7065  N  N   . TYR B  1 293 ? 28.481  30.345  61.887  1.00 5.42  ? 293  TYR B N   1 
ATOM   7066  C  CA  . TYR B  1 293 ? 28.482  30.355  60.422  1.00 6.77  ? 293  TYR B CA  1 
ATOM   7067  C  C   . TYR B  1 293 ? 28.736  31.717  59.784  1.00 8.68  ? 293  TYR B C   1 
ATOM   7068  O  O   . TYR B  1 293 ? 29.460  31.814  58.788  1.00 8.70  ? 293  TYR B O   1 
ATOM   7069  C  CB  . TYR B  1 293 ? 27.140  29.832  59.892  1.00 7.91  ? 293  TYR B CB  1 
ATOM   7070  C  CG  . TYR B  1 293 ? 26.929  30.036  58.400  1.00 9.22  ? 293  TYR B CG  1 
ATOM   7071  C  CD1 . TYR B  1 293 ? 27.697  29.342  57.463  1.00 9.44  ? 293  TYR B CD1 1 
ATOM   7072  C  CD2 . TYR B  1 293 ? 25.958  30.926  57.927  1.00 10.89 ? 293  TYR B CD2 1 
ATOM   7073  C  CE1 . TYR B  1 293 ? 27.504  29.525  56.087  1.00 10.67 ? 293  TYR B CE1 1 
ATOM   7074  C  CE2 . TYR B  1 293 ? 25.755  31.118  56.550  1.00 11.97 ? 293  TYR B CE2 1 
ATOM   7075  C  CZ  . TYR B  1 293 ? 26.532  30.412  55.639  1.00 11.28 ? 293  TYR B CZ  1 
ATOM   7076  O  OH  . TYR B  1 293 ? 26.329  30.595  54.291  1.00 10.07 ? 293  TYR B OH  1 
ATOM   7077  N  N   . GLN B  1 294 ? 28.144  32.768  60.348  1.00 8.40  ? 294  GLN B N   1 
ATOM   7078  C  CA  . GLN B  1 294 ? 28.298  34.089  59.764  1.00 7.83  ? 294  GLN B CA  1 
ATOM   7079  C  C   . GLN B  1 294 ? 29.432  34.941  60.304  1.00 7.15  ? 294  GLN B C   1 
ATOM   7080  O  O   . GLN B  1 294 ? 29.948  35.793  59.582  1.00 8.45  ? 294  GLN B O   1 
ATOM   7081  C  CB  . GLN B  1 294 ? 26.955  34.815  59.821  1.00 7.18  ? 294  GLN B CB  1 
ATOM   7082  C  CG  . GLN B  1 294 ? 25.886  33.945  59.180  1.00 7.27  ? 294  GLN B CG  1 
ATOM   7083  C  CD  . GLN B  1 294 ? 24.770  34.725  58.552  1.00 8.41  ? 294  GLN B CD  1 
ATOM   7084  O  OE1 . GLN B  1 294 ? 23.910  35.273  59.249  1.00 10.54 ? 294  GLN B OE1 1 
ATOM   7085  N  NE2 . GLN B  1 294 ? 24.771  34.789  57.219  1.00 7.68  ? 294  GLN B NE2 1 
ATOM   7086  N  N   . GLU B  1 295 ? 29.835  34.721  61.552  1.00 5.80  ? 295  GLU B N   1 
ATOM   7087  C  CA  . GLU B  1 295 ? 30.955  35.481  62.100  1.00 4.68  ? 295  GLU B CA  1 
ATOM   7088  C  C   . GLU B  1 295 ? 32.197  34.968  61.362  1.00 4.94  ? 295  GLU B C   1 
ATOM   7089  O  O   . GLU B  1 295 ? 33.158  35.705  61.142  1.00 4.26  ? 295  GLU B O   1 
ATOM   7090  C  CB  . GLU B  1 295 ? 31.081  35.251  63.610  1.00 5.51  ? 295  GLU B CB  1 
ATOM   7091  C  CG  . GLU B  1 295 ? 30.314  36.252  64.481  1.00 6.21  ? 295  GLU B CG  1 
ATOM   7092  C  CD  . GLU B  1 295 ? 30.876  37.667  64.396  1.00 7.96  ? 295  GLU B CD  1 
ATOM   7093  O  OE1 . GLU B  1 295 ? 32.112  37.807  64.256  1.00 9.80  ? 295  GLU B OE1 1 
ATOM   7094  O  OE2 . GLU B  1 295 ? 30.091  38.639  64.488  1.00 6.75  ? 295  GLU B OE2 1 
ATOM   7095  N  N   . ALA B  1 296 ? 32.136  33.695  60.969  1.00 4.77  ? 296  ALA B N   1 
ATOM   7096  C  CA  . ALA B  1 296 ? 33.195  33.014  60.218  1.00 3.40  ? 296  ALA B CA  1 
ATOM   7097  C  C   . ALA B  1 296 ? 33.211  33.560  58.785  1.00 2.83  ? 296  ALA B C   1 
ATOM   7098  O  O   . ALA B  1 296 ? 34.249  34.010  58.278  1.00 2.77  ? 296  ALA B O   1 
ATOM   7099  C  CB  . ALA B  1 296 ? 32.921  31.508  60.195  1.00 2.22  ? 296  ALA B CB  1 
ATOM   7100  N  N   . ARG B  1 297 ? 32.044  33.499  58.144  1.00 2.26  ? 297  ARG B N   1 
ATOM   7101  C  CA  . ARG B  1 297 ? 31.848  33.997  56.783  1.00 2.96  ? 297  ARG B CA  1 
ATOM   7102  C  C   . ARG B  1 297 ? 32.323  35.453  56.670  1.00 3.49  ? 297  ARG B C   1 
ATOM   7103  O  O   . ARG B  1 297 ? 32.825  35.883  55.626  1.00 3.51  ? 297  ARG B O   1 
ATOM   7104  C  CB  . ARG B  1 297 ? 30.358  33.885  56.420  1.00 2.53  ? 297  ARG B CB  1 
ATOM   7105  C  CG  . ARG B  1 297 ? 29.907  34.641  55.174  1.00 2.37  ? 297  ARG B CG  1 
ATOM   7106  C  CD  . ARG B  1 297 ? 28.576  34.087  54.668  1.00 2.00  ? 297  ARG B CD  1 
ATOM   7107  N  NE  . ARG B  1 297 ? 27.986  34.904  53.609  1.00 2.42  ? 297  ARG B NE  1 
ATOM   7108  C  CZ  . ARG B  1 297 ? 27.203  35.960  53.825  1.00 3.26  ? 297  ARG B CZ  1 
ATOM   7109  N  NH1 . ARG B  1 297 ? 26.913  36.328  55.068  1.00 4.09  ? 297  ARG B NH1 1 
ATOM   7110  N  NH2 . ARG B  1 297 ? 26.700  36.643  52.803  1.00 2.06  ? 297  ARG B NH2 1 
ATOM   7111  N  N   . LYS B  1 298 ? 32.163  36.205  57.755  1.00 2.52  ? 298  LYS B N   1 
ATOM   7112  C  CA  . LYS B  1 298 ? 32.580  37.591  57.775  1.00 2.00  ? 298  LYS B CA  1 
ATOM   7113  C  C   . LYS B  1 298 ? 34.096  37.614  57.872  1.00 2.00  ? 298  LYS B C   1 
ATOM   7114  O  O   . LYS B  1 298 ? 34.744  38.309  57.103  1.00 2.54  ? 298  LYS B O   1 
ATOM   7115  C  CB  . LYS B  1 298 ? 31.934  38.337  58.960  1.00 3.71  ? 298  LYS B CB  1 
ATOM   7116  C  CG  . LYS B  1 298 ? 32.055  39.875  58.892  1.00 5.02  ? 298  LYS B CG  1 
ATOM   7117  C  CD  . LYS B  1 298 ? 30.855  40.622  59.518  1.00 4.53  ? 298  LYS B CD  1 
ATOM   7118  C  CE  . LYS B  1 298 ? 30.992  40.880  61.022  1.00 5.03  ? 298  LYS B CE  1 
ATOM   7119  N  NZ  . LYS B  1 298 ? 29.826  41.669  61.546  1.00 4.44  ? 298  LYS B NZ  1 
ATOM   7120  N  N   . ILE B  1 299 ? 34.673  36.844  58.791  1.00 2.00  ? 299  ILE B N   1 
ATOM   7121  C  CA  . ILE B  1 299 ? 36.133  36.829  58.929  1.00 2.15  ? 299  ILE B CA  1 
ATOM   7122  C  C   . ILE B  1 299 ? 36.788  36.559  57.580  1.00 3.85  ? 299  ILE B C   1 
ATOM   7123  O  O   . ILE B  1 299 ? 37.691  37.287  57.148  1.00 2.00  ? 299  ILE B O   1 
ATOM   7124  C  CB  . ILE B  1 299 ? 36.635  35.715  59.863  1.00 2.04  ? 299  ILE B CB  1 
ATOM   7125  C  CG1 . ILE B  1 299 ? 35.952  35.787  61.222  1.00 2.99  ? 299  ILE B CG1 1 
ATOM   7126  C  CG2 . ILE B  1 299 ? 38.131  35.876  60.069  1.00 3.00  ? 299  ILE B CG2 1 
ATOM   7127  C  CD1 . ILE B  1 299 ? 36.337  36.990  62.005  1.00 2.94  ? 299  ILE B CD1 1 
ATOM   7128  N  N   . LEU B  1 300 ? 36.310  35.493  56.937  1.00 3.60  ? 300  LEU B N   1 
ATOM   7129  C  CA  . LEU B  1 300 ? 36.803  35.029  55.644  1.00 2.00  ? 300  LEU B CA  1 
ATOM   7130  C  C   . LEU B  1 300 ? 36.731  36.055  54.524  1.00 2.00  ? 300  LEU B C   1 
ATOM   7131  O  O   . LEU B  1 300 ? 37.658  36.182  53.733  1.00 2.52  ? 300  LEU B O   1 
ATOM   7132  C  CB  . LEU B  1 300 ? 36.040  33.772  55.214  1.00 2.29  ? 300  LEU B CB  1 
ATOM   7133  C  CG  . LEU B  1 300 ? 36.607  33.096  53.961  1.00 2.37  ? 300  LEU B CG  1 
ATOM   7134  C  CD1 . LEU B  1 300 ? 38.015  32.628  54.263  1.00 2.00  ? 300  LEU B CD1 1 
ATOM   7135  C  CD2 . LEU B  1 300 ? 35.746  31.926  53.531  1.00 2.00  ? 300  LEU B CD2 1 
ATOM   7136  N  N   . GLY B  1 301 ? 35.622  36.775  54.441  1.00 2.00  ? 301  GLY B N   1 
ATOM   7137  C  CA  . GLY B  1 301 ? 35.489  37.765  53.388  1.00 2.72  ? 301  GLY B CA  1 
ATOM   7138  C  C   . GLY B  1 301 ? 36.481  38.896  53.550  1.00 2.00  ? 301  GLY B C   1 
ATOM   7139  O  O   . GLY B  1 301 ? 37.074  39.375  52.583  1.00 2.00  ? 301  GLY B O   1 
ATOM   7140  N  N   . ALA B  1 302 ? 36.647  39.331  54.792  1.00 2.00  ? 302  ALA B N   1 
ATOM   7141  C  CA  . ALA B  1 302 ? 37.578  40.400  55.099  1.00 2.00  ? 302  ALA B CA  1 
ATOM   7142  C  C   . ALA B  1 302 ? 38.894  39.946  54.500  1.00 2.00  ? 302  ALA B C   1 
ATOM   7143  O  O   . ALA B  1 302 ? 39.642  40.714  53.913  1.00 2.00  ? 302  ALA B O   1 
ATOM   7144  C  CB  . ALA B  1 302 ? 37.708  40.555  56.604  1.00 2.00  ? 302  ALA B CB  1 
ATOM   7145  N  N   . PHE B  1 303 ? 39.142  38.660  54.644  1.00 2.00  ? 303  PHE B N   1 
ATOM   7146  C  CA  . PHE B  1 303 ? 40.348  38.046  54.149  1.00 2.00  ? 303  PHE B CA  1 
ATOM   7147  C  C   . PHE B  1 303 ? 40.514  38.234  52.637  1.00 2.00  ? 303  PHE B C   1 
ATOM   7148  O  O   . PHE B  1 303 ? 41.515  38.779  52.187  1.00 2.02  ? 303  PHE B O   1 
ATOM   7149  C  CB  . PHE B  1 303 ? 40.314  36.567  54.557  1.00 2.84  ? 303  PHE B CB  1 
ATOM   7150  C  CG  . PHE B  1 303 ? 41.364  35.721  53.915  1.00 2.00  ? 303  PHE B CG  1 
ATOM   7151  C  CD1 . PHE B  1 303 ? 42.710  35.955  54.141  1.00 2.00  ? 303  PHE B CD1 1 
ATOM   7152  C  CD2 . PHE B  1 303 ? 40.997  34.669  53.090  1.00 2.00  ? 303  PHE B CD2 1 
ATOM   7153  C  CE1 . PHE B  1 303 ? 43.676  35.149  53.554  1.00 2.00  ? 303  PHE B CE1 1 
ATOM   7154  C  CE2 . PHE B  1 303 ? 41.949  33.861  52.500  1.00 2.00  ? 303  PHE B CE2 1 
ATOM   7155  C  CZ  . PHE B  1 303 ? 43.292  34.101  52.733  1.00 2.25  ? 303  PHE B CZ  1 
ATOM   7156  N  N   . ILE B  1 304 ? 39.527  37.820  51.853  1.00 2.00  ? 304  ILE B N   1 
ATOM   7157  C  CA  . ILE B  1 304 ? 39.629  37.944  50.400  1.00 2.01  ? 304  ILE B CA  1 
ATOM   7158  C  C   . ILE B  1 304 ? 39.766  39.391  49.896  1.00 2.60  ? 304  ILE B C   1 
ATOM   7159  O  O   . ILE B  1 304 ? 40.193  39.633  48.765  1.00 2.00  ? 304  ILE B O   1 
ATOM   7160  C  CB  . ILE B  1 304 ? 38.426  37.273  49.716  1.00 2.00  ? 304  ILE B CB  1 
ATOM   7161  C  CG1 . ILE B  1 304 ? 38.111  35.961  50.438  1.00 2.00  ? 304  ILE B CG1 1 
ATOM   7162  C  CG2 . ILE B  1 304 ? 38.729  37.039  48.251  1.00 2.00  ? 304  ILE B CG2 1 
ATOM   7163  C  CD1 . ILE B  1 304 ? 37.583  34.865  49.564  1.00 2.00  ? 304  ILE B CD1 1 
ATOM   7164  N  N   . GLN B  1 305 ? 39.412  40.354  50.737  1.00 2.44  ? 305  GLN B N   1 
ATOM   7165  C  CA  . GLN B  1 305 ? 39.511  41.753  50.350  1.00 2.00  ? 305  GLN B CA  1 
ATOM   7166  C  C   . GLN B  1 305 ? 40.886  42.311  50.665  1.00 2.00  ? 305  GLN B C   1 
ATOM   7167  O  O   . GLN B  1 305 ? 41.388  43.182  49.960  1.00 2.00  ? 305  GLN B O   1 
ATOM   7168  C  CB  . GLN B  1 305 ? 38.472  42.571  51.104  1.00 2.83  ? 305  GLN B CB  1 
ATOM   7169  C  CG  . GLN B  1 305 ? 37.153  42.687  50.369  1.00 4.20  ? 305  GLN B CG  1 
ATOM   7170  C  CD  . GLN B  1 305 ? 35.961  42.948  51.287  1.00 2.36  ? 305  GLN B CD  1 
ATOM   7171  O  OE1 . GLN B  1 305 ? 35.968  43.872  52.114  1.00 3.17  ? 305  GLN B OE1 1 
ATOM   7172  N  NE2 . GLN B  1 305 ? 34.840  42.246  51.306  1.00 2.00  ? 305  GLN B NE2 1 
ATOM   7173  N  N   . ILE B  1 306 ? 41.526  41.780  51.671  1.00 2.00  ? 306  ILE B N   1 
ATOM   7174  C  CA  . ILE B  1 306 ? 42.845  42.249  52.085  1.00 2.00  ? 306  ILE B CA  1 
ATOM   7175  C  C   . ILE B  1 306 ? 43.951  41.655  51.311  1.00 2.00  ? 306  ILE B C   1 
ATOM   7176  O  O   . ILE B  1 306 ? 44.962  42.333  51.080  1.00 2.55  ? 306  ILE B O   1 
ATOM   7177  C  CB  . ILE B  1 306 ? 43.174  41.825  53.512  1.00 2.00  ? 306  ILE B CB  1 
ATOM   7178  C  CG1 . ILE B  1 306 ? 42.147  42.304  54.536  1.00 2.49  ? 306  ILE B CG1 1 
ATOM   7179  C  CG2 . ILE B  1 306 ? 44.572  42.295  53.867  1.00 2.00  ? 306  ILE B CG2 1 
ATOM   7180  C  CD1 . ILE B  1 306 ? 42.324  41.713  55.919  1.00 2.00  ? 306  ILE B CD1 1 
ATOM   7181  N  N   . ILE B  1 307 ? 43.816  40.417  50.939  1.00 2.00  ? 307  ILE B N   1 
ATOM   7182  C  CA  . ILE B  1 307 ? 44.803  39.777  50.133  1.00 2.00  ? 307  ILE B CA  1 
ATOM   7183  C  C   . ILE B  1 307 ? 44.727  40.425  48.760  1.00 2.00  ? 307  ILE B C   1 
ATOM   7184  O  O   . ILE B  1 307 ? 45.731  40.805  48.177  1.00 2.13  ? 307  ILE B O   1 
ATOM   7185  C  CB  . ILE B  1 307 ? 44.528  38.274  50.047  1.00 2.00  ? 307  ILE B CB  1 
ATOM   7186  C  CG1 . ILE B  1 307 ? 44.682  37.646  51.436  1.00 2.00  ? 307  ILE B CG1 1 
ATOM   7187  C  CG2 . ILE B  1 307 ? 45.471  37.607  49.045  1.00 2.00  ? 307  ILE B CG2 1 
ATOM   7188  C  CD1 . ILE B  1 307 ? 46.036  37.879  52.057  1.00 2.00  ? 307  ILE B CD1 1 
ATOM   7189  N  N   . THR B  1 308 ? 43.496  40.548  48.277  1.00 2.00  ? 308  THR B N   1 
ATOM   7190  C  CA  . THR B  1 308 ? 43.193  41.141  46.976  1.00 2.00  ? 308  THR B CA  1 
ATOM   7191  C  C   . THR B  1 308 ? 43.587  42.609  46.767  1.00 2.00  ? 308  THR B C   1 
ATOM   7192  O  O   . THR B  1 308 ? 44.065  42.973  45.699  1.00 2.00  ? 308  THR B O   1 
ATOM   7193  C  CB  . THR B  1 308 ? 41.690  41.003  46.679  1.00 2.00  ? 308  THR B CB  1 
ATOM   7194  O  OG1 . THR B  1 308 ? 41.411  39.651  46.303  1.00 2.20  ? 308  THR B OG1 1 
ATOM   7195  C  CG2 . THR B  1 308 ? 41.257  41.955  45.571  1.00 2.00  ? 308  THR B CG2 1 
ATOM   7196  N  N   . PHE B  1 309 ? 43.375  43.456  47.767  1.00 2.03  ? 309  PHE B N   1 
ATOM   7197  C  CA  . PHE B  1 309 ? 43.703  44.865  47.618  1.00 2.00  ? 309  PHE B CA  1 
ATOM   7198  C  C   . PHE B  1 309 ? 45.069  45.263  48.144  1.00 2.04  ? 309  PHE B C   1 
ATOM   7199  O  O   . PHE B  1 309 ? 45.566  46.345  47.820  1.00 2.09  ? 309  PHE B O   1 
ATOM   7200  C  CB  . PHE B  1 309 ? 42.646  45.731  48.288  1.00 2.00  ? 309  PHE B CB  1 
ATOM   7201  C  CG  . PHE B  1 309 ? 41.487  46.067  47.402  1.00 2.00  ? 309  PHE B CG  1 
ATOM   7202  C  CD1 . PHE B  1 309 ? 40.566  45.096  47.027  1.00 2.16  ? 309  PHE B CD1 1 
ATOM   7203  C  CD2 . PHE B  1 309 ? 41.306  47.365  46.954  1.00 2.00  ? 309  PHE B CD2 1 
ATOM   7204  C  CE1 . PHE B  1 309 ? 39.478  45.418  46.222  1.00 2.00  ? 309  PHE B CE1 1 
ATOM   7205  C  CE2 . PHE B  1 309 ? 40.226  47.695  46.151  1.00 2.00  ? 309  PHE B CE2 1 
ATOM   7206  C  CZ  . PHE B  1 309 ? 39.310  46.721  45.783  1.00 2.00  ? 309  PHE B CZ  1 
ATOM   7207  N  N   . ARG B  1 310 ? 45.679  44.405  48.953  1.00 2.00  ? 310  ARG B N   1 
ATOM   7208  C  CA  . ARG B  1 310 ? 46.991  44.727  49.497  1.00 2.00  ? 310  ARG B CA  1 
ATOM   7209  C  C   . ARG B  1 310 ? 48.125  44.004  48.808  1.00 2.00  ? 310  ARG B C   1 
ATOM   7210  O  O   . ARG B  1 310 ? 49.191  44.572  48.563  1.00 2.00  ? 310  ARG B O   1 
ATOM   7211  C  CB  . ARG B  1 310 ? 47.080  44.378  50.976  1.00 2.11  ? 310  ARG B CB  1 
ATOM   7212  C  CG  . ARG B  1 310 ? 48.492  44.590  51.527  1.00 2.84  ? 310  ARG B CG  1 
ATOM   7213  C  CD  . ARG B  1 310 ? 48.672  43.961  52.882  1.00 2.00  ? 310  ARG B CD  1 
ATOM   7214  N  NE  . ARG B  1 310 ? 48.734  42.516  52.763  1.00 2.00  ? 310  ARG B NE  1 
ATOM   7215  C  CZ  . ARG B  1 310 ? 48.346  41.681  53.715  1.00 2.04  ? 310  ARG B CZ  1 
ATOM   7216  N  NH1 . ARG B  1 310 ? 47.866  42.161  54.859  1.00 2.00  ? 310  ARG B NH1 1 
ATOM   7217  N  NH2 . ARG B  1 310 ? 48.429  40.369  53.519  1.00 2.06  ? 310  ARG B NH2 1 
ATOM   7218  N  N   . ASP B  1 311 ? 47.899  42.735  48.514  1.00 2.00  ? 311  ASP B N   1 
ATOM   7219  C  CA  . ASP B  1 311 ? 48.933  41.936  47.904  1.00 2.00  ? 311  ASP B CA  1 
ATOM   7220  C  C   . ASP B  1 311 ? 48.754  41.746  46.401  1.00 2.00  ? 311  ASP B C   1 
ATOM   7221  O  O   . ASP B  1 311 ? 49.732  41.744  45.655  1.00 2.00  ? 311  ASP B O   1 
ATOM   7222  C  CB  . ASP B  1 311 ? 49.024  40.591  48.640  1.00 2.73  ? 311  ASP B CB  1 
ATOM   7223  C  CG  . ASP B  1 311 ? 49.288  40.748  50.147  1.00 3.52  ? 311  ASP B CG  1 
ATOM   7224  O  OD1 . ASP B  1 311 ? 49.888  41.782  50.523  1.00 5.26  ? 311  ASP B OD1 1 
ATOM   7225  O  OD2 . ASP B  1 311 ? 48.913  39.852  50.926  1.00 2.98  ? 311  ASP B OD2 1 
ATOM   7226  N  N   . TYR B  1 312 ? 47.509  41.638  45.962  1.00 2.00  ? 312  TYR B N   1 
ATOM   7227  C  CA  . TYR B  1 312 ? 47.205  41.354  44.525  1.00 2.00  ? 312  TYR B CA  1 
ATOM   7228  C  C   . TYR B  1 312 ? 46.963  42.461  43.522  1.00 2.00  ? 312  TYR B C   1 
ATOM   7229  O  O   . TYR B  1 312 ? 47.354  42.325  42.358  1.00 2.24  ? 312  TYR B O   1 
ATOM   7230  C  CB  . TYR B  1 312 ? 45.926  40.528  44.420  1.00 2.00  ? 312  TYR B CB  1 
ATOM   7231  C  CG  . TYR B  1 312 ? 45.635  40.211  42.970  1.00 2.00  ? 312  TYR B CG  1 
ATOM   7232  C  CD1 . TYR B  1 312 ? 46.256  39.100  42.383  1.00 2.00  ? 312  TYR B CD1 1 
ATOM   7233  C  CD2 . TYR B  1 312 ? 44.806  40.997  42.173  1.00 2.00  ? 312  TYR B CD2 1 
ATOM   7234  C  CE1 . TYR B  1 312 ? 46.045  38.783  41.073  1.00 2.00  ? 312  TYR B CE1 1 
ATOM   7235  C  CE2 . TYR B  1 312 ? 44.620  40.689  40.853  1.00 2.00  ? 312  TYR B CE2 1 
ATOM   7236  C  CZ  . TYR B  1 312 ? 45.235  39.580  40.297  1.00 2.00  ? 312  TYR B CZ  1 
ATOM   7237  O  OH  . TYR B  1 312 ? 45.055  39.288  38.958  1.00 2.00  ? 312  TYR B OH  1 
ATOM   7238  N  N   . LEU B  1 313 ? 46.290  43.499  43.928  1.00 2.00  ? 313  LEU B N   1 
ATOM   7239  C  CA  . LEU B  1 313 ? 46.060  44.491  42.903  1.00 2.28  ? 313  LEU B CA  1 
ATOM   7240  C  C   . LEU B  1 313 ? 47.253  45.394  42.755  1.00 5.50  ? 313  LEU B C   1 
ATOM   7241  O  O   . LEU B  1 313 ? 47.447  45.960  41.679  1.00 6.47  ? 313  LEU B O   1 
ATOM   7242  C  CB  . LEU B  1 313 ? 44.825  45.315  43.225  1.00 2.00  ? 313  LEU B CB  1 
ATOM   7243  C  CG  . LEU B  1 313 ? 43.511  44.663  42.845  1.00 2.00  ? 313  LEU B CG  1 
ATOM   7244  C  CD1 . LEU B  1 313 ? 42.392  45.183  43.732  1.00 2.37  ? 313  LEU B CD1 1 
ATOM   7245  C  CD2 . LEU B  1 313 ? 43.185  44.876  41.363  1.00 2.08  ? 313  LEU B CD2 1 
ATOM   7246  N  N   . PRO B  1 314 ? 48.101  45.580  43.789  1.00 2.62  ? 314  PRO B N   1 
ATOM   7247  C  CA  . PRO B  1 314 ? 49.218  46.500  43.514  1.00 2.00  ? 314  PRO B CA  1 
ATOM   7248  C  C   . PRO B  1 314 ? 50.010  46.097  42.307  1.00 2.00  ? 314  PRO B C   1 
ATOM   7249  O  O   . PRO B  1 314 ? 50.330  46.895  41.408  1.00 2.00  ? 314  PRO B O   1 
ATOM   7250  C  CB  . PRO B  1 314 ? 50.064  46.422  44.770  1.00 2.00  ? 314  PRO B CB  1 
ATOM   7251  C  CG  . PRO B  1 314 ? 48.979  46.363  45.813  1.00 2.55  ? 314  PRO B CG  1 
ATOM   7252  C  CD  . PRO B  1 314 ? 47.723  45.834  45.175  1.00 2.00  ? 314  PRO B CD  1 
ATOM   7253  N  N   . ILE B  1 315 ? 50.366  44.792  42.326  1.00 2.67  ? 315  ILE B N   1 
ATOM   7254  C  CA  . ILE B  1 315 ? 51.218  44.173  41.311  1.00 2.82  ? 315  ILE B CA  1 
ATOM   7255  C  C   . ILE B  1 315 ? 50.541  43.816  39.997  1.00 2.61  ? 315  ILE B C   1 
ATOM   7256  O  O   . ILE B  1 315 ? 51.127  43.112  39.168  1.00 2.95  ? 315  ILE B O   1 
ATOM   7257  C  CB  . ILE B  1 315 ? 51.884  42.933  41.937  1.00 2.54  ? 315  ILE B CB  1 
ATOM   7258  C  CG1 . ILE B  1 315 ? 50.885  41.828  42.277  1.00 3.03  ? 315  ILE B CG1 1 
ATOM   7259  C  CG2 . ILE B  1 315 ? 52.662  43.342  43.180  1.00 2.07  ? 315  ILE B CG2 1 
ATOM   7260  C  CD1 . ILE B  1 315 ? 51.525  40.597  42.878  1.00 2.03  ? 315  ILE B CD1 1 
ATOM   7261  N  N   . VAL B  1 316 ? 49.316  44.281  39.762  1.00 2.00  ? 316  VAL B N   1 
ATOM   7262  C  CA  . VAL B  1 316 ? 48.663  44.078  38.475  1.00 2.00  ? 316  VAL B CA  1 
ATOM   7263  C  C   . VAL B  1 316 ? 48.666  45.460  37.835  1.00 2.70  ? 316  VAL B C   1 
ATOM   7264  O  O   . VAL B  1 316 ? 49.257  45.660  36.773  1.00 3.18  ? 316  VAL B O   1 
ATOM   7265  C  CB  . VAL B  1 316 ? 47.213  43.588  38.599  1.00 2.00  ? 316  VAL B CB  1 
ATOM   7266  C  CG1 . VAL B  1 316 ? 46.529  43.661  37.243  1.00 2.00  ? 316  VAL B CG1 1 
ATOM   7267  C  CG2 . VAL B  1 316 ? 47.196  42.153  39.095  1.00 2.32  ? 316  VAL B CG2 1 
ATOM   7268  N  N   . LEU B  1 317 ? 48.024  46.415  38.506  1.00 2.80  ? 317  LEU B N   1 
ATOM   7269  C  CA  . LEU B  1 317 ? 47.954  47.800  38.037  1.00 2.66  ? 317  LEU B CA  1 
ATOM   7270  C  C   . LEU B  1 317 ? 49.292  48.510  38.196  1.00 3.04  ? 317  LEU B C   1 
ATOM   7271  O  O   . LEU B  1 317 ? 49.524  49.565  37.609  1.00 2.00  ? 317  LEU B O   1 
ATOM   7272  C  CB  . LEU B  1 317 ? 46.889  48.566  38.819  1.00 2.00  ? 317  LEU B CB  1 
ATOM   7273  C  CG  . LEU B  1 317 ? 45.426  48.343  38.438  1.00 2.31  ? 317  LEU B CG  1 
ATOM   7274  C  CD1 . LEU B  1 317 ? 45.302  47.166  37.489  1.00 3.35  ? 317  LEU B CD1 1 
ATOM   7275  C  CD2 . LEU B  1 317 ? 44.607  48.113  39.701  1.00 2.56  ? 317  LEU B CD2 1 
ATOM   7276  N  N   . GLY B  1 318 ? 50.155  47.925  39.020  1.00 6.06  ? 318  GLY B N   1 
ATOM   7277  C  CA  . GLY B  1 318 ? 51.478  48.476  39.266  1.00 7.65  ? 318  GLY B CA  1 
ATOM   7278  C  C   . GLY B  1 318 ? 51.563  49.929  39.695  1.00 7.89  ? 318  GLY B C   1 
ATOM   7279  O  O   . GLY B  1 318 ? 51.095  50.312  40.763  1.00 8.79  ? 318  GLY B O   1 
ATOM   7280  N  N   . SER B  1 319 ? 52.175  50.743  38.847  1.00 8.87  ? 319  SER B N   1 
ATOM   7281  C  CA  . SER B  1 319 ? 52.351  52.155  39.132  1.00 9.26  ? 319  SER B CA  1 
ATOM   7282  C  C   . SER B  1 319 ? 51.121  52.980  38.820  1.00 9.52  ? 319  SER B C   1 
ATOM   7283  O  O   . SER B  1 319 ? 51.167  54.198  38.916  1.00 9.48  ? 319  SER B O   1 
ATOM   7284  C  CB  . SER B  1 319 ? 53.522  52.702  38.322  1.00 10.38 ? 319  SER B CB  1 
ATOM   7285  O  OG  . SER B  1 319 ? 53.250  52.612  36.930  1.00 10.74 ? 319  SER B OG  1 
ATOM   7286  N  N   . GLU B  1 320 ? 50.030  52.328  38.436  1.00 11.17 ? 320  GLU B N   1 
ATOM   7287  C  CA  . GLU B  1 320 ? 48.800  53.045  38.104  1.00 13.20 ? 320  GLU B CA  1 
ATOM   7288  C  C   . GLU B  1 320 ? 47.699  52.898  39.158  1.00 14.07 ? 320  GLU B C   1 
ATOM   7289  O  O   . GLU B  1 320 ? 46.551  53.271  38.912  1.00 13.72 ? 320  GLU B O   1 
ATOM   7290  C  CB  . GLU B  1 320 ? 48.257  52.569  36.751  1.00 15.91 ? 320  GLU B CB  1 
ATOM   7291  C  CG  . GLU B  1 320 ? 49.025  53.059  35.530  1.00 20.11 ? 320  GLU B CG  1 
ATOM   7292  C  CD  . GLU B  1 320 ? 48.299  54.171  34.778  1.00 22.76 ? 320  GLU B CD  1 
ATOM   7293  O  OE1 . GLU B  1 320 ? 47.130  53.959  34.380  1.00 24.08 ? 320  GLU B OE1 1 
ATOM   7294  O  OE2 . GLU B  1 320 ? 48.898  55.253  34.575  1.00 24.58 ? 320  GLU B OE2 1 
ATOM   7295  N  N   . MET B  1 321 ? 48.038  52.359  40.328  1.00 14.82 ? 321  MET B N   1 
ATOM   7296  C  CA  . MET B  1 321 ? 47.044  52.169  41.385  1.00 13.96 ? 321  MET B CA  1 
ATOM   7297  C  C   . MET B  1 321 ? 46.748  53.462  42.145  1.00 16.45 ? 321  MET B C   1 
ATOM   7298  O  O   . MET B  1 321 ? 45.586  53.843  42.297  1.00 16.65 ? 321  MET B O   1 
ATOM   7299  C  CB  . MET B  1 321 ? 47.500  51.078  42.362  1.00 12.09 ? 321  MET B CB  1 
ATOM   7300  C  CG  . MET B  1 321 ? 46.423  50.668  43.351  1.00 10.55 ? 321  MET B CG  1 
ATOM   7301  S  SD  . MET B  1 321 ? 46.531  48.931  43.821  1.00 10.09 ? 321  MET B SD  1 
ATOM   7302  C  CE  . MET B  1 321 ? 45.857  48.952  45.499  1.00 9.01  ? 321  MET B CE  1 
ATOM   7303  N  N   . GLN B  1 322 ? 47.794  54.134  42.620  1.00 17.81 ? 322  GLN B N   1 
ATOM   7304  C  CA  . GLN B  1 322 ? 47.619  55.386  43.351  1.00 18.78 ? 322  GLN B CA  1 
ATOM   7305  C  C   . GLN B  1 322 ? 46.717  56.316  42.543  1.00 17.32 ? 322  GLN B C   1 
ATOM   7306  O  O   . GLN B  1 322 ? 45.912  57.065  43.094  1.00 15.32 ? 322  GLN B O   1 
ATOM   7307  C  CB  . GLN B  1 322 ? 48.976  56.055  43.579  1.00 23.89 ? 322  GLN B CB  1 
ATOM   7308  C  CG  . GLN B  1 322 ? 49.980  55.184  44.315  1.00 29.64 ? 322  GLN B CG  1 
ATOM   7309  C  CD  . GLN B  1 322 ? 51.380  55.772  44.303  1.00 32.26 ? 322  GLN B CD  1 
ATOM   7310  O  OE1 . GLN B  1 322 ? 51.982  55.969  43.240  1.00 33.89 ? 322  GLN B OE1 1 
ATOM   7311  N  NE2 . GLN B  1 322 ? 51.908  56.055  45.489  1.00 34.44 ? 322  GLN B NE2 1 
ATOM   7312  N  N   . LYS B  1 323 ? 46.858  56.245  41.227  1.00 14.49 ? 323  LYS B N   1 
ATOM   7313  C  CA  . LYS B  1 323 ? 46.076  57.063  40.317  1.00 13.69 ? 323  LYS B CA  1 
ATOM   7314  C  C   . LYS B  1 323 ? 44.588  56.693  40.292  1.00 14.87 ? 323  LYS B C   1 
ATOM   7315  O  O   . LYS B  1 323 ? 43.730  57.580  40.260  1.00 15.93 ? 323  LYS B O   1 
ATOM   7316  C  CB  . LYS B  1 323 ? 46.665  56.943  38.910  1.00 12.25 ? 323  LYS B CB  1 
ATOM   7317  C  CG  . LYS B  1 323 ? 45.737  57.360  37.778  1.00 12.96 ? 323  LYS B CG  1 
ATOM   7318  C  CD  . LYS B  1 323 ? 46.248  56.805  36.444  1.00 14.39 ? 323  LYS B CD  1 
ATOM   7319  C  CE  . LYS B  1 323 ? 46.739  57.895  35.487  1.00 15.49 ? 323  LYS B CE  1 
ATOM   7320  N  NZ  . LYS B  1 323 ? 45.610  58.731  34.953  1.00 15.75 ? 323  LYS B NZ  1 
ATOM   7321  N  N   . TRP B  1 324 ? 44.284  55.394  40.318  1.00 14.35 ? 324  TRP B N   1 
ATOM   7322  C  CA  . TRP B  1 324 ? 42.895  54.929  40.255  1.00 12.52 ? 324  TRP B CA  1 
ATOM   7323  C  C   . TRP B  1 324 ? 42.235  54.459  41.548  1.00 11.55 ? 324  TRP B C   1 
ATOM   7324  O  O   . TRP B  1 324 ? 41.024  54.597  41.702  1.00 12.24 ? 324  TRP B O   1 
ATOM   7325  C  CB  . TRP B  1 324 ? 42.759  53.813  39.216  1.00 13.70 ? 324  TRP B CB  1 
ATOM   7326  C  CG  . TRP B  1 324 ? 43.033  54.252  37.819  1.00 14.06 ? 324  TRP B CG  1 
ATOM   7327  C  CD1 . TRP B  1 324 ? 44.194  54.091  37.119  1.00 14.40 ? 324  TRP B CD1 1 
ATOM   7328  C  CD2 . TRP B  1 324 ? 42.139  54.963  36.959  1.00 14.15 ? 324  TRP B CD2 1 
ATOM   7329  N  NE1 . TRP B  1 324 ? 44.081  54.662  35.873  1.00 15.27 ? 324  TRP B NE1 1 
ATOM   7330  C  CE2 . TRP B  1 324 ? 42.830  55.206  35.747  1.00 14.95 ? 324  TRP B CE2 1 
ATOM   7331  C  CE3 . TRP B  1 324 ? 40.822  55.421  37.094  1.00 13.66 ? 324  TRP B CE3 1 
ATOM   7332  C  CZ2 . TRP B  1 324 ? 42.245  55.887  34.673  1.00 14.63 ? 324  TRP B CZ2 1 
ATOM   7333  C  CZ3 . TRP B  1 324 ? 40.239  56.097  36.029  1.00 13.95 ? 324  TRP B CZ3 1 
ATOM   7334  C  CH2 . TRP B  1 324 ? 40.953  56.324  34.831  1.00 14.98 ? 324  TRP B CH2 1 
ATOM   7335  N  N   . ILE B  1 325 ? 42.998  53.883  42.466  1.00 9.62  ? 325  ILE B N   1 
ATOM   7336  C  CA  . ILE B  1 325 ? 42.398  53.423  43.705  1.00 8.75  ? 325  ILE B CA  1 
ATOM   7337  C  C   . ILE B  1 325 ? 42.914  54.256  44.861  1.00 9.16  ? 325  ILE B C   1 
ATOM   7338  O  O   . ILE B  1 325 ? 43.666  53.772  45.715  1.00 8.64  ? 325  ILE B O   1 
ATOM   7339  C  CB  . ILE B  1 325 ? 42.697  51.927  43.991  1.00 7.71  ? 325  ILE B CB  1 
ATOM   7340  C  CG1 . ILE B  1 325 ? 42.305  51.061  42.794  1.00 5.84  ? 325  ILE B CG1 1 
ATOM   7341  C  CG2 . ILE B  1 325 ? 41.888  51.461  45.192  1.00 8.58  ? 325  ILE B CG2 1 
ATOM   7342  C  CD1 . ILE B  1 325 ? 42.402  49.580  43.066  1.00 2.18  ? 325  ILE B CD1 1 
ATOM   7343  N  N   . PRO B  1 326 ? 42.523  55.537  44.900  1.00 9.95  ? 326  PRO B N   1 
ATOM   7344  C  CA  . PRO B  1 326 ? 42.976  56.399  45.989  1.00 11.62 ? 326  PRO B CA  1 
ATOM   7345  C  C   . PRO B  1 326 ? 42.770  55.696  47.320  1.00 11.95 ? 326  PRO B C   1 
ATOM   7346  O  O   . PRO B  1 326 ? 41.954  54.783  47.432  1.00 10.97 ? 326  PRO B O   1 
ATOM   7347  C  CB  . PRO B  1 326 ? 42.096  57.643  45.838  1.00 10.58 ? 326  PRO B CB  1 
ATOM   7348  C  CG  . PRO B  1 326 ? 40.868  57.118  45.145  1.00 10.57 ? 326  PRO B CG  1 
ATOM   7349  C  CD  . PRO B  1 326 ? 41.472  56.202  44.117  1.00 10.12 ? 326  PRO B CD  1 
ATOM   7350  N  N   . ARG B  1 327 ? 43.524  56.125  48.320  1.00 14.77 ? 327  ARG B N   1 
ATOM   7351  C  CA  . ARG B  1 327 ? 43.440  55.551  49.653  1.00 17.41 ? 327  ARG B CA  1 
ATOM   7352  C  C   . ARG B  1 327 ? 42.002  55.687  50.203  1.00 15.87 ? 327  ARG B C   1 
ATOM   7353  O  O   . ARG B  1 327 ? 41.406  56.764  50.143  1.00 15.00 ? 327  ARG B O   1 
ATOM   7354  C  CB  . ARG B  1 327 ? 44.482  56.245  50.548  1.00 21.81 ? 327  ARG B CB  1 
ATOM   7355  C  CG  . ARG B  1 327 ? 45.947  56.125  50.016  1.00 28.63 ? 327  ARG B CG  1 
ATOM   7356  C  CD  . ARG B  1 327 ? 46.186  56.902  48.693  1.00 31.81 ? 327  ARG B CD  1 
ATOM   7357  N  NE  . ARG B  1 327 ? 47.420  56.540  47.974  1.00 36.53 ? 327  ARG B NE  1 
ATOM   7358  C  CZ  . ARG B  1 327 ? 48.647  56.992  48.255  1.00 38.06 ? 327  ARG B CZ  1 
ATOM   7359  N  NH1 . ARG B  1 327 ? 48.846  57.844  49.258  1.00 38.87 ? 327  ARG B NH1 1 
ATOM   7360  N  NH2 . ARG B  1 327 ? 49.682  56.599  47.514  1.00 38.51 ? 327  ARG B NH2 1 
ATOM   7361  N  N   . TYR B  1 328 ? 41.453  54.584  50.719  1.00 13.74 ? 328  TYR B N   1 
ATOM   7362  C  CA  . TYR B  1 328 ? 40.077  54.531  51.249  1.00 12.15 ? 328  TYR B CA  1 
ATOM   7363  C  C   . TYR B  1 328 ? 39.683  55.650  52.215  1.00 12.49 ? 328  TYR B C   1 
ATOM   7364  O  O   . TYR B  1 328 ? 40.469  56.048  53.079  1.00 10.82 ? 328  TYR B O   1 
ATOM   7365  C  CB  . TYR B  1 328 ? 39.836  53.174  51.923  1.00 10.89 ? 328  TYR B CB  1 
ATOM   7366  C  CG  . TYR B  1 328 ? 38.402  52.896  52.351  1.00 8.37  ? 328  TYR B CG  1 
ATOM   7367  C  CD1 . TYR B  1 328 ? 37.369  52.854  51.413  1.00 7.13  ? 328  TYR B CD1 1 
ATOM   7368  C  CD2 . TYR B  1 328 ? 38.091  52.610  53.691  1.00 6.81  ? 328  TYR B CD2 1 
ATOM   7369  C  CE1 . TYR B  1 328 ? 36.060  52.529  51.793  1.00 6.18  ? 328  TYR B CE1 1 
ATOM   7370  C  CE2 . TYR B  1 328 ? 36.785  52.283  54.082  1.00 4.88  ? 328  TYR B CE2 1 
ATOM   7371  C  CZ  . TYR B  1 328 ? 35.773  52.242  53.124  1.00 5.63  ? 328  TYR B CZ  1 
ATOM   7372  O  OH  . TYR B  1 328 ? 34.483  51.889  53.469  1.00 2.65  ? 328  TYR B OH  1 
ATOM   7373  N  N   . GLN B  1 329 ? 38.443  56.128  52.074  1.00 13.62 ? 329  GLN B N   1 
ATOM   7374  C  CA  . GLN B  1 329 ? 37.920  57.211  52.906  1.00 13.17 ? 329  GLN B CA  1 
ATOM   7375  C  C   . GLN B  1 329 ? 36.423  57.131  53.230  1.00 11.52 ? 329  GLN B C   1 
ATOM   7376  O  O   . GLN B  1 329 ? 35.714  58.138  53.161  1.00 10.41 ? 329  GLN B O   1 
ATOM   7377  C  CB  . GLN B  1 329 ? 38.226  58.553  52.236  1.00 16.16 ? 329  GLN B CB  1 
ATOM   7378  C  CG  . GLN B  1 329 ? 38.759  59.600  53.202  1.00 19.13 ? 329  GLN B CG  1 
ATOM   7379  C  CD  . GLN B  1 329 ? 39.541  60.706  52.512  1.00 19.96 ? 329  GLN B CD  1 
ATOM   7380  O  OE1 . GLN B  1 329 ? 40.162  61.540  53.179  1.00 21.13 ? 329  GLN B OE1 1 
ATOM   7381  N  NE2 . GLN B  1 329 ? 39.513  60.723  51.176  1.00 19.31 ? 329  GLN B NE2 1 
ATOM   7382  N  N   . GLY B  1 330 ? 35.952  55.934  53.640  1.00 10.00 ? 330  GLY B N   1 
ATOM   7383  C  CA  . GLY B  1 330 ? 34.493  55.750  54.058  1.00 8.94  ? 330  GLY B CA  1 
ATOM   7384  C  C   . GLY B  1 330 ? 33.370  55.334  53.023  1.00 8.81  ? 330  GLY B C   1 
ATOM   7385  O  O   . GLY B  1 330 ? 33.528  55.588  51.821  1.00 7.45  ? 330  GLY B O   1 
ATOM   7386  N  N   . TYR B  1 331 ? 32.204  54.693  53.513  1.00 9.22  ? 331  TYR B N   1 
ATOM   7387  C  CA  . TYR B  1 331 ? 31.095  54.270  52.612  1.00 9.35  ? 331  TYR B CA  1 
ATOM   7388  C  C   . TYR B  1 331 ? 30.505  55.479  51.816  1.00 10.32 ? 331  TYR B C   1 
ATOM   7389  O  O   . TYR B  1 331 ? 29.896  56.385  52.373  1.00 10.64 ? 331  TYR B O   1 
ATOM   7390  C  CB  . TYR B  1 331 ? 29.984  53.486  53.361  1.00 10.95 ? 331  TYR B CB  1 
ATOM   7391  C  CG  . TYR B  1 331 ? 28.773  52.927  52.572  1.00 12.25 ? 331  TYR B CG  1 
ATOM   7392  C  CD1 . TYR B  1 331 ? 28.941  52.173  51.395  1.00 12.91 ? 331  TYR B CD1 1 
ATOM   7393  C  CD2 . TYR B  1 331 ? 27.481  53.162  53.035  1.00 12.51 ? 331  TYR B CD2 1 
ATOM   7394  C  CE1 . TYR B  1 331 ? 27.826  51.689  50.696  1.00 13.15 ? 331  TYR B CE1 1 
ATOM   7395  C  CE2 . TYR B  1 331 ? 26.389  52.680  52.344  1.00 11.95 ? 331  TYR B CE2 1 
ATOM   7396  C  CZ  . TYR B  1 331 ? 26.559  51.957  51.177  1.00 12.35 ? 331  TYR B CZ  1 
ATOM   7397  O  OH  . TYR B  1 331 ? 25.469  51.509  50.491  1.00 13.94 ? 331  TYR B OH  1 
ATOM   7398  N  N   . ASN B  1 332 ? 30.727  55.430  50.516  1.00 12.43 ? 332  ASN B N   1 
ATOM   7399  C  CA  . ASN B  1 332 ? 30.129  56.433  49.642  1.00 13.36 ? 332  ASN B CA  1 
ATOM   7400  C  C   . ASN B  1 332 ? 28.826  55.901  49.109  1.00 11.54 ? 332  ASN B C   1 
ATOM   7401  O  O   . ASN B  1 332 ? 28.722  55.390  47.992  1.00 9.10  ? 332  ASN B O   1 
ATOM   7402  C  CB  . ASN B  1 332 ? 30.999  56.831  48.452  1.00 17.60 ? 332  ASN B CB  1 
ATOM   7403  C  CG  . ASN B  1 332 ? 30.340  57.997  47.740  1.00 26.43 ? 332  ASN B CG  1 
ATOM   7404  O  OD1 . ASN B  1 332 ? 29.126  58.144  47.801  1.00 22.10 ? 332  ASN B OD1 1 
ATOM   7405  N  ND2 . ASN B  1 332 ? 31.136  58.831  47.077  1.00 38.39 ? 332  ASN B ND2 1 
ATOM   7406  N  N   . ASN B  1 333 ? 27.842  56.035  49.956  1.00 10.05 ? 333  ASN B N   1 
ATOM   7407  C  CA  . ASN B  1 333 ? 26.507  55.495  49.704  1.00 9.32  ? 333  ASN B CA  1 
ATOM   7408  C  C   . ASN B  1 333 ? 26.086  55.652  48.236  1.00 7.72  ? 333  ASN B C   1 
ATOM   7409  O  O   . ASN B  1 333 ? 25.276  54.850  47.751  1.00 6.75  ? 333  ASN B O   1 
ATOM   7410  C  CB  . ASN B  1 333 ? 25.574  56.071  50.872  1.00 11.52 ? 333  ASN B CB  1 
ATOM   7411  C  CG  . ASN B  1 333 ? 24.303  56.878  50.609  1.00 13.04 ? 333  ASN B CG  1 
ATOM   7412  O  OD1 . ASN B  1 333 ? 23.307  56.316  50.166  1.00 15.50 ? 333  ASN B OD1 1 
ATOM   7413  N  ND2 . ASN B  1 333 ? 24.351  58.180  50.870  1.00 12.62 ? 333  ASN B ND2 1 
ATOM   7414  N  N   . SER B  1 334 ? 26.631  56.637  47.554  1.00 6.37  ? 334  SER B N   1 
ATOM   7415  C  CA  . SER B  1 334 ? 26.216  56.868  46.183  1.00 5.59  ? 334  SER B CA  1 
ATOM   7416  C  C   . SER B  1 334 ? 27.203  56.486  45.112  1.00 5.94  ? 334  SER B C   1 
ATOM   7417  O  O   . SER B  1 334 ? 27.557  57.334  44.290  1.00 7.02  ? 334  SER B O   1 
ATOM   7418  C  CB  . SER B  1 334 ? 25.841  58.344  46.016  1.00 5.64  ? 334  SER B CB  1 
ATOM   7419  O  OG  . SER B  1 334 ? 24.984  58.773  47.059  1.00 9.63  ? 334  SER B OG  1 
ATOM   7420  N  N   . VAL B  1 335 ? 27.653  55.230  45.090  1.00 4.84  ? 335  VAL B N   1 
ATOM   7421  C  CA  . VAL B  1 335 ? 28.589  54.770  44.059  1.00 2.35  ? 335  VAL B CA  1 
ATOM   7422  C  C   . VAL B  1 335 ? 28.186  53.394  43.530  1.00 2.00  ? 335  VAL B C   1 
ATOM   7423  O  O   . VAL B  1 335 ? 28.006  52.460  44.302  1.00 2.00  ? 335  VAL B O   1 
ATOM   7424  C  CB  . VAL B  1 335 ? 30.015  54.677  44.602  1.00 2.00  ? 335  VAL B CB  1 
ATOM   7425  C  CG1 . VAL B  1 335 ? 30.970  54.162  43.541  1.00 4.04  ? 335  VAL B CG1 1 
ATOM   7426  C  CG2 . VAL B  1 335 ? 30.468  56.034  45.116  1.00 2.00  ? 335  VAL B CG2 1 
ATOM   7427  N  N   . ASP B  1 336 ? 28.025  53.274  42.216  1.00 2.62  ? 336  ASP B N   1 
ATOM   7428  C  CA  . ASP B  1 336 ? 27.612  52.013  41.577  1.00 2.87  ? 336  ASP B CA  1 
ATOM   7429  C  C   . ASP B  1 336 ? 28.531  50.816  41.910  1.00 2.26  ? 336  ASP B C   1 
ATOM   7430  O  O   . ASP B  1 336 ? 29.580  50.628  41.289  1.00 2.00  ? 336  ASP B O   1 
ATOM   7431  C  CB  . ASP B  1 336 ? 27.557  52.215  40.057  1.00 3.08  ? 336  ASP B CB  1 
ATOM   7432  C  CG  . ASP B  1 336 ? 26.476  51.384  39.394  1.00 3.15  ? 336  ASP B CG  1 
ATOM   7433  O  OD1 . ASP B  1 336 ? 26.051  50.379  39.995  1.00 3.15  ? 336  ASP B OD1 1 
ATOM   7434  O  OD2 . ASP B  1 336 ? 26.061  51.729  38.269  1.00 2.29  ? 336  ASP B OD2 1 
ATOM   7435  N  N   . PRO B  1 337 ? 28.125  49.968  42.869  1.00 2.72  ? 337  PRO B N   1 
ATOM   7436  C  CA  . PRO B  1 337 ? 28.952  48.819  43.240  1.00 2.55  ? 337  PRO B CA  1 
ATOM   7437  C  C   . PRO B  1 337 ? 28.795  47.664  42.268  1.00 3.07  ? 337  PRO B C   1 
ATOM   7438  O  O   . PRO B  1 337 ? 29.297  46.568  42.508  1.00 4.16  ? 337  PRO B O   1 
ATOM   7439  C  CB  . PRO B  1 337 ? 28.430  48.469  44.623  1.00 2.00  ? 337  PRO B CB  1 
ATOM   7440  C  CG  . PRO B  1 337 ? 26.948  48.636  44.422  1.00 2.00  ? 337  PRO B CG  1 
ATOM   7441  C  CD  . PRO B  1 337 ? 26.835  49.927  43.586  1.00 2.38  ? 337  PRO B CD  1 
ATOM   7442  N  N   . ARG B  1 338 ? 28.101  47.912  41.167  1.00 2.00  ? 338  ARG B N   1 
ATOM   7443  C  CA  . ARG B  1 338 ? 27.873  46.871  40.179  1.00 2.95  ? 338  ARG B CA  1 
ATOM   7444  C  C   . ARG B  1 338 ? 29.042  46.660  39.220  1.00 2.35  ? 338  ARG B C   1 
ATOM   7445  O  O   . ARG B  1 338 ? 29.870  47.549  39.021  1.00 3.04  ? 338  ARG B O   1 
ATOM   7446  C  CB  . ARG B  1 338 ? 26.618  47.196  39.374  1.00 4.29  ? 338  ARG B CB  1 
ATOM   7447  C  CG  . ARG B  1 338 ? 25.318  47.140  40.168  1.00 5.47  ? 338  ARG B CG  1 
ATOM   7448  C  CD  . ARG B  1 338 ? 24.160  47.590  39.294  1.00 4.57  ? 338  ARG B CD  1 
ATOM   7449  N  NE  . ARG B  1 338 ? 24.416  48.915  38.742  1.00 3.67  ? 338  ARG B NE  1 
ATOM   7450  C  CZ  . ARG B  1 338 ? 23.889  49.360  37.613  1.00 2.75  ? 338  ARG B CZ  1 
ATOM   7451  N  NH1 . ARG B  1 338 ? 23.076  48.585  36.916  1.00 5.31  ? 338  ARG B NH1 1 
ATOM   7452  N  NH2 . ARG B  1 338 ? 24.183  50.571  37.176  1.00 4.79  ? 338  ARG B NH2 1 
ATOM   7453  N  N   . ILE B  1 339 ? 29.097  45.472  38.627  1.00 2.00  ? 339  ILE B N   1 
ATOM   7454  C  CA  . ILE B  1 339 ? 30.143  45.142  37.667  1.00 3.84  ? 339  ILE B CA  1 
ATOM   7455  C  C   . ILE B  1 339 ? 29.676  45.521  36.262  1.00 2.00  ? 339  ILE B C   1 
ATOM   7456  O  O   . ILE B  1 339 ? 28.585  45.147  35.842  1.00 2.00  ? 339  ILE B O   1 
ATOM   7457  C  CB  . ILE B  1 339 ? 30.465  43.626  37.661  1.00 2.57  ? 339  ILE B CB  1 
ATOM   7458  C  CG1 . ILE B  1 339 ? 30.956  43.167  39.041  1.00 2.00  ? 339  ILE B CG1 1 
ATOM   7459  C  CG2 . ILE B  1 339 ? 31.496  43.333  36.582  1.00 2.00  ? 339  ILE B CG2 1 
ATOM   7460  C  CD1 . ILE B  1 339 ? 32.415  43.431  39.300  1.00 2.00  ? 339  ILE B CD1 1 
ATOM   7461  N  N   . SER B  1 340 ? 30.507  46.262  35.542  1.00 2.00  ? 340  SER B N   1 
ATOM   7462  C  CA  . SER B  1 340 ? 30.186  46.675  34.183  1.00 2.12  ? 340  SER B CA  1 
ATOM   7463  C  C   . SER B  1 340 ? 30.409  45.492  33.235  1.00 3.56  ? 340  SER B C   1 
ATOM   7464  O  O   . SER B  1 340 ? 31.156  44.569  33.569  1.00 6.08  ? 340  SER B O   1 
ATOM   7465  C  CB  . SER B  1 340 ? 31.076  47.850  33.793  1.00 2.00  ? 340  SER B CB  1 
ATOM   7466  O  OG  . SER B  1 340 ? 32.409  47.630  34.220  1.00 2.00  ? 340  SER B OG  1 
ATOM   7467  N  N   . ASN B  1 341 ? 29.770  45.507  32.064  1.00 2.34  ? 341  ASN B N   1 
ATOM   7468  C  CA  . ASN B  1 341 ? 29.922  44.406  31.111  1.00 2.00  ? 341  ASN B CA  1 
ATOM   7469  C  C   . ASN B  1 341 ? 31.385  44.257  30.736  1.00 2.00  ? 341  ASN B C   1 
ATOM   7470  O  O   . ASN B  1 341 ? 31.944  43.174  30.801  1.00 2.03  ? 341  ASN B O   1 
ATOM   7471  C  CB  . ASN B  1 341 ? 29.097  44.659  29.843  1.00 2.04  ? 341  ASN B CB  1 
ATOM   7472  C  CG  . ASN B  1 341 ? 28.490  43.383  29.265  1.00 2.00  ? 341  ASN B CG  1 
ATOM   7473  O  OD1 . ASN B  1 341 ? 29.189  42.394  29.036  1.00 2.00  ? 341  ASN B OD1 1 
ATOM   7474  N  ND2 . ASN B  1 341 ? 27.181  43.409  29.019  1.00 2.00  ? 341  ASN B ND2 1 
ATOM   7475  N  N   . VAL B  1 342 ? 32.002  45.364  30.362  1.00 2.00  ? 342  VAL B N   1 
ATOM   7476  C  CA  . VAL B  1 342 ? 33.396  45.366  29.962  1.00 2.00  ? 342  VAL B CA  1 
ATOM   7477  C  C   . VAL B  1 342 ? 34.333  44.741  30.975  1.00 2.00  ? 342  VAL B C   1 
ATOM   7478  O  O   . VAL B  1 342 ? 35.265  44.036  30.603  1.00 2.00  ? 342  VAL B O   1 
ATOM   7479  C  CB  . VAL B  1 342 ? 33.882  46.791  29.684  1.00 2.00  ? 342  VAL B CB  1 
ATOM   7480  C  CG1 . VAL B  1 342 ? 33.849  47.594  30.960  1.00 2.31  ? 342  VAL B CG1 1 
ATOM   7481  C  CG2 . VAL B  1 342 ? 35.274  46.765  29.082  1.00 2.00  ? 342  VAL B CG2 1 
ATOM   7482  N  N   . PHE B  1 343 ? 34.100  44.987  32.256  1.00 2.82  ? 343  PHE B N   1 
ATOM   7483  C  CA  . PHE B  1 343 ? 34.992  44.432  33.269  1.00 2.24  ? 343  PHE B CA  1 
ATOM   7484  C  C   . PHE B  1 343 ? 35.242  42.965  33.035  1.00 2.00  ? 343  PHE B C   1 
ATOM   7485  O  O   . PHE B  1 343 ? 36.382  42.521  33.067  1.00 2.29  ? 343  PHE B O   1 
ATOM   7486  C  CB  . PHE B  1 343 ? 34.426  44.600  34.673  1.00 2.00  ? 343  PHE B CB  1 
ATOM   7487  C  CG  . PHE B  1 343 ? 35.360  44.136  35.747  1.00 2.00  ? 343  PHE B CG  1 
ATOM   7488  C  CD1 . PHE B  1 343 ? 36.547  44.813  35.987  1.00 2.00  ? 343  PHE B CD1 1 
ATOM   7489  C  CD2 . PHE B  1 343 ? 35.057  43.019  36.518  1.00 2.36  ? 343  PHE B CD2 1 
ATOM   7490  C  CE1 . PHE B  1 343 ? 37.423  44.388  36.984  1.00 2.46  ? 343  PHE B CE1 1 
ATOM   7491  C  CE2 . PHE B  1 343 ? 35.924  42.579  37.518  1.00 2.00  ? 343  PHE B CE2 1 
ATOM   7492  C  CZ  . PHE B  1 343 ? 37.112  43.268  37.752  1.00 2.75  ? 343  PHE B CZ  1 
ATOM   7493  N  N   . THR B  1 344 ? 34.165  42.224  32.787  1.00 2.85  ? 344  THR B N   1 
ATOM   7494  C  CA  . THR B  1 344 ? 34.248  40.782  32.557  1.00 6.56  ? 344  THR B CA  1 
ATOM   7495  C  C   . THR B  1 344 ? 34.991  40.390  31.268  1.00 2.34  ? 344  THR B C   1 
ATOM   7496  O  O   . THR B  1 344 ? 35.157  39.204  30.965  1.00 2.61  ? 344  THR B O   1 
ATOM   7497  C  CB  . THR B  1 344 ? 32.826  40.139  32.589  1.00 3.65  ? 344  THR B CB  1 
ATOM   7498  O  OG1 . THR B  1 344 ? 32.212  40.192  31.292  1.00 2.00  ? 344  THR B OG1 1 
ATOM   7499  C  CG2 . THR B  1 344 ? 31.956  40.891  33.579  1.00 2.00  ? 344  THR B CG2 1 
ATOM   7500  N  N   . PHE B  1 345 ? 35.427  41.385  30.505  1.00 2.00  ? 345  PHE B N   1 
ATOM   7501  C  CA  . PHE B  1 345 ? 36.184  41.103  29.303  1.00 2.00  ? 345  PHE B CA  1 
ATOM   7502  C  C   . PHE B  1 345 ? 37.564  41.691  29.519  1.00 3.69  ? 345  PHE B C   1 
ATOM   7503  O  O   . PHE B  1 345 ? 38.524  41.288  28.869  1.00 6.17  ? 345  PHE B O   1 
ATOM   7504  C  CB  . PHE B  1 345 ? 35.541  41.719  28.063  1.00 2.00  ? 345  PHE B CB  1 
ATOM   7505  C  CG  . PHE B  1 345 ? 34.300  41.011  27.605  1.00 2.00  ? 345  PHE B CG  1 
ATOM   7506  C  CD1 . PHE B  1 345 ? 33.037  41.482  27.959  1.00 3.18  ? 345  PHE B CD1 1 
ATOM   7507  C  CD2 . PHE B  1 345 ? 34.387  39.882  26.808  1.00 2.00  ? 345  PHE B CD2 1 
ATOM   7508  C  CE1 . PHE B  1 345 ? 31.870  40.836  27.518  1.00 2.00  ? 345  PHE B CE1 1 
ATOM   7509  C  CE2 . PHE B  1 345 ? 33.228  39.227  26.362  1.00 2.12  ? 345  PHE B CE2 1 
ATOM   7510  C  CZ  . PHE B  1 345 ? 31.969  39.708  26.718  1.00 2.00  ? 345  PHE B CZ  1 
ATOM   7511  N  N   . ALA B  1 346 ? 37.668  42.628  30.457  1.00 3.14  ? 346  ALA B N   1 
ATOM   7512  C  CA  . ALA B  1 346 ? 38.946  43.267  30.753  1.00 2.00  ? 346  ALA B CA  1 
ATOM   7513  C  C   . ALA B  1 346 ? 39.738  42.506  31.792  1.00 2.00  ? 346  ALA B C   1 
ATOM   7514  O  O   . ALA B  1 346 ? 40.937  42.690  31.907  1.00 2.00  ? 346  ALA B O   1 
ATOM   7515  C  CB  . ALA B  1 346 ? 38.724  44.676  31.232  1.00 2.00  ? 346  ALA B CB  1 
ATOM   7516  N  N   . PHE B  1 347 ? 39.065  41.659  32.561  1.00 2.25  ? 347  PHE B N   1 
ATOM   7517  C  CA  . PHE B  1 347 ? 39.736  40.886  33.603  1.00 2.83  ? 347  PHE B CA  1 
ATOM   7518  C  C   . PHE B  1 347 ? 40.106  39.527  33.050  1.00 2.00  ? 347  PHE B C   1 
ATOM   7519  O  O   . PHE B  1 347 ? 40.424  38.610  33.795  1.00 2.10  ? 347  PHE B O   1 
ATOM   7520  C  CB  . PHE B  1 347 ? 38.816  40.717  34.826  1.00 2.00  ? 347  PHE B CB  1 
ATOM   7521  C  CG  . PHE B  1 347 ? 39.536  40.321  36.097  1.00 2.00  ? 347  PHE B CG  1 
ATOM   7522  C  CD1 . PHE B  1 347 ? 40.922  40.437  36.209  1.00 2.33  ? 347  PHE B CD1 1 
ATOM   7523  C  CD2 . PHE B  1 347 ? 38.824  39.868  37.190  1.00 2.00  ? 347  PHE B CD2 1 
ATOM   7524  C  CE1 . PHE B  1 347 ? 41.583  40.110  37.387  1.00 2.00  ? 347  PHE B CE1 1 
ATOM   7525  C  CE2 . PHE B  1 347 ? 39.475  39.541  38.368  1.00 2.00  ? 347  PHE B CE2 1 
ATOM   7526  C  CZ  . PHE B  1 347 ? 40.861  39.664  38.464  1.00 2.00  ? 347  PHE B CZ  1 
ATOM   7527  N  N   . ARG B  1 348 ? 40.073  39.398  31.735  1.00 2.00  ? 348  ARG B N   1 
ATOM   7528  C  CA  . ARG B  1 348 ? 40.388  38.126  31.132  1.00 2.00  ? 348  ARG B CA  1 
ATOM   7529  C  C   . ARG B  1 348 ? 41.847  38.075  30.748  1.00 2.00  ? 348  ARG B C   1 
ATOM   7530  O  O   . ARG B  1 348 ? 42.322  37.077  30.210  1.00 2.00  ? 348  ARG B O   1 
ATOM   7531  C  CB  . ARG B  1 348 ? 39.486  37.896  29.922  1.00 2.07  ? 348  ARG B CB  1 
ATOM   7532  C  CG  . ARG B  1 348 ? 38.003  37.850  30.276  1.00 2.00  ? 348  ARG B CG  1 
ATOM   7533  C  CD  . ARG B  1 348 ? 37.258  36.848  29.422  1.00 2.00  ? 348  ARG B CD  1 
ATOM   7534  N  NE  . ARG B  1 348 ? 35.812  37.017  29.496  1.00 2.00  ? 348  ARG B NE  1 
ATOM   7535  C  CZ  . ARG B  1 348 ? 34.943  36.265  28.830  1.00 2.00  ? 348  ARG B CZ  1 
ATOM   7536  N  NH1 . ARG B  1 348 ? 35.370  35.290  28.042  1.00 2.00  ? 348  ARG B NH1 1 
ATOM   7537  N  NH2 . ARG B  1 348 ? 33.645  36.488  28.941  1.00 2.00  ? 348  ARG B NH2 1 
ATOM   7538  N  N   . PHE B  1 349 ? 42.562  39.154  31.052  1.00 2.00  ? 349  PHE B N   1 
ATOM   7539  C  CA  . PHE B  1 349 ? 43.983  39.236  30.735  1.00 2.54  ? 349  PHE B CA  1 
ATOM   7540  C  C   . PHE B  1 349 ? 44.675  37.999  31.291  1.00 2.45  ? 349  PHE B C   1 
ATOM   7541  O  O   . PHE B  1 349 ? 45.592  37.455  30.677  1.00 2.00  ? 349  PHE B O   1 
ATOM   7542  C  CB  . PHE B  1 349 ? 44.598  40.518  31.322  1.00 2.00  ? 349  PHE B CB  1 
ATOM   7543  C  CG  . PHE B  1 349 ? 44.614  40.563  32.825  1.00 2.00  ? 349  PHE B CG  1 
ATOM   7544  C  CD1 . PHE B  1 349 ? 45.532  39.806  33.553  1.00 2.30  ? 349  PHE B CD1 1 
ATOM   7545  C  CD2 . PHE B  1 349 ? 43.715  41.365  33.519  1.00 2.29  ? 349  PHE B CD2 1 
ATOM   7546  C  CE1 . PHE B  1 349 ? 45.556  39.846  34.947  1.00 2.00  ? 349  PHE B CE1 1 
ATOM   7547  C  CE2 . PHE B  1 349 ? 43.731  41.413  34.920  1.00 2.73  ? 349  PHE B CE2 1 
ATOM   7548  C  CZ  . PHE B  1 349 ? 44.654  40.651  35.634  1.00 2.00  ? 349  PHE B CZ  1 
ATOM   7549  N  N   . GLY B  1 350 ? 44.211  37.551  32.451  1.00 2.00  ? 350  GLY B N   1 
ATOM   7550  C  CA  . GLY B  1 350 ? 44.792  36.380  33.065  1.00 2.00  ? 350  GLY B CA  1 
ATOM   7551  C  C   . GLY B  1 350 ? 44.952  35.261  32.061  1.00 2.11  ? 350  GLY B C   1 
ATOM   7552  O  O   . GLY B  1 350 ? 45.973  34.570  32.063  1.00 3.48  ? 350  GLY B O   1 
ATOM   7553  N  N   . HIS B  1 351 ? 43.962  35.080  31.189  1.00 2.44  ? 351  HIS B N   1 
ATOM   7554  C  CA  . HIS B  1 351 ? 44.035  34.013  30.192  1.00 2.46  ? 351  HIS B CA  1 
ATOM   7555  C  C   . HIS B  1 351 ? 45.393  33.946  29.511  1.00 2.79  ? 351  HIS B C   1 
ATOM   7556  O  O   . HIS B  1 351 ? 45.814  32.885  29.060  1.00 2.81  ? 351  HIS B O   1 
ATOM   7557  C  CB  . HIS B  1 351 ? 42.957  34.166  29.121  1.00 2.00  ? 351  HIS B CB  1 
ATOM   7558  C  CG  . HIS B  1 351 ? 41.579  33.761  29.658  1.00 2.15  ? 351  HIS B CG  1 
ATOM   7559  N  ND1 . HIS B  1 351 ? 40.410  34.052  28.991  1.00 2.68  ? 351  HIS B ND1 1 
ATOM   7560  C  CD2 . HIS B  1 351 ? 41.217  33.099  30.783  1.00 2.00  ? 351  HIS B CD2 1 
ATOM   7561  C  CE1 . HIS B  1 351 ? 39.384  33.591  29.688  1.00 2.75  ? 351  HIS B CE1 1 
ATOM   7562  N  NE2 . HIS B  1 351 ? 39.848  33.009  30.778  1.00 2.00  ? 351  HIS B NE2 1 
ATOM   7563  N  N   . MET B  1 352 ? 46.059  35.071  29.482  1.00 2.64  ? 352  MET B N   1 
ATOM   7564  C  CA  . MET B  1 352 ? 47.340  35.087  28.831  1.00 2.00  ? 352  MET B CA  1 
ATOM   7565  C  C   . MET B  1 352 ? 48.501  34.697  29.806  1.00 2.00  ? 352  MET B C   1 
ATOM   7566  O  O   . MET B  1 352 ? 49.655  34.680  29.391  1.00 2.00  ? 352  MET B O   1 
ATOM   7567  C  CB  . MET B  1 352 ? 47.486  36.416  28.072  1.00 2.38  ? 352  MET B CB  1 
ATOM   7568  C  CG  . MET B  1 352 ? 46.634  36.425  26.799  1.00 2.69  ? 352  MET B CG  1 
ATOM   7569  S  SD  . MET B  1 352 ? 46.720  37.976  25.876  1.00 5.62  ? 352  MET B SD  1 
ATOM   7570  C  CE  . MET B  1 352 ? 45.000  38.206  25.431  1.00 2.00  ? 352  MET B CE  1 
ATOM   7571  N  N   . GLU B  1 353 ? 48.195  34.394  31.055  1.00 2.00  ? 353  GLU B N   1 
ATOM   7572  C  CA  . GLU B  1 353 ? 49.277  34.096  32.020  1.00 2.00  ? 353  GLU B CA  1 
ATOM   7573  C  C   . GLU B  1 353 ? 49.295  32.635  32.466  1.00 2.16  ? 353  GLU B C   1 
ATOM   7574  O  O   . GLU B  1 353 ? 50.067  32.236  33.337  1.00 2.26  ? 353  GLU B O   1 
ATOM   7575  C  CB  . GLU B  1 353 ? 49.142  35.018  33.226  1.00 2.00  ? 353  GLU B CB  1 
ATOM   7576  C  CG  . GLU B  1 353 ? 48.642  36.406  32.868  1.00 2.00  ? 353  GLU B CG  1 
ATOM   7577  C  CD  . GLU B  1 353 ? 48.501  37.307  34.078  1.00 2.00  ? 353  GLU B CD  1 
ATOM   7578  O  OE1 . GLU B  1 353 ? 47.808  36.901  35.041  1.00 2.00  ? 353  GLU B OE1 1 
ATOM   7579  O  OE2 . GLU B  1 353 ? 49.077  38.411  34.058  1.00 2.49  ? 353  GLU B OE2 1 
ATOM   7580  N  N   . VAL B  1 354 ? 48.427  31.837  31.865  1.00 2.47  ? 354  VAL B N   1 
ATOM   7581  C  CA  . VAL B  1 354 ? 48.355  30.428  32.193  1.00 2.00  ? 354  VAL B CA  1 
ATOM   7582  C  C   . VAL B  1 354 ? 49.436  29.656  31.481  1.00 3.43  ? 354  VAL B C   1 
ATOM   7583  O  O   . VAL B  1 354 ? 49.479  29.635  30.248  1.00 4.04  ? 354  VAL B O   1 
ATOM   7584  C  CB  . VAL B  1 354 ? 47.075  29.831  31.734  1.00 2.28  ? 354  VAL B CB  1 
ATOM   7585  C  CG1 . VAL B  1 354 ? 47.018  28.392  32.206  1.00 3.10  ? 354  VAL B CG1 1 
ATOM   7586  C  CG2 . VAL B  1 354 ? 45.918  30.693  32.202  1.00 2.00  ? 354  VAL B CG2 1 
ATOM   7587  N  N   . PRO B  1 355 ? 50.299  28.975  32.242  1.00 2.00  ? 355  PRO B N   1 
ATOM   7588  C  CA  . PRO B  1 355 ? 51.405  28.178  31.711  1.00 2.00  ? 355  PRO B CA  1 
ATOM   7589  C  C   . PRO B  1 355 ? 50.854  26.942  31.022  1.00 2.00  ? 355  PRO B C   1 
ATOM   7590  O  O   . PRO B  1 355 ? 49.686  26.618  31.182  1.00 2.39  ? 355  PRO B O   1 
ATOM   7591  C  CB  . PRO B  1 355 ? 52.211  27.836  32.955  1.00 2.00  ? 355  PRO B CB  1 
ATOM   7592  C  CG  . PRO B  1 355 ? 51.793  28.891  33.961  1.00 2.40  ? 355  PRO B CG  1 
ATOM   7593  C  CD  . PRO B  1 355 ? 50.323  28.976  33.708  1.00 2.00  ? 355  PRO B CD  1 
ATOM   7594  N  N   . SER B  1 356 ? 51.693  26.245  30.266  1.00 2.09  ? 356  SER B N   1 
ATOM   7595  C  CA  . SER B  1 356 ? 51.261  25.058  29.533  1.00 2.00  ? 356  SER B CA  1 
ATOM   7596  C  C   . SER B  1 356 ? 51.377  23.758  30.310  1.00 2.00  ? 356  SER B C   1 
ATOM   7597  O  O   . SER B  1 356 ? 51.072  22.694  29.778  1.00 2.00  ? 356  SER B O   1 
ATOM   7598  C  CB  . SER B  1 356 ? 52.077  24.925  28.261  1.00 2.00  ? 356  SER B CB  1 
ATOM   7599  O  OG  . SER B  1 356 ? 53.444  24.785  28.600  1.00 3.85  ? 356  SER B OG  1 
ATOM   7600  N  N   . THR B  1 357 ? 51.823  23.839  31.559  1.00 2.11  ? 357  THR B N   1 
ATOM   7601  C  CA  . THR B  1 357 ? 51.977  22.649  32.383  1.00 2.00  ? 357  THR B CA  1 
ATOM   7602  C  C   . THR B  1 357 ? 51.851  22.947  33.865  1.00 2.00  ? 357  THR B C   1 
ATOM   7603  O  O   . THR B  1 357 ? 52.264  24.008  34.333  1.00 2.00  ? 357  THR B O   1 
ATOM   7604  C  CB  . THR B  1 357 ? 53.352  22.027  32.208  1.00 2.47  ? 357  THR B CB  1 
ATOM   7605  O  OG1 . THR B  1 357 ? 54.340  22.948  32.690  1.00 3.63  ? 357  THR B OG1 1 
ATOM   7606  C  CG2 . THR B  1 357 ? 53.620  21.719  30.761  1.00 3.44  ? 357  THR B CG2 1 
ATOM   7607  N  N   . VAL B  1 358 ? 51.295  21.985  34.596  1.00 2.00  ? 358  VAL B N   1 
ATOM   7608  C  CA  . VAL B  1 358 ? 51.148  22.079  36.043  1.00 2.00  ? 358  VAL B CA  1 
ATOM   7609  C  C   . VAL B  1 358 ? 51.994  20.962  36.660  1.00 2.00  ? 358  VAL B C   1 
ATOM   7610  O  O   . VAL B  1 358 ? 51.890  19.801  36.266  1.00 2.00  ? 358  VAL B O   1 
ATOM   7611  C  CB  . VAL B  1 358 ? 49.689  21.900  36.477  1.00 2.00  ? 358  VAL B CB  1 
ATOM   7612  C  CG1 . VAL B  1 358 ? 49.624  21.664  37.971  1.00 2.00  ? 358  VAL B CG1 1 
ATOM   7613  C  CG2 . VAL B  1 358 ? 48.889  23.130  36.114  1.00 2.00  ? 358  VAL B CG2 1 
ATOM   7614  N  N   . SER B  1 359 ? 52.839  21.311  37.624  1.00 2.28  ? 359  SER B N   1 
ATOM   7615  C  CA  . SER B  1 359 ? 53.694  20.312  38.248  1.00 2.00  ? 359  SER B CA  1 
ATOM   7616  C  C   . SER B  1 359 ? 53.427  20.070  39.728  1.00 2.00  ? 359  SER B C   1 
ATOM   7617  O  O   . SER B  1 359 ? 52.940  20.949  40.442  1.00 2.04  ? 359  SER B O   1 
ATOM   7618  C  CB  . SER B  1 359 ? 55.172  20.679  38.036  1.00 2.00  ? 359  SER B CB  1 
ATOM   7619  O  OG  . SER B  1 359 ? 55.348  22.071  37.821  1.00 3.26  ? 359  SER B OG  1 
ATOM   7620  N  N   . ARG B  1 360 ? 53.737  18.851  40.164  1.00 2.00  ? 360  ARG B N   1 
ATOM   7621  C  CA  . ARG B  1 360 ? 53.586  18.419  41.553  1.00 2.79  ? 360  ARG B CA  1 
ATOM   7622  C  C   . ARG B  1 360 ? 54.971  18.223  42.203  1.00 2.81  ? 360  ARG B C   1 
ATOM   7623  O  O   . ARG B  1 360 ? 55.777  17.419  41.726  1.00 2.95  ? 360  ARG B O   1 
ATOM   7624  C  CB  . ARG B  1 360 ? 52.815  17.093  41.617  1.00 2.39  ? 360  ARG B CB  1 
ATOM   7625  C  CG  . ARG B  1 360 ? 51.311  17.221  41.499  1.00 2.55  ? 360  ARG B CG  1 
ATOM   7626  C  CD  . ARG B  1 360 ? 50.823  17.167  40.066  1.00 3.95  ? 360  ARG B CD  1 
ATOM   7627  N  NE  . ARG B  1 360 ? 50.171  15.894  39.772  1.00 5.60  ? 360  ARG B NE  1 
ATOM   7628  C  CZ  . ARG B  1 360 ? 50.825  14.775  39.483  1.00 7.60  ? 360  ARG B CZ  1 
ATOM   7629  N  NH1 . ARG B  1 360 ? 52.152  14.778  39.443  1.00 7.81  ? 360  ARG B NH1 1 
ATOM   7630  N  NH2 . ARG B  1 360 ? 50.157  13.650  39.244  1.00 7.95  ? 360  ARG B NH2 1 
ATOM   7631  N  N   . LEU B  1 361 ? 55.245  18.945  43.288  1.00 2.54  ? 361  LEU B N   1 
ATOM   7632  C  CA  . LEU B  1 361 ? 56.533  18.828  43.979  1.00 3.35  ? 361  LEU B CA  1 
ATOM   7633  C  C   . LEU B  1 361 ? 56.387  18.000  45.251  1.00 3.15  ? 361  LEU B C   1 
ATOM   7634  O  O   . LEU B  1 361 ? 55.343  18.017  45.891  1.00 2.00  ? 361  LEU B O   1 
ATOM   7635  C  CB  . LEU B  1 361 ? 57.096  20.216  44.357  1.00 3.54  ? 361  LEU B CB  1 
ATOM   7636  C  CG  . LEU B  1 361 ? 57.330  21.250  43.260  1.00 3.39  ? 361  LEU B CG  1 
ATOM   7637  C  CD1 . LEU B  1 361 ? 57.919  22.526  43.834  1.00 2.00  ? 361  LEU B CD1 1 
ATOM   7638  C  CD2 . LEU B  1 361 ? 58.223  20.682  42.174  1.00 5.52  ? 361  LEU B CD2 1 
ATOM   7639  N  N   . ASP B  1 362 ? 57.413  17.266  45.654  1.00 3.88  ? 362  ASP B N   1 
ATOM   7640  C  CA  . ASP B  1 362 ? 57.363  16.403  46.854  1.00 6.05  ? 362  ASP B CA  1 
ATOM   7641  C  C   . ASP B  1 362 ? 57.997  17.124  48.025  1.00 6.26  ? 362  ASP B C   1 
ATOM   7642  O  O   . ASP B  1 362 ? 58.747  18.069  47.804  1.00 5.87  ? 362  ASP B O   1 
ATOM   7643  C  CB  . ASP B  1 362 ? 58.164  15.146  46.653  1.00 7.62  ? 362  ASP B CB  1 
ATOM   7644  C  CG  . ASP B  1 362 ? 59.636  15.440  46.793  1.00 9.26  ? 362  ASP B CG  1 
ATOM   7645  O  OD1 . ASP B  1 362 ? 60.400  14.473  47.036  1.00 8.52  ? 362  ASP B OD1 1 
ATOM   7646  O  OD2 . ASP B  1 362 ? 60.021  16.615  46.668  1.00 10.45 ? 362  ASP B OD2 1 
ATOM   7647  N  N   . GLU B  1 363 ? 57.709  16.790  49.280  1.00 6.38  ? 363  GLU B N   1 
ATOM   7648  C  CA  . GLU B  1 363 ? 58.168  17.579  50.444  1.00 8.51  ? 363  GLU B CA  1 
ATOM   7649  C  C   . GLU B  1 363 ? 59.402  18.552  50.369  1.00 8.98  ? 363  GLU B C   1 
ATOM   7650  O  O   . GLU B  1 363 ? 59.427  19.543  51.112  1.00 7.71  ? 363  GLU B O   1 
ATOM   7651  C  CB  . GLU B  1 363 ? 58.345  16.623  51.588  1.00 10.20 ? 363  GLU B CB  1 
ATOM   7652  C  CG  . GLU B  1 363 ? 57.045  16.479  52.349  1.00 11.94 ? 363  GLU B CG  1 
ATOM   7653  C  CD  . GLU B  1 363 ? 56.799  15.072  52.785  1.00 14.31 ? 363  GLU B CD  1 
ATOM   7654  O  OE1 . GLU B  1 363 ? 57.048  14.118  52.015  1.00 13.93 ? 363  GLU B OE1 1 
ATOM   7655  O  OE2 . GLU B  1 363 ? 56.336  14.895  53.939  1.00 15.70 ? 363  GLU B OE2 1 
ATOM   7656  N  N   . ASN B  1 364 ? 60.383  18.319  49.515  1.00 9.43  ? 364  ASN B N   1 
ATOM   7657  C  CA  . ASN B  1 364 ? 61.496  19.249  49.461  1.00 10.21 ? 364  ASN B CA  1 
ATOM   7658  C  C   . ASN B  1 364 ? 61.343  20.048  48.174  1.00 9.54  ? 364  ASN B C   1 
ATOM   7659  O  O   . ASN B  1 364 ? 62.298  20.614  47.647  1.00 10.06 ? 364  ASN B O   1 
ATOM   7660  C  CB  . ASN B  1 364 ? 62.829  18.497  49.497  1.00 11.79 ? 364  ASN B CB  1 
ATOM   7661  C  CG  . ASN B  1 364 ? 62.969  17.620  50.732  1.00 12.49 ? 364  ASN B CG  1 
ATOM   7662  O  OD1 . ASN B  1 364 ? 62.844  18.094  51.864  1.00 13.73 ? 364  ASN B OD1 1 
ATOM   7663  N  ND2 . ASN B  1 364 ? 63.227  16.335  50.518  1.00 11.25 ? 364  ASN B ND2 1 
ATOM   7664  N  N   . TYR B  1 365 ? 60.114  20.079  47.674  1.00 9.11  ? 365  TYR B N   1 
ATOM   7665  C  CA  . TYR B  1 365 ? 59.807  20.808  46.461  1.00 9.56  ? 365  TYR B CA  1 
ATOM   7666  C  C   . TYR B  1 365 ? 60.544  20.245  45.235  1.00 10.15 ? 365  TYR B C   1 
ATOM   7667  O  O   . TYR B  1 365 ? 60.833  20.964  44.280  1.00 10.88 ? 365  TYR B O   1 
ATOM   7668  C  CB  . TYR B  1 365 ? 60.130  22.291  46.678  1.00 7.01  ? 365  TYR B CB  1 
ATOM   7669  C  CG  . TYR B  1 365 ? 59.152  23.007  47.604  1.00 6.50  ? 365  TYR B CG  1 
ATOM   7670  C  CD1 . TYR B  1 365 ? 58.232  23.939  47.108  1.00 5.58  ? 365  TYR B CD1 1 
ATOM   7671  C  CD2 . TYR B  1 365 ? 59.158  22.773  48.974  1.00 6.43  ? 365  TYR B CD2 1 
ATOM   7672  C  CE1 . TYR B  1 365 ? 57.353  24.617  47.957  1.00 2.62  ? 365  TYR B CE1 1 
ATOM   7673  C  CE2 . TYR B  1 365 ? 58.280  23.452  49.828  1.00 4.91  ? 365  TYR B CE2 1 
ATOM   7674  C  CZ  . TYR B  1 365 ? 57.389  24.368  49.310  1.00 2.30  ? 365  TYR B CZ  1 
ATOM   7675  O  OH  . TYR B  1 365 ? 56.557  25.048  50.159  1.00 2.00  ? 365  TYR B OH  1 
ATOM   7676  N  N   . GLN B  1 366 ? 60.839  18.950  45.267  1.00 10.85 ? 366  GLN B N   1 
ATOM   7677  C  CA  . GLN B  1 366 ? 61.518  18.287  44.159  1.00 11.23 ? 366  GLN B CA  1 
ATOM   7678  C  C   . GLN B  1 366 ? 60.467  17.635  43.257  1.00 11.10 ? 366  GLN B C   1 
ATOM   7679  O  O   . GLN B  1 366 ? 59.500  17.057  43.751  1.00 9.97  ? 366  GLN B O   1 
ATOM   7680  C  CB  . GLN B  1 366 ? 62.474  17.232  44.706  1.00 14.63 ? 366  GLN B CB  1 
ATOM   7681  C  CG  . GLN B  1 366 ? 63.689  17.816  45.389  1.00 18.47 ? 366  GLN B CG  1 
ATOM   7682  C  CD  . GLN B  1 366 ? 64.632  18.470  44.398  1.00 20.86 ? 366  GLN B CD  1 
ATOM   7683  O  OE1 . GLN B  1 366 ? 64.231  19.351  43.636  1.00 22.49 ? 366  GLN B OE1 1 
ATOM   7684  N  NE2 . GLN B  1 366 ? 65.892  18.038  44.399  1.00 22.75 ? 366  GLN B NE2 1 
ATOM   7685  N  N   . PRO B  1 367 ? 60.638  17.717  41.923  1.00 10.36 ? 367  PRO B N   1 
ATOM   7686  C  CA  . PRO B  1 367 ? 59.637  17.101  41.044  1.00 8.38  ? 367  PRO B CA  1 
ATOM   7687  C  C   . PRO B  1 367 ? 59.458  15.627  41.411  1.00 10.82 ? 367  PRO B C   1 
ATOM   7688  O  O   . PRO B  1 367 ? 60.316  14.799  41.115  1.00 13.59 ? 367  PRO B O   1 
ATOM   7689  C  CB  . PRO B  1 367 ? 60.235  17.311  39.656  1.00 8.14  ? 367  PRO B CB  1 
ATOM   7690  C  CG  . PRO B  1 367 ? 61.709  17.256  39.920  1.00 7.22  ? 367  PRO B CG  1 
ATOM   7691  C  CD  . PRO B  1 367 ? 61.827  18.119  41.149  1.00 8.92  ? 367  PRO B CD  1 
ATOM   7692  N  N   . ARG B  1 368 ? 58.332  15.308  42.044  1.00 10.47 ? 368  ARG B N   1 
ATOM   7693  C  CA  . ARG B  1 368 ? 58.046  13.952  42.519  1.00 8.97  ? 368  ARG B CA  1 
ATOM   7694  C  C   . ARG B  1 368 ? 57.493  12.916  41.562  1.00 9.72  ? 368  ARG B C   1 
ATOM   7695  O  O   . ARG B  1 368 ? 56.407  13.079  41.012  1.00 10.52 ? 368  ARG B O   1 
ATOM   7696  C  CB  . ARG B  1 368 ? 57.072  14.015  43.688  1.00 9.09  ? 368  ARG B CB  1 
ATOM   7697  C  CG  . ARG B  1 368 ? 55.632  14.276  43.256  1.00 6.88  ? 368  ARG B CG  1 
ATOM   7698  C  CD  . ARG B  1 368 ? 54.742  14.523  44.448  1.00 7.80  ? 368  ARG B CD  1 
ATOM   7699  N  NE  . ARG B  1 368 ? 54.171  13.317  45.051  1.00 7.89  ? 368  ARG B NE  1 
ATOM   7700  C  CZ  . ARG B  1 368 ? 53.141  12.642  44.543  1.00 8.66  ? 368  ARG B CZ  1 
ATOM   7701  N  NH1 . ARG B  1 368 ? 52.578  13.044  43.409  1.00 7.95  ? 368  ARG B NH1 1 
ATOM   7702  N  NH2 . ARG B  1 368 ? 52.631  11.601  45.196  1.00 7.71  ? 368  ARG B NH2 1 
ATOM   7703  N  N   . GLY B  1 369 ? 58.221  11.821  41.396  1.00 10.64 ? 369  GLY B N   1 
ATOM   7704  C  CA  . GLY B  1 369 ? 57.721  10.755  40.550  1.00 12.89 ? 369  GLY B CA  1 
ATOM   7705  C  C   . GLY B  1 369 ? 57.936  10.856  39.056  1.00 13.03 ? 369  GLY B C   1 
ATOM   7706  O  O   . GLY B  1 369 ? 58.535  11.807  38.559  1.00 14.22 ? 369  GLY B O   1 
ATOM   7707  N  N   . PRO B  1 370 ? 57.440  9.861   38.309  1.00 12.83 ? 370  PRO B N   1 
ATOM   7708  C  CA  . PRO B  1 370 ? 57.557  9.790   36.853  1.00 11.93 ? 370  PRO B CA  1 
ATOM   7709  C  C   . PRO B  1 370 ? 56.626  10.747  36.125  1.00 10.95 ? 370  PRO B C   1 
ATOM   7710  O  O   . PRO B  1 370 ? 56.850  11.080  34.965  1.00 10.14 ? 370  PRO B O   1 
ATOM   7711  C  CB  . PRO B  1 370 ? 57.206  8.337   36.563  1.00 12.27 ? 370  PRO B CB  1 
ATOM   7712  C  CG  . PRO B  1 370 ? 56.135  8.077   37.559  1.00 12.24 ? 370  PRO B CG  1 
ATOM   7713  C  CD  . PRO B  1 370 ? 56.720  8.683   38.827  1.00 12.59 ? 370  PRO B CD  1 
ATOM   7714  N  N   . GLU B  1 371 ? 55.581  11.197  36.803  1.00 10.43 ? 371  GLU B N   1 
ATOM   7715  C  CA  . GLU B  1 371 ? 54.629  12.077  36.150  1.00 9.55  ? 371  GLU B CA  1 
ATOM   7716  C  C   . GLU B  1 371 ? 54.174  13.213  37.070  1.00 8.82  ? 371  GLU B C   1 
ATOM   7717  O  O   . GLU B  1 371 ? 52.983  13.367  37.363  1.00 8.42  ? 371  GLU B O   1 
ATOM   7718  C  CB  . GLU B  1 371 ? 53.445  11.228  35.678  1.00 9.34  ? 371  GLU B CB  1 
ATOM   7719  C  CG  . GLU B  1 371 ? 53.900  9.903   35.082  1.00 10.74 ? 371  GLU B CG  1 
ATOM   7720  C  CD  . GLU B  1 371 ? 52.771  8.912   34.882  1.00 13.10 ? 371  GLU B CD  1 
ATOM   7721  O  OE1 . GLU B  1 371 ? 51.878  8.848   35.755  1.00 14.70 ? 371  GLU B OE1 1 
ATOM   7722  O  OE2 . GLU B  1 371 ? 52.788  8.183   33.864  1.00 13.48 ? 371  GLU B OE2 1 
ATOM   7723  N  N   . ALA B  1 372 ? 55.133  14.015  37.517  1.00 6.22  ? 372  ALA B N   1 
ATOM   7724  C  CA  . ALA B  1 372 ? 54.820  15.124  38.399  1.00 5.32  ? 372  ALA B CA  1 
ATOM   7725  C  C   . ALA B  1 372 ? 54.464  16.327  37.568  1.00 4.28  ? 372  ALA B C   1 
ATOM   7726  O  O   . ALA B  1 372 ? 53.721  17.210  38.009  1.00 5.80  ? 372  ALA B O   1 
ATOM   7727  C  CB  . ALA B  1 372 ? 56.017  15.450  39.276  1.00 5.54  ? 372  ALA B CB  1 
ATOM   7728  N  N   . GLU B  1 373 ? 54.988  16.334  36.348  1.00 3.16  ? 373  GLU B N   1 
ATOM   7729  C  CA  . GLU B  1 373 ? 54.812  17.442  35.415  1.00 3.36  ? 373  GLU B CA  1 
ATOM   7730  C  C   . GLU B  1 373 ? 53.779  17.196  34.324  1.00 2.00  ? 373  GLU B C   1 
ATOM   7731  O  O   . GLU B  1 373 ? 54.125  16.683  33.270  1.00 3.08  ? 373  GLU B O   1 
ATOM   7732  C  CB  . GLU B  1 373 ? 56.163  17.714  34.785  1.00 2.51  ? 373  GLU B CB  1 
ATOM   7733  C  CG  . GLU B  1 373 ? 56.700  19.073  35.039  1.00 2.00  ? 373  GLU B CG  1 
ATOM   7734  C  CD  . GLU B  1 373 ? 56.654  19.861  33.792  1.00 2.00  ? 373  GLU B CD  1 
ATOM   7735  O  OE1 . GLU B  1 373 ? 55.532  20.070  33.283  1.00 2.00  ? 373  GLU B OE1 1 
ATOM   7736  O  OE2 . GLU B  1 373 ? 57.737  20.246  33.315  1.00 2.29  ? 373  GLU B OE2 1 
ATOM   7737  N  N   . LEU B  1 374 ? 52.528  17.590  34.547  1.00 2.00  ? 374  LEU B N   1 
ATOM   7738  C  CA  . LEU B  1 374 ? 51.481  17.333  33.553  1.00 2.43  ? 374  LEU B CA  1 
ATOM   7739  C  C   . LEU B  1 374 ? 51.126  18.515  32.628  1.00 3.11  ? 374  LEU B C   1 
ATOM   7740  O  O   . LEU B  1 374 ? 51.266  19.685  32.999  1.00 3.86  ? 374  LEU B O   1 
ATOM   7741  C  CB  . LEU B  1 374 ? 50.204  16.827  34.262  1.00 2.00  ? 374  LEU B CB  1 
ATOM   7742  C  CG  . LEU B  1 374 ? 50.298  15.788  35.401  1.00 2.00  ? 374  LEU B CG  1 
ATOM   7743  C  CD1 . LEU B  1 374 ? 48.900  15.414  35.900  1.00 2.00  ? 374  LEU B CD1 1 
ATOM   7744  C  CD2 . LEU B  1 374 ? 51.021  14.550  34.925  1.00 2.00  ? 374  LEU B CD2 1 
ATOM   7745  N  N   . PRO B  1 375 ? 50.520  18.156  31.478  1.00 2.03  ? 375  PRO B N   1 
ATOM   7746  C  CA  . PRO B  1 375 ? 50.030  19.139  30.465  1.00 2.71  ? 375  PRO B CA  1 
ATOM   7747  C  C   . PRO B  1 375 ? 48.868  19.922  30.937  1.00 2.00  ? 375  PRO B C   1 
ATOM   7748  O  O   . PRO B  1 375 ? 47.882  19.288  31.287  1.00 2.00  ? 375  PRO B O   1 
ATOM   7749  C  CB  . PRO B  1 375 ? 49.540  18.299  29.344  1.00 2.17  ? 375  PRO B CB  1 
ATOM   7750  C  CG  . PRO B  1 375 ? 50.594  17.238  29.307  1.00 2.00  ? 375  PRO B CG  1 
ATOM   7751  C  CD  . PRO B  1 375 ? 51.243  17.172  30.649  1.00 2.35  ? 375  PRO B CD  1 
ATOM   7752  N  N   . LEU B  1 376 ? 48.859  21.234  30.968  1.00 2.07  ? 376  LEU B N   1 
ATOM   7753  C  CA  . LEU B  1 376 ? 47.646  21.912  31.357  1.00 2.43  ? 376  LEU B CA  1 
ATOM   7754  C  C   . LEU B  1 376 ? 46.377  21.271  30.783  1.00 2.17  ? 376  LEU B C   1 
ATOM   7755  O  O   . LEU B  1 376 ? 45.335  21.201  31.450  1.00 2.00  ? 376  LEU B O   1 
ATOM   7756  C  CB  . LEU B  1 376 ? 47.746  23.348  30.817  1.00 2.00  ? 376  LEU B CB  1 
ATOM   7757  C  CG  . LEU B  1 376 ? 46.854  24.355  31.491  1.00 2.00  ? 376  LEU B CG  1 
ATOM   7758  C  CD1 . LEU B  1 376 ? 45.557  24.521  30.728  1.00 2.00  ? 376  LEU B CD1 1 
ATOM   7759  C  CD2 . LEU B  1 376 ? 46.582  23.961  32.935  1.00 2.00  ? 376  LEU B CD2 1 
ATOM   7760  N  N   . HIS B  1 377 ? 46.473  20.827  29.552  1.00 2.68  ? 377  HIS B N   1 
ATOM   7761  C  CA  . HIS B  1 377 ? 45.281  20.338  28.883  1.00 3.45  ? 377  HIS B CA  1 
ATOM   7762  C  C   . HIS B  1 377 ? 44.618  19.104  29.475  1.00 2.00  ? 377  HIS B C   1 
ATOM   7763  O  O   . HIS B  1 377 ? 43.416  18.919  29.300  1.00 2.45  ? 377  HIS B O   1 
ATOM   7764  C  CB  . HIS B  1 377 ? 45.590  20.190  27.408  1.00 2.18  ? 377  HIS B CB  1 
ATOM   7765  C  CG  . HIS B  1 377 ? 45.803  18.748  26.949  1.00 2.00  ? 377  HIS B CG  1 
ATOM   7766  N  ND1 . HIS B  1 377 ? 46.843  18.405  26.115  1.00 2.00  ? 377  HIS B ND1 1 
ATOM   7767  C  CD2 . HIS B  1 377 ? 45.111  17.608  27.178  1.00 2.00  ? 377  HIS B CD2 1 
ATOM   7768  C  CE1 . HIS B  1 377 ? 46.783  17.113  25.850  1.00 2.91  ? 377  HIS B CE1 1 
ATOM   7769  N  NE2 . HIS B  1 377 ? 45.741  16.605  26.483  1.00 2.00  ? 377  HIS B NE2 1 
ATOM   7770  N  N   . THR B  1 378 ? 45.372  18.264  30.174  1.00 2.00  ? 378  THR B N   1 
ATOM   7771  C  CA  . THR B  1 378 ? 44.770  17.067  30.758  1.00 2.44  ? 378  THR B CA  1 
ATOM   7772  C  C   . THR B  1 378 ? 44.339  17.314  32.199  1.00 2.37  ? 378  THR B C   1 
ATOM   7773  O  O   . THR B  1 378 ? 44.202  16.372  32.978  1.00 2.00  ? 378  THR B O   1 
ATOM   7774  C  CB  . THR B  1 378 ? 45.744  15.872  30.746  1.00 2.00  ? 378  THR B CB  1 
ATOM   7775  O  OG1 . THR B  1 378 ? 46.664  15.980  31.840  1.00 2.00  ? 378  THR B OG1 1 
ATOM   7776  C  CG2 . THR B  1 378 ? 46.523  15.848  29.449  1.00 3.15  ? 378  THR B CG2 1 
ATOM   7777  N  N   . LEU B  1 379 ? 44.116  18.579  32.545  1.00 2.11  ? 379  LEU B N   1 
ATOM   7778  C  CA  . LEU B  1 379 ? 43.726  18.940  33.904  1.00 2.00  ? 379  LEU B CA  1 
ATOM   7779  C  C   . LEU B  1 379 ? 42.383  19.674  34.057  1.00 2.61  ? 379  LEU B C   1 
ATOM   7780  O  O   . LEU B  1 379 ? 42.003  19.999  35.180  1.00 2.01  ? 379  LEU B O   1 
ATOM   7781  C  CB  . LEU B  1 379 ? 44.834  19.776  34.553  1.00 2.00  ? 379  LEU B CB  1 
ATOM   7782  C  CG  . LEU B  1 379 ? 46.190  19.113  34.795  1.00 2.00  ? 379  LEU B CG  1 
ATOM   7783  C  CD1 . LEU B  1 379 ? 47.186  20.175  35.181  1.00 2.00  ? 379  LEU B CD1 1 
ATOM   7784  C  CD2 . LEU B  1 379 ? 46.086  18.060  35.880  1.00 2.00  ? 379  LEU B CD2 1 
ATOM   7785  N  N   . PHE B  1 380 ? 41.671  19.944  32.955  1.00 2.92  ? 380  PHE B N   1 
ATOM   7786  C  CA  . PHE B  1 380 ? 40.369  20.629  33.031  1.00 2.00  ? 380  PHE B CA  1 
ATOM   7787  C  C   . PHE B  1 380 ? 39.324  19.650  33.519  1.00 2.37  ? 380  PHE B C   1 
ATOM   7788  O  O   . PHE B  1 380 ? 39.202  18.549  32.985  1.00 4.20  ? 380  PHE B O   1 
ATOM   7789  C  CB  . PHE B  1 380 ? 39.901  21.155  31.672  1.00 2.00  ? 380  PHE B CB  1 
ATOM   7790  C  CG  . PHE B  1 380 ? 40.903  21.997  30.974  1.00 2.00  ? 380  PHE B CG  1 
ATOM   7791  C  CD1 . PHE B  1 380 ? 41.587  22.988  31.655  1.00 2.00  ? 380  PHE B CD1 1 
ATOM   7792  C  CD2 . PHE B  1 380 ? 41.183  21.782  29.633  1.00 2.32  ? 380  PHE B CD2 1 
ATOM   7793  C  CE1 . PHE B  1 380 ? 42.539  23.750  31.019  1.00 2.00  ? 380  PHE B CE1 1 
ATOM   7794  C  CE2 . PHE B  1 380 ? 42.136  22.542  28.982  1.00 2.64  ? 380  PHE B CE2 1 
ATOM   7795  C  CZ  . PHE B  1 380 ? 42.818  23.529  29.678  1.00 2.38  ? 380  PHE B CZ  1 
ATOM   7796  N  N   . PHE B  1 381 ? 38.556  20.056  34.521  1.00 3.17  ? 381  PHE B N   1 
ATOM   7797  C  CA  . PHE B  1 381 ? 37.528  19.195  35.084  1.00 2.00  ? 381  PHE B CA  1 
ATOM   7798  C  C   . PHE B  1 381 ? 38.149  17.903  35.546  1.00 2.00  ? 381  PHE B C   1 
ATOM   7799  O  O   . PHE B  1 381 ? 37.599  16.828  35.345  1.00 2.00  ? 381  PHE B O   1 
ATOM   7800  C  CB  . PHE B  1 381 ? 36.459  18.918  34.044  1.00 2.00  ? 381  PHE B CB  1 
ATOM   7801  C  CG  . PHE B  1 381 ? 35.710  20.132  33.651  1.00 2.51  ? 381  PHE B CG  1 
ATOM   7802  C  CD1 . PHE B  1 381 ? 34.828  20.727  34.541  1.00 3.29  ? 381  PHE B CD1 1 
ATOM   7803  C  CD2 . PHE B  1 381 ? 35.927  20.721  32.422  1.00 2.79  ? 381  PHE B CD2 1 
ATOM   7804  C  CE1 . PHE B  1 381 ? 34.174  21.895  34.214  1.00 4.18  ? 381  PHE B CE1 1 
ATOM   7805  C  CE2 . PHE B  1 381 ? 35.280  21.890  32.084  1.00 4.54  ? 381  PHE B CE2 1 
ATOM   7806  C  CZ  . PHE B  1 381 ? 34.401  22.480  32.986  1.00 4.65  ? 381  PHE B CZ  1 
ATOM   7807  N  N   . ASN B  1 382 ? 39.309  18.025  36.173  1.00 2.00  ? 382  ASN B N   1 
ATOM   7808  C  CA  . ASN B  1 382 ? 40.028  16.873  36.674  1.00 2.00  ? 382  ASN B CA  1 
ATOM   7809  C  C   . ASN B  1 382 ? 40.142  16.912  38.195  1.00 3.36  ? 382  ASN B C   1 
ATOM   7810  O  O   . ASN B  1 382 ? 40.766  17.813  38.760  1.00 3.87  ? 382  ASN B O   1 
ATOM   7811  C  CB  . ASN B  1 382 ? 41.420  16.825  36.060  1.00 2.00  ? 382  ASN B CB  1 
ATOM   7812  C  CG  . ASN B  1 382 ? 42.143  15.560  36.400  1.00 2.00  ? 382  ASN B CG  1 
ATOM   7813  O  OD1 . ASN B  1 382 ? 42.310  15.227  37.569  1.00 2.35  ? 382  ASN B OD1 1 
ATOM   7814  N  ND2 . ASN B  1 382 ? 42.575  14.837  35.382  1.00 2.00  ? 382  ASN B ND2 1 
ATOM   7815  N  N   . THR B  1 383 ? 39.532  15.934  38.854  1.00 2.43  ? 383  THR B N   1 
ATOM   7816  C  CA  . THR B  1 383 ? 39.583  15.851  40.306  1.00 2.00  ? 383  THR B CA  1 
ATOM   7817  C  C   . THR B  1 383 ? 40.274  14.570  40.750  1.00 5.15  ? 383  THR B C   1 
ATOM   7818  O  O   . THR B  1 383 ? 40.818  14.512  41.858  1.00 5.23  ? 383  THR B O   1 
ATOM   7819  C  CB  . THR B  1 383 ? 38.181  15.858  40.927  1.00 2.00  ? 383  THR B CB  1 
ATOM   7820  O  OG1 . THR B  1 383 ? 37.335  14.961  40.198  1.00 2.34  ? 383  THR B OG1 1 
ATOM   7821  C  CG2 . THR B  1 383 ? 37.593  17.251  40.908  1.00 2.18  ? 383  THR B CG2 1 
ATOM   7822  N  N   . TRP B  1 384 ? 40.257  13.543  39.897  1.00 3.47  ? 384  TRP B N   1 
ATOM   7823  C  CA  . TRP B  1 384 ? 40.880  12.284  40.271  1.00 2.00  ? 384  TRP B CA  1 
ATOM   7824  C  C   . TRP B  1 384 ? 42.360  12.462  40.496  1.00 2.00  ? 384  TRP B C   1 
ATOM   7825  O  O   . TRP B  1 384 ? 42.938  11.814  41.362  1.00 2.04  ? 384  TRP B O   1 
ATOM   7826  C  CB  . TRP B  1 384 ? 40.625  11.195  39.236  1.00 2.51  ? 384  TRP B CB  1 
ATOM   7827  C  CG  . TRP B  1 384 ? 41.443  11.241  37.992  1.00 2.79  ? 384  TRP B CG  1 
ATOM   7828  C  CD1 . TRP B  1 384 ? 41.076  11.779  36.792  1.00 3.96  ? 384  TRP B CD1 1 
ATOM   7829  C  CD2 . TRP B  1 384 ? 42.702  10.604  37.774  1.00 2.00  ? 384  TRP B CD2 1 
ATOM   7830  N  NE1 . TRP B  1 384 ? 42.022  11.501  35.834  1.00 2.70  ? 384  TRP B NE1 1 
ATOM   7831  C  CE2 . TRP B  1 384 ? 43.034  10.781  36.412  1.00 2.00  ? 384  TRP B CE2 1 
ATOM   7832  C  CE3 . TRP B  1 384 ? 43.582  9.896   38.593  1.00 2.00  ? 384  TRP B CE3 1 
ATOM   7833  C  CZ2 . TRP B  1 384 ? 44.209  10.272  35.851  1.00 2.10  ? 384  TRP B CZ2 1 
ATOM   7834  C  CZ3 . TRP B  1 384 ? 44.752  9.390   38.036  1.00 3.11  ? 384  TRP B CZ3 1 
ATOM   7835  C  CH2 . TRP B  1 384 ? 45.053  9.582   36.677  1.00 2.32  ? 384  TRP B CH2 1 
ATOM   7836  N  N   . ARG B  1 385 ? 42.981  13.347  39.732  1.00 2.00  ? 385  ARG B N   1 
ATOM   7837  C  CA  . ARG B  1 385 ? 44.395  13.598  39.935  1.00 2.35  ? 385  ARG B CA  1 
ATOM   7838  C  C   . ARG B  1 385 ? 44.580  14.175  41.326  1.00 2.00  ? 385  ARG B C   1 
ATOM   7839  O  O   . ARG B  1 385 ? 45.701  14.315  41.798  1.00 2.13  ? 385  ARG B O   1 
ATOM   7840  C  CB  . ARG B  1 385 ? 44.936  14.571  38.894  1.00 2.81  ? 385  ARG B CB  1 
ATOM   7841  C  CG  . ARG B  1 385 ? 45.324  13.899  37.591  1.00 4.40  ? 385  ARG B CG  1 
ATOM   7842  C  CD  . ARG B  1 385 ? 46.486  12.943  37.796  1.00 4.96  ? 385  ARG B CD  1 
ATOM   7843  N  NE  . ARG B  1 385 ? 46.857  12.267  36.558  1.00 5.43  ? 385  ARG B NE  1 
ATOM   7844  C  CZ  . ARG B  1 385 ? 48.047  11.719  36.342  1.00 5.80  ? 385  ARG B CZ  1 
ATOM   7845  N  NH1 . ARG B  1 385 ? 48.982  11.773  37.284  1.00 6.64  ? 385  ARG B NH1 1 
ATOM   7846  N  NH2 . ARG B  1 385 ? 48.302  11.119  35.186  1.00 5.00  ? 385  ARG B NH2 1 
ATOM   7847  N  N   . ILE B  1 386 ? 43.480  14.523  41.983  1.00 2.00  ? 386  ILE B N   1 
ATOM   7848  C  CA  . ILE B  1 386 ? 43.585  15.055  43.332  1.00 3.05  ? 386  ILE B CA  1 
ATOM   7849  C  C   . ILE B  1 386 ? 43.236  13.980  44.336  1.00 3.46  ? 386  ILE B C   1 
ATOM   7850  O  O   . ILE B  1 386 ? 44.062  13.626  45.175  1.00 6.39  ? 386  ILE B O   1 
ATOM   7851  C  CB  . ILE B  1 386 ? 42.632  16.223  43.614  1.00 2.18  ? 386  ILE B CB  1 
ATOM   7852  C  CG1 . ILE B  1 386 ? 42.996  17.448  42.785  1.00 2.00  ? 386  ILE B CG1 1 
ATOM   7853  C  CG2 . ILE B  1 386 ? 42.721  16.584  45.085  1.00 2.00  ? 386  ILE B CG2 1 
ATOM   7854  C  CD1 . ILE B  1 386 ? 42.039  18.614  42.990  1.00 2.00  ? 386  ILE B CD1 1 
ATOM   7855  N  N   . ILE B  1 387 ? 42.007  13.475  44.256  1.00 2.00  ? 387  ILE B N   1 
ATOM   7856  C  CA  . ILE B  1 387 ? 41.531  12.446  45.176  1.00 2.00  ? 387  ILE B CA  1 
ATOM   7857  C  C   . ILE B  1 387 ? 42.466  11.256  45.246  1.00 2.45  ? 387  ILE B C   1 
ATOM   7858  O  O   . ILE B  1 387 ? 42.872  10.827  46.329  1.00 2.37  ? 387  ILE B O   1 
ATOM   7859  C  CB  . ILE B  1 387 ? 40.173  11.883  44.750  1.00 2.42  ? 387  ILE B CB  1 
ATOM   7860  C  CG1 . ILE B  1 387 ? 39.107  12.986  44.755  1.00 2.92  ? 387  ILE B CG1 1 
ATOM   7861  C  CG2 . ILE B  1 387 ? 39.820  10.690  45.640  1.00 2.00  ? 387  ILE B CG2 1 
ATOM   7862  C  CD1 . ILE B  1 387 ? 38.780  13.574  46.116  1.00 2.00  ? 387  ILE B CD1 1 
ATOM   7863  N  N   . LYS B  1 388 ? 42.789  10.737  44.062  1.00 3.86  ? 388  LYS B N   1 
ATOM   7864  C  CA  . LYS B  1 388 ? 43.637  9.562   43.891  1.00 2.45  ? 388  LYS B CA  1 
ATOM   7865  C  C   . LYS B  1 388 ? 45.103  9.802   43.525  1.00 2.00  ? 388  LYS B C   1 
ATOM   7866  O  O   . LYS B  1 388 ? 45.713  8.969   42.854  1.00 2.09  ? 388  LYS B O   1 
ATOM   7867  C  CB  . LYS B  1 388 ? 43.023  8.666   42.819  1.00 2.00  ? 388  LYS B CB  1 
ATOM   7868  C  CG  . LYS B  1 388 ? 41.600  8.262   43.080  1.00 2.00  ? 388  LYS B CG  1 
ATOM   7869  C  CD  . LYS B  1 388 ? 41.221  7.136   42.147  1.00 4.47  ? 388  LYS B CD  1 
ATOM   7870  C  CE  . LYS B  1 388 ? 39.868  6.561   42.507  1.00 6.72  ? 388  LYS B CE  1 
ATOM   7871  N  NZ  . LYS B  1 388 ? 39.801  6.167   43.948  1.00 9.46  ? 388  LYS B NZ  1 
ATOM   7872  N  N   . ASP B  1 389 ? 45.687  10.912  43.953  1.00 2.05  ? 389  ASP B N   1 
ATOM   7873  C  CA  . ASP B  1 389 ? 47.076  11.153  43.599  1.00 2.95  ? 389  ASP B CA  1 
ATOM   7874  C  C   . ASP B  1 389 ? 47.771  12.182  44.480  1.00 3.31  ? 389  ASP B C   1 
ATOM   7875  O  O   . ASP B  1 389 ? 48.062  13.293  44.040  1.00 4.45  ? 389  ASP B O   1 
ATOM   7876  C  CB  . ASP B  1 389 ? 47.161  11.573  42.123  1.00 4.34  ? 389  ASP B CB  1 
ATOM   7877  C  CG  . ASP B  1 389 ? 48.314  10.898  41.380  1.00 5.08  ? 389  ASP B CG  1 
ATOM   7878  O  OD1 . ASP B  1 389 ? 48.494  9.674   41.570  1.00 6.20  ? 389  ASP B OD1 1 
ATOM   7879  O  OD2 . ASP B  1 389 ? 49.027  11.580  40.600  1.00 5.16  ? 389  ASP B OD2 1 
ATOM   7880  N  N   . GLY B  1 390 ? 48.018  11.812  45.733  1.00 3.53  ? 390  GLY B N   1 
ATOM   7881  C  CA  . GLY B  1 390 ? 48.724  12.694  46.648  1.00 4.09  ? 390  GLY B CA  1 
ATOM   7882  C  C   . GLY B  1 390 ? 48.007  13.848  47.321  1.00 3.52  ? 390  GLY B C   1 
ATOM   7883  O  O   . GLY B  1 390 ? 48.627  14.585  48.085  1.00 4.13  ? 390  GLY B O   1 
ATOM   7884  N  N   . GLY B  1 391 ? 46.717  14.023  47.062  1.00 3.87  ? 391  GLY B N   1 
ATOM   7885  C  CA  . GLY B  1 391 ? 46.012  15.122  47.702  1.00 4.31  ? 391  GLY B CA  1 
ATOM   7886  C  C   . GLY B  1 391 ? 46.345  16.435  47.026  1.00 4.61  ? 391  GLY B C   1 
ATOM   7887  O  O   . GLY B  1 391 ? 46.797  16.436  45.880  1.00 6.00  ? 391  GLY B O   1 
ATOM   7888  N  N   . ILE B  1 392 ? 46.148  17.555  47.713  1.00 2.80  ? 392  ILE B N   1 
ATOM   7889  C  CA  . ILE B  1 392 ? 46.433  18.836  47.082  1.00 3.47  ? 392  ILE B CA  1 
ATOM   7890  C  C   . ILE B  1 392 ? 47.676  19.525  47.635  1.00 2.44  ? 392  ILE B C   1 
ATOM   7891  O  O   . ILE B  1 392 ? 48.055  20.620  47.204  1.00 2.00  ? 392  ILE B O   1 
ATOM   7892  C  CB  . ILE B  1 392 ? 45.182  19.772  47.151  1.00 4.34  ? 392  ILE B CB  1 
ATOM   7893  C  CG1 . ILE B  1 392 ? 45.281  20.795  48.304  1.00 4.98  ? 392  ILE B CG1 1 
ATOM   7894  C  CG2 . ILE B  1 392 ? 43.934  18.911  47.242  1.00 3.44  ? 392  ILE B CG2 1 
ATOM   7895  C  CD1 . ILE B  1 392 ? 45.323  20.225  49.708  1.00 5.79  ? 392  ILE B CD1 1 
ATOM   7896  N  N   . ASP B  1 393 ? 48.322  18.862  48.581  1.00 2.47  ? 393  ASP B N   1 
ATOM   7897  C  CA  . ASP B  1 393 ? 49.531  19.393  49.177  1.00 3.07  ? 393  ASP B CA  1 
ATOM   7898  C  C   . ASP B  1 393 ? 50.614  19.557  48.136  1.00 4.57  ? 393  ASP B C   1 
ATOM   7899  O  O   . ASP B  1 393 ? 51.284  20.586  48.095  1.00 7.57  ? 393  ASP B O   1 
ATOM   7900  C  CB  . ASP B  1 393 ? 50.013  18.472  50.277  1.00 4.59  ? 393  ASP B CB  1 
ATOM   7901  C  CG  . ASP B  1 393 ? 49.612  18.959  51.629  1.00 5.67  ? 393  ASP B CG  1 
ATOM   7902  O  OD1 . ASP B  1 393 ? 48.567  19.644  51.727  1.00 5.21  ? 393  ASP B OD1 1 
ATOM   7903  O  OD2 . ASP B  1 393 ? 50.343  18.653  52.590  1.00 7.91  ? 393  ASP B OD2 1 
ATOM   7904  N  N   . PRO B  1 394 ? 50.825  18.534  47.290  1.00 5.40  ? 394  PRO B N   1 
ATOM   7905  C  CA  . PRO B  1 394 ? 51.858  18.644  46.254  1.00 3.86  ? 394  PRO B CA  1 
ATOM   7906  C  C   . PRO B  1 394 ? 51.499  19.658  45.160  1.00 3.53  ? 394  PRO B C   1 
ATOM   7907  O  O   . PRO B  1 394 ? 52.374  20.104  44.417  1.00 3.50  ? 394  PRO B O   1 
ATOM   7908  C  CB  . PRO B  1 394 ? 51.969  17.214  45.718  1.00 3.32  ? 394  PRO B CB  1 
ATOM   7909  C  CG  . PRO B  1 394 ? 50.601  16.642  45.965  1.00 3.34  ? 394  PRO B CG  1 
ATOM   7910  C  CD  . PRO B  1 394 ? 50.297  17.159  47.352  1.00 4.87  ? 394  PRO B CD  1 
ATOM   7911  N  N   . LEU B  1 395 ? 50.217  20.013  45.060  1.00 2.93  ? 395  LEU B N   1 
ATOM   7912  C  CA  . LEU B  1 395 ? 49.777  20.987  44.065  1.00 2.94  ? 395  LEU B CA  1 
ATOM   7913  C  C   . LEU B  1 395 ? 49.994  22.405  44.626  1.00 3.33  ? 395  LEU B C   1 
ATOM   7914  O  O   . LEU B  1 395 ? 50.440  23.307  43.907  1.00 4.12  ? 395  LEU B O   1 
ATOM   7915  C  CB  . LEU B  1 395 ? 48.299  20.764  43.695  1.00 2.00  ? 395  LEU B CB  1 
ATOM   7916  C  CG  . LEU B  1 395 ? 47.863  19.542  42.872  1.00 2.00  ? 395  LEU B CG  1 
ATOM   7917  C  CD1 . LEU B  1 395 ? 46.365  19.568  42.703  1.00 2.00  ? 395  LEU B CD1 1 
ATOM   7918  C  CD2 . LEU B  1 395 ? 48.509  19.549  41.516  1.00 2.00  ? 395  LEU B CD2 1 
ATOM   7919  N  N   . VAL B  1 396 ? 49.686  22.595  45.908  1.00 2.00  ? 396  VAL B N   1 
ATOM   7920  C  CA  . VAL B  1 396 ? 49.882  23.889  46.553  1.00 2.00  ? 396  VAL B CA  1 
ATOM   7921  C  C   . VAL B  1 396 ? 51.360  24.275  46.511  1.00 2.80  ? 396  VAL B C   1 
ATOM   7922  O  O   . VAL B  1 396 ? 51.704  25.455  46.432  1.00 3.48  ? 396  VAL B O   1 
ATOM   7923  C  CB  . VAL B  1 396 ? 49.404  23.854  48.017  1.00 2.00  ? 396  VAL B CB  1 
ATOM   7924  C  CG1 . VAL B  1 396 ? 50.073  24.946  48.828  1.00 2.00  ? 396  VAL B CG1 1 
ATOM   7925  C  CG2 . VAL B  1 396 ? 47.909  24.027  48.053  1.00 2.65  ? 396  VAL B CG2 1 
ATOM   7926  N  N   . ARG B  1 397 ? 52.239  23.283  46.568  1.00 2.76  ? 397  ARG B N   1 
ATOM   7927  C  CA  . ARG B  1 397 ? 53.656  23.582  46.522  1.00 3.28  ? 397  ARG B CA  1 
ATOM   7928  C  C   . ARG B  1 397 ? 53.973  24.084  45.133  1.00 2.24  ? 397  ARG B C   1 
ATOM   7929  O  O   . ARG B  1 397 ? 54.700  25.057  44.967  1.00 2.89  ? 397  ARG B O   1 
ATOM   7930  C  CB  . ARG B  1 397 ? 54.488  22.342  46.825  1.00 5.80  ? 397  ARG B CB  1 
ATOM   7931  C  CG  . ARG B  1 397 ? 54.444  21.898  48.274  1.00 8.41  ? 397  ARG B CG  1 
ATOM   7932  C  CD  . ARG B  1 397 ? 55.805  21.378  48.715  1.00 9.39  ? 397  ARG B CD  1 
ATOM   7933  N  NE  . ARG B  1 397 ? 55.693  20.488  49.862  1.00 10.93 ? 397  ARG B NE  1 
ATOM   7934  C  CZ  . ARG B  1 397 ? 55.042  19.330  49.833  1.00 12.18 ? 397  ARG B CZ  1 
ATOM   7935  N  NH1 . ARG B  1 397 ? 54.447  18.927  48.717  1.00 12.80 ? 397  ARG B NH1 1 
ATOM   7936  N  NH2 . ARG B  1 397 ? 54.988  18.570  50.918  1.00 14.01 ? 397  ARG B NH2 1 
ATOM   7937  N  N   . GLY B  1 398 ? 53.422  23.412  44.133  1.00 2.00  ? 398  GLY B N   1 
ATOM   7938  C  CA  . GLY B  1 398 ? 53.651  23.834  42.768  1.00 2.19  ? 398  GLY B CA  1 
ATOM   7939  C  C   . GLY B  1 398 ? 53.382  25.319  42.655  1.00 2.72  ? 398  GLY B C   1 
ATOM   7940  O  O   . GLY B  1 398 ? 54.241  26.084  42.214  1.00 3.66  ? 398  GLY B O   1 
ATOM   7941  N  N   . LEU B  1 399 ? 52.189  25.728  43.077  1.00 3.39  ? 399  LEU B N   1 
ATOM   7942  C  CA  . LEU B  1 399 ? 51.782  27.133  43.034  1.00 3.67  ? 399  LEU B CA  1 
ATOM   7943  C  C   . LEU B  1 399 ? 52.758  28.080  43.739  1.00 3.59  ? 399  LEU B C   1 
ATOM   7944  O  O   . LEU B  1 399 ? 52.954  29.221  43.317  1.00 4.72  ? 399  LEU B O   1 
ATOM   7945  C  CB  . LEU B  1 399 ? 50.387  27.292  43.647  1.00 2.49  ? 399  LEU B CB  1 
ATOM   7946  C  CG  . LEU B  1 399 ? 49.198  27.010  42.732  1.00 2.00  ? 399  LEU B CG  1 
ATOM   7947  C  CD1 . LEU B  1 399 ? 47.998  26.643  43.577  1.00 2.00  ? 399  LEU B CD1 1 
ATOM   7948  C  CD2 . LEU B  1 399 ? 48.921  28.224  41.862  1.00 2.00  ? 399  LEU B CD2 1 
ATOM   7949  N  N   . LEU B  1 400 ? 53.374  27.620  44.815  1.00 3.25  ? 400  LEU B N   1 
ATOM   7950  C  CA  . LEU B  1 400 ? 54.296  28.482  45.518  1.00 2.00  ? 400  LEU B CA  1 
ATOM   7951  C  C   . LEU B  1 400 ? 55.664  28.568  44.850  1.00 2.04  ? 400  LEU B C   1 
ATOM   7952  O  O   . LEU B  1 400 ? 56.221  29.658  44.746  1.00 3.11  ? 400  LEU B O   1 
ATOM   7953  C  CB  . LEU B  1 400 ? 54.438  28.024  46.971  1.00 2.00  ? 400  LEU B CB  1 
ATOM   7954  C  CG  . LEU B  1 400 ? 53.220  28.281  47.857  1.00 2.00  ? 400  LEU B CG  1 
ATOM   7955  C  CD1 . LEU B  1 400 ? 53.514  27.834  49.271  1.00 2.00  ? 400  LEU B CD1 1 
ATOM   7956  C  CD2 . LEU B  1 400 ? 52.884  29.766  47.837  1.00 2.16  ? 400  LEU B CD2 1 
ATOM   7957  N  N   . ALA B  1 401 ? 56.182  27.437  44.364  1.00 2.00  ? 401  ALA B N   1 
ATOM   7958  C  CA  . ALA B  1 401 ? 57.515  27.388  43.757  1.00 2.00  ? 401  ALA B CA  1 
ATOM   7959  C  C   . ALA B  1 401 ? 57.640  27.661  42.261  1.00 3.69  ? 401  ALA B C   1 
ATOM   7960  O  O   . ALA B  1 401 ? 58.605  28.296  41.835  1.00 4.97  ? 401  ALA B O   1 
ATOM   7961  C  CB  . ALA B  1 401 ? 58.171  26.058  44.082  1.00 2.00  ? 401  ALA B CB  1 
ATOM   7962  N  N   . LYS B  1 402 ? 56.696  27.176  41.460  1.00 2.02  ? 402  LYS B N   1 
ATOM   7963  C  CA  . LYS B  1 402 ? 56.749  27.405  40.016  1.00 2.70  ? 402  LYS B CA  1 
ATOM   7964  C  C   . LYS B  1 402 ? 56.138  28.754  39.643  1.00 2.00  ? 402  LYS B C   1 
ATOM   7965  O  O   . LYS B  1 402 ? 55.289  29.255  40.363  1.00 2.05  ? 402  LYS B O   1 
ATOM   7966  C  CB  . LYS B  1 402 ? 56.009  26.291  39.285  1.00 4.62  ? 402  LYS B CB  1 
ATOM   7967  C  CG  . LYS B  1 402 ? 56.703  24.951  39.342  1.00 7.20  ? 402  LYS B CG  1 
ATOM   7968  C  CD  . LYS B  1 402 ? 57.951  24.937  38.480  1.00 10.49 ? 402  LYS B CD  1 
ATOM   7969  C  CE  . LYS B  1 402 ? 58.575  23.548  38.486  1.00 12.71 ? 402  LYS B CE  1 
ATOM   7970  N  NZ  . LYS B  1 402 ? 59.854  23.479  37.721  1.00 14.66 ? 402  LYS B NZ  1 
ATOM   7971  N  N   . LYS B  1 403 ? 56.564  29.326  38.514  1.00 2.34  ? 403  LYS B N   1 
ATOM   7972  C  CA  . LYS B  1 403 ? 56.071  30.631  38.033  1.00 3.10  ? 403  LYS B CA  1 
ATOM   7973  C  C   . LYS B  1 403 ? 54.998  30.544  36.931  1.00 4.48  ? 403  LYS B C   1 
ATOM   7974  O  O   . LYS B  1 403 ? 54.839  29.512  36.260  1.00 4.75  ? 403  LYS B O   1 
ATOM   7975  C  CB  . LYS B  1 403 ? 57.216  31.475  37.457  1.00 2.43  ? 403  LYS B CB  1 
ATOM   7976  C  CG  . LYS B  1 403 ? 58.581  31.283  38.080  1.00 5.97  ? 403  LYS B CG  1 
ATOM   7977  C  CD  . LYS B  1 403 ? 59.681  31.815  37.147  1.00 7.87  ? 403  LYS B CD  1 
ATOM   7978  C  CE  . LYS B  1 403 ? 61.089  31.551  37.697  1.00 10.61 ? 403  LYS B CE  1 
ATOM   7979  N  NZ  . LYS B  1 403 ? 61.356  30.097  37.958  1.00 13.09 ? 403  LYS B NZ  1 
ATOM   7980  N  N   . SER B  1 404 ? 54.304  31.664  36.725  1.00 3.76  ? 404  SER B N   1 
ATOM   7981  C  CA  . SER B  1 404 ? 53.256  31.780  35.708  1.00 3.66  ? 404  SER B CA  1 
ATOM   7982  C  C   . SER B  1 404 ? 53.843  32.231  34.372  1.00 4.04  ? 404  SER B C   1 
ATOM   7983  O  O   . SER B  1 404 ? 55.024  32.562  34.272  1.00 4.80  ? 404  SER B O   1 
ATOM   7984  C  CB  . SER B  1 404 ? 52.219  32.824  36.125  1.00 4.58  ? 404  SER B CB  1 
ATOM   7985  O  OG  . SER B  1 404 ? 52.216  33.035  37.525  1.00 9.50  ? 404  SER B OG  1 
ATOM   7986  N  N   . LYS B  1 405 ? 53.003  32.258  33.346  1.00 3.47  ? 405  LYS B N   1 
ATOM   7987  C  CA  . LYS B  1 405 ? 53.430  32.705  32.030  1.00 2.05  ? 405  LYS B CA  1 
ATOM   7988  C  C   . LYS B  1 405 ? 53.367  34.219  31.988  1.00 2.00  ? 405  LYS B C   1 
ATOM   7989  O  O   . LYS B  1 405 ? 52.548  34.819  32.671  1.00 2.03  ? 405  LYS B O   1 
ATOM   7990  C  CB  . LYS B  1 405 ? 52.510  32.161  30.948  1.00 2.00  ? 405  LYS B CB  1 
ATOM   7991  C  CG  . LYS B  1 405 ? 52.686  32.868  29.622  1.00 2.00  ? 405  LYS B CG  1 
ATOM   7992  C  CD  . LYS B  1 405 ? 51.808  32.259  28.573  1.00 2.00  ? 405  LYS B CD  1 
ATOM   7993  C  CE  . LYS B  1 405 ? 52.085  32.891  27.242  1.00 2.00  ? 405  LYS B CE  1 
ATOM   7994  N  NZ  . LYS B  1 405 ? 51.723  34.313  27.299  1.00 2.00  ? 405  LYS B NZ  1 
ATOM   7995  N  N   . LEU B  1 406 ? 54.223  34.832  31.179  1.00 2.00  ? 406  LEU B N   1 
ATOM   7996  C  CA  . LEU B  1 406 ? 54.245  36.284  31.042  1.00 2.18  ? 406  LEU B CA  1 
ATOM   7997  C  C   . LEU B  1 406 ? 53.569  36.653  29.717  1.00 2.78  ? 406  LEU B C   1 
ATOM   7998  O  O   . LEU B  1 406 ? 53.751  35.952  28.729  1.00 3.20  ? 406  LEU B O   1 
ATOM   7999  C  CB  . LEU B  1 406 ? 55.690  36.783  31.041  1.00 2.00  ? 406  LEU B CB  1 
ATOM   8000  C  CG  . LEU B  1 406 ? 55.842  38.300  30.979  1.00 2.00  ? 406  LEU B CG  1 
ATOM   8001  C  CD1 . LEU B  1 406 ? 55.459  38.893  32.316  1.00 3.24  ? 406  LEU B CD1 1 
ATOM   8002  C  CD2 . LEU B  1 406 ? 57.261  38.669  30.629  1.00 2.00  ? 406  LEU B CD2 1 
ATOM   8003  N  N   . MET B  1 407 ? 52.789  37.734  29.681  1.00 2.00  ? 407  MET B N   1 
ATOM   8004  C  CA  . MET B  1 407 ? 52.131  38.115  28.431  1.00 2.29  ? 407  MET B CA  1 
ATOM   8005  C  C   . MET B  1 407 ? 53.168  38.687  27.475  1.00 3.36  ? 407  MET B C   1 
ATOM   8006  O  O   . MET B  1 407 ? 53.796  39.707  27.758  1.00 4.70  ? 407  MET B O   1 
ATOM   8007  C  CB  . MET B  1 407 ? 51.032  39.154  28.684  1.00 3.71  ? 407  MET B CB  1 
ATOM   8008  C  CG  . MET B  1 407 ? 50.148  39.504  27.474  1.00 2.32  ? 407  MET B CG  1 
ATOM   8009  S  SD  . MET B  1 407 ? 50.978  40.383  26.121  1.00 6.00  ? 407  MET B SD  1 
ATOM   8010  C  CE  . MET B  1 407 ? 51.272  42.026  26.851  1.00 2.00  ? 407  MET B CE  1 
ATOM   8011  N  N   . ASN B  1 408 ? 53.338  38.024  26.340  1.00 3.95  ? 408  ASN B N   1 
ATOM   8012  C  CA  . ASN B  1 408 ? 54.301  38.444  25.334  1.00 4.90  ? 408  ASN B CA  1 
ATOM   8013  C  C   . ASN B  1 408 ? 53.521  38.796  24.079  1.00 3.20  ? 408  ASN B C   1 
ATOM   8014  O  O   . ASN B  1 408 ? 52.699  38.004  23.625  1.00 3.16  ? 408  ASN B O   1 
ATOM   8015  C  CB  . ASN B  1 408 ? 55.275  37.293  25.063  1.00 8.41  ? 408  ASN B CB  1 
ATOM   8016  C  CG  . ASN B  1 408 ? 56.555  37.749  24.387  1.00 11.83 ? 408  ASN B CG  1 
ATOM   8017  O  OD1 . ASN B  1 408 ? 56.626  37.839  23.157  1.00 13.08 ? 408  ASN B OD1 1 
ATOM   8018  N  ND2 . ASN B  1 408 ? 57.577  38.049  25.193  1.00 12.78 ? 408  ASN B ND2 1 
ATOM   8019  N  N   . GLN B  1 409 ? 53.767  39.972  23.513  1.00 2.90  ? 409  GLN B N   1 
ATOM   8020  C  CA  . GLN B  1 409 ? 53.033  40.376  22.320  1.00 4.10  ? 409  GLN B CA  1 
ATOM   8021  C  C   . GLN B  1 409 ? 52.995  39.323  21.232  1.00 5.16  ? 409  GLN B C   1 
ATOM   8022  O  O   . GLN B  1 409 ? 52.062  39.299  20.419  1.00 4.50  ? 409  GLN B O   1 
ATOM   8023  C  CB  . GLN B  1 409 ? 53.588  41.671  21.748  1.00 3.14  ? 409  GLN B CB  1 
ATOM   8024  C  CG  . GLN B  1 409 ? 52.815  42.851  22.204  1.00 4.36  ? 409  GLN B CG  1 
ATOM   8025  C  CD  . GLN B  1 409 ? 53.594  44.119  22.075  1.00 6.53  ? 409  GLN B CD  1 
ATOM   8026  O  OE1 . GLN B  1 409 ? 54.743  44.212  22.502  1.00 8.01  ? 409  GLN B OE1 1 
ATOM   8027  N  NE2 . GLN B  1 409 ? 52.976  45.132  21.487  1.00 9.51  ? 409  GLN B NE2 1 
ATOM   8028  N  N   . ASN B  1 410 ? 54.006  38.452  21.213  1.00 5.39  ? 410  ASN B N   1 
ATOM   8029  C  CA  . ASN B  1 410 ? 54.059  37.390  20.218  1.00 6.32  ? 410  ASN B CA  1 
ATOM   8030  C  C   . ASN B  1 410 ? 54.131  35.977  20.842  1.00 3.94  ? 410  ASN B C   1 
ATOM   8031  O  O   . ASN B  1 410 ? 54.850  35.088  20.393  1.00 2.88  ? 410  ASN B O   1 
ATOM   8032  C  CB  . ASN B  1 410 ? 55.173  37.701  19.176  1.00 8.87  ? 410  ASN B CB  1 
ATOM   8033  C  CG  . ASN B  1 410 ? 56.449  36.916  19.376  1.00 11.67 ? 410  ASN B CG  1 
ATOM   8034  O  OD1 . ASN B  1 410 ? 57.414  37.416  19.955  1.00 14.04 ? 410  ASN B OD1 1 
ATOM   8035  N  ND2 . ASN B  1 410 ? 56.476  35.682  18.867  1.00 14.40 ? 410  ASN B ND2 1 
ATOM   8036  N  N   . LYS B  1 411 ? 53.322  35.818  21.886  1.00 5.33  ? 411  LYS B N   1 
ATOM   8037  C  CA  . LYS B  1 411 ? 53.114  34.585  22.661  1.00 4.12  ? 411  LYS B CA  1 
ATOM   8038  C  C   . LYS B  1 411 ? 51.999  34.926  23.646  1.00 2.30  ? 411  LYS B C   1 
ATOM   8039  O  O   . LYS B  1 411 ? 52.224  35.068  24.841  1.00 2.00  ? 411  LYS B O   1 
ATOM   8040  C  CB  . LYS B  1 411 ? 54.363  34.132  23.435  1.00 3.92  ? 411  LYS B CB  1 
ATOM   8041  C  CG  . LYS B  1 411 ? 55.406  33.387  22.594  1.00 4.49  ? 411  LYS B CG  1 
ATOM   8042  C  CD  . LYS B  1 411 ? 56.554  32.805  23.436  1.00 4.20  ? 411  LYS B CD  1 
ATOM   8043  C  CE  . LYS B  1 411 ? 57.738  32.436  22.537  1.00 5.17  ? 411  LYS B CE  1 
ATOM   8044  N  NZ  . LYS B  1 411 ? 58.821  31.635  23.187  1.00 4.02  ? 411  LYS B NZ  1 
ATOM   8045  N  N   . MET B  1 412 ? 50.790  35.065  23.116  1.00 2.00  ? 412  MET B N   1 
ATOM   8046  C  CA  . MET B  1 412 ? 49.641  35.434  23.914  1.00 2.00  ? 412  MET B CA  1 
ATOM   8047  C  C   . MET B  1 412 ? 48.978  34.351  24.752  1.00 2.93  ? 412  MET B C   1 
ATOM   8048  O  O   . MET B  1 412 ? 48.932  34.436  25.979  1.00 3.12  ? 412  MET B O   1 
ATOM   8049  C  CB  . MET B  1 412 ? 48.608  36.100  23.005  1.00 2.00  ? 412  MET B CB  1 
ATOM   8050  C  CG  . MET B  1 412 ? 49.039  37.489  22.567  1.00 2.44  ? 412  MET B CG  1 
ATOM   8051  S  SD  . MET B  1 412 ? 47.725  38.484  21.846  1.00 2.00  ? 412  MET B SD  1 
ATOM   8052  C  CE  . MET B  1 412 ? 48.551  39.180  20.433  1.00 2.00  ? 412  MET B CE  1 
ATOM   8053  N  N   . VAL B  1 413 ? 48.470  33.324  24.089  1.00 3.78  ? 413  VAL B N   1 
ATOM   8054  C  CA  . VAL B  1 413 ? 47.771  32.255  24.780  1.00 2.87  ? 413  VAL B CA  1 
ATOM   8055  C  C   . VAL B  1 413 ? 48.339  30.885  24.444  1.00 4.31  ? 413  VAL B C   1 
ATOM   8056  O  O   . VAL B  1 413 ? 48.386  30.506  23.283  1.00 7.46  ? 413  VAL B O   1 
ATOM   8057  C  CB  . VAL B  1 413 ? 46.282  32.297  24.395  1.00 2.00  ? 413  VAL B CB  1 
ATOM   8058  C  CG1 . VAL B  1 413 ? 45.574  31.028  24.840  1.00 2.00  ? 413  VAL B CG1 1 
ATOM   8059  C  CG2 . VAL B  1 413 ? 45.592  33.508  25.005  1.00 2.00  ? 413  VAL B CG2 1 
ATOM   8060  N  N   . THR B  1 414 ? 48.755  30.138  25.453  1.00 2.35  ? 414  THR B N   1 
ATOM   8061  C  CA  . THR B  1 414 ? 49.280  28.811  25.194  1.00 2.00  ? 414  THR B CA  1 
ATOM   8062  C  C   . THR B  1 414 ? 48.265  27.931  24.455  1.00 2.00  ? 414  THR B C   1 
ATOM   8063  O  O   . THR B  1 414 ? 47.063  28.038  24.669  1.00 2.15  ? 414  THR B O   1 
ATOM   8064  C  CB  . THR B  1 414 ? 49.540  28.082  26.488  1.00 2.00  ? 414  THR B CB  1 
ATOM   8065  O  OG1 . THR B  1 414 ? 50.021  26.757  26.199  1.00 2.00  ? 414  THR B OG1 1 
ATOM   8066  C  CG2 . THR B  1 414 ? 48.266  28.004  27.308  1.00 2.70  ? 414  THR B CG2 1 
ATOM   8067  N  N   . SER B  1 415 ? 48.763  27.036  23.608  1.00 3.16  ? 415  SER B N   1 
ATOM   8068  C  CA  . SER B  1 415 ? 47.906  26.104  22.827  1.00 2.00  ? 415  SER B CA  1 
ATOM   8069  C  C   . SER B  1 415 ? 47.069  25.193  23.722  1.00 2.00  ? 415  SER B C   1 
ATOM   8070  O  O   . SER B  1 415 ? 46.001  24.720  23.331  1.00 2.00  ? 415  SER B O   1 
ATOM   8071  C  CB  . SER B  1 415 ? 48.760  25.233  21.907  1.00 2.00  ? 415  SER B CB  1 
ATOM   8072  O  OG  . SER B  1 415 ? 49.499  26.015  20.986  1.00 4.32  ? 415  SER B OG  1 
ATOM   8073  N  N   . GLU B  1 416 ? 47.547  24.974  24.936  1.00 2.00  ? 416  GLU B N   1 
ATOM   8074  C  CA  . GLU B  1 416 ? 46.851  24.114  25.862  1.00 3.39  ? 416  GLU B CA  1 
ATOM   8075  C  C   . GLU B  1 416 ? 45.511  24.758  26.166  1.00 2.06  ? 416  GLU B C   1 
ATOM   8076  O  O   . GLU B  1 416 ? 44.567  24.088  26.585  1.00 2.00  ? 416  GLU B O   1 
ATOM   8077  C  CB  . GLU B  1 416 ? 47.695  23.917  27.128  1.00 3.30  ? 416  GLU B CB  1 
ATOM   8078  C  CG  . GLU B  1 416 ? 48.984  23.096  26.899  1.00 2.94  ? 416  GLU B CG  1 
ATOM   8079  C  CD  . GLU B  1 416 ? 48.730  21.596  26.754  1.00 2.32  ? 416  GLU B CD  1 
ATOM   8080  O  OE1 . GLU B  1 416 ? 49.123  20.996  25.723  1.00 2.00  ? 416  GLU B OE1 1 
ATOM   8081  O  OE2 . GLU B  1 416 ? 48.141  21.020  27.689  1.00 2.00  ? 416  GLU B OE2 1 
ATOM   8082  N  N   . LEU B  1 417 ? 45.431  26.063  25.934  1.00 2.00  ? 417  LEU B N   1 
ATOM   8083  C  CA  . LEU B  1 417 ? 44.190  26.791  26.153  1.00 2.00  ? 417  LEU B CA  1 
ATOM   8084  C  C   . LEU B  1 417 ? 43.565  27.267  24.842  1.00 3.43  ? 417  LEU B C   1 
ATOM   8085  O  O   . LEU B  1 417 ? 42.358  27.512  24.777  1.00 4.05  ? 417  LEU B O   1 
ATOM   8086  C  CB  . LEU B  1 417 ? 44.418  27.998  27.063  1.00 2.00  ? 417  LEU B CB  1 
ATOM   8087  C  CG  . LEU B  1 417 ? 43.950  27.818  28.503  1.00 2.00  ? 417  LEU B CG  1 
ATOM   8088  C  CD1 . LEU B  1 417 ? 43.988  29.154  29.213  1.00 2.00  ? 417  LEU B CD1 1 
ATOM   8089  C  CD2 . LEU B  1 417 ? 42.542  27.246  28.517  1.00 2.00  ? 417  LEU B CD2 1 
ATOM   8090  N  N   . ARG B  1 418 ? 44.378  27.386  23.797  1.00 3.06  ? 418  ARG B N   1 
ATOM   8091  C  CA  . ARG B  1 418 ? 43.882  27.864  22.509  1.00 2.00  ? 418  ARG B CA  1 
ATOM   8092  C  C   . ARG B  1 418 ? 43.631  26.764  21.484  1.00 2.08  ? 418  ARG B C   1 
ATOM   8093  O  O   . ARG B  1 418 ? 43.293  27.055  20.337  1.00 2.00  ? 418  ARG B O   1 
ATOM   8094  C  CB  . ARG B  1 418 ? 44.867  28.878  21.919  1.00 2.04  ? 418  ARG B CB  1 
ATOM   8095  C  CG  . ARG B  1 418 ? 44.331  29.705  20.753  1.00 2.00  ? 418  ARG B CG  1 
ATOM   8096  C  CD  . ARG B  1 418 ? 45.463  30.459  20.076  1.00 2.00  ? 418  ARG B CD  1 
ATOM   8097  N  NE  . ARG B  1 418 ? 46.207  29.568  19.201  1.00 2.07  ? 418  ARG B NE  1 
ATOM   8098  C  CZ  . ARG B  1 418 ? 45.811  29.241  17.976  1.00 2.90  ? 418  ARG B CZ  1 
ATOM   8099  N  NH1 . ARG B  1 418 ? 44.688  29.751  17.493  1.00 3.36  ? 418  ARG B NH1 1 
ATOM   8100  N  NH2 . ARG B  1 418 ? 46.514  28.382  17.247  1.00 2.46  ? 418  ARG B NH2 1 
ATOM   8101  N  N   . ASN B  1 419 ? 43.791  25.505  21.883  1.00 2.97  ? 419  ASN B N   1 
ATOM   8102  C  CA  . ASN B  1 419 ? 43.576  24.408  20.946  1.00 2.00  ? 419  ASN B CA  1 
ATOM   8103  C  C   . ASN B  1 419 ? 42.995  23.147  21.548  1.00 2.00  ? 419  ASN B C   1 
ATOM   8104  O  O   . ASN B  1 419 ? 42.315  22.388  20.863  1.00 2.00  ? 419  ASN B O   1 
ATOM   8105  C  CB  . ASN B  1 419 ? 44.881  24.059  20.240  1.00 2.00  ? 419  ASN B CB  1 
ATOM   8106  C  CG  . ASN B  1 419 ? 44.910  24.546  18.815  1.00 2.00  ? 419  ASN B CG  1 
ATOM   8107  O  OD1 . ASN B  1 419 ? 43.974  24.309  18.052  1.00 2.30  ? 419  ASN B OD1 1 
ATOM   8108  N  ND2 . ASN B  1 419 ? 45.987  25.225  18.441  1.00 2.00  ? 419  ASN B ND2 1 
ATOM   8109  N  N   . LYS B  1 420 ? 43.259  22.929  22.831  1.00 2.10  ? 420  LYS B N   1 
ATOM   8110  C  CA  . LYS B  1 420 ? 42.777  21.740  23.513  1.00 2.00  ? 420  LYS B CA  1 
ATOM   8111  C  C   . LYS B  1 420 ? 41.932  22.053  24.750  1.00 2.22  ? 420  LYS B C   1 
ATOM   8112  O  O   . LYS B  1 420 ? 42.210  21.543  25.829  1.00 3.53  ? 420  LYS B O   1 
ATOM   8113  C  CB  . LYS B  1 420 ? 43.979  20.877  23.916  1.00 2.00  ? 420  LYS B CB  1 
ATOM   8114  C  CG  . LYS B  1 420 ? 44.909  20.502  22.759  1.00 2.11  ? 420  LYS B CG  1 
ATOM   8115  C  CD  . LYS B  1 420 ? 45.990  19.491  23.168  1.00 2.00  ? 420  LYS B CD  1 
ATOM   8116  C  CE  . LYS B  1 420 ? 47.380  20.121  23.168  1.00 2.00  ? 420  LYS B CE  1 
ATOM   8117  N  NZ  . LYS B  1 420 ? 48.333  19.382  22.297  1.00 2.18  ? 420  LYS B NZ  1 
ATOM   8118  N  N   . LEU B  1 421 ? 40.896  22.874  24.609  1.00 2.07  ? 421  LEU B N   1 
ATOM   8119  C  CA  . LEU B  1 421 ? 40.069  23.222  25.766  1.00 2.00  ? 421  LEU B CA  1 
ATOM   8120  C  C   . LEU B  1 421 ? 38.889  22.290  25.925  1.00 2.00  ? 421  LEU B C   1 
ATOM   8121  O  O   . LEU B  1 421 ? 38.252  21.917  24.944  1.00 2.00  ? 421  LEU B O   1 
ATOM   8122  C  CB  . LEU B  1 421 ? 39.558  24.665  25.655  1.00 2.56  ? 421  LEU B CB  1 
ATOM   8123  C  CG  . LEU B  1 421 ? 38.718  25.255  26.799  1.00 2.00  ? 421  LEU B CG  1 
ATOM   8124  C  CD1 . LEU B  1 421 ? 39.435  25.079  28.121  1.00 2.00  ? 421  LEU B CD1 1 
ATOM   8125  C  CD2 . LEU B  1 421 ? 38.459  26.728  26.531  1.00 2.00  ? 421  LEU B CD2 1 
ATOM   8126  N  N   . PHE B  1 422 ? 38.597  21.918  27.167  1.00 2.00  ? 422  PHE B N   1 
ATOM   8127  C  CA  . PHE B  1 422 ? 37.471  21.035  27.443  1.00 2.08  ? 422  PHE B CA  1 
ATOM   8128  C  C   . PHE B  1 422 ? 36.250  21.832  27.893  1.00 2.63  ? 422  PHE B C   1 
ATOM   8129  O  O   . PHE B  1 422 ? 36.324  22.613  28.842  1.00 2.24  ? 422  PHE B O   1 
ATOM   8130  C  CB  . PHE B  1 422 ? 37.825  20.032  28.543  1.00 2.03  ? 422  PHE B CB  1 
ATOM   8131  C  CG  . PHE B  1 422 ? 36.876  18.858  28.628  1.00 2.17  ? 422  PHE B CG  1 
ATOM   8132  C  CD1 . PHE B  1 422 ? 36.855  17.892  27.627  1.00 2.11  ? 422  PHE B CD1 1 
ATOM   8133  C  CD2 . PHE B  1 422 ? 36.017  18.709  29.710  1.00 2.00  ? 422  PHE B CD2 1 
ATOM   8134  C  CE1 . PHE B  1 422 ? 36.000  16.799  27.706  1.00 2.00  ? 422  PHE B CE1 1 
ATOM   8135  C  CE2 . PHE B  1 422 ? 35.156  17.614  29.793  1.00 2.00  ? 422  PHE B CE2 1 
ATOM   8136  C  CZ  . PHE B  1 422 ? 35.150  16.662  28.794  1.00 2.00  ? 422  PHE B CZ  1 
ATOM   8137  N  N   . GLN B  1 423 ? 35.132  21.649  27.204  1.00 2.66  ? 423  GLN B N   1 
ATOM   8138  C  CA  . GLN B  1 423 ? 33.907  22.328  27.591  1.00 3.42  ? 423  GLN B CA  1 
ATOM   8139  C  C   . GLN B  1 423 ? 33.074  21.252  28.252  1.00 3.99  ? 423  GLN B C   1 
ATOM   8140  O  O   . GLN B  1 423 ? 32.876  20.176  27.685  1.00 3.76  ? 423  GLN B O   1 
ATOM   8141  C  CB  . GLN B  1 423 ? 33.174  22.888  26.379  1.00 4.50  ? 423  GLN B CB  1 
ATOM   8142  C  CG  . GLN B  1 423 ? 33.841  24.096  25.747  1.00 3.06  ? 423  GLN B CG  1 
ATOM   8143  C  CD  . GLN B  1 423 ? 33.793  25.314  26.637  1.00 3.28  ? 423  GLN B CD  1 
ATOM   8144  O  OE1 . GLN B  1 423 ? 34.379  25.327  27.717  1.00 3.94  ? 423  GLN B OE1 1 
ATOM   8145  N  NE2 . GLN B  1 423 ? 33.087  26.350  26.189  1.00 4.72  ? 423  GLN B NE2 1 
ATOM   8146  N  N   . PRO B  1 424 ? 32.551  21.541  29.449  1.00 6.05  ? 424  PRO B N   1 
ATOM   8147  C  CA  . PRO B  1 424 ? 31.732  20.619  30.248  1.00 7.91  ? 424  PRO B CA  1 
ATOM   8148  C  C   . PRO B  1 424 ? 30.546  20.025  29.498  1.00 7.97  ? 424  PRO B C   1 
ATOM   8149  O  O   . PRO B  1 424 ? 30.056  18.945  29.833  1.00 7.97  ? 424  PRO B O   1 
ATOM   8150  C  CB  . PRO B  1 424 ? 31.271  21.477  31.435  1.00 8.43  ? 424  PRO B CB  1 
ATOM   8151  C  CG  . PRO B  1 424 ? 32.030  22.777  31.317  1.00 7.15  ? 424  PRO B CG  1 
ATOM   8152  C  CD  . PRO B  1 424 ? 32.322  22.933  29.865  1.00 6.67  ? 424  PRO B CD  1 
ATOM   8153  N  N   . THR B  1 425 ? 30.081  20.742  28.490  1.00 8.33  ? 425  THR B N   1 
ATOM   8154  C  CA  . THR B  1 425 ? 28.952  20.281  27.710  1.00 11.71 ? 425  THR B CA  1 
ATOM   8155  C  C   . THR B  1 425 ? 29.378  19.244  26.667  1.00 13.44 ? 425  THR B C   1 
ATOM   8156  O  O   . THR B  1 425 ? 28.641  18.291  26.376  1.00 12.58 ? 425  THR B O   1 
ATOM   8157  C  CB  . THR B  1 425 ? 28.276  21.483  27.010  1.00 13.25 ? 425  THR B CB  1 
ATOM   8158  O  OG1 . THR B  1 425 ? 27.695  22.337  28.002  1.00 14.68 ? 425  THR B OG1 1 
ATOM   8159  C  CG2 . THR B  1 425 ? 27.192  21.026  26.044  1.00 15.49 ? 425  THR B CG2 1 
ATOM   8160  N  N   . HIS B  1 426 ? 30.584  19.403  26.135  1.00 13.54 ? 426  HIS B N   1 
ATOM   8161  C  CA  . HIS B  1 426 ? 31.046  18.500  25.096  1.00 14.64 ? 426  HIS B CA  1 
ATOM   8162  C  C   . HIS B  1 426 ? 32.049  17.421  25.457  1.00 14.35 ? 426  HIS B C   1 
ATOM   8163  O  O   . HIS B  1 426 ? 32.515  17.339  26.590  1.00 13.95 ? 426  HIS B O   1 
ATOM   8164  C  CB  . HIS B  1 426 ? 31.537  19.341  23.924  1.00 16.12 ? 426  HIS B CB  1 
ATOM   8165  C  CG  . HIS B  1 426 ? 30.476  20.240  23.378  1.00 16.83 ? 426  HIS B CG  1 
ATOM   8166  N  ND1 . HIS B  1 426 ? 29.388  19.762  22.681  1.00 17.63 ? 426  HIS B ND1 1 
ATOM   8167  C  CD2 . HIS B  1 426 ? 30.276  21.571  23.523  1.00 16.94 ? 426  HIS B CD2 1 
ATOM   8168  C  CE1 . HIS B  1 426 ? 28.561  20.758  22.423  1.00 18.61 ? 426  HIS B CE1 1 
ATOM   8169  N  NE2 . HIS B  1 426 ? 29.076  21.866  22.924  1.00 19.29 ? 426  HIS B NE2 1 
ATOM   8170  N  N   . LYS B  1 427 ? 32.364  16.590  24.467  1.00 13.81 ? 427  LYS B N   1 
ATOM   8171  C  CA  . LYS B  1 427 ? 33.274  15.470  24.645  1.00 14.81 ? 427  LYS B CA  1 
ATOM   8172  C  C   . LYS B  1 427 ? 34.737  15.683  24.237  1.00 13.16 ? 427  LYS B C   1 
ATOM   8173  O  O   . LYS B  1 427 ? 35.639  15.151  24.880  1.00 14.15 ? 427  LYS B O   1 
ATOM   8174  C  CB  . LYS B  1 427 ? 32.710  14.237  23.913  1.00 18.05 ? 427  LYS B CB  1 
ATOM   8175  C  CG  . LYS B  1 427 ? 31.303  13.815  24.366  1.00 21.46 ? 427  LYS B CG  1 
ATOM   8176  C  CD  . LYS B  1 427 ? 30.872  12.470  23.769  1.00 23.10 ? 427  LYS B CD  1 
ATOM   8177  C  CE  . LYS B  1 427 ? 29.346  12.285  23.828  1.00 24.25 ? 427  LYS B CE  1 
ATOM   8178  N  NZ  . LYS B  1 427 ? 28.617  13.221  22.907  1.00 24.31 ? 427  LYS B NZ  1 
ATOM   8179  N  N   . ILE B  1 428 ? 34.989  16.447  23.181  1.00 10.82 ? 428  ILE B N   1 
ATOM   8180  C  CA  . ILE B  1 428 ? 36.367  16.653  22.744  1.00 8.90  ? 428  ILE B CA  1 
ATOM   8181  C  C   . ILE B  1 428 ? 37.173  17.646  23.564  1.00 7.71  ? 428  ILE B C   1 
ATOM   8182  O  O   . ILE B  1 428 ? 36.624  18.480  24.279  1.00 8.01  ? 428  ILE B O   1 
ATOM   8183  C  CB  . ILE B  1 428 ? 36.438  17.126  21.275  1.00 10.36 ? 428  ILE B CB  1 
ATOM   8184  C  CG1 . ILE B  1 428 ? 35.406  18.234  21.028  1.00 10.86 ? 428  ILE B CG1 1 
ATOM   8185  C  CG2 . ILE B  1 428 ? 36.239  15.943  20.339  1.00 12.40 ? 428  ILE B CG2 1 
ATOM   8186  C  CD1 . ILE B  1 428 ? 35.579  18.954  19.697  1.00 10.91 ? 428  ILE B CD1 1 
ATOM   8187  N  N   . HIS B  1 429 ? 38.492  17.529  23.455  1.00 6.35  ? 429  HIS B N   1 
ATOM   8188  C  CA  . HIS B  1 429 ? 39.428  18.433  24.121  1.00 5.38  ? 429  HIS B CA  1 
ATOM   8189  C  C   . HIS B  1 429 ? 39.962  19.337  23.016  1.00 5.49  ? 429  HIS B C   1 
ATOM   8190  O  O   . HIS B  1 429 ? 41.173  19.537  22.902  1.00 3.74  ? 429  HIS B O   1 
ATOM   8191  C  CB  . HIS B  1 429 ? 40.615  17.672  24.700  1.00 4.47  ? 429  HIS B CB  1 
ATOM   8192  C  CG  . HIS B  1 429 ? 40.449  17.273  26.127  1.00 3.25  ? 429  HIS B CG  1 
ATOM   8193  N  ND1 . HIS B  1 429 ? 39.489  16.379  26.543  1.00 2.54  ? 429  HIS B ND1 1 
ATOM   8194  C  CD2 . HIS B  1 429 ? 41.163  17.605  27.229  1.00 2.50  ? 429  HIS B CD2 1 
ATOM   8195  C  CE1 . HIS B  1 429 ? 39.621  16.171  27.841  1.00 3.74  ? 429  HIS B CE1 1 
ATOM   8196  N  NE2 . HIS B  1 429 ? 40.630  16.903  28.281  1.00 3.16  ? 429  HIS B NE2 1 
ATOM   8197  N  N   . GLY B  1 430 ? 39.066  19.875  22.194  1.00 4.54  ? 430  GLY B N   1 
ATOM   8198  C  CA  . GLY B  1 430 ? 39.527  20.709  21.102  1.00 4.12  ? 430  GLY B CA  1 
ATOM   8199  C  C   . GLY B  1 430 ? 38.910  22.079  20.910  1.00 3.61  ? 430  GLY B C   1 
ATOM   8200  O  O   . GLY B  1 430 ? 38.817  22.551  19.780  1.00 2.27  ? 430  GLY B O   1 
ATOM   8201  N  N   . PHE B  1 431 ? 38.488  22.732  21.985  1.00 3.60  ? 431  PHE B N   1 
ATOM   8202  C  CA  . PHE B  1 431 ? 37.916  24.057  21.830  1.00 3.71  ? 431  PHE B CA  1 
ATOM   8203  C  C   . PHE B  1 431 ? 39.003  25.106  21.921  1.00 3.91  ? 431  PHE B C   1 
ATOM   8204  O  O   . PHE B  1 431 ? 40.163  24.784  22.158  1.00 5.68  ? 431  PHE B O   1 
ATOM   8205  C  CB  . PHE B  1 431 ? 36.843  24.317  22.877  1.00 4.43  ? 431  PHE B CB  1 
ATOM   8206  C  CG  . PHE B  1 431 ? 35.513  23.713  22.533  1.00 6.28  ? 431  PHE B CG  1 
ATOM   8207  C  CD1 . PHE B  1 431 ? 35.093  22.525  23.122  1.00 6.89  ? 431  PHE B CD1 1 
ATOM   8208  C  CD2 . PHE B  1 431 ? 34.675  24.334  21.619  1.00 5.84  ? 431  PHE B CD2 1 
ATOM   8209  C  CE1 . PHE B  1 431 ? 33.853  21.969  22.806  1.00 7.15  ? 431  PHE B CE1 1 
ATOM   8210  C  CE2 . PHE B  1 431 ? 33.440  23.784  21.301  1.00 6.99  ? 431  PHE B CE2 1 
ATOM   8211  C  CZ  . PHE B  1 431 ? 33.028  22.600  21.895  1.00 5.38  ? 431  PHE B CZ  1 
ATOM   8212  N  N   . ASP B  1 432 ? 38.630  26.364  21.731  1.00 4.62  ? 432  ASP B N   1 
ATOM   8213  C  CA  . ASP B  1 432 ? 39.599  27.455  21.775  1.00 4.79  ? 432  ASP B CA  1 
ATOM   8214  C  C   . ASP B  1 432 ? 39.131  28.598  22.701  1.00 3.68  ? 432  ASP B C   1 
ATOM   8215  O  O   . ASP B  1 432 ? 38.076  29.188  22.468  1.00 4.55  ? 432  ASP B O   1 
ATOM   8216  C  CB  . ASP B  1 432 ? 39.818  27.962  20.341  1.00 2.78  ? 432  ASP B CB  1 
ATOM   8217  C  CG  . ASP B  1 432 ? 40.754  29.150  20.269  1.00 3.37  ? 432  ASP B CG  1 
ATOM   8218  O  OD1 . ASP B  1 432 ? 41.175  29.658  21.330  1.00 5.25  ? 432  ASP B OD1 1 
ATOM   8219  O  OD2 . ASP B  1 432 ? 41.064  29.590  19.143  1.00 4.41  ? 432  ASP B OD2 1 
ATOM   8220  N  N   . LEU B  1 433 ? 39.907  28.911  23.743  1.00 2.03  ? 433  LEU B N   1 
ATOM   8221  C  CA  . LEU B  1 433 ? 39.526  29.988  24.660  1.00 2.32  ? 433  LEU B CA  1 
ATOM   8222  C  C   . LEU B  1 433 ? 39.665  31.384  24.058  1.00 2.00  ? 433  LEU B C   1 
ATOM   8223  O  O   . LEU B  1 433 ? 38.881  32.280  24.373  1.00 2.05  ? 433  LEU B O   1 
ATOM   8224  C  CB  . LEU B  1 433 ? 40.329  29.921  25.965  1.00 2.00  ? 433  LEU B CB  1 
ATOM   8225  C  CG  . LEU B  1 433 ? 39.984  31.012  26.992  1.00 2.00  ? 433  LEU B CG  1 
ATOM   8226  C  CD1 . LEU B  1 433 ? 38.479  31.141  27.148  1.00 2.00  ? 433  LEU B CD1 1 
ATOM   8227  C  CD2 . LEU B  1 433 ? 40.609  30.677  28.318  1.00 2.00  ? 433  LEU B CD2 1 
ATOM   8228  N  N   . ALA B  1 434 ? 40.659  31.573  23.198  1.00 2.00  ? 434  ALA B N   1 
ATOM   8229  C  CA  . ALA B  1 434 ? 40.873  32.867  22.562  1.00 2.00  ? 434  ALA B CA  1 
ATOM   8230  C  C   . ALA B  1 434 ? 39.719  33.235  21.625  1.00 2.03  ? 434  ALA B C   1 
ATOM   8231  O  O   . ALA B  1 434 ? 39.223  34.362  21.649  1.00 2.00  ? 434  ALA B O   1 
ATOM   8232  C  CB  . ALA B  1 434 ? 42.182  32.852  21.790  1.00 2.00  ? 434  ALA B CB  1 
ATOM   8233  N  N   . ALA B  1 435 ? 39.304  32.277  20.797  1.00 2.64  ? 435  ALA B N   1 
ATOM   8234  C  CA  . ALA B  1 435 ? 38.214  32.481  19.846  1.00 2.00  ? 435  ALA B CA  1 
ATOM   8235  C  C   . ALA B  1 435 ? 36.933  32.753  20.606  1.00 2.00  ? 435  ALA B C   1 
ATOM   8236  O  O   . ALA B  1 435 ? 36.187  33.680  20.286  1.00 2.61  ? 435  ALA B O   1 
ATOM   8237  C  CB  . ALA B  1 435 ? 38.046  31.249  18.961  1.00 2.00  ? 435  ALA B CB  1 
ATOM   8238  N  N   . ILE B  1 436 ? 36.672  31.937  21.614  1.00 2.00  ? 436  ILE B N   1 
ATOM   8239  C  CA  . ILE B  1 436 ? 35.480  32.139  22.408  1.00 2.00  ? 436  ILE B CA  1 
ATOM   8240  C  C   . ILE B  1 436 ? 35.494  33.545  23.017  1.00 3.03  ? 436  ILE B C   1 
ATOM   8241  O  O   . ILE B  1 436 ? 34.516  34.288  22.893  1.00 2.00  ? 436  ILE B O   1 
ATOM   8242  C  CB  . ILE B  1 436 ? 35.386  31.119  23.541  1.00 2.12  ? 436  ILE B CB  1 
ATOM   8243  C  CG1 . ILE B  1 436 ? 35.326  29.708  22.965  1.00 2.47  ? 436  ILE B CG1 1 
ATOM   8244  C  CG2 . ILE B  1 436 ? 34.153  31.396  24.378  1.00 2.00  ? 436  ILE B CG2 1 
ATOM   8245  C  CD1 . ILE B  1 436 ? 35.157  28.638  24.014  1.00 2.67  ? 436  ILE B CD1 1 
ATOM   8246  N  N   . ASN B  1 437 ? 36.601  33.909  23.669  1.00 2.57  ? 437  ASN B N   1 
ATOM   8247  C  CA  . ASN B  1 437 ? 36.718  35.229  24.294  1.00 2.00  ? 437  ASN B CA  1 
ATOM   8248  C  C   . ASN B  1 437 ? 36.391  36.331  23.306  1.00 3.49  ? 437  ASN B C   1 
ATOM   8249  O  O   . ASN B  1 437 ? 35.940  37.408  23.698  1.00 2.74  ? 437  ASN B O   1 
ATOM   8250  C  CB  . ASN B  1 437 ? 38.133  35.475  24.821  1.00 2.21  ? 437  ASN B CB  1 
ATOM   8251  C  CG  . ASN B  1 437 ? 38.384  34.817  26.145  1.00 2.00  ? 437  ASN B CG  1 
ATOM   8252  O  OD1 . ASN B  1 437 ? 37.589  34.945  27.062  1.00 2.00  ? 437  ASN B OD1 1 
ATOM   8253  N  ND2 . ASN B  1 437 ? 39.501  34.119  26.260  1.00 2.76  ? 437  ASN B ND2 1 
ATOM   8254  N  N   . LEU B  1 438 ? 36.629  36.052  22.024  1.00 4.57  ? 438  LEU B N   1 
ATOM   8255  C  CA  . LEU B  1 438 ? 36.390  37.021  20.965  1.00 2.58  ? 438  LEU B CA  1 
ATOM   8256  C  C   . LEU B  1 438 ? 34.973  37.130  20.458  1.00 2.29  ? 438  LEU B C   1 
ATOM   8257  O  O   . LEU B  1 438 ? 34.500  38.237  20.230  1.00 2.66  ? 438  LEU B O   1 
ATOM   8258  C  CB  . LEU B  1 438 ? 37.334  36.771  19.799  1.00 2.00  ? 438  LEU B CB  1 
ATOM   8259  C  CG  . LEU B  1 438 ? 38.691  37.411  20.088  1.00 3.11  ? 438  LEU B CG  1 
ATOM   8260  C  CD1 . LEU B  1 438 ? 39.575  37.260  18.865  1.00 2.93  ? 438  LEU B CD1 1 
ATOM   8261  C  CD2 . LEU B  1 438 ? 38.509  38.893  20.450  1.00 2.00  ? 438  LEU B CD2 1 
ATOM   8262  N  N   . GLN B  1 439 ? 34.280  36.020  20.249  1.00 2.70  ? 439  GLN B N   1 
ATOM   8263  C  CA  . GLN B  1 439 ? 32.902  36.177  19.804  1.00 5.44  ? 439  GLN B CA  1 
ATOM   8264  C  C   . GLN B  1 439 ? 32.078  36.640  21.003  1.00 4.91  ? 439  GLN B C   1 
ATOM   8265  O  O   . GLN B  1 439 ? 31.206  37.506  20.874  1.00 4.24  ? 439  GLN B O   1 
ATOM   8266  C  CB  . GLN B  1 439 ? 32.331  34.880  19.206  1.00 6.10  ? 439  GLN B CB  1 
ATOM   8267  C  CG  . GLN B  1 439 ? 32.445  34.860  17.675  1.00 8.05  ? 439  GLN B CG  1 
ATOM   8268  C  CD  . GLN B  1 439 ? 31.528  33.851  17.009  1.00 9.14  ? 439  GLN B CD  1 
ATOM   8269  O  OE1 . GLN B  1 439 ? 30.306  33.925  17.135  1.00 9.12  ? 439  GLN B OE1 1 
ATOM   8270  N  NE2 . GLN B  1 439 ? 32.117  32.901  16.289  1.00 9.95  ? 439  GLN B NE2 1 
ATOM   8271  N  N   . ARG B  1 440 ? 32.395  36.084  22.171  1.00 3.38  ? 440  ARG B N   1 
ATOM   8272  C  CA  . ARG B  1 440 ? 31.708  36.422  23.408  1.00 2.70  ? 440  ARG B CA  1 
ATOM   8273  C  C   . ARG B  1 440 ? 31.715  37.929  23.620  1.00 2.51  ? 440  ARG B C   1 
ATOM   8274  O  O   . ARG B  1 440 ? 30.857  38.464  24.322  1.00 3.95  ? 440  ARG B O   1 
ATOM   8275  C  CB  . ARG B  1 440 ? 32.385  35.729  24.593  1.00 3.69  ? 440  ARG B CB  1 
ATOM   8276  C  CG  . ARG B  1 440 ? 31.707  35.977  25.947  1.00 3.79  ? 440  ARG B CG  1 
ATOM   8277  C  CD  . ARG B  1 440 ? 30.371  35.249  26.048  1.00 4.39  ? 440  ARG B CD  1 
ATOM   8278  N  NE  . ARG B  1 440 ? 30.510  33.818  26.318  1.00 2.58  ? 440  ARG B NE  1 
ATOM   8279  C  CZ  . ARG B  1 440 ? 29.661  32.899  25.871  1.00 2.00  ? 440  ARG B CZ  1 
ATOM   8280  N  NH1 . ARG B  1 440 ? 28.621  33.261  25.129  1.00 2.00  ? 440  ARG B NH1 1 
ATOM   8281  N  NH2 . ARG B  1 440 ? 29.846  31.624  26.167  1.00 2.00  ? 440  ARG B NH2 1 
ATOM   8282  N  N   . CYS B  1 441 ? 32.700  38.608  23.038  1.00 2.00  ? 441  CYS B N   1 
ATOM   8283  C  CA  . CYS B  1 441 ? 32.772  40.058  23.145  1.00 2.00  ? 441  CYS B CA  1 
ATOM   8284  C  C   . CYS B  1 441 ? 31.609  40.558  22.322  1.00 2.00  ? 441  CYS B C   1 
ATOM   8285  O  O   . CYS B  1 441 ? 30.778  41.337  22.780  1.00 2.00  ? 441  CYS B O   1 
ATOM   8286  C  CB  . CYS B  1 441 ? 34.059  40.600  22.528  1.00 2.00  ? 441  CYS B CB  1 
ATOM   8287  S  SG  . CYS B  1 441 ? 35.475  40.756  23.632  1.00 2.03  ? 441  CYS B SG  1 
ATOM   8288  N  N   . ARG B  1 442 ? 31.554  40.079  21.090  1.00 2.99  ? 442  ARG B N   1 
ATOM   8289  C  CA  . ARG B  1 442 ? 30.510  40.467  20.162  1.00 2.89  ? 442  ARG B CA  1 
ATOM   8290  C  C   . ARG B  1 442 ? 29.112  40.122  20.679  1.00 2.00  ? 442  ARG B C   1 
ATOM   8291  O  O   . ARG B  1 442 ? 28.184  40.913  20.521  1.00 2.00  ? 442  ARG B O   1 
ATOM   8292  C  CB  . ARG B  1 442 ? 30.810  39.823  18.812  1.00 2.00  ? 442  ARG B CB  1 
ATOM   8293  C  CG  . ARG B  1 442 ? 32.206  40.202  18.344  1.00 2.00  ? 442  ARG B CG  1 
ATOM   8294  C  CD  . ARG B  1 442 ? 32.650  39.436  17.125  1.00 3.14  ? 442  ARG B CD  1 
ATOM   8295  N  NE  . ARG B  1 442 ? 34.035  39.736  16.780  1.00 2.00  ? 442  ARG B NE  1 
ATOM   8296  C  CZ  . ARG B  1 442 ? 34.639  39.296  15.688  1.00 2.00  ? 442  ARG B CZ  1 
ATOM   8297  N  NH1 . ARG B  1 442 ? 33.985  38.537  14.829  1.00 2.00  ? 442  ARG B NH1 1 
ATOM   8298  N  NH2 . ARG B  1 442 ? 35.895  39.620  15.458  1.00 2.00  ? 442  ARG B NH2 1 
ATOM   8299  N  N   . ASP B  1 443 ? 28.975  38.956  21.308  1.00 2.00  ? 443  ASP B N   1 
ATOM   8300  C  CA  . ASP B  1 443 ? 27.697  38.508  21.880  1.00 2.70  ? 443  ASP B CA  1 
ATOM   8301  C  C   . ASP B  1 443 ? 27.186  39.576  22.862  1.00 2.71  ? 443  ASP B C   1 
ATOM   8302  O  O   . ASP B  1 443 ? 26.028  40.004  22.795  1.00 2.15  ? 443  ASP B O   1 
ATOM   8303  C  CB  . ASP B  1 443 ? 27.899  37.149  22.596  1.00 2.00  ? 443  ASP B CB  1 
ATOM   8304  C  CG  . ASP B  1 443 ? 26.606  36.569  23.211  1.00 2.00  ? 443  ASP B CG  1 
ATOM   8305  O  OD1 . ASP B  1 443 ? 25.484  37.052  22.928  1.00 2.00  ? 443  ASP B OD1 1 
ATOM   8306  O  OD2 . ASP B  1 443 ? 26.727  35.593  23.988  1.00 2.00  ? 443  ASP B OD2 1 
ATOM   8307  N  N   . HIS B  1 444 ? 28.063  40.022  23.755  1.00 2.00  ? 444  HIS B N   1 
ATOM   8308  C  CA  . HIS B  1 444 ? 27.703  41.030  24.743  1.00 2.00  ? 444  HIS B CA  1 
ATOM   8309  C  C   . HIS B  1 444 ? 27.551  42.430  24.165  1.00 2.00  ? 444  HIS B C   1 
ATOM   8310  O  O   . HIS B  1 444 ? 27.052  43.327  24.835  1.00 2.64  ? 444  HIS B O   1 
ATOM   8311  C  CB  . HIS B  1 444 ? 28.728  41.034  25.873  1.00 2.36  ? 444  HIS B CB  1 
ATOM   8312  C  CG  . HIS B  1 444 ? 28.614  39.853  26.779  1.00 2.41  ? 444  HIS B CG  1 
ATOM   8313  N  ND1 . HIS B  1 444 ? 28.035  39.926  28.027  1.00 2.57  ? 444  HIS B ND1 1 
ATOM   8314  C  CD2 . HIS B  1 444 ? 28.936  38.553  26.588  1.00 2.45  ? 444  HIS B CD2 1 
ATOM   8315  C  CE1 . HIS B  1 444 ? 28.001  38.720  28.565  1.00 3.22  ? 444  HIS B CE1 1 
ATOM   8316  N  NE2 . HIS B  1 444 ? 28.539  37.869  27.712  1.00 4.45  ? 444  HIS B NE2 1 
ATOM   8317  N  N   . GLY B  1 445 ? 27.996  42.624  22.930  1.00 2.34  ? 445  GLY B N   1 
ATOM   8318  C  CA  . GLY B  1 445 ? 27.842  43.924  22.297  1.00 2.52  ? 445  GLY B CA  1 
ATOM   8319  C  C   . GLY B  1 445 ? 28.858  45.008  22.584  1.00 2.00  ? 445  GLY B C   1 
ATOM   8320  O  O   . GLY B  1 445 ? 28.618  46.173  22.281  1.00 2.00  ? 445  GLY B O   1 
ATOM   8321  N  N   . MET B  1 446 ? 29.993  44.636  23.156  1.00 2.00  ? 446  MET B N   1 
ATOM   8322  C  CA  . MET B  1 446 ? 31.032  45.604  23.461  1.00 2.00  ? 446  MET B CA  1 
ATOM   8323  C  C   . MET B  1 446 ? 31.317  46.530  22.290  1.00 2.27  ? 446  MET B C   1 
ATOM   8324  O  O   . MET B  1 446 ? 31.157  46.154  21.133  1.00 3.54  ? 446  MET B O   1 
ATOM   8325  C  CB  . MET B  1 446 ? 32.325  44.888  23.818  1.00 2.00  ? 446  MET B CB  1 
ATOM   8326  C  CG  . MET B  1 446 ? 32.202  43.951  24.985  1.00 2.00  ? 446  MET B CG  1 
ATOM   8327  S  SD  . MET B  1 446 ? 31.796  44.825  26.500  1.00 2.00  ? 446  MET B SD  1 
ATOM   8328  C  CE  . MET B  1 446 ? 33.238  45.857  26.621  1.00 2.59  ? 446  MET B CE  1 
ATOM   8329  N  N   . PRO B  1 447 ? 31.698  47.777  22.584  1.00 2.00  ? 447  PRO B N   1 
ATOM   8330  C  CA  . PRO B  1 447 ? 32.025  48.762  21.555  1.00 2.00  ? 447  PRO B CA  1 
ATOM   8331  C  C   . PRO B  1 447 ? 33.468  48.411  21.206  1.00 2.53  ? 447  PRO B C   1 
ATOM   8332  O  O   . PRO B  1 447 ? 33.999  47.439  21.734  1.00 4.21  ? 447  PRO B O   1 
ATOM   8333  C  CB  . PRO B  1 447 ? 31.932  50.084  22.300  1.00 2.00  ? 447  PRO B CB  1 
ATOM   8334  C  CG  . PRO B  1 447 ? 30.959  49.791  23.396  1.00 2.00  ? 447  PRO B CG  1 
ATOM   8335  C  CD  . PRO B  1 447 ? 31.405  48.445  23.859  1.00 2.46  ? 447  PRO B CD  1 
ATOM   8336  N  N   . GLY B  1 448 ? 34.118  49.196  20.357  1.00 2.84  ? 448  GLY B N   1 
ATOM   8337  C  CA  . GLY B  1 448 ? 35.487  48.876  19.984  1.00 2.00  ? 448  GLY B CA  1 
ATOM   8338  C  C   . GLY B  1 448 ? 36.624  49.368  20.864  1.00 2.00  ? 448  GLY B C   1 
ATOM   8339  O  O   . GLY B  1 448 ? 36.427  49.998  21.897  1.00 2.00  ? 448  GLY B O   1 
ATOM   8340  N  N   . TYR B  1 449 ? 37.836  49.055  20.434  1.00 2.00  ? 449  TYR B N   1 
ATOM   8341  C  CA  . TYR B  1 449 ? 39.053  49.454  21.124  1.00 2.00  ? 449  TYR B CA  1 
ATOM   8342  C  C   . TYR B  1 449 ? 39.099  50.980  21.281  1.00 3.10  ? 449  TYR B C   1 
ATOM   8343  O  O   . TYR B  1 449 ? 39.323  51.494  22.373  1.00 2.00  ? 449  TYR B O   1 
ATOM   8344  C  CB  . TYR B  1 449 ? 40.252  48.963  20.307  1.00 2.26  ? 449  TYR B CB  1 
ATOM   8345  C  CG  . TYR B  1 449 ? 41.621  49.366  20.804  1.00 2.00  ? 449  TYR B CG  1 
ATOM   8346  C  CD1 . TYR B  1 449 ? 42.147  48.838  21.984  1.00 2.97  ? 449  TYR B CD1 1 
ATOM   8347  C  CD2 . TYR B  1 449 ? 42.411  50.246  20.070  1.00 2.00  ? 449  TYR B CD2 1 
ATOM   8348  C  CE1 . TYR B  1 449 ? 43.431  49.179  22.416  1.00 2.74  ? 449  TYR B CE1 1 
ATOM   8349  C  CE2 . TYR B  1 449 ? 43.690  50.590  20.494  1.00 2.00  ? 449  TYR B CE2 1 
ATOM   8350  C  CZ  . TYR B  1 449 ? 44.192  50.055  21.665  1.00 2.00  ? 449  TYR B CZ  1 
ATOM   8351  O  OH  . TYR B  1 449 ? 45.445  50.414  22.091  1.00 2.00  ? 449  TYR B OH  1 
ATOM   8352  N  N   . ASN B  1 450 ? 38.878  51.704  20.186  1.00 3.36  ? 450  ASN B N   1 
ATOM   8353  C  CA  . ASN B  1 450 ? 38.914  53.157  20.237  1.00 3.28  ? 450  ASN B CA  1 
ATOM   8354  C  C   . ASN B  1 450 ? 37.861  53.765  21.143  1.00 4.75  ? 450  ASN B C   1 
ATOM   8355  O  O   . ASN B  1 450 ? 38.162  54.640  21.961  1.00 5.35  ? 450  ASN B O   1 
ATOM   8356  C  CB  . ASN B  1 450 ? 38.782  53.754  18.838  1.00 4.22  ? 450  ASN B CB  1 
ATOM   8357  C  CG  . ASN B  1 450 ? 40.117  53.886  18.146  1.00 6.72  ? 450  ASN B CG  1 
ATOM   8358  O  OD1 . ASN B  1 450 ? 41.106  54.262  18.770  1.00 8.78  ? 450  ASN B OD1 1 
ATOM   8359  N  ND2 . ASN B  1 450 ? 40.156  53.590  16.850  1.00 9.01  ? 450  ASN B ND2 1 
ATOM   8360  N  N   . SER B  1 451 ? 36.623  53.318  21.016  1.00 2.63  ? 451  SER B N   1 
ATOM   8361  C  CA  . SER B  1 451 ? 35.604  53.895  21.862  1.00 3.25  ? 451  SER B CA  1 
ATOM   8362  C  C   . SER B  1 451 ? 35.893  53.649  23.346  1.00 4.06  ? 451  SER B C   1 
ATOM   8363  O  O   . SER B  1 451 ? 35.273  54.262  24.216  1.00 5.24  ? 451  SER B O   1 
ATOM   8364  C  CB  . SER B  1 451 ? 34.233  53.359  21.474  1.00 2.76  ? 451  SER B CB  1 
ATOM   8365  O  OG  . SER B  1 451 ? 33.387  54.452  21.163  1.00 7.88  ? 451  SER B OG  1 
ATOM   8366  N  N   . TRP B  1 452 ? 36.841  52.760  23.635  1.00 3.25  ? 452  TRP B N   1 
ATOM   8367  C  CA  . TRP B  1 452 ? 37.210  52.463  25.017  1.00 2.00  ? 452  TRP B CA  1 
ATOM   8368  C  C   . TRP B  1 452 ? 38.463  53.230  25.375  1.00 2.00  ? 452  TRP B C   1 
ATOM   8369  O  O   . TRP B  1 452 ? 38.621  53.676  26.501  1.00 2.00  ? 452  TRP B O   1 
ATOM   8370  C  CB  . TRP B  1 452 ? 37.451  50.970  25.210  1.00 2.53  ? 452  TRP B CB  1 
ATOM   8371  C  CG  . TRP B  1 452 ? 36.194  50.180  25.319  1.00 2.06  ? 452  TRP B CG  1 
ATOM   8372  C  CD1 . TRP B  1 452 ? 35.762  49.197  24.478  1.00 2.00  ? 452  TRP B CD1 1 
ATOM   8373  C  CD2 . TRP B  1 452 ? 35.208  50.294  26.346  1.00 2.58  ? 452  TRP B CD2 1 
ATOM   8374  N  NE1 . TRP B  1 452 ? 34.571  48.691  24.920  1.00 2.00  ? 452  TRP B NE1 1 
ATOM   8375  C  CE2 . TRP B  1 452 ? 34.206  49.347  26.067  1.00 2.13  ? 452  TRP B CE2 1 
ATOM   8376  C  CE3 . TRP B  1 452 ? 35.074  51.108  27.480  1.00 2.18  ? 452  TRP B CE3 1 
ATOM   8377  C  CZ2 . TRP B  1 452 ? 33.078  49.189  26.882  1.00 2.01  ? 452  TRP B CZ2 1 
ATOM   8378  C  CZ3 . TRP B  1 452 ? 33.952  50.948  28.290  1.00 2.09  ? 452  TRP B CZ3 1 
ATOM   8379  C  CH2 . TRP B  1 452 ? 32.971  49.996  27.985  1.00 2.00  ? 452  TRP B CH2 1 
ATOM   8380  N  N   . ARG B  1 453 ? 39.371  53.360  24.416  1.00 2.43  ? 453  ARG B N   1 
ATOM   8381  C  CA  . ARG B  1 453 ? 40.588  54.126  24.651  1.00 2.72  ? 453  ARG B CA  1 
ATOM   8382  C  C   . ARG B  1 453 ? 40.056  55.508  25.010  1.00 2.00  ? 453  ARG B C   1 
ATOM   8383  O  O   . ARG B  1 453 ? 40.667  56.242  25.784  1.00 2.00  ? 453  ARG B O   1 
ATOM   8384  C  CB  . ARG B  1 453 ? 41.438  54.214  23.372  1.00 2.57  ? 453  ARG B CB  1 
ATOM   8385  C  CG  . ARG B  1 453 ? 42.270  52.974  23.030  1.00 2.10  ? 453  ARG B CG  1 
ATOM   8386  C  CD  . ARG B  1 453 ? 43.641  52.988  23.727  1.00 3.65  ? 453  ARG B CD  1 
ATOM   8387  N  NE  . ARG B  1 453 ? 44.332  54.270  23.540  1.00 5.36  ? 453  ARG B NE  1 
ATOM   8388  C  CZ  . ARG B  1 453 ? 45.642  54.467  23.697  1.00 4.14  ? 453  ARG B CZ  1 
ATOM   8389  N  NH1 . ARG B  1 453 ? 46.435  53.464  24.046  1.00 5.11  ? 453  ARG B NH1 1 
ATOM   8390  N  NH2 . ARG B  1 453 ? 46.165  55.673  23.502  1.00 2.66  ? 453  ARG B NH2 1 
ATOM   8391  N  N   . GLY B  1 454 ? 38.899  55.842  24.438  1.00 2.00  ? 454  GLY B N   1 
ATOM   8392  C  CA  . GLY B  1 454 ? 38.284  57.126  24.701  1.00 2.22  ? 454  GLY B CA  1 
ATOM   8393  C  C   . GLY B  1 454 ? 37.814  57.190  26.138  1.00 2.62  ? 454  GLY B C   1 
ATOM   8394  O  O   . GLY B  1 454 ? 38.285  58.007  26.925  1.00 2.95  ? 454  GLY B O   1 
ATOM   8395  N  N   . PHE B  1 455 ? 36.880  56.313  26.480  1.00 2.71  ? 455  PHE B N   1 
ATOM   8396  C  CA  . PHE B  1 455 ? 36.333  56.247  27.828  1.00 2.22  ? 455  PHE B CA  1 
ATOM   8397  C  C   . PHE B  1 455 ? 37.381  56.536  28.897  1.00 2.00  ? 455  PHE B C   1 
ATOM   8398  O  O   . PHE B  1 455 ? 37.045  57.020  29.975  1.00 2.38  ? 455  PHE B O   1 
ATOM   8399  C  CB  . PHE B  1 455 ? 35.740  54.857  28.071  1.00 2.63  ? 455  PHE B CB  1 
ATOM   8400  C  CG  . PHE B  1 455 ? 35.246  54.649  29.464  1.00 2.00  ? 455  PHE B CG  1 
ATOM   8401  C  CD1 . PHE B  1 455 ? 34.019  55.166  29.862  1.00 2.00  ? 455  PHE B CD1 1 
ATOM   8402  C  CD2 . PHE B  1 455 ? 36.019  53.954  30.386  1.00 2.00  ? 455  PHE B CD2 1 
ATOM   8403  C  CE1 . PHE B  1 455 ? 33.562  54.998  31.155  1.00 2.14  ? 455  PHE B CE1 1 
ATOM   8404  C  CE2 . PHE B  1 455 ? 35.573  53.780  31.684  1.00 3.40  ? 455  PHE B CE2 1 
ATOM   8405  C  CZ  . PHE B  1 455 ? 34.338  54.304  32.070  1.00 3.57  ? 455  PHE B CZ  1 
ATOM   8406  N  N   . CYS B  1 456 ? 38.644  56.242  28.593  1.00 2.00  ? 456  CYS B N   1 
ATOM   8407  C  CA  . CYS B  1 456 ? 39.732  56.443  29.548  1.00 2.56  ? 456  CYS B CA  1 
ATOM   8408  C  C   . CYS B  1 456 ? 40.581  57.707  29.372  1.00 3.20  ? 456  CYS B C   1 
ATOM   8409  O  O   . CYS B  1 456 ? 41.188  58.177  30.331  1.00 3.61  ? 456  CYS B O   1 
ATOM   8410  C  CB  . CYS B  1 456 ? 40.634  55.199  29.578  1.00 2.00  ? 456  CYS B CB  1 
ATOM   8411  S  SG  . CYS B  1 456 ? 39.798  53.708  30.225  1.00 2.16  ? 456  CYS B SG  1 
ATOM   8412  N  N   . GLY B  1 457 ? 40.628  58.266  28.169  1.00 2.69  ? 457  GLY B N   1 
ATOM   8413  C  CA  . GLY B  1 457 ? 41.412  59.475  27.975  1.00 3.01  ? 457  GLY B CA  1 
ATOM   8414  C  C   . GLY B  1 457 ? 42.766  59.237  27.337  1.00 4.44  ? 457  GLY B C   1 
ATOM   8415  O  O   . GLY B  1 457 ? 43.777  59.848  27.710  1.00 4.25  ? 457  GLY B O   1 
ATOM   8416  N  N   . LEU B  1 458 ? 42.772  58.330  26.368  1.00 4.71  ? 458  LEU B N   1 
ATOM   8417  C  CA  . LEU B  1 458 ? 43.967  57.969  25.625  1.00 5.46  ? 458  LEU B CA  1 
ATOM   8418  C  C   . LEU B  1 458 ? 43.639  58.213  24.169  1.00 7.37  ? 458  LEU B C   1 
ATOM   8419  O  O   . LEU B  1 458 ? 42.474  58.150  23.792  1.00 9.21  ? 458  LEU B O   1 
ATOM   8420  C  CB  . LEU B  1 458 ? 44.303  56.500  25.851  1.00 4.16  ? 458  LEU B CB  1 
ATOM   8421  C  CG  . LEU B  1 458 ? 44.825  56.214  27.258  1.00 3.97  ? 458  LEU B CG  1 
ATOM   8422  C  CD1 . LEU B  1 458 ? 43.696  56.033  28.270  1.00 3.52  ? 458  LEU B CD1 1 
ATOM   8423  C  CD2 . LEU B  1 458 ? 45.654  54.970  27.175  1.00 4.41  ? 458  LEU B CD2 1 
ATOM   8424  N  N   . SER B  1 459 ? 44.653  58.490  23.354  1.00 8.13  ? 459  SER B N   1 
ATOM   8425  C  CA  . SER B  1 459 ? 44.436  58.766  21.935  1.00 8.28  ? 459  SER B CA  1 
ATOM   8426  C  C   . SER B  1 459 ? 43.781  57.603  21.203  1.00 8.85  ? 459  SER B C   1 
ATOM   8427  O  O   . SER B  1 459 ? 44.125  56.443  21.427  1.00 9.04  ? 459  SER B O   1 
ATOM   8428  C  CB  . SER B  1 459 ? 45.758  59.080  21.249  1.00 8.81  ? 459  SER B CB  1 
ATOM   8429  O  OG  . SER B  1 459 ? 46.464  57.880  20.986  1.00 11.28 ? 459  SER B OG  1 
ATOM   8430  N  N   . GLN B  1 460 ? 42.842  57.923  20.319  1.00 9.81  ? 460  GLN B N   1 
ATOM   8431  C  CA  . GLN B  1 460 ? 42.150  56.906  19.532  1.00 10.25 ? 460  GLN B CA  1 
ATOM   8432  C  C   . GLN B  1 460 ? 42.857  56.827  18.153  1.00 10.12 ? 460  GLN B C   1 
ATOM   8433  O  O   . GLN B  1 460 ? 42.443  57.468  17.186  1.00 10.42 ? 460  GLN B O   1 
ATOM   8434  C  CB  . GLN B  1 460 ? 40.667  57.294  19.381  1.00 9.58  ? 460  GLN B CB  1 
ATOM   8435  C  CG  . GLN B  1 460 ? 40.048  57.929  20.636  1.00 8.90  ? 460  GLN B CG  1 
ATOM   8436  C  CD  . GLN B  1 460 ? 38.567  58.278  20.480  1.00 9.64  ? 460  GLN B CD  1 
ATOM   8437  O  OE1 . GLN B  1 460 ? 37.706  57.406  20.517  1.00 10.95 ? 460  GLN B OE1 1 
ATOM   8438  N  NE2 . GLN B  1 460 ? 38.273  59.559  20.299  1.00 9.60  ? 460  GLN B NE2 1 
ATOM   8439  N  N   . PRO B  1 461 ? 43.927  56.019  18.053  1.00 8.32  ? 461  PRO B N   1 
ATOM   8440  C  CA  . PRO B  1 461 ? 44.674  55.882  16.805  1.00 8.09  ? 461  PRO B CA  1 
ATOM   8441  C  C   . PRO B  1 461 ? 43.799  55.406  15.682  1.00 9.38  ? 461  PRO B C   1 
ATOM   8442  O  O   . PRO B  1 461 ? 42.853  54.659  15.908  1.00 7.77  ? 461  PRO B O   1 
ATOM   8443  C  CB  . PRO B  1 461 ? 45.733  54.862  17.160  1.00 8.62  ? 461  PRO B CB  1 
ATOM   8444  C  CG  . PRO B  1 461 ? 44.962  53.941  18.011  1.00 9.30  ? 461  PRO B CG  1 
ATOM   8445  C  CD  . PRO B  1 461 ? 44.258  54.902  18.951  1.00 8.99  ? 461  PRO B CD  1 
ATOM   8446  N  N   . LYS B  1 462 ? 44.134  55.849  14.473  1.00 11.56 ? 462  LYS B N   1 
ATOM   8447  C  CA  . LYS B  1 462 ? 43.400  55.494  13.264  1.00 14.10 ? 462  LYS B CA  1 
ATOM   8448  C  C   . LYS B  1 462 ? 44.397  55.055  12.179  1.00 15.06 ? 462  LYS B C   1 
ATOM   8449  O  O   . LYS B  1 462 ? 44.133  54.125  11.408  1.00 15.01 ? 462  LYS B O   1 
ATOM   8450  C  CB  . LYS B  1 462 ? 42.563  56.696  12.791  1.00 14.62 ? 462  LYS B CB  1 
ATOM   8451  C  CG  . LYS B  1 462 ? 42.177  57.661  13.923  1.00 16.13 ? 462  LYS B CG  1 
ATOM   8452  C  CD  . LYS B  1 462 ? 40.788  58.290  13.755  1.00 17.71 ? 462  LYS B CD  1 
ATOM   8453  C  CE  . LYS B  1 462 ? 39.678  57.454  14.428  1.00 18.68 ? 462  LYS B CE  1 
ATOM   8454  N  NZ  . LYS B  1 462 ? 38.986  56.482  13.521  1.00 19.69 ? 462  LYS B NZ  1 
ATOM   8455  N  N   . THR B  1 463 ? 45.551  55.714  12.131  1.00 15.05 ? 463  THR B N   1 
ATOM   8456  C  CA  . THR B  1 463 ? 46.571  55.362  11.153  1.00 15.15 ? 463  THR B CA  1 
ATOM   8457  C  C   . THR B  1 463 ? 47.316  54.123  11.625  1.00 15.50 ? 463  THR B C   1 
ATOM   8458  O  O   . THR B  1 463 ? 47.489  53.915  12.825  1.00 16.37 ? 463  THR B O   1 
ATOM   8459  C  CB  . THR B  1 463 ? 47.577  56.514  10.944  1.00 15.17 ? 463  THR B CB  1 
ATOM   8460  O  OG1 . THR B  1 463 ? 48.075  56.966  12.209  1.00 13.92 ? 463  THR B OG1 1 
ATOM   8461  C  CG2 . THR B  1 463 ? 46.906  57.670  10.234  1.00 15.77 ? 463  THR B CG2 1 
ATOM   8462  N  N   . LEU B  1 464 ? 47.734  53.287  10.681  1.00 15.42 ? 464  LEU B N   1 
ATOM   8463  C  CA  . LEU B  1 464 ? 48.463  52.076  11.016  1.00 13.78 ? 464  LEU B CA  1 
ATOM   8464  C  C   . LEU B  1 464 ? 49.762  52.514  11.669  1.00 14.00 ? 464  LEU B C   1 
ATOM   8465  O  O   . LEU B  1 464 ? 50.335  51.792  12.478  1.00 14.36 ? 464  LEU B O   1 
ATOM   8466  C  CB  . LEU B  1 464 ? 48.678  51.234  9.744   1.00 13.53 ? 464  LEU B CB  1 
ATOM   8467  C  CG  . LEU B  1 464 ? 49.900  50.393  9.343   1.00 13.64 ? 464  LEU B CG  1 
ATOM   8468  C  CD1 . LEU B  1 464 ? 50.794  51.247  8.465   1.00 13.88 ? 464  LEU B CD1 1 
ATOM   8469  C  CD2 . LEU B  1 464 ? 50.651  49.840  10.545  1.00 14.44 ? 464  LEU B CD2 1 
ATOM   8470  N  N   . LYS B  1 465 ? 50.208  53.721  11.342  1.00 15.32 ? 465  LYS B N   1 
ATOM   8471  C  CA  . LYS B  1 465 ? 51.427  54.246  11.941  1.00 17.85 ? 465  LYS B CA  1 
ATOM   8472  C  C   . LYS B  1 465 ? 51.032  54.705  13.337  1.00 15.97 ? 465  LYS B C   1 
ATOM   8473  O  O   . LYS B  1 465 ? 51.867  54.841  14.230  1.00 15.75 ? 465  LYS B O   1 
ATOM   8474  C  CB  . LYS B  1 465 ? 51.968  55.424  11.125  1.00 21.88 ? 465  LYS B CB  1 
ATOM   8475  C  CG  . LYS B  1 465 ? 53.496  55.467  11.050  1.00 28.32 ? 465  LYS B CG  1 
ATOM   8476  C  CD  . LYS B  1 465 ? 53.983  56.244  9.821   1.00 31.55 ? 465  LYS B CD  1 
ATOM   8477  C  CE  . LYS B  1 465 ? 55.395  55.807  9.414   1.00 33.09 ? 465  LYS B CE  1 
ATOM   8478  N  NZ  . LYS B  1 465 ? 56.412  56.894  9.537   1.00 35.21 ? 465  LYS B NZ  1 
ATOM   8479  N  N   . GLY B  1 466 ? 49.736  54.933  13.511  1.00 15.07 ? 466  GLY B N   1 
ATOM   8480  C  CA  . GLY B  1 466 ? 49.223  55.364  14.796  1.00 13.75 ? 466  GLY B CA  1 
ATOM   8481  C  C   . GLY B  1 466 ? 49.115  54.200  15.763  1.00 12.22 ? 466  GLY B C   1 
ATOM   8482  O  O   . GLY B  1 466 ? 49.488  54.320  16.936  1.00 12.25 ? 466  GLY B O   1 
ATOM   8483  N  N   . LEU B  1 467 ? 48.604  53.070  15.279  1.00 9.18  ? 467  LEU B N   1 
ATOM   8484  C  CA  . LEU B  1 467 ? 48.469  51.906  16.133  1.00 6.78  ? 467  LEU B CA  1 
ATOM   8485  C  C   . LEU B  1 467 ? 49.860  51.535  16.634  1.00 10.04 ? 467  LEU B C   1 
ATOM   8486  O  O   . LEU B  1 467 ? 50.034  51.118  17.788  1.00 9.90  ? 467  LEU B O   1 
ATOM   8487  C  CB  . LEU B  1 467 ? 47.870  50.731  15.368  1.00 4.17  ? 467  LEU B CB  1 
ATOM   8488  C  CG  . LEU B  1 467 ? 47.477  49.583  16.303  1.00 2.91  ? 467  LEU B CG  1 
ATOM   8489  C  CD1 . LEU B  1 467 ? 46.070  49.797  16.845  1.00 2.00  ? 467  LEU B CD1 1 
ATOM   8490  C  CD2 . LEU B  1 467 ? 47.534  48.286  15.558  1.00 2.46  ? 467  LEU B CD2 1 
ATOM   8491  N  N   . GLN B  1 468 ? 50.854  51.706  15.764  1.00 9.13  ? 468  GLN B N   1 
ATOM   8492  C  CA  . GLN B  1 468 ? 52.235  51.391  16.107  1.00 8.96  ? 468  GLN B CA  1 
ATOM   8493  C  C   . GLN B  1 468 ? 52.742  52.204  17.291  1.00 8.01  ? 468  GLN B C   1 
ATOM   8494  O  O   . GLN B  1 468 ? 53.435  51.682  18.165  1.00 5.45  ? 468  GLN B O   1 
ATOM   8495  C  CB  . GLN B  1 468 ? 53.128  51.602  14.893  1.00 12.57 ? 468  GLN B CB  1 
ATOM   8496  C  CG  . GLN B  1 468 ? 52.890  50.551  13.830  1.00 17.00 ? 468  GLN B CG  1 
ATOM   8497  C  CD  . GLN B  1 468 ? 53.851  50.656  12.672  1.00 19.49 ? 468  GLN B CD  1 
ATOM   8498  O  OE1 . GLN B  1 468 ? 53.888  49.775  11.804  1.00 21.31 ? 468  GLN B OE1 1 
ATOM   8499  N  NE2 . GLN B  1 468 ? 54.638  51.735  12.644  1.00 20.46 ? 468  GLN B NE2 1 
ATOM   8500  N  N   . ALA B  1 469 ? 52.387  53.481  17.322  1.00 7.52  ? 469  ALA B N   1 
ATOM   8501  C  CA  . ALA B  1 469 ? 52.792  54.338  18.424  1.00 7.43  ? 469  ALA B CA  1 
ATOM   8502  C  C   . ALA B  1 469 ? 52.328  53.727  19.747  1.00 6.48  ? 469  ALA B C   1 
ATOM   8503  O  O   . ALA B  1 469 ? 53.127  53.578  20.670  1.00 8.15  ? 469  ALA B O   1 
ATOM   8504  C  CB  . ALA B  1 469 ? 52.200  55.728  18.251  1.00 6.36  ? 469  ALA B CB  1 
ATOM   8505  N  N   . VAL B  1 470 ? 51.045  53.364  19.827  1.00 5.85  ? 470  VAL B N   1 
ATOM   8506  C  CA  . VAL B  1 470 ? 50.461  52.774  21.047  1.00 7.30  ? 470  VAL B CA  1 
ATOM   8507  C  C   . VAL B  1 470 ? 51.005  51.381  21.393  1.00 4.26  ? 470  VAL B C   1 
ATOM   8508  O  O   . VAL B  1 470 ? 51.525  51.151  22.504  1.00 2.00  ? 470  VAL B O   1 
ATOM   8509  C  CB  . VAL B  1 470 ? 48.886  52.686  20.949  1.00 5.59  ? 470  VAL B CB  1 
ATOM   8510  C  CG1 . VAL B  1 470 ? 48.347  51.636  21.900  1.00 4.51  ? 470  VAL B CG1 1 
ATOM   8511  C  CG2 . VAL B  1 470 ? 48.256  54.019  21.323  1.00 5.94  ? 470  VAL B CG2 1 
ATOM   8512  N  N   . LEU B  1 471 ? 50.872  50.463  20.436  1.00 3.38  ? 471  LEU B N   1 
ATOM   8513  C  CA  . LEU B  1 471 ? 51.320  49.085  20.612  1.00 4.34  ? 471  LEU B CA  1 
ATOM   8514  C  C   . LEU B  1 471 ? 52.832  48.940  20.678  1.00 5.23  ? 471  LEU B C   1 
ATOM   8515  O  O   . LEU B  1 471 ? 53.344  47.921  21.143  1.00 2.79  ? 471  LEU B O   1 
ATOM   8516  C  CB  . LEU B  1 471 ? 50.761  48.210  19.493  1.00 2.00  ? 471  LEU B CB  1 
ATOM   8517  C  CG  . LEU B  1 471 ? 49.539  47.383  19.879  1.00 2.00  ? 471  LEU B CG  1 
ATOM   8518  C  CD1 . LEU B  1 471 ? 48.933  47.881  21.176  1.00 2.00  ? 471  LEU B CD1 1 
ATOM   8519  C  CD2 . LEU B  1 471 ? 48.541  47.453  18.756  1.00 2.66  ? 471  LEU B CD2 1 
ATOM   8520  N  N   . LYS B  1 472 ? 53.538  49.968  20.217  1.00 6.26  ? 472  LYS B N   1 
ATOM   8521  C  CA  . LYS B  1 472 ? 54.991  49.966  20.227  1.00 5.81  ? 472  LYS B CA  1 
ATOM   8522  C  C   . LYS B  1 472 ? 55.469  48.645  19.638  1.00 6.24  ? 472  LYS B C   1 
ATOM   8523  O  O   . LYS B  1 472 ? 56.118  47.850  20.319  1.00 6.72  ? 472  LYS B O   1 
ATOM   8524  C  CB  . LYS B  1 472 ? 55.480  50.117  21.660  1.00 8.15  ? 472  LYS B CB  1 
ATOM   8525  C  CG  . LYS B  1 472 ? 56.836  50.745  21.784  1.00 12.40 ? 472  LYS B CG  1 
ATOM   8526  C  CD  . LYS B  1 472 ? 56.825  51.693  22.954  1.00 17.21 ? 472  LYS B CD  1 
ATOM   8527  C  CE  . LYS B  1 472 ? 55.793  52.782  22.707  1.00 20.92 ? 472  LYS B CE  1 
ATOM   8528  N  NZ  . LYS B  1 472 ? 55.632  53.711  23.863  1.00 26.72 ? 472  LYS B NZ  1 
ATOM   8529  N  N   . ASN B  1 473 ? 55.130  48.423  18.370  1.00 6.14  ? 473  ASN B N   1 
ATOM   8530  C  CA  . ASN B  1 473 ? 55.481  47.198  17.649  1.00 6.99  ? 473  ASN B CA  1 
ATOM   8531  C  C   . ASN B  1 473 ? 54.807  47.230  16.273  1.00 8.07  ? 473  ASN B C   1 
ATOM   8532  O  O   . ASN B  1 473 ? 53.579  47.261  16.187  1.00 8.71  ? 473  ASN B O   1 
ATOM   8533  C  CB  . ASN B  1 473 ? 54.986  45.978  18.436  1.00 5.03  ? 473  ASN B CB  1 
ATOM   8534  C  CG  . ASN B  1 473 ? 55.127  44.686  17.663  1.00 4.81  ? 473  ASN B CG  1 
ATOM   8535  O  OD1 . ASN B  1 473 ? 54.652  44.565  16.529  1.00 2.44  ? 473  ASN B OD1 1 
ATOM   8536  N  ND2 . ASN B  1 473 ? 55.773  43.701  18.282  1.00 5.11  ? 473  ASN B ND2 1 
ATOM   8537  N  N   . LYS B  1 474 ? 55.596  47.211  15.200  1.00 9.55  ? 474  LYS B N   1 
ATOM   8538  C  CA  . LYS B  1 474 ? 55.024  47.258  13.853  1.00 11.21 ? 474  LYS B CA  1 
ATOM   8539  C  C   . LYS B  1 474 ? 54.275  46.000  13.400  1.00 11.10 ? 474  LYS B C   1 
ATOM   8540  O  O   . LYS B  1 474 ? 53.066  46.043  13.147  1.00 10.53 ? 474  LYS B O   1 
ATOM   8541  C  CB  . LYS B  1 474 ? 56.098  47.563  12.804  1.00 12.85 ? 474  LYS B CB  1 
ATOM   8542  C  CG  . LYS B  1 474 ? 56.672  48.964  12.831  1.00 15.10 ? 474  LYS B CG  1 
ATOM   8543  C  CD  . LYS B  1 474 ? 57.975  49.000  13.599  1.00 18.82 ? 474  LYS B CD  1 
ATOM   8544  C  CE  . LYS B  1 474 ? 58.993  49.896  12.904  1.00 21.48 ? 474  LYS B CE  1 
ATOM   8545  N  NZ  . LYS B  1 474 ? 59.498  49.304  11.620  1.00 24.85 ? 474  LYS B NZ  1 
ATOM   8546  N  N   . ILE B  1 475 ? 54.992  44.885  13.290  1.00 9.76  ? 475  ILE B N   1 
ATOM   8547  C  CA  . ILE B  1 475 ? 54.375  43.656  12.817  1.00 8.75  ? 475  ILE B CA  1 
ATOM   8548  C  C   . ILE B  1 475 ? 53.128  43.214  13.582  1.00 8.60  ? 475  ILE B C   1 
ATOM   8549  O  O   . ILE B  1 475 ? 52.292  42.487  13.031  1.00 8.45  ? 475  ILE B O   1 
ATOM   8550  C  CB  . ILE B  1 475 ? 55.417  42.519  12.724  1.00 7.72  ? 475  ILE B CB  1 
ATOM   8551  C  CG1 . ILE B  1 475 ? 54.906  41.268  13.428  1.00 7.57  ? 475  ILE B CG1 1 
ATOM   8552  C  CG2 . ILE B  1 475 ? 56.752  43.007  13.257  1.00 7.29  ? 475  ILE B CG2 1 
ATOM   8553  C  CD1 . ILE B  1 475 ? 55.625  40.015  12.993  1.00 9.21  ? 475  ILE B CD1 1 
ATOM   8554  N  N   . LEU B  1 476 ? 52.986  43.635  14.838  1.00 7.04  ? 476  LEU B N   1 
ATOM   8555  C  CA  . LEU B  1 476 ? 51.767  43.283  15.556  1.00 5.58  ? 476  LEU B CA  1 
ATOM   8556  C  C   . LEU B  1 476 ? 50.748  44.289  15.059  1.00 5.64  ? 476  LEU B C   1 
ATOM   8557  O  O   . LEU B  1 476 ? 49.640  43.933  14.665  1.00 6.53  ? 476  LEU B O   1 
ATOM   8558  C  CB  . LEU B  1 476 ? 51.906  43.424  17.072  1.00 4.00  ? 476  LEU B CB  1 
ATOM   8559  C  CG  . LEU B  1 476 ? 50.538  43.341  17.778  1.00 3.10  ? 476  LEU B CG  1 
ATOM   8560  C  CD1 . LEU B  1 476 ? 49.821  42.062  17.373  1.00 2.00  ? 476  LEU B CD1 1 
ATOM   8561  C  CD2 . LEU B  1 476 ? 50.706  43.405  19.294  1.00 2.41  ? 476  LEU B CD2 1 
ATOM   8562  N  N   . ALA B  1 477 ? 51.144  45.554  15.061  1.00 4.74  ? 477  ALA B N   1 
ATOM   8563  C  CA  . ALA B  1 477 ? 50.260  46.613  14.605  1.00 5.81  ? 477  ALA B CA  1 
ATOM   8564  C  C   . ALA B  1 477 ? 49.756  46.319  13.194  1.00 6.28  ? 477  ALA B C   1 
ATOM   8565  O  O   . ALA B  1 477 ? 48.632  46.694  12.827  1.00 3.03  ? 477  ALA B O   1 
ATOM   8566  C  CB  . ALA B  1 477 ? 50.990  47.951  14.639  1.00 5.25  ? 477  ALA B CB  1 
ATOM   8567  N  N   . LYS B  1 478 ? 50.582  45.632  12.407  1.00 7.89  ? 478  LYS B N   1 
ATOM   8568  C  CA  . LYS B  1 478 ? 50.203  45.312  11.037  1.00 10.32 ? 478  LYS B CA  1 
ATOM   8569  C  C   . LYS B  1 478 ? 49.309  44.081  10.949  1.00 8.76  ? 478  LYS B C   1 
ATOM   8570  O  O   . LYS B  1 478 ? 48.172  44.177  10.489  1.00 8.32  ? 478  LYS B O   1 
ATOM   8571  C  CB  . LYS B  1 478 ? 51.445  45.131  10.154  1.00 13.12 ? 478  LYS B CB  1 
ATOM   8572  C  CG  . LYS B  1 478 ? 51.109  45.009  8.660   1.00 17.49 ? 478  LYS B CG  1 
ATOM   8573  C  CD  . LYS B  1 478 ? 52.353  45.063  7.766   1.00 20.87 ? 478  LYS B CD  1 
ATOM   8574  C  CE  . LYS B  1 478 ? 53.041  46.428  7.838   1.00 22.31 ? 478  LYS B CE  1 
ATOM   8575  N  NZ  . LYS B  1 478 ? 54.198  46.554  6.901   1.00 24.38 ? 478  LYS B NZ  1 
ATOM   8576  N  N   . LYS B  1 479 ? 49.806  42.929  11.390  1.00 7.58  ? 479  LYS B N   1 
ATOM   8577  C  CA  . LYS B  1 479 ? 48.999  41.712  11.329  1.00 7.71  ? 479  LYS B CA  1 
ATOM   8578  C  C   . LYS B  1 479 ? 47.585  42.021  11.811  1.00 7.40  ? 479  LYS B C   1 
ATOM   8579  O  O   . LYS B  1 479 ? 46.594  41.568  11.233  1.00 6.86  ? 479  LYS B O   1 
ATOM   8580  C  CB  . LYS B  1 479 ? 49.590  40.607  12.217  1.00 8.04  ? 479  LYS B CB  1 
ATOM   8581  C  CG  . LYS B  1 479 ? 50.917  40.010  11.756  1.00 9.77  ? 479  LYS B CG  1 
ATOM   8582  C  CD  . LYS B  1 479 ? 51.116  38.631  12.401  1.00 11.90 ? 479  LYS B CD  1 
ATOM   8583  C  CE  . LYS B  1 479 ? 52.537  38.088  12.249  1.00 12.22 ? 479  LYS B CE  1 
ATOM   8584  N  NZ  . LYS B  1 479 ? 53.298  38.130  13.542  1.00 12.89 ? 479  LYS B NZ  1 
ATOM   8585  N  N   . LEU B  1 480 ? 47.516  42.820  12.869  1.00 6.59  ? 480  LEU B N   1 
ATOM   8586  C  CA  . LEU B  1 480 ? 46.261  43.201  13.486  1.00 5.65  ? 480  LEU B CA  1 
ATOM   8587  C  C   . LEU B  1 480 ? 45.246  43.742  12.500  1.00 6.69  ? 480  LEU B C   1 
ATOM   8588  O  O   . LEU B  1 480 ? 44.202  43.126  12.280  1.00 7.26  ? 480  LEU B O   1 
ATOM   8589  C  CB  . LEU B  1 480 ? 46.525  44.224  14.591  1.00 5.08  ? 480  LEU B CB  1 
ATOM   8590  C  CG  . LEU B  1 480 ? 45.743  44.054  15.900  1.00 3.90  ? 480  LEU B CG  1 
ATOM   8591  C  CD1 . LEU B  1 480 ? 45.560  42.588  16.217  1.00 3.35  ? 480  LEU B CD1 1 
ATOM   8592  C  CD2 . LEU B  1 480 ? 46.489  44.736  17.032  1.00 3.89  ? 480  LEU B CD2 1 
ATOM   8593  N  N   . LEU B  1 481 ? 45.535  44.880  11.884  1.00 7.81  ? 481  LEU B N   1 
ATOM   8594  C  CA  . LEU B  1 481 ? 44.552  45.418  10.956  1.00 9.75  ? 481  LEU B CA  1 
ATOM   8595  C  C   . LEU B  1 481 ? 44.566  44.919  9.503   1.00 9.34  ? 481  LEU B C   1 
ATOM   8596  O  O   . LEU B  1 481 ? 43.838  45.441  8.662   1.00 8.82  ? 481  LEU B O   1 
ATOM   8597  C  CB  . LEU B  1 481 ? 44.559  46.944  11.014  1.00 8.72  ? 481  LEU B CB  1 
ATOM   8598  C  CG  . LEU B  1 481 ? 45.952  47.535  11.059  1.00 9.99  ? 481  LEU B CG  1 
ATOM   8599  C  CD1 . LEU B  1 481 ? 46.647  47.195  9.752   1.00 12.28 ? 481  LEU B CD1 1 
ATOM   8600  C  CD2 . LEU B  1 481 ? 45.876  49.036  11.268  1.00 11.45 ? 481  LEU B CD2 1 
ATOM   8601  N  N   . ASP B  1 482 ? 45.413  43.955  9.151   1.00 8.73  ? 482  ASP B N   1 
ATOM   8602  C  CA  . ASP B  1 482 ? 45.321  43.360  7.831   1.00 9.30  ? 482  ASP B CA  1 
ATOM   8603  C  C   . ASP B  1 482 ? 43.991  42.600  8.009   1.00 9.19  ? 482  ASP B C   1 
ATOM   8604  O  O   . ASP B  1 482 ? 43.421  42.074  7.058   1.00 9.93  ? 482  ASP B O   1 
ATOM   8605  C  CB  . ASP B  1 482 ? 46.445  42.302  7.514   1.00 12.32 ? 482  ASP B CB  1 
ATOM   8606  C  CG  . ASP B  1 482 ? 47.889  42.743  7.130   1.00 15.86 ? 482  ASP B CG  1 
ATOM   8607  O  OD1 . ASP B  1 482 ? 48.219  43.938  7.311   1.00 16.53 ? 482  ASP B OD1 1 
ATOM   8608  O  OD2 . ASP B  1 482 ? 48.670  41.889  6.663   1.00 16.07 ? 482  ASP B OD2 1 
ATOM   8609  N  N   . LEU B  1 483 ? 43.534  42.553  9.261   1.00 7.33  ? 483  LEU B N   1 
ATOM   8610  C  CA  . LEU B  1 483 ? 42.339  41.825  9.674   1.00 4.53  ? 483  LEU B CA  1 
ATOM   8611  C  C   . LEU B  1 483 ? 41.131  42.672  10.012  1.00 4.12  ? 483  LEU B C   1 
ATOM   8612  O  O   . LEU B  1 483 ? 40.028  42.417  9.536   1.00 4.43  ? 483  LEU B O   1 
ATOM   8613  C  CB  . LEU B  1 483 ? 42.663  40.986  10.898  1.00 4.52  ? 483  LEU B CB  1 
ATOM   8614  C  CG  . LEU B  1 483 ? 43.443  39.708  10.651  1.00 4.77  ? 483  LEU B CG  1 
ATOM   8615  C  CD1 . LEU B  1 483 ? 44.263  39.347  11.874  1.00 4.27  ? 483  LEU B CD1 1 
ATOM   8616  C  CD2 . LEU B  1 483 ? 42.458  38.611  10.303  1.00 6.24  ? 483  LEU B CD2 1 
ATOM   8617  N  N   . TYR B  1 484 ? 41.328  43.661  10.872  1.00 3.12  ? 484  TYR B N   1 
ATOM   8618  C  CA  . TYR B  1 484 ? 40.221  44.507  11.279  1.00 2.17  ? 484  TYR B CA  1 
ATOM   8619  C  C   . TYR B  1 484 ? 39.997  45.651  10.324  1.00 2.00  ? 484  TYR B C   1 
ATOM   8620  O  O   . TYR B  1 484 ? 38.889  46.150  10.204  1.00 2.00  ? 484  TYR B O   1 
ATOM   8621  C  CB  . TYR B  1 484 ? 40.452  45.003  12.707  1.00 2.59  ? 484  TYR B CB  1 
ATOM   8622  C  CG  . TYR B  1 484 ? 40.178  43.912  13.723  1.00 2.96  ? 484  TYR B CG  1 
ATOM   8623  C  CD1 . TYR B  1 484 ? 38.871  43.530  14.019  1.00 2.00  ? 484  TYR B CD1 1 
ATOM   8624  C  CD2 . TYR B  1 484 ? 41.220  43.218  14.332  1.00 2.00  ? 484  TYR B CD2 1 
ATOM   8625  C  CE1 . TYR B  1 484 ? 38.611  42.497  14.883  1.00 2.00  ? 484  TYR B CE1 1 
ATOM   8626  C  CE2 . TYR B  1 484 ? 40.968  42.180  15.198  1.00 2.00  ? 484  TYR B CE2 1 
ATOM   8627  C  CZ  . TYR B  1 484 ? 39.660  41.824  15.470  1.00 2.00  ? 484  TYR B CZ  1 
ATOM   8628  O  OH  . TYR B  1 484 ? 39.405  40.789  16.341  1.00 4.35  ? 484  TYR B OH  1 
ATOM   8629  N  N   . LYS B  1 485 ? 41.060  46.032  9.628   1.00 3.83  ? 485  LYS B N   1 
ATOM   8630  C  CA  . LYS B  1 485 ? 41.049  47.111  8.642   1.00 3.43  ? 485  LYS B CA  1 
ATOM   8631  C  C   . LYS B  1 485 ? 41.070  48.523  9.217   1.00 3.13  ? 485  LYS B C   1 
ATOM   8632  O  O   . LYS B  1 485 ? 41.404  49.475  8.511   1.00 3.37  ? 485  LYS B O   1 
ATOM   8633  C  CB  . LYS B  1 485 ? 39.879  46.936  7.674   1.00 4.55  ? 485  LYS B CB  1 
ATOM   8634  C  CG  . LYS B  1 485 ? 40.063  45.751  6.730   1.00 7.99  ? 485  LYS B CG  1 
ATOM   8635  C  CD  . LYS B  1 485 ? 41.419  45.830  6.014   1.00 11.62 ? 485  LYS B CD  1 
ATOM   8636  C  CE  . LYS B  1 485 ? 41.599  44.734  4.952   1.00 13.82 ? 485  LYS B CE  1 
ATOM   8637  N  NZ  . LYS B  1 485 ? 41.506  43.346  5.502   1.00 14.15 ? 485  LYS B NZ  1 
ATOM   8638  N  N   . THR B  1 486 ? 40.727  48.657  10.497  1.00 4.39  ? 486  THR B N   1 
ATOM   8639  C  CA  . THR B  1 486 ? 40.753  49.955  11.173  1.00 2.79  ? 486  THR B CA  1 
ATOM   8640  C  C   . THR B  1 486 ? 40.745  49.843  12.690  1.00 2.89  ? 486  THR B C   1 
ATOM   8641  O  O   . THR B  1 486 ? 40.042  49.013  13.265  1.00 4.00  ? 486  THR B O   1 
ATOM   8642  C  CB  . THR B  1 486 ? 39.568  50.844  10.799  1.00 3.02  ? 486  THR B CB  1 
ATOM   8643  O  OG1 . THR B  1 486 ? 39.722  52.109  11.455  1.00 4.28  ? 486  THR B OG1 1 
ATOM   8644  C  CG2 . THR B  1 486 ? 38.253  50.218  11.250  1.00 2.00  ? 486  THR B CG2 1 
ATOM   8645  N  N   . PRO B  1 487 ? 41.528  50.692  13.362  1.00 2.55  ? 487  PRO B N   1 
ATOM   8646  C  CA  . PRO B  1 487 ? 41.601  50.682  14.825  1.00 4.75  ? 487  PRO B CA  1 
ATOM   8647  C  C   . PRO B  1 487 ? 40.223  50.682  15.500  1.00 3.32  ? 487  PRO B C   1 
ATOM   8648  O  O   . PRO B  1 487 ? 40.059  50.123  16.590  1.00 2.05  ? 487  PRO B O   1 
ATOM   8649  C  CB  . PRO B  1 487 ? 42.391  51.950  15.132  1.00 3.73  ? 487  PRO B CB  1 
ATOM   8650  C  CG  . PRO B  1 487 ? 43.341  52.022  13.978  1.00 3.69  ? 487  PRO B CG  1 
ATOM   8651  C  CD  . PRO B  1 487 ? 42.453  51.688  12.794  1.00 3.39  ? 487  PRO B CD  1 
ATOM   8652  N  N   . ASP B  1 488 ? 39.235  51.304  14.853  1.00 3.52  ? 488  ASP B N   1 
ATOM   8653  C  CA  . ASP B  1 488 ? 37.885  51.372  15.421  1.00 4.05  ? 488  ASP B CA  1 
ATOM   8654  C  C   . ASP B  1 488 ? 37.156  50.025  15.519  1.00 3.80  ? 488  ASP B C   1 
ATOM   8655  O  O   . ASP B  1 488 ? 36.126  49.944  16.178  1.00 4.74  ? 488  ASP B O   1 
ATOM   8656  C  CB  . ASP B  1 488 ? 36.976  52.333  14.624  1.00 2.00  ? 488  ASP B CB  1 
ATOM   8657  C  CG  . ASP B  1 488 ? 37.459  53.784  14.638  1.00 2.00  ? 488  ASP B CG  1 
ATOM   8658  O  OD1 . ASP B  1 488 ? 37.882  54.294  15.696  1.00 2.00  ? 488  ASP B OD1 1 
ATOM   8659  O  OD2 . ASP B  1 488 ? 37.382  54.434  13.574  1.00 4.10  ? 488  ASP B OD2 1 
ATOM   8660  N  N   . ASN B  1 489 ? 37.669  48.973  14.884  1.00 2.90  ? 489  ASN B N   1 
ATOM   8661  C  CA  . ASN B  1 489 ? 36.970  47.686  14.918  1.00 2.31  ? 489  ASN B CA  1 
ATOM   8662  C  C   . ASN B  1 489 ? 37.543  46.549  15.750  1.00 5.77  ? 489  ASN B C   1 
ATOM   8663  O  O   . ASN B  1 489 ? 36.856  45.549  15.993  1.00 5.41  ? 489  ASN B O   1 
ATOM   8664  C  CB  . ASN B  1 489 ? 36.757  47.195  13.497  1.00 2.00  ? 489  ASN B CB  1 
ATOM   8665  C  CG  . ASN B  1 489 ? 35.557  47.817  12.869  1.00 2.00  ? 489  ASN B CG  1 
ATOM   8666  O  OD1 . ASN B  1 489 ? 35.149  48.905  13.260  1.00 2.00  ? 489  ASN B OD1 1 
ATOM   8667  N  ND2 . ASN B  1 489 ? 34.976  47.140  11.888  1.00 2.00  ? 489  ASN B ND2 1 
ATOM   8668  N  N   . ILE B  1 490 ? 38.794  46.701  16.175  1.00 5.03  ? 490  ILE B N   1 
ATOM   8669  C  CA  . ILE B  1 490 ? 39.483  45.699  16.980  1.00 2.00  ? 490  ILE B CA  1 
ATOM   8670  C  C   . ILE B  1 490 ? 38.703  45.321  18.231  1.00 2.00  ? 490  ILE B C   1 
ATOM   8671  O  O   . ILE B  1 490 ? 38.279  46.195  18.982  1.00 2.00  ? 490  ILE B O   1 
ATOM   8672  C  CB  . ILE B  1 490 ? 40.846  46.229  17.452  1.00 2.00  ? 490  ILE B CB  1 
ATOM   8673  C  CG1 . ILE B  1 490 ? 41.729  46.556  16.250  1.00 2.20  ? 490  ILE B CG1 1 
ATOM   8674  C  CG2 . ILE B  1 490 ? 41.499  45.224  18.373  1.00 2.00  ? 490  ILE B CG2 1 
ATOM   8675  C  CD1 . ILE B  1 490 ? 43.139  46.988  16.639  1.00 2.00  ? 490  ILE B CD1 1 
ATOM   8676  N  N   . ASP B  1 491 ? 38.530  44.023  18.462  1.00 2.00  ? 491  ASP B N   1 
ATOM   8677  C  CA  . ASP B  1 491 ? 37.836  43.539  19.659  1.00 2.79  ? 491  ASP B CA  1 
ATOM   8678  C  C   . ASP B  1 491 ? 38.578  43.945  20.940  1.00 3.20  ? 491  ASP B C   1 
ATOM   8679  O  O   . ASP B  1 491 ? 39.803  43.796  21.056  1.00 3.67  ? 491  ASP B O   1 
ATOM   8680  C  CB  . ASP B  1 491 ? 37.704  42.019  19.622  1.00 2.11  ? 491  ASP B CB  1 
ATOM   8681  C  CG  . ASP B  1 491 ? 36.795  41.550  18.522  1.00 2.57  ? 491  ASP B CG  1 
ATOM   8682  O  OD1 . ASP B  1 491 ? 35.605  41.923  18.541  1.00 3.02  ? 491  ASP B OD1 1 
ATOM   8683  O  OD2 . ASP B  1 491 ? 37.264  40.809  17.637  1.00 4.40  ? 491  ASP B OD2 1 
ATOM   8684  N  N   . ILE B  1 492 ? 37.826  44.432  21.915  1.00 2.00  ? 492  ILE B N   1 
ATOM   8685  C  CA  . ILE B  1 492 ? 38.418  44.882  23.158  1.00 2.03  ? 492  ILE B CA  1 
ATOM   8686  C  C   . ILE B  1 492 ? 39.374  43.883  23.821  1.00 3.39  ? 492  ILE B C   1 
ATOM   8687  O  O   . ILE B  1 492 ? 40.489  44.249  24.205  1.00 4.21  ? 492  ILE B O   1 
ATOM   8688  C  CB  . ILE B  1 492 ? 37.305  45.311  24.141  1.00 2.00  ? 492  ILE B CB  1 
ATOM   8689  C  CG1 . ILE B  1 492 ? 37.916  45.799  25.459  1.00 2.11  ? 492  ILE B CG1 1 
ATOM   8690  C  CG2 . ILE B  1 492 ? 36.322  44.182  24.314  1.00 2.00  ? 492  ILE B CG2 1 
ATOM   8691  C  CD1 . ILE B  1 492 ? 38.824  47.019  25.315  1.00 2.00  ? 492  ILE B CD1 1 
ATOM   8692  N  N   . TRP B  1 493 ? 38.965  42.627  23.952  1.00 2.00  ? 493  TRP B N   1 
ATOM   8693  C  CA  . TRP B  1 493 ? 39.834  41.646  24.588  1.00 2.00  ? 493  TRP B CA  1 
ATOM   8694  C  C   . TRP B  1 493 ? 41.222  41.630  23.980  1.00 2.00  ? 493  TRP B C   1 
ATOM   8695  O  O   . TRP B  1 493 ? 42.223  41.760  24.671  1.00 4.12  ? 493  TRP B O   1 
ATOM   8696  C  CB  . TRP B  1 493 ? 39.250  40.253  24.467  1.00 2.00  ? 493  TRP B CB  1 
ATOM   8697  C  CG  . TRP B  1 493 ? 40.071  39.249  25.149  1.00 2.00  ? 493  TRP B CG  1 
ATOM   8698  C  CD1 . TRP B  1 493 ? 40.205  39.085  26.486  1.00 2.00  ? 493  TRP B CD1 1 
ATOM   8699  C  CD2 . TRP B  1 493 ? 40.871  38.240  24.533  1.00 2.21  ? 493  TRP B CD2 1 
ATOM   8700  N  NE1 . TRP B  1 493 ? 41.036  38.031  26.750  1.00 2.00  ? 493  TRP B NE1 1 
ATOM   8701  C  CE2 . TRP B  1 493 ? 41.461  37.492  25.565  1.00 2.00  ? 493  TRP B CE2 1 
ATOM   8702  C  CE3 . TRP B  1 493 ? 41.145  37.890  23.203  1.00 3.58  ? 493  TRP B CE3 1 
ATOM   8703  C  CZ2 . TRP B  1 493 ? 42.312  36.410  25.316  1.00 2.00  ? 493  TRP B CZ2 1 
ATOM   8704  C  CZ3 . TRP B  1 493 ? 41.994  36.809  22.954  1.00 2.00  ? 493  TRP B CZ3 1 
ATOM   8705  C  CH2 . TRP B  1 493 ? 42.564  36.085  24.007  1.00 2.00  ? 493  TRP B CH2 1 
ATOM   8706  N  N   . ILE B  1 494 ? 41.274  41.474  22.670  1.00 2.00  ? 494  ILE B N   1 
ATOM   8707  C  CA  . ILE B  1 494 ? 42.540  41.421  21.982  1.00 2.00  ? 494  ILE B CA  1 
ATOM   8708  C  C   . ILE B  1 494 ? 43.201  42.799  21.933  1.00 2.34  ? 494  ILE B C   1 
ATOM   8709  O  O   . ILE B  1 494 ? 44.367  42.941  22.304  1.00 2.00  ? 494  ILE B O   1 
ATOM   8710  C  CB  . ILE B  1 494 ? 42.331  40.854  20.566  1.00 2.04  ? 494  ILE B CB  1 
ATOM   8711  C  CG1 . ILE B  1 494 ? 43.561  40.053  20.145  1.00 2.02  ? 494  ILE B CG1 1 
ATOM   8712  C  CG2 . ILE B  1 494 ? 42.020  41.976  19.577  1.00 2.00  ? 494  ILE B CG2 1 
ATOM   8713  C  CD1 . ILE B  1 494 ? 44.762  40.897  19.856  1.00 3.12  ? 494  ILE B CD1 1 
ATOM   8714  N  N   . GLY B  1 495 ? 42.443  43.809  21.505  1.00 2.40  ? 495  GLY B N   1 
ATOM   8715  C  CA  . GLY B  1 495 ? 42.971  45.159  21.400  1.00 2.00  ? 495  GLY B CA  1 
ATOM   8716  C  C   . GLY B  1 495 ? 43.559  45.676  22.692  1.00 2.00  ? 495  GLY B C   1 
ATOM   8717  O  O   . GLY B  1 495 ? 44.563  46.389  22.687  1.00 2.00  ? 495  GLY B O   1 
ATOM   8718  N  N   . GLY B  1 496 ? 42.930  45.308  23.804  1.00 2.35  ? 496  GLY B N   1 
ATOM   8719  C  CA  . GLY B  1 496 ? 43.395  45.744  25.106  1.00 2.00  ? 496  GLY B CA  1 
ATOM   8720  C  C   . GLY B  1 496 ? 44.694  45.082  25.517  1.00 2.00  ? 496  GLY B C   1 
ATOM   8721  O  O   . GLY B  1 496 ? 45.621  45.758  25.976  1.00 2.19  ? 496  GLY B O   1 
ATOM   8722  N  N   . ASN B  1 497 ? 44.759  43.762  25.349  1.00 2.00  ? 497  ASN B N   1 
ATOM   8723  C  CA  . ASN B  1 497 ? 45.943  42.984  25.706  1.00 2.00  ? 497  ASN B CA  1 
ATOM   8724  C  C   . ASN B  1 497 ? 47.135  43.261  24.814  1.00 2.00  ? 497  ASN B C   1 
ATOM   8725  O  O   . ASN B  1 497 ? 48.286  43.068  25.203  1.00 2.00  ? 497  ASN B O   1 
ATOM   8726  C  CB  . ASN B  1 497 ? 45.659  41.506  25.638  1.00 2.34  ? 497  ASN B CB  1 
ATOM   8727  C  CG  . ASN B  1 497 ? 44.794  41.043  26.775  1.00 2.68  ? 497  ASN B CG  1 
ATOM   8728  O  OD1 . ASN B  1 497 ? 45.262  40.319  27.642  1.00 7.08  ? 497  ASN B OD1 1 
ATOM   8729  N  ND2 . ASN B  1 497 ? 43.532  41.442  26.779  1.00 4.27  ? 497  ASN B ND2 1 
ATOM   8730  N  N   . ALA B  1 498 ? 46.854  43.704  23.603  1.00 2.25  ? 498  ALA B N   1 
ATOM   8731  C  CA  . ALA B  1 498 ? 47.911  44.001  22.661  1.00 2.02  ? 498  ALA B CA  1 
ATOM   8732  C  C   . ALA B  1 498 ? 48.857  45.069  23.196  1.00 2.00  ? 498  ALA B C   1 
ATOM   8733  O  O   . ALA B  1 498 ? 50.042  45.062  22.878  1.00 2.00  ? 498  ALA B O   1 
ATOM   8734  C  CB  . ALA B  1 498 ? 47.306  44.445  21.320  1.00 2.56  ? 498  ALA B CB  1 
ATOM   8735  N  N   . GLU B  1 499 ? 48.346  45.979  24.017  1.00 2.00  ? 499  GLU B N   1 
ATOM   8736  C  CA  . GLU B  1 499 ? 49.184  47.054  24.545  1.00 2.75  ? 499  GLU B CA  1 
ATOM   8737  C  C   . GLU B  1 499 ? 50.298  46.567  25.471  1.00 2.27  ? 499  GLU B C   1 
ATOM   8738  O  O   . GLU B  1 499 ? 50.129  45.587  26.198  1.00 2.00  ? 499  GLU B O   1 
ATOM   8739  C  CB  . GLU B  1 499 ? 48.329  48.079  25.297  1.00 2.27  ? 499  GLU B CB  1 
ATOM   8740  C  CG  . GLU B  1 499 ? 46.982  48.366  24.651  1.00 2.51  ? 499  GLU B CG  1 
ATOM   8741  C  CD  . GLU B  1 499 ? 46.283  49.573  25.262  1.00 3.43  ? 499  GLU B CD  1 
ATOM   8742  O  OE1 . GLU B  1 499 ? 46.324  49.725  26.507  1.00 4.31  ? 499  GLU B OE1 1 
ATOM   8743  O  OE2 . GLU B  1 499 ? 45.683  50.363  24.498  1.00 2.21  ? 499  GLU B OE2 1 
ATOM   8744  N  N   . PRO B  1 500 ? 51.466  47.235  25.435  1.00 2.00  ? 500  PRO B N   1 
ATOM   8745  C  CA  . PRO B  1 500 ? 52.571  46.832  26.305  1.00 2.16  ? 500  PRO B CA  1 
ATOM   8746  C  C   . PRO B  1 500 ? 52.173  47.168  27.743  1.00 3.54  ? 500  PRO B C   1 
ATOM   8747  O  O   . PRO B  1 500 ? 51.342  48.052  27.975  1.00 3.20  ? 500  PRO B O   1 
ATOM   8748  C  CB  . PRO B  1 500 ? 53.732  47.674  25.797  1.00 2.00  ? 500  PRO B CB  1 
ATOM   8749  C  CG  . PRO B  1 500 ? 53.053  48.915  25.332  1.00 2.00  ? 500  PRO B CG  1 
ATOM   8750  C  CD  . PRO B  1 500 ? 51.863  48.370  24.587  1.00 2.00  ? 500  PRO B CD  1 
ATOM   8751  N  N   . MET B  1 501 ? 52.766  46.468  28.702  1.00 2.45  ? 501  MET B N   1 
ATOM   8752  C  CA  . MET B  1 501 ? 52.434  46.664  30.105  1.00 2.00  ? 501  MET B CA  1 
ATOM   8753  C  C   . MET B  1 501 ? 53.028  47.898  30.757  1.00 2.00  ? 501  MET B C   1 
ATOM   8754  O  O   . MET B  1 501 ? 54.194  48.235  30.545  1.00 2.13  ? 501  MET B O   1 
ATOM   8755  C  CB  . MET B  1 501 ? 52.866  45.442  30.900  1.00 2.81  ? 501  MET B CB  1 
ATOM   8756  C  CG  . MET B  1 501 ? 52.312  44.134  30.388  1.00 2.00  ? 501  MET B CG  1 
ATOM   8757  S  SD  . MET B  1 501 ? 53.333  42.828  31.064  1.00 6.82  ? 501  MET B SD  1 
ATOM   8758  C  CE  . MET B  1 501 ? 52.552  41.320  30.462  1.00 2.11  ? 501  MET B CE  1 
ATOM   8759  N  N   . VAL B  1 502 ? 52.220  48.555  31.578  1.00 2.00  ? 502  VAL B N   1 
ATOM   8760  C  CA  . VAL B  1 502 ? 52.656  49.741  32.301  1.00 3.20  ? 502  VAL B CA  1 
ATOM   8761  C  C   . VAL B  1 502 ? 53.789  49.370  33.236  1.00 4.38  ? 502  VAL B C   1 
ATOM   8762  O  O   . VAL B  1 502 ? 54.001  48.196  33.532  1.00 5.00  ? 502  VAL B O   1 
ATOM   8763  C  CB  . VAL B  1 502 ? 51.562  50.274  33.174  1.00 2.00  ? 502  VAL B CB  1 
ATOM   8764  C  CG1 . VAL B  1 502 ? 50.306  50.471  32.360  1.00 3.23  ? 502  VAL B CG1 1 
ATOM   8765  C  CG2 . VAL B  1 502 ? 51.332  49.303  34.316  1.00 2.22  ? 502  VAL B CG2 1 
ATOM   8766  N  N   . GLU B  1 503 ? 54.479  50.388  33.737  1.00 7.22  ? 503  GLU B N   1 
ATOM   8767  C  CA  . GLU B  1 503 ? 55.608  50.209  34.646  1.00 8.41  ? 503  GLU B CA  1 
ATOM   8768  C  C   . GLU B  1 503 ? 55.273  49.456  35.941  1.00 7.50  ? 503  GLU B C   1 
ATOM   8769  O  O   . GLU B  1 503 ? 54.409  49.870  36.713  1.00 7.11  ? 503  GLU B O   1 
ATOM   8770  C  CB  . GLU B  1 503 ? 56.214  51.575  34.975  1.00 10.76 ? 503  GLU B CB  1 
ATOM   8771  C  CG  . GLU B  1 503 ? 57.330  51.519  35.983  1.00 16.89 ? 503  GLU B CG  1 
ATOM   8772  C  CD  . GLU B  1 503 ? 58.012  52.861  36.171  1.00 20.12 ? 503  GLU B CD  1 
ATOM   8773  O  OE1 . GLU B  1 503 ? 58.701  53.302  35.223  1.00 21.68 ? 503  GLU B OE1 1 
ATOM   8774  O  OE2 . GLU B  1 503 ? 57.858  53.471  37.261  1.00 21.29 ? 503  GLU B OE2 1 
ATOM   8775  N  N   . ARG B  1 504 ? 55.981  48.349  36.156  1.00 7.40  ? 504  ARG B N   1 
ATOM   8776  C  CA  . ARG B  1 504 ? 55.820  47.480  37.323  1.00 6.96  ? 504  ARG B CA  1 
ATOM   8777  C  C   . ARG B  1 504 ? 54.442  46.837  37.483  1.00 5.38  ? 504  ARG B C   1 
ATOM   8778  O  O   . ARG B  1 504 ? 54.047  46.494  38.596  1.00 4.20  ? 504  ARG B O   1 
ATOM   8779  C  CB  . ARG B  1 504 ? 56.193  48.230  38.603  1.00 9.63  ? 504  ARG B CB  1 
ATOM   8780  C  CG  . ARG B  1 504 ? 57.561  48.899  38.537  1.00 16.70 ? 504  ARG B CG  1 
ATOM   8781  C  CD  . ARG B  1 504 ? 58.138  49.178  39.928  1.00 21.47 ? 504  ARG B CD  1 
ATOM   8782  N  NE  . ARG B  1 504 ? 58.885  48.039  40.463  1.00 26.39 ? 504  ARG B NE  1 
ATOM   8783  C  CZ  . ARG B  1 504 ? 60.011  47.567  39.930  1.00 28.28 ? 504  ARG B CZ  1 
ATOM   8784  N  NH1 . ARG B  1 504 ? 60.527  48.131  38.841  1.00 30.14 ? 504  ARG B NH1 1 
ATOM   8785  N  NH2 . ARG B  1 504 ? 60.627  46.534  40.490  1.00 30.13 ? 504  ARG B NH2 1 
ATOM   8786  N  N   . GLY B  1 505 ? 53.726  46.662  36.371  1.00 4.44  ? 505  GLY B N   1 
ATOM   8787  C  CA  . GLY B  1 505 ? 52.403  46.044  36.397  1.00 3.78  ? 505  GLY B CA  1 
ATOM   8788  C  C   . GLY B  1 505 ? 52.304  44.838  35.463  1.00 3.99  ? 505  GLY B C   1 
ATOM   8789  O  O   . GLY B  1 505 ? 53.331  44.279  35.079  1.00 4.40  ? 505  GLY B O   1 
ATOM   8790  N  N   . ARG B  1 506 ? 51.094  44.419  35.093  1.00 2.17  ? 506  ARG B N   1 
ATOM   8791  C  CA  . ARG B  1 506 ? 50.958  43.271  34.196  1.00 2.00  ? 506  ARG B CA  1 
ATOM   8792  C  C   . ARG B  1 506 ? 49.883  43.461  33.148  1.00 2.13  ? 506  ARG B C   1 
ATOM   8793  O  O   . ARG B  1 506 ? 49.450  42.506  32.495  1.00 2.00  ? 506  ARG B O   1 
ATOM   8794  C  CB  . ARG B  1 506 ? 50.687  41.989  34.976  1.00 2.00  ? 506  ARG B CB  1 
ATOM   8795  C  CG  . ARG B  1 506 ? 51.801  41.576  35.908  1.00 2.92  ? 506  ARG B CG  1 
ATOM   8796  C  CD  . ARG B  1 506 ? 53.140  41.596  35.172  1.00 3.61  ? 506  ARG B CD  1 
ATOM   8797  N  NE  . ARG B  1 506 ? 54.233  41.193  36.028  1.00 5.80  ? 506  ARG B NE  1 
ATOM   8798  C  CZ  . ARG B  1 506 ? 55.519  41.350  35.727  1.00 8.09  ? 506  ARG B CZ  1 
ATOM   8799  N  NH1 . ARG B  1 506 ? 55.865  41.896  34.565  1.00 7.75  ? 506  ARG B NH1 1 
ATOM   8800  N  NH2 . ARG B  1 506 ? 56.460  40.966  36.587  1.00 8.36  ? 506  ARG B NH2 1 
ATOM   8801  N  N   . VAL B  1 507 ? 49.449  44.708  33.011  1.00 2.64  ? 507  VAL B N   1 
ATOM   8802  C  CA  . VAL B  1 507 ? 48.458  45.096  32.019  1.00 2.00  ? 507  VAL B CA  1 
ATOM   8803  C  C   . VAL B  1 507 ? 48.808  46.526  31.634  1.00 3.27  ? 507  VAL B C   1 
ATOM   8804  O  O   . VAL B  1 507 ? 49.422  47.252  32.421  1.00 3.04  ? 507  VAL B O   1 
ATOM   8805  C  CB  . VAL B  1 507 ? 47.032  45.072  32.578  1.00 2.00  ? 507  VAL B CB  1 
ATOM   8806  C  CG1 . VAL B  1 507 ? 46.743  43.726  33.208  1.00 2.05  ? 507  VAL B CG1 1 
ATOM   8807  C  CG2 . VAL B  1 507 ? 46.854  46.191  33.573  1.00 2.03  ? 507  VAL B CG2 1 
ATOM   8808  N  N   . GLY B  1 508 ? 48.411  46.930  30.431  1.00 2.98  ? 508  GLY B N   1 
ATOM   8809  C  CA  . GLY B  1 508 ? 48.718  48.268  29.957  1.00 2.85  ? 508  GLY B CA  1 
ATOM   8810  C  C   . GLY B  1 508 ? 47.772  49.384  30.366  1.00 2.00  ? 508  GLY B C   1 
ATOM   8811  O  O   . GLY B  1 508 ? 46.951  49.217  31.265  1.00 2.00  ? 508  GLY B O   1 
ATOM   8812  N  N   . PRO B  1 509 ? 47.887  50.552  29.715  1.00 2.00  ? 509  PRO B N   1 
ATOM   8813  C  CA  . PRO B  1 509 ? 47.084  51.752  29.946  1.00 2.00  ? 509  PRO B CA  1 
ATOM   8814  C  C   . PRO B  1 509 ? 45.583  51.529  29.995  1.00 2.96  ? 509  PRO B C   1 
ATOM   8815  O  O   . PRO B  1 509 ? 44.920  51.944  30.945  1.00 2.77  ? 509  PRO B O   1 
ATOM   8816  C  CB  . PRO B  1 509 ? 47.466  52.646  28.776  1.00 2.00  ? 509  PRO B CB  1 
ATOM   8817  C  CG  . PRO B  1 509 ? 48.879  52.332  28.575  1.00 2.34  ? 509  PRO B CG  1 
ATOM   8818  C  CD  . PRO B  1 509 ? 48.917  50.822  28.696  1.00 2.79  ? 509  PRO B CD  1 
ATOM   8819  N  N   . LEU B  1 510 ? 45.035  50.888  28.971  1.00 2.01  ? 510  LEU B N   1 
ATOM   8820  C  CA  . LEU B  1 510 ? 43.603  50.692  28.955  1.00 2.00  ? 510  LEU B CA  1 
ATOM   8821  C  C   . LEU B  1 510 ? 43.100  49.666  29.948  1.00 2.20  ? 510  LEU B C   1 
ATOM   8822  O  O   . LEU B  1 510 ? 42.056  49.876  30.559  1.00 3.15  ? 510  LEU B O   1 
ATOM   8823  C  CB  . LEU B  1 510 ? 43.106  50.336  27.560  1.00 2.00  ? 510  LEU B CB  1 
ATOM   8824  C  CG  . LEU B  1 510 ? 41.577  50.245  27.553  1.00 2.00  ? 510  LEU B CG  1 
ATOM   8825  C  CD1 . LEU B  1 510 ? 40.989  51.544  28.074  1.00 2.00  ? 510  LEU B CD1 1 
ATOM   8826  C  CD2 . LEU B  1 510 ? 41.078  49.943  26.158  1.00 2.00  ? 510  LEU B CD2 1 
ATOM   8827  N  N   . LEU B  1 511 ? 43.805  48.554  30.118  1.00 2.00  ? 511  LEU B N   1 
ATOM   8828  C  CA  . LEU B  1 511 ? 43.321  47.584  31.088  1.00 2.00  ? 511  LEU B CA  1 
ATOM   8829  C  C   . LEU B  1 511 ? 43.437  48.131  32.501  1.00 2.00  ? 511  LEU B C   1 
ATOM   8830  O  O   . LEU B  1 511 ? 42.593  47.853  33.342  1.00 2.58  ? 511  LEU B O   1 
ATOM   8831  C  CB  . LEU B  1 511 ? 44.074  46.253  31.004  1.00 2.00  ? 511  LEU B CB  1 
ATOM   8832  C  CG  . LEU B  1 511 ? 43.406  45.132  30.212  1.00 2.00  ? 511  LEU B CG  1 
ATOM   8833  C  CD1 . LEU B  1 511 ? 41.899  45.319  30.181  1.00 2.00  ? 511  LEU B CD1 1 
ATOM   8834  C  CD2 . LEU B  1 511 ? 43.952  45.142  28.819  1.00 2.00  ? 511  LEU B CD2 1 
ATOM   8835  N  N   . ALA B  1 512 ? 44.476  48.910  32.767  1.00 2.00  ? 512  ALA B N   1 
ATOM   8836  C  CA  . ALA B  1 512 ? 44.661  49.463  34.100  1.00 2.00  ? 512  ALA B CA  1 
ATOM   8837  C  C   . ALA B  1 512 ? 43.487  50.365  34.462  1.00 3.84  ? 512  ALA B C   1 
ATOM   8838  O  O   . ALA B  1 512 ? 43.043  50.404  35.614  1.00 4.01  ? 512  ALA B O   1 
ATOM   8839  C  CB  . ALA B  1 512 ? 45.964  50.246  34.165  1.00 2.00  ? 512  ALA B CB  1 
ATOM   8840  N  N   . CYS B  1 513 ? 42.989  51.086  33.463  1.00 2.00  ? 513  CYS B N   1 
ATOM   8841  C  CA  . CYS B  1 513 ? 41.881  52.006  33.641  1.00 2.00  ? 513  CYS B CA  1 
ATOM   8842  C  C   . CYS B  1 513 ? 40.598  51.260  33.941  1.00 2.00  ? 513  CYS B C   1 
ATOM   8843  O  O   . CYS B  1 513 ? 39.949  51.511  34.949  1.00 2.00  ? 513  CYS B O   1 
ATOM   8844  C  CB  . CYS B  1 513 ? 41.732  52.855  32.384  1.00 2.00  ? 513  CYS B CB  1 
ATOM   8845  S  SG  . CYS B  1 513 ? 40.163  53.759  32.222  1.00 3.56  ? 513  CYS B SG  1 
ATOM   8846  N  N   . LEU B  1 514 ? 40.242  50.327  33.072  1.00 2.00  ? 514  LEU B N   1 
ATOM   8847  C  CA  . LEU B  1 514 ? 39.027  49.540  33.256  1.00 2.71  ? 514  LEU B CA  1 
ATOM   8848  C  C   . LEU B  1 514 ? 38.982  48.698  34.531  1.00 2.45  ? 514  LEU B C   1 
ATOM   8849  O  O   . LEU B  1 514 ? 37.904  48.466  35.065  1.00 3.38  ? 514  LEU B O   1 
ATOM   8850  C  CB  . LEU B  1 514 ? 38.798  48.633  32.048  1.00 2.00  ? 514  LEU B CB  1 
ATOM   8851  C  CG  . LEU B  1 514 ? 38.423  49.341  30.754  1.00 2.00  ? 514  LEU B CG  1 
ATOM   8852  C  CD1 . LEU B  1 514 ? 38.509  48.369  29.619  1.00 2.00  ? 514  LEU B CD1 1 
ATOM   8853  C  CD2 . LEU B  1 514 ? 37.021  49.909  30.869  1.00 2.20  ? 514  LEU B CD2 1 
ATOM   8854  N  N   . LEU B  1 515 ? 40.129  48.223  35.011  1.00 2.00  ? 515  LEU B N   1 
ATOM   8855  C  CA  . LEU B  1 515 ? 40.150  47.429  36.234  1.00 2.00  ? 515  LEU B CA  1 
ATOM   8856  C  C   . LEU B  1 515 ? 40.152  48.377  37.417  1.00 2.20  ? 515  LEU B C   1 
ATOM   8857  O  O   . LEU B  1 515 ? 39.342  48.248  38.340  1.00 2.29  ? 515  LEU B O   1 
ATOM   8858  C  CB  . LEU B  1 515 ? 41.397  46.542  36.305  1.00 2.00  ? 515  LEU B CB  1 
ATOM   8859  C  CG  . LEU B  1 515 ? 41.584  45.499  35.204  1.00 2.00  ? 515  LEU B CG  1 
ATOM   8860  C  CD1 . LEU B  1 515 ? 42.710  44.544  35.555  1.00 2.00  ? 515  LEU B CD1 1 
ATOM   8861  C  CD2 . LEU B  1 515 ? 40.299  44.735  35.035  1.00 2.64  ? 515  LEU B CD2 1 
ATOM   8862  N  N   . GLY B  1 516 ? 41.072  49.335  37.376  1.00 2.16  ? 516  GLY B N   1 
ATOM   8863  C  CA  . GLY B  1 516 ? 41.184  50.305  38.448  1.00 2.67  ? 516  GLY B CA  1 
ATOM   8864  C  C   . GLY B  1 516 ? 39.831  50.819  38.887  1.00 2.18  ? 516  GLY B C   1 
ATOM   8865  O  O   . GLY B  1 516 ? 39.452  50.694  40.054  1.00 2.00  ? 516  GLY B O   1 
ATOM   8866  N  N   . ARG B  1 517 ? 39.099  51.388  37.938  1.00 2.65  ? 517  ARG B N   1 
ATOM   8867  C  CA  . ARG B  1 517 ? 37.781  51.920  38.218  1.00 4.07  ? 517  ARG B CA  1 
ATOM   8868  C  C   . ARG B  1 517 ? 36.867  50.882  38.851  1.00 5.33  ? 517  ARG B C   1 
ATOM   8869  O  O   . ARG B  1 517 ? 36.350  51.084  39.959  1.00 5.98  ? 517  ARG B O   1 
ATOM   8870  C  CB  . ARG B  1 517 ? 37.139  52.441  36.935  1.00 5.00  ? 517  ARG B CB  1 
ATOM   8871  C  CG  . ARG B  1 517 ? 37.878  53.602  36.326  1.00 7.46  ? 517  ARG B CG  1 
ATOM   8872  C  CD  . ARG B  1 517 ? 36.948  54.452  35.491  1.00 9.23  ? 517  ARG B CD  1 
ATOM   8873  N  NE  . ARG B  1 517 ? 37.666  55.537  34.834  1.00 12.36 ? 517  ARG B NE  1 
ATOM   8874  C  CZ  . ARG B  1 517 ? 37.077  56.529  34.181  1.00 13.59 ? 517  ARG B CZ  1 
ATOM   8875  N  NH1 . ARG B  1 517 ? 35.752  56.571  34.105  1.00 14.71 ? 517  ARG B NH1 1 
ATOM   8876  N  NH2 . ARG B  1 517 ? 37.813  57.471  33.596  1.00 14.99 ? 517  ARG B NH2 1 
ATOM   8877  N  N   . GLN B  1 518 ? 36.666  49.774  38.145  1.00 3.24  ? 518  GLN B N   1 
ATOM   8878  C  CA  . GLN B  1 518 ? 35.797  48.726  38.642  1.00 2.00  ? 518  GLN B CA  1 
ATOM   8879  C  C   . GLN B  1 518 ? 36.087  48.422  40.097  1.00 2.94  ? 518  GLN B C   1 
ATOM   8880  O  O   . GLN B  1 518 ? 35.207  48.537  40.952  1.00 2.37  ? 518  GLN B O   1 
ATOM   8881  C  CB  . GLN B  1 518 ? 35.963  47.453  37.830  1.00 2.00  ? 518  GLN B CB  1 
ATOM   8882  C  CG  . GLN B  1 518 ? 35.005  46.378  38.259  1.00 2.00  ? 518  GLN B CG  1 
ATOM   8883  C  CD  . GLN B  1 518 ? 33.568  46.765  38.003  1.00 2.24  ? 518  GLN B CD  1 
ATOM   8884  O  OE1 . GLN B  1 518 ? 33.134  46.851  36.855  1.00 4.08  ? 518  GLN B OE1 1 
ATOM   8885  N  NE2 . GLN B  1 518 ? 32.821  47.009  39.071  1.00 2.00  ? 518  GLN B NE2 1 
ATOM   8886  N  N   . PHE B  1 519 ? 37.331  48.050  40.383  1.00 3.22  ? 519  PHE B N   1 
ATOM   8887  C  CA  . PHE B  1 519 ? 37.701  47.712  41.749  1.00 4.59  ? 519  PHE B CA  1 
ATOM   8888  C  C   . PHE B  1 519 ? 37.437  48.793  42.781  1.00 5.76  ? 519  PHE B C   1 
ATOM   8889  O  O   . PHE B  1 519 ? 36.893  48.502  43.848  1.00 6.18  ? 519  PHE B O   1 
ATOM   8890  C  CB  . PHE B  1 519 ? 39.151  47.238  41.805  1.00 2.45  ? 519  PHE B CB  1 
ATOM   8891  C  CG  . PHE B  1 519 ? 39.291  45.774  41.523  1.00 2.19  ? 519  PHE B CG  1 
ATOM   8892  C  CD1 . PHE B  1 519 ? 38.713  44.844  42.377  1.00 2.00  ? 519  PHE B CD1 1 
ATOM   8893  C  CD2 . PHE B  1 519 ? 39.921  45.324  40.368  1.00 2.66  ? 519  PHE B CD2 1 
ATOM   8894  C  CE1 . PHE B  1 519 ? 38.750  43.490  42.086  1.00 2.00  ? 519  PHE B CE1 1 
ATOM   8895  C  CE2 . PHE B  1 519 ? 39.964  43.963  40.066  1.00 2.81  ? 519  PHE B CE2 1 
ATOM   8896  C  CZ  . PHE B  1 519 ? 39.374  43.045  40.930  1.00 2.14  ? 519  PHE B CZ  1 
ATOM   8897  N  N   . GLN B  1 520 ? 37.810  50.032  42.478  1.00 6.62  ? 520  GLN B N   1 
ATOM   8898  C  CA  . GLN B  1 520 ? 37.555  51.135  43.405  1.00 7.01  ? 520  GLN B CA  1 
ATOM   8899  C  C   . GLN B  1 520 ? 36.070  51.132  43.793  1.00 6.99  ? 520  GLN B C   1 
ATOM   8900  O  O   . GLN B  1 520 ? 35.703  51.173  44.973  1.00 4.47  ? 520  GLN B O   1 
ATOM   8901  C  CB  . GLN B  1 520 ? 37.896  52.468  42.732  1.00 9.32  ? 520  GLN B CB  1 
ATOM   8902  C  CG  . GLN B  1 520 ? 37.040  53.646  43.191  1.00 13.37 ? 520  GLN B CG  1 
ATOM   8903  C  CD  . GLN B  1 520 ? 36.848  54.687  42.099  1.00 15.45 ? 520  GLN B CD  1 
ATOM   8904  O  OE1 . GLN B  1 520 ? 35.718  55.036  41.751  1.00 17.36 ? 520  GLN B OE1 1 
ATOM   8905  N  NE2 . GLN B  1 520 ? 37.953  55.187  41.552  1.00 17.37 ? 520  GLN B NE2 1 
ATOM   8906  N  N   . GLN B  1 521 ? 35.222  51.063  42.774  1.00 6.33  ? 521  GLN B N   1 
ATOM   8907  C  CA  . GLN B  1 521 ? 33.786  51.090  42.969  1.00 5.08  ? 521  GLN B CA  1 
ATOM   8908  C  C   . GLN B  1 521 ? 33.184  49.988  43.842  1.00 4.15  ? 521  GLN B C   1 
ATOM   8909  O  O   . GLN B  1 521 ? 32.266  50.254  44.615  1.00 5.17  ? 521  GLN B O   1 
ATOM   8910  C  CB  . GLN B  1 521 ? 33.112  51.162  41.597  1.00 4.09  ? 521  GLN B CB  1 
ATOM   8911  C  CG  . GLN B  1 521 ? 33.361  52.514  40.950  1.00 5.91  ? 521  GLN B CG  1 
ATOM   8912  C  CD  . GLN B  1 521 ? 32.842  52.629  39.533  1.00 8.19  ? 521  GLN B CD  1 
ATOM   8913  O  OE1 . GLN B  1 521 ? 31.738  52.173  39.222  1.00 10.84 ? 521  GLN B OE1 1 
ATOM   8914  N  NE2 . GLN B  1 521 ? 33.631  53.266  38.664  1.00 8.10  ? 521  GLN B NE2 1 
ATOM   8915  N  N   . ILE B  1 522 ? 33.679  48.759  43.746  1.00 3.45  ? 522  ILE B N   1 
ATOM   8916  C  CA  . ILE B  1 522 ? 33.117  47.701  44.584  1.00 2.79  ? 522  ILE B CA  1 
ATOM   8917  C  C   . ILE B  1 522 ? 33.710  47.802  45.989  1.00 3.31  ? 522  ILE B C   1 
ATOM   8918  O  O   . ILE B  1 522 ? 33.272  47.119  46.921  1.00 2.14  ? 522  ILE B O   1 
ATOM   8919  C  CB  . ILE B  1 522 ? 33.386  46.285  43.999  1.00 3.37  ? 522  ILE B CB  1 
ATOM   8920  C  CG1 . ILE B  1 522 ? 34.891  46.015  43.912  1.00 2.72  ? 522  ILE B CG1 1 
ATOM   8921  C  CG2 . ILE B  1 522 ? 32.726  46.161  42.625  1.00 2.00  ? 522  ILE B CG2 1 
ATOM   8922  C  CD1 . ILE B  1 522 ? 35.230  44.617  43.447  1.00 2.00  ? 522  ILE B CD1 1 
ATOM   8923  N  N   . ARG B  1 523 ? 34.705  48.676  46.126  1.00 2.69  ? 523  ARG B N   1 
ATOM   8924  C  CA  . ARG B  1 523 ? 35.368  48.904  47.398  1.00 2.71  ? 523  ARG B CA  1 
ATOM   8925  C  C   . ARG B  1 523 ? 34.789  50.147  48.085  1.00 5.96  ? 523  ARG B C   1 
ATOM   8926  O  O   . ARG B  1 523 ? 34.646  50.169  49.307  1.00 8.39  ? 523  ARG B O   1 
ATOM   8927  C  CB  . ARG B  1 523 ? 36.872  49.062  47.172  1.00 2.00  ? 523  ARG B CB  1 
ATOM   8928  C  CG  . ARG B  1 523 ? 37.662  49.491  48.401  1.00 3.60  ? 523  ARG B CG  1 
ATOM   8929  C  CD  . ARG B  1 523 ? 37.916  50.996  48.398  1.00 4.60  ? 523  ARG B CD  1 
ATOM   8930  N  NE  . ARG B  1 523 ? 39.334  51.304  48.558  1.00 5.08  ? 523  ARG B NE  1 
ATOM   8931  C  CZ  . ARG B  1 523 ? 39.892  52.469  48.244  1.00 5.51  ? 523  ARG B CZ  1 
ATOM   8932  N  NH1 . ARG B  1 523 ? 39.154  53.453  47.744  1.00 3.99  ? 523  ARG B NH1 1 
ATOM   8933  N  NH2 . ARG B  1 523 ? 41.193  52.643  48.428  1.00 5.69  ? 523  ARG B NH2 1 
ATOM   8934  N  N   . ASP B  1 524 ? 34.450  51.177  47.308  1.00 4.39  ? 524  ASP B N   1 
ATOM   8935  C  CA  . ASP B  1 524 ? 33.881  52.404  47.876  1.00 2.73  ? 524  ASP B CA  1 
ATOM   8936  C  C   . ASP B  1 524 ? 32.374  52.287  48.065  1.00 2.00  ? 524  ASP B C   1 
ATOM   8937  O  O   . ASP B  1 524 ? 31.791  52.982  48.891  1.00 2.32  ? 524  ASP B O   1 
ATOM   8938  C  CB  . ASP B  1 524 ? 34.173  53.608  46.971  1.00 2.45  ? 524  ASP B CB  1 
ATOM   8939  C  CG  . ASP B  1 524 ? 35.564  54.176  47.175  1.00 2.57  ? 524  ASP B CG  1 
ATOM   8940  O  OD1 . ASP B  1 524 ? 36.379  53.535  47.867  1.00 4.25  ? 524  ASP B OD1 1 
ATOM   8941  O  OD2 . ASP B  1 524 ? 35.850  55.265  46.641  1.00 2.78  ? 524  ASP B OD2 1 
ATOM   8942  N  N   . GLY B  1 525 ? 31.749  51.404  47.295  1.00 2.66  ? 525  GLY B N   1 
ATOM   8943  C  CA  . GLY B  1 525 ? 30.311  51.242  47.373  1.00 2.00  ? 525  GLY B CA  1 
ATOM   8944  C  C   . GLY B  1 525 ? 29.825  50.065  48.190  1.00 3.03  ? 525  GLY B C   1 
ATOM   8945  O  O   . GLY B  1 525 ? 28.613  49.813  48.234  1.00 2.77  ? 525  GLY B O   1 
ATOM   8946  N  N   . ASP B  1 526 ? 30.750  49.349  48.834  1.00 2.34  ? 526  ASP B N   1 
ATOM   8947  C  CA  . ASP B  1 526 ? 30.398  48.192  49.657  1.00 2.00  ? 526  ASP B CA  1 
ATOM   8948  C  C   . ASP B  1 526 ? 30.245  48.602  51.111  1.00 2.00  ? 526  ASP B C   1 
ATOM   8949  O  O   . ASP B  1 526 ? 31.215  48.976  51.755  1.00 2.00  ? 526  ASP B O   1 
ATOM   8950  C  CB  . ASP B  1 526 ? 31.461  47.102  49.545  1.00 2.00  ? 526  ASP B CB  1 
ATOM   8951  C  CG  . ASP B  1 526 ? 31.239  45.996  50.543  1.00 3.13  ? 526  ASP B CG  1 
ATOM   8952  O  OD1 . ASP B  1 526 ? 30.061  45.793  50.897  1.00 3.60  ? 526  ASP B OD1 1 
ATOM   8953  O  OD2 . ASP B  1 526 ? 32.216  45.336  50.970  1.00 2.45  ? 526  ASP B OD2 1 
ATOM   8954  N  N   . ARG B  1 527 ? 29.024  48.514  51.627  1.00 2.00  ? 527  ARG B N   1 
ATOM   8955  C  CA  . ARG B  1 527 ? 28.727  48.921  53.003  1.00 2.00  ? 527  ARG B CA  1 
ATOM   8956  C  C   . ARG B  1 527 ? 29.426  48.077  54.047  1.00 2.00  ? 527  ARG B C   1 
ATOM   8957  O  O   . ARG B  1 527 ? 29.533  48.482  55.209  1.00 2.00  ? 527  ARG B O   1 
ATOM   8958  C  CB  . ARG B  1 527 ? 27.212  48.880  53.249  1.00 3.21  ? 527  ARG B CB  1 
ATOM   8959  C  CG  . ARG B  1 527 ? 26.765  49.298  54.651  1.00 3.86  ? 527  ARG B CG  1 
ATOM   8960  C  CD  . ARG B  1 527 ? 25.260  49.621  54.683  1.00 3.89  ? 527  ARG B CD  1 
ATOM   8961  N  NE  . ARG B  1 527 ? 24.422  48.449  54.432  1.00 3.15  ? 527  ARG B NE  1 
ATOM   8962  C  CZ  . ARG B  1 527 ? 23.957  47.640  55.383  1.00 3.43  ? 527  ARG B CZ  1 
ATOM   8963  N  NH1 . ARG B  1 527 ? 24.238  47.871  56.661  1.00 2.51  ? 527  ARG B NH1 1 
ATOM   8964  N  NH2 . ARG B  1 527 ? 23.216  46.587  55.057  1.00 3.11  ? 527  ARG B NH2 1 
ATOM   8965  N  N   . PHE B  1 528 ? 29.898  46.904  53.628  1.00 2.95  ? 528  PHE B N   1 
ATOM   8966  C  CA  . PHE B  1 528 ? 30.578  45.980  54.528  1.00 2.41  ? 528  PHE B CA  1 
ATOM   8967  C  C   . PHE B  1 528 ? 32.082  45.898  54.282  1.00 2.63  ? 528  PHE B C   1 
ATOM   8968  O  O   . PHE B  1 528 ? 32.732  44.950  54.728  1.00 3.04  ? 528  PHE B O   1 
ATOM   8969  C  CB  . PHE B  1 528 ? 29.974  44.570  54.433  1.00 2.00  ? 528  PHE B CB  1 
ATOM   8970  C  CG  . PHE B  1 528 ? 28.586  44.448  55.010  1.00 2.00  ? 528  PHE B CG  1 
ATOM   8971  C  CD1 . PHE B  1 528 ? 27.470  44.847  54.283  1.00 2.07  ? 528  PHE B CD1 1 
ATOM   8972  C  CD2 . PHE B  1 528 ? 28.393  43.913  56.271  1.00 2.00  ? 528  PHE B CD2 1 
ATOM   8973  C  CE1 . PHE B  1 528 ? 26.180  44.710  54.806  1.00 2.00  ? 528  PHE B CE1 1 
ATOM   8974  C  CE2 . PHE B  1 528 ? 27.105  43.773  56.801  1.00 2.76  ? 528  PHE B CE2 1 
ATOM   8975  C  CZ  . PHE B  1 528 ? 26.000  44.172  56.064  1.00 2.00  ? 528  PHE B CZ  1 
ATOM   8976  N  N   . TRP B  1 529 ? 32.642  46.869  53.568  1.00 2.00  ? 529  TRP B N   1 
ATOM   8977  C  CA  . TRP B  1 529 ? 34.081  46.845  53.355  1.00 2.00  ? 529  TRP B CA  1 
ATOM   8978  C  C   . TRP B  1 529 ? 34.621  46.791  54.786  1.00 2.00  ? 529  TRP B C   1 
ATOM   8979  O  O   . TRP B  1 529 ? 34.187  47.557  55.639  1.00 2.00  ? 529  TRP B O   1 
ATOM   8980  C  CB  . TRP B  1 529 ? 34.545  48.106  52.622  1.00 2.00  ? 529  TRP B CB  1 
ATOM   8981  C  CG  . TRP B  1 529 ? 36.005  48.088  52.319  1.00 2.51  ? 529  TRP B CG  1 
ATOM   8982  C  CD1 . TRP B  1 529 ? 36.997  48.708  53.025  1.00 4.11  ? 529  TRP B CD1 1 
ATOM   8983  C  CD2 . TRP B  1 529 ? 36.658  47.336  51.293  1.00 3.63  ? 529  TRP B CD2 1 
ATOM   8984  N  NE1 . TRP B  1 529 ? 38.228  48.385  52.507  1.00 3.21  ? 529  TRP B NE1 1 
ATOM   8985  C  CE2 . TRP B  1 529 ? 38.049  47.542  51.442  1.00 2.93  ? 529  TRP B CE2 1 
ATOM   8986  C  CE3 . TRP B  1 529 ? 36.205  46.500  50.264  1.00 3.81  ? 529  TRP B CE3 1 
ATOM   8987  C  CZ2 . TRP B  1 529 ? 38.991  46.943  50.603  1.00 2.69  ? 529  TRP B CZ2 1 
ATOM   8988  C  CZ3 . TRP B  1 529 ? 37.147  45.900  49.428  1.00 4.21  ? 529  TRP B CZ3 1 
ATOM   8989  C  CH2 . TRP B  1 529 ? 38.524  46.127  49.605  1.00 3.10  ? 529  TRP B CH2 1 
ATOM   8990  N  N   . TRP B  1 530 ? 35.536  45.869  55.057  1.00 2.05  ? 530  TRP B N   1 
ATOM   8991  C  CA  . TRP B  1 530 ? 36.061  45.704  56.409  1.00 2.61  ? 530  TRP B CA  1 
ATOM   8992  C  C   . TRP B  1 530 ? 36.535  46.979  57.106  1.00 3.15  ? 530  TRP B C   1 
ATOM   8993  O  O   . TRP B  1 530 ? 36.225  47.204  58.281  1.00 2.97  ? 530  TRP B O   1 
ATOM   8994  C  CB  . TRP B  1 530 ? 37.186  44.664  56.416  1.00 2.93  ? 530  TRP B CB  1 
ATOM   8995  C  CG  . TRP B  1 530 ? 38.354  45.039  55.590  1.00 3.01  ? 530  TRP B CG  1 
ATOM   8996  C  CD1 . TRP B  1 530 ? 38.394  45.150  54.232  1.00 3.27  ? 530  TRP B CD1 1 
ATOM   8997  C  CD2 . TRP B  1 530 ? 39.655  45.397  56.065  1.00 2.62  ? 530  TRP B CD2 1 
ATOM   8998  N  NE1 . TRP B  1 530 ? 39.644  45.560  53.829  1.00 4.20  ? 530  TRP B NE1 1 
ATOM   8999  C  CE2 . TRP B  1 530 ? 40.438  45.719  54.934  1.00 3.13  ? 530  TRP B CE2 1 
ATOM   9000  C  CE3 . TRP B  1 530 ? 40.235  45.478  57.336  1.00 2.00  ? 530  TRP B CE3 1 
ATOM   9001  C  CZ2 . TRP B  1 530 ? 41.773  46.120  55.035  1.00 2.38  ? 530  TRP B CZ2 1 
ATOM   9002  C  CZ3 . TRP B  1 530 ? 41.561  45.876  57.436  1.00 2.00  ? 530  TRP B CZ3 1 
ATOM   9003  C  CH2 . TRP B  1 530 ? 42.316  46.191  56.291  1.00 2.00  ? 530  TRP B CH2 1 
ATOM   9004  N  N   . GLU B  1 531 ? 37.279  47.815  56.395  1.00 3.36  ? 531  GLU B N   1 
ATOM   9005  C  CA  . GLU B  1 531 ? 37.779  49.043  56.990  1.00 3.28  ? 531  GLU B CA  1 
ATOM   9006  C  C   . GLU B  1 531 ? 36.709  50.064  57.333  1.00 4.85  ? 531  GLU B C   1 
ATOM   9007  O  O   . GLU B  1 531 ? 36.916  50.899  58.209  1.00 6.52  ? 531  GLU B O   1 
ATOM   9008  C  CB  . GLU B  1 531 ? 38.813  49.689  56.082  1.00 4.15  ? 531  GLU B CB  1 
ATOM   9009  C  CG  . GLU B  1 531 ? 40.169  49.048  56.188  1.00 6.79  ? 531  GLU B CG  1 
ATOM   9010  C  CD  . GLU B  1 531 ? 41.245  49.908  55.571  1.00 9.20  ? 531  GLU B CD  1 
ATOM   9011  O  OE1 . GLU B  1 531 ? 41.230  50.074  54.329  1.00 9.44  ? 531  GLU B OE1 1 
ATOM   9012  O  OE2 . GLU B  1 531 ? 42.096  50.427  56.334  1.00 10.54 ? 531  GLU B OE2 1 
ATOM   9013  N  N   . ASN B  1 532 ? 35.571  50.020  56.651  1.00 4.44  ? 532  ASN B N   1 
ATOM   9014  C  CA  . ASN B  1 532 ? 34.510  50.971  56.951  1.00 3.61  ? 532  ASN B CA  1 
ATOM   9015  C  C   . ASN B  1 532 ? 34.053  50.804  58.397  1.00 3.07  ? 532  ASN B C   1 
ATOM   9016  O  O   . ASN B  1 532 ? 33.697  49.708  58.827  1.00 3.96  ? 532  ASN B O   1 
ATOM   9017  C  CB  . ASN B  1 532 ? 33.322  50.769  56.027  1.00 3.78  ? 532  ASN B CB  1 
ATOM   9018  C  CG  . ASN B  1 532 ? 32.161  51.661  56.392  1.00 5.19  ? 532  ASN B CG  1 
ATOM   9019  O  OD1 . ASN B  1 532 ? 32.262  52.891  56.350  1.00 4.62  ? 532  ASN B OD1 1 
ATOM   9020  N  ND2 . ASN B  1 532 ? 31.047  51.047  56.767  1.00 7.51  ? 532  ASN B ND2 1 
ATOM   9021  N  N   . PRO B  1 533 ? 34.057  51.896  59.169  1.00 2.00  ? 533  PRO B N   1 
ATOM   9022  C  CA  . PRO B  1 533 ? 33.646  51.867  60.575  1.00 2.00  ? 533  PRO B CA  1 
ATOM   9023  C  C   . PRO B  1 533 ? 32.334  51.124  60.859  1.00 2.00  ? 533  PRO B C   1 
ATOM   9024  O  O   . PRO B  1 533 ? 31.324  51.357  60.193  1.00 2.00  ? 533  PRO B O   1 
ATOM   9025  C  CB  . PRO B  1 533 ? 33.564  53.347  60.925  1.00 2.53  ? 533  PRO B CB  1 
ATOM   9026  C  CG  . PRO B  1 533 ? 34.671  53.936  60.089  1.00 2.00  ? 533  PRO B CG  1 
ATOM   9027  C  CD  . PRO B  1 533 ? 34.458  53.256  58.764  1.00 2.00  ? 533  PRO B CD  1 
ATOM   9028  N  N   . GLY B  1 534 ? 32.358  50.226  61.843  1.00 2.00  ? 534  GLY B N   1 
ATOM   9029  C  CA  . GLY B  1 534 ? 31.158  49.486  62.204  1.00 2.67  ? 534  GLY B CA  1 
ATOM   9030  C  C   . GLY B  1 534 ? 31.096  48.011  61.832  1.00 4.38  ? 534  GLY B C   1 
ATOM   9031  O  O   . GLY B  1 534 ? 30.566  47.198  62.602  1.00 4.15  ? 534  GLY B O   1 
ATOM   9032  N  N   . VAL B  1 535 ? 31.629  47.665  60.658  1.00 3.48  ? 535  VAL B N   1 
ATOM   9033  C  CA  . VAL B  1 535 ? 31.629  46.290  60.152  1.00 2.28  ? 535  VAL B CA  1 
ATOM   9034  C  C   . VAL B  1 535 ? 32.449  45.344  61.024  1.00 2.98  ? 535  VAL B C   1 
ATOM   9035  O  O   . VAL B  1 535 ? 32.140  44.156  61.136  1.00 2.07  ? 535  VAL B O   1 
ATOM   9036  C  CB  . VAL B  1 535 ? 32.172  46.249  58.725  1.00 2.27  ? 535  VAL B CB  1 
ATOM   9037  C  CG1 . VAL B  1 535 ? 32.154  44.833  58.207  1.00 2.31  ? 535  VAL B CG1 1 
ATOM   9038  C  CG2 . VAL B  1 535 ? 31.339  47.161  57.834  1.00 3.03  ? 535  VAL B CG2 1 
ATOM   9039  N  N   . PHE B  1 536 ? 33.517  45.886  61.603  1.00 4.16  ? 536  PHE B N   1 
ATOM   9040  C  CA  . PHE B  1 536 ? 34.402  45.172  62.529  1.00 3.96  ? 536  PHE B CA  1 
ATOM   9041  C  C   . PHE B  1 536 ? 34.833  46.272  63.504  1.00 4.29  ? 536  PHE B C   1 
ATOM   9042  O  O   . PHE B  1 536 ? 34.566  47.454  63.258  1.00 4.82  ? 536  PHE B O   1 
ATOM   9043  C  CB  . PHE B  1 536 ? 35.659  44.613  61.842  1.00 3.57  ? 536  PHE B CB  1 
ATOM   9044  C  CG  . PHE B  1 536 ? 35.401  43.479  60.887  1.00 2.00  ? 536  PHE B CG  1 
ATOM   9045  C  CD1 . PHE B  1 536 ? 35.213  43.719  59.538  1.00 2.35  ? 536  PHE B CD1 1 
ATOM   9046  C  CD2 . PHE B  1 536 ? 35.378  42.170  61.332  1.00 2.09  ? 536  PHE B CD2 1 
ATOM   9047  C  CE1 . PHE B  1 536 ? 35.009  42.670  58.647  1.00 2.32  ? 536  PHE B CE1 1 
ATOM   9048  C  CE2 . PHE B  1 536 ? 35.172  41.117  60.441  1.00 2.02  ? 536  PHE B CE2 1 
ATOM   9049  C  CZ  . PHE B  1 536 ? 34.989  41.371  59.100  1.00 2.00  ? 536  PHE B CZ  1 
ATOM   9050  N  N   . THR B  1 537 ? 35.499  45.907  64.596  1.00 3.91  ? 537  THR B N   1 
ATOM   9051  C  CA  . THR B  1 537 ? 35.942  46.919  65.552  1.00 4.65  ? 537  THR B CA  1 
ATOM   9052  C  C   . THR B  1 537 ? 37.440  47.192  65.430  1.00 7.45  ? 537  THR B C   1 
ATOM   9053  O  O   . THR B  1 537 ? 38.161  46.439  64.774  1.00 7.47  ? 537  THR B O   1 
ATOM   9054  C  CB  . THR B  1 537 ? 35.653  46.508  66.995  1.00 2.49  ? 537  THR B CB  1 
ATOM   9055  O  OG1 . THR B  1 537 ? 36.850  45.997  67.590  1.00 3.45  ? 537  THR B OG1 1 
ATOM   9056  C  CG2 . THR B  1 537 ? 34.573  45.450  67.035  1.00 2.79  ? 537  THR B CG2 1 
ATOM   9057  N  N   . GLU B  1 538 ? 37.896  48.270  66.070  1.00 9.83  ? 538  GLU B N   1 
ATOM   9058  C  CA  . GLU B  1 538 ? 39.303  48.674  66.034  1.00 10.98 ? 538  GLU B CA  1 
ATOM   9059  C  C   . GLU B  1 538 ? 40.227  47.510  66.329  1.00 10.92 ? 538  GLU B C   1 
ATOM   9060  O  O   . GLU B  1 538 ? 41.250  47.339  65.670  1.00 10.34 ? 538  GLU B O   1 
ATOM   9061  C  CB  . GLU B  1 538 ? 39.580  49.797  67.052  1.00 15.48 ? 538  GLU B CB  1 
ATOM   9062  C  CG  . GLU B  1 538 ? 41.033  50.336  67.034  1.00 19.61 ? 538  GLU B CG  1 
ATOM   9063  C  CD  . GLU B  1 538 ? 41.362  51.271  68.205  1.00 20.45 ? 538  GLU B CD  1 
ATOM   9064  O  OE1 . GLU B  1 538 ? 40.520  52.126  68.549  1.00 22.79 ? 538  GLU B OE1 1 
ATOM   9065  O  OE2 . GLU B  1 538 ? 42.472  51.162  68.771  1.00 20.40 ? 538  GLU B OE2 1 
ATOM   9066  N  N   . LYS B  1 539 ? 39.872  46.708  67.322  1.00 10.69 ? 539  LYS B N   1 
ATOM   9067  C  CA  . LYS B  1 539 ? 40.712  45.580  67.682  1.00 12.49 ? 539  LYS B CA  1 
ATOM   9068  C  C   . LYS B  1 539 ? 40.585  44.388  66.747  1.00 13.22 ? 539  LYS B C   1 
ATOM   9069  O  O   . LYS B  1 539 ? 41.550  43.639  66.569  1.00 15.66 ? 539  LYS B O   1 
ATOM   9070  C  CB  . LYS B  1 539 ? 40.441  45.147  69.123  1.00 13.24 ? 539  LYS B CB  1 
ATOM   9071  C  CG  . LYS B  1 539 ? 41.593  45.465  70.070  1.00 14.03 ? 539  LYS B CG  1 
ATOM   9072  C  CD  . LYS B  1 539 ? 41.202  45.238  71.519  1.00 14.60 ? 539  LYS B CD  1 
ATOM   9073  C  CE  . LYS B  1 539 ? 40.672  43.828  71.739  1.00 15.90 ? 539  LYS B CE  1 
ATOM   9074  N  NZ  . LYS B  1 539 ? 41.154  43.246  73.032  1.00 16.58 ? 539  LYS B NZ  1 
ATOM   9075  N  N   . GLN B  1 540 ? 39.415  44.192  66.147  1.00 11.90 ? 540  GLN B N   1 
ATOM   9076  C  CA  . GLN B  1 540 ? 39.269  43.072  65.229  1.00 10.63 ? 540  GLN B CA  1 
ATOM   9077  C  C   . GLN B  1 540 ? 40.091  43.366  63.985  1.00 9.80  ? 540  GLN B C   1 
ATOM   9078  O  O   . GLN B  1 540 ? 40.758  42.483  63.458  1.00 10.19 ? 540  GLN B O   1 
ATOM   9079  C  CB  . GLN B  1 540 ? 37.799  42.839  64.873  1.00 10.99 ? 540  GLN B CB  1 
ATOM   9080  C  CG  . GLN B  1 540 ? 36.974  42.376  66.069  1.00 13.64 ? 540  GLN B CG  1 
ATOM   9081  C  CD  . GLN B  1 540 ? 35.556  41.965  65.705  1.00 14.53 ? 540  GLN B CD  1 
ATOM   9082  O  OE1 . GLN B  1 540 ? 34.832  42.707  65.032  1.00 15.80 ? 540  GLN B OE1 1 
ATOM   9083  N  NE2 . GLN B  1 540 ? 35.145  40.783  66.164  1.00 14.74 ? 540  GLN B NE2 1 
ATOM   9084  N  N   . ARG B  1 541 ? 40.060  44.617  63.533  1.00 9.38  ? 541  ARG B N   1 
ATOM   9085  C  CA  . ARG B  1 541 ? 40.824  45.029  62.358  1.00 9.67  ? 541  ARG B CA  1 
ATOM   9086  C  C   . ARG B  1 541 ? 42.312  44.840  62.586  1.00 10.03 ? 541  ARG B C   1 
ATOM   9087  O  O   . ARG B  1 541 ? 43.005  44.213  61.782  1.00 9.34  ? 541  ARG B O   1 
ATOM   9088  C  CB  . ARG B  1 541 ? 40.558  46.500  62.023  1.00 8.96  ? 541  ARG B CB  1 
ATOM   9089  C  CG  . ARG B  1 541 ? 39.270  46.730  61.272  1.00 8.69  ? 541  ARG B CG  1 
ATOM   9090  C  CD  . ARG B  1 541 ? 39.323  48.026  60.502  1.00 9.32  ? 541  ARG B CD  1 
ATOM   9091  N  NE  . ARG B  1 541 ? 39.273  49.197  61.369  1.00 11.60 ? 541  ARG B NE  1 
ATOM   9092  C  CZ  . ARG B  1 541 ? 38.227  49.524  62.125  1.00 13.05 ? 541  ARG B CZ  1 
ATOM   9093  N  NH1 . ARG B  1 541 ? 37.134  48.765  62.128  1.00 12.79 ? 541  ARG B NH1 1 
ATOM   9094  N  NH2 . ARG B  1 541 ? 38.265  50.624  62.867  1.00 13.64 ? 541  ARG B NH2 1 
ATOM   9095  N  N   . ASP B  1 542 ? 42.806  45.402  63.683  1.00 10.44 ? 542  ASP B N   1 
ATOM   9096  C  CA  . ASP B  1 542 ? 44.212  45.286  64.005  1.00 12.16 ? 542  ASP B CA  1 
ATOM   9097  C  C   . ASP B  1 542 ? 44.715  43.876  63.764  1.00 11.34 ? 542  ASP B C   1 
ATOM   9098  O  O   . ASP B  1 542 ? 45.783  43.660  63.186  1.00 9.91  ? 542  ASP B O   1 
ATOM   9099  C  CB  . ASP B  1 542 ? 44.460  45.690  65.451  1.00 16.14 ? 542  ASP B CB  1 
ATOM   9100  C  CG  . ASP B  1 542 ? 44.949  47.110  65.562  1.00 19.15 ? 542  ASP B CG  1 
ATOM   9101  O  OD1 . ASP B  1 542 ? 45.562  47.568  64.569  1.00 19.86 ? 542  ASP B OD1 1 
ATOM   9102  O  OD2 . ASP B  1 542 ? 44.742  47.762  66.613  1.00 20.68 ? 542  ASP B OD2 1 
ATOM   9103  N  N   . SER B  1 543 ? 43.922  42.912  64.204  1.00 10.80 ? 543  SER B N   1 
ATOM   9104  C  CA  . SER B  1 543 ? 44.268  41.509  64.049  1.00 10.84 ? 543  SER B CA  1 
ATOM   9105  C  C   . SER B  1 543 ? 44.196  41.087  62.577  1.00 9.20  ? 543  SER B C   1 
ATOM   9106  O  O   . SER B  1 543 ? 44.943  40.213  62.136  1.00 9.26  ? 543  SER B O   1 
ATOM   9107  C  CB  . SER B  1 543 ? 43.310  40.649  64.896  1.00 10.90 ? 543  SER B CB  1 
ATOM   9108  O  OG  . SER B  1 543 ? 43.713  39.289  64.932  1.00 11.09 ? 543  SER B OG  1 
ATOM   9109  N  N   . LEU B  1 544 ? 43.308  41.719  61.815  1.00 7.87  ? 544  LEU B N   1 
ATOM   9110  C  CA  . LEU B  1 544 ? 43.138  41.349  60.421  1.00 6.50  ? 544  LEU B CA  1 
ATOM   9111  C  C   . LEU B  1 544 ? 44.241  41.793  59.498  1.00 8.15  ? 544  LEU B C   1 
ATOM   9112  O  O   . LEU B  1 544 ? 44.446  41.173  58.461  1.00 9.71  ? 544  LEU B O   1 
ATOM   9113  C  CB  . LEU B  1 544 ? 41.797  41.854  59.879  1.00 3.83  ? 544  LEU B CB  1 
ATOM   9114  C  CG  . LEU B  1 544 ? 40.537  41.116  60.327  1.00 2.31  ? 544  LEU B CG  1 
ATOM   9115  C  CD1 . LEU B  1 544 ? 39.343  41.932  59.918  1.00 2.00  ? 544  LEU B CD1 1 
ATOM   9116  C  CD2 . LEU B  1 544 ? 40.480  39.725  59.726  1.00 2.00  ? 544  LEU B CD2 1 
ATOM   9117  N  N   . GLN B  1 545 ? 44.966  42.850  59.836  1.00 8.06  ? 545  GLN B N   1 
ATOM   9118  C  CA  . GLN B  1 545 ? 46.007  43.254  58.903  1.00 8.03  ? 545  GLN B CA  1 
ATOM   9119  C  C   . GLN B  1 545 ? 47.145  42.245  58.822  1.00 6.28  ? 545  GLN B C   1 
ATOM   9120  O  O   . GLN B  1 545 ? 47.956  42.291  57.898  1.00 3.62  ? 545  GLN B O   1 
ATOM   9121  C  CB  . GLN B  1 545 ? 46.544  44.640  59.238  1.00 11.80 ? 545  GLN B CB  1 
ATOM   9122  C  CG  . GLN B  1 545 ? 46.171  45.152  60.593  1.00 18.84 ? 545  GLN B CG  1 
ATOM   9123  C  CD  . GLN B  1 545 ? 46.817  46.494  60.860  1.00 21.70 ? 545  GLN B CD  1 
ATOM   9124  O  OE1 . GLN B  1 545 ? 46.329  47.547  60.438  1.00 24.23 ? 545  GLN B OE1 1 
ATOM   9125  N  NE2 . GLN B  1 545 ? 47.956  46.467  61.543  1.00 21.81 ? 545  GLN B NE2 1 
ATOM   9126  N  N   . LYS B  1 546 ? 47.173  41.308  59.766  1.00 5.31  ? 546  LYS B N   1 
ATOM   9127  C  CA  . LYS B  1 546 ? 48.225  40.299  59.803  1.00 5.41  ? 546  LYS B CA  1 
ATOM   9128  C  C   . LYS B  1 546 ? 47.966  39.031  58.997  1.00 5.97  ? 546  LYS B C   1 
ATOM   9129  O  O   . LYS B  1 546 ? 48.808  38.130  58.993  1.00 7.01  ? 546  LYS B O   1 
ATOM   9130  C  CB  . LYS B  1 546 ? 48.557  39.906  61.252  1.00 6.92  ? 546  LYS B CB  1 
ATOM   9131  C  CG  . LYS B  1 546 ? 49.202  41.010  62.104  1.00 8.59  ? 546  LYS B CG  1 
ATOM   9132  C  CD  . LYS B  1 546 ? 49.675  40.460  63.458  1.00 10.44 ? 546  LYS B CD  1 
ATOM   9133  C  CE  . LYS B  1 546 ? 49.601  41.505  64.581  1.00 12.44 ? 546  LYS B CE  1 
ATOM   9134  N  NZ  . LYS B  1 546 ? 50.419  42.738  64.359  1.00 13.76 ? 546  LYS B NZ  1 
ATOM   9135  N  N   . VAL B  1 547 ? 46.827  38.932  58.318  1.00 3.40  ? 547  VAL B N   1 
ATOM   9136  C  CA  . VAL B  1 547 ? 46.592  37.727  57.525  1.00 2.64  ? 547  VAL B CA  1 
ATOM   9137  C  C   . VAL B  1 547 ? 47.572  37.696  56.357  1.00 2.00  ? 547  VAL B C   1 
ATOM   9138  O  O   . VAL B  1 547 ? 48.225  38.696  56.062  1.00 2.00  ? 547  VAL B O   1 
ATOM   9139  C  CB  . VAL B  1 547 ? 45.153  37.646  56.953  1.00 2.00  ? 547  VAL B CB  1 
ATOM   9140  C  CG1 . VAL B  1 547 ? 44.234  36.977  57.936  1.00 2.00  ? 547  VAL B CG1 1 
ATOM   9141  C  CG2 . VAL B  1 547 ? 44.646  39.016  56.624  1.00 2.00  ? 547  VAL B CG2 1 
ATOM   9142  N  N   . SER B  1 548 ? 47.668  36.536  55.712  1.00 2.52  ? 548  SER B N   1 
ATOM   9143  C  CA  . SER B  1 548 ? 48.544  36.323  54.560  1.00 2.05  ? 548  SER B CA  1 
ATOM   9144  C  C   . SER B  1 548 ? 48.167  35.005  53.905  1.00 2.00  ? 548  SER B C   1 
ATOM   9145  O  O   . SER B  1 548 ? 47.706  34.092  54.584  1.00 2.00  ? 548  SER B O   1 
ATOM   9146  C  CB  . SER B  1 548 ? 50.000  36.259  55.006  1.00 2.12  ? 548  SER B CB  1 
ATOM   9147  O  OG  . SER B  1 548 ? 50.122  35.442  56.155  1.00 2.00  ? 548  SER B OG  1 
ATOM   9148  N  N   . PHE B  1 549 ? 48.355  34.900  52.593  1.00 2.73  ? 549  PHE B N   1 
ATOM   9149  C  CA  . PHE B  1 549 ? 48.019  33.656  51.917  1.00 2.00  ? 549  PHE B CA  1 
ATOM   9150  C  C   . PHE B  1 549 ? 48.995  32.584  52.377  1.00 2.00  ? 549  PHE B C   1 
ATOM   9151  O  O   . PHE B  1 549 ? 48.658  31.402  52.439  1.00 2.24  ? 549  PHE B O   1 
ATOM   9152  C  CB  . PHE B  1 549 ? 48.079  33.798  50.393  1.00 2.00  ? 549  PHE B CB  1 
ATOM   9153  C  CG  . PHE B  1 549 ? 47.342  32.714  49.683  1.00 2.00  ? 549  PHE B CG  1 
ATOM   9154  C  CD1 . PHE B  1 549 ? 45.963  32.631  49.777  1.00 2.00  ? 549  PHE B CD1 1 
ATOM   9155  C  CD2 . PHE B  1 549 ? 48.023  31.711  49.027  1.00 2.00  ? 549  PHE B CD2 1 
ATOM   9156  C  CE1 . PHE B  1 549 ? 45.275  31.559  49.236  1.00 2.00  ? 549  PHE B CE1 1 
ATOM   9157  C  CE2 . PHE B  1 549 ? 47.344  30.633  48.483  1.00 2.09  ? 549  PHE B CE2 1 
ATOM   9158  C  CZ  . PHE B  1 549 ? 45.964  30.556  48.589  1.00 2.00  ? 549  PHE B CZ  1 
ATOM   9159  N  N   . SER B  1 550 ? 50.206  33.006  52.715  1.00 2.00  ? 550  SER B N   1 
ATOM   9160  C  CA  . SER B  1 550 ? 51.219  32.079  53.192  1.00 2.65  ? 550  SER B CA  1 
ATOM   9161  C  C   . SER B  1 550 ? 50.651  31.418  54.450  1.00 3.71  ? 550  SER B C   1 
ATOM   9162  O  O   . SER B  1 550 ? 50.692  30.198  54.602  1.00 4.97  ? 550  SER B O   1 
ATOM   9163  C  CB  . SER B  1 550 ? 52.505  32.837  53.531  1.00 2.36  ? 550  SER B CB  1 
ATOM   9164  O  OG  . SER B  1 550 ? 52.674  33.970  52.686  1.00 2.58  ? 550  SER B OG  1 
ATOM   9165  N  N   . ARG B  1 551 ? 50.100  32.233  55.345  1.00 3.40  ? 551  ARG B N   1 
ATOM   9166  C  CA  . ARG B  1 551 ? 49.520  31.710  56.574  1.00 2.91  ? 551  ARG B CA  1 
ATOM   9167  C  C   . ARG B  1 551 ? 48.356  30.786  56.258  1.00 2.03  ? 551  ARG B C   1 
ATOM   9168  O  O   . ARG B  1 551 ? 48.129  29.812  56.965  1.00 2.00  ? 551  ARG B O   1 
ATOM   9169  C  CB  . ARG B  1 551 ? 49.013  32.840  57.470  1.00 3.83  ? 551  ARG B CB  1 
ATOM   9170  C  CG  . ARG B  1 551 ? 48.590  32.357  58.850  1.00 4.63  ? 551  ARG B CG  1 
ATOM   9171  C  CD  . ARG B  1 551 ? 49.821  31.974  59.647  1.00 6.95  ? 551  ARG B CD  1 
ATOM   9172  N  NE  . ARG B  1 551 ? 49.656  30.760  60.442  1.00 6.70  ? 551  ARG B NE  1 
ATOM   9173  C  CZ  . ARG B  1 551 ? 50.661  30.141  61.060  1.00 6.27  ? 551  ARG B CZ  1 
ATOM   9174  N  NH1 . ARG B  1 551 ? 51.898  30.623  60.980  1.00 4.33  ? 551  ARG B NH1 1 
ATOM   9175  N  NH2 . ARG B  1 551 ? 50.434  29.028  61.744  1.00 5.49  ? 551  ARG B NH2 1 
ATOM   9176  N  N   . LEU B  1 552 ? 47.608  31.097  55.202  1.00 2.03  ? 552  LEU B N   1 
ATOM   9177  C  CA  . LEU B  1 552 ? 46.476  30.263  54.845  1.00 2.00  ? 552  LEU B CA  1 
ATOM   9178  C  C   . LEU B  1 552 ? 46.974  28.870  54.593  1.00 2.12  ? 552  LEU B C   1 
ATOM   9179  O  O   . LEU B  1 552 ? 46.292  27.902  54.919  1.00 2.98  ? 552  LEU B O   1 
ATOM   9180  C  CB  . LEU B  1 552 ? 45.760  30.747  53.582  1.00 2.00  ? 552  LEU B CB  1 
ATOM   9181  C  CG  . LEU B  1 552 ? 44.550  29.837  53.327  1.00 2.00  ? 552  LEU B CG  1 
ATOM   9182  C  CD1 . LEU B  1 552 ? 43.659  29.943  54.548  1.00 2.73  ? 552  LEU B CD1 1 
ATOM   9183  C  CD2 . LEU B  1 552 ? 43.777  30.208  52.068  1.00 2.00  ? 552  LEU B CD2 1 
ATOM   9184  N  N   . ILE B  1 553 ? 48.167  28.769  54.012  1.00 2.00  ? 553  ILE B N   1 
ATOM   9185  C  CA  . ILE B  1 553 ? 48.746  27.465  53.704  1.00 2.17  ? 553  ILE B CA  1 
ATOM   9186  C  C   . ILE B  1 553 ? 49.134  26.714  54.973  1.00 2.20  ? 553  ILE B C   1 
ATOM   9187  O  O   . ILE B  1 553 ? 48.734  25.565  55.175  1.00 2.00  ? 553  ILE B O   1 
ATOM   9188  C  CB  . ILE B  1 553 ? 49.977  27.608  52.800  1.00 2.00  ? 553  ILE B CB  1 
ATOM   9189  C  CG1 . ILE B  1 553 ? 49.566  28.272  51.485  1.00 2.00  ? 553  ILE B CG1 1 
ATOM   9190  C  CG2 . ILE B  1 553 ? 50.580  26.253  52.542  1.00 2.00  ? 553  ILE B CG2 1 
ATOM   9191  C  CD1 . ILE B  1 553 ? 50.706  28.523  50.524  1.00 2.00  ? 553  ILE B CD1 1 
ATOM   9192  N  N   . CYS B  1 554 ? 49.897  27.388  55.825  1.00 2.00  ? 554  CYS B N   1 
ATOM   9193  C  CA  . CYS B  1 554 ? 50.375  26.834  57.083  1.00 2.00  ? 554  CYS B CA  1 
ATOM   9194  C  C   . CYS B  1 554 ? 49.321  26.243  58.016  1.00 2.00  ? 554  CYS B C   1 
ATOM   9195  O  O   . CYS B  1 554 ? 49.618  25.348  58.803  1.00 2.22  ? 554  CYS B O   1 
ATOM   9196  C  CB  . CYS B  1 554 ? 51.122  27.912  57.844  1.00 2.86  ? 554  CYS B CB  1 
ATOM   9197  S  SG  . CYS B  1 554 ? 52.666  28.431  57.052  1.00 2.46  ? 554  CYS B SG  1 
ATOM   9198  N  N   . ASP B  1 555 ? 48.099  26.749  57.949  1.00 2.09  ? 555  ASP B N   1 
ATOM   9199  C  CA  . ASP B  1 555 ? 47.054  26.263  58.832  1.00 2.67  ? 555  ASP B CA  1 
ATOM   9200  C  C   . ASP B  1 555 ? 46.161  25.167  58.252  1.00 4.63  ? 555  ASP B C   1 
ATOM   9201  O  O   . ASP B  1 555 ? 45.451  24.495  59.010  1.00 5.32  ? 555  ASP B O   1 
ATOM   9202  C  CB  . ASP B  1 555 ? 46.168  27.426  59.300  1.00 2.41  ? 555  ASP B CB  1 
ATOM   9203  C  CG  . ASP B  1 555 ? 46.929  28.459  60.120  1.00 3.30  ? 555  ASP B CG  1 
ATOM   9204  O  OD1 . ASP B  1 555 ? 47.866  28.065  60.845  1.00 3.23  ? 555  ASP B OD1 1 
ATOM   9205  O  OD2 . ASP B  1 555 ? 46.575  29.662  60.056  1.00 3.35  ? 555  ASP B OD2 1 
ATOM   9206  N  N   . ASN B  1 556 ? 46.194  24.958  56.936  1.00 3.28  ? 556  ASN B N   1 
ATOM   9207  C  CA  . ASN B  1 556 ? 45.318  23.950  56.344  1.00 2.69  ? 556  ASN B CA  1 
ATOM   9208  C  C   . ASN B  1 556 ? 45.946  22.889  55.450  1.00 2.00  ? 556  ASN B C   1 
ATOM   9209  O  O   . ASN B  1 556 ? 45.264  22.290  54.621  1.00 2.79  ? 556  ASN B O   1 
ATOM   9210  C  CB  . ASN B  1 556 ? 44.188  24.656  55.594  1.00 3.62  ? 556  ASN B CB  1 
ATOM   9211  C  CG  . ASN B  1 556 ? 43.306  25.476  56.520  1.00 3.04  ? 556  ASN B CG  1 
ATOM   9212  O  OD1 . ASN B  1 556 ? 42.379  24.951  57.146  1.00 3.49  ? 556  ASN B OD1 1 
ATOM   9213  N  ND2 . ASN B  1 556 ? 43.606  26.766  56.629  1.00 2.00  ? 556  ASN B ND2 1 
ATOM   9214  N  N   . THR B  1 557 ? 47.235  22.642  55.628  1.00 2.00  ? 557  THR B N   1 
ATOM   9215  C  CA  . THR B  1 557 ? 47.935  21.632  54.837  1.00 3.12  ? 557  THR B CA  1 
ATOM   9216  C  C   . THR B  1 557 ? 49.093  21.107  55.681  1.00 2.65  ? 557  THR B C   1 
ATOM   9217  O  O   . THR B  1 557 ? 49.185  21.415  56.869  1.00 3.47  ? 557  THR B O   1 
ATOM   9218  C  CB  . THR B  1 557 ? 48.496  22.241  53.525  1.00 2.75  ? 557  THR B CB  1 
ATOM   9219  O  OG1 . THR B  1 557 ? 49.489  23.229  53.831  1.00 3.34  ? 557  THR B OG1 1 
ATOM   9220  C  CG2 . THR B  1 557 ? 47.390  22.908  52.734  1.00 3.88  ? 557  THR B CG2 1 
ATOM   9221  N  N   . HIS B  1 558 ? 49.973  20.308  55.093  1.00 2.00  ? 558  HIS B N   1 
ATOM   9222  C  CA  . HIS B  1 558 ? 51.117  19.837  55.852  1.00 2.00  ? 558  HIS B CA  1 
ATOM   9223  C  C   . HIS B  1 558 ? 52.421  20.412  55.300  1.00 2.55  ? 558  HIS B C   1 
ATOM   9224  O  O   . HIS B  1 558 ? 53.505  19.846  55.501  1.00 2.00  ? 558  HIS B O   1 
ATOM   9225  C  CB  . HIS B  1 558 ? 51.150  18.314  55.904  1.00 3.91  ? 558  HIS B CB  1 
ATOM   9226  C  CG  . HIS B  1 558 ? 50.013  17.722  56.677  1.00 4.34  ? 558  HIS B CG  1 
ATOM   9227  N  ND1 . HIS B  1 558 ? 48.920  17.142  56.067  1.00 4.81  ? 558  HIS B ND1 1 
ATOM   9228  C  CD2 . HIS B  1 558 ? 49.778  17.662  58.010  1.00 4.51  ? 558  HIS B CD2 1 
ATOM   9229  C  CE1 . HIS B  1 558 ? 48.061  16.753  56.991  1.00 5.50  ? 558  HIS B CE1 1 
ATOM   9230  N  NE2 . HIS B  1 558 ? 48.557  17.057  58.179  1.00 5.46  ? 558  HIS B NE2 1 
ATOM   9231  N  N   . ILE B  1 559 ? 52.292  21.549  54.601  1.00 2.86  ? 559  ILE B N   1 
ATOM   9232  C  CA  . ILE B  1 559 ? 53.445  22.269  54.068  1.00 2.97  ? 559  ILE B CA  1 
ATOM   9233  C  C   . ILE B  1 559 ? 54.045  22.904  55.311  1.00 3.40  ? 559  ILE B C   1 
ATOM   9234  O  O   . ILE B  1 559 ? 53.323  23.244  56.247  1.00 5.08  ? 559  ILE B O   1 
ATOM   9235  C  CB  . ILE B  1 559 ? 53.069  23.385  53.066  1.00 2.08  ? 559  ILE B CB  1 
ATOM   9236  C  CG1 . ILE B  1 559 ? 52.666  22.792  51.708  1.00 2.00  ? 559  ILE B CG1 1 
ATOM   9237  C  CG2 . ILE B  1 559 ? 54.274  24.287  52.840  1.00 2.58  ? 559  ILE B CG2 1 
ATOM   9238  C  CD1 . ILE B  1 559 ? 51.271  22.218  51.650  1.00 2.00  ? 559  ILE B CD1 1 
ATOM   9239  N  N   . THR B  1 560 ? 55.353  23.098  55.308  1.00 3.11  ? 560  THR B N   1 
ATOM   9240  C  CA  . THR B  1 560 ? 56.039  23.603  56.485  1.00 2.08  ? 560  THR B CA  1 
ATOM   9241  C  C   . THR B  1 560 ? 56.903  24.835  56.294  1.00 2.00  ? 560  THR B C   1 
ATOM   9242  O  O   . THR B  1 560 ? 56.981  25.710  57.168  1.00 2.00  ? 560  THR B O   1 
ATOM   9243  C  CB  . THR B  1 560 ? 56.896  22.472  57.022  1.00 3.30  ? 560  THR B CB  1 
ATOM   9244  O  OG1 . THR B  1 560 ? 56.065  21.586  57.779  1.00 2.85  ? 560  THR B OG1 1 
ATOM   9245  C  CG2 . THR B  1 560 ? 58.057  23.002  57.846  1.00 3.84  ? 560  THR B CG2 1 
ATOM   9246  N  N   . LYS B  1 561 ? 57.586  24.849  55.155  1.00 3.30  ? 561  LYS B N   1 
ATOM   9247  C  CA  . LYS B  1 561 ? 58.464  25.931  54.759  1.00 3.32  ? 561  LYS B CA  1 
ATOM   9248  C  C   . LYS B  1 561 ? 57.646  26.627  53.675  1.00 2.62  ? 561  LYS B C   1 
ATOM   9249  O  O   . LYS B  1 561 ? 57.127  25.970  52.768  1.00 2.00  ? 561  LYS B O   1 
ATOM   9250  C  CB  . LYS B  1 561 ? 59.767  25.362  54.179  1.00 5.37  ? 561  LYS B CB  1 
ATOM   9251  C  CG  . LYS B  1 561 ? 60.145  23.946  54.689  1.00 9.97  ? 561  LYS B CG  1 
ATOM   9252  C  CD  . LYS B  1 561 ? 60.730  23.913  56.116  1.00 12.16 ? 561  LYS B CD  1 
ATOM   9253  C  CE  . LYS B  1 561 ? 62.257  24.094  56.130  1.00 14.71 ? 561  LYS B CE  1 
ATOM   9254  N  NZ  . LYS B  1 561 ? 62.709  25.435  55.634  1.00 17.47 ? 561  LYS B NZ  1 
ATOM   9255  N  N   . VAL B  1 562 ? 57.502  27.943  53.797  1.00 2.30  ? 562  VAL B N   1 
ATOM   9256  C  CA  . VAL B  1 562 ? 56.733  28.749  52.852  1.00 2.84  ? 562  VAL B CA  1 
ATOM   9257  C  C   . VAL B  1 562 ? 57.290  30.169  52.765  1.00 3.30  ? 562  VAL B C   1 
ATOM   9258  O  O   . VAL B  1 562 ? 57.942  30.648  53.693  1.00 3.97  ? 562  VAL B O   1 
ATOM   9259  C  CB  . VAL B  1 562 ? 55.256  28.834  53.264  1.00 2.00  ? 562  VAL B CB  1 
ATOM   9260  C  CG1 . VAL B  1 562 ? 54.626  27.465  53.203  1.00 2.00  ? 562  VAL B CG1 1 
ATOM   9261  C  CG2 . VAL B  1 562 ? 55.137  29.422  54.663  1.00 2.00  ? 562  VAL B CG2 1 
ATOM   9262  N  N   . PRO B  1 563 ? 57.012  30.869  51.655  1.00 3.55  ? 563  PRO B N   1 
ATOM   9263  C  CA  . PRO B  1 563 ? 57.464  32.242  51.379  1.00 4.78  ? 563  PRO B CA  1 
ATOM   9264  C  C   . PRO B  1 563 ? 56.730  33.328  52.150  1.00 6.69  ? 563  PRO B C   1 
ATOM   9265  O  O   . PRO B  1 563 ? 55.562  33.156  52.497  1.00 7.45  ? 563  PRO B O   1 
ATOM   9266  C  CB  . PRO B  1 563 ? 57.237  32.388  49.873  1.00 5.41  ? 563  PRO B CB  1 
ATOM   9267  C  CG  . PRO B  1 563 ? 57.014  30.937  49.377  1.00 6.22  ? 563  PRO B CG  1 
ATOM   9268  C  CD  . PRO B  1 563 ? 56.264  30.332  50.510  1.00 3.89  ? 563  PRO B CD  1 
ATOM   9269  N  N   . LEU B  1 564 ? 57.410  34.445  52.416  1.00 7.38  ? 564  LEU B N   1 
ATOM   9270  C  CA  . LEU B  1 564 ? 56.766  35.548  53.126  1.00 7.32  ? 564  LEU B CA  1 
ATOM   9271  C  C   . LEU B  1 564 ? 55.862  36.216  52.103  1.00 8.70  ? 564  LEU B C   1 
ATOM   9272  O  O   . LEU B  1 564 ? 54.762  36.652  52.431  1.00 10.65 ? 564  LEU B O   1 
ATOM   9273  C  CB  . LEU B  1 564 ? 57.777  36.588  53.634  1.00 7.96  ? 564  LEU B CB  1 
ATOM   9274  C  CG  . LEU B  1 564 ? 59.036  36.211  54.430  1.00 9.83  ? 564  LEU B CG  1 
ATOM   9275  C  CD1 . LEU B  1 564 ? 59.866  37.472  54.682  1.00 9.32  ? 564  LEU B CD1 1 
ATOM   9276  C  CD2 . LEU B  1 564 ? 58.664  35.548  55.750  1.00 9.51  ? 564  LEU B CD2 1 
ATOM   9277  N  N   . HIS B  1 565 ? 56.316  36.281  50.855  1.00 7.27  ? 565  HIS B N   1 
ATOM   9278  C  CA  . HIS B  1 565 ? 55.518  36.922  49.816  1.00 7.54  ? 565  HIS B CA  1 
ATOM   9279  C  C   . HIS B  1 565 ? 55.071  35.956  48.712  1.00 7.67  ? 565  HIS B C   1 
ATOM   9280  O  O   . HIS B  1 565 ? 55.640  35.919  47.621  1.00 6.91  ? 565  HIS B O   1 
ATOM   9281  C  CB  . HIS B  1 565 ? 56.309  38.098  49.251  1.00 9.09  ? 565  HIS B CB  1 
ATOM   9282  C  CG  . HIS B  1 565 ? 56.826  39.023  50.310  1.00 10.89 ? 565  HIS B CG  1 
ATOM   9283  N  ND1 . HIS B  1 565 ? 55.992  39.735  51.146  1.00 12.03 ? 565  HIS B ND1 1 
ATOM   9284  C  CD2 . HIS B  1 565 ? 58.089  39.315  50.703  1.00 11.83 ? 565  HIS B CD2 1 
ATOM   9285  C  CE1 . HIS B  1 565 ? 56.718  40.423  52.011  1.00 12.83 ? 565  HIS B CE1 1 
ATOM   9286  N  NE2 . HIS B  1 565 ? 57.994  40.186  51.764  1.00 12.82 ? 565  HIS B NE2 1 
ATOM   9287  N  N   . ALA B  1 566 ? 54.022  35.194  49.016  1.00 6.80  ? 566  ALA B N   1 
ATOM   9288  C  CA  . ALA B  1 566 ? 53.465  34.190  48.115  1.00 4.97  ? 566  ALA B CA  1 
ATOM   9289  C  C   . ALA B  1 566 ? 53.207  34.629  46.689  1.00 4.75  ? 566  ALA B C   1 
ATOM   9290  O  O   . ALA B  1 566 ? 53.035  33.785  45.814  1.00 5.07  ? 566  ALA B O   1 
ATOM   9291  C  CB  . ALA B  1 566 ? 52.184  33.623  48.701  1.00 3.03  ? 566  ALA B CB  1 
ATOM   9292  N  N   . PHE B  1 567 ? 53.177  35.928  46.427  1.00 5.69  ? 567  PHE B N   1 
ATOM   9293  C  CA  . PHE B  1 567 ? 52.906  36.351  45.056  1.00 7.03  ? 567  PHE B CA  1 
ATOM   9294  C  C   . PHE B  1 567 ? 54.092  36.651  44.131  1.00 6.20  ? 567  PHE B C   1 
ATOM   9295  O  O   . PHE B  1 567 ? 53.901  36.860  42.941  1.00 5.07  ? 567  PHE B O   1 
ATOM   9296  C  CB  . PHE B  1 567 ? 51.926  37.536  45.049  1.00 4.37  ? 567  PHE B CB  1 
ATOM   9297  C  CG  . PHE B  1 567 ? 50.523  37.163  45.453  1.00 2.48  ? 567  PHE B CG  1 
ATOM   9298  C  CD1 . PHE B  1 567 ? 49.860  36.119  44.832  1.00 2.70  ? 567  PHE B CD1 1 
ATOM   9299  C  CD2 . PHE B  1 567 ? 49.864  37.859  46.451  1.00 2.61  ? 567  PHE B CD2 1 
ATOM   9300  C  CE1 . PHE B  1 567 ? 48.561  35.777  45.203  1.00 2.49  ? 567  PHE B CE1 1 
ATOM   9301  C  CE2 . PHE B  1 567 ? 48.564  37.520  46.823  1.00 2.00  ? 567  PHE B CE2 1 
ATOM   9302  C  CZ  . PHE B  1 567 ? 47.916  36.479  46.198  1.00 2.00  ? 567  PHE B CZ  1 
ATOM   9303  N  N   . GLN B  1 568 ? 55.312  36.670  44.643  1.00 7.34  ? 568  GLN B N   1 
ATOM   9304  C  CA  . GLN B  1 568 ? 56.424  36.949  43.755  1.00 9.34  ? 568  GLN B CA  1 
ATOM   9305  C  C   . GLN B  1 568 ? 57.291  35.713  43.554  1.00 11.52 ? 568  GLN B C   1 
ATOM   9306  O  O   . GLN B  1 568 ? 57.135  34.724  44.272  1.00 13.40 ? 568  GLN B O   1 
ATOM   9307  C  CB  . GLN B  1 568 ? 57.245  38.123  44.293  1.00 11.43 ? 568  GLN B CB  1 
ATOM   9308  C  CG  . GLN B  1 568 ? 57.649  38.005  45.742  1.00 14.51 ? 568  GLN B CG  1 
ATOM   9309  C  CD  . GLN B  1 568 ? 58.293  39.282  46.266  1.00 17.15 ? 568  GLN B CD  1 
ATOM   9310  O  OE1 . GLN B  1 568 ? 57.679  40.356  46.257  1.00 18.41 ? 568  GLN B OE1 1 
ATOM   9311  N  NE2 . GLN B  1 568 ? 59.538  39.171  46.727  1.00 18.11 ? 568  GLN B NE2 1 
ATOM   9312  N  N   . ALA B  1 569 ? 58.183  35.766  42.562  1.00 11.71 ? 569  ALA B N   1 
ATOM   9313  C  CA  . ALA B  1 569 ? 59.088  34.662  42.240  1.00 11.39 ? 569  ALA B CA  1 
ATOM   9314  C  C   . ALA B  1 569 ? 59.978  34.225  43.415  1.00 12.67 ? 569  ALA B C   1 
ATOM   9315  O  O   . ALA B  1 569 ? 60.743  35.032  43.950  1.00 14.18 ? 569  ALA B O   1 
ATOM   9316  C  CB  . ALA B  1 569 ? 59.959  35.057  41.056  1.00 10.70 ? 569  ALA B CB  1 
ATOM   9317  N  N   . ASN B  1 570 ? 59.875  32.949  43.801  1.00 12.94 ? 570  ASN B N   1 
ATOM   9318  C  CA  . ASN B  1 570 ? 60.632  32.402  44.903  1.00 14.72 ? 570  ASN B CA  1 
ATOM   9319  C  C   . ASN B  1 570 ? 61.204  31.051  44.567  1.00 16.61 ? 570  ASN B C   1 
ATOM   9320  O  O   . ASN B  1 570 ? 60.670  30.289  43.757  1.00 18.12 ? 570  ASN B O   1 
ATOM   9321  C  CB  . ASN B  1 570 ? 59.774  32.271  46.142  1.00 15.39 ? 570  ASN B CB  1 
ATOM   9322  C  CG  . ASN B  1 570 ? 59.346  33.621  46.693  1.00 16.14 ? 570  ASN B CG  1 
ATOM   9323  O  OD1 . ASN B  1 570 ? 58.343  33.714  47.405  1.00 17.22 ? 570  ASN B OD1 1 
ATOM   9324  N  ND2 . ASN B  1 570 ? 60.082  34.672  46.352  1.00 16.47 ? 570  ASN B ND2 1 
ATOM   9325  N  N   . ASN B  1 571 ? 62.566  30.942  44.861  1.00 15.45 ? 571  ASN B N   1 
ATOM   9326  C  CA  . ASN B  1 571 ? 63.318  29.730  44.425  1.00 16.82 ? 571  ASN B CA  1 
ATOM   9327  C  C   . ASN B  1 571 ? 63.039  28.703  45.595  1.00 17.12 ? 571  ASN B C   1 
ATOM   9328  O  O   . ASN B  1 571 ? 62.182  29.085  46.380  1.00 16.13 ? 571  ASN B O   1 
ATOM   9329  C  CB  . ASN B  1 571 ? 64.614  30.200  43.718  1.00 19.29 ? 571  ASN B CB  1 
ATOM   9330  C  CG  . ASN B  1 571 ? 64.224  30.778  42.332  1.00 21.67 ? 571  ASN B CG  1 
ATOM   9331  O  OD1 . ASN B  1 571 ? 64.263  30.040  41.343  1.00 20.85 ? 571  ASN B OD1 1 
ATOM   9332  N  ND2 . ASN B  1 571 ? 63.883  32.065  42.294  1.00 22.58 ? 571  ASN B ND2 1 
ATOM   9333  N  N   . TYR B  1 572 ? 63.585  27.417  45.813  1.00 18.19 ? 572  TYR B N   1 
ATOM   9334  C  CA  . TYR B  1 572 ? 63.130  26.610  47.041  1.00 20.98 ? 572  TYR B CA  1 
ATOM   9335  C  C   . TYR B  1 572 ? 63.988  26.886  48.301  1.00 24.80 ? 572  TYR B C   1 
ATOM   9336  O  O   . TYR B  1 572 ? 63.441  27.514  49.200  1.00 28.36 ? 572  TYR B O   1 
ATOM   9337  C  CB  . TYR B  1 572 ? 63.121  25.016  46.989  1.00 21.36 ? 572  TYR B CB  1 
ATOM   9338  C  CG  . TYR B  1 572 ? 62.891  24.342  48.392  1.00 21.22 ? 572  TYR B CG  1 
ATOM   9339  C  CD1 . TYR B  1 572 ? 61.908  24.800  49.264  1.00 20.18 ? 572  TYR B CD1 1 
ATOM   9340  C  CD2 . TYR B  1 572 ? 63.655  23.264  48.835  1.00 21.22 ? 572  TYR B CD2 1 
ATOM   9341  C  CE1 . TYR B  1 572 ? 61.722  24.185  50.513  1.00 20.18 ? 572  TYR B CE1 1 
ATOM   9342  C  CE2 . TYR B  1 572 ? 63.485  22.644  50.089  1.00 22.30 ? 572  TYR B CE2 1 
ATOM   9343  C  CZ  . TYR B  1 572 ? 62.498  23.127  50.912  1.00 22.08 ? 572  TYR B CZ  1 
ATOM   9344  O  OH  . TYR B  1 572 ? 62.274  22.555  52.137  1.00 23.97 ? 572  TYR B OH  1 
ATOM   9345  N  N   . PRO B  1 573 ? 65.349  26.495  48.495  1.00 24.04 ? 573  PRO B N   1 
ATOM   9346  C  CA  . PRO B  1 573 ? 65.978  26.843  49.877  1.00 23.05 ? 573  PRO B CA  1 
ATOM   9347  C  C   . PRO B  1 573 ? 66.020  28.113  50.610  1.00 24.85 ? 573  PRO B C   1 
ATOM   9348  O  O   . PRO B  1 573 ? 65.893  28.131  51.842  1.00 25.51 ? 573  PRO B O   1 
ATOM   9349  C  CB  . PRO B  1 573 ? 67.426  26.461  49.863  1.00 23.76 ? 573  PRO B CB  1 
ATOM   9350  C  CG  . PRO B  1 573 ? 67.335  25.176  49.195  1.00 24.67 ? 573  PRO B CG  1 
ATOM   9351  C  CD  . PRO B  1 573 ? 66.012  25.136  48.473  1.00 23.93 ? 573  PRO B CD  1 
ATOM   9352  N  N   . HIS B  1 574 ? 66.207  29.161  49.905  1.00 25.34 ? 574  HIS B N   1 
ATOM   9353  C  CA  . HIS B  1 574 ? 66.396  30.413  50.593  1.00 23.48 ? 574  HIS B CA  1 
ATOM   9354  C  C   . HIS B  1 574 ? 65.180  31.221  50.850  1.00 21.27 ? 574  HIS B C   1 
ATOM   9355  O  O   . HIS B  1 574 ? 64.963  31.718  51.969  1.00 20.89 ? 574  HIS B O   1 
ATOM   9356  C  CB  . HIS B  1 574 ? 67.401  31.139  49.751  1.00 29.62 ? 574  HIS B CB  1 
ATOM   9357  C  CG  . HIS B  1 574 ? 68.012  32.308  50.461  1.00 35.25 ? 574  HIS B CG  1 
ATOM   9358  N  ND1 . HIS B  1 574 ? 68.157  32.427  51.830  1.00 37.38 ? 574  HIS B ND1 1 
ATOM   9359  C  CD2 . HIS B  1 574 ? 68.536  33.435  49.930  1.00 36.79 ? 574  HIS B CD2 1 
ATOM   9360  C  CE1 . HIS B  1 574 ? 68.749  33.570  52.111  1.00 38.89 ? 574  HIS B CE1 1 
ATOM   9361  N  NE2 . HIS B  1 574 ? 68.992  34.204  50.977  1.00 39.73 ? 574  HIS B NE2 1 
ATOM   9362  N  N   . ASP B  1 575 ? 64.397  31.361  49.813  1.00 18.07 ? 575  ASP B N   1 
ATOM   9363  C  CA  . ASP B  1 575 ? 63.223  32.216  49.953  1.00 14.90 ? 575  ASP B CA  1 
ATOM   9364  C  C   . ASP B  1 575 ? 62.127  31.657  50.856  1.00 13.12 ? 575  ASP B C   1 
ATOM   9365  O  O   . ASP B  1 575 ? 61.123  32.326  51.122  1.00 14.02 ? 575  ASP B O   1 
ATOM   9366  C  CB  . ASP B  1 575 ? 62.637  32.557  48.586  1.00 15.53 ? 575  ASP B CB  1 
ATOM   9367  C  CG  . ASP B  1 575 ? 63.603  33.351  47.717  1.00 15.91 ? 575  ASP B CG  1 
ATOM   9368  O  OD1 . ASP B  1 575 ? 64.312  34.231  48.250  1.00 15.45 ? 575  ASP B OD1 1 
ATOM   9369  O  OD2 . ASP B  1 575 ? 63.644  33.104  46.494  1.00 17.23 ? 575  ASP B OD2 1 
ATOM   9370  N  N   . PHE B  1 576 ? 62.332  30.436  51.333  1.00 11.47 ? 576  PHE B N   1 
ATOM   9371  C  CA  . PHE B  1 576 ? 61.376  29.771  52.207  1.00 11.64 ? 576  PHE B CA  1 
ATOM   9372  C  C   . PHE B  1 576 ? 61.783  29.813  53.682  1.00 12.22 ? 576  PHE B C   1 
ATOM   9373  O  O   . PHE B  1 576 ? 62.970  29.847  54.015  1.00 12.58 ? 576  PHE B O   1 
ATOM   9374  C  CB  . PHE B  1 576 ? 61.183  28.330  51.745  1.00 11.60 ? 576  PHE B CB  1 
ATOM   9375  C  CG  . PHE B  1 576 ? 60.367  28.210  50.489  1.00 12.82 ? 576  PHE B CG  1 
ATOM   9376  C  CD1 . PHE B  1 576 ? 60.838  28.690  49.268  1.00 12.49 ? 576  PHE B CD1 1 
ATOM   9377  C  CD2 . PHE B  1 576 ? 59.103  27.634  50.532  1.00 14.03 ? 576  PHE B CD2 1 
ATOM   9378  C  CE1 . PHE B  1 576 ? 60.054  28.593  48.112  1.00 12.89 ? 576  PHE B CE1 1 
ATOM   9379  C  CE2 . PHE B  1 576 ? 58.315  27.534  49.387  1.00 13.56 ? 576  PHE B CE2 1 
ATOM   9380  C  CZ  . PHE B  1 576 ? 58.790  28.013  48.176  1.00 13.28 ? 576  PHE B CZ  1 
ATOM   9381  N  N   . VAL B  1 577 ? 60.778  29.807  54.557  1.00 11.37 ? 577  VAL B N   1 
ATOM   9382  C  CA  . VAL B  1 577 ? 60.979  29.858  56.002  1.00 9.22  ? 577  VAL B CA  1 
ATOM   9383  C  C   . VAL B  1 577 ? 59.946  28.997  56.702  1.00 8.84  ? 577  VAL B C   1 
ATOM   9384  O  O   . VAL B  1 577 ? 58.807  28.908  56.256  1.00 7.92  ? 577  VAL B O   1 
ATOM   9385  C  CB  . VAL B  1 577 ? 60.809  31.295  56.503  1.00 9.53  ? 577  VAL B CB  1 
ATOM   9386  C  CG1 . VAL B  1 577 ? 61.728  32.220  55.730  1.00 9.82  ? 577  VAL B CG1 1 
ATOM   9387  C  CG2 . VAL B  1 577 ? 59.357  31.735  56.328  1.00 8.47  ? 577  VAL B CG2 1 
ATOM   9388  N  N   . ASP B  1 578 ? 60.314  28.360  57.802  1.00 9.28  ? 578  ASP B N   1 
ATOM   9389  C  CA  . ASP B  1 578 ? 59.332  27.545  58.503  1.00 10.27 ? 578  ASP B CA  1 
ATOM   9390  C  C   . ASP B  1 578 ? 58.160  28.422  58.964  1.00 8.92  ? 578  ASP B C   1 
ATOM   9391  O  O   . ASP B  1 578 ? 58.364  29.545  59.406  1.00 7.15  ? 578  ASP B O   1 
ATOM   9392  C  CB  . ASP B  1 578 ? 59.948  26.882  59.715  1.00 12.56 ? 578  ASP B CB  1 
ATOM   9393  C  CG  . ASP B  1 578 ? 59.040  25.849  60.310  1.00 14.19 ? 578  ASP B CG  1 
ATOM   9394  O  OD1 . ASP B  1 578 ? 59.020  24.714  59.802  1.00 15.24 ? 578  ASP B OD1 1 
ATOM   9395  O  OD2 . ASP B  1 578 ? 58.324  26.180  61.268  1.00 14.33 ? 578  ASP B OD2 1 
ATOM   9396  N  N   . CYS B  1 579 ? 56.939  27.906  58.889  1.00 8.88  ? 579  CYS B N   1 
ATOM   9397  C  CA  . CYS B  1 579 ? 55.763  28.697  59.266  1.00 9.78  ? 579  CYS B CA  1 
ATOM   9398  C  C   . CYS B  1 579 ? 55.828  29.564  60.531  1.00 11.50 ? 579  CYS B C   1 
ATOM   9399  O  O   . CYS B  1 579 ? 55.173  30.607  60.599  1.00 13.31 ? 579  CYS B O   1 
ATOM   9400  C  CB  . CYS B  1 579 ? 54.534  27.800  59.373  1.00 9.11  ? 579  CYS B CB  1 
ATOM   9401  S  SG  . CYS B  1 579 ? 53.965  27.083  57.789  1.00 11.10 ? 579  CYS B SG  1 
ATOM   9402  N  N   . SER B  1 580 ? 56.589  29.152  61.535  1.00 10.29 ? 580  SER B N   1 
ATOM   9403  C  CA  . SER B  1 580 ? 56.660  29.934  62.765  1.00 9.63  ? 580  SER B CA  1 
ATOM   9404  C  C   . SER B  1 580 ? 57.266  31.328  62.594  1.00 10.22 ? 580  SER B C   1 
ATOM   9405  O  O   . SER B  1 580 ? 57.489  32.044  63.573  1.00 9.72  ? 580  SER B O   1 
ATOM   9406  C  CB  . SER B  1 580 ? 57.451  29.159  63.801  1.00 9.93  ? 580  SER B CB  1 
ATOM   9407  O  OG  . SER B  1 580 ? 58.658  28.693  63.223  1.00 10.73 ? 580  SER B OG  1 
ATOM   9408  N  N   . ALA B  1 581 ? 57.541  31.717  61.357  1.00 9.52  ? 581  ALA B N   1 
ATOM   9409  C  CA  . ALA B  1 581 ? 58.115  33.029  61.114  1.00 11.28 ? 581  ALA B CA  1 
ATOM   9410  C  C   . ALA B  1 581 ? 57.095  33.938  60.544  1.00 13.64 ? 581  ALA B C   1 
ATOM   9411  O  O   . ALA B  1 581 ? 57.384  35.037  60.098  1.00 13.77 ? 581  ALA B O   1 
ATOM   9412  C  CB  . ALA B  1 581 ? 59.316  32.934  60.182  1.00 10.58 ? 581  ALA B CB  1 
ATOM   9413  N  N   . ILE B  1 582 ? 55.913  33.424  60.564  1.00 14.34 ? 582  ILE B N   1 
ATOM   9414  C  CA  . ILE B  1 582 ? 54.869  34.220  59.993  1.00 15.97 ? 582  ILE B CA  1 
ATOM   9415  C  C   . ILE B  1 582 ? 53.663  34.355  60.879  1.00 18.85 ? 582  ILE B C   1 
ATOM   9416  O  O   . ILE B  1 582 ? 53.239  33.417  61.551  1.00 18.87 ? 582  ILE B O   1 
ATOM   9417  C  CB  . ILE B  1 582 ? 54.483  33.663  58.620  1.00 16.02 ? 582  ILE B CB  1 
ATOM   9418  C  CG1 . ILE B  1 582 ? 53.006  33.952  58.363  1.00 18.05 ? 582  ILE B CG1 1 
ATOM   9419  C  CG2 . ILE B  1 582 ? 54.764  32.163  58.553  1.00 15.05 ? 582  ILE B CG2 1 
ATOM   9420  C  CD1 . ILE B  1 582 ? 52.567  33.592  56.961  1.00 22.01 ? 582  ILE B CD1 1 
ATOM   9421  N  N   . ASP B  1 583 ? 53.106  35.592  60.870  1.00 20.03 ? 583  ASP B N   1 
ATOM   9422  C  CA  . ASP B  1 583 ? 51.945  36.052  61.677  1.00 19.92 ? 583  ASP B CA  1 
ATOM   9423  C  C   . ASP B  1 583 ? 50.792  35.036  61.686  1.00 19.23 ? 583  ASP B C   1 
ATOM   9424  O  O   . ASP B  1 583 ? 50.708  34.188  60.803  1.00 17.85 ? 583  ASP B O   1 
ATOM   9425  C  CB  . ASP B  1 583 ? 51.473  37.438  61.217  1.00 22.86 ? 583  ASP B CB  1 
ATOM   9426  C  CG  . ASP B  1 583 ? 52.458  38.551  61.601  1.00 24.18 ? 583  ASP B CG  1 
ATOM   9427  O  OD1 . ASP B  1 583 ? 53.684  38.287  61.636  1.00 24.53 ? 583  ASP B OD1 1 
ATOM   9428  O  OD2 . ASP B  1 583 ? 52.009  39.691  61.859  1.00 23.95 ? 583  ASP B OD2 1 
ATOM   9429  N  N   . LYS B  1 584 ? 49.915  35.132  62.692  1.00 18.51 ? 584  LYS B N   1 
ATOM   9430  C  CA  . LYS B  1 584 ? 48.851  34.137  62.892  1.00 17.47 ? 584  LYS B CA  1 
ATOM   9431  C  C   . LYS B  1 584 ? 47.337  34.454  62.911  1.00 14.37 ? 584  LYS B C   1 
ATOM   9432  O  O   . LYS B  1 584 ? 46.528  33.525  62.902  1.00 14.94 ? 584  LYS B O   1 
ATOM   9433  C  CB  . LYS B  1 584 ? 49.206  33.386  64.187  1.00 20.41 ? 584  LYS B CB  1 
ATOM   9434  C  CG  . LYS B  1 584 ? 48.423  32.118  64.492  1.00 23.71 ? 584  LYS B CG  1 
ATOM   9435  C  CD  . LYS B  1 584 ? 48.745  31.006  63.504  1.00 25.27 ? 584  LYS B CD  1 
ATOM   9436  C  CE  . LYS B  1 584 ? 48.291  29.655  64.043  1.00 26.85 ? 584  LYS B CE  1 
ATOM   9437  N  NZ  . LYS B  1 584 ? 48.930  29.346  65.368  1.00 28.38 ? 584  LYS B NZ  1 
ATOM   9438  N  N   . LEU B  1 585 ? 46.933  35.719  62.920  1.00 11.00 ? 585  LEU B N   1 
ATOM   9439  C  CA  . LEU B  1 585 ? 45.496  36.056  62.996  1.00 8.35  ? 585  LEU B CA  1 
ATOM   9440  C  C   . LEU B  1 585 ? 44.963  35.630  64.358  1.00 7.34  ? 585  LEU B C   1 
ATOM   9441  O  O   . LEU B  1 585 ? 44.447  34.519  64.533  1.00 5.91  ? 585  LEU B O   1 
ATOM   9442  C  CB  . LEU B  1 585 ? 44.636  35.371  61.917  1.00 3.88  ? 585  LEU B CB  1 
ATOM   9443  C  CG  . LEU B  1 585 ? 43.145  35.670  62.187  1.00 2.00  ? 585  LEU B CG  1 
ATOM   9444  C  CD1 . LEU B  1 585 ? 42.922  37.156  62.103  1.00 2.00  ? 585  LEU B CD1 1 
ATOM   9445  C  CD2 . LEU B  1 585 ? 42.228  34.964  61.217  1.00 2.02  ? 585  LEU B CD2 1 
ATOM   9446  N  N   . ASP B  1 586 ? 45.097  36.536  65.316  1.00 6.84  ? 586  ASP B N   1 
ATOM   9447  C  CA  . ASP B  1 586 ? 44.658  36.297  66.672  1.00 5.56  ? 586  ASP B CA  1 
ATOM   9448  C  C   . ASP B  1 586 ? 43.162  36.470  66.755  1.00 4.12  ? 586  ASP B C   1 
ATOM   9449  O  O   . ASP B  1 586 ? 42.681  37.591  66.685  1.00 3.81  ? 586  ASP B O   1 
ATOM   9450  C  CB  . ASP B  1 586 ? 45.315  37.304  67.602  1.00 8.62  ? 586  ASP B CB  1 
ATOM   9451  C  CG  . ASP B  1 586 ? 44.931  37.087  69.036  1.00 11.64 ? 586  ASP B CG  1 
ATOM   9452  O  OD1 . ASP B  1 586 ? 43.913  36.398  69.271  1.00 13.62 ? 586  ASP B OD1 1 
ATOM   9453  O  OD2 . ASP B  1 586 ? 45.640  37.606  69.925  1.00 13.65 ? 586  ASP B OD2 1 
ATOM   9454  N  N   . LEU B  1 587 ? 42.416  35.384  66.914  1.00 2.42  ? 587  LEU B N   1 
ATOM   9455  C  CA  . LEU B  1 587 ? 40.968  35.527  67.005  1.00 3.22  ? 587  LEU B CA  1 
ATOM   9456  C  C   . LEU B  1 587 ? 40.502  35.927  68.410  1.00 2.51  ? 587  LEU B C   1 
ATOM   9457  O  O   . LEU B  1 587 ? 39.307  35.878  68.705  1.00 2.18  ? 587  LEU B O   1 
ATOM   9458  C  CB  . LEU B  1 587 ? 40.253  34.234  66.581  1.00 3.35  ? 587  LEU B CB  1 
ATOM   9459  C  CG  . LEU B  1 587 ? 40.198  33.750  65.124  1.00 4.25  ? 587  LEU B CG  1 
ATOM   9460  C  CD1 . LEU B  1 587 ? 39.298  32.523  65.106  1.00 6.18  ? 587  LEU B CD1 1 
ATOM   9461  C  CD2 . LEU B  1 587 ? 39.646  34.805  64.158  1.00 3.21  ? 587  LEU B CD2 1 
ATOM   9462  N  N   . SER B  1 588 ? 41.427  36.340  69.272  1.00 2.00  ? 588  SER B N   1 
ATOM   9463  C  CA  . SER B  1 588 ? 41.045  36.725  70.629  1.00 3.16  ? 588  SER B CA  1 
ATOM   9464  C  C   . SER B  1 588 ? 39.978  37.836  70.676  1.00 3.46  ? 588  SER B C   1 
ATOM   9465  O  O   . SER B  1 588 ? 38.941  37.679  71.327  1.00 4.74  ? 588  SER B O   1 
ATOM   9466  C  CB  . SER B  1 588 ? 42.283  37.124  71.467  1.00 2.95  ? 588  SER B CB  1 
ATOM   9467  O  OG  . SER B  1 588 ? 42.782  38.418  71.163  1.00 3.64  ? 588  SER B OG  1 
ATOM   9468  N  N   . PRO B  1 589 ? 40.209  38.966  69.987  1.00 2.43  ? 589  PRO B N   1 
ATOM   9469  C  CA  . PRO B  1 589 ? 39.201  40.023  70.029  1.00 2.79  ? 589  PRO B CA  1 
ATOM   9470  C  C   . PRO B  1 589 ? 37.773  39.564  69.752  1.00 3.15  ? 589  PRO B C   1 
ATOM   9471  O  O   . PRO B  1 589 ? 36.822  40.222  70.152  1.00 4.28  ? 589  PRO B O   1 
ATOM   9472  C  CB  . PRO B  1 589 ? 39.706  41.011  68.987  1.00 2.00  ? 589  PRO B CB  1 
ATOM   9473  C  CG  . PRO B  1 589 ? 41.177  40.916  69.166  1.00 2.00  ? 589  PRO B CG  1 
ATOM   9474  C  CD  . PRO B  1 589 ? 41.382  39.416  69.220  1.00 3.16  ? 589  PRO B CD  1 
ATOM   9475  N  N   . TRP B  1 590 ? 37.604  38.441  69.072  1.00 4.25  ? 590  TRP B N   1 
ATOM   9476  C  CA  . TRP B  1 590 ? 36.250  37.982  68.788  1.00 5.26  ? 590  TRP B CA  1 
ATOM   9477  C  C   . TRP B  1 590 ? 35.553  37.457  70.034  1.00 7.71  ? 590  TRP B C   1 
ATOM   9478  O  O   . TRP B  1 590 ? 34.352  37.189  70.013  1.00 6.32  ? 590  TRP B O   1 
ATOM   9479  C  CB  . TRP B  1 590 ? 36.270  36.924  67.680  1.00 4.29  ? 590  TRP B CB  1 
ATOM   9480  C  CG  . TRP B  1 590 ? 36.217  37.546  66.323  1.00 2.74  ? 590  TRP B CG  1 
ATOM   9481  C  CD1 . TRP B  1 590 ? 35.104  37.741  65.560  1.00 2.70  ? 590  TRP B CD1 1 
ATOM   9482  C  CD2 . TRP B  1 590 ? 37.299  38.167  65.621  1.00 2.00  ? 590  TRP B CD2 1 
ATOM   9483  N  NE1 . TRP B  1 590 ? 35.422  38.454  64.430  1.00 3.01  ? 590  TRP B NE1 1 
ATOM   9484  C  CE2 . TRP B  1 590 ? 36.764  38.730  64.443  1.00 2.10  ? 590  TRP B CE2 1 
ATOM   9485  C  CE3 . TRP B  1 590 ? 38.668  38.310  65.876  1.00 2.00  ? 590  TRP B CE3 1 
ATOM   9486  C  CZ2 . TRP B  1 590 ? 37.551  39.425  63.518  1.00 2.00  ? 590  TRP B CZ2 1 
ATOM   9487  C  CZ3 . TRP B  1 590 ? 39.451  39.003  64.956  1.00 2.25  ? 590  TRP B CZ3 1 
ATOM   9488  C  CH2 . TRP B  1 590 ? 38.888  39.551  63.791  1.00 2.47  ? 590  TRP B CH2 1 
ATOM   9489  N  N   . ALA B  1 591 ? 36.312  37.327  71.120  1.00 11.86 ? 591  ALA B N   1 
ATOM   9490  C  CA  . ALA B  1 591 ? 35.777  36.850  72.394  1.00 16.72 ? 591  ALA B CA  1 
ATOM   9491  C  C   . ALA B  1 591 ? 34.624  37.741  72.858  1.00 20.90 ? 591  ALA B C   1 
ATOM   9492  O  O   . ALA B  1 591 ? 34.713  38.968  72.781  1.00 22.31 ? 591  ALA B O   1 
ATOM   9493  C  CB  . ALA B  1 591 ? 36.879  36.847  73.450  1.00 14.07 ? 591  ALA B CB  1 
ATOM   9494  N  N   . SER B  1 592 ? 33.539  37.134  73.331  1.00 25.34 ? 592  SER B N   1 
ATOM   9495  C  CA  . SER B  1 592 ? 32.410  37.923  73.811  1.00 30.20 ? 592  SER B CA  1 
ATOM   9496  C  C   . SER B  1 592 ? 32.192  37.626  75.280  1.00 34.24 ? 592  SER B C   1 
ATOM   9497  O  O   . SER B  1 592 ? 31.956  36.479  75.667  1.00 34.32 ? 592  SER B O   1 
ATOM   9498  C  CB  . SER B  1 592 ? 31.134  37.615  73.027  1.00 30.71 ? 592  SER B CB  1 
ATOM   9499  O  OG  . SER B  1 592 ? 30.122  38.560  73.343  1.00 31.32 ? 592  SER B OG  1 
ATOM   9500  N  N   . ARG B  1 593 ? 32.269  38.677  76.091  1.00 39.34 ? 593  ARG B N   1 
ATOM   9501  C  CA  . ARG B  1 593 ? 32.115  38.571  77.536  1.00 43.43 ? 593  ARG B CA  1 
ATOM   9502  C  C   . ARG B  1 593 ? 30.665  38.845  77.954  1.00 45.33 ? 593  ARG B C   1 
ATOM   9503  O  O   . ARG B  1 593 ? 30.049  39.821  77.517  1.00 45.63 ? 593  ARG B O   1 
ATOM   9504  C  CB  . ARG B  1 593 ? 33.102  39.545  78.196  1.00 45.49 ? 593  ARG B CB  1 
ATOM   9505  C  CG  . ARG B  1 593 ? 34.339  39.793  77.304  1.00 48.75 ? 593  ARG B CG  1 
ATOM   9506  C  CD  . ARG B  1 593 ? 35.580  40.277  78.052  1.00 51.64 ? 593  ARG B CD  1 
ATOM   9507  N  NE  . ARG B  1 593 ? 36.085  39.291  79.010  1.00 55.10 ? 593  ARG B NE  1 
ATOM   9508  C  CZ  . ARG B  1 593 ? 37.197  39.439  79.731  1.00 56.21 ? 593  ARG B CZ  1 
ATOM   9509  N  NH1 . ARG B  1 593 ? 37.940  40.534  79.609  1.00 57.06 ? 593  ARG B NH1 1 
ATOM   9510  N  NH2 . ARG B  1 593 ? 37.563  38.497  80.590  1.00 56.91 ? 593  ARG B NH2 1 
ATOM   9511  N  N   . GLU B  1 594 ? 30.127  37.964  78.793  1.00 47.01 ? 594  GLU B N   1 
ATOM   9512  C  CA  . GLU B  1 594 ? 28.745  38.059  79.260  1.00 49.01 ? 594  GLU B CA  1 
ATOM   9513  C  C   . GLU B  1 594 ? 28.349  39.325  80.008  1.00 50.15 ? 594  GLU B C   1 
ATOM   9514  O  O   . GLU B  1 594 ? 27.820  40.278  79.423  1.00 48.99 ? 594  GLU B O   1 
ATOM   9515  C  CB  . GLU B  1 594 ? 28.418  36.843  80.130  1.00 48.71 ? 594  GLU B CB  1 
ATOM   9516  C  CG  . GLU B  1 594 ? 28.544  35.564  79.359  1.00 48.78 ? 594  GLU B CG  1 
ATOM   9517  C  CD  . GLU B  1 594 ? 27.886  35.692  78.013  1.00 48.07 ? 594  GLU B CD  1 
ATOM   9518  O  OE1 . GLU B  1 594 ? 26.638  35.718  77.968  1.00 47.56 ? 594  GLU B OE1 1 
ATOM   9519  O  OE2 . GLU B  1 594 ? 28.620  35.795  77.008  1.00 48.03 ? 594  GLU B OE2 1 
ATOM   9520  N  N   . ASN B  1 595 ? 28.597  39.311  81.312  1.00 51.49 ? 595  ASN B N   1 
ATOM   9521  C  CA  . ASN B  1 595 ? 28.254  40.429  82.173  1.00 53.26 ? 595  ASN B CA  1 
ATOM   9522  C  C   . ASN B  1 595 ? 29.356  41.497  82.192  1.00 53.58 ? 595  ASN B C   1 
ATOM   9523  O  O   . ASN B  1 595 ? 29.083  42.616  82.684  1.00 53.60 ? 595  ASN B O   1 
ATOM   9524  C  CB  . ASN B  1 595 ? 27.957  39.911  83.593  1.00 54.42 ? 595  ASN B CB  1 
ATOM   9525  C  CG  . ASN B  1 595 ? 26.914  38.782  83.606  1.00 55.64 ? 595  ASN B CG  1 
ATOM   9526  O  OD1 . ASN B  1 595 ? 26.308  38.492  84.640  1.00 56.52 ? 595  ASN B OD1 1 
ATOM   9527  N  ND2 . ASN B  1 595 ? 26.715  38.137  82.458  1.00 55.51 ? 595  ASN B ND2 1 
ATOM   9528  O  OXT . ASN B  1 595 ? 30.476  41.207  81.709  1.00 52.74 ? 595  ASN B OXT 1 
HETATM 9529  C  C1  . NAG C  2 .   ? -15.805 -14.886 -4.151  1.00 40.59 ? 596  NAG A C1  1 
HETATM 9530  C  C2  . NAG C  2 .   ? -17.084 -15.595 -4.677  1.00 44.92 ? 596  NAG A C2  1 
HETATM 9531  C  C3  . NAG C  2 .   ? -17.339 -14.953 -6.029  1.00 48.28 ? 596  NAG A C3  1 
HETATM 9532  C  C4  . NAG C  2 .   ? -17.845 -13.568 -5.668  1.00 49.98 ? 596  NAG A C4  1 
HETATM 9533  C  C5  . NAG C  2 .   ? -16.614 -12.825 -5.227  1.00 46.86 ? 596  NAG A C5  1 
HETATM 9534  C  C6  . NAG C  2 .   ? -16.916 -11.387 -4.946  1.00 47.41 ? 596  NAG A C6  1 
HETATM 9535  C  C7  . NAG C  2 .   ? -18.271 -17.594 -5.071  1.00 58.06 ? 596  NAG A C7  1 
HETATM 9536  C  C8  . NAG C  2 .   ? -18.377 -19.115 -5.288  1.00 58.85 ? 596  NAG A C8  1 
HETATM 9537  N  N2  . NAG C  2 .   ? -17.086 -17.044 -4.778  1.00 53.01 ? 596  NAG A N2  1 
HETATM 9538  O  O3  . NAG C  2 .   ? -18.272 -15.692 -6.846  1.00 48.31 ? 596  NAG A O3  1 
HETATM 9539  O  O4  . NAG C  2 .   ? -18.359 -12.945 -6.848  1.00 54.25 ? 596  NAG A O4  1 
HETATM 9540  O  O5  . NAG C  2 .   ? -16.071 -13.460 -4.023  1.00 42.48 ? 596  NAG A O5  1 
HETATM 9541  O  O6  . NAG C  2 .   ? -17.431 -11.188 -3.658  1.00 48.77 ? 596  NAG A O6  1 
HETATM 9542  O  O7  . NAG C  2 .   ? -19.302 -16.905 -5.134  1.00 60.80 ? 596  NAG A O7  1 
HETATM 9543  C  C1  . NAG D  2 .   ? -19.740 -12.913 -7.050  1.00 61.04 ? 597  NAG A C1  1 
HETATM 9544  C  C2  . NAG D  2 .   ? -19.942 -12.488 -8.500  1.00 63.24 ? 597  NAG A C2  1 
HETATM 9545  C  C3  . NAG D  2 .   ? -21.491 -12.507 -8.810  1.00 64.95 ? 597  NAG A C3  1 
HETATM 9546  C  C4  . NAG D  2 .   ? -22.299 -13.366 -7.880  1.00 66.07 ? 597  NAG A C4  1 
HETATM 9547  C  C5  . NAG D  2 .   ? -21.576 -14.342 -6.910  1.00 66.97 ? 597  NAG A C5  1 
HETATM 9548  C  C6  . NAG D  2 .   ? -21.825 -15.851 -7.099  1.00 69.21 ? 597  NAG A C6  1 
HETATM 9549  C  C7  . NAG D  2 .   ? -17.987 -11.202 -8.981  1.00 67.21 ? 597  NAG A C7  1 
HETATM 9550  C  C8  . NAG D  2 .   ? -17.308 -9.849  -9.254  1.00 67.85 ? 597  NAG A C8  1 
HETATM 9551  N  N2  . NAG D  2 .   ? -19.288 -11.236 -8.731  1.00 65.42 ? 597  NAG A N2  1 
HETATM 9552  O  O3  . NAG D  2 .   ? -21.709 -13.018 -10.106 1.00 65.19 ? 597  NAG A O3  1 
HETATM 9553  O  O4  . NAG D  2 .   ? -23.130 -12.521 -7.087  1.00 66.87 ? 597  NAG A O4  1 
HETATM 9554  O  O5  . NAG D  2 .   ? -20.187 -14.247 -6.967  1.00 62.91 ? 597  NAG A O5  1 
HETATM 9555  O  O6  . NAG D  2 .   ? -21.997 -16.456 -5.822  1.00 73.71 ? 597  NAG A O6  1 
HETATM 9556  O  O7  . NAG D  2 .   ? -17.321 -12.227 -9.054  1.00 68.94 ? 597  NAG A O7  1 
HETATM 9557  C  C1  . NAG E  2 .   ? 19.793  -0.344  -23.300 1.00 35.16 ? 598  NAG A C1  1 
HETATM 9558  C  C2  . NAG E  2 .   ? 20.340  -1.670  -22.757 1.00 37.96 ? 598  NAG A C2  1 
HETATM 9559  C  C3  . NAG E  2 .   ? 21.225  -2.390  -23.792 1.00 40.80 ? 598  NAG A C3  1 
HETATM 9560  C  C4  . NAG E  2 .   ? 20.468  -2.561  -25.117 1.00 43.76 ? 598  NAG A C4  1 
HETATM 9561  C  C5  . NAG E  2 .   ? 19.955  -1.184  -25.559 1.00 40.40 ? 598  NAG A C5  1 
HETATM 9562  C  C6  . NAG E  2 .   ? 19.146  -1.202  -26.837 1.00 39.14 ? 598  NAG A C6  1 
HETATM 9563  C  C7  . NAG E  2 .   ? 20.371  -1.355  -20.357 1.00 37.79 ? 598  NAG A C7  1 
HETATM 9564  C  C8  . NAG E  2 .   ? 21.148  -1.123  -19.073 1.00 37.53 ? 598  NAG A C8  1 
HETATM 9565  N  N2  . NAG E  2 .   ? 21.050  -1.445  -21.505 1.00 38.54 ? 598  NAG A N2  1 
HETATM 9566  O  O3  . NAG E  2 .   ? 21.584  -3.672  -23.287 1.00 44.33 ? 598  NAG A O3  1 
HETATM 9567  O  O4  . NAG E  2 .   ? 21.389  -3.088  -26.113 1.00 52.75 ? 598  NAG A O4  1 
HETATM 9568  O  O5  . NAG E  2 .   ? 19.105  -0.600  -24.538 1.00 36.51 ? 598  NAG A O5  1 
HETATM 9569  O  O6  . NAG E  2 .   ? 18.605  -2.487  -27.088 1.00 37.88 ? 598  NAG A O6  1 
HETATM 9570  O  O7  . NAG E  2 .   ? 19.142  -1.457  -20.303 1.00 38.04 ? 598  NAG A O7  1 
HETATM 9571  C  C1  . NAG F  2 .   ? 21.220  -4.378  -26.622 1.00 61.13 ? 599  NAG A C1  1 
HETATM 9572  C  C2  . NAG F  2 .   ? 22.427  -4.737  -27.518 1.00 64.51 ? 599  NAG A C2  1 
HETATM 9573  C  C3  . NAG F  2 .   ? 22.456  -6.241  -27.900 1.00 66.28 ? 599  NAG A C3  1 
HETATM 9574  C  C4  . NAG F  2 .   ? 22.198  -7.139  -26.683 1.00 66.57 ? 599  NAG A C4  1 
HETATM 9575  C  C5  . NAG F  2 .   ? 20.944  -6.653  -25.952 1.00 65.70 ? 599  NAG A C5  1 
HETATM 9576  C  C6  . NAG F  2 .   ? 20.586  -7.464  -24.719 1.00 67.67 ? 599  NAG A C6  1 
HETATM 9577  C  C7  . NAG F  2 .   ? 22.975  -2.718  -28.729 1.00 69.46 ? 599  NAG A C7  1 
HETATM 9578  C  C8  . NAG F  2 .   ? 22.899  -1.906  -30.019 1.00 70.34 ? 599  NAG A C8  1 
HETATM 9579  N  N2  . NAG F  2 .   ? 22.389  -3.915  -28.714 1.00 67.39 ? 599  NAG A N2  1 
HETATM 9580  O  O3  . NAG F  2 .   ? 23.734  -6.555  -28.448 1.00 69.23 ? 599  NAG A O3  1 
HETATM 9581  O  O4  . NAG F  2 .   ? 22.041  -8.495  -27.100 1.00 66.23 ? 599  NAG A O4  1 
HETATM 9582  O  O5  . NAG F  2 .   ? 21.141  -5.294  -25.520 1.00 61.88 ? 599  NAG A O5  1 
HETATM 9583  O  O6  . NAG F  2 .   ? 21.668  -7.535  -23.804 1.00 72.09 ? 599  NAG A O6  1 
HETATM 9584  O  O7  . NAG F  2 .   ? 23.585  -2.260  -27.760 1.00 70.49 ? 599  NAG A O7  1 
HETATM 9585  C  C1  . NAG G  2 .   ? 22.934  -17.314 2.427   1.00 31.83 ? 600  NAG A C1  1 
HETATM 9586  C  C2  . NAG G  2 .   ? 22.155  -18.446 3.076   1.00 35.11 ? 600  NAG A C2  1 
HETATM 9587  C  C3  . NAG G  2 .   ? 22.571  -19.765 2.409   1.00 37.74 ? 600  NAG A C3  1 
HETATM 9588  C  C4  . NAG G  2 .   ? 22.497  -19.696 0.872   1.00 40.26 ? 600  NAG A C4  1 
HETATM 9589  C  C5  . NAG G  2 .   ? 23.093  -18.391 0.309   1.00 37.34 ? 600  NAG A C5  1 
HETATM 9590  C  C6  . NAG G  2 .   ? 22.685  -18.172 -1.132  1.00 36.55 ? 600  NAG A C6  1 
HETATM 9591  C  C7  . NAG G  2 .   ? 21.498  -18.043 5.375   1.00 38.60 ? 600  NAG A C7  1 
HETATM 9592  C  C8  . NAG G  2 .   ? 21.846  -18.097 6.855   1.00 39.65 ? 600  NAG A C8  1 
HETATM 9593  N  N2  . NAG G  2 .   ? 22.420  -18.469 4.509   1.00 37.34 ? 600  NAG A N2  1 
HETATM 9594  O  O3  . NAG G  2 .   ? 21.701  -20.786 2.858   1.00 39.62 ? 600  NAG A O3  1 
HETATM 9595  O  O4  . NAG G  2 .   ? 23.218  -20.816 0.310   1.00 49.06 ? 600  NAG A O4  1 
HETATM 9596  O  O5  . NAG G  2 .   ? 22.614  -17.243 1.039   1.00 32.38 ? 600  NAG A O5  1 
HETATM 9597  O  O6  . NAG G  2 .   ? 23.410  -17.104 -1.710  1.00 38.31 ? 600  NAG A O6  1 
HETATM 9598  O  O7  . NAG G  2 .   ? 20.392  -17.617 5.026   1.00 39.74 ? 600  NAG A O7  1 
HETATM 9599  C  C1  . NAG H  2 .   ? 22.571  -21.597 -0.634  1.00 57.39 ? 601  NAG A C1  1 
HETATM 9600  C  C2  . NAG H  2 .   ? 23.531  -21.942 -1.783  1.00 62.44 ? 601  NAG A C2  1 
HETATM 9601  C  C3  . NAG H  2 .   ? 23.003  -23.186 -2.530  1.00 64.96 ? 601  NAG A C3  1 
HETATM 9602  C  C4  . NAG H  2 .   ? 22.951  -24.411 -1.593  1.00 66.79 ? 601  NAG A C4  1 
HETATM 9603  C  C5  . NAG H  2 .   ? 22.909  -23.979 -0.128  1.00 65.00 ? 601  NAG A C5  1 
HETATM 9604  C  C6  . NAG H  2 .   ? 24.270  -23.719 0.500   1.00 64.65 ? 601  NAG A C6  1 
HETATM 9605  C  C7  . NAG H  2 .   ? 24.820  -20.220 -2.888  1.00 68.15 ? 601  NAG A C7  1 
HETATM 9606  C  C8  . NAG H  2 .   ? 24.858  -19.017 -3.825  1.00 68.72 ? 601  NAG A C8  1 
HETATM 9607  N  N2  . NAG H  2 .   ? 23.639  -20.799 -2.675  1.00 65.74 ? 601  NAG A N2  1 
HETATM 9608  O  O3  . NAG H  2 .   ? 23.855  -23.472 -3.627  1.00 66.65 ? 601  NAG A O3  1 
HETATM 9609  O  O4  . NAG H  2 .   ? 21.776  -25.206 -1.888  1.00 72.21 ? 601  NAG A O4  1 
HETATM 9610  O  O5  . NAG H  2 .   ? 22.078  -22.788 0.036   1.00 59.95 ? 601  NAG A O5  1 
HETATM 9611  O  O6  . NAG H  2 .   ? 24.206  -23.862 1.909   1.00 67.48 ? 601  NAG A O6  1 
HETATM 9612  O  O7  . NAG H  2 .   ? 25.869  -20.628 -2.368  1.00 69.41 ? 601  NAG A O7  1 
HETATM 9613  C  C1  . MAN I  3 .   ? 21.865  -26.606 -1.867  1.00 77.48 ? 602  MAN A C1  1 
HETATM 9614  C  C2  . MAN I  3 .   ? 22.406  -27.130 -0.517  1.00 79.08 ? 602  MAN A C2  1 
HETATM 9615  C  C3  . MAN I  3 .   ? 23.181  -28.432 -0.730  1.00 80.56 ? 602  MAN A C3  1 
HETATM 9616  C  C4  . MAN I  3 .   ? 22.545  -29.243 -1.859  1.00 80.40 ? 602  MAN A C4  1 
HETATM 9617  C  C5  . MAN I  3 .   ? 22.657  -28.476 -3.182  1.00 80.45 ? 602  MAN A C5  1 
HETATM 9618  C  C6  . MAN I  3 .   ? 21.469  -28.709 -4.100  1.00 79.70 ? 602  MAN A C6  1 
HETATM 9619  O  O2  . MAN I  3 .   ? 21.314  -27.378 0.356   1.00 80.31 ? 602  MAN A O2  1 
HETATM 9620  O  O3  . MAN I  3 .   ? 23.204  -29.186 0.477   1.00 80.82 ? 602  MAN A O3  1 
HETATM 9621  O  O4  . MAN I  3 .   ? 23.172  -30.515 -1.962  1.00 82.17 ? 602  MAN A O4  1 
HETATM 9622  O  O5  . MAN I  3 .   ? 22.717  -27.039 -2.949  1.00 79.10 ? 602  MAN A O5  1 
HETATM 9623  O  O6  . MAN I  3 .   ? 21.759  -28.316 -5.431  1.00 78.70 ? 602  MAN A O6  1 
HETATM 9624  C  C1  . NAG J  2 .   ? -18.425 18.442  -8.620  1.00 44.56 ? 603  NAG A C1  1 
HETATM 9625  C  C2  . NAG J  2 .   ? -19.863 17.912  -8.493  1.00 49.42 ? 603  NAG A C2  1 
HETATM 9626  C  C3  . NAG J  2 .   ? -20.568 18.258  -7.165  1.00 52.82 ? 603  NAG A C3  1 
HETATM 9627  C  C4  . NAG J  2 .   ? -19.871 19.281  -6.206  1.00 53.21 ? 603  NAG A C4  1 
HETATM 9628  C  C5  . NAG J  2 .   ? -18.423 19.674  -6.594  1.00 51.41 ? 603  NAG A C5  1 
HETATM 9629  C  C6  . NAG J  2 .   ? -17.508 19.933  -5.395  1.00 50.89 ? 603  NAG A C6  1 
HETATM 9630  C  C7  . NAG J  2 .   ? -21.399 17.485  -10.329 1.00 60.07 ? 603  NAG A C7  1 
HETATM 9631  C  C8  . NAG J  2 .   ? -22.229 18.042  -11.477 1.00 61.93 ? 603  NAG A C8  1 
HETATM 9632  N  N2  . NAG J  2 .   ? -20.684 18.358  -9.608  1.00 56.50 ? 603  NAG A N2  1 
HETATM 9633  O  O3  . NAG J  2 .   ? -20.788 17.045  -6.466  1.00 57.33 ? 603  NAG A O3  1 
HETATM 9634  O  O4  . NAG J  2 .   ? -20.673 20.455  -6.066  1.00 54.51 ? 603  NAG A O4  1 
HETATM 9635  O  O5  . NAG J  2 .   ? -17.810 18.620  -7.342  1.00 45.87 ? 603  NAG A O5  1 
HETATM 9636  O  O6  . NAG J  2 .   ? -17.493 18.830  -4.501  1.00 53.06 ? 603  NAG A O6  1 
HETATM 9637  O  O7  . NAG J  2 .   ? -21.417 16.269  -10.103 1.00 61.30 ? 603  NAG A O7  1 
HETATM 9638  CA CA  . CA  K  4 .   ? 0.995   8.313   -8.027  1.00 2.00  ? 1001 CA  A CA  1 
HETATM 9639  C  C   . CO3 L  5 .   ? -17.241 -13.136 -0.625  1.00 26.29 ? 2001 CO3 A C   1 
HETATM 9640  O  O1  . CO3 L  5 .   ? -17.008 -12.369 0.401   1.00 26.18 ? 2001 CO3 A O1  1 
HETATM 9641  O  O2  . CO3 L  5 .   ? -16.728 -14.335 -0.678  1.00 27.38 ? 2001 CO3 A O2  1 
HETATM 9642  O  O3  . CO3 L  5 .   ? -17.989 -12.711 -1.598  1.00 24.80 ? 2001 CO3 A O3  1 
HETATM 9643  C  CHA . HEM M  6 .   ? 3.036   1.239   5.893   1.00 3.22  ? 605  HEM A CHA 1 
HETATM 9644  C  CHB . HEM M  6 .   ? 5.371   -2.907  6.160   1.00 2.15  ? 605  HEM A CHB 1 
HETATM 9645  C  CHC . HEM M  6 .   ? 1.582   -4.635  3.354   1.00 2.00  ? 605  HEM A CHC 1 
HETATM 9646  C  CHD . HEM M  6 .   ? -0.846  -0.392  3.294   1.00 2.27  ? 605  HEM A CHD 1 
HETATM 9647  C  C1A . HEM M  6 .   ? 3.987   0.300   6.236   1.00 2.00  ? 605  HEM A C1A 1 
HETATM 9648  C  C2A . HEM M  6 .   ? 5.118   0.562   7.050   1.00 2.00  ? 605  HEM A C2A 1 
HETATM 9649  C  C3A . HEM M  6 .   ? 5.841   -0.549  7.179   1.00 2.00  ? 605  HEM A C3A 1 
HETATM 9650  C  C4A . HEM M  6 .   ? 5.127   -1.564  6.414   1.00 2.00  ? 605  HEM A C4A 1 
HETATM 9651  C  CMA . HEM M  6 .   ? 7.150   -0.626  8.000   1.00 3.54  ? 605  HEM A CMA 1 
HETATM 9652  C  CAA . HEM M  6 .   ? 5.415   1.947   7.663   1.00 2.33  ? 605  HEM A CAA 1 
HETATM 9653  C  CBA . HEM M  6 .   ? 4.536   1.996   8.919   1.00 2.69  ? 605  HEM A CBA 1 
HETATM 9654  C  CGA . HEM M  6 .   ? 4.676   3.325   9.694   1.00 3.33  ? 605  HEM A CGA 1 
HETATM 9655  O  O1A . HEM M  6 .   ? 5.844   3.811   9.963   1.00 4.22  ? 605  HEM A O1A 1 
HETATM 9656  O  O2A . HEM M  6 .   ? 3.566   3.835   10.004  1.00 2.73  ? 605  HEM A O2A 1 
HETATM 9657  C  C1B . HEM M  6 .   ? 4.528   -3.747  5.360   1.00 3.03  ? 605  HEM A C1B 1 
HETATM 9658  C  C2B . HEM M  6 .   ? 4.785   -5.119  4.999   1.00 2.94  ? 605  HEM A C2B 1 
HETATM 9659  C  C3B . HEM M  6 .   ? 3.769   -5.568  4.238   1.00 3.24  ? 605  HEM A C3B 1 
HETATM 9660  C  C4B . HEM M  6 .   ? 2.779   -4.534  4.069   1.00 2.92  ? 605  HEM A C4B 1 
HETATM 9661  C  CMB . HEM M  6 .   ? 5.984   -6.014  5.372   1.00 2.00  ? 605  HEM A CMB 1 
HETATM 9662  C  CAB . HEM M  6 .   ? 3.753   -7.019  3.689   1.00 4.31  ? 605  HEM A CAB 1 
HETATM 9663  C  CBB . HEM M  6 .   ? 3.393   -7.960  4.609   1.00 4.81  ? 605  HEM A CBB 1 
HETATM 9664  C  C1C . HEM M  6 .   ? 0.560   -3.678  3.101   1.00 2.66  ? 605  HEM A C1C 1 
HETATM 9665  C  C2C . HEM M  6 .   ? -0.718  -3.838  2.335   1.00 3.14  ? 605  HEM A C2C 1 
HETATM 9666  C  C3C . HEM M  6 .   ? -1.400  -2.619  2.320   1.00 2.01  ? 605  HEM A C3C 1 
HETATM 9667  C  C4C . HEM M  6 .   ? -0.556  -1.720  3.076   1.00 2.00  ? 605  HEM A C4C 1 
HETATM 9668  C  CMC . HEM M  6 .   ? -1.224  -5.161  1.648   1.00 3.41  ? 605  HEM A CMC 1 
HETATM 9669  C  CAC . HEM M  6 .   ? -2.762  -2.185  1.685   1.00 2.00  ? 605  HEM A CAC 1 
HETATM 9670  C  CBC . HEM M  6 .   ? -3.733  -3.085  1.487   1.00 2.00  ? 605  HEM A CBC 1 
HETATM 9671  C  C1D . HEM M  6 .   ? 0.052   0.427   3.990   1.00 3.57  ? 605  HEM A C1D 1 
HETATM 9672  C  C2D . HEM M  6 .   ? -0.161  1.838   4.089   1.00 3.72  ? 605  HEM A C2D 1 
HETATM 9673  C  C3D . HEM M  6 .   ? 1.036   2.392   4.871   1.00 3.46  ? 605  HEM A C3D 1 
HETATM 9674  C  C4D . HEM M  6 .   ? 1.846   1.199   5.174   1.00 3.63  ? 605  HEM A C4D 1 
HETATM 9675  C  CMD . HEM M  6 .   ? -1.345  2.517   3.513   1.00 2.00  ? 605  HEM A CMD 1 
HETATM 9676  C  CAD . HEM M  6 .   ? 1.312   3.890   5.226   1.00 4.54  ? 605  HEM A CAD 1 
HETATM 9677  C  CBD . HEM M  6 .   ? 1.647   4.751   3.996   1.00 4.69  ? 605  HEM A CBD 1 
HETATM 9678  C  CGD . HEM M  6 .   ? 1.886   6.103   4.556   1.00 5.47  ? 605  HEM A CGD 1 
HETATM 9679  O  O1D . HEM M  6 .   ? 0.929   6.814   4.858   1.00 6.95  ? 605  HEM A O1D 1 
HETATM 9680  O  O2D . HEM M  6 .   ? 3.040   6.532   4.705   1.00 6.19  ? 605  HEM A O2D 1 
HETATM 9681  N  NA  . HEM M  6 .   ? 4.021   -0.981  5.870   1.00 2.00  ? 605  HEM A NA  1 
HETATM 9682  N  NB  . HEM M  6 .   ? 3.289   -3.444  4.757   1.00 4.21  ? 605  HEM A NB  1 
HETATM 9683  N  NC  . HEM M  6 .   ? 0.622   -2.358  3.525   1.00 3.18  ? 605  HEM A NC  1 
HETATM 9684  N  ND  . HEM M  6 .   ? 1.239   0.077   4.640   1.00 3.23  ? 605  HEM A ND  1 
HETATM 9685  FE FE  . HEM M  6 .   ? 2.169   -1.678  4.860   1.00 7.82  ? 605  HEM A FE  1 
HETATM 9686  C  C   . FMT N  7 .   ? 3.692   -23.101 -16.455 1.00 45.95 ? 3001 FMT A C   1 
HETATM 9687  O  O1  . FMT N  7 .   ? 3.438   -23.860 -17.365 1.00 46.41 ? 3001 FMT A O1  1 
HETATM 9688  O  O2  . FMT N  7 .   ? 2.755   -22.790 -15.544 1.00 45.50 ? 3001 FMT A O2  1 
HETATM 9689  C  C   . FMT O  7 .   ? -6.673  13.922  8.271   1.00 19.66 ? 3002 FMT A C   1 
HETATM 9690  O  O1  . FMT O  7 .   ? -7.368  13.663  7.320   1.00 18.10 ? 3002 FMT A O1  1 
HETATM 9691  O  O2  . FMT O  7 .   ? -7.209  14.487  9.367   1.00 21.54 ? 3002 FMT A O2  1 
HETATM 9692  C  C   . FMT P  7 .   ? 6.234   -0.742  3.283   1.00 19.81 ? 3003 FMT A C   1 
HETATM 9693  O  O1  . FMT P  7 .   ? 7.221   -0.027  3.195   1.00 20.77 ? 3003 FMT A O1  1 
HETATM 9694  O  O2  . FMT P  7 .   ? 5.007   -0.307  2.876   1.00 17.34 ? 3003 FMT A O2  1 
HETATM 9695  C  C1  . NAG Q  2 .   ? 59.444  41.589  42.332  1.00 41.12 ? 596  NAG B C1  1 
HETATM 9696  C  C2  . NAG Q  2 .   ? 60.481  42.718  42.280  1.00 44.78 ? 596  NAG B C2  1 
HETATM 9697  C  C3  . NAG Q  2 .   ? 60.592  43.433  43.648  1.00 49.98 ? 596  NAG B C3  1 
HETATM 9698  C  C4  . NAG Q  2 .   ? 59.220  43.817  44.211  1.00 52.19 ? 596  NAG B C4  1 
HETATM 9699  C  C5  . NAG Q  2 .   ? 58.315  42.585  44.198  1.00 49.90 ? 596  NAG B C5  1 
HETATM 9700  C  C6  . NAG Q  2 .   ? 56.901  42.856  44.704  1.00 50.77 ? 596  NAG B C6  1 
HETATM 9701  C  C7  . NAG Q  2 .   ? 62.494  42.719  40.934  1.00 51.03 ? 596  NAG B C7  1 
HETATM 9702  C  C8  . NAG Q  2 .   ? 63.821  42.049  40.605  1.00 51.14 ? 596  NAG B C8  1 
HETATM 9703  N  N2  . NAG Q  2 .   ? 61.765  42.155  41.895  1.00 48.90 ? 596  NAG B N2  1 
HETATM 9704  O  O3  . NAG Q  2 .   ? 61.362  44.614  43.503  1.00 51.33 ? 596  NAG B O3  1 
HETATM 9705  O  O4  . NAG Q  2 .   ? 59.380  44.294  45.566  1.00 59.26 ? 596  NAG B O4  1 
HETATM 9706  O  O5  . NAG Q  2 .   ? 58.198  42.083  42.846  1.00 44.14 ? 596  NAG B O5  1 
HETATM 9707  O  O6  . NAG Q  2 .   ? 56.457  44.159  44.348  1.00 52.79 ? 596  NAG B O6  1 
HETATM 9708  O  O7  . NAG Q  2 .   ? 62.148  43.739  40.326  1.00 52.67 ? 596  NAG B O7  1 
HETATM 9709  C  C1  . NAG R  2 .   ? 58.644  45.402  45.967  1.00 65.68 ? 597  NAG B C1  1 
HETATM 9710  C  C2  . NAG R  2 .   ? 58.536  45.394  47.497  1.00 68.54 ? 597  NAG B C2  1 
HETATM 9711  C  C3  . NAG R  2 .   ? 58.205  46.767  48.135  1.00 70.18 ? 597  NAG B C3  1 
HETATM 9712  C  C4  . NAG R  2 .   ? 58.356  48.022  47.241  1.00 70.62 ? 597  NAG B C4  1 
HETATM 9713  C  C5  . NAG R  2 .   ? 58.562  47.763  45.745  1.00 70.31 ? 597  NAG B C5  1 
HETATM 9714  C  C6  . NAG R  2 .   ? 59.320  48.913  45.098  1.00 70.58 ? 597  NAG B C6  1 
HETATM 9715  C  C7  . NAG R  2 .   ? 57.843  43.198  48.245  1.00 70.28 ? 597  NAG B C7  1 
HETATM 9716  C  C8  . NAG R  2 .   ? 56.704  42.262  48.620  1.00 70.83 ? 597  NAG B C8  1 
HETATM 9717  N  N2  . NAG R  2 .   ? 57.515  44.438  47.887  1.00 69.50 ? 597  NAG B N2  1 
HETATM 9718  O  O3  . NAG R  2 .   ? 59.034  46.943  49.274  1.00 70.99 ? 597  NAG B O3  1 
HETATM 9719  O  O4  . NAG R  2 .   ? 57.204  48.843  47.390  1.00 71.85 ? 597  NAG B O4  1 
HETATM 9720  O  O5  . NAG R  2 .   ? 59.341  46.572  45.534  1.00 67.37 ? 597  NAG B O5  1 
HETATM 9721  O  O6  . NAG R  2 .   ? 59.681  48.615  43.760  1.00 72.63 ? 597  NAG B O6  1 
HETATM 9722  O  O7  . NAG R  2 .   ? 59.007  42.798  48.297  1.00 70.25 ? 597  NAG B O7  1 
HETATM 9723  C  C1  . NAG S  2 .   ? 29.375  17.336  60.404  1.00 28.23 ? 598  NAG B C1  1 
HETATM 9724  C  C2  . NAG S  2 .   ? 30.126  16.285  59.578  1.00 31.35 ? 598  NAG B C2  1 
HETATM 9725  C  C3  . NAG S  2 .   ? 30.412  15.014  60.393  1.00 36.45 ? 598  NAG B C3  1 
HETATM 9726  C  C4  . NAG S  2 .   ? 31.066  15.341  61.735  1.00 39.17 ? 598  NAG B C4  1 
HETATM 9727  C  C5  . NAG S  2 .   ? 30.235  16.402  62.467  1.00 37.51 ? 598  NAG B C5  1 
HETATM 9728  C  C6  . NAG S  2 .   ? 30.902  16.856  63.763  1.00 37.10 ? 598  NAG B C6  1 
HETATM 9729  C  C7  . NAG S  2 .   ? 29.488  16.700  57.281  1.00 34.08 ? 598  NAG B C7  1 
HETATM 9730  C  C8  . NAG S  2 .   ? 28.649  16.334  56.064  1.00 34.19 ? 598  NAG B C8  1 
HETATM 9731  N  N2  . NAG S  2 .   ? 29.350  15.966  58.389  1.00 34.13 ? 598  NAG B N2  1 
HETATM 9732  O  O3  . NAG S  2 .   ? 31.284  14.186  59.646  1.00 34.92 ? 598  NAG B O3  1 
HETATM 9733  O  O4  . NAG S  2 .   ? 31.185  14.136  62.544  1.00 45.97 ? 598  NAG B O4  1 
HETATM 9734  O  O5  . NAG S  2 .   ? 30.071  17.582  61.640  1.00 30.96 ? 598  NAG B O5  1 
HETATM 9735  O  O6  . NAG S  2 .   ? 32.320  16.792  63.668  1.00 40.71 ? 598  NAG B O6  1 
HETATM 9736  O  O7  . NAG S  2 .   ? 30.264  17.657  57.209  1.00 33.48 ? 598  NAG B O7  1 
HETATM 9737  C  C1  . NAG T  2 .   ? 32.468  13.763  62.955  1.00 53.33 ? 599  NAG B C1  1 
HETATM 9738  C  C2  . NAG T  2 .   ? 32.400  12.779  64.155  1.00 57.23 ? 599  NAG B C2  1 
HETATM 9739  C  C3  . NAG T  2 .   ? 33.760  12.089  64.456  1.00 58.96 ? 599  NAG B C3  1 
HETATM 9740  C  C4  . NAG T  2 .   ? 34.571  11.739  63.202  1.00 59.00 ? 599  NAG B C4  1 
HETATM 9741  C  C5  . NAG T  2 .   ? 34.517  12.861  62.160  1.00 58.76 ? 599  NAG B C5  1 
HETATM 9742  C  C6  . NAG T  2 .   ? 35.218  12.489  60.857  1.00 59.32 ? 599  NAG B C6  1 
HETATM 9743  C  C7  . NAG T  2 .   ? 30.876  13.242  65.983  1.00 60.04 ? 599  NAG B C7  1 
HETATM 9744  C  C8  . NAG T  2 .   ? 30.584  14.079  67.216  1.00 60.73 ? 599  NAG B C8  1 
HETATM 9745  N  N2  . NAG T  2 .   ? 32.006  13.523  65.339  1.00 58.67 ? 599  NAG B N2  1 
HETATM 9746  O  O3  . NAG T  2 .   ? 33.540  10.890  65.197  1.00 59.63 ? 599  NAG B O3  1 
HETATM 9747  O  O4  . NAG T  2 .   ? 35.931  11.507  63.569  1.00 60.29 ? 599  NAG B O4  1 
HETATM 9748  O  O5  . NAG T  2 .   ? 33.146  13.170  61.845  1.00 55.37 ? 599  NAG B O5  1 
HETATM 9749  O  O6  . NAG T  2 .   ? 34.294  12.193  59.822  1.00 61.39 ? 599  NAG B O6  1 
HETATM 9750  O  O7  . NAG T  2 .   ? 30.079  12.378  65.620  1.00 60.47 ? 599  NAG B O7  1 
HETATM 9751  C  C1  . NAG U  2 .   ? 42.406  6.587   35.399  1.00 28.12 ? 600  NAG B C1  1 
HETATM 9752  C  C2  . NAG U  2 .   ? 43.818  6.657   34.825  1.00 30.46 ? 600  NAG B C2  1 
HETATM 9753  C  C3  . NAG U  2 .   ? 44.794  5.814   35.614  1.00 34.98 ? 600  NAG B C3  1 
HETATM 9754  C  C4  . NAG U  2 .   ? 44.656  5.964   37.117  1.00 38.28 ? 600  NAG B C4  1 
HETATM 9755  C  C5  . NAG U  2 .   ? 43.158  6.085   37.580  1.00 36.44 ? 600  NAG B C5  1 
HETATM 9756  C  C6  . NAG U  2 .   ? 42.915  6.525   39.020  1.00 36.63 ? 600  NAG B C6  1 
HETATM 9757  C  C7  . NAG U  2 .   ? 43.682  7.097   32.471  1.00 37.23 ? 600  NAG B C7  1 
HETATM 9758  C  C8  . NAG U  2 .   ? 43.691  6.618   31.027  1.00 39.15 ? 600  NAG B C8  1 
HETATM 9759  N  N2  . NAG U  2 .   ? 43.821  6.205   33.448  1.00 36.42 ? 600  NAG B N2  1 
HETATM 9760  O  O3  . NAG U  2 .   ? 46.107  6.211   35.253  1.00 32.52 ? 600  NAG B O3  1 
HETATM 9761  O  O4  . NAG U  2 .   ? 45.234  4.763   37.661  1.00 46.07 ? 600  NAG B O4  1 
HETATM 9762  O  O5  . NAG U  2 .   ? 42.441  7.017   36.749  1.00 30.88 ? 600  NAG B O5  1 
HETATM 9763  O  O6  . NAG U  2 .   ? 41.824  5.807   39.583  1.00 36.87 ? 600  NAG B O6  1 
HETATM 9764  O  O7  . NAG U  2 .   ? 43.576  8.304   32.700  1.00 38.18 ? 600  NAG B O7  1 
HETATM 9765  C  C1  . NAG V  2 .   ? 46.436  4.750   38.368  1.00 54.84 ? 601  NAG B C1  1 
HETATM 9766  C  C2  . NAG V  2 .   ? 46.666  3.318   38.770  1.00 59.00 ? 601  NAG B C2  1 
HETATM 9767  C  C3  . NAG V  2 .   ? 47.951  3.104   39.548  1.00 61.95 ? 601  NAG B C3  1 
HETATM 9768  C  C4  . NAG V  2 .   ? 49.114  3.767   38.829  1.00 64.56 ? 601  NAG B C4  1 
HETATM 9769  C  C5  . NAG V  2 .   ? 48.696  4.414   37.469  1.00 62.24 ? 601  NAG B C5  1 
HETATM 9770  C  C6  . NAG V  2 .   ? 48.490  3.532   36.240  1.00 61.89 ? 601  NAG B C6  1 
HETATM 9771  C  C7  . NAG V  2 .   ? 44.554  2.275   38.850  1.00 61.89 ? 601  NAG B C7  1 
HETATM 9772  C  C8  . NAG V  2 .   ? 43.345  1.823   39.640  1.00 61.22 ? 601  NAG B C8  1 
HETATM 9773  N  N2  . NAG V  2 .   ? 45.514  2.885   39.526  1.00 60.52 ? 601  NAG B N2  1 
HETATM 9774  O  O3  . NAG V  2 .   ? 48.204  1.718   39.674  1.00 62.34 ? 601  NAG B O3  1 
HETATM 9775  O  O4  . NAG V  2 .   ? 49.685  4.770   39.706  1.00 70.57 ? 601  NAG B O4  1 
HETATM 9776  O  O5  . NAG V  2 .   ? 47.521  5.272   37.574  1.00 57.86 ? 601  NAG B O5  1 
HETATM 9777  O  O6  . NAG V  2 .   ? 49.446  3.837   35.224  1.00 62.80 ? 601  NAG B O6  1 
HETATM 9778  O  O7  . NAG V  2 .   ? 44.635  2.060   37.627  1.00 62.32 ? 601  NAG B O7  1 
HETATM 9779  C  C1  . MAN W  3 .   ? 51.135  4.974   39.764  1.00 76.06 ? 602  MAN B C1  1 
HETATM 9780  C  C2  . MAN W  3 .   ? 51.183  5.695   41.131  1.00 78.51 ? 602  MAN B C2  1 
HETATM 9781  C  C3  . MAN W  3 .   ? 52.347  6.668   41.267  1.00 80.52 ? 602  MAN B C3  1 
HETATM 9782  C  C4  . MAN W  3 .   ? 53.535  6.240   40.448  1.00 80.82 ? 602  MAN B C4  1 
HETATM 9783  C  C5  . MAN W  3 .   ? 53.174  6.227   38.981  1.00 80.01 ? 602  MAN B C5  1 
HETATM 9784  C  C6  . MAN W  3 .   ? 54.164  5.482   38.104  1.00 79.57 ? 602  MAN B C6  1 
HETATM 9785  O  O2  . MAN W  3 .   ? 51.211  4.740   42.190  1.00 79.33 ? 602  MAN B O2  1 
HETATM 9786  O  O3  . MAN W  3 .   ? 52.725  6.798   42.633  1.00 82.10 ? 602  MAN B O3  1 
HETATM 9787  O  O4  . MAN W  3 .   ? 54.580  7.185   40.633  1.00 83.16 ? 602  MAN B O4  1 
HETATM 9788  O  O5  . MAN W  3 .   ? 51.837  5.699   38.712  1.00 77.72 ? 602  MAN B O5  1 
HETATM 9789  O  O6  . MAN W  3 .   ? 53.906  5.735   36.729  1.00 79.19 ? 602  MAN B O6  1 
HETATM 9790  C  C1  . NAG X  2 .   ? 31.316  60.168  47.568  1.00 49.84 ? 603  NAG B C1  1 
HETATM 9791  C  C2  . NAG X  2 .   ? 32.727  60.691  47.275  1.00 56.66 ? 603  NAG B C2  1 
HETATM 9792  C  C3  . NAG X  2 .   ? 32.808  62.229  47.093  1.00 60.84 ? 603  NAG B C3  1 
HETATM 9793  C  C4  . NAG X  2 .   ? 31.592  63.080  47.612  1.00 61.77 ? 603  NAG B C4  1 
HETATM 9794  C  C5  . NAG X  2 .   ? 30.302  62.270  47.837  1.00 61.00 ? 603  NAG B C5  1 
HETATM 9795  C  C6  . NAG X  2 .   ? 29.002  63.011  47.530  1.00 62.03 ? 603  NAG B C6  1 
HETATM 9796  C  C7  . NAG X  2 .   ? 34.463  59.293  48.224  1.00 63.27 ? 603  NAG B C7  1 
HETATM 9797  C  C8  . NAG X  2 .   ? 35.280  58.949  49.455  1.00 64.66 ? 603  NAG B C8  1 
HETATM 9798  N  N2  . NAG X  2 .   ? 33.592  60.289  48.367  1.00 61.37 ? 603  NAG B N2  1 
HETATM 9799  O  O3  . NAG X  2 .   ? 32.993  62.517  45.715  1.00 61.58 ? 603  NAG B O3  1 
HETATM 9800  O  O4  . NAG X  2 .   ? 31.943  63.753  48.812  1.00 63.01 ? 603  NAG B O4  1 
HETATM 9801  O  O5  . NAG X  2 .   ? 30.322  61.054  47.065  1.00 56.27 ? 603  NAG B O5  1 
HETATM 9802  O  O6  . NAG X  2 .   ? 29.087  63.817  46.365  1.00 62.20 ? 603  NAG B O6  1 
HETATM 9803  O  O7  . NAG X  2 .   ? 34.642  58.683  47.163  1.00 65.10 ? 603  NAG B O7  1 
HETATM 9804  CA CA  . CA  Y  4 .   ? 30.698  38.166  45.265  1.00 2.00  ? 1002 CA  B CA  1 
HETATM 9805  C  C   . CO3 Z  5 .   ? 58.743  43.852  38.510  1.00 36.42 ? 2002 CO3 B C   1 
HETATM 9806  O  O1  . CO3 Z  5 .   ? 58.875  43.166  37.409  1.00 36.73 ? 2002 CO3 B O1  1 
HETATM 9807  O  O2  . CO3 Z  5 .   ? 57.782  43.567  39.350  1.00 36.01 ? 2002 CO3 B O2  1 
HETATM 9808  O  O3  . CO3 Z  5 .   ? 59.568  44.823  38.775  1.00 35.44 ? 2002 CO3 B O3  1 
HETATM 9809  C  CHA . HEM AA 6 .   ? 35.663  32.579  31.639  1.00 11.34 ? 605  HEM B CHA 1 
HETATM 9810  C  CHB . HEM AA 6 .   ? 38.387  28.675  31.328  1.00 12.22 ? 605  HEM B CHB 1 
HETATM 9811  C  CHC . HEM AA 6 .   ? 41.570  31.424  34.100  1.00 12.55 ? 605  HEM B CHC 1 
HETATM 9812  C  CHD . HEM AA 6 .   ? 38.801  35.424  34.212  1.00 11.51 ? 605  HEM B CHD 1 
HETATM 9813  C  C1A . HEM AA 6 .   ? 36.086  31.323  31.298  1.00 10.11 ? 605  HEM B C1A 1 
HETATM 9814  C  C2A . HEM AA 6 .   ? 35.336  30.427  30.494  1.00 9.55  ? 605  HEM B C2A 1 
HETATM 9815  C  C3A . HEM AA 6 .   ? 36.027  29.285  30.346  1.00 9.99  ? 605  HEM B C3A 1 
HETATM 9816  C  C4A . HEM AA 6 .   ? 37.265  29.482  31.102  1.00 11.09 ? 605  HEM B C4A 1 
HETATM 9817  C  CMA . HEM AA 6 .   ? 35.510  28.081  29.538  1.00 11.24 ? 605  HEM B CMA 1 
HETATM 9818  C  CAA . HEM AA 6 .   ? 33.932  30.778  29.910  1.00 9.82  ? 605  HEM B CAA 1 
HETATM 9819  C  CBA . HEM AA 6 .   ? 34.176  31.698  28.695  1.00 7.76  ? 605  HEM B CBA 1 
HETATM 9820  C  CGA . HEM AA 6 .   ? 32.850  32.156  28.017  1.00 6.39  ? 605  HEM B CGA 1 
HETATM 9821  O  O1A . HEM AA 6 .   ? 32.024  31.297  27.539  1.00 2.47  ? 605  HEM B O1A 1 
HETATM 9822  O  O2A . HEM AA 6 .   ? 32.693  33.406  28.012  1.00 6.58  ? 605  HEM B O2A 1 
HETATM 9823  C  C1B . HEM AA 6 .   ? 39.511  29.096  32.112  1.00 12.38 ? 605  HEM B C1B 1 
HETATM 9824  C  C2B . HEM AA 6 .   ? 40.681  28.320  32.402  1.00 12.70 ? 605  HEM B C2B 1 
HETATM 9825  C  C3B . HEM AA 6 .   ? 41.521  29.061  33.171  1.00 13.74 ? 605  HEM B C3B 1 
HETATM 9826  C  C4B . HEM AA 6 .   ? 40.965  30.373  33.388  1.00 13.32 ? 605  HEM B C4B 1 
HETATM 9827  C  CMB . HEM AA 6 .   ? 41.001  26.874  31.966  1.00 10.62 ? 605  HEM B CMB 1 
HETATM 9828  C  CAB . HEM AA 6 .   ? 42.895  28.520  33.682  1.00 13.80 ? 605  HEM B CAB 1 
HETATM 9829  C  CBB . HEM AA 6 .   ? 43.803  28.138  32.739  1.00 14.97 ? 605  HEM B CBB 1 
HETATM 9830  C  C1C . HEM AA 6 .   ? 41.152  32.753  34.381  1.00 11.45 ? 605  HEM B C1C 1 
HETATM 9831  C  C2C . HEM AA 6 .   ? 41.872  33.847  35.120  1.00 11.02 ? 605  HEM B C2C 1 
HETATM 9832  C  C3C . HEM AA 6 .   ? 41.076  34.981  35.153  1.00 11.49 ? 605  HEM B C3C 1 
HETATM 9833  C  C4C . HEM AA 6 .   ? 39.878  34.601  34.429  1.00 12.20 ? 605  HEM B C4C 1 
HETATM 9834  C  CMC . HEM AA 6 .   ? 43.290  33.734  35.775  1.00 7.62  ? 605  HEM B CMC 1 
HETATM 9835  C  CAC . HEM AA 6 .   ? 41.283  36.411  35.782  1.00 11.73 ? 605  HEM B CAC 1 
HETATM 9836  C  CBC . HEM AA 6 .   ? 42.301  36.647  36.630  1.00 13.33 ? 605  HEM B CBC 1 
HETATM 9837  C  C1D . HEM AA 6 .   ? 37.680  34.928  33.548  1.00 11.59 ? 605  HEM B C1D 1 
HETATM 9838  C  C2D . HEM AA 6 .   ? 36.452  35.660  33.533  1.00 12.72 ? 605  HEM B C2D 1 
HETATM 9839  C  C3D . HEM AA 6 .   ? 35.442  34.799  32.769  1.00 14.14 ? 605  HEM B C3D 1 
HETATM 9840  C  C4D . HEM AA 6 .   ? 36.215  33.617  32.369  1.00 13.01 ? 605  HEM B C4D 1 
HETATM 9841  C  CMD . HEM AA 6 .   ? 36.272  36.987  34.174  1.00 12.54 ? 605  HEM B CMD 1 
HETATM 9842  C  CAD . HEM AA 6 .   ? 33.927  35.158  32.512  1.00 14.05 ? 605  HEM B CAD 1 
HETATM 9843  C  CBD . HEM AA 6 .   ? 33.110  35.270  33.814  1.00 13.47 ? 605  HEM B CBD 1 
HETATM 9844  C  CGD . HEM AA 6 .   ? 31.736  35.619  33.383  1.00 15.49 ? 605  HEM B CGD 1 
HETATM 9845  O  O1D . HEM AA 6 .   ? 31.483  36.778  33.019  1.00 17.08 ? 605  HEM B O1D 1 
HETATM 9846  O  O2D . HEM AA 6 .   ? 30.833  34.771  33.420  1.00 17.01 ? 605  HEM B O2D 1 
HETATM 9847  N  NA  . HEM AA 6 .   ? 37.234  30.738  31.642  1.00 10.63 ? 605  HEM B NA  1 
HETATM 9848  N  NB  . HEM AA 6 .   ? 39.740  30.344  32.735  1.00 13.66 ? 605  HEM B NB  1 
HETATM 9849  N  NC  . HEM AA 6 .   ? 39.937  33.273  33.972  1.00 13.14 ? 605  HEM B NC  1 
HETATM 9850  N  ND  . HEM AA 6 .   ? 37.520  33.725  32.846  1.00 12.31 ? 605  HEM B ND  1 
HETATM 9851  FE FE  . HEM AA 6 .   ? 38.695  32.084  32.605  1.00 12.52 ? 605  HEM B FE  1 
HETATM 9852  C  C   . FMT BA 7 .   ? 57.389  20.467  53.419  1.00 36.99 ? 3004 FMT B C   1 
HETATM 9853  O  O1  . FMT BA 7 .   ? 57.037  20.775  54.536  1.00 37.54 ? 3004 FMT B O1  1 
HETATM 9854  O  O2  . FMT BA 7 .   ? 58.177  21.287  52.697  1.00 36.10 ? 3004 FMT B O2  1 
HETATM 9855  C  C   . FMT CA 7 .   ? 30.104  48.346  29.428  1.00 4.84  ? 3005 FMT B C   1 
HETATM 9856  O  O1  . FMT CA 7 .   ? 29.211  48.508  28.629  1.00 5.53  ? 3005 FMT B O1  1 
HETATM 9857  O  O2  . FMT CA 7 .   ? 30.125  47.246  30.187  1.00 3.97  ? 3005 FMT B O2  1 
HETATM 9858  C  C   . FMT DA 7 .   ? 36.234  29.257  34.063  1.00 19.19 ? 3006 FMT B C   1 
HETATM 9859  O  O1  . FMT DA 7 .   ? 36.585  30.164  34.791  1.00 18.73 ? 3006 FMT B O1  1 
HETATM 9860  O  O2  . FMT DA 7 .   ? 34.924  28.975  33.883  1.00 19.97 ? 3006 FMT B O2  1 
HETATM 9861  O  O   . HOH EA 8 .   ? 13.265  3.671   5.299   1.00 21.85 ? 3004 HOH A O   1 
HETATM 9862  O  O   . HOH EA 8 .   ? 11.453  6.608   5.380   1.00 12.24 ? 3005 HOH A O   1 
HETATM 9863  O  O   . HOH EA 8 .   ? -0.585  -6.332  -21.554 1.00 24.14 ? 3006 HOH A O   1 
HETATM 9864  O  O   . HOH EA 8 .   ? 12.168  -17.863 -12.658 1.00 5.02  ? 3007 HOH A O   1 
HETATM 9865  O  O   . HOH EA 8 .   ? 12.470  -18.719 -22.997 1.00 15.42 ? 3008 HOH A O   1 
HETATM 9866  O  O   . HOH EA 8 .   ? -16.667 1.968   -34.226 1.00 15.32 ? 3009 HOH A O   1 
HETATM 9867  O  O   . HOH EA 8 .   ? -17.981 -0.955  -35.260 1.00 17.24 ? 3010 HOH A O   1 
HETATM 9868  O  O   . HOH EA 8 .   ? 23.164  11.825  21.111  1.00 14.49 ? 3011 HOH A O   1 
HETATM 9869  O  O   . HOH EA 8 .   ? -7.605  21.010  16.725  1.00 2.00  ? 3012 HOH A O   1 
HETATM 9870  O  O   . HOH EA 8 .   ? -6.806  5.372   -37.072 1.00 2.89  ? 3013 HOH A O   1 
HETATM 9871  O  O   . HOH EA 8 .   ? -10.514 -8.014  -18.552 1.00 2.00  ? 3014 HOH A O   1 
HETATM 9872  O  O   . HOH EA 8 .   ? -9.433  -11.142 3.704   1.00 2.00  ? 3015 HOH A O   1 
HETATM 9873  O  O   . HOH EA 8 .   ? -13.842 22.170  -16.058 1.00 2.88  ? 3016 HOH A O   1 
HETATM 9874  O  O   . HOH EA 8 .   ? 2.546   -2.432  31.802  1.00 7.03  ? 3017 HOH A O   1 
HETATM 9875  O  O   . HOH EA 8 .   ? 14.677  -11.494 6.150   1.00 2.00  ? 3018 HOH A O   1 
HETATM 9876  O  O   . HOH EA 8 .   ? -9.233  -6.439  5.773   1.00 2.00  ? 3019 HOH A O   1 
HETATM 9877  O  O   . HOH EA 8 .   ? 10.119  17.153  15.723  1.00 10.55 ? 3020 HOH A O   1 
HETATM 9878  O  O   . HOH EA 8 .   ? 6.697   21.631  14.361  1.00 22.31 ? 3021 HOH A O   1 
HETATM 9879  O  O   . HOH EA 8 .   ? 24.177  -12.984 7.247   1.00 2.00  ? 3022 HOH A O   1 
HETATM 9880  O  O   . HOH EA 8 .   ? 19.371  -0.830  -29.612 1.00 18.66 ? 3023 HOH A O   1 
HETATM 9881  O  O   . HOH EA 8 .   ? 23.639  14.381  24.992  1.00 6.68  ? 3024 HOH A O   1 
HETATM 9882  O  O   . HOH EA 8 .   ? 17.296  12.716  -4.480  1.00 18.17 ? 3025 HOH A O   1 
HETATM 9883  O  O   . HOH EA 8 .   ? -1.848  -10.672 9.545   1.00 4.56  ? 3026 HOH A O   1 
HETATM 9884  O  O   . HOH EA 8 .   ? -7.419  -21.539 -26.141 1.00 5.34  ? 3027 HOH A O   1 
HETATM 9885  O  O   . HOH EA 8 .   ? 6.191   14.524  12.857  1.00 3.69  ? 3028 HOH A O   1 
HETATM 9886  O  O   . HOH EA 8 .   ? 4.823   16.710  -20.088 1.00 7.36  ? 3029 HOH A O   1 
HETATM 9887  O  O   . HOH EA 8 .   ? 10.078  13.699  -20.319 1.00 13.87 ? 3030 HOH A O   1 
HETATM 9888  O  O   . HOH EA 8 .   ? -3.527  -6.985  -19.932 1.00 2.00  ? 3031 HOH A O   1 
HETATM 9889  O  O   . HOH EA 8 .   ? -9.277  5.447   -35.880 1.00 12.85 ? 3032 HOH A O   1 
HETATM 9890  O  O   . HOH EA 8 .   ? 1.969   -17.976 -0.066  1.00 17.38 ? 3033 HOH A O   1 
HETATM 9891  O  O   . HOH EA 8 .   ? -0.138  29.865  0.036   1.00 3.57  ? 3034 HOH A O   1 
HETATM 9892  O  O   . HOH EA 8 .   ? -9.958  -21.441 14.277  1.00 7.80  ? 3035 HOH A O   1 
HETATM 9893  O  O   . HOH EA 8 .   ? 17.769  7.803   8.228   1.00 31.02 ? 3036 HOH A O   1 
HETATM 9894  O  O   . HOH EA 8 .   ? -24.848 8.220   -3.165  1.00 9.80  ? 3037 HOH A O   1 
HETATM 9895  O  O   . HOH EA 8 .   ? 20.329  5.420   -2.765  1.00 2.00  ? 3038 HOH A O   1 
HETATM 9896  O  O   . HOH EA 8 .   ? 22.567  -11.513 9.797   1.00 2.04  ? 3039 HOH A O   1 
HETATM 9897  O  O   . HOH EA 8 .   ? 5.160   4.077   24.042  1.00 4.17  ? 3040 HOH A O   1 
HETATM 9898  O  O   . HOH EA 8 .   ? 0.132   -19.656 5.579   1.00 30.24 ? 3041 HOH A O   1 
HETATM 9899  O  O   . HOH EA 8 .   ? -1.117  20.792  -17.810 1.00 2.00  ? 3042 HOH A O   1 
HETATM 9900  O  O   . HOH EA 8 .   ? -1.086  -6.323  -26.000 1.00 51.52 ? 3043 HOH A O   1 
HETATM 9901  O  O   . HOH EA 8 .   ? -5.789  22.788  14.765  1.00 14.46 ? 3044 HOH A O   1 
HETATM 9902  O  O   . HOH EA 8 .   ? 20.340  5.223   -0.113  1.00 8.05  ? 3045 HOH A O   1 
HETATM 9903  O  O   . HOH EA 8 .   ? -9.746  -9.172  5.467   1.00 4.70  ? 3046 HOH A O   1 
HETATM 9904  O  O   . HOH EA 8 .   ? -10.602 17.250  14.689  1.00 2.00  ? 3047 HOH A O   1 
HETATM 9905  O  O   . HOH EA 8 .   ? 8.786   17.707  18.528  1.00 29.98 ? 3048 HOH A O   1 
HETATM 9906  O  O   . HOH EA 8 .   ? 12.260  -1.270  32.392  1.00 14.00 ? 3049 HOH A O   1 
HETATM 9907  O  O   . HOH EA 8 .   ? -20.049 3.391   4.788   1.00 25.07 ? 3050 HOH A O   1 
HETATM 9908  O  O   . HOH EA 8 .   ? -17.660 4.898   -33.487 1.00 35.90 ? 3051 HOH A O   1 
HETATM 9909  O  O   . HOH EA 8 .   ? -26.419 -3.113  -3.650  1.00 50.74 ? 3052 HOH A O   1 
HETATM 9910  O  O   . HOH EA 8 .   ? -23.474 15.280  -6.191  1.00 45.85 ? 3053 HOH A O   1 
HETATM 9911  O  O   . HOH EA 8 .   ? -19.336 15.105  -5.708  1.00 45.18 ? 3054 HOH A O   1 
HETATM 9912  O  O   . HOH EA 8 .   ? 0.691   -10.533 -25.982 1.00 56.08 ? 3055 HOH A O   1 
HETATM 9913  O  O   . HOH EA 8 .   ? -16.907 -9.614  10.574  1.00 33.56 ? 3056 HOH A O   1 
HETATM 9914  O  O   . HOH EA 8 .   ? -13.626 -11.342 -8.373  1.00 32.65 ? 3057 HOH A O   1 
HETATM 9915  O  O   . HOH EA 8 .   ? -12.541 -4.537  9.184   1.00 16.87 ? 3058 HOH A O   1 
HETATM 9916  O  O   . HOH EA 8 .   ? 10.785  7.353   -15.365 1.00 19.71 ? 3059 HOH A O   1 
HETATM 9917  O  O   . HOH EA 8 .   ? 11.622  -11.767 0.389   1.00 23.72 ? 3060 HOH A O   1 
HETATM 9918  O  O   . HOH EA 8 .   ? 2.723   9.242   -19.509 1.00 20.21 ? 3061 HOH A O   1 
HETATM 9919  O  O   . HOH EA 8 .   ? -5.971  -9.709  16.980  1.00 19.60 ? 3062 HOH A O   1 
HETATM 9920  O  O   . HOH EA 8 .   ? 17.196  -8.306  -16.052 1.00 22.03 ? 3063 HOH A O   1 
HETATM 9921  O  O   . HOH EA 8 .   ? -5.696  9.459   -9.888  1.00 14.35 ? 3064 HOH A O   1 
HETATM 9922  O  O   . HOH EA 8 .   ? 4.659   -17.823 -21.920 1.00 24.65 ? 3065 HOH A O   1 
HETATM 9923  O  O   . HOH EA 8 .   ? 5.027   6.096   -6.046  1.00 6.39  ? 3066 HOH A O   1 
HETATM 9924  O  O   . HOH EA 8 .   ? 3.074   -17.870 -2.372  1.00 13.72 ? 3067 HOH A O   1 
HETATM 9925  O  O   . HOH EA 8 .   ? 4.816   31.192  -16.784 1.00 22.86 ? 3068 HOH A O   1 
HETATM 9926  O  O   . HOH EA 8 .   ? -8.307  24.201  11.025  1.00 25.33 ? 3069 HOH A O   1 
HETATM 9927  O  O   . HOH EA 8 .   ? 3.611   8.199   -13.552 1.00 12.03 ? 3070 HOH A O   1 
HETATM 9928  O  O   . HOH EA 8 .   ? 16.264  5.532   29.629  1.00 40.52 ? 3071 HOH A O   1 
HETATM 9929  O  O   . HOH EA 8 .   ? 13.920  11.009  -17.886 1.00 33.06 ? 3072 HOH A O   1 
HETATM 9930  O  O   . HOH EA 8 .   ? 15.375  7.550   9.998   1.00 41.68 ? 3073 HOH A O   1 
HETATM 9931  O  O   . HOH EA 8 .   ? -0.741  8.069   -16.605 1.00 22.34 ? 3074 HOH A O   1 
HETATM 9932  O  O   . HOH EA 8 .   ? -1.324  26.066  -6.370  1.00 52.53 ? 3075 HOH A O   1 
HETATM 9933  O  O   . HOH EA 8 .   ? 9.265   13.240  -4.914  1.00 34.39 ? 3076 HOH A O   1 
HETATM 9934  O  O   . HOH EA 8 .   ? -6.425  22.333  8.877   1.00 23.69 ? 3077 HOH A O   1 
HETATM 9935  O  O   . HOH EA 8 .   ? 2.787   3.250   -39.196 1.00 35.11 ? 3078 HOH A O   1 
HETATM 9936  O  O   . HOH EA 8 .   ? -10.276 -18.815 -13.832 1.00 36.98 ? 3079 HOH A O   1 
HETATM 9937  O  O   . HOH EA 8 .   ? 25.869  11.726  21.314  1.00 50.36 ? 3080 HOH A O   1 
HETATM 9938  O  O   . HOH EA 8 .   ? 6.457   -9.412  37.623  1.00 32.35 ? 3081 HOH A O   1 
HETATM 9939  O  O   . HOH EA 8 .   ? -4.947  13.083  -26.473 1.00 37.28 ? 3082 HOH A O   1 
HETATM 9940  O  O   . HOH EA 8 .   ? -14.289 -20.912 -1.843  1.00 51.37 ? 3083 HOH A O   1 
HETATM 9941  O  O   . HOH EA 8 .   ? -4.897  20.970  11.608  1.00 43.71 ? 3084 HOH A O   1 
HETATM 9942  O  O   . HOH EA 8 .   ? -2.728  12.036  -28.108 1.00 32.46 ? 3085 HOH A O   1 
HETATM 9943  O  O   . HOH EA 8 .   ? 2.125   -16.823 13.550  1.00 29.07 ? 3086 HOH A O   1 
HETATM 9944  O  O   . HOH EA 8 .   ? 0.789   -0.998  30.901  1.00 60.49 ? 3087 HOH A O   1 
HETATM 9945  O  O   . HOH EA 8 .   ? 2.368   0.074   -40.053 1.00 52.79 ? 3088 HOH A O   1 
HETATM 9946  O  O   . HOH EA 8 .   ? -8.841  -22.613 5.657   1.00 37.86 ? 3089 HOH A O   1 
HETATM 9947  O  O   . HOH FA 8 .   ? 32.479  31.041  32.974  1.00 21.85 ? 3007 HOH B O   1 
HETATM 9948  O  O   . HOH FA 8 .   ? 26.704  28.196  32.253  1.00 30.67 ? 3008 HOH B O   1 
HETATM 9949  O  O   . HOH FA 8 .   ? 26.963  25.680  35.842  1.00 20.46 ? 3009 HOH B O   1 
HETATM 9950  O  O   . HOH FA 8 .   ? 22.490  49.086  33.523  1.00 2.00  ? 3010 HOH B O   1 
HETATM 9951  O  O   . HOH FA 8 .   ? 52.015  23.776  60.438  1.00 2.00  ? 3011 HOH B O   1 
HETATM 9952  O  O   . HOH FA 8 .   ? 29.208  15.491  21.220  1.00 2.00  ? 3012 HOH B O   1 
HETATM 9953  O  O   . HOH FA 8 .   ? 19.962  35.381  19.574  1.00 2.00  ? 3013 HOH B O   1 
HETATM 9954  O  O   . HOH FA 8 .   ? 32.071  19.186  58.568  1.00 11.05 ? 3014 HOH B O   1 
HETATM 9955  O  O   . HOH FA 8 .   ? 27.596  26.220  41.837  1.00 17.61 ? 3015 HOH B O   1 
HETATM 9956  O  O   . HOH FA 8 .   ? 59.892  55.445  38.411  1.00 2.07  ? 3016 HOH B O   1 
HETATM 9957  O  O   . HOH FA 8 .   ? 33.888  2.857   35.469  1.00 28.08 ? 3017 HOH B O   1 
HETATM 9958  O  O   . HOH FA 8 .   ? 37.758  55.660  10.848  1.00 2.00  ? 3018 HOH B O   1 
HETATM 9959  O  O   . HOH FA 8 .   ? 13.955  49.982  22.895  1.00 18.87 ? 3019 HOH B O   1 
HETATM 9960  O  O   . HOH FA 8 .   ? 31.961  35.543  78.538  1.00 2.00  ? 3020 HOH B O   1 
HETATM 9961  O  O   . HOH FA 8 .   ? 48.214  31.249  28.242  1.00 7.68  ? 3021 HOH B O   1 
HETATM 9962  O  O   . HOH FA 8 .   ? 7.271   38.167  41.467  1.00 2.00  ? 3022 HOH B O   1 
HETATM 9963  O  O   . HOH FA 8 .   ? 33.477  21.547  17.408  1.00 2.00  ? 3023 HOH B O   1 
HETATM 9964  O  O   . HOH FA 8 .   ? 33.786  19.084  60.714  1.00 2.70  ? 3024 HOH B O   1 
HETATM 9965  O  O   . HOH FA 8 .   ? 44.535  32.558  58.685  1.00 26.58 ? 3025 HOH B O   1 
HETATM 9966  O  O   . HOH FA 8 .   ? 10.313  37.647  43.017  1.00 13.00 ? 3026 HOH B O   1 
HETATM 9967  O  O   . HOH FA 8 .   ? 31.931  28.731  27.871  1.00 2.00  ? 3027 HOH B O   1 
HETATM 9968  O  O   . HOH FA 8 .   ? 22.193  30.090  54.675  1.00 14.55 ? 3028 HOH B O   1 
HETATM 9969  O  O   . HOH FA 8 .   ? 32.151  36.966  10.231  1.00 4.30  ? 3029 HOH B O   1 
HETATM 9970  O  O   . HOH FA 8 .   ? 20.699  35.176  53.627  1.00 24.28 ? 3030 HOH B O   1 
HETATM 9971  O  O   . HOH FA 8 .   ? 22.049  50.744  21.076  1.00 11.20 ? 3031 HOH B O   1 
HETATM 9972  O  O   . HOH FA 8 .   ? 28.675  29.701  30.755  1.00 12.53 ? 3032 HOH B O   1 
HETATM 9973  O  O   . HOH FA 8 .   ? 54.613  33.950  17.656  1.00 3.79  ? 3033 HOH B O   1 
HETATM 9974  O  O   . HOH FA 8 .   ? 58.629  57.793  37.913  1.00 10.81 ? 3034 HOH B O   1 
HETATM 9975  O  O   . HOH FA 8 .   ? 56.202  58.696  36.376  1.00 20.93 ? 3035 HOH B O   1 
HETATM 9976  O  O   . HOH FA 8 .   ? 19.024  26.704  57.142  1.00 15.58 ? 3036 HOH B O   1 
HETATM 9977  O  O   . HOH FA 8 .   ? 34.243  16.830  59.293  1.00 9.50  ? 3037 HOH B O   1 
HETATM 9978  O  O   . HOH FA 8 .   ? 14.770  44.330  32.580  1.00 13.29 ? 3038 HOH B O   1 
HETATM 9979  O  O   . HOH FA 8 .   ? 27.600  42.473  11.041  1.00 21.78 ? 3039 HOH B O   1 
HETATM 9980  O  O   . HOH FA 8 .   ? 43.542  25.395  0.204   1.00 17.18 ? 3040 HOH B O   1 
HETATM 9981  O  O   . HOH FA 8 .   ? 27.794  58.576  52.148  1.00 34.94 ? 3041 HOH B O   1 
HETATM 9982  O  O   . HOH FA 8 .   ? 23.712  52.193  28.169  1.00 18.35 ? 3042 HOH B O   1 
HETATM 9983  O  O   . HOH FA 8 .   ? 45.907  57.593  14.108  1.00 36.27 ? 3043 HOH B O   1 
HETATM 9984  O  O   . HOH FA 8 .   ? 19.910  35.792  44.278  1.00 26.71 ? 3044 HOH B O   1 
HETATM 9985  O  O   . HOH FA 8 .   ? 36.384  43.363  79.493  1.00 41.98 ? 3045 HOH B O   1 
HETATM 9986  O  O   . HOH FA 8 .   ? 8.475   37.713  52.486  1.00 35.81 ? 3046 HOH B O   1 
HETATM 9987  O  O   . HOH FA 8 .   ? 33.726  60.019  53.799  1.00 54.95 ? 3047 HOH B O   1 
HETATM 9988  O  O   . HOH FA 8 .   ? 19.652  40.486  55.840  1.00 17.54 ? 3048 HOH B O   1 
HETATM 9989  O  O   . HOH FA 8 .   ? 22.705  49.571  26.286  1.00 24.56 ? 3049 HOH B O   1 
HETATM 9990  O  O   . HOH FA 8 .   ? 23.945  42.227  39.718  1.00 10.65 ? 3050 HOH B O   1 
HETATM 9991  O  O   . HOH FA 8 .   ? 47.998  16.060  50.268  1.00 17.08 ? 3051 HOH B O   1 
HETATM 9992  O  O   . HOH FA 8 .   ? 45.064  15.756  23.817  1.00 29.06 ? 3052 HOH B O   1 
HETATM 9993  O  O   . HOH FA 8 .   ? 48.430  44.145  28.804  1.00 16.73 ? 3053 HOH B O   1 
HETATM 9994  O  O   . HOH FA 8 .   ? 34.433  33.046  13.602  1.00 15.28 ? 3054 HOH B O   1 
HETATM 9995  O  O   . HOH FA 8 .   ? 26.688  28.666  52.916  1.00 17.42 ? 3055 HOH B O   1 
HETATM 9996  O  O   . HOH FA 8 .   ? 28.203  25.570  31.702  1.00 20.66 ? 3056 HOH B O   1 
HETATM 9997  O  O   . HOH FA 8 .   ? 27.462  28.616  40.450  1.00 25.05 ? 3057 HOH B O   1 
HETATM 9998  O  O   . HOH FA 8 .   ? 21.427  37.883  57.117  1.00 23.66 ? 3058 HOH B O   1 
HETATM 9999  O  O   . HOH FA 8 .   ? 21.829  51.292  30.317  1.00 25.03 ? 3059 HOH B O   1 
HETATM 10000 O  O   . HOH FA 8 .   ? 31.072  11.881  50.942  1.00 45.28 ? 3060 HOH B O   1 
HETATM 10001 O  O   . HOH FA 8 .   ? 61.621  34.635  29.732  1.00 34.28 ? 3061 HOH B O   1 
HETATM 10002 O  O   . HOH FA 8 .   ? 43.911  21.401  16.400  1.00 39.20 ? 3062 HOH B O   1 
HETATM 10003 O  O   . HOH FA 8 .   ? 38.160  36.356  8.729   1.00 22.79 ? 3063 HOH B O   1 
HETATM 10004 O  O   . HOH FA 8 .   ? 43.839  18.912  14.208  1.00 41.98 ? 3064 HOH B O   1 
HETATM 10005 O  O   . HOH FA 8 .   ? 21.179  27.661  55.154  1.00 34.64 ? 3065 HOH B O   1 
HETATM 10006 O  O   . HOH FA 8 .   ? 34.718  19.927  4.838   1.00 36.40 ? 3066 HOH B O   1 
HETATM 10007 O  O   . HOH FA 8 .   ? 29.191  44.769  64.492  1.00 50.08 ? 3067 HOH B O   1 
HETATM 10008 O  O   . HOH FA 8 .   ? 46.280  27.062  10.194  1.00 43.57 ? 3068 HOH B O   1 
# 
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   1   SER SER A . n 
A 1 2   TRP 2   2   2   TRP TRP A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   VAL 4   4   4   VAL VAL A . n 
A 1 5   GLY 5   5   5   GLY GLY A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   GLY 7   7   7   GLY GLY A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  CYS 15  15  15  CYS CYS A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  THR 23  23  23  THR THR A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  CYS 28  28  28  CYS CYS A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  ASN 30  30  30  ASN ASN A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  ARG 32  32  32  ARG ARG A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  TRP 46  46  46  TRP TRP A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  PRO 48  48  48  PRO PRO A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  TRP 61  61  61  TRP TRP A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ASP 93  93  93  ASP ASP A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 MET 101 101 101 MET MET A . n 
A 1 102 GLN 102 102 102 GLN GLN A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 PHE 113 113 113 PHE PHE A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 CYS 129 129 129 CYS CYS A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 GLU 131 131 131 GLU GLU A . n 
A 1 132 TYR 132 132 132 TYR TYR A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 MET 143 143 143 MET MET A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 PRO 145 145 145 PRO PRO A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 LYS 150 150 150 LYS LYS A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 LYS 152 152 152 LYS LYS A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 CYS 157 157 157 CYS CYS A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 ARG 162 162 162 ARG ARG A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 CYS 167 167 167 CYS CYS A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 PRO 171 171 171 PRO PRO A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 GLN 179 179 179 GLN GLN A . n 
A 1 180 ILE 180 180 180 ILE ILE A . n 
A 1 181 ASN 181 181 181 ASN ASN A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 LEU 187 187 187 LEU LEU A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 PRO 197 197 197 PRO PRO A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ALA 200 200 200 ALA ALA A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 MET 213 213 213 MET MET A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 TRP 220 220 220 TRP TRP A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 HIS 222 222 222 HIS HIS A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 TYR 226 226 226 TYR TYR A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 PRO 228 228 228 PRO PRO A . n 
A 1 229 PHE 229 229 229 PHE PHE A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 MET 232 232 232 MET MET A . n 
A 1 233 LYS 233 233 233 LYS LYS A . n 
A 1 234 PRO 234 234 234 PRO PRO A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 CYS 237 237 237 CYS CYS A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 PHE 239 239 239 PHE PHE A . n 
A 1 240 ILE 240 240 240 ILE ILE A . n 
A 1 241 ASN 241 241 241 ASN ASN A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 VAL 246 246 246 VAL VAL A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 CYS 248 248 248 CYS CYS A . n 
A 1 249 PHE 249 249 249 PHE PHE A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 ILE 260 260 260 ILE ILE A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 HIS 266 266 266 HIS HIS A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 GLU 272 272 272 GLU GLU A . n 
A 1 273 HIS 273 273 273 HIS HIS A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 ARG 275 275 275 ARG ARG A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 ALA 277 277 277 ALA ALA A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ARG 282 282 282 ARG ARG A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 HIS 286 286 286 HIS HIS A . n 
A 1 287 TRP 287 287 287 TRP TRP A . n 
A 1 288 ASP 288 288 288 ASP ASP A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 GLU 295 295 295 GLU GLU A . n 
A 1 296 ALA 296 296 296 ALA ALA A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 PHE 303 303 303 PHE PHE A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 GLN 305 305 305 GLN GLN A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 ILE 307 307 307 ILE ILE A . n 
A 1 308 THR 308 308 308 THR THR A . n 
A 1 309 PHE 309 309 309 PHE PHE A . n 
A 1 310 ARG 310 310 310 ARG ARG A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 PRO 314 314 314 PRO PRO A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 GLY 318 318 318 GLY GLY A . n 
A 1 319 SER 319 319 319 SER SER A . n 
A 1 320 GLU 320 320 320 GLU GLU A . n 
A 1 321 MET 321 321 321 MET MET A . n 
A 1 322 GLN 322 322 322 GLN GLN A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 TRP 324 324 324 TRP TRP A . n 
A 1 325 ILE 325 325 325 ILE ILE A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 ARG 327 327 327 ARG ARG A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 GLN 329 329 329 GLN GLN A . n 
A 1 330 GLY 330 330 330 GLY GLY A . n 
A 1 331 TYR 331 331 331 TYR TYR A . n 
A 1 332 ASN 332 332 332 ASN ASN A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 SER 334 334 334 SER SER A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 ARG 338 338 338 ARG ARG A . n 
A 1 339 ILE 339 339 339 ILE ILE A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 ASN 341 341 341 ASN ASN A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 PHE 345 345 345 PHE PHE A . n 
A 1 346 ALA 346 346 346 ALA ALA A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 ARG 348 348 348 ARG ARG A . n 
A 1 349 PHE 349 349 349 PHE PHE A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 MET 352 352 352 MET MET A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 VAL 354 354 354 VAL VAL A . n 
A 1 355 PRO 355 355 355 PRO PRO A . n 
A 1 356 SER 356 356 356 SER SER A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 VAL 358 358 358 VAL VAL A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 ARG 360 360 360 ARG ARG A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 ASP 362 362 362 ASP ASP A . n 
A 1 363 GLU 363 363 363 GLU GLU A . n 
A 1 364 ASN 364 364 364 ASN ASN A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 GLN 366 366 366 GLN GLN A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 ARG 368 368 368 ARG ARG A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 PRO 370 370 370 PRO PRO A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 ALA 372 372 372 ALA ALA A . n 
A 1 373 GLU 373 373 373 GLU GLU A . n 
A 1 374 LEU 374 374 374 LEU LEU A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 HIS 377 377 377 HIS HIS A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 PHE 380 380 380 PHE PHE A . n 
A 1 381 PHE 381 381 381 PHE PHE A . n 
A 1 382 ASN 382 382 382 ASN ASN A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 TRP 384 384 384 TRP TRP A . n 
A 1 385 ARG 385 385 385 ARG ARG A . n 
A 1 386 ILE 386 386 386 ILE ILE A . n 
A 1 387 ILE 387 387 387 ILE ILE A . n 
A 1 388 LYS 388 388 388 LYS LYS A . n 
A 1 389 ASP 389 389 389 ASP ASP A . n 
A 1 390 GLY 390 390 390 GLY GLY A . n 
A 1 391 GLY 391 391 391 GLY GLY A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 PRO 394 394 394 PRO PRO A . n 
A 1 395 LEU 395 395 395 LEU LEU A . n 
A 1 396 VAL 396 396 396 VAL VAL A . n 
A 1 397 ARG 397 397 397 ARG ARG A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 LEU 399 399 399 LEU LEU A . n 
A 1 400 LEU 400 400 400 LEU LEU A . n 
A 1 401 ALA 401 401 401 ALA ALA A . n 
A 1 402 LYS 402 402 402 LYS LYS A . n 
A 1 403 LYS 403 403 403 LYS LYS A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 LYS 405 405 405 LYS LYS A . n 
A 1 406 LEU 406 406 406 LEU LEU A . n 
A 1 407 MET 407 407 407 MET MET A . n 
A 1 408 ASN 408 408 408 ASN ASN A . n 
A 1 409 GLN 409 409 409 GLN GLN A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LYS 411 411 411 LYS LYS A . n 
A 1 412 MET 412 412 412 MET MET A . n 
A 1 413 VAL 413 413 413 VAL VAL A . n 
A 1 414 THR 414 414 414 THR THR A . n 
A 1 415 SER 415 415 415 SER SER A . n 
A 1 416 GLU 416 416 416 GLU GLU A . n 
A 1 417 LEU 417 417 417 LEU LEU A . n 
A 1 418 ARG 418 418 418 ARG ARG A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 LEU 421 421 421 LEU LEU A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 GLN 423 423 423 GLN GLN A . n 
A 1 424 PRO 424 424 424 PRO PRO A . n 
A 1 425 THR 425 425 425 THR THR A . n 
A 1 426 HIS 426 426 426 HIS HIS A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 HIS 429 429 429 HIS HIS A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 PHE 431 431 431 PHE PHE A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 LEU 433 433 433 LEU LEU A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 ALA 435 435 435 ALA ALA A . n 
A 1 436 ILE 436 436 436 ILE ILE A . n 
A 1 437 ASN 437 437 437 ASN ASN A . n 
A 1 438 LEU 438 438 438 LEU LEU A . n 
A 1 439 GLN 439 439 439 GLN GLN A . n 
A 1 440 ARG 440 440 440 ARG ARG A . n 
A 1 441 CYS 441 441 441 CYS CYS A . n 
A 1 442 ARG 442 442 442 ARG ARG A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 HIS 444 444 444 HIS HIS A . n 
A 1 445 GLY 445 445 445 GLY GLY A . n 
A 1 446 MET 446 446 446 MET MET A . n 
A 1 447 PRO 447 447 447 PRO PRO A . n 
A 1 448 GLY 448 448 448 GLY GLY A . n 
A 1 449 TYR 449 449 449 TYR TYR A . n 
A 1 450 ASN 450 450 450 ASN ASN A . n 
A 1 451 SER 451 451 451 SER SER A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 ARG 453 453 453 ARG ARG A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 CYS 456 456 456 CYS CYS A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 SER 459 459 459 SER SER A . n 
A 1 460 GLN 460 460 460 GLN GLN A . n 
A 1 461 PRO 461 461 461 PRO PRO A . n 
A 1 462 LYS 462 462 462 LYS LYS A . n 
A 1 463 THR 463 463 463 THR THR A . n 
A 1 464 LEU 464 464 464 LEU LEU A . n 
A 1 465 LYS 465 465 465 LYS LYS A . n 
A 1 466 GLY 466 466 466 GLY GLY A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 GLN 468 468 468 GLN GLN A . n 
A 1 469 ALA 469 469 469 ALA ALA A . n 
A 1 470 VAL 470 470 470 VAL VAL A . n 
A 1 471 LEU 471 471 471 LEU LEU A . n 
A 1 472 LYS 472 472 472 LYS LYS A . n 
A 1 473 ASN 473 473 473 ASN ASN A . n 
A 1 474 LYS 474 474 474 LYS LYS A . n 
A 1 475 ILE 475 475 475 ILE ILE A . n 
A 1 476 LEU 476 476 476 LEU LEU A . n 
A 1 477 ALA 477 477 477 ALA ALA A . n 
A 1 478 LYS 478 478 478 LYS LYS A . n 
A 1 479 LYS 479 479 479 LYS LYS A . n 
A 1 480 LEU 480 480 480 LEU LEU A . n 
A 1 481 LEU 481 481 481 LEU LEU A . n 
A 1 482 ASP 482 482 482 ASP ASP A . n 
A 1 483 LEU 483 483 483 LEU LEU A . n 
A 1 484 TYR 484 484 484 TYR TYR A . n 
A 1 485 LYS 485 485 485 LYS LYS A . n 
A 1 486 THR 486 486 486 THR THR A . n 
A 1 487 PRO 487 487 487 PRO PRO A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 ILE 490 490 490 ILE ILE A . n 
A 1 491 ASP 491 491 491 ASP ASP A . n 
A 1 492 ILE 492 492 492 ILE ILE A . n 
A 1 493 TRP 493 493 493 TRP TRP A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 GLY 495 495 495 GLY GLY A . n 
A 1 496 GLY 496 496 496 GLY GLY A . n 
A 1 497 ASN 497 497 497 ASN ASN A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 GLU 499 499 499 GLU GLU A . n 
A 1 500 PRO 500 500 500 PRO PRO A . n 
A 1 501 MET 501 501 501 MET MET A . n 
A 1 502 VAL 502 502 502 VAL VAL A . n 
A 1 503 GLU 503 503 503 GLU GLU A . n 
A 1 504 ARG 504 504 504 ARG ARG A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 ARG 506 506 506 ARG ARG A . n 
A 1 507 VAL 507 507 507 VAL VAL A . n 
A 1 508 GLY 508 508 508 GLY GLY A . n 
A 1 509 PRO 509 509 509 PRO PRO A . n 
A 1 510 LEU 510 510 510 LEU LEU A . n 
A 1 511 LEU 511 511 511 LEU LEU A . n 
A 1 512 ALA 512 512 512 ALA ALA A . n 
A 1 513 CYS 513 513 513 CYS CYS A . n 
A 1 514 LEU 514 514 514 LEU LEU A . n 
A 1 515 LEU 515 515 515 LEU LEU A . n 
A 1 516 GLY 516 516 516 GLY GLY A . n 
A 1 517 ARG 517 517 517 ARG ARG A . n 
A 1 518 GLN 518 518 518 GLN GLN A . n 
A 1 519 PHE 519 519 519 PHE PHE A . n 
A 1 520 GLN 520 520 520 GLN GLN A . n 
A 1 521 GLN 521 521 521 GLN GLN A . n 
A 1 522 ILE 522 522 522 ILE ILE A . n 
A 1 523 ARG 523 523 523 ARG ARG A . n 
A 1 524 ASP 524 524 524 ASP ASP A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 ASP 526 526 526 ASP ASP A . n 
A 1 527 ARG 527 527 527 ARG ARG A . n 
A 1 528 PHE 528 528 528 PHE PHE A . n 
A 1 529 TRP 529 529 529 TRP TRP A . n 
A 1 530 TRP 530 530 530 TRP TRP A . n 
A 1 531 GLU 531 531 531 GLU GLU A . n 
A 1 532 ASN 532 532 532 ASN ASN A . n 
A 1 533 PRO 533 533 533 PRO PRO A . n 
A 1 534 GLY 534 534 534 GLY GLY A . n 
A 1 535 VAL 535 535 535 VAL VAL A . n 
A 1 536 PHE 536 536 536 PHE PHE A . n 
A 1 537 THR 537 537 537 THR THR A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 LYS 539 539 539 LYS LYS A . n 
A 1 540 GLN 540 540 540 GLN GLN A . n 
A 1 541 ARG 541 541 541 ARG ARG A . n 
A 1 542 ASP 542 542 542 ASP ASP A . n 
A 1 543 SER 543 543 543 SER SER A . n 
A 1 544 LEU 544 544 544 LEU LEU A . n 
A 1 545 GLN 545 545 545 GLN GLN A . n 
A 1 546 LYS 546 546 546 LYS LYS A . n 
A 1 547 VAL 547 547 547 VAL VAL A . n 
A 1 548 SER 548 548 548 SER SER A . n 
A 1 549 PHE 549 549 549 PHE PHE A . n 
A 1 550 SER 550 550 550 SER SER A . n 
A 1 551 ARG 551 551 551 ARG ARG A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 ILE 553 553 553 ILE ILE A . n 
A 1 554 CYS 554 554 554 CYS CYS A . n 
A 1 555 ASP 555 555 555 ASP ASP A . n 
A 1 556 ASN 556 556 556 ASN ASN A . n 
A 1 557 THR 557 557 557 THR THR A . n 
A 1 558 HIS 558 558 558 HIS HIS A . n 
A 1 559 ILE 559 559 559 ILE ILE A . n 
A 1 560 THR 560 560 560 THR THR A . n 
A 1 561 LYS 561 561 561 LYS LYS A . n 
A 1 562 VAL 562 562 562 VAL VAL A . n 
A 1 563 PRO 563 563 563 PRO PRO A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 HIS 565 565 565 HIS HIS A . n 
A 1 566 ALA 566 566 566 ALA ALA A . n 
A 1 567 PHE 567 567 567 PHE PHE A . n 
A 1 568 GLN 568 568 568 GLN GLN A . n 
A 1 569 ALA 569 569 569 ALA ALA A . n 
A 1 570 ASN 570 570 570 ASN ASN A . n 
A 1 571 ASN 571 571 571 ASN ASN A . n 
A 1 572 TYR 572 572 572 TYR TYR A . n 
A 1 573 PRO 573 573 573 PRO PRO A . n 
A 1 574 HIS 574 574 574 HIS HIS A . n 
A 1 575 ASP 575 575 575 ASP ASP A . n 
A 1 576 PHE 576 576 576 PHE PHE A . n 
A 1 577 VAL 577 577 577 VAL VAL A . n 
A 1 578 ASP 578 578 578 ASP ASP A . n 
A 1 579 CYS 579 579 579 CYS CYS A . n 
A 1 580 SER 580 580 580 SER SER A . n 
A 1 581 ALA 581 581 581 ALA ALA A . n 
A 1 582 ILE 582 582 582 ILE ILE A . n 
A 1 583 ASP 583 583 583 ASP ASP A . n 
A 1 584 LYS 584 584 584 LYS LYS A . n 
A 1 585 LEU 585 585 585 LEU LEU A . n 
A 1 586 ASP 586 586 586 ASP ASP A . n 
A 1 587 LEU 587 587 587 LEU LEU A . n 
A 1 588 SER 588 588 588 SER SER A . n 
A 1 589 PRO 589 589 589 PRO PRO A . n 
A 1 590 TRP 590 590 590 TRP TRP A . n 
A 1 591 ALA 591 591 591 ALA ALA A . n 
A 1 592 SER 592 592 592 SER SER A . n 
A 1 593 ARG 593 593 593 ARG ARG A . n 
A 1 594 GLU 594 594 594 GLU GLU A . n 
A 1 595 ASN 595 595 595 ASN ASN A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   TRP 2   2   2   TRP TRP B . n 
B 1 3   GLU 3   3   3   GLU GLU B . n 
B 1 4   VAL 4   4   4   VAL VAL B . n 
B 1 5   GLY 5   5   5   GLY GLY B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   GLY 7   7   7   GLY GLY B . n 
B 1 8   ALA 8   8   8   ALA ALA B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  LYS 14  14  14  LYS LYS B . n 
B 1 15  CYS 15  15  15  CYS CYS B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  ASN 18  18  18  ASN ASN B . n 
B 1 19  SER 19  19  19  SER SER B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  THR 23  23  23  THR THR B . n 
B 1 24  ILE 24  24  24  ILE ILE B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  ASP 27  27  27  ASP ASP B . n 
B 1 28  CYS 28  28  28  CYS CYS B . n 
B 1 29  ASN 29  29  29  ASN ASN B . n 
B 1 30  ASN 30  30  30  ASN ASN B . n 
B 1 31  ARG 31  31  31  ARG ARG B . n 
B 1 32  ARG 32  32  32  ARG ARG B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  ALA 35  35  35  ALA ALA B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  ARG 41  41  41  ARG ARG B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  TRP 46  46  46  TRP TRP B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  PRO 48  48  48  PRO PRO B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  GLU 50  50  50  GLU GLU B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  GLU 52  52  52  GLU GLU B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  GLY 54  54  54  GLY GLY B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  TRP 61  61  61  TRP TRP B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  LYS 65  65  65  LYS LYS B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  ASN 68  68  68  ASN ASN B . n 
B 1 69  GLY 69  69  69  GLY GLY B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  SER 79  79  79  SER SER B . n 
B 1 80  ASN 80  80  80  ASN ASN B . n 
B 1 81  LYS 81  81  81  LYS LYS B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  ASP 93  93  93  ASP ASP B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  SER 97  97  97  SER SER B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 MET 101 101 101 MET MET B . n 
B 1 102 GLN 102 102 102 GLN GLN B . n 
B 1 103 TRP 103 103 103 TRP TRP B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 GLN 105 105 105 GLN GLN B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 HIS 109 109 109 HIS HIS B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 ASP 112 112 112 ASP ASP B . n 
B 1 113 PHE 113 113 113 PHE PHE B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 PRO 115 115 115 PRO PRO B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 THR 117 117 117 THR THR B . n 
B 1 118 GLU 118 118 118 GLU GLU B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 SER 122 122 122 SER SER B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 HIS 124 124 124 HIS HIS B . n 
B 1 125 SER 125 125 125 SER SER B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 GLN 128 128 128 GLN GLN B . n 
B 1 129 CYS 129 129 129 CYS CYS B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 GLU 131 131 131 GLU GLU B . n 
B 1 132 TYR 132 132 132 TYR TYR B . n 
B 1 133 CYS 133 133 133 CYS CYS B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 ASN 138 138 138 ASN ASN B . n 
B 1 139 CYS 139 139 139 CYS CYS B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 MET 143 143 143 MET MET B . n 
B 1 144 PHE 144 144 144 PHE PHE B . n 
B 1 145 PRO 145 145 145 PRO PRO B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 ASN 147 147 147 ASN ASN B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 LYS 150 150 150 LYS LYS B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 LYS 152 152 152 LYS LYS B . n 
B 1 153 THR 153 153 153 THR THR B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 GLY 155 155 155 GLY GLY B . n 
B 1 156 LYS 156 156 156 LYS LYS B . n 
B 1 157 CYS 157 157 157 CYS CYS B . n 
B 1 158 MET 158 158 158 MET MET B . n 
B 1 159 PRO 159 159 159 PRO PRO B . n 
B 1 160 PHE 160 160 160 PHE PHE B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 ARG 162 162 162 ARG ARG B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 GLY 164 164 164 GLY GLY B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 VAL 166 166 166 VAL VAL B . n 
B 1 167 CYS 167 167 167 CYS CYS B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 PRO 171 171 171 PRO PRO B . n 
B 1 172 TYR 172 172 172 TYR TYR B . n 
B 1 173 GLN 173 173 173 GLN GLN B . n 
B 1 174 SER 174 174 174 SER SER B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 ALA 176 176 176 ALA ALA B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 ASP 178 178 178 ASP ASP B . n 
B 1 179 GLN 179 179 179 GLN GLN B . n 
B 1 180 ILE 180 180 180 ILE ILE B . n 
B 1 181 ASN 181 181 181 ASN ASN B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 PHE 186 186 186 PHE PHE B . n 
B 1 187 LEU 187 187 187 LEU LEU B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 VAL 192 192 192 VAL VAL B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 SER 195 195 195 SER SER B . n 
B 1 196 GLU 196 196 196 GLU GLU B . n 
B 1 197 PRO 197 197 197 PRO PRO B . n 
B 1 198 SER 198 198 198 SER SER B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 ALA 200 200 200 ALA ALA B . n 
B 1 201 SER 201 201 201 SER SER B . n 
B 1 202 ARG 202 202 202 ARG ARG B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 GLY 211 211 211 GLY GLY B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 MET 213 213 213 MET MET B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 GLN 217 217 217 GLN GLN B . n 
B 1 218 GLU 218 218 218 GLU GLU B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 TRP 220 220 220 TRP TRP B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 HIS 222 222 222 HIS HIS B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 TYR 226 226 226 TYR TYR B . n 
B 1 227 PRO 227 227 227 PRO PRO B . n 
B 1 228 PRO 228 228 228 PRO PRO B . n 
B 1 229 PHE 229 229 229 PHE PHE B . n 
B 1 230 ASN 230 230 230 ASN ASN B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 MET 232 232 232 MET MET B . n 
B 1 233 LYS 233 233 233 LYS LYS B . n 
B 1 234 PRO 234 234 234 PRO PRO B . n 
B 1 235 SER 235 235 235 SER SER B . n 
B 1 236 PRO 236 236 236 PRO PRO B . n 
B 1 237 CYS 237 237 237 CYS CYS B . n 
B 1 238 GLU 238 238 238 GLU GLU B . n 
B 1 239 PHE 239 239 239 PHE PHE B . n 
B 1 240 ILE 240 240 240 ILE ILE B . n 
B 1 241 ASN 241 241 241 ASN ASN B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 VAL 246 246 246 VAL VAL B . n 
B 1 247 PRO 247 247 247 PRO PRO B . n 
B 1 248 CYS 248 248 248 CYS CYS B . n 
B 1 249 PHE 249 249 249 PHE PHE B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 ALA 251 251 251 ALA ALA B . n 
B 1 252 GLY 252 252 252 GLY GLY B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 ALA 256 256 256 ALA ALA B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 GLN 259 259 259 GLN GLN B . n 
B 1 260 ILE 260 260 260 ILE ILE B . n 
B 1 261 LEU 261 261 261 LEU LEU B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 HIS 266 266 266 HIS HIS B . n 
B 1 267 THR 267 267 267 THR THR B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 ARG 271 271 271 ARG ARG B . n 
B 1 272 GLU 272 272 272 GLU GLU B . n 
B 1 273 HIS 273 273 273 HIS HIS B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 ARG 275 275 275 ARG ARG B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 ALA 277 277 277 ALA ALA B . n 
B 1 278 ARG 278 278 278 ARG ARG B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 ARG 282 282 282 ARG ARG B . n 
B 1 283 LEU 283 283 283 LEU LEU B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 PRO 285 285 285 PRO PRO B . n 
B 1 286 HIS 286 286 286 HIS HIS B . n 
B 1 287 TRP 287 287 287 TRP TRP B . n 
B 1 288 ASP 288 288 288 ASP ASP B . n 
B 1 289 GLY 289 289 289 GLY GLY B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 LEU 292 292 292 LEU LEU B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 GLN 294 294 294 GLN GLN B . n 
B 1 295 GLU 295 295 295 GLU GLU B . n 
B 1 296 ALA 296 296 296 ALA ALA B . n 
B 1 297 ARG 297 297 297 ARG ARG B . n 
B 1 298 LYS 298 298 298 LYS LYS B . n 
B 1 299 ILE 299 299 299 ILE ILE B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 GLY 301 301 301 GLY GLY B . n 
B 1 302 ALA 302 302 302 ALA ALA B . n 
B 1 303 PHE 303 303 303 PHE PHE B . n 
B 1 304 ILE 304 304 304 ILE ILE B . n 
B 1 305 GLN 305 305 305 GLN GLN B . n 
B 1 306 ILE 306 306 306 ILE ILE B . n 
B 1 307 ILE 307 307 307 ILE ILE B . n 
B 1 308 THR 308 308 308 THR THR B . n 
B 1 309 PHE 309 309 309 PHE PHE B . n 
B 1 310 ARG 310 310 310 ARG ARG B . n 
B 1 311 ASP 311 311 311 ASP ASP B . n 
B 1 312 TYR 312 312 312 TYR TYR B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 PRO 314 314 314 PRO PRO B . n 
B 1 315 ILE 315 315 315 ILE ILE B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 LEU 317 317 317 LEU LEU B . n 
B 1 318 GLY 318 318 318 GLY GLY B . n 
B 1 319 SER 319 319 319 SER SER B . n 
B 1 320 GLU 320 320 320 GLU GLU B . n 
B 1 321 MET 321 321 321 MET MET B . n 
B 1 322 GLN 322 322 322 GLN GLN B . n 
B 1 323 LYS 323 323 323 LYS LYS B . n 
B 1 324 TRP 324 324 324 TRP TRP B . n 
B 1 325 ILE 325 325 325 ILE ILE B . n 
B 1 326 PRO 326 326 326 PRO PRO B . n 
B 1 327 ARG 327 327 327 ARG ARG B . n 
B 1 328 TYR 328 328 328 TYR TYR B . n 
B 1 329 GLN 329 329 329 GLN GLN B . n 
B 1 330 GLY 330 330 330 GLY GLY B . n 
B 1 331 TYR 331 331 331 TYR TYR B . n 
B 1 332 ASN 332 332 332 ASN ASN B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 SER 334 334 334 SER SER B . n 
B 1 335 VAL 335 335 335 VAL VAL B . n 
B 1 336 ASP 336 336 336 ASP ASP B . n 
B 1 337 PRO 337 337 337 PRO PRO B . n 
B 1 338 ARG 338 338 338 ARG ARG B . n 
B 1 339 ILE 339 339 339 ILE ILE B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 ASN 341 341 341 ASN ASN B . n 
B 1 342 VAL 342 342 342 VAL VAL B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 THR 344 344 344 THR THR B . n 
B 1 345 PHE 345 345 345 PHE PHE B . n 
B 1 346 ALA 346 346 346 ALA ALA B . n 
B 1 347 PHE 347 347 347 PHE PHE B . n 
B 1 348 ARG 348 348 348 ARG ARG B . n 
B 1 349 PHE 349 349 349 PHE PHE B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 HIS 351 351 351 HIS HIS B . n 
B 1 352 MET 352 352 352 MET MET B . n 
B 1 353 GLU 353 353 353 GLU GLU B . n 
B 1 354 VAL 354 354 354 VAL VAL B . n 
B 1 355 PRO 355 355 355 PRO PRO B . n 
B 1 356 SER 356 356 356 SER SER B . n 
B 1 357 THR 357 357 357 THR THR B . n 
B 1 358 VAL 358 358 358 VAL VAL B . n 
B 1 359 SER 359 359 359 SER SER B . n 
B 1 360 ARG 360 360 360 ARG ARG B . n 
B 1 361 LEU 361 361 361 LEU LEU B . n 
B 1 362 ASP 362 362 362 ASP ASP B . n 
B 1 363 GLU 363 363 363 GLU GLU B . n 
B 1 364 ASN 364 364 364 ASN ASN B . n 
B 1 365 TYR 365 365 365 TYR TYR B . n 
B 1 366 GLN 366 366 366 GLN GLN B . n 
B 1 367 PRO 367 367 367 PRO PRO B . n 
B 1 368 ARG 368 368 368 ARG ARG B . n 
B 1 369 GLY 369 369 369 GLY GLY B . n 
B 1 370 PRO 370 370 370 PRO PRO B . n 
B 1 371 GLU 371 371 371 GLU GLU B . n 
B 1 372 ALA 372 372 372 ALA ALA B . n 
B 1 373 GLU 373 373 373 GLU GLU B . n 
B 1 374 LEU 374 374 374 LEU LEU B . n 
B 1 375 PRO 375 375 375 PRO PRO B . n 
B 1 376 LEU 376 376 376 LEU LEU B . n 
B 1 377 HIS 377 377 377 HIS HIS B . n 
B 1 378 THR 378 378 378 THR THR B . n 
B 1 379 LEU 379 379 379 LEU LEU B . n 
B 1 380 PHE 380 380 380 PHE PHE B . n 
B 1 381 PHE 381 381 381 PHE PHE B . n 
B 1 382 ASN 382 382 382 ASN ASN B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 TRP 384 384 384 TRP TRP B . n 
B 1 385 ARG 385 385 385 ARG ARG B . n 
B 1 386 ILE 386 386 386 ILE ILE B . n 
B 1 387 ILE 387 387 387 ILE ILE B . n 
B 1 388 LYS 388 388 388 LYS LYS B . n 
B 1 389 ASP 389 389 389 ASP ASP B . n 
B 1 390 GLY 390 390 390 GLY GLY B . n 
B 1 391 GLY 391 391 391 GLY GLY B . n 
B 1 392 ILE 392 392 392 ILE ILE B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 PRO 394 394 394 PRO PRO B . n 
B 1 395 LEU 395 395 395 LEU LEU B . n 
B 1 396 VAL 396 396 396 VAL VAL B . n 
B 1 397 ARG 397 397 397 ARG ARG B . n 
B 1 398 GLY 398 398 398 GLY GLY B . n 
B 1 399 LEU 399 399 399 LEU LEU B . n 
B 1 400 LEU 400 400 400 LEU LEU B . n 
B 1 401 ALA 401 401 401 ALA ALA B . n 
B 1 402 LYS 402 402 402 LYS LYS B . n 
B 1 403 LYS 403 403 403 LYS LYS B . n 
B 1 404 SER 404 404 404 SER SER B . n 
B 1 405 LYS 405 405 405 LYS LYS B . n 
B 1 406 LEU 406 406 406 LEU LEU B . n 
B 1 407 MET 407 407 407 MET MET B . n 
B 1 408 ASN 408 408 408 ASN ASN B . n 
B 1 409 GLN 409 409 409 GLN GLN B . n 
B 1 410 ASN 410 410 410 ASN ASN B . n 
B 1 411 LYS 411 411 411 LYS LYS B . n 
B 1 412 MET 412 412 412 MET MET B . n 
B 1 413 VAL 413 413 413 VAL VAL B . n 
B 1 414 THR 414 414 414 THR THR B . n 
B 1 415 SER 415 415 415 SER SER B . n 
B 1 416 GLU 416 416 416 GLU GLU B . n 
B 1 417 LEU 417 417 417 LEU LEU B . n 
B 1 418 ARG 418 418 418 ARG ARG B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 LEU 421 421 421 LEU LEU B . n 
B 1 422 PHE 422 422 422 PHE PHE B . n 
B 1 423 GLN 423 423 423 GLN GLN B . n 
B 1 424 PRO 424 424 424 PRO PRO B . n 
B 1 425 THR 425 425 425 THR THR B . n 
B 1 426 HIS 426 426 426 HIS HIS B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 HIS 429 429 429 HIS HIS B . n 
B 1 430 GLY 430 430 430 GLY GLY B . n 
B 1 431 PHE 431 431 431 PHE PHE B . n 
B 1 432 ASP 432 432 432 ASP ASP B . n 
B 1 433 LEU 433 433 433 LEU LEU B . n 
B 1 434 ALA 434 434 434 ALA ALA B . n 
B 1 435 ALA 435 435 435 ALA ALA B . n 
B 1 436 ILE 436 436 436 ILE ILE B . n 
B 1 437 ASN 437 437 437 ASN ASN B . n 
B 1 438 LEU 438 438 438 LEU LEU B . n 
B 1 439 GLN 439 439 439 GLN GLN B . n 
B 1 440 ARG 440 440 440 ARG ARG B . n 
B 1 441 CYS 441 441 441 CYS CYS B . n 
B 1 442 ARG 442 442 442 ARG ARG B . n 
B 1 443 ASP 443 443 443 ASP ASP B . n 
B 1 444 HIS 444 444 444 HIS HIS B . n 
B 1 445 GLY 445 445 445 GLY GLY B . n 
B 1 446 MET 446 446 446 MET MET B . n 
B 1 447 PRO 447 447 447 PRO PRO B . n 
B 1 448 GLY 448 448 448 GLY GLY B . n 
B 1 449 TYR 449 449 449 TYR TYR B . n 
B 1 450 ASN 450 450 450 ASN ASN B . n 
B 1 451 SER 451 451 451 SER SER B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 ARG 453 453 453 ARG ARG B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 PHE 455 455 455 PHE PHE B . n 
B 1 456 CYS 456 456 456 CYS CYS B . n 
B 1 457 GLY 457 457 457 GLY GLY B . n 
B 1 458 LEU 458 458 458 LEU LEU B . n 
B 1 459 SER 459 459 459 SER SER B . n 
B 1 460 GLN 460 460 460 GLN GLN B . n 
B 1 461 PRO 461 461 461 PRO PRO B . n 
B 1 462 LYS 462 462 462 LYS LYS B . n 
B 1 463 THR 463 463 463 THR THR B . n 
B 1 464 LEU 464 464 464 LEU LEU B . n 
B 1 465 LYS 465 465 465 LYS LYS B . n 
B 1 466 GLY 466 466 466 GLY GLY B . n 
B 1 467 LEU 467 467 467 LEU LEU B . n 
B 1 468 GLN 468 468 468 GLN GLN B . n 
B 1 469 ALA 469 469 469 ALA ALA B . n 
B 1 470 VAL 470 470 470 VAL VAL B . n 
B 1 471 LEU 471 471 471 LEU LEU B . n 
B 1 472 LYS 472 472 472 LYS LYS B . n 
B 1 473 ASN 473 473 473 ASN ASN B . n 
B 1 474 LYS 474 474 474 LYS LYS B . n 
B 1 475 ILE 475 475 475 ILE ILE B . n 
B 1 476 LEU 476 476 476 LEU LEU B . n 
B 1 477 ALA 477 477 477 ALA ALA B . n 
B 1 478 LYS 478 478 478 LYS LYS B . n 
B 1 479 LYS 479 479 479 LYS LYS B . n 
B 1 480 LEU 480 480 480 LEU LEU B . n 
B 1 481 LEU 481 481 481 LEU LEU B . n 
B 1 482 ASP 482 482 482 ASP ASP B . n 
B 1 483 LEU 483 483 483 LEU LEU B . n 
B 1 484 TYR 484 484 484 TYR TYR B . n 
B 1 485 LYS 485 485 485 LYS LYS B . n 
B 1 486 THR 486 486 486 THR THR B . n 
B 1 487 PRO 487 487 487 PRO PRO B . n 
B 1 488 ASP 488 488 488 ASP ASP B . n 
B 1 489 ASN 489 489 489 ASN ASN B . n 
B 1 490 ILE 490 490 490 ILE ILE B . n 
B 1 491 ASP 491 491 491 ASP ASP B . n 
B 1 492 ILE 492 492 492 ILE ILE B . n 
B 1 493 TRP 493 493 493 TRP TRP B . n 
B 1 494 ILE 494 494 494 ILE ILE B . n 
B 1 495 GLY 495 495 495 GLY GLY B . n 
B 1 496 GLY 496 496 496 GLY GLY B . n 
B 1 497 ASN 497 497 497 ASN ASN B . n 
B 1 498 ALA 498 498 498 ALA ALA B . n 
B 1 499 GLU 499 499 499 GLU GLU B . n 
B 1 500 PRO 500 500 500 PRO PRO B . n 
B 1 501 MET 501 501 501 MET MET B . n 
B 1 502 VAL 502 502 502 VAL VAL B . n 
B 1 503 GLU 503 503 503 GLU GLU B . n 
B 1 504 ARG 504 504 504 ARG ARG B . n 
B 1 505 GLY 505 505 505 GLY GLY B . n 
B 1 506 ARG 506 506 506 ARG ARG B . n 
B 1 507 VAL 507 507 507 VAL VAL B . n 
B 1 508 GLY 508 508 508 GLY GLY B . n 
B 1 509 PRO 509 509 509 PRO PRO B . n 
B 1 510 LEU 510 510 510 LEU LEU B . n 
B 1 511 LEU 511 511 511 LEU LEU B . n 
B 1 512 ALA 512 512 512 ALA ALA B . n 
B 1 513 CYS 513 513 513 CYS CYS B . n 
B 1 514 LEU 514 514 514 LEU LEU B . n 
B 1 515 LEU 515 515 515 LEU LEU B . n 
B 1 516 GLY 516 516 516 GLY GLY B . n 
B 1 517 ARG 517 517 517 ARG ARG B . n 
B 1 518 GLN 518 518 518 GLN GLN B . n 
B 1 519 PHE 519 519 519 PHE PHE B . n 
B 1 520 GLN 520 520 520 GLN GLN B . n 
B 1 521 GLN 521 521 521 GLN GLN B . n 
B 1 522 ILE 522 522 522 ILE ILE B . n 
B 1 523 ARG 523 523 523 ARG ARG B . n 
B 1 524 ASP 524 524 524 ASP ASP B . n 
B 1 525 GLY 525 525 525 GLY GLY B . n 
B 1 526 ASP 526 526 526 ASP ASP B . n 
B 1 527 ARG 527 527 527 ARG ARG B . n 
B 1 528 PHE 528 528 528 PHE PHE B . n 
B 1 529 TRP 529 529 529 TRP TRP B . n 
B 1 530 TRP 530 530 530 TRP TRP B . n 
B 1 531 GLU 531 531 531 GLU GLU B . n 
B 1 532 ASN 532 532 532 ASN ASN B . n 
B 1 533 PRO 533 533 533 PRO PRO B . n 
B 1 534 GLY 534 534 534 GLY GLY B . n 
B 1 535 VAL 535 535 535 VAL VAL B . n 
B 1 536 PHE 536 536 536 PHE PHE B . n 
B 1 537 THR 537 537 537 THR THR B . n 
B 1 538 GLU 538 538 538 GLU GLU B . n 
B 1 539 LYS 539 539 539 LYS LYS B . n 
B 1 540 GLN 540 540 540 GLN GLN B . n 
B 1 541 ARG 541 541 541 ARG ARG B . n 
B 1 542 ASP 542 542 542 ASP ASP B . n 
B 1 543 SER 543 543 543 SER SER B . n 
B 1 544 LEU 544 544 544 LEU LEU B . n 
B 1 545 GLN 545 545 545 GLN GLN B . n 
B 1 546 LYS 546 546 546 LYS LYS B . n 
B 1 547 VAL 547 547 547 VAL VAL B . n 
B 1 548 SER 548 548 548 SER SER B . n 
B 1 549 PHE 549 549 549 PHE PHE B . n 
B 1 550 SER 550 550 550 SER SER B . n 
B 1 551 ARG 551 551 551 ARG ARG B . n 
B 1 552 LEU 552 552 552 LEU LEU B . n 
B 1 553 ILE 553 553 553 ILE ILE B . n 
B 1 554 CYS 554 554 554 CYS CYS B . n 
B 1 555 ASP 555 555 555 ASP ASP B . n 
B 1 556 ASN 556 556 556 ASN ASN B . n 
B 1 557 THR 557 557 557 THR THR B . n 
B 1 558 HIS 558 558 558 HIS HIS B . n 
B 1 559 ILE 559 559 559 ILE ILE B . n 
B 1 560 THR 560 560 560 THR THR B . n 
B 1 561 LYS 561 561 561 LYS LYS B . n 
B 1 562 VAL 562 562 562 VAL VAL B . n 
B 1 563 PRO 563 563 563 PRO PRO B . n 
B 1 564 LEU 564 564 564 LEU LEU B . n 
B 1 565 HIS 565 565 565 HIS HIS B . n 
B 1 566 ALA 566 566 566 ALA ALA B . n 
B 1 567 PHE 567 567 567 PHE PHE B . n 
B 1 568 GLN 568 568 568 GLN GLN B . n 
B 1 569 ALA 569 569 569 ALA ALA B . n 
B 1 570 ASN 570 570 570 ASN ASN B . n 
B 1 571 ASN 571 571 571 ASN ASN B . n 
B 1 572 TYR 572 572 572 TYR TYR B . n 
B 1 573 PRO 573 573 573 PRO PRO B . n 
B 1 574 HIS 574 574 574 HIS HIS B . n 
B 1 575 ASP 575 575 575 ASP ASP B . n 
B 1 576 PHE 576 576 576 PHE PHE B . n 
B 1 577 VAL 577 577 577 VAL VAL B . n 
B 1 578 ASP 578 578 578 ASP ASP B . n 
B 1 579 CYS 579 579 579 CYS CYS B . n 
B 1 580 SER 580 580 580 SER SER B . n 
B 1 581 ALA 581 581 581 ALA ALA B . n 
B 1 582 ILE 582 582 582 ILE ILE B . n 
B 1 583 ASP 583 583 583 ASP ASP B . n 
B 1 584 LYS 584 584 584 LYS LYS B . n 
B 1 585 LEU 585 585 585 LEU LEU B . n 
B 1 586 ASP 586 586 586 ASP ASP B . n 
B 1 587 LEU 587 587 587 LEU LEU B . n 
B 1 588 SER 588 588 588 SER SER B . n 
B 1 589 PRO 589 589 589 PRO PRO B . n 
B 1 590 TRP 590 590 590 TRP TRP B . n 
B 1 591 ALA 591 591 591 ALA ALA B . n 
B 1 592 SER 592 592 592 SER SER B . n 
B 1 593 ARG 593 593 593 ARG ARG B . n 
B 1 594 GLU 594 594 594 GLU GLU B . n 
B 1 595 ASN 595 595 595 ASN ASN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2 NAG 1  596  1    NAG NAG A . 
D  2 NAG 2  597  2    NAG NAG A . 
E  2 NAG 1  598  3    NAG NAG A . 
F  2 NAG 2  599  4    NAG NAG A . 
G  2 NAG 1  600  5    NAG NAG A . 
H  2 NAG 2  601  6    NAG NAG A . 
I  3 MAN 3  602  7    MAN MAN A . 
J  2 NAG 1  603  8    NAG NAG A . 
K  4 CA  1  1001 1001 CA  CA  A . 
L  5 CO3 1  2001 2001 CO3 CO3 A . 
M  6 HEM 1  605  605  HEM HEM A . 
N  7 FMT 1  3001 3001 FMT FMT A . 
O  7 FMT 1  3002 3002 FMT FMT A . 
P  7 FMT 1  3003 3003 FMT FMT A . 
Q  2 NAG 1  596  1    NAG NAG B . 
R  2 NAG 2  597  2    NAG NAG B . 
S  2 NAG 1  598  3    NAG NAG B . 
T  2 NAG 2  599  4    NAG NAG B . 
U  2 NAG 1  600  5    NAG NAG B . 
V  2 NAG 2  601  6    NAG NAG B . 
W  3 MAN 3  602  7    MAN MAN B . 
X  2 NAG 1  603  8    NAG NAG B . 
Y  4 CA  1  1002 1002 CA  CA  B . 
Z  5 CO3 1  2002 2002 CO3 CO3 B . 
AA 6 HEM 1  605  605  HEM HEM B . 
BA 7 FMT 1  3004 3004 FMT FMT B . 
CA 7 FMT 1  3005 3005 FMT FMT B . 
DA 7 FMT 1  3006 3006 FMT FMT B . 
EA 8 HOH 1  3004 2    HOH HOH A . 
EA 8 HOH 2  3005 3    HOH HOH A . 
EA 8 HOH 3  3006 5    HOH HOH A . 
EA 8 HOH 4  3007 8    HOH HOH A . 
EA 8 HOH 5  3008 9    HOH HOH A . 
EA 8 HOH 6  3009 11   HOH HOH A . 
EA 8 HOH 7  3010 12   HOH HOH A . 
EA 8 HOH 8  3011 14   HOH HOH A . 
EA 8 HOH 9  3012 15   HOH HOH A . 
EA 8 HOH 10 3013 17   HOH HOH A . 
EA 8 HOH 11 3014 20   HOH HOH A . 
EA 8 HOH 12 3015 22   HOH HOH A . 
EA 8 HOH 13 3016 23   HOH HOH A . 
EA 8 HOH 14 3017 24   HOH HOH A . 
EA 8 HOH 15 3018 25   HOH HOH A . 
EA 8 HOH 16 3019 26   HOH HOH A . 
EA 8 HOH 17 3020 27   HOH HOH A . 
EA 8 HOH 18 3021 32   HOH HOH A . 
EA 8 HOH 19 3022 35   HOH HOH A . 
EA 8 HOH 20 3023 36   HOH HOH A . 
EA 8 HOH 21 3024 37   HOH HOH A . 
EA 8 HOH 22 3025 39   HOH HOH A . 
EA 8 HOH 23 3026 40   HOH HOH A . 
EA 8 HOH 24 3027 45   HOH HOH A . 
EA 8 HOH 25 3028 47   HOH HOH A . 
EA 8 HOH 26 3029 48   HOH HOH A . 
EA 8 HOH 27 3030 49   HOH HOH A . 
EA 8 HOH 28 3031 50   HOH HOH A . 
EA 8 HOH 29 3032 51   HOH HOH A . 
EA 8 HOH 30 3033 54   HOH HOH A . 
EA 8 HOH 31 3034 55   HOH HOH A . 
EA 8 HOH 32 3035 56   HOH HOH A . 
EA 8 HOH 33 3036 57   HOH HOH A . 
EA 8 HOH 34 3037 58   HOH HOH A . 
EA 8 HOH 35 3038 60   HOH HOH A . 
EA 8 HOH 36 3039 61   HOH HOH A . 
EA 8 HOH 37 3040 62   HOH HOH A . 
EA 8 HOH 38 3041 65   HOH HOH A . 
EA 8 HOH 39 3042 66   HOH HOH A . 
EA 8 HOH 40 3043 67   HOH HOH A . 
EA 8 HOH 41 3044 69   HOH HOH A . 
EA 8 HOH 42 3045 72   HOH HOH A . 
EA 8 HOH 43 3046 75   HOH HOH A . 
EA 8 HOH 44 3047 76   HOH HOH A . 
EA 8 HOH 45 3048 77   HOH HOH A . 
EA 8 HOH 46 3049 78   HOH HOH A . 
EA 8 HOH 47 3050 79   HOH HOH A . 
EA 8 HOH 48 3051 80   HOH HOH A . 
EA 8 HOH 49 3052 81   HOH HOH A . 
EA 8 HOH 50 3053 82   HOH HOH A . 
EA 8 HOH 51 3054 83   HOH HOH A . 
EA 8 HOH 52 3055 84   HOH HOH A . 
EA 8 HOH 53 3056 85   HOH HOH A . 
EA 8 HOH 54 3057 86   HOH HOH A . 
EA 8 HOH 55 3058 87   HOH HOH A . 
EA 8 HOH 56 3059 94   HOH HOH A . 
EA 8 HOH 57 3060 107  HOH HOH A . 
EA 8 HOH 58 3061 108  HOH HOH A . 
EA 8 HOH 59 3062 109  HOH HOH A . 
EA 8 HOH 60 3063 110  HOH HOH A . 
EA 8 HOH 61 3064 111  HOH HOH A . 
EA 8 HOH 62 3065 112  HOH HOH A . 
EA 8 HOH 63 3066 113  HOH HOH A . 
EA 8 HOH 64 3067 114  HOH HOH A . 
EA 8 HOH 65 3068 115  HOH HOH A . 
EA 8 HOH 66 3069 116  HOH HOH A . 
EA 8 HOH 67 3070 117  HOH HOH A . 
EA 8 HOH 68 3071 118  HOH HOH A . 
EA 8 HOH 69 3072 119  HOH HOH A . 
EA 8 HOH 70 3073 120  HOH HOH A . 
EA 8 HOH 71 3074 121  HOH HOH A . 
EA 8 HOH 72 3075 122  HOH HOH A . 
EA 8 HOH 73 3076 123  HOH HOH A . 
EA 8 HOH 74 3077 124  HOH HOH A . 
EA 8 HOH 75 3078 125  HOH HOH A . 
EA 8 HOH 76 3079 126  HOH HOH A . 
EA 8 HOH 77 3080 127  HOH HOH A . 
EA 8 HOH 78 3081 128  HOH HOH A . 
EA 8 HOH 79 3082 129  HOH HOH A . 
EA 8 HOH 80 3083 130  HOH HOH A . 
EA 8 HOH 81 3084 131  HOH HOH A . 
EA 8 HOH 82 3085 132  HOH HOH A . 
EA 8 HOH 83 3086 133  HOH HOH A . 
EA 8 HOH 84 3087 134  HOH HOH A . 
EA 8 HOH 85 3088 135  HOH HOH A . 
EA 8 HOH 86 3089 136  HOH HOH A . 
FA 8 HOH 1  3007 1    HOH HOH B . 
FA 8 HOH 2  3008 4    HOH HOH B . 
FA 8 HOH 3  3009 6    HOH HOH B . 
FA 8 HOH 4  3010 7    HOH HOH B . 
FA 8 HOH 5  3011 10   HOH HOH B . 
FA 8 HOH 6  3012 13   HOH HOH B . 
FA 8 HOH 7  3013 16   HOH HOH B . 
FA 8 HOH 8  3014 18   HOH HOH B . 
FA 8 HOH 9  3015 19   HOH HOH B . 
FA 8 HOH 10 3016 21   HOH HOH B . 
FA 8 HOH 11 3017 28   HOH HOH B . 
FA 8 HOH 12 3018 29   HOH HOH B . 
FA 8 HOH 13 3019 30   HOH HOH B . 
FA 8 HOH 14 3020 31   HOH HOH B . 
FA 8 HOH 15 3021 33   HOH HOH B . 
FA 8 HOH 16 3022 34   HOH HOH B . 
FA 8 HOH 17 3023 38   HOH HOH B . 
FA 8 HOH 18 3024 41   HOH HOH B . 
FA 8 HOH 19 3025 42   HOH HOH B . 
FA 8 HOH 20 3026 43   HOH HOH B . 
FA 8 HOH 21 3027 44   HOH HOH B . 
FA 8 HOH 22 3028 46   HOH HOH B . 
FA 8 HOH 23 3029 52   HOH HOH B . 
FA 8 HOH 24 3030 53   HOH HOH B . 
FA 8 HOH 25 3031 59   HOH HOH B . 
FA 8 HOH 26 3032 63   HOH HOH B . 
FA 8 HOH 27 3033 64   HOH HOH B . 
FA 8 HOH 28 3034 68   HOH HOH B . 
FA 8 HOH 29 3035 70   HOH HOH B . 
FA 8 HOH 30 3036 71   HOH HOH B . 
FA 8 HOH 31 3037 74   HOH HOH B . 
FA 8 HOH 32 3038 88   HOH HOH B . 
FA 8 HOH 33 3039 89   HOH HOH B . 
FA 8 HOH 34 3040 90   HOH HOH B . 
FA 8 HOH 35 3041 91   HOH HOH B . 
FA 8 HOH 36 3042 92   HOH HOH B . 
FA 8 HOH 37 3043 93   HOH HOH B . 
FA 8 HOH 38 3044 95   HOH HOH B . 
FA 8 HOH 39 3045 96   HOH HOH B . 
FA 8 HOH 40 3046 97   HOH HOH B . 
FA 8 HOH 41 3047 98   HOH HOH B . 
FA 8 HOH 42 3048 99   HOH HOH B . 
FA 8 HOH 43 3049 100  HOH HOH B . 
FA 8 HOH 44 3050 101  HOH HOH B . 
FA 8 HOH 45 3051 102  HOH HOH B . 
FA 8 HOH 46 3052 103  HOH HOH B . 
FA 8 HOH 47 3053 104  HOH HOH B . 
FA 8 HOH 48 3054 105  HOH HOH B . 
FA 8 HOH 49 3055 106  HOH HOH B . 
FA 8 HOH 50 3056 137  HOH HOH B . 
FA 8 HOH 51 3057 138  HOH HOH B . 
FA 8 HOH 52 3058 139  HOH HOH B . 
FA 8 HOH 53 3059 140  HOH HOH B . 
FA 8 HOH 54 3060 141  HOH HOH B . 
FA 8 HOH 55 3061 142  HOH HOH B . 
FA 8 HOH 56 3062 143  HOH HOH B . 
FA 8 HOH 57 3063 144  HOH HOH B . 
FA 8 HOH 58 3064 145  HOH HOH B . 
FA 8 HOH 59 3065 146  HOH HOH B . 
FA 8 HOH 60 3066 147  HOH HOH B . 
FA 8 HOH 61 3067 148  HOH HOH B . 
FA 8 HOH 62 3068 149  HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 95  A ASN 95  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 205 A ASN 205 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 241 A ASN 241 ? ASN 'GLYCOSYLATION SITE' 
4 A ASN 332 A ASN 332 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 95  B ASN 95  ? ASN 'GLYCOSYLATION SITE' 
6 B ASN 205 B ASN 205 ? ASN 'GLYCOSYLATION SITE' 
7 B ASN 241 B ASN 241 ? ASN 'GLYCOSYLATION SITE' 
8 B ASN 332 B ASN 332 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA 
# 
_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_
_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  NE2 ? A  HIS 351 ? A HIS 351 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 NA  ? M  HEM .   ? A HEM 605 ? 1_555 87.8  ? 
2  NE2 ? A  HIS 351 ? A HIS 351 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 NB  ? M  HEM .   ? A HEM 605 ? 1_555 94.3  ? 
3  NA  ? M  HEM .   ? A HEM 605 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 NB  ? M  HEM .   ? A HEM 605 ? 1_555 80.9  ? 
4  NE2 ? A  HIS 351 ? A HIS 351 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 NC  ? M  HEM .   ? A HEM 605 ? 1_555 103.3 ? 
5  NA  ? M  HEM .   ? A HEM 605 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 NC  ? M  HEM .   ? A HEM 605 ? 1_555 168.4 ? 
6  NB  ? M  HEM .   ? A HEM 605 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 NC  ? M  HEM .   ? A HEM 605 ? 1_555 95.0  ? 
7  NE2 ? A  HIS 351 ? A HIS 351 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 ND  ? M  HEM .   ? A HEM 605 ? 1_555 95.8  ? 
8  NA  ? M  HEM .   ? A HEM 605 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 ND  ? M  HEM .   ? A HEM 605 ? 1_555 99.4  ? 
9  NB  ? M  HEM .   ? A HEM 605 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 ND  ? M  HEM .   ? A HEM 605 ? 1_555 169.8 ? 
10 NC  ? M  HEM .   ? A HEM 605 ? 1_555 FE ? M  HEM . ? A HEM 605  ? 1_555 ND  ? M  HEM .   ? A HEM 605 ? 1_555 82.8  ? 
11 NE2 ? B  HIS 351 ? B HIS 351 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 NA  ? AA HEM .   ? B HEM 605 ? 1_555 103.0 ? 
12 NE2 ? B  HIS 351 ? B HIS 351 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 NB  ? AA HEM .   ? B HEM 605 ? 1_555 97.7  ? 
13 NA  ? AA HEM .   ? B HEM 605 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 NB  ? AA HEM .   ? B HEM 605 ? 1_555 81.2  ? 
14 NE2 ? B  HIS 351 ? B HIS 351 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 NC  ? AA HEM .   ? B HEM 605 ? 1_555 89.6  ? 
15 NA  ? AA HEM .   ? B HEM 605 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 NC  ? AA HEM .   ? B HEM 605 ? 1_555 167.3 ? 
16 NB  ? AA HEM .   ? B HEM 605 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 NC  ? AA HEM .   ? B HEM 605 ? 1_555 97.6  ? 
17 NE2 ? B  HIS 351 ? B HIS 351 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 ND  ? AA HEM .   ? B HEM 605 ? 1_555 93.3  ? 
18 NA  ? AA HEM .   ? B HEM 605 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 ND  ? AA HEM .   ? B HEM 605 ? 1_555 99.3  ? 
19 NB  ? AA HEM .   ? B HEM 605 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 ND  ? AA HEM .   ? B HEM 605 ? 1_555 168.6 ? 
20 NC  ? AA HEM .   ? B HEM 605 ? 1_555 FE ? AA HEM . ? B HEM 605  ? 1_555 ND  ? AA HEM .   ? B HEM 605 ? 1_555 79.4  ? 
21 O   ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OD1 ? A  ASP 110 ? A ASP 110 ? 1_555 63.9  ? 
22 O   ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 O   ? A  THR 184 ? A THR 184 ? 1_555 73.4  ? 
23 OD1 ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 O   ? A  THR 184 ? A THR 184 ? 1_555 132.3 ? 
24 O   ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG1 ? A  THR 184 ? A THR 184 ? 1_555 130.2 ? 
25 OD1 ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG1 ? A  THR 184 ? A THR 184 ? 1_555 156.8 ? 
26 O   ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG1 ? A  THR 184 ? A THR 184 ? 1_555 70.1  ? 
27 O   ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 O   ? A  PHE 186 ? A PHE 186 ? 1_555 107.3 ? 
28 OD1 ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 O   ? A  PHE 186 ? A PHE 186 ? 1_555 84.0  ? 
29 O   ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 O   ? A  PHE 186 ? A PHE 186 ? 1_555 89.4  ? 
30 OG1 ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 O   ? A  PHE 186 ? A PHE 186 ? 1_555 105.0 ? 
31 O   ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OD1 ? A  ASP 188 ? A ASP 188 ? 1_555 151.1 ? 
32 OD1 ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OD1 ? A  ASP 188 ? A ASP 188 ? 1_555 87.5  ? 
33 O   ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OD1 ? A  ASP 188 ? A ASP 188 ? 1_555 134.6 ? 
34 OG1 ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OD1 ? A  ASP 188 ? A ASP 188 ? 1_555 75.6  ? 
35 O   ? A  PHE 186 ? A PHE 186 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OD1 ? A  ASP 188 ? A ASP 188 ? 1_555 71.5  ? 
36 O   ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG  ? A  SER 190 ? A SER 190 ? 1_555 95.9  ? 
37 OD1 ? A  ASP 110 ? A ASP 110 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG  ? A  SER 190 ? A SER 190 ? 1_555 88.9  ? 
38 O   ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG  ? A  SER 190 ? A SER 190 ? 1_555 116.6 ? 
39 OG1 ? A  THR 184 ? A THR 184 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG  ? A  SER 190 ? A SER 190 ? 1_555 72.5  ? 
40 O   ? A  PHE 186 ? A PHE 186 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG  ? A  SER 190 ? A SER 190 ? 1_555 149.5 ? 
41 OD1 ? A  ASP 188 ? A ASP 188 ? 1_555 CA ? K  CA  . ? A CA  1001 ? 1_555 OG  ? A  SER 190 ? A SER 190 ? 1_555 78.6  ? 
42 O   ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OD1 ? B  ASP 110 ? B ASP 110 ? 1_555 58.5  ? 
43 O   ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 O   ? B  THR 184 ? B THR 184 ? 1_555 71.6  ? 
44 OD1 ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 O   ? B  THR 184 ? B THR 184 ? 1_555 110.6 ? 
45 O   ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG1 ? B  THR 184 ? B THR 184 ? 1_555 131.0 ? 
46 OD1 ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG1 ? B  THR 184 ? B THR 184 ? 1_555 168.1 ? 
47 O   ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG1 ? B  THR 184 ? B THR 184 ? 1_555 70.7  ? 
48 O   ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 O   ? B  PHE 186 ? B PHE 186 ? 1_555 111.6 ? 
49 OD1 ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 O   ? B  PHE 186 ? B PHE 186 ? 1_555 66.9  ? 
50 O   ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 O   ? B  PHE 186 ? B PHE 186 ? 1_555 94.1  ? 
51 OG1 ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 O   ? B  PHE 186 ? B PHE 186 ? 1_555 101.3 ? 
52 O   ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OD1 ? B  ASP 188 ? B ASP 188 ? 1_555 146.0 ? 
53 OD1 ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OD1 ? B  ASP 188 ? B ASP 188 ? 1_555 91.5  ? 
54 O   ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OD1 ? B  ASP 188 ? B ASP 188 ? 1_555 139.8 ? 
55 OG1 ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OD1 ? B  ASP 188 ? B ASP 188 ? 1_555 81.2  ? 
56 O   ? B  PHE 186 ? B PHE 186 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OD1 ? B  ASP 188 ? B ASP 188 ? 1_555 63.4  ? 
57 O   ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG  ? B  SER 190 ? B SER 190 ? 1_555 84.8  ? 
58 OD1 ? B  ASP 110 ? B ASP 110 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG  ? B  SER 190 ? B SER 190 ? 1_555 98.8  ? 
59 O   ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG  ? B  SER 190 ? B SER 190 ? 1_555 122.5 ? 
60 OG1 ? B  THR 184 ? B THR 184 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG  ? B  SER 190 ? B SER 190 ? 1_555 90.0  ? 
61 O   ? B  PHE 186 ? B PHE 186 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG  ? B  SER 190 ? B SER 190 ? 1_555 143.3 ? 
62 OD1 ? B  ASP 188 ? B ASP 188 ? 1_555 CA ? Y  CA  . ? B CA  1002 ? 1_555 OG  ? B  SER 190 ? B SER 190 ? 1_555 84.5  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2006-10-17 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-18 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Non-polymer description'   
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_software.name' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS       refinement        0.9    ? 1 
MAR345    'data collection' 345DTB ? 2 
DENZO     'data reduction'  .      ? 3 
SCALEPACK 'data scaling'    .      ? 4 
AMoRE     phasing           .      ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   C 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    233 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   CD 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   PRO 
_pdbx_validate_close_contact.auth_seq_id_2    234 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.76 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 N A PRO 9   ? ? CA A PRO 9   ? ? 1.581 1.468 0.113 0.017 N 
2 1 N A ILE 24  ? ? CA A ILE 24  ? ? 1.595 1.459 0.136 0.020 N 
3 1 N A TYR 172 ? ? CA A TYR 172 ? ? 1.583 1.459 0.124 0.020 N 
4 1 N B ARG 67  ? ? CA B ARG 67  ? ? 1.827 1.459 0.368 0.020 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N  A ILE 24  ? ? CA A ILE 24  ? ? C   A ILE 24  ? ? 130.54 111.00 19.54  2.70 N 
2  1 CA A PRO 48  ? ? N  A PRO 48  ? ? CD  A PRO 48  ? ? 103.05 111.70 -8.65  1.40 N 
3  1 CB A LEU 86  ? ? CA A LEU 86  ? ? C   A LEU 86  ? ? 98.63  110.20 -11.57 1.90 N 
4  1 CA A PRO 115 ? ? N  A PRO 115 ? ? CD  A PRO 115 ? ? 102.71 111.70 -8.99  1.40 N 
5  1 C  A PRO 115 ? ? N  A GLU 116 ? ? CA  A GLU 116 ? ? 105.33 121.70 -16.37 2.50 Y 
6  1 C  A PHE 144 ? ? N  A PRO 145 ? ? CD  A PRO 145 ? ? 114.89 128.40 -13.51 2.10 Y 
7  1 CA A PRO 149 ? ? N  A PRO 149 ? ? CD  A PRO 149 ? ? 101.79 111.70 -9.91  1.40 N 
8  1 N  A VAL 166 ? ? CA A VAL 166 ? ? C   A VAL 166 ? ? 130.79 111.00 19.79  2.70 N 
9  1 C  A CYS 167 ? ? N  A PRO 168 ? ? CD  A PRO 168 ? ? 106.35 128.40 -22.05 2.10 Y 
10 1 C  A PRO 170 ? ? N  A PRO 171 ? ? CD  A PRO 171 ? ? 109.51 128.40 -18.89 2.10 Y 
11 1 N  A PRO 171 ? ? CA A PRO 171 ? ? C   A PRO 171 ? ? 137.59 112.10 25.49  2.60 N 
12 1 CA A PRO 171 ? ? C  A PRO 171 ? ? N   A TYR 172 ? ? 141.44 117.20 24.24  2.20 Y 
13 1 O  A PRO 171 ? ? C  A PRO 171 ? ? N   A TYR 172 ? ? 110.31 122.70 -12.39 1.60 Y 
14 1 CB A TYR 172 ? ? CA A TYR 172 ? ? C   A TYR 172 ? ? 93.74  110.40 -16.66 2.00 N 
15 1 CA A TYR 172 ? ? CB A TYR 172 ? ? CG  A TYR 172 ? ? 133.12 113.40 19.72  1.90 N 
16 1 CB A TYR 172 ? ? CG A TYR 172 ? ? CD2 A TYR 172 ? ? 112.20 121.00 -8.80  0.60 N 
17 1 CB A TYR 172 ? ? CG A TYR 172 ? ? CD1 A TYR 172 ? ? 129.62 121.00 8.62   0.60 N 
18 1 N  A GLN 173 ? ? CA A GLN 173 ? ? C   A GLN 173 ? ? 131.75 111.00 20.75  2.70 N 
19 1 C  A SER 208 ? ? N  A PRO 209 ? ? CD  A PRO 209 ? ? 109.26 128.40 -19.14 2.10 Y 
20 1 CA A PRO 209 ? ? N  A PRO 209 ? ? CD  A PRO 209 ? ? 99.73  111.70 -11.97 1.40 N 
21 1 C  A LYS 233 ? ? N  A PRO 234 ? ? CA  A PRO 234 ? ? 137.04 119.30 17.74  1.50 Y 
22 1 C  A LYS 233 ? ? N  A PRO 234 ? ? CD  A PRO 234 ? ? 88.09  128.40 -40.31 2.10 Y 
23 1 CA A PRO 234 ? ? N  A PRO 234 ? ? CD  A PRO 234 ? ? 101.92 111.70 -9.78  1.40 N 
24 1 N  B GLY 7   ? ? CA B GLY 7   ? ? C   B GLY 7   ? ? 131.17 113.10 18.07  2.50 N 
25 1 C  B THR 66  ? ? N  B ARG 67  ? ? CA  B ARG 67  ? ? 99.01  121.70 -22.69 2.50 Y 
26 1 N  B ARG 67  ? ? CA B ARG 67  ? ? CB  B ARG 67  ? ? 79.85  110.60 -30.75 1.80 N 
27 1 N  B LEU 119 ? ? CA B LEU 119 ? ? C   B LEU 119 ? ? 91.91  111.00 -19.09 2.70 N 
28 1 CB B SER 122 ? ? CA B SER 122 ? ? C   B SER 122 ? ? 124.40 110.10 14.30  1.90 N 
29 1 N  B SER 122 ? ? CA B SER 122 ? ? C   B SER 122 ? ? 93.35  111.00 -17.65 2.70 N 
30 1 CA B HIS 124 ? ? CB B HIS 124 ? ? CG  B HIS 124 ? ? 126.27 113.60 12.67  1.70 N 
31 1 CB B HIS 124 ? ? CG B HIS 124 ? ? CD2 B HIS 124 ? ? 138.98 131.40 7.58   1.20 N 
32 1 C  B PRO 171 ? ? N  B TYR 172 ? ? CA  B TYR 172 ? ? 138.81 121.70 17.11  2.50 Y 
33 1 N  B SER 174 ? ? CA B SER 174 ? ? C   B SER 174 ? ? 130.12 111.00 19.12  2.70 N 
34 1 C  B LYS 233 ? ? N  B PRO 234 ? ? CA  B PRO 234 ? ? 165.67 119.30 46.37  1.50 Y 
35 1 C  B LYS 233 ? ? N  B PRO 234 ? ? CD  B PRO 234 ? ? 78.12  128.40 -50.28 2.10 Y 
36 1 CA B PRO 234 ? ? N  B PRO 234 ? ? CD  B PRO 234 ? ? 100.00 111.70 -11.70 1.40 N 
37 1 CA B PRO 375 ? ? N  B PRO 375 ? ? CD  B PRO 375 ? ? 102.62 111.70 -9.08  1.40 N 
38 1 CB B ASN 571 ? ? CA B ASN 571 ? ? C   B ASN 571 ? ? 133.01 110.40 22.61  2.00 N 
39 1 CA B PRO 573 ? ? N  B PRO 573 ? ? CD  B PRO 573 ? ? 92.10  111.70 -19.60 1.40 N 
40 1 N  B PRO 573 ? ? CA B PRO 573 ? ? C   B PRO 573 ? ? 130.41 112.10 18.31  2.60 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 PRO A 9   ? ? -49.79  91.40   
2   1 GLU A 17  ? ? 99.46   -6.57   
3   1 ASN A 18  ? ? -143.72 23.99   
4   1 CYS A 28  ? ? 80.59   -2.91   
5   1 ASN A 40  ? ? 74.18   30.17   
6   1 LEU A 43  ? ? 21.23   103.97  
7   1 ALA A 44  ? ? -29.85  132.17  
8   1 LEU A 55  ? ? -141.40 -44.25  
9   1 ALA A 56  ? ? -160.06 -12.90  
10  1 GLN A 63  ? ? -69.77  26.26   
11  1 ARG A 64  ? ? -157.35 -20.50  
12  1 ASN A 68  ? ? 48.68   24.30   
13  1 THR A 117 ? ? -56.50  -105.90 
14  1 LEU A 119 ? ? -112.67 -93.29  
15  1 SER A 121 ? ? 82.40   88.21   
16  1 SER A 122 ? ? 62.50   85.00   
17  1 GLU A 131 ? ? -148.69 -48.90  
18  1 ASP A 137 ? ? 43.14   -25.72  
19  1 PRO A 145 ? ? -59.85  175.43  
20  1 PHE A 160 ? ? -165.06 116.58  
21  1 VAL A 166 ? ? -63.13  8.94    
22  1 PRO A 168 ? ? -70.63  -140.91 
23  1 THR A 169 ? ? -176.96 -69.46  
24  1 PRO A 170 ? ? -54.39  -166.33 
25  1 PRO A 171 ? ? -64.52  49.27   
26  1 TYR A 172 ? ? -139.61 -96.48  
27  1 GLN A 173 ? ? -140.26 -136.06 
28  1 SER A 174 ? ? 13.32   -53.74  
29  1 MET A 232 ? ? -7.48   105.63  
30  1 PRO A 234 ? ? 78.31   53.72   
31  1 ARG A 245 ? ? 61.47   63.76   
32  1 ALA A 256 ? ? -27.46  -32.77  
33  1 GLN A 294 ? ? 62.67   -12.99  
34  1 ARG A 348 ? ? -66.51  6.33    
35  1 GLU A 363 ? ? -49.46  0.79    
36  1 ILE A 386 ? ? -99.95  -72.11  
37  1 ASP A 389 ? ? -110.71 57.63   
38  1 SER A 404 ? ? -76.57  -169.80 
39  1 GLN A 409 ? ? -33.08  -13.05  
40  1 LYS A 420 ? ? -108.35 40.14   
41  1 HIS A 429 ? ? -104.72 44.71   
42  1 SER A 459 ? ? -39.70  133.75  
43  1 LYS A 474 ? ? -59.57  -70.40  
44  1 LYS A 485 ? ? 64.85   -22.12  
45  1 ARG A 504 ? ? 39.58   23.69   
46  1 HIS A 565 ? ? -110.47 75.05   
47  1 ALA A 566 ? ? -52.94  -4.69   
48  1 ASP A 583 ? ? -46.07  167.78  
49  1 LEU A 585 ? ? 64.02   86.91   
50  1 GLU A 594 ? ? 5.68    -93.96  
51  1 GLU B 3   ? ? -81.16  39.03   
52  1 VAL B 4   ? ? -51.88  79.28   
53  1 ALA B 8   ? ? 160.46  141.89  
54  1 PRO B 9   ? ? -74.34  -83.19  
55  1 VAL B 10  ? ? 64.89   117.37  
56  1 PRO B 11  ? ? -53.02  108.32  
57  1 CYS B 15  ? ? 68.32   174.87  
58  1 ASP B 16  ? ? -102.97 -84.69  
59  1 GLU B 17  ? ? 163.00  -75.75  
60  1 SER B 19  ? ? -39.03  133.97  
61  1 CYS B 28  ? ? 66.08   -3.95   
62  1 PRO B 34  ? ? -55.65  -70.72  
63  1 ALA B 35  ? ? -56.24  -1.98   
64  1 ASN B 40  ? ? 71.58   33.40   
65  1 ALA B 56  ? ? -157.16 -9.70   
66  1 TRP B 61  ? ? -93.91  -62.44  
67  1 GLN B 63  ? ? -8.40   -60.57  
68  1 ARG B 64  ? ? -61.61  28.56   
69  1 PHE B 113 ? ? -169.67 107.60  
70  1 SER B 121 ? ? -154.52 17.13   
71  1 SER B 122 ? ? -144.79 -64.47  
72  1 GLU B 123 ? ? 6.46    147.12  
73  1 ASP B 137 ? ? 59.64   -143.41 
74  1 ASN B 147 ? ? 34.91   47.86   
75  1 CYS B 167 ? ? 70.57   -147.13 
76  1 PRO B 168 ? ? -62.68  -106.64 
77  1 THR B 169 ? ? 172.59  -36.22  
78  1 PRO B 170 ? ? -63.07  -157.44 
79  1 PRO B 171 ? ? -37.87  43.04   
80  1 TYR B 172 ? ? -17.30  142.77  
81  1 GLN B 173 ? ? -155.67 -133.20 
82  1 SER B 174 ? ? 21.78   -85.15  
83  1 SER B 185 ? ? -65.89  0.75    
84  1 LEU B 187 ? ? -68.75  68.63   
85  1 ASN B 205 ? ? -67.18  99.31   
86  1 LEU B 210 ? ? -142.60 37.94   
87  1 ASN B 231 ? ? -65.71  -90.70  
88  1 MET B 232 ? ? -14.04  123.04  
89  1 PRO B 234 ? ? 93.70   60.80   
90  1 ALA B 256 ? ? -39.34  -30.34  
91  1 ILE B 260 ? ? -38.89  -30.14  
92  1 ASN B 284 ? ? -118.21 71.77   
93  1 VAL B 316 ? ? -108.48 -60.03  
94  1 ILE B 325 ? ? -112.99 68.52   
95  1 PRO B 326 ? ? -48.22  157.66  
96  1 GLN B 329 ? ? -146.30 46.63   
97  1 ASN B 333 ? ? -38.97  -26.22  
98  1 SER B 334 ? ? -107.31 56.14   
99  1 ASP B 336 ? ? -55.82  99.15   
100 1 GLU B 363 ? ? -21.61  -28.26  
101 1 PRO B 367 ? ? -54.83  106.67  
102 1 ILE B 386 ? ? -101.68 -60.79  
103 1 LYS B 388 ? ? -99.96  30.29   
104 1 ASP B 389 ? ? -161.25 70.15   
105 1 LYS B 411 ? ? -174.83 71.30   
106 1 ASN B 419 ? ? -145.85 -27.70  
107 1 HIS B 429 ? ? -105.26 47.59   
108 1 PHE B 455 ? ? -35.99  -27.88  
109 1 LYS B 462 ? ? -132.07 -37.09  
110 1 ASN B 473 ? ? 174.22  118.66  
111 1 LYS B 485 ? ? 77.57   -18.05  
112 1 HIS B 565 ? ? -115.87 79.50   
113 1 ALA B 566 ? ? -48.48  -16.43  
114 1 SER B 580 ? ? -63.89  5.98    
115 1 ASP B 583 ? ? -44.73  158.87  
116 1 LEU B 585 ? ? 66.85   87.29   
117 1 GLU B 594 ? ? -59.25  -85.89  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASN 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              570 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   10.86 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE            NAG 
3 ALPHA-D-MANNOSE                   MAN 
4 'CALCIUM ION'                     CA  
5 'CARBONATE ION'                   CO3 
6 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
7 'FORMIC ACID'                     FMT 
8 water                             HOH 
# 
