data_5HZ3
# 
_entry.id   5HZ3 
# 
_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   5HZ3         
WWPDB D_1000217986 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 5HZ1 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                        5HZ3 
_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           179.174 
_cell.length_b           179.174 
_cell.length_c           88.402 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        120.000 
_cell.entry_id           5HZ3 
_cell.Z_PDB              9 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.entry_id                         5HZ3 
_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-PRO-LYS-PRO-SER-THR-ARG-PRO-HYP-ARG-HIS-ASN                    1664.714  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)PKPSTRP(HZP)RHN' DYPKPSTRPPRHN 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   PRO n 
2 4   LYS n 
2 5   PRO n 
2 6   SER n 
2 7   THR n 
2 8   ARG n 
2 9   PRO n 
2 10  HZP n 
2 11  ARG n 
2 12  HIS 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 5HZ3        5HZ3   ? 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 5HZ3 B 1 ? 633 ? C0LGR3 57 ? 689 ? 61 689 
2 2 5HZ3 A 1 ? 13  ? 5HZ3   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 5HZ3 THR B 4  ? UNP C0LGR3 VAL 60  'engineered mutation' 64  1 
1 5HZ3 GLU B 21 ? UNP C0LGR3 GLY 77  'engineered mutation' 81  2 
1 5HZ3 LYS B 22 ? UNP C0LGR3 MET 78  'engineered mutation' 82  3 
1 5HZ3 GLN B 23 ? UNP C0LGR3 ASP 79  'engineered mutation' 83  4 
1 5HZ3 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                   5HZ3 
_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            3.85 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         68.08 
_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                     5HZ3 
_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            2.860 
_reflns.number_obs                   22741 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         93.0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.4000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              5.30 
_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                                 5HZ3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.8600 
_refine.ls_d_res_low                             29.8800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    93.0600 
_refine.ls_number_reflns_obs                     22725 
_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                          0.2431 
_refine.ls_R_factor_R_work                       0.2431 
_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                               26.2220 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            2.4400 
_refine.aniso_B[2][2]                            2.4400 
_refine.aniso_B[3][3]                            -7.9100 
_refine.aniso_B[1][2]                            2.4400 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            -0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9040 
_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                       0.9250 
_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                                134.430 
_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                       2.8600 
_refine_hist.d_res_low                        29.8800 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               4948 
_refine_hist.pdbx_number_residues_total       638 
_refine_hist.pdbx_B_iso_mean_ligand           28.98 
_refine_hist.pdbx_number_atoms_protein        4892 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
_refine_ls_shell.d_res_high                       2.8610 
_refine_ls_shell.d_res_low                        2.9350 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.9400 
_refine_ls_shell.number_reflns_R_work             1783 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.2830 
_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                     5HZ3 
_struct.title                        'Plant peptide hormone receptor RGFR1 in complex with RGFR5' 
_struct.pdbx_descriptor              
;ASP-PTR-PRO-LYS-PRO-SER-THR-ARG-PRO-HYP-ARG-HIS-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        5HZ3 
_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 ? ILE A 540 ? PRO B 590 ILE B 596 5 ? 7 
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 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 ? ? ? ? ? ? ? 1.444 ? 
covale2 covale one  ? A ASN 548 ND2 ? ? ? 1_555 E NAG .  C1 ? ? B ASN 604 B NAG 703 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale3 covale one  ? A ASN 595 ND2 ? ? ? 1_555 F NAG .  C1 ? ? B ASN 651 B NAG 704 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale4 covale both ? B ASP 1   C   ? ? ? 1_555 B PTR 2  N  ? ? A ASP 44  A PTR 45  1_555 ? ? ? ? ? ? ? 1.330 ? 
covale5 covale both ? B PTR 2   C   ? ? ? 1_555 B PRO 3  N  ? ? A PTR 45  A PRO 46  1_555 ? ? ? ? ? ? ? 1.341 ? 
covale6 covale both ? B PRO 9   C   ? ? ? 1_555 B HZP 10 N  ? ? A PRO 52  A HZP 53  1_555 ? ? ? ? ? ? ? 1.333 ? 
covale7 covale both ? B HZP 10  C   ? ? ? 1_555 B ARG 11 N  ? ? A HZP 53  A ARG 54  1_555 ? ? ? ? ? ? ? 1.329 ? 
covale8 covale both ? C NAG .   O4  ? ? ? 1_555 D NAG .  C1 ? ? B NAG 701 B NAG 702 1_555 ? ? ? ? ? ? ? 1.458 ? 
# 
_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 ? 2  ? 
AA3 ? 2  ? 
AA4 ? 2  ? 
AA5 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? 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      
AA3 1  2  ? parallel      
AA4 1  2  ? parallel      
AA5 1  2  ? 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 ? GLU A 124 ? SER B 178 GLU B 180 
AA2 2  ASN A 145 ? ARG A 147 ? ASN B 201 ARG B 203 
AA3 1  SER A 171 ? GLY A 172 ? SER B 227 GLY B 228 
AA3 2  LEU A 193 ? LEU A 194 ? LEU B 249 LEU B 250 
AA4 1  SER A 506 ? GLY A 507 ? SER B 562 GLY B 563 
AA4 2  ASP A 528 ? PHE A 529 ? ASP B 584 PHE B 585 
AA5 1  SER A 602 ? LEU A 605 ? SER B 658 LEU B 661 
AA5 2  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 SER A 41  ? O SER B 97  
AA1 3  4  N LEU A 42  ? N LEU B 98  O ASP A 67  ? O ASP B 123 
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 VAL A 137 ? O VAL B 193 
AA1 7  8  N LEU A 138 ? N LEU B 194 O MET A 162 ? O MET B 218 
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 SER A 234 ? O SER B 290 
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 LYS A 378 ? O LYS B 434 
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 PHE A 426 ? O PHE B 482 
AA1 19 20 N VAL A 427 ? N VAL B 483 O PHE A 450 ? O PHE B 506 
AA1 20 21 N LEU A 451 ? N LEU B 507 O PHE A 473 ? O PHE B 529 
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 
AA3 1  2  N GLY A 172 ? N GLY B 228 O LEU A 193 ? O LEU B 249 
AA4 1  2  N GLY A 507 ? N GLY B 563 O ASP A 528 ? O ASP B 584 
AA5 1  2  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 ? 6 '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 ARG A 83  ? ARG B 139 . ? 8_544 ? 
2  AC1 5 LYS A 368 ? LYS B 424 . ? 1_555 ? 
3  AC1 5 GLY A 372 ? GLY B 428 . ? 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 6 SER A 550 ? SER B 606 . ? 1_555 ? 
12 AC3 6 ASP A 572 ? ASP B 628 . ? 1_555 ? 
13 AC3 6 SER A 574 ? SER B 630 . ? 1_555 ? 
14 AC3 6 SER A 593 ? SER B 649 . ? 1_555 ? 
15 AC3 6 ASN A 595 ? ASN B 651 . ? 1_555 ? 
16 AC3 6 NAG E .   ? NAG B 703 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5HZ3 
_atom_sites.fract_transf_matrix[1][1]   0.005581 
_atom_sites.fract_transf_matrix[1][2]   0.003222 
_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]   0.006445 
_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]   0.011312 
_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   ? 71.065 37.749  -36.775 1.00 50.90  ? 61  CYS B N   1 
ATOM   2    C CA  . CYS A 1 1   ? 69.916 37.430  -35.930 1.00 70.97  ? 61  CYS B CA  1 
ATOM   3    C C   . CYS A 1 1   ? 68.868 36.595  -36.674 1.00 68.40  ? 61  CYS B C   1 
ATOM   4    O O   . CYS A 1 1   ? 67.665 36.739  -36.453 1.00 58.73  ? 61  CYS B O   1 
ATOM   5    C CB  . CYS A 1 1   ? 69.281 38.709  -35.376 1.00 71.32  ? 61  CYS B CB  1 
ATOM   6    N N   . ASN A 1 2   ? 69.345 35.731  -37.564 1.00 78.84  ? 62  ASN B N   1 
ATOM   7    C CA  . ASN A 1 2   ? 68.493 34.822  -38.328 1.00 80.46  ? 62  ASN B CA  1 
ATOM   8    C C   . ASN A 1 2   ? 68.374 33.443  -37.681 1.00 86.07  ? 62  ASN B C   1 
ATOM   9    O O   . ASN A 1 2   ? 67.808 32.524  -38.279 1.00 89.15  ? 62  ASN B O   1 
ATOM   10   C CB  . ASN A 1 2   ? 68.996 34.685  -39.768 1.00 77.15  ? 62  ASN B CB  1 
ATOM   11   N N   . TRP A 1 3   ? 68.922 33.304  -36.473 1.00 84.08  ? 63  TRP B N   1 
ATOM   12   C CA  . TRP A 1 3   ? 69.000 32.014  -35.786 1.00 87.27  ? 63  TRP B CA  1 
ATOM   13   C C   . TRP A 1 3   ? 67.639 31.310  -35.662 1.00 83.90  ? 63  TRP B C   1 
ATOM   14   O O   . TRP A 1 3   ? 66.595 31.960  -35.576 1.00 82.72  ? 63  TRP B O   1 
ATOM   15   C CB  . TRP A 1 3   ? 69.629 32.181  -34.394 1.00 95.26  ? 63  TRP B CB  1 
ATOM   16   C CG  . TRP A 1 3   ? 71.099 32.523  -34.404 1.00 104.60 ? 63  TRP B CG  1 
ATOM   17   C CD1 . TRP A 1 3   ? 71.674 33.700  -34.011 1.00 108.02 ? 63  TRP B CD1 1 
ATOM   18   C CD2 . TRP A 1 3   ? 72.175 31.673  -34.824 1.00 108.15 ? 63  TRP B CD2 1 
ATOM   19   N NE1 . TRP A 1 3   ? 73.040 33.634  -34.161 1.00 110.48 ? 63  TRP B NE1 1 
ATOM   20   C CE2 . TRP A 1 3   ? 73.372 32.402  -34.660 1.00 111.30 ? 63  TRP B CE2 1 
ATOM   21   C CE3 . TRP A 1 3   ? 72.242 30.369  -35.324 1.00 105.58 ? 63  TRP B CE3 1 
ATOM   22   C CZ2 . TRP A 1 3   ? 74.618 31.868  -34.978 1.00 112.85 ? 63  TRP B CZ2 1 
ATOM   23   C CZ3 . TRP A 1 3   ? 73.478 29.842  -35.638 1.00 106.57 ? 63  TRP B CZ3 1 
ATOM   24   C CH2 . TRP A 1 3   ? 74.650 30.590  -35.466 1.00 110.89 ? 63  TRP B CH2 1 
ATOM   25   N N   . THR A 1 4   ? 67.661 29.979  -35.683 1.00 79.04  ? 64  THR B N   1 
ATOM   26   C CA  . THR A 1 4   ? 66.443 29.182  -35.568 1.00 66.82  ? 64  THR B CA  1 
ATOM   27   C C   . THR A 1 4   ? 65.850 29.326  -34.172 1.00 64.40  ? 64  THR B C   1 
ATOM   28   O O   . THR A 1 4   ? 66.532 29.091  -33.174 1.00 65.73  ? 64  THR B O   1 
ATOM   29   C CB  . THR A 1 4   ? 66.717 27.690  -35.843 1.00 58.96  ? 64  THR B CB  1 
ATOM   30   N N   . GLY A 1 5   ? 64.579 29.712  -34.107 1.00 59.80  ? 65  GLY B N   1 
ATOM   31   C CA  . GLY A 1 5   ? 63.927 30.000  -32.842 1.00 55.76  ? 65  GLY B CA  1 
ATOM   32   C C   . GLY A 1 5   ? 63.757 31.491  -32.589 1.00 51.16  ? 65  GLY B C   1 
ATOM   33   O O   . GLY A 1 5   ? 63.202 31.902  -31.569 1.00 44.54  ? 65  GLY B O   1 
ATOM   34   N N   . VAL A 1 6   ? 64.232 32.308  -33.523 1.00 53.25  ? 66  VAL B N   1 
ATOM   35   C CA  . VAL A 1 6   ? 64.105 33.757  -33.400 1.00 54.79  ? 66  VAL B CA  1 
ATOM   36   C C   . VAL A 1 6   ? 63.317 34.331  -34.583 1.00 56.91  ? 66  VAL B C   1 
ATOM   37   O O   . VAL A 1 6   ? 63.525 33.942  -35.728 1.00 51.19  ? 66  VAL B O   1 
ATOM   38   C CB  . VAL A 1 6   ? 65.491 34.452  -33.290 1.00 46.73  ? 66  VAL B CB  1 
ATOM   39   C CG1 . VAL A 1 6   ? 65.327 35.949  -33.094 1.00 46.85  ? 66  VAL B CG1 1 
ATOM   40   C CG2 . VAL A 1 6   ? 66.311 33.858  -32.148 1.00 42.01  ? 66  VAL B CG2 1 
ATOM   41   N N   . LYS A 1 7   ? 62.394 35.240  -34.287 1.00 61.90  ? 67  LYS B N   1 
ATOM   42   C CA  . LYS A 1 7   ? 61.605 35.918  -35.306 1.00 59.25  ? 67  LYS B CA  1 
ATOM   43   C C   . LYS A 1 7   ? 61.835 37.425  -35.195 1.00 60.12  ? 67  LYS B C   1 
ATOM   44   O O   . LYS A 1 7   ? 61.623 38.009  -34.142 1.00 58.24  ? 67  LYS B O   1 
ATOM   45   C CB  . LYS A 1 7   ? 60.111 35.606  -35.132 1.00 60.03  ? 67  LYS B CB  1 
ATOM   46   C CG  . LYS A 1 7   ? 59.730 34.138  -35.311 1.00 62.42  ? 67  LYS B CG  1 
ATOM   47   C CD  . LYS A 1 7   ? 58.208 33.943  -35.340 1.00 66.16  ? 67  LYS B CD  1 
ATOM   48   C CE  . LYS A 1 7   ? 57.547 34.822  -36.407 1.00 72.41  ? 67  LYS B CE  1 
ATOM   49   N NZ  . LYS A 1 7   ? 56.689 34.063  -37.368 1.00 70.77  ? 67  LYS B NZ  1 
ATOM   50   N N   . CYS A 1 8   ? 62.279 38.059  -36.272 1.00 67.69  ? 68  CYS B N   1 
ATOM   51   C CA  . CYS A 1 8   ? 62.497 39.501  -36.247 1.00 71.85  ? 68  CYS B CA  1 
ATOM   52   C C   . CYS A 1 8   ? 61.279 40.253  -36.780 1.00 70.34  ? 68  CYS B C   1 
ATOM   53   O O   . CYS A 1 8   ? 60.629 39.797  -37.720 1.00 69.11  ? 68  CYS B O   1 
ATOM   54   C CB  . CYS A 1 8   ? 63.752 39.872  -37.041 1.00 73.96  ? 68  CYS B CB  1 
ATOM   55   S SG  . CYS A 1 8   ? 65.305 39.752  -36.109 1.00 74.63  ? 68  CYS B SG  1 
ATOM   56   N N   . ASN A 1 9   ? 60.962 41.390  -36.159 1.00 69.31  ? 69  ASN B N   1 
ATOM   57   C CA  . ASN A 1 9   ? 59.859 42.239  -36.613 1.00 69.46  ? 69  ASN B CA  1 
ATOM   58   C C   . ASN A 1 9   ? 60.204 42.898  -37.946 1.00 79.06  ? 69  ASN B C   1 
ATOM   59   O O   . ASN A 1 9   ? 61.377 42.942  -38.323 1.00 88.27  ? 69  ASN B O   1 
ATOM   60   C CB  . ASN A 1 9   ? 59.442 43.271  -35.541 1.00 63.89  ? 69  ASN B CB  1 
ATOM   61   C CG  . ASN A 1 9   ? 60.497 44.352  -35.288 1.00 71.29  ? 69  ASN B CG  1 
ATOM   62   O OD1 . ASN A 1 9   ? 61.622 44.281  -35.779 1.00 80.45  ? 69  ASN B OD1 1 
ATOM   63   N ND2 . ASN A 1 9   ? 60.123 45.362  -34.503 1.00 68.54  ? 69  ASN B ND2 1 
ATOM   64   N N   . ARG A 1 10  ? 59.195 43.379  -38.674 1.00 76.60  ? 70  ARG B N   1 
ATOM   65   C CA  . ARG A 1 10  ? 59.453 44.024  -39.966 1.00 78.96  ? 70  ARG B CA  1 
ATOM   66   C C   . ARG A 1 10  ? 60.242 45.339  -39.851 1.00 78.15  ? 70  ARG B C   1 
ATOM   67   O O   . ARG A 1 10  ? 60.634 45.905  -40.878 1.00 75.80  ? 70  ARG B O   1 
ATOM   68   C CB  . ARG A 1 10  ? 58.167 44.274  -40.769 1.00 82.59  ? 70  ARG B CB  1 
ATOM   69   C CG  . ARG A 1 10  ? 57.269 45.352  -40.205 1.00 83.35  ? 70  ARG B CG  1 
ATOM   70   C CD  . ARG A 1 10  ? 56.364 45.973  -41.268 1.00 81.06  ? 70  ARG B CD  1 
ATOM   71   N NE  . ARG A 1 10  ? 55.918 45.000  -42.261 1.00 80.64  ? 70  ARG B NE  1 
ATOM   72   C CZ  . ARG A 1 10  ? 55.652 45.295  -43.532 1.00 81.11  ? 70  ARG B CZ  1 
ATOM   73   N NH1 . ARG A 1 10  ? 55.780 46.544  -43.968 1.00 80.98  ? 70  ARG B NH1 1 
ATOM   74   N NH2 . ARG A 1 10  ? 55.259 44.342  -44.370 1.00 77.29  ? 70  ARG B NH2 1 
ATOM   75   N N   . ARG A 1 11  ? 60.455 45.841  -38.626 1.00 75.18  ? 71  ARG B N   1 
ATOM   76   C CA  . ARG A 1 11  ? 61.412 46.950  -38.404 1.00 69.05  ? 71  ARG B CA  1 
ATOM   77   C C   . ARG A 1 11  ? 62.829 46.473  -38.003 1.00 68.18  ? 71  ARG B C   1 
ATOM   78   O O   . ARG A 1 11  ? 63.710 47.283  -37.703 1.00 70.22  ? 71  ARG B O   1 
ATOM   79   C CB  . ARG A 1 11  ? 60.866 48.103  -37.497 1.00 99.01  ? 71  ARG B CB  1 
ATOM   80   C CG  . ARG A 1 11  ? 61.115 48.162  -36.014 1.00 98.20  ? 71  ARG B CG  1 
ATOM   81   C CD  . ARG A 1 11  ? 60.887 49.567  -35.525 1.00 95.31  ? 71  ARG B CD  1 
ATOM   82   N NE  . ARG A 1 11  ? 59.563 49.746  -35.012 1.00 91.74  ? 71  ARG B NE  1 
ATOM   83   C CZ  . ARG A 1 11  ? 59.249 49.756  -33.725 1.00 87.75  ? 71  ARG B CZ  1 
ATOM   84   N NH1 . ARG A 1 11  ? 60.183 49.592  -32.831 1.00 87.11  ? 71  ARG B NH1 1 
ATOM   85   N NH2 . ARG A 1 11  ? 57.990 49.937  -33.314 1.00 84.30  ? 71  ARG B NH2 1 
ATOM   86   N N   . GLY A 1 12  ? 63.031 45.159  -37.948 1.00 66.51  ? 72  GLY B N   1 
ATOM   87   C CA  . GLY A 1 12  ? 64.368 44.606  -37.815 1.00 67.43  ? 72  GLY B CA  1 
ATOM   88   C C   . GLY A 1 12  ? 64.856 44.137  -36.456 1.00 71.47  ? 72  GLY B C   1 
ATOM   89   O O   . GLY A 1 12  ? 65.727 43.268  -36.418 1.00 74.47  ? 72  GLY B O   1 
ATOM   90   N N   . GLU A 1 13  ? 64.300 44.658  -35.358 1.00 72.51  ? 73  GLU B N   1 
ATOM   91   C CA  . GLU A 1 13  ? 64.659 44.163  -34.024 1.00 67.50  ? 73  GLU B CA  1 
ATOM   92   C C   . GLU A 1 13  ? 63.939 42.854  -33.676 1.00 63.17  ? 73  GLU B C   1 
ATOM   93   O O   . GLU A 1 13  ? 62.877 42.515  -34.214 1.00 42.72  ? 73  GLU B O   1 
ATOM   94   C CB  . GLU A 1 13  ? 64.455 45.194  -32.893 1.00 69.49  ? 73  GLU B CB  1 
ATOM   95   C CG  . GLU A 1 13  ? 64.977 46.580  -33.126 1.00 76.78  ? 73  GLU B CG  1 
ATOM   96   C CD  . GLU A 1 13  ? 63.889 47.484  -33.602 1.00 79.64  ? 73  GLU B CD  1 
ATOM   97   O OE1 . GLU A 1 13  ? 62.665 47.215  -33.377 1.00 80.16  ? 73  GLU B OE1 1 
ATOM   98   O OE2 . GLU A 1 13  ? 64.194 48.531  -34.238 1.00 79.55  ? 73  GLU B OE2 1 
ATOM   99   N N   . VAL A 1 14  ? 64.555 42.137  -32.751 1.00 62.53  ? 74  VAL B N   1 
ATOM   100  C CA  . VAL A 1 14  ? 64.017 40.921  -32.192 1.00 60.97  ? 74  VAL B CA  1 
ATOM   101  C C   . VAL A 1 14  ? 62.569 41.098  -31.748 1.00 59.25  ? 74  VAL B C   1 
ATOM   102  O O   . VAL A 1 14  ? 62.191 42.073  -31.090 1.00 62.27  ? 74  VAL B O   1 
ATOM   103  C CB  . VAL A 1 14  ? 64.870 40.500  -31.006 1.00 60.99  ? 74  VAL B CB  1 
ATOM   104  C CG1 . VAL A 1 14  ? 64.480 39.124  -30.564 1.00 59.03  ? 74  VAL B CG1 1 
ATOM   105  C CG2 . VAL A 1 14  ? 66.337 40.530  -31.413 1.00 60.71  ? 74  VAL B CG2 1 
ATOM   106  N N   . SER A 1 15  ? 61.766 40.137  -32.174 1.00 52.57  ? 75  SER B N   1 
ATOM   107  C CA  . SER A 1 15  ? 60.343 40.131  -31.935 1.00 46.60  ? 75  SER B CA  1 
ATOM   108  C C   . SER A 1 15  ? 59.999 38.942  -31.038 1.00 52.79  ? 75  SER B C   1 
ATOM   109  O O   . SER A 1 15  ? 59.443 39.126  -29.961 1.00 61.66  ? 75  SER B O   1 
ATOM   110  C CB  . SER A 1 15  ? 59.586 40.074  -33.262 1.00 41.35  ? 75  SER B CB  1 
ATOM   111  O OG  . SER A 1 15  ? 58.354 40.759  -33.176 1.00 40.79  ? 75  SER B OG  1 
ATOM   112  N N   . GLU A 1 16  ? 60.304 37.725  -31.489 1.00 48.06  ? 76  GLU B N   1 
ATOM   113  C CA  . GLU A 1 16  ? 59.941 36.517  -30.746 1.00 46.43  ? 76  GLU B CA  1 
ATOM   114  C C   . GLU A 1 16  ? 61.118 35.594  -30.404 1.00 48.63  ? 76  GLU B C   1 
ATOM   115  O O   . GLU A 1 16  ? 62.002 35.366  -31.231 1.00 48.73  ? 76  GLU B O   1 
ATOM   116  C CB  . GLU A 1 16  ? 58.889 35.711  -31.514 1.00 40.11  ? 76  GLU B CB  1 
ATOM   117  C CG  . GLU A 1 16  ? 57.561 36.419  -31.738 1.00 40.52  ? 76  GLU B CG  1 
ATOM   118  C CD  . GLU A 1 16  ? 56.537 35.510  -32.414 1.00 42.46  ? 76  GLU B CD  1 
ATOM   119  O OE1 . GLU A 1 16  ? 55.585 36.027  -33.051 1.00 35.73  ? 76  GLU B OE1 1 
ATOM   120  O OE2 . GLU A 1 16  ? 56.691 34.270  -32.303 1.00 45.74  ? 76  GLU B OE2 1 
ATOM   121  N N   . ILE A 1 17  ? 61.104 35.052  -29.184 1.00 46.34  ? 77  ILE B N   1 
ATOM   122  C CA  . ILE A 1 17  ? 62.033 33.990  -28.791 1.00 49.64  ? 77  ILE B CA  1 
ATOM   123  C C   . ILE A 1 17  ? 61.289 32.690  -28.484 1.00 50.68  ? 77  ILE B C   1 
ATOM   124  O O   . ILE A 1 17  ? 60.293 32.699  -27.768 1.00 54.03  ? 77  ILE B O   1 
ATOM   125  C CB  . ILE A 1 17  ? 62.903 34.399  -27.584 1.00 53.07  ? 77  ILE B CB  1 
ATOM   126  C CG1 . ILE A 1 17  ? 63.981 35.390  -28.020 1.00 51.61  ? 77  ILE B CG1 1 
ATOM   127  C CG2 . ILE A 1 17  ? 63.564 33.184  -26.952 1.00 54.25  ? 77  ILE B CG2 1 
ATOM   128  C CD1 . ILE A 1 17  ? 64.964 35.717  -26.936 1.00 41.37  ? 77  ILE B CD1 1 
ATOM   129  N N   . GLN A 1 18  ? 61.769 31.581  -29.046 1.00 52.67  ? 78  GLN B N   1 
ATOM   130  C CA  . GLN A 1 18  ? 61.110 30.282  -28.896 1.00 51.79  ? 78  GLN B CA  1 
ATOM   131  C C   . GLN A 1 18  ? 62.076 29.125  -28.627 1.00 57.30  ? 78  GLN B C   1 
ATOM   132  O O   . GLN A 1 18  ? 62.949 28.834  -29.446 1.00 57.34  ? 78  GLN B O   1 
ATOM   133  C CB  . GLN A 1 18  ? 60.297 29.968  -30.148 1.00 45.63  ? 78  GLN B CB  1 
ATOM   134  C CG  . GLN A 1 18  ? 59.938 28.503  -30.294 1.00 42.33  ? 78  GLN B CG  1 
ATOM   135  C CD  . GLN A 1 18  ? 58.486 28.237  -29.996 1.00 44.21  ? 78  GLN B CD  1 
ATOM   136  O OE1 . GLN A 1 18  ? 57.752 29.133  -29.575 1.00 47.53  ? 78  GLN B OE1 1 
ATOM   137  N NE2 . GLN A 1 18  ? 58.056 27.000  -30.219 1.00 43.59  ? 78  GLN B NE2 1 
ATOM   138  N N   . LEU A 1 19  ? 61.905 28.453  -27.491 1.00 62.69  ? 79  LEU B N   1 
ATOM   139  C CA  . LEU A 1 19  ? 62.718 27.281  -27.160 1.00 62.68  ? 79  LEU B CA  1 
ATOM   140  C C   . LEU A 1 19  ? 61.888 26.187  -26.474 1.00 63.27  ? 79  LEU B C   1 
ATOM   141  O O   . LEU A 1 19  ? 61.159 26.465  -25.527 1.00 60.86  ? 79  LEU B O   1 
ATOM   142  C CB  . LEU A 1 19  ? 63.920 27.692  -26.296 1.00 59.90  ? 79  LEU B CB  1 
ATOM   143  C CG  . LEU A 1 19  ? 65.050 28.415  -27.050 1.00 56.58  ? 79  LEU B CG  1 
ATOM   144  C CD1 . LEU A 1 19  ? 65.488 29.694  -26.350 1.00 57.92  ? 79  LEU B CD1 1 
ATOM   145  C CD2 . LEU A 1 19  ? 66.242 27.497  -27.264 1.00 51.90  ? 79  LEU B CD2 1 
ATOM   146  N N   . LYS A 1 20  ? 61.989 24.952  -26.967 1.00 68.76  ? 80  LYS B N   1 
ATOM   147  C CA  . LYS A 1 20  ? 61.248 23.824  -26.388 1.00 72.77  ? 80  LYS B CA  1 
ATOM   148  C C   . LYS A 1 20  ? 62.002 22.485  -26.404 1.00 80.69  ? 80  LYS B C   1 
ATOM   149  O O   . LYS A 1 20  ? 62.570 22.093  -27.426 1.00 78.20  ? 80  LYS B O   1 
ATOM   150  C CB  . LYS A 1 20  ? 59.891 23.663  -27.077 1.00 68.91  ? 80  LYS B CB  1 
ATOM   151  C CG  . LYS A 1 20  ? 58.770 24.482  -26.454 1.00 68.25  ? 80  LYS B CG  1 
ATOM   152  C CD  . LYS A 1 20  ? 57.510 24.397  -27.297 1.00 69.48  ? 80  LYS B CD  1 
ATOM   153  C CE  . LYS A 1 20  ? 57.118 22.952  -27.556 1.00 68.87  ? 80  LYS B CE  1 
ATOM   154  N NZ  . LYS A 1 20  ? 56.167 22.829  -28.692 1.00 65.30  ? 80  LYS B NZ  1 
ATOM   155  N N   . GLU A 1 21  ? 61.971 21.790  -25.264 1.00 89.71  ? 81  GLU B N   1 
ATOM   156  C CA  . GLU A 1 21  ? 62.602 20.476  -25.082 1.00 94.33  ? 81  GLU B CA  1 
ATOM   157  C C   . GLU A 1 21  ? 64.116 20.465  -25.306 1.00 98.87  ? 81  GLU B C   1 
ATOM   158  O O   . GLU A 1 21  ? 64.641 19.569  -25.970 1.00 102.02 ? 81  GLU B O   1 
ATOM   159  C CB  . GLU A 1 21  ? 61.931 19.417  -25.967 1.00 92.77  ? 81  GLU B CB  1 
ATOM   160  N N   . LYS A 1 22  ? 64.809 21.464  -24.766 1.00 98.19  ? 82  LYS B N   1 
ATOM   161  C CA  . LYS A 1 22  ? 66.264 21.551  -24.909 1.00 97.00  ? 82  LYS B CA  1 
ATOM   162  C C   . LYS A 1 22  ? 67.066 21.048  -23.700 1.00 91.97  ? 82  LYS B C   1 
ATOM   163  O O   . LYS A 1 22  ? 68.297 21.108  -23.707 1.00 94.57  ? 82  LYS B O   1 
ATOM   164  C CB  . LYS A 1 22  ? 66.690 22.971  -25.297 1.00 98.01  ? 82  LYS B CB  1 
ATOM   165  N N   . GLN A 1 23  ? 66.367 20.574  -22.669 1.00 82.98  ? 83  GLN B N   1 
ATOM   166  C CA  . GLN A 1 23  ? 66.998 19.958  -21.491 1.00 76.30  ? 83  GLN B CA  1 
ATOM   167  C C   . GLN A 1 23  ? 68.048 20.815  -20.761 1.00 78.53  ? 83  GLN B C   1 
ATOM   168  O O   . GLN A 1 23  ? 69.110 20.319  -20.395 1.00 83.08  ? 83  GLN B O   1 
ATOM   169  C CB  . GLN A 1 23  ? 67.594 18.591  -21.853 1.00 68.50  ? 83  GLN B CB  1 
ATOM   170  N N   . LEU A 1 24  ? 67.723 22.085  -20.526 1.00 74.67  ? 84  LEU B N   1 
ATOM   171  C CA  . LEU A 1 24  ? 68.591 23.039  -19.822 1.00 67.87  ? 84  LEU B CA  1 
ATOM   172  C C   . LEU A 1 24  ? 68.486 22.833  -18.313 1.00 75.11  ? 84  LEU B C   1 
ATOM   173  O O   . LEU A 1 24  ? 68.031 21.780  -17.862 1.00 75.35  ? 84  LEU B O   1 
ATOM   174  C CB  . LEU A 1 24  ? 68.218 24.483  -20.167 1.00 59.75  ? 84  LEU B CB  1 
ATOM   175  C CG  . LEU A 1 24  ? 68.802 25.144  -21.419 1.00 62.70  ? 84  LEU B CG  1 
ATOM   176  C CD1 . LEU A 1 24  ? 68.455 24.386  -22.686 1.00 61.32  ? 84  LEU B CD1 1 
ATOM   177  C CD2 . LEU A 1 24  ? 68.319 26.584  -21.524 1.00 63.86  ? 84  LEU B CD2 1 
ATOM   178  N N   . GLN A 1 25  ? 68.933 23.828  -17.543 1.00 79.57  ? 85  GLN B N   1 
ATOM   179  C CA  . GLN A 1 25  ? 68.808 23.799  -16.083 1.00 78.61  ? 85  GLN B CA  1 
ATOM   180  C C   . GLN A 1 25  ? 69.225 25.118  -15.432 1.00 81.41  ? 85  GLN B C   1 
ATOM   181  O O   . GLN A 1 25  ? 69.865 25.963  -16.062 1.00 81.11  ? 85  GLN B O   1 
ATOM   182  C CB  . GLN A 1 25  ? 69.658 22.667  -15.500 1.00 79.32  ? 85  GLN B CB  1 
ATOM   183  C CG  . GLN A 1 25  ? 69.131 22.097  -14.203 1.00 81.59  ? 85  GLN B CG  1 
ATOM   184  C CD  . GLN A 1 25  ? 69.267 20.592  -14.148 1.00 85.29  ? 85  GLN B CD  1 
ATOM   185  O OE1 . GLN A 1 25  ? 69.941 20.052  -13.272 1.00 88.79  ? 85  GLN B OE1 1 
ATOM   186  N NE2 . GLN A 1 25  ? 68.624 19.902  -15.088 1.00 83.52  ? 85  GLN B NE2 1 
ATOM   187  N N   . GLY A 1 26  ? 68.838 25.288  -14.168 1.00 82.51  ? 86  GLY B N   1 
ATOM   188  C CA  . GLY A 1 26  ? 69.202 26.461  -13.391 1.00 81.65  ? 86  GLY B CA  1 
ATOM   189  C C   . GLY A 1 26  ? 68.185 27.587  -13.441 1.00 76.47  ? 86  GLY B C   1 
ATOM   190  O O   . GLY A 1 26  ? 67.003 27.368  -13.688 1.00 76.00  ? 86  GLY B O   1 
ATOM   191  N N   . SER A 1 27  ? 68.658 28.805  -13.202 1.00 73.20  ? 87  SER B N   1 
ATOM   192  C CA  . SER A 1 27  ? 67.827 29.994  -13.320 1.00 68.29  ? 87  SER B CA  1 
ATOM   193  C C   . SER A 1 27  ? 67.741 30.361  -14.795 1.00 72.85  ? 87  SER B C   1 
ATOM   194  O O   . SER A 1 27  ? 68.064 29.544  -15.657 1.00 72.56  ? 87  SER B O   1 
ATOM   195  C CB  . SER A 1 27  ? 68.389 31.148  -12.487 1.00 61.95  ? 87  SER B CB  1 
ATOM   196  O OG  . SER A 1 27  ? 68.324 30.858  -11.095 1.00 53.37  ? 87  SER B OG  1 
ATOM   197  N N   . LEU A 1 28  ? 67.268 31.561  -15.103 1.00 77.38  ? 88  LEU B N   1 
ATOM   198  C CA  . LEU A 1 28  ? 67.015 31.891  -16.500 1.00 79.77  ? 88  LEU B CA  1 
ATOM   199  C C   . LEU A 1 28  ? 67.423 33.312  -16.879 1.00 81.60  ? 88  LEU B C   1 
ATOM   200  O O   . LEU A 1 28  ? 67.711 34.140  -16.018 1.00 81.35  ? 88  LEU B O   1 
ATOM   201  C CB  . LEU A 1 28  ? 65.538 31.669  -16.814 1.00 79.94  ? 88  LEU B CB  1 
ATOM   202  C CG  . LEU A 1 28  ? 64.592 32.568  -16.018 1.00 80.49  ? 88  LEU B CG  1 
ATOM   203  C CD1 . LEU A 1 28  ? 63.928 33.633  -16.911 1.00 83.72  ? 88  LEU B CD1 1 
ATOM   204  C CD2 . LEU A 1 28  ? 63.554 31.743  -15.249 1.00 77.36  ? 88  LEU B CD2 1 
ATOM   205  N N   . LEU A 1 36  ? 67.229 44.594  -26.612 1.00 64.36  ? 92  LEU B N   1 
ATOM   206  C CA  . LEU A 1 36  ? 66.019 44.099  -27.269 1.00 62.59  ? 92  LEU B CA  1 
ATOM   207  C C   . LEU A 1 36  ? 64.767 44.334  -26.423 1.00 66.38  ? 92  LEU B C   1 
ATOM   208  O O   . LEU A 1 36  ? 64.154 43.405  -25.896 1.00 65.37  ? 92  LEU B O   1 
ATOM   209  C CB  . LEU A 1 36  ? 66.165 42.625  -27.694 1.00 55.54  ? 92  LEU B CB  1 
ATOM   210  C CG  . LEU A 1 36  ? 66.223 41.418  -26.741 1.00 53.01  ? 92  LEU B CG  1 
ATOM   211  C CD1 . LEU A 1 36  ? 66.670 40.187  -27.522 1.00 49.66  ? 92  LEU B CD1 1 
ATOM   212  C CD2 . LEU A 1 36  ? 67.093 41.625  -25.485 1.00 51.36  ? 92  LEU B CD2 1 
ATOM   213  N N   . LYS A 1 37  ? 64.387 45.600  -26.310 1.00 71.03  ? 93  LYS B N   1 
ATOM   214  C CA  . LYS A 1 37  ? 63.235 45.987  -25.509 1.00 71.97  ? 93  LYS B CA  1 
ATOM   215  C C   . LYS A 1 37  ? 61.978 45.950  -26.373 1.00 65.56  ? 93  LYS B C   1 
ATOM   216  O O   . LYS A 1 37  ? 60.904 46.376  -25.949 1.00 62.79  ? 93  LYS B O   1 
ATOM   217  C CB  . LYS A 1 37  ? 63.464 47.364  -24.879 1.00 76.67  ? 93  LYS B CB  1 
ATOM   218  C CG  . LYS A 1 37  ? 64.786 47.444  -24.115 1.00 81.29  ? 93  LYS B CG  1 
ATOM   219  C CD  . LYS A 1 37  ? 65.043 48.816  -23.504 1.00 84.94  ? 93  LYS B CD  1 
ATOM   220  C CE  . LYS A 1 37  ? 64.344 48.989  -22.161 1.00 81.74  ? 93  LYS B CE  1 
ATOM   221  N NZ  . LYS A 1 37  ? 64.713 50.289  -21.528 1.00 80.10  ? 93  LYS B NZ  1 
ATOM   222  N N   . SER A 1 38  ? 62.146 45.464  -27.603 1.00 62.67  ? 94  SER B N   1 
ATOM   223  C CA  . SER A 1 38  ? 61.046 45.274  -28.551 1.00 61.97  ? 94  SER B CA  1 
ATOM   224  C C   . SER A 1 38  ? 60.481 43.842  -28.657 1.00 63.06  ? 94  SER B C   1 
ATOM   225  O O   . SER A 1 38  ? 59.594 43.594  -29.481 1.00 64.26  ? 94  SER B O   1 
ATOM   226  C CB  . SER A 1 38  ? 61.454 45.779  -29.940 1.00 65.15  ? 94  SER B CB  1 
ATOM   227  O OG  . SER A 1 38  ? 62.848 46.031  -29.998 1.00 70.50  ? 94  SER B OG  1 
ATOM   228  N N   . LEU A 1 39  ? 60.982 42.907  -27.848 1.00 62.10  ? 95  LEU B N   1 
ATOM   229  C CA  . LEU A 1 39  ? 60.592 41.499  -27.991 1.00 55.00  ? 95  LEU B CA  1 
ATOM   230  C C   . LEU A 1 39  ? 59.130 41.337  -27.601 1.00 53.12  ? 95  LEU B C   1 
ATOM   231  O O   . LEU A 1 39  ? 58.741 41.652  -26.472 1.00 50.32  ? 95  LEU B O   1 
ATOM   232  C CB  . LEU A 1 39  ? 61.468 40.606  -27.103 1.00 57.09  ? 95  LEU B CB  1 
ATOM   233  C CG  . LEU A 1 39  ? 61.224 39.091  -27.082 1.00 57.90  ? 95  LEU B CG  1 
ATOM   234  C CD1 . LEU A 1 39  ? 61.877 38.390  -28.263 1.00 58.21  ? 95  LEU B CD1 1 
ATOM   235  C CD2 . LEU A 1 39  ? 61.711 38.480  -25.773 1.00 56.22  ? 95  LEU B CD2 1 
ATOM   236  N N   . THR A 1 40  ? 58.323 40.867  -28.552 1.00 50.20  ? 96  THR B N   1 
ATOM   237  C CA  . THR A 1 40  ? 56.875 40.796  -28.364 1.00 42.51  ? 96  THR B CA  1 
ATOM   238  C C   . THR A 1 40  ? 56.305 39.458  -27.828 1.00 40.36  ? 96  THR B C   1 
ATOM   239  O O   . THR A 1 40  ? 55.197 39.414  -27.289 1.00 31.82  ? 96  THR B O   1 
ATOM   240  C CB  . THR A 1 40  ? 56.155 41.276  -29.660 1.00 39.64  ? 96  THR B CB  1 
ATOM   241  O OG1 . THR A 1 40  ? 55.289 42.377  -29.345 1.00 33.64  ? 96  THR B OG1 1 
ATOM   242  C CG2 . THR A 1 40  ? 55.379 40.137  -30.358 1.00 32.25  ? 96  THR B CG2 1 
ATOM   243  N N   . SER A 1 41  ? 57.081 38.387  -27.938 1.00 33.30  ? 97  SER B N   1 
ATOM   244  C CA  . SER A 1 41  ? 56.665 37.088  -27.428 1.00 32.07  ? 97  SER B CA  1 
ATOM   245  C C   . SER A 1 41  ? 57.841 36.289  -26.898 1.00 42.26  ? 97  SER B C   1 
ATOM   246  O O   . SER A 1 41  ? 58.878 36.183  -27.548 1.00 34.12  ? 97  SER B O   1 
ATOM   247  C CB  . SER A 1 41  ? 55.944 36.282  -28.493 1.00 30.71  ? 97  SER B CB  1 
ATOM   248  O OG  . SER A 1 41  ? 56.307 34.917  -28.408 1.00 51.70  ? 97  SER B OG  1 
ATOM   249  N N   . LEU A 1 42  ? 57.660 35.704  -25.720 1.00 43.38  ? 98  LEU B N   1 
ATOM   250  C CA  . LEU A 1 42  ? 58.736 34.973  -25.076 1.00 43.85  ? 98  LEU B CA  1 
ATOM   251  C C   . LEU A 1 42  ? 58.286 33.586  -24.678 1.00 43.14  ? 98  LEU B C   1 
ATOM   252  O O   . LEU A 1 42  ? 57.359 33.431  -23.890 1.00 45.22  ? 98  LEU B O   1 
ATOM   253  C CB  . LEU A 1 42  ? 59.229 35.730  -23.850 1.00 40.64  ? 98  LEU B CB  1 
ATOM   254  C CG  . LEU A 1 42  ? 60.459 35.083  -23.229 1.00 42.50  ? 98  LEU B CG  1 
ATOM   255  C CD1 . LEU A 1 42  ? 61.558 34.956  -24.283 1.00 40.76  ? 98  LEU B CD1 1 
ATOM   256  C CD2 . LEU A 1 42  ? 60.927 35.878  -22.012 1.00 36.74  ? 98  LEU B CD2 1 
ATOM   257  N N   . THR A 1 43  ? 58.935 32.575  -25.238 1.00 40.94  ? 99  THR B N   1 
ATOM   258  C CA  . THR A 1 43  ? 58.604 31.213  -24.883 1.00 36.71  ? 99  THR B CA  1 
ATOM   259  C C   . THR A 1 43  ? 59.843 30.463  -24.476 1.00 42.96  ? 99  THR B C   1 
ATOM   260  O O   . THR A 1 43  ? 60.686 30.127  -25.307 1.00 47.17  ? 99  THR B O   1 
ATOM   261  C CB  . THR A 1 43  ? 57.991 30.476  -26.066 1.00 35.95  ? 99  THR B CB  1 
ATOM   262  O OG1 . THR A 1 43  ? 56.747 31.092  -26.410 1.00 43.77  ? 99  THR B OG1 1 
ATOM   263  C CG2 . THR A 1 43  ? 57.753 29.021  -25.718 1.00 30.36  ? 99  THR B CG2 1 
ATOM   264  N N   . LEU A 1 44  ? 59.939 30.186  -23.184 1.00 47.31  ? 100 LEU B N   1 
ATOM   265  C CA  . LEU A 1 44  ? 60.936 29.270  -22.677 1.00 49.65  ? 100 LEU B CA  1 
ATOM   266  C C   . LEU A 1 44  ? 60.161 28.191  -21.945 1.00 51.83  ? 100 LEU B C   1 
ATOM   267  O O   . LEU A 1 44  ? 59.657 28.417  -20.847 1.00 50.01  ? 100 LEU B O   1 
ATOM   268  C CB  . LEU A 1 44  ? 61.892 30.015  -21.749 1.00 48.36  ? 100 LEU B CB  1 
ATOM   269  C CG  . LEU A 1 44  ? 62.574 31.189  -22.468 1.00 44.97  ? 100 LEU B CG  1 
ATOM   270  C CD1 . LEU A 1 44  ? 63.424 32.029  -21.533 1.00 43.90  ? 100 LEU B CD1 1 
ATOM   271  C CD2 . LEU A 1 44  ? 63.404 30.689  -23.648 1.00 39.62  ? 100 LEU B CD2 1 
ATOM   272  N N   . SER A 1 45  ? 60.101 27.009  -22.549 1.00 53.29  ? 101 SER B N   1 
ATOM   273  C CA  . SER A 1 45  ? 59.177 25.964  -22.129 1.00 50.22  ? 101 SER B CA  1 
ATOM   274  C C   . SER A 1 45  ? 59.812 24.592  -22.326 1.00 50.12  ? 101 SER B C   1 
ATOM   275  O O   . SER A 1 45  ? 60.480 24.360  -23.331 1.00 49.77  ? 101 SER B O   1 
ATOM   276  C CB  . SER A 1 45  ? 57.884 26.076  -22.937 1.00 51.81  ? 101 SER B CB  1 
ATOM   277  O OG  . SER A 1 45  ? 56.985 25.032  -22.619 1.00 61.51  ? 101 SER B OG  1 
ATOM   278  N N   . SER A 1 46  ? 59.598 23.693  -21.366 1.00 51.59  ? 102 SER B N   1 
ATOM   279  C CA  . SER A 1 46  ? 60.262 22.381  -21.339 1.00 54.38  ? 102 SER B CA  1 
ATOM   280  C C   . SER A 1 46  ? 61.787 22.492  -21.219 1.00 59.34  ? 102 SER B C   1 
ATOM   281  O O   . SER A 1 46  ? 62.529 21.702  -21.810 1.00 61.49  ? 102 SER B O   1 
ATOM   282  C CB  . SER A 1 46  ? 59.883 21.539  -22.562 1.00 49.13  ? 102 SER B CB  1 
ATOM   283  O OG  . SER A 1 46  ? 58.478 21.372  -22.644 1.00 46.87  ? 102 SER B OG  1 
ATOM   284  N N   . LEU A 1 47  ? 62.246 23.507  -20.490 1.00 56.09  ? 103 LEU B N   1 
ATOM   285  C CA  . LEU A 1 47  ? 63.678 23.753  -20.327 1.00 53.90  ? 103 LEU B CA  1 
ATOM   286  C C   . LEU A 1 47  ? 64.330 23.316  -19.002 1.00 52.27  ? 103 LEU B C   1 
ATOM   287  O O   . LEU A 1 47  ? 65.513 23.554  -18.788 1.00 53.65  ? 103 LEU B O   1 
ATOM   288  C CB  . LEU A 1 47  ? 64.001 25.208  -20.670 1.00 51.56  ? 103 LEU B CB  1 
ATOM   289  C CG  . LEU A 1 47  ? 63.580 25.523  -22.108 1.00 41.60  ? 103 LEU B CG  1 
ATOM   290  C CD1 . LEU A 1 47  ? 63.741 26.995  -22.411 1.00 41.09  ? 103 LEU B CD1 1 
ATOM   291  C CD2 . LEU A 1 47  ? 64.374 24.671  -23.087 1.00 39.51  ? 103 LEU B CD2 1 
ATOM   292  N N   . GLN A 1 48  ? 63.554 22.710  -18.111 1.00 50.83  ? 104 GLN B N   1 
ATOM   293  C CA  . GLN A 1 48  ? 64.071 22.211  -16.831 1.00 45.24  ? 104 GLN B CA  1 
ATOM   294  C C   . GLN A 1 48  ? 64.715 23.302  -15.968 1.00 43.25  ? 104 GLN B C   1 
ATOM   295  O O   . GLN A 1 48  ? 65.550 23.015  -15.115 1.00 48.46  ? 104 GLN B O   1 
ATOM   296  C CB  . GLN A 1 48  ? 65.038 21.039  -17.047 1.00 37.98  ? 104 GLN B CB  1 
ATOM   297  N N   . LEU A 1 49  ? 64.308 24.548  -16.186 1.00 39.17  ? 105 LEU B N   1 
ATOM   298  C CA  . LEU A 1 49  ? 64.826 25.680  -15.424 1.00 38.88  ? 105 LEU B CA  1 
ATOM   299  C C   . LEU A 1 49  ? 64.364 25.629  -13.972 1.00 42.31  ? 105 LEU B C   1 
ATOM   300  O O   . LEU A 1 49  ? 63.313 25.068  -13.668 1.00 44.69  ? 105 LEU B O   1 
ATOM   301  C CB  . LEU A 1 49  ? 64.355 26.998  -16.040 1.00 42.75  ? 105 LEU B CB  1 
ATOM   302  C CG  . LEU A 1 49  ? 64.970 27.529  -17.339 1.00 53.02  ? 105 LEU B CG  1 
ATOM   303  C CD1 . LEU A 1 49  ? 65.956 26.556  -17.965 1.00 59.68  ? 105 LEU B CD1 1 
ATOM   304  C CD2 . LEU A 1 49  ? 63.878 27.907  -18.338 1.00 50.73  ? 105 LEU B CD2 1 
ATOM   305  N N   . THR A 1 50  ? 65.141 26.235  -13.078 1.00 45.23  ? 106 THR B N   1 
ATOM   306  C CA  . THR A 1 50  ? 64.763 26.321  -11.671 1.00 36.67  ? 106 THR B CA  1 
ATOM   307  C C   . THR A 1 50  ? 64.792 27.743  -11.126 1.00 37.54  ? 106 THR B C   1 
ATOM   308  O O   . THR A 1 50  ? 65.050 28.713  -11.846 1.00 41.74  ? 106 THR B O   1 
ATOM   309  C CB  . THR A 1 50  ? 65.682 25.471  -10.797 1.00 37.39  ? 106 THR B CB  1 
ATOM   310  O OG1 . THR A 1 50  ? 67.040 25.678  -11.203 1.00 41.73  ? 106 THR B OG1 1 
ATOM   311  C CG2 . THR A 1 50  ? 65.331 23.997  -10.929 1.00 36.18  ? 106 THR B CG2 1 
ATOM   312  N N   . GLY A 1 51  ? 64.518 27.855  -9.835  1.00 37.41  ? 107 GLY B N   1 
ATOM   313  C CA  . GLY A 1 51  ? 64.606 29.129  -9.155  1.00 54.72  ? 107 GLY B CA  1 
ATOM   314  C C   . GLY A 1 51  ? 63.432 30.036  -9.425  1.00 49.62  ? 107 GLY B C   1 
ATOM   315  O O   . GLY A 1 51  ? 62.403 29.609  -9.939  1.00 47.17  ? 107 GLY B O   1 
ATOM   316  N N   . VAL A 1 52  ? 63.596 31.300  -9.064  1.00 51.00  ? 108 VAL B N   1 
ATOM   317  C CA  . VAL A 1 52  ? 62.540 32.287  -9.210  1.00 57.60  ? 108 VAL B CA  1 
ATOM   318  C C   . VAL A 1 52  ? 62.438 32.790  -10.655 1.00 59.21  ? 108 VAL B C   1 
ATOM   319  O O   . VAL A 1 52  ? 63.391 32.692  -11.436 1.00 53.45  ? 108 VAL B O   1 
ATOM   320  C CB  . VAL A 1 52  ? 62.767 33.468  -8.232  1.00 48.11  ? 108 VAL B CB  1 
ATOM   321  C CG1 . VAL A 1 52  ? 61.491 34.272  -8.028  1.00 49.76  ? 108 VAL B CG1 1 
ATOM   322  C CG2 . VAL A 1 52  ? 63.261 32.945  -6.892  1.00 46.96  ? 108 VAL B CG2 1 
ATOM   323  N N   . ILE A 1 53  ? 61.252 33.278  -11.010 1.00 61.90  ? 109 ILE B N   1 
ATOM   324  C CA  . ILE A 1 53  ? 61.070 34.089  -12.208 1.00 64.15  ? 109 ILE B CA  1 
ATOM   325  C C   . ILE A 1 53  ? 61.730 35.433  -11.931 1.00 63.27  ? 109 ILE B C   1 
ATOM   326  O O   . ILE A 1 53  ? 61.313 36.145  -11.015 1.00 58.25  ? 109 ILE B O   1 
ATOM   327  C CB  . ILE A 1 53  ? 59.582 34.358  -12.472 1.00 63.71  ? 109 ILE B CB  1 
ATOM   328  C CG1 . ILE A 1 53  ? 58.813 33.055  -12.663 1.00 60.30  ? 109 ILE B CG1 1 
ATOM   329  C CG2 . ILE A 1 53  ? 59.417 35.272  -13.667 1.00 64.61  ? 109 ILE B CG2 1 
ATOM   330  C CD1 . ILE A 1 53  ? 57.316 33.233  -12.721 1.00 56.37  ? 109 ILE B CD1 1 
ATOM   331  N N   . PRO A 1 54  ? 62.773 35.778  -12.698 1.00 67.56  ? 110 PRO B N   1 
ATOM   332  C CA  . PRO A 1 54  ? 63.471 37.042  -12.462 1.00 70.66  ? 110 PRO B CA  1 
ATOM   333  C C   . PRO A 1 54  ? 62.506 38.208  -12.543 1.00 78.21  ? 110 PRO B C   1 
ATOM   334  O O   . PRO A 1 54  ? 61.754 38.298  -13.512 1.00 79.79  ? 110 PRO B O   1 
ATOM   335  C CB  . PRO A 1 54  ? 64.479 37.130  -13.602 1.00 63.62  ? 110 PRO B CB  1 
ATOM   336  C CG  . PRO A 1 54  ? 64.536 35.805  -14.222 1.00 60.90  ? 110 PRO B CG  1 
ATOM   337  C CD  . PRO A 1 54  ? 63.461 34.930  -13.675 1.00 65.12  ? 110 PRO B CD  1 
ATOM   338  N N   . LYS A 1 55  ? 62.559 39.089  -11.547 1.00 79.99  ? 111 LYS B N   1 
ATOM   339  C CA  . LYS A 1 55  ? 61.695 40.261  -11.458 1.00 81.94  ? 111 LYS B CA  1 
ATOM   340  C C   . LYS A 1 55  ? 61.938 41.231  -12.625 1.00 85.02  ? 111 LYS B C   1 
ATOM   341  O O   . LYS A 1 55  ? 61.198 42.198  -12.819 1.00 85.56  ? 111 LYS B O   1 
ATOM   342  C CB  . LYS A 1 55  ? 61.906 40.949  -10.102 1.00 84.04  ? 111 LYS B CB  1 
ATOM   343  C CG  . LYS A 1 55  ? 61.665 40.006  -8.910  1.00 80.31  ? 111 LYS B CG  1 
ATOM   344  C CD  . LYS A 1 55  ? 62.083 40.589  -7.563  1.00 74.77  ? 111 LYS B CD  1 
ATOM   345  C CE  . LYS A 1 55  ? 63.584 40.486  -7.348  1.00 74.76  ? 111 LYS B CE  1 
ATOM   346  N NZ  . LYS A 1 55  ? 64.077 39.086  -7.466  1.00 73.41  ? 111 LYS B NZ  1 
ATOM   347  N N   . GLU A 1 56  ? 62.976 40.952  -13.408 1.00 87.43  ? 112 GLU B N   1 
ATOM   348  C CA  . GLU A 1 56  ? 63.333 41.765  -14.564 1.00 88.93  ? 112 GLU B CA  1 
ATOM   349  C C   . GLU A 1 56  ? 62.507 41.371  -15.776 1.00 90.56  ? 112 GLU B C   1 
ATOM   350  O O   . GLU A 1 56  ? 62.719 41.888  -16.870 1.00 92.76  ? 112 GLU B O   1 
ATOM   351  C CB  . GLU A 1 56  ? 64.816 41.604  -14.905 1.00 90.34  ? 112 GLU B CB  1 
ATOM   352  C CG  . GLU A 1 56  ? 65.766 42.015  -13.801 1.00 93.13  ? 112 GLU B CG  1 
ATOM   353  C CD  . GLU A 1 56  ? 66.778 40.934  -13.488 1.00 95.27  ? 112 GLU B CD  1 
ATOM   354  O OE1 . GLU A 1 56  ? 66.841 39.941  -14.246 1.00 94.05  ? 112 GLU B OE1 1 
ATOM   355  O OE2 . GLU A 1 56  ? 67.505 41.074  -12.481 1.00 97.76  ? 112 GLU B OE2 1 
ATOM   356  N N   . ILE A 1 57  ? 61.587 40.432  -15.591 1.00 89.06  ? 113 ILE B N   1 
ATOM   357  C CA  . ILE A 1 57  ? 60.719 40.011  -16.686 1.00 85.79  ? 113 ILE B CA  1 
ATOM   358  C C   . ILE A 1 57  ? 59.870 41.186  -17.175 1.00 80.96  ? 113 ILE B C   1 
ATOM   359  O O   . ILE A 1 57  ? 59.473 41.231  -18.340 1.00 80.21  ? 113 ILE B O   1 
ATOM   360  C CB  . ILE A 1 57  ? 59.835 38.797  -16.295 1.00 59.10  ? 113 ILE B CB  1 
ATOM   361  C CG1 . ILE A 1 57  ? 60.039 37.637  -17.284 1.00 52.56  ? 113 ILE B CG1 1 
ATOM   362  C CG2 . ILE A 1 57  ? 58.370 39.198  -16.158 1.00 53.07  ? 113 ILE B CG2 1 
ATOM   363  C CD1 . ILE A 1 57  ? 60.061 38.051  -18.732 1.00 48.67  ? 113 ILE B CD1 1 
ATOM   364  N N   . GLY A 1 58  ? 59.617 42.148  -16.291 1.00 78.57  ? 114 GLY B N   1 
ATOM   365  C CA  . GLY A 1 58  ? 58.919 43.362  -16.671 1.00 79.13  ? 114 GLY B CA  1 
ATOM   366  C C   . GLY A 1 58  ? 59.709 44.231  -17.642 1.00 81.04  ? 114 GLY B C   1 
ATOM   367  O O   . GLY A 1 58  ? 59.134 45.108  -18.292 1.00 78.64  ? 114 GLY B O   1 
ATOM   368  N N   . ASP A 1 59  ? 61.018 43.982  -17.748 1.00 82.96  ? 115 ASP B N   1 
ATOM   369  C CA  . ASP A 1 59  ? 61.913 44.777  -18.604 1.00 81.62  ? 115 ASP B CA  1 
ATOM   370  C C   . ASP A 1 59  ? 61.627 44.658  -20.103 1.00 84.20  ? 115 ASP B C   1 
ATOM   371  O O   . ASP A 1 59  ? 62.157 45.439  -20.898 1.00 91.04  ? 115 ASP B O   1 
ATOM   372  C CB  . ASP A 1 59  ? 63.390 44.449  -18.349 1.00 78.50  ? 115 ASP B CB  1 
ATOM   373  C CG  . ASP A 1 59  ? 63.862 44.893  -16.982 1.00 79.98  ? 115 ASP B CG  1 
ATOM   374  O OD1 . ASP A 1 59  ? 63.088 45.575  -16.273 1.00 81.51  ? 115 ASP B OD1 1 
ATOM   375  O OD2 . ASP A 1 59  ? 65.016 44.568  -16.623 1.00 79.51  ? 115 ASP B OD2 1 
ATOM   376  N N   . PHE A 1 60  ? 60.812 43.683  -20.497 1.00 76.06  ? 116 PHE B N   1 
ATOM   377  C CA  . PHE A 1 60  ? 60.331 43.655  -21.870 1.00 66.36  ? 116 PHE B CA  1 
ATOM   378  C C   . PHE A 1 60  ? 58.901 44.174  -21.843 1.00 61.34  ? 116 PHE B C   1 
ATOM   379  O O   . PHE A 1 60  ? 57.970 43.437  -21.537 1.00 59.39  ? 116 PHE B O   1 
ATOM   380  C CB  . PHE A 1 60  ? 60.325 42.226  -22.414 1.00 60.72  ? 116 PHE B CB  1 
ATOM   381  C CG  . PHE A 1 60  ? 61.529 41.407  -22.024 1.00 63.39  ? 116 PHE B CG  1 
ATOM   382  C CD1 . PHE A 1 60  ? 61.548 40.691  -20.832 1.00 64.25  ? 116 PHE B CD1 1 
ATOM   383  C CD2 . PHE A 1 60  ? 62.626 41.321  -22.869 1.00 63.67  ? 116 PHE B CD2 1 
ATOM   384  C CE1 . PHE A 1 60  ? 62.645 39.925  -20.484 1.00 63.98  ? 116 PHE B CE1 1 
ATOM   385  C CE2 . PHE A 1 60  ? 63.726 40.559  -22.528 1.00 60.65  ? 116 PHE B CE2 1 
ATOM   386  C CZ  . PHE A 1 60  ? 63.736 39.860  -21.337 1.00 63.18  ? 116 PHE B CZ  1 
ATOM   387  N N   . THR A 1 61  ? 58.710 45.419  -22.250 1.00 62.39  ? 117 THR B N   1 
ATOM   388  C CA  . THR A 1 61  ? 57.422 46.067  -22.053 1.00 59.08  ? 117 THR B CA  1 
ATOM   389  C C   . THR A 1 61  ? 56.513 45.793  -23.240 1.00 51.28  ? 117 THR B C   1 
ATOM   390  O O   . THR A 1 61  ? 55.348 46.197  -23.253 1.00 44.19  ? 117 THR B O   1 
ATOM   391  C CB  . THR A 1 61  ? 57.585 47.586  -21.803 1.00 61.00  ? 117 THR B CB  1 
ATOM   392  O OG1 . THR A 1 61  ? 58.513 48.137  -22.748 1.00 60.37  ? 117 THR B OG1 1 
ATOM   393  C CG2 . THR A 1 61  ? 58.109 47.836  -20.389 1.00 59.13  ? 117 THR B CG2 1 
ATOM   394  N N   . GLU A 1 62  ? 57.070 45.093  -24.228 1.00 51.95  ? 118 GLU B N   1 
ATOM   395  C CA  . GLU A 1 62  ? 56.390 44.796  -25.486 1.00 49.42  ? 118 GLU B CA  1 
ATOM   396  C C   . GLU A 1 62  ? 55.733 43.411  -25.602 1.00 45.88  ? 118 GLU B C   1 
ATOM   397  O O   . GLU A 1 62  ? 55.220 43.052  -26.655 1.00 42.07  ? 118 GLU B O   1 
ATOM   398  C CB  . GLU A 1 62  ? 57.352 45.033  -26.650 1.00 57.71  ? 118 GLU B CB  1 
ATOM   399  C CG  . GLU A 1 62  ? 56.830 46.052  -27.655 1.00 59.01  ? 118 GLU B CG  1 
ATOM   400  C CD  . GLU A 1 62  ? 56.259 47.288  -26.976 1.00 52.40  ? 118 GLU B CD  1 
ATOM   401  O OE1 . GLU A 1 62  ? 56.927 47.838  -26.069 1.00 45.26  ? 118 GLU B OE1 1 
ATOM   402  O OE2 . GLU A 1 62  ? 55.137 47.702  -27.348 1.00 52.23  ? 118 GLU B OE2 1 
ATOM   403  N N   . LEU A 1 63  ? 55.757 42.633  -24.529 1.00 54.34  ? 119 LEU B N   1 
ATOM   404  C CA  . LEU A 1 63  ? 55.333 41.236  -24.591 1.00 49.63  ? 119 LEU B CA  1 
ATOM   405  C C   . LEU A 1 63  ? 53.816 41.063  -24.647 1.00 46.70  ? 119 LEU B C   1 
ATOM   406  O O   . LEU A 1 63  ? 53.105 41.535  -23.765 1.00 50.26  ? 119 LEU B O   1 
ATOM   407  C CB  . LEU A 1 63  ? 55.884 40.494  -23.376 1.00 44.04  ? 119 LEU B CB  1 
ATOM   408  C CG  . LEU A 1 63  ? 56.545 39.143  -23.628 1.00 48.56  ? 119 LEU B CG  1 
ATOM   409  C CD1 . LEU A 1 63  ? 57.557 39.247  -24.742 1.00 46.42  ? 119 LEU B CD1 1 
ATOM   410  C CD2 . LEU A 1 63  ? 57.220 38.663  -22.350 1.00 53.44  ? 119 LEU B CD2 1 
ATOM   411  N N   . GLU A 1 64  ? 53.322 40.416  -25.701 1.00 38.64  ? 120 GLU B N   1 
ATOM   412  C CA  . GLU A 1 64  ? 51.934 39.965  -25.736 1.00 33.54  ? 120 GLU B CA  1 
ATOM   413  C C   . GLU A 1 64  ? 51.777 38.528  -25.255 1.00 32.11  ? 120 GLU B C   1 
ATOM   414  O O   . GLU A 1 64  ? 50.671 38.084  -24.955 1.00 30.92  ? 120 GLU B O   1 
ATOM   415  C CB  . GLU A 1 64  ? 51.382 40.046  -27.158 1.00 42.26  ? 120 GLU B CB  1 
ATOM   416  C CG  . GLU A 1 64  ? 51.563 41.378  -27.847 1.00 47.81  ? 120 GLU B CG  1 
ATOM   417  C CD  . GLU A 1 64  ? 50.788 41.445  -29.137 1.00 55.21  ? 120 GLU B CD  1 
ATOM   418  O OE1 . GLU A 1 64  ? 50.155 40.427  -29.508 1.00 54.45  ? 120 GLU B OE1 1 
ATOM   419  O OE2 . GLU A 1 64  ? 50.801 42.518  -29.774 1.00 62.45  ? 120 GLU B OE2 1 
ATOM   420  N N   . LEU A 1 65  ? 52.884 37.796  -25.192 1.00 36.86  ? 121 LEU B N   1 
ATOM   421  C CA  . LEU A 1 65  ? 52.836 36.388  -24.827 1.00 27.58  ? 121 LEU B CA  1 
ATOM   422  C C   . LEU A 1 65  ? 54.006 36.008  -23.956 1.00 31.77  ? 121 LEU B C   1 
ATOM   423  O O   . LEU A 1 65  ? 55.156 36.214  -24.336 1.00 32.40  ? 121 LEU B O   1 
ATOM   424  C CB  . LEU A 1 65  ? 52.834 35.495  -26.072 1.00 34.94  ? 121 LEU B CB  1 
ATOM   425  C CG  . LEU A 1 65  ? 53.001 33.991  -25.790 1.00 36.83  ? 121 LEU B CG  1 
ATOM   426  C CD1 . LEU A 1 65  ? 51.957 33.138  -26.506 1.00 29.45  ? 121 LEU B CD1 1 
ATOM   427  C CD2 . LEU A 1 65  ? 54.402 33.498  -26.127 1.00 36.68  ? 121 LEU B CD2 1 
ATOM   428  N N   . LEU A 1 66  ? 53.718 35.421  -22.798 1.00 39.60  ? 122 LEU B N   1 
ATOM   429  C CA  . LEU A 1 66  ? 54.770 34.844  -21.970 1.00 39.41  ? 122 LEU B CA  1 
ATOM   430  C C   . LEU A 1 66  ? 54.418 33.394  -21.699 1.00 32.92  ? 122 LEU B C   1 
ATOM   431  O O   . LEU A 1 66  ? 53.428 33.110  -21.037 1.00 37.36  ? 122 LEU B O   1 
ATOM   432  C CB  . LEU A 1 66  ? 54.923 35.616  -20.658 1.00 36.54  ? 122 LEU B CB  1 
ATOM   433  C CG  . LEU A 1 66  ? 56.118 35.219  -19.784 1.00 38.32  ? 122 LEU B CG  1 
ATOM   434  C CD1 . LEU A 1 66  ? 57.396 35.247  -20.604 1.00 34.46  ? 122 LEU B CD1 1 
ATOM   435  C CD2 . LEU A 1 66  ? 56.246 36.116  -18.555 1.00 31.80  ? 122 LEU B CD2 1 
ATOM   436  N N   . ASP A 1 67  ? 55.206 32.475  -22.243 1.00 29.72  ? 123 ASP B N   1 
ATOM   437  C CA  . ASP A 1 67  ? 55.005 31.061  -21.963 1.00 34.43  ? 123 ASP B CA  1 
ATOM   438  C C   . ASP A 1 67  ? 56.212 30.510  -21.223 1.00 40.98  ? 123 ASP B C   1 
ATOM   439  O O   . ASP A 1 67  ? 57.253 30.246  -21.823 1.00 49.18  ? 123 ASP B O   1 
ATOM   440  C CB  . ASP A 1 67  ? 54.809 30.303  -23.281 1.00 43.45  ? 123 ASP B CB  1 
ATOM   441  C CG  . ASP A 1 67  ? 54.738 28.796  -23.095 1.00 47.13  ? 123 ASP B CG  1 
ATOM   442  O OD1 . ASP A 1 67  ? 54.318 28.338  -22.011 1.00 45.82  ? 123 ASP B OD1 1 
ATOM   443  O OD2 . ASP A 1 67  ? 55.100 28.068  -24.044 1.00 47.43  ? 123 ASP B OD2 1 
ATOM   444  N N   . LEU A 1 68  ? 56.060 30.324  -19.919 1.00 42.34  ? 124 LEU B N   1 
ATOM   445  C CA  . LEU A 1 68  ? 57.097 29.709  -19.097 1.00 40.40  ? 124 LEU B CA  1 
ATOM   446  C C   . LEU A 1 68  ? 56.828 28.244  -18.755 1.00 39.18  ? 124 LEU B C   1 
ATOM   447  O O   . LEU A 1 68  ? 57.558 27.643  -17.969 1.00 41.29  ? 124 LEU B O   1 
ATOM   448  C CB  . LEU A 1 68  ? 57.412 30.559  -17.864 1.00 38.61  ? 124 LEU B CB  1 
ATOM   449  C CG  . LEU A 1 68  ? 58.073 31.881  -18.277 1.00 40.53  ? 124 LEU B CG  1 
ATOM   450  C CD1 . LEU A 1 68  ? 58.438 32.744  -17.072 1.00 32.39  ? 124 LEU B CD1 1 
ATOM   451  C CD2 . LEU A 1 68  ? 59.290 31.625  -19.168 1.00 32.52  ? 124 LEU B CD2 1 
ATOM   452  N N   . SER A 1 69  ? 55.769 27.691  -19.340 1.00 40.37  ? 125 SER B N   1 
ATOM   453  C CA  . SER A 1 69  ? 55.197 26.412  -18.900 1.00 42.12  ? 125 SER B CA  1 
ATOM   454  C C   . SER A 1 69  ? 56.151 25.213  -18.897 1.00 36.37  ? 125 SER B C   1 
ATOM   455  O O   . SER A 1 69  ? 57.114 25.167  -19.662 1.00 30.16  ? 125 SER B O   1 
ATOM   456  C CB  . SER A 1 69  ? 53.937 26.074  -19.714 1.00 37.62  ? 125 SER B CB  1 
ATOM   457  O OG  . SER A 1 69  ? 54.260 25.575  -21.002 1.00 32.18  ? 125 SER B OG  1 
ATOM   458  N N   . ASP A 1 70  ? 55.874 24.260  -18.008 1.00 33.84  ? 126 ASP B N   1 
ATOM   459  C CA  . ASP A 1 70  ? 56.619 23.003  -17.941 1.00 38.69  ? 126 ASP B CA  1 
ATOM   460  C C   . ASP A 1 70  ? 58.114 23.183  -17.647 1.00 46.21  ? 126 ASP B C   1 
ATOM   461  O O   . ASP A 1 70  ? 58.969 22.848  -18.468 1.00 52.55  ? 126 ASP B O   1 
ATOM   462  C CB  . ASP A 1 70  ? 56.436 22.207  -19.239 1.00 37.79  ? 126 ASP B CB  1 
ATOM   463  C CG  . ASP A 1 70  ? 56.826 20.751  -19.085 1.00 40.98  ? 126 ASP B CG  1 
ATOM   464  O OD1 . ASP A 1 70  ? 56.638 20.209  -17.967 1.00 39.30  ? 126 ASP B OD1 1 
ATOM   465  O OD2 . ASP A 1 70  ? 57.318 20.156  -20.076 1.00 36.84  ? 126 ASP B OD2 1 
ATOM   466  N N   . ASN A 1 71  ? 58.410 23.703  -16.461 1.00 45.81  ? 127 ASN B N   1 
ATOM   467  C CA  . ASN A 1 71  ? 59.774 23.840  -15.965 1.00 49.58  ? 127 ASN B CA  1 
ATOM   468  C C   . ASN A 1 71  ? 59.711 23.438  -14.508 1.00 56.15  ? 127 ASN B C   1 
ATOM   469  O O   . ASN A 1 71  ? 58.707 22.890  -14.051 1.00 55.34  ? 127 ASN B O   1 
ATOM   470  C CB  . ASN A 1 71  ? 60.273 25.289  -16.042 1.00 48.88  ? 127 ASN B CB  1 
ATOM   471  C CG  . ASN A 1 71  ? 60.468 25.781  -17.466 1.00 56.63  ? 127 ASN B CG  1 
ATOM   472  O OD1 . ASN A 1 71  ? 60.985 25.066  -18.330 1.00 58.78  ? 127 ASN B OD1 1 
ATOM   473  N ND2 . ASN A 1 71  ? 60.056 27.021  -17.716 1.00 59.59  ? 127 ASN B ND2 1 
ATOM   474  N N   . SER A 1 72  ? 60.797 23.668  -13.785 1.00 56.87  ? 128 SER B N   1 
ATOM   475  C CA  . SER A 1 72  ? 60.773 23.536  -12.338 1.00 46.41  ? 128 SER B CA  1 
ATOM   476  C C   . SER A 1 72  ? 60.634 24.852  -11.584 1.00 31.06  ? 128 SER B C   1 
ATOM   477  O O   . SER A 1 72  ? 60.670 24.853  -10.365 1.00 47.77  ? 128 SER B O   1 
ATOM   478  C CB  . SER A 1 72  ? 61.977 22.740  -11.854 1.00 43.08  ? 128 SER B CB  1 
ATOM   479  O OG  . SER A 1 72  ? 61.842 21.389  -12.249 1.00 43.07  ? 128 SER B OG  1 
ATOM   480  N N   . LEU A 1 73  ? 60.456 25.957  -12.300 1.00 45.35  ? 129 LEU B N   1 
ATOM   481  C CA  . LEU A 1 73  ? 60.547 27.300  -11.708 1.00 50.16  ? 129 LEU B CA  1 
ATOM   482  C C   . LEU A 1 73  ? 59.766 27.497  -10.396 1.00 50.94  ? 129 LEU B C   1 
ATOM   483  O O   . LEU A 1 73  ? 58.667 26.969  -10.228 1.00 50.24  ? 129 LEU B O   1 
ATOM   484  C CB  . LEU A 1 73  ? 60.162 28.363  -12.735 1.00 47.87  ? 129 LEU B CB  1 
ATOM   485  C CG  . LEU A 1 73  ? 61.097 28.340  -13.945 1.00 55.11  ? 129 LEU B CG  1 
ATOM   486  C CD1 . LEU A 1 73  ? 60.599 29.221  -15.080 1.00 56.07  ? 129 LEU B CD1 1 
ATOM   487  C CD2 . LEU A 1 73  ? 62.481 28.770  -13.524 1.00 59.22  ? 129 LEU B CD2 1 
ATOM   488  N N   . SER A 1 74  ? 60.370 28.229  -9.458  1.00 51.79  ? 130 SER B N   1 
ATOM   489  C CA  . SER A 1 74  ? 59.886 28.289  -8.075  1.00 49.24  ? 130 SER B CA  1 
ATOM   490  C C   . SER A 1 74  ? 59.625 29.711  -7.564  1.00 50.75  ? 130 SER B C   1 
ATOM   491  O O   . SER A 1 74  ? 59.662 30.681  -8.323  1.00 33.62  ? 130 SER B O   1 
ATOM   492  C CB  . SER A 1 74  ? 60.877 27.580  -7.138  1.00 42.30  ? 130 SER B CB  1 
ATOM   493  O OG  . SER A 1 74  ? 61.754 26.717  -7.855  1.00 37.89  ? 130 SER B OG  1 
ATOM   494  N N   . GLY A 1 75  ? 59.347 29.821  -6.270  1.00 33.05  ? 131 GLY B N   1 
ATOM   495  C CA  . GLY A 1 75  ? 59.110 31.110  -5.644  1.00 50.92  ? 131 GLY B CA  1 
ATOM   496  C C   . GLY A 1 75  ? 57.791 31.737  -6.044  1.00 47.10  ? 131 GLY B C   1 
ATOM   497  O O   . GLY A 1 75  ? 56.982 31.103  -6.715  1.00 51.07  ? 131 GLY B O   1 
ATOM   498  N N   . ASP A 1 76  ? 57.576 32.986  -5.637  1.00 43.08  ? 132 ASP B N   1 
ATOM   499  C CA  . ASP A 1 76  ? 56.347 33.699  -5.974  1.00 50.18  ? 132 ASP B CA  1 
ATOM   500  C C   . ASP A 1 76  ? 56.306 34.132  -7.445  1.00 53.71  ? 132 ASP B C   1 
ATOM   501  O O   . ASP A 1 76  ? 57.271 33.953  -8.203  1.00 47.70  ? 132 ASP B O   1 
ATOM   502  C CB  . ASP A 1 76  ? 56.185 34.942  -5.090  1.00 58.55  ? 132 ASP B CB  1 
ATOM   503  C CG  . ASP A 1 76  ? 55.788 34.610  -3.659  1.00 62.44  ? 132 ASP B CG  1 
ATOM   504  O OD1 . ASP A 1 76  ? 56.359 33.669  -3.067  1.00 69.45  ? 132 ASP B OD1 1 
ATOM   505  O OD2 . ASP A 1 76  ? 54.904 35.309  -3.118  1.00 58.36  ? 132 ASP B OD2 1 
ATOM   506  N N   . ILE A 1 77  ? 55.182 34.722  -7.837  1.00 57.44  ? 133 ILE B N   1 
ATOM   507  C CA  . ILE A 1 77  ? 55.040 35.297  -9.169  1.00 54.54  ? 133 ILE B CA  1 
ATOM   508  C C   . ILE A 1 77  ? 55.299 36.800  -9.086  1.00 53.03  ? 133 ILE B C   1 
ATOM   509  O O   . ILE A 1 77  ? 54.475 37.542  -8.548  1.00 32.31  ? 133 ILE B O   1 
ATOM   510  C CB  . ILE A 1 77  ? 53.632 35.029  -9.752  1.00 46.33  ? 133 ILE B CB  1 
ATOM   511  C CG1 . ILE A 1 77  ? 53.450 33.537  -10.031 1.00 41.74  ? 133 ILE B CG1 1 
ATOM   512  C CG2 . ILE A 1 77  ? 53.415 35.824  -11.030 1.00 51.12  ? 133 ILE B CG2 1 
ATOM   513  C CD1 . ILE A 1 77  ? 52.032 33.151  -10.367 1.00 26.60  ? 133 ILE B CD1 1 
ATOM   514  N N   . PRO A 1 78  ? 56.444 37.250  -9.630  1.00 47.24  ? 134 PRO B N   1 
ATOM   515  C CA  . PRO A 1 78  ? 56.867 38.643  -9.465  1.00 43.34  ? 134 PRO B CA  1 
ATOM   516  C C   . PRO A 1 78  ? 55.751 39.560  -9.897  1.00 46.78  ? 134 PRO B C   1 
ATOM   517  O O   . PRO A 1 78  ? 55.273 39.412  -11.013 1.00 48.52  ? 134 PRO B O   1 
ATOM   518  C CB  . PRO A 1 78  ? 58.038 38.762  -10.436 1.00 39.02  ? 134 PRO B CB  1 
ATOM   519  C CG  . PRO A 1 78  ? 58.572 37.384  -10.538 1.00 41.45  ? 134 PRO B CG  1 
ATOM   520  C CD  . PRO A 1 78  ? 57.379 36.489  -10.476 1.00 46.46  ? 134 PRO B CD  1 
ATOM   521  N N   . VAL A 1 79  ? 55.355 40.492  -9.034  1.00 52.72  ? 135 VAL B N   1 
ATOM   522  C CA  . VAL A 1 79  ? 54.117 41.247  -9.224  1.00 61.03  ? 135 VAL B CA  1 
ATOM   523  C C   . VAL A 1 79  ? 54.205 42.123  -10.473 1.00 63.36  ? 135 VAL B C   1 
ATOM   524  O O   . VAL A 1 79  ? 53.194 42.467  -11.097 1.00 61.50  ? 135 VAL B O   1 
ATOM   525  C CB  . VAL A 1 79  ? 53.788 42.096  -7.971  1.00 63.63  ? 135 VAL B CB  1 
ATOM   526  C CG1 . VAL A 1 79  ? 52.446 42.793  -8.119  1.00 60.78  ? 135 VAL B CG1 1 
ATOM   527  C CG2 . VAL A 1 79  ? 53.788 41.216  -6.724  1.00 69.70  ? 135 VAL B CG2 1 
ATOM   528  N N   . GLU A 1 80  ? 55.440 42.436  -10.849 1.00 57.90  ? 136 GLU B N   1 
ATOM   529  C CA  . GLU A 1 80  ? 55.728 43.293  -11.982 1.00 55.57  ? 136 GLU B CA  1 
ATOM   530  C C   . GLU A 1 80  ? 55.515 42.566  -13.317 1.00 58.86  ? 136 GLU B C   1 
ATOM   531  O O   . GLU A 1 80  ? 55.492 43.192  -14.383 1.00 62.18  ? 136 GLU B O   1 
ATOM   532  C CB  . GLU A 1 80  ? 57.151 43.837  -11.855 1.00 58.45  ? 136 GLU B CB  1 
ATOM   533  C CG  . GLU A 1 80  ? 57.392 44.670  -10.581 1.00 59.36  ? 136 GLU B CG  1 
ATOM   534  C CD  . GLU A 1 80  ? 57.640 43.834  -9.321  1.00 54.34  ? 136 GLU B CD  1 
ATOM   535  O OE1 . GLU A 1 80  ? 58.810 43.775  -8.881  1.00 51.88  ? 136 GLU B OE1 1 
ATOM   536  O OE2 . GLU A 1 80  ? 56.670 43.249  -8.774  1.00 44.77  ? 136 GLU B OE2 1 
ATOM   537  N N   . ILE A 1 81  ? 55.339 41.245  -13.248 1.00 54.78  ? 137 ILE B N   1 
ATOM   538  C CA  . ILE A 1 81  ? 54.908 40.455  -14.399 1.00 52.68  ? 137 ILE B CA  1 
ATOM   539  C C   . ILE A 1 81  ? 53.514 40.929  -14.796 1.00 51.08  ? 137 ILE B C   1 
ATOM   540  O O   . ILE A 1 81  ? 53.084 40.747  -15.931 1.00 50.19  ? 137 ILE B O   1 
ATOM   541  C CB  . ILE A 1 81  ? 54.880 38.933  -14.080 1.00 43.22  ? 137 ILE B CB  1 
ATOM   542  C CG1 . ILE A 1 81  ? 55.271 38.097  -15.296 1.00 42.17  ? 137 ILE B CG1 1 
ATOM   543  C CG2 . ILE A 1 81  ? 53.507 38.487  -13.603 1.00 31.03  ? 137 ILE B CG2 1 
ATOM   544  C CD1 . ILE A 1 81  ? 55.358 36.601  -15.009 1.00 36.13  ? 137 ILE B CD1 1 
ATOM   545  N N   . PHE A 1 82  ? 52.825 41.550  -13.844 1.00 54.80  ? 138 PHE B N   1 
ATOM   546  C CA  . PHE A 1 82  ? 51.497 42.107  -14.057 1.00 65.86  ? 138 PHE B CA  1 
ATOM   547  C C   . PHE A 1 82  ? 51.553 43.581  -14.438 1.00 67.82  ? 138 PHE B C   1 
ATOM   548  O O   . PHE A 1 82  ? 50.528 44.264  -14.454 1.00 66.32  ? 138 PHE B O   1 
ATOM   549  C CB  . PHE A 1 82  ? 50.619 41.897  -12.826 1.00 75.92  ? 138 PHE B CB  1 
ATOM   550  C CG  . PHE A 1 82  ? 50.557 40.474  -12.389 1.00 81.92  ? 138 PHE B CG  1 
ATOM   551  C CD1 . PHE A 1 82  ? 49.695 39.585  -13.003 1.00 83.32  ? 138 PHE B CD1 1 
ATOM   552  C CD2 . PHE A 1 82  ? 51.382 40.015  -11.384 1.00 85.94  ? 138 PHE B CD2 1 
ATOM   553  C CE1 . PHE A 1 82  ? 49.651 38.265  -12.610 1.00 83.88  ? 138 PHE B CE1 1 
ATOM   554  C CE2 . PHE A 1 82  ? 51.346 38.700  -10.995 1.00 87.93  ? 138 PHE B CE2 1 
ATOM   555  C CZ  . PHE A 1 82  ? 50.476 37.822  -11.601 1.00 86.05  ? 138 PHE B CZ  1 
ATOM   556  N N   . ARG A 1 83  ? 52.758 44.083  -14.684 1.00 67.84  ? 139 ARG B N   1 
ATOM   557  C CA  . ARG A 1 83  ? 52.906 45.431  -15.220 1.00 65.28  ? 139 ARG B CA  1 
ATOM   558  C C   . ARG A 1 83  ? 52.932 45.448  -16.744 1.00 62.19  ? 139 ARG B C   1 
ATOM   559  O O   . ARG A 1 83  ? 53.147 46.500  -17.341 1.00 70.51  ? 139 ARG B O   1 
ATOM   560  C CB  . ARG A 1 83  ? 54.151 46.125  -14.663 1.00 62.25  ? 139 ARG B CB  1 
ATOM   561  C CG  . ARG A 1 83  ? 54.123 46.299  -13.163 1.00 57.03  ? 139 ARG B CG  1 
ATOM   562  C CD  . ARG A 1 83  ? 54.293 47.747  -12.741 1.00 57.25  ? 139 ARG B CD  1 
ATOM   563  N NE  . ARG A 1 83  ? 54.514 47.802  -11.302 1.00 57.33  ? 139 ARG B NE  1 
ATOM   564  C CZ  . ARG A 1 83  ? 55.712 47.826  -10.723 1.00 54.15  ? 139 ARG B CZ  1 
ATOM   565  N NH1 . ARG A 1 83  ? 56.819 47.831  -11.456 1.00 49.83  ? 139 ARG B NH1 1 
ATOM   566  N NH2 . ARG A 1 83  ? 55.801 47.849  -9.402  1.00 54.76  ? 139 ARG B NH2 1 
ATOM   567  N N   . LEU A 1 84  ? 52.723 44.294  -17.374 1.00 53.93  ? 140 LEU B N   1 
ATOM   568  C CA  . LEU A 1 84  ? 52.735 44.233  -18.834 1.00 52.42  ? 140 LEU B CA  1 
ATOM   569  C C   . LEU A 1 84  ? 51.318 44.180  -19.383 1.00 61.94  ? 140 LEU B C   1 
ATOM   570  O O   . LEU A 1 84  ? 50.696 43.118  -19.392 1.00 69.81  ? 140 LEU B O   1 
ATOM   571  C CB  . LEU A 1 84  ? 53.461 42.970  -19.276 1.00 43.80  ? 140 LEU B CB  1 
ATOM   572  C CG  . LEU A 1 84  ? 54.639 42.548  -18.410 1.00 39.52  ? 140 LEU B CG  1 
ATOM   573  C CD1 . LEU A 1 84  ? 54.872 41.063  -18.534 1.00 38.94  ? 140 LEU B CD1 1 
ATOM   574  C CD2 . LEU A 1 84  ? 55.865 43.318  -18.838 1.00 43.51  ? 140 LEU B CD2 1 
ATOM   575  N N   . LYS A 1 85  ? 50.842 45.301  -19.921 1.00 62.61  ? 141 LYS B N   1 
ATOM   576  C CA  . LYS A 1 85  ? 49.430 45.433  -20.275 1.00 60.34  ? 141 LYS B CA  1 
ATOM   577  C C   . LYS A 1 85  ? 49.173 45.094  -21.738 1.00 61.83  ? 141 LYS B C   1 
ATOM   578  O O   . LYS A 1 85  ? 48.054 45.236  -22.241 1.00 67.13  ? 141 LYS B O   1 
ATOM   579  C CB  . LYS A 1 85  ? 48.906 46.834  -19.936 1.00 57.59  ? 141 LYS B CB  1 
ATOM   580  C CG  . LYS A 1 85  ? 47.393 46.908  -19.731 1.00 53.52  ? 141 LYS B CG  1 
ATOM   581  C CD  . LYS A 1 85  ? 46.900 48.348  -19.788 1.00 56.47  ? 141 LYS B CD  1 
ATOM   582  C CE  . LYS A 1 85  ? 47.605 49.230  -18.760 1.00 60.79  ? 141 LYS B CE  1 
ATOM   583  N NZ  . LYS A 1 85  ? 47.195 48.924  -17.349 1.00 64.34  ? 141 LYS B NZ  1 
ATOM   584  N N   . LYS A 1 86  ? 50.215 44.668  -22.436 1.00 59.28  ? 142 LYS B N   1 
ATOM   585  C CA  . LYS A 1 86  ? 50.012 44.143  -23.780 1.00 63.32  ? 142 LYS B CA  1 
ATOM   586  C C   . LYS A 1 86  ? 49.945 42.617  -23.797 1.00 48.05  ? 142 LYS B C   1 
ATOM   587  O O   . LYS A 1 86  ? 49.792 42.011  -24.857 1.00 43.01  ? 142 LYS B O   1 
ATOM   588  C CB  . LYS A 1 86  ? 51.067 44.673  -24.759 1.00 76.96  ? 142 LYS B CB  1 
ATOM   589  C CG  . LYS A 1 86  ? 50.945 46.170  -25.027 1.00 80.77  ? 142 LYS B CG  1 
ATOM   590  C CD  . LYS A 1 86  ? 51.834 46.634  -26.165 1.00 83.99  ? 142 LYS B CD  1 
ATOM   591  C CE  . LYS A 1 86  ? 51.617 48.117  -26.433 1.00 89.27  ? 142 LYS B CE  1 
ATOM   592  N NZ  . LYS A 1 86  ? 52.340 48.577  -27.650 1.00 94.77  ? 142 LYS B NZ  1 
ATOM   593  N N   . LEU A 1 87  ? 50.031 42.005  -22.616 1.00 35.54  ? 143 LEU B N   1 
ATOM   594  C CA  . LEU A 1 87  ? 50.106 40.556  -22.522 1.00 29.22  ? 143 LEU B CA  1 
ATOM   595  C C   . LEU A 1 87  ? 48.717 39.959  -22.758 1.00 30.51  ? 143 LEU B C   1 
ATOM   596  O O   . LEU A 1 87  ? 47.775 40.259  -22.034 1.00 30.09  ? 143 LEU B O   1 
ATOM   597  C CB  . LEU A 1 87  ? 50.636 40.165  -21.147 1.00 27.99  ? 143 LEU B CB  1 
ATOM   598  C CG  . LEU A 1 87  ? 51.228 38.771  -20.962 1.00 50.10  ? 143 LEU B CG  1 
ATOM   599  C CD1 . LEU A 1 87  ? 52.484 38.588  -21.787 1.00 50.85  ? 143 LEU B CD1 1 
ATOM   600  C CD2 . LEU A 1 87  ? 51.535 38.550  -19.497 1.00 47.58  ? 143 LEU B CD2 1 
ATOM   601  N N   . LYS A 1 88  ? 48.590 39.168  -23.822 1.00 30.62  ? 144 LYS B N   1 
ATOM   602  C CA  . LYS A 1 88  ? 47.362 38.449  -24.124 1.00 29.89  ? 144 LYS B CA  1 
ATOM   603  C C   . LYS A 1 88  ? 47.403 37.017  -23.611 1.00 22.46  ? 144 LYS B C   1 
ATOM   604  O O   . LYS A 1 88  ? 46.386 36.327  -23.555 1.00 21.07  ? 144 LYS B O   1 
ATOM   605  C CB  . LYS A 1 88  ? 47.139 38.412  -25.643 1.00 37.42  ? 144 LYS B CB  1 
ATOM   606  C CG  . LYS A 1 88  ? 46.942 39.767  -26.304 1.00 43.32  ? 144 LYS B CG  1 
ATOM   607  C CD  . LYS A 1 88  ? 46.339 39.594  -27.683 1.00 49.98  ? 144 LYS B CD  1 
ATOM   608  C CE  . LYS A 1 88  ? 46.034 40.931  -28.333 1.00 59.17  ? 144 LYS B CE  1 
ATOM   609  N NZ  . LYS A 1 88  ? 47.264 41.742  -28.567 1.00 65.62  ? 144 LYS B NZ  1 
ATOM   610  N N   . THR A 1 89  ? 48.588 36.557  -23.247 1.00 23.42  ? 145 THR B N   1 
ATOM   611  C CA  . THR A 1 89  ? 48.727 35.167  -22.861 1.00 28.37  ? 145 THR B CA  1 
ATOM   612  C C   . THR A 1 89  ? 49.747 34.998  -21.761 1.00 33.40  ? 145 THR B C   1 
ATOM   613  O O   . THR A 1 89  ? 50.862 35.511  -21.846 1.00 36.11  ? 145 THR B O   1 
ATOM   614  C CB  . THR A 1 89  ? 49.116 34.299  -24.055 1.00 37.42  ? 145 THR B CB  1 
ATOM   615  O OG1 . THR A 1 89  ? 48.037 34.288  -24.993 1.00 45.82  ? 145 THR B OG1 1 
ATOM   616  C CG2 . THR A 1 89  ? 49.399 32.883  -23.615 1.00 40.57  ? 145 THR B CG2 1 
ATOM   617  N N   . LEU A 1 90  ? 49.357 34.265  -20.730 1.00 35.59  ? 146 LEU B N   1 
ATOM   618  C CA  . LEU A 1 90  ? 50.252 33.955  -19.640 1.00 35.53  ? 146 LEU B CA  1 
ATOM   619  C C   . LEU A 1 90  ? 50.151 32.472  -19.349 1.00 34.60  ? 146 LEU B C   1 
ATOM   620  O O   . LEU A 1 90  ? 49.088 31.994  -18.960 1.00 34.98  ? 146 LEU B O   1 
ATOM   621  C CB  . LEU A 1 90  ? 49.856 34.764  -18.406 1.00 33.73  ? 146 LEU B CB  1 
ATOM   622  C CG  . LEU A 1 90  ? 50.770 34.744  -17.181 1.00 25.28  ? 146 LEU B CG  1 
ATOM   623  C CD1 . LEU A 1 90  ? 52.223 34.608  -17.575 1.00 26.65  ? 146 LEU B CD1 1 
ATOM   624  C CD2 . LEU A 1 90  ? 50.570 36.030  -16.433 1.00 25.96  ? 146 LEU B CD2 1 
ATOM   625  N N   . SER A 1 91  ? 51.240 31.737  -19.561 1.00 35.30  ? 147 SER B N   1 
ATOM   626  C CA  . SER A 1 91  ? 51.273 30.339  -19.160 1.00 33.42  ? 147 SER B CA  1 
ATOM   627  C C   . SER A 1 91  ? 52.411 30.126  -18.173 1.00 37.62  ? 147 SER B C   1 
ATOM   628  O O   . SER A 1 91  ? 53.580 30.068  -18.557 1.00 42.07  ? 147 SER B O   1 
ATOM   629  C CB  . SER A 1 91  ? 51.481 29.453  -20.390 1.00 33.60  ? 147 SER B CB  1 
ATOM   630  O OG  . SER A 1 91  ? 50.742 29.938  -21.502 1.00 33.98  ? 147 SER B OG  1 
ATOM   631  N N   . LEU A 1 92  ? 52.050 30.007  -16.899 1.00 33.51  ? 148 LEU B N   1 
ATOM   632  C CA  . LEU A 1 92  ? 52.986 29.709  -15.818 1.00 32.46  ? 148 LEU B CA  1 
ATOM   633  C C   . LEU A 1 92  ? 52.897 28.244  -15.361 1.00 35.53  ? 148 LEU B C   1 
ATOM   634  O O   . LEU A 1 92  ? 53.533 27.837  -14.384 1.00 34.79  ? 148 LEU B O   1 
ATOM   635  C CB  . LEU A 1 92  ? 52.806 30.705  -14.659 1.00 34.33  ? 148 LEU B CB  1 
ATOM   636  C CG  . LEU A 1 92  ? 53.201 32.160  -14.980 1.00 37.24  ? 148 LEU B CG  1 
ATOM   637  C CD1 . LEU A 1 92  ? 52.670 33.147  -13.961 1.00 26.72  ? 148 LEU B CD1 1 
ATOM   638  C CD2 . LEU A 1 92  ? 54.698 32.321  -15.108 1.00 28.23  ? 148 LEU B CD2 1 
ATOM   639  N N   . ASN A 1 93  ? 52.066 27.478  -16.059 1.00 36.45  ? 149 ASN B N   1 
ATOM   640  C CA  . ASN A 1 93  ? 51.634 26.151  -15.619 1.00 36.48  ? 149 ASN B CA  1 
ATOM   641  C C   . ASN A 1 93  ? 52.706 25.069  -15.634 1.00 36.93  ? 149 ASN B C   1 
ATOM   642  O O   . ASN A 1 93  ? 53.709 25.184  -16.346 1.00 39.45  ? 149 ASN B O   1 
ATOM   643  C CB  . ASN A 1 93  ? 50.436 25.686  -16.456 1.00 37.16  ? 149 ASN B CB  1 
ATOM   644  C CG  . ASN A 1 93  ? 50.826 25.304  -17.881 1.00 38.93  ? 149 ASN B CG  1 
ATOM   645  O OD1 . ASN A 1 93  ? 51.050 24.132  -18.179 1.00 19.87  ? 149 ASN B OD1 1 
ATOM   646  N ND2 . ASN A 1 93  ? 50.906 26.296  -18.764 1.00 20.69  ? 149 ASN B ND2 1 
ATOM   647  N N   . THR A 1 94  ? 52.459 24.010  -14.860 1.00 32.67  ? 150 THR B N   1 
ATOM   648  C CA  . THR A 1 94  ? 53.356 22.865  -14.768 1.00 25.65  ? 150 THR B CA  1 
ATOM   649  C C   . THR A 1 94  ? 54.702 23.339  -14.235 1.00 29.54  ? 150 THR B C   1 
ATOM   650  O O   . THR A 1 94  ? 55.752 23.046  -14.804 1.00 32.30  ? 150 THR B O   1 
ATOM   651  C CB  . THR A 1 94  ? 53.534 22.154  -16.136 1.00 46.81  ? 150 THR B CB  1 
ATOM   652  O OG1 . THR A 1 94  ? 52.282 22.119  -16.834 1.00 36.85  ? 150 THR B OG1 1 
ATOM   653  C CG2 . THR A 1 94  ? 54.047 20.733  -15.953 1.00 53.50  ? 150 THR B CG2 1 
ATOM   654  N N   . ASN A 1 95  ? 54.647 24.112  -13.155 1.00 27.85  ? 151 ASN B N   1 
ATOM   655  C CA  . ASN A 1 95  ? 55.831 24.586  -12.459 1.00 25.55  ? 151 ASN B CA  1 
ATOM   656  C C   . ASN A 1 95  ? 55.608 24.474  -10.957 1.00 46.48  ? 151 ASN B C   1 
ATOM   657  O O   . ASN A 1 95  ? 54.595 23.943  -10.509 1.00 24.13  ? 151 ASN B O   1 
ATOM   658  C CB  . ASN A 1 95  ? 56.124 26.042  -12.822 1.00 43.18  ? 151 ASN B CB  1 
ATOM   659  C CG  . ASN A 1 95  ? 56.676 26.197  -14.221 1.00 47.01  ? 151 ASN B CG  1 
ATOM   660  O OD1 . ASN A 1 95  ? 57.372 25.326  -14.724 1.00 49.83  ? 151 ASN B OD1 1 
ATOM   661  N ND2 . ASN A 1 95  ? 56.366 27.315  -14.857 1.00 48.25  ? 151 ASN B ND2 1 
ATOM   662  N N   . ASN A 1 96  ? 56.567 24.949  -10.174 1.00 26.76  ? 152 ASN B N   1 
ATOM   663  C CA  . ASN A 1 96  ? 56.419 24.942  -8.728  1.00 31.67  ? 152 ASN B CA  1 
ATOM   664  C C   . ASN A 1 96  ? 56.002 26.246  -8.065  1.00 34.64  ? 152 ASN B C   1 
ATOM   665  O O   . ASN A 1 96  ? 55.964 26.331  -6.837  1.00 32.05  ? 152 ASN B O   1 
ATOM   666  C CB  . ASN A 1 96  ? 57.612 24.289  -8.044  1.00 31.05  ? 152 ASN B CB  1 
ATOM   667  C CG  . ASN A 1 96  ? 57.458 22.790  -7.967  1.00 37.48  ? 152 ASN B CG  1 
ATOM   668  O OD1 . ASN A 1 96  ? 56.415 22.285  -7.538  1.00 38.13  ? 152 ASN B OD1 1 
ATOM   669  N ND2 . ASN A 1 96  ? 58.475 22.064  -8.419  1.00 43.63  ? 152 ASN B ND2 1 
ATOM   670  N N   . LEU A 1 97  ? 55.686 27.246  -8.880  1.00 40.22  ? 153 LEU B N   1 
ATOM   671  C CA  . LEU A 1 97  ? 55.429 28.589  -8.373  1.00 42.18  ? 153 LEU B CA  1 
ATOM   672  C C   . LEU A 1 97  ? 54.461 28.561  -7.200  1.00 37.79  ? 153 LEU B C   1 
ATOM   673  O O   . LEU A 1 97  ? 53.430 27.894  -7.246  1.00 25.44  ? 153 LEU B O   1 
ATOM   674  C CB  . LEU A 1 97  ? 54.846 29.475  -9.474  1.00 36.49  ? 153 LEU B CB  1 
ATOM   675  C CG  . LEU A 1 97  ? 55.570 29.481  -10.813 1.00 36.93  ? 153 LEU B CG  1 
ATOM   676  C CD1 . LEU A 1 97  ? 54.893 30.469  -11.742 1.00 43.79  ? 153 LEU B CD1 1 
ATOM   677  C CD2 . LEU A 1 97  ? 57.034 29.822  -10.633 1.00 37.34  ? 153 LEU B CD2 1 
ATOM   678  N N   . GLU A 1 98  ? 54.828 29.256  -6.132  1.00 27.85  ? 154 GLU B N   1 
ATOM   679  C CA  . GLU A 1 98  ? 53.951 29.386  -4.978  1.00 42.91  ? 154 GLU B CA  1 
ATOM   680  C C   . GLU A 1 98  ? 53.497 30.826  -4.820  1.00 38.14  ? 154 GLU B C   1 
ATOM   681  O O   . GLU A 1 98  ? 53.856 31.686  -5.618  1.00 43.83  ? 154 GLU B O   1 
ATOM   682  C CB  . GLU A 1 98  ? 54.645 28.897  -3.706  1.00 45.73  ? 154 GLU B CB  1 
ATOM   683  C CG  . GLU A 1 98  ? 56.116 29.246  -3.630  1.00 54.56  ? 154 GLU B CG  1 
ATOM   684  C CD  . GLU A 1 98  ? 56.743 28.795  -2.335  1.00 65.36  ? 154 GLU B CD  1 
ATOM   685  O OE1 . GLU A 1 98  ? 57.971 28.966  -2.182  1.00 72.60  ? 154 GLU B OE1 1 
ATOM   686  O OE2 . GLU A 1 98  ? 56.007 28.275  -1.467  1.00 66.68  ? 154 GLU B OE2 1 
ATOM   687  N N   . GLY A 1 99  ? 52.699 31.087  -3.796  1.00 36.67  ? 155 GLY B N   1 
ATOM   688  C CA  . GLY A 1 99  ? 52.251 32.438  -3.533  1.00 27.61  ? 155 GLY B CA  1 
ATOM   689  C C   . GLY A 1 99  ? 50.797 32.660  -3.865  1.00 34.03  ? 155 GLY B C   1 
ATOM   690  O O   . GLY A 1 99  ? 50.152 31.828  -4.500  1.00 34.60  ? 155 GLY B O   1 
ATOM   691  N N   . HIS A 1 100 ? 50.271 33.793  -3.421  1.00 35.76  ? 156 HIS B N   1 
ATOM   692  C CA  . HIS A 1 100 ? 48.921 34.192  -3.781  1.00 44.36  ? 156 HIS B CA  1 
ATOM   693  C C   . HIS A 1 100 ? 48.877 34.631  -5.240  1.00 45.43  ? 156 HIS B C   1 
ATOM   694  O O   . HIS A 1 100 ? 49.910 34.923  -5.843  1.00 46.15  ? 156 HIS B O   1 
ATOM   695  C CB  . HIS A 1 100 ? 48.441 35.323  -2.865  1.00 49.12  ? 156 HIS B CB  1 
ATOM   696  C CG  . HIS A 1 100 ? 48.194 34.888  -1.451  1.00 52.24  ? 156 HIS B CG  1 
ATOM   697  N ND1 . HIS A 1 100 ? 46.997 35.107  -0.806  1.00 53.02  ? 156 HIS B ND1 1 
ATOM   698  C CD2 . HIS A 1 100 ? 48.985 34.235  -0.569  1.00 53.04  ? 156 HIS B CD2 1 
ATOM   699  C CE1 . HIS A 1 100 ? 47.063 34.615  0.419   1.00 53.35  ? 156 HIS B CE1 1 
ATOM   700  N NE2 . HIS A 1 100 ? 48.261 34.077  0.587   1.00 53.19  ? 156 HIS B NE2 1 
ATOM   701  N N   . ILE A 1 101 ? 47.688 34.647  -5.824  1.00 41.61  ? 157 ILE B N   1 
ATOM   702  C CA  . ILE A 1 101 ? 47.538 35.284  -7.121  1.00 38.13  ? 157 ILE B CA  1 
ATOM   703  C C   . ILE A 1 101 ? 47.354 36.777  -6.882  1.00 36.09  ? 157 ILE B C   1 
ATOM   704  O O   . ILE A 1 101 ? 46.379 37.198  -6.258  1.00 35.04  ? 157 ILE B O   1 
ATOM   705  C CB  . ILE A 1 101 ? 46.351 34.728  -7.901  1.00 38.78  ? 157 ILE B CB  1 
ATOM   706  C CG1 . ILE A 1 101 ? 46.591 33.259  -8.250  1.00 37.66  ? 157 ILE B CG1 1 
ATOM   707  C CG2 . ILE A 1 101 ? 46.140 35.539  -9.166  1.00 42.68  ? 157 ILE B CG2 1 
ATOM   708  C CD1 . ILE A 1 101 ? 45.329 32.494  -8.566  1.00 31.95  ? 157 ILE B CD1 1 
ATOM   709  N N   . PRO A 1 102 ? 48.306 37.582  -7.362  1.00 35.62  ? 158 PRO B N   1 
ATOM   710  C CA  . PRO A 1 102 ? 48.311 39.022  -7.100  1.00 27.32  ? 158 PRO B CA  1 
ATOM   711  C C   . PRO A 1 102 ? 47.048 39.705  -7.594  1.00 36.90  ? 158 PRO B C   1 
ATOM   712  O O   . PRO A 1 102 ? 46.543 39.369  -8.660  1.00 45.25  ? 158 PRO B O   1 
ATOM   713  C CB  . PRO A 1 102 ? 49.524 39.507  -7.895  1.00 32.24  ? 158 PRO B CB  1 
ATOM   714  C CG  . PRO A 1 102 ? 50.405 38.318  -7.965  1.00 28.73  ? 158 PRO B CG  1 
ATOM   715  C CD  . PRO A 1 102 ? 49.479 37.169  -8.150  1.00 36.08  ? 158 PRO B CD  1 
ATOM   716  N N   . MET A 1 103 ? 46.548 40.652  -6.811  1.00 34.23  ? 159 MET B N   1 
ATOM   717  C CA  . MET A 1 103 ? 45.369 41.426  -7.174  1.00 36.72  ? 159 MET B CA  1 
ATOM   718  C C   . MET A 1 103 ? 45.629 42.215  -8.462  1.00 39.26  ? 159 MET B C   1 
ATOM   719  O O   . MET A 1 103 ? 44.748 42.358  -9.317  1.00 45.35  ? 159 MET B O   1 
ATOM   720  C CB  . MET A 1 103 ? 45.003 42.367  -6.022  1.00 35.26  ? 159 MET B CB  1 
ATOM   721  C CG  . MET A 1 103 ? 43.716 43.159  -6.200  1.00 38.57  ? 159 MET B CG  1 
ATOM   722  S SD  . MET A 1 103 ? 42.218 42.218  -5.837  1.00 134.43 ? 159 MET B SD  1 
ATOM   723  C CE  . MET A 1 103 ? 41.027 43.550  -5.648  1.00 36.11  ? 159 MET B CE  1 
ATOM   724  N N   . GLU A 1 104 ? 46.864 42.674  -8.624  1.00 32.89  ? 160 GLU B N   1 
ATOM   725  C CA  . GLU A 1 104 ? 47.235 43.511  -9.756  1.00 33.35  ? 160 GLU B CA  1 
ATOM   726  C C   . GLU A 1 104 ? 47.050 42.808  -11.092 1.00 42.09  ? 160 GLU B C   1 
ATOM   727  O O   . GLU A 1 104 ? 47.185 43.429  -12.147 1.00 50.03  ? 160 GLU B O   1 
ATOM   728  C CB  . GLU A 1 104 ? 48.670 44.017  -9.621  1.00 42.89  ? 160 GLU B CB  1 
ATOM   729  C CG  . GLU A 1 104 ? 48.851 45.080  -8.550  1.00 64.15  ? 160 GLU B CG  1 
ATOM   730  C CD  . GLU A 1 104 ? 48.790 44.507  -7.135  1.00 81.31  ? 160 GLU B CD  1 
ATOM   731  O OE1 . GLU A 1 104 ? 48.987 43.280  -6.981  1.00 86.58  ? 160 GLU B OE1 1 
ATOM   732  O OE2 . GLU A 1 104 ? 48.540 45.281  -6.178  1.00 86.33  ? 160 GLU B OE2 1 
ATOM   733  N N   . ILE A 1 105 ? 46.755 41.512  -11.054 1.00 42.40  ? 161 ILE B N   1 
ATOM   734  C CA  . ILE A 1 105 ? 46.428 40.776  -12.272 1.00 43.84  ? 161 ILE B CA  1 
ATOM   735  C C   . ILE A 1 105 ? 45.224 41.407  -12.988 1.00 47.05  ? 161 ILE B C   1 
ATOM   736  O O   . ILE A 1 105 ? 45.114 41.338  -14.214 1.00 43.53  ? 161 ILE B O   1 
ATOM   737  C CB  . ILE A 1 105 ? 46.163 39.282  -11.985 1.00 38.87  ? 161 ILE B CB  1 
ATOM   738  C CG1 . ILE A 1 105 ? 46.323 38.449  -13.253 1.00 36.74  ? 161 ILE B CG1 1 
ATOM   739  C CG2 . ILE A 1 105 ? 44.777 39.074  -11.394 1.00 38.67  ? 161 ILE B CG2 1 
ATOM   740  C CD1 . ILE A 1 105 ? 46.307 36.957  -12.992 1.00 35.49  ? 161 ILE B CD1 1 
ATOM   741  N N   . GLY A 1 106 ? 44.340 42.047  -12.224 1.00 46.12  ? 162 GLY B N   1 
ATOM   742  C CA  . GLY A 1 106 ? 43.189 42.711  -12.811 1.00 43.03  ? 162 GLY B CA  1 
ATOM   743  C C   . GLY A 1 106 ? 43.588 43.859  -13.719 1.00 45.11  ? 162 GLY B C   1 
ATOM   744  O O   . GLY A 1 106 ? 42.794 44.310  -14.540 1.00 46.01  ? 162 GLY B O   1 
ATOM   745  N N   . ASN A 1 107 ? 44.825 44.330  -13.573 1.00 48.05  ? 163 ASN B N   1 
ATOM   746  C CA  . ASN A 1 107 ? 45.327 45.452  -14.367 1.00 55.45  ? 163 ASN B CA  1 
ATOM   747  C C   . ASN A 1 107 ? 45.715 45.076  -15.804 1.00 51.89  ? 163 ASN B C   1 
ATOM   748  O O   . ASN A 1 107 ? 46.043 45.953  -16.609 1.00 46.86  ? 163 ASN B O   1 
ATOM   749  C CB  . ASN A 1 107 ? 46.488 46.161  -13.654 1.00 67.10  ? 163 ASN B CB  1 
ATOM   750  C CG  . ASN A 1 107 ? 46.018 47.114  -12.554 1.00 75.79  ? 163 ASN B CG  1 
ATOM   751  O OD1 . ASN A 1 107 ? 45.908 48.321  -12.770 1.00 77.04  ? 163 ASN B OD1 1 
ATOM   752  N ND2 . ASN A 1 107 ? 45.745 46.570  -11.371 1.00 79.28  ? 163 ASN B ND2 1 
ATOM   753  N N   . LEU A 1 108 ? 45.668 43.787  -16.137 1.00 50.10  ? 164 LEU B N   1 
ATOM   754  C CA  . LEU A 1 108 ? 45.969 43.395  -17.505 1.00 44.77  ? 164 LEU B CA  1 
ATOM   755  C C   . LEU A 1 108 ? 44.682 43.345  -18.315 1.00 37.93  ? 164 LEU B C   1 
ATOM   756  O O   . LEU A 1 108 ? 43.987 42.325  -18.344 1.00 23.26  ? 164 LEU B O   1 
ATOM   757  C CB  . LEU A 1 108 ? 46.596 41.998  -17.517 1.00 42.61  ? 164 LEU B CB  1 
ATOM   758  C CG  . LEU A 1 108 ? 47.860 41.776  -16.696 1.00 26.91  ? 164 LEU B CG  1 
ATOM   759  C CD1 . LEU A 1 108 ? 48.480 40.429  -17.024 1.00 26.57  ? 164 LEU B CD1 1 
ATOM   760  C CD2 . LEU A 1 108 ? 48.844 42.896  -16.951 1.00 28.62  ? 164 LEU B CD2 1 
ATOM   761  N N   . SER A 1 109 ? 44.459 44.397  -19.092 1.00 30.05  ? 165 SER B N   1 
ATOM   762  C CA  . SER A 1 109 ? 43.200 44.569  -19.803 1.00 33.03  ? 165 SER B CA  1 
ATOM   763  C C   . SER A 1 109 ? 43.111 43.558  -20.927 1.00 35.10  ? 165 SER B C   1 
ATOM   764  O O   . SER A 1 109 ? 42.021 43.161  -21.330 1.00 31.09  ? 165 SER B O   1 
ATOM   765  C CB  . SER A 1 109 ? 43.102 45.977  -20.401 1.00 42.32  ? 165 SER B CB  1 
ATOM   766  O OG  . SER A 1 109 ? 43.418 46.979  -19.452 1.00 50.89  ? 165 SER B OG  1 
ATOM   767  N N   . GLY A 1 110 ? 44.267 43.141  -21.432 1.00 36.07  ? 166 GLY B N   1 
ATOM   768  C CA  . GLY A 1 110 ? 44.310 42.373  -22.657 1.00 32.64  ? 166 GLY B CA  1 
ATOM   769  C C   . GLY A 1 110 ? 44.560 40.891  -22.503 1.00 39.14  ? 166 GLY B C   1 
ATOM   770  O O   . GLY A 1 110 ? 44.746 40.200  -23.496 1.00 41.21  ? 166 GLY B O   1 
ATOM   771  N N   . LEU A 1 111 ? 44.556 40.388  -21.272 1.00 41.88  ? 167 LEU B N   1 
ATOM   772  C CA  . LEU A 1 111 ? 44.828 38.970  -21.054 1.00 29.37  ? 167 LEU B CA  1 
ATOM   773  C C   . LEU A 1 111 ? 43.681 38.111  -21.601 1.00 25.33  ? 167 LEU B C   1 
ATOM   774  O O   . LEU A 1 111 ? 42.514 38.305  -21.254 1.00 20.56  ? 167 LEU B O   1 
ATOM   775  C CB  . LEU A 1 111 ? 45.107 38.691  -19.576 1.00 21.78  ? 167 LEU B CB  1 
ATOM   776  C CG  . LEU A 1 111 ? 45.657 37.295  -19.255 1.00 32.90  ? 167 LEU B CG  1 
ATOM   777  C CD1 . LEU A 1 111 ? 46.906 37.011  -20.077 1.00 28.99  ? 167 LEU B CD1 1 
ATOM   778  C CD2 . LEU A 1 111 ? 45.945 37.131  -17.755 1.00 30.27  ? 167 LEU B CD2 1 
ATOM   779  N N   . VAL A 1 112 ? 44.033 37.170  -22.471 1.00 28.82  ? 168 VAL B N   1 
ATOM   780  C CA  . VAL A 1 112 ? 43.063 36.314  -23.158 1.00 29.42  ? 168 VAL B CA  1 
ATOM   781  C C   . VAL A 1 112 ? 43.051 34.900  -22.580 1.00 29.06  ? 168 VAL B C   1 
ATOM   782  O O   . VAL A 1 112 ? 41.999 34.372  -22.217 1.00 26.10  ? 168 VAL B O   1 
ATOM   783  C CB  . VAL A 1 112 ? 43.258 36.290  -24.700 1.00 17.96  ? 168 VAL B CB  1 
ATOM   784  C CG1 . VAL A 1 112 ? 42.290 35.322  -25.335 1.00 16.47  ? 168 VAL B CG1 1 
ATOM   785  C CG2 . VAL A 1 112 ? 43.049 37.669  -25.270 1.00 18.49  ? 168 VAL B CG2 1 
ATOM   786  N N   . GLU A 1 113 ? 44.210 34.258  -22.594 1.00 31.29  ? 169 GLU B N   1 
ATOM   787  C CA  . GLU A 1 113 ? 44.355 32.938  -22.003 1.00 30.95  ? 169 GLU B CA  1 
ATOM   788  C C   . GLU A 1 113 ? 45.296 32.961  -20.788 1.00 30.51  ? 169 GLU B C   1 
ATOM   789  O O   . GLU A 1 113 ? 46.443 33.382  -20.900 1.00 42.39  ? 169 GLU B O   1 
ATOM   790  C CB  . GLU A 1 113 ? 44.888 31.986  -23.064 1.00 32.66  ? 169 GLU B CB  1 
ATOM   791  C CG  . GLU A 1 113 ? 44.443 32.356  -24.461 1.00 38.43  ? 169 GLU B CG  1 
ATOM   792  C CD  . GLU A 1 113 ? 43.400 31.410  -25.015 1.00 47.23  ? 169 GLU B CD  1 
ATOM   793  O OE1 . GLU A 1 113 ? 43.595 30.184  -24.880 1.00 52.15  ? 169 GLU B OE1 1 
ATOM   794  O OE2 . GLU A 1 113 ? 42.390 31.887  -25.586 1.00 48.15  ? 169 GLU B OE2 1 
ATOM   795  N N   . LEU A 1 114 ? 44.812 32.506  -19.635 1.00 25.09  ? 170 LEU B N   1 
ATOM   796  C CA  . LEU A 1 114 ? 45.621 32.463  -18.411 1.00 23.73  ? 170 LEU B CA  1 
ATOM   797  C C   . LEU A 1 114 ? 45.767 31.045  -17.866 1.00 23.88  ? 170 LEU B C   1 
ATOM   798  O O   . LEU A 1 114 ? 44.787 30.470  -17.403 1.00 29.73  ? 170 LEU B O   1 
ATOM   799  C CB  . LEU A 1 114 ? 44.960 33.324  -17.345 1.00 23.75  ? 170 LEU B CB  1 
ATOM   800  C CG  . LEU A 1 114 ? 45.482 33.198  -15.921 1.00 26.51  ? 170 LEU B CG  1 
ATOM   801  C CD1 . LEU A 1 114 ? 46.935 33.614  -15.878 1.00 26.19  ? 170 LEU B CD1 1 
ATOM   802  C CD2 . LEU A 1 114 ? 44.636 34.046  -14.990 1.00 19.23  ? 170 LEU B CD2 1 
ATOM   803  N N   . MET A 1 115 ? 46.975 30.481  -17.917 1.00 23.97  ? 171 MET B N   1 
ATOM   804  C CA  . MET A 1 115 ? 47.191 29.114  -17.426 1.00 31.13  ? 171 MET B CA  1 
ATOM   805  C C   . MET A 1 115 ? 48.140 29.036  -16.225 1.00 34.59  ? 171 MET B C   1 
ATOM   806  O O   . MET A 1 115 ? 49.354 29.121  -16.384 1.00 37.59  ? 171 MET B O   1 
ATOM   807  C CB  . MET A 1 115 ? 47.775 28.252  -18.549 1.00 29.49  ? 171 MET B CB  1 
ATOM   808  C CG  . MET A 1 115 ? 47.159 28.486  -19.906 1.00 21.55  ? 171 MET B CG  1 
ATOM   809  S SD  . MET A 1 115 ? 45.744 27.433  -20.185 1.00 32.85  ? 171 MET B SD  1 
ATOM   810  C CE  . MET A 1 115 ? 45.239 27.955  -21.825 1.00 15.95  ? 171 MET B CE  1 
ATOM   811  N N   . LEU A 1 116 ? 47.580 28.843  -15.038 1.00 19.09  ? 172 LEU B N   1 
ATOM   812  C CA  . LEU A 1 116 ? 48.359 28.723  -13.799 1.00 24.58  ? 172 LEU B CA  1 
ATOM   813  C C   . LEU A 1 116 ? 48.487 27.293  -13.253 1.00 24.70  ? 172 LEU B C   1 
ATOM   814  O O   . LEU A 1 116 ? 49.117 27.063  -12.221 1.00 19.99  ? 172 LEU B O   1 
ATOM   815  C CB  . LEU A 1 116 ? 47.766 29.647  -12.734 1.00 20.00  ? 172 LEU B CB  1 
ATOM   816  C CG  . LEU A 1 116 ? 47.735 31.110  -13.181 1.00 23.09  ? 172 LEU B CG  1 
ATOM   817  C CD1 . LEU A 1 116 ? 46.737 31.902  -12.366 1.00 28.50  ? 172 LEU B CD1 1 
ATOM   818  C CD2 . LEU A 1 116 ? 49.125 31.732  -13.083 1.00 22.44  ? 172 LEU B CD2 1 
ATOM   819  N N   . PHE A 1 117 ? 47.864 26.344  -13.945 1.00 29.89  ? 173 PHE B N   1 
ATOM   820  C CA  . PHE A 1 117 ? 47.591 25.024  -13.380 1.00 17.37  ? 173 PHE B CA  1 
ATOM   821  C C   . PHE A 1 117 ? 48.817 24.145  -13.115 1.00 25.10  ? 173 PHE B C   1 
ATOM   822  O O   . PHE A 1 117 ? 49.896 24.392  -13.651 1.00 25.44  ? 173 PHE B O   1 
ATOM   823  C CB  . PHE A 1 117 ? 46.550 24.281  -14.222 1.00 15.95  ? 173 PHE B CB  1 
ATOM   824  C CG  . PHE A 1 117 ? 47.060 23.792  -15.548 1.00 16.06  ? 173 PHE B CG  1 
ATOM   825  C CD1 . PHE A 1 117 ? 47.721 22.578  -15.650 1.00 23.28  ? 173 PHE B CD1 1 
ATOM   826  C CD2 . PHE A 1 117 ? 46.839 24.527  -16.700 1.00 16.08  ? 173 PHE B CD2 1 
ATOM   827  C CE1 . PHE A 1 117 ? 48.178 22.120  -16.868 1.00 17.43  ? 173 PHE B CE1 1 
ATOM   828  C CE2 . PHE A 1 117 ? 47.289 24.074  -17.936 1.00 16.19  ? 173 PHE B CE2 1 
ATOM   829  C CZ  . PHE A 1 117 ? 47.956 22.871  -18.022 1.00 19.67  ? 173 PHE B CZ  1 
ATOM   830  N N   . ASP A 1 118 ? 48.628 23.125  -12.276 1.00 24.94  ? 174 ASP B N   1 
ATOM   831  C CA  . ASP A 1 118 ? 49.709 22.244  -11.816 1.00 21.96  ? 174 ASP B CA  1 
ATOM   832  C C   . ASP A 1 118 ? 50.886 23.031  -11.260 1.00 21.19  ? 174 ASP B C   1 
ATOM   833  O O   . ASP A 1 118 ? 51.969 23.016  -11.838 1.00 25.36  ? 174 ASP B O   1 
ATOM   834  C CB  . ASP A 1 118 ? 50.200 21.306  -12.923 1.00 24.55  ? 174 ASP B CB  1 
ATOM   835  C CG  . ASP A 1 118 ? 49.259 20.134  -13.170 1.00 29.72  ? 174 ASP B CG  1 
ATOM   836  O OD1 . ASP A 1 118 ? 48.528 19.732  -12.245 1.00 25.82  ? 174 ASP B OD1 1 
ATOM   837  O OD2 . ASP A 1 118 ? 49.260 19.603  -14.298 1.00 38.33  ? 174 ASP B OD2 1 
ATOM   838  N N   . ASN A 1 119 ? 50.656 23.723  -10.149 1.00 20.08  ? 175 ASN B N   1 
ATOM   839  C CA  . ASN A 1 119 ? 51.703 24.442  -9.444  1.00 21.56  ? 175 ASN B CA  1 
ATOM   840  C C   . ASN A 1 119 ? 51.582 24.142  -7.971  1.00 21.48  ? 175 ASN B C   1 
ATOM   841  O O   . ASN A 1 119 ? 50.792 23.290  -7.559  1.00 20.33  ? 175 ASN B O   1 
ATOM   842  C CB  . ASN A 1 119 ? 51.570 25.953  -9.635  1.00 39.41  ? 175 ASN B CB  1 
ATOM   843  C CG  . ASN A 1 119 ? 52.135 26.438  -10.955 1.00 41.14  ? 175 ASN B CG  1 
ATOM   844  O OD1 . ASN A 1 119 ? 53.161 25.961  -11.415 1.00 23.56  ? 175 ASN B OD1 1 
ATOM   845  N ND2 . ASN A 1 119 ? 51.465 27.405  -11.565 1.00 22.57  ? 175 ASN B ND2 1 
ATOM   846  N N   . LYS A 1 120 ? 52.399 24.831  -7.184  1.00 32.33  ? 176 LYS B N   1 
ATOM   847  C CA  . LYS A 1 120 ? 52.315 24.819  -5.728  1.00 33.39  ? 176 LYS B CA  1 
ATOM   848  C C   . LYS A 1 120 ? 51.531 26.007  -5.139  1.00 38.30  ? 176 LYS B C   1 
ATOM   849  O O   . LYS A 1 120 ? 51.575 26.237  -3.939  1.00 46.03  ? 176 LYS B O   1 
ATOM   850  C CB  . LYS A 1 120 ? 53.696 24.646  -5.090  1.00 33.30  ? 176 LYS B CB  1 
ATOM   851  C CG  . LYS A 1 120 ? 54.074 23.182  -4.878  1.00 34.62  ? 176 LYS B CG  1 
ATOM   852  C CD  . LYS A 1 120 ? 52.987 22.468  -4.066  1.00 44.82  ? 176 LYS B CD  1 
ATOM   853  C CE  . LYS A 1 120 ? 53.388 21.049  -3.627  1.00 48.95  ? 176 LYS B CE  1 
ATOM   854  N NZ  . LYS A 1 120 ? 54.425 21.002  -2.536  1.00 47.25  ? 176 LYS B NZ  1 
ATOM   855  N N   . LEU A 1 121 ? 50.841 26.769  -5.987  1.00 39.36  ? 177 LEU B N   1 
ATOM   856  C CA  . LEU A 1 121 ? 50.214 28.033  -5.579  1.00 36.01  ? 177 LEU B CA  1 
ATOM   857  C C   . LEU A 1 121 ? 49.208 27.866  -4.441  1.00 32.51  ? 177 LEU B C   1 
ATOM   858  O O   . LEU A 1 121 ? 48.692 26.773  -4.196  1.00 31.30  ? 177 LEU B O   1 
ATOM   859  C CB  . LEU A 1 121 ? 49.479 28.679  -6.764  1.00 40.59  ? 177 LEU B CB  1 
ATOM   860  C CG  . LEU A 1 121 ? 50.224 29.139  -8.025  1.00 41.76  ? 177 LEU B CG  1 
ATOM   861  C CD1 . LEU A 1 121 ? 49.245 29.697  -9.065  1.00 39.30  ? 177 LEU B CD1 1 
ATOM   862  C CD2 . LEU A 1 121 ? 51.287 30.174  -7.680  1.00 41.08  ? 177 LEU B CD2 1 
ATOM   863  N N   . SER A 1 122 ? 48.967 28.967  -3.733  1.00 35.39  ? 178 SER B N   1 
ATOM   864  C CA  . SER A 1 122 ? 48.043 29.015  -2.601  1.00 35.55  ? 178 SER B CA  1 
ATOM   865  C C   . SER A 1 122 ? 47.342 30.372  -2.549  1.00 33.86  ? 178 SER B C   1 
ATOM   866  O O   . SER A 1 122 ? 47.491 31.198  -3.452  1.00 44.75  ? 178 SER B O   1 
ATOM   867  C CB  . SER A 1 122 ? 48.792 28.775  -1.286  1.00 39.23  ? 178 SER B CB  1 
ATOM   868  O OG  . SER A 1 122 ? 49.889 29.668  -1.140  1.00 24.05  ? 178 SER B OG  1 
ATOM   869  N N   . GLY A 1 123 ? 46.581 30.598  -1.486  1.00 25.07  ? 179 GLY B N   1 
ATOM   870  C CA  . GLY A 1 123 ? 45.874 31.854  -1.311  1.00 28.80  ? 179 GLY B CA  1 
ATOM   871  C C   . GLY A 1 123 ? 44.475 31.803  -1.881  1.00 31.62  ? 179 GLY B C   1 
ATOM   872  O O   . GLY A 1 123 ? 43.995 30.740  -2.251  1.00 35.34  ? 179 GLY B O   1 
ATOM   873  N N   . GLU A 1 124 ? 43.810 32.948  -1.951  1.00 35.30  ? 180 GLU B N   1 
ATOM   874  C CA  . GLU A 1 124 ? 42.511 33.008  -2.608  1.00 33.43  ? 180 GLU B CA  1 
ATOM   875  C C   . GLU A 1 124 ? 42.662 33.448  -4.061  1.00 28.24  ? 180 GLU B C   1 
ATOM   876  O O   . GLU A 1 124 ? 43.755 33.809  -4.514  1.00 22.74  ? 180 GLU B O   1 
ATOM   877  C CB  . GLU A 1 124 ? 41.596 34.006  -1.895  1.00 38.82  ? 180 GLU B CB  1 
ATOM   878  C CG  . GLU A 1 124 ? 40.906 33.502  -0.644  1.00 45.39  ? 180 GLU B CG  1 
ATOM   879  C CD  . GLU A 1 124 ? 39.692 34.347  -0.306  1.00 55.70  ? 180 GLU B CD  1 
ATOM   880  O OE1 . GLU A 1 124 ? 39.573 35.457  -0.868  1.00 56.75  ? 180 GLU B OE1 1 
ATOM   881  O OE2 . GLU A 1 124 ? 38.852 33.900  0.505   1.00 61.59  ? 180 GLU B OE2 1 
ATOM   882  N N   . ILE A 1 125 ? 41.542 33.440  -4.775  1.00 30.36  ? 181 ILE B N   1 
ATOM   883  C CA  . ILE A 1 125 ? 41.478 34.027  -6.100  1.00 32.16  ? 181 ILE B CA  1 
ATOM   884  C C   . ILE A 1 125 ? 41.109 35.475  -5.892  1.00 30.36  ? 181 ILE B C   1 
ATOM   885  O O   . ILE A 1 125 ? 40.092 35.769  -5.270  1.00 34.29  ? 181 ILE B O   1 
ATOM   886  C CB  . ILE A 1 125 ? 40.399 33.370  -6.977  1.00 32.36  ? 181 ILE B CB  1 
ATOM   887  C CG1 . ILE A 1 125 ? 40.797 31.946  -7.344  1.00 32.84  ? 181 ILE B CG1 1 
ATOM   888  C CG2 . ILE A 1 125 ? 40.205 34.157  -8.257  1.00 34.35  ? 181 ILE B CG2 1 
ATOM   889  C CD1 . ILE A 1 125 ? 39.828 31.290  -8.298  1.00 37.83  ? 181 ILE B CD1 1 
ATOM   890  N N   . PRO A 1 126 ? 41.942 36.387  -6.395  1.00 28.84  ? 182 PRO B N   1 
ATOM   891  C CA  . PRO A 1 126 ? 41.697 37.822  -6.236  1.00 20.60  ? 182 PRO B CA  1 
ATOM   892  C C   . PRO A 1 126 ? 40.350 38.191  -6.805  1.00 21.39  ? 182 PRO B C   1 
ATOM   893  O O   . PRO A 1 126 ? 39.920 37.547  -7.750  1.00 25.33  ? 182 PRO B O   1 
ATOM   894  C CB  . PRO A 1 126 ? 42.812 38.464  -7.066  1.00 38.89  ? 182 PRO B CB  1 
ATOM   895  C CG  . PRO A 1 126 ? 43.332 37.372  -7.951  1.00 34.19  ? 182 PRO B CG  1 
ATOM   896  C CD  . PRO A 1 126 ? 43.159 36.113  -7.171  1.00 28.65  ? 182 PRO B CD  1 
ATOM   897  N N   . ARG A 1 127 ? 39.690 39.194  -6.239  1.00 26.47  ? 183 ARG B N   1 
ATOM   898  C CA  . ARG A 1 127 ? 38.390 39.630  -6.745  1.00 26.47  ? 183 ARG B CA  1 
ATOM   899  C C   . ARG A 1 127 ? 38.555 40.398  -8.053  1.00 26.44  ? 183 ARG B C   1 
ATOM   900  O O   . ARG A 1 127 ? 37.567 40.765  -8.681  1.00 32.94  ? 183 ARG B O   1 
ATOM   901  C CB  . ARG A 1 127 ? 37.657 40.518  -5.724  1.00 30.74  ? 183 ARG B CB  1 
ATOM   902  C CG  . ARG A 1 127 ? 38.096 40.375  -4.270  1.00 33.55  ? 183 ARG B CG  1 
ATOM   903  C CD  . ARG A 1 127 ? 37.171 39.463  -3.473  1.00 37.50  ? 183 ARG B CD  1 
ATOM   904  N NE  . ARG A 1 127 ? 35.782 39.915  -3.497  1.00 41.23  ? 183 ARG B NE  1 
ATOM   905  C CZ  . ARG A 1 127 ? 35.317 40.943  -2.796  1.00 47.63  ? 183 ARG B CZ  1 
ATOM   906  N NH1 . ARG A 1 127 ? 36.130 41.640  -2.014  1.00 55.45  ? 183 ARG B NH1 1 
ATOM   907  N NH2 . ARG A 1 127 ? 34.037 41.277  -2.882  1.00 43.91  ? 183 ARG B NH2 1 
ATOM   908  N N   . SER A 1 128 ? 39.807 40.651  -8.436  1.00 27.08  ? 184 SER B N   1 
ATOM   909  C CA  . SER A 1 128 ? 40.158 41.431  -9.632  1.00 29.48  ? 184 SER B CA  1 
ATOM   910  C C   . SER A 1 128 ? 40.031 40.726  -10.990 1.00 24.93  ? 184 SER B C   1 
ATOM   911  O O   . SER A 1 128 ? 40.136 41.380  -12.021 1.00 20.37  ? 184 SER B O   1 
ATOM   912  C CB  . SER A 1 128 ? 41.586 41.951  -9.515  1.00 22.56  ? 184 SER B CB  1 
ATOM   913  O OG  . SER A 1 128 ? 41.651 43.045  -8.637  1.00 72.57  ? 184 SER B OG  1 
ATOM   914  N N   . ILE A 1 129 ? 39.840 39.409  -11.003 1.00 20.09  ? 185 ILE B N   1 
ATOM   915  C CA  . ILE A 1 129 ? 39.671 38.687  -12.261 1.00 24.90  ? 185 ILE B CA  1 
ATOM   916  C C   . ILE A 1 129 ? 38.498 39.257  -13.063 1.00 32.16  ? 185 ILE B C   1 
ATOM   917  O O   . ILE A 1 129 ? 38.426 39.078  -14.273 1.00 35.58  ? 185 ILE B O   1 
ATOM   918  C CB  . ILE A 1 129 ? 39.466 37.159  -12.046 1.00 37.74  ? 185 ILE B CB  1 
ATOM   919  C CG1 . ILE A 1 129 ? 39.024 36.871  -10.610 1.00 33.67  ? 185 ILE B CG1 1 
ATOM   920  C CG2 . ILE A 1 129 ? 40.739 36.363  -12.383 1.00 17.59  ? 185 ILE B CG2 1 
ATOM   921  C CD1 . ILE A 1 129 ? 37.607 37.325  -10.272 1.00 29.05  ? 185 ILE B CD1 1 
ATOM   922  N N   . GLY A 1 130 ? 37.589 39.953  -12.387 1.00 17.20  ? 186 GLY B N   1 
ATOM   923  C CA  . GLY A 1 130 ? 36.445 40.557  -13.050 1.00 20.01  ? 186 GLY B CA  1 
ATOM   924  C C   . GLY A 1 130 ? 36.791 41.783  -13.884 1.00 22.28  ? 186 GLY B C   1 
ATOM   925  O O   . GLY A 1 130 ? 35.998 42.242  -14.711 1.00 21.87  ? 186 GLY B O   1 
ATOM   926  N N   . GLU A 1 131 ? 37.979 42.328  -13.654 1.00 28.43  ? 187 GLU B N   1 
ATOM   927  C CA  . GLU A 1 131 ? 38.484 43.446  -14.440 1.00 32.50  ? 187 GLU B CA  1 
ATOM   928  C C   . GLU A 1 131 ? 38.980 42.974  -15.813 1.00 37.58  ? 187 GLU B C   1 
ATOM   929  O O   . GLU A 1 131 ? 39.173 43.786  -16.719 1.00 44.88  ? 187 GLU B O   1 
ATOM   930  C CB  . GLU A 1 131 ? 39.598 44.179  -13.683 1.00 36.39  ? 187 GLU B CB  1 
ATOM   931  C CG  . GLU A 1 131 ? 39.104 45.001  -12.495 1.00 45.16  ? 187 GLU B CG  1 
ATOM   932  C CD  . GLU A 1 131 ? 40.198 45.853  -11.866 1.00 59.96  ? 187 GLU B CD  1 
ATOM   933  O OE1 . GLU A 1 131 ? 41.213 46.114  -12.549 1.00 69.14  ? 187 GLU B OE1 1 
ATOM   934  O OE2 . GLU A 1 131 ? 40.044 46.261  -10.689 1.00 59.74  ? 187 GLU B OE2 1 
ATOM   935  N N   . LEU A 1 132 ? 39.155 41.664  -15.978 1.00 31.12  ? 188 LEU B N   1 
ATOM   936  C CA  . LEU A 1 132 ? 39.668 41.143  -17.229 1.00 29.42  ? 188 LEU B CA  1 
ATOM   937  C C   . LEU A 1 132 ? 38.466 40.833  -18.100 1.00 29.35  ? 188 LEU B C   1 
ATOM   938  O O   . LEU A 1 132 ? 37.804 39.812  -17.924 1.00 27.63  ? 188 LEU B O   1 
ATOM   939  C CB  . LEU A 1 132 ? 40.419 39.841  -16.963 1.00 18.66  ? 188 LEU B CB  1 
ATOM   940  C CG  . LEU A 1 132 ? 41.449 39.828  -15.837 1.00 19.76  ? 188 LEU B CG  1 
ATOM   941  C CD1 . LEU A 1 132 ? 41.843 38.414  -15.488 1.00 26.81  ? 188 LEU B CD1 1 
ATOM   942  C CD2 . LEU A 1 132 ? 42.665 40.589  -16.248 1.00 21.27  ? 188 LEU B CD2 1 
ATOM   943  N N   . LYS A 1 133 ? 38.212 41.690  -19.081 1.00 27.32  ? 189 LYS B N   1 
ATOM   944  C CA  . LYS A 1 133 ? 36.963 41.594  -19.810 1.00 19.46  ? 189 LYS B CA  1 
ATOM   945  C C   . LYS A 1 133 ? 37.080 40.719  -21.033 1.00 29.29  ? 189 LYS B C   1 
ATOM   946  O O   . LYS A 1 133 ? 36.077 40.235  -21.559 1.00 39.99  ? 189 LYS B O   1 
ATOM   947  C CB  . LYS A 1 133 ? 36.488 42.986  -20.202 1.00 20.75  ? 189 LYS B CB  1 
ATOM   948  C CG  . LYS A 1 133 ? 35.969 43.822  -19.033 1.00 31.54  ? 189 LYS B CG  1 
ATOM   949  C CD  . LYS A 1 133 ? 34.691 43.215  -18.473 1.00 39.42  ? 189 LYS B CD  1 
ATOM   950  C CE  . LYS A 1 133 ? 33.937 44.184  -17.573 1.00 44.48  ? 189 LYS B CE  1 
ATOM   951  N NZ  . LYS A 1 133 ? 34.613 44.397  -16.269 1.00 49.01  ? 189 LYS B NZ  1 
ATOM   952  N N   . ASN A 1 134 ? 38.312 40.511  -21.477 1.00 33.39  ? 190 ASN B N   1 
ATOM   953  C CA  . ASN A 1 134 ? 38.591 39.671  -22.639 1.00 38.89  ? 190 ASN B CA  1 
ATOM   954  C C   . ASN A 1 134 ? 39.107 38.267  -22.295 1.00 39.54  ? 190 ASN B C   1 
ATOM   955  O O   . ASN A 1 134 ? 39.476 37.504  -23.188 1.00 42.23  ? 190 ASN B O   1 
ATOM   956  C CB  . ASN A 1 134 ? 39.511 40.391  -23.625 1.00 50.45  ? 190 ASN B CB  1 
ATOM   957  C CG  . ASN A 1 134 ? 40.878 40.646  -23.048 1.00 75.76  ? 190 ASN B CG  1 
ATOM   958  O OD1 . ASN A 1 134 ? 41.070 40.614  -21.819 1.00 88.79  ? 190 ASN B OD1 1 
ATOM   959  N ND2 . ASN A 1 134 ? 41.851 40.895  -23.924 1.00 82.12  ? 190 ASN B ND2 1 
ATOM   960  N N   . LEU A 1 135 ? 39.169 37.945  -21.003 1.00 40.69  ? 191 LEU B N   1 
ATOM   961  C CA  . LEU A 1 135 ? 39.634 36.631  -20.564 1.00 15.47  ? 191 LEU B CA  1 
ATOM   962  C C   . LEU A 1 135 ? 38.698 35.545  -21.049 1.00 21.65  ? 191 LEU B C   1 
ATOM   963  O O   . LEU A 1 135 ? 37.479 35.689  -21.005 1.00 23.59  ? 191 LEU B O   1 
ATOM   964  C CB  . LEU A 1 135 ? 39.763 36.563  -19.047 1.00 19.99  ? 191 LEU B CB  1 
ATOM   965  C CG  . LEU A 1 135 ? 40.482 35.337  -18.477 1.00 15.76  ? 191 LEU B CG  1 
ATOM   966  C CD1 . LEU A 1 135 ? 41.890 35.208  -19.036 1.00 16.83  ? 191 LEU B CD1 1 
ATOM   967  C CD2 . LEU A 1 135 ? 40.519 35.413  -16.953 1.00 18.47  ? 191 LEU B CD2 1 
ATOM   968  N N   . GLN A 1 136 ? 39.296 34.452  -21.505 1.00 20.18  ? 192 GLN B N   1 
ATOM   969  C CA  . GLN A 1 136 ? 38.602 33.375  -22.200 1.00 19.03  ? 192 GLN B CA  1 
ATOM   970  C C   . GLN A 1 136 ? 38.819 32.041  -21.511 1.00 19.45  ? 192 GLN B C   1 
ATOM   971  O O   . GLN A 1 136 ? 37.878 31.301  -21.239 1.00 20.59  ? 192 GLN B O   1 
ATOM   972  C CB  . GLN A 1 136 ? 39.039 33.304  -23.658 1.00 20.70  ? 192 GLN B CB  1 
ATOM   973  C CG  . GLN A 1 136 ? 38.199 34.156  -24.571 1.00 12.38  ? 192 GLN B CG  1 
ATOM   974  C CD  . GLN A 1 136 ? 38.757 34.196  -25.968 1.00 22.17  ? 192 GLN B CD  1 
ATOM   975  O OE1 . GLN A 1 136 ? 39.235 33.189  -26.485 1.00 29.21  ? 192 GLN B OE1 1 
ATOM   976  N NE2 . GLN A 1 136 ? 38.709 35.361  -26.586 1.00 13.21  ? 192 GLN B NE2 1 
ATOM   977  N N   . VAL A 1 137 ? 40.087 31.688  -21.357 1.00 18.05  ? 193 VAL B N   1 
ATOM   978  C CA  . VAL A 1 137 ? 40.460 30.505  -20.610 1.00 16.58  ? 193 VAL B CA  1 
ATOM   979  C C   . VAL A 1 137 ? 41.166 30.872  -19.312 1.00 18.52  ? 193 VAL B C   1 
ATOM   980  O O   . VAL A 1 137 ? 42.198 31.533  -19.305 1.00 16.47  ? 193 VAL B O   1 
ATOM   981  C CB  . VAL A 1 137 ? 41.336 29.573  -21.458 1.00 17.90  ? 193 VAL B CB  1 
ATOM   982  C CG1 . VAL A 1 137 ? 41.882 28.425  -20.625 1.00 16.85  ? 193 VAL B CG1 1 
ATOM   983  C CG2 . VAL A 1 137 ? 40.522 29.048  -22.612 1.00 23.01  ? 193 VAL B CG2 1 
ATOM   984  N N   . LEU A 1 138 ? 40.577 30.452  -18.205 1.00 22.01  ? 194 LEU B N   1 
ATOM   985  C CA  . LEU A 1 138 ? 41.254 30.519  -16.927 1.00 21.80  ? 194 LEU B CA  1 
ATOM   986  C C   . LEU A 1 138 ? 41.357 29.104  -16.432 1.00 16.33  ? 194 LEU B C   1 
ATOM   987  O O   . LEU A 1 138 ? 40.344 28.475  -16.152 1.00 12.27  ? 194 LEU B O   1 
ATOM   988  C CB  . LEU A 1 138 ? 40.454 31.365  -15.937 1.00 23.63  ? 194 LEU B CB  1 
ATOM   989  C CG  . LEU A 1 138 ? 40.741 31.206  -14.448 1.00 20.21  ? 194 LEU B CG  1 
ATOM   990  C CD1 . LEU A 1 138 ? 42.191 31.497  -14.113 1.00 23.10  ? 194 LEU B CD1 1 
ATOM   991  C CD2 . LEU A 1 138 ? 39.826 32.132  -13.697 1.00 23.29  ? 194 LEU B CD2 1 
ATOM   992  N N   . ARG A 1 139 ? 42.574 28.584  -16.367 1.00 19.72  ? 195 ARG B N   1 
ATOM   993  C CA  . ARG A 1 139 ? 42.774 27.282  -15.762 1.00 25.73  ? 195 ARG B CA  1 
ATOM   994  C C   . ARG A 1 139 ? 43.877 27.328  -14.719 1.00 27.58  ? 195 ARG B C   1 
ATOM   995  O O   . ARG A 1 139 ? 45.064 27.380  -15.071 1.00 15.99  ? 195 ARG B O   1 
ATOM   996  C CB  . ARG A 1 139 ? 43.127 26.283  -16.859 1.00 13.51  ? 195 ARG B CB  1 
ATOM   997  C CG  . ARG A 1 139 ? 41.961 25.974  -17.740 1.00 12.25  ? 195 ARG B CG  1 
ATOM   998  C CD  . ARG A 1 139 ? 42.336 24.995  -18.803 1.00 17.12  ? 195 ARG B CD  1 
ATOM   999  N NE  . ARG A 1 139 ? 43.034 23.825  -18.287 1.00 17.64  ? 195 ARG B NE  1 
ATOM   1000 C CZ  . ARG A 1 139 ? 43.569 22.905  -19.080 1.00 17.55  ? 195 ARG B CZ  1 
ATOM   1001 N NH1 . ARG A 1 139 ? 44.200 21.859  -18.571 1.00 16.98  ? 195 ARG B NH1 1 
ATOM   1002 N NH2 . ARG A 1 139 ? 43.472 23.046  -20.393 1.00 12.04  ? 195 ARG B NH2 1 
ATOM   1003 N N   . ALA A 1 140 ? 43.452 27.323  -13.448 1.00 23.04  ? 196 ALA B N   1 
ATOM   1004 C CA  . ALA A 1 140 ? 44.324 27.316  -12.263 1.00 19.44  ? 196 ALA B CA  1 
ATOM   1005 C C   . ALA A 1 140 ? 44.386 26.038  -11.428 1.00 30.79  ? 196 ALA B C   1 
ATOM   1006 O O   . ALA A 1 140 ? 45.035 26.019  -10.384 1.00 40.37  ? 196 ALA B O   1 
ATOM   1007 C CB  . ALA A 1 140 ? 44.043 28.513  -11.386 1.00 16.15  ? 196 ALA B CB  1 
ATOM   1008 N N   . GLY A 1 141 ? 43.685 24.992  -11.845 1.00 34.05  ? 197 GLY B N   1 
ATOM   1009 C CA  . GLY A 1 141 ? 43.549 23.802  -11.017 1.00 27.45  ? 197 GLY B CA  1 
ATOM   1010 C C   . GLY A 1 141 ? 44.858 23.074  -10.773 1.00 28.91  ? 197 GLY B C   1 
ATOM   1011 O O   . GLY A 1 141 ? 45.902 23.476  -11.275 1.00 38.08  ? 197 GLY B O   1 
ATOM   1012 N N   . GLY A 1 142 ? 44.818 22.003  -9.988  1.00 22.48  ? 198 GLY B N   1 
ATOM   1013 C CA  . GLY A 1 142 ? 46.041 21.298  -9.651  1.00 19.49  ? 198 GLY B CA  1 
ATOM   1014 C C   . GLY A 1 142 ? 46.951 22.149  -8.778  1.00 21.01  ? 198 GLY B C   1 
ATOM   1015 O O   . GLY A 1 142 ? 48.181 22.037  -8.843  1.00 18.38  ? 198 GLY B O   1 
ATOM   1016 N N   . ASN A 1 143 ? 46.337 23.034  -7.993  1.00 15.94  ? 199 ASN B N   1 
ATOM   1017 C CA  . ASN A 1 143 ? 46.997 23.704  -6.884  1.00 17.03  ? 199 ASN B CA  1 
ATOM   1018 C C   . ASN A 1 143 ? 46.222 23.322  -5.645  1.00 23.77  ? 199 ASN B C   1 
ATOM   1019 O O   . ASN A 1 143 ? 45.098 23.790  -5.456  1.00 25.15  ? 199 ASN B O   1 
ATOM   1020 C CB  . ASN A 1 143 ? 46.928 25.225  -7.034  1.00 17.71  ? 199 ASN B CB  1 
ATOM   1021 C CG  . ASN A 1 143 ? 47.783 25.748  -8.174  1.00 36.96  ? 199 ASN B CG  1 
ATOM   1022 O OD1 . ASN A 1 143 ? 48.868 25.239  -8.440  1.00 36.51  ? 199 ASN B OD1 1 
ATOM   1023 N ND2 . ASN A 1 143 ? 47.294 26.779  -8.849  1.00 37.01  ? 199 ASN B ND2 1 
ATOM   1024 N N   . LYS A 1 144 ? 46.815 22.504  -4.779  1.00 23.92  ? 200 LYS B N   1 
ATOM   1025 C CA  . LYS A 1 144 ? 46.055 21.949  -3.665  1.00 24.26  ? 200 LYS B CA  1 
ATOM   1026 C C   . LYS A 1 144 ? 45.657 22.984  -2.616  1.00 21.90  ? 200 LYS B C   1 
ATOM   1027 O O   . LYS A 1 144 ? 44.666 22.794  -1.906  1.00 17.42  ? 200 LYS B O   1 
ATOM   1028 C CB  . LYS A 1 144 ? 46.785 20.766  -3.020  1.00 27.04  ? 200 LYS B CB  1 
ATOM   1029 C CG  . LYS A 1 144 ? 45.865 19.830  -2.240  1.00 32.29  ? 200 LYS B CG  1 
ATOM   1030 C CD  . LYS A 1 144 ? 46.380 18.389  -2.256  1.00 36.92  ? 200 LYS B CD  1 
ATOM   1031 C CE  . LYS A 1 144 ? 46.114 17.675  -0.922  1.00 37.08  ? 200 LYS B CE  1 
ATOM   1032 N NZ  . LYS A 1 144 ? 44.677 17.689  -0.478  1.00 34.38  ? 200 LYS B NZ  1 
ATOM   1033 N N   . ASN A 1 145 ? 46.428 24.061  -2.498  1.00 17.41  ? 201 ASN B N   1 
ATOM   1034 C CA  . ASN A 1 145 ? 46.124 25.070  -1.481  1.00 38.44  ? 201 ASN B CA  1 
ATOM   1035 C C   . ASN A 1 145 ? 45.406 26.329  -1.933  1.00 44.88  ? 201 ASN B C   1 
ATOM   1036 O O   . ASN A 1 145 ? 45.108 27.195  -1.112  1.00 51.61  ? 201 ASN B O   1 
ATOM   1037 C CB  . ASN A 1 145 ? 47.355 25.401  -0.642  1.00 34.39  ? 201 ASN B CB  1 
ATOM   1038 C CG  . ASN A 1 145 ? 47.722 24.271  0.280   1.00 30.41  ? 201 ASN B CG  1 
ATOM   1039 O OD1 . ASN A 1 145 ? 46.869 23.755  1.010   1.00 18.31  ? 201 ASN B OD1 1 
ATOM   1040 N ND2 . ASN A 1 145 ? 48.975 23.838  0.220   1.00 29.38  ? 201 ASN B ND2 1 
ATOM   1041 N N   . LEU A 1 146 ? 45.144 26.430  -3.233  1.00 43.90  ? 202 LEU B N   1 
ATOM   1042 C CA  . LEU A 1 146 ? 44.342 27.523  -3.763  1.00 37.89  ? 202 LEU B CA  1 
ATOM   1043 C C   . LEU A 1 146 ? 42.941 27.341  -3.191  1.00 35.59  ? 202 LEU B C   1 
ATOM   1044 O O   . LEU A 1 146 ? 42.321 26.289  -3.365  1.00 33.63  ? 202 LEU B O   1 
ATOM   1045 C CB  . LEU A 1 146 ? 44.334 27.475  -5.301  1.00 35.96  ? 202 LEU B CB  1 
ATOM   1046 C CG  . LEU A 1 146 ? 43.993 28.724  -6.127  1.00 28.72  ? 202 LEU B CG  1 
ATOM   1047 C CD1 . LEU A 1 146 ? 42.502 28.985  -6.160  1.00 15.92  ? 202 LEU B CD1 1 
ATOM   1048 C CD2 . LEU A 1 146 ? 44.730 29.937  -5.595  1.00 30.36  ? 202 LEU B CD2 1 
ATOM   1049 N N   . ARG A 1 147 ? 42.438 28.372  -2.522  1.00 16.23  ? 203 ARG B N   1 
ATOM   1050 C CA  . ARG A 1 147 ? 41.257 28.222  -1.683  1.00 39.80  ? 203 ARG B CA  1 
ATOM   1051 C C   . ARG A 1 147 ? 40.356 29.445  -1.656  1.00 34.72  ? 203 ARG B C   1 
ATOM   1052 O O   . ARG A 1 147 ? 40.546 30.408  -2.406  1.00 37.54  ? 203 ARG B O   1 
ATOM   1053 C CB  . ARG A 1 147 ? 41.673 27.883  -0.246  1.00 41.15  ? 203 ARG B CB  1 
ATOM   1054 C CG  . ARG A 1 147 ? 42.516 28.967  0.430   1.00 50.01  ? 203 ARG B CG  1 
ATOM   1055 C CD  . ARG A 1 147 ? 42.892 28.589  1.864   1.00 62.90  ? 203 ARG B CD  1 
ATOM   1056 N NE  . ARG A 1 147 ? 41.721 28.492  2.735   1.00 66.13  ? 203 ARG B NE  1 
ATOM   1057 C CZ  . ARG A 1 147 ? 41.273 29.476  3.509   1.00 60.12  ? 203 ARG B CZ  1 
ATOM   1058 N NH1 . ARG A 1 147 ? 41.903 30.642  3.540   1.00 60.49  ? 203 ARG B NH1 1 
ATOM   1059 N NH2 . ARG A 1 147 ? 40.195 29.292  4.257   1.00 60.79  ? 203 ARG B NH2 1 
ATOM   1060 N N   . GLY A 1 148 ? 39.371 29.390  -0.765  1.00 24.68  ? 204 GLY B N   1 
ATOM   1061 C CA  . GLY A 1 148 ? 38.396 30.450  -0.629  1.00 15.80  ? 204 GLY B CA  1 
ATOM   1062 C C   . GLY A 1 148 ? 37.203 30.237  -1.528  1.00 19.07  ? 204 GLY B C   1 
ATOM   1063 O O   . GLY A 1 148 ? 37.179 29.320  -2.355  1.00 24.73  ? 204 GLY B O   1 
ATOM   1064 N N   . GLU A 1 149 ? 36.193 31.079  -1.353  1.00 19.96  ? 205 GLU B N   1 
ATOM   1065 C CA  . GLU A 1 149 ? 35.055 31.077  -2.257  1.00 22.21  ? 205 GLU B CA  1 
ATOM   1066 C C   . GLU A 1 149 ? 35.489 31.525  -3.665  1.00 24.21  ? 205 GLU B C   1 
ATOM   1067 O O   . GLU A 1 149 ? 36.486 32.226  -3.829  1.00 17.08  ? 205 GLU B O   1 
ATOM   1068 C CB  . GLU A 1 149 ? 33.940 31.979  -1.713  1.00 18.32  ? 205 GLU B CB  1 
ATOM   1069 C CG  . GLU A 1 149 ? 33.281 31.468  -0.440  1.00 20.55  ? 205 GLU B CG  1 
ATOM   1070 C CD  . GLU A 1 149 ? 31.763 31.605  -0.454  1.00 41.83  ? 205 GLU B CD  1 
ATOM   1071 O OE1 . GLU A 1 149 ? 31.147 31.569  0.627   1.00 49.75  ? 205 GLU B OE1 1 
ATOM   1072 O OE2 . GLU A 1 149 ? 31.177 31.733  -1.546  1.00 55.25  ? 205 GLU B OE2 1 
ATOM   1073 N N   . LEU A 1 150 ? 34.755 31.101  -4.687  1.00 28.94  ? 206 LEU B N   1 
ATOM   1074 C CA  . LEU A 1 150 ? 34.997 31.622  -6.023  1.00 23.98  ? 206 LEU B CA  1 
ATOM   1075 C C   . LEU A 1 150 ? 34.427 33.035  -6.022  1.00 22.32  ? 206 LEU B C   1 
ATOM   1076 O O   . LEU A 1 150 ? 33.251 33.226  -5.709  1.00 23.27  ? 206 LEU B O   1 
ATOM   1077 C CB  . LEU A 1 150 ? 34.327 30.736  -7.077  1.00 22.83  ? 206 LEU B CB  1 
ATOM   1078 C CG  . LEU A 1 150 ? 34.525 31.050  -8.567  1.00 32.70  ? 206 LEU B CG  1 
ATOM   1079 C CD1 . LEU A 1 150 ? 35.996 31.054  -8.956  1.00 33.41  ? 206 LEU B CD1 1 
ATOM   1080 C CD2 . LEU A 1 150 ? 33.747 30.069  -9.437  1.00 31.08  ? 206 LEU B CD2 1 
ATOM   1081 N N   . PRO A 1 151 ? 35.265 34.036  -6.341  1.00 22.50  ? 207 PRO B N   1 
ATOM   1082 C CA  . PRO A 1 151 ? 34.830 35.436  -6.242  1.00 13.46  ? 207 PRO B CA  1 
ATOM   1083 C C   . PRO A 1 151 ? 33.580 35.720  -7.056  1.00 17.83  ? 207 PRO B C   1 
ATOM   1084 O O   . PRO A 1 151 ? 33.349 35.077  -8.065  1.00 28.74  ? 207 PRO B O   1 
ATOM   1085 C CB  . PRO A 1 151 ? 36.026 36.225  -6.792  1.00 22.34  ? 207 PRO B CB  1 
ATOM   1086 C CG  . PRO A 1 151 ? 36.875 35.228  -7.507  1.00 14.65  ? 207 PRO B CG  1 
ATOM   1087 C CD  . PRO A 1 151 ? 36.657 33.923  -6.812  1.00 19.63  ? 207 PRO B CD  1 
ATOM   1088 N N   . TRP A 1 152 ? 32.779 36.668  -6.598  1.00 12.60  ? 208 TRP B N   1 
ATOM   1089 C CA  . TRP A 1 152 ? 31.529 37.013  -7.247  1.00 25.40  ? 208 TRP B CA  1 
ATOM   1090 C C   . TRP A 1 152 ? 31.862 37.617  -8.610  1.00 27.06  ? 208 TRP B C   1 
ATOM   1091 O O   . TRP A 1 152 ? 31.259 37.290  -9.648  1.00 32.75  ? 208 TRP B O   1 
ATOM   1092 C CB  . TRP A 1 152 ? 30.776 38.022  -6.372  1.00 12.04  ? 208 TRP B CB  1 
ATOM   1093 C CG  . TRP A 1 152 ? 29.491 38.484  -6.954  1.00 28.72  ? 208 TRP B CG  1 
ATOM   1094 C CD1 . TRP A 1 152 ? 29.274 39.625  -7.692  1.00 28.17  ? 208 TRP B CD1 1 
ATOM   1095 C CD2 . TRP A 1 152 ? 28.230 37.816  -6.865  1.00 25.07  ? 208 TRP B CD2 1 
ATOM   1096 N NE1 . TRP A 1 152 ? 27.949 39.703  -8.063  1.00 22.18  ? 208 TRP B NE1 1 
ATOM   1097 C CE2 . TRP A 1 152 ? 27.288 38.606  -7.570  1.00 23.08  ? 208 TRP B CE2 1 
ATOM   1098 C CE3 . TRP A 1 152 ? 27.805 36.624  -6.268  1.00 22.63  ? 208 TRP B CE3 1 
ATOM   1099 C CZ2 . TRP A 1 152 ? 25.942 38.236  -7.684  1.00 20.04  ? 208 TRP B CZ2 1 
ATOM   1100 C CZ3 . TRP A 1 152 ? 26.470 36.260  -6.383  1.00 20.88  ? 208 TRP B CZ3 1 
ATOM   1101 C CH2 . TRP A 1 152 ? 25.553 37.068  -7.083  1.00 18.53  ? 208 TRP B CH2 1 
ATOM   1102 N N   . GLU A 1 153 ? 32.892 38.452  -8.595  1.00 24.36  ? 209 GLU B N   1 
ATOM   1103 C CA  . GLU A 1 153 ? 33.308 39.240  -9.739  1.00 23.64  ? 209 GLU B CA  1 
ATOM   1104 C C   . GLU A 1 153 ? 33.675 38.390  -10.955 1.00 25.88  ? 209 GLU B C   1 
ATOM   1105 O O   . GLU A 1 153 ? 33.829 38.919  -12.057 1.00 25.05  ? 209 GLU B O   1 
ATOM   1106 C CB  . GLU A 1 153 ? 34.494 40.112  -9.337  1.00 26.01  ? 209 GLU B CB  1 
ATOM   1107 C CG  . GLU A 1 153 ? 34.181 41.137  -8.248  1.00 35.49  ? 209 GLU B CG  1 
ATOM   1108 C CD  . GLU A 1 153 ? 34.057 40.548  -6.851  1.00 38.82  ? 209 GLU B CD  1 
ATOM   1109 O OE1 . GLU A 1 153 ? 33.930 39.314  -6.710  1.00 37.97  ? 209 GLU B OE1 1 
ATOM   1110 O OE2 . GLU A 1 153 ? 34.085 41.335  -5.885  1.00 44.85  ? 209 GLU B OE2 1 
ATOM   1111 N N   . ILE A 1 154 ? 33.818 37.081  -10.760 1.00 24.77  ? 210 ILE B N   1 
ATOM   1112 C CA  . ILE A 1 154 ? 34.052 36.166  -11.875 1.00 19.84  ? 210 ILE B CA  1 
ATOM   1113 C C   . ILE A 1 154 ? 32.961 36.265  -12.945 1.00 19.66  ? 210 ILE B C   1 
ATOM   1114 O O   . ILE A 1 154 ? 33.209 35.972  -14.111 1.00 22.01  ? 210 ILE B O   1 
ATOM   1115 C CB  . ILE A 1 154 ? 34.186 34.696  -11.407 1.00 17.08  ? 210 ILE B CB  1 
ATOM   1116 C CG1 . ILE A 1 154 ? 34.818 33.838  -12.502 1.00 11.26  ? 210 ILE B CG1 1 
ATOM   1117 C CG2 . ILE A 1 154 ? 32.830 34.128  -10.998 1.00 16.68  ? 210 ILE B CG2 1 
ATOM   1118 C CD1 . ILE A 1 154 ? 36.059 34.430  -13.102 1.00 14.65  ? 210 ILE B CD1 1 
ATOM   1119 N N   . GLY A 1 155 ? 31.765 36.703  -12.555 1.00 22.75  ? 211 GLY B N   1 
ATOM   1120 C CA  . GLY A 1 155 ? 30.674 36.828  -13.508 1.00 18.26  ? 211 GLY B CA  1 
ATOM   1121 C C   . GLY A 1 155 ? 30.917 37.968  -14.484 1.00 19.28  ? 211 GLY B C   1 
ATOM   1122 O O   . GLY A 1 155 ? 30.221 38.113  -15.488 1.00 14.01  ? 211 GLY B O   1 
ATOM   1123 N N   . ASN A 1 156 ? 31.914 38.791  -14.188 1.00 21.79  ? 212 ASN B N   1 
ATOM   1124 C CA  . ASN A 1 156 ? 32.234 39.915  -15.046 1.00 22.62  ? 212 ASN B CA  1 
ATOM   1125 C C   . ASN A 1 156 ? 33.172 39.548  -16.182 1.00 32.85  ? 212 ASN B C   1 
ATOM   1126 O O   . ASN A 1 156 ? 33.429 40.383  -17.051 1.00 46.08  ? 212 ASN B O   1 
ATOM   1127 C CB  . ASN A 1 156 ? 32.812 41.083  -14.241 1.00 25.84  ? 212 ASN B CB  1 
ATOM   1128 C CG  . ASN A 1 156 ? 31.790 41.713  -13.307 1.00 25.22  ? 212 ASN B CG  1 
ATOM   1129 O OD1 . ASN A 1 156 ? 30.656 41.988  -13.698 1.00 22.13  ? 212 ASN B OD1 1 
ATOM   1130 N ND2 . ASN A 1 156 ? 32.190 41.937  -12.058 1.00 28.30  ? 212 ASN B ND2 1 
ATOM   1131 N N   . CYS A 1 157 ? 33.663 38.309  -16.227 1.00 27.96  ? 213 CYS B N   1 
ATOM   1132 C CA  . CYS A 1 157 ? 34.515 37.966  -17.362 1.00 31.51  ? 213 CYS B CA  1 
ATOM   1133 C C   . CYS A 1 157 ? 33.559 37.477  -18.421 1.00 34.53  ? 213 CYS B C   1 
ATOM   1134 O O   . CYS A 1 157 ? 33.160 36.313  -18.435 1.00 37.89  ? 213 CYS B O   1 
ATOM   1135 C CB  . CYS A 1 157 ? 35.458 36.828  -16.996 1.00 26.33  ? 213 CYS B CB  1 
ATOM   1136 S SG  . CYS A 1 157 ? 36.388 37.113  -15.494 1.00 23.40  ? 213 CYS B SG  1 
ATOM   1137 N N   . GLU A 1 158 ? 33.270 38.353  -19.367 1.00 31.93  ? 214 GLU B N   1 
ATOM   1138 C CA  . GLU A 1 158 ? 32.106 38.159  -20.202 1.00 40.64  ? 214 GLU B CA  1 
ATOM   1139 C C   . GLU A 1 158 ? 32.399 37.159  -21.307 1.00 40.17  ? 214 GLU B C   1 
ATOM   1140 O O   . GLU A 1 158 ? 31.497 36.474  -21.790 1.00 43.24  ? 214 GLU B O   1 
ATOM   1141 C CB  . GLU A 1 158 ? 31.640 39.500  -20.776 1.00 55.04  ? 214 GLU B CB  1 
ATOM   1142 C CG  . GLU A 1 158 ? 32.783 40.411  -21.198 1.00 60.25  ? 214 GLU B CG  1 
ATOM   1143 C CD  . GLU A 1 158 ? 32.322 41.608  -22.001 1.00 63.44  ? 214 GLU B CD  1 
ATOM   1144 O OE1 . GLU A 1 158 ? 31.494 41.434  -22.924 1.00 61.28  ? 214 GLU B OE1 1 
ATOM   1145 O OE2 . GLU A 1 158 ? 32.798 42.725  -21.711 1.00 68.33  ? 214 GLU B OE2 1 
ATOM   1146 N N   . ASN A 1 159 ? 33.667 37.075  -21.699 1.00 33.58  ? 215 ASN B N   1 
ATOM   1147 C CA  . ASN A 1 159 ? 34.070 36.228  -22.814 1.00 21.79  ? 215 ASN B CA  1 
ATOM   1148 C C   . ASN A 1 159 ? 34.554 34.851  -22.400 1.00 12.44  ? 215 ASN B C   1 
ATOM   1149 O O   . ASN A 1 159 ? 35.084 34.097  -23.218 1.00 10.00  ? 215 ASN B O   1 
ATOM   1150 C CB  . ASN A 1 159 ? 35.109 36.928  -23.682 1.00 27.42  ? 215 ASN B CB  1 
ATOM   1151 C CG  . ASN A 1 159 ? 34.568 38.192  -24.331 1.00 25.37  ? 215 ASN B CG  1 
ATOM   1152 O OD1 . ASN A 1 159 ? 33.438 38.624  -24.060 1.00 11.08  ? 215 ASN B OD1 1 
ATOM   1153 N ND2 . ASN A 1 159 ? 35.384 38.805  -25.176 1.00 24.24  ? 215 ASN B ND2 1 
ATOM   1154 N N   . LEU A 1 160 ? 34.400 34.543  -21.120 1.00 18.53  ? 216 LEU B N   1 
ATOM   1155 C CA  . LEU A 1 160 ? 34.828 33.262  -20.586 1.00 12.84  ? 216 LEU B CA  1 
ATOM   1156 C C   . LEU A 1 160 ? 34.235 32.089  -21.346 1.00 16.20  ? 216 LEU B C   1 
ATOM   1157 O O   . LEU A 1 160 ? 33.078 32.096  -21.771 1.00 19.68  ? 216 LEU B O   1 
ATOM   1158 C CB  . LEU A 1 160 ? 34.490 33.143  -19.099 1.00 15.10  ? 216 LEU B CB  1 
ATOM   1159 C CG  . LEU A 1 160 ? 35.646 33.221  -18.096 1.00 19.86  ? 216 LEU B CG  1 
ATOM   1160 C CD1 . LEU A 1 160 ? 35.140 32.890  -16.707 1.00 20.21  ? 216 LEU B CD1 1 
ATOM   1161 C CD2 . LEU A 1 160 ? 36.795 32.301  -18.459 1.00 11.03  ? 216 LEU B CD2 1 
ATOM   1162 N N   . VAL A 1 161 ? 35.082 31.088  -21.510 1.00 20.29  ? 217 VAL B N   1 
ATOM   1163 C CA  . VAL A 1 161 ? 34.835 29.903  -22.319 1.00 22.77  ? 217 VAL B CA  1 
ATOM   1164 C C   . VAL A 1 161 ? 35.176 28.654  -21.489 1.00 21.23  ? 217 VAL B C   1 
ATOM   1165 O O   . VAL A 1 161 ? 34.453 27.655  -21.516 1.00 19.20  ? 217 VAL B O   1 
ATOM   1166 C CB  . VAL A 1 161 ? 35.516 29.999  -23.723 1.00 9.89   ? 217 VAL B CB  1 
ATOM   1167 C CG1 . VAL A 1 161 ? 36.246 28.739  -24.086 1.00 8.17   ? 217 VAL B CG1 1 
ATOM   1168 C CG2 . VAL A 1 161 ? 34.472 30.340  -24.773 1.00 12.23  ? 217 VAL B CG2 1 
ATOM   1169 N N   . MET A 1 162 ? 36.358 28.684  -20.880 1.00 8.57   ? 218 MET B N   1 
ATOM   1170 C CA  . MET A 1 162 ? 36.834 27.613  -20.014 1.00 14.20  ? 218 MET B CA  1 
ATOM   1171 C C   . MET A 1 162 ? 37.199 28.082  -18.578 1.00 18.37  ? 218 MET B C   1 
ATOM   1172 O O   . MET A 1 162 ? 38.083 28.920  -18.354 1.00 15.16  ? 218 MET B O   1 
ATOM   1173 C CB  . MET A 1 162 ? 38.021 26.902  -20.673 1.00 9.08   ? 218 MET B CB  1 
ATOM   1174 C CG  . MET A 1 162 ? 38.854 26.087  -19.712 1.00 9.48   ? 218 MET B CG  1 
ATOM   1175 S SD  . MET A 1 162 ? 38.279 24.396  -19.612 1.00 17.45  ? 218 MET B SD  1 
ATOM   1176 C CE  . MET A 1 162 ? 38.792 23.962  -17.945 1.00 25.10  ? 218 MET B CE  1 
ATOM   1177 N N   . LEU A 1 163 ? 36.499 27.539  -17.598 1.00 8.52   ? 219 LEU B N   1 
ATOM   1178 C CA  . LEU A 1 163 ? 36.872 27.788  -16.216 1.00 14.67  ? 219 LEU B CA  1 
ATOM   1179 C C   . LEU A 1 163 ? 37.202 26.464  -15.582 1.00 8.81   ? 219 LEU B C   1 
ATOM   1180 O O   . LEU A 1 163 ? 36.332 25.611  -15.455 1.00 7.75   ? 219 LEU B O   1 
ATOM   1181 C CB  . LEU A 1 163 ? 35.724 28.446  -15.445 1.00 14.15  ? 219 LEU B CB  1 
ATOM   1182 C CG  . LEU A 1 163 ? 35.921 28.725  -13.949 1.00 12.50  ? 219 LEU B CG  1 
ATOM   1183 C CD1 . LEU A 1 163 ? 37.023 29.751  -13.727 1.00 17.70  ? 219 LEU B CD1 1 
ATOM   1184 C CD2 . LEU A 1 163 ? 34.620 29.218  -13.330 1.00 8.49   ? 219 LEU B CD2 1 
ATOM   1185 N N   . GLY A 1 164 ? 38.445 26.257  -15.191 1.00 9.75   ? 220 GLY B N   1 
ATOM   1186 C CA  . GLY A 1 164 ? 38.595 25.182  -14.257 1.00 18.23  ? 220 GLY B CA  1 
ATOM   1187 C C   . GLY A 1 164 ? 39.679 25.243  -13.222 1.00 23.34  ? 220 GLY B C   1 
ATOM   1188 O O   . GLY A 1 164 ? 40.862 25.486  -13.439 1.00 26.73  ? 220 GLY B O   1 
ATOM   1189 N N   . LEU A 1 165 ? 39.141 24.951  -12.049 1.00 25.55  ? 221 LEU B N   1 
ATOM   1190 C CA  . LEU A 1 165 ? 39.748 24.965  -10.742 1.00 15.50  ? 221 LEU B CA  1 
ATOM   1191 C C   . LEU A 1 165 ? 39.890 23.562  -10.167 1.00 14.13  ? 221 LEU B C   1 
ATOM   1192 O O   . LEU A 1 165 ? 39.916 23.406  -8.957  1.00 22.44  ? 221 LEU B O   1 
ATOM   1193 C CB  . LEU A 1 165 ? 38.995 25.929  -9.829  1.00 10.78  ? 221 LEU B CB  1 
ATOM   1194 C CG  . LEU A 1 165 ? 38.934 27.336  -10.450 1.00 11.34  ? 221 LEU B CG  1 
ATOM   1195 C CD1 . LEU A 1 165 ? 37.934 28.202  -9.726  1.00 13.86  ? 221 LEU B CD1 1 
ATOM   1196 C CD2 . LEU A 1 165 ? 40.299 28.021  -10.469 1.00 12.81  ? 221 LEU B CD2 1 
ATOM   1197 N N   . ALA A 1 166 ? 39.782 22.541  -11.010 1.00 13.23  ? 222 ALA B N   1 
ATOM   1198 C CA  . ALA A 1 166 ? 39.760 21.166  -10.525 1.00 9.09   ? 222 ALA B CA  1 
ATOM   1199 C C   . ALA A 1 166 ? 40.945 20.842  -9.618  1.00 27.97  ? 222 ALA B C   1 
ATOM   1200 O O   . ALA A 1 166 ? 42.036 21.405  -9.764  1.00 11.18  ? 222 ALA B O   1 
ATOM   1201 C CB  . ALA A 1 166 ? 39.711 20.201  -11.677 1.00 41.62  ? 222 ALA B CB  1 
ATOM   1202 N N   . GLU A 1 167 ? 40.701 19.963  -8.654  1.00 9.58   ? 223 GLU B N   1 
ATOM   1203 C CA  . GLU A 1 167 ? 41.734 19.540  -7.714  1.00 21.78  ? 223 GLU B CA  1 
ATOM   1204 C C   . GLU A 1 167 ? 42.358 20.685  -6.906  1.00 16.99  ? 223 GLU B C   1 
ATOM   1205 O O   . GLU A 1 167 ? 43.568 20.695  -6.658  1.00 16.37  ? 223 GLU B O   1 
ATOM   1206 C CB  . GLU A 1 167 ? 42.806 18.723  -8.421  1.00 10.85  ? 223 GLU B CB  1 
ATOM   1207 C CG  . GLU A 1 167 ? 42.350 17.349  -8.784  1.00 57.97  ? 223 GLU B CG  1 
ATOM   1208 C CD  . GLU A 1 167 ? 43.176 16.291  -8.112  1.00 60.66  ? 223 GLU B CD  1 
ATOM   1209 O OE1 . GLU A 1 167 ? 44.361 16.573  -7.810  1.00 66.39  ? 223 GLU B OE1 1 
ATOM   1210 O OE2 . GLU A 1 167 ? 42.640 15.185  -7.877  1.00 59.10  ? 223 GLU B OE2 1 
ATOM   1211 N N   . THR A 1 168 ? 41.529 21.639  -6.493  1.00 13.25  ? 224 THR B N   1 
ATOM   1212 C CA  . THR A 1 168 ? 41.976 22.682  -5.574  1.00 22.43  ? 224 THR B CA  1 
ATOM   1213 C C   . THR A 1 168 ? 41.203 22.608  -4.265  1.00 26.37  ? 224 THR B C   1 
ATOM   1214 O O   . THR A 1 168 ? 40.350 21.734  -4.087  1.00 21.51  ? 224 THR B O   1 
ATOM   1215 C CB  . THR A 1 168 ? 41.798 24.088  -6.160  1.00 12.76  ? 224 THR B CB  1 
ATOM   1216 O OG1 . THR A 1 168 ? 40.403 24.377  -6.312  1.00 11.71  ? 224 THR B OG1 1 
ATOM   1217 C CG2 . THR A 1 168 ? 42.508 24.196  -7.494  1.00 13.20  ? 224 THR B CG2 1 
ATOM   1218 N N   . SER A 1 169 ? 41.513 23.524  -3.351  1.00 12.71  ? 225 SER B N   1 
ATOM   1219 C CA  . SER A 1 169 ? 40.839 23.576  -2.053  1.00 27.32  ? 225 SER B CA  1 
ATOM   1220 C C   . SER A 1 169 ? 39.695 24.558  -2.063  1.00 11.98  ? 225 SER B C   1 
ATOM   1221 O O   . SER A 1 169 ? 39.127 24.869  -1.024  1.00 58.55  ? 225 SER B O   1 
ATOM   1222 C CB  . SER A 1 169 ? 41.819 23.902  -0.926  1.00 13.61  ? 225 SER B CB  1 
ATOM   1223 O OG  . SER A 1 169 ? 42.694 22.810  -0.724  1.00 24.24  ? 225 SER B OG  1 
ATOM   1224 N N   . LEU A 1 170 ? 39.403 25.066  -3.251  1.00 23.52  ? 226 LEU B N   1 
ATOM   1225 C CA  . LEU A 1 170 ? 38.351 26.047  -3.470  1.00 17.68  ? 226 LEU B CA  1 
ATOM   1226 C C   . LEU A 1 170 ? 37.098 25.559  -2.788  1.00 14.39  ? 226 LEU B C   1 
ATOM   1227 O O   . LEU A 1 170 ? 36.809 24.358  -2.809  1.00 13.16  ? 226 LEU B O   1 
ATOM   1228 C CB  . LEU A 1 170 ? 38.074 26.170  -4.970  1.00 10.98  ? 226 LEU B CB  1 
ATOM   1229 C CG  . LEU A 1 170 ? 37.250 27.388  -5.354  1.00 16.39  ? 226 LEU B CG  1 
ATOM   1230 C CD1 . LEU A 1 170 ? 38.103 28.390  -6.117  1.00 15.81  ? 226 LEU B CD1 1 
ATOM   1231 C CD2 . LEU A 1 170 ? 36.023 26.983  -6.138  1.00 15.88  ? 226 LEU B CD2 1 
ATOM   1232 N N   . SER A 1 171 ? 36.371 26.471  -2.152  1.00 10.36  ? 227 SER B N   1 
ATOM   1233 C CA  . SER A 1 171 ? 35.244 26.055  -1.322  1.00 27.12  ? 227 SER B CA  1 
ATOM   1234 C C   . SER A 1 171 ? 34.102 27.029  -1.407  1.00 31.76  ? 227 SER B C   1 
ATOM   1235 O O   . SER A 1 171 ? 34.173 28.031  -2.119  1.00 43.19  ? 227 SER B O   1 
ATOM   1236 C CB  . SER A 1 171 ? 35.658 25.962  0.140   1.00 22.86  ? 227 SER B CB  1 
ATOM   1237 O OG  . SER A 1 171 ? 35.410 27.201  0.774   1.00 19.57  ? 227 SER B OG  1 
ATOM   1238 N N   . GLY A 1 172 ? 33.051 26.731  -0.657  1.00 8.36   ? 228 GLY B N   1 
ATOM   1239 C CA  . GLY A 1 172 ? 31.867 27.567  -0.630  1.00 14.39  ? 228 GLY B CA  1 
ATOM   1240 C C   . GLY A 1 172 ? 30.853 27.157  -1.671  1.00 11.76  ? 228 GLY B C   1 
ATOM   1241 O O   . GLY A 1 172 ? 30.858 26.022  -2.129  1.00 17.33  ? 228 GLY B O   1 
ATOM   1242 N N   . LYS A 1 173 ? 29.983 28.089  -2.042  1.00 15.15  ? 229 LYS B N   1 
ATOM   1243 C CA  . LYS A 1 173 ? 29.045 27.885  -3.139  1.00 13.35  ? 229 LYS B CA  1 
ATOM   1244 C C   . LYS A 1 173 ? 29.516 28.618  -4.415  1.00 21.62  ? 229 LYS B C   1 
ATOM   1245 O O   . LYS A 1 173 ? 30.128 29.692  -4.347  1.00 26.40  ? 229 LYS B O   1 
ATOM   1246 C CB  . LYS A 1 173 ? 27.647 28.368  -2.740  1.00 13.56  ? 229 LYS B CB  1 
ATOM   1247 C CG  . LYS A 1 173 ? 27.442 29.881  -2.896  1.00 27.62  ? 229 LYS B CG  1 
ATOM   1248 C CD  . LYS A 1 173 ? 25.978 30.307  -2.755  1.00 33.00  ? 229 LYS B CD  1 
ATOM   1249 C CE  . LYS A 1 173 ? 25.594 30.607  -1.305  1.00 29.13  ? 229 LYS B CE  1 
ATOM   1250 N NZ  . LYS A 1 173 ? 25.566 29.374  -0.487  1.00 28.22  ? 229 LYS B NZ  1 
ATOM   1251 N N   . LEU A 1 174 ? 29.259 28.018  -5.573  1.00 17.02  ? 230 LEU B N   1 
ATOM   1252 C CA  . LEU A 1 174 ? 29.396 28.734  -6.825  1.00 17.26  ? 230 LEU B CA  1 
ATOM   1253 C C   . LEU A 1 174 ? 28.441 29.907  -6.726  1.00 18.33  ? 230 LEU B C   1 
ATOM   1254 O O   . LEU A 1 174 ? 27.278 29.729  -6.363  1.00 18.42  ? 230 LEU B O   1 
ATOM   1255 C CB  . LEU A 1 174 ? 28.956 27.867  -8.004  1.00 26.25  ? 230 LEU B CB  1 
ATOM   1256 C CG  . LEU A 1 174 ? 29.548 26.484  -8.237  1.00 25.97  ? 230 LEU B CG  1 
ATOM   1257 C CD1 . LEU A 1 174 ? 28.710 25.796  -9.276  1.00 22.47  ? 230 LEU B CD1 1 
ATOM   1258 C CD2 . LEU A 1 174 ? 30.981 26.598  -8.698  1.00 32.90  ? 230 LEU B CD2 1 
ATOM   1259 N N   . PRO A 1 175 ? 28.923 31.115  -7.045  1.00 17.84  ? 231 PRO B N   1 
ATOM   1260 C CA  . PRO A 1 175 ? 28.071 32.297  -6.888  1.00 17.21  ? 231 PRO B CA  1 
ATOM   1261 C C   . PRO A 1 175 ? 27.016 32.349  -7.967  1.00 25.80  ? 231 PRO B C   1 
ATOM   1262 O O   . PRO A 1 175 ? 27.197 31.731  -9.013  1.00 27.58  ? 231 PRO B O   1 
ATOM   1263 C CB  . PRO A 1 175 ? 29.051 33.460  -7.026  1.00 7.95   ? 231 PRO B CB  1 
ATOM   1264 C CG  . PRO A 1 175 ? 30.222 32.903  -7.744  1.00 10.65  ? 231 PRO B CG  1 
ATOM   1265 C CD  . PRO A 1 175 ? 30.295 31.449  -7.462  1.00 11.50  ? 231 PRO B CD  1 
ATOM   1266 N N   . ALA A 1 176 ? 25.928 33.075  -7.723  1.00 31.29  ? 232 ALA B N   1 
ATOM   1267 C CA  . ALA A 1 176 ? 24.882 33.228  -8.734  1.00 25.34  ? 232 ALA B CA  1 
ATOM   1268 C C   . ALA A 1 176 ? 25.415 34.027  -9.927  1.00 25.54  ? 232 ALA B C   1 
ATOM   1269 O O   . ALA A 1 176 ? 24.799 34.069  -10.990 1.00 28.95  ? 232 ALA B O   1 
ATOM   1270 C CB  . ALA A 1 176 ? 23.633 33.891  -8.127  1.00 16.32  ? 232 ALA B CB  1 
ATOM   1271 N N   . SER A 1 177 ? 26.586 34.625  -9.730  1.00 25.82  ? 233 SER B N   1 
ATOM   1272 C CA  . SER A 1 177 ? 27.322 35.365  -10.743 1.00 26.09  ? 233 SER B CA  1 
ATOM   1273 C C   . SER A 1 177 ? 27.467 34.581  -12.043 1.00 30.41  ? 233 SER B C   1 
ATOM   1274 O O   . SER A 1 177 ? 27.581 35.166  -13.119 1.00 32.85  ? 233 SER B O   1 
ATOM   1275 C CB  . SER A 1 177 ? 28.730 35.644  -10.208 1.00 29.79  ? 233 SER B CB  1 
ATOM   1276 O OG  . SER A 1 177 ? 28.827 36.917  -9.610  1.00 39.82  ? 233 SER B OG  1 
ATOM   1277 N N   . ILE A 1 178 ? 27.474 33.255  -11.932 1.00 30.28  ? 234 ILE B N   1 
ATOM   1278 C CA  . ILE A 1 178 ? 27.702 32.379  -13.076 1.00 27.23  ? 234 ILE B CA  1 
ATOM   1279 C C   . ILE A 1 178 ? 26.559 32.492  -14.101 1.00 27.66  ? 234 ILE B C   1 
ATOM   1280 O O   . ILE A 1 178 ? 26.697 32.122  -15.264 1.00 26.37  ? 234 ILE B O   1 
ATOM   1281 C CB  . ILE A 1 178 ? 28.058 30.920  -12.632 1.00 29.98  ? 234 ILE B CB  1 
ATOM   1282 C CG1 . ILE A 1 178 ? 29.532 30.825  -12.259 1.00 29.39  ? 234 ILE B CG1 1 
ATOM   1283 C CG2 . ILE A 1 178 ? 27.916 29.934  -13.754 1.00 41.60  ? 234 ILE B CG2 1 
ATOM   1284 C CD1 . ILE A 1 178 ? 29.905 31.539  -11.012 1.00 42.87  ? 234 ILE B CD1 1 
ATOM   1285 N N   . GLY A 1 179 ? 25.449 33.078  -13.673 1.00 30.70  ? 235 GLY B N   1 
ATOM   1286 C CA  . GLY A 1 179 ? 24.378 33.413  -14.588 1.00 27.85  ? 235 GLY B CA  1 
ATOM   1287 C C   . GLY A 1 179 ? 24.845 34.294  -15.734 1.00 24.09  ? 235 GLY B C   1 
ATOM   1288 O O   . GLY A 1 179 ? 24.269 34.260  -16.832 1.00 21.66  ? 235 GLY B O   1 
ATOM   1289 N N   . ASN A 1 180 ? 25.897 35.074  -15.488 1.00 19.81  ? 236 ASN B N   1 
ATOM   1290 C CA  . ASN A 1 180 ? 26.367 36.056  -16.471 1.00 21.55  ? 236 ASN B CA  1 
ATOM   1291 C C   . ASN A 1 180 ? 27.325 35.569  -17.586 1.00 20.09  ? 236 ASN B C   1 
ATOM   1292 O O   . ASN A 1 180 ? 27.492 36.253  -18.589 1.00 14.34  ? 236 ASN B O   1 
ATOM   1293 C CB  . ASN A 1 180 ? 26.941 37.301  -15.782 1.00 16.37  ? 236 ASN B CB  1 
ATOM   1294 C CG  . ASN A 1 180 ? 25.864 38.291  -15.365 1.00 23.32  ? 236 ASN B CG  1 
ATOM   1295 O OD1 . ASN A 1 180 ? 25.249 38.140  -14.317 1.00 19.76  ? 236 ASN B OD1 1 
ATOM   1296 N ND2 . ASN A 1 180 ? 25.652 39.323  -16.174 1.00 34.79  ? 236 ASN B ND2 1 
ATOM   1297 N N   . LEU A 1 181 ? 27.924 34.391  -17.458 1.00 20.24  ? 237 LEU B N   1 
ATOM   1298 C CA  . LEU A 1 181 ? 28.863 33.980  -18.486 1.00 30.65  ? 237 LEU B CA  1 
ATOM   1299 C C   . LEU A 1 181 ? 28.035 33.255  -19.524 1.00 29.57  ? 237 LEU B C   1 
ATOM   1300 O O   . LEU A 1 181 ? 27.703 32.089  -19.344 1.00 24.60  ? 237 LEU B O   1 
ATOM   1301 C CB  . LEU A 1 181 ? 29.872 32.963  -17.934 1.00 37.36  ? 237 LEU B CB  1 
ATOM   1302 C CG  . LEU A 1 181 ? 30.671 32.994  -16.621 1.00 32.56  ? 237 LEU B CG  1 
ATOM   1303 C CD1 . LEU A 1 181 ? 29.857 33.382  -15.424 1.00 39.26  ? 237 LEU B CD1 1 
ATOM   1304 C CD2 . LEU A 1 181 ? 31.262 31.606  -16.368 1.00 31.30  ? 237 LEU B CD2 1 
ATOM   1305 N N   . LYS A 1 182 ? 27.786 33.926  -20.643 1.00 33.08  ? 238 LYS B N   1 
ATOM   1306 C CA  . LYS A 1 182 ? 26.874 33.440  -21.668 1.00 20.06  ? 238 LYS B CA  1 
ATOM   1307 C C   . LYS A 1 182 ? 27.602 32.700  -22.784 1.00 14.36  ? 238 LYS B C   1 
ATOM   1308 O O   . LYS A 1 182 ? 26.981 32.128  -23.656 1.00 3.48   ? 238 LYS B O   1 
ATOM   1309 C CB  . LYS A 1 182 ? 26.095 34.623  -22.246 1.00 21.15  ? 238 LYS B CB  1 
ATOM   1310 C CG  . LYS A 1 182 ? 24.625 34.678  -21.849 1.00 26.28  ? 238 LYS B CG  1 
ATOM   1311 C CD  . LYS A 1 182 ? 24.399 35.365  -20.526 1.00 23.53  ? 238 LYS B CD  1 
ATOM   1312 C CE  . LYS A 1 182 ? 22.899 35.482  -20.226 1.00 32.14  ? 238 LYS B CE  1 
ATOM   1313 N NZ  . LYS A 1 182 ? 22.608 35.687  -18.763 1.00 36.76  ? 238 LYS B NZ  1 
ATOM   1314 N N   . ARG A 1 183 ? 28.923 32.797  -22.789 1.00 15.15  ? 239 ARG B N   1 
ATOM   1315 C CA  . ARG A 1 183 ? 29.757 32.041  -23.700 1.00 7.77   ? 239 ARG B CA  1 
ATOM   1316 C C   . ARG A 1 183 ? 30.476 30.837  -23.081 1.00 21.81  ? 239 ARG B C   1 
ATOM   1317 O O   . ARG A 1 183 ? 31.198 30.144  -23.798 1.00 29.39  ? 239 ARG B O   1 
ATOM   1318 C CB  . ARG A 1 183 ? 30.779 32.971  -24.347 1.00 11.60  ? 239 ARG B CB  1 
ATOM   1319 C CG  . ARG A 1 183 ? 30.304 34.405  -24.492 1.00 12.81  ? 239 ARG B CG  1 
ATOM   1320 C CD  . ARG A 1 183 ? 31.291 35.224  -25.296 1.00 33.03  ? 239 ARG B CD  1 
ATOM   1321 N NE  . ARG A 1 183 ? 30.937 35.226  -26.716 1.00 55.30  ? 239 ARG B NE  1 
ATOM   1322 C CZ  . ARG A 1 183 ? 31.051 36.282  -27.524 1.00 62.40  ? 239 ARG B CZ  1 
ATOM   1323 N NH1 . ARG A 1 183 ? 31.521 37.435  -27.064 1.00 63.68  ? 239 ARG B NH1 1 
ATOM   1324 N NH2 . ARG A 1 183 ? 30.693 36.186  -28.798 1.00 63.67  ? 239 ARG B NH2 1 
ATOM   1325 N N   . VAL A 1 184 ? 30.319 30.598  -21.771 1.00 29.32  ? 240 VAL B N   1 
ATOM   1326 C CA  . VAL A 1 184 ? 31.142 29.586  -21.085 1.00 5.10   ? 240 VAL B CA  1 
ATOM   1327 C C   . VAL A 1 184 ? 30.767 28.176  -21.517 1.00 4.18   ? 240 VAL B C   1 
ATOM   1328 O O   . VAL A 1 184 ? 29.612 27.778  -21.443 1.00 6.85   ? 240 VAL B O   1 
ATOM   1329 C CB  . VAL A 1 184 ? 31.150 29.743  -19.498 1.00 5.77   ? 240 VAL B CB  1 
ATOM   1330 C CG1 . VAL A 1 184 ? 29.851 29.301  -18.859 1.00 4.35   ? 240 VAL B CG1 1 
ATOM   1331 C CG2 . VAL A 1 184 ? 32.298 28.973  -18.870 1.00 5.90   ? 240 VAL B CG2 1 
ATOM   1332 N N   . GLN A 1 185 ? 31.743 27.463  -22.071 1.00 10.35  ? 241 GLN B N   1 
ATOM   1333 C CA  . GLN A 1 185 ? 31.559 26.083  -22.513 1.00 10.17  ? 241 GLN B CA  1 
ATOM   1334 C C   . GLN A 1 185 ? 31.827 24.955  -21.511 1.00 17.94  ? 241 GLN B C   1 
ATOM   1335 O O   . GLN A 1 185 ? 31.124 23.946  -21.492 1.00 17.74  ? 241 GLN B O   1 
ATOM   1336 C CB  . GLN A 1 185 ? 32.288 25.863  -23.825 1.00 14.00  ? 241 GLN B CB  1 
ATOM   1337 C CG  . GLN A 1 185 ? 31.826 26.857  -24.882 1.00 17.48  ? 241 GLN B CG  1 
ATOM   1338 C CD  . GLN A 1 185 ? 32.291 26.483  -26.260 1.00 17.01  ? 241 GLN B CD  1 
ATOM   1339 O OE1 . GLN A 1 185 ? 32.863 25.408  -26.458 1.00 14.73  ? 241 GLN B OE1 1 
ATOM   1340 N NE2 . GLN A 1 185 ? 32.047 27.363  -27.227 1.00 18.35  ? 241 GLN B NE2 1 
ATOM   1341 N N   . THR A 1 186 ? 32.870 25.118  -20.708 1.00 22.16  ? 242 THR B N   1 
ATOM   1342 C CA  . THR A 1 186 ? 33.292 24.085  -19.779 1.00 4.33   ? 242 THR B CA  1 
ATOM   1343 C C   . THR A 1 186 ? 33.557 24.675  -18.411 1.00 4.91   ? 242 THR B C   1 
ATOM   1344 O O   . THR A 1 186 ? 34.361 25.596  -18.243 1.00 8.94   ? 242 THR B O   1 
ATOM   1345 C CB  . THR A 1 186 ? 34.554 23.355  -20.285 1.00 4.90   ? 242 THR B CB  1 
ATOM   1346 O OG1 . THR A 1 186 ? 34.190 22.473  -21.359 1.00 4.18   ? 242 THR B OG1 1 
ATOM   1347 C CG2 . THR A 1 186 ? 35.206 22.545  -19.184 1.00 5.16   ? 242 THR B CG2 1 
ATOM   1348 N N   . ILE A 1 187 ? 32.860 24.148  -17.420 1.00 20.99  ? 243 ILE B N   1 
ATOM   1349 C CA  . ILE A 1 187 ? 33.190 24.481  -16.059 1.00 18.47  ? 243 ILE B CA  1 
ATOM   1350 C C   . ILE A 1 187 ? 33.731 23.231  -15.416 1.00 9.97   ? 243 ILE B C   1 
ATOM   1351 O O   . ILE A 1 187 ? 33.007 22.253  -15.260 1.00 9.09   ? 243 ILE B O   1 
ATOM   1352 C CB  . ILE A 1 187 ? 31.974 25.008  -15.307 1.00 19.08  ? 243 ILE B CB  1 
ATOM   1353 C CG1 . ILE A 1 187 ? 31.625 26.396  -15.843 1.00 18.25  ? 243 ILE B CG1 1 
ATOM   1354 C CG2 . ILE A 1 187 ? 32.268 25.067  -13.819 1.00 4.71   ? 243 ILE B CG2 1 
ATOM   1355 C CD1 . ILE A 1 187 ? 30.359 26.968  -15.295 1.00 4.07   ? 243 ILE B CD1 1 
ATOM   1356 N N   . ALA A 1 188 ? 35.017 23.235  -15.091 1.00 5.74   ? 244 ALA B N   1 
ATOM   1357 C CA  . ALA A 1 188 ? 35.574 22.106  -14.365 1.00 14.33  ? 244 ALA B CA  1 
ATOM   1358 C C   . ALA A 1 188 ? 35.993 22.524  -12.965 1.00 19.31  ? 244 ALA B C   1 
ATOM   1359 O O   . ALA A 1 188 ? 37.021 23.164  -12.774 1.00 7.51   ? 244 ALA B O   1 
ATOM   1360 C CB  . ALA A 1 188 ? 36.769 21.531  -15.121 1.00 11.47  ? 244 ALA B CB  1 
ATOM   1361 N N   . ILE A 1 189 ? 35.203 22.154  -11.971 1.00 23.83  ? 245 ILE B N   1 
ATOM   1362 C CA  . ILE A 1 189 ? 35.688 22.233  -10.611 1.00 20.19  ? 245 ILE B CA  1 
ATOM   1363 C C   . ILE A 1 189 ? 35.370 20.897  -10.000 1.00 22.53  ? 245 ILE B C   1 
ATOM   1364 O O   . ILE A 1 189 ? 34.255 20.677  -9.535  1.00 30.68  ? 245 ILE B O   1 
ATOM   1365 C CB  . ILE A 1 189 ? 34.962 23.344  -9.827  1.00 13.96  ? 245 ILE B CB  1 
ATOM   1366 C CG1 . ILE A 1 189 ? 34.988 24.649  -10.619 1.00 15.08  ? 245 ILE B CG1 1 
ATOM   1367 C CG2 . ILE A 1 189 ? 35.641 23.574  -8.507  1.00 11.09  ? 245 ILE B CG2 1 
ATOM   1368 C CD1 . ILE A 1 189 ? 34.414 25.838  -9.889  1.00 9.69   ? 245 ILE B CD1 1 
ATOM   1369 N N   . TYR A 1 190 ? 36.380 20.043  -9.902  1.00 19.02  ? 246 TYR B N   1 
ATOM   1370 C CA  . TYR A 1 190 ? 36.153 18.670  -9.496  1.00 12.06  ? 246 TYR B CA  1 
ATOM   1371 C C   . TYR A 1 190 ? 37.249 18.202  -8.578  1.00 17.94  ? 246 TYR B C   1 
ATOM   1372 O O   . TYR A 1 190 ? 38.420 18.556  -8.778  1.00 22.03  ? 246 TYR B O   1 
ATOM   1373 C CB  . TYR A 1 190 ? 35.975 17.718  -10.695 1.00 10.96  ? 246 TYR B CB  1 
ATOM   1374 C CG  . TYR A 1 190 ? 37.117 17.585  -11.693 1.00 12.88  ? 246 TYR B CG  1 
ATOM   1375 C CD1 . TYR A 1 190 ? 38.223 16.800  -11.417 1.00 8.17   ? 246 TYR B CD1 1 
ATOM   1376 C CD2 . TYR A 1 190 ? 37.041 18.186  -12.952 1.00 24.39  ? 246 TYR B CD2 1 
ATOM   1377 C CE1 . TYR A 1 190 ? 39.248 16.654  -12.348 1.00 13.95  ? 246 TYR B CE1 1 
ATOM   1378 C CE2 . TYR A 1 190 ? 38.058 18.046  -13.890 1.00 6.10   ? 246 TYR B CE2 1 
ATOM   1379 C CZ  . TYR A 1 190 ? 39.157 17.281  -13.579 1.00 13.91  ? 246 TYR B CZ  1 
ATOM   1380 O OH  . TYR A 1 190 ? 40.175 17.135  -14.491 1.00 16.01  ? 246 TYR B OH  1 
ATOM   1381 N N   . THR A 1 191 ? 36.856 17.404  -7.579  1.00 16.28  ? 247 THR B N   1 
ATOM   1382 C CA  . THR A 1 191 ? 37.740 17.043  -6.483  1.00 6.32   ? 247 THR B CA  1 
ATOM   1383 C C   . THR A 1 191 ? 38.205 18.341  -5.830  1.00 14.07  ? 247 THR B C   1 
ATOM   1384 O O   . THR A 1 191 ? 39.378 18.689  -5.860  1.00 16.68  ? 247 THR B O   1 
ATOM   1385 C CB  . THR A 1 191 ? 38.937 16.202  -6.969  1.00 37.43  ? 247 THR B CB  1 
ATOM   1386 O OG1 . THR A 1 191 ? 38.471 15.154  -7.836  1.00 6.01   ? 247 THR B OG1 1 
ATOM   1387 C CG2 . THR A 1 191 ? 39.682 15.609  -5.799  1.00 7.39   ? 247 THR B CG2 1 
ATOM   1388 N N   . SER A 1 192 ? 37.245 19.066  -5.268  1.00 20.43  ? 248 SER B N   1 
ATOM   1389 C CA  . SER A 1 192 ? 37.497 20.303  -4.524  1.00 29.75  ? 248 SER B CA  1 
ATOM   1390 C C   . SER A 1 192 ? 36.766 20.326  -3.166  1.00 32.28  ? 248 SER B C   1 
ATOM   1391 O O   . SER A 1 192 ? 36.333 19.282  -2.670  1.00 34.76  ? 248 SER B O   1 
ATOM   1392 C CB  . SER A 1 192 ? 37.160 21.533  -5.368  1.00 34.15  ? 248 SER B CB  1 
ATOM   1393 O OG  . SER A 1 192 ? 38.260 21.899  -6.180  1.00 37.92  ? 248 SER B OG  1 
ATOM   1394 N N   . LEU A 1 193 ? 36.734 21.490  -2.521  1.00 30.78  ? 249 LEU B N   1 
ATOM   1395 C CA  . LEU A 1 193 ? 35.965 21.678  -1.274  1.00 36.05  ? 249 LEU B CA  1 
ATOM   1396 C C   . LEU A 1 193 ? 34.589 22.340  -1.413  1.00 29.69  ? 249 LEU B C   1 
ATOM   1397 O O   . LEU A 1 193 ? 34.033 22.796  -0.417  1.00 36.78  ? 249 LEU B O   1 
ATOM   1398 C CB  . LEU A 1 193 ? 36.810 22.283  -0.140  1.00 8.96   ? 249 LEU B CB  1 
ATOM   1399 C CG  . LEU A 1 193 ? 38.091 21.453  0.012   1.00 37.20  ? 249 LEU B CG  1 
ATOM   1400 C CD1 . LEU A 1 193 ? 39.159 22.126  0.839   1.00 10.90  ? 249 LEU B CD1 1 
ATOM   1401 C CD2 . LEU A 1 193 ? 37.767 20.108  0.580   1.00 8.80   ? 249 LEU B CD2 1 
ATOM   1402 N N   . LEU A 1 194 ? 34.096 22.473  -2.644  1.00 21.89  ? 250 LEU B N   1 
ATOM   1403 C CA  . LEU A 1 194 ? 32.788 23.089  -2.901  1.00 18.88  ? 250 LEU B CA  1 
ATOM   1404 C C   . LEU A 1 194 ? 31.660 22.515  -2.038  1.00 12.52  ? 250 LEU B C   1 
ATOM   1405 O O   . LEU A 1 194 ? 31.600 21.313  -1.804  1.00 19.59  ? 250 LEU B O   1 
ATOM   1406 C CB  . LEU A 1 194 ? 32.398 22.914  -4.373  1.00 16.13  ? 250 LEU B CB  1 
ATOM   1407 C CG  . LEU A 1 194 ? 32.993 23.771  -5.496  1.00 11.00  ? 250 LEU B CG  1 
ATOM   1408 C CD1 . LEU A 1 194 ? 32.174 23.611  -6.782  1.00 11.63  ? 250 LEU B CD1 1 
ATOM   1409 C CD2 . LEU A 1 194 ? 33.046 25.239  -5.096  1.00 14.28  ? 250 LEU B CD2 1 
ATOM   1410 N N   . SER A 1 195 ? 30.780 23.389  -1.558  1.00 4.90   ? 251 SER B N   1 
ATOM   1411 C CA  . SER A 1 195 ? 29.565 22.977  -0.843  1.00 14.83  ? 251 SER B CA  1 
ATOM   1412 C C   . SER A 1 195 ? 28.378 23.856  -1.208  1.00 16.08  ? 251 SER B C   1 
ATOM   1413 O O   . SER A 1 195 ? 28.515 24.796  -1.977  1.00 28.48  ? 251 SER B O   1 
ATOM   1414 C CB  . SER A 1 195 ? 29.762 22.908  0.691   1.00 12.04  ? 251 SER B CB  1 
ATOM   1415 O OG  . SER A 1 195 ? 30.520 23.993  1.214   1.00 15.67  ? 251 SER B OG  1 
ATOM   1416 N N   . GLY A 1 196 ? 27.207 23.558  -0.666  1.00 15.63  ? 252 GLY B N   1 
ATOM   1417 C CA  . GLY A 1 196 ? 26.027 24.324  -1.023  1.00 3.49   ? 252 GLY B CA  1 
ATOM   1418 C C   . GLY A 1 196 ? 25.393 23.799  -2.286  1.00 23.76  ? 252 GLY B C   1 
ATOM   1419 O O   . GLY A 1 196 ? 25.918 22.879  -2.925  1.00 31.12  ? 252 GLY B O   1 
ATOM   1420 N N   . PRO A 1 197 ? 24.242 24.365  -2.656  1.00 13.69  ? 253 PRO B N   1 
ATOM   1421 C CA  . PRO A 1 197 ? 23.572 23.942  -3.886  1.00 14.39  ? 253 PRO B CA  1 
ATOM   1422 C C   . PRO A 1 197 ? 24.191 24.563  -5.154  1.00 18.41  ? 253 PRO B C   1 
ATOM   1423 O O   . PRO A 1 197 ? 24.742 25.672  -5.118  1.00 17.53  ? 253 PRO B O   1 
ATOM   1424 C CB  . PRO A 1 197 ? 22.152 24.478  -3.684  1.00 10.36  ? 253 PRO B CB  1 
ATOM   1425 C CG  . PRO A 1 197 ? 22.370 25.765  -2.988  1.00 2.79   ? 253 PRO B CG  1 
ATOM   1426 C CD  . PRO A 1 197 ? 23.538 25.488  -2.015  1.00 10.05  ? 253 PRO B CD  1 
ATOM   1427 N N   . ILE A 1 198 ? 24.087 23.844  -6.268  1.00 16.16  ? 254 ILE B N   1 
ATOM   1428 C CA  . ILE A 1 198 ? 24.391 24.413  -7.567  1.00 11.89  ? 254 ILE B CA  1 
ATOM   1429 C C   . ILE A 1 198 ? 23.427 25.576  -7.717  1.00 7.92   ? 254 ILE B C   1 
ATOM   1430 O O   . ILE A 1 198 ? 22.235 25.417  -7.472  1.00 9.92   ? 254 ILE B O   1 
ATOM   1431 C CB  . ILE A 1 198 ? 24.137 23.384  -8.682  1.00 18.83  ? 254 ILE B CB  1 
ATOM   1432 C CG1 . ILE A 1 198 ? 25.028 22.159  -8.492  1.00 11.60  ? 254 ILE B CG1 1 
ATOM   1433 C CG2 . ILE A 1 198 ? 24.386 23.987  -10.051 1.00 30.01  ? 254 ILE B CG2 1 
ATOM   1434 C CD1 . ILE A 1 198 ? 24.516 20.929  -9.214  1.00 5.24   ? 254 ILE B CD1 1 
ATOM   1435 N N   . PRO A 1 199 ? 23.934 26.765  -8.074  1.00 2.24   ? 255 PRO B N   1 
ATOM   1436 C CA  . PRO A 1 199 ? 22.992 27.877  -8.220  1.00 8.75   ? 255 PRO B CA  1 
ATOM   1437 C C   . PRO A 1 199 ? 22.110 27.700  -9.459  1.00 14.14  ? 255 PRO B C   1 
ATOM   1438 O O   . PRO A 1 199 ? 22.572 27.285  -10.522 1.00 18.34  ? 255 PRO B O   1 
ATOM   1439 C CB  . PRO A 1 199 ? 23.902 29.102  -8.353  1.00 3.15   ? 255 PRO B CB  1 
ATOM   1440 C CG  . PRO A 1 199 ? 25.182 28.573  -8.861  1.00 13.07  ? 255 PRO B CG  1 
ATOM   1441 C CD  . PRO A 1 199 ? 25.318 27.154  -8.387  1.00 2.65   ? 255 PRO B CD  1 
ATOM   1442 N N   . ASP A 1 200 ? 20.833 28.014  -9.299  1.00 22.80  ? 256 ASP B N   1 
ATOM   1443 C CA  . ASP A 1 200 ? 19.851 27.896  -10.364 1.00 19.00  ? 256 ASP B CA  1 
ATOM   1444 C C   . ASP A 1 200 ? 20.265 28.688  -11.594 1.00 20.63  ? 256 ASP B C   1 
ATOM   1445 O O   . ASP A 1 200 ? 19.997 28.301  -12.739 1.00 24.18  ? 256 ASP B O   1 
ATOM   1446 C CB  . ASP A 1 200 ? 18.505 28.408  -9.853  1.00 17.50  ? 256 ASP B CB  1 
ATOM   1447 C CG  . ASP A 1 200 ? 17.703 27.329  -9.174  1.00 24.99  ? 256 ASP B CG  1 
ATOM   1448 O OD1 . ASP A 1 200 ? 17.937 27.079  -7.969  1.00 37.04  ? 256 ASP B OD1 1 
ATOM   1449 O OD2 . ASP A 1 200 ? 16.846 26.722  -9.856  1.00 21.22  ? 256 ASP B OD2 1 
ATOM   1450 N N   . GLU A 1 201 ? 20.955 29.791  -11.336 1.00 16.03  ? 257 GLU B N   1 
ATOM   1451 C CA  . GLU A 1 201 ? 21.313 30.755  -12.362 1.00 14.26  ? 257 GLU B CA  1 
ATOM   1452 C C   . GLU A 1 201 ? 22.291 30.168  -13.382 1.00 15.97  ? 257 GLU B C   1 
ATOM   1453 O O   . GLU A 1 201 ? 22.582 30.808  -14.388 1.00 22.14  ? 257 GLU B O   1 
ATOM   1454 C CB  . GLU A 1 201 ? 21.872 32.043  -11.727 1.00 9.43   ? 257 GLU B CB  1 
ATOM   1455 C CG  . GLU A 1 201 ? 20.862 32.823  -10.882 1.00 11.89  ? 257 GLU B CG  1 
ATOM   1456 C CD  . GLU A 1 201 ? 20.417 32.060  -9.628  1.00 22.38  ? 257 GLU B CD  1 
ATOM   1457 O OE1 . GLU A 1 201 ? 21.285 31.446  -8.963  1.00 4.73   ? 257 GLU B OE1 1 
ATOM   1458 O OE2 . GLU A 1 201 ? 19.195 32.049  -9.328  1.00 30.67  ? 257 GLU B OE2 1 
ATOM   1459 N N   . ILE A 1 202 ? 22.792 28.957  -13.124 1.00 8.44   ? 258 ILE B N   1 
ATOM   1460 C CA  . ILE A 1 202 ? 23.661 28.273  -14.081 1.00 15.97  ? 258 ILE B CA  1 
ATOM   1461 C C   . ILE A 1 202 ? 22.869 27.884  -15.322 1.00 28.96  ? 258 ILE B C   1 
ATOM   1462 O O   . ILE A 1 202 ? 23.448 27.552  -16.355 1.00 38.11  ? 258 ILE B O   1 
ATOM   1463 C CB  . ILE A 1 202 ? 24.350 27.013  -13.492 1.00 6.07   ? 258 ILE B CB  1 
ATOM   1464 C CG1 . ILE A 1 202 ? 25.685 26.753  -14.197 1.00 5.22   ? 258 ILE B CG1 1 
ATOM   1465 C CG2 . ILE A 1 202 ? 23.459 25.790  -13.614 1.00 4.04   ? 258 ILE B CG2 1 
ATOM   1466 C CD1 . ILE A 1 202 ? 26.433 25.541  -13.692 1.00 5.20   ? 258 ILE B CD1 1 
ATOM   1467 N N   . GLY A 1 203 ? 21.543 27.940  -15.227 1.00 27.02  ? 259 GLY B N   1 
ATOM   1468 C CA  . GLY A 1 203 ? 20.707 27.693  -16.391 1.00 24.64  ? 259 GLY B CA  1 
ATOM   1469 C C   . GLY A 1 203 ? 20.782 28.856  -17.361 1.00 20.92  ? 259 GLY B C   1 
ATOM   1470 O O   . GLY A 1 203 ? 20.276 28.785  -18.482 1.00 20.31  ? 259 GLY B O   1 
ATOM   1471 N N   . TYR A 1 204 ? 21.421 29.934  -16.917 1.00 23.39  ? 260 TYR B N   1 
ATOM   1472 C CA  . TYR A 1 204 ? 21.570 31.143  -17.717 1.00 24.52  ? 260 TYR B CA  1 
ATOM   1473 C C   . TYR A 1 204 ? 22.831 31.133  -18.577 1.00 22.84  ? 260 TYR B C   1 
ATOM   1474 O O   . TYR A 1 204 ? 23.047 32.070  -19.339 1.00 27.35  ? 260 TYR B O   1 
ATOM   1475 C CB  . TYR A 1 204 ? 21.595 32.383  -16.815 1.00 28.69  ? 260 TYR B CB  1 
ATOM   1476 C CG  . TYR A 1 204 ? 20.242 32.849  -16.316 1.00 24.14  ? 260 TYR B CG  1 
ATOM   1477 C CD1 . TYR A 1 204 ? 19.189 33.057  -17.196 1.00 17.33  ? 260 TYR B CD1 1 
ATOM   1478 C CD2 . TYR A 1 204 ? 20.027 33.096  -14.962 1.00 13.61  ? 260 TYR B CD2 1 
ATOM   1479 C CE1 . TYR A 1 204 ? 17.969 33.491  -16.743 1.00 24.41  ? 260 TYR B CE1 1 
ATOM   1480 C CE2 . TYR A 1 204 ? 18.800 33.534  -14.502 1.00 16.02  ? 260 TYR B CE2 1 
ATOM   1481 C CZ  . TYR A 1 204 ? 17.774 33.723  -15.391 1.00 21.35  ? 260 TYR B CZ  1 
ATOM   1482 O OH  . TYR A 1 204 ? 16.547 34.164  -14.945 1.00 23.02  ? 260 TYR B OH  1 
ATOM   1483 N N   . CYS A 1 205 ? 23.664 30.096  -18.466 1.00 17.14  ? 261 CYS B N   1 
ATOM   1484 C CA  . CYS A 1 205 ? 24.797 29.990  -19.381 1.00 23.66  ? 261 CYS B CA  1 
ATOM   1485 C C   . CYS A 1 205 ? 24.388 29.139  -20.584 1.00 22.75  ? 261 CYS B C   1 
ATOM   1486 O O   . CYS A 1 205 ? 24.382 27.913  -20.498 1.00 20.47  ? 261 CYS B O   1 
ATOM   1487 C CB  . CYS A 1 205 ? 25.970 29.291  -18.694 1.00 34.59  ? 261 CYS B CB  1 
ATOM   1488 S SG  . CYS A 1 205 ? 26.115 29.469  -16.890 1.00 13.79  ? 261 CYS B SG  1 
ATOM   1489 N N   . THR A 1 206 ? 24.151 29.777  -21.730 1.00 20.34  ? 262 THR B N   1 
ATOM   1490 C CA  . THR A 1 206 ? 23.480 29.098  -22.846 1.00 14.19  ? 262 THR B CA  1 
ATOM   1491 C C   . THR A 1 206 ? 24.433 28.161  -23.551 1.00 13.08  ? 262 THR B C   1 
ATOM   1492 O O   . THR A 1 206 ? 24.042 27.090  -24.022 1.00 12.19  ? 262 THR B O   1 
ATOM   1493 C CB  . THR A 1 206 ? 22.944 30.075  -23.901 1.00 11.62  ? 262 THR B CB  1 
ATOM   1494 O OG1 . THR A 1 206 ? 24.040 30.599  -24.655 1.00 30.58  ? 262 THR B OG1 1 
ATOM   1495 C CG2 . THR A 1 206 ? 22.183 31.216  -23.260 1.00 6.89   ? 262 THR B CG2 1 
ATOM   1496 N N   . GLU A 1 207 ? 25.690 28.585  -23.595 1.00 12.34  ? 263 GLU B N   1 
ATOM   1497 C CA  . GLU A 1 207 ? 26.752 27.888  -24.291 1.00 11.60  ? 263 GLU B CA  1 
ATOM   1498 C C   . GLU A 1 207 ? 27.390 26.737  -23.512 1.00 13.33  ? 263 GLU B C   1 
ATOM   1499 O O   . GLU A 1 207 ? 28.251 26.055  -24.050 1.00 18.97  ? 263 GLU B O   1 
ATOM   1500 C CB  . GLU A 1 207 ? 27.829 28.900  -24.657 1.00 20.78  ? 263 GLU B CB  1 
ATOM   1501 C CG  . GLU A 1 207 ? 27.356 29.933  -25.658 1.00 34.54  ? 263 GLU B CG  1 
ATOM   1502 C CD  . GLU A 1 207 ? 27.203 29.375  -27.050 1.00 47.41  ? 263 GLU B CD  1 
ATOM   1503 O OE1 . GLU A 1 207 ? 28.210 28.888  -27.614 1.00 50.46  ? 263 GLU B OE1 1 
ATOM   1504 O OE2 . GLU A 1 207 ? 26.072 29.423  -27.578 1.00 53.89  ? 263 GLU B OE2 1 
ATOM   1505 N N   . LEU A 1 208 ? 26.976 26.520  -22.262 1.00 15.09  ? 264 LEU B N   1 
ATOM   1506 C CA  . LEU A 1 208 ? 27.594 25.495  -21.406 1.00 13.99  ? 264 LEU B CA  1 
ATOM   1507 C C   . LEU A 1 208 ? 27.466 24.084  -21.981 1.00 18.80  ? 264 LEU B C   1 
ATOM   1508 O O   . LEU A 1 208 ? 26.371 23.633  -22.320 1.00 18.91  ? 264 LEU B O   1 
ATOM   1509 C CB  . LEU A 1 208 ? 27.034 25.544  -19.974 1.00 12.06  ? 264 LEU B CB  1 
ATOM   1510 C CG  . LEU A 1 208 ? 27.671 24.594  -18.939 1.00 7.50   ? 264 LEU B CG  1 
ATOM   1511 C CD1 . LEU A 1 208 ? 29.026 25.083  -18.499 1.00 2.00   ? 264 LEU B CD1 1 
ATOM   1512 C CD2 . LEU A 1 208 ? 26.790 24.371  -17.728 1.00 2.00   ? 264 LEU B CD2 1 
ATOM   1513 N N   . GLN A 1 209 ? 28.604 23.402  -22.079 1.00 21.81  ? 265 GLN B N   1 
ATOM   1514 C CA  . GLN A 1 209 ? 28.714 22.077  -22.695 1.00 17.42  ? 265 GLN B CA  1 
ATOM   1515 C C   . GLN A 1 209 ? 28.968 20.993  -21.650 1.00 10.63  ? 265 GLN B C   1 
ATOM   1516 O O   . GLN A 1 209 ? 28.267 19.985  -21.617 1.00 8.46   ? 265 GLN B O   1 
ATOM   1517 C CB  . GLN A 1 209 ? 29.761 22.042  -23.831 1.00 14.17  ? 265 GLN B CB  1 
ATOM   1518 C CG  . GLN A 1 209 ? 29.341 22.833  -25.098 1.00 21.73  ? 265 GLN B CG  1 
ATOM   1519 C CD  . GLN A 1 209 ? 30.287 22.664  -26.311 1.00 23.84  ? 265 GLN B CD  1 
ATOM   1520 O OE1 . GLN A 1 209 ? 31.394 22.131  -26.196 1.00 26.82  ? 265 GLN B OE1 1 
ATOM   1521 N NE2 . GLN A 1 209 ? 29.839 23.127  -27.474 1.00 19.78  ? 265 GLN B NE2 1 
ATOM   1522 N N   . ASN A 1 210 ? 30.033 21.163  -20.871 1.00 14.77  ? 266 ASN B N   1 
ATOM   1523 C CA  . ASN A 1 210 ? 30.446 20.188  -19.857 1.00 10.97  ? 266 ASN B CA  1 
ATOM   1524 C C   . ASN A 1 210 ? 30.405 20.745  -18.439 1.00 4.77   ? 266 ASN B C   1 
ATOM   1525 O O   . ASN A 1 210 ? 31.021 21.770  -18.151 1.00 5.41   ? 266 ASN B O   1 
ATOM   1526 C CB  . ASN A 1 210 ? 31.878 19.735  -20.153 1.00 11.83  ? 266 ASN B CB  1 
ATOM   1527 C CG  . ASN A 1 210 ? 32.123 19.508  -21.641 1.00 14.00  ? 266 ASN B CG  1 
ATOM   1528 O OD1 . ASN A 1 210 ? 31.565 18.592  -22.239 1.00 7.27   ? 266 ASN B OD1 1 
ATOM   1529 N ND2 . ASN A 1 210 ? 32.962 20.345  -22.238 1.00 16.94  ? 266 ASN B ND2 1 
ATOM   1530 N N   . LEU A 1 211 ? 29.708 20.082  -17.528 1.00 6.98   ? 267 LEU B N   1 
ATOM   1531 C CA  . LEU A 1 211 ? 29.784 20.529  -16.130 1.00 9.77   ? 267 LEU B CA  1 
ATOM   1532 C C   . LEU A 1 211 ? 30.450 19.491  -15.223 1.00 10.30  ? 267 LEU B C   1 
ATOM   1533 O O   . LEU A 1 211 ? 29.874 18.427  -14.976 1.00 4.13   ? 267 LEU B O   1 
ATOM   1534 C CB  . LEU A 1 211 ? 28.397 20.892  -15.608 1.00 4.10   ? 267 LEU B CB  1 
ATOM   1535 C CG  . LEU A 1 211 ? 28.311 21.545  -14.233 1.00 4.45   ? 267 LEU B CG  1 
ATOM   1536 C CD1 . LEU A 1 211 ? 29.208 22.769  -14.126 1.00 4.63   ? 267 LEU B CD1 1 
ATOM   1537 C CD2 . LEU A 1 211 ? 26.867 21.924  -13.972 1.00 4.66   ? 267 LEU B CD2 1 
ATOM   1538 N N   . TYR A 1 212 ? 31.663 19.774  -14.740 1.00 15.04  ? 268 TYR B N   1 
ATOM   1539 C CA  . TYR A 1 212 ? 32.324 18.801  -13.870 1.00 16.88  ? 268 TYR B CA  1 
ATOM   1540 C C   . TYR A 1 212 ? 32.461 19.362  -12.464 1.00 12.68  ? 268 TYR B C   1 
ATOM   1541 O O   . TYR A 1 212 ? 33.367 20.148  -12.190 1.00 15.50  ? 268 TYR B O   1 
ATOM   1542 C CB  . TYR A 1 212 ? 33.724 18.484  -14.411 1.00 19.13  ? 268 TYR B CB  1 
ATOM   1543 C CG  . TYR A 1 212 ? 33.773 18.134  -15.883 1.00 20.06  ? 268 TYR B CG  1 
ATOM   1544 C CD1 . TYR A 1 212 ? 32.710 17.494  -16.508 1.00 17.12  ? 268 TYR B CD1 1 
ATOM   1545 C CD2 . TYR A 1 212 ? 34.887 18.445  -16.649 1.00 22.13  ? 268 TYR B CD2 1 
ATOM   1546 C CE1 . TYR A 1 212 ? 32.755 17.177  -17.842 1.00 12.82  ? 268 TYR B CE1 1 
ATOM   1547 C CE2 . TYR A 1 212 ? 34.940 18.129  -17.985 1.00 19.22  ? 268 TYR B CE2 1 
ATOM   1548 C CZ  . TYR A 1 212 ? 33.871 17.494  -18.576 1.00 16.64  ? 268 TYR B CZ  1 
ATOM   1549 O OH  . TYR A 1 212 ? 33.916 17.182  -19.915 1.00 14.16  ? 268 TYR B OH  1 
ATOM   1550 N N   . LEU A 1 213 ? 31.531 18.963  -11.600 1.00 9.18   ? 269 LEU B N   1 
ATOM   1551 C CA  . LEU A 1 213 ? 31.513 19.280  -10.171 1.00 9.65   ? 269 LEU B CA  1 
ATOM   1552 C C   . LEU A 1 213 ? 31.765 18.078  -9.251  1.00 17.85  ? 269 LEU B C   1 
ATOM   1553 O O   . LEU A 1 213 ? 31.586 18.162  -8.042  1.00 17.39  ? 269 LEU B O   1 
ATOM   1554 C CB  . LEU A 1 213 ? 30.260 20.080  -9.801  1.00 6.23   ? 269 LEU B CB  1 
ATOM   1555 C CG  . LEU A 1 213 ? 30.239 21.390  -10.607 1.00 12.56  ? 269 LEU B CG  1 
ATOM   1556 C CD1 . LEU A 1 213 ? 28.998 22.233  -10.369 1.00 2.00   ? 269 LEU B CD1 1 
ATOM   1557 C CD2 . LEU A 1 213 ? 31.501 22.193  -10.351 1.00 3.38   ? 269 LEU B CD2 1 
ATOM   1558 N N   . TYR A 1 214 ? 32.098 16.938  -9.843  1.00 27.91  ? 270 TYR B N   1 
ATOM   1559 C CA  . TYR A 1 214 ? 32.198 15.684  -9.098  1.00 22.87  ? 270 TYR B CA  1 
ATOM   1560 C C   . TYR A 1 214 ? 33.219 15.724  -7.975  1.00 10.74  ? 270 TYR B C   1 
ATOM   1561 O O   . TYR A 1 214 ? 34.185 16.487  -8.050  1.00 13.04  ? 270 TYR B O   1 
ATOM   1562 C CB  . TYR A 1 214 ? 32.454 14.499  -10.044 1.00 22.03  ? 270 TYR B CB  1 
ATOM   1563 C CG  . TYR A 1 214 ? 33.813 14.416  -10.719 1.00 11.87  ? 270 TYR B CG  1 
ATOM   1564 C CD1 . TYR A 1 214 ? 34.877 13.803  -10.089 1.00 11.56  ? 270 TYR B CD1 1 
ATOM   1565 C CD2 . TYR A 1 214 ? 34.004 14.882  -12.012 1.00 7.41   ? 270 TYR B CD2 1 
ATOM   1566 C CE1 . TYR A 1 214 ? 36.097 13.684  -10.713 1.00 11.80  ? 270 TYR B CE1 1 
ATOM   1567 C CE2 . TYR A 1 214 ? 35.218 14.778  -12.632 1.00 8.48   ? 270 TYR B CE2 1 
ATOM   1568 C CZ  . TYR A 1 214 ? 36.263 14.182  -11.982 1.00 9.47   ? 270 TYR B CZ  1 
ATOM   1569 O OH  . TYR A 1 214 ? 37.484 14.068  -12.595 1.00 19.35  ? 270 TYR B OH  1 
ATOM   1570 N N   . GLN A 1 215 ? 32.985 14.902  -6.942  1.00 6.11   ? 271 GLN B N   1 
ATOM   1571 C CA  . GLN A 1 215 ? 33.834 14.819  -5.728  1.00 8.98   ? 271 GLN B CA  1 
ATOM   1572 C C   . GLN A 1 215 ? 33.973 16.110  -4.939  1.00 3.39   ? 271 GLN B C   1 
ATOM   1573 O O   . GLN A 1 215 ? 35.052 16.625  -4.740  1.00 13.81  ? 271 GLN B O   1 
ATOM   1574 C CB  . GLN A 1 215 ? 35.197 14.176  -6.006  1.00 3.42   ? 271 GLN B CB  1 
ATOM   1575 C CG  . GLN A 1 215 ? 35.082 12.679  -6.112  1.00 2.89   ? 271 GLN B CG  1 
ATOM   1576 C CD  . GLN A 1 215 ? 36.403 11.978  -6.272  1.00 4.44   ? 271 GLN B CD  1 
ATOM   1577 O OE1 . GLN A 1 215 ? 37.314 12.491  -6.913  1.00 4.31   ? 271 GLN B OE1 1 
ATOM   1578 N NE2 . GLN A 1 215 ? 36.518 10.788  -5.683  1.00 6.16   ? 271 GLN B NE2 1 
ATOM   1579 N N   . ASN A 1 216 ? 32.835 16.648  -4.548  1.00 10.39  ? 272 ASN B N   1 
ATOM   1580 C CA  . ASN A 1 216 ? 32.756 17.730  -3.590  1.00 10.29  ? 272 ASN B CA  1 
ATOM   1581 C C   . ASN A 1 216 ? 31.700 17.301  -2.586  1.00 15.57  ? 272 ASN B C   1 
ATOM   1582 O O   . ASN A 1 216 ? 31.318 16.130  -2.563  1.00 19.45  ? 272 ASN B O   1 
ATOM   1583 C CB  . ASN A 1 216 ? 32.358 19.027  -4.277  1.00 14.70  ? 272 ASN B CB  1 
ATOM   1584 C CG  . ASN A 1 216 ? 33.427 19.533  -5.212  1.00 23.54  ? 272 ASN B CG  1 
ATOM   1585 O OD1 . ASN A 1 216 ? 34.311 20.278  -4.805  1.00 30.37  ? 272 ASN B OD1 1 
ATOM   1586 N ND2 . ASN A 1 216 ? 33.347 19.141  -6.479  1.00 25.12  ? 272 ASN B ND2 1 
ATOM   1587 N N   . SER A 1 217 ? 31.272 18.202  -1.711  1.00 12.11  ? 273 SER B N   1 
ATOM   1588 C CA  . SER A 1 217 ? 30.043 17.937  -0.989  1.00 8.31   ? 273 SER B CA  1 
ATOM   1589 C C   . SER A 1 217 ? 29.072 18.996  -1.438  1.00 14.03  ? 273 SER B C   1 
ATOM   1590 O O   . SER A 1 217 ? 29.060 20.084  -0.900  1.00 28.79  ? 273 SER B O   1 
ATOM   1591 C CB  . SER A 1 217 ? 30.280 18.080  0.515   1.00 10.50  ? 273 SER B CB  1 
ATOM   1592 O OG  . SER A 1 217 ? 31.645 17.860  0.849   1.00 6.28   ? 273 SER B OG  1 
ATOM   1593 N N   . ILE A 1 218 ? 28.185 18.652  -2.353  1.00 11.86  ? 274 ILE B N   1 
ATOM   1594 C CA  . ILE A 1 218 ? 27.308 19.657  -2.926  1.00 9.54   ? 274 ILE B CA  1 
ATOM   1595 C C   . ILE A 1 218 ? 25.932 19.254  -2.483  1.00 7.12   ? 274 ILE B C   1 
ATOM   1596 O O   . ILE A 1 218 ? 25.577 18.085  -2.542  1.00 12.35  ? 274 ILE B O   1 
ATOM   1597 C CB  . ILE A 1 218 ? 27.435 19.747  -4.478  1.00 12.65  ? 274 ILE B CB  1 
ATOM   1598 C CG1 . ILE A 1 218 ? 28.756 20.411  -4.855  1.00 4.51   ? 274 ILE B CG1 1 
ATOM   1599 C CG2 . ILE A 1 218 ? 26.288 20.557  -5.094  1.00 2.00   ? 274 ILE B CG2 1 
ATOM   1600 C CD1 . ILE A 1 218 ? 28.888 20.732  -6.342  1.00 5.13   ? 274 ILE B CD1 1 
ATOM   1601 N N   . SER A 1 219 ? 25.171 20.219  -2.002  1.00 2.00   ? 275 SER B N   1 
ATOM   1602 C CA  . SER A 1 219 ? 23.947 19.912  -1.289  1.00 10.24  ? 275 SER B CA  1 
ATOM   1603 C C   . SER A 1 219 ? 22.792 20.415  -2.113  1.00 6.84   ? 275 SER B C   1 
ATOM   1604 O O   . SER A 1 219 ? 22.984 20.872  -3.231  1.00 10.62  ? 275 SER B O   1 
ATOM   1605 C CB  . SER A 1 219 ? 23.946 20.576  0.088   1.00 2.30   ? 275 SER B CB  1 
ATOM   1606 O OG  . SER A 1 219 ? 23.581 21.940  -0.019  1.00 19.18  ? 275 SER B OG  1 
ATOM   1607 N N   . GLY A 1 220 ? 21.593 20.344  -1.555  1.00 3.47   ? 276 GLY B N   1 
ATOM   1608 C CA  . GLY A 1 220 ? 20.422 20.729  -2.302  1.00 2.00   ? 276 GLY B CA  1 
ATOM   1609 C C   . GLY A 1 220 ? 20.229 19.714  -3.405  1.00 14.65  ? 276 GLY B C   1 
ATOM   1610 O O   . GLY A 1 220 ? 20.759 18.606  -3.327  1.00 10.64  ? 276 GLY B O   1 
ATOM   1611 N N   . SER A 1 221 ? 19.489 20.102  -4.441  1.00 18.77  ? 277 SER B N   1 
ATOM   1612 C CA  . SER A 1 221 ? 19.130 19.206  -5.533  1.00 15.07  ? 277 SER B CA  1 
ATOM   1613 C C   . SER A 1 221 ? 19.598 19.766  -6.875  1.00 17.14  ? 277 SER B C   1 
ATOM   1614 O O   . SER A 1 221 ? 19.929 20.949  -6.973  1.00 19.44  ? 277 SER B O   1 
ATOM   1615 C CB  . SER A 1 221 ? 17.620 19.053  -5.571  1.00 6.89   ? 277 SER B CB  1 
ATOM   1616 O OG  . SER A 1 221 ? 17.035 20.284  -5.953  1.00 5.26   ? 277 SER B OG  1 
ATOM   1617 N N   . ILE A 1 222 ? 19.624 18.915  -7.903  1.00 9.73   ? 278 ILE B N   1 
ATOM   1618 C CA  . ILE A 1 222 ? 20.020 19.340  -9.246  1.00 9.56   ? 278 ILE B CA  1 
ATOM   1619 C C   . ILE A 1 222 ? 18.992 20.310  -9.818  1.00 14.93  ? 278 ILE B C   1 
ATOM   1620 O O   . ILE A 1 222 ? 17.842 19.936  -10.040 1.00 15.31  ? 278 ILE B O   1 
ATOM   1621 C CB  . ILE A 1 222 ? 20.134 18.132  -10.212 1.00 5.82   ? 278 ILE B CB  1 
ATOM   1622 C CG1 . ILE A 1 222 ? 21.262 17.191  -9.783  1.00 2.00   ? 278 ILE B CG1 1 
ATOM   1623 C CG2 . ILE A 1 222 ? 20.349 18.610  -11.640 1.00 3.76   ? 278 ILE B CG2 1 
ATOM   1624 C CD1 . ILE A 1 222 ? 20.988 15.722  -10.102 1.00 2.00   ? 278 ILE B CD1 1 
ATOM   1625 N N   . PRO A 1 223 ? 19.403 21.554  -10.080 1.00 2.00   ? 279 PRO B N   1 
ATOM   1626 C CA  . PRO A 1 223 ? 18.433 22.542  -10.558 1.00 15.95  ? 279 PRO B CA  1 
ATOM   1627 C C   . PRO A 1 223 ? 17.758 22.145  -11.868 1.00 24.04  ? 279 PRO B C   1 
ATOM   1628 O O   . PRO A 1 223 ? 18.412 21.680  -12.800 1.00 36.30  ? 279 PRO B O   1 
ATOM   1629 C CB  . PRO A 1 223 ? 19.264 23.825  -10.712 1.00 2.00   ? 279 PRO B CB  1 
ATOM   1630 C CG  . PRO A 1 223 ? 20.682 23.425  -10.588 1.00 2.00   ? 279 PRO B CG  1 
ATOM   1631 C CD  . PRO A 1 223 ? 20.752 22.113  -9.904  1.00 11.89  ? 279 PRO B CD  1 
ATOM   1632 N N   . THR A 1 224 ? 16.442 22.308  -11.911 1.00 23.47  ? 280 THR B N   1 
ATOM   1633 C CA  . THR A 1 224 ? 15.632 22.037  -13.102 1.00 10.99  ? 280 THR B CA  1 
ATOM   1634 C C   . THR A 1 224 ? 16.119 22.822  -14.328 1.00 10.94  ? 280 THR B C   1 
ATOM   1635 O O   . THR A 1 224 ? 16.067 22.340  -15.453 1.00 21.05  ? 280 THR B O   1 
ATOM   1636 C CB  . THR A 1 224 ? 14.154 22.381  -12.805 1.00 5.23   ? 280 THR B CB  1 
ATOM   1637 O OG1 . THR A 1 224 ? 13.620 21.413  -11.888 1.00 9.48   ? 280 THR B OG1 1 
ATOM   1638 C CG2 . THR A 1 224 ? 13.328 22.364  -14.051 1.00 2.00   ? 280 THR B CG2 1 
ATOM   1639 N N   . THR A 1 225 ? 16.628 24.026  -14.091 1.00 8.31   ? 281 THR B N   1 
ATOM   1640 C CA  . THR A 1 225 ? 17.042 24.934  -15.147 1.00 2.00   ? 281 THR B CA  1 
ATOM   1641 C C   . THR A 1 225 ? 18.180 24.407  -16.010 1.00 2.98   ? 281 THR B C   1 
ATOM   1642 O O   . THR A 1 225 ? 18.436 24.940  -17.093 1.00 12.71  ? 281 THR B O   1 
ATOM   1643 C CB  . THR A 1 225 ? 17.475 26.259  -14.564 1.00 2.00   ? 281 THR B CB  1 
ATOM   1644 O OG1 . THR A 1 225 ? 18.570 26.033  -13.666 1.00 2.33   ? 281 THR B OG1 1 
ATOM   1645 C CG2 . THR A 1 225 ? 16.313 26.898  -13.809 1.00 8.23   ? 281 THR B CG2 1 
ATOM   1646 N N   . ILE A 1 226 ? 18.856 23.358  -15.554 1.00 2.14   ? 282 ILE B N   1 
ATOM   1647 C CA  . ILE A 1 226 ? 19.882 22.720  -16.381 1.00 10.02  ? 282 ILE B CA  1 
ATOM   1648 C C   . ILE A 1 226 ? 19.268 22.114  -17.659 1.00 15.98  ? 282 ILE B C   1 
ATOM   1649 O O   . ILE A 1 226 ? 19.947 21.951  -18.670 1.00 23.77  ? 282 ILE B O   1 
ATOM   1650 C CB  . ILE A 1 226 ? 20.725 21.704  -15.566 1.00 20.64  ? 282 ILE B CB  1 
ATOM   1651 C CG1 . ILE A 1 226 ? 21.411 22.435  -14.415 1.00 12.02  ? 282 ILE B CG1 1 
ATOM   1652 C CG2 . ILE A 1 226 ? 21.775 21.020  -16.433 1.00 25.37  ? 282 ILE B CG2 1 
ATOM   1653 C CD1 . ILE A 1 226 ? 22.508 21.664  -13.770 1.00 4.89   ? 282 ILE B CD1 1 
ATOM   1654 N N   . GLY A 1 227 ? 17.968 21.844  -17.629 1.00 15.96  ? 283 GLY B N   1 
ATOM   1655 C CA  . GLY A 1 227 ? 17.265 21.384  -18.814 1.00 13.94  ? 283 GLY B CA  1 
ATOM   1656 C C   . GLY A 1 227 ? 17.180 22.407  -19.943 1.00 21.91  ? 283 GLY B C   1 
ATOM   1657 O O   . GLY A 1 227 ? 16.910 22.065  -21.099 1.00 28.01  ? 283 GLY B O   1 
ATOM   1658 N N   . GLY A 1 228 ? 17.399 23.678  -19.632 1.00 20.95  ? 284 GLY B N   1 
ATOM   1659 C CA  . GLY A 1 228 ? 17.255 24.677  -20.673 1.00 2.00   ? 284 GLY B CA  1 
ATOM   1660 C C   . GLY A 1 228 ? 18.569 24.891  -21.379 1.00 4.56   ? 284 GLY B C   1 
ATOM   1661 O O   . GLY A 1 228 ? 18.689 25.753  -22.262 1.00 2.00   ? 284 GLY B O   1 
ATOM   1662 N N   . LEU A 1 229 ? 19.554 24.077  -21.012 1.00 6.68   ? 285 LEU B N   1 
ATOM   1663 C CA  . LEU A 1 229 ? 20.864 24.201  -21.615 1.00 13.20  ? 285 LEU B CA  1 
ATOM   1664 C C   . LEU A 1 229 ? 20.855 23.325  -22.857 1.00 17.34  ? 285 LEU B C   1 
ATOM   1665 O O   . LEU A 1 229 ? 21.012 22.107  -22.791 1.00 17.83  ? 285 LEU B O   1 
ATOM   1666 C CB  . LEU A 1 229 ? 21.930 23.719  -20.631 1.00 5.58   ? 285 LEU B CB  1 
ATOM   1667 C CG  . LEU A 1 229 ? 22.045 24.636  -19.418 1.00 7.27   ? 285 LEU B CG  1 
ATOM   1668 C CD1 . LEU A 1 229 ? 23.255 24.293  -18.564 1.00 2.00   ? 285 LEU B CD1 1 
ATOM   1669 C CD2 . LEU A 1 229 ? 22.088 26.084  -19.858 1.00 2.00   ? 285 LEU B CD2 1 
ATOM   1670 N N   . LYS A 1 230 ? 20.750 23.979  -24.004 1.00 21.29  ? 286 LYS B N   1 
ATOM   1671 C CA  . LYS A 1 230 ? 20.421 23.285  -25.240 1.00 17.73  ? 286 LYS B CA  1 
ATOM   1672 C C   . LYS A 1 230 ? 21.659 22.597  -25.799 1.00 13.04  ? 286 LYS B C   1 
ATOM   1673 O O   . LYS A 1 230 ? 21.558 21.576  -26.464 1.00 16.98  ? 286 LYS B O   1 
ATOM   1674 C CB  . LYS A 1 230 ? 19.812 24.251  -26.254 1.00 22.34  ? 286 LYS B CB  1 
ATOM   1675 C CG  . LYS A 1 230 ? 18.898 23.580  -27.264 1.00 33.00  ? 286 LYS B CG  1 
ATOM   1676 C CD  . LYS A 1 230 ? 19.223 23.971  -28.744 1.00 39.06  ? 286 LYS B CD  1 
ATOM   1677 C CE  . LYS A 1 230 ? 20.419 23.198  -29.339 1.00 26.12  ? 286 LYS B CE  1 
ATOM   1678 N NZ  . LYS A 1 230 ? 20.178 21.733  -29.422 1.00 14.73  ? 286 LYS B NZ  1 
ATOM   1679 N N   . LYS A 1 231 ? 22.828 23.143  -25.477 1.00 13.62  ? 287 LYS B N   1 
ATOM   1680 C CA  . LYS A 1 231 ? 24.108 22.623  -25.959 1.00 16.03  ? 287 LYS B CA  1 
ATOM   1681 C C   . LYS A 1 231 ? 24.788 21.653  -24.976 1.00 16.78  ? 287 LYS B C   1 
ATOM   1682 O O   . LYS A 1 231 ? 25.924 21.242  -25.209 1.00 18.82  ? 287 LYS B O   1 
ATOM   1683 C CB  . LYS A 1 231 ? 25.073 23.782  -26.285 1.00 15.68  ? 287 LYS B CB  1 
ATOM   1684 C CG  . LYS A 1 231 ? 24.556 24.831  -27.265 1.00 10.26  ? 287 LYS B CG  1 
ATOM   1685 C CD  . LYS A 1 231 ? 24.575 24.319  -28.694 1.00 29.86  ? 287 LYS B CD  1 
ATOM   1686 C CE  . LYS A 1 231 ? 24.468 25.464  -29.703 1.00 45.93  ? 287 LYS B CE  1 
ATOM   1687 N NZ  . LYS A 1 231 ? 25.702 26.310  -29.792 1.00 48.51  ? 287 LYS B NZ  1 
ATOM   1688 N N   . LEU A 1 232 ? 24.115 21.309  -23.879 1.00 16.86  ? 288 LEU B N   1 
ATOM   1689 C CA  . LEU A 1 232 ? 24.719 20.470  -22.825 1.00 8.95   ? 288 LEU B CA  1 
ATOM   1690 C C   . LEU A 1 232 ? 25.043 19.042  -23.282 1.00 4.56   ? 288 LEU B C   1 
ATOM   1691 O O   . LEU A 1 232 ? 24.249 18.386  -23.960 1.00 11.33  ? 288 LEU B O   1 
ATOM   1692 C CB  . LEU A 1 232 ? 23.837 20.441  -21.559 1.00 16.31  ? 288 LEU B CB  1 
ATOM   1693 C CG  . LEU A 1 232 ? 24.403 19.788  -20.281 1.00 26.22  ? 288 LEU B CG  1 
ATOM   1694 C CD1 . LEU A 1 232 ? 25.314 20.738  -19.494 1.00 2.00   ? 288 LEU B CD1 1 
ATOM   1695 C CD2 . LEU A 1 232 ? 23.302 19.223  -19.381 1.00 2.00   ? 288 LEU B CD2 1 
ATOM   1696 N N   . GLN A 1 233 ? 26.207 18.561  -22.864 1.00 2.00   ? 289 GLN B N   1 
ATOM   1697 C CA  . GLN A 1 233 ? 26.774 17.316  -23.371 1.00 9.83   ? 289 GLN B CA  1 
ATOM   1698 C C   . GLN A 1 233 ? 27.172 16.347  -22.268 1.00 13.69  ? 289 GLN B C   1 
ATOM   1699 O O   . GLN A 1 233 ? 26.775 15.179  -22.281 1.00 15.30  ? 289 GLN B O   1 
ATOM   1700 C CB  . GLN A 1 233 ? 27.937 17.592  -24.332 1.00 17.32  ? 289 GLN B CB  1 
ATOM   1701 C CG  . GLN A 1 233 ? 27.463 18.144  -25.675 1.00 19.63  ? 289 GLN B CG  1 
ATOM   1702 C CD  . GLN A 1 233 ? 28.593 18.577  -26.583 1.00 16.26  ? 289 GLN B CD  1 
ATOM   1703 O OE1 . GLN A 1 233 ? 29.664 17.970  -26.598 1.00 8.81   ? 289 GLN B OE1 1 
ATOM   1704 N NE2 . GLN A 1 233 ? 28.360 19.642  -27.345 1.00 21.02  ? 289 GLN B NE2 1 
ATOM   1705 N N   . SER A 1 234 ? 28.044 16.804  -21.375 1.00 11.08  ? 290 SER B N   1 
ATOM   1706 C CA  . SER A 1 234 ? 28.474 15.979  -20.245 1.00 7.65   ? 290 SER B CA  1 
ATOM   1707 C C   . SER A 1 234 ? 28.084 16.547  -18.862 1.00 10.69  ? 290 SER B C   1 
ATOM   1708 O O   . SER A 1 234 ? 28.326 17.718  -18.535 1.00 4.65   ? 290 SER B O   1 
ATOM   1709 C CB  . SER A 1 234 ? 29.973 15.714  -20.327 1.00 3.95   ? 290 SER B CB  1 
ATOM   1710 O OG  . SER A 1 234 ? 30.696 16.924  -20.319 1.00 19.76  ? 290 SER B OG  1 
ATOM   1711 N N   . LEU A 1 235 ? 27.454 15.717  -18.053 1.00 2.00   ? 291 LEU B N   1 
ATOM   1712 C CA  . LEU A 1 235 ? 27.166 16.129  -16.684 1.00 12.95  ? 291 LEU B CA  1 
ATOM   1713 C C   . LEU A 1 235 ? 27.812 15.163  -15.665 1.00 8.51   ? 291 LEU B C   1 
ATOM   1714 O O   . LEU A 1 235 ? 27.329 14.035  -15.497 1.00 2.48   ? 291 LEU B O   1 
ATOM   1715 C CB  . LEU A 1 235 ? 25.649 16.160  -16.506 1.00 2.00   ? 291 LEU B CB  1 
ATOM   1716 C CG  . LEU A 1 235 ? 24.970 17.184  -15.615 1.00 18.32  ? 291 LEU B CG  1 
ATOM   1717 C CD1 . LEU A 1 235 ? 25.761 18.446  -15.541 1.00 26.57  ? 291 LEU B CD1 1 
ATOM   1718 C CD2 . LEU A 1 235 ? 23.645 17.485  -16.223 1.00 20.25  ? 291 LEU B CD2 1 
ATOM   1719 N N   . LEU A 1 236 ? 28.876 15.593  -14.977 1.00 2.00   ? 292 LEU B N   1 
ATOM   1720 C CA  . LEU A 1 236 ? 29.478 14.736  -13.951 1.00 10.96  ? 292 LEU B CA  1 
ATOM   1721 C C   . LEU A 1 236 ? 29.288 15.339  -12.549 1.00 14.10  ? 292 LEU B C   1 
ATOM   1722 O O   . LEU A 1 236 ? 29.976 16.282  -12.151 1.00 9.66   ? 292 LEU B O   1 
ATOM   1723 C CB  . LEU A 1 236 ? 30.973 14.533  -14.223 1.00 2.96   ? 292 LEU B CB  1 
ATOM   1724 C CG  . LEU A 1 236 ? 31.458 13.842  -15.494 1.00 8.30   ? 292 LEU B CG  1 
ATOM   1725 C CD1 . LEU A 1 236 ? 32.954 14.073  -15.667 1.00 9.45   ? 292 LEU B CD1 1 
ATOM   1726 C CD2 . LEU A 1 236 ? 31.159 12.348  -15.499 1.00 10.61  ? 292 LEU B CD2 1 
ATOM   1727 N N   . LEU A 1 237 ? 28.319 14.797  -11.822 1.00 13.12  ? 293 LEU B N   1 
ATOM   1728 C CA  . LEU A 1 237 ? 27.996 15.239  -10.467 1.00 11.96  ? 293 LEU B CA  1 
ATOM   1729 C C   . LEU A 1 237 ? 28.376 14.260  -9.357  1.00 15.65  ? 293 LEU B C   1 
ATOM   1730 O O   . LEU A 1 237 ? 27.934 14.404  -8.221  1.00 18.35  ? 293 LEU B O   1 
ATOM   1731 C CB  . LEU A 1 237 ? 26.552 15.735  -10.379 1.00 9.67   ? 293 LEU B CB  1 
ATOM   1732 C CG  . LEU A 1 237 ? 26.362 16.822  -11.455 1.00 16.29  ? 293 LEU B CG  1 
ATOM   1733 C CD1 . LEU A 1 237 ? 24.928 17.320  -11.616 1.00 2.00   ? 293 LEU B CD1 1 
ATOM   1734 C CD2 . LEU A 1 237 ? 27.325 17.975  -11.215 1.00 2.00   ? 293 LEU B CD2 1 
ATOM   1735 N N   . TRP A 1 238 ? 29.108 13.211  -9.706  1.00 14.96  ? 294 TRP B N   1 
ATOM   1736 C CA  . TRP A 1 238 ? 29.245 12.085  -8.789  1.00 13.50  ? 294 TRP B CA  1 
ATOM   1737 C C   . TRP A 1 238 ? 30.013 12.366  -7.485  1.00 12.27  ? 294 TRP B C   1 
ATOM   1738 O O   . TRP A 1 238 ? 30.924 13.206  -7.457  1.00 11.25  ? 294 TRP B O   1 
ATOM   1739 C CB  . TRP A 1 238 ? 29.765 10.837  -9.518  1.00 10.00  ? 294 TRP B CB  1 
ATOM   1740 C CG  . TRP A 1 238 ? 31.106 10.970  -10.167 1.00 9.47   ? 294 TRP B CG  1 
ATOM   1741 C CD1 . TRP A 1 238 ? 31.369 11.458  -11.411 1.00 5.54   ? 294 TRP B CD1 1 
ATOM   1742 C CD2 . TRP A 1 238 ? 32.371 10.572  -9.612  1.00 11.26  ? 294 TRP B CD2 1 
ATOM   1743 N NE1 . TRP A 1 238 ? 32.721 11.410  -11.663 1.00 2.26   ? 294 TRP B NE1 1 
ATOM   1744 C CE2 . TRP A 1 238 ? 33.357 10.866  -10.583 1.00 9.11   ? 294 TRP B CE2 1 
ATOM   1745 C CE3 . TRP A 1 238 ? 32.763 10.017  -8.388  1.00 12.27  ? 294 TRP B CE3 1 
ATOM   1746 C CZ2 . TRP A 1 238 ? 34.716 10.615  -10.362 1.00 2.86   ? 294 TRP B CZ2 1 
ATOM   1747 C CZ3 . TRP A 1 238 ? 34.102 9.763   -8.174  1.00 10.08  ? 294 TRP B CZ3 1 
ATOM   1748 C CH2 . TRP A 1 238 ? 35.069 10.068  -9.157  1.00 12.84  ? 294 TRP B CH2 1 
ATOM   1749 N N   . GLN A 1 239 ? 29.636 11.640  -6.428  1.00 2.00   ? 295 GLN B N   1 
ATOM   1750 C CA  . GLN A 1 239 ? 30.152 11.847  -5.083  1.00 2.00   ? 295 GLN B CA  1 
ATOM   1751 C C   . GLN A 1 239 ? 29.933 13.257  -4.595  1.00 5.96   ? 295 GLN B C   1 
ATOM   1752 O O   . GLN A 1 239 ? 30.866 14.050  -4.507  1.00 6.83   ? 295 GLN B O   1 
ATOM   1753 C CB  . GLN A 1 239 ? 31.620 11.468  -4.927  1.00 2.13   ? 295 GLN B CB  1 
ATOM   1754 C CG  . GLN A 1 239 ? 31.860 9.986   -4.707  1.00 2.26   ? 295 GLN B CG  1 
ATOM   1755 C CD  . GLN A 1 239 ? 33.315 9.674   -4.430  1.00 3.43   ? 295 GLN B CD  1 
ATOM   1756 O OE1 . GLN A 1 239 ? 34.089 10.540  -4.007  1.00 2.80   ? 295 GLN B OE1 1 
ATOM   1757 N NE2 . GLN A 1 239 ? 33.699 8.433   -4.675  1.00 2.77   ? 295 GLN B NE2 1 
ATOM   1758 N N   . ASN A 1 240 ? 28.681 13.564  -4.299  1.00 4.40   ? 296 ASN B N   1 
ATOM   1759 C CA  . ASN A 1 240 ? 28.319 14.787  -3.620  1.00 7.49   ? 296 ASN B CA  1 
ATOM   1760 C C   . ASN A 1 240 ? 27.132 14.458  -2.734  1.00 8.58   ? 296 ASN B C   1 
ATOM   1761 O O   . ASN A 1 240 ? 26.811 13.289  -2.550  1.00 9.36   ? 296 ASN B O   1 
ATOM   1762 C CB  . ASN A 1 240 ? 27.967 15.871  -4.628  1.00 14.38  ? 296 ASN B CB  1 
ATOM   1763 C CG  . ASN A 1 240 ? 29.187 16.469  -5.284  1.00 16.65  ? 296 ASN B CG  1 
ATOM   1764 O OD1 . ASN A 1 240 ? 29.703 17.481  -4.834  1.00 22.04  ? 296 ASN B OD1 1 
ATOM   1765 N ND2 . ASN A 1 240 ? 29.651 15.850  -6.357  1.00 24.47  ? 296 ASN B ND2 1 
ATOM   1766 N N   . ASN A 1 241 ? 26.500 15.475  -2.161  1.00 11.44  ? 297 ASN B N   1 
ATOM   1767 C CA  . ASN A 1 241 ? 25.368 15.256  -1.256  1.00 14.37  ? 297 ASN B CA  1 
ATOM   1768 C C   . ASN A 1 241 ? 24.023 15.389  -1.936  1.00 16.84  ? 297 ASN B C   1 
ATOM   1769 O O   . ASN A 1 241 ? 23.003 15.402  -1.260  1.00 25.65  ? 297 ASN B O   1 
ATOM   1770 C CB  . ASN A 1 241 ? 25.414 16.172  -0.018  1.00 16.22  ? 297 ASN B CB  1 
ATOM   1771 C CG  . ASN A 1 241 ? 26.602 15.883  0.892   1.00 22.60  ? 297 ASN B CG  1 
ATOM   1772 O OD1 . ASN A 1 241 ? 27.108 14.757  0.954   1.00 2.06   ? 297 ASN B OD1 1 
ATOM   1773 N ND2 . ASN A 1 241 ? 27.054 16.913  1.605   1.00 28.19  ? 297 ASN B ND2 1 
ATOM   1774 N N   . LEU A 1 242 ? 24.024 15.513  -3.260  1.00 17.44  ? 298 LEU B N   1 
ATOM   1775 C CA  . LEU A 1 242 ? 22.830 15.923  -4.002  1.00 12.35  ? 298 LEU B CA  1 
ATOM   1776 C C   . LEU A 1 242 ? 21.581 15.151  -3.624  1.00 7.13   ? 298 LEU B C   1 
ATOM   1777 O O   . LEU A 1 242 ? 21.559 13.916  -3.625  1.00 8.02   ? 298 LEU B O   1 
ATOM   1778 C CB  . LEU A 1 242 ? 23.054 15.798  -5.519  1.00 15.70  ? 298 LEU B CB  1 
ATOM   1779 C CG  . LEU A 1 242 ? 24.150 16.643  -6.175  1.00 15.51  ? 298 LEU B CG  1 
ATOM   1780 C CD1 . LEU A 1 242 ? 24.226 16.361  -7.665  1.00 15.68  ? 298 LEU B CD1 1 
ATOM   1781 C CD2 . LEU A 1 242 ? 23.888 18.104  -5.925  1.00 2.00   ? 298 LEU B CD2 1 
ATOM   1782 N N   . VAL A 1 243 ? 20.529 15.901  -3.334  1.00 7.27   ? 299 VAL B N   1 
ATOM   1783 C CA  . VAL A 1 243 ? 19.291 15.326  -2.825  1.00 20.91  ? 299 VAL B CA  1 
ATOM   1784 C C   . VAL A 1 243 ? 18.147 15.481  -3.875  1.00 16.98  ? 299 VAL B C   1 
ATOM   1785 O O   . VAL A 1 243 ? 18.354 16.061  -4.933  1.00 18.71  ? 299 VAL B O   1 
ATOM   1786 C CB  . VAL A 1 243 ? 18.974 15.976  -1.436  1.00 8.47   ? 299 VAL B CB  1 
ATOM   1787 C CG1 . VAL A 1 243 ? 18.438 17.393  -1.602  1.00 22.99  ? 299 VAL B CG1 1 
ATOM   1788 C CG2 . VAL A 1 243 ? 18.042 15.115  -0.645  1.00 15.30  ? 299 VAL B CG2 1 
ATOM   1789 N N   . GLY A 1 244 ? 16.955 14.960  -3.616  1.00 12.96  ? 300 GLY B N   1 
ATOM   1790 C CA  . GLY A 1 244 ? 15.844 15.209  -4.523  1.00 2.00   ? 300 GLY B CA  1 
ATOM   1791 C C   . GLY A 1 244 ? 15.726 14.363  -5.787  1.00 8.06   ? 300 GLY B C   1 
ATOM   1792 O O   . GLY A 1 244 ? 16.484 13.409  -6.021  1.00 5.75   ? 300 GLY B O   1 
ATOM   1793 N N   . LYS A 1 245 ? 14.757 14.733  -6.621  1.00 2.39   ? 301 LYS B N   1 
ATOM   1794 C CA  . LYS A 1 245 ? 14.494 14.027  -7.862  1.00 5.57   ? 301 LYS B CA  1 
ATOM   1795 C C   . LYS A 1 245 ? 15.351 14.534  -9.029  1.00 8.99   ? 301 LYS B C   1 
ATOM   1796 O O   . LYS A 1 245 ? 15.643 15.727  -9.112  1.00 9.43   ? 301 LYS B O   1 
ATOM   1797 C CB  . LYS A 1 245 ? 13.012 14.131  -8.200  1.00 9.51   ? 301 LYS B CB  1 
ATOM   1798 C CG  . LYS A 1 245 ? 12.490 15.530  -8.050  1.00 28.81  ? 301 LYS B CG  1 
ATOM   1799 C CD  . LYS A 1 245 ? 11.215 15.746  -8.837  1.00 35.93  ? 301 LYS B CD  1 
ATOM   1800 C CE  . LYS A 1 245 ? 10.124 14.791  -8.415  1.00 39.10  ? 301 LYS B CE  1 
ATOM   1801 N NZ  . LYS A 1 245 ? 8.834  15.244  -9.014  1.00 47.48  ? 301 LYS B NZ  1 
ATOM   1802 N N   . ILE A 1 246 ? 15.758 13.606  -9.907  1.00 13.50  ? 302 ILE B N   1 
ATOM   1803 C CA  . ILE A 1 246 ? 16.393 13.919  -11.193 1.00 10.01  ? 302 ILE B CA  1 
ATOM   1804 C C   . ILE A 1 246 ? 15.401 14.700  -12.051 1.00 2.00   ? 302 ILE B C   1 
ATOM   1805 O O   . ILE A 1 246 ? 14.271 14.254  -12.243 1.00 2.00   ? 302 ILE B O   1 
ATOM   1806 C CB  . ILE A 1 246 ? 16.779 12.621  -11.969 1.00 6.42   ? 302 ILE B CB  1 
ATOM   1807 C CG1 . ILE A 1 246 ? 17.646 11.692  -11.115 1.00 7.09   ? 302 ILE B CG1 1 
ATOM   1808 C CG2 . ILE A 1 246 ? 17.490 12.948  -13.282 1.00 8.87   ? 302 ILE B CG2 1 
ATOM   1809 C CD1 . ILE A 1 246 ? 18.068 10.416  -11.821 1.00 2.00   ? 302 ILE B CD1 1 
ATOM   1810 N N   . PRO A 1 247 ? 15.809 15.878  -12.551 1.00 2.00   ? 303 PRO B N   1 
ATOM   1811 C CA  . PRO A 1 247 ? 14.905 16.707  -13.360 1.00 2.00   ? 303 PRO B CA  1 
ATOM   1812 C C   . PRO A 1 247 ? 14.562 16.079  -14.700 1.00 18.07  ? 303 PRO B C   1 
ATOM   1813 O O   . PRO A 1 247 ? 15.463 15.691  -15.450 1.00 19.65  ? 303 PRO B O   1 
ATOM   1814 C CB  . PRO A 1 247 ? 15.696 18.003  -13.575 1.00 2.00   ? 303 PRO B CB  1 
ATOM   1815 C CG  . PRO A 1 247 ? 17.108 17.665  -13.264 1.00 17.10  ? 303 PRO B CG  1 
ATOM   1816 C CD  . PRO A 1 247 ? 17.085 16.554  -12.260 1.00 5.59   ? 303 PRO B CD  1 
ATOM   1817 N N   . THR A 1 248 ? 13.272 16.018  -15.016 1.00 14.48  ? 304 THR B N   1 
ATOM   1818 C CA  . THR A 1 248 ? 12.824 15.435  -16.274 1.00 14.81  ? 304 THR B CA  1 
ATOM   1819 C C   . THR A 1 248 ? 13.232 16.285  -17.466 1.00 14.35  ? 304 THR B C   1 
ATOM   1820 O O   . THR A 1 248 ? 13.247 15.809  -18.605 1.00 14.43  ? 304 THR B O   1 
ATOM   1821 C CB  . THR A 1 248 ? 11.293 15.312  -16.331 1.00 16.83  ? 304 THR B CB  1 
ATOM   1822 O OG1 . THR A 1 248 ? 10.711 16.621  -16.366 1.00 15.78  ? 304 THR B OG1 1 
ATOM   1823 C CG2 . THR A 1 248 ? 10.773 14.544  -15.145 1.00 2.00   ? 304 THR B CG2 1 
ATOM   1824 N N   . GLU A 1 249 ? 13.536 17.551  -17.205 1.00 7.22   ? 305 GLU B N   1 
ATOM   1825 C CA  . GLU A 1 249 ? 13.904 18.473  -18.267 1.00 2.78   ? 305 GLU B CA  1 
ATOM   1826 C C   . GLU A 1 249 ? 15.253 18.127  -18.889 1.00 14.10  ? 305 GLU B C   1 
ATOM   1827 O O   . GLU A 1 249 ? 15.607 18.669  -19.933 1.00 25.70  ? 305 GLU B O   1 
ATOM   1828 C CB  . GLU A 1 249 ? 13.929 19.913  -17.765 1.00 2.00   ? 305 GLU B CB  1 
ATOM   1829 C CG  . GLU A 1 249 ? 12.566 20.473  -17.430 1.00 6.64   ? 305 GLU B CG  1 
ATOM   1830 C CD  . GLU A 1 249 ? 12.001 19.879  -16.164 1.00 15.91  ? 305 GLU B CD  1 
ATOM   1831 O OE1 . GLU A 1 249 ? 12.809 19.479  -15.295 1.00 21.02  ? 305 GLU B OE1 1 
ATOM   1832 O OE2 . GLU A 1 249 ? 10.758 19.800  -16.048 1.00 15.50  ? 305 GLU B OE2 1 
ATOM   1833 N N   . LEU A 1 250 ? 16.015 17.236  -18.260 1.00 10.81  ? 306 LEU B N   1 
ATOM   1834 C CA  . LEU A 1 250 ? 17.269 16.797  -18.866 1.00 12.44  ? 306 LEU B CA  1 
ATOM   1835 C C   . LEU A 1 250 ? 17.010 16.064  -20.191 1.00 20.59  ? 306 LEU B C   1 
ATOM   1836 O O   . LEU A 1 250 ? 17.923 15.879  -20.986 1.00 24.33  ? 306 LEU B O   1 
ATOM   1837 C CB  . LEU A 1 250 ? 18.072 15.898  -17.918 1.00 8.87   ? 306 LEU B CB  1 
ATOM   1838 C CG  . LEU A 1 250 ? 18.821 16.462  -16.706 1.00 13.06  ? 306 LEU B CG  1 
ATOM   1839 C CD1 . LEU A 1 250 ? 19.571 15.331  -16.041 1.00 23.03  ? 306 LEU B CD1 1 
ATOM   1840 C CD2 . LEU A 1 250 ? 19.796 17.559  -17.070 1.00 4.73   ? 306 LEU B CD2 1 
ATOM   1841 N N   . GLY A 1 251 ? 15.770 15.642  -20.425 1.00 18.67  ? 307 GLY B N   1 
ATOM   1842 C CA  . GLY A 1 251 ? 15.416 15.009  -21.683 1.00 18.99  ? 307 GLY B CA  1 
ATOM   1843 C C   . GLY A 1 251 ? 15.435 15.972  -22.864 1.00 18.09  ? 307 GLY B C   1 
ATOM   1844 O O   . GLY A 1 251 ? 15.462 15.548  -24.011 1.00 22.65  ? 307 GLY B O   1 
ATOM   1845 N N   . ASN A 1 252 ? 15.448 17.269  -22.564 1.00 16.44  ? 308 ASN B N   1 
ATOM   1846 C CA  . ASN A 1 252 ? 15.440 18.348  -23.553 1.00 11.13  ? 308 ASN B CA  1 
ATOM   1847 C C   . ASN A 1 252 ? 16.836 18.765  -24.007 1.00 16.57  ? 308 ASN B C   1 
ATOM   1848 O O   . ASN A 1 252 ? 17.001 19.820  -24.617 1.00 20.02  ? 308 ASN B O   1 
ATOM   1849 C CB  . ASN A 1 252 ? 14.729 19.583  -23.011 1.00 12.21  ? 308 ASN B CB  1 
ATOM   1850 C CG  . ASN A 1 252 ? 13.437 19.260  -22.304 1.00 14.45  ? 308 ASN B CG  1 
ATOM   1851 O OD1 . ASN A 1 252 ? 12.843 18.195  -22.494 1.00 14.43  ? 308 ASN B OD1 1 
ATOM   1852 N ND2 . ASN A 1 252 ? 12.983 20.197  -21.480 1.00 18.03  ? 308 ASN B ND2 1 
ATOM   1853 N N   . CYS A 1 253 ? 17.840 17.974  -23.645 1.00 19.42  ? 309 CYS B N   1 
ATOM   1854 C CA  . CYS A 1 253 ? 19.235 18.283  -23.955 1.00 23.36  ? 309 CYS B CA  1 
ATOM   1855 C C   . CYS A 1 253 ? 19.806 17.265  -24.950 1.00 24.66  ? 309 CYS B C   1 
ATOM   1856 O O   . CYS A 1 253 ? 20.460 16.295  -24.562 1.00 24.14  ? 309 CYS B O   1 
ATOM   1857 C CB  . CYS A 1 253 ? 20.079 18.289  -22.680 1.00 24.71  ? 309 CYS B CB  1 
ATOM   1858 S SG  . CYS A 1 253 ? 19.638 19.571  -21.500 1.00 11.97  ? 309 CYS B SG  1 
ATOM   1859 N N   . PRO A 1 254 ? 19.558 17.507  -26.247 1.00 14.26  ? 310 PRO B N   1 
ATOM   1860 C CA  . PRO A 1 254 ? 19.750 16.585  -27.370 1.00 4.76   ? 310 PRO B CA  1 
ATOM   1861 C C   . PRO A 1 254 ? 21.179 16.077  -27.508 1.00 10.71  ? 310 PRO B C   1 
ATOM   1862 O O   . PRO A 1 254 ? 21.392 14.917  -27.853 1.00 20.70  ? 310 PRO B O   1 
ATOM   1863 C CB  . PRO A 1 254 ? 19.391 17.442  -28.588 1.00 2.00   ? 310 PRO B CB  1 
ATOM   1864 C CG  . PRO A 1 254 ? 18.626 18.582  -28.058 1.00 8.99   ? 310 PRO B CG  1 
ATOM   1865 C CD  . PRO A 1 254 ? 19.198 18.856  -26.713 1.00 6.19   ? 310 PRO B CD  1 
ATOM   1866 N N   . GLU A 1 255 ? 22.153 16.927  -27.221 1.00 15.34  ? 311 GLU B N   1 
ATOM   1867 C CA  . GLU A 1 255 ? 23.545 16.569  -27.434 1.00 2.00   ? 311 GLU B CA  1 
ATOM   1868 C C   . GLU A 1 255 ? 24.174 15.848  -26.249 1.00 8.34   ? 311 GLU B C   1 
ATOM   1869 O O   . GLU A 1 255 ? 25.378 15.606  -26.256 1.00 14.92  ? 311 GLU B O   1 
ATOM   1870 C CB  . GLU A 1 255 ? 24.357 17.812  -27.754 1.00 27.78  ? 311 GLU B CB  1 
ATOM   1871 C CG  . GLU A 1 255 ? 23.976 18.474  -29.051 1.00 33.10  ? 311 GLU B CG  1 
ATOM   1872 C CD  . GLU A 1 255 ? 24.905 19.612  -29.404 1.00 47.39  ? 311 GLU B CD  1 
ATOM   1873 O OE1 . GLU A 1 255 ? 25.822 19.906  -28.606 1.00 49.10  ? 311 GLU B OE1 1 
ATOM   1874 O OE2 . GLU A 1 255 ? 24.722 20.217  -30.479 1.00 59.57  ? 311 GLU B OE2 1 
ATOM   1875 N N   . LEU A 1 256 ? 23.375 15.496  -25.239 1.00 2.00   ? 312 LEU B N   1 
ATOM   1876 C CA  . LEU A 1 256 ? 23.927 15.052  -23.974 1.00 2.00   ? 312 LEU B CA  1 
ATOM   1877 C C   . LEU A 1 256 ? 24.151 13.554  -24.038 1.00 8.09   ? 312 LEU B C   1 
ATOM   1878 O O   . LEU A 1 256 ? 23.223 12.766  -23.974 1.00 2.00   ? 312 LEU B O   1 
ATOM   1879 C CB  . LEU A 1 256 ? 22.938 15.385  -22.847 1.00 2.00   ? 312 LEU B CB  1 
ATOM   1880 C CG  . LEU A 1 256 ? 23.088 14.860  -21.396 1.00 16.83  ? 312 LEU B CG  1 
ATOM   1881 C CD1 . LEU A 1 256 ? 24.154 15.579  -20.595 1.00 13.32  ? 312 LEU B CD1 1 
ATOM   1882 C CD2 . LEU A 1 256 ? 21.773 14.942  -20.663 1.00 2.00   ? 312 LEU B CD2 1 
ATOM   1883 N N   . TRP A 1 257 ? 25.414 13.177  -24.164 1.00 2.00   ? 313 TRP B N   1 
ATOM   1884 C CA  . TRP A 1 257 ? 25.796 11.778  -24.272 1.00 12.26  ? 313 TRP B CA  1 
ATOM   1885 C C   . TRP A 1 257 ? 26.275 11.157  -22.952 1.00 11.23  ? 313 TRP B C   1 
ATOM   1886 O O   . TRP A 1 257 ? 26.361 9.932   -22.831 1.00 13.53  ? 313 TRP B O   1 
ATOM   1887 C CB  . TRP A 1 257 ? 26.890 11.635  -25.346 1.00 8.91   ? 313 TRP B CB  1 
ATOM   1888 C CG  . TRP A 1 257 ? 28.166 12.285  -24.951 1.00 4.32   ? 313 TRP B CG  1 
ATOM   1889 C CD1 . TRP A 1 257 ? 28.460 13.604  -25.031 1.00 2.00   ? 313 TRP B CD1 1 
ATOM   1890 C CD2 . TRP A 1 257 ? 29.306 11.649  -24.377 1.00 2.00   ? 313 TRP B CD2 1 
ATOM   1891 N NE1 . TRP A 1 257 ? 29.716 13.835  -24.545 1.00 2.00   ? 313 TRP B NE1 1 
ATOM   1892 C CE2 . TRP A 1 257 ? 30.261 12.640  -24.135 1.00 2.01   ? 313 TRP B CE2 1 
ATOM   1893 C CE3 . TRP A 1 257 ? 29.614 10.331  -24.036 1.00 13.93  ? 313 TRP B CE3 1 
ATOM   1894 C CZ2 . TRP A 1 257 ? 31.500 12.370  -23.576 1.00 2.38   ? 313 TRP B CZ2 1 
ATOM   1895 C CZ3 . TRP A 1 257 ? 30.853 10.057  -23.483 1.00 2.30   ? 313 TRP B CZ3 1 
ATOM   1896 C CH2 . TRP A 1 257 ? 31.780 11.072  -23.264 1.00 2.51   ? 313 TRP B CH2 1 
ATOM   1897 N N   . LEU A 1 258 ? 26.567 11.991  -21.960 1.00 9.11   ? 314 LEU B N   1 
ATOM   1898 C CA  . LEU A 1 258 ? 27.100 11.475  -20.691 1.00 14.50  ? 314 LEU B CA  1 
ATOM   1899 C C   . LEU A 1 258 ? 26.460 12.077  -19.429 1.00 8.08   ? 314 LEU B C   1 
ATOM   1900 O O   . LEU A 1 258 ? 26.430 13.300  -19.241 1.00 2.00   ? 314 LEU B O   1 
ATOM   1901 C CB  . LEU A 1 258 ? 28.622 11.627  -20.648 1.00 21.84  ? 314 LEU B CB  1 
ATOM   1902 C CG  . LEU A 1 258 ? 29.317 11.148  -19.373 1.00 19.11  ? 314 LEU B CG  1 
ATOM   1903 C CD1 . LEU A 1 258 ? 28.876 9.755   -18.994 1.00 15.99  ? 314 LEU B CD1 1 
ATOM   1904 C CD2 . LEU A 1 258 ? 30.817 11.181  -19.541 1.00 20.25  ? 314 LEU B CD2 1 
ATOM   1905 N N   . ILE A 1 259 ? 25.939 11.202  -18.575 1.00 9.04   ? 315 ILE B N   1 
ATOM   1906 C CA  . ILE A 1 259 ? 25.333 11.624  -17.307 1.00 8.44   ? 315 ILE B CA  1 
ATOM   1907 C C   . ILE A 1 259 ? 25.854 10.780  -16.146 1.00 11.81  ? 315 ILE B C   1 
ATOM   1908 O O   . ILE A 1 259 ? 25.625 9.561   -16.120 1.00 9.04   ? 315 ILE B O   1 
ATOM   1909 C CB  . ILE A 1 259 ? 23.802 11.469  -17.342 1.00 6.04   ? 315 ILE B CB  1 
ATOM   1910 C CG1 . ILE A 1 259 ? 23.212 12.147  -18.588 1.00 9.83   ? 315 ILE B CG1 1 
ATOM   1911 C CG2 . ILE A 1 259 ? 23.181 12.000  -16.056 1.00 4.33   ? 315 ILE B CG2 1 
ATOM   1912 C CD1 . ILE A 1 259 ? 21.703 11.972  -18.722 1.00 8.95   ? 315 ILE B CD1 1 
ATOM   1913 N N   . ASP A 1 260 ? 26.571 11.403  -15.204 1.00 11.99  ? 316 ASP B N   1 
ATOM   1914 C CA  . ASP A 1 260 ? 26.963 10.696  -13.981 1.00 11.21  ? 316 ASP B CA  1 
ATOM   1915 C C   . ASP A 1 260 ? 26.481 11.387  -12.705 1.00 11.18  ? 316 ASP B C   1 
ATOM   1916 O O   . ASP A 1 260 ? 27.016 12.423  -12.287 1.00 4.62   ? 316 ASP B O   1 
ATOM   1917 C CB  . ASP A 1 260 ? 28.479 10.550  -13.930 1.00 14.58  ? 316 ASP B CB  1 
ATOM   1918 C CG  . ASP A 1 260 ? 28.929 9.417   -13.028 1.00 21.77  ? 316 ASP B CG  1 
ATOM   1919 O OD1 . ASP A 1 260 ? 28.235 9.135   -12.031 1.00 23.96  ? 316 ASP B OD1 1 
ATOM   1920 O OD2 . ASP A 1 260 ? 29.979 8.805   -13.316 1.00 19.89  ? 316 ASP B OD2 1 
ATOM   1921 N N   . PHE A 1 261 ? 25.462 10.791  -12.098 1.00 16.60  ? 317 PHE B N   1 
ATOM   1922 C CA  . PHE A 1 261 ? 24.949 11.159  -10.777 1.00 2.00   ? 317 PHE B CA  1 
ATOM   1923 C C   . PHE A 1 261 ? 25.371 10.182  -9.672  1.00 12.61  ? 317 PHE B C   1 
ATOM   1924 O O   . PHE A 1 261 ? 24.862 10.241  -8.552  1.00 6.05   ? 317 PHE B O   1 
ATOM   1925 C CB  . PHE A 1 261 ? 23.443 11.386  -10.821 1.00 2.00   ? 317 PHE B CB  1 
ATOM   1926 C CG  . PHE A 1 261 ? 23.040 12.474  -11.776 1.00 16.08  ? 317 PHE B CG  1 
ATOM   1927 C CD1 . PHE A 1 261 ? 23.958 13.437  -12.165 1.00 2.00   ? 317 PHE B CD1 1 
ATOM   1928 C CD2 . PHE A 1 261 ? 21.759 12.531  -12.297 1.00 3.36   ? 317 PHE B CD2 1 
ATOM   1929 C CE1 . PHE A 1 261 ? 23.606 14.437  -13.043 1.00 18.69  ? 317 PHE B CE1 1 
ATOM   1930 C CE2 . PHE A 1 261 ? 21.402 13.536  -13.185 1.00 4.52   ? 317 PHE B CE2 1 
ATOM   1931 C CZ  . PHE A 1 261 ? 22.329 14.492  -13.558 1.00 2.00   ? 317 PHE B CZ  1 
ATOM   1932 N N   . SER A 1 262 ? 26.256 9.250   -10.002 1.00 2.00   ? 318 SER B N   1 
ATOM   1933 C CA  . SER A 1 262 ? 26.613 8.194   -9.069  1.00 8.52   ? 318 SER B CA  1 
ATOM   1934 C C   . SER A 1 262 ? 27.030 8.713   -7.681  1.00 6.95   ? 318 SER B C   1 
ATOM   1935 O O   . SER A 1 262 ? 27.626 9.776   -7.577  1.00 2.00   ? 318 SER B O   1 
ATOM   1936 C CB  . SER A 1 262 ? 27.740 7.341   -9.650  1.00 9.97   ? 318 SER B CB  1 
ATOM   1937 O OG  . SER A 1 262 ? 27.433 6.875   -10.951 1.00 7.34   ? 318 SER B OG  1 
ATOM   1938 N N   . GLU A 1 263 ? 26.673 7.967   -6.629  1.00 5.76   ? 319 GLU B N   1 
ATOM   1939 C CA  . GLU A 1 263 ? 26.991 8.297   -5.230  1.00 2.00   ? 319 GLU B CA  1 
ATOM   1940 C C   . GLU A 1 263 ? 26.509 9.643   -4.739  1.00 4.51   ? 319 GLU B C   1 
ATOM   1941 O O   . GLU A 1 263 ? 27.296 10.528  -4.430  1.00 2.00   ? 319 GLU B O   1 
ATOM   1942 C CB  . GLU A 1 263 ? 28.468 8.117   -4.923  1.00 2.00   ? 319 GLU B CB  1 
ATOM   1943 C CG  . GLU A 1 263 ? 28.929 6.696   -5.149  1.00 30.56  ? 319 GLU B CG  1 
ATOM   1944 C CD  . GLU A 1 263 ? 30.339 6.477   -4.703  1.00 32.04  ? 319 GLU B CD  1 
ATOM   1945 O OE1 . GLU A 1 263 ? 31.010 5.582   -5.259  1.00 34.47  ? 319 GLU B OE1 1 
ATOM   1946 O OE2 . GLU A 1 263 ? 30.771 7.202   -3.784  1.00 35.64  ? 319 GLU B OE2 1 
ATOM   1947 N N   . ASN A 1 264 ? 25.193 9.761   -4.652  1.00 2.00   ? 320 ASN B N   1 
ATOM   1948 C CA  . ASN A 1 264 ? 24.522 10.896  -4.059  1.00 2.00   ? 320 ASN B CA  1 
ATOM   1949 C C   . ASN A 1 264 ? 23.337 10.362  -3.253  1.00 11.31  ? 320 ASN B C   1 
ATOM   1950 O O   . ASN A 1 264 ? 23.276 9.185   -2.907  1.00 7.75   ? 320 ASN B O   1 
ATOM   1951 C CB  . ASN A 1 264 ? 24.024 11.888  -5.112  1.00 2.00   ? 320 ASN B CB  1 
ATOM   1952 C CG  . ASN A 1 264 ? 25.152 12.616  -5.835  1.00 18.69  ? 320 ASN B CG  1 
ATOM   1953 O OD1 . ASN A 1 264 ? 25.502 13.735  -5.477  1.00 25.93  ? 320 ASN B OD1 1 
ATOM   1954 N ND2 . ASN A 1 264 ? 25.701 11.994  -6.875  1.00 16.57  ? 320 ASN B ND2 1 
ATOM   1955 N N   . LEU A 1 265 ? 22.455 11.264  -2.858  1.00 2.00   ? 321 LEU B N   1 
ATOM   1956 C CA  . LEU A 1 265 ? 21.246 10.920  -2.128  1.00 17.78  ? 321 LEU B CA  1 
ATOM   1957 C C   . LEU A 1 265 ? 19.928 10.903  -2.927  1.00 13.76  ? 321 LEU B C   1 
ATOM   1958 O O   . LEU A 1 265 ? 18.854 10.866  -2.343  1.00 24.67  ? 321 LEU B O   1 
ATOM   1959 C CB  . LEU A 1 265 ? 21.157 11.740  -0.839  1.00 22.52  ? 321 LEU B CB  1 
ATOM   1960 C CG  . LEU A 1 265 ? 22.402 11.504  0.025   1.00 15.10  ? 321 LEU B CG  1 
ATOM   1961 C CD1 . LEU A 1 265 ? 22.581 12.625  1.017   1.00 5.94   ? 321 LEU B CD1 1 
ATOM   1962 C CD2 . LEU A 1 265 ? 22.347 10.144  0.732   1.00 14.06  ? 321 LEU B CD2 1 
ATOM   1963 N N   . LEU A 1 266 ? 19.999 10.994  -4.244  1.00 15.20  ? 322 LEU B N   1 
ATOM   1964 C CA  . LEU A 1 266 ? 18.805 11.261  -5.047  1.00 14.90  ? 322 LEU B CA  1 
ATOM   1965 C C   . LEU A 1 266 ? 17.649 10.299  -4.763  1.00 11.95  ? 322 LEU B C   1 
ATOM   1966 O O   . LEU A 1 266 ? 17.872 9.161   -4.353  1.00 12.81  ? 322 LEU B O   1 
ATOM   1967 C CB  . LEU A 1 266 ? 19.157 11.251  -6.542  1.00 8.05   ? 322 LEU B CB  1 
ATOM   1968 C CG  . LEU A 1 266 ? 20.289 12.187  -6.985  1.00 4.93   ? 322 LEU B CG  1 
ATOM   1969 C CD1 . LEU A 1 266 ? 20.612 11.991  -8.451  1.00 2.37   ? 322 LEU B CD1 1 
ATOM   1970 C CD2 . LEU A 1 266 ? 19.926 13.638  -6.704  1.00 2.00   ? 322 LEU B CD2 1 
ATOM   1971 N N   . THR A 1 267 ? 16.424 10.804  -4.921  1.00 8.92   ? 323 THR B N   1 
ATOM   1972 C CA  . THR A 1 267 ? 15.188 10.016  -4.841  1.00 11.10  ? 323 THR B CA  1 
ATOM   1973 C C   . THR A 1 267 ? 14.329 10.305  -6.069  1.00 9.91   ? 323 THR B C   1 
ATOM   1974 O O   . THR A 1 267 ? 14.587 11.240  -6.804  1.00 11.76  ? 323 THR B O   1 
ATOM   1975 C CB  . THR A 1 267 ? 14.328 10.377  -3.612  1.00 2.00   ? 323 THR B CB  1 
ATOM   1976 O OG1 . THR A 1 267 ? 14.184 11.796  -3.560  1.00 7.93   ? 323 THR B OG1 1 
ATOM   1977 C CG2 . THR A 1 267 ? 14.966 9.898   -2.347  1.00 2.00   ? 323 THR B CG2 1 
ATOM   1978 N N   . GLY A 1 268 ? 13.284 9.523   -6.275  1.00 2.00   ? 324 GLY B N   1 
ATOM   1979 C CA  . GLY A 1 268 ? 12.461 9.700   -7.448  1.00 6.20   ? 324 GLY B CA  1 
ATOM   1980 C C   . GLY A 1 268 ? 12.687 8.617   -8.479  1.00 13.79  ? 324 GLY B C   1 
ATOM   1981 O O   . GLY A 1 268 ? 13.330 7.597   -8.220  1.00 16.38  ? 324 GLY B O   1 
ATOM   1982 N N   . THR A 1 269 ? 12.146 8.857   -9.661  1.00 15.92  ? 325 THR B N   1 
ATOM   1983 C CA  . THR A 1 269 ? 12.114 7.890   -10.740 1.00 15.21  ? 325 THR B CA  1 
ATOM   1984 C C   . THR A 1 269 ? 13.148 8.281   -11.785 1.00 20.69  ? 325 THR B C   1 
ATOM   1985 O O   . THR A 1 269 ? 13.433 9.464   -11.943 1.00 21.55  ? 325 THR B O   1 
ATOM   1986 C CB  . THR A 1 269 ? 10.709 7.922   -11.355 1.00 18.64  ? 325 THR B CB  1 
ATOM   1987 O OG1 . THR A 1 269 ? 9.813  7.244   -10.473 1.00 20.10  ? 325 THR B OG1 1 
ATOM   1988 C CG2 . THR A 1 269 ? 10.657 7.263   -12.727 1.00 27.56  ? 325 THR B CG2 1 
ATOM   1989 N N   . ILE A 1 270 ? 13.745 7.297   -12.462 1.00 22.68  ? 326 ILE B N   1 
ATOM   1990 C CA  . ILE A 1 270 ? 14.488 7.585   -13.683 1.00 14.91  ? 326 ILE B CA  1 
ATOM   1991 C C   . ILE A 1 270 ? 13.485 8.122   -14.688 1.00 8.39   ? 326 ILE B C   1 
ATOM   1992 O O   . ILE A 1 270 ? 12.574 7.399   -15.098 1.00 8.57   ? 326 ILE B O   1 
ATOM   1993 C CB  . ILE A 1 270 ? 15.101 6.321   -14.307 1.00 15.23  ? 326 ILE B CB  1 
ATOM   1994 C CG1 . ILE A 1 270 ? 16.084 5.651   -13.353 1.00 2.00   ? 326 ILE B CG1 1 
ATOM   1995 C CG2 . ILE A 1 270 ? 15.785 6.664   -15.629 1.00 3.96   ? 326 ILE B CG2 1 
ATOM   1996 C CD1 . ILE A 1 270 ? 16.613 4.351   -13.872 1.00 2.00   ? 326 ILE B CD1 1 
ATOM   1997 N N   . PRO A 1 271 ? 13.650 9.388   -15.093 1.00 9.77   ? 327 PRO B N   1 
ATOM   1998 C CA  . PRO A 1 271 ? 12.707 10.096  -15.977 1.00 9.06   ? 327 PRO B CA  1 
ATOM   1999 C C   . PRO A 1 271 ? 12.432 9.405   -17.318 1.00 16.72  ? 327 PRO B C   1 
ATOM   2000 O O   . PRO A 1 271 ? 13.348 8.923   -17.986 1.00 24.22  ? 327 PRO B O   1 
ATOM   2001 C CB  . PRO A 1 271 ? 13.397 11.442  -16.211 1.00 11.73  ? 327 PRO B CB  1 
ATOM   2002 C CG  . PRO A 1 271 ? 14.261 11.637  -14.998 1.00 13.72  ? 327 PRO B CG  1 
ATOM   2003 C CD  . PRO A 1 271 ? 14.753 10.259  -14.649 1.00 14.35  ? 327 PRO B CD  1 
ATOM   2004 N N   . ARG A 1 272 ? 11.162 9.371   -17.706 1.00 15.56  ? 328 ARG B N   1 
ATOM   2005 C CA  . ARG A 1 272 ? 10.763 8.818   -18.995 1.00 11.88  ? 328 ARG B CA  1 
ATOM   2006 C C   . ARG A 1 272 ? 11.215 9.721   -20.141 1.00 22.42  ? 328 ARG B C   1 
ATOM   2007 O O   . ARG A 1 272 ? 11.312 9.274   -21.287 1.00 32.87  ? 328 ARG B O   1 
ATOM   2008 C CB  . ARG A 1 272 ? 9.240  8.599   -19.054 1.00 7.60   ? 328 ARG B CB  1 
ATOM   2009 C CG  . ARG A 1 272 ? 8.751  7.396   -18.241 1.00 14.23  ? 328 ARG B CG  1 
ATOM   2010 C CD  . ARG A 1 272 ? 7.221  7.244   -18.228 1.00 26.76  ? 328 ARG B CD  1 
ATOM   2011 N NE  . ARG A 1 272 ? 6.523  8.436   -17.741 1.00 36.39  ? 328 ARG B NE  1 
ATOM   2012 C CZ  . ARG A 1 272 ? 6.029  9.385   -18.535 1.00 42.31  ? 328 ARG B CZ  1 
ATOM   2013 N NH1 . ARG A 1 272 ? 6.158  9.276   -19.857 1.00 47.80  ? 328 ARG B NH1 1 
ATOM   2014 N NH2 . ARG A 1 272 ? 5.413  10.444  -18.015 1.00 32.39  ? 328 ARG B NH2 1 
ATOM   2015 N N   . SER A 1 273 ? 11.493 10.987  -19.842 1.00 2.00   ? 329 SER B N   1 
ATOM   2016 C CA  . SER A 1 273 ? 11.973 11.903  -20.871 1.00 2.00   ? 329 SER B CA  1 
ATOM   2017 C C   . SER A 1 273 ? 13.346 11.502  -21.424 1.00 7.61   ? 329 SER B C   1 
ATOM   2018 O O   . SER A 1 273 ? 13.725 11.920  -22.522 1.00 14.65  ? 329 SER B O   1 
ATOM   2019 C CB  . SER A 1 273 ? 11.994 13.342  -20.364 1.00 10.31  ? 329 SER B CB  1 
ATOM   2020 O OG  . SER A 1 273 ? 12.611 13.439  -19.095 1.00 13.49  ? 329 SER B OG  1 
ATOM   2021 N N   . PHE A 1 274 ? 14.074 10.682  -20.667 1.00 3.98   ? 330 PHE B N   1 
ATOM   2022 C CA  . PHE A 1 274 ? 15.390 10.187  -21.078 1.00 9.81   ? 330 PHE B CA  1 
ATOM   2023 C C   . PHE A 1 274 ? 15.329 9.469   -22.436 1.00 9.59   ? 330 PHE B C   1 
ATOM   2024 O O   . PHE A 1 274 ? 16.331 9.375   -23.154 1.00 9.75   ? 330 PHE B O   1 
ATOM   2025 C CB  . PHE A 1 274 ? 15.990 9.247   -20.010 1.00 10.09  ? 330 PHE B CB  1 
ATOM   2026 C CG  . PHE A 1 274 ? 16.767 9.952   -18.922 1.00 10.55  ? 330 PHE B CG  1 
ATOM   2027 C CD1 . PHE A 1 274 ? 16.587 11.306  -18.665 1.00 11.55  ? 330 PHE B CD1 1 
ATOM   2028 C CD2 . PHE A 1 274 ? 17.683 9.254   -18.147 1.00 11.61  ? 330 PHE B CD2 1 
ATOM   2029 C CE1 . PHE A 1 274 ? 17.309 11.946  -17.654 1.00 5.32   ? 330 PHE B CE1 1 
ATOM   2030 C CE2 . PHE A 1 274 ? 18.401 9.897   -17.126 1.00 6.21   ? 330 PHE B CE2 1 
ATOM   2031 C CZ  . PHE A 1 274 ? 18.212 11.235  -16.891 1.00 2.00   ? 330 PHE B CZ  1 
ATOM   2032 N N   . GLY A 1 275 ? 14.154 8.958   -22.782 1.00 6.09   ? 331 GLY B N   1 
ATOM   2033 C CA  . GLY A 1 275 ? 13.984 8.295   -24.060 1.00 7.41   ? 331 GLY B CA  1 
ATOM   2034 C C   . GLY A 1 275 ? 14.288 9.248   -25.202 1.00 8.22   ? 331 GLY B C   1 
ATOM   2035 O O   . GLY A 1 275 ? 14.822 8.856   -26.232 1.00 13.59  ? 331 GLY B O   1 
ATOM   2036 N N   . LYS A 1 276 ? 13.958 10.516  -24.998 1.00 3.83   ? 332 LYS B N   1 
ATOM   2037 C CA  . LYS A 1 276 ? 14.196 11.542  -25.987 1.00 5.26   ? 332 LYS B CA  1 
ATOM   2038 C C   . LYS A 1 276 ? 15.685 11.776  -26.241 1.00 17.35  ? 332 LYS B C   1 
ATOM   2039 O O   . LYS A 1 276 ? 16.038 12.531  -27.163 1.00 16.26  ? 332 LYS B O   1 
ATOM   2040 C CB  . LYS A 1 276 ? 13.585 12.864  -25.536 1.00 8.82   ? 332 LYS B CB  1 
ATOM   2041 C CG  . LYS A 1 276 ? 12.100 12.863  -25.263 1.00 22.30  ? 332 LYS B CG  1 
ATOM   2042 C CD  . LYS A 1 276 ? 11.669 14.256  -24.771 1.00 39.95  ? 332 LYS B CD  1 
ATOM   2043 C CE  . LYS A 1 276 ? 10.148 14.428  -24.760 1.00 60.77  ? 332 LYS B CE  1 
ATOM   2044 N NZ  . LYS A 1 276 ? 9.556  14.571  -26.136 1.00 72.41  ? 332 LYS B NZ  1 
ATOM   2045 N N   . LEU A 1 277 ? 16.566 11.171  -25.438 1.00 16.97  ? 333 LEU B N   1 
ATOM   2046 C CA  . LEU A 1 277 ? 17.976 11.531  -25.552 1.00 16.47  ? 333 LEU B CA  1 
ATOM   2047 C C   . LEU A 1 277 ? 18.668 10.590  -26.506 1.00 18.75  ? 333 LEU B C   1 
ATOM   2048 O O   . LEU A 1 277 ? 19.090 9.498   -26.121 1.00 13.71  ? 333 LEU B O   1 
ATOM   2049 C CB  . LEU A 1 277 ? 18.662 11.448  -24.189 1.00 16.03  ? 333 LEU B CB  1 
ATOM   2050 C CG  . LEU A 1 277 ? 18.297 12.475  -23.110 1.00 11.92  ? 333 LEU B CG  1 
ATOM   2051 C CD1 . LEU A 1 277 ? 19.151 12.259  -21.870 1.00 10.29  ? 333 LEU B CD1 1 
ATOM   2052 C CD2 . LEU A 1 277 ? 18.448 13.899  -23.628 1.00 5.78   ? 333 LEU B CD2 1 
ATOM   2053 N N   . GLU A 1 278 ? 18.899 11.088  -27.718 1.00 25.27  ? 334 GLU B N   1 
ATOM   2054 C CA  . GLU A 1 278 ? 19.277 10.257  -28.857 1.00 11.12  ? 334 GLU B CA  1 
ATOM   2055 C C   . GLU A 1 278 ? 20.744 9.901   -28.792 1.00 6.67   ? 334 GLU B C   1 
ATOM   2056 O O   . GLU A 1 278 ? 21.154 8.856   -29.274 1.00 14.78  ? 334 GLU B O   1 
ATOM   2057 C CB  . GLU A 1 278 ? 18.998 11.007  -30.160 1.00 20.52  ? 334 GLU B CB  1 
ATOM   2058 C CG  . GLU A 1 278 ? 17.627 11.679  -30.238 1.00 34.08  ? 334 GLU B CG  1 
ATOM   2059 C CD  . GLU A 1 278 ? 16.601 10.849  -31.000 1.00 40.12  ? 334 GLU B CD  1 
ATOM   2060 O OE1 . GLU A 1 278 ? 16.874 10.499  -32.168 1.00 32.34  ? 334 GLU B OE1 1 
ATOM   2061 O OE2 . GLU A 1 278 ? 15.524 10.547  -30.429 1.00 48.44  ? 334 GLU B OE2 1 
ATOM   2062 N N   . ASN A 1 279 ? 21.532 10.786  -28.193 1.00 11.51  ? 335 ASN B N   1 
ATOM   2063 C CA  . ASN A 1 279 ? 22.978 10.611  -28.107 1.00 9.95   ? 335 ASN B CA  1 
ATOM   2064 C C   . ASN A 1 279 ? 23.564 10.013  -26.828 1.00 9.07   ? 335 ASN B C   1 
ATOM   2065 O O   . ASN A 1 279 ? 24.785 9.949   -26.713 1.00 7.90   ? 335 ASN B O   1 
ATOM   2066 C CB  . ASN A 1 279 ? 23.685 11.923  -28.430 1.00 8.76   ? 335 ASN B CB  1 
ATOM   2067 C CG  . ASN A 1 279 ? 23.200 12.522  -29.729 1.00 9.89   ? 335 ASN B CG  1 
ATOM   2068 O OD1 . ASN A 1 279 ? 22.913 13.720  -29.815 1.00 9.38   ? 335 ASN B OD1 1 
ATOM   2069 N ND2 . ASN A 1 279 ? 23.078 11.681  -30.746 1.00 8.37   ? 335 ASN B ND2 1 
ATOM   2070 N N   . LEU A 1 280 ? 22.725 9.576   -25.880 1.00 10.68  ? 336 LEU B N   1 
ATOM   2071 C CA  . LEU A 1 280 ? 23.233 9.130   -24.582 1.00 2.00   ? 336 LEU B CA  1 
ATOM   2072 C C   . LEU A 1 280 ? 24.024 7.828   -24.773 1.00 7.76   ? 336 LEU B C   1 
ATOM   2073 O O   . LEU A 1 280 ? 23.477 6.812   -25.200 1.00 5.23   ? 336 LEU B O   1 
ATOM   2074 C CB  . LEU A 1 280 ? 22.044 8.899   -23.642 1.00 2.00   ? 336 LEU B CB  1 
ATOM   2075 C CG  . LEU A 1 280 ? 22.124 8.511   -22.143 1.00 9.74   ? 336 LEU B CG  1 
ATOM   2076 C CD1 . LEU A 1 280 ? 22.585 9.673   -21.278 1.00 2.00   ? 336 LEU B CD1 1 
ATOM   2077 C CD2 . LEU A 1 280 ? 20.803 7.983   -21.629 1.00 2.00   ? 336 LEU B CD2 1 
ATOM   2078 N N   . GLN A 1 281 ? 25.327 7.884   -24.500 1.00 2.00   ? 337 GLN B N   1 
ATOM   2079 C CA  . GLN A 1 281 ? 26.189 6.698   -24.462 1.00 14.58  ? 337 GLN B CA  1 
ATOM   2080 C C   . GLN A 1 281 ? 26.259 6.052   -23.081 1.00 19.15  ? 337 GLN B C   1 
ATOM   2081 O O   . GLN A 1 281 ? 26.321 4.828   -22.941 1.00 20.41  ? 337 GLN B O   1 
ATOM   2082 C CB  . GLN A 1 281 ? 27.606 7.005   -24.965 1.00 10.42  ? 337 GLN B CB  1 
ATOM   2083 C CG  . GLN A 1 281 ? 27.671 8.001   -26.096 1.00 16.86  ? 337 GLN B CG  1 
ATOM   2084 C CD  . GLN A 1 281 ? 28.968 7.910   -26.869 1.00 20.10  ? 337 GLN B CD  1 
ATOM   2085 O OE1 . GLN A 1 281 ? 29.923 7.265   -26.442 1.00 14.85  ? 337 GLN B OE1 1 
ATOM   2086 N NE2 . GLN A 1 281 ? 29.001 8.549   -28.022 1.00 29.43  ? 337 GLN B NE2 1 
ATOM   2087 N N   . GLU A 1 282 ? 26.327 6.899   -22.061 1.00 19.03  ? 338 GLU B N   1 
ATOM   2088 C CA  . GLU A 1 282 ? 26.600 6.419   -20.714 1.00 22.46  ? 338 GLU B CA  1 
ATOM   2089 C C   . GLU A 1 282 ? 25.682 7.051   -19.671 1.00 9.25   ? 338 GLU B C   1 
ATOM   2090 O O   . GLU A 1 282 ? 25.578 8.273   -19.579 1.00 5.62   ? 338 GLU B O   1 
ATOM   2091 C CB  . GLU A 1 282 ? 28.070 6.650   -20.379 1.00 29.62  ? 338 GLU B CB  1 
ATOM   2092 C CG  . GLU A 1 282 ? 28.494 6.138   -19.017 1.00 37.65  ? 338 GLU B CG  1 
ATOM   2093 C CD  . GLU A 1 282 ? 29.987 5.863   -18.954 1.00 47.22  ? 338 GLU B CD  1 
ATOM   2094 O OE1 . GLU A 1 282 ? 30.672 6.082   -19.994 1.00 49.11  ? 338 GLU B OE1 1 
ATOM   2095 O OE2 . GLU A 1 282 ? 30.463 5.421   -17.877 1.00 43.84  ? 338 GLU B OE2 1 
ATOM   2096 N N   . LEU A 1 283 ? 24.991 6.207   -18.914 1.00 3.01   ? 339 LEU B N   1 
ATOM   2097 C CA  . LEU A 1 283 ? 24.109 6.676   -17.839 1.00 7.13   ? 339 LEU B CA  1 
ATOM   2098 C C   . LEU A 1 283 ? 24.485 6.014   -16.516 1.00 8.52   ? 339 LEU B C   1 
ATOM   2099 O O   . LEU A 1 283 ? 24.306 4.802   -16.340 1.00 5.77   ? 339 LEU B O   1 
ATOM   2100 C CB  . LEU A 1 283 ? 22.649 6.369   -18.156 1.00 5.79   ? 339 LEU B CB  1 
ATOM   2101 C CG  . LEU A 1 283 ? 21.595 6.800   -17.140 1.00 2.00   ? 339 LEU B CG  1 
ATOM   2102 C CD1 . LEU A 1 283 ? 21.797 8.236   -16.725 1.00 19.45  ? 339 LEU B CD1 1 
ATOM   2103 C CD2 . LEU A 1 283 ? 20.214 6.618   -17.744 1.00 8.33   ? 339 LEU B CD2 1 
ATOM   2104 N N   . GLN A 1 284 ? 25.003 6.817   -15.592 1.00 5.31   ? 340 GLN B N   1 
ATOM   2105 C CA  . GLN A 1 284 ? 25.504 6.299   -14.336 1.00 2.00   ? 340 GLN B CA  1 
ATOM   2106 C C   . GLN A 1 284 ? 24.743 6.945   -13.173 1.00 4.65   ? 340 GLN B C   1 
ATOM   2107 O O   . GLN A 1 284 ? 24.804 8.165   -12.993 1.00 5.23   ? 340 GLN B O   1 
ATOM   2108 C CB  . GLN A 1 284 ? 27.002 6.564   -14.264 1.00 2.00   ? 340 GLN B CB  1 
ATOM   2109 C CG  . GLN A 1 284 ? 27.839 5.633   -15.134 1.00 4.28   ? 340 GLN B CG  1 
ATOM   2110 C CD  . GLN A 1 284 ? 29.135 5.223   -14.438 1.00 24.62  ? 340 GLN B CD  1 
ATOM   2111 O OE1 . GLN A 1 284 ? 29.770 6.025   -13.748 1.00 23.92  ? 340 GLN B OE1 1 
ATOM   2112 N NE2 . GLN A 1 284 ? 29.517 3.960   -14.596 1.00 35.48  ? 340 GLN B NE2 1 
ATOM   2113 N N   . LEU A 1 285 ? 23.897 6.137   -12.524 1.00 2.36   ? 341 LEU B N   1 
ATOM   2114 C CA  . LEU A 1 285 ? 23.119 6.467   -11.316 1.00 3.67   ? 341 LEU B CA  1 
ATOM   2115 C C   . LEU A 1 285 ? 23.501 5.728   -10.011 1.00 4.77   ? 341 LEU B C   1 
ATOM   2116 O O   . LEU A 1 285 ? 22.817 5.842   -8.985  1.00 3.56   ? 341 LEU B O   1 
ATOM   2117 C CB  . LEU A 1 285 ? 21.618 6.386   -11.604 1.00 2.00   ? 341 LEU B CB  1 
ATOM   2118 C CG  . LEU A 1 285 ? 21.278 7.239   -12.832 1.00 2.00   ? 341 LEU B CG  1 
ATOM   2119 C CD1 . LEU A 1 285 ? 19.831 7.051   -13.272 1.00 2.00   ? 341 LEU B CD1 1 
ATOM   2120 C CD2 . LEU A 1 285 ? 21.613 8.722   -12.601 1.00 2.00   ? 341 LEU B CD2 1 
ATOM   2121 N N   . SER A 1 286 ? 24.552 4.926   -10.071 1.00 7.87   ? 342 SER B N   1 
ATOM   2122 C CA  . SER A 1 286 ? 24.897 4.025   -8.980  1.00 5.87   ? 342 SER B CA  1 
ATOM   2123 C C   . SER A 1 286 ? 24.996 4.687   -7.603  1.00 5.93   ? 342 SER B C   1 
ATOM   2124 O O   . SER A 1 286 ? 25.516 5.795   -7.468  1.00 6.37   ? 342 SER B O   1 
ATOM   2125 C CB  . SER A 1 286 ? 26.230 3.352   -9.304  1.00 13.50  ? 342 SER B CB  1 
ATOM   2126 O OG  . SER A 1 286 ? 26.258 2.931   -10.659 1.00 11.60  ? 342 SER B OG  1 
ATOM   2127 N N   . VAL A 1 287 ? 24.534 3.975   -6.575  1.00 12.91  ? 343 VAL B N   1 
ATOM   2128 C CA  . VAL A 1 287 ? 24.551 4.481   -5.195  1.00 2.00   ? 343 VAL B CA  1 
ATOM   2129 C C   . VAL A 1 287 ? 23.743 5.768   -5.026  1.00 13.64  ? 343 VAL B C   1 
ATOM   2130 O O   . VAL A 1 287 ? 24.273 6.872   -4.967  1.00 2.00   ? 343 VAL B O   1 
ATOM   2131 C CB  . VAL A 1 287 ? 25.972 4.620   -4.627  1.00 2.00   ? 343 VAL B CB  1 
ATOM   2132 C CG1 . VAL A 1 287 ? 25.917 4.731   -3.142  1.00 2.00   ? 343 VAL B CG1 1 
ATOM   2133 C CG2 . VAL A 1 287 ? 26.805 3.409   -5.020  1.00 2.00   ? 343 VAL B CG2 1 
ATOM   2134 N N   . ASN A 1 288 ? 22.434 5.587   -5.042  1.00 2.00   ? 344 ASN B N   1 
ATOM   2135 C CA  . ASN A 1 288 ? 21.472 6.622   -4.745  1.00 2.00   ? 344 ASN B CA  1 
ATOM   2136 C C   . ASN A 1 288 ? 20.256 5.924   -4.150  1.00 14.11  ? 344 ASN B C   1 
ATOM   2137 O O   . ASN A 1 288 ? 20.279 4.717   -3.928  1.00 11.73  ? 344 ASN B O   1 
ATOM   2138 C CB  . ASN A 1 288 ? 21.072 7.385   -6.005  1.00 2.00   ? 344 ASN B CB  1 
ATOM   2139 C CG  . ASN A 1 288 ? 22.170 8.302   -6.509  1.00 5.24   ? 344 ASN B CG  1 
ATOM   2140 O OD1 . ASN A 1 288 ? 22.361 9.397   -5.987  1.00 2.00   ? 344 ASN B OD1 1 
ATOM   2141 N ND2 . ASN A 1 288 ? 22.884 7.867   -7.546  1.00 8.28   ? 344 ASN B ND2 1 
ATOM   2142 N N   . GLN A 1 289 ? 19.216 6.691   -3.848  1.00 16.18  ? 345 GLN B N   1 
ATOM   2143 C CA  . GLN A 1 289 ? 17.971 6.145   -3.308  1.00 18.95  ? 345 GLN B CA  1 
ATOM   2144 C C   . GLN A 1 289 ? 16.850 5.963   -4.329  1.00 16.57  ? 345 GLN B C   1 
ATOM   2145 O O   . GLN A 1 289 ? 15.706 5.724   -3.947  1.00 21.32  ? 345 GLN B O   1 
ATOM   2146 C CB  . GLN A 1 289 ? 17.508 6.919   -2.076  1.00 26.13  ? 345 GLN B CB  1 
ATOM   2147 C CG  . GLN A 1 289 ? 18.264 6.537   -0.811  1.00 23.27  ? 345 GLN B CG  1 
ATOM   2148 C CD  . GLN A 1 289 ? 18.330 7.685   0.154   1.00 30.96  ? 345 GLN B CD  1 
ATOM   2149 O OE1 . GLN A 1 289 ? 17.297 8.171   0.623   1.00 38.58  ? 345 GLN B OE1 1 
ATOM   2150 N NE2 . GLN A 1 289 ? 19.545 8.155   0.436   1.00 28.19  ? 345 GLN B NE2 1 
ATOM   2151 N N   . ILE A 1 290 ? 17.188 6.135   -5.607  1.00 13.33  ? 346 ILE B N   1 
ATOM   2152 C CA  . ILE A 1 290 ? 16.246 6.110   -6.733  1.00 9.17   ? 346 ILE B CA  1 
ATOM   2153 C C   . ILE A 1 290 ? 15.303 4.898   -6.731  1.00 14.09  ? 346 ILE B C   1 
ATOM   2154 O O   . ILE A 1 290 ? 15.723 3.763   -6.500  1.00 15.55  ? 346 ILE B O   1 
ATOM   2155 C CB  . ILE A 1 290 ? 17.025 6.168   -8.079  1.00 2.00   ? 346 ILE B CB  1 
ATOM   2156 C CG1 . ILE A 1 290 ? 17.781 7.488   -8.192  1.00 2.00   ? 346 ILE B CG1 1 
ATOM   2157 C CG2 . ILE A 1 290 ? 16.099 6.024   -9.283  1.00 4.22   ? 346 ILE B CG2 1 
ATOM   2158 C CD1 . ILE A 1 290 ? 18.451 7.697   -9.519  1.00 5.42   ? 346 ILE B CD1 1 
ATOM   2159 N N   . SER A 1 291 ? 14.021 5.159   -6.982  1.00 11.37  ? 347 SER B N   1 
ATOM   2160 C CA  . SER A 1 291 ? 12.993 4.123   -6.989  1.00 12.29  ? 347 SER B CA  1 
ATOM   2161 C C   . SER A 1 291 ? 12.268 4.072   -8.336  1.00 19.45  ? 347 SER B C   1 
ATOM   2162 O O   . SER A 1 291 ? 12.653 4.747   -9.288  1.00 37.74  ? 347 SER B O   1 
ATOM   2163 C CB  . SER A 1 291 ? 11.986 4.377   -5.874  1.00 8.93   ? 347 SER B CB  1 
ATOM   2164 O OG  . SER A 1 291 ? 11.442 5.681   -5.992  1.00 12.71  ? 347 SER B OG  1 
ATOM   2165 N N   . GLY A 1 292 ? 11.222 3.258   -8.414  1.00 2.04   ? 348 GLY B N   1 
ATOM   2166 C CA  . GLY A 1 292 ? 10.448 3.110   -9.628  1.00 2.00   ? 348 GLY B CA  1 
ATOM   2167 C C   . GLY A 1 292 ? 10.876 1.865   -10.367 1.00 14.32  ? 348 GLY B C   1 
ATOM   2168 O O   . GLY A 1 292 ? 11.798 1.164   -9.939  1.00 8.03   ? 348 GLY B O   1 
ATOM   2169 N N   . THR A 1 293 ? 10.157 1.554   -11.443 1.00 18.31  ? 349 THR B N   1 
ATOM   2170 C CA  . THR A 1 293 ? 10.592 0.574   -12.446 1.00 14.81  ? 349 THR B CA  1 
ATOM   2171 C C   . THR A 1 293 ? 11.537 1.216   -13.471 1.00 13.81  ? 349 THR B C   1 
ATOM   2172 O O   . THR A 1 293 ? 11.517 2.429   -13.651 1.00 19.80  ? 349 THR B O   1 
ATOM   2173 C CB  . THR A 1 293 ? 9.385  -0.061  -13.158 1.00 11.08  ? 349 THR B CB  1 
ATOM   2174 O OG1 . THR A 1 293 ? 8.471  0.967   -13.539 1.00 18.74  ? 349 THR B OG1 1 
ATOM   2175 C CG2 . THR A 1 293 ? 8.645  -1.011  -12.238 1.00 6.02   ? 349 THR B CG2 1 
ATOM   2176 N N   . ILE A 1 294 ? 12.382 0.424   -14.125 1.00 17.15  ? 350 ILE B N   1 
ATOM   2177 C CA  . ILE A 1 294 ? 13.169 0.953   -15.243 1.00 12.49  ? 350 ILE B CA  1 
ATOM   2178 C C   . ILE A 1 294 ? 12.200 1.284   -16.371 1.00 15.12  ? 350 ILE B C   1 
ATOM   2179 O O   . ILE A 1 294 ? 11.470 0.408   -16.838 1.00 22.32  ? 350 ILE B O   1 
ATOM   2180 C CB  . ILE A 1 294 ? 14.215 -0.055  -15.766 1.00 6.32   ? 350 ILE B CB  1 
ATOM   2181 C CG1 . ILE A 1 294 ? 15.125 -0.529  -14.638 1.00 5.27   ? 350 ILE B CG1 1 
ATOM   2182 C CG2 . ILE A 1 294 ? 15.058 0.575   -16.865 1.00 11.01  ? 350 ILE B CG2 1 
ATOM   2183 C CD1 . ILE A 1 294 ? 15.935 -1.715  -14.995 1.00 2.00   ? 350 ILE B CD1 1 
ATOM   2184 N N   . PRO A 1 295 ? 12.172 2.556   -16.802 1.00 10.26  ? 351 PRO B N   1 
ATOM   2185 C CA  . PRO A 1 295 ? 11.200 3.010   -17.809 1.00 7.45   ? 351 PRO B CA  1 
ATOM   2186 C C   . PRO A 1 295 ? 11.468 2.441   -19.210 1.00 9.41   ? 351 PRO B C   1 
ATOM   2187 O O   . PRO A 1 295 ? 12.612 2.428   -19.671 1.00 12.46  ? 351 PRO B O   1 
ATOM   2188 C CB  . PRO A 1 295 ? 11.352 4.531   -17.780 1.00 4.44   ? 351 PRO B CB  1 
ATOM   2189 C CG  . PRO A 1 295 ? 12.740 4.767   -17.246 1.00 2.00   ? 351 PRO B CG  1 
ATOM   2190 C CD  . PRO A 1 295 ? 13.082 3.627   -16.361 1.00 5.91   ? 351 PRO B CD  1 
ATOM   2191 N N   . GLU A 1 296 ? 10.415 1.973   -19.874 1.00 14.41  ? 352 GLU B N   1 
ATOM   2192 C CA  . GLU A 1 296 ? 10.556 1.361   -21.197 1.00 15.09  ? 352 GLU B CA  1 
ATOM   2193 C C   . GLU A 1 296 ? 11.178 2.328   -22.190 1.00 15.96  ? 352 GLU B C   1 
ATOM   2194 O O   . GLU A 1 296 ? 11.924 1.920   -23.077 1.00 16.85  ? 352 GLU B O   1 
ATOM   2195 C CB  . GLU A 1 296 ? 9.208  0.891   -21.740 1.00 16.53  ? 352 GLU B CB  1 
ATOM   2196 C CG  . GLU A 1 296 ? 8.466  -0.089  -20.851 1.00 26.47  ? 352 GLU B CG  1 
ATOM   2197 C CD  . GLU A 1 296 ? 9.110  -1.461  -20.807 1.00 33.09  ? 352 GLU B CD  1 
ATOM   2198 O OE1 . GLU A 1 296 ? 9.743  -1.791  -19.783 1.00 44.80  ? 352 GLU B OE1 1 
ATOM   2199 O OE2 . GLU A 1 296 ? 8.966  -2.215  -21.788 1.00 27.41  ? 352 GLU B OE2 1 
ATOM   2200 N N   . GLU A 1 297 ? 10.887 3.613   -22.039 1.00 2.00   ? 353 GLU B N   1 
ATOM   2201 C CA  . GLU A 1 297 ? 11.389 4.580   -23.001 1.00 2.00   ? 353 GLU B CA  1 
ATOM   2202 C C   . GLU A 1 297 ? 12.899 4.719   -23.017 1.00 10.30  ? 353 GLU B C   1 
ATOM   2203 O O   . GLU A 1 297 ? 13.447 5.209   -23.988 1.00 13.83  ? 353 GLU B O   1 
ATOM   2204 C CB  . GLU A 1 297 ? 10.710 5.950   -22.873 1.00 6.68   ? 353 GLU B CB  1 
ATOM   2205 C CG  . GLU A 1 297 ? 10.133 6.280   -21.531 1.00 11.20  ? 353 GLU B CG  1 
ATOM   2206 C CD  . GLU A 1 297 ? 8.816  5.577   -21.241 1.00 13.35  ? 353 GLU B CD  1 
ATOM   2207 O OE1 . GLU A 1 297 ? 7.744  6.167   -21.510 1.00 18.18  ? 353 GLU B OE1 1 
ATOM   2208 O OE2 . GLU A 1 297 ? 8.865  4.442   -20.715 1.00 11.82  ? 353 GLU B OE2 1 
ATOM   2209 N N   . LEU A 1 298 ? 13.576 4.273   -21.957 1.00 17.58  ? 354 LEU B N   1 
ATOM   2210 C CA  . LEU A 1 298 ? 15.045 4.325   -21.916 1.00 16.02  ? 354 LEU B CA  1 
ATOM   2211 C C   . LEU A 1 298 ? 15.649 3.383   -22.963 1.00 21.15  ? 354 LEU B C   1 
ATOM   2212 O O   . LEU A 1 298 ? 16.793 3.541   -23.375 1.00 11.12  ? 354 LEU B O   1 
ATOM   2213 C CB  . LEU A 1 298 ? 15.585 4.003   -20.517 1.00 13.02  ? 354 LEU B CB  1 
ATOM   2214 C CG  . LEU A 1 298 ? 17.067 4.335   -20.238 1.00 14.95  ? 354 LEU B CG  1 
ATOM   2215 C CD1 . LEU A 1 298 ? 17.305 5.828   -20.043 1.00 14.06  ? 354 LEU B CD1 1 
ATOM   2216 C CD2 . LEU A 1 298 ? 17.599 3.573   -19.046 1.00 10.67  ? 354 LEU B CD2 1 
ATOM   2217 N N   . THR A 1 299 ? 14.857 2.415   -23.410 1.00 29.67  ? 355 THR B N   1 
ATOM   2218 C CA  . THR A 1 299 ? 15.283 1.506   -24.468 1.00 20.71  ? 355 THR B CA  1 
ATOM   2219 C C   . THR A 1 299 ? 15.285 2.160   -25.866 1.00 13.03  ? 355 THR B C   1 
ATOM   2220 O O   . THR A 1 299 ? 15.682 1.533   -26.837 1.00 16.51  ? 355 THR B O   1 
ATOM   2221 C CB  . THR A 1 299 ? 14.453 0.212   -24.471 1.00 15.30  ? 355 THR B CB  1 
ATOM   2222 O OG1 . THR A 1 299 ? 13.119 0.499   -24.896 1.00 15.24  ? 355 THR B OG1 1 
ATOM   2223 C CG2 . THR A 1 299 ? 14.416 -0.403  -23.075 1.00 6.89   ? 355 THR B CG2 1 
ATOM   2224 N N   . ASN A 1 300 ? 14.851 3.417   -25.954 1.00 5.35   ? 356 ASN B N   1 
ATOM   2225 C CA  . ASN A 1 300 ? 14.931 4.219   -27.181 1.00 2.00   ? 356 ASN B CA  1 
ATOM   2226 C C   . ASN A 1 300 ? 16.302 4.878   -27.347 1.00 18.01  ? 356 ASN B C   1 
ATOM   2227 O O   . ASN A 1 300 ? 16.528 5.693   -28.244 1.00 12.86  ? 356 ASN B O   1 
ATOM   2228 C CB  . ASN A 1 300 ? 13.881 5.319   -27.161 1.00 6.13   ? 356 ASN B CB  1 
ATOM   2229 C CG  . ASN A 1 300 ? 12.691 4.999   -28.017 1.00 19.58  ? 356 ASN B CG  1 
ATOM   2230 O OD1 . ASN A 1 300 ? 12.473 3.849   -28.384 1.00 16.87  ? 356 ASN B OD1 1 
ATOM   2231 N ND2 . ASN A 1 300 ? 11.910 6.021   -28.351 1.00 32.45  ? 356 ASN B ND2 1 
ATOM   2232 N N   . CYS A 1 301 ? 17.206 4.517   -26.451 1.00 29.88  ? 357 CYS B N   1 
ATOM   2233 C CA  . CYS A 1 301 ? 18.478 5.201   -26.220 1.00 29.22  ? 357 CYS B CA  1 
ATOM   2234 C C   . CYS A 1 301 ? 19.658 4.805   -27.096 1.00 28.23  ? 357 CYS B C   1 
ATOM   2235 O O   . CYS A 1 301 ? 20.798 4.886   -26.659 1.00 27.23  ? 357 CYS B O   1 
ATOM   2236 C CB  . CYS A 1 301 ? 18.840 5.291   -24.748 1.00 32.06  ? 357 CYS B CB  1 
ATOM   2237 S SG  . CYS A 1 301 ? 18.023 6.702   -23.989 1.00 19.20  ? 357 CYS B SG  1 
ATOM   2238 N N   . THR A 1 302 ? 19.367 4.382   -28.323 1.00 29.36  ? 358 THR B N   1 
ATOM   2239 C CA  . THR A 1 302 ? 20.193 3.529   -29.177 1.00 23.20  ? 358 THR B CA  1 
ATOM   2240 C C   . THR A 1 302 ? 21.715 3.570   -28.989 1.00 15.80  ? 358 THR B C   1 
ATOM   2241 O O   . THR A 1 302 ? 22.364 2.536   -29.081 1.00 16.42  ? 358 THR B O   1 
ATOM   2242 C CB  . THR A 1 302 ? 19.971 4.040   -30.622 1.00 23.89  ? 358 THR B CB  1 
ATOM   2243 O OG1 . THR A 1 302 ? 18.620 3.800   -31.011 1.00 24.21  ? 358 THR B OG1 1 
ATOM   2244 C CG2 . THR A 1 302 ? 20.913 3.397   -31.618 1.00 36.80  ? 358 THR B CG2 1 
ATOM   2245 N N   . LYS A 1 303 ? 22.291 4.731   -28.713 1.00 9.10   ? 359 LYS B N   1 
ATOM   2246 C CA  . LYS A 1 303 ? 23.743 4.830   -28.631 1.00 2.00   ? 359 LYS B CA  1 
ATOM   2247 C C   . LYS A 1 303 ? 24.354 4.437   -27.265 1.00 7.50   ? 359 LYS B C   1 
ATOM   2248 O O   . LYS A 1 303 ? 25.569 4.503   -27.083 1.00 12.61  ? 359 LYS B O   1 
ATOM   2249 C CB  . LYS A 1 303 ? 24.188 6.231   -29.076 1.00 2.00   ? 359 LYS B CB  1 
ATOM   2250 C CG  . LYS A 1 303 ? 23.717 6.587   -30.504 1.00 3.04   ? 359 LYS B CG  1 
ATOM   2251 C CD  . LYS A 1 303 ? 23.886 8.052   -30.867 1.00 9.16   ? 359 LYS B CD  1 
ATOM   2252 C CE  . LYS A 1 303 ? 25.265 8.338   -31.418 1.00 19.28  ? 359 LYS B CE  1 
ATOM   2253 N NZ  . LYS A 1 303 ? 25.283 9.618   -32.197 1.00 23.53  ? 359 LYS B NZ  1 
ATOM   2254 N N   . LEU A 1 304 ? 23.506 4.015   -26.326 1.00 4.55   ? 360 LEU B N   1 
ATOM   2255 C CA  . LEU A 1 304 ? 23.883 3.657   -24.949 1.00 2.00   ? 360 LEU B CA  1 
ATOM   2256 C C   . LEU A 1 304 ? 24.865 2.502   -24.859 1.00 2.00   ? 360 LEU B C   1 
ATOM   2257 O O   . LEU A 1 304 ? 24.563 1.394   -25.287 1.00 35.19  ? 360 LEU B O   1 
ATOM   2258 C CB  . LEU A 1 304 ? 22.619 3.205   -24.225 1.00 2.00   ? 360 LEU B CB  1 
ATOM   2259 C CG  . LEU A 1 304 ? 22.309 3.330   -22.740 1.00 14.53  ? 360 LEU B CG  1 
ATOM   2260 C CD1 . LEU A 1 304 ? 22.150 4.780   -22.311 1.00 2.00   ? 360 LEU B CD1 1 
ATOM   2261 C CD2 . LEU A 1 304 ? 21.036 2.550   -22.464 1.00 15.40  ? 360 LEU B CD2 1 
ATOM   2262 N N   . THR A 1 305 ? 26.006 2.743   -24.228 1.00 15.47  ? 361 THR B N   1 
ATOM   2263 C CA  . THR A 1 305 ? 27.022 1.716   -24.008 1.00 14.60  ? 361 THR B CA  1 
ATOM   2264 C C   . THR A 1 305 ? 27.007 1.258   -22.560 1.00 15.90  ? 361 THR B C   1 
ATOM   2265 O O   . THR A 1 305 ? 26.934 0.059   -22.286 1.00 13.95  ? 361 THR B O   1 
ATOM   2266 C CB  . THR A 1 305 ? 28.424 2.177   -24.394 1.00 14.79  ? 361 THR B CB  1 
ATOM   2267 O OG1 . THR A 1 305 ? 28.894 3.122   -23.424 1.00 20.85  ? 361 THR B OG1 1 
ATOM   2268 C CG2 . THR A 1 305 ? 28.398 2.802   -25.774 1.00 10.50  ? 361 THR B CG2 1 
ATOM   2269 N N   . HIS A 1 306 ? 27.171 2.211   -21.644 1.00 2.00   ? 362 HIS B N   1 
ATOM   2270 C CA  . HIS A 1 306 ? 27.114 1.921   -20.204 1.00 7.60   ? 362 HIS B CA  1 
ATOM   2271 C C   . HIS A 1 306 ? 25.808 2.375   -19.547 1.00 8.20   ? 362 HIS B C   1 
ATOM   2272 O O   . HIS A 1 306 ? 25.497 3.570   -19.516 1.00 2.00   ? 362 HIS B O   1 
ATOM   2273 C CB  . HIS A 1 306 ? 28.291 2.566   -19.453 1.00 2.00   ? 362 HIS B CB  1 
ATOM   2274 C CG  . HIS A 1 306 ? 29.639 2.147   -19.957 1.00 20.53  ? 362 HIS B CG  1 
ATOM   2275 N ND1 . HIS A 1 306 ? 29.879 1.845   -21.274 1.00 24.31  ? 362 HIS B ND1 1 
ATOM   2276 C CD2 . HIS A 1 306 ? 30.817 2.004   -19.310 1.00 29.01  ? 362 HIS B CD2 1 
ATOM   2277 C CE1 . HIS A 1 306 ? 31.155 1.521   -21.425 1.00 34.39  ? 362 HIS B CE1 1 
ATOM   2278 N NE2 . HIS A 1 306 ? 31.742 1.606   -20.247 1.00 35.70  ? 362 HIS B NE2 1 
ATOM   2279 N N   . LEU A 1 307 ? 25.054 1.418   -19.012 1.00 14.30  ? 363 LEU B N   1 
ATOM   2280 C CA  . LEU A 1 307 ? 23.962 1.727   -18.090 1.00 16.53  ? 363 LEU B CA  1 
ATOM   2281 C C   . LEU A 1 307 ? 24.316 1.183   -16.709 1.00 7.42   ? 363 LEU B C   1 
ATOM   2282 O O   . LEU A 1 307 ? 24.287 -0.030  -16.514 1.00 6.37   ? 363 LEU B O   1 
ATOM   2283 C CB  . LEU A 1 307 ? 22.656 1.088   -18.582 1.00 21.04  ? 363 LEU B CB  1 
ATOM   2284 C CG  . LEU A 1 307 ? 21.347 1.311   -17.810 1.00 23.01  ? 363 LEU B CG  1 
ATOM   2285 C CD1 . LEU A 1 307 ? 20.958 2.790   -17.734 1.00 19.09  ? 363 LEU B CD1 1 
ATOM   2286 C CD2 . LEU A 1 307 ? 20.235 0.506   -18.453 1.00 2.00   ? 363 LEU B CD2 1 
ATOM   2287 N N   . GLU A 1 308 ? 24.658 2.068   -15.764 1.00 10.42  ? 364 GLU B N   1 
ATOM   2288 C CA  . GLU A 1 308 ? 24.909 1.657   -14.380 1.00 8.17   ? 364 GLU B CA  1 
ATOM   2289 C C   . GLU A 1 308 ? 23.842 2.230   -13.461 1.00 8.00   ? 364 GLU B C   1 
ATOM   2290 O O   . GLU A 1 308 ? 23.897 3.398   -13.080 1.00 4.98   ? 364 GLU B O   1 
ATOM   2291 C CB  . GLU A 1 308 ? 26.239 2.227   -13.899 1.00 16.15  ? 364 GLU B CB  1 
ATOM   2292 C CG  . GLU A 1 308 ? 27.417 1.306   -13.999 1.00 19.08  ? 364 GLU B CG  1 
ATOM   2293 C CD  . GLU A 1 308 ? 27.968 1.278   -15.378 1.00 26.99  ? 364 GLU B CD  1 
ATOM   2294 O OE1 . GLU A 1 308 ? 28.976 1.971   -15.619 1.00 27.66  ? 364 GLU B OE1 1 
ATOM   2295 O OE2 . GLU A 1 308 ? 27.381 0.574   -16.224 1.00 36.68  ? 364 GLU B OE2 1 
ATOM   2296 N N   . ILE A 1 309 ? 22.871 1.395   -13.119 1.00 9.91   ? 365 ILE B N   1 
ATOM   2297 C CA  . ILE A 1 309 ? 21.784 1.756   -12.221 1.00 2.00   ? 365 ILE B CA  1 
ATOM   2298 C C   . ILE A 1 309 ? 21.848 1.078   -10.851 1.00 11.69  ? 365 ILE B C   1 
ATOM   2299 O O   . ILE A 1 309 ? 20.889 1.111   -10.082 1.00 13.61  ? 365 ILE B O   1 
ATOM   2300 C CB  . ILE A 1 309 ? 20.401 1.705   -12.908 1.00 16.08  ? 365 ILE B CB  1 
ATOM   2301 C CG1 . ILE A 1 309 ? 20.185 0.375   -13.618 1.00 20.09  ? 365 ILE B CG1 1 
ATOM   2302 C CG2 . ILE A 1 309 ? 20.291 2.815   -13.935 1.00 2.00   ? 365 ILE B CG2 1 
ATOM   2303 C CD1 . ILE A 1 309 ? 18.842 0.278   -14.284 1.00 22.87  ? 365 ILE B CD1 1 
ATOM   2304 N N   . ASP A 1 310 ? 22.961 0.407   -10.584 1.00 13.99  ? 366 ASP B N   1 
ATOM   2305 C CA  . ASP A 1 310 ? 23.117 -0.427  -9.389  1.00 14.78  ? 366 ASP B CA  1 
ATOM   2306 C C   . ASP A 1 310 ? 23.072 0.360   -8.087  1.00 9.49   ? 366 ASP B C   1 
ATOM   2307 O O   . ASP A 1 310 ? 23.215 1.575   -8.095  1.00 4.45   ? 366 ASP B O   1 
ATOM   2308 C CB  . ASP A 1 310 ? 24.442 -1.174  -9.447  1.00 15.50  ? 366 ASP B CB  1 
ATOM   2309 C CG  . ASP A 1 310 ? 25.618 -0.241  -9.428  1.00 22.78  ? 366 ASP B CG  1 
ATOM   2310 O OD1 . ASP A 1 310 ? 25.970 0.274   -10.518 1.00 18.71  ? 366 ASP B OD1 1 
ATOM   2311 O OD2 . ASP A 1 310 ? 26.171 -0.012  -8.324  1.00 24.58  ? 366 ASP B OD2 1 
ATOM   2312 N N   . ASN A 1 311 ? 22.849 -0.356  -6.982  1.00 2.00   ? 367 ASN B N   1 
ATOM   2313 C CA  . ASN A 1 311 ? 22.765 0.219   -5.639  1.00 2.00   ? 367 ASN B CA  1 
ATOM   2314 C C   . ASN A 1 311 ? 21.728 1.322   -5.506  1.00 9.39   ? 367 ASN B C   1 
ATOM   2315 O O   . ASN A 1 311 ? 22.047 2.498   -5.315  1.00 2.00   ? 367 ASN B O   1 
ATOM   2316 C CB  . ASN A 1 311 ? 24.134 0.632   -5.103  1.00 2.00   ? 367 ASN B CB  1 
ATOM   2317 C CG  . ASN A 1 311 ? 24.914 -0.556  -4.561  1.00 15.23  ? 367 ASN B CG  1 
ATOM   2318 O OD1 . ASN A 1 311 ? 24.722 -0.974  -3.418  1.00 20.38  ? 367 ASN B OD1 1 
ATOM   2319 N ND2 . ASN A 1 311 ? 25.774 -1.129  -5.394  1.00 5.03   ? 367 ASN B ND2 1 
ATOM   2320 N N   . ASN A 1 312 ? 20.475 0.896   -5.612  1.00 7.81   ? 368 ASN B N   1 
ATOM   2321 C CA  . ASN A 1 312 ? 19.317 1.770   -5.561  1.00 3.74   ? 368 ASN B CA  1 
ATOM   2322 C C   . ASN A 1 312 ? 18.107 0.985   -5.041  1.00 9.80   ? 368 ASN B C   1 
ATOM   2323 O O   . ASN A 1 312 ? 18.239 -0.132  -4.531  1.00 12.23  ? 368 ASN B O   1 
ATOM   2324 C CB  . ASN A 1 312 ? 19.010 2.349   -6.947  1.00 2.00   ? 368 ASN B CB  1 
ATOM   2325 C CG  . ASN A 1 312 ? 19.872 3.552   -7.295  1.00 13.09  ? 368 ASN B CG  1 
ATOM   2326 O OD1 . ASN A 1 312 ? 19.548 4.676   -6.931  1.00 13.22  ? 368 ASN B OD1 1 
ATOM   2327 N ND2 . ASN A 1 312 ? 20.955 3.325   -8.040  1.00 6.87   ? 368 ASN B ND2 1 
ATOM   2328 N N   . LEU A 1 313 ? 16.943 1.617   -5.123  1.00 4.26   ? 369 LEU B N   1 
ATOM   2329 C CA  . LEU A 1 313 ? 15.661 1.010   -4.804  1.00 2.00   ? 369 LEU B CA  1 
ATOM   2330 C C   . LEU A 1 313 ? 14.800 0.547   -5.998  1.00 11.59  ? 369 LEU B C   1 
ATOM   2331 O O   . LEU A 1 313 ? 13.621 0.249   -5.818  1.00 12.51  ? 369 LEU B O   1 
ATOM   2332 C CB  . LEU A 1 313 ? 14.867 1.920   -3.858  1.00 29.96  ? 369 LEU B CB  1 
ATOM   2333 C CG  . LEU A 1 313 ? 15.579 2.402   -2.578  1.00 22.62  ? 369 LEU B CG  1 
ATOM   2334 C CD1 . LEU A 1 313 ? 14.720 3.422   -1.886  1.00 2.00   ? 369 LEU B CD1 1 
ATOM   2335 C CD2 . LEU A 1 313 ? 15.923 1.269   -1.637  1.00 2.00   ? 369 LEU B CD2 1 
ATOM   2336 N N   . ILE A 1 314 ? 15.343 0.565   -7.213  1.00 11.05  ? 370 ILE B N   1 
ATOM   2337 C CA  . ILE A 1 314 ? 14.556 0.272   -8.416  1.00 8.09   ? 370 ILE B CA  1 
ATOM   2338 C C   . ILE A 1 314 ? 13.782 -1.029  -8.242  1.00 9.09   ? 370 ILE B C   1 
ATOM   2339 O O   . ILE A 1 314 ? 14.327 -2.006  -7.725  1.00 4.19   ? 370 ILE B O   1 
ATOM   2340 C CB  . ILE A 1 314 ? 15.443 0.094   -9.687  1.00 30.30  ? 370 ILE B CB  1 
ATOM   2341 C CG1 . ILE A 1 314 ? 16.472 1.210   -9.828  1.00 2.00   ? 370 ILE B CG1 1 
ATOM   2342 C CG2 . ILE A 1 314 ? 14.579 -0.001  -10.940 1.00 2.00   ? 370 ILE B CG2 1 
ATOM   2343 C CD1 . ILE A 1 314 ? 15.884 2.565   -9.678  1.00 2.34   ? 370 ILE B CD1 1 
ATOM   2344 N N   . THR A 1 315 ? 12.515 -1.035  -8.661  1.00 6.14   ? 371 THR B N   1 
ATOM   2345 C CA  . THR A 1 315 ? 11.718 -2.256  -8.631  1.00 2.00   ? 371 THR B CA  1 
ATOM   2346 C C   . THR A 1 315 ? 11.254 -2.653  -10.012 1.00 4.30   ? 371 THR B C   1 
ATOM   2347 O O   . THR A 1 315 ? 11.532 -1.968  -10.978 1.00 18.35  ? 371 THR B O   1 
ATOM   2348 C CB  . THR A 1 315 ? 10.500 -2.154  -7.673  1.00 16.97  ? 371 THR B CB  1 
ATOM   2349 O OG1 . THR A 1 315 ? 9.633  -1.095  -8.094  1.00 19.91  ? 371 THR B OG1 1 
ATOM   2350 C CG2 . THR A 1 315 ? 10.961 -1.879  -6.261  1.00 2.00   ? 371 THR B CG2 1 
ATOM   2351 N N   . GLY A 1 316 ? 10.542 -3.766  -10.104 1.00 2.00   ? 372 GLY B N   1 
ATOM   2352 C CA  . GLY A 1 316 ? 9.955  -4.167  -11.364 1.00 2.00   ? 372 GLY B CA  1 
ATOM   2353 C C   . GLY A 1 316 ? 10.722 -5.259  -12.065 1.00 24.11  ? 372 GLY B C   1 
ATOM   2354 O O   . GLY A 1 316 ? 11.558 -5.929  -11.465 1.00 24.80  ? 372 GLY B O   1 
ATOM   2355 N N   . GLU A 1 317 ? 10.409 -5.444  -13.345 1.00 24.78  ? 373 GLU B N   1 
ATOM   2356 C CA  . GLU A 1 317 ? 11.096 -6.404  -14.197 1.00 18.46  ? 373 GLU B CA  1 
ATOM   2357 C C   . GLU A 1 317 ? 12.042 -5.651  -15.113 1.00 11.13  ? 373 GLU B C   1 
ATOM   2358 O O   . GLU A 1 317 ? 11.829 -4.473  -15.410 1.00 4.33   ? 373 GLU B O   1 
ATOM   2359 C CB  . GLU A 1 317 ? 10.108 -7.208  -15.040 1.00 12.90  ? 373 GLU B CB  1 
ATOM   2360 C CG  . GLU A 1 317 ? 8.943  -7.761  -14.268 1.00 16.38  ? 373 GLU B CG  1 
ATOM   2361 C CD  . GLU A 1 317 ? 8.341  -8.982  -14.917 1.00 26.33  ? 373 GLU B CD  1 
ATOM   2362 O OE1 . GLU A 1 317 ? 7.144  -9.253  -14.681 1.00 33.38  ? 373 GLU B OE1 1 
ATOM   2363 O OE2 . GLU A 1 317 ? 9.071  -9.681  -15.648 1.00 29.82  ? 373 GLU B OE2 1 
ATOM   2364 N N   . ILE A 1 318 ? 13.122 -6.316  -15.505 1.00 8.88   ? 374 ILE B N   1 
ATOM   2365 C CA  . ILE A 1 318 ? 14.011 -5.778  -16.518 1.00 3.98   ? 374 ILE B CA  1 
ATOM   2366 C C   . ILE A 1 318 ? 13.190 -5.668  -17.793 1.00 8.68   ? 374 ILE B C   1 
ATOM   2367 O O   . ILE A 1 318 ? 12.538 -6.633  -18.193 1.00 18.65  ? 374 ILE B O   1 
ATOM   2368 C CB  . ILE A 1 318 ? 15.229 -6.705  -16.693 1.00 7.00   ? 374 ILE B CB  1 
ATOM   2369 C CG1 . ILE A 1 318 ? 16.088 -6.682  -15.418 1.00 2.26   ? 374 ILE B CG1 1 
ATOM   2370 C CG2 . ILE A 1 318 ? 16.056 -6.296  -17.889 1.00 2.00   ? 374 ILE B CG2 1 
ATOM   2371 C CD1 . ILE A 1 318 ? 16.942 -7.922  -15.200 1.00 2.00   ? 374 ILE B CD1 1 
ATOM   2372 N N   . PRO A 1 319 ? 13.173 -4.478  -18.412 1.00 8.50   ? 375 PRO B N   1 
ATOM   2373 C CA  . PRO A 1 319 ? 12.402 -4.282  -19.652 1.00 11.90  ? 375 PRO B CA  1 
ATOM   2374 C C   . PRO A 1 319 ? 12.893 -5.211  -20.763 1.00 19.93  ? 375 PRO B C   1 
ATOM   2375 O O   . PRO A 1 319 ? 14.099 -5.308  -20.998 1.00 18.51  ? 375 PRO B O   1 
ATOM   2376 C CB  . PRO A 1 319 ? 12.683 -2.823  -20.028 1.00 4.73   ? 375 PRO B CB  1 
ATOM   2377 C CG  . PRO A 1 319 ? 13.204 -2.179  -18.758 1.00 9.36   ? 375 PRO B CG  1 
ATOM   2378 C CD  . PRO A 1 319 ? 13.932 -3.276  -18.030 1.00 8.55   ? 375 PRO B CD  1 
ATOM   2379 N N   . SER A 1 320 ? 11.965 -5.894  -21.428 1.00 24.93  ? 376 SER B N   1 
ATOM   2380 C CA  . SER A 1 320 ? 12.306 -6.837  -22.489 1.00 14.86  ? 376 SER B CA  1 
ATOM   2381 C C   . SER A 1 320 ? 12.818 -6.118  -23.725 1.00 7.41   ? 376 SER B C   1 
ATOM   2382 O O   . SER A 1 320 ? 13.623 -6.663  -24.472 1.00 13.63  ? 376 SER B O   1 
ATOM   2383 C CB  . SER A 1 320 ? 11.089 -7.665  -22.840 1.00 22.26  ? 376 SER B CB  1 
ATOM   2384 O OG  . SER A 1 320 ? 9.924  -6.888  -22.609 1.00 38.98  ? 376 SER B OG  1 
ATOM   2385 N N   . LEU A 1 321 ? 12.399 -4.874  -23.918 1.00 4.28   ? 377 LEU B N   1 
ATOM   2386 C CA  . LEU A 1 321 ? 12.850 -4.098  -25.077 1.00 9.65   ? 377 LEU B CA  1 
ATOM   2387 C C   . LEU A 1 321 ? 14.327 -3.727  -25.007 1.00 15.88  ? 377 LEU B C   1 
ATOM   2388 O O   . LEU A 1 321 ? 14.865 -3.108  -25.926 1.00 21.81  ? 377 LEU B O   1 
ATOM   2389 C CB  . LEU A 1 321 ? 11.978 -2.861  -25.316 1.00 15.89  ? 377 LEU B CB  1 
ATOM   2390 C CG  . LEU A 1 321 ? 10.730 -3.184  -26.147 1.00 21.45  ? 377 LEU B CG  1 
ATOM   2391 C CD1 . LEU A 1 321 ? 9.970  -1.941  -26.539 1.00 2.00   ? 377 LEU B CD1 1 
ATOM   2392 C CD2 . LEU A 1 321 ? 11.139 -3.961  -27.367 1.00 2.00   ? 377 LEU B CD2 1 
ATOM   2393 N N   . MET A 1 322 ? 14.974 -4.126  -23.915 1.00 14.30  ? 378 MET B N   1 
ATOM   2394 C CA  . MET A 1 322 ? 16.403 -3.914  -23.682 1.00 18.82  ? 378 MET B CA  1 
ATOM   2395 C C   . MET A 1 322 ? 17.237 -4.392  -24.871 1.00 24.92  ? 378 MET B C   1 
ATOM   2396 O O   . MET A 1 322 ? 18.391 -3.995  -25.042 1.00 23.74  ? 378 MET B O   1 
ATOM   2397 C CB  . MET A 1 322 ? 16.818 -4.704  -22.445 1.00 25.89  ? 378 MET B CB  1 
ATOM   2398 C CG  . MET A 1 322 ? 18.004 -4.143  -21.723 1.00 36.35  ? 378 MET B CG  1 
ATOM   2399 S SD  . MET A 1 322 ? 17.558 -3.052  -20.360 1.00 18.45  ? 378 MET B SD  1 
ATOM   2400 C CE  . MET A 1 322 ? 19.211 -2.520  -19.929 1.00 31.67  ? 378 MET B CE  1 
ATOM   2401 N N   . SER A 1 323 ? 16.643 -5.280  -25.664 1.00 26.32  ? 379 SER B N   1 
ATOM   2402 C CA  . SER A 1 323 ? 17.190 -5.723  -26.935 1.00 13.55  ? 379 SER B CA  1 
ATOM   2403 C C   . SER A 1 323 ? 17.344 -4.581  -27.931 1.00 9.52   ? 379 SER B C   1 
ATOM   2404 O O   . SER A 1 323 ? 18.095 -4.690  -28.896 1.00 13.95  ? 379 SER B O   1 
ATOM   2405 C CB  . SER A 1 323 ? 16.253 -6.755  -27.539 1.00 12.05  ? 379 SER B CB  1 
ATOM   2406 O OG  . SER A 1 323 ? 14.912 -6.317  -27.427 1.00 15.44  ? 379 SER B OG  1 
ATOM   2407 N N   . ASN A 1 324 ? 16.622 -3.492  -27.717 1.00 4.58   ? 380 ASN B N   1 
ATOM   2408 C CA  . ASN A 1 324 ? 16.729 -2.352  -28.619 1.00 10.76  ? 380 ASN B CA  1 
ATOM   2409 C C   . ASN A 1 324 ? 18.055 -1.608  -28.496 1.00 19.22  ? 380 ASN B C   1 
ATOM   2410 O O   . ASN A 1 324 ? 18.371 -0.754  -29.315 1.00 26.45  ? 380 ASN B O   1 
ATOM   2411 C CB  . ASN A 1 324 ? 15.573 -1.382  -28.398 1.00 15.22  ? 380 ASN B CB  1 
ATOM   2412 C CG  . ASN A 1 324 ? 14.819 -1.087  -29.668 1.00 26.00  ? 380 ASN B CG  1 
ATOM   2413 O OD1 . ASN A 1 324 ? 14.880 0.028   -30.193 1.00 34.09  ? 380 ASN B OD1 1 
ATOM   2414 N ND2 . ASN A 1 324 ? 14.105 -2.090  -30.183 1.00 28.14  ? 380 ASN B ND2 1 
ATOM   2415 N N   . LEU A 1 325 ? 18.836 -1.910  -27.470 1.00 17.65  ? 381 LEU B N   1 
ATOM   2416 C CA  . LEU A 1 325 ? 20.093 -1.209  -27.323 1.00 12.17  ? 381 LEU B CA  1 
ATOM   2417 C C   . LEU A 1 325 ? 21.182 -2.147  -27.799 1.00 21.16  ? 381 LEU B C   1 
ATOM   2418 O O   . LEU A 1 325 ? 21.570 -3.073  -27.090 1.00 29.74  ? 381 LEU B O   1 
ATOM   2419 C CB  . LEU A 1 325 ? 20.303 -0.862  -25.859 1.00 4.54   ? 381 LEU B CB  1 
ATOM   2420 C CG  . LEU A 1 325 ? 19.167 -0.158  -25.113 1.00 4.07   ? 381 LEU B CG  1 
ATOM   2421 C CD1 . LEU A 1 325 ? 19.276 -0.454  -23.593 1.00 2.00   ? 381 LEU B CD1 1 
ATOM   2422 C CD2 . LEU A 1 325 ? 19.186 1.349   -25.402 1.00 2.00   ? 381 LEU B CD2 1 
ATOM   2423 N N   . ARG A 1 326 ? 21.696 -1.897  -28.996 1.00 20.88  ? 382 ARG B N   1 
ATOM   2424 C CA  . ARG A 1 326 ? 22.587 -2.862  -29.616 1.00 16.54  ? 382 ARG B CA  1 
ATOM   2425 C C   . ARG A 1 326 ? 24.035 -2.529  -29.348 1.00 23.75  ? 382 ARG B C   1 
ATOM   2426 O O   . ARG A 1 326 ? 24.925 -3.333  -29.600 1.00 33.33  ? 382 ARG B O   1 
ATOM   2427 C CB  . ARG A 1 326 ? 22.313 -2.954  -31.110 1.00 14.13  ? 382 ARG B CB  1 
ATOM   2428 C CG  . ARG A 1 326 ? 20.855 -3.235  -31.452 1.00 20.73  ? 382 ARG B CG  1 
ATOM   2429 C CD  . ARG A 1 326 ? 20.387 -4.594  -30.935 1.00 29.52  ? 382 ARG B CD  1 
ATOM   2430 N NE  . ARG A 1 326 ? 18.993 -4.851  -31.298 1.00 40.00  ? 382 ARG B NE  1 
ATOM   2431 C CZ  . ARG A 1 326 ? 18.582 -5.863  -32.060 1.00 46.01  ? 382 ARG B CZ  1 
ATOM   2432 N NH1 . ARG A 1 326 ? 19.457 -6.742  -32.536 1.00 45.78  ? 382 ARG B NH1 1 
ATOM   2433 N NH2 . ARG A 1 326 ? 17.292 -6.004  -32.335 1.00 43.26  ? 382 ARG B NH2 1 
ATOM   2434 N N   . SER A 1 327 ? 24.267 -1.338  -28.821 1.00 21.38  ? 383 SER B N   1 
ATOM   2435 C CA  . SER A 1 327 ? 25.619 -0.915  -28.491 1.00 18.10  ? 383 SER B CA  1 
ATOM   2436 C C   . SER A 1 327 ? 25.989 -1.069  -27.006 1.00 15.16  ? 383 SER B C   1 
ATOM   2437 O O   . SER A 1 327 ? 27.110 -0.749  -26.619 1.00 2.53   ? 383 SER B O   1 
ATOM   2438 C CB  . SER A 1 327 ? 25.847 0.518   -28.973 1.00 15.22  ? 383 SER B CB  1 
ATOM   2439 O OG  . SER A 1 327 ? 25.591 0.621   -30.368 1.00 7.79   ? 383 SER B OG  1 
ATOM   2440 N N   . LEU A 1 328 ? 25.047 -1.546  -26.190 1.00 2.11   ? 384 LEU B N   1 
ATOM   2441 C CA  . LEU A 1 328 ? 25.262 -1.735  -24.765 1.00 2.08   ? 384 LEU B CA  1 
ATOM   2442 C C   . LEU A 1 328 ? 26.425 -2.689  -24.499 1.00 18.60  ? 384 LEU B C   1 
ATOM   2443 O O   . LEU A 1 328 ? 26.490 -3.790  -25.042 1.00 17.67  ? 384 LEU B O   1 
ATOM   2444 C CB  . LEU A 1 328 ? 23.980 -2.246  -24.087 1.00 2.00   ? 384 LEU B CB  1 
ATOM   2445 C CG  . LEU A 1 328 ? 23.856 -2.262  -22.540 1.00 8.85   ? 384 LEU B CG  1 
ATOM   2446 C CD1 . LEU A 1 328 ? 23.778 -0.875  -21.947 1.00 2.00   ? 384 LEU B CD1 1 
ATOM   2447 C CD2 . LEU A 1 328 ? 22.663 -3.088  -22.072 1.00 2.00   ? 384 LEU B CD2 1 
ATOM   2448 N N   . THR A 1 329 ? 27.351 -2.246  -23.658 1.00 21.22  ? 385 THR B N   1 
ATOM   2449 C CA  . THR A 1 329 ? 28.505 -3.049  -23.263 1.00 16.65  ? 385 THR B CA  1 
ATOM   2450 C C   . THR A 1 329 ? 28.389 -3.490  -21.808 1.00 8.67   ? 385 THR B C   1 
ATOM   2451 O O   . THR A 1 329 ? 28.455 -4.675  -21.489 1.00 5.92   ? 385 THR B O   1 
ATOM   2452 C CB  . THR A 1 329 ? 29.848 -2.338  -23.536 1.00 11.51  ? 385 THR B CB  1 
ATOM   2453 O OG1 . THR A 1 329 ? 29.752 -0.952  -23.185 1.00 10.01  ? 385 THR B OG1 1 
ATOM   2454 C CG2 . THR A 1 329 ? 30.182 -2.452  -25.000 1.00 4.53   ? 385 THR B CG2 1 
ATOM   2455 N N   . MET A 1 330 ? 28.277 -2.511  -20.930 1.00 8.34   ? 386 MET B N   1 
ATOM   2456 C CA  . MET A 1 330 ? 28.166 -2.751  -19.502 1.00 12.31  ? 386 MET B CA  1 
ATOM   2457 C C   . MET A 1 330 ? 26.739 -2.482  -19.007 1.00 7.55   ? 386 MET B C   1 
ATOM   2458 O O   . MET A 1 330 ? 26.188 -1.403  -19.239 1.00 5.47   ? 386 MET B O   1 
ATOM   2459 C CB  . MET A 1 330 ? 29.161 -1.831  -18.789 1.00 19.98  ? 386 MET B CB  1 
ATOM   2460 C CG  . MET A 1 330 ? 29.158 -1.885  -17.272 1.00 18.79  ? 386 MET B CG  1 
ATOM   2461 S SD  . MET A 1 330 ? 30.450 -0.787  -16.673 1.00 37.60  ? 386 MET B SD  1 
ATOM   2462 C CE  . MET A 1 330 ? 31.837 -1.406  -17.617 1.00 20.07  ? 386 MET B CE  1 
ATOM   2463 N N   . PHE A 1 331 ? 26.142 -3.468  -18.344 1.00 8.34   ? 387 PHE B N   1 
ATOM   2464 C CA  . PHE A 1 331 ? 24.838 -3.300  -17.692 1.00 11.36  ? 387 PHE B CA  1 
ATOM   2465 C C   . PHE A 1 331 ? 24.917 -3.775  -16.224 1.00 11.71  ? 387 PHE B C   1 
ATOM   2466 O O   . PHE A 1 331 ? 25.044 -4.969  -15.972 1.00 15.01  ? 387 PHE B O   1 
ATOM   2467 C CB  . PHE A 1 331 ? 23.785 -4.091  -18.495 1.00 13.73  ? 387 PHE B CB  1 
ATOM   2468 C CG  . PHE A 1 331 ? 22.410 -4.112  -17.881 1.00 9.60   ? 387 PHE B CG  1 
ATOM   2469 C CD1 . PHE A 1 331 ? 21.877 -2.987  -17.270 1.00 5.49   ? 387 PHE B CD1 1 
ATOM   2470 C CD2 . PHE A 1 331 ? 21.631 -5.257  -17.959 1.00 4.93   ? 387 PHE B CD2 1 
ATOM   2471 C CE1 . PHE A 1 331 ? 20.599 -3.012  -16.709 1.00 2.00   ? 387 PHE B CE1 1 
ATOM   2472 C CE2 . PHE A 1 331 ? 20.361 -5.288  -17.402 1.00 5.14   ? 387 PHE B CE2 1 
ATOM   2473 C CZ  . PHE A 1 331 ? 19.843 -4.157  -16.775 1.00 2.91   ? 387 PHE B CZ  1 
ATOM   2474 N N   . PHE A 1 332 ? 24.844 -2.842  -15.267 1.00 12.00  ? 388 PHE B N   1 
ATOM   2475 C CA  . PHE A 1 332 ? 24.904 -3.169  -13.820 1.00 6.61   ? 388 PHE B CA  1 
ATOM   2476 C C   . PHE A 1 332 ? 23.632 -2.696  -13.167 1.00 5.61   ? 388 PHE B C   1 
ATOM   2477 O O   . PHE A 1 332 ? 23.374 -1.488  -13.153 1.00 5.81   ? 388 PHE B O   1 
ATOM   2478 C CB  . PHE A 1 332 ? 26.049 -2.449  -13.096 1.00 2.00   ? 388 PHE B CB  1 
ATOM   2479 C CG  . PHE A 1 332 ? 27.420 -2.887  -13.516 1.00 8.75   ? 388 PHE B CG  1 
ATOM   2480 C CD1 . PHE A 1 332 ? 27.600 -4.009  -14.320 1.00 4.11   ? 388 PHE B CD1 1 
ATOM   2481 C CD2 . PHE A 1 332 ? 28.532 -2.170  -13.110 1.00 2.27   ? 388 PHE B CD2 1 
ATOM   2482 C CE1 . PHE A 1 332 ? 28.867 -4.400  -14.713 1.00 6.93   ? 388 PHE B CE1 1 
ATOM   2483 C CE2 . PHE A 1 332 ? 29.789 -2.553  -13.481 1.00 2.62   ? 388 PHE B CE2 1 
ATOM   2484 C CZ  . PHE A 1 332 ? 29.964 -3.671  -14.289 1.00 11.03  ? 388 PHE B CZ  1 
ATOM   2485 N N   . ALA A 1 333 ? 22.790 -3.639  -12.747 1.00 5.67   ? 389 ALA B N   1 
ATOM   2486 C CA  . ALA A 1 333 ? 21.618 -3.369  -11.908 1.00 2.00   ? 389 ALA B CA  1 
ATOM   2487 C C   . ALA A 1 333 ? 21.682 -3.848  -10.427 1.00 11.00  ? 389 ALA B C   1 
ATOM   2488 O O   . ALA A 1 333 ? 20.676 -3.819  -9.706  1.00 12.53  ? 389 ALA B O   1 
ATOM   2489 C CB  . ALA A 1 333 ? 20.319 -3.809  -12.615 1.00 2.00   ? 389 ALA B CB  1 
ATOM   2490 N N   . TRP A 1 334 ? 22.833 -4.352  -9.996  1.00 9.29   ? 390 TRP B N   1 
ATOM   2491 C CA  . TRP A 1 334 ? 22.937 -4.980  -8.670  1.00 4.51   ? 390 TRP B CA  1 
ATOM   2492 C C   . TRP A 1 334 ? 22.539 -4.100  -7.483  1.00 2.63   ? 390 TRP B C   1 
ATOM   2493 O O   . TRP A 1 334 ? 22.639 -2.877  -7.543  1.00 2.00   ? 390 TRP B O   1 
ATOM   2494 C CB  . TRP A 1 334 ? 24.318 -5.624  -8.441  1.00 10.05  ? 390 TRP B CB  1 
ATOM   2495 C CG  . TRP A 1 334 ? 25.485 -4.685  -8.391  1.00 9.79   ? 390 TRP B CG  1 
ATOM   2496 C CD1 . TRP A 1 334 ? 26.090 -4.078  -9.447  1.00 13.18  ? 390 TRP B CD1 1 
ATOM   2497 C CD2 . TRP A 1 334 ? 26.224 -4.293  -7.226  1.00 10.71  ? 390 TRP B CD2 1 
ATOM   2498 N NE1 . TRP A 1 334 ? 27.135 -3.302  -9.014  1.00 18.32  ? 390 TRP B NE1 1 
ATOM   2499 C CE2 . TRP A 1 334 ? 27.243 -3.424  -7.655  1.00 14.50  ? 390 TRP B CE2 1 
ATOM   2500 C CE3 . TRP A 1 334 ? 26.109 -4.579  -5.864  1.00 8.40   ? 390 TRP B CE3 1 
ATOM   2501 C CZ2 . TRP A 1 334 ? 28.144 -2.842  -6.769  1.00 17.27  ? 390 TRP B CZ2 1 
ATOM   2502 C CZ3 . TRP A 1 334 ? 27.004 -4.003  -4.994  1.00 5.86   ? 390 TRP B CZ3 1 
ATOM   2503 C CH2 . TRP A 1 334 ? 28.008 -3.145  -5.449  1.00 2.17   ? 390 TRP B CH2 1 
ATOM   2504 N N   . GLN A 1 335 ? 22.060 -4.750  -6.420  1.00 3.69   ? 391 GLN B N   1 
ATOM   2505 C CA  . GLN A 1 335 ? 21.534 -4.067  -5.235  1.00 2.77   ? 391 GLN B CA  1 
ATOM   2506 C C   . GLN A 1 335 ? 20.375 -3.144  -5.637  1.00 7.25   ? 391 GLN B C   1 
ATOM   2507 O O   . GLN A 1 335 ? 20.468 -1.910  -5.614  1.00 3.80   ? 391 GLN B O   1 
ATOM   2508 C CB  . GLN A 1 335 ? 22.637 -3.327  -4.446  1.00 2.54   ? 391 GLN B CB  1 
ATOM   2509 C CG  . GLN A 1 335 ? 22.347 -3.102  -2.962  1.00 2.00   ? 391 GLN B CG  1 
ATOM   2510 C CD  . GLN A 1 335 ? 22.184 -4.403  -2.169  1.00 8.90   ? 391 GLN B CD  1 
ATOM   2511 O OE1 . GLN A 1 335 ? 21.082 -4.924  -2.058  1.00 5.88   ? 391 GLN B OE1 1 
ATOM   2512 N NE2 . GLN A 1 335 ? 23.281 -4.921  -1.610  1.00 2.00   ? 391 GLN B NE2 1 
ATOM   2513 N N   . ASN A 1 336 ? 19.295 -3.785  -6.053  1.00 2.00   ? 392 ASN B N   1 
ATOM   2514 C CA  . ASN A 1 336 ? 18.013 -3.144  -6.222  1.00 7.39   ? 392 ASN B CA  1 
ATOM   2515 C C   . ASN A 1 336 ? 16.984 -4.146  -5.748  1.00 12.18  ? 392 ASN B C   1 
ATOM   2516 O O   . ASN A 1 336 ? 17.331 -5.129  -5.099  1.00 16.46  ? 392 ASN B O   1 
ATOM   2517 C CB  . ASN A 1 336 ? 17.762 -2.780  -7.675  1.00 7.60   ? 392 ASN B CB  1 
ATOM   2518 C CG  . ASN A 1 336 ? 18.557 -1.586  -8.110  1.00 11.61  ? 392 ASN B CG  1 
ATOM   2519 O OD1 . ASN A 1 336 ? 18.269 -0.471  -7.696  1.00 12.95  ? 392 ASN B OD1 1 
ATOM   2520 N ND2 . ASN A 1 336 ? 19.563 -1.806  -8.953  1.00 13.74  ? 392 ASN B ND2 1 
ATOM   2521 N N   . LYS A 1 337 ? 15.712 -3.877  -5.992  1.00 12.63  ? 393 LYS B N   1 
ATOM   2522 C CA  . LYS A 1 337 ? 14.729 -4.916  -5.815  1.00 16.65  ? 393 LYS B CA  1 
ATOM   2523 C C   . LYS A 1 337 ? 14.066 -5.195  -7.161  1.00 15.79  ? 393 LYS B C   1 
ATOM   2524 O O   . LYS A 1 337 ? 13.045 -4.605  -7.463  1.00 16.60  ? 393 LYS B O   1 
ATOM   2525 C CB  . LYS A 1 337 ? 13.707 -4.387  -4.814  1.00 18.89  ? 393 LYS B CB  1 
ATOM   2526 C CG  . LYS A 1 337 ? 14.373 -3.902  -3.525  1.00 16.70  ? 393 LYS B CG  1 
ATOM   2527 C CD  . LYS A 1 337 ? 13.711 -2.687  -2.919  1.00 19.79  ? 393 LYS B CD  1 
ATOM   2528 C CE  . LYS A 1 337 ? 12.209 -2.879  -2.804  1.00 41.23  ? 393 LYS B CE  1 
ATOM   2529 N NZ  . LYS A 1 337 ? 11.797 -4.235  -2.298  1.00 52.25  ? 393 LYS B NZ  1 
ATOM   2530 N N   . LEU A 1 338 ? 14.554 -6.195  -7.893  1.00 17.42  ? 394 LEU B N   1 
ATOM   2531 C CA  . LEU A 1 338 ? 14.103 -6.451  -9.261  1.00 2.00   ? 394 LEU B CA  1 
ATOM   2532 C C   . LEU A 1 338 ? 13.429 -7.811  -9.276  1.00 5.27   ? 394 LEU B C   1 
ATOM   2533 O O   . LEU A 1 338 ? 13.939 -8.768  -8.697  1.00 13.92  ? 394 LEU B O   1 
ATOM   2534 C CB  . LEU A 1 338 ? 15.275 -6.463  -10.240 1.00 2.00   ? 394 LEU B CB  1 
ATOM   2535 C CG  . LEU A 1 338 ? 15.912 -5.175  -10.763 1.00 3.41   ? 394 LEU B CG  1 
ATOM   2536 C CD1 . LEU A 1 338 ? 16.879 -5.444  -11.924 1.00 2.00   ? 394 LEU B CD1 1 
ATOM   2537 C CD2 . LEU A 1 338 ? 14.848 -4.191  -11.188 1.00 2.00   ? 394 LEU B CD2 1 
ATOM   2538 N N   . THR A 1 339 ? 12.283 -7.911  -9.932  1.00 6.14   ? 395 THR B N   1 
ATOM   2539 C CA  . THR A 1 339 ? 11.561 -9.173  -9.943  1.00 12.59  ? 395 THR B CA  1 
ATOM   2540 C C   . THR A 1 339 ? 11.463 -9.732  -11.358 1.00 13.59  ? 395 THR B C   1 
ATOM   2541 O O   . THR A 1 339 ? 11.942 -9.099  -12.301 1.00 16.60  ? 395 THR B O   1 
ATOM   2542 C CB  . THR A 1 339 ? 10.166 -9.025  -9.301  1.00 15.49  ? 395 THR B CB  1 
ATOM   2543 O OG1 . THR A 1 339 ? 9.625  -7.731  -9.608  1.00 21.29  ? 395 THR B OG1 1 
ATOM   2544 C CG2 . THR A 1 339 ? 10.274 -9.153  -7.797  1.00 13.06  ? 395 THR B CG2 1 
ATOM   2545 N N   . GLY A 1 340 ? 10.858 -10.917 -11.491 1.00 5.68   ? 396 GLY B N   1 
ATOM   2546 C CA  . GLY A 1 340 ? 10.655 -11.562 -12.780 1.00 9.90   ? 396 GLY B CA  1 
ATOM   2547 C C   . GLY A 1 340 ? 11.862 -12.292 -13.344 1.00 11.15  ? 396 GLY B C   1 
ATOM   2548 O O   . GLY A 1 340 ? 12.886 -12.425 -12.678 1.00 15.43  ? 396 GLY B O   1 
ATOM   2549 N N   . ASN A 1 341 ? 11.731 -12.783 -14.571 1.00 9.93   ? 397 ASN B N   1 
ATOM   2550 C CA  . ASN A 1 341 ? 12.838 -13.418 -15.278 1.00 7.84   ? 397 ASN B CA  1 
ATOM   2551 C C   . ASN A 1 341 ? 13.850 -12.404 -15.787 1.00 9.87   ? 397 ASN B C   1 
ATOM   2552 O O   . ASN A 1 341 ? 13.507 -11.274 -16.124 1.00 9.51   ? 397 ASN B O   1 
ATOM   2553 C CB  . ASN A 1 341 ? 12.335 -14.197 -16.501 1.00 5.55   ? 397 ASN B CB  1 
ATOM   2554 C CG  . ASN A 1 341 ? 11.631 -15.485 -16.132 1.00 10.27  ? 397 ASN B CG  1 
ATOM   2555 O OD1 . ASN A 1 341 ? 12.229 -16.561 -16.163 1.00 17.81  ? 397 ASN B OD1 1 
ATOM   2556 N ND2 . ASN A 1 341 ? 10.344 -15.388 -15.804 1.00 2.63   ? 397 ASN B ND2 1 
ATOM   2557 N N   . ILE A 1 342 ? 15.107 -12.819 -15.851 1.00 12.46  ? 398 ILE B N   1 
ATOM   2558 C CA  . ILE A 1 342 ? 16.057 -12.129 -16.685 1.00 9.98   ? 398 ILE B CA  1 
ATOM   2559 C C   . ILE A 1 342 ? 15.537 -12.415 -18.074 1.00 21.84  ? 398 ILE B C   1 
ATOM   2560 O O   . ILE A 1 342 ? 15.518 -13.577 -18.502 1.00 28.14  ? 398 ILE B O   1 
ATOM   2561 C CB  . ILE A 1 342 ? 17.459 -12.728 -16.504 1.00 10.71  ? 398 ILE B CB  1 
ATOM   2562 C CG1 . ILE A 1 342 ? 18.033 -12.305 -15.140 1.00 9.71   ? 398 ILE B CG1 1 
ATOM   2563 C CG2 . ILE A 1 342 ? 18.381 -12.303 -17.648 1.00 12.11  ? 398 ILE B CG2 1 
ATOM   2564 C CD1 . ILE A 1 342 ? 18.997 -13.299 -14.520 1.00 7.50   ? 398 ILE B CD1 1 
ATOM   2565 N N   . PRO A 1 343 ? 15.084 -11.368 -18.779 1.00 21.34  ? 399 PRO B N   1 
ATOM   2566 C CA  . PRO A 1 343 ? 14.488 -11.489 -20.117 1.00 19.47  ? 399 PRO B CA  1 
ATOM   2567 C C   . PRO A 1 343 ? 15.459 -12.094 -21.113 1.00 23.36  ? 399 PRO B C   1 
ATOM   2568 O O   . PRO A 1 343 ? 16.600 -11.651 -21.161 1.00 2.00   ? 399 PRO B O   1 
ATOM   2569 C CB  . PRO A 1 343 ? 14.209 -10.037 -20.509 1.00 2.00   ? 399 PRO B CB  1 
ATOM   2570 C CG  . PRO A 1 343 ? 15.144 -9.240  -19.704 1.00 24.86  ? 399 PRO B CG  1 
ATOM   2571 C CD  . PRO A 1 343 ? 15.254 -9.962  -18.387 1.00 22.05  ? 399 PRO B CD  1 
ATOM   2572 N N   . GLN A 1 344 ? 15.009 -13.080 -21.892 1.00 26.98  ? 400 GLN B N   1 
ATOM   2573 C CA  . GLN A 1 344 ? 15.852 -13.729 -22.902 1.00 17.11  ? 400 GLN B CA  1 
ATOM   2574 C C   . GLN A 1 344 ? 16.436 -12.703 -23.876 1.00 10.33  ? 400 GLN B C   1 
ATOM   2575 O O   . GLN A 1 344 ? 17.613 -12.775 -24.243 1.00 7.76   ? 400 GLN B O   1 
ATOM   2576 C CB  . GLN A 1 344 ? 15.069 -14.827 -23.649 1.00 21.46  ? 400 GLN B CB  1 
ATOM   2577 C CG  . GLN A 1 344 ? 14.225 -14.376 -24.854 1.00 34.29  ? 400 GLN B CG  1 
ATOM   2578 C CD  . GLN A 1 344 ? 14.982 -14.459 -26.185 1.00 49.24  ? 400 GLN B CD  1 
ATOM   2579 O OE1 . GLN A 1 344 ? 15.866 -15.302 -26.356 1.00 57.75  ? 400 GLN B OE1 1 
ATOM   2580 N NE2 . GLN A 1 344 ? 14.637 -13.581 -27.126 1.00 48.17  ? 400 GLN B NE2 1 
ATOM   2581 N N   . SER A 1 345 ? 15.618 -11.713 -24.233 1.00 9.39   ? 401 SER B N   1 
ATOM   2582 C CA  . SER A 1 345 ? 15.944 -10.736 -25.249 1.00 2.00   ? 401 SER B CA  1 
ATOM   2583 C C   . SER A 1 345 ? 17.131 -9.859  -24.891 1.00 15.00  ? 401 SER B C   1 
ATOM   2584 O O   . SER A 1 345 ? 17.563 -9.041  -25.699 1.00 21.99  ? 401 SER B O   1 
ATOM   2585 C CB  . SER A 1 345 ? 14.747 -9.839  -25.484 1.00 13.14  ? 401 SER B CB  1 
ATOM   2586 O OG  . SER A 1 345 ? 14.634 -8.910  -24.426 1.00 20.21  ? 401 SER B OG  1 
ATOM   2587 N N   . LEU A 1 346 ? 17.637 -9.989  -23.672 1.00 10.07  ? 402 LEU B N   1 
ATOM   2588 C CA  . LEU A 1 346 ? 18.859 -9.291  -23.297 1.00 9.48   ? 402 LEU B CA  1 
ATOM   2589 C C   . LEU A 1 346 ? 20.063 -9.805  -24.096 1.00 8.14   ? 402 LEU B C   1 
ATOM   2590 O O   . LEU A 1 346 ? 21.030 -9.074  -24.320 1.00 10.82  ? 402 LEU B O   1 
ATOM   2591 C CB  . LEU A 1 346 ? 19.121 -9.404  -21.798 1.00 12.60  ? 402 LEU B CB  1 
ATOM   2592 C CG  . LEU A 1 346 ? 20.301 -8.542  -21.353 1.00 9.98   ? 402 LEU B CG  1 
ATOM   2593 C CD1 . LEU A 1 346 ? 19.884 -7.099  -21.373 1.00 8.08   ? 402 LEU B CD1 1 
ATOM   2594 C CD2 . LEU A 1 346 ? 20.810 -8.949  -19.990 1.00 6.10   ? 402 LEU B CD2 1 
ATOM   2595 N N   . SER A 1 347 ? 19.988 -11.047 -24.559 1.00 10.18  ? 403 SER B N   1 
ATOM   2596 C CA  . SER A 1 347 ? 21.058 -11.632 -25.371 1.00 16.72  ? 403 SER B CA  1 
ATOM   2597 C C   . SER A 1 347 ? 21.150 -11.060 -26.795 1.00 19.09  ? 403 SER B C   1 
ATOM   2598 O O   . SER A 1 347 ? 22.065 -11.398 -27.564 1.00 9.53   ? 403 SER B O   1 
ATOM   2599 C CB  . SER A 1 347 ? 20.861 -13.129 -25.476 1.00 15.00  ? 403 SER B CB  1 
ATOM   2600 O OG  . SER A 1 347 ? 19.719 -13.390 -26.266 1.00 15.89  ? 403 SER B OG  1 
ATOM   2601 N N   . GLN A 1 348 ? 20.201 -10.210 -27.167 1.00 20.78  ? 404 GLN B N   1 
ATOM   2602 C CA  . GLN A 1 348 ? 20.313 -9.538  -28.447 1.00 2.57   ? 404 GLN B CA  1 
ATOM   2603 C C   . GLN A 1 348 ? 21.212 -8.314  -28.370 1.00 15.83  ? 404 GLN B C   1 
ATOM   2604 O O   . GLN A 1 348 ? 21.411 -7.625  -29.361 1.00 20.19  ? 404 GLN B O   1 
ATOM   2605 C CB  . GLN A 1 348 ? 18.947 -9.159  -28.994 1.00 2.31   ? 404 GLN B CB  1 
ATOM   2606 C CG  . GLN A 1 348 ? 17.999 -10.330 -29.128 1.00 19.76  ? 404 GLN B CG  1 
ATOM   2607 C CD  . GLN A 1 348 ? 16.716 -9.934  -29.811 1.00 16.10  ? 404 GLN B CD  1 
ATOM   2608 O OE1 . GLN A 1 348 ? 16.698 -9.026  -30.642 1.00 17.48  ? 404 GLN B OE1 1 
ATOM   2609 N NE2 . GLN A 1 348 ? 15.627 -10.597 -29.449 1.00 15.63  ? 404 GLN B NE2 1 
ATOM   2610 N N   . CYS A 1 349 ? 21.757 -8.016  -27.200 1.00 18.67  ? 405 CYS B N   1 
ATOM   2611 C CA  . CYS A 1 349 ? 22.748 -6.955  -27.166 1.00 20.13  ? 405 CYS B CA  1 
ATOM   2612 C C   . CYS A 1 349 ? 24.056 -7.698  -27.356 1.00 31.70  ? 405 CYS B C   1 
ATOM   2613 O O   . CYS A 1 349 ? 24.600 -8.289  -26.413 1.00 31.04  ? 405 CYS B O   1 
ATOM   2614 C CB  . CYS A 1 349 ? 22.728 -6.245  -25.813 1.00 9.89   ? 405 CYS B CB  1 
ATOM   2615 S SG  . CYS A 1 349 ? 21.103 -5.622  -25.273 1.00 10.53  ? 405 CYS B SG  1 
ATOM   2616 N N   . ARG A 1 350 ? 24.596 -7.617  -28.568 1.00 25.56  ? 406 ARG B N   1 
ATOM   2617 C CA  . ARG A 1 350 ? 25.651 -8.541  -28.952 1.00 19.39  ? 406 ARG B CA  1 
ATOM   2618 C C   . ARG A 1 350 ? 26.990 -8.029  -28.471 1.00 3.72   ? 406 ARG B C   1 
ATOM   2619 O O   . ARG A 1 350 ? 27.962 -8.766  -28.459 1.00 10.50  ? 406 ARG B O   1 
ATOM   2620 C CB  . ARG A 1 350 ? 25.665 -8.780  -30.468 1.00 17.68  ? 406 ARG B CB  1 
ATOM   2621 C CG  . ARG A 1 350 ? 24.375 -9.356  -31.081 1.00 10.71  ? 406 ARG B CG  1 
ATOM   2622 C CD  . ARG A 1 350 ? 23.942 -10.671 -30.450 1.00 16.33  ? 406 ARG B CD  1 
ATOM   2623 N NE  . ARG A 1 350 ? 24.924 -11.744 -30.579 1.00 21.27  ? 406 ARG B NE  1 
ATOM   2624 C CZ  . ARG A 1 350 ? 24.886 -12.871 -29.870 1.00 17.82  ? 406 ARG B CZ  1 
ATOM   2625 N NH1 . ARG A 1 350 ? 23.912 -13.063 -28.985 1.00 7.15   ? 406 ARG B NH1 1 
ATOM   2626 N NH2 . ARG A 1 350 ? 25.816 -13.806 -30.041 1.00 18.10  ? 406 ARG B NH2 1 
ATOM   2627 N N   . GLU A 1 351 ? 27.023 -6.766  -28.056 1.00 3.49   ? 407 GLU B N   1 
ATOM   2628 C CA  . GLU A 1 351 ? 28.252 -6.147  -27.586 1.00 6.48   ? 407 GLU B CA  1 
ATOM   2629 C C   . GLU A 1 351 ? 28.457 -6.203  -26.060 1.00 6.38   ? 407 GLU B C   1 
ATOM   2630 O O   . GLU A 1 351 ? 29.420 -5.628  -25.556 1.00 8.34   ? 407 GLU B O   1 
ATOM   2631 C CB  . GLU A 1 351 ? 28.289 -4.690  -28.041 1.00 20.49  ? 407 GLU B CB  1 
ATOM   2632 C CG  . GLU A 1 351 ? 28.347 -4.513  -29.541 1.00 32.54  ? 407 GLU B CG  1 
ATOM   2633 C CD  . GLU A 1 351 ? 29.566 -5.169  -30.148 1.00 39.14  ? 407 GLU B CD  1 
ATOM   2634 O OE1 . GLU A 1 351 ? 29.377 -6.017  -31.040 1.00 40.83  ? 407 GLU B OE1 1 
ATOM   2635 O OE2 . GLU A 1 351 ? 30.704 -4.839  -29.733 1.00 40.61  ? 407 GLU B OE2 1 
ATOM   2636 N N   . LEU A 1 352 ? 27.545 -6.847  -25.324 1.00 5.54   ? 408 LEU B N   1 
ATOM   2637 C CA  . LEU A 1 352 ? 27.669 -6.904  -23.879 1.00 8.28   ? 408 LEU B CA  1 
ATOM   2638 C C   . LEU A 1 352 ? 28.970 -7.570  -23.455 1.00 25.35  ? 408 LEU B C   1 
ATOM   2639 O O   . LEU A 1 352 ? 29.222 -8.731  -23.784 1.00 29.21  ? 408 LEU B O   1 
ATOM   2640 C CB  . LEU A 1 352 ? 26.497 -7.675  -23.270 1.00 3.06   ? 408 LEU B CB  1 
ATOM   2641 C CG  . LEU A 1 352 ? 25.215 -6.875  -23.004 1.00 9.12   ? 408 LEU B CG  1 
ATOM   2642 C CD1 . LEU A 1 352 ? 24.122 -7.804  -22.524 1.00 2.50   ? 408 LEU B CD1 1 
ATOM   2643 C CD2 . LEU A 1 352 ? 25.439 -5.740  -22.001 1.00 2.45   ? 408 LEU B CD2 1 
ATOM   2644 N N   . GLN A 1 353 ? 29.801 -6.812  -22.739 1.00 26.66  ? 409 GLN B N   1 
ATOM   2645 C CA  . GLN A 1 353 ? 30.976 -7.349  -22.062 1.00 22.84  ? 409 GLN B CA  1 
ATOM   2646 C C   . GLN A 1 353 ? 30.684 -7.840  -20.650 1.00 15.63  ? 409 GLN B C   1 
ATOM   2647 O O   . GLN A 1 353 ? 31.198 -8.868  -20.219 1.00 18.81  ? 409 GLN B O   1 
ATOM   2648 C CB  . GLN A 1 353 ? 32.120 -6.346  -22.086 1.00 4.21   ? 409 GLN B CB  1 
ATOM   2649 C CG  . GLN A 1 353 ? 32.440 -5.880  -23.469 1.00 4.36   ? 409 GLN B CG  1 
ATOM   2650 C CD  . GLN A 1 353 ? 33.310 -4.655  -23.484 1.00 4.46   ? 409 GLN B CD  1 
ATOM   2651 O OE1 . GLN A 1 353 ? 33.493 -3.996  -22.467 1.00 26.65  ? 409 GLN B OE1 1 
ATOM   2652 N NE2 . GLN A 1 353 ? 33.851 -4.335  -24.642 1.00 11.05  ? 409 GLN B NE2 1 
ATOM   2653 N N   . ALA A 1 354 ? 29.874 -7.077  -19.922 1.00 12.32  ? 410 ALA B N   1 
ATOM   2654 C CA  . ALA A 1 354 ? 29.631 -7.354  -18.501 1.00 12.03  ? 410 ALA B CA  1 
ATOM   2655 C C   . ALA A 1 354 ? 28.184 -7.178  -18.038 1.00 3.00   ? 410 ALA B C   1 
ATOM   2656 O O   . ALA A 1 354 ? 27.573 -6.148  -18.276 1.00 16.59  ? 410 ALA B O   1 
ATOM   2657 C CB  . ALA A 1 354 ? 30.549 -6.499  -17.652 1.00 3.48   ? 410 ALA B CB  1 
ATOM   2658 N N   . ILE A 1 355 ? 27.657 -8.182  -17.349 1.00 17.62  ? 411 ILE B N   1 
ATOM   2659 C CA  . ILE A 1 355 ? 26.360 -8.064  -16.688 1.00 10.25  ? 411 ILE B CA  1 
ATOM   2660 C C   . ILE A 1 355 ? 26.495 -8.332  -15.194 1.00 11.27  ? 411 ILE B C   1 
ATOM   2661 O O   . ILE A 1 355 ? 27.062 -9.351  -14.806 1.00 13.89  ? 411 ILE B O   1 
ATOM   2662 C CB  . ILE A 1 355 ? 25.347 -9.077  -17.258 1.00 18.15  ? 411 ILE B CB  1 
ATOM   2663 C CG1 . ILE A 1 355 ? 25.112 -8.828  -18.755 1.00 20.74  ? 411 ILE B CG1 1 
ATOM   2664 C CG2 . ILE A 1 355 ? 24.032 -9.020  -16.487 1.00 21.66  ? 411 ILE B CG2 1 
ATOM   2665 C CD1 . ILE A 1 355 ? 24.879 -10.090 -19.528 1.00 2.78   ? 411 ILE B CD1 1 
ATOM   2666 N N   . ASP A 1 356 ? 26.000 -7.419  -14.356 1.00 8.95   ? 412 ASP B N   1 
ATOM   2667 C CA  . ASP A 1 356 ? 25.845 -7.729  -12.941 1.00 11.30  ? 412 ASP B CA  1 
ATOM   2668 C C   . ASP A 1 356 ? 24.422 -7.451  -12.492 1.00 10.23  ? 412 ASP B C   1 
ATOM   2669 O O   . ASP A 1 356 ? 24.008 -6.300  -12.373 1.00 20.87  ? 412 ASP B O   1 
ATOM   2670 C CB  . ASP A 1 356 ? 26.804 -6.880  -12.106 1.00 21.85  ? 412 ASP B CB  1 
ATOM   2671 C CG  . ASP A 1 356 ? 27.023 -7.443  -10.709 1.00 17.72  ? 412 ASP B CG  1 
ATOM   2672 O OD1 . ASP A 1 356 ? 26.177 -8.227  -10.239 1.00 9.15   ? 412 ASP B OD1 1 
ATOM   2673 O OD2 . ASP A 1 356 ? 28.053 -7.113  -10.097 1.00 2.62   ? 412 ASP B OD2 1 
ATOM   2674 N N   . LEU A 1 357 ? 23.682 -8.528  -12.261 1.00 6.68   ? 413 LEU B N   1 
ATOM   2675 C CA  . LEU A 1 357 ? 22.312 -8.482  -11.748 1.00 7.45   ? 413 LEU B CA  1 
ATOM   2676 C C   . LEU A 1 357 ? 22.186 -8.885  -10.274 1.00 10.08  ? 413 LEU B C   1 
ATOM   2677 O O   . LEU A 1 357 ? 21.083 -9.147  -9.782  1.00 8.31   ? 413 LEU B O   1 
ATOM   2678 C CB  . LEU A 1 357 ? 21.351 -9.224  -12.678 1.00 8.54   ? 413 LEU B CB  1 
ATOM   2679 C CG  . LEU A 1 357 ? 21.387 -8.566  -14.071 1.00 6.35   ? 413 LEU B CG  1 
ATOM   2680 C CD1 . LEU A 1 357 ? 20.558 -9.318  -15.092 1.00 2.00   ? 413 LEU B CD1 1 
ATOM   2681 C CD2 . LEU A 1 357 ? 20.943 -7.106  -13.988 1.00 4.85   ? 413 LEU B CD2 1 
ATOM   2682 N N   . SER A 1 358 ? 23.335 -9.002  -9.609  1.00 12.00  ? 414 SER B N   1 
ATOM   2683 C CA  . SER A 1 358 ? 23.445 -9.522  -8.243  1.00 2.00   ? 414 SER B CA  1 
ATOM   2684 C C   . SER A 1 358 ? 22.610 -8.778  -7.218  1.00 19.64  ? 414 SER B C   1 
ATOM   2685 O O   . SER A 1 358 ? 22.269 -7.615  -7.413  1.00 14.24  ? 414 SER B O   1 
ATOM   2686 C CB  . SER A 1 358 ? 24.895 -9.472  -7.769  1.00 2.15   ? 414 SER B CB  1 
ATOM   2687 O OG  . SER A 1 358 ? 25.670 -10.464 -8.404  1.00 8.96   ? 414 SER B OG  1 
ATOM   2688 N N   . TYR A 1 359 ? 22.259 -9.468  -6.134  1.00 2.00   ? 415 TYR B N   1 
ATOM   2689 C CA  . TYR A 1 359 ? 21.545 -8.832  -5.038  1.00 6.24   ? 415 TYR B CA  1 
ATOM   2690 C C   . TYR A 1 359 ? 20.232 -8.232  -5.547  1.00 6.38   ? 415 TYR B C   1 
ATOM   2691 O O   . TYR A 1 359 ? 20.046 -7.016  -5.586  1.00 6.69   ? 415 TYR B O   1 
ATOM   2692 C CB  . TYR A 1 359 ? 22.429 -7.782  -4.336  1.00 2.00   ? 415 TYR B CB  1 
ATOM   2693 C CG  . TYR A 1 359 ? 23.572 -8.395  -3.563  1.00 12.11  ? 415 TYR B CG  1 
ATOM   2694 C CD1 . TYR A 1 359 ? 23.315 -9.204  -2.450  1.00 15.19  ? 415 TYR B CD1 1 
ATOM   2695 C CD2 . TYR A 1 359 ? 24.901 -8.173  -3.929  1.00 2.00   ? 415 TYR B CD2 1 
ATOM   2696 C CE1 . TYR A 1 359 ? 24.337 -9.782  -1.721  1.00 2.04   ? 415 TYR B CE1 1 
ATOM   2697 C CE2 . TYR A 1 359 ? 25.942 -8.751  -3.210  1.00 2.26   ? 415 TYR B CE2 1 
ATOM   2698 C CZ  . TYR A 1 359 ? 25.643 -9.558  -2.100  1.00 15.37  ? 415 TYR B CZ  1 
ATOM   2699 O OH  . TYR A 1 359 ? 26.629 -10.151 -1.353  1.00 10.70  ? 415 TYR B OH  1 
ATOM   2700 N N   . ASN A 1 360 ? 19.335 -9.114  -5.958  1.00 9.67   ? 416 ASN B N   1 
ATOM   2701 C CA  . ASN A 1 360 ? 18.019 -8.737  -6.413  1.00 2.00   ? 416 ASN B CA  1 
ATOM   2702 C C   . ASN A 1 360 ? 17.053 -9.883  -6.138  1.00 18.56  ? 416 ASN B C   1 
ATOM   2703 O O   . ASN A 1 360 ? 17.408 -10.870 -5.499  1.00 21.01  ? 416 ASN B O   1 
ATOM   2704 C CB  . ASN A 1 360 ? 18.061 -8.445  -7.902  1.00 2.00   ? 416 ASN B CB  1 
ATOM   2705 C CG  . ASN A 1 360 ? 18.293 -6.997  -8.198  1.00 2.00   ? 416 ASN B CG  1 
ATOM   2706 O OD1 . ASN A 1 360 ? 17.524 -6.147  -7.774  1.00 2.00   ? 416 ASN B OD1 1 
ATOM   2707 N ND2 . ASN A 1 360 ? 19.353 -6.700  -8.938  1.00 2.00   ? 416 ASN B ND2 1 
ATOM   2708 N N   . SER A 1 361 ? 15.820 -9.739  -6.596  1.00 15.78  ? 417 SER B N   1 
ATOM   2709 C CA  . SER A 1 361 ? 14.823 -10.794 -6.466  1.00 20.24  ? 417 SER B CA  1 
ATOM   2710 C C   . SER A 1 361 ? 14.563 -11.678 -7.699  1.00 25.00  ? 417 SER B C   1 
ATOM   2711 O O   . SER A 1 361 ? 13.607 -12.450 -7.686  1.00 34.69  ? 417 SER B O   1 
ATOM   2712 C CB  . SER A 1 361 ? 13.527 -10.217 -5.922  1.00 24.29  ? 417 SER B CB  1 
ATOM   2713 O OG  . SER A 1 361 ? 13.804 -9.519  -4.728  1.00 27.12  ? 417 SER B OG  1 
ATOM   2714 N N   . LEU A 1 362 ? 15.362 -11.543 -8.760  1.00 19.05  ? 418 LEU B N   1 
ATOM   2715 C CA  . LEU A 1 362 ? 15.058 -12.193 -10.051 1.00 23.53  ? 418 LEU B CA  1 
ATOM   2716 C C   . LEU A 1 362 ? 14.793 -13.687 -9.898  1.00 22.37  ? 418 LEU B C   1 
ATOM   2717 O O   . LEU A 1 362 ? 15.392 -14.349 -9.042  1.00 17.07  ? 418 LEU B O   1 
ATOM   2718 C CB  . LEU A 1 362 ? 16.166 -11.957 -11.089 1.00 2.00   ? 418 LEU B CB  1 
ATOM   2719 C CG  . LEU A 1 362 ? 16.717 -10.532 -11.167 1.00 2.00   ? 418 LEU B CG  1 
ATOM   2720 C CD1 . LEU A 1 362 ? 18.038 -10.522 -11.898 1.00 2.00   ? 418 LEU B CD1 1 
ATOM   2721 C CD2 . LEU A 1 362 ? 15.731 -9.614  -11.828 1.00 2.00   ? 418 LEU B CD2 1 
ATOM   2722 N N   . SER A 1 363 ? 13.864 -14.202 -10.701 1.00 2.00   ? 419 SER B N   1 
ATOM   2723 C CA  . SER A 1 363 ? 13.439 -15.592 -10.572 1.00 10.96  ? 419 SER B CA  1 
ATOM   2724 C C   . SER A 1 363 ? 13.560 -16.395 -11.874 1.00 14.95  ? 419 SER B C   1 
ATOM   2725 O O   . SER A 1 363 ? 14.144 -15.931 -12.856 1.00 26.20  ? 419 SER B O   1 
ATOM   2726 C CB  . SER A 1 363 ? 12.020 -15.697 -9.978  1.00 9.38   ? 419 SER B CB  1 
ATOM   2727 O OG  . SER A 1 363 ? 11.277 -14.496 -10.114 1.00 7.91   ? 419 SER B OG  1 
ATOM   2728 N N   . GLY A 1 364 ? 13.042 -17.619 -11.859 1.00 2.00   ? 420 GLY B N   1 
ATOM   2729 C CA  . GLY A 1 364 ? 13.037 -18.456 -13.042 1.00 8.05   ? 420 GLY B CA  1 
ATOM   2730 C C   . GLY A 1 364 ? 14.430 -18.912 -13.428 1.00 8.89   ? 420 GLY B C   1 
ATOM   2731 O O   . GLY A 1 364 ? 15.389 -18.760 -12.650 1.00 10.31  ? 420 GLY B O   1 
ATOM   2732 N N   . SER A 1 365 ? 14.561 -19.484 -14.620 1.00 5.45   ? 421 SER B N   1 
ATOM   2733 C CA  . SER A 1 365 ? 15.873 -19.913 -15.063 1.00 4.11   ? 421 SER B CA  1 
ATOM   2734 C C   . SER A 1 365 ? 16.668 -18.755 -15.615 1.00 9.24   ? 421 SER B C   1 
ATOM   2735 O O   . SER A 1 365 ? 16.162 -17.641 -15.743 1.00 10.81  ? 421 SER B O   1 
ATOM   2736 C CB  . SER A 1 365 ? 15.751 -20.984 -16.123 1.00 7.21   ? 421 SER B CB  1 
ATOM   2737 O OG  . SER A 1 365 ? 15.312 -22.190 -15.541 1.00 14.46  ? 421 SER B OG  1 
ATOM   2738 N N   . ILE A 1 366 ? 17.924 -19.039 -15.935 1.00 10.99  ? 422 ILE B N   1 
ATOM   2739 C CA  . ILE A 1 366 ? 18.806 -18.089 -16.573 1.00 2.78   ? 422 ILE B CA  1 
ATOM   2740 C C   . ILE A 1 366 ? 18.653 -18.486 -18.013 1.00 29.96  ? 422 ILE B C   1 
ATOM   2741 O O   . ILE A 1 366 ? 18.937 -19.640 -18.374 1.00 24.11  ? 422 ILE B O   1 
ATOM   2742 C CB  . ILE A 1 366 ? 20.279 -18.315 -16.156 1.00 8.66   ? 422 ILE B CB  1 
ATOM   2743 C CG1 . ILE A 1 366 ? 20.446 -18.262 -14.631 1.00 13.57  ? 422 ILE B CG1 1 
ATOM   2744 C CG2 . ILE A 1 366 ? 21.179 -17.285 -16.800 1.00 13.49  ? 422 ILE B CG2 1 
ATOM   2745 C CD1 . ILE A 1 366 ? 21.768 -18.822 -14.115 1.00 11.76  ? 422 ILE B CD1 1 
ATOM   2746 N N   . PRO A 1 367 ? 18.170 -17.551 -18.843 1.00 27.07  ? 423 PRO B N   1 
ATOM   2747 C CA  . PRO A 1 367 ? 17.890 -17.861 -20.247 1.00 16.18  ? 423 PRO B CA  1 
ATOM   2748 C C   . PRO A 1 367 ? 19.179 -18.338 -20.885 1.00 21.99  ? 423 PRO B C   1 
ATOM   2749 O O   . PRO A 1 367 ? 20.250 -17.890 -20.462 1.00 23.64  ? 423 PRO B O   1 
ATOM   2750 C CB  . PRO A 1 367 ? 17.449 -16.517 -20.817 1.00 10.41  ? 423 PRO B CB  1 
ATOM   2751 C CG  . PRO A 1 367 ? 18.066 -15.498 -19.919 1.00 21.79  ? 423 PRO B CG  1 
ATOM   2752 C CD  . PRO A 1 367 ? 18.042 -16.112 -18.551 1.00 27.97  ? 423 PRO B CD  1 
ATOM   2753 N N   . LYS A 1 368 ? 19.094 -19.260 -21.841 1.00 16.30  ? 424 LYS B N   1 
ATOM   2754 C CA  . LYS A 1 368 ? 20.303 -19.870 -22.383 1.00 8.47   ? 424 LYS B CA  1 
ATOM   2755 C C   . LYS A 1 368 ? 20.984 -18.932 -23.371 1.00 8.45   ? 424 LYS B C   1 
ATOM   2756 O O   . LYS A 1 368 ? 22.183 -19.013 -23.593 1.00 14.91  ? 424 LYS B O   1 
ATOM   2757 C CB  . LYS A 1 368 ? 19.992 -21.221 -23.029 1.00 12.43  ? 424 LYS B CB  1 
ATOM   2758 C CG  . LYS A 1 368 ? 19.022 -21.119 -24.182 1.00 26.57  ? 424 LYS B CG  1 
ATOM   2759 C CD  . LYS A 1 368 ? 18.880 -22.433 -24.926 1.00 32.94  ? 424 LYS B CD  1 
ATOM   2760 C CE  . LYS A 1 368 ? 17.829 -22.324 -26.017 1.00 29.72  ? 424 LYS B CE  1 
ATOM   2761 N NZ  . LYS A 1 368 ? 17.466 -23.671 -26.523 1.00 29.94  ? 424 LYS B NZ  1 
ATOM   2762 N N   . GLU A 1 369 ? 20.215 -18.020 -23.939 1.00 11.29  ? 425 GLU B N   1 
ATOM   2763 C CA  . GLU A 1 369 ? 20.709 -17.157 -25.003 1.00 15.91  ? 425 GLU B CA  1 
ATOM   2764 C C   . GLU A 1 369 ? 21.830 -16.230 -24.511 1.00 22.31  ? 425 GLU B C   1 
ATOM   2765 O O   . GLU A 1 369 ? 22.621 -15.717 -25.311 1.00 26.46  ? 425 GLU B O   1 
ATOM   2766 C CB  . GLU A 1 369 ? 19.552 -16.334 -25.589 1.00 16.79  ? 425 GLU B CB  1 
ATOM   2767 C CG  . GLU A 1 369 ? 18.452 -17.124 -26.304 1.00 20.79  ? 425 GLU B CG  1 
ATOM   2768 C CD  . GLU A 1 369 ? 17.499 -17.877 -25.373 1.00 23.84  ? 425 GLU B CD  1 
ATOM   2769 O OE1 . GLU A 1 369 ? 17.554 -17.684 -24.143 1.00 27.92  ? 425 GLU B OE1 1 
ATOM   2770 O OE2 . GLU A 1 369 ? 16.688 -18.678 -25.878 1.00 28.47  ? 425 GLU B OE2 1 
ATOM   2771 N N   . ILE A 1 370 ? 21.895 -16.019 -23.197 1.00 15.06  ? 426 ILE B N   1 
ATOM   2772 C CA  . ILE A 1 370 ? 22.888 -15.121 -22.609 1.00 14.12  ? 426 ILE B CA  1 
ATOM   2773 C C   . ILE A 1 370 ? 24.291 -15.703 -22.766 1.00 17.75  ? 426 ILE B C   1 
ATOM   2774 O O   . ILE A 1 370 ? 25.281 -14.973 -22.819 1.00 22.85  ? 426 ILE B O   1 
ATOM   2775 C CB  . ILE A 1 370 ? 22.597 -14.854 -21.105 1.00 12.21  ? 426 ILE B CB  1 
ATOM   2776 C CG1 . ILE A 1 370 ? 22.628 -13.358 -20.802 1.00 8.18   ? 426 ILE B CG1 1 
ATOM   2777 C CG2 . ILE A 1 370 ? 23.580 -15.596 -20.208 1.00 3.49   ? 426 ILE B CG2 1 
ATOM   2778 C CD1 . ILE A 1 370 ? 21.451 -12.608 -21.382 1.00 7.90   ? 426 ILE B CD1 1 
ATOM   2779 N N   . PHE A 1 371 ? 24.361 -17.027 -22.849 1.00 16.73  ? 427 PHE B N   1 
ATOM   2780 C CA  . PHE A 1 371 ? 25.628 -17.731 -22.986 1.00 21.97  ? 427 PHE B CA  1 
ATOM   2781 C C   . PHE A 1 371 ? 26.026 -17.778 -24.459 1.00 31.79  ? 427 PHE B C   1 
ATOM   2782 O O   . PHE A 1 371 ? 27.063 -18.325 -24.831 1.00 33.04  ? 427 PHE B O   1 
ATOM   2783 C CB  . PHE A 1 371 ? 25.511 -19.138 -22.393 1.00 19.44  ? 427 PHE B CB  1 
ATOM   2784 C CG  . PHE A 1 371 ? 25.300 -19.149 -20.894 1.00 24.24  ? 427 PHE B CG  1 
ATOM   2785 C CD1 . PHE A 1 371 ? 26.371 -18.946 -20.023 1.00 24.08  ? 427 PHE B CD1 1 
ATOM   2786 C CD2 . PHE A 1 371 ? 24.041 -19.356 -20.357 1.00 22.32  ? 427 PHE B CD2 1 
ATOM   2787 C CE1 . PHE A 1 371 ? 26.191 -18.949 -18.649 1.00 21.03  ? 427 PHE B CE1 1 
ATOM   2788 C CE2 . PHE A 1 371 ? 23.855 -19.365 -18.981 1.00 24.57  ? 427 PHE B CE2 1 
ATOM   2789 C CZ  . PHE A 1 371 ? 24.933 -19.163 -18.125 1.00 22.58  ? 427 PHE B CZ  1 
ATOM   2790 N N   . GLY A 1 372 ? 25.179 -17.191 -25.296 1.00 32.25  ? 428 GLY B N   1 
ATOM   2791 C CA  . GLY A 1 372 ? 25.474 -17.053 -26.703 1.00 22.67  ? 428 GLY B CA  1 
ATOM   2792 C C   . GLY A 1 372 ? 26.223 -15.763 -26.940 1.00 17.23  ? 428 GLY B C   1 
ATOM   2793 O O   . GLY A 1 372 ? 26.542 -15.415 -28.084 1.00 11.74  ? 428 GLY B O   1 
ATOM   2794 N N   . LEU A 1 373 ? 26.508 -15.048 -25.856 1.00 4.57   ? 429 LEU B N   1 
ATOM   2795 C CA  . LEU A 1 373 ? 27.197 -13.778 -25.970 1.00 4.51   ? 429 LEU B CA  1 
ATOM   2796 C C   . LEU A 1 373 ? 28.680 -14.042 -26.137 1.00 18.40  ? 429 LEU B C   1 
ATOM   2797 O O   . LEU A 1 373 ? 29.308 -14.693 -25.301 1.00 12.56  ? 429 LEU B O   1 
ATOM   2798 C CB  . LEU A 1 373 ? 26.916 -12.890 -24.764 1.00 11.94  ? 429 LEU B CB  1 
ATOM   2799 C CG  . LEU A 1 373 ? 25.493 -12.337 -24.730 1.00 10.59  ? 429 LEU B CG  1 
ATOM   2800 C CD1 . LEU A 1 373 ? 25.195 -11.656 -23.391 1.00 10.36  ? 429 LEU B CD1 1 
ATOM   2801 C CD2 . LEU A 1 373 ? 25.282 -11.379 -25.903 1.00 4.95   ? 429 LEU B CD2 1 
ATOM   2802 N N   . ARG A 1 374 ? 29.221 -13.564 -27.250 1.00 23.10  ? 430 ARG B N   1 
ATOM   2803 C CA  . ARG A 1 374 ? 30.585 -13.889 -27.643 1.00 21.14  ? 430 ARG B CA  1 
ATOM   2804 C C   . ARG A 1 374 ? 31.641 -13.000 -26.997 1.00 18.03  ? 430 ARG B C   1 
ATOM   2805 O O   . ARG A 1 374 ? 32.808 -13.370 -26.940 1.00 20.42  ? 430 ARG B O   1 
ATOM   2806 C CB  . ARG A 1 374 ? 30.711 -13.859 -29.168 1.00 23.42  ? 430 ARG B CB  1 
ATOM   2807 C CG  . ARG A 1 374 ? 29.977 -15.003 -29.868 1.00 38.40  ? 430 ARG B CG  1 
ATOM   2808 C CD  . ARG A 1 374 ? 30.268 -15.029 -31.374 1.00 51.34  ? 430 ARG B CD  1 
ATOM   2809 N NE  . ARG A 1 374 ? 31.674 -14.741 -31.648 1.00 60.16  ? 430 ARG B NE  1 
ATOM   2810 C CZ  . ARG A 1 374 ? 32.106 -13.633 -32.242 1.00 62.64  ? 430 ARG B CZ  1 
ATOM   2811 N NH1 . ARG A 1 374 ? 31.239 -12.716 -32.648 1.00 59.94  ? 430 ARG B NH1 1 
ATOM   2812 N NH2 . ARG A 1 374 ? 33.404 -13.445 -32.437 1.00 63.77  ? 430 ARG B NH2 1 
ATOM   2813 N N   . ASN A 1 375 ? 31.245 -11.806 -26.572 1.00 17.78  ? 431 ASN B N   1 
ATOM   2814 C CA  . ASN A 1 375 ? 32.166 -10.888 -25.899 1.00 20.63  ? 431 ASN B CA  1 
ATOM   2815 C C   . ASN A 1 375 ? 32.048 -10.752 -24.361 1.00 17.39  ? 431 ASN B C   1 
ATOM   2816 O O   . ASN A 1 375 ? 32.709 -9.910  -23.752 1.00 15.57  ? 431 ASN B O   1 
ATOM   2817 C CB  . ASN A 1 375 ? 32.218 -9.536  -26.619 1.00 31.44  ? 431 ASN B CB  1 
ATOM   2818 C CG  . ASN A 1 375 ? 33.565 -9.281  -27.275 1.00 39.65  ? 431 ASN B CG  1 
ATOM   2819 O OD1 . ASN A 1 375 ? 33.681 -9.204  -28.511 1.00 37.88  ? 431 ASN B OD1 1 
ATOM   2820 N ND2 . ASN A 1 375 ? 34.601 -9.148  -26.446 1.00 43.74  ? 431 ASN B ND2 1 
ATOM   2821 N N   . LEU A 1 376 ? 31.181 -11.553 -23.748 1.00 16.01  ? 432 LEU B N   1 
ATOM   2822 C CA  . LEU A 1 376 ? 30.882 -11.419 -22.331 1.00 4.65   ? 432 LEU B CA  1 
ATOM   2823 C C   . LEU A 1 376 ? 31.979 -12.063 -21.489 1.00 17.15  ? 432 LEU B C   1 
ATOM   2824 O O   . LEU A 1 376 ? 32.173 -13.277 -21.532 1.00 16.70  ? 432 LEU B O   1 
ATOM   2825 C CB  . LEU A 1 376 ? 29.544 -12.106 -22.046 1.00 4.38   ? 432 LEU B CB  1 
ATOM   2826 C CG  . LEU A 1 376 ? 28.817 -11.948 -20.707 1.00 5.07   ? 432 LEU B CG  1 
ATOM   2827 C CD1 . LEU A 1 376 ? 28.367 -10.523 -20.494 1.00 8.18   ? 432 LEU B CD1 1 
ATOM   2828 C CD2 . LEU A 1 376 ? 27.622 -12.875 -20.653 1.00 5.60   ? 432 LEU B CD2 1 
ATOM   2829 N N   . THR A 1 377 ? 32.700 -11.241 -20.727 1.00 19.88  ? 433 THR B N   1 
ATOM   2830 C CA  . THR A 1 377 ? 33.688 -11.733 -19.767 1.00 16.56  ? 433 THR B CA  1 
ATOM   2831 C C   . THR A 1 377 ? 33.196 -11.820 -18.318 1.00 17.65  ? 433 THR B C   1 
ATOM   2832 O O   . THR A 1 377 ? 33.822 -12.486 -17.490 1.00 10.47  ? 433 THR B O   1 
ATOM   2833 C CB  . THR A 1 377 ? 34.917 -10.842 -19.781 1.00 9.68   ? 433 THR B CB  1 
ATOM   2834 O OG1 . THR A 1 377 ? 34.529 -9.520  -19.402 1.00 14.09  ? 433 THR B OG1 1 
ATOM   2835 C CG2 . THR A 1 377 ? 35.488 -10.789 -21.174 1.00 14.59  ? 433 THR B CG2 1 
ATOM   2836 N N   . LYS A 1 378 ? 32.072 -11.170 -18.017 1.00 13.38  ? 434 LYS B N   1 
ATOM   2837 C CA  . LYS A 1 378 ? 31.566 -11.152 -16.646 1.00 7.71   ? 434 LYS B CA  1 
ATOM   2838 C C   . LYS A 1 378 ? 30.058 -11.339 -16.567 1.00 7.68   ? 434 LYS B C   1 
ATOM   2839 O O   . LYS A 1 378 ? 29.295 -10.482 -17.015 1.00 3.67   ? 434 LYS B O   1 
ATOM   2840 C CB  . LYS A 1 378 ? 31.939 -9.841  -15.948 1.00 4.19   ? 434 LYS B CB  1 
ATOM   2841 C CG  . LYS A 1 378 ? 33.414 -9.679  -15.667 1.00 5.73   ? 434 LYS B CG  1 
ATOM   2842 C CD  . LYS A 1 378 ? 33.728 -8.271  -15.211 1.00 4.44   ? 434 LYS B CD  1 
ATOM   2843 C CE  . LYS A 1 378 ? 35.198 -7.962  -15.398 1.00 12.39  ? 434 LYS B CE  1 
ATOM   2844 N NZ  . LYS A 1 378 ? 35.511 -6.661  -14.763 1.00 19.59  ? 434 LYS B NZ  1 
ATOM   2845 N N   . LEU A 1 379 ? 29.635 -12.438 -15.952 1.00 11.75  ? 435 LEU B N   1 
ATOM   2846 C CA  . LEU A 1 379 ? 28.228 -12.664 -15.666 1.00 10.83  ? 435 LEU B CA  1 
ATOM   2847 C C   . LEU A 1 379 ? 28.086 -12.838 -14.148 1.00 13.03  ? 435 LEU B C   1 
ATOM   2848 O O   . LEU A 1 379 ? 28.534 -13.839 -13.591 1.00 14.48  ? 435 LEU B O   1 
ATOM   2849 C CB  . LEU A 1 379 ? 27.744 -13.904 -16.424 1.00 3.78   ? 435 LEU B CB  1 
ATOM   2850 C CG  . LEU A 1 379 ? 26.335 -14.405 -16.129 1.00 9.08   ? 435 LEU B CG  1 
ATOM   2851 C CD1 . LEU A 1 379 ? 25.342 -13.312 -16.441 1.00 5.87   ? 435 LEU B CD1 1 
ATOM   2852 C CD2 . LEU A 1 379 ? 26.011 -15.690 -16.881 1.00 3.73   ? 435 LEU B CD2 1 
ATOM   2853 N N   . LEU A 1 380 ? 27.494 -11.851 -13.477 1.00 11.29  ? 436 LEU B N   1 
ATOM   2854 C CA  . LEU A 1 380 ? 27.367 -11.911 -12.028 1.00 3.14   ? 436 LEU B CA  1 
ATOM   2855 C C   . LEU A 1 380 ? 25.904 -11.834 -11.647 1.00 5.77   ? 436 LEU B C   1 
ATOM   2856 O O   . LEU A 1 380 ? 25.304 -10.757 -11.655 1.00 6.38   ? 436 LEU B O   1 
ATOM   2857 C CB  . LEU A 1 380 ? 28.116 -10.732 -11.419 1.00 3.12   ? 436 LEU B CB  1 
ATOM   2858 C CG  . LEU A 1 380 ? 29.515 -10.592 -12.026 1.00 3.46   ? 436 LEU B CG  1 
ATOM   2859 C CD1 . LEU A 1 380 ? 30.068 -9.168  -11.931 1.00 3.41   ? 436 LEU B CD1 1 
ATOM   2860 C CD2 . LEU A 1 380 ? 30.442 -11.584 -11.381 1.00 3.80   ? 436 LEU B CD2 1 
ATOM   2861 N N   . LEU A 1 381 ? 25.348 -13.000 -11.336 1.00 4.05   ? 437 LEU B N   1 
ATOM   2862 C CA  . LEU A 1 381 ? 23.947 -13.179 -10.966 1.00 2.54   ? 437 LEU B CA  1 
ATOM   2863 C C   . LEU A 1 381 ? 23.752 -13.487 -9.490  1.00 17.67  ? 437 LEU B C   1 
ATOM   2864 O O   . LEU A 1 381 ? 22.674 -13.933 -9.092  1.00 2.32   ? 437 LEU B O   1 
ATOM   2865 C CB  . LEU A 1 381 ? 23.269 -14.219 -11.871 1.00 17.89  ? 437 LEU B CB  1 
ATOM   2866 C CG  . LEU A 1 381 ? 23.317 -13.878 -13.370 1.00 11.97  ? 437 LEU B CG  1 
ATOM   2867 C CD1 . LEU A 1 381 ? 22.823 -15.028 -14.196 1.00 14.94  ? 437 LEU B CD1 1 
ATOM   2868 C CD2 . LEU A 1 381 ? 22.506 -12.639 -13.663 1.00 2.31   ? 437 LEU B CD2 1 
ATOM   2869 N N   . LEU A 1 382 ? 24.826 -13.366 -8.705  1.00 16.87  ? 438 LEU B N   1 
ATOM   2870 C CA  . LEU A 1 382 ? 24.820 -13.829 -7.317  1.00 10.55  ? 438 LEU B CA  1 
ATOM   2871 C C   . LEU A 1 382 ? 23.715 -13.224 -6.470  1.00 15.03  ? 438 LEU B C   1 
ATOM   2872 O O   . LEU A 1 382 ? 23.303 -12.084 -6.681  1.00 2.12   ? 438 LEU B O   1 
ATOM   2873 C CB  . LEU A 1 382 ? 26.187 -13.657 -6.631  1.00 6.10   ? 438 LEU B CB  1 
ATOM   2874 C CG  . LEU A 1 382 ? 26.785 -12.306 -6.203  1.00 4.65   ? 438 LEU B CG  1 
ATOM   2875 C CD1 . LEU A 1 382 ? 26.182 -11.744 -4.930  1.00 2.64   ? 438 LEU B CD1 1 
ATOM   2876 C CD2 . LEU A 1 382 ? 28.295 -12.418 -6.052  1.00 4.09   ? 438 LEU B CD2 1 
ATOM   2877 N N   . SER A 1 383 ? 23.238 -14.016 -5.514  1.00 16.89  ? 439 SER B N   1 
ATOM   2878 C CA  . SER A 1 383 ? 22.214 -13.572 -4.577  1.00 12.23  ? 439 SER B CA  1 
ATOM   2879 C C   . SER A 1 383 ? 20.922 -13.116 -5.270  1.00 7.30   ? 439 SER B C   1 
ATOM   2880 O O   . SER A 1 383 ? 20.642 -11.928 -5.393  1.00 9.67   ? 439 SER B O   1 
ATOM   2881 C CB  . SER A 1 383 ? 22.755 -12.511 -3.616  1.00 9.55   ? 439 SER B CB  1 
ATOM   2882 O OG  . SER A 1 383 ? 21.749 -12.096 -2.712  1.00 19.62  ? 439 SER B OG  1 
ATOM   2883 N N   . ASN A 1 384 ? 20.171 -14.086 -5.760  1.00 2.33   ? 440 ASN B N   1 
ATOM   2884 C CA  . ASN A 1 384 ? 18.829 -13.864 -6.236  1.00 2.00   ? 440 ASN B CA  1 
ATOM   2885 C C   . ASN A 1 384 ? 18.029 -15.094 -5.865  1.00 4.11   ? 440 ASN B C   1 
ATOM   2886 O O   . ASN A 1 384 ? 18.463 -15.919 -5.048  1.00 2.83   ? 440 ASN B O   1 
ATOM   2887 C CB  . ASN A 1 384 ? 18.790 -13.683 -7.763  1.00 5.07   ? 440 ASN B CB  1 
ATOM   2888 C CG  . ASN A 1 384 ? 19.190 -12.285 -8.210  1.00 9.03   ? 440 ASN B CG  1 
ATOM   2889 O OD1 . ASN A 1 384 ? 18.349 -11.407 -8.329  1.00 2.00   ? 440 ASN B OD1 1 
ATOM   2890 N ND2 . ASN A 1 384 ? 20.468 -12.088 -8.487  1.00 2.00   ? 440 ASN B ND2 1 
ATOM   2891 N N   . ASP A 1 385 ? 16.840 -15.172 -6.444  1.00 5.45   ? 441 ASP B N   1 
ATOM   2892 C CA  . ASP A 1 385 ? 15.934 -16.317 -6.360  1.00 6.30   ? 441 ASP B CA  1 
ATOM   2893 C C   . ASP A 1 385 ? 16.000 -17.292 -7.563  1.00 14.56  ? 441 ASP B C   1 
ATOM   2894 O O   . ASP A 1 385 ? 15.008 -17.960 -7.881  1.00 8.79   ? 441 ASP B O   1 
ATOM   2895 C CB  . ASP A 1 385 ? 14.506 -15.880 -6.042  1.00 17.87  ? 441 ASP B CB  1 
ATOM   2896 C CG  . ASP A 1 385 ? 13.667 -17.013 -5.497  1.00 26.44  ? 441 ASP B CG  1 
ATOM   2897 O OD1 . ASP A 1 385 ? 14.265 -18.014 -5.044  1.00 29.72  ? 441 ASP B OD1 1 
ATOM   2898 O OD2 . ASP A 1 385 ? 12.421 -16.904 -5.530  1.00 27.75  ? 441 ASP B OD2 1 
ATOM   2899 N N   . LEU A 1 386 ? 17.088 -17.237 -8.327  1.00 2.00   ? 442 LEU B N   1 
ATOM   2900 C CA  . LEU A 1 386 ? 17.231 -18.064 -9.530  1.00 12.50  ? 442 LEU B CA  1 
ATOM   2901 C C   . LEU A 1 386 ? 17.086 -19.585 -9.347  1.00 13.29  ? 442 LEU B C   1 
ATOM   2902 O O   . LEU A 1 386 ? 17.696 -20.168 -8.464  1.00 22.54  ? 442 LEU B O   1 
ATOM   2903 C CB  . LEU A 1 386 ? 18.558 -17.754 -10.227 1.00 12.51  ? 442 LEU B CB  1 
ATOM   2904 C CG  . LEU A 1 386 ? 18.677 -16.327 -10.760 1.00 4.01   ? 442 LEU B CG  1 
ATOM   2905 C CD1 . LEU A 1 386 ? 20.033 -16.100 -11.394 1.00 11.11  ? 442 LEU B CD1 1 
ATOM   2906 C CD2 . LEU A 1 386 ? 17.544 -16.035 -11.743 1.00 2.00   ? 442 LEU B CD2 1 
ATOM   2907 N N   . SER A 1 387 ? 16.290 -20.209 -10.217 1.00 12.81  ? 443 SER B N   1 
ATOM   2908 C CA  . SER A 1 387 ? 16.059 -21.655 -10.214 1.00 12.64  ? 443 SER B CA  1 
ATOM   2909 C C   . SER A 1 387 ? 16.382 -22.256 -11.590 1.00 12.66  ? 443 SER B C   1 
ATOM   2910 O O   . SER A 1 387 ? 16.795 -21.539 -12.491 1.00 10.71  ? 443 SER B O   1 
ATOM   2911 C CB  . SER A 1 387 ? 14.608 -21.953 -9.844  1.00 2.38   ? 443 SER B CB  1 
ATOM   2912 O OG  . SER A 1 387 ? 13.755 -20.895 -10.260 1.00 15.06  ? 443 SER B OG  1 
ATOM   2913 N N   . GLY A 1 388 ? 16.184 -23.565 -11.748 1.00 3.07   ? 444 GLY B N   1 
ATOM   2914 C CA  . GLY A 1 388 ? 16.479 -24.248 -12.995 1.00 13.34  ? 444 GLY B CA  1 
ATOM   2915 C C   . GLY A 1 388 ? 17.864 -24.877 -13.079 1.00 19.46  ? 444 GLY B C   1 
ATOM   2916 O O   . GLY A 1 388 ? 18.619 -24.870 -12.097 1.00 31.89  ? 444 GLY B O   1 
ATOM   2917 N N   . PHE A 1 389 ? 18.174 -25.472 -14.234 1.00 11.57  ? 445 PHE B N   1 
ATOM   2918 C CA  . PHE A 1 389 ? 19.522 -25.949 -14.543 1.00 4.33   ? 445 PHE B CA  1 
ATOM   2919 C C   . PHE A 1 389 ? 20.400 -24.826 -15.055 1.00 7.48   ? 445 PHE B C   1 
ATOM   2920 O O   . PHE A 1 389 ? 19.915 -23.848 -15.613 1.00 4.03   ? 445 PHE B O   1 
ATOM   2921 C CB  . PHE A 1 389 ? 19.505 -27.001 -15.638 1.00 4.68   ? 445 PHE B CB  1 
ATOM   2922 C CG  . PHE A 1 389 ? 18.776 -28.251 -15.284 1.00 25.89  ? 445 PHE B CG  1 
ATOM   2923 C CD1 . PHE A 1 389 ? 18.903 -28.821 -14.022 1.00 28.14  ? 445 PHE B CD1 1 
ATOM   2924 C CD2 . PHE A 1 389 ? 17.974 -28.872 -16.223 1.00 4.97   ? 445 PHE B CD2 1 
ATOM   2925 C CE1 . PHE A 1 389 ? 18.233 -29.993 -13.709 1.00 29.42  ? 445 PHE B CE1 1 
ATOM   2926 C CE2 . PHE A 1 389 ? 17.310 -30.020 -15.925 1.00 5.13   ? 445 PHE B CE2 1 
ATOM   2927 C CZ  . PHE A 1 389 ? 17.433 -30.590 -14.670 1.00 37.97  ? 445 PHE B CZ  1 
ATOM   2928 N N   . ILE A 1 390 ? 21.704 -24.980 -14.875 1.00 10.83  ? 446 ILE B N   1 
ATOM   2929 C CA  . ILE A 1 390 ? 22.661 -24.198 -15.640 1.00 13.65  ? 446 ILE B CA  1 
ATOM   2930 C C   . ILE A 1 390 ? 22.640 -24.769 -17.035 1.00 26.13  ? 446 ILE B C   1 
ATOM   2931 O O   . ILE A 1 390 ? 22.886 -25.966 -17.225 1.00 30.06  ? 446 ILE B O   1 
ATOM   2932 C CB  . ILE A 1 390 ? 24.077 -24.346 -15.092 1.00 10.87  ? 446 ILE B CB  1 
ATOM   2933 C CG1 . ILE A 1 390 ? 24.221 -23.538 -13.796 1.00 9.17   ? 446 ILE B CG1 1 
ATOM   2934 C CG2 . ILE A 1 390 ? 25.086 -23.891 -16.124 1.00 5.04   ? 446 ILE B CG2 1 
ATOM   2935 C CD1 . ILE A 1 390 ? 25.410 -23.950 -12.965 1.00 4.82   ? 446 ILE B CD1 1 
ATOM   2936 N N   . PRO A 1 391 ? 22.330 -23.923 -18.025 1.00 28.26  ? 447 PRO B N   1 
ATOM   2937 C CA  . PRO A 1 391 ? 22.205 -24.389 -19.410 1.00 17.84  ? 447 PRO B CA  1 
ATOM   2938 C C   . PRO A 1 391 ? 23.507 -25.018 -19.864 1.00 15.99  ? 447 PRO B C   1 
ATOM   2939 O O   . PRO A 1 391 ? 24.567 -24.597 -19.397 1.00 11.70  ? 447 PRO B O   1 
ATOM   2940 C CB  . PRO A 1 391 ? 21.946 -23.100 -20.189 1.00 4.69   ? 447 PRO B CB  1 
ATOM   2941 C CG  . PRO A 1 391 ? 21.412 -22.136 -19.182 1.00 29.36  ? 447 PRO B CG  1 
ATOM   2942 C CD  . PRO A 1 391 ? 22.108 -22.473 -17.901 1.00 27.03  ? 447 PRO B CD  1 
ATOM   2943 N N   . PRO A 1 392 ? 23.429 -26.034 -20.742 1.00 16.33  ? 448 PRO B N   1 
ATOM   2944 C CA  . PRO A 1 392 ? 24.607 -26.620 -21.397 1.00 10.76  ? 448 PRO B CA  1 
ATOM   2945 C C   . PRO A 1 392 ? 25.237 -25.622 -22.345 1.00 15.47  ? 448 PRO B C   1 
ATOM   2946 O O   . PRO A 1 392 ? 26.426 -25.702 -22.630 1.00 6.50   ? 448 PRO B O   1 
ATOM   2947 C CB  . PRO A 1 392 ? 24.034 -27.800 -22.177 1.00 6.47   ? 448 PRO B CB  1 
ATOM   2948 C CG  . PRO A 1 392 ? 22.568 -27.528 -22.276 1.00 20.87  ? 448 PRO B CG  1 
ATOM   2949 C CD  . PRO A 1 392 ? 22.193 -26.764 -21.061 1.00 17.78  ? 448 PRO B CD  1 
ATOM   2950 N N   . ASP A 1 393 ? 24.456 -24.644 -22.783 1.00 5.84   ? 449 ASP B N   1 
ATOM   2951 C CA  . ASP A 1 393 ? 24.966 -23.639 -23.707 1.00 17.02  ? 449 ASP B CA  1 
ATOM   2952 C C   . ASP A 1 393 ? 26.082 -22.808 -23.093 1.00 16.07  ? 449 ASP B C   1 
ATOM   2953 O O   . ASP A 1 393 ? 26.661 -21.955 -23.753 1.00 16.84  ? 449 ASP B O   1 
ATOM   2954 C CB  . ASP A 1 393 ? 23.841 -22.733 -24.193 1.00 20.81  ? 449 ASP B CB  1 
ATOM   2955 C CG  . ASP A 1 393 ? 22.617 -23.517 -24.604 1.00 28.51  ? 449 ASP B CG  1 
ATOM   2956 O OD1 . ASP A 1 393 ? 22.222 -24.434 -23.849 1.00 21.17  ? 449 ASP B OD1 1 
ATOM   2957 O OD2 . ASP A 1 393 ? 22.062 -23.226 -25.683 1.00 38.04  ? 449 ASP B OD2 1 
ATOM   2958 N N   . ILE A 1 394 ? 26.352 -23.040 -21.815 1.00 20.21  ? 450 ILE B N   1 
ATOM   2959 C CA  . ILE A 1 394 ? 27.378 -22.304 -21.087 1.00 20.45  ? 450 ILE B CA  1 
ATOM   2960 C C   . ILE A 1 394 ? 28.766 -22.424 -21.748 1.00 20.93  ? 450 ILE B C   1 
ATOM   2961 O O   . ILE A 1 394 ? 29.594 -21.529 -21.616 1.00 28.89  ? 450 ILE B O   1 
ATOM   2962 C CB  . ILE A 1 394 ? 27.383 -22.711 -19.582 1.00 23.23  ? 450 ILE B CB  1 
ATOM   2963 C CG1 . ILE A 1 394 ? 28.311 -21.815 -18.763 1.00 24.59  ? 450 ILE B CG1 1 
ATOM   2964 C CG2 . ILE A 1 394 ? 27.716 -24.192 -19.402 1.00 21.94  ? 450 ILE B CG2 1 
ATOM   2965 C CD1 . ILE A 1 394 ? 28.373 -22.183 -17.308 1.00 19.59  ? 450 ILE B CD1 1 
ATOM   2966 N N   . GLY A 1 395 ? 29.006 -23.507 -22.486 1.00 14.35  ? 451 GLY B N   1 
ATOM   2967 C CA  . GLY A 1 395 ? 30.256 -23.660 -23.219 1.00 14.52  ? 451 GLY B CA  1 
ATOM   2968 C C   . GLY A 1 395 ? 30.364 -22.786 -24.474 1.00 18.81  ? 451 GLY B C   1 
ATOM   2969 O O   . GLY A 1 395 ? 31.468 -22.495 -24.947 1.00 21.23  ? 451 GLY B O   1 
ATOM   2970 N N   . ASN A 1 396 ? 29.216 -22.379 -25.020 1.00 13.72  ? 452 ASN B N   1 
ATOM   2971 C CA  . ASN A 1 396 ? 29.158 -21.409 -26.113 1.00 13.65  ? 452 ASN B CA  1 
ATOM   2972 C C   . ASN A 1 396 ? 29.736 -20.029 -25.753 1.00 30.19  ? 452 ASN B C   1 
ATOM   2973 O O   . ASN A 1 396 ? 29.950 -19.203 -26.642 1.00 32.32  ? 452 ASN B O   1 
ATOM   2974 C CB  . ASN A 1 396 ? 27.707 -21.180 -26.565 1.00 12.66  ? 452 ASN B CB  1 
ATOM   2975 C CG  . ASN A 1 396 ? 27.068 -22.404 -27.223 1.00 14.66  ? 452 ASN B CG  1 
ATOM   2976 O OD1 . ASN A 1 396 ? 27.439 -23.549 -26.954 1.00 14.19  ? 452 ASN B OD1 1 
ATOM   2977 N ND2 . ASN A 1 396 ? 26.083 -22.145 -28.095 1.00 16.39  ? 452 ASN B ND2 1 
ATOM   2978 N N   . CYS A 1 397 ? 29.959 -19.765 -24.461 1.00 38.72  ? 453 CYS B N   1 
ATOM   2979 C CA  . CYS A 1 397 ? 30.350 -18.423 -24.018 1.00 33.41  ? 453 CYS B CA  1 
ATOM   2980 C C   . CYS A 1 397 ? 31.876 -18.384 -23.964 1.00 30.58  ? 453 CYS B C   1 
ATOM   2981 O O   . CYS A 1 397 ? 32.476 -18.756 -22.963 1.00 22.64  ? 453 CYS B O   1 
ATOM   2982 C CB  . CYS A 1 397 ? 29.774 -18.208 -22.608 1.00 5.62   ? 453 CYS B CB  1 
ATOM   2983 S SG  . CYS A 1 397 ? 29.369 -16.518 -22.095 1.00 31.10  ? 453 CYS B SG  1 
ATOM   2984 N N   . THR A 1 398 ? 32.499 -17.814 -24.991 1.00 41.77  ? 454 THR B N   1 
ATOM   2985 C CA  . THR A 1 398 ? 33.910 -18.118 -25.257 1.00 41.15  ? 454 THR B CA  1 
ATOM   2986 C C   . THR A 1 398 ? 34.824 -17.326 -24.357 1.00 32.09  ? 454 THR B C   1 
ATOM   2987 O O   . THR A 1 398 ? 35.893 -17.798 -23.974 1.00 31.33  ? 454 THR B O   1 
ATOM   2988 C CB  . THR A 1 398 ? 34.326 -17.843 -26.738 1.00 10.90  ? 454 THR B CB  1 
ATOM   2989 O OG1 . THR A 1 398 ? 33.175 -17.510 -27.519 1.00 13.19  ? 454 THR B OG1 1 
ATOM   2990 C CG2 . THR A 1 398 ? 35.007 -19.058 -27.340 1.00 7.93   ? 454 THR B CG2 1 
ATOM   2991 N N   . ASN A 1 399 ? 34.413 -16.096 -24.076 1.00 24.51  ? 455 ASN B N   1 
ATOM   2992 C CA  . ASN A 1 399 ? 35.240 -15.160 -23.334 1.00 20.58  ? 455 ASN B CA  1 
ATOM   2993 C C   . ASN A 1 399 ? 34.910 -15.034 -21.856 1.00 16.31  ? 455 ASN B C   1 
ATOM   2994 O O   . ASN A 1 399 ? 35.456 -14.161 -21.192 1.00 18.16  ? 455 ASN B O   1 
ATOM   2995 C CB  . ASN A 1 399 ? 35.260 -13.785 -24.006 1.00 21.49  ? 455 ASN B CB  1 
ATOM   2996 C CG  . ASN A 1 399 ? 36.073 -13.775 -25.291 1.00 21.33  ? 455 ASN B CG  1 
ATOM   2997 O OD1 . ASN A 1 399 ? 37.300 -13.786 -25.266 1.00 28.58  ? 455 ASN B OD1 1 
ATOM   2998 N ND2 . ASN A 1 399 ? 35.388 -13.746 -26.418 1.00 26.29  ? 455 ASN B ND2 1 
ATOM   2999 N N   . LEU A 1 400 ? 33.991 -15.862 -21.359 1.00 11.14  ? 456 LEU B N   1 
ATOM   3000 C CA  . LEU A 1 400 ? 33.608 -15.808 -19.954 1.00 10.57  ? 456 LEU B CA  1 
ATOM   3001 C C   . LEU A 1 400 ? 34.843 -15.961 -19.089 1.00 18.38  ? 456 LEU B C   1 
ATOM   3002 O O   . LEU A 1 400 ? 35.598 -16.914 -19.219 1.00 18.57  ? 456 LEU B O   1 
ATOM   3003 C CB  . LEU A 1 400 ? 32.583 -16.894 -19.615 1.00 5.81   ? 456 LEU B CB  1 
ATOM   3004 C CG  . LEU A 1 400 ? 31.732 -16.756 -18.346 1.00 5.42   ? 456 LEU B CG  1 
ATOM   3005 C CD1 . LEU A 1 400 ? 30.981 -15.450 -18.320 1.00 4.99   ? 456 LEU B CD1 1 
ATOM   3006 C CD2 . LEU A 1 400 ? 30.764 -17.917 -18.246 1.00 5.37   ? 456 LEU B CD2 1 
ATOM   3007 N N   . TYR A 1 401 ? 35.027 -14.995 -18.204 1.00 26.55  ? 457 TYR B N   1 
ATOM   3008 C CA  . TYR A 1 401 ? 36.198 -14.905 -17.344 1.00 22.32  ? 457 TYR B CA  1 
ATOM   3009 C C   . TYR A 1 401 ? 35.781 -15.071 -15.879 1.00 19.94  ? 457 TYR B C   1 
ATOM   3010 O O   . TYR A 1 401 ? 36.298 -15.928 -15.156 1.00 13.70  ? 457 TYR B O   1 
ATOM   3011 C CB  . TYR A 1 401 ? 36.890 -13.562 -17.548 1.00 9.70   ? 457 TYR B CB  1 
ATOM   3012 C CG  . TYR A 1 401 ? 38.256 -13.466 -16.906 1.00 15.22  ? 457 TYR B CG  1 
ATOM   3013 C CD1 . TYR A 1 401 ? 39.347 -14.102 -17.474 1.00 7.30   ? 457 TYR B CD1 1 
ATOM   3014 C CD2 . TYR A 1 401 ? 38.460 -12.726 -15.746 1.00 11.63  ? 457 TYR B CD2 1 
ATOM   3015 C CE1 . TYR A 1 401 ? 40.594 -14.015 -16.919 1.00 16.31  ? 457 TYR B CE1 1 
ATOM   3016 C CE2 . TYR A 1 401 ? 39.718 -12.631 -15.179 1.00 12.68  ? 457 TYR B CE2 1 
ATOM   3017 C CZ  . TYR A 1 401 ? 40.778 -13.285 -15.770 1.00 20.67  ? 457 TYR B CZ  1 
ATOM   3018 O OH  . TYR A 1 401 ? 42.038 -13.215 -15.229 1.00 31.71  ? 457 TYR B OH  1 
ATOM   3019 N N   . ARG A 1 402 ? 34.888 -14.184 -15.448 1.00 12.86  ? 458 ARG B N   1 
ATOM   3020 C CA  . ARG A 1 402 ? 34.378 -14.174 -14.092 1.00 5.40   ? 458 ARG B CA  1 
ATOM   3021 C C   . ARG A 1 402 ? 32.919 -14.590 -14.063 1.00 8.14   ? 458 ARG B C   1 
ATOM   3022 O O   . ARG A 1 402 ? 32.044 -13.841 -14.486 1.00 8.26   ? 458 ARG B O   1 
ATOM   3023 C CB  . ARG A 1 402 ? 34.526 -12.772 -13.499 1.00 12.23  ? 458 ARG B CB  1 
ATOM   3024 C CG  . ARG A 1 402 ? 34.203 -12.671 -12.021 1.00 15.54  ? 458 ARG B CG  1 
ATOM   3025 C CD  . ARG A 1 402 ? 34.914 -11.482 -11.432 1.00 21.34  ? 458 ARG B CD  1 
ATOM   3026 N NE  . ARG A 1 402 ? 34.421 -11.129 -10.108 1.00 21.57  ? 458 ARG B NE  1 
ATOM   3027 C CZ  . ARG A 1 402 ? 34.901 -11.636 -8.979  1.00 16.46  ? 458 ARG B CZ  1 
ATOM   3028 N NH1 . ARG A 1 402 ? 34.400 -11.257 -7.807  1.00 14.19  ? 458 ARG B NH1 1 
ATOM   3029 N NH2 . ARG A 1 402 ? 35.879 -12.529 -9.023  1.00 13.40  ? 458 ARG B NH2 1 
ATOM   3030 N N   . LEU A 1 403 ? 32.654 -15.773 -13.529 1.00 5.12   ? 459 LEU B N   1 
ATOM   3031 C CA  . LEU A 1 403 ? 31.291 -16.263 -13.456 1.00 13.21  ? 459 LEU B CA  1 
ATOM   3032 C C   . LEU A 1 403 ? 30.856 -16.511 -12.001 1.00 12.60  ? 459 LEU B C   1 
ATOM   3033 O O   . LEU A 1 403 ? 31.442 -17.341 -11.310 1.00 13.96  ? 459 LEU B O   1 
ATOM   3034 C CB  . LEU A 1 403 ? 31.169 -17.542 -14.276 1.00 11.49  ? 459 LEU B CB  1 
ATOM   3035 C CG  . LEU A 1 403 ? 29.796 -18.190 -14.208 1.00 16.11  ? 459 LEU B CG  1 
ATOM   3036 C CD1 . LEU A 1 403 ? 28.792 -17.340 -14.968 1.00 21.36  ? 459 LEU B CD1 1 
ATOM   3037 C CD2 . LEU A 1 403 ? 29.853 -19.609 -14.727 1.00 5.14   ? 459 LEU B CD2 1 
ATOM   3038 N N   . ARG A 1 404 ? 29.846 -15.781 -11.526 1.00 12.55  ? 460 ARG B N   1 
ATOM   3039 C CA  . ARG A 1 404 ? 29.328 -16.018 -10.171 1.00 9.65   ? 460 ARG B CA  1 
ATOM   3040 C C   . ARG A 1 404 ? 27.811 -16.213 -10.149 1.00 7.22   ? 460 ARG B C   1 
ATOM   3041 O O   . ARG A 1 404 ? 27.037 -15.285 -10.414 1.00 6.12   ? 460 ARG B O   1 
ATOM   3042 C CB  . ARG A 1 404 ? 29.716 -14.869 -9.238  1.00 11.16  ? 460 ARG B CB  1 
ATOM   3043 C CG  . ARG A 1 404 ? 31.142 -14.390 -9.419  1.00 12.12  ? 460 ARG B CG  1 
ATOM   3044 C CD  . ARG A 1 404 ? 31.553 -13.569 -8.241  1.00 4.22   ? 460 ARG B CD  1 
ATOM   3045 N NE  . ARG A 1 404 ? 31.359 -14.368 -7.039  1.00 23.05  ? 460 ARG B NE  1 
ATOM   3046 C CZ  . ARG A 1 404 ? 31.379 -13.901 -5.799  1.00 14.72  ? 460 ARG B CZ  1 
ATOM   3047 N NH1 . ARG A 1 404 ? 31.585 -12.609 -5.561  1.00 4.03   ? 460 ARG B NH1 1 
ATOM   3048 N NH2 . ARG A 1 404 ? 31.183 -14.746 -4.799  1.00 9.54   ? 460 ARG B NH2 1 
ATOM   3049 N N   . LEU A 1 405 ? 27.398 -17.444 -9.884  1.00 3.87   ? 461 LEU B N   1 
ATOM   3050 C CA  . LEU A 1 405 ? 25.984 -17.792 -9.823  1.00 7.80   ? 461 LEU B CA  1 
ATOM   3051 C C   . LEU A 1 405 ? 25.498 -18.013 -8.408  1.00 8.62   ? 461 LEU B C   1 
ATOM   3052 O O   . LEU A 1 405 ? 24.361 -18.420 -8.181  1.00 15.51  ? 461 LEU B O   1 
ATOM   3053 C CB  . LEU A 1 405 ? 25.675 -18.982 -10.738 1.00 19.00  ? 461 LEU B CB  1 
ATOM   3054 C CG  . LEU A 1 405 ? 26.051 -18.745 -12.203 1.00 3.92   ? 461 LEU B CG  1 
ATOM   3055 C CD1 . LEU A 1 405 ? 25.640 -19.920 -13.000 1.00 4.10   ? 461 LEU B CD1 1 
ATOM   3056 C CD2 . LEU A 1 405 ? 25.362 -17.514 -12.712 1.00 3.60   ? 461 LEU B CD2 1 
ATOM   3057 N N   . ASN A 1 406 ? 26.396 -17.778 -7.464  1.00 7.74   ? 462 ASN B N   1 
ATOM   3058 C CA  . ASN A 1 406 ? 26.204 -18.176 -6.077  1.00 12.50  ? 462 ASN B CA  1 
ATOM   3059 C C   . ASN A 1 406 ? 25.043 -17.494 -5.345  1.00 13.97  ? 462 ASN B C   1 
ATOM   3060 O O   . ASN A 1 406 ? 24.690 -16.352 -5.627  1.00 11.22  ? 462 ASN B O   1 
ATOM   3061 C CB  . ASN A 1 406 ? 27.516 -18.015 -5.309  1.00 3.78   ? 462 ASN B CB  1 
ATOM   3062 C CG  . ASN A 1 406 ? 27.971 -16.582 -5.234  1.00 15.23  ? 462 ASN B CG  1 
ATOM   3063 O OD1 . ASN A 1 406 ? 28.482 -16.034 -6.202  1.00 21.51  ? 462 ASN B OD1 1 
ATOM   3064 N ND2 . ASN A 1 406 ? 27.793 -15.963 -4.074  1.00 17.67  ? 462 ASN B ND2 1 
ATOM   3065 N N   . GLY A 1 407 ? 24.455 -18.207 -4.391  1.00 18.66  ? 463 GLY B N   1 
ATOM   3066 C CA  . GLY A 1 407 ? 23.322 -17.686 -3.663  1.00 2.80   ? 463 GLY B CA  1 
ATOM   3067 C C   . GLY A 1 407 ? 22.049 -17.660 -4.475  1.00 2.57   ? 463 GLY B C   1 
ATOM   3068 O O   . GLY A 1 407 ? 21.387 -16.630 -4.596  1.00 2.45   ? 463 GLY B O   1 
ATOM   3069 N N   . ASN A 1 408 ? 21.706 -18.807 -5.037  1.00 2.70   ? 464 ASN B N   1 
ATOM   3070 C CA  . ASN A 1 408 ? 20.460 -18.973 -5.768  1.00 2.53   ? 464 ASN B CA  1 
ATOM   3071 C C   . ASN A 1 408 ? 19.944 -20.372 -5.473  1.00 7.79   ? 464 ASN B C   1 
ATOM   3072 O O   . ASN A 1 408 ? 20.445 -21.054 -4.583  1.00 10.96  ? 464 ASN B O   1 
ATOM   3073 C CB  . ASN A 1 408 ? 20.684 -18.817 -7.277  1.00 7.95   ? 464 ASN B CB  1 
ATOM   3074 C CG  . ASN A 1 408 ? 20.903 -17.363 -7.708  1.00 6.27   ? 464 ASN B CG  1 
ATOM   3075 O OD1 . ASN A 1 408 ? 19.971 -16.569 -7.736  1.00 2.16   ? 464 ASN B OD1 1 
ATOM   3076 N ND2 . ASN A 1 408 ? 22.129 -17.031 -8.078  1.00 2.63   ? 464 ASN B ND2 1 
ATOM   3077 N N   . ARG A 1 409 ? 18.911 -20.785 -6.184  1.00 2.58   ? 465 ARG B N   1 
ATOM   3078 C CA  . ARG A 1 409 ? 18.409 -22.159 -6.114  1.00 2.73   ? 465 ARG B CA  1 
ATOM   3079 C C   . ARG A 1 409 ? 18.741 -23.153 -7.244  1.00 3.69   ? 465 ARG B C   1 
ATOM   3080 O O   . ARG A 1 409 ? 18.133 -24.221 -7.285  1.00 13.50  ? 465 ARG B O   1 
ATOM   3081 C CB  . ARG A 1 409 ? 16.919 -22.182 -5.772  1.00 11.20  ? 465 ARG B CB  1 
ATOM   3082 C CG  . ARG A 1 409 ? 16.642 -21.793 -4.343  1.00 5.88   ? 465 ARG B CG  1 
ATOM   3083 C CD  . ARG A 1 409 ? 15.193 -22.001 -3.978  1.00 12.80  ? 465 ARG B CD  1 
ATOM   3084 N NE  . ARG A 1 409 ? 14.308 -21.102 -4.712  1.00 21.12  ? 465 ARG B NE  1 
ATOM   3085 C CZ  . ARG A 1 409 ? 13.465 -21.509 -5.655  1.00 31.17  ? 465 ARG B CZ  1 
ATOM   3086 N NH1 . ARG A 1 409 ? 13.392 -22.798 -5.956  1.00 31.74  ? 465 ARG B NH1 1 
ATOM   3087 N NH2 . ARG A 1 409 ? 12.685 -20.640 -6.286  1.00 32.27  ? 465 ARG B NH2 1 
ATOM   3088 N N   . LEU A 1 410 ? 19.634 -22.793 -8.171  1.00 12.11  ? 466 LEU B N   1 
ATOM   3089 C CA  . LEU A 1 410 ? 19.880 -23.582 -9.408  1.00 12.58  ? 466 LEU B CA  1 
ATOM   3090 C C   . LEU A 1 410 ? 20.047 -25.077 -9.146  1.00 15.32  ? 466 LEU B C   1 
ATOM   3091 O O   . LEU A 1 410 ? 20.789 -25.477 -8.241  1.00 24.15  ? 466 LEU B O   1 
ATOM   3092 C CB  . LEU A 1 410 ? 21.162 -23.110 -10.096 1.00 3.62   ? 466 LEU B CB  1 
ATOM   3093 C CG  . LEU A 1 410 ? 21.332 -21.623 -10.371 1.00 3.39   ? 466 LEU B CG  1 
ATOM   3094 C CD1 . LEU A 1 410 ? 22.787 -21.296 -10.640 1.00 3.62   ? 466 LEU B CD1 1 
ATOM   3095 C CD2 . LEU A 1 410 ? 20.451 -21.209 -11.518 1.00 3.24   ? 466 LEU B CD2 1 
ATOM   3096 N N   . ALA A 1 411 ? 19.354 -25.907 -9.925  1.00 10.61  ? 467 ALA B N   1 
ATOM   3097 C CA  . ALA A 1 411 ? 19.335 -27.341 -9.623  1.00 16.67  ? 467 ALA B CA  1 
ATOM   3098 C C   . ALA A 1 411 ? 20.158 -28.173 -10.594 1.00 4.54   ? 467 ALA B C   1 
ATOM   3099 O O   . ALA A 1 411 ? 20.790 -27.627 -11.490 1.00 12.15  ? 467 ALA B O   1 
ATOM   3100 C CB  . ALA A 1 411 ? 17.923 -27.851 -9.549  1.00 4.03   ? 467 ALA B CB  1 
ATOM   3101 N N   . GLY A 1 412 ? 20.158 -29.492 -10.396 1.00 6.14   ? 468 GLY B N   1 
ATOM   3102 C CA  . GLY A 1 412 ? 20.789 -30.417 -11.326 1.00 5.23   ? 468 GLY B CA  1 
ATOM   3103 C C   . GLY A 1 412 ? 22.303 -30.407 -11.355 1.00 17.39  ? 468 GLY B C   1 
ATOM   3104 O O   . GLY A 1 412 ? 22.931 -29.681 -10.599 1.00 21.65  ? 468 GLY B O   1 
ATOM   3105 N N   . SER A 1 413 ? 22.890 -31.222 -12.231 1.00 20.78  ? 469 SER B N   1 
ATOM   3106 C CA  . SER A 1 413 ? 24.349 -31.318 -12.368 1.00 6.20   ? 469 SER B CA  1 
ATOM   3107 C C   . SER A 1 413 ? 24.982 -30.126 -13.095 1.00 9.69   ? 469 SER B C   1 
ATOM   3108 O O   . SER A 1 413 ? 24.298 -29.358 -13.773 1.00 10.16  ? 469 SER B O   1 
ATOM   3109 C CB  . SER A 1 413 ? 24.741 -32.614 -13.071 1.00 6.68   ? 469 SER B CB  1 
ATOM   3110 O OG  . SER A 1 413 ? 24.087 -33.720 -12.482 1.00 33.56  ? 469 SER B OG  1 
ATOM   3111 N N   . ILE A 1 414 ? 26.290 -29.970 -12.913 1.00 12.06  ? 470 ILE B N   1 
ATOM   3112 C CA  . ILE A 1 414 ? 27.085 -28.986 -13.636 1.00 14.42  ? 470 ILE B CA  1 
ATOM   3113 C C   . ILE A 1 414 ? 27.456 -29.553 -15.005 1.00 20.27  ? 470 ILE B C   1 
ATOM   3114 O O   . ILE A 1 414 ? 28.196 -30.551 -15.094 1.00 12.32  ? 470 ILE B O   1 
ATOM   3115 C CB  . ILE A 1 414 ? 28.386 -28.661 -12.875 1.00 14.93  ? 470 ILE B CB  1 
ATOM   3116 C CG1 . ILE A 1 414 ? 28.069 -28.160 -11.461 1.00 12.87  ? 470 ILE B CG1 1 
ATOM   3117 C CG2 . ILE A 1 414 ? 29.245 -27.668 -13.663 1.00 9.22   ? 470 ILE B CG2 1 
ATOM   3118 C CD1 . ILE A 1 414 ? 29.273 -27.916 -10.612 1.00 6.32   ? 470 ILE B CD1 1 
ATOM   3119 N N   . PRO A 1 415 ? 26.951 -28.916 -16.083 1.00 20.12  ? 471 PRO B N   1 
ATOM   3120 C CA  . PRO A 1 415 ? 27.155 -29.402 -17.447 1.00 20.83  ? 471 PRO B CA  1 
ATOM   3121 C C   . PRO A 1 415 ? 28.629 -29.488 -17.809 1.00 23.34  ? 471 PRO B C   1 
ATOM   3122 O O   . PRO A 1 415 ? 29.410 -28.585 -17.484 1.00 18.22  ? 471 PRO B O   1 
ATOM   3123 C CB  . PRO A 1 415 ? 26.471 -28.337 -18.299 1.00 23.55  ? 471 PRO B CB  1 
ATOM   3124 C CG  . PRO A 1 415 ? 26.475 -27.123 -17.451 1.00 23.73  ? 471 PRO B CG  1 
ATOM   3125 C CD  . PRO A 1 415 ? 26.264 -27.614 -16.072 1.00 18.58  ? 471 PRO B CD  1 
ATOM   3126 N N   . SER A 1 416 ? 28.987 -30.564 -18.504 1.00 21.95  ? 472 SER B N   1 
ATOM   3127 C CA  . SER A 1 416 ? 30.368 -30.864 -18.851 1.00 17.62  ? 472 SER B CA  1 
ATOM   3128 C C   . SER A 1 416 ? 30.903 -29.909 -19.908 1.00 14.22  ? 472 SER B C   1 
ATOM   3129 O O   . SER A 1 416 ? 32.071 -29.967 -20.269 1.00 13.91  ? 472 SER B O   1 
ATOM   3130 C CB  . SER A 1 416 ? 30.475 -32.305 -19.347 1.00 25.15  ? 472 SER B CB  1 
ATOM   3131 O OG  . SER A 1 416 ? 29.922 -33.209 -18.404 1.00 32.39  ? 472 SER B OG  1 
ATOM   3132 N N   . GLU A 1 417 ? 30.046 -29.040 -20.426 1.00 7.91   ? 473 GLU B N   1 
ATOM   3133 C CA  . GLU A 1 417 ? 30.484 -28.105 -21.439 1.00 7.92   ? 473 GLU B CA  1 
ATOM   3134 C C   . GLU A 1 417 ? 31.309 -26.995 -20.852 1.00 15.27  ? 473 GLU B C   1 
ATOM   3135 O O   . GLU A 1 417 ? 31.929 -26.247 -21.575 1.00 26.58  ? 473 GLU B O   1 
ATOM   3136 C CB  . GLU A 1 417 ? 29.295 -27.494 -22.169 1.00 15.58  ? 473 GLU B CB  1 
ATOM   3137 C CG  . GLU A 1 417 ? 27.972 -28.130 -21.850 1.00 22.90  ? 473 GLU B CG  1 
ATOM   3138 C CD  . GLU A 1 417 ? 27.751 -29.412 -22.588 1.00 30.48  ? 473 GLU B CD  1 
ATOM   3139 O OE1 . GLU A 1 417 ? 28.663 -30.261 -22.594 1.00 35.03  ? 473 GLU B OE1 1 
ATOM   3140 O OE2 . GLU A 1 417 ? 26.653 -29.579 -23.148 1.00 38.46  ? 473 GLU B OE2 1 
ATOM   3141 N N   . ILE A 1 418 ? 31.316 -26.876 -19.534 1.00 19.11  ? 474 ILE B N   1 
ATOM   3142 C CA  . ILE A 1 418 ? 31.965 -25.743 -18.890 1.00 13.56  ? 474 ILE B CA  1 
ATOM   3143 C C   . ILE A 1 418 ? 33.477 -25.866 -19.064 1.00 17.38  ? 474 ILE B C   1 
ATOM   3144 O O   . ILE A 1 418 ? 34.220 -24.894 -18.937 1.00 21.84  ? 474 ILE B O   1 
ATOM   3145 C CB  . ILE A 1 418 ? 31.542 -25.628 -17.399 1.00 17.85  ? 474 ILE B CB  1 
ATOM   3146 C CG1 . ILE A 1 418 ? 31.887 -24.244 -16.845 1.00 17.47  ? 474 ILE B CG1 1 
ATOM   3147 C CG2 . ILE A 1 418 ? 32.152 -26.752 -16.560 1.00 16.78  ? 474 ILE B CG2 1 
ATOM   3148 C CD1 . ILE A 1 418 ? 31.446 -24.033 -15.438 1.00 12.71  ? 474 ILE B CD1 1 
ATOM   3149 N N   . GLY A 1 419 ? 33.917 -27.077 -19.384 1.00 23.41  ? 475 GLY B N   1 
ATOM   3150 C CA  . GLY A 1 419 ? 35.296 -27.325 -19.764 1.00 25.36  ? 475 GLY B CA  1 
ATOM   3151 C C   . GLY A 1 419 ? 35.639 -26.829 -21.164 1.00 18.24  ? 475 GLY B C   1 
ATOM   3152 O O   . GLY A 1 419 ? 36.801 -26.868 -21.547 1.00 12.45  ? 475 GLY B O   1 
ATOM   3153 N N   . ASN A 1 420 ? 34.635 -26.378 -21.922 1.00 8.76   ? 476 ASN B N   1 
ATOM   3154 C CA  . ASN A 1 420 ? 34.850 -25.683 -23.181 1.00 8.84   ? 476 ASN B CA  1 
ATOM   3155 C C   . ASN A 1 420 ? 35.469 -24.311 -22.961 1.00 29.48  ? 476 ASN B C   1 
ATOM   3156 O O   . ASN A 1 420 ? 36.057 -23.730 -23.881 1.00 27.71  ? 476 ASN B O   1 
ATOM   3157 C CB  . ASN A 1 420 ? 33.523 -25.489 -23.912 1.00 48.85  ? 476 ASN B CB  1 
ATOM   3158 C CG  . ASN A 1 420 ? 33.538 -26.026 -25.327 1.00 43.17  ? 476 ASN B CG  1 
ATOM   3159 O OD1 . ASN A 1 420 ? 34.575 -26.032 -26.000 1.00 32.47  ? 476 ASN B OD1 1 
ATOM   3160 N ND2 . ASN A 1 420 ? 32.373 -26.476 -25.793 1.00 45.10  ? 476 ASN B ND2 1 
ATOM   3161 N N   . LEU A 1 421 ? 35.352 -23.782 -21.745 1.00 17.11  ? 477 LEU B N   1 
ATOM   3162 C CA  . LEU A 1 421 ? 35.698 -22.376 -21.543 1.00 18.05  ? 477 LEU B CA  1 
ATOM   3163 C C   . LEU A 1 421 ? 37.156 -22.206 -21.152 1.00 23.80  ? 477 LEU B C   1 
ATOM   3164 O O   . LEU A 1 421 ? 37.558 -22.499 -20.029 1.00 30.57  ? 477 LEU B O   1 
ATOM   3165 C CB  . LEU A 1 421 ? 34.791 -21.763 -20.488 1.00 13.79  ? 477 LEU B CB  1 
ATOM   3166 C CG  . LEU A 1 421 ? 33.315 -21.966 -20.791 1.00 13.08  ? 477 LEU B CG  1 
ATOM   3167 C CD1 . LEU A 1 421 ? 32.417 -21.199 -19.825 1.00 17.02  ? 477 LEU B CD1 1 
ATOM   3168 C CD2 . LEU A 1 421 ? 33.071 -21.530 -22.200 1.00 11.59  ? 477 LEU B CD2 1 
ATOM   3169 N N   . LYS A 1 422 ? 37.940 -21.687 -22.090 1.00 26.62  ? 478 LYS B N   1 
ATOM   3170 C CA  . LYS A 1 422 ? 39.390 -21.689 -21.949 1.00 26.30  ? 478 LYS B CA  1 
ATOM   3171 C C   . LYS A 1 422 ? 39.925 -20.415 -21.328 1.00 17.85  ? 478 LYS B C   1 
ATOM   3172 O O   . LYS A 1 422 ? 41.106 -20.336 -20.992 1.00 15.06  ? 478 LYS B O   1 
ATOM   3173 C CB  . LYS A 1 422 ? 40.037 -21.935 -23.308 1.00 9.81   ? 478 LYS B CB  1 
ATOM   3174 C CG  . LYS A 1 422 ? 39.382 -23.078 -24.068 1.00 17.79  ? 478 LYS B CG  1 
ATOM   3175 C CD  . LYS A 1 422 ? 39.838 -24.438 -23.560 1.00 15.14  ? 478 LYS B CD  1 
ATOM   3176 C CE  . LYS A 1 422 ? 38.938 -25.555 -24.083 1.00 16.28  ? 478 LYS B CE  1 
ATOM   3177 N NZ  . LYS A 1 422 ? 39.418 -26.914 -23.669 1.00 12.66  ? 478 LYS B NZ  1 
ATOM   3178 N N   . ASN A 1 423 ? 39.067 -19.408 -21.209 1.00 14.94  ? 479 ASN B N   1 
ATOM   3179 C CA  . ASN A 1 423 ? 39.453 -18.173 -20.545 1.00 24.80  ? 479 ASN B CA  1 
ATOM   3180 C C   . ASN A 1 423 ? 38.927 -18.046 -19.107 1.00 28.46  ? 479 ASN B C   1 
ATOM   3181 O O   . ASN A 1 423 ? 39.177 -17.049 -18.429 1.00 7.85   ? 479 ASN B O   1 
ATOM   3182 C CB  . ASN A 1 423 ? 39.073 -16.967 -21.407 1.00 27.84  ? 479 ASN B CB  1 
ATOM   3183 C CG  . ASN A 1 423 ? 39.564 -17.103 -22.843 1.00 32.79  ? 479 ASN B CG  1 
ATOM   3184 O OD1 . ASN A 1 423 ? 38.887 -17.696 -23.682 1.00 46.09  ? 479 ASN B OD1 1 
ATOM   3185 N ND2 . ASN A 1 423 ? 40.744 -16.563 -23.128 1.00 23.24  ? 479 ASN B ND2 1 
ATOM   3186 N N   . LEU A 1 424 ? 38.217 -19.064 -18.634 1.00 23.07  ? 480 LEU B N   1 
ATOM   3187 C CA  . LEU A 1 424 ? 37.441 -18.899 -17.425 1.00 7.48   ? 480 LEU B CA  1 
ATOM   3188 C C   . LEU A 1 424 ? 38.359 -18.966 -16.213 1.00 24.54  ? 480 LEU B C   1 
ATOM   3189 O O   . LEU A 1 424 ? 38.916 -20.009 -15.870 1.00 17.09  ? 480 LEU B O   1 
ATOM   3190 C CB  . LEU A 1 424 ? 36.399 -20.008 -17.364 1.00 7.34   ? 480 LEU B CB  1 
ATOM   3191 C CG  . LEU A 1 424 ? 35.307 -19.980 -16.295 1.00 7.82   ? 480 LEU B CG  1 
ATOM   3192 C CD1 . LEU A 1 424 ? 34.760 -18.571 -16.047 1.00 6.42   ? 480 LEU B CD1 1 
ATOM   3193 C CD2 . LEU A 1 424 ? 34.201 -20.910 -16.754 1.00 6.76   ? 480 LEU B CD2 1 
ATOM   3194 N N   . ASN A 1 425 ? 38.505 -17.820 -15.563 1.00 28.50  ? 481 ASN B N   1 
ATOM   3195 C CA  . ASN A 1 425 ? 39.365 -17.699 -14.404 1.00 22.98  ? 481 ASN B CA  1 
ATOM   3196 C C   . ASN A 1 425 ? 38.678 -18.046 -13.101 1.00 19.54  ? 481 ASN B C   1 
ATOM   3197 O O   . ASN A 1 425 ? 39.258 -18.720 -12.253 1.00 20.99  ? 481 ASN B O   1 
ATOM   3198 C CB  . ASN A 1 425 ? 39.969 -16.299 -14.323 1.00 21.04  ? 481 ASN B CB  1 
ATOM   3199 C CG  . ASN A 1 425 ? 40.980 -16.175 -13.213 1.00 30.16  ? 481 ASN B CG  1 
ATOM   3200 O OD1 . ASN A 1 425 ? 42.071 -16.733 -13.297 1.00 37.57  ? 481 ASN B OD1 1 
ATOM   3201 N ND2 . ASN A 1 425 ? 40.623 -15.448 -12.158 1.00 31.52  ? 481 ASN B ND2 1 
ATOM   3202 N N   . PHE A 1 426 ? 37.446 -17.561 -12.955 1.00 16.16  ? 482 PHE B N   1 
ATOM   3203 C CA  . PHE A 1 426 ? 36.770 -17.480 -11.656 1.00 10.89  ? 482 PHE B CA  1 
ATOM   3204 C C   . PHE A 1 426 ? 35.343 -17.966 -11.770 1.00 9.74   ? 482 PHE B C   1 
ATOM   3205 O O   . PHE A 1 426 ? 34.509 -17.295 -12.379 1.00 10.08  ? 482 PHE B O   1 
ATOM   3206 C CB  . PHE A 1 426 ? 36.751 -16.004 -11.230 1.00 9.17   ? 482 PHE B CB  1 
ATOM   3207 C CG  . PHE A 1 426 ? 36.302 -15.753 -9.814  1.00 10.60  ? 482 PHE B CG  1 
ATOM   3208 C CD1 . PHE A 1 426 ? 34.955 -15.702 -9.485  1.00 17.20  ? 482 PHE B CD1 1 
ATOM   3209 C CD2 . PHE A 1 426 ? 37.233 -15.507 -8.814  1.00 10.45  ? 482 PHE B CD2 1 
ATOM   3210 C CE1 . PHE A 1 426 ? 34.553 -15.442 -8.181  1.00 5.31   ? 482 PHE B CE1 1 
ATOM   3211 C CE2 . PHE A 1 426 ? 36.837 -15.243 -7.525  1.00 5.95   ? 482 PHE B CE2 1 
ATOM   3212 C CZ  . PHE A 1 426 ? 35.494 -15.216 -7.209  1.00 5.52   ? 482 PHE B CZ  1 
ATOM   3213 N N   . VAL A 1 427 ? 35.027 -19.089 -11.137 1.00 6.21   ? 483 VAL B N   1 
ATOM   3214 C CA  . VAL A 1 427 ? 33.631 -19.501 -11.066 1.00 15.14  ? 483 VAL B CA  1 
ATOM   3215 C C   . VAL A 1 427 ? 33.154 -19.701 -9.628  1.00 13.10  ? 483 VAL B C   1 
ATOM   3216 O O   . VAL A 1 427 ? 33.818 -20.366 -8.832  1.00 16.01  ? 483 VAL B O   1 
ATOM   3217 C CB  . VAL A 1 427 ? 33.313 -20.711 -11.994 1.00 14.80  ? 483 VAL B CB  1 
ATOM   3218 C CG1 . VAL A 1 427 ? 34.535 -21.135 -12.748 1.00 6.55   ? 483 VAL B CG1 1 
ATOM   3219 C CG2 . VAL A 1 427 ? 32.709 -21.880 -11.233 1.00 8.92   ? 483 VAL B CG2 1 
ATOM   3220 N N   . ASP A 1 428 ? 32.026 -19.082 -9.282  1.00 15.80  ? 484 ASP B N   1 
ATOM   3221 C CA  . ASP A 1 428 ? 31.426 -19.315 -7.970  1.00 12.55  ? 484 ASP B CA  1 
ATOM   3222 C C   . ASP A 1 428 ? 29.970 -19.704 -8.138  1.00 10.30  ? 484 ASP B C   1 
ATOM   3223 O O   . ASP A 1 428 ? 29.103 -18.869 -8.418  1.00 5.72   ? 484 ASP B O   1 
ATOM   3224 C CB  . ASP A 1 428 ? 31.539 -18.047 -7.112  1.00 10.57  ? 484 ASP B CB  1 
ATOM   3225 C CG  . ASP A 1 428 ? 30.955 -18.214 -5.718  1.00 16.24  ? 484 ASP B CG  1 
ATOM   3226 O OD1 . ASP A 1 428 ? 30.562 -19.345 -5.344  1.00 16.97  ? 484 ASP B OD1 1 
ATOM   3227 O OD2 . ASP A 1 428 ? 30.901 -17.199 -4.985  1.00 19.85  ? 484 ASP B OD2 1 
ATOM   3228 N N   . ILE A 1 429 ? 29.736 -20.997 -7.959  1.00 4.90   ? 485 ILE B N   1 
ATOM   3229 C CA  . ILE A 1 429 ? 28.425 -21.629 -7.919  1.00 4.69   ? 485 ILE B CA  1 
ATOM   3230 C C   . ILE A 1 429 ? 27.977 -22.027 -6.515  1.00 11.73  ? 485 ILE B C   1 
ATOM   3231 O O   . ILE A 1 429 ? 27.128 -22.896 -6.362  1.00 4.90   ? 485 ILE B O   1 
ATOM   3232 C CB  . ILE A 1 429 ? 28.304 -22.807 -8.883  1.00 12.61  ? 485 ILE B CB  1 
ATOM   3233 C CG1 . ILE A 1 429 ? 29.394 -22.755 -9.948  1.00 7.42   ? 485 ILE B CG1 1 
ATOM   3234 C CG2 . ILE A 1 429 ? 26.942 -22.781 -9.563  1.00 18.86  ? 485 ILE B CG2 1 
ATOM   3235 C CD1 . ILE A 1 429 ? 29.337 -23.918 -10.901 1.00 7.03   ? 485 ILE B CD1 1 
ATOM   3236 N N   . SER A 1 430 ? 28.648 -21.520 -5.493  1.00 4.60   ? 486 SER B N   1 
ATOM   3237 C CA  . SER A 1 430 ? 28.328 -21.920 -4.129  1.00 8.57   ? 486 SER B CA  1 
ATOM   3238 C C   . SER A 1 430 ? 26.898 -21.550 -3.750  1.00 9.36   ? 486 SER B C   1 
ATOM   3239 O O   . SER A 1 430 ? 26.248 -20.784 -4.457  1.00 3.89   ? 486 SER B O   1 
ATOM   3240 C CB  . SER A 1 430 ? 29.311 -21.318 -3.130  1.00 7.86   ? 486 SER B CB  1 
ATOM   3241 O OG  . SER A 1 430 ? 29.315 -19.917 -3.218  1.00 9.09   ? 486 SER B OG  1 
ATOM   3242 N N   . GLU A 1 431 ? 26.396 -22.184 -2.689  1.00 9.75   ? 487 GLU B N   1 
ATOM   3243 C CA  . GLU A 1 431 ? 25.076 -21.897 -2.119  1.00 3.73   ? 487 GLU B CA  1 
ATOM   3244 C C   . GLU A 1 431 ? 23.952 -22.056 -3.120  1.00 3.57   ? 487 GLU B C   1 
ATOM   3245 O O   . GLU A 1 431 ? 23.273 -21.091 -3.473  1.00 7.09   ? 487 GLU B O   1 
ATOM   3246 C CB  . GLU A 1 431 ? 25.039 -20.511 -1.464  1.00 3.50   ? 487 GLU B CB  1 
ATOM   3247 C CG  . GLU A 1 431 ? 25.265 -20.529 0.028   1.00 35.14  ? 487 GLU B CG  1 
ATOM   3248 C CD  . GLU A 1 431 ? 25.565 -19.152 0.585   1.00 32.83  ? 487 GLU B CD  1 
ATOM   3249 O OE1 . GLU A 1 431 ? 25.537 -18.987 1.830   1.00 31.51  ? 487 GLU B OE1 1 
ATOM   3250 O OE2 . GLU A 1 431 ? 25.841 -18.239 -0.226  1.00 31.80  ? 487 GLU B OE2 1 
ATOM   3251 N N   . ASN A 1 432 ? 23.767 -23.293 -3.565  1.00 19.04  ? 488 ASN B N   1 
ATOM   3252 C CA  . ASN A 1 432 ? 22.719 -23.659 -4.526  1.00 18.43  ? 488 ASN B CA  1 
ATOM   3253 C C   . ASN A 1 432 ? 22.205 -25.066 -4.235  1.00 18.70  ? 488 ASN B C   1 
ATOM   3254 O O   . ASN A 1 432 ? 22.485 -25.632 -3.178  1.00 21.97  ? 488 ASN B O   1 
ATOM   3255 C CB  . ASN A 1 432 ? 23.210 -23.570 -5.984  1.00 3.81   ? 488 ASN B CB  1 
ATOM   3256 C CG  . ASN A 1 432 ? 23.130 -22.159 -6.547  1.00 25.02  ? 488 ASN B CG  1 
ATOM   3257 O OD1 . ASN A 1 432 ? 22.056 -21.664 -6.846  1.00 3.31   ? 488 ASN B OD1 1 
ATOM   3258 N ND2 . ASN A 1 432 ? 24.269 -21.519 -6.706  1.00 3.70   ? 488 ASN B ND2 1 
ATOM   3259 N N   . ARG A 1 433 ? 21.410 -25.589 -5.157  1.00 3.80   ? 489 ARG B N   1 
ATOM   3260 C CA  . ARG A 1 433 ? 20.877 -26.948 -5.096  1.00 3.96   ? 489 ARG B CA  1 
ATOM   3261 C C   . ARG A 1 433 ? 21.571 -28.016 -5.954  1.00 22.14  ? 489 ARG B C   1 
ATOM   3262 O O   . ARG A 1 433 ? 21.001 -29.095 -6.142  1.00 26.18  ? 489 ARG B O   1 
ATOM   3263 C CB  . ARG A 1 433 ? 19.388 -26.940 -5.376  1.00 9.18   ? 489 ARG B CB  1 
ATOM   3264 C CG  . ARG A 1 433 ? 18.656 -25.932 -4.541  1.00 3.36   ? 489 ARG B CG  1 
ATOM   3265 C CD  . ARG A 1 433 ? 18.620 -26.319 -3.086  1.00 10.92  ? 489 ARG B CD  1 
ATOM   3266 N NE  . ARG A 1 433 ? 17.264 -26.096 -2.601  1.00 23.00  ? 489 ARG B NE  1 
ATOM   3267 C CZ  . ARG A 1 433 ? 16.815 -24.913 -2.198  1.00 26.82  ? 489 ARG B CZ  1 
ATOM   3268 N NH1 . ARG A 1 433 ? 17.638 -23.869 -2.204  1.00 30.29  ? 489 ARG B NH1 1 
ATOM   3269 N NH2 . ARG A 1 433 ? 15.560 -24.774 -1.781  1.00 18.05  ? 489 ARG B NH2 1 
ATOM   3270 N N   . LEU A 1 434 ? 22.735 -27.693 -6.529  1.00 19.53  ? 490 LEU B N   1 
ATOM   3271 C CA  . LEU A 1 434 ? 23.404 -28.535 -7.531  1.00 4.92   ? 490 LEU B CA  1 
ATOM   3272 C C   . LEU A 1 434 ? 23.574 -29.972 -7.071  1.00 16.39  ? 490 LEU B C   1 
ATOM   3273 O O   . LEU A 1 434 ? 23.766 -30.222 -5.881  1.00 18.79  ? 490 LEU B O   1 
ATOM   3274 C CB  . LEU A 1 434 ? 24.800 -28.000 -7.837  1.00 5.11   ? 490 LEU B CB  1 
ATOM   3275 C CG  . LEU A 1 434 ? 25.013 -26.596 -8.387  1.00 4.91   ? 490 LEU B CG  1 
ATOM   3276 C CD1 . LEU A 1 434 ? 26.493 -26.371 -8.562  1.00 5.18   ? 490 LEU B CD1 1 
ATOM   3277 C CD2 . LEU A 1 434 ? 24.298 -26.376 -9.701  1.00 4.82   ? 490 LEU B CD2 1 
ATOM   3278 N N   . VAL A 1 435 ? 23.502 -30.919 -8.010  1.00 15.94  ? 491 VAL B N   1 
ATOM   3279 C CA  . VAL A 1 435 ? 23.688 -32.337 -7.673  1.00 19.63  ? 491 VAL B CA  1 
ATOM   3280 C C   . VAL A 1 435 ? 24.707 -33.073 -8.536  1.00 13.94  ? 491 VAL B C   1 
ATOM   3281 O O   . VAL A 1 435 ? 25.419 -32.471 -9.330  1.00 23.40  ? 491 VAL B O   1 
ATOM   3282 C CB  . VAL A 1 435 ? 22.366 -33.124 -7.670  1.00 5.78   ? 491 VAL B CB  1 
ATOM   3283 C CG1 . VAL A 1 435 ? 21.499 -32.689 -6.516  1.00 5.41   ? 491 VAL B CG1 1 
ATOM   3284 C CG2 . VAL A 1 435 ? 21.655 -32.927 -8.971  1.00 6.41   ? 491 VAL B CG2 1 
ATOM   3285 N N   . GLY A 1 436 ? 24.795 -34.382 -8.332  1.00 11.48  ? 492 GLY B N   1 
ATOM   3286 C CA  . GLY A 1 436 ? 25.709 -35.222 -9.078  1.00 15.80  ? 492 GLY B CA  1 
ATOM   3287 C C   . GLY A 1 436 ? 27.175 -34.971 -8.798  1.00 9.49   ? 492 GLY B C   1 
ATOM   3288 O O   . GLY A 1 436 ? 27.535 -34.165 -7.952  1.00 10.47  ? 492 GLY B O   1 
ATOM   3289 N N   . SER A 1 437 ? 28.027 -35.679 -9.525  1.00 15.79  ? 493 SER B N   1 
ATOM   3290 C CA  . SER A 1 437 ? 29.467 -35.526 -9.417  1.00 8.07   ? 493 SER B CA  1 
ATOM   3291 C C   . SER A 1 437 ? 29.964 -34.245 -10.071 1.00 15.85  ? 493 SER B C   1 
ATOM   3292 O O   . SER A 1 437 ? 29.273 -33.635 -10.869 1.00 15.83  ? 493 SER B O   1 
ATOM   3293 C CB  . SER A 1 437 ? 30.145 -36.724 -10.054 1.00 14.30  ? 493 SER B CB  1 
ATOM   3294 O OG  . SER A 1 437 ? 29.622 -37.920 -9.515  1.00 22.47  ? 493 SER B OG  1 
ATOM   3295 N N   . ILE A 1 438 ? 31.161 -33.816 -9.703  1.00 23.29  ? 494 ILE B N   1 
ATOM   3296 C CA  . ILE A 1 438 ? 31.814 -32.731 -10.414 1.00 23.00  ? 494 ILE B CA  1 
ATOM   3297 C C   . ILE A 1 438 ? 32.355 -33.301 -11.724 1.00 33.02  ? 494 ILE B C   1 
ATOM   3298 O O   . ILE A 1 438 ? 33.171 -34.232 -11.706 1.00 36.92  ? 494 ILE B O   1 
ATOM   3299 C CB  . ILE A 1 438 ? 32.959 -32.144 -9.585  1.00 19.45  ? 494 ILE B CB  1 
ATOM   3300 C CG1 . ILE A 1 438 ? 32.403 -31.476 -8.319  1.00 23.87  ? 494 ILE B CG1 1 
ATOM   3301 C CG2 . ILE A 1 438 ? 33.775 -31.167 -10.420 1.00 15.32  ? 494 ILE B CG2 1 
ATOM   3302 C CD1 . ILE A 1 438 ? 33.466 -31.021 -7.339  1.00 27.69  ? 494 ILE B CD1 1 
ATOM   3303 N N   . PRO A 1 439 ? 31.884 -32.763 -12.866 1.00 31.98  ? 495 PRO B N   1 
ATOM   3304 C CA  . PRO A 1 439 ? 32.196 -33.299 -14.204 1.00 24.68  ? 495 PRO B CA  1 
ATOM   3305 C C   . PRO A 1 439 ? 33.681 -33.234 -14.573 1.00 19.92  ? 495 PRO B C   1 
ATOM   3306 O O   . PRO A 1 439 ? 34.253 -32.140 -14.586 1.00 17.24  ? 495 PRO B O   1 
ATOM   3307 C CB  . PRO A 1 439 ? 31.402 -32.376 -15.135 1.00 26.34  ? 495 PRO B CB  1 
ATOM   3308 C CG  . PRO A 1 439 ? 31.242 -31.101 -14.359 1.00 30.77  ? 495 PRO B CG  1 
ATOM   3309 C CD  . PRO A 1 439 ? 31.073 -31.536 -12.935 1.00 31.09  ? 495 PRO B CD  1 
ATOM   3310 N N   . PRO A 1 440 ? 34.278 -34.377 -14.956 1.00 9.80   ? 496 PRO B N   1 
ATOM   3311 C CA  . PRO A 1 440 ? 35.718 -34.447 -15.222 1.00 16.50  ? 496 PRO B CA  1 
ATOM   3312 C C   . PRO A 1 440 ? 36.139 -33.510 -16.343 1.00 15.06  ? 496 PRO B C   1 
ATOM   3313 O O   . PRO A 1 440 ? 37.323 -33.208 -16.492 1.00 13.93  ? 496 PRO B O   1 
ATOM   3314 C CB  . PRO A 1 440 ? 35.928 -35.903 -15.639 1.00 11.02  ? 496 PRO B CB  1 
ATOM   3315 C CG  . PRO A 1 440 ? 34.801 -36.631 -15.052 1.00 10.71  ? 496 PRO B CG  1 
ATOM   3316 C CD  . PRO A 1 440 ? 33.641 -35.694 -15.096 1.00 11.72  ? 496 PRO B CD  1 
ATOM   3317 N N   . ALA A 1 441 ? 35.163 -33.053 -17.118 1.00 17.30  ? 497 ALA B N   1 
ATOM   3318 C CA  . ALA A 1 441 ? 35.415 -32.183 -18.254 1.00 10.02  ? 497 ALA B CA  1 
ATOM   3319 C C   . ALA A 1 441 ? 35.961 -30.832 -17.813 1.00 13.85  ? 497 ALA B C   1 
ATOM   3320 O O   . ALA A 1 441 ? 36.638 -30.155 -18.582 1.00 22.07  ? 497 ALA B O   1 
ATOM   3321 C CB  . ALA A 1 441 ? 34.149 -32.018 -19.093 1.00 9.69   ? 497 ALA B CB  1 
ATOM   3322 N N   . ILE A 1 442 ? 35.693 -30.446 -16.569 1.00 17.44  ? 498 ILE B N   1 
ATOM   3323 C CA  . ILE A 1 442 ? 36.218 -29.185 -16.046 1.00 19.44  ? 498 ILE B CA  1 
ATOM   3324 C C   . ILE A 1 442 ? 37.748 -29.168 -16.063 1.00 25.03  ? 498 ILE B C   1 
ATOM   3325 O O   . ILE A 1 442 ? 38.368 -28.108 -16.009 1.00 31.21  ? 498 ILE B O   1 
ATOM   3326 C CB  . ILE A 1 442 ? 35.699 -28.893 -14.627 1.00 24.11  ? 498 ILE B CB  1 
ATOM   3327 C CG1 . ILE A 1 442 ? 35.976 -27.443 -14.229 1.00 24.01  ? 498 ILE B CG1 1 
ATOM   3328 C CG2 . ILE A 1 442 ? 36.324 -29.835 -13.630 1.00 24.67  ? 498 ILE B CG2 1 
ATOM   3329 C CD1 . ILE A 1 442 ? 35.152 -26.975 -13.051 1.00 27.44  ? 498 ILE B CD1 1 
ATOM   3330 N N   . SER A 1 443 ? 38.357 -30.346 -16.178 1.00 28.22  ? 499 SER B N   1 
ATOM   3331 C CA  . SER A 1 443 ? 39.810 -30.458 -16.252 1.00 23.72  ? 499 SER B CA  1 
ATOM   3332 C C   . SER A 1 443 ? 40.346 -29.717 -17.461 1.00 17.71  ? 499 SER B C   1 
ATOM   3333 O O   . SER A 1 443 ? 41.537 -29.404 -17.523 1.00 13.21  ? 499 SER B O   1 
ATOM   3334 C CB  . SER A 1 443 ? 40.232 -31.914 -16.360 1.00 20.09  ? 499 SER B CB  1 
ATOM   3335 O OG  . SER A 1 443 ? 40.617 -32.197 -17.689 1.00 13.14  ? 499 SER B OG  1 
ATOM   3336 N N   . GLY A 1 444 ? 39.463 -29.457 -18.421 1.00 17.33  ? 500 GLY B N   1 
ATOM   3337 C CA  . GLY A 1 444 ? 39.812 -28.711 -19.610 1.00 17.77  ? 500 GLY B CA  1 
ATOM   3338 C C   . GLY A 1 444 ? 39.697 -27.203 -19.481 1.00 28.33  ? 500 GLY B C   1 
ATOM   3339 O O   . GLY A 1 444 ? 39.751 -26.492 -20.487 1.00 29.57  ? 500 GLY B O   1 
ATOM   3340 N N   . CYS A 1 445 ? 39.547 -26.687 -18.263 1.00 35.31  ? 501 CYS B N   1 
ATOM   3341 C CA  . CYS A 1 445 ? 39.577 -25.240 -18.124 1.00 35.62  ? 501 CYS B CA  1 
ATOM   3342 C C   . CYS A 1 445 ? 41.020 -24.882 -17.833 1.00 48.20  ? 501 CYS B C   1 
ATOM   3343 O O   . CYS A 1 445 ? 41.486 -24.993 -16.700 1.00 54.64  ? 501 CYS B O   1 
ATOM   3344 C CB  . CYS A 1 445 ? 38.683 -24.781 -16.972 1.00 20.83  ? 501 CYS B CB  1 
ATOM   3345 S SG  . CYS A 1 445 ? 36.903 -25.025 -17.217 1.00 19.52  ? 501 CYS B SG  1 
ATOM   3346 N N   . GLU A 1 446 ? 41.701 -24.366 -18.849 1.00 46.12  ? 502 GLU B N   1 
ATOM   3347 C CA  . GLU A 1 446 ? 43.137 -24.160 -18.774 1.00 40.56  ? 502 GLU B CA  1 
ATOM   3348 C C   . GLU A 1 446 ? 43.453 -23.027 -17.814 1.00 23.34  ? 502 GLU B C   1 
ATOM   3349 O O   . GLU A 1 446 ? 44.509 -23.001 -17.201 1.00 17.83  ? 502 GLU B O   1 
ATOM   3350 C CB  . GLU A 1 446 ? 43.697 -23.822 -20.163 1.00 55.37  ? 502 GLU B CB  1 
ATOM   3351 C CG  . GLU A 1 446 ? 43.479 -24.891 -21.224 1.00 68.84  ? 502 GLU B CG  1 
ATOM   3352 C CD  . GLU A 1 446 ? 43.929 -24.439 -22.605 1.00 77.30  ? 502 GLU B CD  1 
ATOM   3353 O OE1 . GLU A 1 446 ? 43.729 -25.197 -23.582 1.00 77.55  ? 502 GLU B OE1 1 
ATOM   3354 O OE2 . GLU A 1 446 ? 44.481 -23.322 -22.711 1.00 80.92  ? 502 GLU B OE2 1 
ATOM   3355 N N   . SER A 1 447 ? 42.532 -22.073 -17.734 1.00 21.23  ? 503 SER B N   1 
ATOM   3356 C CA  . SER A 1 447 ? 42.739 -20.819 -17.027 1.00 9.84   ? 503 SER B CA  1 
ATOM   3357 C C   . SER A 1 447 ? 42.136 -20.726 -15.628 1.00 9.41   ? 503 SER B C   1 
ATOM   3358 O O   . SER A 1 447 ? 42.229 -19.676 -14.991 1.00 11.49  ? 503 SER B O   1 
ATOM   3359 C CB  . SER A 1 447 ? 42.231 -19.664 -17.886 1.00 9.49   ? 503 SER B CB  1 
ATOM   3360 O OG  . SER A 1 447 ? 43.273 -19.199 -18.713 1.00 22.93  ? 503 SER B OG  1 
ATOM   3361 N N   . LEU A 1 448 ? 41.521 -21.801 -15.149 1.00 22.27  ? 504 LEU B N   1 
ATOM   3362 C CA  . LEU A 1 448 ? 40.698 -21.699 -13.949 1.00 19.37  ? 504 LEU B CA  1 
ATOM   3363 C C   . LEU A 1 448 ? 41.559 -21.680 -12.686 1.00 20.67  ? 504 LEU B C   1 
ATOM   3364 O O   . LEU A 1 448 ? 42.225 -22.668 -12.355 1.00 15.27  ? 504 LEU B O   1 
ATOM   3365 C CB  . LEU A 1 448 ? 39.722 -22.882 -13.915 1.00 8.74   ? 504 LEU B CB  1 
ATOM   3366 C CG  . LEU A 1 448 ? 38.689 -22.977 -12.793 1.00 16.48  ? 504 LEU B CG  1 
ATOM   3367 C CD1 . LEU A 1 448 ? 37.963 -21.660 -12.638 1.00 7.74   ? 504 LEU B CD1 1 
ATOM   3368 C CD2 . LEU A 1 448 ? 37.704 -24.112 -13.066 1.00 8.19   ? 504 LEU B CD2 1 
ATOM   3369 N N   . GLU A 1 449 ? 41.564 -20.533 -12.003 1.00 25.24  ? 505 GLU B N   1 
ATOM   3370 C CA  . GLU A 1 449 ? 42.290 -20.393 -10.741 1.00 21.74  ? 505 GLU B CA  1 
ATOM   3371 C C   . GLU A 1 449 ? 41.485 -20.401 -9.435  1.00 17.76  ? 505 GLU B C   1 
ATOM   3372 O O   . GLU A 1 449 ? 42.051 -20.649 -8.378  1.00 22.21  ? 505 GLU B O   1 
ATOM   3373 C CB  . GLU A 1 449 ? 43.164 -19.142 -10.800 1.00 16.73  ? 505 GLU B CB  1 
ATOM   3374 C CG  . GLU A 1 449 ? 44.063 -19.110 -12.017 1.00 21.38  ? 505 GLU B CG  1 
ATOM   3375 C CD  . GLU A 1 449 ? 44.743 -17.772 -12.187 1.00 35.06  ? 505 GLU B CD  1 
ATOM   3376 O OE1 . GLU A 1 449 ? 44.611 -16.927 -11.272 1.00 32.86  ? 505 GLU B OE1 1 
ATOM   3377 O OE2 . GLU A 1 449 ? 45.397 -17.562 -13.239 1.00 43.22  ? 505 GLU B OE2 1 
ATOM   3378 N N   . PHE A 1 450 ? 40.176 -20.164 -9.519  1.00 10.34  ? 506 PHE B N   1 
ATOM   3379 C CA  . PHE A 1 450 ? 39.334 -19.970 -8.337  1.00 10.56  ? 506 PHE B CA  1 
ATOM   3380 C C   . PHE A 1 450 ? 38.041 -20.738 -8.536  1.00 13.25  ? 506 PHE B C   1 
ATOM   3381 O O   . PHE A 1 450 ? 37.277 -20.425 -9.447  1.00 17.04  ? 506 PHE B O   1 
ATOM   3382 C CB  . PHE A 1 450 ? 39.021 -18.480 -8.132  1.00 12.81  ? 506 PHE B CB  1 
ATOM   3383 C CG  . PHE A 1 450 ? 38.280 -18.160 -6.833  1.00 20.67  ? 506 PHE B CG  1 
ATOM   3384 C CD1 . PHE A 1 450 ? 36.908 -18.368 -6.712  1.00 15.47  ? 506 PHE B CD1 1 
ATOM   3385 C CD2 . PHE A 1 450 ? 38.961 -17.627 -5.738  1.00 29.16  ? 506 PHE B CD2 1 
ATOM   3386 C CE1 . PHE A 1 450 ? 36.232 -18.056 -5.518  1.00 10.69  ? 506 PHE B CE1 1 
ATOM   3387 C CE2 . PHE A 1 450 ? 38.288 -17.312 -4.536  1.00 20.56  ? 506 PHE B CE2 1 
ATOM   3388 C CZ  . PHE A 1 450 ? 36.923 -17.532 -4.432  1.00 10.95  ? 506 PHE B CZ  1 
ATOM   3389 N N   . LEU A 1 451 ? 37.788 -21.736 -7.691  1.00 9.05   ? 507 LEU B N   1 
ATOM   3390 C CA  . LEU A 1 451 ? 36.593 -22.549 -7.850  1.00 12.48  ? 507 LEU B CA  1 
ATOM   3391 C C   . LEU A 1 451 ? 35.893 -22.740 -6.517  1.00 17.84  ? 507 LEU B C   1 
ATOM   3392 O O   . LEU A 1 451 ? 36.395 -23.444 -5.645  1.00 25.65  ? 507 LEU B O   1 
ATOM   3393 C CB  . LEU A 1 451 ? 36.946 -23.908 -8.469  1.00 7.52   ? 507 LEU B CB  1 
ATOM   3394 C CG  . LEU A 1 451 ? 35.788 -24.868 -8.779  1.00 10.96  ? 507 LEU B CG  1 
ATOM   3395 C CD1 . LEU A 1 451 ? 34.776 -24.250 -9.711  1.00 6.99   ? 507 LEU B CD1 1 
ATOM   3396 C CD2 . LEU A 1 451 ? 36.268 -26.193 -9.338  1.00 7.82   ? 507 LEU B CD2 1 
ATOM   3397 N N   . ASP A 1 452 ? 34.710 -22.151 -6.374  1.00 15.32  ? 508 ASP B N   1 
ATOM   3398 C CA  . ASP A 1 452 ? 33.963 -22.291 -5.136  1.00 14.19  ? 508 ASP B CA  1 
ATOM   3399 C C   . ASP A 1 452 ? 32.595 -22.941 -5.369  1.00 17.91  ? 508 ASP B C   1 
ATOM   3400 O O   . ASP A 1 452 ? 31.683 -22.332 -5.927  1.00 31.18  ? 508 ASP B O   1 
ATOM   3401 C CB  . ASP A 1 452 ? 33.820 -20.926 -4.463  1.00 12.29  ? 508 ASP B CB  1 
ATOM   3402 C CG  . ASP A 1 452 ? 33.017 -20.987 -3.191  1.00 23.04  ? 508 ASP B CG  1 
ATOM   3403 O OD1 . ASP A 1 452 ? 32.988 -22.059 -2.552  1.00 29.81  ? 508 ASP B OD1 1 
ATOM   3404 O OD2 . ASP A 1 452 ? 32.411 -19.955 -2.834  1.00 26.88  ? 508 ASP B OD2 1 
ATOM   3405 N N   . LEU A 1 453 ? 32.492 -24.195 -4.947  1.00 9.82   ? 509 LEU B N   1 
ATOM   3406 C CA  . LEU A 1 453 ? 31.271 -24.982 -4.999  1.00 5.83   ? 509 LEU B CA  1 
ATOM   3407 C C   . LEU A 1 453 ? 30.533 -25.154 -3.669  1.00 5.61   ? 509 LEU B C   1 
ATOM   3408 O O   . LEU A 1 453 ? 29.635 -25.987 -3.564  1.00 11.48  ? 509 LEU B O   1 
ATOM   3409 C CB  . LEU A 1 453 ? 31.536 -26.328 -5.669  1.00 13.05  ? 509 LEU B CB  1 
ATOM   3410 C CG  . LEU A 1 453 ? 32.122 -26.208 -7.082  1.00 17.04  ? 509 LEU B CG  1 
ATOM   3411 C CD1 . LEU A 1 453 ? 32.337 -27.578 -7.698  1.00 19.34  ? 509 LEU B CD1 1 
ATOM   3412 C CD2 . LEU A 1 453 ? 31.228 -25.354 -7.973  1.00 22.95  ? 509 LEU B CD2 1 
ATOM   3413 N N   . HIS A 1 454 ? 30.951 -24.444 -2.629  1.00 5.55   ? 510 HIS B N   1 
ATOM   3414 C CA  . HIS A 1 454 ? 30.467 -24.756 -1.283  1.00 6.89   ? 510 HIS B CA  1 
ATOM   3415 C C   . HIS A 1 454 ? 28.957 -24.630 -1.070  1.00 8.14   ? 510 HIS B C   1 
ATOM   3416 O O   . HIS A 1 454 ? 28.274 -23.914 -1.795  1.00 14.37  ? 510 HIS B O   1 
ATOM   3417 C CB  . HIS A 1 454 ? 31.256 -24.002 -0.211  1.00 5.48   ? 510 HIS B CB  1 
ATOM   3418 C CG  . HIS A 1 454 ? 30.790 -22.599 0.038   1.00 5.12   ? 510 HIS B CG  1 
ATOM   3419 N ND1 . HIS A 1 454 ? 29.574 -22.308 0.606   1.00 4.76   ? 510 HIS B ND1 1 
ATOM   3420 C CD2 . HIS A 1 454 ? 31.417 -21.412 -0.144  1.00 5.11   ? 510 HIS B CD2 1 
ATOM   3421 C CE1 . HIS A 1 454 ? 29.454 -20.995 0.738   1.00 4.54   ? 510 HIS B CE1 1 
ATOM   3422 N NE2 . HIS A 1 454 ? 30.559 -20.433 0.295   1.00 4.74   ? 510 HIS B NE2 1 
ATOM   3423 N N   . THR A 1 455 ? 28.445 -25.368 -0.088  1.00 8.50   ? 511 THR B N   1 
ATOM   3424 C CA  . THR A 1 455 ? 27.016 -25.377 0.224   1.00 4.65   ? 511 THR B CA  1 
ATOM   3425 C C   . THR A 1 455 ? 26.206 -25.759 -1.007  1.00 4.57   ? 511 THR B C   1 
ATOM   3426 O O   . THR A 1 455 ? 25.534 -24.949 -1.619  1.00 4.31   ? 511 THR B O   1 
ATOM   3427 C CB  . THR A 1 455 ? 26.530 -24.052 0.921   1.00 15.05  ? 511 THR B CB  1 
ATOM   3428 O OG1 . THR A 1 455 ? 27.225 -23.891 2.161   1.00 4.42   ? 511 THR B OG1 1 
ATOM   3429 C CG2 . THR A 1 455 ? 25.048 -24.093 1.240   1.00 3.98   ? 511 THR B CG2 1 
ATOM   3430 N N   . ASN A 1 456 ? 26.318 -27.019 -1.383  1.00 18.90  ? 512 ASN B N   1 
ATOM   3431 C CA  . ASN A 1 456 ? 25.518 -27.566 -2.457  1.00 8.31   ? 512 ASN B CA  1 
ATOM   3432 C C   . ASN A 1 456 ? 25.197 -29.000 -2.095  1.00 15.45  ? 512 ASN B C   1 
ATOM   3433 O O   . ASN A 1 456 ? 25.612 -29.499 -1.048  1.00 26.51  ? 512 ASN B O   1 
ATOM   3434 C CB  . ASN A 1 456 ? 26.289 -27.511 -3.785  1.00 10.81  ? 512 ASN B CB  1 
ATOM   3435 C CG  . ASN A 1 456 ? 25.971 -26.272 -4.602  1.00 12.86  ? 512 ASN B CG  1 
ATOM   3436 O OD1 . ASN A 1 456 ? 24.813 -25.979 -4.858  1.00 20.31  ? 512 ASN B OD1 1 
ATOM   3437 N ND2 . ASN A 1 456 ? 26.997 -25.545 -5.018  1.00 4.90   ? 512 ASN B ND2 1 
ATOM   3438 N N   . SER A 1 457 ? 24.461 -29.663 -2.967  1.00 14.88  ? 513 SER B N   1 
ATOM   3439 C CA  . SER A 1 457 ? 24.126 -31.069 -2.790  1.00 14.79  ? 513 SER B CA  1 
ATOM   3440 C C   . SER A 1 457 ? 25.078 -32.040 -3.499  1.00 14.52  ? 513 SER B C   1 
ATOM   3441 O O   . SER A 1 457 ? 24.772 -33.220 -3.608  1.00 20.15  ? 513 SER B O   1 
ATOM   3442 C CB  . SER A 1 457 ? 22.664 -31.328 -3.133  1.00 24.18  ? 513 SER B CB  1 
ATOM   3443 O OG  . SER A 1 457 ? 21.841 -30.490 -2.332  1.00 29.32  ? 513 SER B OG  1 
ATOM   3444 N N   . LEU A 1 458 ? 26.208 -31.540 -3.996  1.00 5.86   ? 514 LEU B N   1 
ATOM   3445 C CA  . LEU A 1 458 ? 27.166 -32.368 -4.747  1.00 17.68  ? 514 LEU B CA  1 
ATOM   3446 C C   . LEU A 1 458 ? 27.545 -33.674 -4.046  1.00 25.85  ? 514 LEU B C   1 
ATOM   3447 O O   . LEU A 1 458 ? 27.682 -33.716 -2.831  1.00 33.34  ? 514 LEU B O   1 
ATOM   3448 C CB  . LEU A 1 458 ? 28.460 -31.591 -5.002  1.00 12.37  ? 514 LEU B CB  1 
ATOM   3449 C CG  . LEU A 1 458 ? 28.437 -30.409 -5.962  1.00 10.28  ? 514 LEU B CG  1 
ATOM   3450 C CD1 . LEU A 1 458 ? 29.804 -29.753 -6.006  1.00 12.12  ? 514 LEU B CD1 1 
ATOM   3451 C CD2 . LEU A 1 458 ? 28.041 -30.908 -7.321  1.00 10.82  ? 514 LEU B CD2 1 
ATOM   3452 N N   . SER A 1 459 ? 27.715 -34.739 -4.825  1.00 24.89  ? 515 SER B N   1 
ATOM   3453 C CA  . SER A 1 459 ? 28.093 -36.038 -4.273  1.00 18.64  ? 515 SER B CA  1 
ATOM   3454 C C   . SER A 1 459 ? 29.115 -36.751 -5.140  1.00 20.84  ? 515 SER B C   1 
ATOM   3455 O O   . SER A 1 459 ? 29.715 -36.158 -6.037  1.00 22.06  ? 515 SER B O   1 
ATOM   3456 C CB  . SER A 1 459 ? 26.874 -36.937 -4.067  1.00 13.98  ? 515 SER B CB  1 
ATOM   3457 O OG  . SER A 1 459 ? 26.262 -37.284 -5.295  1.00 7.34   ? 515 SER B OG  1 
ATOM   3458 N N   . GLY A 1 460 ? 29.339 -38.022 -4.834  1.00 24.81  ? 516 GLY B N   1 
ATOM   3459 C CA  . GLY A 1 460 ? 30.259 -38.834 -5.603  1.00 31.37  ? 516 GLY B CA  1 
ATOM   3460 C C   . GLY A 1 460 ? 31.670 -38.729 -5.070  1.00 35.65  ? 516 GLY B C   1 
ATOM   3461 O O   . GLY A 1 460 ? 31.890 -38.254 -3.950  1.00 36.91  ? 516 GLY B O   1 
ATOM   3462 N N   . SER A 1 461 ? 32.626 -39.168 -5.884  1.00 31.31  ? 517 SER B N   1 
ATOM   3463 C CA  . SER A 1 461 ? 34.023 -39.229 -5.480  1.00 19.31  ? 517 SER B CA  1 
ATOM   3464 C C   . SER A 1 461 ? 34.873 -38.162 -6.186  1.00 15.81  ? 517 SER B C   1 
ATOM   3465 O O   . SER A 1 461 ? 34.818 -38.003 -7.398  1.00 24.15  ? 517 SER B O   1 
ATOM   3466 C CB  . SER A 1 461 ? 34.573 -40.629 -5.769  1.00 17.85  ? 517 SER B CB  1 
ATOM   3467 O OG  . SER A 1 461 ? 35.707 -40.922 -4.971  1.00 27.08  ? 517 SER B OG  1 
ATOM   3468 N N   . LEU A 1 462 ? 35.669 -37.435 -5.417  1.00 15.92  ? 518 LEU B N   1 
ATOM   3469 C CA  . LEU A 1 462 ? 36.586 -36.456 -5.983  1.00 25.44  ? 518 LEU B CA  1 
ATOM   3470 C C   . LEU A 1 462 ? 37.667 -37.190 -6.798  1.00 26.41  ? 518 LEU B C   1 
ATOM   3471 O O   . LEU A 1 462 ? 37.801 -38.405 -6.691  1.00 28.40  ? 518 LEU B O   1 
ATOM   3472 C CB  . LEU A 1 462 ? 37.211 -35.618 -4.861  1.00 33.33  ? 518 LEU B CB  1 
ATOM   3473 C CG  . LEU A 1 462 ? 37.417 -34.120 -5.097  1.00 34.85  ? 518 LEU B CG  1 
ATOM   3474 C CD1 . LEU A 1 462 ? 36.073 -33.416 -5.199  1.00 39.38  ? 518 LEU B CD1 1 
ATOM   3475 C CD2 . LEU A 1 462 ? 38.263 -33.516 -3.992  1.00 32.30  ? 518 LEU B CD2 1 
ATOM   3476 N N   . LEU A 1 463 ? 38.383 -36.474 -7.659  1.00 27.75  ? 519 LEU B N   1 
ATOM   3477 C CA  . LEU A 1 463 ? 39.510 -37.059 -8.390  1.00 43.32  ? 519 LEU B CA  1 
ATOM   3478 C C   . LEU A 1 463 ? 40.563 -35.992 -8.692  1.00 55.35  ? 519 LEU B C   1 
ATOM   3479 O O   . LEU A 1 463 ? 40.234 -34.840 -8.987  1.00 59.55  ? 519 LEU B O   1 
ATOM   3480 C CB  . LEU A 1 463 ? 39.064 -37.723 -9.712  1.00 37.93  ? 519 LEU B CB  1 
ATOM   3481 C CG  . LEU A 1 463 ? 38.673 -39.203 -9.864  1.00 24.44  ? 519 LEU B CG  1 
ATOM   3482 C CD1 . LEU A 1 463 ? 39.270 -40.094 -8.770  1.00 23.10  ? 519 LEU B CD1 1 
ATOM   3483 C CD2 . LEU A 1 463 ? 37.158 -39.371 -9.943  1.00 16.82  ? 519 LEU B CD2 1 
ATOM   3484 N N   . GLY A 1 464 ? 41.829 -36.382 -8.641  1.00 56.87  ? 520 GLY B N   1 
ATOM   3485 C CA  . GLY A 1 464 ? 42.903 -35.466 -8.966  1.00 58.88  ? 520 GLY B CA  1 
ATOM   3486 C C   . GLY A 1 464 ? 42.994 -35.185 -10.454 1.00 56.31  ? 520 GLY B C   1 
ATOM   3487 O O   . GLY A 1 464 ? 43.581 -34.181 -10.857 1.00 52.91  ? 520 GLY B O   1 
ATOM   3488 N N   . THR A 1 465 ? 42.421 -36.073 -11.268 1.00 59.50  ? 521 THR B N   1 
ATOM   3489 C CA  . THR A 1 465 ? 42.463 -35.933 -12.733 1.00 58.31  ? 521 THR B CA  1 
ATOM   3490 C C   . THR A 1 465 ? 41.312 -35.066 -13.238 1.00 42.55  ? 521 THR B C   1 
ATOM   3491 O O   . THR A 1 465 ? 41.222 -34.757 -14.420 1.00 30.59  ? 521 THR B O   1 
ATOM   3492 C CB  . THR A 1 465 ? 42.405 -37.305 -13.465 1.00 62.30  ? 521 THR B CB  1 
ATOM   3493 O OG1 . THR A 1 465 ? 41.077 -37.544 -13.953 1.00 62.34  ? 521 THR B OG1 1 
ATOM   3494 C CG2 . THR A 1 465 ? 42.843 -38.448 -12.539 1.00 60.56  ? 521 THR B CG2 1 
ATOM   3495 N N   . THR A 1 466 ? 40.436 -34.687 -12.317 1.00 37.49  ? 522 THR B N   1 
ATOM   3496 C CA  . THR A 1 466 ? 39.252 -33.910 -12.630 1.00 23.34  ? 522 THR B CA  1 
ATOM   3497 C C   . THR A 1 466 ? 39.548 -32.412 -12.502 1.00 28.52  ? 522 THR B C   1 
ATOM   3498 O O   . THR A 1 466 ? 38.748 -31.572 -12.899 1.00 36.46  ? 522 THR B O   1 
ATOM   3499 C CB  . THR A 1 466 ? 38.113 -34.331 -11.676 1.00 18.02  ? 522 THR B CB  1 
ATOM   3500 O OG1 . THR A 1 466 ? 37.900 -35.742 -11.790 1.00 15.36  ? 522 THR B OG1 1 
ATOM   3501 C CG2 . THR A 1 466 ? 36.819 -33.623 -11.985 1.00 25.79  ? 522 THR B CG2 1 
ATOM   3502 N N   . LEU A 1 467 ? 40.708 -32.071 -11.953 1.00 22.29  ? 523 LEU B N   1 
ATOM   3503 C CA  . LEU A 1 467 ? 40.997 -30.675 -11.660 1.00 23.57  ? 523 LEU B CA  1 
ATOM   3504 C C   . LEU A 1 467 ? 42.096 -30.046 -12.520 1.00 31.00  ? 523 LEU B C   1 
ATOM   3505 O O   . LEU A 1 467 ? 43.205 -30.578 -12.603 1.00 36.47  ? 523 LEU B O   1 
ATOM   3506 C CB  . LEU A 1 467 ? 41.292 -30.496 -10.168 1.00 31.17  ? 523 LEU B CB  1 
ATOM   3507 C CG  . LEU A 1 467 ? 40.188 -30.960 -9.203  1.00 33.90  ? 523 LEU B CG  1 
ATOM   3508 C CD1 . LEU A 1 467 ? 40.676 -30.917 -7.755  1.00 31.30  ? 523 LEU B CD1 1 
ATOM   3509 C CD2 . LEU A 1 467 ? 38.898 -30.142 -9.373  1.00 29.65  ? 523 LEU B CD2 1 
ATOM   3510 N N   . PRO A 1 468 ? 41.787 -28.915 -13.177 1.00 26.81  ? 524 PRO B N   1 
ATOM   3511 C CA  . PRO A 1 468 ? 42.840 -28.138 -13.832 1.00 18.15  ? 524 PRO B CA  1 
ATOM   3512 C C   . PRO A 1 468 ? 43.966 -27.793 -12.874 1.00 16.75  ? 524 PRO B C   1 
ATOM   3513 O O   . PRO A 1 468 ? 43.731 -27.330 -11.760 1.00 24.36  ? 524 PRO B O   1 
ATOM   3514 C CB  . PRO A 1 468 ? 42.122 -26.862 -14.277 1.00 10.60  ? 524 PRO B CB  1 
ATOM   3515 C CG  . PRO A 1 468 ? 40.782 -26.901 -13.640 1.00 30.09  ? 524 PRO B CG  1 
ATOM   3516 C CD  . PRO A 1 468 ? 40.459 -28.334 -13.417 1.00 26.57  ? 524 PRO B CD  1 
ATOM   3517 N N   . LYS A 1 469 ? 45.186 -27.989 -13.349 1.00 19.13  ? 525 LYS B N   1 
ATOM   3518 C CA  . LYS A 1 469 ? 46.398 -27.889 -12.545 1.00 24.51  ? 525 LYS B CA  1 
ATOM   3519 C C   . LYS A 1 469 ? 46.752 -26.455 -12.114 1.00 22.96  ? 525 LYS B C   1 
ATOM   3520 O O   . LYS A 1 469 ? 47.667 -26.240 -11.315 1.00 19.89  ? 525 LYS B O   1 
ATOM   3521 C CB  . LYS A 1 469 ? 47.563 -28.522 -13.322 1.00 21.19  ? 525 LYS B CB  1 
ATOM   3522 C CG  . LYS A 1 469 ? 47.718 -30.035 -13.125 1.00 23.55  ? 525 LYS B CG  1 
ATOM   3523 C CD  . LYS A 1 469 ? 46.393 -30.796 -13.189 1.00 24.71  ? 525 LYS B CD  1 
ATOM   3524 C CE  . LYS A 1 469 ? 46.496 -32.128 -12.472 1.00 33.94  ? 525 LYS B CE  1 
ATOM   3525 N NZ  . LYS A 1 469 ? 45.395 -33.047 -12.848 1.00 42.36  ? 525 LYS B NZ  1 
ATOM   3526 N N   . SER A 1 470 ? 46.019 -25.484 -12.648 1.00 19.50  ? 526 SER B N   1 
ATOM   3527 C CA  . SER A 1 470 ? 46.307 -24.068 -12.429 1.00 17.44  ? 526 SER B CA  1 
ATOM   3528 C C   . SER A 1 470 ? 45.501 -23.458 -11.288 1.00 17.95  ? 526 SER B C   1 
ATOM   3529 O O   . SER A 1 470 ? 45.548 -22.241 -11.072 1.00 10.86  ? 526 SER B O   1 
ATOM   3530 C CB  . SER A 1 470 ? 46.072 -23.271 -13.723 1.00 15.40  ? 526 SER B CB  1 
ATOM   3531 O OG  . SER A 1 470 ? 44.742 -23.425 -14.189 1.00 14.09  ? 526 SER B OG  1 
ATOM   3532 N N   . LEU A 1 471 ? 44.747 -24.302 -10.583 1.00 14.18  ? 527 LEU B N   1 
ATOM   3533 C CA  . LEU A 1 471 ? 43.859 -23.840 -9.519  1.00 15.32  ? 527 LEU B CA  1 
ATOM   3534 C C   . LEU A 1 471 ? 44.620 -23.296 -8.311  1.00 16.31  ? 527 LEU B C   1 
ATOM   3535 O O   . LEU A 1 471 ? 45.485 -23.963 -7.751  1.00 11.14  ? 527 LEU B O   1 
ATOM   3536 C CB  . LEU A 1 471 ? 42.903 -24.959 -9.102  1.00 9.97   ? 527 LEU B CB  1 
ATOM   3537 C CG  . LEU A 1 471 ? 41.610 -24.963 -9.924  1.00 30.55  ? 527 LEU B CG  1 
ATOM   3538 C CD1 . LEU A 1 471 ? 40.831 -26.268 -9.815  1.00 9.50   ? 527 LEU B CD1 1 
ATOM   3539 C CD2 . LEU A 1 471 ? 40.745 -23.777 -9.501  1.00 26.91  ? 527 LEU B CD2 1 
ATOM   3540 N N   . LYS A 1 472 ? 44.342 -22.040 -7.978  1.00 17.49  ? 528 LYS B N   1 
ATOM   3541 C CA  . LYS A 1 472 ? 44.838 -21.428 -6.757  1.00 23.23  ? 528 LYS B CA  1 
ATOM   3542 C C   . LYS A 1 472 ? 43.943 -21.689 -5.540  1.00 31.54  ? 528 LYS B C   1 
ATOM   3543 O O   . LYS A 1 472 ? 44.428 -21.787 -4.412  1.00 32.99  ? 528 LYS B O   1 
ATOM   3544 C CB  . LYS A 1 472 ? 45.048 -19.924 -6.960  1.00 21.74  ? 528 LYS B CB  1 
ATOM   3545 C CG  . LYS A 1 472 ? 46.103 -19.566 -8.003  1.00 17.57  ? 528 LYS B CG  1 
ATOM   3546 C CD  . LYS A 1 472 ? 46.467 -18.087 -7.930  1.00 13.88  ? 528 LYS B CD  1 
ATOM   3547 C CE  . LYS A 1 472 ? 47.338 -17.651 -9.107  1.00 15.38  ? 528 LYS B CE  1 
ATOM   3548 N NZ  . LYS A 1 472 ? 48.610 -18.434 -9.226  1.00 12.10  ? 528 LYS B NZ  1 
ATOM   3549 N N   . PHE A 1 473 ? 42.634 -21.769 -5.783  1.00 35.67  ? 529 PHE B N   1 
ATOM   3550 C CA  . PHE A 1 473 ? 41.632 -21.730 -4.715  1.00 8.55   ? 529 PHE B CA  1 
ATOM   3551 C C   . PHE A 1 473 ? 40.463 -22.698 -4.943  1.00 8.30   ? 529 PHE B C   1 
ATOM   3552 O O   . PHE A 1 473 ? 39.756 -22.594 -5.934  1.00 8.07   ? 529 PHE B O   1 
ATOM   3553 C CB  . PHE A 1 473 ? 41.127 -20.292 -4.591  1.00 16.71  ? 529 PHE B CB  1 
ATOM   3554 C CG  . PHE A 1 473 ? 40.122 -20.082 -3.504  1.00 28.41  ? 529 PHE B CG  1 
ATOM   3555 C CD1 . PHE A 1 473 ? 38.786 -20.419 -3.690  1.00 31.84  ? 529 PHE B CD1 1 
ATOM   3556 C CD2 . PHE A 1 473 ? 40.496 -19.518 -2.304  1.00 33.80  ? 529 PHE B CD2 1 
ATOM   3557 C CE1 . PHE A 1 473 ? 37.853 -20.222 -2.691  1.00 24.03  ? 529 PHE B CE1 1 
ATOM   3558 C CE2 . PHE A 1 473 ? 39.561 -19.319 -1.298  1.00 24.70  ? 529 PHE B CE2 1 
ATOM   3559 C CZ  . PHE A 1 473 ? 38.241 -19.672 -1.496  1.00 12.53  ? 529 PHE B CZ  1 
ATOM   3560 N N   . ILE A 1 474 ? 40.240 -23.606 -3.995  1.00 25.56  ? 530 ILE B N   1 
ATOM   3561 C CA  . ILE A 1 474 ? 39.185 -24.615 -4.102  1.00 8.15   ? 530 ILE B CA  1 
ATOM   3562 C C   . ILE A 1 474 ? 38.369 -24.729 -2.822  1.00 25.37  ? 530 ILE B C   1 
ATOM   3563 O O   . ILE A 1 474 ? 38.926 -25.047 -1.775  1.00 31.30  ? 530 ILE B O   1 
ATOM   3564 C CB  . ILE A 1 474 ? 39.789 -26.003 -4.323  1.00 22.82  ? 530 ILE B CB  1 
ATOM   3565 C CG1 . ILE A 1 474 ? 40.509 -26.088 -5.667  1.00 15.95  ? 530 ILE B CG1 1 
ATOM   3566 C CG2 . ILE A 1 474 ? 38.718 -27.091 -4.208  1.00 23.09  ? 530 ILE B CG2 1 
ATOM   3567 C CD1 . ILE A 1 474 ? 41.230 -27.404 -5.857  1.00 16.04  ? 530 ILE B CD1 1 
ATOM   3568 N N   . ASP A 1 475 ? 37.070 -24.432 -2.886  1.00 20.99  ? 531 ASP B N   1 
ATOM   3569 C CA  . ASP A 1 475 ? 36.177 -24.701 -1.758  1.00 14.64  ? 531 ASP B CA  1 
ATOM   3570 C C   . ASP A 1 475 ? 35.039 -25.625 -2.164  1.00 11.65  ? 531 ASP B C   1 
ATOM   3571 O O   . ASP A 1 475 ? 34.114 -25.197 -2.837  1.00 9.32   ? 531 ASP B O   1 
ATOM   3572 C CB  . ASP A 1 475 ? 35.595 -23.377 -1.271  1.00 15.37  ? 531 ASP B CB  1 
ATOM   3573 C CG  . ASP A 1 475 ? 34.842 -23.502 0.051   1.00 14.23  ? 531 ASP B CG  1 
ATOM   3574 O OD1 . ASP A 1 475 ? 34.571 -24.631 0.504   1.00 10.49  ? 531 ASP B OD1 1 
ATOM   3575 O OD2 . ASP A 1 475 ? 34.505 -22.448 0.634   1.00 14.02  ? 531 ASP B OD2 1 
ATOM   3576 N N   . PHE A 1 476 ? 35.110 -26.883 -1.738  1.00 7.14   ? 532 PHE B N   1 
ATOM   3577 C CA  . PHE A 1 476 ? 34.016 -27.853 -1.914  1.00 16.52  ? 532 PHE B CA  1 
ATOM   3578 C C   . PHE A 1 476 ? 33.184 -28.099 -0.647  1.00 12.61  ? 532 PHE B C   1 
ATOM   3579 O O   . PHE A 1 476 ? 32.428 -29.064 -0.559  1.00 6.71   ? 532 PHE B O   1 
ATOM   3580 C CB  . PHE A 1 476 ? 34.496 -29.161 -2.544  1.00 7.43   ? 532 PHE B CB  1 
ATOM   3581 C CG  . PHE A 1 476 ? 35.151 -28.983 -3.878  1.00 15.73  ? 532 PHE B CG  1 
ATOM   3582 C CD1 . PHE A 1 476 ? 34.981 -27.812 -4.602  1.00 10.58  ? 532 PHE B CD1 1 
ATOM   3583 C CD2 . PHE A 1 476 ? 35.940 -29.984 -4.411  1.00 8.17   ? 532 PHE B CD2 1 
ATOM   3584 C CE1 . PHE A 1 476 ? 35.585 -27.647 -5.827  1.00 9.70   ? 532 PHE B CE1 1 
ATOM   3585 C CE2 . PHE A 1 476 ? 36.547 -29.820 -5.627  1.00 9.44   ? 532 PHE B CE2 1 
ATOM   3586 C CZ  . PHE A 1 476 ? 36.366 -28.652 -6.339  1.00 8.15   ? 532 PHE B CZ  1 
ATOM   3587 N N   . SER A 1 477 ? 33.402 -27.281 0.369   1.00 15.96  ? 533 SER B N   1 
ATOM   3588 C CA  . SER A 1 477 ? 32.790 -27.529 1.668   1.00 18.80  ? 533 SER B CA  1 
ATOM   3589 C C   . SER A 1 477 ? 31.277 -27.579 1.630   1.00 11.93  ? 533 SER B C   1 
ATOM   3590 O O   . SER A 1 477 ? 30.633 -26.999 0.761   1.00 8.02   ? 533 SER B O   1 
ATOM   3591 C CB  . SER A 1 477 ? 33.200 -26.480 2.682   1.00 6.38   ? 533 SER B CB  1 
ATOM   3592 O OG  . SER A 1 477 ? 32.578 -25.258 2.354   1.00 12.85  ? 533 SER B OG  1 
ATOM   3593 N N   . ASP A 1 478 ? 30.727 -28.311 2.584   1.00 9.31   ? 534 ASP B N   1 
ATOM   3594 C CA  . ASP A 1 478 ? 29.288 -28.406 2.758   1.00 12.46  ? 534 ASP B CA  1 
ATOM   3595 C C   . ASP A 1 478 ? 28.627 -29.005 1.524   1.00 10.80  ? 534 ASP B C   1 
ATOM   3596 O O   . ASP A 1 478 ? 27.862 -28.348 0.821   1.00 7.55   ? 534 ASP B O   1 
ATOM   3597 C CB  . ASP A 1 478 ? 28.716 -27.030 3.106   1.00 17.22  ? 534 ASP B CB  1 
ATOM   3598 C CG  . ASP A 1 478 ? 27.299 -27.099 3.593   1.00 15.89  ? 534 ASP B CG  1 
ATOM   3599 O OD1 . ASP A 1 478 ? 26.869 -28.203 4.015   1.00 10.43  ? 534 ASP B OD1 1 
ATOM   3600 O OD2 . ASP A 1 478 ? 26.623 -26.043 3.538   1.00 4.60   ? 534 ASP B OD2 1 
ATOM   3601 N N   . ASN A 1 479 ? 28.952 -30.273 1.285   1.00 11.34  ? 535 ASN B N   1 
ATOM   3602 C CA  . ASN A 1 479 ? 28.394 -31.081 0.205   1.00 11.42  ? 535 ASN B CA  1 
ATOM   3603 C C   . ASN A 1 479 ? 28.233 -32.503 0.722   1.00 14.44  ? 535 ASN B C   1 
ATOM   3604 O O   . ASN A 1 479 ? 28.345 -32.742 1.932   1.00 20.96  ? 535 ASN B O   1 
ATOM   3605 C CB  . ASN A 1 479 ? 29.288 -31.056 -1.044  1.00 6.29   ? 535 ASN B CB  1 
ATOM   3606 C CG  . ASN A 1 479 ? 29.115 -29.791 -1.863  1.00 11.60  ? 535 ASN B CG  1 
ATOM   3607 O OD1 . ASN A 1 479 ? 28.101 -29.603 -2.518  1.00 5.79   ? 535 ASN B OD1 1 
ATOM   3608 N ND2 . ASN A 1 479 ? 30.105 -28.920 -1.829  1.00 6.12   ? 535 ASN B ND2 1 
ATOM   3609 N N   . ALA A 1 480 ? 27.898 -33.423 -0.178  1.00 10.88  ? 536 ALA B N   1 
ATOM   3610 C CA  . ALA A 1 480 ? 27.790 -34.850 0.130   1.00 9.83   ? 536 ALA B CA  1 
ATOM   3611 C C   . ALA A 1 480 ? 29.003 -35.693 -0.291  1.00 17.25  ? 536 ALA B C   1 
ATOM   3612 O O   . ALA A 1 480 ? 28.939 -36.926 -0.250  1.00 15.48  ? 536 ALA B O   1 
ATOM   3613 C CB  . ALA A 1 480 ? 26.518 -35.422 -0.441  1.00 19.02  ? 536 ALA B CB  1 
ATOM   3614 N N   . LEU A 1 481 ? 30.072 -35.039 -0.749  1.00 7.34   ? 537 LEU B N   1 
ATOM   3615 C CA  . LEU A 1 481 ? 31.231 -35.738 -1.314  1.00 7.85   ? 537 LEU B CA  1 
ATOM   3616 C C   . LEU A 1 481 ? 31.764 -36.865 -0.428  1.00 29.86  ? 537 LEU B C   1 
ATOM   3617 O O   . LEU A 1 481 ? 31.876 -36.724 0.786   1.00 25.26  ? 537 LEU B O   1 
ATOM   3618 C CB  . LEU A 1 481 ? 32.369 -34.755 -1.631  1.00 7.96   ? 537 LEU B CB  1 
ATOM   3619 C CG  . LEU A 1 481 ? 32.216 -33.747 -2.773  1.00 10.96  ? 537 LEU B CG  1 
ATOM   3620 C CD1 . LEU A 1 481 ? 33.416 -32.828 -2.835  1.00 10.33  ? 537 LEU B CD1 1 
ATOM   3621 C CD2 . LEU A 1 481 ? 32.046 -34.461 -4.092  1.00 8.85   ? 537 LEU B CD2 1 
ATOM   3622 N N   . SER A 1 482 ? 32.102 -37.986 -1.053  1.00 33.93  ? 538 SER B N   1 
ATOM   3623 C CA  . SER A 1 482 ? 32.502 -39.182 -0.319  1.00 30.69  ? 538 SER B CA  1 
ATOM   3624 C C   . SER A 1 482 ? 33.759 -39.829 -0.886  1.00 33.42  ? 538 SER B C   1 
ATOM   3625 O O   . SER A 1 482 ? 34.433 -39.277 -1.762  1.00 35.95  ? 538 SER B O   1 
ATOM   3626 C CB  . SER A 1 482 ? 31.368 -40.205 -0.295  1.00 29.01  ? 538 SER B CB  1 
ATOM   3627 O OG  . SER A 1 482 ? 31.024 -40.606 -1.613  1.00 32.20  ? 538 SER B OG  1 
ATOM   3628 N N   . SER A 1 483 ? 34.031 -41.023 -0.373  1.00 30.62  ? 539 SER B N   1 
ATOM   3629 C CA  . SER A 1 483 ? 35.271 -41.764 -0.571  1.00 29.39  ? 539 SER B CA  1 
ATOM   3630 C C   . SER A 1 483 ? 36.507 -40.997 -0.114  1.00 31.25  ? 539 SER B C   1 
ATOM   3631 O O   . SER A 1 483 ? 36.459 -40.257 0.865   1.00 36.07  ? 539 SER B O   1 
ATOM   3632 C CB  . SER A 1 483 ? 35.416 -42.199 -2.027  1.00 32.29  ? 539 SER B CB  1 
ATOM   3633 O OG  . SER A 1 483 ? 36.382 -43.229 -2.154  1.00 40.50  ? 539 SER B OG  1 
ATOM   3634 N N   . THR A 1 484 ? 37.604 -41.131 -0.839  1.00 13.43  ? 540 THR B N   1 
ATOM   3635 C CA  . THR A 1 484 ? 38.860 -40.635 -0.309  1.00 20.14  ? 540 THR B CA  1 
ATOM   3636 C C   . THR A 1 484 ? 39.378 -39.460 -1.078  1.00 17.40  ? 540 THR B C   1 
ATOM   3637 O O   . THR A 1 484 ? 39.068 -39.282 -2.250  1.00 29.66  ? 540 THR B O   1 
ATOM   3638 C CB  . THR A 1 484 ? 39.970 -41.684 -0.331  1.00 25.20  ? 540 THR B CB  1 
ATOM   3639 O OG1 . THR A 1 484 ? 40.635 -41.629 -1.598  1.00 32.70  ? 540 THR B OG1 1 
ATOM   3640 C CG2 . THR A 1 484 ? 39.406 -43.075 -0.080  1.00 23.63  ? 540 THR B CG2 1 
ATOM   3641 N N   . LEU A 1 485 ? 40.149 -38.640 -0.383  1.00 21.01  ? 541 LEU B N   1 
ATOM   3642 C CA  . LEU A 1 485 ? 40.881 -37.568 -1.017  1.00 25.05  ? 541 LEU B CA  1 
ATOM   3643 C C   . LEU A 1 485 ? 41.881 -38.256 -1.944  1.00 25.86  ? 541 LEU B C   1 
ATOM   3644 O O   . LEU A 1 485 ? 42.526 -39.228 -1.562  1.00 22.07  ? 541 LEU B O   1 
ATOM   3645 C CB  . LEU A 1 485 ? 41.547 -36.685 0.046   1.00 21.97  ? 541 LEU B CB  1 
ATOM   3646 C CG  . LEU A 1 485 ? 42.294 -35.414 -0.370  1.00 21.16  ? 541 LEU B CG  1 
ATOM   3647 C CD1 . LEU A 1 485 ? 41.425 -34.458 -1.165  1.00 20.73  ? 541 LEU B CD1 1 
ATOM   3648 C CD2 . LEU A 1 485 ? 42.857 -34.716 0.858   1.00 19.69  ? 541 LEU B CD2 1 
ATOM   3649 N N   . PRO A 1 486 ? 41.949 -37.809 -3.202  1.00 37.78  ? 542 PRO B N   1 
ATOM   3650 C CA  . PRO A 1 486 ? 42.828 -38.522 -4.133  1.00 40.04  ? 542 PRO B CA  1 
ATOM   3651 C C   . PRO A 1 486 ? 44.293 -38.142 -3.942  1.00 42.88  ? 542 PRO B C   1 
ATOM   3652 O O   . PRO A 1 486 ? 44.589 -37.054 -3.439  1.00 44.42  ? 542 PRO B O   1 
ATOM   3653 C CB  . PRO A 1 486 ? 42.324 -38.062 -5.499  1.00 41.65  ? 542 PRO B CB  1 
ATOM   3654 C CG  . PRO A 1 486 ? 41.720 -36.713 -5.247  1.00 42.33  ? 542 PRO B CG  1 
ATOM   3655 C CD  . PRO A 1 486 ? 41.144 -36.766 -3.864  1.00 38.40  ? 542 PRO B CD  1 
ATOM   3656 N N   . PRO A 1 487 ? 45.211 -39.047 -4.310  1.00 42.71  ? 543 PRO B N   1 
ATOM   3657 C CA  . PRO A 1 487 ? 46.628 -38.678 -4.354  1.00 41.08  ? 543 PRO B CA  1 
ATOM   3658 C C   . PRO A 1 487 ? 46.895 -37.628 -5.421  1.00 39.13  ? 543 PRO B C   1 
ATOM   3659 O O   . PRO A 1 487 ? 47.886 -36.901 -5.332  1.00 40.36  ? 543 PRO B O   1 
ATOM   3660 C CB  . PRO A 1 487 ? 47.330 -39.994 -4.705  1.00 18.98  ? 543 PRO B CB  1 
ATOM   3661 C CG  . PRO A 1 487 ? 46.253 -40.942 -5.094  1.00 42.54  ? 543 PRO B CG  1 
ATOM   3662 C CD  . PRO A 1 487 ? 45.019 -40.501 -4.406  1.00 44.10  ? 543 PRO B CD  1 
ATOM   3663 N N   . GLY A 1 488 ? 45.997 -37.541 -6.402  1.00 37.14  ? 544 GLY B N   1 
ATOM   3664 C CA  . GLY A 1 488 ? 46.106 -36.577 -7.481  1.00 32.98  ? 544 GLY B CA  1 
ATOM   3665 C C   . GLY A 1 488 ? 46.170 -35.153 -6.975  1.00 30.09  ? 544 GLY B C   1 
ATOM   3666 O O   . GLY A 1 488 ? 46.616 -34.246 -7.675  1.00 28.41  ? 544 GLY B O   1 
ATOM   3667 N N   . ILE A 1 489 ? 45.726 -34.963 -5.740  1.00 36.32  ? 545 ILE B N   1 
ATOM   3668 C CA  . ILE A 1 489 ? 45.767 -33.664 -5.089  1.00 41.56  ? 545 ILE B CA  1 
ATOM   3669 C C   . ILE A 1 489 ? 47.191 -33.114 -5.117  1.00 44.51  ? 545 ILE B C   1 
ATOM   3670 O O   . ILE A 1 489 ? 47.398 -31.900 -5.166  1.00 45.19  ? 545 ILE B O   1 
ATOM   3671 C CB  . ILE A 1 489 ? 45.227 -33.754 -3.633  1.00 39.25  ? 545 ILE B CB  1 
ATOM   3672 C CG1 . ILE A 1 489 ? 44.139 -32.700 -3.384  1.00 34.14  ? 545 ILE B CG1 1 
ATOM   3673 C CG2 . ILE A 1 489 ? 46.359 -33.676 -2.602  1.00 43.34  ? 545 ILE B CG2 1 
ATOM   3674 C CD1 . ILE A 1 489 ? 44.569 -31.278 -3.696  1.00 35.81  ? 545 ILE B CD1 1 
ATOM   3675 N N   . GLY A 1 490 ? 48.167 -34.020 -5.130  1.00 41.92  ? 546 GLY B N   1 
ATOM   3676 C CA  . GLY A 1 490 ? 49.564 -33.638 -5.142  1.00 37.75  ? 546 GLY B CA  1 
ATOM   3677 C C   . GLY A 1 490 ? 49.963 -32.955 -6.432  1.00 35.79  ? 546 GLY B C   1 
ATOM   3678 O O   . GLY A 1 490 ? 51.072 -32.447 -6.547  1.00 42.44  ? 546 GLY B O   1 
ATOM   3679 N N   . LEU A 1 491 ? 49.064 -32.944 -7.409  1.00 26.26  ? 547 LEU B N   1 
ATOM   3680 C CA  . LEU A 1 491 ? 49.361 -32.326 -8.691  1.00 30.99  ? 547 LEU B CA  1 
ATOM   3681 C C   . LEU A 1 491 ? 48.931 -30.865 -8.812  1.00 41.44  ? 547 LEU B C   1 
ATOM   3682 O O   . LEU A 1 491 ? 49.272 -30.210 -9.796  1.00 45.71  ? 547 LEU B O   1 
ATOM   3683 C CB  . LEU A 1 491 ? 48.777 -33.155 -9.833  1.00 33.19  ? 547 LEU B CB  1 
ATOM   3684 C CG  . LEU A 1 491 ? 49.405 -34.543 -9.948  1.00 30.26  ? 547 LEU B CG  1 
ATOM   3685 C CD1 . LEU A 1 491 ? 48.501 -35.472 -10.725 1.00 27.13  ? 547 LEU B CD1 1 
ATOM   3686 C CD2 . LEU A 1 491 ? 50.781 -34.446 -10.592 1.00 26.20  ? 547 LEU B CD2 1 
ATOM   3687 N N   . LEU A 1 492 ? 48.211 -30.331 -7.827  1.00 42.96  ? 548 LEU B N   1 
ATOM   3688 C CA  . LEU A 1 492 ? 47.828 -28.926 -7.931  1.00 30.93  ? 548 LEU B CA  1 
ATOM   3689 C C   . LEU A 1 492 ? 48.846 -28.180 -7.094  1.00 22.75  ? 548 LEU B C   1 
ATOM   3690 O O   . LEU A 1 492 ? 48.715 -28.051 -5.884  1.00 21.79  ? 548 LEU B O   1 
ATOM   3691 C CB  . LEU A 1 492 ? 46.420 -28.715 -7.367  1.00 21.98  ? 548 LEU B CB  1 
ATOM   3692 C CG  . LEU A 1 492 ? 45.374 -29.703 -7.895  1.00 23.29  ? 548 LEU B CG  1 
ATOM   3693 C CD1 . LEU A 1 492 ? 44.148 -29.755 -7.017  1.00 12.29  ? 548 LEU B CD1 1 
ATOM   3694 C CD2 . LEU A 1 492 ? 44.986 -29.317 -9.301  1.00 26.01  ? 548 LEU B CD2 1 
ATOM   3695 N N   . THR A 1 493 ? 49.834 -27.634 -7.785  1.00 23.41  ? 549 THR B N   1 
ATOM   3696 C CA  . THR A 1 493 ? 51.039 -27.148 -7.149  1.00 23.47  ? 549 THR B CA  1 
ATOM   3697 C C   . THR A 1 493 ? 50.927 -25.671 -6.883  1.00 23.14  ? 549 THR B C   1 
ATOM   3698 O O   . THR A 1 493 ? 51.741 -25.092 -6.162  1.00 24.56  ? 549 THR B O   1 
ATOM   3699 C CB  . THR A 1 493 ? 52.252 -27.404 -8.058  1.00 32.10  ? 549 THR B CB  1 
ATOM   3700 O OG1 . THR A 1 493 ? 52.224 -26.502 -9.175  1.00 30.33  ? 549 THR B OG1 1 
ATOM   3701 C CG2 . THR A 1 493 ? 52.224 -28.830 -8.571  1.00 30.72  ? 549 THR B CG2 1 
ATOM   3702 N N   . GLU A 1 494 ? 49.917 -25.062 -7.493  1.00 23.16  ? 550 GLU B N   1 
ATOM   3703 C CA  . GLU A 1 494 ? 49.674 -23.639 -7.345  1.00 25.58  ? 550 GLU B CA  1 
ATOM   3704 C C   . GLU A 1 494 ? 48.584 -23.416 -6.323  1.00 23.40  ? 550 GLU B C   1 
ATOM   3705 O O   . GLU A 1 494 ? 48.252 -22.281 -6.014  1.00 27.52  ? 550 GLU B O   1 
ATOM   3706 C CB  . GLU A 1 494 ? 49.263 -23.034 -8.686  1.00 37.60  ? 550 GLU B CB  1 
ATOM   3707 C CG  . GLU A 1 494 ? 50.164 -23.447 -9.835  1.00 39.87  ? 550 GLU B CG  1 
ATOM   3708 C CD  . GLU A 1 494 ? 51.612 -23.171 -9.526  1.00 45.30  ? 550 GLU B CD  1 
ATOM   3709 O OE1 . GLU A 1 494 ? 51.924 -22.002 -9.202  1.00 44.67  ? 550 GLU B OE1 1 
ATOM   3710 O OE2 . GLU A 1 494 ? 52.429 -24.121 -9.584  1.00 47.46  ? 550 GLU B OE2 1 
ATOM   3711 N N   . LEU A 1 495 ? 48.024 -24.502 -5.802  1.00 22.38  ? 551 LEU B N   1 
ATOM   3712 C CA  . LEU A 1 495 ? 46.893 -24.394 -4.885  1.00 12.17  ? 551 LEU B CA  1 
ATOM   3713 C C   . LEU A 1 495 ? 47.306 -23.658 -3.624  1.00 22.59  ? 551 LEU B C   1 
ATOM   3714 O O   . LEU A 1 495 ? 48.434 -23.780 -3.163  1.00 37.46  ? 551 LEU B O   1 
ATOM   3715 C CB  . LEU A 1 495 ? 46.318 -25.769 -4.556  1.00 12.19  ? 551 LEU B CB  1 
ATOM   3716 C CG  . LEU A 1 495 ? 44.924 -25.780 -3.936  1.00 14.89  ? 551 LEU B CG  1 
ATOM   3717 C CD1 . LEU A 1 495 ? 43.929 -25.050 -4.827  1.00 17.68  ? 551 LEU B CD1 1 
ATOM   3718 C CD2 . LEU A 1 495 ? 44.464 -27.201 -3.687  1.00 11.33  ? 551 LEU B CD2 1 
ATOM   3719 N N   . THR A 1 496 ? 46.391 -22.878 -3.077  1.00 20.79  ? 552 THR B N   1 
ATOM   3720 C CA  . THR A 1 496 ? 46.709 -21.992 -1.962  1.00 21.92  ? 552 THR B CA  1 
ATOM   3721 C C   . THR A 1 496 ? 45.741 -22.197 -0.807  1.00 18.49  ? 552 THR B C   1 
ATOM   3722 O O   . THR A 1 496 ? 46.159 -22.402 0.329   1.00 15.06  ? 552 THR B O   1 
ATOM   3723 C CB  . THR A 1 496 ? 46.791 -20.533 -2.398  1.00 20.45  ? 552 THR B CB  1 
ATOM   3724 O OG1 . THR A 1 496 ? 47.727 -20.438 -3.474  1.00 23.49  ? 552 THR B OG1 1 
ATOM   3725 C CG2 . THR A 1 496 ? 47.287 -19.685 -1.266  1.00 28.06  ? 552 THR B CG2 1 
ATOM   3726 N N   . LYS A 1 497 ? 44.452 -22.039 -1.085  1.00 12.61  ? 553 LYS B N   1 
ATOM   3727 C CA  . LYS A 1 497 ? 43.434 -22.431 -0.123  1.00 15.68  ? 553 LYS B CA  1 
ATOM   3728 C C   . LYS A 1 497 ? 42.691 -23.662 -0.630  1.00 19.38  ? 553 LYS B C   1 
ATOM   3729 O O   . LYS A 1 497 ? 42.319 -23.736 -1.800  1.00 18.60  ? 553 LYS B O   1 
ATOM   3730 C CB  . LYS A 1 497 ? 42.481 -21.268 0.152   1.00 8.62   ? 553 LYS B CB  1 
ATOM   3731 C CG  . LYS A 1 497 ? 43.228 -20.030 0.600   1.00 8.71   ? 553 LYS B CG  1 
ATOM   3732 C CD  . LYS A 1 497 ? 42.353 -18.807 0.699   1.00 8.17   ? 553 LYS B CD  1 
ATOM   3733 C CE  . LYS A 1 497 ? 43.237 -17.581 0.814   1.00 12.65  ? 553 LYS B CE  1 
ATOM   3734 N NZ  . LYS A 1 497 ? 42.472 -16.315 0.917   1.00 13.68  ? 553 LYS B NZ  1 
ATOM   3735 N N   . LEU A 1 498 ? 42.525 -24.648 0.242   1.00 19.39  ? 554 LEU B N   1 
ATOM   3736 C CA  . LEU A 1 498 ? 41.744 -25.826 -0.089  1.00 9.17   ? 554 LEU B CA  1 
ATOM   3737 C C   . LEU A 1 498 ? 40.815 -26.169 1.058   1.00 10.26  ? 554 LEU B C   1 
ATOM   3738 O O   . LEU A 1 498 ? 41.258 -26.539 2.145   1.00 18.66  ? 554 LEU B O   1 
ATOM   3739 C CB  . LEU A 1 498 ? 42.644 -27.019 -0.399  1.00 9.97   ? 554 LEU B CB  1 
ATOM   3740 C CG  . LEU A 1 498 ? 41.944 -28.385 -0.403  1.00 22.42  ? 554 LEU B CG  1 
ATOM   3741 C CD1 . LEU A 1 498 ? 40.797 -28.430 -1.417  1.00 17.34  ? 554 LEU B CD1 1 
ATOM   3742 C CD2 . LEU A 1 498 ? 42.937 -29.504 -0.649  1.00 11.10  ? 554 LEU B CD2 1 
ATOM   3743 N N   . ASN A 1 499 ? 39.520 -26.070 0.795   1.00 8.36   ? 555 ASN B N   1 
ATOM   3744 C CA  . ASN A 1 499 ? 38.522 -26.345 1.802   1.00 16.30  ? 555 ASN B CA  1 
ATOM   3745 C C   . ASN A 1 499 ? 37.568 -27.458 1.370   1.00 14.69  ? 555 ASN B C   1 
ATOM   3746 O O   . ASN A 1 499 ? 36.791 -27.302 0.433   1.00 12.74  ? 555 ASN B O   1 
ATOM   3747 C CB  . ASN A 1 499 ? 37.768 -25.055 2.120   1.00 21.75  ? 555 ASN B CB  1 
ATOM   3748 C CG  . ASN A 1 499 ? 36.713 -25.245 3.167   1.00 24.04  ? 555 ASN B CG  1 
ATOM   3749 O OD1 . ASN A 1 499 ? 36.729 -26.226 3.906   1.00 27.77  ? 555 ASN B OD1 1 
ATOM   3750 N ND2 . ASN A 1 499 ? 35.773 -24.313 3.229   1.00 25.18  ? 555 ASN B ND2 1 
ATOM   3751 N N   . LEU A 1 500 ? 37.699 -28.601 2.028   1.00 22.45  ? 556 LEU B N   1 
ATOM   3752 C CA  . LEU A 1 500 ? 36.836 -29.761 1.846   1.00 8.12   ? 556 LEU B CA  1 
ATOM   3753 C C   . LEU A 1 500 ? 35.832 -30.003 2.948   1.00 11.72  ? 556 LEU B C   1 
ATOM   3754 O O   . LEU A 1 500 ? 35.202 -31.066 2.975   1.00 8.54   ? 556 LEU B O   1 
ATOM   3755 C CB  . LEU A 1 500 ? 37.672 -31.008 1.583   1.00 8.66   ? 556 LEU B CB  1 
ATOM   3756 C CG  . LEU A 1 500 ? 38.470 -30.741 0.305   1.00 17.60  ? 556 LEU B CG  1 
ATOM   3757 C CD1 . LEU A 1 500 ? 39.561 -31.751 0.144   1.00 9.94   ? 556 LEU B CD1 1 
ATOM   3758 C CD2 . LEU A 1 500 ? 37.554 -30.696 -0.926  1.00 8.66   ? 556 LEU B CD2 1 
ATOM   3759 N N   . ALA A 1 501 ? 35.742 -29.064 3.893   1.00 7.59   ? 557 ALA B N   1 
ATOM   3760 C CA  . ALA A 1 501 ? 34.976 -29.264 5.143   1.00 12.09  ? 557 ALA B CA  1 
ATOM   3761 C C   . ALA A 1 501 ? 33.498 -29.631 4.977   1.00 10.87  ? 557 ALA B C   1 
ATOM   3762 O O   . ALA A 1 501 ? 32.869 -29.325 3.965   1.00 8.96   ? 557 ALA B O   1 
ATOM   3763 C CB  . ALA A 1 501 ? 35.104 -28.064 6.063   1.00 7.20   ? 557 ALA B CB  1 
ATOM   3764 N N   . LYS A 1 502 ? 32.969 -30.331 5.973   1.00 11.63  ? 558 LYS B N   1 
ATOM   3765 C CA  . LYS A 1 502 ? 31.563 -30.729 5.988   1.00 13.10  ? 558 LYS B CA  1 
ATOM   3766 C C   . LYS A 1 502 ? 31.188 -31.538 4.739   1.00 13.19  ? 558 LYS B C   1 
ATOM   3767 O O   . LYS A 1 502 ? 30.386 -31.099 3.915   1.00 6.40   ? 558 LYS B O   1 
ATOM   3768 C CB  . LYS A 1 502 ? 30.664 -29.499 6.145   1.00 6.16   ? 558 LYS B CB  1 
ATOM   3769 C CG  . LYS A 1 502 ? 29.429 -29.736 6.970   1.00 15.13  ? 558 LYS B CG  1 
ATOM   3770 C CD  . LYS A 1 502 ? 28.420 -28.639 6.700   1.00 24.28  ? 558 LYS B CD  1 
ATOM   3771 C CE  . LYS A 1 502 ? 27.083 -28.850 7.438   1.00 29.36  ? 558 LYS B CE  1 
ATOM   3772 N NZ  . LYS A 1 502 ? 26.355 -30.106 7.073   1.00 29.11  ? 558 LYS B NZ  1 
ATOM   3773 N N   . ASN A 1 503 ? 31.801 -32.714 4.610   1.00 16.87  ? 559 ASN B N   1 
ATOM   3774 C CA  . ASN A 1 503 ? 31.487 -33.686 3.557   1.00 13.76  ? 559 ASN B CA  1 
ATOM   3775 C C   . ASN A 1 503 ? 31.445 -35.084 4.179   1.00 22.92  ? 559 ASN B C   1 
ATOM   3776 O O   . ASN A 1 503 ? 31.498 -35.233 5.414   1.00 27.92  ? 559 ASN B O   1 
ATOM   3777 C CB  . ASN A 1 503 ? 32.526 -33.654 2.421   1.00 13.45  ? 559 ASN B CB  1 
ATOM   3778 C CG  . ASN A 1 503 ? 32.277 -32.544 1.412   1.00 13.00  ? 559 ASN B CG  1 
ATOM   3779 O OD1 . ASN A 1 503 ? 31.254 -32.521 0.747   1.00 19.61  ? 559 ASN B OD1 1 
ATOM   3780 N ND2 . ASN A 1 503 ? 33.229 -31.640 1.276   1.00 7.59   ? 559 ASN B ND2 1 
ATOM   3781 N N   . ARG A 1 504 ? 31.313 -36.098 3.328   1.00 19.12  ? 560 ARG B N   1 
ATOM   3782 C CA  . ARG A 1 504 ? 31.405 -37.508 3.729   1.00 16.15  ? 560 ARG B CA  1 
ATOM   3783 C C   . ARG A 1 504 ? 32.770 -38.211 3.489   1.00 9.52   ? 560 ARG B C   1 
ATOM   3784 O O   . ARG A 1 504 ? 32.869 -39.432 3.602   1.00 10.20  ? 560 ARG B O   1 
ATOM   3785 C CB  . ARG A 1 504 ? 30.241 -38.295 3.132   1.00 15.21  ? 560 ARG B CB  1 
ATOM   3786 C CG  . ARG A 1 504 ? 28.909 -37.608 3.352   1.00 21.23  ? 560 ARG B CG  1 
ATOM   3787 C CD  . ARG A 1 504 ? 28.278 -37.984 4.692   1.00 41.12  ? 560 ARG B CD  1 
ATOM   3788 N NE  . ARG A 1 504 ? 29.072 -37.573 5.848   1.00 54.12  ? 560 ARG B NE  1 
ATOM   3789 C CZ  . ARG A 1 504 ? 29.632 -38.418 6.710   1.00 59.81  ? 560 ARG B CZ  1 
ATOM   3790 N NH1 . ARG A 1 504 ? 29.478 -39.727 6.551   1.00 62.83  ? 560 ARG B NH1 1 
ATOM   3791 N NH2 . ARG A 1 504 ? 30.338 -37.952 7.733   1.00 57.26  ? 560 ARG B NH2 1 
ATOM   3792 N N   . LEU A 1 505 ? 33.792 -37.445 3.111   1.00 9.60   ? 561 LEU B N   1 
ATOM   3793 C CA  . LEU A 1 505 ? 35.130 -37.970 2.804   1.00 18.64  ? 561 LEU B CA  1 
ATOM   3794 C C   . LEU A 1 505 ? 35.725 -38.854 3.912   1.00 22.97  ? 561 LEU B C   1 
ATOM   3795 O O   . LEU A 1 505 ? 35.515 -38.594 5.092   1.00 27.68  ? 561 LEU B O   1 
ATOM   3796 C CB  . LEU A 1 505 ? 36.087 -36.806 2.493   1.00 13.86  ? 561 LEU B CB  1 
ATOM   3797 C CG  . LEU A 1 505 ? 35.677 -35.833 1.377   1.00 16.54  ? 561 LEU B CG  1 
ATOM   3798 C CD1 . LEU A 1 505 ? 36.464 -34.529 1.418   1.00 19.27  ? 561 LEU B CD1 1 
ATOM   3799 C CD2 . LEU A 1 505 ? 35.872 -36.487 0.027   1.00 13.74  ? 561 LEU B CD2 1 
ATOM   3800 N N   . SER A 1 506 ? 36.465 -39.894 3.526   1.00 24.75  ? 562 SER B N   1 
ATOM   3801 C CA  . SER A 1 506 ? 37.051 -40.834 4.485   1.00 23.38  ? 562 SER B CA  1 
ATOM   3802 C C   . SER A 1 506 ? 38.417 -41.354 4.036   1.00 13.90  ? 562 SER B C   1 
ATOM   3803 O O   . SER A 1 506 ? 39.004 -40.854 3.081   1.00 40.41  ? 562 SER B O   1 
ATOM   3804 C CB  . SER A 1 506 ? 36.121 -42.022 4.711   1.00 22.67  ? 562 SER B CB  1 
ATOM   3805 O OG  . SER A 1 506 ? 36.436 -43.058 3.799   1.00 17.71  ? 562 SER B OG  1 
ATOM   3806 N N   . GLY A 1 507 ? 38.917 -42.363 4.746   1.00 26.79  ? 563 GLY B N   1 
ATOM   3807 C CA  . GLY A 1 507 ? 40.258 -42.876 4.542   1.00 15.67  ? 563 GLY B CA  1 
ATOM   3808 C C   . GLY A 1 507 ? 41.362 -42.020 5.149   1.00 22.40  ? 563 GLY B C   1 
ATOM   3809 O O   . GLY A 1 507 ? 41.099 -41.028 5.821   1.00 15.18  ? 563 GLY B O   1 
ATOM   3810 N N   . GLU A 1 508 ? 42.605 -42.425 4.914   1.00 16.74  ? 564 GLU B N   1 
ATOM   3811 C CA  . GLU A 1 508 ? 43.790 -41.694 5.340   1.00 22.65  ? 564 GLU B CA  1 
ATOM   3812 C C   . GLU A 1 508 ? 43.908 -40.386 4.587   1.00 27.51  ? 564 GLU B C   1 
ATOM   3813 O O   . GLU A 1 508 ? 43.342 -40.229 3.503   1.00 35.95  ? 564 GLU B O   1 
ATOM   3814 C CB  . GLU A 1 508 ? 45.033 -42.503 4.982   1.00 29.63  ? 564 GLU B CB  1 
ATOM   3815 C CG  . GLU A 1 508 ? 45.993 -42.778 6.098   1.00 34.51  ? 564 GLU B CG  1 
ATOM   3816 C CD  . GLU A 1 508 ? 45.712 -44.110 6.728   1.00 42.19  ? 564 GLU B CD  1 
ATOM   3817 O OE1 . GLU A 1 508 ? 44.559 -44.564 6.591   1.00 34.61  ? 564 GLU B OE1 1 
ATOM   3818 O OE2 . GLU A 1 508 ? 46.628 -44.701 7.347   1.00 52.68  ? 564 GLU B OE2 1 
ATOM   3819 N N   . ILE A 1 509 ? 44.662 -39.448 5.150   1.00 24.52  ? 565 ILE B N   1 
ATOM   3820 C CA  . ILE A 1 509 ? 45.168 -38.340 4.355   1.00 24.36  ? 565 ILE B CA  1 
ATOM   3821 C C   . ILE A 1 509 ? 46.362 -38.839 3.539   1.00 32.46  ? 565 ILE B C   1 
ATOM   3822 O O   . ILE A 1 509 ? 47.335 -39.334 4.109   1.00 45.21  ? 565 ILE B O   1 
ATOM   3823 C CB  . ILE A 1 509 ? 45.617 -37.172 5.230   1.00 22.64  ? 565 ILE B CB  1 
ATOM   3824 C CG1 . ILE A 1 509 ? 44.417 -36.543 5.937   1.00 14.98  ? 565 ILE B CG1 1 
ATOM   3825 C CG2 . ILE A 1 509 ? 46.385 -36.145 4.391   1.00 18.24  ? 565 ILE B CG2 1 
ATOM   3826 C CD1 . ILE A 1 509 ? 44.761 -35.285 6.679   1.00 25.72  ? 565 ILE B CD1 1 
ATOM   3827 N N   . PRO A 1 510 ? 46.288 -38.723 2.205   1.00 29.89  ? 566 PRO B N   1 
ATOM   3828 C CA  . PRO A 1 510 ? 47.367 -39.172 1.321   1.00 34.56  ? 566 PRO B CA  1 
ATOM   3829 C C   . PRO A 1 510 ? 48.631 -38.375 1.564   1.00 34.38  ? 566 PRO B C   1 
ATOM   3830 O O   . PRO A 1 510 ? 48.547 -37.175 1.785   1.00 37.52  ? 566 PRO B O   1 
ATOM   3831 C CB  . PRO A 1 510 ? 46.821 -38.876 -0.086  1.00 38.89  ? 566 PRO B CB  1 
ATOM   3832 C CG  . PRO A 1 510 ? 45.833 -37.793 0.112   1.00 37.69  ? 566 PRO B CG  1 
ATOM   3833 C CD  . PRO A 1 510 ? 45.197 -38.080 1.454   1.00 36.70  ? 566 PRO B CD  1 
ATOM   3834 N N   . ARG A 1 511 ? 49.786 -39.027 1.510   1.00 34.12  ? 567 ARG B N   1 
ATOM   3835 C CA  . ARG A 1 511 ? 51.039 -38.374 1.860   1.00 31.43  ? 567 ARG B CA  1 
ATOM   3836 C C   . ARG A 1 511 ? 51.514 -37.400 0.790   1.00 36.66  ? 567 ARG B C   1 
ATOM   3837 O O   . ARG A 1 511 ? 52.409 -36.592 1.043   1.00 33.43  ? 567 ARG B O   1 
ATOM   3838 C CB  . ARG A 1 511 ? 52.114 -39.420 2.133   1.00 34.06  ? 567 ARG B CB  1 
ATOM   3839 C CG  . ARG A 1 511 ? 51.721 -40.427 3.188   1.00 41.31  ? 567 ARG B CG  1 
ATOM   3840 C CD  . ARG A 1 511 ? 52.678 -41.593 3.217   1.00 49.87  ? 567 ARG B CD  1 
ATOM   3841 N NE  . ARG A 1 511 ? 52.321 -42.525 4.276   1.00 54.97  ? 567 ARG B NE  1 
ATOM   3842 C CZ  . ARG A 1 511 ? 52.766 -42.431 5.522   1.00 57.93  ? 567 ARG B CZ  1 
ATOM   3843 N NH1 . ARG A 1 511 ? 53.593 -41.448 5.857   1.00 54.05  ? 567 ARG B NH1 1 
ATOM   3844 N NH2 . ARG A 1 511 ? 52.385 -43.321 6.432   1.00 65.56  ? 567 ARG B NH2 1 
ATOM   3845 N N   . GLU A 1 512 ? 50.910 -37.476 -0.399  1.00 42.07  ? 568 GLU B N   1 
ATOM   3846 C CA  . GLU A 1 512 ? 51.288 -36.609 -1.522  1.00 36.65  ? 568 GLU B CA  1 
ATOM   3847 C C   . GLU A 1 512 ? 50.839 -35.160 -1.363  1.00 38.52  ? 568 GLU B C   1 
ATOM   3848 O O   . GLU A 1 512 ? 51.133 -34.335 -2.212  1.00 42.17  ? 568 GLU B O   1 
ATOM   3849 C CB  . GLU A 1 512 ? 50.802 -37.153 -2.864  1.00 31.74  ? 568 GLU B CB  1 
ATOM   3850 C CG  . GLU A 1 512 ? 49.769 -38.246 -2.764  1.00 37.06  ? 568 GLU B CG  1 
ATOM   3851 C CD  . GLU A 1 512 ? 50.373 -39.623 -2.922  1.00 44.69  ? 568 GLU B CD  1 
ATOM   3852 O OE1 . GLU A 1 512 ? 49.649 -40.625 -2.747  1.00 49.73  ? 568 GLU B OE1 1 
ATOM   3853 O OE2 . GLU A 1 512 ? 51.578 -39.705 -3.221  1.00 44.52  ? 568 GLU B OE2 1 
ATOM   3854 N N   . ILE A 1 513 ? 50.109 -34.845 -0.297  1.00 35.31  ? 569 ILE B N   1 
ATOM   3855 C CA  . ILE A 1 513 ? 49.708 -33.458 -0.070  1.00 29.27  ? 569 ILE B CA  1 
ATOM   3856 C C   . ILE A 1 513 ? 50.952 -32.603 0.164   1.00 27.10  ? 569 ILE B C   1 
ATOM   3857 O O   . ILE A 1 513 ? 50.940 -31.392 -0.047  1.00 30.79  ? 569 ILE B O   1 
ATOM   3858 C CB  . ILE A 1 513 ? 48.699 -33.319 1.103   1.00 39.50  ? 569 ILE B CB  1 
ATOM   3859 C CG1 . ILE A 1 513 ? 48.144 -31.892 1.196   1.00 32.62  ? 569 ILE B CG1 1 
ATOM   3860 C CG2 . ILE A 1 513 ? 49.338 -33.726 2.416   1.00 43.15  ? 569 ILE B CG2 1 
ATOM   3861 C CD1 . ILE A 1 513 ? 46.635 -31.828 1.305   1.00 14.45  ? 569 ILE B CD1 1 
ATOM   3862 N N   . SER A 1 514 ? 52.039 -33.252 0.563   1.00 22.47  ? 570 SER B N   1 
ATOM   3863 C CA  . SER A 1 514 ? 53.265 -32.543 0.885   1.00 28.42  ? 570 SER B CA  1 
ATOM   3864 C C   . SER A 1 514 ? 53.894 -31.987 -0.369  1.00 27.16  ? 570 SER B C   1 
ATOM   3865 O O   . SER A 1 514 ? 54.706 -31.064 -0.308  1.00 31.69  ? 570 SER B O   1 
ATOM   3866 C CB  . SER A 1 514 ? 54.247 -33.457 1.618   1.00 36.55  ? 570 SER B CB  1 
ATOM   3867 O OG  . SER A 1 514 ? 54.252 -34.746 1.034   1.00 43.55  ? 570 SER B OG  1 
ATOM   3868 N N   . THR A 1 515 ? 53.505 -32.529 -1.514  1.00 24.46  ? 571 THR B N   1 
ATOM   3869 C CA  . THR A 1 515 ? 53.992 -31.965 -2.776  1.00 32.79  ? 571 THR B CA  1 
ATOM   3870 C C   . THR A 1 515 ? 53.130 -30.836 -3.343  1.00 30.80  ? 571 THR B C   1 
ATOM   3871 O O   . THR A 1 515 ? 53.361 -30.402 -4.468  1.00 27.63  ? 571 THR B O   1 
ATOM   3872 C CB  . THR A 1 515 ? 54.336 -33.009 -3.885  1.00 20.98  ? 571 THR B CB  1 
ATOM   3873 O OG1 . THR A 1 515 ? 54.945 -32.317 -4.975  1.00 27.51  ? 571 THR B OG1 1 
ATOM   3874 C CG2 . THR A 1 515 ? 53.114 -33.732 -4.380  1.00 20.34  ? 571 THR B CG2 1 
ATOM   3875 N N   . CYS A 1 516 ? 52.139 -30.371 -2.580  1.00 33.11  ? 572 CYS B N   1 
ATOM   3876 C CA  . CYS A 1 516 ? 51.484 -29.120 -2.944  1.00 29.58  ? 572 CYS B CA  1 
ATOM   3877 C C   . CYS A 1 516 ? 52.276 -28.060 -2.221  1.00 34.36  ? 572 CYS B C   1 
ATOM   3878 O O   . CYS A 1 516 ? 52.054 -27.813 -1.038  1.00 40.87  ? 572 CYS B O   1 
ATOM   3879 C CB  . CYS A 1 516 ? 50.065 -29.037 -2.385  1.00 16.02  ? 572 CYS B CB  1 
ATOM   3880 S SG  . CYS A 1 516 ? 48.890 -30.301 -2.871  1.00 23.41  ? 572 CYS B SG  1 
ATOM   3881 N N   . ARG A 1 517 ? 53.114 -27.347 -2.956  1.00 35.31  ? 573 ARG B N   1 
ATOM   3882 C CA  . ARG A 1 517 ? 54.102 -26.489 -2.329  1.00 35.92  ? 573 ARG B CA  1 
ATOM   3883 C C   . ARG A 1 517 ? 53.590 -25.083 -2.006  1.00 29.89  ? 573 ARG B C   1 
ATOM   3884 O O   . ARG A 1 517 ? 54.240 -24.336 -1.273  1.00 36.33  ? 573 ARG B O   1 
ATOM   3885 C CB  . ARG A 1 517 ? 55.369 -26.443 -3.187  1.00 47.33  ? 573 ARG B CB  1 
ATOM   3886 C CG  . ARG A 1 517 ? 56.190 -27.734 -3.128  1.00 62.86  ? 573 ARG B CG  1 
ATOM   3887 C CD  . ARG A 1 517 ? 57.153 -27.752 -1.935  1.00 72.09  ? 573 ARG B CD  1 
ATOM   3888 N NE  . ARG A 1 517 ? 58.386 -27.011 -2.212  1.00 77.80  ? 573 ARG B NE  1 
ATOM   3889 C CZ  . ARG A 1 517 ? 59.317 -26.730 -1.303  1.00 79.82  ? 573 ARG B CZ  1 
ATOM   3890 N NH1 . ARG A 1 517 ? 59.164 -27.116 -0.040  1.00 77.12  ? 573 ARG B NH1 1 
ATOM   3891 N NH2 . ARG A 1 517 ? 60.403 -26.054 -1.657  1.00 81.73  ? 573 ARG B NH2 1 
ATOM   3892 N N   . SER A 1 518 ? 52.431 -24.728 -2.548  1.00 22.99  ? 574 SER B N   1 
ATOM   3893 C CA  . SER A 1 518 ? 51.907 -23.380 -2.378  1.00 18.30  ? 574 SER B CA  1 
ATOM   3894 C C   . SER A 1 518 ? 50.852 -23.226 -1.282  1.00 20.35  ? 574 SER B C   1 
ATOM   3895 O O   . SER A 1 518 ? 50.372 -22.115 -1.062  1.00 25.77  ? 574 SER B O   1 
ATOM   3896 C CB  . SER A 1 518 ? 51.357 -22.845 -3.707  1.00 18.44  ? 574 SER B CB  1 
ATOM   3897 O OG  . SER A 1 518 ? 52.370 -22.270 -4.522  1.00 21.05  ? 574 SER B OG  1 
ATOM   3898 N N   . LEU A 1 519 ? 50.517 -24.303 -0.570  1.00 14.78  ? 575 LEU B N   1 
ATOM   3899 C CA  . LEU A 1 519 ? 49.287 -24.329 0.241   1.00 15.87  ? 575 LEU B CA  1 
ATOM   3900 C C   . LEU A 1 519 ? 49.361 -23.467 1.504   1.00 20.36  ? 575 LEU B C   1 
ATOM   3901 O O   . LEU A 1 519 ? 50.195 -23.704 2.373   1.00 22.49  ? 575 LEU B O   1 
ATOM   3902 C CB  . LEU A 1 519 ? 48.986 -25.768 0.671   1.00 14.98  ? 575 LEU B CB  1 
ATOM   3903 C CG  . LEU A 1 519 ? 47.545 -26.278 0.755   1.00 15.26  ? 575 LEU B CG  1 
ATOM   3904 C CD1 . LEU A 1 519 ? 46.939 -26.398 -0.632  1.00 13.45  ? 575 LEU B CD1 1 
ATOM   3905 C CD2 . LEU A 1 519 ? 47.488 -27.627 1.461   1.00 20.85  ? 575 LEU B CD2 1 
ATOM   3906 N N   . GLN A 1 520 ? 48.499 -22.454 1.589   1.00 12.69  ? 576 GLN B N   1 
ATOM   3907 C CA  . GLN A 1 520 ? 48.384 -21.655 2.798   1.00 17.64  ? 576 GLN B CA  1 
ATOM   3908 C C   . GLN A 1 520 ? 47.220 -22.006 3.734   1.00 15.94  ? 576 GLN B C   1 
ATOM   3909 O O   . GLN A 1 520 ? 47.231 -21.638 4.908   1.00 19.74  ? 576 GLN B O   1 
ATOM   3910 C CB  . GLN A 1 520 ? 48.294 -20.186 2.410   1.00 13.59  ? 576 GLN B CB  1 
ATOM   3911 C CG  . GLN A 1 520 ? 49.480 -19.703 1.624   1.00 12.81  ? 576 GLN B CG  1 
ATOM   3912 C CD  . GLN A 1 520 ? 49.317 -18.263 1.207   1.00 25.53  ? 576 GLN B CD  1 
ATOM   3913 O OE1 . GLN A 1 520 ? 48.417 -17.578 1.679   1.00 30.39  ? 576 GLN B OE1 1 
ATOM   3914 N NE2 . GLN A 1 520 ? 50.174 -17.796 0.309   1.00 21.77  ? 576 GLN B NE2 1 
ATOM   3915 N N   . LEU A 1 521 ? 46.235 -22.731 3.222   1.00 11.11  ? 577 LEU B N   1 
ATOM   3916 C CA  . LEU A 1 521 ? 45.063 -23.092 4.009   1.00 10.40  ? 577 LEU B CA  1 
ATOM   3917 C C   . LEU A 1 521 ? 44.565 -24.471 3.634   1.00 10.44  ? 577 LEU B C   1 
ATOM   3918 O O   . LEU A 1 521 ? 44.356 -24.770 2.464   1.00 23.45  ? 577 LEU B O   1 
ATOM   3919 C CB  . LEU A 1 521 ? 43.935 -22.066 3.829   1.00 25.66  ? 577 LEU B CB  1 
ATOM   3920 C CG  . LEU A 1 521 ? 42.662 -22.222 4.684   1.00 20.59  ? 577 LEU B CG  1 
ATOM   3921 C CD1 . LEU A 1 521 ? 42.196 -20.868 5.201   1.00 18.50  ? 577 LEU B CD1 1 
ATOM   3922 C CD2 . LEU A 1 521 ? 41.526 -22.912 3.926   1.00 8.75   ? 577 LEU B CD2 1 
ATOM   3923 N N   . LEU A 1 522 ? 44.357 -25.302 4.640   1.00 21.28  ? 578 LEU B N   1 
ATOM   3924 C CA  . LEU A 1 522 ? 43.804 -26.620 4.432   1.00 21.75  ? 578 LEU B CA  1 
ATOM   3925 C C   . LEU A 1 522 ? 42.715 -26.812 5.470   1.00 19.21  ? 578 LEU B C   1 
ATOM   3926 O O   . LEU A 1 522 ? 43.006 -26.822 6.668   1.00 13.63  ? 578 LEU B O   1 
ATOM   3927 C CB  . LEU A 1 522 ? 44.901 -27.677 4.577   1.00 11.75  ? 578 LEU B CB  1 
ATOM   3928 C CG  . LEU A 1 522 ? 44.505 -29.153 4.574   1.00 41.91  ? 578 LEU B CG  1 
ATOM   3929 C CD1 . LEU A 1 522 ? 43.717 -29.472 3.342   1.00 11.59  ? 578 LEU B CD1 1 
ATOM   3930 C CD2 . LEU A 1 522 ? 45.729 -30.062 4.666   1.00 13.15  ? 578 LEU B CD2 1 
ATOM   3931 N N   . ASN A 1 523 ? 41.464 -26.927 5.015   1.00 18.00  ? 579 ASN B N   1 
ATOM   3932 C CA  . ASN A 1 523 ? 40.352 -27.266 5.901   1.00 17.95  ? 579 ASN B CA  1 
ATOM   3933 C C   . ASN A 1 523 ? 39.735 -28.618 5.545   1.00 17.58  ? 579 ASN B C   1 
ATOM   3934 O O   . ASN A 1 523 ? 39.018 -28.743 4.567   1.00 13.42  ? 579 ASN B O   1 
ATOM   3935 C CB  . ASN A 1 523 ? 39.293 -26.167 5.843   1.00 8.26   ? 579 ASN B CB  1 
ATOM   3936 C CG  . ASN A 1 523 ? 38.121 -26.421 6.772   1.00 7.91   ? 579 ASN B CG  1 
ATOM   3937 O OD1 . ASN A 1 523 ? 38.091 -27.404 7.509   1.00 12.33  ? 579 ASN B OD1 1 
ATOM   3938 N ND2 . ASN A 1 523 ? 37.142 -25.528 6.737   1.00 7.44   ? 579 ASN B ND2 1 
ATOM   3939 N N   . LEU A 1 524 ? 40.036 -29.624 6.357   1.00 22.63  ? 580 LEU B N   1 
ATOM   3940 C CA  . LEU A 1 524 ? 39.470 -30.960 6.224   1.00 9.70   ? 580 LEU B CA  1 
ATOM   3941 C C   . LEU A 1 524 ? 38.366 -31.259 7.237   1.00 25.37  ? 580 LEU B C   1 
ATOM   3942 O O   . LEU A 1 524 ? 37.932 -32.405 7.364   1.00 9.52   ? 580 LEU B O   1 
ATOM   3943 C CB  . LEU A 1 524 ? 40.569 -32.023 6.244   1.00 10.76  ? 580 LEU B CB  1 
ATOM   3944 C CG  . LEU A 1 524 ? 41.628 -31.796 5.161   1.00 11.25  ? 580 LEU B CG  1 
ATOM   3945 C CD1 . LEU A 1 524 ? 42.701 -32.862 5.186   1.00 12.33  ? 580 LEU B CD1 1 
ATOM   3946 C CD2 . LEU A 1 524 ? 40.971 -31.731 3.798   1.00 10.79  ? 580 LEU B CD2 1 
ATOM   3947 N N   . GLY A 1 525 ? 37.973 -30.239 8.002   1.00 8.69   ? 581 GLY B N   1 
ATOM   3948 C CA  . GLY A 1 525 ? 37.031 -30.387 9.104   1.00 8.34   ? 581 GLY B CA  1 
ATOM   3949 C C   . GLY A 1 525 ? 35.703 -31.064 8.803   1.00 23.58  ? 581 GLY B C   1 
ATOM   3950 O O   . GLY A 1 525 ? 35.177 -30.949 7.696   1.00 21.61  ? 581 GLY B O   1 
ATOM   3951 N N   . GLU A 1 526 ? 35.160 -31.774 9.791   1.00 24.38  ? 582 GLU B N   1 
ATOM   3952 C CA  . GLU A 1 526 ? 33.865 -32.439 9.648   1.00 7.70   ? 582 GLU B CA  1 
ATOM   3953 C C   . GLU A 1 526 ? 33.811 -33.399 8.460   1.00 14.75  ? 582 GLU B C   1 
ATOM   3954 O O   . GLU A 1 526 ? 33.117 -33.143 7.475   1.00 13.29  ? 582 GLU B O   1 
ATOM   3955 C CB  . GLU A 1 526 ? 32.762 -31.415 9.488   1.00 7.12   ? 582 GLU B CB  1 
ATOM   3956 C CG  . GLU A 1 526 ? 31.978 -31.132 10.720  1.00 15.44  ? 582 GLU B CG  1 
ATOM   3957 C CD  . GLU A 1 526 ? 30.669 -30.452 10.388  1.00 17.83  ? 582 GLU B CD  1 
ATOM   3958 O OE1 . GLU A 1 526 ? 29.651 -31.178 10.298  1.00 12.46  ? 582 GLU B OE1 1 
ATOM   3959 O OE2 . GLU A 1 526 ? 30.672 -29.208 10.198  1.00 17.89  ? 582 GLU B OE2 1 
ATOM   3960 N N   . ASN A 1 527 ? 34.545 -34.499 8.554   1.00 16.01  ? 583 ASN B N   1 
ATOM   3961 C CA  . ASN A 1 527 ? 34.452 -35.567 7.576   1.00 15.70  ? 583 ASN B CA  1 
ATOM   3962 C C   . ASN A 1 527 ? 34.630 -36.894 8.288   1.00 22.62  ? 583 ASN B C   1 
ATOM   3963 O O   . ASN A 1 527 ? 34.596 -36.954 9.523   1.00 23.93  ? 583 ASN B O   1 
ATOM   3964 C CB  . ASN A 1 527 ? 35.508 -35.417 6.486   1.00 17.11  ? 583 ASN B CB  1 
ATOM   3965 C CG  . ASN A 1 527 ? 35.161 -34.340 5.480   1.00 19.25  ? 583 ASN B CG  1 
ATOM   3966 O OD1 . ASN A 1 527 ? 34.316 -34.546 4.624   1.00 20.84  ? 583 ASN B OD1 1 
ATOM   3967 N ND2 . ASN A 1 527 ? 35.829 -33.192 5.565   1.00 20.19  ? 583 ASN B ND2 1 
ATOM   3968 N N   . ASP A 1 528 ? 34.777 -37.958 7.504   1.00 26.81  ? 584 ASP B N   1 
ATOM   3969 C CA  . ASP A 1 528 ? 35.038 -39.298 8.033   1.00 33.13  ? 584 ASP B CA  1 
ATOM   3970 C C   . ASP A 1 528 ? 36.508 -39.765 8.054   1.00 25.25  ? 584 ASP B C   1 
ATOM   3971 O O   . ASP A 1 528 ? 36.773 -40.964 8.167   1.00 28.27  ? 584 ASP B O   1 
ATOM   3972 C CB  . ASP A 1 528 ? 34.119 -40.349 7.412   1.00 46.65  ? 584 ASP B CB  1 
ATOM   3973 C CG  . ASP A 1 528 ? 33.744 -41.429 8.408   1.00 58.74  ? 584 ASP B CG  1 
ATOM   3974 O OD1 . ASP A 1 528 ? 33.757 -41.124 9.626   1.00 56.65  ? 584 ASP B OD1 1 
ATOM   3975 O OD2 . ASP A 1 528 ? 33.459 -42.572 7.983   1.00 64.34  ? 584 ASP B OD2 1 
ATOM   3976 N N   . PHE A 1 529 ? 37.448 -38.848 7.839   1.00 19.43  ? 585 PHE B N   1 
ATOM   3977 C CA  . PHE A 1 529 ? 38.865 -39.207 7.790   1.00 17.66  ? 585 PHE B CA  1 
ATOM   3978 C C   . PHE A 1 529 ? 39.312 -39.977 9.012   1.00 21.24  ? 585 PHE B C   1 
ATOM   3979 O O   . PHE A 1 529 ? 38.846 -39.736 10.126  1.00 13.49  ? 585 PHE B O   1 
ATOM   3980 C CB  . PHE A 1 529 ? 39.735 -37.960 7.710   1.00 15.09  ? 585 PHE B CB  1 
ATOM   3981 C CG  . PHE A 1 529 ? 39.655 -37.258 6.406   1.00 15.76  ? 585 PHE B CG  1 
ATOM   3982 C CD1 . PHE A 1 529 ? 40.116 -37.870 5.254   1.00 13.08  ? 585 PHE B CD1 1 
ATOM   3983 C CD2 . PHE A 1 529 ? 39.132 -35.983 6.329   1.00 17.01  ? 585 PHE B CD2 1 
ATOM   3984 C CE1 . PHE A 1 529 ? 40.054 -37.234 4.065   1.00 12.72  ? 585 PHE B CE1 1 
ATOM   3985 C CE2 . PHE A 1 529 ? 39.063 -35.338 5.128   1.00 16.41  ? 585 PHE B CE2 1 
ATOM   3986 C CZ  . PHE A 1 529 ? 39.520 -35.965 3.992   1.00 20.19  ? 585 PHE B CZ  1 
ATOM   3987 N N   . SER A 1 530 ? 40.235 -40.901 8.793   1.00 24.89  ? 586 SER B N   1 
ATOM   3988 C CA  . SER A 1 530 ? 40.726 -41.755 9.857   1.00 21.50  ? 586 SER B CA  1 
ATOM   3989 C C   . SER A 1 530 ? 42.200 -42.016 9.628   1.00 18.35  ? 586 SER B C   1 
ATOM   3990 O O   . SER A 1 530 ? 42.809 -41.442 8.720   1.00 18.72  ? 586 SER B O   1 
ATOM   3991 C CB  . SER A 1 530 ? 39.960 -43.075 9.865   1.00 29.50  ? 586 SER B CB  1 
ATOM   3992 O OG  . SER A 1 530 ? 39.966 -43.665 8.567   1.00 38.80  ? 586 SER B OG  1 
ATOM   3993 N N   . GLY A 1 531 ? 42.767 -42.889 10.456  1.00 17.15  ? 587 GLY B N   1 
ATOM   3994 C CA  . GLY A 1 531 ? 44.190 -43.166 10.420  1.00 19.53  ? 587 GLY B CA  1 
ATOM   3995 C C   . GLY A 1 531 ? 44.963 -42.109 11.184  1.00 21.75  ? 587 GLY B C   1 
ATOM   3996 O O   . GLY A 1 531 ? 44.378 -41.228 11.816  1.00 17.30  ? 587 GLY B O   1 
ATOM   3997 N N   . GLU A 1 532 ? 46.286 -42.200 11.128  1.00 21.33  ? 588 GLU B N   1 
ATOM   3998 C CA  . GLU A 1 532 ? 47.132 -41.234 11.797  1.00 25.20  ? 588 GLU B CA  1 
ATOM   3999 C C   . GLU A 1 532 ? 47.382 -40.074 10.861  1.00 21.64  ? 588 GLU B C   1 
ATOM   4000 O O   . GLU A 1 532 ? 47.548 -40.270 9.665   1.00 33.85  ? 588 GLU B O   1 
ATOM   4001 C CB  . GLU A 1 532 ? 48.462 -41.869 12.209  1.00 38.79  ? 588 GLU B CB  1 
ATOM   4002 C CG  . GLU A 1 532 ? 48.384 -42.819 13.406  1.00 40.98  ? 588 GLU B CG  1 
ATOM   4003 C CD  . GLU A 1 532 ? 49.723 -43.470 13.706  1.00 46.33  ? 588 GLU B CD  1 
ATOM   4004 O OE1 . GLU A 1 532 ? 50.706 -43.152 13.000  1.00 54.00  ? 588 GLU B OE1 1 
ATOM   4005 O OE2 . GLU A 1 532 ? 49.794 -44.302 14.636  1.00 43.50  ? 588 GLU B OE2 1 
ATOM   4006 N N   . ILE A 1 533 ? 47.379 -38.863 11.405  1.00 22.64  ? 589 ILE B N   1 
ATOM   4007 C CA  . ILE A 1 533 ? 47.773 -37.691 10.645  1.00 23.86  ? 589 ILE B CA  1 
ATOM   4008 C C   . ILE A 1 533 ? 49.186 -37.961 10.160  1.00 24.62  ? 589 ILE B C   1 
ATOM   4009 O O   . ILE A 1 533 ? 50.068 -38.251 10.960  1.00 27.13  ? 589 ILE B O   1 
ATOM   4010 C CB  . ILE A 1 533 ? 47.744 -36.404 11.503  1.00 24.11  ? 589 ILE B CB  1 
ATOM   4011 C CG1 . ILE A 1 533 ? 46.404 -36.262 12.232  1.00 16.31  ? 589 ILE B CG1 1 
ATOM   4012 C CG2 . ILE A 1 533 ? 47.993 -35.180 10.632  1.00 25.82  ? 589 ILE B CG2 1 
ATOM   4013 C CD1 . ILE A 1 533 ? 46.365 -35.137 13.253  1.00 15.89  ? 589 ILE B CD1 1 
ATOM   4014 N N   . PRO A 1 534 ? 49.397 -37.901 8.839   1.00 21.71  ? 590 PRO B N   1 
ATOM   4015 C CA  . PRO A 1 534 ? 50.695 -38.296 8.287   1.00 24.61  ? 590 PRO B CA  1 
ATOM   4016 C C   . PRO A 1 534 ? 51.798 -37.302 8.624   1.00 35.57  ? 590 PRO B C   1 
ATOM   4017 O O   . PRO A 1 534 ? 51.552 -36.111 8.827   1.00 33.12  ? 590 PRO B O   1 
ATOM   4018 C CB  . PRO A 1 534 ? 50.444 -38.311 6.779   1.00 25.28  ? 590 PRO B CB  1 
ATOM   4019 C CG  . PRO A 1 534 ? 49.369 -37.306 6.582   1.00 30.71  ? 590 PRO B CG  1 
ATOM   4020 C CD  . PRO A 1 534 ? 48.472 -37.430 7.794   1.00 27.12  ? 590 PRO B CD  1 
ATOM   4021 N N   . ASP A 1 535 ? 53.017 -37.824 8.676   1.00 45.27  ? 591 ASP B N   1 
ATOM   4022 C CA  . ASP A 1 535 ? 54.214 -37.037 8.912   1.00 48.30  ? 591 ASP B CA  1 
ATOM   4023 C C   . ASP A 1 535 ? 54.382 -35.923 7.877   1.00 44.00  ? 591 ASP B C   1 
ATOM   4024 O O   . ASP A 1 535 ? 54.976 -34.887 8.166   1.00 45.21  ? 591 ASP B O   1 
ATOM   4025 C CB  . ASP A 1 535 ? 55.429 -37.961 8.873   1.00 58.07  ? 591 ASP B CB  1 
ATOM   4026 C CG  . ASP A 1 535 ? 56.669 -37.314 9.435   1.00 67.33  ? 591 ASP B CG  1 
ATOM   4027 O OD1 . ASP A 1 535 ? 56.569 -36.699 10.520  1.00 75.48  ? 591 ASP B OD1 1 
ATOM   4028 O OD2 . ASP A 1 535 ? 57.738 -37.419 8.796   1.00 64.66  ? 591 ASP B OD2 1 
ATOM   4029 N N   . GLU A 1 536 ? 53.853 -36.138 6.676   1.00 41.30  ? 592 GLU B N   1 
ATOM   4030 C CA  . GLU A 1 536 ? 54.055 -35.204 5.574   1.00 43.43  ? 592 GLU B CA  1 
ATOM   4031 C C   . GLU A 1 536 ? 53.255 -33.914 5.708   1.00 41.82  ? 592 GLU B C   1 
ATOM   4032 O O   . GLU A 1 536 ? 53.528 -32.936 5.019   1.00 42.01  ? 592 GLU B O   1 
ATOM   4033 C CB  . GLU A 1 536 ? 53.721 -35.864 4.236   1.00 48.01  ? 592 GLU B CB  1 
ATOM   4034 C CG  . GLU A 1 536 ? 54.649 -36.992 3.842   1.00 56.06  ? 592 GLU B CG  1 
ATOM   4035 C CD  . GLU A 1 536 ? 54.262 -38.307 4.483   1.00 65.19  ? 592 GLU B CD  1 
ATOM   4036 O OE1 . GLU A 1 536 ? 53.372 -38.296 5.362   1.00 64.33  ? 592 GLU B OE1 1 
ATOM   4037 O OE2 . GLU A 1 536 ? 54.838 -39.349 4.099   1.00 71.64  ? 592 GLU B OE2 1 
ATOM   4038 N N   . LEU A 1 537 ? 52.264 -33.903 6.587   1.00 39.81  ? 593 LEU B N   1 
ATOM   4039 C CA  . LEU A 1 537 ? 51.397 -32.734 6.690   1.00 30.65  ? 593 LEU B CA  1 
ATOM   4040 C C   . LEU A 1 537 ? 52.157 -31.531 7.210   1.00 29.67  ? 593 LEU B C   1 
ATOM   4041 O O   . LEU A 1 537 ? 51.770 -30.391 6.976   1.00 32.09  ? 593 LEU B O   1 
ATOM   4042 C CB  . LEU A 1 537 ? 50.194 -33.015 7.579   1.00 21.27  ? 593 LEU B CB  1 
ATOM   4043 C CG  . LEU A 1 537 ? 49.040 -32.041 7.386   1.00 23.03  ? 593 LEU B CG  1 
ATOM   4044 C CD1 . LEU A 1 537 ? 48.953 -31.610 5.939   1.00 26.41  ? 593 LEU B CD1 1 
ATOM   4045 C CD2 . LEU A 1 537 ? 47.749 -32.714 7.794   1.00 29.75  ? 593 LEU B CD2 1 
ATOM   4046 N N   . GLY A 1 538 ? 53.255 -31.785 7.905   1.00 32.69  ? 594 GLY B N   1 
ATOM   4047 C CA  . GLY A 1 538 ? 54.047 -30.702 8.434   1.00 36.55  ? 594 GLY B CA  1 
ATOM   4048 C C   . GLY A 1 538 ? 55.035 -30.210 7.413   1.00 41.95  ? 594 GLY B C   1 
ATOM   4049 O O   . GLY A 1 538 ? 55.883 -29.368 7.713   1.00 45.48  ? 594 GLY B O   1 
ATOM   4050 N N   . GLN A 1 539 ? 54.913 -30.709 6.192   1.00 49.53  ? 595 GLN B N   1 
ATOM   4051 C CA  . GLN A 1 539 ? 55.943 -30.438 5.202   1.00 57.18  ? 595 GLN B CA  1 
ATOM   4052 C C   . GLN A 1 539 ? 55.727 -29.290 4.207   1.00 52.08  ? 595 GLN B C   1 
ATOM   4053 O O   . GLN A 1 539 ? 56.603 -28.975 3.398   1.00 54.86  ? 595 GLN B O   1 
ATOM   4054 C CB  . GLN A 1 539 ? 56.431 -31.735 4.544   1.00 69.40  ? 595 GLN B CB  1 
ATOM   4055 C CG  . GLN A 1 539 ? 57.800 -32.117 5.044   1.00 80.61  ? 595 GLN B CG  1 
ATOM   4056 C CD  . GLN A 1 539 ? 58.461 -30.917 5.743   1.00 90.47  ? 595 GLN B CD  1 
ATOM   4057 O OE1 . GLN A 1 539 ? 58.362 -30.763 6.962   1.00 93.47  ? 595 GLN B OE1 1 
ATOM   4058 N NE2 . GLN A 1 539 ? 59.062 -30.025 4.956   1.00 94.35  ? 595 GLN B NE2 1 
ATOM   4059 N N   . ILE A 1 540 ? 54.588 -28.630 4.314   1.00 44.12  ? 596 ILE B N   1 
ATOM   4060 C CA  . ILE A 1 540 ? 54.374 -27.430 3.549   1.00 39.21  ? 596 ILE B CA  1 
ATOM   4061 C C   . ILE A 1 540 ? 54.795 -26.313 4.485   1.00 43.87  ? 596 ILE B C   1 
ATOM   4062 O O   . ILE A 1 540 ? 54.067 -25.979 5.418   1.00 39.97  ? 596 ILE B O   1 
ATOM   4063 C CB  . ILE A 1 540 ? 52.891 -27.317 3.172   1.00 34.05  ? 596 ILE B CB  1 
ATOM   4064 C CG1 . ILE A 1 540 ? 52.336 -28.722 2.922   1.00 24.68  ? 596 ILE B CG1 1 
ATOM   4065 C CG2 . ILE A 1 540 ? 52.699 -26.444 1.934   1.00 33.92  ? 596 ILE B CG2 1 
ATOM   4066 C CD1 . ILE A 1 540 ? 50.850 -28.855 3.090   1.00 16.95  ? 596 ILE B CD1 1 
ATOM   4067 N N   . PRO A 1 541 ? 55.974 -25.713 4.234   1.00 55.12  ? 597 PRO B N   1 
ATOM   4068 C CA  . PRO A 1 541 ? 56.430 -24.614 5.095   1.00 54.69  ? 597 PRO B CA  1 
ATOM   4069 C C   . PRO A 1 541 ? 55.481 -23.452 4.872   1.00 47.98  ? 597 PRO B C   1 
ATOM   4070 O O   . PRO A 1 541 ? 55.411 -22.497 5.647   1.00 41.04  ? 597 PRO B O   1 
ATOM   4071 C CB  . PRO A 1 541 ? 57.819 -24.267 4.532   1.00 56.99  ? 597 PRO B CB  1 
ATOM   4072 C CG  . PRO A 1 541 ? 58.181 -25.384 3.602   1.00 59.59  ? 597 PRO B CG  1 
ATOM   4073 C CD  . PRO A 1 541 ? 56.889 -25.941 3.101   1.00 59.11  ? 597 PRO B CD  1 
ATOM   4074 N N   . SER A 1 542 ? 54.746 -23.574 3.773   1.00 47.67  ? 598 SER B N   1 
ATOM   4075 C CA  . SER A 1 542 ? 53.826 -22.568 3.285   1.00 37.53  ? 598 SER B CA  1 
ATOM   4076 C C   . SER A 1 542 ? 52.557 -22.423 4.131   1.00 27.85  ? 598 SER B C   1 
ATOM   4077 O O   . SER A 1 542 ? 51.887 -21.385 4.054   1.00 15.14  ? 598 SER B O   1 
ATOM   4078 C CB  . SER A 1 542 ? 53.460 -22.904 1.838   1.00 34.89  ? 598 SER B CB  1 
ATOM   4079 O OG  . SER A 1 542 ? 52.679 -21.882 1.262   1.00 41.49  ? 598 SER B OG  1 
ATOM   4080 N N   . LEU A 1 543 ? 52.232 -23.434 4.945   1.00 19.80  ? 599 LEU B N   1 
ATOM   4081 C CA  . LEU A 1 543 ? 50.974 -23.391 5.696   1.00 15.87  ? 599 LEU B CA  1 
ATOM   4082 C C   . LEU A 1 543 ? 51.070 -22.293 6.738   1.00 16.15  ? 599 LEU B C   1 
ATOM   4083 O O   . LEU A 1 543 ? 51.838 -22.380 7.692   1.00 22.47  ? 599 LEU B O   1 
ATOM   4084 C CB  . LEU A 1 543 ? 50.712 -24.721 6.404   1.00 15.93  ? 599 LEU B CB  1 
ATOM   4085 C CG  . LEU A 1 543 ? 49.918 -25.835 5.719   1.00 14.75  ? 599 LEU B CG  1 
ATOM   4086 C CD1 . LEU A 1 543 ? 49.914 -27.085 6.587   1.00 38.07  ? 599 LEU B CD1 1 
ATOM   4087 C CD2 . LEU A 1 543 ? 48.501 -25.385 5.439   1.00 13.56  ? 599 LEU B CD2 1 
ATOM   4088 N N   . ALA A 1 544 ? 50.218 -21.295 6.578   1.00 15.77  ? 600 ALA B N   1 
ATOM   4089 C CA  . ALA A 1 544 ? 50.355 -20.034 7.286   1.00 22.65  ? 600 ALA B CA  1 
ATOM   4090 C C   . ALA A 1 544 ? 49.035 -19.682 7.919   1.00 22.26  ? 600 ALA B C   1 
ATOM   4091 O O   . ALA A 1 544 ? 48.944 -19.423 9.120   1.00 19.10  ? 600 ALA B O   1 
ATOM   4092 C CB  . ALA A 1 544 ? 50.801 -18.942 6.353   1.00 30.62  ? 600 ALA B CB  1 
ATOM   4093 N N   . ILE A 1 545 ? 48.016 -19.618 7.072   1.00 19.47  ? 601 ILE B N   1 
ATOM   4094 C CA  . ILE A 1 545 ? 46.715 -19.119 7.476   1.00 21.84  ? 601 ILE B CA  1 
ATOM   4095 C C   . ILE A 1 545 ? 45.990 -20.061 8.431   1.00 23.17  ? 601 ILE B C   1 
ATOM   4096 O O   . ILE A 1 545 ? 45.700 -19.682 9.569   1.00 21.42  ? 601 ILE B O   1 
ATOM   4097 C CB  . ILE A 1 545 ? 45.818 -18.883 6.259   1.00 19.57  ? 601 ILE B CB  1 
ATOM   4098 C CG1 . ILE A 1 545 ? 46.570 -18.069 5.200   1.00 16.90  ? 601 ILE B CG1 1 
ATOM   4099 C CG2 . ILE A 1 545 ? 44.531 -18.213 6.691   1.00 8.97   ? 601 ILE B CG2 1 
ATOM   4100 C CD1 . ILE A 1 545 ? 45.797 -17.881 3.903   1.00 14.88  ? 601 ILE B CD1 1 
ATOM   4101 N N   . SER A 1 546 ? 45.661 -21.266 7.968   1.00 21.38  ? 602 SER B N   1 
ATOM   4102 C CA  . SER A 1 546 ? 44.887 -22.176 8.804   1.00 20.97  ? 602 SER B CA  1 
ATOM   4103 C C   . SER A 1 546 ? 45.072 -23.673 8.508   1.00 20.34  ? 602 SER B C   1 
ATOM   4104 O O   . SER A 1 546 ? 45.328 -24.070 7.377   1.00 11.01  ? 602 SER B O   1 
ATOM   4105 C CB  . SER A 1 546 ? 43.407 -21.793 8.730   1.00 30.45  ? 602 SER B CB  1 
ATOM   4106 O OG  . SER A 1 546 ? 42.577 -22.826 9.221   1.00 41.15  ? 602 SER B OG  1 
ATOM   4107 N N   . LEU A 1 547 ? 44.971 -24.495 9.552   1.00 19.40  ? 603 LEU B N   1 
ATOM   4108 C CA  . LEU A 1 547 ? 44.867 -25.946 9.391   1.00 15.62  ? 603 LEU B CA  1 
ATOM   4109 C C   . LEU A 1 547 ? 43.772 -26.467 10.312  1.00 17.83  ? 603 LEU B C   1 
ATOM   4110 O O   . LEU A 1 547 ? 43.937 -26.482 11.526  1.00 21.58  ? 603 LEU B O   1 
ATOM   4111 C CB  . LEU A 1 547 ? 46.205 -26.624 9.735   1.00 14.62  ? 603 LEU B CB  1 
ATOM   4112 C CG  . LEU A 1 547 ? 46.368 -28.148 9.624   1.00 13.10  ? 603 LEU B CG  1 
ATOM   4113 C CD1 . LEU A 1 547 ? 46.012 -28.675 8.217   1.00 12.96  ? 603 LEU B CD1 1 
ATOM   4114 C CD2 . LEU A 1 547 ? 47.794 -28.558 10.024  1.00 14.23  ? 603 LEU B CD2 1 
ATOM   4115 N N   . ASN A 1 548 ? 42.675 -26.929 9.724   1.00 21.38  ? 604 ASN B N   1 
ATOM   4116 C CA  . ASN A 1 548 ? 41.539 -27.443 10.477  1.00 17.63  ? 604 ASN B CA  1 
ATOM   4117 C C   . ASN A 1 548 ? 41.372 -28.922 10.152  1.00 27.16  ? 604 ASN B C   1 
ATOM   4118 O O   . ASN A 1 548 ? 40.955 -29.290 9.048   1.00 40.12  ? 604 ASN B O   1 
ATOM   4119 C CB  . ASN A 1 548 ? 40.292 -26.649 10.071  1.00 13.55  ? 604 ASN B CB  1 
ATOM   4120 C CG  . ASN A 1 548 ? 39.068 -26.988 10.890  1.00 15.92  ? 604 ASN B CG  1 
ATOM   4121 O OD1 . ASN A 1 548 ? 38.972 -28.065 11.476  1.00 18.16  ? 604 ASN B OD1 1 
ATOM   4122 N ND2 . ASN A 1 548 ? 38.101 -26.065 10.908  1.00 7.97   ? 604 ASN B ND2 1 
ATOM   4123 N N   . LEU A 1 549 ? 41.759 -29.762 11.102  1.00 21.63  ? 605 LEU B N   1 
ATOM   4124 C CA  . LEU A 1 549 ? 41.559 -31.206 11.038  1.00 11.30  ? 605 LEU B CA  1 
ATOM   4125 C C   . LEU A 1 549 ? 40.385 -31.657 11.907  1.00 11.44  ? 605 LEU B C   1 
ATOM   4126 O O   . LEU A 1 549 ? 40.214 -32.840 12.183  1.00 11.29  ? 605 LEU B O   1 
ATOM   4127 C CB  . LEU A 1 549 ? 42.848 -31.946 11.379  1.00 12.36  ? 605 LEU B CB  1 
ATOM   4128 C CG  . LEU A 1 549 ? 43.949 -31.746 10.335  1.00 12.87  ? 605 LEU B CG  1 
ATOM   4129 C CD1 . LEU A 1 549 ? 45.271 -32.332 10.806  1.00 13.95  ? 605 LEU B CD1 1 
ATOM   4130 C CD2 . LEU A 1 549 ? 43.529 -32.357 9.006   1.00 12.78  ? 605 LEU B CD2 1 
ATOM   4131 N N   . SER A 1 550 ? 39.629 -30.694 12.412  1.00 10.15  ? 606 SER B N   1 
ATOM   4132 C CA  . SER A 1 550 ? 38.631 -30.971 13.435  1.00 22.52  ? 606 SER B CA  1 
ATOM   4133 C C   . SER A 1 550 ? 37.511 -31.889 12.948  1.00 24.55  ? 606 SER B C   1 
ATOM   4134 O O   . SER A 1 550 ? 37.333 -32.094 11.737  1.00 22.04  ? 606 SER B O   1 
ATOM   4135 C CB  . SER A 1 550 ? 38.019 -29.672 13.940  1.00 9.08   ? 606 SER B CB  1 
ATOM   4136 O OG  . SER A 1 550 ? 37.000 -29.244 13.060  1.00 8.29   ? 606 SER B OG  1 
ATOM   4137 N N   . CYS A 1 551 ? 36.794 -32.471 13.908  1.00 21.11  ? 607 CYS B N   1 
ATOM   4138 C CA  . CYS A 1 551 ? 35.611 -33.290 13.633  1.00 9.30   ? 607 CYS B CA  1 
ATOM   4139 C C   . CYS A 1 551 ? 35.820 -34.424 12.616  1.00 17.24  ? 607 CYS B C   1 
ATOM   4140 O O   . CYS A 1 551 ? 35.018 -34.630 11.711  1.00 13.70  ? 607 CYS B O   1 
ATOM   4141 C CB  . CYS A 1 551 ? 34.439 -32.410 13.231  1.00 8.34   ? 607 CYS B CB  1 
ATOM   4142 S SG  . CYS A 1 551 ? 34.130 -31.097 14.415  1.00 15.23  ? 607 CYS B SG  1 
ATOM   4143 N N   . ASN A 1 552 ? 36.902 -35.167 12.798  1.00 10.63  ? 608 ASN B N   1 
ATOM   4144 C CA  . ASN A 1 552 ? 37.108 -36.416 12.101  1.00 11.22  ? 608 ASN B CA  1 
ATOM   4145 C C   . ASN A 1 552 ? 37.348 -37.552 13.095  1.00 30.40  ? 608 ASN B C   1 
ATOM   4146 O O   . ASN A 1 552 ? 37.120 -37.410 14.302  1.00 25.14  ? 608 ASN B O   1 
ATOM   4147 C CB  . ASN A 1 552 ? 38.289 -36.306 11.143  1.00 20.28  ? 608 ASN B CB  1 
ATOM   4148 C CG  . ASN A 1 552 ? 38.014 -35.379 10.004  1.00 18.59  ? 608 ASN B CG  1 
ATOM   4149 O OD1 . ASN A 1 552 ? 37.204 -35.681 9.135   1.00 11.60  ? 608 ASN B OD1 1 
ATOM   4150 N ND2 . ASN A 1 552 ? 38.682 -34.236 9.994   1.00 28.07  ? 608 ASN B ND2 1 
ATOM   4151 N N   . ARG A 1 553 ? 37.742 -38.699 12.562  1.00 27.26  ? 609 ARG B N   1 
ATOM   4152 C CA  . ARG A 1 553 ? 38.138 -39.854 13.355  1.00 22.94  ? 609 ARG B CA  1 
ATOM   4153 C C   . ARG A 1 553 ? 39.648 -40.072 13.583  1.00 25.07  ? 609 ARG B C   1 
ATOM   4154 O O   . ARG A 1 553 ? 40.055 -41.158 13.992  1.00 36.79  ? 609 ARG B O   1 
ATOM   4155 C CB  . ARG A 1 553 ? 37.400 -41.113 12.906  1.00 24.36  ? 609 ARG B CB  1 
ATOM   4156 C CG  . ARG A 1 553 ? 35.924 -41.038 13.268  1.00 26.27  ? 609 ARG B CG  1 
ATOM   4157 C CD  . ARG A 1 553 ? 35.163 -42.287 12.897  1.00 31.23  ? 609 ARG B CD  1 
ATOM   4158 N NE  . ARG A 1 553 ? 35.138 -42.508 11.457  1.00 35.55  ? 609 ARG B NE  1 
ATOM   4159 C CZ  . ARG A 1 553 ? 35.726 -43.535 10.853  1.00 43.91  ? 609 ARG B CZ  1 
ATOM   4160 N NH1 . ARG A 1 553 ? 36.383 -44.439 11.574  1.00 38.77  ? 609 ARG B NH1 1 
ATOM   4161 N NH2 . ARG A 1 553 ? 35.653 -43.661 9.528   1.00 50.86  ? 609 ARG B NH2 1 
ATOM   4162 N N   . PHE A 1 554 ? 40.474 -39.077 13.266  1.00 22.31  ? 610 PHE B N   1 
ATOM   4163 C CA  . PHE A 1 554 ? 41.933 -39.215 13.406  1.00 25.52  ? 610 PHE B CA  1 
ATOM   4164 C C   . PHE A 1 554 ? 42.364 -39.794 14.755  1.00 24.66  ? 610 PHE B C   1 
ATOM   4165 O O   . PHE A 1 554 ? 41.828 -39.437 15.811  1.00 15.34  ? 610 PHE B O   1 
ATOM   4166 C CB  . PHE A 1 554 ? 42.644 -37.857 13.234  1.00 26.54  ? 610 PHE B CB  1 
ATOM   4167 C CG  . PHE A 1 554 ? 42.498 -37.246 11.864  1.00 29.04  ? 610 PHE B CG  1 
ATOM   4168 C CD1 . PHE A 1 554 ? 43.039 -37.872 10.741  1.00 31.48  ? 610 PHE B CD1 1 
ATOM   4169 C CD2 . PHE A 1 554 ? 41.843 -36.031 11.697  1.00 23.82  ? 610 PHE B CD2 1 
ATOM   4170 C CE1 . PHE A 1 554 ? 42.915 -37.311 9.478   1.00 14.53  ? 610 PHE B CE1 1 
ATOM   4171 C CE2 . PHE A 1 554 ? 41.720 -35.460 10.431  1.00 19.39  ? 610 PHE B CE2 1 
ATOM   4172 C CZ  . PHE A 1 554 ? 42.263 -36.103 9.325   1.00 13.61  ? 610 PHE B CZ  1 
ATOM   4173 N N   . VAL A 1 555 ? 43.331 -40.705 14.701  1.00 25.90  ? 611 VAL B N   1 
ATOM   4174 C CA  . VAL A 1 555 ? 43.951 -41.244 15.905  1.00 22.02  ? 611 VAL B CA  1 
ATOM   4175 C C   . VAL A 1 555 ? 45.471 -41.077 15.876  1.00 19.13  ? 611 VAL B C   1 
ATOM   4176 O O   . VAL A 1 555 ? 46.043 -40.564 14.911  1.00 20.85  ? 611 VAL B O   1 
ATOM   4177 C CB  . VAL A 1 555 ? 43.615 -42.732 16.114  1.00 17.87  ? 611 VAL B CB  1 
ATOM   4178 C CG1 . VAL A 1 555 ? 42.110 -42.937 16.263  1.00 17.18  ? 611 VAL B CG1 1 
ATOM   4179 C CG2 . VAL A 1 555 ? 44.165 -43.556 14.980  1.00 18.49  ? 611 VAL B CG2 1 
ATOM   4180 N N   . GLY A 1 556 ? 46.122 -41.512 16.949  1.00 18.77  ? 612 GLY B N   1 
ATOM   4181 C CA  . GLY A 1 556 ? 47.557 -41.379 17.073  1.00 19.57  ? 612 GLY B CA  1 
ATOM   4182 C C   . GLY A 1 556 ? 47.937 -40.051 17.688  1.00 19.26  ? 612 GLY B C   1 
ATOM   4183 O O   . GLY A 1 556 ? 47.090 -39.313 18.166  1.00 19.55  ? 612 GLY B O   1 
ATOM   4184 N N   . GLU A 1 557 ? 49.223 -39.739 17.646  1.00 19.92  ? 613 GLU B N   1 
ATOM   4185 C CA  . GLU A 1 557 ? 49.745 -38.525 18.241  1.00 24.30  ? 613 GLU B CA  1 
ATOM   4186 C C   . GLU A 1 557 ? 49.957 -37.461 17.177  1.00 19.40  ? 613 GLU B C   1 
ATOM   4187 O O   . GLU A 1 557 ? 50.198 -37.775 16.022  1.00 47.17  ? 613 GLU B O   1 
ATOM   4188 C CB  . GLU A 1 557 ? 51.078 -38.799 18.950  1.00 27.69  ? 613 GLU B CB  1 
ATOM   4189 C CG  . GLU A 1 557 ? 51.023 -39.818 20.074  1.00 30.06  ? 613 GLU B CG  1 
ATOM   4190 C CD  . GLU A 1 557 ? 52.349 -39.935 20.812  1.00 36.16  ? 613 GLU B CD  1 
ATOM   4191 O OE1 . GLU A 1 557 ? 53.285 -39.178 20.478  1.00 31.90  ? 613 GLU B OE1 1 
ATOM   4192 O OE2 . GLU A 1 557 ? 52.455 -40.778 21.731  1.00 44.49  ? 613 GLU B OE2 1 
ATOM   4193 N N   . ILE A 1 558 ? 49.822 -36.203 17.570  1.00 34.65  ? 614 ILE B N   1 
ATOM   4194 C CA  . ILE A 1 558 ? 50.214 -35.100 16.715  1.00 29.99  ? 614 ILE B CA  1 
ATOM   4195 C C   . ILE A 1 558 ? 51.628 -35.367 16.246  1.00 27.01  ? 614 ILE B C   1 
ATOM   4196 O O   . ILE A 1 558 ? 52.526 -35.550 17.064  1.00 28.68  ? 614 ILE B O   1 
ATOM   4197 C CB  . ILE A 1 558 ? 50.170 -33.765 17.482  1.00 27.53  ? 614 ILE B CB  1 
ATOM   4198 C CG1 . ILE A 1 558 ? 48.723 -33.297 17.629  1.00 22.16  ? 614 ILE B CG1 1 
ATOM   4199 C CG2 . ILE A 1 558 ? 50.995 -32.701 16.772  1.00 28.81  ? 614 ILE B CG2 1 
ATOM   4200 C CD1 . ILE A 1 558 ? 48.572 -32.065 18.458  1.00 17.53  ? 614 ILE B CD1 1 
ATOM   4201 N N   . PRO A 1 559 ? 51.823 -35.418 14.917  1.00 27.54  ? 615 PRO B N   1 
ATOM   4202 C CA  . PRO A 1 559 ? 53.112 -35.769 14.307  1.00 25.86  ? 615 PRO B CA  1 
ATOM   4203 C C   . PRO A 1 559 ? 54.227 -34.771 14.622  1.00 28.88  ? 615 PRO B C   1 
ATOM   4204 O O   . PRO A 1 559 ? 53.983 -33.587 14.819  1.00 27.45  ? 615 PRO B O   1 
ATOM   4205 C CB  . PRO A 1 559 ? 52.796 -35.792 12.809  1.00 20.43  ? 615 PRO B CB  1 
ATOM   4206 C CG  . PRO A 1 559 ? 51.574 -34.977 12.668  1.00 19.25  ? 615 PRO B CG  1 
ATOM   4207 C CD  . PRO A 1 559 ? 50.782 -35.175 13.905  1.00 24.36  ? 615 PRO B CD  1 
ATOM   4208 N N   . SER A 1 560 ? 55.457 -35.267 14.663  1.00 37.35  ? 616 SER B N   1 
ATOM   4209 C CA  . SER A 1 560 ? 56.601 -34.474 15.094  1.00 32.30  ? 616 SER B CA  1 
ATOM   4210 C C   . SER A 1 560 ? 56.950 -33.350 14.128  1.00 37.51  ? 616 SER B C   1 
ATOM   4211 O O   . SER A 1 560 ? 57.247 -32.238 14.568  1.00 39.02  ? 616 SER B O   1 
ATOM   4212 C CB  . SER A 1 560 ? 57.804 -35.385 15.310  1.00 27.63  ? 616 SER B CB  1 
ATOM   4213 O OG  . SER A 1 560 ? 57.377 -36.630 15.839  1.00 26.16  ? 616 SER B OG  1 
ATOM   4214 N N   . ARG A 1 561 ? 56.888 -33.626 12.821  1.00 38.53  ? 617 ARG B N   1 
ATOM   4215 C CA  . ARG A 1 561 ? 57.206 -32.619 11.802  1.00 34.05  ? 617 ARG B CA  1 
ATOM   4216 C C   . ARG A 1 561 ? 56.292 -31.386 11.912  1.00 39.94  ? 617 ARG B C   1 
ATOM   4217 O O   . ARG A 1 561 ? 56.546 -30.364 11.282  1.00 49.57  ? 617 ARG B O   1 
ATOM   4218 C CB  . ARG A 1 561 ? 57.137 -33.207 10.383  1.00 38.09  ? 617 ARG B CB  1 
ATOM   4219 C CG  . ARG A 1 561 ? 58.293 -34.118 9.994   1.00 52.41  ? 617 ARG B CG  1 
ATOM   4220 C CD  . ARG A 1 561 ? 59.418 -33.352 9.275   1.00 61.13  ? 617 ARG B CD  1 
ATOM   4221 N NE  . ARG A 1 561 ? 59.514 -33.720 7.860   1.00 72.69  ? 617 ARG B NE  1 
ATOM   4222 C CZ  . ARG A 1 561 ? 60.485 -33.328 7.039   1.00 83.57  ? 617 ARG B CZ  1 
ATOM   4223 N NH1 . ARG A 1 561 ? 61.455 -32.547 7.494   1.00 92.08  ? 617 ARG B NH1 1 
ATOM   4224 N NH2 . ARG A 1 561 ? 60.486 -33.732 5.773   1.00 81.60  ? 617 ARG B NH2 1 
ATOM   4225 N N   . PHE A 1 562 ? 55.229 -31.489 12.710  1.00 36.27  ? 618 PHE B N   1 
ATOM   4226 C CA  . PHE A 1 562 ? 54.322 -30.364 12.952  1.00 33.75  ? 618 PHE B CA  1 
ATOM   4227 C C   . PHE A 1 562 ? 55.050 -29.142 13.493  1.00 38.53  ? 618 PHE B C   1 
ATOM   4228 O O   . PHE A 1 562 ? 54.671 -28.011 13.196  1.00 43.56  ? 618 PHE B O   1 
ATOM   4229 C CB  . PHE A 1 562 ? 53.213 -30.756 13.930  1.00 30.46  ? 618 PHE B CB  1 
ATOM   4230 C CG  . PHE A 1 562 ? 51.867 -30.928 13.289  1.00 30.12  ? 618 PHE B CG  1 
ATOM   4231 C CD1 . PHE A 1 562 ? 51.721 -31.675 12.134  1.00 27.57  ? 618 PHE B CD1 1 
ATOM   4232 C CD2 . PHE A 1 562 ? 50.741 -30.354 13.855  1.00 25.26  ? 618 PHE B CD2 1 
ATOM   4233 C CE1 . PHE A 1 562 ? 50.482 -31.841 11.552  1.00 23.74  ? 618 PHE B CE1 1 
ATOM   4234 C CE2 . PHE A 1 562 ? 49.497 -30.516 13.272  1.00 24.13  ? 618 PHE B CE2 1 
ATOM   4235 C CZ  . PHE A 1 562 ? 49.370 -31.261 12.120  1.00 16.34  ? 618 PHE B CZ  1 
ATOM   4236 N N   . SER A 1 563 ? 56.099 -29.373 14.279  1.00 39.82  ? 619 SER B N   1 
ATOM   4237 C CA  . SER A 1 563 ? 56.890 -28.286 14.851  1.00 37.67  ? 619 SER B CA  1 
ATOM   4238 C C   . SER A 1 563 ? 57.538 -27.463 13.742  1.00 39.36  ? 619 SER B C   1 
ATOM   4239 O O   . SER A 1 563 ? 57.996 -26.341 13.975  1.00 40.28  ? 619 SER B O   1 
ATOM   4240 C CB  . SER A 1 563 ? 57.967 -28.837 15.787  1.00 35.70  ? 619 SER B CB  1 
ATOM   4241 O OG  . SER A 1 563 ? 58.961 -29.543 15.059  1.00 37.53  ? 619 SER B OG  1 
ATOM   4242 N N   . ASP A 1 564 ? 57.573 -28.033 12.537  1.00 32.30  ? 620 ASP B N   1 
ATOM   4243 C CA  . ASP A 1 564 ? 58.069 -27.328 11.370  1.00 29.73  ? 620 ASP B CA  1 
ATOM   4244 C C   . ASP A 1 564 ? 57.032 -26.398 10.779  1.00 30.58  ? 620 ASP B C   1 
ATOM   4245 O O   . ASP A 1 564 ? 57.347 -25.649 9.847   1.00 35.18  ? 620 ASP B O   1 
ATOM   4246 C CB  . ASP A 1 564 ? 58.516 -28.291 10.270  1.00 32.66  ? 620 ASP B CB  1 
ATOM   4247 C CG  . ASP A 1 564 ? 59.740 -29.074 10.649  1.00 38.74  ? 620 ASP B CG  1 
ATOM   4248 O OD1 . ASP A 1 564 ? 60.317 -28.793 11.726  1.00 33.61  ? 620 ASP B OD1 1 
ATOM   4249 O OD2 . ASP A 1 564 ? 60.124 -29.966 9.858   1.00 43.79  ? 620 ASP B OD2 1 
ATOM   4250 N N   . LEU A 1 565 ? 55.803 -26.410 11.285  1.00 25.64  ? 621 LEU B N   1 
ATOM   4251 C CA  . LEU A 1 565 ? 54.886 -25.456 10.702  1.00 27.71  ? 621 LEU B CA  1 
ATOM   4252 C C   . LEU A 1 565 ? 55.116 -24.245 11.563  1.00 30.23  ? 621 LEU B C   1 
ATOM   4253 O O   . LEU A 1 565 ? 54.397 -23.992 12.526  1.00 29.07  ? 621 LEU B O   1 
ATOM   4254 C CB  . LEU A 1 565 ? 53.441 -25.941 10.853  1.00 25.22  ? 621 LEU B CB  1 
ATOM   4255 C CG  . LEU A 1 565 ? 53.123 -27.301 10.229  1.00 23.47  ? 621 LEU B CG  1 
ATOM   4256 C CD1 . LEU A 1 565 ? 51.844 -27.926 10.795  1.00 20.73  ? 621 LEU B CD1 1 
ATOM   4257 C CD2 . LEU A 1 565 ? 53.035 -27.158 8.725   1.00 21.31  ? 621 LEU B CD2 1 
ATOM   4258 N N   . LYS A 1 566 ? 56.044 -23.420 11.103  1.00 35.10  ? 622 LYS B N   1 
ATOM   4259 C CA  . LYS A 1 566 ? 56.527 -22.308 11.892  1.00 36.71  ? 622 LYS B CA  1 
ATOM   4260 C C   . LYS A 1 566 ? 55.726 -21.075 11.537  1.00 37.01  ? 622 LYS B C   1 
ATOM   4261 O O   . LYS A 1 566 ? 55.724 -20.093 12.268  1.00 39.84  ? 622 LYS B O   1 
ATOM   4262 C CB  . LYS A 1 566 ? 58.015 -22.084 11.603  1.00 48.27  ? 622 LYS B CB  1 
ATOM   4263 C CG  . LYS A 1 566 ? 58.329 -21.853 10.106  1.00 57.42  ? 622 LYS B CG  1 
ATOM   4264 C CD  . LYS A 1 566 ? 59.837 -21.714 9.835   1.00 57.22  ? 622 LYS B CD  1 
ATOM   4265 C CE  . LYS A 1 566 ? 60.127 -21.366 8.373   1.00 48.42  ? 622 LYS B CE  1 
ATOM   4266 N NZ  . LYS A 1 566 ? 61.592 -21.272 8.111   1.00 47.36  ? 622 LYS B NZ  1 
ATOM   4267 N N   . ASN A 1 567 ? 55.028 -21.133 10.410  1.00 43.22  ? 623 ASN B N   1 
ATOM   4268 C CA  . ASN A 1 567 ? 54.201 -20.009 9.995   1.00 39.83  ? 623 ASN B CA  1 
ATOM   4269 C C   . ASN A 1 567 ? 52.711 -20.147 10.284  1.00 38.44  ? 623 ASN B C   1 
ATOM   4270 O O   . ASN A 1 567 ? 51.947 -19.214 10.049  1.00 44.22  ? 623 ASN B O   1 
ATOM   4271 C CB  . ASN A 1 567 ? 54.460 -19.665 8.530   1.00 39.91  ? 623 ASN B CB  1 
ATOM   4272 C CG  . ASN A 1 567 ? 55.616 -18.696 8.366   1.00 39.23  ? 623 ASN B CG  1 
ATOM   4273 O OD1 . ASN A 1 567 ? 56.783 -19.082 8.454   1.00 38.59  ? 623 ASN B OD1 1 
ATOM   4274 N ND2 . ASN A 1 567 ? 55.296 -17.425 8.147   1.00 39.14  ? 623 ASN B ND2 1 
ATOM   4275 N N   . LEU A 1 568 ? 52.310 -21.302 10.810  1.00 34.70  ? 624 LEU B N   1 
ATOM   4276 C CA  . LEU A 1 568 ? 50.911 -21.579 11.128  1.00 26.31  ? 624 LEU B CA  1 
ATOM   4277 C C   . LEU A 1 568 ? 50.380 -20.609 12.172  1.00 14.22  ? 624 LEU B C   1 
ATOM   4278 O O   . LEU A 1 568 ? 51.003 -20.419 13.208  1.00 26.42  ? 624 LEU B O   1 
ATOM   4279 C CB  . LEU A 1 568 ? 50.776 -23.013 11.638  1.00 25.20  ? 624 LEU B CB  1 
ATOM   4280 C CG  . LEU A 1 568 ? 49.352 -23.507 11.870  1.00 27.95  ? 624 LEU B CG  1 
ATOM   4281 C CD1 . LEU A 1 568 ? 48.509 -23.248 10.632  1.00 13.26  ? 624 LEU B CD1 1 
ATOM   4282 C CD2 . LEU A 1 568 ? 49.346 -24.989 12.239  1.00 14.43  ? 624 LEU B CD2 1 
ATOM   4283 N N   . GLY A 1 569 ? 49.267 -19.947 11.871  1.00 14.24  ? 625 GLY B N   1 
ATOM   4284 C CA  . GLY A 1 569 ? 48.616 -19.076 12.835  1.00 12.67  ? 625 GLY B CA  1 
ATOM   4285 C C   . GLY A 1 569 ? 47.350 -19.621 13.476  1.00 16.84  ? 625 GLY B C   1 
ATOM   4286 O O   . GLY A 1 569 ? 46.933 -19.161 14.541  1.00 12.87  ? 625 GLY B O   1 
ATOM   4287 N N   . VAL A 1 570 ? 46.729 -20.607 12.836  1.00 18.04  ? 626 VAL B N   1 
ATOM   4288 C CA  . VAL A 1 570 ? 45.550 -21.255 13.400  1.00 10.96  ? 626 VAL B CA  1 
ATOM   4289 C C   . VAL A 1 570 ? 45.564 -22.763 13.159  1.00 17.35  ? 626 VAL B C   1 
ATOM   4290 O O   . VAL A 1 570 ? 45.647 -23.229 12.022  1.00 14.44  ? 626 VAL B O   1 
ATOM   4291 C CB  . VAL A 1 570 ? 44.238 -20.689 12.828  1.00 17.09  ? 626 VAL B CB  1 
ATOM   4292 C CG1 . VAL A 1 570 ? 43.057 -21.243 13.601  1.00 25.22  ? 626 VAL B CG1 1 
ATOM   4293 C CG2 . VAL A 1 570 ? 44.221 -19.177 12.878  1.00 15.46  ? 626 VAL B CG2 1 
ATOM   4294 N N   . LEU A 1 571 ? 45.469 -23.530 14.230  1.00 11.54  ? 627 LEU B N   1 
ATOM   4295 C CA  . LEU A 1 571 ? 45.364 -24.971 14.106  1.00 14.00  ? 627 LEU B CA  1 
ATOM   4296 C C   . LEU A 1 571 ? 44.172 -25.431 14.931  1.00 14.87  ? 627 LEU B C   1 
ATOM   4297 O O   . LEU A 1 571 ? 44.020 -25.033 16.084  1.00 21.32  ? 627 LEU B O   1 
ATOM   4298 C CB  . LEU A 1 571 ? 46.655 -25.643 14.568  1.00 12.94  ? 627 LEU B CB  1 
ATOM   4299 C CG  . LEU A 1 571 ? 46.641 -27.166 14.630  1.00 15.79  ? 627 LEU B CG  1 
ATOM   4300 C CD1 . LEU A 1 571 ? 46.409 -27.764 13.256  1.00 17.70  ? 627 LEU B CD1 1 
ATOM   4301 C CD2 . LEU A 1 571 ? 47.930 -27.696 15.219  1.00 18.09  ? 627 LEU B CD2 1 
ATOM   4302 N N   . ASP A 1 572 ? 43.293 -26.221 14.329  1.00 10.92  ? 628 ASP B N   1 
ATOM   4303 C CA  . ASP A 1 572 ? 42.173 -26.786 15.068  1.00 15.30  ? 628 ASP B CA  1 
ATOM   4304 C C   . ASP A 1 572 ? 42.112 -28.294 14.834  1.00 15.96  ? 628 ASP B C   1 
ATOM   4305 O O   . ASP A 1 572 ? 41.772 -28.764 13.747  1.00 15.80  ? 628 ASP B O   1 
ATOM   4306 C CB  . ASP A 1 572 ? 40.871 -26.106 14.640  1.00 9.48   ? 628 ASP B CB  1 
ATOM   4307 C CG  . ASP A 1 572 ? 39.657 -26.663 15.339  1.00 26.90  ? 628 ASP B CG  1 
ATOM   4308 O OD1 . ASP A 1 572 ? 39.807 -27.521 16.232  1.00 21.86  ? 628 ASP B OD1 1 
ATOM   4309 O OD2 . ASP A 1 572 ? 38.541 -26.223 15.005  1.00 25.64  ? 628 ASP B OD2 1 
ATOM   4310 N N   . VAL A 1 573 ? 42.460 -29.044 15.870  1.00 21.29  ? 629 VAL B N   1 
ATOM   4311 C CA  . VAL A 1 573 ? 42.400 -30.501 15.847  1.00 25.14  ? 629 VAL B CA  1 
ATOM   4312 C C   . VAL A 1 573 ? 41.188 -31.092 16.589  1.00 19.10  ? 629 VAL B C   1 
ATOM   4313 O O   . VAL A 1 573 ? 41.072 -32.311 16.737  1.00 15.55  ? 629 VAL B O   1 
ATOM   4314 C CB  . VAL A 1 573 ? 43.724 -31.106 16.326  1.00 34.14  ? 629 VAL B CB  1 
ATOM   4315 C CG1 . VAL A 1 573 ? 44.794 -30.885 15.267  1.00 13.49  ? 629 VAL B CG1 1 
ATOM   4316 C CG2 . VAL A 1 573 ? 44.142 -30.476 17.650  1.00 34.37  ? 629 VAL B CG2 1 
ATOM   4317 N N   . SER A 1 574 ? 40.305 -30.213 17.061  1.00 14.15  ? 630 SER B N   1 
ATOM   4318 C CA  . SER A 1 574 ? 39.218 -30.577 17.969  1.00 16.31  ? 630 SER B CA  1 
ATOM   4319 C C   . SER A 1 574 ? 38.297 -31.678 17.464  1.00 22.01  ? 630 SER B C   1 
ATOM   4320 O O   . SER A 1 574 ? 38.138 -31.872 16.262  1.00 32.52  ? 630 SER B O   1 
ATOM   4321 C CB  . SER A 1 574 ? 38.370 -29.358 18.284  1.00 19.19  ? 630 SER B CB  1 
ATOM   4322 O OG  . SER A 1 574 ? 37.945 -28.752 17.084  1.00 26.65  ? 630 SER B OG  1 
ATOM   4323 N N   . HIS A 1 575 ? 37.711 -32.407 18.407  1.00 14.05  ? 631 HIS B N   1 
ATOM   4324 C CA  . HIS A 1 575 ? 36.798 -33.498 18.100  1.00 19.17  ? 631 HIS B CA  1 
ATOM   4325 C C   . HIS A 1 575 ? 37.471 -34.567 17.226  1.00 25.53  ? 631 HIS B C   1 
ATOM   4326 O O   . HIS A 1 575 ? 37.055 -34.829 16.085  1.00 10.94  ? 631 HIS B O   1 
ATOM   4327 C CB  . HIS A 1 575 ? 35.506 -32.968 17.467  1.00 9.65   ? 631 HIS B CB  1 
ATOM   4328 C CG  . HIS A 1 575 ? 34.702 -32.081 18.379  1.00 9.07   ? 631 HIS B CG  1 
ATOM   4329 N ND1 . HIS A 1 575 ? 34.928 -30.728 18.478  1.00 8.66   ? 631 HIS B ND1 1 
ATOM   4330 C CD2 . HIS A 1 575 ? 33.697 -32.366 19.231  1.00 8.91   ? 631 HIS B CD2 1 
ATOM   4331 C CE1 . HIS A 1 575 ? 34.079 -30.207 19.354  1.00 12.14  ? 631 HIS B CE1 1 
ATOM   4332 N NE2 . HIS A 1 575 ? 33.320 -31.183 19.826  1.00 8.39   ? 631 HIS B NE2 1 
ATOM   4333 N N   . ASN A 1 576 ? 38.513 -35.181 17.791  1.00 22.72  ? 632 ASN B N   1 
ATOM   4334 C CA  . ASN A 1 576 ? 39.173 -36.350 17.210  1.00 21.49  ? 632 ASN B CA  1 
ATOM   4335 C C   . ASN A 1 576 ? 39.502 -37.342 18.313  1.00 25.05  ? 632 ASN B C   1 
ATOM   4336 O O   . ASN A 1 576 ? 39.114 -37.143 19.452  1.00 35.85  ? 632 ASN B O   1 
ATOM   4337 C CB  . ASN A 1 576 ? 40.462 -35.975 16.468  1.00 21.04  ? 632 ASN B CB  1 
ATOM   4338 C CG  . ASN A 1 576 ? 40.209 -35.364 15.105  1.00 25.90  ? 632 ASN B CG  1 
ATOM   4339 O OD1 . ASN A 1 576 ? 39.448 -35.889 14.302  1.00 12.37  ? 632 ASN B OD1 1 
ATOM   4340 N ND2 . ASN A 1 576 ? 40.865 -34.249 14.838  1.00 28.56  ? 632 ASN B ND2 1 
ATOM   4341 N N   . GLN A 1 577 ? 40.177 -38.429 17.949  1.00 22.96  ? 633 GLN B N   1 
ATOM   4342 C CA  . GLN A 1 577 ? 40.668 -39.453 18.880  1.00 25.47  ? 633 GLN B CA  1 
ATOM   4343 C C   . GLN A 1 577 ? 42.164 -39.361 19.248  1.00 27.11  ? 633 GLN B C   1 
ATOM   4344 O O   . GLN A 1 577 ? 42.760 -40.326 19.747  1.00 27.48  ? 633 GLN B O   1 
ATOM   4345 C CB  . GLN A 1 577 ? 40.267 -40.845 18.412  1.00 27.02  ? 633 GLN B CB  1 
ATOM   4346 C CG  . GLN A 1 577 ? 38.794 -41.105 18.591  1.00 20.67  ? 633 GLN B CG  1 
ATOM   4347 C CD  . GLN A 1 577 ? 38.280 -42.184 17.671  1.00 17.91  ? 633 GLN B CD  1 
ATOM   4348 O OE1 . GLN A 1 577 ? 37.236 -42.026 17.035  1.00 19.87  ? 633 GLN B OE1 1 
ATOM   4349 N NE2 . GLN A 1 577 ? 39.009 -43.291 17.591  1.00 17.24  ? 633 GLN B NE2 1 
ATOM   4350 N N   . LEU A 1 578 ? 42.782 -38.243 18.890  1.00 20.44  ? 634 LEU B N   1 
ATOM   4351 C CA  . LEU A 1 578 ? 44.204 -38.017 19.125  1.00 24.27  ? 634 LEU B CA  1 
ATOM   4352 C C   . LEU A 1 578 ? 44.634 -38.189 20.583  1.00 29.59  ? 634 LEU B C   1 
ATOM   4353 O O   . LEU A 1 578 ? 43.884 -37.860 21.495  1.00 34.98  ? 634 LEU B O   1 
ATOM   4354 C CB  . LEU A 1 578 ? 44.565 -36.609 18.666  1.00 21.74  ? 634 LEU B CB  1 
ATOM   4355 C CG  . LEU A 1 578 ? 44.286 -36.321 17.199  1.00 19.10  ? 634 LEU B CG  1 
ATOM   4356 C CD1 . LEU A 1 578 ? 44.590 -34.873 16.892  1.00 20.94  ? 634 LEU B CD1 1 
ATOM   4357 C CD2 . LEU A 1 578 ? 45.124 -37.250 16.346  1.00 16.26  ? 634 LEU B CD2 1 
ATOM   4358 N N   . THR A 1 579 ? 45.852 -38.699 20.782  1.00 17.78  ? 635 THR B N   1 
ATOM   4359 C CA  . THR A 1 579 ? 46.427 -38.936 22.110  1.00 35.54  ? 635 THR B CA  1 
ATOM   4360 C C   . THR A 1 579 ? 47.852 -38.403 22.194  1.00 36.24  ? 635 THR B C   1 
ATOM   4361 O O   . THR A 1 579 ? 48.375 -37.848 21.227  1.00 18.97  ? 635 THR B O   1 
ATOM   4362 C CB  . THR A 1 579 ? 46.489 -40.438 22.470  1.00 19.10  ? 635 THR B CB  1 
ATOM   4363 O OG1 . THR A 1 579 ? 47.208 -41.148 21.453  1.00 24.18  ? 635 THR B OG1 1 
ATOM   4364 C CG2 . THR A 1 579 ? 45.099 -41.030 22.617  1.00 18.60  ? 635 THR B CG2 1 
ATOM   4365 N N   . GLY A 1 580 ? 48.481 -38.586 23.355  1.00 19.60  ? 636 GLY B N   1 
ATOM   4366 C CA  . GLY A 1 580 ? 49.834 -38.107 23.577  1.00 40.46  ? 636 GLY B CA  1 
ATOM   4367 C C   . GLY A 1 580 ? 49.855 -36.668 24.056  1.00 37.94  ? 636 GLY B C   1 
ATOM   4368 O O   . GLY A 1 580 ? 48.805 -36.093 24.313  1.00 36.20  ? 636 GLY B O   1 
ATOM   4369 N N   . ASN A 1 581 ? 51.041 -36.075 24.170  1.00 38.47  ? 637 ASN B N   1 
ATOM   4370 C CA  . ASN A 1 581 ? 51.129 -34.708 24.660  1.00 20.00  ? 637 ASN B CA  1 
ATOM   4371 C C   . ASN A 1 581 ? 51.172 -33.661 23.561  1.00 19.52  ? 637 ASN B C   1 
ATOM   4372 O O   . ASN A 1 581 ? 51.135 -33.983 22.390  1.00 22.57  ? 637 ASN B O   1 
ATOM   4373 C CB  . ASN A 1 581 ? 52.301 -34.548 25.633  1.00 20.87  ? 637 ASN B CB  1 
ATOM   4374 C CG  . ASN A 1 581 ? 53.653 -34.605 24.958  1.00 21.71  ? 637 ASN B CG  1 
ATOM   4375 O OD1 . ASN A 1 581 ? 53.871 -34.014 23.902  1.00 38.25  ? 637 ASN B OD1 1 
ATOM   4376 N ND2 . ASN A 1 581 ? 54.590 -35.290 25.593  1.00 22.67  ? 637 ASN B ND2 1 
ATOM   4377 N N   . LEU A 1 582 ? 51.213 -32.398 23.950  1.00 21.44  ? 638 LEU B N   1 
ATOM   4378 C CA  . LEU A 1 582 ? 51.308 -31.294 23.000  1.00 23.49  ? 638 LEU B CA  1 
ATOM   4379 C C   . LEU A 1 582 ? 52.704 -30.680 22.836  1.00 30.12  ? 638 LEU B C   1 
ATOM   4380 O O   . LEU A 1 582 ? 52.848 -29.667 22.154  1.00 30.18  ? 638 LEU B O   1 
ATOM   4381 C CB  . LEU A 1 582 ? 50.233 -30.243 23.284  1.00 17.78  ? 638 LEU B CB  1 
ATOM   4382 C CG  . LEU A 1 582 ? 48.881 -30.964 23.380  1.00 20.54  ? 638 LEU B CG  1 
ATOM   4383 C CD1 . LEU A 1 582 ? 47.749 -30.081 23.888  1.00 17.10  ? 638 LEU B CD1 1 
ATOM   4384 C CD2 . LEU A 1 582 ? 48.517 -31.597 22.051  1.00 20.94  ? 638 LEU B CD2 1 
ATOM   4385 N N   . ASN A 1 583 ? 53.715 -31.273 23.473  1.00 33.57  ? 639 ASN B N   1 
ATOM   4386 C CA  . ASN A 1 583 ? 55.062 -30.689 23.508  1.00 31.09  ? 639 ASN B CA  1 
ATOM   4387 C C   . ASN A 1 583 ? 55.572 -30.246 22.137  1.00 30.67  ? 639 ASN B C   1 
ATOM   4388 O O   . ASN A 1 583 ? 56.275 -29.246 22.008  1.00 21.68  ? 639 ASN B O   1 
ATOM   4389 C CB  . ASN A 1 583 ? 56.075 -31.666 24.112  1.00 29.32  ? 639 ASN B CB  1 
ATOM   4390 C CG  . ASN A 1 583 ? 55.680 -32.163 25.494  1.00 33.06  ? 639 ASN B CG  1 
ATOM   4391 O OD1 . ASN A 1 583 ? 56.097 -33.245 25.900  1.00 23.16  ? 639 ASN B OD1 1 
ATOM   4392 N ND2 . ASN A 1 583 ? 54.874 -31.385 26.218  1.00 21.78  ? 639 ASN B ND2 1 
ATOM   4393 N N   . VAL A 1 584 ? 55.194 -30.997 21.112  1.00 29.57  ? 640 VAL B N   1 
ATOM   4394 C CA  . VAL A 1 584 ? 55.578 -30.693 19.742  1.00 31.08  ? 640 VAL B CA  1 
ATOM   4395 C C   . VAL A 1 584 ? 54.974 -29.356 19.250  1.00 35.33  ? 640 VAL B C   1 
ATOM   4396 O O   . VAL A 1 584 ? 55.417 -28.789 18.247  1.00 37.28  ? 640 VAL B O   1 
ATOM   4397 C CB  . VAL A 1 584 ? 55.200 -31.875 18.826  1.00 23.79  ? 640 VAL B CB  1 
ATOM   4398 C CG1 . VAL A 1 584 ? 53.732 -32.186 18.967  1.00 27.81  ? 640 VAL B CG1 1 
ATOM   4399 C CG2 . VAL A 1 584 ? 55.569 -31.607 17.384  1.00 23.43  ? 640 VAL B CG2 1 
ATOM   4400 N N   . LEU A 1 585 ? 53.985 -28.844 19.983  1.00 33.56  ? 641 LEU B N   1 
ATOM   4401 C CA  . LEU A 1 585 ? 53.352 -27.561 19.656  1.00 34.82  ? 641 LEU B CA  1 
ATOM   4402 C C   . LEU A 1 585 ? 53.883 -26.363 20.434  1.00 41.05  ? 641 LEU B C   1 
ATOM   4403 O O   . LEU A 1 585 ? 53.407 -25.239 20.233  1.00 42.52  ? 641 LEU B O   1 
ATOM   4404 C CB  . LEU A 1 585 ? 51.842 -27.636 19.880  1.00 26.57  ? 641 LEU B CB  1 
ATOM   4405 C CG  . LEU A 1 585 ? 50.943 -28.056 18.721  1.00 26.31  ? 641 LEU B CG  1 
ATOM   4406 C CD1 . LEU A 1 585 ? 51.713 -28.824 17.652  1.00 31.35  ? 641 LEU B CD1 1 
ATOM   4407 C CD2 . LEU A 1 585 ? 49.808 -28.884 19.279  1.00 21.67  ? 641 LEU B CD2 1 
ATOM   4408 N N   . THR A 1 586 ? 54.836 -26.596 21.336  1.00 42.05  ? 642 THR B N   1 
ATOM   4409 C CA  . THR A 1 586 ? 55.225 -25.556 22.296  1.00 41.98  ? 642 THR B CA  1 
ATOM   4410 C C   . THR A 1 586 ? 56.292 -24.603 21.769  1.00 42.48  ? 642 THR B C   1 
ATOM   4411 O O   . THR A 1 586 ? 56.590 -23.595 22.401  1.00 47.60  ? 642 THR B O   1 
ATOM   4412 C CB  . THR A 1 586 ? 55.624 -26.126 23.695  1.00 21.40  ? 642 THR B CB  1 
ATOM   4413 O OG1 . THR A 1 586 ? 56.813 -26.921 23.587  1.00 21.78  ? 642 THR B OG1 1 
ATOM   4414 C CG2 . THR A 1 586 ? 54.498 -26.965 24.274  1.00 20.11  ? 642 THR B CG2 1 
ATOM   4415 N N   . ASP A 1 587 ? 56.870 -24.921 20.619  1.00 48.59  ? 643 ASP B N   1 
ATOM   4416 C CA  . ASP A 1 587 ? 57.806 -24.000 19.989  1.00 56.00  ? 643 ASP B CA  1 
ATOM   4417 C C   . ASP A 1 587 ? 57.211 -23.133 18.875  1.00 48.85  ? 643 ASP B C   1 
ATOM   4418 O O   . ASP A 1 587 ? 57.936 -22.369 18.239  1.00 42.30  ? 643 ASP B O   1 
ATOM   4419 C CB  . ASP A 1 587 ? 59.057 -24.728 19.498  1.00 64.94  ? 643 ASP B CB  1 
ATOM   4420 C CG  . ASP A 1 587 ? 60.328 -23.960 19.809  1.00 64.05  ? 643 ASP B CG  1 
ATOM   4421 O OD1 . ASP A 1 587 ? 60.269 -23.059 20.679  1.00 54.62  ? 643 ASP B OD1 1 
ATOM   4422 O OD2 . ASP A 1 587 ? 61.378 -24.258 19.193  1.00 67.19  ? 643 ASP B OD2 1 
ATOM   4423 N N   . LEU A 1 588 ? 55.904 -23.217 18.642  1.00 46.19  ? 644 LEU B N   1 
ATOM   4424 C CA  . LEU A 1 588 ? 55.368 -22.522 17.488  1.00 19.04  ? 644 LEU B CA  1 
ATOM   4425 C C   . LEU A 1 588 ? 54.972 -21.129 17.922  1.00 18.55  ? 644 LEU B C   1 
ATOM   4426 O O   . LEU A 1 588 ? 53.867 -20.906 18.399  1.00 42.11  ? 644 LEU B O   1 
ATOM   4427 C CB  . LEU A 1 588 ? 54.136 -23.273 16.972  1.00 18.12  ? 644 LEU B CB  1 
ATOM   4428 C CG  . LEU A 1 588 ? 54.363 -24.723 16.546  1.00 26.42  ? 644 LEU B CG  1 
ATOM   4429 C CD1 . LEU A 1 588 ? 53.083 -25.386 16.123  1.00 17.66  ? 644 LEU B CD1 1 
ATOM   4430 C CD2 . LEU A 1 588 ? 55.350 -24.773 15.418  1.00 19.24  ? 644 LEU B CD2 1 
ATOM   4431 N N   . GLN A 1 589 ? 55.830 -20.165 17.618  1.00 58.86  ? 645 GLN B N   1 
ATOM   4432 C CA  . GLN A 1 589 ? 55.711 -18.832 18.205  1.00 56.38  ? 645 GLN B CA  1 
ATOM   4433 C C   . GLN A 1 589 ? 54.636 -18.009 17.509  1.00 48.07  ? 645 GLN B C   1 
ATOM   4434 O O   . GLN A 1 589 ? 54.047 -17.104 18.101  1.00 44.10  ? 645 GLN B O   1 
ATOM   4435 C CB  . GLN A 1 589 ? 57.063 -18.103 18.179  1.00 60.74  ? 645 GLN B CB  1 
ATOM   4436 C CG  . GLN A 1 589 ? 57.473 -17.542 16.816  1.00 64.83  ? 645 GLN B CG  1 
ATOM   4437 C CD  . GLN A 1 589 ? 57.683 -18.618 15.764  1.00 67.84  ? 645 GLN B CD  1 
ATOM   4438 O OE1 . GLN A 1 589 ? 56.722 -19.141 15.192  1.00 65.20  ? 645 GLN B OE1 1 
ATOM   4439 N NE2 . GLN A 1 589 ? 58.944 -18.952 15.502  1.00 68.73  ? 645 GLN B NE2 1 
ATOM   4440 N N   . ASN A 1 590 ? 54.380 -18.328 16.247  1.00 42.30  ? 646 ASN B N   1 
ATOM   4441 C CA  . ASN A 1 590 ? 53.380 -17.586 15.501  1.00 31.96  ? 646 ASN B CA  1 
ATOM   4442 C C   . ASN A 1 590 ? 51.996 -18.161 15.691  1.00 24.99  ? 646 ASN B C   1 
ATOM   4443 O O   . ASN A 1 590 ? 51.017 -17.638 15.150  1.00 22.12  ? 646 ASN B O   1 
ATOM   4444 C CB  . ASN A 1 590 ? 53.748 -17.503 14.022  1.00 30.62  ? 646 ASN B CB  1 
ATOM   4445 C CG  . ASN A 1 590 ? 54.808 -16.457 13.758  1.00 33.81  ? 646 ASN B CG  1 
ATOM   4446 O OD1 . ASN A 1 590 ? 54.497 -15.288 13.515  1.00 35.99  ? 646 ASN B OD1 1 
ATOM   4447 N ND2 . ASN A 1 590 ? 56.070 -16.864 13.832  1.00 33.35  ? 646 ASN B ND2 1 
ATOM   4448 N N   . LEU A 1 591 ? 51.916 -19.234 16.471  1.00 25.37  ? 647 LEU B N   1 
ATOM   4449 C CA  . LEU A 1 591 ? 50.631 -19.843 16.732  1.00 20.75  ? 647 LEU B CA  1 
ATOM   4450 C C   . LEU A 1 591 ? 49.763 -18.848 17.478  1.00 28.17  ? 647 LEU B C   1 
ATOM   4451 O O   . LEU A 1 591 ? 50.136 -18.320 18.528  1.00 36.05  ? 647 LEU B O   1 
ATOM   4452 C CB  . LEU A 1 591 ? 50.781 -21.139 17.517  1.00 21.85  ? 647 LEU B CB  1 
ATOM   4453 C CG  . LEU A 1 591 ? 49.530 -22.012 17.446  1.00 22.96  ? 647 LEU B CG  1 
ATOM   4454 C CD1 . LEU A 1 591 ? 49.058 -22.152 15.992  1.00 21.49  ? 647 LEU B CD1 1 
ATOM   4455 C CD2 . LEU A 1 591 ? 49.781 -23.373 18.070  1.00 20.92  ? 647 LEU B CD2 1 
ATOM   4456 N N   . VAL A 1 592 ? 48.597 -18.598 16.904  1.00 29.39  ? 648 VAL B N   1 
ATOM   4457 C CA  . VAL A 1 592 ? 47.669 -17.574 17.365  1.00 21.77  ? 648 VAL B CA  1 
ATOM   4458 C C   . VAL A 1 592 ? 46.446 -18.233 18.005  1.00 18.62  ? 648 VAL B C   1 
ATOM   4459 O O   . VAL A 1 592 ? 46.074 -17.888 19.113  1.00 11.50  ? 648 VAL B O   1 
ATOM   4460 C CB  . VAL A 1 592 ? 47.288 -16.600 16.220  1.00 26.15  ? 648 VAL B CB  1 
ATOM   4461 C CG1 . VAL A 1 592 ? 46.149 -15.691 16.624  1.00 20.28  ? 648 VAL B CG1 1 
ATOM   4462 C CG2 . VAL A 1 592 ? 48.499 -15.789 15.815  1.00 31.70  ? 648 VAL B CG2 1 
ATOM   4463 N N   . SER A 1 593 ? 45.772 -19.104 17.254  1.00 21.05  ? 649 SER B N   1 
ATOM   4464 C CA  . SER A 1 593 ? 44.606 -19.829 17.748  1.00 10.61  ? 649 SER B CA  1 
ATOM   4465 C C   . SER A 1 593 ? 44.822 -21.343 17.706  1.00 11.05  ? 649 SER B C   1 
ATOM   4466 O O   . SER A 1 593 ? 45.253 -21.876 16.691  1.00 35.08  ? 649 SER B O   1 
ATOM   4467 C CB  . SER A 1 593 ? 43.373 -19.452 16.931  1.00 23.62  ? 649 SER B CB  1 
ATOM   4468 O OG  . SER A 1 593 ? 42.209 -20.074 17.442  1.00 28.57  ? 649 SER B OG  1 
ATOM   4469 N N   . LEU A 1 594 ? 44.537 -22.027 18.816  1.00 17.25  ? 650 LEU B N   1 
ATOM   4470 C CA  . LEU A 1 594 ? 44.725 -23.476 18.912  1.00 11.68  ? 650 LEU B CA  1 
ATOM   4471 C C   . LEU A 1 594 ? 43.559 -24.146 19.606  1.00 11.23  ? 650 LEU B C   1 
ATOM   4472 O O   . LEU A 1 594 ? 43.330 -23.908 20.793  1.00 41.94  ? 650 LEU B O   1 
ATOM   4473 C CB  . LEU A 1 594 ? 46.006 -23.797 19.692  1.00 14.76  ? 650 LEU B CB  1 
ATOM   4474 C CG  . LEU A 1 594 ? 46.209 -25.261 20.080  1.00 13.26  ? 650 LEU B CG  1 
ATOM   4475 C CD1 . LEU A 1 594 ? 46.303 -26.111 18.816  1.00 49.10  ? 650 LEU B CD1 1 
ATOM   4476 C CD2 . LEU A 1 594 ? 47.443 -25.445 20.945  1.00 14.25  ? 650 LEU B CD2 1 
ATOM   4477 N N   . ASN A 1 595 ? 42.839 -25.014 18.900  1.00 10.91  ? 651 ASN B N   1 
ATOM   4478 C CA  . ASN A 1 595 ? 41.731 -25.719 19.534  1.00 10.57  ? 651 ASN B CA  1 
ATOM   4479 C C   . ASN A 1 595 ? 42.061 -27.198 19.592  1.00 11.22  ? 651 ASN B C   1 
ATOM   4480 O O   . ASN A 1 595 ? 41.961 -27.902 18.595  1.00 25.90  ? 651 ASN B O   1 
ATOM   4481 C CB  . ASN A 1 595 ? 40.442 -25.443 18.756  1.00 9.64   ? 651 ASN B CB  1 
ATOM   4482 C CG  . ASN A 1 595 ? 39.205 -26.006 19.420  1.00 9.25   ? 651 ASN B CG  1 
ATOM   4483 O OD1 . ASN A 1 595 ? 39.264 -27.040 20.063  1.00 9.73   ? 651 ASN B OD1 1 
ATOM   4484 N ND2 . ASN A 1 595 ? 38.062 -25.331 19.262  1.00 16.27  ? 651 ASN B ND2 1 
ATOM   4485 N N   . ILE A 1 596 ? 42.466 -27.652 20.778  1.00 32.94  ? 652 ILE B N   1 
ATOM   4486 C CA  . ILE A 1 596 ? 42.802 -29.058 21.026  1.00 12.47  ? 652 ILE B CA  1 
ATOM   4487 C C   . ILE A 1 596 ? 41.692 -29.830 21.729  1.00 16.41  ? 652 ILE B C   1 
ATOM   4488 O O   . ILE A 1 596 ? 41.871 -30.997 22.089  1.00 12.79  ? 652 ILE B O   1 
ATOM   4489 C CB  . ILE A 1 596 ? 44.145 -29.255 21.793  1.00 13.43  ? 652 ILE B CB  1 
ATOM   4490 C CG1 . ILE A 1 596 ? 44.280 -28.278 22.960  1.00 13.41  ? 652 ILE B CG1 1 
ATOM   4491 C CG2 . ILE A 1 596 ? 45.314 -29.087 20.865  1.00 13.93  ? 652 ILE B CG2 1 
ATOM   4492 C CD1 . ILE A 1 596 ? 43.627 -28.745 24.233  1.00 13.41  ? 652 ILE B CD1 1 
ATOM   4493 N N   . SER A 1 597 ? 40.564 -29.160 21.938  1.00 15.28  ? 653 SER B N   1 
ATOM   4494 C CA  . SER A 1 597 ? 39.492 -29.658 22.781  1.00 11.22  ? 653 SER B CA  1 
ATOM   4495 C C   . SER A 1 597 ? 38.897 -30.955 22.248  1.00 33.48  ? 653 SER B C   1 
ATOM   4496 O O   . SER A 1 597 ? 39.048 -31.277 21.070  1.00 11.26  ? 653 SER B O   1 
ATOM   4497 C CB  . SER A 1 597 ? 38.395 -28.617 22.856  1.00 10.34  ? 653 SER B CB  1 
ATOM   4498 O OG  . SER A 1 597 ? 37.601 -28.691 21.689  1.00 15.04  ? 653 SER B OG  1 
ATOM   4499 N N   . TYR A 1 598 ? 38.242 -31.699 23.136  1.00 32.93  ? 654 TYR B N   1 
ATOM   4500 C CA  . TYR A 1 598 ? 37.597 -32.967 22.794  1.00 11.52  ? 654 TYR B CA  1 
ATOM   4501 C C   . TYR A 1 598 ? 38.525 -33.915 22.048  1.00 21.80  ? 654 TYR B C   1 
ATOM   4502 O O   . TYR A 1 598 ? 38.308 -34.227 20.876  1.00 23.51  ? 654 TYR B O   1 
ATOM   4503 C CB  . TYR A 1 598 ? 36.303 -32.734 22.009  1.00 18.37  ? 654 TYR B CB  1 
ATOM   4504 C CG  . TYR A 1 598 ? 35.231 -32.079 22.841  1.00 15.54  ? 654 TYR B CG  1 
ATOM   4505 C CD1 . TYR A 1 598 ? 34.391 -32.835 23.663  1.00 15.95  ? 654 TYR B CD1 1 
ATOM   4506 C CD2 . TYR A 1 598 ? 35.076 -30.702 22.835  1.00 20.39  ? 654 TYR B CD2 1 
ATOM   4507 C CE1 . TYR A 1 598 ? 33.420 -32.233 24.443  1.00 9.80   ? 654 TYR B CE1 1 
ATOM   4508 C CE2 . TYR A 1 598 ? 34.107 -30.090 23.614  1.00 27.15  ? 654 TYR B CE2 1 
ATOM   4509 C CZ  . TYR A 1 598 ? 33.281 -30.858 24.410  1.00 28.92  ? 654 TYR B CZ  1 
ATOM   4510 O OH  . TYR A 1 598 ? 32.319 -30.231 25.166  1.00 26.97  ? 654 TYR B OH  1 
ATOM   4511 N N   . ASN A 1 599 ? 39.567 -34.350 22.749  1.00 23.19  ? 655 ASN B N   1 
ATOM   4512 C CA  . ASN A 1 599 ? 40.504 -35.353 22.269  1.00 20.14  ? 655 ASN B CA  1 
ATOM   4513 C C   . ASN A 1 599 ? 40.987 -36.170 23.464  1.00 22.16  ? 655 ASN B C   1 
ATOM   4514 O O   . ASN A 1 599 ? 40.495 -35.996 24.573  1.00 19.01  ? 655 ASN B O   1 
ATOM   4515 C CB  . ASN A 1 599 ? 41.688 -34.695 21.562  1.00 24.85  ? 655 ASN B CB  1 
ATOM   4516 C CG  . ASN A 1 599 ? 41.448 -34.491 20.076  1.00 14.16  ? 655 ASN B CG  1 
ATOM   4517 O OD1 . ASN A 1 599 ? 41.407 -35.450 19.320  1.00 13.81  ? 655 ASN B OD1 1 
ATOM   4518 N ND2 . ASN A 1 599 ? 41.320 -33.238 19.652  1.00 12.93  ? 655 ASN B ND2 1 
ATOM   4519 N N   . ASP A 1 600 ? 41.905 -37.099 23.231  1.00 28.09  ? 656 ASP B N   1 
ATOM   4520 C CA  . ASP A 1 600 ? 42.458 -37.930 24.303  1.00 25.37  ? 656 ASP B CA  1 
ATOM   4521 C C   . ASP A 1 600 ? 43.818 -37.515 24.867  1.00 23.82  ? 656 ASP B C   1 
ATOM   4522 O O   . ASP A 1 600 ? 44.477 -38.307 25.530  1.00 33.24  ? 656 ASP B O   1 
ATOM   4523 C CB  . ASP A 1 600 ? 42.347 -39.426 23.994  1.00 30.42  ? 656 ASP B CB  1 
ATOM   4524 C CG  . ASP A 1 600 ? 40.911 -39.942 24.128  1.00 29.94  ? 656 ASP B CG  1 
ATOM   4525 O OD1 . ASP A 1 600 ? 40.372 -39.893 25.256  1.00 27.37  ? 656 ASP B OD1 1 
ATOM   4526 O OD2 . ASP A 1 600 ? 40.330 -40.394 23.111  1.00 24.21  ? 656 ASP B OD2 1 
ATOM   4527 N N   . PHE A 1 601 ? 44.261 -36.309 24.532  1.00 16.47  ? 657 PHE B N   1 
ATOM   4528 C CA  . PHE A 1 601 ? 45.538 -35.772 25.010  1.00 17.05  ? 657 PHE B CA  1 
ATOM   4529 C C   . PHE A 1 601 ? 45.736 -35.765 26.542  1.00 17.43  ? 657 PHE B C   1 
ATOM   4530 O O   . PHE A 1 601 ? 44.786 -35.637 27.311  1.00 17.00  ? 657 PHE B O   1 
ATOM   4531 C CB  . PHE A 1 601 ? 45.734 -34.341 24.506  1.00 35.86  ? 657 PHE B CB  1 
ATOM   4532 C CG  . PHE A 1 601 ? 45.766 -34.211 23.018  1.00 16.28  ? 657 PHE B CG  1 
ATOM   4533 C CD1 . PHE A 1 601 ? 46.784 -34.784 22.279  1.00 48.48  ? 657 PHE B CD1 1 
ATOM   4534 C CD2 . PHE A 1 601 ? 44.804 -33.477 22.355  1.00 22.84  ? 657 PHE B CD2 1 
ATOM   4535 C CE1 . PHE A 1 601 ? 46.824 -34.652 20.913  1.00 16.76  ? 657 PHE B CE1 1 
ATOM   4536 C CE2 . PHE A 1 601 ? 44.844 -33.344 20.978  1.00 23.24  ? 657 PHE B CE2 1 
ATOM   4537 C CZ  . PHE A 1 601 ? 45.856 -33.929 20.263  1.00 15.83  ? 657 PHE B CZ  1 
ATOM   4538 N N   . SER A 1 602 ? 46.995 -35.908 26.953  1.00 18.27  ? 658 SER B N   1 
ATOM   4539 C CA  . SER A 1 602 ? 47.403 -35.905 28.356  1.00 35.59  ? 658 SER B CA  1 
ATOM   4540 C C   . SER A 1 602 ? 48.843 -35.408 28.505  1.00 34.29  ? 658 SER B C   1 
ATOM   4541 O O   . SER A 1 602 ? 49.621 -35.448 27.559  1.00 19.77  ? 658 SER B O   1 
ATOM   4542 C CB  . SER A 1 602 ? 47.240 -37.294 28.994  1.00 19.30  ? 658 SER B CB  1 
ATOM   4543 O OG  . SER A 1 602 ? 47.970 -38.287 28.314  1.00 51.41  ? 658 SER B OG  1 
ATOM   4544 N N   . GLY A 1 603 ? 49.200 -34.970 29.710  1.00 31.70  ? 659 GLY B N   1 
ATOM   4545 C CA  . GLY A 1 603 ? 50.503 -34.377 29.952  1.00 20.40  ? 659 GLY B CA  1 
ATOM   4546 C C   . GLY A 1 603 ? 50.421 -32.892 30.210  1.00 19.93  ? 659 GLY B C   1 
ATOM   4547 O O   . GLY A 1 603 ? 49.359 -32.303 30.085  1.00 19.07  ? 659 GLY B O   1 
ATOM   4548 N N   . ASP A 1 604 ? 51.544 -32.285 30.570  1.00 20.54  ? 660 ASP B N   1 
ATOM   4549 C CA  . ASP A 1 604 ? 51.541 -30.902 31.039  1.00 33.94  ? 660 ASP B CA  1 
ATOM   4550 C C   . ASP A 1 604 ? 51.831 -29.872 29.953  1.00 34.48  ? 660 ASP B C   1 
ATOM   4551 O O   . ASP A 1 604 ? 52.587 -30.133 29.020  1.00 42.45  ? 660 ASP B O   1 
ATOM   4552 C CB  . ASP A 1 604 ? 52.509 -30.714 32.216  1.00 21.09  ? 660 ASP B CB  1 
ATOM   4553 C CG  . ASP A 1 604 ? 53.930 -31.119 31.875  1.00 31.15  ? 660 ASP B CG  1 
ATOM   4554 O OD1 . ASP A 1 604 ? 54.113 -31.990 30.998  1.00 32.09  ? 660 ASP B OD1 1 
ATOM   4555 O OD2 . ASP A 1 604 ? 54.867 -30.563 32.485  1.00 31.99  ? 660 ASP B OD2 1 
ATOM   4556 N N   . LEU A 1 605 ? 51.229 -28.694 30.095  1.00 32.40  ? 661 LEU B N   1 
ATOM   4557 C CA  . LEU A 1 605 ? 51.527 -27.573 29.220  1.00 31.80  ? 661 LEU B CA  1 
ATOM   4558 C C   . LEU A 1 605 ? 52.227 -26.496 30.041  1.00 38.10  ? 661 LEU B C   1 
ATOM   4559 O O   . LEU A 1 605 ? 51.909 -26.302 31.210  1.00 40.85  ? 661 LEU B O   1 
ATOM   4560 C CB  . LEU A 1 605 ? 50.227 -26.996 28.669  1.00 26.08  ? 661 LEU B CB  1 
ATOM   4561 C CG  . LEU A 1 605 ? 49.325 -27.957 27.897  1.00 28.61  ? 661 LEU B CG  1 
ATOM   4562 C CD1 . LEU A 1 605 ? 47.919 -27.386 27.785  1.00 23.80  ? 661 LEU B CD1 1 
ATOM   4563 C CD2 . LEU A 1 605 ? 49.917 -28.267 26.521  1.00 17.57  ? 661 LEU B CD2 1 
ATOM   4564 N N   . PRO A 1 606 ? 53.179 -25.778 29.425  1.00 35.91  ? 662 PRO B N   1 
ATOM   4565 C CA  . PRO A 1 606 ? 53.886 -24.693 30.111  1.00 28.31  ? 662 PRO B CA  1 
ATOM   4566 C C   . PRO A 1 606 ? 52.940 -23.578 30.531  1.00 32.26  ? 662 PRO B C   1 
ATOM   4567 O O   . PRO A 1 606 ? 51.803 -23.527 30.073  1.00 34.11  ? 662 PRO B O   1 
ATOM   4568 C CB  . PRO A 1 606 ? 54.879 -24.193 29.057  1.00 31.54  ? 662 PRO B CB  1 
ATOM   4569 C CG  . PRO A 1 606 ? 54.327 -24.664 27.750  1.00 34.55  ? 662 PRO B CG  1 
ATOM   4570 C CD  . PRO A 1 606 ? 53.689 -25.984 28.059  1.00 35.35  ? 662 PRO B CD  1 
ATOM   4571 N N   . ASN A 1 607 ? 53.418 -22.708 31.416  1.00 35.39  ? 663 ASN B N   1 
ATOM   4572 C CA  . ASN A 1 607 ? 52.649 -21.601 31.983  1.00 25.78  ? 663 ASN B CA  1 
ATOM   4573 C C   . ASN A 1 607 ? 52.750 -20.340 31.118  1.00 33.49  ? 663 ASN B C   1 
ATOM   4574 O O   . ASN A 1 607 ? 52.491 -19.239 31.587  1.00 41.73  ? 663 ASN B O   1 
ATOM   4575 C CB  . ASN A 1 607 ? 53.060 -21.330 33.428  1.00 26.13  ? 663 ASN B CB  1 
ATOM   4576 C CG  . ASN A 1 607 ? 51.970 -20.633 34.247  1.00 26.31  ? 663 ASN B CG  1 
ATOM   4577 O OD1 . ASN A 1 607 ? 51.076 -19.980 33.710  1.00 18.53  ? 663 ASN B OD1 1 
ATOM   4578 N ND2 . ASN A 1 607 ? 52.069 -20.752 35.571  1.00 30.36  ? 663 ASN B ND2 1 
ATOM   4579 N N   . THR A 1 608 ? 53.219 -20.494 29.881  1.00 35.03  ? 664 THR B N   1 
ATOM   4580 C CA  . THR A 1 608 ? 53.292 -19.383 28.934  1.00 28.01  ? 664 THR B CA  1 
ATOM   4581 C C   . THR A 1 608 ? 51.925 -18.701 28.827  1.00 36.35  ? 664 THR B C   1 
ATOM   4582 O O   . THR A 1 608 ? 50.896 -19.302 29.159  1.00 30.50  ? 664 THR B O   1 
ATOM   4583 C CB  . THR A 1 608 ? 53.709 -19.865 27.531  1.00 36.95  ? 664 THR B CB  1 
ATOM   4584 O OG1 . THR A 1 608 ? 52.566 -20.403 26.853  1.00 45.34  ? 664 THR B OG1 1 
ATOM   4585 C CG2 . THR A 1 608 ? 54.815 -20.913 27.605  1.00 19.95  ? 664 THR B CG2 1 
ATOM   4586 N N   . PRO A 1 609 ? 51.908 -17.417 28.410  1.00 50.62  ? 665 PRO B N   1 
ATOM   4587 C CA  . PRO A 1 609 ? 50.634 -16.685 28.323  1.00 46.11  ? 665 PRO B CA  1 
ATOM   4588 C C   . PRO A 1 609 ? 49.729 -17.278 27.254  1.00 40.32  ? 665 PRO B C   1 
ATOM   4589 O O   . PRO A 1 609 ? 48.510 -17.068 27.269  1.00 37.13  ? 665 PRO B O   1 
ATOM   4590 C CB  . PRO A 1 609 ? 51.063 -15.269 27.924  1.00 41.16  ? 665 PRO B CB  1 
ATOM   4591 C CG  . PRO A 1 609 ? 52.510 -15.179 28.311  1.00 44.94  ? 665 PRO B CG  1 
ATOM   4592 C CD  . PRO A 1 609 ? 53.058 -16.554 28.087  1.00 49.53  ? 665 PRO B CD  1 
ATOM   4593 N N   . PHE A 1 610 ? 50.325 -18.012 26.324  1.00 33.15  ? 666 PHE B N   1 
ATOM   4594 C CA  . PHE A 1 610 ? 49.525 -18.742 25.363  1.00 37.11  ? 666 PHE B CA  1 
ATOM   4595 C C   . PHE A 1 610 ? 48.566 -19.718 26.050  1.00 44.38  ? 666 PHE B C   1 
ATOM   4596 O O   . PHE A 1 610 ? 47.351 -19.559 25.970  1.00 41.31  ? 666 PHE B O   1 
ATOM   4597 C CB  . PHE A 1 610 ? 50.407 -19.493 24.377  1.00 36.25  ? 666 PHE B CB  1 
ATOM   4598 C CG  . PHE A 1 610 ? 49.683 -19.921 23.135  1.00 43.60  ? 666 PHE B CG  1 
ATOM   4599 C CD1 . PHE A 1 610 ? 48.313 -19.767 23.022  1.00 47.50  ? 666 PHE B CD1 1 
ATOM   4600 C CD2 . PHE A 1 610 ? 50.374 -20.460 22.070  1.00 58.01  ? 666 PHE B CD2 1 
ATOM   4601 C CE1 . PHE A 1 610 ? 47.642 -20.157 21.887  1.00 56.86  ? 666 PHE B CE1 1 
ATOM   4602 C CE2 . PHE A 1 610 ? 49.707 -20.853 20.918  1.00 64.52  ? 666 PHE B CE2 1 
ATOM   4603 C CZ  . PHE A 1 610 ? 48.338 -20.702 20.829  1.00 62.44  ? 666 PHE B CZ  1 
ATOM   4604 N N   . PHE A 1 611 ? 49.115 -20.734 26.708  1.00 47.22  ? 667 PHE B N   1 
ATOM   4605 C CA  . PHE A 1 611 ? 48.302 -21.858 27.157  1.00 39.40  ? 667 PHE B CA  1 
ATOM   4606 C C   . PHE A 1 611 ? 47.345 -21.522 28.293  1.00 42.34  ? 667 PHE B C   1 
ATOM   4607 O O   . PHE A 1 611 ? 46.341 -22.210 28.492  1.00 39.89  ? 667 PHE B O   1 
ATOM   4608 C CB  . PHE A 1 611 ? 49.189 -23.053 27.494  1.00 31.18  ? 667 PHE B CB  1 
ATOM   4609 C CG  . PHE A 1 611 ? 50.012 -23.524 26.333  1.00 25.28  ? 667 PHE B CG  1 
ATOM   4610 C CD1 . PHE A 1 611 ? 49.510 -24.459 25.438  1.00 24.66  ? 667 PHE B CD1 1 
ATOM   4611 C CD2 . PHE A 1 611 ? 51.277 -23.014 26.119  1.00 23.19  ? 667 PHE B CD2 1 
ATOM   4612 C CE1 . PHE A 1 611 ? 50.267 -24.889 24.363  1.00 16.61  ? 667 PHE B CE1 1 
ATOM   4613 C CE2 . PHE A 1 611 ? 52.035 -23.438 25.043  1.00 32.63  ? 667 PHE B CE2 1 
ATOM   4614 C CZ  . PHE A 1 611 ? 51.527 -24.380 24.165  1.00 17.36  ? 667 PHE B CZ  1 
ATOM   4615 N N   . ARG A 1 612 ? 47.638 -20.451 29.026  1.00 51.32  ? 668 ARG B N   1 
ATOM   4616 C CA  . ARG A 1 612 ? 46.740 -20.003 30.091  1.00 56.14  ? 668 ARG B CA  1 
ATOM   4617 C C   . ARG A 1 612 ? 45.531 -19.310 29.467  1.00 48.51  ? 668 ARG B C   1 
ATOM   4618 O O   . ARG A 1 612 ? 44.553 -18.998 30.151  1.00 37.49  ? 668 ARG B O   1 
ATOM   4619 C CB  . ARG A 1 612 ? 47.461 -19.065 31.069  1.00 66.55  ? 668 ARG B CB  1 
ATOM   4620 C CG  . ARG A 1 612 ? 47.866 -17.726 30.459  1.00 77.65  ? 668 ARG B CG  1 
ATOM   4621 C CD  . ARG A 1 612 ? 48.415 -16.740 31.492  1.00 82.19  ? 668 ARG B CD  1 
ATOM   4622 N NE  . ARG A 1 612 ? 49.834 -16.949 31.772  1.00 82.83  ? 668 ARG B NE  1 
ATOM   4623 C CZ  . ARG A 1 612 ? 50.650 -16.011 32.246  1.00 79.30  ? 668 ARG B CZ  1 
ATOM   4624 N NH1 . ARG A 1 612 ? 50.191 -14.789 32.487  1.00 78.06  ? 668 ARG B NH1 1 
ATOM   4625 N NH2 . ARG A 1 612 ? 51.927 -16.291 32.472  1.00 75.01  ? 668 ARG B NH2 1 
ATOM   4626 N N   . ARG A 1 613 ? 45.636 -19.037 28.169  1.00 54.09  ? 669 ARG B N   1 
ATOM   4627 C CA  . ARG A 1 613 ? 44.532 -18.497 27.386  1.00 55.93  ? 669 ARG B CA  1 
ATOM   4628 C C   . ARG A 1 613 ? 43.570 -19.591 26.894  1.00 49.72  ? 669 ARG B C   1 
ATOM   4629 O O   . ARG A 1 613 ? 42.370 -19.344 26.762  1.00 55.29  ? 669 ARG B O   1 
ATOM   4630 C CB  . ARG A 1 613 ? 45.072 -17.656 26.226  1.00 65.08  ? 669 ARG B CB  1 
ATOM   4631 C CG  . ARG A 1 613 ? 44.030 -16.992 25.357  1.00 73.19  ? 669 ARG B CG  1 
ATOM   4632 C CD  . ARG A 1 613 ? 44.706 -16.178 24.255  1.00 78.53  ? 669 ARG B CD  1 
ATOM   4633 N NE  . ARG A 1 613 ? 45.619 -15.176 24.806  1.00 78.60  ? 669 ARG B NE  1 
ATOM   4634 C CZ  . ARG A 1 613 ? 46.862 -14.977 24.378  1.00 75.00  ? 669 ARG B CZ  1 
ATOM   4635 N NH1 . ARG A 1 613 ? 47.621 -14.047 24.944  1.00 77.15  ? 669 ARG B NH1 1 
ATOM   4636 N NH2 . ARG A 1 613 ? 47.348 -15.705 23.382  1.00 68.37  ? 669 ARG B NH2 1 
ATOM   4637 N N   . LEU A 1 614 ? 44.095 -20.784 26.606  1.00 40.65  ? 670 LEU B N   1 
ATOM   4638 C CA  . LEU A 1 614 ? 43.245 -21.924 26.258  1.00 34.03  ? 670 LEU B CA  1 
ATOM   4639 C C   . LEU A 1 614 ? 42.199 -22.083 27.353  1.00 36.59  ? 670 LEU B C   1 
ATOM   4640 O O   . LEU A 1 614 ? 42.538 -22.074 28.537  1.00 35.76  ? 670 LEU B O   1 
ATOM   4641 C CB  . LEU A 1 614 ? 44.055 -23.224 26.145  1.00 30.21  ? 670 LEU B CB  1 
ATOM   4642 C CG  . LEU A 1 614 ? 45.207 -23.325 25.144  1.00 34.55  ? 670 LEU B CG  1 
ATOM   4643 C CD1 . LEU A 1 614 ? 45.746 -24.761 25.036  1.00 13.73  ? 670 LEU B CD1 1 
ATOM   4644 C CD2 . LEU A 1 614 ? 44.780 -22.796 23.779  1.00 33.30  ? 670 LEU B CD2 1 
ATOM   4645 N N   . PRO A 1 615 ? 40.921 -22.224 26.965  1.00 37.73  ? 671 PRO B N   1 
ATOM   4646 C CA  . PRO A 1 615 ? 39.839 -22.357 27.953  1.00 33.35  ? 671 PRO B CA  1 
ATOM   4647 C C   . PRO A 1 615 ? 40.078 -23.555 28.861  1.00 39.48  ? 671 PRO B C   1 
ATOM   4648 O O   . PRO A 1 615 ? 40.810 -24.466 28.483  1.00 48.33  ? 671 PRO B O   1 
ATOM   4649 C CB  . PRO A 1 615 ? 38.598 -22.602 27.087  1.00 30.00  ? 671 PRO B CB  1 
ATOM   4650 C CG  . PRO A 1 615 ? 38.957 -22.061 25.722  1.00 33.45  ? 671 PRO B CG  1 
ATOM   4651 C CD  . PRO A 1 615 ? 40.431 -22.299 25.575  1.00 34.16  ? 671 PRO B CD  1 
ATOM   4652 N N   . LEU A 1 616 ? 39.494 -23.551 30.052  1.00 38.37  ? 672 LEU B N   1 
ATOM   4653 C CA  . LEU A 1 616 ? 39.680 -24.667 30.966  1.00 35.01  ? 672 LEU B CA  1 
ATOM   4654 C C   . LEU A 1 616 ? 38.779 -25.840 30.590  1.00 34.31  ? 672 LEU B C   1 
ATOM   4655 O O   . LEU A 1 616 ? 39.147 -26.992 30.785  1.00 41.42  ? 672 LEU B O   1 
ATOM   4656 C CB  . LEU A 1 616 ? 39.447 -24.236 32.411  1.00 42.29  ? 672 LEU B CB  1 
ATOM   4657 C CG  . LEU A 1 616 ? 40.237 -24.986 33.491  1.00 44.83  ? 672 LEU B CG  1 
ATOM   4658 C CD1 . LEU A 1 616 ? 41.735 -24.899 33.240  1.00 43.24  ? 672 LEU B CD1 1 
ATOM   4659 C CD2 . LEU A 1 616 ? 39.901 -24.424 34.863  1.00 49.46  ? 672 LEU B CD2 1 
ATOM   4660 N N   . SER A 1 617 ? 37.601 -25.549 30.047  1.00 32.25  ? 673 SER B N   1 
ATOM   4661 C CA  . SER A 1 617 ? 36.732 -26.605 29.537  1.00 35.29  ? 673 SER B CA  1 
ATOM   4662 C C   . SER A 1 617 ? 37.390 -27.280 28.339  1.00 33.56  ? 673 SER B C   1 
ATOM   4663 O O   . SER A 1 617 ? 37.175 -28.466 28.085  1.00 38.64  ? 673 SER B O   1 
ATOM   4664 C CB  . SER A 1 617 ? 35.362 -26.055 29.147  1.00 41.41  ? 673 SER B CB  1 
ATOM   4665 O OG  . SER A 1 617 ? 35.488 -24.978 28.236  1.00 48.13  ? 673 SER B OG  1 
ATOM   4666 N N   . ASP A 1 618 ? 38.197 -26.519 27.607  1.00 27.97  ? 674 ASP B N   1 
ATOM   4667 C CA  . ASP A 1 618 ? 38.985 -27.081 26.517  1.00 28.57  ? 674 ASP B CA  1 
ATOM   4668 C C   . ASP A 1 618 ? 39.893 -28.194 27.028  1.00 29.80  ? 674 ASP B C   1 
ATOM   4669 O O   . ASP A 1 618 ? 39.889 -29.301 26.490  1.00 33.07  ? 674 ASP B O   1 
ATOM   4670 C CB  . ASP A 1 618 ? 39.812 -25.995 25.821  1.00 26.32  ? 674 ASP B CB  1 
ATOM   4671 C CG  . ASP A 1 618 ? 39.198 -25.546 24.508  1.00 33.29  ? 674 ASP B CG  1 
ATOM   4672 O OD1 . ASP A 1 618 ? 37.970 -25.715 24.335  1.00 35.18  ? 674 ASP B OD1 1 
ATOM   4673 O OD2 . ASP A 1 618 ? 39.944 -25.035 23.645  1.00 38.96  ? 674 ASP B OD2 1 
ATOM   4674 N N   . LEU A 1 619 ? 40.659 -27.905 28.076  1.00 25.05  ? 675 LEU B N   1 
ATOM   4675 C CA  . LEU A 1 619 ? 41.550 -28.897 28.657  1.00 13.29  ? 675 LEU B CA  1 
ATOM   4676 C C   . LEU A 1 619 ? 40.742 -30.019 29.302  1.00 15.85  ? 675 LEU B C   1 
ATOM   4677 O O   . LEU A 1 619 ? 41.185 -31.169 29.356  1.00 14.00  ? 675 LEU B O   1 
ATOM   4678 C CB  . LEU A 1 619 ? 42.477 -28.242 29.674  1.00 20.76  ? 675 LEU B CB  1 
ATOM   4679 C CG  . LEU A 1 619 ? 43.415 -27.133 29.186  1.00 16.82  ? 675 LEU B CG  1 
ATOM   4680 C CD1 . LEU A 1 619 ? 44.313 -26.649 30.321  1.00 18.84  ? 675 LEU B CD1 1 
ATOM   4681 C CD2 . LEU A 1 619 ? 44.257 -27.616 28.026  1.00 16.26  ? 675 LEU B CD2 1 
ATOM   4682 N N   . ALA A 1 620 ? 39.540 -29.674 29.751  1.00 16.97  ? 676 ALA B N   1 
ATOM   4683 C CA  . ALA A 1 620 ? 38.663 -30.584 30.487  1.00 18.20  ? 676 ALA B CA  1 
ATOM   4684 C C   . ALA A 1 620 ? 38.042 -31.687 29.636  1.00 22.41  ? 676 ALA B C   1 
ATOM   4685 O O   . ALA A 1 620 ? 37.607 -32.716 30.166  1.00 28.76  ? 676 ALA B O   1 
ATOM   4686 C CB  . ALA A 1 620 ? 37.564 -29.792 31.179  1.00 12.33  ? 676 ALA B CB  1 
ATOM   4687 N N   . SER A 1 621 ? 37.985 -31.470 28.324  1.00 19.37  ? 677 SER B N   1 
ATOM   4688 C CA  . SER A 1 621 ? 37.356 -32.428 27.413  1.00 12.19  ? 677 SER B CA  1 
ATOM   4689 C C   . SER A 1 621 ? 38.318 -33.532 27.002  1.00 20.88  ? 677 SER B C   1 
ATOM   4690 O O   . SER A 1 621 ? 37.924 -34.514 26.377  1.00 25.93  ? 677 SER B O   1 
ATOM   4691 C CB  . SER A 1 621 ? 36.784 -31.716 26.184  1.00 11.40  ? 677 SER B CB  1 
ATOM   4692 O OG  . SER A 1 621 ? 37.714 -30.807 25.624  1.00 12.51  ? 677 SER B OG  1 
ATOM   4693 N N   . ASN A 1 622 ? 39.581 -33.364 27.376  1.00 13.54  ? 678 ASN B N   1 
ATOM   4694 C CA  . ASN A 1 622 ? 40.637 -34.340 27.108  1.00 14.35  ? 678 ASN B CA  1 
ATOM   4695 C C   . ASN A 1 622 ? 40.791 -35.448 28.165  1.00 15.08  ? 678 ASN B C   1 
ATOM   4696 O O   . ASN A 1 622 ? 39.902 -35.663 28.982  1.00 24.25  ? 678 ASN B O   1 
ATOM   4697 C CB  . ASN A 1 622 ? 41.969 -33.627 26.882  1.00 23.08  ? 678 ASN B CB  1 
ATOM   4698 C CG  . ASN A 1 622 ? 41.999 -32.850 25.587  1.00 22.31  ? 678 ASN B CG  1 
ATOM   4699 O OD1 . ASN A 1 622 ? 42.190 -33.424 24.524  1.00 21.20  ? 678 ASN B OD1 1 
ATOM   4700 N ND2 . ASN A 1 622 ? 41.814 -31.540 25.669  1.00 13.63  ? 678 ASN B ND2 1 
ATOM   4701 N N   . ARG A 1 623 ? 41.902 -36.181 28.103  1.00 15.88  ? 679 ARG B N   1 
ATOM   4702 C CA  . ARG A 1 623 ? 42.211 -37.214 29.088  1.00 18.22  ? 679 ARG B CA  1 
ATOM   4703 C C   . ARG A 1 623 ? 42.974 -36.656 30.297  1.00 26.03  ? 679 ARG B C   1 
ATOM   4704 O O   . ARG A 1 623 ? 42.493 -36.713 31.424  1.00 31.82  ? 679 ARG B O   1 
ATOM   4705 C CB  . ARG A 1 623 ? 43.018 -38.351 28.447  1.00 17.37  ? 679 ARG B CB  1 
ATOM   4706 C CG  . ARG A 1 623 ? 43.304 -39.531 29.374  1.00 21.31  ? 679 ARG B CG  1 
ATOM   4707 C CD  . ARG A 1 623 ? 44.079 -40.654 28.682  1.00 27.38  ? 679 ARG B CD  1 
ATOM   4708 N NE  . ARG A 1 623 ? 45.518 -40.609 28.951  1.00 42.90  ? 679 ARG B NE  1 
ATOM   4709 C CZ  . ARG A 1 623 ? 46.224 -41.610 29.478  1.00 51.95  ? 679 ARG B CZ  1 
ATOM   4710 N NH1 . ARG A 1 623 ? 45.637 -42.751 29.804  1.00 49.81  ? 679 ARG B NH1 1 
ATOM   4711 N NH2 . ARG A 1 623 ? 47.528 -41.474 29.675  1.00 59.84  ? 679 ARG B NH2 1 
ATOM   4712 N N   . GLY A 1 624 ? 44.207 -36.228 30.048  1.00 26.10  ? 680 GLY B N   1 
ATOM   4713 C CA  . GLY A 1 624 ? 45.125 -35.690 31.042  1.00 17.98  ? 680 GLY B CA  1 
ATOM   4714 C C   . GLY A 1 624 ? 45.636 -34.259 31.001  1.00 17.74  ? 680 GLY B C   1 
ATOM   4715 O O   . GLY A 1 624 ? 46.763 -34.043 31.401  1.00 23.75  ? 680 GLY B O   1 
ATOM   4716 N N   . LEU A 1 625 ? 44.947 -33.304 30.407  1.00 33.21  ? 681 LEU B N   1 
ATOM   4717 C CA  . LEU A 1 625 ? 45.604 -32.008 30.210  1.00 16.80  ? 681 LEU B CA  1 
ATOM   4718 C C   . LEU A 1 625 ? 45.539 -31.071 31.402  1.00 24.70  ? 681 LEU B C   1 
ATOM   4719 O O   . LEU A 1 625 ? 44.471 -30.894 32.012  1.00 19.38  ? 681 LEU B O   1 
ATOM   4720 C CB  . LEU A 1 625 ? 45.079 -31.306 28.956  1.00 17.63  ? 681 LEU B CB  1 
ATOM   4721 C CG  . LEU A 1 625 ? 45.692 -31.853 27.669  1.00 16.25  ? 681 LEU B CG  1 
ATOM   4722 C CD1 . LEU A 1 625 ? 45.087 -31.181 26.471  1.00 15.45  ? 681 LEU B CD1 1 
ATOM   4723 C CD2 . LEU A 1 625 ? 47.196 -31.644 27.701  1.00 33.69  ? 681 LEU B CD2 1 
ATOM   4724 N N   . TYR A 1 626 ? 46.696 -30.500 31.750  1.00 17.31  ? 682 TYR B N   1 
ATOM   4725 C CA  . TYR A 1 626 ? 46.793 -29.506 32.825  1.00 25.31  ? 682 TYR B CA  1 
ATOM   4726 C C   . TYR A 1 626 ? 48.003 -28.588 32.663  1.00 17.78  ? 682 TYR B C   1 
ATOM   4727 O O   . TYR A 1 626 ? 49.056 -29.034 32.224  1.00 18.43  ? 682 TYR B O   1 
ATOM   4728 C CB  . TYR A 1 626 ? 46.857 -30.210 34.185  1.00 17.93  ? 682 TYR B CB  1 
ATOM   4729 C CG  . TYR A 1 626 ? 48.167 -30.913 34.443  1.00 18.95  ? 682 TYR B CG  1 
ATOM   4730 C CD1 . TYR A 1 626 ? 48.433 -32.149 33.880  1.00 19.33  ? 682 TYR B CD1 1 
ATOM   4731 C CD2 . TYR A 1 626 ? 49.143 -30.334 35.232  1.00 19.58  ? 682 TYR B CD2 1 
ATOM   4732 C CE1 . TYR A 1 626 ? 49.622 -32.795 34.105  1.00 20.28  ? 682 TYR B CE1 1 
ATOM   4733 C CE2 . TYR A 1 626 ? 50.337 -30.968 35.452  1.00 20.53  ? 682 TYR B CE2 1 
ATOM   4734 C CZ  . TYR A 1 626 ? 50.572 -32.201 34.889  1.00 20.87  ? 682 TYR B CZ  1 
ATOM   4735 O OH  . TYR A 1 626 ? 51.768 -32.839 35.118  1.00 21.86  ? 682 TYR B OH  1 
ATOM   4736 N N   . ILE A 1 627 ? 47.871 -27.327 33.068  1.00 17.49  ? 683 ILE B N   1 
ATOM   4737 C CA  . ILE A 1 627 ? 49.014 -26.409 33.063  1.00 35.89  ? 683 ILE B CA  1 
ATOM   4738 C C   . ILE A 1 627 ? 49.967 -26.666 34.226  1.00 18.95  ? 683 ILE B C   1 
ATOM   4739 O O   . ILE A 1 627 ? 49.537 -26.860 35.353  1.00 45.89  ? 683 ILE B O   1 
ATOM   4740 C CB  . ILE A 1 627 ? 48.588 -24.925 33.118  1.00 31.65  ? 683 ILE B CB  1 
ATOM   4741 C CG1 . ILE A 1 627 ? 47.586 -24.599 32.012  1.00 31.16  ? 683 ILE B CG1 1 
ATOM   4742 C CG2 . ILE A 1 627 ? 49.815 -24.003 33.034  1.00 27.95  ? 683 ILE B CG2 1 
ATOM   4743 C CD1 . ILE A 1 627 ? 46.178 -24.427 32.524  1.00 37.74  ? 683 ILE B CD1 1 
ATOM   4744 N N   . SER A 1 628 ? 51.262 -26.661 33.941  1.00 28.60  ? 684 SER B N   1 
ATOM   4745 C CA  . SER A 1 628 ? 52.272 -26.936 34.945  1.00 31.18  ? 684 SER B CA  1 
ATOM   4746 C C   . SER A 1 628 ? 53.018 -25.682 35.391  1.00 34.04  ? 684 SER B C   1 
ATOM   4747 O O   . SER A 1 628 ? 52.810 -24.590 34.860  1.00 36.52  ? 684 SER B O   1 
ATOM   4748 C CB  . SER A 1 628 ? 53.300 -27.902 34.379  1.00 31.62  ? 684 SER B CB  1 
ATOM   4749 O OG  . SER A 1 628 ? 54.330 -27.171 33.737  1.00 33.40  ? 684 SER B OG  1 
ATOM   4750 N N   . ASN A 1 629 ? 53.916 -25.870 36.355  1.00 32.37  ? 685 ASN B N   1 
ATOM   4751 C CA  . ASN A 1 629 ? 54.771 -24.809 36.859  1.00 22.61  ? 685 ASN B CA  1 
ATOM   4752 C C   . ASN A 1 629 ? 56.206 -25.304 36.836  1.00 30.58  ? 685 ASN B C   1 
ATOM   4753 O O   . ASN A 1 629 ? 56.522 -26.333 37.436  1.00 33.71  ? 685 ASN B O   1 
ATOM   4754 C CB  . ASN A 1 629 ? 54.396 -24.441 38.294  1.00 22.69  ? 685 ASN B CB  1 
ATOM   4755 C CG  . ASN A 1 629 ? 53.112 -23.646 38.385  1.00 23.82  ? 685 ASN B CG  1 
ATOM   4756 O OD1 . ASN A 1 629 ? 53.099 -22.432 38.178  1.00 21.50  ? 685 ASN B OD1 1 
ATOM   4757 N ND2 . ASN A 1 629 ? 52.022 -24.324 38.719  1.00 27.43  ? 685 ASN B ND2 1 
ATOM   4758 N N   . ALA A 1 630 ? 57.076 -24.576 36.146  1.00 28.97  ? 686 ALA B N   1 
ATOM   4759 C CA  . ALA A 1 630 ? 58.459 -25.007 36.004  1.00 25.19  ? 686 ALA B CA  1 
ATOM   4760 C C   . ALA A 1 630 ? 59.180 -24.965 37.345  1.00 34.29  ? 686 ALA B C   1 
ATOM   4761 O O   . ALA A 1 630 ? 58.924 -24.095 38.180  1.00 35.20  ? 686 ALA B O   1 
ATOM   4762 C CB  . ALA A 1 630 ? 59.186 -24.165 34.971  1.00 25.41  ? 686 ALA B CB  1 
ATOM   4763 N N   . ILE A 1 631 ? 60.077 -25.926 37.542  1.00 26.97  ? 687 ILE B N   1 
ATOM   4764 C CA  . ILE A 1 631 ? 60.881 -25.999 38.746  1.00 31.58  ? 687 ILE B CA  1 
ATOM   4765 C C   . ILE A 1 631 ? 61.895 -24.860 38.753  1.00 28.65  ? 687 ILE B C   1 
ATOM   4766 O O   . ILE A 1 631 ? 62.673 -24.707 37.823  1.00 29.05  ? 687 ILE B O   1 
ATOM   4767 C CB  . ILE A 1 631 ? 61.560 -27.374 38.858  1.00 28.67  ? 687 ILE B CB  1 
ATOM   4768 C CG1 . ILE A 1 631 ? 60.485 -28.462 38.888  1.00 27.98  ? 687 ILE B CG1 1 
ATOM   4769 C CG2 . ILE A 1 631 ? 62.452 -27.438 40.082  1.00 29.72  ? 687 ILE B CG2 1 
ATOM   4770 C CD1 . ILE A 1 631 ? 61.005 -29.843 39.138  1.00 75.50  ? 687 ILE B CD1 1 
ATOM   4771 N N   . SER A 1 632 ? 61.867 -24.055 39.809  1.00 31.08  ? 688 SER B N   1 
ATOM   4772 C CA  . SER A 1 632 ? 62.695 -22.862 39.889  1.00 36.47  ? 688 SER B CA  1 
ATOM   4773 C C   . SER A 1 632 ? 64.159 -23.234 40.084  1.00 43.45  ? 688 SER B C   1 
ATOM   4774 O O   . SER A 1 632 ? 64.495 -24.011 40.976  1.00 47.45  ? 688 SER B O   1 
ATOM   4775 C CB  . SER A 1 632 ? 62.217 -21.965 41.038  1.00 36.83  ? 688 SER B CB  1 
ATOM   4776 O OG  . SER A 1 632 ? 63.307 -21.373 41.732  1.00 37.03  ? 688 SER B OG  1 
ATOM   4777 N N   . ASP B 2 1   ? 50.359 15.314  -13.336 1.00 60.20  ? 44  ASP A N   1 
ATOM   4778 C CA  . ASP B 2 1   ? 49.373 16.378  -13.476 1.00 65.18  ? 44  ASP A CA  1 
ATOM   4779 C C   . ASP B 2 1   ? 48.227 16.171  -12.494 1.00 61.75  ? 44  ASP A C   1 
ATOM   4780 O O   . ASP B 2 1   ? 48.213 15.193  -11.747 1.00 67.97  ? 44  ASP A O   1 
ATOM   4781 C CB  . ASP B 2 1   ? 48.812 16.395  -14.900 1.00 69.83  ? 44  ASP A CB  1 
ATOM   4782 C CG  . ASP B 2 1   ? 49.856 16.755  -15.941 1.00 76.92  ? 44  ASP A CG  1 
ATOM   4783 O OD1 . ASP B 2 1   ? 51.063 16.665  -15.633 1.00 79.59  ? 44  ASP A OD1 1 
ATOM   4784 O OD2 . ASP B 2 1   ? 49.465 17.121  -17.073 1.00 79.20  ? 44  ASP A OD2 1 
HETATM 4785 N N   . PTR B 2 2   ? 47.269 17.094  -12.480 1.00 48.11  ? 45  PTR A N   1 
HETATM 4786 C CA  . PTR B 2 2   ? 45.976 16.767  -11.901 1.00 36.06  ? 45  PTR A CA  1 
HETATM 4787 C C   . PTR B 2 2   ? 45.288 15.942  -12.987 1.00 32.06  ? 45  PTR A C   1 
HETATM 4788 O O   . PTR B 2 2   ? 45.482 16.205  -14.180 1.00 25.18  ? 45  PTR A O   1 
HETATM 4789 C CB  . PTR B 2 2   ? 45.153 17.949  -11.358 1.00 33.05  ? 45  PTR A CB  1 
HETATM 4790 C CG  . PTR B 2 2   ? 44.537 18.877  -12.383 1.00 27.31  ? 45  PTR A CG  1 
HETATM 4791 C CD1 . PTR B 2 2   ? 43.197 18.770  -12.738 1.00 10.73  ? 45  PTR A CD1 1 
HETATM 4792 C CD2 . PTR B 2 2   ? 45.284 19.882  -12.962 1.00 12.99  ? 45  PTR A CD2 1 
HETATM 4793 C CE1 . PTR B 2 2   ? 42.626 19.639  -13.651 1.00 10.49  ? 45  PTR A CE1 1 
HETATM 4794 C CE2 . PTR B 2 2   ? 44.729 20.750  -13.872 1.00 16.94  ? 45  PTR A CE2 1 
HETATM 4795 C CZ  . PTR B 2 2   ? 43.399 20.634  -14.210 1.00 14.09  ? 45  PTR A CZ  1 
HETATM 4796 O OH  . PTR B 2 2   ? 42.911 21.449  -15.099 1.00 11.73  ? 45  PTR A OH  1 
HETATM 4797 P P   . PTR B 2 2   ? 42.068 22.767  -14.757 1.00 11.21  ? 45  PTR A P   1 
HETATM 4798 O O1P . PTR B 2 2   ? 41.295 23.163  -16.025 1.00 10.60  ? 45  PTR A O1P 1 
HETATM 4799 O O2P . PTR B 2 2   ? 41.043 22.485  -13.649 1.00 20.69  ? 45  PTR A O2P 1 
HETATM 4800 O O3P . PTR B 2 2   ? 42.999 23.851  -14.357 1.00 26.35  ? 45  PTR A O3P 1 
ATOM   4801 N N   . PRO B 2 3   ? 44.528 14.915  -12.578 1.00 33.93  ? 46  PRO A N   1 
ATOM   4802 C CA  . PRO B 2 3   ? 43.944 13.959  -13.532 1.00 9.58   ? 46  PRO A CA  1 
ATOM   4803 C C   . PRO B 2 3   ? 42.813 14.524  -14.382 1.00 29.33  ? 46  PRO A C   1 
ATOM   4804 O O   . PRO B 2 3   ? 42.025 15.358  -13.937 1.00 32.86  ? 46  PRO A O   1 
ATOM   4805 C CB  . PRO B 2 3   ? 43.434 12.827  -12.637 1.00 8.85   ? 46  PRO A CB  1 
ATOM   4806 C CG  . PRO B 2 3   ? 43.297 13.429  -11.282 1.00 9.02   ? 46  PRO A CG  1 
ATOM   4807 C CD  . PRO B 2 3   ? 44.307 14.527  -11.174 1.00 10.27  ? 46  PRO A CD  1 
ATOM   4808 N N   . LYS B 2 4   ? 42.756 14.054  -15.620 1.00 8.45   ? 47  LYS A N   1 
ATOM   4809 C CA  . LYS B 2 4   ? 41.717 14.425  -16.559 1.00 7.62   ? 47  LYS A CA  1 
ATOM   4810 C C   . LYS B 2 4   ? 40.362 14.018  -15.986 1.00 15.59  ? 47  LYS A C   1 
ATOM   4811 O O   . LYS B 2 4   ? 40.298 13.109  -15.160 1.00 14.34  ? 47  LYS A O   1 
ATOM   4812 C CB  . LYS B 2 4   ? 41.985 13.732  -17.906 1.00 14.36  ? 47  LYS A CB  1 
ATOM   4813 C CG  . LYS B 2 4   ? 43.013 14.435  -18.772 1.00 15.94  ? 47  LYS A CG  1 
ATOM   4814 C CD  . LYS B 2 4   ? 44.327 13.695  -18.837 1.00 27.27  ? 47  LYS A CD  1 
ATOM   4815 C CE  . LYS B 2 4   ? 44.246 12.495  -19.772 1.00 29.64  ? 47  LYS A CE  1 
ATOM   4816 N NZ  . LYS B 2 4   ? 45.597 11.891  -20.013 1.00 32.01  ? 47  LYS A NZ  1 
ATOM   4817 N N   . PRO B 2 5   ? 39.275 14.687  -16.418 1.00 13.00  ? 48  PRO A N   1 
ATOM   4818 C CA  . PRO B 2 5   ? 37.920 14.425  -15.897 1.00 7.48   ? 48  PRO A CA  1 
ATOM   4819 C C   . PRO B 2 5   ? 37.537 12.964  -16.040 1.00 12.37  ? 48  PRO A C   1 
ATOM   4820 O O   . PRO B 2 5   ? 37.902 12.355  -17.045 1.00 7.52   ? 48  PRO A O   1 
ATOM   4821 C CB  . PRO B 2 5   ? 37.019 15.257  -16.811 1.00 10.60  ? 48  PRO A CB  1 
ATOM   4822 C CG  . PRO B 2 5   ? 37.923 16.314  -17.410 1.00 13.90  ? 48  PRO A CG  1 
ATOM   4823 C CD  . PRO B 2 5   ? 39.280 15.701  -17.490 1.00 13.62  ? 48  PRO A CD  1 
ATOM   4824 N N   . SER B 2 6   ? 36.825 12.402  -15.065 1.00 14.60  ? 49  SER A N   1 
ATOM   4825 C CA  . SER B 2 6   ? 36.420 11.005  -15.176 1.00 10.99  ? 49  SER A CA  1 
ATOM   4826 C C   . SER B 2 6   ? 35.085 10.704  -14.527 1.00 10.55  ? 49  SER A C   1 
ATOM   4827 O O   . SER B 2 6   ? 34.612 11.440  -13.667 1.00 34.20  ? 49  SER A O   1 
ATOM   4828 C CB  . SER B 2 6   ? 37.500 10.070  -14.621 1.00 12.33  ? 49  SER A CB  1 
ATOM   4829 O OG  . SER B 2 6   ? 37.446 9.991   -13.206 1.00 18.10  ? 49  SER A OG  1 
ATOM   4830 N N   . THR B 2 7   ? 34.481 9.612   -14.975 1.00 6.62   ? 50  THR A N   1 
ATOM   4831 C CA  . THR B 2 7   ? 33.276 9.069   -14.366 1.00 11.16  ? 50  THR A CA  1 
ATOM   4832 C C   . THR B 2 7   ? 33.658 8.332   -13.074 1.00 8.34   ? 50  THR A C   1 
ATOM   4833 O O   . THR B 2 7   ? 34.813 7.951   -12.893 1.00 3.11   ? 50  THR A O   1 
ATOM   4834 C CB  . THR B 2 7   ? 32.532 8.098   -15.335 1.00 2.49   ? 50  THR A CB  1 
ATOM   4835 O OG1 . THR B 2 7   ? 33.438 7.104   -15.818 1.00 5.37   ? 50  THR A OG1 1 
ATOM   4836 C CG2 . THR B 2 7   ? 31.999 8.837   -16.519 1.00 2.33   ? 50  THR A CG2 1 
ATOM   4837 N N   . ARG B 2 8   ? 32.704 8.172   -12.162 1.00 2.45   ? 51  ARG A N   1 
ATOM   4838 C CA  . ARG B 2 8   ? 32.924 7.299   -11.025 1.00 19.59  ? 51  ARG A CA  1 
ATOM   4839 C C   . ARG B 2 8   ? 33.316 5.916   -11.531 1.00 5.80   ? 51  ARG A C   1 
ATOM   4840 O O   . ARG B 2 8   ? 32.661 5.372   -12.405 1.00 11.66  ? 51  ARG A O   1 
ATOM   4841 C CB  . ARG B 2 8   ? 31.675 7.175   -10.157 1.00 19.75  ? 51  ARG A CB  1 
ATOM   4842 C CG  . ARG B 2 8   ? 31.820 6.043   -9.159  1.00 2.34   ? 51  ARG A CG  1 
ATOM   4843 C CD  . ARG B 2 8   ? 30.536 5.616   -8.576  1.00 3.38   ? 51  ARG A CD  1 
ATOM   4844 N NE  . ARG B 2 8   ? 30.307 4.187   -8.734  1.00 2.09   ? 51  ARG A NE  1 
ATOM   4845 C CZ  . ARG B 2 8   ? 30.228 3.331   -7.724  1.00 15.96  ? 51  ARG A CZ  1 
ATOM   4846 N NH1 . ARG B 2 8   ? 30.392 3.757   -6.474  1.00 17.03  ? 51  ARG A NH1 1 
ATOM   4847 N NH2 . ARG B 2 8   ? 29.991 2.047   -7.959  1.00 19.30  ? 51  ARG A NH2 1 
ATOM   4848 N N   . PRO B 2 9   ? 34.401 5.359   -10.987 1.00 3.11   ? 52  PRO A N   1 
ATOM   4849 C CA  . PRO B 2 9   ? 34.864 4.040   -11.404 1.00 3.35   ? 52  PRO A CA  1 
ATOM   4850 C C   . PRO B 2 9   ? 33.783 3.008   -11.164 1.00 27.68  ? 52  PRO A C   1 
ATOM   4851 O O   . PRO B 2 9   ? 33.174 3.043   -10.101 1.00 27.68  ? 52  PRO A O   1 
ATOM   4852 C CB  . PRO B 2 9   ? 36.063 3.801   -10.497 1.00 3.72   ? 52  PRO A CB  1 
ATOM   4853 C CG  . PRO B 2 9   ? 36.550 5.187   -10.163 1.00 3.76   ? 52  PRO A CG  1 
ATOM   4854 C CD  . PRO B 2 9   ? 35.317 5.989   -10.021 1.00 3.32   ? 52  PRO A CD  1 
HETATM 4855 N N   . HZP B 2 10  ? 33.511 2.129   -12.129 1.00 22.98  ? 53  HZP A N   1 
HETATM 4856 C CA  . HZP B 2 10  ? 32.427 1.166   -11.935 1.00 13.91  ? 53  HZP A CA  1 
HETATM 4857 C C   . HZP B 2 10  ? 32.787 -0.014  -11.017 1.00 8.83   ? 53  HZP A C   1 
HETATM 4858 O O   . HZP B 2 10  ? 33.946 -0.480  -10.981 1.00 8.55   ? 53  HZP A O   1 
HETATM 4859 C CB  . HZP B 2 10  ? 32.054 0.694   -13.321 1.00 2.89   ? 53  HZP A CB  1 
HETATM 4860 C CG  . HZP B 2 10  ? 32.474 1.811   -14.227 1.00 19.19  ? 53  HZP A CG  1 
HETATM 4861 C CD  . HZP B 2 10  ? 33.607 2.547   -13.542 1.00 8.42   ? 53  HZP A CD  1 
HETATM 4862 O OD1 . HZP B 2 10  ? 32.899 1.238   -15.442 1.00 42.39  ? 53  HZP A OD1 1 
ATOM   4863 N N   . ARG B 2 11  ? 31.779 -0.465  -10.277 1.00 14.28  ? 54  ARG A N   1 
ATOM   4864 C CA  . ARG B 2 11  ? 31.925 -1.520  -9.301  1.00 15.13  ? 54  ARG A CA  1 
ATOM   4865 C C   . ARG B 2 11  ? 31.020 -2.694  -9.665  1.00 12.51  ? 54  ARG A C   1 
ATOM   4866 O O   . ARG B 2 11  ? 29.864 -2.504  -10.088 1.00 15.59  ? 54  ARG A O   1 
ATOM   4867 C CB  . ARG B 2 11  ? 31.534 -1.032  -7.899  1.00 12.81  ? 54  ARG A CB  1 
ATOM   4868 C CG  . ARG B 2 11  ? 32.580 -0.261  -7.132  1.00 9.95   ? 54  ARG A CG  1 
ATOM   4869 C CD  . ARG B 2 11  ? 32.561 -0.613  -5.620  1.00 61.31  ? 54  ARG A CD  1 
ATOM   4870 N NE  . ARG B 2 11  ? 31.213 -0.733  -5.040  1.00 57.73  ? 54  ARG A NE  1 
ATOM   4871 C CZ  . ARG B 2 11  ? 30.564 0.254   -4.419  1.00 50.85  ? 54  ARG A CZ  1 
ATOM   4872 N NH1 . ARG B 2 11  ? 31.129 1.454   -4.308  1.00 52.09  ? 54  ARG A NH1 1 
ATOM   4873 N NH2 . ARG B 2 11  ? 29.346 0.052   -3.914  1.00 39.15  ? 54  ARG A NH2 1 
ATOM   4874 N N   . HIS B 2 12  ? 31.532 -3.909  -9.501  1.00 6.85   ? 55  HIS A N   1 
ATOM   4875 C CA  . HIS B 2 12  ? 30.691 -5.091  -9.644  1.00 3.02   ? 55  HIS A CA  1 
ATOM   4876 C C   . HIS B 2 12  ? 31.090 -6.085  -8.551  1.00 9.67   ? 55  HIS A C   1 
ATOM   4877 O O   . HIS B 2 12  ? 32.095 -5.906  -7.867  1.00 3.43   ? 55  HIS A O   1 
ATOM   4878 C CB  . HIS B 2 12  ? 30.846 -5.693  -11.051 1.00 19.22  ? 55  HIS A CB  1 
ATOM   4879 C CG  . HIS B 2 12  ? 32.256 -6.099  -11.377 1.00 16.99  ? 55  HIS A CG  1 
ATOM   4880 N ND1 . HIS B 2 12  ? 32.808 -7.282  -10.939 1.00 16.95  ? 55  HIS A ND1 1 
ATOM   4881 C CD2 . HIS B 2 12  ? 33.219 -5.463  -12.074 1.00 14.48  ? 55  HIS A CD2 1 
ATOM   4882 C CE1 . HIS B 2 12  ? 34.062 -7.362  -11.356 1.00 11.69  ? 55  HIS A CE1 1 
ATOM   4883 N NE2 . HIS B 2 12  ? 34.334 -6.269  -12.053 1.00 11.69  ? 55  HIS A NE2 1 
ATOM   4884 N N   . ASN B 2 13  ? 30.301 -7.130  -8.381  1.00 11.73  ? 56  ASN A N   1 
ATOM   4885 C CA  . ASN B 2 13  ? 30.631 -8.169  -7.416  1.00 18.77  ? 56  ASN A CA  1 
ATOM   4886 C C   . ASN B 2 13  ? 31.586 -9.172  -8.038  1.00 19.14  ? 56  ASN A C   1 
ATOM   4887 O O   . ASN B 2 13  ? 32.003 -8.973  -9.178  1.00 18.04  ? 56  ASN A O   1 
ATOM   4888 C CB  . ASN B 2 13  ? 29.361 -8.858  -6.904  1.00 17.11  ? 56  ASN A CB  1 
ATOM   4889 C CG  . ASN B 2 13  ? 28.434 -7.899  -6.200  1.00 17.78  ? 56  ASN A CG  1 
ATOM   4890 O OD1 . ASN B 2 13  ? 28.406 -7.845  -4.975  1.00 32.11  ? 56  ASN A OD1 1 
ATOM   4891 N ND2 . ASN B 2 13  ? 27.685 -7.114  -6.970  1.00 17.87  ? 56  ASN A ND2 1 
ATOM   4892 O OXT . ASN B 2 13  ? 31.975 -10.171 -7.425  1.00 11.03  ? 56  ASN A OXT 1 
HETATM 4893 C C1  . NAG C 3 .   ? 25.259 -23.289 -28.407 1.00 21.46  ? 701 NAG B C1  1 
HETATM 4894 C C2  . NAG C 3 .   ? 23.997 -22.563 -28.894 1.00 23.30  ? 701 NAG B C2  1 
HETATM 4895 C C3  . NAG C 3 .   ? 23.038 -23.500 -29.618 1.00 35.25  ? 701 NAG B C3  1 
HETATM 4896 C C4  . NAG C 3 .   ? 23.783 -24.284 -30.688 1.00 40.20  ? 701 NAG B C4  1 
HETATM 4897 C C5  . NAG C 3 .   ? 24.973 -24.999 -30.054 1.00 38.88  ? 701 NAG B C5  1 
HETATM 4898 C C6  . NAG C 3 .   ? 25.777 -25.805 -31.068 1.00 47.40  ? 701 NAG B C6  1 
HETATM 4899 C C7  . NAG C 3 .   ? 23.260 -20.683 -27.579 1.00 16.63  ? 701 NAG B C7  1 
HETATM 4900 C C8  . NAG C 3 .   ? 22.418 -20.175 -26.449 1.00 18.16  ? 701 NAG B C8  1 
HETATM 4901 N N2  . NAG C 3 .   ? 23.284 -21.990 -27.774 1.00 20.56  ? 701 NAG B N2  1 
HETATM 4902 O O3  . NAG C 3 .   ? 21.940 -22.785 -30.156 1.00 35.65  ? 701 NAG B O3  1 
HETATM 4903 O O4  . NAG C 3 .   ? 22.909 -25.228 -31.263 1.00 43.91  ? 701 NAG B O4  1 
HETATM 4904 O O5  . NAG C 3 .   ? 25.833 -24.063 -29.443 1.00 29.70  ? 701 NAG B O5  1 
HETATM 4905 O O6  . NAG C 3 .   ? 26.133 -24.999 -32.173 1.00 55.63  ? 701 NAG B O6  1 
HETATM 4906 O O7  . NAG C 3 .   ? 23.899 -19.910 -28.278 1.00 17.08  ? 701 NAG B O7  1 
HETATM 4907 C C1  . NAG D 3 .   ? 22.209 -26.291 -31.975 1.00 54.22  ? 702 NAG B C1  1 
HETATM 4908 C C2  . NAG D 3 .   ? 21.498 -27.612 -32.259 1.00 59.79  ? 702 NAG B C2  1 
HETATM 4909 C C3  . NAG D 3 .   ? 20.803 -27.623 -33.623 1.00 67.53  ? 702 NAG B C3  1 
HETATM 4910 C C4  . NAG D 3 .   ? 20.138 -26.289 -33.984 1.00 65.06  ? 702 NAG B C4  1 
HETATM 4911 C C5  . NAG D 3 .   ? 21.026 -25.100 -33.612 1.00 59.88  ? 702 NAG B C5  1 
HETATM 4912 C C6  . NAG D 3 .   ? 20.332 -23.760 -33.829 1.00 55.07  ? 702 NAG B C6  1 
HETATM 4913 C C7  . NAG D 3 .   ? 22.565 -29.424 -31.048 1.00 47.64  ? 702 NAG B C7  1 
HETATM 4914 C C8  . NAG D 3 .   ? 23.409 -30.664 -31.107 1.00 34.18  ? 702 NAG B C8  1 
HETATM 4915 N N2  . NAG D 3 .   ? 22.451 -28.710 -32.165 1.00 53.15  ? 702 NAG B N2  1 
HETATM 4916 O O3  . NAG D 3 .   ? 19.831 -28.650 -33.615 1.00 71.43  ? 702 NAG B O3  1 
HETATM 4917 O O4  . NAG D 3 .   ? 19.819 -26.265 -35.366 1.00 63.67  ? 702 NAG B O4  1 
HETATM 4918 O O5  . NAG D 3 .   ? 21.369 -25.191 -32.249 1.00 58.46  ? 702 NAG B O5  1 
HETATM 4919 O O6  . NAG D 3 .   ? 19.458 -23.494 -32.752 1.00 50.66  ? 702 NAG B O6  1 
HETATM 4920 O O7  . NAG D 3 .   ? 22.013 -29.095 -29.994 1.00 52.56  ? 702 NAG B O7  1 
HETATM 4921 C C1  . NAG E 3 .   ? 37.059 -26.408 11.842  1.00 7.72   ? 703 NAG B C1  1 
HETATM 4922 C C2  . NAG E 3 .   ? 36.626 -25.010 12.261  1.00 7.40   ? 703 NAG B C2  1 
HETATM 4923 C C3  . NAG E 3 .   ? 35.302 -25.025 13.003  1.00 7.04   ? 703 NAG B C3  1 
HETATM 4924 C C4  . NAG E 3 .   ? 34.262 -25.802 12.206  1.00 6.78   ? 703 NAG B C4  1 
HETATM 4925 C C5  . NAG E 3 .   ? 34.772 -27.221 11.954  1.00 7.13   ? 703 NAG B C5  1 
HETATM 4926 C C6  . NAG E 3 .   ? 33.758 -28.070 11.172  1.00 10.28  ? 703 NAG B C6  1 
HETATM 4927 C C7  . NAG E 3 .   ? 37.895 -23.043 12.956  1.00 32.44  ? 703 NAG B C7  1 
HETATM 4928 C C8  . NAG E 3 .   ? 39.297 -22.552 13.173  1.00 7.98   ? 703 NAG B C8  1 
HETATM 4929 N N2  . NAG E 3 .   ? 37.669 -24.356 13.034  1.00 27.91  ? 703 NAG B N2  1 
HETATM 4930 O O3  . NAG E 3 .   ? 34.917 -23.685 13.081  1.00 6.74   ? 703 NAG B O3  1 
HETATM 4931 O O4  . NAG E 3 .   ? 32.958 -25.793 12.763  1.00 6.42   ? 703 NAG B O4  1 
HETATM 4932 O O5  . NAG E 3 .   ? 36.009 -27.159 11.255  1.00 7.47   ? 703 NAG B O5  1 
HETATM 4933 O O6  . NAG E 3 .   ? 33.528 -27.526 9.884   1.00 8.60   ? 703 NAG B O6  1 
HETATM 4934 O O7  . NAG E 3 .   ? 37.003 -22.233 12.722  1.00 38.52  ? 703 NAG B O7  1 
HETATM 4935 C C1  . NAG F 3 .   ? 38.009 -24.452 18.113  1.00 14.26  ? 704 NAG B C1  1 
HETATM 4936 C C2  . NAG F 3 .   ? 36.607 -24.483 17.483  1.00 7.74   ? 704 NAG B C2  1 
HETATM 4937 C C3  . NAG F 3 .   ? 36.306 -23.294 16.561  1.00 12.60  ? 704 NAG B C3  1 
HETATM 4938 C C4  . NAG F 3 .   ? 36.806 -21.983 17.148  1.00 8.71   ? 704 NAG B C4  1 
HETATM 4939 C C5  . NAG F 3 .   ? 38.287 -22.155 17.461  1.00 11.35  ? 704 NAG B C5  1 
HETATM 4940 C C6  . NAG F 3 .   ? 38.926 -20.889 18.007  1.00 18.49  ? 704 NAG B C6  1 
HETATM 4941 C C7  . NAG F 3 .   ? 35.264 -26.399 16.724  1.00 25.37  ? 704 NAG B C7  1 
HETATM 4942 C C8  . NAG F 3 .   ? 35.194 -27.613 15.836  1.00 7.58   ? 704 NAG B C8  1 
HETATM 4943 N N2  . NAG F 3 .   ? 36.428 -25.739 16.767  1.00 24.80  ? 704 NAG B N2  1 
HETATM 4944 O O3  . NAG F 3 .   ? 34.916 -23.188 16.347  1.00 17.28  ? 704 NAG B O3  1 
HETATM 4945 O O4  . NAG F 3 .   ? 36.539 -20.886 16.286  1.00 7.15   ? 704 NAG B O4  1 
HETATM 4946 O O5  . NAG F 3 .   ? 38.414 -23.140 18.465  1.00 10.71  ? 704 NAG B O5  1 
HETATM 4947 O O6  . NAG F 3 .   ? 38.392 -20.679 19.300  1.00 30.16  ? 704 NAG B O6  1 
HETATM 4948 O O7  . NAG F 3 .   ? 34.272 -26.053 17.363  1.00 7.21   ? 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 631 687 687 ILE ILE B . n 
A 1 632 SER 632 688 688 SER SER 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   PRO 3   46  46  PRO PRO A . n 
B 2 4   LYS 4   47  47  LYS LYS A . n 
B 2 5   PRO 5   48  48  PRO PRO A . n 
B 2 6   SER 6   49  49  SER SER A . n 
B 2 7   THR 7   50  50  THR THR A . n 
B 2 8   ARG 8   51  51  ARG ARG 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  ARG 11  54  54  ARG ARG A . n 
B 2 12  HIS 12  55  55  HIS HIS 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)' 3010  ? 
1 MORE         7     ? 
1 'SSA (A^2)'  26690 ? 
# 
_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      ? ? ? 'phenix.refine: 1.8_1069' 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   O4 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   NAG 
_pdbx_validate_close_contact.auth_seq_id_1    701 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O5 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   NAG 
_pdbx_validate_close_contact.auth_seq_id_2    702 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.83 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              237 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              237 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              237 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                129.44 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            14.14 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_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 ASP B 126 ? ? 60.72   64.28   
2  1 GLN B 192 ? ? -123.74 -56.21  
3  1 VAL B 217 ? ? -130.67 -49.03  
4  1 GLN B 289 ? ? -128.00 -57.40  
5  1 GLN B 295 ? ? 56.80   72.01   
6  1 VAL B 343 ? ? 60.02   74.32   
7  1 THR B 358 ? ? -27.86  -37.35  
8  1 SER B 439 ? ? 58.39   73.93   
9  1 THR B 511 ? ? 56.19   70.30   
10 1 ASP B 534 ? ? 61.35   65.68   
11 1 SER B 539 ? ? 57.94   -142.89 
12 1 THR B 552 ? ? -127.82 -56.77  
13 1 ALA B 600 ? ? -130.30 -56.30  
# 
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 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 
# 
