data_5HZ1
# 
_entry.id   5HZ1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5HZ1         
WWPDB D_1000217985 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 5HZ3 unspecified 
PDB . 5HZ0 unspecified 
PDB . 5HYX unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5HZ1 
_pdbx_database_status.recvd_initial_deposition_date   2016-02-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Song, W.' 1 ? 
'Han, Z.'  2 ? 
'Chai, J.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Plant Receptor' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Song, W.' 1 
primary 'Han, Z.'  2 
primary 'Chai, J.' 3 
# 
_cell.length_a           183.466 
_cell.length_b           183.466 
_cell.length_c           87.610 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.entry_id           5HZ1 
_cell.Z_PDB              9 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.entry_id                         5HZ1 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Probable LRR receptor-like serine/threonine-protein kinase At4g26540' 69202.875 1 2.7.11.1 
'V64T, G81E, M82K, D83Q, N104Q' 'UNP residues 57-689' ? 
2 polymer     syn ASP-PTR-TRP-ARG-ALA-LYS-HIS-HIS-PRO-HYP-LYS-ASN-ASN                    1763.826  1 ?        ? ? ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                                                 221.208   4 ?        ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;CNWTGVKCNRRGEVSEIQLKEKQLQGSLPVTSLRSLKSLTSLTLSSLQLTGVIPKEIGDFTELELLDLSDNSLSGDIPVE
IFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENL
VMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQN
NLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEELTNCTKLTHLEIDNNLITGEIPS
LMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSGFIPPDIGNCTNL
YRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNA
LSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIPDELGQIPSLAISLNLSCNRFVGEIPS
RFSDLKNLGVLDVSHNQLTGNLNVLTDLQNLVSLNISYNDFSGDLPNTPFFRRLPLSDLASNRGLYISNAIST
;
;CNWTGVKCNRRGEVSEIQLKEKQLQGSLPVTSLRSLKSLTSLTLSSLQLTGVIPKEIGDFTELELLDLSDNSLSGDIPVE
IFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENL
VMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQN
NLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEELTNCTKLTHLEIDNNLITGEIPS
LMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSGFIPPDIGNCTNL
YRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNA
LSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIPDELGQIPSLAISLNLSCNRFVGEIPS
RFSDLKNLGVLDVSHNQLTGNLNVLTDLQNLVSLNISYNDFSGDLPNTPFFRRLPLSDLASNRGLYISNAIST
;
B ? 
2 'polypeptide(L)' no yes 'D(PTR)WRAKHHP(HZP)KNN' DYWRAKHHPPKNN A ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   ASN n 
1 3   TRP n 
1 4   THR n 
1 5   GLY n 
1 6   VAL n 
1 7   LYS n 
1 8   CYS n 
1 9   ASN n 
1 10  ARG n 
1 11  ARG n 
1 12  GLY n 
1 13  GLU n 
1 14  VAL n 
1 15  SER n 
1 16  GLU n 
1 17  ILE n 
1 18  GLN n 
1 19  LEU n 
1 20  LYS n 
1 21  GLU n 
1 22  LYS n 
1 23  GLN n 
1 24  LEU n 
1 25  GLN n 
1 26  GLY n 
1 27  SER n 
1 28  LEU n 
1 29  PRO n 
1 30  VAL n 
1 31  THR n 
1 32  SER n 
1 33  LEU n 
1 34  ARG n 
1 35  SER n 
1 36  LEU n 
1 37  LYS n 
1 38  SER n 
1 39  LEU n 
1 40  THR n 
1 41  SER n 
1 42  LEU n 
1 43  THR n 
1 44  LEU n 
1 45  SER n 
1 46  SER n 
1 47  LEU n 
1 48  GLN n 
1 49  LEU n 
1 50  THR n 
1 51  GLY n 
1 52  VAL n 
1 53  ILE n 
1 54  PRO n 
1 55  LYS n 
1 56  GLU n 
1 57  ILE n 
1 58  GLY n 
1 59  ASP n 
1 60  PHE n 
1 61  THR n 
1 62  GLU n 
1 63  LEU n 
1 64  GLU n 
1 65  LEU n 
1 66  LEU n 
1 67  ASP n 
1 68  LEU n 
1 69  SER n 
1 70  ASP n 
1 71  ASN n 
1 72  SER n 
1 73  LEU n 
1 74  SER n 
1 75  GLY n 
1 76  ASP n 
1 77  ILE n 
1 78  PRO n 
1 79  VAL n 
1 80  GLU n 
1 81  ILE n 
1 82  PHE n 
1 83  ARG n 
1 84  LEU n 
1 85  LYS n 
1 86  LYS n 
1 87  LEU n 
1 88  LYS n 
1 89  THR n 
1 90  LEU n 
1 91  SER n 
1 92  LEU n 
1 93  ASN n 
1 94  THR n 
1 95  ASN n 
1 96  ASN n 
1 97  LEU n 
1 98  GLU n 
1 99  GLY n 
1 100 HIS n 
1 101 ILE n 
1 102 PRO n 
1 103 MET n 
1 104 GLU n 
1 105 ILE n 
1 106 GLY n 
1 107 ASN n 
1 108 LEU n 
1 109 SER n 
1 110 GLY n 
1 111 LEU n 
1 112 VAL n 
1 113 GLU n 
1 114 LEU n 
1 115 MET n 
1 116 LEU n 
1 117 PHE n 
1 118 ASP n 
1 119 ASN n 
1 120 LYS n 
1 121 LEU n 
1 122 SER n 
1 123 GLY n 
1 124 GLU n 
1 125 ILE n 
1 126 PRO n 
1 127 ARG n 
1 128 SER n 
1 129 ILE n 
1 130 GLY n 
1 131 GLU n 
1 132 LEU n 
1 133 LYS n 
1 134 ASN n 
1 135 LEU n 
1 136 GLN n 
1 137 VAL n 
1 138 LEU n 
1 139 ARG n 
1 140 ALA n 
1 141 GLY n 
1 142 GLY n 
1 143 ASN n 
1 144 LYS n 
1 145 ASN n 
1 146 LEU n 
1 147 ARG n 
1 148 GLY n 
1 149 GLU n 
1 150 LEU n 
1 151 PRO n 
1 152 TRP n 
1 153 GLU n 
1 154 ILE n 
1 155 GLY n 
1 156 ASN n 
1 157 CYS n 
1 158 GLU n 
1 159 ASN n 
1 160 LEU n 
1 161 VAL n 
1 162 MET n 
1 163 LEU n 
1 164 GLY n 
1 165 LEU n 
1 166 ALA n 
1 167 GLU n 
1 168 THR n 
1 169 SER n 
1 170 LEU n 
1 171 SER n 
1 172 GLY n 
1 173 LYS n 
1 174 LEU n 
1 175 PRO n 
1 176 ALA n 
1 177 SER n 
1 178 ILE n 
1 179 GLY n 
1 180 ASN n 
1 181 LEU n 
1 182 LYS n 
1 183 ARG n 
1 184 VAL n 
1 185 GLN n 
1 186 THR n 
1 187 ILE n 
1 188 ALA n 
1 189 ILE n 
1 190 TYR n 
1 191 THR n 
1 192 SER n 
1 193 LEU n 
1 194 LEU n 
1 195 SER n 
1 196 GLY n 
1 197 PRO n 
1 198 ILE n 
1 199 PRO n 
1 200 ASP n 
1 201 GLU n 
1 202 ILE n 
1 203 GLY n 
1 204 TYR n 
1 205 CYS n 
1 206 THR n 
1 207 GLU n 
1 208 LEU n 
1 209 GLN n 
1 210 ASN n 
1 211 LEU n 
1 212 TYR n 
1 213 LEU n 
1 214 TYR n 
1 215 GLN n 
1 216 ASN n 
1 217 SER n 
1 218 ILE n 
1 219 SER n 
1 220 GLY n 
1 221 SER n 
1 222 ILE n 
1 223 PRO n 
1 224 THR n 
1 225 THR n 
1 226 ILE n 
1 227 GLY n 
1 228 GLY n 
1 229 LEU n 
1 230 LYS n 
1 231 LYS n 
1 232 LEU n 
1 233 GLN n 
1 234 SER n 
1 235 LEU n 
1 236 LEU n 
1 237 LEU n 
1 238 TRP n 
1 239 GLN n 
1 240 ASN n 
1 241 ASN n 
1 242 LEU n 
1 243 VAL n 
1 244 GLY n 
1 245 LYS n 
1 246 ILE n 
1 247 PRO n 
1 248 THR n 
1 249 GLU n 
1 250 LEU n 
1 251 GLY n 
1 252 ASN n 
1 253 CYS n 
1 254 PRO n 
1 255 GLU n 
1 256 LEU n 
1 257 TRP n 
1 258 LEU n 
1 259 ILE n 
1 260 ASP n 
1 261 PHE n 
1 262 SER n 
1 263 GLU n 
1 264 ASN n 
1 265 LEU n 
1 266 LEU n 
1 267 THR n 
1 268 GLY n 
1 269 THR n 
1 270 ILE n 
1 271 PRO n 
1 272 ARG n 
1 273 SER n 
1 274 PHE n 
1 275 GLY n 
1 276 LYS n 
1 277 LEU n 
1 278 GLU n 
1 279 ASN n 
1 280 LEU n 
1 281 GLN n 
1 282 GLU n 
1 283 LEU n 
1 284 GLN n 
1 285 LEU n 
1 286 SER n 
1 287 VAL n 
1 288 ASN n 
1 289 GLN n 
1 290 ILE n 
1 291 SER n 
1 292 GLY n 
1 293 THR n 
1 294 ILE n 
1 295 PRO n 
1 296 GLU n 
1 297 GLU n 
1 298 LEU n 
1 299 THR n 
1 300 ASN n 
1 301 CYS n 
1 302 THR n 
1 303 LYS n 
1 304 LEU n 
1 305 THR n 
1 306 HIS n 
1 307 LEU n 
1 308 GLU n 
1 309 ILE n 
1 310 ASP n 
1 311 ASN n 
1 312 ASN n 
1 313 LEU n 
1 314 ILE n 
1 315 THR n 
1 316 GLY n 
1 317 GLU n 
1 318 ILE n 
1 319 PRO n 
1 320 SER n 
1 321 LEU n 
1 322 MET n 
1 323 SER n 
1 324 ASN n 
1 325 LEU n 
1 326 ARG n 
1 327 SER n 
1 328 LEU n 
1 329 THR n 
1 330 MET n 
1 331 PHE n 
1 332 PHE n 
1 333 ALA n 
1 334 TRP n 
1 335 GLN n 
1 336 ASN n 
1 337 LYS n 
1 338 LEU n 
1 339 THR n 
1 340 GLY n 
1 341 ASN n 
1 342 ILE n 
1 343 PRO n 
1 344 GLN n 
1 345 SER n 
1 346 LEU n 
1 347 SER n 
1 348 GLN n 
1 349 CYS n 
1 350 ARG n 
1 351 GLU n 
1 352 LEU n 
1 353 GLN n 
1 354 ALA n 
1 355 ILE n 
1 356 ASP n 
1 357 LEU n 
1 358 SER n 
1 359 TYR n 
1 360 ASN n 
1 361 SER n 
1 362 LEU n 
1 363 SER n 
1 364 GLY n 
1 365 SER n 
1 366 ILE n 
1 367 PRO n 
1 368 LYS n 
1 369 GLU n 
1 370 ILE n 
1 371 PHE n 
1 372 GLY n 
1 373 LEU n 
1 374 ARG n 
1 375 ASN n 
1 376 LEU n 
1 377 THR n 
1 378 LYS n 
1 379 LEU n 
1 380 LEU n 
1 381 LEU n 
1 382 LEU n 
1 383 SER n 
1 384 ASN n 
1 385 ASP n 
1 386 LEU n 
1 387 SER n 
1 388 GLY n 
1 389 PHE n 
1 390 ILE n 
1 391 PRO n 
1 392 PRO n 
1 393 ASP n 
1 394 ILE n 
1 395 GLY n 
1 396 ASN n 
1 397 CYS n 
1 398 THR n 
1 399 ASN n 
1 400 LEU n 
1 401 TYR n 
1 402 ARG n 
1 403 LEU n 
1 404 ARG n 
1 405 LEU n 
1 406 ASN n 
1 407 GLY n 
1 408 ASN n 
1 409 ARG n 
1 410 LEU n 
1 411 ALA n 
1 412 GLY n 
1 413 SER n 
1 414 ILE n 
1 415 PRO n 
1 416 SER n 
1 417 GLU n 
1 418 ILE n 
1 419 GLY n 
1 420 ASN n 
1 421 LEU n 
1 422 LYS n 
1 423 ASN n 
1 424 LEU n 
1 425 ASN n 
1 426 PHE n 
1 427 VAL n 
1 428 ASP n 
1 429 ILE n 
1 430 SER n 
1 431 GLU n 
1 432 ASN n 
1 433 ARG n 
1 434 LEU n 
1 435 VAL n 
1 436 GLY n 
1 437 SER n 
1 438 ILE n 
1 439 PRO n 
1 440 PRO n 
1 441 ALA n 
1 442 ILE n 
1 443 SER n 
1 444 GLY n 
1 445 CYS n 
1 446 GLU n 
1 447 SER n 
1 448 LEU n 
1 449 GLU n 
1 450 PHE n 
1 451 LEU n 
1 452 ASP n 
1 453 LEU n 
1 454 HIS n 
1 455 THR n 
1 456 ASN n 
1 457 SER n 
1 458 LEU n 
1 459 SER n 
1 460 GLY n 
1 461 SER n 
1 462 LEU n 
1 463 LEU n 
1 464 GLY n 
1 465 THR n 
1 466 THR n 
1 467 LEU n 
1 468 PRO n 
1 469 LYS n 
1 470 SER n 
1 471 LEU n 
1 472 LYS n 
1 473 PHE n 
1 474 ILE n 
1 475 ASP n 
1 476 PHE n 
1 477 SER n 
1 478 ASP n 
1 479 ASN n 
1 480 ALA n 
1 481 LEU n 
1 482 SER n 
1 483 SER n 
1 484 THR n 
1 485 LEU n 
1 486 PRO n 
1 487 PRO n 
1 488 GLY n 
1 489 ILE n 
1 490 GLY n 
1 491 LEU n 
1 492 LEU n 
1 493 THR n 
1 494 GLU n 
1 495 LEU n 
1 496 THR n 
1 497 LYS n 
1 498 LEU n 
1 499 ASN n 
1 500 LEU n 
1 501 ALA n 
1 502 LYS n 
1 503 ASN n 
1 504 ARG n 
1 505 LEU n 
1 506 SER n 
1 507 GLY n 
1 508 GLU n 
1 509 ILE n 
1 510 PRO n 
1 511 ARG n 
1 512 GLU n 
1 513 ILE n 
1 514 SER n 
1 515 THR n 
1 516 CYS n 
1 517 ARG n 
1 518 SER n 
1 519 LEU n 
1 520 GLN n 
1 521 LEU n 
1 522 LEU n 
1 523 ASN n 
1 524 LEU n 
1 525 GLY n 
1 526 GLU n 
1 527 ASN n 
1 528 ASP n 
1 529 PHE n 
1 530 SER n 
1 531 GLY n 
1 532 GLU n 
1 533 ILE n 
1 534 PRO n 
1 535 ASP n 
1 536 GLU n 
1 537 LEU n 
1 538 GLY n 
1 539 GLN n 
1 540 ILE n 
1 541 PRO n 
1 542 SER n 
1 543 LEU n 
1 544 ALA n 
1 545 ILE n 
1 546 SER n 
1 547 LEU n 
1 548 ASN n 
1 549 LEU n 
1 550 SER n 
1 551 CYS n 
1 552 ASN n 
1 553 ARG n 
1 554 PHE n 
1 555 VAL n 
1 556 GLY n 
1 557 GLU n 
1 558 ILE n 
1 559 PRO n 
1 560 SER n 
1 561 ARG n 
1 562 PHE n 
1 563 SER n 
1 564 ASP n 
1 565 LEU n 
1 566 LYS n 
1 567 ASN n 
1 568 LEU n 
1 569 GLY n 
1 570 VAL n 
1 571 LEU n 
1 572 ASP n 
1 573 VAL n 
1 574 SER n 
1 575 HIS n 
1 576 ASN n 
1 577 GLN n 
1 578 LEU n 
1 579 THR n 
1 580 GLY n 
1 581 ASN n 
1 582 LEU n 
1 583 ASN n 
1 584 VAL n 
1 585 LEU n 
1 586 THR n 
1 587 ASP n 
1 588 LEU n 
1 589 GLN n 
1 590 ASN n 
1 591 LEU n 
1 592 VAL n 
1 593 SER n 
1 594 LEU n 
1 595 ASN n 
1 596 ILE n 
1 597 SER n 
1 598 TYR n 
1 599 ASN n 
1 600 ASP n 
1 601 PHE n 
1 602 SER n 
1 603 GLY n 
1 604 ASP n 
1 605 LEU n 
1 606 PRO n 
1 607 ASN n 
1 608 THR n 
1 609 PRO n 
1 610 PHE n 
1 611 PHE n 
1 612 ARG n 
1 613 ARG n 
1 614 LEU n 
1 615 PRO n 
1 616 LEU n 
1 617 SER n 
1 618 ASP n 
1 619 LEU n 
1 620 ALA n 
1 621 SER n 
1 622 ASN n 
1 623 ARG n 
1 624 GLY n 
1 625 LEU n 
1 626 TYR n 
1 627 ILE n 
1 628 SER n 
1 629 ASN n 
1 630 ALA n 
1 631 ILE n 
1 632 SER n 
1 633 THR n 
2 1   ASP n 
2 2   PTR n 
2 3   TRP n 
2 4   ARG n 
2 5   ALA n 
2 6   LYS n 
2 7   HIS n 
2 8   HIS n 
2 9   PRO n 
2 10  HZP n 
2 11  LYS n 
2 12  ASN n 
2 13  ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   633 
_entity_src_gen.gene_src_common_name               'Mouse-ear cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'At4g26540, M3E9.30' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Insect cell expression vector pTIE1' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     266783 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       13 
_pdbx_entity_src_syn.organism_scientific    Arabidopsis 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       3701 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Y4265_ARATH C0LGR3 ? 1 
;CNWVGVKCNRRGEVSEIQLKGMDLQGSLPVTSLRSLKSLTSLTLSSLNLTGVIPKEIGDFTELELLDLSDNSLSGDIPVE
IFRLKKLKTLSLNTNNLEGHIPMEIGNLSGLVELMLFDNKLSGEIPRSIGELKNLQVLRAGGNKNLRGELPWEIGNCENL
VMLGLAETSLSGKLPASIGNLKRVQTIAIYTSLLSGPIPDEIGYCTELQNLYLYQNSISGSIPTTIGGLKKLQSLLLWQN
NLVGKIPTELGNCPELWLIDFSENLLTGTIPRSFGKLENLQELQLSVNQISGTIPEELTNCTKLTHLEIDNNLITGEIPS
LMSNLRSLTMFFAWQNKLTGNIPQSLSQCRELQAIDLSYNSLSGSIPKEIFGLRNLTKLLLLSNDLSGFIPPDIGNCTNL
YRLRLNGNRLAGSIPSEIGNLKNLNFVDISENRLVGSIPPAISGCESLEFLDLHTNSLSGSLLGTTLPKSLKFIDFSDNA
LSSTLPPGIGLLTELTKLNLAKNRLSGEIPREISTCRSLQLLNLGENDFSGEIPDELGQIPSLAISLNLSCNRFVGEIPS
RFSDLKNLGVLDVSHNQLTGNLNVLTDLQNLVSLNISYNDFSGDLPNTPFFRRLPLSDLASNRGLYISNAIST
;
57 
2 PDB 5HZ1        5HZ1   ? 2 ? 1  
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5HZ1 B 1 ? 633 ? C0LGR3 57 ? 689 ? 61 689 
2 2 5HZ1 A 1 ? 13  ? 5HZ1   44 ? 56  ? 44 56  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 5HZ1 THR B 4  ? UNP C0LGR3 VAL 60  'engineered mutation' 64  1 
1 5HZ1 GLU B 21 ? UNP C0LGR3 GLY 77  'engineered mutation' 81  2 
1 5HZ1 LYS B 22 ? UNP C0LGR3 MET 78  'engineered mutation' 82  3 
1 5HZ1 GLN B 23 ? UNP C0LGR3 ASP 79  'engineered mutation' 83  4 
1 5HZ1 GLN B 48 ? UNP C0LGR3 ASN 104 'engineered mutation' 104 5 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                    ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                   ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                 ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'            ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                   ?                 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                  ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                    ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                  ?                 'C6 H10 N3 O2 1' 156.162 
HZP 'L-peptide linking' n '(4S)-4-hydroxy-L-proline' ?                 'C5 H9 N O3'     131.130 
ILE 'L-peptide linking' y ISOLEUCINE                 ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                    ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                     ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                 ?                 'C5 H11 N O2 S'  149.211 
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 
PTR 'L-peptide linking' n O-PHOSPHOTYROSINE          PHOSPHONOTYROSINE 'C9 H12 N O6 P'  261.168 
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.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5HZ1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            4.00 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         69.24 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MES monohydrate pH 6.0, 22% (v/v) polyethylene glycol (PEG) 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'OXFORD RUBY CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-12-21 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             LAUE 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.entry_id                     5HZ1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             99.000 
_reflns.d_resolution_high            2.59 
_reflns.number_obs                   33780 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        31.8000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.20 
_reflns.pdbx_Rrim_I_all              ? 
_reflns.pdbx_Rpim_I_all              ? 
_reflns.pdbx_CC_half                 ? 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
_reflns_shell.d_res_high                  . 
_reflns_shell.d_res_low                   ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.entry_id                                 5HZ1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.5900 
_refine.ls_d_res_low                             35.4200 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.9100 
_refine.ls_number_reflns_obs                     33780 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  'U VALUES      : REFINED INDIVIDUALLY' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2342 
_refine.ls_R_factor_R_work                       0.2342 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               25.6860 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            1.1500 
_refine.aniso_B[2][2]                            1.1500 
_refine.aniso_B[3][3]                            -3.7300 
_refine.aniso_B[1][2]                            1.1500 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            -0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9340 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       0.3630 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                214.610 
_refine.B_iso_min                                2.000 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.5900 
_refine_hist.d_res_low                        35.4200 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4942 
_refine_hist.pdbx_number_residues_total       636 
_refine_hist.pdbx_B_iso_mean_ligand           23.67 
_refine_hist.pdbx_number_atoms_protein        4886 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
_refine_ls_shell.d_res_high                       2.5910 
_refine_ls_shell.d_res_low                        2.6590 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               91.5200 
_refine_ls_shell.number_reflns_R_work             2310 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.2930 
_refine_ls_shell.R_factor_R_free                  ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                     5HZ1 
_struct.title                        'Plant peptide hormone receptor RGFR1 in complex with RGF3' 
_struct.pdbx_descriptor              
;ASP-PTR-TRP-ARG-ALA-LYS-HIS-HIS-PRO-HYP-LYS-ASN-ASN, Probable LRR receptor-like serine/threonine-protein kinase At4g26540 (E.C.2.7.11.1)
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5HZ1 
_struct_keywords.text            'Plant Receptor, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 54  ? PHE A 60  ? PRO B 110 PHE B 116 5 ? 7 
HELX_P HELX_P2  AA2 PRO A 78  ? LEU A 84  ? PRO B 134 LEU B 140 5 ? 7 
HELX_P HELX_P3  AA3 PRO A 102 ? LEU A 108 ? PRO B 158 LEU B 164 5 ? 7 
HELX_P HELX_P4  AA4 PRO A 126 ? LEU A 132 ? PRO B 182 LEU B 188 5 ? 7 
HELX_P HELX_P5  AA5 PRO A 151 ? CYS A 157 ? PRO B 207 CYS B 213 5 ? 7 
HELX_P HELX_P6  AA6 PRO A 175 ? LEU A 181 ? PRO B 231 LEU B 237 5 ? 7 
HELX_P HELX_P7  AA7 PRO A 199 ? CYS A 205 ? PRO B 255 CYS B 261 5 ? 7 
HELX_P HELX_P8  AA8 PRO A 223 ? LEU A 229 ? PRO B 279 LEU B 285 5 ? 7 
HELX_P HELX_P9  AA9 PRO A 247 ? CYS A 253 ? PRO B 303 CYS B 309 5 ? 7 
HELX_P HELX_P10 AB1 PRO A 271 ? LEU A 277 ? PRO B 327 LEU B 333 5 ? 7 
HELX_P HELX_P11 AB2 PRO A 295 ? CYS A 301 ? PRO B 351 CYS B 357 5 ? 7 
HELX_P HELX_P12 AB3 PRO A 319 ? LEU A 325 ? PRO B 375 LEU B 381 5 ? 7 
HELX_P HELX_P13 AB4 PRO A 343 ? CYS A 349 ? PRO B 399 CYS B 405 5 ? 7 
HELX_P HELX_P14 AB5 PRO A 367 ? LEU A 373 ? PRO B 423 LEU B 429 5 ? 7 
HELX_P HELX_P15 AB6 PRO A 391 ? CYS A 397 ? PRO B 447 CYS B 453 5 ? 7 
HELX_P HELX_P16 AB7 PRO A 415 ? LEU A 421 ? PRO B 471 LEU B 477 5 ? 7 
HELX_P HELX_P17 AB8 PRO A 439 ? CYS A 445 ? PRO B 495 CYS B 501 5 ? 7 
HELX_P HELX_P18 AB9 LEU A 463 ? LEU A 467 ? LEU B 519 LEU B 523 5 ? 5 
HELX_P HELX_P19 AC1 PRO A 486 ? LEU A 492 ? PRO B 542 LEU B 548 5 ? 7 
HELX_P HELX_P20 AC2 PRO A 510 ? CYS A 516 ? PRO B 566 CYS B 572 5 ? 7 
HELX_P HELX_P21 AC3 PRO A 534 ? GLY A 538 ? PRO B 590 GLY B 594 5 ? 5 
HELX_P HELX_P22 AC4 PRO A 559 ? LEU A 565 ? PRO B 615 LEU B 621 5 ? 7 
HELX_P HELX_P23 AC5 LEU A 582 ? THR A 586 ? LEU B 638 THR B 642 5 ? 5 
HELX_P HELX_P24 AC6 THR A 608 ? LEU A 614 ? THR B 664 LEU B 670 1 ? 7 
HELX_P HELX_P25 AC7 PRO A 615 ? SER A 621 ? PRO B 671 SER B 677 1 ? 7 
# 
_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 
covale1 covale one  ? A ASN 396 ND2 ? ? ? 1_555 C NAG .  C1 ? ? B ASN 452 B NAG 701 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale2 covale one  ? A ASN 548 ND2 ? ? ? 1_555 E NAG .  C1 ? ? B ASN 604 B NAG 703 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale3 covale one  ? A ASN 595 ND2 ? ? ? 1_555 F NAG .  C1 ? ? B ASN 651 B NAG 704 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale4 covale both ? B ASP 1   C   ? ? ? 1_555 B PTR 2  N  ? ? A ASP 44  A PTR 45  1_555 ? ? ? ? ? ? ? 1.328 ? 
covale5 covale both ? B PTR 2   C   ? ? ? 1_555 B TRP 3  N  ? ? A PTR 45  A TRP 46  1_555 ? ? ? ? ? ? ? 1.330 ? 
covale6 covale both ? B PRO 9   C   ? ? ? 1_555 B HZP 10 N  ? ? A PRO 52  A HZP 53  1_555 ? ? ? ? ? ? ? 1.328 ? 
covale7 covale both ? B HZP 10  C   ? ? ? 1_555 B LYS 11 N  ? ? A HZP 53  A LYS 54  1_555 ? ? ? ? ? ? ? 1.323 ? 
covale8 covale both ? C NAG .   O4  ? ? ? 1_555 D NAG .  C1 ? ? B NAG 701 B NAG 702 1_555 ? ? ? ? ? ? ? 1.446 ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 26 ? 
AA2 ? 5  ? 
AA3 ? 5  ? 
AA4 ? 2  ? 
AA5 ? 2  ? 
AA6 ? 3  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA1 14 15 ? parallel      
AA1 15 16 ? parallel      
AA1 16 17 ? parallel      
AA1 17 18 ? parallel      
AA1 18 19 ? parallel      
AA1 19 20 ? parallel      
AA1 20 21 ? parallel      
AA1 21 22 ? parallel      
AA1 22 23 ? parallel      
AA1 23 24 ? parallel      
AA1 24 25 ? parallel      
AA1 25 26 ? parallel      
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? parallel      
AA3 1  2  ? parallel      
AA3 2  3  ? parallel      
AA3 3  4  ? parallel      
AA3 4  5  ? parallel      
AA4 1  2  ? parallel      
AA5 1  2  ? parallel      
AA6 1  2  ? parallel      
AA6 2  3  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 6   ? CYS A 8   ? VAL B 66  CYS B 68  
AA1 2  VAL A 14  ? LYS A 20  ? VAL B 74  LYS B 80  
AA1 3  SER A 41  ? SER A 45  ? SER B 97  SER B 101 
AA1 4  LEU A 65  ? ASP A 67  ? LEU B 121 ASP B 123 
AA1 5  THR A 89  ? SER A 91  ? THR B 145 SER B 147 
AA1 6  GLU A 113 ? MET A 115 ? GLU B 169 MET B 171 
AA1 7  VAL A 137 ? ARG A 139 ? VAL B 193 ARG B 195 
AA1 8  MET A 162 ? GLY A 164 ? MET B 218 GLY B 220 
AA1 9  THR A 186 ? ALA A 188 ? THR B 242 ALA B 244 
AA1 10 ASN A 210 ? TYR A 212 ? ASN B 266 TYR B 268 
AA1 11 SER A 234 ? LEU A 236 ? SER B 290 LEU B 292 
AA1 12 LEU A 258 ? ASP A 260 ? LEU B 314 ASP B 316 
AA1 13 GLU A 282 ? GLN A 284 ? GLU B 338 GLN B 340 
AA1 14 HIS A 306 ? GLU A 308 ? HIS B 362 GLU B 364 
AA1 15 MET A 330 ? PHE A 332 ? MET B 386 PHE B 388 
AA1 16 ALA A 354 ? ASP A 356 ? ALA B 410 ASP B 412 
AA1 17 LYS A 378 ? LEU A 380 ? LYS B 434 LEU B 436 
AA1 18 ARG A 402 ? ARG A 404 ? ARG B 458 ARG B 460 
AA1 19 PHE A 426 ? ASP A 428 ? PHE B 482 ASP B 484 
AA1 20 PHE A 450 ? ASP A 452 ? PHE B 506 ASP B 508 
AA1 21 PHE A 473 ? ASP A 475 ? PHE B 529 ASP B 531 
AA1 22 LYS A 497 ? ASN A 499 ? LYS B 553 ASN B 555 
AA1 23 LEU A 521 ? ASN A 523 ? LEU B 577 ASN B 579 
AA1 24 SER A 546 ? ASN A 548 ? SER B 602 ASN B 604 
AA1 25 VAL A 570 ? ASP A 572 ? VAL B 626 ASP B 628 
AA1 26 SER A 593 ? ASN A 595 ? SER B 649 ASN B 651 
AA2 1  SER A 122 ? GLY A 123 ? SER B 178 GLY B 179 
AA2 2  ASN A 145 ? GLY A 148 ? ASN B 201 GLY B 204 
AA2 3  SER A 169 ? GLY A 172 ? SER B 225 GLY B 228 
AA2 4  LEU A 193 ? GLY A 196 ? LEU B 249 GLY B 252 
AA2 5  SER A 217 ? ILE A 218 ? SER B 273 ILE B 274 
AA3 1  THR A 315 ? GLY A 316 ? THR B 371 GLY B 372 
AA3 2  LYS A 337 ? GLY A 340 ? LYS B 393 GLY B 396 
AA3 3  SER A 361 ? GLY A 364 ? SER B 417 GLY B 420 
AA3 4  ASP A 385 ? GLY A 388 ? ASP B 441 GLY B 444 
AA3 5  ARG A 409 ? LEU A 410 ? ARG B 465 LEU B 466 
AA4 1  SER A 459 ? GLY A 460 ? SER B 515 GLY B 516 
AA4 2  ALA A 480 ? LEU A 481 ? ALA B 536 LEU B 537 
AA5 1  SER A 530 ? GLU A 532 ? SER B 586 GLU B 588 
AA5 2  ARG A 553 ? VAL A 555 ? ARG B 609 VAL B 611 
AA6 1  THR A 579 ? GLY A 580 ? THR B 635 GLY B 636 
AA6 2  ASP A 600 ? LEU A 605 ? ASP B 656 LEU B 661 
AA6 3  GLY A 624 ? ILE A 627 ? GLY B 680 ILE B 683 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N LYS A 7   ? N LYS B 67  O SER A 15  ? O SER B 75  
AA1 2  3  N ILE A 17  ? N ILE B 77  O THR A 43  ? O THR B 99  
AA1 3  4  N LEU A 42  ? N LEU B 98  O LEU A 65  ? O LEU B 121 
AA1 4  5  N LEU A 66  ? N LEU B 122 O SER A 91  ? O SER B 147 
AA1 5  6  N LEU A 90  ? N LEU B 146 O MET A 115 ? O MET B 171 
AA1 6  7  N LEU A 114 ? N LEU B 170 O ARG A 139 ? O ARG B 195 
AA1 7  8  N LEU A 138 ? N LEU B 194 O GLY A 164 ? O GLY B 220 
AA1 8  9  N LEU A 163 ? N LEU B 219 O ALA A 188 ? O ALA B 244 
AA1 9  10 N ILE A 187 ? N ILE B 243 O TYR A 212 ? O TYR B 268 
AA1 10 11 N LEU A 211 ? N LEU B 267 O LEU A 236 ? O LEU B 292 
AA1 11 12 N LEU A 235 ? N LEU B 291 O ASP A 260 ? O ASP B 316 
AA1 12 13 N ILE A 259 ? N ILE B 315 O GLN A 284 ? O GLN B 340 
AA1 13 14 N LEU A 283 ? N LEU B 339 O HIS A 306 ? O HIS B 362 
AA1 14 15 N LEU A 307 ? N LEU B 363 O MET A 330 ? O MET B 386 
AA1 15 16 N PHE A 331 ? N PHE B 387 O ALA A 354 ? O ALA B 410 
AA1 16 17 N ILE A 355 ? N ILE B 411 O LEU A 380 ? O LEU B 436 
AA1 17 18 N LEU A 379 ? N LEU B 435 O ARG A 404 ? O ARG B 460 
AA1 18 19 N LEU A 403 ? N LEU B 459 O ASP A 428 ? O ASP B 484 
AA1 19 20 N VAL A 427 ? N VAL B 483 O ASP A 452 ? O ASP B 508 
AA1 20 21 N LEU A 451 ? N LEU B 507 O ASP A 475 ? O ASP B 531 
AA1 21 22 N ILE A 474 ? N ILE B 530 O ASN A 499 ? O ASN B 555 
AA1 22 23 N LEU A 498 ? N LEU B 554 O ASN A 523 ? O ASN B 579 
AA1 23 24 N LEU A 522 ? N LEU B 578 O ASN A 548 ? O ASN B 604 
AA1 24 25 N LEU A 547 ? N LEU B 603 O ASP A 572 ? O ASP B 628 
AA1 25 26 N LEU A 571 ? N LEU B 627 O SER A 593 ? O SER B 649 
AA2 1  2  N GLY A 123 ? N GLY B 179 O ARG A 147 ? O ARG B 203 
AA2 2  3  N GLY A 148 ? N GLY B 204 O SER A 171 ? O SER B 227 
AA2 3  4  N GLY A 172 ? N GLY B 228 O SER A 195 ? O SER B 251 
AA2 4  5  N LEU A 194 ? N LEU B 250 O SER A 217 ? O SER B 273 
AA3 1  2  N GLY A 316 ? N GLY B 372 O THR A 339 ? O THR B 395 
AA3 2  3  N LEU A 338 ? N LEU B 394 O SER A 361 ? O SER B 417 
AA3 3  4  N LEU A 362 ? N LEU B 418 O ASP A 385 ? O ASP B 441 
AA3 4  5  N LEU A 386 ? N LEU B 442 O ARG A 409 ? O ARG B 465 
AA4 1  2  N GLY A 460 ? N GLY B 516 O ALA A 480 ? O ALA B 536 
AA5 1  2  N GLY A 531 ? N GLY B 587 O VAL A 555 ? O VAL B 611 
AA6 1  2  N GLY A 580 ? N GLY B 636 O SER A 602 ? O SER B 658 
AA6 2  3  N LEU A 605 ? N LEU B 661 O TYR A 626 ? O TYR B 682 
# 
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 B ASN 452 ? 5 'binding site for Poly-Saccharide residues NAG B 701 through NAG B 702 bound to ASN B 452' 
AC2 Software B NAG 703 ? 5 'binding site for Mono-Saccharide NAG B 703 bound to ASN B 604'                            
AC3 Software B NAG 704 ? 5 'binding site for Mono-Saccharide NAG B 704 bound to ASN B 651'                            
# 
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 LYS A 55  ? LYS B 111 . ? 6_565 ? 
2  AC1 5 ARG A 83  ? ARG B 139 . ? 6_565 ? 
3  AC1 5 LYS A 368 ? LYS B 424 . ? 1_555 ? 
4  AC1 5 ASP A 393 ? ASP B 449 . ? 1_555 ? 
5  AC1 5 ASN A 396 ? ASN B 452 . ? 1_555 ? 
6  AC2 5 GLU A 526 ? GLU B 582 . ? 1_555 ? 
7  AC2 5 ASN A 548 ? ASN B 604 . ? 1_555 ? 
8  AC2 5 SER A 550 ? SER B 606 . ? 1_555 ? 
9  AC2 5 ASP A 572 ? ASP B 628 . ? 1_555 ? 
10 AC2 5 NAG F .   ? NAG B 704 . ? 1_555 ? 
11 AC3 5 ASP A 572 ? ASP B 628 . ? 1_555 ? 
12 AC3 5 SER A 574 ? SER B 630 . ? 1_555 ? 
13 AC3 5 SER A 593 ? SER B 649 . ? 1_555 ? 
14 AC3 5 ASN A 595 ? ASN B 651 . ? 1_555 ? 
15 AC3 5 NAG E .   ? NAG B 703 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5HZ1 
_atom_sites.fract_transf_matrix[1][1]   0.005451 
_atom_sites.fract_transf_matrix[1][2]   0.003147 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006294 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.011414 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . CYS A 1 1   ? 70.174 67.966  -23.765 1.00 51.86  ? 61  CYS B N   1 
ATOM   2    C CA  . CYS A 1 1   ? 69.762 67.610  -22.408 1.00 64.91  ? 61  CYS B CA  1 
ATOM   3    C C   . CYS A 1 1   ? 68.894 68.699  -21.769 1.00 71.53  ? 61  CYS B C   1 
ATOM   4    O O   . CYS A 1 1   ? 67.671 68.645  -21.847 1.00 69.93  ? 61  CYS B O   1 
ATOM   5    C CB  . CYS A 1 1   ? 70.982 67.298  -21.524 1.00 65.50  ? 61  CYS B CB  1 
ATOM   6    N N   . ASN A 1 2   ? 69.523 69.641  -21.075 1.00 79.30  ? 62  ASN B N   1 
ATOM   7    C CA  . ASN A 1 2   ? 68.806 70.775  -20.480 1.00 77.94  ? 62  ASN B CA  1 
ATOM   8    C C   . ASN A 1 2   ? 68.861 72.161  -21.158 1.00 75.36  ? 62  ASN B C   1 
ATOM   9    O O   . ASN A 1 2   ? 68.287 73.108  -20.617 1.00 71.72  ? 62  ASN B O   1 
ATOM   10   C CB  . ASN A 1 2   ? 69.149 70.913  -18.992 1.00 77.93  ? 62  ASN B CB  1 
ATOM   11   N N   . TRP A 1 3   ? 69.528 72.304  -22.308 1.00 74.58  ? 63  TRP B N   1 
ATOM   12   C CA  . TRP A 1 3   ? 69.828 73.656  -22.831 1.00 74.45  ? 63  TRP B CA  1 
ATOM   13   C C   . TRP A 1 3   ? 68.550 74.393  -23.309 1.00 75.64  ? 63  TRP B C   1 
ATOM   14   O O   . TRP A 1 3   ? 67.453 73.822  -23.306 1.00 64.46  ? 63  TRP B O   1 
ATOM   15   C CB  . TRP A 1 3   ? 70.936 73.590  -23.918 1.00 117.41 ? 63  TRP B CB  1 
ATOM   16   C CG  . TRP A 1 3   ? 71.375 74.920  -24.579 1.00 118.04 ? 63  TRP B CG  1 
ATOM   17   C CD1 . TRP A 1 3   ? 71.002 75.380  -25.817 1.00 116.89 ? 63  TRP B CD1 1 
ATOM   18   C CD2 . TRP A 1 3   ? 72.272 75.917  -24.042 1.00 116.62 ? 63  TRP B CD2 1 
ATOM   19   N NE1 . TRP A 1 3   ? 71.595 76.596  -26.074 1.00 116.33 ? 63  TRP B NE1 1 
ATOM   20   C CE2 . TRP A 1 3   ? 72.378 76.948  -25.006 1.00 116.07 ? 63  TRP B CE2 1 
ATOM   21   C CE3 . TRP A 1 3   ? 72.984 76.042  -22.844 1.00 111.55 ? 63  TRP B CE3 1 
ATOM   22   C CZ2 . TRP A 1 3   ? 73.168 78.084  -24.806 1.00 111.33 ? 63  TRP B CZ2 1 
ATOM   23   C CZ3 . TRP A 1 3   ? 73.766 77.173  -22.650 1.00 109.21 ? 63  TRP B CZ3 1 
ATOM   24   C CH2 . TRP A 1 3   ? 73.850 78.177  -23.626 1.00 108.85 ? 63  TRP B CH2 1 
ATOM   25   N N   . THR A 1 4   ? 68.693 75.652  -23.721 1.00 80.61  ? 64  THR B N   1 
ATOM   26   C CA  . THR A 1 4   ? 67.538 76.537  -23.871 1.00 79.97  ? 64  THR B CA  1 
ATOM   27   C C   . THR A 1 4   ? 66.751 76.251  -25.143 1.00 81.62  ? 64  THR B C   1 
ATOM   28   O O   . THR A 1 4   ? 67.265 76.397  -26.256 1.00 85.22  ? 64  THR B O   1 
ATOM   29   C CB  . THR A 1 4   ? 67.959 78.026  -23.862 1.00 79.16  ? 64  THR B CB  1 
ATOM   30   N N   . GLY A 1 5   ? 65.488 75.869  -24.964 1.00 74.80  ? 65  GLY B N   1 
ATOM   31   C CA  . GLY A 1 5   ? 64.639 75.477  -26.075 1.00 65.78  ? 65  GLY B CA  1 
ATOM   32   C C   . GLY A 1 5   ? 64.377 73.982  -26.143 1.00 56.44  ? 65  GLY B C   1 
ATOM   33   O O   . GLY A 1 5   ? 63.524 73.528  -26.904 1.00 54.72  ? 65  GLY B O   1 
ATOM   34   N N   . VAL A 1 6   ? 65.107 73.212  -25.345 1.00 50.77  ? 66  VAL B N   1 
ATOM   35   C CA  . VAL A 1 6   ? 64.943 71.766  -25.337 1.00 46.32  ? 66  VAL B CA  1 
ATOM   36   C C   . VAL A 1 6   ? 64.085 71.326  -24.163 1.00 53.32  ? 66  VAL B C   1 
ATOM   37   O O   . VAL A 1 6   ? 64.152 71.900  -23.075 1.00 56.48  ? 66  VAL B O   1 
ATOM   38   C CB  . VAL A 1 6   ? 66.292 71.043  -25.252 1.00 44.13  ? 66  VAL B CB  1 
ATOM   39   C CG1 . VAL A 1 6   ? 66.104 69.547  -25.451 1.00 47.31  ? 66  VAL B CG1 1 
ATOM   40   C CG2 . VAL A 1 6   ? 67.252 71.591  -26.285 1.00 38.60  ? 66  VAL B CG2 1 
ATOM   41   N N   . LYS A 1 7   ? 63.259 70.316  -24.397 1.00 54.76  ? 67  LYS B N   1 
ATOM   42   C CA  . LYS A 1 7   ? 62.481 69.711  -23.332 1.00 55.76  ? 67  LYS B CA  1 
ATOM   43   C C   . LYS A 1 7   ? 62.631 68.194  -23.439 1.00 58.51  ? 67  LYS B C   1 
ATOM   44   O O   . LYS A 1 7   ? 62.830 67.663  -24.537 1.00 57.48  ? 67  LYS B O   1 
ATOM   45   C CB  . LYS A 1 7   ? 61.013 70.141  -23.425 1.00 55.64  ? 67  LYS B CB  1 
ATOM   46   C CG  . LYS A 1 7   ? 60.800 71.658  -23.373 1.00 58.22  ? 67  LYS B CG  1 
ATOM   47   C CD  . LYS A 1 7   ? 59.333 72.025  -23.611 1.00 59.24  ? 67  LYS B CD  1 
ATOM   48   C CE  . LYS A 1 7   ? 59.113 73.540  -23.692 1.00 58.90  ? 67  LYS B CE  1 
ATOM   49   N NZ  . LYS A 1 7   ? 57.680 73.914  -23.957 1.00 51.87  ? 67  LYS B NZ  1 
ATOM   50   N N   . CYS A 1 8   ? 62.565 67.502  -22.300 1.00 58.78  ? 68  CYS B N   1 
ATOM   51   C CA  . CYS A 1 8   ? 62.785 66.054  -22.270 1.00 57.52  ? 68  CYS B CA  1 
ATOM   52   C C   . CYS A 1 8   ? 61.626 65.286  -21.645 1.00 55.55  ? 68  CYS B C   1 
ATOM   53   O O   . CYS A 1 8   ? 60.835 65.849  -20.888 1.00 55.01  ? 68  CYS B O   1 
ATOM   54   C CB  . CYS A 1 8   ? 64.086 65.712  -21.536 1.00 59.24  ? 68  CYS B CB  1 
ATOM   55   S SG  . CYS A 1 8   ? 65.576 65.695  -22.565 1.00 87.30  ? 68  CYS B SG  1 
ATOM   56   N N   . ASN A 1 9   ? 61.535 63.999  -21.979 1.00 59.29  ? 69  ASN B N   1 
ATOM   57   C CA  . ASN A 1 9   ? 60.518 63.114  -21.424 1.00 66.66  ? 69  ASN B CA  1 
ATOM   58   C C   . ASN A 1 9   ? 60.880 62.701  -19.990 1.00 72.07  ? 69  ASN B C   1 
ATOM   59   O O   . ASN A 1 9   ? 61.957 63.044  -19.488 1.00 67.67  ? 69  ASN B O   1 
ATOM   60   C CB  . ASN A 1 9   ? 60.383 61.878  -22.322 1.00 69.66  ? 69  ASN B CB  1 
ATOM   61   C CG  . ASN A 1 9   ? 59.150 61.052  -22.006 1.00 80.04  ? 69  ASN B CG  1 
ATOM   62   O OD1 . ASN A 1 9   ? 58.307 61.450  -21.194 1.00 84.78  ? 69  ASN B OD1 1 
ATOM   63   N ND2 . ASN A 1 9   ? 59.034 59.895  -22.651 1.00 81.98  ? 69  ASN B ND2 1 
ATOM   64   N N   . ARG A 1 10  ? 59.995 61.959  -19.329 1.00 75.70  ? 70  ARG B N   1 
ATOM   65   C CA  . ARG A 1 10  ? 60.321 61.431  -18.010 1.00 79.22  ? 70  ARG B CA  1 
ATOM   66   C C   . ARG A 1 10  ? 61.324 60.281  -18.099 1.00 85.53  ? 70  ARG B C   1 
ATOM   67   O O   . ARG A 1 10  ? 62.093 60.056  -17.168 1.00 88.98  ? 70  ARG B O   1 
ATOM   68   C CB  . ARG A 1 10  ? 59.068 61.025  -17.223 1.00 76.71  ? 70  ARG B CB  1 
ATOM   69   C CG  . ARG A 1 10  ? 58.085 60.130  -17.959 1.00 78.47  ? 70  ARG B CG  1 
ATOM   70   C CD  . ARG A 1 10  ? 56.964 59.678  -17.019 1.00 77.77  ? 70  ARG B CD  1 
ATOM   71   N NE  . ARG A 1 10  ? 56.465 60.773  -16.184 1.00 74.44  ? 70  ARG B NE  1 
ATOM   72   C CZ  . ARG A 1 10  ? 55.857 60.608  -15.010 1.00 72.58  ? 70  ARG B CZ  1 
ATOM   73   N NH1 . ARG A 1 10  ? 55.666 59.389  -14.516 1.00 73.17  ? 70  ARG B NH1 1 
ATOM   74   N NH2 . ARG A 1 10  ? 55.447 61.665  -14.323 1.00 69.15  ? 70  ARG B NH2 1 
ATOM   75   N N   . ARG A 1 11  ? 61.343 59.574  -19.226 1.00 84.33  ? 71  ARG B N   1 
ATOM   76   C CA  . ARG A 1 11  ? 62.310 58.494  -19.417 1.00 80.88  ? 71  ARG B CA  1 
ATOM   77   C C   . ARG A 1 11  ? 63.659 59.036  -19.920 1.00 77.29  ? 71  ARG B C   1 
ATOM   78   O O   . ARG A 1 11  ? 64.576 58.268  -20.211 1.00 82.93  ? 71  ARG B O   1 
ATOM   79   C CB  . ARG A 1 11  ? 61.750 57.383  -20.327 1.00 85.87  ? 71  ARG B CB  1 
ATOM   80   C CG  . ARG A 1 11  ? 61.358 57.852  -21.716 1.00 97.65  ? 71  ARG B CG  1 
ATOM   81   C CD  . ARG A 1 11  ? 60.758 56.738  -22.564 1.00 105.31 ? 71  ARG B CD  1 
ATOM   82   N NE  . ARG A 1 11  ? 61.679 55.627  -22.823 1.00 111.28 ? 71  ARG B NE  1 
ATOM   83   C CZ  . ARG A 1 11  ? 61.589 54.828  -23.883 1.00 115.65 ? 71  ARG B CZ  1 
ATOM   84   N NH1 . ARG A 1 11  ? 60.646 55.045  -24.795 1.00 115.67 ? 71  ARG B NH1 1 
ATOM   85   N NH2 . ARG A 1 11  ? 62.459 53.841  -24.054 1.00 118.07 ? 71  ARG B NH2 1 
ATOM   86   N N   . GLY A 1 12  ? 63.765 60.361  -20.036 1.00 69.64  ? 72  GLY B N   1 
ATOM   87   C CA  . GLY A 1 12  ? 65.038 61.018  -20.312 1.00 62.06  ? 72  GLY B CA  1 
ATOM   88   C C   . GLY A 1 12  ? 65.382 61.359  -21.757 1.00 57.22  ? 72  GLY B C   1 
ATOM   89   O O   . GLY A 1 12  ? 66.476 61.869  -22.037 1.00 49.99  ? 72  GLY B O   1 
ATOM   90   N N   . GLU A 1 13  ? 64.452 61.077  -22.669 1.00 62.43  ? 73  GLU B N   1 
ATOM   91   C CA  . GLU A 1 13  ? 64.641 61.344  -24.095 1.00 65.46  ? 73  GLU B CA  1 
ATOM   92   C C   . GLU A 1 13  ? 64.099 62.715  -24.516 1.00 62.00  ? 73  GLU B C   1 
ATOM   93   O O   . GLU A 1 13  ? 63.094 63.192  -23.984 1.00 61.97  ? 73  GLU B O   1 
ATOM   94   C CB  . GLU A 1 13  ? 63.971 60.245  -24.912 1.00 70.23  ? 73  GLU B CB  1 
ATOM   95   C CG  . GLU A 1 13  ? 64.168 58.858  -24.329 1.00 77.79  ? 73  GLU B CG  1 
ATOM   96   C CD  . GLU A 1 13  ? 63.141 57.897  -24.853 1.00 85.62  ? 73  GLU B CD  1 
ATOM   97   O OE1 . GLU A 1 13  ? 62.024 58.353  -25.198 1.00 84.99  ? 73  GLU B OE1 1 
ATOM   98   O OE2 . GLU A 1 13  ? 63.457 56.696  -24.935 1.00 90.75  ? 73  GLU B OE2 1 
ATOM   99   N N   . VAL A 1 14  ? 64.781 63.352  -25.463 1.00 57.18  ? 74  VAL B N   1 
ATOM   100  C CA  . VAL A 1 14  ? 64.338 64.651  -25.945 1.00 53.60  ? 74  VAL B CA  1 
ATOM   101  C C   . VAL A 1 14  ? 62.943 64.551  -26.557 1.00 47.45  ? 74  VAL B C   1 
ATOM   102  O O   . VAL A 1 14  ? 62.711 63.814  -27.525 1.00 39.33  ? 74  VAL B O   1 
ATOM   103  C CB  . VAL A 1 14  ? 65.305 65.177  -27.012 1.00 50.50  ? 74  VAL B CB  1 
ATOM   104  C CG1 . VAL A 1 14  ? 64.771 66.450  -27.625 1.00 41.66  ? 74  VAL B CG1 1 
ATOM   105  C CG2 . VAL A 1 14  ? 66.695 65.389  -26.406 1.00 39.03  ? 74  VAL B CG2 1 
ATOM   106  N N   . SER A 1 15  ? 62.013 65.286  -25.958 1.00 43.55  ? 75  SER B N   1 
ATOM   107  C CA  . SER A 1 15  ? 60.643 65.292  -26.417 1.00 32.79  ? 75  SER B CA  1 
ATOM   108  C C   . SER A 1 15  ? 60.194 66.551  -27.165 1.00 42.93  ? 75  SER B C   1 
ATOM   109  O O   . SER A 1 15  ? 59.135 66.538  -27.785 1.00 39.06  ? 75  SER B O   1 
ATOM   110  C CB  . SER A 1 15  ? 59.729 65.040  -25.224 1.00 41.74  ? 75  SER B CB  1 
ATOM   111  O OG  . SER A 1 15  ? 58.490 64.497  -25.630 1.00 47.20  ? 75  SER B OG  1 
ATOM   112  N N   . GLU A 1 16  ? 60.989 67.621  -27.143 1.00 32.26  ? 76  GLU B N   1 
ATOM   113  C CA  . GLU A 1 16  ? 60.551 68.894  -27.730 1.00 32.78  ? 76  GLU B CA  1 
ATOM   114  C C   . GLU A 1 16  ? 61.696 69.793  -28.152 1.00 45.65  ? 76  GLU B C   1 
ATOM   115  O O   . GLU A 1 16  ? 62.752 69.803  -27.524 1.00 55.30  ? 76  GLU B O   1 
ATOM   116  C CB  . GLU A 1 16  ? 59.654 69.689  -26.773 1.00 36.33  ? 76  GLU B CB  1 
ATOM   117  C CG  . GLU A 1 16  ? 58.243 69.157  -26.604 1.00 44.97  ? 76  GLU B CG  1 
ATOM   118  C CD  . GLU A 1 16  ? 57.415 70.007  -25.663 1.00 55.84  ? 76  GLU B CD  1 
ATOM   119  O OE1 . GLU A 1 16  ? 56.886 69.460  -24.668 1.00 51.84  ? 76  GLU B OE1 1 
ATOM   120  O OE2 . GLU A 1 16  ? 57.292 71.224  -25.927 1.00 63.39  ? 76  GLU B OE2 1 
ATOM   121  N N   . ILE A 1 17  ? 61.457 70.570  -29.203 1.00 31.53  ? 77  ILE B N   1 
ATOM   122  C CA  . ILE A 1 17  ? 62.404 71.550  -29.692 1.00 37.35  ? 77  ILE B CA  1 
ATOM   123  C C   . ILE A 1 17  ? 61.624 72.800  -30.061 1.00 43.57  ? 77  ILE B C   1 
ATOM   124  O O   . ILE A 1 17  ? 60.661 72.733  -30.823 1.00 46.72  ? 77  ILE B O   1 
ATOM   125  C CB  . ILE A 1 17  ? 63.126 71.028  -30.934 1.00 40.66  ? 77  ILE B CB  1 
ATOM   126  C CG1 . ILE A 1 17  ? 64.065 69.885  -30.557 1.00 39.31  ? 77  ILE B CG1 1 
ATOM   127  C CG2 . ILE A 1 17  ? 63.882 72.146  -31.638 1.00 39.28  ? 77  ILE B CG2 1 
ATOM   128  C CD1 . ILE A 1 17  ? 64.566 69.118  -31.752 1.00 34.82  ? 77  ILE B CD1 1 
ATOM   129  N N   . GLN A 1 18  ? 62.015 73.935  -29.499 1.00 46.37  ? 78  GLN B N   1 
ATOM   130  C CA  . GLN A 1 18  ? 61.332 75.183  -29.786 1.00 48.68  ? 78  GLN B CA  1 
ATOM   131  C C   . GLN A 1 18  ? 62.298 76.335  -30.004 1.00 58.75  ? 78  GLN B C   1 
ATOM   132  O O   . GLN A 1 18  ? 63.030 76.725  -29.091 1.00 61.34  ? 78  GLN B O   1 
ATOM   133  C CB  . GLN A 1 18  ? 60.384 75.526  -28.645 1.00 48.39  ? 78  GLN B CB  1 
ATOM   134  C CG  . GLN A 1 18  ? 59.756 76.893  -28.774 1.00 53.26  ? 78  GLN B CG  1 
ATOM   135  C CD  . GLN A 1 18  ? 58.434 76.978  -28.047 1.00 59.95  ? 78  GLN B CD  1 
ATOM   136  O OE1 . GLN A 1 18  ? 57.653 76.023  -28.041 1.00 60.45  ? 78  GLN B OE1 1 
ATOM   137  N NE2 . GLN A 1 18  ? 58.177 78.120  -27.422 1.00 62.04  ? 78  GLN B NE2 1 
ATOM   138  N N   . LEU A 1 19  ? 62.281 76.894  -31.209 1.00 61.08  ? 79  LEU B N   1 
ATOM   139  C CA  . LEU A 1 19  ? 63.099 78.058  -31.525 1.00 63.24  ? 79  LEU B CA  1 
ATOM   140  C C   . LEU A 1 19  ? 62.264 79.154  -32.191 1.00 65.36  ? 79  LEU B C   1 
ATOM   141  O O   . LEU A 1 19  ? 61.794 78.984  -33.315 1.00 61.54  ? 79  LEU B O   1 
ATOM   142  C CB  . LEU A 1 19  ? 64.246 77.652  -32.446 1.00 62.71  ? 79  LEU B CB  1 
ATOM   143  C CG  . LEU A 1 19  ? 65.144 76.509  -31.970 1.00 62.43  ? 79  LEU B CG  1 
ATOM   144  C CD1 . LEU A 1 19  ? 66.278 76.275  -32.959 1.00 60.31  ? 79  LEU B CD1 1 
ATOM   145  C CD2 . LEU A 1 19  ? 65.696 76.791  -30.582 1.00 61.06  ? 79  LEU B CD2 1 
ATOM   146  N N   . LYS A 1 20  ? 62.097 80.283  -31.508 1.00 69.70  ? 80  LYS B N   1 
ATOM   147  C CA  . LYS A 1 20  ? 61.295 81.383  -32.043 1.00 70.48  ? 80  LYS B CA  1 
ATOM   148  C C   . LYS A 1 20  ? 62.055 82.709  -32.134 1.00 80.10  ? 80  LYS B C   1 
ATOM   149  O O   . LYS A 1 20  ? 62.642 83.170  -31.156 1.00 83.85  ? 80  LYS B O   1 
ATOM   150  C CB  . LYS A 1 20  ? 60.002 81.567  -31.239 1.00 67.03  ? 80  LYS B CB  1 
ATOM   151  C CG  . LYS A 1 20  ? 58.929 80.525  -31.533 1.00 69.65  ? 80  LYS B CG  1 
ATOM   152  C CD  . LYS A 1 20  ? 57.571 80.921  -30.948 1.00 71.45  ? 80  LYS B CD  1 
ATOM   153  C CE  . LYS A 1 20  ? 56.717 81.703  -31.947 1.00 75.27  ? 80  LYS B CE  1 
ATOM   154  N NZ  . LYS A 1 20  ? 57.275 83.044  -32.286 1.00 78.20  ? 80  LYS B NZ  1 
ATOM   155  N N   . GLU A 1 21  ? 62.026 83.303  -33.326 1.00 85.64  ? 81  GLU B N   1 
ATOM   156  C CA  . GLU A 1 21  ? 62.618 84.615  -33.624 1.00 85.93  ? 81  GLU B CA  1 
ATOM   157  C C   . GLU A 1 21  ? 64.099 84.759  -33.276 1.00 85.78  ? 81  GLU B C   1 
ATOM   158  O O   . GLU A 1 21  ? 64.471 85.607  -32.463 1.00 87.06  ? 81  GLU B O   1 
ATOM   159  C CB  . GLU A 1 21  ? 61.815 85.729  -32.942 1.00 86.99  ? 81  GLU B CB  1 
ATOM   160  N N   . LYS A 1 22  ? 64.938 83.926  -33.884 1.00 85.13  ? 82  LYS B N   1 
ATOM   161  C CA  . LYS A 1 22  ? 66.389 84.043  -33.718 1.00 84.73  ? 82  LYS B CA  1 
ATOM   162  C C   . LYS A 1 22  ? 67.207 84.662  -34.873 1.00 86.50  ? 82  LYS B C   1 
ATOM   163  O O   . LYS A 1 22  ? 68.427 84.775  -34.750 1.00 92.46  ? 82  LYS B O   1 
ATOM   164  C CB  . LYS A 1 22  ? 67.001 82.719  -33.233 1.00 82.92  ? 82  LYS B CB  1 
ATOM   165  N N   . GLN A 1 23  ? 66.567 85.038  -35.983 1.00 81.37  ? 83  GLN B N   1 
ATOM   166  C CA  . GLN A 1 23  ? 67.292 85.659  -37.113 1.00 80.03  ? 83  GLN B CA  1 
ATOM   167  C C   . GLN A 1 23  ? 68.414 84.807  -37.742 1.00 80.15  ? 83  GLN B C   1 
ATOM   168  O O   . GLN A 1 23  ? 69.594 85.024  -37.475 1.00 85.42  ? 83  GLN B O   1 
ATOM   169  C CB  . GLN A 1 23  ? 67.825 87.050  -36.743 1.00 77.73  ? 83  GLN B CB  1 
ATOM   170  N N   . LEU A 1 24  ? 68.035 83.818  -38.543 1.00 74.30  ? 84  LEU B N   1 
ATOM   171  C CA  . LEU A 1 24  ? 68.977 82.866  -39.131 1.00 73.47  ? 84  LEU B CA  1 
ATOM   172  C C   . LEU A 1 24  ? 68.869 82.867  -40.649 1.00 81.24  ? 84  LEU B C   1 
ATOM   173  O O   . LEU A 1 24  ? 68.238 83.747  -41.236 1.00 82.78  ? 84  LEU B O   1 
ATOM   174  C CB  . LEU A 1 24  ? 68.679 81.443  -38.669 1.00 66.83  ? 84  LEU B CB  1 
ATOM   175  C CG  . LEU A 1 24  ? 68.889 80.950  -37.247 1.00 63.18  ? 84  LEU B CG  1 
ATOM   176  C CD1 . LEU A 1 24  ? 67.958 81.643  -36.293 1.00 67.75  ? 84  LEU B CD1 1 
ATOM   177  C CD2 . LEU A 1 24  ? 68.638 79.454  -37.226 1.00 57.14  ? 84  LEU B CD2 1 
ATOM   178  N N   . GLN A 1 25  ? 69.525 81.892  -41.279 1.00 84.62  ? 85  GLN B N   1 
ATOM   179  C CA  . GLN A 1 25  ? 69.366 81.644  -42.712 1.00 86.63  ? 85  GLN B CA  1 
ATOM   180  C C   . GLN A 1 25  ? 69.356 80.138  -43.001 1.00 84.27  ? 85  GLN B C   1 
ATOM   181  O O   . GLN A 1 25  ? 69.453 79.327  -42.080 1.00 79.49  ? 85  GLN B O   1 
ATOM   182  C CB  . GLN A 1 25  ? 70.495 82.317  -43.500 1.00 91.74  ? 85  GLN B CB  1 
ATOM   183  C CG  . GLN A 1 25  ? 70.061 82.936  -44.826 1.00 93.27  ? 85  GLN B CG  1 
ATOM   184  C CD  . GLN A 1 25  ? 69.612 84.381  -44.680 1.00 92.71  ? 85  GLN B CD  1 
ATOM   185  O OE1 . GLN A 1 25  ? 69.823 85.007  -43.640 1.00 94.84  ? 85  GLN B OE1 1 
ATOM   186  N NE2 . GLN A 1 25  ? 68.993 84.919  -45.724 1.00 88.98  ? 85  GLN B NE2 1 
ATOM   187  N N   . GLY A 1 26  ? 69.212 79.775  -44.276 1.00 85.88  ? 86  GLY B N   1 
ATOM   188  C CA  . GLY A 1 26  ? 69.450 78.412  -44.737 1.00 84.67  ? 86  GLY B CA  1 
ATOM   189  C C   . GLY A 1 26  ? 68.402 77.338  -44.488 1.00 80.00  ? 86  GLY B C   1 
ATOM   190  O O   . GLY A 1 26  ? 67.323 77.610  -43.971 1.00 84.47  ? 86  GLY B O   1 
ATOM   191  N N   . SER A 1 27  ? 68.744 76.106  -44.861 1.00 73.73  ? 87  SER B N   1 
ATOM   192  C CA  . SER A 1 27  ? 67.861 74.946  -44.735 1.00 71.08  ? 87  SER B CA  1 
ATOM   193  C C   . SER A 1 27  ? 67.877 74.351  -43.335 1.00 82.12  ? 87  SER B C   1 
ATOM   194  O O   . SER A 1 27  ? 68.366 74.969  -42.393 1.00 89.40  ? 87  SER B O   1 
ATOM   195  C CB  . SER A 1 27  ? 68.234 73.863  -45.746 1.00 63.35  ? 87  SER B CB  1 
ATOM   196  O OG  . SER A 1 27  ? 68.012 74.302  -47.070 1.00 60.10  ? 87  SER B OG  1 
ATOM   197  N N   . LEU A 1 28  ? 67.322 73.150  -43.206 1.00 84.79  ? 88  LEU B N   1 
ATOM   198  C CA  . LEU A 1 28  ? 67.198 72.502  -41.905 1.00 87.20  ? 88  LEU B CA  1 
ATOM   199  C C   . LEU A 1 28  ? 67.236 70.980  -42.021 1.00 86.98  ? 88  LEU B C   1 
ATOM   200  O O   . LEU A 1 28  ? 67.094 70.431  -43.113 1.00 85.11  ? 88  LEU B O   1 
ATOM   201  C CB  . LEU A 1 28  ? 65.912 72.959  -41.201 1.00 84.73  ? 88  LEU B CB  1 
ATOM   202  C CG  . LEU A 1 28  ? 64.553 72.768  -41.889 1.00 79.29  ? 88  LEU B CG  1 
ATOM   203  C CD1 . LEU A 1 28  ? 63.445 72.924  -40.871 1.00 72.25  ? 88  LEU B CD1 1 
ATOM   204  C CD2 . LEU A 1 28  ? 64.328 73.740  -43.044 1.00 81.53  ? 88  LEU B CD2 1 
ATOM   205  N N   . LEU A 1 36  ? 67.092 61.533  -33.079 1.00 54.91  ? 92  LEU B N   1 
ATOM   206  C CA  . LEU A 1 36  ? 66.215 61.638  -31.917 1.00 55.87  ? 92  LEU B CA  1 
ATOM   207  C C   . LEU A 1 36  ? 64.779 61.293  -32.297 1.00 56.25  ? 92  LEU B C   1 
ATOM   208  O O   . LEU A 1 36  ? 63.969 62.158  -32.622 1.00 49.41  ? 92  LEU B O   1 
ATOM   209  C CB  . LEU A 1 36  ? 66.315 63.029  -31.274 1.00 53.27  ? 92  LEU B CB  1 
ATOM   210  C CG  . LEU A 1 36  ? 66.421 64.261  -32.180 1.00 45.64  ? 92  LEU B CG  1 
ATOM   211  C CD1 . LEU A 1 36  ? 65.120 65.002  -32.210 1.00 50.97  ? 92  LEU B CD1 1 
ATOM   212  C CD2 . LEU A 1 36  ? 67.516 65.194  -31.721 1.00 41.65  ? 92  LEU B CD2 1 
ATOM   213  N N   . LYS A 1 37  ? 64.470 60.007  -32.244 1.00 63.23  ? 93  LYS B N   1 
ATOM   214  C CA  . LYS A 1 37  ? 63.233 59.501  -32.814 1.00 64.89  ? 93  LYS B CA  1 
ATOM   215  C C   . LYS A 1 37  ? 62.077 59.477  -31.806 1.00 58.91  ? 93  LYS B C   1 
ATOM   216  O O   . LYS A 1 37  ? 61.016 58.904  -32.068 1.00 58.14  ? 93  LYS B O   1 
ATOM   217  C CB  . LYS A 1 37  ? 63.486 58.164  -33.523 1.00 69.37  ? 93  LYS B CB  1 
ATOM   218  C CG  . LYS A 1 37  ? 64.527 58.314  -34.653 1.00 74.46  ? 93  LYS B CG  1 
ATOM   219  C CD  . LYS A 1 37  ? 65.020 56.992  -35.232 1.00 77.86  ? 93  LYS B CD  1 
ATOM   220  C CE  . LYS A 1 37  ? 63.996 56.365  -36.172 1.00 78.45  ? 93  LYS B CE  1 
ATOM   221  N NZ  . LYS A 1 37  ? 64.549 55.182  -36.900 1.00 78.53  ? 93  LYS B NZ  1 
ATOM   222  N N   . SER A 1 38  ? 62.308 60.080  -30.641 1.00 51.32  ? 94  SER B N   1 
ATOM   223  C CA  . SER A 1 38  ? 61.283 60.214  -29.601 1.00 50.93  ? 94  SER B CA  1 
ATOM   224  C C   . SER A 1 38  ? 60.524 61.558  -29.623 1.00 50.48  ? 94  SER B C   1 
ATOM   225  O O   . SER A 1 38  ? 59.702 61.832  -28.740 1.00 46.74  ? 94  SER B O   1 
ATOM   226  C CB  . SER A 1 38  ? 61.910 59.999  -28.222 1.00 50.17  ? 94  SER B CB  1 
ATOM   227  O OG  . SER A 1 38  ? 62.965 60.923  -28.019 1.00 51.85  ? 94  SER B OG  1 
ATOM   228  N N   . LEU A 1 39  ? 60.810 62.389  -30.622 1.00 47.78  ? 95  LEU B N   1 
ATOM   229  C CA  . LEU A 1 39  ? 60.271 63.748  -30.707 1.00 41.51  ? 95  LEU B CA  1 
ATOM   230  C C   . LEU A 1 39  ? 58.750 63.848  -30.752 1.00 44.40  ? 95  LEU B C   1 
ATOM   231  O O   . LEU A 1 39  ? 58.078 63.035  -31.378 1.00 50.02  ? 95  LEU B O   1 
ATOM   232  C CB  . LEU A 1 39  ? 60.846 64.465  -31.922 1.00 38.71  ? 95  LEU B CB  1 
ATOM   233  C CG  . LEU A 1 39  ? 60.924 65.976  -31.759 1.00 38.78  ? 95  LEU B CG  1 
ATOM   234  C CD1 . LEU A 1 39  ? 61.505 66.307  -30.395 1.00 40.54  ? 95  LEU B CD1 1 
ATOM   235  C CD2 . LEU A 1 39  ? 61.787 66.554  -32.864 1.00 43.67  ? 95  LEU B CD2 1 
ATOM   236  N N   . THR A 1 40  ? 58.232 64.886  -30.105 1.00 40.00  ? 96  THR B N   1 
ATOM   237  C CA  . THR A 1 40  ? 56.797 65.119  -29.953 1.00 34.91  ? 96  THR B CA  1 
ATOM   238  C C   . THR A 1 40  ? 56.371 66.472  -30.539 1.00 36.49  ? 96  THR B C   1 
ATOM   239  O O   . THR A 1 40  ? 55.468 66.544  -31.372 1.00 37.40  ? 96  THR B O   1 
ATOM   240  C CB  . THR A 1 40  ? 56.353 64.986  -28.482 1.00 39.03  ? 96  THR B CB  1 
ATOM   241  O OG1 . THR A 1 40  ? 56.168 63.601  -28.170 1.00 36.68  ? 96  THR B OG1 1 
ATOM   242  C CG2 . THR A 1 40  ? 55.044 65.717  -28.240 1.00 46.09  ? 96  THR B CG2 1 
ATOM   243  N N   . SER A 1 41  ? 56.968 67.548  -30.043 1.00 28.11  ? 97  SER B N   1 
ATOM   244  C CA  . SER A 1 41  ? 56.679 68.878  -30.550 1.00 40.43  ? 97  SER B CA  1 
ATOM   245  C C   . SER A 1 41  ? 57.907 69.509  -31.202 1.00 41.03  ? 97  SER B C   1 
ATOM   246  O O   . SER A 1 41  ? 58.983 69.536  -30.615 1.00 42.24  ? 97  SER B O   1 
ATOM   247  C CB  . SER A 1 41  ? 56.143 69.775  -29.430 1.00 40.04  ? 97  SER B CB  1 
ATOM   248  O OG  . SER A 1 41  ? 56.433 71.140  -29.684 1.00 42.92  ? 97  SER B OG  1 
ATOM   249  N N   . LEU A 1 42  ? 57.746 70.011  -32.421 1.00 27.81  ? 98  LEU B N   1 
ATOM   250  C CA  . LEU A 1 42  ? 58.846 70.678  -33.098 1.00 36.83  ? 98  LEU B CA  1 
ATOM   251  C C   . LEU A 1 42  ? 58.451 72.051  -33.631 1.00 35.99  ? 98  LEU B C   1 
ATOM   252  O O   . LEU A 1 42  ? 57.670 72.152  -34.573 1.00 35.40  ? 98  LEU B O   1 
ATOM   253  C CB  . LEU A 1 42  ? 59.354 69.807  -34.245 1.00 29.22  ? 98  LEU B CB  1 
ATOM   254  C CG  . LEU A 1 42  ? 60.410 70.444  -35.150 1.00 32.64  ? 98  LEU B CG  1 
ATOM   255  C CD1 . LEU A 1 42  ? 61.706 70.671  -34.383 1.00 31.19  ? 98  LEU B CD1 1 
ATOM   256  C CD2 . LEU A 1 42  ? 60.658 69.583  -36.389 1.00 30.38  ? 98  LEU B CD2 1 
ATOM   257  N N   . THR A 1 43  ? 59.009 73.103  -33.039 1.00 27.99  ? 99  THR B N   1 
ATOM   258  C CA  . THR A 1 43  ? 58.779 74.458  -33.520 1.00 27.33  ? 99  THR B CA  1 
ATOM   259  C C   . THR A 1 43  ? 60.059 75.112  -34.020 1.00 34.33  ? 99  THR B C   1 
ATOM   260  O O   . THR A 1 43  ? 60.971 75.396  -33.245 1.00 35.88  ? 99  THR B O   1 
ATOM   261  C CB  . THR A 1 43  ? 58.148 75.365  -32.439 1.00 39.67  ? 99  THR B CB  1 
ATOM   262  O OG1 . THR A 1 43  ? 56.804 74.947  -32.179 1.00 41.87  ? 99  THR B OG1 1 
ATOM   263  C CG2 . THR A 1 43  ? 58.113 76.813  -32.911 1.00 26.13  ? 99  THR B CG2 1 
ATOM   264  N N   . LEU A 1 44  ? 60.137 75.315  -35.329 1.00 36.89  ? 100 LEU B N   1 
ATOM   265  C CA  . LEU A 1 44  ? 61.127 76.219  -35.895 1.00 38.10  ? 100 LEU B CA  1 
ATOM   266  C C   . LEU A 1 44  ? 60.375 77.350  -36.584 1.00 37.69  ? 100 LEU B C   1 
ATOM   267  O O   . LEU A 1 44  ? 59.869 77.187  -37.691 1.00 36.67  ? 100 LEU B O   1 
ATOM   268  C CB  . LEU A 1 44  ? 62.008 75.460  -36.877 1.00 29.82  ? 100 LEU B CB  1 
ATOM   269  C CG  . LEU A 1 44  ? 62.666 74.237  -36.229 1.00 34.60  ? 100 LEU B CG  1 
ATOM   270  C CD1 . LEU A 1 44  ? 63.402 73.415  -37.247 1.00 33.94  ? 100 LEU B CD1 1 
ATOM   271  C CD2 . LEU A 1 44  ? 63.615 74.659  -35.108 1.00 40.19  ? 100 LEU B CD2 1 
ATOM   272  N N   . SER A 1 45  ? 60.357 78.517  -35.952 1.00 41.10  ? 101 SER B N   1 
ATOM   273  C CA  . SER A 1 45  ? 59.434 79.570  -36.346 1.00 41.67  ? 101 SER B CA  1 
ATOM   274  C C   . SER A 1 45  ? 60.052 80.955  -36.225 1.00 45.25  ? 101 SER B C   1 
ATOM   275  O O   . SER A 1 45  ? 60.757 81.249  -35.258 1.00 44.27  ? 101 SER B O   1 
ATOM   276  C CB  . SER A 1 45  ? 58.170 79.501  -35.486 1.00 45.74  ? 101 SER B CB  1 
ATOM   277  O OG  . SER A 1 45  ? 57.320 80.608  -35.737 1.00 51.74  ? 101 SER B OG  1 
ATOM   278  N N   . SER A 1 46  ? 59.764 81.801  -37.211 1.00 44.78  ? 102 SER B N   1 
ATOM   279  C CA  . SER A 1 46  ? 60.269 83.166  -37.244 1.00 41.30  ? 102 SER B CA  1 
ATOM   280  C C   . SER A 1 46  ? 61.799 83.198  -37.247 1.00 43.51  ? 102 SER B C   1 
ATOM   281  O O   . SER A 1 46  ? 62.410 84.071  -36.636 1.00 46.84  ? 102 SER B O   1 
ATOM   282  C CB  . SER A 1 46  ? 59.695 83.968  -36.079 1.00 41.12  ? 102 SER B CB  1 
ATOM   283  O OG  . SER A 1 46  ? 58.303 83.709  -35.939 1.00 39.03  ? 102 SER B OG  1 
ATOM   284  N N   . LEU A 1 47  ? 62.404 82.215  -37.913 1.00 38.69  ? 103 LEU B N   1 
ATOM   285  C CA  . LEU A 1 47  ? 63.857 82.132  -38.047 1.00 42.19  ? 103 LEU B CA  1 
ATOM   286  C C   . LEU A 1 47  ? 64.411 82.607  -39.388 1.00 49.65  ? 103 LEU B C   1 
ATOM   287  O O   . LEU A 1 47  ? 65.605 82.490  -39.637 1.00 52.47  ? 103 LEU B O   1 
ATOM   288  C CB  . LEU A 1 47  ? 64.325 80.709  -37.774 1.00 41.45  ? 103 LEU B CB  1 
ATOM   289  C CG  . LEU A 1 47  ? 63.663 80.086  -36.549 1.00 38.09  ? 103 LEU B CG  1 
ATOM   290  C CD1 . LEU A 1 47  ? 64.041 78.631  -36.454 1.00 33.11  ? 103 LEU B CD1 1 
ATOM   291  C CD2 . LEU A 1 47  ? 64.048 80.837  -35.279 1.00 42.93  ? 103 LEU B CD2 1 
ATOM   292  N N   . GLN A 1 48  ? 63.540 83.092  -40.266 1.00 54.85  ? 104 GLN B N   1 
ATOM   293  C CA  . GLN A 1 48  ? 63.941 83.497  -41.615 1.00 49.79  ? 104 GLN B CA  1 
ATOM   294  C C   . GLN A 1 48  ? 64.652 82.375  -42.396 1.00 46.68  ? 104 GLN B C   1 
ATOM   295  O O   . GLN A 1 48  ? 65.567 82.640  -43.178 1.00 48.27  ? 104 GLN B O   1 
ATOM   296  C CB  . GLN A 1 48  ? 64.798 84.773  -41.575 1.00 45.26  ? 104 GLN B CB  1 
ATOM   297  N N   . LEU A 1 49  ? 64.217 81.133  -42.189 1.00 38.07  ? 105 LEU B N   1 
ATOM   298  C CA  . LEU A 1 49  ? 64.794 79.975  -42.879 1.00 34.26  ? 105 LEU B CA  1 
ATOM   299  C C   . LEU A 1 49  ? 64.455 79.953  -44.369 1.00 38.69  ? 105 LEU B C   1 
ATOM   300  O O   . LEU A 1 49  ? 63.495 80.580  -44.806 1.00 40.93  ? 105 LEU B O   1 
ATOM   301  C CB  . LEU A 1 49  ? 64.309 78.669  -42.241 1.00 32.60  ? 105 LEU B CB  1 
ATOM   302  C CG  . LEU A 1 49  ? 64.437 78.498  -40.721 1.00 39.61  ? 105 LEU B CG  1 
ATOM   303  C CD1 . LEU A 1 49  ? 63.768 77.198  -40.252 1.00 36.72  ? 105 LEU B CD1 1 
ATOM   304  C CD2 . LEU A 1 49  ? 65.893 78.542  -40.282 1.00 40.53  ? 105 LEU B CD2 1 
ATOM   305  N N   . THR A 1 50  ? 65.247 79.228  -45.151 1.00 41.88  ? 106 THR B N   1 
ATOM   306  C CA  . THR A 1 50  ? 64.976 79.093  -46.581 1.00 44.73  ? 106 THR B CA  1 
ATOM   307  C C   . THR A 1 50  ? 65.135 77.647  -47.036 1.00 41.61  ? 106 THR B C   1 
ATOM   308  O O   . THR A 1 50  ? 65.504 76.773  -46.246 1.00 32.35  ? 106 THR B O   1 
ATOM   309  C CB  . THR A 1 50  ? 65.875 80.023  -47.456 1.00 46.91  ? 106 THR B CB  1 
ATOM   310  O OG1 . THR A 1 50  ? 67.248 79.887  -47.066 1.00 53.89  ? 106 THR B OG1 1 
ATOM   311  C CG2 . THR A 1 50  ? 65.460 81.480  -47.304 1.00 39.72  ? 106 THR B CG2 1 
ATOM   312  N N   . GLY A 1 51  ? 64.863 77.406  -48.315 1.00 34.85  ? 107 GLY B N   1 
ATOM   313  C CA  . GLY A 1 51  ? 64.915 76.064  -48.861 1.00 40.86  ? 107 GLY B CA  1 
ATOM   314  C C   . GLY A 1 51  ? 63.600 75.325  -48.724 1.00 48.56  ? 107 GLY B C   1 
ATOM   315  O O   . GLY A 1 51  ? 62.611 75.883  -48.252 1.00 53.77  ? 107 GLY B O   1 
ATOM   316  N N   . VAL A 1 52  ? 63.588 74.074  -49.176 1.00 52.19  ? 108 VAL B N   1 
ATOM   317  C CA  . VAL A 1 52  ? 62.452 73.173  -49.006 1.00 30.52  ? 108 VAL B CA  1 
ATOM   318  C C   . VAL A 1 52  ? 62.378 72.597  -47.597 1.00 37.08  ? 108 VAL B C   1 
ATOM   319  O O   . VAL A 1 52  ? 63.368 72.598  -46.859 1.00 31.59  ? 108 VAL B O   1 
ATOM   320  C CB  . VAL A 1 52  ? 62.527 71.973  -49.977 1.00 33.44  ? 108 VAL B CB  1 
ATOM   321  C CG1 . VAL A 1 52  ? 62.423 72.436  -51.421 1.00 30.79  ? 108 VAL B CG1 1 
ATOM   322  C CG2 . VAL A 1 52  ? 63.807 71.155  -49.731 1.00 32.52  ? 108 VAL B CG2 1 
ATOM   323  N N   . ILE A 1 53  ? 61.186 72.121  -47.234 1.00 35.11  ? 109 ILE B N   1 
ATOM   324  C CA  . ILE A 1 53  ? 60.986 71.276  -46.064 1.00 29.79  ? 109 ILE B CA  1 
ATOM   325  C C   . ILE A 1 53  ? 61.519 69.894  -46.390 1.00 42.36  ? 109 ILE B C   1 
ATOM   326  O O   . ILE A 1 53  ? 61.038 69.254  -47.329 1.00 45.63  ? 109 ILE B O   1 
ATOM   327  C CB  . ILE A 1 53  ? 59.490 71.108  -45.756 1.00 28.48  ? 109 ILE B CB  1 
ATOM   328  C CG1 . ILE A 1 53  ? 58.891 72.421  -45.236 1.00 27.50  ? 109 ILE B CG1 1 
ATOM   329  C CG2 . ILE A 1 53  ? 59.271 69.958  -44.781 1.00 28.68  ? 109 ILE B CG2 1 
ATOM   330  C CD1 . ILE A 1 53  ? 57.383 72.492  -45.340 1.00 26.14  ? 109 ILE B CD1 1 
ATOM   331  N N   . PRO A 1 54  ? 62.507 69.420  -45.614 1.00 38.60  ? 110 PRO B N   1 
ATOM   332  C CA  . PRO A 1 54  ? 63.111 68.112  -45.888 1.00 36.82  ? 110 PRO B CA  1 
ATOM   333  C C   . PRO A 1 54  ? 62.040 67.050  -45.714 1.00 43.35  ? 110 PRO B C   1 
ATOM   334  O O   . PRO A 1 54  ? 61.256 67.183  -44.777 1.00 58.58  ? 110 PRO B O   1 
ATOM   335  C CB  . PRO A 1 54  ? 64.166 67.972  -44.782 1.00 34.01  ? 110 PRO B CB  1 
ATOM   336  C CG  . PRO A 1 54  ? 64.311 69.339  -44.166 1.00 33.67  ? 110 PRO B CG  1 
ATOM   337  C CD  . PRO A 1 54  ? 62.992 70.007  -44.354 1.00 36.71  ? 110 PRO B CD  1 
ATOM   338  N N   . LYS A 1 55  ? 61.988 66.023  -46.557 1.00 38.82  ? 111 LYS B N   1 
ATOM   339  C CA  . LYS A 1 55  ? 60.909 65.046  -46.411 1.00 43.71  ? 111 LYS B CA  1 
ATOM   340  C C   . LYS A 1 55  ? 61.177 63.972  -45.357 1.00 48.56  ? 111 LYS B C   1 
ATOM   341  O O   . LYS A 1 55  ? 60.381 63.047  -45.177 1.00 47.25  ? 111 LYS B O   1 
ATOM   342  C CB  . LYS A 1 55  ? 60.441 64.443  -47.745 1.00 47.88  ? 111 LYS B CB  1 
ATOM   343  C CG  . LYS A 1 55  ? 61.458 64.275  -48.867 1.00 39.98  ? 111 LYS B CG  1 
ATOM   344  C CD  . LYS A 1 55  ? 60.683 63.900  -50.134 1.00 36.36  ? 111 LYS B CD  1 
ATOM   345  C CE  . LYS A 1 55  ? 61.534 63.902  -51.389 1.00 42.80  ? 111 LYS B CE  1 
ATOM   346  N NZ  . LYS A 1 55  ? 62.377 62.673  -51.476 1.00 52.62  ? 111 LYS B NZ  1 
ATOM   347  N N   . GLU A 1 56  ? 62.300 64.110  -44.658 1.00 49.84  ? 112 GLU B N   1 
ATOM   348  C CA  . GLU A 1 56  ? 62.621 63.225  -43.550 1.00 50.62  ? 112 GLU B CA  1 
ATOM   349  C C   . GLU A 1 56  ? 61.808 63.575  -42.300 1.00 52.17  ? 112 GLU B C   1 
ATOM   350  O O   . GLU A 1 56  ? 61.828 62.844  -41.306 1.00 54.73  ? 112 GLU B O   1 
ATOM   351  C CB  . GLU A 1 56  ? 64.123 63.249  -43.255 1.00 56.87  ? 112 GLU B CB  1 
ATOM   352  C CG  . GLU A 1 56  ? 64.986 62.657  -44.371 1.00 63.44  ? 112 GLU B CG  1 
ATOM   353  C CD  . GLU A 1 56  ? 65.357 63.679  -45.432 1.00 72.03  ? 112 GLU B CD  1 
ATOM   354  O OE1 . GLU A 1 56  ? 66.179 64.571  -45.128 1.00 78.73  ? 112 GLU B OE1 1 
ATOM   355  O OE2 . GLU A 1 56  ? 64.832 63.592  -46.566 1.00 69.97  ? 112 GLU B OE2 1 
ATOM   356  N N   . ILE A 1 57  ? 61.093 64.695  -42.359 1.00 45.69  ? 113 ILE B N   1 
ATOM   357  C CA  . ILE A 1 57  ? 60.165 65.087  -41.301 1.00 36.12  ? 113 ILE B CA  1 
ATOM   358  C C   . ILE A 1 57  ? 59.145 63.982  -41.042 1.00 37.41  ? 113 ILE B C   1 
ATOM   359  O O   . ILE A 1 57  ? 58.743 63.746  -39.905 1.00 47.22  ? 113 ILE B O   1 
ATOM   360  C CB  . ILE A 1 57  ? 59.438 66.396  -41.678 1.00 40.87  ? 113 ILE B CB  1 
ATOM   361  C CG1 . ILE A 1 57  ? 60.358 67.596  -41.460 1.00 45.70  ? 113 ILE B CG1 1 
ATOM   362  C CG2 . ILE A 1 57  ? 58.177 66.591  -40.859 1.00 37.50  ? 113 ILE B CG2 1 
ATOM   363  C CD1 . ILE A 1 57  ? 60.432 68.059  -40.019 1.00 41.79  ? 113 ILE B CD1 1 
ATOM   364  N N   . GLY A 1 58  ? 58.754 63.277  -42.096 1.00 30.71  ? 114 GLY B N   1 
ATOM   365  C CA  . GLY A 1 58  ? 57.794 62.197  -41.982 1.00 34.58  ? 114 GLY B CA  1 
ATOM   366  C C   . GLY A 1 58  ? 58.335 60.989  -41.240 1.00 44.07  ? 114 GLY B C   1 
ATOM   367  O O   . GLY A 1 58  ? 57.630 59.992  -41.083 1.00 48.58  ? 114 GLY B O   1 
ATOM   368  N N   . ASP A 1 59  ? 59.588 61.060  -40.795 1.00 51.05  ? 115 ASP B N   1 
ATOM   369  C CA  . ASP A 1 59  ? 60.157 59.991  -39.969 1.00 53.99  ? 115 ASP B CA  1 
ATOM   370  C C   . ASP A 1 59  ? 59.899 60.130  -38.462 1.00 51.51  ? 115 ASP B C   1 
ATOM   371  O O   . ASP A 1 59  ? 60.013 59.144  -37.733 1.00 51.25  ? 115 ASP B O   1 
ATOM   372  C CB  . ASP A 1 59  ? 61.666 59.823  -40.215 1.00 54.40  ? 115 ASP B CB  1 
ATOM   373  C CG  . ASP A 1 59  ? 61.994 59.387  -41.638 1.00 55.98  ? 115 ASP B CG  1 
ATOM   374  O OD1 . ASP A 1 59  ? 61.101 58.859  -42.343 1.00 54.06  ? 115 ASP B OD1 1 
ATOM   375  O OD2 . ASP A 1 59  ? 63.165 59.569  -42.045 1.00 58.96  ? 115 ASP B OD2 1 
ATOM   376  N N   . PHE A 1 60  ? 59.514 61.315  -37.983 1.00 51.21  ? 116 PHE B N   1 
ATOM   377  C CA  . PHE A 1 60  ? 59.345 61.458  -36.538 1.00 44.11  ? 116 PHE B CA  1 
ATOM   378  C C   . PHE A 1 60  ? 57.913 61.078  -36.242 1.00 46.28  ? 116 PHE B C   1 
ATOM   379  O O   . PHE A 1 60  ? 57.009 61.899  -36.338 1.00 44.83  ? 116 PHE B O   1 
ATOM   380  C CB  . PHE A 1 60  ? 59.534 62.915  -36.101 1.00 35.21  ? 116 PHE B CB  1 
ATOM   381  C CG  . PHE A 1 60  ? 60.909 63.473  -36.363 1.00 39.98  ? 116 PHE B CG  1 
ATOM   382  C CD1 . PHE A 1 60  ? 62.007 63.025  -35.646 1.00 41.49  ? 116 PHE B CD1 1 
ATOM   383  C CD2 . PHE A 1 60  ? 61.094 64.488  -37.294 1.00 39.80  ? 116 PHE B CD2 1 
ATOM   384  C CE1 . PHE A 1 60  ? 63.272 63.555  -35.877 1.00 42.22  ? 116 PHE B CE1 1 
ATOM   385  C CE2 . PHE A 1 60  ? 62.356 65.022  -37.525 1.00 37.54  ? 116 PHE B CE2 1 
ATOM   386  C CZ  . PHE A 1 60  ? 63.444 64.552  -36.820 1.00 38.15  ? 116 PHE B CZ  1 
ATOM   387  N N   . THR A 1 61  ? 57.725 59.863  -35.749 1.00 50.60  ? 117 THR B N   1 
ATOM   388  C CA  . THR A 1 61  ? 56.395 59.278  -35.736 1.00 52.40  ? 117 THR B CA  1 
ATOM   389  C C   . THR A 1 61  ? 55.587 59.797  -34.567 1.00 52.52  ? 117 THR B C   1 
ATOM   390  O O   . THR A 1 61  ? 54.363 59.755  -34.584 1.00 61.64  ? 117 THR B O   1 
ATOM   391  C CB  . THR A 1 61  ? 56.458 57.746  -35.665 1.00 56.72  ? 117 THR B CB  1 
ATOM   392  O OG1 . THR A 1 61  ? 57.640 57.280  -36.328 1.00 48.33  ? 117 THR B OG1 1 
ATOM   393  C CG2 . THR A 1 61  ? 55.222 57.139  -36.325 1.00 65.13  ? 117 THR B CG2 1 
ATOM   394  N N   . GLU A 1 62  ? 56.278 60.299  -33.553 1.00 43.64  ? 118 GLU B N   1 
ATOM   395  C CA  . GLU A 1 62  ? 55.608 60.743  -32.346 1.00 42.86  ? 118 GLU B CA  1 
ATOM   396  C C   . GLU A 1 62  ? 55.290 62.232  -32.386 1.00 38.78  ? 118 GLU B C   1 
ATOM   397  O O   . GLU A 1 62  ? 54.766 62.785  -31.417 1.00 42.23  ? 118 GLU B O   1 
ATOM   398  C CB  . GLU A 1 62  ? 56.447 60.391  -31.103 1.00 48.21  ? 118 GLU B CB  1 
ATOM   399  C CG  . GLU A 1 62  ? 55.903 59.211  -30.304 1.00 48.47  ? 118 GLU B CG  1 
ATOM   400  C CD  . GLU A 1 62  ? 55.548 58.034  -31.193 1.00 53.19  ? 118 GLU B CD  1 
ATOM   401  O OE1 . GLU A 1 62  ? 56.427 57.578  -31.954 1.00 56.03  ? 118 GLU B OE1 1 
ATOM   402  O OE2 . GLU A 1 62  ? 54.389 57.572  -31.148 1.00 53.98  ? 118 GLU B OE2 1 
ATOM   403  N N   . LEU A 1 63  ? 55.614 62.882  -33.499 1.00 34.95  ? 119 LEU B N   1 
ATOM   404  C CA  . LEU A 1 63  ? 55.332 64.305  -33.644 1.00 33.32  ? 119 LEU B CA  1 
ATOM   405  C C   . LEU A 1 63  ? 53.830 64.564  -33.513 1.00 29.38  ? 119 LEU B C   1 
ATOM   406  O O   . LEU A 1 63  ? 53.024 63.971  -34.236 1.00 25.61  ? 119 LEU B O   1 
ATOM   407  C CB  . LEU A 1 63  ? 55.826 64.785  -35.005 1.00 34.85  ? 119 LEU B CB  1 
ATOM   408  C CG  . LEU A 1 63  ? 56.531 66.133  -35.061 1.00 33.13  ? 119 LEU B CG  1 
ATOM   409  C CD1 . LEU A 1 63  ? 57.443 66.302  -33.861 1.00 28.66  ? 119 LEU B CD1 1 
ATOM   410  C CD2 . LEU A 1 63  ? 57.321 66.211  -36.361 1.00 28.98  ? 119 LEU B CD2 1 
ATOM   411  N N   . GLU A 1 64  ? 53.451 65.386  -32.538 1.00 26.99  ? 120 GLU B N   1 
ATOM   412  C CA  . GLU A 1 64  ? 52.077 65.876  -32.443 1.00 28.17  ? 120 GLU B CA  1 
ATOM   413  C C   . GLU A 1 64  ? 51.928 67.343  -32.835 1.00 23.56  ? 120 GLU B C   1 
ATOM   414  O O   . GLU A 1 64  ? 50.805 67.845  -32.994 1.00 22.47  ? 120 GLU B O   1 
ATOM   415  C CB  . GLU A 1 64  ? 51.555 65.668  -31.015 1.00 29.02  ? 120 GLU B CB  1 
ATOM   416  C CG  . GLU A 1 64  ? 51.393 64.205  -30.619 1.00 37.33  ? 120 GLU B CG  1 
ATOM   417  C CD  . GLU A 1 64  ? 51.794 63.934  -29.171 1.00 47.02  ? 120 GLU B CD  1 
ATOM   418  O OE1 . GLU A 1 64  ? 51.922 64.907  -28.396 1.00 50.40  ? 120 GLU B OE1 1 
ATOM   419  O OE2 . GLU A 1 64  ? 51.994 62.748  -28.811 1.00 47.03  ? 120 GLU B OE2 1 
ATOM   420  N N   . LEU A 1 65  ? 53.063 68.028  -32.970 1.00 24.27  ? 121 LEU B N   1 
ATOM   421  C CA  . LEU A 1 65  ? 53.083 69.435  -33.349 1.00 23.81  ? 121 LEU B CA  1 
ATOM   422  C C   . LEU A 1 65  ? 54.263 69.745  -34.247 1.00 31.33  ? 121 LEU B C   1 
ATOM   423  O O   . LEU A 1 65  ? 55.411 69.495  -33.885 1.00 32.54  ? 121 LEU B O   1 
ATOM   424  C CB  . LEU A 1 65  ? 53.121 70.347  -32.128 1.00 23.63  ? 121 LEU B CB  1 
ATOM   425  C CG  . LEU A 1 65  ? 53.043 71.856  -32.417 1.00 33.16  ? 121 LEU B CG  1 
ATOM   426  C CD1 . LEU A 1 65  ? 52.135 72.561  -31.422 1.00 33.09  ? 121 LEU B CD1 1 
ATOM   427  C CD2 . LEU A 1 65  ? 54.408 72.520  -32.397 1.00 33.97  ? 121 LEU B CD2 1 
ATOM   428  N N   . LEU A 1 66  ? 53.967 70.331  -35.399 1.00 26.62  ? 122 LEU B N   1 
ATOM   429  C CA  . LEU A 1 66  ? 54.981 70.817  -36.308 1.00 27.83  ? 122 LEU B CA  1 
ATOM   430  C C   . LEU A 1 66  ? 54.642 72.267  -36.634 1.00 28.33  ? 122 LEU B C   1 
ATOM   431  O O   . LEU A 1 66  ? 53.626 72.548  -37.267 1.00 23.08  ? 122 LEU B O   1 
ATOM   432  C CB  . LEU A 1 66  ? 54.968 69.980  -37.592 1.00 28.86  ? 122 LEU B CB  1 
ATOM   433  C CG  . LEU A 1 66  ? 56.052 70.290  -38.623 1.00 27.82  ? 122 LEU B CG  1 
ATOM   434  C CD1 . LEU A 1 66  ? 57.399 69.887  -38.048 1.00 27.17  ? 122 LEU B CD1 1 
ATOM   435  C CD2 . LEU A 1 66  ? 55.767 69.571  -39.937 1.00 25.78  ? 122 LEU B CD2 1 
ATOM   436  N N   . ASP A 1 67  ? 55.469 73.197  -36.177 1.00 31.90  ? 123 ASP B N   1 
ATOM   437  C CA  . ASP A 1 67  ? 55.242 74.587  -36.523 1.00 32.15  ? 123 ASP B CA  1 
ATOM   438  C C   . ASP A 1 67  ? 56.465 75.095  -37.244 1.00 36.74  ? 123 ASP B C   1 
ATOM   439  O O   . ASP A 1 67  ? 57.527 75.280  -36.645 1.00 36.58  ? 123 ASP B O   1 
ATOM   440  C CB  . ASP A 1 67  ? 54.950 75.427  -35.282 1.00 23.47  ? 123 ASP B CB  1 
ATOM   441  C CG  . ASP A 1 67  ? 54.734 76.895  -35.602 1.00 34.71  ? 123 ASP B CG  1 
ATOM   442  O OD1 . ASP A 1 67  ? 54.787 77.283  -36.787 1.00 37.30  ? 123 ASP B OD1 1 
ATOM   443  O OD2 . ASP A 1 67  ? 54.500 77.677  -34.661 1.00 39.87  ? 123 ASP B OD2 1 
ATOM   444  N N   . LEU A 1 68  ? 56.291 75.274  -38.549 1.00 35.30  ? 124 LEU B N   1 
ATOM   445  C CA  . LEU A 1 68  ? 57.269 75.875  -39.430 1.00 30.57  ? 124 LEU B CA  1 
ATOM   446  C C   . LEU A 1 68  ? 56.941 77.321  -39.810 1.00 33.34  ? 124 LEU B C   1 
ATOM   447  O O   . LEU A 1 68  ? 57.567 77.889  -40.716 1.00 31.36  ? 124 LEU B O   1 
ATOM   448  C CB  . LEU A 1 68  ? 57.528 74.973  -40.634 1.00 30.27  ? 124 LEU B CB  1 
ATOM   449  C CG  . LEU A 1 68  ? 58.032 73.599  -40.148 1.00 35.32  ? 124 LEU B CG  1 
ATOM   450  C CD1 . LEU A 1 68  ? 58.414 72.674  -41.309 1.00 32.62  ? 124 LEU B CD1 1 
ATOM   451  C CD2 . LEU A 1 68  ? 59.186 73.723  -39.145 1.00 27.52  ? 124 LEU B CD2 1 
ATOM   452  N N   . SER A 1 69  ? 55.929 77.894  -39.157 1.00 26.62  ? 125 SER B N   1 
ATOM   453  C CA  . SER A 1 69  ? 55.367 79.175  -39.601 1.00 29.76  ? 125 SER B CA  1 
ATOM   454  C C   . SER A 1 69  ? 56.324 80.355  -39.512 1.00 34.16  ? 125 SER B C   1 
ATOM   455  O O   . SER A 1 69  ? 57.348 80.292  -38.832 1.00 34.64  ? 125 SER B O   1 
ATOM   456  C CB  . SER A 1 69  ? 54.080 79.515  -38.856 1.00 27.21  ? 125 SER B CB  1 
ATOM   457  O OG  . SER A 1 69  ? 54.360 79.825  -37.504 1.00 32.08  ? 125 SER B OG  1 
ATOM   458  N N   . ASP A 1 70  ? 55.978 81.413  -40.245 1.00 40.97  ? 126 ASP B N   1 
ATOM   459  C CA  . ASP A 1 70  ? 56.736 82.669  -40.294 1.00 40.18  ? 126 ASP B CA  1 
ATOM   460  C C   . ASP A 1 70  ? 58.195 82.471  -40.716 1.00 39.21  ? 126 ASP B C   1 
ATOM   461  O O   . ASP A 1 70  ? 59.121 82.972  -40.081 1.00 39.62  ? 126 ASP B O   1 
ATOM   462  C CB  . ASP A 1 70  ? 56.632 83.436  -38.970 1.00 34.74  ? 126 ASP B CB  1 
ATOM   463  C CG  . ASP A 1 70  ? 57.136 84.874  -39.079 1.00 38.52  ? 126 ASP B CG  1 
ATOM   464  O OD1 . ASP A 1 70  ? 57.011 85.484  -40.165 1.00 32.14  ? 126 ASP B OD1 1 
ATOM   465  O OD2 . ASP A 1 70  ? 57.660 85.394  -38.066 1.00 48.76  ? 126 ASP B OD2 1 
ATOM   466  N N   . ASN A 1 71  ? 58.383 81.726  -41.796 1.00 33.78  ? 127 ASN B N   1 
ATOM   467  C CA  . ASN A 1 71  ? 59.694 81.580  -42.402 1.00 34.25  ? 127 ASN B CA  1 
ATOM   468  C C   . ASN A 1 71  ? 59.635 81.961  -43.872 1.00 37.38  ? 127 ASN B C   1 
ATOM   469  O O   . ASN A 1 71  ? 58.623 82.472  -44.360 1.00 37.09  ? 127 ASN B O   1 
ATOM   470  C CB  . ASN A 1 71  ? 60.196 80.144  -42.270 1.00 32.77  ? 127 ASN B CB  1 
ATOM   471  C CG  . ASN A 1 71  ? 60.791 79.864  -40.926 1.00 31.23  ? 127 ASN B CG  1 
ATOM   472  O OD1 . ASN A 1 71  ? 61.738 80.524  -40.515 1.00 40.58  ? 127 ASN B OD1 1 
ATOM   473  N ND2 . ASN A 1 71  ? 60.237 78.887  -40.220 1.00 27.60  ? 127 ASN B ND2 1 
ATOM   474  N N   . SER A 1 72  ? 60.749 81.758  -44.561 1.00 39.71  ? 128 SER B N   1 
ATOM   475  C CA  . SER A 1 72  ? 60.807 81.918  -46.008 1.00 38.56  ? 128 SER B CA  1 
ATOM   476  C C   . SER A 1 72  ? 60.738 80.629  -46.840 1.00 39.72  ? 128 SER B C   1 
ATOM   477  O O   . SER A 1 72  ? 61.047 80.660  -48.023 1.00 39.98  ? 128 SER B O   1 
ATOM   478  C CB  . SER A 1 72  ? 61.964 82.807  -46.435 1.00 38.33  ? 128 SER B CB  1 
ATOM   479  O OG  . SER A 1 72  ? 61.544 83.642  -47.495 1.00 40.14  ? 128 SER B OG  1 
ATOM   480  N N   . LEU A 1 73  ? 60.408 79.502  -46.210 1.00 39.78  ? 129 LEU B N   1 
ATOM   481  C CA  . LEU A 1 73  ? 60.406 78.187  -46.878 1.00 39.10  ? 129 LEU B CA  1 
ATOM   482  C C   . LEU A 1 73  ? 59.670 78.140  -48.223 1.00 41.51  ? 129 LEU B C   1 
ATOM   483  O O   . LEU A 1 73  ? 58.601 78.732  -48.389 1.00 39.54  ? 129 LEU B O   1 
ATOM   484  C CB  . LEU A 1 73  ? 59.802 77.116  -45.959 1.00 35.31  ? 129 LEU B CB  1 
ATOM   485  C CG  . LEU A 1 73  ? 60.368 76.992  -44.543 1.00 38.54  ? 129 LEU B CG  1 
ATOM   486  C CD1 . LEU A 1 73  ? 59.520 76.049  -43.690 1.00 28.65  ? 129 LEU B CD1 1 
ATOM   487  C CD2 . LEU A 1 73  ? 61.828 76.538  -44.583 1.00 44.23  ? 129 LEU B CD2 1 
ATOM   488  N N   . SER A 1 74  ? 60.262 77.421  -49.175 1.00 42.58  ? 130 SER B N   1 
ATOM   489  C CA  . SER A 1 74  ? 59.709 77.281  -50.522 1.00 38.59  ? 130 SER B CA  1 
ATOM   490  C C   . SER A 1 74  ? 59.538 75.805  -50.900 1.00 37.69  ? 130 SER B C   1 
ATOM   491  O O   . SER A 1 74  ? 59.764 74.915  -50.072 1.00 38.68  ? 130 SER B O   1 
ATOM   492  C CB  . SER A 1 74  ? 60.597 78.002  -51.549 1.00 35.34  ? 130 SER B CB  1 
ATOM   493  O OG  . SER A 1 74  ? 61.978 77.734  -51.327 1.00 39.19  ? 130 SER B OG  1 
ATOM   494  N N   . GLY A 1 75  ? 59.128 75.556  -52.144 1.00 32.18  ? 131 GLY B N   1 
ATOM   495  C CA  . GLY A 1 75  ? 58.876 74.205  -52.621 1.00 27.07  ? 131 GLY B CA  1 
ATOM   496  C C   . GLY A 1 75  ? 57.520 73.635  -52.233 1.00 33.85  ? 131 GLY B C   1 
ATOM   497  O O   . GLY A 1 75  ? 56.657 74.351  -51.735 1.00 42.54  ? 131 GLY B O   1 
ATOM   498  N N   . ASP A 1 76  ? 57.339 72.338  -52.467 1.00 40.65  ? 132 ASP B N   1 
ATOM   499  C CA  . ASP A 1 76  ? 56.122 71.613  -52.088 1.00 40.88  ? 132 ASP B CA  1 
ATOM   500  C C   . ASP A 1 76  ? 55.981 71.334  -50.597 1.00 36.16  ? 132 ASP B C   1 
ATOM   501  O O   . ASP A 1 76  ? 56.949 71.387  -49.842 1.00 37.37  ? 132 ASP B O   1 
ATOM   502  C CB  . ASP A 1 76  ? 56.052 70.275  -52.819 1.00 49.31  ? 132 ASP B CB  1 
ATOM   503  C CG  . ASP A 1 76  ? 55.543 70.417  -54.221 1.00 57.41  ? 132 ASP B CG  1 
ATOM   504  O OD1 . ASP A 1 76  ? 55.905 71.419  -54.872 1.00 63.63  ? 132 ASP B OD1 1 
ATOM   505  O OD2 . ASP A 1 76  ? 54.773 69.538  -54.665 1.00 59.23  ? 132 ASP B OD2 1 
ATOM   506  N N   . ILE A 1 77  ? 54.754 71.040  -50.182 1.00 34.09  ? 133 ILE B N   1 
ATOM   507  C CA  . ILE A 1 77  ? 54.526 70.449  -48.879 1.00 30.46  ? 133 ILE B CA  1 
ATOM   508  C C   . ILE A 1 77  ? 54.669 68.955  -49.108 1.00 29.68  ? 133 ILE B C   1 
ATOM   509  O O   . ILE A 1 77  ? 53.770 68.326  -49.675 1.00 27.41  ? 133 ILE B O   1 
ATOM   510  C CB  . ILE A 1 77  ? 53.093 70.722  -48.386 1.00 25.23  ? 133 ILE B CB  1 
ATOM   511  C CG1 . ILE A 1 77  ? 52.874 72.219  -48.170 1.00 22.54  ? 133 ILE B CG1 1 
ATOM   512  C CG2 . ILE A 1 77  ? 52.795 69.926  -47.108 1.00 23.67  ? 133 ILE B CG2 1 
ATOM   513  C CD1 . ILE A 1 77  ? 51.428 72.582  -47.838 1.00 25.46  ? 133 ILE B CD1 1 
ATOM   514  N N   . PRO A 1 78  ? 55.791 68.375  -48.654 1.00 26.29  ? 134 PRO B N   1 
ATOM   515  C CA  . PRO A 1 78  ? 56.091 66.976  -48.960 1.00 27.08  ? 134 PRO B CA  1 
ATOM   516  C C   . PRO A 1 78  ? 54.969 66.058  -48.488 1.00 34.15  ? 134 PRO B C   1 
ATOM   517  O O   . PRO A 1 78  ? 54.394 66.259  -47.418 1.00 37.67  ? 134 PRO B O   1 
ATOM   518  C CB  . PRO A 1 78  ? 57.373 66.709  -48.165 1.00 28.25  ? 134 PRO B CB  1 
ATOM   519  C CG  . PRO A 1 78  ? 57.974 68.035  -47.963 1.00 28.97  ? 134 PRO B CG  1 
ATOM   520  C CD  . PRO A 1 78  ? 56.832 68.994  -47.824 1.00 26.92  ? 134 PRO B CD  1 
ATOM   521  N N   . VAL A 1 79  ? 54.661 65.062  -49.304 1.00 27.93  ? 135 VAL B N   1 
ATOM   522  C CA  . VAL A 1 79  ? 53.603 64.097  -49.030 1.00 29.70  ? 135 VAL B CA  1 
ATOM   523  C C   . VAL A 1 79  ? 53.934 63.282  -47.777 1.00 34.01  ? 135 VAL B C   1 
ATOM   524  O O   . VAL A 1 79  ? 53.043 62.883  -47.020 1.00 26.19  ? 135 VAL B O   1 
ATOM   525  C CB  . VAL A 1 79  ? 53.409 63.181  -50.276 1.00 41.53  ? 135 VAL B CB  1 
ATOM   526  C CG1 . VAL A 1 79  ? 52.603 61.937  -49.959 1.00 26.32  ? 135 VAL B CG1 1 
ATOM   527  C CG2 . VAL A 1 79  ? 52.770 63.976  -51.424 1.00 35.38  ? 135 VAL B CG2 1 
ATOM   528  N N   . GLU A 1 80  ? 55.232 63.078  -47.558 1.00 37.07  ? 136 GLU B N   1 
ATOM   529  C CA  . GLU A 1 80  ? 55.760 62.353  -46.405 1.00 38.02  ? 136 GLU B CA  1 
ATOM   530  C C   . GLU A 1 80  ? 55.360 62.976  -45.055 1.00 38.91  ? 136 GLU B C   1 
ATOM   531  O O   . GLU A 1 80  ? 55.272 62.282  -44.040 1.00 37.72  ? 136 GLU B O   1 
ATOM   532  C CB  . GLU A 1 80  ? 57.293 62.249  -46.506 1.00 39.41  ? 136 GLU B CB  1 
ATOM   533  C CG  . GLU A 1 80  ? 57.818 61.316  -47.613 1.00 39.95  ? 136 GLU B CG  1 
ATOM   534  C CD  . GLU A 1 80  ? 57.632 61.859  -49.041 1.00 40.29  ? 136 GLU B CD  1 
ATOM   535  O OE1 . GLU A 1 80  ? 57.246 63.043  -49.207 1.00 29.65  ? 136 GLU B OE1 1 
ATOM   536  O OE2 . GLU A 1 80  ? 57.867 61.085  -50.000 1.00 36.38  ? 136 GLU B OE2 1 
ATOM   537  N N   . ILE A 1 81  ? 55.132 64.285  -45.042 1.00 33.45  ? 137 ILE B N   1 
ATOM   538  C CA  . ILE A 1 81  ? 54.637 64.960  -43.842 1.00 32.30  ? 137 ILE B CA  1 
ATOM   539  C C   . ILE A 1 81  ? 53.348 64.310  -43.330 1.00 33.98  ? 137 ILE B C   1 
ATOM   540  O O   . ILE A 1 81  ? 53.088 64.296  -42.122 1.00 36.91  ? 137 ILE B O   1 
ATOM   541  C CB  . ILE A 1 81  ? 54.432 66.479  -44.099 1.00 31.42  ? 137 ILE B CB  1 
ATOM   542  C CG1 . ILE A 1 81  ? 55.602 67.282  -43.532 1.00 31.86  ? 137 ILE B CG1 1 
ATOM   543  C CG2 . ILE A 1 81  ? 53.125 66.982  -43.511 1.00 24.47  ? 137 ILE B CG2 1 
ATOM   544  C CD1 . ILE A 1 81  ? 55.513 68.754  -43.849 1.00 25.81  ? 137 ILE B CD1 1 
ATOM   545  N N   . PHE A 1 82  ? 52.571 63.726  -44.244 1.00 33.56  ? 138 PHE B N   1 
ATOM   546  C CA  . PHE A 1 82  ? 51.290 63.105  -43.885 1.00 37.78  ? 138 PHE B CA  1 
ATOM   547  C C   . PHE A 1 82  ? 51.440 61.644  -43.446 1.00 42.69  ? 138 PHE B C   1 
ATOM   548  O O   . PHE A 1 82  ? 50.451 60.926  -43.260 1.00 39.07  ? 138 PHE B O   1 
ATOM   549  C CB  . PHE A 1 82  ? 50.261 63.263  -45.004 1.00 40.53  ? 138 PHE B CB  1 
ATOM   550  C CG  . PHE A 1 82  ? 50.134 64.675  -45.489 1.00 44.62  ? 138 PHE B CG  1 
ATOM   551  C CD1 . PHE A 1 82  ? 49.638 65.661  -44.657 1.00 43.89  ? 138 PHE B CD1 1 
ATOM   552  C CD2 . PHE A 1 82  ? 50.542 65.025  -46.759 1.00 45.86  ? 138 PHE B CD2 1 
ATOM   553  C CE1 . PHE A 1 82  ? 49.539 66.963  -45.087 1.00 40.79  ? 138 PHE B CE1 1 
ATOM   554  C CE2 . PHE A 1 82  ? 50.446 66.334  -47.190 1.00 45.15  ? 138 PHE B CE2 1 
ATOM   555  C CZ  . PHE A 1 82  ? 49.945 67.299  -46.356 1.00 42.46  ? 138 PHE B CZ  1 
ATOM   556  N N   . ARG A 1 83  ? 52.688 61.206  -43.307 1.00 44.68  ? 139 ARG B N   1 
ATOM   557  C CA  . ARG A 1 83  ? 52.974 59.938  -42.657 1.00 45.36  ? 139 ARG B CA  1 
ATOM   558  C C   . ARG A 1 83  ? 52.868 60.059  -41.134 1.00 42.63  ? 139 ARG B C   1 
ATOM   559  O O   . ARG A 1 83  ? 52.871 59.044  -40.437 1.00 44.16  ? 139 ARG B O   1 
ATOM   560  C CB  . ARG A 1 83  ? 54.369 59.428  -43.034 1.00 50.78  ? 139 ARG B CB  1 
ATOM   561  C CG  . ARG A 1 83  ? 54.536 58.998  -44.490 1.00 54.31  ? 139 ARG B CG  1 
ATOM   562  C CD  . ARG A 1 83  ? 55.987 58.586  -44.746 1.00 63.05  ? 139 ARG B CD  1 
ATOM   563  N NE  . ARG A 1 83  ? 56.232 58.108  -46.108 1.00 63.73  ? 139 ARG B NE  1 
ATOM   564  C CZ  . ARG A 1 83  ? 57.448 57.937  -46.617 1.00 58.14  ? 139 ARG B CZ  1 
ATOM   565  N NH1 . ARG A 1 83  ? 58.513 58.220  -45.875 1.00 59.59  ? 139 ARG B NH1 1 
ATOM   566  N NH2 . ARG A 1 83  ? 57.605 57.494  -47.858 1.00 54.36  ? 139 ARG B NH2 1 
ATOM   567  N N   . LEU A 1 84  ? 52.730 61.280  -40.610 1.00 39.07  ? 140 LEU B N   1 
ATOM   568  C CA  . LEU A 1 84  ? 52.797 61.447  -39.163 1.00 36.72  ? 140 LEU B CA  1 
ATOM   569  C C   . LEU A 1 84  ? 51.396 61.301  -38.610 1.00 35.08  ? 140 LEU B C   1 
ATOM   570  O O   . LEU A 1 84  ? 50.643 62.265  -38.524 1.00 29.20  ? 140 LEU B O   1 
ATOM   571  C CB  . LEU A 1 84  ? 53.301 62.857  -38.827 1.00 26.15  ? 140 LEU B CB  1 
ATOM   572  C CG  . LEU A 1 84  ? 54.581 63.382  -39.476 1.00 27.02  ? 140 LEU B CG  1 
ATOM   573  C CD1 . LEU A 1 84  ? 54.772 64.864  -39.246 1.00 32.09  ? 140 LEU B CD1 1 
ATOM   574  C CD2 . LEU A 1 84  ? 55.780 62.630  -38.986 1.00 28.34  ? 140 LEU B CD2 1 
ATOM   575  N N   . LYS A 1 85  ? 51.105 60.124  -38.078 1.00 38.02  ? 141 LYS B N   1 
ATOM   576  C CA  . LYS A 1 85  ? 49.718 59.737  -37.861 1.00 37.98  ? 141 LYS B CA  1 
ATOM   577  C C   . LYS A 1 85  ? 49.162 60.358  -36.579 1.00 36.33  ? 141 LYS B C   1 
ATOM   578  O O   . LYS A 1 85  ? 47.955 60.391  -36.370 1.00 39.23  ? 141 LYS B O   1 
ATOM   579  C CB  . LYS A 1 85  ? 49.595 58.203  -37.844 1.00 42.50  ? 141 LYS B CB  1 
ATOM   580  C CG  . LYS A 1 85  ? 48.359 57.638  -38.545 1.00 49.96  ? 141 LYS B CG  1 
ATOM   581  C CD  . LYS A 1 85  ? 48.446 57.796  -40.054 1.00 61.59  ? 141 LYS B CD  1 
ATOM   582  C CE  . LYS A 1 85  ? 47.147 57.374  -40.747 1.00 68.55  ? 141 LYS B CE  1 
ATOM   583  N NZ  . LYS A 1 85  ? 46.862 55.919  -40.649 1.00 73.32  ? 141 LYS B NZ  1 
ATOM   584  N N   . LYS A 1 86  ? 50.059 60.827  -35.719 1.00 37.38  ? 142 LYS B N   1 
ATOM   585  C CA  . LYS A 1 86  ? 49.693 61.414  -34.430 1.00 31.37  ? 142 LYS B CA  1 
ATOM   586  C C   . LYS A 1 86  ? 49.670 62.936  -34.437 1.00 30.99  ? 142 LYS B C   1 
ATOM   587  O O   . LYS A 1 86  ? 49.557 63.566  -33.387 1.00 39.45  ? 142 LYS B O   1 
ATOM   588  C CB  . LYS A 1 86  ? 50.613 60.890  -33.320 1.00 34.09  ? 142 LYS B CB  1 
ATOM   589  C CG  . LYS A 1 86  ? 50.510 59.384  -33.131 1.00 34.83  ? 142 LYS B CG  1 
ATOM   590  C CD  . LYS A 1 86  ? 51.556 58.837  -32.181 1.00 40.62  ? 142 LYS B CD  1 
ATOM   591  C CE  . LYS A 1 86  ? 51.363 57.337  -31.997 1.00 46.33  ? 142 LYS B CE  1 
ATOM   592  N NZ  . LYS A 1 86  ? 51.949 56.829  -30.719 1.00 53.84  ? 142 LYS B NZ  1 
ATOM   593  N N   . LEU A 1 87  ? 49.851 63.531  -35.605 1.00 28.23  ? 143 LEU B N   1 
ATOM   594  C CA  . LEU A 1 87  ? 49.912 64.980  -35.692 1.00 24.49  ? 143 LEU B CA  1 
ATOM   595  C C   . LEU A 1 87  ? 48.564 65.614  -35.355 1.00 23.69  ? 143 LEU B C   1 
ATOM   596  O O   . LEU A 1 87  ? 47.521 65.148  -35.818 1.00 22.55  ? 143 LEU B O   1 
ATOM   597  C CB  . LEU A 1 87  ? 50.358 65.401  -37.082 1.00 25.81  ? 143 LEU B CB  1 
ATOM   598  C CG  . LEU A 1 87  ? 50.879 66.824  -37.155 1.00 25.28  ? 143 LEU B CG  1 
ATOM   599  C CD1 . LEU A 1 87  ? 52.181 66.904  -36.387 1.00 23.78  ? 143 LEU B CD1 1 
ATOM   600  C CD2 . LEU A 1 87  ? 51.063 67.234  -38.618 1.00 24.77  ? 143 LEU B CD2 1 
ATOM   601  N N   . LYS A 1 88  ? 48.610 66.673  -34.545 1.00 21.07  ? 144 LYS B N   1 
ATOM   602  C CA  . LYS A 1 88  ? 47.434 67.406  -34.070 1.00 19.94  ? 144 LYS B CA  1 
ATOM   603  C C   . LYS A 1 88  ? 47.423 68.856  -34.562 1.00 22.58  ? 144 LYS B C   1 
ATOM   604  O O   . LYS A 1 88  ? 46.389 69.365  -34.997 1.00 24.86  ? 144 LYS B O   1 
ATOM   605  C CB  . LYS A 1 88  ? 47.227 67.278  -32.559 1.00 19.88  ? 144 LYS B CB  1 
ATOM   606  C CG  . LYS A 1 88  ? 46.678 65.917  -32.146 1.00 25.82  ? 144 LYS B CG  1 
ATOM   607  C CD  . LYS A 1 88  ? 46.748 65.706  -30.639 1.00 33.68  ? 144 LYS B CD  1 
ATOM   608  C CE  . LYS A 1 88  ? 45.758 66.613  -29.888 1.00 39.87  ? 144 LYS B CE  1 
ATOM   609  N NZ  . LYS A 1 88  ? 46.035 66.736  -28.413 1.00 38.36  ? 144 LYS B NZ  1 
ATOM   610  N N   . THR A 1 89  ? 48.525 69.562  -34.357 1.00 20.04  ? 145 THR B N   1 
ATOM   611  C CA  . THR A 1 89  ? 48.715 70.855  -35.008 1.00 19.75  ? 145 THR B CA  1 
ATOM   612  C C   . THR A 1 89  ? 49.676 70.746  -36.186 1.00 24.09  ? 145 THR B C   1 
ATOM   613  O O   . THR A 1 89  ? 50.771 70.190  -36.055 1.00 28.22  ? 145 THR B O   1 
ATOM   614  C CB  . THR A 1 89  ? 49.309 71.888  -34.039 1.00 24.86  ? 145 THR B CB  1 
ATOM   615  O OG1 . THR A 1 89  ? 48.440 72.038  -32.915 1.00 23.57  ? 145 THR B OG1 1 
ATOM   616  C CG2 . THR A 1 89  ? 49.469 73.227  -34.724 1.00 24.68  ? 145 THR B CG2 1 
ATOM   617  N N   . LEU A 1 90  ? 49.262 71.261  -37.341 1.00 22.94  ? 146 LEU B N   1 
ATOM   618  C CA  . LEU A 1 90  ? 50.183 71.467  -38.454 1.00 27.20  ? 146 LEU B CA  1 
ATOM   619  C C   . LEU A 1 90  ? 50.164 72.940  -38.827 1.00 20.12  ? 146 LEU B C   1 
ATOM   620  O O   . LEU A 1 90  ? 49.173 73.426  -39.341 1.00 19.20  ? 146 LEU B O   1 
ATOM   621  C CB  . LEU A 1 90  ? 49.793 70.614  -39.665 1.00 25.50  ? 146 LEU B CB  1 
ATOM   622  C CG  . LEU A 1 90  ? 50.678 70.794  -40.919 1.00 25.21  ? 146 LEU B CG  1 
ATOM   623  C CD1 . LEU A 1 90  ? 52.126 70.446  -40.621 1.00 22.44  ? 146 LEU B CD1 1 
ATOM   624  C CD2 . LEU A 1 90  ? 50.172 69.985  -42.087 1.00 21.07  ? 146 LEU B CD2 1 
ATOM   625  N N   . SER A 1 91  ? 51.255 73.650  -38.550 1.00 35.25  ? 147 SER B N   1 
ATOM   626  C CA  . SER A 1 91  ? 51.319 75.080  -38.818 1.00 29.43  ? 147 SER B CA  1 
ATOM   627  C C   . SER A 1 91  ? 52.395 75.357  -39.867 1.00 30.49  ? 147 SER B C   1 
ATOM   628  O O   . SER A 1 91  ? 53.582 75.416  -39.555 1.00 40.49  ? 147 SER B O   1 
ATOM   629  C CB  . SER A 1 91  ? 51.689 75.788  -37.505 1.00 23.12  ? 147 SER B CB  1 
ATOM   630  O OG  . SER A 1 91  ? 50.950 76.974  -37.284 1.00 25.89  ? 147 SER B OG  1 
ATOM   631  N N   . LEU A 1 92  ? 51.980 75.527  -41.114 1.00 24.16  ? 148 LEU B N   1 
ATOM   632  C CA  . LEU A 1 92  ? 52.894 75.891  -42.198 1.00 21.33  ? 148 LEU B CA  1 
ATOM   633  C C   . LEU A 1 92  ? 52.763 77.314  -42.742 1.00 30.42  ? 148 LEU B C   1 
ATOM   634  O O   . LEU A 1 92  ? 53.378 77.650  -43.747 1.00 21.20  ? 148 LEU B O   1 
ATOM   635  C CB  . LEU A 1 92  ? 52.855 74.859  -43.316 1.00 21.61  ? 148 LEU B CB  1 
ATOM   636  C CG  . LEU A 1 92  ? 53.122 73.434  -42.842 1.00 25.14  ? 148 LEU B CG  1 
ATOM   637  C CD1 . LEU A 1 92  ? 52.961 72.467  -44.009 1.00 25.52  ? 148 LEU B CD1 1 
ATOM   638  C CD2 . LEU A 1 92  ? 54.503 73.316  -42.208 1.00 23.44  ? 148 LEU B CD2 1 
ATOM   639  N N   . ASN A 1 93  ? 51.910 78.118  -42.120 1.00 19.91  ? 149 ASN B N   1 
ATOM   640  C CA  . ASN A 1 93  ? 51.525 79.424  -42.660 1.00 19.25  ? 149 ASN B CA  1 
ATOM   641  C C   . ASN A 1 93  ? 52.688 80.416  -42.792 1.00 19.91  ? 149 ASN B C   1 
ATOM   642  O O   . ASN A 1 93  ? 53.739 80.226  -42.198 1.00 20.82  ? 149 ASN B O   1 
ATOM   643  C CB  . ASN A 1 93  ? 50.403 80.031  -41.811 1.00 18.23  ? 149 ASN B CB  1 
ATOM   644  C CG  . ASN A 1 93  ? 50.799 80.178  -40.355 1.00 18.53  ? 149 ASN B CG  1 
ATOM   645  O OD1 . ASN A 1 93  ? 50.739 79.224  -39.586 1.00 19.73  ? 149 ASN B OD1 1 
ATOM   646  N ND2 . ASN A 1 93  ? 51.221 81.373  -39.975 1.00 20.25  ? 149 ASN B ND2 1 
ATOM   647  N N   . THR A 1 94  ? 52.497 81.444  -43.616 1.00 24.46  ? 150 THR B N   1 
ATOM   648  C CA  . THR A 1 94  ? 53.481 82.514  -43.819 1.00 19.99  ? 150 THR B CA  1 
ATOM   649  C C   . THR A 1 94  ? 54.831 82.008  -44.308 1.00 23.27  ? 150 THR B C   1 
ATOM   650  O O   . THR A 1 94  ? 55.852 82.113  -43.621 1.00 23.18  ? 150 THR B O   1 
ATOM   651  C CB  . THR A 1 94  ? 53.694 83.346  -42.563 1.00 28.70  ? 150 THR B CB  1 
ATOM   652  O OG1 . THR A 1 94  ? 52.475 83.381  -41.813 1.00 29.82  ? 150 THR B OG1 1 
ATOM   653  C CG2 . THR A 1 94  ? 54.121 84.768  -42.941 1.00 20.01  ? 150 THR B CG2 1 
ATOM   654  N N   . ASN A 1 95  ? 54.812 81.456  -45.509 1.00 24.23  ? 151 ASN B N   1 
ATOM   655  C CA  . ASN A 1 95  ? 56.007 80.999  -46.176 1.00 28.86  ? 151 ASN B CA  1 
ATOM   656  C C   . ASN A 1 95  ? 55.824 81.246  -47.666 1.00 31.29  ? 151 ASN B C   1 
ATOM   657  O O   . ASN A 1 95  ? 54.895 81.945  -48.078 1.00 35.01  ? 151 ASN B O   1 
ATOM   658  C CB  . ASN A 1 95  ? 56.229 79.510  -45.912 1.00 28.16  ? 151 ASN B CB  1 
ATOM   659  C CG  . ASN A 1 95  ? 56.820 79.241  -44.551 1.00 32.76  ? 151 ASN B CG  1 
ATOM   660  O OD1 . ASN A 1 95  ? 57.972 79.573  -44.293 1.00 24.54  ? 151 ASN B OD1 1 
ATOM   661  N ND2 . ASN A 1 95  ? 56.043 78.614  -43.677 1.00 34.27  ? 151 ASN B ND2 1 
ATOM   662  N N   . ASN A 1 96  ? 56.734 80.704  -48.460 1.00 23.11  ? 152 ASN B N   1 
ATOM   663  C CA  . ASN A 1 96  ? 56.622 80.710  -49.917 1.00 32.08  ? 152 ASN B CA  1 
ATOM   664  C C   . ASN A 1 96  ? 56.095 79.415  -50.544 1.00 35.86  ? 152 ASN B C   1 
ATOM   665  O O   . ASN A 1 96  ? 56.271 79.179  -51.743 1.00 42.23  ? 152 ASN B O   1 
ATOM   666  C CB  . ASN A 1 96  ? 57.901 81.214  -50.564 1.00 34.08  ? 152 ASN B CB  1 
ATOM   667  C CG  . ASN A 1 96  ? 58.196 82.647  -50.182 1.00 38.98  ? 152 ASN B CG  1 
ATOM   668  O OD1 . ASN A 1 96  ? 57.279 83.465  -50.071 1.00 41.12  ? 152 ASN B OD1 1 
ATOM   669  N ND2 . ASN A 1 96  ? 59.472 82.956  -49.946 1.00 38.50  ? 152 ASN B ND2 1 
ATOM   670  N N   . LEU A 1 97  ? 55.552 78.537  -49.704 1.00 23.89  ? 153 LEU B N   1 
ATOM   671  C CA  . LEU A 1 97  ? 55.179 77.189  -50.125 1.00 23.77  ? 153 LEU B CA  1 
ATOM   672  C C   . LEU A 1 97  ? 54.286 77.111  -51.366 1.00 23.01  ? 153 LEU B C   1 
ATOM   673  O O   . LEU A 1 97  ? 53.254 77.771  -51.442 1.00 26.70  ? 153 LEU B O   1 
ATOM   674  C CB  . LEU A 1 97  ? 54.557 76.441  -48.946 1.00 22.55  ? 153 LEU B CB  1 
ATOM   675  C CG  . LEU A 1 97  ? 55.603 76.200  -47.860 1.00 23.46  ? 153 LEU B CG  1 
ATOM   676  C CD1 . LEU A 1 97  ? 54.975 75.836  -46.533 1.00 23.04  ? 153 LEU B CD1 1 
ATOM   677  C CD2 . LEU A 1 97  ? 56.569 75.123  -48.320 1.00 24.62  ? 153 LEU B CD2 1 
ATOM   678  N N   . GLU A 1 98  ? 54.698 76.299  -52.338 1.00 30.36  ? 154 GLU B N   1 
ATOM   679  C CA  . GLU A 1 98  ? 53.949 76.151  -53.596 1.00 30.30  ? 154 GLU B CA  1 
ATOM   680  C C   . GLU A 1 98  ? 53.439 74.724  -53.792 1.00 23.12  ? 154 GLU B C   1 
ATOM   681  O O   . GLU A 1 98  ? 53.710 73.850  -52.975 1.00 27.37  ? 154 GLU B O   1 
ATOM   682  C CB  . GLU A 1 98  ? 54.796 76.587  -54.794 1.00 29.84  ? 154 GLU B CB  1 
ATOM   683  C CG  . GLU A 1 98  ? 56.206 76.010  -54.799 1.00 44.89  ? 154 GLU B CG  1 
ATOM   684  C CD  . GLU A 1 98  ? 56.979 76.309  -56.085 1.00 59.78  ? 154 GLU B CD  1 
ATOM   685  O OE1 . GLU A 1 98  ? 56.360 76.738  -57.090 1.00 58.23  ? 154 GLU B OE1 1 
ATOM   686  O OE2 . GLU A 1 98  ? 58.215 76.103  -56.087 1.00 67.77  ? 154 GLU B OE2 1 
ATOM   687  N N   . GLY A 1 99  ? 52.690 74.491  -54.864 1.00 21.98  ? 155 GLY B N   1 
ATOM   688  C CA  . GLY A 1 99  ? 52.111 73.178  -55.105 1.00 27.67  ? 155 GLY B CA  1 
ATOM   689  C C   . GLY A 1 99  ? 50.653 72.974  -54.701 1.00 28.63  ? 155 GLY B C   1 
ATOM   690  O O   . GLY A 1 99  ? 49.963 73.907  -54.293 1.00 31.47  ? 155 GLY B O   1 
ATOM   691  N N   . HIS A 1 100 ? 50.171 71.747  -54.870 1.00 25.16  ? 156 HIS B N   1 
ATOM   692  C CA  . HIS A 1 100 ? 48.863 71.342  -54.372 1.00 20.22  ? 156 HIS B CA  1 
ATOM   693  C C   . HIS A 1 100 ? 48.909 70.935  -52.897 1.00 33.78  ? 156 HIS B C   1 
ATOM   694  O O   . HIS A 1 100 ? 49.957 70.564  -52.375 1.00 38.48  ? 156 HIS B O   1 
ATOM   695  C CB  . HIS A 1 100 ? 48.283 70.200  -55.209 1.00 20.29  ? 156 HIS B CB  1 
ATOM   696  C CG  . HIS A 1 100 ? 47.940 70.591  -56.614 1.00 46.53  ? 156 HIS B CG  1 
ATOM   697  N ND1 . HIS A 1 100 ? 47.109 69.835  -57.415 1.00 47.54  ? 156 HIS B ND1 1 
ATOM   698  C CD2 . HIS A 1 100 ? 48.320 71.654  -57.365 1.00 48.27  ? 156 HIS B CD2 1 
ATOM   699  C CE1 . HIS A 1 100 ? 46.987 70.418  -58.596 1.00 50.06  ? 156 HIS B CE1 1 
ATOM   700  N NE2 . HIS A 1 100 ? 47.713 71.522  -58.593 1.00 49.19  ? 156 HIS B NE2 1 
ATOM   701  N N   . ILE A 1 101 ? 47.773 71.031  -52.220 1.00 28.68  ? 157 ILE B N   1 
ATOM   702  C CA  . ILE A 1 101 ? 47.618 70.345  -50.957 1.00 27.93  ? 157 ILE B CA  1 
ATOM   703  C C   . ILE A 1 101 ? 47.327 68.899  -51.323 1.00 30.37  ? 157 ILE B C   1 
ATOM   704  O O   . ILE A 1 101 ? 46.286 68.608  -51.909 1.00 28.16  ? 157 ILE B O   1 
ATOM   705  C CB  . ILE A 1 101 ? 46.441 70.896  -50.139 1.00 27.76  ? 157 ILE B CB  1 
ATOM   706  C CG1 . ILE A 1 101 ? 46.573 72.412  -49.939 1.00 26.76  ? 157 ILE B CG1 1 
ATOM   707  C CG2 . ILE A 1 101 ? 46.359 70.189  -48.796 1.00 27.07  ? 157 ILE B CG2 1 
ATOM   708  C CD1 . ILE A 1 101 ? 45.376 73.040  -49.275 1.00 16.88  ? 157 ILE B CD1 1 
ATOM   709  N N   . PRO A 1 102 ? 48.251 67.987  -50.982 1.00 29.58  ? 158 PRO B N   1 
ATOM   710  C CA  . PRO A 1 102 ? 48.188 66.562  -51.337 1.00 24.46  ? 158 PRO B CA  1 
ATOM   711  C C   . PRO A 1 102 ? 46.912 65.890  -50.797 1.00 30.39  ? 158 PRO B C   1 
ATOM   712  O O   . PRO A 1 102 ? 46.455 66.306  -49.739 1.00 31.59  ? 158 PRO B O   1 
ATOM   713  C CB  . PRO A 1 102 ? 49.419 65.985  -50.628 1.00 30.71  ? 158 PRO B CB  1 
ATOM   714  C CG  . PRO A 1 102 ? 50.323 67.174  -50.389 1.00 29.01  ? 158 PRO B CG  1 
ATOM   715  C CD  . PRO A 1 102 ? 49.394 68.287  -50.102 1.00 27.41  ? 158 PRO B CD  1 
ATOM   716  N N   . MET A 1 103 ? 46.362 64.885  -51.488 1.00 27.50  ? 159 MET B N   1 
ATOM   717  C CA  . MET A 1 103 ? 45.191 64.154  -50.986 1.00 25.43  ? 159 MET B CA  1 
ATOM   718  C C   . MET A 1 103 ? 45.499 63.419  -49.685 1.00 32.33  ? 159 MET B C   1 
ATOM   719  O O   . MET A 1 103 ? 44.633 63.269  -48.808 1.00 34.59  ? 159 MET B O   1 
ATOM   720  C CB  . MET A 1 103 ? 44.694 63.129  -52.002 1.00 33.31  ? 159 MET B CB  1 
ATOM   721  C CG  . MET A 1 103 ? 44.277 63.707  -53.353 1.00 44.06  ? 159 MET B CG  1 
ATOM   722  S SD  . MET A 1 103 ? 42.791 64.749  -53.328 1.00 214.61 ? 159 MET B SD  1 
ATOM   723  C CE  . MET A 1 103 ? 41.506 63.600  -52.832 1.00 52.46  ? 159 MET B CE  1 
ATOM   724  N N   . GLU A 1 104 ? 46.750 62.996  -49.533 1.00 35.25  ? 160 GLU B N   1 
ATOM   725  C CA  . GLU A 1 104 ? 47.128 62.167  -48.395 1.00 32.61  ? 160 GLU B CA  1 
ATOM   726  C C   . GLU A 1 104 ? 46.915 62.910  -47.093 1.00 32.50  ? 160 GLU B C   1 
ATOM   727  O O   . GLU A 1 104 ? 47.105 62.347  -46.029 1.00 36.84  ? 160 GLU B O   1 
ATOM   728  C CB  . GLU A 1 104 ? 48.586 61.710  -48.483 1.00 35.96  ? 160 GLU B CB  1 
ATOM   729  C CG  . GLU A 1 104 ? 48.869 60.706  -49.573 1.00 43.71  ? 160 GLU B CG  1 
ATOM   730  C CD  . GLU A 1 104 ? 49.159 61.359  -50.914 1.00 49.01  ? 160 GLU B CD  1 
ATOM   731  O OE1 . GLU A 1 104 ? 49.059 62.602  -51.021 1.00 48.50  ? 160 GLU B OE1 1 
ATOM   732  O OE2 . GLU A 1 104 ? 49.494 60.621  -51.863 1.00 51.91  ? 160 GLU B OE2 1 
ATOM   733  N N   . ILE A 1 105 ? 46.554 64.186  -47.177 1.00 34.20  ? 161 ILE B N   1 
ATOM   734  C CA  . ILE A 1 105 ? 46.273 64.963  -45.979 1.00 31.25  ? 161 ILE B CA  1 
ATOM   735  C C   . ILE A 1 105 ? 45.138 64.332  -45.192 1.00 27.77  ? 161 ILE B C   1 
ATOM   736  O O   . ILE A 1 105 ? 45.109 64.415  -43.964 1.00 29.27  ? 161 ILE B O   1 
ATOM   737  C CB  . ILE A 1 105 ? 45.951 66.445  -46.278 1.00 30.84  ? 161 ILE B CB  1 
ATOM   738  C CG1 . ILE A 1 105 ? 46.056 67.262  -44.989 1.00 19.11  ? 161 ILE B CG1 1 
ATOM   739  C CG2 . ILE A 1 105 ? 44.570 66.597  -46.936 1.00 25.47  ? 161 ILE B CG2 1 
ATOM   740  C CD1 . ILE A 1 105 ? 45.720 68.701  -45.155 1.00 21.94  ? 161 ILE B CD1 1 
ATOM   741  N N   . GLY A 1 106 ? 44.230 63.656  -45.886 1.00 26.94  ? 162 GLY B N   1 
ATOM   742  C CA  . GLY A 1 106 ? 43.140 62.982  -45.199 1.00 28.18  ? 162 GLY B CA  1 
ATOM   743  C C   . GLY A 1 106 ? 43.620 61.848  -44.300 1.00 29.00  ? 162 GLY B C   1 
ATOM   744  O O   . GLY A 1 106 ? 42.841 61.252  -43.556 1.00 27.30  ? 162 GLY B O   1 
ATOM   745  N N   . ASN A 1 107 ? 44.908 61.539  -44.368 1.00 31.90  ? 163 ASN B N   1 
ATOM   746  C CA  . ASN A 1 107 ? 45.464 60.482  -43.538 1.00 37.51  ? 163 ASN B CA  1 
ATOM   747  C C   . ASN A 1 107 ? 45.747 60.915  -42.108 1.00 41.90  ? 163 ASN B C   1 
ATOM   748  O O   . ASN A 1 107 ? 45.837 60.068  -41.226 1.00 47.66  ? 163 ASN B O   1 
ATOM   749  C CB  . ASN A 1 107 ? 46.724 59.887  -44.162 1.00 40.27  ? 163 ASN B CB  1 
ATOM   750  C CG  . ASN A 1 107 ? 46.520 58.463  -44.646 1.00 49.59  ? 163 ASN B CG  1 
ATOM   751  O OD1 . ASN A 1 107 ? 46.881 57.501  -43.957 1.00 55.11  ? 163 ASN B OD1 1 
ATOM   752  N ND2 . ASN A 1 107 ? 45.948 58.317  -45.841 1.00 46.74  ? 163 ASN B ND2 1 
ATOM   753  N N   . LEU A 1 108 ? 45.837 62.217  -41.842 1.00 38.50  ? 164 LEU B N   1 
ATOM   754  C CA  . LEU A 1 108 ? 46.254 62.596  -40.505 1.00 33.48  ? 164 LEU B CA  1 
ATOM   755  C C   . LEU A 1 108 ? 44.985 62.612  -39.708 1.00 37.33  ? 164 LEU B C   1 
ATOM   756  O O   . LEU A 1 108 ? 44.318 63.632  -39.592 1.00 36.78  ? 164 LEU B O   1 
ATOM   757  C CB  . LEU A 1 108 ? 46.803 64.016  -40.510 1.00 20.69  ? 164 LEU B CB  1 
ATOM   758  C CG  . LEU A 1 108 ? 48.045 64.309  -41.349 1.00 21.50  ? 164 LEU B CG  1 
ATOM   759  C CD1 . LEU A 1 108 ? 48.427 65.769  -41.211 1.00 21.23  ? 164 LEU B CD1 1 
ATOM   760  C CD2 . LEU A 1 108 ? 49.184 63.424  -40.928 1.00 22.68  ? 164 LEU B CD2 1 
ATOM   761  N N   . SER A 1 109 ? 44.769 61.513  -39.006 1.00 40.01  ? 165 SER B N   1 
ATOM   762  C CA  . SER A 1 109 ? 43.453 61.154  -38.529 1.00 34.63  ? 165 SER B CA  1 
ATOM   763  C C   . SER A 1 109 ? 43.045 62.069  -37.388 1.00 35.99  ? 165 SER B C   1 
ATOM   764  O O   . SER A 1 109 ? 41.864 62.343  -37.199 1.00 37.59  ? 165 SER B O   1 
ATOM   765  C CB  . SER A 1 109 ? 43.464 59.688  -38.080 1.00 36.12  ? 165 SER B CB  1 
ATOM   766  O OG  . SER A 1 109 ? 42.159 59.149  -38.001 1.00 35.13  ? 165 SER B OG  1 
ATOM   767  N N   . GLY A 1 110 ? 44.031 62.536  -36.629 1.00 40.04  ? 166 GLY B N   1 
ATOM   768  C CA  . GLY A 1 110 ? 43.775 63.342  -35.452 1.00 18.74  ? 166 GLY B CA  1 
ATOM   769  C C   . GLY A 1 110 ? 44.151 64.806  -35.543 1.00 18.47  ? 166 GLY B C   1 
ATOM   770  O O   . GLY A 1 110 ? 44.267 65.477  -34.523 1.00 31.52  ? 166 GLY B O   1 
ATOM   771  N N   . LEU A 1 111 ? 44.377 65.300  -36.753 1.00 18.45  ? 167 LEU B N   1 
ATOM   772  C CA  . LEU A 1 111 ? 44.598 66.728  -36.958 1.00 19.29  ? 167 LEU B CA  1 
ATOM   773  C C   . LEU A 1 111 ? 43.470 67.594  -36.377 1.00 25.06  ? 167 LEU B C   1 
ATOM   774  O O   . LEU A 1 111 ? 42.283 67.341  -36.606 1.00 25.27  ? 167 LEU B O   1 
ATOM   775  C CB  . LEU A 1 111 ? 44.740 67.045  -38.442 1.00 18.09  ? 167 LEU B CB  1 
ATOM   776  C CG  . LEU A 1 111 ? 45.498 68.340  -38.722 1.00 24.17  ? 167 LEU B CG  1 
ATOM   777  C CD1 . LEU A 1 111 ? 46.850 68.263  -38.022 1.00 19.16  ? 167 LEU B CD1 1 
ATOM   778  C CD2 . LEU A 1 111 ? 45.658 68.554  -40.217 1.00 18.23  ? 167 LEU B CD2 1 
ATOM   779  N N   . VAL A 1 112 ? 43.869 68.615  -35.624 1.00 17.89  ? 168 VAL B N   1 
ATOM   780  C CA  . VAL A 1 112 ? 42.954 69.585  -35.050 1.00 17.48  ? 168 VAL B CA  1 
ATOM   781  C C   . VAL A 1 112 ? 43.179 70.958  -35.686 1.00 22.22  ? 168 VAL B C   1 
ATOM   782  O O   . VAL A 1 112 ? 42.240 71.581  -36.189 1.00 22.48  ? 168 VAL B O   1 
ATOM   783  C CB  . VAL A 1 112 ? 42.999 69.614  -33.502 1.00 21.49  ? 168 VAL B CB  1 
ATOM   784  C CG1 . VAL A 1 112 ? 42.066 70.711  -32.957 1.00 15.08  ? 168 VAL B CG1 1 
ATOM   785  C CG2 . VAL A 1 112 ? 42.605 68.246  -32.947 1.00 16.24  ? 168 VAL B CG2 1 
ATOM   786  N N   . GLU A 1 113 ? 44.411 71.450  -35.602 1.00 22.50  ? 169 GLU B N   1 
ATOM   787  C CA  . GLU A 1 113 ? 44.766 72.732  -36.208 1.00 22.08  ? 169 GLU B CA  1 
ATOM   788  C C   . GLU A 1 113 ? 45.494 72.574  -37.538 1.00 27.46  ? 169 GLU B C   1 
ATOM   789  O O   . GLU A 1 113 ? 46.486 71.854  -37.632 1.00 30.06  ? 169 GLU B O   1 
ATOM   790  C CB  . GLU A 1 113 ? 45.638 73.530  -35.243 1.00 16.64  ? 169 GLU B CB  1 
ATOM   791  C CG  . GLU A 1 113 ? 45.128 73.503  -33.800 1.00 29.66  ? 169 GLU B CG  1 
ATOM   792  C CD  . GLU A 1 113 ? 43.789 74.190  -33.640 1.00 28.44  ? 169 GLU B CD  1 
ATOM   793  O OE1 . GLU A 1 113 ? 43.399 74.958  -34.550 1.00 36.82  ? 169 GLU B OE1 1 
ATOM   794  O OE2 . GLU A 1 113 ? 43.121 73.966  -32.610 1.00 21.93  ? 169 GLU B OE2 1 
ATOM   795  N N   . LEU A 1 114 ? 44.994 73.240  -38.572 1.00 16.23  ? 170 LEU B N   1 
ATOM   796  C CA  . LEU A 1 114 ? 45.673 73.238  -39.861 1.00 16.71  ? 170 LEU B CA  1 
ATOM   797  C C   . LEU A 1 114 ? 45.823 74.653  -40.396 1.00 16.38  ? 170 LEU B C   1 
ATOM   798  O O   . LEU A 1 114 ? 44.842 75.247  -40.859 1.00 16.76  ? 170 LEU B O   1 
ATOM   799  C CB  . LEU A 1 114 ? 44.871 72.398  -40.857 1.00 16.43  ? 170 LEU B CB  1 
ATOM   800  C CG  . LEU A 1 114 ? 45.339 72.352  -42.311 1.00 21.04  ? 170 LEU B CG  1 
ATOM   801  C CD1 . LEU A 1 114 ? 46.725 71.722  -42.432 1.00 17.96  ? 170 LEU B CD1 1 
ATOM   802  C CD2 . LEU A 1 114 ? 44.318 71.602  -43.158 1.00 16.79  ? 170 LEU B CD2 1 
ATOM   803  N N   . MET A 1 115 ? 47.056 75.165  -40.397 1.00 17.11  ? 171 MET B N   1 
ATOM   804  C CA  . MET A 1 115 ? 47.315 76.527  -40.854 1.00 20.18  ? 171 MET B CA  1 
ATOM   805  C C   . MET A 1 115 ? 48.173 76.559  -42.112 1.00 17.51  ? 171 MET B C   1 
ATOM   806  O O   . MET A 1 115 ? 49.386 76.368  -42.053 1.00 21.29  ? 171 MET B O   1 
ATOM   807  C CB  . MET A 1 115 ? 48.053 77.284  -39.748 1.00 23.77  ? 171 MET B CB  1 
ATOM   808  C CG  . MET A 1 115 ? 47.380 77.202  -38.385 1.00 17.63  ? 171 MET B CG  1 
ATOM   809  S SD  . MET A 1 115 ? 45.833 78.104  -38.386 1.00 32.01  ? 171 MET B SD  1 
ATOM   810  C CE  . MET A 1 115 ? 45.495 78.215  -36.606 1.00 15.20  ? 171 MET B CE  1 
ATOM   811  N N   . LEU A 1 116 ? 47.541 76.804  -43.252 1.00 18.24  ? 172 LEU B N   1 
ATOM   812  C CA  . LEU A 1 116 ? 48.272 76.963  -44.509 1.00 17.48  ? 172 LEU B CA  1 
ATOM   813  C C   . LEU A 1 116 ? 48.362 78.385  -45.029 1.00 17.15  ? 172 LEU B C   1 
ATOM   814  O O   . LEU A 1 116 ? 48.917 78.607  -46.089 1.00 17.51  ? 172 LEU B O   1 
ATOM   815  C CB  . LEU A 1 116 ? 47.726 76.027  -45.581 1.00 17.39  ? 172 LEU B CB  1 
ATOM   816  C CG  . LEU A 1 116 ? 47.773 74.578  -45.100 1.00 19.00  ? 172 LEU B CG  1 
ATOM   817  C CD1 . LEU A 1 116 ? 47.213 73.619  -46.143 1.00 17.79  ? 172 LEU B CD1 1 
ATOM   818  C CD2 . LEU A 1 116 ? 49.189 74.189  -44.666 1.00 19.00  ? 172 LEU B CD2 1 
ATOM   819  N N   . PHE A 1 117 ? 47.800 79.342  -44.295 1.00 35.07  ? 173 PHE B N   1 
ATOM   820  C CA  . PHE A 1 117 ? 47.564 80.664  -44.864 1.00 15.95  ? 173 PHE B CA  1 
ATOM   821  C C   . PHE A 1 117 ? 48.819 81.464  -45.243 1.00 16.65  ? 173 PHE B C   1 
ATOM   822  O O   . PHE A 1 117 ? 49.907 81.221  -44.733 1.00 17.52  ? 173 PHE B O   1 
ATOM   823  C CB  . PHE A 1 117 ? 46.586 81.485  -44.012 1.00 15.04  ? 173 PHE B CB  1 
ATOM   824  C CG  . PHE A 1 117 ? 47.035 81.717  -42.597 1.00 24.95  ? 173 PHE B CG  1 
ATOM   825  C CD1 . PHE A 1 117 ? 47.863 82.778  -42.284 1.00 23.43  ? 173 PHE B CD1 1 
ATOM   826  C CD2 . PHE A 1 117 ? 46.588 80.902  -41.570 1.00 20.37  ? 173 PHE B CD2 1 
ATOM   827  C CE1 . PHE A 1 117 ? 48.258 83.006  -40.975 1.00 20.92  ? 173 PHE B CE1 1 
ATOM   828  C CE2 . PHE A 1 117 ? 46.979 81.122  -40.263 1.00 21.57  ? 173 PHE B CE2 1 
ATOM   829  C CZ  . PHE A 1 117 ? 47.815 82.175  -39.964 1.00 22.59  ? 173 PHE B CZ  1 
ATOM   830  N N   . ASP A 1 118 ? 48.648 82.399  -46.173 1.00 23.54  ? 174 ASP B N   1 
ATOM   831  C CA  . ASP A 1 118 ? 49.742 83.236  -46.672 1.00 16.89  ? 174 ASP B CA  1 
ATOM   832  C C   . ASP A 1 118 ? 50.910 82.420  -47.237 1.00 29.03  ? 174 ASP B C   1 
ATOM   833  O O   . ASP A 1 118 ? 52.022 82.395  -46.697 1.00 18.83  ? 174 ASP B O   1 
ATOM   834  C CB  . ASP A 1 118 ? 50.212 84.247  -45.616 1.00 20.04  ? 174 ASP B CB  1 
ATOM   835  C CG  . ASP A 1 118 ? 49.113 85.244  -45.210 1.00 20.67  ? 174 ASP B CG  1 
ATOM   836  O OD1 . ASP A 1 118 ? 48.386 85.756  -46.087 1.00 27.56  ? 174 ASP B OD1 1 
ATOM   837  O OD2 . ASP A 1 118 ? 48.971 85.520  -44.003 1.00 25.15  ? 174 ASP B OD2 1 
ATOM   838  N N   . ASN A 1 119 ? 50.638 81.761  -48.352 1.00 26.85  ? 175 ASN B N   1 
ATOM   839  C CA  . ASN A 1 119 ? 51.647 81.011  -49.064 1.00 18.93  ? 175 ASN B CA  1 
ATOM   840  C C   . ASN A 1 119 ? 51.470 81.234  -50.565 1.00 20.82  ? 175 ASN B C   1 
ATOM   841  O O   . ASN A 1 119 ? 50.819 82.185  -50.996 1.00 18.05  ? 175 ASN B O   1 
ATOM   842  C CB  . ASN A 1 119 ? 51.577 79.525  -48.708 1.00 26.82  ? 175 ASN B CB  1 
ATOM   843  C CG  . ASN A 1 119 ? 52.355 79.187  -47.453 1.00 30.64  ? 175 ASN B CG  1 
ATOM   844  O OD1 . ASN A 1 119 ? 53.532 79.474  -47.365 1.00 36.89  ? 175 ASN B OD1 1 
ATOM   845  N ND2 . ASN A 1 119 ? 51.696 78.578  -46.474 1.00 34.08  ? 175 ASN B ND2 1 
ATOM   846  N N   . LYS A 1 120 ? 52.160 80.424  -51.349 1.00 25.02  ? 176 LYS B N   1 
ATOM   847  C CA  . LYS A 1 120 ? 52.008 80.378  -52.801 1.00 20.27  ? 176 LYS B CA  1 
ATOM   848  C C   . LYS A 1 120 ? 51.166 79.212  -53.335 1.00 20.62  ? 176 LYS B C   1 
ATOM   849  O O   . LYS A 1 120 ? 51.302 78.831  -54.498 1.00 22.07  ? 176 LYS B O   1 
ATOM   850  C CB  . LYS A 1 120 ? 53.345 80.570  -53.518 1.00 20.51  ? 176 LYS B CB  1 
ATOM   851  C CG  . LYS A 1 120 ? 53.931 81.958  -53.256 1.00 31.52  ? 176 LYS B CG  1 
ATOM   852  C CD  . LYS A 1 120 ? 55.162 82.248  -54.114 1.00 43.25  ? 176 LYS B CD  1 
ATOM   853  C CE  . LYS A 1 120 ? 55.601 83.707  -53.970 1.00 47.35  ? 176 LYS B CE  1 
ATOM   854  N NZ  . LYS A 1 120 ? 56.805 84.017  -54.794 1.00 47.72  ? 176 LYS B NZ  1 
ATOM   855  N N   . LEU A 1 121 ? 50.382 78.574  -52.468 1.00 22.30  ? 177 LEU B N   1 
ATOM   856  C CA  . LEU A 1 121 ? 49.682 77.338  -52.843 1.00 18.70  ? 177 LEU B CA  1 
ATOM   857  C C   . LEU A 1 121 ? 48.723 77.460  -54.050 1.00 25.32  ? 177 LEU B C   1 
ATOM   858  O O   . LEU A 1 121 ? 48.268 78.553  -54.397 1.00 31.11  ? 177 LEU B O   1 
ATOM   859  C CB  . LEU A 1 121 ? 48.913 76.789  -51.638 1.00 18.25  ? 177 LEU B CB  1 
ATOM   860  C CG  . LEU A 1 121 ? 49.735 76.222  -50.490 1.00 18.96  ? 177 LEU B CG  1 
ATOM   861  C CD1 . LEU A 1 121 ? 48.822 75.827  -49.333 1.00 18.37  ? 177 LEU B CD1 1 
ATOM   862  C CD2 . LEU A 1 121 ? 50.552 75.034  -50.989 1.00 19.96  ? 177 LEU B CD2 1 
ATOM   863  N N   . SER A 1 122 ? 48.448 76.322  -54.689 1.00 18.27  ? 178 SER B N   1 
ATOM   864  C CA  . SER A 1 122 ? 47.573 76.244  -55.862 1.00 27.57  ? 178 SER B CA  1 
ATOM   865  C C   . SER A 1 122 ? 46.757 74.947  -55.896 1.00 30.12  ? 178 SER B C   1 
ATOM   866  O O   . SER A 1 122 ? 46.676 74.224  -54.897 1.00 34.69  ? 178 SER B O   1 
ATOM   867  C CB  . SER A 1 122 ? 48.367 76.413  -57.167 1.00 18.39  ? 178 SER B CB  1 
ATOM   868  O OG  . SER A 1 122 ? 49.489 75.553  -57.213 1.00 37.68  ? 178 SER B OG  1 
ATOM   869  N N   . GLY A 1 123 ? 46.133 74.677  -57.041 1.00 17.45  ? 179 GLY B N   1 
ATOM   870  C CA  . GLY A 1 123 ? 45.271 73.517  -57.200 1.00 23.88  ? 179 GLY B CA  1 
ATOM   871  C C   . GLY A 1 123 ? 43.958 73.607  -56.433 1.00 27.52  ? 179 GLY B C   1 
ATOM   872  O O   . GLY A 1 123 ? 43.514 74.687  -56.051 1.00 30.95  ? 179 GLY B O   1 
ATOM   873  N N   . GLU A 1 124 ? 43.324 72.465  -56.201 1.00 24.80  ? 180 GLU B N   1 
ATOM   874  C CA  . GLU A 1 124 ? 42.076 72.464  -55.465 1.00 16.54  ? 180 GLU B CA  1 
ATOM   875  C C   . GLU A 1 124 ? 42.265 72.003  -54.026 1.00 19.96  ? 180 GLU B C   1 
ATOM   876  O O   . GLU A 1 124 ? 43.334 71.533  -53.626 1.00 28.88  ? 180 GLU B O   1 
ATOM   877  C CB  . GLU A 1 124 ? 41.057 71.542  -56.141 1.00 21.08  ? 180 GLU B CB  1 
ATOM   878  C CG  . GLU A 1 124 ? 40.586 71.973  -57.515 1.00 32.81  ? 180 GLU B CG  1 
ATOM   879  C CD  . GLU A 1 124 ? 39.420 71.127  -58.009 1.00 46.85  ? 180 GLU B CD  1 
ATOM   880  O OE1 . GLU A 1 124 ? 39.664 70.104  -58.691 1.00 50.06  ? 180 GLU B OE1 1 
ATOM   881  O OE2 . GLU A 1 124 ? 38.255 71.480  -57.707 1.00 52.97  ? 180 GLU B OE2 1 
ATOM   882  N N   . ILE A 1 125 ? 41.200 72.111  -53.255 1.00 20.21  ? 181 ILE B N   1 
ATOM   883  C CA  . ILE A 1 125 ? 41.194 71.561  -51.926 1.00 22.88  ? 181 ILE B CA  1 
ATOM   884  C C   . ILE A 1 125 ? 40.743 70.121  -52.079 1.00 29.71  ? 181 ILE B C   1 
ATOM   885  O O   . ILE A 1 125 ? 39.712 69.842  -52.695 1.00 33.75  ? 181 ILE B O   1 
ATOM   886  C CB  . ILE A 1 125 ? 40.249 72.336  -51.028 1.00 21.19  ? 181 ILE B CB  1 
ATOM   887  C CG1 . ILE A 1 125 ? 40.834 73.717  -50.758 1.00 18.47  ? 181 ILE B CG1 1 
ATOM   888  C CG2 . ILE A 1 125 ? 40.032 71.606  -49.736 1.00 19.12  ? 181 ILE B CG2 1 
ATOM   889  C CD1 . ILE A 1 125 ? 39.931 74.607  -49.993 1.00 15.49  ? 181 ILE B CD1 1 
ATOM   890  N N   . PRO A 1 126 ? 41.540 69.196  -51.548 1.00 25.53  ? 182 PRO B N   1 
ATOM   891  C CA  . PRO A 1 126 ? 41.305 67.760  -51.703 1.00 20.80  ? 182 PRO B CA  1 
ATOM   892  C C   . PRO A 1 126 ? 39.949 67.367  -51.140 1.00 21.83  ? 182 PRO B C   1 
ATOM   893  O O   . PRO A 1 126 ? 39.575 67.910  -50.114 1.00 27.82  ? 182 PRO B O   1 
ATOM   894  C CB  . PRO A 1 126 ? 42.413 67.144  -50.849 1.00 27.49  ? 182 PRO B CB  1 
ATOM   895  C CG  . PRO A 1 126 ? 43.463 68.202  -50.769 1.00 26.73  ? 182 PRO B CG  1 
ATOM   896  C CD  . PRO A 1 126 ? 42.728 69.485  -50.731 1.00 18.50  ? 182 PRO B CD  1 
ATOM   897  N N   . ARG A 1 127 ? 39.235 66.450  -51.791 1.00 20.20  ? 183 ARG B N   1 
ATOM   898  C CA  . ARG A 1 127 ? 38.003 65.880  -51.244 1.00 23.84  ? 183 ARG B CA  1 
ATOM   899  C C   . ARG A 1 127 ? 38.312 65.127  -49.938 1.00 27.61  ? 183 ARG B C   1 
ATOM   900  O O   . ARG A 1 127 ? 37.417 64.807  -49.153 1.00 34.04  ? 183 ARG B O   1 
ATOM   901  C CB  . ARG A 1 127 ? 37.336 64.926  -52.255 1.00 36.16  ? 183 ARG B CB  1 
ATOM   902  C CG  . ARG A 1 127 ? 36.932 65.525  -53.622 1.00 47.40  ? 183 ARG B CG  1 
ATOM   903  C CD  . ARG A 1 127 ? 35.878 66.632  -53.446 1.00 68.90  ? 183 ARG B CD  1 
ATOM   904  N NE  . ARG A 1 127 ? 34.915 66.741  -54.541 1.00 83.74  ? 183 ARG B NE  1 
ATOM   905  C CZ  . ARG A 1 127 ? 33.732 67.342  -54.426 1.00 87.39  ? 183 ARG B CZ  1 
ATOM   906  N NH1 . ARG A 1 127 ? 33.370 67.865  -53.270 1.00 88.29  ? 183 ARG B NH1 1 
ATOM   907  N NH2 . ARG A 1 127 ? 32.904 67.411  -55.457 1.00 91.90  ? 183 ARG B NH2 1 
ATOM   908  N N   . SER A 1 128 ? 39.591 64.852  -49.715 1.00 24.21  ? 184 SER B N   1 
ATOM   909  C CA  . SER A 1 128 ? 40.060 64.154  -48.526 1.00 20.32  ? 184 SER B CA  1 
ATOM   910  C C   . SER A 1 128 ? 39.810 64.863  -47.193 1.00 24.60  ? 184 SER B C   1 
ATOM   911  O O   . SER A 1 128 ? 39.808 64.196  -46.156 1.00 21.00  ? 184 SER B O   1 
ATOM   912  C CB  . SER A 1 128 ? 41.557 63.891  -48.637 1.00 20.32  ? 184 SER B CB  1 
ATOM   913  O OG  . SER A 1 128 ? 41.797 62.624  -49.195 1.00 35.71  ? 184 SER B OG  1 
ATOM   914  N N   . ILE A 1 129 ? 39.638 66.191  -47.198 1.00 18.85  ? 185 ILE B N   1 
ATOM   915  C CA  . ILE A 1 129 ? 39.513 66.913  -45.929 1.00 20.84  ? 185 ILE B CA  1 
ATOM   916  C C   . ILE A 1 129 ? 38.349 66.377  -45.125 1.00 21.05  ? 185 ILE B C   1 
ATOM   917  O O   . ILE A 1 129 ? 38.366 66.452  -43.902 1.00 20.44  ? 185 ILE B O   1 
ATOM   918  C CB  . ILE A 1 129 ? 39.358 68.457  -46.062 1.00 28.87  ? 185 ILE B CB  1 
ATOM   919  C CG1 . ILE A 1 129 ? 38.745 68.840  -47.403 1.00 30.49  ? 185 ILE B CG1 1 
ATOM   920  C CG2 . ILE A 1 129 ? 40.692 69.174  -45.850 1.00 21.70  ? 185 ILE B CG2 1 
ATOM   921  C CD1 . ILE A 1 129 ? 37.292 68.538  -47.527 1.00 30.62  ? 185 ILE B CD1 1 
ATOM   922  N N   . GLY A 1 130 ? 37.364 65.802  -45.814 1.00 14.33  ? 186 GLY B N   1 
ATOM   923  C CA  . GLY A 1 130 ? 36.207 65.221  -45.156 1.00 13.88  ? 186 GLY B CA  1 
ATOM   924  C C   . GLY A 1 130 ? 36.556 64.127  -44.160 1.00 20.96  ? 186 GLY B C   1 
ATOM   925  O O   . GLY A 1 130 ? 35.793 63.839  -43.251 1.00 26.96  ? 186 GLY B O   1 
ATOM   926  N N   . GLU A 1 131 ? 37.719 63.516  -44.319 1.00 15.27  ? 187 GLU B N   1 
ATOM   927  C CA  . GLU A 1 131 ? 38.109 62.429  -43.443 1.00 23.87  ? 187 GLU B CA  1 
ATOM   928  C C   . GLU A 1 131 ? 38.578 62.935  -42.100 1.00 29.29  ? 187 GLU B C   1 
ATOM   929  O O   . GLU A 1 131 ? 38.574 62.186  -41.127 1.00 43.58  ? 187 GLU B O   1 
ATOM   930  C CB  . GLU A 1 131 ? 39.193 61.571  -44.084 1.00 26.99  ? 187 GLU B CB  1 
ATOM   931  C CG  . GLU A 1 131 ? 38.679 60.689  -45.212 1.00 44.30  ? 187 GLU B CG  1 
ATOM   932  C CD  . GLU A 1 131 ? 39.804 60.074  -46.021 1.00 64.35  ? 187 GLU B CD  1 
ATOM   933  O OE1 . GLU A 1 131 ? 40.982 60.361  -45.706 1.00 68.67  ? 187 GLU B OE1 1 
ATOM   934  O OE2 . GLU A 1 131 ? 39.515 59.309  -46.972 1.00 70.86  ? 187 GLU B OE2 1 
ATOM   935  N N   . LEU A 1 132 ? 38.934 64.213  -42.012 1.00 21.27  ? 188 LEU B N   1 
ATOM   936  C CA  . LEU A 1 132 ? 39.527 64.678  -40.776 1.00 20.01  ? 188 LEU B CA  1 
ATOM   937  C C   . LEU A 1 132 ? 38.400 65.113  -39.874 1.00 15.51  ? 188 LEU B C   1 
ATOM   938  O O   . LEU A 1 132 ? 37.889 66.217  -39.995 1.00 25.59  ? 188 LEU B O   1 
ATOM   939  C CB  . LEU A 1 132 ? 40.408 65.888  -41.075 1.00 26.46  ? 188 LEU B CB  1 
ATOM   940  C CG  . LEU A 1 132 ? 41.402 65.713  -42.219 1.00 29.94  ? 188 LEU B CG  1 
ATOM   941  C CD1 . LEU A 1 132 ? 41.974 67.046  -42.667 1.00 16.39  ? 188 LEU B CD1 1 
ATOM   942  C CD2 . LEU A 1 132 ? 42.504 64.769  -41.782 1.00 17.52  ? 188 LEU B CD2 1 
ATOM   943  N N   . LYS A 1 133 ? 38.074 64.270  -38.906 1.00 17.52  ? 189 LYS B N   1 
ATOM   944  C CA  . LYS A 1 133 ? 36.865 64.481  -38.118 1.00 16.49  ? 189 LYS B CA  1 
ATOM   945  C C   . LYS A 1 133 ? 37.109 65.150  -36.788 1.00 15.18  ? 189 LYS B C   1 
ATOM   946  O O   . LYS A 1 133 ? 36.168 65.466  -36.068 1.00 26.13  ? 189 LYS B O   1 
ATOM   947  C CB  . LYS A 1 133 ? 36.091 63.175  -37.939 1.00 25.90  ? 189 LYS B CB  1 
ATOM   948  C CG  . LYS A 1 133 ? 35.453 62.667  -39.237 1.00 29.25  ? 189 LYS B CG  1 
ATOM   949  C CD  . LYS A 1 133 ? 34.211 61.831  -38.957 1.00 33.16  ? 189 LYS B CD  1 
ATOM   950  C CE  . LYS A 1 133 ? 33.297 61.826  -40.165 1.00 36.58  ? 189 LYS B CE  1 
ATOM   951  N NZ  . LYS A 1 133 ? 34.110 61.775  -41.417 1.00 37.95  ? 189 LYS B NZ  1 
ATOM   952  N N   . ASN A 1 134 ? 38.374 65.365  -36.455 1.00 20.05  ? 190 ASN B N   1 
ATOM   953  C CA  . ASN A 1 134 ? 38.729 66.181  -35.303 1.00 14.48  ? 190 ASN B CA  1 
ATOM   954  C C   . ASN A 1 134 ? 39.124 67.590  -35.694 1.00 14.23  ? 190 ASN B C   1 
ATOM   955  O O   . ASN A 1 134 ? 39.460 68.404  -34.835 1.00 46.70  ? 190 ASN B O   1 
ATOM   956  C CB  . ASN A 1 134 ? 39.860 65.526  -34.510 1.00 15.38  ? 190 ASN B CB  1 
ATOM   957  C CG  . ASN A 1 134 ? 39.512 64.133  -34.066 1.00 27.53  ? 190 ASN B CG  1 
ATOM   958  O OD1 . ASN A 1 134 ? 40.107 63.161  -34.526 1.00 33.39  ? 190 ASN B OD1 1 
ATOM   959  N ND2 . ASN A 1 134 ? 38.532 64.021  -33.181 1.00 15.10  ? 190 ASN B ND2 1 
ATOM   960  N N   . LEU A 1 135 ? 39.114 67.868  -36.993 1.00 14.15  ? 191 LEU B N   1 
ATOM   961  C CA  . LEU A 1 135 ? 39.540 69.169  -37.476 1.00 13.98  ? 191 LEU B CA  1 
ATOM   962  C C   . LEU A 1 135 ? 38.650 70.267  -36.886 1.00 13.07  ? 191 LEU B C   1 
ATOM   963  O O   . LEU A 1 135 ? 37.417 70.214  -36.935 1.00 12.38  ? 191 LEU B O   1 
ATOM   964  C CB  . LEU A 1 135 ? 39.561 69.209  -39.003 1.00 14.02  ? 191 LEU B CB  1 
ATOM   965  C CG  . LEU A 1 135 ? 40.195 70.436  -39.665 1.00 14.01  ? 191 LEU B CG  1 
ATOM   966  C CD1 . LEU A 1 135 ? 41.649 70.569  -39.246 1.00 14.86  ? 191 LEU B CD1 1 
ATOM   967  C CD2 . LEU A 1 135 ? 40.060 70.391  -41.206 1.00 14.00  ? 191 LEU B CD2 1 
ATOM   968  N N   . GLN A 1 136 ? 39.308 71.245  -36.289 1.00 13.14  ? 192 GLN B N   1 
ATOM   969  C CA  . GLN A 1 136 ? 38.647 72.359  -35.644 1.00 12.39  ? 192 GLN B CA  1 
ATOM   970  C C   . GLN A 1 136 ? 38.789 73.616  -36.483 1.00 16.24  ? 192 GLN B C   1 
ATOM   971  O O   . GLN A 1 136 ? 37.798 74.312  -36.725 1.00 15.35  ? 192 GLN B O   1 
ATOM   972  C CB  . GLN A 1 136 ? 39.147 72.555  -34.219 1.00 12.63  ? 192 GLN B CB  1 
ATOM   973  C CG  . GLN A 1 136 ? 38.389 71.687  -33.233 1.00 12.44  ? 192 GLN B CG  1 
ATOM   974  C CD  . GLN A 1 136 ? 38.894 71.776  -31.800 1.00 12.73  ? 192 GLN B CD  1 
ATOM   975  O OE1 . GLN A 1 136 ? 39.283 72.843  -31.319 1.00 26.47  ? 192 GLN B OE1 1 
ATOM   976  N NE2 . GLN A 1 136 ? 38.858 70.647  -31.099 1.00 13.07  ? 192 GLN B NE2 1 
ATOM   977  N N   . VAL A 1 137 ? 40.042 73.941  -36.812 1.00 12.77  ? 193 VAL B N   1 
ATOM   978  C CA  . VAL A 1 137 ? 40.422 75.134  -37.559 1.00 26.42  ? 193 VAL B CA  1 
ATOM   979  C C   . VAL A 1 137 ? 41.145 74.786  -38.868 1.00 27.52  ? 193 VAL B C   1 
ATOM   980  O O   . VAL A 1 137 ? 42.171 74.088  -38.867 1.00 14.09  ? 193 VAL B O   1 
ATOM   981  C CB  . VAL A 1 137 ? 41.339 76.039  -36.697 1.00 16.30  ? 193 VAL B CB  1 
ATOM   982  C CG1 . VAL A 1 137 ? 42.111 77.038  -37.558 1.00 17.78  ? 193 VAL B CG1 1 
ATOM   983  C CG2 . VAL A 1 137 ? 40.530 76.763  -35.639 1.00 19.24  ? 193 VAL B CG2 1 
ATOM   984  N N   . LEU A 1 138 ? 40.588 75.255  -39.986 1.00 20.81  ? 194 LEU B N   1 
ATOM   985  C CA  . LEU A 1 138 ? 41.256 75.164  -41.278 1.00 13.23  ? 194 LEU B CA  1 
ATOM   986  C C   . LEU A 1 138 ? 41.402 76.585  -41.788 1.00 30.74  ? 194 LEU B C   1 
ATOM   987  O O   . LEU A 1 138 ? 40.402 77.246  -42.061 1.00 12.13  ? 194 LEU B O   1 
ATOM   988  C CB  . LEU A 1 138 ? 40.450 74.283  -42.267 1.00 14.74  ? 194 LEU B CB  1 
ATOM   989  C CG  . LEU A 1 138 ? 40.641 74.444  -43.807 1.00 17.33  ? 194 LEU B CG  1 
ATOM   990  C CD1 . LEU A 1 138 ? 42.094 74.383  -44.218 1.00 19.20  ? 194 LEU B CD1 1 
ATOM   991  C CD2 . LEU A 1 138 ? 39.863 73.420  -44.621 1.00 13.06  ? 194 LEU B CD2 1 
ATOM   992  N N   . ARG A 1 139 ? 42.635 77.083  -41.879 1.00 13.56  ? 195 ARG B N   1 
ATOM   993  C CA  . ARG A 1 139 ? 42.838 78.389  -42.507 1.00 19.45  ? 195 ARG B CA  1 
ATOM   994  C C   . ARG A 1 139 ? 43.895 78.314  -43.608 1.00 24.11  ? 195 ARG B C   1 
ATOM   995  O O   . ARG A 1 139 ? 45.100 78.224  -43.344 1.00 21.08  ? 195 ARG B O   1 
ATOM   996  C CB  . ARG A 1 139 ? 43.220 79.427  -41.454 1.00 13.29  ? 195 ARG B CB  1 
ATOM   997  C CG  . ARG A 1 139 ? 42.200 79.502  -40.299 1.00 24.06  ? 195 ARG B CG  1 
ATOM   998  C CD  . ARG A 1 139 ? 42.574 80.509  -39.220 1.00 14.25  ? 195 ARG B CD  1 
ATOM   999  N NE  . ARG A 1 139 ? 42.866 81.808  -39.800 1.00 21.06  ? 195 ARG B NE  1 
ATOM   1000 C CZ  . ARG A 1 139 ? 43.809 82.626  -39.344 1.00 25.28  ? 195 ARG B CZ  1 
ATOM   1001 N NH1 . ARG A 1 139 ? 44.039 83.786  -39.953 1.00 25.80  ? 195 ARG B NH1 1 
ATOM   1002 N NH2 . ARG A 1 139 ? 44.530 82.271  -38.290 1.00 18.29  ? 195 ARG B NH2 1 
ATOM   1003 N N   . ALA A 1 140 ? 43.391 78.318  -44.842 1.00 13.77  ? 196 ALA B N   1 
ATOM   1004 C CA  . ALA A 1 140 ? 44.172 78.303  -46.079 1.00 16.19  ? 196 ALA B CA  1 
ATOM   1005 C C   . ALA A 1 140 ? 44.152 79.612  -46.853 1.00 17.29  ? 196 ALA B C   1 
ATOM   1006 O O   . ALA A 1 140 ? 44.579 79.660  -48.010 1.00 15.96  ? 196 ALA B O   1 
ATOM   1007 C CB  . ALA A 1 140 ? 43.751 77.148  -46.967 1.00 19.97  ? 196 ALA B CB  1 
ATOM   1008 N N   . GLY A 1 141 ? 43.563 80.647  -46.270 1.00 20.03  ? 197 GLY B N   1 
ATOM   1009 C CA  . GLY A 1 141 ? 43.405 81.901  -46.978 1.00 17.94  ? 197 GLY B CA  1 
ATOM   1010 C C   . GLY A 1 141 ? 44.718 82.521  -47.419 1.00 14.13  ? 197 GLY B C   1 
ATOM   1011 O O   . GLY A 1 141 ? 45.796 82.064  -47.050 1.00 17.66  ? 197 GLY B O   1 
ATOM   1012 N N   . GLY A 1 142 ? 44.630 83.554  -48.244 1.00 18.59  ? 198 GLY B N   1 
ATOM   1013 C CA  . GLY A 1 142 ? 45.817 84.244  -48.701 1.00 21.58  ? 198 GLY B CA  1 
ATOM   1014 C C   . GLY A 1 142 ? 46.690 83.364  -49.575 1.00 23.34  ? 198 GLY B C   1 
ATOM   1015 O O   . GLY A 1 142 ? 47.922 83.476  -49.554 1.00 20.27  ? 198 GLY B O   1 
ATOM   1016 N N   . ASN A 1 143 ? 46.067 82.441  -50.303 1.00 21.65  ? 199 ASN B N   1 
ATOM   1017 C CA  . ASN A 1 143 ? 46.757 81.803  -51.416 1.00 20.66  ? 199 ASN B CA  1 
ATOM   1018 C C   . ASN A 1 143 ? 46.047 82.159  -52.714 1.00 21.79  ? 199 ASN B C   1 
ATOM   1019 O O   . ASN A 1 143 ? 44.993 81.594  -53.023 1.00 22.96  ? 199 ASN B O   1 
ATOM   1020 C CB  . ASN A 1 143 ? 46.815 80.288  -51.228 1.00 15.74  ? 199 ASN B CB  1 
ATOM   1021 C CG  . ASN A 1 143 ? 47.745 79.873  -50.089 1.00 29.63  ? 199 ASN B CG  1 
ATOM   1022 O OD1 . ASN A 1 143 ? 48.949 79.753  -50.284 1.00 21.48  ? 199 ASN B OD1 1 
ATOM   1023 N ND2 . ASN A 1 143 ? 47.187 79.639  -48.905 1.00 16.07  ? 199 ASN B ND2 1 
ATOM   1024 N N   . LYS A 1 144 ? 46.654 83.044  -53.500 1.00 15.00  ? 200 LYS B N   1 
ATOM   1025 C CA  . LYS A 1 144 ? 45.972 83.617  -54.657 1.00 19.62  ? 200 LYS B CA  1 
ATOM   1026 C C   . LYS A 1 144 ? 45.472 82.585  -55.649 1.00 24.74  ? 200 LYS B C   1 
ATOM   1027 O O   . LYS A 1 144 ? 44.429 82.782  -56.280 1.00 29.06  ? 200 LYS B O   1 
ATOM   1028 C CB  . LYS A 1 144 ? 46.839 84.651  -55.385 1.00 18.53  ? 200 LYS B CB  1 
ATOM   1029 C CG  . LYS A 1 144 ? 45.976 85.725  -56.020 1.00 26.79  ? 200 LYS B CG  1 
ATOM   1030 C CD  . LYS A 1 144 ? 46.678 86.504  -57.108 1.00 33.80  ? 200 LYS B CD  1 
ATOM   1031 C CE  . LYS A 1 144 ? 45.653 87.315  -57.901 1.00 38.73  ? 200 LYS B CE  1 
ATOM   1032 N NZ  . LYS A 1 144 ? 44.890 88.255  -57.023 1.00 41.08  ? 200 LYS B NZ  1 
ATOM   1033 N N   . ASN A 1 145 ? 46.222 81.497  -55.799 1.00 23.34  ? 201 ASN B N   1 
ATOM   1034 C CA  . ASN A 1 145 ? 45.885 80.463  -56.784 1.00 19.75  ? 201 ASN B CA  1 
ATOM   1035 C C   . ASN A 1 145 ? 45.161 79.212  -56.304 1.00 23.62  ? 201 ASN B C   1 
ATOM   1036 O O   . ASN A 1 145 ? 44.969 78.270  -57.082 1.00 24.63  ? 201 ASN B O   1 
ATOM   1037 C CB  . ASN A 1 145 ? 47.098 80.112  -57.628 1.00 17.91  ? 201 ASN B CB  1 
ATOM   1038 C CG  . ASN A 1 145 ? 47.490 81.249  -58.519 1.00 23.10  ? 201 ASN B CG  1 
ATOM   1039 O OD1 . ASN A 1 145 ? 46.645 81.822  -59.215 1.00 30.61  ? 201 ASN B OD1 1 
ATOM   1040 N ND2 . ASN A 1 145 ? 48.756 81.630  -58.469 1.00 25.46  ? 201 ASN B ND2 1 
ATOM   1041 N N   . LEU A 1 146 ? 44.793 79.190  -55.024 1.00 25.43  ? 202 LEU B N   1 
ATOM   1042 C CA  . LEU A 1 146 ? 43.987 78.104  -54.485 1.00 22.73  ? 202 LEU B CA  1 
ATOM   1043 C C   . LEU A 1 146 ? 42.641 78.245  -55.171 1.00 22.65  ? 202 LEU B C   1 
ATOM   1044 O O   . LEU A 1 146 ? 42.004 79.283  -55.060 1.00 27.17  ? 202 LEU B O   1 
ATOM   1045 C CB  . LEU A 1 146 ? 43.851 78.279  -52.974 1.00 27.02  ? 202 LEU B CB  1 
ATOM   1046 C CG  . LEU A 1 146 ? 43.460 77.096  -52.088 1.00 30.21  ? 202 LEU B CG  1 
ATOM   1047 C CD1 . LEU A 1 146 ? 41.997 76.725  -52.281 1.00 37.84  ? 202 LEU B CD1 1 
ATOM   1048 C CD2 . LEU A 1 146 ? 44.359 75.909  -52.373 1.00 26.97  ? 202 LEU B CD2 1 
ATOM   1049 N N   . ARG A 1 147 ? 42.212 77.204  -55.881 1.00 26.71  ? 203 ARG B N   1 
ATOM   1050 C CA  . ARG A 1 147 ? 41.071 77.325  -56.787 1.00 26.28  ? 203 ARG B CA  1 
ATOM   1051 C C   . ARG A 1 147 ? 40.090 76.180  -56.665 1.00 26.96  ? 203 ARG B C   1 
ATOM   1052 O O   . ARG A 1 147 ? 40.244 75.306  -55.814 1.00 30.34  ? 203 ARG B O   1 
ATOM   1053 C CB  . ARG A 1 147 ? 41.519 77.452  -58.247 1.00 25.50  ? 203 ARG B CB  1 
ATOM   1054 C CG  . ARG A 1 147 ? 42.203 76.213  -58.833 1.00 34.02  ? 203 ARG B CG  1 
ATOM   1055 C CD  . ARG A 1 147 ? 42.190 76.216  -60.381 1.00 36.91  ? 203 ARG B CD  1 
ATOM   1056 N NE  . ARG A 1 147 ? 40.820 76.228  -60.894 1.00 42.51  ? 203 ARG B NE  1 
ATOM   1057 C CZ  . ARG A 1 147 ? 40.050 75.146  -61.010 1.00 41.47  ? 203 ARG B CZ  1 
ATOM   1058 N NH1 . ARG A 1 147 ? 40.511 73.945  -60.667 1.00 44.61  ? 203 ARG B NH1 1 
ATOM   1059 N NH2 . ARG A 1 147 ? 38.812 75.266  -61.465 1.00 35.61  ? 203 ARG B NH2 1 
ATOM   1060 N N   . GLY A 1 148 ? 39.077 76.194  -57.525 1.00 23.65  ? 204 GLY B N   1 
ATOM   1061 C CA  . GLY A 1 148 ? 38.042 75.186  -57.469 1.00 24.88  ? 204 GLY B CA  1 
ATOM   1062 C C   . GLY A 1 148 ? 36.961 75.483  -56.449 1.00 27.32  ? 204 GLY B C   1 
ATOM   1063 O O   . GLY A 1 148 ? 36.985 76.512  -55.769 1.00 32.44  ? 204 GLY B O   1 
ATOM   1064 N N   . GLU A 1 149 ? 35.986 74.586  -56.372 1.00 21.59  ? 205 GLU B N   1 
ATOM   1065 C CA  . GLU A 1 149 ? 34.877 74.741  -55.457 1.00 17.14  ? 205 GLU B CA  1 
ATOM   1066 C C   . GLU A 1 149 ? 35.296 74.244  -54.088 1.00 22.16  ? 205 GLU B C   1 
ATOM   1067 O O   . GLU A 1 149 ? 36.172 73.392  -53.983 1.00 21.38  ? 205 GLU B O   1 
ATOM   1068 C CB  . GLU A 1 149 ? 33.648 73.977  -55.956 1.00 15.87  ? 205 GLU B CB  1 
ATOM   1069 C CG  . GLU A 1 149 ? 33.206 74.341  -57.366 1.00 21.97  ? 205 GLU B CG  1 
ATOM   1070 C CD  . GLU A 1 149 ? 31.722 74.121  -57.569 1.00 44.60  ? 205 GLU B CD  1 
ATOM   1071 O OE1 . GLU A 1 149 ? 31.256 74.130  -58.732 1.00 48.58  ? 205 GLU B OE1 1 
ATOM   1072 O OE2 . GLU A 1 149 ? 31.013 73.951  -56.551 1.00 58.81  ? 205 GLU B OE2 1 
ATOM   1073 N N   . LEU A 1 150 ? 34.696 74.788  -53.036 1.00 25.51  ? 206 LEU B N   1 
ATOM   1074 C CA  . LEU A 1 150 ? 34.899 74.207  -51.722 1.00 24.92  ? 206 LEU B CA  1 
ATOM   1075 C C   . LEU A 1 150 ? 34.267 72.835  -51.846 1.00 27.87  ? 206 LEU B C   1 
ATOM   1076 O O   . LEU A 1 150 ? 33.136 72.724  -52.312 1.00 27.94  ? 206 LEU B O   1 
ATOM   1077 C CB  . LEU A 1 150 ? 34.218 75.044  -50.638 1.00 22.02  ? 206 LEU B CB  1 
ATOM   1078 C CG  . LEU A 1 150 ? 34.332 74.478  -49.229 1.00 31.09  ? 206 LEU B CG  1 
ATOM   1079 C CD1 . LEU A 1 150 ? 35.795 74.455  -48.771 1.00 33.04  ? 206 LEU B CD1 1 
ATOM   1080 C CD2 . LEU A 1 150 ? 33.439 75.241  -48.235 1.00 30.21  ? 206 LEU B CD2 1 
ATOM   1081 N N   . PRO A 1 151 ? 35.016 71.774  -51.512 1.00 27.68  ? 207 PRO B N   1 
ATOM   1082 C CA  . PRO A 1 151 ? 34.469 70.426  -51.675 1.00 15.32  ? 207 PRO B CA  1 
ATOM   1083 C C   . PRO A 1 151 ? 33.267 70.125  -50.769 1.00 22.62  ? 207 PRO B C   1 
ATOM   1084 O O   . PRO A 1 151 ? 33.229 70.540  -49.609 1.00 25.83  ? 207 PRO B O   1 
ATOM   1085 C CB  . PRO A 1 151 ? 35.658 69.523  -51.326 1.00 17.26  ? 207 PRO B CB  1 
ATOM   1086 C CG  . PRO A 1 151 ? 36.623 70.385  -50.605 1.00 12.73  ? 207 PRO B CG  1 
ATOM   1087 C CD  . PRO A 1 151 ? 36.446 71.747  -51.163 1.00 26.41  ? 207 PRO B CD  1 
ATOM   1088 N N   . TRP A 1 152 ? 32.301 69.404  -51.326 1.00 11.07  ? 208 TRP B N   1 
ATOM   1089 C CA  . TRP A 1 152 ? 31.160 68.843  -50.610 1.00 20.58  ? 208 TRP B CA  1 
ATOM   1090 C C   . TRP A 1 152 ? 31.564 68.120  -49.319 1.00 25.76  ? 208 TRP B C   1 
ATOM   1091 O O   . TRP A 1 152 ? 30.926 68.273  -48.265 1.00 23.27  ? 208 TRP B O   1 
ATOM   1092 C CB  . TRP A 1 152 ? 30.458 67.853  -51.531 1.00 21.67  ? 208 TRP B CB  1 
ATOM   1093 C CG  . TRP A 1 152 ? 29.301 67.160  -50.916 1.00 34.43  ? 208 TRP B CG  1 
ATOM   1094 C CD1 . TRP A 1 152 ? 29.311 65.956  -50.272 1.00 41.33  ? 208 TRP B CD1 1 
ATOM   1095 C CD2 . TRP A 1 152 ? 27.946 67.612  -50.903 1.00 36.95  ? 208 TRP B CD2 1 
ATOM   1096 N NE1 . TRP A 1 152 ? 28.045 65.638  -49.847 1.00 43.04  ? 208 TRP B NE1 1 
ATOM   1097 C CE2 . TRP A 1 152 ? 27.187 66.641  -50.222 1.00 39.80  ? 208 TRP B CE2 1 
ATOM   1098 C CE3 . TRP A 1 152 ? 27.298 68.751  -51.392 1.00 36.50  ? 208 TRP B CE3 1 
ATOM   1099 C CZ2 . TRP A 1 152 ? 25.816 66.774  -50.017 1.00 36.42  ? 208 TRP B CZ2 1 
ATOM   1100 C CZ3 . TRP A 1 152 ? 25.933 68.880  -51.189 1.00 34.76  ? 208 TRP B CZ3 1 
ATOM   1101 C CH2 . TRP A 1 152 ? 25.209 67.901  -50.508 1.00 31.58  ? 208 TRP B CH2 1 
ATOM   1102 N N   . GLU A 1 153 ? 32.645 67.350  -49.398 1.00 23.08  ? 209 GLU B N   1 
ATOM   1103 C CA  . GLU A 1 153 ? 33.138 66.610  -48.239 1.00 18.77  ? 209 GLU B CA  1 
ATOM   1104 C C   . GLU A 1 153 ? 33.480 67.481  -47.024 1.00 22.33  ? 209 GLU B C   1 
ATOM   1105 O O   . GLU A 1 153 ? 33.625 66.962  -45.919 1.00 22.98  ? 209 GLU B O   1 
ATOM   1106 C CB  . GLU A 1 153 ? 34.347 65.760  -48.610 1.00 18.87  ? 209 GLU B CB  1 
ATOM   1107 C CG  . GLU A 1 153 ? 33.991 64.501  -49.385 1.00 22.40  ? 209 GLU B CG  1 
ATOM   1108 C CD  . GLU A 1 153 ? 33.668 64.770  -50.837 1.00 26.61  ? 209 GLU B CD  1 
ATOM   1109 O OE1 . GLU A 1 153 ? 33.850 65.921  -51.293 1.00 23.40  ? 209 GLU B OE1 1 
ATOM   1110 O OE2 . GLU A 1 153 ? 33.233 63.822  -51.516 1.00 30.43  ? 209 GLU B OE2 1 
ATOM   1111 N N   . ILE A 1 154 ? 33.606 68.794  -47.208 1.00 17.40  ? 210 ILE B N   1 
ATOM   1112 C CA  . ILE A 1 154 ? 33.863 69.663  -46.062 1.00 15.12  ? 210 ILE B CA  1 
ATOM   1113 C C   . ILE A 1 154 ? 32.754 69.508  -45.031 1.00 18.88  ? 210 ILE B C   1 
ATOM   1114 O O   . ILE A 1 154 ? 32.960 69.783  -43.859 1.00 26.64  ? 210 ILE B O   1 
ATOM   1115 C CB  . ILE A 1 154 ? 33.993 71.161  -46.441 1.00 28.97  ? 210 ILE B CB  1 
ATOM   1116 C CG1 . ILE A 1 154 ? 34.565 71.959  -45.267 1.00 10.72  ? 210 ILE B CG1 1 
ATOM   1117 C CG2 . ILE A 1 154 ? 32.639 71.758  -46.836 1.00 22.13  ? 210 ILE B CG2 1 
ATOM   1118 C CD1 . ILE A 1 154 ? 36.033 71.775  -45.062 1.00 11.50  ? 210 ILE B CD1 1 
ATOM   1119 N N   . GLY A 1 155 ? 31.578 69.061  -45.462 1.00 17.61  ? 211 GLY B N   1 
ATOM   1120 C CA  . GLY A 1 155 ? 30.480 68.863  -44.531 1.00 16.94  ? 211 GLY B CA  1 
ATOM   1121 C C   . GLY A 1 155 ? 30.773 67.795  -43.485 1.00 22.52  ? 211 GLY B C   1 
ATOM   1122 O O   . GLY A 1 155 ? 30.132 67.744  -42.439 1.00 27.09  ? 211 GLY B O   1 
ATOM   1123 N N   . ASN A 1 156 ? 31.748 66.939  -43.759 1.00 23.13  ? 212 ASN B N   1 
ATOM   1124 C CA  . ASN A 1 156 ? 32.043 65.832  -42.857 1.00 21.36  ? 212 ASN B CA  1 
ATOM   1125 C C   . ASN A 1 156 ? 32.989 66.210  -41.726 1.00 21.33  ? 212 ASN B C   1 
ATOM   1126 O O   . ASN A 1 156 ? 33.198 65.421  -40.801 1.00 27.40  ? 212 ASN B O   1 
ATOM   1127 C CB  . ASN A 1 156 ? 32.567 64.614  -43.618 1.00 22.74  ? 212 ASN B CB  1 
ATOM   1128 C CG  . ASN A 1 156 ? 31.571 64.100  -44.641 1.00 31.80  ? 212 ASN B CG  1 
ATOM   1129 O OD1 . ASN A 1 156 ? 30.403 63.878  -44.325 1.00 36.17  ? 212 ASN B OD1 1 
ATOM   1130 N ND2 . ASN A 1 156 ? 32.022 63.929  -45.880 1.00 33.57  ? 212 ASN B ND2 1 
ATOM   1131 N N   . CYS A 1 157 ? 33.533 67.421  -41.752 1.00 14.57  ? 213 CYS B N   1 
ATOM   1132 C CA  . CYS A 1 157 ? 34.356 67.793  -40.618 1.00 20.15  ? 213 CYS B CA  1 
ATOM   1133 C C   . CYS A 1 157 ? 33.423 68.461  -39.621 1.00 19.80  ? 213 CYS B C   1 
ATOM   1134 O O   . CYS A 1 157 ? 33.260 69.673  -39.634 1.00 18.72  ? 213 CYS B O   1 
ATOM   1135 C CB  . CYS A 1 157 ? 35.413 68.803  -41.077 1.00 15.83  ? 213 CYS B CB  1 
ATOM   1136 S SG  . CYS A 1 157 ? 36.475 68.219  -42.428 1.00 25.76  ? 213 CYS B SG  1 
ATOM   1137 N N   . GLU A 1 158 ? 32.948 67.695  -38.650 1.00 20.64  ? 214 GLU B N   1 
ATOM   1138 C CA  . GLU A 1 158 ? 31.821 68.159  -37.845 1.00 27.87  ? 214 GLU B CA  1 
ATOM   1139 C C   . GLU A 1 158 ? 32.250 68.860  -36.570 1.00 21.12  ? 214 GLU B C   1 
ATOM   1140 O O   . GLU A 1 158 ? 31.426 69.364  -35.825 1.00 29.42  ? 214 GLU B O   1 
ATOM   1141 C CB  . GLU A 1 158 ? 30.843 67.018  -37.555 1.00 45.47  ? 214 GLU B CB  1 
ATOM   1142 C CG  . GLU A 1 158 ? 30.014 66.600  -38.779 1.00 55.57  ? 214 GLU B CG  1 
ATOM   1143 C CD  . GLU A 1 158 ? 29.011 65.491  -38.480 1.00 60.07  ? 214 GLU B CD  1 
ATOM   1144 O OE1 . GLU A 1 158 ? 28.750 65.201  -37.290 1.00 61.31  ? 214 GLU B OE1 1 
ATOM   1145 O OE2 . GLU A 1 158 ? 28.482 64.905  -39.446 1.00 62.37  ? 214 GLU B OE2 1 
ATOM   1146 N N   . ASN A 1 159 ? 33.550 68.900  -36.339 1.00 18.27  ? 215 ASN B N   1 
ATOM   1147 C CA  . ASN A 1 159 ? 34.100 69.688  -35.264 1.00 10.70  ? 215 ASN B CA  1 
ATOM   1148 C C   . ASN A 1 159 ? 34.593 71.065  -35.718 1.00 10.53  ? 215 ASN B C   1 
ATOM   1149 O O   . ASN A 1 159 ? 35.121 71.816  -34.910 1.00 24.80  ? 215 ASN B O   1 
ATOM   1150 C CB  . ASN A 1 159 ? 35.255 68.926  -34.611 1.00 24.43  ? 215 ASN B CB  1 
ATOM   1151 C CG  . ASN A 1 159 ? 34.780 67.788  -33.703 1.00 27.21  ? 215 ASN B CG  1 
ATOM   1152 O OD1 . ASN A 1 159 ? 33.594 67.459  -33.656 1.00 23.75  ? 215 ASN B OD1 1 
ATOM   1153 N ND2 . ASN A 1 159 ? 35.716 67.182  -32.984 1.00 31.97  ? 215 ASN B ND2 1 
ATOM   1154 N N   . LEU A 1 160 ? 34.450 71.389  -37.000 1.00 10.39  ? 216 LEU B N   1 
ATOM   1155 C CA  . LEU A 1 160 ? 35.007 72.639  -37.516 1.00 10.31  ? 216 LEU B CA  1 
ATOM   1156 C C   . LEU A 1 160 ? 34.416 73.825  -36.783 1.00 10.30  ? 216 LEU B C   1 
ATOM   1157 O O   . LEU A 1 160 ? 33.204 73.966  -36.681 1.00 8.96   ? 216 LEU B O   1 
ATOM   1158 C CB  . LEU A 1 160 ? 34.734 72.803  -39.021 1.00 10.17  ? 216 LEU B CB  1 
ATOM   1159 C CG  . LEU A 1 160 ? 35.909 72.629  -39.989 1.00 17.22  ? 216 LEU B CG  1 
ATOM   1160 C CD1 . LEU A 1 160 ? 35.465 72.934  -41.410 1.00 16.77  ? 216 LEU B CD1 1 
ATOM   1161 C CD2 . LEU A 1 160 ? 37.088 73.485  -39.613 1.00 11.24  ? 216 LEU B CD2 1 
ATOM   1162 N N   . VAL A 1 161 ? 35.272 74.638  -36.195 1.00 9.81   ? 217 VAL B N   1 
ATOM   1163 C CA  . VAL A 1 161 ? 34.776 75.867  -35.622 1.00 22.01  ? 217 VAL B CA  1 
ATOM   1164 C C   . VAL A 1 161 ? 35.140 77.113  -36.442 1.00 17.09  ? 217 VAL B C   1 
ATOM   1165 O O   . VAL A 1 161 ? 34.475 78.150  -36.356 1.00 8.40   ? 217 VAL B O   1 
ATOM   1166 C CB  . VAL A 1 161 ? 35.268 75.982  -34.152 1.00 9.38   ? 217 VAL B CB  1 
ATOM   1167 C CG1 . VAL A 1 161 ? 36.704 76.451  -34.104 1.00 10.05  ? 217 VAL B CG1 1 
ATOM   1168 C CG2 . VAL A 1 161 ? 34.406 76.909  -33.394 1.00 28.02  ? 217 VAL B CG2 1 
ATOM   1169 N N   . MET A 1 162 ? 36.169 76.980  -37.275 1.00 14.51  ? 218 MET B N   1 
ATOM   1170 C CA  . MET A 1 162 ? 36.713 78.109  -38.024 1.00 14.40  ? 218 MET B CA  1 
ATOM   1171 C C   . MET A 1 162 ? 37.125 77.638  -39.408 1.00 14.44  ? 218 MET B C   1 
ATOM   1172 O O   . MET A 1 162 ? 37.896 76.677  -39.538 1.00 10.75  ? 218 MET B O   1 
ATOM   1173 C CB  . MET A 1 162 ? 37.928 78.714  -37.291 1.00 14.58  ? 218 MET B CB  1 
ATOM   1174 C CG  . MET A 1 162 ? 38.864 79.586  -38.184 1.00 26.13  ? 218 MET B CG  1 
ATOM   1175 S SD  . MET A 1 162 ? 38.224 81.217  -38.673 1.00 24.51  ? 218 MET B SD  1 
ATOM   1176 C CE  . MET A 1 162 ? 39.298 81.668  -40.010 1.00 22.92  ? 218 MET B CE  1 
ATOM   1177 N N   . LEU A 1 163 ? 36.620 78.311  -40.434 1.00 9.62   ? 219 LEU B N   1 
ATOM   1178 C CA  . LEU A 1 163 ? 37.016 78.027  -41.810 1.00 9.96   ? 219 LEU B CA  1 
ATOM   1179 C C   . LEU A 1 163 ? 37.353 79.338  -42.487 1.00 16.49  ? 219 LEU B C   1 
ATOM   1180 O O   . LEU A 1 163 ? 36.477 80.179  -42.690 1.00 9.12   ? 219 LEU B O   1 
ATOM   1181 C CB  . LEU A 1 163 ? 35.879 77.337  -42.584 1.00 20.62  ? 219 LEU B CB  1 
ATOM   1182 C CG  . LEU A 1 163 ? 35.956 77.196  -44.135 1.00 25.97  ? 219 LEU B CG  1 
ATOM   1183 C CD1 . LEU A 1 163 ? 36.931 76.126  -44.582 1.00 10.60  ? 219 LEU B CD1 1 
ATOM   1184 C CD2 . LEU A 1 163 ? 34.627 76.876  -44.747 1.00 9.21   ? 219 LEU B CD2 1 
ATOM   1185 N N   . GLY A 1 164 ? 38.602 79.519  -42.894 1.00 10.48  ? 220 GLY B N   1 
ATOM   1186 C CA  . GLY A 1 164 ? 38.778 80.605  -43.813 1.00 10.32  ? 220 GLY B CA  1 
ATOM   1187 C C   . GLY A 1 164 ? 39.768 80.376  -44.912 1.00 11.00  ? 220 GLY B C   1 
ATOM   1188 O O   . GLY A 1 164 ? 40.897 79.914  -44.774 1.00 19.73  ? 220 GLY B O   1 
ATOM   1189 N N   . LEU A 1 165 ? 39.194 80.722  -46.056 1.00 14.20  ? 221 LEU B N   1 
ATOM   1190 C CA  . LEU A 1 165 ? 39.698 80.628  -47.414 1.00 11.01  ? 221 LEU B CA  1 
ATOM   1191 C C   . LEU A 1 165 ? 39.885 81.974  -48.098 1.00 11.54  ? 221 LEU B C   1 
ATOM   1192 O O   . LEU A 1 165 ? 39.763 82.041  -49.311 1.00 11.65  ? 221 LEU B O   1 
ATOM   1193 C CB  . LEU A 1 165 ? 38.862 79.640  -48.221 1.00 10.86  ? 221 LEU B CB  1 
ATOM   1194 C CG  . LEU A 1 165 ? 38.907 78.272  -47.513 1.00 14.44  ? 221 LEU B CG  1 
ATOM   1195 C CD1 . LEU A 1 165 ? 37.769 77.343  -47.893 1.00 10.90  ? 221 LEU B CD1 1 
ATOM   1196 C CD2 . LEU A 1 165 ? 40.245 77.598  -47.759 1.00 13.38  ? 221 LEU B CD2 1 
ATOM   1197 N N   . ALA A 1 166 ? 39.941 83.057  -47.333 1.00 10.51  ? 222 ALA B N   1 
ATOM   1198 C CA  . ALA A 1 166 ? 39.878 84.412  -47.898 1.00 13.95  ? 222 ALA B CA  1 
ATOM   1199 C C   . ALA A 1 166 ? 41.031 84.753  -48.844 1.00 10.80  ? 222 ALA B C   1 
ATOM   1200 O O   . ALA A 1 166 ? 42.095 84.146  -48.774 1.00 11.81  ? 222 ALA B O   1 
ATOM   1201 C CB  . ALA A 1 166 ? 39.792 85.443  -46.774 1.00 16.11  ? 222 ALA B CB  1 
ATOM   1202 N N   . GLU A 1 167 ? 40.808 85.716  -49.737 1.00 18.66  ? 223 GLU B N   1 
ATOM   1203 C CA  . GLU A 1 167 ? 41.797 86.071  -50.764 1.00 17.30  ? 223 GLU B CA  1 
ATOM   1204 C C   . GLU A 1 167 ? 42.350 84.847  -51.494 1.00 20.30  ? 223 GLU B C   1 
ATOM   1205 O O   . GLU A 1 167 ? 43.556 84.641  -51.555 1.00 22.84  ? 223 GLU B O   1 
ATOM   1206 C CB  . GLU A 1 167 ? 42.930 86.926  -50.186 1.00 11.49  ? 223 GLU B CB  1 
ATOM   1207 C CG  . GLU A 1 167 ? 42.426 88.261  -49.639 1.00 19.89  ? 223 GLU B CG  1 
ATOM   1208 C CD  . GLU A 1 167 ? 43.517 89.297  -49.440 1.00 21.23  ? 223 GLU B CD  1 
ATOM   1209 O OE1 . GLU A 1 167 ? 44.502 89.292  -50.201 1.00 31.71  ? 223 GLU B OE1 1 
ATOM   1210 O OE2 . GLU A 1 167 ? 43.391 90.122  -48.509 1.00 25.99  ? 223 GLU B OE2 1 
ATOM   1211 N N   . THR A 1 168 ? 41.449 84.017  -52.007 1.00 12.08  ? 224 THR B N   1 
ATOM   1212 C CA  . THR A 1 168 ? 41.837 82.886  -52.818 1.00 12.04  ? 224 THR B CA  1 
ATOM   1213 C C   . THR A 1 168 ? 41.040 82.941  -54.118 1.00 15.89  ? 224 THR B C   1 
ATOM   1214 O O   . THR A 1 168 ? 40.289 83.885  -54.357 1.00 14.65  ? 224 THR B O   1 
ATOM   1215 C CB  . THR A 1 168 ? 41.587 81.538  -52.102 1.00 12.15  ? 224 THR B CB  1 
ATOM   1216 O OG1 . THR A 1 168 ? 40.208 81.434  -51.747 1.00 11.50  ? 224 THR B OG1 1 
ATOM   1217 C CG2 . THR A 1 168 ? 42.410 81.434  -50.854 1.00 12.58  ? 224 THR B CG2 1 
ATOM   1218 N N   . SER A 1 169 ? 41.255 81.960  -54.983 1.00 13.49  ? 225 SER B N   1 
ATOM   1219 C CA  . SER A 1 169 ? 40.491 81.833  -56.221 1.00 15.88  ? 225 SER B CA  1 
ATOM   1220 C C   . SER A 1 169 ? 39.335 80.846  -56.113 1.00 14.11  ? 225 SER B C   1 
ATOM   1221 O O   . SER A 1 169 ? 38.777 80.424  -57.120 1.00 21.21  ? 225 SER B O   1 
ATOM   1222 C CB  . SER A 1 169 ? 41.396 81.551  -57.406 1.00 14.90  ? 225 SER B CB  1 
ATOM   1223 O OG  . SER A 1 169 ? 42.276 82.649  -57.568 1.00 16.40  ? 225 SER B OG  1 
ATOM   1224 N N   . LEU A 1 170 ? 39.043 80.432  -54.887 1.00 11.26  ? 226 LEU B N   1 
ATOM   1225 C CA  . LEU A 1 170 ? 37.918 79.551  -54.605 1.00 18.75  ? 226 LEU B CA  1 
ATOM   1226 C C   . LEU A 1 170 ? 36.693 80.108  -55.297 1.00 17.04  ? 226 LEU B C   1 
ATOM   1227 O O   . LEU A 1 170 ? 36.441 81.314  -55.261 1.00 19.69  ? 226 LEU B O   1 
ATOM   1228 C CB  . LEU A 1 170 ? 37.669 79.486  -53.096 1.00 16.76  ? 226 LEU B CB  1 
ATOM   1229 C CG  . LEU A 1 170 ? 37.035 78.191  -52.578 1.00 28.18  ? 226 LEU B CG  1 
ATOM   1230 C CD1 . LEU A 1 170 ? 37.976 76.994  -52.735 1.00 26.73  ? 226 LEU B CD1 1 
ATOM   1231 C CD2 . LEU A 1 170 ? 36.623 78.352  -51.128 1.00 30.53  ? 226 LEU B CD2 1 
ATOM   1232 N N   . SER A 1 171 ? 35.945 79.235  -55.953 1.00 19.12  ? 227 SER B N   1 
ATOM   1233 C CA  . SER A 1 171 ? 34.901 79.691  -56.855 1.00 21.29  ? 227 SER B CA  1 
ATOM   1234 C C   . SER A 1 171 ? 33.649 78.844  -56.758 1.00 21.01  ? 227 SER B C   1 
ATOM   1235 O O   . SER A 1 171 ? 33.533 77.978  -55.895 1.00 29.97  ? 227 SER B O   1 
ATOM   1236 C CB  . SER A 1 171 ? 35.404 79.645  -58.295 1.00 23.48  ? 227 SER B CB  1 
ATOM   1237 O OG  . SER A 1 171 ? 35.781 78.326  -58.640 1.00 24.33  ? 227 SER B OG  1 
ATOM   1238 N N   . GLY A 1 172 ? 32.715 79.097  -57.666 1.00 17.55  ? 228 GLY B N   1 
ATOM   1239 C CA  . GLY A 1 172 ? 31.461 78.373  -57.672 1.00 15.61  ? 228 GLY B CA  1 
ATOM   1240 C C   . GLY A 1 172 ? 30.621 78.711  -56.460 1.00 18.64  ? 228 GLY B C   1 
ATOM   1241 O O   . GLY A 1 172 ? 30.796 79.753  -55.836 1.00 25.58  ? 228 GLY B O   1 
ATOM   1242 N N   . LYS A 1 173 ? 29.712 77.810  -56.122 1.00 14.45  ? 229 LYS B N   1 
ATOM   1243 C CA  . LYS A 1 173 ? 28.787 78.034  -55.037 1.00 14.84  ? 229 LYS B CA  1 
ATOM   1244 C C   . LYS A 1 173 ? 29.170 77.183  -53.826 1.00 21.46  ? 229 LYS B C   1 
ATOM   1245 O O   . LYS A 1 173 ? 29.708 76.082  -53.961 1.00 30.54  ? 229 LYS B O   1 
ATOM   1246 C CB  . LYS A 1 173 ? 27.361 77.716  -55.500 1.00 13.98  ? 229 LYS B CB  1 
ATOM   1247 C CG  . LYS A 1 173 ? 27.048 76.238  -55.551 1.00 21.93  ? 229 LYS B CG  1 
ATOM   1248 C CD  . LYS A 1 173 ? 25.607 75.980  -55.950 1.00 36.33  ? 229 LYS B CD  1 
ATOM   1249 C CE  . LYS A 1 173 ? 25.413 76.065  -57.453 1.00 44.84  ? 229 LYS B CE  1 
ATOM   1250 N NZ  . LYS A 1 173 ? 25.273 77.465  -57.937 1.00 51.40  ? 229 LYS B NZ  1 
ATOM   1251 N N   . LEU A 1 174 ? 28.911 77.717  -52.641 1.00 20.07  ? 230 LEU B N   1 
ATOM   1252 C CA  . LEU A 1 174 ? 29.118 76.984  -51.403 1.00 15.47  ? 230 LEU B CA  1 
ATOM   1253 C C   . LEU A 1 174 ? 28.162 75.805  -51.355 1.00 15.08  ? 230 LEU B C   1 
ATOM   1254 O O   . LEU A 1 174 ? 26.976 75.956  -51.612 1.00 26.15  ? 230 LEU B O   1 
ATOM   1255 C CB  . LEU A 1 174 ? 28.866 77.900  -50.214 1.00 19.59  ? 230 LEU B CB  1 
ATOM   1256 C CG  . LEU A 1 174 ? 29.878 79.017  -49.955 1.00 16.02  ? 230 LEU B CG  1 
ATOM   1257 C CD1 . LEU A 1 174 ? 29.485 79.753  -48.701 1.00 15.88  ? 230 LEU B CD1 1 
ATOM   1258 C CD2 . LEU A 1 174 ? 31.265 78.423  -49.790 1.00 17.60  ? 230 LEU B CD2 1 
ATOM   1259 N N   . PRO A 1 175 ? 28.675 74.621  -51.020 1.00 15.78  ? 231 PRO B N   1 
ATOM   1260 C CA  . PRO A 1 175 ? 27.845 73.415  -51.075 1.00 15.13  ? 231 PRO B CA  1 
ATOM   1261 C C   . PRO A 1 175 ? 26.845 73.342  -49.917 1.00 16.33  ? 231 PRO B C   1 
ATOM   1262 O O   . PRO A 1 175 ? 27.142 73.776  -48.809 1.00 10.64  ? 231 PRO B O   1 
ATOM   1263 C CB  . PRO A 1 175 ? 28.869 72.300  -50.918 1.00 14.55  ? 231 PRO B CB  1 
ATOM   1264 C CG  . PRO A 1 175 ? 29.910 72.915  -49.990 1.00 11.21  ? 231 PRO B CG  1 
ATOM   1265 C CD  . PRO A 1 175 ? 30.005 74.359  -50.436 1.00 14.69  ? 231 PRO B CD  1 
ATOM   1266 N N   . ALA A 1 176 ? 25.682 72.764  -50.184 1.00 17.24  ? 232 ALA B N   1 
ATOM   1267 C CA  . ALA A 1 176 ? 24.659 72.539  -49.176 1.00 14.72  ? 232 ALA B CA  1 
ATOM   1268 C C   . ALA A 1 176 ? 25.224 71.768  -47.984 1.00 17.45  ? 232 ALA B C   1 
ATOM   1269 O O   . ALA A 1 176 ? 24.728 71.882  -46.869 1.00 23.98  ? 232 ALA B O   1 
ATOM   1270 C CB  . ALA A 1 176 ? 23.492 71.780  -49.796 1.00 7.60   ? 232 ALA B CB  1 
ATOM   1271 N N   . SER A 1 177 ? 26.281 71.005  -48.233 1.00 16.74  ? 233 SER B N   1 
ATOM   1272 C CA  . SER A 1 177 ? 27.024 70.292  -47.196 1.00 14.25  ? 233 SER B CA  1 
ATOM   1273 C C   . SER A 1 177 ? 27.390 71.170  -46.011 1.00 18.47  ? 233 SER B C   1 
ATOM   1274 O O   . SER A 1 177 ? 27.464 70.700  -44.883 1.00 17.62  ? 233 SER B O   1 
ATOM   1275 C CB  . SER A 1 177 ? 28.333 69.803  -47.789 1.00 19.39  ? 233 SER B CB  1 
ATOM   1276 O OG  . SER A 1 177 ? 28.253 68.434  -48.090 1.00 39.64  ? 233 SER B OG  1 
ATOM   1277 N N   . ILE A 1 178 ? 27.657 72.442  -46.284 1.00 14.99  ? 234 ILE B N   1 
ATOM   1278 C CA  . ILE A 1 178 ? 28.045 73.390  -45.261 1.00 9.50   ? 234 ILE B CA  1 
ATOM   1279 C C   . ILE A 1 178 ? 27.044 73.374  -44.097 1.00 11.56  ? 234 ILE B C   1 
ATOM   1280 O O   . ILE A 1 178 ? 27.415 73.647  -42.959 1.00 16.20  ? 234 ILE B O   1 
ATOM   1281 C CB  . ILE A 1 178 ? 28.193 74.816  -45.869 1.00 28.11  ? 234 ILE B CB  1 
ATOM   1282 C CG1 . ILE A 1 178 ? 29.279 75.609  -45.156 1.00 30.45  ? 234 ILE B CG1 1 
ATOM   1283 C CG2 . ILE A 1 178 ? 26.876 75.575  -45.848 1.00 24.12  ? 234 ILE B CG2 1 
ATOM   1284 C CD1 . ILE A 1 178 ? 30.639 75.057  -45.355 1.00 33.65  ? 234 ILE B CD1 1 
ATOM   1285 N N   . GLY A 1 179 ? 25.788 73.012  -44.371 1.00 15.47  ? 235 GLY B N   1 
ATOM   1286 C CA  . GLY A 1 179 ? 24.751 72.962  -43.341 1.00 11.78  ? 235 GLY B CA  1 
ATOM   1287 C C   . GLY A 1 179 ? 24.957 71.874  -42.283 1.00 19.58  ? 235 GLY B C   1 
ATOM   1288 O O   . GLY A 1 179 ? 24.253 71.816  -41.277 1.00 17.72  ? 235 GLY B O   1 
ATOM   1289 N N   . ASN A 1 180 ? 25.920 70.995  -42.517 1.00 18.13  ? 236 ASN B N   1 
ATOM   1290 C CA  . ASN A 1 180 ? 26.233 69.936  -41.580 1.00 26.27  ? 236 ASN B CA  1 
ATOM   1291 C C   . ASN A 1 180 ? 27.271 70.356  -40.556 1.00 27.21  ? 236 ASN B C   1 
ATOM   1292 O O   . ASN A 1 180 ? 27.540 69.627  -39.606 1.00 24.65  ? 236 ASN B O   1 
ATOM   1293 C CB  . ASN A 1 180 ? 26.693 68.681  -42.317 1.00 30.45  ? 236 ASN B CB  1 
ATOM   1294 C CG  . ASN A 1 180 ? 25.535 67.827  -42.753 1.00 42.69  ? 236 ASN B CG  1 
ATOM   1295 O OD1 . ASN A 1 180 ? 25.354 67.550  -43.942 1.00 38.10  ? 236 ASN B OD1 1 
ATOM   1296 N ND2 . ASN A 1 180 ? 24.719 67.412  -41.783 1.00 52.27  ? 236 ASN B ND2 1 
ATOM   1297 N N   . LEU A 1 181 ? 27.827 71.552  -40.710 1.00 24.26  ? 237 LEU B N   1 
ATOM   1298 C CA  . LEU A 1 181 ? 28.811 71.961  -39.737 1.00 18.71  ? 237 LEU B CA  1 
ATOM   1299 C C   . LEU A 1 181 ? 27.997 72.648  -38.667 1.00 17.27  ? 237 LEU B C   1 
ATOM   1300 O O   . LEU A 1 181 ? 27.679 73.831  -38.766 1.00 25.57  ? 237 LEU B O   1 
ATOM   1301 C CB  . LEU A 1 181 ? 29.780 72.964  -40.380 1.00 17.50  ? 237 LEU B CB  1 
ATOM   1302 C CG  . LEU A 1 181 ? 30.541 72.516  -41.641 1.00 20.32  ? 237 LEU B CG  1 
ATOM   1303 C CD1 . LEU A 1 181 ? 31.417 73.634  -42.174 1.00 8.51   ? 237 LEU B CD1 1 
ATOM   1304 C CD2 . LEU A 1 181 ? 31.387 71.284  -41.352 1.00 9.17   ? 237 LEU B CD2 1 
ATOM   1305 N N   . LYS A 1 182 ? 27.740 71.916  -37.595 1.00 17.53  ? 238 LYS B N   1 
ATOM   1306 C CA  . LYS A 1 182 ? 26.842 72.391  -36.554 1.00 20.88  ? 238 LYS B CA  1 
ATOM   1307 C C   . LYS A 1 182 ? 27.624 73.090  -35.481 1.00 13.80  ? 238 LYS B C   1 
ATOM   1308 O O   . LYS A 1 182 ? 27.050 73.696  -34.585 1.00 26.13  ? 238 LYS B O   1 
ATOM   1309 C CB  . LYS A 1 182 ? 26.063 71.222  -35.935 1.00 30.31  ? 238 LYS B CB  1 
ATOM   1310 C CG  . LYS A 1 182 ? 24.636 71.048  -36.460 1.00 29.07  ? 238 LYS B CG  1 
ATOM   1311 C CD  . LYS A 1 182 ? 24.591 70.300  -37.769 1.00 33.99  ? 238 LYS B CD  1 
ATOM   1312 C CE  . LYS A 1 182 ? 23.194 70.348  -38.391 1.00 41.49  ? 238 LYS B CE  1 
ATOM   1313 N NZ  . LYS A 1 182 ? 23.119 69.583  -39.677 1.00 49.27  ? 238 LYS B NZ  1 
ATOM   1314 N N   . ARG A 1 183 ? 28.939 72.953  -35.522 1.00 12.83  ? 239 ARG B N   1 
ATOM   1315 C CA  . ARG A 1 183 ? 29.776 73.680  -34.570 1.00 13.41  ? 239 ARG B CA  1 
ATOM   1316 C C   . ARG A 1 183 ? 30.491 74.903  -35.115 1.00 12.91  ? 239 ARG B C   1 
ATOM   1317 O O   . ARG A 1 183 ? 31.227 75.517  -34.354 1.00 10.77  ? 239 ARG B O   1 
ATOM   1318 C CB  . ARG A 1 183 ? 30.792 72.752  -33.890 1.00 17.27  ? 239 ARG B CB  1 
ATOM   1319 C CG  . ARG A 1 183 ? 30.165 71.487  -33.348 1.00 22.92  ? 239 ARG B CG  1 
ATOM   1320 C CD  . ARG A 1 183 ? 31.102 70.733  -32.448 1.00 43.60  ? 239 ARG B CD  1 
ATOM   1321 N NE  . ARG A 1 183 ? 30.452 70.464  -31.168 1.00 67.65  ? 239 ARG B NE  1 
ATOM   1322 C CZ  . ARG A 1 183 ? 30.927 69.646  -30.235 1.00 78.02  ? 239 ARG B CZ  1 
ATOM   1323 N NH1 . ARG A 1 183 ? 32.070 69.000  -30.436 1.00 78.84  ? 239 ARG B NH1 1 
ATOM   1324 N NH2 . ARG A 1 183 ? 30.253 69.474  -29.101 1.00 81.27  ? 239 ARG B NH2 1 
ATOM   1325 N N   . VAL A 1 184 ? 30.341 75.229  -36.410 1.00 7.24   ? 240 VAL B N   1 
ATOM   1326 C CA  . VAL A 1 184 ? 31.160 76.294  -37.016 1.00 7.32   ? 240 VAL B CA  1 
ATOM   1327 C C   . VAL A 1 184 ? 30.771 77.705  -36.556 1.00 6.73   ? 240 VAL B C   1 
ATOM   1328 O O   . VAL A 1 184 ? 29.604 78.039  -36.427 1.00 12.37  ? 240 VAL B O   1 
ATOM   1329 C CB  . VAL A 1 184 ? 31.223 76.196  -38.588 1.00 16.53  ? 240 VAL B CB  1 
ATOM   1330 C CG1 . VAL A 1 184 ? 30.058 76.941  -39.252 1.00 6.77   ? 240 VAL B CG1 1 
ATOM   1331 C CG2 . VAL A 1 184 ? 32.548 76.727  -39.114 1.00 7.94   ? 240 VAL B CG2 1 
ATOM   1332 N N   . GLN A 1 185 ? 31.763 78.543  -36.315 1.00 6.95   ? 241 GLN B N   1 
ATOM   1333 C CA  . GLN A 1 185 ? 31.530 79.827  -35.657 1.00 13.26  ? 241 GLN B CA  1 
ATOM   1334 C C   . GLN A 1 185 ? 31.825 81.000  -36.570 1.00 12.30  ? 241 GLN B C   1 
ATOM   1335 O O   . GLN A 1 185 ? 31.032 81.941  -36.680 1.00 7.64   ? 241 GLN B O   1 
ATOM   1336 C CB  . GLN A 1 185 ? 32.290 79.937  -34.334 1.00 6.78   ? 241 GLN B CB  1 
ATOM   1337 C CG  . GLN A 1 185 ? 31.642 79.190  -33.176 1.00 19.67  ? 241 GLN B CG  1 
ATOM   1338 C CD  . GLN A 1 185 ? 32.349 79.443  -31.834 1.00 23.81  ? 241 GLN B CD  1 
ATOM   1339 O OE1 . GLN A 1 185 ? 32.853 78.513  -31.200 1.00 23.57  ? 241 GLN B OE1 1 
ATOM   1340 N NE2 . GLN A 1 185 ? 32.378 80.706  -31.402 1.00 24.77  ? 241 GLN B NE2 1 
ATOM   1341 N N   . THR A 1 186 ? 33.038 80.998  -37.105 1.00 19.59  ? 242 THR B N   1 
ATOM   1342 C CA  . THR A 1 186 ? 33.403 81.900  -38.186 1.00 17.49  ? 242 THR B CA  1 
ATOM   1343 C C   . THR A 1 186 ? 33.571 81.204  -39.544 1.00 7.83   ? 242 THR B C   1 
ATOM   1344 O O   . THR A 1 186 ? 34.302 80.221  -39.675 1.00 8.61   ? 242 THR B O   1 
ATOM   1345 C CB  . THR A 1 186 ? 34.693 82.640  -37.857 1.00 18.76  ? 242 THR B CB  1 
ATOM   1346 O OG1 . THR A 1 186 ? 34.470 83.469  -36.705 1.00 17.71  ? 242 THR B OG1 1 
ATOM   1347 C CG2 . THR A 1 186 ? 35.117 83.494  -39.056 1.00 7.45   ? 242 THR B CG2 1 
ATOM   1348 N N   . ILE A 1 187 ? 32.882 81.728  -40.551 1.00 10.85  ? 243 ILE B N   1 
ATOM   1349 C CA  . ILE A 1 187 ? 33.173 81.381  -41.934 1.00 7.11   ? 243 ILE B CA  1 
ATOM   1350 C C   . ILE A 1 187 ? 33.741 82.597  -42.662 1.00 18.19  ? 243 ILE B C   1 
ATOM   1351 O O   . ILE A 1 187 ? 33.041 83.577  -42.865 1.00 6.55   ? 243 ILE B O   1 
ATOM   1352 C CB  . ILE A 1 187 ? 31.935 80.826  -42.645 1.00 15.72  ? 243 ILE B CB  1 
ATOM   1353 C CG1 . ILE A 1 187 ? 31.606 79.456  -42.051 1.00 6.91   ? 243 ILE B CG1 1 
ATOM   1354 C CG2 . ILE A 1 187 ? 32.174 80.713  -44.185 1.00 11.81  ? 243 ILE B CG2 1 
ATOM   1355 C CD1 . ILE A 1 187 ? 30.330 78.859  -42.547 1.00 7.51   ? 243 ILE B CD1 1 
ATOM   1356 N N   . ALA A 1 188 ? 35.030 82.557  -43.001 1.00 16.83  ? 244 ALA B N   1 
ATOM   1357 C CA  . ALA A 1 188 ? 35.635 83.688  -43.690 1.00 10.56  ? 244 ALA B CA  1 
ATOM   1358 C C   . ALA A 1 188 ? 36.103 83.314  -45.090 1.00 11.03  ? 244 ALA B C   1 
ATOM   1359 O O   . ALA A 1 188 ? 37.179 82.736  -45.276 1.00 11.49  ? 244 ALA B O   1 
ATOM   1360 C CB  . ALA A 1 188 ? 36.798 84.212  -42.874 1.00 8.29   ? 244 ALA B CB  1 
ATOM   1361 N N   . ILE A 1 189 ? 35.315 83.665  -46.096 1.00 17.86  ? 245 ILE B N   1 
ATOM   1362 C CA  . ILE A 1 189 ? 35.797 83.521  -47.461 1.00 14.24  ? 245 ILE B CA  1 
ATOM   1363 C C   . ILE A 1 189 ? 35.454 84.806  -48.198 1.00 12.23  ? 245 ILE B C   1 
ATOM   1364 O O   . ILE A 1 189 ? 34.421 84.894  -48.848 1.00 14.38  ? 245 ILE B O   1 
ATOM   1365 C CB  . ILE A 1 189 ? 35.088 82.314  -48.137 1.00 9.72   ? 245 ILE B CB  1 
ATOM   1366 C CG1 . ILE A 1 189 ? 35.180 81.081  -47.229 1.00 8.48   ? 245 ILE B CG1 1 
ATOM   1367 C CG2 . ILE A 1 189 ? 35.690 82.012  -49.515 1.00 15.06  ? 245 ILE B CG2 1 
ATOM   1368 C CD1 . ILE A 1 189 ? 34.342 79.878  -47.648 1.00 8.43   ? 245 ILE B CD1 1 
ATOM   1369 N N   . TYR A 1 190 ? 36.407 85.726  -48.252 1.00 12.45  ? 246 TYR B N   1 
ATOM   1370 C CA  . TYR A 1 190 ? 36.147 87.053  -48.788 1.00 10.55  ? 246 TYR B CA  1 
ATOM   1371 C C   . TYR A 1 190 ? 37.274 87.476  -49.725 1.00 13.45  ? 246 TYR B C   1 
ATOM   1372 O O   . TYR A 1 190 ? 38.413 87.010  -49.589 1.00 18.65  ? 246 TYR B O   1 
ATOM   1373 C CB  . TYR A 1 190 ? 35.950 88.075  -47.658 1.00 9.04   ? 246 TYR B CB  1 
ATOM   1374 C CG  . TYR A 1 190 ? 37.083 88.148  -46.652 1.00 11.77  ? 246 TYR B CG  1 
ATOM   1375 C CD1 . TYR A 1 190 ? 38.258 88.809  -46.953 1.00 8.22   ? 246 TYR B CD1 1 
ATOM   1376 C CD2 . TYR A 1 190 ? 36.959 87.576  -45.390 1.00 8.39   ? 246 TYR B CD2 1 
ATOM   1377 C CE1 . TYR A 1 190 ? 39.280 88.879  -46.049 1.00 8.74   ? 246 TYR B CE1 1 
ATOM   1378 C CE2 . TYR A 1 190 ? 37.985 87.652  -44.466 1.00 8.22   ? 246 TYR B CE2 1 
ATOM   1379 C CZ  . TYR A 1 190 ? 39.141 88.300  -44.803 1.00 9.70   ? 246 TYR B CZ  1 
ATOM   1380 O OH  . TYR A 1 190 ? 40.184 88.376  -43.907 1.00 9.97   ? 246 TYR B OH  1 
ATOM   1381 N N   . THR A 1 191 ? 36.947 88.362  -50.662 1.00 14.61  ? 247 THR B N   1 
ATOM   1382 C CA  . THR A 1 191 ? 37.878 88.741  -51.718 1.00 21.64  ? 247 THR B CA  1 
ATOM   1383 C C   . THR A 1 191 ? 38.322 87.484  -52.457 1.00 8.86   ? 247 THR B C   1 
ATOM   1384 O O   . THR A 1 191 ? 39.495 87.163  -52.540 1.00 9.57   ? 247 THR B O   1 
ATOM   1385 C CB  . THR A 1 191 ? 39.068 89.513  -51.146 1.00 26.75  ? 247 THR B CB  1 
ATOM   1386 O OG1 . THR A 1 191 ? 38.597 90.393  -50.109 1.00 8.23   ? 247 THR B OG1 1 
ATOM   1387 C CG2 . THR A 1 191 ? 39.783 90.293  -52.258 1.00 9.02   ? 247 THR B CG2 1 
ATOM   1388 N N   . SER A 1 192 ? 37.331 86.748  -52.931 1.00 11.74  ? 248 SER B N   1 
ATOM   1389 C CA  . SER A 1 192 ? 37.545 85.524  -53.692 1.00 19.69  ? 248 SER B CA  1 
ATOM   1390 C C   . SER A 1 192 ? 36.764 85.518  -55.005 1.00 21.55  ? 248 SER B C   1 
ATOM   1391 O O   . SER A 1 192 ? 36.391 86.572  -55.519 1.00 18.48  ? 248 SER B O   1 
ATOM   1392 C CB  . SER A 1 192 ? 37.245 84.283  -52.860 1.00 17.53  ? 248 SER B CB  1 
ATOM   1393 O OG  . SER A 1 192 ? 38.262 84.094  -51.901 1.00 12.59  ? 248 SER B OG  1 
ATOM   1394 N N   . LEU A 1 193 ? 36.667 84.340  -55.607 1.00 19.33  ? 249 LEU B N   1 
ATOM   1395 C CA  . LEU A 1 193 ? 35.899 84.125  -56.840 1.00 19.12  ? 249 LEU B CA  1 
ATOM   1396 C C   . LEU A 1 193 ? 34.498 83.511  -56.686 1.00 13.72  ? 249 LEU B C   1 
ATOM   1397 O O   . LEU A 1 193 ? 33.937 83.033  -57.664 1.00 20.26  ? 249 LEU B O   1 
ATOM   1398 C CB  . LEU A 1 193 ? 36.735 83.385  -57.898 1.00 9.57   ? 249 LEU B CB  1 
ATOM   1399 C CG  . LEU A 1 193 ? 38.048 84.123  -58.198 1.00 36.17  ? 249 LEU B CG  1 
ATOM   1400 C CD1 . LEU A 1 193 ? 38.947 83.375  -59.190 1.00 10.83  ? 249 LEU B CD1 1 
ATOM   1401 C CD2 . LEU A 1 193 ? 37.737 85.518  -58.692 1.00 9.60   ? 249 LEU B CD2 1 
ATOM   1402 N N   . LEU A 1 194 ? 33.983 83.408  -55.467 1.00 15.12  ? 250 LEU B N   1 
ATOM   1403 C CA  . LEU A 1 194 ? 32.654 82.804  -55.247 1.00 11.83  ? 250 LEU B CA  1 
ATOM   1404 C C   . LEU A 1 194 ? 31.528 83.395  -56.102 1.00 12.47  ? 250 LEU B C   1 
ATOM   1405 O O   . LEU A 1 194 ? 31.403 84.616  -56.223 1.00 13.47  ? 250 LEU B O   1 
ATOM   1406 C CB  . LEU A 1 194 ? 32.245 82.933  -53.781 1.00 11.44  ? 250 LEU B CB  1 
ATOM   1407 C CG  . LEU A 1 194 ? 32.898 82.057  -52.717 1.00 20.73  ? 250 LEU B CG  1 
ATOM   1408 C CD1 . LEU A 1 194 ? 32.146 82.257  -51.371 1.00 8.45   ? 250 LEU B CD1 1 
ATOM   1409 C CD2 . LEU A 1 194 ? 32.936 80.578  -53.133 1.00 8.09   ? 250 LEU B CD2 1 
ATOM   1410 N N   . SER A 1 195 ? 30.704 82.526  -56.680 1.00 9.72   ? 251 SER B N   1 
ATOM   1411 C CA  . SER A 1 195 ? 29.515 82.954  -57.424 1.00 17.11  ? 251 SER B CA  1 
ATOM   1412 C C   . SER A 1 195 ? 28.350 82.013  -57.157 1.00 18.80  ? 251 SER B C   1 
ATOM   1413 O O   . SER A 1 195 ? 28.490 81.030  -56.444 1.00 28.88  ? 251 SER B O   1 
ATOM   1414 C CB  . SER A 1 195 ? 29.799 83.022  -58.928 1.00 20.01  ? 251 SER B CB  1 
ATOM   1415 O OG  . SER A 1 195 ? 30.468 81.853  -59.361 1.00 26.12  ? 251 SER B OG  1 
ATOM   1416 N N   . GLY A 1 196 ? 27.193 82.307  -57.731 1.00 19.62  ? 252 GLY B N   1 
ATOM   1417 C CA  . GLY A 1 196 ? 26.003 81.541  -57.404 1.00 21.67  ? 252 GLY B CA  1 
ATOM   1418 C C   . GLY A 1 196 ? 25.464 81.930  -56.037 1.00 19.87  ? 252 GLY B C   1 
ATOM   1419 O O   . GLY A 1 196 ? 26.032 82.779  -55.348 1.00 13.43  ? 252 GLY B O   1 
ATOM   1420 N N   . PRO A 1 197 ? 24.338 81.336  -55.651 1.00 19.23  ? 253 PRO B N   1 
ATOM   1421 C CA  . PRO A 1 197 ? 23.675 81.696  -54.393 1.00 14.97  ? 253 PRO B CA  1 
ATOM   1422 C C   . PRO A 1 197 ? 24.273 81.097  -53.102 1.00 18.25  ? 253 PRO B C   1 
ATOM   1423 O O   . PRO A 1 197 ? 24.891 80.031  -53.118 1.00 22.41  ? 253 PRO B O   1 
ATOM   1424 C CB  . PRO A 1 197 ? 22.231 81.216  -54.610 1.00 14.31  ? 253 PRO B CB  1 
ATOM   1425 C CG  . PRO A 1 197 ? 22.344 80.108  -55.617 1.00 18.16  ? 253 PRO B CG  1 
ATOM   1426 C CD  . PRO A 1 197 ? 23.499 80.484  -56.515 1.00 22.13  ? 253 PRO B CD  1 
ATOM   1427 N N   . ILE A 1 198 ? 24.089 81.820  -51.995 1.00 16.20  ? 254 ILE B N   1 
ATOM   1428 C CA  . ILE A 1 198 ? 24.346 81.314  -50.653 1.00 10.87  ? 254 ILE B CA  1 
ATOM   1429 C C   . ILE A 1 198 ? 23.351 80.195  -50.412 1.00 12.81  ? 254 ILE B C   1 
ATOM   1430 O O   . ILE A 1 198 ? 22.152 80.392  -50.599 1.00 17.08  ? 254 ILE B O   1 
ATOM   1431 C CB  . ILE A 1 198 ? 24.098 82.414  -49.599 1.00 14.70  ? 254 ILE B CB  1 
ATOM   1432 C CG1 . ILE A 1 198 ? 25.037 83.598  -49.818 1.00 9.20   ? 254 ILE B CG1 1 
ATOM   1433 C CG2 . ILE A 1 198 ? 24.268 81.873  -48.165 1.00 19.25  ? 254 ILE B CG2 1 
ATOM   1434 C CD1 . ILE A 1 198 ? 24.569 84.856  -49.113 1.00 5.52   ? 254 ILE B CD1 1 
ATOM   1435 N N   . PRO A 1 199 ? 23.831 79.004  -50.020 1.00 13.15  ? 255 PRO B N   1 
ATOM   1436 C CA  . PRO A 1 199 ? 22.829 77.938  -49.882 1.00 9.70   ? 255 PRO B CA  1 
ATOM   1437 C C   . PRO A 1 199 ? 21.950 78.174  -48.664 1.00 12.34  ? 255 PRO B C   1 
ATOM   1438 O O   . PRO A 1 199 ? 22.470 78.584  -47.620 1.00 15.16  ? 255 PRO B O   1 
ATOM   1439 C CB  . PRO A 1 199 ? 23.671 76.673  -49.709 1.00 8.35   ? 255 PRO B CB  1 
ATOM   1440 C CG  . PRO A 1 199 ? 24.996 77.162  -49.180 1.00 11.33  ? 255 PRO B CG  1 
ATOM   1441 C CD  . PRO A 1 199 ? 25.204 78.541  -49.756 1.00 10.09  ? 255 PRO B CD  1 
ATOM   1442 N N   . ASP A 1 200 ? 20.647 77.934  -48.810 1.00 4.25   ? 256 ASP B N   1 
ATOM   1443 C CA  . ASP A 1 200 ? 19.709 77.991  -47.700 1.00 10.69  ? 256 ASP B CA  1 
ATOM   1444 C C   . ASP A 1 200 ? 20.169 77.129  -46.518 1.00 15.33  ? 256 ASP B C   1 
ATOM   1445 O O   . ASP A 1 200 ? 19.982 77.512  -45.345 1.00 14.32  ? 256 ASP B O   1 
ATOM   1446 C CB  . ASP A 1 200 ? 18.297 77.601  -48.146 1.00 11.71  ? 256 ASP B CB  1 
ATOM   1447 C CG  . ASP A 1 200 ? 17.635 78.682  -48.983 1.00 31.02  ? 256 ASP B CG  1 
ATOM   1448 O OD1 . ASP A 1 200 ? 16.976 79.572  -48.398 1.00 36.47  ? 256 ASP B OD1 1 
ATOM   1449 O OD2 . ASP A 1 200 ? 17.778 78.646  -50.227 1.00 41.13  ? 256 ASP B OD2 1 
ATOM   1450 N N   . GLU A 1 201 ? 20.827 76.009  -46.819 1.00 9.60   ? 257 GLU B N   1 
ATOM   1451 C CA  . GLU A 1 201 ? 21.290 75.100  -45.771 1.00 14.08  ? 257 GLU B CA  1 
ATOM   1452 C C   . GLU A 1 201 ? 22.174 75.772  -44.736 1.00 11.71  ? 257 GLU B C   1 
ATOM   1453 O O   . GLU A 1 201 ? 22.368 75.239  -43.656 1.00 18.85  ? 257 GLU B O   1 
ATOM   1454 C CB  . GLU A 1 201 ? 21.983 73.869  -46.346 1.00 16.80  ? 257 GLU B CB  1 
ATOM   1455 C CG  . GLU A 1 201 ? 21.040 72.958  -47.097 1.00 15.64  ? 257 GLU B CG  1 
ATOM   1456 C CD  . GLU A 1 201 ? 20.809 73.415  -48.539 1.00 21.77  ? 257 GLU B CD  1 
ATOM   1457 O OE1 . GLU A 1 201 ? 21.320 74.498  -48.933 1.00 14.38  ? 257 GLU B OE1 1 
ATOM   1458 O OE2 . GLU A 1 201 ? 20.127 72.672  -49.286 1.00 28.87  ? 257 GLU B OE2 1 
ATOM   1459 N N   . ILE A 1 202 ? 22.696 76.947  -45.055 1.00 6.92   ? 258 ILE B N   1 
ATOM   1460 C CA  . ILE A 1 202 ? 23.528 77.658  -44.098 1.00 9.58   ? 258 ILE B CA  1 
ATOM   1461 C C   . ILE A 1 202 ? 22.776 77.974  -42.804 1.00 8.06   ? 258 ILE B C   1 
ATOM   1462 O O   . ILE A 1 202 ? 23.389 78.148  -41.764 1.00 12.02  ? 258 ILE B O   1 
ATOM   1463 C CB  . ILE A 1 202 ? 24.137 78.960  -44.694 1.00 22.77  ? 258 ILE B CB  1 
ATOM   1464 C CG1 . ILE A 1 202 ? 25.625 79.049  -44.340 1.00 20.41  ? 258 ILE B CG1 1 
ATOM   1465 C CG2 . ILE A 1 202 ? 23.384 80.196  -44.212 1.00 21.17  ? 258 ILE B CG2 1 
ATOM   1466 C CD1 . ILE A 1 202 ? 26.146 80.440  -44.238 1.00 13.60  ? 258 ILE B CD1 1 
ATOM   1467 N N   . GLY A 1 203 ? 21.450 78.032  -42.866 1.00 7.34   ? 259 GLY B N   1 
ATOM   1468 C CA  . GLY A 1 203 ? 20.657 78.296  -41.678 1.00 15.69  ? 259 GLY B CA  1 
ATOM   1469 C C   . GLY A 1 203 ? 20.732 77.149  -40.670 1.00 20.59  ? 259 GLY B C   1 
ATOM   1470 O O   . GLY A 1 203 ? 20.359 77.306  -39.502 1.00 11.97  ? 259 GLY B O   1 
ATOM   1471 N N   . TYR A 1 204 ? 21.219 75.995  -41.126 1.00 20.29  ? 260 TYR B N   1 
ATOM   1472 C CA  . TYR A 1 204 ? 21.476 74.855  -40.248 1.00 14.88  ? 260 TYR B CA  1 
ATOM   1473 C C   . TYR A 1 204 ? 22.745 75.007  -39.406 1.00 15.96  ? 260 TYR B C   1 
ATOM   1474 O O   . TYR A 1 204 ? 23.006 74.155  -38.558 1.00 22.17  ? 260 TYR B O   1 
ATOM   1475 C CB  . TYR A 1 204 ? 21.571 73.539  -41.031 1.00 7.63   ? 260 TYR B CB  1 
ATOM   1476 C CG  . TYR A 1 204 ? 20.272 73.047  -41.608 1.00 4.87   ? 260 TYR B CG  1 
ATOM   1477 C CD1 . TYR A 1 204 ? 19.104 73.027  -40.852 1.00 4.56   ? 260 TYR B CD1 1 
ATOM   1478 C CD2 . TYR A 1 204 ? 20.208 72.617  -42.930 1.00 9.15   ? 260 TYR B CD2 1 
ATOM   1479 C CE1 . TYR A 1 204 ? 17.903 72.574  -41.401 1.00 5.09   ? 260 TYR B CE1 1 
ATOM   1480 C CE2 . TYR A 1 204 ? 19.033 72.157  -43.477 1.00 5.00   ? 260 TYR B CE2 1 
ATOM   1481 C CZ  . TYR A 1 204 ? 17.881 72.136  -42.721 1.00 12.93  ? 260 TYR B CZ  1 
ATOM   1482 O OH  . TYR A 1 204 ? 16.713 71.678  -43.311 1.00 12.91  ? 260 TYR B OH  1 
ATOM   1483 N N   . CYS A 1 205 ? 23.532 76.068  -39.604 1.00 9.01   ? 261 CYS B N   1 
ATOM   1484 C CA  . CYS A 1 205 ? 24.754 76.157  -38.815 1.00 10.24  ? 261 CYS B CA  1 
ATOM   1485 C C   . CYS A 1 205 ? 24.433 76.910  -37.548 1.00 19.56  ? 261 CYS B C   1 
ATOM   1486 O O   . CYS A 1 205 ? 24.592 78.132  -37.474 1.00 21.60  ? 261 CYS B O   1 
ATOM   1487 C CB  . CYS A 1 205 ? 25.800 76.940  -39.604 1.00 5.17   ? 261 CYS B CB  1 
ATOM   1488 S SG  . CYS A 1 205 ? 26.209 76.160  -41.175 1.00 13.37  ? 261 CYS B SG  1 
ATOM   1489 N N   . THR A 1 206 ? 24.162 76.152  -36.495 1.00 22.49  ? 262 THR B N   1 
ATOM   1490 C CA  . THR A 1 206 ? 23.412 76.696  -35.366 1.00 18.37  ? 262 THR B CA  1 
ATOM   1491 C C   . THR A 1 206 ? 24.288 77.586  -34.507 1.00 14.21  ? 262 THR B C   1 
ATOM   1492 O O   . THR A 1 206 ? 23.796 78.483  -33.840 1.00 19.87  ? 262 THR B O   1 
ATOM   1493 C CB  . THR A 1 206 ? 22.727 75.571  -34.524 1.00 25.28  ? 262 THR B CB  1 
ATOM   1494 O OG1 . THR A 1 206 ? 23.142 75.654  -33.158 1.00 31.11  ? 262 THR B OG1 1 
ATOM   1495 C CG2 . THR A 1 206 ? 23.096 74.212  -35.045 1.00 22.00  ? 262 THR B CG2 1 
ATOM   1496 N N   . GLU A 1 207 ? 25.591 77.341  -34.559 1.00 4.71   ? 263 GLU B N   1 
ATOM   1497 C CA  . GLU A 1 207 ? 26.572 78.111  -33.810 1.00 4.81   ? 263 GLU B CA  1 
ATOM   1498 C C   . GLU A 1 207 ? 27.229 79.259  -34.572 1.00 4.77   ? 263 GLU B C   1 
ATOM   1499 O O   . GLU A 1 207 ? 28.096 79.902  -34.026 1.00 7.52   ? 263 GLU B O   1 
ATOM   1500 C CB  . GLU A 1 207 ? 27.683 77.172  -33.317 1.00 8.93   ? 263 GLU B CB  1 
ATOM   1501 C CG  . GLU A 1 207 ? 27.169 76.053  -32.450 1.00 10.81  ? 263 GLU B CG  1 
ATOM   1502 C CD  . GLU A 1 207 ? 26.630 76.581  -31.133 1.00 24.82  ? 263 GLU B CD  1 
ATOM   1503 O OE1 . GLU A 1 207 ? 27.310 77.440  -30.520 1.00 27.13  ? 263 GLU B OE1 1 
ATOM   1504 O OE2 . GLU A 1 207 ? 25.526 76.153  -30.719 1.00 29.10  ? 263 GLU B OE2 1 
ATOM   1505 N N   . LEU A 1 208 ? 26.854 79.495  -35.831 1.00 17.35  ? 264 LEU B N   1 
ATOM   1506 C CA  . LEU A 1 208 ? 27.464 80.564  -36.634 1.00 4.61   ? 264 LEU B CA  1 
ATOM   1507 C C   . LEU A 1 208 ? 27.364 81.964  -36.006 1.00 14.60  ? 264 LEU B C   1 
ATOM   1508 O O   . LEU A 1 208 ? 26.300 82.390  -35.564 1.00 5.36   ? 264 LEU B O   1 
ATOM   1509 C CB  . LEU A 1 208 ? 26.862 80.599  -38.035 1.00 9.72   ? 264 LEU B CB  1 
ATOM   1510 C CG  . LEU A 1 208 ? 27.669 81.407  -39.046 1.00 6.02   ? 264 LEU B CG  1 
ATOM   1511 C CD1 . LEU A 1 208 ? 29.022 80.753  -39.199 1.00 5.30   ? 264 LEU B CD1 1 
ATOM   1512 C CD2 . LEU A 1 208 ? 26.950 81.464  -40.389 1.00 6.68   ? 264 LEU B CD2 1 
ATOM   1513 N N   . GLN A 1 209 ? 28.487 82.672  -35.993 1.00 4.44   ? 265 GLN B N   1 
ATOM   1514 C CA  . GLN A 1 209 ? 28.625 83.951  -35.304 1.00 8.58   ? 265 GLN B CA  1 
ATOM   1515 C C   . GLN A 1 209 ? 29.028 85.008  -36.304 1.00 5.22   ? 265 GLN B C   1 
ATOM   1516 O O   . GLN A 1 209 ? 28.459 86.095  -36.339 1.00 8.50   ? 265 GLN B O   1 
ATOM   1517 C CB  . GLN A 1 209 ? 29.638 83.894  -34.135 1.00 5.30   ? 265 GLN B CB  1 
ATOM   1518 C CG  . GLN A 1 209 ? 29.206 83.024  -32.967 1.00 21.09  ? 265 GLN B CG  1 
ATOM   1519 C CD  . GLN A 1 209 ? 30.082 83.183  -31.719 1.00 31.43  ? 265 GLN B CD  1 
ATOM   1520 O OE1 . GLN A 1 209 ? 30.951 84.064  -31.641 1.00 28.08  ? 265 GLN B OE1 1 
ATOM   1521 N NE2 . GLN A 1 209 ? 29.850 82.317  -30.735 1.00 35.17  ? 265 GLN B NE2 1 
ATOM   1522 N N   . ASN A 1 210 ? 30.116 84.718  -37.009 1.00 4.68   ? 266 ASN B N   1 
ATOM   1523 C CA  . ASN A 1 210 ? 30.647 85.591  -38.040 1.00 4.75   ? 266 ASN B CA  1 
ATOM   1524 C C   . ASN A 1 210 ? 30.615 84.959  -39.427 1.00 9.14   ? 266 ASN B C   1 
ATOM   1525 O O   . ASN A 1 210 ? 31.203 83.891  -39.655 1.00 9.65   ? 266 ASN B O   1 
ATOM   1526 C CB  . ASN A 1 210 ? 32.076 85.966  -37.676 1.00 7.06   ? 266 ASN B CB  1 
ATOM   1527 C CG  . ASN A 1 210 ? 32.217 86.311  -36.215 1.00 6.92   ? 266 ASN B CG  1 
ATOM   1528 O OD1 . ASN A 1 210 ? 31.466 87.123  -35.684 1.00 8.80   ? 266 ASN B OD1 1 
ATOM   1529 N ND2 . ASN A 1 210 ? 33.145 85.652  -35.543 1.00 10.57  ? 266 ASN B ND2 1 
ATOM   1530 N N   . LEU A 1 211 ? 29.914 85.609  -40.353 1.00 7.69   ? 267 LEU B N   1 
ATOM   1531 C CA  . LEU A 1 211 ? 29.862 85.127  -41.738 1.00 4.71   ? 267 LEU B CA  1 
ATOM   1532 C C   . LEU A 1 211 ? 30.386 86.213  -42.653 1.00 17.92  ? 267 LEU B C   1 
ATOM   1533 O O   . LEU A 1 211 ? 29.747 87.268  -42.784 1.00 4.25   ? 267 LEU B O   1 
ATOM   1534 C CB  . LEU A 1 211 ? 28.431 84.754  -42.130 1.00 4.26   ? 267 LEU B CB  1 
ATOM   1535 C CG  . LEU A 1 211 ? 28.254 84.335  -43.592 1.00 12.83  ? 267 LEU B CG  1 
ATOM   1536 C CD1 . LEU A 1 211 ? 29.117 83.121  -43.924 1.00 5.05   ? 267 LEU B CD1 1 
ATOM   1537 C CD2 . LEU A 1 211 ? 26.789 84.061  -43.909 1.00 9.82   ? 267 LEU B CD2 1 
ATOM   1538 N N   . TYR A 1 212 ? 31.563 85.981  -43.244 1.00 5.33   ? 268 TYR B N   1 
ATOM   1539 C CA  . TYR A 1 212 ? 32.178 86.959  -44.133 1.00 11.24  ? 268 TYR B CA  1 
ATOM   1540 C C   . TYR A 1 212 ? 32.332 86.430  -45.544 1.00 15.39  ? 268 TYR B C   1 
ATOM   1541 O O   . TYR A 1 212 ? 33.235 85.649  -45.828 1.00 15.61  ? 268 TYR B O   1 
ATOM   1542 C CB  . TYR A 1 212 ? 33.567 87.332  -43.609 1.00 11.99  ? 268 TYR B CB  1 
ATOM   1543 C CG  . TYR A 1 212 ? 33.578 87.766  -42.155 1.00 11.52  ? 268 TYR B CG  1 
ATOM   1544 C CD1 . TYR A 1 212 ? 32.514 88.467  -41.618 1.00 11.49  ? 268 TYR B CD1 1 
ATOM   1545 C CD2 . TYR A 1 212 ? 34.659 87.467  -41.320 1.00 12.53  ? 268 TYR B CD2 1 
ATOM   1546 C CE1 . TYR A 1 212 ? 32.514 88.854  -40.287 1.00 17.97  ? 268 TYR B CE1 1 
ATOM   1547 C CE2 . TYR A 1 212 ? 34.669 87.865  -39.983 1.00 13.14  ? 268 TYR B CE2 1 
ATOM   1548 C CZ  . TYR A 1 212 ? 33.590 88.559  -39.481 1.00 17.59  ? 268 TYR B CZ  1 
ATOM   1549 O OH  . TYR A 1 212 ? 33.567 88.955  -38.162 1.00 23.36  ? 268 TYR B OH  1 
ATOM   1550 N N   . LEU A 1 213 ? 31.428 86.858  -46.414 1.00 15.82  ? 269 LEU B N   1 
ATOM   1551 C CA  . LEU A 1 213 ? 31.431 86.544  -47.844 1.00 10.11  ? 269 LEU B CA  1 
ATOM   1552 C C   . LEU A 1 213 ? 31.722 87.710  -48.830 1.00 17.39  ? 269 LEU B C   1 
ATOM   1553 O O   . LEU A 1 213 ? 31.411 87.619  -50.025 1.00 10.98  ? 269 LEU B O   1 
ATOM   1554 C CB  . LEU A 1 213 ? 30.195 85.705  -48.203 1.00 14.21  ? 269 LEU B CB  1 
ATOM   1555 C CG  . LEU A 1 213 ? 30.123 84.403  -47.374 1.00 12.38  ? 269 LEU B CG  1 
ATOM   1556 C CD1 . LEU A 1 213 ? 28.832 83.670  -47.557 1.00 5.10   ? 269 LEU B CD1 1 
ATOM   1557 C CD2 . LEU A 1 213 ? 31.285 83.459  -47.695 1.00 6.13   ? 269 LEU B CD2 1 
ATOM   1558 N N   . TYR A 1 214 ? 32.180 88.848  -48.320 1.00 17.25  ? 270 TYR B N   1 
ATOM   1559 C CA  . TYR A 1 214 ? 32.279 90.055  -49.152 1.00 14.78  ? 270 TYR B CA  1 
ATOM   1560 C C   . TYR A 1 214 ? 33.278 89.991  -50.345 1.00 14.58  ? 270 TYR B C   1 
ATOM   1561 O O   . TYR A 1 214 ? 34.184 89.161  -50.374 1.00 11.21  ? 270 TYR B O   1 
ATOM   1562 C CB  . TYR A 1 214 ? 32.505 91.295  -48.270 1.00 7.18   ? 270 TYR B CB  1 
ATOM   1563 C CG  . TYR A 1 214 ? 33.802 91.321  -47.469 1.00 7.45   ? 270 TYR B CG  1 
ATOM   1564 C CD1 . TYR A 1 214 ? 34.958 91.861  -48.006 1.00 5.95   ? 270 TYR B CD1 1 
ATOM   1565 C CD2 . TYR A 1 214 ? 33.851 90.861  -46.152 1.00 13.89  ? 270 TYR B CD2 1 
ATOM   1566 C CE1 . TYR A 1 214 ? 36.138 91.925  -47.278 1.00 6.49   ? 270 TYR B CE1 1 
ATOM   1567 C CE2 . TYR A 1 214 ? 35.036 90.908  -45.412 1.00 7.10   ? 270 TYR B CE2 1 
ATOM   1568 C CZ  . TYR A 1 214 ? 36.178 91.442  -45.988 1.00 9.85   ? 270 TYR B CZ  1 
ATOM   1569 O OH  . TYR A 1 214 ? 37.366 91.513  -45.278 1.00 9.85   ? 270 TYR B OH  1 
ATOM   1570 N N   . GLN A 1 215 ? 33.086 90.852  -51.340 1.00 14.31  ? 271 GLN B N   1 
ATOM   1571 C CA  . GLN A 1 215 ? 33.954 90.870  -52.544 1.00 13.08  ? 271 GLN B CA  1 
ATOM   1572 C C   . GLN A 1 215 ? 34.056 89.533  -53.283 1.00 9.25   ? 271 GLN B C   1 
ATOM   1573 O O   . GLN A 1 215 ? 35.143 88.987  -53.476 1.00 9.34   ? 271 GLN B O   1 
ATOM   1574 C CB  . GLN A 1 215 ? 35.342 91.435  -52.245 1.00 10.60  ? 271 GLN B CB  1 
ATOM   1575 C CG  . GLN A 1 215 ? 35.269 92.775  -51.520 1.00 19.48  ? 271 GLN B CG  1 
ATOM   1576 C CD  . GLN A 1 215 ? 36.610 93.452  -51.387 1.00 17.61  ? 271 GLN B CD  1 
ATOM   1577 O OE1 . GLN A 1 215 ? 37.508 92.967  -50.697 1.00 21.08  ? 271 GLN B OE1 1 
ATOM   1578 N NE2 . GLN A 1 215 ? 36.756 94.583  -52.055 1.00 14.95  ? 271 GLN B NE2 1 
ATOM   1579 N N   . ASN A 1 216 ? 32.899 89.011  -53.661 1.00 6.03   ? 272 ASN B N   1 
ATOM   1580 C CA  . ASN A 1 216 ? 32.784 87.857  -54.537 1.00 12.27  ? 272 ASN B CA  1 
ATOM   1581 C C   . ASN A 1 216 ? 31.779 88.224  -55.649 1.00 9.62   ? 272 ASN B C   1 
ATOM   1582 O O   . ASN A 1 216 ? 31.452 89.397  -55.842 1.00 5.57   ? 272 ASN B O   1 
ATOM   1583 C CB  . ASN A 1 216 ? 32.318 86.610  -53.761 1.00 13.96  ? 272 ASN B CB  1 
ATOM   1584 C CG  . ASN A 1 216 ? 33.383 86.069  -52.811 1.00 18.15  ? 272 ASN B CG  1 
ATOM   1585 O OD1 . ASN A 1 216 ? 34.350 85.434  -53.243 1.00 7.47   ? 272 ASN B OD1 1 
ATOM   1586 N ND2 . ASN A 1 216 ? 33.204 86.311  -51.506 1.00 7.57   ? 272 ASN B ND2 1 
ATOM   1587 N N   . SER A 1 217 ? 31.372 87.241  -56.431 1.00 6.10   ? 273 SER B N   1 
ATOM   1588 C CA  . SER A 1 217 ? 30.253 87.384  -57.368 1.00 12.28  ? 273 SER B CA  1 
ATOM   1589 C C   . SER A 1 217 ? 28.916 86.786  -56.936 1.00 11.73  ? 273 SER B C   1 
ATOM   1590 O O   . SER A 1 217 ? 28.087 86.479  -57.780 1.00 29.66  ? 273 SER B O   1 
ATOM   1591 C CB  . SER A 1 217 ? 30.631 86.996  -58.795 1.00 10.82  ? 273 SER B CB  1 
ATOM   1592 O OG  . SER A 1 217 ? 31.747 87.774  -59.187 1.00 15.12  ? 273 SER B OG  1 
ATOM   1593 N N   . ILE A 1 218 ? 28.769 86.496  -55.653 1.00 10.02  ? 274 ILE B N   1 
ATOM   1594 C CA  . ILE A 1 218 ? 27.578 85.822  -55.126 1.00 8.57   ? 274 ILE B CA  1 
ATOM   1595 C C   . ILE A 1 218 ? 26.266 86.446  -55.610 1.00 12.51  ? 274 ILE B C   1 
ATOM   1596 O O   . ILE A 1 218 ? 26.083 87.671  -55.588 1.00 5.98   ? 274 ILE B O   1 
ATOM   1597 C CB  . ILE A 1 218 ? 27.606 85.786  -53.576 1.00 4.75   ? 274 ILE B CB  1 
ATOM   1598 C CG1 . ILE A 1 218 ? 28.804 84.955  -53.077 1.00 7.66   ? 274 ILE B CG1 1 
ATOM   1599 C CG2 . ILE A 1 218 ? 26.315 85.223  -53.031 1.00 4.41   ? 274 ILE B CG2 1 
ATOM   1600 C CD1 . ILE A 1 218 ? 29.105 85.154  -51.589 1.00 14.14  ? 274 ILE B CD1 1 
ATOM   1601 N N   . SER A 1 219 ? 25.375 85.579  -56.084 1.00 17.71  ? 275 SER B N   1 
ATOM   1602 C CA  . SER A 1 219 ? 24.135 86.003  -56.724 1.00 9.79   ? 275 SER B CA  1 
ATOM   1603 C C   . SER A 1 219 ? 22.945 85.435  -55.974 1.00 14.89  ? 275 SER B C   1 
ATOM   1604 O O   . SER A 1 219 ? 23.105 84.782  -54.949 1.00 28.28  ? 275 SER B O   1 
ATOM   1605 C CB  . SER A 1 219 ? 24.103 85.511  -58.161 1.00 11.50  ? 275 SER B CB  1 
ATOM   1606 O OG  . SER A 1 219 ? 24.271 84.101  -58.194 1.00 18.64  ? 275 SER B OG  1 
ATOM   1607 N N   . GLY A 1 220 ? 21.744 85.673  -56.481 1.00 7.27   ? 276 GLY B N   1 
ATOM   1608 C CA  . GLY A 1 220 ? 20.560 85.240  -55.770 1.00 4.65   ? 276 GLY B CA  1 
ATOM   1609 C C   . GLY A 1 220 ? 20.228 86.200  -54.642 1.00 16.57  ? 276 GLY B C   1 
ATOM   1610 O O   . GLY A 1 220 ? 20.725 87.330  -54.605 1.00 23.12  ? 276 GLY B O   1 
ATOM   1611 N N   . SER A 1 221 ? 19.374 85.749  -53.732 1.00 4.79   ? 277 SER B N   1 
ATOM   1612 C CA  . SER A 1 221 ? 18.931 86.553  -52.609 1.00 10.30  ? 277 SER B CA  1 
ATOM   1613 C C   . SER A 1 221 ? 19.468 86.017  -51.275 1.00 8.82   ? 277 SER B C   1 
ATOM   1614 O O   . SER A 1 221 ? 19.786 84.834  -51.156 1.00 10.51  ? 277 SER B O   1 
ATOM   1615 C CB  . SER A 1 221 ? 17.406 86.627  -52.586 1.00 14.47  ? 277 SER B CB  1 
ATOM   1616 O OG  . SER A 1 221 ? 16.837 85.352  -52.404 1.00 21.15  ? 277 SER B OG  1 
ATOM   1617 N N   . ILE A 1 222 ? 19.613 86.903  -50.294 1.00 12.22  ? 278 ILE B N   1 
ATOM   1618 C CA  . ILE A 1 222 ? 20.014 86.497  -48.947 1.00 10.99  ? 278 ILE B CA  1 
ATOM   1619 C C   . ILE A 1 222 ? 18.973 85.538  -48.417 1.00 7.01   ? 278 ILE B C   1 
ATOM   1620 O O   . ILE A 1 222 ? 17.807 85.904  -48.300 1.00 9.83   ? 278 ILE B O   1 
ATOM   1621 C CB  . ILE A 1 222 ? 20.062 87.706  -48.000 1.00 5.44   ? 278 ILE B CB  1 
ATOM   1622 C CG1 . ILE A 1 222 ? 21.095 88.715  -48.495 1.00 5.07   ? 278 ILE B CG1 1 
ATOM   1623 C CG2 . ILE A 1 222 ? 20.398 87.258  -46.589 1.00 2.16   ? 278 ILE B CG2 1 
ATOM   1624 C CD1 . ILE A 1 222 ? 20.852 90.103  -48.033 1.00 6.85   ? 278 ILE B CD1 1 
ATOM   1625 N N   . PRO A 1 223 ? 19.374 84.303  -48.110 1.00 5.22   ? 279 PRO B N   1 
ATOM   1626 C CA  . PRO A 1 223 ? 18.370 83.320  -47.696 1.00 2.76   ? 279 PRO B CA  1 
ATOM   1627 C C   . PRO A 1 223 ? 17.680 83.705  -46.405 1.00 5.18   ? 279 PRO B C   1 
ATOM   1628 O O   . PRO A 1 223 ? 18.295 84.244  -45.492 1.00 19.06  ? 279 PRO B O   1 
ATOM   1629 C CB  . PRO A 1 223 ? 19.181 82.033  -47.522 1.00 3.05   ? 279 PRO B CB  1 
ATOM   1630 C CG  . PRO A 1 223 ? 20.581 82.501  -47.368 1.00 7.16   ? 279 PRO B CG  1 
ATOM   1631 C CD  . PRO A 1 223 ? 20.706 83.701  -48.234 1.00 6.32   ? 279 PRO B CD  1 
ATOM   1632 N N   . THR A 1 224 ? 16.385 83.442  -46.357 1.00 6.97   ? 280 THR B N   1 
ATOM   1633 C CA  . THR A 1 224 ? 15.554 83.719  -45.198 1.00 9.53   ? 280 THR B CA  1 
ATOM   1634 C C   . THR A 1 224 ? 16.046 82.946  -43.964 1.00 14.75  ? 280 THR B C   1 
ATOM   1635 O O   . THR A 1 224 ? 16.001 83.451  -42.839 1.00 14.83  ? 280 THR B O   1 
ATOM   1636 C CB  . THR A 1 224 ? 14.107 83.310  -45.502 1.00 5.75   ? 280 THR B CB  1 
ATOM   1637 O OG1 . THR A 1 224 ? 13.547 84.228  -46.449 1.00 18.38  ? 280 THR B OG1 1 
ATOM   1638 C CG2 . THR A 1 224 ? 13.292 83.369  -44.260 1.00 9.20   ? 280 THR B CG2 1 
ATOM   1639 N N   . THR A 1 225 ? 16.545 81.736  -44.204 1.00 2.66   ? 281 THR B N   1 
ATOM   1640 C CA  . THR A 1 225 ? 16.979 80.813  -43.167 1.00 2.76   ? 281 THR B CA  1 
ATOM   1641 C C   . THR A 1 225 ? 18.012 81.417  -42.230 1.00 12.06  ? 281 THR B C   1 
ATOM   1642 O O   . THR A 1 225 ? 18.179 80.965  -41.096 1.00 21.63  ? 281 THR B O   1 
ATOM   1643 C CB  . THR A 1 225 ? 17.546 79.529  -43.788 1.00 14.99  ? 281 THR B CB  1 
ATOM   1644 O OG1 . THR A 1 225 ? 18.681 79.840  -44.621 1.00 9.65   ? 281 THR B OG1 1 
ATOM   1645 C CG2 . THR A 1 225 ? 16.470 78.861  -44.636 1.00 9.75   ? 281 THR B CG2 1 
ATOM   1646 N N   . ILE A 1 226 ? 18.667 82.475  -42.685 1.00 9.98   ? 282 ILE B N   1 
ATOM   1647 C CA  . ILE A 1 226 ? 19.681 83.142  -41.879 1.00 17.83  ? 282 ILE B CA  1 
ATOM   1648 C C   . ILE A 1 226 ? 19.096 83.743  -40.598 1.00 17.13  ? 282 ILE B C   1 
ATOM   1649 O O   . ILE A 1 226 ? 19.799 83.919  -39.614 1.00 22.68  ? 282 ILE B O   1 
ATOM   1650 C CB  . ILE A 1 226 ? 20.544 84.114  -42.753 1.00 17.67  ? 282 ILE B CB  1 
ATOM   1651 C CG1 . ILE A 1 226 ? 21.611 83.295  -43.481 1.00 24.09  ? 282 ILE B CG1 1 
ATOM   1652 C CG2 . ILE A 1 226 ? 21.257 85.160  -41.943 1.00 12.11  ? 282 ILE B CG2 1 
ATOM   1653 C CD1 . ILE A 1 226 ? 22.555 84.132  -44.321 1.00 34.94  ? 282 ILE B CD1 1 
ATOM   1654 N N   . GLY A 1 227 ? 17.790 83.985  -40.586 1.00 19.45  ? 283 GLY B N   1 
ATOM   1655 C CA  . GLY A 1 227 ? 17.129 84.493  -39.394 1.00 14.24  ? 283 GLY B CA  1 
ATOM   1656 C C   . GLY A 1 227 ? 17.062 83.492  -38.250 1.00 14.14  ? 283 GLY B C   1 
ATOM   1657 O O   . GLY A 1 227 ? 16.852 83.858  -37.093 1.00 31.14  ? 283 GLY B O   1 
ATOM   1658 N N   . GLY A 1 228 ? 17.237 82.217  -38.557 1.00 10.57  ? 284 GLY B N   1 
ATOM   1659 C CA  . GLY A 1 228 ? 17.172 81.210  -37.519 1.00 2.38   ? 284 GLY B CA  1 
ATOM   1660 C C   . GLY A 1 228 ? 18.523 80.978  -36.875 1.00 20.62  ? 284 GLY B C   1 
ATOM   1661 O O   . GLY A 1 228 ? 18.650 80.064  -36.058 1.00 19.34  ? 284 GLY B O   1 
ATOM   1662 N N   . LEU A 1 229 ? 19.529 81.789  -37.223 1.00 10.15  ? 285 LEU B N   1 
ATOM   1663 C CA  . LEU A 1 229 ? 20.840 81.636  -36.599 1.00 6.86   ? 285 LEU B CA  1 
ATOM   1664 C C   . LEU A 1 229 ? 20.903 82.564  -35.383 1.00 10.96  ? 285 LEU B C   1 
ATOM   1665 O O   . LEU A 1 229 ? 21.185 83.753  -35.522 1.00 12.14  ? 285 LEU B O   1 
ATOM   1666 C CB  . LEU A 1 229 ? 21.928 82.070  -37.593 1.00 4.95   ? 285 LEU B CB  1 
ATOM   1667 C CG  . LEU A 1 229 ? 22.057 81.295  -38.909 1.00 10.56  ? 285 LEU B CG  1 
ATOM   1668 C CD1 . LEU A 1 229 ? 23.112 81.894  -39.836 1.00 10.93  ? 285 LEU B CD1 1 
ATOM   1669 C CD2 . LEU A 1 229 ? 22.376 79.844  -38.646 1.00 9.13   ? 285 LEU B CD2 1 
ATOM   1670 N N   . LYS A 1 230 ? 20.752 82.010  -34.186 1.00 11.58  ? 286 LYS B N   1 
ATOM   1671 C CA  . LYS A 1 230 ? 20.575 82.844  -32.982 1.00 12.74  ? 286 LYS B CA  1 
ATOM   1672 C C   . LYS A 1 230 ? 21.886 83.401  -32.410 1.00 12.37  ? 286 LYS B C   1 
ATOM   1673 O O   . LYS A 1 230 ? 21.871 84.351  -31.628 1.00 14.47  ? 286 LYS B O   1 
ATOM   1674 C CB  . LYS A 1 230 ? 19.780 82.098  -31.879 1.00 4.49   ? 286 LYS B CB  1 
ATOM   1675 C CG  . LYS A 1 230 ? 18.333 81.704  -32.260 1.00 9.96   ? 286 LYS B CG  1 
ATOM   1676 C CD  . LYS A 1 230 ? 17.599 82.880  -32.923 1.00 20.91  ? 286 LYS B CD  1 
ATOM   1677 C CE  . LYS A 1 230 ? 16.082 82.668  -33.084 1.00 20.73  ? 286 LYS B CE  1 
ATOM   1678 N NZ  . LYS A 1 230 ? 15.681 82.215  -34.460 1.00 23.36  ? 286 LYS B NZ  1 
ATOM   1679 N N   . LYS A 1 231 ? 23.016 82.819  -32.795 1.00 8.09   ? 287 LYS B N   1 
ATOM   1680 C CA  . LYS A 1 231 ? 24.290 83.285  -32.284 1.00 9.65   ? 287 LYS B CA  1 
ATOM   1681 C C   . LYS A 1 231 ? 24.968 84.285  -33.216 1.00 7.30   ? 287 LYS B C   1 
ATOM   1682 O O   . LYS A 1 231 ? 26.085 84.713  -32.944 1.00 15.19  ? 287 LYS B O   1 
ATOM   1683 C CB  . LYS A 1 231 ? 25.241 82.116  -32.018 1.00 21.38  ? 287 LYS B CB  1 
ATOM   1684 C CG  . LYS A 1 231 ? 24.685 80.996  -31.160 1.00 25.29  ? 287 LYS B CG  1 
ATOM   1685 C CD  . LYS A 1 231 ? 24.373 81.452  -29.755 1.00 33.00  ? 287 LYS B CD  1 
ATOM   1686 C CE  . LYS A 1 231 ? 24.000 80.256  -28.880 1.00 38.54  ? 287 LYS B CE  1 
ATOM   1687 N NZ  . LYS A 1 231 ? 25.142 79.289  -28.750 1.00 37.40  ? 287 LYS B NZ  1 
ATOM   1688 N N   . LEU A 1 232 ? 24.303 84.657  -34.309 1.00 8.45   ? 288 LEU B N   1 
ATOM   1689 C CA  . LEU A 1 232 ? 24.924 85.516  -35.328 1.00 14.68  ? 288 LEU B CA  1 
ATOM   1690 C C   . LEU A 1 232 ? 25.223 86.928  -34.815 1.00 15.44  ? 288 LEU B C   1 
ATOM   1691 O O   . LEU A 1 232 ? 24.370 87.600  -34.230 1.00 15.44  ? 288 LEU B O   1 
ATOM   1692 C CB  . LEU A 1 232 ? 24.057 85.592  -36.579 1.00 10.00  ? 288 LEU B CB  1 
ATOM   1693 C CG  . LEU A 1 232 ? 24.677 86.152  -37.866 1.00 7.85   ? 288 LEU B CG  1 
ATOM   1694 C CD1 . LEU A 1 232 ? 25.739 85.224  -38.440 1.00 6.39   ? 288 LEU B CD1 1 
ATOM   1695 C CD2 . LEU A 1 232 ? 23.588 86.385  -38.896 1.00 4.24   ? 288 LEU B CD2 1 
ATOM   1696 N N   . GLN A 1 233 ? 26.448 87.367  -35.055 1.00 5.97   ? 289 GLN B N   1 
ATOM   1697 C CA  . GLN A 1 233 ? 26.943 88.643  -34.541 1.00 14.69  ? 289 GLN B CA  1 
ATOM   1698 C C   . GLN A 1 233 ? 27.294 89.569  -35.701 1.00 11.74  ? 289 GLN B C   1 
ATOM   1699 O O   . GLN A 1 233 ? 26.878 90.728  -35.734 1.00 16.69  ? 289 GLN B O   1 
ATOM   1700 C CB  . GLN A 1 233 ? 28.103 88.447  -33.547 1.00 2.88   ? 289 GLN B CB  1 
ATOM   1701 C CG  . GLN A 1 233 ? 27.809 87.305  -32.575 1.00 30.52  ? 289 GLN B CG  1 
ATOM   1702 C CD  . GLN A 1 233 ? 28.607 87.327  -31.278 1.00 22.51  ? 289 GLN B CD  1 
ATOM   1703 O OE1 . GLN A 1 233 ? 29.773 87.718  -31.248 1.00 17.91  ? 289 GLN B OE1 1 
ATOM   1704 N NE2 . GLN A 1 233 ? 27.971 86.880  -30.195 1.00 25.01  ? 289 GLN B NE2 1 
ATOM   1705 N N   . SER A 1 234 ? 28.140 89.084  -36.597 1.00 7.20   ? 290 SER B N   1 
ATOM   1706 C CA  . SER A 1 234 ? 28.596 89.912  -37.698 1.00 16.29  ? 290 SER B CA  1 
ATOM   1707 C C   . SER A 1 234 ? 28.318 89.250  -39.039 1.00 17.23  ? 290 SER B C   1 
ATOM   1708 O O   . SER A 1 234 ? 28.576 88.060  -39.227 1.00 19.64  ? 290 SER B O   1 
ATOM   1709 C CB  . SER A 1 234 ? 30.082 90.188  -37.544 1.00 11.38  ? 290 SER B CB  1 
ATOM   1710 O OG  . SER A 1 234 ? 30.777 88.957  -37.485 1.00 16.23  ? 290 SER B OG  1 
ATOM   1711 N N   . LEU A 1 235 ? 27.765 90.034  -39.955 1.00 2.70   ? 291 LEU B N   1 
ATOM   1712 C CA  . LEU A 1 235 ? 27.407 89.563  -41.291 1.00 9.76   ? 291 LEU B CA  1 
ATOM   1713 C C   . LEU A 1 235 ? 28.002 90.539  -42.318 1.00 13.67  ? 291 LEU B C   1 
ATOM   1714 O O   . LEU A 1 235 ? 27.565 91.690  -42.408 1.00 6.18   ? 291 LEU B O   1 
ATOM   1715 C CB  . LEU A 1 235 ? 25.889 89.531  -41.406 1.00 2.24   ? 291 LEU B CB  1 
ATOM   1716 C CG  . LEU A 1 235 ? 25.222 88.804  -42.568 1.00 14.90  ? 291 LEU B CG  1 
ATOM   1717 C CD1 . LEU A 1 235 ? 25.702 87.364  -42.650 1.00 13.65  ? 291 LEU B CD1 1 
ATOM   1718 C CD2 . LEU A 1 235 ? 23.707 88.847  -42.400 1.00 2.92   ? 291 LEU B CD2 1 
ATOM   1719 N N   . LEU A 1 236 ? 29.016 90.101  -43.063 1.00 6.81   ? 292 LEU B N   1 
ATOM   1720 C CA  . LEU A 1 236 ? 29.552 90.946  -44.113 1.00 6.35   ? 292 LEU B CA  1 
ATOM   1721 C C   . LEU A 1 236 ? 29.325 90.311  -45.467 1.00 7.58   ? 292 LEU B C   1 
ATOM   1722 O O   . LEU A 1 236 ? 29.989 89.348  -45.834 1.00 12.80  ? 292 LEU B O   1 
ATOM   1723 C CB  . LEU A 1 236 ? 31.043 91.174  -43.894 1.00 10.35  ? 292 LEU B CB  1 
ATOM   1724 C CG  . LEU A 1 236 ? 31.418 91.816  -42.558 1.00 6.59   ? 292 LEU B CG  1 
ATOM   1725 C CD1 . LEU A 1 236 ? 32.924 91.928  -42.437 1.00 5.31   ? 292 LEU B CD1 1 
ATOM   1726 C CD2 . LEU A 1 236 ? 30.793 93.188  -42.419 1.00 4.47   ? 292 LEU B CD2 1 
ATOM   1727 N N   . LEU A 1 237 ? 28.406 90.837  -46.231 1.00 11.85  ? 293 LEU B N   1 
ATOM   1728 C CA  . LEU A 1 237 ? 28.118 90.380  -47.571 1.00 10.92  ? 293 LEU B CA  1 
ATOM   1729 C C   . LEU A 1 237 ? 28.323 91.475  -48.569 1.00 12.69  ? 293 LEU B C   1 
ATOM   1730 O O   . LEU A 1 237 ? 27.789 91.417  -49.607 1.00 8.17   ? 293 LEU B O   1 
ATOM   1731 C CB  . LEU A 1 237 ? 26.679 89.882  -47.687 1.00 5.58   ? 293 LEU B CB  1 
ATOM   1732 C CG  . LEU A 1 237 ? 26.250 88.736  -46.807 1.00 11.08  ? 293 LEU B CG  1 
ATOM   1733 C CD1 . LEU A 1 237 ? 24.855 88.373  -46.909 1.00 2.63   ? 293 LEU B CD1 1 
ATOM   1734 C CD2 . LEU A 1 237 ? 27.089 87.587  -47.026 1.00 9.34   ? 293 LEU B CD2 1 
ATOM   1735 N N   . TRP A 1 238 ? 29.068 92.499  -48.228 1.00 14.22  ? 294 TRP B N   1 
ATOM   1736 C CA  . TRP A 1 238 ? 29.251 93.612  -49.115 1.00 14.05  ? 294 TRP B CA  1 
ATOM   1737 C C   . TRP A 1 238 ? 30.035 93.308  -50.373 1.00 13.25  ? 294 TRP B C   1 
ATOM   1738 O O   . TRP A 1 238 ? 30.920 92.533  -50.371 1.00 19.07  ? 294 TRP B O   1 
ATOM   1739 C CB  . TRP A 1 238 ? 29.795 94.863  -48.413 1.00 3.14   ? 294 TRP B CB  1 
ATOM   1740 C CG  . TRP A 1 238 ? 31.091 94.718  -47.864 1.00 3.71   ? 294 TRP B CG  1 
ATOM   1741 C CD1 . TRP A 1 238 ? 31.371 94.157  -46.721 1.00 16.17  ? 294 TRP B CD1 1 
ATOM   1742 C CD2 . TRP A 1 238 ? 32.318 95.122  -48.418 1.00 7.44   ? 294 TRP B CD2 1 
ATOM   1743 N NE1 . TRP A 1 238 ? 32.656 94.158  -46.495 1.00 15.26  ? 294 TRP B NE1 1 
ATOM   1744 C CE2 . TRP A 1 238 ? 33.286 94.763  -47.528 1.00 11.66  ? 294 TRP B CE2 1 
ATOM   1745 C CE3 . TRP A 1 238 ? 32.695 95.752  -49.594 1.00 9.30   ? 294 TRP B CE3 1 
ATOM   1746 C CZ2 . TRP A 1 238 ? 34.618 94.989  -47.750 1.00 5.30   ? 294 TRP B CZ2 1 
ATOM   1747 C CZ3 . TRP A 1 238 ? 33.998 95.985  -49.810 1.00 4.86   ? 294 TRP B CZ3 1 
ATOM   1748 C CH2 . TRP A 1 238 ? 34.953 95.618  -48.889 1.00 8.64   ? 294 TRP B CH2 1 
ATOM   1749 N N   . GLN A 1 239 ? 29.691 94.016  -51.430 1.00 24.31  ? 295 GLN B N   1 
ATOM   1750 C CA  . GLN A 1 239 ? 30.263 93.873  -52.760 1.00 21.72  ? 295 GLN B CA  1 
ATOM   1751 C C   . GLN A 1 239 ? 30.141 92.528  -53.493 1.00 15.44  ? 295 GLN B C   1 
ATOM   1752 O O   . GLN A 1 239 ? 31.066 91.883  -53.771 1.00 4.71   ? 295 GLN B O   1 
ATOM   1753 C CB  . GLN A 1 239 ? 31.686 94.360  -52.743 1.00 21.95  ? 295 GLN B CB  1 
ATOM   1754 C CG  . GLN A 1 239 ? 32.139 94.860  -53.990 1.00 28.23  ? 295 GLN B CG  1 
ATOM   1755 C CD  . GLN A 1 239 ? 33.451 95.524  -53.910 1.00 35.31  ? 295 GLN B CD  1 
ATOM   1756 O OE1 . GLN A 1 239 ? 33.555 96.657  -53.482 1.00 37.32  ? 295 GLN B OE1 1 
ATOM   1757 N NE2 . GLN A 1 239 ? 34.455 94.864  -54.383 1.00 33.54  ? 295 GLN B NE2 1 
ATOM   1758 N N   . ASN A 1 240 ? 28.914 92.143  -53.705 1.00 15.67  ? 296 ASN B N   1 
ATOM   1759 C CA  . ASN A 1 240 ? 28.478 90.996  -54.461 1.00 14.57  ? 296 ASN B CA  1 
ATOM   1760 C C   . ASN A 1 240 ? 27.417 91.392  -55.489 1.00 8.59   ? 296 ASN B C   1 
ATOM   1761 O O   . ASN A 1 240 ? 27.313 92.514  -55.838 1.00 12.41  ? 296 ASN B O   1 
ATOM   1762 C CB  . ASN A 1 240 ? 27.967 89.907  -53.521 1.00 3.88   ? 296 ASN B CB  1 
ATOM   1763 C CG  . ASN A 1 240 ? 29.044 89.238  -52.765 1.00 8.16   ? 296 ASN B CG  1 
ATOM   1764 O OD1 . ASN A 1 240 ? 29.731 88.423  -53.267 1.00 8.38   ? 296 ASN B OD1 1 
ATOM   1765 N ND2 . ASN A 1 240 ? 29.140 89.546  -51.530 1.00 4.22   ? 296 ASN B ND2 1 
ATOM   1766 N N   . ASN A 1 241 ? 26.691 90.421  -56.006 1.00 7.37   ? 297 ASN B N   1 
ATOM   1767 C CA  . ASN A 1 241 ? 25.558 90.577  -56.916 1.00 10.43  ? 297 ASN B CA  1 
ATOM   1768 C C   . ASN A 1 241 ? 24.193 90.337  -56.313 1.00 16.14  ? 297 ASN B C   1 
ATOM   1769 O O   . ASN A 1 241 ? 23.262 89.994  -57.037 1.00 17.40  ? 297 ASN B O   1 
ATOM   1770 C CB  . ASN A 1 241 ? 25.777 89.814  -58.208 1.00 3.83   ? 297 ASN B CB  1 
ATOM   1771 C CG  . ASN A 1 241 ? 26.985 90.322  -58.951 1.00 5.25   ? 297 ASN B CG  1 
ATOM   1772 O OD1 . ASN A 1 241 ? 27.113 91.518  -59.174 1.00 10.49  ? 297 ASN B OD1 1 
ATOM   1773 N ND2 . ASN A 1 241 ? 27.905 89.431  -59.281 1.00 12.43  ? 297 ASN B ND2 1 
ATOM   1774 N N   . LEU A 1 242 ? 24.118 90.342  -54.985 1.00 15.47  ? 298 LEU B N   1 
ATOM   1775 C CA  . LEU A 1 242 ? 22.887 89.972  -54.282 1.00 11.92  ? 298 LEU B CA  1 
ATOM   1776 C C   . LEU A 1 242 ? 21.631 90.744  -54.685 1.00 3.45   ? 298 LEU B C   1 
ATOM   1777 O O   . LEU A 1 242 ? 21.646 91.946  -54.869 1.00 7.00   ? 298 LEU B O   1 
ATOM   1778 C CB  . LEU A 1 242 ? 23.087 90.023  -52.772 1.00 2.47   ? 298 LEU B CB  1 
ATOM   1779 C CG  . LEU A 1 242 ? 24.065 88.999  -52.195 1.00 13.51  ? 298 LEU B CG  1 
ATOM   1780 C CD1 . LEU A 1 242 ? 24.507 89.427  -50.809 1.00 14.11  ? 298 LEU B CD1 1 
ATOM   1781 C CD2 . LEU A 1 242 ? 23.429 87.628  -52.134 1.00 2.93   ? 298 LEU B CD2 1 
ATOM   1782 N N   . VAL A 1 243 ? 20.532 90.018  -54.758 1.00 10.57  ? 299 VAL B N   1 
ATOM   1783 C CA  . VAL A 1 243 ? 19.316 90.471  -55.413 1.00 12.96  ? 299 VAL B CA  1 
ATOM   1784 C C   . VAL A 1 243 ? 18.150 90.205  -54.459 1.00 12.24  ? 299 VAL B C   1 
ATOM   1785 O O   . VAL A 1 243 ? 18.311 89.452  -53.512 1.00 15.54  ? 299 VAL B O   1 
ATOM   1786 C CB  . VAL A 1 243 ? 19.199 89.675  -56.745 1.00 18.91  ? 299 VAL B CB  1 
ATOM   1787 C CG1 . VAL A 1 243 ? 17.953 88.795  -56.815 1.00 6.30   ? 299 VAL B CG1 1 
ATOM   1788 C CG2 . VAL A 1 243 ? 19.384 90.581  -57.925 1.00 2.55   ? 299 VAL B CG2 1 
ATOM   1789 N N   . GLY A 1 244 ? 17.003 90.836  -54.671 1.00 9.85   ? 300 GLY B N   1 
ATOM   1790 C CA  . GLY A 1 244 ? 15.826 90.579  -53.849 1.00 2.20   ? 300 GLY B CA  1 
ATOM   1791 C C   . GLY A 1 244 ? 15.761 91.448  -52.601 1.00 13.30  ? 300 GLY B C   1 
ATOM   1792 O O   . GLY A 1 244 ? 16.528 92.399  -52.458 1.00 22.07  ? 300 GLY B O   1 
ATOM   1793 N N   . LYS A 1 245 ? 14.858 91.118  -51.684 1.00 9.43   ? 301 LYS B N   1 
ATOM   1794 C CA  . LYS A 1 245 ? 14.656 91.929  -50.480 1.00 17.19  ? 301 LYS B CA  1 
ATOM   1795 C C   . LYS A 1 245 ? 15.462 91.423  -49.278 1.00 19.76  ? 301 LYS B C   1 
ATOM   1796 O O   . LYS A 1 245 ? 15.776 90.237  -49.179 1.00 25.66  ? 301 LYS B O   1 
ATOM   1797 C CB  . LYS A 1 245 ? 13.159 92.061  -50.124 1.00 19.60  ? 301 LYS B CB  1 
ATOM   1798 C CG  . LYS A 1 245 ? 12.517 90.829  -49.510 1.00 23.91  ? 301 LYS B CG  1 
ATOM   1799 C CD  . LYS A 1 245 ? 10.989 90.964  -49.425 1.00 38.39  ? 301 LYS B CD  1 
ATOM   1800 C CE  . LYS A 1 245 ? 10.370 91.077  -50.824 1.00 47.14  ? 301 LYS B CE  1 
ATOM   1801 N NZ  . LYS A 1 245 ? 8.886  91.246  -50.836 1.00 46.48  ? 301 LYS B NZ  1 
ATOM   1802 N N   . ILE A 1 246 ? 15.856 92.347  -48.409 1.00 13.73  ? 302 ILE B N   1 
ATOM   1803 C CA  . ILE A 1 246 ? 16.423 91.993  -47.118 1.00 11.17  ? 302 ILE B CA  1 
ATOM   1804 C C   . ILE A 1 246 ? 15.424 91.187  -46.283 1.00 9.61   ? 302 ILE B C   1 
ATOM   1805 O O   . ILE A 1 246 ? 14.308 91.624  -46.045 1.00 11.22  ? 302 ILE B O   1 
ATOM   1806 C CB  . ILE A 1 246 ? 16.819 93.237  -46.347 1.00 9.74   ? 302 ILE B CB  1 
ATOM   1807 C CG1 . ILE A 1 246 ? 17.817 94.049  -47.166 1.00 9.56   ? 302 ILE B CG1 1 
ATOM   1808 C CG2 . ILE A 1 246 ? 17.391 92.854  -44.983 1.00 11.51  ? 302 ILE B CG2 1 
ATOM   1809 C CD1 . ILE A 1 246 ? 18.175 95.397  -46.545 1.00 13.09  ? 302 ILE B CD1 1 
ATOM   1810 N N   . PRO A 1 247 ? 15.822 89.987  -45.857 1.00 9.72   ? 303 PRO B N   1 
ATOM   1811 C CA  . PRO A 1 247 ? 14.894 89.136  -45.111 1.00 5.71   ? 303 PRO B CA  1 
ATOM   1812 C C   . PRO A 1 247 ? 14.479 89.765  -43.771 1.00 10.97  ? 303 PRO B C   1 
ATOM   1813 O O   . PRO A 1 247 ? 15.287 90.157  -42.956 1.00 10.14  ? 303 PRO B O   1 
ATOM   1814 C CB  . PRO A 1 247 ? 15.711 87.863  -44.854 1.00 2.00   ? 303 PRO B CB  1 
ATOM   1815 C CG  . PRO A 1 247 ? 16.887 87.934  -45.780 1.00 12.81  ? 303 PRO B CG  1 
ATOM   1816 C CD  . PRO A 1 247 ? 17.156 89.379  -46.003 1.00 8.04   ? 303 PRO B CD  1 
ATOM   1817 N N   . THR A 1 248 ? 13.188 89.833  -43.554 1.00 16.53  ? 304 THR B N   1 
ATOM   1818 C CA  . THR A 1 248 ? 12.627 90.291  -42.305 1.00 14.98  ? 304 THR B CA  1 
ATOM   1819 C C   . THR A 1 248 ? 13.183 89.502  -41.114 1.00 16.33  ? 304 THR B C   1 
ATOM   1820 O O   . THR A 1 248 ? 13.419 90.046  -40.018 1.00 11.09  ? 304 THR B O   1 
ATOM   1821 C CB  . THR A 1 248 ? 11.116 90.127  -42.411 1.00 12.42  ? 304 THR B CB  1 
ATOM   1822 O OG1 . THR A 1 248 ? 10.577 91.300  -43.043 1.00 16.72  ? 304 THR B OG1 1 
ATOM   1823 C CG2 . THR A 1 248 ? 10.504 89.918  -41.084 1.00 6.49   ? 304 THR B CG2 1 
ATOM   1824 N N   . GLU A 1 249 ? 13.445 88.222  -41.349 1.00 6.26   ? 305 GLU B N   1 
ATOM   1825 C CA  . GLU A 1 249 ? 13.846 87.352  -40.263 1.00 2.68   ? 305 GLU B CA  1 
ATOM   1826 C C   . GLU A 1 249 ? 15.220 87.681  -39.662 1.00 9.10   ? 305 GLU B C   1 
ATOM   1827 O O   . GLU A 1 249 ? 15.550 87.184  -38.581 1.00 9.78   ? 305 GLU B O   1 
ATOM   1828 C CB  . GLU A 1 249 ? 13.760 85.888  -40.682 1.00 2.00   ? 305 GLU B CB  1 
ATOM   1829 C CG  . GLU A 1 249 ? 12.337 85.385  -40.786 1.00 10.86  ? 305 GLU B CG  1 
ATOM   1830 C CD  . GLU A 1 249 ? 11.719 85.633  -42.142 1.00 17.07  ? 305 GLU B CD  1 
ATOM   1831 O OE1 . GLU A 1 249 ? 12.435 86.132  -43.031 1.00 16.00  ? 305 GLU B OE1 1 
ATOM   1832 O OE2 . GLU A 1 249 ? 10.520 85.331  -42.321 1.00 20.65  ? 305 GLU B OE2 1 
ATOM   1833 N N   . LEU A 1 250 ? 16.009 88.517  -40.341 1.00 5.70   ? 306 LEU B N   1 
ATOM   1834 C CA  . LEU A 1 250 ? 17.270 89.011  -39.775 1.00 6.08   ? 306 LEU B CA  1 
ATOM   1835 C C   . LEU A 1 250 ? 17.032 89.725  -38.455 1.00 20.68  ? 306 LEU B C   1 
ATOM   1836 O O   . LEU A 1 250 ? 17.880 89.697  -37.565 1.00 25.77  ? 306 LEU B O   1 
ATOM   1837 C CB  . LEU A 1 250 ? 17.976 89.963  -40.724 1.00 9.81   ? 306 LEU B CB  1 
ATOM   1838 C CG  . LEU A 1 250 ? 18.938 89.236  -41.645 1.00 24.15  ? 306 LEU B CG  1 
ATOM   1839 C CD1 . LEU A 1 250 ? 19.600 90.202  -42.589 1.00 31.95  ? 306 LEU B CD1 1 
ATOM   1840 C CD2 . LEU A 1 250 ? 19.963 88.521  -40.795 1.00 29.38  ? 306 LEU B CD2 1 
ATOM   1841 N N   . GLY A 1 251 ? 15.863 90.341  -38.312 1.00 12.62  ? 307 GLY B N   1 
ATOM   1842 C CA  . GLY A 1 251 ? 15.536 90.966  -37.050 1.00 12.35  ? 307 GLY B CA  1 
ATOM   1843 C C   . GLY A 1 251 ? 15.322 89.990  -35.899 1.00 14.88  ? 307 GLY B C   1 
ATOM   1844 O O   . GLY A 1 251 ? 14.995 90.410  -34.798 1.00 17.84  ? 307 GLY B O   1 
ATOM   1845 N N   . ASN A 1 252 ? 15.483 88.693  -36.149 1.00 16.09  ? 308 ASN B N   1 
ATOM   1846 C CA  . ASN A 1 252 ? 15.367 87.683  -35.088 1.00 22.92  ? 308 ASN B CA  1 
ATOM   1847 C C   . ASN A 1 252 ? 16.685 87.202  -34.484 1.00 23.57  ? 308 ASN B C   1 
ATOM   1848 O O   . ASN A 1 252 ? 16.682 86.317  -33.632 1.00 29.91  ? 308 ASN B O   1 
ATOM   1849 C CB  . ASN A 1 252 ? 14.563 86.470  -35.561 1.00 21.99  ? 308 ASN B CB  1 
ATOM   1850 C CG  . ASN A 1 252 ? 13.153 86.830  -35.947 1.00 25.59  ? 308 ASN B CG  1 
ATOM   1851 O OD1 . ASN A 1 252 ? 12.543 87.716  -35.343 1.00 25.92  ? 308 ASN B OD1 1 
ATOM   1852 N ND2 . ASN A 1 252 ? 12.625 86.155  -36.973 1.00 26.39  ? 308 ASN B ND2 1 
ATOM   1853 N N   . CYS A 1 253 ? 17.806 87.755  -34.936 1.00 21.37  ? 309 CYS B N   1 
ATOM   1854 C CA  . CYS A 1 253 ? 19.086 87.416  -34.327 1.00 21.93  ? 309 CYS B CA  1 
ATOM   1855 C C   . CYS A 1 253 ? 19.450 88.434  -33.235 1.00 15.95  ? 309 CYS B C   1 
ATOM   1856 O O   . CYS A 1 253 ? 19.942 89.522  -33.515 1.00 6.34   ? 309 CYS B O   1 
ATOM   1857 C CB  . CYS A 1 253 ? 20.172 87.387  -35.402 1.00 25.37  ? 309 CYS B CB  1 
ATOM   1858 S SG  . CYS A 1 253 ? 19.684 86.539  -36.939 1.00 19.13  ? 309 CYS B SG  1 
ATOM   1859 N N   . PRO A 1 254 ? 19.254 88.053  -31.973 1.00 12.71  ? 310 PRO B N   1 
ATOM   1860 C CA  . PRO A 1 254 ? 19.410 89.007  -30.878 1.00 9.79   ? 310 PRO B CA  1 
ATOM   1861 C C   . PRO A 1 254 ? 20.832 89.549  -30.767 1.00 19.66  ? 310 PRO B C   1 
ATOM   1862 O O   . PRO A 1 254 ? 21.033 90.656  -30.263 1.00 25.55  ? 310 PRO B O   1 
ATOM   1863 C CB  . PRO A 1 254 ? 19.087 88.159  -29.636 1.00 9.96   ? 310 PRO B CB  1 
ATOM   1864 C CG  . PRO A 1 254 ? 18.228 87.075  -30.130 1.00 11.40  ? 310 PRO B CG  1 
ATOM   1865 C CD  . PRO A 1 254 ? 18.743 86.753  -31.507 1.00 10.94  ? 310 PRO B CD  1 
ATOM   1866 N N   . GLU A 1 255 ? 21.812 88.777  -31.218 1.00 17.46  ? 311 GLU B N   1 
ATOM   1867 C CA  . GLU A 1 255 ? 23.204 89.107  -30.923 1.00 11.63  ? 311 GLU B CA  1 
ATOM   1868 C C   . GLU A 1 255 ? 23.892 89.890  -32.038 1.00 12.50  ? 311 GLU B C   1 
ATOM   1869 O O   . GLU A 1 255 ? 25.088 90.143  -31.970 1.00 16.77  ? 311 GLU B O   1 
ATOM   1870 C CB  . GLU A 1 255 ? 23.991 87.840  -30.575 1.00 15.10  ? 311 GLU B CB  1 
ATOM   1871 C CG  . GLU A 1 255 ? 23.504 87.154  -29.319 1.00 21.13  ? 311 GLU B CG  1 
ATOM   1872 C CD  . GLU A 1 255 ? 23.606 88.063  -28.130 1.00 46.64  ? 311 GLU B CD  1 
ATOM   1873 O OE1 . GLU A 1 255 ? 24.608 88.807  -28.050 1.00 57.49  ? 311 GLU B OE1 1 
ATOM   1874 O OE2 . GLU A 1 255 ? 22.684 88.058  -27.285 1.00 54.43  ? 311 GLU B OE2 1 
ATOM   1875 N N   . LEU A 1 256 ? 23.134 90.276  -33.060 1.00 10.36  ? 312 LEU B N   1 
ATOM   1876 C CA  . LEU A 1 256 ? 23.725 90.814  -34.273 1.00 10.77  ? 312 LEU B CA  1 
ATOM   1877 C C   . LEU A 1 256 ? 24.128 92.253  -34.060 1.00 9.29   ? 312 LEU B C   1 
ATOM   1878 O O   . LEU A 1 256 ? 23.280 93.103  -33.785 1.00 3.02   ? 312 LEU B O   1 
ATOM   1879 C CB  . LEU A 1 256 ? 22.678 90.746  -35.377 1.00 11.30  ? 312 LEU B CB  1 
ATOM   1880 C CG  . LEU A 1 256 ? 23.024 90.874  -36.850 1.00 12.78  ? 312 LEU B CG  1 
ATOM   1881 C CD1 . LEU A 1 256 ? 24.138 89.935  -37.214 1.00 2.00   ? 312 LEU B CD1 1 
ATOM   1882 C CD2 . LEU A 1 256 ? 21.781 90.520  -37.647 1.00 12.00  ? 312 LEU B CD2 1 
ATOM   1883 N N   . TRP A 1 257 ? 25.428 92.531  -34.126 1.00 7.73   ? 313 TRP B N   1 
ATOM   1884 C CA  . TRP A 1 257 ? 25.878 93.913  -33.985 1.00 10.56  ? 313 TRP B CA  1 
ATOM   1885 C C   . TRP A 1 257 ? 26.391 94.622  -35.244 1.00 14.39  ? 313 TRP B C   1 
ATOM   1886 O O   . TRP A 1 257 ? 26.528 95.852  -35.246 1.00 16.23  ? 313 TRP B O   1 
ATOM   1887 C CB  . TRP A 1 257 ? 26.922 94.007  -32.873 1.00 6.14   ? 313 TRP B CB  1 
ATOM   1888 C CG  . TRP A 1 257 ? 28.239 93.424  -33.258 1.00 9.52   ? 313 TRP B CG  1 
ATOM   1889 C CD1 . TRP A 1 257 ? 28.611 92.110  -33.171 1.00 3.81   ? 313 TRP B CD1 1 
ATOM   1890 C CD2 . TRP A 1 257 ? 29.362 94.128  -33.793 1.00 2.41   ? 313 TRP B CD2 1 
ATOM   1891 N NE1 . TRP A 1 257 ? 29.897 91.955  -33.633 1.00 3.59   ? 313 TRP B NE1 1 
ATOM   1892 C CE2 . TRP A 1 257 ? 30.387 93.179  -34.009 1.00 3.05   ? 313 TRP B CE2 1 
ATOM   1893 C CE3 . TRP A 1 257 ? 29.615 95.467  -34.092 1.00 7.97   ? 313 TRP B CE3 1 
ATOM   1894 C CZ2 . TRP A 1 257 ? 31.634 93.527  -34.520 1.00 3.63   ? 313 TRP B CZ2 1 
ATOM   1895 C CZ3 . TRP A 1 257 ? 30.865 95.818  -34.587 1.00 2.92   ? 313 TRP B CZ3 1 
ATOM   1896 C CH2 . TRP A 1 257 ? 31.857 94.846  -34.798 1.00 7.20   ? 313 TRP B CH2 1 
ATOM   1897 N N   . LEU A 1 258 ? 26.636 93.870  -36.317 1.00 15.18  ? 314 LEU B N   1 
ATOM   1898 C CA  . LEU A 1 258 ? 27.155 94.450  -37.565 1.00 9.90   ? 314 LEU B CA  1 
ATOM   1899 C C   . LEU A 1 258 ? 26.507 93.812  -38.792 1.00 12.88  ? 314 LEU B C   1 
ATOM   1900 O O   . LEU A 1 258 ? 26.561 92.586  -38.952 1.00 18.57  ? 314 LEU B O   1 
ATOM   1901 C CB  . LEU A 1 258 ? 28.687 94.335  -37.659 1.00 2.15   ? 314 LEU B CB  1 
ATOM   1902 C CG  . LEU A 1 258 ? 29.288 94.658  -39.046 1.00 10.21  ? 314 LEU B CG  1 
ATOM   1903 C CD1 . LEU A 1 258 ? 28.965 96.053  -39.495 1.00 9.00   ? 314 LEU B CD1 1 
ATOM   1904 C CD2 . LEU A 1 258 ? 30.786 94.476  -39.077 1.00 10.28  ? 314 LEU B CD2 1 
ATOM   1905 N N   . ILE A 1 259 ? 25.899 94.646  -39.642 1.00 5.57   ? 315 ILE B N   1 
ATOM   1906 C CA  . ILE A 1 259 ? 25.308 94.186  -40.895 1.00 9.11   ? 315 ILE B CA  1 
ATOM   1907 C C   . ILE A 1 259 ? 25.831 95.018  -42.075 1.00 8.30   ? 315 ILE B C   1 
ATOM   1908 O O   . ILE A 1 259 ? 25.540 96.211  -42.177 1.00 9.88   ? 315 ILE B O   1 
ATOM   1909 C CB  . ILE A 1 259 ? 23.773 94.339  -40.844 1.00 15.96  ? 315 ILE B CB  1 
ATOM   1910 C CG1 . ILE A 1 259 ? 23.163 93.442  -39.766 1.00 13.00  ? 315 ILE B CG1 1 
ATOM   1911 C CG2 . ILE A 1 259 ? 23.147 94.042  -42.203 1.00 11.74  ? 315 ILE B CG2 1 
ATOM   1912 C CD1 . ILE A 1 259 ? 21.639 93.609  -39.644 1.00 11.25  ? 315 ILE B CD1 1 
ATOM   1913 N N   . ASP A 1 260 ? 26.624 94.418  -42.950 1.00 7.09   ? 316 ASP B N   1 
ATOM   1914 C CA  . ASP A 1 260 ? 27.082 95.156  -44.123 1.00 11.84  ? 316 ASP B CA  1 
ATOM   1915 C C   . ASP A 1 260 ? 26.669 94.449  -45.409 1.00 16.58  ? 316 ASP B C   1 
ATOM   1916 O O   . ASP A 1 260 ? 27.207 93.395  -45.754 1.00 11.72  ? 316 ASP B O   1 
ATOM   1917 C CB  . ASP A 1 260 ? 28.590 95.326  -44.087 1.00 7.59   ? 316 ASP B CB  1 
ATOM   1918 C CG  . ASP A 1 260 ? 29.065 96.449  -44.978 1.00 12.86  ? 316 ASP B CG  1 
ATOM   1919 O OD1 . ASP A 1 260 ? 28.359 96.764  -45.949 1.00 16.89  ? 316 ASP B OD1 1 
ATOM   1920 O OD2 . ASP A 1 260 ? 30.137 97.027  -44.706 1.00 7.95   ? 316 ASP B OD2 1 
ATOM   1921 N N   . PHE A 1 261 ? 25.663 95.027  -46.062 1.00 15.47  ? 317 PHE B N   1 
ATOM   1922 C CA  . PHE A 1 261 ? 25.157 94.625  -47.380 1.00 16.57  ? 317 PHE B CA  1 
ATOM   1923 C C   . PHE A 1 261 ? 25.553 95.579  -48.510 1.00 19.88  ? 317 PHE B C   1 
ATOM   1924 O O   . PHE A 1 261 ? 25.000 95.505  -49.600 1.00 13.46  ? 317 PHE B O   1 
ATOM   1925 C CB  . PHE A 1 261 ? 23.641 94.408  -47.360 1.00 3.13   ? 317 PHE B CB  1 
ATOM   1926 C CG  . PHE A 1 261 ? 23.188 93.372  -46.359 1.00 5.41   ? 317 PHE B CG  1 
ATOM   1927 C CD1 . PHE A 1 261 ? 24.059 92.397  -45.903 1.00 9.81   ? 317 PHE B CD1 1 
ATOM   1928 C CD2 . PHE A 1 261 ? 21.889 93.372  -45.880 1.00 5.25   ? 317 PHE B CD2 1 
ATOM   1929 C CE1 . PHE A 1 261 ? 23.645 91.441  -44.983 1.00 11.95  ? 317 PHE B CE1 1 
ATOM   1930 C CE2 . PHE A 1 261 ? 21.462 92.416  -44.969 1.00 12.36  ? 317 PHE B CE2 1 
ATOM   1931 C CZ  . PHE A 1 261 ? 22.346 91.451  -44.518 1.00 15.18  ? 317 PHE B CZ  1 
ATOM   1932 N N   . SER A 1 262 ? 26.435 96.527  -48.231 1.00 2.00   ? 318 SER B N   1 
ATOM   1933 C CA  . SER A 1 262 ? 26.761 97.556  -49.205 1.00 14.18  ? 318 SER B CA  1 
ATOM   1934 C C   . SER A 1 262 ? 27.141 97.021  -50.596 1.00 4.76   ? 318 SER B C   1 
ATOM   1935 O O   . SER A 1 262 ? 27.691 95.932  -50.721 1.00 10.11  ? 318 SER B O   1 
ATOM   1936 C CB  . SER A 1 262 ? 27.917 98.409  -48.682 1.00 15.18  ? 318 SER B CB  1 
ATOM   1937 O OG  . SER A 1 262 ? 27.689 98.775  -47.343 1.00 12.34  ? 318 SER B OG  1 
ATOM   1938 N N   . GLU A 1 263 ? 26.816 97.798  -51.632 1.00 8.22   ? 319 GLU B N   1 
ATOM   1939 C CA  . GLU A 1 263 ? 27.218 97.490  -53.022 1.00 11.94  ? 319 GLU B CA  1 
ATOM   1940 C C   . GLU A 1 263 ? 26.733 96.150  -53.519 1.00 13.84  ? 319 GLU B C   1 
ATOM   1941 O O   . GLU A 1 263 ? 27.530 95.282  -53.889 1.00 2.76   ? 319 GLU B O   1 
ATOM   1942 C CB  . GLU A 1 263 ? 28.729 97.606  -53.232 1.00 9.84   ? 319 GLU B CB  1 
ATOM   1943 C CG  . GLU A 1 263 ? 29.240 99.007  -53.031 1.00 24.85  ? 319 GLU B CG  1 
ATOM   1944 C CD  . GLU A 1 263 ? 30.509 99.266  -53.784 1.00 45.68  ? 319 GLU B CD  1 
ATOM   1945 O OE1 . GLU A 1 263 ? 31.463 99.797  -53.168 1.00 50.97  ? 319 GLU B OE1 1 
ATOM   1946 O OE2 . GLU A 1 263 ? 30.544 98.946  -54.997 1.00 53.22  ? 319 GLU B OE2 1 
ATOM   1947 N N   . ASN A 1 264 ? 25.415 95.995  -53.457 1.00 7.72   ? 320 ASN B N   1 
ATOM   1948 C CA  . ASN A 1 264 ? 24.707 94.864  -54.026 1.00 6.45   ? 320 ASN B CA  1 
ATOM   1949 C C   . ASN A 1 264 ? 23.558 95.382  -54.913 1.00 15.21  ? 320 ASN B C   1 
ATOM   1950 O O   . ASN A 1 264 ? 23.542 96.555  -55.322 1.00 11.21  ? 320 ASN B O   1 
ATOM   1951 C CB  . ASN A 1 264 ? 24.193 93.923  -52.929 1.00 8.89   ? 320 ASN B CB  1 
ATOM   1952 C CG  . ASN A 1 264 ? 25.271 92.954  -52.426 1.00 13.47  ? 320 ASN B CG  1 
ATOM   1953 O OD1 . ASN A 1 264 ? 25.552 91.947  -53.066 1.00 16.34  ? 320 ASN B OD1 1 
ATOM   1954 N ND2 . ASN A 1 264 ? 25.862 93.251  -51.271 1.00 3.93   ? 320 ASN B ND2 1 
ATOM   1955 N N   . LEU A 1 265 ? 22.686 94.473  -55.321 1.00 9.44   ? 321 LEU B N   1 
ATOM   1956 C CA  . LEU A 1 265 ? 21.486 94.796  -56.085 1.00 7.17   ? 321 LEU B CA  1 
ATOM   1957 C C   . LEU A 1 265 ? 20.173 94.773  -55.282 1.00 14.10  ? 321 LEU B C   1 
ATOM   1958 O O   . LEU A 1 265 ? 19.101 94.639  -55.851 1.00 19.33  ? 321 LEU B O   1 
ATOM   1959 C CB  . LEU A 1 265 ? 21.419 93.983  -57.383 1.00 15.39  ? 321 LEU B CB  1 
ATOM   1960 C CG  . LEU A 1 265 ? 22.649 94.184  -58.288 1.00 16.31  ? 321 LEU B CG  1 
ATOM   1961 C CD1 . LEU A 1 265 ? 22.752 93.115  -59.388 1.00 10.06  ? 321 LEU B CD1 1 
ATOM   1962 C CD2 . LEU A 1 265 ? 22.644 95.571  -58.897 1.00 10.09  ? 321 LEU B CD2 1 
ATOM   1963 N N   . LEU A 1 266 ? 20.260 94.756  -53.962 1.00 19.16  ? 322 LEU B N   1 
ATOM   1964 C CA  . LEU A 1 266 ? 19.063 94.647  -53.117 1.00 11.10  ? 322 LEU B CA  1 
ATOM   1965 C C   . LEU A 1 266 ? 17.936 95.648  -53.401 1.00 8.35   ? 322 LEU B C   1 
ATOM   1966 O O   . LEU A 1 266 ? 18.178 96.820  -53.657 1.00 8.70   ? 322 LEU B O   1 
ATOM   1967 C CB  . LEU A 1 266 ? 19.455 94.732  -51.643 1.00 3.84   ? 322 LEU B CB  1 
ATOM   1968 C CG  . LEU A 1 266 ? 20.521 93.712  -51.246 1.00 3.15   ? 322 LEU B CG  1 
ATOM   1969 C CD1 . LEU A 1 266 ? 21.048 93.984  -49.862 1.00 2.00   ? 322 LEU B CD1 1 
ATOM   1970 C CD2 . LEU A 1 266 ? 19.911 92.323  -51.324 1.00 2.65   ? 322 LEU B CD2 1 
ATOM   1971 N N   . THR A 1 267 ? 16.704 95.153  -53.347 1.00 3.33   ? 323 THR B N   1 
ATOM   1972 C CA  . THR A 1 267 ? 15.507 95.971  -53.430 1.00 3.69   ? 323 THR B CA  1 
ATOM   1973 C C   . THR A 1 267 ? 14.613 95.708  -52.228 1.00 9.91   ? 323 THR B C   1 
ATOM   1974 O O   . THR A 1 267 ? 15.003 95.046  -51.271 1.00 21.52  ? 323 THR B O   1 
ATOM   1975 C CB  . THR A 1 267 ? 14.678 95.649  -54.663 1.00 9.39   ? 323 THR B CB  1 
ATOM   1976 O OG1 . THR A 1 267 ? 14.367 94.253  -54.643 1.00 12.13  ? 323 THR B OG1 1 
ATOM   1977 C CG2 . THR A 1 267 ? 15.442 95.999  -55.942 1.00 2.00   ? 323 THR B CG2 1 
ATOM   1978 N N   . GLY A 1 268 ? 13.405 96.247  -52.287 1.00 9.42   ? 324 GLY B N   1 
ATOM   1979 C CA  . GLY A 1 268 ? 12.484 96.177  -51.175 1.00 5.39   ? 324 GLY B CA  1 
ATOM   1980 C C   . GLY A 1 268 ? 12.762 97.316  -50.212 1.00 13.88  ? 324 GLY B C   1 
ATOM   1981 O O   . GLY A 1 268 ? 13.299 98.363  -50.570 1.00 25.39  ? 324 GLY B O   1 
ATOM   1982 N N   . THR A 1 269 ? 12.450 97.066  -48.960 1.00 11.30  ? 325 THR B N   1 
ATOM   1983 C CA  . THR A 1 269 ? 12.362 98.100  -47.948 1.00 12.62  ? 325 THR B CA  1 
ATOM   1984 C C   . THR A 1 269 ? 13.318 97.784  -46.775 1.00 15.04  ? 325 THR B C   1 
ATOM   1985 O O   . THR A 1 269 ? 13.733 96.625  -46.595 1.00 6.83   ? 325 THR B O   1 
ATOM   1986 C CB  . THR A 1 269 ? 10.884 98.124  -47.512 1.00 13.14  ? 325 THR B CB  1 
ATOM   1987 O OG1 . THR A 1 269 ? 10.210 99.226  -48.142 1.00 12.50  ? 325 THR B OG1 1 
ATOM   1988 C CG2 . THR A 1 269 ? 10.720 98.128  -46.029 1.00 2.00   ? 325 THR B CG2 1 
ATOM   1989 N N   . ILE A 1 270 ? 13.720 98.793  -46.005 1.00 15.62  ? 326 ILE B N   1 
ATOM   1990 C CA  . ILE A 1 270 ? 14.458 98.497  -44.778 1.00 10.28  ? 326 ILE B CA  1 
ATOM   1991 C C   . ILE A 1 270 ? 13.442 97.927  -43.783 1.00 17.00  ? 326 ILE B C   1 
ATOM   1992 O O   . ILE A 1 270 ? 12.475 98.602  -43.393 1.00 24.20  ? 326 ILE B O   1 
ATOM   1993 C CB  . ILE A 1 270 ? 15.152 99.738  -44.200 1.00 15.19  ? 326 ILE B CB  1 
ATOM   1994 C CG1 . ILE A 1 270 ? 16.155 100.334 -45.203 1.00 7.65   ? 326 ILE B CG1 1 
ATOM   1995 C CG2 . ILE A 1 270 ? 15.841 99.410  -42.870 1.00 9.17   ? 326 ILE B CG2 1 
ATOM   1996 C CD1 . ILE A 1 270 ? 16.961 101.506 -44.607 1.00 2.95   ? 326 ILE B CD1 1 
ATOM   1997 N N   . PRO A 1 271 ? 13.623 96.663  -43.393 1.00 10.91  ? 327 PRO B N   1 
ATOM   1998 C CA  . PRO A 1 271 ? 12.544 96.009  -42.644 1.00 10.82  ? 327 PRO B CA  1 
ATOM   1999 C C   . PRO A 1 271 ? 12.363 96.510  -41.204 1.00 6.73   ? 327 PRO B C   1 
ATOM   2000 O O   . PRO A 1 271 ? 13.323 96.792  -40.486 1.00 12.78  ? 327 PRO B O   1 
ATOM   2001 C CB  . PRO A 1 271 ? 12.948 94.532  -42.669 1.00 2.00   ? 327 PRO B CB  1 
ATOM   2002 C CG  . PRO A 1 271 ? 14.417 94.541  -42.839 1.00 10.34  ? 327 PRO B CG  1 
ATOM   2003 C CD  . PRO A 1 271 ? 14.760 95.760  -43.641 1.00 11.51  ? 327 PRO B CD  1 
ATOM   2004 N N   . ARG A 1 272 ? 11.105 96.588  -40.797 1.00 8.22   ? 328 ARG B N   1 
ATOM   2005 C CA  . ARG A 1 272 ? 10.708 97.066  -39.480 1.00 16.29  ? 328 ARG B CA  1 
ATOM   2006 C C   . ARG A 1 272 ? 11.266 96.205  -38.337 1.00 16.27  ? 328 ARG B C   1 
ATOM   2007 O O   . ARG A 1 272 ? 11.573 96.712  -37.247 1.00 24.58  ? 328 ARG B O   1 
ATOM   2008 C CB  . ARG A 1 272 ? 9.179  97.155  -39.423 1.00 11.54  ? 328 ARG B CB  1 
ATOM   2009 C CG  . ARG A 1 272 ? 8.603  98.159  -40.421 1.00 16.31  ? 328 ARG B CG  1 
ATOM   2010 C CD  . ARG A 1 272 ? 7.082  98.318  -40.303 1.00 28.58  ? 328 ARG B CD  1 
ATOM   2011 N NE  . ARG A 1 272 ? 6.363  97.151  -40.814 1.00 42.00  ? 328 ARG B NE  1 
ATOM   2012 C CZ  . ARG A 1 272 ? 5.881  96.168  -40.055 1.00 47.29  ? 328 ARG B CZ  1 
ATOM   2013 N NH1 . ARG A 1 272 ? 6.032  96.207  -38.732 1.00 51.44  ? 328 ARG B NH1 1 
ATOM   2014 N NH2 . ARG A 1 272 ? 5.247  95.145  -40.620 1.00 39.84  ? 328 ARG B NH2 1 
ATOM   2015 N N   . SER A 1 273 ? 11.428 94.912  -38.605 1.00 7.22   ? 329 SER B N   1 
ATOM   2016 C CA  . SER A 1 273 ? 11.897 93.966  -37.597 1.00 5.13   ? 329 SER B CA  1 
ATOM   2017 C C   . SER A 1 273 ? 13.242 94.377  -37.030 1.00 13.83  ? 329 SER B C   1 
ATOM   2018 O O   . SER A 1 273 ? 13.570 94.007  -35.904 1.00 18.33  ? 329 SER B O   1 
ATOM   2019 C CB  . SER A 1 273 ? 11.991 92.549  -38.171 1.00 9.43   ? 329 SER B CB  1 
ATOM   2020 O OG  . SER A 1 273 ? 12.992 92.466  -39.184 1.00 14.88  ? 329 SER B OG  1 
ATOM   2021 N N   . PHE A 1 274 ? 14.010 95.146  -37.797 1.00 2.00   ? 330 PHE B N   1 
ATOM   2022 C CA  . PHE A 1 274 ? 15.294 95.659  -37.319 1.00 9.78   ? 330 PHE B CA  1 
ATOM   2023 C C   . PHE A 1 274 ? 15.208 96.367  -35.963 1.00 7.06   ? 330 PHE B C   1 
ATOM   2024 O O   . PHE A 1 274 ? 16.185 96.378  -35.208 1.00 12.46  ? 330 PHE B O   1 
ATOM   2025 C CB  . PHE A 1 274 ? 15.951 96.593  -38.344 1.00 11.75  ? 330 PHE B CB  1 
ATOM   2026 C CG  . PHE A 1 274 ? 16.757 95.879  -39.388 1.00 11.22  ? 330 PHE B CG  1 
ATOM   2027 C CD1 . PHE A 1 274 ? 16.599 94.514  -39.599 1.00 16.58  ? 330 PHE B CD1 1 
ATOM   2028 C CD2 . PHE A 1 274 ? 17.683 96.568  -40.157 1.00 13.12  ? 330 PHE B CD2 1 
ATOM   2029 C CE1 . PHE A 1 274 ? 17.339 93.854  -40.581 1.00 15.39  ? 330 PHE B CE1 1 
ATOM   2030 C CE2 . PHE A 1 274 ? 18.429 95.916  -41.134 1.00 7.18   ? 330 PHE B CE2 1 
ATOM   2031 C CZ  . PHE A 1 274 ? 18.264 94.560  -41.338 1.00 8.74   ? 330 PHE B CZ  1 
ATOM   2032 N N   . GLY A 1 275 ? 14.053 96.943  -35.637 1.00 8.54   ? 331 GLY B N   1 
ATOM   2033 C CA  . GLY A 1 275 ? 13.861 97.524  -34.309 1.00 10.32  ? 331 GLY B CA  1 
ATOM   2034 C C   . GLY A 1 275 ? 14.143 96.571  -33.144 1.00 9.79   ? 331 GLY B C   1 
ATOM   2035 O O   . GLY A 1 275 ? 14.525 96.989  -32.061 1.00 12.34  ? 331 GLY B O   1 
ATOM   2036 N N   . LYS A 1 276 ? 13.958 95.278  -33.370 1.00 12.70  ? 332 LYS B N   1 
ATOM   2037 C CA  . LYS A 1 276 ? 14.166 94.279  -32.336 1.00 10.73  ? 332 LYS B CA  1 
ATOM   2038 C C   . LYS A 1 276 ? 15.652 93.980  -32.109 1.00 17.83  ? 332 LYS B C   1 
ATOM   2039 O O   . LYS A 1 276 ? 15.996 93.199  -31.224 1.00 20.75  ? 332 LYS B O   1 
ATOM   2040 C CB  . LYS A 1 276 ? 13.412 92.985  -32.663 1.00 2.69   ? 332 LYS B CB  1 
ATOM   2041 C CG  . LYS A 1 276 ? 11.917 93.156  -32.911 1.00 12.12  ? 332 LYS B CG  1 
ATOM   2042 C CD  . LYS A 1 276 ? 11.225 91.811  -33.024 1.00 20.13  ? 332 LYS B CD  1 
ATOM   2043 C CE  . LYS A 1 276 ? 11.740 91.027  -34.217 1.00 36.32  ? 332 LYS B CE  1 
ATOM   2044 N NZ  . LYS A 1 276 ? 11.677 89.549  -33.997 1.00 45.77  ? 332 LYS B NZ  1 
ATOM   2045 N N   . LEU A 1 277 ? 16.542 94.574  -32.900 1.00 15.93  ? 333 LEU B N   1 
ATOM   2046 C CA  . LEU A 1 277 ? 17.946 94.240  -32.727 1.00 10.71  ? 333 LEU B CA  1 
ATOM   2047 C C   . LEU A 1 277 ? 18.569 95.214  -31.751 1.00 14.79  ? 333 LEU B C   1 
ATOM   2048 O O   . LEU A 1 277 ? 18.955 96.317  -32.112 1.00 20.11  ? 333 LEU B O   1 
ATOM   2049 C CB  . LEU A 1 277 ? 18.668 94.343  -34.063 1.00 6.71   ? 333 LEU B CB  1 
ATOM   2050 C CG  . LEU A 1 277 ? 18.150 93.404  -35.156 1.00 14.66  ? 333 LEU B CG  1 
ATOM   2051 C CD1 . LEU A 1 277 ? 18.802 93.724  -36.504 1.00 4.85   ? 333 LEU B CD1 1 
ATOM   2052 C CD2 . LEU A 1 277 ? 18.363 91.933  -34.758 1.00 11.76  ? 333 LEU B CD2 1 
ATOM   2053 N N   . GLU A 1 278 ? 18.762 94.755  -30.525 1.00 19.05  ? 334 GLU B N   1 
ATOM   2054 C CA  . GLU A 1 278 ? 19.122 95.649  -29.439 1.00 14.10  ? 334 GLU B CA  1 
ATOM   2055 C C   . GLU A 1 278 ? 20.620 95.772  -29.344 1.00 16.65  ? 334 GLU B C   1 
ATOM   2056 O O   . GLU A 1 278 ? 21.140 96.637  -28.649 1.00 12.45  ? 334 GLU B O   1 
ATOM   2057 C CB  . GLU A 1 278 ? 18.525 95.136  -28.141 1.00 17.96  ? 334 GLU B CB  1 
ATOM   2058 C CG  . GLU A 1 278 ? 17.014 95.341  -28.097 1.00 38.89  ? 334 GLU B CG  1 
ATOM   2059 C CD  . GLU A 1 278 ? 16.376 94.918  -26.787 1.00 53.64  ? 334 GLU B CD  1 
ATOM   2060 O OE1 . GLU A 1 278 ? 16.754 93.844  -26.260 1.00 54.37  ? 334 GLU B OE1 1 
ATOM   2061 O OE2 . GLU A 1 278 ? 15.491 95.663  -26.295 1.00 58.44  ? 334 GLU B OE2 1 
ATOM   2062 N N   . ASN A 1 279 ? 21.318 94.891  -30.045 1.00 14.54  ? 335 ASN B N   1 
ATOM   2063 C CA  . ASN A 1 279 ? 22.760 94.978  -30.105 1.00 11.74  ? 335 ASN B CA  1 
ATOM   2064 C C   . ASN A 1 279 ? 23.334 95.599  -31.377 1.00 14.04  ? 335 ASN B C   1 
ATOM   2065 O O   . ASN A 1 279 ? 24.554 95.660  -31.533 1.00 17.92  ? 335 ASN B O   1 
ATOM   2066 C CB  . ASN A 1 279 ? 23.406 93.638  -29.769 1.00 13.04  ? 335 ASN B CB  1 
ATOM   2067 C CG  . ASN A 1 279 ? 23.182 93.242  -28.315 1.00 10.89  ? 335 ASN B CG  1 
ATOM   2068 O OD1 . ASN A 1 279 ? 23.732 93.858  -27.404 1.00 22.59  ? 335 ASN B OD1 1 
ATOM   2069 N ND2 . ASN A 1 279 ? 22.368 92.216  -28.094 1.00 3.97   ? 335 ASN B ND2 1 
ATOM   2070 N N   . LEU A 1 280 ? 22.482 96.066  -32.285 1.00 9.61   ? 336 LEU B N   1 
ATOM   2071 C CA  . LEU A 1 280 ? 23.007 96.528  -33.571 1.00 13.01  ? 336 LEU B CA  1 
ATOM   2072 C C   . LEU A 1 280 ? 23.811 97.805  -33.386 1.00 14.90  ? 336 LEU B C   1 
ATOM   2073 O O   . LEU A 1 280 ? 23.276 98.808  -32.917 1.00 21.56  ? 336 LEU B O   1 
ATOM   2074 C CB  . LEU A 1 280 ? 21.860 96.818  -34.530 1.00 10.10  ? 336 LEU B CB  1 
ATOM   2075 C CG  . LEU A 1 280 ? 22.283 97.199  -35.952 1.00 10.37  ? 336 LEU B CG  1 
ATOM   2076 C CD1 . LEU A 1 280 ? 23.038 96.054  -36.662 1.00 3.49   ? 336 LEU B CD1 1 
ATOM   2077 C CD2 . LEU A 1 280 ? 21.054 97.620  -36.747 1.00 3.31   ? 336 LEU B CD2 1 
ATOM   2078 N N   . GLN A 1 281 ? 25.101 97.774  -33.710 1.00 8.86   ? 337 GLN B N   1 
ATOM   2079 C CA  . GLN A 1 281 ? 25.875 99.013  -33.669 1.00 12.00  ? 337 GLN B CA  1 
ATOM   2080 C C   . GLN A 1 281 ? 26.164 99.655  -35.014 1.00 12.88  ? 337 GLN B C   1 
ATOM   2081 O O   . GLN A 1 281 ? 26.419 100.854 -35.103 1.00 24.48  ? 337 GLN B O   1 
ATOM   2082 C CB  . GLN A 1 281 ? 27.197 98.762  -32.953 1.00 11.88  ? 337 GLN B CB  1 
ATOM   2083 C CG  . GLN A 1 281 ? 27.020 98.377  -31.500 1.00 15.63  ? 337 GLN B CG  1 
ATOM   2084 C CD  . GLN A 1 281 ? 28.320 97.941  -30.883 1.00 19.26  ? 337 GLN B CD  1 
ATOM   2085 O OE1 . GLN A 1 281 ? 29.385 98.477  -31.210 1.00 16.51  ? 337 GLN B OE1 1 
ATOM   2086 N NE2 . GLN A 1 281 ? 28.251 96.947  -29.999 1.00 22.28  ? 337 GLN B NE2 1 
ATOM   2087 N N   . GLU A 1 282 ? 26.109 98.849  -36.060 1.00 9.86   ? 338 GLU B N   1 
ATOM   2088 C CA  . GLU A 1 282 ? 26.527 99.293  -37.386 1.00 14.80  ? 338 GLU B CA  1 
ATOM   2089 C C   . GLU A 1 282 ? 25.654 98.678  -38.476 1.00 11.02  ? 338 GLU B C   1 
ATOM   2090 O O   . GLU A 1 282 ? 25.578 97.436  -38.602 1.00 9.78   ? 338 GLU B O   1 
ATOM   2091 C CB  . GLU A 1 282 ? 28.000 98.945  -37.596 1.00 18.53  ? 338 GLU B CB  1 
ATOM   2092 C CG  . GLU A 1 282 ? 28.637 99.510  -38.844 1.00 32.42  ? 338 GLU B CG  1 
ATOM   2093 C CD  . GLU A 1 282 ? 30.128 99.741  -38.635 1.00 48.38  ? 338 GLU B CD  1 
ATOM   2094 O OE1 . GLU A 1 282 ? 30.550 99.785  -37.449 1.00 57.51  ? 338 GLU B OE1 1 
ATOM   2095 O OE2 . GLU A 1 282 ? 30.867 99.879  -39.639 1.00 40.57  ? 338 GLU B OE2 1 
ATOM   2096 N N   . LEU A 1 283 ? 24.999 99.548  -39.245 1.00 2.00   ? 339 LEU B N   1 
ATOM   2097 C CA  . LEU A 1 283 ? 24.190 99.133  -40.386 1.00 15.30  ? 339 LEU B CA  1 
ATOM   2098 C C   . LEU A 1 283 ? 24.686 99.824  -41.671 1.00 9.12   ? 339 LEU B C   1 
ATOM   2099 O O   . LEU A 1 283 ? 24.538 101.035 -41.825 1.00 5.71   ? 339 LEU B O   1 
ATOM   2100 C CB  . LEU A 1 283 ? 22.718 99.449  -40.109 1.00 2.00   ? 339 LEU B CB  1 
ATOM   2101 C CG  . LEU A 1 283 ? 21.670 99.204  -41.202 1.00 8.26   ? 339 LEU B CG  1 
ATOM   2102 C CD1 . LEU A 1 283 ? 21.651 97.766  -41.701 1.00 3.40   ? 339 LEU B CD1 1 
ATOM   2103 C CD2 . LEU A 1 283 ? 20.291 99.583  -40.681 1.00 5.28   ? 339 LEU B CD2 1 
ATOM   2104 N N   . GLN A 1 284 ? 25.292 99.057  -42.574 1.00 12.96  ? 340 GLN B N   1 
ATOM   2105 C CA  . GLN A 1 284 ? 25.687 99.582  -43.882 1.00 11.70  ? 340 GLN B CA  1 
ATOM   2106 C C   . GLN A 1 284 ? 24.921 98.918  -45.016 1.00 11.93  ? 340 GLN B C   1 
ATOM   2107 O O   . GLN A 1 284 ? 25.097 97.734  -45.295 1.00 16.24  ? 340 GLN B O   1 
ATOM   2108 C CB  . GLN A 1 284 ? 27.188 99.434  -44.085 1.00 10.36  ? 340 GLN B CB  1 
ATOM   2109 C CG  . GLN A 1 284 ? 27.944 100.056 -42.928 1.00 13.08  ? 340 GLN B CG  1 
ATOM   2110 C CD  . GLN A 1 284 ? 29.353 100.451 -43.269 1.00 22.65  ? 340 GLN B CD  1 
ATOM   2111 O OE1 . GLN A 1 284 ? 29.943 101.278 -42.583 1.00 38.87  ? 340 GLN B OE1 1 
ATOM   2112 N NE2 . GLN A 1 284 ? 29.910 99.858  -44.318 1.00 22.62  ? 340 GLN B NE2 1 
ATOM   2113 N N   . LEU A 1 285 ? 24.000 99.688  -45.584 1.00 14.30  ? 341 LEU B N   1 
ATOM   2114 C CA  . LEU A 1 285 ? 23.244 99.365  -46.795 1.00 4.55   ? 341 LEU B CA  1 
ATOM   2115 C C   . LEU A 1 285 ? 23.668 100.132 -48.047 1.00 6.44   ? 341 LEU B C   1 
ATOM   2116 O O   . LEU A 1 285 ? 22.965 100.118 -49.046 1.00 13.25  ? 341 LEU B O   1 
ATOM   2117 C CB  . LEU A 1 285 ? 21.747 99.490  -46.536 1.00 2.00   ? 341 LEU B CB  1 
ATOM   2118 C CG  . LEU A 1 285 ? 21.336 98.639  -45.321 1.00 2.93   ? 341 LEU B CG  1 
ATOM   2119 C CD1 . LEU A 1 285 ? 19.842 98.763  -45.034 1.00 2.00   ? 341 LEU B CD1 1 
ATOM   2120 C CD2 . LEU A 1 285 ? 21.730 97.170  -45.512 1.00 2.00   ? 341 LEU B CD2 1 
ATOM   2121 N N   . SER A 1 286 ? 24.773 100.864 -47.978 1.00 11.01  ? 342 SER B N   1 
ATOM   2122 C CA  . SER A 1 286 ? 25.185 101.751 -49.078 1.00 11.24  ? 342 SER B CA  1 
ATOM   2123 C C   . SER A 1 286 ? 25.234 101.114 -50.479 1.00 12.36  ? 342 SER B C   1 
ATOM   2124 O O   . SER A 1 286 ? 25.610 99.955  -50.632 1.00 8.55   ? 342 SER B O   1 
ATOM   2125 C CB  . SER A 1 286 ? 26.560 102.321 -48.765 1.00 5.06   ? 342 SER B CB  1 
ATOM   2126 O OG  . SER A 1 286 ? 26.543 102.965 -47.512 1.00 7.35   ? 342 SER B OG  1 
ATOM   2127 N N   . VAL A 1 287 ? 24.867 101.890 -51.499 1.00 15.09  ? 343 VAL B N   1 
ATOM   2128 C CA  . VAL A 1 287 ? 24.897 101.439 -52.905 1.00 2.35   ? 343 VAL B CA  1 
ATOM   2129 C C   . VAL A 1 287 ? 24.047 100.196 -53.177 1.00 2.00   ? 343 VAL B C   1 
ATOM   2130 O O   . VAL A 1 287 ? 24.551 99.103  -53.370 1.00 13.38  ? 343 VAL B O   1 
ATOM   2131 C CB  . VAL A 1 287 ? 26.322 101.219 -53.431 1.00 8.47   ? 343 VAL B CB  1 
ATOM   2132 C CG1 . VAL A 1 287 ? 26.330 101.285 -54.971 1.00 2.00   ? 343 VAL B CG1 1 
ATOM   2133 C CG2 . VAL A 1 287 ? 27.287 102.267 -52.832 1.00 2.00   ? 343 VAL B CG2 1 
ATOM   2134 N N   . ASN A 1 288 ? 22.742 100.387 -53.124 1.00 3.31   ? 344 ASN B N   1 
ATOM   2135 C CA  . ASN A 1 288 ? 21.769 99.379  -53.465 1.00 3.77   ? 344 ASN B CA  1 
ATOM   2136 C C   . ASN A 1 288 ? 20.559 100.069 -54.089 1.00 10.91  ? 344 ASN B C   1 
ATOM   2137 O O   . ASN A 1 288 ? 20.632 101.208 -54.521 1.00 15.38  ? 344 ASN B O   1 
ATOM   2138 C CB  . ASN A 1 288 ? 21.325 98.591  -52.236 1.00 9.68   ? 344 ASN B CB  1 
ATOM   2139 C CG  . ASN A 1 288 ? 22.311 97.509  -51.838 1.00 15.12  ? 344 ASN B CG  1 
ATOM   2140 O OD1 . ASN A 1 288 ? 22.354 96.439  -52.450 1.00 10.44  ? 344 ASN B OD1 1 
ATOM   2141 N ND2 . ASN A 1 288 ? 23.091 97.771  -50.787 1.00 6.25   ? 344 ASN B ND2 1 
ATOM   2142 N N   . GLN A 1 289 ? 19.495 99.307  -54.252 1.00 10.30  ? 345 GLN B N   1 
ATOM   2143 C CA  . GLN A 1 289 ? 18.212 99.778  -54.754 1.00 14.24  ? 345 GLN B CA  1 
ATOM   2144 C C   . GLN A 1 289 ? 17.076 99.872  -53.754 1.00 15.63  ? 345 GLN B C   1 
ATOM   2145 O O   . GLN A 1 289 ? 15.916 99.693  -54.147 1.00 9.11   ? 345 GLN B O   1 
ATOM   2146 C CB  . GLN A 1 289 ? 17.806 99.092  -56.044 1.00 10.40  ? 345 GLN B CB  1 
ATOM   2147 C CG  . GLN A 1 289 ? 18.655 99.543  -57.209 1.00 15.54  ? 345 GLN B CG  1 
ATOM   2148 C CD  . GLN A 1 289 ? 18.721 98.480  -58.277 1.00 31.20  ? 345 GLN B CD  1 
ATOM   2149 O OE1 . GLN A 1 289 ? 17.687 98.018  -58.768 1.00 33.99  ? 345 GLN B OE1 1 
ATOM   2150 N NE2 . GLN A 1 289 ? 19.938 98.054  -58.620 1.00 38.28  ? 345 GLN B NE2 1 
ATOM   2151 N N   . ILE A 1 290 ? 17.415 99.911  -52.469 1.00 12.07  ? 346 ILE B N   1 
ATOM   2152 C CA  . ILE A 1 290 ? 16.410 99.927  -51.412 1.00 12.87  ? 346 ILE B CA  1 
ATOM   2153 C C   . ILE A 1 290 ? 15.396 101.089 -51.505 1.00 14.12  ? 346 ILE B C   1 
ATOM   2154 O O   . ILE A 1 290 ? 15.761 102.275 -51.531 1.00 7.86   ? 346 ILE B O   1 
ATOM   2155 C CB  . ILE A 1 290 ? 17.090 99.907  -50.032 1.00 6.20   ? 346 ILE B CB  1 
ATOM   2156 C CG1 . ILE A 1 290 ? 17.929 98.638  -49.905 1.00 9.80   ? 346 ILE B CG1 1 
ATOM   2157 C CG2 . ILE A 1 290 ? 16.046 99.975  -48.920 1.00 4.07   ? 346 ILE B CG2 1 
ATOM   2158 C CD1 . ILE A 1 290 ? 18.730 98.544  -48.620 1.00 19.69  ? 346 ILE B CD1 1 
ATOM   2159 N N   . SER A 1 291 ? 14.117 100.733 -51.569 1.00 10.96  ? 347 SER B N   1 
ATOM   2160 C CA  . SER A 1 291 ? 13.040 101.724 -51.628 1.00 14.73  ? 347 SER B CA  1 
ATOM   2161 C C   . SER A 1 291 ? 12.407 101.890 -50.253 1.00 16.22  ? 347 SER B C   1 
ATOM   2162 O O   . SER A 1 291 ? 12.939 101.399 -49.258 1.00 23.21  ? 347 SER B O   1 
ATOM   2163 C CB  . SER A 1 291 ? 11.993 101.368 -52.699 1.00 2.00   ? 347 SER B CB  1 
ATOM   2164 O OG  . SER A 1 291 ? 11.719 99.977  -52.692 1.00 19.00  ? 347 SER B OG  1 
ATOM   2165 N N   . GLY A 1 292 ? 11.288 102.604 -50.204 1.00 11.44  ? 348 GLY B N   1 
ATOM   2166 C CA  . GLY A 1 292 ? 10.552 102.790 -48.969 1.00 5.37   ? 348 GLY B CA  1 
ATOM   2167 C C   . GLY A 1 292 ? 11.099 103.954 -48.164 1.00 12.01  ? 348 GLY B C   1 
ATOM   2168 O O   . GLY A 1 292 ? 11.927 104.722 -48.656 1.00 20.54  ? 348 GLY B O   1 
ATOM   2169 N N   . THR A 1 293 ? 10.646 104.073 -46.918 1.00 5.11   ? 349 THR B N   1 
ATOM   2170 C CA  . THR A 1 293 ? 11.139 105.096 -45.999 1.00 8.09   ? 349 THR B CA  1 
ATOM   2171 C C   . THR A 1 293 ? 11.884 104.454 -44.823 1.00 10.54  ? 349 THR B C   1 
ATOM   2172 O O   . THR A 1 293 ? 11.663 103.292 -44.507 1.00 17.76  ? 349 THR B O   1 
ATOM   2173 C CB  . THR A 1 293 ? 9.973  105.892 -45.403 1.00 6.16   ? 349 THR B CB  1 
ATOM   2174 O OG1 . THR A 1 293 ? 9.285  105.064 -44.462 1.00 15.04  ? 349 THR B OG1 1 
ATOM   2175 C CG2 . THR A 1 293 ? 8.997  106.339 -46.494 1.00 2.03   ? 349 THR B CG2 1 
ATOM   2176 N N   . ILE A 1 294 ? 12.755 105.216 -44.172 1.00 11.52  ? 350 ILE B N   1 
ATOM   2177 C CA  . ILE A 1 294 ? 13.450 104.734 -42.977 1.00 14.25  ? 350 ILE B CA  1 
ATOM   2178 C C   . ILE A 1 294 ? 12.423 104.433 -41.891 1.00 11.06  ? 350 ILE B C   1 
ATOM   2179 O O   . ILE A 1 294 ? 11.729 105.330 -41.423 1.00 14.18  ? 350 ILE B O   1 
ATOM   2180 C CB  . ILE A 1 294 ? 14.432 105.791 -42.445 1.00 12.54  ? 350 ILE B CB  1 
ATOM   2181 C CG1 . ILE A 1 294 ? 15.315 106.307 -43.590 1.00 2.78   ? 350 ILE B CG1 1 
ATOM   2182 C CG2 . ILE A 1 294 ? 15.257 105.225 -41.290 1.00 7.76   ? 350 ILE B CG2 1 
ATOM   2183 C CD1 . ILE A 1 294 ? 15.986 107.606 -43.309 1.00 2.00   ? 350 ILE B CD1 1 
ATOM   2184 N N   . PRO A 1 295 ? 12.290 103.154 -41.516 1.00 6.32   ? 351 PRO B N   1 
ATOM   2185 C CA  . PRO A 1 295 ? 11.209 102.853 -40.582 1.00 8.19   ? 351 PRO B CA  1 
ATOM   2186 C C   . PRO A 1 295 ? 11.498 103.418 -39.194 1.00 9.87   ? 351 PRO B C   1 
ATOM   2187 O O   . PRO A 1 295 ? 12.618 103.298 -38.719 1.00 12.85  ? 351 PRO B O   1 
ATOM   2188 C CB  . PRO A 1 295 ? 11.178 101.321 -40.570 1.00 3.65   ? 351 PRO B CB  1 
ATOM   2189 C CG  . PRO A 1 295 ? 12.533 100.901 -41.059 1.00 4.39   ? 351 PRO B CG  1 
ATOM   2190 C CD  . PRO A 1 295 ? 12.933 101.936 -42.039 1.00 2.00   ? 351 PRO B CD  1 
ATOM   2191 N N   . GLU A 1 296 ? 10.503 104.032 -38.564 1.00 12.93  ? 352 GLU B N   1 
ATOM   2192 C CA  . GLU A 1 296 ? 10.665 104.554 -37.206 1.00 21.55  ? 352 GLU B CA  1 
ATOM   2193 C C   . GLU A 1 296 ? 11.157 103.526 -36.191 1.00 17.62  ? 352 GLU B C   1 
ATOM   2194 O O   . GLU A 1 296 ? 11.904 103.876 -35.281 1.00 11.24  ? 352 GLU B O   1 
ATOM   2195 C CB  . GLU A 1 296 ? 9.395  105.242 -36.708 1.00 27.17  ? 352 GLU B CB  1 
ATOM   2196 C CG  . GLU A 1 296 ? 9.191  106.624 -37.326 1.00 42.22  ? 352 GLU B CG  1 
ATOM   2197 C CD  . GLU A 1 296 ? 8.775  107.657 -36.305 1.00 56.30  ? 352 GLU B CD  1 
ATOM   2198 O OE1 . GLU A 1 296 ? 9.526  108.649 -36.117 1.00 59.99  ? 352 GLU B OE1 1 
ATOM   2199 O OE2 . GLU A 1 296 ? 7.698  107.469 -35.692 1.00 59.43  ? 352 GLU B OE2 1 
ATOM   2200 N N   . GLU A 1 297 ? 10.792 102.258 -36.358 1.00 14.58  ? 353 GLU B N   1 
ATOM   2201 C CA  . GLU A 1 297 ? 11.274 101.258 -35.412 1.00 14.71  ? 353 GLU B CA  1 
ATOM   2202 C C   . GLU A 1 297 ? 12.796 101.100 -35.378 1.00 8.81   ? 353 GLU B C   1 
ATOM   2203 O O   . GLU A 1 297 ? 13.335 100.615 -34.388 1.00 17.17  ? 353 GLU B O   1 
ATOM   2204 C CB  . GLU A 1 297 ? 10.545 99.910  -35.529 1.00 15.16  ? 353 GLU B CB  1 
ATOM   2205 C CG  . GLU A 1 297 ? 10.032 99.583  -36.890 1.00 30.19  ? 353 GLU B CG  1 
ATOM   2206 C CD  . GLU A 1 297 ? 8.722  100.262 -37.192 1.00 30.68  ? 353 GLU B CD  1 
ATOM   2207 O OE1 . GLU A 1 297 ? 7.700  99.878  -36.584 1.00 27.44  ? 353 GLU B OE1 1 
ATOM   2208 O OE2 . GLU A 1 297 ? 8.724  101.180 -38.040 1.00 34.73  ? 353 GLU B OE2 1 
ATOM   2209 N N   . LEU A 1 298 ? 13.487 101.548 -36.427 1.00 11.66  ? 354 LEU B N   1 
ATOM   2210 C CA  . LEU A 1 298 ? 14.963 101.543 -36.462 1.00 10.88  ? 354 LEU B CA  1 
ATOM   2211 C C   . LEU A 1 298 ? 15.513 102.458 -35.378 1.00 16.12  ? 354 LEU B C   1 
ATOM   2212 O O   . LEU A 1 298 ? 16.652 102.293 -34.930 1.00 12.86  ? 354 LEU B O   1 
ATOM   2213 C CB  . LEU A 1 298 ? 15.500 102.046 -37.811 1.00 7.72   ? 354 LEU B CB  1 
ATOM   2214 C CG  . LEU A 1 298 ? 16.665 101.326 -38.513 1.00 14.68  ? 354 LEU B CG  1 
ATOM   2215 C CD1 . LEU A 1 298 ? 17.516 102.281 -39.321 1.00 7.54   ? 354 LEU B CD1 1 
ATOM   2216 C CD2 . LEU A 1 298 ? 17.541 100.550 -37.571 1.00 21.53  ? 354 LEU B CD2 1 
ATOM   2217 N N   . THR A 1 299 ? 14.724 103.455 -34.984 1.00 10.43  ? 355 THR B N   1 
ATOM   2218 C CA  . THR A 1 299 ? 15.157 104.336 -33.914 1.00 17.38  ? 355 THR B CA  1 
ATOM   2219 C C   . THR A 1 299 ? 15.110 103.646 -32.557 1.00 11.21  ? 355 THR B C   1 
ATOM   2220 O O   . THR A 1 299 ? 15.561 104.209 -31.579 1.00 5.66   ? 355 THR B O   1 
ATOM   2221 C CB  . THR A 1 299 ? 14.329 105.612 -33.829 1.00 21.22  ? 355 THR B CB  1 
ATOM   2222 O OG1 . THR A 1 299 ? 13.055 105.309 -33.246 1.00 17.80  ? 355 THR B OG1 1 
ATOM   2223 C CG2 . THR A 1 299 ? 14.183 106.255 -35.217 1.00 12.82  ? 355 THR B CG2 1 
ATOM   2224 N N   . ASN A 1 300 ? 14.569 102.433 -32.498 1.00 8.26   ? 356 ASN B N   1 
ATOM   2225 C CA  . ASN A 1 300 ? 14.645 101.634 -31.278 1.00 12.18  ? 356 ASN B CA  1 
ATOM   2226 C C   . ASN A 1 300 ? 16.023 100.981 -31.066 1.00 17.50  ? 356 ASN B C   1 
ATOM   2227 O O   . ASN A 1 300 ? 16.267 100.396 -30.005 1.00 18.72  ? 356 ASN B O   1 
ATOM   2228 C CB  . ASN A 1 300 ? 13.570 100.542 -31.272 1.00 20.35  ? 356 ASN B CB  1 
ATOM   2229 C CG  . ASN A 1 300 ? 12.698 100.587 -30.045 1.00 29.30  ? 356 ASN B CG  1 
ATOM   2230 O OD1 . ASN A 1 300 ? 12.246 101.656 -29.628 1.00 31.30  ? 356 ASN B OD1 1 
ATOM   2231 N ND2 . ASN A 1 300 ? 12.451 99.417  -29.453 1.00 36.86  ? 356 ASN B ND2 1 
ATOM   2232 N N   . CYS A 1 301 ? 16.936 101.088 -32.040 1.00 13.61  ? 357 CYS B N   1 
ATOM   2233 C CA  . CYS A 1 301 ? 18.204 100.383 -31.894 1.00 13.09  ? 357 CYS B CA  1 
ATOM   2234 C C   . CYS A 1 301 ? 19.157 101.306 -31.150 1.00 20.68  ? 357 CYS B C   1 
ATOM   2235 O O   . CYS A 1 301 ? 19.890 102.106 -31.741 1.00 11.70  ? 357 CYS B O   1 
ATOM   2236 C CB  . CYS A 1 301 ? 18.791 100.071 -33.270 1.00 12.44  ? 357 CYS B CB  1 
ATOM   2237 S SG  . CYS A 1 301 ? 17.812 98.963  -34.348 1.00 20.34  ? 357 CYS B SG  1 
ATOM   2238 N N   . THR A 1 302 ? 19.249 101.054 -29.853 1.00 22.34  ? 358 THR B N   1 
ATOM   2239 C CA  . THR A 1 302 ? 19.748 102.028 -28.895 1.00 16.89  ? 358 THR B CA  1 
ATOM   2240 C C   . THR A 1 302 ? 21.242 102.217 -29.077 1.00 13.49  ? 358 THR B C   1 
ATOM   2241 O O   . THR A 1 302 ? 21.799 103.272 -28.774 1.00 17.96  ? 358 THR B O   1 
ATOM   2242 C CB  . THR A 1 302 ? 19.395 101.557 -27.449 1.00 22.73  ? 358 THR B CB  1 
ATOM   2243 O OG1 . THR A 1 302 ? 18.122 102.100 -27.069 1.00 26.70  ? 358 THR B OG1 1 
ATOM   2244 C CG2 . THR A 1 302 ? 20.435 101.977 -26.441 1.00 16.16  ? 358 THR B CG2 1 
ATOM   2245 N N   . LYS A 1 303 ? 21.882 101.184 -29.609 1.00 16.20  ? 359 LYS B N   1 
ATOM   2246 C CA  . LYS A 1 303 ? 23.330 101.155 -29.669 1.00 11.69  ? 359 LYS B CA  1 
ATOM   2247 C C   . LYS A 1 303 ? 23.947 101.580 -30.997 1.00 7.65   ? 359 LYS B C   1 
ATOM   2248 O O   . LYS A 1 303 ? 25.168 101.540 -31.130 1.00 13.44  ? 359 LYS B O   1 
ATOM   2249 C CB  . LYS A 1 303 ? 23.849 99.782  -29.241 1.00 15.55  ? 359 LYS B CB  1 
ATOM   2250 C CG  . LYS A 1 303 ? 23.408 99.400  -27.838 1.00 22.21  ? 359 LYS B CG  1 
ATOM   2251 C CD  . LYS A 1 303 ? 24.430 98.519  -27.139 1.00 28.02  ? 359 LYS B CD  1 
ATOM   2252 C CE  . LYS A 1 303 ? 24.108 97.040  -27.294 1.00 35.15  ? 359 LYS B CE  1 
ATOM   2253 N NZ  . LYS A 1 303 ? 25.094 96.180  -26.564 1.00 35.86  ? 359 LYS B NZ  1 
ATOM   2254 N N   . LEU A 1 304 ? 23.134 101.997 -31.967 1.00 4.12   ? 360 LEU B N   1 
ATOM   2255 C CA  . LEU A 1 304 ? 23.673 102.310 -33.287 1.00 2.19   ? 360 LEU B CA  1 
ATOM   2256 C C   . LEU A 1 304 ? 24.692 103.428 -33.195 1.00 8.72   ? 360 LEU B C   1 
ATOM   2257 O O   . LEU A 1 304 ? 24.370 104.536 -32.759 1.00 15.05  ? 360 LEU B O   1 
ATOM   2258 C CB  . LEU A 1 304 ? 22.532 102.794 -34.165 1.00 7.38   ? 360 LEU B CB  1 
ATOM   2259 C CG  . LEU A 1 304 ? 22.483 102.399 -35.634 1.00 11.37  ? 360 LEU B CG  1 
ATOM   2260 C CD1 . LEU A 1 304 ? 22.776 100.912 -35.808 1.00 6.76   ? 360 LEU B CD1 1 
ATOM   2261 C CD2 . LEU A 1 304 ? 21.098 102.730 -36.148 1.00 11.85  ? 360 LEU B CD2 1 
ATOM   2262 N N   . THR A 1 305 ? 25.934 103.135 -33.572 1.00 8.29   ? 361 THR B N   1 
ATOM   2263 C CA  . THR A 1 305 ? 26.910 104.182 -33.875 1.00 7.89   ? 361 THR B CA  1 
ATOM   2264 C C   . THR A 1 305 ? 26.953 104.616 -35.352 1.00 6.51   ? 361 THR B C   1 
ATOM   2265 O O   . THR A 1 305 ? 27.019 105.808 -35.645 1.00 12.69  ? 361 THR B O   1 
ATOM   2266 C CB  . THR A 1 305 ? 28.316 103.847 -33.332 1.00 11.56  ? 361 THR B CB  1 
ATOM   2267 O OG1 . THR A 1 305 ? 28.872 102.752 -34.068 1.00 20.29  ? 361 THR B OG1 1 
ATOM   2268 C CG2 . THR A 1 305 ? 28.221 103.454 -31.869 1.00 4.06   ? 361 THR B CG2 1 
ATOM   2269 N N   . HIS A 1 306 ? 26.914 103.649 -36.273 1.00 6.56   ? 362 HIS B N   1 
ATOM   2270 C CA  . HIS A 1 306 ? 27.059 103.930 -37.723 1.00 9.21   ? 362 HIS B CA  1 
ATOM   2271 C C   . HIS A 1 306 ? 25.835 103.539 -38.547 1.00 12.43  ? 362 HIS B C   1 
ATOM   2272 O O   . HIS A 1 306 ? 25.475 102.355 -38.623 1.00 7.52   ? 362 HIS B O   1 
ATOM   2273 C CB  . HIS A 1 306 ? 28.265 103.205 -38.332 1.00 3.08   ? 362 HIS B CB  1 
ATOM   2274 C CG  . HIS A 1 306 ? 29.591 103.660 -37.803 1.00 18.43  ? 362 HIS B CG  1 
ATOM   2275 N ND1 . HIS A 1 306 ? 29.942 103.556 -36.474 1.00 28.66  ? 362 HIS B ND1 1 
ATOM   2276 C CD2 . HIS A 1 306 ? 30.659 104.204 -38.430 1.00 29.52  ? 362 HIS B CD2 1 
ATOM   2277 C CE1 . HIS A 1 306 ? 31.165 104.023 -36.302 1.00 24.67  ? 362 HIS B CE1 1 
ATOM   2278 N NE2 . HIS A 1 306 ? 31.623 104.420 -37.475 1.00 31.09  ? 362 HIS B NE2 1 
ATOM   2279 N N   . LEU A 1 307 ? 25.200 104.532 -39.169 1.00 12.38  ? 363 LEU B N   1 
ATOM   2280 C CA  . LEU A 1 307 ? 24.110 104.260 -40.104 1.00 9.37   ? 363 LEU B CA  1 
ATOM   2281 C C   . LEU A 1 307 ? 24.415 104.798 -41.514 1.00 11.63  ? 363 LEU B C   1 
ATOM   2282 O O   . LEU A 1 307 ? 24.362 106.019 -41.759 1.00 9.76   ? 363 LEU B O   1 
ATOM   2283 C CB  . LEU A 1 307 ? 22.808 104.859 -39.576 1.00 2.12   ? 363 LEU B CB  1 
ATOM   2284 C CG  . LEU A 1 307 ? 21.578 104.591 -40.441 1.00 11.11  ? 363 LEU B CG  1 
ATOM   2285 C CD1 . LEU A 1 307 ? 21.276 103.096 -40.475 1.00 6.74   ? 363 LEU B CD1 1 
ATOM   2286 C CD2 . LEU A 1 307 ? 20.373 105.385 -39.943 1.00 4.27   ? 363 LEU B CD2 1 
ATOM   2287 N N   . GLU A 1 308 ? 24.708 103.886 -42.446 1.00 10.30  ? 364 GLU B N   1 
ATOM   2288 C CA  . GLU A 1 308 ? 24.971 104.295 -43.824 1.00 10.31  ? 364 GLU B CA  1 
ATOM   2289 C C   . GLU A 1 308 ? 24.013 103.654 -44.801 1.00 15.97  ? 364 GLU B C   1 
ATOM   2290 O O   . GLU A 1 308 ? 24.120 102.460 -45.116 1.00 16.10  ? 364 GLU B O   1 
ATOM   2291 C CB  . GLU A 1 308 ? 26.397 103.955 -44.212 1.00 11.46  ? 364 GLU B CB  1 
ATOM   2292 C CG  . GLU A 1 308 ? 27.391 104.980 -43.705 1.00 22.87  ? 364 GLU B CG  1 
ATOM   2293 C CD  . GLU A 1 308 ? 28.394 104.367 -42.789 1.00 33.87  ? 364 GLU B CD  1 
ATOM   2294 O OE1 . GLU A 1 308 ? 29.404 103.852 -43.315 1.00 41.87  ? 364 GLU B OE1 1 
ATOM   2295 O OE2 . GLU A 1 308 ? 28.159 104.383 -41.558 1.00 32.88  ? 364 GLU B OE2 1 
ATOM   2296 N N   . ILE A 1 309 ? 23.057 104.475 -45.232 1.00 6.78   ? 365 ILE B N   1 
ATOM   2297 C CA  . ILE A 1 309 ? 22.043 104.139 -46.214 1.00 4.67   ? 365 ILE B CA  1 
ATOM   2298 C C   . ILE A 1 309 ? 22.155 104.842 -47.557 1.00 10.06  ? 365 ILE B C   1 
ATOM   2299 O O   . ILE A 1 309 ? 21.176 104.923 -48.298 1.00 13.52  ? 365 ILE B O   1 
ATOM   2300 C CB  . ILE A 1 309 ? 20.623 104.181 -45.650 1.00 10.30  ? 365 ILE B CB  1 
ATOM   2301 C CG1 . ILE A 1 309 ? 20.301 105.566 -45.091 1.00 3.59   ? 365 ILE B CG1 1 
ATOM   2302 C CG2 . ILE A 1 309 ? 20.438 103.054 -44.627 1.00 2.00   ? 365 ILE B CG2 1 
ATOM   2303 C CD1 . ILE A 1 309 ? 18.891 105.665 -44.557 1.00 2.00   ? 365 ILE B CD1 1 
ATOM   2304 N N   . ASP A 1 310 ? 23.292 105.475 -47.796 1.00 6.81   ? 366 ASP B N   1 
ATOM   2305 C CA  . ASP A 1 310 ? 23.486 106.302 -48.986 1.00 10.09  ? 366 ASP B CA  1 
ATOM   2306 C C   . ASP A 1 310 ? 23.368 105.512 -50.321 1.00 13.27  ? 366 ASP B C   1 
ATOM   2307 O O   . ASP A 1 310 ? 23.410 104.283 -50.332 1.00 2.00   ? 366 ASP B O   1 
ATOM   2308 C CB  . ASP A 1 310 ? 24.843 107.007 -48.889 1.00 5.40   ? 366 ASP B CB  1 
ATOM   2309 C CG  . ASP A 1 310 ? 26.004 106.021 -48.820 1.00 16.05  ? 366 ASP B CG  1 
ATOM   2310 O OD1 . ASP A 1 310 ? 26.239 105.427 -47.732 1.00 17.78  ? 366 ASP B OD1 1 
ATOM   2311 O OD2 . ASP A 1 310 ? 26.675 105.832 -49.863 1.00 22.22  ? 366 ASP B OD2 1 
ATOM   2312 N N   . ASN A 1 311 ? 23.147 106.228 -51.425 1.00 7.18   ? 367 ASN B N   1 
ATOM   2313 C CA  . ASN A 1 311 ? 23.047 105.620 -52.759 1.00 2.00   ? 367 ASN B CA  1 
ATOM   2314 C C   . ASN A 1 311 ? 21.996 104.512 -52.864 1.00 4.70   ? 367 ASN B C   1 
ATOM   2315 O O   . ASN A 1 311 ? 22.310 103.347 -53.140 1.00 2.00   ? 367 ASN B O   1 
ATOM   2316 C CB  . ASN A 1 311 ? 24.419 105.117 -53.237 1.00 3.47   ? 367 ASN B CB  1 
ATOM   2317 C CG  . ASN A 1 311 ? 25.367 106.256 -53.589 1.00 8.14   ? 367 ASN B CG  1 
ATOM   2318 O OD1 . ASN A 1 311 ? 25.288 106.818 -54.674 1.00 18.69  ? 367 ASN B OD1 1 
ATOM   2319 N ND2 . ASN A 1 311 ? 26.256 106.610 -52.663 1.00 2.87   ? 367 ASN B ND2 1 
ATOM   2320 N N   . ASN A 1 312 ? 20.745 104.907 -52.654 1.00 2.74   ? 368 ASN B N   1 
ATOM   2321 C CA  . ASN A 1 312 ? 19.591 104.008 -52.707 1.00 3.83   ? 368 ASN B CA  1 
ATOM   2322 C C   . ASN A 1 312 ? 18.361 104.741 -53.264 1.00 10.18  ? 368 ASN B C   1 
ATOM   2323 O O   . ASN A 1 312 ? 18.469 105.806 -53.859 1.00 6.76   ? 368 ASN B O   1 
ATOM   2324 C CB  . ASN A 1 312 ? 19.276 103.468 -51.313 1.00 8.52   ? 368 ASN B CB  1 
ATOM   2325 C CG  . ASN A 1 312 ? 20.243 102.369 -50.870 1.00 16.59  ? 368 ASN B CG  1 
ATOM   2326 O OD1 . ASN A 1 312 ? 20.131 101.228 -51.315 1.00 12.88  ? 368 ASN B OD1 1 
ATOM   2327 N ND2 . ASN A 1 312 ? 21.185 102.707 -49.967 1.00 10.47  ? 368 ASN B ND2 1 
ATOM   2328 N N   . LEU A 1 313 ? 17.202 104.120 -53.140 1.00 14.27  ? 369 LEU B N   1 
ATOM   2329 C CA  . LEU A 1 313 ? 15.932 104.733 -53.529 1.00 14.09  ? 369 LEU B CA  1 
ATOM   2330 C C   . LEU A 1 313 ? 15.047 105.259 -52.381 1.00 15.60  ? 369 LEU B C   1 
ATOM   2331 O O   . LEU A 1 313 ? 13.845 105.419 -52.573 1.00 8.20   ? 369 LEU B O   1 
ATOM   2332 C CB  . LEU A 1 313 ? 15.170 103.847 -54.526 1.00 17.90  ? 369 LEU B CB  1 
ATOM   2333 C CG  . LEU A 1 313 ? 15.984 103.454 -55.782 1.00 21.33  ? 369 LEU B CG  1 
ATOM   2334 C CD1 . LEU A 1 313 ? 15.252 102.419 -56.653 1.00 10.97  ? 369 LEU B CD1 1 
ATOM   2335 C CD2 . LEU A 1 313 ? 16.386 104.667 -56.615 1.00 2.00   ? 369 LEU B CD2 1 
ATOM   2336 N N   . ILE A 1 314 ? 15.583 105.376 -51.163 1.00 22.18  ? 370 ILE B N   1 
ATOM   2337 C CA  . ILE A 1 314 ? 14.767 105.797 -50.008 1.00 11.77  ? 370 ILE B CA  1 
ATOM   2338 C C   . ILE A 1 314 ? 14.018 107.131 -50.198 1.00 10.84  ? 370 ILE B C   1 
ATOM   2339 O O   . ILE A 1 314 ? 14.574 108.107 -50.700 1.00 14.09  ? 370 ILE B O   1 
ATOM   2340 C CB  . ILE A 1 314 ? 15.586 105.918 -48.722 1.00 13.63  ? 370 ILE B CB  1 
ATOM   2341 C CG1 . ILE A 1 314 ? 16.633 104.811 -48.604 1.00 13.98  ? 370 ILE B CG1 1 
ATOM   2342 C CG2 . ILE A 1 314 ? 14.661 105.903 -47.500 1.00 18.33  ? 370 ILE B CG2 1 
ATOM   2343 C CD1 . ILE A 1 314 ? 16.076 103.490 -48.384 1.00 5.31   ? 370 ILE B CD1 1 
ATOM   2344 N N   . THR A 1 315 ? 12.757 107.163 -49.776 1.00 6.72   ? 371 THR B N   1 
ATOM   2345 C CA  . THR A 1 315 ? 11.914 108.349 -49.862 1.00 7.65   ? 371 THR B CA  1 
ATOM   2346 C C   . THR A 1 315 ? 11.371 108.665 -48.469 1.00 15.75  ? 371 THR B C   1 
ATOM   2347 O O   . THR A 1 315 ? 11.622 107.923 -47.520 1.00 21.13  ? 371 THR B O   1 
ATOM   2348 C CB  . THR A 1 315 ? 10.699 108.066 -50.757 1.00 9.34   ? 371 THR B CB  1 
ATOM   2349 O OG1 . THR A 1 315 ? 10.049 106.885 -50.284 1.00 12.75  ? 371 THR B OG1 1 
ATOM   2350 C CG2 . THR A 1 315 ? 11.114 107.820 -52.226 1.00 5.41   ? 371 THR B CG2 1 
ATOM   2351 N N   . GLY A 1 316 ? 10.602 109.750 -48.359 1.00 16.29  ? 372 GLY B N   1 
ATOM   2352 C CA  . GLY A 1 316 ? 9.957  110.129 -47.123 1.00 2.00   ? 372 GLY B CA  1 
ATOM   2353 C C   . GLY A 1 316 ? 10.840 111.045 -46.323 1.00 12.87  ? 372 GLY B C   1 
ATOM   2354 O O   . GLY A 1 316 ? 11.839 111.558 -46.846 1.00 9.68   ? 372 GLY B O   1 
ATOM   2355 N N   . GLU A 1 317 ? 10.495 111.222 -45.044 1.00 5.34   ? 373 GLU B N   1 
ATOM   2356 C CA  . GLU A 1 317 ? 11.200 112.140 -44.161 1.00 6.78   ? 373 GLU B CA  1 
ATOM   2357 C C   . GLU A 1 317 ? 12.139 111.392 -43.236 1.00 15.08  ? 373 GLU B C   1 
ATOM   2358 O O   . GLU A 1 317 ? 11.913 110.221 -42.916 1.00 15.09  ? 373 GLU B O   1 
ATOM   2359 C CB  . GLU A 1 317 ? 10.226 112.943 -43.311 1.00 6.69   ? 373 GLU B CB  1 
ATOM   2360 C CG  . GLU A 1 317 ? 9.260  113.770 -44.128 1.00 18.77  ? 373 GLU B CG  1 
ATOM   2361 C CD  . GLU A 1 317 ? 8.662  114.898 -43.321 1.00 26.23  ? 373 GLU B CD  1 
ATOM   2362 O OE1 . GLU A 1 317 ? 7.580  115.395 -43.692 1.00 26.35  ? 373 GLU B OE1 1 
ATOM   2363 O OE2 . GLU A 1 317 ? 9.291  115.301 -42.321 1.00 35.85  ? 373 GLU B OE2 1 
ATOM   2364 N N   . ILE A 1 318 ? 13.225 112.058 -42.853 1.00 13.37  ? 374 ILE B N   1 
ATOM   2365 C CA  . ILE A 1 318 ? 14.090 111.546 -41.807 1.00 12.34  ? 374 ILE B CA  1 
ATOM   2366 C C   . ILE A 1 318 ? 13.293 111.689 -40.530 1.00 10.81  ? 374 ILE B C   1 
ATOM   2367 O O   . ILE A 1 318 ? 12.843 112.786 -40.216 1.00 12.63  ? 374 ILE B O   1 
ATOM   2368 C CB  . ILE A 1 318 ? 15.364 112.367 -41.697 1.00 6.33   ? 374 ILE B CB  1 
ATOM   2369 C CG1 . ILE A 1 318 ? 16.204 112.200 -42.963 1.00 2.00   ? 374 ILE B CG1 1 
ATOM   2370 C CG2 . ILE A 1 318 ? 16.155 111.970 -40.446 1.00 7.18   ? 374 ILE B CG2 1 
ATOM   2371 C CD1 . ILE A 1 318 ? 17.229 113.302 -43.148 1.00 12.24  ? 374 ILE B CD1 1 
ATOM   2372 N N   . PRO A 1 319 ? 13.092 110.578 -39.804 1.00 6.84   ? 375 PRO B N   1 
ATOM   2373 C CA  . PRO A 1 319 ? 12.230 110.594 -38.620 1.00 9.90   ? 375 PRO B CA  1 
ATOM   2374 C C   . PRO A 1 319 ? 12.858 111.371 -37.471 1.00 8.52   ? 375 PRO B C   1 
ATOM   2375 O O   . PRO A 1 319 ? 14.065 111.253 -37.250 1.00 15.92  ? 375 PRO B O   1 
ATOM   2376 C CB  . PRO A 1 319 ? 12.094 109.105 -38.260 1.00 7.04   ? 375 PRO B CB  1 
ATOM   2377 C CG  . PRO A 1 319 ? 13.259 108.458 -38.856 1.00 2.00   ? 375 PRO B CG  1 
ATOM   2378 C CD  . PRO A 1 319 ? 13.680 109.253 -40.050 1.00 2.00   ? 375 PRO B CD  1 
ATOM   2379 N N   . SER A 1 320 ? 12.051 112.143 -36.749 1.00 9.45   ? 376 SER B N   1 
ATOM   2380 C CA  . SER A 1 320 ? 12.540 112.899 -35.588 1.00 13.88  ? 376 SER B CA  1 
ATOM   2381 C C   . SER A 1 320 ? 12.990 112.008 -34.437 1.00 13.30  ? 376 SER B C   1 
ATOM   2382 O O   . SER A 1 320 ? 13.875 112.377 -33.664 1.00 25.13  ? 376 SER B O   1 
ATOM   2383 C CB  . SER A 1 320 ? 11.470 113.848 -35.091 1.00 20.00  ? 376 SER B CB  1 
ATOM   2384 O OG  . SER A 1 320 ? 10.250 113.147 -34.993 1.00 36.75  ? 376 SER B OG  1 
ATOM   2385 N N   . LEU A 1 321 ? 12.415 110.813 -34.348 1.00 16.69  ? 377 LEU B N   1 
ATOM   2386 C CA  . LEU A 1 321 ? 12.781 109.847 -33.309 1.00 18.23  ? 377 LEU B CA  1 
ATOM   2387 C C   . LEU A 1 321 ? 14.238 109.413 -33.425 1.00 16.15  ? 377 LEU B C   1 
ATOM   2388 O O   . LEU A 1 321 ? 14.736 108.650 -32.614 1.00 18.86  ? 377 LEU B O   1 
ATOM   2389 C CB  . LEU A 1 321 ? 11.839 108.643 -33.294 1.00 20.64  ? 377 LEU B CB  1 
ATOM   2390 C CG  . LEU A 1 321 ? 10.586 108.931 -32.455 1.00 27.49  ? 377 LEU B CG  1 
ATOM   2391 C CD1 . LEU A 1 321 ? 9.609  107.744 -32.410 1.00 23.29  ? 377 LEU B CD1 1 
ATOM   2392 C CD2 . LEU A 1 321 ? 10.981 109.382 -31.046 1.00 20.81  ? 377 LEU B CD2 1 
ATOM   2393 N N   . MET A 1 322 ? 14.904 109.903 -34.459 1.00 10.86  ? 378 MET B N   1 
ATOM   2394 C CA  . MET A 1 322 ? 16.345 109.799 -34.584 1.00 19.25  ? 378 MET B CA  1 
ATOM   2395 C C   . MET A 1 322 ? 17.017 110.229 -33.280 1.00 20.13  ? 378 MET B C   1 
ATOM   2396 O O   . MET A 1 322 ? 18.097 109.735 -32.920 1.00 23.22  ? 378 MET B O   1 
ATOM   2397 C CB  . MET A 1 322 ? 16.795 110.730 -35.696 1.00 23.07  ? 378 MET B CB  1 
ATOM   2398 C CG  . MET A 1 322 ? 17.864 110.173 -36.562 1.00 30.33  ? 378 MET B CG  1 
ATOM   2399 S SD  . MET A 1 322 ? 17.311 108.976 -37.768 1.00 25.96  ? 378 MET B SD  1 
ATOM   2400 C CE  . MET A 1 322 ? 18.943 108.447 -38.281 1.00 20.13  ? 378 MET B CE  1 
ATOM   2401 N N   . SER A 1 323 ? 16.383 111.165 -32.579 1.00 14.31  ? 379 SER B N   1 
ATOM   2402 C CA  . SER A 1 323 ? 16.926 111.661 -31.315 1.00 12.50  ? 379 SER B CA  1 
ATOM   2403 C C   . SER A 1 323 ? 17.124 110.556 -30.271 1.00 14.72  ? 379 SER B C   1 
ATOM   2404 O O   . SER A 1 323 ? 17.896 110.719 -29.328 1.00 11.36  ? 379 SER B O   1 
ATOM   2405 C CB  . SER A 1 323 ? 16.009 112.731 -30.752 1.00 11.49  ? 379 SER B CB  1 
ATOM   2406 O OG  . SER A 1 323 ? 14.669 112.305 -30.865 1.00 10.21  ? 379 SER B OG  1 
ATOM   2407 N N   . ASN A 1 324 ? 16.429 109.435 -30.438 1.00 14.31  ? 380 ASN B N   1 
ATOM   2408 C CA  . ASN A 1 324 ? 16.614 108.297 -29.550 1.00 9.58   ? 380 ASN B CA  1 
ATOM   2409 C C   . ASN A 1 324 ? 17.882 107.498 -29.802 1.00 17.00  ? 380 ASN B C   1 
ATOM   2410 O O   . ASN A 1 324 ? 18.229 106.645 -28.993 1.00 24.92  ? 380 ASN B O   1 
ATOM   2411 C CB  . ASN A 1 324 ? 15.401 107.361 -29.570 1.00 17.10  ? 380 ASN B CB  1 
ATOM   2412 C CG  . ASN A 1 324 ? 14.442 107.647 -28.445 1.00 35.39  ? 380 ASN B CG  1 
ATOM   2413 O OD1 . ASN A 1 324 ? 13.419 108.294 -28.642 1.00 40.54  ? 380 ASN B OD1 1 
ATOM   2414 N ND2 . ASN A 1 324 ? 14.782 107.189 -27.242 1.00 43.46  ? 380 ASN B ND2 1 
ATOM   2415 N N   . LEU A 1 325 ? 18.586 107.749 -30.903 1.00 15.63  ? 381 LEU B N   1 
ATOM   2416 C CA  . LEU A 1 325 ? 19.836 107.034 -31.086 1.00 14.01  ? 381 LEU B CA  1 
ATOM   2417 C C   . LEU A 1 325 ? 20.907 107.919 -30.491 1.00 18.70  ? 381 LEU B C   1 
ATOM   2418 O O   . LEU A 1 325 ? 21.502 108.745 -31.191 1.00 16.76  ? 381 LEU B O   1 
ATOM   2419 C CB  . LEU A 1 325 ? 20.108 106.867 -32.585 1.00 3.34   ? 381 LEU B CB  1 
ATOM   2420 C CG  . LEU A 1 325 ? 18.972 106.193 -33.360 1.00 9.60   ? 381 LEU B CG  1 
ATOM   2421 C CD1 . LEU A 1 325 ? 19.118 106.315 -34.877 1.00 4.70   ? 381 LEU B CD1 1 
ATOM   2422 C CD2 . LEU A 1 325 ? 18.845 104.725 -32.938 1.00 10.80  ? 381 LEU B CD2 1 
ATOM   2423 N N   . ARG A 1 326 ? 21.261 107.637 -29.244 1.00 17.97  ? 382 ARG B N   1 
ATOM   2424 C CA  . ARG A 1 326 ? 22.086 108.569 -28.477 1.00 16.26  ? 382 ARG B CA  1 
ATOM   2425 C C   . ARG A 1 326 ? 23.544 108.257 -28.674 1.00 12.55  ? 382 ARG B C   1 
ATOM   2426 O O   . ARG A 1 326 ? 24.401 109.023 -28.248 1.00 16.66  ? 382 ARG B O   1 
ATOM   2427 C CB  . ARG A 1 326 ? 21.733 108.552 -26.983 1.00 5.83   ? 382 ARG B CB  1 
ATOM   2428 C CG  . ARG A 1 326 ? 20.333 109.070 -26.669 1.00 9.04   ? 382 ARG B CG  1 
ATOM   2429 C CD  . ARG A 1 326 ? 20.247 110.561 -26.937 1.00 25.01  ? 382 ARG B CD  1 
ATOM   2430 N NE  . ARG A 1 326 ? 18.882 110.983 -27.226 1.00 36.78  ? 382 ARG B NE  1 
ATOM   2431 C CZ  . ARG A 1 326 ? 18.019 111.416 -26.312 1.00 44.95  ? 382 ARG B CZ  1 
ATOM   2432 N NH1 . ARG A 1 326 ? 18.379 111.485 -25.036 1.00 46.64  ? 382 ARG B NH1 1 
ATOM   2433 N NH2 . ARG A 1 326 ? 16.792 111.780 -26.679 1.00 46.38  ? 382 ARG B NH2 1 
ATOM   2434 N N   . SER A 1 327 ? 23.824 107.115 -29.296 1.00 8.93   ? 383 SER B N   1 
ATOM   2435 C CA  . SER A 1 327 ? 25.198 106.760 -29.621 1.00 12.02  ? 383 SER B CA  1 
ATOM   2436 C C   . SER A 1 327 ? 25.628 107.003 -31.066 1.00 14.84  ? 383 SER B C   1 
ATOM   2437 O O   . SER A 1 327 ? 26.774 106.712 -31.407 1.00 21.67  ? 383 SER B O   1 
ATOM   2438 C CB  . SER A 1 327 ? 25.487 105.318 -29.212 1.00 16.17  ? 383 SER B CB  1 
ATOM   2439 O OG  . SER A 1 327 ? 25.531 105.216 -27.798 1.00 13.25  ? 383 SER B OG  1 
ATOM   2440 N N   . LEU A 1 328 ? 24.730 107.524 -31.908 1.00 11.17  ? 384 LEU B N   1 
ATOM   2441 C CA  . LEU A 1 328 ? 25.037 107.695 -33.333 1.00 7.52   ? 384 LEU B CA  1 
ATOM   2442 C C   . LEU A 1 328 ? 26.249 108.595 -33.537 1.00 6.00   ? 384 LEU B C   1 
ATOM   2443 O O   . LEU A 1 328 ? 26.241 109.740 -33.125 1.00 12.25  ? 384 LEU B O   1 
ATOM   2444 C CB  . LEU A 1 328 ? 23.841 108.348 -34.028 1.00 9.88   ? 384 LEU B CB  1 
ATOM   2445 C CG  . LEU A 1 328 ? 23.664 108.231 -35.547 1.00 4.96   ? 384 LEU B CG  1 
ATOM   2446 C CD1 . LEU A 1 328 ? 23.492 106.784 -35.889 1.00 3.76   ? 384 LEU B CD1 1 
ATOM   2447 C CD2 . LEU A 1 328 ? 22.441 109.009 -35.986 1.00 2.00   ? 384 LEU B CD2 1 
ATOM   2448 N N   . THR A 1 329 ? 27.307 108.088 -34.155 1.00 8.36   ? 385 THR B N   1 
ATOM   2449 C CA  . THR A 1 329 ? 28.391 108.979 -34.560 1.00 12.97  ? 385 THR B CA  1 
ATOM   2450 C C   . THR A 1 329 ? 28.426 109.318 -36.048 1.00 12.10  ? 385 THR B C   1 
ATOM   2451 O O   . THR A 1 329 ? 29.013 110.324 -36.439 1.00 14.22  ? 385 THR B O   1 
ATOM   2452 C CB  . THR A 1 329 ? 29.753 108.404 -34.136 1.00 17.64  ? 385 THR B CB  1 
ATOM   2453 O OG1 . THR A 1 329 ? 30.100 107.314 -35.003 1.00 19.95  ? 385 THR B OG1 1 
ATOM   2454 C CG2 . THR A 1 329 ? 29.675 107.905 -32.697 1.00 2.61   ? 385 THR B CG2 1 
ATOM   2455 N N   . MET A 1 330 ? 27.760 108.507 -36.866 1.00 8.67   ? 386 MET B N   1 
ATOM   2456 C CA  . MET A 1 330 ? 27.868 108.630 -38.329 1.00 12.07  ? 386 MET B CA  1 
ATOM   2457 C C   . MET A 1 330 ? 26.518 108.417 -39.021 1.00 10.91  ? 386 MET B C   1 
ATOM   2458 O O   . MET A 1 330 ? 25.921 107.348 -38.886 1.00 9.68   ? 386 MET B O   1 
ATOM   2459 C CB  . MET A 1 330 ? 28.921 107.648 -38.876 1.00 16.96  ? 386 MET B CB  1 
ATOM   2460 C CG  . MET A 1 330 ? 29.099 107.681 -40.407 1.00 34.47  ? 386 MET B CG  1 
ATOM   2461 S SD  . MET A 1 330 ? 30.630 106.936 -41.073 1.00 35.47  ? 386 MET B SD  1 
ATOM   2462 C CE  . MET A 1 330 ? 31.751 107.299 -39.715 1.00 9.96   ? 386 MET B CE  1 
ATOM   2463 N N   . PHE A 1 331 ? 26.026 109.423 -39.743 1.00 2.00   ? 387 PHE B N   1 
ATOM   2464 C CA  . PHE A 1 331 ? 24.773 109.252 -40.480 1.00 2.00   ? 387 PHE B CA  1 
ATOM   2465 C C   . PHE A 1 331 ? 24.946 109.670 -41.948 1.00 12.14  ? 387 PHE B C   1 
ATOM   2466 O O   . PHE A 1 331 ? 25.063 110.864 -42.258 1.00 20.80  ? 387 PHE B O   1 
ATOM   2467 C CB  . PHE A 1 331 ? 23.677 110.078 -39.809 1.00 2.00   ? 387 PHE B CB  1 
ATOM   2468 C CG  . PHE A 1 331 ? 22.324 109.942 -40.438 1.00 9.11   ? 387 PHE B CG  1 
ATOM   2469 C CD1 . PHE A 1 331 ? 21.896 108.733 -40.959 1.00 10.68  ? 387 PHE B CD1 1 
ATOM   2470 C CD2 . PHE A 1 331 ? 21.458 111.024 -40.476 1.00 8.66   ? 387 PHE B CD2 1 
ATOM   2471 C CE1 . PHE A 1 331 ? 20.640 108.611 -41.535 1.00 7.77   ? 387 PHE B CE1 1 
ATOM   2472 C CE2 . PHE A 1 331 ? 20.205 110.900 -41.048 1.00 7.91   ? 387 PHE B CE2 1 
ATOM   2473 C CZ  . PHE A 1 331 ? 19.796 109.688 -41.567 1.00 2.00   ? 387 PHE B CZ  1 
ATOM   2474 N N   . PHE A 1 332 ? 24.936 108.685 -42.845 1.00 4.97   ? 388 PHE B N   1 
ATOM   2475 C CA  . PHE A 1 332 ? 25.058 108.934 -44.282 1.00 2.16   ? 388 PHE B CA  1 
ATOM   2476 C C   . PHE A 1 332 ? 23.795 108.417 -44.976 1.00 11.71  ? 388 PHE B C   1 
ATOM   2477 O O   . PHE A 1 332 ? 23.563 107.192 -45.056 1.00 9.86   ? 388 PHE B O   1 
ATOM   2478 C CB  . PHE A 1 332 ? 26.250 108.149 -44.860 1.00 2.00   ? 388 PHE B CB  1 
ATOM   2479 C CG  . PHE A 1 332 ? 27.609 108.692 -44.481 1.00 4.84   ? 388 PHE B CG  1 
ATOM   2480 C CD1 . PHE A 1 332 ? 27.745 109.777 -43.623 1.00 5.10   ? 388 PHE B CD1 1 
ATOM   2481 C CD2 . PHE A 1 332 ? 28.758 108.124 -45.021 1.00 5.23   ? 388 PHE B CD2 1 
ATOM   2482 C CE1 . PHE A 1 332 ? 29.014 110.280 -43.286 1.00 9.45   ? 388 PHE B CE1 1 
ATOM   2483 C CE2 . PHE A 1 332 ? 30.014 108.621 -44.704 1.00 12.72  ? 388 PHE B CE2 1 
ATOM   2484 C CZ  . PHE A 1 332 ? 30.144 109.705 -43.828 1.00 10.75  ? 388 PHE B CZ  1 
ATOM   2485 N N   . ALA A 1 333 ? 22.948 109.351 -45.396 1.00 12.51  ? 389 ALA B N   1 
ATOM   2486 C CA  . ALA A 1 333 ? 21.819 109.106 -46.300 1.00 10.99  ? 389 ALA B CA  1 
ATOM   2487 C C   . ALA A 1 333 ? 21.961 109.676 -47.720 1.00 17.10  ? 389 ALA B C   1 
ATOM   2488 O O   . ALA A 1 333 ? 20.974 109.744 -48.451 1.00 22.24  ? 389 ALA B O   1 
ATOM   2489 C CB  . ALA A 1 333 ? 20.504 109.541 -45.668 1.00 12.77  ? 389 ALA B CB  1 
ATOM   2490 N N   . TRP A 1 334 ? 23.132 110.196 -48.071 1.00 12.80  ? 390 TRP B N   1 
ATOM   2491 C CA  . TRP A 1 334 ? 23.268 110.947 -49.323 1.00 3.70   ? 390 TRP B CA  1 
ATOM   2492 C C   . TRP A 1 334 ? 22.869 110.161 -50.580 1.00 4.97   ? 390 TRP B C   1 
ATOM   2493 O O   . TRP A 1 334 ? 22.928 108.930 -50.587 1.00 6.18   ? 390 TRP B O   1 
ATOM   2494 C CB  . TRP A 1 334 ? 24.665 111.574 -49.456 1.00 6.17   ? 390 TRP B CB  1 
ATOM   2495 C CG  . TRP A 1 334 ? 25.861 110.626 -49.525 1.00 12.54  ? 390 TRP B CG  1 
ATOM   2496 C CD1 . TRP A 1 334 ? 26.509 110.023 -48.472 1.00 12.88  ? 390 TRP B CD1 1 
ATOM   2497 C CD2 . TRP A 1 334 ? 26.582 110.238 -50.710 1.00 12.24  ? 390 TRP B CD2 1 
ATOM   2498 N NE1 . TRP A 1 334 ? 27.567 109.257 -48.941 1.00 12.88  ? 390 TRP B NE1 1 
ATOM   2499 C CE2 . TRP A 1 334 ? 27.635 109.382 -50.306 1.00 13.09  ? 390 TRP B CE2 1 
ATOM   2500 C CE3 . TRP A 1 334 ? 26.434 110.526 -52.075 1.00 14.03  ? 390 TRP B CE3 1 
ATOM   2501 C CZ2 . TRP A 1 334 ? 28.537 108.820 -51.220 1.00 14.04  ? 390 TRP B CZ2 1 
ATOM   2502 C CZ3 . TRP A 1 334 ? 27.333 109.960 -52.984 1.00 4.31   ? 390 TRP B CZ3 1 
ATOM   2503 C CH2 . TRP A 1 334 ? 28.365 109.120 -52.551 1.00 3.81   ? 390 TRP B CH2 1 
ATOM   2504 N N   . GLN A 1 335 ? 22.406 110.878 -51.611 1.00 5.03   ? 391 GLN B N   1 
ATOM   2505 C CA  . GLN A 1 335 ? 21.942 110.276 -52.877 1.00 2.00   ? 391 GLN B CA  1 
ATOM   2506 C C   . GLN A 1 335 ? 20.779 109.323 -52.631 1.00 7.34   ? 391 GLN B C   1 
ATOM   2507 O O   . GLN A 1 335 ? 20.897 108.097 -52.793 1.00 9.54   ? 391 GLN B O   1 
ATOM   2508 C CB  . GLN A 1 335 ? 23.091 109.581 -53.638 1.00 2.00   ? 391 GLN B CB  1 
ATOM   2509 C CG  . GLN A 1 335 ? 22.742 109.087 -55.035 1.00 7.55   ? 391 GLN B CG  1 
ATOM   2510 C CD  . GLN A 1 335 ? 22.241 110.200 -55.960 1.00 11.76  ? 391 GLN B CD  1 
ATOM   2511 O OE1 . GLN A 1 335 ? 23.035 110.938 -56.534 1.00 12.49  ? 391 GLN B OE1 1 
ATOM   2512 N NE2 . GLN A 1 335 ? 20.916 110.336 -56.076 1.00 13.44  ? 391 GLN B NE2 1 
ATOM   2513 N N   . ASN A 1 336 ? 19.659 109.905 -52.207 1.00 2.60   ? 392 ASN B N   1 
ATOM   2514 C CA  . ASN A 1 336 ? 18.395 109.198 -52.082 1.00 2.00   ? 392 ASN B CA  1 
ATOM   2515 C C   . ASN A 1 336 ? 17.297 110.145 -52.542 1.00 4.57   ? 392 ASN B C   1 
ATOM   2516 O O   . ASN A 1 336 ? 17.582 111.216 -53.057 1.00 9.55   ? 392 ASN B O   1 
ATOM   2517 C CB  . ASN A 1 336 ? 18.158 108.789 -50.622 1.00 9.71   ? 392 ASN B CB  1 
ATOM   2518 C CG  . ASN A 1 336 ? 18.770 107.437 -50.280 1.00 13.93  ? 392 ASN B CG  1 
ATOM   2519 O OD1 . ASN A 1 336 ? 18.285 106.389 -50.730 1.00 12.81  ? 392 ASN B OD1 1 
ATOM   2520 N ND2 . ASN A 1 336 ? 19.833 107.451 -49.469 1.00 11.26  ? 392 ASN B ND2 1 
ATOM   2521 N N   . LYS A 1 337 ? 16.045 109.744 -52.352 1.00 9.64   ? 393 LYS B N   1 
ATOM   2522 C CA  . LYS A 1 337 ? 14.848 110.563 -52.626 1.00 5.41   ? 393 LYS B CA  1 
ATOM   2523 C C   . LYS A 1 337 ? 14.221 111.266 -51.395 1.00 14.76  ? 393 LYS B C   1 
ATOM   2524 O O   . LYS A 1 337 ? 13.003 111.496 -51.387 1.00 15.97  ? 393 LYS B O   1 
ATOM   2525 C CB  . LYS A 1 337 ? 13.800 109.771 -53.402 1.00 11.64  ? 393 LYS B CB  1 
ATOM   2526 C CG  . LYS A 1 337 ? 14.333 109.095 -54.662 1.00 19.49  ? 393 LYS B CG  1 
ATOM   2527 C CD  . LYS A 1 337 ? 14.848 110.141 -55.606 1.00 35.48  ? 393 LYS B CD  1 
ATOM   2528 C CE  . LYS A 1 337 ? 15.538 109.547 -56.838 1.00 48.59  ? 393 LYS B CE  1 
ATOM   2529 N NZ  . LYS A 1 337 ? 16.165 110.632 -57.685 1.00 51.87  ? 393 LYS B NZ  1 
ATOM   2530 N N   . LEU A 1 338 ? 14.977 111.412 -50.302 1.00 11.28  ? 394 LEU B N   1 
ATOM   2531 C CA  . LEU A 1 338 ? 14.464 112.059 -49.084 1.00 4.26   ? 394 LEU B CA  1 
ATOM   2532 C C   . LEU A 1 338 ? 13.877 113.465 -49.260 1.00 8.12   ? 394 LEU B C   1 
ATOM   2533 O O   . LEU A 1 338 ? 14.461 114.317 -49.938 1.00 13.03  ? 394 LEU B O   1 
ATOM   2534 C CB  . LEU A 1 338 ? 15.552 112.122 -48.008 1.00 2.44   ? 394 LEU B CB  1 
ATOM   2535 C CG  . LEU A 1 338 ? 16.160 110.805 -47.523 1.00 8.87   ? 394 LEU B CG  1 
ATOM   2536 C CD1 . LEU A 1 338 ? 17.304 111.070 -46.535 1.00 5.69   ? 394 LEU B CD1 1 
ATOM   2537 C CD2 . LEU A 1 338 ? 15.109 109.925 -46.892 1.00 5.26   ? 394 LEU B CD2 1 
ATOM   2538 N N   . THR A 1 339 ? 12.736 113.711 -48.619 1.00 4.38   ? 395 THR B N   1 
ATOM   2539 C CA  . THR A 1 339 ? 12.118 115.035 -48.633 1.00 5.06   ? 395 THR B CA  1 
ATOM   2540 C C   . THR A 1 339 ? 11.786 115.482 -47.229 1.00 9.27   ? 395 THR B C   1 
ATOM   2541 O O   . THR A 1 339 ? 11.950 114.720 -46.281 1.00 22.28  ? 395 THR B O   1 
ATOM   2542 C CB  . THR A 1 339 ? 10.793 115.044 -49.436 1.00 12.59  ? 395 THR B CB  1 
ATOM   2543 O OG1 . THR A 1 339 ? 9.836  114.194 -48.790 1.00 15.24  ? 395 THR B OG1 1 
ATOM   2544 C CG2 . THR A 1 339 ? 11.026 114.563 -50.857 1.00 11.72  ? 395 THR B CG2 1 
ATOM   2545 N N   . GLY A 1 340 ? 11.267 116.702 -47.105 1.00 8.34   ? 396 GLY B N   1 
ATOM   2546 C CA  . GLY A 1 340 ? 10.877 117.243 -45.811 1.00 5.72   ? 396 GLY B CA  1 
ATOM   2547 C C   . GLY A 1 340 ? 12.032 117.993 -45.174 1.00 10.26  ? 396 GLY B C   1 
ATOM   2548 O O   . GLY A 1 340 ? 13.107 118.106 -45.779 1.00 11.44  ? 396 GLY B O   1 
ATOM   2549 N N   . ASN A 1 341 ? 11.805 118.516 -43.967 1.00 6.60   ? 397 ASN B N   1 
ATOM   2550 C CA  . ASN A 1 341 ? 12.842 119.209 -43.211 1.00 2.06   ? 397 ASN B CA  1 
ATOM   2551 C C   . ASN A 1 341 ? 13.869 118.252 -42.666 1.00 13.31  ? 397 ASN B C   1 
ATOM   2552 O O   . ASN A 1 341 ? 13.594 117.070 -42.472 1.00 19.81  ? 397 ASN B O   1 
ATOM   2553 C CB  . ASN A 1 341 ? 12.247 119.977 -42.031 1.00 2.42   ? 397 ASN B CB  1 
ATOM   2554 C CG  . ASN A 1 341 ? 11.721 121.350 -42.420 1.00 13.01  ? 397 ASN B CG  1 
ATOM   2555 O OD1 . ASN A 1 341 ? 10.665 121.468 -43.021 1.00 13.70  ? 397 ASN B OD1 1 
ATOM   2556 N ND2 . ASN A 1 341 ? 12.441 122.396 -42.037 1.00 21.65  ? 397 ASN B ND2 1 
ATOM   2557 N N   . ILE A 1 342 ? 15.067 118.766 -42.432 1.00 17.23  ? 398 ILE B N   1 
ATOM   2558 C CA  . ILE A 1 342 ? 16.035 118.074 -41.602 1.00 12.68  ? 398 ILE B CA  1 
ATOM   2559 C C   . ILE A 1 342 ? 15.572 118.295 -40.168 1.00 3.68   ? 398 ILE B C   1 
ATOM   2560 O O   . ILE A 1 342 ? 15.464 119.426 -39.735 1.00 3.61   ? 398 ILE B O   1 
ATOM   2561 C CB  . ILE A 1 342 ? 17.411 118.715 -41.736 1.00 12.34  ? 398 ILE B CB  1 
ATOM   2562 C CG1 . ILE A 1 342 ? 17.922 118.601 -43.171 1.00 6.37   ? 398 ILE B CG1 1 
ATOM   2563 C CG2 . ILE A 1 342 ? 18.384 118.095 -40.739 1.00 19.70  ? 398 ILE B CG2 1 
ATOM   2564 C CD1 . ILE A 1 342 ? 19.110 119.489 -43.451 1.00 2.00   ? 398 ILE B CD1 1 
ATOM   2565 N N   . PRO A 1 343 ? 15.286 117.217 -39.434 1.00 7.21   ? 399 PRO B N   1 
ATOM   2566 C CA  . PRO A 1 343 ? 14.738 117.364 -38.075 1.00 9.83   ? 399 PRO B CA  1 
ATOM   2567 C C   . PRO A 1 343 ? 15.736 117.959 -37.080 1.00 14.13  ? 399 PRO B C   1 
ATOM   2568 O O   . PRO A 1 343 ? 16.851 117.442 -36.955 1.00 14.03  ? 399 PRO B O   1 
ATOM   2569 C CB  . PRO A 1 343 ? 14.430 115.915 -37.674 1.00 17.31  ? 399 PRO B CB  1 
ATOM   2570 C CG  . PRO A 1 343 ? 15.436 115.086 -38.494 1.00 13.86  ? 399 PRO B CG  1 
ATOM   2571 C CD  . PRO A 1 343 ? 15.507 115.807 -39.811 1.00 3.10   ? 399 PRO B CD  1 
ATOM   2572 N N   . GLN A 1 344 ? 15.321 118.991 -36.346 1.00 16.49  ? 400 GLN B N   1 
ATOM   2573 C CA  . GLN A 1 344 ? 16.140 119.542 -35.263 1.00 21.73  ? 400 GLN B CA  1 
ATOM   2574 C C   . GLN A 1 344 ? 16.514 118.485 -34.201 1.00 18.49  ? 400 GLN B C   1 
ATOM   2575 O O   . GLN A 1 344 ? 17.551 118.603 -33.532 1.00 14.11  ? 400 GLN B O   1 
ATOM   2576 C CB  . GLN A 1 344 ? 15.435 120.734 -34.590 1.00 18.99  ? 400 GLN B CB  1 
ATOM   2577 C CG  . GLN A 1 344 ? 14.243 120.361 -33.717 1.00 29.27  ? 400 GLN B CG  1 
ATOM   2578 C CD  . GLN A 1 344 ? 14.494 120.604 -32.226 1.00 42.28  ? 400 GLN B CD  1 
ATOM   2579 O OE1 . GLN A 1 344 ? 14.680 121.745 -31.800 1.00 47.03  ? 400 GLN B OE1 1 
ATOM   2580 N NE2 . GLN A 1 344 ? 14.501 119.530 -31.431 1.00 43.48  ? 400 GLN B NE2 1 
ATOM   2581 N N   . SER A 1 345 ? 15.677 117.455 -34.065 1.00 8.54   ? 401 SER B N   1 
ATOM   2582 C CA  . SER A 1 345 ? 15.851 116.445 -33.026 1.00 3.86   ? 401 SER B CA  1 
ATOM   2583 C C   . SER A 1 345 ? 17.104 115.622 -33.257 1.00 15.10  ? 401 SER B C   1 
ATOM   2584 O O   . SER A 1 345 ? 17.573 114.921 -32.368 1.00 28.37  ? 401 SER B O   1 
ATOM   2585 C CB  . SER A 1 345 ? 14.639 115.523 -32.958 1.00 10.06  ? 401 SER B CB  1 
ATOM   2586 O OG  . SER A 1 345 ? 14.599 114.673 -34.087 1.00 18.31  ? 401 SER B OG  1 
ATOM   2587 N N   . LEU A 1 346 ? 17.642 115.711 -34.462 1.00 13.43  ? 402 LEU B N   1 
ATOM   2588 C CA  . LEU A 1 346 ? 18.904 115.068 -34.795 1.00 8.44   ? 402 LEU B CA  1 
ATOM   2589 C C   . LEU A 1 346 ? 20.029 115.641 -33.937 1.00 18.74  ? 402 LEU B C   1 
ATOM   2590 O O   . LEU A 1 346 ? 21.021 114.963 -33.664 1.00 31.11  ? 402 LEU B O   1 
ATOM   2591 C CB  . LEU A 1 346 ? 19.195 115.274 -36.277 1.00 8.45   ? 402 LEU B CB  1 
ATOM   2592 C CG  . LEU A 1 346 ? 20.118 114.333 -37.042 1.00 20.30  ? 402 LEU B CG  1 
ATOM   2593 C CD1 . LEU A 1 346 ? 19.888 112.916 -36.615 1.00 23.11  ? 402 LEU B CD1 1 
ATOM   2594 C CD2 . LEU A 1 346 ? 19.876 114.474 -38.553 1.00 21.11  ? 402 LEU B CD2 1 
ATOM   2595 N N   . SER A 1 347 ? 19.863 116.881 -33.482 1.00 14.10  ? 403 SER B N   1 
ATOM   2596 C CA  . SER A 1 347 ? 20.823 117.479 -32.560 1.00 19.85  ? 403 SER B CA  1 
ATOM   2597 C C   . SER A 1 347 ? 20.840 116.812 -31.165 1.00 18.14  ? 403 SER B C   1 
ATOM   2598 O O   . SER A 1 347 ? 21.698 117.131 -30.333 1.00 17.18  ? 403 SER B O   1 
ATOM   2599 C CB  . SER A 1 347 ? 20.551 118.973 -32.404 1.00 23.69  ? 403 SER B CB  1 
ATOM   2600 O OG  . SER A 1 347 ? 19.497 119.196 -31.481 1.00 19.74  ? 403 SER B OG  1 
ATOM   2601 N N   . GLN A 1 348 ? 19.899 115.912 -30.883 1.00 7.62   ? 404 GLN B N   1 
ATOM   2602 C CA  . GLN A 1 348 ? 19.961 115.227 -29.593 1.00 11.83  ? 404 GLN B CA  1 
ATOM   2603 C C   . GLN A 1 348 ? 20.928 114.042 -29.585 1.00 19.29  ? 404 GLN B C   1 
ATOM   2604 O O   . GLN A 1 348 ? 21.227 113.504 -28.522 1.00 25.78  ? 404 GLN B O   1 
ATOM   2605 C CB  . GLN A 1 348 ? 18.583 114.814 -29.088 1.00 11.86  ? 404 GLN B CB  1 
ATOM   2606 C CG  . GLN A 1 348 ? 17.688 115.982 -28.728 1.00 9.24   ? 404 GLN B CG  1 
ATOM   2607 C CD  . GLN A 1 348 ? 16.305 115.527 -28.355 1.00 27.11  ? 404 GLN B CD  1 
ATOM   2608 O OE1 . GLN A 1 348 ? 16.142 114.592 -27.573 1.00 43.32  ? 404 GLN B OE1 1 
ATOM   2609 N NE2 . GLN A 1 348 ? 15.296 116.169 -28.923 1.00 30.39  ? 404 GLN B NE2 1 
ATOM   2610 N N   . CYS A 1 349 ? 21.455 113.664 -30.749 1.00 21.37  ? 405 CYS B N   1 
ATOM   2611 C CA  . CYS A 1 349 ? 22.461 112.609 -30.768 1.00 14.84  ? 405 CYS B CA  1 
ATOM   2612 C C   . CYS A 1 349 ? 23.737 113.374 -30.629 1.00 19.87  ? 405 CYS B C   1 
ATOM   2613 O O   . CYS A 1 349 ? 24.271 113.896 -31.614 1.00 21.49  ? 405 CYS B O   1 
ATOM   2614 C CB  . CYS A 1 349 ? 22.480 111.899 -32.133 1.00 9.24   ? 405 CYS B CB  1 
ATOM   2615 S SG  . CYS A 1 349 ? 20.862 111.455 -32.826 1.00 13.32  ? 405 CYS B SG  1 
ATOM   2616 N N   . ARG A 1 350 ? 24.285 113.376 -29.423 1.00 25.35  ? 406 ARG B N   1 
ATOM   2617 C CA  . ARG A 1 350 ? 25.323 114.350 -29.113 1.00 22.82  ? 406 ARG B CA  1 
ATOM   2618 C C   . ARG A 1 350 ? 26.687 113.867 -29.624 1.00 13.13  ? 406 ARG B C   1 
ATOM   2619 O O   . ARG A 1 350 ? 27.623 114.643 -29.725 1.00 15.19  ? 406 ARG B O   1 
ATOM   2620 C CB  . ARG A 1 350 ? 25.344 114.696 -27.606 1.00 21.21  ? 406 ARG B CB  1 
ATOM   2621 C CG  . ARG A 1 350 ? 24.027 115.244 -27.015 1.00 19.73  ? 406 ARG B CG  1 
ATOM   2622 C CD  . ARG A 1 350 ? 23.580 116.574 -27.653 1.00 22.94  ? 406 ARG B CD  1 
ATOM   2623 N NE  . ARG A 1 350 ? 24.552 117.651 -27.458 1.00 25.12  ? 406 ARG B NE  1 
ATOM   2624 C CZ  . ARG A 1 350 ? 24.532 118.834 -28.079 1.00 24.20  ? 406 ARG B CZ  1 
ATOM   2625 N NH1 . ARG A 1 350 ? 23.587 119.143 -28.965 1.00 23.91  ? 406 ARG B NH1 1 
ATOM   2626 N NH2 . ARG A 1 350 ? 25.476 119.722 -27.815 1.00 25.03  ? 406 ARG B NH2 1 
ATOM   2627 N N   . GLU A 1 351 ? 26.789 112.586 -29.963 1.00 7.59   ? 407 GLU B N   1 
ATOM   2628 C CA  . GLU A 1 351 ? 28.056 112.034 -30.446 1.00 11.51  ? 407 GLU B CA  1 
ATOM   2629 C C   . GLU A 1 351 ? 28.341 112.220 -31.944 1.00 13.86  ? 407 GLU B C   1 
ATOM   2630 O O   . GLU A 1 351 ? 29.433 111.861 -32.381 1.00 17.48  ? 407 GLU B O   1 
ATOM   2631 C CB  . GLU A 1 351 ? 28.166 110.534 -30.125 1.00 11.43  ? 407 GLU B CB  1 
ATOM   2632 C CG  . GLU A 1 351 ? 27.700 110.132 -28.741 1.00 20.17  ? 407 GLU B CG  1 
ATOM   2633 C CD  . GLU A 1 351 ? 28.489 110.794 -27.628 1.00 34.03  ? 407 GLU B CD  1 
ATOM   2634 O OE1 . GLU A 1 351 ? 27.871 111.184 -26.610 1.00 46.01  ? 407 GLU B OE1 1 
ATOM   2635 O OE2 . GLU A 1 351 ? 29.726 110.917 -27.761 1.00 34.35  ? 407 GLU B OE2 1 
ATOM   2636 N N   . LEU A 1 352 ? 27.403 112.768 -32.728 1.00 9.20   ? 408 LEU B N   1 
ATOM   2637 C CA  . LEU A 1 352 ? 27.578 112.769 -34.196 1.00 14.18  ? 408 LEU B CA  1 
ATOM   2638 C C   . LEU A 1 352 ? 28.876 113.422 -34.681 1.00 23.55  ? 408 LEU B C   1 
ATOM   2639 O O   . LEU A 1 352 ? 29.142 114.596 -34.432 1.00 24.29  ? 408 LEU B O   1 
ATOM   2640 C CB  . LEU A 1 352 ? 26.402 113.449 -34.894 1.00 8.24   ? 408 LEU B CB  1 
ATOM   2641 C CG  . LEU A 1 352 ? 25.131 112.620 -35.112 1.00 10.78  ? 408 LEU B CG  1 
ATOM   2642 C CD1 . LEU A 1 352 ? 23.984 113.485 -35.638 1.00 5.10   ? 408 LEU B CD1 1 
ATOM   2643 C CD2 . LEU A 1 352 ? 25.417 111.460 -36.041 1.00 6.26   ? 408 LEU B CD2 1 
ATOM   2644 N N   . GLN A 1 353 ? 29.693 112.626 -35.362 1.00 21.91  ? 409 GLN B N   1 
ATOM   2645 C CA  . GLN A 1 353 ? 30.895 113.125 -36.005 1.00 17.19  ? 409 GLN B CA  1 
ATOM   2646 C C   . GLN A 1 353 ? 30.690 113.600 -37.440 1.00 19.23  ? 409 GLN B C   1 
ATOM   2647 O O   . GLN A 1 353 ? 31.328 114.555 -37.887 1.00 18.39  ? 409 GLN B O   1 
ATOM   2648 C CB  . GLN A 1 353 ? 32.032 112.115 -35.870 1.00 12.93  ? 409 GLN B CB  1 
ATOM   2649 C CG  . GLN A 1 353 ? 32.518 112.000 -34.437 1.00 10.64  ? 409 GLN B CG  1 
ATOM   2650 C CD  . GLN A 1 353 ? 33.149 110.655 -34.118 1.00 16.59  ? 409 GLN B CD  1 
ATOM   2651 O OE1 . GLN A 1 353 ? 33.637 109.948 -35.011 1.00 22.07  ? 409 GLN B OE1 1 
ATOM   2652 N NE2 . GLN A 1 353 ? 33.132 110.289 -32.839 1.00 10.52  ? 409 GLN B NE2 1 
ATOM   2653 N N   . ALA A 1 354 ? 29.827 112.891 -38.167 1.00 17.56  ? 410 ALA B N   1 
ATOM   2654 C CA  . ALA A 1 354 ? 29.638 113.139 -39.595 1.00 6.10   ? 410 ALA B CA  1 
ATOM   2655 C C   . ALA A 1 354 ? 28.186 112.996 -40.034 1.00 8.39   ? 410 ALA B C   1 
ATOM   2656 O O   . ALA A 1 354 ? 27.548 111.952 -39.808 1.00 11.26  ? 410 ALA B O   1 
ATOM   2657 C CB  . ALA A 1 354 ? 30.514 112.208 -40.396 1.00 2.58   ? 410 ALA B CB  1 
ATOM   2658 N N   . ILE A 1 355 ? 27.672 114.039 -40.682 1.00 6.21   ? 411 ILE B N   1 
ATOM   2659 C CA  . ILE A 1 355 ? 26.353 113.972 -41.304 1.00 6.16   ? 411 ILE B CA  1 
ATOM   2660 C C   . ILE A 1 355 ? 26.492 114.205 -42.820 1.00 8.75   ? 411 ILE B C   1 
ATOM   2661 O O   . ILE A 1 355 ? 27.057 115.221 -43.221 1.00 4.96   ? 411 ILE B O   1 
ATOM   2662 C CB  . ILE A 1 355 ? 25.443 115.028 -40.697 1.00 2.00   ? 411 ILE B CB  1 
ATOM   2663 C CG1 . ILE A 1 355 ? 25.507 114.941 -39.184 1.00 4.84   ? 411 ILE B CG1 1 
ATOM   2664 C CG2 . ILE A 1 355 ? 24.016 114.852 -41.166 1.00 8.17   ? 411 ILE B CG2 1 
ATOM   2665 C CD1 . ILE A 1 355 ? 24.717 116.020 -38.463 1.00 2.00   ? 411 ILE B CD1 1 
ATOM   2666 N N   . ASP A 1 356 ? 26.040 113.266 -43.660 1.00 9.71   ? 412 ASP B N   1 
ATOM   2667 C CA  . ASP A 1 356 ? 25.955 113.553 -45.110 1.00 2.81   ? 412 ASP B CA  1 
ATOM   2668 C C   . ASP A 1 356 ? 24.567 113.215 -45.653 1.00 4.59   ? 412 ASP B C   1 
ATOM   2669 O O   . ASP A 1 356 ? 24.176 112.048 -45.752 1.00 2.00   ? 412 ASP B O   1 
ATOM   2670 C CB  . ASP A 1 356 ? 27.039 112.811 -45.890 1.00 2.00   ? 412 ASP B CB  1 
ATOM   2671 C CG  . ASP A 1 356 ? 27.185 113.303 -47.343 1.00 23.92  ? 412 ASP B CG  1 
ATOM   2672 O OD1 . ASP A 1 356 ? 26.286 114.003 -47.871 1.00 19.99  ? 412 ASP B OD1 1 
ATOM   2673 O OD2 . ASP A 1 356 ? 28.215 112.970 -47.971 1.00 19.83  ? 412 ASP B OD2 1 
ATOM   2674 N N   . LEU A 1 357 ? 23.817 114.271 -45.948 1.00 8.41   ? 413 LEU B N   1 
ATOM   2675 C CA  . LEU A 1 357 ? 22.491 114.203 -46.546 1.00 2.00   ? 413 LEU B CA  1 
ATOM   2676 C C   . LEU A 1 357 ? 22.433 114.658 -48.007 1.00 8.24   ? 413 LEU B C   1 
ATOM   2677 O O   . LEU A 1 357 ? 21.353 114.953 -48.522 1.00 6.65   ? 413 LEU B O   1 
ATOM   2678 C CB  . LEU A 1 357 ? 21.446 114.864 -45.659 1.00 15.04  ? 413 LEU B CB  1 
ATOM   2679 C CG  . LEU A 1 357 ? 21.477 114.302 -44.223 1.00 16.22  ? 413 LEU B CG  1 
ATOM   2680 C CD1 . LEU A 1 357 ? 20.499 115.027 -43.347 1.00 2.00   ? 413 LEU B CD1 1 
ATOM   2681 C CD2 . LEU A 1 357 ? 21.209 112.799 -44.202 1.00 15.48  ? 413 LEU B CD2 1 
ATOM   2682 N N   . SER A 1 358 ? 23.593 114.810 -48.641 1.00 2.00   ? 414 SER B N   1 
ATOM   2683 C CA  . SER A 1 358 ? 23.675 115.447 -49.954 1.00 5.65   ? 414 SER B CA  1 
ATOM   2684 C C   . SER A 1 358 ? 22.843 114.677 -50.976 1.00 10.89  ? 414 SER B C   1 
ATOM   2685 O O   . SER A 1 358 ? 22.496 113.522 -50.745 1.00 9.76   ? 414 SER B O   1 
ATOM   2686 C CB  . SER A 1 358 ? 25.133 115.520 -50.451 1.00 7.19   ? 414 SER B CB  1 
ATOM   2687 O OG  . SER A 1 358 ? 26.053 115.962 -49.453 1.00 2.10   ? 414 SER B OG  1 
ATOM   2688 N N   . TYR A 1 359 ? 22.479 115.340 -52.076 1.00 9.35   ? 415 TYR B N   1 
ATOM   2689 C CA  . TYR A 1 359 ? 21.771 114.687 -53.178 1.00 4.62   ? 415 TYR B CA  1 
ATOM   2690 C C   . TYR A 1 359 ? 20.433 114.099 -52.779 1.00 2.93   ? 415 TYR B C   1 
ATOM   2691 O O   . TYR A 1 359 ? 20.177 112.919 -52.996 1.00 4.71   ? 415 TYR B O   1 
ATOM   2692 C CB  . TYR A 1 359 ? 22.638 113.604 -53.823 1.00 8.64   ? 415 TYR B CB  1 
ATOM   2693 C CG  . TYR A 1 359 ? 23.877 114.159 -54.471 1.00 2.00   ? 415 TYR B CG  1 
ATOM   2694 C CD1 . TYR A 1 359 ? 23.797 114.910 -55.641 1.00 2.00   ? 415 TYR B CD1 1 
ATOM   2695 C CD2 . TYR A 1 359 ? 25.123 113.941 -53.920 1.00 3.40   ? 415 TYR B CD2 1 
ATOM   2696 C CE1 . TYR A 1 359 ? 24.936 115.422 -56.240 1.00 2.00   ? 415 TYR B CE1 1 
ATOM   2697 C CE2 . TYR A 1 359 ? 26.267 114.459 -54.507 1.00 2.24   ? 415 TYR B CE2 1 
ATOM   2698 C CZ  . TYR A 1 359 ? 26.159 115.190 -55.661 1.00 5.18   ? 415 TYR B CZ  1 
ATOM   2699 O OH  . TYR A 1 359 ? 27.291 115.687 -56.232 1.00 20.87  ? 415 TYR B OH  1 
ATOM   2700 N N   . ASN A 1 360 ? 19.595 114.928 -52.166 1.00 8.02   ? 416 ASN B N   1 
ATOM   2701 C CA  . ASN A 1 360 ? 18.238 114.550 -51.840 1.00 2.00   ? 416 ASN B CA  1 
ATOM   2702 C C   . ASN A 1 360 ? 17.334 115.679 -52.272 1.00 6.95   ? 416 ASN B C   1 
ATOM   2703 O O   . ASN A 1 360 ? 17.750 116.579 -52.985 1.00 9.12   ? 416 ASN B O   1 
ATOM   2704 C CB  . ASN A 1 360 ? 18.076 114.286 -50.332 1.00 2.00   ? 416 ASN B CB  1 
ATOM   2705 C CG  . ASN A 1 360 ? 18.538 112.881 -49.916 1.00 5.95   ? 416 ASN B CG  1 
ATOM   2706 O OD1 . ASN A 1 360 ? 17.881 111.894 -50.226 1.00 12.10  ? 416 ASN B OD1 1 
ATOM   2707 N ND2 . ASN A 1 360 ? 19.657 112.797 -49.202 1.00 2.00   ? 416 ASN B ND2 1 
ATOM   2708 N N   . SER A 1 361 ? 16.070 115.579 -51.899 1.00 9.49   ? 417 SER B N   1 
ATOM   2709 C CA  . SER A 1 361 ? 15.101 116.650 -52.034 1.00 8.10   ? 417 SER B CA  1 
ATOM   2710 C C   . SER A 1 361 ? 14.784 117.438 -50.752 1.00 11.03  ? 417 SER B C   1 
ATOM   2711 O O   . SER A 1 361 ? 13.681 117.990 -50.623 1.00 12.98  ? 417 SER B O   1 
ATOM   2712 C CB  . SER A 1 361 ? 13.850 116.165 -52.734 1.00 10.10  ? 417 SER B CB  1 
ATOM   2713 O OG  . SER A 1 361 ? 14.147 115.991 -54.096 1.00 14.40  ? 417 SER B OG  1 
ATOM   2714 N N   . LEU A 1 362 ? 15.640 117.347 -49.745 1.00 5.55   ? 418 LEU B N   1 
ATOM   2715 C CA  . LEU A 1 362 ? 15.338 118.017 -48.474 1.00 11.61  ? 418 LEU B CA  1 
ATOM   2716 C C   . LEU A 1 362 ? 15.068 119.493 -48.692 1.00 11.05  ? 418 LEU B C   1 
ATOM   2717 O O   . LEU A 1 362 ? 15.652 120.112 -49.583 1.00 10.22  ? 418 LEU B O   1 
ATOM   2718 C CB  . LEU A 1 362 ? 16.474 117.828 -47.462 1.00 2.00   ? 418 LEU B CB  1 
ATOM   2719 C CG  . LEU A 1 362 ? 16.676 116.360 -47.086 1.00 2.00   ? 418 LEU B CG  1 
ATOM   2720 C CD1 . LEU A 1 362 ? 18.050 116.111 -46.499 1.00 2.00   ? 418 LEU B CD1 1 
ATOM   2721 C CD2 . LEU A 1 362 ? 15.565 115.920 -46.147 1.00 2.00   ? 418 LEU B CD2 1 
ATOM   2722 N N   . SER A 1 363 ? 14.163 120.054 -47.898 1.00 13.24  ? 419 SER B N   1 
ATOM   2723 C CA  . SER A 1 363 ? 13.840 121.461 -48.038 1.00 12.10  ? 419 SER B CA  1 
ATOM   2724 C C   . SER A 1 363 ? 13.715 122.088 -46.664 1.00 13.81  ? 419 SER B C   1 
ATOM   2725 O O   . SER A 1 363 ? 13.856 121.398 -45.666 1.00 18.33  ? 419 SER B O   1 
ATOM   2726 C CB  . SER A 1 363 ? 12.542 121.638 -48.832 1.00 13.63  ? 419 SER B CB  1 
ATOM   2727 O OG  . SER A 1 363 ? 11.452 121.016 -48.176 1.00 12.81  ? 419 SER B OG  1 
ATOM   2728 N N   . GLY A 1 364 ? 13.424 123.387 -46.619 1.00 11.61  ? 420 GLY B N   1 
ATOM   2729 C CA  . GLY A 1 364 ? 13.296 124.093 -45.362 1.00 2.80   ? 420 GLY B CA  1 
ATOM   2730 C C   . GLY A 1 364 ? 14.621 124.680 -44.905 1.00 22.14  ? 420 GLY B C   1 
ATOM   2731 O O   . GLY A 1 364 ? 15.610 124.661 -45.652 1.00 16.99  ? 420 GLY B O   1 
ATOM   2732 N N   . SER A 1 365 ? 14.642 125.205 -43.678 1.00 11.36  ? 421 SER B N   1 
ATOM   2733 C CA  . SER A 1 365 ? 15.852 125.774 -43.105 1.00 3.41   ? 421 SER B CA  1 
ATOM   2734 C C   . SER A 1 365 ? 16.749 124.686 -42.577 1.00 6.29   ? 421 SER B C   1 
ATOM   2735 O O   . SER A 1 365 ? 16.274 123.596 -42.274 1.00 10.58  ? 421 SER B O   1 
ATOM   2736 C CB  . SER A 1 365 ? 15.511 126.722 -41.969 1.00 17.55  ? 421 SER B CB  1 
ATOM   2737 O OG  . SER A 1 365 ? 15.180 127.993 -42.477 1.00 22.78  ? 421 SER B OG  1 
ATOM   2738 N N   . ILE A 1 366 ? 18.046 124.973 -42.503 1.00 3.53   ? 422 ILE B N   1 
ATOM   2739 C CA  . ILE A 1 366 ? 18.957 124.165 -41.710 1.00 10.94  ? 422 ILE B CA  1 
ATOM   2740 C C   . ILE A 1 366 ? 18.708 124.539 -40.246 1.00 13.15  ? 422 ILE B C   1 
ATOM   2741 O O   . ILE A 1 366 ? 18.862 125.710 -39.864 1.00 11.77  ? 422 ILE B O   1 
ATOM   2742 C CB  . ILE A 1 366 ? 20.443 124.452 -42.064 1.00 8.38   ? 422 ILE B CB  1 
ATOM   2743 C CG1 . ILE A 1 366 ? 20.697 124.232 -43.549 1.00 8.38   ? 422 ILE B CG1 1 
ATOM   2744 C CG2 . ILE A 1 366 ? 21.382 123.554 -41.227 1.00 12.65  ? 422 ILE B CG2 1 
ATOM   2745 C CD1 . ILE A 1 366 ? 22.041 124.701 -44.029 1.00 18.32  ? 422 ILE B CD1 1 
ATOM   2746 N N   . PRO A 1 367 ? 18.298 123.560 -39.424 1.00 14.09  ? 423 PRO B N   1 
ATOM   2747 C CA  . PRO A 1 367 ? 17.948 123.844 -38.025 1.00 3.75   ? 423 PRO B CA  1 
ATOM   2748 C C   . PRO A 1 367 ? 19.188 124.255 -37.253 1.00 5.55   ? 423 PRO B C   1 
ATOM   2749 O O   . PRO A 1 367 ? 20.200 123.565 -37.334 1.00 4.04   ? 423 PRO B O   1 
ATOM   2750 C CB  . PRO A 1 367 ? 17.433 122.493 -37.512 1.00 5.25   ? 423 PRO B CB  1 
ATOM   2751 C CG  . PRO A 1 367 ? 18.105 121.491 -38.354 1.00 12.84  ? 423 PRO B CG  1 
ATOM   2752 C CD  . PRO A 1 367 ? 18.232 122.121 -39.727 1.00 12.54  ? 423 PRO B CD  1 
ATOM   2753 N N   . LYS A 1 368 ? 19.116 125.337 -36.487 1.00 8.58   ? 424 LYS B N   1 
ATOM   2754 C CA  . LYS A 1 368 ? 20.311 125.846 -35.826 1.00 5.32   ? 424 LYS B CA  1 
ATOM   2755 C C   . LYS A 1 368 ? 20.912 124.882 -34.815 1.00 8.86   ? 424 LYS B C   1 
ATOM   2756 O O   . LYS A 1 368 ? 22.106 124.932 -34.535 1.00 9.87   ? 424 LYS B O   1 
ATOM   2757 C CB  . LYS A 1 368 ? 19.996 127.150 -35.138 1.00 7.54   ? 424 LYS B CB  1 
ATOM   2758 C CG  . LYS A 1 368 ? 18.960 127.031 -34.062 1.00 6.12   ? 424 LYS B CG  1 
ATOM   2759 C CD  . LYS A 1 368 ? 18.677 128.412 -33.514 1.00 12.40  ? 424 LYS B CD  1 
ATOM   2760 C CE  . LYS A 1 368 ? 17.567 128.398 -32.478 1.00 24.21  ? 424 LYS B CE  1 
ATOM   2761 N NZ  . LYS A 1 368 ? 17.056 129.785 -32.253 1.00 32.44  ? 424 LYS B NZ  1 
ATOM   2762 N N   . GLU A 1 369 ? 20.085 123.991 -34.284 1.00 6.77   ? 425 GLU B N   1 
ATOM   2763 C CA  . GLU A 1 369 ? 20.512 123.089 -33.230 1.00 13.27  ? 425 GLU B CA  1 
ATOM   2764 C C   . GLU A 1 369 ? 21.629 122.167 -33.694 1.00 15.22  ? 425 GLU B C   1 
ATOM   2765 O O   . GLU A 1 369 ? 22.474 121.750 -32.920 1.00 23.04  ? 425 GLU B O   1 
ATOM   2766 C CB  . GLU A 1 369 ? 19.324 122.281 -32.700 1.00 18.77  ? 425 GLU B CB  1 
ATOM   2767 C CG  . GLU A 1 369 ? 18.304 123.108 -31.897 1.00 21.33  ? 425 GLU B CG  1 
ATOM   2768 C CD  . GLU A 1 369 ? 17.281 123.846 -32.771 1.00 33.69  ? 425 GLU B CD  1 
ATOM   2769 O OE1 . GLU A 1 369 ? 17.276 123.674 -34.014 1.00 32.27  ? 425 GLU B OE1 1 
ATOM   2770 O OE2 . GLU A 1 369 ? 16.474 124.613 -32.204 1.00 41.91  ? 425 GLU B OE2 1 
ATOM   2771 N N   . ILE A 1 370 ? 21.655 121.870 -34.976 1.00 18.51  ? 426 ILE B N   1 
ATOM   2772 C CA  . ILE A 1 370 ? 22.659 120.955 -35.484 1.00 20.29  ? 426 ILE B CA  1 
ATOM   2773 C C   . ILE A 1 370 ? 24.060 121.562 -35.290 1.00 20.56  ? 426 ILE B C   1 
ATOM   2774 O O   . ILE A 1 370 ? 25.064 120.846 -35.223 1.00 14.23  ? 426 ILE B O   1 
ATOM   2775 C CB  . ILE A 1 370 ? 22.381 120.604 -36.965 1.00 21.78  ? 426 ILE B CB  1 
ATOM   2776 C CG1 . ILE A 1 370 ? 22.536 119.110 -37.209 1.00 28.90  ? 426 ILE B CG1 1 
ATOM   2777 C CG2 . ILE A 1 370 ? 23.264 121.395 -37.888 1.00 24.43  ? 426 ILE B CG2 1 
ATOM   2778 C CD1 . ILE A 1 370 ? 21.297 118.319 -36.848 1.00 31.98  ? 426 ILE B CD1 1 
ATOM   2779 N N   . PHE A 1 371 ? 24.118 122.886 -35.163 1.00 16.98  ? 427 PHE B N   1 
ATOM   2780 C CA  . PHE A 1 371 ? 25.401 123.562 -35.067 1.00 19.66  ? 427 PHE B CA  1 
ATOM   2781 C C   . PHE A 1 371 ? 25.875 123.616 -33.607 1.00 23.60  ? 427 PHE B C   1 
ATOM   2782 O O   . PHE A 1 371 ? 26.941 124.163 -33.302 1.00 22.99  ? 427 PHE B O   1 
ATOM   2783 C CB  . PHE A 1 371 ? 25.338 124.959 -35.711 1.00 16.94  ? 427 PHE B CB  1 
ATOM   2784 C CG  . PHE A 1 371 ? 25.345 124.943 -37.234 1.00 13.95  ? 427 PHE B CG  1 
ATOM   2785 C CD1 . PHE A 1 371 ? 26.486 124.564 -37.937 1.00 17.28  ? 427 PHE B CD1 1 
ATOM   2786 C CD2 . PHE A 1 371 ? 24.228 125.344 -37.958 1.00 14.84  ? 427 PHE B CD2 1 
ATOM   2787 C CE1 . PHE A 1 371 ? 26.519 124.563 -39.335 1.00 9.24   ? 427 PHE B CE1 1 
ATOM   2788 C CE2 . PHE A 1 371 ? 24.242 125.350 -39.358 1.00 11.79  ? 427 PHE B CE2 1 
ATOM   2789 C CZ  . PHE A 1 371 ? 25.394 124.953 -40.045 1.00 13.71  ? 427 PHE B CZ  1 
ATOM   2790 N N   . GLY A 1 372 ? 25.079 123.036 -32.708 1.00 19.60  ? 428 GLY B N   1 
ATOM   2791 C CA  . GLY A 1 372 ? 25.459 122.935 -31.315 1.00 6.40   ? 428 GLY B CA  1 
ATOM   2792 C C   . GLY A 1 372 ? 26.195 121.641 -31.018 1.00 22.65  ? 428 GLY B C   1 
ATOM   2793 O O   . GLY A 1 372 ? 26.597 121.378 -29.876 1.00 14.64  ? 428 GLY B O   1 
ATOM   2794 N N   . LEU A 1 373 ? 26.388 120.819 -32.046 1.00 23.02  ? 429 LEU B N   1 
ATOM   2795 C CA  . LEU A 1 373 ? 27.137 119.575 -31.877 1.00 15.78  ? 429 LEU B CA  1 
ATOM   2796 C C   . LEU A 1 373 ? 28.636 119.892 -31.757 1.00 16.63  ? 429 LEU B C   1 
ATOM   2797 O O   . LEU A 1 373 ? 29.215 120.543 -32.627 1.00 25.48  ? 429 LEU B O   1 
ATOM   2798 C CB  . LEU A 1 373 ? 26.831 118.615 -33.027 1.00 14.21  ? 429 LEU B CB  1 
ATOM   2799 C CG  . LEU A 1 373 ? 25.357 118.169 -33.092 1.00 15.74  ? 429 LEU B CG  1 
ATOM   2800 C CD1 . LEU A 1 373 ? 24.989 117.550 -34.442 1.00 13.74  ? 429 LEU B CD1 1 
ATOM   2801 C CD2 . LEU A 1 373 ? 25.002 117.202 -31.951 1.00 9.52   ? 429 LEU B CD2 1 
ATOM   2802 N N   . ARG A 1 374 ? 29.247 119.477 -30.649 1.00 14.13  ? 430 ARG B N   1 
ATOM   2803 C CA  . ARG A 1 374 ? 30.603 119.918 -30.325 1.00 16.69  ? 430 ARG B CA  1 
ATOM   2804 C C   . ARG A 1 374 ? 31.619 119.013 -30.974 1.00 15.13  ? 430 ARG B C   1 
ATOM   2805 O O   . ARG A 1 374 ? 32.816 119.322 -31.008 1.00 17.62  ? 430 ARG B O   1 
ATOM   2806 C CB  . ARG A 1 374 ? 30.837 119.931 -28.807 1.00 27.56  ? 430 ARG B CB  1 
ATOM   2807 C CG  . ARG A 1 374 ? 29.920 120.858 -27.997 1.00 41.57  ? 430 ARG B CG  1 
ATOM   2808 C CD  . ARG A 1 374 ? 30.151 120.710 -26.475 1.00 56.47  ? 430 ARG B CD  1 
ATOM   2809 N NE  . ARG A 1 374 ? 31.535 121.002 -26.079 1.00 61.17  ? 430 ARG B NE  1 
ATOM   2810 C CZ  . ARG A 1 374 ? 32.393 120.101 -25.599 1.00 56.47  ? 430 ARG B CZ  1 
ATOM   2811 N NH1 . ARG A 1 374 ? 32.019 118.840 -25.428 1.00 48.63  ? 430 ARG B NH1 1 
ATOM   2812 N NH2 . ARG A 1 374 ? 33.628 120.465 -25.279 1.00 59.48  ? 430 ARG B NH2 1 
ATOM   2813 N N   . ASN A 1 375 ? 31.162 117.846 -31.405 1.00 7.50   ? 431 ASN B N   1 
ATOM   2814 C CA  . ASN A 1 375 ? 32.045 116.934 -32.115 1.00 12.82  ? 431 ASN B CA  1 
ATOM   2815 C C   . ASN A 1 375 ? 31.888 116.792 -33.616 1.00 10.64  ? 431 ASN B C   1 
ATOM   2816 O O   . ASN A 1 375 ? 32.578 115.973 -34.216 1.00 13.26  ? 431 ASN B O   1 
ATOM   2817 C CB  . ASN A 1 375 ? 32.110 115.574 -31.437 1.00 25.95  ? 431 ASN B CB  1 
ATOM   2818 C CG  . ASN A 1 375 ? 33.310 115.447 -30.542 1.00 28.15  ? 431 ASN B CG  1 
ATOM   2819 O OD1 . ASN A 1 375 ? 33.182 115.352 -29.315 1.00 32.93  ? 431 ASN B OD1 1 
ATOM   2820 N ND2 . ASN A 1 375 ? 34.498 115.447 -31.150 1.00 30.00  ? 431 ASN B ND2 1 
ATOM   2821 N N   . LEU A 1 376 ? 30.985 117.558 -34.226 1.00 9.17   ? 432 LEU B N   1 
ATOM   2822 C CA  . LEU A 1 376 ? 30.675 117.332 -35.628 1.00 11.59  ? 432 LEU B CA  1 
ATOM   2823 C C   . LEU A 1 376 ? 31.839 117.887 -36.452 1.00 5.25   ? 432 LEU B C   1 
ATOM   2824 O O   . LEU A 1 376 ? 32.087 119.092 -36.451 1.00 21.50  ? 432 LEU B O   1 
ATOM   2825 C CB  . LEU A 1 376 ? 29.396 118.096 -35.969 1.00 13.18  ? 432 LEU B CB  1 
ATOM   2826 C CG  . LEU A 1 376 ? 28.749 117.989 -37.349 1.00 20.29  ? 432 LEU B CG  1 
ATOM   2827 C CD1 . LEU A 1 376 ? 28.376 116.539 -37.681 1.00 3.34   ? 432 LEU B CD1 1 
ATOM   2828 C CD2 . LEU A 1 376 ? 27.517 118.888 -37.410 1.00 3.88   ? 432 LEU B CD2 1 
ATOM   2829 N N   . THR A 1 377 ? 32.576 116.992 -37.112 1.00 10.35  ? 433 THR B N   1 
ATOM   2830 C CA  . THR A 1 377 ? 33.653 117.373 -38.043 1.00 10.82  ? 433 THR B CA  1 
ATOM   2831 C C   . THR A 1 377 ? 33.206 117.599 -39.480 1.00 9.17   ? 433 THR B C   1 
ATOM   2832 O O   . THR A 1 377 ? 33.757 118.450 -40.172 1.00 13.47  ? 433 THR B O   1 
ATOM   2833 C CB  . THR A 1 377 ? 34.872 116.405 -38.000 1.00 12.74  ? 433 THR B CB  1 
ATOM   2834 O OG1 . THR A 1 377 ? 34.449 115.078 -38.310 1.00 21.55  ? 433 THR B OG1 1 
ATOM   2835 C CG2 . THR A 1 377 ? 35.477 116.390 -36.635 1.00 9.24   ? 433 THR B CG2 1 
ATOM   2836 N N   . LYS A 1 378 ? 32.228 116.812 -39.934 1.00 10.38  ? 434 LYS B N   1 
ATOM   2837 C CA  . LYS A 1 378 ? 31.752 116.877 -41.328 1.00 7.15   ? 434 LYS B CA  1 
ATOM   2838 C C   . LYS A 1 378 ? 30.257 117.133 -41.412 1.00 3.48   ? 434 LYS B C   1 
ATOM   2839 O O   . LYS A 1 378 ? 29.455 116.344 -40.895 1.00 8.12   ? 434 LYS B O   1 
ATOM   2840 C CB  . LYS A 1 378 ? 32.048 115.570 -42.071 1.00 8.58   ? 434 LYS B CB  1 
ATOM   2841 C CG  . LYS A 1 378 ? 33.509 115.248 -42.211 1.00 14.06  ? 434 LYS B CG  1 
ATOM   2842 C CD  . LYS A 1 378 ? 33.718 113.893 -42.855 1.00 8.63   ? 434 LYS B CD  1 
ATOM   2843 C CE  . LYS A 1 378 ? 35.205 113.584 -42.963 1.00 9.81   ? 434 LYS B CE  1 
ATOM   2844 N NZ  . LYS A 1 378 ? 35.422 112.228 -43.527 1.00 14.94  ? 434 LYS B NZ  1 
ATOM   2845 N N   . LEU A 1 379 ? 29.883 118.223 -42.073 1.00 3.53   ? 435 LEU B N   1 
ATOM   2846 C CA  . LEU A 1 379 ? 28.481 118.485 -42.362 1.00 6.22   ? 435 LEU B CA  1 
ATOM   2847 C C   . LEU A 1 379 ? 28.302 118.660 -43.868 1.00 11.59  ? 435 LEU B C   1 
ATOM   2848 O O   . LEU A 1 379 ? 28.780 119.636 -44.447 1.00 19.44  ? 435 LEU B O   1 
ATOM   2849 C CB  . LEU A 1 379 ? 28.009 119.739 -41.617 1.00 3.44   ? 435 LEU B CB  1 
ATOM   2850 C CG  . LEU A 1 379 ? 26.556 120.137 -41.854 1.00 5.31   ? 435 LEU B CG  1 
ATOM   2851 C CD1 . LEU A 1 379 ? 25.656 118.916 -41.698 1.00 8.13   ? 435 LEU B CD1 1 
ATOM   2852 C CD2 . LEU A 1 379 ? 26.134 121.192 -40.873 1.00 4.78   ? 435 LEU B CD2 1 
ATOM   2853 N N   . LEU A 1 380 ? 27.618 117.716 -44.508 1.00 15.37  ? 436 LEU B N   1 
ATOM   2854 C CA  . LEU A 1 380 ? 27.482 117.748 -45.963 1.00 2.00   ? 436 LEU B CA  1 
ATOM   2855 C C   . LEU A 1 380 ? 26.027 117.656 -46.324 1.00 6.06   ? 436 LEU B C   1 
ATOM   2856 O O   . LEU A 1 380 ? 25.398 116.600 -46.178 1.00 5.75   ? 436 LEU B O   1 
ATOM   2857 C CB  . LEU A 1 380 ? 28.244 116.571 -46.566 1.00 2.00   ? 436 LEU B CB  1 
ATOM   2858 C CG  . LEU A 1 380 ? 29.680 116.457 -46.029 1.00 15.40  ? 436 LEU B CG  1 
ATOM   2859 C CD1 . LEU A 1 380 ? 30.355 115.165 -46.451 1.00 22.43  ? 436 LEU B CD1 1 
ATOM   2860 C CD2 . LEU A 1 380 ? 30.508 117.654 -46.470 1.00 14.63  ? 436 LEU B CD2 1 
ATOM   2861 N N   . LEU A 1 381 ? 25.496 118.811 -46.714 1.00 4.82   ? 437 LEU B N   1 
ATOM   2862 C CA  . LEU A 1 381 ? 24.120 119.001 -47.177 1.00 5.31   ? 437 LEU B CA  1 
ATOM   2863 C C   . LEU A 1 381 ? 23.951 119.335 -48.667 1.00 10.81  ? 437 LEU B C   1 
ATOM   2864 O O   . LEU A 1 381 ? 22.889 119.825 -49.070 1.00 5.00   ? 437 LEU B O   1 
ATOM   2865 C CB  . LEU A 1 381 ? 23.380 120.003 -46.285 1.00 5.16   ? 437 LEU B CB  1 
ATOM   2866 C CG  . LEU A 1 381 ? 23.426 119.672 -44.786 1.00 6.06   ? 437 LEU B CG  1 
ATOM   2867 C CD1 . LEU A 1 381 ? 22.760 120.761 -43.977 1.00 9.83   ? 437 LEU B CD1 1 
ATOM   2868 C CD2 . LEU A 1 381 ? 22.752 118.345 -44.525 1.00 2.00   ? 437 LEU B CD2 1 
ATOM   2869 N N   . LEU A 1 382 ? 25.019 119.224 -49.454 1.00 9.22   ? 438 LEU B N   1 
ATOM   2870 C CA  . LEU A 1 382 ? 24.982 119.724 -50.827 1.00 13.59  ? 438 LEU B CA  1 
ATOM   2871 C C   . LEU A 1 382 ? 23.906 119.098 -51.726 1.00 12.75  ? 438 LEU B C   1 
ATOM   2872 O O   . LEU A 1 382 ? 23.462 117.981 -51.511 1.00 17.37  ? 438 LEU B O   1 
ATOM   2873 C CB  . LEU A 1 382 ? 26.364 119.671 -51.509 1.00 14.48  ? 438 LEU B CB  1 
ATOM   2874 C CG  . LEU A 1 382 ? 26.981 118.315 -51.836 1.00 12.15  ? 438 LEU B CG  1 
ATOM   2875 C CD1 . LEU A 1 382 ? 26.636 117.903 -53.258 1.00 2.13   ? 438 LEU B CD1 1 
ATOM   2876 C CD2 . LEU A 1 382 ? 28.484 118.336 -51.615 1.00 6.13   ? 438 LEU B CD2 1 
ATOM   2877 N N   . SER A 1 383 ? 23.489 119.861 -52.727 1.00 8.14   ? 439 SER B N   1 
ATOM   2878 C CA  . SER A 1 383 ? 22.453 119.449 -53.666 1.00 10.50  ? 439 SER B CA  1 
ATOM   2879 C C   . SER A 1 383 ? 21.162 118.993 -52.999 1.00 7.15   ? 439 SER B C   1 
ATOM   2880 O O   . SER A 1 383 ? 20.822 117.812 -52.993 1.00 9.55   ? 439 SER B O   1 
ATOM   2881 C CB  . SER A 1 383 ? 22.958 118.416 -54.661 1.00 9.20   ? 439 SER B CB  1 
ATOM   2882 O OG  . SER A 1 383 ? 21.978 118.209 -55.663 1.00 15.09  ? 439 SER B OG  1 
ATOM   2883 N N   . ASN A 1 384 ? 20.451 119.960 -52.440 1.00 4.68   ? 440 ASN B N   1 
ATOM   2884 C CA  . ASN A 1 384 ? 19.109 119.745 -51.917 1.00 7.83   ? 440 ASN B CA  1 
ATOM   2885 C C   . ASN A 1 384 ? 18.250 120.956 -52.322 1.00 8.57   ? 440 ASN B C   1 
ATOM   2886 O O   . ASN A 1 384 ? 18.600 121.711 -53.227 1.00 6.32   ? 440 ASN B O   1 
ATOM   2887 C CB  . ASN A 1 384 ? 19.140 119.556 -50.390 1.00 9.57   ? 440 ASN B CB  1 
ATOM   2888 C CG  . ASN A 1 384 ? 19.511 118.119 -49.967 1.00 12.48  ? 440 ASN B CG  1 
ATOM   2889 O OD1 . ASN A 1 384 ? 18.693 117.221 -50.072 1.00 10.75  ? 440 ASN B OD1 1 
ATOM   2890 N ND2 . ASN A 1 384 ? 20.728 117.919 -49.463 1.00 2.00   ? 440 ASN B ND2 1 
ATOM   2891 N N   . ASP A 1 385 ? 17.074 121.079 -51.744 1.00 12.28  ? 441 ASP B N   1 
ATOM   2892 C CA  . ASP A 1 385 ? 16.265 122.285 -51.885 1.00 8.72   ? 441 ASP B CA  1 
ATOM   2893 C C   . ASP A 1 385 ? 16.299 123.229 -50.669 1.00 5.11   ? 441 ASP B C   1 
ATOM   2894 O O   . ASP A 1 385 ? 15.332 123.942 -50.423 1.00 6.70   ? 441 ASP B O   1 
ATOM   2895 C CB  . ASP A 1 385 ? 14.854 122.015 -52.420 1.00 15.00  ? 441 ASP B CB  1 
ATOM   2896 C CG  . ASP A 1 385 ? 14.228 123.257 -53.055 1.00 28.52  ? 441 ASP B CG  1 
ATOM   2897 O OD1 . ASP A 1 385 ? 14.979 124.065 -53.653 1.00 30.73  ? 441 ASP B OD1 1 
ATOM   2898 O OD2 . ASP A 1 385 ? 12.993 123.440 -52.941 1.00 34.65  ? 441 ASP B OD2 1 
ATOM   2899 N N   . LEU A 1 386 ? 17.307 123.091 -49.815 1.00 5.48   ? 442 LEU B N   1 
ATOM   2900 C CA  . LEU A 1 386 ? 17.393 123.876 -48.569 1.00 2.02   ? 442 LEU B CA  1 
ATOM   2901 C C   . LEU A 1 386 ? 17.331 125.377 -48.808 1.00 2.37   ? 442 LEU B C   1 
ATOM   2902 O O   . LEU A 1 386 ? 17.774 125.858 -49.845 1.00 7.07   ? 442 LEU B O   1 
ATOM   2903 C CB  . LEU A 1 386 ? 18.686 123.536 -47.818 1.00 2.00   ? 442 LEU B CB  1 
ATOM   2904 C CG  . LEU A 1 386 ? 18.818 122.129 -47.233 1.00 2.00   ? 442 LEU B CG  1 
ATOM   2905 C CD1 . LEU A 1 386 ? 20.223 121.906 -46.710 1.00 2.00   ? 442 LEU B CD1 1 
ATOM   2906 C CD2 . LEU A 1 386 ? 17.784 121.907 -46.128 1.00 2.00   ? 442 LEU B CD2 1 
ATOM   2907 N N   . SER A 1 387 ? 16.766 126.119 -47.863 1.00 2.72   ? 443 SER B N   1 
ATOM   2908 C CA  . SER A 1 387 ? 16.764 127.587 -47.941 1.00 7.73   ? 443 SER B CA  1 
ATOM   2909 C C   . SER A 1 387 ? 16.781 128.263 -46.574 1.00 10.40  ? 443 SER B C   1 
ATOM   2910 O O   . SER A 1 387 ? 16.983 127.628 -45.543 1.00 12.23  ? 443 SER B O   1 
ATOM   2911 C CB  . SER A 1 387 ? 15.574 128.107 -48.749 1.00 3.22   ? 443 SER B CB  1 
ATOM   2912 O OG  . SER A 1 387 ? 14.353 127.805 -48.105 1.00 4.83   ? 443 SER B OG  1 
ATOM   2913 N N   . GLY A 1 388 ? 16.562 129.569 -46.570 1.00 12.46  ? 444 GLY B N   1 
ATOM   2914 C CA  . GLY A 1 388 ? 16.659 130.316 -45.336 1.00 7.00   ? 444 GLY B CA  1 
ATOM   2915 C C   . GLY A 1 388 ? 18.089 130.744 -45.090 1.00 15.03  ? 444 GLY B C   1 
ATOM   2916 O O   . GLY A 1 388 ? 18.955 130.621 -45.978 1.00 17.86  ? 444 GLY B O   1 
ATOM   2917 N N   . PHE A 1 389 ? 18.330 131.269 -43.891 1.00 13.59  ? 445 PHE B N   1 
ATOM   2918 C CA  . PHE A 1 389 ? 19.639 131.780 -43.505 1.00 5.76   ? 445 PHE B CA  1 
ATOM   2919 C C   . PHE A 1 389 ? 20.571 130.688 -43.046 1.00 10.00  ? 445 PHE B C   1 
ATOM   2920 O O   . PHE A 1 389 ? 20.129 129.632 -42.607 1.00 19.49  ? 445 PHE B O   1 
ATOM   2921 C CB  . PHE A 1 389 ? 19.501 132.813 -42.389 1.00 6.44   ? 445 PHE B CB  1 
ATOM   2922 C CG  . PHE A 1 389 ? 18.717 134.033 -42.781 1.00 6.79   ? 445 PHE B CG  1 
ATOM   2923 C CD1 . PHE A 1 389 ? 18.805 134.552 -44.068 1.00 17.97  ? 445 PHE B CD1 1 
ATOM   2924 C CD2 . PHE A 1 389 ? 17.870 134.654 -41.865 1.00 15.95  ? 445 PHE B CD2 1 
ATOM   2925 C CE1 . PHE A 1 389 ? 18.072 135.686 -44.436 1.00 22.38  ? 445 PHE B CE1 1 
ATOM   2926 C CE2 . PHE A 1 389 ? 17.133 135.779 -42.213 1.00 7.54   ? 445 PHE B CE2 1 
ATOM   2927 C CZ  . PHE A 1 389 ? 17.240 136.303 -43.504 1.00 24.55  ? 445 PHE B CZ  1 
ATOM   2928 N N   . ILE A 1 390 ? 21.867 130.947 -43.153 1.00 10.61  ? 446 ILE B N   1 
ATOM   2929 C CA  . ILE A 1 390 ? 22.835 130.222 -42.347 1.00 12.78  ? 446 ILE B CA  1 
ATOM   2930 C C   . ILE A 1 390 ? 22.726 130.819 -40.950 1.00 13.64  ? 446 ILE B C   1 
ATOM   2931 O O   . ILE A 1 390 ? 22.876 132.022 -40.770 1.00 24.21  ? 446 ILE B O   1 
ATOM   2932 C CB  . ILE A 1 390 ? 24.268 130.352 -42.886 1.00 6.12   ? 446 ILE B CB  1 
ATOM   2933 C CG1 . ILE A 1 390 ? 24.336 129.835 -44.327 1.00 5.61   ? 446 ILE B CG1 1 
ATOM   2934 C CG2 . ILE A 1 390 ? 25.226 129.534 -42.047 1.00 7.08   ? 446 ILE B CG2 1 
ATOM   2935 C CD1 . ILE A 1 390 ? 25.681 129.999 -44.977 1.00 5.86   ? 446 ILE B CD1 1 
ATOM   2936 N N   . PRO A 1 391 ? 22.412 129.980 -39.961 1.00 11.12  ? 447 PRO B N   1 
ATOM   2937 C CA  . PRO A 1 391 ? 22.187 130.483 -38.601 1.00 6.79   ? 447 PRO B CA  1 
ATOM   2938 C C   . PRO A 1 391 ? 23.491 130.965 -38.015 1.00 14.66  ? 447 PRO B C   1 
ATOM   2939 O O   . PRO A 1 391 ? 24.531 130.364 -38.278 1.00 12.54  ? 447 PRO B O   1 
ATOM   2940 C CB  . PRO A 1 391 ? 21.693 129.242 -37.832 1.00 6.38   ? 447 PRO B CB  1 
ATOM   2941 C CG  . PRO A 1 391 ? 21.284 128.247 -38.891 1.00 11.56  ? 447 PRO B CG  1 
ATOM   2942 C CD  . PRO A 1 391 ? 22.153 128.534 -40.086 1.00 10.29  ? 447 PRO B CD  1 
ATOM   2943 N N   . PRO A 1 392 ? 23.443 132.039 -37.222 1.00 23.16  ? 448 PRO B N   1 
ATOM   2944 C CA  . PRO A 1 392 ? 24.619 132.538 -36.478 1.00 27.00  ? 448 PRO B CA  1 
ATOM   2945 C C   . PRO A 1 392 ? 25.225 131.464 -35.563 1.00 15.86  ? 448 PRO B C   1 
ATOM   2946 O O   . PRO A 1 392 ? 26.436 131.407 -35.318 1.00 30.70  ? 448 PRO B O   1 
ATOM   2947 C CB  . PRO A 1 392 ? 24.060 133.719 -35.667 1.00 29.49  ? 448 PRO B CB  1 
ATOM   2948 C CG  . PRO A 1 392 ? 22.544 133.563 -35.711 1.00 26.96  ? 448 PRO B CG  1 
ATOM   2949 C CD  . PRO A 1 392 ? 22.235 132.850 -36.994 1.00 22.40  ? 448 PRO B CD  1 
ATOM   2950 N N   . ASP A 1 393 ? 24.384 130.536 -35.136 1.00 17.94  ? 449 ASP B N   1 
ATOM   2951 C CA  . ASP A 1 393 ? 24.839 129.421 -34.307 1.00 12.63  ? 449 ASP B CA  1 
ATOM   2952 C C   . ASP A 1 393 ? 25.922 128.589 -34.967 1.00 9.07   ? 449 ASP B C   1 
ATOM   2953 O O   . ASP A 1 393 ? 26.507 127.739 -34.314 1.00 10.36  ? 449 ASP B O   1 
ATOM   2954 C CB  . ASP A 1 393 ? 23.677 128.504 -33.980 1.00 10.75  ? 449 ASP B CB  1 
ATOM   2955 C CG  . ASP A 1 393 ? 22.475 129.263 -33.533 1.00 21.22  ? 449 ASP B CG  1 
ATOM   2956 O OD1 . ASP A 1 393 ? 21.894 129.954 -34.411 1.00 19.95  ? 449 ASP B OD1 1 
ATOM   2957 O OD2 . ASP A 1 393 ? 22.138 129.182 -32.313 1.00 16.21  ? 449 ASP B OD2 1 
ATOM   2958 N N   . ILE A 1 394 ? 26.163 128.807 -36.259 1.00 7.55   ? 450 ILE B N   1 
ATOM   2959 C CA  . ILE A 1 394 ? 27.225 128.096 -36.953 1.00 7.35   ? 450 ILE B CA  1 
ATOM   2960 C C   . ILE A 1 394 ? 28.534 128.197 -36.157 1.00 16.29  ? 450 ILE B C   1 
ATOM   2961 O O   . ILE A 1 394 ? 29.308 127.237 -36.110 1.00 22.99  ? 450 ILE B O   1 
ATOM   2962 C CB  . ILE A 1 394 ? 27.382 128.575 -38.431 1.00 8.65   ? 450 ILE B CB  1 
ATOM   2963 C CG1 . ILE A 1 394 ? 28.439 127.761 -39.177 1.00 14.45  ? 450 ILE B CG1 1 
ATOM   2964 C CG2 . ILE A 1 394 ? 27.711 130.050 -38.511 1.00 7.90   ? 450 ILE B CG2 1 
ATOM   2965 C CD1 . ILE A 1 394 ? 28.373 127.930 -40.710 1.00 14.86  ? 450 ILE B CD1 1 
ATOM   2966 N N   . GLY A 1 395 ? 28.749 129.324 -35.477 1.00 14.04  ? 451 GLY B N   1 
ATOM   2967 C CA  . GLY A 1 395 ? 29.965 129.484 -34.679 1.00 17.58  ? 451 GLY B CA  1 
ATOM   2968 C C   . GLY A 1 395 ? 30.093 128.649 -33.401 1.00 19.28  ? 451 GLY B C   1 
ATOM   2969 O O   . GLY A 1 395 ? 31.168 128.571 -32.813 1.00 21.25  ? 451 GLY B O   1 
ATOM   2970 N N   . ASN A 1 396 ? 28.994 128.046 -32.958 1.00 17.58  ? 452 ASN B N   1 
ATOM   2971 C CA  . ASN A 1 396 ? 28.992 127.150 -31.804 1.00 18.07  ? 452 ASN B CA  1 
ATOM   2972 C C   . ASN A 1 396 ? 29.612 125.784 -32.116 1.00 18.63  ? 452 ASN B C   1 
ATOM   2973 O O   . ASN A 1 396 ? 29.866 125.011 -31.198 1.00 21.92  ? 452 ASN B O   1 
ATOM   2974 C CB  . ASN A 1 396 ? 27.555 126.888 -31.313 1.00 8.52   ? 452 ASN B CB  1 
ATOM   2975 C CG  . ASN A 1 396 ? 26.890 128.111 -30.694 1.00 10.93  ? 452 ASN B CG  1 
ATOM   2976 O OD1 . ASN A 1 396 ? 27.164 129.247 -31.077 1.00 14.06  ? 452 ASN B OD1 1 
ATOM   2977 N ND2 . ASN A 1 396 ? 26.006 127.868 -29.716 1.00 12.96  ? 452 ASN B ND2 1 
ATOM   2978 N N   . CYS A 1 397 ? 29.851 125.479 -33.394 1.00 18.20  ? 453 CYS B N   1 
ATOM   2979 C CA  . CYS A 1 397 ? 30.119 124.096 -33.791 1.00 17.06  ? 453 CYS B CA  1 
ATOM   2980 C C   . CYS A 1 397 ? 31.615 123.984 -33.900 1.00 22.08  ? 453 CYS B C   1 
ATOM   2981 O O   . CYS A 1 397 ? 32.213 124.075 -34.996 1.00 14.66  ? 453 CYS B O   1 
ATOM   2982 C CB  . CYS A 1 397 ? 29.492 123.854 -35.181 1.00 10.70  ? 453 CYS B CB  1 
ATOM   2983 S SG  . CYS A 1 397 ? 29.363 122.130 -35.788 1.00 19.22  ? 453 CYS B SG  1 
ATOM   2984 N N   . THR A 1 398 ? 32.190 123.574 -32.784 1.00 19.60  ? 454 THR B N   1 
ATOM   2985 C CA  . THR A 1 398 ? 33.547 123.981 -32.474 1.00 23.06  ? 454 THR B CA  1 
ATOM   2986 C C   . THR A 1 398 ? 34.570 123.189 -33.263 1.00 19.58  ? 454 THR B C   1 
ATOM   2987 O O   . THR A 1 398 ? 35.623 123.694 -33.606 1.00 9.45   ? 454 THR B O   1 
ATOM   2988 C CB  . THR A 1 398 ? 33.789 123.930 -30.945 1.00 24.01  ? 454 THR B CB  1 
ATOM   2989 O OG1 . THR A 1 398 ? 33.278 125.137 -30.366 1.00 29.55  ? 454 THR B OG1 1 
ATOM   2990 C CG2 . THR A 1 398 ? 35.274 123.810 -30.606 1.00 18.97  ? 454 THR B CG2 1 
ATOM   2991 N N   . ASN A 1 399 ? 34.244 121.936 -33.537 1.00 14.17  ? 455 ASN B N   1 
ATOM   2992 C CA  . ASN A 1 399 ? 35.153 121.059 -34.253 1.00 9.58   ? 455 ASN B CA  1 
ATOM   2993 C C   . ASN A 1 399 ? 34.885 120.952 -35.751 1.00 16.11  ? 455 ASN B C   1 
ATOM   2994 O O   . ASN A 1 399 ? 35.467 120.088 -36.400 1.00 10.62  ? 455 ASN B O   1 
ATOM   2995 C CB  . ASN A 1 399 ? 35.211 119.671 -33.601 1.00 9.20   ? 455 ASN B CB  1 
ATOM   2996 C CG  . ASN A 1 399 ? 36.118 119.645 -32.374 1.00 24.54  ? 455 ASN B CG  1 
ATOM   2997 O OD1 . ASN A 1 399 ? 37.340 119.761 -32.494 1.00 30.17  ? 455 ASN B OD1 1 
ATOM   2998 N ND2 . ASN A 1 399 ? 35.522 119.510 -31.190 1.00 15.97  ? 455 ASN B ND2 1 
ATOM   2999 N N   . LEU A 1 400 ? 33.973 121.770 -36.289 1.00 7.41   ? 456 LEU B N   1 
ATOM   3000 C CA  . LEU A 1 400 ? 33.681 121.702 -37.726 1.00 6.94   ? 456 LEU B CA  1 
ATOM   3001 C C   . LEU A 1 400 ? 34.938 121.766 -38.585 1.00 7.33   ? 456 LEU B C   1 
ATOM   3002 O O   . LEU A 1 400 ? 35.734 122.683 -38.480 1.00 13.68  ? 456 LEU B O   1 
ATOM   3003 C CB  . LEU A 1 400 ? 32.744 122.827 -38.152 1.00 6.86   ? 456 LEU B CB  1 
ATOM   3004 C CG  . LEU A 1 400 ? 31.976 122.500 -39.426 1.00 12.29  ? 456 LEU B CG  1 
ATOM   3005 C CD1 . LEU A 1 400 ? 31.341 121.090 -39.350 1.00 5.47   ? 456 LEU B CD1 1 
ATOM   3006 C CD2 . LEU A 1 400 ? 30.936 123.566 -39.693 1.00 6.10   ? 456 LEU B CD2 1 
ATOM   3007 N N   . TYR A 1 401 ? 35.076 120.791 -39.467 1.00 20.02  ? 457 TYR B N   1 
ATOM   3008 C CA  . TYR A 1 401 ? 36.248 120.658 -40.328 1.00 16.07  ? 457 TYR B CA  1 
ATOM   3009 C C   . TYR A 1 401 ? 35.892 120.874 -41.803 1.00 16.70  ? 457 TYR B C   1 
ATOM   3010 O O   . TYR A 1 401 ? 36.442 121.755 -42.468 1.00 24.23  ? 457 TYR B O   1 
ATOM   3011 C CB  . TYR A 1 401 ? 36.879 119.279 -40.130 1.00 14.70  ? 457 TYR B CB  1 
ATOM   3012 C CG  . TYR A 1 401 ? 38.187 119.108 -40.843 1.00 15.73  ? 457 TYR B CG  1 
ATOM   3013 C CD1 . TYR A 1 401 ? 39.371 119.572 -40.276 1.00 17.02  ? 457 TYR B CD1 1 
ATOM   3014 C CD2 . TYR A 1 401 ? 38.246 118.492 -42.078 1.00 7.41   ? 457 TYR B CD2 1 
ATOM   3015 C CE1 . TYR A 1 401 ? 40.586 119.420 -40.930 1.00 13.15  ? 457 TYR B CE1 1 
ATOM   3016 C CE2 . TYR A 1 401 ? 39.448 118.347 -42.735 1.00 11.54  ? 457 TYR B CE2 1 
ATOM   3017 C CZ  . TYR A 1 401 ? 40.610 118.812 -42.159 1.00 12.05  ? 457 TYR B CZ  1 
ATOM   3018 O OH  . TYR A 1 401 ? 41.796 118.654 -42.810 1.00 20.02  ? 457 TYR B OH  1 
ATOM   3019 N N   . ARG A 1 402 ? 35.001 120.028 -42.315 1.00 11.19  ? 458 ARG B N   1 
ATOM   3020 C CA  . ARG A 1 402 ? 34.527 120.121 -43.694 1.00 5.73   ? 458 ARG B CA  1 
ATOM   3021 C C   . ARG A 1 402 ? 33.026 120.474 -43.737 1.00 8.92   ? 458 ARG B C   1 
ATOM   3022 O O   . ARG A 1 402 ? 32.176 119.758 -43.179 1.00 10.53  ? 458 ARG B O   1 
ATOM   3023 C CB  . ARG A 1 402 ? 34.827 118.801 -44.408 1.00 6.13   ? 458 ARG B CB  1 
ATOM   3024 C CG  . ARG A 1 402 ? 34.351 118.670 -45.850 1.00 4.98   ? 458 ARG B CG  1 
ATOM   3025 C CD  . ARG A 1 402 ? 34.715 117.268 -46.353 1.00 9.95   ? 458 ARG B CD  1 
ATOM   3026 N NE  . ARG A 1 402 ? 34.438 117.081 -47.769 1.00 14.49  ? 458 ARG B NE  1 
ATOM   3027 C CZ  . ARG A 1 402 ? 35.197 117.567 -48.746 1.00 15.60  ? 458 ARG B CZ  1 
ATOM   3028 N NH1 . ARG A 1 402 ? 34.857 117.352 -50.011 1.00 12.08  ? 458 ARG B NH1 1 
ATOM   3029 N NH2 . ARG A 1 402 ? 36.288 118.275 -48.453 1.00 11.93  ? 458 ARG B NH2 1 
ATOM   3030 N N   . LEU A 1 403 ? 32.711 121.601 -44.369 1.00 6.40   ? 459 LEU B N   1 
ATOM   3031 C CA  . LEU A 1 403 ? 31.335 122.077 -44.467 1.00 9.00   ? 459 LEU B CA  1 
ATOM   3032 C C   . LEU A 1 403 ? 30.915 122.252 -45.931 1.00 16.18  ? 459 LEU B C   1 
ATOM   3033 O O   . LEU A 1 403 ? 31.502 123.062 -46.657 1.00 20.34  ? 459 LEU B O   1 
ATOM   3034 C CB  . LEU A 1 403 ? 31.201 123.419 -43.759 1.00 5.35   ? 459 LEU B CB  1 
ATOM   3035 C CG  . LEU A 1 403 ? 29.838 124.113 -43.962 1.00 16.21  ? 459 LEU B CG  1 
ATOM   3036 C CD1 . LEU A 1 403 ? 28.689 123.298 -43.371 1.00 4.51   ? 459 LEU B CD1 1 
ATOM   3037 C CD2 . LEU A 1 403 ? 29.835 125.529 -43.385 1.00 10.42  ? 459 LEU B CD2 1 
ATOM   3038 N N   . ARG A 1 404 ? 29.905 121.509 -46.378 1.00 13.90  ? 460 ARG B N   1 
ATOM   3039 C CA  . ARG A 1 404 ? 29.426 121.718 -47.738 1.00 14.61  ? 460 ARG B CA  1 
ATOM   3040 C C   . ARG A 1 404 ? 27.928 121.947 -47.781 1.00 17.05  ? 460 ARG B C   1 
ATOM   3041 O O   . ARG A 1 404 ? 27.138 121.041 -47.470 1.00 11.89  ? 460 ARG B O   1 
ATOM   3042 C CB  . ARG A 1 404 ? 29.815 120.549 -48.624 1.00 10.84  ? 460 ARG B CB  1 
ATOM   3043 C CG  . ARG A 1 404 ? 31.317 120.323 -48.688 1.00 8.80   ? 460 ARG B CG  1 
ATOM   3044 C CD  . ARG A 1 404 ? 31.697 119.414 -49.827 1.00 3.54   ? 460 ARG B CD  1 
ATOM   3045 N NE  . ARG A 1 404 ? 31.548 120.127 -51.088 1.00 27.26  ? 460 ARG B NE  1 
ATOM   3046 C CZ  . ARG A 1 404 ? 31.904 119.657 -52.279 1.00 20.31  ? 460 ARG B CZ  1 
ATOM   3047 N NH1 . ARG A 1 404 ? 32.444 118.447 -52.401 1.00 3.45   ? 460 ARG B NH1 1 
ATOM   3048 N NH2 . ARG A 1 404 ? 31.722 120.419 -53.346 1.00 7.10   ? 460 ARG B NH2 1 
ATOM   3049 N N   . LEU A 1 405 ? 27.563 123.193 -48.096 1.00 12.30  ? 461 LEU B N   1 
ATOM   3050 C CA  . LEU A 1 405 ? 26.164 123.610 -48.276 1.00 9.05   ? 461 LEU B CA  1 
ATOM   3051 C C   . LEU A 1 405 ? 25.752 123.825 -49.730 1.00 3.78   ? 461 LEU B C   1 
ATOM   3052 O O   . LEU A 1 405 ? 24.656 124.278 -50.016 1.00 9.74   ? 461 LEU B O   1 
ATOM   3053 C CB  . LEU A 1 405 ? 25.843 124.826 -47.416 1.00 3.48   ? 461 LEU B CB  1 
ATOM   3054 C CG  . LEU A 1 405 ? 26.259 124.604 -45.959 1.00 12.57  ? 461 LEU B CG  1 
ATOM   3055 C CD1 . LEU A 1 405 ? 25.779 125.738 -45.059 1.00 4.22   ? 461 LEU B CD1 1 
ATOM   3056 C CD2 . LEU A 1 405 ? 25.763 123.241 -45.438 1.00 3.25   ? 461 LEU B CD2 1 
ATOM   3057 N N   . ASN A 1 406 ? 26.659 123.537 -50.646 1.00 5.09   ? 462 ASN B N   1 
ATOM   3058 C CA  . ASN A 1 406 ? 26.522 124.000 -52.019 1.00 5.47   ? 462 ASN B CA  1 
ATOM   3059 C C   . ASN A 1 406 ? 25.391 123.337 -52.827 1.00 10.69  ? 462 ASN B C   1 
ATOM   3060 O O   . ASN A 1 406 ? 25.055 122.180 -52.609 1.00 11.74  ? 462 ASN B O   1 
ATOM   3061 C CB  . ASN A 1 406 ? 27.880 123.925 -52.738 1.00 3.05   ? 462 ASN B CB  1 
ATOM   3062 C CG  . ASN A 1 406 ? 28.443 122.521 -52.780 1.00 15.22  ? 462 ASN B CG  1 
ATOM   3063 O OD1 . ASN A 1 406 ? 28.805 121.957 -51.752 1.00 16.25  ? 462 ASN B OD1 1 
ATOM   3064 N ND2 . ASN A 1 406 ? 28.549 121.956 -53.981 1.00 11.54  ? 462 ASN B ND2 1 
ATOM   3065 N N   . GLY A 1 407 ? 24.807 124.077 -53.768 1.00 8.82   ? 463 GLY B N   1 
ATOM   3066 C CA  . GLY A 1 407 ? 23.707 123.558 -54.559 1.00 6.47   ? 463 GLY B CA  1 
ATOM   3067 C C   . GLY A 1 407 ? 22.393 123.561 -53.812 1.00 12.41  ? 463 GLY B C   1 
ATOM   3068 O O   . GLY A 1 407 ? 21.651 122.567 -53.809 1.00 15.33  ? 463 GLY B O   1 
ATOM   3069 N N   . ASN A 1 408 ? 22.107 124.689 -53.169 1.00 7.58   ? 464 ASN B N   1 
ATOM   3070 C CA  . ASN A 1 408 ? 20.839 124.895 -52.473 1.00 6.03   ? 464 ASN B CA  1 
ATOM   3071 C C   . ASN A 1 408 ? 20.271 126.284 -52.804 1.00 16.23  ? 464 ASN B C   1 
ATOM   3072 O O   . ASN A 1 408 ? 20.701 126.930 -53.764 1.00 21.56  ? 464 ASN B O   1 
ATOM   3073 C CB  . ASN A 1 408 ? 21.015 124.734 -50.969 1.00 8.87   ? 464 ASN B CB  1 
ATOM   3074 C CG  . ASN A 1 408 ? 21.139 123.290 -50.550 1.00 15.04  ? 464 ASN B CG  1 
ATOM   3075 O OD1 . ASN A 1 408 ? 20.161 122.553 -50.601 1.00 19.03  ? 464 ASN B OD1 1 
ATOM   3076 N ND2 . ASN A 1 408 ? 22.341 122.874 -50.121 1.00 11.48  ? 464 ASN B ND2 1 
ATOM   3077 N N   . ARG A 1 409 ? 19.240 126.680 -52.076 1.00 2.25   ? 465 ARG B N   1 
ATOM   3078 C CA  . ARG A 1 409 ? 18.667 128.034 -52.115 1.00 4.90   ? 465 ARG B CA  1 
ATOM   3079 C C   . ARG A 1 409 ? 19.016 128.995 -50.978 1.00 13.96  ? 465 ARG B C   1 
ATOM   3080 O O   . ARG A 1 409 ? 18.225 129.897 -50.694 1.00 21.76  ? 465 ARG B O   1 
ATOM   3081 C CB  . ARG A 1 409 ? 17.164 128.022 -52.373 1.00 10.25  ? 465 ARG B CB  1 
ATOM   3082 C CG  . ARG A 1 409 ? 16.827 127.836 -53.822 1.00 5.51   ? 465 ARG B CG  1 
ATOM   3083 C CD  . ARG A 1 409 ? 15.338 128.051 -54.067 1.00 14.54  ? 465 ARG B CD  1 
ATOM   3084 N NE  . ARG A 1 409 ? 14.467 127.004 -53.533 1.00 15.91  ? 465 ARG B NE  1 
ATOM   3085 C CZ  . ARG A 1 409 ? 13.552 127.194 -52.576 1.00 18.04  ? 465 ARG B CZ  1 
ATOM   3086 N NH1 . ARG A 1 409 ? 13.390 128.392 -52.019 1.00 13.60  ? 465 ARG B NH1 1 
ATOM   3087 N NH2 . ARG A 1 409 ? 12.792 126.177 -52.169 1.00 12.41  ? 465 ARG B NH2 1 
ATOM   3088 N N   . LEU A 1 410 ? 20.070 128.715 -50.215 1.00 10.70  ? 466 LEU B N   1 
ATOM   3089 C CA  . LEU A 1 410 ? 20.391 129.544 -49.037 1.00 7.05   ? 466 LEU B CA  1 
ATOM   3090 C C   . LEU A 1 410 ? 20.417 131.046 -49.332 1.00 12.02  ? 466 LEU B C   1 
ATOM   3091 O O   . LEU A 1 410 ? 20.960 131.470 -50.357 1.00 8.82   ? 466 LEU B O   1 
ATOM   3092 C CB  . LEU A 1 410 ? 21.709 129.108 -48.418 1.00 4.00   ? 466 LEU B CB  1 
ATOM   3093 C CG  . LEU A 1 410 ? 21.737 127.631 -48.080 1.00 3.49   ? 466 LEU B CG  1 
ATOM   3094 C CD1 . LEU A 1 410 ? 23.124 127.247 -47.641 1.00 11.56  ? 466 LEU B CD1 1 
ATOM   3095 C CD2 . LEU A 1 410 ? 20.699 127.284 -47.007 1.00 3.39   ? 466 LEU B CD2 1 
ATOM   3096 N N   . ALA A 1 411 ? 19.813 131.837 -48.438 1.00 17.66  ? 467 ALA B N   1 
ATOM   3097 C CA  . ALA A 1 411 ? 19.689 133.295 -48.615 1.00 13.56  ? 467 ALA B CA  1 
ATOM   3098 C C   . ALA A 1 411 ? 20.357 134.066 -47.475 1.00 8.85   ? 467 ALA B C   1 
ATOM   3099 O O   . ALA A 1 411 ? 20.887 133.461 -46.538 1.00 10.98  ? 467 ALA B O   1 
ATOM   3100 C CB  . ALA A 1 411 ? 18.224 133.696 -48.727 1.00 5.33   ? 467 ALA B CB  1 
ATOM   3101 N N   . GLY A 1 412 ? 20.326 135.393 -47.543 1.00 6.56   ? 468 GLY B N   1 
ATOM   3102 C CA  . GLY A 1 412 ? 20.966 136.216 -46.525 1.00 7.24   ? 468 GLY B CA  1 
ATOM   3103 C C   . GLY A 1 412 ? 22.485 136.273 -46.648 1.00 11.84  ? 468 GLY B C   1 
ATOM   3104 O O   . GLY A 1 412 ? 23.049 135.900 -47.668 1.00 13.48  ? 468 GLY B O   1 
ATOM   3105 N N   . SER A 1 413 ? 23.168 136.715 -45.601 1.00 9.65   ? 469 SER B N   1 
ATOM   3106 C CA  . SER A 1 413 ? 24.619 136.844 -45.687 1.00 10.86  ? 469 SER B CA  1 
ATOM   3107 C C   . SER A 1 413 ? 25.382 135.842 -44.816 1.00 13.85  ? 469 SER B C   1 
ATOM   3108 O O   . SER A 1 413 ? 24.828 135.255 -43.877 1.00 15.20  ? 469 SER B O   1 
ATOM   3109 C CB  . SER A 1 413 ? 25.054 138.282 -45.409 1.00 9.63   ? 469 SER B CB  1 
ATOM   3110 O OG  . SER A 1 413 ? 24.310 138.820 -44.344 1.00 14.01  ? 469 SER B OG  1 
ATOM   3111 N N   . ILE A 1 414 ? 26.630 135.582 -45.185 1.00 11.70  ? 470 ILE B N   1 
ATOM   3112 C CA  . ILE A 1 414 ? 27.433 134.621 -44.452 1.00 8.40   ? 470 ILE B CA  1 
ATOM   3113 C C   . ILE A 1 414 ? 27.697 135.220 -43.081 1.00 10.81  ? 470 ILE B C   1 
ATOM   3114 O O   . ILE A 1 414 ? 28.322 136.277 -42.974 1.00 9.73   ? 470 ILE B O   1 
ATOM   3115 C CB  . ILE A 1 414 ? 28.763 134.339 -45.167 1.00 16.65  ? 470 ILE B CB  1 
ATOM   3116 C CG1 . ILE A 1 414 ? 28.510 133.841 -46.595 1.00 17.90  ? 470 ILE B CG1 1 
ATOM   3117 C CG2 . ILE A 1 414 ? 29.603 133.336 -44.375 1.00 10.01  ? 470 ILE B CG2 1 
ATOM   3118 C CD1 . ILE A 1 414 ? 29.752 133.785 -47.438 1.00 8.13   ? 470 ILE B CD1 1 
ATOM   3119 N N   . PRO A 1 415 ? 27.196 134.565 -42.025 1.00 12.89  ? 471 PRO B N   1 
ATOM   3120 C CA  . PRO A 1 415 ? 27.255 135.149 -40.683 1.00 10.38  ? 471 PRO B CA  1 
ATOM   3121 C C   . PRO A 1 415 ? 28.692 135.307 -40.187 1.00 13.29  ? 471 PRO B C   1 
ATOM   3122 O O   . PRO A 1 415 ? 29.535 134.466 -40.488 1.00 17.31  ? 471 PRO B O   1 
ATOM   3123 C CB  . PRO A 1 415 ? 26.483 134.134 -39.834 1.00 13.27  ? 471 PRO B CB  1 
ATOM   3124 C CG  . PRO A 1 415 ? 26.528 132.869 -40.606 1.00 12.03  ? 471 PRO B CG  1 
ATOM   3125 C CD  . PRO A 1 415 ? 26.496 133.272 -42.035 1.00 12.18  ? 471 PRO B CD  1 
ATOM   3126 N N   . SER A 1 416 ? 28.968 136.383 -39.456 1.00 14.37  ? 472 SER B N   1 
ATOM   3127 C CA  . SER A 1 416 ? 30.314 136.663 -38.954 1.00 15.45  ? 472 SER B CA  1 
ATOM   3128 C C   . SER A 1 416 ? 30.837 135.566 -38.045 1.00 19.54  ? 472 SER B C   1 
ATOM   3129 O O   . SER A 1 416 ? 32.046 135.362 -37.922 1.00 24.99  ? 472 SER B O   1 
ATOM   3130 C CB  . SER A 1 416 ? 30.324 137.970 -38.168 1.00 19.79  ? 472 SER B CB  1 
ATOM   3131 O OG  . SER A 1 416 ? 30.309 139.080 -39.042 1.00 40.35  ? 472 SER B OG  1 
ATOM   3132 N N   . GLU A 1 417 ? 29.927 134.859 -37.391 1.00 16.76  ? 473 GLU B N   1 
ATOM   3133 C CA  . GLU A 1 417 ? 30.353 133.930 -36.354 1.00 16.97  ? 473 GLU B CA  1 
ATOM   3134 C C   . GLU A 1 417 ? 31.038 132.698 -36.937 1.00 19.04  ? 473 GLU B C   1 
ATOM   3135 O O   . GLU A 1 417 ? 31.601 131.899 -36.198 1.00 20.67  ? 473 GLU B O   1 
ATOM   3136 C CB  . GLU A 1 417 ? 29.205 133.556 -35.413 1.00 14.05  ? 473 GLU B CB  1 
ATOM   3137 C CG  . GLU A 1 417 ? 27.848 133.891 -35.965 1.00 30.01  ? 473 GLU B CG  1 
ATOM   3138 C CD  . GLU A 1 417 ? 27.459 135.331 -35.776 1.00 32.91  ? 473 GLU B CD  1 
ATOM   3139 O OE1 . GLU A 1 417 ? 27.527 136.090 -36.760 1.00 43.45  ? 473 GLU B OE1 1 
ATOM   3140 O OE2 . GLU A 1 417 ? 27.081 135.705 -34.652 1.00 34.09  ? 473 GLU B OE2 1 
ATOM   3141 N N   . ILE A 1 418 ? 31.030 132.565 -38.265 1.00 17.33  ? 474 ILE B N   1 
ATOM   3142 C CA  . ILE A 1 418 ? 31.785 131.496 -38.898 1.00 13.63  ? 474 ILE B CA  1 
ATOM   3143 C C   . ILE A 1 418 ? 33.258 131.665 -38.528 1.00 21.47  ? 474 ILE B C   1 
ATOM   3144 O O   . ILE A 1 418 ? 34.019 130.692 -38.474 1.00 24.26  ? 474 ILE B O   1 
ATOM   3145 C CB  . ILE A 1 418 ? 31.584 131.451 -40.440 1.00 17.76  ? 474 ILE B CB  1 
ATOM   3146 C CG1 . ILE A 1 418 ? 32.233 130.199 -41.038 1.00 14.58  ? 474 ILE B CG1 1 
ATOM   3147 C CG2 . ILE A 1 418 ? 32.141 132.698 -41.105 1.00 19.43  ? 474 ILE B CG2 1 
ATOM   3148 C CD1 . ILE A 1 418 ? 31.930 130.012 -42.500 1.00 18.14  ? 474 ILE B CD1 1 
ATOM   3149 N N   . GLY A 1 419 ? 33.639 132.902 -38.224 1.00 11.16  ? 475 GLY B N   1 
ATOM   3150 C CA  . GLY A 1 419 ? 34.999 133.200 -37.827 1.00 20.93  ? 475 GLY B CA  1 
ATOM   3151 C C   . GLY A 1 419 ? 35.434 132.616 -36.494 1.00 20.85  ? 475 GLY B C   1 
ATOM   3152 O O   . GLY A 1 419 ? 36.610 132.712 -36.150 1.00 12.84  ? 475 GLY B O   1 
ATOM   3153 N N   . ASN A 1 420 ? 34.505 132.023 -35.740 1.00 17.90  ? 476 ASN B N   1 
ATOM   3154 C CA  . ASN A 1 420 ? 34.870 131.367 -34.483 1.00 26.05  ? 476 ASN B CA  1 
ATOM   3155 C C   . ASN A 1 420 ? 35.359 129.937 -34.668 1.00 30.17  ? 476 ASN B C   1 
ATOM   3156 O O   . ASN A 1 420 ? 35.811 129.297 -33.712 1.00 35.71  ? 476 ASN B O   1 
ATOM   3157 C CB  . ASN A 1 420 ? 33.715 131.386 -33.478 1.00 37.24  ? 476 ASN B CB  1 
ATOM   3158 C CG  . ASN A 1 420 ? 33.562 132.723 -32.798 1.00 53.57  ? 476 ASN B CG  1 
ATOM   3159 O OD1 . ASN A 1 420 ? 34.374 133.097 -31.945 1.00 62.05  ? 476 ASN B OD1 1 
ATOM   3160 N ND2 . ASN A 1 420 ? 32.514 133.453 -33.162 1.00 57.37  ? 476 ASN B ND2 1 
ATOM   3161 N N   . LEU A 1 421 ? 35.283 129.442 -35.900 1.00 27.59  ? 477 LEU B N   1 
ATOM   3162 C CA  . LEU A 1 421 ? 35.657 128.069 -36.181 1.00 20.68  ? 477 LEU B CA  1 
ATOM   3163 C C   . LEU A 1 421 ? 37.115 128.029 -36.581 1.00 11.01  ? 477 LEU B C   1 
ATOM   3164 O O   . LEU A 1 421 ? 37.475 128.476 -37.658 1.00 36.05  ? 477 LEU B O   1 
ATOM   3165 C CB  . LEU A 1 421 ? 34.789 127.533 -37.315 1.00 22.01  ? 477 LEU B CB  1 
ATOM   3166 C CG  . LEU A 1 421 ? 33.295 127.591 -37.006 1.00 16.33  ? 477 LEU B CG  1 
ATOM   3167 C CD1 . LEU A 1 421 ? 32.506 126.900 -38.077 1.00 11.91  ? 477 LEU B CD1 1 
ATOM   3168 C CD2 . LEU A 1 421 ? 33.023 126.940 -35.662 1.00 16.55  ? 477 LEU B CD2 1 
ATOM   3169 N N   . LYS A 1 422 ? 37.942 127.488 -35.692 1.00 12.48  ? 478 LYS B N   1 
ATOM   3170 C CA  . LYS A 1 422 ? 39.392 127.466 -35.857 1.00 13.86  ? 478 LYS B CA  1 
ATOM   3171 C C   . LYS A 1 422 ? 39.871 126.173 -36.489 1.00 15.70  ? 478 LYS B C   1 
ATOM   3172 O O   . LYS A 1 422 ? 41.037 126.056 -36.869 1.00 20.73  ? 478 LYS B O   1 
ATOM   3173 C CB  . LYS A 1 422 ? 40.088 127.634 -34.505 1.00 16.22  ? 478 LYS B CB  1 
ATOM   3174 C CG  . LYS A 1 422 ? 39.607 128.819 -33.694 1.00 18.40  ? 478 LYS B CG  1 
ATOM   3175 C CD  . LYS A 1 422 ? 39.827 130.119 -34.439 1.00 24.46  ? 478 LYS B CD  1 
ATOM   3176 C CE  . LYS A 1 422 ? 39.134 131.275 -33.742 1.00 31.35  ? 478 LYS B CE  1 
ATOM   3177 N NZ  . LYS A 1 422 ? 39.405 132.566 -34.435 1.00 36.76  ? 478 LYS B NZ  1 
ATOM   3178 N N   . ASN A 1 423 ? 38.994 125.182 -36.565 1.00 12.77  ? 479 ASN B N   1 
ATOM   3179 C CA  . ASN A 1 423 ? 39.344 123.938 -37.252 1.00 21.92  ? 479 ASN B CA  1 
ATOM   3180 C C   . ASN A 1 423 ? 38.774 123.816 -38.661 1.00 21.28  ? 479 ASN B C   1 
ATOM   3181 O O   . ASN A 1 423 ? 38.916 122.770 -39.293 1.00 23.59  ? 479 ASN B O   1 
ATOM   3182 C CB  . ASN A 1 423 ? 39.006 122.709 -36.406 1.00 23.12  ? 479 ASN B CB  1 
ATOM   3183 C CG  . ASN A 1 423 ? 39.518 122.830 -34.986 1.00 31.71  ? 479 ASN B CG  1 
ATOM   3184 O OD1 . ASN A 1 423 ? 38.752 122.705 -34.033 1.00 37.46  ? 479 ASN B OD1 1 
ATOM   3185 N ND2 . ASN A 1 423 ? 40.817 123.082 -34.834 1.00 35.75  ? 479 ASN B ND2 1 
ATOM   3186 N N   . LEU A 1 424 ? 38.109 124.866 -39.142 1.00 18.00  ? 480 LEU B N   1 
ATOM   3187 C CA  . LEU A 1 424 ? 37.373 124.747 -40.377 1.00 9.07   ? 480 LEU B CA  1 
ATOM   3188 C C   . LEU A 1 424 ? 38.391 124.787 -41.518 1.00 14.33  ? 480 LEU B C   1 
ATOM   3189 O O   . LEU A 1 424 ? 39.057 125.796 -41.751 1.00 14.51  ? 480 LEU B O   1 
ATOM   3190 C CB  . LEU A 1 424 ? 36.403 125.919 -40.477 1.00 21.79  ? 480 LEU B CB  1 
ATOM   3191 C CG  . LEU A 1 424 ? 35.429 126.015 -41.647 1.00 8.37   ? 480 LEU B CG  1 
ATOM   3192 C CD1 . LEU A 1 424 ? 34.583 124.750 -41.723 1.00 8.03   ? 480 LEU B CD1 1 
ATOM   3193 C CD2 . LEU A 1 424 ? 34.554 127.214 -41.433 1.00 8.47   ? 480 LEU B CD2 1 
ATOM   3194 N N   . ASN A 1 425 ? 38.527 123.647 -42.190 1.00 11.51  ? 481 ASN B N   1 
ATOM   3195 C CA  . ASN A 1 425 ? 39.471 123.462 -43.286 1.00 18.95  ? 481 ASN B CA  1 
ATOM   3196 C C   . ASN A 1 425 ? 38.962 123.795 -44.679 1.00 18.11  ? 481 ASN B C   1 
ATOM   3197 O O   . ASN A 1 425 ? 39.686 124.353 -45.508 1.00 17.89  ? 481 ASN B O   1 
ATOM   3198 C CB  . ASN A 1 425 ? 40.025 122.042 -43.279 1.00 20.94  ? 481 ASN B CB  1 
ATOM   3199 C CG  . ASN A 1 425 ? 41.112 121.854 -44.300 1.00 17.67  ? 481 ASN B CG  1 
ATOM   3200 O OD1 . ASN A 1 425 ? 40.901 121.246 -45.348 1.00 18.50  ? 481 ASN B OD1 1 
ATOM   3201 N ND2 . ASN A 1 425 ? 42.285 122.400 -44.011 1.00 19.21  ? 481 ASN B ND2 1 
ATOM   3202 N N   . PHE A 1 426 ? 37.723 123.384 -44.926 1.00 14.41  ? 482 PHE B N   1 
ATOM   3203 C CA  . PHE A 1 426 ? 37.156 123.326 -46.272 1.00 11.90  ? 482 PHE B CA  1 
ATOM   3204 C C   . PHE A 1 426 ? 35.720 123.806 -46.161 1.00 12.49  ? 482 PHE B C   1 
ATOM   3205 O O   . PHE A 1 426 ? 34.923 123.206 -45.424 1.00 9.41   ? 482 PHE B O   1 
ATOM   3206 C CB  . PHE A 1 426 ? 37.191 121.861 -46.719 1.00 7.05   ? 482 PHE B CB  1 
ATOM   3207 C CG  . PHE A 1 426 ? 36.665 121.600 -48.095 1.00 12.87  ? 482 PHE B CG  1 
ATOM   3208 C CD1 . PHE A 1 426 ? 35.305 121.700 -48.378 1.00 16.18  ? 482 PHE B CD1 1 
ATOM   3209 C CD2 . PHE A 1 426 ? 37.526 121.196 -49.104 1.00 6.77   ? 482 PHE B CD2 1 
ATOM   3210 C CE1 . PHE A 1 426 ? 34.817 121.437 -49.655 1.00 10.18  ? 482 PHE B CE1 1 
ATOM   3211 C CE2 . PHE A 1 426 ? 37.051 120.929 -50.380 1.00 12.94  ? 482 PHE B CE2 1 
ATOM   3212 C CZ  . PHE A 1 426 ? 35.698 121.042 -50.659 1.00 7.90   ? 482 PHE B CZ  1 
ATOM   3213 N N   . VAL A 1 427 ? 35.376 124.864 -46.889 1.00 7.04   ? 483 VAL B N   1 
ATOM   3214 C CA  . VAL A 1 427 ? 33.994 125.331 -46.926 1.00 17.39  ? 483 VAL B CA  1 
ATOM   3215 C C   . VAL A 1 427 ? 33.522 125.526 -48.357 1.00 14.52  ? 483 VAL B C   1 
ATOM   3216 O O   . VAL A 1 427 ? 34.151 126.254 -49.128 1.00 6.64   ? 483 VAL B O   1 
ATOM   3217 C CB  . VAL A 1 427 ? 33.804 126.661 -46.151 1.00 19.63  ? 483 VAL B CB  1 
ATOM   3218 C CG1 . VAL A 1 427 ? 34.986 127.523 -46.344 1.00 26.11  ? 483 VAL B CG1 1 
ATOM   3219 C CG2 . VAL A 1 427 ? 32.548 127.411 -46.624 1.00 6.76   ? 483 VAL B CG2 1 
ATOM   3220 N N   . ASP A 1 428 ? 32.419 124.871 -48.709 1.00 11.19  ? 484 ASP B N   1 
ATOM   3221 C CA  . ASP A 1 428 ? 31.784 125.117 -49.986 1.00 5.17   ? 484 ASP B CA  1 
ATOM   3222 C C   . ASP A 1 428 ? 30.342 125.572 -49.793 1.00 11.11  ? 484 ASP B C   1 
ATOM   3223 O O   . ASP A 1 428 ? 29.473 124.799 -49.371 1.00 15.10  ? 484 ASP B O   1 
ATOM   3224 C CB  . ASP A 1 428 ? 31.840 123.849 -50.835 1.00 14.00  ? 484 ASP B CB  1 
ATOM   3225 C CG  . ASP A 1 428 ? 31.426 124.088 -52.256 1.00 21.40  ? 484 ASP B CG  1 
ATOM   3226 O OD1 . ASP A 1 428 ? 31.161 125.259 -52.595 1.00 30.18  ? 484 ASP B OD1 1 
ATOM   3227 O OD2 . ASP A 1 428 ? 31.392 123.116 -53.045 1.00 24.19  ? 484 ASP B OD2 1 
ATOM   3228 N N   . ILE A 1 429 ? 30.118 126.857 -50.035 1.00 8.81   ? 485 ILE B N   1 
ATOM   3229 C CA  . ILE A 1 429 ? 28.783 127.458 -50.119 1.00 7.48   ? 485 ILE B CA  1 
ATOM   3230 C C   . ILE A 1 429 ? 28.307 127.856 -51.509 1.00 10.40  ? 485 ILE B C   1 
ATOM   3231 O O   . ILE A 1 429 ? 27.374 128.654 -51.636 1.00 5.63   ? 485 ILE B O   1 
ATOM   3232 C CB  . ILE A 1 429 ? 28.546 128.560 -49.098 1.00 14.86  ? 485 ILE B CB  1 
ATOM   3233 C CG1 . ILE A 1 429 ? 29.331 128.247 -47.827 1.00 9.76   ? 485 ILE B CG1 1 
ATOM   3234 C CG2 . ILE A 1 429 ? 27.062 128.596 -48.724 1.00 19.03  ? 485 ILE B CG2 1 
ATOM   3235 C CD1 . ILE A 1 429 ? 28.816 128.956 -46.633 1.00 10.60  ? 485 ILE B CD1 1 
ATOM   3236 N N   . SER A 1 430 ? 29.012 127.400 -52.543 1.00 14.85  ? 486 SER B N   1 
ATOM   3237 C CA  . SER A 1 430 ? 28.706 127.782 -53.929 1.00 11.26  ? 486 SER B CA  1 
ATOM   3238 C C   . SER A 1 430 ? 27.294 127.381 -54.363 1.00 12.59  ? 486 SER B C   1 
ATOM   3239 O O   . SER A 1 430 ? 26.623 126.604 -53.686 1.00 3.43   ? 486 SER B O   1 
ATOM   3240 C CB  . SER A 1 430 ? 29.715 127.171 -54.896 1.00 11.79  ? 486 SER B CB  1 
ATOM   3241 O OG  . SER A 1 430 ? 29.629 125.764 -54.881 1.00 11.47  ? 486 SER B OG  1 
ATOM   3242 N N   . GLU A 1 431 ? 26.818 128.007 -55.437 1.00 8.18   ? 487 GLU B N   1 
ATOM   3243 C CA  . GLU A 1 431 ? 25.460 127.789 -55.954 1.00 9.69   ? 487 GLU B CA  1 
ATOM   3244 C C   . GLU A 1 431 ? 24.341 127.971 -54.930 1.00 6.46   ? 487 GLU B C   1 
ATOM   3245 O O   . GLU A 1 431 ? 23.639 127.026 -54.579 1.00 5.76   ? 487 GLU B O   1 
ATOM   3246 C CB  . GLU A 1 431 ? 25.338 126.432 -56.642 1.00 9.04   ? 487 GLU B CB  1 
ATOM   3247 C CG  . GLU A 1 431 ? 25.951 126.411 -58.043 1.00 5.04   ? 487 GLU B CG  1 
ATOM   3248 C CD  . GLU A 1 431 ? 25.784 125.070 -58.719 1.00 16.94  ? 487 GLU B CD  1 
ATOM   3249 O OE1 . GLU A 1 431 ? 25.322 125.046 -59.881 1.00 24.11  ? 487 GLU B OE1 1 
ATOM   3250 O OE2 . GLU A 1 431 ? 26.130 124.041 -58.089 1.00 19.53  ? 487 GLU B OE2 1 
ATOM   3251 N N   . ASN A 1 432 ? 24.188 129.199 -54.461 1.00 10.22  ? 488 ASN B N   1 
ATOM   3252 C CA  . ASN A 1 432 ? 23.156 129.533 -53.506 1.00 11.56  ? 488 ASN B CA  1 
ATOM   3253 C C   . ASN A 1 432 ? 22.673 130.939 -53.815 1.00 12.58  ? 488 ASN B C   1 
ATOM   3254 O O   . ASN A 1 432 ? 22.996 131.483 -54.853 1.00 16.68  ? 488 ASN B O   1 
ATOM   3255 C CB  . ASN A 1 432 ? 23.671 129.399 -52.062 1.00 12.45  ? 488 ASN B CB  1 
ATOM   3256 C CG  . ASN A 1 432 ? 23.500 127.973 -51.502 1.00 11.39  ? 488 ASN B CG  1 
ATOM   3257 O OD1 . ASN A 1 432 ? 22.389 127.545 -51.190 1.00 11.54  ? 488 ASN B OD1 1 
ATOM   3258 N ND2 . ASN A 1 432 ? 24.598 127.244 -51.381 1.00 8.24   ? 488 ASN B ND2 1 
ATOM   3259 N N   . ARG A 1 433 ? 21.830 131.489 -52.964 1.00 11.81  ? 489 ARG B N   1 
ATOM   3260 C CA  . ARG A 1 433 ? 21.344 132.856 -53.126 1.00 11.20  ? 489 ARG B CA  1 
ATOM   3261 C C   . ARG A 1 433 ? 21.969 133.890 -52.178 1.00 12.21  ? 489 ARG B C   1 
ATOM   3262 O O   . ARG A 1 433 ? 21.387 134.956 -51.941 1.00 18.02  ? 489 ARG B O   1 
ATOM   3263 C CB  . ARG A 1 433 ? 19.816 132.892 -53.196 1.00 18.09  ? 489 ARG B CB  1 
ATOM   3264 C CG  . ARG A 1 433 ? 19.267 131.733 -54.029 1.00 27.31  ? 489 ARG B CG  1 
ATOM   3265 C CD  . ARG A 1 433 ? 18.600 132.154 -55.326 1.00 33.66  ? 489 ARG B CD  1 
ATOM   3266 N NE  . ARG A 1 433 ? 17.143 132.019 -55.222 1.00 46.70  ? 489 ARG B NE  1 
ATOM   3267 C CZ  . ARG A 1 433 ? 16.410 131.075 -55.816 1.00 44.71  ? 489 ARG B CZ  1 
ATOM   3268 N NH1 . ARG A 1 433 ? 16.971 130.161 -56.600 1.00 35.19  ? 489 ARG B NH1 1 
ATOM   3269 N NH2 . ARG A 1 433 ? 15.096 131.059 -55.635 1.00 47.51  ? 489 ARG B NH2 1 
ATOM   3270 N N   . LEU A 1 434 ? 23.075 133.519 -51.532 1.00 15.50  ? 490 LEU B N   1 
ATOM   3271 C CA  . LEU A 1 434 ? 23.752 134.399 -50.554 1.00 16.54  ? 490 LEU B CA  1 
ATOM   3272 C C   . LEU A 1 434 ? 24.006 135.832 -51.050 1.00 16.20  ? 490 LEU B C   1 
ATOM   3273 O O   . LEU A 1 434 ? 24.411 136.054 -52.196 1.00 19.27  ? 490 LEU B O   1 
ATOM   3274 C CB  . LEU A 1 434 ? 25.105 133.806 -50.173 1.00 6.32   ? 490 LEU B CB  1 
ATOM   3275 C CG  . LEU A 1 434 ? 25.132 132.431 -49.519 1.00 11.42  ? 490 LEU B CG  1 
ATOM   3276 C CD1 . LEU A 1 434 ? 26.561 131.988 -49.362 1.00 7.38   ? 490 LEU B CD1 1 
ATOM   3277 C CD2 . LEU A 1 434 ? 24.446 132.494 -48.188 1.00 5.97   ? 490 LEU B CD2 1 
ATOM   3278 N N   . VAL A 1 435 ? 23.785 136.798 -50.172 1.00 17.31  ? 491 VAL B N   1 
ATOM   3279 C CA  . VAL A 1 435 ? 23.955 138.216 -50.507 1.00 17.10  ? 491 VAL B CA  1 
ATOM   3280 C C   . VAL A 1 435 ? 24.947 138.892 -49.583 1.00 8.65   ? 491 VAL B C   1 
ATOM   3281 O O   . VAL A 1 435 ? 25.542 138.244 -48.731 1.00 23.68  ? 491 VAL B O   1 
ATOM   3282 C CB  . VAL A 1 435 ? 22.606 138.975 -50.467 1.00 8.02   ? 491 VAL B CB  1 
ATOM   3283 C CG1 . VAL A 1 435 ? 21.720 138.513 -51.615 1.00 7.44   ? 491 VAL B CG1 1 
ATOM   3284 C CG2 . VAL A 1 435 ? 21.894 138.759 -49.123 1.00 8.04   ? 491 VAL B CG2 1 
ATOM   3285 N N   . GLY A 1 436 ? 25.137 140.194 -49.767 1.00 31.53  ? 492 GLY B N   1 
ATOM   3286 C CA  . GLY A 1 436 ? 26.025 140.990 -48.930 1.00 10.04  ? 492 GLY B CA  1 
ATOM   3287 C C   . GLY A 1 436 ? 27.518 140.807 -49.165 1.00 13.00  ? 492 GLY B C   1 
ATOM   3288 O O   . GLY A 1 436 ? 27.946 140.215 -50.143 1.00 19.20  ? 492 GLY B O   1 
ATOM   3289 N N   . SER A 1 437 ? 28.316 141.346 -48.255 1.00 15.65  ? 493 SER B N   1 
ATOM   3290 C CA  . SER A 1 437 ? 29.769 141.230 -48.305 1.00 19.76  ? 493 SER B CA  1 
ATOM   3291 C C   . SER A 1 437 ? 30.286 139.904 -47.774 1.00 19.03  ? 493 SER B C   1 
ATOM   3292 O O   . SER A 1 437 ? 29.603 139.228 -47.009 1.00 22.32  ? 493 SER B O   1 
ATOM   3293 C CB  . SER A 1 437 ? 30.405 142.365 -47.499 1.00 12.27  ? 493 SER B CB  1 
ATOM   3294 O OG  . SER A 1 437 ? 30.273 143.584 -48.195 1.00 29.58  ? 493 SER B OG  1 
ATOM   3295 N N   . ILE A 1 438 ? 31.490 139.528 -48.192 1.00 15.54  ? 494 ILE B N   1 
ATOM   3296 C CA  . ILE A 1 438 ? 32.245 138.521 -47.467 1.00 18.19  ? 494 ILE B CA  1 
ATOM   3297 C C   . ILE A 1 438 ? 32.705 139.145 -46.137 1.00 27.36  ? 494 ILE B C   1 
ATOM   3298 O O   . ILE A 1 438 ? 33.450 140.136 -46.132 1.00 28.32  ? 494 ILE B O   1 
ATOM   3299 C CB  . ILE A 1 438 ? 33.462 138.066 -48.267 1.00 17.95  ? 494 ILE B CB  1 
ATOM   3300 C CG1 . ILE A 1 438 ? 33.022 137.275 -49.492 1.00 20.29  ? 494 ILE B CG1 1 
ATOM   3301 C CG2 . ILE A 1 438 ? 34.342 137.190 -47.423 1.00 19.91  ? 494 ILE B CG2 1 
ATOM   3302 C CD1 . ILE A 1 438 ? 34.070 137.208 -50.578 1.00 18.99  ? 494 ILE B CD1 1 
ATOM   3303 N N   . PRO A 1 439 ? 32.233 138.591 -45.002 1.00 24.43  ? 495 PRO B N   1 
ATOM   3304 C CA  . PRO A 1 439 ? 32.489 139.214 -43.688 1.00 16.65  ? 495 PRO B CA  1 
ATOM   3305 C C   . PRO A 1 439 ? 33.950 139.143 -43.254 1.00 22.64  ? 495 PRO B C   1 
ATOM   3306 O O   . PRO A 1 439 ? 34.528 138.057 -43.236 1.00 28.75  ? 495 PRO B O   1 
ATOM   3307 C CB  . PRO A 1 439 ? 31.623 138.387 -42.732 1.00 11.82  ? 495 PRO B CB  1 
ATOM   3308 C CG  . PRO A 1 439 ? 31.510 137.043 -43.401 1.00 21.16  ? 495 PRO B CG  1 
ATOM   3309 C CD  . PRO A 1 439 ? 31.469 137.332 -44.888 1.00 18.39  ? 495 PRO B CD  1 
ATOM   3310 N N   . PRO A 1 440 ? 34.528 140.285 -42.851 1.00 24.59  ? 496 PRO B N   1 
ATOM   3311 C CA  . PRO A 1 440 ? 35.916 140.387 -42.377 1.00 22.57  ? 496 PRO B CA  1 
ATOM   3312 C C   . PRO A 1 440 ? 36.287 139.342 -41.324 1.00 25.26  ? 496 PRO B C   1 
ATOM   3313 O O   . PRO A 1 440 ? 37.439 138.883 -41.295 1.00 29.86  ? 496 PRO B O   1 
ATOM   3314 C CB  . PRO A 1 440 ? 35.960 141.790 -41.773 1.00 15.36  ? 496 PRO B CB  1 
ATOM   3315 C CG  . PRO A 1 440 ? 35.006 142.566 -42.629 1.00 26.77  ? 496 PRO B CG  1 
ATOM   3316 C CD  . PRO A 1 440 ? 33.886 141.610 -42.955 1.00 24.47  ? 496 PRO B CD  1 
ATOM   3317 N N   . ALA A 1 441 ? 35.321 138.957 -40.488 1.00 20.68  ? 497 ALA B N   1 
ATOM   3318 C CA  . ALA A 1 441 ? 35.574 138.000 -39.408 1.00 19.12  ? 497 ALA B CA  1 
ATOM   3319 C C   . ALA A 1 441 ? 36.043 136.617 -39.895 1.00 20.41  ? 497 ALA B C   1 
ATOM   3320 O O   . ALA A 1 441 ? 36.527 135.815 -39.105 1.00 15.29  ? 497 ALA B O   1 
ATOM   3321 C CB  . ALA A 1 441 ? 34.357 137.860 -38.529 1.00 13.64  ? 497 ALA B CB  1 
ATOM   3322 N N   . ILE A 1 442 ? 35.900 136.329 -41.187 1.00 21.10  ? 498 ILE B N   1 
ATOM   3323 C CA  . ILE A 1 442 ? 36.354 135.041 -41.701 1.00 25.14  ? 498 ILE B CA  1 
ATOM   3324 C C   . ILE A 1 442 ? 37.882 134.959 -41.624 1.00 28.87  ? 498 ILE B C   1 
ATOM   3325 O O   . ILE A 1 442 ? 38.468 133.881 -41.709 1.00 31.07  ? 498 ILE B O   1 
ATOM   3326 C CB  . ILE A 1 442 ? 35.801 134.748 -43.140 1.00 39.20  ? 498 ILE B CB  1 
ATOM   3327 C CG1 . ILE A 1 442 ? 36.097 133.309 -43.567 1.00 35.98  ? 498 ILE B CG1 1 
ATOM   3328 C CG2 . ILE A 1 442 ? 36.343 135.727 -44.160 1.00 32.75  ? 498 ILE B CG2 1 
ATOM   3329 C CD1 . ILE A 1 442 ? 35.501 132.947 -44.900 1.00 30.55  ? 498 ILE B CD1 1 
ATOM   3330 N N   . SER A 1 443 ? 38.518 136.111 -41.421 1.00 30.57  ? 499 SER B N   1 
ATOM   3331 C CA  . SER A 1 443 ? 39.952 136.162 -41.174 1.00 31.72  ? 499 SER B CA  1 
ATOM   3332 C C   . SER A 1 443 ? 40.302 135.312 -39.955 1.00 30.70  ? 499 SER B C   1 
ATOM   3333 O O   . SER A 1 443 ? 41.440 134.881 -39.774 1.00 35.83  ? 499 SER B O   1 
ATOM   3334 C CB  . SER A 1 443 ? 40.357 137.601 -40.904 1.00 31.86  ? 499 SER B CB  1 
ATOM   3335 O OG  . SER A 1 443 ? 39.593 138.107 -39.823 1.00 31.51  ? 499 SER B OG  1 
ATOM   3336 N N   . GLY A 1 444 ? 39.304 135.072 -39.120 1.00 28.06  ? 500 GLY B N   1 
ATOM   3337 C CA  . GLY A 1 444 ? 39.490 134.311 -37.904 1.00 28.92  ? 500 GLY B CA  1 
ATOM   3338 C C   . GLY A 1 444 ? 39.553 132.806 -38.094 1.00 34.11  ? 500 GLY B C   1 
ATOM   3339 O O   . GLY A 1 444 ? 39.829 132.096 -37.128 1.00 31.13  ? 500 GLY B O   1 
ATOM   3340 N N   . CYS A 1 445 ? 39.328 132.303 -39.311 1.00 29.37  ? 501 CYS B N   1 
ATOM   3341 C CA  . CYS A 1 445 ? 39.401 130.862 -39.486 1.00 29.16  ? 501 CYS B CA  1 
ATOM   3342 C C   . CYS A 1 445 ? 40.832 130.547 -39.863 1.00 32.10  ? 501 CYS B C   1 
ATOM   3343 O O   . CYS A 1 445 ? 41.204 130.586 -41.040 1.00 26.32  ? 501 CYS B O   1 
ATOM   3344 C CB  . CYS A 1 445 ? 38.505 130.418 -40.646 1.00 28.06  ? 501 CYS B CB  1 
ATOM   3345 S SG  . CYS A 1 445 ? 36.739 130.742 -40.478 1.00 15.74  ? 501 CYS B SG  1 
ATOM   3346 N N   . GLU A 1 446 ? 41.601 130.092 -38.883 1.00 37.07  ? 502 GLU B N   1 
ATOM   3347 C CA  . GLU A 1 446 ? 43.044 130.032 -39.063 1.00 38.60  ? 502 GLU B CA  1 
ATOM   3348 C C   . GLU A 1 446 ? 43.477 128.774 -39.808 1.00 28.68  ? 502 GLU B C   1 
ATOM   3349 O O   . GLU A 1 446 ? 44.613 128.672 -40.257 1.00 26.64  ? 502 GLU B O   1 
ATOM   3350 C CB  . GLU A 1 446 ? 43.783 130.202 -37.726 1.00 44.65  ? 502 GLU B CB  1 
ATOM   3351 C CG  . GLU A 1 446 ? 43.259 129.354 -36.572 1.00 58.01  ? 502 GLU B CG  1 
ATOM   3352 C CD  . GLU A 1 446 ? 43.627 129.935 -35.196 1.00 69.54  ? 502 GLU B CD  1 
ATOM   3353 O OE1 . GLU A 1 446 ? 43.805 129.148 -34.231 1.00 67.67  ? 502 GLU B OE1 1 
ATOM   3354 O OE2 . GLU A 1 446 ? 43.725 131.181 -35.080 1.00 74.84  ? 502 GLU B OE2 1 
ATOM   3355 N N   . SER A 1 447 ? 42.561 127.818 -39.917 1.00 21.78  ? 503 SER B N   1 
ATOM   3356 C CA  . SER A 1 447 ? 42.824 126.567 -40.611 1.00 13.98  ? 503 SER B CA  1 
ATOM   3357 C C   . SER A 1 447 ? 42.262 126.515 -42.032 1.00 17.09  ? 503 SER B C   1 
ATOM   3358 O O   . SER A 1 447 ? 42.364 125.486 -42.705 1.00 16.75  ? 503 SER B O   1 
ATOM   3359 C CB  . SER A 1 447 ? 42.286 125.397 -39.789 1.00 17.59  ? 503 SER B CB  1 
ATOM   3360 O OG  . SER A 1 447 ? 43.165 125.094 -38.720 1.00 21.99  ? 503 SER B OG  1 
ATOM   3361 N N   . LEU A 1 448 ? 41.640 127.604 -42.476 1.00 15.34  ? 504 LEU B N   1 
ATOM   3362 C CA  . LEU A 1 448 ? 40.887 127.562 -43.717 1.00 11.85  ? 504 LEU B CA  1 
ATOM   3363 C C   . LEU A 1 448 ? 41.793 127.418 -44.943 1.00 15.78  ? 504 LEU B C   1 
ATOM   3364 O O   . LEU A 1 448 ? 42.724 128.199 -45.138 1.00 12.18  ? 504 LEU B O   1 
ATOM   3365 C CB  . LEU A 1 448 ? 39.991 128.783 -43.845 1.00 17.63  ? 504 LEU B CB  1 
ATOM   3366 C CG  . LEU A 1 448 ? 39.040 128.743 -45.031 1.00 10.41  ? 504 LEU B CG  1 
ATOM   3367 C CD1 . LEU A 1 448 ? 38.094 127.544 -44.865 1.00 9.55   ? 504 LEU B CD1 1 
ATOM   3368 C CD2 . LEU A 1 448 ? 38.289 130.049 -45.097 1.00 10.51  ? 504 LEU B CD2 1 
ATOM   3369 N N   . GLU A 1 449 ? 41.500 126.400 -45.749 1.00 13.58  ? 505 GLU B N   1 
ATOM   3370 C CA  . GLU A 1 449 ? 42.324 125.999 -46.895 1.00 15.64  ? 505 GLU B CA  1 
ATOM   3371 C C   . GLU A 1 449 ? 41.590 126.136 -48.220 1.00 11.61  ? 505 GLU B C   1 
ATOM   3372 O O   . GLU A 1 449 ? 42.149 126.642 -49.193 1.00 10.75  ? 505 GLU B O   1 
ATOM   3373 C CB  . GLU A 1 449 ? 42.973 124.620 -46.703 1.00 22.79  ? 505 GLU B CB  1 
ATOM   3374 C CG  . GLU A 1 449 ? 44.204 124.669 -45.766 1.00 26.74  ? 505 GLU B CG  1 
ATOM   3375 C CD  . GLU A 1 449 ? 44.932 123.329 -45.619 1.00 36.87  ? 505 GLU B CD  1 
ATOM   3376 O OE1 . GLU A 1 449 ? 44.263 122.286 -45.432 1.00 39.30  ? 505 GLU B OE1 1 
ATOM   3377 O OE2 . GLU A 1 449 ? 46.183 123.323 -45.683 1.00 38.85  ? 505 GLU B OE2 1 
ATOM   3378 N N   . PHE A 1 450 ? 40.392 125.559 -48.275 1.00 16.34  ? 506 PHE B N   1 
ATOM   3379 C CA  . PHE A 1 450 ? 39.512 125.595 -49.441 1.00 8.96   ? 506 PHE B CA  1 
ATOM   3380 C C   . PHE A 1 450 ? 38.288 126.499 -49.178 1.00 14.97  ? 506 PHE B C   1 
ATOM   3381 O O   . PHE A 1 450 ? 37.545 126.273 -48.221 1.00 15.96  ? 506 PHE B O   1 
ATOM   3382 C CB  . PHE A 1 450 ? 39.082 124.159 -49.732 1.00 23.81  ? 506 PHE B CB  1 
ATOM   3383 C CG  . PHE A 1 450 ? 38.189 123.999 -50.930 1.00 29.97  ? 506 PHE B CG  1 
ATOM   3384 C CD1 . PHE A 1 450 ? 36.820 124.207 -50.833 1.00 28.62  ? 506 PHE B CD1 1 
ATOM   3385 C CD2 . PHE A 1 450 ? 38.720 123.593 -52.160 1.00 31.87  ? 506 PHE B CD2 1 
ATOM   3386 C CE1 . PHE A 1 450 ? 35.992 124.036 -51.960 1.00 30.84  ? 506 PHE B CE1 1 
ATOM   3387 C CE2 . PHE A 1 450 ? 37.911 123.421 -53.273 1.00 24.23  ? 506 PHE B CE2 1 
ATOM   3388 C CZ  . PHE A 1 450 ? 36.542 123.641 -53.175 1.00 27.06  ? 506 PHE B CZ  1 
ATOM   3389 N N   . LEU A 1 451 ? 38.094 127.536 -49.998 1.00 14.64  ? 507 LEU B N   1 
ATOM   3390 C CA  . LEU A 1 451 ? 36.908 128.395 -49.888 1.00 8.50   ? 507 LEU B CA  1 
ATOM   3391 C C   . LEU A 1 451 ? 36.184 128.571 -51.229 1.00 20.54  ? 507 LEU B C   1 
ATOM   3392 O O   . LEU A 1 451 ? 36.676 129.290 -52.127 1.00 14.47  ? 507 LEU B O   1 
ATOM   3393 C CB  . LEU A 1 451 ? 37.310 129.771 -49.356 1.00 9.24   ? 507 LEU B CB  1 
ATOM   3394 C CG  . LEU A 1 451 ? 36.213 130.831 -49.200 1.00 19.45  ? 507 LEU B CG  1 
ATOM   3395 C CD1 . LEU A 1 451 ? 35.093 130.339 -48.317 1.00 12.11  ? 507 LEU B CD1 1 
ATOM   3396 C CD2 . LEU A 1 451 ? 36.778 132.144 -48.635 1.00 21.05  ? 507 LEU B CD2 1 
ATOM   3397 N N   . ASP A 1 452 ? 35.005 127.958 -51.357 1.00 7.29   ? 508 ASP B N   1 
ATOM   3398 C CA  . ASP A 1 452 ? 34.252 128.061 -52.594 1.00 6.85   ? 508 ASP B CA  1 
ATOM   3399 C C   . ASP A 1 452 ? 32.906 128.765 -52.379 1.00 11.73  ? 508 ASP B C   1 
ATOM   3400 O O   . ASP A 1 452 ? 31.929 128.152 -51.932 1.00 8.78   ? 508 ASP B O   1 
ATOM   3401 C CB  . ASP A 1 452 ? 34.021 126.650 -53.158 1.00 22.08  ? 508 ASP B CB  1 
ATOM   3402 C CG  . ASP A 1 452 ? 33.677 126.639 -54.660 1.00 22.59  ? 508 ASP B CG  1 
ATOM   3403 O OD1 . ASP A 1 452 ? 33.091 127.613 -55.192 1.00 22.68  ? 508 ASP B OD1 1 
ATOM   3404 O OD2 . ASP A 1 452 ? 33.992 125.622 -55.309 1.00 28.79  ? 508 ASP B OD2 1 
ATOM   3405 N N   . LEU A 1 453 ? 32.867 130.041 -52.754 1.00 8.22   ? 509 LEU B N   1 
ATOM   3406 C CA  . LEU A 1 453 ? 31.664 130.871 -52.760 1.00 6.79   ? 509 LEU B CA  1 
ATOM   3407 C C   . LEU A 1 453 ? 31.011 131.093 -54.155 1.00 14.99  ? 509 LEU B C   1 
ATOM   3408 O O   . LEU A 1 453 ? 30.182 131.983 -54.304 1.00 9.04   ? 509 LEU B O   1 
ATOM   3409 C CB  . LEU A 1 453 ? 31.930 132.199 -52.054 1.00 12.34  ? 509 LEU B CB  1 
ATOM   3410 C CG  . LEU A 1 453 ? 32.434 132.075 -50.609 1.00 17.93  ? 509 LEU B CG  1 
ATOM   3411 C CD1 . LEU A 1 453 ? 32.801 133.416 -50.016 1.00 14.35  ? 509 LEU B CD1 1 
ATOM   3412 C CD2 . LEU A 1 453 ? 31.393 131.400 -49.750 1.00 27.35  ? 509 LEU B CD2 1 
ATOM   3413 N N   . HIS A 1 454 ? 31.432 130.383 -55.194 1.00 6.22   ? 510 HIS B N   1 
ATOM   3414 C CA  . HIS A 1 454 ? 30.977 130.771 -56.539 1.00 8.36   ? 510 HIS B CA  1 
ATOM   3415 C C   . HIS A 1 454 ? 29.454 130.674 -56.812 1.00 12.87  ? 510 HIS B C   1 
ATOM   3416 O O   . HIS A 1 454 ? 28.749 129.903 -56.172 1.00 14.76  ? 510 HIS B O   1 
ATOM   3417 C CB  . HIS A 1 454 ? 31.798 130.080 -57.653 1.00 6.02   ? 510 HIS B CB  1 
ATOM   3418 C CG  . HIS A 1 454 ? 31.380 128.671 -57.943 1.00 11.11  ? 510 HIS B CG  1 
ATOM   3419 N ND1 . HIS A 1 454 ? 32.095 127.574 -57.505 1.00 14.79  ? 510 HIS B ND1 1 
ATOM   3420 C CD2 . HIS A 1 454 ? 30.340 128.176 -58.659 1.00 6.45   ? 510 HIS B CD2 1 
ATOM   3421 C CE1 . HIS A 1 454 ? 31.504 126.467 -57.921 1.00 9.41   ? 510 HIS B CE1 1 
ATOM   3422 N NE2 . HIS A 1 454 ? 30.436 126.805 -58.623 1.00 9.42   ? 510 HIS B NE2 1 
ATOM   3423 N N   . THR A 1 455 ? 28.966 131.465 -57.771 1.00 12.45  ? 511 THR B N   1 
ATOM   3424 C CA  . THR A 1 455 ? 27.553 131.456 -58.173 1.00 6.64   ? 511 THR B CA  1 
ATOM   3425 C C   . THR A 1 455 ? 26.633 131.795 -56.989 1.00 17.68  ? 511 THR B C   1 
ATOM   3426 O O   . THR A 1 455 ? 25.851 130.974 -56.484 1.00 13.50  ? 511 THR B O   1 
ATOM   3427 C CB  . THR A 1 455 ? 27.154 130.152 -58.938 1.00 14.82  ? 511 THR B CB  1 
ATOM   3428 O OG1 . THR A 1 455 ? 27.888 130.086 -60.169 1.00 7.15   ? 511 THR B OG1 1 
ATOM   3429 C CG2 . THR A 1 455 ? 25.639 130.105 -59.281 1.00 3.81   ? 511 THR B CG2 1 
ATOM   3430 N N   . ASN A 1 456 ? 26.780 133.033 -56.534 1.00 18.05  ? 512 ASN B N   1 
ATOM   3431 C CA  . ASN A 1 456 ? 25.937 133.587 -55.503 1.00 8.36   ? 512 ASN B CA  1 
ATOM   3432 C C   . ASN A 1 456 ? 25.665 135.027 -55.886 1.00 14.55  ? 512 ASN B C   1 
ATOM   3433 O O   . ASN A 1 456 ? 26.066 135.465 -56.958 1.00 17.82  ? 512 ASN B O   1 
ATOM   3434 C CB  . ASN A 1 456 ? 26.636 133.511 -54.144 1.00 7.07   ? 512 ASN B CB  1 
ATOM   3435 C CG  . ASN A 1 456 ? 26.358 132.206 -53.422 1.00 10.01  ? 512 ASN B CG  1 
ATOM   3436 O OD1 . ASN A 1 456 ? 25.225 131.943 -53.026 1.00 6.37   ? 512 ASN B OD1 1 
ATOM   3437 N ND2 . ASN A 1 456 ? 27.392 131.390 -53.234 1.00 6.21   ? 512 ASN B ND2 1 
ATOM   3438 N N   . SER A 1 457 ? 24.954 135.745 -55.032 1.00 13.98  ? 513 SER B N   1 
ATOM   3439 C CA  . SER A 1 457 ? 24.698 137.172 -55.214 1.00 13.11  ? 513 SER B CA  1 
ATOM   3440 C C   . SER A 1 457 ? 25.599 138.087 -54.393 1.00 16.73  ? 513 SER B C   1 
ATOM   3441 O O   . SER A 1 457 ? 25.200 139.211 -54.056 1.00 14.17  ? 513 SER B O   1 
ATOM   3442 C CB  . SER A 1 457 ? 23.222 137.513 -55.093 1.00 20.74  ? 513 SER B CB  1 
ATOM   3443 O OG  . SER A 1 457 ? 22.527 136.863 -56.143 1.00 25.95  ? 513 SER B OG  1 
ATOM   3444 N N   . LEU A 1 458 ? 26.724 137.550 -53.924 1.00 12.23  ? 514 LEU B N   1 
ATOM   3445 C CA  . LEU A 1 458 ? 27.650 138.317 -53.101 1.00 8.49   ? 514 LEU B CA  1 
ATOM   3446 C C   . LEU A 1 458 ? 28.056 139.604 -53.796 1.00 13.06  ? 514 LEU B C   1 
ATOM   3447 O O   . LEU A 1 458 ? 28.116 139.659 -55.023 1.00 21.09  ? 514 LEU B O   1 
ATOM   3448 C CB  . LEU A 1 458 ? 28.904 137.492 -52.804 1.00 9.23   ? 514 LEU B CB  1 
ATOM   3449 C CG  . LEU A 1 458 ? 28.726 136.201 -52.002 1.00 8.54   ? 514 LEU B CG  1 
ATOM   3450 C CD1 . LEU A 1 458 ? 30.063 135.499 -51.755 1.00 8.67   ? 514 LEU B CD1 1 
ATOM   3451 C CD2 . LEU A 1 458 ? 28.041 136.540 -50.714 1.00 8.20   ? 514 LEU B CD2 1 
ATOM   3452 N N   . SER A 1 459 ? 28.330 140.641 -53.014 1.00 9.76   ? 515 SER B N   1 
ATOM   3453 C CA  . SER A 1 459 ? 28.750 141.923 -53.559 1.00 10.41  ? 515 SER B CA  1 
ATOM   3454 C C   . SER A 1 459 ? 29.604 142.707 -52.590 1.00 14.55  ? 515 SER B C   1 
ATOM   3455 O O   . SER A 1 459 ? 30.009 142.215 -51.537 1.00 25.27  ? 515 SER B O   1 
ATOM   3456 C CB  . SER A 1 459 ? 27.549 142.788 -53.902 1.00 15.94  ? 515 SER B CB  1 
ATOM   3457 O OG  . SER A 1 459 ? 27.015 143.328 -52.709 1.00 23.11  ? 515 SER B OG  1 
ATOM   3458 N N   . GLY A 1 460 ? 29.859 143.957 -52.949 1.00 17.70  ? 516 GLY B N   1 
ATOM   3459 C CA  . GLY A 1 460 ? 30.724 144.787 -52.146 1.00 13.82  ? 516 GLY B CA  1 
ATOM   3460 C C   . GLY A 1 460 ? 32.158 144.659 -52.610 1.00 17.95  ? 516 GLY B C   1 
ATOM   3461 O O   . GLY A 1 460 ? 32.431 144.242 -53.735 1.00 19.19  ? 516 GLY B O   1 
ATOM   3462 N N   . SER A 1 461 ? 33.073 145.026 -51.729 1.00 13.70  ? 517 SER B N   1 
ATOM   3463 C CA  . SER A 1 461 ? 34.474 145.071 -52.061 1.00 20.71  ? 517 SER B CA  1 
ATOM   3464 C C   . SER A 1 461 ? 35.188 143.844 -51.507 1.00 29.00  ? 517 SER B C   1 
ATOM   3465 O O   . SER A 1 461 ? 34.565 142.939 -50.955 1.00 32.55  ? 517 SER B O   1 
ATOM   3466 C CB  . SER A 1 461 ? 35.083 146.383 -51.559 1.00 16.41  ? 517 SER B CB  1 
ATOM   3467 O OG  . SER A 1 461 ? 36.493 146.307 -51.478 1.00 27.39  ? 517 SER B OG  1 
ATOM   3468 N N   . LEU A 1 462 ? 36.496 143.799 -51.706 1.00 31.43  ? 518 LEU B N   1 
ATOM   3469 C CA  . LEU A 1 462 ? 37.280 142.615 -51.404 1.00 35.65  ? 518 LEU B CA  1 
ATOM   3470 C C   . LEU A 1 462 ? 38.560 143.068 -50.716 1.00 45.38  ? 518 LEU B C   1 
ATOM   3471 O O   . LEU A 1 462 ? 39.359 143.789 -51.312 1.00 56.01  ? 518 LEU B O   1 
ATOM   3472 C CB  . LEU A 1 462 ? 37.609 141.901 -52.718 1.00 31.63  ? 518 LEU B CB  1 
ATOM   3473 C CG  . LEU A 1 462 ? 37.876 140.395 -52.768 1.00 34.35  ? 518 LEU B CG  1 
ATOM   3474 C CD1 . LEU A 1 462 ? 36.593 139.619 -52.559 1.00 37.99  ? 518 LEU B CD1 1 
ATOM   3475 C CD2 . LEU A 1 462 ? 38.519 140.000 -54.093 1.00 26.02  ? 518 LEU B CD2 1 
ATOM   3476 N N   . LEU A 1 463 ? 38.766 142.671 -49.468 1.00 47.32  ? 519 LEU B N   1 
ATOM   3477 C CA  . LEU A 1 463 ? 39.942 143.144 -48.743 1.00 54.83  ? 519 LEU B CA  1 
ATOM   3478 C C   . LEU A 1 463 ? 40.885 141.974 -48.449 1.00 56.68  ? 519 LEU B C   1 
ATOM   3479 O O   . LEU A 1 463 ? 40.435 140.870 -48.134 1.00 60.13  ? 519 LEU B O   1 
ATOM   3480 C CB  . LEU A 1 463 ? 39.551 143.856 -47.437 1.00 52.26  ? 519 LEU B CB  1 
ATOM   3481 C CG  . LEU A 1 463 ? 38.642 145.093 -47.329 1.00 41.81  ? 519 LEU B CG  1 
ATOM   3482 C CD1 . LEU A 1 463 ? 38.005 145.524 -48.640 1.00 38.09  ? 519 LEU B CD1 1 
ATOM   3483 C CD2 . LEU A 1 463 ? 37.558 144.860 -46.260 1.00 30.09  ? 519 LEU B CD2 1 
ATOM   3484 N N   . GLY A 1 464 ? 42.188 142.211 -48.555 1.00 49.19  ? 520 GLY B N   1 
ATOM   3485 C CA  . GLY A 1 464 ? 43.161 141.200 -48.190 1.00 50.95  ? 520 GLY B CA  1 
ATOM   3486 C C   . GLY A 1 464 ? 43.071 140.886 -46.707 1.00 60.36  ? 520 GLY B C   1 
ATOM   3487 O O   . GLY A 1 464 ? 43.334 139.760 -46.284 1.00 60.88  ? 520 GLY B O   1 
ATOM   3488 N N   . THR A 1 465 ? 42.686 141.894 -45.922 1.00 61.90  ? 521 THR B N   1 
ATOM   3489 C CA  . THR A 1 465 ? 42.504 141.767 -44.473 1.00 62.20  ? 521 THR B CA  1 
ATOM   3490 C C   . THR A 1 465 ? 41.348 140.834 -44.120 1.00 48.93  ? 521 THR B C   1 
ATOM   3491 O O   . THR A 1 465 ? 41.209 140.371 -42.984 1.00 41.14  ? 521 THR B O   1 
ATOM   3492 C CB  . THR A 1 465 ? 42.187 143.137 -43.847 1.00 72.17  ? 521 THR B CB  1 
ATOM   3493 O OG1 . THR A 1 465 ? 41.087 143.736 -44.549 1.00 75.57  ? 521 THR B OG1 1 
ATOM   3494 C CG2 . THR A 1 465 ? 43.401 144.061 -43.921 1.00 74.33  ? 521 THR B CG2 1 
ATOM   3495 N N   . THR A 1 466 ? 40.507 140.582 -45.109 1.00 38.80  ? 522 THR B N   1 
ATOM   3496 C CA  . THR A 1 466 ? 39.309 139.812 -44.905 1.00 39.73  ? 522 THR B CA  1 
ATOM   3497 C C   . THR A 1 466 ? 39.599 138.308 -45.011 1.00 47.09  ? 522 THR B C   1 
ATOM   3498 O O   . THR A 1 466 ? 38.796 137.492 -44.573 1.00 54.39  ? 522 THR B O   1 
ATOM   3499 C CB  . THR A 1 466 ? 38.225 140.284 -45.900 1.00 46.33  ? 522 THR B CB  1 
ATOM   3500 O OG1 . THR A 1 466 ? 38.035 141.699 -45.749 1.00 45.61  ? 522 THR B OG1 1 
ATOM   3501 C CG2 . THR A 1 466 ? 36.902 139.574 -45.677 1.00 48.07  ? 522 THR B CG2 1 
ATOM   3502 N N   . LEU A 1 467 ? 40.768 137.932 -45.533 1.00 42.79  ? 523 LEU B N   1 
ATOM   3503 C CA  . LEU A 1 467 ? 41.034 136.512 -45.807 1.00 32.67  ? 523 LEU B CA  1 
ATOM   3504 C C   . LEU A 1 467 ? 42.216 135.935 -45.026 1.00 30.31  ? 523 LEU B C   1 
ATOM   3505 O O   . LEU A 1 467 ? 43.238 136.601 -44.858 1.00 26.44  ? 523 LEU B O   1 
ATOM   3506 C CB  . LEU A 1 467 ? 41.279 136.309 -47.303 1.00 28.82  ? 523 LEU B CB  1 
ATOM   3507 C CG  . LEU A 1 467 ? 40.186 136.778 -48.276 1.00 25.72  ? 523 LEU B CG  1 
ATOM   3508 C CD1 . LEU A 1 467 ? 40.664 136.670 -49.720 1.00 24.77  ? 523 LEU B CD1 1 
ATOM   3509 C CD2 . LEU A 1 467 ? 38.892 135.997 -48.076 1.00 22.16  ? 523 LEU B CD2 1 
ATOM   3510 N N   . PRO A 1 468 ? 42.081 134.680 -44.552 1.00 27.10  ? 524 PRO B N   1 
ATOM   3511 C CA  . PRO A 1 468 ? 43.173 134.027 -43.812 1.00 19.41  ? 524 PRO B CA  1 
ATOM   3512 C C   . PRO A 1 468 ? 44.295 133.555 -44.728 1.00 22.86  ? 524 PRO B C   1 
ATOM   3513 O O   . PRO A 1 468 ? 44.010 133.025 -45.805 1.00 28.33  ? 524 PRO B O   1 
ATOM   3514 C CB  . PRO A 1 468 ? 42.481 132.848 -43.105 1.00 17.44  ? 524 PRO B CB  1 
ATOM   3515 C CG  . PRO A 1 468 ? 41.218 132.607 -43.856 1.00 16.07  ? 524 PRO B CG  1 
ATOM   3516 C CD  . PRO A 1 468 ? 40.824 133.911 -44.509 1.00 22.42  ? 524 PRO B CD  1 
ATOM   3517 N N   . LYS A 1 469 ? 45.543 133.713 -44.286 1.00 24.24  ? 525 LYS B N   1 
ATOM   3518 C CA  . LYS A 1 469 ? 46.724 133.525 -45.135 1.00 26.53  ? 525 LYS B CA  1 
ATOM   3519 C C   . LYS A 1 469 ? 47.077 132.065 -45.420 1.00 29.20  ? 525 LYS B C   1 
ATOM   3520 O O   . LYS A 1 469 ? 47.948 131.770 -46.243 1.00 41.84  ? 525 LYS B O   1 
ATOM   3521 C CB  . LYS A 1 469 ? 47.931 134.245 -44.531 1.00 34.82  ? 525 LYS B CB  1 
ATOM   3522 C CG  . LYS A 1 469 ? 48.005 135.725 -44.871 1.00 43.50  ? 525 LYS B CG  1 
ATOM   3523 C CD  . LYS A 1 469 ? 46.879 136.530 -44.234 1.00 48.00  ? 525 LYS B CD  1 
ATOM   3524 C CE  . LYS A 1 469 ? 46.696 137.867 -44.944 1.00 56.73  ? 525 LYS B CE  1 
ATOM   3525 N NZ  . LYS A 1 469 ? 45.533 138.650 -44.436 1.00 57.47  ? 525 LYS B NZ  1 
ATOM   3526 N N   . SER A 1 470 ? 46.384 131.159 -44.745 1.00 19.29  ? 526 SER B N   1 
ATOM   3527 C CA  . SER A 1 470 ? 46.509 129.730 -44.992 1.00 18.20  ? 526 SER B CA  1 
ATOM   3528 C C   . SER A 1 470 ? 45.686 129.277 -46.202 1.00 20.40  ? 526 SER B C   1 
ATOM   3529 O O   . SER A 1 470 ? 45.684 128.090 -46.531 1.00 23.07  ? 526 SER B O   1 
ATOM   3530 C CB  . SER A 1 470 ? 46.006 128.959 -43.770 1.00 19.03  ? 526 SER B CB  1 
ATOM   3531 O OG  . SER A 1 470 ? 44.604 129.168 -43.607 1.00 18.53  ? 526 SER B OG  1 
ATOM   3532 N N   . LEU A 1 471 ? 44.967 130.197 -46.849 1.00 16.83  ? 527 LEU B N   1 
ATOM   3533 C CA  . LEU A 1 471 ? 44.165 129.827 -48.031 1.00 17.45  ? 527 LEU B CA  1 
ATOM   3534 C C   . LEU A 1 471 ? 44.965 129.267 -49.205 1.00 13.23  ? 527 LEU B C   1 
ATOM   3535 O O   . LEU A 1 471 ? 46.004 129.788 -49.579 1.00 14.61  ? 527 LEU B O   1 
ATOM   3536 C CB  . LEU A 1 471 ? 43.285 130.984 -48.493 1.00 21.40  ? 527 LEU B CB  1 
ATOM   3537 C CG  . LEU A 1 471 ? 41.903 130.921 -47.843 1.00 22.98  ? 527 LEU B CG  1 
ATOM   3538 C CD1 . LEU A 1 471 ? 41.076 132.189 -48.100 1.00 12.21  ? 527 LEU B CD1 1 
ATOM   3539 C CD2 . LEU A 1 471 ? 41.199 129.676 -48.367 1.00 21.99  ? 527 LEU B CD2 1 
ATOM   3540 N N   . LYS A 1 472 ? 44.451 128.184 -49.765 1.00 25.73  ? 528 LYS B N   1 
ATOM   3541 C CA  . LYS A 1 472 ? 45.043 127.490 -50.907 1.00 22.80  ? 528 LYS B CA  1 
ATOM   3542 C C   . LYS A 1 472 ? 44.164 127.673 -52.143 1.00 25.77  ? 528 LYS B C   1 
ATOM   3543 O O   . LYS A 1 472 ? 44.650 128.014 -53.225 1.00 26.16  ? 528 LYS B O   1 
ATOM   3544 C CB  . LYS A 1 472 ? 45.276 126.004 -50.615 1.00 16.53  ? 528 LYS B CB  1 
ATOM   3545 C CG  . LYS A 1 472 ? 46.325 125.719 -49.546 1.00 15.16  ? 528 LYS B CG  1 
ATOM   3546 C CD  . LYS A 1 472 ? 46.843 124.282 -49.695 1.00 26.02  ? 528 LYS B CD  1 
ATOM   3547 C CE  . LYS A 1 472 ? 47.725 123.845 -48.518 1.00 36.96  ? 528 LYS B CE  1 
ATOM   3548 N NZ  . LYS A 1 472 ? 48.477 124.982 -47.902 1.00 46.55  ? 528 LYS B NZ  1 
ATOM   3549 N N   . PHE A 1 473 ? 42.889 127.322 -52.002 1.00 20.27  ? 529 PHE B N   1 
ATOM   3550 C CA  . PHE A 1 473 ? 41.937 127.418 -53.100 1.00 20.76  ? 529 PHE B CA  1 
ATOM   3551 C C   . PHE A 1 473 ? 40.894 128.511 -52.816 1.00 21.07  ? 529 PHE B C   1 
ATOM   3552 O O   . PHE A 1 473 ? 40.249 128.484 -51.768 1.00 27.38  ? 529 PHE B O   1 
ATOM   3553 C CB  . PHE A 1 473 ? 41.282 126.047 -53.288 1.00 16.04  ? 529 PHE B CB  1 
ATOM   3554 C CG  . PHE A 1 473 ? 40.234 125.992 -54.370 1.00 22.99  ? 529 PHE B CG  1 
ATOM   3555 C CD1 . PHE A 1 473 ? 38.928 126.440 -54.133 1.00 23.36  ? 529 PHE B CD1 1 
ATOM   3556 C CD2 . PHE A 1 473 ? 40.538 125.454 -55.619 1.00 19.53  ? 529 PHE B CD2 1 
ATOM   3557 C CE1 . PHE A 1 473 ? 37.959 126.371 -55.134 1.00 18.34  ? 529 PHE B CE1 1 
ATOM   3558 C CE2 . PHE A 1 473 ? 39.577 125.392 -56.618 1.00 12.52  ? 529 PHE B CE2 1 
ATOM   3559 C CZ  . PHE A 1 473 ? 38.286 125.840 -56.374 1.00 9.99   ? 529 PHE B CZ  1 
ATOM   3560 N N   . ILE A 1 474 ? 40.733 129.467 -53.738 1.00 16.54  ? 530 ILE B N   1 
ATOM   3561 C CA  . ILE A 1 474 ? 39.677 130.490 -53.623 1.00 16.85  ? 530 ILE B CA  1 
ATOM   3562 C C   . ILE A 1 474 ? 38.818 130.546 -54.882 1.00 16.30  ? 530 ILE B C   1 
ATOM   3563 O O   . ILE A 1 474 ? 39.343 130.703 -55.977 1.00 19.97  ? 530 ILE B O   1 
ATOM   3564 C CB  . ILE A 1 474 ? 40.245 131.919 -53.420 1.00 18.05  ? 530 ILE B CB  1 
ATOM   3565 C CG1 . ILE A 1 474 ? 40.839 132.105 -52.027 1.00 17.39  ? 530 ILE B CG1 1 
ATOM   3566 C CG2 . ILE A 1 474 ? 39.157 132.969 -53.619 1.00 11.86  ? 530 ILE B CG2 1 
ATOM   3567 C CD1 . ILE A 1 474 ? 41.573 133.422 -51.874 1.00 12.39  ? 530 ILE B CD1 1 
ATOM   3568 N N   . ASP A 1 475 ? 37.502 130.401 -54.743 1.00 17.55  ? 531 ASP B N   1 
ATOM   3569 C CA  . ASP A 1 475 ? 36.635 130.639 -55.886 1.00 15.70  ? 531 ASP B CA  1 
ATOM   3570 C C   . ASP A 1 475 ? 35.476 131.543 -55.512 1.00 13.07  ? 531 ASP B C   1 
ATOM   3571 O O   . ASP A 1 475 ? 34.498 131.078 -54.946 1.00 15.08  ? 531 ASP B O   1 
ATOM   3572 C CB  . ASP A 1 475 ? 36.079 129.292 -56.342 1.00 17.66  ? 531 ASP B CB  1 
ATOM   3573 C CG  . ASP A 1 475 ? 35.454 129.340 -57.715 1.00 19.51  ? 531 ASP B CG  1 
ATOM   3574 O OD1 . ASP A 1 475 ? 35.215 130.448 -58.243 1.00 16.37  ? 531 ASP B OD1 1 
ATOM   3575 O OD2 . ASP A 1 475 ? 35.196 128.241 -58.257 1.00 26.97  ? 531 ASP B OD2 1 
ATOM   3576 N N   . PHE A 1 476 ? 35.561 132.813 -55.901 1.00 18.63  ? 532 PHE B N   1 
ATOM   3577 C CA  . PHE A 1 476 ? 34.473 133.796 -55.734 1.00 8.66   ? 532 PHE B CA  1 
ATOM   3578 C C   . PHE A 1 476 ? 33.707 134.082 -57.017 1.00 10.89  ? 532 PHE B C   1 
ATOM   3579 O O   . PHE A 1 476 ? 32.965 135.050 -57.094 1.00 11.65  ? 532 PHE B O   1 
ATOM   3580 C CB  . PHE A 1 476 ? 34.954 135.091 -55.101 1.00 9.45   ? 532 PHE B CB  1 
ATOM   3581 C CG  . PHE A 1 476 ? 35.528 134.914 -53.728 1.00 14.38  ? 532 PHE B CG  1 
ATOM   3582 C CD1 . PHE A 1 476 ? 35.261 133.777 -52.992 1.00 18.14  ? 532 PHE B CD1 1 
ATOM   3583 C CD2 . PHE A 1 476 ? 36.342 135.888 -53.174 1.00 18.23  ? 532 PHE B CD2 1 
ATOM   3584 C CE1 . PHE A 1 476 ? 35.803 133.611 -51.730 1.00 23.97  ? 532 PHE B CE1 1 
ATOM   3585 C CE2 . PHE A 1 476 ? 36.880 135.731 -51.924 1.00 16.28  ? 532 PHE B CE2 1 
ATOM   3586 C CZ  . PHE A 1 476 ? 36.609 134.590 -51.197 1.00 24.40  ? 532 PHE B CZ  1 
ATOM   3587 N N   . SER A 1 477 ? 33.953 133.294 -58.053 1.00 10.15  ? 533 SER B N   1 
ATOM   3588 C CA  . SER A 1 477 ? 33.384 133.586 -59.358 1.00 8.85   ? 533 SER B CA  1 
ATOM   3589 C C   . SER A 1 477 ? 31.860 133.596 -59.430 1.00 11.78  ? 533 SER B C   1 
ATOM   3590 O O   . SER A 1 477 ? 31.173 133.016 -58.597 1.00 6.77   ? 533 SER B O   1 
ATOM   3591 C CB  . SER A 1 477 ? 33.950 132.647 -60.423 1.00 11.20  ? 533 SER B CB  1 
ATOM   3592 O OG  . SER A 1 477 ? 33.782 131.287 -60.083 1.00 10.83  ? 533 SER B OG  1 
ATOM   3593 N N   . ASP A 1 478 ? 31.352 134.294 -60.441 1.00 15.57  ? 534 ASP B N   1 
ATOM   3594 C CA  . ASP A 1 478 ? 29.924 134.405 -60.695 1.00 8.20   ? 534 ASP B CA  1 
ATOM   3595 C C   . ASP A 1 478 ? 29.207 135.006 -59.496 1.00 10.35  ? 534 ASP B C   1 
ATOM   3596 O O   . ASP A 1 478 ? 28.332 134.391 -58.889 1.00 9.71   ? 534 ASP B O   1 
ATOM   3597 C CB  . ASP A 1 478 ? 29.349 133.040 -61.077 1.00 6.58   ? 534 ASP B CB  1 
ATOM   3598 C CG  . ASP A 1 478 ? 27.967 133.131 -61.663 1.00 18.42  ? 534 ASP B CG  1 
ATOM   3599 O OD1 . ASP A 1 478 ? 27.493 134.265 -61.908 1.00 24.61  ? 534 ASP B OD1 1 
ATOM   3600 O OD2 . ASP A 1 478 ? 27.358 132.058 -61.888 1.00 22.78  ? 534 ASP B OD2 1 
ATOM   3601 N N   . ASN A 1 479 ? 29.583 136.243 -59.189 1.00 19.44  ? 535 ASN B N   1 
ATOM   3602 C CA  . ASN A 1 479 ? 28.966 137.029 -58.136 1.00 7.65   ? 535 ASN B CA  1 
ATOM   3603 C C   . ASN A 1 479 ? 28.842 138.450 -58.656 1.00 13.38  ? 535 ASN B C   1 
ATOM   3604 O O   . ASN A 1 479 ? 28.991 138.688 -59.860 1.00 16.54  ? 535 ASN B O   1 
ATOM   3605 C CB  . ASN A 1 479 ? 29.808 136.995 -56.849 1.00 8.06   ? 535 ASN B CB  1 
ATOM   3606 C CG  . ASN A 1 479 ? 29.531 135.753 -55.988 1.00 21.33  ? 535 ASN B CG  1 
ATOM   3607 O OD1 . ASN A 1 479 ? 28.488 135.651 -55.350 1.00 16.13  ? 535 ASN B OD1 1 
ATOM   3608 N ND2 . ASN A 1 479 ? 30.479 134.824 -55.952 1.00 7.50   ? 535 ASN B ND2 1 
ATOM   3609 N N   . ALA A 1 480 ? 28.473 139.365 -57.768 1.00 9.04   ? 536 ALA B N   1 
ATOM   3610 C CA  . ALA A 1 480 ? 28.457 140.815 -58.021 1.00 12.46  ? 536 ALA B CA  1 
ATOM   3611 C C   . ALA A 1 480 ? 29.611 141.627 -57.417 1.00 16.00  ? 536 ALA B C   1 
ATOM   3612 O O   . ALA A 1 480 ? 29.438 142.822 -57.191 1.00 17.89  ? 536 ALA B O   1 
ATOM   3613 C CB  . ALA A 1 480 ? 27.110 141.438 -57.681 1.00 12.75  ? 536 ALA B CB  1 
ATOM   3614 N N   . LEU A 1 481 ? 30.696 140.972 -57.001 1.00 15.69  ? 537 LEU B N   1 
ATOM   3615 C CA  . LEU A 1 481 ? 31.812 141.656 -56.319 1.00 21.39  ? 537 LEU B CA  1 
ATOM   3616 C C   . LEU A 1 481 ? 32.355 142.838 -57.120 1.00 23.15  ? 537 LEU B C   1 
ATOM   3617 O O   . LEU A 1 481 ? 32.302 142.833 -58.352 1.00 22.93  ? 537 LEU B O   1 
ATOM   3618 C CB  . LEU A 1 481 ? 32.968 140.688 -56.039 1.00 10.92  ? 537 LEU B CB  1 
ATOM   3619 C CG  . LEU A 1 481 ? 32.750 139.561 -55.035 1.00 16.91  ? 537 LEU B CG  1 
ATOM   3620 C CD1 . LEU A 1 481 ? 34.020 138.734 -54.853 1.00 11.22  ? 537 LEU B CD1 1 
ATOM   3621 C CD2 . LEU A 1 481 ? 32.250 140.096 -53.712 1.00 10.71  ? 537 LEU B CD2 1 
ATOM   3622 N N   . SER A 1 482 ? 32.874 143.852 -56.423 1.00 26.27  ? 538 SER B N   1 
ATOM   3623 C CA  . SER A 1 482 ? 33.367 145.058 -57.100 1.00 24.41  ? 538 SER B CA  1 
ATOM   3624 C C   . SER A 1 482 ? 34.549 145.788 -56.450 1.00 18.78  ? 538 SER B C   1 
ATOM   3625 O O   . SER A 1 482 ? 35.194 145.295 -55.530 1.00 19.30  ? 538 SER B O   1 
ATOM   3626 C CB  . SER A 1 482 ? 32.229 146.058 -57.355 1.00 28.57  ? 538 SER B CB  1 
ATOM   3627 O OG  . SER A 1 482 ? 31.783 146.643 -56.142 1.00 36.10  ? 538 SER B OG  1 
ATOM   3628 N N   . SER A 1 483 ? 34.784 146.989 -56.966 1.00 23.33  ? 539 SER B N   1 
ATOM   3629 C CA  . SER A 1 483 ? 35.981 147.792 -56.747 1.00 28.06  ? 539 SER B CA  1 
ATOM   3630 C C   . SER A 1 483 ? 37.264 147.058 -57.134 1.00 29.04  ? 539 SER B C   1 
ATOM   3631 O O   . SER A 1 483 ? 37.247 146.208 -58.017 1.00 31.44  ? 539 SER B O   1 
ATOM   3632 C CB  . SER A 1 483 ? 36.051 148.265 -55.292 1.00 30.18  ? 539 SER B CB  1 
ATOM   3633 O OG  . SER A 1 483 ? 36.580 149.578 -55.216 1.00 32.15  ? 539 SER B OG  1 
ATOM   3634 N N   . THR A 1 484 ? 38.354 147.307 -56.417 1.00 30.63  ? 540 THR B N   1 
ATOM   3635 C CA  . THR A 1 484 ? 39.650 146.831 -56.890 1.00 35.06  ? 540 THR B CA  1 
ATOM   3636 C C   . THR A 1 484 ? 40.105 145.579 -56.184 1.00 37.13  ? 540 THR B C   1 
ATOM   3637 O O   . THR A 1 484 ? 39.841 145.378 -54.991 1.00 48.97  ? 540 THR B O   1 
ATOM   3638 C CB  . THR A 1 484 ? 40.799 147.880 -56.745 1.00 49.67  ? 540 THR B CB  1 
ATOM   3639 O OG1 . THR A 1 484 ? 41.156 148.032 -55.362 1.00 43.39  ? 540 THR B OG1 1 
ATOM   3640 C CG2 . THR A 1 484 ? 40.421 149.223 -57.365 1.00 18.07  ? 540 THR B CG2 1 
ATOM   3641 N N   . LEU A 1 485 ? 40.790 144.736 -56.945 1.00 24.09  ? 541 LEU B N   1 
ATOM   3642 C CA  . LEU A 1 485 ? 41.511 143.628 -56.369 1.00 27.72  ? 541 LEU B CA  1 
ATOM   3643 C C   . LEU A 1 485 ? 42.520 144.227 -55.388 1.00 39.92  ? 541 LEU B C   1 
ATOM   3644 O O   . LEU A 1 485 ? 43.393 145.002 -55.779 1.00 42.69  ? 541 LEU B O   1 
ATOM   3645 C CB  . LEU A 1 485 ? 42.197 142.831 -57.469 1.00 23.09  ? 541 LEU B CB  1 
ATOM   3646 C CG  . LEU A 1 485 ? 42.836 141.512 -57.056 1.00 27.54  ? 541 LEU B CG  1 
ATOM   3647 C CD1 . LEU A 1 485 ? 41.818 140.619 -56.390 1.00 29.38  ? 541 LEU B CD1 1 
ATOM   3648 C CD2 . LEU A 1 485 ? 43.424 140.833 -58.260 1.00 21.32  ? 541 LEU B CD2 1 
ATOM   3649 N N   . PRO A 1 486 ? 42.374 143.889 -54.096 1.00 44.83  ? 542 PRO B N   1 
ATOM   3650 C CA  . PRO A 1 486 ? 43.155 144.497 -53.016 1.00 42.73  ? 542 PRO B CA  1 
ATOM   3651 C C   . PRO A 1 486 ? 44.612 144.090 -53.089 1.00 42.33  ? 542 PRO B C   1 
ATOM   3652 O O   . PRO A 1 486 ? 44.912 142.921 -53.327 1.00 41.65  ? 542 PRO B O   1 
ATOM   3653 C CB  . PRO A 1 486 ? 42.526 143.897 -51.764 1.00 46.87  ? 542 PRO B CB  1 
ATOM   3654 C CG  . PRO A 1 486 ? 42.026 142.563 -52.217 1.00 49.23  ? 542 PRO B CG  1 
ATOM   3655 C CD  . PRO A 1 486 ? 41.490 142.822 -53.596 1.00 46.06  ? 542 PRO B CD  1 
ATOM   3656 N N   . PRO A 1 487 ? 45.519 145.048 -52.876 1.00 41.89  ? 543 PRO B N   1 
ATOM   3657 C CA  . PRO A 1 487 ? 46.954 144.751 -52.872 1.00 40.84  ? 543 PRO B CA  1 
ATOM   3658 C C   . PRO A 1 487 ? 47.297 143.671 -51.839 1.00 44.96  ? 543 PRO B C   1 
ATOM   3659 O O   . PRO A 1 487 ? 48.248 142.900 -52.030 1.00 41.14  ? 543 PRO B O   1 
ATOM   3660 C CB  . PRO A 1 487 ? 47.593 146.099 -52.508 1.00 33.95  ? 543 PRO B CB  1 
ATOM   3661 C CG  . PRO A 1 487 ? 46.488 146.938 -51.963 1.00 34.44  ? 543 PRO B CG  1 
ATOM   3662 C CD  . PRO A 1 487 ? 45.237 146.468 -52.611 1.00 37.99  ? 543 PRO B CD  1 
ATOM   3663 N N   . GLY A 1 488 ? 46.479 143.584 -50.788 1.00 45.23  ? 544 GLY B N   1 
ATOM   3664 C CA  . GLY A 1 488 ? 46.662 142.617 -49.717 1.00 39.95  ? 544 GLY B CA  1 
ATOM   3665 C C   . GLY A 1 488 ? 46.581 141.182 -50.204 1.00 37.73  ? 544 GLY B C   1 
ATOM   3666 O O   . GLY A 1 488 ? 46.865 140.230 -49.466 1.00 37.85  ? 544 GLY B O   1 
ATOM   3667 N N   . ILE A 1 489 ? 46.190 141.026 -51.462 1.00 31.99  ? 545 ILE B N   1 
ATOM   3668 C CA  . ILE A 1 489 ? 46.137 139.714 -52.072 1.00 31.91  ? 545 ILE B CA  1 
ATOM   3669 C C   . ILE A 1 489 ? 47.536 139.111 -52.061 1.00 31.69  ? 545 ILE B C   1 
ATOM   3670 O O   . ILE A 1 489 ? 47.695 137.893 -52.053 1.00 32.63  ? 545 ILE B O   1 
ATOM   3671 C CB  . ILE A 1 489 ? 45.564 139.788 -53.511 1.00 35.72  ? 545 ILE B CB  1 
ATOM   3672 C CG1 . ILE A 1 489 ? 45.106 138.409 -53.980 1.00 33.84  ? 545 ILE B CG1 1 
ATOM   3673 C CG2 . ILE A 1 489 ? 46.566 140.433 -54.488 1.00 30.45  ? 545 ILE B CG2 1 
ATOM   3674 C CD1 . ILE A 1 489 ? 46.167 137.631 -54.736 1.00 39.82  ? 545 ILE B CD1 1 
ATOM   3675 N N   . GLY A 1 490 ? 48.551 139.973 -52.029 1.00 30.68  ? 546 GLY B N   1 
ATOM   3676 C CA  . GLY A 1 490 ? 49.927 139.515 -52.015 1.00 30.96  ? 546 GLY B CA  1 
ATOM   3677 C C   . GLY A 1 490 ? 50.296 138.775 -50.742 1.00 40.44  ? 546 GLY B C   1 
ATOM   3678 O O   . GLY A 1 490 ? 51.316 138.089 -50.688 1.00 45.05  ? 546 GLY B O   1 
ATOM   3679 N N   . LEU A 1 491 ? 49.468 138.900 -49.709 1.00 41.87  ? 547 LEU B N   1 
ATOM   3680 C CA  . LEU A 1 491 ? 49.799 138.293 -48.427 1.00 37.53  ? 547 LEU B CA  1 
ATOM   3681 C C   . LEU A 1 491 ? 49.492 136.812 -48.391 1.00 39.77  ? 547 LEU B C   1 
ATOM   3682 O O   . LEU A 1 491 ? 49.985 136.105 -47.515 1.00 44.74  ? 547 LEU B O   1 
ATOM   3683 C CB  . LEU A 1 491 ? 49.066 138.991 -47.290 1.00 39.02  ? 547 LEU B CB  1 
ATOM   3684 C CG  . LEU A 1 491 ? 49.522 140.424 -47.059 1.00 40.88  ? 547 LEU B CG  1 
ATOM   3685 C CD1 . LEU A 1 491 ? 48.726 141.049 -45.931 1.00 41.49  ? 547 LEU B CD1 1 
ATOM   3686 C CD2 . LEU A 1 491 ? 51.009 140.433 -46.763 1.00 34.16  ? 547 LEU B CD2 1 
ATOM   3687 N N   . LEU A 1 492 ? 48.694 136.322 -49.338 1.00 34.97  ? 548 LEU B N   1 
ATOM   3688 C CA  . LEU A 1 492 ? 48.370 134.911 -49.292 1.00 36.01  ? 548 LEU B CA  1 
ATOM   3689 C C   . LEU A 1 492 ? 49.438 134.235 -50.120 1.00 40.70  ? 548 LEU B C   1 
ATOM   3690 O O   . LEU A 1 492 ? 49.389 134.244 -51.345 1.00 42.98  ? 548 LEU B O   1 
ATOM   3691 C CB  . LEU A 1 492 ? 46.996 134.660 -49.915 1.00 35.89  ? 548 LEU B CB  1 
ATOM   3692 C CG  . LEU A 1 492 ? 45.853 135.614 -49.554 1.00 36.00  ? 548 LEU B CG  1 
ATOM   3693 C CD1 . LEU A 1 492 ? 44.675 135.391 -50.479 1.00 35.41  ? 548 LEU B CD1 1 
ATOM   3694 C CD2 . LEU A 1 492 ? 45.413 135.440 -48.114 1.00 34.56  ? 548 LEU B CD2 1 
ATOM   3695 N N   . THR A 1 493 ? 50.377 133.599 -49.434 1.00 40.19  ? 549 THR B N   1 
ATOM   3696 C CA  . THR A 1 493 ? 51.561 133.055 -50.081 1.00 37.96  ? 549 THR B CA  1 
ATOM   3697 C C   . THR A 1 493 ? 51.336 131.600 -50.432 1.00 35.71  ? 549 THR B C   1 
ATOM   3698 O O   . THR A 1 493 ? 52.133 130.994 -51.149 1.00 34.51  ? 549 THR B O   1 
ATOM   3699 C CB  . THR A 1 493 ? 52.772 133.146 -49.139 1.00 42.21  ? 549 THR B CB  1 
ATOM   3700 O OG1 . THR A 1 493 ? 52.676 132.134 -48.122 1.00 40.92  ? 549 THR B OG1 1 
ATOM   3701 C CG2 . THR A 1 493 ? 52.799 134.506 -48.471 1.00 46.46  ? 549 THR B CG2 1 
ATOM   3702 N N   . GLU A 1 494 ? 50.254 131.043 -49.893 1.00 37.31  ? 550 GLU B N   1 
ATOM   3703 C CA  . GLU A 1 494 ? 49.936 129.632 -50.055 1.00 33.38  ? 550 GLU B CA  1 
ATOM   3704 C C   . GLU A 1 494 ? 48.963 129.397 -51.199 1.00 27.08  ? 550 GLU B C   1 
ATOM   3705 O O   . GLU A 1 494 ? 48.730 128.264 -51.615 1.00 25.07  ? 550 GLU B O   1 
ATOM   3706 C CB  . GLU A 1 494 ? 49.327 129.106 -48.758 1.00 38.84  ? 550 GLU B CB  1 
ATOM   3707 C CG  . GLU A 1 494 ? 50.106 129.480 -47.504 1.00 47.14  ? 550 GLU B CG  1 
ATOM   3708 C CD  . GLU A 1 494 ? 51.342 128.622 -47.296 1.00 55.76  ? 550 GLU B CD  1 
ATOM   3709 O OE1 . GLU A 1 494 ? 51.980 128.745 -46.225 1.00 63.68  ? 550 GLU B OE1 1 
ATOM   3710 O OE2 . GLU A 1 494 ? 51.674 127.821 -48.194 1.00 54.75  ? 550 GLU B OE2 1 
ATOM   3711 N N   . LEU A 1 495 ? 48.396 130.485 -51.698 1.00 24.39  ? 551 LEU B N   1 
ATOM   3712 C CA  . LEU A 1 495 ? 47.302 130.416 -52.649 1.00 22.17  ? 551 LEU B CA  1 
ATOM   3713 C C   . LEU A 1 495 ? 47.720 129.698 -53.942 1.00 25.70  ? 551 LEU B C   1 
ATOM   3714 O O   . LEU A 1 495 ? 48.719 130.036 -54.579 1.00 30.14  ? 551 LEU B O   1 
ATOM   3715 C CB  . LEU A 1 495 ? 46.790 131.828 -52.928 1.00 27.01  ? 551 LEU B CB  1 
ATOM   3716 C CG  . LEU A 1 495 ? 45.539 131.992 -53.781 1.00 26.58  ? 551 LEU B CG  1 
ATOM   3717 C CD1 . LEU A 1 495 ? 44.363 131.316 -53.093 1.00 28.92  ? 551 LEU B CD1 1 
ATOM   3718 C CD2 . LEU A 1 495 ? 45.272 133.477 -54.008 1.00 21.31  ? 551 LEU B CD2 1 
ATOM   3719 N N   . THR A 1 496 ? 46.935 128.702 -54.315 1.00 30.85  ? 552 THR B N   1 
ATOM   3720 C CA  . THR A 1 496 ? 47.254 127.811 -55.419 1.00 33.68  ? 552 THR B CA  1 
ATOM   3721 C C   . THR A 1 496 ? 46.346 128.091 -56.608 1.00 32.35  ? 552 THR B C   1 
ATOM   3722 O O   . THR A 1 496 ? 46.814 128.344 -57.705 1.00 37.96  ? 552 THR B O   1 
ATOM   3723 C CB  . THR A 1 496 ? 47.154 126.348 -54.976 1.00 34.03  ? 552 THR B CB  1 
ATOM   3724 O OG1 . THR A 1 496 ? 48.273 126.055 -54.131 1.00 35.00  ? 552 THR B OG1 1 
ATOM   3725 C CG2 . THR A 1 496 ? 47.187 125.421 -56.166 1.00 33.79  ? 552 THR B CG2 1 
ATOM   3726 N N   . LYS A 1 497 ? 45.043 127.971 -56.396 1.00 30.85  ? 553 LYS B N   1 
ATOM   3727 C CA  . LYS A 1 497 ? 44.073 128.350 -57.403 1.00 20.08  ? 553 LYS B CA  1 
ATOM   3728 C C   . LYS A 1 497 ? 43.293 129.575 -56.935 1.00 18.24  ? 553 LYS B C   1 
ATOM   3729 O O   . LYS A 1 497 ? 42.824 129.623 -55.796 1.00 18.40  ? 553 LYS B O   1 
ATOM   3730 C CB  . LYS A 1 497 ? 43.143 127.176 -57.689 1.00 17.82  ? 553 LYS B CB  1 
ATOM   3731 C CG  . LYS A 1 497 ? 43.894 125.890 -57.991 1.00 21.98  ? 553 LYS B CG  1 
ATOM   3732 C CD  . LYS A 1 497 ? 42.996 124.812 -58.575 1.00 26.77  ? 553 LYS B CD  1 
ATOM   3733 C CE  . LYS A 1 497 ? 43.800 123.531 -58.814 1.00 28.96  ? 553 LYS B CE  1 
ATOM   3734 N NZ  . LYS A 1 497 ? 43.008 122.440 -59.473 1.00 30.99  ? 553 LYS B NZ  1 
ATOM   3735 N N   . LEU A 1 498 ? 43.179 130.570 -57.809 1.00 18.83  ? 554 LEU B N   1 
ATOM   3736 C CA  . LEU A 1 498 ? 42.430 131.784 -57.508 1.00 11.68  ? 554 LEU B CA  1 
ATOM   3737 C C   . LEU A 1 498 ? 41.489 132.098 -58.653 1.00 22.62  ? 554 LEU B C   1 
ATOM   3738 O O   . LEU A 1 498 ? 41.941 132.378 -59.768 1.00 21.61  ? 554 LEU B O   1 
ATOM   3739 C CB  . LEU A 1 498 ? 43.386 132.950 -57.332 1.00 12.63  ? 554 LEU B CB  1 
ATOM   3740 C CG  . LEU A 1 498 ? 42.751 134.333 -57.253 1.00 21.00  ? 554 LEU B CG  1 
ATOM   3741 C CD1 . LEU A 1 498 ? 41.695 134.351 -56.163 1.00 20.87  ? 554 LEU B CD1 1 
ATOM   3742 C CD2 . LEU A 1 498 ? 43.824 135.382 -56.979 1.00 13.78  ? 554 LEU B CD2 1 
ATOM   3743 N N   . ASN A 1 499 ? 40.185 132.055 -58.388 1.00 24.01  ? 555 ASN B N   1 
ATOM   3744 C CA  . ASN A 1 499 ? 39.208 132.332 -59.431 1.00 10.01  ? 555 ASN B CA  1 
ATOM   3745 C C   . ASN A 1 499 ? 38.179 133.390 -59.027 1.00 15.65  ? 555 ASN B C   1 
ATOM   3746 O O   . ASN A 1 499 ? 37.273 133.143 -58.217 1.00 16.58  ? 555 ASN B O   1 
ATOM   3747 C CB  . ASN A 1 499 ? 38.529 131.026 -59.839 1.00 9.20   ? 555 ASN B CB  1 
ATOM   3748 C CG  . ASN A 1 499 ? 37.481 131.221 -60.914 1.00 24.60  ? 555 ASN B CG  1 
ATOM   3749 O OD1 . ASN A 1 499 ? 37.288 132.320 -61.428 1.00 27.01  ? 555 ASN B OD1 1 
ATOM   3750 N ND2 . ASN A 1 499 ? 36.799 130.149 -61.261 1.00 8.00   ? 555 ASN B ND2 1 
ATOM   3751 N N   . LEU A 1 500 ? 38.352 134.566 -59.629 1.00 14.37  ? 556 LEU B N   1 
ATOM   3752 C CA  . LEU A 1 500 ? 37.532 135.767 -59.434 1.00 12.33  ? 556 LEU B CA  1 
ATOM   3753 C C   . LEU A 1 500 ? 36.571 136.112 -60.566 1.00 18.24  ? 556 LEU B C   1 
ATOM   3754 O O   . LEU A 1 500 ? 36.070 137.244 -60.624 1.00 17.33  ? 556 LEU B O   1 
ATOM   3755 C CB  . LEU A 1 500 ? 38.415 136.958 -59.127 1.00 16.09  ? 556 LEU B CB  1 
ATOM   3756 C CG  . LEU A 1 500 ? 39.146 136.729 -57.811 1.00 24.22  ? 556 LEU B CG  1 
ATOM   3757 C CD1 . LEU A 1 500 ? 40.185 137.801 -57.629 1.00 26.15  ? 556 LEU B CD1 1 
ATOM   3758 C CD2 . LEU A 1 500 ? 38.163 136.695 -56.628 1.00 22.04  ? 556 LEU B CD2 1 
ATOM   3759 N N   . ALA A 1 501 ? 36.417 135.196 -61.518 1.00 9.55   ? 557 ALA B N   1 
ATOM   3760 C CA  . ALA A 1 501 ? 35.778 135.501 -62.803 1.00 9.31   ? 557 ALA B CA  1 
ATOM   3761 C C   . ALA A 1 501 ? 34.301 135.848 -62.707 1.00 18.98  ? 557 ALA B C   1 
ATOM   3762 O O   . ALA A 1 501 ? 33.637 135.526 -61.720 1.00 13.22  ? 557 ALA B O   1 
ATOM   3763 C CB  . ALA A 1 501 ? 35.978 134.347 -63.795 1.00 8.93   ? 557 ALA B CB  1 
ATOM   3764 N N   . LYS A 1 502 ? 33.796 136.509 -63.748 1.00 20.18  ? 558 LYS B N   1 
ATOM   3765 C CA  . LYS A 1 502 ? 32.385 136.863 -63.834 1.00 15.55  ? 558 LYS B CA  1 
ATOM   3766 C C   . LYS A 1 502 ? 31.962 137.643 -62.600 1.00 12.56  ? 558 LYS B C   1 
ATOM   3767 O O   . LYS A 1 502 ? 31.061 137.242 -61.856 1.00 11.54  ? 558 LYS B O   1 
ATOM   3768 C CB  . LYS A 1 502 ? 31.505 135.632 -64.061 1.00 7.52   ? 558 LYS B CB  1 
ATOM   3769 C CG  . LYS A 1 502 ? 30.162 135.969 -64.656 1.00 35.43  ? 558 LYS B CG  1 
ATOM   3770 C CD  . LYS A 1 502 ? 29.420 134.709 -65.058 1.00 42.07  ? 558 LYS B CD  1 
ATOM   3771 C CE  . LYS A 1 502 ? 28.276 135.029 -66.028 1.00 50.29  ? 558 LYS B CE  1 
ATOM   3772 N NZ  . LYS A 1 502 ? 27.359 136.081 -65.507 1.00 49.03  ? 558 LYS B NZ  1 
ATOM   3773 N N   . ASN A 1 503 ? 32.681 138.735 -62.367 1.00 18.41  ? 559 ASN B N   1 
ATOM   3774 C CA  . ASN A 1 503 ? 32.324 139.727 -61.362 1.00 14.28  ? 559 ASN B CA  1 
ATOM   3775 C C   . ASN A 1 503 ? 32.372 141.135 -61.954 1.00 23.98  ? 559 ASN B C   1 
ATOM   3776 O O   . ASN A 1 503 ? 32.552 141.309 -63.166 1.00 33.13  ? 559 ASN B O   1 
ATOM   3777 C CB  . ASN A 1 503 ? 33.233 139.599 -60.138 1.00 13.81  ? 559 ASN B CB  1 
ATOM   3778 C CG  . ASN A 1 503 ? 32.754 138.524 -59.173 1.00 22.49  ? 559 ASN B CG  1 
ATOM   3779 O OD1 . ASN A 1 503 ? 31.725 138.693 -58.531 1.00 24.85  ? 559 ASN B OD1 1 
ATOM   3780 N ND2 . ASN A 1 503 ? 33.497 137.419 -59.066 1.00 9.37   ? 559 ASN B ND2 1 
ATOM   3781 N N   . ARG A 1 504 ? 32.150 142.127 -61.105 1.00 20.25  ? 560 ARG B N   1 
ATOM   3782 C CA  . ARG A 1 504 ? 32.236 143.544 -61.475 1.00 24.04  ? 560 ARG B CA  1 
ATOM   3783 C C   . ARG A 1 504 ? 33.548 144.248 -61.102 1.00 24.01  ? 560 ARG B C   1 
ATOM   3784 O O   . ARG A 1 504 ? 33.568 145.468 -60.975 1.00 29.59  ? 560 ARG B O   1 
ATOM   3785 C CB  . ARG A 1 504 ? 31.016 144.332 -61.002 1.00 30.57  ? 560 ARG B CB  1 
ATOM   3786 C CG  . ARG A 1 504 ? 29.740 143.969 -61.741 1.00 38.89  ? 560 ARG B CG  1 
ATOM   3787 C CD  . ARG A 1 504 ? 28.695 143.410 -60.789 1.00 50.06  ? 560 ARG B CD  1 
ATOM   3788 N NE  . ARG A 1 504 ? 27.457 143.036 -61.477 1.00 62.65  ? 560 ARG B NE  1 
ATOM   3789 C CZ  . ARG A 1 504 ? 27.229 141.851 -62.053 1.00 63.91  ? 560 ARG B CZ  1 
ATOM   3790 N NH1 . ARG A 1 504 ? 28.154 140.893 -62.046 1.00 57.21  ? 560 ARG B NH1 1 
ATOM   3791 N NH2 . ARG A 1 504 ? 26.064 141.624 -62.644 1.00 65.48  ? 560 ARG B NH2 1 
ATOM   3792 N N   . LEU A 1 505 ? 34.585 143.482 -60.776 1.00 18.03  ? 561 LEU B N   1 
ATOM   3793 C CA  . LEU A 1 505 ? 35.883 144.036 -60.349 1.00 18.89  ? 561 LEU B CA  1 
ATOM   3794 C C   . LEU A 1 505 ? 36.551 145.012 -61.364 1.00 25.79  ? 561 LEU B C   1 
ATOM   3795 O O   . LEU A 1 505 ? 36.443 144.828 -62.582 1.00 22.73  ? 561 LEU B O   1 
ATOM   3796 C CB  . LEU A 1 505 ? 36.841 142.876 -59.992 1.00 17.39  ? 561 LEU B CB  1 
ATOM   3797 C CG  . LEU A 1 505 ? 36.502 142.012 -58.757 1.00 22.10  ? 561 LEU B CG  1 
ATOM   3798 C CD1 . LEU A 1 505 ? 37.367 140.749 -58.643 1.00 19.34  ? 561 LEU B CD1 1 
ATOM   3799 C CD2 . LEU A 1 505 ? 36.628 142.823 -57.473 1.00 21.67  ? 561 LEU B CD2 1 
ATOM   3800 N N   . SER A 1 506 ? 37.252 146.034 -60.859 1.00 22.36  ? 562 SER B N   1 
ATOM   3801 C CA  . SER A 1 506 ? 37.878 147.056 -61.718 1.00 21.80  ? 562 SER B CA  1 
ATOM   3802 C C   . SER A 1 506 ? 39.267 147.537 -61.267 1.00 23.61  ? 562 SER B C   1 
ATOM   3803 O O   . SER A 1 506 ? 39.828 147.047 -60.286 1.00 21.10  ? 562 SER B O   1 
ATOM   3804 C CB  . SER A 1 506 ? 36.957 148.263 -61.857 1.00 22.31  ? 562 SER B CB  1 
ATOM   3805 O OG  . SER A 1 506 ? 36.697 148.821 -60.578 1.00 36.04  ? 562 SER B OG  1 
ATOM   3806 N N   . GLY A 1 507 ? 39.819 148.506 -62.000 1.00 25.58  ? 563 GLY B N   1 
ATOM   3807 C CA  . GLY A 1 507 ? 41.172 148.987 -61.743 1.00 21.01  ? 563 GLY B CA  1 
ATOM   3808 C C   . GLY A 1 507 ? 42.237 148.109 -62.386 1.00 24.02  ? 563 GLY B C   1 
ATOM   3809 O O   . GLY A 1 507 ? 41.910 147.267 -63.223 1.00 22.22  ? 563 GLY B O   1 
ATOM   3810 N N   . GLU A 1 508 ? 43.501 148.307 -62.006 1.00 29.65  ? 564 GLU B N   1 
ATOM   3811 C CA  . GLU A 1 508 ? 44.610 147.492 -62.508 1.00 34.90  ? 564 GLU B CA  1 
ATOM   3812 C C   . GLU A 1 508 ? 44.751 146.187 -61.741 1.00 36.26  ? 564 GLU B C   1 
ATOM   3813 O O   . GLU A 1 508 ? 44.087 145.966 -60.729 1.00 45.55  ? 564 GLU B O   1 
ATOM   3814 C CB  . GLU A 1 508 ? 45.937 148.237 -62.339 1.00 42.30  ? 564 GLU B CB  1 
ATOM   3815 C CG  . GLU A 1 508 ? 46.506 148.890 -63.579 1.00 58.69  ? 564 GLU B CG  1 
ATOM   3816 C CD  . GLU A 1 508 ? 45.989 150.297 -63.765 1.00 70.49  ? 564 GLU B CD  1 
ATOM   3817 O OE1 . GLU A 1 508 ? 44.880 150.577 -63.256 1.00 77.09  ? 564 GLU B OE1 1 
ATOM   3818 O OE2 . GLU A 1 508 ? 46.686 151.118 -64.405 1.00 68.40  ? 564 GLU B OE2 1 
ATOM   3819 N N   . ILE A 1 509 ? 45.669 145.350 -62.209 1.00 31.99  ? 565 ILE B N   1 
ATOM   3820 C CA  . ILE A 1 509 ? 46.132 144.197 -61.460 1.00 29.92  ? 565 ILE B CA  1 
ATOM   3821 C C   . ILE A 1 509 ? 47.283 144.686 -60.591 1.00 37.53  ? 565 ILE B C   1 
ATOM   3822 O O   . ILE A 1 509 ? 48.313 145.116 -61.116 1.00 43.72  ? 565 ILE B O   1 
ATOM   3823 C CB  . ILE A 1 509 ? 46.658 143.106 -62.404 1.00 23.69  ? 565 ILE B CB  1 
ATOM   3824 C CG1 . ILE A 1 509 ? 45.541 142.584 -63.305 1.00 19.52  ? 565 ILE B CG1 1 
ATOM   3825 C CG2 . ILE A 1 509 ? 47.286 141.965 -61.624 1.00 21.67  ? 565 ILE B CG2 1 
ATOM   3826 C CD1 . ILE A 1 509 ? 46.055 141.699 -64.442 1.00 17.00  ? 565 ILE B CD1 1 
ATOM   3827 N N   . PRO A 1 510 ? 47.109 144.645 -59.260 1.00 34.35  ? 566 PRO B N   1 
ATOM   3828 C CA  . PRO A 1 510 ? 48.135 145.140 -58.342 1.00 33.03  ? 566 PRO B CA  1 
ATOM   3829 C C   . PRO A 1 510 ? 49.407 144.321 -58.471 1.00 41.35  ? 566 PRO B C   1 
ATOM   3830 O O   . PRO A 1 510 ? 49.326 143.102 -58.577 1.00 43.62  ? 566 PRO B O   1 
ATOM   3831 C CB  . PRO A 1 510 ? 47.503 144.916 -56.972 1.00 28.47  ? 566 PRO B CB  1 
ATOM   3832 C CG  . PRO A 1 510 ? 46.530 143.827 -57.175 1.00 29.32  ? 566 PRO B CG  1 
ATOM   3833 C CD  . PRO A 1 510 ? 45.960 144.085 -58.533 1.00 31.12  ? 566 PRO B CD  1 
ATOM   3834 N N   . ARG A 1 511 ? 50.562 144.981 -58.462 1.00 40.79  ? 567 ARG B N   1 
ATOM   3835 C CA  . ARG A 1 511 ? 51.825 144.298 -58.698 1.00 39.04  ? 567 ARG B CA  1 
ATOM   3836 C C   . ARG A 1 511 ? 52.186 143.359 -57.540 1.00 35.55  ? 567 ARG B C   1 
ATOM   3837 O O   . ARG A 1 511 ? 53.009 142.442 -57.688 1.00 29.86  ? 567 ARG B O   1 
ATOM   3838 C CB  . ARG A 1 511 ? 52.925 145.326 -58.966 1.00 45.03  ? 567 ARG B CB  1 
ATOM   3839 C CG  . ARG A 1 511 ? 52.556 146.312 -60.069 1.00 42.78  ? 567 ARG B CG  1 
ATOM   3840 C CD  . ARG A 1 511 ? 53.599 147.406 -60.268 1.00 43.52  ? 567 ARG B CD  1 
ATOM   3841 N NE  . ARG A 1 511 ? 53.085 148.467 -61.132 1.00 47.28  ? 567 ARG B NE  1 
ATOM   3842 C CZ  . ARG A 1 511 ? 53.066 148.411 -62.463 1.00 47.02  ? 567 ARG B CZ  1 
ATOM   3843 N NH1 . ARG A 1 511 ? 53.536 147.343 -63.100 1.00 50.68  ? 567 ARG B NH1 1 
ATOM   3844 N NH2 . ARG A 1 511 ? 52.565 149.422 -63.162 1.00 39.09  ? 567 ARG B NH2 1 
ATOM   3845 N N   . GLU A 1 512 ? 51.532 143.568 -56.398 1.00 37.22  ? 568 GLU B N   1 
ATOM   3846 C CA  . GLU A 1 512 ? 51.722 142.716 -55.225 1.00 39.42  ? 568 GLU B CA  1 
ATOM   3847 C C   . GLU A 1 512 ? 51.356 141.269 -55.537 1.00 42.03  ? 568 GLU B C   1 
ATOM   3848 O O   . GLU A 1 512 ? 51.780 140.342 -54.833 1.00 39.18  ? 568 GLU B O   1 
ATOM   3849 C CB  . GLU A 1 512 ? 50.886 143.226 -54.057 1.00 45.78  ? 568 GLU B CB  1 
ATOM   3850 C CG  . GLU A 1 512 ? 50.079 144.459 -54.382 1.00 53.07  ? 568 GLU B CG  1 
ATOM   3851 C CD  . GLU A 1 512 ? 50.884 145.731 -54.269 1.00 58.37  ? 568 GLU B CD  1 
ATOM   3852 O OE1 . GLU A 1 512 ? 50.302 146.821 -54.442 1.00 59.84  ? 568 GLU B OE1 1 
ATOM   3853 O OE2 . GLU A 1 512 ? 52.098 145.641 -54.004 1.00 63.22  ? 568 GLU B OE2 1 
ATOM   3854 N N   . ILE A 1 513 ? 50.595 141.085 -56.616 1.00 45.09  ? 569 ILE B N   1 
ATOM   3855 C CA  . ILE A 1 513 ? 50.260 139.761 -57.124 1.00 42.22  ? 569 ILE B CA  1 
ATOM   3856 C C   . ILE A 1 513 ? 51.508 138.890 -57.274 1.00 40.92  ? 569 ILE B C   1 
ATOM   3857 O O   . ILE A 1 513 ? 51.440 137.672 -57.086 1.00 42.87  ? 569 ILE B O   1 
ATOM   3858 C CB  . ILE A 1 513 ? 49.492 139.827 -58.482 1.00 35.17  ? 569 ILE B CB  1 
ATOM   3859 C CG1 . ILE A 1 513 ? 48.854 138.477 -58.819 1.00 26.06  ? 569 ILE B CG1 1 
ATOM   3860 C CG2 . ILE A 1 513 ? 50.394 140.289 -59.620 1.00 38.75  ? 569 ILE B CG2 1 
ATOM   3861 C CD1 . ILE A 1 513 ? 47.480 138.308 -58.229 1.00 16.95  ? 569 ILE B CD1 1 
ATOM   3862 N N   . SER A 1 514 ? 52.646 139.515 -57.581 1.00 33.22  ? 570 SER B N   1 
ATOM   3863 C CA  . SER A 1 514 ? 53.879 138.766 -57.830 1.00 38.00  ? 570 SER B CA  1 
ATOM   3864 C C   . SER A 1 514 ? 54.396 138.011 -56.614 1.00 42.70  ? 570 SER B C   1 
ATOM   3865 O O   . SER A 1 514 ? 55.210 137.090 -56.750 1.00 41.93  ? 570 SER B O   1 
ATOM   3866 C CB  . SER A 1 514 ? 54.983 139.686 -58.342 1.00 38.13  ? 570 SER B CB  1 
ATOM   3867 O OG  . SER A 1 514 ? 55.346 140.624 -57.352 1.00 38.57  ? 570 SER B OG  1 
ATOM   3868 N N   . THR A 1 515 ? 53.931 138.392 -55.426 1.00 46.70  ? 571 THR B N   1 
ATOM   3869 C CA  . THR A 1 515 ? 54.425 137.742 -54.214 1.00 43.77  ? 571 THR B CA  1 
ATOM   3870 C C   . THR A 1 515 ? 53.619 136.503 -53.851 1.00 45.60  ? 571 THR B C   1 
ATOM   3871 O O   . THR A 1 515 ? 53.819 135.931 -52.778 1.00 52.29  ? 571 THR B O   1 
ATOM   3872 C CB  . THR A 1 515 ? 54.534 138.694 -53.003 1.00 41.78  ? 571 THR B CB  1 
ATOM   3873 O OG1 . THR A 1 515 ? 53.244 139.209 -52.660 1.00 42.75  ? 571 THR B OG1 1 
ATOM   3874 C CG2 . THR A 1 515 ? 55.475 139.841 -53.314 1.00 40.84  ? 571 THR B CG2 1 
ATOM   3875 N N   . CYS A 1 516 ? 52.700 136.089 -54.725 1.00 38.55  ? 572 CYS B N   1 
ATOM   3876 C CA  . CYS A 1 516 ? 52.010 134.838 -54.473 1.00 33.20  ? 572 CYS B CA  1 
ATOM   3877 C C   . CYS A 1 516 ? 52.836 133.785 -55.180 1.00 33.39  ? 572 CYS B C   1 
ATOM   3878 O O   . CYS A 1 516 ? 52.652 133.518 -56.367 1.00 29.57  ? 572 CYS B O   1 
ATOM   3879 C CB  . CYS A 1 516 ? 50.606 134.866 -55.089 1.00 26.48  ? 572 CYS B CB  1 
ATOM   3880 S SG  . CYS A 1 516 ? 49.444 136.123 -54.450 1.00 37.16  ? 572 CYS B SG  1 
ATOM   3881 N N   . ARG A 1 517 ? 53.659 133.089 -54.415 1.00 32.48  ? 573 ARG B N   1 
ATOM   3882 C CA  . ARG A 1 517 ? 54.711 132.295 -55.027 1.00 41.18  ? 573 ARG B CA  1 
ATOM   3883 C C   . ARG A 1 517 ? 54.191 130.933 -55.423 1.00 37.29  ? 573 ARG B C   1 
ATOM   3884 O O   . ARG A 1 517 ? 54.823 130.214 -56.192 1.00 37.61  ? 573 ARG B O   1 
ATOM   3885 C CB  . ARG A 1 517 ? 55.909 132.172 -54.083 1.00 50.23  ? 573 ARG B CB  1 
ATOM   3886 C CG  . ARG A 1 517 ? 55.545 132.216 -52.600 1.00 58.62  ? 573 ARG B CG  1 
ATOM   3887 C CD  . ARG A 1 517 ? 56.757 131.922 -51.734 1.00 65.66  ? 573 ARG B CD  1 
ATOM   3888 N NE  . ARG A 1 517 ? 56.507 132.166 -50.316 1.00 74.08  ? 573 ARG B NE  1 
ATOM   3889 C CZ  . ARG A 1 517 ? 56.605 133.360 -49.735 1.00 79.53  ? 573 ARG B CZ  1 
ATOM   3890 N NH1 . ARG A 1 517 ? 56.932 134.426 -50.458 1.00 78.44  ? 573 ARG B NH1 1 
ATOM   3891 N NH2 . ARG A 1 517 ? 56.370 133.490 -48.432 1.00 78.67  ? 573 ARG B NH2 1 
ATOM   3892 N N   . SER A 1 518 ? 53.031 130.579 -54.887 1.00 36.10  ? 574 SER B N   1 
ATOM   3893 C CA  . SER A 1 518 ? 52.473 129.254 -55.117 1.00 28.87  ? 574 SER B CA  1 
ATOM   3894 C C   . SER A 1 518 ? 51.418 129.177 -56.220 1.00 24.07  ? 574 SER B C   1 
ATOM   3895 O O   . SER A 1 518 ? 50.923 128.093 -56.522 1.00 25.91  ? 574 SER B O   1 
ATOM   3896 C CB  . SER A 1 518 ? 51.937 128.674 -53.812 1.00 26.98  ? 574 SER B CB  1 
ATOM   3897 O OG  . SER A 1 518 ? 53.005 128.234 -52.988 1.00 34.92  ? 574 SER B OG  1 
ATOM   3898 N N   . LEU A 1 519 ? 51.103 130.303 -56.854 1.00 25.75  ? 575 LEU B N   1 
ATOM   3899 C CA  . LEU A 1 519 ? 49.880 130.371 -57.656 1.00 23.41  ? 575 LEU B CA  1 
ATOM   3900 C C   . LEU A 1 519 ? 49.979 129.605 -58.982 1.00 21.91  ? 575 LEU B C   1 
ATOM   3901 O O   . LEU A 1 519 ? 50.768 129.948 -59.870 1.00 22.65  ? 575 LEU B O   1 
ATOM   3902 C CB  . LEU A 1 519 ? 49.545 131.834 -57.936 1.00 19.51  ? 575 LEU B CB  1 
ATOM   3903 C CG  . LEU A 1 519 ? 48.122 132.127 -58.390 1.00 21.50  ? 575 LEU B CG  1 
ATOM   3904 C CD1 . LEU A 1 519 ? 47.148 131.409 -57.486 1.00 22.37  ? 575 LEU B CD1 1 
ATOM   3905 C CD2 . LEU A 1 519 ? 47.850 133.627 -58.369 1.00 19.06  ? 575 LEU B CD2 1 
ATOM   3906 N N   . GLN A 1 520 ? 49.174 128.549 -59.084 1.00 19.82  ? 576 GLN B N   1 
ATOM   3907 C CA  . GLN A 1 520 ? 49.061 127.736 -60.292 1.00 23.88  ? 576 GLN B CA  1 
ATOM   3908 C C   . GLN A 1 520 ? 47.998 128.202 -61.290 1.00 21.76  ? 576 GLN B C   1 
ATOM   3909 O O   . GLN A 1 520 ? 48.169 128.084 -62.502 1.00 21.20  ? 576 GLN B O   1 
ATOM   3910 C CB  . GLN A 1 520 ? 48.903 126.250 -59.932 1.00 26.06  ? 576 GLN B CB  1 
ATOM   3911 C CG  . GLN A 1 520 ? 50.168 125.615 -59.313 1.00 19.45  ? 576 GLN B CG  1 
ATOM   3912 C CD  . GLN A 1 520 ? 49.932 124.195 -58.786 1.00 27.88  ? 576 GLN B CD  1 
ATOM   3913 O OE1 . GLN A 1 520 ? 49.034 123.492 -59.242 1.00 29.86  ? 576 GLN B OE1 1 
ATOM   3914 N NE2 . GLN A 1 520 ? 50.743 123.775 -57.816 1.00 35.89  ? 576 GLN B NE2 1 
ATOM   3915 N N   . LEU A 1 521 ? 46.884 128.706 -60.771 1.00 23.12  ? 577 LEU B N   1 
ATOM   3916 C CA  . LEU A 1 521 ? 45.747 129.053 -61.613 1.00 17.64  ? 577 LEU B CA  1 
ATOM   3917 C C   . LEU A 1 521 ? 45.259 130.438 -61.288 1.00 17.07  ? 577 LEU B C   1 
ATOM   3918 O O   . LEU A 1 521 ? 44.966 130.735 -60.126 1.00 18.73  ? 577 LEU B O   1 
ATOM   3919 C CB  . LEU A 1 521 ? 44.597 128.073 -61.388 1.00 12.68  ? 577 LEU B CB  1 
ATOM   3920 C CG  . LEU A 1 521 ? 43.341 128.263 -62.259 1.00 19.55  ? 577 LEU B CG  1 
ATOM   3921 C CD1 . LEU A 1 521 ? 42.695 126.916 -62.580 1.00 10.18  ? 577 LEU B CD1 1 
ATOM   3922 C CD2 . LEU A 1 521 ? 42.309 129.194 -61.615 1.00 10.59  ? 577 LEU B CD2 1 
ATOM   3923 N N   . LEU A 1 522 ? 45.120 131.281 -62.306 1.00 16.05  ? 578 LEU B N   1 
ATOM   3924 C CA  . LEU A 1 522 ? 44.538 132.599 -62.058 1.00 15.47  ? 578 LEU B CA  1 
ATOM   3925 C C   . LEU A 1 522 ? 43.450 132.895 -63.066 1.00 14.88  ? 578 LEU B C   1 
ATOM   3926 O O   . LEU A 1 522 ? 43.732 133.056 -64.239 1.00 14.91  ? 578 LEU B O   1 
ATOM   3927 C CB  . LEU A 1 522 ? 45.614 133.687 -62.114 1.00 13.90  ? 578 LEU B CB  1 
ATOM   3928 C CG  . LEU A 1 522 ? 45.113 135.131 -62.028 1.00 16.40  ? 578 LEU B CG  1 
ATOM   3929 C CD1 . LEU A 1 522 ? 44.469 135.396 -60.675 1.00 17.08  ? 578 LEU B CD1 1 
ATOM   3930 C CD2 . LEU A 1 522 ? 46.228 136.131 -62.296 1.00 15.09  ? 578 LEU B CD2 1 
ATOM   3931 N N   . ASN A 1 523 ? 42.206 132.988 -62.614 1.00 17.89  ? 579 ASN B N   1 
ATOM   3932 C CA  . ASN A 1 523 ? 41.137 133.367 -63.518 1.00 11.17  ? 579 ASN B CA  1 
ATOM   3933 C C   . ASN A 1 523 ? 40.533 134.718 -63.145 1.00 11.84  ? 579 ASN B C   1 
ATOM   3934 O O   . ASN A 1 523 ? 39.794 134.832 -62.169 1.00 11.73  ? 579 ASN B O   1 
ATOM   3935 C CB  . ASN A 1 523 ? 40.052 132.298 -63.520 1.00 10.24  ? 579 ASN B CB  1 
ATOM   3936 C CG  . ASN A 1 523 ? 39.051 132.489 -64.641 1.00 19.63  ? 579 ASN B CG  1 
ATOM   3937 O OD1 . ASN A 1 523 ? 39.011 133.538 -65.285 1.00 22.86  ? 579 ASN B OD1 1 
ATOM   3938 N ND2 . ASN A 1 523 ? 38.230 131.480 -64.874 1.00 9.01   ? 579 ASN B ND2 1 
ATOM   3939 N N   . LEU A 1 524 ? 40.870 135.731 -63.936 1.00 13.50  ? 580 LEU B N   1 
ATOM   3940 C CA  . LEU A 1 524 ? 40.289 137.076 -63.860 1.00 16.47  ? 580 LEU B CA  1 
ATOM   3941 C C   . LEU A 1 524 ? 39.227 137.378 -64.928 1.00 17.28  ? 580 LEU B C   1 
ATOM   3942 O O   . LEU A 1 524 ? 38.840 138.531 -65.120 1.00 11.81  ? 580 LEU B O   1 
ATOM   3943 C CB  . LEU A 1 524 ? 41.378 138.134 -63.860 1.00 13.00  ? 580 LEU B CB  1 
ATOM   3944 C CG  . LEU A 1 524 ? 42.365 137.897 -62.723 1.00 19.33  ? 580 LEU B CG  1 
ATOM   3945 C CD1 . LEU A 1 524 ? 43.394 139.006 -62.677 1.00 14.49  ? 580 LEU B CD1 1 
ATOM   3946 C CD2 . LEU A 1 524 ? 41.618 137.814 -61.421 1.00 18.68  ? 580 LEU B CD2 1 
ATOM   3947 N N   . GLY A 1 525 ? 38.829 136.357 -65.676 1.00 13.87  ? 581 GLY B N   1 
ATOM   3948 C CA  . GLY A 1 525 ? 37.881 136.523 -66.769 1.00 10.54  ? 581 GLY B CA  1 
ATOM   3949 C C   . GLY A 1 525 ? 36.572 137.248 -66.490 1.00 15.30  ? 581 GLY B C   1 
ATOM   3950 O O   . GLY A 1 525 ? 36.052 137.220 -65.374 1.00 16.42  ? 581 GLY B O   1 
ATOM   3951 N N   . GLU A 1 526 ? 36.063 137.942 -67.508 1.00 18.27  ? 582 GLU B N   1 
ATOM   3952 C CA  . GLU A 1 526 ? 34.722 138.513 -67.461 1.00 9.84   ? 582 GLU B CA  1 
ATOM   3953 C C   . GLU A 1 526 ? 34.544 139.468 -66.264 1.00 17.45  ? 582 GLU B C   1 
ATOM   3954 O O   . GLU A 1 526 ? 33.677 139.293 -65.393 1.00 13.24  ? 582 GLU B O   1 
ATOM   3955 C CB  . GLU A 1 526 ? 33.694 137.388 -67.463 1.00 8.96   ? 582 GLU B CB  1 
ATOM   3956 C CG  . GLU A 1 526 ? 32.462 137.653 -68.294 1.00 30.53  ? 582 GLU B CG  1 
ATOM   3957 C CD  . GLU A 1 526 ? 31.622 136.394 -68.498 1.00 36.37  ? 582 GLU B CD  1 
ATOM   3958 O OE1 . GLU A 1 526 ? 30.385 136.469 -68.338 1.00 44.86  ? 582 GLU B OE1 1 
ATOM   3959 O OE2 . GLU A 1 526 ? 32.193 135.328 -68.823 1.00 30.28  ? 582 GLU B OE2 1 
ATOM   3960 N N   . ASN A 1 527 ? 35.428 140.455 -66.213 1.00 14.83  ? 583 ASN B N   1 
ATOM   3961 C CA  . ASN A 1 527 ? 35.331 141.551 -65.276 1.00 11.42  ? 583 ASN B CA  1 
ATOM   3962 C C   . ASN A 1 527 ? 35.483 142.876 -66.022 1.00 17.45  ? 583 ASN B C   1 
ATOM   3963 O O   . ASN A 1 527 ? 35.499 142.913 -67.254 1.00 22.02  ? 583 ASN B O   1 
ATOM   3964 C CB  . ASN A 1 527 ? 36.409 141.422 -64.196 1.00 30.39  ? 583 ASN B CB  1 
ATOM   3965 C CG  . ASN A 1 527 ? 36.008 140.472 -63.069 1.00 25.05  ? 583 ASN B CG  1 
ATOM   3966 O OD1 . ASN A 1 527 ? 35.274 140.854 -62.163 1.00 26.31  ? 583 ASN B OD1 1 
ATOM   3967 N ND2 . ASN A 1 527 ? 36.510 139.241 -63.113 1.00 20.81  ? 583 ASN B ND2 1 
ATOM   3968 N N   . ASP A 1 528 ? 35.551 143.966 -65.271 1.00 18.29  ? 584 ASP B N   1 
ATOM   3969 C CA  . ASP A 1 528 ? 35.879 145.294 -65.804 1.00 21.46  ? 584 ASP B CA  1 
ATOM   3970 C C   . ASP A 1 528 ? 37.341 145.783 -65.654 1.00 26.46  ? 584 ASP B C   1 
ATOM   3971 O O   . ASP A 1 528 ? 37.576 146.990 -65.637 1.00 28.20  ? 584 ASP B O   1 
ATOM   3972 C CB  . ASP A 1 528 ? 34.872 146.367 -65.394 1.00 31.05  ? 584 ASP B CB  1 
ATOM   3973 C CG  . ASP A 1 528 ? 34.835 147.518 -66.382 1.00 51.32  ? 584 ASP B CG  1 
ATOM   3974 O OD1 . ASP A 1 528 ? 34.946 147.257 -67.603 1.00 57.04  ? 584 ASP B OD1 1 
ATOM   3975 O OD2 . ASP A 1 528 ? 34.717 148.682 -65.943 1.00 59.45  ? 584 ASP B OD2 1 
ATOM   3976 N N   . PHE A 1 529 ? 38.284 144.880 -65.386 1.00 14.20  ? 585 PHE B N   1 
ATOM   3977 C CA  . PHE A 1 529 ? 39.699 145.254 -65.271 1.00 15.05  ? 585 PHE B CA  1 
ATOM   3978 C C   . PHE A 1 529 ? 40.201 146.043 -66.480 1.00 23.64  ? 585 PHE B C   1 
ATOM   3979 O O   . PHE A 1 529 ? 39.826 145.774 -67.645 1.00 17.99  ? 585 PHE B O   1 
ATOM   3980 C CB  . PHE A 1 529 ? 40.596 144.019 -65.107 1.00 20.87  ? 585 PHE B CB  1 
ATOM   3981 C CG  . PHE A 1 529 ? 40.444 143.306 -63.790 1.00 22.54  ? 585 PHE B CG  1 
ATOM   3982 C CD1 . PHE A 1 529 ? 40.883 143.891 -62.608 1.00 19.66  ? 585 PHE B CD1 1 
ATOM   3983 C CD2 . PHE A 1 529 ? 39.880 142.039 -63.738 1.00 27.25  ? 585 PHE B CD2 1 
ATOM   3984 C CE1 . PHE A 1 529 ? 40.743 143.233 -61.406 1.00 22.10  ? 585 PHE B CE1 1 
ATOM   3985 C CE2 . PHE A 1 529 ? 39.735 141.371 -62.525 1.00 27.18  ? 585 PHE B CE2 1 
ATOM   3986 C CZ  . PHE A 1 529 ? 40.166 141.963 -61.364 1.00 21.63  ? 585 PHE B CZ  1 
ATOM   3987 N N   . SER A 1 530 ? 41.067 147.008 -66.201 1.00 24.62  ? 586 SER B N   1 
ATOM   3988 C CA  . SER A 1 530 ? 41.567 147.901 -67.239 1.00 28.05  ? 586 SER B CA  1 
ATOM   3989 C C   . SER A 1 530 ? 43.038 148.223 -67.025 1.00 26.60  ? 586 SER B C   1 
ATOM   3990 O O   . SER A 1 530 ? 43.681 147.668 -66.131 1.00 25.82  ? 586 SER B O   1 
ATOM   3991 C CB  . SER A 1 530 ? 40.753 149.194 -67.255 1.00 32.76  ? 586 SER B CB  1 
ATOM   3992 O OG  . SER A 1 530 ? 40.838 149.850 -66.000 1.00 32.63  ? 586 SER B OG  1 
ATOM   3993 N N   . GLY A 1 531 ? 43.562 149.127 -67.850 1.00 28.96  ? 587 GLY B N   1 
ATOM   3994 C CA  . GLY A 1 531 ? 44.970 149.475 -67.827 1.00 24.87  ? 587 GLY B CA  1 
ATOM   3995 C C   . GLY A 1 531 ? 45.866 148.436 -68.483 1.00 29.69  ? 587 GLY B C   1 
ATOM   3996 O O   . GLY A 1 531 ? 45.472 147.739 -69.420 1.00 38.23  ? 587 GLY B O   1 
ATOM   3997 N N   . GLU A 1 532 ? 47.088 148.331 -67.985 1.00 27.08  ? 588 GLU B N   1 
ATOM   3998 C CA  . GLU A 1 532 ? 48.093 147.506 -68.625 1.00 27.96  ? 588 GLU B CA  1 
ATOM   3999 C C   . GLU A 1 532 ? 48.407 146.302 -67.756 1.00 28.12  ? 588 GLU B C   1 
ATOM   4000 O O   . GLU A 1 532 ? 48.627 146.438 -66.547 1.00 42.63  ? 588 GLU B O   1 
ATOM   4001 C CB  . GLU A 1 532 ? 49.354 148.334 -68.872 1.00 29.60  ? 588 GLU B CB  1 
ATOM   4002 C CG  . GLU A 1 532 ? 50.154 147.912 -70.087 1.00 43.37  ? 588 GLU B CG  1 
ATOM   4003 C CD  . GLU A 1 532 ? 51.092 149.010 -70.583 1.00 52.86  ? 588 GLU B CD  1 
ATOM   4004 O OE1 . GLU A 1 532 ? 51.465 149.889 -69.772 1.00 49.80  ? 588 GLU B OE1 1 
ATOM   4005 O OE2 . GLU A 1 532 ? 51.450 148.992 -71.786 1.00 53.05  ? 588 GLU B OE2 1 
ATOM   4006 N N   . ILE A 1 533 ? 48.412 145.125 -68.367 1.00 22.95  ? 589 ILE B N   1 
ATOM   4007 C CA  . ILE A 1 533 ? 48.763 143.907 -67.660 1.00 25.39  ? 589 ILE B CA  1 
ATOM   4008 C C   . ILE A 1 533 ? 50.163 144.095 -67.123 1.00 32.18  ? 589 ILE B C   1 
ATOM   4009 O O   . ILE A 1 533 ? 51.115 144.229 -67.901 1.00 26.86  ? 589 ILE B O   1 
ATOM   4010 C CB  . ILE A 1 533 ? 48.791 142.703 -68.599 1.00 28.26  ? 589 ILE B CB  1 
ATOM   4011 C CG1 . ILE A 1 533 ? 47.447 142.530 -69.308 1.00 26.42  ? 589 ILE B CG1 1 
ATOM   4012 C CG2 . ILE A 1 533 ? 49.156 141.444 -67.839 1.00 34.00  ? 589 ILE B CG2 1 
ATOM   4013 C CD1 . ILE A 1 533 ? 47.525 141.661 -70.537 1.00 17.77  ? 589 ILE B CD1 1 
ATOM   4014 N N   . PRO A 1 534 ? 50.293 144.091 -65.789 1.00 32.93  ? 590 PRO B N   1 
ATOM   4015 C CA  . PRO A 1 534 ? 51.559 144.421 -65.130 1.00 38.23  ? 590 PRO B CA  1 
ATOM   4016 C C   . PRO A 1 534 ? 52.653 143.439 -65.526 1.00 39.29  ? 590 PRO B C   1 
ATOM   4017 O O   . PRO A 1 534 ? 52.360 142.311 -65.913 1.00 41.16  ? 590 PRO B O   1 
ATOM   4018 C CB  . PRO A 1 534 ? 51.223 144.294 -63.638 1.00 40.90  ? 590 PRO B CB  1 
ATOM   4019 C CG  . PRO A 1 534 ? 50.073 143.328 -63.597 1.00 38.82  ? 590 PRO B CG  1 
ATOM   4020 C CD  . PRO A 1 534 ? 49.270 143.632 -64.836 1.00 35.17  ? 590 PRO B CD  1 
ATOM   4021 N N   . ASP A 1 535 ? 53.901 143.880 -65.449 1.00 38.80  ? 591 ASP B N   1 
ATOM   4022 C CA  . ASP A 1 535 ? 55.035 143.032 -65.764 1.00 37.41  ? 591 ASP B CA  1 
ATOM   4023 C C   . ASP A 1 535 ? 55.179 141.932 -64.696 1.00 37.89  ? 591 ASP B C   1 
ATOM   4024 O O   . ASP A 1 535 ? 55.551 140.795 -65.002 1.00 33.09  ? 591 ASP B O   1 
ATOM   4025 C CB  . ASP A 1 535 ? 56.289 143.905 -65.849 1.00 45.38  ? 591 ASP B CB  1 
ATOM   4026 C CG  . ASP A 1 535 ? 57.341 143.345 -66.794 1.00 56.87  ? 591 ASP B CG  1 
ATOM   4027 O OD1 . ASP A 1 535 ? 57.180 143.468 -68.037 1.00 53.23  ? 591 ASP B OD1 1 
ATOM   4028 O OD2 . ASP A 1 535 ? 58.346 142.805 -66.277 1.00 63.55  ? 591 ASP B OD2 1 
ATOM   4029 N N   . GLU A 1 536 ? 54.850 142.274 -63.449 1.00 44.27  ? 592 GLU B N   1 
ATOM   4030 C CA  . GLU A 1 536 ? 55.001 141.366 -62.307 1.00 47.22  ? 592 GLU B CA  1 
ATOM   4031 C C   . GLU A 1 536 ? 54.072 140.158 -62.385 1.00 47.82  ? 592 GLU B C   1 
ATOM   4032 O O   . GLU A 1 536 ? 54.199 139.196 -61.629 1.00 50.86  ? 592 GLU B O   1 
ATOM   4033 C CB  . GLU A 1 536 ? 54.768 142.115 -60.990 1.00 45.54  ? 592 GLU B CB  1 
ATOM   4034 C CG  . GLU A 1 536 ? 55.711 143.277 -60.744 1.00 46.72  ? 592 GLU B CG  1 
ATOM   4035 C CD  . GLU A 1 536 ? 55.255 144.551 -61.422 1.00 49.74  ? 592 GLU B CD  1 
ATOM   4036 O OE1 . GLU A 1 536 ? 54.269 144.497 -62.189 1.00 46.36  ? 592 GLU B OE1 1 
ATOM   4037 O OE2 . GLU A 1 536 ? 55.878 145.607 -61.185 1.00 56.60  ? 592 GLU B OE2 1 
ATOM   4038 N N   . LEU A 1 537 ? 53.141 140.207 -63.319 1.00 43.13  ? 593 LEU B N   1 
ATOM   4039 C CA  . LEU A 1 537 ? 52.267 139.082 -63.523 1.00 36.15  ? 593 LEU B CA  1 
ATOM   4040 C C   . LEU A 1 537 ? 53.036 137.952 -64.234 1.00 36.29  ? 593 LEU B C   1 
ATOM   4041 O O   . LEU A 1 537 ? 52.722 136.771 -64.078 1.00 34.48  ? 593 LEU B O   1 
ATOM   4042 C CB  . LEU A 1 537 ? 51.007 139.534 -64.258 1.00 37.31  ? 593 LEU B CB  1 
ATOM   4043 C CG  . LEU A 1 537 ? 49.977 138.432 -64.440 1.00 31.38  ? 593 LEU B CG  1 
ATOM   4044 C CD1 . LEU A 1 537 ? 49.638 137.751 -63.115 1.00 30.74  ? 593 LEU B CD1 1 
ATOM   4045 C CD2 . LEU A 1 537 ? 48.752 139.025 -65.069 1.00 29.27  ? 593 LEU B CD2 1 
ATOM   4046 N N   . GLY A 1 538 ? 54.075 138.328 -64.972 1.00 41.82  ? 594 GLY B N   1 
ATOM   4047 C CA  . GLY A 1 538 ? 55.000 137.364 -65.520 1.00 42.51  ? 594 GLY B CA  1 
ATOM   4048 C C   . GLY A 1 538 ? 55.832 136.753 -64.433 1.00 47.03  ? 594 GLY B C   1 
ATOM   4049 O O   . GLY A 1 538 ? 56.386 135.658 -64.629 1.00 47.41  ? 594 GLY B O   1 
ATOM   4050 N N   . GLN A 1 539 ? 55.898 137.429 -63.291 1.00 48.02  ? 595 GLN B N   1 
ATOM   4051 C CA  . GLN A 1 539 ? 56.909 137.121 -62.304 1.00 46.35  ? 595 GLN B CA  1 
ATOM   4052 C C   . GLN A 1 539 ? 56.568 135.856 -61.454 1.00 50.37  ? 595 GLN B C   1 
ATOM   4053 O O   . GLN A 1 539 ? 57.241 135.574 -60.456 1.00 50.42  ? 595 GLN B O   1 
ATOM   4054 C CB  . GLN A 1 539 ? 57.174 138.331 -61.420 1.00 55.33  ? 595 GLN B CB  1 
ATOM   4055 C CG  . GLN A 1 539 ? 58.632 138.629 -61.139 1.00 58.16  ? 595 GLN B CG  1 
ATOM   4056 C CD  . GLN A 1 539 ? 58.923 140.094 -61.276 1.00 60.52  ? 595 GLN B CD  1 
ATOM   4057 O OE1 . GLN A 1 539 ? 58.124 140.906 -60.816 1.00 60.25  ? 595 GLN B OE1 1 
ATOM   4058 N NE2 . GLN A 1 539 ? 60.017 140.453 -61.989 1.00 60.31  ? 595 GLN B NE2 1 
ATOM   4059 N N   . ILE A 1 540 ? 55.527 135.098 -61.830 1.00 46.34  ? 596 ILE B N   1 
ATOM   4060 C CA  . ILE A 1 540 ? 55.068 133.911 -61.056 1.00 39.22  ? 596 ILE B CA  1 
ATOM   4061 C C   . ILE A 1 540 ? 55.264 132.600 -61.834 1.00 45.73  ? 596 ILE B C   1 
ATOM   4062 O O   . ILE A 1 540 ? 54.336 132.104 -62.486 1.00 49.51  ? 596 ILE B O   1 
ATOM   4063 C CB  . ILE A 1 540 ? 53.561 133.998 -60.710 1.00 33.44  ? 596 ILE B CB  1 
ATOM   4064 C CG1 . ILE A 1 540 ? 53.191 135.448 -60.431 1.00 29.25  ? 596 ILE B CG1 1 
ATOM   4065 C CG2 . ILE A 1 540 ? 53.134 133.017 -59.560 1.00 27.80  ? 596 ILE B CG2 1 
ATOM   4066 C CD1 . ILE A 1 540 ? 51.729 135.701 -60.450 1.00 25.36  ? 596 ILE B CD1 1 
ATOM   4067 N N   . PRO A 1 541 ? 56.474 132.030 -61.776 1.00 47.18  ? 597 PRO B N   1 
ATOM   4068 C CA  . PRO A 1 541 ? 56.833 130.831 -62.546 1.00 45.86  ? 597 PRO B CA  1 
ATOM   4069 C C   . PRO A 1 541 ? 56.002 129.606 -62.186 1.00 43.47  ? 597 PRO B C   1 
ATOM   4070 O O   . PRO A 1 541 ? 55.987 128.633 -62.950 1.00 39.86  ? 597 PRO B O   1 
ATOM   4071 C CB  . PRO A 1 541 ? 58.295 130.583 -62.151 1.00 48.89  ? 597 PRO B CB  1 
ATOM   4072 C CG  . PRO A 1 541 ? 58.771 131.872 -61.594 1.00 49.68  ? 597 PRO B CG  1 
ATOM   4073 C CD  . PRO A 1 541 ? 57.590 132.501 -60.944 1.00 48.24  ? 597 PRO B CD  1 
ATOM   4074 N N   . SER A 1 542 ? 55.338 129.639 -61.032 1.00 40.99  ? 598 SER B N   1 
ATOM   4075 C CA  . SER A 1 542 ? 54.469 128.532 -60.648 1.00 31.37  ? 598 SER B CA  1 
ATOM   4076 C C   . SER A 1 542 ? 53.219 128.479 -61.523 1.00 27.73  ? 598 SER B C   1 
ATOM   4077 O O   . SER A 1 542 ? 52.599 127.423 -61.627 1.00 28.30  ? 598 SER B O   1 
ATOM   4078 C CB  . SER A 1 542 ? 54.104 128.570 -59.157 1.00 31.33  ? 598 SER B CB  1 
ATOM   4079 O OG  . SER A 1 542 ? 53.448 129.776 -58.799 1.00 33.72  ? 598 SER B OG  1 
ATOM   4080 N N   . LEU A 1 543 ? 52.859 129.600 -62.162 1.00 32.25  ? 599 LEU B N   1 
ATOM   4081 C CA  . LEU A 1 543 ? 51.677 129.617 -63.034 1.00 29.49  ? 599 LEU B CA  1 
ATOM   4082 C C   . LEU A 1 543 ? 51.846 128.565 -64.108 1.00 19.82  ? 599 LEU B C   1 
ATOM   4083 O O   . LEU A 1 543 ? 52.720 128.662 -64.950 1.00 28.72  ? 599 LEU B O   1 
ATOM   4084 C CB  . LEU A 1 543 ? 51.489 130.993 -63.678 1.00 32.00  ? 599 LEU B CB  1 
ATOM   4085 C CG  . LEU A 1 543 ? 50.574 131.935 -62.895 1.00 30.02  ? 599 LEU B CG  1 
ATOM   4086 C CD1 . LEU A 1 543 ? 50.488 133.304 -63.544 1.00 28.96  ? 599 LEU B CD1 1 
ATOM   4087 C CD2 . LEU A 1 543 ? 49.206 131.298 -62.800 1.00 27.81  ? 599 LEU B CD2 1 
ATOM   4088 N N   . ALA A 1 544 ? 50.957 127.585 -64.073 1.00 20.81  ? 600 ALA B N   1 
ATOM   4089 C CA  . ALA A 1 544 ? 51.114 126.325 -64.786 1.00 26.56  ? 600 ALA B CA  1 
ATOM   4090 C C   . ALA A 1 544 ? 49.822 125.921 -65.476 1.00 33.40  ? 600 ALA B C   1 
ATOM   4091 O O   . ALA A 1 544 ? 49.788 125.691 -66.690 1.00 38.37  ? 600 ALA B O   1 
ATOM   4092 C CB  . ALA A 1 544 ? 51.606 125.232 -63.851 1.00 25.94  ? 600 ALA B CB  1 
ATOM   4093 N N   . ILE A 1 545 ? 48.762 125.805 -64.676 1.00 29.96  ? 601 ILE B N   1 
ATOM   4094 C CA  . ILE A 1 545 ? 47.491 125.265 -65.147 1.00 25.44  ? 601 ILE B CA  1 
ATOM   4095 C C   . ILE A 1 545 ? 46.804 126.204 -66.147 1.00 27.26  ? 601 ILE B C   1 
ATOM   4096 O O   . ILE A 1 545 ? 46.682 125.861 -67.321 1.00 40.30  ? 601 ILE B O   1 
ATOM   4097 C CB  . ILE A 1 545 ? 46.543 124.989 -63.975 1.00 24.93  ? 601 ILE B CB  1 
ATOM   4098 C CG1 . ILE A 1 545 ? 47.145 123.942 -63.029 1.00 29.66  ? 601 ILE B CG1 1 
ATOM   4099 C CG2 . ILE A 1 545 ? 45.209 124.523 -64.479 1.00 18.09  ? 601 ILE B CG2 1 
ATOM   4100 C CD1 . ILE A 1 545 ? 46.328 123.714 -61.761 1.00 17.69  ? 601 ILE B CD1 1 
ATOM   4101 N N   . SER A 1 546 ? 46.360 127.376 -65.704 1.00 20.89  ? 602 SER B N   1 
ATOM   4102 C CA  . SER A 1 546 ? 45.834 128.373 -66.635 1.00 14.93  ? 602 SER B CA  1 
ATOM   4103 C C   . SER A 1 546 ? 45.887 129.809 -66.118 1.00 17.70  ? 602 SER B C   1 
ATOM   4104 O O   . SER A 1 546 ? 45.893 130.076 -64.907 1.00 17.30  ? 602 SER B O   1 
ATOM   4105 C CB  . SER A 1 546 ? 44.399 128.047 -67.038 1.00 15.97  ? 602 SER B CB  1 
ATOM   4106 O OG  . SER A 1 546 ? 43.487 128.528 -66.067 1.00 26.97  ? 602 SER B OG  1 
ATOM   4107 N N   . LEU A 1 547 ? 45.899 130.734 -67.068 1.00 22.88  ? 603 LEU B N   1 
ATOM   4108 C CA  . LEU A 1 547 ? 45.853 132.157 -66.785 1.00 19.17  ? 603 LEU B CA  1 
ATOM   4109 C C   . LEU A 1 547 ? 44.782 132.740 -67.695 1.00 16.53  ? 603 LEU B C   1 
ATOM   4110 O O   . LEU A 1 547 ? 44.935 132.739 -68.920 1.00 20.18  ? 603 LEU B O   1 
ATOM   4111 C CB  . LEU A 1 547 ? 47.215 132.773 -67.104 1.00 21.37  ? 603 LEU B CB  1 
ATOM   4112 C CG  . LEU A 1 547 ? 47.377 134.287 -67.123 1.00 15.08  ? 603 LEU B CG  1 
ATOM   4113 C CD1 . LEU A 1 547 ? 46.882 134.887 -65.835 1.00 22.31  ? 603 LEU B CD1 1 
ATOM   4114 C CD2 . LEU A 1 547 ? 48.840 134.640 -67.359 1.00 16.14  ? 603 LEU B CD2 1 
ATOM   4115 N N   . ASN A 1 548 ? 43.691 133.223 -67.107 1.00 15.28  ? 604 ASN B N   1 
ATOM   4116 C CA  . ASN A 1 548 ? 42.570 133.722 -67.893 1.00 12.03  ? 604 ASN B CA  1 
ATOM   4117 C C   . ASN A 1 548 ? 42.309 135.191 -67.552 1.00 16.41  ? 604 ASN B C   1 
ATOM   4118 O O   . ASN A 1 548 ? 41.877 135.530 -66.445 1.00 13.91  ? 604 ASN B O   1 
ATOM   4119 C CB  . ASN A 1 548 ? 41.350 132.835 -67.679 1.00 11.07  ? 604 ASN B CB  1 
ATOM   4120 C CG  . ASN A 1 548 ? 40.225 133.127 -68.639 1.00 14.44  ? 604 ASN B CG  1 
ATOM   4121 O OD1 . ASN A 1 548 ? 40.175 134.203 -69.253 1.00 15.04  ? 604 ASN B OD1 1 
ATOM   4122 N ND2 . ASN A 1 548 ? 39.281 132.165 -68.755 1.00 12.71  ? 604 ASN B ND2 1 
ATOM   4123 N N   . LEU A 1 549 ? 42.677 136.053 -68.503 1.00 17.06  ? 605 LEU B N   1 
ATOM   4124 C CA  . LEU A 1 549 ? 42.474 137.494 -68.431 1.00 13.26  ? 605 LEU B CA  1 
ATOM   4125 C C   . LEU A 1 549 ? 41.350 138.017 -69.318 1.00 17.48  ? 605 LEU B C   1 
ATOM   4126 O O   . LEU A 1 549 ? 41.202 139.228 -69.470 1.00 19.20  ? 605 LEU B O   1 
ATOM   4127 C CB  . LEU A 1 549 ? 43.781 138.245 -68.689 1.00 14.26  ? 605 LEU B CB  1 
ATOM   4128 C CG  . LEU A 1 549 ? 44.922 138.027 -67.681 1.00 15.92  ? 605 LEU B CG  1 
ATOM   4129 C CD1 . LEU A 1 549 ? 46.131 138.845 -68.072 1.00 16.65  ? 605 LEU B CD1 1 
ATOM   4130 C CD2 . LEU A 1 549 ? 44.521 138.337 -66.222 1.00 14.74  ? 605 LEU B CD2 1 
ATOM   4131 N N   . SER A 1 550 ? 40.607 137.118 -69.956 1.00 15.67  ? 606 SER B N   1 
ATOM   4132 C CA  . SER A 1 550 ? 39.727 137.520 -71.054 1.00 15.35  ? 606 SER B CA  1 
ATOM   4133 C C   . SER A 1 550 ? 38.510 138.327 -70.611 1.00 18.30  ? 606 SER B C   1 
ATOM   4134 O O   . SER A 1 550 ? 38.269 138.513 -69.420 1.00 20.28  ? 606 SER B O   1 
ATOM   4135 C CB  . SER A 1 550 ? 39.224 136.284 -71.788 1.00 18.99  ? 606 SER B CB  1 
ATOM   4136 O OG  . SER A 1 550 ? 38.200 135.652 -71.030 1.00 20.64  ? 606 SER B OG  1 
ATOM   4137 N N   . CYS A 1 551 ? 37.743 138.782 -71.597 1.00 21.19  ? 607 CYS B N   1 
ATOM   4138 C CA  . CYS A 1 551 ? 36.547 139.603 -71.384 1.00 17.15  ? 607 CYS B CA  1 
ATOM   4139 C C   . CYS A 1 551 ? 36.748 140.714 -70.351 1.00 18.85  ? 607 CYS B C   1 
ATOM   4140 O O   . CYS A 1 551 ? 35.987 140.866 -69.394 1.00 20.49  ? 607 CYS B O   1 
ATOM   4141 C CB  . CYS A 1 551 ? 35.335 138.734 -71.098 1.00 10.18  ? 607 CYS B CB  1 
ATOM   4142 S SG  . CYS A 1 551 ? 35.218 137.375 -72.283 1.00 15.58  ? 607 CYS B SG  1 
ATOM   4143 N N   . ASN A 1 552 ? 37.813 141.473 -70.545 1.00 20.48  ? 608 ASN B N   1 
ATOM   4144 C CA  . ASN A 1 552 ? 38.043 142.674 -69.767 1.00 21.62  ? 608 ASN B CA  1 
ATOM   4145 C C   . ASN A 1 552 ? 38.272 143.846 -70.696 1.00 21.56  ? 608 ASN B C   1 
ATOM   4146 O O   . ASN A 1 552 ? 37.982 143.769 -71.883 1.00 32.77  ? 608 ASN B O   1 
ATOM   4147 C CB  . ASN A 1 552 ? 39.227 142.508 -68.818 1.00 24.30  ? 608 ASN B CB  1 
ATOM   4148 C CG  . ASN A 1 552 ? 38.871 141.717 -67.581 1.00 23.39  ? 608 ASN B CG  1 
ATOM   4149 O OD1 . ASN A 1 552 ? 38.194 142.222 -66.692 1.00 25.37  ? 608 ASN B OD1 1 
ATOM   4150 N ND2 . ASN A 1 552 ? 39.339 140.474 -67.508 1.00 18.68  ? 608 ASN B ND2 1 
ATOM   4151 N N   . ARG A 1 553 ? 38.697 144.958 -70.116 1.00 23.48  ? 609 ARG B N   1 
ATOM   4152 C CA  . ARG A 1 553 ? 39.165 146.141 -70.843 1.00 15.01  ? 609 ARG B CA  1 
ATOM   4153 C C   . ARG A 1 553 ? 40.678 146.397 -70.957 1.00 20.39  ? 609 ARG B C   1 
ATOM   4154 O O   . ARG A 1 553 ? 41.080 147.553 -71.048 1.00 20.93  ? 609 ARG B O   1 
ATOM   4155 C CB  . ARG A 1 553 ? 38.349 147.392 -70.522 1.00 15.19  ? 609 ARG B CB  1 
ATOM   4156 C CG  . ARG A 1 553 ? 36.950 147.342 -71.153 1.00 19.47  ? 609 ARG B CG  1 
ATOM   4157 C CD  . ARG A 1 553 ? 36.114 148.575 -70.830 1.00 29.94  ? 609 ARG B CD  1 
ATOM   4158 N NE  . ARG A 1 553 ? 36.092 148.902 -69.399 1.00 37.73  ? 609 ARG B NE  1 
ATOM   4159 C CZ  . ARG A 1 553 ? 36.756 149.918 -68.856 1.00 46.80  ? 609 ARG B CZ  1 
ATOM   4160 N NH1 . ARG A 1 553 ? 37.498 150.710 -69.618 1.00 51.83  ? 609 ARG B NH1 1 
ATOM   4161 N NH2 . ARG A 1 553 ? 36.678 150.150 -67.552 1.00 52.13  ? 609 ARG B NH2 1 
ATOM   4162 N N   . PHE A 1 554 ? 41.511 145.376 -70.763 1.00 21.04  ? 610 PHE B N   1 
ATOM   4163 C CA  . PHE A 1 554 ? 42.970 145.559 -70.800 1.00 16.71  ? 610 PHE B CA  1 
ATOM   4164 C C   . PHE A 1 554 ? 43.461 146.228 -72.079 1.00 25.57  ? 610 PHE B C   1 
ATOM   4165 O O   . PHE A 1 554 ? 42.893 146.023 -73.168 1.00 26.26  ? 610 PHE B O   1 
ATOM   4166 C CB  . PHE A 1 554 ? 43.696 144.217 -70.666 1.00 16.54  ? 610 PHE B CB  1 
ATOM   4167 C CG  . PHE A 1 554 ? 43.564 143.582 -69.312 1.00 27.02  ? 610 PHE B CG  1 
ATOM   4168 C CD1 . PHE A 1 554 ? 44.188 144.144 -68.203 1.00 31.20  ? 610 PHE B CD1 1 
ATOM   4169 C CD2 . PHE A 1 554 ? 42.835 142.417 -69.145 1.00 23.60  ? 610 PHE B CD2 1 
ATOM   4170 C CE1 . PHE A 1 554 ? 44.074 143.565 -66.960 1.00 28.75  ? 610 PHE B CE1 1 
ATOM   4171 C CE2 . PHE A 1 554 ? 42.709 141.836 -67.901 1.00 23.63  ? 610 PHE B CE2 1 
ATOM   4172 C CZ  . PHE A 1 554 ? 43.330 142.413 -66.805 1.00 27.08  ? 610 PHE B CZ  1 
ATOM   4173 N N   . VAL A 1 555 ? 44.515 147.033 -71.944 1.00 20.43  ? 611 VAL B N   1 
ATOM   4174 C CA  . VAL A 1 555 ? 45.181 147.634 -73.105 1.00 18.85  ? 611 VAL B CA  1 
ATOM   4175 C C   . VAL A 1 555 ? 46.700 147.538 -73.038 1.00 24.65  ? 611 VAL B C   1 
ATOM   4176 O O   . VAL A 1 555 ? 47.270 146.999 -72.079 1.00 31.43  ? 611 VAL B O   1 
ATOM   4177 C CB  . VAL A 1 555 ? 44.807 149.109 -73.292 1.00 19.30  ? 611 VAL B CB  1 
ATOM   4178 C CG1 . VAL A 1 555 ? 43.291 149.257 -73.427 1.00 18.53  ? 611 VAL B CG1 1 
ATOM   4179 C CG2 . VAL A 1 555 ? 45.370 149.954 -72.148 1.00 20.00  ? 611 VAL B CG2 1 
ATOM   4180 N N   . GLY A 1 556 ? 47.351 148.085 -74.060 1.00 22.27  ? 612 GLY B N   1 
ATOM   4181 C CA  . GLY A 1 556 ? 48.793 147.970 -74.203 1.00 28.81  ? 612 GLY B CA  1 
ATOM   4182 C C   . GLY A 1 556 ? 49.194 146.593 -74.701 1.00 31.08  ? 612 GLY B C   1 
ATOM   4183 O O   . GLY A 1 556 ? 48.347 145.808 -75.122 1.00 32.55  ? 612 GLY B O   1 
ATOM   4184 N N   . GLU A 1 557 ? 50.485 146.288 -74.648 1.00 29.99  ? 613 GLU B N   1 
ATOM   4185 C CA  . GLU A 1 557 ? 50.968 145.035 -75.201 1.00 21.40  ? 613 GLU B CA  1 
ATOM   4186 C C   . GLU A 1 557 ? 51.057 143.911 -74.180 1.00 20.98  ? 613 GLU B C   1 
ATOM   4187 O O   . GLU A 1 557 ? 50.878 144.122 -72.978 1.00 43.54  ? 613 GLU B O   1 
ATOM   4188 C CB  . GLU A 1 557 ? 52.343 145.254 -75.837 1.00 22.44  ? 613 GLU B CB  1 
ATOM   4189 C CG  . GLU A 1 557 ? 52.327 146.211 -77.016 1.00 39.67  ? 613 GLU B CG  1 
ATOM   4190 C CD  . GLU A 1 557 ? 53.701 146.374 -77.659 1.00 40.32  ? 613 GLU B CD  1 
ATOM   4191 O OE1 . GLU A 1 557 ? 54.720 146.150 -76.966 1.00 37.34  ? 613 GLU B OE1 1 
ATOM   4192 O OE2 . GLU A 1 557 ? 53.757 146.722 -78.857 1.00 38.96  ? 613 GLU B OE2 1 
ATOM   4193 N N   . ILE A 1 558 ? 51.367 142.715 -74.669 1.00 24.53  ? 614 ILE B N   1 
ATOM   4194 C CA  . ILE A 1 558 ? 51.689 141.594 -73.803 1.00 25.85  ? 614 ILE B CA  1 
ATOM   4195 C C   . ILE A 1 558 ? 53.081 141.868 -73.255 1.00 38.62  ? 614 ILE B C   1 
ATOM   4196 O O   . ILE A 1 558 ? 54.045 141.914 -74.014 1.00 45.00  ? 614 ILE B O   1 
ATOM   4197 C CB  . ILE A 1 558 ? 51.693 140.257 -74.571 1.00 20.09  ? 614 ILE B CB  1 
ATOM   4198 C CG1 . ILE A 1 558 ? 50.373 140.052 -75.308 1.00 31.03  ? 614 ILE B CG1 1 
ATOM   4199 C CG2 . ILE A 1 558 ? 51.887 139.099 -73.630 1.00 19.79  ? 614 ILE B CG2 1 
ATOM   4200 C CD1 . ILE A 1 558 ? 50.234 138.672 -75.920 1.00 31.51  ? 614 ILE B CD1 1 
ATOM   4201 N N   . PRO A 1 559 ? 53.190 142.065 -71.934 1.00 41.77  ? 615 PRO B N   1 
ATOM   4202 C CA  . PRO A 1 559 ? 54.458 142.462 -71.314 1.00 37.52  ? 615 PRO B CA  1 
ATOM   4203 C C   . PRO A 1 559 ? 55.540 141.419 -71.578 1.00 32.37  ? 615 PRO B C   1 
ATOM   4204 O O   . PRO A 1 559 ? 55.248 140.214 -71.584 1.00 27.53  ? 615 PRO B O   1 
ATOM   4205 C CB  . PRO A 1 559 ? 54.108 142.537 -69.825 1.00 47.13  ? 615 PRO B CB  1 
ATOM   4206 C CG  . PRO A 1 559 ? 52.933 141.628 -69.663 1.00 41.58  ? 615 PRO B CG  1 
ATOM   4207 C CD  . PRO A 1 559 ? 52.156 141.741 -70.935 1.00 39.51  ? 615 PRO B CD  1 
ATOM   4208 N N   . SER A 1 560 ? 56.765 141.881 -71.814 1.00 34.15  ? 616 SER B N   1 
ATOM   4209 C CA  . SER A 1 560 ? 57.841 141.001 -72.267 1.00 31.43  ? 616 SER B CA  1 
ATOM   4210 C C   . SER A 1 560 ? 58.097 139.873 -71.283 1.00 28.68  ? 616 SER B C   1 
ATOM   4211 O O   . SER A 1 560 ? 58.482 138.757 -71.669 1.00 32.28  ? 616 SER B O   1 
ATOM   4212 C CB  . SER A 1 560 ? 59.120 141.791 -72.552 1.00 35.25  ? 616 SER B CB  1 
ATOM   4213 O OG  . SER A 1 560 ? 59.489 142.584 -71.440 1.00 42.26  ? 616 SER B OG  1 
ATOM   4214 N N   . ARG A 1 561 ? 57.830 140.139 -70.011 1.00 30.16  ? 617 ARG B N   1 
ATOM   4215 C CA  . ARG A 1 561 ? 58.108 139.133 -69.006 1.00 41.15  ? 617 ARG B CA  1 
ATOM   4216 C C   . ARG A 1 561 ? 57.305 137.848 -69.183 1.00 43.86  ? 617 ARG B C   1 
ATOM   4217 O O   . ARG A 1 561 ? 57.680 136.809 -68.639 1.00 48.53  ? 617 ARG B O   1 
ATOM   4218 C CB  . ARG A 1 561 ? 57.908 139.666 -67.597 1.00 52.61  ? 617 ARG B CB  1 
ATOM   4219 C CG  . ARG A 1 561 ? 58.848 138.988 -66.617 1.00 72.19  ? 617 ARG B CG  1 
ATOM   4220 C CD  . ARG A 1 561 ? 58.296 138.895 -65.224 1.00 92.91  ? 617 ARG B CD  1 
ATOM   4221 N NE  . ARG A 1 561 ? 59.158 138.113 -64.371 1.00 108.05 ? 617 ARG B NE  1 
ATOM   4222 C CZ  . ARG A 1 561 ? 59.159 136.797 -64.397 1.00 118.17 ? 617 ARG B CZ  1 
ATOM   4223 N NH1 . ARG A 1 561 ? 58.282 136.213 -65.175 1.00 120.64 ? 617 ARG B NH1 1 
ATOM   4224 N NH2 . ARG A 1 561 ? 60.001 136.080 -63.656 1.00 122.74 ? 617 ARG B NH2 1 
ATOM   4225 N N   . PHE A 1 562 ? 56.234 137.889 -69.975 1.00 38.18  ? 618 PHE B N   1 
ATOM   4226 C CA  . PHE A 1 562 ? 55.445 136.677 -70.196 1.00 35.09  ? 618 PHE B CA  1 
ATOM   4227 C C   . PHE A 1 562 ? 56.265 135.589 -70.860 1.00 39.00  ? 618 PHE B C   1 
ATOM   4228 O O   . PHE A 1 562 ? 55.837 134.431 -70.902 1.00 44.49  ? 618 PHE B O   1 
ATOM   4229 C CB  . PHE A 1 562 ? 54.175 136.928 -71.013 1.00 32.56  ? 618 PHE B CB  1 
ATOM   4230 C CG  . PHE A 1 562 ? 53.001 137.397 -70.197 1.00 34.44  ? 618 PHE B CG  1 
ATOM   4231 C CD1 . PHE A 1 562 ? 53.193 138.068 -68.990 1.00 42.47  ? 618 PHE B CD1 1 
ATOM   4232 C CD2 . PHE A 1 562 ? 51.702 137.167 -70.635 1.00 26.95  ? 618 PHE B CD2 1 
ATOM   4233 C CE1 . PHE A 1 562 ? 52.119 138.514 -68.242 1.00 19.62  ? 618 PHE B CE1 1 
ATOM   4234 C CE2 . PHE A 1 562 ? 50.617 137.615 -69.899 1.00 19.82  ? 618 PHE B CE2 1 
ATOM   4235 C CZ  . PHE A 1 562 ? 50.830 138.291 -68.693 1.00 21.19  ? 618 PHE B CZ  1 
ATOM   4236 N N   . SER A 1 563 ? 57.442 135.949 -71.375 1.00 40.11  ? 619 SER B N   1 
ATOM   4237 C CA  . SER A 1 563 ? 58.336 134.921 -71.902 1.00 40.63  ? 619 SER B CA  1 
ATOM   4238 C C   . SER A 1 563 ? 58.840 134.007 -70.789 1.00 48.04  ? 619 SER B C   1 
ATOM   4239 O O   . SER A 1 563 ? 59.278 132.886 -71.057 1.00 52.79  ? 619 SER B O   1 
ATOM   4240 C CB  . SER A 1 563 ? 59.509 135.525 -72.675 1.00 33.86  ? 619 SER B CB  1 
ATOM   4241 O OG  . SER A 1 563 ? 60.103 136.587 -71.957 1.00 34.44  ? 619 SER B OG  1 
ATOM   4242 N N   . ASP A 1 564 ? 58.762 134.475 -69.543 1.00 44.32  ? 620 ASP B N   1 
ATOM   4243 C CA  . ASP A 1 564 ? 59.234 133.669 -68.422 1.00 46.12  ? 620 ASP B CA  1 
ATOM   4244 C C   . ASP A 1 564 ? 58.278 132.569 -67.975 1.00 46.36  ? 620 ASP B C   1 
ATOM   4245 O O   . ASP A 1 564 ? 58.701 131.668 -67.256 1.00 47.55  ? 620 ASP B O   1 
ATOM   4246 C CB  . ASP A 1 564 ? 59.533 134.518 -67.192 1.00 44.46  ? 620 ASP B CB  1 
ATOM   4247 C CG  . ASP A 1 564 ? 60.817 135.315 -67.301 1.00 46.96  ? 620 ASP B CG  1 
ATOM   4248 O OD1 . ASP A 1 564 ? 61.678 135.020 -68.164 1.00 45.10  ? 620 ASP B OD1 1 
ATOM   4249 O OD2 . ASP A 1 564 ? 60.966 136.247 -66.485 1.00 45.56  ? 620 ASP B OD2 1 
ATOM   4250 N N   . LEU A 1 565 ? 57.011 132.592 -68.381 1.00 38.82  ? 621 LEU B N   1 
ATOM   4251 C CA  . LEU A 1 565 ? 56.149 131.592 -67.782 1.00 38.66  ? 621 LEU B CA  1 
ATOM   4252 C C   . LEU A 1 565 ? 56.280 130.365 -68.640 1.00 40.56  ? 621 LEU B C   1 
ATOM   4253 O O   . LEU A 1 565 ? 55.476 130.125 -69.540 1.00 38.59  ? 621 LEU B O   1 
ATOM   4254 C CB  . LEU A 1 565 ? 54.699 132.060 -67.840 1.00 31.82  ? 621 LEU B CB  1 
ATOM   4255 C CG  . LEU A 1 565 ? 54.468 133.392 -67.142 1.00 29.54  ? 621 LEU B CG  1 
ATOM   4256 C CD1 . LEU A 1 565 ? 53.214 134.056 -67.676 1.00 21.60  ? 621 LEU B CD1 1 
ATOM   4257 C CD2 . LEU A 1 565 ? 54.387 133.158 -65.635 1.00 31.07  ? 621 LEU B CD2 1 
ATOM   4258 N N   . LYS A 1 566 ? 57.199 129.506 -68.219 1.00 38.44  ? 622 LYS B N   1 
ATOM   4259 C CA  . LYS A 1 566 ? 57.681 128.419 -69.049 1.00 40.02  ? 622 LYS B CA  1 
ATOM   4260 C C   . LYS A 1 566 ? 56.824 127.201 -68.759 1.00 40.81  ? 622 LYS B C   1 
ATOM   4261 O O   . LYS A 1 566 ? 56.849 126.212 -69.493 1.00 43.19  ? 622 LYS B O   1 
ATOM   4262 C CB  . LYS A 1 566 ? 59.158 128.145 -68.724 1.00 43.76  ? 622 LYS B CB  1 
ATOM   4263 C CG  . LYS A 1 566 ? 60.084 128.048 -69.928 1.00 51.08  ? 622 LYS B CG  1 
ATOM   4264 C CD  . LYS A 1 566 ? 60.316 129.405 -70.581 1.00 55.09  ? 622 LYS B CD  1 
ATOM   4265 C CE  . LYS A 1 566 ? 61.000 129.254 -71.935 1.00 57.41  ? 622 LYS B CE  1 
ATOM   4266 N NZ  . LYS A 1 566 ? 60.714 130.406 -72.848 1.00 60.22  ? 622 LYS B NZ  1 
ATOM   4267 N N   . ASN A 1 567 ? 56.063 127.283 -67.672 1.00 37.49  ? 623 ASN B N   1 
ATOM   4268 C CA  . ASN A 1 567 ? 55.158 126.204 -67.297 1.00 43.09  ? 623 ASN B CA  1 
ATOM   4269 C C   . ASN A 1 567 ? 53.679 126.386 -67.692 1.00 38.77  ? 623 ASN B C   1 
ATOM   4270 O O   . ASN A 1 567 ? 52.875 125.474 -67.493 1.00 42.58  ? 623 ASN B O   1 
ATOM   4271 C CB  . ASN A 1 567 ? 55.270 125.916 -65.791 1.00 45.79  ? 623 ASN B CB  1 
ATOM   4272 C CG  . ASN A 1 567 ? 56.587 125.250 -65.412 1.00 45.21  ? 623 ASN B CG  1 
ATOM   4273 O OD1 . ASN A 1 567 ? 57.111 124.407 -66.144 1.00 45.81  ? 623 ASN B OD1 1 
ATOM   4274 N ND2 . ASN A 1 567 ? 57.121 125.624 -64.257 1.00 43.60  ? 623 ASN B ND2 1 
ATOM   4275 N N   . LEU A 1 568 ? 53.319 127.536 -68.256 1.00 32.71  ? 624 LEU B N   1 
ATOM   4276 C CA  . LEU A 1 568 ? 51.911 127.824 -68.516 1.00 28.65  ? 624 LEU B CA  1 
ATOM   4277 C C   . LEU A 1 568 ? 51.358 126.973 -69.648 1.00 26.04  ? 624 LEU B C   1 
ATOM   4278 O O   . LEU A 1 568 ? 51.852 127.026 -70.763 1.00 36.33  ? 624 LEU B O   1 
ATOM   4279 C CB  . LEU A 1 568 ? 51.723 129.299 -68.841 1.00 16.67  ? 624 LEU B CB  1 
ATOM   4280 C CG  . LEU A 1 568 ? 50.279 129.777 -68.988 1.00 29.05  ? 624 LEU B CG  1 
ATOM   4281 C CD1 . LEU A 1 568 ? 49.444 129.455 -67.732 1.00 20.68  ? 624 LEU B CD1 1 
ATOM   4282 C CD2 . LEU A 1 568 ? 50.265 131.268 -69.273 1.00 27.47  ? 624 LEU B CD2 1 
ATOM   4283 N N   . GLY A 1 569 ? 50.329 126.188 -69.358 1.00 24.40  ? 625 GLY B N   1 
ATOM   4284 C CA  . GLY A 1 569 ? 49.720 125.340 -70.366 1.00 24.77  ? 625 GLY B CA  1 
ATOM   4285 C C   . GLY A 1 569 ? 48.578 125.981 -71.138 1.00 28.35  ? 625 GLY B C   1 
ATOM   4286 O O   . GLY A 1 569 ? 48.333 125.647 -72.296 1.00 36.45  ? 625 GLY B O   1 
ATOM   4287 N N   . VAL A 1 570 ? 47.873 126.908 -70.499 1.00 24.71  ? 626 VAL B N   1 
ATOM   4288 C CA  . VAL A 1 570 ? 46.688 127.516 -71.100 1.00 24.51  ? 626 VAL B CA  1 
ATOM   4289 C C   . VAL A 1 570 ? 46.676 129.023 -70.855 1.00 22.71  ? 626 VAL B C   1 
ATOM   4290 O O   . VAL A 1 570 ? 46.903 129.485 -69.733 1.00 20.51  ? 626 VAL B O   1 
ATOM   4291 C CB  . VAL A 1 570 ? 45.399 126.860 -70.562 1.00 23.83  ? 626 VAL B CB  1 
ATOM   4292 C CG1 . VAL A 1 570 ? 44.159 127.611 -71.039 1.00 14.14  ? 626 VAL B CG1 1 
ATOM   4293 C CG2 . VAL A 1 570 ? 45.335 125.392 -70.979 1.00 24.34  ? 626 VAL B CG2 1 
ATOM   4294 N N   . LEU A 1 571 ? 46.448 129.788 -71.917 1.00 23.28  ? 627 LEU B N   1 
ATOM   4295 C CA  . LEU A 1 571 ? 46.436 131.246 -71.826 1.00 13.74  ? 627 LEU B CA  1 
ATOM   4296 C C   . LEU A 1 571 ? 45.282 131.859 -72.618 1.00 17.89  ? 627 LEU B C   1 
ATOM   4297 O O   . LEU A 1 571 ? 45.211 131.703 -73.839 1.00 28.06  ? 627 LEU B O   1 
ATOM   4298 C CB  . LEU A 1 571 ? 47.759 131.802 -72.354 1.00 14.77  ? 627 LEU B CB  1 
ATOM   4299 C CG  . LEU A 1 571 ? 47.892 133.320 -72.338 1.00 21.83  ? 627 LEU B CG  1 
ATOM   4300 C CD1 . LEU A 1 571 ? 47.753 133.905 -70.909 1.00 15.28  ? 627 LEU B CD1 1 
ATOM   4301 C CD2 . LEU A 1 571 ? 49.218 133.684 -72.934 1.00 21.00  ? 627 LEU B CD2 1 
ATOM   4302 N N   . ASP A 1 572 ? 44.377 132.550 -71.927 1.00 21.90  ? 628 ASP B N   1 
ATOM   4303 C CA  . ASP A 1 572 ? 43.285 133.262 -72.593 1.00 20.48  ? 628 ASP B CA  1 
ATOM   4304 C C   . ASP A 1 572 ? 43.300 134.753 -72.264 1.00 25.07  ? 628 ASP B C   1 
ATOM   4305 O O   . ASP A 1 572 ? 42.958 135.149 -71.145 1.00 29.86  ? 628 ASP B O   1 
ATOM   4306 C CB  . ASP A 1 572 ? 41.944 132.659 -72.173 1.00 18.68  ? 628 ASP B CB  1 
ATOM   4307 C CG  . ASP A 1 572 ? 40.799 133.065 -73.090 1.00 25.50  ? 628 ASP B CG  1 
ATOM   4308 O OD1 . ASP A 1 572 ? 40.950 134.053 -73.838 1.00 28.30  ? 628 ASP B OD1 1 
ATOM   4309 O OD2 . ASP A 1 572 ? 39.738 132.395 -73.055 1.00 24.37  ? 628 ASP B OD2 1 
ATOM   4310 N N   . VAL A 1 573 ? 43.704 135.561 -73.245 1.00 17.45  ? 629 VAL B N   1 
ATOM   4311 C CA  . VAL A 1 573 ? 43.614 137.024 -73.208 1.00 13.86  ? 629 VAL B CA  1 
ATOM   4312 C C   . VAL A 1 573 ? 42.481 137.600 -74.045 1.00 13.46  ? 629 VAL B C   1 
ATOM   4313 O O   . VAL A 1 573 ? 42.370 138.809 -74.186 1.00 19.68  ? 629 VAL B O   1 
ATOM   4314 C CB  . VAL A 1 573 ? 44.950 137.696 -73.621 1.00 14.89  ? 629 VAL B CB  1 
ATOM   4315 C CG1 . VAL A 1 573 ? 46.056 137.277 -72.666 1.00 15.36  ? 629 VAL B CG1 1 
ATOM   4316 C CG2 . VAL A 1 573 ? 45.321 137.328 -75.061 1.00 15.07  ? 629 VAL B CG2 1 
ATOM   4317 N N   . SER A 1 574 ? 41.652 136.739 -74.611 1.00 12.75  ? 630 SER B N   1 
ATOM   4318 C CA  . SER A 1 574 ? 40.696 137.129 -75.653 1.00 12.44  ? 630 SER B CA  1 
ATOM   4319 C C   . SER A 1 574 ? 39.704 138.188 -75.209 1.00 12.25  ? 630 SER B C   1 
ATOM   4320 O O   . SER A 1 574 ? 39.486 138.376 -74.024 1.00 14.13  ? 630 SER B O   1 
ATOM   4321 C CB  . SER A 1 574 ? 39.892 135.912 -76.088 1.00 24.35  ? 630 SER B CB  1 
ATOM   4322 O OG  . SER A 1 574 ? 39.039 135.498 -75.028 1.00 20.11  ? 630 SER B OG  1 
ATOM   4323 N N   . HIS A 1 575 ? 39.112 138.891 -76.170 1.00 20.53  ? 631 HIS B N   1 
ATOM   4324 C CA  . HIS A 1 575 ? 38.147 139.951 -75.870 1.00 15.75  ? 631 HIS B CA  1 
ATOM   4325 C C   . HIS A 1 575 ? 38.710 141.014 -74.975 1.00 13.94  ? 631 HIS B C   1 
ATOM   4326 O O   . HIS A 1 575 ? 38.128 141.331 -73.938 1.00 18.30  ? 631 HIS B O   1 
ATOM   4327 C CB  . HIS A 1 575 ? 36.874 139.413 -75.214 1.00 12.19  ? 631 HIS B CB  1 
ATOM   4328 C CG  . HIS A 1 575 ? 35.972 138.711 -76.168 1.00 10.68  ? 631 HIS B CG  1 
ATOM   4329 N ND1 . HIS A 1 575 ? 35.968 137.339 -76.309 1.00 19.24  ? 631 HIS B ND1 1 
ATOM   4330 C CD2 . HIS A 1 575 ? 35.073 139.191 -77.055 1.00 12.65  ? 631 HIS B CD2 1 
ATOM   4331 C CE1 . HIS A 1 575 ? 35.087 137.002 -77.234 1.00 22.83  ? 631 HIS B CE1 1 
ATOM   4332 N NE2 . HIS A 1 575 ? 34.532 138.107 -77.704 1.00 20.98  ? 631 HIS B NE2 1 
ATOM   4333 N N   . ASN A 1 576 ? 39.848 141.550 -75.374 1.00 15.92  ? 632 ASN B N   1 
ATOM   4334 C CA  . ASN A 1 576 ? 40.372 142.758 -74.766 1.00 18.39  ? 632 ASN B CA  1 
ATOM   4335 C C   . ASN A 1 576 ? 40.756 143.746 -75.866 1.00 19.13  ? 632 ASN B C   1 
ATOM   4336 O O   . ASN A 1 576 ? 40.407 143.556 -77.028 1.00 19.00  ? 632 ASN B O   1 
ATOM   4337 C CB  . ASN A 1 576 ? 41.564 142.445 -73.861 1.00 20.52  ? 632 ASN B CB  1 
ATOM   4338 C CG  . ASN A 1 576 ? 41.148 141.789 -72.576 1.00 24.62  ? 632 ASN B CG  1 
ATOM   4339 O OD1 . ASN A 1 576 ? 40.638 142.450 -71.675 1.00 24.31  ? 632 ASN B OD1 1 
ATOM   4340 N ND2 . ASN A 1 576 ? 41.364 140.483 -72.474 1.00 26.58  ? 632 ASN B ND2 1 
ATOM   4341 N N   . GLN A 1 577 ? 41.389 144.840 -75.461 1.00 17.92  ? 633 GLN B N   1 
ATOM   4342 C CA  . GLN A 1 577 ? 41.936 145.854 -76.352 1.00 16.42  ? 633 GLN B CA  1 
ATOM   4343 C C   . GLN A 1 577 ? 43.437 145.788 -76.579 1.00 17.21  ? 633 GLN B C   1 
ATOM   4344 O O   . GLN A 1 577 ? 44.057 146.803 -76.894 1.00 26.94  ? 633 GLN B O   1 
ATOM   4345 C CB  . GLN A 1 577 ? 41.428 147.240 -76.004 1.00 30.07  ? 633 GLN B CB  1 
ATOM   4346 C CG  . GLN A 1 577 ? 39.939 147.359 -76.257 1.00 26.02  ? 633 GLN B CG  1 
ATOM   4347 C CD  . GLN A 1 577 ? 39.293 148.409 -75.386 1.00 41.57  ? 633 GLN B CD  1 
ATOM   4348 O OE1 . GLN A 1 577 ? 38.846 148.125 -74.268 1.00 44.68  ? 633 GLN B OE1 1 
ATOM   4349 N NE2 . GLN A 1 577 ? 39.245 149.637 -75.888 1.00 49.32  ? 633 GLN B NE2 1 
ATOM   4350 N N   . LEU A 1 578 ? 44.031 144.642 -76.260 1.00 19.01  ? 634 LEU B N   1 
ATOM   4351 C CA  . LEU A 1 578 ? 45.471 144.395 -76.427 1.00 17.79  ? 634 LEU B CA  1 
ATOM   4352 C C   . LEU A 1 578 ? 46.078 144.675 -77.829 1.00 26.90  ? 634 LEU B C   1 
ATOM   4353 O O   . LEU A 1 578 ? 45.470 144.368 -78.852 1.00 17.95  ? 634 LEU B O   1 
ATOM   4354 C CB  . LEU A 1 578 ? 45.767 142.959 -75.991 1.00 17.39  ? 634 LEU B CB  1 
ATOM   4355 C CG  . LEU A 1 578 ? 45.399 142.743 -74.515 1.00 24.61  ? 634 LEU B CG  1 
ATOM   4356 C CD1 . LEU A 1 578 ? 45.413 141.273 -74.087 1.00 18.65  ? 634 LEU B CD1 1 
ATOM   4357 C CD2 . LEU A 1 578 ? 46.321 143.576 -73.614 1.00 24.79  ? 634 LEU B CD2 1 
ATOM   4358 N N   . THR A 1 579 ? 47.282 145.253 -77.864 1.00 27.98  ? 635 THR B N   1 
ATOM   4359 C CA  . THR A 1 579 ? 47.960 145.580 -79.137 1.00 27.19  ? 635 THR B CA  1 
ATOM   4360 C C   . THR A 1 579 ? 49.368 144.988 -79.358 1.00 26.79  ? 635 THR B C   1 
ATOM   4361 O O   . THR A 1 579 ? 49.926 144.279 -78.504 1.00 20.63  ? 635 THR B O   1 
ATOM   4362 C CB  . THR A 1 579 ? 48.064 147.118 -79.380 1.00 20.63  ? 635 THR B CB  1 
ATOM   4363 O OG1 . THR A 1 579 ? 48.823 147.739 -78.331 1.00 23.98  ? 635 THR B OG1 1 
ATOM   4364 C CG2 . THR A 1 579 ? 46.681 147.762 -79.470 1.00 20.07  ? 635 THR B CG2 1 
ATOM   4365 N N   . GLY A 1 580 ? 49.934 145.301 -80.524 1.00 21.20  ? 636 GLY B N   1 
ATOM   4366 C CA  . GLY A 1 580 ? 51.254 144.821 -80.889 1.00 21.92  ? 636 GLY B CA  1 
ATOM   4367 C C   . GLY A 1 580 ? 51.235 143.361 -81.287 1.00 21.42  ? 636 GLY B C   1 
ATOM   4368 O O   . GLY A 1 580 ? 50.181 142.815 -81.597 1.00 33.76  ? 636 GLY B O   1 
ATOM   4369 N N   . ASN A 1 581 ? 52.397 142.718 -81.269 1.00 21.98  ? 637 ASN B N   1 
ATOM   4370 C CA  . ASN A 1 581 ? 52.488 141.346 -81.738 1.00 25.20  ? 637 ASN B CA  1 
ATOM   4371 C C   . ASN A 1 581 ? 52.617 140.293 -80.657 1.00 28.85  ? 637 ASN B C   1 
ATOM   4372 O O   . ASN A 1 581 ? 52.518 140.576 -79.463 1.00 31.20  ? 637 ASN B O   1 
ATOM   4373 C CB  . ASN A 1 581 ? 53.606 141.180 -82.769 1.00 26.53  ? 637 ASN B CB  1 
ATOM   4374 C CG  . ASN A 1 581 ? 54.966 141.517 -82.212 1.00 32.81  ? 637 ASN B CG  1 
ATOM   4375 O OD1 . ASN A 1 581 ? 55.433 140.893 -81.264 1.00 36.09  ? 637 ASN B OD1 1 
ATOM   4376 N ND2 . ASN A 1 581 ? 55.622 142.497 -82.814 1.00 35.81  ? 637 ASN B ND2 1 
ATOM   4377 N N   . LEU A 1 582 ? 52.792 139.062 -81.112 1.00 28.89  ? 638 LEU B N   1 
ATOM   4378 C CA  . LEU A 1 582 ? 52.855 137.894 -80.246 1.00 24.61  ? 638 LEU B CA  1 
ATOM   4379 C C   . LEU A 1 582 ? 54.257 137.377 -79.968 1.00 21.44  ? 638 LEU B C   1 
ATOM   4380 O O   . LEU A 1 582 ? 54.402 136.325 -79.359 1.00 36.16  ? 638 LEU B O   1 
ATOM   4381 C CB  . LEU A 1 582 ? 51.980 136.780 -80.831 1.00 19.76  ? 638 LEU B CB  1 
ATOM   4382 C CG  . LEU A 1 582 ? 50.516 137.208 -80.986 1.00 23.63  ? 638 LEU B CG  1 
ATOM   4383 C CD1 . LEU A 1 582 ? 49.633 136.028 -81.341 1.00 21.41  ? 638 LEU B CD1 1 
ATOM   4384 C CD2 . LEU A 1 582 ? 50.004 137.882 -79.691 1.00 28.46  ? 638 LEU B CD2 1 
ATOM   4385 N N   . ASN A 1 583 ? 55.278 138.075 -80.461 1.00 36.37  ? 639 ASN B N   1 
ATOM   4386 C CA  . ASN A 1 583 ? 56.660 137.559 -80.437 1.00 32.04  ? 639 ASN B CA  1 
ATOM   4387 C C   . ASN A 1 583 ? 57.134 137.058 -79.080 1.00 33.43  ? 639 ASN B C   1 
ATOM   4388 O O   . ASN A 1 583 ? 57.886 136.082 -78.994 1.00 34.92  ? 639 ASN B O   1 
ATOM   4389 C CB  . ASN A 1 583 ? 57.643 138.599 -80.979 1.00 26.32  ? 639 ASN B CB  1 
ATOM   4390 C CG  . ASN A 1 583 ? 57.373 138.939 -82.429 1.00 26.83  ? 639 ASN B CG  1 
ATOM   4391 O OD1 . ASN A 1 583 ? 56.660 138.212 -83.126 1.00 30.56  ? 639 ASN B OD1 1 
ATOM   4392 N ND2 . ASN A 1 583 ? 57.930 140.046 -82.889 1.00 25.34  ? 639 ASN B ND2 1 
ATOM   4393 N N   . VAL A 1 584 ? 56.664 137.724 -78.030 1.00 31.03  ? 640 VAL B N   1 
ATOM   4394 C CA  . VAL A 1 584 ? 57.023 137.409 -76.664 1.00 36.15  ? 640 VAL B CA  1 
ATOM   4395 C C   . VAL A 1 584 ? 56.625 135.973 -76.309 1.00 41.91  ? 640 VAL B C   1 
ATOM   4396 O O   . VAL A 1 584 ? 57.202 135.358 -75.404 1.00 41.35  ? 640 VAL B O   1 
ATOM   4397 C CB  . VAL A 1 584 ? 56.343 138.406 -75.712 1.00 43.74  ? 640 VAL B CB  1 
ATOM   4398 C CG1 . VAL A 1 584 ? 54.829 138.355 -75.886 1.00 41.75  ? 640 VAL B CG1 1 
ATOM   4399 C CG2 . VAL A 1 584 ? 56.735 138.145 -74.268 1.00 49.34  ? 640 VAL B CG2 1 
ATOM   4400 N N   . LEU A 1 585 ? 55.644 135.440 -77.036 1.00 38.94  ? 641 LEU B N   1 
ATOM   4401 C CA  . LEU A 1 585 ? 55.116 134.103 -76.772 1.00 32.68  ? 641 LEU B CA  1 
ATOM   4402 C C   . LEU A 1 585 ? 55.739 132.968 -77.587 1.00 36.85  ? 641 LEU B C   1 
ATOM   4403 O O   . LEU A 1 585 ? 55.479 131.797 -77.296 1.00 37.87  ? 641 LEU B O   1 
ATOM   4404 C CB  . LEU A 1 585 ? 53.599 134.090 -76.978 1.00 28.46  ? 641 LEU B CB  1 
ATOM   4405 C CG  . LEU A 1 585 ? 52.662 134.468 -75.827 1.00 28.93  ? 641 LEU B CG  1 
ATOM   4406 C CD1 . LEU A 1 585 ? 53.327 135.346 -74.773 1.00 29.43  ? 641 LEU B CD1 1 
ATOM   4407 C CD2 . LEU A 1 585 ? 51.418 135.153 -76.364 1.00 29.60  ? 641 LEU B CD2 1 
ATOM   4408 N N   . THR A 1 586 ? 56.554 133.298 -78.593 1.00 43.57  ? 642 THR B N   1 
ATOM   4409 C CA  . THR A 1 586 ? 57.014 132.290 -79.567 1.00 44.34  ? 642 THR B CA  1 
ATOM   4410 C C   . THR A 1 586 ? 57.824 131.177 -78.911 1.00 41.38  ? 642 THR B C   1 
ATOM   4411 O O   . THR A 1 586 ? 57.935 130.074 -79.457 1.00 37.98  ? 642 THR B O   1 
ATOM   4412 C CB  . THR A 1 586 ? 57.832 132.899 -80.769 1.00 44.78  ? 642 THR B CB  1 
ATOM   4413 O OG1 . THR A 1 586 ? 58.958 133.637 -80.288 1.00 43.58  ? 642 THR B OG1 1 
ATOM   4414 C CG2 . THR A 1 586 ? 56.967 133.819 -81.628 1.00 44.41  ? 642 THR B CG2 1 
ATOM   4415 N N   . ASP A 1 587 ? 58.372 131.485 -77.736 1.00 41.06  ? 643 ASP B N   1 
ATOM   4416 C CA  . ASP A 1 587 ? 59.285 130.601 -77.013 1.00 50.12  ? 643 ASP B CA  1 
ATOM   4417 C C   . ASP A 1 587 ? 58.671 129.746 -75.899 1.00 48.05  ? 643 ASP B C   1 
ATOM   4418 O O   . ASP A 1 587 ? 59.401 129.061 -75.180 1.00 44.60  ? 643 ASP B O   1 
ATOM   4419 C CB  . ASP A 1 587 ? 60.467 131.400 -76.456 1.00 61.37  ? 643 ASP B CB  1 
ATOM   4420 C CG  . ASP A 1 587 ? 61.806 130.861 -76.922 1.00 67.82  ? 643 ASP B CG  1 
ATOM   4421 O OD1 . ASP A 1 587 ? 61.885 130.397 -78.082 1.00 71.41  ? 643 ASP B OD1 1 
ATOM   4422 O OD2 . ASP A 1 587 ? 62.773 130.904 -76.126 1.00 67.59  ? 643 ASP B OD2 1 
ATOM   4423 N N   . LEU A 1 588 ? 57.354 129.781 -75.726 1.00 47.01  ? 644 LEU B N   1 
ATOM   4424 C CA  . LEU A 1 588 ? 56.781 128.925 -74.699 1.00 40.54  ? 644 LEU B CA  1 
ATOM   4425 C C   . LEU A 1 588 ? 56.428 127.610 -75.369 1.00 45.22  ? 644 LEU B C   1 
ATOM   4426 O O   . LEU A 1 588 ? 55.419 127.495 -76.069 1.00 48.67  ? 644 LEU B O   1 
ATOM   4427 C CB  . LEU A 1 588 ? 55.531 129.560 -74.085 1.00 25.64  ? 644 LEU B CB  1 
ATOM   4428 C CG  . LEU A 1 588 ? 55.719 130.961 -73.499 1.00 28.56  ? 644 LEU B CG  1 
ATOM   4429 C CD1 . LEU A 1 588 ? 54.378 131.587 -73.085 1.00 26.15  ? 644 LEU B CD1 1 
ATOM   4430 C CD2 . LEU A 1 588 ? 56.691 130.935 -72.319 1.00 28.44  ? 644 LEU B CD2 1 
ATOM   4431 N N   . GLN A 1 589 ? 57.248 126.603 -75.090 1.00 44.74  ? 645 GLN B N   1 
ATOM   4432 C CA  . GLN A 1 589 ? 57.118 125.294 -75.713 1.00 49.85  ? 645 GLN B CA  1 
ATOM   4433 C C   . GLN A 1 589 ? 56.043 124.475 -75.003 1.00 50.67  ? 645 GLN B C   1 
ATOM   4434 O O   . GLN A 1 589 ? 55.520 123.501 -75.551 1.00 53.11  ? 645 GLN B O   1 
ATOM   4435 C CB  . GLN A 1 589 ? 58.466 124.560 -75.696 1.00 57.78  ? 645 GLN B CB  1 
ATOM   4436 C CG  . GLN A 1 589 ? 58.907 124.029 -74.319 1.00 69.62  ? 645 GLN B CG  1 
ATOM   4437 C CD  . GLN A 1 589 ? 59.398 125.112 -73.352 1.00 75.79  ? 645 GLN B CD  1 
ATOM   4438 O OE1 . GLN A 1 589 ? 59.356 126.307 -73.652 1.00 82.63  ? 645 GLN B OE1 1 
ATOM   4439 N NE2 . GLN A 1 589 ? 59.868 124.686 -72.182 1.00 72.27  ? 645 GLN B NE2 1 
ATOM   4440 N N   . ASN A 1 590 ? 55.714 124.883 -73.780 1.00 48.36  ? 646 ASN B N   1 
ATOM   4441 C CA  . ASN A 1 590 ? 54.669 124.222 -73.008 1.00 48.12  ? 646 ASN B CA  1 
ATOM   4442 C C   . ASN A 1 590 ? 53.296 124.872 -73.165 1.00 41.75  ? 646 ASN B C   1 
ATOM   4443 O O   . ASN A 1 590 ? 52.317 124.421 -72.581 1.00 33.09  ? 646 ASN B O   1 
ATOM   4444 C CB  . ASN A 1 590 ? 55.061 124.143 -71.537 1.00 55.29  ? 646 ASN B CB  1 
ATOM   4445 C CG  . ASN A 1 590 ? 56.153 123.128 -71.287 1.00 60.95  ? 646 ASN B CG  1 
ATOM   4446 O OD1 . ASN A 1 590 ? 56.188 122.074 -71.924 1.00 64.39  ? 646 ASN B OD1 1 
ATOM   4447 N ND2 . ASN A 1 590 ? 57.056 123.439 -70.360 1.00 59.33  ? 646 ASN B ND2 1 
ATOM   4448 N N   . LEU A 1 591 ? 53.217 125.927 -73.964 1.00 42.00  ? 647 LEU B N   1 
ATOM   4449 C CA  . LEU A 1 591 ? 51.923 126.513 -74.250 1.00 39.40  ? 647 LEU B CA  1 
ATOM   4450 C C   . LEU A 1 591 ? 51.114 125.561 -75.127 1.00 43.11  ? 647 LEU B C   1 
ATOM   4451 O O   . LEU A 1 591 ? 51.592 125.081 -76.156 1.00 52.83  ? 647 LEU B O   1 
ATOM   4452 C CB  . LEU A 1 591 ? 52.080 127.871 -74.918 1.00 40.57  ? 647 LEU B CB  1 
ATOM   4453 C CG  . LEU A 1 591 ? 50.828 128.743 -74.892 1.00 34.20  ? 647 LEU B CG  1 
ATOM   4454 C CD1 . LEU A 1 591 ? 50.219 128.756 -73.494 1.00 32.80  ? 647 LEU B CD1 1 
ATOM   4455 C CD2 . LEU A 1 591 ? 51.192 130.141 -75.327 1.00 32.14  ? 647 LEU B CD2 1 
ATOM   4456 N N   . VAL A 1 592 ? 49.887 125.293 -74.699 1.00 35.99  ? 648 VAL B N   1 
ATOM   4457 C CA  . VAL A 1 592 ? 49.011 124.320 -75.335 1.00 32.67  ? 648 VAL B CA  1 
ATOM   4458 C C   . VAL A 1 592 ? 47.799 125.020 -75.942 1.00 32.20  ? 648 VAL B C   1 
ATOM   4459 O O   . VAL A 1 592 ? 47.514 124.878 -77.126 1.00 33.77  ? 648 VAL B O   1 
ATOM   4460 C CB  . VAL A 1 592 ? 48.557 123.237 -74.339 1.00 37.55  ? 648 VAL B CB  1 
ATOM   4461 C CG1 . VAL A 1 592 ? 47.653 122.221 -75.023 1.00 36.26  ? 648 VAL B CG1 1 
ATOM   4462 C CG2 . VAL A 1 592 ? 49.773 122.554 -73.715 1.00 37.78  ? 648 VAL B CG2 1 
ATOM   4463 N N   . SER A 1 593 ? 47.051 125.725 -75.106 1.00 32.06  ? 649 SER B N   1 
ATOM   4464 C CA  . SER A 1 593 ? 45.883 126.468 -75.565 1.00 25.91  ? 649 SER B CA  1 
ATOM   4465 C C   . SER A 1 593 ? 46.162 127.977 -75.526 1.00 19.81  ? 649 SER B C   1 
ATOM   4466 O O   . SER A 1 593 ? 46.596 128.513 -74.508 1.00 27.85  ? 649 SER B O   1 
ATOM   4467 C CB  . SER A 1 593 ? 44.669 126.086 -74.702 1.00 25.72  ? 649 SER B CB  1 
ATOM   4468 O OG  . SER A 1 593 ? 43.530 126.878 -74.973 1.00 26.34  ? 649 SER B OG  1 
ATOM   4469 N N   . LEU A 1 594 ? 45.944 128.658 -76.646 1.00 21.46  ? 650 LEU B N   1 
ATOM   4470 C CA  . LEU A 1 594 ? 46.152 130.109 -76.725 1.00 21.07  ? 650 LEU B CA  1 
ATOM   4471 C C   . LEU A 1 594 ? 44.935 130.714 -77.339 1.00 13.15  ? 650 LEU B C   1 
ATOM   4472 O O   . LEU A 1 594 ? 44.622 130.393 -78.472 1.00 25.06  ? 650 LEU B O   1 
ATOM   4473 C CB  . LEU A 1 594 ? 47.353 130.467 -77.609 1.00 14.63  ? 650 LEU B CB  1 
ATOM   4474 C CG  . LEU A 1 594 ? 47.713 131.964 -77.702 1.00 15.23  ? 650 LEU B CG  1 
ATOM   4475 C CD1 . LEU A 1 594 ? 47.858 132.588 -76.326 1.00 15.35  ? 650 LEU B CD1 1 
ATOM   4476 C CD2 . LEU A 1 594 ? 48.988 132.203 -78.504 1.00 16.22  ? 650 LEU B CD2 1 
ATOM   4477 N N   . ASN A 1 595 ? 44.228 131.565 -76.603 1.00 12.85  ? 651 ASN B N   1 
ATOM   4478 C CA  . ASN A 1 595 ? 43.128 132.289 -77.216 1.00 12.46  ? 651 ASN B CA  1 
ATOM   4479 C C   . ASN A 1 595 ? 43.461 133.787 -77.260 1.00 24.20  ? 651 ASN B C   1 
ATOM   4480 O O   . ASN A 1 595 ? 43.393 134.483 -76.248 1.00 39.04  ? 651 ASN B O   1 
ATOM   4481 C CB  . ASN A 1 595 ? 41.821 132.003 -76.458 1.00 11.56  ? 651 ASN B CB  1 
ATOM   4482 C CG  . ASN A 1 595 ? 40.593 132.453 -77.219 1.00 11.09  ? 651 ASN B CG  1 
ATOM   4483 O OD1 . ASN A 1 595 ? 40.708 133.338 -78.068 1.00 11.49  ? 651 ASN B OD1 1 
ATOM   4484 N ND2 . ASN A 1 595 ? 39.397 131.868 -76.924 1.00 10.26  ? 651 ASN B ND2 1 
ATOM   4485 N N   . ILE A 1 596 ? 43.852 134.269 -78.436 1.00 20.61  ? 652 ILE B N   1 
ATOM   4486 C CA  . ILE A 1 596 ? 44.171 135.687 -78.639 1.00 18.34  ? 652 ILE B CA  1 
ATOM   4487 C C   . ILE A 1 596 ? 43.102 136.524 -79.353 1.00 13.91  ? 652 ILE B C   1 
ATOM   4488 O O   . ILE A 1 596 ? 43.331 137.685 -79.676 1.00 22.08  ? 652 ILE B O   1 
ATOM   4489 C CB  . ILE A 1 596 ? 45.590 135.914 -79.233 1.00 15.17  ? 652 ILE B CB  1 
ATOM   4490 C CG1 . ILE A 1 596 ? 45.838 135.071 -80.505 1.00 15.23  ? 652 ILE B CG1 1 
ATOM   4491 C CG2 . ILE A 1 596 ? 46.631 135.576 -78.183 1.00 15.59  ? 652 ILE B CG2 1 
ATOM   4492 C CD1 . ILE A 1 596 ? 44.895 135.310 -81.630 1.00 14.88  ? 652 ILE B CD1 1 
ATOM   4493 N N   . SER A 1 597 ? 41.967 135.907 -79.638 1.00 13.11  ? 653 SER B N   1 
ATOM   4494 C CA  . SER A 1 597 ? 40.933 136.518 -80.464 1.00 26.51  ? 653 SER B CA  1 
ATOM   4495 C C   . SER A 1 597 ? 40.269 137.743 -79.827 1.00 12.80  ? 653 SER B C   1 
ATOM   4496 O O   . SER A 1 597 ? 40.368 137.957 -78.627 1.00 25.31  ? 653 SER B O   1 
ATOM   4497 C CB  . SER A 1 597 ? 39.881 135.471 -80.832 1.00 12.01  ? 653 SER B CB  1 
ATOM   4498 O OG  . SER A 1 597 ? 38.998 135.261 -79.758 1.00 14.09  ? 653 SER B OG  1 
ATOM   4499 N N   . TYR A 1 598 ? 39.611 138.548 -80.660 1.00 12.85  ? 654 TYR B N   1 
ATOM   4500 C CA  . TYR A 1 598 ? 38.944 139.799 -80.267 1.00 12.86  ? 654 TYR B CA  1 
ATOM   4501 C C   . TYR A 1 598 ? 39.836 140.772 -79.518 1.00 22.60  ? 654 TYR B C   1 
ATOM   4502 O O   . TYR A 1 598 ? 39.500 141.258 -78.441 1.00 29.15  ? 654 TYR B O   1 
ATOM   4503 C CB  . TYR A 1 598 ? 37.638 139.533 -79.520 1.00 28.16  ? 654 TYR B CB  1 
ATOM   4504 C CG  . TYR A 1 598 ? 36.641 138.791 -80.370 1.00 27.01  ? 654 TYR B CG  1 
ATOM   4505 C CD1 . TYR A 1 598 ? 35.768 139.476 -81.206 1.00 23.40  ? 654 TYR B CD1 1 
ATOM   4506 C CD2 . TYR A 1 598 ? 36.597 137.400 -80.367 1.00 26.82  ? 654 TYR B CD2 1 
ATOM   4507 C CE1 . TYR A 1 598 ? 34.862 138.796 -82.001 1.00 16.64  ? 654 TYR B CE1 1 
ATOM   4508 C CE2 . TYR A 1 598 ? 35.696 136.716 -81.153 1.00 20.72  ? 654 TYR B CE2 1 
ATOM   4509 C CZ  . TYR A 1 598 ? 34.834 137.421 -81.968 1.00 25.38  ? 654 TYR B CZ  1 
ATOM   4510 O OH  . TYR A 1 598 ? 33.932 136.748 -82.760 1.00 39.65  ? 654 TYR B OH  1 
ATOM   4511 N N   . ASN A 1 599 ? 40.985 141.043 -80.115 1.00 14.34  ? 655 ASN B N   1 
ATOM   4512 C CA  . ASN A 1 599 ? 41.883 142.072 -79.650 1.00 15.15  ? 655 ASN B CA  1 
ATOM   4513 C C   . ASN A 1 599 ? 42.279 142.958 -80.839 1.00 18.48  ? 655 ASN B C   1 
ATOM   4514 O O   . ASN A 1 599 ? 41.705 142.855 -81.925 1.00 16.88  ? 655 ASN B O   1 
ATOM   4515 C CB  . ASN A 1 599 ? 43.121 141.454 -78.982 1.00 15.54  ? 655 ASN B CB  1 
ATOM   4516 C CG  . ASN A 1 599 ? 42.843 140.946 -77.567 1.00 19.91  ? 655 ASN B CG  1 
ATOM   4517 O OD1 . ASN A 1 599 ? 42.781 141.724 -76.617 1.00 15.26  ? 655 ASN B OD1 1 
ATOM   4518 N ND2 . ASN A 1 599 ? 42.703 139.636 -77.425 1.00 19.23  ? 655 ASN B ND2 1 
ATOM   4519 N N   . ASP A 1 600 ? 43.197 143.882 -80.583 1.00 18.21  ? 656 ASP B N   1 
ATOM   4520 C CA  . ASP A 1 600 ? 43.845 144.738 -81.580 1.00 17.42  ? 656 ASP B CA  1 
ATOM   4521 C C   . ASP A 1 600 ? 45.252 144.298 -82.017 1.00 18.11  ? 656 ASP B C   1 
ATOM   4522 O O   . ASP A 1 600 ? 46.035 145.134 -82.429 1.00 30.19  ? 656 ASP B O   1 
ATOM   4523 C CB  . ASP A 1 600 ? 43.822 146.208 -81.163 1.00 32.98  ? 656 ASP B CB  1 
ATOM   4524 C CG  . ASP A 1 600 ? 42.423 146.704 -80.881 1.00 39.14  ? 656 ASP B CG  1 
ATOM   4525 O OD1 . ASP A 1 600 ? 41.572 146.664 -81.800 1.00 16.97  ? 656 ASP B OD1 1 
ATOM   4526 O OD2 . ASP A 1 600 ? 42.174 147.131 -79.733 1.00 45.49  ? 656 ASP B OD2 1 
ATOM   4527 N N   . PHE A 1 601 ? 45.631 143.053 -81.758 1.00 17.84  ? 657 PHE B N   1 
ATOM   4528 C CA  . PHE A 1 601 ? 46.918 142.521 -82.219 1.00 18.48  ? 657 PHE B CA  1 
ATOM   4529 C C   . PHE A 1 601 ? 47.157 142.692 -83.756 1.00 28.10  ? 657 PHE B C   1 
ATOM   4530 O O   . PHE A 1 601 ? 46.233 142.592 -84.573 1.00 24.23  ? 657 PHE B O   1 
ATOM   4531 C CB  . PHE A 1 601 ? 47.055 141.026 -81.849 1.00 18.00  ? 657 PHE B CB  1 
ATOM   4532 C CG  . PHE A 1 601 ? 47.086 140.741 -80.362 1.00 30.45  ? 657 PHE B CG  1 
ATOM   4533 C CD1 . PHE A 1 601 ? 48.115 141.224 -79.559 1.00 27.69  ? 657 PHE B CD1 1 
ATOM   4534 C CD2 . PHE A 1 601 ? 46.106 139.947 -79.773 1.00 29.89  ? 657 PHE B CD2 1 
ATOM   4535 C CE1 . PHE A 1 601 ? 48.150 140.942 -78.209 1.00 24.72  ? 657 PHE B CE1 1 
ATOM   4536 C CE2 . PHE A 1 601 ? 46.132 139.662 -78.419 1.00 28.88  ? 657 PHE B CE2 1 
ATOM   4537 C CZ  . PHE A 1 601 ? 47.156 140.158 -77.633 1.00 27.56  ? 657 PHE B CZ  1 
ATOM   4538 N N   . SER A 1 602 ? 48.402 142.961 -84.139 1.00 23.77  ? 658 SER B N   1 
ATOM   4539 C CA  . SER A 1 602 ? 48.777 143.001 -85.546 1.00 20.25  ? 658 SER B CA  1 
ATOM   4540 C C   . SER A 1 602 ? 50.186 142.448 -85.694 1.00 21.86  ? 658 SER B C   1 
ATOM   4541 O O   . SER A 1 602 ? 50.925 142.329 -84.710 1.00 23.18  ? 658 SER B O   1 
ATOM   4542 C CB  . SER A 1 602 ? 48.694 144.425 -86.120 1.00 20.79  ? 658 SER B CB  1 
ATOM   4543 O OG  . SER A 1 602 ? 49.825 145.199 -85.789 1.00 56.12  ? 658 SER B OG  1 
ATOM   4544 N N   . GLY A 1 603 ? 50.573 142.121 -86.918 1.00 23.42  ? 659 GLY B N   1 
ATOM   4545 C CA  . GLY A 1 603 ? 51.884 141.544 -87.128 1.00 22.07  ? 659 GLY B CA  1 
ATOM   4546 C C   . GLY A 1 603 ? 51.857 140.092 -87.541 1.00 21.67  ? 659 GLY B C   1 
ATOM   4547 O O   . GLY A 1 603 ? 50.817 139.406 -87.531 1.00 22.86  ? 659 GLY B O   1 
ATOM   4548 N N   . ASP A 1 604 ? 53.013 139.615 -87.958 1.00 22.41  ? 660 ASP B N   1 
ATOM   4549 C CA  . ASP A 1 604 ? 53.086 138.256 -88.446 1.00 36.64  ? 660 ASP B CA  1 
ATOM   4550 C C   . ASP A 1 604 ? 53.497 137.280 -87.367 1.00 35.27  ? 660 ASP B C   1 
ATOM   4551 O O   . ASP A 1 604 ? 54.323 137.573 -86.511 1.00 37.34  ? 660 ASP B O   1 
ATOM   4552 C CB  . ASP A 1 604 ? 54.002 138.138 -89.662 1.00 37.34  ? 660 ASP B CB  1 
ATOM   4553 C CG  . ASP A 1 604 ? 55.401 138.597 -89.380 1.00 41.99  ? 660 ASP B CG  1 
ATOM   4554 O OD1 . ASP A 1 604 ? 55.642 139.819 -89.401 1.00 50.41  ? 660 ASP B OD1 1 
ATOM   4555 O OD2 . ASP A 1 604 ? 56.268 137.737 -89.146 1.00 49.92  ? 660 ASP B OD2 1 
ATOM   4556 N N   . LEU A 1 605 ? 52.862 136.123 -87.415 1.00 38.37  ? 661 LEU B N   1 
ATOM   4557 C CA  . LEU A 1 605 ? 53.246 134.980 -86.632 1.00 43.65  ? 661 LEU B CA  1 
ATOM   4558 C C   . LEU A 1 605 ? 54.252 134.183 -87.462 1.00 56.75  ? 661 LEU B C   1 
ATOM   4559 O O   . LEU A 1 605 ? 54.234 134.236 -88.703 1.00 54.75  ? 661 LEU B O   1 
ATOM   4560 C CB  . LEU A 1 605 ? 52.012 134.125 -86.370 1.00 37.65  ? 661 LEU B CB  1 
ATOM   4561 C CG  . LEU A 1 605 ? 50.745 134.867 -85.948 1.00 28.13  ? 661 LEU B CG  1 
ATOM   4562 C CD1 . LEU A 1 605 ? 49.516 134.004 -86.166 1.00 21.10  ? 661 LEU B CD1 1 
ATOM   4563 C CD2 . LEU A 1 605 ? 50.845 135.297 -84.510 1.00 25.65  ? 661 LEU B CD2 1 
ATOM   4564 N N   . PRO A 1 606 ? 55.139 133.441 -86.778 1.00 59.10  ? 662 PRO B N   1 
ATOM   4565 C CA  . PRO A 1 606 ? 56.028 132.484 -87.444 1.00 58.13  ? 662 PRO B CA  1 
ATOM   4566 C C   . PRO A 1 606 ? 55.202 131.325 -88.005 1.00 58.36  ? 662 PRO B C   1 
ATOM   4567 O O   . PRO A 1 606 ? 54.041 131.168 -87.624 1.00 46.38  ? 662 PRO B O   1 
ATOM   4568 C CB  . PRO A 1 606 ? 56.922 131.997 -86.303 1.00 49.10  ? 662 PRO B CB  1 
ATOM   4569 C CG  . PRO A 1 606 ? 56.076 132.165 -85.083 1.00 47.18  ? 662 PRO B CG  1 
ATOM   4570 C CD  . PRO A 1 606 ? 55.297 133.418 -85.312 1.00 46.67  ? 662 PRO B CD  1 
ATOM   4571 N N   . ASN A 1 607 ? 55.790 130.527 -88.889 1.00 63.33  ? 663 ASN B N   1 
ATOM   4572 C CA  . ASN A 1 607 ? 55.092 129.373 -89.452 1.00 65.47  ? 663 ASN B CA  1 
ATOM   4573 C C   . ASN A 1 607 ? 55.246 128.089 -88.611 1.00 74.94  ? 663 ASN B C   1 
ATOM   4574 O O   . ASN A 1 607 ? 54.874 127.004 -89.064 1.00 75.37  ? 663 ASN B O   1 
ATOM   4575 C CB  . ASN A 1 607 ? 55.488 129.131 -90.911 1.00 59.14  ? 663 ASN B CB  1 
ATOM   4576 C CG  . ASN A 1 607 ? 54.348 128.548 -91.737 1.00 56.05  ? 663 ASN B CG  1 
ATOM   4577 O OD1 . ASN A 1 607 ? 54.300 128.712 -92.958 1.00 54.77  ? 663 ASN B OD1 1 
ATOM   4578 N ND2 . ASN A 1 607 ? 53.422 127.871 -91.072 1.00 54.66  ? 663 ASN B ND2 1 
ATOM   4579 N N   . THR A 1 608 ? 55.815 128.217 -87.407 1.00 75.24  ? 664 THR B N   1 
ATOM   4580 C CA  . THR A 1 608 ? 55.989 127.085 -86.494 1.00 67.63  ? 664 THR B CA  1 
ATOM   4581 C C   . THR A 1 608 ? 54.651 126.375 -86.279 1.00 66.87  ? 664 THR B C   1 
ATOM   4582 O O   . THR A 1 608 ? 53.596 126.988 -86.445 1.00 67.93  ? 664 THR B O   1 
ATOM   4583 C CB  . THR A 1 608 ? 56.526 127.541 -85.122 1.00 59.95  ? 664 THR B CB  1 
ATOM   4584 O OG1 . THR A 1 608 ? 55.428 127.855 -84.257 1.00 58.04  ? 664 THR B OG1 1 
ATOM   4585 C CG2 . THR A 1 608 ? 57.457 128.730 -85.266 1.00 55.75  ? 664 THR B CG2 1 
ATOM   4586 N N   . PRO A 1 609 ? 54.686 125.076 -85.919 1.00 64.08  ? 665 PRO B N   1 
ATOM   4587 C CA  . PRO A 1 609 ? 53.432 124.316 -85.973 1.00 63.00  ? 665 PRO B CA  1 
ATOM   4588 C C   . PRO A 1 609 ? 52.394 124.841 -84.983 1.00 54.57  ? 665 PRO B C   1 
ATOM   4589 O O   . PRO A 1 609 ? 51.189 124.740 -85.251 1.00 52.00  ? 665 PRO B O   1 
ATOM   4590 C CB  . PRO A 1 609 ? 53.872 122.902 -85.591 1.00 64.32  ? 665 PRO B CB  1 
ATOM   4591 C CG  . PRO A 1 609 ? 55.054 123.121 -84.705 1.00 62.03  ? 665 PRO B CG  1 
ATOM   4592 C CD  . PRO A 1 609 ? 55.766 124.304 -85.275 1.00 59.25  ? 665 PRO B CD  1 
ATOM   4593 N N   . PHE A 1 610 ? 52.848 125.413 -83.870 1.00 44.06  ? 666 PHE B N   1 
ATOM   4594 C CA  . PHE A 1 610 ? 51.902 125.918 -82.887 1.00 44.68  ? 666 PHE B CA  1 
ATOM   4595 C C   . PHE A 1 610 ? 51.114 127.125 -83.371 1.00 51.21  ? 666 PHE B C   1 
ATOM   4596 O O   . PHE A 1 610 ? 49.893 127.173 -83.237 1.00 50.59  ? 666 PHE B O   1 
ATOM   4597 C CB  . PHE A 1 610 ? 52.567 126.264 -81.569 1.00 43.92  ? 666 PHE B CB  1 
ATOM   4598 C CG  . PHE A 1 610 ? 51.595 126.736 -80.540 1.00 46.63  ? 666 PHE B CG  1 
ATOM   4599 C CD1 . PHE A 1 610 ? 50.530 125.930 -80.167 1.00 43.12  ? 666 PHE B CD1 1 
ATOM   4600 C CD2 . PHE A 1 610 ? 51.707 127.998 -79.978 1.00 50.32  ? 666 PHE B CD2 1 
ATOM   4601 C CE1 . PHE A 1 610 ? 49.615 126.357 -79.222 1.00 42.93  ? 666 PHE B CE1 1 
ATOM   4602 C CE2 . PHE A 1 610 ? 50.791 128.434 -79.034 1.00 47.43  ? 666 PHE B CE2 1 
ATOM   4603 C CZ  . PHE A 1 610 ? 49.743 127.611 -78.656 1.00 44.51  ? 666 PHE B CZ  1 
ATOM   4604 N N   . PHE A 1 611 ? 51.808 128.112 -83.919 1.00 54.06  ? 667 PHE B N   1 
ATOM   4605 C CA  . PHE A 1 611 ? 51.110 129.283 -84.423 1.00 50.86  ? 667 PHE B CA  1 
ATOM   4606 C C   . PHE A 1 611 ? 50.302 128.962 -85.676 1.00 55.38  ? 667 PHE B C   1 
ATOM   4607 O O   . PHE A 1 611 ? 49.268 129.577 -85.929 1.00 63.41  ? 667 PHE B O   1 
ATOM   4608 C CB  . PHE A 1 611 ? 52.070 130.448 -84.622 1.00 45.41  ? 667 PHE B CB  1 
ATOM   4609 C CG  . PHE A 1 611 ? 52.598 130.995 -83.338 1.00 48.03  ? 667 PHE B CG  1 
ATOM   4610 C CD1 . PHE A 1 611 ? 51.903 131.973 -82.656 1.00 49.49  ? 667 PHE B CD1 1 
ATOM   4611 C CD2 . PHE A 1 611 ? 53.766 130.501 -82.786 1.00 58.51  ? 667 PHE B CD2 1 
ATOM   4612 C CE1 . PHE A 1 611 ? 52.373 132.471 -81.456 1.00 53.04  ? 667 PHE B CE1 1 
ATOM   4613 C CE2 . PHE A 1 611 ? 54.247 130.994 -81.586 1.00 63.20  ? 667 PHE B CE2 1 
ATOM   4614 C CZ  . PHE A 1 611 ? 53.548 131.981 -80.920 1.00 60.82  ? 667 PHE B CZ  1 
ATOM   4615 N N   . ARG A 1 612 ? 50.752 127.975 -86.441 1.00 51.39  ? 668 ARG B N   1 
ATOM   4616 C CA  . ARG A 1 612 ? 49.971 127.492 -87.570 1.00 53.06  ? 668 ARG B CA  1 
ATOM   4617 C C   . ARG A 1 612 ? 48.688 126.821 -87.075 1.00 59.27  ? 668 ARG B C   1 
ATOM   4618 O O   . ARG A 1 612 ? 47.664 126.828 -87.763 1.00 62.35  ? 668 ARG B O   1 
ATOM   4619 C CB  . ARG A 1 612 ? 50.796 126.517 -88.407 1.00 60.19  ? 668 ARG B CB  1 
ATOM   4620 C CG  . ARG A 1 612 ? 50.076 125.973 -89.646 1.00 66.69  ? 668 ARG B CG  1 
ATOM   4621 C CD  . ARG A 1 612 ? 49.891 127.034 -90.729 1.00 66.54  ? 668 ARG B CD  1 
ATOM   4622 N NE  . ARG A 1 612 ? 49.525 126.431 -92.008 1.00 68.96  ? 668 ARG B NE  1 
ATOM   4623 C CZ  . ARG A 1 612 ? 48.279 126.319 -92.462 1.00 70.28  ? 668 ARG B CZ  1 
ATOM   4624 N NH1 . ARG A 1 612 ? 47.259 126.778 -91.744 1.00 68.44  ? 668 ARG B NH1 1 
ATOM   4625 N NH2 . ARG A 1 612 ? 48.056 125.752 -93.641 1.00 69.95  ? 668 ARG B NH2 1 
ATOM   4626 N N   . ARG A 1 613 ? 48.746 126.248 -85.874 1.00 61.18  ? 669 ARG B N   1 
ATOM   4627 C CA  . ARG A 1 613 ? 47.569 125.634 -85.262 1.00 61.12  ? 669 ARG B CA  1 
ATOM   4628 C C   . ARG A 1 613 ? 46.418 126.631 -85.041 1.00 56.36  ? 669 ARG B C   1 
ATOM   4629 O O   . ARG A 1 613 ? 45.249 126.256 -85.157 1.00 60.24  ? 669 ARG B O   1 
ATOM   4630 C CB  . ARG A 1 613 ? 47.951 124.929 -83.946 1.00 68.29  ? 669 ARG B CB  1 
ATOM   4631 C CG  . ARG A 1 613 ? 46.830 124.841 -82.893 1.00 72.71  ? 669 ARG B CG  1 
ATOM   4632 C CD  . ARG A 1 613 ? 47.380 124.491 -81.506 1.00 74.39  ? 669 ARG B CD  1 
ATOM   4633 N NE  . ARG A 1 613 ? 46.379 124.621 -80.442 1.00 74.25  ? 669 ARG B NE  1 
ATOM   4634 C CZ  . ARG A 1 613 ? 46.085 125.763 -79.817 1.00 71.57  ? 669 ARG B CZ  1 
ATOM   4635 N NH1 . ARG A 1 613 ? 45.168 125.790 -78.859 1.00 65.01  ? 669 ARG B NH1 1 
ATOM   4636 N NH2 . ARG A 1 613 ? 46.701 126.886 -80.151 1.00 74.81  ? 669 ARG B NH2 1 
ATOM   4637 N N   . LEU A 1 614 ? 46.740 127.892 -84.739 1.00 45.15  ? 670 LEU B N   1 
ATOM   4638 C CA  . LEU A 1 614 ? 45.709 128.885 -84.392 1.00 34.43  ? 670 LEU B CA  1 
ATOM   4639 C C   . LEU A 1 614 ? 44.669 129.082 -85.488 1.00 31.21  ? 670 LEU B C   1 
ATOM   4640 O O   . LEU A 1 614 ? 45.015 129.366 -86.641 1.00 38.68  ? 670 LEU B O   1 
ATOM   4641 C CB  . LEU A 1 614 ? 46.315 130.249 -84.054 1.00 27.00  ? 670 LEU B CB  1 
ATOM   4642 C CG  . LEU A 1 614 ? 47.293 130.385 -82.901 1.00 27.77  ? 670 LEU B CG  1 
ATOM   4643 C CD1 . LEU A 1 614 ? 47.653 131.847 -82.709 1.00 27.51  ? 670 LEU B CD1 1 
ATOM   4644 C CD2 . LEU A 1 614 ? 46.702 129.795 -81.637 1.00 24.62  ? 670 LEU B CD2 1 
ATOM   4645 N N   . PRO A 1 615 ? 43.388 128.977 -85.115 1.00 24.73  ? 671 PRO B N   1 
ATOM   4646 C CA  . PRO A 1 615 ? 42.278 129.110 -86.066 1.00 23.35  ? 671 PRO B CA  1 
ATOM   4647 C C   . PRO A 1 615 ? 42.281 130.457 -86.785 1.00 28.22  ? 671 PRO B C   1 
ATOM   4648 O O   . PRO A 1 615 ? 42.489 131.505 -86.182 1.00 29.68  ? 671 PRO B O   1 
ATOM   4649 C CB  . PRO A 1 615 ? 41.021 128.945 -85.194 1.00 24.21  ? 671 PRO B CB  1 
ATOM   4650 C CG  . PRO A 1 615 ? 41.471 129.160 -83.774 1.00 23.93  ? 671 PRO B CG  1 
ATOM   4651 C CD  . PRO A 1 615 ? 42.941 128.880 -83.708 1.00 28.22  ? 671 PRO B CD  1 
ATOM   4652 N N   . LEU A 1 616 ? 42.063 130.410 -88.092 1.00 37.23  ? 672 LEU B N   1 
ATOM   4653 C CA  . LEU A 1 616 ? 42.078 131.603 -88.921 1.00 31.37  ? 672 LEU B CA  1 
ATOM   4654 C C   . LEU A 1 616 ? 41.034 132.608 -88.446 1.00 27.54  ? 672 LEU B C   1 
ATOM   4655 O O   . LEU A 1 616 ? 41.204 133.821 -88.600 1.00 33.70  ? 672 LEU B O   1 
ATOM   4656 C CB  . LEU A 1 616 ? 41.852 131.228 -90.391 1.00 22.07  ? 672 LEU B CB  1 
ATOM   4657 C CG  . LEU A 1 616 ? 42.186 132.292 -91.443 1.00 23.79  ? 672 LEU B CG  1 
ATOM   4658 C CD1 . LEU A 1 616 ? 43.333 133.225 -91.008 1.00 15.83  ? 672 LEU B CD1 1 
ATOM   4659 C CD2 . LEU A 1 616 ? 42.530 131.620 -92.764 1.00 25.66  ? 672 LEU B CD2 1 
ATOM   4660 N N   . SER A 1 617 ? 39.961 132.098 -87.854 1.00 22.34  ? 673 SER B N   1 
ATOM   4661 C CA  . SER A 1 617 ? 38.914 132.956 -87.311 1.00 30.44  ? 673 SER B CA  1 
ATOM   4662 C C   . SER A 1 617 ? 39.403 133.734 -86.093 1.00 32.07  ? 673 SER B C   1 
ATOM   4663 O O   . SER A 1 617 ? 38.888 134.815 -85.807 1.00 33.16  ? 673 SER B O   1 
ATOM   4664 C CB  . SER A 1 617 ? 37.678 132.133 -86.945 1.00 34.79  ? 673 SER B CB  1 
ATOM   4665 O OG  . SER A 1 617 ? 38.052 130.848 -86.466 1.00 41.40  ? 673 SER B OG  1 
ATOM   4666 N N   . ASP A 1 618 ? 40.381 133.182 -85.372 1.00 28.51  ? 674 ASP B N   1 
ATOM   4667 C CA  . ASP A 1 618 ? 40.992 133.884 -84.240 1.00 26.72  ? 674 ASP B CA  1 
ATOM   4668 C C   . ASP A 1 618 ? 41.830 135.053 -84.745 1.00 27.27  ? 674 ASP B C   1 
ATOM   4669 O O   . ASP A 1 618 ? 41.827 136.123 -84.144 1.00 29.85  ? 674 ASP B O   1 
ATOM   4670 C CB  . ASP A 1 618 ? 41.856 132.942 -83.400 1.00 33.28  ? 674 ASP B CB  1 
ATOM   4671 C CG  . ASP A 1 618 ? 41.048 132.146 -82.384 1.00 43.27  ? 674 ASP B CG  1 
ATOM   4672 O OD1 . ASP A 1 618 ? 39.802 132.168 -82.467 1.00 44.70  ? 674 ASP B OD1 1 
ATOM   4673 O OD2 . ASP A 1 618 ? 41.660 131.497 -81.500 1.00 47.84  ? 674 ASP B OD2 1 
ATOM   4674 N N   . LEU A 1 619 ? 42.540 134.842 -85.853 1.00 25.59  ? 675 LEU B N   1 
ATOM   4675 C CA  . LEU A 1 619 ? 43.269 135.921 -86.522 1.00 29.40  ? 675 LEU B CA  1 
ATOM   4676 C C   . LEU A 1 619 ? 42.332 136.984 -87.112 1.00 26.55  ? 675 LEU B C   1 
ATOM   4677 O O   . LEU A 1 619 ? 42.683 138.156 -87.179 1.00 30.19  ? 675 LEU B O   1 
ATOM   4678 C CB  . LEU A 1 619 ? 44.160 135.372 -87.643 1.00 30.14  ? 675 LEU B CB  1 
ATOM   4679 C CG  . LEU A 1 619 ? 45.142 134.254 -87.289 1.00 32.07  ? 675 LEU B CG  1 
ATOM   4680 C CD1 . LEU A 1 619 ? 45.994 133.864 -88.495 1.00 16.39  ? 675 LEU B CD1 1 
ATOM   4681 C CD2 . LEU A 1 619 ? 46.002 134.698 -86.150 1.00 16.13  ? 675 LEU B CD2 1 
ATOM   4682 N N   . ALA A 1 620 ? 41.142 136.577 -87.539 1.00 23.61  ? 676 ALA B N   1 
ATOM   4683 C CA  . ALA A 1 620 ? 40.229 137.492 -88.236 1.00 19.73  ? 676 ALA B CA  1 
ATOM   4684 C C   . ALA A 1 620 ? 39.565 138.538 -87.327 1.00 19.20  ? 676 ALA B C   1 
ATOM   4685 O O   . ALA A 1 620 ? 39.071 139.570 -87.804 1.00 16.63  ? 676 ALA B O   1 
ATOM   4686 C CB  . ALA A 1 620 ? 39.177 136.701 -89.000 1.00 13.42  ? 676 ALA B CB  1 
ATOM   4687 N N   . SER A 1 621 ? 39.556 138.271 -86.023 1.00 18.65  ? 677 SER B N   1 
ATOM   4688 C CA  . SER A 1 621 ? 39.021 139.213 -85.037 1.00 14.73  ? 677 SER B CA  1 
ATOM   4689 C C   . SER A 1 621 ? 40.063 140.206 -84.499 1.00 19.88  ? 677 SER B C   1 
ATOM   4690 O O   . SER A 1 621 ? 39.792 140.927 -83.539 1.00 26.88  ? 677 SER B O   1 
ATOM   4691 C CB  . SER A 1 621 ? 38.359 138.468 -83.877 1.00 18.16  ? 677 SER B CB  1 
ATOM   4692 O OG  . SER A 1 621 ? 39.258 137.544 -83.286 1.00 27.51  ? 677 SER B OG  1 
ATOM   4693 N N   . ASN A 1 622 ? 41.264 140.198 -85.072 1.00 14.85  ? 678 ASN B N   1 
ATOM   4694 C CA  . ASN A 1 622 ? 42.293 141.163 -84.708 1.00 15.68  ? 678 ASN B CA  1 
ATOM   4695 C C   . ASN A 1 622 ? 42.530 142.279 -85.731 1.00 17.98  ? 678 ASN B C   1 
ATOM   4696 O O   . ASN A 1 622 ? 41.784 142.426 -86.688 1.00 20.76  ? 678 ASN B O   1 
ATOM   4697 C CB  . ASN A 1 622 ? 43.585 140.456 -84.335 1.00 26.50  ? 678 ASN B CB  1 
ATOM   4698 C CG  . ASN A 1 622 ? 43.517 139.846 -82.951 1.00 36.41  ? 678 ASN B CG  1 
ATOM   4699 O OD1 . ASN A 1 622 ? 43.931 140.465 -81.969 1.00 37.92  ? 678 ASN B OD1 1 
ATOM   4700 N ND2 . ASN A 1 622 ? 42.969 138.636 -82.860 1.00 33.97  ? 678 ASN B ND2 1 
ATOM   4701 N N   . ARG A 1 623 ? 43.548 143.094 -85.503 1.00 17.16  ? 679 ARG B N   1 
ATOM   4702 C CA  . ARG A 1 623 ? 43.813 144.214 -86.394 1.00 26.38  ? 679 ARG B CA  1 
ATOM   4703 C C   . ARG A 1 623 ? 44.626 143.851 -87.640 1.00 24.12  ? 679 ARG B C   1 
ATOM   4704 O O   . ARG A 1 623 ? 44.212 144.136 -88.752 1.00 32.31  ? 679 ARG B O   1 
ATOM   4705 C CB  . ARG A 1 623 ? 44.510 145.342 -85.630 1.00 36.24  ? 679 ARG B CB  1 
ATOM   4706 C CG  . ARG A 1 623 ? 44.794 146.556 -86.481 1.00 39.00  ? 679 ARG B CG  1 
ATOM   4707 C CD  . ARG A 1 623 ? 45.530 147.601 -85.691 1.00 43.94  ? 679 ARG B CD  1 
ATOM   4708 N NE  . ARG A 1 623 ? 44.704 148.147 -84.623 1.00 51.89  ? 679 ARG B NE  1 
ATOM   4709 C CZ  . ARG A 1 623 ? 45.160 148.976 -83.693 1.00 59.27  ? 679 ARG B CZ  1 
ATOM   4710 N NH1 . ARG A 1 623 ? 46.441 149.345 -83.701 1.00 58.96  ? 679 ARG B NH1 1 
ATOM   4711 N NH2 . ARG A 1 623 ? 44.341 149.429 -82.751 1.00 62.56  ? 679 ARG B NH2 1 
ATOM   4712 N N   . GLY A 1 624 ? 45.852 143.396 -87.424 1.00 22.88  ? 680 GLY B N   1 
ATOM   4713 C CA  . GLY A 1 624 ? 46.768 142.912 -88.454 1.00 25.87  ? 680 GLY B CA  1 
ATOM   4714 C C   . GLY A 1 624 ? 47.402 141.518 -88.457 1.00 19.40  ? 680 GLY B C   1 
ATOM   4715 O O   . GLY A 1 624 ? 48.515 141.419 -88.965 1.00 20.16  ? 680 GLY B O   1 
ATOM   4716 N N   . LEU A 1 625 ? 46.861 140.516 -87.768 1.00 18.62  ? 681 LEU B N   1 
ATOM   4717 C CA  . LEU A 1 625 ? 47.576 139.231 -87.613 1.00 18.64  ? 681 LEU B CA  1 
ATOM   4718 C C   . LEU A 1 625 ? 47.589 138.321 -88.853 1.00 18.63  ? 681 LEU B C   1 
ATOM   4719 O O   . LEU A 1 625 ? 46.553 138.102 -89.474 1.00 18.05  ? 681 LEU B O   1 
ATOM   4720 C CB  . LEU A 1 625 ? 47.017 138.426 -86.435 1.00 17.84  ? 681 LEU B CB  1 
ATOM   4721 C CG  . LEU A 1 625 ? 47.162 138.995 -85.026 1.00 26.72  ? 681 LEU B CG  1 
ATOM   4722 C CD1 . LEU A 1 625 ? 46.453 138.094 -84.033 1.00 21.82  ? 681 LEU B CD1 1 
ATOM   4723 C CD2 . LEU A 1 625 ? 48.639 139.175 -84.661 1.00 25.78  ? 681 LEU B CD2 1 
ATOM   4724 N N   . TYR A 1 626 ? 48.758 137.778 -89.204 1.00 19.28  ? 682 TYR B N   1 
ATOM   4725 C CA  . TYR A 1 626 ? 48.804 136.826 -90.328 1.00 31.20  ? 682 TYR B CA  1 
ATOM   4726 C C   . TYR A 1 626 ? 49.996 135.895 -90.210 1.00 19.81  ? 682 TYR B C   1 
ATOM   4727 O O   . TYR A 1 626 ? 50.971 136.241 -89.562 1.00 21.57  ? 682 TYR B O   1 
ATOM   4728 C CB  . TYR A 1 626 ? 48.839 137.548 -91.700 1.00 19.83  ? 682 TYR B CB  1 
ATOM   4729 C CG  . TYR A 1 626 ? 50.108 138.333 -91.946 1.00 20.92  ? 682 TYR B CG  1 
ATOM   4730 C CD1 . TYR A 1 626 ? 50.285 139.581 -91.369 1.00 25.92  ? 682 TYR B CD1 1 
ATOM   4731 C CD2 . TYR A 1 626 ? 51.142 137.821 -92.723 1.00 21.66  ? 682 TYR B CD2 1 
ATOM   4732 C CE1 . TYR A 1 626 ? 51.445 140.309 -91.575 1.00 28.52  ? 682 TYR B CE1 1 
ATOM   4733 C CE2 . TYR A 1 626 ? 52.307 138.538 -92.915 1.00 22.68  ? 682 TYR B CE2 1 
ATOM   4734 C CZ  . TYR A 1 626 ? 52.448 139.786 -92.340 1.00 22.98  ? 682 TYR B CZ  1 
ATOM   4735 O OH  . TYR A 1 626 ? 53.585 140.532 -92.498 1.00 24.02  ? 682 TYR B OH  1 
ATOM   4736 N N   . ILE A 1 627 ? 49.928 134.727 -90.849 1.00 25.47  ? 683 ILE B N   1 
ATOM   4737 C CA  . ILE A 1 627 ? 51.092 133.851 -90.922 1.00 26.07  ? 683 ILE B CA  1 
ATOM   4738 C C   . ILE A 1 627 ? 51.995 134.301 -92.066 1.00 29.44  ? 683 ILE B C   1 
ATOM   4739 O O   . ILE A 1 627 ? 51.569 134.364 -93.212 1.00 26.18  ? 683 ILE B O   1 
ATOM   4740 C CB  . ILE A 1 627 ? 50.718 132.365 -91.126 1.00 26.42  ? 683 ILE B CB  1 
ATOM   4741 C CG1 . ILE A 1 627 ? 50.401 131.684 -89.797 1.00 26.02  ? 683 ILE B CG1 1 
ATOM   4742 C CG2 . ILE A 1 627 ? 51.895 131.615 -91.721 1.00 31.14  ? 683 ILE B CG2 1 
ATOM   4743 C CD1 . ILE A 1 627 ? 49.008 131.907 -89.284 1.00 31.10  ? 683 ILE B CD1 1 
ATOM   4744 N N   . SER A 1 628 ? 53.240 134.639 -91.758 1.00 46.99  ? 684 SER B N   1 
ATOM   4745 C CA  . SER A 1 628 ? 54.193 134.932 -92.822 1.00 60.42  ? 684 SER B CA  1 
ATOM   4746 C C   . SER A 1 628 ? 55.012 133.682 -93.084 1.00 66.97  ? 684 SER B C   1 
ATOM   4747 O O   . SER A 1 628 ? 55.464 133.012 -92.153 1.00 66.83  ? 684 SER B O   1 
ATOM   4748 C CB  . SER A 1 628 ? 55.104 136.120 -92.475 1.00 60.09  ? 684 SER B CB  1 
ATOM   4749 O OG  . SER A 1 628 ? 56.173 135.743 -91.621 1.00 52.78  ? 684 SER B OG  1 
ATOM   4750 N N   . ASN A 1 629 ? 55.185 133.354 -94.355 1.00 73.05  ? 685 ASN B N   1 
ATOM   4751 C CA  . ASN A 1 629 ? 55.991 132.199 -94.711 1.00 83.18  ? 685 ASN B CA  1 
ATOM   4752 C C   . ASN A 1 629 ? 57.479 132.574 -94.805 1.00 86.75  ? 685 ASN B C   1 
ATOM   4753 O O   . ASN A 1 629 ? 57.860 133.502 -95.527 1.00 81.31  ? 685 ASN B O   1 
ATOM   4754 C CB  . ASN A 1 629 ? 55.449 131.537 -95.983 1.00 85.49  ? 685 ASN B CB  1 
ATOM   4755 C CG  . ASN A 1 629 ? 54.017 131.024 -95.805 1.00 83.46  ? 685 ASN B CG  1 
ATOM   4756 O OD1 . ASN A 1 629 ? 53.096 131.447 -96.504 1.00 83.86  ? 685 ASN B OD1 1 
ATOM   4757 N ND2 . ASN A 1 629 ? 53.832 130.115 -94.857 1.00 81.80  ? 685 ASN B ND2 1 
ATOM   4758 N N   . ALA A 1 630 ? 58.305 131.848 -94.050 1.00 92.63  ? 686 ALA B N   1 
ATOM   4759 C CA  . ALA A 1 630 ? 59.712 132.204 -93.830 1.00 96.35  ? 686 ALA B CA  1 
ATOM   4760 C C   . ALA A 1 630 ? 60.589 132.122 -95.091 1.00 100.79 ? 686 ALA B C   1 
ATOM   4761 O O   . ALA A 1 630 ? 60.213 131.489 -96.081 1.00 98.62  ? 686 ALA B O   1 
ATOM   4762 C CB  . ALA A 1 630 ? 60.306 131.367 -92.691 1.00 91.16  ? 686 ALA B CB  1 
ATOM   4763 N N   . ASP B 2 1   ? 50.768 89.476  -46.729 1.00 35.87  ? 44  ASP A N   1 
ATOM   4764 C CA  . ASP B 2 1   ? 49.739 88.936  -45.853 1.00 34.89  ? 44  ASP A CA  1 
ATOM   4765 C C   . ASP B 2 1   ? 48.347 89.385  -46.287 1.00 30.32  ? 44  ASP A C   1 
ATOM   4766 O O   . ASP B 2 1   ? 48.146 90.539  -46.678 1.00 32.79  ? 44  ASP A O   1 
ATOM   4767 C CB  . ASP B 2 1   ? 50.011 89.356  -44.413 1.00 40.85  ? 44  ASP A CB  1 
ATOM   4768 C CG  . ASP B 2 1   ? 51.277 88.738  -43.860 1.00 48.32  ? 44  ASP A CG  1 
ATOM   4769 O OD1 . ASP B 2 1   ? 52.161 88.356  -44.667 1.00 51.39  ? 44  ASP A OD1 1 
ATOM   4770 O OD2 . ASP B 2 1   ? 51.384 88.632  -42.619 1.00 50.44  ? 44  ASP A OD2 1 
HETATM 4771 N N   . PTR B 2 2   ? 47.384 88.472  -46.231 1.00 21.06  ? 45  PTR A N   1 
HETATM 4772 C CA  . PTR B 2 2   ? 46.030 88.819  -46.644 1.00 21.62  ? 45  PTR A CA  1 
HETATM 4773 C C   . PTR B 2 2   ? 45.393 89.722  -45.588 1.00 24.54  ? 45  PTR A C   1 
HETATM 4774 O O   . PTR B 2 2   ? 45.789 89.700  -44.417 1.00 12.66  ? 45  PTR A O   1 
HETATM 4775 C CB  . PTR B 2 2   ? 45.165 87.612  -47.044 1.00 18.09  ? 45  PTR A CB  1 
HETATM 4776 C CG  . PTR B 2 2   ? 44.612 86.732  -45.926 1.00 12.48  ? 45  PTR A CG  1 
HETATM 4777 C CD1 . PTR B 2 2   ? 43.331 86.929  -45.413 1.00 14.32  ? 45  PTR A CD1 1 
HETATM 4778 C CD2 . PTR B 2 2   ? 45.339 85.658  -45.442 1.00 15.63  ? 45  PTR A CD2 1 
HETATM 4779 C CE1 . PTR B 2 2   ? 42.817 86.101  -44.420 1.00 14.54  ? 45  PTR A CE1 1 
HETATM 4780 C CE2 . PTR B 2 2   ? 44.831 84.829  -44.453 1.00 15.27  ? 45  PTR A CE2 1 
HETATM 4781 C CZ  . PTR B 2 2   ? 43.573 85.044  -43.949 1.00 12.15  ? 45  PTR A CZ  1 
HETATM 4782 O OH  . PTR B 2 2   ? 43.120 84.244  -43.015 1.00 24.26  ? 45  PTR A OH  1 
HETATM 4783 P P   . PTR B 2 2   ? 42.232 82.928  -43.338 1.00 11.79  ? 45  PTR A P   1 
HETATM 4784 O O1P . PTR B 2 2   ? 41.207 83.195  -44.436 1.00 15.15  ? 45  PTR A O1P 1 
HETATM 4785 O O2P . PTR B 2 2   ? 43.133 81.848  -43.801 1.00 16.28  ? 45  PTR A O2P 1 
HETATM 4786 O O3P . PTR B 2 2   ? 41.493 82.507  -42.060 1.00 17.51  ? 45  PTR A O3P 1 
ATOM   4787 N N   . TRP B 2 3   ? 44.423 90.525  -46.017 1.00 13.83  ? 46  TRP A N   1 
ATOM   4788 C CA  . TRP B 2 3   ? 43.816 91.498  -45.121 1.00 20.22  ? 46  TRP A CA  1 
ATOM   4789 C C   . TRP B 2 3   ? 42.809 90.865  -44.155 1.00 19.80  ? 46  TRP A C   1 
ATOM   4790 O O   . TRP B 2 3   ? 42.074 89.935  -44.510 1.00 18.95  ? 46  TRP A O   1 
ATOM   4791 C CB  . TRP B 2 3   ? 43.151 92.622  -45.919 1.00 22.07  ? 46  TRP A CB  1 
ATOM   4792 C CG  . TRP B 2 3   ? 44.100 93.606  -46.528 1.00 23.35  ? 46  TRP A CG  1 
ATOM   4793 C CD1 . TRP B 2 3   ? 45.455 93.668  -46.350 1.00 30.65  ? 46  TRP A CD1 1 
ATOM   4794 C CD2 . TRP B 2 3   ? 43.763 94.678  -47.416 1.00 28.75  ? 46  TRP A CD2 1 
ATOM   4795 N NE1 . TRP B 2 3   ? 45.983 94.712  -47.078 1.00 32.76  ? 46  TRP A NE1 1 
ATOM   4796 C CE2 . TRP B 2 3   ? 44.963 95.349  -47.740 1.00 33.73  ? 46  TRP A CE2 1 
ATOM   4797 C CE3 . TRP B 2 3   ? 42.561 95.136  -47.972 1.00 33.89  ? 46  TRP A CE3 1 
ATOM   4798 C CZ2 . TRP B 2 3   ? 44.995 96.456  -48.591 1.00 33.05  ? 46  TRP A CZ2 1 
ATOM   4799 C CZ3 . TRP B 2 3   ? 42.594 96.229  -48.824 1.00 40.35  ? 46  TRP A CZ3 1 
ATOM   4800 C CH2 . TRP B 2 3   ? 43.805 96.877  -49.126 1.00 38.22  ? 46  TRP A CH2 1 
ATOM   4801 N N   . ARG B 2 4   ? 42.786 91.379  -42.931 1.00 22.63  ? 47  ARG A N   1 
ATOM   4802 C CA  . ARG B 2 4   ? 41.796 90.986  -41.937 1.00 23.32  ? 47  ARG A CA  1 
ATOM   4803 C C   . ARG B 2 4   ? 40.409 91.427  -42.402 1.00 22.42  ? 47  ARG A C   1 
ATOM   4804 O O   . ARG B 2 4   ? 40.292 92.286  -43.274 1.00 34.98  ? 47  ARG A O   1 
ATOM   4805 C CB  . ARG B 2 4   ? 42.123 91.665  -40.617 1.00 34.17  ? 47  ARG A CB  1 
ATOM   4806 C CG  . ARG B 2 4   ? 42.307 93.173  -40.759 1.00 45.45  ? 47  ARG A CG  1 
ATOM   4807 C CD  . ARG B 2 4   ? 42.755 93.815  -39.459 1.00 58.00  ? 47  ARG A CD  1 
ATOM   4808 N NE  . ARG B 2 4   ? 41.634 94.039  -38.556 1.00 72.46  ? 47  ARG A NE  1 
ATOM   4809 C CZ  . ARG B 2 4   ? 41.673 94.856  -37.509 1.00 85.12  ? 47  ARG A CZ  1 
ATOM   4810 N NH1 . ARG B 2 4   ? 42.782 95.531  -37.235 1.00 88.91  ? 47  ARG A NH1 1 
ATOM   4811 N NH2 . ARG B 2 4   ? 40.601 95.001  -36.737 1.00 88.68  ? 47  ARG A NH2 1 
ATOM   4812 N N   . ALA B 2 5   ? 39.366 90.827  -41.837 1.00 15.95  ? 48  ALA A N   1 
ATOM   4813 C CA  . ALA B 2 5   ? 37.989 91.168  -42.185 1.00 10.55  ? 48  ALA A CA  1 
ATOM   4814 C C   . ALA B 2 5   ? 37.718 92.651  -42.000 1.00 12.86  ? 48  ALA A C   1 
ATOM   4815 O O   . ALA B 2 5   ? 38.101 93.222  -40.982 1.00 18.86  ? 48  ALA A O   1 
ATOM   4816 C CB  . ALA B 2 5   ? 37.007 90.350  -41.370 1.00 7.06   ? 48  ALA A CB  1 
ATOM   4817 N N   . LYS B 2 6   ? 37.060 93.260  -42.992 1.00 14.50  ? 49  LYS A N   1 
ATOM   4818 C CA  . LYS B 2 6   ? 36.717 94.690  -42.973 1.00 14.83  ? 49  LYS A CA  1 
ATOM   4819 C C   . LYS B 2 6   ? 35.295 94.938  -43.446 1.00 8.76   ? 49  LYS A C   1 
ATOM   4820 O O   . LYS B 2 6   ? 34.738 94.148  -44.211 1.00 15.52  ? 49  LYS A O   1 
ATOM   4821 C CB  . LYS B 2 6   ? 37.647 95.476  -43.894 1.00 6.59   ? 49  LYS A CB  1 
ATOM   4822 C CG  . LYS B 2 6   ? 39.075 95.557  -43.445 1.00 21.31  ? 49  LYS A CG  1 
ATOM   4823 C CD  . LYS B 2 6   ? 39.861 96.481  -44.384 1.00 33.80  ? 49  LYS A CD  1 
ATOM   4824 C CE  . LYS B 2 6   ? 41.286 96.706  -43.889 1.00 38.47  ? 49  LYS A CE  1 
ATOM   4825 N NZ  . LYS B 2 6   ? 42.031 95.414  -43.836 1.00 39.09  ? 49  LYS A NZ  1 
ATOM   4826 N N   . HIS B 2 7   ? 34.709 96.050  -43.032 1.00 12.25  ? 50  HIS A N   1 
ATOM   4827 C CA  . HIS B 2 7   ? 33.425 96.439  -43.617 1.00 17.01  ? 50  HIS A CA  1 
ATOM   4828 C C   . HIS B 2 7   ? 33.670 97.232  -44.895 1.00 13.59  ? 50  HIS A C   1 
ATOM   4829 O O   . HIS B 2 7   ? 34.815 97.595  -45.191 1.00 15.49  ? 50  HIS A O   1 
ATOM   4830 C CB  . HIS B 2 7   ? 32.589 97.264  -42.622 1.00 20.23  ? 50  HIS A CB  1 
ATOM   4831 C CG  . HIS B 2 7   ? 33.191 98.590  -42.262 1.00 30.24  ? 50  HIS A CG  1 
ATOM   4832 N ND1 . HIS B 2 7   ? 32.622 99.435  -41.335 1.00 38.58  ? 50  HIS A ND1 1 
ATOM   4833 C CD2 . HIS B 2 7   ? 34.314 99.214  -42.699 1.00 36.66  ? 50  HIS A CD2 1 
ATOM   4834 C CE1 . HIS B 2 7   ? 33.363 100.524 -41.217 1.00 39.26  ? 50  HIS A CE1 1 
ATOM   4835 N NE2 . HIS B 2 7   ? 34.396 100.415 -42.031 1.00 39.79  ? 50  HIS A NE2 1 
ATOM   4836 N N   . HIS B 2 8   ? 32.594 97.536  -45.623 1.00 11.91  ? 51  HIS A N   1 
ATOM   4837 C CA  . HIS B 2 8   ? 32.652 98.401  -46.800 1.00 10.88  ? 51  HIS A CA  1 
ATOM   4838 C C   . HIS B 2 8   ? 33.097 99.786  -46.341 1.00 15.51  ? 51  HIS A C   1 
ATOM   4839 O O   . HIS B 2 8   ? 32.547 100.321 -45.382 1.00 18.15  ? 51  HIS A O   1 
ATOM   4840 C CB  . HIS B 2 8   ? 31.263 98.492  -47.424 1.00 8.73   ? 51  HIS A CB  1 
ATOM   4841 C CG  . HIS B 2 8   ? 31.135 99.521  -48.503 1.00 13.73  ? 51  HIS A CG  1 
ATOM   4842 N ND1 . HIS B 2 8   ? 30.660 100.798 -48.267 1.00 14.37  ? 51  HIS A ND1 1 
ATOM   4843 C CD2 . HIS B 2 8   ? 31.381 99.456  -49.836 1.00 12.17  ? 51  HIS A CD2 1 
ATOM   4844 C CE1 . HIS B 2 8   ? 30.636 101.474 -49.401 1.00 8.72   ? 51  HIS A CE1 1 
ATOM   4845 N NE2 . HIS B 2 8   ? 31.069 100.687 -50.368 1.00 15.75  ? 51  HIS A NE2 1 
ATOM   4846 N N   . PRO B 2 9   ? 34.106 100.365 -47.008 1.00 14.21  ? 52  PRO A N   1 
ATOM   4847 C CA  . PRO B 2 9   ? 34.587 101.695 -46.618 1.00 20.28  ? 52  PRO A CA  1 
ATOM   4848 C C   . PRO B 2 9   ? 33.500 102.737 -46.857 1.00 26.53  ? 52  PRO A C   1 
ATOM   4849 O O   . PRO B 2 9   ? 32.824 102.679 -47.881 1.00 23.24  ? 52  PRO A O   1 
ATOM   4850 C CB  . PRO B 2 9   ? 35.762 101.946 -47.582 1.00 10.13  ? 52  PRO A CB  1 
ATOM   4851 C CG  . PRO B 2 9   ? 36.112 100.616 -48.139 1.00 5.15   ? 52  PRO A CG  1 
ATOM   4852 C CD  . PRO B 2 9   ? 34.818 99.858  -48.189 1.00 14.02  ? 52  PRO A CD  1 
HETATM 4853 N N   . HZP B 2 10  ? 33.322 103.666 -45.925 1.00 28.02  ? 53  HZP A N   1 
HETATM 4854 C CA  . HZP B 2 10  ? 32.309 104.689 -46.100 1.00 21.36  ? 53  HZP A CA  1 
HETATM 4855 C C   . HZP B 2 10  ? 32.835 105.801 -46.990 1.00 19.10  ? 53  HZP A C   1 
HETATM 4856 O O   . HZP B 2 10  ? 34.013 106.133 -46.961 1.00 20.69  ? 53  HZP A O   1 
HETATM 4857 C CB  . HZP B 2 10  ? 31.968 105.167 -44.700 1.00 22.58  ? 53  HZP A CB  1 
HETATM 4858 C CG  . HZP B 2 10  ? 32.458 104.058 -43.789 1.00 32.35  ? 53  HZP A CG  1 
HETATM 4859 C CD  . HZP B 2 10  ? 33.617 103.382 -44.510 1.00 24.91  ? 53  HZP A CD  1 
HETATM 4860 O OD1 . HZP B 2 10  ? 32.869 104.587 -42.549 1.00 48.94  ? 53  HZP A OD1 1 
ATOM   4861 N N   . LYS B 2 11  ? 31.948 106.350 -47.804 1.00 17.03  ? 54  LYS A N   1 
ATOM   4862 C CA  . LYS B 2 11  ? 32.306 107.381 -48.758 1.00 15.29  ? 54  LYS A CA  1 
ATOM   4863 C C   . LYS B 2 11  ? 31.411 108.574 -48.441 1.00 18.05  ? 54  LYS A C   1 
ATOM   4864 O O   . LYS B 2 11  ? 30.191 108.439 -48.296 1.00 15.98  ? 54  LYS A O   1 
ATOM   4865 C CB  . LYS B 2 11  ? 32.093 106.849 -50.189 1.00 17.68  ? 54  LYS A CB  1 
ATOM   4866 C CG  . LYS B 2 11  ? 32.415 107.805 -51.365 1.00 22.97  ? 54  LYS A CG  1 
ATOM   4867 C CD  . LYS B 2 11  ? 32.241 107.135 -52.766 1.00 48.32  ? 54  LYS A CD  1 
ATOM   4868 C CE  . LYS B 2 11  ? 30.765 106.799 -53.092 1.00 54.70  ? 54  LYS A CE  1 
ATOM   4869 N NZ  . LYS B 2 11  ? 30.460 106.398 -54.519 1.00 48.17  ? 54  LYS A NZ  1 
ATOM   4870 N N   . ASN B 2 12  ? 32.013 109.747 -48.316 1.00 19.00  ? 55  ASN A N   1 
ATOM   4871 C CA  . ASN B 2 12  ? 31.232 110.956 -48.113 1.00 19.11  ? 55  ASN A CA  1 
ATOM   4872 C C   . ASN B 2 12  ? 31.599 111.973 -49.188 1.00 13.05  ? 55  ASN A C   1 
ATOM   4873 O O   . ASN B 2 12  ? 32.539 111.770 -49.934 1.00 10.80  ? 55  ASN A O   1 
ATOM   4874 C CB  . ASN B 2 12  ? 31.381 111.517 -46.678 1.00 20.41  ? 55  ASN A CB  1 
ATOM   4875 C CG  . ASN B 2 12  ? 32.782 112.054 -46.383 1.00 17.57  ? 55  ASN A CG  1 
ATOM   4876 O OD1 . ASN B 2 12  ? 33.507 111.493 -45.560 1.00 15.78  ? 55  ASN A OD1 1 
ATOM   4877 N ND2 . ASN B 2 12  ? 33.162 113.157 -47.049 1.00 9.86   ? 55  ASN A ND2 1 
ATOM   4878 N N   . ASN B 2 13  ? 30.834 113.047 -49.291 1.00 18.42  ? 56  ASN A N   1 
ATOM   4879 C CA  . ASN B 2 13  ? 31.082 114.050 -50.321 1.00 20.25  ? 56  ASN A CA  1 
ATOM   4880 C C   . ASN B 2 13  ? 32.113 115.090 -49.915 1.00 22.62  ? 56  ASN A C   1 
ATOM   4881 O O   . ASN B 2 13  ? 32.655 115.029 -48.805 1.00 19.96  ? 56  ASN A O   1 
ATOM   4882 C CB  . ASN B 2 13  ? 29.767 114.710 -50.736 1.00 19.85  ? 56  ASN A CB  1 
ATOM   4883 C CG  . ASN B 2 13  ? 28.866 113.747 -51.481 1.00 19.00  ? 56  ASN A CG  1 
ATOM   4884 O OD1 . ASN B 2 13  ? 29.014 113.565 -52.683 1.00 22.35  ? 56  ASN A OD1 1 
ATOM   4885 N ND2 . ASN B 2 13  ? 27.969 113.085 -50.762 1.00 17.26  ? 56  ASN A ND2 1 
ATOM   4886 O OXT . ASN B 2 13  ? 32.433 115.989 -50.700 1.00 23.86  ? 56  ASN A OXT 1 
HETATM 4887 C C1  . NAG C 3 .   ? 25.196 129.013 -29.367 1.00 17.83  ? 701 NAG B C1  1 
HETATM 4888 C C2  . NAG C 3 .   ? 23.901 128.324 -28.929 1.00 22.94  ? 701 NAG B C2  1 
HETATM 4889 C C3  . NAG C 3 .   ? 22.960 129.418 -28.439 1.00 26.29  ? 701 NAG B C3  1 
HETATM 4890 C C4  . NAG C 3 .   ? 23.598 130.188 -27.290 1.00 27.64  ? 701 NAG B C4  1 
HETATM 4891 C C5  . NAG C 3 .   ? 24.887 130.808 -27.815 1.00 24.91  ? 701 NAG B C5  1 
HETATM 4892 C C6  . NAG C 3 .   ? 25.622 131.756 -26.842 1.00 24.55  ? 701 NAG B C6  1 
HETATM 4893 C C7  . NAG C 3 .   ? 23.054 126.319 -30.162 1.00 22.39  ? 701 NAG B C7  1 
HETATM 4894 C C8  . NAG C 3 .   ? 22.404 125.892 -31.446 1.00 21.55  ? 701 NAG B C8  1 
HETATM 4895 N N2  . NAG C 3 .   ? 23.274 127.633 -30.043 1.00 24.76  ? 701 NAG B N2  1 
HETATM 4896 O O3  . NAG C 3 .   ? 21.678 128.905 -28.124 1.00 27.23  ? 701 NAG B O3  1 
HETATM 4897 O O4  . NAG C 3 .   ? 22.718 131.215 -26.925 1.00 30.85  ? 701 NAG B O4  1 
HETATM 4898 O O5  . NAG C 3 .   ? 25.720 129.776 -28.293 1.00 22.00  ? 701 NAG B O5  1 
HETATM 4899 O O6  . NAG C 3 .   ? 25.994 131.197 -25.599 1.00 25.43  ? 701 NAG B O6  1 
HETATM 4900 O O7  . NAG C 3 .   ? 23.342 125.469 -29.323 1.00 18.52  ? 701 NAG B O7  1 
HETATM 4901 C C1  . NAG D 3 .   ? 22.127 131.446 -25.626 1.00 30.59  ? 702 NAG B C1  1 
HETATM 4902 C C2  . NAG D 3 .   ? 21.557 132.851 -25.437 1.00 31.95  ? 702 NAG B C2  1 
HETATM 4903 C C3  . NAG D 3 .   ? 21.067 133.081 -24.013 1.00 36.91  ? 702 NAG B C3  1 
HETATM 4904 C C4  . NAG D 3 .   ? 20.282 131.899 -23.450 1.00 39.50  ? 702 NAG B C4  1 
HETATM 4905 C C5  . NAG D 3 .   ? 20.972 130.560 -23.737 1.00 38.54  ? 702 NAG B C5  1 
HETATM 4906 C C6  . NAG D 3 .   ? 20.070 129.400 -23.337 1.00 35.55  ? 702 NAG B C6  1 
HETATM 4907 C C7  . NAG D 3 .   ? 22.750 134.489 -26.860 1.00 33.34  ? 702 NAG B C7  1 
HETATM 4908 C C8  . NAG D 3 .   ? 23.899 135.459 -26.894 1.00 27.02  ? 702 NAG B C8  1 
HETATM 4909 N N2  . NAG D 3 .   ? 22.588 133.838 -25.701 1.00 33.41  ? 702 NAG B N2  1 
HETATM 4910 O O3  . NAG D 3 .   ? 20.253 134.229 -24.010 1.00 38.43  ? 702 NAG B O3  1 
HETATM 4911 O O4  . NAG D 3 .   ? 20.118 132.075 -22.053 1.00 47.05  ? 702 NAG B O4  1 
HETATM 4912 O O5  . NAG D 3 .   ? 21.319 130.404 -25.108 1.00 36.19  ? 702 NAG B O5  1 
HETATM 4913 O O6  . NAG D 3 .   ? 20.676 128.207 -23.769 1.00 35.49  ? 702 NAG B O6  1 
HETATM 4914 O O7  . NAG D 3 .   ? 22.037 134.335 -27.860 1.00 30.62  ? 702 NAG B O7  1 
HETATM 4915 C C1  . NAG E 3 .   ? 38.227 132.417 -69.722 1.00 11.43  ? 703 NAG B C1  1 
HETATM 4916 C C2  . NAG E 3 .   ? 37.722 131.038 -70.166 1.00 13.07  ? 703 NAG B C2  1 
HETATM 4917 C C3  . NAG E 3 .   ? 36.423 131.106 -70.982 1.00 15.32  ? 703 NAG B C3  1 
HETATM 4918 C C4  . NAG E 3 .   ? 35.392 131.966 -70.250 1.00 18.05  ? 703 NAG B C4  1 
HETATM 4919 C C5  . NAG E 3 .   ? 36.038 133.333 -70.049 1.00 15.68  ? 703 NAG B C5  1 
HETATM 4920 C C6  . NAG E 3 .   ? 35.087 134.355 -69.441 1.00 14.56  ? 703 NAG B C6  1 
HETATM 4921 C C7  . NAG E 3 .   ? 39.115 129.057 -70.684 1.00 21.21  ? 703 NAG B C7  1 
HETATM 4922 C C8  . NAG E 3 .   ? 40.366 128.561 -71.350 1.00 9.46   ? 703 NAG B C8  1 
HETATM 4923 N N2  . NAG E 3 .   ? 38.781 130.335 -70.883 1.00 9.05   ? 703 NAG B N2  1 
HETATM 4924 O O3  . NAG E 3 .   ? 35.941 129.794 -71.151 1.00 22.16  ? 703 NAG B O3  1 
HETATM 4925 O O4  . NAG E 3 .   ? 34.083 132.017 -70.834 1.00 7.27   ? 703 NAG B O4  1 
HETATM 4926 O O5  . NAG E 3 .   ? 37.160 133.180 -69.193 1.00 12.04  ? 703 NAG B O5  1 
HETATM 4927 O O6  . NAG E 3 .   ? 34.576 133.835 -68.237 1.00 19.88  ? 703 NAG B O6  1 
HETATM 4928 O O7  . NAG E 3 .   ? 38.458 128.281 -70.000 1.00 29.13  ? 703 NAG B O7  1 
HETATM 4929 C C1  . NAG F 3 .   ? 39.341 130.757 -76.000 1.00 9.83   ? 704 NAG B C1  1 
HETATM 4930 C C2  . NAG F 3 .   ? 37.956 130.594 -75.337 1.00 20.39  ? 704 NAG B C2  1 
HETATM 4931 C C3  . NAG F 3 .   ? 37.878 129.371 -74.403 1.00 20.54  ? 704 NAG B C3  1 
HETATM 4932 C C4  . NAG F 3 .   ? 38.387 128.105 -75.084 1.00 25.33  ? 704 NAG B C4  1 
HETATM 4933 C C5  . NAG F 3 .   ? 39.778 128.404 -75.673 1.00 24.13  ? 704 NAG B C5  1 
HETATM 4934 C C6  . NAG F 3 .   ? 40.343 127.220 -76.443 1.00 22.18  ? 704 NAG B C6  1 
HETATM 4935 C C7  . NAG F 3 .   ? 36.525 132.575 -74.864 1.00 18.14  ? 704 NAG B C7  1 
HETATM 4936 C C8  . NAG F 3 .   ? 36.470 133.880 -74.128 1.00 10.70  ? 704 NAG B C8  1 
HETATM 4937 N N2  . NAG F 3 .   ? 37.581 131.796 -74.599 1.00 18.63  ? 704 NAG B N2  1 
HETATM 4938 O O3  . NAG F 3 .   ? 36.537 129.152 -74.032 1.00 19.46  ? 704 NAG B O3  1 
HETATM 4939 O O4  . NAG F 3 .   ? 38.309 126.969 -74.214 1.00 21.27  ? 704 NAG B O4  1 
HETATM 4940 O O5  . NAG F 3 .   ? 39.738 129.518 -76.565 1.00 11.55  ? 704 NAG B O5  1 
HETATM 4941 O O6  . NAG F 3 .   ? 39.543 127.004 -77.590 1.00 26.18  ? 704 NAG B O6  1 
HETATM 4942 O O7  . NAG F 3 .   ? 35.622 132.294 -75.654 1.00 27.34  ? 704 NAG B O7  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   CYS 1   61  61  CYS CYS B . n 
A 1 2   ASN 2   62  62  ASN ASN B . n 
A 1 3   TRP 3   63  63  TRP TRP B . n 
A 1 4   THR 4   64  64  THR THR B . n 
A 1 5   GLY 5   65  65  GLY GLY B . n 
A 1 6   VAL 6   66  66  VAL VAL B . n 
A 1 7   LYS 7   67  67  LYS LYS B . n 
A 1 8   CYS 8   68  68  CYS CYS B . n 
A 1 9   ASN 9   69  69  ASN ASN B . n 
A 1 10  ARG 10  70  70  ARG ARG B . n 
A 1 11  ARG 11  71  71  ARG ARG B . n 
A 1 12  GLY 12  72  72  GLY GLY B . n 
A 1 13  GLU 13  73  73  GLU GLU B . n 
A 1 14  VAL 14  74  74  VAL VAL B . n 
A 1 15  SER 15  75  75  SER SER B . n 
A 1 16  GLU 16  76  76  GLU GLU B . n 
A 1 17  ILE 17  77  77  ILE ILE B . n 
A 1 18  GLN 18  78  78  GLN GLN B . n 
A 1 19  LEU 19  79  79  LEU LEU B . n 
A 1 20  LYS 20  80  80  LYS LYS B . n 
A 1 21  GLU 21  81  81  GLU GLU B . n 
A 1 22  LYS 22  82  82  LYS LYS B . n 
A 1 23  GLN 23  83  83  GLN GLN B . n 
A 1 24  LEU 24  84  84  LEU LEU B . n 
A 1 25  GLN 25  85  85  GLN GLN B . n 
A 1 26  GLY 26  86  86  GLY GLY B . n 
A 1 27  SER 27  87  87  SER SER B . n 
A 1 28  LEU 28  88  88  LEU LEU B . n 
A 1 29  PRO 29  88  ?   ?   ?   B A n 
A 1 30  VAL 30  88  ?   ?   ?   B B n 
A 1 31  THR 31  88  ?   ?   ?   B C n 
A 1 32  SER 32  88  ?   ?   ?   B D n 
A 1 33  LEU 33  88  ?   ?   ?   B E n 
A 1 34  ARG 34  88  ?   ?   ?   B F n 
A 1 35  SER 35  88  ?   ?   ?   B G n 
A 1 36  LEU 36  92  92  LEU LEU B . n 
A 1 37  LYS 37  93  93  LYS LYS B . n 
A 1 38  SER 38  94  94  SER SER B . n 
A 1 39  LEU 39  95  95  LEU LEU B . n 
A 1 40  THR 40  96  96  THR THR B . n 
A 1 41  SER 41  97  97  SER SER B . n 
A 1 42  LEU 42  98  98  LEU LEU B . n 
A 1 43  THR 43  99  99  THR THR B . n 
A 1 44  LEU 44  100 100 LEU LEU B . n 
A 1 45  SER 45  101 101 SER SER B . n 
A 1 46  SER 46  102 102 SER SER B . n 
A 1 47  LEU 47  103 103 LEU LEU B . n 
A 1 48  GLN 48  104 104 GLN GLN B . n 
A 1 49  LEU 49  105 105 LEU LEU B . n 
A 1 50  THR 50  106 106 THR THR B . n 
A 1 51  GLY 51  107 107 GLY GLY B . n 
A 1 52  VAL 52  108 108 VAL VAL B . n 
A 1 53  ILE 53  109 109 ILE ILE B . n 
A 1 54  PRO 54  110 110 PRO PRO B . n 
A 1 55  LYS 55  111 111 LYS LYS B . n 
A 1 56  GLU 56  112 112 GLU GLU B . n 
A 1 57  ILE 57  113 113 ILE ILE B . n 
A 1 58  GLY 58  114 114 GLY GLY B . n 
A 1 59  ASP 59  115 115 ASP ASP B . n 
A 1 60  PHE 60  116 116 PHE PHE B . n 
A 1 61  THR 61  117 117 THR THR B . n 
A 1 62  GLU 62  118 118 GLU GLU B . n 
A 1 63  LEU 63  119 119 LEU LEU B . n 
A 1 64  GLU 64  120 120 GLU GLU B . n 
A 1 65  LEU 65  121 121 LEU LEU B . n 
A 1 66  LEU 66  122 122 LEU LEU B . n 
A 1 67  ASP 67  123 123 ASP ASP B . n 
A 1 68  LEU 68  124 124 LEU LEU B . n 
A 1 69  SER 69  125 125 SER SER B . n 
A 1 70  ASP 70  126 126 ASP ASP B . n 
A 1 71  ASN 71  127 127 ASN ASN B . n 
A 1 72  SER 72  128 128 SER SER B . n 
A 1 73  LEU 73  129 129 LEU LEU B . n 
A 1 74  SER 74  130 130 SER SER B . n 
A 1 75  GLY 75  131 131 GLY GLY B . n 
A 1 76  ASP 76  132 132 ASP ASP B . n 
A 1 77  ILE 77  133 133 ILE ILE B . n 
A 1 78  PRO 78  134 134 PRO PRO B . n 
A 1 79  VAL 79  135 135 VAL VAL B . n 
A 1 80  GLU 80  136 136 GLU GLU B . n 
A 1 81  ILE 81  137 137 ILE ILE B . n 
A 1 82  PHE 82  138 138 PHE PHE B . n 
A 1 83  ARG 83  139 139 ARG ARG B . n 
A 1 84  LEU 84  140 140 LEU LEU B . n 
A 1 85  LYS 85  141 141 LYS LYS B . n 
A 1 86  LYS 86  142 142 LYS LYS B . n 
A 1 87  LEU 87  143 143 LEU LEU B . n 
A 1 88  LYS 88  144 144 LYS LYS B . n 
A 1 89  THR 89  145 145 THR THR B . n 
A 1 90  LEU 90  146 146 LEU LEU B . n 
A 1 91  SER 91  147 147 SER SER B . n 
A 1 92  LEU 92  148 148 LEU LEU B . n 
A 1 93  ASN 93  149 149 ASN ASN B . n 
A 1 94  THR 94  150 150 THR THR B . n 
A 1 95  ASN 95  151 151 ASN ASN B . n 
A 1 96  ASN 96  152 152 ASN ASN B . n 
A 1 97  LEU 97  153 153 LEU LEU B . n 
A 1 98  GLU 98  154 154 GLU GLU B . n 
A 1 99  GLY 99  155 155 GLY GLY B . n 
A 1 100 HIS 100 156 156 HIS HIS B . n 
A 1 101 ILE 101 157 157 ILE ILE B . n 
A 1 102 PRO 102 158 158 PRO PRO B . n 
A 1 103 MET 103 159 159 MET MET B . n 
A 1 104 GLU 104 160 160 GLU GLU B . n 
A 1 105 ILE 105 161 161 ILE ILE B . n 
A 1 106 GLY 106 162 162 GLY GLY B . n 
A 1 107 ASN 107 163 163 ASN ASN B . n 
A 1 108 LEU 108 164 164 LEU LEU B . n 
A 1 109 SER 109 165 165 SER SER B . n 
A 1 110 GLY 110 166 166 GLY GLY B . n 
A 1 111 LEU 111 167 167 LEU LEU B . n 
A 1 112 VAL 112 168 168 VAL VAL B . n 
A 1 113 GLU 113 169 169 GLU GLU B . n 
A 1 114 LEU 114 170 170 LEU LEU B . n 
A 1 115 MET 115 171 171 MET MET B . n 
A 1 116 LEU 116 172 172 LEU LEU B . n 
A 1 117 PHE 117 173 173 PHE PHE B . n 
A 1 118 ASP 118 174 174 ASP ASP B . n 
A 1 119 ASN 119 175 175 ASN ASN B . n 
A 1 120 LYS 120 176 176 LYS LYS B . n 
A 1 121 LEU 121 177 177 LEU LEU B . n 
A 1 122 SER 122 178 178 SER SER B . n 
A 1 123 GLY 123 179 179 GLY GLY B . n 
A 1 124 GLU 124 180 180 GLU GLU B . n 
A 1 125 ILE 125 181 181 ILE ILE B . n 
A 1 126 PRO 126 182 182 PRO PRO B . n 
A 1 127 ARG 127 183 183 ARG ARG B . n 
A 1 128 SER 128 184 184 SER SER B . n 
A 1 129 ILE 129 185 185 ILE ILE B . n 
A 1 130 GLY 130 186 186 GLY GLY B . n 
A 1 131 GLU 131 187 187 GLU GLU B . n 
A 1 132 LEU 132 188 188 LEU LEU B . n 
A 1 133 LYS 133 189 189 LYS LYS B . n 
A 1 134 ASN 134 190 190 ASN ASN B . n 
A 1 135 LEU 135 191 191 LEU LEU B . n 
A 1 136 GLN 136 192 192 GLN GLN B . n 
A 1 137 VAL 137 193 193 VAL VAL B . n 
A 1 138 LEU 138 194 194 LEU LEU B . n 
A 1 139 ARG 139 195 195 ARG ARG B . n 
A 1 140 ALA 140 196 196 ALA ALA B . n 
A 1 141 GLY 141 197 197 GLY GLY B . n 
A 1 142 GLY 142 198 198 GLY GLY B . n 
A 1 143 ASN 143 199 199 ASN ASN B . n 
A 1 144 LYS 144 200 200 LYS LYS B . n 
A 1 145 ASN 145 201 201 ASN ASN B . n 
A 1 146 LEU 146 202 202 LEU LEU B . n 
A 1 147 ARG 147 203 203 ARG ARG B . n 
A 1 148 GLY 148 204 204 GLY GLY B . n 
A 1 149 GLU 149 205 205 GLU GLU B . n 
A 1 150 LEU 150 206 206 LEU LEU B . n 
A 1 151 PRO 151 207 207 PRO PRO B . n 
A 1 152 TRP 152 208 208 TRP TRP B . n 
A 1 153 GLU 153 209 209 GLU GLU B . n 
A 1 154 ILE 154 210 210 ILE ILE B . n 
A 1 155 GLY 155 211 211 GLY GLY B . n 
A 1 156 ASN 156 212 212 ASN ASN B . n 
A 1 157 CYS 157 213 213 CYS CYS B . n 
A 1 158 GLU 158 214 214 GLU GLU B . n 
A 1 159 ASN 159 215 215 ASN ASN B . n 
A 1 160 LEU 160 216 216 LEU LEU B . n 
A 1 161 VAL 161 217 217 VAL VAL B . n 
A 1 162 MET 162 218 218 MET MET B . n 
A 1 163 LEU 163 219 219 LEU LEU B . n 
A 1 164 GLY 164 220 220 GLY GLY B . n 
A 1 165 LEU 165 221 221 LEU LEU B . n 
A 1 166 ALA 166 222 222 ALA ALA B . n 
A 1 167 GLU 167 223 223 GLU GLU B . n 
A 1 168 THR 168 224 224 THR THR B . n 
A 1 169 SER 169 225 225 SER SER B . n 
A 1 170 LEU 170 226 226 LEU LEU B . n 
A 1 171 SER 171 227 227 SER SER B . n 
A 1 172 GLY 172 228 228 GLY GLY B . n 
A 1 173 LYS 173 229 229 LYS LYS B . n 
A 1 174 LEU 174 230 230 LEU LEU B . n 
A 1 175 PRO 175 231 231 PRO PRO B . n 
A 1 176 ALA 176 232 232 ALA ALA B . n 
A 1 177 SER 177 233 233 SER SER B . n 
A 1 178 ILE 178 234 234 ILE ILE B . n 
A 1 179 GLY 179 235 235 GLY GLY B . n 
A 1 180 ASN 180 236 236 ASN ASN B . n 
A 1 181 LEU 181 237 237 LEU LEU B . n 
A 1 182 LYS 182 238 238 LYS LYS B . n 
A 1 183 ARG 183 239 239 ARG ARG B . n 
A 1 184 VAL 184 240 240 VAL VAL B . n 
A 1 185 GLN 185 241 241 GLN GLN B . n 
A 1 186 THR 186 242 242 THR THR B . n 
A 1 187 ILE 187 243 243 ILE ILE B . n 
A 1 188 ALA 188 244 244 ALA ALA B . n 
A 1 189 ILE 189 245 245 ILE ILE B . n 
A 1 190 TYR 190 246 246 TYR TYR B . n 
A 1 191 THR 191 247 247 THR THR B . n 
A 1 192 SER 192 248 248 SER SER B . n 
A 1 193 LEU 193 249 249 LEU LEU B . n 
A 1 194 LEU 194 250 250 LEU LEU B . n 
A 1 195 SER 195 251 251 SER SER B . n 
A 1 196 GLY 196 252 252 GLY GLY B . n 
A 1 197 PRO 197 253 253 PRO PRO B . n 
A 1 198 ILE 198 254 254 ILE ILE B . n 
A 1 199 PRO 199 255 255 PRO PRO B . n 
A 1 200 ASP 200 256 256 ASP ASP B . n 
A 1 201 GLU 201 257 257 GLU GLU B . n 
A 1 202 ILE 202 258 258 ILE ILE B . n 
A 1 203 GLY 203 259 259 GLY GLY B . n 
A 1 204 TYR 204 260 260 TYR TYR B . n 
A 1 205 CYS 205 261 261 CYS CYS B . n 
A 1 206 THR 206 262 262 THR THR B . n 
A 1 207 GLU 207 263 263 GLU GLU B . n 
A 1 208 LEU 208 264 264 LEU LEU B . n 
A 1 209 GLN 209 265 265 GLN GLN B . n 
A 1 210 ASN 210 266 266 ASN ASN B . n 
A 1 211 LEU 211 267 267 LEU LEU B . n 
A 1 212 TYR 212 268 268 TYR TYR B . n 
A 1 213 LEU 213 269 269 LEU LEU B . n 
A 1 214 TYR 214 270 270 TYR TYR B . n 
A 1 215 GLN 215 271 271 GLN GLN B . n 
A 1 216 ASN 216 272 272 ASN ASN B . n 
A 1 217 SER 217 273 273 SER SER B . n 
A 1 218 ILE 218 274 274 ILE ILE B . n 
A 1 219 SER 219 275 275 SER SER B . n 
A 1 220 GLY 220 276 276 GLY GLY B . n 
A 1 221 SER 221 277 277 SER SER B . n 
A 1 222 ILE 222 278 278 ILE ILE B . n 
A 1 223 PRO 223 279 279 PRO PRO B . n 
A 1 224 THR 224 280 280 THR THR B . n 
A 1 225 THR 225 281 281 THR THR B . n 
A 1 226 ILE 226 282 282 ILE ILE B . n 
A 1 227 GLY 227 283 283 GLY GLY B . n 
A 1 228 GLY 228 284 284 GLY GLY B . n 
A 1 229 LEU 229 285 285 LEU LEU B . n 
A 1 230 LYS 230 286 286 LYS LYS B . n 
A 1 231 LYS 231 287 287 LYS LYS B . n 
A 1 232 LEU 232 288 288 LEU LEU B . n 
A 1 233 GLN 233 289 289 GLN GLN B . n 
A 1 234 SER 234 290 290 SER SER B . n 
A 1 235 LEU 235 291 291 LEU LEU B . n 
A 1 236 LEU 236 292 292 LEU LEU B . n 
A 1 237 LEU 237 293 293 LEU LEU B . n 
A 1 238 TRP 238 294 294 TRP TRP B . n 
A 1 239 GLN 239 295 295 GLN GLN B . n 
A 1 240 ASN 240 296 296 ASN ASN B . n 
A 1 241 ASN 241 297 297 ASN ASN B . n 
A 1 242 LEU 242 298 298 LEU LEU B . n 
A 1 243 VAL 243 299 299 VAL VAL B . n 
A 1 244 GLY 244 300 300 GLY GLY B . n 
A 1 245 LYS 245 301 301 LYS LYS B . n 
A 1 246 ILE 246 302 302 ILE ILE B . n 
A 1 247 PRO 247 303 303 PRO PRO B . n 
A 1 248 THR 248 304 304 THR THR B . n 
A 1 249 GLU 249 305 305 GLU GLU B . n 
A 1 250 LEU 250 306 306 LEU LEU B . n 
A 1 251 GLY 251 307 307 GLY GLY B . n 
A 1 252 ASN 252 308 308 ASN ASN B . n 
A 1 253 CYS 253 309 309 CYS CYS B . n 
A 1 254 PRO 254 310 310 PRO PRO B . n 
A 1 255 GLU 255 311 311 GLU GLU B . n 
A 1 256 LEU 256 312 312 LEU LEU B . n 
A 1 257 TRP 257 313 313 TRP TRP B . n 
A 1 258 LEU 258 314 314 LEU LEU B . n 
A 1 259 ILE 259 315 315 ILE ILE B . n 
A 1 260 ASP 260 316 316 ASP ASP B . n 
A 1 261 PHE 261 317 317 PHE PHE B . n 
A 1 262 SER 262 318 318 SER SER B . n 
A 1 263 GLU 263 319 319 GLU GLU B . n 
A 1 264 ASN 264 320 320 ASN ASN B . n 
A 1 265 LEU 265 321 321 LEU LEU B . n 
A 1 266 LEU 266 322 322 LEU LEU B . n 
A 1 267 THR 267 323 323 THR THR B . n 
A 1 268 GLY 268 324 324 GLY GLY B . n 
A 1 269 THR 269 325 325 THR THR B . n 
A 1 270 ILE 270 326 326 ILE ILE B . n 
A 1 271 PRO 271 327 327 PRO PRO B . n 
A 1 272 ARG 272 328 328 ARG ARG B . n 
A 1 273 SER 273 329 329 SER SER B . n 
A 1 274 PHE 274 330 330 PHE PHE B . n 
A 1 275 GLY 275 331 331 GLY GLY B . n 
A 1 276 LYS 276 332 332 LYS LYS B . n 
A 1 277 LEU 277 333 333 LEU LEU B . n 
A 1 278 GLU 278 334 334 GLU GLU B . n 
A 1 279 ASN 279 335 335 ASN ASN B . n 
A 1 280 LEU 280 336 336 LEU LEU B . n 
A 1 281 GLN 281 337 337 GLN GLN B . n 
A 1 282 GLU 282 338 338 GLU GLU B . n 
A 1 283 LEU 283 339 339 LEU LEU B . n 
A 1 284 GLN 284 340 340 GLN GLN B . n 
A 1 285 LEU 285 341 341 LEU LEU B . n 
A 1 286 SER 286 342 342 SER SER B . n 
A 1 287 VAL 287 343 343 VAL VAL B . n 
A 1 288 ASN 288 344 344 ASN ASN B . n 
A 1 289 GLN 289 345 345 GLN GLN B . n 
A 1 290 ILE 290 346 346 ILE ILE B . n 
A 1 291 SER 291 347 347 SER SER B . n 
A 1 292 GLY 292 348 348 GLY GLY B . n 
A 1 293 THR 293 349 349 THR THR B . n 
A 1 294 ILE 294 350 350 ILE ILE B . n 
A 1 295 PRO 295 351 351 PRO PRO B . n 
A 1 296 GLU 296 352 352 GLU GLU B . n 
A 1 297 GLU 297 353 353 GLU GLU B . n 
A 1 298 LEU 298 354 354 LEU LEU B . n 
A 1 299 THR 299 355 355 THR THR B . n 
A 1 300 ASN 300 356 356 ASN ASN B . n 
A 1 301 CYS 301 357 357 CYS CYS B . n 
A 1 302 THR 302 358 358 THR THR B . n 
A 1 303 LYS 303 359 359 LYS LYS B . n 
A 1 304 LEU 304 360 360 LEU LEU B . n 
A 1 305 THR 305 361 361 THR THR B . n 
A 1 306 HIS 306 362 362 HIS HIS B . n 
A 1 307 LEU 307 363 363 LEU LEU B . n 
A 1 308 GLU 308 364 364 GLU GLU B . n 
A 1 309 ILE 309 365 365 ILE ILE B . n 
A 1 310 ASP 310 366 366 ASP ASP B . n 
A 1 311 ASN 311 367 367 ASN ASN B . n 
A 1 312 ASN 312 368 368 ASN ASN B . n 
A 1 313 LEU 313 369 369 LEU LEU B . n 
A 1 314 ILE 314 370 370 ILE ILE B . n 
A 1 315 THR 315 371 371 THR THR B . n 
A 1 316 GLY 316 372 372 GLY GLY B . n 
A 1 317 GLU 317 373 373 GLU GLU B . n 
A 1 318 ILE 318 374 374 ILE ILE B . n 
A 1 319 PRO 319 375 375 PRO PRO B . n 
A 1 320 SER 320 376 376 SER SER B . n 
A 1 321 LEU 321 377 377 LEU LEU B . n 
A 1 322 MET 322 378 378 MET MET B . n 
A 1 323 SER 323 379 379 SER SER B . n 
A 1 324 ASN 324 380 380 ASN ASN B . n 
A 1 325 LEU 325 381 381 LEU LEU B . n 
A 1 326 ARG 326 382 382 ARG ARG B . n 
A 1 327 SER 327 383 383 SER SER B . n 
A 1 328 LEU 328 384 384 LEU LEU B . n 
A 1 329 THR 329 385 385 THR THR B . n 
A 1 330 MET 330 386 386 MET MET B . n 
A 1 331 PHE 331 387 387 PHE PHE B . n 
A 1 332 PHE 332 388 388 PHE PHE B . n 
A 1 333 ALA 333 389 389 ALA ALA B . n 
A 1 334 TRP 334 390 390 TRP TRP B . n 
A 1 335 GLN 335 391 391 GLN GLN B . n 
A 1 336 ASN 336 392 392 ASN ASN B . n 
A 1 337 LYS 337 393 393 LYS LYS B . n 
A 1 338 LEU 338 394 394 LEU LEU B . n 
A 1 339 THR 339 395 395 THR THR B . n 
A 1 340 GLY 340 396 396 GLY GLY B . n 
A 1 341 ASN 341 397 397 ASN ASN B . n 
A 1 342 ILE 342 398 398 ILE ILE B . n 
A 1 343 PRO 343 399 399 PRO PRO B . n 
A 1 344 GLN 344 400 400 GLN GLN B . n 
A 1 345 SER 345 401 401 SER SER B . n 
A 1 346 LEU 346 402 402 LEU LEU B . n 
A 1 347 SER 347 403 403 SER SER B . n 
A 1 348 GLN 348 404 404 GLN GLN B . n 
A 1 349 CYS 349 405 405 CYS CYS B . n 
A 1 350 ARG 350 406 406 ARG ARG B . n 
A 1 351 GLU 351 407 407 GLU GLU B . n 
A 1 352 LEU 352 408 408 LEU LEU B . n 
A 1 353 GLN 353 409 409 GLN GLN B . n 
A 1 354 ALA 354 410 410 ALA ALA B . n 
A 1 355 ILE 355 411 411 ILE ILE B . n 
A 1 356 ASP 356 412 412 ASP ASP B . n 
A 1 357 LEU 357 413 413 LEU LEU B . n 
A 1 358 SER 358 414 414 SER SER B . n 
A 1 359 TYR 359 415 415 TYR TYR B . n 
A 1 360 ASN 360 416 416 ASN ASN B . n 
A 1 361 SER 361 417 417 SER SER B . n 
A 1 362 LEU 362 418 418 LEU LEU B . n 
A 1 363 SER 363 419 419 SER SER B . n 
A 1 364 GLY 364 420 420 GLY GLY B . n 
A 1 365 SER 365 421 421 SER SER B . n 
A 1 366 ILE 366 422 422 ILE ILE B . n 
A 1 367 PRO 367 423 423 PRO PRO B . n 
A 1 368 LYS 368 424 424 LYS LYS B . n 
A 1 369 GLU 369 425 425 GLU GLU B . n 
A 1 370 ILE 370 426 426 ILE ILE B . n 
A 1 371 PHE 371 427 427 PHE PHE B . n 
A 1 372 GLY 372 428 428 GLY GLY B . n 
A 1 373 LEU 373 429 429 LEU LEU B . n 
A 1 374 ARG 374 430 430 ARG ARG B . n 
A 1 375 ASN 375 431 431 ASN ASN B . n 
A 1 376 LEU 376 432 432 LEU LEU B . n 
A 1 377 THR 377 433 433 THR THR B . n 
A 1 378 LYS 378 434 434 LYS LYS B . n 
A 1 379 LEU 379 435 435 LEU LEU B . n 
A 1 380 LEU 380 436 436 LEU LEU B . n 
A 1 381 LEU 381 437 437 LEU LEU B . n 
A 1 382 LEU 382 438 438 LEU LEU B . n 
A 1 383 SER 383 439 439 SER SER B . n 
A 1 384 ASN 384 440 440 ASN ASN B . n 
A 1 385 ASP 385 441 441 ASP ASP B . n 
A 1 386 LEU 386 442 442 LEU LEU B . n 
A 1 387 SER 387 443 443 SER SER B . n 
A 1 388 GLY 388 444 444 GLY GLY B . n 
A 1 389 PHE 389 445 445 PHE PHE B . n 
A 1 390 ILE 390 446 446 ILE ILE B . n 
A 1 391 PRO 391 447 447 PRO PRO B . n 
A 1 392 PRO 392 448 448 PRO PRO B . n 
A 1 393 ASP 393 449 449 ASP ASP B . n 
A 1 394 ILE 394 450 450 ILE ILE B . n 
A 1 395 GLY 395 451 451 GLY GLY B . n 
A 1 396 ASN 396 452 452 ASN ASN B . n 
A 1 397 CYS 397 453 453 CYS CYS B . n 
A 1 398 THR 398 454 454 THR THR B . n 
A 1 399 ASN 399 455 455 ASN ASN B . n 
A 1 400 LEU 400 456 456 LEU LEU B . n 
A 1 401 TYR 401 457 457 TYR TYR B . n 
A 1 402 ARG 402 458 458 ARG ARG B . n 
A 1 403 LEU 403 459 459 LEU LEU B . n 
A 1 404 ARG 404 460 460 ARG ARG B . n 
A 1 405 LEU 405 461 461 LEU LEU B . n 
A 1 406 ASN 406 462 462 ASN ASN B . n 
A 1 407 GLY 407 463 463 GLY GLY B . n 
A 1 408 ASN 408 464 464 ASN ASN B . n 
A 1 409 ARG 409 465 465 ARG ARG B . n 
A 1 410 LEU 410 466 466 LEU LEU B . n 
A 1 411 ALA 411 467 467 ALA ALA B . n 
A 1 412 GLY 412 468 468 GLY GLY B . n 
A 1 413 SER 413 469 469 SER SER B . n 
A 1 414 ILE 414 470 470 ILE ILE B . n 
A 1 415 PRO 415 471 471 PRO PRO B . n 
A 1 416 SER 416 472 472 SER SER B . n 
A 1 417 GLU 417 473 473 GLU GLU B . n 
A 1 418 ILE 418 474 474 ILE ILE B . n 
A 1 419 GLY 419 475 475 GLY GLY B . n 
A 1 420 ASN 420 476 476 ASN ASN B . n 
A 1 421 LEU 421 477 477 LEU LEU B . n 
A 1 422 LYS 422 478 478 LYS LYS B . n 
A 1 423 ASN 423 479 479 ASN ASN B . n 
A 1 424 LEU 424 480 480 LEU LEU B . n 
A 1 425 ASN 425 481 481 ASN ASN B . n 
A 1 426 PHE 426 482 482 PHE PHE B . n 
A 1 427 VAL 427 483 483 VAL VAL B . n 
A 1 428 ASP 428 484 484 ASP ASP B . n 
A 1 429 ILE 429 485 485 ILE ILE B . n 
A 1 430 SER 430 486 486 SER SER B . n 
A 1 431 GLU 431 487 487 GLU GLU B . n 
A 1 432 ASN 432 488 488 ASN ASN B . n 
A 1 433 ARG 433 489 489 ARG ARG B . n 
A 1 434 LEU 434 490 490 LEU LEU B . n 
A 1 435 VAL 435 491 491 VAL VAL B . n 
A 1 436 GLY 436 492 492 GLY GLY B . n 
A 1 437 SER 437 493 493 SER SER B . n 
A 1 438 ILE 438 494 494 ILE ILE B . n 
A 1 439 PRO 439 495 495 PRO PRO B . n 
A 1 440 PRO 440 496 496 PRO PRO B . n 
A 1 441 ALA 441 497 497 ALA ALA B . n 
A 1 442 ILE 442 498 498 ILE ILE B . n 
A 1 443 SER 443 499 499 SER SER B . n 
A 1 444 GLY 444 500 500 GLY GLY B . n 
A 1 445 CYS 445 501 501 CYS CYS B . n 
A 1 446 GLU 446 502 502 GLU GLU B . n 
A 1 447 SER 447 503 503 SER SER B . n 
A 1 448 LEU 448 504 504 LEU LEU B . n 
A 1 449 GLU 449 505 505 GLU GLU B . n 
A 1 450 PHE 450 506 506 PHE PHE B . n 
A 1 451 LEU 451 507 507 LEU LEU B . n 
A 1 452 ASP 452 508 508 ASP ASP B . n 
A 1 453 LEU 453 509 509 LEU LEU B . n 
A 1 454 HIS 454 510 510 HIS HIS B . n 
A 1 455 THR 455 511 511 THR THR B . n 
A 1 456 ASN 456 512 512 ASN ASN B . n 
A 1 457 SER 457 513 513 SER SER B . n 
A 1 458 LEU 458 514 514 LEU LEU B . n 
A 1 459 SER 459 515 515 SER SER B . n 
A 1 460 GLY 460 516 516 GLY GLY B . n 
A 1 461 SER 461 517 517 SER SER B . n 
A 1 462 LEU 462 518 518 LEU LEU B . n 
A 1 463 LEU 463 519 519 LEU LEU B . n 
A 1 464 GLY 464 520 520 GLY GLY B . n 
A 1 465 THR 465 521 521 THR THR B . n 
A 1 466 THR 466 522 522 THR THR B . n 
A 1 467 LEU 467 523 523 LEU LEU B . n 
A 1 468 PRO 468 524 524 PRO PRO B . n 
A 1 469 LYS 469 525 525 LYS LYS B . n 
A 1 470 SER 470 526 526 SER SER B . n 
A 1 471 LEU 471 527 527 LEU LEU B . n 
A 1 472 LYS 472 528 528 LYS LYS B . n 
A 1 473 PHE 473 529 529 PHE PHE B . n 
A 1 474 ILE 474 530 530 ILE ILE B . n 
A 1 475 ASP 475 531 531 ASP ASP B . n 
A 1 476 PHE 476 532 532 PHE PHE B . n 
A 1 477 SER 477 533 533 SER SER B . n 
A 1 478 ASP 478 534 534 ASP ASP B . n 
A 1 479 ASN 479 535 535 ASN ASN B . n 
A 1 480 ALA 480 536 536 ALA ALA B . n 
A 1 481 LEU 481 537 537 LEU LEU B . n 
A 1 482 SER 482 538 538 SER SER B . n 
A 1 483 SER 483 539 539 SER SER B . n 
A 1 484 THR 484 540 540 THR THR B . n 
A 1 485 LEU 485 541 541 LEU LEU B . n 
A 1 486 PRO 486 542 542 PRO PRO B . n 
A 1 487 PRO 487 543 543 PRO PRO B . n 
A 1 488 GLY 488 544 544 GLY GLY B . n 
A 1 489 ILE 489 545 545 ILE ILE B . n 
A 1 490 GLY 490 546 546 GLY GLY B . n 
A 1 491 LEU 491 547 547 LEU LEU B . n 
A 1 492 LEU 492 548 548 LEU LEU B . n 
A 1 493 THR 493 549 549 THR THR B . n 
A 1 494 GLU 494 550 550 GLU GLU B . n 
A 1 495 LEU 495 551 551 LEU LEU B . n 
A 1 496 THR 496 552 552 THR THR B . n 
A 1 497 LYS 497 553 553 LYS LYS B . n 
A 1 498 LEU 498 554 554 LEU LEU B . n 
A 1 499 ASN 499 555 555 ASN ASN B . n 
A 1 500 LEU 500 556 556 LEU LEU B . n 
A 1 501 ALA 501 557 557 ALA ALA B . n 
A 1 502 LYS 502 558 558 LYS LYS B . n 
A 1 503 ASN 503 559 559 ASN ASN B . n 
A 1 504 ARG 504 560 560 ARG ARG B . n 
A 1 505 LEU 505 561 561 LEU LEU B . n 
A 1 506 SER 506 562 562 SER SER B . n 
A 1 507 GLY 507 563 563 GLY GLY B . n 
A 1 508 GLU 508 564 564 GLU GLU B . n 
A 1 509 ILE 509 565 565 ILE ILE B . n 
A 1 510 PRO 510 566 566 PRO PRO B . n 
A 1 511 ARG 511 567 567 ARG ARG B . n 
A 1 512 GLU 512 568 568 GLU GLU B . n 
A 1 513 ILE 513 569 569 ILE ILE B . n 
A 1 514 SER 514 570 570 SER SER B . n 
A 1 515 THR 515 571 571 THR THR B . n 
A 1 516 CYS 516 572 572 CYS CYS B . n 
A 1 517 ARG 517 573 573 ARG ARG B . n 
A 1 518 SER 518 574 574 SER SER B . n 
A 1 519 LEU 519 575 575 LEU LEU B . n 
A 1 520 GLN 520 576 576 GLN GLN B . n 
A 1 521 LEU 521 577 577 LEU LEU B . n 
A 1 522 LEU 522 578 578 LEU LEU B . n 
A 1 523 ASN 523 579 579 ASN ASN B . n 
A 1 524 LEU 524 580 580 LEU LEU B . n 
A 1 525 GLY 525 581 581 GLY GLY B . n 
A 1 526 GLU 526 582 582 GLU GLU B . n 
A 1 527 ASN 527 583 583 ASN ASN B . n 
A 1 528 ASP 528 584 584 ASP ASP B . n 
A 1 529 PHE 529 585 585 PHE PHE B . n 
A 1 530 SER 530 586 586 SER SER B . n 
A 1 531 GLY 531 587 587 GLY GLY B . n 
A 1 532 GLU 532 588 588 GLU GLU B . n 
A 1 533 ILE 533 589 589 ILE ILE B . n 
A 1 534 PRO 534 590 590 PRO PRO B . n 
A 1 535 ASP 535 591 591 ASP ASP B . n 
A 1 536 GLU 536 592 592 GLU GLU B . n 
A 1 537 LEU 537 593 593 LEU LEU B . n 
A 1 538 GLY 538 594 594 GLY GLY B . n 
A 1 539 GLN 539 595 595 GLN GLN B . n 
A 1 540 ILE 540 596 596 ILE ILE B . n 
A 1 541 PRO 541 597 597 PRO PRO B . n 
A 1 542 SER 542 598 598 SER SER B . n 
A 1 543 LEU 543 599 599 LEU LEU B . n 
A 1 544 ALA 544 600 600 ALA ALA B . n 
A 1 545 ILE 545 601 601 ILE ILE B . n 
A 1 546 SER 546 602 602 SER SER B . n 
A 1 547 LEU 547 603 603 LEU LEU B . n 
A 1 548 ASN 548 604 604 ASN ASN B . n 
A 1 549 LEU 549 605 605 LEU LEU B . n 
A 1 550 SER 550 606 606 SER SER B . n 
A 1 551 CYS 551 607 607 CYS CYS B . n 
A 1 552 ASN 552 608 608 ASN ASN B . n 
A 1 553 ARG 553 609 609 ARG ARG B . n 
A 1 554 PHE 554 610 610 PHE PHE B . n 
A 1 555 VAL 555 611 611 VAL VAL B . n 
A 1 556 GLY 556 612 612 GLY GLY B . n 
A 1 557 GLU 557 613 613 GLU GLU B . n 
A 1 558 ILE 558 614 614 ILE ILE B . n 
A 1 559 PRO 559 615 615 PRO PRO B . n 
A 1 560 SER 560 616 616 SER SER B . n 
A 1 561 ARG 561 617 617 ARG ARG B . n 
A 1 562 PHE 562 618 618 PHE PHE B . n 
A 1 563 SER 563 619 619 SER SER B . n 
A 1 564 ASP 564 620 620 ASP ASP B . n 
A 1 565 LEU 565 621 621 LEU LEU B . n 
A 1 566 LYS 566 622 622 LYS LYS B . n 
A 1 567 ASN 567 623 623 ASN ASN B . n 
A 1 568 LEU 568 624 624 LEU LEU B . n 
A 1 569 GLY 569 625 625 GLY GLY B . n 
A 1 570 VAL 570 626 626 VAL VAL B . n 
A 1 571 LEU 571 627 627 LEU LEU B . n 
A 1 572 ASP 572 628 628 ASP ASP B . n 
A 1 573 VAL 573 629 629 VAL VAL B . n 
A 1 574 SER 574 630 630 SER SER B . n 
A 1 575 HIS 575 631 631 HIS HIS B . n 
A 1 576 ASN 576 632 632 ASN ASN B . n 
A 1 577 GLN 577 633 633 GLN GLN B . n 
A 1 578 LEU 578 634 634 LEU LEU B . n 
A 1 579 THR 579 635 635 THR THR B . n 
A 1 580 GLY 580 636 636 GLY GLY B . n 
A 1 581 ASN 581 637 637 ASN ASN B . n 
A 1 582 LEU 582 638 638 LEU LEU B . n 
A 1 583 ASN 583 639 639 ASN ASN B . n 
A 1 584 VAL 584 640 640 VAL VAL B . n 
A 1 585 LEU 585 641 641 LEU LEU B . n 
A 1 586 THR 586 642 642 THR THR B . n 
A 1 587 ASP 587 643 643 ASP ASP B . n 
A 1 588 LEU 588 644 644 LEU LEU B . n 
A 1 589 GLN 589 645 645 GLN GLN B . n 
A 1 590 ASN 590 646 646 ASN ASN B . n 
A 1 591 LEU 591 647 647 LEU LEU B . n 
A 1 592 VAL 592 648 648 VAL VAL B . n 
A 1 593 SER 593 649 649 SER SER B . n 
A 1 594 LEU 594 650 650 LEU LEU B . n 
A 1 595 ASN 595 651 651 ASN ASN B . n 
A 1 596 ILE 596 652 652 ILE ILE B . n 
A 1 597 SER 597 653 653 SER SER B . n 
A 1 598 TYR 598 654 654 TYR TYR B . n 
A 1 599 ASN 599 655 655 ASN ASN B . n 
A 1 600 ASP 600 656 656 ASP ASP B . n 
A 1 601 PHE 601 657 657 PHE PHE B . n 
A 1 602 SER 602 658 658 SER SER B . n 
A 1 603 GLY 603 659 659 GLY GLY B . n 
A 1 604 ASP 604 660 660 ASP ASP B . n 
A 1 605 LEU 605 661 661 LEU LEU B . n 
A 1 606 PRO 606 662 662 PRO PRO B . n 
A 1 607 ASN 607 663 663 ASN ASN B . n 
A 1 608 THR 608 664 664 THR THR B . n 
A 1 609 PRO 609 665 665 PRO PRO B . n 
A 1 610 PHE 610 666 666 PHE PHE B . n 
A 1 611 PHE 611 667 667 PHE PHE B . n 
A 1 612 ARG 612 668 668 ARG ARG B . n 
A 1 613 ARG 613 669 669 ARG ARG B . n 
A 1 614 LEU 614 670 670 LEU LEU B . n 
A 1 615 PRO 615 671 671 PRO PRO B . n 
A 1 616 LEU 616 672 672 LEU LEU B . n 
A 1 617 SER 617 673 673 SER SER B . n 
A 1 618 ASP 618 674 674 ASP ASP B . n 
A 1 619 LEU 619 675 675 LEU LEU B . n 
A 1 620 ALA 620 676 676 ALA ALA B . n 
A 1 621 SER 621 677 677 SER SER B . n 
A 1 622 ASN 622 678 678 ASN ASN B . n 
A 1 623 ARG 623 679 679 ARG ARG B . n 
A 1 624 GLY 624 680 680 GLY GLY B . n 
A 1 625 LEU 625 681 681 LEU LEU B . n 
A 1 626 TYR 626 682 682 TYR TYR B . n 
A 1 627 ILE 627 683 683 ILE ILE B . n 
A 1 628 SER 628 684 684 SER SER B . n 
A 1 629 ASN 629 685 685 ASN ASN B . n 
A 1 630 ALA 630 686 686 ALA ALA B . n 
A 1 631 ILE 631 687 ?   ?   ?   B . n 
A 1 632 SER 632 688 ?   ?   ?   B . n 
A 1 633 THR 633 689 ?   ?   ?   B . n 
B 2 1   ASP 1   44  44  ASP ASP A . n 
B 2 2   PTR 2   45  45  PTR PTR A . n 
B 2 3   TRP 3   46  46  TRP TRP A . n 
B 2 4   ARG 4   47  47  ARG ARG A . n 
B 2 5   ALA 5   48  48  ALA ALA A . n 
B 2 6   LYS 6   49  49  LYS LYS A . n 
B 2 7   HIS 7   50  50  HIS HIS A . n 
B 2 8   HIS 8   51  51  HIS HIS A . n 
B 2 9   PRO 9   52  52  PRO PRO A . n 
B 2 10  HZP 10  53  53  HZP HYP A . n 
B 2 11  LYS 11  54  54  LYS LYS A . n 
B 2 12  ASN 12  55  55  ASN ASN A . n 
B 2 13  ASN 13  56  56  ASN ASN A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 NAG 1 701 4521 NAG NAG B . 
D 3 NAG 2 702 4522 NAG NAG B . 
E 3 NAG 1 703 6041 NAG NAG B . 
F 3 NAG 1 704 6501 NAG NAG B . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2920  ? 
1 MORE         10    ? 
1 'SSA (A^2)'  26610 ? 
# 
_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 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2017-03-22 
# 
_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_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .    1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20 3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-2000    ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .    5 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    6 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLY 
_pdbx_validate_close_contact.auth_seq_id_1    594 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NH1 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   ARG 
_pdbx_validate_close_contact.auth_seq_id_2    617 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.05 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              617 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              617 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              617 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.20 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.10 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                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 GLN B 83  ? ? 59.45   76.49   
2  1 LEU B 84  ? ? -123.10 -169.77 
3  1 THR B 96  ? ? -121.55 -57.93  
4  1 SER B 248 ? ? -128.92 -165.68 
5  1 GLN B 265 ? ? -121.56 -54.37  
6  1 GLN B 295 ? ? 60.46   60.25   
7  1 ASN B 296 ? ? -129.21 -163.20 
8  1 ASN B 320 ? ? -128.74 -169.10 
9  1 VAL B 343 ? ? 58.07   70.60   
10 1 SER B 439 ? ? 53.25   71.19   
11 1 SER B 539 ? ? 56.42   -146.17 
12 1 ALA B 600 ? ? -135.76 -57.09  
13 1 ASN B 608 ? ? -126.80 -169.99 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 B CYS 61  ? SG  ? A CYS 1  SG  
2  1 Y 1 B ASN 62  ? CG  ? A ASN 2  CG  
3  1 Y 1 B ASN 62  ? OD1 ? A ASN 2  OD1 
4  1 Y 1 B ASN 62  ? ND2 ? A ASN 2  ND2 
5  1 Y 1 B THR 64  ? OG1 ? A THR 4  OG1 
6  1 Y 1 B THR 64  ? CG2 ? A THR 4  CG2 
7  1 Y 1 B GLU 81  ? CG  ? A GLU 21 CG  
8  1 Y 1 B GLU 81  ? CD  ? A GLU 21 CD  
9  1 Y 1 B GLU 81  ? OE1 ? A GLU 21 OE1 
10 1 Y 1 B GLU 81  ? OE2 ? A GLU 21 OE2 
11 1 Y 1 B LYS 82  ? CG  ? A LYS 22 CG  
12 1 Y 1 B LYS 82  ? CD  ? A LYS 22 CD  
13 1 Y 1 B LYS 82  ? CE  ? A LYS 22 CE  
14 1 Y 1 B LYS 82  ? NZ  ? A LYS 22 NZ  
15 1 Y 1 B GLN 83  ? CG  ? A GLN 23 CG  
16 1 Y 1 B GLN 83  ? CD  ? A GLN 23 CD  
17 1 Y 1 B GLN 83  ? OE1 ? A GLN 23 OE1 
18 1 Y 1 B GLN 83  ? NE2 ? A GLN 23 NE2 
19 1 Y 1 B GLN 104 ? CG  ? A GLN 48 CG  
20 1 Y 1 B GLN 104 ? CD  ? A GLN 48 CD  
21 1 Y 1 B GLN 104 ? OE1 ? A GLN 48 OE1 
22 1 Y 1 B GLN 104 ? NE2 ? A GLN 48 NE2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B PRO 88  A A PRO 29  
2  1 Y 1 B VAL 88  B A VAL 30  
3  1 Y 1 B THR 88  C A THR 31  
4  1 Y 1 B SER 88  D A SER 32  
5  1 Y 1 B LEU 88  E A LEU 33  
6  1 Y 1 B ARG 88  F A ARG 34  
7  1 Y 1 B SER 88  G A SER 35  
8  1 Y 1 B ILE 687 ? A ILE 631 
9  1 Y 1 B SER 688 ? A SER 632 
10 1 Y 1 B THR 689 ? A THR 633 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        N-ACETYL-D-GLUCOSAMINE 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
