data_2QMJ
# 
_entry.id   2QMJ 
# 
_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   2QMJ         
RCSB  RCSB043785   
WWPDB D_1000043785 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2QLY 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2QMJ 
_pdbx_database_status.recvd_initial_deposition_date   2007-07-16 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Sim, L.'    1 
'Rose, D.R.' 2 
# 
_citation.id                        primary 
_citation.title                     
;Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            375 
_citation.page_first                782 
_citation.page_last                 792 
_citation.year                      2008 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   18036614 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2007.10.069 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Sim, L.'              1 
primary 'Quezada-Calvillo, R.' 2 
primary 'Sterchi, E.E.'        3 
primary 'Nichols, B.L.'        4 
primary 'Rose, D.R.'           5 
# 
_cell.entry_id           2QMJ 
_cell.length_a           86.970 
_cell.length_b           109.367 
_cell.length_c           109.271 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2QMJ 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Maltase-glucoamylase, intestinal' 98585.992 1   3.2.1.- ? 'SEQUENCE DATABASE RESIDUES 87-954' ? 
2 non-polymer man ALPHA-ACARBOSE                     645.605   1   ?       ? ?                                   ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE             221.208   4   ?       ? ?                                   ? 
4 non-polymer syn 'SULFATE ION'                      96.063    1   ?       ? ?                                   ? 
5 non-polymer syn GLYCEROL                           92.094    9   ?       ? ?                                   ? 
6 water       nat water                              18.015    626 ?       ? ?                                   ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWAH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ALA n 
1 3   GLU n 
1 4   CYS n 
1 5   PRO n 
1 6   VAL n 
1 7   VAL n 
1 8   ASN n 
1 9   GLU n 
1 10  LEU n 
1 11  GLU n 
1 12  ARG n 
1 13  ILE n 
1 14  ASN n 
1 15  CYS n 
1 16  ILE n 
1 17  PRO n 
1 18  ASP n 
1 19  GLN n 
1 20  PRO n 
1 21  PRO n 
1 22  THR n 
1 23  LYS n 
1 24  ALA n 
1 25  THR n 
1 26  CYS n 
1 27  ASP n 
1 28  GLN n 
1 29  ARG n 
1 30  GLY n 
1 31  CYS n 
1 32  CYS n 
1 33  TRP n 
1 34  ASN n 
1 35  PRO n 
1 36  GLN n 
1 37  GLY n 
1 38  ALA n 
1 39  VAL n 
1 40  SER n 
1 41  VAL n 
1 42  PRO n 
1 43  TRP n 
1 44  CYS n 
1 45  TYR n 
1 46  TYR n 
1 47  SER n 
1 48  LYS n 
1 49  ASN n 
1 50  HIS n 
1 51  SER n 
1 52  TYR n 
1 53  HIS n 
1 54  VAL n 
1 55  GLU n 
1 56  GLY n 
1 57  ASN n 
1 58  LEU n 
1 59  VAL n 
1 60  ASN n 
1 61  THR n 
1 62  ASN n 
1 63  ALA n 
1 64  GLY n 
1 65  PHE n 
1 66  THR n 
1 67  ALA n 
1 68  ARG n 
1 69  LEU n 
1 70  LYS n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  SER n 
1 76  PRO n 
1 77  VAL n 
1 78  PHE n 
1 79  GLY n 
1 80  SER n 
1 81  ASN n 
1 82  VAL n 
1 83  ASP n 
1 84  ASN n 
1 85  VAL n 
1 86  LEU n 
1 87  LEU n 
1 88  THR n 
1 89  ALA n 
1 90  GLU n 
1 91  TYR n 
1 92  GLN n 
1 93  THR n 
1 94  SER n 
1 95  ASN n 
1 96  ARG n 
1 97  PHE n 
1 98  HIS n 
1 99  PHE n 
1 100 LYS n 
1 101 LEU n 
1 102 THR n 
1 103 ASP n 
1 104 GLN n 
1 105 THR n 
1 106 ASN n 
1 107 ASN n 
1 108 ARG n 
1 109 PHE n 
1 110 GLU n 
1 111 VAL n 
1 112 PRO n 
1 113 HIS n 
1 114 GLU n 
1 115 HIS n 
1 116 VAL n 
1 117 GLN n 
1 118 SER n 
1 119 PHE n 
1 120 SER n 
1 121 GLY n 
1 122 ASN n 
1 123 ALA n 
1 124 ALA n 
1 125 ALA n 
1 126 SER n 
1 127 LEU n 
1 128 THR n 
1 129 TYR n 
1 130 GLN n 
1 131 VAL n 
1 132 GLU n 
1 133 ILE n 
1 134 SER n 
1 135 ARG n 
1 136 GLN n 
1 137 PRO n 
1 138 PHE n 
1 139 SER n 
1 140 ILE n 
1 141 LYS n 
1 142 VAL n 
1 143 THR n 
1 144 ARG n 
1 145 ARG n 
1 146 SER n 
1 147 ASN n 
1 148 ASN n 
1 149 ARG n 
1 150 VAL n 
1 151 LEU n 
1 152 PHE n 
1 153 ASP n 
1 154 SER n 
1 155 SER n 
1 156 ILE n 
1 157 GLY n 
1 158 PRO n 
1 159 LEU n 
1 160 LEU n 
1 161 PHE n 
1 162 ALA n 
1 163 ASP n 
1 164 GLN n 
1 165 PHE n 
1 166 LEU n 
1 167 GLN n 
1 168 LEU n 
1 169 SER n 
1 170 THR n 
1 171 ARG n 
1 172 LEU n 
1 173 PRO n 
1 174 SER n 
1 175 THR n 
1 176 ASN n 
1 177 VAL n 
1 178 TYR n 
1 179 GLY n 
1 180 LEU n 
1 181 GLY n 
1 182 GLU n 
1 183 HIS n 
1 184 VAL n 
1 185 HIS n 
1 186 GLN n 
1 187 GLN n 
1 188 TYR n 
1 189 ARG n 
1 190 HIS n 
1 191 ASP n 
1 192 MET n 
1 193 ASN n 
1 194 TRP n 
1 195 LYS n 
1 196 THR n 
1 197 TRP n 
1 198 PRO n 
1 199 ILE n 
1 200 PHE n 
1 201 ASN n 
1 202 ARG n 
1 203 ASP n 
1 204 THR n 
1 205 THR n 
1 206 PRO n 
1 207 ASN n 
1 208 GLY n 
1 209 ASN n 
1 210 GLY n 
1 211 THR n 
1 212 ASN n 
1 213 LEU n 
1 214 TYR n 
1 215 GLY n 
1 216 ALA n 
1 217 GLN n 
1 218 THR n 
1 219 PHE n 
1 220 PHE n 
1 221 LEU n 
1 222 CYS n 
1 223 LEU n 
1 224 GLU n 
1 225 ASP n 
1 226 ALA n 
1 227 SER n 
1 228 GLY n 
1 229 LEU n 
1 230 SER n 
1 231 PHE n 
1 232 GLY n 
1 233 VAL n 
1 234 PHE n 
1 235 LEU n 
1 236 MET n 
1 237 ASN n 
1 238 SER n 
1 239 ASN n 
1 240 ALA n 
1 241 MET n 
1 242 GLU n 
1 243 VAL n 
1 244 VAL n 
1 245 LEU n 
1 246 GLN n 
1 247 PRO n 
1 248 ALA n 
1 249 PRO n 
1 250 ALA n 
1 251 ILE n 
1 252 THR n 
1 253 TYR n 
1 254 ARG n 
1 255 THR n 
1 256 ILE n 
1 257 GLY n 
1 258 GLY n 
1 259 ILE n 
1 260 LEU n 
1 261 ASP n 
1 262 PHE n 
1 263 TYR n 
1 264 VAL n 
1 265 PHE n 
1 266 LEU n 
1 267 GLY n 
1 268 ASN n 
1 269 THR n 
1 270 PRO n 
1 271 GLU n 
1 272 GLN n 
1 273 VAL n 
1 274 VAL n 
1 275 GLN n 
1 276 GLU n 
1 277 TYR n 
1 278 LEU n 
1 279 GLU n 
1 280 LEU n 
1 281 ILE n 
1 282 GLY n 
1 283 ARG n 
1 284 PRO n 
1 285 ALA n 
1 286 LEU n 
1 287 PRO n 
1 288 SER n 
1 289 TYR n 
1 290 TRP n 
1 291 ALA n 
1 292 LEU n 
1 293 GLY n 
1 294 PHE n 
1 295 HIS n 
1 296 LEU n 
1 297 SER n 
1 298 ARG n 
1 299 TYR n 
1 300 GLU n 
1 301 TYR n 
1 302 GLY n 
1 303 THR n 
1 304 LEU n 
1 305 ASP n 
1 306 ASN n 
1 307 MET n 
1 308 ARG n 
1 309 GLU n 
1 310 VAL n 
1 311 VAL n 
1 312 GLU n 
1 313 ARG n 
1 314 ASN n 
1 315 ARG n 
1 316 ALA n 
1 317 ALA n 
1 318 GLN n 
1 319 LEU n 
1 320 PRO n 
1 321 TYR n 
1 322 ASP n 
1 323 VAL n 
1 324 GLN n 
1 325 HIS n 
1 326 ALA n 
1 327 ASP n 
1 328 ILE n 
1 329 ASP n 
1 330 TYR n 
1 331 MET n 
1 332 ASP n 
1 333 GLU n 
1 334 ARG n 
1 335 ARG n 
1 336 ASP n 
1 337 PHE n 
1 338 THR n 
1 339 TYR n 
1 340 ASP n 
1 341 SER n 
1 342 VAL n 
1 343 ASP n 
1 344 PHE n 
1 345 LYS n 
1 346 GLY n 
1 347 PHE n 
1 348 PRO n 
1 349 GLU n 
1 350 PHE n 
1 351 VAL n 
1 352 ASN n 
1 353 GLU n 
1 354 LEU n 
1 355 HIS n 
1 356 ASN n 
1 357 ASN n 
1 358 GLY n 
1 359 GLN n 
1 360 LYS n 
1 361 LEU n 
1 362 VAL n 
1 363 ILE n 
1 364 ILE n 
1 365 VAL n 
1 366 ASP n 
1 367 PRO n 
1 368 ALA n 
1 369 ILE n 
1 370 SER n 
1 371 ASN n 
1 372 ASN n 
1 373 SER n 
1 374 SER n 
1 375 SER n 
1 376 SER n 
1 377 LYS n 
1 378 PRO n 
1 379 TYR n 
1 380 GLY n 
1 381 PRO n 
1 382 TYR n 
1 383 ASP n 
1 384 ARG n 
1 385 GLY n 
1 386 SER n 
1 387 ASP n 
1 388 MET n 
1 389 LYS n 
1 390 ILE n 
1 391 TRP n 
1 392 VAL n 
1 393 ASN n 
1 394 SER n 
1 395 SER n 
1 396 ASP n 
1 397 GLY n 
1 398 VAL n 
1 399 THR n 
1 400 PRO n 
1 401 LEU n 
1 402 ILE n 
1 403 GLY n 
1 404 GLU n 
1 405 VAL n 
1 406 TRP n 
1 407 PRO n 
1 408 GLY n 
1 409 GLN n 
1 410 THR n 
1 411 VAL n 
1 412 PHE n 
1 413 PRO n 
1 414 ASP n 
1 415 TYR n 
1 416 THR n 
1 417 ASN n 
1 418 PRO n 
1 419 ASN n 
1 420 CYS n 
1 421 ALA n 
1 422 VAL n 
1 423 TRP n 
1 424 TRP n 
1 425 THR n 
1 426 LYS n 
1 427 GLU n 
1 428 PHE n 
1 429 GLU n 
1 430 LEU n 
1 431 PHE n 
1 432 HIS n 
1 433 ASN n 
1 434 GLN n 
1 435 VAL n 
1 436 GLU n 
1 437 PHE n 
1 438 ASP n 
1 439 GLY n 
1 440 ILE n 
1 441 TRP n 
1 442 ILE n 
1 443 ASP n 
1 444 MET n 
1 445 ASN n 
1 446 GLU n 
1 447 VAL n 
1 448 SER n 
1 449 ASN n 
1 450 PHE n 
1 451 VAL n 
1 452 ASP n 
1 453 GLY n 
1 454 SER n 
1 455 VAL n 
1 456 SER n 
1 457 GLY n 
1 458 CYS n 
1 459 SER n 
1 460 THR n 
1 461 ASN n 
1 462 ASN n 
1 463 LEU n 
1 464 ASN n 
1 465 ASN n 
1 466 PRO n 
1 467 PRO n 
1 468 PHE n 
1 469 THR n 
1 470 PRO n 
1 471 ARG n 
1 472 ILE n 
1 473 LEU n 
1 474 ASP n 
1 475 GLY n 
1 476 TYR n 
1 477 LEU n 
1 478 PHE n 
1 479 CYS n 
1 480 LYS n 
1 481 THR n 
1 482 LEU n 
1 483 CYS n 
1 484 MET n 
1 485 ASP n 
1 486 ALA n 
1 487 VAL n 
1 488 GLN n 
1 489 HIS n 
1 490 TRP n 
1 491 GLY n 
1 492 LYS n 
1 493 GLN n 
1 494 TYR n 
1 495 ASP n 
1 496 ILE n 
1 497 HIS n 
1 498 ASN n 
1 499 LEU n 
1 500 TYR n 
1 501 GLY n 
1 502 TYR n 
1 503 SER n 
1 504 MET n 
1 505 ALA n 
1 506 VAL n 
1 507 ALA n 
1 508 THR n 
1 509 ALA n 
1 510 GLU n 
1 511 ALA n 
1 512 ALA n 
1 513 LYS n 
1 514 THR n 
1 515 VAL n 
1 516 PHE n 
1 517 PRO n 
1 518 ASN n 
1 519 LYS n 
1 520 ARG n 
1 521 SER n 
1 522 PHE n 
1 523 ILE n 
1 524 LEU n 
1 525 THR n 
1 526 ARG n 
1 527 SER n 
1 528 THR n 
1 529 PHE n 
1 530 ALA n 
1 531 GLY n 
1 532 SER n 
1 533 GLY n 
1 534 LYS n 
1 535 PHE n 
1 536 ALA n 
1 537 ALA n 
1 538 HIS n 
1 539 TRP n 
1 540 LEU n 
1 541 GLY n 
1 542 ASP n 
1 543 ASN n 
1 544 THR n 
1 545 ALA n 
1 546 THR n 
1 547 TRP n 
1 548 ASP n 
1 549 ASP n 
1 550 LEU n 
1 551 ARG n 
1 552 TRP n 
1 553 SER n 
1 554 ILE n 
1 555 PRO n 
1 556 GLY n 
1 557 VAL n 
1 558 LEU n 
1 559 GLU n 
1 560 PHE n 
1 561 ASN n 
1 562 LEU n 
1 563 PHE n 
1 564 GLY n 
1 565 ILE n 
1 566 PRO n 
1 567 MET n 
1 568 VAL n 
1 569 GLY n 
1 570 PRO n 
1 571 ASP n 
1 572 ILE n 
1 573 CYS n 
1 574 GLY n 
1 575 PHE n 
1 576 ALA n 
1 577 LEU n 
1 578 ASP n 
1 579 THR n 
1 580 PRO n 
1 581 GLU n 
1 582 GLU n 
1 583 LEU n 
1 584 CYS n 
1 585 ARG n 
1 586 ARG n 
1 587 TRP n 
1 588 MET n 
1 589 GLN n 
1 590 LEU n 
1 591 GLY n 
1 592 ALA n 
1 593 PHE n 
1 594 TYR n 
1 595 PRO n 
1 596 PHE n 
1 597 SER n 
1 598 ARG n 
1 599 ASN n 
1 600 HIS n 
1 601 ASN n 
1 602 GLY n 
1 603 GLN n 
1 604 GLY n 
1 605 TYR n 
1 606 LYS n 
1 607 ASP n 
1 608 GLN n 
1 609 ASP n 
1 610 PRO n 
1 611 ALA n 
1 612 SER n 
1 613 PHE n 
1 614 GLY n 
1 615 ALA n 
1 616 ASP n 
1 617 SER n 
1 618 LEU n 
1 619 LEU n 
1 620 LEU n 
1 621 ASN n 
1 622 SER n 
1 623 SER n 
1 624 ARG n 
1 625 HIS n 
1 626 TYR n 
1 627 LEU n 
1 628 ASN n 
1 629 ILE n 
1 630 ARG n 
1 631 TYR n 
1 632 THR n 
1 633 LEU n 
1 634 LEU n 
1 635 PRO n 
1 636 TYR n 
1 637 LEU n 
1 638 TYR n 
1 639 THR n 
1 640 LEU n 
1 641 PHE n 
1 642 PHE n 
1 643 ARG n 
1 644 ALA n 
1 645 HIS n 
1 646 SER n 
1 647 ARG n 
1 648 GLY n 
1 649 ASP n 
1 650 THR n 
1 651 VAL n 
1 652 ALA n 
1 653 ARG n 
1 654 PRO n 
1 655 LEU n 
1 656 LEU n 
1 657 HIS n 
1 658 GLU n 
1 659 PHE n 
1 660 TYR n 
1 661 GLU n 
1 662 ASP n 
1 663 ASN n 
1 664 SER n 
1 665 THR n 
1 666 TRP n 
1 667 ASP n 
1 668 VAL n 
1 669 HIS n 
1 670 GLN n 
1 671 GLN n 
1 672 PHE n 
1 673 LEU n 
1 674 TRP n 
1 675 GLY n 
1 676 PRO n 
1 677 GLY n 
1 678 LEU n 
1 679 LEU n 
1 680 ILE n 
1 681 THR n 
1 682 PRO n 
1 683 VAL n 
1 684 LEU n 
1 685 ASP n 
1 686 GLU n 
1 687 GLY n 
1 688 ALA n 
1 689 GLU n 
1 690 LYS n 
1 691 VAL n 
1 692 MET n 
1 693 ALA n 
1 694 TYR n 
1 695 VAL n 
1 696 PRO n 
1 697 ASP n 
1 698 ALA n 
1 699 VAL n 
1 700 TRP n 
1 701 TYR n 
1 702 ASP n 
1 703 TYR n 
1 704 GLU n 
1 705 THR n 
1 706 GLY n 
1 707 SER n 
1 708 GLN n 
1 709 VAL n 
1 710 ARG n 
1 711 TRP n 
1 712 ARG n 
1 713 LYS n 
1 714 GLN n 
1 715 LYS n 
1 716 VAL n 
1 717 GLU n 
1 718 MET n 
1 719 GLU n 
1 720 LEU n 
1 721 PRO n 
1 722 GLY n 
1 723 ASP n 
1 724 LYS n 
1 725 ILE n 
1 726 GLY n 
1 727 LEU n 
1 728 HIS n 
1 729 LEU n 
1 730 ARG n 
1 731 GLY n 
1 732 GLY n 
1 733 TYR n 
1 734 ILE n 
1 735 PHE n 
1 736 PRO n 
1 737 THR n 
1 738 GLN n 
1 739 GLN n 
1 740 PRO n 
1 741 ASN n 
1 742 THR n 
1 743 THR n 
1 744 THR n 
1 745 LEU n 
1 746 ALA n 
1 747 SER n 
1 748 ARG n 
1 749 LYS n 
1 750 ASN n 
1 751 PRO n 
1 752 LEU n 
1 753 GLY n 
1 754 LEU n 
1 755 ILE n 
1 756 ILE n 
1 757 ALA n 
1 758 LEU n 
1 759 ASP n 
1 760 GLU n 
1 761 ASN n 
1 762 LYS n 
1 763 GLU n 
1 764 ALA n 
1 765 LYS n 
1 766 GLY n 
1 767 GLU n 
1 768 LEU n 
1 769 PHE n 
1 770 TRP n 
1 771 ASP n 
1 772 ASP n 
1 773 GLY n 
1 774 GLU n 
1 775 THR n 
1 776 LYS n 
1 777 ASP n 
1 778 THR n 
1 779 VAL n 
1 780 ALA n 
1 781 ASN n 
1 782 LYS n 
1 783 VAL n 
1 784 TYR n 
1 785 LEU n 
1 786 LEU n 
1 787 CYS n 
1 788 GLU n 
1 789 PHE n 
1 790 SER n 
1 791 VAL n 
1 792 THR n 
1 793 GLN n 
1 794 ASN n 
1 795 ARG n 
1 796 LEU n 
1 797 GLU n 
1 798 VAL n 
1 799 ASN n 
1 800 ILE n 
1 801 SER n 
1 802 GLN n 
1 803 SER n 
1 804 THR n 
1 805 TYR n 
1 806 LYS n 
1 807 ASP n 
1 808 PRO n 
1 809 ASN n 
1 810 ASN n 
1 811 LEU n 
1 812 ALA n 
1 813 PHE n 
1 814 ASN n 
1 815 GLU n 
1 816 ILE n 
1 817 LYS n 
1 818 ILE n 
1 819 LEU n 
1 820 GLY n 
1 821 THR n 
1 822 GLU n 
1 823 GLU n 
1 824 PRO n 
1 825 SER n 
1 826 ASN n 
1 827 VAL n 
1 828 THR n 
1 829 VAL n 
1 830 LYS n 
1 831 HIS n 
1 832 ASN n 
1 833 GLY n 
1 834 VAL n 
1 835 PRO n 
1 836 SER n 
1 837 GLN n 
1 838 THR n 
1 839 SER n 
1 840 PRO n 
1 841 THR n 
1 842 VAL n 
1 843 THR n 
1 844 TYR n 
1 845 ASP n 
1 846 SER n 
1 847 ASN n 
1 848 LEU n 
1 849 LYS n 
1 850 VAL n 
1 851 ALA n 
1 852 ILE n 
1 853 ILE n 
1 854 THR n 
1 855 ASP n 
1 856 ILE n 
1 857 ASP n 
1 858 LEU n 
1 859 LEU n 
1 860 LEU n 
1 861 GLY n 
1 862 GLU n 
1 863 ALA n 
1 864 TYR n 
1 865 THR n 
1 866 VAL n 
1 867 GLU n 
1 868 TRP n 
1 869 ALA n 
1 870 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 'MGAM, MGA, MGAML' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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               'fruit fly' 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_entity_src_gen.host_org_genus                     Drosophila 
_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               'S2 cells' 
_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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMT-BiP-V5-His 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MGA_HUMAN 
_struct_ref.pdbx_db_accession          O43451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGS
NVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLL
FADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNA
MEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLP
YDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTP
LIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCK
TLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEF
NLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTL
FFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMEL
PGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDDGETKDTVANKVYLLCEFSVTQNRLEVNI
SQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEW
;
_struct_ref.pdbx_align_begin           87 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              2QMJ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 868 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O43451 
_struct_ref_seq.db_align_beg                  87 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  954 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       868 
# 
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 2QMJ ALA A 869 ? UNP O43451 ? ? 'EXPRESSION TAG' 869 1 
1 2QMJ HIS A 870 ? UNP O43451 ? ? 'EXPRESSION TAG' 870 2 
# 
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 
ACR saccharide          . ALPHA-ACARBOSE         '1,4-DEOXY-4-((5-HYDROXYMETHYL-2,3,4-TRIHYDROXYCYCLOHEX-5,6-ENYL)AMINO)FRUCTOSE' 
'C25 H43 N O18'  645.605 
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  
GOL non-polymer         . GLYCEROL               'GLYCERIN; PROPANE-1,2,3-TRIOL'                                                  
'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE              ?                                                                                
'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ?                                                                                
'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ?                                                                                
'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ?                                                                                
'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ?                                                                                
'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ?                                                                                
'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ?                                                                                
'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ?                                                                                
'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ?                                                                                
'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ?                                                                                
'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'          ?                                                                                
'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE              ?                                                                                
'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ?                                                                                
'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ?                                                                                
'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ?                                                                                
'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          2QMJ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.64 
_exptl_crystal.density_percent_sol   53.33 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
'20% PEG 3350, 0.2M sodium sulfate, 4% 1,1,1,3,3,3-hexafluoro-2-propanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2007-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9175 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE F1' 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9175 
# 
_reflns.entry_id                     2QMJ 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.d_resolution_high            1.9 
_reflns.d_resolution_low             30 
_reflns.number_all                   ? 
_reflns.number_obs                   82234 
_reflns.percent_possible_obs         98.7 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.109 
_reflns.pdbx_netI_over_sigmaI        15.3 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              7.6 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.90 
_reflns_shell.d_res_low              1.97 
_reflns_shell.percent_possible_all   96.2 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.401 
_reflns_shell.meanI_over_sigI_obs    3.4 
_reflns_shell.pdbx_redundancy        6.4 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      7898 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2QMJ 
_refine.ls_number_reflns_obs                     77676 
_refine.ls_number_reflns_all                     77676 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.78 
_refine.ls_d_res_high                            1.9 
_refine.ls_percent_reflns_obs                    98.16 
_refine.ls_R_factor_obs                          0.17923 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17729 
_refine.ls_R_factor_R_free                       0.21516 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  4082 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.954 
_refine.correlation_coeff_Fo_to_Fc_free          0.939 
_refine.B_iso_mean                               24.108 
_refine.aniso_B[1][1]                            0.00 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB entry 2QLY' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.140 
_refine.pdbx_overall_ESU_R_Free                  0.132 
_refine.overall_SU_ML                            0.091 
_refine.overall_SU_B                             3.081 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6912 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         159 
_refine_hist.number_atoms_solvent             626 
_refine_hist.number_atoms_total               7697 
_refine_hist.d_res_high                       1.9 
_refine_hist.d_res_low                        19.78 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         0.016  0.022  ? 7319 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      1.672  1.959  ? 9986 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   6.847  5.000  ? 871  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   36.176 24.317 ? 366  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   12.914 15.000 ? 1103 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   18.486 15.000 ? 39   'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.116  0.200  ? 1080 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.007  0.020  ? 5660 'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.209  0.200  ? 3620 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          0.318  0.200  ? 5025 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.162  0.200  ? 662  'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.240  0.200  ? 68   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.171  0.200  ? 20   'X-RAY DIFFRACTION' ? 
r_mcbond_it              1.110  1.500  ? 4424 'X-RAY DIFFRACTION' ? 
r_mcangle_it             1.750  2.000  ? 7006 'X-RAY DIFFRACTION' ? 
r_scbond_it              2.713  3.000  ? 3328 'X-RAY DIFFRACTION' ? 
r_scangle_it             4.098  4.500  ? 2971 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.9 
_refine_ls_shell.d_res_low                        1.943 
_refine_ls_shell.number_reflns_R_work             5349 
_refine_ls_shell.R_factor_R_work                  0.259 
_refine_ls_shell.percent_reflns_obs               93.15 
_refine_ls_shell.R_factor_R_free                  0.343 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             269 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2QMJ 
_struct.title                     
'Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose' 
_struct.pdbx_descriptor           'Maltase-glucoamylase, intestinal' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2QMJ 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Hydrolase, Glycosyl Hydrolase Family 31, Glycoprotein, Glycosidase, Membrane, Multifunctional enzyme, Signal-anchor, Sulfation, Transmembrane
;
# 
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 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 5 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 6 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
1 'The biological assembly is a monomer' 
0 ?                                      
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ASN A 8   ? ARG A 12  ? ASN A 8   ARG A 12  5 ? 5  
HELX_P HELX_P2  2  THR A 22  ? GLY A 30  ? THR A 22  GLY A 30  1 ? 9  
HELX_P HELX_P3  3  SER A 155 ? GLY A 157 ? SER A 155 GLY A 157 5 ? 3  
HELX_P HELX_P4  4  THR A 269 ? GLY A 282 ? THR A 269 GLY A 282 1 ? 14 
HELX_P HELX_P5  5  SER A 288 ? LEU A 292 ? SER A 288 LEU A 292 5 ? 5  
HELX_P HELX_P6  6  THR A 303 ? ALA A 317 ? THR A 303 ALA A 317 1 ? 15 
HELX_P HELX_P7  7  ASP A 327 ? MET A 331 ? ASP A 327 MET A 331 5 ? 5  
HELX_P HELX_P8  8  GLY A 346 ? ASN A 357 ? GLY A 346 ASN A 357 1 ? 12 
HELX_P HELX_P9  9  TYR A 379 ? LYS A 389 ? TYR A 379 LYS A 389 1 ? 11 
HELX_P HELX_P10 10 ASN A 417 ? ASN A 433 ? ASN A 417 ASN A 433 1 ? 17 
HELX_P HELX_P11 11 ILE A 472 ? TYR A 476 ? ILE A 472 TYR A 476 5 ? 5  
HELX_P HELX_P12 12 GLN A 493 ? HIS A 497 ? GLN A 493 HIS A 497 1 ? 5  
HELX_P HELX_P13 13 LEU A 499 ? PHE A 516 ? LEU A 499 PHE A 516 1 ? 18 
HELX_P HELX_P14 14 GLY A 531 ? PHE A 535 ? GLY A 531 PHE A 535 5 ? 5  
HELX_P HELX_P15 15 THR A 546 ? PHE A 563 ? THR A 546 PHE A 563 1 ? 18 
HELX_P HELX_P16 16 PRO A 580 ? ALA A 592 ? PRO A 580 ALA A 592 1 ? 13 
HELX_P HELX_P17 17 ASP A 609 ? GLY A 614 ? ASP A 609 GLY A 614 5 ? 6  
HELX_P HELX_P18 18 SER A 617 ? LEU A 633 ? SER A 617 LEU A 633 1 ? 17 
HELX_P HELX_P19 19 LEU A 633 ? ARG A 647 ? LEU A 633 ARG A 647 1 ? 15 
HELX_P HELX_P20 20 PRO A 654 ? PHE A 659 ? PRO A 654 PHE A 659 1 ? 6  
HELX_P HELX_P21 21 ASP A 662 ? TRP A 666 ? ASP A 662 TRP A 666 5 ? 5  
HELX_P HELX_P22 22 THR A 743 ? ARG A 748 ? THR A 743 ARG A 748 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 15  SG  ? ? ? 1_555 A CYS 31  SG ? ? A CYS 15   A CYS 31   1_555 ? ? ? ? ? ? ? 2.063 ? 
disulf2 disulf ? ? A CYS 26  SG  ? ? ? 1_555 A CYS 44  SG ? ? A CYS 26   A CYS 44   1_555 ? ? ? ? ? ? ? 2.916 ? 
disulf3 disulf ? ? A CYS 573 SG  ? ? ? 1_555 A CYS 584 SG ? ? A CYS 573  A CYS 584  1_555 ? ? ? ? ? ? ? 2.086 ? 
covale1 covale ? ? A ASN 209 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 209  A NAG 2005 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale2 covale ? ? A ASN 393 ND2 ? ? ? 1_555 O NAG .   C1 ? ? A ASN 393  X NAG 2003 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale3 covale ? ? A ASN 741 ND2 A ? ? 1_555 C NAG .   C1 A ? A ASN 741  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale4 covale ? ? A ASN 741 ND2 B ? ? 1_555 C NAG .   C1 B ? A ASN 741  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale5 covale ? ? O NAG .   O4  ? ? ? 1_555 P NAG .   C1 ? ? X NAG 2003 X NAG 2004 1_555 ? ? ? ? ? ? ? 1.442 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLN 136 A . ? GLN 136 A PRO 137 A ? PRO 137 A 1 3.32  
2 GLY 181 A . ? GLY 181 A GLU 182 A ? GLU 182 A 1 -3.15 
3 ALA 248 A . ? ALA 248 A PRO 249 A ? PRO 249 A 1 -2.67 
4 GLU 446 A . ? GLU 446 A VAL 447 A ? VAL 447 A 1 4.87  
5 PRO 835 A . ? PRO 835 A SER 836 A ? SER 836 A 1 15.30 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 8  ? 
C ? 3  ? 
D ? 5  ? 
E ? 9  ? 
F ? 3  ? 
G ? 2  ? 
H ? 5  ? 
I ? 2  ? 
J ? 10 ? 
K ? 9  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? anti-parallel 
B 1 2  ? anti-parallel 
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? anti-parallel 
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
D 1 2  ? anti-parallel 
D 2 3  ? anti-parallel 
D 3 4  ? anti-parallel 
D 4 5  ? anti-parallel 
E 1 2  ? parallel      
E 2 3  ? parallel      
E 3 4  ? parallel      
E 4 5  ? parallel      
E 5 6  ? parallel      
E 6 7  ? parallel      
E 7 8  ? parallel      
E 8 9  ? parallel      
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
G 1 2  ? anti-parallel 
H 1 2  ? anti-parallel 
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? anti-parallel 
I 1 2  ? anti-parallel 
J 1 2  ? anti-parallel 
J 2 3  ? anti-parallel 
J 3 4  ? anti-parallel 
J 4 5  ? anti-parallel 
J 5 6  ? parallel      
J 6 7  ? anti-parallel 
J 7 8  ? parallel      
J 8 9  ? anti-parallel 
J 9 10 ? anti-parallel 
K 1 2  ? anti-parallel 
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? anti-parallel 
K 5 6  ? parallel      
K 6 7  ? anti-parallel 
K 7 8  ? parallel      
K 8 9  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  CYS A 32  ? TRP A 33  ? CYS A 32  TRP A 33  
A 2  CYS A 44  ? TYR A 45  ? CYS A 44  TYR A 45  
B 1  TYR A 52  ? ASN A 60  ? TYR A 52  ASN A 60  
B 2  GLY A 64  ? ASN A 71  ? GLY A 64  ASN A 71  
B 3  ASN A 84  ? THR A 93  ? ASN A 84  THR A 93  
B 4  ARG A 96  ? ASP A 103 ? ARG A 96  ASP A 103 
B 5  LEU A 260 ? GLY A 267 ? LEU A 260 GLY A 267 
B 6  SER A 230 ? LEU A 235 ? SER A 230 LEU A 235 
B 7  GLN A 217 ? LEU A 223 ? GLN A 217 LEU A 223 
B 8  VAL A 177 ? GLY A 181 ? VAL A 177 GLY A 181 
C 1  TYR A 129 ? SER A 134 ? TYR A 129 SER A 134 
C 2  SER A 139 ? ARG A 144 ? SER A 139 ARG A 144 
C 3  VAL A 150 ? ASP A 153 ? VAL A 150 ASP A 153 
D 1  LEU A 160 ? ALA A 162 ? LEU A 160 ALA A 162 
D 2  PHE A 165 ? ARG A 171 ? PHE A 165 ARG A 171 
D 3  ALA A 250 ? THR A 255 ? ALA A 250 THR A 255 
D 4  MET A 241 ? GLN A 246 ? MET A 241 GLN A 246 
D 5  LYS A 195 ? ILE A 199 ? LYS A 195 ILE A 199 
E 1  VAL A 568 ? GLY A 569 ? VAL A 568 GLY A 569 
E 2  ALA A 537 ? TRP A 539 ? ALA A 537 TRP A 539 
E 3  ILE A 523 ? THR A 525 ? ILE A 523 THR A 525 
E 4  GLY A 439 ? ILE A 442 ? GLY A 439 ILE A 442 
E 5  LYS A 360 ? VAL A 365 ? LYS A 360 VAL A 365 
E 6  VAL A 323 ? ALA A 326 ? VAL A 323 ALA A 326 
E 7  PHE A 294 ? LEU A 296 ? PHE A 294 LEU A 296 
E 8  SER A 597 ? ASN A 599 ? SER A 597 ASN A 599 
E 9  ASP A 571 ? ILE A 572 ? ASP A 571 ILE A 572 
F 1  ILE A 369 ? SER A 370 ? ILE A 369 SER A 370 
F 2  GLY A 408 ? VAL A 411 ? GLY A 408 VAL A 411 
F 3  GLY A 403 ? VAL A 405 ? GLY A 403 VAL A 405 
G 1  VAL A 487 ? GLN A 488 ? VAL A 487 GLN A 488 
G 2  GLY A 491 ? LYS A 492 ? GLY A 491 LYS A 492 
H 1  ALA A 652 ? ARG A 653 ? ALA A 652 ARG A 653 
H 2  PHE A 672 ? TRP A 674 ? PHE A 672 TRP A 674 
H 3  LEU A 678 ? THR A 681 ? LEU A 678 THR A 681 
H 4  GLY A 726 ? ARG A 730 ? GLY A 726 ARG A 730 
H 5  TRP A 700 ? ASP A 702 ? TRP A 700 ASP A 702 
I 1  LYS A 690 ? VAL A 695 ? LYS A 690 VAL A 695 
I 2  GLN A 714 ? GLU A 719 ? GLN A 714 GLU A 719 
J 1  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
J 2  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
J 3  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
J 4  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
J 5  GLU A 763 ? TRP A 770 ? GLU A 763 TRP A 770 
J 6  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
J 7  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
J 8  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
J 9  VAL A 850 ? THR A 854 ? VAL A 850 THR A 854 
J 10 THR A 841 ? ASP A 845 ? THR A 841 ASP A 845 
K 1  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
K 2  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
K 3  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
K 4  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
K 5  GLU A 763 ? TRP A 770 ? GLU A 763 TRP A 770 
K 6  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
K 7  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
K 8  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
K 9  LEU A 858 ? LEU A 859 ? LEU A 858 LEU A 859 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N CYS A 32  ? N CYS A 32  O TYR A 45  ? O TYR A 45  
B 1 2  N HIS A 53  ? N HIS A 53  O LYS A 70  ? O LYS A 70  
B 2 3  N LEU A 69  ? N LEU A 69  O VAL A 85  ? O VAL A 85  
B 3 4  N GLU A 90  ? N GLU A 90  O HIS A 98  ? O HIS A 98  
B 4 5  N PHE A 99  ? N PHE A 99  O PHE A 262 ? O PHE A 262 
B 5 6  O GLY A 267 ? O GLY A 267 N SER A 230 ? N SER A 230 
B 6 7  O PHE A 231 ? O PHE A 231 N CYS A 222 ? N CYS A 222 
B 7 8  O LEU A 221 ? O LEU A 221 N TYR A 178 ? N TYR A 178 
C 1 2  N GLN A 130 ? N GLN A 130 O THR A 143 ? O THR A 143 
C 2 3  N VAL A 142 ? N VAL A 142 O LEU A 151 ? O LEU A 151 
D 1 2  N ALA A 162 ? N ALA A 162 O PHE A 165 ? O PHE A 165 
D 2 3  N LEU A 166 ? N LEU A 166 O THR A 255 ? O THR A 255 
D 3 4  O THR A 252 ? O THR A 252 N VAL A 244 ? N VAL A 244 
D 4 5  O LEU A 245 ? O LEU A 245 N LYS A 195 ? N LYS A 195 
E 1 2  O GLY A 569 ? O GLY A 569 N HIS A 538 ? N HIS A 538 
E 2 3  O ALA A 537 ? O ALA A 537 N ILE A 523 ? N ILE A 523 
E 3 4  O LEU A 524 ? O LEU A 524 N ILE A 442 ? N ILE A 442 
E 4 5  O TRP A 441 ? O TRP A 441 N ILE A 363 ? N ILE A 363 
E 5 6  O LYS A 360 ? O LYS A 360 N GLN A 324 ? N GLN A 324 
E 6 7  O HIS A 325 ? O HIS A 325 N LEU A 296 ? N LEU A 296 
E 7 8  N HIS A 295 ? N HIS A 295 O SER A 597 ? O SER A 597 
E 8 9  O ARG A 598 ? O ARG A 598 N ILE A 572 ? N ILE A 572 
F 1 2  N ILE A 369 ? N ILE A 369 O VAL A 411 ? O VAL A 411 
F 2 3  O THR A 410 ? O THR A 410 N GLY A 403 ? N GLY A 403 
G 1 2  N GLN A 488 ? N GLN A 488 O GLY A 491 ? O GLY A 491 
H 1 2  N ARG A 653 ? N ARG A 653 O LEU A 673 ? O LEU A 673 
H 2 3  N PHE A 672 ? N PHE A 672 O ILE A 680 ? O ILE A 680 
H 3 4  N THR A 681 ? N THR A 681 O GLY A 726 ? O GLY A 726 
H 4 5  O LEU A 729 ? O LEU A 729 N TYR A 701 ? N TYR A 701 
I 1 2  N VAL A 691 ? N VAL A 691 O MET A 718 ? O MET A 718 
J 1 2  N SER A 825 ? N SER A 825 O ALA A 869 ? O ALA A 869 
J 2 3  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
J 3 4  O ASN A 799 ? O ASN A 799 N GLU A 788 ? N GLU A 788 
J 4 5  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
J 5 6  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
J 6 7  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
J 7 8  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
J 8 9  N ILE A 816 ? N ILE A 816 O ILE A 853 ? O ILE A 853 
J 9 10 O THR A 854 ? O THR A 854 N THR A 841 ? N THR A 841 
K 1 2  N SER A 825 ? N SER A 825 O ALA A 869 ? O ALA A 869 
K 2 3  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
K 3 4  O ASN A 799 ? O ASN A 799 N GLU A 788 ? N GLU A 788 
K 4 5  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
K 5 6  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
K 6 7  N PHE A 735 ? N PHE A 735 O ILE A 755 ? O ILE A 755 
K 7 8  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
K 8 9  N PHE A 813 ? N PHE A 813 O LEU A 858 ? O LEU A 858 
# 
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 ? ? ? ? 19 'BINDING SITE FOR RESIDUE ACR A 1001' 
AC2 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG A 2001' 
AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG X 2003' 
AC4 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG X 2004' 
AC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 2005' 
AC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 A 4001' 
AC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3001' 
AC8 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE GOL A 3002' 
AC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3003' 
BC1 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE GOL A 3004' 
BC2 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE GOL A 3005' 
BC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL A 3006' 
BC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3007' 
BC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE GOL A 3008' 
BC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3009' 
# 
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 19 ASP A 203 ? ASP A 203  . ? 1_555 ? 
2   AC1 19 THR A 205 ? THR A 205  . ? 1_555 ? 
3   AC1 19 ASN A 207 ? ASN A 207  . ? 1_555 ? 
4   AC1 19 TYR A 299 ? TYR A 299  . ? 1_555 ? 
5   AC1 19 ASP A 327 ? ASP A 327  . ? 1_555 ? 
6   AC1 19 ILE A 328 ? ILE A 328  . ? 1_555 ? 
7   AC1 19 ILE A 364 ? ILE A 364  . ? 1_555 ? 
8   AC1 19 TRP A 441 ? TRP A 441  . ? 1_555 ? 
9   AC1 19 ASP A 443 ? ASP A 443  . ? 1_555 ? 
10  AC1 19 MET A 444 ? MET A 444  . ? 1_555 ? 
11  AC1 19 ARG A 526 ? ARG A 526  . ? 1_555 ? 
12  AC1 19 TRP A 539 ? TRP A 539  . ? 1_555 ? 
13  AC1 19 ASP A 542 ? ASP A 542  . ? 1_555 ? 
14  AC1 19 HIS A 600 ? HIS A 600  . ? 1_555 ? 
15  AC1 19 HOH Q .   ? HOH A 4081 . ? 1_555 ? 
16  AC1 19 HOH Q .   ? HOH A 4623 . ? 1_555 ? 
17  AC1 19 HOH Q .   ? HOH A 4625 . ? 1_555 ? 
18  AC1 19 HOH Q .   ? HOH A 4626 . ? 1_555 ? 
19  AC1 19 HOH Q .   ? HOH A 4627 . ? 1_555 ? 
20  AC2 9  SER A 146 ? SER A 146  . ? 3_444 ? 
21  AC2 9  ASN A 147 ? ASN A 147  . ? 3_444 ? 
22  AC2 9  ASN A 148 ? ASN A 148  . ? 3_444 ? 
23  AC2 9  GLN A 318 ? GLN A 318  . ? 1_555 ? 
24  AC2 9  PRO A 740 ? PRO A 740  . ? 1_555 ? 
25  AC2 9  ASN A 741 ? ASN A 741  . ? 1_555 ? 
26  AC2 9  THR A 742 ? THR A 742  . ? 1_555 ? 
27  AC2 9  ALA A 746 ? ALA A 746  . ? 1_555 ? 
28  AC2 9  ASN A 750 ? ASN A 750  . ? 1_555 ? 
29  AC3 10 LYS A 389 ? LYS A 389  . ? 1_555 ? 
30  AC3 10 ASN A 393 ? ASN A 393  . ? 1_555 ? 
31  AC3 10 GLY A 397 ? GLY A 397  . ? 1_555 ? 
32  AC3 10 VAL A 398 ? VAL A 398  . ? 1_555 ? 
33  AC3 10 VAL A 487 ? VAL A 487  . ? 1_555 ? 
34  AC3 10 GLN A 488 ? GLN A 488  . ? 1_555 ? 
35  AC3 10 HIS A 489 ? HIS A 489  . ? 1_555 ? 
36  AC3 10 HOH Q .   ? HOH A 4141 . ? 1_555 ? 
37  AC3 10 HOH Q .   ? HOH A 4622 . ? 1_555 ? 
38  AC3 10 NAG P .   ? NAG X 2004 . ? 1_555 ? 
39  AC4 3  LYS A 389 ? LYS A 389  . ? 1_555 ? 
40  AC4 3  HOH Q .   ? HOH A 4518 . ? 1_555 ? 
41  AC4 3  NAG O .   ? NAG X 2003 . ? 1_555 ? 
42  AC5 3  ASN A 207 ? ASN A 207  . ? 1_555 ? 
43  AC5 3  GLY A 208 ? GLY A 208  . ? 1_555 ? 
44  AC5 3  ASN A 209 ? ASN A 209  . ? 1_555 ? 
45  AC6 6  SER A 126 ? SER A 126  . ? 1_555 ? 
46  AC6 6  HIS A 625 ? HIS A 625  . ? 3_454 ? 
47  AC6 6  ASN A 628 ? ASN A 628  . ? 3_454 ? 
48  AC6 6  HOH Q .   ? HOH A 4143 . ? 3_454 ? 
49  AC6 6  HOH Q .   ? HOH A 4151 . ? 3_454 ? 
50  AC6 6  HOH Q .   ? HOH A 4486 . ? 1_555 ? 
51  AC7 5  ARG A 96  ? ARG A 96   . ? 1_555 ? 
52  AC7 5  GLN A 117 ? GLN A 117  . ? 1_555 ? 
53  AC7 5  PHE A 119 ? PHE A 119  . ? 1_555 ? 
54  AC7 5  HOH Q .   ? HOH A 4167 . ? 1_555 ? 
55  AC7 5  HOH Q .   ? HOH A 4352 . ? 1_555 ? 
56  AC8 6  ALA A 285 ? ALA A 285  . ? 1_555 ? 
57  AC8 6  ALA A 536 ? ALA A 536  . ? 1_555 ? 
58  AC8 6  ALA A 537 ? ALA A 537  . ? 1_555 ? 
59  AC8 6  HOH Q .   ? HOH A 4009 . ? 1_555 ? 
60  AC8 6  HOH Q .   ? HOH A 4211 . ? 1_555 ? 
61  AC8 6  HOH Q .   ? HOH A 4621 . ? 1_555 ? 
62  AC9 5  ASN A 306 ? ASN A 306  . ? 1_555 ? 
63  AC9 5  GLU A 309 ? GLU A 309  . ? 1_555 ? 
64  AC9 5  ARG A 313 ? ARG A 313  . ? 1_555 ? 
65  AC9 5  ASP A 607 ? ASP A 607  . ? 1_555 ? 
66  AC9 5  HOH Q .   ? HOH A 4061 . ? 1_555 ? 
67  BC1 8  LEU A 286 ? LEU A 286  . ? 1_555 ? 
68  BC1 8  ARG A 520 ? ARG A 520  . ? 1_555 ? 
69  BC1 8  HIS A 645 ? HIS A 645  . ? 1_555 ? 
70  BC1 8  ASP A 777 ? ASP A 777  . ? 1_555 ? 
71  BC1 8  THR A 778 ? THR A 778  . ? 1_555 ? 
72  BC1 8  VAL A 779 ? VAL A 779  . ? 1_555 ? 
73  BC1 8  ALA A 780 ? ALA A 780  . ? 1_555 ? 
74  BC1 8  HOH Q .   ? HOH A 4169 . ? 1_555 ? 
75  BC2 8  TRP A 290 ? TRP A 290  . ? 1_555 ? 
76  BC2 8  LYS A 360 ? LYS A 360  . ? 1_555 ? 
77  BC2 8  ASP A 438 ? ASP A 438  . ? 1_555 ? 
78  BC2 8  PHE A 516 ? PHE A 516  . ? 1_555 ? 
79  BC2 8  SER A 521 ? SER A 521  . ? 1_555 ? 
80  BC2 8  GLU A 774 ? GLU A 774  . ? 1_555 ? 
81  BC2 8  HOH Q .   ? HOH A 4069 . ? 1_555 ? 
82  BC2 8  HOH Q .   ? HOH A 4322 . ? 1_555 ? 
83  BC3 7  PHE A 65  ? PHE A 65   . ? 1_555 ? 
84  BC3 7  VAL A 131 ? VAL A 131  . ? 1_555 ? 
85  BC3 7  GLU A 132 ? GLU A 132  . ? 1_555 ? 
86  BC3 7  ILE A 133 ? ILE A 133  . ? 1_555 ? 
87  BC3 7  THR A 843 ? THR A 843  . ? 3_454 ? 
88  BC3 7  THR A 854 ? THR A 854  . ? 3_454 ? 
89  BC3 7  HOH Q .   ? HOH A 4174 . ? 3_454 ? 
90  BC4 4  GLU A 582 ? GLU A 582  . ? 1_555 ? 
91  BC4 4  ARG A 585 ? ARG A 585  . ? 1_555 ? 
92  BC4 4  GLU A 689 ? GLU A 689  . ? 1_555 ? 
93  BC4 4  GLY A 722 ? GLY A 722  . ? 1_555 ? 
94  BC5 7  TYR A 626 ? TYR A 626  . ? 1_555 ? 
95  BC5 7  ASP A 702 ? ASP A 702  . ? 1_555 ? 
96  BC5 7  TYR A 703 ? TYR A 703  . ? 1_555 ? 
97  BC5 7  GLU A 704 ? GLU A 704  . ? 1_555 ? 
98  BC5 7  ILE A 725 ? ILE A 725  . ? 1_555 ? 
99  BC5 7  GLY A 726 ? GLY A 726  . ? 1_555 ? 
100 BC5 7  LEU A 727 ? LEU A 727  . ? 1_555 ? 
101 BC6 4  GLU A 689 ? GLU A 689  . ? 1_555 ? 
102 BC6 4  GLY A 722 ? GLY A 722  . ? 1_555 ? 
103 BC6 4  HOH Q .   ? HOH A 4517 . ? 1_555 ? 
104 BC6 4  HOH Q .   ? HOH A 4542 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2QMJ 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2QMJ 
_atom_sites.fract_transf_matrix[1][1]   0.011498 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009144 
_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]   0.009152 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . VAL A 1 7   ? -33.555 35.392  9.718   1.00 45.90  ? 7    VAL A N   1 
ATOM   2    C CA  . VAL A 1 7   ? -34.363 34.832  8.589   1.00 44.85  ? 7    VAL A CA  1 
ATOM   3    C C   . VAL A 1 7   ? -35.327 33.727  9.040   1.00 43.39  ? 7    VAL A C   1 
ATOM   4    O O   . VAL A 1 7   ? -35.067 33.042  10.038  1.00 44.40  ? 7    VAL A O   1 
ATOM   5    C CB  . VAL A 1 7   ? -33.446 34.240  7.468   1.00 45.19  ? 7    VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 7   ? -32.987 35.340  6.491   1.00 47.06  ? 7    VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 7   ? -32.259 33.499  8.060   1.00 45.60  ? 7    VAL A CG2 1 
ATOM   8    N N   . ASN A 1 8   ? -36.432 33.575  8.303   1.00 40.85  ? 8    ASN A N   1 
ATOM   9    C CA  . ASN A 1 8   ? -37.230 32.347  8.284   1.00 37.30  ? 8    ASN A CA  1 
ATOM   10   C C   . ASN A 1 8   ? -36.279 31.158  8.396   1.00 34.77  ? 8    ASN A C   1 
ATOM   11   O O   . ASN A 1 8   ? -35.303 31.070  7.652   1.00 33.35  ? 8    ASN A O   1 
ATOM   12   C CB  . ASN A 1 8   ? -38.006 32.286  6.970   1.00 38.31  ? 8    ASN A CB  1 
ATOM   13   C CG  . ASN A 1 8   ? -38.936 31.068  6.871   1.00 40.46  ? 8    ASN A CG  1 
ATOM   14   O OD1 . ASN A 1 8   ? -38.489 29.934  6.805   1.00 40.02  ? 8    ASN A OD1 1 
ATOM   15   N ND2 . ASN A 1 8   ? -40.246 31.317  6.848   1.00 46.13  ? 8    ASN A ND2 1 
ATOM   16   N N   . GLU A 1 9   ? -36.534 30.258  9.338   1.00 32.23  ? 9    GLU A N   1 
ATOM   17   C CA  . GLU A 1 9   ? -35.607 29.158  9.562   1.00 31.17  ? 9    GLU A CA  1 
ATOM   18   C C   . GLU A 1 9   ? -35.413 28.213  8.362   1.00 28.06  ? 9    GLU A C   1 
ATOM   19   O O   . GLU A 1 9   ? -34.342 27.623  8.211   1.00 26.66  ? 9    GLU A O   1 
ATOM   20   C CB  . GLU A 1 9   ? -35.929 28.397  10.860  1.00 32.05  ? 9    GLU A CB  1 
ATOM   21   C CG  . GLU A 1 9   ? -37.280 27.723  10.936  1.00 33.85  ? 9    GLU A CG  1 
ATOM   22   C CD  . GLU A 1 9   ? -37.509 27.070  12.306  1.00 35.83  ? 9    GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 9   ? -37.419 27.768  13.353  1.00 42.04  ? 9    GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 9   ? -37.779 25.840  12.343  1.00 44.06  ? 9    GLU A OE2 1 
ATOM   25   N N   . LEU A 1 10  ? -36.417 28.092  7.489   1.00 24.70  ? 10   LEU A N   1 
ATOM   26   C CA  . LEU A 1 10  ? -36.288 27.220  6.308   1.00 23.22  ? 10   LEU A CA  1 
ATOM   27   C C   . LEU A 1 10  ? -35.288 27.783  5.308   1.00 21.73  ? 10   LEU A C   1 
ATOM   28   O O   . LEU A 1 10  ? -34.803 27.058  4.431   1.00 21.53  ? 10   LEU A O   1 
ATOM   29   C CB  . LEU A 1 10  ? -37.640 27.010  5.609   1.00 22.64  ? 10   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 10  ? -38.777 26.443  6.454   1.00 23.95  ? 10   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 10  ? -40.014 26.207  5.571   1.00 26.10  ? 10   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 10  ? -38.374 25.155  7.175   1.00 23.96  ? 10   LEU A CD2 1 
ATOM   33   N N   . GLU A 1 11  ? -34.978 29.071  5.445   1.00 20.47  ? 11   GLU A N   1 
ATOM   34   C CA  . GLU A 1 11  ? -34.047 29.746  4.540   1.00 21.54  ? 11   GLU A CA  1 
ATOM   35   C C   . GLU A 1 11  ? -32.623 29.808  5.082   1.00 20.15  ? 11   GLU A C   1 
ATOM   36   O O   . GLU A 1 11  ? -31.733 30.358  4.420   1.00 19.05  ? 11   GLU A O   1 
ATOM   37   C CB  . GLU A 1 11  ? -34.507 31.143  4.182   1.00 21.41  ? 11   GLU A CB  1 
ATOM   38   C CG  . GLU A 1 11  ? -35.832 31.156  3.371   1.00 25.94  ? 11   GLU A CG  1 
ATOM   39   C CD  . GLU A 1 11  ? -36.392 32.559  3.109   1.00 28.25  ? 11   GLU A CD  1 
ATOM   40   O OE1 . GLU A 1 11  ? -35.638 33.567  3.183   1.00 36.76  ? 11   GLU A OE1 1 
ATOM   41   O OE2 . GLU A 1 11  ? -37.628 32.643  2.822   1.00 36.78  ? 11   GLU A OE2 1 
ATOM   42   N N   . ARG A 1 12  ? -32.402 29.248  6.267   1.00 19.18  ? 12   ARG A N   1 
ATOM   43   C CA  . ARG A 1 12  ? -31.025 29.281  6.816   1.00 19.60  ? 12   ARG A CA  1 
ATOM   44   C C   . ARG A 1 12  ? -30.078 28.384  6.047   1.00 18.72  ? 12   ARG A C   1 
ATOM   45   O O   . ARG A 1 12  ? -30.403 27.235  5.771   1.00 19.34  ? 12   ARG A O   1 
ATOM   46   C CB  . ARG A 1 12  ? -31.028 28.876  8.273   1.00 19.78  ? 12   ARG A CB  1 
ATOM   47   C CG  . ARG A 1 12  ? -31.658 29.919  9.146   1.00 23.73  ? 12   ARG A CG  1 
ATOM   48   C CD  . ARG A 1 12  ? -31.897 29.291  10.474  1.00 28.27  ? 12   ARG A CD  1 
ATOM   49   N NE  . ARG A 1 12  ? -32.759 30.077  11.329  1.00 33.50  ? 12   ARG A NE  1 
ATOM   50   C CZ  . ARG A 1 12  ? -32.887 29.847  12.635  1.00 36.79  ? 12   ARG A CZ  1 
ATOM   51   N NH1 . ARG A 1 12  ? -32.179 28.881  13.241  1.00 37.33  ? 12   ARG A NH1 1 
ATOM   52   N NH2 . ARG A 1 12  ? -33.721 30.591  13.327  1.00 38.58  ? 12   ARG A NH2 1 
ATOM   53   N N   . ILE A 1 13  ? -28.892 28.890  5.742   1.00 17.60  ? 13   ILE A N   1 
ATOM   54   C CA  . ILE A 1 13  ? -27.919 28.146  4.951   1.00 17.21  ? 13   ILE A CA  1 
ATOM   55   C C   . ILE A 1 13  ? -26.823 27.755  5.949   1.00 17.38  ? 13   ILE A C   1 
ATOM   56   O O   . ILE A 1 13  ? -26.250 28.617  6.595   1.00 16.09  ? 13   ILE A O   1 
ATOM   57   C CB  . ILE A 1 13  ? -27.342 29.011  3.830   1.00 17.07  ? 13   ILE A CB  1 
ATOM   58   C CG1 . ILE A 1 13  ? -28.450 29.438  2.860   1.00 17.02  ? 13   ILE A CG1 1 
ATOM   59   C CG2 . ILE A 1 13  ? -26.295 28.263  3.007   1.00 16.78  ? 13   ILE A CG2 1 
ATOM   60   C CD1 . ILE A 1 13  ? -29.098 28.266  2.097   1.00 16.52  ? 13   ILE A CD1 1 
ATOM   61   N N   . ASN A 1 14  ? -26.592 26.458  6.076   1.00 16.54  ? 14   ASN A N   1 
ATOM   62   C CA  . ASN A 1 14  ? -25.848 25.896  7.173   1.00 16.34  ? 14   ASN A CA  1 
ATOM   63   C C   . ASN A 1 14  ? -24.382 26.316  7.012   1.00 16.18  ? 14   ASN A C   1 
ATOM   64   O O   . ASN A 1 14  ? -23.796 26.097  5.968   1.00 15.44  ? 14   ASN A O   1 
ATOM   65   C CB  . ASN A 1 14  ? -26.000 24.383  7.124   1.00 16.42  ? 14   ASN A CB  1 
ATOM   66   C CG  . ASN A 1 14  ? -25.188 23.651  8.226   1.00 19.16  ? 14   ASN A CG  1 
ATOM   67   O OD1 . ASN A 1 14  ? -24.659 24.268  9.148   1.00 18.97  ? 14   ASN A OD1 1 
ATOM   68   N ND2 . ASN A 1 14  ? -25.070 22.336  8.088   1.00 20.07  ? 14   ASN A ND2 1 
ATOM   69   N N   . CYS A 1 15  ? -23.832 26.931  8.059   1.00 18.20  ? 15   CYS A N   1 
ATOM   70   C CA  . CYS A 1 15  ? -22.444 27.418  8.111   1.00 19.29  ? 15   CYS A CA  1 
ATOM   71   C C   . CYS A 1 15  ? -21.483 26.380  8.738   1.00 19.06  ? 15   CYS A C   1 
ATOM   72   O O   . CYS A 1 15  ? -20.232 26.560  8.768   1.00 18.26  ? 15   CYS A O   1 
ATOM   73   C CB  . CYS A 1 15  ? -22.435 28.749  8.933   1.00 20.41  ? 15   CYS A CB  1 
ATOM   74   S SG  . CYS A 1 15  ? -20.788 29.412  9.270   1.00 24.87  ? 15   CYS A SG  1 
ATOM   75   N N   . ILE A 1 16  ? -22.061 25.307  9.268   1.00 18.34  ? 16   ILE A N   1 
ATOM   76   C CA  . ILE A 1 16  ? -21.244 24.255  9.878   1.00 18.84  ? 16   ILE A CA  1 
ATOM   77   C C   . ILE A 1 16  ? -21.647 22.908  9.266   1.00 20.06  ? 16   ILE A C   1 
ATOM   78   O O   . ILE A 1 16  ? -22.297 22.089  9.918   1.00 20.28  ? 16   ILE A O   1 
ATOM   79   C CB  . ILE A 1 16  ? -21.298 24.229  11.428  1.00 17.91  ? 16   ILE A CB  1 
ATOM   80   C CG1 . ILE A 1 16  ? -20.879 25.555  12.033  1.00 16.77  ? 16   ILE A CG1 1 
ATOM   81   C CG2 . ILE A 1 16  ? -20.316 23.188  11.977  1.00 19.32  ? 16   ILE A CG2 1 
ATOM   82   C CD1 . ILE A 1 16  ? -21.068 25.611  13.567  1.00 17.43  ? 16   ILE A CD1 1 
ATOM   83   N N   . PRO A 1 17  ? -21.261 22.687  8.005   1.00 20.86  ? 17   PRO A N   1 
ATOM   84   C CA  . PRO A 1 17  ? -21.585 21.439  7.329   1.00 22.52  ? 17   PRO A CA  1 
ATOM   85   C C   . PRO A 1 17  ? -20.701 20.257  7.758   1.00 24.30  ? 17   PRO A C   1 
ATOM   86   O O   . PRO A 1 17  ? -21.044 19.106  7.453   1.00 25.28  ? 17   PRO A O   1 
ATOM   87   C CB  . PRO A 1 17  ? -21.293 21.785  5.872   1.00 22.29  ? 17   PRO A CB  1 
ATOM   88   C CG  . PRO A 1 17  ? -20.109 22.717  5.964   1.00 23.16  ? 17   PRO A CG  1 
ATOM   89   C CD  . PRO A 1 17  ? -20.504 23.595  7.122   1.00 21.65  ? 17   PRO A CD  1 
ATOM   90   N N   . ASP A 1 18  ? -19.602 20.547  8.469   1.00 24.03  ? 18   ASP A N   1 
ATOM   91   C CA  . ASP A 1 18  ? -18.467 19.640  8.639   1.00 26.04  ? 18   ASP A CA  1 
ATOM   92   C C   . ASP A 1 18  ? -18.344 19.001  10.018  1.00 27.51  ? 18   ASP A C   1 
ATOM   93   O O   . ASP A 1 18  ? -17.422 18.190  10.237  1.00 28.11  ? 18   ASP A O   1 
ATOM   94   C CB  . ASP A 1 18  ? -17.159 20.390  8.378   1.00 25.44  ? 18   ASP A CB  1 
ATOM   95   C CG  . ASP A 1 18  ? -17.049 21.722  9.173   1.00 27.45  ? 18   ASP A CG  1 
ATOM   96   O OD1 . ASP A 1 18  ? -18.056 22.455  9.295   1.00 23.39  ? 18   ASP A OD1 1 
ATOM   97   O OD2 . ASP A 1 18  ? -15.927 22.067  9.666   1.00 27.19  ? 18   ASP A OD2 1 
ATOM   98   N N   . GLN A 1 19  ? -19.203 19.408  10.953  1.00 27.82  ? 19   GLN A N   1 
ATOM   99   C CA  . GLN A 1 19  ? -19.101 18.967  12.353  1.00 29.07  ? 19   GLN A CA  1 
ATOM   100  C C   . GLN A 1 19  ? -20.396 19.219  13.121  1.00 29.45  ? 19   GLN A C   1 
ATOM   101  O O   . GLN A 1 19  ? -21.274 19.909  12.607  1.00 28.99  ? 19   GLN A O   1 
ATOM   102  C CB  . GLN A 1 19  ? -17.892 19.634  13.031  1.00 29.62  ? 19   GLN A CB  1 
ATOM   103  C CG  . GLN A 1 19  ? -18.008 21.092  13.255  1.00 29.55  ? 19   GLN A CG  1 
ATOM   104  C CD  . GLN A 1 19  ? -16.666 21.744  13.519  1.00 32.70  ? 19   GLN A CD  1 
ATOM   105  O OE1 . GLN A 1 19  ? -15.647 21.378  12.937  1.00 37.04  ? 19   GLN A OE1 1 
ATOM   106  N NE2 . GLN A 1 19  ? -16.663 22.729  14.388  1.00 31.45  ? 19   GLN A NE2 1 
ATOM   107  N N   . PRO A 1 20  ? -20.555 18.622  14.342  1.00 29.83  ? 20   PRO A N   1 
ATOM   108  C CA  . PRO A 1 20  ? -21.754 19.020  15.116  1.00 29.50  ? 20   PRO A CA  1 
ATOM   109  C C   . PRO A 1 20  ? -21.661 20.512  15.500  1.00 27.88  ? 20   PRO A C   1 
ATOM   110  O O   . PRO A 1 20  ? -20.588 20.941  15.912  1.00 28.61  ? 20   PRO A O   1 
ATOM   111  C CB  . PRO A 1 20  ? -21.708 18.119  16.364  1.00 29.05  ? 20   PRO A CB  1 
ATOM   112  C CG  . PRO A 1 20  ? -20.242 17.661  16.473  1.00 30.37  ? 20   PRO A CG  1 
ATOM   113  C CD  . PRO A 1 20  ? -19.746 17.589  15.038  1.00 30.41  ? 20   PRO A CD  1 
ATOM   114  N N   . PRO A 1 21  ? -22.757 21.277  15.347  1.00 27.16  ? 21   PRO A N   1 
ATOM   115  C CA  . PRO A 1 21  ? -22.751 22.751  15.473  1.00 26.17  ? 21   PRO A CA  1 
ATOM   116  C C   . PRO A 1 21  ? -22.415 23.200  16.903  1.00 25.57  ? 21   PRO A C   1 
ATOM   117  O O   . PRO A 1 21  ? -23.004 22.699  17.868  1.00 25.53  ? 21   PRO A O   1 
ATOM   118  C CB  . PRO A 1 21  ? -24.191 23.160  15.097  1.00 25.97  ? 21   PRO A CB  1 
ATOM   119  C CG  . PRO A 1 21  ? -25.003 21.956  15.355  1.00 27.08  ? 21   PRO A CG  1 
ATOM   120  C CD  . PRO A 1 21  ? -24.106 20.765  15.040  1.00 27.31  ? 21   PRO A CD  1 
ATOM   121  N N   . THR A 1 22  ? -21.454 24.111  17.042  1.00 24.31  ? 22   THR A N   1 
ATOM   122  C CA  . THR A 1 22  ? -21.198 24.714  18.335  1.00 23.35  ? 22   THR A CA  1 
ATOM   123  C C   . THR A 1 22  ? -21.225 26.242  18.204  1.00 23.23  ? 22   THR A C   1 
ATOM   124  O O   . THR A 1 22  ? -20.873 26.777  17.159  1.00 23.32  ? 22   THR A O   1 
ATOM   125  C CB  . THR A 1 22  ? -19.835 24.242  18.932  1.00 23.14  ? 22   THR A CB  1 
ATOM   126  O OG1 . THR A 1 22  ? -18.768 24.657  18.095  1.00 24.85  ? 22   THR A OG1 1 
ATOM   127  C CG2 . THR A 1 22  ? -19.760 22.723  19.045  1.00 22.92  ? 22   THR A CG2 1 
ATOM   128  N N   . LYS A 1 23  ? -21.610 26.932  19.264  1.00 23.55  ? 23   LYS A N   1 
ATOM   129  C CA  . LYS A 1 23  ? -21.518 28.388  19.275  1.00 24.57  ? 23   LYS A CA  1 
ATOM   130  C C   . LYS A 1 23  ? -20.070 28.832  19.072  1.00 23.85  ? 23   LYS A C   1 
ATOM   131  O O   . LYS A 1 23  ? -19.829 29.813  18.382  1.00 23.01  ? 23   LYS A O   1 
ATOM   132  C CB  . LYS A 1 23  ? -22.112 29.002  20.558  1.00 25.65  ? 23   LYS A CB  1 
ATOM   133  C CG  . LYS A 1 23  ? -22.264 30.545  20.470  1.00 27.20  ? 23   LYS A CG  1 
ATOM   134  C CD  . LYS A 1 23  ? -22.687 31.198  21.784  1.00 28.16  ? 23   LYS A CD  1 
ATOM   135  C CE  . LYS A 1 23  ? -23.101 32.695  21.563  1.00 31.00  ? 23   LYS A CE  1 
ATOM   136  N NZ  . LYS A 1 23  ? -22.057 33.561  20.899  1.00 33.62  ? 23   LYS A NZ  1 
ATOM   137  N N   . ALA A 1 24  ? -19.093 28.124  19.640  1.00 23.50  ? 24   ALA A N   1 
ATOM   138  C CA  . ALA A 1 24  ? -17.711 28.550  19.504  1.00 24.06  ? 24   ALA A CA  1 
ATOM   139  C C   . ALA A 1 24  ? -17.272 28.567  18.039  1.00 24.48  ? 24   ALA A C   1 
ATOM   140  O O   . ALA A 1 24  ? -16.683 29.552  17.561  1.00 25.38  ? 24   ALA A O   1 
ATOM   141  C CB  . ALA A 1 24  ? -16.758 27.665  20.362  1.00 25.09  ? 24   ALA A CB  1 
ATOM   142  N N   . THR A 1 25  ? -17.561 27.491  17.305  1.00 23.35  ? 25   THR A N   1 
ATOM   143  C CA  . THR A 1 25  ? -17.232 27.459  15.875  1.00 23.74  ? 25   THR A CA  1 
ATOM   144  C C   . THR A 1 25  ? -18.058 28.509  15.109  1.00 22.99  ? 25   THR A C   1 
ATOM   145  O O   . THR A 1 25  ? -17.549 29.172  14.229  1.00 22.31  ? 25   THR A O   1 
ATOM   146  C CB  . THR A 1 25  ? -17.457 26.065  15.282  1.00 23.53  ? 25   THR A CB  1 
ATOM   147  O OG1 . THR A 1 25  ? -16.501 25.161  15.844  1.00 26.26  ? 25   THR A OG1 1 
ATOM   148  C CG2 . THR A 1 25  ? -17.267 26.054  13.762  1.00 22.56  ? 25   THR A CG2 1 
ATOM   149  N N   . CYS A 1 26  ? -19.325 28.646  15.466  1.00 24.40  ? 26   CYS A N   1 
ATOM   150  C CA  . CYS A 1 26  ? -20.188 29.628  14.820  1.00 24.80  ? 26   CYS A CA  1 
ATOM   151  C C   . CYS A 1 26  ? -19.580 31.032  14.925  1.00 25.10  ? 26   CYS A C   1 
ATOM   152  O O   . CYS A 1 26  ? -19.404 31.737  13.908  1.00 24.09  ? 26   CYS A O   1 
ATOM   153  C CB  . CYS A 1 26  ? -21.558 29.572  15.468  1.00 25.46  ? 26   CYS A CB  1 
ATOM   154  S SG  . CYS A 1 26  ? -22.736 30.662  14.641  1.00 30.48  ? 26   CYS A SG  1 
ATOM   155  N N   . ASP A 1 27  ? -19.191 31.411  16.148  1.00 25.36  ? 27   ASP A N   1 
ATOM   156  C CA  . ASP A 1 27  ? -18.568 32.726  16.400  1.00 26.02  ? 27   ASP A CA  1 
ATOM   157  C C   . ASP A 1 27  ? -17.270 32.905  15.619  1.00 26.54  ? 27   ASP A C   1 
ATOM   158  O O   . ASP A 1 27  ? -17.071 33.946  14.998  1.00 27.52  ? 27   ASP A O   1 
ATOM   159  C CB  . ASP A 1 27  ? -18.309 32.936  17.888  1.00 25.86  ? 27   ASP A CB  1 
ATOM   160  C CG  . ASP A 1 27  ? -19.591 33.106  18.702  1.00 29.03  ? 27   ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 27  ? -20.692 33.305  18.142  1.00 28.47  ? 27   ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 27  ? -19.507 33.022  19.940  1.00 34.17  ? 27   ASP A OD2 1 
ATOM   163  N N   . GLN A 1 28  ? -16.387 31.906  15.630  1.00 26.27  ? 28   GLN A N   1 
ATOM   164  C CA  . GLN A 1 28  ? -15.121 31.993  14.865  1.00 26.01  ? 28   GLN A CA  1 
ATOM   165  C C   . GLN A 1 28  ? -15.357 32.211  13.364  1.00 25.62  ? 28   GLN A C   1 
ATOM   166  O O   . GLN A 1 28  ? -14.553 32.859  12.671  1.00 24.40  ? 28   GLN A O   1 
ATOM   167  C CB  . GLN A 1 28  ? -14.247 30.730  15.097  1.00 26.66  ? 28   GLN A CB  1 
ATOM   168  C CG  . GLN A 1 28  ? -12.970 30.644  14.218  1.00 28.56  ? 28   GLN A CG  1 
ATOM   169  C CD  . GLN A 1 28  ? -11.927 31.734  14.551  1.00 35.58  ? 28   GLN A CD  1 
ATOM   170  O OE1 . GLN A 1 28  ? -12.023 32.409  15.587  1.00 39.16  ? 28   GLN A OE1 1 
ATOM   171  N NE2 . GLN A 1 28  ? -10.929 31.900  13.678  1.00 34.31  ? 28   GLN A NE2 1 
ATOM   172  N N   . ARG A 1 29  ? -16.471 31.680  12.865  1.00 24.85  ? 29   ARG A N   1 
ATOM   173  C CA  . ARG A 1 29  ? -16.736 31.727  11.433  1.00 24.70  ? 29   ARG A CA  1 
ATOM   174  C C   . ARG A 1 29  ? -17.545 32.966  11.046  1.00 24.94  ? 29   ARG A C   1 
ATOM   175  O O   . ARG A 1 29  ? -17.774 33.222  9.858   1.00 24.08  ? 29   ARG A O   1 
ATOM   176  C CB  . ARG A 1 29  ? -17.451 30.442  10.997  1.00 24.98  ? 29   ARG A CB  1 
ATOM   177  C CG  . ARG A 1 29  ? -16.613 29.216  11.130  1.00 24.61  ? 29   ARG A CG  1 
ATOM   178  C CD  . ARG A 1 29  ? -17.268 27.994  10.513  1.00 26.80  ? 29   ARG A CD  1 
ATOM   179  N NE  . ARG A 1 29  ? -16.344 26.887  10.703  1.00 26.40  ? 29   ARG A NE  1 
ATOM   180  C CZ  . ARG A 1 29  ? -16.579 25.634  10.378  1.00 25.07  ? 29   ARG A CZ  1 
ATOM   181  N NH1 . ARG A 1 29  ? -17.728 25.281  9.810   1.00 19.27  ? 29   ARG A NH1 1 
ATOM   182  N NH2 . ARG A 1 29  ? -15.643 24.736  10.637  1.00 24.66  ? 29   ARG A NH2 1 
ATOM   183  N N   . GLY A 1 30  ? -17.953 33.744  12.050  1.00 23.95  ? 30   GLY A N   1 
ATOM   184  C CA  . GLY A 1 30  ? -18.685 34.968  11.814  1.00 24.62  ? 30   GLY A CA  1 
ATOM   185  C C   . GLY A 1 30  ? -20.110 34.667  11.382  1.00 24.59  ? 30   GLY A C   1 
ATOM   186  O O   . GLY A 1 30  ? -20.712 35.459  10.662  1.00 25.49  ? 30   GLY A O   1 
ATOM   187  N N   . CYS A 1 31  ? -20.664 33.546  11.835  1.00 23.75  ? 31   CYS A N   1 
ATOM   188  C CA  . CYS A 1 31  ? -22.010 33.140  11.431  1.00 23.39  ? 31   CYS A CA  1 
ATOM   189  C C   . CYS A 1 31  ? -23.043 33.426  12.504  1.00 23.65  ? 31   CYS A C   1 
ATOM   190  O O   . CYS A 1 31  ? -22.720 34.006  13.537  1.00 23.00  ? 31   CYS A O   1 
ATOM   191  C CB  . CYS A 1 31  ? -22.010 31.664  11.019  1.00 23.92  ? 31   CYS A CB  1 
ATOM   192  S SG  . CYS A 1 31  ? -21.146 31.436  9.452   1.00 24.55  ? 31   CYS A SG  1 
ATOM   193  N N   . CYS A 1 32  ? -24.295 33.075  12.239  1.00 23.41  ? 32   CYS A N   1 
ATOM   194  C CA  . CYS A 1 32  ? -25.398 33.349  13.147  1.00 24.45  ? 32   CYS A CA  1 
ATOM   195  C C   . CYS A 1 32  ? -25.719 32.100  13.950  1.00 24.63  ? 32   CYS A C   1 
ATOM   196  O O   . CYS A 1 32  ? -25.688 31.002  13.399  1.00 23.10  ? 32   CYS A O   1 
ATOM   197  C CB  . CYS A 1 32  ? -26.630 33.742  12.346  1.00 24.80  ? 32   CYS A CB  1 
ATOM   198  S SG  . CYS A 1 32  ? -26.335 35.132  11.289  1.00 28.59  ? 32   CYS A SG  1 
ATOM   199  N N   . TRP A 1 33  ? -26.031 32.264  15.236  1.00 25.81  ? 33   TRP A N   1 
ATOM   200  C CA  . TRP A 1 33  ? -26.322 31.140  16.144  1.00 27.54  ? 33   TRP A CA  1 
ATOM   201  C C   . TRP A 1 33  ? -27.762 31.170  16.686  1.00 28.98  ? 33   TRP A C   1 
ATOM   202  O O   . TRP A 1 33  ? -28.152 32.128  17.341  1.00 28.50  ? 33   TRP A O   1 
ATOM   203  C CB  . TRP A 1 33  ? -25.331 31.148  17.313  1.00 28.41  ? 33   TRP A CB  1 
ATOM   204  C CG  . TRP A 1 33  ? -25.524 30.023  18.295  1.00 29.68  ? 33   TRP A CG  1 
ATOM   205  C CD1 . TRP A 1 33  ? -26.077 30.114  19.545  1.00 30.33  ? 33   TRP A CD1 1 
ATOM   206  C CD2 . TRP A 1 33  ? -25.172 28.636  18.107  1.00 29.66  ? 33   TRP A CD2 1 
ATOM   207  N NE1 . TRP A 1 33  ? -26.079 28.874  20.147  1.00 28.97  ? 33   TRP A NE1 1 
ATOM   208  C CE2 . TRP A 1 33  ? -25.536 27.950  19.289  1.00 29.80  ? 33   TRP A CE2 1 
ATOM   209  C CE3 . TRP A 1 33  ? -24.590 27.912  17.055  1.00 28.19  ? 33   TRP A CE3 1 
ATOM   210  C CZ2 . TRP A 1 33  ? -25.334 26.573  19.450  1.00 29.13  ? 33   TRP A CZ2 1 
ATOM   211  C CZ3 . TRP A 1 33  ? -24.386 26.556  17.216  1.00 29.65  ? 33   TRP A CZ3 1 
ATOM   212  C CH2 . TRP A 1 33  ? -24.763 25.895  18.412  1.00 29.92  ? 33   TRP A CH2 1 
ATOM   213  N N   . ASN A 1 34  ? -28.546 30.123  16.436  1.00 29.90  ? 34   ASN A N   1 
ATOM   214  C CA  . ASN A 1 34  ? -29.914 30.050  16.969  1.00 32.60  ? 34   ASN A CA  1 
ATOM   215  C C   . ASN A 1 34  ? -30.319 28.586  17.045  1.00 34.51  ? 34   ASN A C   1 
ATOM   216  O O   . ASN A 1 34  ? -30.874 28.047  16.088  1.00 34.13  ? 34   ASN A O   1 
ATOM   217  C CB  . ASN A 1 34  ? -30.885 30.884  16.108  1.00 32.35  ? 34   ASN A CB  1 
ATOM   218  C CG  . ASN A 1 34  ? -32.363 30.825  16.598  1.00 35.29  ? 34   ASN A CG  1 
ATOM   219  O OD1 . ASN A 1 34  ? -32.759 29.971  17.387  1.00 37.48  ? 34   ASN A OD1 1 
ATOM   220  N ND2 . ASN A 1 34  ? -33.167 31.739  16.097  1.00 35.73  ? 34   ASN A ND2 1 
ATOM   221  N N   . PRO A 1 35  ? -29.999 27.915  18.173  1.00 37.01  ? 35   PRO A N   1 
ATOM   222  C CA  . PRO A 1 35  ? -30.353 26.511  18.297  1.00 38.90  ? 35   PRO A CA  1 
ATOM   223  C C   . PRO A 1 35  ? -31.842 26.229  18.402  1.00 41.11  ? 35   PRO A C   1 
ATOM   224  O O   . PRO A 1 35  ? -32.210 25.073  18.324  1.00 42.91  ? 35   PRO A O   1 
ATOM   225  C CB  . PRO A 1 35  ? -29.655 26.063  19.600  1.00 38.34  ? 35   PRO A CB  1 
ATOM   226  C CG  . PRO A 1 35  ? -28.719 27.113  19.926  1.00 37.70  ? 35   PRO A CG  1 
ATOM   227  C CD  . PRO A 1 35  ? -29.270 28.388  19.361  1.00 37.08  ? 35   PRO A CD  1 
ATOM   228  N N   . GLN A 1 36  ? -32.699 27.232  18.539  1.00 43.15  ? 36   GLN A N   1 
ATOM   229  C CA  . GLN A 1 36  ? -34.107 26.947  18.888  1.00 45.88  ? 36   GLN A CA  1 
ATOM   230  C C   . GLN A 1 36  ? -35.013 26.481  17.723  1.00 46.72  ? 36   GLN A C   1 
ATOM   231  O O   . GLN A 1 36  ? -36.249 26.470  17.868  1.00 47.41  ? 36   GLN A O   1 
ATOM   232  C CB  . GLN A 1 36  ? -34.774 28.114  19.661  1.00 46.40  ? 36   GLN A CB  1 
ATOM   233  C CG  . GLN A 1 36  ? -33.816 29.110  20.366  1.00 49.93  ? 36   GLN A CG  1 
ATOM   234  C CD  . GLN A 1 36  ? -33.027 28.495  21.514  1.00 53.42  ? 36   GLN A CD  1 
ATOM   235  O OE1 . GLN A 1 36  ? -33.531 27.630  22.236  1.00 56.53  ? 36   GLN A OE1 1 
ATOM   236  N NE2 . GLN A 1 36  ? -31.783 28.943  21.690  1.00 53.89  ? 36   GLN A NE2 1 
ATOM   237  N N   . GLY A 1 37  ? -34.419 26.072  16.596  1.00 47.11  ? 37   GLY A N   1 
ATOM   238  C CA  . GLY A 1 37  ? -35.204 25.587  15.445  1.00 46.90  ? 37   GLY A CA  1 
ATOM   239  C C   . GLY A 1 37  ? -35.828 24.194  15.601  1.00 46.87  ? 37   GLY A C   1 
ATOM   240  O O   . GLY A 1 37  ? -35.723 23.559  16.672  1.00 47.88  ? 37   GLY A O   1 
ATOM   241  N N   . ALA A 1 38  ? -36.484 23.724  14.530  1.00 45.48  ? 38   ALA A N   1 
ATOM   242  C CA  . ALA A 1 38  ? -36.973 22.334  14.409  1.00 43.60  ? 38   ALA A CA  1 
ATOM   243  C C   . ALA A 1 38  ? -35.854 21.373  13.982  1.00 42.31  ? 38   ALA A C   1 
ATOM   244  O O   . ALA A 1 38  ? -34.745 21.814  13.661  1.00 41.54  ? 38   ALA A O   1 
ATOM   245  C CB  . ALA A 1 38  ? -38.102 22.284  13.412  1.00 43.78  ? 38   ALA A CB  1 
ATOM   246  N N   . VAL A 1 39  ? -36.141 20.069  13.957  1.00 40.06  ? 39   VAL A N   1 
ATOM   247  C CA  . VAL A 1 39  ? -35.125 19.085  13.534  1.00 38.42  ? 39   VAL A CA  1 
ATOM   248  C C   . VAL A 1 39  ? -34.482 19.449  12.174  1.00 36.22  ? 39   VAL A C   1 
ATOM   249  O O   . VAL A 1 39  ? -35.177 19.857  11.238  1.00 35.60  ? 39   VAL A O   1 
ATOM   250  C CB  . VAL A 1 39  ? -35.662 17.614  13.539  1.00 38.48  ? 39   VAL A CB  1 
ATOM   251  C CG1 . VAL A 1 39  ? -36.879 17.429  12.589  1.00 39.55  ? 39   VAL A CG1 1 
ATOM   252  C CG2 . VAL A 1 39  ? -34.533 16.627  13.226  1.00 39.05  ? 39   VAL A CG2 1 
ATOM   253  N N   . SER A 1 40  ? -33.157 19.356  12.111  1.00 33.67  ? 40   SER A N   1 
ATOM   254  C CA  . SER A 1 40  ? -32.375 19.560  10.865  1.00 32.23  ? 40   SER A CA  1 
ATOM   255  C C   . SER A 1 40  ? -32.247 21.019  10.449  1.00 30.04  ? 40   SER A C   1 
ATOM   256  O O   . SER A 1 40  ? -31.425 21.324  9.593   1.00 30.23  ? 40   SER A O   1 
ATOM   257  C CB  . SER A 1 40  ? -32.917 18.749  9.669   1.00 32.59  ? 40   SER A CB  1 
ATOM   258  O OG  . SER A 1 40  ? -33.209 17.415  10.023  1.00 33.29  ? 40   SER A OG  1 
ATOM   259  N N   . VAL A 1 41  ? -33.016 21.918  11.064  1.00 27.62  ? 41   VAL A N   1 
ATOM   260  C CA  . VAL A 1 41  ? -32.795 23.362  10.848  1.00 26.13  ? 41   VAL A CA  1 
ATOM   261  C C   . VAL A 1 41  ? -31.404 23.704  11.414  1.00 25.10  ? 41   VAL A C   1 
ATOM   262  O O   . VAL A 1 41  ? -31.126 23.399  12.580  1.00 25.31  ? 41   VAL A O   1 
ATOM   263  C CB  . VAL A 1 41  ? -33.876 24.221  11.512  1.00 26.53  ? 41   VAL A CB  1 
ATOM   264  C CG1 . VAL A 1 41  ? -33.540 25.717  11.391  1.00 25.23  ? 41   VAL A CG1 1 
ATOM   265  C CG2 . VAL A 1 41  ? -35.215 23.927  10.879  1.00 25.62  ? 41   VAL A CG2 1 
ATOM   266  N N   . PRO A 1 42  ? -30.520 24.290  10.587  1.00 23.53  ? 42   PRO A N   1 
ATOM   267  C CA  . PRO A 1 42  ? -29.151 24.511  11.048  1.00 24.03  ? 42   PRO A CA  1 
ATOM   268  C C   . PRO A 1 42  ? -29.113 25.475  12.224  1.00 24.05  ? 42   PRO A C   1 
ATOM   269  O O   . PRO A 1 42  ? -29.735 26.527  12.186  1.00 24.16  ? 42   PRO A O   1 
ATOM   270  C CB  . PRO A 1 42  ? -28.435 25.099  9.825   1.00 23.30  ? 42   PRO A CB  1 
ATOM   271  C CG  . PRO A 1 42  ? -29.462 25.503  8.909   1.00 24.91  ? 42   PRO A CG  1 
ATOM   272  C CD  . PRO A 1 42  ? -30.717 24.753  9.205   1.00 23.13  ? 42   PRO A CD  1 
ATOM   273  N N   . TRP A 1 43  ? -28.410 25.083  13.281  1.00 23.82  ? 43   TRP A N   1 
ATOM   274  C CA  . TRP A 1 43  ? -28.225 25.951  14.448  1.00 23.59  ? 43   TRP A CA  1 
ATOM   275  C C   . TRP A 1 43  ? -27.318 27.139  14.111  1.00 22.45  ? 43   TRP A C   1 
ATOM   276  O O   . TRP A 1 43  ? -27.438 28.231  14.665  1.00 22.52  ? 43   TRP A O   1 
ATOM   277  C CB  . TRP A 1 43  ? -27.612 25.119  15.576  1.00 24.97  ? 43   TRP A CB  1 
ATOM   278  C CG  . TRP A 1 43  ? -28.598 24.179  16.213  1.00 26.99  ? 43   TRP A CG  1 
ATOM   279  C CD1 . TRP A 1 43  ? -29.881 23.914  15.800  1.00 28.81  ? 43   TRP A CD1 1 
ATOM   280  C CD2 . TRP A 1 43  ? -28.374 23.368  17.370  1.00 29.14  ? 43   TRP A CD2 1 
ATOM   281  N NE1 . TRP A 1 43  ? -30.467 23.002  16.642  1.00 29.59  ? 43   TRP A NE1 1 
ATOM   282  C CE2 . TRP A 1 43  ? -29.565 22.649  17.613  1.00 29.35  ? 43   TRP A CE2 1 
ATOM   283  C CE3 . TRP A 1 43  ? -27.286 23.199  18.241  1.00 28.27  ? 43   TRP A CE3 1 
ATOM   284  C CZ2 . TRP A 1 43  ? -29.695 21.753  18.676  1.00 28.66  ? 43   TRP A CZ2 1 
ATOM   285  C CZ3 . TRP A 1 43  ? -27.406 22.299  19.293  1.00 29.08  ? 43   TRP A CZ3 1 
ATOM   286  C CH2 . TRP A 1 43  ? -28.613 21.595  19.509  1.00 29.56  ? 43   TRP A CH2 1 
ATOM   287  N N   . CYS A 1 44  ? -26.410 26.903  13.184  1.00 21.57  ? 44   CYS A N   1 
ATOM   288  C CA  . CYS A 1 44  ? -25.468 27.916  12.764  1.00 21.24  ? 44   CYS A CA  1 
ATOM   289  C C   . CYS A 1 44  ? -25.602 28.132  11.259  1.00 20.57  ? 44   CYS A C   1 
ATOM   290  O O   . CYS A 1 44  ? -25.411 27.200  10.461  1.00 19.52  ? 44   CYS A O   1 
ATOM   291  C CB  . CYS A 1 44  ? -24.054 27.487  13.121  1.00 20.20  ? 44   CYS A CB  1 
ATOM   292  S SG  . CYS A 1 44  ? -22.745 28.617  12.562  1.00 24.56  ? 44   CYS A SG  1 
ATOM   293  N N   . TYR A 1 45  ? -25.890 29.366  10.876  1.00 20.96  ? 45   TYR A N   1 
ATOM   294  C CA  . TYR A 1 45  ? -26.178 29.673  9.479   1.00 21.78  ? 45   TYR A CA  1 
ATOM   295  C C   . TYR A 1 45  ? -25.550 30.986  9.079   1.00 21.48  ? 45   TYR A C   1 
ATOM   296  O O   . TYR A 1 45  ? -25.215 31.805  9.938   1.00 20.99  ? 45   TYR A O   1 
ATOM   297  C CB  . TYR A 1 45  ? -27.690 29.711  9.273   1.00 22.45  ? 45   TYR A CB  1 
ATOM   298  C CG  . TYR A 1 45  ? -28.422 30.687  10.164  1.00 24.06  ? 45   TYR A CG  1 
ATOM   299  C CD1 . TYR A 1 45  ? -28.795 31.949  9.689   1.00 24.29  ? 45   TYR A CD1 1 
ATOM   300  C CD2 . TYR A 1 45  ? -28.764 30.345  11.477  1.00 24.46  ? 45   TYR A CD2 1 
ATOM   301  C CE1 . TYR A 1 45  ? -29.461 32.851  10.508  1.00 25.25  ? 45   TYR A CE1 1 
ATOM   302  C CE2 . TYR A 1 45  ? -29.423 31.235  12.297  1.00 23.83  ? 45   TYR A CE2 1 
ATOM   303  C CZ  . TYR A 1 45  ? -29.769 32.476  11.806  1.00 25.33  ? 45   TYR A CZ  1 
ATOM   304  O OH  . TYR A 1 45  ? -30.419 33.352  12.640  1.00 29.62  ? 45   TYR A OH  1 
ATOM   305  N N   . TYR A 1 46  ? -25.349 31.170  7.782   1.00 21.73  ? 46   TYR A N   1 
ATOM   306  C CA  . TYR A 1 46  ? -24.598 32.297  7.292   1.00 24.06  ? 46   TYR A CA  1 
ATOM   307  C C   . TYR A 1 46  ? -25.325 33.610  7.534   1.00 25.98  ? 46   TYR A C   1 
ATOM   308  O O   . TYR A 1 46  ? -26.549 33.682  7.451   1.00 25.41  ? 46   TYR A O   1 
ATOM   309  C CB  . TYR A 1 46  ? -24.237 32.126  5.823   1.00 22.96  ? 46   TYR A CB  1 
ATOM   310  C CG  . TYR A 1 46  ? -23.185 31.086  5.585   1.00 23.88  ? 46   TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 46  ? -21.832 31.344  5.882   1.00 21.63  ? 46   TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 46  ? -23.517 29.852  5.033   1.00 21.40  ? 46   TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 46  ? -20.843 30.369  5.648   1.00 22.78  ? 46   TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 46  ? -22.527 28.872  4.819   1.00 21.80  ? 46   TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 46  ? -21.208 29.149  5.123   1.00 23.82  ? 46   TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 46  ? -20.267 28.160  4.905   1.00 24.34  ? 46   TYR A OH  1 
ATOM   317  N N   . SER A 1 47  ? -24.561 34.639  7.887   1.00 29.31  ? 47   SER A N   1 
ATOM   318  C CA  . SER A 1 47  ? -25.122 35.977  8.077   1.00 33.46  ? 47   SER A CA  1 
ATOM   319  C C   . SER A 1 47  ? -25.377 36.649  6.736   1.00 36.59  ? 47   SER A C   1 
ATOM   320  O O   . SER A 1 47  ? -24.857 36.206  5.702   1.00 36.54  ? 47   SER A O   1 
ATOM   321  C CB  . SER A 1 47  ? -24.189 36.844  8.896   1.00 32.86  ? 47   SER A CB  1 
ATOM   322  O OG  . SER A 1 47  ? -22.957 36.967  8.218   1.00 33.33  ? 47   SER A OG  1 
ATOM   323  N N   . LYS A 1 48  ? -26.150 37.735  6.782   1.00 40.55  ? 48   LYS A N   1 
ATOM   324  C CA  . LYS A 1 48  ? -26.656 38.451  5.588   1.00 44.59  ? 48   LYS A CA  1 
ATOM   325  C C   . LYS A 1 48  ? -25.616 39.107  4.683   1.00 45.41  ? 48   LYS A C   1 
ATOM   326  O O   . LYS A 1 48  ? -25.949 39.525  3.570   1.00 46.46  ? 48   LYS A O   1 
ATOM   327  C CB  . LYS A 1 48  ? -27.704 39.505  5.983   1.00 44.38  ? 48   LYS A CB  1 
ATOM   328  C CG  . LYS A 1 48  ? -29.145 38.998  5.984   1.00 46.85  ? 48   LYS A CG  1 
ATOM   329  C CD  . LYS A 1 48  ? -30.097 40.064  6.530   1.00 47.66  ? 48   LYS A CD  1 
ATOM   330  C CE  . LYS A 1 48  ? -30.669 41.000  5.436   1.00 52.43  ? 48   LYS A CE  1 
ATOM   331  N NZ  . LYS A 1 48  ? -31.959 40.469  4.878   1.00 53.93  ? 48   LYS A NZ  1 
ATOM   332  N N   . ASN A 1 49  ? -24.378 39.205  5.145   1.00 46.77  ? 49   ASN A N   1 
ATOM   333  C CA  . ASN A 1 49  ? -23.343 39.885  4.401   1.00 48.57  ? 49   ASN A CA  1 
ATOM   334  C C   . ASN A 1 49  ? -22.076 39.260  4.919   1.00 48.94  ? 49   ASN A C   1 
ATOM   335  O O   . ASN A 1 49  ? -21.692 39.457  6.080   1.00 50.20  ? 49   ASN A O   1 
ATOM   336  C CB  . ASN A 1 49  ? -23.373 41.402  4.704   1.00 49.45  ? 49   ASN A CB  1 
ATOM   337  C CG  . ASN A 1 49  ? -23.155 42.289  3.456   1.00 51.49  ? 49   ASN A CG  1 
ATOM   338  O OD1 . ASN A 1 49  ? -22.208 42.099  2.675   1.00 54.20  ? 49   ASN A OD1 1 
ATOM   339  N ND2 . ASN A 1 49  ? -24.018 43.295  3.301   1.00 53.94  ? 49   ASN A ND2 1 
ATOM   340  N N   . HIS A 1 50  ? -21.448 38.466  4.070   1.00 48.99  ? 50   HIS A N   1 
ATOM   341  C CA  . HIS A 1 50  ? -20.381 37.572  4.493   1.00 48.64  ? 50   HIS A CA  1 
ATOM   342  C C   . HIS A 1 50  ? -19.344 37.524  3.369   1.00 47.05  ? 50   HIS A C   1 
ATOM   343  O O   . HIS A 1 50  ? -18.127 37.515  3.617   1.00 47.87  ? 50   HIS A O   1 
ATOM   344  C CB  . HIS A 1 50  ? -20.977 36.151  4.750   1.00 49.83  ? 50   HIS A CB  1 
ATOM   345  C CG  . HIS A 1 50  ? -19.977 35.113  5.208   1.00 52.36  ? 50   HIS A CG  1 
ATOM   346  N ND1 . HIS A 1 50  ? -19.831 34.746  6.532   1.00 54.54  ? 50   HIS A ND1 1 
ATOM   347  C CD2 . HIS A 1 50  ? -19.095 34.352  4.511   1.00 53.41  ? 50   HIS A CD2 1 
ATOM   348  C CE1 . HIS A 1 50  ? -18.889 33.822  6.633   1.00 54.64  ? 50   HIS A CE1 1 
ATOM   349  N NE2 . HIS A 1 50  ? -18.425 33.566  5.421   1.00 53.77  ? 50   HIS A NE2 1 
ATOM   350  N N   . SER A 1 51  ? -19.844 37.529  2.130   1.00 43.70  ? 51   SER A N   1 
ATOM   351  C CA  . SER A 1 51  ? -19.143 36.870  1.032   1.00 40.36  ? 51   SER A CA  1 
ATOM   352  C C   . SER A 1 51  ? -18.377 37.785  0.056   1.00 37.53  ? 51   SER A C   1 
ATOM   353  O O   . SER A 1 51  ? -17.322 38.321  0.395   1.00 38.90  ? 51   SER A O   1 
ATOM   354  C CB  . SER A 1 51  ? -20.116 35.942  0.283   1.00 40.74  ? 51   SER A CB  1 
ATOM   355  O OG  . SER A 1 51  ? -21.158 36.667  -0.343  1.00 39.63  ? 51   SER A OG  1 
ATOM   356  N N   . TYR A 1 52  ? -18.899 37.937  -1.152  1.00 32.70  ? 52   TYR A N   1 
ATOM   357  C CA  . TYR A 1 52  ? -18.220 38.686  -2.193  1.00 28.23  ? 52   TYR A CA  1 
ATOM   358  C C   . TYR A 1 52  ? -19.013 39.930  -2.501  1.00 26.89  ? 52   TYR A C   1 
ATOM   359  O O   . TYR A 1 52  ? -20.235 39.972  -2.302  1.00 26.24  ? 52   TYR A O   1 
ATOM   360  C CB  . TYR A 1 52  ? -18.045 37.807  -3.450  1.00 26.68  ? 52   TYR A CB  1 
ATOM   361  C CG  . TYR A 1 52  ? -16.907 36.821  -3.305  1.00 24.26  ? 52   TYR A CG  1 
ATOM   362  C CD1 . TYR A 1 52  ? -17.070 35.622  -2.593  1.00 19.91  ? 52   TYR A CD1 1 
ATOM   363  C CD2 . TYR A 1 52  ? -15.663 37.089  -3.864  1.00 22.07  ? 52   TYR A CD2 1 
ATOM   364  C CE1 . TYR A 1 52  ? -16.018 34.696  -2.455  1.00 23.33  ? 52   TYR A CE1 1 
ATOM   365  C CE2 . TYR A 1 52  ? -14.583 36.168  -3.707  1.00 23.78  ? 52   TYR A CE2 1 
ATOM   366  C CZ  . TYR A 1 52  ? -14.776 35.000  -3.005  1.00 23.57  ? 52   TYR A CZ  1 
ATOM   367  O OH  . TYR A 1 52  ? -13.723 34.126  -2.878  1.00 25.46  ? 52   TYR A OH  1 
ATOM   368  N N   . HIS A 1 53  ? -18.327 40.957  -2.974  1.00 25.73  ? 53   HIS A N   1 
ATOM   369  C CA  . HIS A 1 53  ? -19.036 42.089  -3.515  1.00 26.12  ? 53   HIS A CA  1 
ATOM   370  C C   . HIS A 1 53  ? -18.497 42.375  -4.888  1.00 24.46  ? 53   HIS A C   1 
ATOM   371  O O   . HIS A 1 53  ? -17.347 42.072  -5.205  1.00 24.18  ? 53   HIS A O   1 
ATOM   372  C CB  . HIS A 1 53  ? -18.973 43.317  -2.587  1.00 27.10  ? 53   HIS A CB  1 
ATOM   373  C CG  . HIS A 1 53  ? -17.595 43.856  -2.406  1.00 29.71  ? 53   HIS A CG  1 
ATOM   374  N ND1 . HIS A 1 53  ? -17.107 44.913  -3.144  1.00 34.73  ? 53   HIS A ND1 1 
ATOM   375  C CD2 . HIS A 1 53  ? -16.585 43.462  -1.599  1.00 33.16  ? 53   HIS A CD2 1 
ATOM   376  C CE1 . HIS A 1 53  ? -15.854 45.148  -2.798  1.00 33.28  ? 53   HIS A CE1 1 
ATOM   377  N NE2 . HIS A 1 53  ? -15.512 44.278  -1.867  1.00 33.33  ? 53   HIS A NE2 1 
ATOM   378  N N   . VAL A 1 54  ? -19.354 42.944  -5.725  1.00 23.84  ? 54   VAL A N   1 
ATOM   379  C CA  . VAL A 1 54  ? -18.925 43.377  -7.042  1.00 23.24  ? 54   VAL A CA  1 
ATOM   380  C C   . VAL A 1 54  ? -18.013 44.604  -6.863  1.00 23.92  ? 54   VAL A C   1 
ATOM   381  O O   . VAL A 1 54  ? -18.358 45.555  -6.149  1.00 24.54  ? 54   VAL A O   1 
ATOM   382  C CB  . VAL A 1 54  ? -20.131 43.716  -7.954  1.00 23.14  ? 54   VAL A CB  1 
ATOM   383  C CG1 . VAL A 1 54  ? -19.651 44.238  -9.296  1.00 23.25  ? 54   VAL A CG1 1 
ATOM   384  C CG2 . VAL A 1 54  ? -20.983 42.455  -8.163  1.00 22.49  ? 54   VAL A CG2 1 
ATOM   385  N N   . GLU A 1 55  ? -16.868 44.566  -7.526  1.00 23.95  ? 55   GLU A N   1 
ATOM   386  C CA  . GLU A 1 55  ? -15.951 45.674  -7.536  1.00 26.47  ? 55   GLU A CA  1 
ATOM   387  C C   . GLU A 1 55  ? -16.077 46.427  -8.871  1.00 26.20  ? 55   GLU A C   1 
ATOM   388  O O   . GLU A 1 55  ? -15.783 45.887  -9.958  1.00 26.71  ? 55   GLU A O   1 
ATOM   389  C CB  . GLU A 1 55  ? -14.529 45.169  -7.292  1.00 27.39  ? 55   GLU A CB  1 
ATOM   390  C CG  . GLU A 1 55  ? -13.441 46.257  -7.269  1.00 34.61  ? 55   GLU A CG  1 
ATOM   391  C CD  . GLU A 1 55  ? -13.293 46.993  -5.913  1.00 42.76  ? 55   GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 55  ? -14.119 46.786  -4.981  1.00 45.39  ? 55   GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 55  ? -12.320 47.783  -5.779  1.00 46.06  ? 55   GLU A OE2 1 
ATOM   394  N N   . GLY A 1 56  ? -16.561 47.658  -8.787  1.00 25.59  ? 56   GLY A N   1 
ATOM   395  C CA  . GLY A 1 56  ? -16.633 48.506  -9.962  1.00 25.65  ? 56   GLY A CA  1 
ATOM   396  C C   . GLY A 1 56  ? -17.787 48.118  -10.866 1.00 24.93  ? 56   GLY A C   1 
ATOM   397  O O   . GLY A 1 56  ? -18.802 47.581  -10.400 1.00 25.60  ? 56   GLY A O   1 
ATOM   398  N N   . ASN A 1 57  ? -17.648 48.391  -12.149 1.00 23.52  ? 57   ASN A N   1 
ATOM   399  C CA  . ASN A 1 57  ? -18.763 48.181  -13.102 1.00 22.14  ? 57   ASN A CA  1 
ATOM   400  C C   . ASN A 1 57  ? -18.697 46.820  -13.759 1.00 20.90  ? 57   ASN A C   1 
ATOM   401  O O   . ASN A 1 57  ? -17.609 46.266  -13.978 1.00 20.91  ? 57   ASN A O   1 
ATOM   402  C CB  . ASN A 1 57  ? -18.749 49.246  -14.208 1.00 22.35  ? 57   ASN A CB  1 
ATOM   403  C CG  . ASN A 1 57  ? -19.010 50.652  -13.685 1.00 23.28  ? 57   ASN A CG  1 
ATOM   404  O OD1 . ASN A 1 57  ? -19.632 50.834  -12.642 1.00 22.73  ? 57   ASN A OD1 1 
ATOM   405  N ND2 . ASN A 1 57  ? -18.526 51.652  -14.416 1.00 24.31  ? 57   ASN A ND2 1 
ATOM   406  N N   . LEU A 1 58  ? -19.861 46.282  -14.089 1.00 19.52  ? 58   LEU A N   1 
ATOM   407  C CA  . LEU A 1 58  ? -19.966 45.195  -15.046 1.00 19.76  ? 58   LEU A CA  1 
ATOM   408  C C   . LEU A 1 58  ? -19.568 45.681  -16.418 1.00 19.29  ? 58   LEU A C   1 
ATOM   409  O O   . LEU A 1 58  ? -19.831 46.834  -16.784 1.00 19.79  ? 58   LEU A O   1 
ATOM   410  C CB  . LEU A 1 58  ? -21.403 44.625  -15.121 1.00 18.72  ? 58   LEU A CB  1 
ATOM   411  C CG  . LEU A 1 58  ? -21.832 43.553  -14.113 1.00 20.73  ? 58   LEU A CG  1 
ATOM   412  C CD1 . LEU A 1 58  ? -21.456 43.965  -12.726 1.00 20.77  ? 58   LEU A CD1 1 
ATOM   413  C CD2 . LEU A 1 58  ? -23.375 43.281  -14.154 1.00 19.80  ? 58   LEU A CD2 1 
ATOM   414  N N   . VAL A 1 59  ? -18.908 44.805  -17.161 1.00 20.01  ? 59   VAL A N   1 
ATOM   415  C CA  . VAL A 1 59  ? -18.469 45.105  -18.525 1.00 21.20  ? 59   VAL A CA  1 
ATOM   416  C C   . VAL A 1 59  ? -19.256 44.271  -19.534 1.00 20.51  ? 59   VAL A C   1 
ATOM   417  O O   . VAL A 1 59  ? -19.223 43.067  -19.465 1.00 19.64  ? 59   VAL A O   1 
ATOM   418  C CB  . VAL A 1 59  ? -16.980 44.736  -18.708 1.00 21.55  ? 59   VAL A CB  1 
ATOM   419  C CG1 . VAL A 1 59  ? -16.509 45.115  -20.100 1.00 23.57  ? 59   VAL A CG1 1 
ATOM   420  C CG2 . VAL A 1 59  ? -16.154 45.400  -17.628 1.00 23.27  ? 59   VAL A CG2 1 
ATOM   421  N N   . ASN A 1 60  ? -19.918 44.914  -20.494 1.00 21.11  ? 60   ASN A N   1 
ATOM   422  C CA  . ASN A 1 60  ? -20.491 44.193  -21.636 1.00 21.02  ? 60   ASN A CA  1 
ATOM   423  C C   . ASN A 1 60  ? -19.462 43.518  -22.499 1.00 22.36  ? 60   ASN A C   1 
ATOM   424  O O   . ASN A 1 60  ? -18.410 44.104  -22.783 1.00 21.78  ? 60   ASN A O   1 
ATOM   425  C CB  . ASN A 1 60  ? -21.227 45.152  -22.533 1.00 22.65  ? 60   ASN A CB  1 
ATOM   426  C CG  . ASN A 1 60  ? -22.492 45.617  -21.910 1.00 22.31  ? 60   ASN A CG  1 
ATOM   427  O OD1 . ASN A 1 60  ? -23.490 44.904  -21.902 1.00 27.77  ? 60   ASN A OD1 1 
ATOM   428  N ND2 . ASN A 1 60  ? -22.453 46.783  -21.322 1.00 22.99  ? 60   ASN A ND2 1 
ATOM   429  N N   . THR A 1 61  ? -19.773 42.297  -22.924 1.00 20.89  ? 61   THR A N   1 
ATOM   430  C CA  . THR A 1 61  ? -18.931 41.545  -23.832 1.00 21.60  ? 61   THR A CA  1 
ATOM   431  C C   . THR A 1 61  ? -19.880 41.177  -24.970 1.00 21.69  ? 61   THR A C   1 
ATOM   432  O O   . THR A 1 61  ? -21.104 41.353  -24.842 1.00 21.71  ? 61   THR A O   1 
ATOM   433  C CB  . THR A 1 61  ? -18.425 40.272  -23.185 1.00 21.67  ? 61   THR A CB  1 
ATOM   434  O OG1 . THR A 1 61  ? -19.550 39.457  -22.817 1.00 22.43  ? 61   THR A OG1 1 
ATOM   435  C CG2 . THR A 1 61  ? -17.573 40.554  -21.932 1.00 21.65  ? 61   THR A CG2 1 
ATOM   436  N N   . ASN A 1 62  ? -19.334 40.685  -26.072 1.00 22.18  ? 62   ASN A N   1 
ATOM   437  C CA  . ASN A 1 62  ? -20.166 40.192  -27.184 1.00 23.52  ? 62   ASN A CA  1 
ATOM   438  C C   . ASN A 1 62  ? -21.211 39.148  -26.750 1.00 22.41  ? 62   ASN A C   1 
ATOM   439  O O   . ASN A 1 62  ? -22.339 39.151  -27.254 1.00 23.10  ? 62   ASN A O   1 
ATOM   440  C CB  . ASN A 1 62  ? -19.272 39.599  -28.292 1.00 24.44  ? 62   ASN A CB  1 
ATOM   441  C CG  . ASN A 1 62  ? -18.512 40.675  -29.084 1.00 29.26  ? 62   ASN A CG  1 
ATOM   442  O OD1 . ASN A 1 62  ? -17.391 40.439  -29.578 1.00 34.78  ? 62   ASN A OD1 1 
ATOM   443  N ND2 . ASN A 1 62  ? -19.120 41.839  -29.229 1.00 29.40  ? 62   ASN A ND2 1 
ATOM   444  N N   . ALA A 1 63  ? -20.813 38.267  -25.828 1.00 21.50  ? 63   ALA A N   1 
ATOM   445  C CA  . ALA A 1 63  ? -21.622 37.126  -25.357 1.00 20.93  ? 63   ALA A CA  1 
ATOM   446  C C   . ALA A 1 63  ? -22.569 37.468  -24.204 1.00 20.74  ? 63   ALA A C   1 
ATOM   447  O O   . ALA A 1 63  ? -23.559 36.771  -23.993 1.00 20.88  ? 63   ALA A O   1 
ATOM   448  C CB  . ALA A 1 63  ? -20.689 36.004  -24.932 1.00 22.02  ? 63   ALA A CB  1 
ATOM   449  N N   . GLY A 1 64  ? -22.241 38.507  -23.433 1.00 19.49  ? 64   GLY A N   1 
ATOM   450  C CA  . GLY A 1 64  ? -22.985 38.880  -22.234 1.00 18.91  ? 64   GLY A CA  1 
ATOM   451  C C   . GLY A 1 64  ? -22.257 39.953  -21.427 1.00 18.72  ? 64   GLY A C   1 
ATOM   452  O O   . GLY A 1 64  ? -22.192 41.115  -21.832 1.00 18.41  ? 64   GLY A O   1 
ATOM   453  N N   . PHE A 1 65  ? -21.699 39.571  -20.292 1.00 18.10  ? 65   PHE A N   1 
ATOM   454  C CA  . PHE A 1 65  ? -20.965 40.516  -19.442 1.00 18.11  ? 65   PHE A CA  1 
ATOM   455  C C   . PHE A 1 65  ? -20.000 39.799  -18.532 1.00 19.21  ? 65   PHE A C   1 
ATOM   456  O O   . PHE A 1 65  ? -20.109 38.570  -18.329 1.00 17.82  ? 65   PHE A O   1 
ATOM   457  C CB  . PHE A 1 65  ? -21.885 41.384  -18.590 1.00 18.90  ? 65   PHE A CB  1 
ATOM   458  C CG  . PHE A 1 65  ? -22.766 40.594  -17.634 1.00 20.97  ? 65   PHE A CG  1 
ATOM   459  C CD1 . PHE A 1 65  ? -22.337 40.326  -16.328 1.00 20.48  ? 65   PHE A CD1 1 
ATOM   460  C CD2 . PHE A 1 65  ? -24.040 40.147  -18.041 1.00 23.67  ? 65   PHE A CD2 1 
ATOM   461  C CE1 . PHE A 1 65  ? -23.114 39.597  -15.449 1.00 19.07  ? 65   PHE A CE1 1 
ATOM   462  C CE2 . PHE A 1 65  ? -24.858 39.445  -17.172 1.00 19.62  ? 65   PHE A CE2 1 
ATOM   463  C CZ  . PHE A 1 65  ? -24.413 39.157  -15.876 1.00 20.19  ? 65   PHE A CZ  1 
ATOM   464  N N   . THR A 1 66  ? -19.039 40.573  -18.006 1.00 18.09  ? 66   THR A N   1 
ATOM   465  C CA  . THR A 1 66  ? -18.220 40.111  -16.902 1.00 19.04  ? 66   THR A CA  1 
ATOM   466  C C   . THR A 1 66  ? -18.289 41.059  -15.708 1.00 19.18  ? 66   THR A C   1 
ATOM   467  O O   . THR A 1 66  ? -18.567 42.256  -15.852 1.00 21.26  ? 66   THR A O   1 
ATOM   468  C CB  . THR A 1 66  ? -16.748 39.945  -17.344 1.00 19.02  ? 66   THR A CB  1 
ATOM   469  O OG1 . THR A 1 66  ? -16.278 41.171  -17.910 1.00 21.49  ? 66   THR A OG1 1 
ATOM   470  C CG2 . THR A 1 66  ? -16.608 38.850  -18.400 1.00 18.88  ? 66   THR A CG2 1 
ATOM   471  N N   . ALA A 1 67  ? -18.026 40.514  -14.523 1.00 19.74  ? 67   ALA A N   1 
ATOM   472  C CA  . ALA A 1 67  ? -17.911 41.278  -13.313 1.00 20.36  ? 67   ALA A CA  1 
ATOM   473  C C   . ALA A 1 67  ? -16.705 40.788  -12.532 1.00 21.19  ? 67   ALA A C   1 
ATOM   474  O O   . ALA A 1 67  ? -16.335 39.604  -12.588 1.00 21.30  ? 67   ALA A O   1 
ATOM   475  C CB  . ALA A 1 67  ? -19.139 41.093  -12.483 1.00 19.35  ? 67   ALA A CB  1 
ATOM   476  N N   . ARG A 1 68  ? -16.080 41.715  -11.827 1.00 21.37  ? 68   ARG A N   1 
ATOM   477  C CA  A ARG A 1 68  ? -15.028 41.365  -10.874 0.50 22.48  ? 68   ARG A CA  1 
ATOM   478  C CA  B ARG A 1 68  ? -15.019 41.378  -10.866 0.50 22.84  ? 68   ARG A CA  1 
ATOM   479  C C   . ARG A 1 68  ? -15.654 41.336  -9.494  1.00 22.92  ? 68   ARG A C   1 
ATOM   480  O O   . ARG A 1 68  ? -16.319 42.299  -9.096  1.00 23.46  ? 68   ARG A O   1 
ATOM   481  C CB  A ARG A 1 68  ? -13.872 42.370  -10.955 0.50 22.55  ? 68   ARG A CB  1 
ATOM   482  C CB  B ARG A 1 68  ? -13.875 42.409  -10.905 0.50 22.53  ? 68   ARG A CB  1 
ATOM   483  C CG  A ARG A 1 68  ? -13.039 42.230  -12.214 0.50 23.40  ? 68   ARG A CG  1 
ATOM   484  C CG  B ARG A 1 68  ? -12.979 42.394  -9.662  0.50 22.99  ? 68   ARG A CG  1 
ATOM   485  C CD  A ARG A 1 68  ? -12.223 43.496  -12.504 0.50 27.74  ? 68   ARG A CD  1 
ATOM   486  C CD  B ARG A 1 68  ? -11.927 43.494  -9.698  0.50 24.95  ? 68   ARG A CD  1 
ATOM   487  N NE  A ARG A 1 68  ? -10.880 43.181  -12.982 0.50 29.78  ? 68   ARG A NE  1 
ATOM   488  N NE  B ARG A 1 68  ? -10.931 43.336  -8.639  0.50 27.29  ? 68   ARG A NE  1 
ATOM   489  C CZ  A ARG A 1 68  ? -10.166 43.945  -13.809 0.50 32.51  ? 68   ARG A CZ  1 
ATOM   490  C CZ  B ARG A 1 68  ? -10.049 44.276  -8.295  0.50 30.14  ? 68   ARG A CZ  1 
ATOM   491  N NH1 A ARG A 1 68  ? -10.661 45.086  -14.281 0.50 32.96  ? 68   ARG A NH1 1 
ATOM   492  N NH1 B ARG A 1 68  ? -10.042 45.446  -8.916  0.50 30.24  ? 68   ARG A NH1 1 
ATOM   493  N NH2 A ARG A 1 68  ? -8.944  43.560  -14.172 0.50 33.22  ? 68   ARG A NH2 1 
ATOM   494  N NH2 B ARG A 1 68  ? -9.166  44.053  -7.326  0.50 30.70  ? 68   ARG A NH2 1 
ATOM   495  N N   . LEU A 1 69  ? -15.486 40.204  -8.794  1.00 22.60  ? 69   LEU A N   1 
ATOM   496  C CA  . LEU A 1 69  ? -15.956 40.043  -7.448  1.00 23.65  ? 69   LEU A CA  1 
ATOM   497  C C   . LEU A 1 69  ? -14.757 40.072  -6.495  1.00 25.58  ? 69   LEU A C   1 
ATOM   498  O O   . LEU A 1 69  ? -13.697 39.493  -6.776  1.00 24.90  ? 69   LEU A O   1 
ATOM   499  C CB  . LEU A 1 69  ? -16.721 38.736  -7.296  1.00 23.76  ? 69   LEU A CB  1 
ATOM   500  C CG  . LEU A 1 69  ? -17.789 38.413  -8.332  1.00 24.01  ? 69   LEU A CG  1 
ATOM   501  C CD1 . LEU A 1 69  ? -18.617 37.234  -7.796  1.00 23.13  ? 69   LEU A CD1 1 
ATOM   502  C CD2 . LEU A 1 69  ? -18.636 39.617  -8.576  1.00 23.62  ? 69   LEU A CD2 1 
ATOM   503  N N   . LYS A 1 70  ? -14.910 40.779  -5.395  1.00 27.17  ? 70   LYS A N   1 
ATOM   504  C CA  . LYS A 1 70  ? -13.825 40.896  -4.453  1.00 31.12  ? 70   LYS A CA  1 
ATOM   505  C C   . LYS A 1 70  ? -14.289 40.305  -3.143  1.00 31.16  ? 70   LYS A C   1 
ATOM   506  O O   . LYS A 1 70  ? -15.398 40.557  -2.703  1.00 30.35  ? 70   LYS A O   1 
ATOM   507  C CB  . LYS A 1 70  ? -13.394 42.370  -4.329  1.00 30.69  ? 70   LYS A CB  1 
ATOM   508  C CG  . LYS A 1 70  ? -12.055 42.616  -3.628  1.00 34.90  ? 70   LYS A CG  1 
ATOM   509  C CD  . LYS A 1 70  ? -11.689 44.120  -3.683  1.00 34.75  ? 70   LYS A CD  1 
ATOM   510  C CE  . LYS A 1 70  ? -10.572 44.464  -2.665  1.00 42.52  ? 70   LYS A CE  1 
ATOM   511  N NZ  . LYS A 1 70  ? -9.956  45.791  -2.972  1.00 43.30  ? 70   LYS A NZ  1 
ATOM   512  N N   . ASN A 1 71  ? -13.436 39.486  -2.537  1.00 34.17  ? 71   ASN A N   1 
ATOM   513  C CA  . ASN A 1 71  ? -13.749 38.858  -1.268  1.00 37.48  ? 71   ASN A CA  1 
ATOM   514  C C   . ASN A 1 71  ? -13.823 39.903  -0.162  1.00 39.86  ? 71   ASN A C   1 
ATOM   515  O O   . ASN A 1 71  ? -12.872 40.652  0.062   1.00 40.02  ? 71   ASN A O   1 
ATOM   516  C CB  . ASN A 1 71  ? -12.704 37.779  -0.933  1.00 37.70  ? 71   ASN A CB  1 
ATOM   517  C CG  . ASN A 1 71  ? -13.039 36.999  0.322   1.00 38.57  ? 71   ASN A CG  1 
ATOM   518  O OD1 . ASN A 1 71  ? -14.158 36.508  0.498   1.00 38.83  ? 71   ASN A OD1 1 
ATOM   519  N ND2 . ASN A 1 71  ? -12.054 36.885  1.219   1.00 41.61  ? 71   ASN A ND2 1 
ATOM   520  N N   . LEU A 1 72  ? -14.972 39.949  0.502   1.00 43.18  ? 72   LEU A N   1 
ATOM   521  C CA  . LEU A 1 72  ? -15.146 40.700  1.748   1.00 46.65  ? 72   LEU A CA  1 
ATOM   522  C C   . LEU A 1 72  ? -14.462 39.923  2.884   1.00 48.64  ? 72   LEU A C   1 
ATOM   523  O O   . LEU A 1 72  ? -14.695 38.720  3.040   1.00 48.79  ? 72   LEU A O   1 
ATOM   524  C CB  . LEU A 1 72  ? -16.642 40.892  2.061   1.00 46.86  ? 72   LEU A CB  1 
ATOM   525  C CG  . LEU A 1 72  ? -17.480 41.886  1.247   1.00 47.53  ? 72   LEU A CG  1 
ATOM   526  C CD1 . LEU A 1 72  ? -18.968 41.600  1.395   1.00 48.38  ? 72   LEU A CD1 1 
ATOM   527  C CD2 . LEU A 1 72  ? -17.172 43.351  1.643   1.00 48.18  ? 72   LEU A CD2 1 
ATOM   528  N N   . PRO A 1 73  ? -13.644 40.614  3.700   1.00 50.86  ? 73   PRO A N   1 
ATOM   529  C CA  . PRO A 1 73  ? -12.760 39.916  4.660   1.00 52.29  ? 73   PRO A CA  1 
ATOM   530  C C   . PRO A 1 73  ? -13.506 38.825  5.455   1.00 52.99  ? 73   PRO A C   1 
ATOM   531  O O   . PRO A 1 73  ? -14.620 39.049  5.934   1.00 53.03  ? 73   PRO A O   1 
ATOM   532  C CB  . PRO A 1 73  ? -12.248 41.051  5.572   1.00 52.62  ? 73   PRO A CB  1 
ATOM   533  C CG  . PRO A 1 73  ? -12.320 42.310  4.695   1.00 52.84  ? 73   PRO A CG  1 
ATOM   534  C CD  . PRO A 1 73  ? -13.545 42.088  3.801   1.00 51.41  ? 73   PRO A CD  1 
ATOM   535  N N   . SER A 1 74  ? -12.907 37.645  5.556   1.00 53.83  ? 74   SER A N   1 
ATOM   536  C CA  . SER A 1 74  ? -13.649 36.475  6.013   1.00 54.66  ? 74   SER A CA  1 
ATOM   537  C C   . SER A 1 74  ? -12.719 35.420  6.614   1.00 54.83  ? 74   SER A C   1 
ATOM   538  O O   . SER A 1 74  ? -11.569 35.293  6.188   1.00 54.88  ? 74   SER A O   1 
ATOM   539  C CB  . SER A 1 74  ? -14.427 35.889  4.830   1.00 54.85  ? 74   SER A CB  1 
ATOM   540  O OG  . SER A 1 74  ? -15.455 35.034  5.277   1.00 56.60  ? 74   SER A OG  1 
ATOM   541  N N   . SER A 1 75  ? -13.214 34.664  7.597   1.00 55.07  ? 75   SER A N   1 
ATOM   542  C CA  . SER A 1 75  ? -12.400 33.627  8.266   1.00 55.22  ? 75   SER A CA  1 
ATOM   543  C C   . SER A 1 75  ? -12.101 32.439  7.322   1.00 54.68  ? 75   SER A C   1 
ATOM   544  O O   . SER A 1 75  ? -12.970 32.039  6.553   1.00 55.05  ? 75   SER A O   1 
ATOM   545  C CB  . SER A 1 75  ? -13.095 33.153  9.549   1.00 55.46  ? 75   SER A CB  1 
ATOM   546  O OG  . SER A 1 75  ? -14.335 32.537  9.237   1.00 56.82  ? 75   SER A OG  1 
ATOM   547  N N   . PRO A 1 76  ? -10.872 31.875  7.371   1.00 54.03  ? 76   PRO A N   1 
ATOM   548  C CA  . PRO A 1 76  ? -10.510 30.869  6.375   1.00 53.31  ? 76   PRO A CA  1 
ATOM   549  C C   . PRO A 1 76  ? -10.799 29.426  6.831   1.00 52.27  ? 76   PRO A C   1 
ATOM   550  O O   . PRO A 1 76  ? -9.876  28.695  7.221   1.00 53.02  ? 76   PRO A O   1 
ATOM   551  C CB  . PRO A 1 76  ? -9.003  31.099  6.194   1.00 53.44  ? 76   PRO A CB  1 
ATOM   552  C CG  . PRO A 1 76  ? -8.534  31.687  7.515   1.00 53.98  ? 76   PRO A CG  1 
ATOM   553  C CD  . PRO A 1 76  ? -9.760  32.114  8.311   1.00 54.33  ? 76   PRO A CD  1 
ATOM   554  N N   . VAL A 1 77  ? -12.065 29.016  6.747   1.00 50.37  ? 77   VAL A N   1 
ATOM   555  C CA  . VAL A 1 77  ? -12.512 27.728  7.294   1.00 48.31  ? 77   VAL A CA  1 
ATOM   556  C C   . VAL A 1 77  ? -11.934 26.495  6.592   1.00 47.09  ? 77   VAL A C   1 
ATOM   557  O O   . VAL A 1 77  ? -11.345 25.618  7.239   1.00 47.13  ? 77   VAL A O   1 
ATOM   558  C CB  . VAL A 1 77  ? -14.047 27.644  7.323   1.00 48.42  ? 77   VAL A CB  1 
ATOM   559  C CG1 . VAL A 1 77  ? -14.484 26.338  7.943   1.00 48.47  ? 77   VAL A CG1 1 
ATOM   560  C CG2 . VAL A 1 77  ? -14.619 28.823  8.093   1.00 48.40  ? 77   VAL A CG2 1 
ATOM   561  N N   . PHE A 1 78  ? -12.110 26.410  5.278   1.00 44.90  ? 78   PHE A N   1 
ATOM   562  C CA  . PHE A 1 78  ? -11.616 25.251  4.535   1.00 43.24  ? 78   PHE A CA  1 
ATOM   563  C C   . PHE A 1 78  ? -10.465 25.674  3.676   1.00 43.63  ? 78   PHE A C   1 
ATOM   564  O O   . PHE A 1 78  ? -10.304 25.235  2.532   1.00 43.40  ? 78   PHE A O   1 
ATOM   565  C CB  . PHE A 1 78  ? -12.742 24.579  3.769   1.00 41.70  ? 78   PHE A CB  1 
ATOM   566  C CG  . PHE A 1 78  ? -13.857 24.176  4.653   1.00 39.61  ? 78   PHE A CG  1 
ATOM   567  C CD1 . PHE A 1 78  ? -15.090 24.778  4.552   1.00 37.02  ? 78   PHE A CD1 1 
ATOM   568  C CD2 . PHE A 1 78  ? -13.644 23.247  5.661   1.00 37.81  ? 78   PHE A CD2 1 
ATOM   569  C CE1 . PHE A 1 78  ? -16.120 24.424  5.404   1.00 39.27  ? 78   PHE A CE1 1 
ATOM   570  C CE2 . PHE A 1 78  ? -14.668 22.890  6.518   1.00 36.86  ? 78   PHE A CE2 1 
ATOM   571  C CZ  . PHE A 1 78  ? -15.907 23.479  6.388   1.00 38.60  ? 78   PHE A CZ  1 
ATOM   572  N N   . GLY A 1 79  ? -9.671  26.551  4.289   1.00 43.94  ? 79   GLY A N   1 
ATOM   573  C CA  . GLY A 1 79  ? -8.415  27.027  3.761   1.00 44.09  ? 79   GLY A CA  1 
ATOM   574  C C   . GLY A 1 79  ? -8.488  28.123  2.722   1.00 44.24  ? 79   GLY A C   1 
ATOM   575  O O   . GLY A 1 79  ? -9.372  29.004  2.765   1.00 43.87  ? 79   GLY A O   1 
ATOM   576  N N   . SER A 1 80  ? -7.530  28.007  1.793   1.00 44.40  ? 80   SER A N   1 
ATOM   577  C CA  . SER A 1 80  ? -7.129  28.982  0.768   1.00 44.19  ? 80   SER A CA  1 
ATOM   578  C C   . SER A 1 80  ? -8.220  29.660  -0.079  1.00 43.24  ? 80   SER A C   1 
ATOM   579  O O   . SER A 1 80  ? -8.503  29.227  -1.199  1.00 43.26  ? 80   SER A O   1 
ATOM   580  C CB  . SER A 1 80  ? -6.092  28.331  -0.166  1.00 44.70  ? 80   SER A CB  1 
ATOM   581  O OG  . SER A 1 80  ? -4.967  27.882  0.573   1.00 46.81  ? 80   SER A OG  1 
ATOM   582  N N   . ASN A 1 81  ? -8.756  30.751  0.460   1.00 41.18  ? 81   ASN A N   1 
ATOM   583  C CA  . ASN A 1 81  ? -9.801  31.546  -0.147  1.00 40.21  ? 81   ASN A CA  1 
ATOM   584  C C   . ASN A 1 81  ? -9.371  32.350  -1.400  1.00 39.34  ? 81   ASN A C   1 
ATOM   585  O O   . ASN A 1 81  ? -8.186  32.682  -1.564  1.00 39.80  ? 81   ASN A O   1 
ATOM   586  C CB  . ASN A 1 81  ? -10.351 32.472  0.909   1.00 40.01  ? 81   ASN A CB  1 
ATOM   587  C CG  . ASN A 1 81  ? -11.702 32.948  0.579   1.00 42.63  ? 81   ASN A CG  1 
ATOM   588  O OD1 . ASN A 1 81  ? -11.889 33.659  -0.402  1.00 45.66  ? 81   ASN A OD1 1 
ATOM   589  N ND2 . ASN A 1 81  ? -12.683 32.559  1.388   1.00 44.62  ? 81   ASN A ND2 1 
ATOM   590  N N   . VAL A 1 82  ? -10.322 32.645  -2.293  1.00 36.83  ? 82   VAL A N   1 
ATOM   591  C CA  . VAL A 1 82  ? -9.976  33.259  -3.575  1.00 34.87  ? 82   VAL A CA  1 
ATOM   592  C C   . VAL A 1 82  ? -10.382 34.734  -3.527  1.00 34.65  ? 82   VAL A C   1 
ATOM   593  O O   . VAL A 1 82  ? -11.577 35.059  -3.451  1.00 34.39  ? 82   VAL A O   1 
ATOM   594  C CB  . VAL A 1 82  ? -10.545 32.436  -4.806  1.00 35.14  ? 82   VAL A CB  1 
ATOM   595  C CG1 . VAL A 1 82  ? -10.507 33.219  -6.076  1.00 33.40  ? 82   VAL A CG1 1 
ATOM   596  C CG2 . VAL A 1 82  ? -9.750  31.148  -4.996  1.00 33.47  ? 82   VAL A CG2 1 
ATOM   597  N N   . ASP A 1 83  ? -9.386  35.621  -3.528  1.00 32.88  ? 83   ASP A N   1 
ATOM   598  C CA  . ASP A 1 83  ? -9.625  37.046  -3.271  1.00 33.75  ? 83   ASP A CA  1 
ATOM   599  C C   . ASP A 1 83  ? -10.316 37.779  -4.411  1.00 32.05  ? 83   ASP A C   1 
ATOM   600  O O   . ASP A 1 83  ? -11.192 38.593  -4.161  1.00 33.16  ? 83   ASP A O   1 
ATOM   601  C CB  . ASP A 1 83  ? -8.336  37.782  -2.918  1.00 34.66  ? 83   ASP A CB  1 
ATOM   602  C CG  . ASP A 1 83  ? -7.771  37.337  -1.589  1.00 39.49  ? 83   ASP A CG  1 
ATOM   603  O OD1 . ASP A 1 83  ? -8.577  36.951  -0.694  1.00 43.77  ? 83   ASP A OD1 1 
ATOM   604  O OD2 . ASP A 1 83  ? -6.523  37.357  -1.446  1.00 43.49  ? 83   ASP A OD2 1 
ATOM   605  N N   . ASN A 1 84  ? -9.928  37.478  -5.645  1.00 29.99  ? 84   ASN A N   1 
ATOM   606  C CA  . ASN A 1 84  ? -10.530 38.093  -6.819  1.00 28.54  ? 84   ASN A CA  1 
ATOM   607  C C   . ASN A 1 84  ? -11.126 37.050  -7.706  1.00 26.71  ? 84   ASN A C   1 
ATOM   608  O O   . ASN A 1 84  ? -10.415 36.226  -8.274  1.00 25.51  ? 84   ASN A O   1 
ATOM   609  C CB  . ASN A 1 84  ? -9.487  38.862  -7.598  1.00 29.81  ? 84   ASN A CB  1 
ATOM   610  C CG  . ASN A 1 84  ? -8.927  39.998  -6.810  1.00 32.77  ? 84   ASN A CG  1 
ATOM   611  O OD1 . ASN A 1 84  ? -7.856  39.872  -6.230  1.00 39.58  ? 84   ASN A OD1 1 
ATOM   612  N ND2 . ASN A 1 84  ? -9.678  41.099  -6.723  1.00 37.32  ? 84   ASN A ND2 1 
ATOM   613  N N   . VAL A 1 85  ? -12.444 37.104  -7.800  1.00 24.20  ? 85   VAL A N   1 
ATOM   614  C CA  . VAL A 1 85  ? -13.237 36.147  -8.563  1.00 22.51  ? 85   VAL A CA  1 
ATOM   615  C C   . VAL A 1 85  ? -13.797 36.866  -9.801  1.00 22.22  ? 85   VAL A C   1 
ATOM   616  O O   . VAL A 1 85  ? -14.200 38.041  -9.723  1.00 22.76  ? 85   VAL A O   1 
ATOM   617  C CB  . VAL A 1 85  ? -14.333 35.541  -7.637  1.00 22.07  ? 85   VAL A CB  1 
ATOM   618  C CG1 . VAL A 1 85  ? -15.510 34.850  -8.436  1.00 19.56  ? 85   VAL A CG1 1 
ATOM   619  C CG2 . VAL A 1 85  ? -13.684 34.549  -6.670  1.00 22.24  ? 85   VAL A CG2 1 
ATOM   620  N N   . LEU A 1 86  ? -13.786 36.184  -10.941 1.00 20.80  ? 86   LEU A N   1 
ATOM   621  C CA  . LEU A 1 86  ? -14.316 36.739  -12.148 1.00 20.83  ? 86   LEU A CA  1 
ATOM   622  C C   . LEU A 1 86  ? -15.613 36.003  -12.412 1.00 20.19  ? 86   LEU A C   1 
ATOM   623  O O   . LEU A 1 86  ? -15.652 34.778  -12.371 1.00 20.03  ? 86   LEU A O   1 
ATOM   624  C CB  . LEU A 1 86  ? -13.357 36.542  -13.329 1.00 20.83  ? 86   LEU A CB  1 
ATOM   625  C CG  . LEU A 1 86  ? -13.801 37.094  -14.701 1.00 21.31  ? 86   LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 86  ? -13.685 38.588  -14.756 1.00 23.19  ? 86   LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 86  ? -12.999 36.491  -15.827 1.00 23.03  ? 86   LEU A CD2 1 
ATOM   628  N N   . LEU A 1 87  ? -16.663 36.778  -12.639 1.00 19.48  ? 87   LEU A N   1 
ATOM   629  C CA  . LEU A 1 87  ? -17.920 36.285  -13.183 1.00 19.13  ? 87   LEU A CA  1 
ATOM   630  C C   . LEU A 1 87  ? -17.941 36.540  -14.690 1.00 18.43  ? 87   LEU A C   1 
ATOM   631  O O   . LEU A 1 87  ? -17.742 37.668  -15.141 1.00 18.09  ? 87   LEU A O   1 
ATOM   632  C CB  . LEU A 1 87  ? -19.089 37.013  -12.498 1.00 17.62  ? 87   LEU A CB  1 
ATOM   633  C CG  . LEU A 1 87  ? -20.511 36.720  -13.043 1.00 21.03  ? 87   LEU A CG  1 
ATOM   634  C CD1 . LEU A 1 87  ? -20.910 35.275  -12.879 1.00 19.51  ? 87   LEU A CD1 1 
ATOM   635  C CD2 . LEU A 1 87  ? -21.521 37.576  -12.330 1.00 20.03  ? 87   LEU A CD2 1 
ATOM   636  N N   . THR A 1 88  ? -18.170 35.488  -15.475 1.00 19.18  ? 88   THR A N   1 
ATOM   637  C CA  . THR A 1 88  ? -18.344 35.597  -16.901 1.00 19.09  ? 88   THR A CA  1 
ATOM   638  C C   . THR A 1 88  ? -19.732 35.023  -17.182 1.00 18.71  ? 88   THR A C   1 
ATOM   639  O O   . THR A 1 88  ? -20.015 33.887  -16.804 1.00 18.04  ? 88   THR A O   1 
ATOM   640  C CB  . THR A 1 88  ? -17.314 34.770  -17.625 1.00 20.04  ? 88   THR A CB  1 
ATOM   641  O OG1 . THR A 1 88  ? -16.009 35.248  -17.289 1.00 23.44  ? 88   THR A OG1 1 
ATOM   642  C CG2 . THR A 1 88  ? -17.488 34.858  -19.151 1.00 21.92  ? 88   THR A CG2 1 
ATOM   643  N N   . ALA A 1 89  ? -20.577 35.821  -17.831 1.00 17.68  ? 89   ALA A N   1 
ATOM   644  C CA  . ALA A 1 89  ? -21.965 35.447  -18.136 1.00 17.58  ? 89   ALA A CA  1 
ATOM   645  C C   . ALA A 1 89  ? -22.178 35.492  -19.628 1.00 17.87  ? 89   ALA A C   1 
ATOM   646  O O   . ALA A 1 89  ? -21.713 36.441  -20.316 1.00 17.66  ? 89   ALA A O   1 
ATOM   647  C CB  . ALA A 1 89  ? -22.909 36.420  -17.443 1.00 16.97  ? 89   ALA A CB  1 
ATOM   648  N N   . GLU A 1 90  ? -22.839 34.462  -20.170 1.00 17.74  ? 90   GLU A N   1 
ATOM   649  C CA  . GLU A 1 90  ? -23.042 34.390  -21.612 1.00 18.44  ? 90   GLU A CA  1 
ATOM   650  C C   . GLU A 1 90  ? -24.490 34.051  -21.883 1.00 18.65  ? 90   GLU A C   1 
ATOM   651  O O   . GLU A 1 90  ? -24.985 33.071  -21.352 1.00 17.59  ? 90   GLU A O   1 
ATOM   652  C CB  . GLU A 1 90  ? -22.145 33.317  -22.221 1.00 18.61  ? 90   GLU A CB  1 
ATOM   653  C CG  . GLU A 1 90  ? -20.637 33.586  -21.978 1.00 22.63  ? 90   GLU A CG  1 
ATOM   654  C CD  . GLU A 1 90  ? -19.779 32.425  -22.393 1.00 26.46  ? 90   GLU A CD  1 
ATOM   655  O OE1 . GLU A 1 90  ? -20.276 31.277  -22.370 1.00 25.16  ? 90   GLU A OE1 1 
ATOM   656  O OE2 . GLU A 1 90  ? -18.607 32.650  -22.779 1.00 31.15  ? 90   GLU A OE2 1 
ATOM   657  N N   . TYR A 1 91  ? -25.157 34.899  -22.668 1.00 18.63  ? 91   TYR A N   1 
ATOM   658  C CA  . TYR A 1 91  ? -26.537 34.656  -23.104 1.00 19.09  ? 91   TYR A CA  1 
ATOM   659  C C   . TYR A 1 91  ? -26.438 33.772  -24.327 1.00 17.80  ? 91   TYR A C   1 
ATOM   660  O O   . TYR A 1 91  ? -26.546 34.228  -25.474 1.00 17.71  ? 91   TYR A O   1 
ATOM   661  C CB  . TYR A 1 91  ? -27.225 35.976  -23.412 1.00 20.92  ? 91   TYR A CB  1 
ATOM   662  C CG  . TYR A 1 91  ? -27.318 36.951  -22.232 1.00 23.10  ? 91   TYR A CG  1 
ATOM   663  C CD1 . TYR A 1 91  ? -28.269 36.781  -21.243 1.00 26.44  ? 91   TYR A CD1 1 
ATOM   664  C CD2 . TYR A 1 91  ? -26.486 38.070  -22.135 1.00 25.86  ? 91   TYR A CD2 1 
ATOM   665  C CE1 . TYR A 1 91  ? -28.388 37.689  -20.158 1.00 27.13  ? 91   TYR A CE1 1 
ATOM   666  C CE2 . TYR A 1 91  ? -26.592 38.996  -21.043 1.00 26.83  ? 91   TYR A CE2 1 
ATOM   667  C CZ  . TYR A 1 91  ? -27.535 38.784  -20.060 1.00 27.40  ? 91   TYR A CZ  1 
ATOM   668  O OH  . TYR A 1 91  ? -27.692 39.666  -19.008 1.00 24.30  ? 91   TYR A OH  1 
ATOM   669  N N   . GLN A 1 92  ? -26.205 32.493  -24.078 1.00 16.40  ? 92   GLN A N   1 
ATOM   670  C CA  . GLN A 1 92  ? -25.887 31.559  -25.168 1.00 16.38  ? 92   GLN A CA  1 
ATOM   671  C C   . GLN A 1 92  ? -27.036 31.310  -26.145 1.00 15.42  ? 92   GLN A C   1 
ATOM   672  O O   . GLN A 1 92  ? -26.816 31.282  -27.351 1.00 15.35  ? 92   GLN A O   1 
ATOM   673  C CB  . GLN A 1 92  ? -25.400 30.248  -24.611 1.00 15.83  ? 92   GLN A CB  1 
ATOM   674  C CG  . GLN A 1 92  ? -24.063 30.387  -23.865 1.00 19.69  ? 92   GLN A CG  1 
ATOM   675  C CD  . GLN A 1 92  ? -23.432 29.028  -23.585 1.00 19.84  ? 92   GLN A CD  1 
ATOM   676  O OE1 . GLN A 1 92  ? -24.096 27.990  -23.639 1.00 18.57  ? 92   GLN A OE1 1 
ATOM   677  N NE2 . GLN A 1 92  ? -22.146 29.037  -23.291 1.00 18.86  ? 92   GLN A NE2 1 
ATOM   678  N N   . THR A 1 93  ? -28.239 31.126  -25.630 1.00 14.59  ? 93   THR A N   1 
ATOM   679  C CA  . THR A 1 93  ? -29.377 30.958  -26.518 1.00 15.42  ? 93   THR A CA  1 
ATOM   680  C C   . THR A 1 93  ? -30.557 31.585  -25.855 1.00 16.01  ? 93   THR A C   1 
ATOM   681  O O   . THR A 1 93  ? -30.484 32.016  -24.705 1.00 14.42  ? 93   THR A O   1 
ATOM   682  C CB  . THR A 1 93  ? -29.765 29.472  -26.772 1.00 16.89  ? 93   THR A CB  1 
ATOM   683  O OG1 . THR A 1 93  ? -30.508 28.972  -25.650 1.00 17.93  ? 93   THR A OG1 1 
ATOM   684  C CG2 . THR A 1 93  ? -28.617 28.570  -27.085 1.00 18.27  ? 93   THR A CG2 1 
ATOM   685  N N   . SER A 1 94  ? -31.679 31.646  -26.569 1.00 15.09  ? 94   SER A N   1 
ATOM   686  C CA  . SER A 1 94  ? -32.885 32.192  -25.966 1.00 16.96  ? 94   SER A CA  1 
ATOM   687  C C   . SER A 1 94  ? -33.326 31.438  -24.716 1.00 16.35  ? 94   SER A C   1 
ATOM   688  O O   . SER A 1 94  ? -34.064 32.007  -23.859 1.00 17.22  ? 94   SER A O   1 
ATOM   689  C CB  . SER A 1 94  ? -34.034 32.109  -26.989 1.00 17.54  ? 94   SER A CB  1 
ATOM   690  O OG  . SER A 1 94  ? -33.761 32.925  -28.104 1.00 24.23  ? 94   SER A OG  1 
ATOM   691  N N   . ASN A 1 95  ? -32.948 30.163  -24.628 1.00 15.00  ? 95   ASN A N   1 
ATOM   692  C CA  . ASN A 1 95  ? -33.378 29.342  -23.521 1.00 16.14  ? 95   ASN A CA  1 
ATOM   693  C C   . ASN A 1 95  ? -32.278 28.823  -22.614 1.00 15.99  ? 95   ASN A C   1 
ATOM   694  O O   . ASN A 1 95  ? -32.548 28.021  -21.737 1.00 16.14  ? 95   ASN A O   1 
ATOM   695  C CB  . ASN A 1 95  ? -34.215 28.162  -24.019 1.00 16.84  ? 95   ASN A CB  1 
ATOM   696  C CG  . ASN A 1 95  ? -35.459 28.610  -24.729 1.00 21.25  ? 95   ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 95  ? -36.555 28.568  -24.163 1.00 29.80  ? 95   ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 95  ? -35.312 29.031  -25.961 1.00 21.91  ? 95   ASN A ND2 1 
ATOM   699  N N   . ARG A 1 96  ? -31.042 29.283  -22.807 1.00 15.69  ? 96   ARG A N   1 
ATOM   700  C CA  . ARG A 1 96  ? -29.927 28.713  -22.043 1.00 15.30  ? 96   ARG A CA  1 
ATOM   701  C C   . ARG A 1 96  ? -28.997 29.849  -21.652 1.00 15.39  ? 96   ARG A C   1 
ATOM   702  O O   . ARG A 1 96  ? -28.532 30.606  -22.515 1.00 16.81  ? 96   ARG A O   1 
ATOM   703  C CB  . ARG A 1 96  ? -29.127 27.684  -22.885 1.00 15.14  ? 96   ARG A CB  1 
ATOM   704  C CG  . ARG A 1 96  ? -27.956 27.095  -22.087 1.00 15.99  ? 96   ARG A CG  1 
ATOM   705  C CD  . ARG A 1 96  ? -27.232 26.022  -22.853 1.00 19.26  ? 96   ARG A CD  1 
ATOM   706  N NE  . ARG A 1 96  ? -26.348 26.496  -23.905 1.00 18.43  ? 96   ARG A NE  1 
ATOM   707  C CZ  . ARG A 1 96  ? -26.409 26.121  -25.179 1.00 21.73  ? 96   ARG A CZ  1 
ATOM   708  N NH1 . ARG A 1 96  ? -27.379 25.302  -25.614 1.00 20.98  ? 96   ARG A NH1 1 
ATOM   709  N NH2 . ARG A 1 96  ? -25.507 26.586  -26.044 1.00 21.58  ? 96   ARG A NH2 1 
ATOM   710  N N   . PHE A 1 97  ? -28.760 29.970  -20.353 1.00 14.79  ? 97   PHE A N   1 
ATOM   711  C CA  . PHE A 1 97  ? -27.878 30.954  -19.812 1.00 14.16  ? 97   PHE A CA  1 
ATOM   712  C C   . PHE A 1 97  ? -26.674 30.196  -19.262 1.00 15.16  ? 97   PHE A C   1 
ATOM   713  O O   . PHE A 1 97  ? -26.817 29.141  -18.663 1.00 15.81  ? 97   PHE A O   1 
ATOM   714  C CB  . PHE A 1 97  ? -28.594 31.741  -18.696 1.00 14.17  ? 97   PHE A CB  1 
ATOM   715  C CG  . PHE A 1 97  ? -27.722 32.776  -18.010 1.00 15.39  ? 97   PHE A CG  1 
ATOM   716  C CD1 . PHE A 1 97  ? -27.147 33.842  -18.747 1.00 13.37  ? 97   PHE A CD1 1 
ATOM   717  C CD2 . PHE A 1 97  ? -27.464 32.682  -16.666 1.00 13.70  ? 97   PHE A CD2 1 
ATOM   718  C CE1 . PHE A 1 97  ? -26.334 34.775  -18.151 1.00 17.66  ? 97   PHE A CE1 1 
ATOM   719  C CE2 . PHE A 1 97  ? -26.647 33.647  -16.039 1.00 16.70  ? 97   PHE A CE2 1 
ATOM   720  C CZ  . PHE A 1 97  ? -26.068 34.667  -16.781 1.00 15.89  ? 97   PHE A CZ  1 
ATOM   721  N N   . HIS A 1 98  ? -25.501 30.785  -19.407 1.00 15.78  ? 98   HIS A N   1 
ATOM   722  C CA  . HIS A 1 98  ? -24.322 30.148  -18.898 1.00 15.89  ? 98   HIS A CA  1 
ATOM   723  C C   . HIS A 1 98  ? -23.621 31.191  -18.020 1.00 15.33  ? 98   HIS A C   1 
ATOM   724  O O   . HIS A 1 98  ? -23.418 32.330  -18.441 1.00 14.97  ? 98   HIS A O   1 
ATOM   725  C CB  . HIS A 1 98  ? -23.500 29.722  -20.102 1.00 16.71  ? 98   HIS A CB  1 
ATOM   726  C CG  . HIS A 1 98  ? -22.120 29.261  -19.769 1.00 18.36  ? 98   HIS A CG  1 
ATOM   727  N ND1 . HIS A 1 98  ? -21.862 28.354  -18.765 1.00 20.51  ? 98   HIS A ND1 1 
ATOM   728  C CD2 . HIS A 1 98  ? -20.917 29.574  -20.319 1.00 19.74  ? 98   HIS A CD2 1 
ATOM   729  C CE1 . HIS A 1 98  ? -20.553 28.129  -18.705 1.00 16.23  ? 98   HIS A CE1 1 
ATOM   730  N NE2 . HIS A 1 98  ? -19.966 28.843  -19.647 1.00 22.45  ? 98   HIS A NE2 1 
ATOM   731  N N   . PHE A 1 99  ? -23.293 30.849  -16.785 1.00 16.18  ? 99   PHE A N   1 
ATOM   732  C CA  . PHE A 1 99  ? -22.356 31.715  -16.038 1.00 17.90  ? 99   PHE A CA  1 
ATOM   733  C C   . PHE A 1 99  ? -21.271 30.917  -15.337 1.00 18.80  ? 99   PHE A C   1 
ATOM   734  O O   . PHE A 1 99  ? -21.491 29.782  -14.919 1.00 19.07  ? 99   PHE A O   1 
ATOM   735  C CB  . PHE A 1 99  ? -23.072 32.672  -15.063 1.00 18.56  ? 99   PHE A CB  1 
ATOM   736  C CG  . PHE A 1 99  ? -23.707 31.999  -13.862 1.00 19.92  ? 99   PHE A CG  1 
ATOM   737  C CD1 . PHE A 1 99  ? -23.027 31.923  -12.653 1.00 21.07  ? 99   PHE A CD1 1 
ATOM   738  C CD2 . PHE A 1 99  ? -24.990 31.468  -13.942 1.00 20.66  ? 99   PHE A CD2 1 
ATOM   739  C CE1 . PHE A 1 99  ? -23.609 31.305  -11.528 1.00 19.26  ? 99   PHE A CE1 1 
ATOM   740  C CE2 . PHE A 1 99  ? -25.611 30.879  -12.807 1.00 22.27  ? 99   PHE A CE2 1 
ATOM   741  C CZ  . PHE A 1 99  ? -24.907 30.790  -11.611 1.00 21.80  ? 99   PHE A CZ  1 
ATOM   742  N N   . LYS A 1 100 ? -20.095 31.508  -15.219 1.00 19.12  ? 100  LYS A N   1 
ATOM   743  C CA  . LYS A 1 100 ? -19.010 30.841  -14.531 1.00 20.68  ? 100  LYS A CA  1 
ATOM   744  C C   . LYS A 1 100 ? -18.218 31.756  -13.616 1.00 20.08  ? 100  LYS A C   1 
ATOM   745  O O   . LYS A 1 100 ? -18.070 32.955  -13.873 1.00 20.27  ? 100  LYS A O   1 
ATOM   746  C CB  . LYS A 1 100 ? -18.130 30.048  -15.493 1.00 21.42  ? 100  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 100 ? -17.239 30.837  -16.377 1.00 24.86  ? 100  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 100 ? -16.445 29.928  -17.329 1.00 29.44  ? 100  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 100 ? -15.686 30.832  -18.324 1.00 35.27  ? 100  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? -14.606 30.121  -19.051 1.00 37.51  ? 100  LYS A NZ  1 
ATOM   751  N N   . LEU A 1 101 ? -17.791 31.189  -12.497 1.00 18.97  ? 101  LEU A N   1 
ATOM   752  C CA  . LEU A 1 101 ? -17.085 31.970  -11.503 1.00 19.87  ? 101  LEU A CA  1 
ATOM   753  C C   . LEU A 1 101 ? -15.721 31.316  -11.479 1.00 19.60  ? 101  LEU A C   1 
ATOM   754  O O   . LEU A 1 101 ? -15.624 30.107  -11.280 1.00 19.63  ? 101  LEU A O   1 
ATOM   755  C CB  . LEU A 1 101 ? -17.758 31.876  -10.133 1.00 19.70  ? 101  LEU A CB  1 
ATOM   756  C CG  . LEU A 1 101 ? -19.172 32.502  -10.079 1.00 19.85  ? 101  LEU A CG  1 
ATOM   757  C CD1 . LEU A 1 101 ? -19.912 31.992  -8.911  1.00 23.18  ? 101  LEU A CD1 1 
ATOM   758  C CD2 . LEU A 1 101 ? -19.113 34.008  -10.014 1.00 20.59  ? 101  LEU A CD2 1 
ATOM   759  N N   . THR A 1 102 ? -14.695 32.099  -11.743 1.00 20.77  ? 102  THR A N   1 
ATOM   760  C CA  . THR A 1 102 ? -13.334 31.583  -11.803 1.00 21.63  ? 102  THR A CA  1 
ATOM   761  C C   . THR A 1 102 ? -12.446 32.447  -10.917 1.00 21.87  ? 102  THR A C   1 
ATOM   762  O O   . THR A 1 102 ? -12.882 33.475  -10.416 1.00 21.19  ? 102  THR A O   1 
ATOM   763  C CB  . THR A 1 102 ? -12.812 31.597  -13.267 1.00 22.31  ? 102  THR A CB  1 
ATOM   764  O OG1 . THR A 1 102 ? -12.986 32.904  -13.828 1.00 23.06  ? 102  THR A OG1 1 
ATOM   765  C CG2 . THR A 1 102 ? -13.598 30.608  -14.129 1.00 23.71  ? 102  THR A CG2 1 
ATOM   766  N N   . ASP A 1 103 ? -11.202 32.029  -10.729 1.00 22.47  ? 103  ASP A N   1 
ATOM   767  C CA  . ASP A 1 103 ? -10.197 32.841  -10.044 1.00 24.27  ? 103  ASP A CA  1 
ATOM   768  C C   . ASP A 1 103 ? -9.632  33.821  -11.071 1.00 25.18  ? 103  ASP A C   1 
ATOM   769  O O   . ASP A 1 103 ? -9.046  33.426  -12.071 1.00 24.53  ? 103  ASP A O   1 
ATOM   770  C CB  . ASP A 1 103 ? -9.097  31.936  -9.477  1.00 23.09  ? 103  ASP A CB  1 
ATOM   771  C CG  . ASP A 1 103 ? -8.050  32.701  -8.631  1.00 28.13  ? 103  ASP A CG  1 
ATOM   772  O OD1 . ASP A 1 103 ? -7.912  33.941  -8.750  1.00 28.33  ? 103  ASP A OD1 1 
ATOM   773  O OD2 . ASP A 1 103 ? -7.335  32.024  -7.850  1.00 30.17  ? 103  ASP A OD2 1 
ATOM   774  N N   . GLN A 1 104 ? -9.831  35.099  -10.818 1.00 27.79  ? 104  GLN A N   1 
ATOM   775  C CA  . GLN A 1 104 ? -9.464  36.155  -11.757 1.00 32.04  ? 104  GLN A CA  1 
ATOM   776  C C   . GLN A 1 104 ? -7.988  36.047  -12.127 1.00 32.52  ? 104  GLN A C   1 
ATOM   777  O O   . GLN A 1 104 ? -7.606  36.345  -13.262 1.00 33.27  ? 104  GLN A O   1 
ATOM   778  C CB  . GLN A 1 104 ? -9.758  37.487  -11.066 1.00 31.65  ? 104  GLN A CB  1 
ATOM   779  C CG  . GLN A 1 104 ? -10.070 38.706  -11.893 1.00 34.60  ? 104  GLN A CG  1 
ATOM   780  C CD  . GLN A 1 104 ? -10.423 39.857  -10.945 1.00 35.27  ? 104  GLN A CD  1 
ATOM   781  O OE1 . GLN A 1 104 ? -11.551 39.937  -10.421 1.00 40.66  ? 104  GLN A OE1 1 
ATOM   782  N NE2 . GLN A 1 104 ? -9.445  40.701  -10.656 1.00 37.91  ? 104  GLN A NE2 1 
ATOM   783  N N   . THR A 1 105 ? -7.175  35.569  -11.173 1.00 34.35  ? 105  THR A N   1 
ATOM   784  C CA  . THR A 1 105 ? -5.709  35.614  -11.262 1.00 36.31  ? 105  THR A CA  1 
ATOM   785  C C   . THR A 1 105 ? -5.036  34.256  -11.471 1.00 36.14  ? 105  THR A C   1 
ATOM   786  O O   . THR A 1 105 ? -3.831  34.207  -11.671 1.00 37.43  ? 105  THR A O   1 
ATOM   787  C CB  . THR A 1 105 ? -5.071  36.248  -9.989  1.00 36.68  ? 105  THR A CB  1 
ATOM   788  O OG1 . THR A 1 105 ? -5.004  35.263  -8.951  1.00 40.24  ? 105  THR A OG1 1 
ATOM   789  C CG2 . THR A 1 105 ? -5.879  37.436  -9.485  1.00 37.98  ? 105  THR A CG2 1 
ATOM   790  N N   . ASN A 1 106 ? -5.786  33.154  -11.401 1.00 35.37  ? 106  ASN A N   1 
ATOM   791  C CA  . ASN A 1 106 ? -5.217  31.831  -11.673 1.00 34.76  ? 106  ASN A CA  1 
ATOM   792  C C   . ASN A 1 106 ? -6.145  30.919  -12.471 1.00 33.04  ? 106  ASN A C   1 
ATOM   793  O O   . ASN A 1 106 ? -7.354  30.888  -12.247 1.00 32.67  ? 106  ASN A O   1 
ATOM   794  C CB  . ASN A 1 106 ? -4.843  31.114  -10.375 1.00 35.94  ? 106  ASN A CB  1 
ATOM   795  C CG  . ASN A 1 106 ? -3.808  31.874  -9.551  1.00 39.47  ? 106  ASN A CG  1 
ATOM   796  O OD1 . ASN A 1 106 ? -4.125  32.399  -8.473  1.00 43.75  ? 106  ASN A OD1 1 
ATOM   797  N ND2 . ASN A 1 106 ? -2.567  31.924  -10.039 1.00 42.39  ? 106  ASN A ND2 1 
ATOM   798  N N   . ASN A 1 107 ? -5.565  30.165  -13.385 1.00 31.06  ? 107  ASN A N   1 
ATOM   799  C CA  . ASN A 1 107 ? -6.281  29.112  -14.064 1.00 29.88  ? 107  ASN A CA  1 
ATOM   800  C C   . ASN A 1 107 ? -6.602  27.983  -13.086 1.00 27.91  ? 107  ASN A C   1 
ATOM   801  O O   . ASN A 1 107 ? -5.753  27.580  -12.306 1.00 28.54  ? 107  ASN A O   1 
ATOM   802  C CB  . ASN A 1 107 ? -5.458  28.589  -15.249 1.00 30.72  ? 107  ASN A CB  1 
ATOM   803  C CG  . ASN A 1 107 ? -5.359  29.615  -16.392 1.00 34.58  ? 107  ASN A CG  1 
ATOM   804  O OD1 . ASN A 1 107 ? -4.276  29.866  -16.910 1.00 41.64  ? 107  ASN A OD1 1 
ATOM   805  N ND2 . ASN A 1 107 ? -6.490  30.215  -16.773 1.00 37.06  ? 107  ASN A ND2 1 
ATOM   806  N N   . ARG A 1 108 ? -7.842  27.508  -13.099 1.00 24.10  ? 108  ARG A N   1 
ATOM   807  C CA  . ARG A 1 108 ? -8.232  26.385  -12.255 1.00 21.23  ? 108  ARG A CA  1 
ATOM   808  C C   . ARG A 1 108 ? -8.741  25.239  -13.139 1.00 19.78  ? 108  ARG A C   1 
ATOM   809  O O   . ARG A 1 108 ? -8.995  25.435  -14.322 1.00 18.91  ? 108  ARG A O   1 
ATOM   810  C CB  . ARG A 1 108 ? -9.306  26.803  -11.238 1.00 21.13  ? 108  ARG A CB  1 
ATOM   811  C CG  . ARG A 1 108 ? -8.852  27.854  -10.251 1.00 18.62  ? 108  ARG A CG  1 
ATOM   812  C CD  . ARG A 1 108 ? -9.971  28.282  -9.345  1.00 17.17  ? 108  ARG A CD  1 
ATOM   813  N NE  . ARG A 1 108 ? -10.585 27.128  -8.683  1.00 17.24  ? 108  ARG A NE  1 
ATOM   814  C CZ  . ARG A 1 108 ? -10.087 26.510  -7.615  1.00 21.88  ? 108  ARG A CZ  1 
ATOM   815  N NH1 . ARG A 1 108 ? -8.965  26.955  -7.013  1.00 17.92  ? 108  ARG A NH1 1 
ATOM   816  N NH2 . ARG A 1 108 ? -10.727 25.450  -7.121  1.00 18.75  ? 108  ARG A NH2 1 
ATOM   817  N N   . PHE A 1 109 ? -8.889  24.041  -12.566 1.00 18.62  ? 109  PHE A N   1 
ATOM   818  C CA  . PHE A 1 109 ? -9.268  22.896  -13.359 1.00 17.33  ? 109  PHE A CA  1 
ATOM   819  C C   . PHE A 1 109 ? -10.703 23.125  -13.899 1.00 17.46  ? 109  PHE A C   1 
ATOM   820  O O   . PHE A 1 109 ? -11.575 23.509  -13.130 1.00 16.75  ? 109  PHE A O   1 
ATOM   821  C CB  . PHE A 1 109 ? -9.249  21.601  -12.525 1.00 17.79  ? 109  PHE A CB  1 
ATOM   822  C CG  . PHE A 1 109 ? -9.856  20.440  -13.256 1.00 16.49  ? 109  PHE A CG  1 
ATOM   823  C CD1 . PHE A 1 109 ? -9.104  19.736  -14.192 1.00 19.95  ? 109  PHE A CD1 1 
ATOM   824  C CD2 . PHE A 1 109 ? -11.213 20.135  -13.095 1.00 17.09  ? 109  PHE A CD2 1 
ATOM   825  C CE1 . PHE A 1 109 ? -9.677  18.697  -14.921 1.00 19.14  ? 109  PHE A CE1 1 
ATOM   826  C CE2 . PHE A 1 109 ? -11.806 19.104  -13.819 1.00 16.69  ? 109  PHE A CE2 1 
ATOM   827  C CZ  . PHE A 1 109 ? -11.025 18.372  -14.721 1.00 17.41  ? 109  PHE A CZ  1 
ATOM   828  N N   . GLU A 1 110 ? -10.910 22.912  -15.194 1.00 18.21  ? 110  GLU A N   1 
ATOM   829  C CA  . GLU A 1 110 ? -12.254 23.001  -15.798 1.00 19.00  ? 110  GLU A CA  1 
ATOM   830  C C   . GLU A 1 110 ? -12.471 21.699  -16.516 1.00 19.64  ? 110  GLU A C   1 
ATOM   831  O O   . GLU A 1 110 ? -11.522 21.187  -17.116 1.00 19.53  ? 110  GLU A O   1 
ATOM   832  C CB  . GLU A 1 110 ? -12.266 24.180  -16.773 1.00 19.98  ? 110  GLU A CB  1 
ATOM   833  C CG  . GLU A 1 110 ? -12.054 25.496  -16.046 1.00 22.13  ? 110  GLU A CG  1 
ATOM   834  C CD  . GLU A 1 110 ? -12.329 26.715  -16.889 1.00 32.09  ? 110  GLU A CD  1 
ATOM   835  O OE1 . GLU A 1 110 ? -13.388 26.762  -17.578 1.00 36.51  ? 110  GLU A OE1 1 
ATOM   836  O OE2 . GLU A 1 110 ? -11.505 27.650  -16.805 1.00 32.36  ? 110  GLU A OE2 1 
ATOM   837  N N   . VAL A 1 111 ? -13.692 21.141  -16.466 1.00 18.55  ? 111  VAL A N   1 
ATOM   838  C CA  . VAL A 1 111 ? -13.955 19.826  -17.053 1.00 17.79  ? 111  VAL A CA  1 
ATOM   839  C C   . VAL A 1 111 ? -13.673 19.845  -18.550 1.00 18.89  ? 111  VAL A C   1 
ATOM   840  O O   . VAL A 1 111 ? -14.261 20.646  -19.278 1.00 19.29  ? 111  VAL A O   1 
ATOM   841  C CB  . VAL A 1 111 ? -15.427 19.385  -16.815 1.00 18.20  ? 111  VAL A CB  1 
ATOM   842  C CG1 . VAL A 1 111 ? -15.722 18.058  -17.505 1.00 16.78  ? 111  VAL A CG1 1 
ATOM   843  C CG2 . VAL A 1 111 ? -15.716 19.310  -15.322 1.00 17.85  ? 111  VAL A CG2 1 
ATOM   844  N N   . PRO A 1 112 ? -12.787 18.958  -19.041 1.00 18.54  ? 112  PRO A N   1 
ATOM   845  C CA  . PRO A 1 112 ? -12.532 18.936  -20.477 1.00 20.02  ? 112  PRO A CA  1 
ATOM   846  C C   . PRO A 1 112 ? -13.585 18.115  -21.226 1.00 20.24  ? 112  PRO A C   1 
ATOM   847  O O   . PRO A 1 112 ? -13.285 17.077  -21.807 1.00 21.17  ? 112  PRO A O   1 
ATOM   848  C CB  . PRO A 1 112 ? -11.161 18.270  -20.585 1.00 20.22  ? 112  PRO A CB  1 
ATOM   849  C CG  . PRO A 1 112 ? -11.021 17.486  -19.392 1.00 20.06  ? 112  PRO A CG  1 
ATOM   850  C CD  . PRO A 1 112 ? -11.941 17.990  -18.314 1.00 19.87  ? 112  PRO A CD  1 
ATOM   851  N N   . HIS A 1 113 ? -14.823 18.572  -21.178 1.00 20.29  ? 113  HIS A N   1 
ATOM   852  C CA  . HIS A 1 113 ? -15.902 17.803  -21.780 1.00 19.59  ? 113  HIS A CA  1 
ATOM   853  C C   . HIS A 1 113 ? -15.700 17.531  -23.273 1.00 20.03  ? 113  HIS A C   1 
ATOM   854  O O   . HIS A 1 113 ? -15.178 18.379  -23.993 1.00 19.60  ? 113  HIS A O   1 
ATOM   855  C CB  . HIS A 1 113 ? -17.208 18.524  -21.559 1.00 19.59  ? 113  HIS A CB  1 
ATOM   856  C CG  . HIS A 1 113 ? -18.371 17.604  -21.571 1.00 21.15  ? 113  HIS A CG  1 
ATOM   857  N ND1 . HIS A 1 113 ? -19.188 17.459  -22.673 1.00 20.44  ? 113  HIS A ND1 1 
ATOM   858  C CD2 . HIS A 1 113 ? -18.827 16.731  -20.640 1.00 21.37  ? 113  HIS A CD2 1 
ATOM   859  C CE1 . HIS A 1 113 ? -20.131 16.572  -22.397 1.00 19.45  ? 113  HIS A CE1 1 
ATOM   860  N NE2 . HIS A 1 113 ? -19.930 16.111  -21.175 1.00 19.08  ? 113  HIS A NE2 1 
ATOM   861  N N   . GLU A 1 114 ? -16.126 16.355  -23.734 1.00 20.07  ? 114  GLU A N   1 
ATOM   862  C CA  . GLU A 1 114 ? -15.909 15.951  -25.110 1.00 21.24  ? 114  GLU A CA  1 
ATOM   863  C C   . GLU A 1 114 ? -16.936 16.623  -26.012 1.00 21.55  ? 114  GLU A C   1 
ATOM   864  O O   . GLU A 1 114 ? -16.638 16.894  -27.155 1.00 22.11  ? 114  GLU A O   1 
ATOM   865  C CB  . GLU A 1 114 ? -15.973 14.430  -25.248 1.00 21.90  ? 114  GLU A CB  1 
ATOM   866  C CG  . GLU A 1 114 ? -15.755 13.829  -26.652 1.00 24.87  ? 114  GLU A CG  1 
ATOM   867  C CD  . GLU A 1 114 ? -16.982 13.929  -27.575 1.00 28.93  ? 114  GLU A CD  1 
ATOM   868  O OE1 . GLU A 1 114 ? -18.134 14.081  -27.104 1.00 25.62  ? 114  GLU A OE1 1 
ATOM   869  O OE2 . GLU A 1 114 ? -16.788 13.849  -28.796 1.00 31.94  ? 114  GLU A OE2 1 
ATOM   870  N N   . HIS A 1 115 ? -18.138 16.890  -25.513 1.00 20.20  ? 115  HIS A N   1 
ATOM   871  C CA  . HIS A 1 115 ? -19.153 17.482  -26.388 1.00 20.97  ? 115  HIS A CA  1 
ATOM   872  C C   . HIS A 1 115 ? -19.218 19.013  -26.271 1.00 21.24  ? 115  HIS A C   1 
ATOM   873  O O   . HIS A 1 115 ? -19.293 19.733  -27.279 1.00 21.42  ? 115  HIS A O   1 
ATOM   874  C CB  . HIS A 1 115 ? -20.527 16.862  -26.089 1.00 20.04  ? 115  HIS A CB  1 
ATOM   875  C CG  . HIS A 1 115 ? -21.593 17.258  -27.061 1.00 21.67  ? 115  HIS A CG  1 
ATOM   876  N ND1 . HIS A 1 115 ? -21.709 16.677  -28.306 1.00 23.40  ? 115  HIS A ND1 1 
ATOM   877  C CD2 . HIS A 1 115 ? -22.595 18.165  -26.970 1.00 19.95  ? 115  HIS A CD2 1 
ATOM   878  C CE1 . HIS A 1 115 ? -22.733 17.215  -28.948 1.00 23.19  ? 115  HIS A CE1 1 
ATOM   879  N NE2 . HIS A 1 115 ? -23.287 18.125  -28.160 1.00 21.04  ? 115  HIS A NE2 1 
ATOM   880  N N   . VAL A 1 116 ? -19.269 19.511  -25.039 1.00 21.22  ? 116  VAL A N   1 
ATOM   881  C CA  . VAL A 1 116 ? -19.506 20.917  -24.788 1.00 21.23  ? 116  VAL A CA  1 
ATOM   882  C C   . VAL A 1 116 ? -18.312 21.698  -25.315 1.00 23.43  ? 116  VAL A C   1 
ATOM   883  O O   . VAL A 1 116 ? -17.168 21.286  -25.117 1.00 22.94  ? 116  VAL A O   1 
ATOM   884  C CB  . VAL A 1 116 ? -19.737 21.175  -23.297 1.00 21.30  ? 116  VAL A CB  1 
ATOM   885  C CG1 . VAL A 1 116 ? -19.734 22.679  -22.954 1.00 19.51  ? 116  VAL A CG1 1 
ATOM   886  C CG2 . VAL A 1 116 ? -21.044 20.504  -22.855 1.00 18.82  ? 116  VAL A CG2 1 
ATOM   887  N N   . GLN A 1 117 ? -18.602 22.775  -26.037 1.00 24.64  ? 117  GLN A N   1 
ATOM   888  C CA  . GLN A 1 117 ? -17.569 23.667  -26.572 1.00 28.39  ? 117  GLN A CA  1 
ATOM   889  C C   . GLN A 1 117 ? -17.626 25.010  -25.908 1.00 28.32  ? 117  GLN A C   1 
ATOM   890  O O   . GLN A 1 117 ? -18.675 25.406  -25.401 1.00 28.44  ? 117  GLN A O   1 
ATOM   891  C CB  . GLN A 1 117 ? -17.778 23.875  -28.055 1.00 28.33  ? 117  GLN A CB  1 
ATOM   892  C CG  . GLN A 1 117 ? -17.492 22.667  -28.894 1.00 33.26  ? 117  GLN A CG  1 
ATOM   893  C CD  . GLN A 1 117 ? -17.330 23.092  -30.336 1.00 41.26  ? 117  GLN A CD  1 
ATOM   894  O OE1 . GLN A 1 117 ? -18.302 23.494  -30.982 1.00 45.47  ? 117  GLN A OE1 1 
ATOM   895  N NE2 . GLN A 1 117 ? -16.089 23.074  -30.834 1.00 42.14  ? 117  GLN A NE2 1 
ATOM   896  N N   . SER A 1 118 ? -16.501 25.722  -25.923 1.00 29.74  ? 118  SER A N   1 
ATOM   897  C CA  . SER A 1 118 ? -16.526 27.100  -25.465 1.00 30.86  ? 118  SER A CA  1 
ATOM   898  C C   . SER A 1 118 ? -17.351 27.909  -26.451 1.00 30.24  ? 118  SER A C   1 
ATOM   899  O O   . SER A 1 118 ? -17.402 27.631  -27.657 1.00 28.81  ? 118  SER A O   1 
ATOM   900  C CB  . SER A 1 118 ? -15.124 27.677  -25.271 1.00 31.37  ? 118  SER A CB  1 
ATOM   901  O OG  . SER A 1 118 ? -14.453 27.627  -26.498 1.00 35.55  ? 118  SER A OG  1 
ATOM   902  N N   . PHE A 1 119 ? -18.060 28.866  -25.894 1.00 30.67  ? 119  PHE A N   1 
ATOM   903  C CA  . PHE A 1 119 ? -18.892 29.740  -26.651 1.00 32.15  ? 119  PHE A CA  1 
ATOM   904  C C   . PHE A 1 119 ? -18.073 30.846  -27.292 1.00 33.43  ? 119  PHE A C   1 
ATOM   905  O O   . PHE A 1 119 ? -17.263 31.497  -26.645 1.00 33.48  ? 119  PHE A O   1 
ATOM   906  C CB  . PHE A 1 119 ? -19.920 30.338  -25.708 1.00 31.61  ? 119  PHE A CB  1 
ATOM   907  C CG  . PHE A 1 119 ? -20.955 31.133  -26.384 1.00 30.58  ? 119  PHE A CG  1 
ATOM   908  C CD1 . PHE A 1 119 ? -21.882 30.525  -27.223 1.00 30.28  ? 119  PHE A CD1 1 
ATOM   909  C CD2 . PHE A 1 119 ? -21.028 32.493  -26.186 1.00 30.03  ? 119  PHE A CD2 1 
ATOM   910  C CE1 . PHE A 1 119 ? -22.861 31.270  -27.853 1.00 30.12  ? 119  PHE A CE1 1 
ATOM   911  C CE2 . PHE A 1 119 ? -22.018 33.254  -26.827 1.00 30.94  ? 119  PHE A CE2 1 
ATOM   912  C CZ  . PHE A 1 119 ? -22.934 32.632  -27.656 1.00 30.56  ? 119  PHE A CZ  1 
ATOM   913  N N   . SER A 1 120 ? -18.284 31.047  -28.580 1.00 35.30  ? 120  SER A N   1 
ATOM   914  C CA  . SER A 1 120 ? -17.765 32.236  -29.264 1.00 36.88  ? 120  SER A CA  1 
ATOM   915  C C   . SER A 1 120 ? -18.976 32.814  -29.961 1.00 37.33  ? 120  SER A C   1 
ATOM   916  O O   . SER A 1 120 ? -19.939 32.097  -30.261 1.00 38.53  ? 120  SER A O   1 
ATOM   917  C CB  . SER A 1 120 ? -16.679 31.847  -30.272 1.00 37.23  ? 120  SER A CB  1 
ATOM   918  O OG  . SER A 1 120 ? -17.121 30.740  -31.051 1.00 40.07  ? 120  SER A OG  1 
ATOM   919  N N   . GLY A 1 121 ? -18.990 34.108  -30.198 1.00 37.51  ? 121  GLY A N   1 
ATOM   920  C CA  . GLY A 1 121 ? -20.213 34.663  -30.780 1.00 36.76  ? 121  GLY A CA  1 
ATOM   921  C C   . GLY A 1 121 ? -21.014 35.485  -29.792 1.00 35.43  ? 121  GLY A C   1 
ATOM   922  O O   . GLY A 1 121 ? -20.542 35.820  -28.708 1.00 34.66  ? 121  GLY A O   1 
ATOM   923  N N   . ASN A 1 122 ? -22.235 35.822  -30.178 1.00 33.93  ? 122  ASN A N   1 
ATOM   924  C CA  . ASN A 1 122 ? -22.860 36.973  -29.584 1.00 31.91  ? 122  ASN A CA  1 
ATOM   925  C C   . ASN A 1 122 ? -24.057 36.585  -28.767 1.00 29.66  ? 122  ASN A C   1 
ATOM   926  O O   . ASN A 1 122 ? -24.697 35.593  -29.065 1.00 28.92  ? 122  ASN A O   1 
ATOM   927  C CB  . ASN A 1 122 ? -23.276 37.941  -30.693 1.00 33.11  ? 122  ASN A CB  1 
ATOM   928  C CG  . ASN A 1 122 ? -22.095 38.424  -31.511 1.00 35.62  ? 122  ASN A CG  1 
ATOM   929  O OD1 . ASN A 1 122 ? -21.013 38.687  -30.978 1.00 37.66  ? 122  ASN A OD1 1 
ATOM   930  N ND2 . ASN A 1 122 ? -22.293 38.524  -32.814 1.00 36.47  ? 122  ASN A ND2 1 
ATOM   931  N N   . ALA A 1 123 ? -24.365 37.402  -27.774 1.00 27.43  ? 123  ALA A N   1 
ATOM   932  C CA  . ALA A 1 123 ? -25.541 37.216  -26.938 1.00 26.25  ? 123  ALA A CA  1 
ATOM   933  C C   . ALA A 1 123 ? -26.767 36.938  -27.820 1.00 26.54  ? 123  ALA A C   1 
ATOM   934  O O   . ALA A 1 123 ? -26.926 37.543  -28.896 1.00 25.51  ? 123  ALA A O   1 
ATOM   935  C CB  . ALA A 1 123 ? -25.750 38.428  -26.084 1.00 26.13  ? 123  ALA A CB  1 
ATOM   936  N N   . ALA A 1 124 ? -27.630 36.026  -27.381 1.00 25.82  ? 124  ALA A N   1 
ATOM   937  C CA  . ALA A 1 124 ? -28.774 35.636  -28.187 1.00 25.54  ? 124  ALA A CA  1 
ATOM   938  C C   . ALA A 1 124 ? -29.847 36.709  -28.130 1.00 26.20  ? 124  ALA A C   1 
ATOM   939  O O   . ALA A 1 124 ? -29.943 37.431  -27.157 1.00 26.60  ? 124  ALA A O   1 
ATOM   940  C CB  . ALA A 1 124 ? -29.333 34.321  -27.720 1.00 24.93  ? 124  ALA A CB  1 
ATOM   941  N N   . ALA A 1 125 ? -30.637 36.794  -29.188 1.00 26.88  ? 125  ALA A N   1 
ATOM   942  C CA  . ALA A 1 125 ? -31.797 37.671  -29.257 1.00 28.27  ? 125  ALA A CA  1 
ATOM   943  C C   . ALA A 1 125 ? -33.014 36.963  -28.641 1.00 28.53  ? 125  ALA A C   1 
ATOM   944  O O   . ALA A 1 125 ? -33.037 35.722  -28.523 1.00 30.11  ? 125  ALA A O   1 
ATOM   945  C CB  . ALA A 1 125 ? -32.071 38.032  -30.744 1.00 28.72  ? 125  ALA A CB  1 
ATOM   946  N N   . SER A 1 126 ? -34.024 37.730  -28.234 1.00 28.37  ? 126  SER A N   1 
ATOM   947  C CA  . SER A 1 126 ? -35.305 37.155  -27.812 1.00 28.04  ? 126  SER A CA  1 
ATOM   948  C C   . SER A 1 126 ? -35.146 36.197  -26.644 1.00 26.75  ? 126  SER A C   1 
ATOM   949  O O   . SER A 1 126 ? -35.614 35.050  -26.700 1.00 27.41  ? 126  SER A O   1 
ATOM   950  C CB  . SER A 1 126 ? -35.991 36.438  -28.976 1.00 28.07  ? 126  SER A CB  1 
ATOM   951  O OG  . SER A 1 126 ? -36.153 37.325  -30.077 1.00 32.06  ? 126  SER A OG  1 
ATOM   952  N N   . LEU A 1 127 ? -34.488 36.656  -25.583 1.00 24.70  ? 127  LEU A N   1 
ATOM   953  C CA  . LEU A 1 127 ? -34.256 35.792  -24.424 1.00 22.70  ? 127  LEU A CA  1 
ATOM   954  C C   . LEU A 1 127 ? -35.575 35.490  -23.725 1.00 22.50  ? 127  LEU A C   1 
ATOM   955  O O   . LEU A 1 127 ? -36.416 36.371  -23.602 1.00 23.22  ? 127  LEU A O   1 
ATOM   956  C CB  . LEU A 1 127 ? -33.336 36.484  -23.450 1.00 22.61  ? 127  LEU A CB  1 
ATOM   957  C CG  . LEU A 1 127 ? -31.966 36.864  -24.032 1.00 19.91  ? 127  LEU A CG  1 
ATOM   958  C CD1 . LEU A 1 127 ? -31.168 37.605  -22.969 1.00 25.73  ? 127  LEU A CD1 1 
ATOM   959  C CD2 . LEU A 1 127 ? -31.253 35.643  -24.506 1.00 19.77  ? 127  LEU A CD2 1 
ATOM   960  N N   . THR A 1 128 ? -35.748 34.262  -23.249 1.00 21.04  ? 128  THR A N   1 
ATOM   961  C CA  . THR A 1 128 ? -36.921 33.926  -22.421 1.00 20.46  ? 128  THR A CA  1 
ATOM   962  C C   . THR A 1 128 ? -36.646 34.257  -20.961 1.00 19.31  ? 128  THR A C   1 
ATOM   963  O O   . THR A 1 128 ? -37.485 34.103  -20.097 1.00 16.98  ? 128  THR A O   1 
ATOM   964  C CB  . THR A 1 128 ? -37.279 32.437  -22.561 1.00 21.00  ? 128  THR A CB  1 
ATOM   965  O OG1 . THR A 1 128 ? -36.197 31.639  -22.081 1.00 22.69  ? 128  THR A OG1 1 
ATOM   966  C CG2 . THR A 1 128 ? -37.503 32.098  -23.991 1.00 21.34  ? 128  THR A CG2 1 
ATOM   967  N N   . TYR A 1 129 ? -35.413 34.672  -20.658 1.00 18.16  ? 129  TYR A N   1 
ATOM   968  C CA  . TYR A 1 129 ? -35.052 34.942  -19.271 1.00 18.41  ? 129  TYR A CA  1 
ATOM   969  C C   . TYR A 1 129 ? -34.389 36.337  -19.122 1.00 18.32  ? 129  TYR A C   1 
ATOM   970  O O   . TYR A 1 129 ? -33.955 36.943  -20.119 1.00 17.14  ? 129  TYR A O   1 
ATOM   971  C CB  . TYR A 1 129 ? -34.093 33.868  -18.742 1.00 18.04  ? 129  TYR A CB  1 
ATOM   972  C CG  . TYR A 1 129 ? -32.860 33.738  -19.599 1.00 16.77  ? 129  TYR A CG  1 
ATOM   973  C CD1 . TYR A 1 129 ? -31.709 34.477  -19.316 1.00 18.45  ? 129  TYR A CD1 1 
ATOM   974  C CD2 . TYR A 1 129 ? -32.841 32.880  -20.694 1.00 16.88  ? 129  TYR A CD2 1 
ATOM   975  C CE1 . TYR A 1 129 ? -30.580 34.382  -20.145 1.00 14.58  ? 129  TYR A CE1 1 
ATOM   976  C CE2 . TYR A 1 129 ? -31.696 32.765  -21.517 1.00 15.34  ? 129  TYR A CE2 1 
ATOM   977  C CZ  . TYR A 1 129 ? -30.586 33.506  -21.217 1.00 15.96  ? 129  TYR A CZ  1 
ATOM   978  O OH  . TYR A 1 129 ? -29.461 33.377  -22.036 1.00 19.66  ? 129  TYR A OH  1 
ATOM   979  N N   . GLN A 1 130 ? -34.290 36.805  -17.879 1.00 18.13  ? 130  GLN A N   1 
ATOM   980  C CA  . GLN A 1 130 ? -33.529 38.016  -17.569 1.00 20.81  ? 130  GLN A CA  1 
ATOM   981  C C   . GLN A 1 130 ? -32.552 37.693  -16.443 1.00 19.81  ? 130  GLN A C   1 
ATOM   982  O O   . GLN A 1 130 ? -32.838 36.862  -15.592 1.00 21.00  ? 130  GLN A O   1 
ATOM   983  C CB  . GLN A 1 130 ? -34.481 39.117  -17.124 1.00 21.22  ? 130  GLN A CB  1 
ATOM   984  C CG  . GLN A 1 130 ? -33.926 40.513  -17.080 1.00 27.53  ? 130  GLN A CG  1 
ATOM   985  C CD  . GLN A 1 130 ? -35.012 41.517  -16.743 1.00 35.39  ? 130  GLN A CD  1 
ATOM   986  O OE1 . GLN A 1 130 ? -36.212 41.265  -16.988 1.00 37.53  ? 130  GLN A OE1 1 
ATOM   987  N NE2 . GLN A 1 130 ? -34.612 42.659  -16.176 1.00 37.65  ? 130  GLN A NE2 1 
ATOM   988  N N   . VAL A 1 131 ? -31.410 38.348  -16.443 1.00 19.10  ? 131  VAL A N   1 
ATOM   989  C CA  . VAL A 1 131 ? -30.403 38.130  -15.413 1.00 18.50  ? 131  VAL A CA  1 
ATOM   990  C C   . VAL A 1 131 ? -30.263 39.449  -14.652 1.00 20.08  ? 131  VAL A C   1 
ATOM   991  O O   . VAL A 1 131 ? -30.328 40.539  -15.246 1.00 19.34  ? 131  VAL A O   1 
ATOM   992  C CB  . VAL A 1 131 ? -29.105 37.695  -16.043 1.00 17.37  ? 131  VAL A CB  1 
ATOM   993  C CG1 . VAL A 1 131 ? -27.966 37.487  -14.957 1.00 17.22  ? 131  VAL A CG1 1 
ATOM   994  C CG2 . VAL A 1 131 ? -29.374 36.393  -16.859 1.00 18.50  ? 131  VAL A CG2 1 
ATOM   995  N N   . GLU A 1 132 ? -30.128 39.350  -13.337 1.00 19.88  ? 132  GLU A N   1 
ATOM   996  C CA  . GLU A 1 132 ? -29.993 40.519  -12.487 1.00 21.88  ? 132  GLU A CA  1 
ATOM   997  C C   . GLU A 1 132 ? -28.832 40.241  -11.528 1.00 21.58  ? 132  GLU A C   1 
ATOM   998  O O   . GLU A 1 132 ? -28.762 39.172  -10.906 1.00 20.97  ? 132  GLU A O   1 
ATOM   999  C CB  . GLU A 1 132 ? -31.314 40.760  -11.756 1.00 24.05  ? 132  GLU A CB  1 
ATOM   1000 C CG  . GLU A 1 132 ? -31.220 41.549  -10.478 1.00 32.44  ? 132  GLU A CG  1 
ATOM   1001 C CD  . GLU A 1 132 ? -31.487 43.050  -10.631 1.00 41.26  ? 132  GLU A CD  1 
ATOM   1002 O OE1 . GLU A 1 132 ? -31.788 43.529  -11.774 1.00 45.43  ? 132  GLU A OE1 1 
ATOM   1003 O OE2 . GLU A 1 132 ? -31.408 43.739  -9.574  1.00 42.86  ? 132  GLU A OE2 1 
ATOM   1004 N N   . ILE A 1 133 ? -27.927 41.196  -11.419 1.00 19.03  ? 133  ILE A N   1 
ATOM   1005 C CA  . ILE A 1 133 ? -26.775 41.065  -10.522 1.00 19.05  ? 133  ILE A CA  1 
ATOM   1006 C C   . ILE A 1 133 ? -26.916 42.113  -9.422  1.00 19.04  ? 133  ILE A C   1 
ATOM   1007 O O   . ILE A 1 133 ? -27.149 43.293  -9.715  1.00 17.89  ? 133  ILE A O   1 
ATOM   1008 C CB  . ILE A 1 133 ? -25.483 41.294  -11.317 1.00 18.79  ? 133  ILE A CB  1 
ATOM   1009 C CG1 . ILE A 1 133 ? -25.382 40.323  -12.506 1.00 19.00  ? 133  ILE A CG1 1 
ATOM   1010 C CG2 . ILE A 1 133 ? -24.169 41.226  -10.404 1.00 18.13  ? 133  ILE A CG2 1 
ATOM   1011 C CD1 . ILE A 1 133 ? -25.193 38.828  -12.114 1.00 22.71  ? 133  ILE A CD1 1 
ATOM   1012 N N   . SER A 1 134 ? -26.813 41.678  -8.163  1.00 19.25  ? 134  SER A N   1 
ATOM   1013 C CA  . SER A 1 134 ? -26.719 42.566  -7.017  1.00 21.89  ? 134  SER A CA  1 
ATOM   1014 C C   . SER A 1 134 ? -25.259 42.634  -6.649  1.00 23.46  ? 134  SER A C   1 
ATOM   1015 O O   . SER A 1 134 ? -24.567 41.648  -6.760  1.00 22.79  ? 134  SER A O   1 
ATOM   1016 C CB  . SER A 1 134 ? -27.529 42.029  -5.850  1.00 22.23  ? 134  SER A CB  1 
ATOM   1017 O OG  . SER A 1 134 ? -28.929 42.145  -6.174  1.00 27.04  ? 134  SER A OG  1 
ATOM   1018 N N   . ARG A 1 135 ? -24.816 43.794  -6.186  1.00 26.03  ? 135  ARG A N   1 
ATOM   1019 C CA  . ARG A 1 135 ? -23.416 44.077  -5.986  1.00 28.15  ? 135  ARG A CA  1 
ATOM   1020 C C   . ARG A 1 135 ? -22.970 43.880  -4.554  1.00 28.29  ? 135  ARG A C   1 
ATOM   1021 O O   . ARG A 1 135 ? -21.850 43.465  -4.295  1.00 28.39  ? 135  ARG A O   1 
ATOM   1022 C CB  . ARG A 1 135 ? -23.171 45.569  -6.221  1.00 31.23  ? 135  ARG A CB  1 
ATOM   1023 C CG  . ARG A 1 135 ? -23.190 46.135  -7.633  1.00 35.45  ? 135  ARG A CG  1 
ATOM   1024 C CD  . ARG A 1 135 ? -23.055 47.630  -7.439  1.00 41.56  ? 135  ARG A CD  1 
ATOM   1025 N NE  . ARG A 1 135 ? -21.661 47.997  -7.321  1.00 49.15  ? 135  ARG A NE  1 
ATOM   1026 C CZ  . ARG A 1 135 ? -20.827 48.086  -8.352  1.00 51.17  ? 135  ARG A CZ  1 
ATOM   1027 N NH1 . ARG A 1 135 ? -21.254 47.839  -9.612  1.00 51.95  ? 135  ARG A NH1 1 
ATOM   1028 N NH2 . ARG A 1 135 ? -19.562 48.423  -8.107  1.00 52.41  ? 135  ARG A NH2 1 
ATOM   1029 N N   . GLN A 1 136 ? -23.798 44.311  -3.615  1.00 28.39  ? 136  GLN A N   1 
ATOM   1030 C CA  . GLN A 1 136 ? -23.312 44.466  -2.231  1.00 29.58  ? 136  GLN A CA  1 
ATOM   1031 C C   . GLN A 1 136 ? -24.333 43.881  -1.275  1.00 28.51  ? 136  GLN A C   1 
ATOM   1032 O O   . GLN A 1 136 ? -25.212 44.584  -0.807  1.00 30.69  ? 136  GLN A O   1 
ATOM   1033 C CB  . GLN A 1 136 ? -23.004 45.939  -1.865  1.00 29.55  ? 136  GLN A CB  1 
ATOM   1034 C CG  . GLN A 1 136 ? -22.534 46.884  -2.996  1.00 33.72  ? 136  GLN A CG  1 
ATOM   1035 C CD  . GLN A 1 136 ? -21.071 46.678  -3.420  1.00 40.40  ? 136  GLN A CD  1 
ATOM   1036 O OE1 . GLN A 1 136 ? -20.177 46.491  -2.578  1.00 41.90  ? 136  GLN A OE1 1 
ATOM   1037 N NE2 . GLN A 1 136 ? -20.821 46.721  -4.739  1.00 40.24  ? 136  GLN A NE2 1 
ATOM   1038 N N   . PRO A 1 137 ? -24.264 42.579  -1.012  1.00 27.48  ? 137  PRO A N   1 
ATOM   1039 C CA  . PRO A 1 137 ? -23.311 41.575  -1.443  1.00 25.88  ? 137  PRO A CA  1 
ATOM   1040 C C   . PRO A 1 137 ? -23.666 40.980  -2.821  1.00 24.93  ? 137  PRO A C   1 
ATOM   1041 O O   . PRO A 1 137 ? -24.774 41.184  -3.332  1.00 22.83  ? 137  PRO A O   1 
ATOM   1042 C CB  . PRO A 1 137 ? -23.442 40.517  -0.346  1.00 26.69  ? 137  PRO A CB  1 
ATOM   1043 C CG  . PRO A 1 137 ? -24.895 40.607  0.083   1.00 27.05  ? 137  PRO A CG  1 
ATOM   1044 C CD  . PRO A 1 137 ? -25.349 41.999  -0.192  1.00 27.56  ? 137  PRO A CD  1 
ATOM   1045 N N   . PHE A 1 138 ? -22.712 40.281  -3.430  1.00 23.22  ? 138  PHE A N   1 
ATOM   1046 C CA  . PHE A 1 138 ? -22.936 39.695  -4.746  1.00 21.92  ? 138  PHE A CA  1 
ATOM   1047 C C   . PHE A 1 138 ? -24.081 38.701  -4.708  1.00 21.43  ? 138  PHE A C   1 
ATOM   1048 O O   . PHE A 1 138 ? -24.112 37.793  -3.866  1.00 20.83  ? 138  PHE A O   1 
ATOM   1049 C CB  . PHE A 1 138 ? -21.694 38.937  -5.228  1.00 21.25  ? 138  PHE A CB  1 
ATOM   1050 C CG  . PHE A 1 138 ? -21.952 38.065  -6.438  1.00 21.67  ? 138  PHE A CG  1 
ATOM   1051 C CD1 . PHE A 1 138 ? -22.053 36.671  -6.315  1.00 20.43  ? 138  PHE A CD1 1 
ATOM   1052 C CD2 . PHE A 1 138 ? -22.129 38.641  -7.695  1.00 20.62  ? 138  PHE A CD2 1 
ATOM   1053 C CE1 . PHE A 1 138 ? -22.315 35.873  -7.441  1.00 22.49  ? 138  PHE A CE1 1 
ATOM   1054 C CE2 . PHE A 1 138 ? -22.381 37.831  -8.831  1.00 21.96  ? 138  PHE A CE2 1 
ATOM   1055 C CZ  . PHE A 1 138 ? -22.473 36.457  -8.699  1.00 20.42  ? 138  PHE A CZ  1 
ATOM   1056 N N   . SER A 1 139 ? -25.010 38.845  -5.642  1.00 20.88  ? 139  SER A N   1 
ATOM   1057 C CA  . SER A 1 139 ? -25.855 37.719  -5.971  1.00 20.45  ? 139  SER A CA  1 
ATOM   1058 C C   . SER A 1 139 ? -26.265 37.758  -7.433  1.00 19.48  ? 139  SER A C   1 
ATOM   1059 O O   . SER A 1 139 ? -26.078 38.775  -8.119  1.00 19.05  ? 139  SER A O   1 
ATOM   1060 C CB  . SER A 1 139 ? -27.041 37.621  -5.035  1.00 20.47  ? 139  SER A CB  1 
ATOM   1061 O OG  . SER A 1 139 ? -27.904 38.691  -5.267  1.00 22.68  ? 139  SER A OG  1 
ATOM   1062 N N   . ILE A 1 140 ? -26.724 36.615  -7.932  1.00 17.98  ? 140  ILE A N   1 
ATOM   1063 C CA  . ILE A 1 140 ? -27.153 36.500  -9.314  1.00 18.84  ? 140  ILE A CA  1 
ATOM   1064 C C   . ILE A 1 140 ? -28.526 35.868  -9.309  1.00 18.40  ? 140  ILE A C   1 
ATOM   1065 O O   . ILE A 1 140 ? -28.807 34.932  -8.558  1.00 18.83  ? 140  ILE A O   1 
ATOM   1066 C CB  . ILE A 1 140 ? -26.171 35.688  -10.194 1.00 18.88  ? 140  ILE A CB  1 
ATOM   1067 C CG1 . ILE A 1 140 ? -26.654 35.603  -11.666 1.00 19.59  ? 140  ILE A CG1 1 
ATOM   1068 C CG2 . ILE A 1 140 ? -25.885 34.257  -9.600  1.00 18.43  ? 140  ILE A CG2 1 
ATOM   1069 C CD1 . ILE A 1 140 ? -25.495 35.111  -12.681 1.00 19.55  ? 140  ILE A CD1 1 
ATOM   1070 N N   . LYS A 1 141 ? -29.373 36.386  -10.160 1.00 19.37  ? 141  LYS A N   1 
ATOM   1071 C CA  . LYS A 1 141 ? -30.746 35.952  -10.218 1.00 19.87  ? 141  LYS A CA  1 
ATOM   1072 C C   . LYS A 1 141 ? -31.118 35.769  -11.689 1.00 20.08  ? 141  LYS A C   1 
ATOM   1073 O O   . LYS A 1 141 ? -30.704 36.548  -12.550 1.00 20.93  ? 141  LYS A O   1 
ATOM   1074 C CB  . LYS A 1 141 ? -31.586 37.057  -9.581  1.00 21.94  ? 141  LYS A CB  1 
ATOM   1075 C CG  . LYS A 1 141 ? -33.065 36.819  -9.578  1.00 27.43  ? 141  LYS A CG  1 
ATOM   1076 C CD  . LYS A 1 141 ? -33.832 38.116  -9.243  1.00 36.06  ? 141  LYS A CD  1 
ATOM   1077 C CE  . LYS A 1 141 ? -33.670 38.551  -7.805  1.00 40.62  ? 141  LYS A CE  1 
ATOM   1078 N NZ  . LYS A 1 141 ? -34.541 39.770  -7.599  1.00 44.33  ? 141  LYS A NZ  1 
ATOM   1079 N N   . VAL A 1 142 ? -31.865 34.716  -11.998 1.00 19.10  ? 142  VAL A N   1 
ATOM   1080 C CA  . VAL A 1 142 ? -32.351 34.497  -13.337 1.00 18.38  ? 142  VAL A CA  1 
ATOM   1081 C C   . VAL A 1 142 ? -33.864 34.357  -13.199 1.00 18.24  ? 142  VAL A C   1 
ATOM   1082 O O   . VAL A 1 142 ? -34.343 33.560  -12.403 1.00 16.66  ? 142  VAL A O   1 
ATOM   1083 C CB  . VAL A 1 142 ? -31.795 33.225  -13.955 1.00 19.25  ? 142  VAL A CB  1 
ATOM   1084 C CG1 . VAL A 1 142 ? -32.381 33.020  -15.333 1.00 17.94  ? 142  VAL A CG1 1 
ATOM   1085 C CG2 . VAL A 1 142 ? -30.257 33.262  -14.063 1.00 19.33  ? 142  VAL A CG2 1 
ATOM   1086 N N   . THR A 1 143 ? -34.588 35.187  -13.936 1.00 18.49  ? 143  THR A N   1 
ATOM   1087 C CA  . THR A 1 143 ? -36.031 35.239  -13.850 1.00 20.04  ? 143  THR A CA  1 
ATOM   1088 C C   . THR A 1 143 ? -36.582 34.934  -15.219 1.00 19.68  ? 143  THR A C   1 
ATOM   1089 O O   . THR A 1 143 ? -35.959 35.212  -16.236 1.00 20.53  ? 143  THR A O   1 
ATOM   1090 C CB  . THR A 1 143 ? -36.506 36.638  -13.469 1.00 19.91  ? 143  THR A CB  1 
ATOM   1091 O OG1 . THR A 1 143 ? -35.991 37.552  -14.450 1.00 25.71  ? 143  THR A OG1 1 
ATOM   1092 C CG2 . THR A 1 143 ? -35.962 37.020  -12.114 1.00 19.60  ? 143  THR A CG2 1 
ATOM   1093 N N   . ARG A 1 144 ? -37.762 34.360  -15.230 1.00 18.99  ? 144  ARG A N   1 
ATOM   1094 C CA  . ARG A 1 144 ? -38.442 34.078  -16.472 1.00 19.36  ? 144  ARG A CA  1 
ATOM   1095 C C   . ARG A 1 144 ? -39.112 35.391  -16.905 1.00 19.07  ? 144  ARG A C   1 
ATOM   1096 O O   . ARG A 1 144 ? -39.845 36.013  -16.113 1.00 18.64  ? 144  ARG A O   1 
ATOM   1097 C CB  . ARG A 1 144 ? -39.484 33.000  -16.211 1.00 18.11  ? 144  ARG A CB  1 
ATOM   1098 C CG  . ARG A 1 144 ? -40.344 32.665  -17.419 1.00 18.29  ? 144  ARG A CG  1 
ATOM   1099 C CD  . ARG A 1 144 ? -41.299 31.536  -17.076 1.00 16.17  ? 144  ARG A CD  1 
ATOM   1100 N NE  . ARG A 1 144 ? -40.648 30.230  -16.922 1.00 17.14  ? 144  ARG A NE  1 
ATOM   1101 C CZ  . ARG A 1 144 ? -40.217 29.472  -17.939 1.00 14.86  ? 144  ARG A CZ  1 
ATOM   1102 N NH1 . ARG A 1 144 ? -40.327 29.880  -19.203 1.00 18.13  ? 144  ARG A NH1 1 
ATOM   1103 N NH2 . ARG A 1 144 ? -39.668 28.302  -17.687 1.00 13.74  ? 144  ARG A NH2 1 
ATOM   1104 N N   . ARG A 1 145 ? -38.853 35.821  -18.132 1.00 20.07  ? 145  ARG A N   1 
ATOM   1105 C CA  . ARG A 1 145 ? -39.343 37.129  -18.596 1.00 23.11  ? 145  ARG A CA  1 
ATOM   1106 C C   . ARG A 1 145 ? -40.873 37.192  -18.634 1.00 23.20  ? 145  ARG A C   1 
ATOM   1107 O O   . ARG A 1 145 ? -41.493 38.210  -18.250 1.00 22.14  ? 145  ARG A O   1 
ATOM   1108 C CB  . ARG A 1 145 ? -38.778 37.460  -19.969 1.00 23.13  ? 145  ARG A CB  1 
ATOM   1109 C CG  . ARG A 1 145 ? -37.395 38.115  -19.931 1.00 28.35  ? 145  ARG A CG  1 
ATOM   1110 C CD  . ARG A 1 145 ? -37.047 38.919  -21.207 1.00 28.81  ? 145  ARG A CD  1 
ATOM   1111 N NE  . ARG A 1 145 ? -38.234 39.226  -22.004 1.00 41.29  ? 145  ARG A NE  1 
ATOM   1112 C CZ  . ARG A 1 145 ? -38.227 39.587  -23.291 1.00 43.94  ? 145  ARG A CZ  1 
ATOM   1113 N NH1 . ARG A 1 145 ? -37.084 39.699  -23.966 1.00 45.86  ? 145  ARG A NH1 1 
ATOM   1114 N NH2 . ARG A 1 145 ? -39.380 39.829  -23.912 1.00 46.11  ? 145  ARG A NH2 1 
ATOM   1115 N N   . SER A 1 146 ? -41.493 36.107  -19.083 1.00 22.61  ? 146  SER A N   1 
ATOM   1116 C CA  . SER A 1 146 ? -42.952 36.151  -19.289 1.00 22.98  ? 146  SER A CA  1 
ATOM   1117 C C   . SER A 1 146 ? -43.741 36.449  -18.003 1.00 23.50  ? 146  SER A C   1 
ATOM   1118 O O   . SER A 1 146 ? -44.666 37.260  -18.014 1.00 24.76  ? 146  SER A O   1 
ATOM   1119 C CB  . SER A 1 146 ? -43.440 34.864  -19.943 1.00 22.27  ? 146  SER A CB  1 
ATOM   1120 O OG  . SER A 1 146 ? -43.378 33.795  -19.016 1.00 22.42  ? 146  SER A OG  1 
ATOM   1121 N N   . ASN A 1 147 ? -43.385 35.822  -16.885 1.00 23.55  ? 147  ASN A N   1 
ATOM   1122 C CA  . ASN A 1 147 ? -44.154 36.022  -15.645 1.00 23.24  ? 147  ASN A CA  1 
ATOM   1123 C C   . ASN A 1 147 ? -43.314 36.571  -14.483 1.00 23.02  ? 147  ASN A C   1 
ATOM   1124 O O   . ASN A 1 147 ? -43.786 36.671  -13.357 1.00 23.93  ? 147  ASN A O   1 
ATOM   1125 C CB  . ASN A 1 147 ? -44.861 34.727  -15.231 1.00 23.47  ? 147  ASN A CB  1 
ATOM   1126 C CG  . ASN A 1 147 ? -43.887 33.588  -14.985 1.00 23.49  ? 147  ASN A CG  1 
ATOM   1127 O OD1 . ASN A 1 147 ? -42.662 33.755  -15.090 1.00 20.68  ? 147  ASN A OD1 1 
ATOM   1128 N ND2 . ASN A 1 147 ? -44.427 32.434  -14.636 1.00 21.25  ? 147  ASN A ND2 1 
ATOM   1129 N N   . ASN A 1 148 ? -42.080 36.944  -14.785 1.00 21.89  ? 148  ASN A N   1 
ATOM   1130 C CA  . ASN A 1 148 ? -41.100 37.381  -13.796 1.00 22.13  ? 148  ASN A CA  1 
ATOM   1131 C C   . ASN A 1 148 ? -40.878 36.398  -12.656 1.00 20.89  ? 148  ASN A C   1 
ATOM   1132 O O   . ASN A 1 148 ? -40.521 36.805  -11.544 1.00 21.53  ? 148  ASN A O   1 
ATOM   1133 C CB  . ASN A 1 148 ? -41.415 38.809  -13.288 1.00 23.43  ? 148  ASN A CB  1 
ATOM   1134 C CG  . ASN A 1 148 ? -41.105 39.887  -14.341 1.00 26.11  ? 148  ASN A CG  1 
ATOM   1135 O OD1 . ASN A 1 148 ? -41.770 40.911  -14.385 1.00 32.99  ? 148  ASN A OD1 1 
ATOM   1136 N ND2 . ASN A 1 148 ? -40.088 39.658  -15.178 1.00 22.67  ? 148  ASN A ND2 1 
ATOM   1137 N N   . ARG A 1 149 ? -41.044 35.111  -12.929 1.00 19.09  ? 149  ARG A N   1 
ATOM   1138 C CA  . ARG A 1 149 ? -40.879 34.101  -11.858 1.00 18.97  ? 149  ARG A CA  1 
ATOM   1139 C C   . ARG A 1 149 ? -39.384 34.011  -11.622 1.00 18.45  ? 149  ARG A C   1 
ATOM   1140 O O   . ARG A 1 149 ? -38.626 33.871  -12.573 1.00 18.89  ? 149  ARG A O   1 
ATOM   1141 C CB  . ARG A 1 149 ? -41.408 32.758  -12.295 1.00 18.84  ? 149  ARG A CB  1 
ATOM   1142 C CG  . ARG A 1 149 ? -41.048 31.597  -11.358 1.00 23.39  ? 149  ARG A CG  1 
ATOM   1143 C CD  . ARG A 1 149 ? -42.154 31.359  -10.404 1.00 29.52  ? 149  ARG A CD  1 
ATOM   1144 N NE  . ARG A 1 149 ? -43.329 30.863  -11.125 1.00 33.34  ? 149  ARG A NE  1 
ATOM   1145 C CZ  . ARG A 1 149 ? -44.531 30.735  -10.575 1.00 39.94  ? 149  ARG A CZ  1 
ATOM   1146 N NH1 . ARG A 1 149 ? -44.726 31.076  -9.290  1.00 40.56  ? 149  ARG A NH1 1 
ATOM   1147 N NH2 . ARG A 1 149 ? -45.544 30.275  -11.306 1.00 38.65  ? 149  ARG A NH2 1 
ATOM   1148 N N   . VAL A 1 150 ? -38.965 34.128  -10.374 1.00 18.50  ? 150  VAL A N   1 
ATOM   1149 C CA  . VAL A 1 150 ? -37.528 34.000  -10.072 1.00 18.68  ? 150  VAL A CA  1 
ATOM   1150 C C   . VAL A 1 150 ? -37.184 32.517  -10.093 1.00 17.83  ? 150  VAL A C   1 
ATOM   1151 O O   . VAL A 1 150 ? -37.795 31.710  -9.357  1.00 17.97  ? 150  VAL A O   1 
ATOM   1152 C CB  . VAL A 1 150 ? -37.157 34.629  -8.703  1.00 19.66  ? 150  VAL A CB  1 
ATOM   1153 C CG1 . VAL A 1 150 ? -35.682 34.386  -8.393  1.00 20.18  ? 150  VAL A CG1 1 
ATOM   1154 C CG2 . VAL A 1 150 ? -37.447 36.138  -8.722  1.00 21.30  ? 150  VAL A CG2 1 
ATOM   1155 N N   . LEU A 1 151 ? -36.209 32.157  -10.928 1.00 16.73  ? 151  LEU A N   1 
ATOM   1156 C CA  . LEU A 1 151 ? -35.871 30.752  -11.124 1.00 16.94  ? 151  LEU A CA  1 
ATOM   1157 C C   . LEU A 1 151 ? -34.619 30.399  -10.322 1.00 17.99  ? 151  LEU A C   1 
ATOM   1158 O O   . LEU A 1 151 ? -34.627 29.517  -9.478  1.00 19.34  ? 151  LEU A O   1 
ATOM   1159 C CB  . LEU A 1 151 ? -35.650 30.441  -12.613 1.00 16.39  ? 151  LEU A CB  1 
ATOM   1160 C CG  . LEU A 1 151 ? -36.860 30.792  -13.512 1.00 15.46  ? 151  LEU A CG  1 
ATOM   1161 C CD1 . LEU A 1 151 ? -36.525 30.332  -14.915 1.00 15.00  ? 151  LEU A CD1 1 
ATOM   1162 C CD2 . LEU A 1 151 ? -38.091 30.151  -12.997 1.00 18.31  ? 151  LEU A CD2 1 
ATOM   1163 N N   . PHE A 1 152 ? -33.553 31.104  -10.638 1.00 18.18  ? 152  PHE A N   1 
ATOM   1164 C CA  . PHE A 1 152 ? -32.273 30.964  -9.941  1.00 19.01  ? 152  PHE A CA  1 
ATOM   1165 C C   . PHE A 1 152 ? -32.085 32.278  -9.152  1.00 19.30  ? 152  PHE A C   1 
ATOM   1166 O O   . PHE A 1 152 ? -32.346 33.390  -9.671  1.00 20.20  ? 152  PHE A O   1 
ATOM   1167 C CB  . PHE A 1 152 ? -31.182 30.836  -10.978 1.00 18.77  ? 152  PHE A CB  1 
ATOM   1168 C CG  . PHE A 1 152 ? -29.872 30.340  -10.424 1.00 20.50  ? 152  PHE A CG  1 
ATOM   1169 C CD1 . PHE A 1 152 ? -29.509 28.996  -10.554 1.00 20.40  ? 152  PHE A CD1 1 
ATOM   1170 C CD2 . PHE A 1 152 ? -29.014 31.211  -9.772  1.00 20.79  ? 152  PHE A CD2 1 
ATOM   1171 C CE1 . PHE A 1 152 ? -28.262 28.524  -10.069 1.00 23.17  ? 152  PHE A CE1 1 
ATOM   1172 C CE2 . PHE A 1 152 ? -27.762 30.749  -9.270  1.00 20.42  ? 152  PHE A CE2 1 
ATOM   1173 C CZ  . PHE A 1 152 ? -27.407 29.413  -9.404  1.00 21.08  ? 152  PHE A CZ  1 
ATOM   1174 N N   . ASP A 1 153 ? -31.704 32.169  -7.893  1.00 19.18  ? 153  ASP A N   1 
ATOM   1175 C CA  . ASP A 1 153 ? -31.522 33.352  -7.046  1.00 19.69  ? 153  ASP A CA  1 
ATOM   1176 C C   . ASP A 1 153 ? -30.532 32.933  -5.991  1.00 18.81  ? 153  ASP A C   1 
ATOM   1177 O O   . ASP A 1 153 ? -30.905 32.278  -5.016  1.00 19.22  ? 153  ASP A O   1 
ATOM   1178 C CB  . ASP A 1 153 ? -32.834 33.748  -6.361  1.00 19.77  ? 153  ASP A CB  1 
ATOM   1179 C CG  . ASP A 1 153 ? -32.688 34.971  -5.451  1.00 22.83  ? 153  ASP A CG  1 
ATOM   1180 O OD1 . ASP A 1 153 ? -31.588 35.609  -5.396  1.00 25.21  ? 153  ASP A OD1 1 
ATOM   1181 O OD2 . ASP A 1 153 ? -33.694 35.297  -4.769  1.00 27.40  ? 153  ASP A OD2 1 
ATOM   1182 N N   . SER A 1 154 ? -29.273 33.276  -6.177  1.00 19.07  ? 154  SER A N   1 
ATOM   1183 C CA  . SER A 1 154 ? -28.258 32.936  -5.181  1.00 18.51  ? 154  SER A CA  1 
ATOM   1184 C C   . SER A 1 154 ? -28.286 33.777  -3.886  1.00 19.34  ? 154  SER A C   1 
ATOM   1185 O O   . SER A 1 154 ? -27.507 33.500  -2.950  1.00 19.09  ? 154  SER A O   1 
ATOM   1186 C CB  . SER A 1 154 ? -26.874 33.038  -5.811  1.00 18.88  ? 154  SER A CB  1 
ATOM   1187 O OG  . SER A 1 154 ? -26.481 34.415  -5.911  1.00 20.73  ? 154  SER A OG  1 
ATOM   1188 N N   . SER A 1 155 ? -29.144 34.803  -3.818  1.00 19.15  ? 155  SER A N   1 
ATOM   1189 C CA  . SER A 1 155 ? -29.116 35.733  -2.686  1.00 19.71  ? 155  SER A CA  1 
ATOM   1190 C C   . SER A 1 155 ? -29.487 35.084  -1.349  1.00 19.28  ? 155  SER A C   1 
ATOM   1191 O O   . SER A 1 155 ? -29.292 35.691  -0.308  1.00 18.49  ? 155  SER A O   1 
ATOM   1192 C CB  . SER A 1 155 ? -30.009 36.964  -2.952  1.00 20.70  ? 155  SER A CB  1 
ATOM   1193 O OG  . SER A 1 155 ? -31.370 36.561  -2.934  1.00 21.77  ? 155  SER A OG  1 
ATOM   1194 N N   . ILE A 1 156 ? -29.994 33.851  -1.374  1.00 18.57  ? 156  ILE A N   1 
ATOM   1195 C CA  . ILE A 1 156 ? -30.313 33.136  -0.122  1.00 18.84  ? 156  ILE A CA  1 
ATOM   1196 C C   . ILE A 1 156 ? -29.022 32.840  0.685   1.00 18.46  ? 156  ILE A C   1 
ATOM   1197 O O   . ILE A 1 156 ? -29.044 32.710  1.893   1.00 19.97  ? 156  ILE A O   1 
ATOM   1198 C CB  . ILE A 1 156 ? -31.122 31.843  -0.390  1.00 19.09  ? 156  ILE A CB  1 
ATOM   1199 C CG1 . ILE A 1 156 ? -31.717 31.296  0.920   1.00 18.80  ? 156  ILE A CG1 1 
ATOM   1200 C CG2 . ILE A 1 156 ? -30.319 30.804  -1.216  1.00 21.12  ? 156  ILE A CG2 1 
ATOM   1201 C CD1 . ILE A 1 156 ? -32.658 30.091  0.748   1.00 18.35  ? 156  ILE A CD1 1 
ATOM   1202 N N   . GLY A 1 157 ? -27.892 32.758  0.017   1.00 17.53  ? 157  GLY A N   1 
ATOM   1203 C CA  . GLY A 1 157 ? -26.706 32.374  0.733   1.00 17.00  ? 157  GLY A CA  1 
ATOM   1204 C C   . GLY A 1 157 ? -25.507 33.045  0.120   1.00 16.89  ? 157  GLY A C   1 
ATOM   1205 O O   . GLY A 1 157 ? -25.595 33.815  -0.843  1.00 16.26  ? 157  GLY A O   1 
ATOM   1206 N N   . PRO A 1 158 ? -24.364 32.804  0.726   1.00 16.87  ? 158  PRO A N   1 
ATOM   1207 C CA  . PRO A 1 158 ? -23.099 33.352  0.248   1.00 17.31  ? 158  PRO A CA  1 
ATOM   1208 C C   . PRO A 1 158 ? -22.559 32.684  -1.032  1.00 17.47  ? 158  PRO A C   1 
ATOM   1209 O O   . PRO A 1 158 ? -22.998 31.608  -1.412  1.00 18.40  ? 158  PRO A O   1 
ATOM   1210 C CB  . PRO A 1 158 ? -22.163 33.062  1.428   1.00 17.77  ? 158  PRO A CB  1 
ATOM   1211 C CG  . PRO A 1 158 ? -22.642 31.794  1.994   1.00 16.93  ? 158  PRO A CG  1 
ATOM   1212 C CD  . PRO A 1 158 ? -24.207 31.981  1.934   1.00 16.82  ? 158  PRO A CD  1 
ATOM   1213 N N   . LEU A 1 159 ? -21.610 33.329  -1.705  1.00 17.47  ? 159  LEU A N   1 
ATOM   1214 C CA  . LEU A 1 159 ? -20.758 32.618  -2.622  1.00 17.08  ? 159  LEU A CA  1 
ATOM   1215 C C   . LEU A 1 159 ? -19.544 32.313  -1.785  1.00 18.47  ? 159  LEU A C   1 
ATOM   1216 O O   . LEU A 1 159 ? -19.010 33.249  -1.163  1.00 17.96  ? 159  LEU A O   1 
ATOM   1217 C CB  . LEU A 1 159 ? -20.334 33.511  -3.797  1.00 17.09  ? 159  LEU A CB  1 
ATOM   1218 C CG  . LEU A 1 159 ? -19.065 33.092  -4.576  1.00 15.79  ? 159  LEU A CG  1 
ATOM   1219 C CD1 . LEU A 1 159 ? -19.136 31.675  -5.226  1.00 14.23  ? 159  LEU A CD1 1 
ATOM   1220 C CD2 . LEU A 1 159 ? -18.721 34.181  -5.621  1.00 17.22  ? 159  LEU A CD2 1 
ATOM   1221 N N   . LEU A 1 160 ? -19.111 31.038  -1.753  1.00 18.34  ? 160  LEU A N   1 
ATOM   1222 C CA  . LEU A 1 160 ? -17.853 30.661  -1.074  1.00 18.59  ? 160  LEU A CA  1 
ATOM   1223 C C   . LEU A 1 160 ? -16.965 30.134  -2.141  1.00 19.61  ? 160  LEU A C   1 
ATOM   1224 O O   . LEU A 1 160 ? -17.425 29.400  -3.005  1.00 17.69  ? 160  LEU A O   1 
ATOM   1225 C CB  . LEU A 1 160 ? -18.090 29.605  0.018   1.00 18.54  ? 160  LEU A CB  1 
ATOM   1226 C CG  . LEU A 1 160 ? -19.172 30.137  0.983   1.00 18.19  ? 160  LEU A CG  1 
ATOM   1227 C CD1 . LEU A 1 160 ? -19.750 29.061  1.859   1.00 22.80  ? 160  LEU A CD1 1 
ATOM   1228 C CD2 . LEU A 1 160 ? -18.678 31.261  1.860   1.00 19.34  ? 160  LEU A CD2 1 
ATOM   1229 N N   . PHE A 1 161 ? -15.684 30.524  -2.115  1.00 19.47  ? 161  PHE A N   1 
ATOM   1230 C CA  . PHE A 1 161 ? -14.785 30.140  -3.173  1.00 20.49  ? 161  PHE A CA  1 
ATOM   1231 C C   . PHE A 1 161 ? -13.360 30.036  -2.619  1.00 21.37  ? 161  PHE A C   1 
ATOM   1232 O O   . PHE A 1 161 ? -12.575 30.986  -2.740  1.00 23.14  ? 161  PHE A O   1 
ATOM   1233 C CB  . PHE A 1 161 ? -14.835 31.186  -4.292  1.00 20.94  ? 161  PHE A CB  1 
ATOM   1234 C CG  . PHE A 1 161 ? -14.372 30.690  -5.647  1.00 23.05  ? 161  PHE A CG  1 
ATOM   1235 C CD1 . PHE A 1 161 ? -15.189 30.834  -6.772  1.00 27.55  ? 161  PHE A CD1 1 
ATOM   1236 C CD2 . PHE A 1 161 ? -13.126 30.089  -5.810  1.00 26.89  ? 161  PHE A CD2 1 
ATOM   1237 C CE1 . PHE A 1 161 ? -14.762 30.371  -8.019  1.00 27.32  ? 161  PHE A CE1 1 
ATOM   1238 C CE2 . PHE A 1 161 ? -12.675 29.640  -7.055  1.00 26.71  ? 161  PHE A CE2 1 
ATOM   1239 C CZ  . PHE A 1 161 ? -13.476 29.789  -8.158  1.00 27.13  ? 161  PHE A CZ  1 
ATOM   1240 N N   . ALA A 1 162 ? -13.042 28.901  -2.005  1.00 21.71  ? 162  ALA A N   1 
ATOM   1241 C CA  . ALA A 1 162 ? -11.671 28.583  -1.621  1.00 21.07  ? 162  ALA A CA  1 
ATOM   1242 C C   . ALA A 1 162 ? -11.169 27.526  -2.576  1.00 22.13  ? 162  ALA A C   1 
ATOM   1243 O O   . ALA A 1 162 ? -11.936 26.912  -3.313  1.00 21.03  ? 162  ALA A O   1 
ATOM   1244 C CB  . ALA A 1 162 ? -11.616 28.098  -0.198  1.00 21.87  ? 162  ALA A CB  1 
ATOM   1245 N N   . ASP A 1 163 ? -9.867  27.285  -2.564  1.00 21.28  ? 163  ASP A N   1 
ATOM   1246 C CA  . ASP A 1 163 ? -9.281  26.358  -3.503  1.00 22.37  ? 163  ASP A CA  1 
ATOM   1247 C C   . ASP A 1 163 ? -9.953  24.976  -3.441  1.00 21.31  ? 163  ASP A C   1 
ATOM   1248 O O   . ASP A 1 163 ? -10.131 24.314  -4.481  1.00 20.90  ? 163  ASP A O   1 
ATOM   1249 C CB  . ASP A 1 163 ? -7.772  26.297  -3.241  1.00 23.62  ? 163  ASP A CB  1 
ATOM   1250 C CG  . ASP A 1 163 ? -7.017  25.447  -4.247  1.00 27.79  ? 163  ASP A CG  1 
ATOM   1251 O OD1 . ASP A 1 163 ? -7.208  25.578  -5.481  1.00 32.76  ? 163  ASP A OD1 1 
ATOM   1252 O OD2 . ASP A 1 163 ? -6.207  24.629  -3.783  1.00 30.21  ? 163  ASP A OD2 1 
ATOM   1253 N N   . GLN A 1 164 ? -10.340 24.548  -2.234  1.00 19.26  ? 164  GLN A N   1 
ATOM   1254 C CA  . GLN A 1 164 ? -10.900 23.215  -2.073  1.00 18.23  ? 164  GLN A CA  1 
ATOM   1255 C C   . GLN A 1 164 ? -12.234 23.292  -1.396  1.00 18.12  ? 164  GLN A C   1 
ATOM   1256 O O   . GLN A 1 164 ? -12.647 22.353  -0.706  1.00 17.83  ? 164  GLN A O   1 
ATOM   1257 C CB  . GLN A 1 164 ? -9.967  22.306  -1.276  1.00 18.42  ? 164  GLN A CB  1 
ATOM   1258 C CG  . GLN A 1 164 ? -8.618  22.143  -1.980  1.00 17.59  ? 164  GLN A CG  1 
ATOM   1259 C CD  . GLN A 1 164 ? -7.764  21.099  -1.316  1.00 20.67  ? 164  GLN A CD  1 
ATOM   1260 O OE1 . GLN A 1 164 ? -8.017  19.889  -1.434  1.00 21.02  ? 164  GLN A OE1 1 
ATOM   1261 N NE2 . GLN A 1 164 ? -6.752  21.544  -0.615  1.00 19.82  ? 164  GLN A NE2 1 
ATOM   1262 N N   . PHE A 1 165 ? -12.917 24.419  -1.581  1.00 17.72  ? 165  PHE A N   1 
ATOM   1263 C CA  . PHE A 1 165 ? -14.273 24.543  -1.074  1.00 18.27  ? 165  PHE A CA  1 
ATOM   1264 C C   . PHE A 1 165 ? -15.016 25.633  -1.809  1.00 17.83  ? 165  PHE A C   1 
ATOM   1265 O O   . PHE A 1 165 ? -14.723 26.837  -1.627  1.00 17.29  ? 165  PHE A O   1 
ATOM   1266 C CB  . PHE A 1 165 ? -14.321 24.830  0.418   1.00 19.19  ? 165  PHE A CB  1 
ATOM   1267 C CG  . PHE A 1 165 ? -15.685 24.674  1.014   1.00 19.99  ? 165  PHE A CG  1 
ATOM   1268 C CD1 . PHE A 1 165 ? -16.109 23.438  1.494   1.00 22.83  ? 165  PHE A CD1 1 
ATOM   1269 C CD2 . PHE A 1 165 ? -16.548 25.753  1.110   1.00 24.42  ? 165  PHE A CD2 1 
ATOM   1270 C CE1 . PHE A 1 165 ? -17.394 23.288  2.074   1.00 24.79  ? 165  PHE A CE1 1 
ATOM   1271 C CE2 . PHE A 1 165 ? -17.817 25.612  1.684   1.00 24.68  ? 165  PHE A CE2 1 
ATOM   1272 C CZ  . PHE A 1 165 ? -18.238 24.390  2.173   1.00 23.90  ? 165  PHE A CZ  1 
ATOM   1273 N N   . LEU A 1 166 ? -16.009 25.228  -2.612  1.00 16.65  ? 166  LEU A N   1 
ATOM   1274 C CA  . LEU A 1 166 ? -16.751 26.206  -3.430  1.00 16.63  ? 166  LEU A CA  1 
ATOM   1275 C C   . LEU A 1 166 ? -18.230 25.926  -3.205  1.00 16.50  ? 166  LEU A C   1 
ATOM   1276 O O   . LEU A 1 166 ? -18.628 24.779  -3.192  1.00 17.12  ? 166  LEU A O   1 
ATOM   1277 C CB  . LEU A 1 166 ? -16.413 26.056  -4.909  1.00 16.43  ? 166  LEU A CB  1 
ATOM   1278 C CG  . LEU A 1 166 ? -14.990 26.335  -5.393  1.00 19.40  ? 166  LEU A CG  1 
ATOM   1279 C CD1 . LEU A 1 166 ? -14.120 25.115  -5.195  1.00 20.57  ? 166  LEU A CD1 1 
ATOM   1280 C CD2 . LEU A 1 166 ? -15.084 26.694  -6.858  1.00 22.01  ? 166  LEU A CD2 1 
ATOM   1281 N N   . GLN A 1 167 ? -19.012 26.949  -2.932  1.00 16.10  ? 167  GLN A N   1 
ATOM   1282 C CA  . GLN A 1 167 ? -20.422 26.731  -2.654  1.00 16.76  ? 167  GLN A CA  1 
ATOM   1283 C C   . GLN A 1 167 ? -21.269 27.893  -3.226  1.00 16.84  ? 167  GLN A C   1 
ATOM   1284 O O   . GLN A 1 167 ? -20.888 29.072  -3.140  1.00 16.81  ? 167  GLN A O   1 
ATOM   1285 C CB  . GLN A 1 167 ? -20.657 26.628  -1.141  1.00 17.01  ? 167  GLN A CB  1 
ATOM   1286 C CG  . GLN A 1 167 ? -22.125 26.541  -0.753  1.00 17.63  ? 167  GLN A CG  1 
ATOM   1287 C CD  . GLN A 1 167 ? -22.330 26.330  0.735   1.00 18.40  ? 167  GLN A CD  1 
ATOM   1288 O OE1 . GLN A 1 167 ? -23.151 27.025  1.381   1.00 19.77  ? 167  GLN A OE1 1 
ATOM   1289 N NE2 . GLN A 1 167 ? -21.599 25.378  1.296   1.00 13.66  ? 167  GLN A NE2 1 
ATOM   1290 N N   . LEU A 1 168 ? -22.400 27.549  -3.825  1.00 17.36  ? 168  LEU A N   1 
ATOM   1291 C CA  . LEU A 1 168 ? -23.391 28.557  -4.173  1.00 16.94  ? 168  LEU A CA  1 
ATOM   1292 C C   . LEU A 1 168 ? -24.757 27.918  -3.975  1.00 17.49  ? 168  LEU A C   1 
ATOM   1293 O O   . LEU A 1 168 ? -24.929 26.705  -4.155  1.00 16.30  ? 168  LEU A O   1 
ATOM   1294 C CB  . LEU A 1 168 ? -23.202 29.001  -5.626  1.00 17.92  ? 168  LEU A CB  1 
ATOM   1295 C CG  . LEU A 1 168 ? -23.952 30.303  -6.014  1.00 18.67  ? 168  LEU A CG  1 
ATOM   1296 C CD1 . LEU A 1 168 ? -23.267 31.565  -5.427  1.00 18.44  ? 168  LEU A CD1 1 
ATOM   1297 C CD2 . LEU A 1 168 ? -24.104 30.391  -7.532  1.00 21.52  ? 168  LEU A CD2 1 
ATOM   1298 N N   . SER A 1 169 ? -25.720 28.727  -3.564  1.00 17.83  ? 169  SER A N   1 
ATOM   1299 C CA  . SER A 1 169 ? -27.054 28.238  -3.333  1.00 17.71  ? 169  SER A CA  1 
ATOM   1300 C C   . SER A 1 169 ? -27.979 28.933  -4.314  1.00 18.06  ? 169  SER A C   1 
ATOM   1301 O O   . SER A 1 169 ? -27.620 29.948  -4.891  1.00 18.48  ? 169  SER A O   1 
ATOM   1302 C CB  . SER A 1 169 ? -27.501 28.579  -1.916  1.00 17.50  ? 169  SER A CB  1 
ATOM   1303 O OG  . SER A 1 169 ? -26.548 28.126  -0.981  1.00 17.78  ? 169  SER A OG  1 
ATOM   1304 N N   . THR A 1 170 ? -29.170 28.376  -4.504  1.00 17.82  ? 170  THR A N   1 
ATOM   1305 C CA  . THR A 1 170 ? -30.207 29.083  -5.214  1.00 18.68  ? 170  THR A CA  1 
ATOM   1306 C C   . THR A 1 170 ? -31.558 28.770  -4.559  1.00 17.75  ? 170  THR A C   1 
ATOM   1307 O O   . THR A 1 170 ? -31.833 27.626  -4.190  1.00 17.26  ? 170  THR A O   1 
ATOM   1308 C CB  . THR A 1 170 ? -30.248 28.710  -6.710  1.00 19.66  ? 170  THR A CB  1 
ATOM   1309 O OG1 . THR A 1 170 ? -31.399 29.312  -7.324  1.00 21.21  ? 170  THR A OG1 1 
ATOM   1310 C CG2 . THR A 1 170 ? -30.328 27.176  -6.920  1.00 20.48  ? 170  THR A CG2 1 
ATOM   1311 N N   . ARG A 1 171 ? -32.378 29.788  -4.409  1.00 17.66  ? 171  ARG A N   1 
ATOM   1312 C CA  . ARG A 1 171 ? -33.800 29.559  -4.141  1.00 18.58  ? 171  ARG A CA  1 
ATOM   1313 C C   . ARG A 1 171 ? -34.401 28.810  -5.316  1.00 18.55  ? 171  ARG A C   1 
ATOM   1314 O O   . ARG A 1 171 ? -33.856 28.839  -6.443  1.00 19.15  ? 171  ARG A O   1 
ATOM   1315 C CB  . ARG A 1 171 ? -34.526 30.882  -3.978  1.00 18.93  ? 171  ARG A CB  1 
ATOM   1316 C CG  . ARG A 1 171 ? -34.098 31.681  -2.803  1.00 21.26  ? 171  ARG A CG  1 
ATOM   1317 C CD  . ARG A 1 171 ? -34.948 32.956  -2.708  1.00 25.61  ? 171  ARG A CD  1 
ATOM   1318 N NE  . ARG A 1 171 ? -34.065 34.079  -2.381  1.00 33.07  ? 171  ARG A NE  1 
ATOM   1319 C CZ  . ARG A 1 171 ? -33.833 34.493  -1.153  1.00 32.68  ? 171  ARG A CZ  1 
ATOM   1320 N NH1 . ARG A 1 171 ? -34.468 33.914  -0.140  1.00 34.15  ? 171  ARG A NH1 1 
ATOM   1321 N NH2 . ARG A 1 171 ? -33.008 35.506  -0.952  1.00 36.76  ? 171  ARG A NH2 1 
ATOM   1322 N N   . LEU A 1 172 ? -35.542 28.167  -5.073  1.00 17.77  ? 172  LEU A N   1 
ATOM   1323 C CA  . LEU A 1 172 ? -36.265 27.480  -6.126  1.00 18.20  ? 172  LEU A CA  1 
ATOM   1324 C C   . LEU A 1 172 ? -37.691 27.936  -6.062  1.00 18.45  ? 172  LEU A C   1 
ATOM   1325 O O   . LEU A 1 172 ? -38.148 28.294  -4.995  1.00 17.30  ? 172  LEU A O   1 
ATOM   1326 C CB  . LEU A 1 172 ? -36.199 25.960  -5.929  1.00 18.68  ? 172  LEU A CB  1 
ATOM   1327 C CG  . LEU A 1 172 ? -34.825 25.323  -6.136  1.00 19.93  ? 172  LEU A CG  1 
ATOM   1328 C CD1 . LEU A 1 172 ? -34.838 23.866  -5.708  1.00 23.32  ? 172  LEU A CD1 1 
ATOM   1329 C CD2 . LEU A 1 172 ? -34.318 25.483  -7.571  1.00 21.99  ? 172  LEU A CD2 1 
ATOM   1330 N N   . PRO A 1 173 ? -38.384 27.971  -7.213  1.00 19.85  ? 173  PRO A N   1 
ATOM   1331 C CA  . PRO A 1 173 ? -39.776 28.456  -7.254  1.00 20.71  ? 173  PRO A CA  1 
ATOM   1332 C C   . PRO A 1 173 ? -40.808 27.431  -6.837  1.00 21.61  ? 173  PRO A C   1 
ATOM   1333 O O   . PRO A 1 173 ? -41.998 27.789  -6.686  1.00 22.36  ? 173  PRO A O   1 
ATOM   1334 C CB  . PRO A 1 173 ? -39.959 28.856  -8.730  1.00 20.58  ? 173  PRO A CB  1 
ATOM   1335 C CG  . PRO A 1 173 ? -39.060 27.942  -9.488  1.00 19.80  ? 173  PRO A CG  1 
ATOM   1336 C CD  . PRO A 1 173 ? -37.883 27.615  -8.554  1.00 20.68  ? 173  PRO A CD  1 
ATOM   1337 N N   . SER A 1 174 ? -40.401 26.170  -6.663  1.00 21.53  ? 174  SER A N   1 
ATOM   1338 C CA  . SER A 1 174 ? -41.323 25.108  -6.266  1.00 21.02  ? 174  SER A CA  1 
ATOM   1339 C C   . SER A 1 174 ? -40.550 23.951  -5.640  1.00 21.27  ? 174  SER A C   1 
ATOM   1340 O O   . SER A 1 174 ? -39.311 23.887  -5.701  1.00 21.28  ? 174  SER A O   1 
ATOM   1341 C CB  . SER A 1 174 ? -42.130 24.584  -7.474  1.00 21.33  ? 174  SER A CB  1 
ATOM   1342 O OG  . SER A 1 174 ? -41.342 23.691  -8.245  1.00 19.52  ? 174  SER A OG  1 
ATOM   1343 N N   . THR A 1 175 ? -41.288 23.028  -5.051  1.00 20.29  ? 175  THR A N   1 
ATOM   1344 C CA  . THR A 1 175 ? -40.681 21.807  -4.539  1.00 20.21  ? 175  THR A CA  1 
ATOM   1345 C C   . THR A 1 175 ? -40.745 20.637  -5.543  1.00 18.97  ? 175  THR A C   1 
ATOM   1346 O O   . THR A 1 175 ? -40.454 19.489  -5.175  1.00 18.65  ? 175  THR A O   1 
ATOM   1347 C CB  . THR A 1 175 ? -41.368 21.401  -3.201  1.00 21.52  ? 175  THR A CB  1 
ATOM   1348 O OG1 . THR A 1 175 ? -42.785 21.338  -3.438  1.00 22.70  ? 175  THR A OG1 1 
ATOM   1349 C CG2 . THR A 1 175 ? -41.076 22.448  -2.126  1.00 22.06  ? 175  THR A CG2 1 
ATOM   1350 N N   . ASN A 1 176 ? -41.131 20.907  -6.797  1.00 17.00  ? 176  ASN A N   1 
ATOM   1351 C CA  . ASN A 1 176 ? -41.225 19.837  -7.788  1.00 16.52  ? 176  ASN A CA  1 
ATOM   1352 C C   . ASN A 1 176 ? -39.864 19.776  -8.423  1.00 15.63  ? 176  ASN A C   1 
ATOM   1353 O O   . ASN A 1 176 ? -39.671 20.402  -9.429  1.00 15.26  ? 176  ASN A O   1 
ATOM   1354 C CB  . ASN A 1 176 ? -42.226 20.190  -8.877  1.00 15.80  ? 176  ASN A CB  1 
ATOM   1355 C CG  . ASN A 1 176 ? -43.607 20.448  -8.322  1.00 21.10  ? 176  ASN A CG  1 
ATOM   1356 O OD1 . ASN A 1 176 ? -44.074 19.717  -7.446  1.00 21.65  ? 176  ASN A OD1 1 
ATOM   1357 N ND2 . ASN A 1 176 ? -44.251 21.501  -8.799  1.00 21.63  ? 176  ASN A ND2 1 
ATOM   1358 N N   . VAL A 1 177 ? -38.939 19.069  -7.781  1.00 15.43  ? 177  VAL A N   1 
ATOM   1359 C CA  . VAL A 1 177 ? -37.515 19.013  -8.164  1.00 14.56  ? 177  VAL A CA  1 
ATOM   1360 C C   . VAL A 1 177 ? -37.157 17.553  -8.452  1.00 13.70  ? 177  VAL A C   1 
ATOM   1361 O O   . VAL A 1 177 ? -37.412 16.655  -7.636  1.00 14.30  ? 177  VAL A O   1 
ATOM   1362 C CB  . VAL A 1 177 ? -36.601 19.551  -7.033  1.00 14.89  ? 177  VAL A CB  1 
ATOM   1363 C CG1 . VAL A 1 177 ? -35.137 19.278  -7.387  1.00 15.11  ? 177  VAL A CG1 1 
ATOM   1364 C CG2 . VAL A 1 177 ? -36.834 21.057  -6.849  1.00 17.64  ? 177  VAL A CG2 1 
ATOM   1365 N N   . TYR A 1 178 ? -36.586 17.307  -9.616  1.00 13.94  ? 178  TYR A N   1 
ATOM   1366 C CA  . TYR A 1 178 ? -36.338 15.944  -10.067 1.00 13.19  ? 178  TYR A CA  1 
ATOM   1367 C C   . TYR A 1 178 ? -34.917 15.900  -10.581 1.00 13.25  ? 178  TYR A C   1 
ATOM   1368 O O   . TYR A 1 178 ? -34.540 16.796  -11.320 1.00 13.79  ? 178  TYR A O   1 
ATOM   1369 C CB  . TYR A 1 178 ? -37.227 15.635  -11.255 1.00 13.11  ? 178  TYR A CB  1 
ATOM   1370 C CG  . TYR A 1 178 ? -38.679 15.900  -10.903 1.00 12.85  ? 178  TYR A CG  1 
ATOM   1371 C CD1 . TYR A 1 178 ? -39.417 14.977  -10.212 1.00 12.94  ? 178  TYR A CD1 1 
ATOM   1372 C CD2 . TYR A 1 178 ? -39.254 17.121  -11.228 1.00 13.70  ? 178  TYR A CD2 1 
ATOM   1373 C CE1 . TYR A 1 178 ? -40.789 15.264  -9.881  1.00 9.32   ? 178  TYR A CE1 1 
ATOM   1374 C CE2 . TYR A 1 178 ? -40.586 17.432  -10.917 1.00 15.09  ? 178  TYR A CE2 1 
ATOM   1375 C CZ  . TYR A 1 178 ? -41.320 16.523  -10.197 1.00 12.47  ? 178  TYR A CZ  1 
ATOM   1376 O OH  . TYR A 1 178 ? -42.689 16.806  -9.889  1.00 16.48  ? 178  TYR A OH  1 
ATOM   1377 N N   . GLY A 1 179 ? -34.171 14.838  -10.298 1.00 14.01  ? 179  GLY A N   1 
ATOM   1378 C CA  . GLY A 1 179 ? -32.794 14.788  -10.850 1.00 13.07  ? 179  GLY A CA  1 
ATOM   1379 C C   . GLY A 1 179 ? -31.713 14.553  -9.818  1.00 14.36  ? 179  GLY A C   1 
ATOM   1380 O O   . GLY A 1 179 ? -31.987 14.083  -8.727  1.00 16.17  ? 179  GLY A O   1 
ATOM   1381 N N   . LEU A 1 180 ? -30.476 14.861  -10.183 1.00 14.36  ? 180  LEU A N   1 
ATOM   1382 C CA  . LEU A 1 180 ? -29.296 14.528  -9.375  1.00 14.50  ? 180  LEU A CA  1 
ATOM   1383 C C   . LEU A 1 180 ? -28.987 13.043  -9.354  1.00 14.92  ? 180  LEU A C   1 
ATOM   1384 O O   . LEU A 1 180 ? -29.873 12.191  -9.396  1.00 14.95  ? 180  LEU A O   1 
ATOM   1385 C CB  . LEU A 1 180 ? -29.395 15.044  -7.936  1.00 14.38  ? 180  LEU A CB  1 
ATOM   1386 C CG  . LEU A 1 180 ? -29.832 16.492  -7.724  1.00 17.83  ? 180  LEU A CG  1 
ATOM   1387 C CD1 . LEU A 1 180 ? -30.123 16.697  -6.248  1.00 19.00  ? 180  LEU A CD1 1 
ATOM   1388 C CD2 . LEU A 1 180 ? -28.784 17.516  -8.322  1.00 16.79  ? 180  LEU A CD2 1 
ATOM   1389 N N   . GLY A 1 181 ? -27.706 12.687  -9.291  1.00 12.82  ? 181  GLY A N   1 
ATOM   1390 C CA  . GLY A 1 181 ? -27.416 11.290  -9.292  1.00 13.36  ? 181  GLY A CA  1 
ATOM   1391 C C   . GLY A 1 181 ? -25.902 11.127  -9.184  1.00 13.43  ? 181  GLY A C   1 
ATOM   1392 O O   . GLY A 1 181 ? -25.215 12.111  -9.174  1.00 15.04  ? 181  GLY A O   1 
ATOM   1393 N N   . GLU A 1 182 ? -25.408 9.899   -9.133  1.00 15.43  ? 182  GLU A N   1 
ATOM   1394 C CA  . GLU A 1 182 ? -26.257 8.693   -9.108  1.00 14.32  ? 182  GLU A CA  1 
ATOM   1395 C C   . GLU A 1 182 ? -26.597 8.239   -7.703  1.00 15.15  ? 182  GLU A C   1 
ATOM   1396 O O   . GLU A 1 182 ? -25.699 8.056   -6.886  1.00 14.00  ? 182  GLU A O   1 
ATOM   1397 C CB  . GLU A 1 182 ? -25.588 7.538   -9.834  1.00 15.78  ? 182  GLU A CB  1 
ATOM   1398 C CG  . GLU A 1 182 ? -26.606 6.400   -10.066 1.00 15.07  ? 182  GLU A CG  1 
ATOM   1399 C CD  . GLU A 1 182 ? -26.040 5.320   -10.951 1.00 20.55  ? 182  GLU A CD  1 
ATOM   1400 O OE1 . GLU A 1 182 ? -24.849 5.439   -11.328 1.00 20.58  ? 182  GLU A OE1 1 
ATOM   1401 O OE2 . GLU A 1 182 ? -26.780 4.367   -11.255 1.00 21.90  ? 182  GLU A OE2 1 
ATOM   1402 N N   . HIS A 1 183 ? -27.901 8.065   -7.402  1.00 14.49  ? 183  HIS A N   1 
ATOM   1403 C CA  . HIS A 1 183 ? -28.301 7.727   -6.042  1.00 15.59  ? 183  HIS A CA  1 
ATOM   1404 C C   . HIS A 1 183 ? -29.530 6.848   -6.165  1.00 16.24  ? 183  HIS A C   1 
ATOM   1405 O O   . HIS A 1 183 ? -30.195 6.805   -7.232  1.00 15.63  ? 183  HIS A O   1 
ATOM   1406 C CB  . HIS A 1 183 ? -28.749 8.956   -5.172  1.00 16.50  ? 183  HIS A CB  1 
ATOM   1407 C CG  . HIS A 1 183 ? -27.880 10.166  -5.283  1.00 16.77  ? 183  HIS A CG  1 
ATOM   1408 N ND1 . HIS A 1 183 ? -26.588 10.210  -4.793  1.00 19.27  ? 183  HIS A ND1 1 
ATOM   1409 C CD2 . HIS A 1 183 ? -28.134 11.391  -5.786  1.00 10.71  ? 183  HIS A CD2 1 
ATOM   1410 C CE1 . HIS A 1 183 ? -26.064 11.392  -5.046  1.00 12.98  ? 183  HIS A CE1 1 
ATOM   1411 N NE2 . HIS A 1 183 ? -26.973 12.126  -5.660  1.00 17.76  ? 183  HIS A NE2 1 
ATOM   1412 N N   . VAL A 1 184 ? -29.847 6.186   -5.058  1.00 16.15  ? 184  VAL A N   1 
ATOM   1413 C CA  . VAL A 1 184 ? -31.180 5.623   -4.883  1.00 15.79  ? 184  VAL A CA  1 
ATOM   1414 C C   . VAL A 1 184 ? -31.985 6.622   -4.025  1.00 16.97  ? 184  VAL A C   1 
ATOM   1415 O O   . VAL A 1 184 ? -31.784 6.720   -2.804  1.00 17.93  ? 184  VAL A O   1 
ATOM   1416 C CB  . VAL A 1 184 ? -31.132 4.185   -4.288  1.00 15.24  ? 184  VAL A CB  1 
ATOM   1417 C CG1 . VAL A 1 184 ? -32.583 3.699   -3.863  1.00 12.46  ? 184  VAL A CG1 1 
ATOM   1418 C CG2 . VAL A 1 184 ? -30.542 3.242   -5.300  1.00 13.81  ? 184  VAL A CG2 1 
ATOM   1419 N N   . HIS A 1 185 ? -32.843 7.411   -4.677  1.00 17.12  ? 185  HIS A N   1 
ATOM   1420 C CA  . HIS A 1 185 ? -33.631 8.454   -3.997  1.00 16.31  ? 185  HIS A CA  1 
ATOM   1421 C C   . HIS A 1 185 ? -34.876 7.861   -3.375  1.00 17.28  ? 185  HIS A C   1 
ATOM   1422 O O   . HIS A 1 185 ? -35.486 8.498   -2.498  1.00 16.86  ? 185  HIS A O   1 
ATOM   1423 C CB  . HIS A 1 185 ? -34.023 9.615   -4.944  1.00 16.02  ? 185  HIS A CB  1 
ATOM   1424 C CG  . HIS A 1 185 ? -32.836 10.371  -5.509  1.00 16.85  ? 185  HIS A CG  1 
ATOM   1425 N ND1 . HIS A 1 185 ? -32.776 10.804  -6.820  1.00 14.86  ? 185  HIS A ND1 1 
ATOM   1426 C CD2 . HIS A 1 185 ? -31.660 10.748  -4.937  1.00 17.89  ? 185  HIS A CD2 1 
ATOM   1427 C CE1 . HIS A 1 185 ? -31.619 11.416  -7.029  1.00 19.89  ? 185  HIS A CE1 1 
ATOM   1428 N NE2 . HIS A 1 185 ? -30.907 11.374  -5.911  1.00 16.39  ? 185  HIS A NE2 1 
ATOM   1429 N N   . GLN A 1 186 ? -35.242 6.670   -3.832  1.00 18.17  ? 186  GLN A N   1 
ATOM   1430 C CA  . GLN A 1 186 ? -36.449 5.929   -3.381  1.00 20.28  ? 186  GLN A CA  1 
ATOM   1431 C C   . GLN A 1 186 ? -37.724 6.569   -3.861  1.00 21.61  ? 186  GLN A C   1 
ATOM   1432 O O   . GLN A 1 186 ? -38.675 5.877   -4.139  1.00 24.49  ? 186  GLN A O   1 
ATOM   1433 C CB  . GLN A 1 186 ? -36.476 5.701   -1.873  1.00 19.75  ? 186  GLN A CB  1 
ATOM   1434 C CG  . GLN A 1 186 ? -35.129 5.180   -1.338  1.00 20.96  ? 186  GLN A CG  1 
ATOM   1435 C CD  . GLN A 1 186 ? -35.220 4.828   0.121   1.00 24.27  ? 186  GLN A CD  1 
ATOM   1436 O OE1 . GLN A 1 186 ? -36.310 4.558   0.646   1.00 24.84  ? 186  GLN A OE1 1 
ATOM   1437 N NE2 . GLN A 1 186 ? -34.104 4.837   0.781   1.00 23.70  ? 186  GLN A NE2 1 
ATOM   1438 N N   . GLN A 1 187 ? -37.747 7.882   -4.025  1.00 21.91  ? 187  GLN A N   1 
ATOM   1439 C CA  . GLN A 1 187 ? -38.905 8.507   -4.652  1.00 20.81  ? 187  GLN A CA  1 
ATOM   1440 C C   . GLN A 1 187 ? -38.379 9.331   -5.824  1.00 19.56  ? 187  GLN A C   1 
ATOM   1441 O O   . GLN A 1 187 ? -37.186 9.501   -5.954  1.00 19.25  ? 187  GLN A O   1 
ATOM   1442 C CB  . GLN A 1 187 ? -39.675 9.329   -3.633  1.00 21.71  ? 187  GLN A CB  1 
ATOM   1443 C CG  . GLN A 1 187 ? -38.832 10.473  -3.067  1.00 25.12  ? 187  GLN A CG  1 
ATOM   1444 C CD  . GLN A 1 187 ? -39.372 11.027  -1.751  1.00 33.05  ? 187  GLN A CD  1 
ATOM   1445 O OE1 . GLN A 1 187 ? -39.919 12.140  -1.705  1.00 37.77  ? 187  GLN A OE1 1 
ATOM   1446 N NE2 . GLN A 1 187 ? -39.201 10.264  -0.673  1.00 35.31  ? 187  GLN A NE2 1 
ATOM   1447 N N   . TYR A 1 188 ? -39.253 9.817   -6.692  1.00 18.37  ? 188  TYR A N   1 
ATOM   1448 C CA  . TYR A 1 188 ? -38.802 10.576  -7.840  1.00 18.09  ? 188  TYR A CA  1 
ATOM   1449 C C   . TYR A 1 188 ? -38.766 12.103  -7.563  1.00 18.41  ? 188  TYR A C   1 
ATOM   1450 O O   . TYR A 1 188 ? -37.758 12.779  -7.843  1.00 18.35  ? 188  TYR A O   1 
ATOM   1451 C CB  . TYR A 1 188 ? -39.672 10.235  -9.082  1.00 18.12  ? 188  TYR A CB  1 
ATOM   1452 C CG  . TYR A 1 188 ? -39.226 10.928  -10.347 1.00 16.32  ? 188  TYR A CG  1 
ATOM   1453 C CD1 . TYR A 1 188 ? -37.925 10.785  -10.832 1.00 17.82  ? 188  TYR A CD1 1 
ATOM   1454 C CD2 . TYR A 1 188 ? -40.094 11.764  -11.037 1.00 14.45  ? 188  TYR A CD2 1 
ATOM   1455 C CE1 . TYR A 1 188 ? -37.493 11.433  -11.984 1.00 15.63  ? 188  TYR A CE1 1 
ATOM   1456 C CE2 . TYR A 1 188 ? -39.670 12.435  -12.214 1.00 14.76  ? 188  TYR A CE2 1 
ATOM   1457 C CZ  . TYR A 1 188 ? -38.376 12.262  -12.662 1.00 15.68  ? 188  TYR A CZ  1 
ATOM   1458 O OH  . TYR A 1 188 ? -37.978 12.912  -13.802 1.00 16.43  ? 188  TYR A OH  1 
ATOM   1459 N N   . ARG A 1 189 ? -39.860 12.658  -7.050  1.00 17.22  ? 189  ARG A N   1 
ATOM   1460 C CA  . ARG A 1 189 ? -39.855 14.055  -6.649  1.00 17.44  ? 189  ARG A CA  1 
ATOM   1461 C C   . ARG A 1 189 ? -39.062 14.183  -5.363  1.00 18.65  ? 189  ARG A C   1 
ATOM   1462 O O   . ARG A 1 189 ? -39.253 13.440  -4.410  1.00 18.74  ? 189  ARG A O   1 
ATOM   1463 C CB  . ARG A 1 189 ? -41.243 14.606  -6.406  1.00 18.33  ? 189  ARG A CB  1 
ATOM   1464 C CG  . ARG A 1 189 ? -41.166 16.099  -6.140  1.00 18.20  ? 189  ARG A CG  1 
ATOM   1465 C CD  . ARG A 1 189 ? -42.504 16.765  -5.994  1.00 21.57  ? 189  ARG A CD  1 
ATOM   1466 N NE  . ARG A 1 189 ? -43.356 16.213  -4.950  1.00 25.11  ? 189  ARG A NE  1 
ATOM   1467 C CZ  . ARG A 1 189 ? -44.636 16.585  -4.813  1.00 31.37  ? 189  ARG A CZ  1 
ATOM   1468 N NH1 . ARG A 1 189 ? -45.142 17.533  -5.607  1.00 29.51  ? 189  ARG A NH1 1 
ATOM   1469 N NH2 . ARG A 1 189 ? -45.415 16.036  -3.880  1.00 31.12  ? 189  ARG A NH2 1 
ATOM   1470 N N   . HIS A 1 190 ? -38.152 15.123  -5.341  1.00 18.92  ? 190  HIS A N   1 
ATOM   1471 C CA  . HIS A 1 190 ? -37.277 15.225  -4.183  1.00 21.48  ? 190  HIS A CA  1 
ATOM   1472 C C   . HIS A 1 190 ? -37.923 15.560  -2.873  1.00 23.95  ? 190  HIS A C   1 
ATOM   1473 O O   . HIS A 1 190 ? -38.782 16.439  -2.782  1.00 24.87  ? 190  HIS A O   1 
ATOM   1474 C CB  . HIS A 1 190 ? -36.145 16.172  -4.470  1.00 20.55  ? 190  HIS A CB  1 
ATOM   1475 C CG  . HIS A 1 190 ? -34.988 15.470  -5.065  1.00 21.66  ? 190  HIS A CG  1 
ATOM   1476 N ND1 . HIS A 1 190 ? -34.809 15.349  -6.425  1.00 24.36  ? 190  HIS A ND1 1 
ATOM   1477 C CD2 . HIS A 1 190 ? -33.994 14.766  -4.489  1.00 22.56  ? 190  HIS A CD2 1 
ATOM   1478 C CE1 . HIS A 1 190 ? -33.700 14.670  -6.662  1.00 19.61  ? 190  HIS A CE1 1 
ATOM   1479 N NE2 . HIS A 1 190 ? -33.196 14.293  -5.503  1.00 24.62  ? 190  HIS A NE2 1 
ATOM   1480 N N   . ASP A 1 191 ? -37.512 14.808  -1.855  1.00 26.34  ? 191  ASP A N   1 
ATOM   1481 C CA  . ASP A 1 191 ? -37.707 15.229  -0.491  1.00 27.64  ? 191  ASP A CA  1 
ATOM   1482 C C   . ASP A 1 191 ? -36.842 16.476  -0.263  1.00 27.45  ? 191  ASP A C   1 
ATOM   1483 O O   . ASP A 1 191 ? -35.588 16.381  -0.178  1.00 25.73  ? 191  ASP A O   1 
ATOM   1484 C CB  . ASP A 1 191 ? -37.298 14.106  0.442   1.00 29.00  ? 191  ASP A CB  1 
ATOM   1485 C CG  . ASP A 1 191 ? -37.691 14.384  1.858   1.00 33.46  ? 191  ASP A CG  1 
ATOM   1486 O OD1 . ASP A 1 191 ? -37.976 15.570  2.152   1.00 35.00  ? 191  ASP A OD1 1 
ATOM   1487 O OD2 . ASP A 1 191 ? -37.733 13.422  2.666   1.00 39.73  ? 191  ASP A OD2 1 
ATOM   1488 N N   . MET A 1 192 ? -37.514 17.640  -0.203  1.00 26.93  ? 192  MET A N   1 
ATOM   1489 C CA  . MET A 1 192 ? -36.858 18.946  0.063   1.00 25.98  ? 192  MET A CA  1 
ATOM   1490 C C   . MET A 1 192 ? -36.640 19.186  1.553   1.00 26.78  ? 192  MET A C   1 
ATOM   1491 O O   . MET A 1 192 ? -36.235 20.268  1.934   1.00 25.85  ? 192  MET A O   1 
ATOM   1492 C CB  . MET A 1 192 ? -37.643 20.134  -0.552  1.00 25.47  ? 192  MET A CB  1 
ATOM   1493 C CG  . MET A 1 192 ? -37.745 20.166  -2.115  1.00 24.98  ? 192  MET A CG  1 
ATOM   1494 S SD  . MET A 1 192 ? -36.136 20.022  -2.988  1.00 26.24  ? 192  MET A SD  1 
ATOM   1495 C CE  . MET A 1 192 ? -35.496 21.679  -2.767  1.00 25.02  ? 192  MET A CE  1 
ATOM   1496 N N   . ASN A 1 193 ? -36.892 18.180  2.391   1.00 26.68  ? 193  ASN A N   1 
ATOM   1497 C CA  . ASN A 1 193 ? -36.764 18.336  3.830   1.00 27.87  ? 193  ASN A CA  1 
ATOM   1498 C C   . ASN A 1 193 ? -35.345 18.127  4.419   1.00 26.96  ? 193  ASN A C   1 
ATOM   1499 O O   . ASN A 1 193 ? -35.073 17.141  5.121   1.00 28.88  ? 193  ASN A O   1 
ATOM   1500 C CB  . ASN A 1 193 ? -37.800 17.487  4.567   1.00 29.03  ? 193  ASN A CB  1 
ATOM   1501 C CG  . ASN A 1 193 ? -39.214 18.081  4.488   1.00 33.16  ? 193  ASN A CG  1 
ATOM   1502 O OD1 . ASN A 1 193 ? -40.198 17.343  4.412   1.00 41.17  ? 193  ASN A OD1 1 
ATOM   1503 N ND2 . ASN A 1 193 ? -39.318 19.408  4.519   1.00 34.65  ? 193  ASN A ND2 1 
ATOM   1504 N N   . TRP A 1 194 ? -34.462 19.065  4.146   1.00 24.49  ? 194  TRP A N   1 
ATOM   1505 C CA  . TRP A 1 194 ? -33.094 19.028  4.677   1.00 23.25  ? 194  TRP A CA  1 
ATOM   1506 C C   . TRP A 1 194 ? -32.441 17.707  4.341   1.00 23.28  ? 194  TRP A C   1 
ATOM   1507 O O   . TRP A 1 194 ? -32.327 16.825  5.203   1.00 25.90  ? 194  TRP A O   1 
ATOM   1508 C CB  . TRP A 1 194 ? -33.099 19.234  6.193   1.00 21.70  ? 194  TRP A CB  1 
ATOM   1509 C CG  . TRP A 1 194 ? -33.818 20.478  6.632   1.00 19.70  ? 194  TRP A CG  1 
ATOM   1510 C CD1 . TRP A 1 194 ? -35.094 20.557  7.180   1.00 19.08  ? 194  TRP A CD1 1 
ATOM   1511 C CD2 . TRP A 1 194 ? -33.327 21.822  6.551   1.00 17.48  ? 194  TRP A CD2 1 
ATOM   1512 N NE1 . TRP A 1 194 ? -35.406 21.872  7.443   1.00 16.62  ? 194  TRP A NE1 1 
ATOM   1513 C CE2 . TRP A 1 194 ? -34.342 22.668  7.078   1.00 19.23  ? 194  TRP A CE2 1 
ATOM   1514 C CE3 . TRP A 1 194 ? -32.106 22.397  6.106   1.00 17.52  ? 194  TRP A CE3 1 
ATOM   1515 C CZ2 . TRP A 1 194 ? -34.186 24.061  7.165   1.00 17.48  ? 194  TRP A CZ2 1 
ATOM   1516 C CZ3 . TRP A 1 194 ? -31.947 23.757  6.194   1.00 16.77  ? 194  TRP A CZ3 1 
ATOM   1517 C CH2 . TRP A 1 194 ? -32.986 24.590  6.721   1.00 19.75  ? 194  TRP A CH2 1 
ATOM   1518 N N   . LYS A 1 195 ? -32.045 17.548  3.088   1.00 21.71  ? 195  LYS A N   1 
ATOM   1519 C CA  . LYS A 1 195 ? -31.401 16.313  2.614   1.00 20.90  ? 195  LYS A CA  1 
ATOM   1520 C C   . LYS A 1 195 ? -30.121 16.661  1.908   1.00 19.73  ? 195  LYS A C   1 
ATOM   1521 O O   . LYS A 1 195 ? -30.097 17.630  1.136   1.00 19.49  ? 195  LYS A O   1 
ATOM   1522 C CB  . LYS A 1 195 ? -32.322 15.558  1.653   1.00 21.47  ? 195  LYS A CB  1 
ATOM   1523 C CG  . LYS A 1 195 ? -33.332 14.623  2.341   1.00 27.34  ? 195  LYS A CG  1 
ATOM   1524 C CD  . LYS A 1 195 ? -32.628 13.363  2.948   1.00 32.11  ? 195  LYS A CD  1 
ATOM   1525 C CE  . LYS A 1 195 ? -31.608 12.700  1.938   1.00 33.79  ? 195  LYS A CE  1 
ATOM   1526 N NZ  . LYS A 1 195 ? -30.817 11.447  2.368   1.00 34.11  ? 195  LYS A NZ  1 
ATOM   1527 N N   . THR A 1 196 ? -29.060 15.906  2.180   1.00 17.97  ? 196  THR A N   1 
ATOM   1528 C CA  . THR A 1 196 ? -27.768 16.123  1.515   1.00 16.74  ? 196  THR A CA  1 
ATOM   1529 C C   . THR A 1 196 ? -27.381 14.884  0.681   1.00 16.42  ? 196  THR A C   1 
ATOM   1530 O O   . THR A 1 196 ? -27.342 13.771  1.220   1.00 16.72  ? 196  THR A O   1 
ATOM   1531 C CB  . THR A 1 196 ? -26.620 16.451  2.544   1.00 17.26  ? 196  THR A CB  1 
ATOM   1532 O OG1 . THR A 1 196 ? -26.901 17.673  3.266   1.00 17.76  ? 196  THR A OG1 1 
ATOM   1533 C CG2 . THR A 1 196 ? -25.308 16.621  1.837   1.00 18.33  ? 196  THR A CG2 1 
ATOM   1534 N N   . TRP A 1 197 ? -27.057 15.082  -0.606  1.00 16.40  ? 197  TRP A N   1 
ATOM   1535 C CA  . TRP A 1 197 ? -26.752 14.005  -1.560  1.00 15.60  ? 197  TRP A CA  1 
ATOM   1536 C C   . TRP A 1 197 ? -25.326 14.135  -2.035  1.00 15.26  ? 197  TRP A C   1 
ATOM   1537 O O   . TRP A 1 197 ? -25.009 15.083  -2.761  1.00 15.78  ? 197  TRP A O   1 
ATOM   1538 C CB  . TRP A 1 197 ? -27.690 14.039  -2.776  1.00 16.19  ? 197  TRP A CB  1 
ATOM   1539 C CG  . TRP A 1 197 ? -29.129 13.704  -2.377  1.00 15.01  ? 197  TRP A CG  1 
ATOM   1540 C CD1 . TRP A 1 197 ? -30.141 14.592  -2.155  1.00 19.14  ? 197  TRP A CD1 1 
ATOM   1541 C CD2 . TRP A 1 197 ? -29.663 12.402  -2.090  1.00 17.10  ? 197  TRP A CD2 1 
ATOM   1542 N NE1 . TRP A 1 197 ? -31.288 13.918  -1.765  1.00 18.92  ? 197  TRP A NE1 1 
ATOM   1543 C CE2 . TRP A 1 197 ? -31.019 12.575  -1.718  1.00 17.67  ? 197  TRP A CE2 1 
ATOM   1544 C CE3 . TRP A 1 197 ? -29.126 11.095  -2.110  1.00 17.84  ? 197  TRP A CE3 1 
ATOM   1545 C CZ2 . TRP A 1 197 ? -31.846 11.493  -1.398  1.00 16.66  ? 197  TRP A CZ2 1 
ATOM   1546 C CZ3 . TRP A 1 197 ? -29.947 10.029  -1.792  1.00 18.65  ? 197  TRP A CZ3 1 
ATOM   1547 C CH2 . TRP A 1 197 ? -31.298 10.232  -1.433  1.00 16.94  ? 197  TRP A CH2 1 
ATOM   1548 N N   . PRO A 1 198 ? -24.458 13.211  -1.608  1.00 15.45  ? 198  PRO A N   1 
ATOM   1549 C CA  . PRO A 1 198 ? -23.086 13.314  -2.062  1.00 14.84  ? 198  PRO A CA  1 
ATOM   1550 C C   . PRO A 1 198 ? -22.954 12.741  -3.476  1.00 14.91  ? 198  PRO A C   1 
ATOM   1551 O O   . PRO A 1 198 ? -23.661 11.802  -3.828  1.00 14.75  ? 198  PRO A O   1 
ATOM   1552 C CB  . PRO A 1 198 ? -22.347 12.459  -1.037  1.00 15.13  ? 198  PRO A CB  1 
ATOM   1553 C CG  . PRO A 1 198 ? -23.341 11.364  -0.680  1.00 16.56  ? 198  PRO A CG  1 
ATOM   1554 C CD  . PRO A 1 198 ? -24.659 12.093  -0.655  1.00 14.36  ? 198  PRO A CD  1 
ATOM   1555 N N   . ILE A 1 199 ? -22.065 13.301  -4.288  1.00 14.42  ? 199  ILE A N   1 
ATOM   1556 C CA  . ILE A 1 199 ? -21.868 12.828  -5.632  1.00 14.41  ? 199  ILE A CA  1 
ATOM   1557 C C   . ILE A 1 199 ? -20.373 12.612  -5.799  1.00 14.63  ? 199  ILE A C   1 
ATOM   1558 O O   . ILE A 1 199 ? -19.592 13.564  -5.743  1.00 13.91  ? 199  ILE A O   1 
ATOM   1559 C CB  . ILE A 1 199 ? -22.356 13.876  -6.663  1.00 15.51  ? 199  ILE A CB  1 
ATOM   1560 C CG1 . ILE A 1 199 ? -23.866 14.132  -6.440  1.00 16.16  ? 199  ILE A CG1 1 
ATOM   1561 C CG2 . ILE A 1 199 ? -22.032 13.400  -8.095  1.00 15.11  ? 199  ILE A CG2 1 
ATOM   1562 C CD1 . ILE A 1 199 ? -24.455 15.286  -7.275  1.00 16.36  ? 199  ILE A CD1 1 
ATOM   1563 N N   . PHE A 1 200 ? -20.002 11.353  -5.977  1.00 14.05  ? 200  PHE A N   1 
ATOM   1564 C CA  . PHE A 1 200 ? -18.585 10.988  -6.185  1.00 14.98  ? 200  PHE A CA  1 
ATOM   1565 C C   . PHE A 1 200 ? -18.600 9.533   -6.581  1.00 14.72  ? 200  PHE A C   1 
ATOM   1566 O O   . PHE A 1 200 ? -19.032 8.655   -5.804  1.00 16.33  ? 200  PHE A O   1 
ATOM   1567 C CB  . PHE A 1 200 ? -17.819 11.147  -4.888  1.00 15.22  ? 200  PHE A CB  1 
ATOM   1568 C CG  . PHE A 1 200 ? -16.344 10.969  -5.062  1.00 16.54  ? 200  PHE A CG  1 
ATOM   1569 C CD1 . PHE A 1 200 ? -15.627 11.878  -5.804  1.00 16.54  ? 200  PHE A CD1 1 
ATOM   1570 C CD2 . PHE A 1 200 ? -15.727 9.877   -4.522  1.00 17.31  ? 200  PHE A CD2 1 
ATOM   1571 C CE1 . PHE A 1 200 ? -14.224 11.729  -5.965  1.00 17.76  ? 200  PHE A CE1 1 
ATOM   1572 C CE2 . PHE A 1 200 ? -14.348 9.706   -4.697  1.00 21.43  ? 200  PHE A CE2 1 
ATOM   1573 C CZ  . PHE A 1 200 ? -13.634 10.625  -5.410  1.00 17.29  ? 200  PHE A CZ  1 
ATOM   1574 N N   . ASN A 1 201 ? -18.154 9.282   -7.801  1.00 15.55  ? 201  ASN A N   1 
ATOM   1575 C CA  . ASN A 1 201 ? -18.311 7.984   -8.429  1.00 14.86  ? 201  ASN A CA  1 
ATOM   1576 C C   . ASN A 1 201 ? -17.732 6.891   -7.585  1.00 16.35  ? 201  ASN A C   1 
ATOM   1577 O O   . ASN A 1 201 ? -16.548 6.906   -7.216  1.00 15.19  ? 201  ASN A O   1 
ATOM   1578 C CB  . ASN A 1 201 ? -17.703 8.012   -9.802  1.00 16.24  ? 201  ASN A CB  1 
ATOM   1579 C CG  . ASN A 1 201 ? -18.493 8.893   -10.748 1.00 14.11  ? 201  ASN A CG  1 
ATOM   1580 O OD1 . ASN A 1 201 ? -19.529 9.446   -10.358 1.00 21.23  ? 201  ASN A OD1 1 
ATOM   1581 N ND2 . ASN A 1 201 ? -18.074 8.963   -12.004 1.00 14.78  ? 201  ASN A ND2 1 
ATOM   1582 N N   . ARG A 1 202 ? -18.573 5.939   -7.262  1.00 15.11  ? 202  ARG A N   1 
ATOM   1583 C CA  . ARG A 1 202 ? -18.190 4.937   -6.244  1.00 15.86  ? 202  ARG A CA  1 
ATOM   1584 C C   . ARG A 1 202 ? -18.909 3.627   -6.467  1.00 16.81  ? 202  ARG A C   1 
ATOM   1585 O O   . ARG A 1 202 ? -20.162 3.578   -6.694  1.00 14.85  ? 202  ARG A O   1 
ATOM   1586 C CB  . ARG A 1 202 ? -18.439 5.483   -4.828  1.00 15.46  ? 202  ARG A CB  1 
ATOM   1587 C CG  . ARG A 1 202 ? -18.432 4.452   -3.700  1.00 15.79  ? 202  ARG A CG  1 
ATOM   1588 C CD  . ARG A 1 202 ? -17.009 3.923   -3.446  1.00 17.84  ? 202  ARG A CD  1 
ATOM   1589 N NE  . ARG A 1 202 ? -17.077 2.742   -2.577  1.00 21.06  ? 202  ARG A NE  1 
ATOM   1590 C CZ  . ARG A 1 202 ? -16.846 2.751   -1.261  1.00 22.83  ? 202  ARG A CZ  1 
ATOM   1591 N NH1 . ARG A 1 202 ? -16.507 3.872   -0.634  1.00 20.16  ? 202  ARG A NH1 1 
ATOM   1592 N NH2 . ARG A 1 202 ? -16.969 1.626   -0.573  1.00 22.36  ? 202  ARG A NH2 1 
ATOM   1593 N N   . ASP A 1 203 ? -18.117 2.557   -6.414  1.00 18.55  ? 203  ASP A N   1 
ATOM   1594 C CA  . ASP A 1 203 ? -18.619 1.204   -6.413  1.00 20.38  ? 203  ASP A CA  1 
ATOM   1595 C C   . ASP A 1 203 ? -19.244 0.905   -5.061  1.00 20.97  ? 203  ASP A C   1 
ATOM   1596 O O   . ASP A 1 203 ? -18.532 0.616   -4.084  1.00 20.40  ? 203  ASP A O   1 
ATOM   1597 C CB  . ASP A 1 203 ? -17.443 0.244   -6.697  1.00 20.93  ? 203  ASP A CB  1 
ATOM   1598 C CG  . ASP A 1 203 ? -17.862 -1.229  -6.760  1.00 23.62  ? 203  ASP A CG  1 
ATOM   1599 O OD1 . ASP A 1 203 ? -19.071 -1.562  -6.607  1.00 24.39  ? 203  ASP A OD1 1 
ATOM   1600 O OD2 . ASP A 1 203 ? -16.938 -2.048  -6.996  1.00 27.53  ? 203  ASP A OD2 1 
ATOM   1601 N N   . THR A 1 204 ? -20.566 1.023   -4.975  1.00 21.12  ? 204  THR A N   1 
ATOM   1602 C CA  . THR A 1 204 ? -21.256 0.542   -3.807  1.00 23.93  ? 204  THR A CA  1 
ATOM   1603 C C   . THR A 1 204 ? -22.655 0.183   -4.090  1.00 22.67  ? 204  THR A C   1 
ATOM   1604 O O   . THR A 1 204 ? -23.163 0.467   -5.157  1.00 23.10  ? 204  THR A O   1 
ATOM   1605 C CB  . THR A 1 204 ? -21.341 1.505   -2.680  1.00 24.87  ? 204  THR A CB  1 
ATOM   1606 O OG1 . THR A 1 204 ? -21.565 2.816   -3.169  1.00 28.30  ? 204  THR A OG1 1 
ATOM   1607 C CG2 . THR A 1 204 ? -20.072 1.420   -1.839  1.00 30.85  ? 204  THR A CG2 1 
ATOM   1608 N N   . THR A 1 205 ? -23.286 -0.430  -3.105  1.00 21.62  ? 205  THR A N   1 
ATOM   1609 C CA  . THR A 1 205 ? -24.569 -1.041  -3.327  1.00 21.89  ? 205  THR A CA  1 
ATOM   1610 C C   . THR A 1 205 ? -25.667 0.008   -3.413  1.00 21.14  ? 205  THR A C   1 
ATOM   1611 O O   . THR A 1 205 ? -25.808 0.834   -2.522  1.00 20.71  ? 205  THR A O   1 
ATOM   1612 C CB  . THR A 1 205 ? -24.897 -2.025  -2.209  1.00 22.98  ? 205  THR A CB  1 
ATOM   1613 O OG1 . THR A 1 205 ? -23.807 -2.931  -2.059  1.00 27.00  ? 205  THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 205 ? -26.142 -2.806  -2.551  1.00 20.35  ? 205  THR A CG2 1 
ATOM   1615 N N   . PRO A 1 206 ? -26.456 -0.034  -4.492  1.00 20.80  ? 206  PRO A N   1 
ATOM   1616 C CA  . PRO A 1 206 ? -27.635 0.826   -4.545  1.00 20.81  ? 206  PRO A CA  1 
ATOM   1617 C C   . PRO A 1 206 ? -28.714 0.365   -3.579  1.00 21.58  ? 206  PRO A C   1 
ATOM   1618 O O   . PRO A 1 206 ? -29.669 -0.321  -3.970  1.00 23.85  ? 206  PRO A O   1 
ATOM   1619 C CB  . PRO A 1 206 ? -28.131 0.684   -5.979  1.00 20.11  ? 206  PRO A CB  1 
ATOM   1620 C CG  . PRO A 1 206 ? -27.602 -0.678  -6.441  1.00 21.22  ? 206  PRO A CG  1 
ATOM   1621 C CD  . PRO A 1 206 ? -26.288 -0.871  -5.700  1.00 20.67  ? 206  PRO A CD  1 
ATOM   1622 N N   . ASN A 1 207 ? -28.637 0.826   -2.349  1.00 21.66  ? 207  ASN A N   1 
ATOM   1623 C CA  . ASN A 1 207 ? -29.584 0.358   -1.323  1.00 21.70  ? 207  ASN A CA  1 
ATOM   1624 C C   . ASN A 1 207 ? -30.321 1.534   -0.686  1.00 21.55  ? 207  ASN A C   1 
ATOM   1625 O O   . ASN A 1 207 ? -30.323 2.652   -1.223  1.00 21.09  ? 207  ASN A O   1 
ATOM   1626 C CB  . ASN A 1 207 ? -28.821 -0.489  -0.282  1.00 22.15  ? 207  ASN A CB  1 
ATOM   1627 C CG  . ASN A 1 207 ? -27.670 0.272   0.337   1.00 23.29  ? 207  ASN A CG  1 
ATOM   1628 O OD1 . ASN A 1 207 ? -27.729 1.487   0.425   1.00 26.09  ? 207  ASN A OD1 1 
ATOM   1629 N ND2 . ASN A 1 207 ? -26.617 -0.429  0.761   1.00 24.59  ? 207  ASN A ND2 1 
ATOM   1630 N N   . GLY A 1 208 ? -30.916 1.297   0.475   1.00 21.11  ? 208  GLY A N   1 
ATOM   1631 C CA  . GLY A 1 208 ? -31.654 2.344   1.192   1.00 22.23  ? 208  GLY A CA  1 
ATOM   1632 C C   . GLY A 1 208 ? -30.851 3.404   1.913   1.00 22.67  ? 208  GLY A C   1 
ATOM   1633 O O   . GLY A 1 208 ? -31.436 4.271   2.522   1.00 22.38  ? 208  GLY A O   1 
ATOM   1634 N N   . ASN A 1 209 ? -29.517 3.344   1.846   1.00 23.35  ? 209  ASN A N   1 
ATOM   1635 C CA  . ASN A 1 209 ? -28.667 4.266   2.602   1.00 23.76  ? 209  ASN A CA  1 
ATOM   1636 C C   . ASN A 1 209 ? -28.380 5.612   1.946   1.00 23.19  ? 209  ASN A C   1 
ATOM   1637 O O   . ASN A 1 209 ? -27.741 6.475   2.560   1.00 23.72  ? 209  ASN A O   1 
ATOM   1638 C CB  . ASN A 1 209 ? -27.337 3.590   2.982   1.00 24.45  ? 209  ASN A CB  1 
ATOM   1639 C CG  . ASN A 1 209 ? -27.536 2.503   4.012   1.00 31.07  ? 209  ASN A CG  1 
ATOM   1640 O OD1 . ASN A 1 209 ? -28.280 2.696   4.988   1.00 35.58  ? 209  ASN A OD1 1 
ATOM   1641 N ND2 . ASN A 1 209 ? -26.947 1.330   3.766   1.00 38.41  ? 209  ASN A ND2 1 
ATOM   1642 N N   . GLY A 1 210 ? -28.829 5.794   0.713   1.00 21.86  ? 210  GLY A N   1 
ATOM   1643 C CA  . GLY A 1 210 ? -28.705 7.095   0.051   1.00 20.75  ? 210  GLY A CA  1 
ATOM   1644 C C   . GLY A 1 210 ? -27.286 7.620   -0.114  1.00 19.55  ? 210  GLY A C   1 
ATOM   1645 O O   . GLY A 1 210 ? -27.059 8.834   0.003   1.00 20.15  ? 210  GLY A O   1 
ATOM   1646 N N   . THR A 1 211 ? -26.340 6.718   -0.380  1.00 18.08  ? 211  THR A N   1 
ATOM   1647 C CA  . THR A 1 211 ? -24.946 7.094   -0.672  1.00 17.21  ? 211  THR A CA  1 
ATOM   1648 C C   . THR A 1 211 ? -24.699 7.571   -2.107  1.00 16.27  ? 211  THR A C   1 
ATOM   1649 O O   . THR A 1 211 ? -25.546 7.420   -3.015  1.00 15.30  ? 211  THR A O   1 
ATOM   1650 C CB  . THR A 1 211 ? -23.948 5.896   -0.371  1.00 16.41  ? 211  THR A CB  1 
ATOM   1651 O OG1 . THR A 1 211 ? -24.032 4.903   -1.407  1.00 17.78  ? 211  THR A OG1 1 
ATOM   1652 C CG2 . THR A 1 211 ? -24.274 5.226   0.961   1.00 17.73  ? 211  THR A CG2 1 
ATOM   1653 N N   . ASN A 1 212 ? -23.491 8.092   -2.342  1.00 14.73  ? 212  ASN A N   1 
ATOM   1654 C CA  . ASN A 1 212 ? -23.026 8.249   -3.697  1.00 14.91  ? 212  ASN A CA  1 
ATOM   1655 C C   . ASN A 1 212 ? -22.873 6.877   -4.343  1.00 15.01  ? 212  ASN A C   1 
ATOM   1656 O O   . ASN A 1 212 ? -22.487 5.914   -3.684  1.00 15.19  ? 212  ASN A O   1 
ATOM   1657 C CB  . ASN A 1 212 ? -21.643 8.935   -3.692  1.00 14.00  ? 212  ASN A CB  1 
ATOM   1658 C CG  . ASN A 1 212 ? -20.715 8.372   -2.630  1.00 15.52  ? 212  ASN A CG  1 
ATOM   1659 O OD1 . ASN A 1 212 ? -21.101 8.202   -1.454  1.00 15.45  ? 212  ASN A OD1 1 
ATOM   1660 N ND2 . ASN A 1 212 ? -19.445 8.133   -3.031  1.00 14.23  ? 212  ASN A ND2 1 
ATOM   1661 N N   . LEU A 1 213 ? -23.194 6.776   -5.625  1.00 14.08  ? 213  LEU A N   1 
ATOM   1662 C CA  . LEU A 1 213 ? -23.072 5.510   -6.331  1.00 13.62  ? 213  LEU A CA  1 
ATOM   1663 C C   . LEU A 1 213 ? -22.180 5.701   -7.554  1.00 14.39  ? 213  LEU A C   1 
ATOM   1664 O O   . LEU A 1 213 ? -21.273 6.527   -7.543  1.00 14.83  ? 213  LEU A O   1 
ATOM   1665 C CB  . LEU A 1 213 ? -24.482 4.965   -6.696  1.00 12.80  ? 213  LEU A CB  1 
ATOM   1666 C CG  . LEU A 1 213 ? -25.357 4.738   -5.469  1.00 12.88  ? 213  LEU A CG  1 
ATOM   1667 C CD1 . LEU A 1 213 ? -26.774 4.513   -6.068  1.00 10.47  ? 213  LEU A CD1 1 
ATOM   1668 C CD2 . LEU A 1 213 ? -24.934 3.595   -4.552  1.00 16.18  ? 213  LEU A CD2 1 
ATOM   1669 N N   . TYR A 1 214 ? -22.408 4.945   -8.610  1.00 15.32  ? 214  TYR A N   1 
ATOM   1670 C CA  . TYR A 1 214 ? -21.402 4.773   -9.655  1.00 15.38  ? 214  TYR A CA  1 
ATOM   1671 C C   . TYR A 1 214 ? -21.136 5.999   -10.531 1.00 17.38  ? 214  TYR A C   1 
ATOM   1672 O O   . TYR A 1 214 ? -20.018 6.128   -11.050 1.00 16.99  ? 214  TYR A O   1 
ATOM   1673 C CB  . TYR A 1 214 ? -21.797 3.618   -10.576 1.00 15.43  ? 214  TYR A CB  1 
ATOM   1674 C CG  . TYR A 1 214 ? -22.317 2.460   -9.834  1.00 16.23  ? 214  TYR A CG  1 
ATOM   1675 C CD1 . TYR A 1 214 ? -21.435 1.592   -9.189  1.00 14.96  ? 214  TYR A CD1 1 
ATOM   1676 C CD2 . TYR A 1 214 ? -23.682 2.223   -9.736  1.00 12.40  ? 214  TYR A CD2 1 
ATOM   1677 C CE1 . TYR A 1 214 ? -21.890 0.492   -8.463  1.00 16.25  ? 214  TYR A CE1 1 
ATOM   1678 C CE2 . TYR A 1 214 ? -24.142 1.123   -8.998  1.00 17.44  ? 214  TYR A CE2 1 
ATOM   1679 C CZ  . TYR A 1 214 ? -23.250 0.271   -8.395  1.00 15.28  ? 214  TYR A CZ  1 
ATOM   1680 O OH  . TYR A 1 214 ? -23.647 -0.847  -7.721  1.00 17.92  ? 214  TYR A OH  1 
ATOM   1681 N N   . GLY A 1 215 ? -22.146 6.880   -10.677 1.00 15.88  ? 215  GLY A N   1 
ATOM   1682 C CA  . GLY A 1 215 ? -22.058 8.011   -11.609 1.00 16.04  ? 215  GLY A CA  1 
ATOM   1683 C C   . GLY A 1 215 ? -22.208 9.389   -10.985 1.00 14.57  ? 215  GLY A C   1 
ATOM   1684 O O   . GLY A 1 215 ? -22.538 9.514   -9.830  1.00 16.32  ? 215  GLY A O   1 
ATOM   1685 N N   . ALA A 1 216 ? -21.985 10.435  -11.762 1.00 14.50  ? 216  ALA A N   1 
ATOM   1686 C CA  . ALA A 1 216 ? -22.031 11.778  -11.229 1.00 14.60  ? 216  ALA A CA  1 
ATOM   1687 C C   . ALA A 1 216 ? -22.882 12.623  -12.158 1.00 14.78  ? 216  ALA A C   1 
ATOM   1688 O O   . ALA A 1 216 ? -22.510 12.842  -13.312 1.00 15.51  ? 216  ALA A O   1 
ATOM   1689 C CB  . ALA A 1 216 ? -20.584 12.378  -11.142 1.00 15.05  ? 216  ALA A CB  1 
ATOM   1690 N N   . GLN A 1 217 ? -24.027 13.068  -11.665 1.00 14.89  ? 217  GLN A N   1 
ATOM   1691 C CA  . GLN A 1 217 ? -25.036 13.747  -12.503 1.00 15.39  ? 217  GLN A CA  1 
ATOM   1692 C C   . GLN A 1 217 ? -25.602 14.958  -11.713 1.00 16.14  ? 217  GLN A C   1 
ATOM   1693 O O   . GLN A 1 217 ? -26.369 14.769  -10.756 1.00 15.74  ? 217  GLN A O   1 
ATOM   1694 C CB  . GLN A 1 217 ? -26.160 12.776  -12.895 1.00 15.22  ? 217  GLN A CB  1 
ATOM   1695 C CG  . GLN A 1 217 ? -25.724 11.488  -13.708 1.00 13.85  ? 217  GLN A CG  1 
ATOM   1696 C CD  . GLN A 1 217 ? -25.308 11.819  -15.116 1.00 16.09  ? 217  GLN A CD  1 
ATOM   1697 O OE1 . GLN A 1 217 ? -25.608 12.905  -15.644 1.00 14.97  ? 217  GLN A OE1 1 
ATOM   1698 N NE2 . GLN A 1 217 ? -24.603 10.909  -15.736 1.00 15.19  ? 217  GLN A NE2 1 
ATOM   1699 N N   . THR A 1 218 ? -25.162 16.181  -12.055 1.00 15.09  ? 218  THR A N   1 
ATOM   1700 C CA  . THR A 1 218 ? -25.525 17.347  -11.259 1.00 16.36  ? 218  THR A CA  1 
ATOM   1701 C C   . THR A 1 218 ? -26.798 18.041  -11.797 1.00 15.56  ? 218  THR A C   1 
ATOM   1702 O O   . THR A 1 218 ? -27.322 18.980  -11.183 1.00 18.13  ? 218  THR A O   1 
ATOM   1703 C CB  . THR A 1 218 ? -24.417 18.371  -11.237 1.00 16.88  ? 218  THR A CB  1 
ATOM   1704 O OG1 . THR A 1 218 ? -24.202 18.834  -12.568 1.00 17.83  ? 218  THR A OG1 1 
ATOM   1705 C CG2 . THR A 1 218 ? -23.094 17.762  -10.720 1.00 15.41  ? 218  THR A CG2 1 
ATOM   1706 N N   . PHE A 1 219 ? -27.305 17.557  -12.919 1.00 14.96  ? 219  PHE A N   1 
ATOM   1707 C CA  . PHE A 1 219 ? -28.523 18.126  -13.476 1.00 13.24  ? 219  PHE A CA  1 
ATOM   1708 C C   . PHE A 1 219 ? -29.761 17.920  -12.587 1.00 14.16  ? 219  PHE A C   1 
ATOM   1709 O O   . PHE A 1 219 ? -30.045 16.824  -12.096 1.00 13.89  ? 219  PHE A O   1 
ATOM   1710 C CB  . PHE A 1 219 ? -28.779 17.536  -14.864 1.00 13.90  ? 219  PHE A CB  1 
ATOM   1711 C CG  . PHE A 1 219 ? -30.081 18.045  -15.515 1.00 12.91  ? 219  PHE A CG  1 
ATOM   1712 C CD1 . PHE A 1 219 ? -30.146 19.358  -15.998 1.00 13.51  ? 219  PHE A CD1 1 
ATOM   1713 C CD2 . PHE A 1 219 ? -31.207 17.229  -15.597 1.00 16.22  ? 219  PHE A CD2 1 
ATOM   1714 C CE1 . PHE A 1 219 ? -31.319 19.868  -16.581 1.00 15.58  ? 219  PHE A CE1 1 
ATOM   1715 C CE2 . PHE A 1 219 ? -32.391 17.725  -16.182 1.00 16.14  ? 219  PHE A CE2 1 
ATOM   1716 C CZ  . PHE A 1 219 ? -32.440 19.038  -16.679 1.00 13.51  ? 219  PHE A CZ  1 
ATOM   1717 N N   . PHE A 1 220 ? -30.549 18.977  -12.442 1.00 14.61  ? 220  PHE A N   1 
ATOM   1718 C CA  . PHE A 1 220 ? -31.931 18.787  -11.967 1.00 14.65  ? 220  PHE A CA  1 
ATOM   1719 C C   . PHE A 1 220 ? -32.913 19.623  -12.763 1.00 14.57  ? 220  PHE A C   1 
ATOM   1720 O O   . PHE A 1 220 ? -32.534 20.590  -13.371 1.00 13.74  ? 220  PHE A O   1 
ATOM   1721 C CB  . PHE A 1 220 ? -32.054 19.093  -10.473 1.00 16.48  ? 220  PHE A CB  1 
ATOM   1722 C CG  . PHE A 1 220 ? -32.021 20.570  -10.135 1.00 18.54  ? 220  PHE A CG  1 
ATOM   1723 C CD1 . PHE A 1 220 ? -33.201 21.335  -10.153 1.00 17.88  ? 220  PHE A CD1 1 
ATOM   1724 C CD2 . PHE A 1 220 ? -30.807 21.206  -9.808  1.00 20.00  ? 220  PHE A CD2 1 
ATOM   1725 C CE1 . PHE A 1 220 ? -33.184 22.689  -9.851  1.00 20.07  ? 220  PHE A CE1 1 
ATOM   1726 C CE2 . PHE A 1 220 ? -30.780 22.573  -9.502  1.00 19.25  ? 220  PHE A CE2 1 
ATOM   1727 C CZ  . PHE A 1 220 ? -31.980 23.310  -9.505  1.00 21.03  ? 220  PHE A CZ  1 
ATOM   1728 N N   . LEU A 1 221 ? -34.195 19.249  -12.692 1.00 13.63  ? 221  LEU A N   1 
ATOM   1729 C CA  . LEU A 1 221 ? -35.258 19.900  -13.400 1.00 15.46  ? 221  LEU A CA  1 
ATOM   1730 C C   . LEU A 1 221 ? -36.280 20.314  -12.346 1.00 14.89  ? 221  LEU A C   1 
ATOM   1731 O O   . LEU A 1 221 ? -36.545 19.554  -11.413 1.00 13.85  ? 221  LEU A O   1 
ATOM   1732 C CB  . LEU A 1 221 ? -35.955 18.883  -14.339 1.00 14.55  ? 221  LEU A CB  1 
ATOM   1733 C CG  . LEU A 1 221 ? -37.039 19.374  -15.282 1.00 17.54  ? 221  LEU A CG  1 
ATOM   1734 C CD1 . LEU A 1 221 ? -36.967 18.549  -16.548 1.00 18.10  ? 221  LEU A CD1 1 
ATOM   1735 C CD2 . LEU A 1 221 ? -38.381 19.111  -14.591 1.00 17.85  ? 221  LEU A CD2 1 
ATOM   1736 N N   . CYS A 1 222 ? -36.859 21.494  -12.529 1.00 15.88  ? 222  CYS A N   1 
ATOM   1737 C CA  . CYS A 1 222 ? -37.910 22.000  -11.647 1.00 15.59  ? 222  CYS A CA  1 
ATOM   1738 C C   . CYS A 1 222 ? -39.130 22.366  -12.469 1.00 16.21  ? 222  CYS A C   1 
ATOM   1739 O O   . CYS A 1 222 ? -39.049 23.202  -13.374 1.00 15.60  ? 222  CYS A O   1 
ATOM   1740 C CB  . CYS A 1 222 ? -37.407 23.224  -10.920 1.00 16.24  ? 222  CYS A CB  1 
ATOM   1741 S SG  . CYS A 1 222 ? -38.608 23.959  -9.809  1.00 20.11  ? 222  CYS A SG  1 
ATOM   1742 N N   . LEU A 1 223 ? -40.244 21.741  -12.128 1.00 16.24  ? 223  LEU A N   1 
ATOM   1743 C CA  . LEU A 1 223 ? -41.542 22.113  -12.701 1.00 16.81  ? 223  LEU A CA  1 
ATOM   1744 C C   . LEU A 1 223 ? -42.133 23.235  -11.808 1.00 17.50  ? 223  LEU A C   1 
ATOM   1745 O O   . LEU A 1 223 ? -42.487 23.012  -10.654 1.00 17.86  ? 223  LEU A O   1 
ATOM   1746 C CB  . LEU A 1 223 ? -42.471 20.911  -12.749 1.00 17.38  ? 223  LEU A CB  1 
ATOM   1747 C CG  . LEU A 1 223 ? -43.957 21.204  -13.068 1.00 15.70  ? 223  LEU A CG  1 
ATOM   1748 C CD1 . LEU A 1 223 ? -44.153 21.715  -14.483 1.00 12.47  ? 223  LEU A CD1 1 
ATOM   1749 C CD2 . LEU A 1 223 ? -44.871 20.002  -12.783 1.00 18.07  ? 223  LEU A CD2 1 
ATOM   1750 N N   . GLU A 1 224 ? -42.244 24.422  -12.391 1.00 18.37  ? 224  GLU A N   1 
ATOM   1751 C CA  . GLU A 1 224 ? -42.622 25.645  -11.685 1.00 18.46  ? 224  GLU A CA  1 
ATOM   1752 C C   . GLU A 1 224 ? -44.066 25.634  -11.235 1.00 19.68  ? 224  GLU A C   1 
ATOM   1753 O O   . GLU A 1 224 ? -44.337 26.039  -10.125 1.00 19.57  ? 224  GLU A O   1 
ATOM   1754 C CB  . GLU A 1 224 ? -42.352 26.859  -12.585 1.00 18.63  ? 224  GLU A CB  1 
ATOM   1755 C CG  . GLU A 1 224 ? -40.846 27.022  -12.905 1.00 20.21  ? 224  GLU A CG  1 
ATOM   1756 C CD  . GLU A 1 224 ? -40.575 27.876  -14.141 1.00 22.64  ? 224  GLU A CD  1 
ATOM   1757 O OE1 . GLU A 1 224 ? -41.235 28.938  -14.342 1.00 24.02  ? 224  GLU A OE1 1 
ATOM   1758 O OE2 . GLU A 1 224 ? -39.650 27.502  -14.883 1.00 23.99  ? 224  GLU A OE2 1 
ATOM   1759 N N   . ASP A 1 225 ? -44.981 25.164  -12.085 1.00 20.30  ? 225  ASP A N   1 
ATOM   1760 C CA  . ASP A 1 225 ? -46.408 25.183  -11.750 1.00 21.69  ? 225  ASP A CA  1 
ATOM   1761 C C   . ASP A 1 225 ? -47.188 24.363  -12.772 1.00 21.30  ? 225  ASP A C   1 
ATOM   1762 O O   . ASP A 1 225 ? -46.609 23.844  -13.742 1.00 20.94  ? 225  ASP A O   1 
ATOM   1763 C CB  . ASP A 1 225 ? -46.924 26.640  -11.694 1.00 22.25  ? 225  ASP A CB  1 
ATOM   1764 C CG  . ASP A 1 225 ? -46.709 27.420  -13.001 1.00 26.07  ? 225  ASP A CG  1 
ATOM   1765 O OD1 . ASP A 1 225 ? -47.113 26.964  -14.116 1.00 28.90  ? 225  ASP A OD1 1 
ATOM   1766 O OD2 . ASP A 1 225 ? -46.133 28.542  -12.930 1.00 32.88  ? 225  ASP A OD2 1 
ATOM   1767 N N   . ALA A 1 226 ? -48.493 24.259  -12.559 1.00 21.16  ? 226  ALA A N   1 
ATOM   1768 C CA  . ALA A 1 226 ? -49.354 23.444  -13.410 1.00 20.26  ? 226  ALA A CA  1 
ATOM   1769 C C   . ALA A 1 226 ? -49.417 23.873  -14.872 1.00 20.48  ? 226  ALA A C   1 
ATOM   1770 O O   . ALA A 1 226 ? -49.930 23.122  -15.698 1.00 21.44  ? 226  ALA A O   1 
ATOM   1771 C CB  . ALA A 1 226 ? -50.768 23.356  -12.809 1.00 21.18  ? 226  ALA A CB  1 
ATOM   1772 N N   . SER A 1 227 ? -48.926 25.059  -15.228 1.00 19.36  ? 227  SER A N   1 
ATOM   1773 C CA  . SER A 1 227 ? -48.913 25.438  -16.631 1.00 20.35  ? 227  SER A CA  1 
ATOM   1774 C C   . SER A 1 227 ? -47.875 24.650  -17.446 1.00 20.56  ? 227  SER A C   1 
ATOM   1775 O O   . SER A 1 227 ? -47.960 24.617  -18.680 1.00 20.81  ? 227  SER A O   1 
ATOM   1776 C CB  . SER A 1 227 ? -48.644 26.929  -16.820 1.00 21.33  ? 227  SER A CB  1 
ATOM   1777 O OG  . SER A 1 227 ? -47.333 27.224  -16.337 1.00 24.70  ? 227  SER A OG  1 
ATOM   1778 N N   . GLY A 1 228 ? -46.918 24.021  -16.756 1.00 18.06  ? 228  GLY A N   1 
ATOM   1779 C CA  . GLY A 1 228 ? -45.904 23.235  -17.443 1.00 16.46  ? 228  GLY A CA  1 
ATOM   1780 C C   . GLY A 1 228 ? -44.565 23.941  -17.453 1.00 15.70  ? 228  GLY A C   1 
ATOM   1781 O O   . GLY A 1 228 ? -43.539 23.321  -17.697 1.00 14.46  ? 228  GLY A O   1 
ATOM   1782 N N   . LEU A 1 229 ? -44.569 25.249  -17.195 1.00 15.49  ? 229  LEU A N   1 
ATOM   1783 C CA  . LEU A 1 229 ? -43.331 26.035  -17.250 1.00 15.12  ? 229  LEU A CA  1 
ATOM   1784 C C   . LEU A 1 229 ? -42.320 25.382  -16.291 1.00 15.39  ? 229  LEU A C   1 
ATOM   1785 O O   . LEU A 1 229 ? -42.673 25.067  -15.153 1.00 14.96  ? 229  LEU A O   1 
ATOM   1786 C CB  . LEU A 1 229 ? -43.573 27.485  -16.821 1.00 15.37  ? 229  LEU A CB  1 
ATOM   1787 C CG  . LEU A 1 229 ? -44.405 28.322  -17.834 1.00 13.96  ? 229  LEU A CG  1 
ATOM   1788 C CD1 . LEU A 1 229 ? -44.638 29.728  -17.309 1.00 17.25  ? 229  LEU A CD1 1 
ATOM   1789 C CD2 . LEU A 1 229 ? -43.861 28.331  -19.227 1.00 14.77  ? 229  LEU A CD2 1 
ATOM   1790 N N   . SER A 1 230 ? -41.102 25.165  -16.780 1.00 15.74  ? 230  SER A N   1 
ATOM   1791 C CA  . SER A 1 230 ? -40.116 24.356  -16.053 1.00 15.17  ? 230  SER A CA  1 
ATOM   1792 C C   . SER A 1 230 ? -38.735 24.942  -16.372 1.00 14.67  ? 230  SER A C   1 
ATOM   1793 O O   . SER A 1 230 ? -38.538 25.642  -17.381 1.00 12.60  ? 230  SER A O   1 
ATOM   1794 C CB  . SER A 1 230 ? -40.151 22.879  -16.517 1.00 13.89  ? 230  SER A CB  1 
ATOM   1795 O OG  . SER A 1 230 ? -41.402 22.246  -16.237 1.00 18.01  ? 230  SER A OG  1 
ATOM   1796 N N   . PHE A 1 231 ? -37.754 24.643  -15.527 1.00 14.15  ? 231  PHE A N   1 
ATOM   1797 C CA  . PHE A 1 231 ? -36.373 25.084  -15.880 1.00 13.42  ? 231  PHE A CA  1 
ATOM   1798 C C   . PHE A 1 231 ? -35.457 24.033  -15.309 1.00 13.65  ? 231  PHE A C   1 
ATOM   1799 O O   . PHE A 1 231 ? -35.910 23.149  -14.557 1.00 12.75  ? 231  PHE A O   1 
ATOM   1800 C CB  . PHE A 1 231 ? -36.047 26.493  -15.329 1.00 15.29  ? 231  PHE A CB  1 
ATOM   1801 C CG  . PHE A 1 231 ? -35.798 26.531  -13.854 1.00 16.62  ? 231  PHE A CG  1 
ATOM   1802 C CD1 . PHE A 1 231 ? -34.494 26.633  -13.366 1.00 17.78  ? 231  PHE A CD1 1 
ATOM   1803 C CD2 . PHE A 1 231 ? -36.865 26.434  -12.937 1.00 15.72  ? 231  PHE A CD2 1 
ATOM   1804 C CE1 . PHE A 1 231 ? -34.242 26.670  -11.983 1.00 19.73  ? 231  PHE A CE1 1 
ATOM   1805 C CE2 . PHE A 1 231 ? -36.619 26.488  -11.551 1.00 17.26  ? 231  PHE A CE2 1 
ATOM   1806 C CZ  . PHE A 1 231 ? -35.282 26.590  -11.074 1.00 18.27  ? 231  PHE A CZ  1 
ATOM   1807 N N   . GLY A 1 232 ? -34.167 24.098  -15.663 1.00 12.92  ? 232  GLY A N   1 
ATOM   1808 C CA  . GLY A 1 232 ? -33.287 23.105  -15.131 1.00 12.28  ? 232  GLY A CA  1 
ATOM   1809 C C   . GLY A 1 232 ? -31.933 23.774  -14.930 1.00 11.53  ? 232  GLY A C   1 
ATOM   1810 O O   . GLY A 1 232 ? -31.708 24.878  -15.383 1.00 12.11  ? 232  GLY A O   1 
ATOM   1811 N N   . VAL A 1 233 ? -31.091 23.116  -14.175 1.00 12.70  ? 233  VAL A N   1 
ATOM   1812 C CA  . VAL A 1 233 ? -29.766 23.670  -13.835 1.00 12.30  ? 233  VAL A CA  1 
ATOM   1813 C C   . VAL A 1 233 ? -28.737 22.556  -13.931 1.00 13.39  ? 233  VAL A C   1 
ATOM   1814 O O   . VAL A 1 233 ? -28.996 21.436  -13.495 1.00 13.11  ? 233  VAL A O   1 
ATOM   1815 C CB  . VAL A 1 233 ? -29.743 24.241  -12.392 1.00 13.04  ? 233  VAL A CB  1 
ATOM   1816 C CG1 . VAL A 1 233 ? -28.308 24.741  -12.001 1.00 10.91  ? 233  VAL A CG1 1 
ATOM   1817 C CG2 . VAL A 1 233 ? -30.718 25.424  -12.177 1.00 12.72  ? 233  VAL A CG2 1 
ATOM   1818 N N   . PHE A 1 234 ? -27.547 22.871  -14.468 1.00 12.17  ? 234  PHE A N   1 
ATOM   1819 C CA  . PHE A 1 234 ? -26.524 21.879  -14.552 1.00 12.84  ? 234  PHE A CA  1 
ATOM   1820 C C   . PHE A 1 234 ? -25.238 22.579  -14.094 1.00 12.85  ? 234  PHE A C   1 
ATOM   1821 O O   . PHE A 1 234 ? -25.011 23.728  -14.456 1.00 11.65  ? 234  PHE A O   1 
ATOM   1822 C CB  . PHE A 1 234 ? -26.379 21.412  -15.983 1.00 13.52  ? 234  PHE A CB  1 
ATOM   1823 C CG  . PHE A 1 234 ? -25.107 20.648  -16.242 1.00 12.46  ? 234  PHE A CG  1 
ATOM   1824 C CD1 . PHE A 1 234 ? -24.879 19.410  -15.613 1.00 13.18  ? 234  PHE A CD1 1 
ATOM   1825 C CD2 . PHE A 1 234 ? -24.207 21.117  -17.163 1.00 15.18  ? 234  PHE A CD2 1 
ATOM   1826 C CE1 . PHE A 1 234 ? -23.725 18.683  -15.849 1.00 16.59  ? 234  PHE A CE1 1 
ATOM   1827 C CE2 . PHE A 1 234 ? -23.012 20.376  -17.428 1.00 17.19  ? 234  PHE A CE2 1 
ATOM   1828 C CZ  . PHE A 1 234 ? -22.776 19.182  -16.740 1.00 13.46  ? 234  PHE A CZ  1 
ATOM   1829 N N   . LEU A 1 235 ? -24.471 21.895  -13.242 1.00 13.68  ? 235  LEU A N   1 
ATOM   1830 C CA  . LEU A 1 235 ? -23.140 22.360  -12.825 1.00 14.69  ? 235  LEU A CA  1 
ATOM   1831 C C   . LEU A 1 235 ? -22.088 21.499  -13.519 1.00 13.96  ? 235  LEU A C   1 
ATOM   1832 O O   . LEU A 1 235 ? -22.085 20.291  -13.327 1.00 15.08  ? 235  LEU A O   1 
ATOM   1833 C CB  . LEU A 1 235 ? -23.011 22.232  -11.302 1.00 14.85  ? 235  LEU A CB  1 
ATOM   1834 C CG  . LEU A 1 235 ? -21.596 22.473  -10.697 1.00 16.13  ? 235  LEU A CG  1 
ATOM   1835 C CD1 . LEU A 1 235 ? -21.089 23.867  -11.020 1.00 15.32  ? 235  LEU A CD1 1 
ATOM   1836 C CD2 . LEU A 1 235 ? -21.619 22.204  -9.193  1.00 17.03  ? 235  LEU A CD2 1 
ATOM   1837 N N   . MET A 1 236 ? -21.222 22.111  -14.336 1.00 13.39  ? 236  MET A N   1 
ATOM   1838 C CA  . MET A 1 236 ? -20.169 21.423  -15.049 1.00 15.18  ? 236  MET A CA  1 
ATOM   1839 C C   . MET A 1 236 ? -18.946 21.421  -14.109 1.00 15.26  ? 236  MET A C   1 
ATOM   1840 O O   . MET A 1 236 ? -18.123 22.343  -14.148 1.00 16.15  ? 236  MET A O   1 
ATOM   1841 C CB  . MET A 1 236 ? -19.766 22.204  -16.317 1.00 14.81  ? 236  MET A CB  1 
ATOM   1842 C CG  . MET A 1 236 ? -18.644 21.483  -17.127 1.00 18.22  ? 236  MET A CG  1 
ATOM   1843 S SD  . MET A 1 236 ? -19.062 19.904  -17.868 1.00 22.75  ? 236  MET A SD  1 
ATOM   1844 C CE  . MET A 1 236 ? -19.640 20.497  -19.482 1.00 22.11  ? 236  MET A CE  1 
ATOM   1845 N N   . ASN A 1 237 ? -18.869 20.398  -13.269 1.00 15.65  ? 237  ASN A N   1 
ATOM   1846 C CA  . ASN A 1 237 ? -17.823 20.269  -12.245 1.00 15.08  ? 237  ASN A CA  1 
ATOM   1847 C C   . ASN A 1 237 ? -17.726 18.782  -11.961 1.00 15.69  ? 237  ASN A C   1 
ATOM   1848 O O   . ASN A 1 237 ? -18.742 18.083  -11.781 1.00 13.81  ? 237  ASN A O   1 
ATOM   1849 C CB  . ASN A 1 237 ? -18.192 21.102  -10.982 1.00 13.33  ? 237  ASN A CB  1 
ATOM   1850 C CG  . ASN A 1 237 ? -17.099 21.061  -9.870  1.00 16.07  ? 237  ASN A CG  1 
ATOM   1851 O OD1 . ASN A 1 237 ? -16.950 20.074  -9.177  1.00 16.08  ? 237  ASN A OD1 1 
ATOM   1852 N ND2 . ASN A 1 237 ? -16.471 22.183  -9.632  1.00 14.25  ? 237  ASN A ND2 1 
ATOM   1853 N N   . SER A 1 238 ? -16.506 18.272  -11.981 1.00 14.93  ? 238  SER A N   1 
ATOM   1854 C CA  . SER A 1 238 ? -16.285 16.864  -11.725 1.00 16.82  ? 238  SER A CA  1 
ATOM   1855 C C   . SER A 1 238 ? -15.554 16.492  -10.390 1.00 17.50  ? 238  SER A C   1 
ATOM   1856 O O   . SER A 1 238 ? -15.084 15.364  -10.258 1.00 19.08  ? 238  SER A O   1 
ATOM   1857 C CB  . SER A 1 238 ? -15.490 16.306  -12.897 1.00 17.91  ? 238  SER A CB  1 
ATOM   1858 O OG  . SER A 1 238 ? -14.276 17.010  -13.006 1.00 16.26  ? 238  SER A OG  1 
ATOM   1859 N N   . ASN A 1 239 ? -15.359 17.454  -9.490  1.00 17.30  ? 239  ASN A N   1 
ATOM   1860 C CA  . ASN A 1 239 ? -14.822 17.207  -8.141  1.00 17.26  ? 239  ASN A CA  1 
ATOM   1861 C C   . ASN A 1 239 ? -15.884 16.580  -7.244  1.00 17.13  ? 239  ASN A C   1 
ATOM   1862 O O   . ASN A 1 239 ? -17.097 16.612  -7.585  1.00 16.11  ? 239  ASN A O   1 
ATOM   1863 C CB  . ASN A 1 239 ? -14.289 18.513  -7.542  1.00 16.35  ? 239  ASN A CB  1 
ATOM   1864 C CG  . ASN A 1 239 ? -13.046 18.997  -8.271  1.00 18.06  ? 239  ASN A CG  1 
ATOM   1865 O OD1 . ASN A 1 239 ? -11.914 18.665  -7.879  1.00 21.01  ? 239  ASN A OD1 1 
ATOM   1866 N ND2 . ASN A 1 239 ? -13.235 19.765  -9.329  1.00 14.42  ? 239  ASN A ND2 1 
ATOM   1867 N N   . ALA A 1 240 ? -15.453 15.957  -6.144  1.00 15.34  ? 240  ALA A N   1 
ATOM   1868 C CA  . ALA A 1 240 ? -16.419 15.472  -5.142  1.00 16.66  ? 240  ALA A CA  1 
ATOM   1869 C C   . ALA A 1 240 ? -17.272 16.619  -4.700  1.00 16.41  ? 240  ALA A C   1 
ATOM   1870 O O   . ALA A 1 240 ? -16.791 17.726  -4.505  1.00 15.75  ? 240  ALA A O   1 
ATOM   1871 C CB  . ALA A 1 240 ? -15.716 14.851  -3.915  1.00 17.10  ? 240  ALA A CB  1 
ATOM   1872 N N   . MET A 1 241 ? -18.563 16.357  -4.561  1.00 16.35  ? 241  MET A N   1 
ATOM   1873 C CA  . MET A 1 241 ? -19.424 17.415  -4.159  1.00 17.05  ? 241  MET A CA  1 
ATOM   1874 C C   . MET A 1 241 ? -20.581 16.829  -3.395  1.00 15.86  ? 241  MET A C   1 
ATOM   1875 O O   . MET A 1 241 ? -20.744 15.611  -3.330  1.00 15.20  ? 241  MET A O   1 
ATOM   1876 C CB  . MET A 1 241 ? -19.910 18.184  -5.389  1.00 17.52  ? 241  MET A CB  1 
ATOM   1877 C CG  . MET A 1 241 ? -20.841 17.402  -6.255  1.00 18.70  ? 241  MET A CG  1 
ATOM   1878 S SD  . MET A 1 241 ? -21.587 18.520  -7.461  1.00 22.43  ? 241  MET A SD  1 
ATOM   1879 C CE  . MET A 1 241 ? -20.140 18.684  -8.514  1.00 17.18  ? 241  MET A CE  1 
ATOM   1880 N N   . GLU A 1 242 ? -21.380 17.703  -2.812  1.00 16.19  ? 242  GLU A N   1 
ATOM   1881 C CA  . GLU A 1 242 ? -22.673 17.282  -2.330  1.00 16.24  ? 242  GLU A CA  1 
ATOM   1882 C C   . GLU A 1 242 ? -23.720 18.350  -2.602  1.00 16.05  ? 242  GLU A C   1 
ATOM   1883 O O   . GLU A 1 242 ? -23.416 19.522  -2.824  1.00 16.93  ? 242  GLU A O   1 
ATOM   1884 C CB  . GLU A 1 242 ? -22.632 16.880  -0.860  1.00 16.48  ? 242  GLU A CB  1 
ATOM   1885 C CG  . GLU A 1 242 ? -22.300 17.986  0.105   1.00 18.85  ? 242  GLU A CG  1 
ATOM   1886 C CD  . GLU A 1 242 ? -21.838 17.445  1.456   1.00 26.33  ? 242  GLU A CD  1 
ATOM   1887 O OE1 . GLU A 1 242 ? -21.619 16.210  1.588   1.00 25.61  ? 242  GLU A OE1 1 
ATOM   1888 O OE2 . GLU A 1 242 ? -21.673 18.265  2.391   1.00 27.60  ? 242  GLU A OE2 1 
ATOM   1889 N N   . VAL A 1 243 ? -24.974 17.941  -2.602  1.00 16.77  ? 243  VAL A N   1 
ATOM   1890 C CA  . VAL A 1 243 ? -25.999 18.875  -2.957  1.00 16.33  ? 243  VAL A CA  1 
ATOM   1891 C C   . VAL A 1 243 ? -26.950 18.849  -1.801  1.00 16.85  ? 243  VAL A C   1 
ATOM   1892 O O   . VAL A 1 243 ? -27.346 17.767  -1.363  1.00 16.50  ? 243  VAL A O   1 
ATOM   1893 C CB  . VAL A 1 243 ? -26.702 18.460  -4.294  1.00 17.36  ? 243  VAL A CB  1 
ATOM   1894 C CG1 . VAL A 1 243 ? -27.845 19.365  -4.578  1.00 16.81  ? 243  VAL A CG1 1 
ATOM   1895 C CG2 . VAL A 1 243 ? -25.720 18.536  -5.464  1.00 17.65  ? 243  VAL A CG2 1 
ATOM   1896 N N   . VAL A 1 244 ? -27.308 20.034  -1.297  1.00 15.68  ? 244  VAL A N   1 
ATOM   1897 C CA  . VAL A 1 244 ? -28.087 20.137  -0.082  1.00 15.51  ? 244  VAL A CA  1 
ATOM   1898 C C   . VAL A 1 244 ? -29.445 20.695  -0.450  1.00 14.70  ? 244  VAL A C   1 
ATOM   1899 O O   . VAL A 1 244 ? -29.543 21.752  -1.028  1.00 14.67  ? 244  VAL A O   1 
ATOM   1900 C CB  . VAL A 1 244 ? -27.430 21.068  0.912   1.00 15.53  ? 244  VAL A CB  1 
ATOM   1901 C CG1 . VAL A 1 244 ? -28.276 21.173  2.223   1.00 15.80  ? 244  VAL A CG1 1 
ATOM   1902 C CG2 . VAL A 1 244 ? -26.015 20.570  1.184   1.00 17.95  ? 244  VAL A CG2 1 
ATOM   1903 N N   . LEU A 1 245 ? -30.476 19.989  -0.070  1.00 15.64  ? 245  LEU A N   1 
ATOM   1904 C CA  . LEU A 1 245 ? -31.829 20.413  -0.428  1.00 16.01  ? 245  LEU A CA  1 
ATOM   1905 C C   . LEU A 1 245 ? -32.500 20.828  0.834   1.00 16.85  ? 245  LEU A C   1 
ATOM   1906 O O   . LEU A 1 245 ? -32.417 20.113  1.837   1.00 18.44  ? 245  LEU A O   1 
ATOM   1907 C CB  . LEU A 1 245 ? -32.587 19.240  -1.047  1.00 16.65  ? 245  LEU A CB  1 
ATOM   1908 C CG  . LEU A 1 245 ? -31.925 18.557  -2.262  1.00 17.41  ? 245  LEU A CG  1 
ATOM   1909 C CD1 . LEU A 1 245 ? -32.835 17.423  -2.686  1.00 21.49  ? 245  LEU A CD1 1 
ATOM   1910 C CD2 . LEU A 1 245 ? -31.805 19.522  -3.365  1.00 19.18  ? 245  LEU A CD2 1 
ATOM   1911 N N   . GLN A 1 246 ? -33.187 21.963  0.813   1.00 16.88  ? 246  GLN A N   1 
ATOM   1912 C CA  . GLN A 1 246 ? -33.917 22.394  2.021   1.00 16.82  ? 246  GLN A CA  1 
ATOM   1913 C C   . GLN A 1 246 ? -35.278 22.997  1.694   1.00 17.35  ? 246  GLN A C   1 
ATOM   1914 O O   . GLN A 1 246 ? -35.495 23.385  0.538   1.00 17.30  ? 246  GLN A O   1 
ATOM   1915 C CB  . GLN A 1 246 ? -33.067 23.355  2.810   1.00 16.26  ? 246  GLN A CB  1 
ATOM   1916 C CG  . GLN A 1 246 ? -32.897 24.728  2.205   1.00 15.16  ? 246  GLN A CG  1 
ATOM   1917 C CD  . GLN A 1 246 ? -31.798 25.458  2.956   1.00 17.75  ? 246  GLN A CD  1 
ATOM   1918 O OE1 . GLN A 1 246 ? -30.621 25.120  2.822   1.00 17.21  ? 246  GLN A OE1 1 
ATOM   1919 N NE2 . GLN A 1 246 ? -32.176 26.461  3.756   1.00 15.12  ? 246  GLN A NE2 1 
ATOM   1920 N N   . PRO A 1 247 ? -36.197 23.079  2.692   1.00 18.43  ? 247  PRO A N   1 
ATOM   1921 C CA  . PRO A 1 247 ? -37.587 23.415  2.385   1.00 19.17  ? 247  PRO A CA  1 
ATOM   1922 C C   . PRO A 1 247 ? -37.929 24.866  2.103   1.00 20.01  ? 247  PRO A C   1 
ATOM   1923 O O   . PRO A 1 247 ? -39.101 25.156  1.918   1.00 22.21  ? 247  PRO A O   1 
ATOM   1924 C CB  . PRO A 1 247 ? -38.364 22.967  3.646   1.00 19.28  ? 247  PRO A CB  1 
ATOM   1925 C CG  . PRO A 1 247 ? -37.374 22.358  4.556   1.00 20.54  ? 247  PRO A CG  1 
ATOM   1926 C CD  . PRO A 1 247 ? -36.022 22.798  4.118   1.00 19.53  ? 247  PRO A CD  1 
ATOM   1927 N N   . ALA A 1 248 ? -36.957 25.768  2.066   1.00 20.87  ? 248  ALA A N   1 
ATOM   1928 C CA  . ALA A 1 248 ? -37.168 27.167  1.641   1.00 20.58  ? 248  ALA A CA  1 
ATOM   1929 C C   . ALA A 1 248 ? -38.201 27.382  0.506   1.00 22.49  ? 248  ALA A C   1 
ATOM   1930 O O   . ALA A 1 248 ? -39.077 28.263  0.654   1.00 21.08  ? 248  ALA A O   1 
ATOM   1931 C CB  . ALA A 1 248 ? -35.829 27.820  1.277   1.00 20.93  ? 248  ALA A CB  1 
ATOM   1932 N N   . PRO A 1 249 ? -38.116 26.594  -0.651  1.00 20.80  ? 249  PRO A N   1 
ATOM   1933 C CA  . PRO A 1 249 ? -37.164 25.559  -1.084  1.00 19.56  ? 249  PRO A CA  1 
ATOM   1934 C C   . PRO A 1 249 ? -35.881 26.125  -1.664  1.00 18.72  ? 249  PRO A C   1 
ATOM   1935 O O   . PRO A 1 249 ? -35.886 27.201  -2.273  1.00 18.01  ? 249  PRO A O   1 
ATOM   1936 C CB  . PRO A 1 249 ? -37.924 24.811  -2.183  1.00 19.85  ? 249  PRO A CB  1 
ATOM   1937 C CG  . PRO A 1 249 ? -38.912 25.751  -2.696  1.00 20.39  ? 249  PRO A CG  1 
ATOM   1938 C CD  . PRO A 1 249 ? -39.214 26.762  -1.623  1.00 21.18  ? 249  PRO A CD  1 
ATOM   1939 N N   . ALA A 1 250 ? -34.794 25.389  -1.508  1.00 17.27  ? 250  ALA A N   1 
ATOM   1940 C CA  . ALA A 1 250 ? -33.525 25.879  -2.032  1.00 16.58  ? 250  ALA A CA  1 
ATOM   1941 C C   . ALA A 1 250 ? -32.602 24.720  -2.214  1.00 16.06  ? 250  ALA A C   1 
ATOM   1942 O O   . ALA A 1 250 ? -32.786 23.666  -1.595  1.00 14.57  ? 250  ALA A O   1 
ATOM   1943 C CB  . ALA A 1 250 ? -32.944 26.862  -1.070  1.00 16.33  ? 250  ALA A CB  1 
ATOM   1944 N N   . ILE A 1 251 ? -31.581 24.912  -3.049  1.00 15.88  ? 251  ILE A N   1 
ATOM   1945 C CA  . ILE A 1 251 ? -30.593 23.889  -3.249  1.00 16.90  ? 251  ILE A CA  1 
ATOM   1946 C C   . ILE A 1 251 ? -29.245 24.555  -3.154  1.00 16.36  ? 251  ILE A C   1 
ATOM   1947 O O   . ILE A 1 251 ? -29.099 25.677  -3.603  1.00 16.07  ? 251  ILE A O   1 
ATOM   1948 C CB  . ILE A 1 251 ? -30.781 23.142  -4.612  1.00 17.14  ? 251  ILE A CB  1 
ATOM   1949 C CG1 . ILE A 1 251 ? -29.573 22.274  -4.973  1.00 19.68  ? 251  ILE A CG1 1 
ATOM   1950 C CG2 . ILE A 1 251 ? -31.082 24.122  -5.755  1.00 21.48  ? 251  ILE A CG2 1 
ATOM   1951 C CD1 . ILE A 1 251 ? -29.904 21.192  -6.046  1.00 20.56  ? 251  ILE A CD1 1 
ATOM   1952 N N   . THR A 1 252 ? -28.290 23.866  -2.542  1.00 15.80  ? 252  THR A N   1 
ATOM   1953 C CA  . THR A 1 252 ? -26.938 24.365  -2.413  1.00 17.20  ? 252  THR A CA  1 
ATOM   1954 C C   . THR A 1 252 ? -26.009 23.332  -3.033  1.00 17.12  ? 252  THR A C   1 
ATOM   1955 O O   . THR A 1 252 ? -26.171 22.133  -2.805  1.00 16.50  ? 252  THR A O   1 
ATOM   1956 C CB  . THR A 1 252 ? -26.604 24.566  -0.932  1.00 17.66  ? 252  THR A CB  1 
ATOM   1957 O OG1 . THR A 1 252 ? -27.468 25.588  -0.400  1.00 17.39  ? 252  THR A OG1 1 
ATOM   1958 C CG2 . THR A 1 252 ? -25.154 25.001  -0.739  1.00 18.22  ? 252  THR A CG2 1 
ATOM   1959 N N   . TYR A 1 253 ? -25.073 23.797  -3.845  1.00 17.33  ? 253  TYR A N   1 
ATOM   1960 C CA  . TYR A 1 253 ? -24.029 22.949  -4.400  1.00 18.15  ? 253  TYR A CA  1 
ATOM   1961 C C   . TYR A 1 253 ? -22.773 23.276  -3.626  1.00 18.33  ? 253  TYR A C   1 
ATOM   1962 O O   . TYR A 1 253 ? -22.465 24.446  -3.443  1.00 17.41  ? 253  TYR A O   1 
ATOM   1963 C CB  . TYR A 1 253 ? -23.772 23.306  -5.858  1.00 20.12  ? 253  TYR A CB  1 
ATOM   1964 C CG  . TYR A 1 253 ? -24.803 22.803  -6.859  1.00 21.74  ? 253  TYR A CG  1 
ATOM   1965 C CD1 . TYR A 1 253 ? -24.641 21.559  -7.459  1.00 24.60  ? 253  TYR A CD1 1 
ATOM   1966 C CD2 . TYR A 1 253 ? -25.904 23.572  -7.214  1.00 24.34  ? 253  TYR A CD2 1 
ATOM   1967 C CE1 . TYR A 1 253 ? -25.569 21.068  -8.400  1.00 26.10  ? 253  TYR A CE1 1 
ATOM   1968 C CE2 . TYR A 1 253 ? -26.854 23.093  -8.161  1.00 23.29  ? 253  TYR A CE2 1 
ATOM   1969 C CZ  . TYR A 1 253 ? -26.663 21.844  -8.745  1.00 25.87  ? 253  TYR A CZ  1 
ATOM   1970 O OH  . TYR A 1 253 ? -27.560 21.348  -9.694  1.00 25.99  ? 253  TYR A OH  1 
ATOM   1971 N N   . ARG A 1 254 ? -22.035 22.244  -3.232  1.00 18.14  ? 254  ARG A N   1 
ATOM   1972 C CA  . ARG A 1 254 ? -20.849 22.377  -2.385  1.00 18.93  ? 254  ARG A CA  1 
ATOM   1973 C C   . ARG A 1 254 ? -19.833 21.441  -3.004  1.00 18.31  ? 254  ARG A C   1 
ATOM   1974 O O   . ARG A 1 254 ? -20.004 20.247  -2.902  1.00 19.86  ? 254  ARG A O   1 
ATOM   1975 C CB  . ARG A 1 254 ? -21.263 21.907  -0.981  1.00 19.75  ? 254  ARG A CB  1 
ATOM   1976 C CG  . ARG A 1 254 ? -20.310 22.192  0.203   1.00 21.04  ? 254  ARG A CG  1 
ATOM   1977 C CD  . ARG A 1 254 ? -20.930 21.600  1.462   1.00 20.45  ? 254  ARG A CD  1 
ATOM   1978 N NE  . ARG A 1 254 ? -22.033 22.395  2.038   1.00 20.41  ? 254  ARG A NE  1 
ATOM   1979 C CZ  . ARG A 1 254 ? -22.987 21.900  2.822   1.00 22.56  ? 254  ARG A CZ  1 
ATOM   1980 N NH1 . ARG A 1 254 ? -23.036 20.601  3.094   1.00 23.83  ? 254  ARG A NH1 1 
ATOM   1981 N NH2 . ARG A 1 254 ? -23.902 22.694  3.349   1.00 24.28  ? 254  ARG A NH2 1 
ATOM   1982 N N   . THR A 1 255 ? -18.788 21.951  -3.659  1.00 17.54  ? 255  THR A N   1 
ATOM   1983 C CA  . THR A 1 255 ? -17.810 21.095  -4.325  1.00 17.33  ? 255  THR A CA  1 
ATOM   1984 C C   . THR A 1 255 ? -16.395 21.392  -3.761  1.00 17.40  ? 255  THR A C   1 
ATOM   1985 O O   . THR A 1 255 ? -16.172 22.442  -3.186  1.00 17.46  ? 255  THR A O   1 
ATOM   1986 C CB  . THR A 1 255 ? -17.845 21.251  -5.861  1.00 17.59  ? 255  THR A CB  1 
ATOM   1987 O OG1 . THR A 1 255 ? -16.884 20.375  -6.474  1.00 20.52  ? 255  THR A OG1 1 
ATOM   1988 C CG2 . THR A 1 255 ? -17.561 22.672  -6.296  1.00 19.15  ? 255  THR A CG2 1 
ATOM   1989 N N   . ILE A 1 256 ? -15.460 20.475  -3.945  1.00 17.19  ? 256  ILE A N   1 
ATOM   1990 C CA  . ILE A 1 256 ? -14.134 20.627  -3.301  1.00 16.60  ? 256  ILE A CA  1 
ATOM   1991 C C   . ILE A 1 256 ? -13.031 20.898  -4.309  1.00 16.82  ? 256  ILE A C   1 
ATOM   1992 O O   . ILE A 1 256 ? -11.811 20.753  -4.020  1.00 17.23  ? 256  ILE A O   1 
ATOM   1993 C CB  . ILE A 1 256 ? -13.792 19.441  -2.348  1.00 16.94  ? 256  ILE A CB  1 
ATOM   1994 C CG1 . ILE A 1 256 ? -13.692 18.119  -3.115  1.00 16.53  ? 256  ILE A CG1 1 
ATOM   1995 C CG2 . ILE A 1 256 ? -14.831 19.308  -1.258  1.00 16.19  ? 256  ILE A CG2 1 
ATOM   1996 C CD1 . ILE A 1 256 ? -13.158 16.989  -2.261  1.00 16.99  ? 256  ILE A CD1 1 
ATOM   1997 N N   . GLY A 1 257 ? -13.435 21.328  -5.500  1.00 15.91  ? 257  GLY A N   1 
ATOM   1998 C CA  . GLY A 1 257 ? -12.432 21.880  -6.400  1.00 14.89  ? 257  GLY A CA  1 
ATOM   1999 C C   . GLY A 1 257 ? -13.044 22.425  -7.650  1.00 15.13  ? 257  GLY A C   1 
ATOM   2000 O O   . GLY A 1 257 ? -14.280 22.580  -7.751  1.00 14.56  ? 257  GLY A O   1 
ATOM   2001 N N   . GLY A 1 258 ? -12.172 22.688  -8.609  1.00 13.45  ? 258  GLY A N   1 
ATOM   2002 C CA  . GLY A 1 258 ? -12.557 23.231  -9.912  1.00 13.70  ? 258  GLY A CA  1 
ATOM   2003 C C   . GLY A 1 258 ? -13.189 24.582  -9.807  1.00 13.63  ? 258  GLY A C   1 
ATOM   2004 O O   . GLY A 1 258 ? -12.830 25.417  -8.949  1.00 13.90  ? 258  GLY A O   1 
ATOM   2005 N N   . ILE A 1 259 ? -14.207 24.802  -10.643 1.00 15.18  ? 259  ILE A N   1 
ATOM   2006 C CA  . ILE A 1 259 ? -14.839 26.110  -10.699 1.00 16.08  ? 259  ILE A CA  1 
ATOM   2007 C C   . ILE A 1 259 ? -16.363 25.938  -10.690 1.00 16.79  ? 259  ILE A C   1 
ATOM   2008 O O   . ILE A 1 259 ? -16.878 24.840  -10.937 1.00 16.42  ? 259  ILE A O   1 
ATOM   2009 C CB  . ILE A 1 259 ? -14.396 26.941  -11.985 1.00 15.91  ? 259  ILE A CB  1 
ATOM   2010 C CG1 . ILE A 1 259 ? -14.827 26.249  -13.288 1.00 16.08  ? 259  ILE A CG1 1 
ATOM   2011 C CG2 . ILE A 1 259 ? -12.865 27.134  -12.035 1.00 15.26  ? 259  ILE A CG2 1 
ATOM   2012 C CD1 . ILE A 1 259 ? -14.977 27.193  -14.523 1.00 17.06  ? 259  ILE A CD1 1 
ATOM   2013 N N   . LEU A 1 260 ? -17.058 27.032  -10.431 1.00 16.92  ? 260  LEU A N   1 
ATOM   2014 C CA  . LEU A 1 260 ? -18.521 26.983  -10.464 1.00 17.44  ? 260  LEU A CA  1 
ATOM   2015 C C   . LEU A 1 260 ? -18.904 27.377  -11.884 1.00 18.34  ? 260  LEU A C   1 
ATOM   2016 O O   . LEU A 1 260 ? -18.770 28.536  -12.256 1.00 19.85  ? 260  LEU A O   1 
ATOM   2017 C CB  . LEU A 1 260 ? -19.110 27.913  -9.411  1.00 16.45  ? 260  LEU A CB  1 
ATOM   2018 C CG  . LEU A 1 260 ? -18.884 27.472  -7.968  1.00 17.63  ? 260  LEU A CG  1 
ATOM   2019 C CD1 . LEU A 1 260 ? -19.438 28.491  -6.972  1.00 21.04  ? 260  LEU A CD1 1 
ATOM   2020 C CD2 . LEU A 1 260 ? -19.463 26.035  -7.676  1.00 17.48  ? 260  LEU A CD2 1 
ATOM   2021 N N   . ASP A 1 261 ? -19.321 26.394  -12.676 1.00 18.55  ? 261  ASP A N   1 
ATOM   2022 C CA  . ASP A 1 261 ? -19.598 26.593  -14.091 1.00 18.17  ? 261  ASP A CA  1 
ATOM   2023 C C   . ASP A 1 261 ? -21.034 26.102  -14.282 1.00 18.58  ? 261  ASP A C   1 
ATOM   2024 O O   . ASP A 1 261 ? -21.244 24.896  -14.340 1.00 17.23  ? 261  ASP A O   1 
ATOM   2025 C CB  . ASP A 1 261 ? -18.638 25.737  -14.924 1.00 19.32  ? 261  ASP A CB  1 
ATOM   2026 C CG  . ASP A 1 261 ? -18.819 25.945  -16.434 1.00 23.03  ? 261  ASP A CG  1 
ATOM   2027 O OD1 . ASP A 1 261 ? -19.764 26.662  -16.812 1.00 25.59  ? 261  ASP A OD1 1 
ATOM   2028 O OD2 . ASP A 1 261 ? -18.049 25.405  -17.253 1.00 21.28  ? 261  ASP A OD2 1 
ATOM   2029 N N   . PHE A 1 262 ? -21.984 27.048  -14.368 1.00 16.66  ? 262  PHE A N   1 
ATOM   2030 C CA  . PHE A 1 262 ? -23.434 26.767  -14.281 1.00 16.37  ? 262  PHE A CA  1 
ATOM   2031 C C   . PHE A 1 262 ? -24.134 27.039  -15.593 1.00 15.23  ? 262  PHE A C   1 
ATOM   2032 O O   . PHE A 1 262 ? -23.827 28.044  -16.273 1.00 15.46  ? 262  PHE A O   1 
ATOM   2033 C CB  . PHE A 1 262 ? -24.098 27.644  -13.206 1.00 16.37  ? 262  PHE A CB  1 
ATOM   2034 C CG  . PHE A 1 262 ? -23.973 27.104  -11.785 1.00 17.81  ? 262  PHE A CG  1 
ATOM   2035 C CD1 . PHE A 1 262 ? -24.745 26.012  -11.356 1.00 16.67  ? 262  PHE A CD1 1 
ATOM   2036 C CD2 . PHE A 1 262 ? -23.067 27.686  -10.871 1.00 16.16  ? 262  PHE A CD2 1 
ATOM   2037 C CE1 . PHE A 1 262 ? -24.640 25.499  -10.039 1.00 18.54  ? 262  PHE A CE1 1 
ATOM   2038 C CE2 . PHE A 1 262 ? -22.974 27.175  -9.537  1.00 15.52  ? 262  PHE A CE2 1 
ATOM   2039 C CZ  . PHE A 1 262 ? -23.741 26.079  -9.137  1.00 20.03  ? 262  PHE A CZ  1 
ATOM   2040 N N   . TYR A 1 263 ? -25.115 26.206  -15.911 1.00 14.72  ? 263  TYR A N   1 
ATOM   2041 C CA  . TYR A 1 263 ? -26.023 26.486  -17.046 1.00 13.84  ? 263  TYR A CA  1 
ATOM   2042 C C   . TYR A 1 263 ? -27.426 26.464  -16.490 1.00 14.29  ? 263  TYR A C   1 
ATOM   2043 O O   . TYR A 1 263 ? -27.723 25.679  -15.588 1.00 13.98  ? 263  TYR A O   1 
ATOM   2044 C CB  . TYR A 1 263 ? -25.906 25.391  -18.104 1.00 14.09  ? 263  TYR A CB  1 
ATOM   2045 C CG  . TYR A 1 263 ? -24.543 25.379  -18.808 1.00 15.60  ? 263  TYR A CG  1 
ATOM   2046 C CD1 . TYR A 1 263 ? -24.374 26.005  -20.049 1.00 17.64  ? 263  TYR A CD1 1 
ATOM   2047 C CD2 . TYR A 1 263 ? -23.455 24.747  -18.225 1.00 16.92  ? 263  TYR A CD2 1 
ATOM   2048 C CE1 . TYR A 1 263 ? -23.157 25.968  -20.732 1.00 16.60  ? 263  TYR A CE1 1 
ATOM   2049 C CE2 . TYR A 1 263 ? -22.210 24.729  -18.882 1.00 16.66  ? 263  TYR A CE2 1 
ATOM   2050 C CZ  . TYR A 1 263 ? -22.094 25.336  -20.139 1.00 17.62  ? 263  TYR A CZ  1 
ATOM   2051 O OH  . TYR A 1 263 ? -20.924 25.376  -20.837 1.00 15.36  ? 263  TYR A OH  1 
ATOM   2052 N N   . VAL A 1 264 ? -28.267 27.344  -17.008 1.00 13.18  ? 264  VAL A N   1 
ATOM   2053 C CA  . VAL A 1 264 ? -29.641 27.430  -16.544 1.00 13.49  ? 264  VAL A CA  1 
ATOM   2054 C C   . VAL A 1 264 ? -30.468 27.336  -17.843 1.00 13.86  ? 264  VAL A C   1 
ATOM   2055 O O   . VAL A 1 264 ? -30.139 28.001  -18.840 1.00 14.89  ? 264  VAL A O   1 
ATOM   2056 C CB  . VAL A 1 264 ? -29.957 28.740  -15.752 1.00 12.55  ? 264  VAL A CB  1 
ATOM   2057 C CG1 . VAL A 1 264 ? -31.513 28.842  -15.378 1.00 13.53  ? 264  VAL A CG1 1 
ATOM   2058 C CG2 . VAL A 1 264 ? -29.155 28.877  -14.443 1.00 13.84  ? 264  VAL A CG2 1 
ATOM   2059 N N   . PHE A 1 265 ? -31.523 26.509  -17.832 1.00 13.83  ? 265  PHE A N   1 
ATOM   2060 C CA  . PHE A 1 265 ? -32.258 26.163  -19.060 1.00 13.83  ? 265  PHE A CA  1 
ATOM   2061 C C   . PHE A 1 265 ? -33.709 26.457  -18.786 1.00 13.41  ? 265  PHE A C   1 
ATOM   2062 O O   . PHE A 1 265 ? -34.163 26.068  -17.727 1.00 14.51  ? 265  PHE A O   1 
ATOM   2063 C CB  . PHE A 1 265 ? -32.163 24.636  -19.343 1.00 13.74  ? 265  PHE A CB  1 
ATOM   2064 C CG  . PHE A 1 265 ? -30.739 24.083  -19.401 1.00 15.32  ? 265  PHE A CG  1 
ATOM   2065 C CD1 . PHE A 1 265 ? -29.982 24.222  -20.543 1.00 15.53  ? 265  PHE A CD1 1 
ATOM   2066 C CD2 . PHE A 1 265 ? -30.219 23.373  -18.313 1.00 17.10  ? 265  PHE A CD2 1 
ATOM   2067 C CE1 . PHE A 1 265 ? -28.643 23.725  -20.610 1.00 17.01  ? 265  PHE A CE1 1 
ATOM   2068 C CE2 . PHE A 1 265 ? -28.877 22.868  -18.363 1.00 18.23  ? 265  PHE A CE2 1 
ATOM   2069 C CZ  . PHE A 1 265 ? -28.114 23.042  -19.532 1.00 16.39  ? 265  PHE A CZ  1 
ATOM   2070 N N   . LEU A 1 266 ? -34.445 27.057  -19.736 1.00 13.83  ? 266  LEU A N   1 
ATOM   2071 C CA  . LEU A 1 266 ? -35.880 27.298  -19.488 1.00 14.70  ? 266  LEU A CA  1 
ATOM   2072 C C   . LEU A 1 266 ? -36.648 26.564  -20.550 1.00 15.04  ? 266  LEU A C   1 
ATOM   2073 O O   . LEU A 1 266 ? -36.203 26.488  -21.679 1.00 15.79  ? 266  LEU A O   1 
ATOM   2074 C CB  . LEU A 1 266 ? -36.215 28.801  -19.602 1.00 13.97  ? 266  LEU A CB  1 
ATOM   2075 C CG  . LEU A 1 266 ? -35.904 29.670  -18.378 1.00 13.55  ? 266  LEU A CG  1 
ATOM   2076 C CD1 . LEU A 1 266 ? -34.387 29.989  -18.271 1.00 17.73  ? 266  LEU A CD1 1 
ATOM   2077 C CD2 . LEU A 1 266 ? -36.707 30.971  -18.527 1.00 15.27  ? 266  LEU A CD2 1 
ATOM   2078 N N   . GLY A 1 267 ? -37.823 26.056  -20.217 1.00 15.58  ? 267  GLY A N   1 
ATOM   2079 C CA  . GLY A 1 267 ? -38.672 25.479  -21.251 1.00 15.28  ? 267  GLY A CA  1 
ATOM   2080 C C   . GLY A 1 267 ? -40.113 25.708  -20.899 1.00 15.51  ? 267  GLY A C   1 
ATOM   2081 O O   . GLY A 1 267 ? -40.450 26.092  -19.758 1.00 15.28  ? 267  GLY A O   1 
ATOM   2082 N N   . ASN A 1 268 ? -40.978 25.484  -21.884 1.00 16.06  ? 268  ASN A N   1 
ATOM   2083 C CA  . ASN A 1 268 ? -42.392 25.615  -21.636 1.00 17.12  ? 268  ASN A CA  1 
ATOM   2084 C C   . ASN A 1 268 ? -43.008 24.392  -21.014 1.00 17.64  ? 268  ASN A C   1 
ATOM   2085 O O   . ASN A 1 268 ? -44.155 24.438  -20.557 1.00 16.89  ? 268  ASN A O   1 
ATOM   2086 C CB  . ASN A 1 268 ? -43.112 25.962  -22.938 1.00 17.60  ? 268  ASN A CB  1 
ATOM   2087 C CG  . ASN A 1 268 ? -42.777 27.354  -23.390 1.00 20.94  ? 268  ASN A CG  1 
ATOM   2088 O OD1 . ASN A 1 268 ? -42.435 28.205  -22.570 1.00 24.51  ? 268  ASN A OD1 1 
ATOM   2089 N ND2 . ASN A 1 268 ? -42.863 27.601  -24.691 1.00 22.67  ? 268  ASN A ND2 1 
ATOM   2090 N N   . THR A 1 269 ? -42.254 23.290  -20.999 1.00 17.07  ? 269  THR A N   1 
ATOM   2091 C CA  . THR A 1 269 ? -42.734 22.009  -20.466 1.00 16.62  ? 269  THR A CA  1 
ATOM   2092 C C   . THR A 1 269 ? -41.500 21.304  -19.891 1.00 15.44  ? 269  THR A C   1 
ATOM   2093 O O   . THR A 1 269 ? -40.389 21.651  -20.269 1.00 15.72  ? 269  THR A O   1 
ATOM   2094 C CB  . THR A 1 269 ? -43.283 21.058  -21.589 1.00 15.08  ? 269  THR A CB  1 
ATOM   2095 O OG1 . THR A 1 269 ? -42.237 20.783  -22.542 1.00 17.19  ? 269  THR A OG1 1 
ATOM   2096 C CG2 . THR A 1 269 ? -44.490 21.640  -22.322 1.00 17.43  ? 269  THR A CG2 1 
ATOM   2097 N N   . PRO A 1 270 ? -41.695 20.284  -19.029 1.00 15.41  ? 270  PRO A N   1 
ATOM   2098 C CA  . PRO A 1 270 ? -40.533 19.501  -18.578 1.00 14.46  ? 270  PRO A CA  1 
ATOM   2099 C C   . PRO A 1 270 ? -39.722 18.881  -19.718 1.00 15.34  ? 270  PRO A C   1 
ATOM   2100 O O   . PRO A 1 270 ? -38.464 18.932  -19.683 1.00 14.55  ? 270  PRO A O   1 
ATOM   2101 C CB  . PRO A 1 270 ? -41.165 18.415  -17.712 1.00 14.35  ? 270  PRO A CB  1 
ATOM   2102 C CG  . PRO A 1 270 ? -42.416 19.142  -17.112 1.00 14.36  ? 270  PRO A CG  1 
ATOM   2103 C CD  . PRO A 1 270 ? -42.936 19.855  -18.349 1.00 14.23  ? 270  PRO A CD  1 
ATOM   2104 N N   . GLU A 1 271 ? -40.398 18.355  -20.743 1.00 15.02  ? 271  GLU A N   1 
ATOM   2105 C CA  . GLU A 1 271 ? -39.652 17.788  -21.867 1.00 15.80  ? 271  GLU A CA  1 
ATOM   2106 C C   . GLU A 1 271 ? -38.744 18.805  -22.568 1.00 15.86  ? 271  GLU A C   1 
ATOM   2107 O O   . GLU A 1 271 ? -37.636 18.450  -23.006 1.00 14.96  ? 271  GLU A O   1 
ATOM   2108 C CB  . GLU A 1 271 ? -40.586 17.132  -22.900 1.00 16.12  ? 271  GLU A CB  1 
ATOM   2109 C CG  . GLU A 1 271 ? -41.181 15.825  -22.454 1.00 19.93  ? 271  GLU A CG  1 
ATOM   2110 C CD  . GLU A 1 271 ? -40.143 14.709  -22.437 1.00 22.65  ? 271  GLU A CD  1 
ATOM   2111 O OE1 . GLU A 1 271 ? -39.597 14.339  -23.535 1.00 22.09  ? 271  GLU A OE1 1 
ATOM   2112 O OE2 . GLU A 1 271 ? -39.865 14.219  -21.317 1.00 22.87  ? 271  GLU A OE2 1 
ATOM   2113 N N   . GLN A 1 272 ? -39.219 20.050  -22.713 1.00 15.20  ? 272  GLN A N   1 
ATOM   2114 C CA  . GLN A 1 272 ? -38.386 21.083  -23.352 1.00 16.34  ? 272  GLN A CA  1 
ATOM   2115 C C   . GLN A 1 272 ? -37.104 21.397  -22.551 1.00 15.36  ? 272  GLN A C   1 
ATOM   2116 O O   . GLN A 1 272 ? -36.059 21.642  -23.145 1.00 16.14  ? 272  GLN A O   1 
ATOM   2117 C CB  . GLN A 1 272 ? -39.175 22.340  -23.589 1.00 15.00  ? 272  GLN A CB  1 
ATOM   2118 C CG  . GLN A 1 272 ? -40.115 22.158  -24.782 1.00 19.13  ? 272  GLN A CG  1 
ATOM   2119 C CD  . GLN A 1 272 ? -40.969 23.369  -25.020 1.00 25.62  ? 272  GLN A CD  1 
ATOM   2120 O OE1 . GLN A 1 272 ? -40.687 24.480  -24.508 1.00 27.71  ? 272  GLN A OE1 1 
ATOM   2121 N NE2 . GLN A 1 272 ? -42.053 23.169  -25.769 1.00 29.13  ? 272  GLN A NE2 1 
ATOM   2122 N N   . VAL A 1 273 ? -37.208 21.378  -21.229 1.00 15.50  ? 273  VAL A N   1 
ATOM   2123 C CA  . VAL A 1 273 ? -35.997 21.489  -20.340 1.00 14.75  ? 273  VAL A CA  1 
ATOM   2124 C C   . VAL A 1 273 ? -34.988 20.375  -20.610 1.00 15.75  ? 273  VAL A C   1 
ATOM   2125 O O   . VAL A 1 273 ? -33.774 20.632  -20.761 1.00 16.84  ? 273  VAL A O   1 
ATOM   2126 C CB  . VAL A 1 273 ? -36.380 21.498  -18.855 1.00 15.08  ? 273  VAL A CB  1 
ATOM   2127 C CG1 . VAL A 1 273 ? -35.117 21.569  -17.945 1.00 11.77  ? 273  VAL A CG1 1 
ATOM   2128 C CG2 . VAL A 1 273 ? -37.238 22.683  -18.570 1.00 16.20  ? 273  VAL A CG2 1 
ATOM   2129 N N   . VAL A 1 274 ? -35.462 19.130  -20.637 1.00 14.86  ? 274  VAL A N   1 
ATOM   2130 C CA  . VAL A 1 274 ? -34.590 17.993  -20.980 1.00 15.11  ? 274  VAL A CA  1 
ATOM   2131 C C   . VAL A 1 274 ? -33.966 18.199  -22.353 1.00 15.14  ? 274  VAL A C   1 
ATOM   2132 O O   . VAL A 1 274 ? -32.733 18.046  -22.513 1.00 11.64  ? 274  VAL A O   1 
ATOM   2133 C CB  . VAL A 1 274 ? -35.305 16.628  -20.911 1.00 16.07  ? 274  VAL A CB  1 
ATOM   2134 C CG1 . VAL A 1 274 ? -34.307 15.504  -21.228 1.00 14.43  ? 274  VAL A CG1 1 
ATOM   2135 C CG2 . VAL A 1 274 ? -35.961 16.419  -19.508 1.00 13.79  ? 274  VAL A CG2 1 
ATOM   2136 N N   . GLN A 1 275 ? -34.784 18.589  -23.349 1.00 13.30  ? 275  GLN A N   1 
ATOM   2137 C CA  . GLN A 1 275 ? -34.242 18.901  -24.696 1.00 13.88  ? 275  GLN A CA  1 
ATOM   2138 C C   . GLN A 1 275 ? -33.151 19.984  -24.675 1.00 14.48  ? 275  GLN A C   1 
ATOM   2139 O O   . GLN A 1 275 ? -32.142 19.853  -25.369 1.00 13.63  ? 275  GLN A O   1 
ATOM   2140 C CB  . GLN A 1 275 ? -35.358 19.319  -25.675 1.00 14.55  ? 275  GLN A CB  1 
ATOM   2141 C CG  . GLN A 1 275 ? -36.337 18.167  -25.943 1.00 13.45  ? 275  GLN A CG  1 
ATOM   2142 C CD  . GLN A 1 275 ? -37.609 18.665  -26.584 1.00 19.84  ? 275  GLN A CD  1 
ATOM   2143 O OE1 . GLN A 1 275 ? -37.843 19.865  -26.623 1.00 19.21  ? 275  GLN A OE1 1 
ATOM   2144 N NE2 . GLN A 1 275 ? -38.441 17.740  -27.090 1.00 19.29  ? 275  GLN A NE2 1 
ATOM   2145 N N   . GLU A 1 276 ? -33.351 21.022  -23.854 1.00 13.56  ? 276  GLU A N   1 
ATOM   2146 C CA  . GLU A 1 276 ? -32.364 22.078  -23.720 1.00 14.02  ? 276  GLU A CA  1 
ATOM   2147 C C   . GLU A 1 276 ? -31.078 21.580  -23.065 1.00 13.61  ? 276  GLU A C   1 
ATOM   2148 O O   . GLU A 1 276 ? -29.995 21.932  -23.540 1.00 14.07  ? 276  GLU A O   1 
ATOM   2149 C CB  . GLU A 1 276 ? -32.904 23.255  -22.894 1.00 14.92  ? 276  GLU A CB  1 
ATOM   2150 C CG  . GLU A 1 276 ? -34.029 24.007  -23.623 1.00 16.39  ? 276  GLU A CG  1 
ATOM   2151 C CD  . GLU A 1 276 ? -33.518 24.738  -24.864 1.00 24.09  ? 276  GLU A CD  1 
ATOM   2152 O OE1 . GLU A 1 276 ? -32.268 24.891  -25.049 1.00 25.52  ? 276  GLU A OE1 1 
ATOM   2153 O OE2 . GLU A 1 276 ? -34.375 25.197  -25.637 1.00 24.92  ? 276  GLU A OE2 1 
ATOM   2154 N N   . TYR A 1 277 ? -31.226 20.787  -21.996 1.00 12.30  ? 277  TYR A N   1 
ATOM   2155 C CA  . TYR A 1 277 ? -30.080 20.190  -21.309 1.00 15.03  ? 277  TYR A CA  1 
ATOM   2156 C C   . TYR A 1 277 ? -29.299 19.317  -22.281 1.00 14.07  ? 277  TYR A C   1 
ATOM   2157 O O   . TYR A 1 277 ? -28.075 19.406  -22.382 1.00 14.09  ? 277  TYR A O   1 
ATOM   2158 C CB  . TYR A 1 277 ? -30.555 19.359  -20.097 1.00 15.08  ? 277  TYR A CB  1 
ATOM   2159 C CG  . TYR A 1 277 ? -29.431 18.575  -19.432 1.00 14.54  ? 277  TYR A CG  1 
ATOM   2160 C CD1 . TYR A 1 277 ? -28.230 19.197  -19.076 1.00 15.42  ? 277  TYR A CD1 1 
ATOM   2161 C CD2 . TYR A 1 277 ? -29.576 17.225  -19.167 1.00 13.87  ? 277  TYR A CD2 1 
ATOM   2162 C CE1 . TYR A 1 277 ? -27.195 18.467  -18.454 1.00 16.05  ? 277  TYR A CE1 1 
ATOM   2163 C CE2 . TYR A 1 277 ? -28.540 16.469  -18.578 1.00 17.18  ? 277  TYR A CE2 1 
ATOM   2164 C CZ  . TYR A 1 277 ? -27.365 17.104  -18.231 1.00 14.91  ? 277  TYR A CZ  1 
ATOM   2165 O OH  . TYR A 1 277 ? -26.351 16.364  -17.655 1.00 17.99  ? 277  TYR A OH  1 
ATOM   2166 N N   . LEU A 1 278 ? -30.001 18.468  -23.029 1.00 13.63  ? 278  LEU A N   1 
ATOM   2167 C CA  . LEU A 1 278 ? -29.278 17.546  -23.914 1.00 14.87  ? 278  LEU A CA  1 
ATOM   2168 C C   . LEU A 1 278 ? -28.680 18.220  -25.146 1.00 15.11  ? 278  LEU A C   1 
ATOM   2169 O O   . LEU A 1 278 ? -27.672 17.737  -25.726 1.00 16.12  ? 278  LEU A O   1 
ATOM   2170 C CB  . LEU A 1 278 ? -30.128 16.314  -24.305 1.00 15.44  ? 278  LEU A CB  1 
ATOM   2171 C CG  . LEU A 1 278 ? -30.704 15.561  -23.065 1.00 16.08  ? 278  LEU A CG  1 
ATOM   2172 C CD1 . LEU A 1 278 ? -31.622 14.411  -23.495 1.00 13.57  ? 278  LEU A CD1 1 
ATOM   2173 C CD2 . LEU A 1 278 ? -29.585 15.054  -22.114 1.00 16.71  ? 278  LEU A CD2 1 
ATOM   2174 N N   . GLU A 1 279 ? -29.281 19.320  -25.566 1.00 15.60  ? 279  GLU A N   1 
ATOM   2175 C CA  . GLU A 1 279 ? -28.698 20.115  -26.653 1.00 16.14  ? 279  GLU A CA  1 
ATOM   2176 C C   . GLU A 1 279 ? -27.308 20.622  -26.224 1.00 17.29  ? 279  GLU A C   1 
ATOM   2177 O O   . GLU A 1 279 ? -26.369 20.681  -27.025 1.00 18.39  ? 279  GLU A O   1 
ATOM   2178 C CB  . GLU A 1 279 ? -29.669 21.242  -27.034 1.00 16.50  ? 279  GLU A CB  1 
ATOM   2179 C CG  . GLU A 1 279 ? -29.077 22.396  -27.845 1.00 21.17  ? 279  GLU A CG  1 
ATOM   2180 C CD  . GLU A 1 279 ? -28.502 21.975  -29.193 1.00 28.74  ? 279  GLU A CD  1 
ATOM   2181 O OE1 . GLU A 1 279 ? -28.968 20.973  -29.777 1.00 30.47  ? 279  GLU A OE1 1 
ATOM   2182 O OE2 . GLU A 1 279 ? -27.578 22.660  -29.696 1.00 31.42  ? 279  GLU A OE2 1 
ATOM   2183 N N   . LEU A 1 280 ? -27.191 21.000  -24.960 1.00 17.06  ? 280  LEU A N   1 
ATOM   2184 C CA  . LEU A 1 280 ? -25.891 21.378  -24.397 1.00 16.87  ? 280  LEU A CA  1 
ATOM   2185 C C   . LEU A 1 280 ? -24.948 20.164  -24.255 1.00 16.35  ? 280  LEU A C   1 
ATOM   2186 O O   . LEU A 1 280 ? -23.887 20.122  -24.900 1.00 17.25  ? 280  LEU A O   1 
ATOM   2187 C CB  . LEU A 1 280 ? -26.059 22.126  -23.073 1.00 16.29  ? 280  LEU A CB  1 
ATOM   2188 C CG  . LEU A 1 280 ? -24.644 22.331  -22.484 1.00 18.81  ? 280  LEU A CG  1 
ATOM   2189 C CD1 . LEU A 1 280 ? -23.874 23.362  -23.300 1.00 14.42  ? 280  LEU A CD1 1 
ATOM   2190 C CD2 . LEU A 1 280 ? -24.767 22.691  -21.078 1.00 17.79  ? 280  LEU A CD2 1 
ATOM   2191 N N   . ILE A 1 281 ? -25.312 19.166  -23.453 1.00 16.26  ? 281  ILE A N   1 
ATOM   2192 C CA  . ILE A 1 281 ? -24.322 18.132  -23.055 1.00 17.02  ? 281  ILE A CA  1 
ATOM   2193 C C   . ILE A 1 281 ? -24.140 17.003  -24.035 1.00 16.75  ? 281  ILE A C   1 
ATOM   2194 O O   . ILE A 1 281 ? -23.181 16.241  -23.906 1.00 17.98  ? 281  ILE A O   1 
ATOM   2195 C CB  . ILE A 1 281 ? -24.646 17.387  -21.734 1.00 17.99  ? 281  ILE A CB  1 
ATOM   2196 C CG1 . ILE A 1 281 ? -26.105 16.903  -21.751 1.00 17.17  ? 281  ILE A CG1 1 
ATOM   2197 C CG2 . ILE A 1 281 ? -24.157 18.148  -20.501 1.00 22.67  ? 281  ILE A CG2 1 
ATOM   2198 C CD1 . ILE A 1 281 ? -26.242 15.583  -21.154 1.00 19.98  ? 281  ILE A CD1 1 
ATOM   2199 N N   . GLY A 1 282 ? -25.047 16.865  -25.000 1.00 14.48  ? 282  GLY A N   1 
ATOM   2200 C CA  . GLY A 1 282 ? -24.938 15.774  -25.937 1.00 16.05  ? 282  GLY A CA  1 
ATOM   2201 C C   . GLY A 1 282 ? -26.143 14.854  -25.836 1.00 15.62  ? 282  GLY A C   1 
ATOM   2202 O O   . GLY A 1 282 ? -26.402 14.264  -24.775 1.00 15.62  ? 282  GLY A O   1 
ATOM   2203 N N   . ARG A 1 283 ? -26.877 14.738  -26.944 1.00 15.89  ? 283  ARG A N   1 
ATOM   2204 C CA  . ARG A 1 283 ? -28.032 13.829  -26.993 1.00 16.37  ? 283  ARG A CA  1 
ATOM   2205 C C   . ARG A 1 283 ? -27.595 12.362  -27.014 1.00 16.25  ? 283  ARG A C   1 
ATOM   2206 O O   . ARG A 1 283 ? -26.493 12.051  -27.486 1.00 17.98  ? 283  ARG A O   1 
ATOM   2207 C CB  . ARG A 1 283 ? -28.961 14.160  -28.198 1.00 15.70  ? 283  ARG A CB  1 
ATOM   2208 C CG  . ARG A 1 283 ? -29.856 15.359  -27.942 1.00 15.16  ? 283  ARG A CG  1 
ATOM   2209 C CD  . ARG A 1 283 ? -30.782 15.670  -29.172 1.00 18.10  ? 283  ARG A CD  1 
ATOM   2210 N NE  . ARG A 1 283 ? -30.003 16.123  -30.320 1.00 17.83  ? 283  ARG A NE  1 
ATOM   2211 C CZ  . ARG A 1 283 ? -29.574 17.363  -30.516 1.00 21.33  ? 283  ARG A CZ  1 
ATOM   2212 N NH1 . ARG A 1 283 ? -29.851 18.339  -29.658 1.00 20.98  ? 283  ARG A NH1 1 
ATOM   2213 N NH2 . ARG A 1 283 ? -28.847 17.628  -31.589 1.00 22.98  ? 283  ARG A NH2 1 
ATOM   2214 N N   . PRO A 1 284 ? -28.450 11.447  -26.508 1.00 16.30  ? 284  PRO A N   1 
ATOM   2215 C CA  . PRO A 1 284 ? -28.087 10.023  -26.446 1.00 16.23  ? 284  PRO A CA  1 
ATOM   2216 C C   . PRO A 1 284 ? -27.894 9.402   -27.820 1.00 15.68  ? 284  PRO A C   1 
ATOM   2217 O O   . PRO A 1 284 ? -28.522 9.830   -28.790 1.00 16.57  ? 284  PRO A O   1 
ATOM   2218 C CB  . PRO A 1 284 ? -29.307 9.369   -25.782 1.00 18.05  ? 284  PRO A CB  1 
ATOM   2219 C CG  . PRO A 1 284 ? -30.398 10.273  -26.021 1.00 16.95  ? 284  PRO A CG  1 
ATOM   2220 C CD  . PRO A 1 284 ? -29.815 11.675  -25.981 1.00 15.37  ? 284  PRO A CD  1 
ATOM   2221 N N   . ALA A 1 285 ? -26.964 8.456   -27.911 1.00 17.04  ? 285  ALA A N   1 
ATOM   2222 C CA  . ALA A 1 285 ? -26.802 7.609   -29.091 1.00 16.98  ? 285  ALA A CA  1 
ATOM   2223 C C   . ALA A 1 285 ? -28.129 6.933   -29.452 1.00 17.24  ? 285  ALA A C   1 
ATOM   2224 O O   . ALA A 1 285 ? -28.894 6.550   -28.564 1.00 16.39  ? 285  ALA A O   1 
ATOM   2225 C CB  . ALA A 1 285 ? -25.706 6.538   -28.837 1.00 17.04  ? 285  ALA A CB  1 
ATOM   2226 N N   . LEU A 1 286 ? -28.389 6.795   -30.749 1.00 17.71  ? 286  LEU A N   1 
ATOM   2227 C CA  . LEU A 1 286 ? -29.482 5.933   -31.209 1.00 18.44  ? 286  LEU A CA  1 
ATOM   2228 C C   . LEU A 1 286 ? -28.953 4.515   -31.046 1.00 17.13  ? 286  LEU A C   1 
ATOM   2229 O O   . LEU A 1 286 ? -27.852 4.187   -31.561 1.00 18.10  ? 286  LEU A O   1 
ATOM   2230 C CB  . LEU A 1 286 ? -29.820 6.245   -32.675 1.00 18.50  ? 286  LEU A CB  1 
ATOM   2231 C CG  . LEU A 1 286 ? -30.933 5.437   -33.317 1.00 18.64  ? 286  LEU A CG  1 
ATOM   2232 C CD1 . LEU A 1 286 ? -32.303 5.841   -32.681 1.00 17.56  ? 286  LEU A CD1 1 
ATOM   2233 C CD2 . LEU A 1 286 ? -30.964 5.719   -34.811 1.00 19.42  ? 286  LEU A CD2 1 
ATOM   2234 N N   . PRO A 1 287 ? -29.679 3.663   -30.312 1.00 17.14  ? 287  PRO A N   1 
ATOM   2235 C CA  . PRO A 1 287 ? -29.142 2.305   -30.099 1.00 16.44  ? 287  PRO A CA  1 
ATOM   2236 C C   . PRO A 1 287 ? -29.274 1.442   -31.363 1.00 15.42  ? 287  PRO A C   1 
ATOM   2237 O O   . PRO A 1 287 ? -30.028 1.791   -32.312 1.00 15.41  ? 287  PRO A O   1 
ATOM   2238 C CB  . PRO A 1 287 ? -30.056 1.726   -29.015 1.00 17.26  ? 287  PRO A CB  1 
ATOM   2239 C CG  . PRO A 1 287 ? -31.324 2.405   -29.244 1.00 18.39  ? 287  PRO A CG  1 
ATOM   2240 C CD  . PRO A 1 287 ? -31.012 3.819   -29.690 1.00 15.97  ? 287  PRO A CD  1 
ATOM   2241 N N   . SER A 1 288 ? -28.535 0.346   -31.390 1.00 14.92  ? 288  SER A N   1 
ATOM   2242 C CA  . SER A 1 288 ? -28.755 -0.699  -32.395 1.00 13.79  ? 288  SER A CA  1 
ATOM   2243 C C   . SER A 1 288 ? -30.124 -1.198  -32.058 1.00 14.98  ? 288  SER A C   1 
ATOM   2244 O O   . SER A 1 288 ? -30.481 -1.303  -30.867 1.00 13.50  ? 288  SER A O   1 
ATOM   2245 C CB  . SER A 1 288 ? -27.766 -1.838  -32.250 1.00 15.27  ? 288  SER A CB  1 
ATOM   2246 O OG  . SER A 1 288 ? -26.447 -1.398  -32.580 1.00 14.45  ? 288  SER A OG  1 
ATOM   2247 N N   . TYR A 1 289 ? -30.892 -1.526  -33.076 1.00 13.83  ? 289  TYR A N   1 
ATOM   2248 C CA  . TYR A 1 289 ? -32.271 -1.968  -32.770 1.00 14.41  ? 289  TYR A CA  1 
ATOM   2249 C C   . TYR A 1 289 ? -32.192 -3.267  -31.937 1.00 14.82  ? 289  TYR A C   1 
ATOM   2250 O O   . TYR A 1 289 ? -33.029 -3.515  -31.057 1.00 15.33  ? 289  TYR A O   1 
ATOM   2251 C CB  . TYR A 1 289 ? -32.956 -2.168  -34.106 1.00 14.89  ? 289  TYR A CB  1 
ATOM   2252 C CG  . TYR A 1 289 ? -34.436 -2.350  -34.078 1.00 15.62  ? 289  TYR A CG  1 
ATOM   2253 C CD1 . TYR A 1 289 ? -35.262 -1.309  -34.417 1.00 17.60  ? 289  TYR A CD1 1 
ATOM   2254 C CD2 . TYR A 1 289 ? -34.991 -3.592  -33.839 1.00 15.34  ? 289  TYR A CD2 1 
ATOM   2255 C CE1 . TYR A 1 289 ? -36.673 -1.487  -34.480 1.00 17.83  ? 289  TYR A CE1 1 
ATOM   2256 C CE2 . TYR A 1 289 ? -36.392 -3.781  -33.889 1.00 18.06  ? 289  TYR A CE2 1 
ATOM   2257 C CZ  . TYR A 1 289 ? -37.192 -2.712  -34.211 1.00 16.99  ? 289  TYR A CZ  1 
ATOM   2258 O OH  . TYR A 1 289 ? -38.547 -2.861  -34.294 1.00 17.46  ? 289  TYR A OH  1 
ATOM   2259 N N   . TRP A 1 290 ? -31.146 -4.079  -32.150 1.00 15.50  ? 290  TRP A N   1 
ATOM   2260 C CA  . TRP A 1 290 ? -31.040 -5.309  -31.360 1.00 16.36  ? 290  TRP A CA  1 
ATOM   2261 C C   . TRP A 1 290 ? -30.855 -5.124  -29.853 1.00 16.30  ? 290  TRP A C   1 
ATOM   2262 O O   . TRP A 1 290 ? -31.273 -5.997  -29.051 1.00 16.57  ? 290  TRP A O   1 
ATOM   2263 C CB  . TRP A 1 290 ? -30.023 -6.279  -31.934 1.00 17.39  ? 290  TRP A CB  1 
ATOM   2264 C CG  . TRP A 1 290 ? -28.623 -5.789  -31.987 1.00 16.02  ? 290  TRP A CG  1 
ATOM   2265 C CD1 . TRP A 1 290 ? -27.961 -5.324  -33.064 1.00 17.12  ? 290  TRP A CD1 1 
ATOM   2266 C CD2 . TRP A 1 290 ? -27.696 -5.797  -30.896 1.00 17.36  ? 290  TRP A CD2 1 
ATOM   2267 N NE1 . TRP A 1 290 ? -26.634 -5.038  -32.715 1.00 15.79  ? 290  TRP A NE1 1 
ATOM   2268 C CE2 . TRP A 1 290 ? -26.465 -5.314  -31.386 1.00 17.08  ? 290  TRP A CE2 1 
ATOM   2269 C CE3 . TRP A 1 290 ? -27.800 -6.145  -29.539 1.00 16.25  ? 290  TRP A CE3 1 
ATOM   2270 C CZ2 . TRP A 1 290 ? -25.335 -5.205  -30.576 1.00 18.81  ? 290  TRP A CZ2 1 
ATOM   2271 C CZ3 . TRP A 1 290 ? -26.670 -6.040  -28.736 1.00 19.60  ? 290  TRP A CZ3 1 
ATOM   2272 C CH2 . TRP A 1 290 ? -25.467 -5.575  -29.262 1.00 18.59  ? 290  TRP A CH2 1 
ATOM   2273 N N   . ALA A 1 291 ? -30.310 -3.973  -29.475 1.00 15.27  ? 291  ALA A N   1 
ATOM   2274 C CA  . ALA A 1 291 ? -30.080 -3.669  -28.054 1.00 15.56  ? 291  ALA A CA  1 
ATOM   2275 C C   . ALA A 1 291 ? -31.420 -3.417  -27.367 1.00 15.69  ? 291  ALA A C   1 
ATOM   2276 O O   . ALA A 1 291 ? -31.501 -3.444  -26.160 1.00 14.86  ? 291  ALA A O   1 
ATOM   2277 C CB  . ALA A 1 291 ? -29.205 -2.497  -27.930 1.00 15.65  ? 291  ALA A CB  1 
ATOM   2278 N N   . LEU A 1 292 ? -32.474 -3.179  -28.145 1.00 15.43  ? 292  LEU A N   1 
ATOM   2279 C CA  . LEU A 1 292 ? -33.816 -2.974  -27.557 1.00 15.95  ? 292  LEU A CA  1 
ATOM   2280 C C   . LEU A 1 292 ? -34.477 -4.259  -27.111 1.00 16.59  ? 292  LEU A C   1 
ATOM   2281 O O   . LEU A 1 292 ? -35.548 -4.254  -26.433 1.00 17.24  ? 292  LEU A O   1 
ATOM   2282 C CB  . LEU A 1 292 ? -34.746 -2.281  -28.571 1.00 16.49  ? 292  LEU A CB  1 
ATOM   2283 C CG  . LEU A 1 292 ? -34.422 -0.914  -29.177 1.00 18.86  ? 292  LEU A CG  1 
ATOM   2284 C CD1 . LEU A 1 292 ? -35.495 -0.559  -30.219 1.00 26.03  ? 292  LEU A CD1 1 
ATOM   2285 C CD2 . LEU A 1 292 ? -34.396 0.090   -28.128 1.00 23.52  ? 292  LEU A CD2 1 
ATOM   2286 N N   . GLY A 1 293 ? -33.923 -5.377  -27.531 1.00 16.48  ? 293  GLY A N   1 
ATOM   2287 C CA  . GLY A 1 293 ? -34.503 -6.643  -27.133 1.00 16.32  ? 293  GLY A CA  1 
ATOM   2288 C C   . GLY A 1 293 ? -34.107 -7.026  -25.726 1.00 16.32  ? 293  GLY A C   1 
ATOM   2289 O O   . GLY A 1 293 ? -33.463 -6.240  -24.971 1.00 17.16  ? 293  GLY A O   1 
ATOM   2290 N N   . PHE A 1 294 ? -34.454 -8.247  -25.360 1.00 15.34  ? 294  PHE A N   1 
ATOM   2291 C CA  . PHE A 1 294 ? -34.198 -8.742  -24.016 1.00 14.93  ? 294  PHE A CA  1 
ATOM   2292 C C   . PHE A 1 294 ? -32.780 -9.284  -23.938 1.00 14.82  ? 294  PHE A C   1 
ATOM   2293 O O   . PHE A 1 294 ? -32.351 -10.002 -24.843 1.00 16.31  ? 294  PHE A O   1 
ATOM   2294 C CB  . PHE A 1 294 ? -35.178 -9.849  -23.703 1.00 13.63  ? 294  PHE A CB  1 
ATOM   2295 C CG  . PHE A 1 294 ? -35.012 -10.449 -22.332 1.00 14.82  ? 294  PHE A CG  1 
ATOM   2296 C CD1 . PHE A 1 294 ? -35.210 -9.664  -21.182 1.00 11.62  ? 294  PHE A CD1 1 
ATOM   2297 C CD2 . PHE A 1 294 ? -34.625 -11.782 -22.195 1.00 15.12  ? 294  PHE A CD2 1 
ATOM   2298 C CE1 . PHE A 1 294 ? -35.058 -10.209 -19.898 1.00 15.21  ? 294  PHE A CE1 1 
ATOM   2299 C CE2 . PHE A 1 294 ? -34.471 -12.360 -20.908 1.00 14.99  ? 294  PHE A CE2 1 
ATOM   2300 C CZ  . PHE A 1 294 ? -34.685 -11.555 -19.757 1.00 16.58  ? 294  PHE A CZ  1 
ATOM   2301 N N   . HIS A 1 295 ? -32.060 -8.914  -22.882 1.00 14.97  ? 295  HIS A N   1 
ATOM   2302 C CA  . HIS A 1 295 ? -30.684 -9.369  -22.642 1.00 14.92  ? 295  HIS A CA  1 
ATOM   2303 C C   . HIS A 1 295 ? -30.675 -10.356 -21.458 1.00 14.57  ? 295  HIS A C   1 
ATOM   2304 O O   . HIS A 1 295 ? -31.338 -10.137 -20.432 1.00 14.51  ? 295  HIS A O   1 
ATOM   2305 C CB  . HIS A 1 295 ? -29.745 -8.201  -22.247 1.00 14.24  ? 295  HIS A CB  1 
ATOM   2306 C CG  . HIS A 1 295 ? -29.636 -7.089  -23.254 1.00 14.19  ? 295  HIS A CG  1 
ATOM   2307 N ND1 . HIS A 1 295 ? -30.731 -6.363  -23.717 1.00 18.10  ? 295  HIS A ND1 1 
ATOM   2308 C CD2 . HIS A 1 295 ? -28.551 -6.536  -23.835 1.00 10.52  ? 295  HIS A CD2 1 
ATOM   2309 C CE1 . HIS A 1 295 ? -30.309 -5.429  -24.557 1.00 11.94  ? 295  HIS A CE1 1 
ATOM   2310 N NE2 . HIS A 1 295 ? -28.992 -5.532  -24.658 1.00 17.02  ? 295  HIS A NE2 1 
ATOM   2311 N N   . LEU A 1 296 ? -29.837 -11.391 -21.535 1.00 16.54  ? 296  LEU A N   1 
ATOM   2312 C CA  . LEU A 1 296 ? -29.682 -12.328 -20.408 1.00 16.45  ? 296  LEU A CA  1 
ATOM   2313 C C   . LEU A 1 296 ? -28.213 -12.421 -20.001 1.00 17.40  ? 296  LEU A C   1 
ATOM   2314 O O   . LEU A 1 296 ? -27.299 -12.347 -20.852 1.00 17.03  ? 296  LEU A O   1 
ATOM   2315 C CB  . LEU A 1 296 ? -30.200 -13.706 -20.798 1.00 17.18  ? 296  LEU A CB  1 
ATOM   2316 C CG  . LEU A 1 296 ? -30.439 -14.771 -19.714 1.00 18.51  ? 296  LEU A CG  1 
ATOM   2317 C CD1 . LEU A 1 296 ? -31.449 -14.315 -18.614 1.00 16.76  ? 296  LEU A CD1 1 
ATOM   2318 C CD2 . LEU A 1 296 ? -30.917 -16.058 -20.389 1.00 17.13  ? 296  LEU A CD2 1 
ATOM   2319 N N   . SER A 1 297 ? -28.004 -12.601 -18.710 1.00 18.44  ? 297  SER A N   1 
ATOM   2320 C CA  . SER A 1 297 ? -26.665 -12.535 -18.147 1.00 19.82  ? 297  SER A CA  1 
ATOM   2321 C C   . SER A 1 297 ? -26.616 -13.232 -16.792 1.00 19.91  ? 297  SER A C   1 
ATOM   2322 O O   . SER A 1 297 ? -27.631 -13.389 -16.112 1.00 19.70  ? 297  SER A O   1 
ATOM   2323 C CB  . SER A 1 297 ? -26.293 -11.052 -17.966 1.00 19.75  ? 297  SER A CB  1 
ATOM   2324 O OG  . SER A 1 297 ? -24.927 -10.897 -17.603 1.00 22.07  ? 297  SER A OG  1 
ATOM   2325 N N   . ARG A 1 298 ? -25.424 -13.653 -16.377 1.00 18.41  ? 298  ARG A N   1 
ATOM   2326 C CA  . ARG A 1 298 ? -25.183 -13.840 -14.951 1.00 18.98  ? 298  ARG A CA  1 
ATOM   2327 C C   . ARG A 1 298 ? -23.703 -13.807 -14.735 1.00 19.08  ? 298  ARG A C   1 
ATOM   2328 O O   . ARG A 1 298 ? -22.930 -14.040 -15.663 1.00 17.51  ? 298  ARG A O   1 
ATOM   2329 C CB  . ARG A 1 298 ? -25.786 -15.123 -14.336 1.00 18.84  ? 298  ARG A CB  1 
ATOM   2330 C CG  . ARG A 1 298 ? -24.978 -16.407 -14.538 1.00 22.67  ? 298  ARG A CG  1 
ATOM   2331 C CD  . ARG A 1 298 ? -25.447 -17.556 -13.624 1.00 22.48  ? 298  ARG A CD  1 
ATOM   2332 N NE  . ARG A 1 298 ? -25.229 -17.294 -12.190 1.00 25.87  ? 298  ARG A NE  1 
ATOM   2333 C CZ  . ARG A 1 298 ? -25.966 -17.832 -11.215 1.00 23.33  ? 298  ARG A CZ  1 
ATOM   2334 N NH1 . ARG A 1 298 ? -26.955 -18.659 -11.505 1.00 23.43  ? 298  ARG A NH1 1 
ATOM   2335 N NH2 . ARG A 1 298 ? -25.726 -17.538 -9.944  1.00 22.31  ? 298  ARG A NH2 1 
ATOM   2336 N N   . TYR A 1 299 ? -23.341 -13.499 -13.500 1.00 19.30  ? 299  TYR A N   1 
ATOM   2337 C CA  . TYR A 1 299 ? -21.985 -13.611 -13.016 1.00 20.02  ? 299  TYR A CA  1 
ATOM   2338 C C   . TYR A 1 299 ? -21.803 -15.094 -12.659 1.00 20.98  ? 299  TYR A C   1 
ATOM   2339 O O   . TYR A 1 299 ? -22.584 -15.678 -11.889 1.00 20.56  ? 299  TYR A O   1 
ATOM   2340 C CB  . TYR A 1 299 ? -21.835 -12.714 -11.793 1.00 20.20  ? 299  TYR A CB  1 
ATOM   2341 C CG  . TYR A 1 299 ? -20.451 -12.682 -11.150 1.00 20.25  ? 299  TYR A CG  1 
ATOM   2342 C CD1 . TYR A 1 299 ? -20.301 -12.259 -9.827  1.00 22.78  ? 299  TYR A CD1 1 
ATOM   2343 C CD2 . TYR A 1 299 ? -19.333 -13.056 -11.844 1.00 18.88  ? 299  TYR A CD2 1 
ATOM   2344 C CE1 . TYR A 1 299 ? -19.046 -12.206 -9.214  1.00 23.17  ? 299  TYR A CE1 1 
ATOM   2345 C CE2 . TYR A 1 299 ? -18.053 -13.010 -11.234 1.00 22.79  ? 299  TYR A CE2 1 
ATOM   2346 C CZ  . TYR A 1 299 ? -17.935 -12.582 -9.918  1.00 22.13  ? 299  TYR A CZ  1 
ATOM   2347 O OH  . TYR A 1 299 ? -16.695 -12.538 -9.300  1.00 23.58  ? 299  TYR A OH  1 
ATOM   2348 N N   . GLU A 1 300 ? -20.805 -15.713 -13.285 1.00 21.99  ? 300  GLU A N   1 
ATOM   2349 C CA  . GLU A 1 300 ? -20.433 -17.097 -13.005 1.00 23.56  ? 300  GLU A CA  1 
ATOM   2350 C C   . GLU A 1 300 ? -21.470 -18.120 -13.444 1.00 23.64  ? 300  GLU A C   1 
ATOM   2351 O O   . GLU A 1 300 ? -22.073 -18.813 -12.619 1.00 24.69  ? 300  GLU A O   1 
ATOM   2352 C CB  . GLU A 1 300 ? -20.028 -17.307 -11.531 1.00 24.26  ? 300  GLU A CB  1 
ATOM   2353 C CG  . GLU A 1 300 ? -18.665 -16.687 -11.151 1.00 27.52  ? 300  GLU A CG  1 
ATOM   2354 C CD  . GLU A 1 300 ? -17.440 -17.413 -11.703 1.00 33.25  ? 300  GLU A CD  1 
ATOM   2355 O OE1 . GLU A 1 300 ? -17.540 -18.601 -12.112 1.00 34.94  ? 300  GLU A OE1 1 
ATOM   2356 O OE2 . GLU A 1 300 ? -16.356 -16.779 -11.704 1.00 36.49  ? 300  GLU A OE2 1 
ATOM   2357 N N   . TYR A 1 301 ? -21.677 -18.208 -14.751 1.00 22.73  ? 301  TYR A N   1 
ATOM   2358 C CA  . TYR A 1 301 ? -22.081 -19.491 -15.332 1.00 22.01  ? 301  TYR A CA  1 
ATOM   2359 C C   . TYR A 1 301 ? -21.037 -20.555 -14.973 1.00 22.54  ? 301  TYR A C   1 
ATOM   2360 O O   . TYR A 1 301 ? -21.383 -21.692 -14.694 1.00 22.02  ? 301  TYR A O   1 
ATOM   2361 C CB  . TYR A 1 301 ? -22.220 -19.400 -16.839 1.00 21.20  ? 301  TYR A CB  1 
ATOM   2362 C CG  . TYR A 1 301 ? -23.387 -18.540 -17.249 1.00 19.99  ? 301  TYR A CG  1 
ATOM   2363 C CD1 . TYR A 1 301 ? -24.701 -19.001 -17.085 1.00 20.89  ? 301  TYR A CD1 1 
ATOM   2364 C CD2 . TYR A 1 301 ? -23.183 -17.264 -17.789 1.00 20.02  ? 301  TYR A CD2 1 
ATOM   2365 C CE1 . TYR A 1 301 ? -25.793 -18.210 -17.466 1.00 19.25  ? 301  TYR A CE1 1 
ATOM   2366 C CE2 . TYR A 1 301 ? -24.272 -16.453 -18.196 1.00 20.97  ? 301  TYR A CE2 1 
ATOM   2367 C CZ  . TYR A 1 301 ? -25.573 -16.938 -18.021 1.00 20.49  ? 301  TYR A CZ  1 
ATOM   2368 O OH  . TYR A 1 301 ? -26.708 -16.182 -18.376 1.00 20.34  ? 301  TYR A OH  1 
ATOM   2369 N N   . GLY A 1 302 ? -19.766 -20.161 -14.998 1.00 22.50  ? 302  GLY A N   1 
ATOM   2370 C CA  . GLY A 1 302 ? -18.657 -21.028 -14.563 1.00 23.83  ? 302  GLY A CA  1 
ATOM   2371 C C   . GLY A 1 302 ? -17.996 -21.706 -15.749 1.00 23.51  ? 302  GLY A C   1 
ATOM   2372 O O   . GLY A 1 302 ? -16.751 -21.688 -15.894 1.00 24.07  ? 302  GLY A O   1 
ATOM   2373 N N   . THR A 1 303 ? -18.838 -22.287 -16.603 1.00 23.16  ? 303  THR A N   1 
ATOM   2374 C CA  . THR A 1 303 ? -18.409 -22.952 -17.832 1.00 23.62  ? 303  THR A CA  1 
ATOM   2375 C C   . THR A 1 303 ? -19.304 -22.582 -19.017 1.00 23.83  ? 303  THR A C   1 
ATOM   2376 O O   . THR A 1 303 ? -20.490 -22.236 -18.846 1.00 22.60  ? 303  THR A O   1 
ATOM   2377 C CB  . THR A 1 303 ? -18.429 -24.506 -17.727 1.00 23.11  ? 303  THR A CB  1 
ATOM   2378 O OG1 . THR A 1 303 ? -19.785 -24.977 -17.633 1.00 24.72  ? 303  THR A OG1 1 
ATOM   2379 C CG2 . THR A 1 303 ? -17.635 -24.999 -16.509 1.00 24.26  ? 303  THR A CG2 1 
ATOM   2380 N N   . LEU A 1 304 ? -18.730 -22.714 -20.214 1.00 23.76  ? 304  LEU A N   1 
ATOM   2381 C CA  . LEU A 1 304 ? -19.483 -22.511 -21.442 1.00 24.01  ? 304  LEU A CA  1 
ATOM   2382 C C   . LEU A 1 304 ? -20.639 -23.507 -21.524 1.00 24.68  ? 304  LEU A C   1 
ATOM   2383 O O   . LEU A 1 304 ? -21.729 -23.163 -21.996 1.00 24.27  ? 304  LEU A O   1 
ATOM   2384 C CB  . LEU A 1 304 ? -18.569 -22.621 -22.650 1.00 23.51  ? 304  LEU A CB  1 
ATOM   2385 C CG  . LEU A 1 304 ? -19.173 -22.324 -24.029 1.00 24.73  ? 304  LEU A CG  1 
ATOM   2386 C CD1 . LEU A 1 304 ? -19.909 -20.992 -24.036 1.00 22.76  ? 304  LEU A CD1 1 
ATOM   2387 C CD2 . LEU A 1 304 ? -18.074 -22.311 -25.108 1.00 22.30  ? 304  LEU A CD2 1 
ATOM   2388 N N   . ASP A 1 305 ? -20.422 -24.734 -21.042 1.00 24.99  ? 305  ASP A N   1 
ATOM   2389 C CA  . ASP A 1 305 ? -21.503 -25.729 -20.974 1.00 25.84  ? 305  ASP A CA  1 
ATOM   2390 C C   . ASP A 1 305 ? -22.688 -25.229 -20.169 1.00 25.08  ? 305  ASP A C   1 
ATOM   2391 O O   . ASP A 1 305 ? -23.848 -25.426 -20.573 1.00 23.65  ? 305  ASP A O   1 
ATOM   2392 C CB  . ASP A 1 305 ? -21.031 -27.064 -20.370 1.00 27.31  ? 305  ASP A CB  1 
ATOM   2393 C CG  . ASP A 1 305 ? -20.184 -27.907 -21.342 1.00 32.39  ? 305  ASP A CG  1 
ATOM   2394 O OD1 . ASP A 1 305 ? -20.047 -27.547 -22.534 1.00 36.73  ? 305  ASP A OD1 1 
ATOM   2395 O OD2 . ASP A 1 305 ? -19.652 -28.957 -20.891 1.00 38.31  ? 305  ASP A OD2 1 
ATOM   2396 N N   . ASN A 1 306 ? -22.412 -24.609 -19.023 1.00 24.63  ? 306  ASN A N   1 
ATOM   2397 C CA  . ASN A 1 306 ? -23.495 -24.056 -18.168 1.00 25.67  ? 306  ASN A CA  1 
ATOM   2398 C C   . ASN A 1 306 ? -24.196 -22.893 -18.856 1.00 24.46  ? 306  ASN A C   1 
ATOM   2399 O O   . ASN A 1 306 ? -25.425 -22.789 -18.802 1.00 25.98  ? 306  ASN A O   1 
ATOM   2400 C CB  . ASN A 1 306 ? -22.959 -23.612 -16.798 1.00 25.79  ? 306  ASN A CB  1 
ATOM   2401 C CG  . ASN A 1 306 ? -22.567 -24.803 -15.911 1.00 28.49  ? 306  ASN A CG  1 
ATOM   2402 O OD1 . ASN A 1 306 ? -22.972 -25.932 -16.170 1.00 30.50  ? 306  ASN A OD1 1 
ATOM   2403 N ND2 . ASN A 1 306 ? -21.753 -24.552 -14.889 1.00 27.38  ? 306  ASN A ND2 1 
ATOM   2404 N N   . MET A 1 307 ? -23.414 -22.025 -19.484 1.00 23.61  ? 307  MET A N   1 
ATOM   2405 C CA  . MET A 1 307 ? -23.964 -20.881 -20.233 1.00 23.95  ? 307  MET A CA  1 
ATOM   2406 C C   . MET A 1 307 ? -24.810 -21.392 -21.387 1.00 24.12  ? 307  MET A C   1 
ATOM   2407 O O   . MET A 1 307 ? -25.949 -20.968 -21.544 1.00 23.02  ? 307  MET A O   1 
ATOM   2408 C CB  . MET A 1 307 ? -22.873 -19.933 -20.733 1.00 23.21  ? 307  MET A CB  1 
ATOM   2409 C CG  . MET A 1 307 ? -23.405 -18.717 -21.529 1.00 22.65  ? 307  MET A CG  1 
ATOM   2410 S SD  . MET A 1 307 ? -22.052 -17.787 -22.211 1.00 27.50  ? 307  MET A SD  1 
ATOM   2411 C CE  . MET A 1 307 ? -21.397 -16.976 -20.760 1.00 25.04  ? 307  MET A CE  1 
ATOM   2412 N N   . ARG A 1 308 ? -24.274 -22.354 -22.155 1.00 23.83  ? 308  ARG A N   1 
ATOM   2413 C CA  . ARG A 1 308 ? -25.013 -22.922 -23.274 1.00 25.82  ? 308  ARG A CA  1 
ATOM   2414 C C   . ARG A 1 308 ? -26.319 -23.593 -22.832 1.00 24.53  ? 308  ARG A C   1 
ATOM   2415 O O   . ARG A 1 308 ? -27.315 -23.479 -23.531 1.00 24.22  ? 308  ARG A O   1 
ATOM   2416 C CB  . ARG A 1 308 ? -24.096 -23.832 -24.111 1.00 25.68  ? 308  ARG A CB  1 
ATOM   2417 C CG  . ARG A 1 308 ? -24.758 -24.702 -25.171 1.00 31.66  ? 308  ARG A CG  1 
ATOM   2418 C CD  . ARG A 1 308 ? -23.671 -25.597 -25.817 1.00 31.00  ? 308  ARG A CD  1 
ATOM   2419 N NE  . ARG A 1 308 ? -22.828 -24.882 -26.770 1.00 39.46  ? 308  ARG A NE  1 
ATOM   2420 C CZ  . ARG A 1 308 ? -21.501 -24.986 -26.818 1.00 41.96  ? 308  ARG A CZ  1 
ATOM   2421 N NH1 . ARG A 1 308 ? -20.861 -25.742 -25.937 1.00 44.73  ? 308  ARG A NH1 1 
ATOM   2422 N NH2 . ARG A 1 308 ? -20.808 -24.327 -27.734 1.00 43.18  ? 308  ARG A NH2 1 
ATOM   2423 N N   . GLU A 1 309 ? -26.332 -24.262 -21.680 1.00 24.00  ? 309  GLU A N   1 
ATOM   2424 C CA  . GLU A 1 309 ? -27.561 -24.888 -21.160 1.00 26.25  ? 309  GLU A CA  1 
ATOM   2425 C C   . GLU A 1 309 ? -28.659 -23.846 -20.828 1.00 24.14  ? 309  GLU A C   1 
ATOM   2426 O O   . GLU A 1 309 ? -29.865 -24.047 -21.089 1.00 23.72  ? 309  GLU A O   1 
ATOM   2427 C CB  . GLU A 1 309 ? -27.250 -25.752 -19.918 1.00 26.09  ? 309  GLU A CB  1 
ATOM   2428 C CG  . GLU A 1 309 ? -28.512 -26.320 -19.223 1.00 30.81  ? 309  GLU A CG  1 
ATOM   2429 C CD  . GLU A 1 309 ? -28.208 -27.144 -17.953 1.00 32.37  ? 309  GLU A CD  1 
ATOM   2430 O OE1 . GLU A 1 309 ? -27.003 -27.279 -17.582 1.00 36.41  ? 309  GLU A OE1 1 
ATOM   2431 O OE2 . GLU A 1 309 ? -29.199 -27.608 -17.307 1.00 37.72  ? 309  GLU A OE2 1 
ATOM   2432 N N   . VAL A 1 310 ? -28.237 -22.733 -20.240 1.00 22.94  ? 310  VAL A N   1 
ATOM   2433 C CA  . VAL A 1 310 ? -29.137 -21.611 -19.963 1.00 21.58  ? 310  VAL A CA  1 
ATOM   2434 C C   . VAL A 1 310 ? -29.696 -21.011 -21.255 1.00 20.78  ? 310  VAL A C   1 
ATOM   2435 O O   . VAL A 1 310 ? -30.919 -20.809 -21.369 1.00 20.45  ? 310  VAL A O   1 
ATOM   2436 C CB  . VAL A 1 310 ? -28.412 -20.523 -19.083 1.00 21.65  ? 310  VAL A CB  1 
ATOM   2437 C CG1 . VAL A 1 310 ? -29.268 -19.267 -18.933 1.00 20.10  ? 310  VAL A CG1 1 
ATOM   2438 C CG2 . VAL A 1 310 ? -28.107 -21.121 -17.713 1.00 22.57  ? 310  VAL A CG2 1 
ATOM   2439 N N   . VAL A 1 311 ? -28.809 -20.741 -22.216 1.00 20.21  ? 311  VAL A N   1 
ATOM   2440 C CA  . VAL A 1 311 ? -29.186 -20.204 -23.521 1.00 20.68  ? 311  VAL A CA  1 
ATOM   2441 C C   . VAL A 1 311 ? -30.230 -21.139 -24.139 1.00 21.41  ? 311  VAL A C   1 
ATOM   2442 O O   . VAL A 1 311 ? -31.300 -20.698 -24.588 1.00 20.96  ? 311  VAL A O   1 
ATOM   2443 C CB  . VAL A 1 311 ? -27.965 -20.069 -24.488 1.00 20.62  ? 311  VAL A CB  1 
ATOM   2444 C CG1 . VAL A 1 311 ? -28.417 -19.678 -25.896 1.00 21.23  ? 311  VAL A CG1 1 
ATOM   2445 C CG2 . VAL A 1 311 ? -26.962 -19.009 -23.993 1.00 19.95  ? 311  VAL A CG2 1 
ATOM   2446 N N   . GLU A 1 312 ? -29.936 -22.435 -24.115 1.00 21.91  ? 312  GLU A N   1 
ATOM   2447 C CA  . GLU A 1 312 ? -30.752 -23.382 -24.819 1.00 23.31  ? 312  GLU A CA  1 
ATOM   2448 C C   . GLU A 1 312 ? -32.132 -23.581 -24.195 1.00 22.99  ? 312  GLU A C   1 
ATOM   2449 O O   . GLU A 1 312 ? -33.098 -23.685 -24.949 1.00 23.01  ? 312  GLU A O   1 
ATOM   2450 C CB  . GLU A 1 312 ? -29.985 -24.675 -25.113 1.00 25.29  ? 312  GLU A CB  1 
ATOM   2451 C CG  . GLU A 1 312 ? -28.970 -24.454 -26.273 1.00 32.09  ? 312  GLU A CG  1 
ATOM   2452 C CD  . GLU A 1 312 ? -29.608 -23.766 -27.534 1.00 41.59  ? 312  GLU A CD  1 
ATOM   2453 O OE1 . GLU A 1 312 ? -30.652 -24.281 -28.047 1.00 46.85  ? 312  GLU A OE1 1 
ATOM   2454 O OE2 . GLU A 1 312 ? -29.060 -22.725 -28.019 1.00 42.36  ? 312  GLU A OE2 1 
ATOM   2455 N N   . ARG A 1 313 ? -32.256 -23.566 -22.861 1.00 21.51  ? 313  ARG A N   1 
ATOM   2456 C CA  . ARG A 1 313 ? -33.613 -23.706 -22.257 1.00 22.16  ? 313  ARG A CA  1 
ATOM   2457 C C   . ARG A 1 313 ? -34.496 -22.468 -22.468 1.00 21.39  ? 313  ARG A C   1 
ATOM   2458 O O   . ARG A 1 313 ? -35.739 -22.580 -22.598 1.00 21.65  ? 313  ARG A O   1 
ATOM   2459 C CB  . ARG A 1 313 ? -33.590 -24.145 -20.788 1.00 21.93  ? 313  ARG A CB  1 
ATOM   2460 C CG  . ARG A 1 313 ? -32.920 -23.156 -19.837 1.00 22.73  ? 313  ARG A CG  1 
ATOM   2461 C CD  . ARG A 1 313 ? -33.228 -23.545 -18.412 1.00 24.30  ? 313  ARG A CD  1 
ATOM   2462 N NE  . ARG A 1 313 ? -32.540 -22.671 -17.480 1.00 24.10  ? 313  ARG A NE  1 
ATOM   2463 C CZ  . ARG A 1 313 ? -31.619 -23.076 -16.610 1.00 26.96  ? 313  ARG A CZ  1 
ATOM   2464 N NH1 . ARG A 1 313 ? -31.284 -24.365 -16.521 1.00 29.73  ? 313  ARG A NH1 1 
ATOM   2465 N NH2 . ARG A 1 313 ? -31.052 -22.198 -15.795 1.00 25.64  ? 313  ARG A NH2 1 
ATOM   2466 N N   . ASN A 1 314 ? -33.864 -21.298 -22.531 1.00 20.80  ? 314  ASN A N   1 
ATOM   2467 C CA  . ASN A 1 314 ? -34.595 -20.063 -22.859 1.00 21.36  ? 314  ASN A CA  1 
ATOM   2468 C C   . ASN A 1 314 ? -34.996 -19.967 -24.318 1.00 21.90  ? 314  ASN A C   1 
ATOM   2469 O O   . ASN A 1 314 ? -36.116 -19.533 -24.624 1.00 21.58  ? 314  ASN A O   1 
ATOM   2470 C CB  . ASN A 1 314 ? -33.853 -18.826 -22.343 1.00 21.45  ? 314  ASN A CB  1 
ATOM   2471 C CG  . ASN A 1 314 ? -33.917 -18.733 -20.834 1.00 20.95  ? 314  ASN A CG  1 
ATOM   2472 O OD1 . ASN A 1 314 ? -34.912 -18.260 -20.271 1.00 18.82  ? 314  ASN A OD1 1 
ATOM   2473 N ND2 . ASN A 1 314 ? -32.893 -19.242 -20.164 1.00 17.43  ? 314  ASN A ND2 1 
ATOM   2474 N N   . ARG A 1 315 ? -34.115 -20.413 -25.218 1.00 21.32  ? 315  ARG A N   1 
ATOM   2475 C CA  . ARG A 1 315 ? -34.493 -20.577 -26.623 1.00 21.70  ? 315  ARG A CA  1 
ATOM   2476 C C   . ARG A 1 315 ? -35.599 -21.618 -26.848 1.00 22.36  ? 315  ARG A C   1 
ATOM   2477 O O   . ARG A 1 315 ? -36.561 -21.361 -27.596 1.00 22.62  ? 315  ARG A O   1 
ATOM   2478 C CB  . ARG A 1 315 ? -33.267 -20.895 -27.468 1.00 21.40  ? 315  ARG A CB  1 
ATOM   2479 C CG  . ARG A 1 315 ? -32.379 -19.685 -27.650 1.00 21.21  ? 315  ARG A CG  1 
ATOM   2480 C CD  . ARG A 1 315 ? -31.325 -19.924 -28.687 1.00 24.81  ? 315  ARG A CD  1 
ATOM   2481 N NE  . ARG A 1 315 ? -31.911 -19.963 -30.008 1.00 29.44  ? 315  ARG A NE  1 
ATOM   2482 C CZ  . ARG A 1 315 ? -32.098 -21.068 -30.727 1.00 34.48  ? 315  ARG A CZ  1 
ATOM   2483 N NH1 . ARG A 1 315 ? -31.724 -22.264 -30.262 1.00 36.82  ? 315  ARG A NH1 1 
ATOM   2484 N NH2 . ARG A 1 315 ? -32.642 -20.969 -31.933 1.00 35.77  ? 315  ARG A NH2 1 
ATOM   2485 N N   . ALA A 1 316 ? -35.491 -22.768 -26.170 1.00 22.78  ? 316  ALA A N   1 
ATOM   2486 C CA  . ALA A 1 316 ? -36.515 -23.833 -26.253 1.00 23.50  ? 316  ALA A CA  1 
ATOM   2487 C C   . ALA A 1 316 ? -37.897 -23.332 -25.810 1.00 23.82  ? 316  ALA A C   1 
ATOM   2488 O O   . ALA A 1 316 ? -38.945 -23.740 -26.363 1.00 23.65  ? 316  ALA A O   1 
ATOM   2489 C CB  . ALA A 1 316 ? -36.100 -25.040 -25.400 1.00 23.87  ? 316  ALA A CB  1 
ATOM   2490 N N   . ALA A 1 317 ? -37.896 -22.425 -24.837 1.00 23.00  ? 317  ALA A N   1 
ATOM   2491 C CA  . ALA A 1 317 ? -39.126 -21.793 -24.345 1.00 22.78  ? 317  ALA A CA  1 
ATOM   2492 C C   . ALA A 1 317 ? -39.697 -20.696 -25.270 1.00 22.23  ? 317  ALA A C   1 
ATOM   2493 O O   . ALA A 1 317 ? -40.788 -20.175 -24.989 1.00 23.20  ? 317  ALA A O   1 
ATOM   2494 C CB  . ALA A 1 317 ? -38.899 -21.241 -22.943 1.00 22.70  ? 317  ALA A CB  1 
ATOM   2495 N N   . GLN A 1 318 ? -39.002 -20.368 -26.358 1.00 21.00  ? 318  GLN A N   1 
ATOM   2496 C CA  . GLN A 1 318 ? -39.429 -19.320 -27.316 1.00 22.81  ? 318  GLN A CA  1 
ATOM   2497 C C   . GLN A 1 318 ? -39.490 -17.957 -26.621 1.00 22.91  ? 318  GLN A C   1 
ATOM   2498 O O   . GLN A 1 318 ? -40.400 -17.158 -26.867 1.00 23.76  ? 318  GLN A O   1 
ATOM   2499 C CB  . GLN A 1 318 ? -40.805 -19.617 -27.997 1.00 23.54  ? 318  GLN A CB  1 
ATOM   2500 C CG  . GLN A 1 318 ? -40.893 -20.973 -28.757 1.00 25.96  ? 318  GLN A CG  1 
ATOM   2501 C CD  . GLN A 1 318 ? -39.695 -21.191 -29.675 1.00 29.90  ? 318  GLN A CD  1 
ATOM   2502 O OE1 . GLN A 1 318 ? -39.418 -20.389 -30.574 1.00 31.64  ? 318  GLN A OE1 1 
ATOM   2503 N NE2 . GLN A 1 318 ? -38.952 -22.266 -29.427 1.00 33.78  ? 318  GLN A NE2 1 
ATOM   2504 N N   . LEU A 1 319 ? -38.542 -17.717 -25.724 1.00 22.69  ? 319  LEU A N   1 
ATOM   2505 C CA  . LEU A 1 319 ? -38.477 -16.428 -25.028 1.00 22.91  ? 319  LEU A CA  1 
ATOM   2506 C C   . LEU A 1 319 ? -37.954 -15.418 -26.038 1.00 21.79  ? 319  LEU A C   1 
ATOM   2507 O O   . LEU A 1 319 ? -36.957 -15.687 -26.737 1.00 22.33  ? 319  LEU A O   1 
ATOM   2508 C CB  . LEU A 1 319 ? -37.535 -16.517 -23.816 1.00 21.74  ? 319  LEU A CB  1 
ATOM   2509 C CG  . LEU A 1 319 ? -37.626 -15.345 -22.825 1.00 21.84  ? 319  LEU A CG  1 
ATOM   2510 C CD1 . LEU A 1 319 ? -38.915 -15.391 -21.956 1.00 21.06  ? 319  LEU A CD1 1 
ATOM   2511 C CD2 . LEU A 1 319 ? -36.369 -15.296 -21.982 1.00 19.29  ? 319  LEU A CD2 1 
ATOM   2512 N N   . PRO A 1 320 ? -38.594 -14.242 -26.121 1.00 21.13  ? 320  PRO A N   1 
ATOM   2513 C CA  . PRO A 1 320 ? -37.949 -13.206 -26.918 1.00 20.03  ? 320  PRO A CA  1 
ATOM   2514 C C   . PRO A 1 320 ? -36.614 -12.883 -26.211 1.00 19.51  ? 320  PRO A C   1 
ATOM   2515 O O   . PRO A 1 320 ? -36.596 -12.692 -24.986 1.00 19.37  ? 320  PRO A O   1 
ATOM   2516 C CB  . PRO A 1 320 ? -38.948 -12.058 -26.845 1.00 19.75  ? 320  PRO A CB  1 
ATOM   2517 C CG  . PRO A 1 320 ? -40.236 -12.741 -26.490 1.00 20.37  ? 320  PRO A CG  1 
ATOM   2518 C CD  . PRO A 1 320 ? -39.851 -13.763 -25.527 1.00 20.04  ? 320  PRO A CD  1 
ATOM   2519 N N   . TYR A 1 321 ? -35.502 -12.888 -26.954 1.00 19.16  ? 321  TYR A N   1 
ATOM   2520 C CA  . TYR A 1 321 ? -34.189 -13.037 -26.325 1.00 18.61  ? 321  TYR A CA  1 
ATOM   2521 C C   . TYR A 1 321 ? -33.105 -12.744 -27.335 1.00 18.63  ? 321  TYR A C   1 
ATOM   2522 O O   . TYR A 1 321 ? -32.758 -13.603 -28.160 1.00 19.10  ? 321  TYR A O   1 
ATOM   2523 C CB  . TYR A 1 321 ? -34.087 -14.467 -25.721 1.00 18.69  ? 321  TYR A CB  1 
ATOM   2524 C CG  . TYR A 1 321 ? -32.746 -15.026 -25.206 1.00 19.22  ? 321  TYR A CG  1 
ATOM   2525 C CD1 . TYR A 1 321 ? -31.687 -14.213 -24.798 1.00 17.94  ? 321  TYR A CD1 1 
ATOM   2526 C CD2 . TYR A 1 321 ? -32.597 -16.404 -25.062 1.00 19.86  ? 321  TYR A CD2 1 
ATOM   2527 C CE1 . TYR A 1 321 ? -30.469 -14.802 -24.286 1.00 16.69  ? 321  TYR A CE1 1 
ATOM   2528 C CE2 . TYR A 1 321 ? -31.428 -16.977 -24.558 1.00 21.87  ? 321  TYR A CE2 1 
ATOM   2529 C CZ  . TYR A 1 321 ? -30.378 -16.171 -24.181 1.00 19.71  ? 321  TYR A CZ  1 
ATOM   2530 O OH  . TYR A 1 321 ? -29.255 -16.769 -23.704 1.00 23.37  ? 321  TYR A OH  1 
ATOM   2531 N N   . ASP A 1 322 ? -32.599 -11.511 -27.313 1.00 17.18  ? 322  ASP A N   1 
ATOM   2532 C CA  . ASP A 1 322 ? -31.736 -11.068 -28.377 1.00 17.45  ? 322  ASP A CA  1 
ATOM   2533 C C   . ASP A 1 322 ? -30.265 -11.147 -28.013 1.00 17.20  ? 322  ASP A C   1 
ATOM   2534 O O   . ASP A 1 322 ? -29.394 -11.314 -28.910 1.00 17.38  ? 322  ASP A O   1 
ATOM   2535 C CB  . ASP A 1 322 ? -32.053 -9.633  -28.758 1.00 18.16  ? 322  ASP A CB  1 
ATOM   2536 C CG  . ASP A 1 322 ? -32.990 -9.552  -29.923 1.00 20.69  ? 322  ASP A CG  1 
ATOM   2537 O OD1 . ASP A 1 322 ? -32.496 -9.239  -31.033 1.00 21.89  ? 322  ASP A OD1 1 
ATOM   2538 O OD2 . ASP A 1 322 ? -34.203 -9.829  -29.699 1.00 21.17  ? 322  ASP A OD2 1 
ATOM   2539 N N   . VAL A 1 323 ? -29.982 -10.987 -26.721 1.00 16.68  ? 323  VAL A N   1 
ATOM   2540 C CA  . VAL A 1 323 ? -28.605 -10.734 -26.331 1.00 16.07  ? 323  VAL A CA  1 
ATOM   2541 C C   . VAL A 1 323 ? -28.168 -11.623 -25.182 1.00 15.45  ? 323  VAL A C   1 
ATOM   2542 O O   . VAL A 1 323 ? -28.886 -11.797 -24.207 1.00 15.25  ? 323  VAL A O   1 
ATOM   2543 C CB  . VAL A 1 323 ? -28.369 -9.222  -25.963 1.00 15.49  ? 323  VAL A CB  1 
ATOM   2544 C CG1 . VAL A 1 323 ? -26.866 -8.936  -25.892 1.00 15.41  ? 323  VAL A CG1 1 
ATOM   2545 C CG2 . VAL A 1 323 ? -28.960 -8.306  -27.000 1.00 15.20  ? 323  VAL A CG2 1 
ATOM   2546 N N   . GLN A 1 324 ? -26.956 -12.181 -25.273 1.00 16.08  ? 324  GLN A N   1 
ATOM   2547 C CA  . GLN A 1 324 ? -26.444 -12.946 -24.154 1.00 15.49  ? 324  GLN A CA  1 
ATOM   2548 C C   . GLN A 1 324 ? -25.192 -12.197 -23.697 1.00 16.23  ? 324  GLN A C   1 
ATOM   2549 O O   . GLN A 1 324 ? -24.404 -11.823 -24.541 1.00 15.82  ? 324  GLN A O   1 
ATOM   2550 C CB  . GLN A 1 324 ? -26.092 -14.376 -24.622 1.00 17.27  ? 324  GLN A CB  1 
ATOM   2551 C CG  . GLN A 1 324 ? -25.443 -15.287 -23.537 1.00 15.97  ? 324  GLN A CG  1 
ATOM   2552 C CD  . GLN A 1 324 ? -26.305 -15.414 -22.275 1.00 16.99  ? 324  GLN A CD  1 
ATOM   2553 O OE1 . GLN A 1 324 ? -27.520 -15.657 -22.350 1.00 20.01  ? 324  GLN A OE1 1 
ATOM   2554 N NE2 . GLN A 1 324 ? -25.683 -15.269 -21.118 1.00 14.44  ? 324  GLN A NE2 1 
ATOM   2555 N N   . HIS A 1 325 ? -25.028 -11.976 -22.390 1.00 16.86  ? 325  HIS A N   1 
ATOM   2556 C CA  . HIS A 1 325 ? -23.827 -11.290 -21.883 1.00 18.64  ? 325  HIS A CA  1 
ATOM   2557 C C   . HIS A 1 325 ? -22.883 -12.354 -21.309 1.00 17.92  ? 325  HIS A C   1 
ATOM   2558 O O   . HIS A 1 325 ? -23.312 -13.383 -20.811 1.00 19.77  ? 325  HIS A O   1 
ATOM   2559 C CB  . HIS A 1 325 ? -24.168 -10.215 -20.822 1.00 19.15  ? 325  HIS A CB  1 
ATOM   2560 C CG  . HIS A 1 325 ? -24.974 -9.066  -21.348 1.00 19.67  ? 325  HIS A CG  1 
ATOM   2561 N ND1 . HIS A 1 325 ? -24.795 -7.775  -20.916 1.00 21.41  ? 325  HIS A ND1 1 
ATOM   2562 C CD2 . HIS A 1 325 ? -25.975 -9.019  -22.264 1.00 20.47  ? 325  HIS A CD2 1 
ATOM   2563 C CE1 . HIS A 1 325 ? -25.629 -6.977  -21.552 1.00 22.78  ? 325  HIS A CE1 1 
ATOM   2564 N NE2 . HIS A 1 325 ? -26.357 -7.709  -22.378 1.00 21.67  ? 325  HIS A NE2 1 
ATOM   2565 N N   . ALA A 1 326 ? -21.597 -12.127 -21.428 1.00 19.12  ? 326  ALA A N   1 
ATOM   2566 C CA  . ALA A 1 326 ? -20.638 -13.073 -20.907 1.00 18.77  ? 326  ALA A CA  1 
ATOM   2567 C C   . ALA A 1 326 ? -19.872 -12.258 -19.876 1.00 18.86  ? 326  ALA A C   1 
ATOM   2568 O O   . ALA A 1 326 ? -19.178 -11.302 -20.238 1.00 18.63  ? 326  ALA A O   1 
ATOM   2569 C CB  . ALA A 1 326 ? -19.686 -13.550 -22.030 1.00 18.80  ? 326  ALA A CB  1 
ATOM   2570 N N   . ASP A 1 327 ? -19.975 -12.667 -18.624 1.00 18.10  ? 327  ASP A N   1 
ATOM   2571 C CA  . ASP A 1 327 ? -19.338 -11.957 -17.505 1.00 19.38  ? 327  ASP A CA  1 
ATOM   2572 C C   . ASP A 1 327 ? -17.902 -12.513 -17.348 1.00 19.59  ? 327  ASP A C   1 
ATOM   2573 O O   . ASP A 1 327 ? -17.472 -13.310 -18.173 1.00 19.12  ? 327  ASP A O   1 
ATOM   2574 C CB  . ASP A 1 327 ? -20.185 -12.174 -16.253 1.00 20.36  ? 327  ASP A CB  1 
ATOM   2575 C CG  . ASP A 1 327 ? -20.002 -11.097 -15.213 1.00 22.03  ? 327  ASP A CG  1 
ATOM   2576 O OD1 . ASP A 1 327 ? -18.890 -10.532 -15.095 1.00 25.24  ? 327  ASP A OD1 1 
ATOM   2577 O OD2 . ASP A 1 327 ? -20.982 -10.842 -14.482 1.00 21.71  ? 327  ASP A OD2 1 
ATOM   2578 N N   . ILE A 1 328 ? -17.179 -12.129 -16.296 1.00 20.19  ? 328  ILE A N   1 
ATOM   2579 C CA  . ILE A 1 328 ? -15.719 -12.400 -16.237 1.00 21.61  ? 328  ILE A CA  1 
ATOM   2580 C C   . ILE A 1 328 ? -15.337 -13.867 -16.151 1.00 22.31  ? 328  ILE A C   1 
ATOM   2581 O O   . ILE A 1 328 ? -14.147 -14.189 -16.317 1.00 23.92  ? 328  ILE A O   1 
ATOM   2582 C CB  . ILE A 1 328 ? -15.000 -11.631 -15.069 1.00 21.21  ? 328  ILE A CB  1 
ATOM   2583 C CG1 . ILE A 1 328 ? -15.598 -12.025 -13.698 1.00 21.40  ? 328  ILE A CG1 1 
ATOM   2584 C CG2 . ILE A 1 328 ? -15.053 -10.129 -15.327 1.00 21.36  ? 328  ILE A CG2 1 
ATOM   2585 C CD1 . ILE A 1 328 ? -14.936 -11.300 -12.458 1.00 20.46  ? 328  ILE A CD1 1 
ATOM   2586 N N   . ASP A 1 329 ? -16.311 -14.754 -15.902 1.00 22.84  ? 329  ASP A N   1 
ATOM   2587 C CA  . ASP A 1 329 ? -16.022 -16.196 -16.005 1.00 23.67  ? 329  ASP A CA  1 
ATOM   2588 C C   . ASP A 1 329 ? -15.496 -16.647 -17.395 1.00 22.44  ? 329  ASP A C   1 
ATOM   2589 O O   . ASP A 1 329 ? -14.818 -17.662 -17.473 1.00 22.76  ? 329  ASP A O   1 
ATOM   2590 C CB  . ASP A 1 329 ? -17.166 -17.092 -15.475 1.00 24.28  ? 329  ASP A CB  1 
ATOM   2591 C CG  . ASP A 1 329 ? -18.562 -16.596 -15.842 1.00 27.98  ? 329  ASP A CG  1 
ATOM   2592 O OD1 . ASP A 1 329 ? -18.852 -15.383 -15.765 1.00 30.26  ? 329  ASP A OD1 1 
ATOM   2593 O OD2 . ASP A 1 329 ? -19.411 -17.450 -16.155 1.00 31.62  ? 329  ASP A OD2 1 
ATOM   2594 N N   . TYR A 1 330 ? -15.738 -15.891 -18.477 1.00 21.15  ? 330  TYR A N   1 
ATOM   2595 C CA  . TYR A 1 330 ? -15.278 -16.349 -19.806 1.00 19.64  ? 330  TYR A CA  1 
ATOM   2596 C C   . TYR A 1 330 ? -13.779 -16.180 -19.916 1.00 20.03  ? 330  TYR A C   1 
ATOM   2597 O O   . TYR A 1 330 ? -13.118 -16.822 -20.737 1.00 20.58  ? 330  TYR A O   1 
ATOM   2598 C CB  . TYR A 1 330 ? -15.994 -15.634 -20.973 1.00 19.78  ? 330  TYR A CB  1 
ATOM   2599 C CG  . TYR A 1 330 ? -15.555 -14.213 -21.252 1.00 19.01  ? 330  TYR A CG  1 
ATOM   2600 C CD1 . TYR A 1 330 ? -14.373 -13.939 -21.926 1.00 19.26  ? 330  TYR A CD1 1 
ATOM   2601 C CD2 . TYR A 1 330 ? -16.348 -13.144 -20.880 1.00 20.34  ? 330  TYR A CD2 1 
ATOM   2602 C CE1 . TYR A 1 330 ? -13.981 -12.659 -22.172 1.00 19.76  ? 330  TYR A CE1 1 
ATOM   2603 C CE2 . TYR A 1 330 ? -15.964 -11.849 -21.107 1.00 18.32  ? 330  TYR A CE2 1 
ATOM   2604 C CZ  . TYR A 1 330 ? -14.753 -11.610 -21.741 1.00 19.30  ? 330  TYR A CZ  1 
ATOM   2605 O OH  . TYR A 1 330 ? -14.353 -10.336 -22.012 1.00 17.28  ? 330  TYR A OH  1 
ATOM   2606 N N   . MET A 1 331 ? -13.248 -15.307 -19.088 1.00 18.52  ? 331  MET A N   1 
ATOM   2607 C CA  . MET A 1 331 ? -11.844 -14.913 -19.201 1.00 19.75  ? 331  MET A CA  1 
ATOM   2608 C C   . MET A 1 331 ? -10.908 -15.994 -18.669 1.00 19.79  ? 331  MET A C   1 
ATOM   2609 O O   . MET A 1 331 ? -11.302 -16.853 -17.874 1.00 20.35  ? 331  MET A O   1 
ATOM   2610 C CB  . MET A 1 331 ? -11.595 -13.626 -18.425 1.00 17.73  ? 331  MET A CB  1 
ATOM   2611 C CG  . MET A 1 331 ? -12.368 -12.378 -18.974 1.00 19.80  ? 331  MET A CG  1 
ATOM   2612 S SD  . MET A 1 331 ? -12.133 -10.943 -17.925 1.00 21.94  ? 331  MET A SD  1 
ATOM   2613 C CE  . MET A 1 331 ? -13.205 -9.746  -18.793 1.00 17.01  ? 331  MET A CE  1 
ATOM   2614 N N   . ASP A 1 332 ? -9.648  -15.908 -19.082 1.00 21.69  ? 332  ASP A N   1 
ATOM   2615 C CA  . ASP A 1 332 ? -8.609  -16.752 -18.501 1.00 23.64  ? 332  ASP A CA  1 
ATOM   2616 C C   . ASP A 1 332 ? -8.128  -16.109 -17.202 1.00 23.30  ? 332  ASP A C   1 
ATOM   2617 O O   . ASP A 1 332 ? -7.316  -15.171 -17.214 1.00 22.85  ? 332  ASP A O   1 
ATOM   2618 C CB  . ASP A 1 332 ? -7.449  -16.909 -19.482 1.00 24.05  ? 332  ASP A CB  1 
ATOM   2619 C CG  . ASP A 1 332 ? -6.439  -17.958 -19.023 1.00 29.73  ? 332  ASP A CG  1 
ATOM   2620 O OD1 . ASP A 1 332 ? -6.643  -18.557 -17.946 1.00 32.50  ? 332  ASP A OD1 1 
ATOM   2621 O OD2 . ASP A 1 332 ? -5.462  -18.174 -19.763 1.00 35.14  ? 332  ASP A OD2 1 
ATOM   2622 N N   . GLU A 1 333 ? -8.642  -16.608 -16.081 1.00 23.65  ? 333  GLU A N   1 
ATOM   2623 C CA  . GLU A 1 333 ? -8.291  -16.089 -14.741 1.00 24.45  ? 333  GLU A CA  1 
ATOM   2624 C C   . GLU A 1 333 ? -8.642  -14.596 -14.590 1.00 23.57  ? 333  GLU A C   1 
ATOM   2625 O O   . GLU A 1 333 ? -7.867  -13.786 -14.042 1.00 21.72  ? 333  GLU A O   1 
ATOM   2626 C CB  . GLU A 1 333 ? -6.809  -16.361 -14.398 1.00 25.67  ? 333  GLU A CB  1 
ATOM   2627 C CG  . GLU A 1 333 ? -6.389  -17.857 -14.528 1.00 32.13  ? 333  GLU A CG  1 
ATOM   2628 C CD  . GLU A 1 333 ? -6.924  -18.775 -13.400 1.00 39.77  ? 333  GLU A CD  1 
ATOM   2629 O OE1 . GLU A 1 333 ? -7.569  -18.291 -12.426 1.00 40.66  ? 333  GLU A OE1 1 
ATOM   2630 O OE2 . GLU A 1 333 ? -6.673  -20.008 -13.489 1.00 43.54  ? 333  GLU A OE2 1 
ATOM   2631 N N   . ARG A 1 334 ? -9.825  -14.251 -15.103 1.00 22.72  ? 334  ARG A N   1 
ATOM   2632 C CA  . ARG A 1 334 ? -10.394 -12.940 -14.954 1.00 23.07  ? 334  ARG A CA  1 
ATOM   2633 C C   . ARG A 1 334 ? -9.578  -11.821 -15.596 1.00 22.48  ? 334  ARG A C   1 
ATOM   2634 O O   . ARG A 1 334 ? -9.630  -10.688 -15.155 1.00 23.84  ? 334  ARG A O   1 
ATOM   2635 C CB  . ARG A 1 334 ? -10.709 -12.678 -13.480 1.00 23.02  ? 334  ARG A CB  1 
ATOM   2636 C CG  . ARG A 1 334 ? -11.828 -13.602 -12.989 1.00 24.73  ? 334  ARG A CG  1 
ATOM   2637 C CD  . ARG A 1 334 ? -12.054 -13.610 -11.461 1.00 25.26  ? 334  ARG A CD  1 
ATOM   2638 N NE  . ARG A 1 334 ? -13.302 -14.326 -11.157 1.00 29.15  ? 334  ARG A NE  1 
ATOM   2639 C CZ  . ARG A 1 334 ? -13.934 -14.288 -9.987  1.00 33.20  ? 334  ARG A CZ  1 
ATOM   2640 N NH1 . ARG A 1 334 ? -13.439 -13.559 -8.981  1.00 35.06  ? 334  ARG A NH1 1 
ATOM   2641 N NH2 . ARG A 1 334 ? -15.061 -14.962 -9.824  1.00 32.79  ? 334  ARG A NH2 1 
ATOM   2642 N N   . ARG A 1 335 ? -8.850  -12.131 -16.657 1.00 21.38  ? 335  ARG A N   1 
ATOM   2643 C CA  . ARG A 1 335 ? -8.091  -11.114 -17.364 1.00 21.09  ? 335  ARG A CA  1 
ATOM   2644 C C   . ARG A 1 335 ? -8.680  -10.743 -18.694 1.00 21.25  ? 335  ARG A C   1 
ATOM   2645 O O   . ARG A 1 335 ? -9.045  -11.637 -19.464 1.00 22.09  ? 335  ARG A O   1 
ATOM   2646 C CB  . ARG A 1 335 ? -6.688  -11.636 -17.622 1.00 21.77  ? 335  ARG A CB  1 
ATOM   2647 C CG  . ARG A 1 335 ? -5.932  -11.803 -16.323 1.00 22.26  ? 335  ARG A CG  1 
ATOM   2648 C CD  . ARG A 1 335 ? -4.547  -12.334 -16.576 1.00 26.80  ? 335  ARG A CD  1 
ATOM   2649 N NE  . ARG A 1 335 ? -4.646  -13.656 -17.193 1.00 29.67  ? 335  ARG A NE  1 
ATOM   2650 C CZ  . ARG A 1 335 ? -3.629  -14.279 -17.774 1.00 35.06  ? 335  ARG A CZ  1 
ATOM   2651 N NH1 . ARG A 1 335 ? -2.433  -13.699 -17.806 1.00 33.13  ? 335  ARG A NH1 1 
ATOM   2652 N NH2 . ARG A 1 335 ? -3.808  -15.482 -18.320 1.00 35.53  ? 335  ARG A NH2 1 
ATOM   2653 N N   . ASP A 1 336 ? -8.732  -9.436  -18.984 1.00 21.52  ? 336  ASP A N   1 
ATOM   2654 C CA  . ASP A 1 336 ? -9.341  -8.935  -20.229 1.00 21.86  ? 336  ASP A CA  1 
ATOM   2655 C C   . ASP A 1 336 ? -8.611  -9.528  -21.412 1.00 22.29  ? 336  ASP A C   1 
ATOM   2656 O O   . ASP A 1 336 ? -7.393  -9.763  -21.348 1.00 22.10  ? 336  ASP A O   1 
ATOM   2657 C CB  . ASP A 1 336 ? -9.171  -7.434  -20.373 1.00 21.45  ? 336  ASP A CB  1 
ATOM   2658 C CG  . ASP A 1 336 ? -10.088 -6.621  -19.490 1.00 22.83  ? 336  ASP A CG  1 
ATOM   2659 O OD1 . ASP A 1 336 ? -11.161 -7.098  -19.037 1.00 22.87  ? 336  ASP A OD1 1 
ATOM   2660 O OD2 . ASP A 1 336 ? -9.734  -5.437  -19.306 1.00 27.32  ? 336  ASP A OD2 1 
ATOM   2661 N N   . PHE A 1 337 ? -9.356  -9.723  -22.498 1.00 21.27  ? 337  PHE A N   1 
ATOM   2662 C CA  . PHE A 1 337 ? -8.806  -10.061 -23.821 1.00 21.57  ? 337  PHE A CA  1 
ATOM   2663 C C   . PHE A 1 337 ? -8.176  -11.455 -23.872 1.00 21.95  ? 337  PHE A C   1 
ATOM   2664 O O   . PHE A 1 337 ? -7.272  -11.697 -24.660 1.00 22.43  ? 337  PHE A O   1 
ATOM   2665 C CB  . PHE A 1 337 ? -7.830  -9.001  -24.346 1.00 21.43  ? 337  PHE A CB  1 
ATOM   2666 C CG  . PHE A 1 337 ? -8.341  -7.593  -24.228 1.00 21.32  ? 337  PHE A CG  1 
ATOM   2667 C CD1 . PHE A 1 337 ? -9.517  -7.202  -24.893 1.00 20.36  ? 337  PHE A CD1 1 
ATOM   2668 C CD2 . PHE A 1 337 ? -7.701  -6.674  -23.392 1.00 19.20  ? 337  PHE A CD2 1 
ATOM   2669 C CE1 . PHE A 1 337 ? -9.979  -5.888  -24.763 1.00 19.15  ? 337  PHE A CE1 1 
ATOM   2670 C CE2 . PHE A 1 337 ? -8.181  -5.359  -23.244 1.00 20.03  ? 337  PHE A CE2 1 
ATOM   2671 C CZ  . PHE A 1 337 ? -9.330  -4.985  -23.936 1.00 19.46  ? 337  PHE A CZ  1 
ATOM   2672 N N   . THR A 1 338 ? -8.730  -12.359 -23.068 1.00 22.07  ? 338  THR A N   1 
ATOM   2673 C CA  . THR A 1 338 ? -8.454  -13.777 -23.098 1.00 22.00  ? 338  THR A CA  1 
ATOM   2674 C C   . THR A 1 338 ? -9.770  -14.525 -22.910 1.00 22.77  ? 338  THR A C   1 
ATOM   2675 O O   . THR A 1 338 ? -10.753 -13.952 -22.431 1.00 22.06  ? 338  THR A O   1 
ATOM   2676 C CB  . THR A 1 338 ? -7.541  -14.153 -21.919 1.00 22.74  ? 338  THR A CB  1 
ATOM   2677 O OG1 . THR A 1 338 ? -8.240  -14.004 -20.674 1.00 22.06  ? 338  THR A OG1 1 
ATOM   2678 C CG2 . THR A 1 338 ? -6.252  -13.284 -21.919 1.00 20.39  ? 338  THR A CG2 1 
ATOM   2679 N N   . TYR A 1 339 ? -9.804  -15.802 -23.250 1.00 22.07  ? 339  TYR A N   1 
ATOM   2680 C CA  . TYR A 1 339 ? -10.865 -16.635 -22.714 1.00 23.66  ? 339  TYR A CA  1 
ATOM   2681 C C   . TYR A 1 339 ? -10.239 -17.903 -22.144 1.00 24.46  ? 339  TYR A C   1 
ATOM   2682 O O   . TYR A 1 339 ? -9.100  -18.250 -22.502 1.00 23.89  ? 339  TYR A O   1 
ATOM   2683 C CB  . TYR A 1 339 ? -11.963 -16.902 -23.750 1.00 24.74  ? 339  TYR A CB  1 
ATOM   2684 C CG  . TYR A 1 339 ? -11.598 -17.771 -24.946 1.00 24.68  ? 339  TYR A CG  1 
ATOM   2685 C CD1 . TYR A 1 339 ? -11.744 -19.156 -24.887 1.00 25.43  ? 339  TYR A CD1 1 
ATOM   2686 C CD2 . TYR A 1 339 ? -11.162 -17.204 -26.144 1.00 27.09  ? 339  TYR A CD2 1 
ATOM   2687 C CE1 . TYR A 1 339 ? -11.436 -19.960 -25.982 1.00 26.30  ? 339  TYR A CE1 1 
ATOM   2688 C CE2 . TYR A 1 339 ? -10.844 -18.004 -27.249 1.00 26.71  ? 339  TYR A CE2 1 
ATOM   2689 C CZ  . TYR A 1 339 ? -10.998 -19.371 -27.152 1.00 27.17  ? 339  TYR A CZ  1 
ATOM   2690 O OH  . TYR A 1 339 ? -10.687 -20.171 -28.222 1.00 29.70  ? 339  TYR A OH  1 
ATOM   2691 N N   . ASP A 1 340 ? -10.965 -18.552 -21.239 1.00 24.27  ? 340  ASP A N   1 
ATOM   2692 C CA  . ASP A 1 340 ? -10.506 -19.731 -20.542 1.00 25.94  ? 340  ASP A CA  1 
ATOM   2693 C C   . ASP A 1 340 ? -10.595 -20.918 -21.499 1.00 26.08  ? 340  ASP A C   1 
ATOM   2694 O O   . ASP A 1 340 ? -11.682 -21.432 -21.788 1.00 25.69  ? 340  ASP A O   1 
ATOM   2695 C CB  . ASP A 1 340 ? -11.389 -19.946 -19.323 1.00 26.01  ? 340  ASP A CB  1 
ATOM   2696 C CG  . ASP A 1 340 ? -10.904 -21.071 -18.411 1.00 29.00  ? 340  ASP A CG  1 
ATOM   2697 O OD1 . ASP A 1 340 ? -10.228 -22.020 -18.872 1.00 29.27  ? 340  ASP A OD1 1 
ATOM   2698 O OD2 . ASP A 1 340 ? -11.264 -21.024 -17.224 1.00 30.51  ? 340  ASP A OD2 1 
ATOM   2699 N N   . SER A 1 341 ? -9.433  -21.365 -21.963 1.00 26.78  ? 341  SER A N   1 
ATOM   2700 C CA  . SER A 1 341 ? -9.333  -22.423 -22.970 1.00 27.77  ? 341  SER A CA  1 
ATOM   2701 C C   . SER A 1 341 ? -9.790  -23.791 -22.479 1.00 27.61  ? 341  SER A C   1 
ATOM   2702 O O   . SER A 1 341 ? -9.979  -24.684 -23.286 1.00 29.22  ? 341  SER A O   1 
ATOM   2703 C CB  . SER A 1 341 ? -7.883  -22.517 -23.439 1.00 28.51  ? 341  SER A CB  1 
ATOM   2704 O OG  . SER A 1 341 ? -7.095  -22.916 -22.319 1.00 31.68  ? 341  SER A OG  1 
ATOM   2705 N N   . VAL A 1 342 ? -9.981  -23.968 -21.172 1.00 27.80  ? 342  VAL A N   1 
ATOM   2706 C CA  . VAL A 1 342 ? -10.578 -25.200 -20.620 1.00 27.50  ? 342  VAL A CA  1 
ATOM   2707 C C   . VAL A 1 342 ? -12.075 -25.061 -20.370 1.00 26.55  ? 342  VAL A C   1 
ATOM   2708 O O   . VAL A 1 342 ? -12.876 -25.771 -20.977 1.00 27.03  ? 342  VAL A O   1 
ATOM   2709 C CB  . VAL A 1 342 ? -9.840  -25.672 -19.322 1.00 27.97  ? 342  VAL A CB  1 
ATOM   2710 C CG1 . VAL A 1 342 ? -10.544 -26.852 -18.663 1.00 26.70  ? 342  VAL A CG1 1 
ATOM   2711 C CG2 . VAL A 1 342 ? -8.402  -26.041 -19.666 1.00 29.85  ? 342  VAL A CG2 1 
ATOM   2712 N N   . ASP A 1 343 ? -12.469 -24.159 -19.475 1.00 25.25  ? 343  ASP A N   1 
ATOM   2713 C CA  . ASP A 1 343 ? -13.896 -24.032 -19.141 1.00 24.62  ? 343  ASP A CA  1 
ATOM   2714 C C   . ASP A 1 343 ? -14.713 -23.369 -20.237 1.00 23.35  ? 343  ASP A C   1 
ATOM   2715 O O   . ASP A 1 343 ? -15.932 -23.553 -20.281 1.00 22.57  ? 343  ASP A O   1 
ATOM   2716 C CB  . ASP A 1 343 ? -14.079 -23.250 -17.846 1.00 25.06  ? 343  ASP A CB  1 
ATOM   2717 C CG  . ASP A 1 343 ? -13.693 -24.057 -16.616 1.00 28.04  ? 343  ASP A CG  1 
ATOM   2718 O OD1 . ASP A 1 343 ? -13.399 -25.262 -16.748 1.00 31.51  ? 343  ASP A OD1 1 
ATOM   2719 O OD2 . ASP A 1 343 ? -13.708 -23.477 -15.518 1.00 31.11  ? 343  ASP A OD2 1 
ATOM   2720 N N   . PHE A 1 344 ? -14.062 -22.547 -21.049 1.00 22.84  ? 344  PHE A N   1 
ATOM   2721 C CA  . PHE A 1 344 ? -14.725 -21.879 -22.187 1.00 23.44  ? 344  PHE A CA  1 
ATOM   2722 C C   . PHE A 1 344 ? -14.099 -22.344 -23.508 1.00 23.74  ? 344  PHE A C   1 
ATOM   2723 O O   . PHE A 1 344 ? -13.980 -21.588 -24.464 1.00 22.64  ? 344  PHE A O   1 
ATOM   2724 C CB  . PHE A 1 344 ? -14.792 -20.345 -22.022 1.00 22.66  ? 344  PHE A CB  1 
ATOM   2725 C CG  . PHE A 1 344 ? -15.918 -19.894 -21.097 1.00 25.20  ? 344  PHE A CG  1 
ATOM   2726 C CD1 . PHE A 1 344 ? -15.815 -20.037 -19.698 1.00 25.12  ? 344  PHE A CD1 1 
ATOM   2727 C CD2 . PHE A 1 344 ? -17.120 -19.392 -21.634 1.00 23.98  ? 344  PHE A CD2 1 
ATOM   2728 C CE1 . PHE A 1 344 ? -16.909 -19.667 -18.849 1.00 23.93  ? 344  PHE A CE1 1 
ATOM   2729 C CE2 . PHE A 1 344 ? -18.199 -19.016 -20.796 1.00 23.33  ? 344  PHE A CE2 1 
ATOM   2730 C CZ  . PHE A 1 344 ? -18.091 -19.154 -19.417 1.00 25.30  ? 344  PHE A CZ  1 
ATOM   2731 N N   . LYS A 1 345 ? -13.724 -23.623 -23.554 1.00 25.89  ? 345  LYS A N   1 
ATOM   2732 C CA  . LYS A 1 345 ? -13.177 -24.221 -24.789 1.00 27.50  ? 345  LYS A CA  1 
ATOM   2733 C C   . LYS A 1 345 ? -14.323 -24.259 -25.768 1.00 26.83  ? 345  LYS A C   1 
ATOM   2734 O O   . LYS A 1 345 ? -15.414 -24.720 -25.435 1.00 27.60  ? 345  LYS A O   1 
ATOM   2735 C CB  . LYS A 1 345 ? -12.679 -25.645 -24.542 1.00 28.39  ? 345  LYS A CB  1 
ATOM   2736 C CG  . LYS A 1 345 ? -11.996 -26.297 -25.778 1.00 30.59  ? 345  LYS A CG  1 
ATOM   2737 C CD  . LYS A 1 345 ? -11.740 -27.817 -25.533 1.00 30.51  ? 345  LYS A CD  1 
ATOM   2738 C CE  . LYS A 1 345 ? -10.882 -28.453 -26.646 1.00 35.36  ? 345  LYS A CE  1 
ATOM   2739 N NZ  . LYS A 1 345 ? -11.175 -29.920 -26.709 1.00 39.71  ? 345  LYS A NZ  1 
ATOM   2740 N N   . GLY A 1 346 ? -14.094 -23.738 -26.953 1.00 27.23  ? 346  GLY A N   1 
ATOM   2741 C CA  . GLY A 1 346 ? -15.147 -23.685 -27.966 1.00 27.02  ? 346  GLY A CA  1 
ATOM   2742 C C   . GLY A 1 346 ? -16.002 -22.433 -27.932 1.00 26.93  ? 346  GLY A C   1 
ATOM   2743 O O   . GLY A 1 346 ? -17.048 -22.381 -28.579 1.00 26.48  ? 346  GLY A O   1 
ATOM   2744 N N   . PHE A 1 347 ? -15.557 -21.425 -27.177 1.00 26.22  ? 347  PHE A N   1 
ATOM   2745 C CA  . PHE A 1 347 ? -16.196 -20.098 -27.163 1.00 25.73  ? 347  PHE A CA  1 
ATOM   2746 C C   . PHE A 1 347 ? -16.496 -19.546 -28.594 1.00 25.05  ? 347  PHE A C   1 
ATOM   2747 O O   . PHE A 1 347 ? -17.641 -19.136 -28.846 1.00 25.19  ? 347  PHE A O   1 
ATOM   2748 C CB  . PHE A 1 347 ? -15.369 -19.121 -26.290 1.00 25.93  ? 347  PHE A CB  1 
ATOM   2749 C CG  . PHE A 1 347 ? -16.153 -17.963 -25.715 1.00 25.92  ? 347  PHE A CG  1 
ATOM   2750 C CD1 . PHE A 1 347 ? -17.546 -18.037 -25.522 1.00 28.24  ? 347  PHE A CD1 1 
ATOM   2751 C CD2 . PHE A 1 347 ? -15.486 -16.816 -25.303 1.00 27.59  ? 347  PHE A CD2 1 
ATOM   2752 C CE1 . PHE A 1 347 ? -18.248 -16.961 -24.968 1.00 26.48  ? 347  PHE A CE1 1 
ATOM   2753 C CE2 . PHE A 1 347 ? -16.178 -15.736 -24.763 1.00 26.86  ? 347  PHE A CE2 1 
ATOM   2754 C CZ  . PHE A 1 347 ? -17.565 -15.816 -24.598 1.00 26.10  ? 347  PHE A CZ  1 
ATOM   2755 N N   . PRO A 1 348 ? -15.503 -19.579 -29.540 1.00 24.70  ? 348  PRO A N   1 
ATOM   2756 C CA  . PRO A 1 348 ? -15.767 -19.135 -30.907 1.00 24.39  ? 348  PRO A CA  1 
ATOM   2757 C C   . PRO A 1 348 ? -16.871 -19.910 -31.599 1.00 24.27  ? 348  PRO A C   1 
ATOM   2758 O O   . PRO A 1 348 ? -17.648 -19.299 -32.334 1.00 24.31  ? 348  PRO A O   1 
ATOM   2759 C CB  . PRO A 1 348 ? -14.409 -19.332 -31.607 1.00 24.21  ? 348  PRO A CB  1 
ATOM   2760 C CG  . PRO A 1 348 ? -13.442 -19.158 -30.475 1.00 23.65  ? 348  PRO A CG  1 
ATOM   2761 C CD  . PRO A 1 348 ? -14.087 -19.975 -29.423 1.00 24.63  ? 348  PRO A CD  1 
ATOM   2762 N N   . GLU A 1 349 ? -17.002 -21.207 -31.316 1.00 23.23  ? 349  GLU A N   1 
ATOM   2763 C CA  . GLU A 1 349 ? -18.085 -21.987 -31.924 1.00 24.93  ? 349  GLU A CA  1 
ATOM   2764 C C   . GLU A 1 349 ? -19.450 -21.584 -31.336 1.00 23.89  ? 349  GLU A C   1 
ATOM   2765 O O   . GLU A 1 349 ? -20.471 -21.560 -32.026 1.00 21.74  ? 349  GLU A O   1 
ATOM   2766 C CB  . GLU A 1 349 ? -17.881 -23.496 -31.726 1.00 24.92  ? 349  GLU A CB  1 
ATOM   2767 C CG  . GLU A 1 349 ? -16.638 -24.099 -32.419 1.00 28.79  ? 349  GLU A CG  1 
ATOM   2768 C CD  . GLU A 1 349 ? -16.084 -25.331 -31.688 1.00 30.24  ? 349  GLU A CD  1 
ATOM   2769 O OE1 . GLU A 1 349 ? -16.896 -26.252 -31.397 1.00 35.73  ? 349  GLU A OE1 1 
ATOM   2770 O OE2 . GLU A 1 349 ? -14.839 -25.379 -31.438 1.00 33.44  ? 349  GLU A OE2 1 
ATOM   2771 N N   . PHE A 1 350 ? -19.446 -21.289 -30.047 1.00 23.23  ? 350  PHE A N   1 
ATOM   2772 C CA  . PHE A 1 350 ? -20.657 -20.817 -29.350 1.00 22.26  ? 350  PHE A CA  1 
ATOM   2773 C C   . PHE A 1 350 ? -21.106 -19.463 -29.884 1.00 21.59  ? 350  PHE A C   1 
ATOM   2774 O O   . PHE A 1 350 ? -22.318 -19.206 -30.043 1.00 20.97  ? 350  PHE A O   1 
ATOM   2775 C CB  . PHE A 1 350 ? -20.405 -20.733 -27.837 1.00 22.66  ? 350  PHE A CB  1 
ATOM   2776 C CG  . PHE A 1 350 ? -21.504 -20.001 -27.067 1.00 23.20  ? 350  PHE A CG  1 
ATOM   2777 C CD1 . PHE A 1 350 ? -22.719 -20.627 -26.812 1.00 23.90  ? 350  PHE A CD1 1 
ATOM   2778 C CD2 . PHE A 1 350 ? -21.292 -18.716 -26.584 1.00 23.06  ? 350  PHE A CD2 1 
ATOM   2779 C CE1 . PHE A 1 350 ? -23.742 -19.970 -26.092 1.00 24.86  ? 350  PHE A CE1 1 
ATOM   2780 C CE2 . PHE A 1 350 ? -22.295 -18.051 -25.852 1.00 23.12  ? 350  PHE A CE2 1 
ATOM   2781 C CZ  . PHE A 1 350 ? -23.529 -18.699 -25.609 1.00 23.82  ? 350  PHE A CZ  1 
ATOM   2782 N N   . VAL A 1 351 ? -20.153 -18.586 -30.155 1.00 20.03  ? 351  VAL A N   1 
ATOM   2783 C CA  . VAL A 1 351 ? -20.449 -17.294 -30.792 1.00 21.46  ? 351  VAL A CA  1 
ATOM   2784 C C   . VAL A 1 351 ? -21.192 -17.475 -32.142 1.00 21.35  ? 351  VAL A C   1 
ATOM   2785 O O   . VAL A 1 351 ? -22.229 -16.835 -32.392 1.00 20.83  ? 351  VAL A O   1 
ATOM   2786 C CB  . VAL A 1 351 ? -19.178 -16.426 -30.871 1.00 21.67  ? 351  VAL A CB  1 
ATOM   2787 C CG1 . VAL A 1 351 ? -19.432 -15.117 -31.616 1.00 23.03  ? 351  VAL A CG1 1 
ATOM   2788 C CG2 . VAL A 1 351 ? -18.748 -16.105 -29.468 1.00 22.06  ? 351  VAL A CG2 1 
ATOM   2789 N N   . ASN A 1 352 ? -20.711 -18.422 -32.950 1.00 21.00  ? 352  ASN A N   1 
ATOM   2790 C CA  . ASN A 1 352 ? -21.364 -18.757 -34.217 1.00 20.56  ? 352  ASN A CA  1 
ATOM   2791 C C   . ASN A 1 352 ? -22.773 -19.258 -34.000 1.00 19.95  ? 352  ASN A C   1 
ATOM   2792 O O   . ASN A 1 352 ? -23.659 -18.916 -34.777 1.00 18.45  ? 352  ASN A O   1 
ATOM   2793 C CB  . ASN A 1 352 ? -20.595 -19.842 -34.954 1.00 20.88  ? 352  ASN A CB  1 
ATOM   2794 C CG  . ASN A 1 352 ? -19.348 -19.322 -35.617 1.00 22.92  ? 352  ASN A CG  1 
ATOM   2795 O OD1 . ASN A 1 352 ? -19.008 -18.160 -35.498 1.00 23.53  ? 352  ASN A OD1 1 
ATOM   2796 N ND2 . ASN A 1 352 ? -18.679 -20.184 -36.355 1.00 25.21  ? 352  ASN A ND2 1 
ATOM   2797 N N   . GLU A 1 353 ? -22.958 -20.108 -32.994 1.00 20.06  ? 353  GLU A N   1 
ATOM   2798 C CA  . GLU A 1 353 ? -24.303 -20.608 -32.647 1.00 22.20  ? 353  GLU A CA  1 
ATOM   2799 C C   . GLU A 1 353 ? -25.210 -19.434 -32.292 1.00 21.25  ? 353  GLU A C   1 
ATOM   2800 O O   . GLU A 1 353 ? -26.349 -19.397 -32.742 1.00 20.86  ? 353  GLU A O   1 
ATOM   2801 C CB  . GLU A 1 353 ? -24.286 -21.604 -31.470 1.00 21.08  ? 353  GLU A CB  1 
ATOM   2802 C CG  . GLU A 1 353 ? -23.652 -22.925 -31.821 1.00 26.70  ? 353  GLU A CG  1 
ATOM   2803 C CD  . GLU A 1 353 ? -23.178 -23.777 -30.623 1.00 28.04  ? 353  GLU A CD  1 
ATOM   2804 O OE1 . GLU A 1 353 ? -23.097 -23.302 -29.446 1.00 32.82  ? 353  GLU A OE1 1 
ATOM   2805 O OE2 . GLU A 1 353 ? -22.847 -24.947 -30.907 1.00 33.72  ? 353  GLU A OE2 1 
ATOM   2806 N N   . LEU A 1 354 ? -24.725 -18.507 -31.456 1.00 19.79  ? 354  LEU A N   1 
ATOM   2807 C CA  . LEU A 1 354 ? -25.539 -17.341 -31.106 1.00 19.54  ? 354  LEU A CA  1 
ATOM   2808 C C   . LEU A 1 354 ? -25.933 -16.613 -32.378 1.00 19.63  ? 354  LEU A C   1 
ATOM   2809 O O   . LEU A 1 354 ? -27.136 -16.347 -32.620 1.00 18.11  ? 354  LEU A O   1 
ATOM   2810 C CB  . LEU A 1 354 ? -24.793 -16.378 -30.159 1.00 19.57  ? 354  LEU A CB  1 
ATOM   2811 C CG  . LEU A 1 354 ? -24.691 -16.743 -28.670 1.00 19.88  ? 354  LEU A CG  1 
ATOM   2812 C CD1 . LEU A 1 354 ? -23.873 -15.613 -28.018 1.00 17.96  ? 354  LEU A CD1 1 
ATOM   2813 C CD2 . LEU A 1 354 ? -26.068 -16.894 -27.969 1.00 21.06  ? 354  LEU A CD2 1 
ATOM   2814 N N   . HIS A 1 355 ? -24.939 -16.357 -33.223 1.00 18.30  ? 355  HIS A N   1 
ATOM   2815 C CA  . HIS A 1 355 ? -25.165 -15.588 -34.432 1.00 20.52  ? 355  HIS A CA  1 
ATOM   2816 C C   . HIS A 1 355 ? -26.136 -16.262 -35.396 1.00 21.13  ? 355  HIS A C   1 
ATOM   2817 O O   . HIS A 1 355 ? -27.004 -15.610 -35.951 1.00 20.47  ? 355  HIS A O   1 
ATOM   2818 C CB  . HIS A 1 355 ? -23.844 -15.224 -35.097 1.00 20.60  ? 355  HIS A CB  1 
ATOM   2819 C CG  . HIS A 1 355 ? -23.062 -14.192 -34.328 1.00 21.75  ? 355  HIS A CG  1 
ATOM   2820 N ND1 . HIS A 1 355 ? -21.720 -13.960 -34.541 1.00 21.25  ? 355  HIS A ND1 1 
ATOM   2821 C CD2 . HIS A 1 355 ? -23.442 -13.320 -33.356 1.00 19.54  ? 355  HIS A CD2 1 
ATOM   2822 C CE1 . HIS A 1 355 ? -21.309 -12.990 -33.738 1.00 20.79  ? 355  HIS A CE1 1 
ATOM   2823 N NE2 . HIS A 1 355 ? -22.322 -12.609 -32.989 1.00 22.70  ? 355  HIS A NE2 1 
ATOM   2824 N N   . ASN A 1 356 ? -25.974 -17.567 -35.573 1.00 21.45  ? 356  ASN A N   1 
ATOM   2825 C CA  . ASN A 1 356 ? -26.884 -18.364 -36.399 1.00 22.42  ? 356  ASN A CA  1 
ATOM   2826 C C   . ASN A 1 356 ? -28.319 -18.361 -35.873 1.00 23.13  ? 356  ASN A C   1 
ATOM   2827 O O   . ASN A 1 356 ? -29.271 -18.624 -36.622 1.00 22.85  ? 356  ASN A O   1 
ATOM   2828 C CB  . ASN A 1 356 ? -26.384 -19.818 -36.450 1.00 23.10  ? 356  ASN A CB  1 
ATOM   2829 C CG  . ASN A 1 356 ? -27.143 -20.641 -37.458 1.00 25.18  ? 356  ASN A CG  1 
ATOM   2830 O OD1 . ASN A 1 356 ? -27.431 -20.156 -38.540 1.00 28.73  ? 356  ASN A OD1 1 
ATOM   2831 N ND2 . ASN A 1 356 ? -27.515 -21.863 -37.095 1.00 26.31  ? 356  ASN A ND2 1 
ATOM   2832 N N   . ASN A 1 357 ? -28.473 -18.120 -34.577 1.00 22.49  ? 357  ASN A N   1 
ATOM   2833 C CA  . ASN A 1 357 ? -29.814 -18.057 -33.976 1.00 23.23  ? 357  ASN A CA  1 
ATOM   2834 C C   . ASN A 1 357 ? -30.380 -16.641 -33.943 1.00 22.49  ? 357  ASN A C   1 
ATOM   2835 O O   . ASN A 1 357 ? -31.460 -16.386 -33.362 1.00 22.24  ? 357  ASN A O   1 
ATOM   2836 C CB  . ASN A 1 357 ? -29.785 -18.680 -32.581 1.00 24.12  ? 357  ASN A CB  1 
ATOM   2837 C CG  . ASN A 1 357 ? -29.486 -20.196 -32.619 1.00 28.20  ? 357  ASN A CG  1 
ATOM   2838 O OD1 . ASN A 1 357 ? -28.738 -20.690 -31.811 1.00 35.03  ? 357  ASN A OD1 1 
ATOM   2839 N ND2 . ASN A 1 357 ? -30.068 -20.911 -33.562 1.00 31.32  ? 357  ASN A ND2 1 
ATOM   2840 N N   . GLY A 1 358 ? -29.651 -15.718 -34.557 1.00 21.32  ? 358  GLY A N   1 
ATOM   2841 C CA  . GLY A 1 358 ? -30.076 -14.329 -34.643 1.00 21.05  ? 358  GLY A CA  1 
ATOM   2842 C C   . GLY A 1 358 ? -29.736 -13.519 -33.401 1.00 20.00  ? 358  GLY A C   1 
ATOM   2843 O O   . GLY A 1 358 ? -30.133 -12.371 -33.272 1.00 20.51  ? 358  GLY A O   1 
ATOM   2844 N N   . GLN A 1 359 ? -28.923 -14.083 -32.520 1.00 18.99  ? 359  GLN A N   1 
ATOM   2845 C CA  . GLN A 1 359 ? -28.610 -13.413 -31.279 1.00 17.97  ? 359  GLN A CA  1 
ATOM   2846 C C   . GLN A 1 359 ? -27.237 -12.740 -31.273 1.00 17.90  ? 359  GLN A C   1 
ATOM   2847 O O   . GLN A 1 359 ? -26.406 -12.934 -32.170 1.00 18.08  ? 359  GLN A O   1 
ATOM   2848 C CB  . GLN A 1 359 ? -28.686 -14.426 -30.153 1.00 17.66  ? 359  GLN A CB  1 
ATOM   2849 C CG  . GLN A 1 359 ? -30.086 -14.956 -29.924 1.00 20.51  ? 359  GLN A CG  1 
ATOM   2850 C CD  . GLN A 1 359 ? -30.062 -16.115 -28.971 1.00 22.83  ? 359  GLN A CD  1 
ATOM   2851 O OE1 . GLN A 1 359 ? -29.422 -17.130 -29.239 1.00 24.32  ? 359  GLN A OE1 1 
ATOM   2852 N NE2 . GLN A 1 359 ? -30.749 -15.973 -27.839 1.00 20.74  ? 359  GLN A NE2 1 
ATOM   2853 N N   . LYS A 1 360 ? -27.001 -11.949 -30.222 1.00 17.76  ? 360  LYS A N   1 
ATOM   2854 C CA  . LYS A 1 360 ? -25.791 -11.143 -30.098 1.00 17.61  ? 360  LYS A CA  1 
ATOM   2855 C C   . LYS A 1 360 ? -25.074 -11.493 -28.809 1.00 17.90  ? 360  LYS A C   1 
ATOM   2856 O O   . LYS A 1 360 ? -25.689 -11.902 -27.829 1.00 17.55  ? 360  LYS A O   1 
ATOM   2857 C CB  . LYS A 1 360 ? -26.133 -9.648  -30.117 1.00 18.64  ? 360  LYS A CB  1 
ATOM   2858 C CG  . LYS A 1 360 ? -26.959 -9.209  -31.364 1.00 19.36  ? 360  LYS A CG  1 
ATOM   2859 C CD  . LYS A 1 360 ? -26.113 -9.210  -32.646 1.00 19.93  ? 360  LYS A CD  1 
ATOM   2860 C CE  . LYS A 1 360 ? -26.952 -8.905  -33.898 1.00 25.71  ? 360  LYS A CE  1 
ATOM   2861 N NZ  . LYS A 1 360 ? -26.117 -8.507  -35.085 1.00 31.50  ? 360  LYS A NZ  1 
ATOM   2862 N N   . LEU A 1 361 ? -23.761 -11.340 -28.834 1.00 17.92  ? 361  LEU A N   1 
ATOM   2863 C CA  . LEU A 1 361 ? -22.932 -11.577 -27.657 1.00 18.08  ? 361  LEU A CA  1 
ATOM   2864 C C   . LEU A 1 361 ? -22.388 -10.238 -27.190 1.00 16.65  ? 361  LEU A C   1 
ATOM   2865 O O   . LEU A 1 361 ? -21.816 -9.484  -27.964 1.00 17.92  ? 361  LEU A O   1 
ATOM   2866 C CB  . LEU A 1 361 ? -21.757 -12.527 -27.976 1.00 18.08  ? 361  LEU A CB  1 
ATOM   2867 C CG  . LEU A 1 361 ? -20.738 -12.588 -26.823 1.00 18.82  ? 361  LEU A CG  1 
ATOM   2868 C CD1 . LEU A 1 361 ? -21.329 -13.331 -25.626 1.00 18.51  ? 361  LEU A CD1 1 
ATOM   2869 C CD2 . LEU A 1 361 ? -19.403 -13.219 -27.294 1.00 18.93  ? 361  LEU A CD2 1 
ATOM   2870 N N   . VAL A 1 362 ? -22.603 -9.930  -25.929 1.00 16.88  ? 362  VAL A N   1 
ATOM   2871 C CA  . VAL A 1 362 ? -21.979 -8.781  -25.313 1.00 16.69  ? 362  VAL A CA  1 
ATOM   2872 C C   . VAL A 1 362 ? -20.977 -9.301  -24.272 1.00 16.23  ? 362  VAL A C   1 
ATOM   2873 O O   . VAL A 1 362 ? -21.333 -10.114 -23.424 1.00 17.04  ? 362  VAL A O   1 
ATOM   2874 C CB  . VAL A 1 362 ? -23.035 -7.857  -24.654 1.00 16.74  ? 362  VAL A CB  1 
ATOM   2875 C CG1 . VAL A 1 362 ? -22.352 -6.839  -23.736 1.00 15.51  ? 362  VAL A CG1 1 
ATOM   2876 C CG2 . VAL A 1 362 ? -23.861 -7.158  -25.734 1.00 14.37  ? 362  VAL A CG2 1 
ATOM   2877 N N   . ILE A 1 363 ? -19.743 -8.814  -24.329 1.00 16.20  ? 363  ILE A N   1 
ATOM   2878 C CA  . ILE A 1 363 ? -18.707 -9.232  -23.375 1.00 17.55  ? 363  ILE A CA  1 
ATOM   2879 C C   . ILE A 1 363 ? -18.359 -8.124  -22.379 1.00 15.98  ? 363  ILE A C   1 
ATOM   2880 O O   . ILE A 1 363 ? -18.295 -6.972  -22.741 1.00 16.29  ? 363  ILE A O   1 
ATOM   2881 C CB  . ILE A 1 363 ? -17.380 -9.684  -24.093 1.00 17.39  ? 363  ILE A CB  1 
ATOM   2882 C CG1 . ILE A 1 363 ? -16.817 -8.588  -25.006 1.00 18.76  ? 363  ILE A CG1 1 
ATOM   2883 C CG2 . ILE A 1 363 ? -17.642 -10.974 -24.861 1.00 19.46  ? 363  ILE A CG2 1 
ATOM   2884 C CD1 . ILE A 1 363 ? -15.288 -8.765  -25.364 1.00 19.11  ? 363  ILE A CD1 1 
ATOM   2885 N N   . ILE A 1 364 ? -18.093 -8.505  -21.138 1.00 16.07  ? 364  ILE A N   1 
ATOM   2886 C CA  . ILE A 1 364 ? -17.708 -7.564  -20.119 1.00 16.17  ? 364  ILE A CA  1 
ATOM   2887 C C   . ILE A 1 364 ? -16.217 -7.365  -20.347 1.00 17.92  ? 364  ILE A C   1 
ATOM   2888 O O   . ILE A 1 364 ? -15.531 -8.328  -20.688 1.00 16.78  ? 364  ILE A O   1 
ATOM   2889 C CB  . ILE A 1 364 ? -17.995 -8.090  -18.679 1.00 15.68  ? 364  ILE A CB  1 
ATOM   2890 C CG1 . ILE A 1 364 ? -17.983 -6.927  -17.672 1.00 16.47  ? 364  ILE A CG1 1 
ATOM   2891 C CG2 . ILE A 1 364 ? -17.010 -9.228  -18.238 1.00 17.99  ? 364  ILE A CG2 1 
ATOM   2892 C CD1 . ILE A 1 364 ? -18.524 -7.264  -16.265 1.00 17.05  ? 364  ILE A CD1 1 
ATOM   2893 N N   . VAL A 1 365 ? -15.768 -6.134  -20.166 1.00 18.46  ? 365  VAL A N   1 
ATOM   2894 C CA  . VAL A 1 365 ? -14.367 -5.774  -20.222 1.00 21.22  ? 365  VAL A CA  1 
ATOM   2895 C C   . VAL A 1 365 ? -14.168 -4.841  -19.007 1.00 21.42  ? 365  VAL A C   1 
ATOM   2896 O O   . VAL A 1 365 ? -15.022 -4.001  -18.704 1.00 21.58  ? 365  VAL A O   1 
ATOM   2897 C CB  . VAL A 1 365 ? -13.996 -5.089  -21.585 1.00 21.63  ? 365  VAL A CB  1 
ATOM   2898 C CG1 . VAL A 1 365 ? -12.516 -4.898  -21.687 1.00 24.10  ? 365  VAL A CG1 1 
ATOM   2899 C CG2 . VAL A 1 365 ? -14.426 -5.941  -22.761 1.00 23.25  ? 365  VAL A CG2 1 
ATOM   2900 N N   . ASP A 1 366 ? -13.051 -5.018  -18.286 1.00 21.30  ? 366  ASP A N   1 
ATOM   2901 C CA  . ASP A 1 366 ? -12.787 -4.236  -17.089 1.00 20.99  ? 366  ASP A CA  1 
ATOM   2902 C C   . ASP A 1 366 ? -11.642 -3.282  -17.451 1.00 21.15  ? 366  ASP A C   1 
ATOM   2903 O O   . ASP A 1 366 ? -10.904 -3.564  -18.387 1.00 19.41  ? 366  ASP A O   1 
ATOM   2904 C CB  . ASP A 1 366 ? -12.423 -5.159  -15.896 1.00 21.01  ? 366  ASP A CB  1 
ATOM   2905 C CG  . ASP A 1 366 ? -13.617 -6.016  -15.399 1.00 26.49  ? 366  ASP A CG  1 
ATOM   2906 O OD1 . ASP A 1 366 ? -14.733 -5.478  -15.200 1.00 25.40  ? 366  ASP A OD1 1 
ATOM   2907 O OD2 . ASP A 1 366 ? -13.420 -7.231  -15.171 1.00 28.91  ? 366  ASP A OD2 1 
ATOM   2908 N N   . PRO A 1 367 ? -11.563 -2.111  -16.800 1.00 20.38  ? 367  PRO A N   1 
ATOM   2909 C CA  . PRO A 1 367 ? -10.467 -1.259  -17.159 1.00 21.39  ? 367  PRO A CA  1 
ATOM   2910 C C   . PRO A 1 367 ? -9.154  -1.847  -16.637 1.00 21.98  ? 367  PRO A C   1 
ATOM   2911 O O   . PRO A 1 367 ? -8.131  -1.749  -17.326 1.00 23.32  ? 367  PRO A O   1 
ATOM   2912 C CB  . PRO A 1 367 ? -10.799 0.068   -16.452 1.00 20.90  ? 367  PRO A CB  1 
ATOM   2913 C CG  . PRO A 1 367 ? -11.699 -0.304  -15.339 1.00 21.81  ? 367  PRO A CG  1 
ATOM   2914 C CD  . PRO A 1 367 ? -12.466 -1.490  -15.815 1.00 21.17  ? 367  PRO A CD  1 
ATOM   2915 N N   . ALA A 1 368 ? -9.159  -2.463  -15.453 1.00 21.90  ? 368  ALA A N   1 
ATOM   2916 C CA  . ALA A 1 368 ? -7.836  -2.762  -14.849 1.00 22.07  ? 368  ALA A CA  1 
ATOM   2917 C C   . ALA A 1 368 ? -7.214  -3.923  -15.578 1.00 21.96  ? 368  ALA A C   1 
ATOM   2918 O O   . ALA A 1 368 ? -7.912  -4.856  -15.968 1.00 22.80  ? 368  ALA A O   1 
ATOM   2919 C CB  . ALA A 1 368 ? -7.962  -3.060  -13.405 1.00 22.79  ? 368  ALA A CB  1 
ATOM   2920 N N   . ILE A 1 369 ? -5.901  -3.855  -15.749 1.00 20.87  ? 369  ILE A N   1 
ATOM   2921 C CA  . ILE A 1 369 ? -5.132  -4.785  -16.562 1.00 21.20  ? 369  ILE A CA  1 
ATOM   2922 C C   . ILE A 1 369 ? -4.111  -5.441  -15.636 1.00 21.05  ? 369  ILE A C   1 
ATOM   2923 O O   . ILE A 1 369 ? -3.337  -4.739  -14.979 1.00 20.88  ? 369  ILE A O   1 
ATOM   2924 C CB  . ILE A 1 369 ? -4.366  -4.053  -17.711 1.00 20.44  ? 369  ILE A CB  1 
ATOM   2925 C CG1 . ILE A 1 369 ? -5.344  -3.399  -18.705 1.00 20.83  ? 369  ILE A CG1 1 
ATOM   2926 C CG2 . ILE A 1 369 ? -3.407  -5.007  -18.455 1.00 22.58  ? 369  ILE A CG2 1 
ATOM   2927 C CD1 . ILE A 1 369 ? -6.420  -4.347  -19.267 1.00 19.45  ? 369  ILE A CD1 1 
ATOM   2928 N N   . SER A 1 370 ? -4.128  -6.769  -15.600 1.00 21.53  ? 370  SER A N   1 
ATOM   2929 C CA  . SER A 1 370 ? -3.184  -7.555  -14.815 1.00 23.64  ? 370  SER A CA  1 
ATOM   2930 C C   . SER A 1 370 ? -1.749  -7.136  -15.138 1.00 23.69  ? 370  SER A C   1 
ATOM   2931 O O   . SER A 1 370 ? -1.418  -7.029  -16.302 1.00 24.14  ? 370  SER A O   1 
ATOM   2932 C CB  . SER A 1 370 ? -3.322  -9.021  -15.196 1.00 23.22  ? 370  SER A CB  1 
ATOM   2933 O OG  . SER A 1 370 ? -2.352  -9.784  -14.504 1.00 25.21  ? 370  SER A OG  1 
ATOM   2934 N N   . ASN A 1 371 ? -0.912  -6.916  -14.130 1.00 24.65  ? 371  ASN A N   1 
ATOM   2935 C CA  . ASN A 1 371 ? 0.487   -6.540  -14.414 1.00 25.86  ? 371  ASN A CA  1 
ATOM   2936 C C   . ASN A 1 371 ? 1.433   -7.741  -14.336 1.00 27.63  ? 371  ASN A C   1 
ATOM   2937 O O   . ASN A 1 371 ? 2.645   -7.587  -14.233 1.00 27.16  ? 371  ASN A O   1 
ATOM   2938 C CB  . ASN A 1 371 ? 0.994   -5.396  -13.504 1.00 25.00  ? 371  ASN A CB  1 
ATOM   2939 C CG  . ASN A 1 371 ? 1.110   -5.799  -12.039 1.00 25.87  ? 371  ASN A CG  1 
ATOM   2940 O OD1 . ASN A 1 371 ? 0.647   -6.865  -11.629 1.00 25.70  ? 371  ASN A OD1 1 
ATOM   2941 N ND2 . ASN A 1 371 ? 1.719   -4.924  -11.233 1.00 27.35  ? 371  ASN A ND2 1 
ATOM   2942 N N   . ASN A 1 372 ? 0.873   -8.930  -14.383 1.00 28.39  ? 372  ASN A N   1 
ATOM   2943 C CA  . ASN A 1 372 ? 1.657   -10.141 -14.230 1.00 30.76  ? 372  ASN A CA  1 
ATOM   2944 C C   . ASN A 1 372 ? 2.022   -10.656 -15.614 1.00 31.39  ? 372  ASN A C   1 
ATOM   2945 O O   . ASN A 1 372 ? 1.201   -11.248 -16.292 1.00 31.84  ? 372  ASN A O   1 
ATOM   2946 C CB  . ASN A 1 372 ? 0.859   -11.172 -13.429 1.00 31.21  ? 372  ASN A CB  1 
ATOM   2947 C CG  . ASN A 1 372 ? 1.725   -12.307 -12.908 1.00 33.86  ? 372  ASN A CG  1 
ATOM   2948 O OD1 . ASN A 1 372 ? 2.722   -12.661 -13.516 1.00 34.07  ? 372  ASN A OD1 1 
ATOM   2949 N ND2 . ASN A 1 372 ? 1.327   -12.891 -11.790 1.00 37.00  ? 372  ASN A ND2 1 
ATOM   2950 N N   . SER A 1 373 ? 3.257   -10.406 -16.037 1.00 33.17  ? 373  SER A N   1 
ATOM   2951 C CA  . SER A 1 373 ? 3.711   -10.822 -17.348 1.00 34.30  ? 373  SER A CA  1 
ATOM   2952 C C   . SER A 1 373 ? 5.208   -11.076 -17.286 1.00 36.38  ? 373  SER A C   1 
ATOM   2953 O O   . SER A 1 373 ? 5.928   -10.308 -16.684 1.00 36.89  ? 373  SER A O   1 
ATOM   2954 C CB  . SER A 1 373 ? 3.435   -9.726  -18.366 1.00 34.34  ? 373  SER A CB  1 
ATOM   2955 O OG  . SER A 1 373 ? 3.731   -10.141 -19.687 1.00 32.46  ? 373  SER A OG  1 
ATOM   2956 N N   . SER A 1 374 ? 5.648   -12.165 -17.905 1.00 38.26  ? 374  SER A N   1 
ATOM   2957 C CA  . SER A 1 374 ? 7.065   -12.552 -17.953 1.00 40.99  ? 374  SER A CA  1 
ATOM   2958 C C   . SER A 1 374 ? 7.382   -12.970 -19.384 1.00 42.16  ? 374  SER A C   1 
ATOM   2959 O O   . SER A 1 374 ? 6.455   -13.191 -20.166 1.00 42.58  ? 374  SER A O   1 
ATOM   2960 C CB  . SER A 1 374 ? 7.324   -13.725 -16.986 1.00 40.53  ? 374  SER A CB  1 
ATOM   2961 O OG  . SER A 1 374 ? 6.360   -14.774 -17.149 1.00 41.19  ? 374  SER A OG  1 
ATOM   2962 N N   . SER A 1 375 ? 8.668   -13.080 -19.739 1.00 43.84  ? 375  SER A N   1 
ATOM   2963 C CA  . SER A 1 375 ? 9.058   -13.734 -21.006 1.00 45.06  ? 375  SER A CA  1 
ATOM   2964 C C   . SER A 1 375 ? 8.446   -15.145 -21.100 1.00 45.32  ? 375  SER A C   1 
ATOM   2965 O O   . SER A 1 375 ? 7.905   -15.553 -22.140 1.00 46.13  ? 375  SER A O   1 
ATOM   2966 C CB  . SER A 1 375 ? 10.584  -13.825 -21.124 1.00 45.84  ? 375  SER A CB  1 
ATOM   2967 O OG  . SER A 1 375 ? 11.195  -12.556 -20.920 1.00 47.64  ? 375  SER A OG  1 
ATOM   2968 N N   . SER A 1 376 ? 8.512   -15.865 -19.987 1.00 45.30  ? 376  SER A N   1 
ATOM   2969 C CA  . SER A 1 376 ? 7.973   -17.208 -19.870 1.00 45.47  ? 376  SER A CA  1 
ATOM   2970 C C   . SER A 1 376 ? 6.473   -17.257 -20.205 1.00 44.82  ? 376  SER A C   1 
ATOM   2971 O O   . SER A 1 376 ? 6.024   -18.109 -20.976 1.00 45.06  ? 376  SER A O   1 
ATOM   2972 C CB  . SER A 1 376 ? 8.222   -17.718 -18.442 1.00 45.69  ? 376  SER A CB  1 
ATOM   2973 O OG  . SER A 1 376 ? 7.848   -19.076 -18.284 1.00 47.45  ? 376  SER A OG  1 
ATOM   2974 N N   . LYS A 1 377 ? 5.702   -16.344 -19.614 1.00 43.48  ? 377  LYS A N   1 
ATOM   2975 C CA  . LYS A 1 377 ? 4.255   -16.294 -19.842 1.00 42.07  ? 377  LYS A CA  1 
ATOM   2976 C C   . LYS A 1 377 ? 3.801   -14.825 -20.065 1.00 39.39  ? 377  LYS A C   1 
ATOM   2977 O O   . LYS A 1 377 ? 3.407   -14.132 -19.115 1.00 38.44  ? 377  LYS A O   1 
ATOM   2978 C CB  . LYS A 1 377 ? 3.540   -16.938 -18.654 1.00 42.88  ? 377  LYS A CB  1 
ATOM   2979 C CG  . LYS A 1 377 ? 2.384   -17.867 -19.040 1.00 46.88  ? 377  LYS A CG  1 
ATOM   2980 C CD  . LYS A 1 377 ? 2.812   -19.341 -19.057 1.00 50.78  ? 377  LYS A CD  1 
ATOM   2981 C CE  . LYS A 1 377 ? 1.701   -20.223 -19.639 1.00 51.72  ? 377  LYS A CE  1 
ATOM   2982 N NZ  . LYS A 1 377 ? 1.908   -21.668 -19.335 1.00 52.68  ? 377  LYS A NZ  1 
ATOM   2983 N N   . PRO A 1 378 ? 3.948   -14.318 -21.304 1.00 37.54  ? 378  PRO A N   1 
ATOM   2984 C CA  . PRO A 1 378 ? 3.586   -12.913 -21.550 1.00 35.66  ? 378  PRO A CA  1 
ATOM   2985 C C   . PRO A 1 378 ? 2.078   -12.643 -21.443 1.00 33.37  ? 378  PRO A C   1 
ATOM   2986 O O   . PRO A 1 378 ? 1.284   -13.485 -21.824 1.00 33.60  ? 378  PRO A O   1 
ATOM   2987 C CB  . PRO A 1 378 ? 4.076   -12.652 -22.982 1.00 35.97  ? 378  PRO A CB  1 
ATOM   2988 C CG  . PRO A 1 378 ? 4.260   -13.991 -23.601 1.00 36.78  ? 378  PRO A CG  1 
ATOM   2989 C CD  . PRO A 1 378 ? 4.516   -14.971 -22.502 1.00 37.34  ? 378  PRO A CD  1 
ATOM   2990 N N   . TYR A 1 379 ? 1.701   -11.487 -20.902 1.00 30.67  ? 379  TYR A N   1 
ATOM   2991 C CA  . TYR A 1 379 ? 0.308   -11.055 -20.982 1.00 27.85  ? 379  TYR A CA  1 
ATOM   2992 C C   . TYR A 1 379 ? 0.324   -9.856  -21.896 1.00 26.13  ? 379  TYR A C   1 
ATOM   2993 O O   . TYR A 1 379 ? 0.689   -8.750  -21.489 1.00 25.86  ? 379  TYR A O   1 
ATOM   2994 C CB  . TYR A 1 379 ? -0.290  -10.743 -19.592 1.00 26.21  ? 379  TYR A CB  1 
ATOM   2995 C CG  . TYR A 1 379 ? -1.745  -10.287 -19.634 1.00 24.32  ? 379  TYR A CG  1 
ATOM   2996 C CD1 . TYR A 1 379 ? -2.734  -11.052 -20.289 1.00 21.21  ? 379  TYR A CD1 1 
ATOM   2997 C CD2 . TYR A 1 379 ? -2.135  -9.104  -19.007 1.00 24.07  ? 379  TYR A CD2 1 
ATOM   2998 C CE1 . TYR A 1 379 ? -4.104  -10.607 -20.323 1.00 23.02  ? 379  TYR A CE1 1 
ATOM   2999 C CE2 . TYR A 1 379 ? -3.473  -8.668  -19.029 1.00 22.88  ? 379  TYR A CE2 1 
ATOM   3000 C CZ  . TYR A 1 379 ? -4.441  -9.418  -19.683 1.00 23.21  ? 379  TYR A CZ  1 
ATOM   3001 O OH  . TYR A 1 379 ? -5.754  -8.951  -19.688 1.00 23.21  ? 379  TYR A OH  1 
ATOM   3002 N N   . GLY A 1 380 ? -0.025  -10.115 -23.155 1.00 25.11  ? 380  GLY A N   1 
ATOM   3003 C CA  . GLY A 1 380 ? -0.002  -9.134  -24.241 1.00 23.97  ? 380  GLY A CA  1 
ATOM   3004 C C   . GLY A 1 380 ? -0.568  -7.765  -23.938 1.00 23.11  ? 380  GLY A C   1 
ATOM   3005 O O   . GLY A 1 380 ? 0.081   -6.785  -24.204 1.00 22.10  ? 380  GLY A O   1 
ATOM   3006 N N   . PRO A 1 381 ? -1.821  -7.682  -23.405 1.00 22.79  ? 381  PRO A N   1 
ATOM   3007 C CA  . PRO A 1 381 ? -2.435  -6.359  -23.081 1.00 22.32  ? 381  PRO A CA  1 
ATOM   3008 C C   . PRO A 1 381 ? -1.601  -5.469  -22.155 1.00 22.28  ? 381  PRO A C   1 
ATOM   3009 O O   . PRO A 1 381 ? -1.492  -4.265  -22.382 1.00 22.50  ? 381  PRO A O   1 
ATOM   3010 C CB  . PRO A 1 381 ? -3.790  -6.750  -22.439 1.00 21.78  ? 381  PRO A CB  1 
ATOM   3011 C CG  . PRO A 1 381 ? -4.102  -8.050  -23.092 1.00 21.79  ? 381  PRO A CG  1 
ATOM   3012 C CD  . PRO A 1 381 ? -2.768  -8.786  -23.170 1.00 22.64  ? 381  PRO A CD  1 
ATOM   3013 N N   . TYR A 1 382 ? -0.977  -6.067  -21.151 1.00 23.33  ? 382  TYR A N   1 
ATOM   3014 C CA  . TYR A 1 382 ? -0.093  -5.335  -20.254 1.00 23.87  ? 382  TYR A CA  1 
ATOM   3015 C C   . TYR A 1 382 ? 1.202   -4.939  -20.948 1.00 24.20  ? 382  TYR A C   1 
ATOM   3016 O O   . TYR A 1 382 ? 1.670   -3.803  -20.795 1.00 23.65  ? 382  TYR A O   1 
ATOM   3017 C CB  . TYR A 1 382 ? 0.224   -6.165  -19.007 1.00 24.53  ? 382  TYR A CB  1 
ATOM   3018 C CG  . TYR A 1 382 ? 1.249   -5.515  -18.119 1.00 25.08  ? 382  TYR A CG  1 
ATOM   3019 C CD1 . TYR A 1 382 ? 0.913   -4.396  -17.366 1.00 24.83  ? 382  TYR A CD1 1 
ATOM   3020 C CD2 . TYR A 1 382 ? 2.566   -6.001  -18.043 1.00 27.32  ? 382  TYR A CD2 1 
ATOM   3021 C CE1 . TYR A 1 382 ? 1.833   -3.772  -16.547 1.00 26.84  ? 382  TYR A CE1 1 
ATOM   3022 C CE2 . TYR A 1 382 ? 3.514   -5.377  -17.219 1.00 27.24  ? 382  TYR A CE2 1 
ATOM   3023 C CZ  . TYR A 1 382 ? 3.128   -4.259  -16.467 1.00 27.65  ? 382  TYR A CZ  1 
ATOM   3024 O OH  . TYR A 1 382 ? 4.027   -3.593  -15.640 1.00 28.46  ? 382  TYR A OH  1 
ATOM   3025 N N   . ASP A 1 383 ? 1.808   -5.871  -21.686 1.00 24.53  ? 383  ASP A N   1 
ATOM   3026 C CA  . ASP A 1 383 ? 3.059   -5.541  -22.396 1.00 26.06  ? 383  ASP A CA  1 
ATOM   3027 C C   . ASP A 1 383 ? 2.874   -4.395  -23.381 1.00 25.92  ? 383  ASP A C   1 
ATOM   3028 O O   . ASP A 1 383 ? 3.690   -3.476  -23.412 1.00 25.51  ? 383  ASP A O   1 
ATOM   3029 C CB  . ASP A 1 383 ? 3.609   -6.763  -23.149 1.00 26.69  ? 383  ASP A CB  1 
ATOM   3030 C CG  . ASP A 1 383 ? 3.974   -7.920  -22.232 1.00 29.92  ? 383  ASP A CG  1 
ATOM   3031 O OD1 . ASP A 1 383 ? 4.034   -7.759  -20.988 1.00 31.15  ? 383  ASP A OD1 1 
ATOM   3032 O OD2 . ASP A 1 383 ? 4.209   -9.023  -22.784 1.00 35.00  ? 383  ASP A OD2 1 
ATOM   3033 N N   . ARG A 1 384 ? 1.805   -4.471  -24.192 1.00 24.68  ? 384  ARG A N   1 
ATOM   3034 C CA  . ARG A 1 384 ? 1.528   -3.471  -25.217 1.00 24.94  ? 384  ARG A CA  1 
ATOM   3035 C C   . ARG A 1 384 ? 1.181   -2.144  -24.574 1.00 24.39  ? 384  ARG A C   1 
ATOM   3036 O O   . ARG A 1 384 ? 1.645   -1.100  -25.031 1.00 24.61  ? 384  ARG A O   1 
ATOM   3037 C CB  . ARG A 1 384 ? 0.392   -3.927  -26.156 1.00 24.36  ? 384  ARG A CB  1 
ATOM   3038 C CG  . ARG A 1 384 ? 0.756   -5.046  -27.146 1.00 24.90  ? 384  ARG A CG  1 
ATOM   3039 C CD  . ARG A 1 384 ? -0.388  -5.417  -28.097 1.00 26.33  ? 384  ARG A CD  1 
ATOM   3040 N NE  . ARG A 1 384 ? -1.450  -6.167  -27.430 1.00 26.45  ? 384  ARG A NE  1 
ATOM   3041 C CZ  . ARG A 1 384 ? -1.487  -7.492  -27.351 1.00 26.63  ? 384  ARG A CZ  1 
ATOM   3042 N NH1 . ARG A 1 384 ? -0.522  -8.210  -27.899 1.00 28.37  ? 384  ARG A NH1 1 
ATOM   3043 N NH2 . ARG A 1 384 ? -2.480  -8.104  -26.724 1.00 25.71  ? 384  ARG A NH2 1 
ATOM   3044 N N   . GLY A 1 385 ? 0.389   -2.186  -23.494 1.00 24.02  ? 385  GLY A N   1 
ATOM   3045 C CA  . GLY A 1 385 ? 0.069   -0.982  -22.708 1.00 23.57  ? 385  GLY A CA  1 
ATOM   3046 C C   . GLY A 1 385 ? 1.288   -0.327  -22.060 1.00 24.59  ? 385  GLY A C   1 
ATOM   3047 O O   . GLY A 1 385 ? 1.415   0.888   -22.064 1.00 22.99  ? 385  GLY A O   1 
ATOM   3048 N N   . SER A 1 386 ? 2.198   -1.133  -21.516 1.00 25.49  ? 386  SER A N   1 
ATOM   3049 C CA  . SER A 1 386 ? 3.449   -0.586  -20.934 1.00 27.62  ? 386  SER A CA  1 
ATOM   3050 C C   . SER A 1 386 ? 4.369   0.007   -21.992 1.00 27.98  ? 386  SER A C   1 
ATOM   3051 O O   . SER A 1 386 ? 4.966   1.039   -21.777 1.00 28.75  ? 386  SER A O   1 
ATOM   3052 C CB  . SER A 1 386 ? 4.210   -1.659  -20.167 1.00 26.99  ? 386  SER A CB  1 
ATOM   3053 O OG  . SER A 1 386 ? 3.347   -2.236  -19.236 1.00 27.71  ? 386  SER A OG  1 
ATOM   3054 N N   . ASP A 1 387 ? 4.458   -0.658  -23.136 1.00 30.17  ? 387  ASP A N   1 
ATOM   3055 C CA  . ASP A 1 387 ? 5.202   -0.142  -24.286 1.00 30.98  ? 387  ASP A CA  1 
ATOM   3056 C C   . ASP A 1 387 ? 4.690   1.222   -24.722 1.00 31.23  ? 387  ASP A C   1 
ATOM   3057 O O   . ASP A 1 387 ? 5.476   2.096   -25.092 1.00 29.99  ? 387  ASP A O   1 
ATOM   3058 C CB  . ASP A 1 387 ? 5.111   -1.119  -25.449 1.00 31.97  ? 387  ASP A CB  1 
ATOM   3059 C CG  . ASP A 1 387 ? 6.006   -2.350  -25.260 1.00 36.03  ? 387  ASP A CG  1 
ATOM   3060 O OD1 . ASP A 1 387 ? 6.809   -2.417  -24.284 1.00 38.00  ? 387  ASP A OD1 1 
ATOM   3061 O OD2 . ASP A 1 387 ? 5.895   -3.258  -26.106 1.00 40.11  ? 387  ASP A OD2 1 
ATOM   3062 N N   . MET A 1 388 ? 3.367   1.414   -24.672 1.00 30.01  ? 388  MET A N   1 
ATOM   3063 C CA  . MET A 1 388 ? 2.780   2.694   -25.062 1.00 31.35  ? 388  MET A CA  1 
ATOM   3064 C C   . MET A 1 388 ? 2.705   3.738   -23.944 1.00 29.13  ? 388  MET A C   1 
ATOM   3065 O O   . MET A 1 388 ? 2.400   4.901   -24.192 1.00 29.35  ? 388  MET A O   1 
ATOM   3066 C CB  . MET A 1 388 ? 1.410   2.488   -25.712 1.00 30.42  ? 388  MET A CB  1 
ATOM   3067 C CG  . MET A 1 388 ? 1.490   1.703   -27.023 1.00 34.31  ? 388  MET A CG  1 
ATOM   3068 S SD  . MET A 1 388 ? -0.149  1.464   -27.719 1.00 37.12  ? 388  MET A SD  1 
ATOM   3069 C CE  . MET A 1 388 ? -0.504  3.155   -28.206 1.00 34.81  ? 388  MET A CE  1 
ATOM   3070 N N   . LYS A 1 389 ? 2.991   3.310   -22.723 1.00 27.76  ? 389  LYS A N   1 
ATOM   3071 C CA  . LYS A 1 389 ? 3.093   4.190   -21.558 1.00 27.10  ? 389  LYS A CA  1 
ATOM   3072 C C   . LYS A 1 389 ? 1.762   4.915   -21.243 1.00 24.93  ? 389  LYS A C   1 
ATOM   3073 O O   . LYS A 1 389 ? 1.759   6.100   -20.911 1.00 24.29  ? 389  LYS A O   1 
ATOM   3074 C CB  . LYS A 1 389 ? 4.288   5.169   -21.685 1.00 26.69  ? 389  LYS A CB  1 
ATOM   3075 C CG  . LYS A 1 389 ? 5.641   4.446   -21.801 1.00 28.47  ? 389  LYS A CG  1 
ATOM   3076 C CD  . LYS A 1 389 ? 6.782   5.427   -21.984 1.00 30.95  ? 389  LYS A CD  1 
ATOM   3077 C CE  . LYS A 1 389 ? 8.129   4.683   -22.131 1.00 37.02  ? 389  LYS A CE  1 
ATOM   3078 N NZ  . LYS A 1 389 ? 8.435   3.823   -20.912 1.00 40.29  ? 389  LYS A NZ  1 
ATOM   3079 N N   . ILE A 1 390 ? 0.671   4.152   -21.299 1.00 23.90  ? 390  ILE A N   1 
ATOM   3080 C CA  . ILE A 1 390 ? -0.691  4.695   -21.207 1.00 22.31  ? 390  ILE A CA  1 
ATOM   3081 C C   . ILE A 1 390 ? -1.385  4.417   -19.866 1.00 22.39  ? 390  ILE A C   1 
ATOM   3082 O O   . ILE A 1 390 ? -2.619  4.538   -19.757 1.00 20.42  ? 390  ILE A O   1 
ATOM   3083 C CB  . ILE A 1 390 ? -1.597  4.219   -22.403 1.00 23.64  ? 390  ILE A CB  1 
ATOM   3084 C CG1 . ILE A 1 390 ? -1.494  2.718   -22.693 1.00 24.14  ? 390  ILE A CG1 1 
ATOM   3085 C CG2 . ILE A 1 390 ? -1.260  5.012   -23.673 1.00 23.72  ? 390  ILE A CG2 1 
ATOM   3086 C CD1 . ILE A 1 390 ? -2.182  1.756   -21.693 1.00 24.96  ? 390  ILE A CD1 1 
ATOM   3087 N N   . TRP A 1 391 ? -0.613  4.041   -18.838 1.00 20.71  ? 391  TRP A N   1 
ATOM   3088 C CA  . TRP A 1 391 ? -1.223  3.800   -17.515 1.00 21.13  ? 391  TRP A CA  1 
ATOM   3089 C C   . TRP A 1 391 ? -1.417  5.069   -16.712 1.00 20.10  ? 391  TRP A C   1 
ATOM   3090 O O   . TRP A 1 391 ? -0.750  6.069   -16.954 1.00 21.02  ? 391  TRP A O   1 
ATOM   3091 C CB  . TRP A 1 391 ? -0.445  2.772   -16.680 1.00 21.50  ? 391  TRP A CB  1 
ATOM   3092 C CG  . TRP A 1 391 ? 0.007   1.544   -17.414 1.00 21.08  ? 391  TRP A CG  1 
ATOM   3093 C CD1 . TRP A 1 391 ? 1.312   1.114   -17.578 1.00 23.12  ? 391  TRP A CD1 1 
ATOM   3094 C CD2 . TRP A 1 391 ? -0.810  0.586   -18.071 1.00 22.58  ? 391  TRP A CD2 1 
ATOM   3095 N NE1 . TRP A 1 391 ? 1.335   -0.062  -18.289 1.00 23.28  ? 391  TRP A NE1 1 
ATOM   3096 C CE2 . TRP A 1 391 ? 0.046   -0.403  -18.607 1.00 21.33  ? 391  TRP A CE2 1 
ATOM   3097 C CE3 . TRP A 1 391 ? -2.191  0.456   -18.258 1.00 17.66  ? 391  TRP A CE3 1 
ATOM   3098 C CZ2 . TRP A 1 391 ? -0.437  -1.499  -19.320 1.00 23.26  ? 391  TRP A CZ2 1 
ATOM   3099 C CZ3 . TRP A 1 391 ? -2.664  -0.627  -18.969 1.00 23.14  ? 391  TRP A CZ3 1 
ATOM   3100 C CH2 . TRP A 1 391 ? -1.795  -1.593  -19.490 1.00 21.91  ? 391  TRP A CH2 1 
ATOM   3101 N N   . VAL A 1 392 ? -2.339  5.020   -15.751 1.00 19.79  ? 392  VAL A N   1 
ATOM   3102 C CA  . VAL A 1 392 ? -2.444  6.026   -14.717 1.00 18.91  ? 392  VAL A CA  1 
ATOM   3103 C C   . VAL A 1 392 ? -1.192  5.890   -13.841 1.00 20.67  ? 392  VAL A C   1 
ATOM   3104 O O   . VAL A 1 392 ? -0.848  4.773   -13.433 1.00 20.96  ? 392  VAL A O   1 
ATOM   3105 C CB  . VAL A 1 392 ? -3.671  5.778   -13.822 1.00 18.04  ? 392  VAL A CB  1 
ATOM   3106 C CG1 . VAL A 1 392 ? -3.687  6.778   -12.661 1.00 17.43  ? 392  VAL A CG1 1 
ATOM   3107 C CG2 . VAL A 1 392 ? -4.955  5.842   -14.657 1.00 16.12  ? 392  VAL A CG2 1 
ATOM   3108 N N   . ASN A 1 393 ? -0.528  7.016   -13.596 1.00 21.52  ? 393  ASN A N   1 
ATOM   3109 C CA  . ASN A 1 393 ? 0.682   7.064   -12.785 1.00 23.06  ? 393  ASN A CA  1 
ATOM   3110 C C   . ASN A 1 393 ? 0.403   7.488   -11.374 1.00 23.91  ? 393  ASN A C   1 
ATOM   3111 O O   . ASN A 1 393 ? -0.610  8.126   -11.077 1.00 21.73  ? 393  ASN A O   1 
ATOM   3112 C CB  . ASN A 1 393 ? 1.699   8.039   -13.395 1.00 22.91  ? 393  ASN A CB  1 
ATOM   3113 C CG  . ASN A 1 393 ? 2.191   7.581   -14.744 1.00 22.07  ? 393  ASN A CG  1 
ATOM   3114 O OD1 . ASN A 1 393 ? 2.132   6.395   -15.063 1.00 22.78  ? 393  ASN A OD1 1 
ATOM   3115 N ND2 . ASN A 1 393 ? 2.655   8.521   -15.545 1.00 23.36  ? 393  ASN A ND2 1 
ATOM   3116 N N   . SER A 1 394 ? 1.335   7.115   -10.505 1.00 25.93  ? 394  SER A N   1 
ATOM   3117 C CA  . SER A 1 394 ? 1.380   7.613   -9.152  1.00 27.91  ? 394  SER A CA  1 
ATOM   3118 C C   . SER A 1 394 ? 1.765   9.079   -9.140  1.00 28.33  ? 394  SER A C   1 
ATOM   3119 O O   . SER A 1 394 ? 2.125   9.651   -10.161 1.00 28.55  ? 394  SER A O   1 
ATOM   3120 C CB  . SER A 1 394 ? 2.389   6.795   -8.338  1.00 28.84  ? 394  SER A CB  1 
ATOM   3121 O OG  . SER A 1 394 ? 2.002   5.444   -8.320  1.00 34.02  ? 394  SER A OG  1 
ATOM   3122 N N   . SER A 1 395 ? 1.701   9.699   -7.971  1.00 29.11  ? 395  SER A N   1 
ATOM   3123 C CA  . SER A 1 395 ? 1.996   11.114  -7.859  1.00 30.46  ? 395  SER A CA  1 
ATOM   3124 C C   . SER A 1 395 ? 3.405   11.518  -8.333  1.00 30.93  ? 395  SER A C   1 
ATOM   3125 O O   . SER A 1 395 ? 3.617   12.677  -8.650  1.00 31.98  ? 395  SER A O   1 
ATOM   3126 C CB  . SER A 1 395 ? 1.738   11.604  -6.432  1.00 30.41  ? 395  SER A CB  1 
ATOM   3127 O OG  . SER A 1 395 ? 2.550   10.894  -5.514  1.00 31.72  ? 395  SER A OG  1 
ATOM   3128 N N   . ASP A 1 396 ? 4.353   10.589  -8.411  1.00 31.37  ? 396  ASP A N   1 
ATOM   3129 C CA  . ASP A 1 396 ? 5.677   10.941  -8.982  1.00 31.95  ? 396  ASP A CA  1 
ATOM   3130 C C   . ASP A 1 396 ? 5.585   11.286  -10.471 1.00 31.70  ? 396  ASP A C   1 
ATOM   3131 O O   . ASP A 1 396 ? 6.526   11.821  -11.063 1.00 31.52  ? 396  ASP A O   1 
ATOM   3132 C CB  . ASP A 1 396 ? 6.743   9.870   -8.707  1.00 32.48  ? 396  ASP A CB  1 
ATOM   3133 C CG  . ASP A 1 396 ? 6.455   8.538   -9.398  1.00 34.35  ? 396  ASP A CG  1 
ATOM   3134 O OD1 . ASP A 1 396 ? 5.574   8.475   -10.291 1.00 35.43  ? 396  ASP A OD1 1 
ATOM   3135 O OD2 . ASP A 1 396 ? 7.142   7.548   -9.055  1.00 36.12  ? 396  ASP A OD2 1 
ATOM   3136 N N   . GLY A 1 397 ? 4.430   10.991  -11.071 1.00 30.85  ? 397  GLY A N   1 
ATOM   3137 C CA  . GLY A 1 397 ? 4.191   11.321  -12.463 1.00 29.81  ? 397  GLY A CA  1 
ATOM   3138 C C   . GLY A 1 397 ? 4.806   10.345  -13.456 1.00 29.77  ? 397  GLY A C   1 
ATOM   3139 O O   . GLY A 1 397 ? 4.629   10.531  -14.658 1.00 29.83  ? 397  GLY A O   1 
ATOM   3140 N N   . VAL A 1 398 ? 5.515   9.309   -12.983 1.00 29.14  ? 398  VAL A N   1 
ATOM   3141 C CA  . VAL A 1 398 ? 6.239   8.381   -13.904 1.00 29.33  ? 398  VAL A CA  1 
ATOM   3142 C C   . VAL A 1 398 ? 6.068   6.889   -13.637 1.00 28.43  ? 398  VAL A C   1 
ATOM   3143 O O   . VAL A 1 398 ? 6.314   6.061   -14.512 1.00 29.24  ? 398  VAL A O   1 
ATOM   3144 C CB  . VAL A 1 398 ? 7.764   8.695   -14.027 1.00 30.55  ? 398  VAL A CB  1 
ATOM   3145 C CG1 . VAL A 1 398 ? 7.999   9.950   -14.862 1.00 31.89  ? 398  VAL A CG1 1 
ATOM   3146 C CG2 . VAL A 1 398 ? 8.419   8.784   -12.642 1.00 30.60  ? 398  VAL A CG2 1 
ATOM   3147 N N   . THR A 1 399 ? 5.624   6.539   -12.439 1.00 27.46  ? 399  THR A N   1 
ATOM   3148 C CA  . THR A 1 399 ? 5.449   5.158   -12.074 1.00 26.98  ? 399  THR A CA  1 
ATOM   3149 C C   . THR A 1 399 ? 3.974   4.793   -12.193 1.00 25.96  ? 399  THR A C   1 
ATOM   3150 O O   . THR A 1 399 ? 3.155   5.388   -11.512 1.00 24.01  ? 399  THR A O   1 
ATOM   3151 C CB  . THR A 1 399 ? 5.943   4.926   -10.634 1.00 27.80  ? 399  THR A CB  1 
ATOM   3152 O OG1 . THR A 1 399 ? 7.299   5.394   -10.545 1.00 29.10  ? 399  THR A OG1 1 
ATOM   3153 C CG2 . THR A 1 399 ? 5.890   3.461   -10.256 1.00 28.21  ? 399  THR A CG2 1 
ATOM   3154 N N   . PRO A 1 400 ? 3.650   3.818   -13.053 1.00 25.68  ? 400  PRO A N   1 
ATOM   3155 C CA  . PRO A 1 400 ? 2.261   3.371   -13.099 1.00 24.77  ? 400  PRO A CA  1 
ATOM   3156 C C   . PRO A 1 400 ? 1.729   2.951   -11.725 1.00 25.00  ? 400  PRO A C   1 
ATOM   3157 O O   . PRO A 1 400 ? 2.385   2.193   -10.967 1.00 23.95  ? 400  PRO A O   1 
ATOM   3158 C CB  . PRO A 1 400 ? 2.308   2.161   -14.041 1.00 25.57  ? 400  PRO A CB  1 
ATOM   3159 C CG  . PRO A 1 400 ? 3.452   2.379   -14.893 1.00 26.35  ? 400  PRO A CG  1 
ATOM   3160 C CD  . PRO A 1 400 ? 4.485   3.111   -14.040 1.00 24.46  ? 400  PRO A CD  1 
ATOM   3161 N N   . LEU A 1 401 ? 0.529   3.422   -11.405 1.00 23.33  ? 401  LEU A N   1 
ATOM   3162 C CA  . LEU A 1 401 ? -0.088  3.080   -10.139 1.00 23.81  ? 401  LEU A CA  1 
ATOM   3163 C C   . LEU A 1 401 ? -0.560  1.620   -10.095 1.00 23.68  ? 401  LEU A C   1 
ATOM   3164 O O   . LEU A 1 401 ? -1.238  1.151   -11.021 1.00 23.63  ? 401  LEU A O   1 
ATOM   3165 C CB  . LEU A 1 401 ? -1.254  4.057   -9.864  1.00 22.54  ? 401  LEU A CB  1 
ATOM   3166 C CG  . LEU A 1 401 ? -2.029  3.883   -8.547  1.00 25.48  ? 401  LEU A CG  1 
ATOM   3167 C CD1 . LEU A 1 401 ? -2.613  5.179   -8.101  1.00 24.96  ? 401  LEU A CD1 1 
ATOM   3168 C CD2 . LEU A 1 401 ? -3.151  2.825   -8.667  1.00 26.70  ? 401  LEU A CD2 1 
ATOM   3169 N N   . ILE A 1 402 ? -0.245  0.921   -8.997  1.00 23.09  ? 402  ILE A N   1 
ATOM   3170 C CA  . ILE A 1 402 ? -0.648  -0.470  -8.841  1.00 22.87  ? 402  ILE A CA  1 
ATOM   3171 C C   . ILE A 1 402 ? -1.815  -0.600  -7.867  1.00 22.41  ? 402  ILE A C   1 
ATOM   3172 O O   . ILE A 1 402 ? -1.751  -0.124  -6.734  1.00 22.38  ? 402  ILE A O   1 
ATOM   3173 C CB  . ILE A 1 402 ? 0.507   -1.392  -8.344  1.00 23.37  ? 402  ILE A CB  1 
ATOM   3174 C CG1 . ILE A 1 402 ? 1.811   -1.213  -9.151  1.00 24.59  ? 402  ILE A CG1 1 
ATOM   3175 C CG2 . ILE A 1 402 ? 0.069   -2.844  -8.331  1.00 22.33  ? 402  ILE A CG2 1 
ATOM   3176 C CD1 . ILE A 1 402 ? 1.661   -1.408  -10.619 1.00 28.51  ? 402  ILE A CD1 1 
ATOM   3177 N N   . GLY A 1 403 ? -2.891  -1.226  -8.324  1.00 21.76  ? 403  GLY A N   1 
ATOM   3178 C CA  . GLY A 1 403 ? -4.036  -1.482  -7.455  1.00 20.86  ? 403  GLY A CA  1 
ATOM   3179 C C   . GLY A 1 403 ? -4.392  -2.948  -7.532  1.00 21.29  ? 403  GLY A C   1 
ATOM   3180 O O   . GLY A 1 403 ? -3.595  -3.758  -7.963  1.00 21.78  ? 403  GLY A O   1 
ATOM   3181 N N   . GLU A 1 404 ? -5.599  -3.322  -7.131  1.00 20.93  ? 404  GLU A N   1 
ATOM   3182 C CA  . GLU A 1 404 ? -5.966  -4.711  -7.189  1.00 22.21  ? 404  GLU A CA  1 
ATOM   3183 C C   . GLU A 1 404 ? -7.404  -4.830  -7.652  1.00 21.97  ? 404  GLU A C   1 
ATOM   3184 O O   . GLU A 1 404 ? -8.273  -4.195  -7.083  1.00 22.16  ? 404  GLU A O   1 
ATOM   3185 C CB  . GLU A 1 404 ? -5.834  -5.325  -5.789  1.00 23.53  ? 404  GLU A CB  1 
ATOM   3186 C CG  . GLU A 1 404 ? -5.978  -6.822  -5.764  1.00 29.25  ? 404  GLU A CG  1 
ATOM   3187 C CD  . GLU A 1 404 ? -6.336  -7.339  -4.374  1.00 37.84  ? 404  GLU A CD  1 
ATOM   3188 O OE1 . GLU A 1 404 ? -5.811  -6.753  -3.391  1.00 39.54  ? 404  GLU A OE1 1 
ATOM   3189 O OE2 . GLU A 1 404 ? -7.145  -8.306  -4.274  1.00 39.01  ? 404  GLU A OE2 1 
ATOM   3190 N N   . VAL A 1 405 ? -7.651  -5.630  -8.679  1.00 21.48  ? 405  VAL A N   1 
ATOM   3191 C CA  . VAL A 1 405 ? -9.043  -5.920  -9.079  1.00 21.35  ? 405  VAL A CA  1 
ATOM   3192 C C   . VAL A 1 405 ? -9.173  -7.421  -9.321  1.00 21.64  ? 405  VAL A C   1 
ATOM   3193 O O   . VAL A 1 405 ? -8.523  -8.190  -8.630  1.00 22.38  ? 405  VAL A O   1 
ATOM   3194 C CB  . VAL A 1 405 ? -9.591  -4.973  -10.220 1.00 20.33  ? 405  VAL A CB  1 
ATOM   3195 C CG1 . VAL A 1 405 ? -11.136 -4.920  -10.155 1.00 20.19  ? 405  VAL A CG1 1 
ATOM   3196 C CG2 . VAL A 1 405 ? -9.076  -3.554  -10.005 1.00 19.40  ? 405  VAL A CG2 1 
ATOM   3197 N N   . TRP A 1 406 ? -10.039 -7.850  -10.228 1.00 22.02  ? 406  TRP A N   1 
ATOM   3198 C CA  . TRP A 1 406 ? -10.361 -9.266  -10.419 1.00 22.28  ? 406  TRP A CA  1 
ATOM   3199 C C   . TRP A 1 406 ? -9.166  -10.191 -10.694 1.00 22.77  ? 406  TRP A C   1 
ATOM   3200 O O   . TRP A 1 406 ? -9.086  -11.268 -10.109 1.00 23.02  ? 406  TRP A O   1 
ATOM   3201 C CB  . TRP A 1 406 ? -11.401 -9.418  -11.528 1.00 21.59  ? 406  TRP A CB  1 
ATOM   3202 C CG  . TRP A 1 406 ? -12.731 -8.762  -11.192 1.00 19.72  ? 406  TRP A CG  1 
ATOM   3203 C CD1 . TRP A 1 406 ? -13.357 -7.791  -11.903 1.00 21.32  ? 406  TRP A CD1 1 
ATOM   3204 C CD2 . TRP A 1 406 ? -13.580 -9.050  -10.069 1.00 22.83  ? 406  TRP A CD2 1 
ATOM   3205 N NE1 . TRP A 1 406 ? -14.566 -7.453  -11.304 1.00 20.31  ? 406  TRP A NE1 1 
ATOM   3206 C CE2 . TRP A 1 406 ? -14.729 -8.218  -10.181 1.00 19.06  ? 406  TRP A CE2 1 
ATOM   3207 C CE3 . TRP A 1 406 ? -13.500 -9.947  -8.994  1.00 21.56  ? 406  TRP A CE3 1 
ATOM   3208 C CZ2 . TRP A 1 406 ? -15.756 -8.223  -9.232  1.00 23.03  ? 406  TRP A CZ2 1 
ATOM   3209 C CZ3 . TRP A 1 406 ? -14.522 -9.962  -8.053  1.00 22.96  ? 406  TRP A CZ3 1 
ATOM   3210 C CH2 . TRP A 1 406 ? -15.651 -9.107  -8.185  1.00 22.54  ? 406  TRP A CH2 1 
ATOM   3211 N N   . PRO A 1 407 ? -8.247  -9.790  -11.579 1.00 23.56  ? 407  PRO A N   1 
ATOM   3212 C CA  . PRO A 1 407 ? -7.138  -10.721 -11.788 1.00 24.65  ? 407  PRO A CA  1 
ATOM   3213 C C   . PRO A 1 407 ? -5.997  -10.698 -10.725 1.00 26.24  ? 407  PRO A C   1 
ATOM   3214 O O   . PRO A 1 407 ? -4.982  -11.396 -10.900 1.00 27.48  ? 407  PRO A O   1 
ATOM   3215 C CB  . PRO A 1 407 ? -6.614  -10.313 -13.169 1.00 24.22  ? 407  PRO A CB  1 
ATOM   3216 C CG  . PRO A 1 407 ? -6.868  -8.874  -13.263 1.00 22.93  ? 407  PRO A CG  1 
ATOM   3217 C CD  . PRO A 1 407 ? -8.142  -8.606  -12.453 1.00 24.40  ? 407  PRO A CD  1 
ATOM   3218 N N   . GLY A 1 408 ? -6.158  -9.933  -9.651  1.00 25.76  ? 408  GLY A N   1 
ATOM   3219 C CA  . GLY A 1 408 ? -5.031  -9.637  -8.745  1.00 25.25  ? 408  GLY A CA  1 
ATOM   3220 C C   . GLY A 1 408 ? -4.446  -8.256  -8.991  1.00 24.74  ? 408  GLY A C   1 
ATOM   3221 O O   . GLY A 1 408 ? -5.167  -7.352  -9.377  1.00 24.47  ? 408  GLY A O   1 
ATOM   3222 N N   . GLN A 1 409 ? -3.129  -8.070  -8.795  1.00 23.87  ? 409  GLN A N   1 
ATOM   3223 C CA  . GLN A 1 409 ? -2.529  -6.744  -8.992  1.00 23.56  ? 409  GLN A CA  1 
ATOM   3224 C C   . GLN A 1 409 ? -2.708  -6.261  -10.402 1.00 22.23  ? 409  GLN A C   1 
ATOM   3225 O O   . GLN A 1 409 ? -2.581  -7.041  -11.363 1.00 22.35  ? 409  GLN A O   1 
ATOM   3226 C CB  . GLN A 1 409 ? -1.033  -6.721  -8.682  1.00 23.92  ? 409  GLN A CB  1 
ATOM   3227 C CG  . GLN A 1 409 ? -0.714  -6.378  -7.270  1.00 29.54  ? 409  GLN A CG  1 
ATOM   3228 C CD  . GLN A 1 409 ? 0.791   -6.299  -7.014  1.00 33.93  ? 409  GLN A CD  1 
ATOM   3229 O OE1 . GLN A 1 409 ? 1.611   -6.029  -7.921  1.00 36.35  ? 409  GLN A OE1 1 
ATOM   3230 N NE2 . GLN A 1 409 ? 1.155   -6.521  -5.771  1.00 38.51  ? 409  GLN A NE2 1 
ATOM   3231 N N   . THR A 1 410 ? -2.976  -4.964  -10.536 1.00 20.86  ? 410  THR A N   1 
ATOM   3232 C CA  . THR A 1 410 ? -3.297  -4.415  -11.836 1.00 20.29  ? 410  THR A CA  1 
ATOM   3233 C C   . THR A 1 410 ? -2.789  -3.017  -11.954 1.00 19.79  ? 410  THR A C   1 
ATOM   3234 O O   . THR A 1 410 ? -2.608  -2.333  -10.955 1.00 21.56  ? 410  THR A O   1 
ATOM   3235 C CB  . THR A 1 410 ? -4.846  -4.316  -12.023 1.00 19.89  ? 410  THR A CB  1 
ATOM   3236 O OG1 . THR A 1 410 ? -5.395  -3.674  -10.869 1.00 20.87  ? 410  THR A OG1 1 
ATOM   3237 C CG2 . THR A 1 410 ? -5.431  -5.684  -12.161 1.00 21.20  ? 410  THR A CG2 1 
ATOM   3238 N N   . VAL A 1 411 ? -2.566  -2.599  -13.193 1.00 19.79  ? 411  VAL A N   1 
ATOM   3239 C CA  . VAL A 1 411 ? -2.406  -1.192  -13.540 1.00 18.68  ? 411  VAL A CA  1 
ATOM   3240 C C   . VAL A 1 411 ? -3.736  -0.715  -14.184 1.00 18.99  ? 411  VAL A C   1 
ATOM   3241 O O   . VAL A 1 411 ? -4.588  -1.520  -14.519 1.00 20.22  ? 411  VAL A O   1 
ATOM   3242 C CB  . VAL A 1 411 ? -1.280  -0.986  -14.508 1.00 18.76  ? 411  VAL A CB  1 
ATOM   3243 C CG1 . VAL A 1 411 ? 0.083   -1.192  -13.776 1.00 16.81  ? 411  VAL A CG1 1 
ATOM   3244 C CG2 . VAL A 1 411 ? -1.423  -1.948  -15.671 1.00 17.84  ? 411  VAL A CG2 1 
ATOM   3245 N N   . PHE A 1 412 ? -3.870  0.579   -14.368 1.00 19.40  ? 412  PHE A N   1 
ATOM   3246 C CA  . PHE A 1 412 ? -5.142  1.189   -14.800 1.00 19.99  ? 412  PHE A CA  1 
ATOM   3247 C C   . PHE A 1 412 ? -4.897  2.042   -16.046 1.00 19.57  ? 412  PHE A C   1 
ATOM   3248 O O   . PHE A 1 412 ? -4.016  2.897   -16.051 1.00 20.18  ? 412  PHE A O   1 
ATOM   3249 C CB  . PHE A 1 412 ? -5.692  2.049   -13.646 1.00 19.29  ? 412  PHE A CB  1 
ATOM   3250 C CG  . PHE A 1 412 ? -6.097  1.243   -12.450 1.00 20.16  ? 412  PHE A CG  1 
ATOM   3251 C CD1 . PHE A 1 412 ? -7.393  0.740   -12.354 1.00 18.14  ? 412  PHE A CD1 1 
ATOM   3252 C CD2 . PHE A 1 412 ? -5.171  0.954   -11.437 1.00 20.75  ? 412  PHE A CD2 1 
ATOM   3253 C CE1 . PHE A 1 412 ? -7.789  -0.032  -11.257 1.00 20.72  ? 412  PHE A CE1 1 
ATOM   3254 C CE2 . PHE A 1 412 ? -5.543  0.179   -10.334 1.00 21.25  ? 412  PHE A CE2 1 
ATOM   3255 C CZ  . PHE A 1 412 ? -6.867  -0.326  -10.247 1.00 21.98  ? 412  PHE A CZ  1 
ATOM   3256 N N   . PRO A 1 413 ? -5.665  1.806   -17.116 1.00 19.62  ? 413  PRO A N   1 
ATOM   3257 C CA  . PRO A 1 413 ? -5.463  2.626   -18.282 1.00 19.48  ? 413  PRO A CA  1 
ATOM   3258 C C   . PRO A 1 413 ? -5.859  4.075   -18.052 1.00 19.94  ? 413  PRO A C   1 
ATOM   3259 O O   . PRO A 1 413 ? -6.838  4.376   -17.338 1.00 21.16  ? 413  PRO A O   1 
ATOM   3260 C CB  . PRO A 1 413 ? -6.369  1.979   -19.343 1.00 19.77  ? 413  PRO A CB  1 
ATOM   3261 C CG  . PRO A 1 413 ? -6.669  0.632   -18.831 1.00 19.86  ? 413  PRO A CG  1 
ATOM   3262 C CD  . PRO A 1 413 ? -6.693  0.782   -17.333 1.00 18.57  ? 413  PRO A CD  1 
ATOM   3263 N N   . ASP A 1 414 ? -5.131  4.970   -18.689 1.00 19.00  ? 414  ASP A N   1 
ATOM   3264 C CA  . ASP A 1 414 ? -5.464  6.388   -18.608 1.00 20.13  ? 414  ASP A CA  1 
ATOM   3265 C C   . ASP A 1 414 ? -6.249  6.733   -19.868 1.00 19.83  ? 414  ASP A C   1 
ATOM   3266 O O   . ASP A 1 414 ? -5.680  7.068   -20.911 1.00 19.75  ? 414  ASP A O   1 
ATOM   3267 C CB  . ASP A 1 414 ? -4.192  7.277   -18.498 1.00 19.89  ? 414  ASP A CB  1 
ATOM   3268 C CG  . ASP A 1 414 ? -4.508  8.779   -18.674 1.00 22.63  ? 414  ASP A CG  1 
ATOM   3269 O OD1 . ASP A 1 414 ? -5.709  9.186   -18.581 1.00 21.16  ? 414  ASP A OD1 1 
ATOM   3270 O OD2 . ASP A 1 414 ? -3.584  9.564   -18.947 1.00 21.99  ? 414  ASP A OD2 1 
ATOM   3271 N N   . TYR A 1 415 ? -7.570  6.645   -19.795 1.00 20.86  ? 415  TYR A N   1 
ATOM   3272 C CA  . TYR A 1 415 ? -8.348  6.806   -21.019 1.00 20.28  ? 415  TYR A CA  1 
ATOM   3273 C C   . TYR A 1 415 ? -8.419  8.247   -21.466 1.00 21.55  ? 415  TYR A C   1 
ATOM   3274 O O   . TYR A 1 415 ? -8.924  8.524   -22.565 1.00 21.22  ? 415  TYR A O   1 
ATOM   3275 C CB  . TYR A 1 415 ? -9.730  6.200   -20.835 1.00 20.65  ? 415  TYR A CB  1 
ATOM   3276 C CG  . TYR A 1 415 ? -9.740  4.695   -20.651 1.00 20.13  ? 415  TYR A CG  1 
ATOM   3277 C CD1 . TYR A 1 415 ? -9.570  3.837   -21.733 1.00 19.71  ? 415  TYR A CD1 1 
ATOM   3278 C CD2 . TYR A 1 415 ? -9.968  4.132   -19.395 1.00 18.07  ? 415  TYR A CD2 1 
ATOM   3279 C CE1 . TYR A 1 415 ? -9.629  2.455   -21.578 1.00 18.96  ? 415  TYR A CE1 1 
ATOM   3280 C CE2 . TYR A 1 415 ? -10.014 2.757   -19.221 1.00 18.74  ? 415  TYR A CE2 1 
ATOM   3281 C CZ  . TYR A 1 415 ? -9.835  1.926   -20.320 1.00 19.45  ? 415  TYR A CZ  1 
ATOM   3282 O OH  . TYR A 1 415 ? -9.888  0.574   -20.130 1.00 19.37  ? 415  TYR A OH  1 
ATOM   3283 N N   . THR A 1 416 ? -7.895  9.179   -20.654 1.00 20.86  ? 416  THR A N   1 
ATOM   3284 C CA  . THR A 1 416 ? -7.867  10.591  -21.059 1.00 21.97  ? 416  THR A CA  1 
ATOM   3285 C C   . THR A 1 416 ? -6.719  10.890  -22.026 1.00 23.48  ? 416  THR A C   1 
ATOM   3286 O O   . THR A 1 416 ? -6.700  11.938  -22.664 1.00 24.00  ? 416  THR A O   1 
ATOM   3287 C CB  . THR A 1 416 ? -7.870  11.563  -19.863 1.00 21.69  ? 416  THR A CB  1 
ATOM   3288 O OG1 . THR A 1 416 ? -6.581  11.599  -19.233 1.00 22.48  ? 416  THR A OG1 1 
ATOM   3289 C CG2 . THR A 1 416 ? -8.929  11.170  -18.853 1.00 21.11  ? 416  THR A CG2 1 
ATOM   3290 N N   . ASN A 1 417 ? -5.762  9.976   -22.110 1.00 24.11  ? 417  ASN A N   1 
ATOM   3291 C CA  . ASN A 1 417 ? -4.669  10.070  -23.066 1.00 25.75  ? 417  ASN A CA  1 
ATOM   3292 C C   . ASN A 1 417 ? -5.188  9.529   -24.407 1.00 27.17  ? 417  ASN A C   1 
ATOM   3293 O O   . ASN A 1 417 ? -5.609  8.384   -24.474 1.00 26.81  ? 417  ASN A O   1 
ATOM   3294 C CB  . ASN A 1 417 ? -3.515  9.225   -22.527 1.00 25.17  ? 417  ASN A CB  1 
ATOM   3295 C CG  . ASN A 1 417 ? -2.284  9.230   -23.428 1.00 27.65  ? 417  ASN A CG  1 
ATOM   3296 O OD1 . ASN A 1 417 ? -2.365  9.540   -24.607 1.00 28.17  ? 417  ASN A OD1 1 
ATOM   3297 N ND2 . ASN A 1 417 ? -1.136  8.870   -22.856 1.00 27.75  ? 417  ASN A ND2 1 
ATOM   3298 N N   . PRO A 1 418 ? -5.187  10.359  -25.483 1.00 29.35  ? 418  PRO A N   1 
ATOM   3299 C CA  . PRO A 1 418 ? -5.608  9.884   -26.831 1.00 30.22  ? 418  PRO A CA  1 
ATOM   3300 C C   . PRO A 1 418 ? -4.924  8.587   -27.284 1.00 30.05  ? 418  PRO A C   1 
ATOM   3301 O O   . PRO A 1 418 ? -5.560  7.751   -27.934 1.00 29.32  ? 418  PRO A O   1 
ATOM   3302 C CB  . PRO A 1 418 ? -5.215  11.041  -27.773 1.00 31.07  ? 418  PRO A CB  1 
ATOM   3303 C CG  . PRO A 1 418 ? -4.429  12.019  -26.927 1.00 30.89  ? 418  PRO A CG  1 
ATOM   3304 C CD  . PRO A 1 418 ? -4.818  11.785  -25.496 1.00 29.87  ? 418  PRO A CD  1 
ATOM   3305 N N   . ASN A 1 419 ? -3.660  8.409   -26.905 1.00 29.66  ? 419  ASN A N   1 
ATOM   3306 C CA  . ASN A 1 419 ? -2.913  7.202   -27.248 1.00 29.94  ? 419  ASN A CA  1 
ATOM   3307 C C   . ASN A 1 419 ? -3.436  5.969   -26.535 1.00 28.16  ? 419  ASN A C   1 
ATOM   3308 O O   . ASN A 1 419 ? -3.220  4.840   -26.980 1.00 27.01  ? 419  ASN A O   1 
ATOM   3309 C CB  . ASN A 1 419 ? -1.431  7.366   -26.893 1.00 31.09  ? 419  ASN A CB  1 
ATOM   3310 C CG  . ASN A 1 419 ? -0.707  8.305   -27.844 1.00 36.28  ? 419  ASN A CG  1 
ATOM   3311 O OD1 . ASN A 1 419 ? -1.095  8.444   -29.013 1.00 42.47  ? 419  ASN A OD1 1 
ATOM   3312 N ND2 . ASN A 1 419 ? 0.346   8.960   -27.353 1.00 39.96  ? 419  ASN A ND2 1 
ATOM   3313 N N   . CYS A 1 420 ? -4.063  6.182   -25.384 1.00 26.79  ? 420  CYS A N   1 
ATOM   3314 C CA  . CYS A 1 420 ? -4.687  5.083   -24.681 1.00 25.93  ? 420  CYS A CA  1 
ATOM   3315 C C   . CYS A 1 420 ? -5.826  4.499   -25.518 1.00 25.80  ? 420  CYS A C   1 
ATOM   3316 O O   . CYS A 1 420 ? -6.028  3.295   -25.547 1.00 25.42  ? 420  CYS A O   1 
ATOM   3317 C CB  . CYS A 1 420 ? -5.179  5.515   -23.306 1.00 26.05  ? 420  CYS A CB  1 
ATOM   3318 S SG  . CYS A 1 420 ? -5.798  4.118   -22.302 1.00 26.51  ? 420  CYS A SG  1 
ATOM   3319 N N   . ALA A 1 421 ? -6.561  5.355   -26.216 1.00 25.79  ? 421  ALA A N   1 
ATOM   3320 C CA  . ALA A 1 421 ? -7.614  4.869   -27.093 1.00 25.41  ? 421  ALA A CA  1 
ATOM   3321 C C   . ALA A 1 421 ? -7.027  4.062   -28.249 1.00 25.33  ? 421  ALA A C   1 
ATOM   3322 O O   . ALA A 1 421 ? -7.622  3.105   -28.702 1.00 26.18  ? 421  ALA A O   1 
ATOM   3323 C CB  . ALA A 1 421 ? -8.439  6.011   -27.594 1.00 25.93  ? 421  ALA A CB  1 
ATOM   3324 N N   . VAL A 1 422 ? -5.834  4.412   -28.716 1.00 25.05  ? 422  VAL A N   1 
ATOM   3325 C CA  . VAL A 1 422 ? -5.190  3.581   -29.745 1.00 24.06  ? 422  VAL A CA  1 
ATOM   3326 C C   . VAL A 1 422 ? -4.841  2.188   -29.190 1.00 22.83  ? 422  VAL A C   1 
ATOM   3327 O O   . VAL A 1 422 ? -5.098  1.178   -29.828 1.00 23.16  ? 422  VAL A O   1 
ATOM   3328 C CB  . VAL A 1 422 ? -3.924  4.262   -30.305 1.00 24.39  ? 422  VAL A CB  1 
ATOM   3329 C CG1 . VAL A 1 422 ? -3.176  3.307   -31.217 1.00 25.18  ? 422  VAL A CG1 1 
ATOM   3330 C CG2 . VAL A 1 422 ? -4.291  5.598   -30.987 1.00 24.39  ? 422  VAL A CG2 1 
ATOM   3331 N N   . TRP A 1 423 ? -4.269  2.140   -27.991 1.00 21.81  ? 423  TRP A N   1 
ATOM   3332 C CA  . TRP A 1 423 ? -3.962  0.869   -27.340 1.00 21.02  ? 423  TRP A CA  1 
ATOM   3333 C C   . TRP A 1 423 ? -5.236  0.021   -27.146 1.00 20.06  ? 423  TRP A C   1 
ATOM   3334 O O   . TRP A 1 423 ? -5.241  -1.168  -27.444 1.00 18.90  ? 423  TRP A O   1 
ATOM   3335 C CB  . TRP A 1 423 ? -3.264  1.123   -25.989 1.00 21.78  ? 423  TRP A CB  1 
ATOM   3336 C CG  . TRP A 1 423 ? -3.271  -0.057  -25.069 1.00 22.38  ? 423  TRP A CG  1 
ATOM   3337 C CD1 . TRP A 1 423 ? -2.441  -1.139  -25.101 1.00 21.96  ? 423  TRP A CD1 1 
ATOM   3338 C CD2 . TRP A 1 423 ? -4.191  -0.278  -23.986 1.00 22.44  ? 423  TRP A CD2 1 
ATOM   3339 N NE1 . TRP A 1 423 ? -2.774  -2.023  -24.080 1.00 23.54  ? 423  TRP A NE1 1 
ATOM   3340 C CE2 . TRP A 1 423 ? -3.844  -1.510  -23.386 1.00 22.66  ? 423  TRP A CE2 1 
ATOM   3341 C CE3 . TRP A 1 423 ? -5.257  0.472   -23.448 1.00 21.74  ? 423  TRP A CE3 1 
ATOM   3342 C CZ2 . TRP A 1 423 ? -4.540  -2.033  -22.294 1.00 22.99  ? 423  TRP A CZ2 1 
ATOM   3343 C CZ3 . TRP A 1 423 ? -5.949  -0.044  -22.353 1.00 21.64  ? 423  TRP A CZ3 1 
ATOM   3344 C CH2 . TRP A 1 423 ? -5.583  -1.290  -21.788 1.00 22.00  ? 423  TRP A CH2 1 
ATOM   3345 N N   . TRP A 1 424 ? -6.296  0.662   -26.645 1.00 19.17  ? 424  TRP A N   1 
ATOM   3346 C CA  . TRP A 1 424 ? -7.570  -0.010  -26.325 1.00 19.28  ? 424  TRP A CA  1 
ATOM   3347 C C   . TRP A 1 424 ? -8.158  -0.579  -27.595 1.00 18.39  ? 424  TRP A C   1 
ATOM   3348 O O   . TRP A 1 424 ? -8.582  -1.704  -27.622 1.00 19.47  ? 424  TRP A O   1 
ATOM   3349 C CB  . TRP A 1 424 ? -8.496  1.044   -25.702 1.00 18.45  ? 424  TRP A CB  1 
ATOM   3350 C CG  . TRP A 1 424 ? -9.780  0.620   -25.017 1.00 19.90  ? 424  TRP A CG  1 
ATOM   3351 C CD1 . TRP A 1 424 ? -11.018 1.157   -25.258 1.00 16.90  ? 424  TRP A CD1 1 
ATOM   3352 C CD2 . TRP A 1 424 ? -9.944  -0.293  -23.922 1.00 19.18  ? 424  TRP A CD2 1 
ATOM   3353 N NE1 . TRP A 1 424 ? -11.951 0.602   -24.416 1.00 18.23  ? 424  TRP A NE1 1 
ATOM   3354 C CE2 . TRP A 1 424 ? -11.332 -0.290  -23.584 1.00 20.69  ? 424  TRP A CE2 1 
ATOM   3355 C CE3 . TRP A 1 424 ? -9.077  -1.134  -23.207 1.00 17.67  ? 424  TRP A CE3 1 
ATOM   3356 C CZ2 . TRP A 1 424 ? -11.861 -1.094  -22.568 1.00 17.88  ? 424  TRP A CZ2 1 
ATOM   3357 C CZ3 . TRP A 1 424 ? -9.599  -1.924  -22.183 1.00 18.26  ? 424  TRP A CZ3 1 
ATOM   3358 C CH2 . TRP A 1 424 ? -10.987 -1.892  -21.867 1.00 19.78  ? 424  TRP A CH2 1 
ATOM   3359 N N   . THR A 1 425 ? -8.189  0.214   -28.648 1.00 20.18  ? 425  THR A N   1 
ATOM   3360 C CA  . THR A 1 425 ? -8.734  -0.239  -29.925 1.00 21.34  ? 425  THR A CA  1 
ATOM   3361 C C   . THR A 1 425 ? -7.990  -1.477  -30.429 1.00 22.07  ? 425  THR A C   1 
ATOM   3362 O O   . THR A 1 425 ? -8.610  -2.451  -30.810 1.00 21.34  ? 425  THR A O   1 
ATOM   3363 C CB  . THR A 1 425 ? -8.646  0.889   -30.996 1.00 21.69  ? 425  THR A CB  1 
ATOM   3364 O OG1 . THR A 1 425 ? -9.345  2.049   -30.528 1.00 21.95  ? 425  THR A OG1 1 
ATOM   3365 C CG2 . THR A 1 425 ? -9.194  0.435   -32.354 1.00 23.92  ? 425  THR A CG2 1 
ATOM   3366 N N   . LYS A 1 426 ? -6.651  -1.448  -30.394 1.00 22.88  ? 426  LYS A N   1 
ATOM   3367 C CA  . LYS A 1 426 ? -5.871  -2.590  -30.862 1.00 23.35  ? 426  LYS A CA  1 
ATOM   3368 C C   . LYS A 1 426 ? -6.153  -3.823  -30.023 1.00 22.04  ? 426  LYS A C   1 
ATOM   3369 O O   . LYS A 1 426 ? -6.233  -4.919  -30.571 1.00 22.45  ? 426  LYS A O   1 
ATOM   3370 C CB  . LYS A 1 426 ? -4.375  -2.268  -30.908 1.00 24.01  ? 426  LYS A CB  1 
ATOM   3371 C CG  . LYS A 1 426 ? -3.477  -3.396  -31.479 1.00 29.92  ? 426  LYS A CG  1 
ATOM   3372 C CD  . LYS A 1 426 ? -3.876  -3.788  -32.905 1.00 36.95  ? 426  LYS A CD  1 
ATOM   3373 C CE  . LYS A 1 426 ? -2.669  -3.920  -33.832 1.00 41.12  ? 426  LYS A CE  1 
ATOM   3374 N NZ  . LYS A 1 426 ? -3.121  -3.790  -35.264 1.00 42.02  ? 426  LYS A NZ  1 
ATOM   3375 N N   . GLU A 1 427 ? -6.359  -3.666  -28.709 1.00 22.12  ? 427  GLU A N   1 
ATOM   3376 C CA  . GLU A 1 427 ? -6.663  -4.837  -27.877 1.00 21.37  ? 427  GLU A CA  1 
ATOM   3377 C C   . GLU A 1 427 ? -7.999  -5.449  -28.285 1.00 20.89  ? 427  GLU A C   1 
ATOM   3378 O O   . GLU A 1 427 ? -8.146  -6.664  -28.335 1.00 20.17  ? 427  GLU A O   1 
ATOM   3379 C CB  . GLU A 1 427 ? -6.680  -4.535  -26.371 1.00 22.21  ? 427  GLU A CB  1 
ATOM   3380 C CG  . GLU A 1 427 ? -5.359  -4.139  -25.743 1.00 22.92  ? 427  GLU A CG  1 
ATOM   3381 C CD  . GLU A 1 427 ? -4.218  -5.142  -25.969 1.00 25.23  ? 427  GLU A CD  1 
ATOM   3382 O OE1 . GLU A 1 427 ? -4.458  -6.369  -26.058 1.00 27.69  ? 427  GLU A OE1 1 
ATOM   3383 O OE2 . GLU A 1 427 ? -3.065  -4.673  -26.070 1.00 27.94  ? 427  GLU A OE2 1 
ATOM   3384 N N   . PHE A 1 428 ? -8.984  -4.604  -28.580 1.00 20.95  ? 428  PHE A N   1 
ATOM   3385 C CA  . PHE A 1 428 ? -10.277 -5.138  -29.008 1.00 20.92  ? 428  PHE A CA  1 
ATOM   3386 C C   . PHE A 1 428 ? -10.182 -5.767  -30.385 1.00 21.13  ? 428  PHE A C   1 
ATOM   3387 O O   . PHE A 1 428 ? -10.736 -6.786  -30.576 1.00 22.26  ? 428  PHE A O   1 
ATOM   3388 C CB  . PHE A 1 428 ? -11.325 -4.054  -29.023 1.00 20.35  ? 428  PHE A CB  1 
ATOM   3389 C CG  . PHE A 1 428 ? -11.926 -3.812  -27.688 1.00 21.25  ? 428  PHE A CG  1 
ATOM   3390 C CD1 . PHE A 1 428 ? -12.902 -4.682  -27.182 1.00 25.18  ? 428  PHE A CD1 1 
ATOM   3391 C CD2 . PHE A 1 428 ? -11.545 -2.718  -26.931 1.00 24.23  ? 428  PHE A CD2 1 
ATOM   3392 C CE1 . PHE A 1 428 ? -13.489 -4.430  -25.923 1.00 24.93  ? 428  PHE A CE1 1 
ATOM   3393 C CE2 . PHE A 1 428 ? -12.128 -2.479  -25.683 1.00 23.99  ? 428  PHE A CE2 1 
ATOM   3394 C CZ  . PHE A 1 428 ? -13.099 -3.332  -25.201 1.00 23.75  ? 428  PHE A CZ  1 
ATOM   3395 N N   . GLU A 1 429 ? -9.462  -5.154  -31.325 1.00 23.62  ? 429  GLU A N   1 
ATOM   3396 C CA  . GLU A 1 429 ? -9.259  -5.761  -32.658 1.00 25.79  ? 429  GLU A CA  1 
ATOM   3397 C C   . GLU A 1 429 ? -8.694  -7.168  -32.534 1.00 24.54  ? 429  GLU A C   1 
ATOM   3398 O O   . GLU A 1 429 ? -9.188  -8.094  -33.147 1.00 24.71  ? 429  GLU A O   1 
ATOM   3399 C CB  . GLU A 1 429 ? -8.265  -4.947  -33.492 1.00 25.50  ? 429  GLU A CB  1 
ATOM   3400 C CG  . GLU A 1 429 ? -8.723  -3.562  -33.949 1.00 30.28  ? 429  GLU A CG  1 
ATOM   3401 C CD  . GLU A 1 429 ? -7.626  -2.882  -34.795 1.00 31.29  ? 429  GLU A CD  1 
ATOM   3402 O OE1 . GLU A 1 429 ? -7.230  -3.515  -35.814 1.00 39.10  ? 429  GLU A OE1 1 
ATOM   3403 O OE2 . GLU A 1 429 ? -7.132  -1.762  -34.423 1.00 37.76  ? 429  GLU A OE2 1 
ATOM   3404 N N   . LEU A 1 430 ? -7.612  -7.315  -31.773 1.00 25.23  ? 430  LEU A N   1 
ATOM   3405 C CA  . LEU A 1 430 ? -7.010  -8.622  -31.543 1.00 24.64  ? 430  LEU A CA  1 
ATOM   3406 C C   . LEU A 1 430 ? -7.962  -9.635  -30.912 1.00 24.94  ? 430  LEU A C   1 
ATOM   3407 O O   . LEU A 1 430 ? -8.027  -10.794 -31.353 1.00 24.40  ? 430  LEU A O   1 
ATOM   3408 C CB  . LEU A 1 430 ? -5.735  -8.479  -30.700 1.00 26.58  ? 430  LEU A CB  1 
ATOM   3409 C CG  . LEU A 1 430 ? -4.615  -7.578  -31.265 1.00 27.74  ? 430  LEU A CG  1 
ATOM   3410 C CD1 . LEU A 1 430 ? -3.577  -7.299  -30.190 1.00 28.67  ? 430  LEU A CD1 1 
ATOM   3411 C CD2 . LEU A 1 430 ? -3.946  -8.125  -32.536 1.00 32.35  ? 430  LEU A CD2 1 
ATOM   3412 N N   . PHE A 1 431 ? -8.731  -9.231  -29.897 1.00 23.86  ? 431  PHE A N   1 
ATOM   3413 C CA  . PHE A 1 431 ? -9.647  -10.175 -29.269 1.00 24.05  ? 431  PHE A CA  1 
ATOM   3414 C C   . PHE A 1 431 ? -10.851 -10.501 -30.146 1.00 24.23  ? 431  PHE A C   1 
ATOM   3415 O O   . PHE A 1 431 ? -11.394 -11.615 -30.090 1.00 23.85  ? 431  PHE A O   1 
ATOM   3416 C CB  . PHE A 1 431 ? -10.150 -9.654  -27.934 1.00 23.70  ? 431  PHE A CB  1 
ATOM   3417 C CG  . PHE A 1 431 ? -10.768 -10.716 -27.074 1.00 23.90  ? 431  PHE A CG  1 
ATOM   3418 C CD1 . PHE A 1 431 ? -10.057 -11.893 -26.785 1.00 24.08  ? 431  PHE A CD1 1 
ATOM   3419 C CD2 . PHE A 1 431 ? -12.029 -10.526 -26.518 1.00 25.12  ? 431  PHE A CD2 1 
ATOM   3420 C CE1 . PHE A 1 431 ? -10.612 -12.858 -25.964 1.00 25.63  ? 431  PHE A CE1 1 
ATOM   3421 C CE2 . PHE A 1 431 ? -12.608 -11.488 -25.687 1.00 24.63  ? 431  PHE A CE2 1 
ATOM   3422 C CZ  . PHE A 1 431 ? -11.917 -12.650 -25.411 1.00 26.21  ? 431  PHE A CZ  1 
ATOM   3423 N N   . HIS A 1 432 ? -11.287 -9.516  -30.924 1.00 25.02  ? 432  HIS A N   1 
ATOM   3424 C CA  . HIS A 1 432 ? -12.424 -9.725  -31.824 1.00 26.41  ? 432  HIS A CA  1 
ATOM   3425 C C   . HIS A 1 432 ? -12.071 -10.729 -32.924 1.00 27.49  ? 432  HIS A C   1 
ATOM   3426 O O   . HIS A 1 432 ? -12.952 -11.426 -33.423 1.00 26.74  ? 432  HIS A O   1 
ATOM   3427 C CB  . HIS A 1 432 ? -12.923 -8.419  -32.425 1.00 25.71  ? 432  HIS A CB  1 
ATOM   3428 C CG  . HIS A 1 432 ? -14.270 -8.541  -33.069 1.00 28.64  ? 432  HIS A CG  1 
ATOM   3429 N ND1 . HIS A 1 432 ? -14.437 -8.645  -34.434 1.00 30.17  ? 432  HIS A ND1 1 
ATOM   3430 C CD2 . HIS A 1 432 ? -15.515 -8.605  -32.534 1.00 28.73  ? 432  HIS A CD2 1 
ATOM   3431 C CE1 . HIS A 1 432 ? -15.726 -8.750  -34.713 1.00 30.51  ? 432  HIS A CE1 1 
ATOM   3432 N NE2 . HIS A 1 432 ? -16.402 -8.734  -33.577 1.00 29.83  ? 432  HIS A NE2 1 
ATOM   3433 N N   . ASN A 1 433 ? -10.781 -10.825 -33.258 1.00 29.13  ? 433  ASN A N   1 
ATOM   3434 C CA  . ASN A 1 433 ? -10.306 -11.866 -34.179 1.00 31.45  ? 433  ASN A CA  1 
ATOM   3435 C C   . ASN A 1 433 ? -10.503 -13.289 -33.678 1.00 31.86  ? 433  ASN A C   1 
ATOM   3436 O O   . ASN A 1 433 ? -10.513 -14.210 -34.478 1.00 33.62  ? 433  ASN A O   1 
ATOM   3437 C CB  . ASN A 1 433 ? -8.834  -11.643 -34.541 1.00 31.78  ? 433  ASN A CB  1 
ATOM   3438 C CG  . ASN A 1 433 ? -8.645  -10.410 -35.374 1.00 35.21  ? 433  ASN A CG  1 
ATOM   3439 O OD1 . ASN A 1 433 ? -9.622  -9.813  -35.842 1.00 39.02  ? 433  ASN A OD1 1 
ATOM   3440 N ND2 . ASN A 1 433 ? -7.401  -9.999  -35.557 1.00 38.26  ? 433  ASN A ND2 1 
ATOM   3441 N N   . GLN A 1 434 ? -10.647 -13.459 -32.363 1.00 31.47  ? 434  GLN A N   1 
ATOM   3442 C CA  . GLN A 1 434 ? -10.819 -14.756 -31.727 1.00 31.60  ? 434  GLN A CA  1 
ATOM   3443 C C   . GLN A 1 434 ? -12.273 -15.003 -31.356 1.00 30.32  ? 434  GLN A C   1 
ATOM   3444 O O   . GLN A 1 434 ? -12.796 -16.073 -31.596 1.00 29.97  ? 434  GLN A O   1 
ATOM   3445 C CB  . GLN A 1 434 ? -9.947  -14.855 -30.477 1.00 30.88  ? 434  GLN A CB  1 
ATOM   3446 C CG  . GLN A 1 434 ? -8.489  -14.448 -30.706 1.00 35.18  ? 434  GLN A CG  1 
ATOM   3447 C CD  . GLN A 1 434 ? -7.611  -14.646 -29.479 1.00 36.01  ? 434  GLN A CD  1 
ATOM   3448 O OE1 . GLN A 1 434 ? -7.383  -13.702 -28.702 1.00 41.81  ? 434  GLN A OE1 1 
ATOM   3449 N NE2 . GLN A 1 434 ? -7.107  -15.876 -29.296 1.00 41.15  ? 434  GLN A NE2 1 
ATOM   3450 N N   . VAL A 1 435 ? -12.917 -14.002 -30.755 1.00 28.94  ? 435  VAL A N   1 
ATOM   3451 C CA  . VAL A 1 435 ? -14.276 -14.122 -30.240 1.00 27.47  ? 435  VAL A CA  1 
ATOM   3452 C C   . VAL A 1 435 ? -15.062 -12.972 -30.883 1.00 27.09  ? 435  VAL A C   1 
ATOM   3453 O O   . VAL A 1 435 ? -14.777 -11.811 -30.608 1.00 26.28  ? 435  VAL A O   1 
ATOM   3454 C CB  . VAL A 1 435 ? -14.308 -13.971 -28.709 1.00 27.47  ? 435  VAL A CB  1 
ATOM   3455 C CG1 . VAL A 1 435 ? -15.730 -14.223 -28.170 1.00 26.88  ? 435  VAL A CG1 1 
ATOM   3456 C CG2 . VAL A 1 435 ? -13.305 -14.923 -28.030 1.00 26.98  ? 435  VAL A CG2 1 
ATOM   3457 N N   . GLU A 1 436 ? -16.021 -13.286 -31.747 1.00 26.23  ? 436  GLU A N   1 
ATOM   3458 C CA  . GLU A 1 436 ? -16.712 -12.223 -32.522 1.00 26.12  ? 436  GLU A CA  1 
ATOM   3459 C C   . GLU A 1 436 ? -17.908 -11.629 -31.797 1.00 24.37  ? 436  GLU A C   1 
ATOM   3460 O O   . GLU A 1 436 ? -19.081 -11.823 -32.202 1.00 23.44  ? 436  GLU A O   1 
ATOM   3461 C CB  . GLU A 1 436 ? -17.106 -12.710 -33.906 1.00 26.67  ? 436  GLU A CB  1 
ATOM   3462 C CG  . GLU A 1 436 ? -15.881 -12.902 -34.792 1.00 33.24  ? 436  GLU A CG  1 
ATOM   3463 C CD  . GLU A 1 436 ? -16.233 -13.112 -36.250 1.00 41.70  ? 436  GLU A CD  1 
ATOM   3464 O OE1 . GLU A 1 436 ? -17.430 -13.377 -36.573 1.00 42.39  ? 436  GLU A OE1 1 
ATOM   3465 O OE2 . GLU A 1 436 ? -15.284 -13.017 -37.067 1.00 44.19  ? 436  GLU A OE2 1 
ATOM   3466 N N   . PHE A 1 437 ? -17.590 -10.961 -30.694 1.00 22.97  ? 437  PHE A N   1 
ATOM   3467 C CA  . PHE A 1 437 ? -18.582 -10.273 -29.838 1.00 21.84  ? 437  PHE A CA  1 
ATOM   3468 C C   . PHE A 1 437 ? -19.203 -9.095  -30.602 1.00 20.93  ? 437  PHE A C   1 
ATOM   3469 O O   . PHE A 1 437 ? -18.588 -8.560  -31.520 1.00 20.01  ? 437  PHE A O   1 
ATOM   3470 C CB  . PHE A 1 437 ? -17.947 -9.810  -28.507 1.00 21.09  ? 437  PHE A CB  1 
ATOM   3471 C CG  . PHE A 1 437 ? -16.792 -8.891  -28.695 1.00 21.22  ? 437  PHE A CG  1 
ATOM   3472 C CD1 . PHE A 1 437 ? -16.986 -7.523  -28.861 1.00 18.54  ? 437  PHE A CD1 1 
ATOM   3473 C CD2 . PHE A 1 437 ? -15.501 -9.406  -28.783 1.00 20.29  ? 437  PHE A CD2 1 
ATOM   3474 C CE1 . PHE A 1 437 ? -15.919 -6.661  -29.081 1.00 22.40  ? 437  PHE A CE1 1 
ATOM   3475 C CE2 . PHE A 1 437 ? -14.423 -8.545  -29.015 1.00 18.18  ? 437  PHE A CE2 1 
ATOM   3476 C CZ  . PHE A 1 437 ? -14.647 -7.174  -29.167 1.00 20.35  ? 437  PHE A CZ  1 
ATOM   3477 N N   . ASP A 1 438 ? -20.405 -8.680  -30.188 1.00 19.38  ? 438  ASP A N   1 
ATOM   3478 C CA  . ASP A 1 438 ? -21.181 -7.667  -30.910 1.00 18.71  ? 438  ASP A CA  1 
ATOM   3479 C C   . ASP A 1 438 ? -21.309 -6.345  -30.141 1.00 17.36  ? 438  ASP A C   1 
ATOM   3480 O O   . ASP A 1 438 ? -21.648 -5.322  -30.704 1.00 17.17  ? 438  ASP A O   1 
ATOM   3481 C CB  . ASP A 1 438 ? -22.572 -8.216  -31.114 1.00 19.09  ? 438  ASP A CB  1 
ATOM   3482 C CG  . ASP A 1 438 ? -22.557 -9.456  -31.953 1.00 20.17  ? 438  ASP A CG  1 
ATOM   3483 O OD1 . ASP A 1 438 ? -22.218 -9.326  -33.153 1.00 20.92  ? 438  ASP A OD1 1 
ATOM   3484 O OD2 . ASP A 1 438 ? -22.824 -10.538 -31.405 1.00 22.24  ? 438  ASP A OD2 1 
ATOM   3485 N N   . GLY A 1 439 ? -21.077 -6.399  -28.841 1.00 17.77  ? 439  GLY A N   1 
ATOM   3486 C CA  . GLY A 1 439 ? -21.121 -5.208  -27.983 1.00 17.05  ? 439  GLY A CA  1 
ATOM   3487 C C   . GLY A 1 439 ? -20.242 -5.408  -26.753 1.00 17.81  ? 439  GLY A C   1 
ATOM   3488 O O   . GLY A 1 439 ? -19.736 -6.520  -26.516 1.00 18.41  ? 439  GLY A O   1 
ATOM   3489 N N   . ILE A 1 440 ? -20.083 -4.339  -25.973 1.00 17.72  ? 440  ILE A N   1 
ATOM   3490 C CA  . ILE A 1 440 ? -19.090 -4.291  -24.904 1.00 18.07  ? 440  ILE A CA  1 
ATOM   3491 C C   . ILE A 1 440 ? -19.762 -3.738  -23.656 1.00 17.63  ? 440  ILE A C   1 
ATOM   3492 O O   . ILE A 1 440 ? -20.508 -2.762  -23.707 1.00 17.45  ? 440  ILE A O   1 
ATOM   3493 C CB  . ILE A 1 440 ? -17.892 -3.409  -25.289 1.00 18.74  ? 440  ILE A CB  1 
ATOM   3494 C CG1 . ILE A 1 440 ? -17.199 -3.968  -26.562 1.00 19.62  ? 440  ILE A CG1 1 
ATOM   3495 C CG2 . ILE A 1 440 ? -16.891 -3.344  -24.132 1.00 21.60  ? 440  ILE A CG2 1 
ATOM   3496 C CD1 . ILE A 1 440 ? -16.376 -2.914  -27.339 1.00 23.80  ? 440  ILE A CD1 1 
ATOM   3497 N N   . TRP A 1 441 ? -19.491 -4.391  -22.537 1.00 16.13  ? 441  TRP A N   1 
ATOM   3498 C CA  . TRP A 1 441 ? -20.058 -4.022  -21.266 1.00 16.85  ? 441  TRP A CA  1 
ATOM   3499 C C   . TRP A 1 441 ? -18.862 -3.596  -20.434 1.00 17.06  ? 441  TRP A C   1 
ATOM   3500 O O   . TRP A 1 441 ? -18.040 -4.430  -20.094 1.00 17.08  ? 441  TRP A O   1 
ATOM   3501 C CB  . TRP A 1 441 ? -20.784 -5.241  -20.719 1.00 17.35  ? 441  TRP A CB  1 
ATOM   3502 C CG  . TRP A 1 441 ? -21.126 -5.224  -19.294 1.00 16.78  ? 441  TRP A CG  1 
ATOM   3503 C CD1 . TRP A 1 441 ? -21.169 -4.138  -18.460 1.00 19.02  ? 441  TRP A CD1 1 
ATOM   3504 C CD2 . TRP A 1 441 ? -21.514 -6.352  -18.515 1.00 19.07  ? 441  TRP A CD2 1 
ATOM   3505 N NE1 . TRP A 1 441 ? -21.550 -4.530  -17.193 1.00 21.68  ? 441  TRP A NE1 1 
ATOM   3506 C CE2 . TRP A 1 441 ? -21.780 -5.881  -17.199 1.00 20.34  ? 441  TRP A CE2 1 
ATOM   3507 C CE3 . TRP A 1 441 ? -21.683 -7.726  -18.799 1.00 18.32  ? 441  TRP A CE3 1 
ATOM   3508 C CZ2 . TRP A 1 441 ? -22.190 -6.734  -16.165 1.00 20.45  ? 441  TRP A CZ2 1 
ATOM   3509 C CZ3 . TRP A 1 441 ? -22.055 -8.580  -17.765 1.00 18.44  ? 441  TRP A CZ3 1 
ATOM   3510 C CH2 . TRP A 1 441 ? -22.283 -8.074  -16.453 1.00 18.33  ? 441  TRP A CH2 1 
ATOM   3511 N N   . ILE A 1 442 ? -18.727 -2.294  -20.206 1.00 17.20  ? 442  ILE A N   1 
ATOM   3512 C CA  . ILE A 1 442 ? -17.607 -1.734  -19.401 1.00 18.32  ? 442  ILE A CA  1 
ATOM   3513 C C   . ILE A 1 442 ? -18.055 -1.526  -17.961 1.00 19.29  ? 442  ILE A C   1 
ATOM   3514 O O   . ILE A 1 442 ? -19.118 -0.892  -17.677 1.00 20.13  ? 442  ILE A O   1 
ATOM   3515 C CB  . ILE A 1 442 ? -16.935 -0.479  -20.037 1.00 19.02  ? 442  ILE A CB  1 
ATOM   3516 C CG1 . ILE A 1 442 ? -17.958 0.652   -20.289 1.00 17.14  ? 442  ILE A CG1 1 
ATOM   3517 C CG2 . ILE A 1 442 ? -16.171 -0.866  -21.343 1.00 17.73  ? 442  ILE A CG2 1 
ATOM   3518 C CD1 . ILE A 1 442 ? -17.338 1.954   -20.845 1.00 19.32  ? 442  ILE A CD1 1 
ATOM   3519 N N   . ASP A 1 443 ? -17.320 -2.169  -17.060 1.00 19.23  ? 443  ASP A N   1 
ATOM   3520 C CA  . ASP A 1 443 ? -17.686 -2.281  -15.670 1.00 20.15  ? 443  ASP A CA  1 
ATOM   3521 C C   . ASP A 1 443 ? -16.502 -1.859  -14.766 1.00 20.53  ? 443  ASP A C   1 
ATOM   3522 O O   . ASP A 1 443 ? -15.391 -1.677  -15.258 1.00 20.22  ? 443  ASP A O   1 
ATOM   3523 C CB  . ASP A 1 443 ? -18.024 -3.729  -15.405 1.00 20.78  ? 443  ASP A CB  1 
ATOM   3524 C CG  . ASP A 1 443 ? -18.601 -3.950  -14.035 1.00 23.48  ? 443  ASP A CG  1 
ATOM   3525 O OD1 . ASP A 1 443 ? -19.281 -3.028  -13.516 1.00 23.79  ? 443  ASP A OD1 1 
ATOM   3526 O OD2 . ASP A 1 443 ? -18.335 -5.039  -13.476 1.00 27.53  ? 443  ASP A OD2 1 
ATOM   3527 N N   . MET A 1 444 ? -16.766 -1.709  -13.465 1.00 20.24  ? 444  MET A N   1 
ATOM   3528 C CA  . MET A 1 444 ? -15.720 -1.414  -12.462 1.00 20.46  ? 444  MET A CA  1 
ATOM   3529 C C   . MET A 1 444 ? -15.005 -0.108  -12.795 1.00 19.93  ? 444  MET A C   1 
ATOM   3530 O O   . MET A 1 444 ? -13.838 0.082   -12.441 1.00 19.07  ? 444  MET A O   1 
ATOM   3531 C CB  . MET A 1 444 ? -14.702 -2.557  -12.435 1.00 20.92  ? 444  MET A CB  1 
ATOM   3532 C CG  . MET A 1 444 ? -15.270 -3.938  -12.228 1.00 22.38  ? 444  MET A CG  1 
ATOM   3533 S SD  . MET A 1 444 ? -16.183 -4.089  -10.687 1.00 27.23  ? 444  MET A SD  1 
ATOM   3534 C CE  . MET A 1 444 ? -14.751 -4.150  -9.568  1.00 19.05  ? 444  MET A CE  1 
ATOM   3535 N N   . ASN A 1 445 ? -15.680 0.788   -13.527 1.00 18.49  ? 445  ASN A N   1 
ATOM   3536 C CA  . ASN A 1 445 ? -14.980 1.945   -14.107 1.00 16.84  ? 445  ASN A CA  1 
ATOM   3537 C C   . ASN A 1 445 ? -15.233 3.278   -13.395 1.00 17.04  ? 445  ASN A C   1 
ATOM   3538 O O   . ASN A 1 445 ? -15.169 4.341   -13.989 1.00 16.95  ? 445  ASN A O   1 
ATOM   3539 C CB  . ASN A 1 445 ? -15.190 2.029   -15.611 1.00 15.54  ? 445  ASN A CB  1 
ATOM   3540 C CG  . ASN A 1 445 ? -16.687 2.149   -15.986 1.00 17.01  ? 445  ASN A CG  1 
ATOM   3541 O OD1 . ASN A 1 445 ? -17.559 2.058   -15.148 1.00 17.05  ? 445  ASN A OD1 1 
ATOM   3542 N ND2 . ASN A 1 445 ? -16.943 2.401   -17.244 1.00 16.45  ? 445  ASN A ND2 1 
ATOM   3543 N N   . GLU A 1 446 ? -15.425 3.202   -12.090 1.00 16.92  ? 446  GLU A N   1 
ATOM   3544 C CA  . GLU A 1 446 ? -15.503 4.416   -11.255 1.00 18.73  ? 446  GLU A CA  1 
ATOM   3545 C C   . GLU A 1 446 ? -14.244 5.260   -11.082 1.00 20.39  ? 446  GLU A C   1 
ATOM   3546 O O   . GLU A 1 446 ? -14.364 6.474   -10.951 1.00 20.98  ? 446  GLU A O   1 
ATOM   3547 C CB  . GLU A 1 446 ? -16.064 4.072   -9.871  1.00 19.16  ? 446  GLU A CB  1 
ATOM   3548 C CG  . GLU A 1 446 ? -17.536 3.621   -9.899  1.00 18.60  ? 446  GLU A CG  1 
ATOM   3549 C CD  . GLU A 1 446 ? -17.784 2.240   -10.557 1.00 25.65  ? 446  GLU A CD  1 
ATOM   3550 O OE1 . GLU A 1 446 ? -16.936 1.331   -10.412 1.00 23.04  ? 446  GLU A OE1 1 
ATOM   3551 O OE2 . GLU A 1 446 ? -18.870 2.065   -11.210 1.00 27.51  ? 446  GLU A OE2 1 
ATOM   3552 N N   . VAL A 1 447 ? -13.024 4.699   -11.029 1.00 21.47  ? 447  VAL A N   1 
ATOM   3553 C CA  . VAL A 1 447 ? -12.659 3.324   -11.209 1.00 22.79  ? 447  VAL A CA  1 
ATOM   3554 C C   . VAL A 1 447 ? -12.670 2.570   -9.850  1.00 23.72  ? 447  VAL A C   1 
ATOM   3555 O O   . VAL A 1 447 ? -12.422 3.155   -8.793  1.00 24.65  ? 447  VAL A O   1 
ATOM   3556 C CB  . VAL A 1 447 ? -11.284 3.292   -11.948 1.00 23.57  ? 447  VAL A CB  1 
ATOM   3557 C CG1 . VAL A 1 447 ? -10.180 3.703   -11.038 1.00 26.57  ? 447  VAL A CG1 1 
ATOM   3558 C CG2 . VAL A 1 447 ? -11.027 1.932   -12.546 1.00 25.72  ? 447  VAL A CG2 1 
ATOM   3559 N N   . SER A 1 448 ? -13.059 1.301   -9.873  1.00 23.02  ? 448  SER A N   1 
ATOM   3560 C CA  . SER A 1 448 ? -13.165 0.496   -8.669  1.00 24.03  ? 448  SER A CA  1 
ATOM   3561 C C   . SER A 1 448 ? -11.806 -0.187  -8.401  1.00 23.41  ? 448  SER A C   1 
ATOM   3562 O O   . SER A 1 448 ? -11.140 -0.666  -9.340  1.00 23.96  ? 448  SER A O   1 
ATOM   3563 C CB  . SER A 1 448 ? -14.315 -0.491  -8.820  1.00 24.55  ? 448  SER A CB  1 
ATOM   3564 O OG  . SER A 1 448 ? -14.460 -1.323  -7.683  1.00 29.30  ? 448  SER A OG  1 
ATOM   3565 N N   . ASN A 1 449 ? -11.377 -0.151  -7.143  1.00 21.44  ? 449  ASN A N   1 
ATOM   3566 C CA  . ASN A 1 449 ? -10.081 -0.710  -6.687  1.00 21.21  ? 449  ASN A CA  1 
ATOM   3567 C C   . ASN A 1 449 ? -10.392 -1.535  -5.420  1.00 21.61  ? 449  ASN A C   1 
ATOM   3568 O O   . ASN A 1 449 ? -11.218 -1.121  -4.559  1.00 22.25  ? 449  ASN A O   1 
ATOM   3569 C CB  . ASN A 1 449 ? -9.127  0.446   -6.400  1.00 20.12  ? 449  ASN A CB  1 
ATOM   3570 C CG  . ASN A 1 449 ? -7.661  0.024   -6.289  1.00 21.42  ? 449  ASN A CG  1 
ATOM   3571 O OD1 . ASN A 1 449 ? -7.316  -1.147  -6.375  1.00 20.91  ? 449  ASN A OD1 1 
ATOM   3572 N ND2 . ASN A 1 449 ? -6.801  1.002   -6.095  1.00 20.96  ? 449  ASN A ND2 1 
ATOM   3573 N N   . PHE A 1 450 ? -9.858  -2.748  -5.343  1.00 21.14  ? 450  PHE A N   1 
ATOM   3574 C CA  . PHE A 1 450 ? -10.118 -3.616  -4.195  1.00 22.12  ? 450  PHE A CA  1 
ATOM   3575 C C   . PHE A 1 450 ? -9.221  -3.239  -3.015  1.00 23.35  ? 450  PHE A C   1 
ATOM   3576 O O   . PHE A 1 450 ? -9.421  -3.729  -1.910  1.00 24.23  ? 450  PHE A O   1 
ATOM   3577 C CB  . PHE A 1 450 ? -9.922  -5.103  -4.546  1.00 21.65  ? 450  PHE A CB  1 
ATOM   3578 C CG  . PHE A 1 450 ? -10.980 -5.658  -5.484  1.00 21.72  ? 450  PHE A CG  1 
ATOM   3579 C CD1 . PHE A 1 450 ? -12.145 -4.938  -5.757  1.00 22.01  ? 450  PHE A CD1 1 
ATOM   3580 C CD2 . PHE A 1 450 ? -10.820 -6.913  -6.057  1.00 23.75  ? 450  PHE A CD2 1 
ATOM   3581 C CE1 . PHE A 1 450 ? -13.117 -5.445  -6.609  1.00 22.34  ? 450  PHE A CE1 1 
ATOM   3582 C CE2 . PHE A 1 450 ? -11.810 -7.434  -6.908  1.00 24.31  ? 450  PHE A CE2 1 
ATOM   3583 C CZ  . PHE A 1 450 ? -12.948 -6.693  -7.180  1.00 22.23  ? 450  PHE A CZ  1 
ATOM   3584 N N   . VAL A 1 451 ? -8.231  -2.394  -3.270  1.00 23.12  ? 451  VAL A N   1 
ATOM   3585 C CA  . VAL A 1 451 ? -7.463  -1.750  -2.214  1.00 23.55  ? 451  VAL A CA  1 
ATOM   3586 C C   . VAL A 1 451 ? -7.810  -0.254  -2.218  1.00 23.71  ? 451  VAL A C   1 
ATOM   3587 O O   . VAL A 1 451 ? -8.251  0.273   -3.229  1.00 23.01  ? 451  VAL A O   1 
ATOM   3588 C CB  . VAL A 1 451 ? -5.906  -1.970  -2.393  1.00 22.93  ? 451  VAL A CB  1 
ATOM   3589 C CG1 . VAL A 1 451 ? -5.558  -3.425  -2.267  1.00 24.38  ? 451  VAL A CG1 1 
ATOM   3590 C CG2 . VAL A 1 451 ? -5.410  -1.429  -3.732  1.00 22.85  ? 451  VAL A CG2 1 
ATOM   3591 N N   . ASP A 1 452 ? -7.614  0.432   -1.093  1.00 23.95  ? 452  ASP A N   1 
ATOM   3592 C CA  . ASP A 1 452 ? -7.896  1.846   -1.033  1.00 24.49  ? 452  ASP A CA  1 
ATOM   3593 C C   . ASP A 1 452 ? -6.708  2.617   -1.575  1.00 24.47  ? 452  ASP A C   1 
ATOM   3594 O O   . ASP A 1 452 ? -5.647  2.625   -0.948  1.00 24.88  ? 452  ASP A O   1 
ATOM   3595 C CB  . ASP A 1 452 ? -8.228  2.245   0.407   1.00 24.90  ? 452  ASP A CB  1 
ATOM   3596 C CG  . ASP A 1 452 ? -9.564  1.654   0.888   1.00 28.29  ? 452  ASP A CG  1 
ATOM   3597 O OD1 . ASP A 1 452 ? -10.402 1.214   0.048   1.00 27.30  ? 452  ASP A OD1 1 
ATOM   3598 O OD2 . ASP A 1 452 ? -9.780  1.637   2.129   1.00 32.28  ? 452  ASP A OD2 1 
ATOM   3599 N N   . GLY A 1 453 ? -6.856  3.213   -2.762  1.00 22.72  ? 453  GLY A N   1 
ATOM   3600 C CA  . GLY A 1 453 ? -5.824  4.058   -3.342  1.00 22.69  ? 453  GLY A CA  1 
ATOM   3601 C C   . GLY A 1 453 ? -4.816  3.319   -4.209  1.00 23.37  ? 453  GLY A C   1 
ATOM   3602 O O   . GLY A 1 453 ? -4.742  3.496   -5.419  1.00 22.83  ? 453  GLY A O   1 
ATOM   3603 N N   . SER A 1 454 ? -4.018  2.476   -3.583  1.00 23.61  ? 454  SER A N   1 
ATOM   3604 C CA  . SER A 1 454 ? -3.084  1.670   -4.327  1.00 24.47  ? 454  SER A CA  1 
ATOM   3605 C C   . SER A 1 454 ? -2.613  0.575   -3.375  1.00 24.82  ? 454  SER A C   1 
ATOM   3606 O O   . SER A 1 454 ? -2.993  0.568   -2.195  1.00 24.86  ? 454  SER A O   1 
ATOM   3607 C CB  . SER A 1 454 ? -1.919  2.522   -4.788  1.00 24.80  ? 454  SER A CB  1 
ATOM   3608 O OG  . SER A 1 454 ? -1.040  2.784   -3.699  1.00 28.78  ? 454  SER A OG  1 
ATOM   3609 N N   . VAL A 1 455 ? -1.836  -0.369  -3.891  1.00 25.38  ? 455  VAL A N   1 
ATOM   3610 C CA  . VAL A 1 455 ? -1.297  -1.440  -3.060  1.00 26.15  ? 455  VAL A CA  1 
ATOM   3611 C C   . VAL A 1 455 ? -0.397  -0.886  -1.925  1.00 27.14  ? 455  VAL A C   1 
ATOM   3612 O O   . VAL A 1 455 ? -0.123  -1.567  -0.938  1.00 27.55  ? 455  VAL A O   1 
ATOM   3613 C CB  . VAL A 1 455 ? -0.588  -2.541  -3.909  1.00 26.39  ? 455  VAL A CB  1 
ATOM   3614 C CG1 . VAL A 1 455 ? -1.570  -3.199  -4.893  1.00 24.35  ? 455  VAL A CG1 1 
ATOM   3615 C CG2 . VAL A 1 455 ? 0.685   -2.030  -4.617  1.00 26.12  ? 455  VAL A CG2 1 
ATOM   3616 N N   . SER A 1 456 ? 0.016   0.359   -2.033  1.00 27.61  ? 456  SER A N   1 
ATOM   3617 C CA  . SER A 1 456 ? 0.764   0.967   -0.941  1.00 29.99  ? 456  SER A CA  1 
ATOM   3618 C C   . SER A 1 456 ? 0.008   2.127   -0.262  1.00 29.24  ? 456  SER A C   1 
ATOM   3619 O O   . SER A 1 456 ? 0.592   2.987   0.376   1.00 31.00  ? 456  SER A O   1 
ATOM   3620 C CB  . SER A 1 456 ? 2.171   1.315   -1.399  1.00 29.41  ? 456  SER A CB  1 
ATOM   3621 O OG  . SER A 1 456 ? 2.166   2.486   -2.169  1.00 34.04  ? 456  SER A OG  1 
ATOM   3622 N N   . GLY A 1 457 ? -1.315  2.107   -0.351  1.00 28.94  ? 457  GLY A N   1 
ATOM   3623 C CA  . GLY A 1 457 ? -2.135  3.176   0.205   1.00 28.18  ? 457  GLY A CA  1 
ATOM   3624 C C   . GLY A 1 457 ? -1.924  4.506   -0.499  1.00 28.37  ? 457  GLY A C   1 
ATOM   3625 O O   . GLY A 1 457 ? -1.548  4.544   -1.669  1.00 28.16  ? 457  GLY A O   1 
ATOM   3626 N N   . CYS A 1 458 ? -2.165  5.598   0.231   1.00 27.97  ? 458  CYS A N   1 
ATOM   3627 C CA  . CYS A 1 458 ? -2.081  6.963   -0.295  1.00 27.88  ? 458  CYS A CA  1 
ATOM   3628 C C   . CYS A 1 458 ? -1.333  7.853   0.663   1.00 26.98  ? 458  CYS A C   1 
ATOM   3629 O O   . CYS A 1 458 ? -1.584  7.788   1.850   1.00 27.50  ? 458  CYS A O   1 
ATOM   3630 C CB  . CYS A 1 458 ? -3.475  7.582   -0.356  1.00 27.99  ? 458  CYS A CB  1 
ATOM   3631 S SG  . CYS A 1 458 ? -4.614  6.638   -1.293  1.00 32.07  ? 458  CYS A SG  1 
ATOM   3632 N N   . SER A 1 459 ? -0.517  8.754   0.151   1.00 27.04  ? 459  SER A N   1 
ATOM   3633 C CA  . SER A 1 459 ? 0.141   9.736   1.027   1.00 28.15  ? 459  SER A CA  1 
ATOM   3634 C C   . SER A 1 459 ? -0.845  10.689  1.667   1.00 27.37  ? 459  SER A C   1 
ATOM   3635 O O   . SER A 1 459 ? -1.882  11.018  1.094   1.00 26.83  ? 459  SER A O   1 
ATOM   3636 C CB  . SER A 1 459 ? 1.193   10.536  0.270   1.00 28.41  ? 459  SER A CB  1 
ATOM   3637 O OG  . SER A 1 459 ? 1.968   9.630   -0.492  1.00 33.27  ? 459  SER A OG  1 
ATOM   3638 N N   . THR A 1 460 ? -0.528  11.125  2.878   1.00 26.77  ? 460  THR A N   1 
ATOM   3639 C CA  . THR A 1 460 ? -1.380  12.088  3.557   1.00 26.70  ? 460  THR A CA  1 
ATOM   3640 C C   . THR A 1 460 ? -1.012  13.418  2.928   1.00 26.39  ? 460  THR A C   1 
ATOM   3641 O O   . THR A 1 460 ? 0.154   13.801  2.909   1.00 26.86  ? 460  THR A O   1 
ATOM   3642 C CB  . THR A 1 460 ? -1.121  12.113  5.074   1.00 27.30  ? 460  THR A CB  1 
ATOM   3643 O OG1 . THR A 1 460 ? -1.338  10.800  5.622   1.00 24.84  ? 460  THR A OG1 1 
ATOM   3644 C CG2 . THR A 1 460 ? -2.048  13.151  5.759   1.00 26.68  ? 460  THR A CG2 1 
ATOM   3645 N N   . ASN A 1 461 ? -1.996  14.099  2.349   1.00 23.59  ? 461  ASN A N   1 
ATOM   3646 C CA  . ASN A 1 461 ? -1.749  15.377  1.692   1.00 22.19  ? 461  ASN A CA  1 
ATOM   3647 C C   . ASN A 1 461 ? -3.115  15.992  1.408   1.00 22.00  ? 461  ASN A C   1 
ATOM   3648 O O   . ASN A 1 461 ? -4.116  15.358  1.710   1.00 20.69  ? 461  ASN A O   1 
ATOM   3649 C CB  . ASN A 1 461 ? -0.890  15.231  0.425   1.00 22.29  ? 461  ASN A CB  1 
ATOM   3650 C CG  . ASN A 1 461 ? -1.529  14.389  -0.648  1.00 23.29  ? 461  ASN A CG  1 
ATOM   3651 O OD1 . ASN A 1 461 ? -2.745  14.504  -0.930  1.00 22.92  ? 461  ASN A OD1 1 
ATOM   3652 N ND2 . ASN A 1 461 ? -0.718  13.560  -1.289  1.00 21.74  ? 461  ASN A ND2 1 
ATOM   3653 N N   . ASN A 1 462 ? -3.159  17.194  0.840   1.00 21.42  ? 462  ASN A N   1 
ATOM   3654 C CA  . ASN A 1 462 ? -4.444  17.914  0.742   1.00 21.86  ? 462  ASN A CA  1 
ATOM   3655 C C   . ASN A 1 462 ? -5.422  17.354  -0.302  1.00 20.27  ? 462  ASN A C   1 
ATOM   3656 O O   . ASN A 1 462 ? -6.605  17.714  -0.297  1.00 21.36  ? 462  ASN A O   1 
ATOM   3657 C CB  . ASN A 1 462 ? -4.220  19.397  0.524   1.00 22.90  ? 462  ASN A CB  1 
ATOM   3658 C CG  . ASN A 1 462 ? -3.553  19.698  -0.796  1.00 29.05  ? 462  ASN A CG  1 
ATOM   3659 O OD1 . ASN A 1 462 ? -2.492  19.127  -1.139  1.00 34.70  ? 462  ASN A OD1 1 
ATOM   3660 N ND2 . ASN A 1 462 ? -4.156  20.615  -1.564  1.00 33.23  ? 462  ASN A ND2 1 
ATOM   3661 N N   . LEU A 1 463 ? -4.916  16.502  -1.180  1.00 20.48  ? 463  LEU A N   1 
ATOM   3662 C CA  . LEU A 1 463 ? -5.701  15.811  -2.219  1.00 18.99  ? 463  LEU A CA  1 
ATOM   3663 C C   . LEU A 1 463 ? -6.320  14.550  -1.646  1.00 20.07  ? 463  LEU A C   1 
ATOM   3664 O O   . LEU A 1 463 ? -7.556  14.354  -1.738  1.00 18.71  ? 463  LEU A O   1 
ATOM   3665 C CB  . LEU A 1 463 ? -4.854  15.496  -3.452  1.00 19.40  ? 463  LEU A CB  1 
ATOM   3666 C CG  . LEU A 1 463 ? -4.207  16.712  -4.145  1.00 19.81  ? 463  LEU A CG  1 
ATOM   3667 C CD1 . LEU A 1 463 ? -3.711  16.292  -5.508  1.00 20.34  ? 463  LEU A CD1 1 
ATOM   3668 C CD2 . LEU A 1 463 ? -5.190  17.832  -4.315  1.00 24.39  ? 463  LEU A CD2 1 
ATOM   3669 N N   . ASN A 1 464 ? -5.501  13.714  -0.998  1.00 18.52  ? 464  ASN A N   1 
ATOM   3670 C CA  . ASN A 1 464 ? -6.027  12.488  -0.359  1.00 20.01  ? 464  ASN A CA  1 
ATOM   3671 C C   . ASN A 1 464 ? -6.819  12.767  0.900   1.00 19.88  ? 464  ASN A C   1 
ATOM   3672 O O   . ASN A 1 464 ? -7.737  12.034  1.255   1.00 20.18  ? 464  ASN A O   1 
ATOM   3673 C CB  . ASN A 1 464 ? -4.894  11.482  -0.061  1.00 19.55  ? 464  ASN A CB  1 
ATOM   3674 C CG  . ASN A 1 464 ? -4.287  10.916  -1.303  1.00 22.62  ? 464  ASN A CG  1 
ATOM   3675 O OD1 . ASN A 1 464 ? -3.054  10.800  -1.413  1.00 27.54  ? 464  ASN A OD1 1 
ATOM   3676 N ND2 . ASN A 1 464 ? -5.123  10.551  -2.260  1.00 21.47  ? 464  ASN A ND2 1 
ATOM   3677 N N   . ASN A 1 465 ? -6.463  13.853  1.571   1.00 20.77  ? 465  ASN A N   1 
ATOM   3678 C CA  . ASN A 1 465 ? -7.106  14.260  2.820   1.00 21.80  ? 465  ASN A CA  1 
ATOM   3679 C C   . ASN A 1 465 ? -7.458  15.743  2.792   1.00 21.71  ? 465  ASN A C   1 
ATOM   3680 O O   . ASN A 1 465 ? -6.723  16.581  3.331   1.00 20.86  ? 465  ASN A O   1 
ATOM   3681 C CB  . ASN A 1 465 ? -6.187  13.929  4.011   1.00 22.52  ? 465  ASN A CB  1 
ATOM   3682 C CG  . ASN A 1 465 ? -5.805  12.463  4.040   1.00 23.24  ? 465  ASN A CG  1 
ATOM   3683 O OD1 . ASN A 1 465 ? -6.517  11.653  4.617   1.00 25.17  ? 465  ASN A OD1 1 
ATOM   3684 N ND2 . ASN A 1 465 ? -4.680  12.116  3.400   1.00 22.73  ? 465  ASN A ND2 1 
ATOM   3685 N N   . PRO A 1 466 ? -8.573  16.095  2.121   1.00 20.56  ? 466  PRO A N   1 
ATOM   3686 C CA  . PRO A 1 466 ? -8.812  17.518  1.913   1.00 20.54  ? 466  PRO A CA  1 
ATOM   3687 C C   . PRO A 1 466 ? -9.409  18.188  3.157   1.00 20.26  ? 466  PRO A C   1 
ATOM   3688 O O   . PRO A 1 466 ? -9.857  17.487  4.061   1.00 21.58  ? 466  PRO A O   1 
ATOM   3689 C CB  . PRO A 1 466 ? -9.808  17.518  0.716   1.00 19.80  ? 466  PRO A CB  1 
ATOM   3690 C CG  . PRO A 1 466 ? -10.603 16.268  0.930   1.00 20.13  ? 466  PRO A CG  1 
ATOM   3691 C CD  . PRO A 1 466 ? -9.610  15.255  1.475   1.00 21.40  ? 466  PRO A CD  1 
ATOM   3692 N N   . PRO A 1 467 ? -9.424  19.532  3.203   1.00 20.65  ? 467  PRO A N   1 
ATOM   3693 C CA  . PRO A 1 467 ? -9.979  20.269  4.346   1.00 20.72  ? 467  PRO A CA  1 
ATOM   3694 C C   . PRO A 1 467 ? -11.463 19.949  4.606   1.00 21.59  ? 467  PRO A C   1 
ATOM   3695 O O   . PRO A 1 467 ? -11.906 19.898  5.761   1.00 21.97  ? 467  PRO A O   1 
ATOM   3696 C CB  . PRO A 1 467 ? -9.759  21.742  3.984   1.00 20.98  ? 467  PRO A CB  1 
ATOM   3697 C CG  . PRO A 1 467 ? -9.191  21.776  2.600   1.00 21.23  ? 467  PRO A CG  1 
ATOM   3698 C CD  . PRO A 1 467 ? -8.850  20.406  2.158   1.00 20.50  ? 467  PRO A CD  1 
ATOM   3699 N N   . PHE A 1 468 ? -12.224 19.703  3.535   1.00 20.90  ? 468  PHE A N   1 
ATOM   3700 C CA  . PHE A 1 468 ? -13.624 19.311  3.660   1.00 20.06  ? 468  PHE A CA  1 
ATOM   3701 C C   . PHE A 1 468 ? -13.885 18.071  2.786   1.00 19.30  ? 468  PHE A C   1 
ATOM   3702 O O   . PHE A 1 468 ? -13.440 18.007  1.639   1.00 19.64  ? 468  PHE A O   1 
ATOM   3703 C CB  . PHE A 1 468 ? -14.528 20.430  3.182   1.00 19.70  ? 468  PHE A CB  1 
ATOM   3704 C CG  . PHE A 1 468 ? -15.992 20.074  3.247   1.00 19.93  ? 468  PHE A CG  1 
ATOM   3705 C CD1 . PHE A 1 468 ? -16.654 20.084  4.469   1.00 22.11  ? 468  PHE A CD1 1 
ATOM   3706 C CD2 . PHE A 1 468 ? -16.677 19.653  2.092   1.00 19.22  ? 468  PHE A CD2 1 
ATOM   3707 C CE1 . PHE A 1 468 ? -18.015 19.748  4.553   1.00 21.54  ? 468  PHE A CE1 1 
ATOM   3708 C CE2 . PHE A 1 468 ? -18.048 19.293  2.153   1.00 19.73  ? 468  PHE A CE2 1 
ATOM   3709 C CZ  . PHE A 1 468 ? -18.700 19.341  3.375   1.00 20.45  ? 468  PHE A CZ  1 
ATOM   3710 N N   . THR A 1 469 ? -14.559 17.072  3.348   1.00 19.06  ? 469  THR A N   1 
ATOM   3711 C CA  . THR A 1 469 ? -14.917 15.869  2.609   1.00 18.78  ? 469  THR A CA  1 
ATOM   3712 C C   . THR A 1 469 ? -16.454 15.837  2.600   1.00 18.85  ? 469  THR A C   1 
ATOM   3713 O O   . THR A 1 469 ? -17.063 15.841  3.665   1.00 18.42  ? 469  THR A O   1 
ATOM   3714 C CB  . THR A 1 469 ? -14.290 14.597  3.273   1.00 20.81  ? 469  THR A CB  1 
ATOM   3715 O OG1 . THR A 1 469 ? -12.865 14.797  3.447   1.00 21.33  ? 469  THR A OG1 1 
ATOM   3716 C CG2 . THR A 1 469 ? -14.515 13.327  2.414   1.00 20.06  ? 469  THR A CG2 1 
ATOM   3717 N N   . PRO A 1 470 ? -17.084 15.843  1.395   1.00 18.31  ? 470  PRO A N   1 
ATOM   3718 C CA  . PRO A 1 470 ? -18.567 15.687  1.343   1.00 19.11  ? 470  PRO A CA  1 
ATOM   3719 C C   . PRO A 1 470 ? -18.924 14.347  1.996   1.00 19.31  ? 470  PRO A C   1 
ATOM   3720 O O   . PRO A 1 470 ? -18.045 13.518  2.191   1.00 19.87  ? 470  PRO A O   1 
ATOM   3721 C CB  . PRO A 1 470 ? -18.878 15.645  -0.171  1.00 17.80  ? 470  PRO A CB  1 
ATOM   3722 C CG  . PRO A 1 470 ? -17.707 16.243  -0.831  1.00 19.55  ? 470  PRO A CG  1 
ATOM   3723 C CD  . PRO A 1 470 ? -16.487 15.980  0.053   1.00 18.87  ? 470  PRO A CD  1 
ATOM   3724 N N   . ARG A 1 471 ? -20.193 14.085  2.298   1.00 19.26  ? 471  ARG A N   1 
ATOM   3725 C CA  . ARG A 1 471 ? -20.523 12.864  3.018   1.00 19.52  ? 471  ARG A CA  1 
ATOM   3726 C C   . ARG A 1 471 ? -20.543 11.602  2.149   1.00 19.07  ? 471  ARG A C   1 
ATOM   3727 O O   . ARG A 1 471 ? -21.505 10.853  2.153   1.00 19.92  ? 471  ARG A O   1 
ATOM   3728 C CB  . ARG A 1 471 ? -21.847 13.038  3.756   1.00 20.21  ? 471  ARG A CB  1 
ATOM   3729 C CG  . ARG A 1 471 ? -22.987 13.417  2.852   1.00 23.92  ? 471  ARG A CG  1 
ATOM   3730 C CD  . ARG A 1 471 ? -24.231 13.561  3.645   1.00 28.80  ? 471  ARG A CD  1 
ATOM   3731 N NE  . ARG A 1 471 ? -24.068 14.627  4.630   1.00 31.92  ? 471  ARG A NE  1 
ATOM   3732 C CZ  . ARG A 1 471 ? -24.992 14.931  5.536   1.00 35.84  ? 471  ARG A CZ  1 
ATOM   3733 N NH1 . ARG A 1 471 ? -26.143 14.241  5.575   1.00 35.46  ? 471  ARG A NH1 1 
ATOM   3734 N NH2 . ARG A 1 471 ? -24.766 15.924  6.397   1.00 34.00  ? 471  ARG A NH2 1 
ATOM   3735 N N   . ILE A 1 472 ? -19.442 11.331  1.457   1.00 19.14  ? 472  ILE A N   1 
ATOM   3736 C CA  . ILE A 1 472 ? -19.331 10.152  0.635   1.00 17.70  ? 472  ILE A CA  1 
ATOM   3737 C C   . ILE A 1 472 ? -19.261 8.904   1.519   1.00 18.09  ? 472  ILE A C   1 
ATOM   3738 O O   . ILE A 1 472 ? -18.845 8.977   2.681   1.00 19.50  ? 472  ILE A O   1 
ATOM   3739 C CB  . ILE A 1 472 ? -18.114 10.222  -0.305  1.00 16.90  ? 472  ILE A CB  1 
ATOM   3740 C CG1 . ILE A 1 472 ? -16.805 10.412  0.468   1.00 18.84  ? 472  ILE A CG1 1 
ATOM   3741 C CG2 . ILE A 1 472 ? -18.301 11.307  -1.333  1.00 17.97  ? 472  ILE A CG2 1 
ATOM   3742 C CD1 . ILE A 1 472 ? -15.622 10.222  -0.393  1.00 20.37  ? 472  ILE A CD1 1 
ATOM   3743 N N   . LEU A 1 473 ? -19.626 7.763   0.953   1.00 17.86  ? 473  LEU A N   1 
ATOM   3744 C CA  . LEU A 1 473 ? -19.597 6.518   1.670   1.00 18.84  ? 473  LEU A CA  1 
ATOM   3745 C C   . LEU A 1 473 ? -18.173 6.284   2.188   1.00 19.14  ? 473  LEU A C   1 
ATOM   3746 O O   . LEU A 1 473 ? -17.228 6.407   1.429   1.00 20.01  ? 473  LEU A O   1 
ATOM   3747 C CB  . LEU A 1 473 ? -20.055 5.404   0.739   1.00 18.47  ? 473  LEU A CB  1 
ATOM   3748 C CG  . LEU A 1 473 ? -20.105 3.981   1.314   1.00 19.04  ? 473  LEU A CG  1 
ATOM   3749 C CD1 . LEU A 1 473 ? -20.937 3.799   2.565   1.00 20.60  ? 473  LEU A CD1 1 
ATOM   3750 C CD2 . LEU A 1 473 ? -20.520 3.043   0.237   1.00 17.81  ? 473  LEU A CD2 1 
ATOM   3751 N N   . ASP A 1 474 ? -18.041 6.035   3.494   1.00 20.71  ? 474  ASP A N   1 
ATOM   3752 C CA  . ASP A 1 474 ? -16.771 5.715   4.140   1.00 21.96  ? 474  ASP A CA  1 
ATOM   3753 C C   . ASP A 1 474 ? -15.927 6.934   4.486   1.00 21.73  ? 474  ASP A C   1 
ATOM   3754 O O   . ASP A 1 474 ? -14.976 6.825   5.260   1.00 22.36  ? 474  ASP A O   1 
ATOM   3755 C CB  . ASP A 1 474 ? -15.923 4.760   3.290   1.00 22.44  ? 474  ASP A CB  1 
ATOM   3756 C CG  . ASP A 1 474 ? -16.497 3.356   3.213   1.00 26.56  ? 474  ASP A CG  1 
ATOM   3757 O OD1 . ASP A 1 474 ? -17.090 2.839   4.204   1.00 31.85  ? 474  ASP A OD1 1 
ATOM   3758 O OD2 . ASP A 1 474 ? -16.348 2.739   2.139   1.00 29.74  ? 474  ASP A OD2 1 
ATOM   3759 N N   . GLY A 1 475 ? -16.241 8.081   3.903   1.00 20.12  ? 475  GLY A N   1 
ATOM   3760 C CA  . GLY A 1 475 ? -15.650 9.337   4.324   1.00 20.10  ? 475  GLY A CA  1 
ATOM   3761 C C   . GLY A 1 475 ? -14.220 9.615   3.880   1.00 19.72  ? 475  GLY A C   1 
ATOM   3762 O O   . GLY A 1 475 ? -13.626 10.549  4.374   1.00 20.91  ? 475  GLY A O   1 
ATOM   3763 N N   . TYR A 1 476 ? -13.666 8.827   2.963   1.00 19.11  ? 476  TYR A N   1 
ATOM   3764 C CA  . TYR A 1 476 ? -12.397 9.165   2.355   1.00 19.85  ? 476  TYR A CA  1 
ATOM   3765 C C   . TYR A 1 476 ? -12.521 8.998   0.867   1.00 19.38  ? 476  TYR A C   1 
ATOM   3766 O O   . TYR A 1 476 ? -13.117 8.019   0.393   1.00 17.29  ? 476  TYR A O   1 
ATOM   3767 C CB  . TYR A 1 476 ? -11.252 8.258   2.840   1.00 22.02  ? 476  TYR A CB  1 
ATOM   3768 C CG  . TYR A 1 476 ? -10.961 8.361   4.322   1.00 23.92  ? 476  TYR A CG  1 
ATOM   3769 C CD1 . TYR A 1 476 ? -9.810  9.028   4.794   1.00 25.53  ? 476  TYR A CD1 1 
ATOM   3770 C CD2 . TYR A 1 476 ? -11.810 7.770   5.253   1.00 25.68  ? 476  TYR A CD2 1 
ATOM   3771 C CE1 . TYR A 1 476 ? -9.556  9.108   6.165   1.00 25.65  ? 476  TYR A CE1 1 
ATOM   3772 C CE2 . TYR A 1 476 ? -11.566 7.852   6.617   1.00 26.29  ? 476  TYR A CE2 1 
ATOM   3773 C CZ  . TYR A 1 476 ? -10.452 8.509   7.062   1.00 25.96  ? 476  TYR A CZ  1 
ATOM   3774 O OH  . TYR A 1 476 ? -10.235 8.582   8.422   1.00 27.54  ? 476  TYR A OH  1 
ATOM   3775 N N   . LEU A 1 477 ? -11.896 9.923   0.134   1.00 19.68  ? 477  LEU A N   1 
ATOM   3776 C CA  . LEU A 1 477 ? -12.036 9.987   -1.335  1.00 19.73  ? 477  LEU A CA  1 
ATOM   3777 C C   . LEU A 1 477 ? -11.457 8.763   -2.003  1.00 19.63  ? 477  LEU A C   1 
ATOM   3778 O O   . LEU A 1 477 ? -12.016 8.231   -2.981  1.00 18.19  ? 477  LEU A O   1 
ATOM   3779 C CB  . LEU A 1 477 ? -11.355 11.248  -1.868  1.00 19.61  ? 477  LEU A CB  1 
ATOM   3780 C CG  . LEU A 1 477 ? -12.027 12.579  -1.520  1.00 21.79  ? 477  LEU A CG  1 
ATOM   3781 C CD1 . LEU A 1 477 ? -11.128 13.730  -2.004  1.00 20.56  ? 477  LEU A CD1 1 
ATOM   3782 C CD2 . LEU A 1 477 ? -13.387 12.686  -2.163  1.00 20.46  ? 477  LEU A CD2 1 
ATOM   3783 N N   . PHE A 1 478 ? -10.374 8.251   -1.426  1.00 18.51  ? 478  PHE A N   1 
ATOM   3784 C CA  . PHE A 1 478 ? -9.631  7.204   -2.105  1.00 19.16  ? 478  PHE A CA  1 
ATOM   3785 C C   . PHE A 1 478 ? -10.153 5.835   -1.763  1.00 20.09  ? 478  PHE A C   1 
ATOM   3786 O O   . PHE A 1 478 ? -9.611  4.853   -2.230  1.00 19.66  ? 478  PHE A O   1 
ATOM   3787 C CB  . PHE A 1 478 ? -8.164  7.284   -1.733  1.00 19.69  ? 478  PHE A CB  1 
ATOM   3788 C CG  . PHE A 1 478 ? -7.944  7.383   -0.255  1.00 19.56  ? 478  PHE A CG  1 
ATOM   3789 C CD1 . PHE A 1 478 ? -7.990  6.249   0.542   1.00 23.36  ? 478  PHE A CD1 1 
ATOM   3790 C CD2 . PHE A 1 478 ? -7.684  8.611   0.343   1.00 19.58  ? 478  PHE A CD2 1 
ATOM   3791 C CE1 . PHE A 1 478 ? -7.812  6.338   1.927   1.00 19.37  ? 478  PHE A CE1 1 
ATOM   3792 C CE2 . PHE A 1 478 ? -7.491  8.700   1.735   1.00 17.11  ? 478  PHE A CE2 1 
ATOM   3793 C CZ  . PHE A 1 478 ? -7.553  7.556   2.509   1.00 16.26  ? 478  PHE A CZ  1 
ATOM   3794 N N   . CYS A 1 479 ? -11.217 5.754   -0.951  1.00 21.29  ? 479  CYS A N   1 
ATOM   3795 C CA  A CYS A 1 479 ? -11.773 4.454   -0.595  0.50 21.24  ? 479  CYS A CA  1 
ATOM   3796 C CA  B CYS A 1 479 ? -11.820 4.488   -0.580  0.50 21.73  ? 479  CYS A CA  1 
ATOM   3797 C C   . CYS A 1 479 ? -12.309 3.712   -1.813  1.00 21.48  ? 479  CYS A C   1 
ATOM   3798 O O   . CYS A 1 479 ? -13.115 4.245   -2.594  1.00 21.14  ? 479  CYS A O   1 
ATOM   3799 C CB  A CYS A 1 479 ? -12.866 4.580   0.470   0.50 21.63  ? 479  CYS A CB  1 
ATOM   3800 C CB  B CYS A 1 479 ? -13.005 4.761   0.353   0.50 22.18  ? 479  CYS A CB  1 
ATOM   3801 S SG  A CYS A 1 479 ? -12.180 4.782   2.110   0.50 23.14  ? 479  CYS A SG  1 
ATOM   3802 S SG  B CYS A 1 479 ? -13.788 3.308   0.957   0.50 26.42  ? 479  CYS A SG  1 
ATOM   3803 N N   . LYS A 1 480 ? -11.846 2.472   -1.956  1.00 20.96  ? 480  LYS A N   1 
ATOM   3804 C CA  . LYS A 1 480 ? -12.196 1.594   -3.088  1.00 21.48  ? 480  LYS A CA  1 
ATOM   3805 C C   . LYS A 1 480 ? -11.956 2.242   -4.462  1.00 20.59  ? 480  LYS A C   1 
ATOM   3806 O O   . LYS A 1 480 ? -12.656 1.929   -5.439  1.00 19.77  ? 480  LYS A O   1 
ATOM   3807 C CB  . LYS A 1 480 ? -13.640 1.042   -2.965  1.00 23.77  ? 480  LYS A CB  1 
ATOM   3808 C CG  . LYS A 1 480 ? -13.899 0.046   -1.786  1.00 26.38  ? 480  LYS A CG  1 
ATOM   3809 C CD  . LYS A 1 480 ? -12.736 -0.930  -1.521  1.00 30.75  ? 480  LYS A CD  1 
ATOM   3810 C CE  . LYS A 1 480 ? -13.012 -1.768  -0.254  1.00 32.84  ? 480  LYS A CE  1 
ATOM   3811 N NZ  . LYS A 1 480 ? -11.767 -1.960  0.579   1.00 38.53  ? 480  LYS A NZ  1 
ATOM   3812 N N   . THR A 1 481 ? -10.963 3.128   -4.548  1.00 18.55  ? 481  THR A N   1 
ATOM   3813 C CA  . THR A 1 481 ? -10.596 3.740   -5.845  1.00 18.25  ? 481  THR A CA  1 
ATOM   3814 C C   . THR A 1 481 ? -9.115  4.075   -5.873  1.00 18.52  ? 481  THR A C   1 
ATOM   3815 O O   . THR A 1 481 ? -8.393  3.520   -5.077  1.00 18.16  ? 481  THR A O   1 
ATOM   3816 C CB  . THR A 1 481 ? -11.500 4.950   -6.283  1.00 18.90  ? 481  THR A CB  1 
ATOM   3817 O OG1 . THR A 1 481 ? -11.131 5.330   -7.618  1.00 18.94  ? 481  THR A OG1 1 
ATOM   3818 C CG2 . THR A 1 481 ? -11.341 6.149   -5.355  1.00 18.06  ? 481  THR A CG2 1 
ATOM   3819 N N   . LEU A 1 482 ? -8.674  4.968   -6.772  1.00 18.52  ? 482  LEU A N   1 
ATOM   3820 C CA  . LEU A 1 482 ? -7.250  5.351   -6.888  1.00 19.76  ? 482  LEU A CA  1 
ATOM   3821 C C   . LEU A 1 482 ? -6.930  6.513   -5.944  1.00 19.49  ? 482  LEU A C   1 
ATOM   3822 O O   . LEU A 1 482 ? -7.845  7.262   -5.530  1.00 19.21  ? 482  LEU A O   1 
ATOM   3823 C CB  . LEU A 1 482 ? -6.908  5.713   -8.338  1.00 18.70  ? 482  LEU A CB  1 
ATOM   3824 C CG  . LEU A 1 482 ? -7.401  4.724   -9.396  1.00 21.10  ? 482  LEU A CG  1 
ATOM   3825 C CD1 . LEU A 1 482 ? -6.986  5.145   -10.785 1.00 22.69  ? 482  LEU A CD1 1 
ATOM   3826 C CD2 . LEU A 1 482 ? -6.927  3.292   -9.089  1.00 22.79  ? 482  LEU A CD2 1 
ATOM   3827 N N   . CYS A 1 483 ? -5.662  6.601   -5.518  1.00 19.79  ? 483  CYS A N   1 
ATOM   3828 C CA  . CYS A 1 483 ? -5.146  7.792   -4.891  1.00 20.32  ? 483  CYS A CA  1 
ATOM   3829 C C   . CYS A 1 483 ? -5.594  9.049   -5.645  1.00 20.03  ? 483  CYS A C   1 
ATOM   3830 O O   . CYS A 1 483 ? -5.574  9.085   -6.891  1.00 20.40  ? 483  CYS A O   1 
ATOM   3831 C CB  . CYS A 1 483 ? -3.604  7.762   -4.939  1.00 21.79  ? 483  CYS A CB  1 
ATOM   3832 S SG  . CYS A 1 483 ? -2.982  6.344   -4.015  1.00 31.41  ? 483  CYS A SG  1 
ATOM   3833 N N   . MET A 1 484 ? -5.990  10.074  -4.888  1.00 19.50  ? 484  MET A N   1 
ATOM   3834 C CA  . MET A 1 484 ? -6.434  11.365  -5.451  1.00 19.08  ? 484  MET A CA  1 
ATOM   3835 C C   . MET A 1 484 ? -5.272  12.148  -6.064  1.00 19.05  ? 484  MET A C   1 
ATOM   3836 O O   . MET A 1 484 ? -5.492  13.075  -6.837  1.00 19.84  ? 484  MET A O   1 
ATOM   3837 C CB  . MET A 1 484 ? -7.110  12.205  -4.383  1.00 17.98  ? 484  MET A CB  1 
ATOM   3838 C CG  . MET A 1 484 ? -8.452  11.655  -3.894  1.00 19.07  ? 484  MET A CG  1 
ATOM   3839 S SD  . MET A 1 484 ? -9.604  11.602  -5.309  1.00 19.89  ? 484  MET A SD  1 
ATOM   3840 C CE  . MET A 1 484 ? -9.784  9.871   -5.593  1.00 16.76  ? 484  MET A CE  1 
ATOM   3841 N N   . ASP A 1 485 ? -4.040  11.806  -5.690  1.00 20.24  ? 485  ASP A N   1 
ATOM   3842 C CA  . ASP A 1 485 ? -2.867  12.435  -6.304  1.00 20.74  ? 485  ASP A CA  1 
ATOM   3843 C C   . ASP A 1 485 ? -2.267  11.648  -7.484  1.00 21.06  ? 485  ASP A C   1 
ATOM   3844 O O   . ASP A 1 485 ? -1.224  12.027  -8.034  1.00 21.96  ? 485  ASP A O   1 
ATOM   3845 C CB  . ASP A 1 485 ? -1.810  12.843  -5.246  1.00 21.86  ? 485  ASP A CB  1 
ATOM   3846 C CG  . ASP A 1 485 ? -1.286  11.666  -4.409  1.00 23.35  ? 485  ASP A CG  1 
ATOM   3847 O OD1 . ASP A 1 485 ? -1.737  10.504  -4.592  1.00 23.33  ? 485  ASP A OD1 1 
ATOM   3848 O OD2 . ASP A 1 485 ? -0.415  11.922  -3.534  1.00 25.90  ? 485  ASP A OD2 1 
ATOM   3849 N N   . ALA A 1 486 ? -2.965  10.600  -7.909  1.00 20.50  ? 486  ALA A N   1 
ATOM   3850 C CA  . ALA A 1 486 ? -2.635  9.893   -9.134  1.00 20.22  ? 486  ALA A CA  1 
ATOM   3851 C C   . ALA A 1 486 ? -2.813  10.857  -10.307 1.00 21.04  ? 486  ALA A C   1 
ATOM   3852 O O   . ALA A 1 486 ? -3.575  11.841  -10.231 1.00 20.02  ? 486  ALA A O   1 
ATOM   3853 C CB  . ALA A 1 486 ? -3.505  8.623   -9.299  1.00 20.53  ? 486  ALA A CB  1 
ATOM   3854 N N   . VAL A 1 487 ? -2.087  10.567  -11.376 1.00 20.53  ? 487  VAL A N   1 
ATOM   3855 C CA  . VAL A 1 487 ? -1.807  11.508  -12.441 1.00 22.01  ? 487  VAL A CA  1 
ATOM   3856 C C   . VAL A 1 487 ? -2.235  10.913  -13.778 1.00 21.43  ? 487  VAL A C   1 
ATOM   3857 O O   . VAL A 1 487 ? -1.843  9.797   -14.130 1.00 21.03  ? 487  VAL A O   1 
ATOM   3858 C CB  . VAL A 1 487 ? -0.259  11.823  -12.418 1.00 22.42  ? 487  VAL A CB  1 
ATOM   3859 C CG1 . VAL A 1 487 ? 0.260   12.257  -13.751 1.00 24.88  ? 487  VAL A CG1 1 
ATOM   3860 C CG2 . VAL A 1 487 ? 0.008   12.905  -11.370 1.00 24.20  ? 487  VAL A CG2 1 
ATOM   3861 N N   . GLN A 1 488 ? -3.069  11.664  -14.503 1.00 20.90  ? 488  GLN A N   1 
ATOM   3862 C CA  . GLN A 1 488 ? -3.523  11.295  -15.831 1.00 20.17  ? 488  GLN A CA  1 
ATOM   3863 C C   . GLN A 1 488 ? -3.315  12.458  -16.800 1.00 20.53  ? 488  GLN A C   1 
ATOM   3864 O O   . GLN A 1 488 ? -3.031  13.587  -16.391 1.00 20.97  ? 488  GLN A O   1 
ATOM   3865 C CB  . GLN A 1 488 ? -5.005  10.943  -15.765 1.00 20.30  ? 488  GLN A CB  1 
ATOM   3866 C CG  . GLN A 1 488 ? -5.236  9.566   -15.163 1.00 21.20  ? 488  GLN A CG  1 
ATOM   3867 C CD  . GLN A 1 488 ? -6.707  9.178   -15.081 1.00 24.66  ? 488  GLN A CD  1 
ATOM   3868 O OE1 . GLN A 1 488 ? -7.302  8.714   -16.054 1.00 29.10  ? 488  GLN A OE1 1 
ATOM   3869 N NE2 . GLN A 1 488 ? -7.276  9.325   -13.912 1.00 24.78  ? 488  GLN A NE2 1 
ATOM   3870 N N   . HIS A 1 489 ? -3.434  12.186  -18.090 1.00 21.24  ? 489  HIS A N   1 
ATOM   3871 C CA  . HIS A 1 489 ? -3.328  13.256  -19.116 1.00 22.01  ? 489  HIS A CA  1 
ATOM   3872 C C   . HIS A 1 489 ? -4.203  14.512  -18.814 1.00 22.03  ? 489  HIS A C   1 
ATOM   3873 O O   . HIS A 1 489 ? -3.700  15.620  -18.856 1.00 21.84  ? 489  HIS A O   1 
ATOM   3874 C CB  . HIS A 1 489 ? -3.574  12.679  -20.520 1.00 22.98  ? 489  HIS A CB  1 
ATOM   3875 C CG  . HIS A 1 489 ? -3.465  13.693  -21.604 1.00 26.03  ? 489  HIS A CG  1 
ATOM   3876 N ND1 . HIS A 1 489 ? -4.547  14.094  -22.361 1.00 29.09  ? 489  HIS A ND1 1 
ATOM   3877 C CD2 . HIS A 1 489 ? -2.408  14.428  -22.030 1.00 28.97  ? 489  HIS A CD2 1 
ATOM   3878 C CE1 . HIS A 1 489 ? -4.160  15.024  -23.218 1.00 28.82  ? 489  HIS A CE1 1 
ATOM   3879 N NE2 . HIS A 1 489 ? -2.869  15.248  -23.034 1.00 30.73  ? 489  HIS A NE2 1 
ATOM   3880 N N   . TRP A 1 490 ? -5.487  14.355  -18.446 1.00 21.67  ? 490  TRP A N   1 
ATOM   3881 C CA  . TRP A 1 490 ? -6.295  15.519  -18.105 1.00 21.51  ? 490  TRP A CA  1 
ATOM   3882 C C   . TRP A 1 490 ? -6.045  16.163  -16.748 1.00 21.93  ? 490  TRP A C   1 
ATOM   3883 O O   . TRP A 1 490 ? -6.573  17.236  -16.493 1.00 22.64  ? 490  TRP A O   1 
ATOM   3884 C CB  . TRP A 1 490 ? -7.804  15.206  -18.146 1.00 20.45  ? 490  TRP A CB  1 
ATOM   3885 C CG  . TRP A 1 490 ? -8.380  14.960  -19.489 1.00 21.56  ? 490  TRP A CG  1 
ATOM   3886 C CD1 . TRP A 1 490 ? -7.796  15.203  -20.707 1.00 22.18  ? 490  TRP A CD1 1 
ATOM   3887 C CD2 . TRP A 1 490 ? -9.701  14.467  -19.768 1.00 21.78  ? 490  TRP A CD2 1 
ATOM   3888 N NE1 . TRP A 1 490 ? -8.644  14.831  -21.717 1.00 21.62  ? 490  TRP A NE1 1 
ATOM   3889 C CE2 . TRP A 1 490 ? -9.819  14.368  -21.170 1.00 23.29  ? 490  TRP A CE2 1 
ATOM   3890 C CE3 . TRP A 1 490 ? -10.766 14.030  -18.962 1.00 23.40  ? 490  TRP A CE3 1 
ATOM   3891 C CZ2 . TRP A 1 490 ? -10.983 13.913  -21.794 1.00 22.27  ? 490  TRP A CZ2 1 
ATOM   3892 C CZ3 . TRP A 1 490 ? -11.927 13.569  -19.588 1.00 22.66  ? 490  TRP A CZ3 1 
ATOM   3893 C CH2 . TRP A 1 490 ? -12.015 13.506  -20.987 1.00 22.19  ? 490  TRP A CH2 1 
ATOM   3894 N N   . GLY A 1 491 ? -5.347  15.492  -15.838 1.00 21.56  ? 491  GLY A N   1 
ATOM   3895 C CA  . GLY A 1 491 ? -5.028  16.100  -14.552 1.00 21.22  ? 491  GLY A CA  1 
ATOM   3896 C C   . GLY A 1 491 ? -4.912  15.072  -13.456 1.00 21.38  ? 491  GLY A C   1 
ATOM   3897 O O   . GLY A 1 491 ? -4.740  13.891  -13.723 1.00 22.08  ? 491  GLY A O   1 
ATOM   3898 N N   . LYS A 1 492 ? -5.021  15.516  -12.212 1.00 21.92  ? 492  LYS A N   1 
ATOM   3899 C CA  . LYS A 1 492 ? -4.887  14.613  -11.091 1.00 22.48  ? 492  LYS A CA  1 
ATOM   3900 C C   . LYS A 1 492 ? -6.227  13.952  -10.805 1.00 21.16  ? 492  LYS A C   1 
ATOM   3901 O O   . LYS A 1 492 ? -7.294  14.526  -11.098 1.00 20.41  ? 492  LYS A O   1 
ATOM   3902 C CB  . LYS A 1 492 ? -4.294  15.350  -9.874  1.00 23.03  ? 492  LYS A CB  1 
ATOM   3903 C CG  . LYS A 1 492 ? -2.769  15.588  -10.054 1.00 25.20  ? 492  LYS A CG  1 
ATOM   3904 C CD  . LYS A 1 492 ? -2.056  16.140  -8.807  1.00 26.22  ? 492  LYS A CD  1 
ATOM   3905 C CE  . LYS A 1 492 ? -0.476  15.967  -8.892  1.00 29.99  ? 492  LYS A CE  1 
ATOM   3906 N NZ  . LYS A 1 492 ? 0.030   14.706  -8.149  1.00 30.13  ? 492  LYS A NZ  1 
ATOM   3907 N N   . GLN A 1 493 ? -6.179  12.750  -10.242 1.00 19.38  ? 493  GLN A N   1 
ATOM   3908 C CA  . GLN A 1 493 ? -7.410  12.023  -9.921  1.00 20.40  ? 493  GLN A CA  1 
ATOM   3909 C C   . GLN A 1 493 ? -8.413  12.862  -9.100  1.00 19.43  ? 493  GLN A C   1 
ATOM   3910 O O   . GLN A 1 493 ? -9.624  12.744  -9.293  1.00 20.08  ? 493  GLN A O   1 
ATOM   3911 C CB  . GLN A 1 493 ? -7.002  10.708  -9.256  1.00 21.38  ? 493  GLN A CB  1 
ATOM   3912 C CG  . GLN A 1 493 ? -8.083  9.795   -8.805  1.00 23.56  ? 493  GLN A CG  1 
ATOM   3913 C CD  . GLN A 1 493 ? -8.761  9.020   -9.930  1.00 25.92  ? 493  GLN A CD  1 
ATOM   3914 O OE1 . GLN A 1 493 ? -8.346  9.038   -11.100 1.00 25.29  ? 493  GLN A OE1 1 
ATOM   3915 N NE2 . GLN A 1 493 ? -9.815  8.322   -9.559  1.00 24.28  ? 493  GLN A NE2 1 
ATOM   3916 N N   . TYR A 1 494 ? -7.918  13.701  -8.190  1.00 17.75  ? 494  TYR A N   1 
ATOM   3917 C CA  . TYR A 1 494 ? -8.762  14.603  -7.388  1.00 18.75  ? 494  TYR A CA  1 
ATOM   3918 C C   . TYR A 1 494 ? -9.802  15.326  -8.251  1.00 19.64  ? 494  TYR A C   1 
ATOM   3919 O O   . TYR A 1 494 ? -10.971 15.494  -7.856  1.00 19.40  ? 494  TYR A O   1 
ATOM   3920 C CB  . TYR A 1 494 ? -7.875  15.649  -6.706  1.00 17.20  ? 494  TYR A CB  1 
ATOM   3921 C CG  . TYR A 1 494 ? -8.563  16.536  -5.711  1.00 15.87  ? 494  TYR A CG  1 
ATOM   3922 C CD1 . TYR A 1 494 ? -8.789  16.098  -4.396  1.00 15.01  ? 494  TYR A CD1 1 
ATOM   3923 C CD2 . TYR A 1 494 ? -9.026  17.797  -6.079  1.00 17.29  ? 494  TYR A CD2 1 
ATOM   3924 C CE1 . TYR A 1 494 ? -9.403  16.916  -3.453  1.00 15.43  ? 494  TYR A CE1 1 
ATOM   3925 C CE2 . TYR A 1 494 ? -9.644  18.608  -5.166  1.00 17.42  ? 494  TYR A CE2 1 
ATOM   3926 C CZ  . TYR A 1 494 ? -9.843  18.159  -3.847  1.00 18.32  ? 494  TYR A CZ  1 
ATOM   3927 O OH  . TYR A 1 494 ? -10.414 19.001  -2.923  1.00 16.13  ? 494  TYR A OH  1 
ATOM   3928 N N   . ASP A 1 495 ? -9.339  15.776  -9.416  1.00 19.67  ? 495  ASP A N   1 
ATOM   3929 C CA  . ASP A 1 495 ? -10.145 16.575  -10.337 1.00 19.93  ? 495  ASP A CA  1 
ATOM   3930 C C   . ASP A 1 495 ? -10.913 15.720  -11.344 1.00 20.73  ? 495  ASP A C   1 
ATOM   3931 O O   . ASP A 1 495 ? -12.029 16.090  -11.733 1.00 21.53  ? 495  ASP A O   1 
ATOM   3932 C CB  . ASP A 1 495 ? -9.239  17.557  -11.101 1.00 20.02  ? 495  ASP A CB  1 
ATOM   3933 C CG  . ASP A 1 495 ? -8.731  18.705  -10.236 1.00 22.31  ? 495  ASP A CG  1 
ATOM   3934 O OD1 . ASP A 1 495 ? -9.490  19.227  -9.352  1.00 23.81  ? 495  ASP A OD1 1 
ATOM   3935 O OD2 . ASP A 1 495 ? -7.539  19.096  -10.454 1.00 22.42  ? 495  ASP A OD2 1 
ATOM   3936 N N   . ILE A 1 496 ? -10.325 14.594  -11.770 1.00 19.48  ? 496  ILE A N   1 
ATOM   3937 C CA  . ILE A 1 496 ? -10.883 13.838  -12.901 1.00 20.01  ? 496  ILE A CA  1 
ATOM   3938 C C   . ILE A 1 496 ? -11.509 12.501  -12.543 1.00 18.18  ? 496  ILE A C   1 
ATOM   3939 O O   . ILE A 1 496 ? -12.001 11.784  -13.428 1.00 19.43  ? 496  ILE A O   1 
ATOM   3940 C CB  . ILE A 1 496 ? -9.881  13.690  -14.070 1.00 21.21  ? 496  ILE A CB  1 
ATOM   3941 C CG1 . ILE A 1 496 ? -8.667  12.918  -13.625 1.00 22.67  ? 496  ILE A CG1 1 
ATOM   3942 C CG2 . ILE A 1 496 ? -9.438  15.052  -14.613 1.00 20.95  ? 496  ILE A CG2 1 
ATOM   3943 C CD1 . ILE A 1 496 ? -7.991  12.301  -14.765 1.00 26.82  ? 496  ILE A CD1 1 
ATOM   3944 N N   . HIS A 1 497 ? -11.540 12.176  -11.249 1.00 17.62  ? 497  HIS A N   1 
ATOM   3945 C CA  . HIS A 1 497 ? -12.055 10.883  -10.789 1.00 16.24  ? 497  HIS A CA  1 
ATOM   3946 C C   . HIS A 1 497 ? -13.478 10.633  -11.356 1.00 15.83  ? 497  HIS A C   1 
ATOM   3947 O O   . HIS A 1 497 ? -13.755 9.547   -11.860 1.00 15.85  ? 497  HIS A O   1 
ATOM   3948 C CB  . HIS A 1 497 ? -12.118 10.849  -9.273  1.00 15.97  ? 497  HIS A CB  1 
ATOM   3949 C CG  . HIS A 1 497 ? -12.786 9.633   -8.727  1.00 16.52  ? 497  HIS A CG  1 
ATOM   3950 N ND1 . HIS A 1 497 ? -14.154 9.566   -8.504  1.00 17.45  ? 497  HIS A ND1 1 
ATOM   3951 C CD2 . HIS A 1 497 ? -12.289 8.427   -8.387  1.00 13.37  ? 497  HIS A CD2 1 
ATOM   3952 C CE1 . HIS A 1 497 ? -14.451 8.387   -7.996  1.00 13.57  ? 497  HIS A CE1 1 
ATOM   3953 N NE2 . HIS A 1 497 ? -13.341 7.674   -7.927  1.00 21.43  ? 497  HIS A NE2 1 
ATOM   3954 N N   . ASN A 1 498 ? -14.349 11.634  -11.281 1.00 16.30  ? 498  ASN A N   1 
ATOM   3955 C CA  . ASN A 1 498 ? -15.730 11.449  -11.780 1.00 16.47  ? 498  ASN A CA  1 
ATOM   3956 C C   . ASN A 1 498 ? -15.799 11.331  -13.300 1.00 17.19  ? 498  ASN A C   1 
ATOM   3957 O O   . ASN A 1 498 ? -16.853 11.122  -13.867 1.00 16.50  ? 498  ASN A O   1 
ATOM   3958 C CB  . ASN A 1 498 ? -16.616 12.610  -11.307 1.00 16.10  ? 498  ASN A CB  1 
ATOM   3959 C CG  . ASN A 1 498 ? -17.037 12.486  -9.860  1.00 17.62  ? 498  ASN A CG  1 
ATOM   3960 O OD1 . ASN A 1 498 ? -17.631 13.411  -9.267  1.00 22.45  ? 498  ASN A OD1 1 
ATOM   3961 N ND2 . ASN A 1 498 ? -16.775 11.367  -9.289  1.00 16.65  ? 498  ASN A ND2 1 
ATOM   3962 N N   . LEU A 1 499 ? -14.673 11.527  -13.971 1.00 15.77  ? 499  LEU A N   1 
ATOM   3963 C CA  . LEU A 1 499 ? -14.599 11.433  -15.423 1.00 17.02  ? 499  LEU A CA  1 
ATOM   3964 C C   . LEU A 1 499 ? -13.995 10.149  -15.954 1.00 17.61  ? 499  LEU A C   1 
ATOM   3965 O O   . LEU A 1 499 ? -13.801 10.011  -17.160 1.00 17.35  ? 499  LEU A O   1 
ATOM   3966 C CB  . LEU A 1 499 ? -13.825 12.636  -16.011 1.00 16.49  ? 499  LEU A CB  1 
ATOM   3967 C CG  . LEU A 1 499 ? -14.305 14.055  -15.632 1.00 17.14  ? 499  LEU A CG  1 
ATOM   3968 C CD1 . LEU A 1 499 ? -13.432 15.166  -16.217 1.00 16.41  ? 499  LEU A CD1 1 
ATOM   3969 C CD2 . LEU A 1 499 ? -15.795 14.257  -16.063 1.00 16.16  ? 499  LEU A CD2 1 
ATOM   3970 N N   . TYR A 1 500 ? -13.635 9.219   -15.072 1.00 17.69  ? 500  TYR A N   1 
ATOM   3971 C CA  . TYR A 1 500 ? -12.988 7.997   -15.558 1.00 17.44  ? 500  TYR A CA  1 
ATOM   3972 C C   . TYR A 1 500 ? -13.910 7.145   -16.410 1.00 17.14  ? 500  TYR A C   1 
ATOM   3973 O O   . TYR A 1 500 ? -13.524 6.702   -17.492 1.00 18.62  ? 500  TYR A O   1 
ATOM   3974 C CB  . TYR A 1 500 ? -12.405 7.166   -14.402 1.00 17.83  ? 500  TYR A CB  1 
ATOM   3975 C CG  . TYR A 1 500 ? -11.468 6.079   -14.861 1.00 16.52  ? 500  TYR A CG  1 
ATOM   3976 C CD1 . TYR A 1 500 ? -10.105 6.266   -14.822 1.00 17.55  ? 500  TYR A CD1 1 
ATOM   3977 C CD2 . TYR A 1 500 ? -11.943 4.864   -15.333 1.00 15.13  ? 500  TYR A CD2 1 
ATOM   3978 C CE1 . TYR A 1 500 ? -9.243  5.288   -15.259 1.00 16.81  ? 500  TYR A CE1 1 
ATOM   3979 C CE2 . TYR A 1 500 ? -11.087 3.865   -15.773 1.00 16.14  ? 500  TYR A CE2 1 
ATOM   3980 C CZ  . TYR A 1 500 ? -9.715  4.105   -15.723 1.00 17.82  ? 500  TYR A CZ  1 
ATOM   3981 O OH  . TYR A 1 500 ? -8.821  3.167   -16.125 1.00 19.77  ? 500  TYR A OH  1 
ATOM   3982 N N   . GLY A 1 501 ? -15.127 6.890   -15.938 1.00 17.61  ? 501  GLY A N   1 
ATOM   3983 C CA  . GLY A 1 501 ? -16.006 6.046   -16.712 1.00 16.91  ? 501  GLY A CA  1 
ATOM   3984 C C   . GLY A 1 501 ? -16.444 6.750   -17.977 1.00 16.99  ? 501  GLY A C   1 
ATOM   3985 O O   . GLY A 1 501 ? -16.682 6.116   -18.995 1.00 17.81  ? 501  GLY A O   1 
ATOM   3986 N N   . TYR A 1 502 ? -16.585 8.063   -17.897 1.00 16.88  ? 502  TYR A N   1 
ATOM   3987 C CA  . TYR A 1 502 ? -16.910 8.877   -19.083 1.00 16.94  ? 502  TYR A CA  1 
ATOM   3988 C C   . TYR A 1 502 ? -15.762 8.759   -20.114 1.00 16.60  ? 502  TYR A C   1 
ATOM   3989 O O   . TYR A 1 502 ? -15.998 8.435   -21.259 1.00 16.24  ? 502  TYR A O   1 
ATOM   3990 C CB  . TYR A 1 502 ? -17.151 10.310  -18.626 1.00 16.58  ? 502  TYR A CB  1 
ATOM   3991 C CG  . TYR A 1 502 ? -17.268 11.354  -19.706 1.00 17.12  ? 502  TYR A CG  1 
ATOM   3992 C CD1 . TYR A 1 502 ? -18.466 11.548  -20.381 1.00 16.51  ? 502  TYR A CD1 1 
ATOM   3993 C CD2 . TYR A 1 502 ? -16.174 12.191  -20.029 1.00 18.17  ? 502  TYR A CD2 1 
ATOM   3994 C CE1 . TYR A 1 502 ? -18.574 12.504  -21.377 1.00 17.62  ? 502  TYR A CE1 1 
ATOM   3995 C CE2 . TYR A 1 502 ? -16.287 13.173  -21.008 1.00 16.99  ? 502  TYR A CE2 1 
ATOM   3996 C CZ  . TYR A 1 502 ? -17.513 13.325  -21.668 1.00 20.13  ? 502  TYR A CZ  1 
ATOM   3997 O OH  . TYR A 1 502 ? -17.663 14.283  -22.637 1.00 20.95  ? 502  TYR A OH  1 
ATOM   3998 N N   . SER A 1 503 ? -14.513 8.948   -19.694 1.00 16.47  ? 503  SER A N   1 
ATOM   3999 C CA  . SER A 1 503 ? -13.401 8.855   -20.650 1.00 16.53  ? 503  SER A CA  1 
ATOM   4000 C C   . SER A 1 503 ? -13.290 7.447   -21.239 1.00 17.04  ? 503  SER A C   1 
ATOM   4001 O O   . SER A 1 503 ? -12.960 7.269   -22.417 1.00 16.57  ? 503  SER A O   1 
ATOM   4002 C CB  . SER A 1 503 ? -12.095 9.318   -19.980 1.00 16.95  ? 503  SER A CB  1 
ATOM   4003 O OG  . SER A 1 503 ? -11.784 8.422   -18.933 1.00 15.70  ? 503  SER A OG  1 
ATOM   4004 N N   . MET A 1 504 ? -13.563 6.426   -20.421 1.00 17.21  ? 504  MET A N   1 
ATOM   4005 C CA  . MET A 1 504 ? -13.532 5.060   -20.865 1.00 17.43  ? 504  MET A CA  1 
ATOM   4006 C C   . MET A 1 504 ? -14.638 4.807   -21.924 1.00 16.97  ? 504  MET A C   1 
ATOM   4007 O O   . MET A 1 504 ? -14.387 4.138   -22.921 1.00 15.24  ? 504  MET A O   1 
ATOM   4008 C CB  . MET A 1 504 ? -13.674 4.092   -19.678 1.00 17.82  ? 504  MET A CB  1 
ATOM   4009 C CG  . MET A 1 504 ? -13.513 2.633   -20.084 1.00 18.26  ? 504  MET A CG  1 
ATOM   4010 S SD  . MET A 1 504 ? -13.763 1.521   -18.694 1.00 18.58  ? 504  MET A SD  1 
ATOM   4011 C CE  . MET A 1 504 ? -13.398 -0.053  -19.493 1.00 19.15  ? 504  MET A CE  1 
ATOM   4012 N N   . ALA A 1 505 ? -15.845 5.319   -21.689 1.00 16.66  ? 505  ALA A N   1 
ATOM   4013 C CA  . ALA A 1 505 ? -16.922 5.178   -22.705 1.00 16.75  ? 505  ALA A CA  1 
ATOM   4014 C C   . ALA A 1 505 ? -16.526 5.870   -24.019 1.00 17.90  ? 505  ALA A C   1 
ATOM   4015 O O   . ALA A 1 505 ? -16.731 5.291   -25.102 1.00 18.26  ? 505  ALA A O   1 
ATOM   4016 C CB  . ALA A 1 505 ? -18.304 5.720   -22.174 1.00 15.85  ? 505  ALA A CB  1 
ATOM   4017 N N   . VAL A 1 506 ? -15.888 7.043   -23.926 1.00 18.41  ? 506  VAL A N   1 
ATOM   4018 C CA  . VAL A 1 506 ? -15.462 7.777   -25.133 1.00 19.12  ? 506  VAL A CA  1 
ATOM   4019 C C   . VAL A 1 506 ? -14.435 6.951   -25.935 1.00 20.14  ? 506  VAL A C   1 
ATOM   4020 O O   . VAL A 1 506 ? -14.568 6.777   -27.163 1.00 18.67  ? 506  VAL A O   1 
ATOM   4021 C CB  . VAL A 1 506 ? -14.911 9.205   -24.776 1.00 19.43  ? 506  VAL A CB  1 
ATOM   4022 C CG1 . VAL A 1 506 ? -14.196 9.855   -25.972 1.00 20.29  ? 506  VAL A CG1 1 
ATOM   4023 C CG2 . VAL A 1 506 ? -16.043 10.125  -24.230 1.00 19.30  ? 506  VAL A CG2 1 
ATOM   4024 N N   . ALA A 1 507 ? -13.418 6.429   -25.219 1.00 20.22  ? 507  ALA A N   1 
ATOM   4025 C CA  . ALA A 1 507 ? -12.407 5.522   -25.788 1.00 20.05  ? 507  ALA A CA  1 
ATOM   4026 C C   . ALA A 1 507 ? -13.006 4.266   -26.361 1.00 19.80  ? 507  ALA A C   1 
ATOM   4027 O O   . ALA A 1 507 ? -12.539 3.763   -27.366 1.00 20.53  ? 507  ALA A O   1 
ATOM   4028 C CB  . ALA A 1 507 ? -11.393 5.136   -24.691 1.00 19.95  ? 507  ALA A CB  1 
ATOM   4029 N N   . THR A 1 508 ? -13.998 3.704   -25.680 1.00 19.81  ? 508  THR A N   1 
ATOM   4030 C CA  . THR A 1 508 ? -14.624 2.474   -26.135 1.00 19.91  ? 508  THR A CA  1 
ATOM   4031 C C   . THR A 1 508 ? -15.408 2.726   -27.438 1.00 20.29  ? 508  THR A C   1 
ATOM   4032 O O   . THR A 1 508 ? -15.329 1.930   -28.378 1.00 19.70  ? 508  THR A O   1 
ATOM   4033 C CB  . THR A 1 508 ? -15.467 1.816   -25.005 1.00 20.20  ? 508  THR A CB  1 
ATOM   4034 O OG1 . THR A 1 508 ? -14.585 1.501   -23.913 1.00 19.72  ? 508  THR A OG1 1 
ATOM   4035 C CG2 . THR A 1 508 ? -16.130 0.535   -25.462 1.00 18.21  ? 508  THR A CG2 1 
ATOM   4036 N N   . ALA A 1 509 ? -16.141 3.828   -27.496 1.00 20.44  ? 509  ALA A N   1 
ATOM   4037 C CA  . ALA A 1 509 ? -16.819 4.229   -28.751 1.00 21.33  ? 509  ALA A CA  1 
ATOM   4038 C C   . ALA A 1 509 ? -15.768 4.436   -29.870 1.00 22.24  ? 509  ALA A C   1 
ATOM   4039 O O   . ALA A 1 509 ? -15.939 3.982   -31.009 1.00 21.90  ? 509  ALA A O   1 
ATOM   4040 C CB  . ALA A 1 509 ? -17.623 5.492   -28.537 1.00 21.97  ? 509  ALA A CB  1 
ATOM   4041 N N   . GLU A 1 510 ? -14.656 5.068   -29.531 1.00 22.99  ? 510  GLU A N   1 
ATOM   4042 C CA  . GLU A 1 510 ? -13.566 5.223   -30.495 1.00 24.63  ? 510  GLU A CA  1 
ATOM   4043 C C   . GLU A 1 510 ? -13.122 3.861   -31.021 1.00 23.33  ? 510  GLU A C   1 
ATOM   4044 O O   . GLU A 1 510 ? -12.968 3.697   -32.239 1.00 23.73  ? 510  GLU A O   1 
ATOM   4045 C CB  . GLU A 1 510 ? -12.403 6.016   -29.868 1.00 25.38  ? 510  GLU A CB  1 
ATOM   4046 C CG  . GLU A 1 510 ? -11.294 6.472   -30.834 1.00 32.62  ? 510  GLU A CG  1 
ATOM   4047 C CD  . GLU A 1 510 ? -11.767 7.489   -31.902 1.00 41.00  ? 510  GLU A CD  1 
ATOM   4048 O OE1 . GLU A 1 510 ? -12.720 8.273   -31.647 1.00 44.06  ? 510  GLU A OE1 1 
ATOM   4049 O OE2 . GLU A 1 510 ? -11.176 7.495   -33.011 1.00 45.93  ? 510  GLU A OE2 1 
ATOM   4050 N N   . ALA A 1 511 ? -12.946 2.877   -30.125 1.00 22.69  ? 511  ALA A N   1 
ATOM   4051 C CA  . ALA A 1 511 ? -12.561 1.521   -30.507 1.00 21.98  ? 511  ALA A CA  1 
ATOM   4052 C C   . ALA A 1 511 ? -13.597 0.866   -31.438 1.00 22.19  ? 511  ALA A C   1 
ATOM   4053 O O   . ALA A 1 511 ? -13.243 0.125   -32.381 1.00 20.94  ? 511  ALA A O   1 
ATOM   4054 C CB  . ALA A 1 511 ? -12.328 0.638   -29.250 1.00 22.31  ? 511  ALA A CB  1 
ATOM   4055 N N   . ALA A 1 512 ? -14.883 1.122   -31.172 1.00 21.80  ? 512  ALA A N   1 
ATOM   4056 C CA  . ALA A 1 512 ? -15.945 0.583   -31.990 1.00 22.84  ? 512  ALA A CA  1 
ATOM   4057 C C   . ALA A 1 512 ? -15.843 1.038   -33.454 1.00 23.24  ? 512  ALA A C   1 
ATOM   4058 O O   . ALA A 1 512 ? -16.248 0.302   -34.352 1.00 24.32  ? 512  ALA A O   1 
ATOM   4059 C CB  . ALA A 1 512 ? -17.354 0.953   -31.386 1.00 22.12  ? 512  ALA A CB  1 
ATOM   4060 N N   . LYS A 1 513 ? -15.308 2.229   -33.695 1.00 24.60  ? 513  LYS A N   1 
ATOM   4061 C CA  . LYS A 1 513 ? -15.127 2.744   -35.065 1.00 26.67  ? 513  LYS A CA  1 
ATOM   4062 C C   . LYS A 1 513 ? -14.270 1.804   -35.904 1.00 26.51  ? 513  LYS A C   1 
ATOM   4063 O O   . LYS A 1 513 ? -14.432 1.731   -37.121 1.00 26.87  ? 513  LYS A O   1 
ATOM   4064 C CB  . LYS A 1 513 ? -14.448 4.119   -35.077 1.00 26.50  ? 513  LYS A CB  1 
ATOM   4065 C CG  . LYS A 1 513 ? -15.212 5.261   -34.435 1.00 27.79  ? 513  LYS A CG  1 
ATOM   4066 C CD  . LYS A 1 513 ? -14.423 6.561   -34.600 1.00 29.00  ? 513  LYS A CD  1 
ATOM   4067 C CE  . LYS A 1 513 ? -15.160 7.736   -33.970 1.00 34.03  ? 513  LYS A CE  1 
ATOM   4068 N NZ  . LYS A 1 513 ? -14.330 8.988   -34.053 1.00 39.20  ? 513  LYS A NZ  1 
ATOM   4069 N N   . THR A 1 514 ? -13.332 1.112   -35.258 1.00 26.68  ? 514  THR A N   1 
ATOM   4070 C CA  . THR A 1 514 ? -12.412 0.200   -35.955 1.00 24.96  ? 514  THR A CA  1 
ATOM   4071 C C   . THR A 1 514 ? -12.930 -1.209  -35.921 1.00 24.38  ? 514  THR A C   1 
ATOM   4072 O O   . THR A 1 514 ? -12.933 -1.900  -36.939 1.00 23.73  ? 514  THR A O   1 
ATOM   4073 C CB  . THR A 1 514 ? -11.009 0.253   -35.310 1.00 26.20  ? 514  THR A CB  1 
ATOM   4074 O OG1 . THR A 1 514 ? -10.426 1.508   -35.623 1.00 25.74  ? 514  THR A OG1 1 
ATOM   4075 C CG2 . THR A 1 514 ? -10.097 -0.833  -35.857 1.00 27.40  ? 514  THR A CG2 1 
ATOM   4076 N N   . VAL A 1 515 ? -13.401 -1.646  -34.748 1.00 22.17  ? 515  VAL A N   1 
ATOM   4077 C CA  . VAL A 1 515 ? -13.785 -3.040  -34.570 1.00 22.86  ? 515  VAL A CA  1 
ATOM   4078 C C   . VAL A 1 515 ? -15.146 -3.338  -35.264 1.00 22.13  ? 515  VAL A C   1 
ATOM   4079 O O   . VAL A 1 515 ? -15.373 -4.430  -35.800 1.00 21.67  ? 515  VAL A O   1 
ATOM   4080 C CB  . VAL A 1 515 ? -13.852 -3.366  -33.069 1.00 22.96  ? 515  VAL A CB  1 
ATOM   4081 C CG1 . VAL A 1 515 ? -14.499 -4.742  -32.818 1.00 24.38  ? 515  VAL A CG1 1 
ATOM   4082 C CG2 . VAL A 1 515 ? -12.457 -3.268  -32.457 1.00 24.59  ? 515  VAL A CG2 1 
ATOM   4083 N N   . PHE A 1 516 ? -16.024 -2.346  -35.269 1.00 22.06  ? 516  PHE A N   1 
ATOM   4084 C CA  . PHE A 1 516 ? -17.371 -2.490  -35.879 1.00 22.46  ? 516  PHE A CA  1 
ATOM   4085 C C   . PHE A 1 516 ? -17.571 -1.394  -36.925 1.00 23.47  ? 516  PHE A C   1 
ATOM   4086 O O   . PHE A 1 516 ? -18.305 -0.437  -36.679 1.00 22.68  ? 516  PHE A O   1 
ATOM   4087 C CB  . PHE A 1 516 ? -18.455 -2.365  -34.794 1.00 23.08  ? 516  PHE A CB  1 
ATOM   4088 C CG  . PHE A 1 516 ? -18.341 -3.397  -33.718 1.00 22.35  ? 516  PHE A CG  1 
ATOM   4089 C CD1 . PHE A 1 516 ? -18.484 -4.748  -34.017 1.00 23.84  ? 516  PHE A CD1 1 
ATOM   4090 C CD2 . PHE A 1 516 ? -18.069 -3.019  -32.415 1.00 21.76  ? 516  PHE A CD2 1 
ATOM   4091 C CE1 . PHE A 1 516 ? -18.360 -5.702  -33.011 1.00 26.74  ? 516  PHE A CE1 1 
ATOM   4092 C CE2 . PHE A 1 516 ? -17.957 -3.961  -31.403 1.00 22.42  ? 516  PHE A CE2 1 
ATOM   4093 C CZ  . PHE A 1 516 ? -18.099 -5.289  -31.693 1.00 22.85  ? 516  PHE A CZ  1 
ATOM   4094 N N   . PRO A 1 517 ? -16.870 -1.486  -38.069 1.00 24.30  ? 517  PRO A N   1 
ATOM   4095 C CA  . PRO A 1 517 ? -16.874 -0.331  -38.967 1.00 25.34  ? 517  PRO A CA  1 
ATOM   4096 C C   . PRO A 1 517 ? -18.274 0.039   -39.440 1.00 24.89  ? 517  PRO A C   1 
ATOM   4097 O O   . PRO A 1 517 ? -18.999 -0.818  -39.920 1.00 24.56  ? 517  PRO A O   1 
ATOM   4098 C CB  . PRO A 1 517 ? -16.000 -0.804  -40.154 1.00 25.31  ? 517  PRO A CB  1 
ATOM   4099 C CG  . PRO A 1 517 ? -15.090 -1.768  -39.556 1.00 24.94  ? 517  PRO A CG  1 
ATOM   4100 C CD  . PRO A 1 517 ? -15.982 -2.544  -38.586 1.00 25.12  ? 517  PRO A CD  1 
ATOM   4101 N N   . ASN A 1 518 ? -18.609 1.308   -39.250 1.00 25.28  ? 518  ASN A N   1 
ATOM   4102 C CA  . ASN A 1 518 ? -19.900 1.908   -39.590 1.00 26.32  ? 518  ASN A CA  1 
ATOM   4103 C C   . ASN A 1 518 ? -21.127 1.364   -38.887 1.00 25.26  ? 518  ASN A C   1 
ATOM   4104 O O   . ASN A 1 518 ? -22.230 1.625   -39.344 1.00 25.59  ? 518  ASN A O   1 
ATOM   4105 C CB  . ASN A 1 518 ? -20.121 1.888   -41.102 1.00 27.89  ? 518  ASN A CB  1 
ATOM   4106 C CG  . ASN A 1 518 ? -19.067 2.682   -41.825 1.00 31.90  ? 518  ASN A CG  1 
ATOM   4107 O OD1 . ASN A 1 518 ? -18.918 3.891   -41.592 1.00 36.88  ? 518  ASN A OD1 1 
ATOM   4108 N ND2 . ASN A 1 518 ? -18.299 2.004   -42.689 1.00 36.60  ? 518  ASN A ND2 1 
ATOM   4109 N N   . LYS A 1 519 ? -20.927 0.618   -37.799 1.00 23.90  ? 519  LYS A N   1 
ATOM   4110 C CA  . LYS A 1 519 ? -22.027 0.091   -36.989 1.00 22.93  ? 519  LYS A CA  1 
ATOM   4111 C C   . LYS A 1 519 ? -22.089 0.806   -35.654 1.00 22.10  ? 519  LYS A C   1 
ATOM   4112 O O   . LYS A 1 519 ? -21.074 1.353   -35.171 1.00 21.37  ? 519  LYS A O   1 
ATOM   4113 C CB  . LYS A 1 519 ? -21.906 -1.438  -36.762 1.00 23.96  ? 519  LYS A CB  1 
ATOM   4114 C CG  . LYS A 1 519 ? -21.774 -2.305  -38.048 1.00 25.69  ? 519  LYS A CG  1 
ATOM   4115 C CD  . LYS A 1 519 ? -22.968 -2.150  -39.000 1.00 29.89  ? 519  LYS A CD  1 
ATOM   4116 C CE  . LYS A 1 519 ? -22.679 -2.817  -40.374 1.00 31.23  ? 519  LYS A CE  1 
ATOM   4117 N NZ  . LYS A 1 519 ? -23.948 -2.890  -41.170 1.00 35.32  ? 519  LYS A NZ  1 
ATOM   4118 N N   . ARG A 1 520 ? -23.292 0.802   -35.058 1.00 19.76  ? 520  ARG A N   1 
ATOM   4119 C CA  . ARG A 1 520 ? -23.501 1.368   -33.726 1.00 18.69  ? 520  ARG A CA  1 
ATOM   4120 C C   . ARG A 1 520 ? -22.885 0.485   -32.636 1.00 17.96  ? 520  ARG A C   1 
ATOM   4121 O O   . ARG A 1 520 ? -22.392 1.022   -31.645 1.00 18.85  ? 520  ARG A O   1 
ATOM   4122 C CB  . ARG A 1 520 ? -25.014 1.537   -33.437 1.00 18.14  ? 520  ARG A CB  1 
ATOM   4123 C CG  . ARG A 1 520 ? -25.652 2.560   -34.343 1.00 16.33  ? 520  ARG A CG  1 
ATOM   4124 C CD  . ARG A 1 520 ? -27.172 2.378   -34.321 1.00 18.10  ? 520  ARG A CD  1 
ATOM   4125 N NE  . ARG A 1 520 ? -27.680 2.907   -35.568 1.00 16.52  ? 520  ARG A NE  1 
ATOM   4126 C CZ  . ARG A 1 520 ? -28.963 2.936   -35.902 1.00 19.25  ? 520  ARG A CZ  1 
ATOM   4127 N NH1 . ARG A 1 520 ? -29.868 2.479   -35.052 1.00 12.61  ? 520  ARG A NH1 1 
ATOM   4128 N NH2 . ARG A 1 520 ? -29.314 3.411   -37.087 1.00 18.02  ? 520  ARG A NH2 1 
ATOM   4129 N N   . SER A 1 521 ? -23.009 -0.833  -32.790 1.00 17.15  ? 521  SER A N   1 
ATOM   4130 C CA  . SER A 1 521 ? -22.673 -1.799  -31.739 1.00 16.67  ? 521  SER A CA  1 
ATOM   4131 C C   . SER A 1 521 ? -23.519 -1.433  -30.503 1.00 17.46  ? 521  SER A C   1 
ATOM   4132 O O   . SER A 1 521 ? -24.695 -0.971  -30.650 1.00 17.54  ? 521  SER A O   1 
ATOM   4133 C CB  . SER A 1 521 ? -21.148 -1.750  -31.490 1.00 15.82  ? 521  SER A CB  1 
ATOM   4134 O OG  . SER A 1 521 ? -20.779 -2.689  -30.501 1.00 16.75  ? 521  SER A OG  1 
ATOM   4135 N N   . PHE A 1 522 ? -22.955 -1.605  -29.315 1.00 16.83  ? 522  PHE A N   1 
ATOM   4136 C CA  . PHE A 1 522 ? -23.643 -1.391  -28.037 1.00 16.73  ? 522  PHE A CA  1 
ATOM   4137 C C   . PHE A 1 522 ? -22.531 -1.256  -26.998 1.00 16.14  ? 522  PHE A C   1 
ATOM   4138 O O   . PHE A 1 522 ? -21.652 -2.104  -26.954 1.00 15.67  ? 522  PHE A O   1 
ATOM   4139 C CB  . PHE A 1 522 ? -24.449 -2.640  -27.710 1.00 16.42  ? 522  PHE A CB  1 
ATOM   4140 C CG  . PHE A 1 522 ? -25.081 -2.659  -26.341 1.00 17.62  ? 522  PHE A CG  1 
ATOM   4141 C CD1 . PHE A 1 522 ? -26.149 -1.811  -26.045 1.00 15.61  ? 522  PHE A CD1 1 
ATOM   4142 C CD2 . PHE A 1 522 ? -24.650 -3.565  -25.359 1.00 14.72  ? 522  PHE A CD2 1 
ATOM   4143 C CE1 . PHE A 1 522 ? -26.737 -1.852  -24.766 1.00 17.11  ? 522  PHE A CE1 1 
ATOM   4144 C CE2 . PHE A 1 522 ? -25.244 -3.616  -24.103 1.00 17.53  ? 522  PHE A CE2 1 
ATOM   4145 C CZ  . PHE A 1 522 ? -26.296 -2.765  -23.810 1.00 15.54  ? 522  PHE A CZ  1 
ATOM   4146 N N   . ILE A 1 523 ? -22.581 -0.207  -26.188 1.00 15.46  ? 523  ILE A N   1 
ATOM   4147 C CA  . ILE A 1 523 ? -21.734 -0.092  -25.020 1.00 16.23  ? 523  ILE A CA  1 
ATOM   4148 C C   . ILE A 1 523 ? -22.598 0.114   -23.825 1.00 16.21  ? 523  ILE A C   1 
ATOM   4149 O O   . ILE A 1 523 ? -23.490 0.961   -23.844 1.00 17.45  ? 523  ILE A O   1 
ATOM   4150 C CB  . ILE A 1 523 ? -20.776 1.081   -25.124 1.00 15.88  ? 523  ILE A CB  1 
ATOM   4151 C CG1 . ILE A 1 523 ? -19.907 0.899   -26.381 1.00 16.68  ? 523  ILE A CG1 1 
ATOM   4152 C CG2 . ILE A 1 523 ? -19.939 1.228   -23.796 1.00 15.14  ? 523  ILE A CG2 1 
ATOM   4153 C CD1 . ILE A 1 523 ? -19.166 2.158   -26.765 1.00 20.19  ? 523  ILE A CD1 1 
ATOM   4154 N N   . LEU A 1 524 ? -22.374 -0.692  -22.792 1.00 16.05  ? 524  LEU A N   1 
ATOM   4155 C CA  . LEU A 1 524 ? -23.097 -0.579  -21.516 1.00 15.97  ? 524  LEU A CA  1 
ATOM   4156 C C   . LEU A 1 524 ? -22.071 -0.184  -20.459 1.00 16.97  ? 524  LEU A C   1 
ATOM   4157 O O   . LEU A 1 524 ? -21.082 -0.892  -20.319 1.00 19.21  ? 524  LEU A O   1 
ATOM   4158 C CB  . LEU A 1 524 ? -23.688 -1.914  -21.158 1.00 15.79  ? 524  LEU A CB  1 
ATOM   4159 C CG  . LEU A 1 524 ? -24.449 -2.048  -19.835 1.00 16.40  ? 524  LEU A CG  1 
ATOM   4160 C CD1 . LEU A 1 524 ? -25.780 -1.177  -19.811 1.00 14.78  ? 524  LEU A CD1 1 
ATOM   4161 C CD2 . LEU A 1 524 ? -24.760 -3.496  -19.542 1.00 14.92  ? 524  LEU A CD2 1 
ATOM   4162 N N   . THR A 1 525 ? -22.285 0.901   -19.711 1.00 16.25  ? 525  THR A N   1 
ATOM   4163 C CA  . THR A 1 525 ? -21.270 1.364   -18.723 1.00 17.10  ? 525  THR A CA  1 
ATOM   4164 C C   . THR A 1 525 ? -21.874 1.485   -17.340 1.00 18.36  ? 525  THR A C   1 
ATOM   4165 O O   . THR A 1 525 ? -23.078 1.741   -17.184 1.00 17.67  ? 525  THR A O   1 
ATOM   4166 C CB  . THR A 1 525 ? -20.618 2.719   -19.127 1.00 17.53  ? 525  THR A CB  1 
ATOM   4167 O OG1 . THR A 1 525 ? -19.571 3.083   -18.204 1.00 16.42  ? 525  THR A OG1 1 
ATOM   4168 C CG2 . THR A 1 525 ? -21.665 3.824   -19.136 1.00 15.64  ? 525  THR A CG2 1 
ATOM   4169 N N   . ARG A 1 526 ? -21.044 1.249   -16.330 1.00 17.08  ? 526  ARG A N   1 
ATOM   4170 C CA  . ARG A 1 526 ? -21.484 1.437   -14.970 1.00 17.35  ? 526  ARG A CA  1 
ATOM   4171 C C   . ARG A 1 526 ? -21.351 2.896   -14.559 1.00 17.18  ? 526  ARG A C   1 
ATOM   4172 O O   . ARG A 1 526 ? -22.348 3.534   -14.243 1.00 17.04  ? 526  ARG A O   1 
ATOM   4173 C CB  . ARG A 1 526 ? -20.751 0.503   -13.976 1.00 16.88  ? 526  ARG A CB  1 
ATOM   4174 C CG  . ARG A 1 526 ? -21.577 0.347   -12.665 1.00 17.77  ? 526  ARG A CG  1 
ATOM   4175 C CD  . ARG A 1 526 ? -21.148 -0.864  -11.867 1.00 17.34  ? 526  ARG A CD  1 
ATOM   4176 N NE  . ARG A 1 526 ? -19.895 -0.560  -11.215 1.00 21.10  ? 526  ARG A NE  1 
ATOM   4177 C CZ  . ARG A 1 526 ? -19.205 -1.391  -10.440 1.00 22.96  ? 526  ARG A CZ  1 
ATOM   4178 N NH1 . ARG A 1 526 ? -19.632 -2.626  -10.219 1.00 26.22  ? 526  ARG A NH1 1 
ATOM   4179 N NH2 . ARG A 1 526 ? -18.054 -0.971  -9.909  1.00 22.02  ? 526  ARG A NH2 1 
ATOM   4180 N N   . SER A 1 527 ? -20.120 3.421   -14.563 1.00 15.79  ? 527  SER A N   1 
ATOM   4181 C CA  . SER A 1 527 ? -19.851 4.796   -14.182 1.00 16.86  ? 527  SER A CA  1 
ATOM   4182 C C   . SER A 1 527 ? -20.180 5.768   -15.335 1.00 16.47  ? 527  SER A C   1 
ATOM   4183 O O   . SER A 1 527 ? -19.926 5.451   -16.491 1.00 17.32  ? 527  SER A O   1 
ATOM   4184 C CB  . SER A 1 527 ? -18.363 4.950   -13.806 1.00 17.48  ? 527  SER A CB  1 
ATOM   4185 O OG  . SER A 1 527 ? -18.139 6.221   -13.278 1.00 22.06  ? 527  SER A OG  1 
ATOM   4186 N N   . THR A 1 528 ? -20.797 6.896   -15.011 1.00 16.53  ? 528  THR A N   1 
ATOM   4187 C CA  . THR A 1 528 ? -21.249 7.896   -16.011 1.00 15.93  ? 528  THR A CA  1 
ATOM   4188 C C   . THR A 1 528 ? -20.909 9.274   -15.485 1.00 16.01  ? 528  THR A C   1 
ATOM   4189 O O   . THR A 1 528 ? -20.773 9.479   -14.294 1.00 16.20  ? 528  THR A O   1 
ATOM   4190 C CB  . THR A 1 528 ? -22.807 7.866   -16.297 1.00 16.00  ? 528  THR A CB  1 
ATOM   4191 O OG1 . THR A 1 528 ? -23.515 8.179   -15.100 1.00 16.49  ? 528  THR A OG1 1 
ATOM   4192 C CG2 . THR A 1 528 ? -23.273 6.517   -16.827 1.00 18.06  ? 528  THR A CG2 1 
ATOM   4193 N N   . PHE A 1 529 ? -20.798 10.232  -16.394 1.00 14.87  ? 529  PHE A N   1 
ATOM   4194 C CA  . PHE A 1 529 ? -20.768 11.616  -16.063 1.00 15.11  ? 529  PHE A CA  1 
ATOM   4195 C C   . PHE A 1 529 ? -21.839 12.237  -17.002 1.00 14.85  ? 529  PHE A C   1 
ATOM   4196 O O   . PHE A 1 529 ? -22.398 11.545  -17.858 1.00 15.89  ? 529  PHE A O   1 
ATOM   4197 C CB  . PHE A 1 529 ? -19.346 12.168  -16.327 1.00 14.92  ? 529  PHE A CB  1 
ATOM   4198 C CG  . PHE A 1 529 ? -19.139 13.568  -15.856 1.00 15.47  ? 529  PHE A CG  1 
ATOM   4199 C CD1 . PHE A 1 529 ? -19.138 13.867  -14.495 1.00 17.04  ? 529  PHE A CD1 1 
ATOM   4200 C CD2 . PHE A 1 529 ? -18.962 14.595  -16.766 1.00 18.96  ? 529  PHE A CD2 1 
ATOM   4201 C CE1 . PHE A 1 529 ? -18.968 15.179  -14.041 1.00 17.26  ? 529  PHE A CE1 1 
ATOM   4202 C CE2 . PHE A 1 529 ? -18.797 15.925  -16.337 1.00 19.27  ? 529  PHE A CE2 1 
ATOM   4203 C CZ  . PHE A 1 529 ? -18.799 16.221  -14.967 1.00 17.83  ? 529  PHE A CZ  1 
ATOM   4204 N N   . ALA A 1 530 ? -22.136 13.505  -16.820 1.00 14.18  ? 530  ALA A N   1 
ATOM   4205 C CA  . ALA A 1 530 ? -23.020 14.229  -17.730 1.00 16.08  ? 530  ALA A CA  1 
ATOM   4206 C C   . ALA A 1 530 ? -22.529 14.096  -19.181 1.00 16.49  ? 530  ALA A C   1 
ATOM   4207 O O   . ALA A 1 530 ? -21.370 14.395  -19.498 1.00 17.50  ? 530  ALA A O   1 
ATOM   4208 C CB  . ALA A 1 530 ? -23.077 15.675  -17.302 1.00 15.07  ? 530  ALA A CB  1 
ATOM   4209 N N   . GLY A 1 531 ? -23.407 13.620  -20.049 1.00 17.30  ? 531  GLY A N   1 
ATOM   4210 C CA  . GLY A 1 531 ? -23.058 13.370  -21.458 1.00 16.95  ? 531  GLY A CA  1 
ATOM   4211 C C   . GLY A 1 531 ? -22.682 11.951  -21.832 1.00 16.51  ? 531  GLY A C   1 
ATOM   4212 O O   . GLY A 1 531 ? -22.439 11.666  -23.002 1.00 15.77  ? 531  GLY A O   1 
ATOM   4213 N N   . SER A 1 532 ? -22.612 11.037  -20.859 1.00 16.60  ? 532  SER A N   1 
ATOM   4214 C CA  . SER A 1 532 ? -22.242 9.638   -21.154 1.00 14.81  ? 532  SER A CA  1 
ATOM   4215 C C   . SER A 1 532 ? -23.227 8.944   -22.087 1.00 14.55  ? 532  SER A C   1 
ATOM   4216 O O   . SER A 1 532 ? -22.858 7.988   -22.800 1.00 13.97  ? 532  SER A O   1 
ATOM   4217 C CB  . SER A 1 532 ? -22.128 8.775   -19.873 1.00 14.83  ? 532  SER A CB  1 
ATOM   4218 O OG  . SER A 1 532 ? -20.904 9.077   -19.190 1.00 15.01  ? 532  SER A OG  1 
ATOM   4219 N N   . GLY A 1 533 ? -24.476 9.384   -22.047 1.00 15.05  ? 533  GLY A N   1 
ATOM   4220 C CA  . GLY A 1 533 ? -25.514 8.775   -22.906 1.00 14.43  ? 533  GLY A CA  1 
ATOM   4221 C C   . GLY A 1 533 ? -25.205 8.900   -24.417 1.00 15.36  ? 533  GLY A C   1 
ATOM   4222 O O   . GLY A 1 533 ? -25.745 8.131   -25.239 1.00 14.38  ? 533  GLY A O   1 
ATOM   4223 N N   . LYS A 1 534 ? -24.362 9.865   -24.794 1.00 14.59  ? 534  LYS A N   1 
ATOM   4224 C CA  . LYS A 1 534 ? -23.966 10.020  -26.198 1.00 16.87  ? 534  LYS A CA  1 
ATOM   4225 C C   . LYS A 1 534 ? -23.222 8.764   -26.672 1.00 17.85  ? 534  LYS A C   1 
ATOM   4226 O O   . LYS A 1 534 ? -23.191 8.446   -27.854 1.00 19.04  ? 534  LYS A O   1 
ATOM   4227 C CB  . LYS A 1 534 ? -23.128 11.313  -26.361 1.00 17.19  ? 534  LYS A CB  1 
ATOM   4228 C CG  . LYS A 1 534 ? -22.573 11.596  -27.728 1.00 18.45  ? 534  LYS A CG  1 
ATOM   4229 C CD  . LYS A 1 534 ? -21.828 12.937  -27.752 1.00 19.09  ? 534  LYS A CD  1 
ATOM   4230 C CE  . LYS A 1 534 ? -21.072 13.170  -29.110 1.00 21.69  ? 534  LYS A CE  1 
ATOM   4231 N NZ  . LYS A 1 534 ? -20.074 14.299  -29.002 1.00 23.98  ? 534  LYS A NZ  1 
ATOM   4232 N N   . PHE A 1 535 ? -22.660 8.021   -25.725 1.00 18.02  ? 535  PHE A N   1 
ATOM   4233 C CA  . PHE A 1 535 ? -21.822 6.850   -26.016 1.00 18.08  ? 535  PHE A CA  1 
ATOM   4234 C C   . PHE A 1 535 ? -22.386 5.519   -25.560 1.00 18.47  ? 535  PHE A C   1 
ATOM   4235 O O   . PHE A 1 535 ? -22.109 4.470   -26.172 1.00 18.75  ? 535  PHE A O   1 
ATOM   4236 C CB  . PHE A 1 535 ? -20.445 7.050   -25.365 1.00 19.12  ? 535  PHE A CB  1 
ATOM   4237 C CG  . PHE A 1 535 ? -19.804 8.330   -25.764 1.00 22.64  ? 535  PHE A CG  1 
ATOM   4238 C CD1 . PHE A 1 535 ? -19.191 8.456   -27.012 1.00 23.37  ? 535  PHE A CD1 1 
ATOM   4239 C CD2 . PHE A 1 535 ? -19.858 9.442   -24.922 1.00 23.90  ? 535  PHE A CD2 1 
ATOM   4240 C CE1 . PHE A 1 535 ? -18.631 9.672   -27.412 1.00 25.27  ? 535  PHE A CE1 1 
ATOM   4241 C CE2 . PHE A 1 535 ? -19.308 10.650  -25.328 1.00 26.77  ? 535  PHE A CE2 1 
ATOM   4242 C CZ  . PHE A 1 535 ? -18.687 10.755  -26.571 1.00 23.68  ? 535  PHE A CZ  1 
ATOM   4243 N N   . ALA A 1 536 ? -23.147 5.512   -24.471 1.00 16.00  ? 536  ALA A N   1 
ATOM   4244 C CA  . ALA A 1 536 ? -23.367 4.256   -23.815 1.00 15.50  ? 536  ALA A CA  1 
ATOM   4245 C C   . ALA A 1 536 ? -24.739 4.176   -23.168 1.00 15.16  ? 536  ALA A C   1 
ATOM   4246 O O   . ALA A 1 536 ? -25.313 5.204   -22.839 1.00 16.37  ? 536  ALA A O   1 
ATOM   4247 C CB  . ALA A 1 536 ? -22.297 4.077   -22.753 1.00 15.52  ? 536  ALA A CB  1 
ATOM   4248 N N   . ALA A 1 537 ? -25.240 2.955   -23.011 1.00 15.04  ? 537  ALA A N   1 
ATOM   4249 C CA  . ALA A 1 537 ? -26.303 2.591   -22.091 1.00 14.53  ? 537  ALA A CA  1 
ATOM   4250 C C   . ALA A 1 537 ? -25.781 2.492   -20.633 1.00 14.94  ? 537  ALA A C   1 
ATOM   4251 O O   . ALA A 1 537 ? -24.556 2.438   -20.373 1.00 14.72  ? 537  ALA A O   1 
ATOM   4252 C CB  . ALA A 1 537 ? -26.928 1.232   -22.530 1.00 14.84  ? 537  ALA A CB  1 
ATOM   4253 N N   . HIS A 1 538 ? -26.709 2.380   -19.692 1.00 13.99  ? 538  HIS A N   1 
ATOM   4254 C CA  . HIS A 1 538 ? -26.356 2.260   -18.290 1.00 15.12  ? 538  HIS A CA  1 
ATOM   4255 C C   . HIS A 1 538 ? -27.217 1.240   -17.605 1.00 15.46  ? 538  HIS A C   1 
ATOM   4256 O O   . HIS A 1 538 ? -28.415 1.077   -17.948 1.00 16.31  ? 538  HIS A O   1 
ATOM   4257 C CB  . HIS A 1 538 ? -26.455 3.650   -17.592 1.00 13.63  ? 538  HIS A CB  1 
ATOM   4258 C CG  . HIS A 1 538 ? -26.212 3.622   -16.108 1.00 16.31  ? 538  HIS A CG  1 
ATOM   4259 N ND1 . HIS A 1 538 ? -25.004 3.234   -15.549 1.00 15.07  ? 538  HIS A ND1 1 
ATOM   4260 C CD2 . HIS A 1 538 ? -27.016 3.963   -15.067 1.00 17.59  ? 538  HIS A CD2 1 
ATOM   4261 C CE1 . HIS A 1 538 ? -25.074 3.348   -14.234 1.00 16.44  ? 538  HIS A CE1 1 
ATOM   4262 N NE2 . HIS A 1 538 ? -26.286 3.785   -13.912 1.00 17.73  ? 538  HIS A NE2 1 
ATOM   4263 N N   . TRP A 1 539 ? -26.654 0.524   -16.631 1.00 16.03  ? 539  TRP A N   1 
ATOM   4264 C CA  . TRP A 1 539 ? -27.527 -0.215  -15.707 1.00 16.65  ? 539  TRP A CA  1 
ATOM   4265 C C   . TRP A 1 539 ? -27.334 0.243   -14.275 1.00 16.61  ? 539  TRP A C   1 
ATOM   4266 O O   . TRP A 1 539 ? -26.258 0.760   -13.897 1.00 17.02  ? 539  TRP A O   1 
ATOM   4267 C CB  . TRP A 1 539 ? -27.464 -1.764  -15.834 1.00 16.59  ? 539  TRP A CB  1 
ATOM   4268 C CG  . TRP A 1 539 ? -26.401 -2.429  -14.994 1.00 16.75  ? 539  TRP A CG  1 
ATOM   4269 C CD1 . TRP A 1 539 ? -26.583 -3.261  -13.910 1.00 16.65  ? 539  TRP A CD1 1 
ATOM   4270 C CD2 . TRP A 1 539 ? -24.993 -2.328  -15.195 1.00 16.61  ? 539  TRP A CD2 1 
ATOM   4271 N NE1 . TRP A 1 539 ? -25.336 -3.677  -13.432 1.00 17.77  ? 539  TRP A NE1 1 
ATOM   4272 C CE2 . TRP A 1 539 ? -24.361 -3.120  -14.206 1.00 16.78  ? 539  TRP A CE2 1 
ATOM   4273 C CE3 . TRP A 1 539 ? -24.203 -1.665  -16.138 1.00 17.82  ? 539  TRP A CE3 1 
ATOM   4274 C CZ2 . TRP A 1 539 ? -22.974 -3.248  -14.115 1.00 16.45  ? 539  TRP A CZ2 1 
ATOM   4275 C CZ3 . TRP A 1 539 ? -22.822 -1.776  -16.040 1.00 18.04  ? 539  TRP A CZ3 1 
ATOM   4276 C CH2 . TRP A 1 539 ? -22.221 -2.569  -15.031 1.00 17.89  ? 539  TRP A CH2 1 
ATOM   4277 N N   . LEU A 1 540 ? -28.375 0.051   -13.472 1.00 16.66  ? 540  LEU A N   1 
ATOM   4278 C CA  . LEU A 1 540 ? -28.413 0.693   -12.168 1.00 16.71  ? 540  LEU A CA  1 
ATOM   4279 C C   . LEU A 1 540 ? -27.565 -0.051  -11.116 1.00 17.26  ? 540  LEU A C   1 
ATOM   4280 O O   . LEU A 1 540 ? -27.649 0.250   -9.921  1.00 17.40  ? 540  LEU A O   1 
ATOM   4281 C CB  . LEU A 1 540 ? -29.869 0.828   -11.701 1.00 17.32  ? 540  LEU A CB  1 
ATOM   4282 C CG  . LEU A 1 540 ? -30.657 1.762   -12.633 1.00 17.73  ? 540  LEU A CG  1 
ATOM   4283 C CD1 . LEU A 1 540 ? -32.131 1.744   -12.245 1.00 18.36  ? 540  LEU A CD1 1 
ATOM   4284 C CD2 . LEU A 1 540 ? -30.101 3.203   -12.620 1.00 19.22  ? 540  LEU A CD2 1 
ATOM   4285 N N   . GLY A 1 541 ? -26.798 -1.038  -11.563 1.00 16.68  ? 541  GLY A N   1 
ATOM   4286 C CA  . GLY A 1 541 ? -25.710 -1.648  -10.742 1.00 17.48  ? 541  GLY A CA  1 
ATOM   4287 C C   . GLY A 1 541 ? -26.158 -2.868  -9.960  1.00 17.59  ? 541  GLY A C   1 
ATOM   4288 O O   . GLY A 1 541 ? -27.194 -3.487  -10.290 1.00 17.05  ? 541  GLY A O   1 
ATOM   4289 N N   . ASP A 1 542 ? -25.431 -3.159  -8.881  1.00 16.98  ? 542  ASP A N   1 
ATOM   4290 C CA  . ASP A 1 542 ? -25.583 -4.370  -8.047  1.00 18.06  ? 542  ASP A CA  1 
ATOM   4291 C C   . ASP A 1 542 ? -26.740 -4.317  -7.033  1.00 18.54  ? 542  ASP A C   1 
ATOM   4292 O O   . ASP A 1 542 ? -26.537 -4.192  -5.820  1.00 19.89  ? 542  ASP A O   1 
ATOM   4293 C CB  . ASP A 1 542 ? -24.252 -4.631  -7.325  1.00 19.19  ? 542  ASP A CB  1 
ATOM   4294 C CG  . ASP A 1 542 ? -23.077 -4.767  -8.288  1.00 23.05  ? 542  ASP A CG  1 
ATOM   4295 O OD1 . ASP A 1 542 ? -23.267 -5.303  -9.415  1.00 27.81  ? 542  ASP A OD1 1 
ATOM   4296 O OD2 . ASP A 1 542 ? -21.940 -4.381  -7.906  1.00 27.97  ? 542  ASP A OD2 1 
ATOM   4297 N N   . ASN A 1 543 ? -27.964 -4.431  -7.534  1.00 16.63  ? 543  ASN A N   1 
ATOM   4298 C CA  . ASN A 1 543 ? -29.127 -4.399  -6.676  1.00 16.58  ? 543  ASN A CA  1 
ATOM   4299 C C   . ASN A 1 543 ? -29.377 -5.759  -5.989  1.00 17.07  ? 543  ASN A C   1 
ATOM   4300 O O   . ASN A 1 543 ? -28.561 -6.688  -6.071  1.00 16.58  ? 543  ASN A O   1 
ATOM   4301 C CB  . ASN A 1 543 ? -30.358 -3.920  -7.499  1.00 15.78  ? 543  ASN A CB  1 
ATOM   4302 C CG  . ASN A 1 543 ? -30.779 -4.919  -8.569  1.00 15.70  ? 543  ASN A CG  1 
ATOM   4303 O OD1 . ASN A 1 543 ? -30.075 -5.872  -8.843  1.00 18.17  ? 543  ASN A OD1 1 
ATOM   4304 N ND2 . ASN A 1 543 ? -31.979 -4.733  -9.149  1.00 16.66  ? 543  ASN A ND2 1 
ATOM   4305 N N   . THR A 1 544 ? -30.534 -5.907  -5.345  1.00 18.41  ? 544  THR A N   1 
ATOM   4306 C CA  . THR A 1 544 ? -30.763 -7.056  -4.505  1.00 18.74  ? 544  THR A CA  1 
ATOM   4307 C C   . THR A 1 544 ? -32.158 -7.546  -4.836  1.00 19.24  ? 544  THR A C   1 
ATOM   4308 O O   . THR A 1 544 ? -32.991 -6.734  -5.257  1.00 16.42  ? 544  THR A O   1 
ATOM   4309 C CB  . THR A 1 544 ? -30.621 -6.628  -3.016  1.00 19.89  ? 544  THR A CB  1 
ATOM   4310 O OG1 . THR A 1 544 ? -29.345 -5.975  -2.868  1.00 23.82  ? 544  THR A OG1 1 
ATOM   4311 C CG2 . THR A 1 544 ? -30.612 -7.826  -2.079  1.00 21.77  ? 544  THR A CG2 1 
ATOM   4312 N N   . ALA A 1 545 ? -32.388 -8.856  -4.693  1.00 18.26  ? 545  ALA A N   1 
ATOM   4313 C CA  . ALA A 1 545 ? -33.693 -9.436  -4.956  1.00 19.20  ? 545  ALA A CA  1 
ATOM   4314 C C   . ALA A 1 545 ? -34.620 -9.130  -3.799  1.00 19.82  ? 545  ALA A C   1 
ATOM   4315 O O   . ALA A 1 545 ? -34.939 -10.015 -2.996  1.00 19.88  ? 545  ALA A O   1 
ATOM   4316 C CB  . ALA A 1 545 ? -33.574 -10.942 -5.201  1.00 20.01  ? 545  ALA A CB  1 
ATOM   4317 N N   . THR A 1 546 ? -35.017 -7.870  -3.688  1.00 19.04  ? 546  THR A N   1 
ATOM   4318 C CA  . THR A 1 546 ? -36.021 -7.462  -2.677  1.00 19.37  ? 546  THR A CA  1 
ATOM   4319 C C   . THR A 1 546 ? -37.143 -6.664  -3.315  1.00 17.52  ? 546  THR A C   1 
ATOM   4320 O O   . THR A 1 546 ? -36.971 -6.053  -4.371  1.00 14.83  ? 546  THR A O   1 
ATOM   4321 C CB  . THR A 1 546 ? -35.420 -6.625  -1.515  1.00 20.34  ? 546  THR A CB  1 
ATOM   4322 O OG1 . THR A 1 546 ? -35.103 -5.289  -1.953  1.00 22.50  ? 546  THR A OG1 1 
ATOM   4323 C CG2 . THR A 1 546 ? -34.156 -7.256  -0.958  1.00 20.83  ? 546  THR A CG2 1 
ATOM   4324 N N   . TRP A 1 547 ? -38.312 -6.639  -2.670  1.00 17.18  ? 547  TRP A N   1 
ATOM   4325 C CA  . TRP A 1 547 ? -39.344 -5.770  -3.180  1.00 17.98  ? 547  TRP A CA  1 
ATOM   4326 C C   . TRP A 1 547 ? -38.965 -4.279  -3.155  1.00 18.29  ? 547  TRP A C   1 
ATOM   4327 O O   . TRP A 1 547 ? -39.412 -3.536  -4.027  1.00 18.06  ? 547  TRP A O   1 
ATOM   4328 C CB  . TRP A 1 547 ? -40.660 -6.014  -2.445  1.00 17.63  ? 547  TRP A CB  1 
ATOM   4329 C CG  . TRP A 1 547 ? -41.162 -7.377  -2.750  1.00 17.16  ? 547  TRP A CG  1 
ATOM   4330 C CD1 . TRP A 1 547 ? -40.832 -8.547  -2.112  1.00 20.03  ? 547  TRP A CD1 1 
ATOM   4331 C CD2 . TRP A 1 547 ? -42.080 -7.727  -3.790  1.00 19.79  ? 547  TRP A CD2 1 
ATOM   4332 N NE1 . TRP A 1 547 ? -41.526 -9.604  -2.682  1.00 19.64  ? 547  TRP A NE1 1 
ATOM   4333 C CE2 . TRP A 1 547 ? -42.280 -9.124  -3.723  1.00 19.83  ? 547  TRP A CE2 1 
ATOM   4334 C CE3 . TRP A 1 547 ? -42.754 -6.992  -4.782  1.00 18.09  ? 547  TRP A CE3 1 
ATOM   4335 C CZ2 . TRP A 1 547 ? -43.125 -9.801  -4.611  1.00 20.87  ? 547  TRP A CZ2 1 
ATOM   4336 C CZ3 . TRP A 1 547 ? -43.593 -7.672  -5.669  1.00 18.37  ? 547  TRP A CZ3 1 
ATOM   4337 C CH2 . TRP A 1 547 ? -43.774 -9.059  -5.571  1.00 17.47  ? 547  TRP A CH2 1 
ATOM   4338 N N   . ASP A 1 548 ? -38.176 -3.843  -2.165  1.00 18.57  ? 548  ASP A N   1 
ATOM   4339 C CA  . ASP A 1 548 ? -37.714 -2.466  -2.120  1.00 19.30  ? 548  ASP A CA  1 
ATOM   4340 C C   . ASP A 1 548 ? -36.914 -2.147  -3.394  1.00 19.23  ? 548  ASP A C   1 
ATOM   4341 O O   . ASP A 1 548 ? -37.183 -1.121  -4.036  1.00 18.42  ? 548  ASP A O   1 
ATOM   4342 C CB  . ASP A 1 548 ? -36.830 -2.185  -0.909  1.00 20.30  ? 548  ASP A CB  1 
ATOM   4343 C CG  . ASP A 1 548 ? -37.618 -1.879  0.358   1.00 23.45  ? 548  ASP A CG  1 
ATOM   4344 O OD1 . ASP A 1 548 ? -38.784 -1.389  0.319   1.00 24.61  ? 548  ASP A OD1 1 
ATOM   4345 O OD2 . ASP A 1 548 ? -37.027 -2.116  1.417   1.00 27.16  ? 548  ASP A OD2 1 
ATOM   4346 N N   . ASP A 1 549 ? -35.982 -3.027  -3.781  1.00 18.46  ? 549  ASP A N   1 
ATOM   4347 C CA  . ASP A 1 549 ? -35.177 -2.774  -4.994  1.00 18.10  ? 549  ASP A CA  1 
ATOM   4348 C C   . ASP A 1 549 ? -36.035 -2.664  -6.253  1.00 17.94  ? 549  ASP A C   1 
ATOM   4349 O O   . ASP A 1 549 ? -35.763 -1.843  -7.133  1.00 17.36  ? 549  ASP A O   1 
ATOM   4350 C CB  . ASP A 1 549 ? -34.087 -3.810  -5.191  1.00 18.60  ? 549  ASP A CB  1 
ATOM   4351 C CG  . ASP A 1 549 ? -32.987 -3.714  -4.137  1.00 22.48  ? 549  ASP A CG  1 
ATOM   4352 O OD1 . ASP A 1 549 ? -31.850 -3.361  -4.488  1.00 23.69  ? 549  ASP A OD1 1 
ATOM   4353 O OD2 . ASP A 1 549 ? -33.260 -4.051  -2.957  1.00 28.93  ? 549  ASP A OD2 1 
ATOM   4354 N N   . LEU A 1 550 ? -37.088 -3.474  -6.340  1.00 17.34  ? 550  LEU A N   1 
ATOM   4355 C CA  . LEU A 1 550 ? -37.999 -3.390  -7.469  1.00 17.37  ? 550  LEU A CA  1 
ATOM   4356 C C   . LEU A 1 550 ? -38.681 -2.011  -7.534  1.00 17.85  ? 550  LEU A C   1 
ATOM   4357 O O   . LEU A 1 550 ? -38.670 -1.356  -8.583  1.00 17.44  ? 550  LEU A O   1 
ATOM   4358 C CB  . LEU A 1 550 ? -39.040 -4.517  -7.363  1.00 16.93  ? 550  LEU A CB  1 
ATOM   4359 C CG  . LEU A 1 550 ? -40.288 -4.414  -8.266  1.00 20.12  ? 550  LEU A CG  1 
ATOM   4360 C CD1 . LEU A 1 550 ? -39.874 -4.688  -9.690  1.00 21.97  ? 550  LEU A CD1 1 
ATOM   4361 C CD2 . LEU A 1 550 ? -41.277 -5.407  -7.821  1.00 20.68  ? 550  LEU A CD2 1 
ATOM   4362 N N   . ARG A 1 551 ? -39.275 -1.576  -6.410  1.00 17.74  ? 551  ARG A N   1 
ATOM   4363 C CA  . ARG A 1 551 ? -39.845 -0.221  -6.307  1.00 17.83  ? 551  ARG A CA  1 
ATOM   4364 C C   . ARG A 1 551 ? -38.826 0.909   -6.636  1.00 17.79  ? 551  ARG A C   1 
ATOM   4365 O O   . ARG A 1 551 ? -39.126 1.862   -7.362  1.00 18.70  ? 551  ARG A O   1 
ATOM   4366 C CB  . ARG A 1 551 ? -40.413 -0.047  -4.904  1.00 18.25  ? 551  ARG A CB  1 
ATOM   4367 C CG  . ARG A 1 551 ? -41.718 -0.862  -4.739  1.00 18.13  ? 551  ARG A CG  1 
ATOM   4368 C CD  . ARG A 1 551 ? -42.400 -0.570  -3.389  1.00 22.69  ? 551  ARG A CD  1 
ATOM   4369 N NE  . ARG A 1 551 ? -41.624 -1.053  -2.243  1.00 24.90  ? 551  ARG A NE  1 
ATOM   4370 C CZ  . ARG A 1 551 ? -41.827 -2.222  -1.631  1.00 26.18  ? 551  ARG A CZ  1 
ATOM   4371 N NH1 . ARG A 1 551 ? -42.745 -3.074  -2.068  1.00 23.71  ? 551  ARG A NH1 1 
ATOM   4372 N NH2 . ARG A 1 551 ? -41.093 -2.558  -0.587  1.00 23.74  ? 551  ARG A NH2 1 
ATOM   4373 N N   . TRP A 1 552 ? -37.626 0.784   -6.107  1.00 16.74  ? 552  TRP A N   1 
ATOM   4374 C CA  . TRP A 1 552 ? -36.626 1.853   -6.255  1.00 16.51  ? 552  TRP A CA  1 
ATOM   4375 C C   . TRP A 1 552 ? -36.091 1.975   -7.659  1.00 16.35  ? 552  TRP A C   1 
ATOM   4376 O O   . TRP A 1 552 ? -35.422 2.977   -8.006  1.00 17.14  ? 552  TRP A O   1 
ATOM   4377 C CB  . TRP A 1 552 ? -35.476 1.586   -5.318  1.00 17.87  ? 552  TRP A CB  1 
ATOM   4378 C CG  . TRP A 1 552 ? -35.889 1.719   -3.884  1.00 19.61  ? 552  TRP A CG  1 
ATOM   4379 C CD1 . TRP A 1 552 ? -36.989 2.366   -3.392  1.00 19.64  ? 552  TRP A CD1 1 
ATOM   4380 C CD2 . TRP A 1 552 ? -35.177 1.204   -2.764  1.00 20.91  ? 552  TRP A CD2 1 
ATOM   4381 N NE1 . TRP A 1 552 ? -37.022 2.245   -2.023  1.00 21.16  ? 552  TRP A NE1 1 
ATOM   4382 C CE2 . TRP A 1 552 ? -35.902 1.547   -1.619  1.00 22.09  ? 552  TRP A CE2 1 
ATOM   4383 C CE3 . TRP A 1 552 ? -34.003 0.448   -2.627  1.00 21.36  ? 552  TRP A CE3 1 
ATOM   4384 C CZ2 . TRP A 1 552 ? -35.481 1.173   -0.331  1.00 21.45  ? 552  TRP A CZ2 1 
ATOM   4385 C CZ3 . TRP A 1 552 ? -33.591 0.061   -1.345  1.00 21.66  ? 552  TRP A CZ3 1 
ATOM   4386 C CH2 . TRP A 1 552 ? -34.336 0.429   -0.224  1.00 21.15  ? 552  TRP A CH2 1 
ATOM   4387 N N   . SER A 1 553 ? -36.311 0.936   -8.458  1.00 15.49  ? 553  SER A N   1 
ATOM   4388 C CA  . SER A 1 553 ? -35.845 0.950   -9.843  1.00 15.99  ? 553  SER A CA  1 
ATOM   4389 C C   . SER A 1 553 ? -36.523 2.012   -10.699 1.00 15.79  ? 553  SER A C   1 
ATOM   4390 O O   . SER A 1 553 ? -35.885 2.557   -11.596 1.00 15.86  ? 553  SER A O   1 
ATOM   4391 C CB  . SER A 1 553 ? -35.933 -0.428  -10.525 1.00 15.65  ? 553  SER A CB  1 
ATOM   4392 O OG  . SER A 1 553 ? -37.298 -0.762  -10.836 1.00 15.75  ? 553  SER A OG  1 
ATOM   4393 N N   . ILE A 1 554 ? -37.812 2.290   -10.466 1.00 16.22  ? 554  ILE A N   1 
ATOM   4394 C CA  . ILE A 1 554 ? -38.482 3.201   -11.366 1.00 16.08  ? 554  ILE A CA  1 
ATOM   4395 C C   . ILE A 1 554 ? -37.932 4.616   -11.282 1.00 15.85  ? 554  ILE A C   1 
ATOM   4396 O O   . ILE A 1 554 ? -37.662 5.196   -12.315 1.00 16.77  ? 554  ILE A O   1 
ATOM   4397 C CB  . ILE A 1 554 ? -40.026 3.152   -11.246 1.00 17.09  ? 554  ILE A CB  1 
ATOM   4398 C CG1 . ILE A 1 554 ? -40.487 1.747   -11.681 1.00 19.86  ? 554  ILE A CG1 1 
ATOM   4399 C CG2 . ILE A 1 554 ? -40.658 4.201   -12.170 1.00 17.58  ? 554  ILE A CG2 1 
ATOM   4400 C CD1 . ILE A 1 554 ? -41.930 1.387   -11.330 1.00 17.98  ? 554  ILE A CD1 1 
ATOM   4401 N N   . PRO A 1 555 ? -37.823 5.204   -10.075 1.00 15.00  ? 555  PRO A N   1 
ATOM   4402 C CA  . PRO A 1 555 ? -37.228 6.545   -10.111 1.00 16.73  ? 555  PRO A CA  1 
ATOM   4403 C C   . PRO A 1 555 ? -35.830 6.544   -10.726 1.00 15.44  ? 555  PRO A C   1 
ATOM   4404 O O   . PRO A 1 555 ? -35.483 7.517   -11.393 1.00 15.89  ? 555  PRO A O   1 
ATOM   4405 C CB  . PRO A 1 555 ? -37.177 6.978   -8.633  1.00 16.38  ? 555  PRO A CB  1 
ATOM   4406 C CG  . PRO A 1 555 ? -38.230 6.175   -7.956  1.00 14.80  ? 555  PRO A CG  1 
ATOM   4407 C CD  . PRO A 1 555 ? -38.298 4.848   -8.721  1.00 16.27  ? 555  PRO A CD  1 
ATOM   4408 N N   . GLY A 1 556 ? -35.068 5.460   -10.558 1.00 15.94  ? 556  GLY A N   1 
ATOM   4409 C CA  . GLY A 1 556 ? -33.668 5.418   -11.117 1.00 14.00  ? 556  GLY A CA  1 
ATOM   4410 C C   . GLY A 1 556 ? -33.706 5.450   -12.640 1.00 15.70  ? 556  GLY A C   1 
ATOM   4411 O O   . GLY A 1 556 ? -32.901 6.130   -13.280 1.00 16.85  ? 556  GLY A O   1 
ATOM   4412 N N   . VAL A 1 557 ? -34.688 4.756   -13.229 1.00 15.34  ? 557  VAL A N   1 
ATOM   4413 C CA  . VAL A 1 557 ? -34.840 4.729   -14.674 1.00 15.03  ? 557  VAL A CA  1 
ATOM   4414 C C   . VAL A 1 557 ? -35.281 6.104   -15.190 1.00 15.31  ? 557  VAL A C   1 
ATOM   4415 O O   . VAL A 1 557 ? -34.748 6.609   -16.196 1.00 14.67  ? 557  VAL A O   1 
ATOM   4416 C CB  . VAL A 1 557 ? -35.828 3.606   -15.105 1.00 15.35  ? 557  VAL A CB  1 
ATOM   4417 C CG1 . VAL A 1 557 ? -36.344 3.848   -16.504 1.00 16.41  ? 557  VAL A CG1 1 
ATOM   4418 C CG2 . VAL A 1 557 ? -35.117 2.220   -15.013 1.00 13.54  ? 557  VAL A CG2 1 
ATOM   4419 N N   . LEU A 1 558 ? -36.250 6.734   -14.497 1.00 14.47  ? 558  LEU A N   1 
ATOM   4420 C CA  . LEU A 1 558 ? -36.731 8.061   -14.906 1.00 14.99  ? 558  LEU A CA  1 
ATOM   4421 C C   . LEU A 1 558 ? -35.614 9.101   -14.829 1.00 13.91  ? 558  LEU A C   1 
ATOM   4422 O O   . LEU A 1 558 ? -35.444 9.946   -15.712 1.00 13.86  ? 558  LEU A O   1 
ATOM   4423 C CB  . LEU A 1 558 ? -37.898 8.496   -14.011 1.00 13.81  ? 558  LEU A CB  1 
ATOM   4424 C CG  . LEU A 1 558 ? -39.132 7.606   -14.204 1.00 14.52  ? 558  LEU A CG  1 
ATOM   4425 C CD1 . LEU A 1 558 ? -40.159 8.029   -13.222 1.00 14.75  ? 558  LEU A CD1 1 
ATOM   4426 C CD2 . LEU A 1 558 ? -39.634 7.660   -15.650 1.00 15.29  ? 558  LEU A CD2 1 
ATOM   4427 N N   . GLU A 1 559 ? -34.859 9.068   -13.750 1.00 14.00  ? 559  GLU A N   1 
ATOM   4428 C CA  . GLU A 1 559 ? -33.750 10.007  -13.611 1.00 14.64  ? 559  GLU A CA  1 
ATOM   4429 C C   . GLU A 1 559 ? -32.746 9.892   -14.734 1.00 14.09  ? 559  GLU A C   1 
ATOM   4430 O O   . GLU A 1 559 ? -32.327 10.906  -15.269 1.00 13.58  ? 559  GLU A O   1 
ATOM   4431 C CB  . GLU A 1 559 ? -33.070 9.836   -12.249 1.00 14.88  ? 559  GLU A CB  1 
ATOM   4432 C CG  . GLU A 1 559 ? -33.988 10.363  -11.111 1.00 15.30  ? 559  GLU A CG  1 
ATOM   4433 C CD  . GLU A 1 559 ? -33.677 9.724   -9.741  1.00 22.35  ? 559  GLU A CD  1 
ATOM   4434 O OE1 . GLU A 1 559 ? -32.705 8.899   -9.638  1.00 20.87  ? 559  GLU A OE1 1 
ATOM   4435 O OE2 . GLU A 1 559 ? -34.403 10.067  -8.767  1.00 21.58  ? 559  GLU A OE2 1 
ATOM   4436 N N   . PHE A 1 560 ? -32.326 8.684   -15.083 1.00 14.03  ? 560  PHE A N   1 
ATOM   4437 C CA  . PHE A 1 560 ? -31.358 8.570   -16.195 1.00 13.80  ? 560  PHE A CA  1 
ATOM   4438 C C   . PHE A 1 560 ? -31.872 9.032   -17.528 1.00 14.49  ? 560  PHE A C   1 
ATOM   4439 O O   . PHE A 1 560 ? -31.090 9.474   -18.356 1.00 13.33  ? 560  PHE A O   1 
ATOM   4440 C CB  . PHE A 1 560 ? -30.710 7.207   -16.247 1.00 14.04  ? 560  PHE A CB  1 
ATOM   4441 C CG  . PHE A 1 560 ? -29.584 7.128   -15.309 1.00 15.31  ? 560  PHE A CG  1 
ATOM   4442 C CD1 . PHE A 1 560 ? -29.807 6.754   -13.994 1.00 16.47  ? 560  PHE A CD1 1 
ATOM   4443 C CD2 . PHE A 1 560 ? -28.303 7.549   -15.714 1.00 16.42  ? 560  PHE A CD2 1 
ATOM   4444 C CE1 . PHE A 1 560 ? -28.749 6.760   -13.073 1.00 21.91  ? 560  PHE A CE1 1 
ATOM   4445 C CE2 . PHE A 1 560 ? -27.254 7.558   -14.798 1.00 18.46  ? 560  PHE A CE2 1 
ATOM   4446 C CZ  . PHE A 1 560 ? -27.495 7.150   -13.490 1.00 16.58  ? 560  PHE A CZ  1 
ATOM   4447 N N   . ASN A 1 561 ? -33.193 8.951   -17.730 1.00 13.85  ? 561  ASN A N   1 
ATOM   4448 C CA  . ASN A 1 561 ? -33.808 9.549   -18.921 1.00 13.95  ? 561  ASN A CA  1 
ATOM   4449 C C   . ASN A 1 561 ? -33.664 11.088  -18.935 1.00 14.71  ? 561  ASN A C   1 
ATOM   4450 O O   . ASN A 1 561 ? -33.340 11.691  -19.971 1.00 15.73  ? 561  ASN A O   1 
ATOM   4451 C CB  . ASN A 1 561 ? -35.276 9.066   -19.071 1.00 13.48  ? 561  ASN A CB  1 
ATOM   4452 C CG  . ASN A 1 561 ? -35.356 7.773   -19.833 1.00 12.36  ? 561  ASN A CG  1 
ATOM   4453 O OD1 . ASN A 1 561 ? -35.651 7.791   -21.017 1.00 14.29  ? 561  ASN A OD1 1 
ATOM   4454 N ND2 . ASN A 1 561 ? -35.023 6.636   -19.177 1.00 13.59  ? 561  ASN A ND2 1 
ATOM   4455 N N   . LEU A 1 562 ? -33.855 11.736  -17.783 1.00 15.93  ? 562  LEU A N   1 
ATOM   4456 C CA  . LEU A 1 562 ? -33.486 13.158  -17.634 1.00 15.25  ? 562  LEU A CA  1 
ATOM   4457 C C   . LEU A 1 562 ? -32.016 13.428  -17.977 1.00 15.58  ? 562  LEU A C   1 
ATOM   4458 O O   . LEU A 1 562 ? -31.707 14.436  -18.570 1.00 15.67  ? 562  LEU A O   1 
ATOM   4459 C CB  . LEU A 1 562 ? -33.727 13.648  -16.203 1.00 15.30  ? 562  LEU A CB  1 
ATOM   4460 C CG  . LEU A 1 562 ? -35.067 13.560  -15.490 1.00 18.53  ? 562  LEU A CG  1 
ATOM   4461 C CD1 . LEU A 1 562 ? -34.877 14.334  -14.157 1.00 18.96  ? 562  LEU A CD1 1 
ATOM   4462 C CD2 . LEU A 1 562 ? -36.216 14.149  -16.371 1.00 16.35  ? 562  LEU A CD2 1 
ATOM   4463 N N   . PHE A 1 563 ? -31.113 12.528  -17.608 1.00 15.52  ? 563  PHE A N   1 
ATOM   4464 C CA  . PHE A 1 563 ? -29.656 12.743  -17.831 1.00 15.62  ? 563  PHE A CA  1 
ATOM   4465 C C   . PHE A 1 563 ? -29.238 12.392  -19.259 1.00 15.98  ? 563  PHE A C   1 
ATOM   4466 O O   . PHE A 1 563 ? -28.037 12.436  -19.616 1.00 17.07  ? 563  PHE A O   1 
ATOM   4467 C CB  . PHE A 1 563 ? -28.864 11.865  -16.812 1.00 14.68  ? 563  PHE A CB  1 
ATOM   4468 C CG  . PHE A 1 563 ? -29.240 12.106  -15.364 1.00 14.29  ? 563  PHE A CG  1 
ATOM   4469 C CD1 . PHE A 1 563 ? -29.665 13.379  -14.932 1.00 13.92  ? 563  PHE A CD1 1 
ATOM   4470 C CD2 . PHE A 1 563 ? -29.144 11.063  -14.428 1.00 15.81  ? 563  PHE A CD2 1 
ATOM   4471 C CE1 . PHE A 1 563 ? -30.007 13.601  -13.627 1.00 13.59  ? 563  PHE A CE1 1 
ATOM   4472 C CE2 . PHE A 1 563 ? -29.487 11.284  -13.092 1.00 17.66  ? 563  PHE A CE2 1 
ATOM   4473 C CZ  . PHE A 1 563 ? -29.919 12.559  -12.706 1.00 14.26  ? 563  PHE A CZ  1 
ATOM   4474 N N   . GLY A 1 564 ? -30.208 12.017  -20.095 1.00 15.37  ? 564  GLY A N   1 
ATOM   4475 C CA  . GLY A 1 564 ? -29.905 11.657  -21.481 1.00 15.22  ? 564  GLY A CA  1 
ATOM   4476 C C   . GLY A 1 564 ? -29.244 10.308  -21.663 1.00 14.40  ? 564  GLY A C   1 
ATOM   4477 O O   . GLY A 1 564 ? -28.486 10.099  -22.626 1.00 15.07  ? 564  GLY A O   1 
ATOM   4478 N N   . ILE A 1 565 ? -29.489 9.394   -20.723 1.00 12.99  ? 565  ILE A N   1 
ATOM   4479 C CA  . ILE A 1 565 ? -29.118 7.984   -20.854 1.00 14.01  ? 565  ILE A CA  1 
ATOM   4480 C C   . ILE A 1 565 ? -30.443 7.189   -20.824 1.00 14.52  ? 565  ILE A C   1 
ATOM   4481 O O   . ILE A 1 565 ? -30.763 6.512   -19.846 1.00 13.31  ? 565  ILE A O   1 
ATOM   4482 C CB  . ILE A 1 565 ? -28.237 7.554   -19.719 1.00 15.39  ? 565  ILE A CB  1 
ATOM   4483 C CG1 . ILE A 1 565 ? -27.091 8.579   -19.612 1.00 16.26  ? 565  ILE A CG1 1 
ATOM   4484 C CG2 . ILE A 1 565 ? -27.714 6.117   -19.956 1.00 18.91  ? 565  ILE A CG2 1 
ATOM   4485 C CD1 . ILE A 1 565 ? -26.125 8.423   -18.416 1.00 21.30  ? 565  ILE A CD1 1 
ATOM   4486 N N   . PRO A 1 566 ? -31.205 7.278   -21.911 1.00 14.91  ? 566  PRO A N   1 
ATOM   4487 C CA  . PRO A 1 566 ? -32.523 6.670   -21.834 1.00 15.05  ? 566  PRO A CA  1 
ATOM   4488 C C   . PRO A 1 566 ? -32.485 5.139   -21.820 1.00 15.06  ? 566  PRO A C   1 
ATOM   4489 O O   . PRO A 1 566 ? -33.413 4.538   -21.333 1.00 14.08  ? 566  PRO A O   1 
ATOM   4490 C CB  . PRO A 1 566 ? -33.215 7.165   -23.098 1.00 15.19  ? 566  PRO A CB  1 
ATOM   4491 C CG  . PRO A 1 566 ? -32.049 7.440   -24.070 1.00 14.06  ? 566  PRO A CG  1 
ATOM   4492 C CD  . PRO A 1 566 ? -30.951 7.958   -23.193 1.00 15.10  ? 566  PRO A CD  1 
ATOM   4493 N N   . MET A 1 567 ? -31.437 4.530   -22.380 1.00 15.10  ? 567  MET A N   1 
ATOM   4494 C CA  . MET A 1 567 ? -31.352 3.087   -22.328 1.00 16.00  ? 567  MET A CA  1 
ATOM   4495 C C   . MET A 1 567 ? -30.769 2.689   -20.964 1.00 15.06  ? 567  MET A C   1 
ATOM   4496 O O   . MET A 1 567 ? -29.545 2.610   -20.795 1.00 14.79  ? 567  MET A O   1 
ATOM   4497 C CB  . MET A 1 567 ? -30.547 2.534   -23.502 1.00 14.44  ? 567  MET A CB  1 
ATOM   4498 C CG  . MET A 1 567 ? -30.630 1.041   -23.516 1.00 17.82  ? 567  MET A CG  1 
ATOM   4499 S SD  . MET A 1 567 ? -30.001 0.246   -24.990 1.00 22.86  ? 567  MET A SD  1 
ATOM   4500 C CE  . MET A 1 567 ? -31.528 0.077   -25.929 1.00 20.50  ? 567  MET A CE  1 
ATOM   4501 N N   . VAL A 1 568 ? -31.653 2.463   -19.982 1.00 12.72  ? 568  VAL A N   1 
ATOM   4502 C CA  . VAL A 1 568 ? -31.209 2.228   -18.619 1.00 13.77  ? 568  VAL A CA  1 
ATOM   4503 C C   . VAL A 1 568 ? -32.208 1.265   -18.022 1.00 15.21  ? 568  VAL A C   1 
ATOM   4504 O O   . VAL A 1 568 ? -33.392 1.279   -18.390 1.00 14.66  ? 568  VAL A O   1 
ATOM   4505 C CB  . VAL A 1 568 ? -31.132 3.580   -17.795 1.00 12.93  ? 568  VAL A CB  1 
ATOM   4506 C CG1 . VAL A 1 568 ? -32.471 4.366   -17.860 1.00 12.45  ? 568  VAL A CG1 1 
ATOM   4507 C CG2 . VAL A 1 568 ? -30.656 3.365   -16.325 1.00 13.81  ? 568  VAL A CG2 1 
ATOM   4508 N N   . GLY A 1 569 ? -31.734 0.444   -17.096 1.00 16.30  ? 569  GLY A N   1 
ATOM   4509 C CA  . GLY A 1 569 ? -32.610 -0.475  -16.382 1.00 16.98  ? 569  GLY A CA  1 
ATOM   4510 C C   . GLY A 1 569 ? -31.830 -1.095  -15.242 1.00 17.98  ? 569  GLY A C   1 
ATOM   4511 O O   . GLY A 1 569 ? -30.607 -0.968  -15.209 1.00 17.95  ? 569  GLY A O   1 
ATOM   4512 N N   . PRO A 1 570 ? -32.513 -1.747  -14.295 1.00 17.62  ? 570  PRO A N   1 
ATOM   4513 C CA  . PRO A 1 570 ? -31.791 -2.472  -13.261 1.00 18.53  ? 570  PRO A CA  1 
ATOM   4514 C C   . PRO A 1 570 ? -31.426 -3.919  -13.722 1.00 19.38  ? 570  PRO A C   1 
ATOM   4515 O O   . PRO A 1 570 ? -31.699 -4.324  -14.882 1.00 19.98  ? 570  PRO A O   1 
ATOM   4516 C CB  . PRO A 1 570 ? -32.838 -2.564  -12.142 1.00 18.05  ? 570  PRO A CB  1 
ATOM   4517 C CG  . PRO A 1 570 ? -34.149 -2.763  -12.914 1.00 18.84  ? 570  PRO A CG  1 
ATOM   4518 C CD  . PRO A 1 570 ? -33.974 -1.849  -14.131 1.00 19.37  ? 570  PRO A CD  1 
ATOM   4519 N N   . ASP A 1 571 ? -30.856 -4.714  -12.809 1.00 19.68  ? 571  ASP A N   1 
ATOM   4520 C CA  . ASP A 1 571 ? -30.730 -6.171  -13.027 1.00 18.94  ? 571  ASP A CA  1 
ATOM   4521 C C   . ASP A 1 571 ? -32.106 -6.740  -12.661 1.00 19.05  ? 571  ASP A C   1 
ATOM   4522 O O   . ASP A 1 571 ? -32.487 -6.740  -11.484 1.00 19.12  ? 571  ASP A O   1 
ATOM   4523 C CB  . ASP A 1 571 ? -29.658 -6.756  -12.116 1.00 18.48  ? 571  ASP A CB  1 
ATOM   4524 C CG  . ASP A 1 571 ? -28.230 -6.399  -12.561 1.00 19.47  ? 571  ASP A CG  1 
ATOM   4525 O OD1 . ASP A 1 571 ? -28.039 -5.950  -13.710 1.00 23.44  ? 571  ASP A OD1 1 
ATOM   4526 O OD2 . ASP A 1 571 ? -27.254 -6.553  -11.765 1.00 24.51  ? 571  ASP A OD2 1 
ATOM   4527 N N   . ILE A 1 572 ? -32.867 -7.183  -13.658 1.00 18.78  ? 572  ILE A N   1 
ATOM   4528 C CA  . ILE A 1 572 ? -34.220 -7.640  -13.416 1.00 18.12  ? 572  ILE A CA  1 
ATOM   4529 C C   . ILE A 1 572 ? -34.091 -8.913  -12.548 1.00 18.73  ? 572  ILE A C   1 
ATOM   4530 O O   . ILE A 1 572 ? -33.206 -9.767  -12.795 1.00 19.18  ? 572  ILE A O   1 
ATOM   4531 C CB  . ILE A 1 572 ? -34.973 -7.982  -14.724 1.00 18.54  ? 572  ILE A CB  1 
ATOM   4532 C CG1 . ILE A 1 572 ? -35.264 -6.703  -15.532 1.00 17.71  ? 572  ILE A CG1 1 
ATOM   4533 C CG2 . ILE A 1 572 ? -36.290 -8.748  -14.433 1.00 19.11  ? 572  ILE A CG2 1 
ATOM   4534 C CD1 . ILE A 1 572 ? -35.817 -6.986  -16.942 1.00 18.73  ? 572  ILE A CD1 1 
ATOM   4535 N N   . CYS A 1 573 ? -34.931 -8.985  -11.523 1.00 18.74  ? 573  CYS A N   1 
ATOM   4536 C CA  . CYS A 1 573 ? -34.987 -10.097 -10.558 1.00 19.15  ? 573  CYS A CA  1 
ATOM   4537 C C   . CYS A 1 573 ? -34.002 -9.961  -9.416  1.00 19.96  ? 573  CYS A C   1 
ATOM   4538 O O   . CYS A 1 573 ? -34.189 -10.569 -8.378  1.00 20.32  ? 573  CYS A O   1 
ATOM   4539 C CB  . CYS A 1 573 ? -34.913 -11.475 -11.247 1.00 20.44  ? 573  CYS A CB  1 
ATOM   4540 S SG  . CYS A 1 573 ? -36.483 -11.729 -12.177 1.00 22.80  ? 573  CYS A SG  1 
ATOM   4541 N N   . GLY A 1 574 ? -32.950 -9.167  -9.604  1.00 18.41  ? 574  GLY A N   1 
ATOM   4542 C CA  . GLY A 1 574 ? -32.123 -8.778  -8.487  1.00 19.27  ? 574  GLY A CA  1 
ATOM   4543 C C   . GLY A 1 574 ? -30.777 -9.450  -8.649  1.00 19.40  ? 574  GLY A C   1 
ATOM   4544 O O   . GLY A 1 574 ? -30.698 -10.658 -8.772  1.00 21.08  ? 574  GLY A O   1 
ATOM   4545 N N   . PHE A 1 575 ? -29.733 -8.664  -8.625  1.00 19.05  ? 575  PHE A N   1 
ATOM   4546 C CA  . PHE A 1 575 ? -28.403 -9.204  -8.721  1.00 19.32  ? 575  PHE A CA  1 
ATOM   4547 C C   . PHE A 1 575 ? -28.083 -10.106 -7.503  1.00 19.03  ? 575  PHE A C   1 
ATOM   4548 O O   . PHE A 1 575 ? -28.019 -11.324 -7.647  1.00 19.99  ? 575  PHE A O   1 
ATOM   4549 C CB  . PHE A 1 575 ? -27.418 -8.073  -8.866  1.00 18.62  ? 575  PHE A CB  1 
ATOM   4550 C CG  . PHE A 1 575 ? -26.018 -8.519  -9.033  1.00 20.40  ? 575  PHE A CG  1 
ATOM   4551 C CD1 . PHE A 1 575 ? -25.608 -9.096  -10.228 1.00 18.81  ? 575  PHE A CD1 1 
ATOM   4552 C CD2 . PHE A 1 575 ? -25.089 -8.349  -7.990  1.00 20.84  ? 575  PHE A CD2 1 
ATOM   4553 C CE1 . PHE A 1 575 ? -24.295 -9.497  -10.392 1.00 18.62  ? 575  PHE A CE1 1 
ATOM   4554 C CE2 . PHE A 1 575 ? -23.756 -8.761  -8.145  1.00 22.47  ? 575  PHE A CE2 1 
ATOM   4555 C CZ  . PHE A 1 575 ? -23.360 -9.327  -9.358  1.00 21.21  ? 575  PHE A CZ  1 
ATOM   4556 N N   . ALA A 1 576 ? -27.885 -9.520  -6.319  1.00 19.55  ? 576  ALA A N   1 
ATOM   4557 C CA  . ALA A 1 576 ? -27.583 -10.302 -5.096  1.00 20.45  ? 576  ALA A CA  1 
ATOM   4558 C C   . ALA A 1 576 ? -28.810 -11.036 -4.554  1.00 20.81  ? 576  ALA A C   1 
ATOM   4559 O O   . ALA A 1 576 ? -29.913 -10.511 -4.632  1.00 21.27  ? 576  ALA A O   1 
ATOM   4560 C CB  . ALA A 1 576 ? -26.987 -9.366  -3.999  1.00 20.46  ? 576  ALA A CB  1 
ATOM   4561 N N   . LEU A 1 577 ? -28.602 -12.242 -4.008  1.00 20.83  ? 577  LEU A N   1 
ATOM   4562 C CA  . LEU A 1 577 ? -29.638 -13.047 -3.341  1.00 22.01  ? 577  LEU A CA  1 
ATOM   4563 C C   . LEU A 1 577 ? -30.406 -13.917 -4.336  1.00 21.94  ? 577  LEU A C   1 
ATOM   4564 O O   . LEU A 1 577 ? -30.486 -13.590 -5.519  1.00 21.25  ? 577  LEU A O   1 
ATOM   4565 C CB  . LEU A 1 577 ? -30.607 -12.181 -2.510  1.00 21.60  ? 577  LEU A CB  1 
ATOM   4566 C CG  . LEU A 1 577 ? -30.236 -11.837 -1.081  1.00 25.34  ? 577  LEU A CG  1 
ATOM   4567 C CD1 . LEU A 1 577 ? -28.726 -11.744 -0.842  1.00 25.22  ? 577  LEU A CD1 1 
ATOM   4568 C CD2 . LEU A 1 577 ? -30.956 -10.631 -0.627  1.00 24.34  ? 577  LEU A CD2 1 
ATOM   4569 N N   . ASP A 1 578 ? -30.919 -15.044 -3.838  1.00 22.34  ? 578  ASP A N   1 
ATOM   4570 C CA  . ASP A 1 578 ? -31.867 -15.889 -4.540  1.00 23.87  ? 578  ASP A CA  1 
ATOM   4571 C C   . ASP A 1 578 ? -33.171 -15.117 -4.659  1.00 23.66  ? 578  ASP A C   1 
ATOM   4572 O O   . ASP A 1 578 ? -33.629 -14.535 -3.672  1.00 24.08  ? 578  ASP A O   1 
ATOM   4573 C CB  . ASP A 1 578 ? -32.167 -17.153 -3.729  1.00 23.87  ? 578  ASP A CB  1 
ATOM   4574 C CG  . ASP A 1 578 ? -30.951 -18.036 -3.534  1.00 27.50  ? 578  ASP A CG  1 
ATOM   4575 O OD1 . ASP A 1 578 ? -29.879 -17.772 -4.121  1.00 26.43  ? 578  ASP A OD1 1 
ATOM   4576 O OD2 . ASP A 1 578 ? -31.079 -19.016 -2.777  1.00 30.13  ? 578  ASP A OD2 1 
ATOM   4577 N N   . THR A 1 579 ? -33.772 -15.120 -5.845  1.00 22.74  ? 579  THR A N   1 
ATOM   4578 C CA  . THR A 1 579 ? -34.978 -14.343 -6.049  1.00 21.80  ? 579  THR A CA  1 
ATOM   4579 C C   . THR A 1 579 ? -36.222 -15.202 -5.778  1.00 22.30  ? 579  THR A C   1 
ATOM   4580 O O   . THR A 1 579 ? -36.317 -16.313 -6.285  1.00 22.10  ? 579  THR A O   1 
ATOM   4581 C CB  . THR A 1 579 ? -34.990 -13.677 -7.461  1.00 21.42  ? 579  THR A CB  1 
ATOM   4582 O OG1 . THR A 1 579 ? -35.948 -12.620 -7.498  1.00 22.83  ? 579  THR A OG1 1 
ATOM   4583 C CG2 . THR A 1 579 ? -35.292 -14.675 -8.598  1.00 20.77  ? 579  THR A CG2 1 
ATOM   4584 N N   . PRO A 1 580 ? -37.150 -14.706 -4.952  1.00 22.57  ? 580  PRO A N   1 
ATOM   4585 C CA  . PRO A 1 580 ? -38.420 -15.450 -4.847  1.00 23.02  ? 580  PRO A CA  1 
ATOM   4586 C C   . PRO A 1 580 ? -39.179 -15.458 -6.176  1.00 23.52  ? 580  PRO A C   1 
ATOM   4587 O O   . PRO A 1 580 ? -39.135 -14.476 -6.940  1.00 22.23  ? 580  PRO A O   1 
ATOM   4588 C CB  . PRO A 1 580 ? -39.239 -14.665 -3.814  1.00 23.46  ? 580  PRO A CB  1 
ATOM   4589 C CG  . PRO A 1 580 ? -38.435 -13.504 -3.384  1.00 23.83  ? 580  PRO A CG  1 
ATOM   4590 C CD  . PRO A 1 580 ? -37.103 -13.486 -4.122  1.00 23.26  ? 580  PRO A CD  1 
ATOM   4591 N N   . GLU A 1 581 ? -39.905 -16.538 -6.452  1.00 23.44  ? 581  GLU A N   1 
ATOM   4592 C CA  . GLU A 1 581 ? -40.675 -16.617 -7.689  1.00 23.24  ? 581  GLU A CA  1 
ATOM   4593 C C   . GLU A 1 581 ? -41.628 -15.415 -7.889  1.00 22.31  ? 581  GLU A C   1 
ATOM   4594 O O   . GLU A 1 581 ? -41.830 -14.939 -9.003  1.00 22.16  ? 581  GLU A O   1 
ATOM   4595 C CB  . GLU A 1 581 ? -41.489 -17.910 -7.718  1.00 22.80  ? 581  GLU A CB  1 
ATOM   4596 C CG  . GLU A 1 581 ? -42.135 -18.179 -9.034  1.00 23.64  ? 581  GLU A CG  1 
ATOM   4597 C CD  . GLU A 1 581 ? -43.515 -17.557 -9.164  1.00 25.91  ? 581  GLU A CD  1 
ATOM   4598 O OE1 . GLU A 1 581 ? -44.114 -17.072 -8.162  1.00 27.47  ? 581  GLU A OE1 1 
ATOM   4599 O OE2 . GLU A 1 581 ? -44.011 -17.552 -10.299 1.00 28.88  ? 581  GLU A OE2 1 
ATOM   4600 N N   . GLU A 1 582 ? -42.265 -14.962 -6.823  1.00 21.67  ? 582  GLU A N   1 
ATOM   4601 C CA  . GLU A 1 582 ? -43.301 -13.963 -6.992  1.00 21.50  ? 582  GLU A CA  1 
ATOM   4602 C C   . GLU A 1 582 ? -42.623 -12.643 -7.355  1.00 20.52  ? 582  GLU A C   1 
ATOM   4603 O O   . GLU A 1 582 ? -43.090 -11.906 -8.223  1.00 18.40  ? 582  GLU A O   1 
ATOM   4604 C CB  . GLU A 1 582 ? -44.126 -13.813 -5.731  1.00 21.80  ? 582  GLU A CB  1 
ATOM   4605 C CG  . GLU A 1 582 ? -45.230 -12.788 -5.898  1.00 23.38  ? 582  GLU A CG  1 
ATOM   4606 C CD  . GLU A 1 582 ? -45.807 -12.312 -4.581  1.00 28.72  ? 582  GLU A CD  1 
ATOM   4607 O OE1 . GLU A 1 582 ? -45.467 -12.883 -3.503  1.00 32.01  ? 582  GLU A OE1 1 
ATOM   4608 O OE2 . GLU A 1 582 ? -46.607 -11.354 -4.618  1.00 27.46  ? 582  GLU A OE2 1 
ATOM   4609 N N   . LEU A 1 583 ? -41.486 -12.383 -6.716  1.00 20.11  ? 583  LEU A N   1 
ATOM   4610 C CA  . LEU A 1 583 ? -40.788 -11.149 -6.960  1.00 19.10  ? 583  LEU A CA  1 
ATOM   4611 C C   . LEU A 1 583 ? -40.246 -11.190 -8.383  1.00 19.51  ? 583  LEU A C   1 
ATOM   4612 O O   . LEU A 1 583 ? -40.405 -10.231 -9.128  1.00 19.04  ? 583  LEU A O   1 
ATOM   4613 C CB  . LEU A 1 583 ? -39.673 -10.908 -5.927  1.00 19.06  ? 583  LEU A CB  1 
ATOM   4614 C CG  . LEU A 1 583 ? -38.663 -9.798  -6.275  1.00 18.86  ? 583  LEU A CG  1 
ATOM   4615 C CD1 . LEU A 1 583 ? -39.311 -8.427  -6.250  1.00 16.19  ? 583  LEU A CD1 1 
ATOM   4616 C CD2 . LEU A 1 583 ? -37.448 -9.809  -5.337  1.00 18.63  ? 583  LEU A CD2 1 
ATOM   4617 N N   . CYS A 1 584 ? -39.630 -12.302 -8.775  1.00 21.05  ? 584  CYS A N   1 
ATOM   4618 C CA  . CYS A 1 584 ? -39.059 -12.381 -10.123 1.00 20.67  ? 584  CYS A CA  1 
ATOM   4619 C C   . CYS A 1 584 ? -40.164 -12.278 -11.186 1.00 20.15  ? 584  CYS A C   1 
ATOM   4620 O O   . CYS A 1 584 ? -39.986 -11.631 -12.202 1.00 20.09  ? 584  CYS A O   1 
ATOM   4621 C CB  . CYS A 1 584 ? -38.233 -13.639 -10.287 1.00 20.62  ? 584  CYS A CB  1 
ATOM   4622 S SG  . CYS A 1 584 ? -37.093 -13.674 -11.735 1.00 23.52  ? 584  CYS A SG  1 
ATOM   4623 N N   . ARG A 1 585 ? -41.327 -12.866 -10.923 1.00 19.62  ? 585  ARG A N   1 
ATOM   4624 C CA  . ARG A 1 585 ? -42.431 -12.795 -11.880 1.00 18.98  ? 585  ARG A CA  1 
ATOM   4625 C C   . ARG A 1 585 ? -42.895 -11.355 -12.042 1.00 17.88  ? 585  ARG A C   1 
ATOM   4626 O O   . ARG A 1 585 ? -43.051 -10.880 -13.175 1.00 17.80  ? 585  ARG A O   1 
ATOM   4627 C CB  . ARG A 1 585 ? -43.592 -13.703 -11.436 1.00 18.88  ? 585  ARG A CB  1 
ATOM   4628 C CG  . ARG A 1 585 ? -44.902 -13.513 -12.191 1.00 20.68  ? 585  ARG A CG  1 
ATOM   4629 C CD  . ARG A 1 585 ? -45.806 -14.758 -12.011 1.00 19.76  ? 585  ARG A CD  1 
ATOM   4630 N NE  . ARG A 1 585 ? -45.823 -15.251 -10.635 1.00 20.86  ? 585  ARG A NE  1 
ATOM   4631 C CZ  . ARG A 1 585 ? -46.503 -14.675 -9.634  1.00 21.58  ? 585  ARG A CZ  1 
ATOM   4632 N NH1 . ARG A 1 585 ? -47.189 -13.569 -9.845  1.00 24.02  ? 585  ARG A NH1 1 
ATOM   4633 N NH2 . ARG A 1 585 ? -46.470 -15.173 -8.408  1.00 18.59  ? 585  ARG A NH2 1 
ATOM   4634 N N   . ARG A 1 586 ? -43.071 -10.641 -10.921 1.00 17.63  ? 586  ARG A N   1 
ATOM   4635 C CA  . ARG A 1 586 ? -43.454 -9.218  -10.997 1.00 15.98  ? 586  ARG A CA  1 
ATOM   4636 C C   . ARG A 1 586 ? -42.370 -8.376  -11.652 1.00 15.76  ? 586  ARG A C   1 
ATOM   4637 O O   . ARG A 1 586 ? -42.656 -7.443  -12.383 1.00 15.66  ? 586  ARG A O   1 
ATOM   4638 C CB  . ARG A 1 586 ? -43.809 -8.633  -9.628  1.00 15.64  ? 586  ARG A CB  1 
ATOM   4639 C CG  . ARG A 1 586 ? -45.029 -9.268  -8.983  1.00 16.42  ? 586  ARG A CG  1 
ATOM   4640 C CD  . ARG A 1 586 ? -46.151 -9.331  -9.974  1.00 17.24  ? 586  ARG A CD  1 
ATOM   4641 N NE  . ARG A 1 586 ? -47.452 -9.455  -9.328  1.00 19.42  ? 586  ARG A NE  1 
ATOM   4642 C CZ  . ARG A 1 586 ? -48.607 -9.392  -9.984  1.00 20.75  ? 586  ARG A CZ  1 
ATOM   4643 N NH1 . ARG A 1 586 ? -48.603 -9.219  -11.291 1.00 18.64  ? 586  ARG A NH1 1 
ATOM   4644 N NH2 . ARG A 1 586 ? -49.766 -9.502  -9.328  1.00 19.97  ? 586  ARG A NH2 1 
ATOM   4645 N N   . TRP A 1 587 ? -41.107 -8.703  -11.383 1.00 15.63  ? 587  TRP A N   1 
ATOM   4646 C CA  . TRP A 1 587 ? -40.055 -7.891  -11.899 1.00 15.25  ? 587  TRP A CA  1 
ATOM   4647 C C   . TRP A 1 587 ? -39.869 -8.133  -13.391 1.00 16.02  ? 587  TRP A C   1 
ATOM   4648 O O   . TRP A 1 587 ? -39.568 -7.190  -14.141 1.00 16.16  ? 587  TRP A O   1 
ATOM   4649 C CB  . TRP A 1 587 ? -38.740 -8.238  -11.174 1.00 15.11  ? 587  TRP A CB  1 
ATOM   4650 C CG  . TRP A 1 587 ? -37.825 -7.058  -11.029 1.00 15.61  ? 587  TRP A CG  1 
ATOM   4651 C CD1 . TRP A 1 587 ? -37.677 -6.003  -11.893 1.00 15.42  ? 587  TRP A CD1 1 
ATOM   4652 C CD2 . TRP A 1 587 ? -36.875 -6.852  -9.965  1.00 15.96  ? 587  TRP A CD2 1 
ATOM   4653 N NE1 . TRP A 1 587 ? -36.698 -5.143  -11.432 1.00 16.40  ? 587  TRP A NE1 1 
ATOM   4654 C CE2 . TRP A 1 587 ? -36.195 -5.638  -10.244 1.00 16.79  ? 587  TRP A CE2 1 
ATOM   4655 C CE3 . TRP A 1 587 ? -36.553 -7.568  -8.797  1.00 13.81  ? 587  TRP A CE3 1 
ATOM   4656 C CZ2 . TRP A 1 587 ? -35.198 -5.115  -9.382  1.00 16.55  ? 587  TRP A CZ2 1 
ATOM   4657 C CZ3 . TRP A 1 587 ? -35.545 -7.032  -7.931  1.00 15.01  ? 587  TRP A CZ3 1 
ATOM   4658 C CH2 . TRP A 1 587 ? -34.913 -5.822  -8.232  1.00 14.54  ? 587  TRP A CH2 1 
ATOM   4659 N N   . MET A 1 588 ? -40.061 -9.381  -13.833 1.00 15.51  ? 588  MET A N   1 
ATOM   4660 C CA  . MET A 1 588 ? -40.052 -9.693  -15.263 1.00 15.70  ? 588  MET A CA  1 
ATOM   4661 C C   . MET A 1 588 ? -41.148 -8.970  -16.003 1.00 16.41  ? 588  MET A C   1 
ATOM   4662 O O   . MET A 1 588 ? -40.905 -8.466  -17.102 1.00 15.54  ? 588  MET A O   1 
ATOM   4663 C CB  . MET A 1 588 ? -40.111 -11.205 -15.554 1.00 15.80  ? 588  MET A CB  1 
ATOM   4664 C CG  . MET A 1 588 ? -38.733 -11.891 -15.370 1.00 17.29  ? 588  MET A CG  1 
ATOM   4665 S SD  . MET A 1 588 ? -37.447 -11.363 -16.549 1.00 20.77  ? 588  MET A SD  1 
ATOM   4666 C CE  . MET A 1 588 ? -38.125 -11.800 -18.151 1.00 21.06  ? 588  MET A CE  1 
ATOM   4667 N N   . GLN A 1 589 ? -42.344 -8.912  -15.402 1.00 15.60  ? 589  GLN A N   1 
ATOM   4668 C CA  . GLN A 1 589 ? -43.459 -8.155  -15.985 1.00 16.40  ? 589  GLN A CA  1 
ATOM   4669 C C   . GLN A 1 589 ? -43.140 -6.692  -16.174 1.00 16.96  ? 589  GLN A C   1 
ATOM   4670 O O   . GLN A 1 589 ? -43.390 -6.136  -17.243 1.00 17.39  ? 589  GLN A O   1 
ATOM   4671 C CB  . GLN A 1 589 ? -44.692 -8.274  -15.075 1.00 17.40  ? 589  GLN A CB  1 
ATOM   4672 C CG  . GLN A 1 589 ? -45.266 -9.685  -15.166 1.00 18.96  ? 589  GLN A CG  1 
ATOM   4673 C CD  . GLN A 1 589 ? -46.328 -10.016 -14.125 1.00 17.94  ? 589  GLN A CD  1 
ATOM   4674 O OE1 . GLN A 1 589 ? -46.577 -9.267  -13.164 1.00 18.50  ? 589  GLN A OE1 1 
ATOM   4675 N NE2 . GLN A 1 589 ? -46.931 -11.166 -14.304 1.00 19.81  ? 589  GLN A NE2 1 
ATOM   4676 N N   . LEU A 1 590 ? -42.551 -6.071  -15.137 1.00 16.89  ? 590  LEU A N   1 
ATOM   4677 C CA  . LEU A 1 590 ? -42.131 -4.674  -15.216 1.00 16.71  ? 590  LEU A CA  1 
ATOM   4678 C C   . LEU A 1 590 ? -40.960 -4.534  -16.158 1.00 16.00  ? 590  LEU A C   1 
ATOM   4679 O O   . LEU A 1 590 ? -40.906 -3.586  -16.954 1.00 15.28  ? 590  LEU A O   1 
ATOM   4680 C CB  . LEU A 1 590 ? -41.731 -4.124  -13.835 1.00 15.50  ? 590  LEU A CB  1 
ATOM   4681 C CG  . LEU A 1 590 ? -41.183 -2.696  -13.837 1.00 16.66  ? 590  LEU A CG  1 
ATOM   4682 C CD1 . LEU A 1 590 ? -42.152 -1.696  -14.559 1.00 16.59  ? 590  LEU A CD1 1 
ATOM   4683 C CD2 . LEU A 1 590 ? -41.012 -2.330  -12.393 1.00 18.92  ? 590  LEU A CD2 1 
ATOM   4684 N N   . GLY A 1 591 ? -39.992 -5.442  -15.976 1.00 16.68  ? 591  GLY A N   1 
ATOM   4685 C CA  . GLY A 1 591 ? -38.752 -5.471  -16.737 1.00 17.87  ? 591  GLY A CA  1 
ATOM   4686 C C   . GLY A 1 591 ? -38.909 -5.564  -18.239 1.00 16.85  ? 591  GLY A C   1 
ATOM   4687 O O   . GLY A 1 591 ? -38.025 -5.126  -18.980 1.00 16.64  ? 591  GLY A O   1 
ATOM   4688 N N   . ALA A 1 592 ? -40.030 -6.131  -18.686 1.00 16.70  ? 592  ALA A N   1 
ATOM   4689 C CA  . ALA A 1 592 ? -40.343 -6.129  -20.100 1.00 15.95  ? 592  ALA A CA  1 
ATOM   4690 C C   . ALA A 1 592 ? -40.491 -4.714  -20.657 1.00 15.85  ? 592  ALA A C   1 
ATOM   4691 O O   . ALA A 1 592 ? -40.409 -4.506  -21.863 1.00 15.71  ? 592  ALA A O   1 
ATOM   4692 C CB  . ALA A 1 592 ? -41.602 -6.992  -20.386 1.00 16.39  ? 592  ALA A CB  1 
ATOM   4693 N N   . PHE A 1 593 ? -40.729 -3.736  -19.786 1.00 15.57  ? 593  PHE A N   1 
ATOM   4694 C CA  . PHE A 1 593 ? -40.869 -2.322  -20.211 1.00 15.86  ? 593  PHE A CA  1 
ATOM   4695 C C   . PHE A 1 593 ? -39.761 -1.365  -19.740 1.00 15.81  ? 593  PHE A C   1 
ATOM   4696 O O   . PHE A 1 593 ? -39.909 -0.146  -19.856 1.00 16.19  ? 593  PHE A O   1 
ATOM   4697 C CB  . PHE A 1 593 ? -42.264 -1.866  -19.799 1.00 16.06  ? 593  PHE A CB  1 
ATOM   4698 C CG  . PHE A 1 593 ? -43.298 -2.747  -20.408 1.00 15.85  ? 593  PHE A CG  1 
ATOM   4699 C CD1 . PHE A 1 593 ? -43.691 -2.526  -21.738 1.00 16.75  ? 593  PHE A CD1 1 
ATOM   4700 C CD2 . PHE A 1 593 ? -43.719 -3.903  -19.755 1.00 14.25  ? 593  PHE A CD2 1 
ATOM   4701 C CE1 . PHE A 1 593 ? -44.595 -3.396  -22.380 1.00 14.73  ? 593  PHE A CE1 1 
ATOM   4702 C CE2 . PHE A 1 593 ? -44.664 -4.786  -20.404 1.00 14.47  ? 593  PHE A CE2 1 
ATOM   4703 C CZ  . PHE A 1 593 ? -45.061 -4.513  -21.697 1.00 13.63  ? 593  PHE A CZ  1 
ATOM   4704 N N   . TYR A 1 594 ? -38.657 -1.887  -19.194 1.00 14.39  ? 594  TYR A N   1 
ATOM   4705 C CA  . TYR A 1 594 ? -37.537 -0.988  -18.930 1.00 14.79  ? 594  TYR A CA  1 
ATOM   4706 C C   . TYR A 1 594 ? -36.920 -0.728  -20.302 1.00 16.48  ? 594  TYR A C   1 
ATOM   4707 O O   . TYR A 1 594 ? -36.934 -1.634  -21.140 1.00 17.39  ? 594  TYR A O   1 
ATOM   4708 C CB  . TYR A 1 594 ? -36.455 -1.648  -18.067 1.00 13.79  ? 594  TYR A CB  1 
ATOM   4709 C CG  . TYR A 1 594 ? -36.764 -1.852  -16.611 1.00 14.64  ? 594  TYR A CG  1 
ATOM   4710 C CD1 . TYR A 1 594 ? -37.291 -0.835  -15.806 1.00 16.21  ? 594  TYR A CD1 1 
ATOM   4711 C CD2 . TYR A 1 594 ? -36.492 -3.085  -16.018 1.00 15.46  ? 594  TYR A CD2 1 
ATOM   4712 C CE1 . TYR A 1 594 ? -37.555 -1.066  -14.423 1.00 14.16  ? 594  TYR A CE1 1 
ATOM   4713 C CE2 . TYR A 1 594 ? -36.729 -3.315  -14.681 1.00 15.98  ? 594  TYR A CE2 1 
ATOM   4714 C CZ  . TYR A 1 594 ? -37.255 -2.312  -13.891 1.00 14.61  ? 594  TYR A CZ  1 
ATOM   4715 O OH  . TYR A 1 594 ? -37.460 -2.620  -12.571 1.00 16.67  ? 594  TYR A OH  1 
ATOM   4716 N N   . PRO A 1 595 ? -36.420 0.492   -20.556 1.00 17.89  ? 595  PRO A N   1 
ATOM   4717 C CA  . PRO A 1 595 ? -35.784 0.747   -21.844 1.00 17.18  ? 595  PRO A CA  1 
ATOM   4718 C C   . PRO A 1 595 ? -34.557 -0.114  -22.138 1.00 18.31  ? 595  PRO A C   1 
ATOM   4719 O O   . PRO A 1 595 ? -34.368 -0.499  -23.289 1.00 19.05  ? 595  PRO A O   1 
ATOM   4720 C CB  . PRO A 1 595 ? -35.453 2.240   -21.825 1.00 17.02  ? 595  PRO A CB  1 
ATOM   4721 C CG  . PRO A 1 595 ? -36.080 2.803   -20.632 1.00 18.99  ? 595  PRO A CG  1 
ATOM   4722 C CD  . PRO A 1 595 ? -36.505 1.692   -19.699 1.00 17.82  ? 595  PRO A CD  1 
ATOM   4723 N N   . PHE A 1 596 ? -33.758 -0.410  -21.112 1.00 17.21  ? 596  PHE A N   1 
ATOM   4724 C CA  . PHE A 1 596 ? -32.739 -1.468  -21.167 1.00 17.04  ? 596  PHE A CA  1 
ATOM   4725 C C   . PHE A 1 596 ? -33.269 -2.601  -20.289 1.00 16.80  ? 596  PHE A C   1 
ATOM   4726 O O   . PHE A 1 596 ? -33.407 -2.422  -19.079 1.00 16.04  ? 596  PHE A O   1 
ATOM   4727 C CB  . PHE A 1 596 ? -31.410 -0.981  -20.584 1.00 17.14  ? 596  PHE A CB  1 
ATOM   4728 C CG  . PHE A 1 596 ? -30.378 -2.052  -20.490 1.00 17.74  ? 596  PHE A CG  1 
ATOM   4729 C CD1 . PHE A 1 596 ? -29.970 -2.715  -21.652 1.00 18.46  ? 596  PHE A CD1 1 
ATOM   4730 C CD2 . PHE A 1 596 ? -29.834 -2.438  -19.259 1.00 17.98  ? 596  PHE A CD2 1 
ATOM   4731 C CE1 . PHE A 1 596 ? -29.065 -3.726  -21.596 1.00 15.60  ? 596  PHE A CE1 1 
ATOM   4732 C CE2 . PHE A 1 596 ? -28.866 -3.460  -19.193 1.00 15.35  ? 596  PHE A CE2 1 
ATOM   4733 C CZ  . PHE A 1 596 ? -28.497 -4.107  -20.378 1.00 18.63  ? 596  PHE A CZ  1 
ATOM   4734 N N   . SER A 1 597 ? -33.587 -3.739  -20.922 1.00 16.71  ? 597  SER A N   1 
ATOM   4735 C CA  . SER A 1 597 ? -34.266 -4.909  -20.296 1.00 16.87  ? 597  SER A CA  1 
ATOM   4736 C C   . SER A 1 597 ? -33.278 -6.077  -20.189 1.00 17.05  ? 597  SER A C   1 
ATOM   4737 O O   . SER A 1 597 ? -33.048 -6.794  -21.183 1.00 18.11  ? 597  SER A O   1 
ATOM   4738 C CB  . SER A 1 597 ? -35.457 -5.344  -21.168 1.00 15.68  ? 597  SER A CB  1 
ATOM   4739 O OG  . SER A 1 597 ? -36.140 -6.427  -20.542 1.00 16.42  ? 597  SER A OG  1 
ATOM   4740 N N   . ARG A 1 598 ? -32.679 -6.252  -19.015 1.00 16.62  ? 598  ARG A N   1 
ATOM   4741 C CA  . ARG A 1 598 ? -31.738 -7.322  -18.785 1.00 16.08  ? 598  ARG A CA  1 
ATOM   4742 C C   . ARG A 1 598 ? -31.944 -8.012  -17.450 1.00 14.95  ? 598  ARG A C   1 
ATOM   4743 O O   . ARG A 1 598 ? -32.048 -7.361  -16.407 1.00 15.56  ? 598  ARG A O   1 
ATOM   4744 C CB  . ARG A 1 598 ? -30.281 -6.830  -18.889 1.00 15.08  ? 598  ARG A CB  1 
ATOM   4745 C CG  . ARG A 1 598 ? -29.311 -7.909  -18.561 1.00 17.41  ? 598  ARG A CG  1 
ATOM   4746 C CD  . ARG A 1 598 ? -27.891 -7.435  -18.728 1.00 13.34  ? 598  ARG A CD  1 
ATOM   4747 N NE  . ARG A 1 598 ? -27.471 -6.631  -17.579 1.00 18.73  ? 598  ARG A NE  1 
ATOM   4748 C CZ  . ARG A 1 598 ? -26.209 -6.497  -17.197 1.00 19.31  ? 598  ARG A CZ  1 
ATOM   4749 N NH1 . ARG A 1 598 ? -25.249 -7.026  -17.927 1.00 18.58  ? 598  ARG A NH1 1 
ATOM   4750 N NH2 . ARG A 1 598 ? -25.904 -5.783  -16.120 1.00 22.87  ? 598  ARG A NH2 1 
ATOM   4751 N N   . ASN A 1 599 ? -32.037 -9.333  -17.492 1.00 14.96  ? 599  ASN A N   1 
ATOM   4752 C CA  . ASN A 1 599 ? -32.084 -10.166 -16.290 1.00 16.60  ? 599  ASN A CA  1 
ATOM   4753 C C   . ASN A 1 599 ? -30.628 -10.583 -16.049 1.00 17.35  ? 599  ASN A C   1 
ATOM   4754 O O   . ASN A 1 599 ? -30.013 -11.259 -16.893 1.00 19.25  ? 599  ASN A O   1 
ATOM   4755 C CB  . ASN A 1 599 ? -32.987 -11.389 -16.579 1.00 15.99  ? 599  ASN A CB  1 
ATOM   4756 C CG  . ASN A 1 599 ? -33.091 -12.387 -15.406 1.00 17.62  ? 599  ASN A CG  1 
ATOM   4757 O OD1 . ASN A 1 599 ? -32.098 -12.752 -14.754 1.00 16.32  ? 599  ASN A OD1 1 
ATOM   4758 N ND2 . ASN A 1 599 ? -34.318 -12.855 -15.155 1.00 16.87  ? 599  ASN A ND2 1 
ATOM   4759 N N   . HIS A 1 600 ? -30.068 -10.154 -14.923 1.00 17.03  ? 600  HIS A N   1 
ATOM   4760 C CA  . HIS A 1 600 ? -28.700 -10.488 -14.559 1.00 17.77  ? 600  HIS A CA  1 
ATOM   4761 C C   . HIS A 1 600 ? -28.657 -10.922 -13.069 1.00 18.17  ? 600  HIS A C   1 
ATOM   4762 O O   . HIS A 1 600 ? -29.485 -10.484 -12.272 1.00 20.00  ? 600  HIS A O   1 
ATOM   4763 C CB  . HIS A 1 600 ? -27.853 -9.273  -14.860 1.00 17.81  ? 600  HIS A CB  1 
ATOM   4764 C CG  . HIS A 1 600 ? -26.426 -9.375  -14.429 1.00 16.20  ? 600  HIS A CG  1 
ATOM   4765 N ND1 . HIS A 1 600 ? -25.588 -10.396 -14.818 1.00 20.08  ? 600  HIS A ND1 1 
ATOM   4766 C CD2 . HIS A 1 600 ? -25.665 -8.521  -13.710 1.00 18.09  ? 600  HIS A CD2 1 
ATOM   4767 C CE1 . HIS A 1 600 ? -24.377 -10.194 -14.322 1.00 18.48  ? 600  HIS A CE1 1 
ATOM   4768 N NE2 . HIS A 1 600 ? -24.397 -9.057  -13.647 1.00 17.99  ? 600  HIS A NE2 1 
ATOM   4769 N N   . ASN A 1 601 ? -27.700 -11.781 -12.681 1.00 17.65  ? 601  ASN A N   1 
ATOM   4770 C CA  . ASN A 1 601 ? -27.732 -12.440 -11.384 1.00 16.58  ? 601  ASN A CA  1 
ATOM   4771 C C   . ASN A 1 601 ? -26.278 -12.547 -10.869 1.00 17.54  ? 601  ASN A C   1 
ATOM   4772 O O   . ASN A 1 601 ? -25.360 -12.633 -11.667 1.00 17.17  ? 601  ASN A O   1 
ATOM   4773 C CB  . ASN A 1 601 ? -28.312 -13.826 -11.577 1.00 16.33  ? 601  ASN A CB  1 
ATOM   4774 C CG  . ASN A 1 601 ? -28.573 -14.581 -10.264 1.00 17.10  ? 601  ASN A CG  1 
ATOM   4775 O OD1 . ASN A 1 601 ? -28.654 -14.005 -9.168  1.00 17.17  ? 601  ASN A OD1 1 
ATOM   4776 N ND2 . ASN A 1 601 ? -28.734 -15.895 -10.392 1.00 19.39  ? 601  ASN A ND2 1 
ATOM   4777 N N   . GLY A 1 602 ? -26.093 -12.503 -9.551  1.00 18.33  ? 602  GLY A N   1 
ATOM   4778 C CA  . GLY A 1 602 ? -24.745 -12.568 -8.954  1.00 18.42  ? 602  GLY A CA  1 
ATOM   4779 C C   . GLY A 1 602 ? -24.221 -14.005 -8.868  1.00 19.91  ? 602  GLY A C   1 
ATOM   4780 O O   . GLY A 1 602 ? -24.870 -14.957 -9.317  1.00 19.56  ? 602  GLY A O   1 
ATOM   4781 N N   . GLN A 1 603 ? -23.032 -14.144 -8.300  1.00 21.10  ? 603  GLN A N   1 
ATOM   4782 C CA  . GLN A 1 603 ? -22.339 -15.417 -8.263  1.00 23.24  ? 603  GLN A CA  1 
ATOM   4783 C C   . GLN A 1 603 ? -23.002 -16.321 -7.238  1.00 23.91  ? 603  GLN A C   1 
ATOM   4784 O O   . GLN A 1 603 ? -23.338 -15.864 -6.154  1.00 24.25  ? 603  GLN A O   1 
ATOM   4785 C CB  . GLN A 1 603 ? -20.880 -15.178 -7.886  1.00 24.10  ? 603  GLN A CB  1 
ATOM   4786 C CG  . GLN A 1 603 ? -20.103 -16.451 -7.612  1.00 28.64  ? 603  GLN A CG  1 
ATOM   4787 C CD  . GLN A 1 603 ? -18.625 -16.186 -7.377  1.00 33.68  ? 603  GLN A CD  1 
ATOM   4788 O OE1 . GLN A 1 603 ? -18.229 -15.180 -6.775  1.00 36.02  ? 603  GLN A OE1 1 
ATOM   4789 N NE2 . GLN A 1 603 ? -17.798 -17.103 -7.847  1.00 36.77  ? 603  GLN A NE2 1 
ATOM   4790 N N   . GLY A 1 604 ? -23.230 -17.584 -7.611  1.00 24.49  ? 604  GLY A N   1 
ATOM   4791 C CA  . GLY A 1 604 ? -23.656 -18.623 -6.656  1.00 24.94  ? 604  GLY A CA  1 
ATOM   4792 C C   . GLY A 1 604 ? -25.132 -18.704 -6.361  1.00 25.66  ? 604  GLY A C   1 
ATOM   4793 O O   . GLY A 1 604 ? -25.587 -19.756 -5.926  1.00 25.76  ? 604  GLY A O   1 
ATOM   4794 N N   . TYR A 1 605 ? -25.892 -17.632 -6.615  1.00 24.91  ? 605  TYR A N   1 
ATOM   4795 C CA  . TYR A 1 605 ? -27.321 -17.614 -6.311  1.00 25.33  ? 605  TYR A CA  1 
ATOM   4796 C C   . TYR A 1 605 ? -28.101 -18.528 -7.253  1.00 25.75  ? 605  TYR A C   1 
ATOM   4797 O O   . TYR A 1 605 ? -27.642 -18.847 -8.345  1.00 26.14  ? 605  TYR A O   1 
ATOM   4798 C CB  . TYR A 1 605 ? -27.899 -16.182 -6.299  1.00 25.37  ? 605  TYR A CB  1 
ATOM   4799 C CG  . TYR A 1 605 ? -27.082 -15.254 -5.431  1.00 25.36  ? 605  TYR A CG  1 
ATOM   4800 C CD1 . TYR A 1 605 ? -27.054 -15.407 -4.040  1.00 25.16  ? 605  TYR A CD1 1 
ATOM   4801 C CD2 . TYR A 1 605 ? -26.297 -14.259 -5.999  1.00 23.71  ? 605  TYR A CD2 1 
ATOM   4802 C CE1 . TYR A 1 605 ? -26.277 -14.570 -3.244  1.00 26.76  ? 605  TYR A CE1 1 
ATOM   4803 C CE2 . TYR A 1 605 ? -25.511 -13.433 -5.219  1.00 25.37  ? 605  TYR A CE2 1 
ATOM   4804 C CZ  . TYR A 1 605 ? -25.506 -13.599 -3.843  1.00 26.02  ? 605  TYR A CZ  1 
ATOM   4805 O OH  . TYR A 1 605 ? -24.741 -12.759 -3.080  1.00 28.33  ? 605  TYR A OH  1 
ATOM   4806 N N   . LYS A 1 606 ? -29.274 -18.956 -6.813  1.00 25.71  ? 606  LYS A N   1 
ATOM   4807 C CA  . LYS A 1 606 ? -30.080 -19.871 -7.601  1.00 27.56  ? 606  LYS A CA  1 
ATOM   4808 C C   . LYS A 1 606 ? -30.359 -19.203 -8.951  1.00 26.56  ? 606  LYS A C   1 
ATOM   4809 O O   . LYS A 1 606 ? -30.433 -17.977 -9.032  1.00 25.86  ? 606  LYS A O   1 
ATOM   4810 C CB  . LYS A 1 606 ? -31.344 -20.254 -6.827  1.00 27.78  ? 606  LYS A CB  1 
ATOM   4811 C CG  . LYS A 1 606 ? -32.623 -19.687 -7.335  1.00 30.71  ? 606  LYS A CG  1 
ATOM   4812 C CD  . LYS A 1 606 ? -33.826 -20.305 -6.583  1.00 31.73  ? 606  LYS A CD  1 
ATOM   4813 C CE  . LYS A 1 606 ? -35.151 -19.824 -7.208  1.00 39.22  ? 606  LYS A CE  1 
ATOM   4814 N NZ  . LYS A 1 606 ? -36.268 -19.673 -6.207  1.00 43.44  ? 606  LYS A NZ  1 
ATOM   4815 N N   . ASP A 1 607 ? -30.440 -19.995 -10.015 1.00 25.66  ? 607  ASP A N   1 
ATOM   4816 C CA  . ASP A 1 607 ? -30.724 -19.469 -11.345 1.00 25.21  ? 607  ASP A CA  1 
ATOM   4817 C C   . ASP A 1 607 ? -32.015 -18.647 -11.325 1.00 23.69  ? 607  ASP A C   1 
ATOM   4818 O O   . ASP A 1 607 ? -32.982 -18.982 -10.636 1.00 23.91  ? 607  ASP A O   1 
ATOM   4819 C CB  . ASP A 1 607 ? -30.878 -20.601 -12.366 1.00 24.92  ? 607  ASP A CB  1 
ATOM   4820 C CG  . ASP A 1 607 ? -29.640 -21.419 -12.517 1.00 26.89  ? 607  ASP A CG  1 
ATOM   4821 O OD1 . ASP A 1 607 ? -28.550 -20.927 -12.137 1.00 30.84  ? 607  ASP A OD1 1 
ATOM   4822 O OD2 . ASP A 1 607 ? -29.744 -22.561 -13.039 1.00 27.42  ? 607  ASP A OD2 1 
ATOM   4823 N N   . GLN A 1 608 ? -32.028 -17.577 -12.111 1.00 22.91  ? 608  GLN A N   1 
ATOM   4824 C CA  . GLN A 1 608 ? -33.225 -16.754 -12.219 1.00 21.70  ? 608  GLN A CA  1 
ATOM   4825 C C   . GLN A 1 608 ? -33.535 -16.367 -13.658 1.00 21.31  ? 608  GLN A C   1 
ATOM   4826 O O   . GLN A 1 608 ? -34.371 -15.509 -13.891 1.00 19.77  ? 608  GLN A O   1 
ATOM   4827 C CB  . GLN A 1 608 ? -33.110 -15.523 -11.300 1.00 21.50  ? 608  GLN A CB  1 
ATOM   4828 C CG  . GLN A 1 608 ? -32.040 -14.551 -11.674 1.00 21.54  ? 608  GLN A CG  1 
ATOM   4829 C CD  . GLN A 1 608 ? -31.831 -13.444 -10.621 1.00 21.84  ? 608  GLN A CD  1 
ATOM   4830 O OE1 . GLN A 1 608 ? -31.846 -13.703 -9.415  1.00 22.72  ? 608  GLN A OE1 1 
ATOM   4831 N NE2 . GLN A 1 608 ? -31.637 -12.209 -11.086 1.00 19.17  ? 608  GLN A NE2 1 
ATOM   4832 N N   . ASP A 1 609 ? -32.857 -17.003 -14.625 1.00 20.15  ? 609  ASP A N   1 
ATOM   4833 C CA  . ASP A 1 609 ? -33.255 -16.867 -15.993 1.00 19.84  ? 609  ASP A CA  1 
ATOM   4834 C C   . ASP A 1 609 ? -34.705 -17.353 -16.112 1.00 19.45  ? 609  ASP A C   1 
ATOM   4835 O O   . ASP A 1 609 ? -35.140 -18.232 -15.368 1.00 20.17  ? 609  ASP A O   1 
ATOM   4836 C CB  . ASP A 1 609 ? -32.340 -17.645 -16.937 1.00 20.81  ? 609  ASP A CB  1 
ATOM   4837 C CG  . ASP A 1 609 ? -32.299 -19.117 -16.620 1.00 21.55  ? 609  ASP A CG  1 
ATOM   4838 O OD1 . ASP A 1 609 ? -31.552 -19.497 -15.700 1.00 21.78  ? 609  ASP A OD1 1 
ATOM   4839 O OD2 . ASP A 1 609 ? -32.983 -19.893 -17.321 1.00 22.07  ? 609  ASP A OD2 1 
ATOM   4840 N N   . PRO A 1 610 ? -35.483 -16.730 -16.990 1.00 18.74  ? 610  PRO A N   1 
ATOM   4841 C CA  . PRO A 1 610 ? -36.918 -17.064 -17.005 1.00 19.46  ? 610  PRO A CA  1 
ATOM   4842 C C   . PRO A 1 610 ? -37.270 -18.574 -17.111 1.00 20.28  ? 610  PRO A C   1 
ATOM   4843 O O   . PRO A 1 610 ? -38.110 -19.053 -16.344 1.00 20.11  ? 610  PRO A O   1 
ATOM   4844 C CB  . PRO A 1 610 ? -37.436 -16.250 -18.196 1.00 18.64  ? 610  PRO A CB  1 
ATOM   4845 C CG  . PRO A 1 610 ? -36.532 -15.036 -18.218 1.00 19.73  ? 610  PRO A CG  1 
ATOM   4846 C CD  . PRO A 1 610 ? -35.165 -15.656 -17.956 1.00 18.89  ? 610  PRO A CD  1 
ATOM   4847 N N   . ALA A 1 611 ? -36.609 -19.313 -18.006 1.00 20.99  ? 611  ALA A N   1 
ATOM   4848 C CA  . ALA A 1 611 ? -36.965 -20.725 -18.241 1.00 21.43  ? 611  ALA A CA  1 
ATOM   4849 C C   . ALA A 1 611 ? -36.569 -21.654 -17.085 1.00 22.49  ? 611  ALA A C   1 
ATOM   4850 O O   . ALA A 1 611 ? -37.115 -22.766 -16.965 1.00 22.51  ? 611  ALA A O   1 
ATOM   4851 C CB  . ALA A 1 611 ? -36.400 -21.215 -19.561 1.00 20.23  ? 611  ALA A CB  1 
ATOM   4852 N N   . SER A 1 612 ? -35.685 -21.175 -16.191 1.00 23.39  ? 612  SER A N   1 
ATOM   4853 C CA  . SER A 1 612 ? -35.300 -21.928 -14.977 1.00 24.09  ? 612  SER A CA  1 
ATOM   4854 C C   . SER A 1 612 ? -36.467 -22.177 -14.011 1.00 25.36  ? 612  SER A C   1 
ATOM   4855 O O   . SER A 1 612 ? -36.433 -23.106 -13.199 1.00 25.36  ? 612  SER A O   1 
ATOM   4856 C CB  . SER A 1 612 ? -34.129 -21.257 -14.249 1.00 24.27  ? 612  SER A CB  1 
ATOM   4857 O OG  . SER A 1 612 ? -34.583 -20.129 -13.505 1.00 25.83  ? 612  SER A OG  1 
ATOM   4858 N N   . PHE A 1 613 ? -37.524 -21.376 -14.128 1.00 25.43  ? 613  PHE A N   1 
ATOM   4859 C CA  . PHE A 1 613 ? -38.705 -21.559 -13.272 1.00 25.86  ? 613  PHE A CA  1 
ATOM   4860 C C   . PHE A 1 613 ? -39.636 -22.667 -13.705 1.00 26.94  ? 613  PHE A C   1 
ATOM   4861 O O   . PHE A 1 613 ? -40.680 -22.932 -13.055 1.00 27.67  ? 613  PHE A O   1 
ATOM   4862 C CB  . PHE A 1 613 ? -39.432 -20.222 -13.110 1.00 25.24  ? 613  PHE A CB  1 
ATOM   4863 C CG  . PHE A 1 613 ? -38.600 -19.216 -12.379 1.00 23.65  ? 613  PHE A CG  1 
ATOM   4864 C CD1 . PHE A 1 613 ? -38.778 -19.014 -11.022 1.00 24.38  ? 613  PHE A CD1 1 
ATOM   4865 C CD2 . PHE A 1 613 ? -37.589 -18.514 -13.046 1.00 22.86  ? 613  PHE A CD2 1 
ATOM   4866 C CE1 . PHE A 1 613 ? -37.955 -18.080 -10.327 1.00 25.87  ? 613  PHE A CE1 1 
ATOM   4867 C CE2 . PHE A 1 613 ? -36.786 -17.569 -12.373 1.00 21.89  ? 613  PHE A CE2 1 
ATOM   4868 C CZ  . PHE A 1 613 ? -36.970 -17.368 -11.019 1.00 23.15  ? 613  PHE A CZ  1 
ATOM   4869 N N   . GLY A 1 614 ? -39.278 -23.312 -14.809 1.00 27.85  ? 614  GLY A N   1 
ATOM   4870 C CA  . GLY A 1 614 ? -40.090 -24.390 -15.341 1.00 28.43  ? 614  GLY A CA  1 
ATOM   4871 C C   . GLY A 1 614 ? -40.720 -24.077 -16.677 1.00 29.57  ? 614  GLY A C   1 
ATOM   4872 O O   . GLY A 1 614 ? -41.240 -22.969 -16.904 1.00 28.45  ? 614  GLY A O   1 
ATOM   4873 N N   . ALA A 1 615 ? -40.679 -25.068 -17.566 1.00 30.26  ? 615  ALA A N   1 
ATOM   4874 C CA  . ALA A 1 615 ? -41.171 -24.915 -18.931 1.00 31.63  ? 615  ALA A CA  1 
ATOM   4875 C C   . ALA A 1 615 ? -42.614 -24.493 -18.991 1.00 32.28  ? 615  ALA A C   1 
ATOM   4876 O O   . ALA A 1 615 ? -43.017 -23.869 -19.973 1.00 33.61  ? 615  ALA A O   1 
ATOM   4877 C CB  . ALA A 1 615 ? -40.990 -26.205 -19.715 1.00 32.57  ? 615  ALA A CB  1 
ATOM   4878 N N   . ASP A 1 616 ? -43.398 -24.845 -17.975 1.00 32.31  ? 616  ASP A N   1 
ATOM   4879 C CA  . ASP A 1 616 ? -44.827 -24.539 -17.985 1.00 32.77  ? 616  ASP A CA  1 
ATOM   4880 C C   . ASP A 1 616 ? -45.243 -23.638 -16.816 1.00 30.65  ? 616  ASP A C   1 
ATOM   4881 O O   . ASP A 1 616 ? -46.421 -23.558 -16.468 1.00 30.92  ? 616  ASP A O   1 
ATOM   4882 C CB  . ASP A 1 616 ? -45.676 -25.836 -18.043 1.00 34.42  ? 616  ASP A CB  1 
ATOM   4883 C CG  . ASP A 1 616 ? -45.668 -26.501 -19.449 1.00 40.20  ? 616  ASP A CG  1 
ATOM   4884 O OD1 . ASP A 1 616 ? -45.390 -27.732 -19.549 1.00 45.29  ? 616  ASP A OD1 1 
ATOM   4885 O OD2 . ASP A 1 616 ? -45.933 -25.796 -20.467 1.00 45.10  ? 616  ASP A OD2 1 
ATOM   4886 N N   . SER A 1 617 ? -44.273 -22.938 -16.232 1.00 28.44  ? 617  SER A N   1 
ATOM   4887 C CA  . SER A 1 617 ? -44.514 -22.095 -15.053 1.00 26.07  ? 617  SER A CA  1 
ATOM   4888 C C   . SER A 1 617 ? -45.254 -20.827 -15.396 1.00 24.40  ? 617  SER A C   1 
ATOM   4889 O O   . SER A 1 617 ? -45.165 -20.342 -16.513 1.00 23.75  ? 617  SER A O   1 
ATOM   4890 C CB  . SER A 1 617 ? -43.198 -21.715 -14.404 1.00 25.36  ? 617  SER A CB  1 
ATOM   4891 O OG  . SER A 1 617 ? -42.362 -20.984 -15.295 1.00 24.75  ? 617  SER A OG  1 
ATOM   4892 N N   . LEU A 1 618 ? -45.979 -20.289 -14.419 1.00 23.95  ? 618  LEU A N   1 
ATOM   4893 C CA  . LEU A 1 618 ? -46.581 -18.973 -14.545 1.00 23.43  ? 618  LEU A CA  1 
ATOM   4894 C C   . LEU A 1 618 ? -45.545 -17.869 -14.859 1.00 22.83  ? 618  LEU A C   1 
ATOM   4895 O O   . LEU A 1 618 ? -45.813 -16.984 -15.660 1.00 21.69  ? 618  LEU A O   1 
ATOM   4896 C CB  . LEU A 1 618 ? -47.403 -18.628 -13.294 1.00 23.75  ? 618  LEU A CB  1 
ATOM   4897 C CG  . LEU A 1 618 ? -48.100 -17.269 -13.371 1.00 24.28  ? 618  LEU A CG  1 
ATOM   4898 C CD1 . LEU A 1 618 ? -49.071 -17.207 -14.551 1.00 28.75  ? 618  LEU A CD1 1 
ATOM   4899 C CD2 . LEU A 1 618 ? -48.803 -16.953 -12.067 1.00 27.74  ? 618  LEU A CD2 1 
ATOM   4900 N N   . LEU A 1 619 ? -44.361 -17.943 -14.258 1.00 22.17  ? 619  LEU A N   1 
ATOM   4901 C CA  . LEU A 1 619 ? -43.331 -16.934 -14.490 1.00 21.51  ? 619  LEU A CA  1 
ATOM   4902 C C   . LEU A 1 619 ? -42.888 -16.962 -15.939 1.00 21.49  ? 619  LEU A C   1 
ATOM   4903 O O   . LEU A 1 619 ? -42.809 -15.921 -16.589 1.00 21.81  ? 619  LEU A O   1 
ATOM   4904 C CB  . LEU A 1 619 ? -42.122 -17.133 -13.551 1.00 21.38  ? 619  LEU A CB  1 
ATOM   4905 C CG  . LEU A 1 619 ? -41.015 -16.085 -13.667 1.00 20.84  ? 619  LEU A CG  1 
ATOM   4906 C CD1 . LEU A 1 619 ? -40.247 -15.933 -12.348 1.00 19.28  ? 619  LEU A CD1 1 
ATOM   4907 C CD2 . LEU A 1 619 ? -40.034 -16.322 -14.859 1.00 20.96  ? 619  LEU A CD2 1 
ATOM   4908 N N   . LEU A 1 620 ? -42.602 -18.154 -16.466 1.00 21.62  ? 620  LEU A N   1 
ATOM   4909 C CA  . LEU A 1 620 ? -42.144 -18.253 -17.837 1.00 21.43  ? 620  LEU A CA  1 
ATOM   4910 C C   . LEU A 1 620 ? -43.246 -17.794 -18.783 1.00 20.08  ? 620  LEU A C   1 
ATOM   4911 O O   . LEU A 1 620 ? -42.999 -17.011 -19.701 1.00 18.00  ? 620  LEU A O   1 
ATOM   4912 C CB  . LEU A 1 620 ? -41.697 -19.686 -18.184 1.00 22.27  ? 620  LEU A CB  1 
ATOM   4913 C CG  . LEU A 1 620 ? -41.175 -19.824 -19.615 1.00 23.62  ? 620  LEU A CG  1 
ATOM   4914 C CD1 . LEU A 1 620 ? -39.987 -18.883 -19.863 1.00 24.22  ? 620  LEU A CD1 1 
ATOM   4915 C CD2 . LEU A 1 620 ? -40.773 -21.285 -19.915 1.00 24.00  ? 620  LEU A CD2 1 
ATOM   4916 N N   . ASN A 1 621 ? -44.464 -18.270 -18.560 1.00 20.59  ? 621  ASN A N   1 
ATOM   4917 C CA  . ASN A 1 621 ? -45.570 -17.888 -19.441 1.00 21.57  ? 621  ASN A CA  1 
ATOM   4918 C C   . ASN A 1 621 ? -45.767 -16.389 -19.471 1.00 21.01  ? 621  ASN A C   1 
ATOM   4919 O O   . ASN A 1 621 ? -45.911 -15.792 -20.553 1.00 21.80  ? 621  ASN A O   1 
ATOM   4920 C CB  . ASN A 1 621 ? -46.892 -18.567 -19.032 1.00 22.66  ? 621  ASN A CB  1 
ATOM   4921 C CG  . ASN A 1 621 ? -46.869 -20.072 -19.269 1.00 28.47  ? 621  ASN A CG  1 
ATOM   4922 O OD1 . ASN A 1 621 ? -46.122 -20.579 -20.118 1.00 34.24  ? 621  ASN A OD1 1 
ATOM   4923 N ND2 . ASN A 1 621 ? -47.716 -20.802 -18.525 1.00 36.95  ? 621  ASN A ND2 1 
ATOM   4924 N N   . SER A 1 622 ? -45.775 -15.776 -18.295 1.00 21.06  ? 622  SER A N   1 
ATOM   4925 C CA  . SER A 1 622 ? -46.010 -14.339 -18.227 1.00 21.09  ? 622  SER A CA  1 
ATOM   4926 C C   . SER A 1 622 ? -44.850 -13.517 -18.792 1.00 19.86  ? 622  SER A C   1 
ATOM   4927 O O   . SER A 1 622 ? -45.060 -12.520 -19.516 1.00 18.18  ? 622  SER A O   1 
ATOM   4928 C CB  . SER A 1 622 ? -46.332 -13.928 -16.810 1.00 22.13  ? 622  SER A CB  1 
ATOM   4929 O OG  . SER A 1 622 ? -46.614 -12.548 -16.826 1.00 27.85  ? 622  SER A OG  1 
ATOM   4930 N N   . SER A 1 623 ? -43.626 -13.931 -18.461 1.00 18.32  ? 623  SER A N   1 
ATOM   4931 C CA  . SER A 1 623 ? -42.456 -13.342 -19.068 1.00 19.25  ? 623  SER A CA  1 
ATOM   4932 C C   . SER A 1 623 ? -42.508 -13.328 -20.572 1.00 18.53  ? 623  SER A C   1 
ATOM   4933 O O   . SER A 1 623 ? -42.254 -12.297 -21.198 1.00 19.30  ? 623  SER A O   1 
ATOM   4934 C CB  . SER A 1 623 ? -41.191 -14.084 -18.614 1.00 19.59  ? 623  SER A CB  1 
ATOM   4935 O OG  . SER A 1 623 ? -41.067 -13.988 -17.223 1.00 21.02  ? 623  SER A OG  1 
ATOM   4936 N N   . ARG A 1 624 ? -42.787 -14.488 -21.177 1.00 18.90  ? 624  ARG A N   1 
ATOM   4937 C CA  . ARG A 1 624 ? -42.817 -14.583 -22.620 1.00 18.91  ? 624  ARG A CA  1 
ATOM   4938 C C   . ARG A 1 624 ? -43.932 -13.681 -23.136 1.00 18.29  ? 624  ARG A C   1 
ATOM   4939 O O   . ARG A 1 624 ? -43.766 -13.002 -24.123 1.00 17.26  ? 624  ARG A O   1 
ATOM   4940 C CB  . ARG A 1 624 ? -43.068 -16.043 -23.079 1.00 18.74  ? 624  ARG A CB  1 
ATOM   4941 C CG  . ARG A 1 624 ? -43.134 -16.233 -24.594 1.00 19.27  ? 624  ARG A CG  1 
ATOM   4942 C CD  . ARG A 1 624 ? -43.191 -17.748 -24.944 1.00 22.07  ? 624  ARG A CD  1 
ATOM   4943 N NE  . ARG A 1 624 ? -44.183 -18.353 -24.071 1.00 26.88  ? 624  ARG A NE  1 
ATOM   4944 C CZ  . ARG A 1 624 ? -44.035 -19.437 -23.324 1.00 27.55  ? 624  ARG A CZ  1 
ATOM   4945 N NH1 . ARG A 1 624 ? -42.927 -20.189 -23.336 1.00 27.74  ? 624  ARG A NH1 1 
ATOM   4946 N NH2 . ARG A 1 624 ? -45.061 -19.789 -22.566 1.00 29.59  ? 624  ARG A NH2 1 
ATOM   4947 N N   . HIS A 1 625 ? -45.050 -13.666 -22.426 1.00 18.46  ? 625  HIS A N   1 
ATOM   4948 C CA  . HIS A 1 625 ? -46.210 -12.897 -22.863 1.00 18.22  ? 625  HIS A CA  1 
ATOM   4949 C C   . HIS A 1 625 ? -45.889 -11.401 -22.961 1.00 17.60  ? 625  HIS A C   1 
ATOM   4950 O O   . HIS A 1 625 ? -46.159 -10.753 -23.995 1.00 16.29  ? 625  HIS A O   1 
ATOM   4951 C CB  . HIS A 1 625 ? -47.359 -13.101 -21.885 1.00 18.85  ? 625  HIS A CB  1 
ATOM   4952 C CG  . HIS A 1 625 ? -48.616 -12.408 -22.307 1.00 19.93  ? 625  HIS A CG  1 
ATOM   4953 N ND1 . HIS A 1 625 ? -49.111 -11.310 -21.643 1.00 22.54  ? 625  HIS A ND1 1 
ATOM   4954 C CD2 . HIS A 1 625 ? -49.448 -12.621 -23.355 1.00 23.15  ? 625  HIS A CD2 1 
ATOM   4955 C CE1 . HIS A 1 625 ? -50.218 -10.893 -22.239 1.00 23.32  ? 625  HIS A CE1 1 
ATOM   4956 N NE2 . HIS A 1 625 ? -50.434 -11.659 -23.293 1.00 25.54  ? 625  HIS A NE2 1 
ATOM   4957 N N   . TYR A 1 626 ? -45.323 -10.856 -21.884 1.00 17.18  ? 626  TYR A N   1 
ATOM   4958 C CA  . TYR A 1 626 ? -45.051 -9.422  -21.823 1.00 16.74  ? 626  TYR A CA  1 
ATOM   4959 C C   . TYR A 1 626 ? -43.821 -9.058  -22.623 1.00 15.24  ? 626  TYR A C   1 
ATOM   4960 O O   . TYR A 1 626 ? -43.769 -7.965  -23.195 1.00 15.21  ? 626  TYR A O   1 
ATOM   4961 C CB  . TYR A 1 626 ? -44.992 -8.903  -20.363 1.00 16.30  ? 626  TYR A CB  1 
ATOM   4962 C CG  . TYR A 1 626 ? -46.389 -8.772  -19.824 1.00 18.76  ? 626  TYR A CG  1 
ATOM   4963 C CD1 . TYR A 1 626 ? -46.867 -9.628  -18.820 1.00 16.95  ? 626  TYR A CD1 1 
ATOM   4964 C CD2 . TYR A 1 626 ? -47.255 -7.852  -20.379 1.00 16.37  ? 626  TYR A CD2 1 
ATOM   4965 C CE1 . TYR A 1 626 ? -48.207 -9.544  -18.378 1.00 16.58  ? 626  TYR A CE1 1 
ATOM   4966 C CE2 . TYR A 1 626 ? -48.605 -7.757  -19.943 1.00 18.36  ? 626  TYR A CE2 1 
ATOM   4967 C CZ  . TYR A 1 626 ? -49.039 -8.609  -18.930 1.00 15.73  ? 626  TYR A CZ  1 
ATOM   4968 O OH  . TYR A 1 626 ? -50.341 -8.521  -18.477 1.00 21.09  ? 626  TYR A OH  1 
ATOM   4969 N N   . LEU A 1 627 ? -42.850 -9.968  -22.715 1.00 15.31  ? 627  LEU A N   1 
ATOM   4970 C CA  . LEU A 1 627 ? -41.768 -9.727  -23.672 1.00 15.38  ? 627  LEU A CA  1 
ATOM   4971 C C   . LEU A 1 627 ? -42.290 -9.720  -25.106 1.00 16.19  ? 627  LEU A C   1 
ATOM   4972 O O   . LEU A 1 627 ? -41.793 -8.957  -25.938 1.00 16.60  ? 627  LEU A O   1 
ATOM   4973 C CB  . LEU A 1 627 ? -40.593 -10.706 -23.501 1.00 13.05  ? 627  LEU A CB  1 
ATOM   4974 C CG  . LEU A 1 627 ? -39.750 -10.400 -22.256 1.00 14.73  ? 627  LEU A CG  1 
ATOM   4975 C CD1 . LEU A 1 627 ? -38.797 -11.564 -22.024 1.00 15.85  ? 627  LEU A CD1 1 
ATOM   4976 C CD2 . LEU A 1 627 ? -39.036 -9.048  -22.446 1.00 14.76  ? 627  LEU A CD2 1 
ATOM   4977 N N   . ASN A 1 628 ? -43.299 -10.539 -25.411 1.00 16.29  ? 628  ASN A N   1 
ATOM   4978 C CA  . ASN A 1 628 ? -43.822 -10.510 -26.748 1.00 16.64  ? 628  ASN A CA  1 
ATOM   4979 C C   . ASN A 1 628 ? -44.548 -9.185  -27.021 1.00 15.04  ? 628  ASN A C   1 
ATOM   4980 O O   . ASN A 1 628 ? -44.548 -8.699  -28.144 1.00 14.54  ? 628  ASN A O   1 
ATOM   4981 C CB  . ASN A 1 628 ? -44.725 -11.691 -27.040 1.00 17.43  ? 628  ASN A CB  1 
ATOM   4982 C CG  . ASN A 1 628 ? -43.964 -12.889 -27.557 1.00 20.26  ? 628  ASN A CG  1 
ATOM   4983 O OD1 . ASN A 1 628 ? -44.278 -14.040 -27.207 1.00 24.56  ? 628  ASN A OD1 1 
ATOM   4984 N ND2 . ASN A 1 628 ? -42.951 -12.633 -28.356 1.00 19.21  ? 628  ASN A ND2 1 
ATOM   4985 N N   . ILE A 1 629 ? -45.157 -8.608  -25.982 1.00 14.90  ? 629  ILE A N   1 
ATOM   4986 C CA  . ILE A 1 629 ? -45.731 -7.269  -26.116 1.00 13.81  ? 629  ILE A CA  1 
ATOM   4987 C C   . ILE A 1 629 ? -44.632 -6.225  -26.306 1.00 13.65  ? 629  ILE A C   1 
ATOM   4988 O O   . ILE A 1 629 ? -44.725 -5.351  -27.152 1.00 12.92  ? 629  ILE A O   1 
ATOM   4989 C CB  . ILE A 1 629 ? -46.634 -6.921  -24.908 1.00 14.20  ? 629  ILE A CB  1 
ATOM   4990 C CG1 . ILE A 1 629 ? -47.911 -7.790  -24.989 1.00 12.85  ? 629  ILE A CG1 1 
ATOM   4991 C CG2 . ILE A 1 629 ? -46.925 -5.398  -24.921 1.00 14.54  ? 629  ILE A CG2 1 
ATOM   4992 C CD1 . ILE A 1 629 ? -48.761 -7.783  -23.695 1.00 15.86  ? 629  ILE A CD1 1 
ATOM   4993 N N   . ARG A 1 630 ? -43.595 -6.292  -25.491 1.00 12.99  ? 630  ARG A N   1 
ATOM   4994 C CA  . ARG A 1 630 ? -42.441 -5.374  -25.744 1.00 12.87  ? 630  ARG A CA  1 
ATOM   4995 C C   . ARG A 1 630 ? -41.971 -5.419  -27.170 1.00 12.26  ? 630  ARG A C   1 
ATOM   4996 O O   . ARG A 1 630 ? -41.864 -4.368  -27.820 1.00 12.91  ? 630  ARG A O   1 
ATOM   4997 C CB  . ARG A 1 630 ? -41.287 -5.694  -24.809 1.00 12.25  ? 630  ARG A CB  1 
ATOM   4998 C CG  . ARG A 1 630 ? -40.002 -4.848  -25.146 1.00 12.07  ? 630  ARG A CG  1 
ATOM   4999 C CD  . ARG A 1 630 ? -38.768 -5.465  -24.501 1.00 14.10  ? 630  ARG A CD  1 
ATOM   5000 N NE  . ARG A 1 630 ? -37.628 -4.556  -24.616 1.00 13.13  ? 630  ARG A NE  1 
ATOM   5001 C CZ  . ARG A 1 630 ? -37.397 -3.535  -23.775 1.00 17.02  ? 630  ARG A CZ  1 
ATOM   5002 N NH1 . ARG A 1 630 ? -38.235 -3.287  -22.750 1.00 16.13  ? 630  ARG A NH1 1 
ATOM   5003 N NH2 . ARG A 1 630 ? -36.340 -2.756  -23.946 1.00 16.25  ? 630  ARG A NH2 1 
ATOM   5004 N N   . TYR A 1 631 ? -41.683 -6.621  -27.695 1.00 12.94  ? 631  TYR A N   1 
ATOM   5005 C CA  . TYR A 1 631 ? -41.195 -6.755  -29.070 1.00 13.63  ? 631  TYR A CA  1 
ATOM   5006 C C   . TYR A 1 631 ? -42.186 -6.234  -30.124 1.00 13.38  ? 631  TYR A C   1 
ATOM   5007 O O   . TYR A 1 631 ? -41.823 -5.556  -31.063 1.00 14.45  ? 631  TYR A O   1 
ATOM   5008 C CB  . TYR A 1 631 ? -40.866 -8.219  -29.337 1.00 13.45  ? 631  TYR A CB  1 
ATOM   5009 C CG  . TYR A 1 631 ? -39.472 -8.587  -28.865 1.00 16.32  ? 631  TYR A CG  1 
ATOM   5010 C CD1 . TYR A 1 631 ? -39.057 -8.340  -27.552 1.00 17.34  ? 631  TYR A CD1 1 
ATOM   5011 C CD2 . TYR A 1 631 ? -38.552 -9.150  -29.756 1.00 17.58  ? 631  TYR A CD2 1 
ATOM   5012 C CE1 . TYR A 1 631 ? -37.744 -8.680  -27.120 1.00 16.93  ? 631  TYR A CE1 1 
ATOM   5013 C CE2 . TYR A 1 631 ? -37.230 -9.496  -29.326 1.00 18.92  ? 631  TYR A CE2 1 
ATOM   5014 C CZ  . TYR A 1 631 ? -36.850 -9.238  -28.035 1.00 17.76  ? 631  TYR A CZ  1 
ATOM   5015 O OH  . TYR A 1 631 ? -35.580 -9.599  -27.640 1.00 17.62  ? 631  TYR A OH  1 
ATOM   5016 N N   . THR A 1 632 ? -43.470 -6.493  -29.903 1.00 14.15  ? 632  THR A N   1 
ATOM   5017 C CA  . THR A 1 632 ? -44.515 -5.934  -30.782 1.00 14.72  ? 632  THR A CA  1 
ATOM   5018 C C   . THR A 1 632 ? -44.436 -4.415  -30.869 1.00 15.02  ? 632  THR A C   1 
ATOM   5019 O O   . THR A 1 632 ? -44.640 -3.826  -31.933 1.00 15.89  ? 632  THR A O   1 
ATOM   5020 C CB  . THR A 1 632 ? -45.925 -6.310  -30.224 1.00 15.07  ? 632  THR A CB  1 
ATOM   5021 O OG1 . THR A 1 632 ? -46.041 -7.731  -30.096 1.00 16.54  ? 632  THR A OG1 1 
ATOM   5022 C CG2 . THR A 1 632 ? -47.066 -5.767  -31.132 1.00 17.23  ? 632  THR A CG2 1 
ATOM   5023 N N   . LEU A 1 633 ? -44.139 -3.770  -29.741 1.00 14.53  ? 633  LEU A N   1 
ATOM   5024 C CA  . LEU A 1 633 ? -44.090 -2.299  -29.676 1.00 14.69  ? 633  LEU A CA  1 
ATOM   5025 C C   . LEU A 1 633 ? -42.701 -1.778  -29.933 1.00 14.72  ? 633  LEU A C   1 
ATOM   5026 O O   . LEU A 1 633 ? -42.474 -0.602  -29.775 1.00 14.63  ? 633  LEU A O   1 
ATOM   5027 C CB  . LEU A 1 633 ? -44.532 -1.774  -28.300 1.00 13.60  ? 633  LEU A CB  1 
ATOM   5028 C CG  . LEU A 1 633 ? -46.057 -2.033  -28.065 1.00 13.51  ? 633  LEU A CG  1 
ATOM   5029 C CD1 . LEU A 1 633 ? -46.349 -1.839  -26.573 1.00 11.91  ? 633  LEU A CD1 1 
ATOM   5030 C CD2 . LEU A 1 633 ? -46.782 -1.031  -28.900 1.00 16.40  ? 633  LEU A CD2 1 
ATOM   5031 N N   . LEU A 1 634 ? -41.797 -2.620  -30.398 1.00 16.05  ? 634  LEU A N   1 
ATOM   5032 C CA  . LEU A 1 634 ? -40.475 -2.098  -30.688 1.00 15.93  ? 634  LEU A CA  1 
ATOM   5033 C C   . LEU A 1 634 ? -40.384 -0.958  -31.729 1.00 15.66  ? 634  LEU A C   1 
ATOM   5034 O O   . LEU A 1 634 ? -39.489 -0.122  -31.607 1.00 17.23  ? 634  LEU A O   1 
ATOM   5035 C CB  . LEU A 1 634 ? -39.467 -3.223  -31.013 1.00 17.58  ? 634  LEU A CB  1 
ATOM   5036 C CG  . LEU A 1 634 ? -38.913 -4.079  -29.867 1.00 19.61  ? 634  LEU A CG  1 
ATOM   5037 C CD1 . LEU A 1 634 ? -37.946 -5.128  -30.434 1.00 20.46  ? 634  LEU A CD1 1 
ATOM   5038 C CD2 . LEU A 1 634 ? -38.224 -3.211  -28.777 1.00 19.66  ? 634  LEU A CD2 1 
ATOM   5039 N N   . PRO A 1 635 ? -41.211 -0.965  -32.802 1.00 14.01  ? 635  PRO A N   1 
ATOM   5040 C CA  . PRO A 1 635 ? -41.149 0.177   -33.697 1.00 14.52  ? 635  PRO A CA  1 
ATOM   5041 C C   . PRO A 1 635 ? -41.501 1.476   -32.969 1.00 13.96  ? 635  PRO A C   1 
ATOM   5042 O O   . PRO A 1 635 ? -40.936 2.471   -33.249 1.00 15.52  ? 635  PRO A O   1 
ATOM   5043 C CB  . PRO A 1 635 ? -42.217 -0.154  -34.768 1.00 15.46  ? 635  PRO A CB  1 
ATOM   5044 C CG  . PRO A 1 635 ? -42.204 -1.648  -34.807 1.00 13.44  ? 635  PRO A CG  1 
ATOM   5045 C CD  . PRO A 1 635 ? -42.138 -1.989  -33.331 1.00 14.52  ? 635  PRO A CD  1 
ATOM   5046 N N   . TYR A 1 636 ? -42.461 1.445   -32.049 1.00 12.81  ? 636  TYR A N   1 
ATOM   5047 C CA  . TYR A 1 636 ? -42.772 2.603   -31.216 1.00 13.03  ? 636  TYR A CA  1 
ATOM   5048 C C   . TYR A 1 636 ? -41.571 2.978   -30.302 1.00 13.27  ? 636  TYR A C   1 
ATOM   5049 O O   . TYR A 1 636 ? -41.074 4.129   -30.312 1.00 14.40  ? 636  TYR A O   1 
ATOM   5050 C CB  . TYR A 1 636 ? -44.039 2.255   -30.402 1.00 11.70  ? 636  TYR A CB  1 
ATOM   5051 C CG  . TYR A 1 636 ? -44.472 3.338   -29.421 1.00 14.14  ? 636  TYR A CG  1 
ATOM   5052 C CD1 . TYR A 1 636 ? -44.820 4.617   -29.856 1.00 13.71  ? 636  TYR A CD1 1 
ATOM   5053 C CD2 . TYR A 1 636 ? -44.545 3.061   -28.074 1.00 13.71  ? 636  TYR A CD2 1 
ATOM   5054 C CE1 . TYR A 1 636 ? -45.206 5.616   -28.935 1.00 14.40  ? 636  TYR A CE1 1 
ATOM   5055 C CE2 . TYR A 1 636 ? -44.927 4.033   -27.148 1.00 13.76  ? 636  TYR A CE2 1 
ATOM   5056 C CZ  . TYR A 1 636 ? -45.261 5.296   -27.583 1.00 12.20  ? 636  TYR A CZ  1 
ATOM   5057 O OH  . TYR A 1 636 ? -45.613 6.239   -26.625 1.00 13.34  ? 636  TYR A OH  1 
ATOM   5058 N N   . LEU A 1 637 ? -41.103 2.036   -29.508 1.00 13.51  ? 637  LEU A N   1 
ATOM   5059 C CA  . LEU A 1 637 ? -39.880 2.277   -28.683 1.00 13.63  ? 637  LEU A CA  1 
ATOM   5060 C C   . LEU A 1 637 ? -38.712 2.840   -29.478 1.00 13.69  ? 637  LEU A C   1 
ATOM   5061 O O   . LEU A 1 637 ? -38.092 3.792   -29.042 1.00 13.78  ? 637  LEU A O   1 
ATOM   5062 C CB  . LEU A 1 637 ? -39.474 1.012   -27.936 1.00 12.73  ? 637  LEU A CB  1 
ATOM   5063 C CG  . LEU A 1 637 ? -38.347 1.197   -26.895 1.00 13.86  ? 637  LEU A CG  1 
ATOM   5064 C CD1 . LEU A 1 637 ? -38.750 2.204   -25.781 1.00 14.89  ? 637  LEU A CD1 1 
ATOM   5065 C CD2 . LEU A 1 637 ? -37.997 -0.154  -26.352 1.00 13.52  ? 637  LEU A CD2 1 
ATOM   5066 N N   . TYR A 1 638 ? -38.420 2.259   -30.642 1.00 14.31  ? 638  TYR A N   1 
ATOM   5067 C CA  . TYR A 1 638 ? -37.334 2.731   -31.524 1.00 13.62  ? 638  TYR A CA  1 
ATOM   5068 C C   . TYR A 1 638 ? -37.526 4.166   -31.990 1.00 13.33  ? 638  TYR A C   1 
ATOM   5069 O O   . TYR A 1 638 ? -36.601 4.962   -32.006 1.00 12.95  ? 638  TYR A O   1 
ATOM   5070 C CB  . TYR A 1 638 ? -37.199 1.789   -32.743 1.00 14.18  ? 638  TYR A CB  1 
ATOM   5071 C CG  . TYR A 1 638 ? -35.917 1.959   -33.531 1.00 14.10  ? 638  TYR A CG  1 
ATOM   5072 C CD1 . TYR A 1 638 ? -34.669 1.933   -32.890 1.00 14.68  ? 638  TYR A CD1 1 
ATOM   5073 C CD2 . TYR A 1 638 ? -35.941 2.160   -34.895 1.00 10.51  ? 638  TYR A CD2 1 
ATOM   5074 C CE1 . TYR A 1 638 ? -33.485 2.071   -33.618 1.00 15.35  ? 638  TYR A CE1 1 
ATOM   5075 C CE2 . TYR A 1 638 ? -34.766 2.303   -35.638 1.00 13.59  ? 638  TYR A CE2 1 
ATOM   5076 C CZ  . TYR A 1 638 ? -33.543 2.258   -35.003 1.00 15.09  ? 638  TYR A CZ  1 
ATOM   5077 O OH  . TYR A 1 638 ? -32.348 2.378   -35.754 1.00 16.09  ? 638  TYR A OH  1 
ATOM   5078 N N   . THR A 1 639 ? -38.751 4.531   -32.344 1.00 11.79  ? 639  THR A N   1 
ATOM   5079 C CA  . THR A 1 639 ? -39.034 5.871   -32.758 1.00 11.36  ? 639  THR A CA  1 
ATOM   5080 C C   . THR A 1 639 ? -38.856 6.818   -31.546 1.00 11.20  ? 639  THR A C   1 
ATOM   5081 O O   . THR A 1 639 ? -38.435 7.951   -31.725 1.00 12.29  ? 639  THR A O   1 
ATOM   5082 C CB  . THR A 1 639 ? -40.520 5.966   -33.309 1.00 10.70  ? 639  THR A CB  1 
ATOM   5083 O OG1 . THR A 1 639 ? -40.633 5.098   -34.445 1.00 13.01  ? 639  THR A OG1 1 
ATOM   5084 C CG2 . THR A 1 639 ? -40.864 7.384   -33.733 1.00 13.50  ? 639  THR A CG2 1 
ATOM   5085 N N   . LEU A 1 640 ? -39.156 6.347   -30.336 1.00 10.80  ? 640  LEU A N   1 
ATOM   5086 C CA  . LEU A 1 640 ? -38.966 7.170   -29.131 1.00 11.08  ? 640  LEU A CA  1 
ATOM   5087 C C   . LEU A 1 640 ? -37.452 7.403   -28.954 1.00 11.49  ? 640  LEU A C   1 
ATOM   5088 O O   . LEU A 1 640 ? -37.031 8.502   -28.602 1.00 11.51  ? 640  LEU A O   1 
ATOM   5089 C CB  . LEU A 1 640 ? -39.513 6.503   -27.885 1.00 9.95   ? 640  LEU A CB  1 
ATOM   5090 C CG  . LEU A 1 640 ? -41.059 6.390   -27.830 1.00 10.32  ? 640  LEU A CG  1 
ATOM   5091 C CD1 . LEU A 1 640 ? -41.365 5.731   -26.512 1.00 10.72  ? 640  LEU A CD1 1 
ATOM   5092 C CD2 . LEU A 1 640 ? -41.618 7.771   -27.967 1.00 11.97  ? 640  LEU A CD2 1 
ATOM   5093 N N   . PHE A 1 641 ? -36.677 6.366   -29.169 1.00 12.22  ? 641  PHE A N   1 
ATOM   5094 C CA  . PHE A 1 641 ? -35.194 6.552   -29.159 1.00 14.12  ? 641  PHE A CA  1 
ATOM   5095 C C   . PHE A 1 641 ? -34.713 7.469   -30.263 1.00 13.24  ? 641  PHE A C   1 
ATOM   5096 O O   . PHE A 1 641 ? -33.746 8.213   -30.067 1.00 13.78  ? 641  PHE A O   1 
ATOM   5097 C CB  . PHE A 1 641 ? -34.444 5.221   -29.220 1.00 14.07  ? 641  PHE A CB  1 
ATOM   5098 C CG  . PHE A 1 641 ? -34.309 4.524   -27.871 1.00 15.88  ? 641  PHE A CG  1 
ATOM   5099 C CD1 . PHE A 1 641 ? -33.279 4.903   -26.977 1.00 14.49  ? 641  PHE A CD1 1 
ATOM   5100 C CD2 . PHE A 1 641 ? -35.194 3.533   -27.503 1.00 15.38  ? 641  PHE A CD2 1 
ATOM   5101 C CE1 . PHE A 1 641 ? -33.139 4.266   -25.745 1.00 14.51  ? 641  PHE A CE1 1 
ATOM   5102 C CE2 . PHE A 1 641 ? -35.070 2.874   -26.274 1.00 17.52  ? 641  PHE A CE2 1 
ATOM   5103 C CZ  . PHE A 1 641 ? -34.038 3.249   -25.378 1.00 16.60  ? 641  PHE A CZ  1 
ATOM   5104 N N   . PHE A 1 642 ? -35.342 7.420   -31.442 1.00 14.75  ? 642  PHE A N   1 
ATOM   5105 C CA  . PHE A 1 642 ? -35.012 8.381   -32.494 1.00 14.37  ? 642  PHE A CA  1 
ATOM   5106 C C   . PHE A 1 642 ? -35.233 9.833   -32.042 1.00 13.98  ? 642  PHE A C   1 
ATOM   5107 O O   . PHE A 1 642 ? -34.368 10.710  -32.240 1.00 14.67  ? 642  PHE A O   1 
ATOM   5108 C CB  . PHE A 1 642 ? -35.742 8.094   -33.819 1.00 13.98  ? 642  PHE A CB  1 
ATOM   5109 C CG  . PHE A 1 642 ? -35.797 9.259   -34.740 1.00 13.71  ? 642  PHE A CG  1 
ATOM   5110 C CD1 . PHE A 1 642 ? -34.680 9.680   -35.451 1.00 12.28  ? 642  PHE A CD1 1 
ATOM   5111 C CD2 . PHE A 1 642 ? -37.016 9.935   -34.942 1.00 14.24  ? 642  PHE A CD2 1 
ATOM   5112 C CE1 . PHE A 1 642 ? -34.762 10.793  -36.339 1.00 15.11  ? 642  PHE A CE1 1 
ATOM   5113 C CE2 . PHE A 1 642 ? -37.110 11.017  -35.818 1.00 12.61  ? 642  PHE A CE2 1 
ATOM   5114 C CZ  . PHE A 1 642 ? -35.980 11.472  -36.510 1.00 16.66  ? 642  PHE A CZ  1 
ATOM   5115 N N   . ARG A 1 643 ? -36.342 10.071  -31.362 1.00 14.15  ? 643  ARG A N   1 
ATOM   5116 C CA  . ARG A 1 643 ? -36.626 11.400  -30.875 1.00 13.48  ? 643  ARG A CA  1 
ATOM   5117 C C   . ARG A 1 643 ? -35.700 11.796  -29.743 1.00 13.33  ? 643  ARG A C   1 
ATOM   5118 O O   . ARG A 1 643 ? -35.316 12.954  -29.682 1.00 13.64  ? 643  ARG A O   1 
ATOM   5119 C CB  . ARG A 1 643 ? -38.089 11.545  -30.452 1.00 14.89  ? 643  ARG A CB  1 
ATOM   5120 C CG  . ARG A 1 643 ? -39.057 11.516  -31.648 1.00 13.44  ? 643  ARG A CG  1 
ATOM   5121 C CD  . ARG A 1 643 ? -38.744 12.579  -32.692 1.00 16.57  ? 643  ARG A CD  1 
ATOM   5122 N NE  . ARG A 1 643 ? -39.891 12.775  -33.601 1.00 24.27  ? 643  ARG A NE  1 
ATOM   5123 C CZ  . ARG A 1 643 ? -39.869 13.541  -34.690 1.00 26.84  ? 643  ARG A CZ  1 
ATOM   5124 N NH1 . ARG A 1 643 ? -38.783 14.237  -35.000 1.00 26.36  ? 643  ARG A NH1 1 
ATOM   5125 N NH2 . ARG A 1 643 ? -40.948 13.646  -35.459 1.00 24.24  ? 643  ARG A NH2 1 
ATOM   5126 N N   . ALA A 1 644 ? -35.314 10.852  -28.884 1.00 12.56  ? 644  ALA A N   1 
ATOM   5127 C CA  . ALA A 1 644 ? -34.302 11.188  -27.834 1.00 13.08  ? 644  ALA A CA  1 
ATOM   5128 C C   . ALA A 1 644 ? -32.990 11.601  -28.498 1.00 14.13  ? 644  ALA A C   1 
ATOM   5129 O O   . ALA A 1 644 ? -32.336 12.587  -28.100 1.00 15.58  ? 644  ALA A O   1 
ATOM   5130 C CB  . ALA A 1 644 ? -34.107 9.962   -26.876 1.00 11.44  ? 644  ALA A CB  1 
ATOM   5131 N N   . HIS A 1 645 ? -32.558 10.811  -29.476 1.00 14.37  ? 645  HIS A N   1 
ATOM   5132 C CA  . HIS A 1 645 ? -31.311 11.096  -30.190 1.00 14.18  ? 645  HIS A CA  1 
ATOM   5133 C C   . HIS A 1 645 ? -31.357 12.409  -30.983 1.00 14.40  ? 645  HIS A C   1 
ATOM   5134 O O   . HIS A 1 645 ? -30.370 13.123  -31.026 1.00 15.06  ? 645  HIS A O   1 
ATOM   5135 C CB  . HIS A 1 645 ? -30.965 9.927   -31.134 1.00 14.64  ? 645  HIS A CB  1 
ATOM   5136 C CG  . HIS A 1 645 ? -29.772 10.189  -32.013 1.00 15.97  ? 645  HIS A CG  1 
ATOM   5137 N ND1 . HIS A 1 645 ? -28.478 10.203  -31.538 1.00 19.95  ? 645  HIS A ND1 1 
ATOM   5138 C CD2 . HIS A 1 645 ? -29.687 10.448  -33.343 1.00 20.83  ? 645  HIS A CD2 1 
ATOM   5139 C CE1 . HIS A 1 645 ? -27.640 10.466  -32.532 1.00 20.22  ? 645  HIS A CE1 1 
ATOM   5140 N NE2 . HIS A 1 645 ? -28.348 10.621  -33.640 1.00 24.20  ? 645  HIS A NE2 1 
ATOM   5141 N N   . SER A 1 646 ? -32.479 12.708  -31.632 1.00 15.18  ? 646  SER A N   1 
ATOM   5142 C CA  . SER A 1 646 ? -32.516 13.790  -32.596 1.00 16.96  ? 646  SER A CA  1 
ATOM   5143 C C   . SER A 1 646 ? -33.047 15.091  -32.017 1.00 18.07  ? 646  SER A C   1 
ATOM   5144 O O   . SER A 1 646 ? -32.688 16.192  -32.468 1.00 18.47  ? 646  SER A O   1 
ATOM   5145 C CB  . SER A 1 646 ? -33.302 13.363  -33.840 1.00 17.49  ? 646  SER A CB  1 
ATOM   5146 O OG  . SER A 1 646 ? -34.669 13.120  -33.522 1.00 17.77  ? 646  SER A OG  1 
ATOM   5147 N N   . ARG A 1 647 ? -33.894 14.975  -31.004 1.00 16.96  ? 647  ARG A N   1 
ATOM   5148 C CA  . ARG A 1 647 ? -34.580 16.116  -30.463 1.00 17.44  ? 647  ARG A CA  1 
ATOM   5149 C C   . ARG A 1 647 ? -34.279 16.308  -28.968 1.00 16.44  ? 647  ARG A C   1 
ATOM   5150 O O   . ARG A 1 647 ? -34.295 17.430  -28.437 1.00 17.30  ? 647  ARG A O   1 
ATOM   5151 C CB  . ARG A 1 647 ? -36.095 15.931  -30.700 1.00 17.23  ? 647  ARG A CB  1 
ATOM   5152 C CG  . ARG A 1 647 ? -36.828 17.226  -30.535 1.00 21.74  ? 647  ARG A CG  1 
ATOM   5153 C CD  . ARG A 1 647 ? -38.216 17.153  -31.150 1.00 25.23  ? 647  ARG A CD  1 
ATOM   5154 N NE  . ARG A 1 647 ? -39.027 16.115  -30.554 1.00 22.41  ? 647  ARG A NE  1 
ATOM   5155 C CZ  . ARG A 1 647 ? -40.144 15.655  -31.114 1.00 24.27  ? 647  ARG A CZ  1 
ATOM   5156 N NH1 . ARG A 1 647 ? -40.565 16.144  -32.283 1.00 24.31  ? 647  ARG A NH1 1 
ATOM   5157 N NH2 . ARG A 1 647 ? -40.828 14.706  -30.520 1.00 23.77  ? 647  ARG A NH2 1 
ATOM   5158 N N   . GLY A 1 648 ? -34.009 15.206  -28.290 1.00 16.07  ? 648  GLY A N   1 
ATOM   5159 C CA  . GLY A 1 648 ? -33.706 15.207  -26.861 1.00 17.34  ? 648  GLY A CA  1 
ATOM   5160 C C   . GLY A 1 648 ? -34.854 14.816  -25.942 1.00 17.66  ? 648  GLY A C   1 
ATOM   5161 O O   . GLY A 1 648 ? -34.794 15.092  -24.757 1.00 18.31  ? 648  GLY A O   1 
ATOM   5162 N N   . ASP A 1 649 ? -35.901 14.211  -26.485 1.00 18.01  ? 649  ASP A N   1 
ATOM   5163 C CA  . ASP A 1 649 ? -37.058 13.723  -25.707 1.00 18.73  ? 649  ASP A CA  1 
ATOM   5164 C C   . ASP A 1 649 ? -36.659 12.595  -24.732 1.00 18.90  ? 649  ASP A C   1 
ATOM   5165 O O   . ASP A 1 649 ? -35.658 11.880  -24.979 1.00 19.31  ? 649  ASP A O   1 
ATOM   5166 C CB  . ASP A 1 649 ? -38.092 13.096  -26.673 1.00 19.68  ? 649  ASP A CB  1 
ATOM   5167 C CG  . ASP A 1 649 ? -38.719 14.097  -27.651 1.00 21.68  ? 649  ASP A CG  1 
ATOM   5168 O OD1 . ASP A 1 649 ? -38.109 15.112  -28.013 1.00 21.22  ? 649  ASP A OD1 1 
ATOM   5169 O OD2 . ASP A 1 649 ? -39.860 13.842  -28.109 1.00 25.64  ? 649  ASP A OD2 1 
ATOM   5170 N N   . THR A 1 650 ? -37.419 12.395  -23.645 1.00 16.56  ? 650  THR A N   1 
ATOM   5171 C CA  . THR A 1 650 ? -37.194 11.204  -22.795 1.00 15.26  ? 650  THR A CA  1 
ATOM   5172 C C   . THR A 1 650 ? -37.865 9.997   -23.498 1.00 15.42  ? 650  THR A C   1 
ATOM   5173 O O   . THR A 1 650 ? -38.751 10.179  -24.368 1.00 16.11  ? 650  THR A O   1 
ATOM   5174 C CB  . THR A 1 650 ? -37.798 11.380  -21.381 1.00 15.69  ? 650  THR A CB  1 
ATOM   5175 O OG1 . THR A 1 650 ? -39.209 11.717  -21.526 1.00 15.38  ? 650  THR A OG1 1 
ATOM   5176 C CG2 . THR A 1 650 ? -37.127 12.516  -20.650 1.00 16.56  ? 650  THR A CG2 1 
ATOM   5177 N N   . VAL A 1 651 ? -37.503 8.801   -23.068 1.00 13.82  ? 651  VAL A N   1 
ATOM   5178 C CA  . VAL A 1 651 ? -38.058 7.548   -23.594 1.00 12.84  ? 651  VAL A CA  1 
ATOM   5179 C C   . VAL A 1 651 ? -38.994 6.958   -22.536 1.00 13.01  ? 651  VAL A C   1 
ATOM   5180 O O   . VAL A 1 651 ? -40.231 6.972   -22.728 1.00 14.32  ? 651  VAL A O   1 
ATOM   5181 C CB  . VAL A 1 651 ? -36.888 6.582   -24.040 1.00 11.99  ? 651  VAL A CB  1 
ATOM   5182 C CG1 . VAL A 1 651 ? -37.427 5.200   -24.404 1.00 10.45  ? 651  VAL A CG1 1 
ATOM   5183 C CG2 . VAL A 1 651 ? -36.167 7.164   -25.230 1.00 11.54  ? 651  VAL A CG2 1 
ATOM   5184 N N   . ALA A 1 652 ? -38.442 6.460   -21.419 1.00 14.17  ? 652  ALA A N   1 
ATOM   5185 C CA  . ALA A 1 652 ? -39.183 6.250   -20.157 1.00 14.18  ? 652  ALA A CA  1 
ATOM   5186 C C   . ALA A 1 652 ? -39.416 7.636   -19.523 1.00 14.76  ? 652  ALA A C   1 
ATOM   5187 O O   . ALA A 1 652 ? -38.485 8.408   -19.234 1.00 14.83  ? 652  ALA A O   1 
ATOM   5188 C CB  . ALA A 1 652 ? -38.390 5.331   -19.174 1.00 13.22  ? 652  ALA A CB  1 
ATOM   5189 N N   . ARG A 1 653 ? -40.671 7.973   -19.326 1.00 14.86  ? 653  ARG A N   1 
ATOM   5190 C CA  . ARG A 1 653 ? -41.030 9.343   -19.097 1.00 15.00  ? 653  ARG A CA  1 
ATOM   5191 C C   . ARG A 1 653 ? -41.916 9.393   -17.874 1.00 14.15  ? 653  ARG A C   1 
ATOM   5192 O O   . ARG A 1 653 ? -42.787 8.524   -17.720 1.00 15.15  ? 653  ARG A O   1 
ATOM   5193 C CB  . ARG A 1 653 ? -41.804 9.839   -20.332 1.00 15.47  ? 653  ARG A CB  1 
ATOM   5194 C CG  . ARG A 1 653 ? -42.033 11.306  -20.314 1.00 15.75  ? 653  ARG A CG  1 
ATOM   5195 C CD  . ARG A 1 653 ? -42.703 11.742  -21.602 1.00 18.85  ? 653  ARG A CD  1 
ATOM   5196 N NE  . ARG A 1 653 ? -41.747 11.558  -22.704 1.00 16.38  ? 653  ARG A NE  1 
ATOM   5197 C CZ  . ARG A 1 653 ? -42.030 11.782  -23.979 1.00 19.26  ? 653  ARG A CZ  1 
ATOM   5198 N NH1 . ARG A 1 653 ? -43.230 12.231  -24.352 1.00 12.61  ? 653  ARG A NH1 1 
ATOM   5199 N NH2 . ARG A 1 653 ? -41.106 11.546  -24.893 1.00 17.17  ? 653  ARG A NH2 1 
ATOM   5200 N N   . PRO A 1 654 ? -41.723 10.407  -16.985 1.00 14.79  ? 654  PRO A N   1 
ATOM   5201 C CA  . PRO A 1 654 ? -42.666 10.529  -15.847 1.00 13.68  ? 654  PRO A CA  1 
ATOM   5202 C C   . PRO A 1 654 ? -44.048 10.885  -16.313 1.00 13.70  ? 654  PRO A C   1 
ATOM   5203 O O   . PRO A 1 654 ? -44.201 11.548  -17.331 1.00 14.52  ? 654  PRO A O   1 
ATOM   5204 C CB  . PRO A 1 654 ? -42.102 11.695  -15.040 1.00 14.28  ? 654  PRO A CB  1 
ATOM   5205 C CG  . PRO A 1 654 ? -40.560 11.757  -15.479 1.00 14.05  ? 654  PRO A CG  1 
ATOM   5206 C CD  . PRO A 1 654 ? -40.633 11.406  -16.931 1.00 12.81  ? 654  PRO A CD  1 
ATOM   5207 N N   . LEU A 1 655 ? -45.069 10.493  -15.561 1.00 13.53  ? 655  LEU A N   1 
ATOM   5208 C CA  . LEU A 1 655 ? -46.404 10.949  -15.884 1.00 14.79  ? 655  LEU A CA  1 
ATOM   5209 C C   . LEU A 1 655 ? -46.532 12.456  -15.972 1.00 14.00  ? 655  LEU A C   1 
ATOM   5210 O O   . LEU A 1 655 ? -47.250 12.964  -16.807 1.00 15.26  ? 655  LEU A O   1 
ATOM   5211 C CB  . LEU A 1 655 ? -47.421 10.421  -14.847 1.00 15.44  ? 655  LEU A CB  1 
ATOM   5212 C CG  . LEU A 1 655 ? -48.063 9.055   -15.167 1.00 16.15  ? 655  LEU A CG  1 
ATOM   5213 C CD1 . LEU A 1 655 ? -47.064 7.924   -15.266 1.00 19.11  ? 655  LEU A CD1 1 
ATOM   5214 C CD2 . LEU A 1 655 ? -49.161 8.724   -14.091 1.00 15.54  ? 655  LEU A CD2 1 
ATOM   5215 N N   . LEU A 1 656 ? -45.887 13.164  -15.051 1.00 13.53  ? 656  LEU A N   1 
ATOM   5216 C CA  . LEU A 1 656 ? -45.940 14.602  -14.978 1.00 13.50  ? 656  LEU A CA  1 
ATOM   5217 C C   . LEU A 1 656 ? -45.347 15.292  -16.214 1.00 13.54  ? 656  LEU A C   1 
ATOM   5218 O O   . LEU A 1 656 ? -45.628 16.449  -16.436 1.00 13.22  ? 656  LEU A O   1 
ATOM   5219 C CB  . LEU A 1 656 ? -45.222 15.065  -13.695 1.00 13.91  ? 656  LEU A CB  1 
ATOM   5220 C CG  . LEU A 1 656 ? -43.700 14.995  -13.703 1.00 15.65  ? 656  LEU A CG  1 
ATOM   5221 C CD1 . LEU A 1 656 ? -43.112 16.407  -13.981 1.00 17.58  ? 656  LEU A CD1 1 
ATOM   5222 C CD2 . LEU A 1 656 ? -43.180 14.473  -12.367 1.00 18.01  ? 656  LEU A CD2 1 
ATOM   5223 N N   . HIS A 1 657 ? -44.477 14.632  -17.007 1.00 14.95  ? 657  HIS A N   1 
ATOM   5224 C CA  . HIS A 1 657 ? -44.014 15.271  -18.260 1.00 13.59  ? 657  HIS A CA  1 
ATOM   5225 C C   . HIS A 1 657 ? -45.131 15.435  -19.297 1.00 15.32  ? 657  HIS A C   1 
ATOM   5226 O O   . HIS A 1 657 ? -45.097 16.331  -20.136 1.00 15.57  ? 657  HIS A O   1 
ATOM   5227 C CB  . HIS A 1 657 ? -42.857 14.512  -18.869 1.00 14.66  ? 657  HIS A CB  1 
ATOM   5228 C CG  . HIS A 1 657 ? -41.567 14.742  -18.124 1.00 9.95   ? 657  HIS A CG  1 
ATOM   5229 N ND1 . HIS A 1 657 ? -40.331 14.758  -18.747 1.00 13.46  ? 657  HIS A ND1 1 
ATOM   5230 C CD2 . HIS A 1 657 ? -41.338 15.033  -16.824 1.00 11.32  ? 657  HIS A CD2 1 
ATOM   5231 C CE1 . HIS A 1 657 ? -39.386 15.012  -17.852 1.00 11.77  ? 657  HIS A CE1 1 
ATOM   5232 N NE2 . HIS A 1 657 ? -39.958 15.189  -16.679 1.00 13.02  ? 657  HIS A NE2 1 
ATOM   5233 N N   . GLU A 1 658 ? -46.133 14.580  -19.193 1.00 14.46  ? 658  GLU A N   1 
ATOM   5234 C CA  . GLU A 1 658 ? -47.293 14.684  -20.078 1.00 15.18  ? 658  GLU A CA  1 
ATOM   5235 C C   . GLU A 1 658 ? -48.502 15.285  -19.389 1.00 16.60  ? 658  GLU A C   1 
ATOM   5236 O O   . GLU A 1 658 ? -49.395 15.817  -20.048 1.00 17.81  ? 658  GLU A O   1 
ATOM   5237 C CB  . GLU A 1 658 ? -47.669 13.312  -20.582 1.00 14.70  ? 658  GLU A CB  1 
ATOM   5238 C CG  . GLU A 1 658 ? -46.641 12.679  -21.547 1.00 16.31  ? 658  GLU A CG  1 
ATOM   5239 C CD  . GLU A 1 658 ? -46.445 13.481  -22.813 1.00 19.78  ? 658  GLU A CD  1 
ATOM   5240 O OE1 . GLU A 1 658 ? -47.456 13.884  -23.447 1.00 21.01  ? 658  GLU A OE1 1 
ATOM   5241 O OE2 . GLU A 1 658 ? -45.262 13.685  -23.190 1.00 19.43  ? 658  GLU A OE2 1 
ATOM   5242 N N   . PHE A 1 659 ? -48.551 15.167  -18.078 1.00 15.95  ? 659  PHE A N   1 
ATOM   5243 C CA  . PHE A 1 659 ? -49.768 15.514  -17.348 1.00 16.23  ? 659  PHE A CA  1 
ATOM   5244 C C   . PHE A 1 659 ? -49.477 16.544  -16.244 1.00 16.41  ? 659  PHE A C   1 
ATOM   5245 O O   . PHE A 1 659 ? -50.073 16.501  -15.168 1.00 15.63  ? 659  PHE A O   1 
ATOM   5246 C CB  . PHE A 1 659 ? -50.398 14.230  -16.814 1.00 15.32  ? 659  PHE A CB  1 
ATOM   5247 C CG  . PHE A 1 659 ? -50.788 13.263  -17.914 1.00 16.50  ? 659  PHE A CG  1 
ATOM   5248 C CD1 . PHE A 1 659 ? -51.848 13.563  -18.759 1.00 16.97  ? 659  PHE A CD1 1 
ATOM   5249 C CD2 . PHE A 1 659 ? -50.061 12.084  -18.129 1.00 14.95  ? 659  PHE A CD2 1 
ATOM   5250 C CE1 . PHE A 1 659 ? -52.237 12.681  -19.815 1.00 15.14  ? 659  PHE A CE1 1 
ATOM   5251 C CE2 . PHE A 1 659 ? -50.450 11.192  -19.161 1.00 15.07  ? 659  PHE A CE2 1 
ATOM   5252 C CZ  . PHE A 1 659 ? -51.555 11.524  -20.008 1.00 14.09  ? 659  PHE A CZ  1 
ATOM   5253 N N   . TYR A 1 660 ? -48.550 17.469  -16.538 1.00 16.78  ? 660  TYR A N   1 
ATOM   5254 C CA  . TYR A 1 660 ? -48.064 18.494  -15.557 1.00 17.88  ? 660  TYR A CA  1 
ATOM   5255 C C   . TYR A 1 660 ? -49.189 19.396  -15.080 1.00 17.62  ? 660  TYR A C   1 
ATOM   5256 O O   . TYR A 1 660 ? -49.069 19.957  -14.019 1.00 18.00  ? 660  TYR A O   1 
ATOM   5257 C CB  . TYR A 1 660 ? -46.940 19.367  -16.140 1.00 16.71  ? 660  TYR A CB  1 
ATOM   5258 C CG  . TYR A 1 660 ? -47.199 19.761  -17.568 1.00 16.80  ? 660  TYR A CG  1 
ATOM   5259 C CD1 . TYR A 1 660 ? -48.014 20.832  -17.890 1.00 14.51  ? 660  TYR A CD1 1 
ATOM   5260 C CD2 . TYR A 1 660 ? -46.627 19.022  -18.629 1.00 18.46  ? 660  TYR A CD2 1 
ATOM   5261 C CE1 . TYR A 1 660 ? -48.274 21.166  -19.234 1.00 17.35  ? 660  TYR A CE1 1 
ATOM   5262 C CE2 . TYR A 1 660 ? -46.879 19.335  -19.933 1.00 18.50  ? 660  TYR A CE2 1 
ATOM   5263 C CZ  . TYR A 1 660 ? -47.700 20.407  -20.234 1.00 20.86  ? 660  TYR A CZ  1 
ATOM   5264 O OH  . TYR A 1 660 ? -47.907 20.681  -21.563 1.00 23.02  ? 660  TYR A OH  1 
ATOM   5265 N N   . GLU A 1 661 ? -50.284 19.534  -15.856 1.00 18.54  ? 661  GLU A N   1 
ATOM   5266 C CA  A GLU A 1 661 ? -51.463 20.314  -15.465 0.50 18.98  ? 661  GLU A CA  1 
ATOM   5267 C CA  B GLU A 1 661 ? -51.414 20.367  -15.416 0.50 19.28  ? 661  GLU A CA  1 
ATOM   5268 C C   . GLU A 1 661 ? -52.136 19.741  -14.232 1.00 19.47  ? 661  GLU A C   1 
ATOM   5269 O O   . GLU A 1 661 ? -52.921 20.419  -13.545 1.00 19.75  ? 661  GLU A O   1 
ATOM   5270 C CB  A GLU A 1 661 ? -52.496 20.330  -16.611 0.50 18.98  ? 661  GLU A CB  1 
ATOM   5271 C CB  B GLU A 1 661 ? -52.407 20.679  -16.569 0.50 18.81  ? 661  GLU A CB  1 
ATOM   5272 C CG  A GLU A 1 661 ? -51.958 20.773  -17.987 0.50 20.22  ? 661  GLU A CG  1 
ATOM   5273 C CG  B GLU A 1 661 ? -51.900 21.736  -17.588 0.50 19.20  ? 661  GLU A CG  1 
ATOM   5274 C CD  A GLU A 1 661 ? -51.453 19.625  -18.895 0.50 24.18  ? 661  GLU A CD  1 
ATOM   5275 C CD  B GLU A 1 661 ? -52.753 21.882  -18.865 0.50 21.85  ? 661  GLU A CD  1 
ATOM   5276 O OE1 A GLU A 1 661 ? -51.164 18.477  -18.426 0.50 19.35  ? 661  GLU A OE1 1 
ATOM   5277 O OE1 B GLU A 1 661 ? -53.989 21.625  -18.830 0.50 25.88  ? 661  GLU A OE1 1 
ATOM   5278 O OE2 A GLU A 1 661 ? -51.317 19.912  -20.108 0.50 26.19  ? 661  GLU A OE2 1 
ATOM   5279 O OE2 B GLU A 1 661 ? -52.194 22.278  -19.918 0.50 24.45  ? 661  GLU A OE2 1 
ATOM   5280 N N   . ASP A 1 662 ? -51.856 18.470  -13.975 1.00 18.73  ? 662  ASP A N   1 
ATOM   5281 C CA  . ASP A 1 662 ? -52.524 17.707  -12.934 1.00 18.84  ? 662  ASP A CA  1 
ATOM   5282 C C   . ASP A 1 662 ? -51.556 17.439  -11.811 1.00 19.60  ? 662  ASP A C   1 
ATOM   5283 O O   . ASP A 1 662 ? -50.730 16.545  -11.918 1.00 17.28  ? 662  ASP A O   1 
ATOM   5284 C CB  . ASP A 1 662 ? -53.052 16.403  -13.573 1.00 17.99  ? 662  ASP A CB  1 
ATOM   5285 C CG  . ASP A 1 662 ? -53.820 15.496  -12.598 1.00 20.66  ? 662  ASP A CG  1 
ATOM   5286 O OD1 . ASP A 1 662 ? -53.969 15.823  -11.407 1.00 20.78  ? 662  ASP A OD1 1 
ATOM   5287 O OD2 . ASP A 1 662 ? -54.321 14.440  -13.063 1.00 22.09  ? 662  ASP A OD2 1 
ATOM   5288 N N   . ASN A 1 663 ? -51.688 18.189  -10.706 1.00 19.43  ? 663  ASN A N   1 
ATOM   5289 C CA  . ASN A 1 663 ? -50.773 18.025  -9.583  1.00 19.86  ? 663  ASN A CA  1 
ATOM   5290 C C   . ASN A 1 663 ? -50.745 16.624  -8.929  1.00 19.19  ? 663  ASN A C   1 
ATOM   5291 O O   . ASN A 1 663 ? -49.736 16.278  -8.280  1.00 18.53  ? 663  ASN A O   1 
ATOM   5292 C CB  . ASN A 1 663 ? -50.992 19.122  -8.519  1.00 19.95  ? 663  ASN A CB  1 
ATOM   5293 C CG  . ASN A 1 663 ? -52.248 18.900  -7.720  1.00 24.30  ? 663  ASN A CG  1 
ATOM   5294 O OD1 . ASN A 1 663 ? -53.264 18.408  -8.234  1.00 26.37  ? 663  ASN A OD1 1 
ATOM   5295 N ND2 . ASN A 1 663 ? -52.194 19.263  -6.453  1.00 29.62  ? 663  ASN A ND2 1 
ATOM   5296 N N   . SER A 1 664 ? -51.795 15.797  -9.132  1.00 19.87  ? 664  SER A N   1 
ATOM   5297 C CA  . SER A 1 664 ? -51.747 14.406  -8.663  1.00 20.23  ? 664  SER A CA  1 
ATOM   5298 C C   . SER A 1 664 ? -50.642 13.578  -9.346  1.00 19.63  ? 664  SER A C   1 
ATOM   5299 O O   . SER A 1 664 ? -50.301 12.501  -8.855  1.00 20.60  ? 664  SER A O   1 
ATOM   5300 C CB  . SER A 1 664 ? -53.079 13.656  -8.853  1.00 21.80  ? 664  SER A CB  1 
ATOM   5301 O OG  . SER A 1 664 ? -54.148 14.355  -8.248  1.00 21.67  ? 664  SER A OG  1 
ATOM   5302 N N   . THR A 1 665 ? -50.086 14.070  -10.448 1.00 18.44  ? 665  THR A N   1 
ATOM   5303 C CA  . THR A 1 665 ? -49.010 13.336  -11.125 1.00 16.93  ? 665  THR A CA  1 
ATOM   5304 C C   . THR A 1 665 ? -47.588 13.728  -10.668 1.00 17.54  ? 665  THR A C   1 
ATOM   5305 O O   . THR A 1 665 ? -46.640 13.057  -11.032 1.00 16.61  ? 665  THR A O   1 
ATOM   5306 C CB  . THR A 1 665 ? -49.060 13.499  -12.620 1.00 16.90  ? 665  THR A CB  1 
ATOM   5307 O OG1 . THR A 1 665 ? -48.758 14.859  -12.977 1.00 18.03  ? 665  THR A OG1 1 
ATOM   5308 C CG2 . THR A 1 665 ? -50.434 13.063  -13.201 1.00 15.86  ? 665  THR A CG2 1 
ATOM   5309 N N   . TRP A 1 666 ? -47.454 14.805  -9.896  1.00 16.66  ? 666  TRP A N   1 
ATOM   5310 C CA  . TRP A 1 666 ? -46.142 15.400  -9.618  1.00 18.35  ? 666  TRP A CA  1 
ATOM   5311 C C   . TRP A 1 666 ? -45.261 14.517  -8.745  1.00 18.28  ? 666  TRP A C   1 
ATOM   5312 O O   . TRP A 1 666 ? -44.041 14.656  -8.737  1.00 19.22  ? 666  TRP A O   1 
ATOM   5313 C CB  . TRP A 1 666 ? -46.320 16.784  -8.971  1.00 18.22  ? 666  TRP A CB  1 
ATOM   5314 C CG  . TRP A 1 666 ? -46.976 17.847  -9.852  1.00 19.50  ? 666  TRP A CG  1 
ATOM   5315 C CD1 . TRP A 1 666 ? -47.333 17.740  -11.165 1.00 18.52  ? 666  TRP A CD1 1 
ATOM   5316 C CD2 . TRP A 1 666 ? -47.311 19.182  -9.448  1.00 20.68  ? 666  TRP A CD2 1 
ATOM   5317 N NE1 . TRP A 1 666 ? -47.893 18.935  -11.613 1.00 18.99  ? 666  TRP A NE1 1 
ATOM   5318 C CE2 . TRP A 1 666 ? -47.882 19.838  -10.576 1.00 19.03  ? 666  TRP A CE2 1 
ATOM   5319 C CE3 . TRP A 1 666 ? -47.201 19.885  -8.233  1.00 22.43  ? 666  TRP A CE3 1 
ATOM   5320 C CZ2 . TRP A 1 666 ? -48.331 21.173  -10.527 1.00 21.36  ? 666  TRP A CZ2 1 
ATOM   5321 C CZ3 . TRP A 1 666 ? -47.654 21.237  -8.184  1.00 20.27  ? 666  TRP A CZ3 1 
ATOM   5322 C CH2 . TRP A 1 666 ? -48.199 21.858  -9.330  1.00 20.69  ? 666  TRP A CH2 1 
ATOM   5323 N N   . ASP A 1 667 ? -45.867 13.597  -8.006  1.00 19.19  ? 667  ASP A N   1 
ATOM   5324 C CA  . ASP A 1 667 ? -45.057 12.714  -7.191  1.00 22.16  ? 667  ASP A CA  1 
ATOM   5325 C C   . ASP A 1 667 ? -45.174 11.239  -7.598  1.00 21.35  ? 667  ASP A C   1 
ATOM   5326 O O   . ASP A 1 667 ? -44.642 10.364  -6.919  1.00 22.38  ? 667  ASP A O   1 
ATOM   5327 C CB  . ASP A 1 667 ? -45.392 12.894  -5.718  1.00 24.18  ? 667  ASP A CB  1 
ATOM   5328 C CG  . ASP A 1 667 ? -46.849 12.668  -5.441  1.00 31.38  ? 667  ASP A CG  1 
ATOM   5329 O OD1 . ASP A 1 667 ? -47.602 12.274  -6.391  1.00 38.14  ? 667  ASP A OD1 1 
ATOM   5330 O OD2 . ASP A 1 667 ? -47.246 12.918  -4.276  1.00 40.94  ? 667  ASP A OD2 1 
ATOM   5331 N N   . VAL A 1 668 ? -45.858 10.970  -8.702  1.00 20.35  ? 668  VAL A N   1 
ATOM   5332 C CA  . VAL A 1 668 ? -46.053 9.589   -9.160  1.00 19.64  ? 668  VAL A CA  1 
ATOM   5333 C C   . VAL A 1 668 ? -44.726 8.977   -9.607  1.00 19.76  ? 668  VAL A C   1 
ATOM   5334 O O   . VAL A 1 668 ? -44.092 9.501   -10.508 1.00 19.66  ? 668  VAL A O   1 
ATOM   5335 C CB  . VAL A 1 668 ? -47.111 9.481   -10.264 1.00 19.45  ? 668  VAL A CB  1 
ATOM   5336 C CG1 . VAL A 1 668 ? -47.032 8.142   -10.916 1.00 19.34  ? 668  VAL A CG1 1 
ATOM   5337 C CG2 . VAL A 1 668 ? -48.504 9.708   -9.671  1.00 20.26  ? 668  VAL A CG2 1 
ATOM   5338 N N   . HIS A 1 669 ? -44.300 7.901   -8.934  1.00 19.92  ? 669  HIS A N   1 
ATOM   5339 C CA  . HIS A 1 669 ? -43.049 7.200   -9.273  1.00 21.61  ? 669  HIS A CA  1 
ATOM   5340 C C   . HIS A 1 669 ? -43.248 5.668   -9.276  1.00 21.33  ? 669  HIS A C   1 
ATOM   5341 O O   . HIS A 1 669 ? -42.278 4.934   -9.389  1.00 20.82  ? 669  HIS A O   1 
ATOM   5342 C CB  . HIS A 1 669 ? -41.918 7.577   -8.281  1.00 21.20  ? 669  HIS A CB  1 
ATOM   5343 C CG  . HIS A 1 669 ? -42.228 7.232   -6.864  1.00 25.37  ? 669  HIS A CG  1 
ATOM   5344 N ND1 . HIS A 1 669 ? -41.826 6.051   -6.284  1.00 30.09  ? 669  HIS A ND1 1 
ATOM   5345 C CD2 . HIS A 1 669 ? -42.977 7.867   -5.934  1.00 29.95  ? 669  HIS A CD2 1 
ATOM   5346 C CE1 . HIS A 1 669 ? -42.270 5.995   -5.044  1.00 30.56  ? 669  HIS A CE1 1 
ATOM   5347 N NE2 . HIS A 1 669 ? -42.967 7.087   -4.802  1.00 30.69  ? 669  HIS A NE2 1 
ATOM   5348 N N   . GLN A 1 670 ? -44.494 5.209   -9.129  1.00 20.26  ? 670  GLN A N   1 
ATOM   5349 C CA  . GLN A 1 670 ? -44.831 3.787   -9.163  1.00 21.73  ? 670  GLN A CA  1 
ATOM   5350 C C   . GLN A 1 670 ? -45.433 3.358   -10.514 1.00 18.81  ? 670  GLN A C   1 
ATOM   5351 O O   . GLN A 1 670 ? -45.757 2.192   -10.715 1.00 18.26  ? 670  GLN A O   1 
ATOM   5352 C CB  . GLN A 1 670 ? -45.808 3.432   -8.031  1.00 21.77  ? 670  GLN A CB  1 
ATOM   5353 C CG  . GLN A 1 670 ? -45.118 3.326   -6.645  1.00 26.10  ? 670  GLN A CG  1 
ATOM   5354 C CD  . GLN A 1 670 ? -45.974 2.511   -5.634  1.00 28.56  ? 670  GLN A CD  1 
ATOM   5355 O OE1 . GLN A 1 670 ? -45.441 1.771   -4.778  1.00 36.42  ? 670  GLN A OE1 1 
ATOM   5356 N NE2 . GLN A 1 670 ? -47.305 2.611   -5.771  1.00 34.08  ? 670  GLN A NE2 1 
ATOM   5357 N N   . GLN A 1 671 ? -45.545 4.326   -11.423 1.00 16.51  ? 671  GLN A N   1 
ATOM   5358 C CA  . GLN A 1 671 ? -45.980 4.119   -12.774 1.00 16.18  ? 671  GLN A CA  1 
ATOM   5359 C C   . GLN A 1 671 ? -45.105 5.014   -13.625 1.00 15.48  ? 671  GLN A C   1 
ATOM   5360 O O   . GLN A 1 671 ? -44.494 5.955   -13.110 1.00 16.79  ? 671  GLN A O   1 
ATOM   5361 C CB  . GLN A 1 671 ? -47.420 4.621   -12.942 1.00 15.49  ? 671  GLN A CB  1 
ATOM   5362 C CG  . GLN A 1 671 ? -48.459 3.847   -12.193 1.00 19.51  ? 671  GLN A CG  1 
ATOM   5363 C CD  . GLN A 1 671 ? -49.786 4.588   -12.209 1.00 18.53  ? 671  GLN A CD  1 
ATOM   5364 O OE1 . GLN A 1 671 ? -50.037 5.453   -11.372 1.00 19.66  ? 671  GLN A OE1 1 
ATOM   5365 N NE2 . GLN A 1 671 ? -50.608 4.287   -13.187 1.00 22.98  ? 671  GLN A NE2 1 
ATOM   5366 N N   . PHE A 1 672 ? -45.001 4.680   -14.903 1.00 15.37  ? 672  PHE A N   1 
ATOM   5367 C CA  . PHE A 1 672 ? -44.372 5.539   -15.886 1.00 15.64  ? 672  PHE A CA  1 
ATOM   5368 C C   . PHE A 1 672 ? -44.944 5.318   -17.281 1.00 15.47  ? 672  PHE A C   1 
ATOM   5369 O O   . PHE A 1 672 ? -45.764 4.419   -17.482 1.00 15.78  ? 672  PHE A O   1 
ATOM   5370 C CB  . PHE A 1 672 ? -42.833 5.356   -15.861 1.00 15.92  ? 672  PHE A CB  1 
ATOM   5371 C CG  . PHE A 1 672 ? -42.360 3.994   -16.300 1.00 18.85  ? 672  PHE A CG  1 
ATOM   5372 C CD1 . PHE A 1 672 ? -41.694 3.837   -17.519 1.00 20.83  ? 672  PHE A CD1 1 
ATOM   5373 C CD2 . PHE A 1 672 ? -42.508 2.880   -15.474 1.00 19.57  ? 672  PHE A CD2 1 
ATOM   5374 C CE1 . PHE A 1 672 ? -41.254 2.588   -17.940 1.00 19.40  ? 672  PHE A CE1 1 
ATOM   5375 C CE2 . PHE A 1 672 ? -42.065 1.620   -15.883 1.00 21.81  ? 672  PHE A CE2 1 
ATOM   5376 C CZ  . PHE A 1 672 ? -41.425 1.474   -17.119 1.00 18.16  ? 672  PHE A CZ  1 
ATOM   5377 N N   . LEU A 1 673 ? -44.514 6.147   -18.232 1.00 14.70  ? 673  LEU A N   1 
ATOM   5378 C CA  . LEU A 1 673 ? -44.926 6.054   -19.611 1.00 15.50  ? 673  LEU A CA  1 
ATOM   5379 C C   . LEU A 1 673 ? -43.789 5.599   -20.500 1.00 16.66  ? 673  LEU A C   1 
ATOM   5380 O O   . LEU A 1 673 ? -42.620 5.909   -20.217 1.00 15.66  ? 673  LEU A O   1 
ATOM   5381 C CB  . LEU A 1 673 ? -45.300 7.439   -20.088 1.00 16.08  ? 673  LEU A CB  1 
ATOM   5382 C CG  . LEU A 1 673 ? -46.337 8.190   -19.249 1.00 18.05  ? 673  LEU A CG  1 
ATOM   5383 C CD1 . LEU A 1 673 ? -46.336 9.609   -19.786 1.00 18.02  ? 673  LEU A CD1 1 
ATOM   5384 C CD2 . LEU A 1 673 ? -47.698 7.543   -19.426 1.00 21.07  ? 673  LEU A CD2 1 
ATOM   5385 N N   . TRP A 1 674 ? -44.117 4.884   -21.564 1.00 16.06  ? 674  TRP A N   1 
ATOM   5386 C CA  . TRP A 1 674 ? -43.219 4.921   -22.718 1.00 16.02  ? 674  TRP A CA  1 
ATOM   5387 C C   . TRP A 1 674 ? -43.621 6.089   -23.578 1.00 16.68  ? 674  TRP A C   1 
ATOM   5388 O O   . TRP A 1 674 ? -44.750 6.068   -24.129 1.00 16.06  ? 674  TRP A O   1 
ATOM   5389 C CB  . TRP A 1 674 ? -43.403 3.664   -23.543 1.00 17.00  ? 674  TRP A CB  1 
ATOM   5390 C CG  . TRP A 1 674 ? -42.577 2.497   -23.138 1.00 17.65  ? 674  TRP A CG  1 
ATOM   5391 C CD1 . TRP A 1 674 ? -41.912 2.293   -21.952 1.00 20.37  ? 674  TRP A CD1 1 
ATOM   5392 C CD2 . TRP A 1 674 ? -42.338 1.347   -23.941 1.00 18.54  ? 674  TRP A CD2 1 
ATOM   5393 N NE1 . TRP A 1 674 ? -41.257 1.083   -21.986 1.00 20.76  ? 674  TRP A NE1 1 
ATOM   5394 C CE2 . TRP A 1 674 ? -41.504 0.479   -23.191 1.00 19.67  ? 674  TRP A CE2 1 
ATOM   5395 C CE3 . TRP A 1 674 ? -42.737 0.971   -25.242 1.00 16.71  ? 674  TRP A CE3 1 
ATOM   5396 C CZ2 . TRP A 1 674 ? -41.056 -0.744  -23.693 1.00 19.31  ? 674  TRP A CZ2 1 
ATOM   5397 C CZ3 . TRP A 1 674 ? -42.298 -0.248  -25.735 1.00 17.06  ? 674  TRP A CZ3 1 
ATOM   5398 C CH2 . TRP A 1 674 ? -41.477 -1.098  -24.952 1.00 18.64  ? 674  TRP A CH2 1 
ATOM   5399 N N   . GLY A 1 675 ? -42.734 7.078   -23.738 1.00 14.90  ? 675  GLY A N   1 
ATOM   5400 C CA  . GLY A 1 675 ? -43.061 8.263   -24.567 1.00 14.98  ? 675  GLY A CA  1 
ATOM   5401 C C   . GLY A 1 675 ? -44.389 8.878   -24.069 1.00 15.33  ? 675  GLY A C   1 
ATOM   5402 O O   . GLY A 1 675 ? -44.627 8.901   -22.868 1.00 14.06  ? 675  GLY A O   1 
ATOM   5403 N N   . PRO A 1 676 ? -45.213 9.422   -24.978 1.00 15.74  ? 676  PRO A N   1 
ATOM   5404 C CA  . PRO A 1 676 ? -46.457 10.082  -24.528 1.00 17.36  ? 676  PRO A CA  1 
ATOM   5405 C C   . PRO A 1 676 ? -47.653 9.172   -24.303 1.00 17.93  ? 676  PRO A C   1 
ATOM   5406 O O   . PRO A 1 676 ? -48.596 9.581   -23.599 1.00 19.12  ? 676  PRO A O   1 
ATOM   5407 C CB  . PRO A 1 676 ? -46.745 11.069  -25.659 1.00 17.00  ? 676  PRO A CB  1 
ATOM   5408 C CG  . PRO A 1 676 ? -46.177 10.309  -26.923 1.00 17.81  ? 676  PRO A CG  1 
ATOM   5409 C CD  . PRO A 1 676 ? -44.968 9.580   -26.428 1.00 15.44  ? 676  PRO A CD  1 
ATOM   5410 N N   . GLY A 1 677 ? -47.622 7.945   -24.828 1.00 18.24  ? 677  GLY A N   1 
ATOM   5411 C CA  . GLY A 1 677 ? -48.894 7.226   -25.093 1.00 18.94  ? 677  GLY A CA  1 
ATOM   5412 C C   . GLY A 1 677 ? -49.163 5.919   -24.374 1.00 18.53  ? 677  GLY A C   1 
ATOM   5413 O O   . GLY A 1 677 ? -50.301 5.444   -24.379 1.00 19.36  ? 677  GLY A O   1 
ATOM   5414 N N   . LEU A 1 678 ? -48.135 5.319   -23.775 1.00 17.76  ? 678  LEU A N   1 
ATOM   5415 C CA  . LEU A 1 678 ? -48.281 3.996   -23.101 1.00 17.43  ? 678  LEU A CA  1 
ATOM   5416 C C   . LEU A 1 678 ? -48.011 4.108   -21.614 1.00 17.58  ? 678  LEU A C   1 
ATOM   5417 O O   . LEU A 1 678 ? -46.887 4.424   -21.199 1.00 16.27  ? 678  LEU A O   1 
ATOM   5418 C CB  . LEU A 1 678 ? -47.327 2.938   -23.704 1.00 16.83  ? 678  LEU A CB  1 
ATOM   5419 C CG  . LEU A 1 678 ? -47.271 1.552   -23.017 1.00 16.94  ? 678  LEU A CG  1 
ATOM   5420 C CD1 . LEU A 1 678 ? -48.590 0.761   -23.262 1.00 18.57  ? 678  LEU A CD1 1 
ATOM   5421 C CD2 . LEU A 1 678 ? -46.115 0.716   -23.492 1.00 17.31  ? 678  LEU A CD2 1 
ATOM   5422 N N   . LEU A 1 679 ? -49.025 3.801   -20.810 1.00 16.45  ? 679  LEU A N   1 
ATOM   5423 C CA  . LEU A 1 679 ? -48.962 3.903   -19.362 1.00 16.07  ? 679  LEU A CA  1 
ATOM   5424 C C   . LEU A 1 679 ? -48.695 2.510   -18.798 1.00 15.50  ? 679  LEU A C   1 
ATOM   5425 O O   . LEU A 1 679 ? -49.437 1.565   -19.065 1.00 14.60  ? 679  LEU A O   1 
ATOM   5426 C CB  . LEU A 1 679 ? -50.332 4.408   -18.852 1.00 15.54  ? 679  LEU A CB  1 
ATOM   5427 C CG  . LEU A 1 679 ? -50.520 4.503   -17.348 1.00 14.45  ? 679  LEU A CG  1 
ATOM   5428 C CD1 . LEU A 1 679 ? -49.490 5.464   -16.690 1.00 16.01  ? 679  LEU A CD1 1 
ATOM   5429 C CD2 . LEU A 1 679 ? -51.977 4.903   -17.020 1.00 17.48  ? 679  LEU A CD2 1 
ATOM   5430 N N   . ILE A 1 680 ? -47.610 2.372   -18.049 1.00 14.34  ? 680  ILE A N   1 
ATOM   5431 C CA  . ILE A 1 680 ? -47.238 1.109   -17.433 1.00 14.16  ? 680  ILE A CA  1 
ATOM   5432 C C   . ILE A 1 680 ? -47.521 1.173   -15.932 1.00 14.58  ? 680  ILE A C   1 
ATOM   5433 O O   . ILE A 1 680 ? -46.994 2.044   -15.221 1.00 16.58  ? 680  ILE A O   1 
ATOM   5434 C CB  . ILE A 1 680 ? -45.686 0.796   -17.699 1.00 14.86  ? 680  ILE A CB  1 
ATOM   5435 C CG1 . ILE A 1 680 ? -45.439 0.655   -19.209 1.00 17.07  ? 680  ILE A CG1 1 
ATOM   5436 C CG2 . ILE A 1 680 ? -45.258 -0.509  -16.992 1.00 15.76  ? 680  ILE A CG2 1 
ATOM   5437 C CD1 . ILE A 1 680 ? -44.313 1.527   -19.707 1.00 23.23  ? 680  ILE A CD1 1 
ATOM   5438 N N   . THR A 1 681 ? -48.248 0.183   -15.420 1.00 14.10  ? 681  THR A N   1 
ATOM   5439 C CA  . THR A 1 681 ? -48.689 0.165   -14.018 1.00 14.49  ? 681  THR A CA  1 
ATOM   5440 C C   . THR A 1 681 ? -48.418 -1.203  -13.446 1.00 14.44  ? 681  THR A C   1 
ATOM   5441 O O   . THR A 1 681 ? -49.238 -2.133  -13.538 1.00 15.46  ? 681  THR A O   1 
ATOM   5442 C CB  . THR A 1 681 ? -50.241 0.483   -13.907 1.00 12.67  ? 681  THR A CB  1 
ATOM   5443 O OG1 . THR A 1 681 ? -50.449 1.761   -14.479 1.00 17.93  ? 681  THR A OG1 1 
ATOM   5444 C CG2 . THR A 1 681 ? -50.660 0.579   -12.445 1.00 15.33  ? 681  THR A CG2 1 
ATOM   5445 N N   . PRO A 1 682 ? -47.222 -1.377  -12.875 1.00 14.65  ? 682  PRO A N   1 
ATOM   5446 C CA  . PRO A 1 682 ? -46.832 -2.622  -12.235 1.00 14.87  ? 682  PRO A CA  1 
ATOM   5447 C C   . PRO A 1 682 ? -47.375 -2.855  -10.833 1.00 15.38  ? 682  PRO A C   1 
ATOM   5448 O O   . PRO A 1 682 ? -47.667 -1.901  -10.080 1.00 15.99  ? 682  PRO A O   1 
ATOM   5449 C CB  . PRO A 1 682 ? -45.304 -2.478  -12.127 1.00 14.36  ? 682  PRO A CB  1 
ATOM   5450 C CG  . PRO A 1 682 ? -45.122 -0.984  -11.934 1.00 13.65  ? 682  PRO A CG  1 
ATOM   5451 C CD  . PRO A 1 682 ? -46.143 -0.372  -12.870 1.00 14.58  ? 682  PRO A CD  1 
ATOM   5452 N N   . VAL A 1 683 ? -47.488 -4.134  -10.486 1.00 17.27  ? 683  VAL A N   1 
ATOM   5453 C CA  . VAL A 1 683 ? -47.647 -4.539  -9.100  1.00 18.61  ? 683  VAL A CA  1 
ATOM   5454 C C   . VAL A 1 683 ? -46.274 -4.518  -8.452  1.00 20.06  ? 683  VAL A C   1 
ATOM   5455 O O   . VAL A 1 683 ? -45.340 -5.129  -8.964  1.00 19.61  ? 683  VAL A O   1 
ATOM   5456 C CB  . VAL A 1 683 ? -48.293 -5.912  -9.005  1.00 18.75  ? 683  VAL A CB  1 
ATOM   5457 C CG1 . VAL A 1 683 ? -48.215 -6.454  -7.564  1.00 20.23  ? 683  VAL A CG1 1 
ATOM   5458 C CG2 . VAL A 1 683 ? -49.743 -5.800  -9.469  1.00 19.48  ? 683  VAL A CG2 1 
ATOM   5459 N N   . LEU A 1 684 ? -46.149 -3.774  -7.355  1.00 20.21  ? 684  LEU A N   1 
ATOM   5460 C CA  . LEU A 1 684 ? -44.833 -3.553  -6.737  1.00 22.44  ? 684  LEU A CA  1 
ATOM   5461 C C   . LEU A 1 684 ? -44.795 -4.015  -5.279  1.00 23.22  ? 684  LEU A C   1 
ATOM   5462 O O   . LEU A 1 684 ? -43.843 -3.719  -4.569  1.00 22.84  ? 684  LEU A O   1 
ATOM   5463 C CB  . LEU A 1 684 ? -44.465 -2.070  -6.809  1.00 21.40  ? 684  LEU A CB  1 
ATOM   5464 C CG  . LEU A 1 684 ? -44.422 -1.562  -8.234  1.00 20.96  ? 684  LEU A CG  1 
ATOM   5465 C CD1 . LEU A 1 684 ? -44.257 -0.053  -8.230  1.00 22.39  ? 684  LEU A CD1 1 
ATOM   5466 C CD2 . LEU A 1 684 ? -43.299 -2.254  -8.984  1.00 21.94  ? 684  LEU A CD2 1 
ATOM   5467 N N   . ASP A 1 685 ? -45.854 -4.706  -4.840  1.00 24.80  ? 685  ASP A N   1 
ATOM   5468 C CA  . ASP A 1 685 ? -45.965 -5.136  -3.432  1.00 25.77  ? 685  ASP A CA  1 
ATOM   5469 C C   . ASP A 1 685 ? -46.182 -6.637  -3.274  1.00 25.79  ? 685  ASP A C   1 
ATOM   5470 O O   . ASP A 1 685 ? -46.980 -7.242  -3.982  1.00 23.34  ? 685  ASP A O   1 
ATOM   5471 C CB  . ASP A 1 685 ? -47.064 -4.369  -2.723  1.00 27.93  ? 685  ASP A CB  1 
ATOM   5472 C CG  . ASP A 1 685 ? -46.771 -2.888  -2.636  1.00 31.74  ? 685  ASP A CG  1 
ATOM   5473 O OD1 . ASP A 1 685 ? -45.797 -2.488  -1.950  1.00 37.22  ? 685  ASP A OD1 1 
ATOM   5474 O OD2 . ASP A 1 685 ? -47.506 -2.114  -3.278  1.00 37.27  ? 685  ASP A OD2 1 
ATOM   5475 N N   . GLU A 1 686 ? -45.419 -7.228  -2.356  1.00 26.10  ? 686  GLU A N   1 
ATOM   5476 C CA  . GLU A 1 686 ? -45.500 -8.646  -2.065  1.00 27.04  ? 686  GLU A CA  1 
ATOM   5477 C C   . GLU A 1 686 ? -46.922 -9.072  -1.754  1.00 26.98  ? 686  GLU A C   1 
ATOM   5478 O O   . GLU A 1 686 ? -47.594 -8.459  -0.916  1.00 26.63  ? 686  GLU A O   1 
ATOM   5479 C CB  . GLU A 1 686 ? -44.603 -9.004  -0.892  1.00 27.18  ? 686  GLU A CB  1 
ATOM   5480 C CG  . GLU A 1 686 ? -44.347 -10.479 -0.819  1.00 29.65  ? 686  GLU A CG  1 
ATOM   5481 C CD  . GLU A 1 686 ? -43.371 -10.857 0.270   1.00 34.94  ? 686  GLU A CD  1 
ATOM   5482 O OE1 . GLU A 1 686 ? -42.508 -10.032 0.603   1.00 34.88  ? 686  GLU A OE1 1 
ATOM   5483 O OE2 . GLU A 1 686 ? -43.481 -11.987 0.810   1.00 39.91  ? 686  GLU A OE2 1 
ATOM   5484 N N   . GLY A 1 687 ? -47.375 -10.107 -2.449  1.00 26.68  ? 687  GLY A N   1 
ATOM   5485 C CA  . GLY A 1 687 ? -48.677 -10.697 -2.163  1.00 27.31  ? 687  GLY A CA  1 
ATOM   5486 C C   . GLY A 1 687 ? -49.817 -10.018 -2.864  1.00 27.75  ? 687  GLY A C   1 
ATOM   5487 O O   . GLY A 1 687 ? -50.926 -10.518 -2.829  1.00 28.07  ? 687  GLY A O   1 
ATOM   5488 N N   . ALA A 1 688 ? -49.543 -8.893  -3.526  1.00 27.35  ? 688  ALA A N   1 
ATOM   5489 C CA  . ALA A 1 688 ? -50.594 -8.099  -4.152  1.00 27.27  ? 688  ALA A CA  1 
ATOM   5490 C C   . ALA A 1 688 ? -51.077 -8.637  -5.497  1.00 27.66  ? 688  ALA A C   1 
ATOM   5491 O O   . ALA A 1 688 ? -50.289 -9.130  -6.297  1.00 26.12  ? 688  ALA A O   1 
ATOM   5492 C CB  . ALA A 1 688 ? -50.158 -6.597  -4.273  1.00 27.42  ? 688  ALA A CB  1 
ATOM   5493 N N   . GLU A 1 689 ? -52.394 -8.536  -5.719  1.00 28.23  ? 689  GLU A N   1 
ATOM   5494 C CA  . GLU A 1 689 ? -53.031 -8.816  -7.012  1.00 29.97  ? 689  GLU A CA  1 
ATOM   5495 C C   . GLU A 1 689 ? -53.875 -7.587  -7.427  1.00 28.89  ? 689  GLU A C   1 
ATOM   5496 O O   . GLU A 1 689 ? -54.879 -7.666  -8.173  1.00 27.38  ? 689  GLU A O   1 
ATOM   5497 C CB  . GLU A 1 689 ? -53.824 -10.135 -6.971  1.00 30.21  ? 689  GLU A CB  1 
ATOM   5498 C CG  . GLU A 1 689 ? -52.916 -11.387 -6.939  1.00 32.81  ? 689  GLU A CG  1 
ATOM   5499 C CD  . GLU A 1 689 ? -53.627 -12.678 -7.375  1.00 35.75  ? 689  GLU A CD  1 
ATOM   5500 O OE1 . GLU A 1 689 ? -54.734 -12.928 -6.827  1.00 39.19  ? 689  GLU A OE1 1 
ATOM   5501 O OE2 . GLU A 1 689 ? -53.093 -13.429 -8.278  1.00 41.46  ? 689  GLU A OE2 1 
ATOM   5502 N N   . LYS A 1 690 ? -53.426 -6.450  -6.910  1.00 29.17  ? 690  LYS A N   1 
ATOM   5503 C CA  . LYS A 1 690 ? -54.016 -5.139  -7.113  1.00 30.71  ? 690  LYS A CA  1 
ATOM   5504 C C   . LYS A 1 690 ? -52.880 -4.155  -7.065  1.00 30.57  ? 690  LYS A C   1 
ATOM   5505 O O   . LYS A 1 690 ? -51.811 -4.453  -6.503  1.00 31.44  ? 690  LYS A O   1 
ATOM   5506 C CB  . LYS A 1 690 ? -54.941 -4.759  -5.958  1.00 31.11  ? 690  LYS A CB  1 
ATOM   5507 C CG  . LYS A 1 690 ? -56.311 -5.379  -6.007  1.00 35.41  ? 690  LYS A CG  1 
ATOM   5508 C CD  . LYS A 1 690 ? -56.972 -5.256  -4.650  1.00 40.19  ? 690  LYS A CD  1 
ATOM   5509 C CE  . LYS A 1 690 ? -58.293 -6.027  -4.601  1.00 44.14  ? 690  LYS A CE  1 
ATOM   5510 N NZ  . LYS A 1 690 ? -59.125 -5.583  -3.416  1.00 45.12  ? 690  LYS A NZ  1 
ATOM   5511 N N   . VAL A 1 691 ? -53.100 -2.986  -7.653  1.00 30.11  ? 691  VAL A N   1 
ATOM   5512 C CA  . VAL A 1 691 ? -52.216 -1.872  -7.424  1.00 31.18  ? 691  VAL A CA  1 
ATOM   5513 C C   . VAL A 1 691 ? -53.036 -0.587  -7.352  1.00 30.24  ? 691  VAL A C   1 
ATOM   5514 O O   . VAL A 1 691 ? -53.988 -0.397  -8.127  1.00 29.42  ? 691  VAL A O   1 
ATOM   5515 C CB  . VAL A 1 691 ? -51.146 -1.812  -8.495  1.00 30.83  ? 691  VAL A CB  1 
ATOM   5516 C CG1 . VAL A 1 691 ? -51.705 -1.231  -9.761  1.00 34.08  ? 691  VAL A CG1 1 
ATOM   5517 C CG2 . VAL A 1 691 ? -49.990 -0.989  -8.018  1.00 35.14  ? 691  VAL A CG2 1 
ATOM   5518 N N   . MET A 1 692 ? -52.704 0.238   -6.359  1.00 30.13  ? 692  MET A N   1 
ATOM   5519 C CA  . MET A 1 692 ? -53.250 1.589   -6.240  1.00 30.54  ? 692  MET A CA  1 
ATOM   5520 C C   . MET A 1 692 ? -52.482 2.402   -7.283  1.00 28.83  ? 692  MET A C   1 
ATOM   5521 O O   . MET A 1 692 ? -51.260 2.490   -7.231  1.00 29.03  ? 692  MET A O   1 
ATOM   5522 C CB  . MET A 1 692 ? -53.080 2.158   -4.817  1.00 32.18  ? 692  MET A CB  1 
ATOM   5523 C CG  . MET A 1 692 ? -54.079 1.579   -3.775  1.00 36.45  ? 692  MET A CG  1 
ATOM   5524 S SD  . MET A 1 692 ? -55.822 1.996   -4.150  1.00 48.78  ? 692  MET A SD  1 
ATOM   5525 C CE  . MET A 1 692 ? -56.739 1.251   -2.773  1.00 42.34  ? 692  MET A CE  1 
ATOM   5526 N N   . ALA A 1 693 ? -53.210 2.932   -8.250  1.00 27.04  ? 693  ALA A N   1 
ATOM   5527 C CA  . ALA A 1 693 ? -52.600 3.598   -9.402  1.00 25.36  ? 693  ALA A CA  1 
ATOM   5528 C C   . ALA A 1 693 ? -53.287 4.910   -9.671  1.00 24.34  ? 693  ALA A C   1 
ATOM   5529 O O   . ALA A 1 693 ? -54.476 5.073   -9.381  1.00 24.84  ? 693  ALA A O   1 
ATOM   5530 C CB  . ALA A 1 693 ? -52.724 2.708   -10.637 1.00 24.78  ? 693  ALA A CB  1 
ATOM   5531 N N   . TYR A 1 694 ? -52.566 5.815   -10.310 1.00 22.43  ? 694  TYR A N   1 
ATOM   5532 C CA  . TYR A 1 694 ? -53.185 7.018   -10.823 1.00 20.98  ? 694  TYR A CA  1 
ATOM   5533 C C   . TYR A 1 694 ? -53.510 6.910   -12.333 1.00 20.50  ? 694  TYR A C   1 
ATOM   5534 O O   . TYR A 1 694 ? -52.673 6.505   -13.151 1.00 20.61  ? 694  TYR A O   1 
ATOM   5535 C CB  . TYR A 1 694 ? -52.371 8.277   -10.466 1.00 21.12  ? 694  TYR A CB  1 
ATOM   5536 C CG  . TYR A 1 694 ? -53.169 9.520   -10.755 1.00 21.92  ? 694  TYR A CG  1 
ATOM   5537 C CD1 . TYR A 1 694 ? -54.238 9.870   -9.934  1.00 22.51  ? 694  TYR A CD1 1 
ATOM   5538 C CD2 . TYR A 1 694 ? -52.890 10.323  -11.859 1.00 21.31  ? 694  TYR A CD2 1 
ATOM   5539 C CE1 . TYR A 1 694 ? -55.006 10.986  -10.201 1.00 21.49  ? 694  TYR A CE1 1 
ATOM   5540 C CE2 . TYR A 1 694 ? -53.647 11.457  -12.136 1.00 22.00  ? 694  TYR A CE2 1 
ATOM   5541 C CZ  . TYR A 1 694 ? -54.702 11.777  -11.290 1.00 21.67  ? 694  TYR A CZ  1 
ATOM   5542 O OH  . TYR A 1 694 ? -55.468 12.877  -11.536 1.00 21.84  ? 694  TYR A OH  1 
ATOM   5543 N N   . VAL A 1 695 ? -54.755 7.204   -12.690 1.00 17.84  ? 695  VAL A N   1 
ATOM   5544 C CA  . VAL A 1 695 ? -55.139 7.283   -14.090 1.00 17.99  ? 695  VAL A CA  1 
ATOM   5545 C C   . VAL A 1 695 ? -55.242 8.766   -14.512 1.00 18.02  ? 695  VAL A C   1 
ATOM   5546 O O   . VAL A 1 695 ? -56.133 9.511   -14.042 1.00 17.81  ? 695  VAL A O   1 
ATOM   5547 C CB  . VAL A 1 695 ? -56.479 6.532   -14.332 1.00 18.37  ? 695  VAL A CB  1 
ATOM   5548 C CG1 . VAL A 1 695 ? -56.886 6.633   -15.771 1.00 16.77  ? 695  VAL A CG1 1 
ATOM   5549 C CG2 . VAL A 1 695 ? -56.386 5.078   -13.861 1.00 19.58  ? 695  VAL A CG2 1 
ATOM   5550 N N   . PRO A 1 696 ? -54.291 9.239   -15.346 1.00 17.52  ? 696  PRO A N   1 
ATOM   5551 C CA  . PRO A 1 696 ? -54.289 10.637  -15.779 1.00 17.32  ? 696  PRO A CA  1 
ATOM   5552 C C   . PRO A 1 696 ? -55.533 11.069  -16.601 1.00 18.00  ? 696  PRO A C   1 
ATOM   5553 O O   . PRO A 1 696 ? -56.318 10.234  -17.050 1.00 17.66  ? 696  PRO A O   1 
ATOM   5554 C CB  . PRO A 1 696 ? -53.011 10.734  -16.625 1.00 17.63  ? 696  PRO A CB  1 
ATOM   5555 C CG  . PRO A 1 696 ? -52.096 9.630   -16.073 1.00 16.55  ? 696  PRO A CG  1 
ATOM   5556 C CD  . PRO A 1 696 ? -53.106 8.498   -15.843 1.00 17.53  ? 696  PRO A CD  1 
ATOM   5557 N N   . ASP A 1 697 ? -55.625 12.374  -16.813 1.00 18.88  ? 697  ASP A N   1 
ATOM   5558 C CA  . ASP A 1 697 ? -56.670 13.066  -17.554 1.00 19.89  ? 697  ASP A CA  1 
ATOM   5559 C C   . ASP A 1 697 ? -56.556 12.818  -19.057 1.00 20.44  ? 697  ASP A C   1 
ATOM   5560 O O   . ASP A 1 697 ? -56.095 13.676  -19.835 1.00 20.56  ? 697  ASP A O   1 
ATOM   5561 C CB  . ASP A 1 697 ? -56.586 14.558  -17.227 1.00 20.56  ? 697  ASP A CB  1 
ATOM   5562 C CG  . ASP A 1 697 ? -57.809 15.348  -17.686 1.00 24.82  ? 697  ASP A CG  1 
ATOM   5563 O OD1 . ASP A 1 697 ? -58.786 14.759  -18.220 1.00 26.82  ? 697  ASP A OD1 1 
ATOM   5564 O OD2 . ASP A 1 697 ? -57.779 16.586  -17.505 1.00 27.47  ? 697  ASP A OD2 1 
ATOM   5565 N N   . ALA A 1 698 ? -56.999 11.631  -19.470 1.00 19.22  ? 698  ALA A N   1 
ATOM   5566 C CA  . ALA A 1 698 ? -56.976 11.258  -20.875 1.00 18.51  ? 698  ALA A CA  1 
ATOM   5567 C C   . ALA A 1 698 ? -57.938 10.130  -21.021 1.00 17.50  ? 698  ALA A C   1 
ATOM   5568 O O   . ALA A 1 698 ? -58.306 9.483   -20.036 1.00 17.35  ? 698  ALA A O   1 
ATOM   5569 C CB  . ALA A 1 698 ? -55.542 10.771  -21.309 1.00 16.98  ? 698  ALA A CB  1 
ATOM   5570 N N   . VAL A 1 699 ? -58.291 9.856   -22.263 1.00 17.93  ? 699  VAL A N   1 
ATOM   5571 C CA  . VAL A 1 699 ? -58.984 8.609   -22.613 1.00 18.69  ? 699  VAL A CA  1 
ATOM   5572 C C   . VAL A 1 699 ? -57.931 7.488   -22.537 1.00 18.84  ? 699  VAL A C   1 
ATOM   5573 O O   . VAL A 1 699 ? -56.828 7.679   -23.042 1.00 18.14  ? 699  VAL A O   1 
ATOM   5574 C CB  . VAL A 1 699 ? -59.551 8.695   -24.050 1.00 18.87  ? 699  VAL A CB  1 
ATOM   5575 C CG1 . VAL A 1 699 ? -59.980 7.327   -24.532 1.00 20.83  ? 699  VAL A CG1 1 
ATOM   5576 C CG2 . VAL A 1 699 ? -60.697 9.695   -24.127 1.00 21.20  ? 699  VAL A CG2 1 
ATOM   5577 N N   . TRP A 1 700 ? -58.215 6.377   -21.857 1.00 16.97  ? 700  TRP A N   1 
ATOM   5578 C CA  . TRP A 1 700 ? -57.270 5.244   -21.850 1.00 18.08  ? 700  TRP A CA  1 
ATOM   5579 C C   . TRP A 1 700 ? -57.934 3.943   -22.285 1.00 18.39  ? 700  TRP A C   1 
ATOM   5580 O O   . TRP A 1 700 ? -59.093 3.678   -21.937 1.00 19.30  ? 700  TRP A O   1 
ATOM   5581 C CB  . TRP A 1 700 ? -56.655 5.006   -20.470 1.00 16.87  ? 700  TRP A CB  1 
ATOM   5582 C CG  . TRP A 1 700 ? -55.892 6.167   -19.934 1.00 18.09  ? 700  TRP A CG  1 
ATOM   5583 C CD1 . TRP A 1 700 ? -56.357 7.143   -19.105 1.00 17.54  ? 700  TRP A CD1 1 
ATOM   5584 C CD2 . TRP A 1 700 ? -54.518 6.480   -20.203 1.00 15.63  ? 700  TRP A CD2 1 
ATOM   5585 N NE1 . TRP A 1 700 ? -55.366 8.057   -18.837 1.00 17.17  ? 700  TRP A NE1 1 
ATOM   5586 C CE2 . TRP A 1 700 ? -54.229 7.684   -19.516 1.00 17.39  ? 700  TRP A CE2 1 
ATOM   5587 C CE3 . TRP A 1 700 ? -53.517 5.868   -20.986 1.00 16.35  ? 700  TRP A CE3 1 
ATOM   5588 C CZ2 . TRP A 1 700 ? -52.960 8.278   -19.540 1.00 19.11  ? 700  TRP A CZ2 1 
ATOM   5589 C CZ3 . TRP A 1 700 ? -52.251 6.463   -21.039 1.00 15.28  ? 700  TRP A CZ3 1 
ATOM   5590 C CH2 . TRP A 1 700 ? -51.988 7.673   -20.322 1.00 16.56  ? 700  TRP A CH2 1 
ATOM   5591 N N   . TYR A 1 701 ? -57.169 3.110   -22.984 1.00 17.67  ? 701  TYR A N   1 
ATOM   5592 C CA  . TYR A 1 701 ? -57.626 1.796   -23.435 1.00 17.10  ? 701  TYR A CA  1 
ATOM   5593 C C   . TYR A 1 701 ? -56.733 0.697   -22.892 1.00 18.40  ? 701  TYR A C   1 
ATOM   5594 O O   . TYR A 1 701 ? -55.502 0.803   -22.952 1.00 15.88  ? 701  TYR A O   1 
ATOM   5595 C CB  . TYR A 1 701 ? -57.563 1.754   -24.954 1.00 17.16  ? 701  TYR A CB  1 
ATOM   5596 C CG  . TYR A 1 701 ? -58.369 2.827   -25.666 1.00 17.45  ? 701  TYR A CG  1 
ATOM   5597 C CD1 . TYR A 1 701 ? -59.742 2.636   -25.891 1.00 18.54  ? 701  TYR A CD1 1 
ATOM   5598 C CD2 . TYR A 1 701 ? -57.769 4.018   -26.127 1.00 17.03  ? 701  TYR A CD2 1 
ATOM   5599 C CE1 . TYR A 1 701 ? -60.492 3.585   -26.548 1.00 17.31  ? 701  TYR A CE1 1 
ATOM   5600 C CE2 . TYR A 1 701 ? -58.526 5.020   -26.788 1.00 18.12  ? 701  TYR A CE2 1 
ATOM   5601 C CZ  . TYR A 1 701 ? -59.913 4.769   -26.982 1.00 16.87  ? 701  TYR A CZ  1 
ATOM   5602 O OH  . TYR A 1 701 ? -60.735 5.672   -27.628 1.00 18.01  ? 701  TYR A OH  1 
ATOM   5603 N N   . ASP A 1 702 ? -57.334 -0.362  -22.371 1.00 18.20  ? 702  ASP A N   1 
ATOM   5604 C CA  . ASP A 1 702 ? -56.598 -1.594  -22.055 1.00 19.25  ? 702  ASP A CA  1 
ATOM   5605 C C   . ASP A 1 702 ? -55.838 -2.128  -23.281 1.00 19.37  ? 702  ASP A C   1 
ATOM   5606 O O   . ASP A 1 702 ? -56.419 -2.356  -24.373 1.00 17.53  ? 702  ASP A O   1 
ATOM   5607 C CB  . ASP A 1 702 ? -57.565 -2.649  -21.497 1.00 21.07  ? 702  ASP A CB  1 
ATOM   5608 C CG  . ASP A 1 702 ? -56.852 -3.882  -21.070 1.00 25.22  ? 702  ASP A CG  1 
ATOM   5609 O OD1 . ASP A 1 702 ? -56.580 -3.979  -19.871 1.00 32.53  ? 702  ASP A OD1 1 
ATOM   5610 O OD2 . ASP A 1 702 ? -56.501 -4.715  -21.935 1.00 28.53  ? 702  ASP A OD2 1 
ATOM   5611 N N   . TYR A 1 703 ? -54.515 -2.287  -23.138 1.00 18.81  ? 703  TYR A N   1 
ATOM   5612 C CA  . TYR A 1 703 ? -53.702 -2.663  -24.274 1.00 20.23  ? 703  TYR A CA  1 
ATOM   5613 C C   . TYR A 1 703 ? -54.164 -3.988  -24.901 1.00 22.36  ? 703  TYR A C   1 
ATOM   5614 O O   . TYR A 1 703 ? -54.258 -4.104  -26.123 1.00 23.53  ? 703  TYR A O   1 
ATOM   5615 C CB  . TYR A 1 703 ? -52.201 -2.737  -23.892 1.00 20.25  ? 703  TYR A CB  1 
ATOM   5616 C CG  . TYR A 1 703 ? -51.391 -3.310  -25.021 1.00 21.53  ? 703  TYR A CG  1 
ATOM   5617 C CD1 . TYR A 1 703 ? -50.848 -2.478  -25.994 1.00 19.08  ? 703  TYR A CD1 1 
ATOM   5618 C CD2 . TYR A 1 703 ? -51.210 -4.698  -25.148 1.00 20.97  ? 703  TYR A CD2 1 
ATOM   5619 C CE1 . TYR A 1 703 ? -50.124 -3.004  -27.071 1.00 19.87  ? 703  TYR A CE1 1 
ATOM   5620 C CE2 . TYR A 1 703 ? -50.501 -5.233  -26.212 1.00 21.82  ? 703  TYR A CE2 1 
ATOM   5621 C CZ  . TYR A 1 703 ? -49.951 -4.371  -27.160 1.00 21.26  ? 703  TYR A CZ  1 
ATOM   5622 O OH  . TYR A 1 703 ? -49.234 -4.873  -28.214 1.00 24.59  ? 703  TYR A OH  1 
ATOM   5623 N N   . GLU A 1 704 ? -54.461 -4.983  -24.077 1.00 23.70  ? 704  GLU A N   1 
ATOM   5624 C CA  . GLU A 1 704 ? -54.756 -6.310  -24.614 1.00 25.37  ? 704  GLU A CA  1 
ATOM   5625 C C   . GLU A 1 704 ? -56.147 -6.460  -25.210 1.00 24.33  ? 704  GLU A C   1 
ATOM   5626 O O   . GLU A 1 704 ? -56.291 -7.028  -26.278 1.00 25.23  ? 704  GLU A O   1 
ATOM   5627 C CB  . GLU A 1 704 ? -54.514 -7.377  -23.569 1.00 25.65  ? 704  GLU A CB  1 
ATOM   5628 C CG  . GLU A 1 704 ? -53.000 -7.569  -23.385 1.00 31.92  ? 704  GLU A CG  1 
ATOM   5629 C CD  . GLU A 1 704 ? -52.659 -8.894  -22.787 1.00 37.59  ? 704  GLU A CD  1 
ATOM   5630 O OE1 . GLU A 1 704 ? -52.890 -9.947  -23.462 1.00 40.38  ? 704  GLU A OE1 1 
ATOM   5631 O OE2 . GLU A 1 704 ? -52.152 -8.873  -21.643 1.00 38.73  ? 704  GLU A OE2 1 
ATOM   5632 N N   . THR A 1 705 ? -57.154 -5.950  -24.514 1.00 24.26  ? 705  THR A N   1 
ATOM   5633 C CA  . THR A 1 705 ? -58.533 -6.054  -24.998 1.00 23.29  ? 705  THR A CA  1 
ATOM   5634 C C   . THR A 1 705 ? -58.895 -4.890  -25.904 1.00 22.94  ? 705  THR A C   1 
ATOM   5635 O O   . THR A 1 705 ? -59.769 -5.013  -26.766 1.00 22.28  ? 705  THR A O   1 
ATOM   5636 C CB  . THR A 1 705 ? -59.527 -6.106  -23.839 1.00 23.35  ? 705  THR A CB  1 
ATOM   5637 O OG1 . THR A 1 705 ? -59.480 -4.887  -23.124 1.00 23.29  ? 705  THR A OG1 1 
ATOM   5638 C CG2 . THR A 1 705 ? -59.204 -7.206  -22.856 1.00 26.93  ? 705  THR A CG2 1 
ATOM   5639 N N   . GLY A 1 706 ? -58.237 -3.747  -25.717 1.00 20.66  ? 706  GLY A N   1 
ATOM   5640 C CA  . GLY A 1 706 ? -58.590 -2.554  -26.442 1.00 20.15  ? 706  GLY A CA  1 
ATOM   5641 C C   . GLY A 1 706 ? -59.796 -1.826  -25.843 1.00 20.47  ? 706  GLY A C   1 
ATOM   5642 O O   . GLY A 1 706 ? -60.210 -0.794  -26.367 1.00 19.02  ? 706  GLY A O   1 
ATOM   5643 N N   . SER A 1 707 ? -60.343 -2.303  -24.732 1.00 21.09  ? 707  SER A N   1 
ATOM   5644 C CA  . SER A 1 707 ? -61.515 -1.577  -24.220 1.00 22.19  ? 707  SER A CA  1 
ATOM   5645 C C   . SER A 1 707 ? -61.166 -0.299  -23.475 1.00 22.33  ? 707  SER A C   1 
ATOM   5646 O O   . SER A 1 707 ? -60.143 -0.220  -22.770 1.00 20.08  ? 707  SER A O   1 
ATOM   5647 C CB  . SER A 1 707 ? -62.444 -2.461  -23.403 1.00 23.76  ? 707  SER A CB  1 
ATOM   5648 O OG  . SER A 1 707 ? -61.940 -2.669  -22.127 1.00 30.24  ? 707  SER A OG  1 
ATOM   5649 N N   . GLN A 1 708 ? -62.015 0.709   -23.653 1.00 22.17  ? 708  GLN A N   1 
ATOM   5650 C CA  . GLN A 1 708 ? -61.844 1.981   -22.983 1.00 23.95  ? 708  GLN A CA  1 
ATOM   5651 C C   . GLN A 1 708 ? -62.130 1.856   -21.485 1.00 24.78  ? 708  GLN A C   1 
ATOM   5652 O O   . GLN A 1 708 ? -63.166 1.347   -21.089 1.00 26.49  ? 708  GLN A O   1 
ATOM   5653 C CB  . GLN A 1 708 ? -62.735 3.030   -23.621 1.00 23.72  ? 708  GLN A CB  1 
ATOM   5654 C CG  . GLN A 1 708 ? -62.479 4.426   -23.093 1.00 24.45  ? 708  GLN A CG  1 
ATOM   5655 C CD  . GLN A 1 708 ? -63.383 5.479   -23.745 1.00 27.71  ? 708  GLN A CD  1 
ATOM   5656 O OE1 . GLN A 1 708 ? -63.895 5.285   -24.839 1.00 27.20  ? 708  GLN A OE1 1 
ATOM   5657 N NE2 . GLN A 1 708 ? -63.531 6.621   -23.082 1.00 28.14  ? 708  GLN A NE2 1 
ATOM   5658 N N   . VAL A 1 709 ? -61.203 2.288   -20.645 1.00 24.19  ? 709  VAL A N   1 
ATOM   5659 C CA  . VAL A 1 709 ? -61.427 2.207   -19.206 1.00 24.88  ? 709  VAL A CA  1 
ATOM   5660 C C   . VAL A 1 709 ? -62.422 3.303   -18.811 1.00 25.32  ? 709  VAL A C   1 
ATOM   5661 O O   . VAL A 1 709 ? -62.557 4.319   -19.522 1.00 23.49  ? 709  VAL A O   1 
ATOM   5662 C CB  . VAL A 1 709 ? -60.109 2.271   -18.377 1.00 25.79  ? 709  VAL A CB  1 
ATOM   5663 C CG1 . VAL A 1 709 ? -59.175 1.194   -18.848 1.00 26.43  ? 709  VAL A CG1 1 
ATOM   5664 C CG2 . VAL A 1 709 ? -59.439 3.665   -18.452 1.00 23.67  ? 709  VAL A CG2 1 
ATOM   5665 N N   . ARG A 1 710 ? -63.153 3.069   -17.723 1.00 26.06  ? 710  ARG A N   1 
ATOM   5666 C CA  . ARG A 1 710 ? -64.076 4.093   -17.228 1.00 29.86  ? 710  ARG A CA  1 
ATOM   5667 C C   . ARG A 1 710 ? -63.276 5.199   -16.506 1.00 29.35  ? 710  ARG A C   1 
ATOM   5668 O O   . ARG A 1 710 ? -63.682 6.355   -16.484 1.00 31.80  ? 710  ARG A O   1 
ATOM   5669 C CB  . ARG A 1 710 ? -65.167 3.489   -16.327 1.00 29.66  ? 710  ARG A CB  1 
ATOM   5670 C CG  . ARG A 1 710 ? -64.625 2.631   -15.159 1.00 33.42  ? 710  ARG A CG  1 
ATOM   5671 C CD  . ARG A 1 710 ? -65.703 2.302   -14.081 1.00 35.16  ? 710  ARG A CD  1 
ATOM   5672 N NE  . ARG A 1 710 ? -65.068 1.997   -12.790 1.00 46.61  ? 710  ARG A NE  1 
ATOM   5673 C CZ  . ARG A 1 710 ? -64.726 2.908   -11.872 1.00 51.07  ? 710  ARG A CZ  1 
ATOM   5674 N NH1 . ARG A 1 710 ? -64.953 4.209   -12.084 1.00 53.82  ? 710  ARG A NH1 1 
ATOM   5675 N NH2 . ARG A 1 710 ? -64.151 2.527   -10.728 1.00 52.40  ? 710  ARG A NH2 1 
ATOM   5676 N N   . TRP A 1 711 ? -62.111 4.871   -15.981 1.00 28.51  ? 711  TRP A N   1 
ATOM   5677 C CA  . TRP A 1 711 ? -61.364 5.845   -15.180 1.00 27.43  ? 711  TRP A CA  1 
ATOM   5678 C C   . TRP A 1 711 ? -60.791 7.014   -15.965 1.00 26.00  ? 711  TRP A C   1 
ATOM   5679 O O   . TRP A 1 711 ? -60.316 6.845   -17.082 1.00 25.19  ? 711  TRP A O   1 
ATOM   5680 C CB  . TRP A 1 711 ? -60.222 5.148   -14.483 1.00 28.29  ? 711  TRP A CB  1 
ATOM   5681 C CG  . TRP A 1 711 ? -60.609 3.858   -13.818 1.00 31.00  ? 711  TRP A CG  1 
ATOM   5682 C CD1 . TRP A 1 711 ? -61.649 3.646   -12.938 1.00 32.12  ? 711  TRP A CD1 1 
ATOM   5683 C CD2 . TRP A 1 711 ? -59.944 2.605   -13.965 1.00 32.55  ? 711  TRP A CD2 1 
ATOM   5684 N NE1 . TRP A 1 711 ? -61.661 2.335   -12.542 1.00 32.83  ? 711  TRP A NE1 1 
ATOM   5685 C CE2 . TRP A 1 711 ? -60.627 1.673   -13.154 1.00 33.19  ? 711  TRP A CE2 1 
ATOM   5686 C CE3 . TRP A 1 711 ? -58.836 2.173   -14.711 1.00 31.51  ? 711  TRP A CE3 1 
ATOM   5687 C CZ2 . TRP A 1 711 ? -60.230 0.337   -13.057 1.00 32.40  ? 711  TRP A CZ2 1 
ATOM   5688 C CZ3 . TRP A 1 711 ? -58.450 0.837   -14.616 1.00 31.81  ? 711  TRP A CZ3 1 
ATOM   5689 C CH2 . TRP A 1 711 ? -59.139 -0.058  -13.793 1.00 31.39  ? 711  TRP A CH2 1 
ATOM   5690 N N   . ARG A 1 712 ? -60.774 8.195   -15.344 1.00 24.99  ? 712  ARG A N   1 
ATOM   5691 C CA  . ARG A 1 712 ? -60.082 9.352   -15.920 1.00 23.84  ? 712  ARG A CA  1 
ATOM   5692 C C   . ARG A 1 712 ? -59.728 10.347  -14.827 1.00 22.99  ? 712  ARG A C   1 
ATOM   5693 O O   . ARG A 1 712 ? -60.588 10.754  -14.025 1.00 21.51  ? 712  ARG A O   1 
ATOM   5694 C CB  . ARG A 1 712 ? -60.953 10.050  -16.965 1.00 24.59  ? 712  ARG A CB  1 
ATOM   5695 C CG  . ARG A 1 712 ? -60.235 11.197  -17.657 1.00 23.82  ? 712  ARG A CG  1 
ATOM   5696 C CD  . ARG A 1 712 ? -60.983 11.706  -18.855 1.00 28.67  ? 712  ARG A CD  1 
ATOM   5697 N NE  . ARG A 1 712 ? -60.159 12.704  -19.538 1.00 28.83  ? 712  ARG A NE  1 
ATOM   5698 C CZ  . ARG A 1 712 ? -60.267 13.038  -20.810 1.00 29.90  ? 712  ARG A CZ  1 
ATOM   5699 N NH1 . ARG A 1 712 ? -61.155 12.431  -21.589 1.00 28.77  ? 712  ARG A NH1 1 
ATOM   5700 N NH2 . ARG A 1 712 ? -59.456 13.964  -21.306 1.00 30.89  ? 712  ARG A NH2 1 
ATOM   5701 N N   . LYS A 1 713 ? -58.459 10.748  -14.778 1.00 21.26  ? 713  LYS A N   1 
ATOM   5702 C CA  . LYS A 1 713 ? -58.039 11.744  -13.793 1.00 21.24  ? 713  LYS A CA  1 
ATOM   5703 C C   . LYS A 1 713 ? -58.389 11.330  -12.355 1.00 21.63  ? 713  LYS A C   1 
ATOM   5704 O O   . LYS A 1 713 ? -59.043 12.067  -11.597 1.00 20.95  ? 713  LYS A O   1 
ATOM   5705 C CB  . LYS A 1 713 ? -58.588 13.151  -14.130 1.00 20.92  ? 713  LYS A CB  1 
ATOM   5706 C CG  . LYS A 1 713 ? -57.751 14.271  -13.465 1.00 22.07  ? 713  LYS A CG  1 
ATOM   5707 C CD  . LYS A 1 713 ? -58.223 15.704  -13.861 1.00 20.27  ? 713  LYS A CD  1 
ATOM   5708 C CE  . LYS A 1 713 ? -57.230 16.774  -13.306 1.00 22.21  ? 713  LYS A CE  1 
ATOM   5709 N NZ  . LYS A 1 713 ? -57.575 18.185  -13.655 1.00 24.49  ? 713  LYS A NZ  1 
ATOM   5710 N N   . GLN A 1 714 ? -57.944 10.152  -11.957 1.00 21.33  ? 714  GLN A N   1 
ATOM   5711 C CA  . GLN A 1 714 ? -58.346 9.658   -10.651 1.00 22.74  ? 714  GLN A CA  1 
ATOM   5712 C C   . GLN A 1 714 ? -57.480 8.521   -10.197 1.00 23.17  ? 714  GLN A C   1 
ATOM   5713 O O   . GLN A 1 714 ? -56.860 7.813   -11.013 1.00 22.70  ? 714  GLN A O   1 
ATOM   5714 C CB  . GLN A 1 714 ? -59.813 9.204   -10.660 1.00 22.74  ? 714  GLN A CB  1 
ATOM   5715 C CG  . GLN A 1 714 ? -60.078 7.982   -11.526 1.00 24.32  ? 714  GLN A CG  1 
ATOM   5716 C CD  . GLN A 1 714 ? -61.556 7.689   -11.607 1.00 28.76  ? 714  GLN A CD  1 
ATOM   5717 O OE1 . GLN A 1 714 ? -62.142 7.220   -10.627 1.00 34.46  ? 714  GLN A OE1 1 
ATOM   5718 N NE2 . GLN A 1 714 ? -62.182 7.994   -12.747 1.00 24.96  ? 714  GLN A NE2 1 
ATOM   5719 N N   . LYS A 1 715 ? -57.468 8.334   -8.891  1.00 23.89  ? 715  LYS A N   1 
ATOM   5720 C CA  . LYS A 1 715 ? -56.770 7.224   -8.298  1.00 27.33  ? 715  LYS A CA  1 
ATOM   5721 C C   . LYS A 1 715 ? -57.711 6.039   -8.364  1.00 27.07  ? 715  LYS A C   1 
ATOM   5722 O O   . LYS A 1 715 ? -58.904 6.199   -8.110  1.00 28.42  ? 715  LYS A O   1 
ATOM   5723 C CB  . LYS A 1 715 ? -56.404 7.522   -6.859  1.00 26.45  ? 715  LYS A CB  1 
ATOM   5724 C CG  . LYS A 1 715 ? -55.235 6.667   -6.385  1.00 30.53  ? 715  LYS A CG  1 
ATOM   5725 C CD  . LYS A 1 715 ? -54.783 6.980   -4.935  1.00 31.83  ? 715  LYS A CD  1 
ATOM   5726 C CE  . LYS A 1 715 ? -53.348 6.455   -4.692  1.00 37.36  ? 715  LYS A CE  1 
ATOM   5727 N NZ  . LYS A 1 715 ? -52.369 6.804   -5.799  1.00 40.68  ? 715  LYS A NZ  1 
ATOM   5728 N N   . VAL A 1 716 ? -57.192 4.872   -8.739  1.00 27.29  ? 716  VAL A N   1 
ATOM   5729 C CA  . VAL A 1 716 ? -57.985 3.626   -8.800  1.00 28.18  ? 716  VAL A CA  1 
ATOM   5730 C C   . VAL A 1 716 ? -57.206 2.458   -8.177  1.00 28.76  ? 716  VAL A C   1 
ATOM   5731 O O   . VAL A 1 716 ? -55.986 2.511   -8.069  1.00 29.12  ? 716  VAL A O   1 
ATOM   5732 C CB  . VAL A 1 716 ? -58.342 3.242   -10.248 1.00 27.80  ? 716  VAL A CB  1 
ATOM   5733 C CG1 . VAL A 1 716 ? -59.111 4.372   -10.936 1.00 28.39  ? 716  VAL A CG1 1 
ATOM   5734 C CG2 . VAL A 1 716 ? -57.080 2.919   -11.053 1.00 28.19  ? 716  VAL A CG2 1 
ATOM   5735 N N   . GLU A 1 717 ? -57.905 1.404   -7.782  1.00 29.57  ? 717  GLU A N   1 
ATOM   5736 C CA  . GLU A 1 717 ? -57.217 0.151   -7.480  1.00 30.74  ? 717  GLU A CA  1 
ATOM   5737 C C   . GLU A 1 717 ? -57.386 -0.718  -8.725  1.00 29.78  ? 717  GLU A C   1 
ATOM   5738 O O   . GLU A 1 717 ? -58.505 -1.114  -9.098  1.00 29.66  ? 717  GLU A O   1 
ATOM   5739 C CB  . GLU A 1 717 ? -57.750 -0.527  -6.208  1.00 31.64  ? 717  GLU A CB  1 
ATOM   5740 C CG  . GLU A 1 717 ? -59.110 -1.168  -6.393  1.00 38.66  ? 717  GLU A CG  1 
ATOM   5741 C CD  . GLU A 1 717 ? -59.328 -2.369  -5.470  1.00 46.84  ? 717  GLU A CD  1 
ATOM   5742 O OE1 . GLU A 1 717 ? -58.714 -2.394  -4.361  1.00 49.53  ? 717  GLU A OE1 1 
ATOM   5743 O OE2 . GLU A 1 717 ? -60.108 -3.275  -5.866  1.00 49.29  ? 717  GLU A OE2 1 
ATOM   5744 N N   . MET A 1 718 ? -56.286 -0.938  -9.427  1.00 28.07  ? 718  MET A N   1 
ATOM   5745 C CA  . MET A 1 718 ? -56.346 -1.668  -10.673 1.00 28.00  ? 718  MET A CA  1 
ATOM   5746 C C   . MET A 1 718 ? -56.186 -3.142  -10.339 1.00 27.17  ? 718  MET A C   1 
ATOM   5747 O O   . MET A 1 718 ? -55.294 -3.490  -9.564  1.00 26.61  ? 718  MET A O   1 
ATOM   5748 C CB  . MET A 1 718 ? -55.198 -1.197  -11.556 1.00 28.12  ? 718  MET A CB  1 
ATOM   5749 C CG  . MET A 1 718 ? -55.452 -1.306  -13.014 1.00 30.67  ? 718  MET A CG  1 
ATOM   5750 S SD  . MET A 1 718 ? -54.028 -0.587  -13.857 1.00 29.09  ? 718  MET A SD  1 
ATOM   5751 C CE  . MET A 1 718 ? -54.393 1.162   -13.925 1.00 23.58  ? 718  MET A CE  1 
ATOM   5752 N N   . GLU A 1 719 ? -57.032 -4.005  -10.888 1.00 26.61  ? 719  GLU A N   1 
ATOM   5753 C CA  . GLU A 1 719 ? -56.962 -5.435  -10.528 1.00 27.09  ? 719  GLU A CA  1 
ATOM   5754 C C   . GLU A 1 719 ? -55.890 -6.073  -11.398 1.00 26.05  ? 719  GLU A C   1 
ATOM   5755 O O   . GLU A 1 719 ? -56.011 -6.102  -12.619 1.00 26.04  ? 719  GLU A O   1 
ATOM   5756 C CB  . GLU A 1 719 ? -58.282 -6.167  -10.771 1.00 28.37  ? 719  GLU A CB  1 
ATOM   5757 C CG  . GLU A 1 719 ? -59.509 -5.492  -10.175 1.00 35.48  ? 719  GLU A CG  1 
ATOM   5758 C CD  . GLU A 1 719 ? -59.736 -5.793  -8.695  1.00 44.04  ? 719  GLU A CD  1 
ATOM   5759 O OE1 . GLU A 1 719 ? -58.758 -6.079  -7.973  1.00 47.89  ? 719  GLU A OE1 1 
ATOM   5760 O OE2 . GLU A 1 719 ? -60.915 -5.721  -8.246  1.00 48.30  ? 719  GLU A OE2 1 
ATOM   5761 N N   . LEU A 1 720 ? -54.840 -6.567  -10.774 1.00 24.28  ? 720  LEU A N   1 
ATOM   5762 C CA  . LEU A 1 720 ? -53.734 -7.116  -11.545 1.00 24.05  ? 720  LEU A CA  1 
ATOM   5763 C C   . LEU A 1 720 ? -53.275 -8.438  -10.929 1.00 23.04  ? 720  LEU A C   1 
ATOM   5764 O O   . LEU A 1 720 ? -52.359 -8.466  -10.117 1.00 21.86  ? 720  LEU A O   1 
ATOM   5765 C CB  . LEU A 1 720 ? -52.602 -6.110  -11.664 1.00 22.72  ? 720  LEU A CB  1 
ATOM   5766 C CG  . LEU A 1 720 ? -52.858 -4.772  -12.350 1.00 25.21  ? 720  LEU A CG  1 
ATOM   5767 C CD1 . LEU A 1 720 ? -51.625 -3.910  -12.120 1.00 22.72  ? 720  LEU A CD1 1 
ATOM   5768 C CD2 . LEU A 1 720 ? -53.212 -4.943  -13.834 1.00 24.74  ? 720  LEU A CD2 1 
ATOM   5769 N N   . PRO A 1 721 ? -53.918 -9.544  -11.340 1.00 23.58  ? 721  PRO A N   1 
ATOM   5770 C CA  . PRO A 1 721 ? -53.583 -10.892 -10.822 1.00 24.28  ? 721  PRO A CA  1 
ATOM   5771 C C   . PRO A 1 721 ? -52.143 -11.276 -11.192 1.00 24.09  ? 721  PRO A C   1 
ATOM   5772 O O   . PRO A 1 721 ? -51.483 -10.521 -11.912 1.00 24.49  ? 721  PRO A O   1 
ATOM   5773 C CB  . PRO A 1 721 ? -54.610 -11.811 -11.479 1.00 24.76  ? 721  PRO A CB  1 
ATOM   5774 C CG  . PRO A 1 721 ? -55.256 -11.013 -12.553 1.00 25.04  ? 721  PRO A CG  1 
ATOM   5775 C CD  . PRO A 1 721 ? -55.023 -9.560  -12.309 1.00 23.85  ? 721  PRO A CD  1 
ATOM   5776 N N   . GLY A 1 722 ? -51.643 -12.394 -10.679 1.00 23.27  ? 722  GLY A N   1 
ATOM   5777 C CA  . GLY A 1 722 ? -50.204 -12.727 -10.828 1.00 22.89  ? 722  GLY A CA  1 
ATOM   5778 C C   . GLY A 1 722 ? -49.636 -12.777 -12.242 1.00 22.38  ? 722  GLY A C   1 
ATOM   5779 O O   . GLY A 1 722 ? -48.405 -12.732 -12.421 1.00 22.64  ? 722  GLY A O   1 
ATOM   5780 N N   . ASP A 1 723 ? -50.516 -12.899 -13.239 1.00 22.55  ? 723  ASP A N   1 
ATOM   5781 C CA  . ASP A 1 723 ? -50.129 -12.944 -14.646 1.00 23.38  ? 723  ASP A CA  1 
ATOM   5782 C C   . ASP A 1 723 ? -50.246 -11.591 -15.394 1.00 22.52  ? 723  ASP A C   1 
ATOM   5783 O O   . ASP A 1 723 ? -50.068 -11.552 -16.610 1.00 22.75  ? 723  ASP A O   1 
ATOM   5784 C CB  . ASP A 1 723 ? -50.883 -14.065 -15.406 1.00 24.42  ? 723  ASP A CB  1 
ATOM   5785 C CG  . ASP A 1 723 ? -52.418 -13.848 -15.473 1.00 28.12  ? 723  ASP A CG  1 
ATOM   5786 O OD1 . ASP A 1 723 ? -53.007 -13.131 -14.628 1.00 26.29  ? 723  ASP A OD1 1 
ATOM   5787 O OD2 . ASP A 1 723 ? -53.052 -14.436 -16.389 1.00 34.00  ? 723  ASP A OD2 1 
ATOM   5788 N N   . LYS A 1 724 ? -50.547 -10.496 -14.675 1.00 21.64  ? 724  LYS A N   1 
ATOM   5789 C CA  . LYS A 1 724 ? -50.814 -9.198  -15.323 1.00 20.18  ? 724  LYS A CA  1 
ATOM   5790 C C   . LYS A 1 724 ? -49.990 -8.047  -14.807 1.00 19.01  ? 724  LYS A C   1 
ATOM   5791 O O   . LYS A 1 724 ? -49.672 -7.989  -13.626 1.00 20.23  ? 724  LYS A O   1 
ATOM   5792 C CB  . LYS A 1 724 ? -52.295 -8.784  -15.177 1.00 21.56  ? 724  LYS A CB  1 
ATOM   5793 C CG  . LYS A 1 724 ? -53.296 -9.758  -15.792 1.00 22.61  ? 724  LYS A CG  1 
ATOM   5794 C CD  . LYS A 1 724 ? -53.011 -10.069 -17.241 1.00 26.70  ? 724  LYS A CD  1 
ATOM   5795 C CE  . LYS A 1 724 ? -54.085 -11.023 -17.850 1.00 27.50  ? 724  LYS A CE  1 
ATOM   5796 N NZ  . LYS A 1 724 ? -53.939 -11.084 -19.341 1.00 33.67  ? 724  LYS A NZ  1 
ATOM   5797 N N   . ILE A 1 725 ? -49.701 -7.120  -15.720 1.00 17.05  ? 725  ILE A N   1 
ATOM   5798 C CA  . ILE A 1 725 ? -49.265 -5.795  -15.379 1.00 17.50  ? 725  ILE A CA  1 
ATOM   5799 C C   . ILE A 1 725 ? -50.133 -4.845  -16.144 1.00 17.01  ? 725  ILE A C   1 
ATOM   5800 O O   . ILE A 1 725 ? -50.591 -5.172  -17.213 1.00 18.17  ? 725  ILE A O   1 
ATOM   5801 C CB  . ILE A 1 725 ? -47.769 -5.587  -15.789 1.00 16.13  ? 725  ILE A CB  1 
ATOM   5802 C CG1 . ILE A 1 725 ? -47.358 -4.139  -15.689 1.00 16.20  ? 725  ILE A CG1 1 
ATOM   5803 C CG2 . ILE A 1 725 ? -47.531 -6.046  -17.194 1.00 18.37  ? 725  ILE A CG2 1 
ATOM   5804 C CD1 . ILE A 1 725 ? -45.790 -3.998  -15.552 1.00 16.39  ? 725  ILE A CD1 1 
ATOM   5805 N N   . GLY A 1 726 ? -50.406 -3.681  -15.573 1.00 17.68  ? 726  GLY A N   1 
ATOM   5806 C CA  . GLY A 1 726 ? -51.239 -2.695  -16.258 1.00 16.81  ? 726  GLY A CA  1 
ATOM   5807 C C   . GLY A 1 726 ? -50.533 -2.068  -17.450 1.00 16.37  ? 726  GLY A C   1 
ATOM   5808 O O   . GLY A 1 726 ? -49.400 -1.580  -17.334 1.00 15.13  ? 726  GLY A O   1 
ATOM   5809 N N   . LEU A 1 727 ? -51.201 -2.081  -18.600 1.00 15.90  ? 727  LEU A N   1 
ATOM   5810 C CA  . LEU A 1 727 ? -50.690 -1.418  -19.796 1.00 16.44  ? 727  LEU A CA  1 
ATOM   5811 C C   . LEU A 1 727 ? -51.874 -0.763  -20.424 1.00 16.73  ? 727  LEU A C   1 
ATOM   5812 O O   . LEU A 1 727 ? -52.838 -1.483  -20.778 1.00 17.70  ? 727  LEU A O   1 
ATOM   5813 C CB  . LEU A 1 727 ? -50.156 -2.421  -20.818 1.00 15.63  ? 727  LEU A CB  1 
ATOM   5814 C CG  . LEU A 1 727 ? -48.956 -3.249  -20.418 1.00 18.02  ? 727  LEU A CG  1 
ATOM   5815 C CD1 . LEU A 1 727 ? -48.734 -4.319  -21.491 1.00 18.36  ? 727  LEU A CD1 1 
ATOM   5816 C CD2 . LEU A 1 727 ? -47.804 -2.274  -20.325 1.00 14.62  ? 727  LEU A CD2 1 
ATOM   5817 N N   . HIS A 1 728 ? -51.816 0.567   -20.597 1.00 16.12  ? 728  HIS A N   1 
ATOM   5818 C CA  . HIS A 1 728 ? -52.928 1.299   -21.216 1.00 16.33  ? 728  HIS A CA  1 
ATOM   5819 C C   . HIS A 1 728 ? -52.441 2.225   -22.273 1.00 16.59  ? 728  HIS A C   1 
ATOM   5820 O O   . HIS A 1 728 ? -51.396 2.855   -22.127 1.00 15.93  ? 728  HIS A O   1 
ATOM   5821 C CB  . HIS A 1 728 ? -53.670 2.078   -20.149 1.00 16.12  ? 728  HIS A CB  1 
ATOM   5822 C CG  . HIS A 1 728 ? -54.346 1.183   -19.179 1.00 17.52  ? 728  HIS A CG  1 
ATOM   5823 N ND1 . HIS A 1 728 ? -53.689 0.625   -18.103 1.00 14.04  ? 728  HIS A ND1 1 
ATOM   5824 C CD2 . HIS A 1 728 ? -55.585 0.625   -19.200 1.00 12.16  ? 728  HIS A CD2 1 
ATOM   5825 C CE1 . HIS A 1 728 ? -54.509 -0.187  -17.457 1.00 19.15  ? 728  HIS A CE1 1 
ATOM   5826 N NE2 . HIS A 1 728 ? -55.668 -0.198  -18.101 1.00 16.01  ? 728  HIS A NE2 1 
ATOM   5827 N N   . LEU A 1 729 ? -53.207 2.296   -23.351 1.00 15.88  ? 729  LEU A N   1 
ATOM   5828 C CA  . LEU A 1 729 ? -52.913 3.190   -24.454 1.00 15.35  ? 729  LEU A CA  1 
ATOM   5829 C C   . LEU A 1 729 ? -53.687 4.491   -24.345 1.00 16.15  ? 729  LEU A C   1 
ATOM   5830 O O   . LEU A 1 729 ? -54.930 4.490   -24.138 1.00 16.46  ? 729  LEU A O   1 
ATOM   5831 C CB  . LEU A 1 729 ? -53.171 2.507   -25.805 1.00 13.99  ? 729  LEU A CB  1 
ATOM   5832 C CG  . LEU A 1 729 ? -52.218 1.306   -26.077 1.00 13.17  ? 729  LEU A CG  1 
ATOM   5833 C CD1 . LEU A 1 729 ? -52.546 0.663   -27.388 1.00 15.64  ? 729  LEU A CD1 1 
ATOM   5834 C CD2 . LEU A 1 729 ? -50.752 1.748   -26.166 1.00 15.89  ? 729  LEU A CD2 1 
ATOM   5835 N N   . ARG A 1 730 ? -52.972 5.589   -24.551 1.00 15.27  ? 730  ARG A N   1 
ATOM   5836 C CA  . ARG A 1 730 ? -53.536 6.935   -24.501 1.00 15.90  ? 730  ARG A CA  1 
ATOM   5837 C C   . ARG A 1 730 ? -54.320 7.326   -25.731 1.00 15.45  ? 730  ARG A C   1 
ATOM   5838 O O   . ARG A 1 730 ? -53.820 7.307   -26.840 1.00 14.67  ? 730  ARG A O   1 
ATOM   5839 C CB  . ARG A 1 730 ? -52.440 7.957   -24.235 1.00 16.16  ? 730  ARG A CB  1 
ATOM   5840 C CG  . ARG A 1 730 ? -52.958 9.393   -23.946 1.00 15.65  ? 730  ARG A CG  1 
ATOM   5841 C CD  . ARG A 1 730 ? -51.725 10.198  -23.587 1.00 15.24  ? 730  ARG A CD  1 
ATOM   5842 N NE  . ARG A 1 730 ? -51.993 11.625  -23.489 1.00 15.16  ? 730  ARG A NE  1 
ATOM   5843 C CZ  . ARG A 1 730 ? -51.042 12.543  -23.373 1.00 16.48  ? 730  ARG A CZ  1 
ATOM   5844 N NH1 . ARG A 1 730 ? -49.750 12.184  -23.359 1.00 17.29  ? 730  ARG A NH1 1 
ATOM   5845 N NH2 . ARG A 1 730 ? -51.378 13.825  -23.288 1.00 18.76  ? 730  ARG A NH2 1 
ATOM   5846 N N   . GLY A 1 731 ? -55.578 7.724   -25.529 1.00 15.59  ? 731  GLY A N   1 
ATOM   5847 C CA  . GLY A 1 731 ? -56.341 8.285   -26.622 1.00 15.87  ? 731  GLY A CA  1 
ATOM   5848 C C   . GLY A 1 731 ? -55.649 9.491   -27.235 1.00 15.75  ? 731  GLY A C   1 
ATOM   5849 O O   . GLY A 1 731 ? -55.188 10.399  -26.527 1.00 16.59  ? 731  GLY A O   1 
ATOM   5850 N N   . GLY A 1 732 ? -55.568 9.495   -28.564 1.00 14.64  ? 732  GLY A N   1 
ATOM   5851 C CA  . GLY A 1 732 ? -55.025 10.626  -29.320 1.00 14.92  ? 732  GLY A CA  1 
ATOM   5852 C C   . GLY A 1 732 ? -53.693 10.245  -29.937 1.00 14.30  ? 732  GLY A C   1 
ATOM   5853 O O   . GLY A 1 732 ? -53.081 11.051  -30.634 1.00 14.44  ? 732  GLY A O   1 
ATOM   5854 N N   . TYR A 1 733 ? -53.324 8.986   -29.724 1.00 14.17  ? 733  TYR A N   1 
ATOM   5855 C CA  . TYR A 1 733 ? -52.038 8.464   -30.196 1.00 14.91  ? 733  TYR A CA  1 
ATOM   5856 C C   . TYR A 1 733 ? -52.159 7.226   -31.100 1.00 14.53  ? 733  TYR A C   1 
ATOM   5857 O O   . TYR A 1 733 ? -53.065 6.393   -30.951 1.00 13.97  ? 733  TYR A O   1 
ATOM   5858 C CB  . TYR A 1 733 ? -51.111 8.264   -28.982 1.00 14.37  ? 733  TYR A CB  1 
ATOM   5859 C CG  . TYR A 1 733 ? -50.773 9.576   -28.354 1.00 16.99  ? 733  TYR A CG  1 
ATOM   5860 C CD1 . TYR A 1 733 ? -49.635 10.306  -28.779 1.00 19.40  ? 733  TYR A CD1 1 
ATOM   5861 C CD2 . TYR A 1 733 ? -51.599 10.136  -27.377 1.00 16.92  ? 733  TYR A CD2 1 
ATOM   5862 C CE1 . TYR A 1 733 ? -49.350 11.543  -28.228 1.00 18.90  ? 733  TYR A CE1 1 
ATOM   5863 C CE2 . TYR A 1 733 ? -51.331 11.400  -26.843 1.00 20.45  ? 733  TYR A CE2 1 
ATOM   5864 C CZ  . TYR A 1 733 ? -50.195 12.081  -27.274 1.00 21.21  ? 733  TYR A CZ  1 
ATOM   5865 O OH  . TYR A 1 733 ? -49.920 13.312  -26.736 1.00 21.58  ? 733  TYR A OH  1 
ATOM   5866 N N   . ILE A 1 734 ? -51.240 7.135   -32.067 1.00 14.46  ? 734  ILE A N   1 
ATOM   5867 C CA  . ILE A 1 734 ? -51.184 6.024   -33.023 1.00 13.73  ? 734  ILE A CA  1 
ATOM   5868 C C   . ILE A 1 734 ? -49.857 5.351   -32.832 1.00 16.54  ? 734  ILE A C   1 
ATOM   5869 O O   . ILE A 1 734 ? -48.821 6.058   -32.853 1.00 15.25  ? 734  ILE A O   1 
ATOM   5870 C CB  . ILE A 1 734 ? -51.339 6.520   -34.450 1.00 13.77  ? 734  ILE A CB  1 
ATOM   5871 C CG1 . ILE A 1 734 ? -52.756 7.148   -34.577 1.00 14.69  ? 734  ILE A CG1 1 
ATOM   5872 C CG2 . ILE A 1 734 ? -51.192 5.325   -35.496 1.00 13.21  ? 734  ILE A CG2 1 
ATOM   5873 C CD1 . ILE A 1 734 ? -53.021 7.910   -35.834 1.00 13.01  ? 734  ILE A CD1 1 
ATOM   5874 N N   . PHE A 1 735 ? -49.915 4.042   -32.575 1.00 15.95  ? 735  PHE A N   1 
ATOM   5875 C CA  . PHE A 1 735 ? -48.740 3.242   -32.178 1.00 15.42  ? 735  PHE A CA  1 
ATOM   5876 C C   . PHE A 1 735 ? -48.409 2.281   -33.310 1.00 15.34  ? 735  PHE A C   1 
ATOM   5877 O O   . PHE A 1 735 ? -49.247 1.429   -33.685 1.00 15.88  ? 735  PHE A O   1 
ATOM   5878 C CB  . PHE A 1 735 ? -49.011 2.452   -30.899 1.00 14.78  ? 735  PHE A CB  1 
ATOM   5879 C CG  . PHE A 1 735 ? -49.468 3.305   -29.750 1.00 16.73  ? 735  PHE A CG  1 
ATOM   5880 C CD1 . PHE A 1 735 ? -48.573 3.752   -28.791 1.00 16.25  ? 735  PHE A CD1 1 
ATOM   5881 C CD2 . PHE A 1 735 ? -50.812 3.683   -29.646 1.00 12.41  ? 735  PHE A CD2 1 
ATOM   5882 C CE1 . PHE A 1 735 ? -48.997 4.579   -27.736 1.00 14.64  ? 735  PHE A CE1 1 
ATOM   5883 C CE2 . PHE A 1 735 ? -51.247 4.513   -28.602 1.00 10.52  ? 735  PHE A CE2 1 
ATOM   5884 C CZ  . PHE A 1 735 ? -50.376 4.944   -27.639 1.00 14.65  ? 735  PHE A CZ  1 
ATOM   5885 N N   . PRO A 1 736 ? -47.196 2.420   -33.868 1.00 15.23  ? 736  PRO A N   1 
ATOM   5886 C CA  . PRO A 1 736 ? -46.710 1.431   -34.828 1.00 15.09  ? 736  PRO A CA  1 
ATOM   5887 C C   . PRO A 1 736 ? -46.223 0.158   -34.130 1.00 16.03  ? 736  PRO A C   1 
ATOM   5888 O O   . PRO A 1 736 ? -45.497 0.203   -33.087 1.00 15.20  ? 736  PRO A O   1 
ATOM   5889 C CB  . PRO A 1 736 ? -45.556 2.155   -35.539 1.00 13.97  ? 736  PRO A CB  1 
ATOM   5890 C CG  . PRO A 1 736 ? -45.012 3.083   -34.480 1.00 15.45  ? 736  PRO A CG  1 
ATOM   5891 C CD  . PRO A 1 736 ? -46.213 3.500   -33.628 1.00 13.30  ? 736  PRO A CD  1 
ATOM   5892 N N   . THR A 1 737 ? -46.613 -0.981  -34.703 1.00 15.16  ? 737  THR A N   1 
ATOM   5893 C CA  . THR A 1 737 ? -46.297 -2.279  -34.129 1.00 15.66  ? 737  THR A CA  1 
ATOM   5894 C C   . THR A 1 737 ? -45.713 -3.174  -35.234 1.00 15.31  ? 737  THR A C   1 
ATOM   5895 O O   . THR A 1 737 ? -45.821 -2.876  -36.423 1.00 17.52  ? 737  THR A O   1 
ATOM   5896 C CB  . THR A 1 737 ? -47.556 -2.983  -33.561 1.00 17.61  ? 737  THR A CB  1 
ATOM   5897 O OG1 . THR A 1 737 ? -48.426 -3.290  -34.646 1.00 18.27  ? 737  THR A OG1 1 
ATOM   5898 C CG2 . THR A 1 737 ? -48.336 -2.092  -32.544 1.00 17.32  ? 737  THR A CG2 1 
ATOM   5899 N N   . GLN A 1 738 ? -45.071 -4.256  -34.839 1.00 15.42  ? 738  GLN A N   1 
ATOM   5900 C CA  . GLN A 1 738 ? -44.538 -5.246  -35.782 1.00 15.40  ? 738  GLN A CA  1 
ATOM   5901 C C   . GLN A 1 738 ? -44.641 -6.608  -35.116 1.00 15.60  ? 738  GLN A C   1 
ATOM   5902 O O   . GLN A 1 738 ? -44.239 -6.768  -33.956 1.00 16.15  ? 738  GLN A O   1 
ATOM   5903 C CB  . GLN A 1 738 ? -43.081 -4.909  -36.139 1.00 15.77  ? 738  GLN A CB  1 
ATOM   5904 C CG  . GLN A 1 738 ? -42.480 -5.851  -37.215 1.00 14.18  ? 738  GLN A CG  1 
ATOM   5905 C CD  . GLN A 1 738 ? -41.195 -5.267  -37.820 1.00 17.82  ? 738  GLN A CD  1 
ATOM   5906 O OE1 . GLN A 1 738 ? -40.394 -4.733  -37.092 1.00 15.76  ? 738  GLN A OE1 1 
ATOM   5907 N NE2 . GLN A 1 738 ? -41.016 -5.371  -39.131 1.00 17.98  ? 738  GLN A NE2 1 
ATOM   5908 N N   . GLN A 1 739 ? -45.187 -7.597  -35.837 1.00 15.22  ? 739  GLN A N   1 
ATOM   5909 C CA  . GLN A 1 739 ? -45.391 -8.913  -35.315 1.00 16.49  ? 739  GLN A CA  1 
ATOM   5910 C C   . GLN A 1 739 ? -44.070 -9.370  -34.694 1.00 17.20  ? 739  GLN A C   1 
ATOM   5911 O O   . GLN A 1 739 ? -43.018 -9.281  -35.352 1.00 18.16  ? 739  GLN A O   1 
ATOM   5912 C CB  . GLN A 1 739 ? -45.783 -9.884  -36.430 1.00 16.39  ? 739  GLN A CB  1 
ATOM   5913 C CG  . GLN A 1 739 ? -45.803 -11.323 -35.972 1.00 18.96  ? 739  GLN A CG  1 
ATOM   5914 C CD  . GLN A 1 739 ? -46.085 -12.279 -37.105 1.00 23.24  ? 739  GLN A CD  1 
ATOM   5915 O OE1 . GLN A 1 739 ? -46.249 -11.842 -38.244 1.00 25.93  ? 739  GLN A OE1 1 
ATOM   5916 N NE2 . GLN A 1 739 ? -46.193 -13.600 -36.791 1.00 20.78  ? 739  GLN A NE2 1 
ATOM   5917 N N   . PRO A 1 740 ? -44.138 -9.837  -33.445 1.00 17.37  ? 740  PRO A N   1 
ATOM   5918 C CA  . PRO A 1 740 ? -42.915 -10.182 -32.717 1.00 18.08  ? 740  PRO A CA  1 
ATOM   5919 C C   . PRO A 1 740 ? -42.314 -11.536 -33.178 1.00 20.19  ? 740  PRO A C   1 
ATOM   5920 O O   . PRO A 1 740 ? -42.972 -12.376 -33.793 1.00 18.94  ? 740  PRO A O   1 
ATOM   5921 C CB  . PRO A 1 740 ? -43.378 -10.252 -31.264 1.00 17.08  ? 740  PRO A CB  1 
ATOM   5922 C CG  . PRO A 1 740 ? -44.850 -10.656 -31.359 1.00 18.02  ? 740  PRO A CG  1 
ATOM   5923 C CD  . PRO A 1 740 ? -45.360 -9.992  -32.622 1.00 15.57  ? 740  PRO A CD  1 
ATOM   5924 N N   . ASN A 1 741 ? -41.036 -11.715 -32.903 1.00 21.26  ? 741  ASN A N   1 
ATOM   5925 C CA  A ASN A 1 741 ? -40.367 -12.985 -33.131 0.50 21.10  ? 741  ASN A CA  1 
ATOM   5926 C CA  B ASN A 1 741 ? -40.386 -13.000 -33.098 0.50 21.46  ? 741  ASN A CA  1 
ATOM   5927 C C   . ASN A 1 741 ? -39.404 -13.046 -31.944 1.00 21.28  ? 741  ASN A C   1 
ATOM   5928 O O   . ASN A 1 741 ? -39.301 -12.069 -31.171 1.00 21.38  ? 741  ASN A O   1 
ATOM   5929 C CB  A ASN A 1 741 ? -39.659 -13.002 -34.506 0.50 20.70  ? 741  ASN A CB  1 
ATOM   5930 C CB  B ASN A 1 741 ? -39.687 -13.057 -34.459 0.50 21.43  ? 741  ASN A CB  1 
ATOM   5931 C CG  A ASN A 1 741 ? -39.438 -14.439 -35.075 0.50 21.58  ? 741  ASN A CG  1 
ATOM   5932 C CG  B ASN A 1 741 ? -39.327 -14.499 -34.919 0.50 23.62  ? 741  ASN A CG  1 
ATOM   5933 O OD1 A ASN A 1 741 ? -39.256 -15.385 -34.321 0.50 20.54  ? 741  ASN A OD1 1 
ATOM   5934 O OD1 B ASN A 1 741 ? -38.716 -14.661 -35.971 0.50 27.12  ? 741  ASN A OD1 1 
ATOM   5935 N ND2 A ASN A 1 741 ? -39.406 -14.566 -36.426 0.50 24.34  ? 741  ASN A ND2 1 
ATOM   5936 N ND2 B ASN A 1 741 ? -39.678 -15.518 -34.144 0.50 25.63  ? 741  ASN A ND2 1 
ATOM   5937 N N   . THR A 1 742 ? -38.717 -14.154 -31.772 1.00 20.64  ? 742  THR A N   1 
ATOM   5938 C CA  . THR A 1 742 ? -37.830 -14.275 -30.608 1.00 19.62  ? 742  THR A CA  1 
ATOM   5939 C C   . THR A 1 742 ? -36.520 -13.492 -30.697 1.00 19.20  ? 742  THR A C   1 
ATOM   5940 O O   . THR A 1 742 ? -35.781 -13.457 -29.706 1.00 18.37  ? 742  THR A O   1 
ATOM   5941 C CB  . THR A 1 742 ? -37.500 -15.740 -30.342 1.00 20.21  ? 742  THR A CB  1 
ATOM   5942 O OG1 . THR A 1 742 ? -36.855 -16.248 -31.504 1.00 19.83  ? 742  THR A OG1 1 
ATOM   5943 C CG2 . THR A 1 742 ? -38.794 -16.539 -30.047 1.00 18.97  ? 742  THR A CG2 1 
ATOM   5944 N N   . THR A 1 743 ? -36.227 -12.898 -31.852 1.00 18.37  ? 743  THR A N   1 
ATOM   5945 C CA  . THR A 1 743 ? -35.108 -11.978 -31.998 1.00 18.84  ? 743  THR A CA  1 
ATOM   5946 C C   . THR A 1 743 ? -35.531 -10.817 -32.869 1.00 18.83  ? 743  THR A C   1 
ATOM   5947 O O   . THR A 1 743 ? -36.451 -10.944 -33.681 1.00 19.31  ? 743  THR A O   1 
ATOM   5948 C CB  . THR A 1 743 ? -33.856 -12.638 -32.662 1.00 17.50  ? 743  THR A CB  1 
ATOM   5949 O OG1 . THR A 1 743 ? -34.125 -12.862 -34.043 1.00 18.31  ? 743  THR A OG1 1 
ATOM   5950 C CG2 . THR A 1 743 ? -33.506 -13.980 -32.009 1.00 17.09  ? 743  THR A CG2 1 
ATOM   5951 N N   . THR A 1 744 ? -34.858 -9.682  -32.721 1.00 19.16  ? 744  THR A N   1 
ATOM   5952 C CA  . THR A 1 744 ? -35.165 -8.530  -33.572 1.00 20.75  ? 744  THR A CA  1 
ATOM   5953 C C   . THR A 1 744 ? -34.628 -8.711  -35.003 1.00 21.18  ? 744  THR A C   1 
ATOM   5954 O O   . THR A 1 744 ? -35.176 -8.147  -35.937 1.00 20.94  ? 744  THR A O   1 
ATOM   5955 C CB  . THR A 1 744 ? -34.637 -7.209  -33.002 1.00 20.94  ? 744  THR A CB  1 
ATOM   5956 O OG1 . THR A 1 744 ? -33.202 -7.262  -32.926 1.00 21.03  ? 744  THR A OG1 1 
ATOM   5957 C CG2 . THR A 1 744 ? -35.232 -6.906  -31.617 1.00 20.33  ? 744  THR A CG2 1 
ATOM   5958 N N   . LEU A 1 745 ? -33.556 -9.485  -35.187 1.00 21.18  ? 745  LEU A N   1 
ATOM   5959 C CA  . LEU A 1 745 ? -33.097 -9.790  -36.551 1.00 21.84  ? 745  LEU A CA  1 
ATOM   5960 C C   . LEU A 1 745 ? -34.292 -10.275 -37.370 1.00 21.60  ? 745  LEU A C   1 
ATOM   5961 O O   . LEU A 1 745 ? -34.547 -9.787  -38.468 1.00 21.62  ? 745  LEU A O   1 
ATOM   5962 C CB  . LEU A 1 745 ? -32.030 -10.901 -36.558 1.00 22.37  ? 745  LEU A CB  1 
ATOM   5963 C CG  . LEU A 1 745 ? -31.429 -11.204 -37.938 1.00 24.90  ? 745  LEU A CG  1 
ATOM   5964 C CD1 . LEU A 1 745 ? -30.638 -10.030 -38.409 1.00 26.22  ? 745  LEU A CD1 1 
ATOM   5965 C CD2 . LEU A 1 745 ? -30.503 -12.417 -37.933 1.00 24.53  ? 745  LEU A CD2 1 
ATOM   5966 N N   . ALA A 1 746 ? -35.019 -11.224 -36.798 1.00 20.27  ? 746  ALA A N   1 
ATOM   5967 C CA  . ALA A 1 746 ? -36.209 -11.785 -37.411 1.00 20.69  ? 746  ALA A CA  1 
ATOM   5968 C C   . ALA A 1 746 ? -37.455 -10.900 -37.317 1.00 20.45  ? 746  ALA A C   1 
ATOM   5969 O O   . ALA A 1 746 ? -38.167 -10.765 -38.315 1.00 20.83  ? 746  ALA A O   1 
ATOM   5970 C CB  . ALA A 1 746 ? -36.477 -13.152 -36.857 1.00 20.47  ? 746  ALA A CB  1 
ATOM   5971 N N   . SER A 1 747 ? -37.727 -10.264 -36.175 1.00 18.96  ? 747  SER A N   1 
ATOM   5972 C CA  . SER A 1 747 ? -39.018 -9.523  -36.036 1.00 18.85  ? 747  SER A CA  1 
ATOM   5973 C C   . SER A 1 747 ? -39.079 -8.341  -37.026 1.00 18.60  ? 747  SER A C   1 
ATOM   5974 O O   . SER A 1 747 ? -40.143 -8.008  -37.514 1.00 18.16  ? 747  SER A O   1 
ATOM   5975 C CB  . SER A 1 747 ? -39.215 -9.046  -34.590 1.00 18.51  ? 747  SER A CB  1 
ATOM   5976 O OG  . SER A 1 747 ? -38.250 -8.061  -34.282 1.00 18.46  ? 747  SER A OG  1 
ATOM   5977 N N   . ARG A 1 748 ? -37.919 -7.758  -37.349 1.00 16.88  ? 748  ARG A N   1 
ATOM   5978 C CA  . ARG A 1 748 ? -37.834 -6.625  -38.270 1.00 18.33  ? 748  ARG A CA  1 
ATOM   5979 C C   . ARG A 1 748 ? -38.265 -6.954  -39.703 1.00 17.72  ? 748  ARG A C   1 
ATOM   5980 O O   . ARG A 1 748 ? -38.449 -6.046  -40.498 1.00 18.87  ? 748  ARG A O   1 
ATOM   5981 C CB  . ARG A 1 748 ? -36.397 -6.064  -38.304 1.00 17.49  ? 748  ARG A CB  1 
ATOM   5982 C CG  . ARG A 1 748 ? -35.993 -5.292  -37.036 1.00 17.43  ? 748  ARG A CG  1 
ATOM   5983 C CD  . ARG A 1 748 ? -34.496 -4.849  -37.121 1.00 18.14  ? 748  ARG A CD  1 
ATOM   5984 N NE  . ARG A 1 748 ? -34.238 -4.144  -38.380 1.00 16.63  ? 748  ARG A NE  1 
ATOM   5985 C CZ  . ARG A 1 748 ? -34.434 -2.837  -38.562 1.00 18.22  ? 748  ARG A CZ  1 
ATOM   5986 N NH1 . ARG A 1 748 ? -34.812 -2.048  -37.544 1.00 19.81  ? 748  ARG A NH1 1 
ATOM   5987 N NH2 . ARG A 1 748 ? -34.207 -2.298  -39.750 1.00 17.63  ? 748  ARG A NH2 1 
ATOM   5988 N N   . LYS A 1 749 ? -38.365 -8.234  -40.038 1.00 18.87  ? 749  LYS A N   1 
ATOM   5989 C CA  . LYS A 1 749 ? -38.849 -8.690  -41.361 1.00 20.19  ? 749  LYS A CA  1 
ATOM   5990 C C   . LYS A 1 749 ? -40.368 -8.954  -41.348 1.00 19.62  ? 749  LYS A C   1 
ATOM   5991 O O   . LYS A 1 749 ? -40.966 -9.302  -42.368 1.00 19.74  ? 749  LYS A O   1 
ATOM   5992 C CB  . LYS A 1 749 ? -38.111 -9.978  -41.754 1.00 21.33  ? 749  LYS A CB  1 
ATOM   5993 C CG  . LYS A 1 749 ? -36.571 -9.820  -41.728 1.00 22.63  ? 749  LYS A CG  1 
ATOM   5994 C CD  . LYS A 1 749 ? -35.835 -11.154 -41.960 1.00 23.61  ? 749  LYS A CD  1 
ATOM   5995 C CE  . LYS A 1 749 ? -34.316 -11.000 -41.804 1.00 26.03  ? 749  LYS A CE  1 
ATOM   5996 N NZ  . LYS A 1 749 ? -33.505 -12.263 -42.107 1.00 26.88  ? 749  LYS A NZ  1 
ATOM   5997 N N   . ASN A 1 750 ? -41.000 -8.770  -40.206 1.00 18.82  ? 750  ASN A N   1 
ATOM   5998 C CA  . ASN A 1 750 ? -42.436 -9.134  -40.073 1.00 18.56  ? 750  ASN A CA  1 
ATOM   5999 C C   . ASN A 1 750 ? -43.421 -8.020  -40.494 1.00 17.92  ? 750  ASN A C   1 
ATOM   6000 O O   . ASN A 1 750 ? -43.050 -6.858  -40.585 1.00 17.49  ? 750  ASN A O   1 
ATOM   6001 C CB  . ASN A 1 750 ? -42.761 -9.587  -38.670 1.00 18.12  ? 750  ASN A CB  1 
ATOM   6002 C CG  . ASN A 1 750 ? -42.293 -10.995 -38.385 1.00 21.46  ? 750  ASN A CG  1 
ATOM   6003 O OD1 . ASN A 1 750 ? -42.059 -11.786 -39.308 1.00 25.41  ? 750  ASN A OD1 1 
ATOM   6004 N ND2 . ASN A 1 750 ? -42.159 -11.329 -37.103 1.00 19.25  ? 750  ASN A ND2 1 
ATOM   6005 N N   . PRO A 1 751 ? -44.683 -8.391  -40.761 1.00 18.50  ? 751  PRO A N   1 
ATOM   6006 C CA  . PRO A 1 751 ? -45.744 -7.430  -41.036 1.00 18.43  ? 751  PRO A CA  1 
ATOM   6007 C C   . PRO A 1 751 ? -45.891 -6.391  -39.913 1.00 17.27  ? 751  PRO A C   1 
ATOM   6008 O O   . PRO A 1 751 ? -45.760 -6.735  -38.750 1.00 18.04  ? 751  PRO A O   1 
ATOM   6009 C CB  . PRO A 1 751 ? -46.979 -8.316  -41.071 1.00 19.59  ? 751  PRO A CB  1 
ATOM   6010 C CG  . PRO A 1 751 ? -46.452 -9.614  -41.591 1.00 20.68  ? 751  PRO A CG  1 
ATOM   6011 C CD  . PRO A 1 751 ? -45.171 -9.779  -40.882 1.00 18.93  ? 751  PRO A CD  1 
ATOM   6012 N N   . LEU A 1 752 ? -46.174 -5.144  -40.280 1.00 16.81  ? 752  LEU A N   1 
ATOM   6013 C CA  . LEU A 1 752 ? -46.378 -4.088  -39.296 1.00 17.15  ? 752  LEU A CA  1 
ATOM   6014 C C   . LEU A 1 752 ? -47.867 -3.886  -39.059 1.00 18.37  ? 752  LEU A C   1 
ATOM   6015 O O   . LEU A 1 752 ? -48.660 -4.361  -39.812 1.00 17.35  ? 752  LEU A O   1 
ATOM   6016 C CB  . LEU A 1 752 ? -45.795 -2.777  -39.805 1.00 19.69  ? 752  LEU A CB  1 
ATOM   6017 C CG  . LEU A 1 752 ? -44.454 -2.896  -40.539 1.00 20.34  ? 752  LEU A CG  1 
ATOM   6018 C CD1 . LEU A 1 752 ? -44.201 -1.644  -41.356 1.00 25.48  ? 752  LEU A CD1 1 
ATOM   6019 C CD2 . LEU A 1 752 ? -43.396 -3.066  -39.518 1.00 22.65  ? 752  LEU A CD2 1 
ATOM   6020 N N   . GLY A 1 753 ? -48.199 -3.128  -38.025 1.00 18.09  ? 753  GLY A N   1 
ATOM   6021 C CA  . GLY A 1 753 ? -49.582 -2.812  -37.704 1.00 18.44  ? 753  GLY A CA  1 
ATOM   6022 C C   . GLY A 1 753 ? -49.614 -1.399  -37.174 1.00 18.45  ? 753  GLY A C   1 
ATOM   6023 O O   . GLY A 1 753 ? -48.575 -0.804  -36.889 1.00 16.27  ? 753  GLY A O   1 
ATOM   6024 N N   . LEU A 1 754 ? -50.812 -0.845  -37.078 1.00 17.90  ? 754  LEU A N   1 
ATOM   6025 C CA  . LEU A 1 754 ? -51.015 0.395   -36.409 1.00 18.11  ? 754  LEU A CA  1 
ATOM   6026 C C   . LEU A 1 754 ? -52.077 0.173   -35.343 1.00 17.89  ? 754  LEU A C   1 
ATOM   6027 O O   . LEU A 1 754 ? -53.087 -0.514  -35.605 1.00 18.97  ? 754  LEU A O   1 
ATOM   6028 C CB  . LEU A 1 754 ? -51.469 1.480   -37.399 1.00 17.02  ? 754  LEU A CB  1 
ATOM   6029 C CG  . LEU A 1 754 ? -50.509 2.008   -38.438 1.00 20.63  ? 754  LEU A CG  1 
ATOM   6030 C CD1 . LEU A 1 754 ? -51.307 3.019   -39.289 1.00 21.73  ? 754  LEU A CD1 1 
ATOM   6031 C CD2 . LEU A 1 754 ? -49.245 2.672   -37.727 1.00 15.61  ? 754  LEU A CD2 1 
ATOM   6032 N N   . ILE A 1 755 ? -51.863 0.737   -34.156 1.00 17.51  ? 755  ILE A N   1 
ATOM   6033 C CA  . ILE A 1 755 ? -52.958 0.851   -33.158 1.00 18.01  ? 755  ILE A CA  1 
ATOM   6034 C C   . ILE A 1 755 ? -53.342 2.336   -33.070 1.00 18.39  ? 755  ILE A C   1 
ATOM   6035 O O   . ILE A 1 755 ? -52.515 3.193   -32.732 1.00 17.55  ? 755  ILE A O   1 
ATOM   6036 C CB  . ILE A 1 755 ? -52.559 0.308   -31.747 1.00 18.35  ? 755  ILE A CB  1 
ATOM   6037 C CG1 . ILE A 1 755 ? -51.994 -1.111  -31.817 1.00 18.89  ? 755  ILE A CG1 1 
ATOM   6038 C CG2 . ILE A 1 755 ? -53.748 0.354   -30.768 1.00 15.98  ? 755  ILE A CG2 1 
ATOM   6039 C CD1 . ILE A 1 755 ? -51.503 -1.638  -30.428 1.00 20.34  ? 755  ILE A CD1 1 
ATOM   6040 N N   . ILE A 1 756 ? -54.582 2.641   -33.422 1.00 18.31  ? 756  ILE A N   1 
ATOM   6041 C CA  . ILE A 1 756 ? -55.081 3.996   -33.386 1.00 17.89  ? 756  ILE A CA  1 
ATOM   6042 C C   . ILE A 1 756 ? -55.967 4.093   -32.137 1.00 19.94  ? 756  ILE A C   1 
ATOM   6043 O O   . ILE A 1 756 ? -57.057 3.527   -32.111 1.00 19.44  ? 756  ILE A O   1 
ATOM   6044 C CB  . ILE A 1 756 ? -55.905 4.255   -34.675 1.00 18.48  ? 756  ILE A CB  1 
ATOM   6045 C CG1 . ILE A 1 756 ? -54.945 4.201   -35.883 1.00 16.50  ? 756  ILE A CG1 1 
ATOM   6046 C CG2 . ILE A 1 756 ? -56.631 5.610   -34.599 1.00 16.18  ? 756  ILE A CG2 1 
ATOM   6047 C CD1 . ILE A 1 756 ? -55.584 4.093   -37.243 1.00 15.95  ? 756  ILE A CD1 1 
ATOM   6048 N N   . ALA A 1 757 ? -55.517 4.805   -31.106 1.00 19.84  ? 757  ALA A N   1 
ATOM   6049 C CA  . ALA A 1 757 ? -56.307 4.975   -29.887 1.00 19.27  ? 757  ALA A CA  1 
ATOM   6050 C C   . ALA A 1 757 ? -57.000 6.328   -30.044 1.00 19.35  ? 757  ALA A C   1 
ATOM   6051 O O   . ALA A 1 757 ? -56.363 7.357   -29.967 1.00 18.94  ? 757  ALA A O   1 
ATOM   6052 C CB  . ALA A 1 757 ? -55.374 4.987   -28.662 1.00 19.36  ? 757  ALA A CB  1 
ATOM   6053 N N   . LEU A 1 758 ? -58.304 6.336   -30.313 1.00 19.33  ? 758  LEU A N   1 
ATOM   6054 C CA  . LEU A 1 758 ? -58.988 7.594   -30.577 1.00 18.99  ? 758  LEU A CA  1 
ATOM   6055 C C   . LEU A 1 758 ? -59.196 8.462   -29.308 1.00 18.56  ? 758  LEU A C   1 
ATOM   6056 O O   . LEU A 1 758 ? -59.509 7.937   -28.245 1.00 17.90  ? 758  LEU A O   1 
ATOM   6057 C CB  . LEU A 1 758 ? -60.327 7.304   -31.285 1.00 19.28  ? 758  LEU A CB  1 
ATOM   6058 C CG  . LEU A 1 758 ? -60.243 6.707   -32.680 1.00 19.50  ? 758  LEU A CG  1 
ATOM   6059 C CD1 . LEU A 1 758 ? -61.655 6.543   -33.194 1.00 20.75  ? 758  LEU A CD1 1 
ATOM   6060 C CD2 . LEU A 1 758 ? -59.424 7.588   -33.600 1.00 21.95  ? 758  LEU A CD2 1 
ATOM   6061 N N   . ASP A 1 759 ? -59.011 9.786   -29.419 1.00 19.87  ? 759  ASP A N   1 
ATOM   6062 C CA  . ASP A 1 759 ? -59.299 10.684  -28.289 1.00 21.13  ? 759  ASP A CA  1 
ATOM   6063 C C   . ASP A 1 759 ? -60.807 11.022  -28.309 1.00 22.79  ? 759  ASP A C   1 
ATOM   6064 O O   . ASP A 1 759 ? -61.523 10.441  -29.120 1.00 21.30  ? 759  ASP A O   1 
ATOM   6065 C CB  . ASP A 1 759 ? -58.432 11.945  -28.295 1.00 22.09  ? 759  ASP A CB  1 
ATOM   6066 C CG  . ASP A 1 759 ? -58.708 12.887  -29.461 1.00 24.42  ? 759  ASP A CG  1 
ATOM   6067 O OD1 . ASP A 1 759 ? -59.784 12.822  -30.113 1.00 27.57  ? 759  ASP A OD1 1 
ATOM   6068 O OD2 . ASP A 1 759 ? -57.804 13.723  -29.736 1.00 27.64  ? 759  ASP A OD2 1 
ATOM   6069 N N   . GLU A 1 760 ? -61.245 11.943  -27.446 1.00 24.37  ? 760  GLU A N   1 
ATOM   6070 C CA  . GLU A 1 760 ? -62.682 12.290  -27.297 1.00 27.56  ? 760  GLU A CA  1 
ATOM   6071 C C   . GLU A 1 760 ? -63.233 12.902  -28.573 1.00 27.93  ? 760  GLU A C   1 
ATOM   6072 O O   . GLU A 1 760 ? -64.450 12.872  -28.836 1.00 29.98  ? 760  GLU A O   1 
ATOM   6073 C CB  . GLU A 1 760 ? -62.871 13.296  -26.140 1.00 29.12  ? 760  GLU A CB  1 
ATOM   6074 C CG  . GLU A 1 760 ? -62.048 12.988  -24.873 1.00 34.70  ? 760  GLU A CG  1 
ATOM   6075 C CD  . GLU A 1 760 ? -60.707 13.747  -24.793 1.00 41.42  ? 760  GLU A CD  1 
ATOM   6076 O OE1 . GLU A 1 760 ? -60.700 14.851  -24.181 1.00 45.77  ? 760  GLU A OE1 1 
ATOM   6077 O OE2 . GLU A 1 760 ? -59.668 13.253  -25.311 1.00 40.00  ? 760  GLU A OE2 1 
ATOM   6078 N N   . ASN A 1 761 ? -62.352 13.494  -29.371 1.00 27.25  ? 761  ASN A N   1 
ATOM   6079 C CA  . ASN A 1 761 ? -62.751 14.027  -30.666 1.00 27.29  ? 761  ASN A CA  1 
ATOM   6080 C C   . ASN A 1 761 ? -62.586 13.057  -31.818 1.00 25.32  ? 761  ASN A C   1 
ATOM   6081 O O   . ASN A 1 761 ? -62.764 13.433  -32.964 1.00 25.43  ? 761  ASN A O   1 
ATOM   6082 C CB  . ASN A 1 761 ? -62.024 15.340  -30.916 1.00 28.04  ? 761  ASN A CB  1 
ATOM   6083 C CG  . ASN A 1 761 ? -62.256 16.327  -29.779 1.00 31.68  ? 761  ASN A CG  1 
ATOM   6084 O OD1 . ASN A 1 761 ? -63.405 16.522  -29.329 1.00 34.90  ? 761  ASN A OD1 1 
ATOM   6085 N ND2 . ASN A 1 761 ? -61.189 16.910  -29.278 1.00 30.22  ? 761  ASN A ND2 1 
ATOM   6086 N N   . LYS A 1 762 ? -62.293 11.799  -31.483 1.00 23.76  ? 762  LYS A N   1 
ATOM   6087 C CA  A LYS A 1 762 ? -62.087 10.710  -32.442 0.50 23.30  ? 762  LYS A CA  1 
ATOM   6088 C CA  B LYS A 1 762 ? -62.149 10.744  -32.501 0.50 23.27  ? 762  LYS A CA  1 
ATOM   6089 C C   . LYS A 1 762 ? -60.980 11.065  -33.434 1.00 22.43  ? 762  LYS A C   1 
ATOM   6090 O O   . LYS A 1 762 ? -61.061 10.851  -34.646 1.00 22.72  ? 762  LYS A O   1 
ATOM   6091 C CB  A LYS A 1 762 ? -63.422 10.211  -33.058 0.50 23.42  ? 762  LYS A CB  1 
ATOM   6092 C CB  B LYS A 1 762 ? -63.478 10.500  -33.291 0.50 23.17  ? 762  LYS A CB  1 
ATOM   6093 C CG  A LYS A 1 762 ? -64.432 9.725   -31.967 0.50 24.46  ? 762  LYS A CG  1 
ATOM   6094 C CG  B LYS A 1 762 ? -64.740 10.275  -32.410 0.50 24.43  ? 762  LYS A CG  1 
ATOM   6095 C CD  A LYS A 1 762 ? -63.773 8.800   -30.911 0.50 23.52  ? 762  LYS A CD  1 
ATOM   6096 C CD  B LYS A 1 762 ? -64.420 9.352   -31.217 0.50 23.98  ? 762  LYS A CD  1 
ATOM   6097 C CE  A LYS A 1 762 ? -64.630 8.573   -29.658 0.50 23.48  ? 762  LYS A CE  1 
ATOM   6098 C CE  B LYS A 1 762 ? -65.659 8.706   -30.608 0.50 24.28  ? 762  LYS A CE  1 
ATOM   6099 N NZ  A LYS A 1 762 ? -63.896 7.791   -28.619 0.50 24.89  ? 762  LYS A NZ  1 
ATOM   6100 N NZ  B LYS A 1 762 ? -66.128 9.391   -29.397 0.50 22.78  ? 762  LYS A NZ  1 
ATOM   6101 N N   . GLU A 1 763 ? -59.910 11.605  -32.855 1.00 21.36  ? 763  GLU A N   1 
ATOM   6102 C CA  . GLU A 1 763 ? -58.696 11.970  -33.595 1.00 21.27  ? 763  GLU A CA  1 
ATOM   6103 C C   . GLU A 1 763 ? -57.488 11.328  -32.940 1.00 18.42  ? 763  GLU A C   1 
ATOM   6104 O O   . GLU A 1 763 ? -57.548 10.913  -31.802 1.00 16.71  ? 763  GLU A O   1 
ATOM   6105 C CB  . GLU A 1 763 ? -58.500 13.488  -33.646 1.00 21.25  ? 763  GLU A CB  1 
ATOM   6106 C CG  . GLU A 1 763 ? -59.693 14.236  -34.275 1.00 25.98  ? 763  GLU A CG  1 
ATOM   6107 C CD  . GLU A 1 763 ? -59.433 15.702  -34.485 1.00 27.75  ? 763  GLU A CD  1 
ATOM   6108 O OE1 . GLU A 1 763 ? -58.651 16.308  -33.698 1.00 36.10  ? 763  GLU A OE1 1 
ATOM   6109 O OE2 . GLU A 1 763 ? -60.026 16.254  -35.443 1.00 35.61  ? 763  GLU A OE2 1 
ATOM   6110 N N   . ALA A 1 764 ? -56.373 11.256  -33.675 1.00 17.72  ? 764  ALA A N   1 
ATOM   6111 C CA  . ALA A 1 764 ? -55.180 10.632  -33.107 1.00 16.11  ? 764  ALA A CA  1 
ATOM   6112 C C   . ALA A 1 764 ? -54.032 10.937  -34.016 1.00 15.44  ? 764  ALA A C   1 
ATOM   6113 O O   . ALA A 1 764 ? -54.241 11.237  -35.177 1.00 15.78  ? 764  ALA A O   1 
ATOM   6114 C CB  . ALA A 1 764 ? -55.346 9.101   -33.006 1.00 16.21  ? 764  ALA A CB  1 
ATOM   6115 N N   . LYS A 1 765 ? -52.815 10.891  -33.490 1.00 14.75  ? 765  LYS A N   1 
ATOM   6116 C CA  . LYS A 1 765 ? -51.658 11.252  -34.339 1.00 16.07  ? 765  LYS A CA  1 
ATOM   6117 C C   . LYS A 1 765 ? -50.546 10.329  -33.918 1.00 14.67  ? 765  LYS A C   1 
ATOM   6118 O O   . LYS A 1 765 ? -50.542 9.877   -32.799 1.00 14.43  ? 765  LYS A O   1 
ATOM   6119 C CB  . LYS A 1 765 ? -51.203 12.706  -34.102 1.00 18.99  ? 765  LYS A CB  1 
ATOM   6120 C CG  . LYS A 1 765 ? -52.186 13.794  -34.578 1.00 25.86  ? 765  LYS A CG  1 
ATOM   6121 C CD  . LYS A 1 765 ? -51.417 14.994  -35.146 1.00 35.70  ? 765  LYS A CD  1 
ATOM   6122 C CE  . LYS A 1 765 ? -52.357 16.193  -35.376 1.00 39.96  ? 765  LYS A CE  1 
ATOM   6123 N NZ  . LYS A 1 765 ? -53.401 15.925  -36.425 1.00 42.78  ? 765  LYS A NZ  1 
ATOM   6124 N N   . GLY A 1 766 ? -49.614 10.014  -34.821 1.00 14.32  ? 766  GLY A N   1 
ATOM   6125 C CA  . GLY A 1 766 ? -48.483 9.221   -34.390 1.00 14.09  ? 766  GLY A CA  1 
ATOM   6126 C C   . GLY A 1 766 ? -47.391 9.375   -35.452 1.00 13.66  ? 766  GLY A C   1 
ATOM   6127 O O   . GLY A 1 766 ? -47.546 10.100  -36.446 1.00 13.27  ? 766  GLY A O   1 
ATOM   6128 N N   . GLU A 1 767 ? -46.289 8.686   -35.250 1.00 15.44  ? 767  GLU A N   1 
ATOM   6129 C CA  . GLU A 1 767 ? -45.239 8.673   -36.252 1.00 15.75  ? 767  GLU A CA  1 
ATOM   6130 C C   . GLU A 1 767 ? -44.458 7.365   -36.175 1.00 15.70  ? 767  GLU A C   1 
ATOM   6131 O O   . GLU A 1 767 ? -44.605 6.575   -35.215 1.00 13.74  ? 767  GLU A O   1 
ATOM   6132 C CB  . GLU A 1 767 ? -44.346 9.881   -36.054 1.00 17.52  ? 767  GLU A CB  1 
ATOM   6133 C CG  . GLU A 1 767 ? -43.519 9.815   -34.763 1.00 20.42  ? 767  GLU A CG  1 
ATOM   6134 C CD  . GLU A 1 767 ? -42.845 11.122  -34.391 1.00 26.69  ? 767  GLU A CD  1 
ATOM   6135 O OE1 . GLU A 1 767 ? -42.856 12.089  -35.195 1.00 30.93  ? 767  GLU A OE1 1 
ATOM   6136 O OE2 . GLU A 1 767 ? -42.255 11.171  -33.296 1.00 30.73  ? 767  GLU A OE2 1 
ATOM   6137 N N   . LEU A 1 768 ? -43.614 7.138   -37.183 1.00 16.34  ? 768  LEU A N   1 
ATOM   6138 C CA  . LEU A 1 768 ? -42.767 5.965   -37.232 1.00 15.90  ? 768  LEU A CA  1 
ATOM   6139 C C   . LEU A 1 768 ? -41.455 6.340   -37.899 1.00 15.95  ? 768  LEU A C   1 
ATOM   6140 O O   . LEU A 1 768 ? -41.439 6.861   -39.003 1.00 16.53  ? 768  LEU A O   1 
ATOM   6141 C CB  . LEU A 1 768 ? -43.426 4.799   -38.002 1.00 17.18  ? 768  LEU A CB  1 
ATOM   6142 C CG  . LEU A 1 768 ? -42.504 3.590   -38.281 1.00 15.66  ? 768  LEU A CG  1 
ATOM   6143 C CD1 . LEU A 1 768 ? -41.989 2.940   -36.954 1.00 15.70  ? 768  LEU A CD1 1 
ATOM   6144 C CD2 . LEU A 1 768 ? -43.264 2.549   -39.090 1.00 17.24  ? 768  LEU A CD2 1 
ATOM   6145 N N   . PHE A 1 769 ? -40.369 6.120   -37.184 1.00 14.72  ? 769  PHE A N   1 
ATOM   6146 C CA  . PHE A 1 769 ? -39.006 6.233   -37.750 1.00 14.33  ? 769  PHE A CA  1 
ATOM   6147 C C   . PHE A 1 769 ? -38.531 4.837   -38.169 1.00 14.59  ? 769  PHE A C   1 
ATOM   6148 O O   . PHE A 1 769 ? -38.747 3.850   -37.442 1.00 14.99  ? 769  PHE A O   1 
ATOM   6149 C CB  . PHE A 1 769 ? -38.103 6.778   -36.646 1.00 14.59  ? 769  PHE A CB  1 
ATOM   6150 C CG  . PHE A 1 769 ? -36.645 6.730   -36.987 1.00 12.79  ? 769  PHE A CG  1 
ATOM   6151 C CD1 . PHE A 1 769 ? -36.078 7.683   -37.827 1.00 15.64  ? 769  PHE A CD1 1 
ATOM   6152 C CD2 . PHE A 1 769 ? -35.851 5.734   -36.471 1.00 14.04  ? 769  PHE A CD2 1 
ATOM   6153 C CE1 . PHE A 1 769 ? -34.679 7.644   -38.098 1.00 12.78  ? 769  PHE A CE1 1 
ATOM   6154 C CE2 . PHE A 1 769 ? -34.459 5.710   -36.767 1.00 12.81  ? 769  PHE A CE2 1 
ATOM   6155 C CZ  . PHE A 1 769 ? -33.930 6.643   -37.595 1.00 14.94  ? 769  PHE A CZ  1 
ATOM   6156 N N   . TRP A 1 770 ? -37.889 4.717   -39.338 1.00 15.90  ? 770  TRP A N   1 
ATOM   6157 C CA  . TRP A 1 770 ? -37.408 3.406   -39.759 1.00 16.83  ? 770  TRP A CA  1 
ATOM   6158 C C   . TRP A 1 770 ? -36.115 3.589   -40.549 1.00 16.66  ? 770  TRP A C   1 
ATOM   6159 O O   . TRP A 1 770 ? -36.054 4.371   -41.500 1.00 16.71  ? 770  TRP A O   1 
ATOM   6160 C CB  . TRP A 1 770 ? -38.427 2.645   -40.603 1.00 17.91  ? 770  TRP A CB  1 
ATOM   6161 C CG  . TRP A 1 770 ? -38.141 1.167   -40.652 1.00 17.25  ? 770  TRP A CG  1 
ATOM   6162 C CD1 . TRP A 1 770 ? -37.562 0.459   -41.691 1.00 17.85  ? 770  TRP A CD1 1 
ATOM   6163 C CD2 . TRP A 1 770 ? -38.406 0.203   -39.621 1.00 21.86  ? 770  TRP A CD2 1 
ATOM   6164 N NE1 . TRP A 1 770 ? -37.483 -0.869  -41.373 1.00 16.80  ? 770  TRP A NE1 1 
ATOM   6165 C CE2 . TRP A 1 770 ? -37.973 -1.065  -40.110 1.00 18.47  ? 770  TRP A CE2 1 
ATOM   6166 C CE3 . TRP A 1 770 ? -38.977 0.280   -38.329 1.00 22.82  ? 770  TRP A CE3 1 
ATOM   6167 C CZ2 . TRP A 1 770 ? -38.104 -2.253  -39.360 1.00 20.07  ? 770  TRP A CZ2 1 
ATOM   6168 C CZ3 . TRP A 1 770 ? -39.089 -0.906  -37.568 1.00 21.07  ? 770  TRP A CZ3 1 
ATOM   6169 C CH2 . TRP A 1 770 ? -38.659 -2.159  -38.097 1.00 20.53  ? 770  TRP A CH2 1 
ATOM   6170 N N   . ASP A 1 771 ? -35.075 2.908   -40.102 1.00 17.49  ? 771  ASP A N   1 
ATOM   6171 C CA  . ASP A 1 771 ? -33.808 2.898   -40.837 1.00 16.68  ? 771  ASP A CA  1 
ATOM   6172 C C   . ASP A 1 771 ? -33.279 1.466   -40.774 1.00 17.31  ? 771  ASP A C   1 
ATOM   6173 O O   . ASP A 1 771 ? -34.004 0.557   -40.414 1.00 17.80  ? 771  ASP A O   1 
ATOM   6174 C CB  . ASP A 1 771 ? -32.837 3.960   -40.268 1.00 16.74  ? 771  ASP A CB  1 
ATOM   6175 C CG  . ASP A 1 771 ? -32.299 3.625   -38.858 1.00 15.54  ? 771  ASP A CG  1 
ATOM   6176 O OD1 . ASP A 1 771 ? -32.706 2.635   -38.252 1.00 18.91  ? 771  ASP A OD1 1 
ATOM   6177 O OD2 . ASP A 1 771 ? -31.424 4.381   -38.342 1.00 18.30  ? 771  ASP A OD2 1 
ATOM   6178 N N   . ASP A 1 772 ? -31.997 1.246   -41.066 1.00 17.56  ? 772  ASP A N   1 
ATOM   6179 C CA  . ASP A 1 772 ? -31.525 -0.109  -41.133 1.00 17.53  ? 772  ASP A CA  1 
ATOM   6180 C C   . ASP A 1 772 ? -31.229 -0.707  -39.749 1.00 17.07  ? 772  ASP A C   1 
ATOM   6181 O O   . ASP A 1 772 ? -30.886 -1.864  -39.657 1.00 16.93  ? 772  ASP A O   1 
ATOM   6182 C CB  . ASP A 1 772 ? -30.330 -0.244  -42.132 1.00 17.87  ? 772  ASP A CB  1 
ATOM   6183 C CG  . ASP A 1 772 ? -29.020 0.276   -41.556 1.00 21.81  ? 772  ASP A CG  1 
ATOM   6184 O OD1 . ASP A 1 772 ? -29.023 0.702   -40.373 1.00 19.23  ? 772  ASP A OD1 1 
ATOM   6185 O OD2 . ASP A 1 772 ? -27.979 0.304   -42.299 1.00 23.59  ? 772  ASP A OD2 1 
ATOM   6186 N N   . GLY A 1 773 ? -31.371 0.071   -38.672 1.00 17.46  ? 773  GLY A N   1 
ATOM   6187 C CA  . GLY A 1 773 ? -31.346 -0.503  -37.309 1.00 17.13  ? 773  GLY A CA  1 
ATOM   6188 C C   . GLY A 1 773 ? -29.915 -0.687  -36.787 1.00 17.84  ? 773  GLY A C   1 
ATOM   6189 O O   . GLY A 1 773 ? -29.707 -1.168  -35.669 1.00 17.16  ? 773  GLY A O   1 
ATOM   6190 N N   . GLU A 1 774 ? -28.912 -0.332  -37.582 1.00 18.49  ? 774  GLU A N   1 
ATOM   6191 C CA  . GLU A 1 774 ? -27.547 -0.602  -37.121 1.00 20.91  ? 774  GLU A CA  1 
ATOM   6192 C C   . GLU A 1 774 ? -26.419 0.282   -37.628 1.00 19.94  ? 774  GLU A C   1 
ATOM   6193 O O   . GLU A 1 774 ? -25.379 0.363   -36.967 1.00 19.39  ? 774  GLU A O   1 
ATOM   6194 C CB  . GLU A 1 774 ? -27.189 -2.078  -37.330 1.00 21.33  ? 774  GLU A CB  1 
ATOM   6195 C CG  . GLU A 1 774 ? -27.348 -2.618  -38.730 1.00 26.73  ? 774  GLU A CG  1 
ATOM   6196 C CD  . GLU A 1 774 ? -26.686 -3.998  -38.891 1.00 27.70  ? 774  GLU A CD  1 
ATOM   6197 O OE1 . GLU A 1 774 ? -26.915 -4.899  -38.047 1.00 35.61  ? 774  GLU A OE1 1 
ATOM   6198 O OE2 . GLU A 1 774 ? -25.925 -4.170  -39.875 1.00 35.83  ? 774  GLU A OE2 1 
ATOM   6199 N N   . THR A 1 775 ? -26.612 0.945   -38.762 1.00 20.28  ? 775  THR A N   1 
ATOM   6200 C CA  . THR A 1 775 ? -25.565 1.832   -39.310 1.00 21.57  ? 775  THR A CA  1 
ATOM   6201 C C   . THR A 1 775 ? -25.401 3.080   -38.473 1.00 22.26  ? 775  THR A C   1 
ATOM   6202 O O   . THR A 1 775 ? -26.403 3.679   -38.021 1.00 20.52  ? 775  THR A O   1 
ATOM   6203 C CB  . THR A 1 775 ? -25.847 2.159   -40.778 1.00 20.62  ? 775  THR A CB  1 
ATOM   6204 O OG1 . THR A 1 775 ? -25.877 0.923   -41.491 1.00 22.12  ? 775  THR A OG1 1 
ATOM   6205 C CG2 . THR A 1 775 ? -24.773 3.020   -41.365 1.00 22.79  ? 775  THR A CG2 1 
ATOM   6206 N N   . LYS A 1 776 ? -24.144 3.465   -38.226 1.00 23.22  ? 776  LYS A N   1 
ATOM   6207 C CA  . LYS A 1 776 ? -23.862 4.688   -37.464 1.00 26.22  ? 776  LYS A CA  1 
ATOM   6208 C C   . LYS A 1 776 ? -24.130 5.922   -38.348 1.00 26.96  ? 776  LYS A C   1 
ATOM   6209 O O   . LYS A 1 776 ? -23.883 5.894   -39.548 1.00 27.68  ? 776  LYS A O   1 
ATOM   6210 C CB  . LYS A 1 776 ? -22.414 4.667   -36.879 1.00 26.76  ? 776  LYS A CB  1 
ATOM   6211 C CG  . LYS A 1 776 ? -22.165 5.673   -35.728 1.00 29.83  ? 776  LYS A CG  1 
ATOM   6212 C CD  . LYS A 1 776 ? -20.785 5.506   -35.056 1.00 28.51  ? 776  LYS A CD  1 
ATOM   6213 C CE  . LYS A 1 776 ? -20.835 4.520   -33.858 1.00 32.05  ? 776  LYS A CE  1 
ATOM   6214 N NZ  . LYS A 1 776 ? -19.707 4.613   -32.823 1.00 31.70  ? 776  LYS A NZ  1 
ATOM   6215 N N   . ASP A 1 777 ? -24.707 6.974   -37.778 1.00 28.33  ? 777  ASP A N   1 
ATOM   6216 C CA  . ASP A 1 777 ? -24.934 8.241   -38.535 1.00 29.56  ? 777  ASP A CA  1 
ATOM   6217 C C   . ASP A 1 777 ? -26.074 8.240   -39.588 1.00 28.08  ? 777  ASP A C   1 
ATOM   6218 O O   . ASP A 1 777 ? -26.133 9.103   -40.454 1.00 28.75  ? 777  ASP A O   1 
ATOM   6219 C CB  . ASP A 1 777 ? -23.615 8.737   -39.150 1.00 31.23  ? 777  ASP A CB  1 
ATOM   6220 C CG  . ASP A 1 777 ? -22.627 9.230   -38.094 1.00 36.38  ? 777  ASP A CG  1 
ATOM   6221 O OD1 . ASP A 1 777 ? -23.095 9.656   -37.002 1.00 41.22  ? 777  ASP A OD1 1 
ATOM   6222 O OD2 . ASP A 1 777 ? -21.388 9.214   -38.362 1.00 41.55  ? 777  ASP A OD2 1 
ATOM   6223 N N   . THR A 1 778 ? -26.986 7.279   -39.521 1.00 26.57  ? 778  THR A N   1 
ATOM   6224 C CA  . THR A 1 778 ? -28.086 7.282   -40.470 1.00 25.38  ? 778  THR A CA  1 
ATOM   6225 C C   . THR A 1 778 ? -28.952 8.517   -40.278 1.00 24.99  ? 778  THR A C   1 
ATOM   6226 O O   . THR A 1 778 ? -29.625 8.939   -41.217 1.00 26.11  ? 778  THR A O   1 
ATOM   6227 C CB  . THR A 1 778 ? -28.999 6.049   -40.346 1.00 25.25  ? 778  THR A CB  1 
ATOM   6228 O OG1 . THR A 1 778 ? -29.509 5.975   -39.016 1.00 26.38  ? 778  THR A OG1 1 
ATOM   6229 C CG2 . THR A 1 778 ? -28.267 4.800   -40.651 1.00 23.42  ? 778  THR A CG2 1 
ATOM   6230 N N   . VAL A 1 779 ? -28.968 9.080   -39.070 1.00 23.93  ? 779  VAL A N   1 
ATOM   6231 C CA  . VAL A 1 779 ? -29.802 10.253  -38.819 1.00 23.60  ? 779  VAL A CA  1 
ATOM   6232 C C   . VAL A 1 779 ? -29.080 11.503  -39.340 1.00 24.60  ? 779  VAL A C   1 
ATOM   6233 O O   . VAL A 1 779 ? -29.636 12.270  -40.127 1.00 23.21  ? 779  VAL A O   1 
ATOM   6234 C CB  . VAL A 1 779 ? -30.250 10.373  -37.348 1.00 23.09  ? 779  VAL A CB  1 
ATOM   6235 C CG1 . VAL A 1 779 ? -31.014 11.655  -37.129 1.00 22.48  ? 779  VAL A CG1 1 
ATOM   6236 C CG2 . VAL A 1 779 ? -31.096 9.156   -36.928 1.00 23.04  ? 779  VAL A CG2 1 
ATOM   6237 N N   . ALA A 1 780 ? -27.812 11.657  -38.955 1.00 25.36  ? 780  ALA A N   1 
ATOM   6238 C CA  . ALA A 1 780 ? -26.987 12.747  -39.457 1.00 26.82  ? 780  ALA A CA  1 
ATOM   6239 C C   . ALA A 1 780 ? -26.842 12.723  -40.973 1.00 27.33  ? 780  ALA A C   1 
ATOM   6240 O O   . ALA A 1 780 ? -26.874 13.766  -41.608 1.00 27.94  ? 780  ALA A O   1 
ATOM   6241 C CB  . ALA A 1 780 ? -25.582 12.761  -38.768 1.00 26.48  ? 780  ALA A CB  1 
ATOM   6242 N N   . ASN A 1 781 ? -26.698 11.542  -41.561 1.00 28.23  ? 781  ASN A N   1 
ATOM   6243 C CA  . ASN A 1 781 ? -26.613 11.424  -43.003 1.00 28.89  ? 781  ASN A CA  1 
ATOM   6244 C C   . ASN A 1 781 ? -27.976 11.319  -43.687 1.00 28.44  ? 781  ASN A C   1 
ATOM   6245 O O   . ASN A 1 781 ? -28.058 11.148  -44.896 1.00 28.39  ? 781  ASN A O   1 
ATOM   6246 C CB  . ASN A 1 781 ? -25.735 10.254  -43.374 1.00 29.78  ? 781  ASN A CB  1 
ATOM   6247 C CG  . ASN A 1 781 ? -24.328 10.437  -42.862 1.00 33.34  ? 781  ASN A CG  1 
ATOM   6248 O OD1 . ASN A 1 781 ? -23.690 9.491   -42.393 1.00 38.39  ? 781  ASN A OD1 1 
ATOM   6249 N ND2 . ASN A 1 781 ? -23.850 11.681  -42.905 1.00 33.17  ? 781  ASN A ND2 1 
ATOM   6250 N N   . LYS A 1 782 ? -29.037 11.427  -42.907 1.00 27.84  ? 782  LYS A N   1 
ATOM   6251 C CA  . LYS A 1 782 ? -30.404 11.377  -43.464 1.00 26.69  ? 782  LYS A CA  1 
ATOM   6252 C C   . LYS A 1 782 ? -30.685 10.199  -44.397 1.00 25.38  ? 782  LYS A C   1 
ATOM   6253 O O   . LYS A 1 782 ? -31.164 10.396  -45.535 1.00 25.61  ? 782  LYS A O   1 
ATOM   6254 C CB  . LYS A 1 782 ? -30.710 12.660  -44.232 1.00 28.27  ? 782  LYS A CB  1 
ATOM   6255 C CG  . LYS A 1 782 ? -30.490 13.919  -43.483 1.00 31.17  ? 782  LYS A CG  1 
ATOM   6256 C CD  . LYS A 1 782 ? -31.768 14.406  -42.862 1.00 37.23  ? 782  LYS A CD  1 
ATOM   6257 C CE  . LYS A 1 782 ? -31.545 15.796  -42.290 1.00 40.89  ? 782  LYS A CE  1 
ATOM   6258 N NZ  . LYS A 1 782 ? -32.377 15.963  -41.057 1.00 43.70  ? 782  LYS A NZ  1 
ATOM   6259 N N   . VAL A 1 783 ? -30.433 8.988   -43.910 1.00 22.43  ? 783  VAL A N   1 
ATOM   6260 C CA  . VAL A 1 783 ? -30.785 7.753   -44.591 1.00 21.21  ? 783  VAL A CA  1 
ATOM   6261 C C   . VAL A 1 783 ? -31.841 7.106   -43.686 1.00 20.93  ? 783  VAL A C   1 
ATOM   6262 O O   . VAL A 1 783 ? -31.560 6.246   -42.860 1.00 21.38  ? 783  VAL A O   1 
ATOM   6263 C CB  . VAL A 1 783 ? -29.545 6.830   -44.853 1.00 21.62  ? 783  VAL A CB  1 
ATOM   6264 C CG1 . VAL A 1 783 ? -29.922 5.636   -45.711 1.00 21.42  ? 783  VAL A CG1 1 
ATOM   6265 C CG2 . VAL A 1 783 ? -28.444 7.614   -45.543 1.00 22.34  ? 783  VAL A CG2 1 
ATOM   6266 N N   . TYR A 1 784 ? -33.068 7.571   -43.814 1.00 19.50  ? 784  TYR A N   1 
ATOM   6267 C CA  . TYR A 1 784 ? -34.140 6.962   -43.013 1.00 18.55  ? 784  TYR A CA  1 
ATOM   6268 C C   . TYR A 1 784 ? -35.474 7.312   -43.565 1.00 18.69  ? 784  TYR A C   1 
ATOM   6269 O O   . TYR A 1 784 ? -35.567 8.192   -44.410 1.00 20.43  ? 784  TYR A O   1 
ATOM   6270 C CB  . TYR A 1 784 ? -34.082 7.394   -41.549 1.00 17.84  ? 784  TYR A CB  1 
ATOM   6271 C CG  . TYR A 1 784 ? -34.176 8.889   -41.223 1.00 18.84  ? 784  TYR A CG  1 
ATOM   6272 C CD1 . TYR A 1 784 ? -35.391 9.476   -40.872 1.00 17.13  ? 784  TYR A CD1 1 
ATOM   6273 C CD2 . TYR A 1 784 ? -33.025 9.683   -41.156 1.00 17.58  ? 784  TYR A CD2 1 
ATOM   6274 C CE1 . TYR A 1 784 ? -35.469 10.833  -40.532 1.00 20.04  ? 784  TYR A CE1 1 
ATOM   6275 C CE2 . TYR A 1 784 ? -33.086 11.011  -40.810 1.00 20.57  ? 784  TYR A CE2 1 
ATOM   6276 C CZ  . TYR A 1 784 ? -34.316 11.579  -40.497 1.00 20.20  ? 784  TYR A CZ  1 
ATOM   6277 O OH  . TYR A 1 784 ? -34.379 12.895  -40.148 1.00 19.65  ? 784  TYR A OH  1 
ATOM   6278 N N   . LEU A 1 785 ? -36.477 6.625   -43.045 1.00 17.22  ? 785  LEU A N   1 
ATOM   6279 C CA  . LEU A 1 785 ? -37.887 6.879   -43.372 1.00 17.84  ? 785  LEU A CA  1 
ATOM   6280 C C   . LEU A 1 785 ? -38.492 7.504   -42.126 1.00 17.18  ? 785  LEU A C   1 
ATOM   6281 O O   . LEU A 1 785 ? -38.312 6.985   -41.015 1.00 18.24  ? 785  LEU A O   1 
ATOM   6282 C CB  . LEU A 1 785 ? -38.575 5.566   -43.683 1.00 17.81  ? 785  LEU A CB  1 
ATOM   6283 C CG  . LEU A 1 785 ? -40.127 5.647   -43.674 1.00 20.19  ? 785  LEU A CG  1 
ATOM   6284 C CD1 . LEU A 1 785 ? -40.573 6.472   -44.857 1.00 20.42  ? 785  LEU A CD1 1 
ATOM   6285 C CD2 . LEU A 1 785 ? -40.692 4.284   -43.722 1.00 23.63  ? 785  LEU A CD2 1 
ATOM   6286 N N   . LEU A 1 786 ? -39.182 8.626   -42.268 1.00 17.38  ? 786  LEU A N   1 
ATOM   6287 C CA  . LEU A 1 786 ? -40.027 9.092   -41.163 1.00 17.91  ? 786  LEU A CA  1 
ATOM   6288 C C   . LEU A 1 786 ? -41.423 9.283   -41.722 1.00 19.16  ? 786  LEU A C   1 
ATOM   6289 O O   . LEU A 1 786 ? -41.592 10.023  -42.674 1.00 19.18  ? 786  LEU A O   1 
ATOM   6290 C CB  . LEU A 1 786 ? -39.504 10.396  -40.570 1.00 17.13  ? 786  LEU A CB  1 
ATOM   6291 C CG  . LEU A 1 786 ? -40.120 11.018  -39.304 1.00 17.60  ? 786  LEU A CG  1 
ATOM   6292 C CD1 . LEU A 1 786 ? -39.942 10.065  -38.141 1.00 20.11  ? 786  LEU A CD1 1 
ATOM   6293 C CD2 . LEU A 1 786 ? -39.521 12.401  -39.007 1.00 19.10  ? 786  LEU A CD2 1 
ATOM   6294 N N   . CYS A 1 787 ? -42.411 8.589   -41.185 1.00 20.22  ? 787  CYS A N   1 
ATOM   6295 C CA  . CYS A 1 787 ? -43.778 8.887   -41.610 1.00 22.11  ? 787  CYS A CA  1 
ATOM   6296 C C   . CYS A 1 787 ? -44.628 9.325   -40.442 1.00 21.96  ? 787  CYS A C   1 
ATOM   6297 O O   . CYS A 1 787 ? -44.269 9.125   -39.296 1.00 19.20  ? 787  CYS A O   1 
ATOM   6298 C CB  . CYS A 1 787 ? -44.433 7.734   -42.337 1.00 23.40  ? 787  CYS A CB  1 
ATOM   6299 S SG  . CYS A 1 787 ? -44.259 6.167   -41.613 1.00 32.35  ? 787  CYS A SG  1 
ATOM   6300 N N   . GLU A 1 788 ? -45.744 9.964   -40.779 1.00 21.53  ? 788  GLU A N   1 
ATOM   6301 C CA  . GLU A 1 788 ? -46.649 10.559  -39.817 1.00 23.29  ? 788  GLU A CA  1 
ATOM   6302 C C   . GLU A 1 788 ? -48.010 9.972   -40.093 1.00 22.32  ? 788  GLU A C   1 
ATOM   6303 O O   . GLU A 1 788 ? -48.400 9.763   -41.260 1.00 24.38  ? 788  GLU A O   1 
ATOM   6304 C CB  . GLU A 1 788 ? -46.631 12.094  -39.946 1.00 23.80  ? 788  GLU A CB  1 
ATOM   6305 C CG  . GLU A 1 788 ? -45.192 12.697  -39.696 1.00 32.30  ? 788  GLU A CG  1 
ATOM   6306 C CD  . GLU A 1 788 ? -44.730 12.695  -38.207 1.00 41.10  ? 788  GLU A CD  1 
ATOM   6307 O OE1 . GLU A 1 788 ? -45.598 12.753  -37.292 1.00 46.48  ? 788  GLU A OE1 1 
ATOM   6308 O OE2 . GLU A 1 788 ? -43.495 12.666  -37.941 1.00 41.80  ? 788  GLU A OE2 1 
ATOM   6309 N N   . PHE A 1 789 ? -48.721 9.644   -39.027 1.00 22.11  ? 789  PHE A N   1 
ATOM   6310 C CA  . PHE A 1 789 ? -50.068 9.113   -39.116 1.00 20.57  ? 789  PHE A CA  1 
ATOM   6311 C C   . PHE A 1 789 ? -50.961 10.131  -38.478 1.00 21.63  ? 789  PHE A C   1 
ATOM   6312 O O   . PHE A 1 789 ? -50.597 10.710  -37.456 1.00 20.89  ? 789  PHE A O   1 
ATOM   6313 C CB  . PHE A 1 789 ? -50.177 7.809   -38.316 1.00 20.69  ? 789  PHE A CB  1 
ATOM   6314 C CG  . PHE A 1 789 ? -49.066 6.848   -38.599 1.00 22.84  ? 789  PHE A CG  1 
ATOM   6315 C CD1 . PHE A 1 789 ? -48.975 6.216   -39.856 1.00 21.74  ? 789  PHE A CD1 1 
ATOM   6316 C CD2 . PHE A 1 789 ? -48.078 6.601   -37.635 1.00 22.55  ? 789  PHE A CD2 1 
ATOM   6317 C CE1 . PHE A 1 789 ? -47.927 5.330   -40.144 1.00 22.73  ? 789  PHE A CE1 1 
ATOM   6318 C CE2 . PHE A 1 789 ? -47.017 5.708   -37.904 1.00 24.11  ? 789  PHE A CE2 1 
ATOM   6319 C CZ  . PHE A 1 789 ? -46.941 5.069   -39.163 1.00 23.95  ? 789  PHE A CZ  1 
ATOM   6320 N N   . SER A 1 790 ? -52.117 10.381  -39.081 1.00 21.82  ? 790  SER A N   1 
ATOM   6321 C CA  . SER A 1 790 ? -53.163 11.161  -38.399 1.00 23.71  ? 790  SER A CA  1 
ATOM   6322 C C   . SER A 1 790 ? -54.558 10.701  -38.764 1.00 23.39  ? 790  SER A C   1 
ATOM   6323 O O   . SER A 1 790 ? -54.812 10.269  -39.882 1.00 23.92  ? 790  SER A O   1 
ATOM   6324 C CB  . SER A 1 790 ? -53.008 12.674  -38.628 1.00 24.72  ? 790  SER A CB  1 
ATOM   6325 O OG  . SER A 1 790 ? -52.974 12.978  -39.999 1.00 29.08  ? 790  SER A OG  1 
ATOM   6326 N N   . VAL A 1 791 ? -55.458 10.793  -37.800 1.00 24.03  ? 791  VAL A N   1 
ATOM   6327 C CA  . VAL A 1 791 ? -56.834 10.411  -37.983 1.00 25.39  ? 791  VAL A CA  1 
ATOM   6328 C C   . VAL A 1 791 ? -57.653 11.608  -37.537 1.00 26.83  ? 791  VAL A C   1 
ATOM   6329 O O   . VAL A 1 791 ? -57.427 12.143  -36.470 1.00 24.41  ? 791  VAL A O   1 
ATOM   6330 C CB  . VAL A 1 791 ? -57.179 9.162   -37.144 1.00 25.49  ? 791  VAL A CB  1 
ATOM   6331 C CG1 . VAL A 1 791 ? -58.708 8.880   -37.177 1.00 25.08  ? 791  VAL A CG1 1 
ATOM   6332 C CG2 . VAL A 1 791 ? -56.374 7.980   -37.636 1.00 24.74  ? 791  VAL A CG2 1 
ATOM   6333 N N   . THR A 1 792 ? -58.530 12.088  -38.405 1.00 29.65  ? 792  THR A N   1 
ATOM   6334 C CA  . THR A 1 792 ? -59.482 13.118  -38.010 1.00 33.65  ? 792  THR A CA  1 
ATOM   6335 C C   . THR A 1 792 ? -60.657 12.778  -38.833 1.00 34.92  ? 792  THR A C   1 
ATOM   6336 O O   . THR A 1 792 ? -60.543 12.697  -40.074 1.00 35.42  ? 792  THR A O   1 
ATOM   6337 C CB  . THR A 1 792 ? -59.072 14.565  -38.348 1.00 33.25  ? 792  THR A CB  1 
ATOM   6338 O OG1 . THR A 1 792 ? -58.569 14.609  -39.676 1.00 36.84  ? 792  THR A OG1 1 
ATOM   6339 C CG2 . THR A 1 792 ? -58.018 15.096  -37.406 1.00 37.07  ? 792  THR A CG2 1 
ATOM   6340 N N   . GLN A 1 793 ? -61.761 12.606  -38.101 1.00 36.73  ? 793  GLN A N   1 
ATOM   6341 C CA  . GLN A 1 793 ? -62.997 11.903  -38.473 1.00 38.14  ? 793  GLN A CA  1 
ATOM   6342 C C   . GLN A 1 793 ? -63.070 11.196  -39.837 1.00 37.17  ? 793  GLN A C   1 
ATOM   6343 O O   . GLN A 1 793 ? -62.939 11.828  -40.908 1.00 37.23  ? 793  GLN A O   1 
ATOM   6344 C CB  . GLN A 1 793 ? -64.283 12.726  -38.140 1.00 39.33  ? 793  GLN A CB  1 
ATOM   6345 C CG  . GLN A 1 793 ? -64.082 14.203  -37.629 1.00 43.33  ? 793  GLN A CG  1 
ATOM   6346 C CD  . GLN A 1 793 ? -62.946 14.347  -36.588 1.00 45.36  ? 793  GLN A CD  1 
ATOM   6347 O OE1 . GLN A 1 793 ? -62.922 13.648  -35.571 1.00 47.49  ? 793  GLN A OE1 1 
ATOM   6348 N NE2 . GLN A 1 793 ? -62.000 15.243  -36.863 1.00 45.88  ? 793  GLN A NE2 1 
ATOM   6349 N N   . ASN A 1 794 ? -63.294 9.880   -39.771 1.00 35.70  ? 794  ASN A N   1 
ATOM   6350 C CA  . ASN A 1 794 ? -63.525 9.082   -40.974 1.00 34.93  ? 794  ASN A CA  1 
ATOM   6351 C C   . ASN A 1 794 ? -62.258 8.886   -41.801 1.00 32.36  ? 794  ASN A C   1 
ATOM   6352 O O   . ASN A 1 794 ? -62.360 8.383   -42.903 1.00 31.40  ? 794  ASN A O   1 
ATOM   6353 C CB  . ASN A 1 794 ? -64.551 9.759   -41.927 1.00 35.82  ? 794  ASN A CB  1 
ATOM   6354 C CG  . ASN A 1 794 ? -65.924 10.040  -41.266 1.00 40.40  ? 794  ASN A CG  1 
ATOM   6355 O OD1 . ASN A 1 794 ? -66.214 11.183  -40.846 1.00 44.37  ? 794  ASN A OD1 1 
ATOM   6356 N ND2 . ASN A 1 794 ? -66.773 9.013   -41.202 1.00 40.54  ? 794  ASN A ND2 1 
ATOM   6357 N N   . ARG A 1 795 ? -61.090 9.330   -41.337 1.00 30.68  ? 795  ARG A N   1 
ATOM   6358 C CA  . ARG A 1 795 ? -59.929 9.347   -42.247 1.00 29.32  ? 795  ARG A CA  1 
ATOM   6359 C C   . ARG A 1 795 ? -58.564 9.169   -41.556 1.00 27.63  ? 795  ARG A C   1 
ATOM   6360 O O   . ARG A 1 795 ? -58.204 9.990   -40.717 1.00 27.06  ? 795  ARG A O   1 
ATOM   6361 C CB  . ARG A 1 795 ? -59.961 10.660  -43.035 1.00 29.49  ? 795  ARG A CB  1 
ATOM   6362 C CG  . ARG A 1 795 ? -58.929 10.854  -44.131 1.00 30.83  ? 795  ARG A CG  1 
ATOM   6363 C CD  . ARG A 1 795 ? -59.267 12.139  -44.914 1.00 33.04  ? 795  ARG A CD  1 
ATOM   6364 N NE  . ARG A 1 795 ? -58.338 12.394  -46.017 1.00 44.49  ? 795  ARG A NE  1 
ATOM   6365 C CZ  . ARG A 1 795 ? -58.692 12.878  -47.215 1.00 46.97  ? 795  ARG A CZ  1 
ATOM   6366 N NH1 . ARG A 1 795 ? -59.973 13.152  -47.477 1.00 49.95  ? 795  ARG A NH1 1 
ATOM   6367 N NH2 . ARG A 1 795 ? -57.771 13.066  -48.164 1.00 47.14  ? 795  ARG A NH2 1 
ATOM   6368 N N   . LEU A 1 796 ? -57.816 8.124   -41.935 1.00 24.96  ? 796  LEU A N   1 
ATOM   6369 C CA  . LEU A 1 796 ? -56.407 7.964   -41.545 1.00 24.03  ? 796  LEU A CA  1 
ATOM   6370 C C   . LEU A 1 796 ? -55.587 8.412   -42.722 1.00 24.22  ? 796  LEU A C   1 
ATOM   6371 O O   . LEU A 1 796 ? -55.845 7.988   -43.850 1.00 24.60  ? 796  LEU A O   1 
ATOM   6372 C CB  . LEU A 1 796 ? -56.057 6.493   -41.236 1.00 23.90  ? 796  LEU A CB  1 
ATOM   6373 C CG  . LEU A 1 796 ? -54.563 6.105   -41.274 1.00 22.12  ? 796  LEU A CG  1 
ATOM   6374 C CD1 . LEU A 1 796 ? -53.852 6.672   -40.050 1.00 17.27  ? 796  LEU A CD1 1 
ATOM   6375 C CD2 . LEU A 1 796 ? -54.419 4.599   -41.311 1.00 21.92  ? 796  LEU A CD2 1 
ATOM   6376 N N   . GLU A 1 797 ? -54.615 9.277   -42.476 1.00 24.94  ? 797  GLU A N   1 
ATOM   6377 C CA  . GLU A 1 797 ? -53.655 9.656   -43.489 1.00 26.73  ? 797  GLU A CA  1 
ATOM   6378 C C   . GLU A 1 797 ? -52.291 9.161   -43.050 1.00 25.02  ? 797  GLU A C   1 
ATOM   6379 O O   . GLU A 1 797 ? -51.912 9.317   -41.877 1.00 22.96  ? 797  GLU A O   1 
ATOM   6380 C CB  . GLU A 1 797 ? -53.631 11.185  -43.686 1.00 27.22  ? 797  GLU A CB  1 
ATOM   6381 C CG  . GLU A 1 797 ? -55.011 11.750  -44.107 1.00 31.97  ? 797  GLU A CG  1 
ATOM   6382 C CD  . GLU A 1 797 ? -55.163 13.276  -43.964 1.00 34.30  ? 797  GLU A CD  1 
ATOM   6383 O OE1 . GLU A 1 797 ? -54.154 13.986  -43.667 1.00 42.09  ? 797  GLU A OE1 1 
ATOM   6384 O OE2 . GLU A 1 797 ? -56.317 13.775  -44.173 1.00 43.42  ? 797  GLU A OE2 1 
ATOM   6385 N N   . VAL A 1 798 ? -51.578 8.535   -43.990 1.00 24.85  ? 798  VAL A N   1 
ATOM   6386 C CA  . VAL A 1 798 ? -50.173 8.143   -43.805 1.00 23.86  ? 798  VAL A CA  1 
ATOM   6387 C C   . VAL A 1 798 ? -49.349 9.064   -44.717 1.00 24.02  ? 798  VAL A C   1 
ATOM   6388 O O   . VAL A 1 798 ? -49.547 9.069   -45.937 1.00 23.38  ? 798  VAL A O   1 
ATOM   6389 C CB  . VAL A 1 798 ? -49.919 6.632   -44.158 1.00 24.17  ? 798  VAL A CB  1 
ATOM   6390 C CG1 . VAL A 1 798 ? -48.466 6.241   -43.806 1.00 22.84  ? 798  VAL A CG1 1 
ATOM   6391 C CG2 . VAL A 1 798 ? -50.887 5.727   -43.441 1.00 24.99  ? 798  VAL A CG2 1 
ATOM   6392 N N   . ASN A 1 799 ? -48.511 9.900   -44.110 1.00 23.62  ? 799  ASN A N   1 
ATOM   6393 C CA  . ASN A 1 799 ? -47.803 10.989  -44.747 1.00 25.43  ? 799  ASN A CA  1 
ATOM   6394 C C   . ASN A 1 799 ? -46.300 10.746  -44.592 1.00 25.37  ? 799  ASN A C   1 
ATOM   6395 O O   . ASN A 1 799 ? -45.846 10.450  -43.501 1.00 25.84  ? 799  ASN A O   1 
ATOM   6396 C CB  . ASN A 1 799 ? -48.078 12.275  -43.964 1.00 26.74  ? 799  ASN A CB  1 
ATOM   6397 C CG  . ASN A 1 799 ? -48.795 13.332  -44.770 1.00 32.99  ? 799  ASN A CG  1 
ATOM   6398 O OD1 . ASN A 1 799 ? -48.221 14.393  -45.086 1.00 39.13  ? 799  ASN A OD1 1 
ATOM   6399 N ND2 . ASN A 1 799 ? -50.080 13.093  -45.053 1.00 36.77  ? 799  ASN A ND2 1 
ATOM   6400 N N   . ILE A 1 800 ? -45.530 10.913  -45.650 1.00 24.93  ? 800  ILE A N   1 
ATOM   6401 C CA  . ILE A 1 800 ? -44.097 10.641  -45.595 1.00 25.29  ? 800  ILE A CA  1 
ATOM   6402 C C   . ILE A 1 800 ? -43.353 11.956  -45.505 1.00 25.40  ? 800  ILE A C   1 
ATOM   6403 O O   . ILE A 1 800 ? -43.457 12.801  -46.396 1.00 25.03  ? 800  ILE A O   1 
ATOM   6404 C CB  . ILE A 1 800 ? -43.614 9.873   -46.859 1.00 25.20  ? 800  ILE A CB  1 
ATOM   6405 C CG1 . ILE A 1 800 ? -44.549 8.709   -47.187 1.00 25.03  ? 800  ILE A CG1 1 
ATOM   6406 C CG2 . ILE A 1 800 ? -42.210 9.376   -46.684 1.00 24.96  ? 800  ILE A CG2 1 
ATOM   6407 C CD1 . ILE A 1 800 ? -44.786 7.723   -46.039 1.00 26.18  ? 800  ILE A CD1 1 
ATOM   6408 N N   . SER A 1 801 ? -42.604 12.158  -44.431 1.00 25.30  ? 801  SER A N   1 
ATOM   6409 C CA  . SER A 1 801 ? -41.860 13.382  -44.344 1.00 26.62  ? 801  SER A CA  1 
ATOM   6410 C C   . SER A 1 801 ? -40.394 13.194  -44.741 1.00 26.71  ? 801  SER A C   1 
ATOM   6411 O O   . SER A 1 801 ? -39.790 14.122  -45.213 1.00 28.28  ? 801  SER A O   1 
ATOM   6412 C CB  . SER A 1 801 ? -42.009 14.044  -42.982 1.00 27.31  ? 801  SER A CB  1 
ATOM   6413 O OG  . SER A 1 801 ? -41.136 13.467  -42.031 1.00 29.97  ? 801  SER A OG  1 
ATOM   6414 N N   . GLN A 1 802 ? -39.829 12.008  -44.562 1.00 25.90  ? 802  GLN A N   1 
ATOM   6415 C CA  . GLN A 1 802 ? -38.454 11.759  -45.026 1.00 25.27  ? 802  GLN A CA  1 
ATOM   6416 C C   . GLN A 1 802 ? -38.486 10.384  -45.607 1.00 25.26  ? 802  GLN A C   1 
ATOM   6417 O O   . GLN A 1 802 ? -39.086 9.457   -45.028 1.00 23.74  ? 802  GLN A O   1 
ATOM   6418 C CB  . GLN A 1 802 ? -37.443 11.844  -43.877 1.00 25.33  ? 802  GLN A CB  1 
ATOM   6419 C CG  . GLN A 1 802 ? -35.964 11.461  -44.219 1.00 27.24  ? 802  GLN A CG  1 
ATOM   6420 C CD  . GLN A 1 802 ? -35.218 12.563  -44.910 1.00 32.21  ? 802  GLN A CD  1 
ATOM   6421 O OE1 . GLN A 1 802 ? -34.381 12.326  -45.802 1.00 34.29  ? 802  GLN A OE1 1 
ATOM   6422 N NE2 . GLN A 1 802 ? -35.524 13.778  -44.536 1.00 31.69  ? 802  GLN A NE2 1 
ATOM   6423 N N   . SER A 1 803 ? -37.812 10.222  -46.734 1.00 25.88  ? 803  SER A N   1 
ATOM   6424 C CA  . SER A 1 803 ? -37.988 9.032   -47.501 1.00 27.76  ? 803  SER A CA  1 
ATOM   6425 C C   . SER A 1 803 ? -36.681 8.569   -48.143 1.00 27.66  ? 803  SER A C   1 
ATOM   6426 O O   . SER A 1 803 ? -36.640 8.280   -49.334 1.00 28.74  ? 803  SER A O   1 
ATOM   6427 C CB  . SER A 1 803 ? -39.031 9.331   -48.578 1.00 28.51  ? 803  SER A CB  1 
ATOM   6428 O OG  . SER A 1 803 ? -39.252 8.164   -49.313 1.00 33.26  ? 803  SER A OG  1 
ATOM   6429 N N   . THR A 1 804 ? -35.611 8.501   -47.369 1.00 26.16  ? 804  THR A N   1 
ATOM   6430 C CA  . THR A 1 804 ? -34.330 8.155   -47.958 1.00 25.80  ? 804  THR A CA  1 
ATOM   6431 C C   . THR A 1 804 ? -33.839 6.763   -47.577 1.00 25.54  ? 804  THR A C   1 
ATOM   6432 O O   . THR A 1 804 ? -32.685 6.432   -47.809 1.00 25.99  ? 804  THR A O   1 
ATOM   6433 C CB  . THR A 1 804 ? -33.282 9.208   -47.645 1.00 25.46  ? 804  THR A CB  1 
ATOM   6434 O OG1 . THR A 1 804 ? -33.389 9.588   -46.268 1.00 25.45  ? 804  THR A OG1 1 
ATOM   6435 C CG2 . THR A 1 804 ? -33.512 10.450  -48.494 1.00 25.86  ? 804  THR A CG2 1 
ATOM   6436 N N   . TYR A 1 805 ? -34.714 5.933   -47.022 1.00 24.15  ? 805  TYR A N   1 
ATOM   6437 C CA  . TYR A 1 805 ? -34.353 4.561   -46.786 1.00 24.66  ? 805  TYR A CA  1 
ATOM   6438 C C   . TYR A 1 805 ? -35.539 3.686   -47.103 1.00 25.12  ? 805  TYR A C   1 
ATOM   6439 O O   . TYR A 1 805 ? -36.627 3.907   -46.583 1.00 25.73  ? 805  TYR A O   1 
ATOM   6440 C CB  . TYR A 1 805 ? -33.912 4.314   -45.327 1.00 24.05  ? 805  TYR A CB  1 
ATOM   6441 C CG  . TYR A 1 805 ? -33.612 2.856   -45.051 1.00 23.56  ? 805  TYR A CG  1 
ATOM   6442 C CD1 . TYR A 1 805 ? -32.427 2.257   -45.541 1.00 20.88  ? 805  TYR A CD1 1 
ATOM   6443 C CD2 . TYR A 1 805 ? -34.515 2.059   -44.344 1.00 20.33  ? 805  TYR A CD2 1 
ATOM   6444 C CE1 . TYR A 1 805 ? -32.166 0.906   -45.310 1.00 22.01  ? 805  TYR A CE1 1 
ATOM   6445 C CE2 . TYR A 1 805 ? -34.258 0.721   -44.112 1.00 21.13  ? 805  TYR A CE2 1 
ATOM   6446 C CZ  . TYR A 1 805 ? -33.091 0.155   -44.585 1.00 22.97  ? 805  TYR A CZ  1 
ATOM   6447 O OH  . TYR A 1 805 ? -32.859 -1.164  -44.349 1.00 23.01  ? 805  TYR A OH  1 
ATOM   6448 N N   . LYS A 1 806 ? -35.334 2.688   -47.949 1.00 25.36  ? 806  LYS A N   1 
ATOM   6449 C CA  . LYS A 1 806 ? -36.401 1.752   -48.214 1.00 25.44  ? 806  LYS A CA  1 
ATOM   6450 C C   . LYS A 1 806 ? -35.915 0.381   -47.788 1.00 24.62  ? 806  LYS A C   1 
ATOM   6451 O O   . LYS A 1 806 ? -34.950 -0.143  -48.344 1.00 24.99  ? 806  LYS A O   1 
ATOM   6452 C CB  . LYS A 1 806 ? -36.833 1.756   -49.688 1.00 26.68  ? 806  LYS A CB  1 
ATOM   6453 C CG  . LYS A 1 806 ? -38.057 0.815   -49.883 1.00 27.63  ? 806  LYS A CG  1 
ATOM   6454 C CD  . LYS A 1 806 ? -39.086 1.309   -50.896 1.00 29.90  ? 806  LYS A CD  1 
ATOM   6455 C CE  . LYS A 1 806 ? -40.372 0.462   -50.791 1.00 30.16  ? 806  LYS A CE  1 
ATOM   6456 N NZ  . LYS A 1 806 ? -41.362 0.729   -51.870 1.00 34.71  ? 806  LYS A NZ  1 
ATOM   6457 N N   . ASP A 1 807 ? -36.586 -0.183  -46.788 1.00 22.68  ? 807  ASP A N   1 
ATOM   6458 C CA  . ASP A 1 807 ? -36.282 -1.491  -46.255 1.00 21.55  ? 807  ASP A CA  1 
ATOM   6459 C C   . ASP A 1 807 ? -36.499 -2.581  -47.320 1.00 22.41  ? 807  ASP A C   1 
ATOM   6460 O O   . ASP A 1 807 ? -37.556 -2.645  -47.966 1.00 20.40  ? 807  ASP A O   1 
ATOM   6461 C CB  . ASP A 1 807 ? -37.169 -1.754  -45.032 1.00 21.95  ? 807  ASP A CB  1 
ATOM   6462 C CG  . ASP A 1 807 ? -36.741 -2.982  -44.257 1.00 23.52  ? 807  ASP A CG  1 
ATOM   6463 O OD1 . ASP A 1 807 ? -36.783 -4.086  -44.837 1.00 25.82  ? 807  ASP A OD1 1 
ATOM   6464 O OD2 . ASP A 1 807 ? -36.370 -2.853  -43.073 1.00 25.09  ? 807  ASP A OD2 1 
ATOM   6465 N N   . PRO A 1 808 ? -35.487 -3.435  -47.535 1.00 23.14  ? 808  PRO A N   1 
ATOM   6466 C CA  . PRO A 1 808 ? -35.626 -4.418  -48.618 1.00 23.32  ? 808  PRO A CA  1 
ATOM   6467 C C   . PRO A 1 808 ? -36.544 -5.598  -48.322 1.00 23.06  ? 808  PRO A C   1 
ATOM   6468 O O   . PRO A 1 808 ? -36.764 -6.439  -49.200 1.00 23.97  ? 808  PRO A O   1 
ATOM   6469 C CB  . PRO A 1 808 ? -34.187 -4.908  -48.787 1.00 22.33  ? 808  PRO A CB  1 
ATOM   6470 C CG  . PRO A 1 808 ? -33.659 -4.869  -47.389 1.00 24.40  ? 808  PRO A CG  1 
ATOM   6471 C CD  . PRO A 1 808 ? -34.168 -3.543  -46.872 1.00 23.75  ? 808  PRO A CD  1 
ATOM   6472 N N   . ASN A 1 809 ? -37.070 -5.687  -47.103 1.00 23.03  ? 809  ASN A N   1 
ATOM   6473 C CA  . ASN A 1 809 ? -37.948 -6.799  -46.745 1.00 22.83  ? 809  ASN A CA  1 
ATOM   6474 C C   . ASN A 1 809 ? -39.427 -6.666  -47.093 1.00 23.23  ? 809  ASN A C   1 
ATOM   6475 O O   . ASN A 1 809 ? -40.233 -7.370  -46.514 1.00 23.95  ? 809  ASN A O   1 
ATOM   6476 C CB  . ASN A 1 809 ? -37.781 -7.153  -45.269 1.00 22.49  ? 809  ASN A CB  1 
ATOM   6477 C CG  . ASN A 1 809 ? -36.401 -7.701  -44.975 1.00 24.07  ? 809  ASN A CG  1 
ATOM   6478 O OD1 . ASN A 1 809 ? -35.654 -7.145  -44.184 1.00 28.68  ? 809  ASN A OD1 1 
ATOM   6479 N ND2 . ASN A 1 809 ? -36.043 -8.750  -45.662 1.00 23.42  ? 809  ASN A ND2 1 
ATOM   6480 N N   . ASN A 1 810 ? -39.793 -5.790  -48.011 1.00 24.06  ? 810  ASN A N   1 
ATOM   6481 C CA  . ASN A 1 810 ? -41.222 -5.695  -48.428 1.00 24.42  ? 810  ASN A CA  1 
ATOM   6482 C C   . ASN A 1 810 ? -42.156 -5.444  -47.232 1.00 23.28  ? 810  ASN A C   1 
ATOM   6483 O O   . ASN A 1 810 ? -43.168 -6.138  -47.073 1.00 24.12  ? 810  ASN A O   1 
ATOM   6484 C CB  . ASN A 1 810 ? -41.688 -6.974  -49.199 1.00 25.00  ? 810  ASN A CB  1 
ATOM   6485 C CG  . ASN A 1 810 ? -43.085 -6.826  -49.872 1.00 26.46  ? 810  ASN A CG  1 
ATOM   6486 O OD1 . ASN A 1 810 ? -43.434 -5.751  -50.373 1.00 33.24  ? 810  ASN A OD1 1 
ATOM   6487 N ND2 . ASN A 1 810 ? -43.856 -7.933  -49.924 1.00 27.51  ? 810  ASN A ND2 1 
ATOM   6488 N N   . LEU A 1 811 ? -41.812 -4.484  -46.378 1.00 21.90  ? 811  LEU A N   1 
ATOM   6489 C CA  . LEU A 1 811 ? -42.566 -4.298  -45.132 1.00 20.13  ? 811  LEU A CA  1 
ATOM   6490 C C   . LEU A 1 811 ? -43.844 -3.543  -45.427 1.00 19.71  ? 811  LEU A C   1 
ATOM   6491 O O   . LEU A 1 811 ? -43.859 -2.580  -46.209 1.00 19.15  ? 811  LEU A O   1 
ATOM   6492 C CB  . LEU A 1 811 ? -41.736 -3.534  -44.092 1.00 20.12  ? 811  LEU A CB  1 
ATOM   6493 C CG  . LEU A 1 811 ? -40.447 -4.215  -43.598 1.00 20.27  ? 811  LEU A CG  1 
ATOM   6494 C CD1 . LEU A 1 811 ? -39.722 -3.347  -42.532 1.00 20.76  ? 811  LEU A CD1 1 
ATOM   6495 C CD2 . LEU A 1 811 ? -40.708 -5.628  -43.077 1.00 16.87  ? 811  LEU A CD2 1 
ATOM   6496 N N   . ALA A 1 812 ? -44.918 -3.919  -44.746 1.00 19.81  ? 812  ALA A N   1 
ATOM   6497 C CA  . ALA A 1 812 ? -46.135 -3.176  -44.965 1.00 19.73  ? 812  ALA A CA  1 
ATOM   6498 C C   . ALA A 1 812 ? -47.013 -3.299  -43.734 1.00 19.81  ? 812  ALA A C   1 
ATOM   6499 O O   . ALA A 1 812 ? -46.915 -4.268  -42.964 1.00 19.23  ? 812  ALA A O   1 
ATOM   6500 C CB  . ALA A 1 812 ? -46.862 -3.750  -46.202 1.00 19.53  ? 812  ALA A CB  1 
ATOM   6501 N N   . PHE A 1 813 ? -47.878 -2.316  -43.560 1.00 20.05  ? 813  PHE A N   1 
ATOM   6502 C CA  . PHE A 1 813 ? -48.896 -2.392  -42.530 1.00 19.89  ? 813  PHE A CA  1 
ATOM   6503 C C   . PHE A 1 813 ? -49.967 -3.320  -43.048 1.00 20.93  ? 813  PHE A C   1 
ATOM   6504 O O   . PHE A 1 813 ? -50.595 -3.039  -44.086 1.00 21.64  ? 813  PHE A O   1 
ATOM   6505 C CB  . PHE A 1 813 ? -49.467 -1.013  -42.222 1.00 20.41  ? 813  PHE A CB  1 
ATOM   6506 C CG  . PHE A 1 813 ? -48.442 -0.027  -41.770 1.00 21.88  ? 813  PHE A CG  1 
ATOM   6507 C CD1 . PHE A 1 813 ? -47.991 -0.032  -40.446 1.00 20.47  ? 813  PHE A CD1 1 
ATOM   6508 C CD2 . PHE A 1 813 ? -47.902 0.891   -42.671 1.00 22.18  ? 813  PHE A CD2 1 
ATOM   6509 C CE1 . PHE A 1 813 ? -47.004 0.881   -40.032 1.00 19.05  ? 813  PHE A CE1 1 
ATOM   6510 C CE2 . PHE A 1 813 ? -46.930 1.805   -42.270 1.00 24.40  ? 813  PHE A CE2 1 
ATOM   6511 C CZ  . PHE A 1 813 ? -46.473 1.801   -40.934 1.00 22.08  ? 813  PHE A CZ  1 
ATOM   6512 N N   . ASN A 1 814 ? -50.173 -4.434  -42.360 1.00 20.46  ? 814  ASN A N   1 
ATOM   6513 C CA  . ASN A 1 814 ? -51.203 -5.340  -42.798 1.00 21.23  ? 814  ASN A CA  1 
ATOM   6514 C C   . ASN A 1 814 ? -52.355 -5.415  -41.823 1.00 20.99  ? 814  ASN A C   1 
ATOM   6515 O O   . ASN A 1 814 ? -53.243 -6.223  -42.009 1.00 19.75  ? 814  ASN A O   1 
ATOM   6516 C CB  . ASN A 1 814 ? -50.664 -6.722  -43.141 1.00 22.87  ? 814  ASN A CB  1 
ATOM   6517 C CG  . ASN A 1 814 ? -50.344 -7.540  -41.935 1.00 26.77  ? 814  ASN A CG  1 
ATOM   6518 O OD1 . ASN A 1 814 ? -50.224 -7.026  -40.807 1.00 31.91  ? 814  ASN A OD1 1 
ATOM   6519 N ND2 . ASN A 1 814 ? -50.185 -8.853  -42.151 1.00 33.52  ? 814  ASN A ND2 1 
ATOM   6520 N N   . GLU A 1 815 ? -52.315 -4.593  -40.774 1.00 20.61  ? 815  GLU A N   1 
ATOM   6521 C CA  . GLU A 1 815 ? -53.407 -4.589  -39.792 1.00 23.17  ? 815  GLU A CA  1 
ATOM   6522 C C   . GLU A 1 815 ? -53.486 -3.198  -39.184 1.00 21.93  ? 815  GLU A C   1 
ATOM   6523 O O   . GLU A 1 815 ? -52.453 -2.594  -38.834 1.00 20.37  ? 815  GLU A O   1 
ATOM   6524 C CB  . GLU A 1 815 ? -53.200 -5.650  -38.694 1.00 22.74  ? 815  GLU A CB  1 
ATOM   6525 C CG  . GLU A 1 815 ? -54.412 -5.810  -37.723 1.00 27.00  ? 815  GLU A CG  1 
ATOM   6526 C CD  . GLU A 1 815 ? -54.276 -6.979  -36.744 1.00 29.54  ? 815  GLU A CD  1 
ATOM   6527 O OE1 . GLU A 1 815 ? -53.891 -8.112  -37.148 1.00 38.33  ? 815  GLU A OE1 1 
ATOM   6528 O OE2 . GLU A 1 815 ? -54.588 -6.767  -35.545 1.00 39.98  ? 815  GLU A OE2 1 
ATOM   6529 N N   . ILE A 1 816 ? -54.715 -2.685  -39.089 1.00 21.00  ? 816  ILE A N   1 
ATOM   6530 C CA  . ILE A 1 816 ? -54.972 -1.419  -38.397 1.00 20.11  ? 816  ILE A CA  1 
ATOM   6531 C C   . ILE A 1 816 ? -56.039 -1.708  -37.335 1.00 20.94  ? 816  ILE A C   1 
ATOM   6532 O O   . ILE A 1 816 ? -57.119 -2.188  -37.661 1.00 19.22  ? 816  ILE A O   1 
ATOM   6533 C CB  . ILE A 1 816 ? -55.452 -0.324  -39.345 1.00 20.15  ? 816  ILE A CB  1 
ATOM   6534 C CG1 . ILE A 1 816 ? -54.358 -0.005  -40.400 1.00 21.93  ? 816  ILE A CG1 1 
ATOM   6535 C CG2 . ILE A 1 816 ? -55.805 0.935   -38.556 1.00 19.82  ? 816  ILE A CG2 1 
ATOM   6536 C CD1 . ILE A 1 816 ? -54.817 0.918   -41.538 1.00 20.45  ? 816  ILE A CD1 1 
ATOM   6537 N N   . LYS A 1 817 ? -55.716 -1.443  -36.069 1.00 20.05  ? 817  LYS A N   1 
ATOM   6538 C CA  . LYS A 1 817 ? -56.674 -1.626  -35.000 1.00 20.71  ? 817  LYS A CA  1 
ATOM   6539 C C   . LYS A 1 817 ? -57.101 -0.252  -34.503 1.00 20.75  ? 817  LYS A C   1 
ATOM   6540 O O   . LYS A 1 817 ? -56.267 0.544   -34.127 1.00 20.62  ? 817  LYS A O   1 
ATOM   6541 C CB  . LYS A 1 817 ? -56.050 -2.462  -33.880 1.00 20.52  ? 817  LYS A CB  1 
ATOM   6542 C CG  . LYS A 1 817 ? -56.905 -2.704  -32.663 1.00 22.81  ? 817  LYS A CG  1 
ATOM   6543 C CD  . LYS A 1 817 ? -56.248 -3.774  -31.866 1.00 27.20  ? 817  LYS A CD  1 
ATOM   6544 C CE  . LYS A 1 817 ? -56.972 -4.110  -30.621 1.00 33.41  ? 817  LYS A CE  1 
ATOM   6545 N NZ  . LYS A 1 817 ? -55.985 -4.799  -29.671 1.00 36.25  ? 817  LYS A NZ  1 
ATOM   6546 N N   . ILE A 1 818 ? -58.414 0.013   -34.509 1.00 20.23  ? 818  ILE A N   1 
ATOM   6547 C CA  . ILE A 1 818 ? -58.935 1.323   -34.095 1.00 20.26  ? 818  ILE A CA  1 
ATOM   6548 C C   . ILE A 1 818 ? -59.700 1.130   -32.806 1.00 20.25  ? 818  ILE A C   1 
ATOM   6549 O O   . ILE A 1 818 ? -60.587 0.296   -32.752 1.00 19.45  ? 818  ILE A O   1 
ATOM   6550 C CB  . ILE A 1 818 ? -59.878 1.923   -35.157 1.00 20.40  ? 818  ILE A CB  1 
ATOM   6551 C CG1 . ILE A 1 818 ? -59.156 2.043   -36.518 1.00 21.06  ? 818  ILE A CG1 1 
ATOM   6552 C CG2 . ILE A 1 818 ? -60.443 3.254   -34.668 1.00 19.09  ? 818  ILE A CG2 1 
ATOM   6553 C CD1 . ILE A 1 818 ? -60.094 2.355   -37.705 1.00 22.78  ? 818  ILE A CD1 1 
ATOM   6554 N N   . LEU A 1 819 ? -59.329 1.887   -31.772 1.00 19.02  ? 819  LEU A N   1 
ATOM   6555 C CA  . LEU A 1 819 ? -59.932 1.772   -30.444 1.00 19.35  ? 819  LEU A CA  1 
ATOM   6556 C C   . LEU A 1 819 ? -60.877 2.971   -30.248 1.00 19.41  ? 819  LEU A C   1 
ATOM   6557 O O   . LEU A 1 819 ? -60.580 4.070   -30.688 1.00 19.10  ? 819  LEU A O   1 
ATOM   6558 C CB  . LEU A 1 819 ? -58.831 1.763   -29.345 1.00 19.18  ? 819  LEU A CB  1 
ATOM   6559 C CG  . LEU A 1 819 ? -57.663 0.774   -29.530 1.00 18.84  ? 819  LEU A CG  1 
ATOM   6560 C CD1 . LEU A 1 819 ? -56.569 0.852   -28.403 1.00 18.02  ? 819  LEU A CD1 1 
ATOM   6561 C CD2 . LEU A 1 819 ? -58.172 -0.676  -29.633 1.00 14.97  ? 819  LEU A CD2 1 
ATOM   6562 N N   . GLY A 1 820 ? -62.014 2.738   -29.610 1.00 19.95  ? 820  GLY A N   1 
ATOM   6563 C CA  . GLY A 1 820 ? -62.945 3.824   -29.245 1.00 20.79  ? 820  GLY A CA  1 
ATOM   6564 C C   . GLY A 1 820 ? -63.729 4.296   -30.458 1.00 22.11  ? 820  GLY A C   1 
ATOM   6565 O O   . GLY A 1 820 ? -64.056 5.480   -30.582 1.00 22.89  ? 820  GLY A O   1 
ATOM   6566 N N   . THR A 1 821 ? -64.020 3.373   -31.370 1.00 22.53  ? 821  THR A N   1 
ATOM   6567 C CA  . THR A 1 821 ? -64.776 3.709   -32.573 1.00 22.87  ? 821  THR A CA  1 
ATOM   6568 C C   . THR A 1 821 ? -66.164 3.046   -32.673 1.00 22.63  ? 821  THR A C   1 
ATOM   6569 O O   . THR A 1 821 ? -66.393 1.935   -32.177 1.00 20.99  ? 821  THR A O   1 
ATOM   6570 C CB  . THR A 1 821 ? -63.970 3.406   -33.842 1.00 23.73  ? 821  THR A CB  1 
ATOM   6571 O OG1 . THR A 1 821 ? -64.719 3.848   -34.979 1.00 25.17  ? 821  THR A OG1 1 
ATOM   6572 C CG2 . THR A 1 821 ? -63.677 1.896   -33.954 1.00 21.07  ? 821  THR A CG2 1 
ATOM   6573 N N   . GLU A 1 822 ? -67.090 3.762   -33.305 1.00 23.51  ? 822  GLU A N   1 
ATOM   6574 C CA  . GLU A 1 822 ? -68.340 3.192   -33.753 1.00 25.76  ? 822  GLU A CA  1 
ATOM   6575 C C   . GLU A 1 822 ? -68.003 2.312   -34.963 1.00 26.50  ? 822  GLU A C   1 
ATOM   6576 O O   . GLU A 1 822 ? -66.921 2.455   -35.558 1.00 26.01  ? 822  GLU A O   1 
ATOM   6577 C CB  . GLU A 1 822 ? -69.328 4.315   -34.138 1.00 25.85  ? 822  GLU A CB  1 
ATOM   6578 C CG  . GLU A 1 822 ? -69.887 5.083   -32.910 1.00 28.77  ? 822  GLU A CG  1 
ATOM   6579 C CD  . GLU A 1 822 ? -70.397 4.164   -31.808 1.00 33.91  ? 822  GLU A CD  1 
ATOM   6580 O OE1 . GLU A 1 822 ? -71.296 3.327   -32.068 1.00 38.62  ? 822  GLU A OE1 1 
ATOM   6581 O OE2 . GLU A 1 822 ? -69.906 4.278   -30.665 1.00 37.18  ? 822  GLU A OE2 1 
ATOM   6582 N N   . GLU A 1 823 ? -68.905 1.410   -35.333 1.00 27.86  ? 823  GLU A N   1 
ATOM   6583 C CA  . GLU A 1 823 ? -68.654 0.524   -36.485 1.00 28.90  ? 823  GLU A CA  1 
ATOM   6584 C C   . GLU A 1 823 ? -68.280 1.281   -37.761 1.00 29.28  ? 823  GLU A C   1 
ATOM   6585 O O   . GLU A 1 823 ? -69.098 2.060   -38.272 1.00 29.18  ? 823  GLU A O   1 
ATOM   6586 C CB  . GLU A 1 823 ? -69.875 -0.360  -36.763 1.00 29.74  ? 823  GLU A CB  1 
ATOM   6587 C CG  . GLU A 1 823 ? -69.531 -1.472  -37.736 1.00 32.33  ? 823  GLU A CG  1 
ATOM   6588 C CD  . GLU A 1 823 ? -70.531 -2.612  -37.783 1.00 36.57  ? 823  GLU A CD  1 
ATOM   6589 O OE1 . GLU A 1 823 ? -71.654 -2.499  -37.231 1.00 37.00  ? 823  GLU A OE1 1 
ATOM   6590 O OE2 . GLU A 1 823 ? -70.176 -3.628  -38.419 1.00 37.50  ? 823  GLU A OE2 1 
ATOM   6591 N N   . PRO A 1 824 ? -67.055 1.066   -38.285 1.00 29.60  ? 824  PRO A N   1 
ATOM   6592 C CA  . PRO A 1 824 ? -66.768 1.634   -39.602 1.00 30.87  ? 824  PRO A CA  1 
ATOM   6593 C C   . PRO A 1 824 ? -67.467 0.864   -40.723 1.00 32.42  ? 824  PRO A C   1 
ATOM   6594 O O   . PRO A 1 824 ? -67.713 -0.348  -40.607 1.00 33.80  ? 824  PRO A O   1 
ATOM   6595 C CB  . PRO A 1 824 ? -65.251 1.489   -39.763 1.00 30.51  ? 824  PRO A CB  1 
ATOM   6596 C CG  . PRO A 1 824 ? -64.748 0.820   -38.502 1.00 30.39  ? 824  PRO A CG  1 
ATOM   6597 C CD  . PRO A 1 824 ? -65.918 0.314   -37.727 1.00 29.25  ? 824  PRO A CD  1 
ATOM   6598 N N   . SER A 1 825 ? -67.805 1.571   -41.787 1.00 32.67  ? 825  SER A N   1 
ATOM   6599 C CA  . SER A 1 825 ? -68.430 0.936   -42.931 1.00 33.48  ? 825  SER A CA  1 
ATOM   6600 C C   . SER A 1 825 ? -67.802 1.576   -44.139 1.00 32.81  ? 825  SER A C   1 
ATOM   6601 O O   . SER A 1 825 ? -67.248 2.670   -44.016 1.00 32.07  ? 825  SER A O   1 
ATOM   6602 C CB  . SER A 1 825 ? -69.943 1.157   -42.906 1.00 33.39  ? 825  SER A CB  1 
ATOM   6603 O OG  . SER A 1 825 ? -70.256 2.506   -43.192 1.00 36.32  ? 825  SER A OG  1 
ATOM   6604 N N   . ASN A 1 826 ? -67.872 0.890   -45.283 1.00 32.77  ? 826  ASN A N   1 
ATOM   6605 C CA  . ASN A 1 826 ? -67.327 1.379   -46.559 1.00 33.36  ? 826  ASN A CA  1 
ATOM   6606 C C   . ASN A 1 826 ? -65.872 1.804   -46.457 1.00 32.26  ? 826  ASN A C   1 
ATOM   6607 O O   . ASN A 1 826 ? -65.541 2.919   -46.848 1.00 32.26  ? 826  ASN A O   1 
ATOM   6608 C CB  . ASN A 1 826 ? -68.111 2.588   -47.070 1.00 33.87  ? 826  ASN A CB  1 
ATOM   6609 C CG  . ASN A 1 826 ? -69.596 2.331   -47.158 1.00 38.72  ? 826  ASN A CG  1 
ATOM   6610 O OD1 . ASN A 1 826 ? -70.047 1.176   -47.136 1.00 42.56  ? 826  ASN A OD1 1 
ATOM   6611 N ND2 . ASN A 1 826 ? -70.375 3.414   -47.242 1.00 41.37  ? 826  ASN A ND2 1 
ATOM   6612 N N   . VAL A 1 827 ? -65.025 0.942   -45.912 1.00 31.24  ? 827  VAL A N   1 
ATOM   6613 C CA  . VAL A 1 827 ? -63.611 1.274   -45.747 1.00 30.15  ? 827  VAL A CA  1 
ATOM   6614 C C   . VAL A 1 827 ? -62.907 1.259   -47.096 1.00 29.63  ? 827  VAL A C   1 
ATOM   6615 O O   . VAL A 1 827 ? -62.960 0.284   -47.827 1.00 29.56  ? 827  VAL A O   1 
ATOM   6616 C CB  . VAL A 1 827 ? -62.931 0.361   -44.717 1.00 30.11  ? 827  VAL A CB  1 
ATOM   6617 C CG1 . VAL A 1 827 ? -61.489 0.771   -44.530 1.00 30.10  ? 827  VAL A CG1 1 
ATOM   6618 C CG2 . VAL A 1 827 ? -63.693 0.428   -43.396 1.00 30.29  ? 827  VAL A CG2 1 
ATOM   6619 N N   . THR A 1 828 ? -62.277 2.377   -47.422 1.00 29.73  ? 828  THR A N   1 
ATOM   6620 C CA  . THR A 1 828 ? -61.645 2.591   -48.708 1.00 30.44  ? 828  THR A CA  1 
ATOM   6621 C C   . THR A 1 828 ? -60.181 2.935   -48.482 1.00 29.85  ? 828  THR A C   1 
ATOM   6622 O O   . THR A 1 828 ? -59.846 3.633   -47.527 1.00 29.30  ? 828  THR A O   1 
ATOM   6623 C CB  . THR A 1 828 ? -62.305 3.779   -49.448 1.00 30.74  ? 828  THR A CB  1 
ATOM   6624 O OG1 . THR A 1 828 ? -63.682 3.459   -49.715 1.00 34.32  ? 828  THR A OG1 1 
ATOM   6625 C CG2 . THR A 1 828 ? -61.603 4.035   -50.786 1.00 33.30  ? 828  THR A CG2 1 
ATOM   6626 N N   . VAL A 1 829 ? -59.327 2.465   -49.376 1.00 29.21  ? 829  VAL A N   1 
ATOM   6627 C CA  . VAL A 1 829 ? -57.899 2.742   -49.268 1.00 29.73  ? 829  VAL A CA  1 
ATOM   6628 C C   . VAL A 1 829 ? -57.473 3.425   -50.548 1.00 30.31  ? 829  VAL A C   1 
ATOM   6629 O O   . VAL A 1 829 ? -57.756 2.919   -51.637 1.00 30.57  ? 829  VAL A O   1 
ATOM   6630 C CB  . VAL A 1 829 ? -57.097 1.453   -49.073 1.00 29.72  ? 829  VAL A CB  1 
ATOM   6631 C CG1 . VAL A 1 829 ? -55.606 1.741   -49.087 1.00 28.38  ? 829  VAL A CG1 1 
ATOM   6632 C CG2 . VAL A 1 829 ? -57.535 0.739   -47.814 1.00 28.49  ? 829  VAL A CG2 1 
ATOM   6633 N N   . LYS A 1 830 ? -56.842 4.587   -50.425 1.00 30.28  ? 830  LYS A N   1 
ATOM   6634 C CA  . LYS A 1 830 ? -56.307 5.301   -51.569 1.00 32.17  ? 830  LYS A CA  1 
ATOM   6635 C C   . LYS A 1 830 ? -54.790 5.375   -51.454 1.00 32.25  ? 830  LYS A C   1 
ATOM   6636 O O   . LYS A 1 830 ? -54.263 5.557   -50.369 1.00 30.27  ? 830  LYS A O   1 
ATOM   6637 C CB  . LYS A 1 830 ? -56.880 6.715   -51.657 1.00 32.01  ? 830  LYS A CB  1 
ATOM   6638 C CG  . LYS A 1 830 ? -58.381 6.765   -51.969 1.00 33.68  ? 830  LYS A CG  1 
ATOM   6639 C CD  . LYS A 1 830 ? -58.856 8.205   -52.207 1.00 35.02  ? 830  LYS A CD  1 
ATOM   6640 C CE  . LYS A 1 830 ? -60.355 8.228   -52.565 1.00 42.69  ? 830  LYS A CE  1 
ATOM   6641 N NZ  . LYS A 1 830 ? -60.814 9.566   -53.120 1.00 44.67  ? 830  LYS A NZ  1 
ATOM   6642 N N   . HIS A 1 831 ? -54.110 5.231   -52.582 1.00 34.30  ? 831  HIS A N   1 
ATOM   6643 C CA  . HIS A 1 831 ? -52.657 5.332   -52.645 1.00 36.80  ? 831  HIS A CA  1 
ATOM   6644 C C   . HIS A 1 831 ? -52.335 6.538   -53.494 1.00 38.96  ? 831  HIS A C   1 
ATOM   6645 O O   . HIS A 1 831 ? -52.786 6.620   -54.643 1.00 38.88  ? 831  HIS A O   1 
ATOM   6646 C CB  . HIS A 1 831 ? -52.046 4.036   -53.216 1.00 36.58  ? 831  HIS A CB  1 
ATOM   6647 C CG  . HIS A 1 831 ? -50.546 4.047   -53.330 1.00 36.77  ? 831  HIS A CG  1 
ATOM   6648 N ND1 . HIS A 1 831 ? -49.860 3.164   -54.137 1.00 38.13  ? 831  HIS A ND1 1 
ATOM   6649 C CD2 . HIS A 1 831 ? -49.601 4.828   -52.745 1.00 37.61  ? 831  HIS A CD2 1 
ATOM   6650 C CE1 . HIS A 1 831 ? -48.560 3.402   -54.047 1.00 38.60  ? 831  HIS A CE1 1 
ATOM   6651 N NE2 . HIS A 1 831 ? -48.376 4.406   -53.208 1.00 37.04  ? 831  HIS A NE2 1 
ATOM   6652 N N   . ASN A 1 832 ? -51.563 7.469   -52.918 1.00 41.44  ? 832  ASN A N   1 
ATOM   6653 C CA  . ASN A 1 832 ? -51.269 8.767   -53.532 1.00 44.15  ? 832  ASN A CA  1 
ATOM   6654 C C   . ASN A 1 832 ? -52.513 9.457   -54.087 1.00 45.50  ? 832  ASN A C   1 
ATOM   6655 O O   . ASN A 1 832 ? -52.431 10.155  -55.093 1.00 46.03  ? 832  ASN A O   1 
ATOM   6656 C CB  . ASN A 1 832 ? -50.224 8.625   -54.651 1.00 44.59  ? 832  ASN A CB  1 
ATOM   6657 C CG  . ASN A 1 832 ? -48.846 8.295   -54.126 1.00 46.54  ? 832  ASN A CG  1 
ATOM   6658 O OD1 . ASN A 1 832 ? -48.332 8.974   -53.240 1.00 48.79  ? 832  ASN A OD1 1 
ATOM   6659 N ND2 . ASN A 1 832 ? -48.236 7.243   -54.675 1.00 48.49  ? 832  ASN A ND2 1 
ATOM   6660 N N   . GLY A 1 833 ? -53.663 9.240   -53.448 1.00 46.89  ? 833  GLY A N   1 
ATOM   6661 C CA  . GLY A 1 833 ? -54.920 9.820   -53.911 1.00 48.49  ? 833  GLY A CA  1 
ATOM   6662 C C   . GLY A 1 833 ? -55.770 8.909   -54.773 1.00 49.89  ? 833  GLY A C   1 
ATOM   6663 O O   . GLY A 1 833 ? -56.927 9.224   -55.051 1.00 50.17  ? 833  GLY A O   1 
ATOM   6664 N N   . VAL A 1 834 ? -55.214 7.766   -55.167 1.00 51.02  ? 834  VAL A N   1 
ATOM   6665 C CA  . VAL A 1 834 ? -55.831 6.854   -56.130 1.00 52.20  ? 834  VAL A CA  1 
ATOM   6666 C C   . VAL A 1 834 ? -56.330 5.572   -55.450 1.00 53.48  ? 834  VAL A C   1 
ATOM   6667 O O   . VAL A 1 834 ? -55.539 4.850   -54.840 1.00 53.10  ? 834  VAL A O   1 
ATOM   6668 C CB  . VAL A 1 834 ? -54.801 6.461   -57.244 1.00 52.34  ? 834  VAL A CB  1 
ATOM   6669 C CG1 . VAL A 1 834 ? -55.373 5.406   -58.214 1.00 51.88  ? 834  VAL A CG1 1 
ATOM   6670 C CG2 . VAL A 1 834 ? -54.278 7.704   -57.989 1.00 51.90  ? 834  VAL A CG2 1 
ATOM   6671 N N   . PRO A 1 835 ? -57.645 5.281   -55.546 1.00 54.94  ? 835  PRO A N   1 
ATOM   6672 C CA  . PRO A 1 835 ? -58.090 3.940   -55.151 1.00 56.13  ? 835  PRO A CA  1 
ATOM   6673 C C   . PRO A 1 835 ? -57.850 3.035   -56.348 1.00 57.49  ? 835  PRO A C   1 
ATOM   6674 O O   . PRO A 1 835 ? -58.154 3.460   -57.465 1.00 58.45  ? 835  PRO A O   1 
ATOM   6675 C CB  . PRO A 1 835 ? -59.588 4.123   -54.899 1.00 56.26  ? 835  PRO A CB  1 
ATOM   6676 C CG  . PRO A 1 835 ? -59.996 5.320   -55.730 1.00 55.21  ? 835  PRO A CG  1 
ATOM   6677 C CD  . PRO A 1 835 ? -58.758 6.135   -56.017 1.00 55.18  ? 835  PRO A CD  1 
ATOM   6678 N N   . SER A 1 836 ? -57.339 1.811   -56.196 1.00 58.63  ? 836  SER A N   1 
ATOM   6679 C CA  . SER A 1 836 ? -57.225 1.034   -54.964 1.00 59.41  ? 836  SER A CA  1 
ATOM   6680 C C   . SER A 1 836 ? -58.573 0.766   -54.311 1.00 59.63  ? 836  SER A C   1 
ATOM   6681 O O   . SER A 1 836 ? -59.382 0.014   -54.864 1.00 59.65  ? 836  SER A O   1 
ATOM   6682 C CB  . SER A 1 836 ? -56.183 1.594   -53.992 1.00 59.65  ? 836  SER A CB  1 
ATOM   6683 O OG  . SER A 1 836 ? -55.847 0.610   -53.023 1.00 60.51  ? 836  SER A OG  1 
ATOM   6684 N N   . THR A 1 838 ? -59.593 -3.233  -54.333 1.00 45.16  ? 838  THR A N   1 
ATOM   6685 C CA  . THR A 1 838 ? -59.290 -3.583  -52.935 1.00 45.00  ? 838  THR A CA  1 
ATOM   6686 C C   . THR A 1 838 ? -60.355 -3.021  -51.987 1.00 43.49  ? 838  THR A C   1 
ATOM   6687 O O   . THR A 1 838 ? -60.577 -1.807  -51.951 1.00 44.56  ? 838  THR A O   1 
ATOM   6688 C CB  . THR A 1 838 ? -57.906 -3.054  -52.458 1.00 45.20  ? 838  THR A CB  1 
ATOM   6689 O OG1 . THR A 1 838 ? -57.930 -1.618  -52.374 1.00 47.83  ? 838  THR A OG1 1 
ATOM   6690 C CG2 . THR A 1 838 ? -56.771 -3.502  -53.385 1.00 46.94  ? 838  THR A CG2 1 
ATOM   6691 N N   . SER A 1 839 ? -61.036 -3.903  -51.265 1.00 41.27  ? 839  SER A N   1 
ATOM   6692 C CA  . SER A 1 839 ? -61.853 -3.512  -50.118 1.00 39.00  ? 839  SER A CA  1 
ATOM   6693 C C   . SER A 1 839 ? -61.314 -4.348  -48.969 1.00 36.08  ? 839  SER A C   1 
ATOM   6694 O O   . SER A 1 839 ? -61.353 -5.572  -49.050 1.00 36.99  ? 839  SER A O   1 
ATOM   6695 C CB  . SER A 1 839 ? -63.322 -3.830  -50.357 1.00 39.53  ? 839  SER A CB  1 
ATOM   6696 O OG  . SER A 1 839 ? -64.071 -3.650  -49.164 1.00 41.93  ? 839  SER A OG  1 
ATOM   6697 N N   . PRO A 1 840 ? -60.758 -3.704  -47.922 1.00 32.95  ? 840  PRO A N   1 
ATOM   6698 C CA  . PRO A 1 840 ? -60.172 -4.501  -46.848 1.00 29.95  ? 840  PRO A CA  1 
ATOM   6699 C C   . PRO A 1 840 ? -61.202 -5.244  -46.027 1.00 27.59  ? 840  PRO A C   1 
ATOM   6700 O O   . PRO A 1 840 ? -62.390 -4.940  -46.096 1.00 27.01  ? 840  PRO A O   1 
ATOM   6701 C CB  . PRO A 1 840 ? -59.491 -3.459  -45.974 1.00 29.97  ? 840  PRO A CB  1 
ATOM   6702 C CG  . PRO A 1 840 ? -60.247 -2.212  -46.229 1.00 32.35  ? 840  PRO A CG  1 
ATOM   6703 C CD  . PRO A 1 840 ? -60.577 -2.258  -47.681 1.00 32.73  ? 840  PRO A CD  1 
ATOM   6704 N N   . THR A 1 841 ? -60.740 -6.212  -45.243 1.00 24.50  ? 841  THR A N   1 
ATOM   6705 C CA  . THR A 1 841 ? -61.612 -6.907  -44.289 1.00 23.16  ? 841  THR A CA  1 
ATOM   6706 C C   . THR A 1 841 ? -61.719 -6.092  -43.007 1.00 22.48  ? 841  THR A C   1 
ATOM   6707 O O   . THR A 1 841 ? -60.707 -5.609  -42.493 1.00 20.43  ? 841  THR A O   1 
ATOM   6708 C CB  . THR A 1 841 ? -61.057 -8.332  -44.008 1.00 23.29  ? 841  THR A CB  1 
ATOM   6709 O OG1 . THR A 1 841 ? -61.217 -9.138  -45.182 1.00 24.12  ? 841  THR A OG1 1 
ATOM   6710 C CG2 . THR A 1 841 ? -61.739 -9.003  -42.829 1.00 22.50  ? 841  THR A CG2 1 
ATOM   6711 N N   . VAL A 1 842 ? -62.945 -5.899  -42.512 1.00 21.08  ? 842  VAL A N   1 
ATOM   6712 C CA  . VAL A 1 842 ? -63.158 -5.190  -41.251 1.00 21.43  ? 842  VAL A CA  1 
ATOM   6713 C C   . VAL A 1 842 ? -63.883 -6.092  -40.260 1.00 21.40  ? 842  VAL A C   1 
ATOM   6714 O O   . VAL A 1 842 ? -64.951 -6.661  -40.584 1.00 21.02  ? 842  VAL A O   1 
ATOM   6715 C CB  . VAL A 1 842 ? -64.007 -3.909  -41.455 1.00 22.39  ? 842  VAL A CB  1 
ATOM   6716 C CG1 . VAL A 1 842 ? -64.231 -3.201  -40.104 1.00 22.31  ? 842  VAL A CG1 1 
ATOM   6717 C CG2 . VAL A 1 842 ? -63.330 -3.005  -42.475 1.00 24.95  ? 842  VAL A CG2 1 
ATOM   6718 N N   . THR A 1 843 ? -63.280 -6.271  -39.082 1.00 19.95  ? 843  THR A N   1 
ATOM   6719 C CA  . THR A 1 843 ? -63.917 -6.975  -37.989 1.00 20.93  ? 843  THR A CA  1 
ATOM   6720 C C   . THR A 1 843 ? -64.299 -5.955  -36.918 1.00 20.46  ? 843  THR A C   1 
ATOM   6721 O O   . THR A 1 843 ? -63.515 -5.086  -36.583 1.00 20.51  ? 843  THR A O   1 
ATOM   6722 C CB  . THR A 1 843 ? -62.966 -7.991  -37.411 1.00 20.69  ? 843  THR A CB  1 
ATOM   6723 O OG1 . THR A 1 843 ? -62.420 -8.785  -38.488 1.00 24.61  ? 843  THR A OG1 1 
ATOM   6724 C CG2 . THR A 1 843 ? -63.621 -8.868  -36.378 1.00 22.22  ? 843  THR A CG2 1 
ATOM   6725 N N   . TYR A 1 844 ? -65.496 -6.074  -36.371 1.00 20.02  ? 844  TYR A N   1 
ATOM   6726 C CA  . TYR A 1 844 ? -65.912 -5.105  -35.397 1.00 19.52  ? 844  TYR A CA  1 
ATOM   6727 C C   . TYR A 1 844 ? -66.450 -5.767  -34.143 1.00 20.30  ? 844  TYR A C   1 
ATOM   6728 O O   . TYR A 1 844 ? -67.183 -6.760  -34.203 1.00 19.26  ? 844  TYR A O   1 
ATOM   6729 C CB  . TYR A 1 844 ? -66.918 -4.115  -36.019 1.00 19.44  ? 844  TYR A CB  1 
ATOM   6730 C CG  . TYR A 1 844 ? -67.265 -3.005  -35.070 1.00 18.94  ? 844  TYR A CG  1 
ATOM   6731 C CD1 . TYR A 1 844 ? -66.291 -2.120  -34.636 1.00 16.50  ? 844  TYR A CD1 1 
ATOM   6732 C CD2 . TYR A 1 844 ? -68.565 -2.875  -34.558 1.00 18.76  ? 844  TYR A CD2 1 
ATOM   6733 C CE1 . TYR A 1 844 ? -66.577 -1.100  -33.719 1.00 18.00  ? 844  TYR A CE1 1 
ATOM   6734 C CE2 . TYR A 1 844 ? -68.879 -1.872  -33.666 1.00 17.22  ? 844  TYR A CE2 1 
ATOM   6735 C CZ  . TYR A 1 844 ? -67.888 -0.980  -33.250 1.00 18.07  ? 844  TYR A CZ  1 
ATOM   6736 O OH  . TYR A 1 844 ? -68.200 0.015   -32.364 1.00 20.88  ? 844  TYR A OH  1 
ATOM   6737 N N   . ASP A 1 845 ? -66.055 -5.223  -32.996 1.00 20.40  ? 845  ASP A N   1 
ATOM   6738 C CA  . ASP A 1 845 ? -66.533 -5.647  -31.707 1.00 22.36  ? 845  ASP A CA  1 
ATOM   6739 C C   . ASP A 1 845 ? -67.392 -4.519  -31.149 1.00 23.15  ? 845  ASP A C   1 
ATOM   6740 O O   . ASP A 1 845 ? -66.865 -3.526  -30.666 1.00 22.70  ? 845  ASP A O   1 
ATOM   6741 C CB  . ASP A 1 845 ? -65.334 -5.881  -30.778 1.00 22.77  ? 845  ASP A CB  1 
ATOM   6742 C CG  . ASP A 1 845 ? -65.721 -6.547  -29.462 1.00 25.43  ? 845  ASP A CG  1 
ATOM   6743 O OD1 . ASP A 1 845 ? -66.831 -6.325  -28.911 1.00 26.17  ? 845  ASP A OD1 1 
ATOM   6744 O OD2 . ASP A 1 845 ? -64.897 -7.321  -28.963 1.00 27.08  ? 845  ASP A OD2 1 
ATOM   6745 N N   . SER A 1 846 ? -68.709 -4.679  -31.163 1.00 24.90  ? 846  SER A N   1 
ATOM   6746 C CA  . SER A 1 846 ? -69.584 -3.575  -30.756 1.00 26.51  ? 846  SER A CA  1 
ATOM   6747 C C   . SER A 1 846 ? -69.618 -3.342  -29.248 1.00 27.12  ? 846  SER A C   1 
ATOM   6748 O O   . SER A 1 846 ? -69.884 -2.229  -28.807 1.00 28.42  ? 846  SER A O   1 
ATOM   6749 C CB  . SER A 1 846 ? -71.000 -3.778  -31.307 1.00 26.87  ? 846  SER A CB  1 
ATOM   6750 O OG  . SER A 1 846 ? -71.488 -5.011  -30.844 1.00 28.76  ? 846  SER A OG  1 
ATOM   6751 N N   . ASN A 1 847 ? -69.333 -4.373  -28.468 1.00 27.38  ? 847  ASN A N   1 
ATOM   6752 C CA  . ASN A 1 847 ? -69.220 -4.274  -27.019 1.00 28.13  ? 847  ASN A CA  1 
ATOM   6753 C C   . ASN A 1 847 ? -67.965 -3.485  -26.596 1.00 27.02  ? 847  ASN A C   1 
ATOM   6754 O O   . ASN A 1 847 ? -68.037 -2.618  -25.734 1.00 27.16  ? 847  ASN A O   1 
ATOM   6755 C CB  . ASN A 1 847 ? -69.183 -5.681  -26.406 1.00 29.69  ? 847  ASN A CB  1 
ATOM   6756 C CG  . ASN A 1 847 ? -69.147 -5.668  -24.872 1.00 36.60  ? 847  ASN A CG  1 
ATOM   6757 O OD1 . ASN A 1 847 ? -68.163 -6.127  -24.261 1.00 42.61  ? 847  ASN A OD1 1 
ATOM   6758 N ND2 . ASN A 1 847 ? -70.221 -5.143  -24.234 1.00 39.65  ? 847  ASN A ND2 1 
ATOM   6759 N N   . LEU A 1 848 ? -66.827 -3.771  -27.220 1.00 25.07  ? 848  LEU A N   1 
ATOM   6760 C CA  . LEU A 1 848 ? -65.560 -3.115  -26.869 1.00 24.30  ? 848  LEU A CA  1 
ATOM   6761 C C   . LEU A 1 848 ? -65.295 -1.817  -27.647 1.00 22.00  ? 848  LEU A C   1 
ATOM   6762 O O   . LEU A 1 848 ? -64.369 -1.062  -27.311 1.00 20.91  ? 848  LEU A O   1 
ATOM   6763 C CB  . LEU A 1 848 ? -64.408 -4.122  -27.088 1.00 24.94  ? 848  LEU A CB  1 
ATOM   6764 C CG  . LEU A 1 848 ? -63.937 -4.904  -25.849 1.00 26.70  ? 848  LEU A CG  1 
ATOM   6765 C CD1 . LEU A 1 848 ? -65.028 -5.215  -24.837 1.00 29.44  ? 848  LEU A CD1 1 
ATOM   6766 C CD2 . LEU A 1 848 ? -63.162 -6.136  -26.217 1.00 27.48  ? 848  LEU A CD2 1 
ATOM   6767 N N   . LYS A 1 849 ? -66.082 -1.581  -28.702 1.00 19.41  ? 849  LYS A N   1 
ATOM   6768 C CA  . LYS A 1 849 ? -65.885 -0.480  -29.652 1.00 18.27  ? 849  LYS A CA  1 
ATOM   6769 C C   . LYS A 1 849 ? -64.477 -0.531  -30.313 1.00 18.36  ? 849  LYS A C   1 
ATOM   6770 O O   . LYS A 1 849 ? -63.803 0.472   -30.398 1.00 16.61  ? 849  LYS A O   1 
ATOM   6771 C CB  . LYS A 1 849 ? -66.139 0.885   -28.994 1.00 18.29  ? 849  LYS A CB  1 
ATOM   6772 C CG  . LYS A 1 849 ? -67.475 0.981   -28.223 1.00 20.58  ? 849  LYS A CG  1 
ATOM   6773 C CD  . LYS A 1 849 ? -68.608 1.000   -29.219 1.00 22.11  ? 849  LYS A CD  1 
ATOM   6774 C CE  . LYS A 1 849 ? -69.993 1.222   -28.556 1.00 25.69  ? 849  LYS A CE  1 
ATOM   6775 N NZ  . LYS A 1 849 ? -71.118 1.062   -29.573 1.00 28.46  ? 849  LYS A NZ  1 
ATOM   6776 N N   . VAL A 1 850 ? -64.106 -1.715  -30.779 1.00 17.82  ? 850  VAL A N   1 
ATOM   6777 C CA  . VAL A 1 850 ? -62.846 -1.962  -31.467 1.00 17.89  ? 850  VAL A CA  1 
ATOM   6778 C C   . VAL A 1 850 ? -63.108 -2.485  -32.873 1.00 17.25  ? 850  VAL A C   1 
ATOM   6779 O O   . VAL A 1 850 ? -63.883 -3.465  -33.059 1.00 17.94  ? 850  VAL A O   1 
ATOM   6780 C CB  . VAL A 1 850 ? -62.018 -3.012  -30.706 1.00 17.65  ? 850  VAL A CB  1 
ATOM   6781 C CG1 . VAL A 1 850 ? -60.660 -3.295  -31.429 1.00 19.03  ? 850  VAL A CG1 1 
ATOM   6782 C CG2 . VAL A 1 850 ? -61.797 -2.575  -29.252 1.00 17.40  ? 850  VAL A CG2 1 
ATOM   6783 N N   . ALA A 1 851 ? -62.437 -1.872  -33.851 1.00 16.74  ? 851  ALA A N   1 
ATOM   6784 C CA  . ALA A 1 851 ? -62.467 -2.323  -35.236 1.00 16.19  ? 851  ALA A CA  1 
ATOM   6785 C C   . ALA A 1 851 ? -61.055 -2.786  -35.576 1.00 18.02  ? 851  ALA A C   1 
ATOM   6786 O O   . ALA A 1 851 ? -60.095 -2.161  -35.132 1.00 15.29  ? 851  ALA A O   1 
ATOM   6787 C CB  . ALA A 1 851 ? -62.837 -1.199  -36.144 1.00 15.78  ? 851  ALA A CB  1 
ATOM   6788 N N   . ILE A 1 852 ? -60.950 -3.882  -36.320 1.00 17.65  ? 852  ILE A N   1 
ATOM   6789 C CA  . ILE A 1 852 ? -59.636 -4.258  -36.858 1.00 18.91  ? 852  ILE A CA  1 
ATOM   6790 C C   . ILE A 1 852 ? -59.771 -4.370  -38.352 1.00 18.84  ? 852  ILE A C   1 
ATOM   6791 O O   . ILE A 1 852 ? -60.633 -5.099  -38.849 1.00 19.04  ? 852  ILE A O   1 
ATOM   6792 C CB  . ILE A 1 852 ? -59.103 -5.564  -36.301 1.00 19.25  ? 852  ILE A CB  1 
ATOM   6793 C CG1 . ILE A 1 852 ? -59.070 -5.533  -34.776 1.00 21.22  ? 852  ILE A CG1 1 
ATOM   6794 C CG2 . ILE A 1 852 ? -57.638 -5.814  -36.865 1.00 19.38  ? 852  ILE A CG2 1 
ATOM   6795 C CD1 . ILE A 1 852 ? -58.824 -6.902  -34.165 1.00 25.77  ? 852  ILE A CD1 1 
ATOM   6796 N N   . ILE A 1 853 ? -58.901 -3.669  -39.066 1.00 18.81  ? 853  ILE A N   1 
ATOM   6797 C CA  . ILE A 1 853 ? -58.931 -3.674  -40.513 1.00 19.67  ? 853  ILE A CA  1 
ATOM   6798 C C   . ILE A 1 853 ? -57.799 -4.574  -40.934 1.00 21.36  ? 853  ILE A C   1 
ATOM   6799 O O   . ILE A 1 853 ? -56.638 -4.404  -40.512 1.00 19.32  ? 853  ILE A O   1 
ATOM   6800 C CB  . ILE A 1 853 ? -58.735 -2.271  -41.123 1.00 20.21  ? 853  ILE A CB  1 
ATOM   6801 C CG1 . ILE A 1 853 ? -59.812 -1.298  -40.608 1.00 21.29  ? 853  ILE A CG1 1 
ATOM   6802 C CG2 . ILE A 1 853 ? -58.734 -2.332  -42.652 1.00 20.39  ? 853  ILE A CG2 1 
ATOM   6803 C CD1 . ILE A 1 853 ? -59.533 0.147   -40.961 1.00 24.33  ? 853  ILE A CD1 1 
ATOM   6804 N N   . THR A 1 854 ? -58.128 -5.510  -41.802 1.00 20.87  ? 854  THR A N   1 
ATOM   6805 C CA  . THR A 1 854 ? -57.150 -6.488  -42.218 1.00 23.55  ? 854  THR A CA  1 
ATOM   6806 C C   . THR A 1 854 ? -57.314 -6.710  -43.737 1.00 23.64  ? 854  THR A C   1 
ATOM   6807 O O   . THR A 1 854 ? -58.134 -6.029  -44.374 1.00 21.89  ? 854  THR A O   1 
ATOM   6808 C CB  . THR A 1 854 ? -57.351 -7.722  -41.320 1.00 23.37  ? 854  THR A CB  1 
ATOM   6809 O OG1 . THR A 1 854 ? -56.151 -8.482  -41.247 1.00 31.26  ? 854  THR A OG1 1 
ATOM   6810 C CG2 . THR A 1 854 ? -58.514 -8.540  -41.757 1.00 18.40  ? 854  THR A CG2 1 
ATOM   6811 N N   . ASP A 1 855 ? -56.520 -7.625  -44.307 1.00 24.93  ? 855  ASP A N   1 
ATOM   6812 C CA  . ASP A 1 855 ? -56.470 -7.843  -45.753 1.00 26.77  ? 855  ASP A CA  1 
ATOM   6813 C C   . ASP A 1 855 ? -56.098 -6.512  -46.436 1.00 26.68  ? 855  ASP A C   1 
ATOM   6814 O O   . ASP A 1 855 ? -56.749 -6.029  -47.375 1.00 25.82  ? 855  ASP A O   1 
ATOM   6815 C CB  . ASP A 1 855 ? -57.794 -8.434  -46.251 1.00 26.44  ? 855  ASP A CB  1 
ATOM   6816 C CG  . ASP A 1 855 ? -57.712 -8.950  -47.680 1.00 31.45  ? 855  ASP A CG  1 
ATOM   6817 O OD1 . ASP A 1 855 ? -56.586 -9.318  -48.117 1.00 34.38  ? 855  ASP A OD1 1 
ATOM   6818 O OD2 . ASP A 1 855 ? -58.783 -8.975  -48.364 1.00 33.47  ? 855  ASP A OD2 1 
ATOM   6819 N N   . ILE A 1 856 ? -55.037 -5.909  -45.908 1.00 26.45  ? 856  ILE A N   1 
ATOM   6820 C CA  . ILE A 1 856 ? -54.617 -4.614  -46.351 1.00 27.36  ? 856  ILE A CA  1 
ATOM   6821 C C   . ILE A 1 856 ? -53.108 -4.730  -46.467 1.00 26.40  ? 856  ILE A C   1 
ATOM   6822 O O   . ILE A 1 856 ? -52.503 -5.564  -45.803 1.00 25.85  ? 856  ILE A O   1 
ATOM   6823 C CB  . ILE A 1 856 ? -55.156 -3.498  -45.358 1.00 27.31  ? 856  ILE A CB  1 
ATOM   6824 C CG1 . ILE A 1 856 ? -55.143 -2.113  -45.976 1.00 29.15  ? 856  ILE A CG1 1 
ATOM   6825 C CG2 . ILE A 1 856 ? -54.423 -3.501  -44.017 1.00 28.64  ? 856  ILE A CG2 1 
ATOM   6826 C CD1 . ILE A 1 856 ? -55.645 -0.990  -45.005 1.00 30.67  ? 856  ILE A CD1 1 
ATOM   6827 N N   . ASP A 1 857 ? -52.515 -3.936  -47.337 1.00 26.40  ? 857  ASP A N   1 
ATOM   6828 C CA  . ASP A 1 857 ? -51.073 -3.991  -47.531 1.00 27.81  ? 857  ASP A CA  1 
ATOM   6829 C C   . ASP A 1 857 ? -50.583 -2.580  -47.824 1.00 26.29  ? 857  ASP A C   1 
ATOM   6830 O O   . ASP A 1 857 ? -50.443 -2.203  -48.982 1.00 27.86  ? 857  ASP A O   1 
ATOM   6831 C CB  . ASP A 1 857 ? -50.793 -4.946  -48.695 1.00 28.93  ? 857  ASP A CB  1 
ATOM   6832 C CG  . ASP A 1 857 ? -49.341 -5.160  -48.936 1.00 34.06  ? 857  ASP A CG  1 
ATOM   6833 O OD1 . ASP A 1 857 ? -48.623 -5.604  -48.007 1.00 39.38  ? 857  ASP A OD1 1 
ATOM   6834 O OD2 . ASP A 1 857 ? -48.920 -4.896  -50.077 1.00 41.75  ? 857  ASP A OD2 1 
ATOM   6835 N N   . LEU A 1 858 ? -50.339 -1.778  -46.781 1.00 24.37  ? 858  LEU A N   1 
ATOM   6836 C CA  . LEU A 1 858 ? -49.911 -0.405  -46.966 1.00 22.05  ? 858  LEU A CA  1 
ATOM   6837 C C   . LEU A 1 858 ? -48.414 -0.358  -46.877 1.00 22.62  ? 858  LEU A C   1 
ATOM   6838 O O   . LEU A 1 858 ? -47.853 -0.444  -45.785 1.00 22.11  ? 858  LEU A O   1 
ATOM   6839 C CB  . LEU A 1 858 ? -50.508 0.502   -45.896 1.00 22.73  ? 858  LEU A CB  1 
ATOM   6840 C CG  . LEU A 1 858 ? -52.017 0.405   -45.580 1.00 22.44  ? 858  LEU A CG  1 
ATOM   6841 C CD1 . LEU A 1 858 ? -52.371 1.512   -44.638 1.00 23.27  ? 858  LEU A CD1 1 
ATOM   6842 C CD2 . LEU A 1 858 ? -52.833 0.527   -46.857 1.00 23.54  ? 858  LEU A CD2 1 
ATOM   6843 N N   . LEU A 1 859 ? -47.752 -0.247  -48.017 1.00 21.36  ? 859  LEU A N   1 
ATOM   6844 C CA  . LEU A 1 859 ? -46.304 -0.392  -48.022 1.00 21.41  ? 859  LEU A CA  1 
ATOM   6845 C C   . LEU A 1 859 ? -45.645 0.704   -47.196 1.00 21.62  ? 859  LEU A C   1 
ATOM   6846 O O   . LEU A 1 859 ? -45.951 1.886   -47.326 1.00 20.25  ? 859  LEU A O   1 
ATOM   6847 C CB  . LEU A 1 859 ? -45.768 -0.371  -49.452 1.00 20.80  ? 859  LEU A CB  1 
ATOM   6848 C CG  . LEU A 1 859 ? -46.365 -1.430  -50.404 1.00 22.53  ? 859  LEU A CG  1 
ATOM   6849 C CD1 . LEU A 1 859 ? -45.980 -1.096  -51.843 1.00 25.29  ? 859  LEU A CD1 1 
ATOM   6850 C CD2 . LEU A 1 859 ? -45.965 -2.874  -50.040 1.00 24.53  ? 859  LEU A CD2 1 
ATOM   6851 N N   . LEU A 1 860 ? -44.738 0.289   -46.328 1.00 22.27  ? 860  LEU A N   1 
ATOM   6852 C CA  . LEU A 1 860 ? -43.929 1.229   -45.582 1.00 23.51  ? 860  LEU A CA  1 
ATOM   6853 C C   . LEU A 1 860 ? -43.200 2.184   -46.533 1.00 23.87  ? 860  LEU A C   1 
ATOM   6854 O O   . LEU A 1 860 ? -42.572 1.756   -47.514 1.00 25.32  ? 860  LEU A O   1 
ATOM   6855 C CB  . LEU A 1 860 ? -42.922 0.443   -44.721 1.00 23.54  ? 860  LEU A CB  1 
ATOM   6856 C CG  . LEU A 1 860 ? -42.208 1.216   -43.631 1.00 24.57  ? 860  LEU A CG  1 
ATOM   6857 C CD1 . LEU A 1 860 ? -43.158 1.717   -42.574 1.00 25.80  ? 860  LEU A CD1 1 
ATOM   6858 C CD2 . LEU A 1 860 ? -41.138 0.330   -43.035 1.00 27.60  ? 860  LEU A CD2 1 
ATOM   6859 N N   . GLY A 1 861 ? -43.323 3.471   -46.286 1.00 22.55  ? 861  GLY A N   1 
ATOM   6860 C CA  . GLY A 1 861 ? -42.684 4.432   -47.156 1.00 23.11  ? 861  GLY A CA  1 
ATOM   6861 C C   . GLY A 1 861 ? -43.578 5.019   -48.224 1.00 23.62  ? 861  GLY A C   1 
ATOM   6862 O O   . GLY A 1 861 ? -43.138 5.849   -48.989 1.00 25.24  ? 861  GLY A O   1 
ATOM   6863 N N   . GLU A 1 862 ? -44.845 4.620   -48.268 1.00 22.17  ? 862  GLU A N   1 
ATOM   6864 C CA  . GLU A 1 862 ? -45.763 5.122   -49.286 1.00 21.83  ? 862  GLU A CA  1 
ATOM   6865 C C   . GLU A 1 862 ? -46.889 5.863   -48.575 1.00 21.47  ? 862  GLU A C   1 
ATOM   6866 O O   . GLU A 1 862 ? -47.254 5.502   -47.469 1.00 20.45  ? 862  GLU A O   1 
ATOM   6867 C CB  . GLU A 1 862 ? -46.394 3.962   -50.094 1.00 22.87  ? 862  GLU A CB  1 
ATOM   6868 C CG  . GLU A 1 862 ? -45.510 3.253   -51.112 1.00 24.33  ? 862  GLU A CG  1 
ATOM   6869 C CD  . GLU A 1 862 ? -44.955 4.220   -52.126 1.00 30.74  ? 862  GLU A CD  1 
ATOM   6870 O OE1 . GLU A 1 862 ? -45.748 4.885   -52.838 1.00 32.32  ? 862  GLU A OE1 1 
ATOM   6871 O OE2 . GLU A 1 862 ? -43.712 4.334   -52.206 1.00 31.37  ? 862  GLU A OE2 1 
ATOM   6872 N N   . ALA A 1 863 ? -47.459 6.852   -49.249 1.00 20.80  ? 863  ALA A N   1 
ATOM   6873 C CA  . ALA A 1 863 ? -48.542 7.668   -48.702 1.00 20.89  ? 863  ALA A CA  1 
ATOM   6874 C C   . ALA A 1 863 ? -49.883 7.036   -49.018 1.00 21.56  ? 863  ALA A C   1 
ATOM   6875 O O   . ALA A 1 863 ? -50.109 6.575   -50.150 1.00 21.47  ? 863  ALA A O   1 
ATOM   6876 C CB  . ALA A 1 863 ? -48.497 9.031   -49.316 1.00 20.89  ? 863  ALA A CB  1 
ATOM   6877 N N   . TYR A 1 864 ? -50.773 7.031   -48.028 1.00 21.14  ? 864  TYR A N   1 
ATOM   6878 C CA  . TYR A 1 864 ? -52.061 6.375   -48.166 1.00 21.53  ? 864  TYR A CA  1 
ATOM   6879 C C   . TYR A 1 864 ? -53.089 7.207   -47.432 1.00 22.11  ? 864  TYR A C   1 
ATOM   6880 O O   . TYR A 1 864 ? -52.745 7.947   -46.516 1.00 20.83  ? 864  TYR A O   1 
ATOM   6881 C CB  . TYR A 1 864 ? -52.072 4.974   -47.538 1.00 20.41  ? 864  TYR A CB  1 
ATOM   6882 C CG  . TYR A 1 864 ? -51.267 3.964   -48.275 1.00 20.29  ? 864  TYR A CG  1 
ATOM   6883 C CD1 . TYR A 1 864 ? -51.777 3.310   -49.401 1.00 18.27  ? 864  TYR A CD1 1 
ATOM   6884 C CD2 . TYR A 1 864 ? -49.956 3.667   -47.856 1.00 19.59  ? 864  TYR A CD2 1 
ATOM   6885 C CE1 . TYR A 1 864 ? -51.015 2.372   -50.083 1.00 20.19  ? 864  TYR A CE1 1 
ATOM   6886 C CE2 . TYR A 1 864 ? -49.186 2.754   -48.552 1.00 16.62  ? 864  TYR A CE2 1 
ATOM   6887 C CZ  . TYR A 1 864 ? -49.698 2.115   -49.640 1.00 19.55  ? 864  TYR A CZ  1 
ATOM   6888 O OH  . TYR A 1 864 ? -48.910 1.196   -50.281 1.00 20.80  ? 864  TYR A OH  1 
ATOM   6889 N N   . THR A 1 865 ? -54.348 7.072   -47.852 1.00 23.92  ? 865  THR A N   1 
ATOM   6890 C CA  . THR A 1 865 ? -55.481 7.551   -47.090 1.00 26.43  ? 865  THR A CA  1 
ATOM   6891 C C   . THR A 1 865 ? -56.402 6.342   -46.870 1.00 26.50  ? 865  THR A C   1 
ATOM   6892 O O   . THR A 1 865 ? -56.625 5.576   -47.781 1.00 28.19  ? 865  THR A O   1 
ATOM   6893 C CB  . THR A 1 865 ? -56.203 8.696   -47.853 1.00 26.72  ? 865  THR A CB  1 
ATOM   6894 O OG1 . THR A 1 865 ? -55.256 9.753   -48.124 1.00 30.01  ? 865  THR A OG1 1 
ATOM   6895 C CG2 . THR A 1 865 ? -57.313 9.274   -47.008 1.00 29.11  ? 865  THR A CG2 1 
ATOM   6896 N N   . VAL A 1 866 ? -56.873 6.113   -45.651 1.00 26.58  ? 866  VAL A N   1 
ATOM   6897 C CA  . VAL A 1 866 ? -57.862 5.065   -45.433 1.00 26.07  ? 866  VAL A CA  1 
ATOM   6898 C C   . VAL A 1 866 ? -59.063 5.823   -44.902 1.00 26.75  ? 866  VAL A C   1 
ATOM   6899 O O   . VAL A 1 866 ? -58.930 6.579   -43.944 1.00 26.09  ? 866  VAL A O   1 
ATOM   6900 C CB  . VAL A 1 866 ? -57.387 3.981   -44.442 1.00 25.59  ? 866  VAL A CB  1 
ATOM   6901 C CG1 . VAL A 1 866 ? -58.429 2.884   -44.262 1.00 26.33  ? 866  VAL A CG1 1 
ATOM   6902 C CG2 . VAL A 1 866 ? -56.027 3.375   -44.903 1.00 24.86  ? 866  VAL A CG2 1 
ATOM   6903 N N   . GLU A 1 867 ? -60.221 5.636   -45.534 1.00 27.45  ? 867  GLU A N   1 
ATOM   6904 C CA  . GLU A 1 867 ? -61.411 6.408   -45.182 1.00 29.73  ? 867  GLU A CA  1 
ATOM   6905 C C   . GLU A 1 867 ? -62.545 5.467   -44.869 1.00 28.53  ? 867  GLU A C   1 
ATOM   6906 O O   . GLU A 1 867 ? -62.620 4.392   -45.430 1.00 27.98  ? 867  GLU A O   1 
ATOM   6907 C CB  . GLU A 1 867 ? -61.820 7.321   -46.343 1.00 29.38  ? 867  GLU A CB  1 
ATOM   6908 C CG  . GLU A 1 867 ? -60.869 8.508   -46.575 1.00 33.99  ? 867  GLU A CG  1 
ATOM   6909 C CD  . GLU A 1 867 ? -61.301 9.404   -47.742 1.00 34.60  ? 867  GLU A CD  1 
ATOM   6910 O OE1 . GLU A 1 867 ? -61.065 9.018   -48.918 1.00 38.21  ? 867  GLU A OE1 1 
ATOM   6911 O OE2 . GLU A 1 867 ? -61.861 10.499  -47.460 1.00 41.05  ? 867  GLU A OE2 1 
ATOM   6912 N N   . TRP A 1 868 ? -63.419 5.868   -43.958 1.00 29.54  ? 868  TRP A N   1 
ATOM   6913 C CA  . TRP A 1 868 ? -64.591 5.071   -43.653 1.00 30.62  ? 868  TRP A CA  1 
ATOM   6914 C C   . TRP A 1 868 ? -65.777 5.956   -43.320 1.00 31.82  ? 868  TRP A C   1 
ATOM   6915 O O   . TRP A 1 868 ? -65.634 7.155   -43.071 1.00 31.04  ? 868  TRP A O   1 
ATOM   6916 C CB  . TRP A 1 868 ? -64.313 4.091   -42.503 1.00 29.68  ? 868  TRP A CB  1 
ATOM   6917 C CG  . TRP A 1 868 ? -63.873 4.722   -41.236 1.00 29.79  ? 868  TRP A CG  1 
ATOM   6918 C CD1 . TRP A 1 868 ? -64.663 5.099   -40.191 1.00 29.61  ? 868  TRP A CD1 1 
ATOM   6919 C CD2 . TRP A 1 868 ? -62.529 5.051   -40.867 1.00 29.53  ? 868  TRP A CD2 1 
ATOM   6920 N NE1 . TRP A 1 868 ? -63.895 5.641   -39.183 1.00 28.41  ? 868  TRP A NE1 1 
ATOM   6921 C CE2 . TRP A 1 868 ? -62.580 5.631   -39.583 1.00 30.06  ? 868  TRP A CE2 1 
ATOM   6922 C CE3 . TRP A 1 868 ? -61.282 4.896   -41.497 1.00 29.02  ? 868  TRP A CE3 1 
ATOM   6923 C CZ2 . TRP A 1 868 ? -61.430 6.057   -38.905 1.00 30.18  ? 868  TRP A CZ2 1 
ATOM   6924 C CZ3 . TRP A 1 868 ? -60.137 5.327   -40.827 1.00 27.28  ? 868  TRP A CZ3 1 
ATOM   6925 C CH2 . TRP A 1 868 ? -60.223 5.905   -39.544 1.00 28.58  ? 868  TRP A CH2 1 
ATOM   6926 N N   . ALA A 1 869 ? -66.952 5.349   -43.320 1.00 33.97  ? 869  ALA A N   1 
ATOM   6927 C CA  . ALA A 1 869 ? -68.168 6.023   -42.902 1.00 35.91  ? 869  ALA A CA  1 
ATOM   6928 C C   . ALA A 1 869 ? -68.639 5.330   -41.629 1.00 37.88  ? 869  ALA A C   1 
ATOM   6929 O O   . ALA A 1 869 ? -68.021 4.356   -41.172 1.00 37.11  ? 869  ALA A O   1 
ATOM   6930 C CB  . ALA A 1 869 ? -69.205 5.920   -43.981 1.00 36.14  ? 869  ALA A CB  1 
ATOM   6931 N N   . HIS A 1 870 ? -69.710 5.852   -41.040 1.00 39.74  ? 870  HIS A N   1 
ATOM   6932 C CA  . HIS A 1 870 ? -70.301 5.238   -39.862 1.00 41.81  ? 870  HIS A CA  1 
ATOM   6933 C C   . HIS A 1 870 ? -71.758 4.837   -40.115 1.00 42.68  ? 870  HIS A C   1 
ATOM   6934 O O   . HIS A 1 870 ? -72.667 5.655   -39.984 1.00 44.15  ? 870  HIS A O   1 
ATOM   6935 C CB  . HIS A 1 870 ? -70.178 6.173   -38.666 1.00 42.39  ? 870  HIS A CB  1 
ATOM   6936 C CG  . HIS A 1 870 ? -68.778 6.315   -38.162 1.00 44.13  ? 870  HIS A CG  1 
ATOM   6937 N ND1 . HIS A 1 870 ? -68.124 5.301   -37.493 1.00 45.72  ? 870  HIS A ND1 1 
ATOM   6938 C CD2 . HIS A 1 870 ? -67.904 7.348   -38.225 1.00 45.96  ? 870  HIS A CD2 1 
ATOM   6939 C CE1 . HIS A 1 870 ? -66.910 5.706   -37.163 1.00 46.14  ? 870  HIS A CE1 1 
ATOM   6940 N NE2 . HIS A 1 870 ? -66.751 6.944   -37.595 1.00 46.01  ? 870  HIS A NE2 1 
HETATM 6941 C C1A . ACR B 2 .   ? -19.671 -5.990  -10.611 1.00 27.17  ? 1001 ACR A C1A 1 
HETATM 6942 C C2A . ACR B 2 .   ? -20.730 -5.683  -11.690 1.00 24.26  ? 1001 ACR A C2A 1 
HETATM 6943 C C3A . ACR B 2 .   ? -21.560 -6.936  -11.971 1.00 23.98  ? 1001 ACR A C3A 1 
HETATM 6944 C C4A . ACR B 2 .   ? -20.667 -7.964  -12.639 1.00 21.49  ? 1001 ACR A C4A 1 
HETATM 6945 C C5A . ACR B 2 .   ? -19.347 -8.105  -11.911 1.00 22.16  ? 1001 ACR A C5A 1 
HETATM 6946 C C6A . ACR B 2 .   ? -18.589 -9.368  -12.180 1.00 23.23  ? 1001 ACR A C6A 1 
HETATM 6947 C C7A . ACR B 2 .   ? -18.833 -7.168  -11.099 1.00 22.16  ? 1001 ACR A C7A 1 
HETATM 6948 O O2A . ACR B 2 .   ? -21.598 -4.643  -11.261 1.00 25.02  ? 1001 ACR A O2A 1 
HETATM 6949 O O3A . ACR B 2 .   ? -22.795 -6.725  -12.743 1.00 18.66  ? 1001 ACR A O3A 1 
HETATM 6950 O O4A . ACR B 2 .   ? -21.341 -9.222  -12.655 1.00 24.78  ? 1001 ACR A O4A 1 
HETATM 6951 O O6A . ACR B 2 .   ? -17.857 -9.052  -13.380 1.00 26.24  ? 1001 ACR A O6A 1 
HETATM 6952 C C1B . ACR B 2 .   ? -18.217 -6.743  -5.386  1.00 30.43  ? 1001 ACR A C1B 1 
HETATM 6953 C C2B . ACR B 2 .   ? -17.840 -5.556  -6.271  1.00 30.34  ? 1001 ACR A C2B 1 
HETATM 6954 C C3B . ACR B 2 .   ? -18.974 -5.248  -7.262  1.00 27.16  ? 1001 ACR A C3B 1 
HETATM 6955 C C4B . ACR B 2 .   ? -19.240 -6.467  -8.146  1.00 27.94  ? 1001 ACR A C4B 1 
HETATM 6956 C C5B . ACR B 2 .   ? -19.594 -7.651  -7.221  1.00 28.48  ? 1001 ACR A C5B 1 
HETATM 6957 C C6B . ACR B 2 .   ? -19.763 -8.957  -7.990  1.00 28.96  ? 1001 ACR A C6B 1 
HETATM 6958 N N4B . ACR B 2 .   ? -20.200 -6.177  -9.233  1.00 28.16  ? 1001 ACR A N4B 1 
HETATM 6959 O O2B . ACR B 2 .   ? -17.624 -4.418  -5.439  1.00 28.67  ? 1001 ACR A O2B 1 
HETATM 6960 O O3B . ACR B 2 .   ? -18.618 -4.157  -8.104  1.00 27.80  ? 1001 ACR A O3B 1 
HETATM 6961 O O5B . ACR B 2 .   ? -18.541 -7.843  -6.242  1.00 27.94  ? 1001 ACR A O5B 1 
HETATM 6962 C C1C . ACR B 2 .   ? -21.057 -7.738  -0.958  1.00 48.71  ? 1001 ACR A C1C 1 
HETATM 6963 C C2C . ACR B 2 .   ? -19.534 -7.739  -1.040  1.00 46.42  ? 1001 ACR A C2C 1 
HETATM 6964 C C3C . ACR B 2 .   ? -19.020 -6.961  -2.255  1.00 44.64  ? 1001 ACR A C3C 1 
HETATM 6965 C C4C . ACR B 2 .   ? -19.722 -7.338  -3.560  1.00 42.22  ? 1001 ACR A C4C 1 
HETATM 6966 C C5C . ACR B 2 .   ? -21.242 -7.338  -3.363  1.00 45.44  ? 1001 ACR A C5C 1 
HETATM 6967 C C6C . ACR B 2 .   ? -21.995 -7.854  -4.585  1.00 46.16  ? 1001 ACR A C6C 1 
HETATM 6968 O O2C . ACR B 2 .   ? -19.040 -7.061  0.109   1.00 49.06  ? 1001 ACR A O2C 1 
HETATM 6969 O O3C . ACR B 2 .   ? -17.604 -7.128  -2.405  1.00 44.16  ? 1001 ACR A O3C 1 
HETATM 6970 O O4C . ACR B 2 .   ? -19.345 -6.391  -4.560  1.00 36.71  ? 1001 ACR A O4C 1 
HETATM 6971 O O5C . ACR B 2 .   ? -21.593 -8.154  -2.226  1.00 48.08  ? 1001 ACR A O5C 1 
HETATM 6972 O O6C . ACR B 2 .   ? -23.397 -7.936  -4.288  1.00 47.81  ? 1001 ACR A O6C 1 
HETATM 6973 C C1D . ACR B 2 .   ? -24.436 -4.540  1.835   1.00 58.11  ? 1001 ACR A C1D 1 
HETATM 6974 C C2D . ACR B 2 .   ? -22.960 -4.623  2.306   1.00 58.20  ? 1001 ACR A C2D 1 
HETATM 6975 C C3D . ACR B 2 .   ? -21.993 -5.060  1.199   1.00 57.23  ? 1001 ACR A C3D 1 
HETATM 6976 C C4D . ACR B 2 .   ? -22.487 -6.269  0.398   1.00 54.84  ? 1001 ACR A C4D 1 
HETATM 6977 C C5D . ACR B 2 .   ? -23.907 -5.941  -0.121  1.00 55.11  ? 1001 ACR A C5D 1 
HETATM 6978 C C6D . ACR B 2 .   ? -24.541 -7.046  -0.971  1.00 54.21  ? 1001 ACR A C6D 1 
HETATM 6979 O O1D . ACR B 2 .   ? -24.725 -3.278  1.208   1.00 59.32  ? 1001 ACR A O1D 1 
HETATM 6980 O O2D . ACR B 2 .   ? -22.490 -3.360  2.819   1.00 59.17  ? 1001 ACR A O2D 1 
HETATM 6981 O O3D . ACR B 2 .   ? -20.679 -5.312  1.738   1.00 58.19  ? 1001 ACR A O3D 1 
HETATM 6982 O O4D . ACR B 2 .   ? -21.517 -6.416  -0.648  1.00 51.12  ? 1001 ACR A O4D 1 
HETATM 6983 O O5D . ACR B 2 .   ? -24.819 -5.618  0.955   1.00 55.98  ? 1001 ACR A O5D 1 
HETATM 6984 O O6D . ACR B 2 .   ? -25.849 -6.622  -1.396  1.00 52.98  ? 1001 ACR A O6D 1 
HETATM 6985 C C1  A NAG C 3 .   ? -39.030 -15.899 -36.871 0.50 21.69  ? 2001 NAG A C1  1 
HETATM 6986 C C1  B NAG C 3 .   ? -39.076 -16.719 -34.686 0.50 26.71  ? 2001 NAG A C1  1 
HETATM 6987 C C2  A NAG C 3 .   ? -39.647 -16.019 -38.264 0.50 21.78  ? 2001 NAG A C2  1 
HETATM 6988 C C2  B NAG C 3 .   ? -39.606 -18.100 -34.291 0.50 28.21  ? 2001 NAG A C2  1 
HETATM 6989 C C3  A NAG C 3 .   ? -39.279 -17.396 -38.876 0.50 23.80  ? 2001 NAG A C3  1 
HETATM 6990 C C3  B NAG C 3 .   ? -38.572 -19.112 -34.713 0.50 29.28  ? 2001 NAG A C3  1 
HETATM 6991 C C4  A NAG C 3 .   ? -37.776 -17.702 -38.786 0.50 23.65  ? 2001 NAG A C4  1 
HETATM 6992 C C4  B NAG C 3 .   ? -38.635 -19.131 -36.229 0.50 29.79  ? 2001 NAG A C4  1 
HETATM 6993 C C5  A NAG C 3 .   ? -37.242 -17.411 -37.385 0.50 24.41  ? 2001 NAG A C5  1 
HETATM 6994 C C5  B NAG C 3 .   ? -38.344 -17.755 -36.819 0.50 29.08  ? 2001 NAG A C5  1 
HETATM 6995 C C6  A NAG C 3 .   ? -35.724 -17.590 -37.322 0.50 24.33  ? 2001 NAG A C6  1 
HETATM 6996 C C6  B NAG C 3 .   ? -38.929 -17.747 -38.228 0.50 27.90  ? 2001 NAG A C6  1 
HETATM 6997 C C7  A NAG C 3 .   ? -41.978 -14.972 -38.131 0.50 24.99  ? 2001 NAG A C7  1 
HETATM 6998 C C7  B NAG C 3 .   ? -41.139 -18.242 -32.372 0.50 27.94  ? 2001 NAG A C7  1 
HETATM 6999 C C8  A NAG C 3 .   ? -42.334 -14.416 -36.771 0.50 25.31  ? 2001 NAG A C8  1 
HETATM 7000 C C8  B NAG C 3 .   ? -41.988 -17.066 -32.764 0.50 26.29  ? 2001 NAG A C8  1 
HETATM 7001 N N2  A NAG C 3 .   ? -41.096 -15.983 -38.173 0.50 23.26  ? 2001 NAG A N2  1 
HETATM 7002 N N2  B NAG C 3 .   ? -39.906 -18.268 -32.879 0.50 25.46  ? 2001 NAG A N2  1 
HETATM 7003 O O3  A NAG C 3 .   ? -39.712 -17.501 -40.225 0.50 20.87  ? 2001 NAG A O3  1 
HETATM 7004 O O3  B NAG C 3 .   ? -38.959 -20.361 -34.220 0.50 31.87  ? 2001 NAG A O3  1 
HETATM 7005 O O4  A NAG C 3 .   ? -37.500 -19.050 -39.103 0.50 27.00  ? 2001 NAG A O4  1 
HETATM 7006 O O4  B NAG C 3 .   ? -37.755 -20.099 -36.767 0.50 31.44  ? 2001 NAG A O4  1 
HETATM 7007 O O5  A NAG C 3 .   ? -37.625 -16.094 -37.016 0.50 23.26  ? 2001 NAG A O5  1 
HETATM 7008 O O5  B NAG C 3 .   ? -38.894 -16.644 -36.099 0.50 25.89  ? 2001 NAG A O5  1 
HETATM 7009 O O6  A NAG C 3 .   ? -35.379 -17.914 -35.994 0.50 27.89  ? 2001 NAG A O6  1 
HETATM 7010 O O6  B NAG C 3 .   ? -37.888 -17.641 -39.175 0.50 26.69  ? 2001 NAG A O6  1 
HETATM 7011 O O7  A NAG C 3 .   ? -42.561 -14.567 -39.143 0.50 26.25  ? 2001 NAG A O7  1 
HETATM 7012 O O7  B NAG C 3 .   ? -41.576 -19.113 -31.604 0.50 25.94  ? 2001 NAG A O7  1 
HETATM 7013 C C1  . NAG D 3 .   ? -26.869 0.395   4.878   1.00 42.52  ? 2005 NAG A C1  1 
HETATM 7014 C C2  . NAG D 3 .   ? -27.828 -0.785  4.663   1.00 45.29  ? 2005 NAG A C2  1 
HETATM 7015 C C3  . NAG D 3 .   ? -27.405 -2.026  5.473   1.00 47.00  ? 2005 NAG A C3  1 
HETATM 7016 C C4  . NAG D 3 .   ? -25.898 -2.322  5.411   1.00 48.67  ? 2005 NAG A C4  1 
HETATM 7017 C C5  . NAG D 3 .   ? -25.162 -1.063  5.848   1.00 48.89  ? 2005 NAG A C5  1 
HETATM 7018 C C6  . NAG D 3 .   ? -23.635 -1.218  5.864   1.00 50.77  ? 2005 NAG A C6  1 
HETATM 7019 C C7  . NAG D 3 .   ? -30.201 -0.201  4.099   1.00 44.07  ? 2005 NAG A C7  1 
HETATM 7020 C C8  . NAG D 3 .   ? -31.485 0.359   4.651   1.00 44.29  ? 2005 NAG A C8  1 
HETATM 7021 N N2  . NAG D 3 .   ? -29.206 -0.400  4.975   1.00 44.50  ? 2005 NAG A N2  1 
HETATM 7022 O O3  . NAG D 3 .   ? -28.101 -3.155  4.994   1.00 48.18  ? 2005 NAG A O3  1 
HETATM 7023 O O4  . NAG D 3 .   ? -25.546 -3.449  6.208   1.00 51.16  ? 2005 NAG A O4  1 
HETATM 7024 O O5  . NAG D 3 .   ? -25.526 -0.056  4.913   1.00 46.83  ? 2005 NAG A O5  1 
HETATM 7025 O O6  . NAG D 3 .   ? -23.042 -0.125  6.551   1.00 52.73  ? 2005 NAG A O6  1 
HETATM 7026 O O7  . NAG D 3 .   ? -30.132 -0.443  2.893   1.00 43.35  ? 2005 NAG A O7  1 
HETATM 7027 S S   . SO4 E 4 .   ? -38.965 39.629  -28.868 1.00 38.60  ? 4001 SO4 A S   1 
HETATM 7028 O O1  . SO4 E 4 .   ? -37.929 39.764  -29.881 1.00 40.45  ? 4001 SO4 A O1  1 
HETATM 7029 O O2  . SO4 E 4 .   ? -40.260 39.228  -29.397 1.00 40.07  ? 4001 SO4 A O2  1 
HETATM 7030 O O3  . SO4 E 4 .   ? -38.503 38.646  -27.911 1.00 41.85  ? 4001 SO4 A O3  1 
HETATM 7031 O O4  . SO4 E 4 .   ? -39.111 40.853  -28.103 1.00 41.83  ? 4001 SO4 A O4  1 
HETATM 7032 C C1  . GOL F 5 .   ? -21.747 25.546  -28.426 1.00 40.42  ? 3001 GOL A C1  1 
HETATM 7033 O O1  . GOL F 5 .   ? -21.113 26.390  -29.358 1.00 46.73  ? 3001 GOL A O1  1 
HETATM 7034 C C2  . GOL F 5 .   ? -21.644 26.200  -27.060 1.00 40.67  ? 3001 GOL A C2  1 
HETATM 7035 O O2  . GOL F 5 .   ? -22.613 27.241  -26.984 1.00 39.99  ? 3001 GOL A O2  1 
HETATM 7036 C C3  . GOL F 5 .   ? -21.851 25.137  -25.979 1.00 37.47  ? 3001 GOL A C3  1 
HETATM 7037 O O3  . GOL F 5 .   ? -21.254 23.919  -26.385 1.00 35.51  ? 3001 GOL A O3  1 
HETATM 7038 C C1  . GOL G 5 .   ? -26.998 2.069   -26.423 1.00 27.87  ? 3002 GOL A C1  1 
HETATM 7039 O O1  . GOL G 5 .   ? -26.080 2.217   -27.478 1.00 28.75  ? 3002 GOL A O1  1 
HETATM 7040 C C2  . GOL G 5 .   ? -27.290 3.446   -25.817 1.00 29.57  ? 3002 GOL A C2  1 
HETATM 7041 O O2  . GOL G 5 .   ? -26.143 4.268   -25.918 1.00 31.00  ? 3002 GOL A O2  1 
HETATM 7042 C C3  . GOL G 5 .   ? -28.426 4.108   -26.600 1.00 29.77  ? 3002 GOL A C3  1 
HETATM 7043 O O3  . GOL G 5 .   ? -28.702 5.388   -26.060 1.00 31.16  ? 3002 GOL A O3  1 
HETATM 7044 C C1  . GOL H 5 .   ? -27.927 -25.004 -15.472 1.00 36.95  ? 3003 GOL A C1  1 
HETATM 7045 O O1  . GOL H 5 .   ? -29.117 -25.326 -14.779 1.00 39.82  ? 3003 GOL A O1  1 
HETATM 7046 C C2  . GOL H 5 .   ? -27.427 -23.656 -14.991 1.00 37.02  ? 3003 GOL A C2  1 
HETATM 7047 O O2  . GOL H 5 .   ? -27.557 -23.618 -13.590 1.00 37.54  ? 3003 GOL A O2  1 
HETATM 7048 C C3  . GOL H 5 .   ? -25.953 -23.535 -15.355 1.00 35.04  ? 3003 GOL A C3  1 
HETATM 7049 O O3  . GOL H 5 .   ? -25.493 -22.214 -15.139 1.00 32.62  ? 3003 GOL A O3  1 
HETATM 7050 C C1  . GOL I 5 .   ? -26.180 7.600   -34.949 1.00 45.26  ? 3004 GOL A C1  1 
HETATM 7051 O O1  . GOL I 5 .   ? -26.122 6.187   -34.844 1.00 41.65  ? 3004 GOL A O1  1 
HETATM 7052 C C2  . GOL I 5 .   ? -26.949 8.049   -36.197 1.00 44.10  ? 3004 GOL A C2  1 
HETATM 7053 O O2  . GOL I 5 .   ? -27.995 7.139   -36.449 1.00 43.04  ? 3004 GOL A O2  1 
HETATM 7054 C C3  . GOL I 5 .   ? -27.458 9.487   -36.091 1.00 44.35  ? 3004 GOL A C3  1 
HETATM 7055 O O3  . GOL I 5 .   ? -26.480 10.495  -36.245 1.00 43.10  ? 3004 GOL A O3  1 
HETATM 7056 C C1  . GOL J 5 .   ? -24.039 -5.765  -34.919 1.00 45.62  ? 3005 GOL A C1  1 
HETATM 7057 O O1  . GOL J 5 .   ? -24.941 -4.686  -35.079 1.00 43.74  ? 3005 GOL A O1  1 
HETATM 7058 C C2  . GOL J 5 .   ? -22.654 -5.130  -34.837 1.00 45.56  ? 3005 GOL A C2  1 
HETATM 7059 O O2  . GOL J 5 .   ? -22.377 -4.766  -33.496 1.00 40.33  ? 3005 GOL A O2  1 
HETATM 7060 C C3  . GOL J 5 .   ? -21.614 -6.069  -35.442 1.00 45.99  ? 3005 GOL A C3  1 
HETATM 7061 O O3  . GOL J 5 .   ? -21.377 -7.170  -34.580 1.00 45.37  ? 3005 GOL A O3  1 
HETATM 7062 C C1  . GOL K 5 .   ? -27.133 43.082  -14.342 1.00 40.13  ? 3006 GOL A C1  1 
HETATM 7063 O O1  . GOL K 5 .   ? -28.179 43.244  -13.403 1.00 38.41  ? 3006 GOL A O1  1 
HETATM 7064 C C2  . GOL K 5 .   ? -27.575 42.352  -15.606 1.00 41.71  ? 3006 GOL A C2  1 
HETATM 7065 O O2  . GOL K 5 .   ? -28.568 43.069  -16.300 1.00 43.34  ? 3006 GOL A O2  1 
HETATM 7066 C C3  . GOL K 5 .   ? -26.388 42.341  -16.549 1.00 42.02  ? 3006 GOL A C3  1 
HETATM 7067 O O3  . GOL K 5 .   ? -26.132 43.639  -17.029 1.00 39.69  ? 3006 GOL A O3  1 
HETATM 7068 C C1  . GOL L 5 .   ? -50.712 -14.563 -5.551  1.00 42.26  ? 3007 GOL A C1  1 
HETATM 7069 O O1  . GOL L 5 .   ? -51.532 -13.711 -4.777  1.00 47.18  ? 3007 GOL A O1  1 
HETATM 7070 C C2  . GOL L 5 .   ? -49.389 -13.853 -5.807  1.00 38.78  ? 3007 GOL A C2  1 
HETATM 7071 O O2  . GOL L 5 .   ? -48.418 -14.802 -6.218  1.00 37.42  ? 3007 GOL A O2  1 
HETATM 7072 C C3  . GOL L 5 .   ? -49.621 -12.871 -6.941  1.00 36.13  ? 3007 GOL A C3  1 
HETATM 7073 O O3  . GOL L 5 .   ? -48.412 -12.739 -7.670  1.00 30.28  ? 3007 GOL A O3  1 
HETATM 7074 C C1  . GOL M 5 .   ? -53.676 -4.054  -19.009 1.00 48.21  ? 3008 GOL A C1  1 
HETATM 7075 O O1  . GOL M 5 .   ? -53.498 -4.392  -17.666 1.00 51.39  ? 3008 GOL A O1  1 
HETATM 7076 C C2  . GOL M 5 .   ? -53.412 -5.282  -19.868 1.00 47.72  ? 3008 GOL A C2  1 
HETATM 7077 O O2  . GOL M 5 .   ? -53.837 -4.996  -21.178 1.00 47.43  ? 3008 GOL A O2  1 
HETATM 7078 C C3  . GOL M 5 .   ? -51.928 -5.623  -19.914 1.00 45.42  ? 3008 GOL A C3  1 
HETATM 7079 O O3  . GOL M 5 .   ? -51.780 -7.024  -19.937 1.00 43.70  ? 3008 GOL A O3  1 
HETATM 7080 C C1  . GOL N 5 .   ? -52.530 -16.204 -12.377 1.00 67.47  ? 3009 GOL A C1  1 
HETATM 7081 O O1  . GOL N 5 .   ? -52.982 -17.197 -13.276 1.00 67.10  ? 3009 GOL A O1  1 
HETATM 7082 C C2  . GOL N 5 .   ? -53.339 -16.263 -11.085 1.00 68.24  ? 3009 GOL A C2  1 
HETATM 7083 O O2  . GOL N 5 .   ? -52.847 -15.328 -10.138 1.00 68.02  ? 3009 GOL A O2  1 
HETATM 7084 C C3  . GOL N 5 .   ? -54.799 -15.960 -11.401 1.00 68.46  ? 3009 GOL A C3  1 
HETATM 7085 O O3  . GOL N 5 .   ? -55.465 -15.548 -10.226 1.00 69.65  ? 3009 GOL A O3  1 
HETATM 7086 C C1  . NAG O 3 .   ? 3.105   8.055   -16.836 1.00 28.02  ? 2003 NAG X C1  1 
HETATM 7087 C C2  . NAG O 3 .   ? 2.975   9.337   -17.667 1.00 30.06  ? 2003 NAG X C2  1 
HETATM 7088 C C3  . NAG O 3 .   ? 3.603   9.197   -19.066 1.00 31.67  ? 2003 NAG X C3  1 
HETATM 7089 C C4  . NAG O 3 .   ? 5.039   8.692   -19.003 1.00 32.48  ? 2003 NAG X C4  1 
HETATM 7090 C C5  . NAG O 3 .   ? 5.073   7.487   -18.071 1.00 31.20  ? 2003 NAG X C5  1 
HETATM 7091 C C6  . NAG O 3 .   ? 6.520   7.049   -17.862 1.00 29.24  ? 2003 NAG X C6  1 
HETATM 7092 C C7  . NAG O 3 .   ? 1.165   10.889  -17.292 1.00 32.80  ? 2003 NAG X C7  1 
HETATM 7093 C C8  . NAG O 3 .   ? -0.315  11.160  -17.378 1.00 33.56  ? 2003 NAG X C8  1 
HETATM 7094 N N2  . NAG O 3 .   ? 1.589   9.743   -17.789 1.00 31.58  ? 2003 NAG X N2  1 
HETATM 7095 O O3  . NAG O 3 .   ? 3.558   10.431  -19.720 1.00 28.34  ? 2003 NAG X O3  1 
HETATM 7096 O O4  . NAG O 3 .   ? 5.515   8.244   -20.267 1.00 39.56  ? 2003 NAG X O4  1 
HETATM 7097 O O5  . NAG O 3 .   ? 4.485   7.742   -16.807 1.00 28.87  ? 2003 NAG X O5  1 
HETATM 7098 O O6  . NAG O 3 .   ? 6.524   5.850   -17.112 1.00 32.53  ? 2003 NAG X O6  1 
HETATM 7099 O O7  . NAG O 3 .   ? 1.920   11.708  -16.776 1.00 35.25  ? 2003 NAG X O7  1 
HETATM 7100 C C1  . NAG P 3 .   ? 6.048   9.281   -21.115 1.00 44.54  ? 2004 NAG X C1  1 
HETATM 7101 C C2  . NAG P 3 .   ? 7.495   8.948   -21.500 1.00 47.18  ? 2004 NAG X C2  1 
HETATM 7102 C C3  . NAG P 3 .   ? 8.074   9.835   -22.598 1.00 49.16  ? 2004 NAG X C3  1 
HETATM 7103 C C4  . NAG P 3 .   ? 7.086   9.989   -23.754 1.00 49.84  ? 2004 NAG X C4  1 
HETATM 7104 C C5  . NAG P 3 .   ? 5.726   10.409  -23.179 1.00 49.17  ? 2004 NAG X C5  1 
HETATM 7105 C C6  . NAG P 3 .   ? 4.683   10.614  -24.273 1.00 49.35  ? 2004 NAG X C6  1 
HETATM 7106 C C7  . NAG P 3 .   ? 9.160   8.057   -20.001 1.00 51.79  ? 2004 NAG X C7  1 
HETATM 7107 C C8  . NAG P 3 .   ? 9.949   8.248   -18.733 1.00 52.06  ? 2004 NAG X C8  1 
HETATM 7108 N N2  . NAG P 3 .   ? 8.363   9.062   -20.355 1.00 49.64  ? 2004 NAG X N2  1 
HETATM 7109 O O3  . NAG P 3 .   ? 9.281   9.249   -23.042 1.00 49.97  ? 2004 NAG X O3  1 
HETATM 7110 O O4  . NAG P 3 .   ? 7.580   10.935  -24.698 1.00 52.89  ? 2004 NAG X O4  1 
HETATM 7111 O O5  . NAG P 3 .   ? 5.253   9.416   -22.270 1.00 46.23  ? 2004 NAG X O5  1 
HETATM 7112 O O6  . NAG P 3 .   ? 4.192   9.337   -24.611 1.00 48.98  ? 2004 NAG X O6  1 
HETATM 7113 O O7  . NAG P 3 .   ? 9.263   7.021   -20.665 1.00 53.47  ? 2004 NAG X O7  1 
HETATM 7114 O O   . HOH Q 6 .   ? -25.613 11.809  -20.971 1.00 14.30  ? 4002 HOH A O   1 
HETATM 7115 O O   . HOH Q 6 .   ? -29.825 -14.263 -14.863 1.00 17.71  ? 4003 HOH A O   1 
HETATM 7116 O O   . HOH Q 6 .   ? -15.340 33.607  -15.096 1.00 19.90  ? 4004 HOH A O   1 
HETATM 7117 O O   . HOH Q 6 .   ? -33.180 -3.763  -23.867 1.00 14.13  ? 4005 HOH A O   1 
HETATM 7118 O O   . HOH Q 6 .   ? -41.642 -6.857  -33.388 1.00 17.51  ? 4006 HOH A O   1 
HETATM 7119 O O   . HOH Q 6 .   ? -29.887 9.248   -9.416  1.00 19.88  ? 4007 HOH A O   1 
HETATM 7120 O O   . HOH Q 6 .   ? -23.556 6.010   -13.495 1.00 19.83  ? 4008 HOH A O   1 
HETATM 7121 O O   . HOH Q 6 .   ? -26.786 -0.049  -29.143 1.00 14.28  ? 4009 HOH A O   1 
HETATM 7122 O O   . HOH Q 6 .   ? -10.332 11.771  1.614   1.00 16.95  ? 4010 HOH A O   1 
HETATM 7123 O O   . HOH Q 6 .   ? -21.784 13.942  -24.554 1.00 13.07  ? 4011 HOH A O   1 
HETATM 7124 O O   . HOH Q 6 .   ? -35.456 12.807  -8.800  1.00 17.27  ? 4012 HOH A O   1 
HETATM 7125 O O   . HOH Q 6 .   ? -26.072 15.741  -15.021 1.00 16.97  ? 4013 HOH A O   1 
HETATM 7126 O O   . HOH Q 6 .   ? -35.419 -17.417 -27.922 1.00 19.29  ? 4014 HOH A O   1 
HETATM 7127 O O   . HOH Q 6 .   ? -29.566 -2.905  -10.956 1.00 16.75  ? 4015 HOH A O   1 
HETATM 7128 O O   . HOH Q 6 .   ? -29.785 24.399  -24.432 1.00 14.36  ? 4016 HOH A O   1 
HETATM 7129 O O   . HOH Q 6 .   ? -21.850 9.388   -7.108  1.00 14.16  ? 4017 HOH A O   1 
HETATM 7130 O O   . HOH Q 6 .   ? -2.005  2.379   -13.290 1.00 20.60  ? 4018 HOH A O   1 
HETATM 7131 O O   . HOH Q 6 .   ? -22.268 25.454  21.640  1.00 23.11  ? 4019 HOH A O   1 
HETATM 7132 O O   . HOH Q 6 .   ? -18.977 23.193  15.623  1.00 23.69  ? 4020 HOH A O   1 
HETATM 7133 O O   . HOH Q 6 .   ? -15.669 22.796  -15.001 1.00 19.13  ? 4021 HOH A O   1 
HETATM 7134 O O   . HOH Q 6 .   ? -28.101 3.028   -9.306  1.00 20.46  ? 4022 HOH A O   1 
HETATM 7135 O O   . HOH Q 6 .   ? -36.562 -19.278 -29.497 1.00 24.18  ? 4023 HOH A O   1 
HETATM 7136 O O   . HOH Q 6 .   ? -33.489 -2.193  -8.568  1.00 12.26  ? 4024 HOH A O   1 
HETATM 7137 O O   . HOH Q 6 .   ? -26.577 11.933  -23.523 1.00 18.93  ? 4025 HOH A O   1 
HETATM 7138 O O   . HOH Q 6 .   ? -26.320 13.843  -18.199 1.00 13.62  ? 4026 HOH A O   1 
HETATM 7139 O O   . HOH Q 6 .   ? -25.443 31.383  -2.620  1.00 18.95  ? 4027 HOH A O   1 
HETATM 7140 O O   . HOH Q 6 .   ? -34.717 5.284   -6.465  1.00 19.81  ? 4028 HOH A O   1 
HETATM 7141 O O   . HOH Q 6 .   ? -51.447 1.027   -17.062 1.00 15.82  ? 4029 HOH A O   1 
HETATM 7142 O O   . HOH Q 6 .   ? -44.059 8.606   -13.375 1.00 17.21  ? 4030 HOH A O   1 
HETATM 7143 O O   . HOH Q 6 .   ? -12.629 16.191  -5.744  1.00 20.39  ? 4031 HOH A O   1 
HETATM 7144 O O   . HOH Q 6 .   ? -43.271 17.870  -21.102 1.00 18.67  ? 4032 HOH A O   1 
HETATM 7145 O O   . HOH Q 6 .   ? -29.161 -18.558 -15.120 1.00 21.09  ? 4033 HOH A O   1 
HETATM 7146 O O   . HOH Q 6 .   ? -28.036 6.074   -3.037  1.00 21.41  ? 4034 HOH A O   1 
HETATM 7147 O O   . HOH Q 6 .   ? -42.135 10.948  -6.260  1.00 18.40  ? 4035 HOH A O   1 
HETATM 7148 O O   . HOH Q 6 .   ? -19.160 37.252  -21.263 1.00 21.44  ? 4036 HOH A O   1 
HETATM 7149 O O   . HOH Q 6 .   ? -39.543 -5.472  -34.574 1.00 17.42  ? 4037 HOH A O   1 
HETATM 7150 O O   . HOH Q 6 .   ? -14.051 22.773  -12.790 1.00 15.86  ? 4038 HOH A O   1 
HETATM 7151 O O   . HOH Q 6 .   ? -6.088  -8.393  -16.786 1.00 20.78  ? 4039 HOH A O   1 
HETATM 7152 O O   . HOH Q 6 .   ? -45.155 11.562  -12.575 1.00 16.34  ? 4040 HOH A O   1 
HETATM 7153 O O   . HOH Q 6 .   ? -33.310 -4.279  -17.111 1.00 18.46  ? 4041 HOH A O   1 
HETATM 7154 O O   . HOH Q 6 .   ? -11.658 7.207   -11.193 1.00 19.97  ? 4042 HOH A O   1 
HETATM 7155 O O   . HOH Q 6 .   ? -15.776 24.588  -16.908 1.00 20.76  ? 4043 HOH A O   1 
HETATM 7156 O O   . HOH Q 6 .   ? -40.053 34.083  -20.732 1.00 19.36  ? 4044 HOH A O   1 
HETATM 7157 O O   . HOH Q 6 .   ? -31.303 5.143   -0.712  1.00 22.29  ? 4045 HOH A O   1 
HETATM 7158 O O   . HOH Q 6 .   ? -41.809 31.918  -20.379 1.00 24.05  ? 4046 HOH A O   1 
HETATM 7159 O O   . HOH Q 6 .   ? -17.161 6.852   -1.476  1.00 21.06  ? 4047 HOH A O   1 
HETATM 7160 O O   . HOH Q 6 .   ? -32.626 2.927   -8.674  1.00 21.60  ? 4048 HOH A O   1 
HETATM 7161 O O   . HOH Q 6 .   ? -15.719 7.567   -13.130 1.00 18.44  ? 4049 HOH A O   1 
HETATM 7162 O O   . HOH Q 6 .   ? -9.177  25.323  0.296   1.00 17.37  ? 4050 HOH A O   1 
HETATM 7163 O O   . HOH Q 6 .   ? -28.442 24.658  4.607   1.00 17.97  ? 4051 HOH A O   1 
HETATM 7164 O O   . HOH Q 6 .   ? -18.819 10.418  4.916   1.00 29.27  ? 4052 HOH A O   1 
HETATM 7165 O O   . HOH Q 6 .   ? -57.070 11.207  -24.528 1.00 19.71  ? 4053 HOH A O   1 
HETATM 7166 O O   . HOH Q 6 .   ? -11.291 -3.441  -13.565 1.00 21.88  ? 4054 HOH A O   1 
HETATM 7167 O O   . HOH Q 6 .   ? -36.298 -5.337  -41.945 1.00 21.44  ? 4055 HOH A O   1 
HETATM 7168 O O   . HOH Q 6 .   ? -44.906 -5.952  -11.827 1.00 21.12  ? 4056 HOH A O   1 
HETATM 7169 O O   . HOH Q 6 .   ? -36.576 14.916  -34.225 1.00 24.90  ? 4057 HOH A O   1 
HETATM 7170 O O   . HOH Q 6 .   ? -21.806 -2.301  -6.395  1.00 18.36  ? 4058 HOH A O   1 
HETATM 7171 O O   . HOH Q 6 .   ? -29.771 24.478  0.232   1.00 22.50  ? 4059 HOH A O   1 
HETATM 7172 O O   . HOH Q 6 .   ? -14.402 20.196  -11.697 1.00 19.66  ? 4060 HOH A O   1 
HETATM 7173 O O   . HOH Q 6 .   ? -27.279 -20.375 -14.096 1.00 21.71  ? 4061 HOH A O   1 
HETATM 7174 O O   . HOH Q 6 .   ? -40.889 11.386  -27.815 1.00 20.10  ? 4062 HOH A O   1 
HETATM 7175 O O   . HOH Q 6 .   ? -29.635 -16.575 -13.288 1.00 18.84  ? 4063 HOH A O   1 
HETATM 7176 O O   . HOH Q 6 .   ? -46.509 7.223   -32.572 1.00 17.08  ? 4064 HOH A O   1 
HETATM 7177 O O   . HOH Q 6 .   ? -26.214 16.132  -29.393 1.00 21.94  ? 4065 HOH A O   1 
HETATM 7178 O O   . HOH Q 6 .   ? -24.582 48.484  -21.252 1.00 22.88  ? 4066 HOH A O   1 
HETATM 7179 O O   . HOH Q 6 .   ? -1.474  -11.809 -16.090 1.00 25.55  ? 4067 HOH A O   1 
HETATM 7180 O O   . HOH Q 6 .   ? -32.805 7.110   -7.721  1.00 16.01  ? 4068 HOH A O   1 
HETATM 7181 O O   . HOH Q 6 .   ? -24.948 -1.955  -34.724 1.00 20.71  ? 4069 HOH A O   1 
HETATM 7182 O O   . HOH Q 6 .   ? -19.433 13.966  -24.514 1.00 17.28  ? 4070 HOH A O   1 
HETATM 7183 O O   . HOH Q 6 .   ? -47.248 3.576   -45.589 1.00 25.12  ? 4071 HOH A O   1 
HETATM 7184 O O   . HOH Q 6 .   ? -14.343 6.718   -2.796  1.00 27.73  ? 4072 HOH A O   1 
HETATM 7185 O O   . HOH Q 6 .   ? -9.460  21.803  -8.413  1.00 21.41  ? 4073 HOH A O   1 
HETATM 7186 O O   . HOH Q 6 .   ? -11.886 20.211  0.626   1.00 21.20  ? 4074 HOH A O   1 
HETATM 7187 O O   . HOH Q 6 .   ? -28.605 21.998  5.655   1.00 18.52  ? 4075 HOH A O   1 
HETATM 7188 O O   . HOH Q 6 .   ? -19.528 6.622   -18.966 1.00 18.34  ? 4076 HOH A O   1 
HETATM 7189 O O   . HOH Q 6 .   ? -28.782 -16.377 -16.944 1.00 18.14  ? 4077 HOH A O   1 
HETATM 7190 O O   . HOH Q 6 .   ? -32.004 18.284  -27.651 1.00 19.31  ? 4078 HOH A O   1 
HETATM 7191 O O   . HOH Q 6 .   ? -9.882  30.176  -12.334 1.00 21.49  ? 4079 HOH A O   1 
HETATM 7192 O O   . HOH Q 6 .   ? -30.645 3.412   -42.718 1.00 24.28  ? 4080 HOH A O   1 
HETATM 7193 O O   . HOH Q 6 .   ? -16.284 -6.859  -13.674 1.00 24.84  ? 4081 HOH A O   1 
HETATM 7194 O O   . HOH Q 6 .   ? -29.718 -0.911  -8.963  1.00 22.44  ? 4082 HOH A O   1 
HETATM 7195 O O   . HOH Q 6 .   ? -28.058 31.773  6.141   1.00 21.23  ? 4083 HOH A O   1 
HETATM 7196 O O   . HOH Q 6 .   ? -53.767 13.999  -15.559 1.00 21.78  ? 4084 HOH A O   1 
HETATM 7197 O O   . HOH Q 6 .   ? -33.958 14.513  -1.508  1.00 22.38  ? 4085 HOH A O   1 
HETATM 7198 O O   . HOH Q 6 .   ? -15.161 2.827   -6.205  1.00 19.90  ? 4086 HOH A O   1 
HETATM 7199 O O   . HOH Q 6 .   ? -46.354 6.598   -7.458  1.00 23.09  ? 4087 HOH A O   1 
HETATM 7200 O O   . HOH Q 6 .   ? -36.319 30.717  -7.216  1.00 18.91  ? 4088 HOH A O   1 
HETATM 7201 O O   . HOH Q 6 .   ? -24.192 25.445  3.352   1.00 23.69  ? 4089 HOH A O   1 
HETATM 7202 O O   . HOH Q 6 .   ? -11.406 -1.425  -11.866 1.00 26.32  ? 4090 HOH A O   1 
HETATM 7203 O O   . HOH Q 6 .   ? -62.279 0.626   -27.580 1.00 20.97  ? 4091 HOH A O   1 
HETATM 7204 O O   . HOH Q 6 .   ? -47.727 0.630   -9.640  1.00 25.11  ? 4092 HOH A O   1 
HETATM 7205 O O   . HOH Q 6 .   ? -25.354 4.068   -31.212 1.00 24.09  ? 4093 HOH A O   1 
HETATM 7206 O O   . HOH Q 6 .   ? -24.301 29.243  -0.228  1.00 20.87  ? 4094 HOH A O   1 
HETATM 7207 O O   . HOH Q 6 .   ? -39.645 28.669  -21.718 1.00 26.24  ? 4095 HOH A O   1 
HETATM 7208 O O   . HOH Q 6 .   ? -49.469 15.950  -22.754 1.00 19.79  ? 4096 HOH A O   1 
HETATM 7209 O O   . HOH Q 6 .   ? -29.917 -12.687 -7.753  1.00 12.92  ? 4097 HOH A O   1 
HETATM 7210 O O   . HOH Q 6 .   ? -6.211  -8.046  -27.068 1.00 25.17  ? 4098 HOH A O   1 
HETATM 7211 O O   . HOH Q 6 .   ? -42.400 -16.375 -4.159  1.00 26.64  ? 4099 HOH A O   1 
HETATM 7212 O O   . HOH Q 6 .   ? -8.092  23.705  -9.863  1.00 26.23  ? 4100 HOH A O   1 
HETATM 7213 O O   . HOH Q 6 .   ? -14.632 32.359  -0.172  1.00 24.71  ? 4101 HOH A O   1 
HETATM 7214 O O   . HOH Q 6 .   ? -29.056 -5.148  -15.992 1.00 19.62  ? 4102 HOH A O   1 
HETATM 7215 O O   . HOH Q 6 .   ? -54.191 -7.857  -3.682  1.00 29.68  ? 4103 HOH A O   1 
HETATM 7216 O O   . HOH Q 6 .   ? -25.565 24.393  11.974  1.00 21.03  ? 4104 HOH A O   1 
HETATM 7217 O O   . HOH Q 6 .   ? -27.340 3.833   -1.470  1.00 25.02  ? 4105 HOH A O   1 
HETATM 7218 O O   . HOH Q 6 .   ? -38.814 9.927   -27.076 1.00 20.65  ? 4106 HOH A O   1 
HETATM 7219 O O   . HOH Q 6 .   ? -8.582  -7.415  -16.881 1.00 22.25  ? 4107 HOH A O   1 
HETATM 7220 O O   . HOH Q 6 .   ? -33.278 -7.910  -39.768 1.00 29.29  ? 4108 HOH A O   1 
HETATM 7221 O O   . HOH Q 6 .   ? -25.936 21.509  5.336   1.00 22.09  ? 4109 HOH A O   1 
HETATM 7222 O O   . HOH Q 6 .   ? -21.379 25.715  4.100   1.00 21.50  ? 4110 HOH A O   1 
HETATM 7223 O O   . HOH Q 6 .   ? -30.475 39.990  -18.685 1.00 25.64  ? 4111 HOH A O   1 
HETATM 7224 O O   . HOH Q 6 .   ? -24.896 19.076  4.506   1.00 23.88  ? 4112 HOH A O   1 
HETATM 7225 O O   . HOH Q 6 .   ? -2.925  -2.732  -27.847 1.00 21.62  ? 4113 HOH A O   1 
HETATM 7226 O O   . HOH Q 6 .   ? 2.027   4.575   -18.040 1.00 26.31  ? 4114 HOH A O   1 
HETATM 7227 O O   . HOH Q 6 .   ? -27.906 22.107  13.264  1.00 29.70  ? 4115 HOH A O   1 
HETATM 7228 O O   . HOH Q 6 .   ? -34.061 -5.602  -40.811 1.00 22.01  ? 4116 HOH A O   1 
HETATM 7229 O O   . HOH Q 6 .   ? -11.286 12.525  3.910   1.00 31.11  ? 4117 HOH A O   1 
HETATM 7230 O O   . HOH Q 6 .   ? -7.311  -16.463 -24.674 1.00 30.66  ? 4118 HOH A O   1 
HETATM 7231 O O   . HOH Q 6 .   ? -31.896 -15.892 -7.906  1.00 25.29  ? 4119 HOH A O   1 
HETATM 7232 O O   . HOH Q 6 .   ? -25.668 19.073  -29.031 1.00 25.39  ? 4120 HOH A O   1 
HETATM 7233 O O   . HOH Q 6 .   ? -13.361 13.778  -9.108  1.00 23.63  ? 4121 HOH A O   1 
HETATM 7234 O O   . HOH Q 6 .   ? -60.171 -7.662  -39.617 1.00 24.01  ? 4122 HOH A O   1 
HETATM 7235 O O   . HOH Q 6 .   ? -41.524 2.811   -7.545  1.00 25.95  ? 4123 HOH A O   1 
HETATM 7236 O O   . HOH Q 6 .   ? -12.283 -15.927 -15.591 1.00 21.81  ? 4124 HOH A O   1 
HETATM 7237 O O   . HOH Q 6 .   ? -16.009 -16.005 -32.440 1.00 30.25  ? 4125 HOH A O   1 
HETATM 7238 O O   . HOH Q 6 .   ? -38.112 -8.938  -49.614 1.00 20.53  ? 4126 HOH A O   1 
HETATM 7239 O O   . HOH Q 6 .   ? -43.602 29.778  -13.649 1.00 26.37  ? 4127 HOH A O   1 
HETATM 7240 O O   . HOH Q 6 .   ? -21.064 -15.060 -17.529 1.00 27.16  ? 4128 HOH A O   1 
HETATM 7241 O O   . HOH Q 6 .   ? -45.087 4.393   -44.527 1.00 33.76  ? 4129 HOH A O   1 
HETATM 7242 O O   . HOH Q 6 .   ? -17.497 8.923   -15.344 1.00 21.34  ? 4130 HOH A O   1 
HETATM 7243 O O   . HOH Q 6 .   ? -45.845 32.960  -18.369 1.00 29.92  ? 4131 HOH A O   1 
HETATM 7244 O O   . HOH Q 6 .   ? -39.192 15.132  -14.131 1.00 22.21  ? 4132 HOH A O   1 
HETATM 7245 O O   . HOH Q 6 .   ? -15.028 23.136  -19.208 1.00 24.94  ? 4133 HOH A O   1 
HETATM 7246 O O   . HOH Q 6 .   ? -13.584 -19.829 -16.187 1.00 26.30  ? 4134 HOH A O   1 
HETATM 7247 O O   . HOH Q 6 .   ? -22.060 -11.883 -6.897  1.00 26.70  ? 4135 HOH A O   1 
HETATM 7248 O O   . HOH Q 6 .   ? -42.203 -14.462 -30.208 1.00 30.83  ? 4136 HOH A O   1 
HETATM 7249 O O   . HOH Q 6 .   ? -2.647  -9.669  -11.875 1.00 24.32  ? 4137 HOH A O   1 
HETATM 7250 O O   . HOH Q 6 .   ? -43.741 -19.513 -11.735 1.00 23.52  ? 4138 HOH A O   1 
HETATM 7251 O O   . HOH Q 6 .   ? -47.541 -6.231  -12.623 1.00 22.74  ? 4139 HOH A O   1 
HETATM 7252 O O   . HOH Q 6 .   ? -22.536 15.669  -14.058 1.00 23.75  ? 4140 HOH A O   1 
HETATM 7253 O O   . HOH Q 6 .   ? 0.401   7.181   -18.912 1.00 20.74  ? 4141 HOH A O   1 
HETATM 7254 O O   . HOH Q 6 .   ? -5.764  18.340  -12.094 1.00 29.05  ? 4142 HOH A O   1 
HETATM 7255 O O   . HOH Q 6 .   ? -46.623 -17.103 -23.056 1.00 28.28  ? 4143 HOH A O   1 
HETATM 7256 O O   . HOH Q 6 .   ? -43.774 13.032  -27.089 1.00 24.99  ? 4144 HOH A O   1 
HETATM 7257 O O   . HOH Q 6 .   ? -7.234  29.405  -7.532  1.00 26.27  ? 4145 HOH A O   1 
HETATM 7258 O O   . HOH Q 6 .   ? -41.244 14.935  -25.728 1.00 23.37  ? 4146 HOH A O   1 
HETATM 7259 O O   . HOH Q 6 .   ? -48.225 -2.460  -6.027  1.00 34.60  ? 4147 HOH A O   1 
HETATM 7260 O O   . HOH Q 6 .   ? -60.981 -8.293  -47.920 1.00 31.06  ? 4148 HOH A O   1 
HETATM 7261 O O   . HOH Q 6 .   ? -39.989 -2.232  -47.032 1.00 22.91  ? 4149 HOH A O   1 
HETATM 7262 O O   . HOH Q 6 .   ? -53.481 16.555  -17.200 1.00 26.31  ? 4150 HOH A O   1 
HETATM 7263 O O   . HOH Q 6 .   ? -48.108 -11.362 -25.901 1.00 23.62  ? 4151 HOH A O   1 
HETATM 7264 O O   . HOH Q 6 .   ? -36.417 -15.060 -34.295 1.00 31.03  ? 4152 HOH A O   1 
HETATM 7265 O O   . HOH Q 6 .   ? -40.078 -18.738 -4.092  1.00 34.12  ? 4153 HOH A O   1 
HETATM 7266 O O   . HOH Q 6 .   ? -41.923 -21.636 -11.027 1.00 28.62  ? 4154 HOH A O   1 
HETATM 7267 O O   . HOH Q 6 .   ? -31.698 -0.774  -5.550  1.00 28.22  ? 4155 HOH A O   1 
HETATM 7268 O O   . HOH Q 6 .   ? -32.899 -17.465 -31.133 1.00 25.80  ? 4156 HOH A O   1 
HETATM 7269 O O   . HOH Q 6 .   ? -66.437 6.611   -33.853 1.00 29.49  ? 4157 HOH A O   1 
HETATM 7270 O O   . HOH Q 6 .   ? -45.385 -13.720 -33.847 1.00 29.79  ? 4158 HOH A O   1 
HETATM 7271 O O   . HOH Q 6 .   ? -24.419 1.351   1.839   1.00 28.88  ? 4159 HOH A O   1 
HETATM 7272 O O   . HOH Q 6 .   ? -22.955 8.408   1.829   1.00 26.92  ? 4160 HOH A O   1 
HETATM 7273 O O   . HOH Q 6 .   ? -20.365 26.768  -23.048 1.00 24.50  ? 4161 HOH A O   1 
HETATM 7274 O O   . HOH Q 6 .   ? -9.513  7.569   -17.731 1.00 26.85  ? 4162 HOH A O   1 
HETATM 7275 O O   . HOH Q 6 .   ? -30.548 4.262   -8.864  1.00 22.12  ? 4163 HOH A O   1 
HETATM 7276 O O   . HOH Q 6 .   ? -10.757 -8.161  -15.119 1.00 27.47  ? 4164 HOH A O   1 
HETATM 7277 O O   . HOH Q 6 .   ? -31.259 31.326  -29.330 1.00 32.68  ? 4165 HOH A O   1 
HETATM 7278 O O   . HOH Q 6 .   ? -26.897 24.595  2.417   1.00 24.72  ? 4166 HOH A O   1 
HETATM 7279 O O   . HOH Q 6 .   ? -23.177 21.788  -26.922 1.00 23.94  ? 4167 HOH A O   1 
HETATM 7280 O O   . HOH Q 6 .   ? -48.177 -7.149  -43.832 1.00 43.39  ? 4168 HOH A O   1 
HETATM 7281 O O   . HOH Q 6 .   ? -25.937 7.486   -32.560 1.00 29.83  ? 4169 HOH A O   1 
HETATM 7282 O O   . HOH Q 6 .   ? -16.977 44.436  -11.862 1.00 25.92  ? 4170 HOH A O   1 
HETATM 7283 O O   . HOH Q 6 .   ? -33.724 -2.984  -42.568 1.00 27.42  ? 4171 HOH A O   1 
HETATM 7284 O O   . HOH Q 6 .   ? -49.710 25.080  -10.083 1.00 29.83  ? 4172 HOH A O   1 
HETATM 7285 O O   . HOH Q 6 .   ? -36.716 29.769  -1.823  1.00 27.62  ? 4173 HOH A O   1 
HETATM 7286 O O   . HOH Q 6 .   ? -63.366 -11.380 -37.410 1.00 500.00 ? 4174 HOH A O   1 
HETATM 7287 O O   . HOH Q 6 .   ? -10.075 28.607  -14.776 1.00 24.70  ? 4175 HOH A O   1 
HETATM 7288 O O   . HOH Q 6 .   ? -17.589 46.710  -23.146 1.00 28.47  ? 4176 HOH A O   1 
HETATM 7289 O O   . HOH Q 6 .   ? -34.096 -15.893 -29.255 1.00 22.40  ? 4177 HOH A O   1 
HETATM 7290 O O   . HOH Q 6 .   ? -40.876 34.502  -8.273  1.00 23.75  ? 4178 HOH A O   1 
HETATM 7291 O O   . HOH Q 6 .   ? -43.682 -5.419  -0.800  1.00 26.95  ? 4179 HOH A O   1 
HETATM 7292 O O   . HOH Q 6 .   ? -19.086 24.345  -19.530 1.00 26.20  ? 4180 HOH A O   1 
HETATM 7293 O O   . HOH Q 6 .   ? -30.065 19.974  4.425   1.00 37.17  ? 4181 HOH A O   1 
HETATM 7294 O O   . HOH Q 6 .   ? -19.987 6.235   5.340   1.00 28.47  ? 4182 HOH A O   1 
HETATM 7295 O O   . HOH Q 6 .   ? -5.477  -13.642 -12.942 1.00 25.66  ? 4183 HOH A O   1 
HETATM 7296 O O   . HOH Q 6 .   ? -9.983  -19.061 -15.599 1.00 27.62  ? 4184 HOH A O   1 
HETATM 7297 O O   . HOH Q 6 .   ? -17.190 12.684  5.096   1.00 29.64  ? 4185 HOH A O   1 
HETATM 7298 O O   . HOH Q 6 .   ? -71.379 1.461   -34.078 1.00 27.84  ? 4186 HOH A O   1 
HETATM 7299 O O   . HOH Q 6 .   ? -38.305 -8.086  -0.094  1.00 28.66  ? 4187 HOH A O   1 
HETATM 7300 O O   . HOH Q 6 .   ? -60.476 -7.380  -27.604 1.00 30.33  ? 4188 HOH A O   1 
HETATM 7301 O O   . HOH Q 6 .   ? -35.256 -20.968 -10.679 1.00 34.62  ? 4189 HOH A O   1 
HETATM 7302 O O   . HOH Q 6 .   ? -65.363 8.898   -38.729 1.00 37.72  ? 4190 HOH A O   1 
HETATM 7303 O O   . HOH Q 6 .   ? -31.675 -6.196  -35.141 1.00 29.45  ? 4191 HOH A O   1 
HETATM 7304 O O   . HOH Q 6 .   ? -32.832 2.454   -49.290 1.00 29.32  ? 4192 HOH A O   1 
HETATM 7305 O O   . HOH Q 6 .   ? -46.004 9.271   -31.079 1.00 34.77  ? 4193 HOH A O   1 
HETATM 7306 O O   . HOH Q 6 .   ? -42.342 -16.336 -28.266 1.00 25.37  ? 4194 HOH A O   1 
HETATM 7307 O O   . HOH Q 6 .   ? -44.443 18.106  -23.570 1.00 23.46  ? 4195 HOH A O   1 
HETATM 7308 O O   . HOH Q 6 .   ? -8.722  22.196  -5.663  1.00 27.59  ? 4196 HOH A O   1 
HETATM 7309 O O   . HOH Q 6 .   ? -29.147 21.507  8.271   1.00 35.96  ? 4197 HOH A O   1 
HETATM 7310 O O   . HOH Q 6 .   ? 1.347   1.998   -6.813  1.00 28.27  ? 4198 HOH A O   1 
HETATM 7311 O O   . HOH Q 6 .   ? -62.673 0.340   -16.334 1.00 33.60  ? 4199 HOH A O   1 
HETATM 7312 O O   . HOH Q 6 .   ? -16.985 -12.180 -6.485  1.00 29.31  ? 4200 HOH A O   1 
HETATM 7313 O O   . HOH Q 6 .   ? -29.787 -3.088  -3.008  1.00 31.62  ? 4201 HOH A O   1 
HETATM 7314 O O   . HOH Q 6 .   ? -31.575 26.718  -26.691 1.00 30.87  ? 4202 HOH A O   1 
HETATM 7315 O O   . HOH Q 6 .   ? -46.578 11.924  -48.075 1.00 24.40  ? 4203 HOH A O   1 
HETATM 7316 O O   . HOH Q 6 .   ? -31.002 -10.020 -33.250 1.00 34.04  ? 4204 HOH A O   1 
HETATM 7317 O O   . HOH Q 6 .   ? -15.007 42.579  -15.442 1.00 32.51  ? 4205 HOH A O   1 
HETATM 7318 O O   . HOH Q 6 .   ? -37.778 22.170  8.791   1.00 29.42  ? 4206 HOH A O   1 
HETATM 7319 O O   . HOH Q 6 .   ? -17.517 -26.043 -20.902 1.00 30.40  ? 4207 HOH A O   1 
HETATM 7320 O O   . HOH Q 6 .   ? -42.928 11.208  -29.367 1.00 28.88  ? 4208 HOH A O   1 
HETATM 7321 O O   . HOH Q 6 .   ? -22.674 -19.074 -9.950  1.00 25.07  ? 4209 HOH A O   1 
HETATM 7322 O O   . HOH Q 6 .   ? -10.794 3.579   -33.881 1.00 28.13  ? 4210 HOH A O   1 
HETATM 7323 O O   . HOH Q 6 .   ? -28.645 5.647   -23.377 1.00 26.06  ? 4211 HOH A O   1 
HETATM 7324 O O   . HOH Q 6 .   ? -37.602 32.050  -5.558  1.00 33.53  ? 4212 HOH A O   1 
HETATM 7325 O O   . HOH Q 6 .   ? -14.923 17.052  6.222   1.00 30.63  ? 4213 HOH A O   1 
HETATM 7326 O O   . HOH Q 6 .   ? -15.414 21.742  -22.736 1.00 30.68  ? 4214 HOH A O   1 
HETATM 7327 O O   . HOH Q 6 .   ? -55.755 17.691  -16.416 1.00 26.35  ? 4215 HOH A O   1 
HETATM 7328 O O   . HOH Q 6 .   ? -28.835 17.529  5.179   1.00 25.68  ? 4216 HOH A O   1 
HETATM 7329 O O   . HOH Q 6 .   ? -44.647 -17.687 -5.550  1.00 34.02  ? 4217 HOH A O   1 
HETATM 7330 O O   . HOH Q 6 .   ? -28.730 2.620   -44.227 1.00 27.82  ? 4218 HOH A O   1 
HETATM 7331 O O   . HOH Q 6 .   ? -47.686 -9.948  -6.451  1.00 27.44  ? 4219 HOH A O   1 
HETATM 7332 O O   . HOH Q 6 .   ? -46.101 -21.739 -11.880 1.00 33.68  ? 4220 HOH A O   1 
HETATM 7333 O O   . HOH Q 6 .   ? -12.868 24.636  -20.262 1.00 30.82  ? 4221 HOH A O   1 
HETATM 7334 O O   . HOH Q 6 .   ? -18.516 2.145   -35.191 1.00 26.49  ? 4222 HOH A O   1 
HETATM 7335 O O   . HOH Q 6 .   ? -21.951 34.789  7.851   1.00 33.68  ? 4223 HOH A O   1 
HETATM 7336 O O   . HOH Q 6 .   ? -44.242 6.070   -32.763 1.00 25.70  ? 4224 HOH A O   1 
HETATM 7337 O O   . HOH Q 6 .   ? -42.326 -1.614  -48.248 1.00 28.95  ? 4225 HOH A O   1 
HETATM 7338 O O   . HOH Q 6 .   ? -58.856 10.125  -7.124  1.00 30.89  ? 4226 HOH A O   1 
HETATM 7339 O O   . HOH Q 6 .   ? -24.439 2.090   -0.756  1.00 28.24  ? 4227 HOH A O   1 
HETATM 7340 O O   . HOH Q 6 .   ? -28.520 -19.809 -29.571 1.00 34.26  ? 4228 HOH A O   1 
HETATM 7341 O O   . HOH Q 6 .   ? -25.923 11.519  -30.093 1.00 25.90  ? 4229 HOH A O   1 
HETATM 7342 O O   . HOH Q 6 .   ? -46.183 8.008   -51.663 1.00 31.41  ? 4230 HOH A O   1 
HETATM 7343 O O   . HOH Q 6 .   ? -42.800 19.687  -24.911 1.00 28.08  ? 4231 HOH A O   1 
HETATM 7344 O O   . HOH Q 6 .   ? -24.146 9.693   -30.110 1.00 26.05  ? 4232 HOH A O   1 
HETATM 7345 O O   . HOH Q 6 .   ? -10.959 -12.329 -8.340  1.00 32.24  ? 4233 HOH A O   1 
HETATM 7346 O O   . HOH Q 6 .   ? -36.684 14.109  -39.571 1.00 37.53  ? 4234 HOH A O   1 
HETATM 7347 O O   . HOH Q 6 .   ? -47.695 14.365  -26.322 1.00 30.29  ? 4235 HOH A O   1 
HETATM 7348 O O   . HOH Q 6 .   ? -23.298 23.112  20.358  1.00 28.75  ? 4236 HOH A O   1 
HETATM 7349 O O   . HOH Q 6 .   ? -37.126 12.431  -48.375 1.00 33.89  ? 4237 HOH A O   1 
HETATM 7350 O O   . HOH Q 6 .   ? -44.675 -6.772  -44.364 1.00 35.20  ? 4238 HOH A O   1 
HETATM 7351 O O   . HOH Q 6 .   ? 2.013   10.308  3.886   1.00 36.62  ? 4239 HOH A O   1 
HETATM 7352 O O   . HOH Q 6 .   ? -17.078 22.962  -20.789 1.00 26.64  ? 4240 HOH A O   1 
HETATM 7353 O O   . HOH Q 6 .   ? -40.011 18.364  -0.110  1.00 33.83  ? 4241 HOH A O   1 
HETATM 7354 O O   . HOH Q 6 .   ? -40.518 35.384  -22.947 1.00 34.89  ? 4242 HOH A O   1 
HETATM 7355 O O   . HOH Q 6 .   ? -15.400 8.518   -29.145 1.00 34.26  ? 4243 HOH A O   1 
HETATM 7356 O O   . HOH Q 6 .   ? -49.190 -12.939 -18.330 1.00 30.81  ? 4244 HOH A O   1 
HETATM 7357 O O   . HOH Q 6 .   ? -38.160 -5.186  0.591   1.00 27.73  ? 4245 HOH A O   1 
HETATM 7358 O O   . HOH Q 6 .   ? -4.031  9.530   2.992   1.00 30.22  ? 4246 HOH A O   1 
HETATM 7359 O O   . HOH Q 6 .   ? -48.883 5.474   -8.909  1.00 29.20  ? 4247 HOH A O   1 
HETATM 7360 O O   . HOH Q 6 .   ? -46.454 25.628  -20.426 1.00 33.64  ? 4248 HOH A O   1 
HETATM 7361 O O   . HOH Q 6 .   ? -33.072 10.706  -22.663 1.00 21.30  ? 4249 HOH A O   1 
HETATM 7362 O O   . HOH Q 6 .   ? -19.296 26.393  21.891  1.00 28.44  ? 4250 HOH A O   1 
HETATM 7363 O O   . HOH Q 6 .   ? -64.412 0.151   -24.923 1.00 29.67  ? 4251 HOH A O   1 
HETATM 7364 O O   . HOH Q 6 .   ? -41.182 -12.265 -1.905  1.00 32.92  ? 4252 HOH A O   1 
HETATM 7365 O O   . HOH Q 6 .   ? -35.519 12.555  -2.491  1.00 26.90  ? 4253 HOH A O   1 
HETATM 7366 O O   . HOH Q 6 .   ? -14.479 41.431  -19.907 1.00 34.60  ? 4254 HOH A O   1 
HETATM 7367 O O   . HOH Q 6 .   ? -14.699 5.743   -5.631  1.00 31.11  ? 4255 HOH A O   1 
HETATM 7368 O O   . HOH Q 6 .   ? -50.310 -3.042  -4.252  1.00 31.56  ? 4256 HOH A O   1 
HETATM 7369 O O   . HOH Q 6 .   ? -30.759 32.881  3.999   1.00 27.04  ? 4257 HOH A O   1 
HETATM 7370 O O   . HOH Q 6 .   ? -46.870 18.895  -23.336 1.00 31.55  ? 4258 HOH A O   1 
HETATM 7371 O O   . HOH Q 6 .   ? -54.600 13.230  -23.724 1.00 25.55  ? 4259 HOH A O   1 
HETATM 7372 O O   . HOH Q 6 .   ? -7.683  35.814  -6.728  1.00 30.79  ? 4260 HOH A O   1 
HETATM 7373 O O   . HOH Q 6 .   ? -37.694 10.524  -17.581 1.00 32.91  ? 4261 HOH A O   1 
HETATM 7374 O O   . HOH Q 6 .   ? -33.438 38.726  -12.854 1.00 34.57  ? 4262 HOH A O   1 
HETATM 7375 O O   . HOH Q 6 .   ? -6.989  -1.135  1.259   1.00 30.05  ? 4263 HOH A O   1 
HETATM 7376 O O   . HOH Q 6 .   ? -0.510  8.712   -2.545  1.00 31.89  ? 4264 HOH A O   1 
HETATM 7377 O O   . HOH Q 6 .   ? -43.475 30.999  -22.173 1.00 32.78  ? 4265 HOH A O   1 
HETATM 7378 O O   . HOH Q 6 .   ? -49.526 2.471   -8.952  1.00 31.79  ? 4266 HOH A O   1 
HETATM 7379 O O   . HOH Q 6 .   ? -42.989 2.421   -4.923  1.00 40.23  ? 4267 HOH A O   1 
HETATM 7380 O O   . HOH Q 6 .   ? -37.202 -24.434 -21.798 1.00 27.88  ? 4268 HOH A O   1 
HETATM 7381 O O   . HOH Q 6 .   ? -50.236 24.783  -19.875 1.00 33.61  ? 4269 HOH A O   1 
HETATM 7382 O O   . HOH Q 6 .   ? -1.420  9.010   -20.096 1.00 27.70  ? 4270 HOH A O   1 
HETATM 7383 O O   . HOH Q 6 .   ? -32.548 22.322  14.628  1.00 31.56  ? 4271 HOH A O   1 
HETATM 7384 O O   . HOH Q 6 .   ? -19.310 15.837  5.261   1.00 32.12  ? 4272 HOH A O   1 
HETATM 7385 O O   . HOH Q 6 .   ? -57.683 -2.248  -17.800 1.00 32.97  ? 4273 HOH A O   1 
HETATM 7386 O O   . HOH Q 6 .   ? -30.247 26.005  -29.025 1.00 33.90  ? 4274 HOH A O   1 
HETATM 7387 O O   . HOH Q 6 .   ? -20.031 -27.456 -16.744 1.00 37.39  ? 4275 HOH A O   1 
HETATM 7388 O O   . HOH Q 6 .   ? -11.888 -9.064  -22.614 1.00 28.92  ? 4276 HOH A O   1 
HETATM 7389 O O   . HOH Q 6 .   ? -21.350 4.583   -28.824 1.00 30.35  ? 4277 HOH A O   1 
HETATM 7390 O O   . HOH Q 6 .   ? 3.198   3.170   -8.217  1.00 40.27  ? 4278 HOH A O   1 
HETATM 7391 O O   . HOH Q 6 .   ? -18.871 16.005  -9.808  1.00 35.91  ? 4279 HOH A O   1 
HETATM 7392 O O   . HOH Q 6 .   ? -54.122 -2.318  -49.521 1.00 32.66  ? 4280 HOH A O   1 
HETATM 7393 O O   . HOH Q 6 .   ? -30.317 -22.803 -9.370  1.00 35.58  ? 4281 HOH A O   1 
HETATM 7394 O O   . HOH Q 6 .   ? -30.101 -15.691 -1.008  1.00 35.12  ? 4282 HOH A O   1 
HETATM 7395 O O   . HOH Q 6 .   ? -3.097  -11.047 -25.941 1.00 37.50  ? 4283 HOH A O   1 
HETATM 7396 O O   . HOH Q 6 .   ? -6.530  34.751  -3.977  1.00 32.76  ? 4284 HOH A O   1 
HETATM 7397 O O   . HOH Q 6 .   ? -33.525 23.110  17.858  1.00 35.55  ? 4285 HOH A O   1 
HETATM 7398 O O   . HOH Q 6 .   ? -58.791 16.111  -30.742 1.00 34.40  ? 4286 HOH A O   1 
HETATM 7399 O O   . HOH Q 6 .   ? -22.014 -0.830  -0.409  1.00 37.18  ? 4287 HOH A O   1 
HETATM 7400 O O   . HOH Q 6 .   ? -27.671 25.325  -28.786 1.00 31.00  ? 4288 HOH A O   1 
HETATM 7401 O O   . HOH Q 6 .   ? -53.791 -8.170  -43.691 1.00 33.24  ? 4289 HOH A O   1 
HETATM 7402 O O   . HOH Q 6 .   ? -12.082 16.354  5.409   1.00 40.57  ? 4290 HOH A O   1 
HETATM 7403 O O   . HOH Q 6 .   ? -15.149 -19.250 -13.249 1.00 34.81  ? 4291 HOH A O   1 
HETATM 7404 O O   . HOH Q 6 .   ? -31.663 -26.900 -18.177 1.00 35.14  ? 4292 HOH A O   1 
HETATM 7405 O O   . HOH Q 6 .   ? -18.123 0.597   2.677   1.00 46.24  ? 4293 HOH A O   1 
HETATM 7406 O O   . HOH Q 6 .   ? -23.859 -10.085 -35.186 1.00 47.92  ? 4294 HOH A O   1 
HETATM 7407 O O   . HOH Q 6 .   ? -64.769 3.056   -26.370 1.00 32.47  ? 4295 HOH A O   1 
HETATM 7408 O O   . HOH Q 6 .   ? -60.883 -6.868  -31.323 1.00 33.03  ? 4296 HOH A O   1 
HETATM 7409 O O   . HOH Q 6 .   ? -31.989 0.180   -8.131  1.00 30.41  ? 4297 HOH A O   1 
HETATM 7410 O O   . HOH Q 6 .   ? -0.640  -1.902  -29.091 1.00 32.30  ? 4298 HOH A O   1 
HETATM 7411 O O   . HOH Q 6 .   ? 4.345   0.057   -11.568 1.00 37.09  ? 4299 HOH A O   1 
HETATM 7412 O O   . HOH Q 6 .   ? -25.012 35.123  -3.742  1.00 33.14  ? 4300 HOH A O   1 
HETATM 7413 O O   . HOH Q 6 .   ? -7.873  1.954   3.800   1.00 34.20  ? 4301 HOH A O   1 
HETATM 7414 O O   . HOH Q 6 .   ? 3.353   -2.747  -12.815 1.00 35.78  ? 4302 HOH A O   1 
HETATM 7415 O O   . HOH Q 6 .   ? -24.615 34.828  16.594  1.00 33.98  ? 4303 HOH A O   1 
HETATM 7416 O O   . HOH Q 6 .   ? -3.589  5.334   3.080   1.00 38.96  ? 4304 HOH A O   1 
HETATM 7417 O O   . HOH Q 6 .   ? -15.743 -22.800 -12.934 1.00 36.82  ? 4305 HOH A O   1 
HETATM 7418 O O   . HOH Q 6 .   ? -56.351 -3.697  -15.577 1.00 44.13  ? 4306 HOH A O   1 
HETATM 7419 O O   . HOH Q 6 .   ? -8.995  12.808  5.407   1.00 31.88  ? 4307 HOH A O   1 
HETATM 7420 O O   . HOH Q 6 .   ? -39.784 0.753   -1.143  1.00 36.42  ? 4308 HOH A O   1 
HETATM 7421 O O   . HOH Q 6 .   ? -30.634 -2.184  -45.388 1.00 37.43  ? 4309 HOH A O   1 
HETATM 7422 O O   . HOH Q 6 .   ? -23.296 3.473   -30.118 1.00 34.10  ? 4310 HOH A O   1 
HETATM 7423 O O   . HOH Q 6 .   ? -27.332 40.119  -2.832  1.00 41.88  ? 4311 HOH A O   1 
HETATM 7424 O O   . HOH Q 6 .   ? -51.504 10.684  -7.139  1.00 37.20  ? 4312 HOH A O   1 
HETATM 7425 O O   . HOH Q 6 .   ? -33.450 28.290  -27.600 1.00 31.84  ? 4313 HOH A O   1 
HETATM 7426 O O   . HOH Q 6 .   ? -12.162 16.222  -24.421 1.00 33.30  ? 4314 HOH A O   1 
HETATM 7427 O O   . HOH Q 6 .   ? -14.116 20.493  9.737   1.00 39.83  ? 4315 HOH A O   1 
HETATM 7428 O O   . HOH Q 6 .   ? -30.007 35.113  -31.564 1.00 35.04  ? 4316 HOH A O   1 
HETATM 7429 O O   . HOH Q 6 .   ? -10.272 30.421  11.405  1.00 44.52  ? 4317 HOH A O   1 
HETATM 7430 O O   . HOH Q 6 .   ? -35.926 12.149  -5.267  1.00 28.94  ? 4318 HOH A O   1 
HETATM 7431 O O   . HOH Q 6 .   ? -49.321 -7.246  -37.840 1.00 44.90  ? 4319 HOH A O   1 
HETATM 7432 O O   . HOH Q 6 .   ? -49.931 -0.153  -52.130 1.00 34.09  ? 4320 HOH A O   1 
HETATM 7433 O O   . HOH Q 6 .   ? -34.126 39.686  -20.767 1.00 35.59  ? 4321 HOH A O   1 
HETATM 7434 O O   . HOH Q 6 .   ? -19.147 -8.824  -34.812 1.00 33.89  ? 4322 HOH A O   1 
HETATM 7435 O O   . HOH Q 6 .   ? -37.378 20.144  10.589  1.00 40.66  ? 4323 HOH A O   1 
HETATM 7436 O O   . HOH Q 6 .   ? -49.427 -7.505  -28.484 1.00 30.80  ? 4324 HOH A O   1 
HETATM 7437 O O   . HOH Q 6 .   ? -11.670 -1.794  -39.179 1.00 41.75  ? 4325 HOH A O   1 
HETATM 7438 O O   . HOH Q 6 .   ? -53.382 -4.971  -29.207 1.00 43.59  ? 4326 HOH A O   1 
HETATM 7439 O O   . HOH Q 6 .   ? -1.659  -10.310 -7.815  1.00 33.33  ? 4327 HOH A O   1 
HETATM 7440 O O   . HOH Q 6 .   ? -7.571  -18.968 -24.937 1.00 38.40  ? 4328 HOH A O   1 
HETATM 7441 O O   . HOH Q 6 .   ? -35.658 0.432   -38.193 1.00 26.01  ? 4329 HOH A O   1 
HETATM 7442 O O   . HOH Q 6 .   ? -28.147 11.019  1.436   1.00 38.20  ? 4330 HOH A O   1 
HETATM 7443 O O   . HOH Q 6 .   ? -39.782 32.060  -7.545  1.00 33.96  ? 4331 HOH A O   1 
HETATM 7444 O O   . HOH Q 6 .   ? 4.785   7.959   -6.667  1.00 52.63  ? 4332 HOH A O   1 
HETATM 7445 O O   . HOH Q 6 .   ? -33.938 39.658  -25.481 1.00 33.25  ? 4333 HOH A O   1 
HETATM 7446 O O   . HOH Q 6 .   ? -0.065  8.160   -5.883  1.00 32.48  ? 4334 HOH A O   1 
HETATM 7447 O O   . HOH Q 6 .   ? -50.491 12.238  -41.434 1.00 30.58  ? 4335 HOH A O   1 
HETATM 7448 O O   . HOH Q 6 .   ? -34.367 4.310   3.961   1.00 45.00  ? 4336 HOH A O   1 
HETATM 7449 O O   . HOH Q 6 .   ? -30.697 -26.426 -21.780 1.00 31.79  ? 4337 HOH A O   1 
HETATM 7450 O O   . HOH Q 6 .   ? -16.597 -25.923 -23.350 1.00 33.02  ? 4338 HOH A O   1 
HETATM 7451 O O   . HOH Q 6 .   ? -51.160 27.375  -12.398 1.00 37.26  ? 4339 HOH A O   1 
HETATM 7452 O O   . HOH Q 6 .   ? -58.140 -8.554  -27.969 1.00 42.25  ? 4340 HOH A O   1 
HETATM 7453 O O   . HOH Q 6 .   ? 2.076   -7.467  -29.102 1.00 41.20  ? 4341 HOH A O   1 
HETATM 7454 O O   . HOH Q 6 .   ? -69.777 -6.235  -37.334 1.00 38.36  ? 4342 HOH A O   1 
HETATM 7455 O O   . HOH Q 6 .   ? -48.182 0.268   -6.838  1.00 41.90  ? 4343 HOH A O   1 
HETATM 7456 O O   . HOH Q 6 .   ? -67.807 -2.015  -44.422 1.00 42.89  ? 4344 HOH A O   1 
HETATM 7457 O O   . HOH Q 6 .   ? -38.482 1.346   -45.233 1.00 33.59  ? 4345 HOH A O   1 
HETATM 7458 O O   . HOH Q 6 .   ? -19.404 -26.780 -31.470 1.00 36.99  ? 4346 HOH A O   1 
HETATM 7459 O O   . HOH Q 6 .   ? -14.519 -27.476 -17.625 1.00 38.98  ? 4347 HOH A O   1 
HETATM 7460 O O   . HOH Q 6 .   ? 5.212   1.852   -18.468 1.00 48.95  ? 4348 HOH A O   1 
HETATM 7461 O O   . HOH Q 6 .   ? -6.478  -1.250  -38.063 1.00 37.87  ? 4349 HOH A O   1 
HETATM 7462 O O   . HOH Q 6 .   ? -22.827 6.897   4.008   1.00 38.78  ? 4350 HOH A O   1 
HETATM 7463 O O   . HOH Q 6 .   ? -14.182 35.755  -19.093 1.00 33.01  ? 4351 HOH A O   1 
HETATM 7464 O O   . HOH Q 6 .   ? -20.200 29.051  -30.149 1.00 51.06  ? 4352 HOH A O   1 
HETATM 7465 O O   . HOH Q 6 .   ? -3.469  10.212  6.424   1.00 32.85  ? 4353 HOH A O   1 
HETATM 7466 O O   . HOH Q 6 .   ? -14.873 31.325  19.162  1.00 37.91  ? 4354 HOH A O   1 
HETATM 7467 O O   . HOH Q 6 .   ? -39.184 -27.476 -16.935 1.00 38.36  ? 4355 HOH A O   1 
HETATM 7468 O O   . HOH Q 6 .   ? -26.195 40.443  -29.417 1.00 42.46  ? 4356 HOH A O   1 
HETATM 7469 O O   . HOH Q 6 .   ? -39.120 28.663  -24.573 1.00 31.93  ? 4357 HOH A O   1 
HETATM 7470 O O   . HOH Q 6 .   ? -42.986 11.572  -3.917  1.00 49.43  ? 4358 HOH A O   1 
HETATM 7471 O O   . HOH Q 6 .   ? -55.232 14.315  -36.121 1.00 43.01  ? 4359 HOH A O   1 
HETATM 7472 O O   . HOH Q 6 .   ? -39.572 18.334  -33.951 1.00 40.72  ? 4360 HOH A O   1 
HETATM 7473 O O   . HOH Q 6 .   ? -18.231 35.787  -27.589 1.00 37.51  ? 4361 HOH A O   1 
HETATM 7474 O O   . HOH Q 6 .   ? -23.825 42.211  -23.727 1.00 36.54  ? 4362 HOH A O   1 
HETATM 7475 O O   . HOH Q 6 .   ? -28.319 20.164  14.568  1.00 42.26  ? 4363 HOH A O   1 
HETATM 7476 O O   . HOH Q 6 .   ? -31.909 -3.248  -0.681  1.00 50.43  ? 4364 HOH A O   1 
HETATM 7477 O O   . HOH Q 6 .   ? -37.282 30.418  -27.052 1.00 32.00  ? 4365 HOH A O   1 
HETATM 7478 O O   . HOH Q 6 .   ? -11.289 8.711   -23.798 1.00 40.74  ? 4366 HOH A O   1 
HETATM 7479 O O   . HOH Q 6 .   ? -20.664 35.878  14.477  1.00 39.27  ? 4367 HOH A O   1 
HETATM 7480 O O   . HOH Q 6 .   ? -26.485 45.042  -3.741  1.00 35.78  ? 4368 HOH A O   1 
HETATM 7481 O O   . HOH Q 6 .   ? -29.601 15.512  -38.843 1.00 43.89  ? 4369 HOH A O   1 
HETATM 7482 O O   . HOH Q 6 .   ? 4.280   -0.391  -17.085 1.00 43.88  ? 4370 HOH A O   1 
HETATM 7483 O O   . HOH Q 6 .   ? -55.417 13.723  -31.129 1.00 36.47  ? 4371 HOH A O   1 
HETATM 7484 O O   . HOH Q 6 .   ? -23.634 -17.116 -3.385  1.00 44.37  ? 4372 HOH A O   1 
HETATM 7485 O O   . HOH Q 6 .   ? -30.567 -4.063  -37.955 1.00 39.04  ? 4373 HOH A O   1 
HETATM 7486 O O   . HOH Q 6 .   ? -48.373 -6.156  -35.806 1.00 39.72  ? 4374 HOH A O   1 
HETATM 7487 O O   . HOH Q 6 .   ? -8.525  4.199   -32.303 1.00 35.20  ? 4375 HOH A O   1 
HETATM 7488 O O   . HOH Q 6 .   ? -12.741 43.553  -19.377 1.00 42.41  ? 4376 HOH A O   1 
HETATM 7489 O O   . HOH Q 6 .   ? 1.632   -8.962  -10.426 1.00 37.05  ? 4377 HOH A O   1 
HETATM 7490 O O   . HOH Q 6 .   ? -12.800 -28.192 -21.818 1.00 39.34  ? 4378 HOH A O   1 
HETATM 7491 O O   . HOH Q 6 .   ? -36.460 31.736  -0.057  1.00 38.40  ? 4379 HOH A O   1 
HETATM 7492 O O   . HOH Q 6 .   ? -31.569 7.344   -28.016 1.00 31.35  ? 4380 HOH A O   1 
HETATM 7493 O O   . HOH Q 6 .   ? -30.269 -4.161  -35.034 1.00 29.09  ? 4381 HOH A O   1 
HETATM 7494 O O   . HOH Q 6 .   ? -17.742 37.567  -25.443 1.00 34.19  ? 4382 HOH A O   1 
HETATM 7495 O O   . HOH Q 6 .   ? -64.281 6.477   -35.808 1.00 44.06  ? 4383 HOH A O   1 
HETATM 7496 O O   . HOH Q 6 .   ? -39.055 38.968  -10.268 1.00 40.86  ? 4384 HOH A O   1 
HETATM 7497 O O   . HOH Q 6 .   ? -8.209  -9.815  -6.386  1.00 34.13  ? 4385 HOH A O   1 
HETATM 7498 O O   . HOH Q 6 .   ? -12.654 -22.814 -31.573 1.00 45.30  ? 4386 HOH A O   1 
HETATM 7499 O O   . HOH Q 6 .   ? -21.209 43.927  0.312   1.00 43.91  ? 4387 HOH A O   1 
HETATM 7500 O O   . HOH Q 6 .   ? -13.492 46.299  -11.721 1.00 40.42  ? 4388 HOH A O   1 
HETATM 7501 O O   . HOH Q 6 .   ? -40.628 -4.885  1.287   1.00 35.82  ? 4389 HOH A O   1 
HETATM 7502 O O   . HOH Q 6 .   ? -41.956 -3.593  -50.848 1.00 45.38  ? 4390 HOH A O   1 
HETATM 7503 O O   . HOH Q 6 .   ? -16.401 40.668  -26.372 1.00 35.95  ? 4391 HOH A O   1 
HETATM 7504 O O   . HOH Q 6 .   ? -44.051 24.048  -4.604  1.00 35.61  ? 4392 HOH A O   1 
HETATM 7505 O O   . HOH Q 6 .   ? -53.591 8.809   -50.649 1.00 48.26  ? 4393 HOH A O   1 
HETATM 7506 O O   . HOH Q 6 .   ? -8.623  22.096  -16.905 1.00 34.82  ? 4394 HOH A O   1 
HETATM 7507 O O   . HOH Q 6 .   ? -29.819 39.911  -8.061  1.00 38.82  ? 4395 HOH A O   1 
HETATM 7508 O O   . HOH Q 6 .   ? -36.654 35.132  -4.962  1.00 40.26  ? 4396 HOH A O   1 
HETATM 7509 O O   . HOH Q 6 .   ? -26.236 21.704  11.396  1.00 37.41  ? 4397 HOH A O   1 
HETATM 7510 O O   . HOH Q 6 .   ? -26.067 6.429   -43.326 1.00 34.96  ? 4398 HOH A O   1 
HETATM 7511 O O   . HOH Q 6 .   ? -60.014 7.621   -19.443 1.00 29.97  ? 4399 HOH A O   1 
HETATM 7512 O O   . HOH Q 6 .   ? -5.287  28.336  -9.312  1.00 37.96  ? 4400 HOH A O   1 
HETATM 7513 O O   . HOH Q 6 .   ? -16.790 -27.640 -18.843 1.00 40.78  ? 4401 HOH A O   1 
HETATM 7514 O O   . HOH Q 6 .   ? -43.146 -8.873  -43.909 1.00 35.27  ? 4402 HOH A O   1 
HETATM 7515 O O   . HOH Q 6 .   ? 3.454   -9.803  -25.565 1.00 44.09  ? 4403 HOH A O   1 
HETATM 7516 O O   . HOH Q 6 .   ? 2.100   13.887  -0.462  1.00 35.78  ? 4404 HOH A O   1 
HETATM 7517 O O   . HOH Q 6 .   ? -18.197 36.475  15.316  1.00 38.74  ? 4405 HOH A O   1 
HETATM 7518 O O   . HOH Q 6 .   ? -37.860 39.248  -16.073 1.00 37.31  ? 4406 HOH A O   1 
HETATM 7519 O O   . HOH Q 6 .   ? -53.356 -0.642  -51.135 1.00 49.31  ? 4407 HOH A O   1 
HETATM 7520 O O   . HOH Q 6 .   ? -1.265  9.456   8.227   1.00 41.91  ? 4408 HOH A O   1 
HETATM 7521 O O   . HOH Q 6 .   ? -9.579  -19.122 -30.216 1.00 32.81  ? 4409 HOH A O   1 
HETATM 7522 O O   . HOH Q 6 .   ? -6.089  25.070  -8.509  1.00 44.20  ? 4410 HOH A O   1 
HETATM 7523 O O   . HOH Q 6 .   ? -54.138 16.122  -19.815 1.00 36.38  ? 4411 HOH A O   1 
HETATM 7524 O O   . HOH Q 6 .   ? -17.618 35.370  -22.635 1.00 36.22  ? 4412 HOH A O   1 
HETATM 7525 O O   . HOH Q 6 .   ? -35.741 15.519  -37.497 1.00 46.73  ? 4413 HOH A O   1 
HETATM 7526 O O   . HOH Q 6 .   ? -40.530 20.524  1.870   1.00 39.47  ? 4414 HOH A O   1 
HETATM 7527 O O   . HOH Q 6 .   ? -20.795 17.965  -13.520 1.00 28.77  ? 4415 HOH A O   1 
HETATM 7528 O O   . HOH Q 6 .   ? -33.802 22.379  -28.014 1.00 42.58  ? 4416 HOH A O   1 
HETATM 7529 O O   . HOH Q 6 .   ? -6.936  -20.378 -21.034 1.00 41.59  ? 4417 HOH A O   1 
HETATM 7530 O O   . HOH Q 6 .   ? -69.877 -6.370  -33.503 1.00 44.85  ? 4418 HOH A O   1 
HETATM 7531 O O   . HOH Q 6 .   ? -10.579 -11.116 -6.162  1.00 42.18  ? 4419 HOH A O   1 
HETATM 7532 O O   . HOH Q 6 .   ? -26.802 -23.258 -34.813 1.00 52.50  ? 4420 HOH A O   1 
HETATM 7533 O O   . HOH Q 6 .   ? -9.144  -15.682 -11.080 1.00 40.64  ? 4421 HOH A O   1 
HETATM 7534 O O   . HOH Q 6 .   ? -8.469  6.650   -31.905 1.00 49.69  ? 4422 HOH A O   1 
HETATM 7535 O O   . HOH Q 6 .   ? -7.617  25.904  -17.012 1.00 50.67  ? 4423 HOH A O   1 
HETATM 7536 O O   . HOH Q 6 .   ? -30.717 6.903   -48.988 1.00 39.38  ? 4424 HOH A O   1 
HETATM 7537 O O   . HOH Q 6 .   ? -43.129 -26.095 -15.391 1.00 41.47  ? 4425 HOH A O   1 
HETATM 7538 O O   . HOH Q 6 .   ? -57.108 -6.734  -19.453 1.00 43.49  ? 4426 HOH A O   1 
HETATM 7539 O O   . HOH Q 6 .   ? -26.140 33.138  -29.316 1.00 29.53  ? 4427 HOH A O   1 
HETATM 7540 O O   . HOH Q 6 .   ? -35.005 -14.309 -40.111 1.00 47.25  ? 4428 HOH A O   1 
HETATM 7541 O O   . HOH Q 6 .   ? -7.368  -22.212 -18.946 1.00 48.85  ? 4429 HOH A O   1 
HETATM 7542 O O   . HOH Q 6 .   ? -51.029 28.869  -14.180 1.00 53.17  ? 4430 HOH A O   1 
HETATM 7543 O O   . HOH Q 6 .   ? -6.025  22.148  -5.252  1.00 43.11  ? 4431 HOH A O   1 
HETATM 7544 O O   . HOH Q 6 .   ? -56.583 -3.002  -49.556 1.00 43.18  ? 4432 HOH A O   1 
HETATM 7545 O O   . HOH Q 6 .   ? -28.492 -1.242  -44.698 1.00 41.48  ? 4433 HOH A O   1 
HETATM 7546 O O   . HOH Q 6 .   ? -48.373 12.986  -36.708 1.00 36.05  ? 4434 HOH A O   1 
HETATM 7547 O O   . HOH Q 6 .   ? -16.143 36.785  -29.810 1.00 41.35  ? 4435 HOH A O   1 
HETATM 7548 O O   . HOH Q 6 .   ? -26.598 4.300   -44.439 1.00 41.77  ? 4436 HOH A O   1 
HETATM 7549 O O   . HOH Q 6 .   ? -11.553 -23.055 -27.836 1.00 37.83  ? 4437 HOH A O   1 
HETATM 7550 O O   . HOH Q 6 .   ? -59.101 -3.297  -12.875 1.00 41.50  ? 4438 HOH A O   1 
HETATM 7551 O O   . HOH Q 6 .   ? -14.516 31.524  -26.525 1.00 49.66  ? 4439 HOH A O   1 
HETATM 7552 O O   . HOH Q 6 .   ? -40.771 28.877  -3.705  1.00 37.90  ? 4440 HOH A O   1 
HETATM 7553 O O   . HOH Q 6 .   ? -55.349 17.451  -9.835  1.00 43.02  ? 4441 HOH A O   1 
HETATM 7554 O O   . HOH Q 6 .   ? -8.969  15.426  5.693   1.00 41.48  ? 4442 HOH A O   1 
HETATM 7555 O O   . HOH Q 6 .   ? -42.149 -6.965  1.048   1.00 35.20  ? 4443 HOH A O   1 
HETATM 7556 O O   . HOH Q 6 .   ? -30.974 -4.013  -41.422 1.00 40.63  ? 4444 HOH A O   1 
HETATM 7557 O O   . HOH Q 6 .   ? -23.550 -22.149 -12.695 1.00 41.28  ? 4445 HOH A O   1 
HETATM 7558 O O   . HOH Q 6 .   ? -45.657 -3.688  0.534   1.00 41.15  ? 4446 HOH A O   1 
HETATM 7559 O O   . HOH Q 6 .   ? -26.812 -21.809 -10.200 1.00 47.93  ? 4447 HOH A O   1 
HETATM 7560 O O   . HOH Q 6 .   ? -56.805 -6.918  -30.616 1.00 41.38  ? 4448 HOH A O   1 
HETATM 7561 O O   . HOH Q 6 .   ? -42.872 25.958  -27.530 1.00 49.51  ? 4449 HOH A O   1 
HETATM 7562 O O   . HOH Q 6 .   ? -19.251 -12.028 -5.629  1.00 44.17  ? 4450 HOH A O   1 
HETATM 7563 O O   . HOH Q 6 .   ? -0.441  18.814  0.747   1.00 41.79  ? 4451 HOH A O   1 
HETATM 7564 O O   . HOH Q 6 .   ? -55.385 -13.184 -15.147 1.00 41.38  ? 4452 HOH A O   1 
HETATM 7565 O O   . HOH Q 6 .   ? -14.641 -13.450 -5.975  1.00 44.89  ? 4453 HOH A O   1 
HETATM 7566 O O   . HOH Q 6 .   ? -33.303 -26.903 -23.261 1.00 38.93  ? 4454 HOH A O   1 
HETATM 7567 O O   . HOH Q 6 .   ? -35.459 10.456  -0.732  1.00 38.68  ? 4455 HOH A O   1 
HETATM 7568 O O   . HOH Q 6 .   ? -9.917  -5.925  -13.634 1.00 35.68  ? 4456 HOH A O   1 
HETATM 7569 O O   . HOH Q 6 .   ? 10.224  -15.594 -17.587 1.00 49.05  ? 4457 HOH A O   1 
HETATM 7570 O O   . HOH Q 6 .   ? -52.892 26.910  -14.181 1.00 40.33  ? 4458 HOH A O   1 
HETATM 7571 O O   . HOH Q 6 .   ? -16.367 2.775   -38.432 1.00 42.80  ? 4459 HOH A O   1 
HETATM 7572 O O   . HOH Q 6 .   ? -26.588 4.818   -47.089 1.00 42.58  ? 4460 HOH A O   1 
HETATM 7573 O O   . HOH Q 6 .   ? -17.448 49.122  -6.272  1.00 41.16  ? 4461 HOH A O   1 
HETATM 7574 O O   . HOH Q 6 .   ? -60.715 -6.284  -52.744 1.00 50.31  ? 4462 HOH A O   1 
HETATM 7575 O O   . HOH Q 6 .   ? -60.318 -5.026  -20.332 1.00 39.80  ? 4463 HOH A O   1 
HETATM 7576 O O   . HOH Q 6 .   ? -16.506 -19.483 -38.155 1.00 46.83  ? 4464 HOH A O   1 
HETATM 7577 O O   . HOH Q 6 .   ? -21.546 16.969  4.735   1.00 40.69  ? 4465 HOH A O   1 
HETATM 7578 O O   . HOH Q 6 .   ? -26.849 36.646  -31.850 1.00 48.34  ? 4466 HOH A O   1 
HETATM 7579 O O   . HOH Q 6 .   ? -17.331 31.989  21.138  1.00 45.99  ? 4467 HOH A O   1 
HETATM 7580 O O   . HOH Q 6 .   ? -70.122 8.941   -41.205 1.00 49.55  ? 4468 HOH A O   1 
HETATM 7581 O O   . HOH Q 6 .   ? -14.188 16.802  -28.297 1.00 38.73  ? 4469 HOH A O   1 
HETATM 7582 O O   . HOH Q 6 .   ? -5.057  0.825   -32.651 1.00 40.14  ? 4470 HOH A O   1 
HETATM 7583 O O   . HOH Q 6 .   ? -36.191 -23.109 -31.011 1.00 48.20  ? 4471 HOH A O   1 
HETATM 7584 O O   . HOH Q 6 .   ? -53.502 -7.588  -27.578 1.00 52.41  ? 4472 HOH A O   1 
HETATM 7585 O O   . HOH Q 6 .   ? -22.049 -3.578  -3.917  1.00 36.32  ? 4473 HOH A O   1 
HETATM 7586 O O   . HOH Q 6 .   ? -50.524 15.554  -45.868 1.00 55.37  ? 4474 HOH A O   1 
HETATM 7587 O O   . HOH Q 6 .   ? -31.710 -0.514  -48.870 1.00 47.83  ? 4475 HOH A O   1 
HETATM 7588 O O   . HOH Q 6 .   ? -17.999 8.426   7.042   1.00 47.76  ? 4476 HOH A O   1 
HETATM 7589 O O   . HOH Q 6 .   ? -27.115 28.892  22.855  1.00 37.21  ? 4477 HOH A O   1 
HETATM 7590 O O   . HOH Q 6 .   ? -45.914 24.803  -7.951  1.00 40.40  ? 4478 HOH A O   1 
HETATM 7591 O O   . HOH Q 6 .   ? -53.122 13.731  -30.109 1.00 33.48  ? 4479 HOH A O   1 
HETATM 7592 O O   . HOH Q 6 .   ? -36.605 25.142  -24.582 1.00 41.75  ? 4480 HOH A O   1 
HETATM 7593 O O   . HOH Q 6 .   ? -46.355 13.586  -35.073 1.00 57.58  ? 4481 HOH A O   1 
HETATM 7594 O O   . HOH Q 6 .   ? -47.009 -19.505 -9.649  1.00 50.38  ? 4482 HOH A O   1 
HETATM 7595 O O   . HOH Q 6 .   ? -56.769 12.595  -41.398 1.00 37.73  ? 4483 HOH A O   1 
HETATM 7596 O O   . HOH Q 6 .   ? -56.717 14.010  -9.306  1.00 39.29  ? 4484 HOH A O   1 
HETATM 7597 O O   . HOH Q 6 .   ? -10.550 7.487   10.887  1.00 40.36  ? 4485 HOH A O   1 
HETATM 7598 O O   . HOH Q 6 .   ? -35.016 40.274  -29.335 1.00 39.36  ? 4486 HOH A O   1 
HETATM 7599 O O   . HOH Q 6 .   ? -12.623 -21.503 -13.257 1.00 38.49  ? 4487 HOH A O   1 
HETATM 7600 O O   . HOH Q 6 .   ? -37.875 -10.937 -46.015 1.00 51.64  ? 4488 HOH A O   1 
HETATM 7601 O O   . HOH Q 6 .   ? -2.556  29.461  -7.901  1.00 49.90  ? 4489 HOH A O   1 
HETATM 7602 O O   . HOH Q 6 .   ? -48.965 -10.431 -38.712 1.00 47.00  ? 4490 HOH A O   1 
HETATM 7603 O O   . HOH Q 6 .   ? -50.506 14.492  -30.748 1.00 48.10  ? 4491 HOH A O   1 
HETATM 7604 O O   . HOH Q 6 .   ? -34.377 -2.909  1.667   1.00 38.16  ? 4492 HOH A O   1 
HETATM 7605 O O   . HOH Q 6 .   ? -25.462 31.092  23.887  1.00 49.73  ? 4493 HOH A O   1 
HETATM 7606 O O   . HOH Q 6 .   ? -46.944 -13.368 -1.231  1.00 36.64  ? 4494 HOH A O   1 
HETATM 7607 O O   . HOH Q 6 .   ? -40.614 3.596   -2.845  1.00 48.00  ? 4495 HOH A O   1 
HETATM 7608 O O   . HOH Q 6 .   ? -43.561 -27.339 -22.044 1.00 46.68  ? 4496 HOH A O   1 
HETATM 7609 O O   . HOH Q 6 .   ? -21.673 21.050  -28.979 1.00 30.75  ? 4497 HOH A O   1 
HETATM 7610 O O   . HOH Q 6 .   ? -70.266 -1.377  -24.981 1.00 40.05  ? 4498 HOH A O   1 
HETATM 7611 O O   . HOH Q 6 .   ? -20.687 6.876   -30.170 1.00 49.46  ? 4499 HOH A O   1 
HETATM 7612 O O   . HOH Q 6 .   ? -10.964 -17.927 -32.555 1.00 43.50  ? 4500 HOH A O   1 
HETATM 7613 O O   . HOH Q 6 .   ? -47.821 17.842  -5.188  1.00 49.57  ? 4501 HOH A O   1 
HETATM 7614 O O   . HOH Q 6 .   ? 7.207   -9.877  -21.579 1.00 44.87  ? 4502 HOH A O   1 
HETATM 7615 O O   . HOH Q 6 .   ? -37.492 36.268  10.163  1.00 53.57  ? 4503 HOH A O   1 
HETATM 7616 O O   . HOH Q 6 .   ? -61.031 1.710   -8.089  1.00 40.04  ? 4504 HOH A O   1 
HETATM 7617 O O   . HOH Q 6 .   ? -24.307 -21.047 -10.279 1.00 43.73  ? 4505 HOH A O   1 
HETATM 7618 O O   . HOH Q 6 .   ? -29.547 29.261  23.182  1.00 48.98  ? 4506 HOH A O   1 
HETATM 7619 O O   . HOH Q 6 .   ? -49.417 -21.638 -15.976 1.00 46.37  ? 4507 HOH A O   1 
HETATM 7620 O O   . HOH Q 6 .   ? -31.346 -6.608  -37.926 1.00 39.74  ? 4508 HOH A O   1 
HETATM 7621 O O   . HOH Q 6 .   ? -56.941 -14.264 -12.957 1.00 41.44  ? 4509 HOH A O   1 
HETATM 7622 O O   . HOH Q 6 .   ? 1.366   -14.015 -17.269 1.00 36.23  ? 4510 HOH A O   1 
HETATM 7623 O O   . HOH Q 6 .   ? -37.557 -24.587 -18.896 1.00 37.01  ? 4511 HOH A O   1 
HETATM 7624 O O   . HOH Q 6 .   ? -29.479 13.948  4.091   1.00 38.73  ? 4512 HOH A O   1 
HETATM 7625 O O   . HOH Q 6 .   ? -62.066 8.316   -36.147 1.00 40.08  ? 4513 HOH A O   1 
HETATM 7626 O O   . HOH Q 6 .   ? -24.847 26.579  -29.328 1.00 66.53  ? 4514 HOH A O   1 
HETATM 7627 O O   . HOH Q 6 .   ? 1.020   7.975   -24.519 1.00 42.65  ? 4515 HOH A O   1 
HETATM 7628 O O   . HOH Q 6 .   ? -43.550 15.546  -33.359 1.00 50.92  ? 4516 HOH A O   1 
HETATM 7629 O O   . HOH Q 6 .   ? -57.184 -13.842 -10.557 1.00 45.16  ? 4517 HOH A O   1 
HETATM 7630 O O   . HOH Q 6 .   ? 2.407   8.360   -22.330 1.00 38.69  ? 4518 HOH A O   1 
HETATM 7631 O O   . HOH Q 6 .   ? -63.264 10.614  -21.554 1.00 34.90  ? 4519 HOH A O   1 
HETATM 7632 O O   . HOH Q 6 .   ? -41.840 -12.579 -42.012 1.00 34.90  ? 4520 HOH A O   1 
HETATM 7633 O O   . HOH Q 6 .   ? -48.807 -12.269 -40.851 1.00 49.21  ? 4521 HOH A O   1 
HETATM 7634 O O   . HOH Q 6 .   ? -17.085 -6.151  -36.901 1.00 41.31  ? 4522 HOH A O   1 
HETATM 7635 O O   . HOH Q 6 .   ? -39.347 30.118  2.962   1.00 41.39  ? 4523 HOH A O   1 
HETATM 7636 O O   . HOH Q 6 .   ? -23.477 40.946  -28.876 1.00 34.90  ? 4524 HOH A O   1 
HETATM 7637 O O   . HOH Q 6 .   ? -27.463 13.614  -36.104 1.00 55.22  ? 4525 HOH A O   1 
HETATM 7638 O O   . HOH Q 6 .   ? 2.310   -2.278  -0.408  1.00 42.17  ? 4526 HOH A O   1 
HETATM 7639 O O   . HOH Q 6 .   ? -7.880  18.763  -18.300 1.00 41.98  ? 4527 HOH A O   1 
HETATM 7640 O O   . HOH Q 6 .   ? -13.752 27.357  12.129  1.00 41.16  ? 4528 HOH A O   1 
HETATM 7641 O O   . HOH Q 6 .   ? -12.552 42.159  -15.634 1.00 53.55  ? 4529 HOH A O   1 
HETATM 7642 O O   . HOH Q 6 .   ? -42.796 13.458  -31.912 1.00 48.07  ? 4530 HOH A O   1 
HETATM 7643 O O   . HOH Q 6 .   ? -18.150 4.328   -37.134 1.00 46.68  ? 4531 HOH A O   1 
HETATM 7644 O O   . HOH Q 6 .   ? -44.989 20.925  -5.275  1.00 35.63  ? 4532 HOH A O   1 
HETATM 7645 O O   . HOH Q 6 .   ? -6.957  24.424  0.357   1.00 40.31  ? 4533 HOH A O   1 
HETATM 7646 O O   . HOH Q 6 .   ? -13.025 28.549  3.328   1.00 41.79  ? 4534 HOH A O   1 
HETATM 7647 O O   . HOH Q 6 .   ? -1.141  -12.416 -23.982 1.00 44.05  ? 4535 HOH A O   1 
HETATM 7648 O O   . HOH Q 6 .   ? -66.320 -0.106  -23.702 1.00 39.69  ? 4536 HOH A O   1 
HETATM 7649 O O   . HOH Q 6 .   ? -2.518  0.615   -33.052 1.00 46.33  ? 4537 HOH A O   1 
HETATM 7650 O O   . HOH Q 6 .   ? -59.051 4.997   -59.807 1.00 46.60  ? 4538 HOH A O   1 
HETATM 7651 O O   . HOH Q 6 .   ? -19.515 -4.795  -37.696 1.00 37.06  ? 4539 HOH A O   1 
HETATM 7652 O O   . HOH Q 6 .   ? -71.437 2.185   -39.746 1.00 38.88  ? 4540 HOH A O   1 
HETATM 7653 O O   . HOH Q 6 .   ? -48.304 29.878  -9.479  1.00 41.89  ? 4541 HOH A O   1 
HETATM 7654 O O   . HOH Q 6 .   ? -50.505 -16.260 -9.395  1.00 47.84  ? 4542 HOH A O   1 
HETATM 7655 O O   . HOH Q 6 .   ? -12.605 30.124  10.991  1.00 49.12  ? 4543 HOH A O   1 
HETATM 7656 O O   . HOH Q 6 .   ? -25.773 -20.366 -28.626 1.00 42.03  ? 4544 HOH A O   1 
HETATM 7657 O O   . HOH Q 6 .   ? -22.099 -14.371 -4.185  1.00 46.26  ? 4545 HOH A O   1 
HETATM 7658 O O   . HOH Q 6 .   ? -23.016 36.890  -1.774  1.00 39.95  ? 4546 HOH A O   1 
HETATM 7659 O O   . HOH Q 6 .   ? -50.091 28.871  -11.086 1.00 42.68  ? 4547 HOH A O   1 
HETATM 7660 O O   . HOH Q 6 .   ? -33.334 -14.965 -36.151 1.00 46.21  ? 4548 HOH A O   1 
HETATM 7661 O O   . HOH Q 6 .   ? -56.854 10.573  -57.754 1.00 48.39  ? 4549 HOH A O   1 
HETATM 7662 O O   . HOH Q 6 .   ? -28.597 31.356  22.073  1.00 49.99  ? 4550 HOH A O   1 
HETATM 7663 O O   . HOH Q 6 .   ? 8.007   -9.884  -15.090 1.00 53.79  ? 4551 HOH A O   1 
HETATM 7664 O O   . HOH Q 6 .   ? -41.332 23.667  1.511   1.00 37.31  ? 4552 HOH A O   1 
HETATM 7665 O O   . HOH Q 6 .   ? -48.323 -0.460  -54.588 1.00 59.42  ? 4553 HOH A O   1 
HETATM 7666 O O   . HOH Q 6 .   ? -14.813 33.939  18.037  1.00 34.59  ? 4554 HOH A O   1 
HETATM 7667 O O   . HOH Q 6 .   ? -10.058 41.136  -1.499  1.00 56.82  ? 4555 HOH A O   1 
HETATM 7668 O O   . HOH Q 6 .   ? -13.946 19.278  7.448   1.00 45.19  ? 4556 HOH A O   1 
HETATM 7669 O O   . HOH Q 6 .   ? -7.453  24.681  5.984   1.00 50.59  ? 4557 HOH A O   1 
HETATM 7670 O O   . HOH Q 6 .   ? -12.618 34.319  16.999  1.00 35.40  ? 4558 HOH A O   1 
HETATM 7671 O O   . HOH Q 6 .   ? -42.301 9.648   -31.297 1.00 39.45  ? 4559 HOH A O   1 
HETATM 7672 O O   . HOH Q 6 .   ? 2.227   -14.635 -10.793 1.00 42.45  ? 4560 HOH A O   1 
HETATM 7673 O O   . HOH Q 6 .   ? -37.543 17.775  8.606   1.00 41.39  ? 4561 HOH A O   1 
HETATM 7674 O O   . HOH Q 6 .   ? -12.908 -17.566 -34.449 1.00 48.05  ? 4562 HOH A O   1 
HETATM 7675 O O   . HOH Q 6 .   ? -8.231  8.036   -25.014 1.00 51.11  ? 4563 HOH A O   1 
HETATM 7676 O O   . HOH Q 6 .   ? -40.176 -9.722  -45.166 1.00 47.34  ? 4564 HOH A O   1 
HETATM 7677 O O   . HOH Q 6 .   ? -39.015 26.293  -25.328 1.00 43.95  ? 4565 HOH A O   1 
HETATM 7678 O O   . HOH Q 6 .   ? -43.406 -13.910 -2.337  1.00 39.90  ? 4566 HOH A O   1 
HETATM 7679 O O   . HOH Q 6 .   ? -56.332 14.544  -27.591 1.00 38.83  ? 4567 HOH A O   1 
HETATM 7680 O O   . HOH Q 6 .   ? -24.268 6.910   -41.798 1.00 48.66  ? 4568 HOH A O   1 
HETATM 7681 O O   . HOH Q 6 .   ? -49.927 -15.133 -19.579 1.00 44.47  ? 4569 HOH A O   1 
HETATM 7682 O O   . HOH Q 6 .   ? 5.641   -6.147  -19.834 1.00 42.68  ? 4570 HOH A O   1 
HETATM 7683 O O   . HOH Q 6 .   ? -10.310 9.101   -25.927 1.00 42.15  ? 4571 HOH A O   1 
HETATM 7684 O O   . HOH Q 6 .   ? -6.261  3.172   -33.594 1.00 40.99  ? 4572 HOH A O   1 
HETATM 7685 O O   . HOH Q 6 .   ? -17.359 16.548  7.202   1.00 43.01  ? 4573 HOH A O   1 
HETATM 7686 O O   . HOH Q 6 .   ? -31.112 16.406  -34.757 1.00 33.99  ? 4574 HOH A O   1 
HETATM 7687 O O   . HOH Q 6 .   ? -38.329 14.748  -41.827 1.00 50.33  ? 4575 HOH A O   1 
HETATM 7688 O O   . HOH Q 6 .   ? 3.956   -7.541  -27.043 1.00 45.35  ? 4576 HOH A O   1 
HETATM 7689 O O   . HOH Q 6 .   ? -47.728 11.970  -31.511 1.00 47.37  ? 4577 HOH A O   1 
HETATM 7690 O O   . HOH Q 6 .   ? -34.548 -24.579 -29.409 1.00 45.22  ? 4578 HOH A O   1 
HETATM 7691 O O   . HOH Q 6 .   ? -54.914 15.249  -33.304 1.00 52.39  ? 4579 HOH A O   1 
HETATM 7692 O O   . HOH Q 6 .   ? -7.314  8.343   -29.973 1.00 44.23  ? 4580 HOH A O   1 
HETATM 7693 O O   . HOH Q 6 .   ? -72.614 -1.332  -33.347 1.00 41.30  ? 4581 HOH A O   1 
HETATM 7694 O O   . HOH Q 6 .   ? 2.403   -17.582 -10.060 1.00 52.19  ? 4582 HOH A O   1 
HETATM 7695 O O   . HOH Q 6 .   ? -45.445 23.868  -25.284 1.00 54.21  ? 4583 HOH A O   1 
HETATM 7696 O O   . HOH Q 6 .   ? -32.205 33.809  -30.130 1.00 42.05  ? 4584 HOH A O   1 
HETATM 7697 O O   . HOH Q 6 .   ? -25.214 9.706   2.402   1.00 51.81  ? 4585 HOH A O   1 
HETATM 7698 O O   . HOH Q 6 .   ? -28.307 14.533  -32.730 1.00 42.44  ? 4586 HOH A O   1 
HETATM 7699 O O   . HOH Q 6 .   ? -23.322 34.912  -32.891 1.00 46.64  ? 4587 HOH A O   1 
HETATM 7700 O O   . HOH Q 6 .   ? -38.847 4.158   -47.591 1.00 43.78  ? 4588 HOH A O   1 
HETATM 7701 O O   . HOH Q 6 .   ? -44.651 -22.547 -21.612 1.00 42.59  ? 4589 HOH A O   1 
HETATM 7702 O O   . HOH Q 6 .   ? -1.121  18.821  -3.147  1.00 63.17  ? 4590 HOH A O   1 
HETATM 7703 O O   . HOH Q 6 .   ? -13.434 20.646  -23.508 1.00 34.54  ? 4591 HOH A O   1 
HETATM 7704 O O   . HOH Q 6 .   ? -12.473 38.516  -18.736 1.00 38.50  ? 4592 HOH A O   1 
HETATM 7705 O O   . HOH Q 6 .   ? -40.844 17.940  -3.025  1.00 47.77  ? 4593 HOH A O   1 
HETATM 7706 O O   . HOH Q 6 .   ? -39.887 4.794   -49.772 1.00 43.10  ? 4594 HOH A O   1 
HETATM 7707 O O   . HOH Q 6 .   ? -0.135  5.332   -5.892  1.00 53.38  ? 4595 HOH A O   1 
HETATM 7708 O O   . HOH Q 6 .   ? -4.869  0.621   0.875   1.00 42.10  ? 4596 HOH A O   1 
HETATM 7709 O O   . HOH Q 6 .   ? -72.262 -1.654  -26.784 1.00 51.15  ? 4597 HOH A O   1 
HETATM 7710 O O   . HOH Q 6 .   ? -60.916 18.675  -33.646 1.00 52.29  ? 4598 HOH A O   1 
HETATM 7711 O O   . HOH Q 6 .   ? -43.447 34.723  -8.884  1.00 42.21  ? 4599 HOH A O   1 
HETATM 7712 O O   . HOH Q 6 .   ? -36.166 20.992  17.329  1.00 44.16  ? 4600 HOH A O   1 
HETATM 7713 O O   . HOH Q 6 .   ? -42.225 14.738  -39.590 1.00 50.37  ? 4601 HOH A O   1 
HETATM 7714 O O   . HOH Q 6 .   ? -12.874 -17.449 -13.452 1.00 41.47  ? 4602 HOH A O   1 
HETATM 7715 O O   . HOH Q 6 .   ? -47.992 -12.589 -33.218 1.00 38.55  ? 4603 HOH A O   1 
HETATM 7716 O O   . HOH Q 6 .   ? -20.073 -15.643 -35.859 1.00 32.54  ? 4604 HOH A O   1 
HETATM 7717 O O   . HOH Q 6 .   ? -35.982 17.560  -34.132 1.00 48.83  ? 4605 HOH A O   1 
HETATM 7718 O O   . HOH Q 6 .   ? -28.682 5.068   -49.344 1.00 45.41  ? 4606 HOH A O   1 
HETATM 7719 O O   . HOH Q 6 .   ? -42.088 23.396  4.717   1.00 40.32  ? 4607 HOH A O   1 
HETATM 7720 O O   . HOH Q 6 .   ? -18.121 16.190  -30.184 1.00 50.87  ? 4608 HOH A O   1 
HETATM 7721 O O   . HOH Q 6 .   ? -14.267 -1.647  -4.737  1.00 45.33  ? 4609 HOH A O   1 
HETATM 7722 O O   . HOH Q 6 .   ? -62.492 -7.336  -29.832 1.00 43.36  ? 4610 HOH A O   1 
HETATM 7723 O O   . HOH Q 6 .   ? -27.689 42.796  -2.551  1.00 58.52  ? 4611 HOH A O   1 
HETATM 7724 O O   . HOH Q 6 .   ? -36.512 22.723  -26.476 1.00 48.55  ? 4612 HOH A O   1 
HETATM 7725 O O   . HOH Q 6 .   ? -15.279 47.100  -15.027 1.00 46.77  ? 4613 HOH A O   1 
HETATM 7726 O O   . HOH Q 6 .   ? -55.769 18.635  -20.499 1.00 51.12  ? 4614 HOH A O   1 
HETATM 7727 O O   . HOH Q 6 .   ? -35.619 -27.022 -22.079 1.00 49.03  ? 4615 HOH A O   1 
HETATM 7728 O O   . HOH Q 6 .   ? -49.350 12.619  -48.494 1.00 46.51  ? 4616 HOH A O   1 
HETATM 7729 O O   . HOH Q 6 .   ? -32.162 37.314  11.120  1.00 32.00  ? 4617 HOH A O   1 
HETATM 7730 O O   . HOH Q 6 .   ? -14.804 -21.270 -14.760 1.00 22.19  ? 4618 HOH A O   1 
HETATM 7731 O O   . HOH Q 6 .   ? -33.527 12.056  -24.384 1.00 31.84  ? 4619 HOH A O   1 
HETATM 7732 O O   . HOH Q 6 .   ? -40.194 16.191  -37.635 1.00 43.49  ? 4620 HOH A O   1 
HETATM 7733 O O   . HOH Q 6 .   ? -23.772 2.259   -27.442 1.00 27.67  ? 4621 HOH A O   1 
HETATM 7734 O O   . HOH Q 6 .   ? 4.502   4.108   -17.988 1.00 35.90  ? 4622 HOH A O   1 
HETATM 7735 O O   . HOH Q 6 .   ? -23.614 -10.715 -4.870  1.00 37.41  ? 4623 HOH A O   1 
HETATM 7736 O O   . HOH Q 6 .   ? -22.547 -0.184  1.966   1.00 50.28  ? 4624 HOH A O   1 
HETATM 7737 O O   . HOH Q 6 .   ? -19.594 -3.190  -3.608  1.00 34.99  ? 4625 HOH A O   1 
HETATM 7738 O O   . HOH Q 6 .   ? -27.687 -3.600  1.091   1.00 31.66  ? 4626 HOH A O   1 
HETATM 7739 O O   . HOH Q 6 .   ? -24.750 -5.700  -11.582 1.00 20.21  ? 4627 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   CYS 4   4   ?   ?   ?   A . n 
A 1 5   PRO 5   5   ?   ?   ?   A . n 
A 1 6   VAL 6   6   ?   ?   ?   A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  ARG 12  12  12  ARG ARG A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  CYS 15  15  15  CYS CYS A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  CYS 26  26  26  CYS CYS A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  ARG 29  29  29  ARG ARG A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  CYS 31  31  31  CYS CYS A . n 
A 1 32  CYS 32  32  32  CYS CYS A . n 
A 1 33  TRP 33  33  33  TRP TRP A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  ASN 60  60  60  ASN ASN A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  ASN 81  81  81  ASN ASN A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  TYR 91  91  91  TYR TYR A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 GLN 104 104 104 GLN GLN A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ASN 106 106 106 ASN ASN A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 HIS 115 115 115 HIS HIS A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 TYR 129 129 129 TYR TYR A . n 
A 1 130 GLN 130 130 130 GLN GLN A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 LYS 141 141 141 LYS LYS A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 ASN 148 148 148 ASN ASN A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PRO 158 158 158 PRO PRO A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 PRO 173 173 173 PRO PRO A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 HIS 183 183 183 HIS HIS A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 HIS 185 185 185 HIS HIS A . n 
A 1 186 GLN 186 186 186 GLN GLN A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ARG 189 189 189 ARG ARG A . n 
A 1 190 HIS 190 190 190 HIS HIS A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 ASN 193 193 193 ASN ASN A . n 
A 1 194 TRP 194 194 194 TRP TRP A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 TRP 197 197 197 TRP TRP A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 ASN 201 201 201 ASN ASN A . n 
A 1 202 ARG 202 202 202 ARG ARG A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 ASN 207 207 207 ASN ASN A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 GLN 217 217 217 GLN GLN A . n 
A 1 218 THR 218 218 218 THR THR A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 CYS 222 222 222 CYS CYS A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 ASP 225 225 225 ASP ASP A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 MET 236 236 236 MET MET A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 PRO 247 247 247 PRO PRO A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 THR 252 252 252 THR THR A . n 
A 1 253 TYR 253 253 253 TYR TYR A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 GLY 257 257 257 GLY GLY A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 PHE 262 262 262 PHE PHE A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 PHE 265 265 265 PHE PHE A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 PRO 270 270 270 PRO PRO A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 VAL 274 274 274 VAL VAL A . n 
A 1 275 GLN 275 275 275 GLN GLN A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 TYR 277 277 277 TYR TYR A . n 
A 1 278 LEU 278 278 278 LEU LEU A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 ARG 283 283 283 ARG ARG A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 PRO 287 287 287 PRO PRO A . n 
A 1 288 SER 288 288 288 SER SER A . n 
A 1 289 TYR 289 289 289 TYR TYR A . n 
A 1 290 TRP 290 290 290 TRP TRP A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 LEU 292 292 292 LEU LEU A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 HIS 295 295 295 HIS HIS A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 TYR 299 299 299 TYR TYR A . n 
A 1 300 GLU 300 300 300 GLU GLU A . n 
A 1 301 TYR 301 301 301 TYR TYR A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 LEU 304 304 304 LEU LEU A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 ASN 306 306 306 ASN ASN A . n 
A 1 307 MET 307 307 307 MET MET A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 GLU 309 309 309 GLU GLU A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 ARG 313 313 313 ARG ARG A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 ARG 315 315 315 ARG ARG A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 GLN 318 318 318 GLN GLN A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 PRO 320 320 320 PRO PRO A . n 
A 1 321 TYR 321 321 321 TYR TYR A . n 
A 1 322 ASP 322 322 322 ASP ASP A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 GLN 324 324 324 GLN GLN A . n 
A 1 325 HIS 325 325 325 HIS HIS A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 ASP 327 327 327 ASP ASP A . n 
A 1 328 ILE 328 328 328 ILE ILE A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 MET 331 331 331 MET MET A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 GLU 333 333 333 GLU GLU A . n 
A 1 334 ARG 334 334 334 ARG ARG A . n 
A 1 335 ARG 335 335 335 ARG ARG A . n 
A 1 336 ASP 336 336 336 ASP ASP A . n 
A 1 337 PHE 337 337 337 PHE PHE A . n 
A 1 338 THR 338 338 338 THR THR A . n 
A 1 339 TYR 339 339 339 TYR TYR A . n 
A 1 340 ASP 340 340 340 ASP ASP A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 VAL 342 342 342 VAL VAL A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 PHE 344 344 344 PHE PHE A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 GLY 346 346 346 GLY GLY A . n 
A 1 347 PHE 347 347 347 PHE PHE A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 GLU 349 349 349 GLU GLU A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 GLU 353 353 353 GLU GLU A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 HIS 355 355 355 HIS HIS A . n 
A 1 356 ASN 356 356 356 ASN ASN A . n 
A 1 357 ASN 357 357 357 ASN ASN A . n 
A 1 358 GLY 358 358 358 GLY GLY A . n 
A 1 359 GLN 359 359 359 GLN GLN A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 LEU 361 361 361 LEU LEU A . n 
A 1 362 VAL 362 362 362 VAL VAL A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 ASP 366 366 366 ASP ASP A . n 
A 1 367 PRO 367 367 367 PRO PRO A . n 
A 1 368 ALA 368 368 368 ALA ALA A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 ASN 372 372 372 ASN ASN A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 SER 374 374 374 SER SER A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 SER 376 376 376 SER SER A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 PRO 378 378 378 PRO PRO A . n 
A 1 379 TYR 379 379 379 TYR TYR A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 PRO 381 381 381 PRO PRO A . n 
A 1 382 TYR 382 382 382 TYR TYR A . n 
A 1 383 ASP 383 383 383 ASP ASP A . n 
A 1 384 ARG 384 384 384 ARG ARG A . n 
A 1 385 GLY 385 385 385 GLY GLY A . n 
A 1 386 SER 386 386 386 SER SER A . n 
A 1 387 ASP 387 387 387 ASP ASP A . n 
A 1 388 MET 388 388 388 MET MET A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 ILE 390 390 390 ILE ILE A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 VAL 392 392 392 VAL VAL A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 SER 394 394 394 SER SER A . n 
A 1 395 SER 395 395 395 SER SER A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 GLY 397 397 397 GLY GLY A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 THR 399 399 399 THR THR A . n 
A 1 400 PRO 400 400 400 PRO PRO A . n 
A 1 401 LEU 401 401 401 LEU LEU A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 GLY 403 403 403 GLY GLY A . n 
A 1 404 GLU 404 404 404 GLU GLU A . n 
A 1 405 VAL 405 405 405 VAL VAL A . n 
A 1 406 TRP 406 406 406 TRP TRP A . n 
A 1 407 PRO 407 407 407 PRO PRO A . n 
A 1 408 GLY 408 408 408 GLY GLY A . n 
A 1 409 GLN 409 409 409 GLN GLN A . n 
A 1 410 THR 410 410 410 THR THR A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 PHE 412 412 412 PHE PHE A . n 
A 1 413 PRO 413 413 413 PRO PRO A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 TYR 415 415 415 TYR TYR A . n 
A 1 416 THR 416 416 416 THR THR A . n 
A 1 417 ASN 417 417 417 ASN ASN A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 CYS 420 420 420 CYS CYS A . n 
A 1 421 ALA 421 421 421 ALA ALA A . n 
A 1 422 VAL 422 422 422 VAL VAL A . n 
A 1 423 TRP 423 423 423 TRP TRP A . n 
A 1 424 TRP 424 424 424 TRP TRP A . n 
A 1 425 THR 425 425 425 THR THR A . n 
A 1 426 LYS 426 426 426 LYS LYS A . n 
A 1 427 GLU 427 427 427 GLU GLU A . n 
A 1 428 PHE 428 428 428 PHE PHE A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 LEU 430 430 430 LEU LEU A . n 
A 1 431 PHE 431 431 431 PHE PHE A . n 
A 1 432 HIS 432 432 432 HIS HIS A . n 
A 1 433 ASN 433 433 433 ASN ASN A . n 
A 1 434 GLN 434 434 434 GLN GLN A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 GLU 436 436 436 GLU GLU A . n 
A 1 437 PHE 437 437 437 PHE PHE A . n 
A 1 438 ASP 438 438 438 ASP ASP A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 ILE 440 440 440 ILE ILE A . n 
A 1 441 TRP 441 441 441 TRP TRP A . n 
A 1 442 ILE 442 442 442 ILE ILE A . n 
A 1 443 ASP 443 443 443 ASP ASP A . n 
A 1 444 MET 444 444 444 MET MET A . n 
A 1 445 ASN 445 445 445 ASN ASN A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 VAL 447 447 447 VAL VAL A . n 
A 1 448 SER 448 448 448 SER SER A . n 
A 1 449 ASN 449 449 449 ASN ASN A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 VAL 451 451 451 VAL VAL A . n 
A 1 452 ASP 452 452 452 ASP ASP A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 SER 454 454 454 SER SER A . n 
A 1 455 VAL 455 455 455 VAL VAL A . n 
A 1 456 SER 456 456 456 SER SER A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 CYS 458 458 458 CYS CYS A . n 
A 1 459 SER 459 459 459 SER SER A . n 
A 1 460 THR 460 460 460 THR THR A . n 
A 1 461 ASN 461 461 461 ASN ASN A . n 
A 1 462 ASN 462 462 462 ASN ASN A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 ASN 464 464 464 ASN ASN A . n 
A 1 465 ASN 465 465 465 ASN ASN A . n 
A 1 466 PRO 466 466 466 PRO PRO A . n 
A 1 467 PRO 467 467 467 PRO PRO A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 THR 469 469 469 THR THR A . n 
A 1 470 PRO 470 470 470 PRO PRO A . n 
A 1 471 ARG 471 471 471 ARG ARG A . n 
A 1 472 ILE 472 472 472 ILE ILE A . n 
A 1 473 LEU 473 473 473 LEU LEU A . n 
A 1 474 ASP 474 474 474 ASP ASP A . n 
A 1 475 GLY 475 475 475 GLY GLY A . n 
A 1 476 TYR 476 476 476 TYR TYR A . n 
A 1 477 LEU 477 477 477 LEU LEU A . n 
A 1 478 PHE 478 478 478 PHE PHE A . n 
A 1 479 CYS 479 479 479 CYS CYS A . n 
A 1 480 LYS 480 480 480 LYS LYS A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 LEU 482 482 482 LEU LEU A . n 
A 1 483 CYS 483 483 483 CYS CYS A . n 
A 1 484 MET 484 484 484 MET MET A . n 
A 1 485 ASP 485 485 485 ASP ASP A . n 
A 1 486 ALA 486 486 486 ALA ALA A . n 
A 1 487 VAL 487 487 487 VAL VAL A . n 
A 1 488 GLN 488 488 488 GLN GLN A . n 
A 1 489 HIS 489 489 489 HIS HIS A . n 
A 1 490 TRP 490 490 490 TRP TRP A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 LYS 492 492 492 LYS LYS A . n 
A 1 493 GLN 493 493 493 GLN GLN A . n 
A 1 494 TYR 494 494 494 TYR TYR A . n 
A 1 495 ASP 495 495 495 ASP ASP A . n 
A 1 496 ILE 496 496 496 ILE ILE A . n 
A 1 497 HIS 497 497 497 HIS HIS A . n 
A 1 498 ASN 498 498 498 ASN ASN A . n 
A 1 499 LEU 499 499 499 LEU LEU A . n 
A 1 500 TYR 500 500 500 TYR TYR A . n 
A 1 501 GLY 501 501 501 GLY GLY A . n 
A 1 502 TYR 502 502 502 TYR TYR A . n 
A 1 503 SER 503 503 503 SER SER A . n 
A 1 504 MET 504 504 504 MET MET A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 VAL 506 506 506 VAL VAL A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 THR 508 508 508 THR THR A . n 
A 1 509 ALA 509 509 509 ALA ALA A . n 
A 1 510 GLU 510 510 510 GLU GLU A . n 
A 1 511 ALA 511 511 511 ALA ALA A . n 
A 1 512 ALA 512 512 512 ALA ALA A . n 
A 1 513 LYS 513 513 513 LYS LYS A . n 
A 1 514 THR 514 514 514 THR THR A . n 
A 1 515 VAL 515 515 515 VAL VAL A . n 
A 1 516 PHE 516 516 516 PHE PHE A . n 
A 1 517 PRO 517 517 517 PRO PRO A . n 
A 1 518 ASN 518 518 518 ASN ASN A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 ARG 520 520 520 ARG ARG A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 PHE 522 522 522 PHE PHE A . n 
A 1 523 ILE 523 523 523 ILE ILE A . n 
A 1 524 LEU 524 524 524 LEU LEU A . n 
A 1 525 THR 525 525 525 THR THR A . n 
A 1 526 ARG 526 526 526 ARG ARG A . n 
A 1 527 SER 527 527 527 SER SER A . n 
A 1 528 THR 528 528 528 THR THR A . n 
A 1 529 PHE 529 529 529 PHE PHE A . n 
A 1 530 ALA 530 530 530 ALA ALA A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 SER 532 532 532 SER SER A . n 
A 1 533 GLY 533 533 533 GLY GLY A . n 
A 1 534 LYS 534 534 534 LYS LYS A . n 
A 1 535 PHE 535 535 535 PHE PHE A . n 
A 1 536 ALA 536 536 536 ALA ALA A . n 
A 1 537 ALA 537 537 537 ALA ALA A . n 
A 1 538 HIS 538 538 538 HIS HIS A . n 
A 1 539 TRP 539 539 539 TRP TRP A . n 
A 1 540 LEU 540 540 540 LEU LEU A . n 
A 1 541 GLY 541 541 541 GLY GLY A . n 
A 1 542 ASP 542 542 542 ASP ASP A . n 
A 1 543 ASN 543 543 543 ASN ASN A . n 
A 1 544 THR 544 544 544 THR THR A . n 
A 1 545 ALA 545 545 545 ALA ALA A . n 
A 1 546 THR 546 546 546 THR THR A . n 
A 1 547 TRP 547 547 547 TRP TRP A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 ASP 549 549 549 ASP ASP A . n 
A 1 550 LEU 550 550 550 LEU LEU A . n 
A 1 551 ARG 551 551 551 ARG ARG A . n 
A 1 552 TRP 552 552 552 TRP TRP A . n 
A 1 553 SER 553 553 553 SER SER A . n 
A 1 554 ILE 554 554 554 ILE ILE A . n 
A 1 555 PRO 555 555 555 PRO PRO A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 VAL 557 557 557 VAL VAL A . n 
A 1 558 LEU 558 558 558 LEU LEU A . n 
A 1 559 GLU 559 559 559 GLU GLU A . n 
A 1 560 PHE 560 560 560 PHE PHE A . n 
A 1 561 ASN 561 561 561 ASN ASN A . n 
A 1 562 LEU 562 562 562 LEU LEU A . n 
A 1 563 PHE 563 563 563 PHE PHE A . n 
A 1 564 GLY 564 564 564 GLY GLY A . n 
A 1 565 ILE 565 565 565 ILE ILE A . n 
A 1 566 PRO 566 566 566 PRO PRO A . n 
A 1 567 MET 567 567 567 MET MET A . n 
A 1 568 VAL 568 568 568 VAL VAL A . n 
A 1 569 GLY 569 569 569 GLY GLY A . n 
A 1 570 PRO 570 570 570 PRO PRO A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 ILE 572 572 572 ILE ILE A . n 
A 1 573 CYS 573 573 573 CYS CYS A . n 
A 1 574 GLY 574 574 574 GLY GLY A . n 
A 1 575 PHE 575 575 575 PHE PHE A . n 
A 1 576 ALA 576 576 576 ALA ALA A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 ASP 578 578 578 ASP ASP A . n 
A 1 579 THR 579 579 579 THR THR A . n 
A 1 580 PRO 580 580 580 PRO PRO A . n 
A 1 581 GLU 581 581 581 GLU GLU A . n 
A 1 582 GLU 582 582 582 GLU GLU A . n 
A 1 583 LEU 583 583 583 LEU LEU A . n 
A 1 584 CYS 584 584 584 CYS CYS A . n 
A 1 585 ARG 585 585 585 ARG ARG A . n 
A 1 586 ARG 586 586 586 ARG ARG A . n 
A 1 587 TRP 587 587 587 TRP TRP A . n 
A 1 588 MET 588 588 588 MET MET A . n 
A 1 589 GLN 589 589 589 GLN GLN A . n 
A 1 590 LEU 590 590 590 LEU LEU A . n 
A 1 591 GLY 591 591 591 GLY GLY A . n 
A 1 592 ALA 592 592 592 ALA ALA A . n 
A 1 593 PHE 593 593 593 PHE PHE A . n 
A 1 594 TYR 594 594 594 TYR TYR A . n 
A 1 595 PRO 595 595 595 PRO PRO A . n 
A 1 596 PHE 596 596 596 PHE PHE A . n 
A 1 597 SER 597 597 597 SER SER A . n 
A 1 598 ARG 598 598 598 ARG ARG A . n 
A 1 599 ASN 599 599 599 ASN ASN A . n 
A 1 600 HIS 600 600 600 HIS HIS A . n 
A 1 601 ASN 601 601 601 ASN ASN A . n 
A 1 602 GLY 602 602 602 GLY GLY A . n 
A 1 603 GLN 603 603 603 GLN GLN A . n 
A 1 604 GLY 604 604 604 GLY GLY A . n 
A 1 605 TYR 605 605 605 TYR TYR A . n 
A 1 606 LYS 606 606 606 LYS LYS A . n 
A 1 607 ASP 607 607 607 ASP ASP A . n 
A 1 608 GLN 608 608 608 GLN GLN A . n 
A 1 609 ASP 609 609 609 ASP ASP A . n 
A 1 610 PRO 610 610 610 PRO PRO A . n 
A 1 611 ALA 611 611 611 ALA ALA A . n 
A 1 612 SER 612 612 612 SER SER A . n 
A 1 613 PHE 613 613 613 PHE PHE A . n 
A 1 614 GLY 614 614 614 GLY GLY A . n 
A 1 615 ALA 615 615 615 ALA ALA A . n 
A 1 616 ASP 616 616 616 ASP ASP A . n 
A 1 617 SER 617 617 617 SER SER A . n 
A 1 618 LEU 618 618 618 LEU LEU A . n 
A 1 619 LEU 619 619 619 LEU LEU A . n 
A 1 620 LEU 620 620 620 LEU LEU A . n 
A 1 621 ASN 621 621 621 ASN ASN A . n 
A 1 622 SER 622 622 622 SER SER A . n 
A 1 623 SER 623 623 623 SER SER A . n 
A 1 624 ARG 624 624 624 ARG ARG A . n 
A 1 625 HIS 625 625 625 HIS HIS A . n 
A 1 626 TYR 626 626 626 TYR TYR A . n 
A 1 627 LEU 627 627 627 LEU LEU A . n 
A 1 628 ASN 628 628 628 ASN ASN A . n 
A 1 629 ILE 629 629 629 ILE ILE A . n 
A 1 630 ARG 630 630 630 ARG ARG A . n 
A 1 631 TYR 631 631 631 TYR TYR A . n 
A 1 632 THR 632 632 632 THR THR A . n 
A 1 633 LEU 633 633 633 LEU LEU A . n 
A 1 634 LEU 634 634 634 LEU LEU A . n 
A 1 635 PRO 635 635 635 PRO PRO A . n 
A 1 636 TYR 636 636 636 TYR TYR A . n 
A 1 637 LEU 637 637 637 LEU LEU A . n 
A 1 638 TYR 638 638 638 TYR TYR A . n 
A 1 639 THR 639 639 639 THR THR A . n 
A 1 640 LEU 640 640 640 LEU LEU A . n 
A 1 641 PHE 641 641 641 PHE PHE A . n 
A 1 642 PHE 642 642 642 PHE PHE A . n 
A 1 643 ARG 643 643 643 ARG ARG A . n 
A 1 644 ALA 644 644 644 ALA ALA A . n 
A 1 645 HIS 645 645 645 HIS HIS A . n 
A 1 646 SER 646 646 646 SER SER A . n 
A 1 647 ARG 647 647 647 ARG ARG A . n 
A 1 648 GLY 648 648 648 GLY GLY A . n 
A 1 649 ASP 649 649 649 ASP ASP A . n 
A 1 650 THR 650 650 650 THR THR A . n 
A 1 651 VAL 651 651 651 VAL VAL A . n 
A 1 652 ALA 652 652 652 ALA ALA A . n 
A 1 653 ARG 653 653 653 ARG ARG A . n 
A 1 654 PRO 654 654 654 PRO PRO A . n 
A 1 655 LEU 655 655 655 LEU LEU A . n 
A 1 656 LEU 656 656 656 LEU LEU A . n 
A 1 657 HIS 657 657 657 HIS HIS A . n 
A 1 658 GLU 658 658 658 GLU GLU A . n 
A 1 659 PHE 659 659 659 PHE PHE A . n 
A 1 660 TYR 660 660 660 TYR TYR A . n 
A 1 661 GLU 661 661 661 GLU GLU A . n 
A 1 662 ASP 662 662 662 ASP ASP A . n 
A 1 663 ASN 663 663 663 ASN ASN A . n 
A 1 664 SER 664 664 664 SER SER A . n 
A 1 665 THR 665 665 665 THR THR A . n 
A 1 666 TRP 666 666 666 TRP TRP A . n 
A 1 667 ASP 667 667 667 ASP ASP A . n 
A 1 668 VAL 668 668 668 VAL VAL A . n 
A 1 669 HIS 669 669 669 HIS HIS A . n 
A 1 670 GLN 670 670 670 GLN GLN A . n 
A 1 671 GLN 671 671 671 GLN GLN A . n 
A 1 672 PHE 672 672 672 PHE PHE A . n 
A 1 673 LEU 673 673 673 LEU LEU A . n 
A 1 674 TRP 674 674 674 TRP TRP A . n 
A 1 675 GLY 675 675 675 GLY GLY A . n 
A 1 676 PRO 676 676 676 PRO PRO A . n 
A 1 677 GLY 677 677 677 GLY GLY A . n 
A 1 678 LEU 678 678 678 LEU LEU A . n 
A 1 679 LEU 679 679 679 LEU LEU A . n 
A 1 680 ILE 680 680 680 ILE ILE A . n 
A 1 681 THR 681 681 681 THR THR A . n 
A 1 682 PRO 682 682 682 PRO PRO A . n 
A 1 683 VAL 683 683 683 VAL VAL A . n 
A 1 684 LEU 684 684 684 LEU LEU A . n 
A 1 685 ASP 685 685 685 ASP ASP A . n 
A 1 686 GLU 686 686 686 GLU GLU A . n 
A 1 687 GLY 687 687 687 GLY GLY A . n 
A 1 688 ALA 688 688 688 ALA ALA A . n 
A 1 689 GLU 689 689 689 GLU GLU A . n 
A 1 690 LYS 690 690 690 LYS LYS A . n 
A 1 691 VAL 691 691 691 VAL VAL A . n 
A 1 692 MET 692 692 692 MET MET A . n 
A 1 693 ALA 693 693 693 ALA ALA A . n 
A 1 694 TYR 694 694 694 TYR TYR A . n 
A 1 695 VAL 695 695 695 VAL VAL A . n 
A 1 696 PRO 696 696 696 PRO PRO A . n 
A 1 697 ASP 697 697 697 ASP ASP A . n 
A 1 698 ALA 698 698 698 ALA ALA A . n 
A 1 699 VAL 699 699 699 VAL VAL A . n 
A 1 700 TRP 700 700 700 TRP TRP A . n 
A 1 701 TYR 701 701 701 TYR TYR A . n 
A 1 702 ASP 702 702 702 ASP ASP A . n 
A 1 703 TYR 703 703 703 TYR TYR A . n 
A 1 704 GLU 704 704 704 GLU GLU A . n 
A 1 705 THR 705 705 705 THR THR A . n 
A 1 706 GLY 706 706 706 GLY GLY A . n 
A 1 707 SER 707 707 707 SER SER A . n 
A 1 708 GLN 708 708 708 GLN GLN A . n 
A 1 709 VAL 709 709 709 VAL VAL A . n 
A 1 710 ARG 710 710 710 ARG ARG A . n 
A 1 711 TRP 711 711 711 TRP TRP A . n 
A 1 712 ARG 712 712 712 ARG ARG A . n 
A 1 713 LYS 713 713 713 LYS LYS A . n 
A 1 714 GLN 714 714 714 GLN GLN A . n 
A 1 715 LYS 715 715 715 LYS LYS A . n 
A 1 716 VAL 716 716 716 VAL VAL A . n 
A 1 717 GLU 717 717 717 GLU GLU A . n 
A 1 718 MET 718 718 718 MET MET A . n 
A 1 719 GLU 719 719 719 GLU GLU A . n 
A 1 720 LEU 720 720 720 LEU LEU A . n 
A 1 721 PRO 721 721 721 PRO PRO A . n 
A 1 722 GLY 722 722 722 GLY GLY A . n 
A 1 723 ASP 723 723 723 ASP ASP A . n 
A 1 724 LYS 724 724 724 LYS LYS A . n 
A 1 725 ILE 725 725 725 ILE ILE A . n 
A 1 726 GLY 726 726 726 GLY GLY A . n 
A 1 727 LEU 727 727 727 LEU LEU A . n 
A 1 728 HIS 728 728 728 HIS HIS A . n 
A 1 729 LEU 729 729 729 LEU LEU A . n 
A 1 730 ARG 730 730 730 ARG ARG A . n 
A 1 731 GLY 731 731 731 GLY GLY A . n 
A 1 732 GLY 732 732 732 GLY GLY A . n 
A 1 733 TYR 733 733 733 TYR TYR A . n 
A 1 734 ILE 734 734 734 ILE ILE A . n 
A 1 735 PHE 735 735 735 PHE PHE A . n 
A 1 736 PRO 736 736 736 PRO PRO A . n 
A 1 737 THR 737 737 737 THR THR A . n 
A 1 738 GLN 738 738 738 GLN GLN A . n 
A 1 739 GLN 739 739 739 GLN GLN A . n 
A 1 740 PRO 740 740 740 PRO PRO A . n 
A 1 741 ASN 741 741 741 ASN ASN A . n 
A 1 742 THR 742 742 742 THR THR A . n 
A 1 743 THR 743 743 743 THR THR A . n 
A 1 744 THR 744 744 744 THR THR A . n 
A 1 745 LEU 745 745 745 LEU LEU A . n 
A 1 746 ALA 746 746 746 ALA ALA A . n 
A 1 747 SER 747 747 747 SER SER A . n 
A 1 748 ARG 748 748 748 ARG ARG A . n 
A 1 749 LYS 749 749 749 LYS LYS A . n 
A 1 750 ASN 750 750 750 ASN ASN A . n 
A 1 751 PRO 751 751 751 PRO PRO A . n 
A 1 752 LEU 752 752 752 LEU LEU A . n 
A 1 753 GLY 753 753 753 GLY GLY A . n 
A 1 754 LEU 754 754 754 LEU LEU A . n 
A 1 755 ILE 755 755 755 ILE ILE A . n 
A 1 756 ILE 756 756 756 ILE ILE A . n 
A 1 757 ALA 757 757 757 ALA ALA A . n 
A 1 758 LEU 758 758 758 LEU LEU A . n 
A 1 759 ASP 759 759 759 ASP ASP A . n 
A 1 760 GLU 760 760 760 GLU GLU A . n 
A 1 761 ASN 761 761 761 ASN ASN A . n 
A 1 762 LYS 762 762 762 LYS LYS A . n 
A 1 763 GLU 763 763 763 GLU GLU A . n 
A 1 764 ALA 764 764 764 ALA ALA A . n 
A 1 765 LYS 765 765 765 LYS LYS A . n 
A 1 766 GLY 766 766 766 GLY GLY A . n 
A 1 767 GLU 767 767 767 GLU GLU A . n 
A 1 768 LEU 768 768 768 LEU LEU A . n 
A 1 769 PHE 769 769 769 PHE PHE A . n 
A 1 770 TRP 770 770 770 TRP TRP A . n 
A 1 771 ASP 771 771 771 ASP ASP A . n 
A 1 772 ASP 772 772 772 ASP ASP A . n 
A 1 773 GLY 773 773 773 GLY GLY A . n 
A 1 774 GLU 774 774 774 GLU GLU A . n 
A 1 775 THR 775 775 775 THR THR A . n 
A 1 776 LYS 776 776 776 LYS LYS A . n 
A 1 777 ASP 777 777 777 ASP ASP A . n 
A 1 778 THR 778 778 778 THR THR A . n 
A 1 779 VAL 779 779 779 VAL VAL A . n 
A 1 780 ALA 780 780 780 ALA ALA A . n 
A 1 781 ASN 781 781 781 ASN ASN A . n 
A 1 782 LYS 782 782 782 LYS LYS A . n 
A 1 783 VAL 783 783 783 VAL VAL A . n 
A 1 784 TYR 784 784 784 TYR TYR A . n 
A 1 785 LEU 785 785 785 LEU LEU A . n 
A 1 786 LEU 786 786 786 LEU LEU A . n 
A 1 787 CYS 787 787 787 CYS CYS A . n 
A 1 788 GLU 788 788 788 GLU GLU A . n 
A 1 789 PHE 789 789 789 PHE PHE A . n 
A 1 790 SER 790 790 790 SER SER A . n 
A 1 791 VAL 791 791 791 VAL VAL A . n 
A 1 792 THR 792 792 792 THR THR A . n 
A 1 793 GLN 793 793 793 GLN GLN A . n 
A 1 794 ASN 794 794 794 ASN ASN A . n 
A 1 795 ARG 795 795 795 ARG ARG A . n 
A 1 796 LEU 796 796 796 LEU LEU A . n 
A 1 797 GLU 797 797 797 GLU GLU A . n 
A 1 798 VAL 798 798 798 VAL VAL A . n 
A 1 799 ASN 799 799 799 ASN ASN A . n 
A 1 800 ILE 800 800 800 ILE ILE A . n 
A 1 801 SER 801 801 801 SER SER A . n 
A 1 802 GLN 802 802 802 GLN GLN A . n 
A 1 803 SER 803 803 803 SER SER A . n 
A 1 804 THR 804 804 804 THR THR A . n 
A 1 805 TYR 805 805 805 TYR TYR A . n 
A 1 806 LYS 806 806 806 LYS LYS A . n 
A 1 807 ASP 807 807 807 ASP ASP A . n 
A 1 808 PRO 808 808 808 PRO PRO A . n 
A 1 809 ASN 809 809 809 ASN ASN A . n 
A 1 810 ASN 810 810 810 ASN ASN A . n 
A 1 811 LEU 811 811 811 LEU LEU A . n 
A 1 812 ALA 812 812 812 ALA ALA A . n 
A 1 813 PHE 813 813 813 PHE PHE A . n 
A 1 814 ASN 814 814 814 ASN ASN A . n 
A 1 815 GLU 815 815 815 GLU GLU A . n 
A 1 816 ILE 816 816 816 ILE ILE A . n 
A 1 817 LYS 817 817 817 LYS LYS A . n 
A 1 818 ILE 818 818 818 ILE ILE A . n 
A 1 819 LEU 819 819 819 LEU LEU A . n 
A 1 820 GLY 820 820 820 GLY GLY A . n 
A 1 821 THR 821 821 821 THR THR A . n 
A 1 822 GLU 822 822 822 GLU GLU A . n 
A 1 823 GLU 823 823 823 GLU GLU A . n 
A 1 824 PRO 824 824 824 PRO PRO A . n 
A 1 825 SER 825 825 825 SER SER A . n 
A 1 826 ASN 826 826 826 ASN ASN A . n 
A 1 827 VAL 827 827 827 VAL VAL A . n 
A 1 828 THR 828 828 828 THR THR A . n 
A 1 829 VAL 829 829 829 VAL VAL A . n 
A 1 830 LYS 830 830 830 LYS LYS A . n 
A 1 831 HIS 831 831 831 HIS HIS A . n 
A 1 832 ASN 832 832 832 ASN ASN A . n 
A 1 833 GLY 833 833 833 GLY GLY A . n 
A 1 834 VAL 834 834 834 VAL VAL A . n 
A 1 835 PRO 835 835 835 PRO PRO A . n 
A 1 836 SER 836 836 836 SER SER A . n 
A 1 837 GLN 837 837 ?   ?   ?   A . n 
A 1 838 THR 838 838 838 THR THR A . n 
A 1 839 SER 839 839 839 SER SER A . n 
A 1 840 PRO 840 840 840 PRO PRO A . n 
A 1 841 THR 841 841 841 THR THR A . n 
A 1 842 VAL 842 842 842 VAL VAL A . n 
A 1 843 THR 843 843 843 THR THR A . n 
A 1 844 TYR 844 844 844 TYR TYR A . n 
A 1 845 ASP 845 845 845 ASP ASP A . n 
A 1 846 SER 846 846 846 SER SER A . n 
A 1 847 ASN 847 847 847 ASN ASN A . n 
A 1 848 LEU 848 848 848 LEU LEU A . n 
A 1 849 LYS 849 849 849 LYS LYS A . n 
A 1 850 VAL 850 850 850 VAL VAL A . n 
A 1 851 ALA 851 851 851 ALA ALA A . n 
A 1 852 ILE 852 852 852 ILE ILE A . n 
A 1 853 ILE 853 853 853 ILE ILE A . n 
A 1 854 THR 854 854 854 THR THR A . n 
A 1 855 ASP 855 855 855 ASP ASP A . n 
A 1 856 ILE 856 856 856 ILE ILE A . n 
A 1 857 ASP 857 857 857 ASP ASP A . n 
A 1 858 LEU 858 858 858 LEU LEU A . n 
A 1 859 LEU 859 859 859 LEU LEU A . n 
A 1 860 LEU 860 860 860 LEU LEU A . n 
A 1 861 GLY 861 861 861 GLY GLY A . n 
A 1 862 GLU 862 862 862 GLU GLU A . n 
A 1 863 ALA 863 863 863 ALA ALA A . n 
A 1 864 TYR 864 864 864 TYR TYR A . n 
A 1 865 THR 865 865 865 THR THR A . n 
A 1 866 VAL 866 866 866 VAL VAL A . n 
A 1 867 GLU 867 867 867 GLU GLU A . n 
A 1 868 TRP 868 868 868 TRP TRP A . n 
A 1 869 ALA 869 869 869 ALA ALA A . n 
A 1 870 HIS 870 870 870 HIS HIS 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 
B 2 ACR 1   1001 1001 ACR ACR A . 
C 3 NAG 1   2001 2001 NAG NAG A . 
D 3 NAG 1   2005 2005 NAG NAG A . 
E 4 SO4 1   4001 4001 SO4 SO4 A . 
F 5 GOL 1   3001 3001 GOL GOL A . 
G 5 GOL 1   3002 3002 GOL GOL A . 
H 5 GOL 1   3003 3003 GOL GOL A . 
I 5 GOL 1   3004 3004 GOL GOL A . 
J 5 GOL 1   3005 3005 GOL GOL A . 
K 5 GOL 1   3006 3006 GOL GOL A . 
L 5 GOL 1   3007 3007 GOL GOL A . 
M 5 GOL 1   3008 3008 GOL GOL A . 
N 5 GOL 1   3009 3009 GOL GOL A . 
O 3 NAG 1   2003 2003 NAG NAG X . 
P 3 NAG 2   2004 2004 NAG NAG X . 
Q 6 HOH 1   4002 1    HOH HOH A . 
Q 6 HOH 2   4003 2    HOH HOH A . 
Q 6 HOH 3   4004 3    HOH HOH A . 
Q 6 HOH 4   4005 4    HOH HOH A . 
Q 6 HOH 5   4006 5    HOH HOH A . 
Q 6 HOH 6   4007 6    HOH HOH A . 
Q 6 HOH 7   4008 7    HOH HOH A . 
Q 6 HOH 8   4009 8    HOH HOH A . 
Q 6 HOH 9   4010 9    HOH HOH A . 
Q 6 HOH 10  4011 10   HOH HOH A . 
Q 6 HOH 11  4012 11   HOH HOH A . 
Q 6 HOH 12  4013 12   HOH HOH A . 
Q 6 HOH 13  4014 13   HOH HOH A . 
Q 6 HOH 14  4015 14   HOH HOH A . 
Q 6 HOH 15  4016 15   HOH HOH A . 
Q 6 HOH 16  4017 16   HOH HOH A . 
Q 6 HOH 17  4018 17   HOH HOH A . 
Q 6 HOH 18  4019 18   HOH HOH A . 
Q 6 HOH 19  4020 19   HOH HOH A . 
Q 6 HOH 20  4021 20   HOH HOH A . 
Q 6 HOH 21  4022 21   HOH HOH A . 
Q 6 HOH 22  4023 22   HOH HOH A . 
Q 6 HOH 23  4024 23   HOH HOH A . 
Q 6 HOH 24  4025 24   HOH HOH A . 
Q 6 HOH 25  4026 25   HOH HOH A . 
Q 6 HOH 26  4027 26   HOH HOH A . 
Q 6 HOH 27  4028 27   HOH HOH A . 
Q 6 HOH 28  4029 28   HOH HOH A . 
Q 6 HOH 29  4030 29   HOH HOH A . 
Q 6 HOH 30  4031 30   HOH HOH A . 
Q 6 HOH 31  4032 31   HOH HOH A . 
Q 6 HOH 32  4033 32   HOH HOH A . 
Q 6 HOH 33  4034 33   HOH HOH A . 
Q 6 HOH 34  4035 34   HOH HOH A . 
Q 6 HOH 35  4036 35   HOH HOH A . 
Q 6 HOH 36  4037 36   HOH HOH A . 
Q 6 HOH 37  4038 37   HOH HOH A . 
Q 6 HOH 38  4039 38   HOH HOH A . 
Q 6 HOH 39  4040 39   HOH HOH A . 
Q 6 HOH 40  4041 40   HOH HOH A . 
Q 6 HOH 41  4042 41   HOH HOH A . 
Q 6 HOH 42  4043 43   HOH HOH A . 
Q 6 HOH 43  4044 44   HOH HOH A . 
Q 6 HOH 44  4045 45   HOH HOH A . 
Q 6 HOH 45  4046 46   HOH HOH A . 
Q 6 HOH 46  4047 47   HOH HOH A . 
Q 6 HOH 47  4048 48   HOH HOH A . 
Q 6 HOH 48  4049 49   HOH HOH A . 
Q 6 HOH 49  4050 50   HOH HOH A . 
Q 6 HOH 50  4051 51   HOH HOH A . 
Q 6 HOH 51  4052 52   HOH HOH A . 
Q 6 HOH 52  4053 53   HOH HOH A . 
Q 6 HOH 53  4054 55   HOH HOH A . 
Q 6 HOH 54  4055 56   HOH HOH A . 
Q 6 HOH 55  4056 57   HOH HOH A . 
Q 6 HOH 56  4057 58   HOH HOH A . 
Q 6 HOH 57  4058 59   HOH HOH A . 
Q 6 HOH 58  4059 60   HOH HOH A . 
Q 6 HOH 59  4060 61   HOH HOH A . 
Q 6 HOH 60  4061 62   HOH HOH A . 
Q 6 HOH 61  4062 63   HOH HOH A . 
Q 6 HOH 62  4063 64   HOH HOH A . 
Q 6 HOH 63  4064 66   HOH HOH A . 
Q 6 HOH 64  4065 67   HOH HOH A . 
Q 6 HOH 65  4066 68   HOH HOH A . 
Q 6 HOH 66  4067 69   HOH HOH A . 
Q 6 HOH 67  4068 70   HOH HOH A . 
Q 6 HOH 68  4069 72   HOH HOH A . 
Q 6 HOH 69  4070 73   HOH HOH A . 
Q 6 HOH 70  4071 75   HOH HOH A . 
Q 6 HOH 71  4072 76   HOH HOH A . 
Q 6 HOH 72  4073 77   HOH HOH A . 
Q 6 HOH 73  4074 78   HOH HOH A . 
Q 6 HOH 74  4075 79   HOH HOH A . 
Q 6 HOH 75  4076 80   HOH HOH A . 
Q 6 HOH 76  4077 81   HOH HOH A . 
Q 6 HOH 77  4078 82   HOH HOH A . 
Q 6 HOH 78  4079 83   HOH HOH A . 
Q 6 HOH 79  4080 84   HOH HOH A . 
Q 6 HOH 80  4081 85   HOH HOH A . 
Q 6 HOH 81  4082 86   HOH HOH A . 
Q 6 HOH 82  4083 87   HOH HOH A . 
Q 6 HOH 83  4084 88   HOH HOH A . 
Q 6 HOH 84  4085 89   HOH HOH A . 
Q 6 HOH 85  4086 90   HOH HOH A . 
Q 6 HOH 86  4087 91   HOH HOH A . 
Q 6 HOH 87  4088 93   HOH HOH A . 
Q 6 HOH 88  4089 94   HOH HOH A . 
Q 6 HOH 89  4090 95   HOH HOH A . 
Q 6 HOH 90  4091 96   HOH HOH A . 
Q 6 HOH 91  4092 97   HOH HOH A . 
Q 6 HOH 92  4093 98   HOH HOH A . 
Q 6 HOH 93  4094 99   HOH HOH A . 
Q 6 HOH 94  4095 100  HOH HOH A . 
Q 6 HOH 95  4096 101  HOH HOH A . 
Q 6 HOH 96  4097 102  HOH HOH A . 
Q 6 HOH 97  4098 103  HOH HOH A . 
Q 6 HOH 98  4099 104  HOH HOH A . 
Q 6 HOH 99  4100 105  HOH HOH A . 
Q 6 HOH 100 4101 107  HOH HOH A . 
Q 6 HOH 101 4102 108  HOH HOH A . 
Q 6 HOH 102 4103 109  HOH HOH A . 
Q 6 HOH 103 4104 111  HOH HOH A . 
Q 6 HOH 104 4105 112  HOH HOH A . 
Q 6 HOH 105 4106 114  HOH HOH A . 
Q 6 HOH 106 4107 115  HOH HOH A . 
Q 6 HOH 107 4108 116  HOH HOH A . 
Q 6 HOH 108 4109 118  HOH HOH A . 
Q 6 HOH 109 4110 120  HOH HOH A . 
Q 6 HOH 110 4111 121  HOH HOH A . 
Q 6 HOH 111 4112 122  HOH HOH A . 
Q 6 HOH 112 4113 123  HOH HOH A . 
Q 6 HOH 113 4114 124  HOH HOH A . 
Q 6 HOH 114 4115 125  HOH HOH A . 
Q 6 HOH 115 4116 126  HOH HOH A . 
Q 6 HOH 116 4117 127  HOH HOH A . 
Q 6 HOH 117 4118 128  HOH HOH A . 
Q 6 HOH 118 4119 129  HOH HOH A . 
Q 6 HOH 119 4120 130  HOH HOH A . 
Q 6 HOH 120 4121 131  HOH HOH A . 
Q 6 HOH 121 4122 132  HOH HOH A . 
Q 6 HOH 122 4123 133  HOH HOH A . 
Q 6 HOH 123 4124 134  HOH HOH A . 
Q 6 HOH 124 4125 135  HOH HOH A . 
Q 6 HOH 125 4126 136  HOH HOH A . 
Q 6 HOH 126 4127 137  HOH HOH A . 
Q 6 HOH 127 4128 138  HOH HOH A . 
Q 6 HOH 128 4129 139  HOH HOH A . 
Q 6 HOH 129 4130 140  HOH HOH A . 
Q 6 HOH 130 4131 141  HOH HOH A . 
Q 6 HOH 131 4132 142  HOH HOH A . 
Q 6 HOH 132 4133 143  HOH HOH A . 
Q 6 HOH 133 4134 144  HOH HOH A . 
Q 6 HOH 134 4135 145  HOH HOH A . 
Q 6 HOH 135 4136 146  HOH HOH A . 
Q 6 HOH 136 4137 147  HOH HOH A . 
Q 6 HOH 137 4138 148  HOH HOH A . 
Q 6 HOH 138 4139 149  HOH HOH A . 
Q 6 HOH 139 4140 150  HOH HOH A . 
Q 6 HOH 140 4141 151  HOH HOH A . 
Q 6 HOH 141 4142 152  HOH HOH A . 
Q 6 HOH 142 4143 154  HOH HOH A . 
Q 6 HOH 143 4144 157  HOH HOH A . 
Q 6 HOH 144 4145 158  HOH HOH A . 
Q 6 HOH 145 4146 159  HOH HOH A . 
Q 6 HOH 146 4147 160  HOH HOH A . 
Q 6 HOH 147 4148 161  HOH HOH A . 
Q 6 HOH 148 4149 162  HOH HOH A . 
Q 6 HOH 149 4150 163  HOH HOH A . 
Q 6 HOH 150 4151 164  HOH HOH A . 
Q 6 HOH 151 4152 165  HOH HOH A . 
Q 6 HOH 152 4153 166  HOH HOH A . 
Q 6 HOH 153 4154 167  HOH HOH A . 
Q 6 HOH 154 4155 168  HOH HOH A . 
Q 6 HOH 155 4156 169  HOH HOH A . 
Q 6 HOH 156 4157 170  HOH HOH A . 
Q 6 HOH 157 4158 171  HOH HOH A . 
Q 6 HOH 158 4159 172  HOH HOH A . 
Q 6 HOH 159 4160 173  HOH HOH A . 
Q 6 HOH 160 4161 175  HOH HOH A . 
Q 6 HOH 161 4162 177  HOH HOH A . 
Q 6 HOH 162 4163 178  HOH HOH A . 
Q 6 HOH 163 4164 179  HOH HOH A . 
Q 6 HOH 164 4165 180  HOH HOH A . 
Q 6 HOH 165 4166 182  HOH HOH A . 
Q 6 HOH 166 4167 184  HOH HOH A . 
Q 6 HOH 167 4168 185  HOH HOH A . 
Q 6 HOH 168 4169 187  HOH HOH A . 
Q 6 HOH 169 4170 188  HOH HOH A . 
Q 6 HOH 170 4171 189  HOH HOH A . 
Q 6 HOH 171 4172 190  HOH HOH A . 
Q 6 HOH 172 4173 191  HOH HOH A . 
Q 6 HOH 173 4174 192  HOH HOH A . 
Q 6 HOH 174 4175 193  HOH HOH A . 
Q 6 HOH 175 4176 194  HOH HOH A . 
Q 6 HOH 176 4177 195  HOH HOH A . 
Q 6 HOH 177 4178 196  HOH HOH A . 
Q 6 HOH 178 4179 197  HOH HOH A . 
Q 6 HOH 179 4180 198  HOH HOH A . 
Q 6 HOH 180 4181 199  HOH HOH A . 
Q 6 HOH 181 4182 200  HOH HOH A . 
Q 6 HOH 182 4183 201  HOH HOH A . 
Q 6 HOH 183 4184 202  HOH HOH A . 
Q 6 HOH 184 4185 203  HOH HOH A . 
Q 6 HOH 185 4186 204  HOH HOH A . 
Q 6 HOH 186 4187 206  HOH HOH A . 
Q 6 HOH 187 4188 207  HOH HOH A . 
Q 6 HOH 188 4189 208  HOH HOH A . 
Q 6 HOH 189 4190 209  HOH HOH A . 
Q 6 HOH 190 4191 211  HOH HOH A . 
Q 6 HOH 191 4192 213  HOH HOH A . 
Q 6 HOH 192 4193 214  HOH HOH A . 
Q 6 HOH 193 4194 215  HOH HOH A . 
Q 6 HOH 194 4195 216  HOH HOH A . 
Q 6 HOH 195 4196 217  HOH HOH A . 
Q 6 HOH 196 4197 218  HOH HOH A . 
Q 6 HOH 197 4198 219  HOH HOH A . 
Q 6 HOH 198 4199 220  HOH HOH A . 
Q 6 HOH 199 4200 221  HOH HOH A . 
Q 6 HOH 200 4201 222  HOH HOH A . 
Q 6 HOH 201 4202 223  HOH HOH A . 
Q 6 HOH 202 4203 225  HOH HOH A . 
Q 6 HOH 203 4204 226  HOH HOH A . 
Q 6 HOH 204 4205 227  HOH HOH A . 
Q 6 HOH 205 4206 228  HOH HOH A . 
Q 6 HOH 206 4207 229  HOH HOH A . 
Q 6 HOH 207 4208 230  HOH HOH A . 
Q 6 HOH 208 4209 232  HOH HOH A . 
Q 6 HOH 209 4210 233  HOH HOH A . 
Q 6 HOH 210 4211 234  HOH HOH A . 
Q 6 HOH 211 4212 237  HOH HOH A . 
Q 6 HOH 212 4213 238  HOH HOH A . 
Q 6 HOH 213 4214 239  HOH HOH A . 
Q 6 HOH 214 4215 240  HOH HOH A . 
Q 6 HOH 215 4216 241  HOH HOH A . 
Q 6 HOH 216 4217 242  HOH HOH A . 
Q 6 HOH 217 4218 244  HOH HOH A . 
Q 6 HOH 218 4219 245  HOH HOH A . 
Q 6 HOH 219 4220 246  HOH HOH A . 
Q 6 HOH 220 4221 247  HOH HOH A . 
Q 6 HOH 221 4222 248  HOH HOH A . 
Q 6 HOH 222 4223 249  HOH HOH A . 
Q 6 HOH 223 4224 250  HOH HOH A . 
Q 6 HOH 224 4225 251  HOH HOH A . 
Q 6 HOH 225 4226 252  HOH HOH A . 
Q 6 HOH 226 4227 255  HOH HOH A . 
Q 6 HOH 227 4228 256  HOH HOH A . 
Q 6 HOH 228 4229 257  HOH HOH A . 
Q 6 HOH 229 4230 258  HOH HOH A . 
Q 6 HOH 230 4231 259  HOH HOH A . 
Q 6 HOH 231 4232 260  HOH HOH A . 
Q 6 HOH 232 4233 261  HOH HOH A . 
Q 6 HOH 233 4234 262  HOH HOH A . 
Q 6 HOH 234 4235 263  HOH HOH A . 
Q 6 HOH 235 4236 264  HOH HOH A . 
Q 6 HOH 236 4237 265  HOH HOH A . 
Q 6 HOH 237 4238 266  HOH HOH A . 
Q 6 HOH 238 4239 267  HOH HOH A . 
Q 6 HOH 239 4240 269  HOH HOH A . 
Q 6 HOH 240 4241 271  HOH HOH A . 
Q 6 HOH 241 4242 272  HOH HOH A . 
Q 6 HOH 242 4243 273  HOH HOH A . 
Q 6 HOH 243 4244 275  HOH HOH A . 
Q 6 HOH 244 4245 276  HOH HOH A . 
Q 6 HOH 245 4246 277  HOH HOH A . 
Q 6 HOH 246 4247 278  HOH HOH A . 
Q 6 HOH 247 4248 279  HOH HOH A . 
Q 6 HOH 248 4249 280  HOH HOH A . 
Q 6 HOH 249 4250 281  HOH HOH A . 
Q 6 HOH 250 4251 282  HOH HOH A . 
Q 6 HOH 251 4252 283  HOH HOH A . 
Q 6 HOH 252 4253 284  HOH HOH A . 
Q 6 HOH 253 4254 285  HOH HOH A . 
Q 6 HOH 254 4255 286  HOH HOH A . 
Q 6 HOH 255 4256 287  HOH HOH A . 
Q 6 HOH 256 4257 288  HOH HOH A . 
Q 6 HOH 257 4258 289  HOH HOH A . 
Q 6 HOH 258 4259 290  HOH HOH A . 
Q 6 HOH 259 4260 291  HOH HOH A . 
Q 6 HOH 260 4261 292  HOH HOH A . 
Q 6 HOH 261 4262 294  HOH HOH A . 
Q 6 HOH 262 4263 295  HOH HOH A . 
Q 6 HOH 263 4264 296  HOH HOH A . 
Q 6 HOH 264 4265 297  HOH HOH A . 
Q 6 HOH 265 4266 298  HOH HOH A . 
Q 6 HOH 266 4267 299  HOH HOH A . 
Q 6 HOH 267 4268 301  HOH HOH A . 
Q 6 HOH 268 4269 302  HOH HOH A . 
Q 6 HOH 269 4270 303  HOH HOH A . 
Q 6 HOH 270 4271 306  HOH HOH A . 
Q 6 HOH 271 4272 307  HOH HOH A . 
Q 6 HOH 272 4273 308  HOH HOH A . 
Q 6 HOH 273 4274 309  HOH HOH A . 
Q 6 HOH 274 4275 310  HOH HOH A . 
Q 6 HOH 275 4276 311  HOH HOH A . 
Q 6 HOH 276 4277 312  HOH HOH A . 
Q 6 HOH 277 4278 313  HOH HOH A . 
Q 6 HOH 278 4279 315  HOH HOH A . 
Q 6 HOH 279 4280 316  HOH HOH A . 
Q 6 HOH 280 4281 317  HOH HOH A . 
Q 6 HOH 281 4282 318  HOH HOH A . 
Q 6 HOH 282 4283 319  HOH HOH A . 
Q 6 HOH 283 4284 320  HOH HOH A . 
Q 6 HOH 284 4285 321  HOH HOH A . 
Q 6 HOH 285 4286 322  HOH HOH A . 
Q 6 HOH 286 4287 323  HOH HOH A . 
Q 6 HOH 287 4288 324  HOH HOH A . 
Q 6 HOH 288 4289 325  HOH HOH A . 
Q 6 HOH 289 4290 326  HOH HOH A . 
Q 6 HOH 290 4291 327  HOH HOH A . 
Q 6 HOH 291 4292 328  HOH HOH A . 
Q 6 HOH 292 4293 329  HOH HOH A . 
Q 6 HOH 293 4294 331  HOH HOH A . 
Q 6 HOH 294 4295 332  HOH HOH A . 
Q 6 HOH 295 4296 333  HOH HOH A . 
Q 6 HOH 296 4297 334  HOH HOH A . 
Q 6 HOH 297 4298 335  HOH HOH A . 
Q 6 HOH 298 4299 336  HOH HOH A . 
Q 6 HOH 299 4300 337  HOH HOH A . 
Q 6 HOH 300 4301 338  HOH HOH A . 
Q 6 HOH 301 4302 339  HOH HOH A . 
Q 6 HOH 302 4303 340  HOH HOH A . 
Q 6 HOH 303 4304 341  HOH HOH A . 
Q 6 HOH 304 4305 342  HOH HOH A . 
Q 6 HOH 305 4306 343  HOH HOH A . 
Q 6 HOH 306 4307 345  HOH HOH A . 
Q 6 HOH 307 4308 346  HOH HOH A . 
Q 6 HOH 308 4309 347  HOH HOH A . 
Q 6 HOH 309 4310 348  HOH HOH A . 
Q 6 HOH 310 4311 349  HOH HOH A . 
Q 6 HOH 311 4312 350  HOH HOH A . 
Q 6 HOH 312 4313 351  HOH HOH A . 
Q 6 HOH 313 4314 352  HOH HOH A . 
Q 6 HOH 314 4315 353  HOH HOH A . 
Q 6 HOH 315 4316 354  HOH HOH A . 
Q 6 HOH 316 4317 356  HOH HOH A . 
Q 6 HOH 317 4318 357  HOH HOH A . 
Q 6 HOH 318 4319 358  HOH HOH A . 
Q 6 HOH 319 4320 359  HOH HOH A . 
Q 6 HOH 320 4321 360  HOH HOH A . 
Q 6 HOH 321 4322 361  HOH HOH A . 
Q 6 HOH 322 4323 362  HOH HOH A . 
Q 6 HOH 323 4324 363  HOH HOH A . 
Q 6 HOH 324 4325 364  HOH HOH A . 
Q 6 HOH 325 4326 365  HOH HOH A . 
Q 6 HOH 326 4327 366  HOH HOH A . 
Q 6 HOH 327 4328 367  HOH HOH A . 
Q 6 HOH 328 4329 368  HOH HOH A . 
Q 6 HOH 329 4330 369  HOH HOH A . 
Q 6 HOH 330 4331 370  HOH HOH A . 
Q 6 HOH 331 4332 371  HOH HOH A . 
Q 6 HOH 332 4333 372  HOH HOH A . 
Q 6 HOH 333 4334 373  HOH HOH A . 
Q 6 HOH 334 4335 374  HOH HOH A . 
Q 6 HOH 335 4336 375  HOH HOH A . 
Q 6 HOH 336 4337 376  HOH HOH A . 
Q 6 HOH 337 4338 377  HOH HOH A . 
Q 6 HOH 338 4339 379  HOH HOH A . 
Q 6 HOH 339 4340 382  HOH HOH A . 
Q 6 HOH 340 4341 383  HOH HOH A . 
Q 6 HOH 341 4342 384  HOH HOH A . 
Q 6 HOH 342 4343 385  HOH HOH A . 
Q 6 HOH 343 4344 386  HOH HOH A . 
Q 6 HOH 344 4345 387  HOH HOH A . 
Q 6 HOH 345 4346 388  HOH HOH A . 
Q 6 HOH 346 4347 389  HOH HOH A . 
Q 6 HOH 347 4348 390  HOH HOH A . 
Q 6 HOH 348 4349 391  HOH HOH A . 
Q 6 HOH 349 4350 392  HOH HOH A . 
Q 6 HOH 350 4351 393  HOH HOH A . 
Q 6 HOH 351 4352 395  HOH HOH A . 
Q 6 HOH 352 4353 396  HOH HOH A . 
Q 6 HOH 353 4354 397  HOH HOH A . 
Q 6 HOH 354 4355 398  HOH HOH A . 
Q 6 HOH 355 4356 399  HOH HOH A . 
Q 6 HOH 356 4357 400  HOH HOH A . 
Q 6 HOH 357 4358 402  HOH HOH A . 
Q 6 HOH 358 4359 403  HOH HOH A . 
Q 6 HOH 359 4360 404  HOH HOH A . 
Q 6 HOH 360 4361 405  HOH HOH A . 
Q 6 HOH 361 4362 406  HOH HOH A . 
Q 6 HOH 362 4363 407  HOH HOH A . 
Q 6 HOH 363 4364 408  HOH HOH A . 
Q 6 HOH 364 4365 409  HOH HOH A . 
Q 6 HOH 365 4366 410  HOH HOH A . 
Q 6 HOH 366 4367 411  HOH HOH A . 
Q 6 HOH 367 4368 413  HOH HOH A . 
Q 6 HOH 368 4369 414  HOH HOH A . 
Q 6 HOH 369 4370 415  HOH HOH A . 
Q 6 HOH 370 4371 416  HOH HOH A . 
Q 6 HOH 371 4372 417  HOH HOH A . 
Q 6 HOH 372 4373 419  HOH HOH A . 
Q 6 HOH 373 4374 420  HOH HOH A . 
Q 6 HOH 374 4375 421  HOH HOH A . 
Q 6 HOH 375 4376 422  HOH HOH A . 
Q 6 HOH 376 4377 423  HOH HOH A . 
Q 6 HOH 377 4378 424  HOH HOH A . 
Q 6 HOH 378 4379 425  HOH HOH A . 
Q 6 HOH 379 4380 426  HOH HOH A . 
Q 6 HOH 380 4381 427  HOH HOH A . 
Q 6 HOH 381 4382 428  HOH HOH A . 
Q 6 HOH 382 4383 429  HOH HOH A . 
Q 6 HOH 383 4384 431  HOH HOH A . 
Q 6 HOH 384 4385 432  HOH HOH A . 
Q 6 HOH 385 4386 433  HOH HOH A . 
Q 6 HOH 386 4387 435  HOH HOH A . 
Q 6 HOH 387 4388 436  HOH HOH A . 
Q 6 HOH 388 4389 437  HOH HOH A . 
Q 6 HOH 389 4390 438  HOH HOH A . 
Q 6 HOH 390 4391 441  HOH HOH A . 
Q 6 HOH 391 4392 442  HOH HOH A . 
Q 6 HOH 392 4393 443  HOH HOH A . 
Q 6 HOH 393 4394 444  HOH HOH A . 
Q 6 HOH 394 4395 445  HOH HOH A . 
Q 6 HOH 395 4396 446  HOH HOH A . 
Q 6 HOH 396 4397 447  HOH HOH A . 
Q 6 HOH 397 4398 448  HOH HOH A . 
Q 6 HOH 398 4399 449  HOH HOH A . 
Q 6 HOH 399 4400 450  HOH HOH A . 
Q 6 HOH 400 4401 451  HOH HOH A . 
Q 6 HOH 401 4402 453  HOH HOH A . 
Q 6 HOH 402 4403 454  HOH HOH A . 
Q 6 HOH 403 4404 455  HOH HOH A . 
Q 6 HOH 404 4405 456  HOH HOH A . 
Q 6 HOH 405 4406 457  HOH HOH A . 
Q 6 HOH 406 4407 458  HOH HOH A . 
Q 6 HOH 407 4408 459  HOH HOH A . 
Q 6 HOH 408 4409 460  HOH HOH A . 
Q 6 HOH 409 4410 461  HOH HOH A . 
Q 6 HOH 410 4411 462  HOH HOH A . 
Q 6 HOH 411 4412 463  HOH HOH A . 
Q 6 HOH 412 4413 464  HOH HOH A . 
Q 6 HOH 413 4414 465  HOH HOH A . 
Q 6 HOH 414 4415 466  HOH HOH A . 
Q 6 HOH 415 4416 467  HOH HOH A . 
Q 6 HOH 416 4417 468  HOH HOH A . 
Q 6 HOH 417 4418 470  HOH HOH A . 
Q 6 HOH 418 4419 472  HOH HOH A . 
Q 6 HOH 419 4420 473  HOH HOH A . 
Q 6 HOH 420 4421 474  HOH HOH A . 
Q 6 HOH 421 4422 475  HOH HOH A . 
Q 6 HOH 422 4423 476  HOH HOH A . 
Q 6 HOH 423 4424 477  HOH HOH A . 
Q 6 HOH 424 4425 478  HOH HOH A . 
Q 6 HOH 425 4426 479  HOH HOH A . 
Q 6 HOH 426 4427 480  HOH HOH A . 
Q 6 HOH 427 4428 481  HOH HOH A . 
Q 6 HOH 428 4429 482  HOH HOH A . 
Q 6 HOH 429 4430 483  HOH HOH A . 
Q 6 HOH 430 4431 484  HOH HOH A . 
Q 6 HOH 431 4432 485  HOH HOH A . 
Q 6 HOH 432 4433 486  HOH HOH A . 
Q 6 HOH 433 4434 487  HOH HOH A . 
Q 6 HOH 434 4435 488  HOH HOH A . 
Q 6 HOH 435 4436 489  HOH HOH A . 
Q 6 HOH 436 4437 490  HOH HOH A . 
Q 6 HOH 437 4438 491  HOH HOH A . 
Q 6 HOH 438 4439 492  HOH HOH A . 
Q 6 HOH 439 4440 493  HOH HOH A . 
Q 6 HOH 440 4441 494  HOH HOH A . 
Q 6 HOH 441 4442 495  HOH HOH A . 
Q 6 HOH 442 4443 496  HOH HOH A . 
Q 6 HOH 443 4444 497  HOH HOH A . 
Q 6 HOH 444 4445 498  HOH HOH A . 
Q 6 HOH 445 4446 499  HOH HOH A . 
Q 6 HOH 446 4447 500  HOH HOH A . 
Q 6 HOH 447 4448 501  HOH HOH A . 
Q 6 HOH 448 4449 502  HOH HOH A . 
Q 6 HOH 449 4450 503  HOH HOH A . 
Q 6 HOH 450 4451 504  HOH HOH A . 
Q 6 HOH 451 4452 505  HOH HOH A . 
Q 6 HOH 452 4453 506  HOH HOH A . 
Q 6 HOH 453 4454 507  HOH HOH A . 
Q 6 HOH 454 4455 508  HOH HOH A . 
Q 6 HOH 455 4456 509  HOH HOH A . 
Q 6 HOH 456 4457 510  HOH HOH A . 
Q 6 HOH 457 4458 513  HOH HOH A . 
Q 6 HOH 458 4459 515  HOH HOH A . 
Q 6 HOH 459 4460 516  HOH HOH A . 
Q 6 HOH 460 4461 517  HOH HOH A . 
Q 6 HOH 461 4462 518  HOH HOH A . 
Q 6 HOH 462 4463 519  HOH HOH A . 
Q 6 HOH 463 4464 521  HOH HOH A . 
Q 6 HOH 464 4465 522  HOH HOH A . 
Q 6 HOH 465 4466 525  HOH HOH A . 
Q 6 HOH 466 4467 526  HOH HOH A . 
Q 6 HOH 467 4468 527  HOH HOH A . 
Q 6 HOH 468 4469 528  HOH HOH A . 
Q 6 HOH 469 4470 529  HOH HOH A . 
Q 6 HOH 470 4471 530  HOH HOH A . 
Q 6 HOH 471 4472 531  HOH HOH A . 
Q 6 HOH 472 4473 532  HOH HOH A . 
Q 6 HOH 473 4474 533  HOH HOH A . 
Q 6 HOH 474 4475 534  HOH HOH A . 
Q 6 HOH 475 4476 535  HOH HOH A . 
Q 6 HOH 476 4477 536  HOH HOH A . 
Q 6 HOH 477 4478 537  HOH HOH A . 
Q 6 HOH 478 4479 538  HOH HOH A . 
Q 6 HOH 479 4480 539  HOH HOH A . 
Q 6 HOH 480 4481 540  HOH HOH A . 
Q 6 HOH 481 4482 541  HOH HOH A . 
Q 6 HOH 482 4483 542  HOH HOH A . 
Q 6 HOH 483 4484 543  HOH HOH A . 
Q 6 HOH 484 4485 544  HOH HOH A . 
Q 6 HOH 485 4486 545  HOH HOH A . 
Q 6 HOH 486 4487 546  HOH HOH A . 
Q 6 HOH 487 4488 547  HOH HOH A . 
Q 6 HOH 488 4489 548  HOH HOH A . 
Q 6 HOH 489 4490 552  HOH HOH A . 
Q 6 HOH 490 4491 553  HOH HOH A . 
Q 6 HOH 491 4492 554  HOH HOH A . 
Q 6 HOH 492 4493 556  HOH HOH A . 
Q 6 HOH 493 4494 557  HOH HOH A . 
Q 6 HOH 494 4495 558  HOH HOH A . 
Q 6 HOH 495 4496 559  HOH HOH A . 
Q 6 HOH 496 4497 560  HOH HOH A . 
Q 6 HOH 497 4498 561  HOH HOH A . 
Q 6 HOH 498 4499 562  HOH HOH A . 
Q 6 HOH 499 4500 563  HOH HOH A . 
Q 6 HOH 500 4501 564  HOH HOH A . 
Q 6 HOH 501 4502 565  HOH HOH A . 
Q 6 HOH 502 4503 566  HOH HOH A . 
Q 6 HOH 503 4504 567  HOH HOH A . 
Q 6 HOH 504 4505 568  HOH HOH A . 
Q 6 HOH 505 4506 569  HOH HOH A . 
Q 6 HOH 506 4507 570  HOH HOH A . 
Q 6 HOH 507 4508 571  HOH HOH A . 
Q 6 HOH 508 4509 572  HOH HOH A . 
Q 6 HOH 509 4510 573  HOH HOH A . 
Q 6 HOH 510 4511 574  HOH HOH A . 
Q 6 HOH 511 4512 575  HOH HOH A . 
Q 6 HOH 512 4513 576  HOH HOH A . 
Q 6 HOH 513 4514 577  HOH HOH A . 
Q 6 HOH 514 4515 579  HOH HOH A . 
Q 6 HOH 515 4516 580  HOH HOH A . 
Q 6 HOH 516 4517 582  HOH HOH A . 
Q 6 HOH 517 4518 583  HOH HOH A . 
Q 6 HOH 518 4519 585  HOH HOH A . 
Q 6 HOH 519 4520 586  HOH HOH A . 
Q 6 HOH 520 4521 587  HOH HOH A . 
Q 6 HOH 521 4522 588  HOH HOH A . 
Q 6 HOH 522 4523 589  HOH HOH A . 
Q 6 HOH 523 4524 592  HOH HOH A . 
Q 6 HOH 524 4525 593  HOH HOH A . 
Q 6 HOH 525 4526 594  HOH HOH A . 
Q 6 HOH 526 4527 595  HOH HOH A . 
Q 6 HOH 527 4528 596  HOH HOH A . 
Q 6 HOH 528 4529 597  HOH HOH A . 
Q 6 HOH 529 4530 599  HOH HOH A . 
Q 6 HOH 530 4531 601  HOH HOH A . 
Q 6 HOH 531 4532 602  HOH HOH A . 
Q 6 HOH 532 4533 603  HOH HOH A . 
Q 6 HOH 533 4534 604  HOH HOH A . 
Q 6 HOH 534 4535 605  HOH HOH A . 
Q 6 HOH 535 4536 606  HOH HOH A . 
Q 6 HOH 536 4537 607  HOH HOH A . 
Q 6 HOH 537 4538 608  HOH HOH A . 
Q 6 HOH 538 4539 611  HOH HOH A . 
Q 6 HOH 539 4540 612  HOH HOH A . 
Q 6 HOH 540 4541 613  HOH HOH A . 
Q 6 HOH 541 4542 614  HOH HOH A . 
Q 6 HOH 542 4543 615  HOH HOH A . 
Q 6 HOH 543 4544 616  HOH HOH A . 
Q 6 HOH 544 4545 617  HOH HOH A . 
Q 6 HOH 545 4546 618  HOH HOH A . 
Q 6 HOH 546 4547 623  HOH HOH A . 
Q 6 HOH 547 4548 624  HOH HOH A . 
Q 6 HOH 548 4549 625  HOH HOH A . 
Q 6 HOH 549 4550 626  HOH HOH A . 
Q 6 HOH 550 4551 627  HOH HOH A . 
Q 6 HOH 551 4552 628  HOH HOH A . 
Q 6 HOH 552 4553 629  HOH HOH A . 
Q 6 HOH 553 4554 630  HOH HOH A . 
Q 6 HOH 554 4555 631  HOH HOH A . 
Q 6 HOH 555 4556 632  HOH HOH A . 
Q 6 HOH 556 4557 633  HOH HOH A . 
Q 6 HOH 557 4558 634  HOH HOH A . 
Q 6 HOH 558 4559 635  HOH HOH A . 
Q 6 HOH 559 4560 636  HOH HOH A . 
Q 6 HOH 560 4561 637  HOH HOH A . 
Q 6 HOH 561 4562 638  HOH HOH A . 
Q 6 HOH 562 4563 639  HOH HOH A . 
Q 6 HOH 563 4564 640  HOH HOH A . 
Q 6 HOH 564 4565 641  HOH HOH A . 
Q 6 HOH 565 4566 642  HOH HOH A . 
Q 6 HOH 566 4567 643  HOH HOH A . 
Q 6 HOH 567 4568 646  HOH HOH A . 
Q 6 HOH 568 4569 653  HOH HOH A . 
Q 6 HOH 569 4570 656  HOH HOH A . 
Q 6 HOH 570 4571 657  HOH HOH A . 
Q 6 HOH 571 4572 658  HOH HOH A . 
Q 6 HOH 572 4573 659  HOH HOH A . 
Q 6 HOH 573 4574 660  HOH HOH A . 
Q 6 HOH 574 4575 661  HOH HOH A . 
Q 6 HOH 575 4576 662  HOH HOH A . 
Q 6 HOH 576 4577 663  HOH HOH A . 
Q 6 HOH 577 4578 665  HOH HOH A . 
Q 6 HOH 578 4579 666  HOH HOH A . 
Q 6 HOH 579 4580 667  HOH HOH A . 
Q 6 HOH 580 4581 668  HOH HOH A . 
Q 6 HOH 581 4582 669  HOH HOH A . 
Q 6 HOH 582 4583 670  HOH HOH A . 
Q 6 HOH 583 4584 671  HOH HOH A . 
Q 6 HOH 584 4585 672  HOH HOH A . 
Q 6 HOH 585 4586 673  HOH HOH A . 
Q 6 HOH 586 4587 674  HOH HOH A . 
Q 6 HOH 587 4588 677  HOH HOH A . 
Q 6 HOH 588 4589 678  HOH HOH A . 
Q 6 HOH 589 4590 679  HOH HOH A . 
Q 6 HOH 590 4591 681  HOH HOH A . 
Q 6 HOH 591 4592 684  HOH HOH A . 
Q 6 HOH 592 4593 687  HOH HOH A . 
Q 6 HOH 593 4594 689  HOH HOH A . 
Q 6 HOH 594 4595 692  HOH HOH A . 
Q 6 HOH 595 4596 693  HOH HOH A . 
Q 6 HOH 596 4597 694  HOH HOH A . 
Q 6 HOH 597 4598 696  HOH HOH A . 
Q 6 HOH 598 4599 697  HOH HOH A . 
Q 6 HOH 599 4600 698  HOH HOH A . 
Q 6 HOH 600 4601 700  HOH HOH A . 
Q 6 HOH 601 4602 701  HOH HOH A . 
Q 6 HOH 602 4603 702  HOH HOH A . 
Q 6 HOH 603 4604 703  HOH HOH A . 
Q 6 HOH 604 4605 705  HOH HOH A . 
Q 6 HOH 605 4606 706  HOH HOH A . 
Q 6 HOH 606 4607 707  HOH HOH A . 
Q 6 HOH 607 4608 709  HOH HOH A . 
Q 6 HOH 608 4609 710  HOH HOH A . 
Q 6 HOH 609 4610 713  HOH HOH A . 
Q 6 HOH 610 4611 714  HOH HOH A . 
Q 6 HOH 611 4612 715  HOH HOH A . 
Q 6 HOH 612 4613 717  HOH HOH A . 
Q 6 HOH 613 4614 718  HOH HOH A . 
Q 6 HOH 614 4615 721  HOH HOH A . 
Q 6 HOH 615 4616 723  HOH HOH A . 
Q 6 HOH 616 4617 724  HOH HOH A . 
Q 6 HOH 617 4618 725  HOH HOH A . 
Q 6 HOH 618 4619 726  HOH HOH A . 
Q 6 HOH 619 4620 727  HOH HOH A . 
Q 6 HOH 620 4621 728  HOH HOH A . 
Q 6 HOH 621 4622 355  HOH HOH A . 
Q 6 HOH 622 4623 418  HOH HOH A . 
Q 6 HOH 623 4624 471  HOH HOH A . 
Q 6 HOH 624 4625 591  HOH HOH A . 
Q 6 HOH 625 4626 729  HOH HOH A . 
Q 6 HOH 626 4627 730  HOH HOH A . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 209 A ASN 209 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 393 A ASN 393 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 741 A ASN 741 ? ASN 'GLYCOSYLATION SITE' 
# 
_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,G,H,I,J,K,L,M,N,O,P,Q 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2008-01-08 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement        5.2.0019 ? 1 
HKL-2000 'data collection' .        ? 2 
HKL-2000 'data reduction'  .        ? 3 
HKL-2000 'data scaling'    .        ? 4 
PHASER   phasing           .        ? 5 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              624 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              624 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              624 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.00 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.30 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 8   ? ? -36.09  128.07  
2  1 ASN A 34  ? ? -155.98 87.54   
3  1 SER A 40  ? ? 75.14   -11.82  
4  1 HIS A 50  ? ? -143.87 -38.34  
5  1 SER A 51  ? ? -103.03 -107.77 
6  1 SER A 80  ? ? -47.56  86.16   
7  1 PHE A 161 ? ? -150.53 82.42   
8  1 LEU A 180 ? ? 70.62   146.30  
9  1 GLN A 186 ? ? 70.61   -30.85  
10 1 TRP A 194 ? ? 53.77   75.28   
11 1 PHE A 200 ? ? -170.49 116.33  
12 1 ASN A 207 ? ? -124.06 -162.23 
13 1 LEU A 213 ? ? -124.18 -149.53 
14 1 GLU A 300 ? ? 68.29   65.28   
15 1 TYR A 321 ? ? -169.10 97.14   
16 1 VAL A 342 ? ? -96.23  -63.01  
17 1 VAL A 405 ? ? -134.40 -148.97 
18 1 ASP A 474 ? ? 82.41   -15.98  
19 1 SER A 521 ? ? 56.96   -144.31 
20 1 ILE A 565 ? ? -117.58 72.58   
21 1 CYS A 573 ? ? 85.17   -21.20  
22 1 PHE A 575 ? ? -63.88  -71.93  
23 1 LEU A 577 ? ? 86.93   152.27  
24 1 VAL A 651 ? ? -107.16 -70.32  
25 1 GLU A 774 ? ? -153.03 -21.94  
26 1 GLN A 793 ? ? 3.29    119.99  
27 1 SER A 803 ? ? -143.27 48.63   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    300 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    301 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.74 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1   ? A SER 1   
2 1 Y 1 A ALA 2   ? A ALA 2   
3 1 Y 1 A GLU 3   ? A GLU 3   
4 1 Y 1 A CYS 4   ? A CYS 4   
5 1 Y 1 A PRO 5   ? A PRO 5   
6 1 Y 1 A VAL 6   ? A VAL 6   
7 1 Y 1 A GLN 837 ? A GLN 837 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 ALPHA-ACARBOSE         ACR 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 'SULFATE ION'          SO4 
5 GLYCEROL               GOL 
6 water                  HOH 
# 
