data_2QLY
# 
_entry.id   2QLY 
# 
_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   2QLY         
RCSB  RCSB043764   
WWPDB D_1000043764 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          2QMJ 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2QLY 
_pdbx_database_status.recvd_initial_deposition_date   2007-07-13 
_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           2QLY 
_cell.length_a           93.167 
_cell.length_b           107.645 
_cell.length_c           111.966 
_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                         2QLY 
_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 N-ACETYL-D-GLUCOSAMINE             221.208   5   ?       ? ?                                   ? 
3 non-polymer syn GLYCEROL                           92.094    11  ?       ? ?                                   ? 
4 water       nat water                              18.015    565 ?       ? ?                                   ? 
# 
_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              2QLY 
_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 2QLY ALA A 869 ? UNP O43451 ? ? 'EXPRESSION TAG' 869 1 
1 2QLY 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 
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 
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          2QLY 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.85 
_exptl_crystal.density_percent_sol   56.80 
_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   2006-06-01 
_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                     2QLY 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   77808 
_reflns.number_all                   77964 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.083 
_reflns.pdbx_netI_over_sigmaI        17.4 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              6.3 
_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             2.00 
_reflns_shell.d_res_low              2.07 
_reflns_shell.percent_possible_all   100 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.52 
_reflns_shell.meanI_over_sigI_obs    3.0 
_reflns_shell.pdbx_redundancy        6.1 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2QLY 
_refine.ls_number_reflns_obs                     72397 
_refine.ls_number_reflns_all                     ? 
_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                             19.88 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_R_factor_obs                          0.18075 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17845 
_refine.ls_R_factor_R_free                       0.22382 
_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                  3842 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.B_iso_mean                               31.089 
_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                      ? 
_refine.pdbx_method_to_determine_struct          SAD 
_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                       0.155 
_refine.pdbx_overall_ESU_R_Free                  0.148 
_refine.overall_SU_ML                            0.102 
_refine.overall_SU_B                             3.643 
_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         136 
_refine_hist.number_atoms_solvent             565 
_refine_hist.number_atoms_total               7613 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        19.88 
# 
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             0.017  0.022  ? 7296 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.710  1.951  ? 9948 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.011  5.000  ? 875  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       37.078 24.266 ? 368  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.595 15.000 ? 1104 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       17.315 15.000 ? 40   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 1064 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 5681 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.211  0.200  ? 3434 'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              0.318  0.200  ? 4974 'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.163  0.200  ? 650  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.279  0.200  ? 58   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.257  0.200  ? 9    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.196  1.500  ? 4430 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.913  2.000  ? 7023 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.946  3.000  ? 3304 'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.541  4.500  ? 2919 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.051 
_refine_ls_shell.number_reflns_R_work             5210 
_refine_ls_shell.R_factor_R_work                  0.237 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.R_factor_R_free                  0.302 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             274 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2QLY 
_struct.title                     'Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase' 
_struct.pdbx_descriptor           'Maltase-glucoamylase, intestinal' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2QLY 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'beta-alpha-barrel, Glycoprotein, Glycosidase, Hydrolase, 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 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
O N N 3 ? 
P N N 3 ? 
Q N N 3 ? 
R N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   'The biological assembly is a monomer' 
# 
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 ? VAL A 435 ? ASN A 417 VAL A 435 1 ? 19 
HELX_P HELX_P11 11 GLN A 493 ? HIS A 497 ? GLN A 493 HIS A 497 1 ? 5  
HELX_P HELX_P12 12 LEU A 499 ? PHE A 516 ? LEU A 499 PHE A 516 1 ? 18 
HELX_P HELX_P13 13 GLY A 531 ? PHE A 535 ? GLY A 531 PHE A 535 5 ? 5  
HELX_P HELX_P14 14 THR A 546 ? PHE A 563 ? THR A 546 PHE A 563 1 ? 18 
HELX_P HELX_P15 15 PRO A 580 ? ALA A 592 ? PRO A 580 ALA A 592 1 ? 13 
HELX_P HELX_P16 16 ASP A 609 ? GLY A 614 ? ASP A 609 GLY A 614 5 ? 6  
HELX_P HELX_P17 17 SER A 617 ? LEU A 633 ? SER A 617 LEU A 633 1 ? 17 
HELX_P HELX_P18 18 LEU A 633 ? ARG A 647 ? LEU A 633 ARG A 647 1 ? 15 
HELX_P HELX_P19 19 PRO A 654 ? TYR A 660 ? PRO A 654 TYR A 660 1 ? 7  
HELX_P HELX_P20 20 ASP A 662 ? TRP A 666 ? ASP A 662 TRP A 666 5 ? 5  
HELX_P HELX_P21 21 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 ? ? ? ? ? ? ? 2.059 ? 
disulf2 disulf ? ? A CYS 573 SG  ? ? ? 1_555 A CYS 584 SG ? ? A CYS 573  A CYS 584  1_555 ? ? ? ? ? ? ? 2.062 ? 
covale1 covale ? ? A ASN 209 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 209  A NAG 2005 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale2 covale ? ? A ASN 393 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 393  A NAG 2003 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale3 covale ? ? A ASN 741 ND2 ? ? ? 1_555 B NAG .   C1 ? ? A ASN 741  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale4 covale ? ? B NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? A NAG 2001 A NAG 2002 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale5 covale ? ? D NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? A NAG 2003 A NAG 2004 1_555 ? ? ? ? ? ? ? 1.435 ? 
# 
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 -4.26 
2 GLY 181 A . ? GLY 181 A GLU 182 A ? GLU 182 A 1 1.44  
3 ALA 248 A . ? ALA 248 A PRO 249 A ? PRO 249 A 1 2.81  
4 GLU 446 A . ? GLU 446 A VAL 447 A ? VAL 447 A 1 5.84  
5 PRO 835 A . ? PRO 835 A SER 836 A ? SER 836 A 1 0.62  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 3  ? 
C ? 8  ? 
D ? 3  ? 
E ? 5  ? 
F ? 9  ? 
G ? 3  ? 
H ? 2  ? 
I ? 5  ? 
J ? 2  ? 
K ? 11 ? 
L ? 10 ? 
# 
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 
C 1  2  ? anti-parallel 
C 2  3  ? anti-parallel 
C 3  4  ? anti-parallel 
C 4  5  ? anti-parallel 
C 5  6  ? anti-parallel 
C 6  7  ? anti-parallel 
C 7  8  ? anti-parallel 
D 1  2  ? anti-parallel 
D 2  3  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
F 1  2  ? parallel      
F 2  3  ? parallel      
F 3  4  ? parallel      
F 4  5  ? parallel      
F 5  6  ? parallel      
F 6  7  ? parallel      
F 7  8  ? parallel      
F 8  9  ? parallel      
G 1  2  ? anti-parallel 
G 2  3  ? anti-parallel 
H 1  2  ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
J 1  2  ? 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  ? anti-parallel 
K 6  7  ? parallel      
K 7  8  ? anti-parallel 
K 8  9  ? parallel      
K 9  10 ? anti-parallel 
K 10 11 ? anti-parallel 
L 1  2  ? anti-parallel 
L 2  3  ? anti-parallel 
L 3  4  ? anti-parallel 
L 4  5  ? anti-parallel 
L 5  6  ? anti-parallel 
L 6  7  ? parallel      
L 7  8  ? anti-parallel 
L 8  9  ? parallel      
L 9  10 ? 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  ? VAL A 54  ? TYR A 52  VAL A 54  
B 2  GLY A 64  ? ASN A 71  ? GLY A 64  ASN A 71  
B 3  VAL A 59  ? ASN A 60  ? VAL A 59  ASN A 60  
C 1  TYR A 52  ? VAL A 54  ? TYR A 52  VAL A 54  
C 2  GLY A 64  ? ASN A 71  ? GLY A 64  ASN A 71  
C 3  ASN A 84  ? THR A 93  ? ASN A 84  THR A 93  
C 4  ARG A 96  ? ASP A 103 ? ARG A 96  ASP A 103 
C 5  LEU A 260 ? GLY A 267 ? LEU A 260 GLY A 267 
C 6  SER A 230 ? LEU A 235 ? SER A 230 LEU A 235 
C 7  GLN A 217 ? LEU A 223 ? GLN A 217 LEU A 223 
C 8  VAL A 177 ? GLY A 181 ? VAL A 177 GLY A 181 
D 1  TYR A 129 ? SER A 134 ? TYR A 129 SER A 134 
D 2  SER A 139 ? ARG A 144 ? SER A 139 ARG A 144 
D 3  VAL A 150 ? ASP A 153 ? VAL A 150 ASP A 153 
E 1  LEU A 160 ? ALA A 162 ? LEU A 160 ALA A 162 
E 2  PHE A 165 ? ARG A 171 ? PHE A 165 ARG A 171 
E 3  ALA A 250 ? THR A 255 ? ALA A 250 THR A 255 
E 4  MET A 241 ? GLN A 246 ? MET A 241 GLN A 246 
E 5  LYS A 195 ? ILE A 199 ? LYS A 195 ILE A 199 
F 1  VAL A 568 ? GLY A 569 ? VAL A 568 GLY A 569 
F 2  ALA A 537 ? TRP A 539 ? ALA A 537 TRP A 539 
F 3  ILE A 523 ? THR A 525 ? ILE A 523 THR A 525 
F 4  GLY A 439 ? ILE A 442 ? GLY A 439 ILE A 442 
F 5  LYS A 360 ? VAL A 365 ? LYS A 360 VAL A 365 
F 6  VAL A 323 ? ALA A 326 ? VAL A 323 ALA A 326 
F 7  PHE A 294 ? LEU A 296 ? PHE A 294 LEU A 296 
F 8  SER A 597 ? ASN A 599 ? SER A 597 ASN A 599 
F 9  ASP A 571 ? ILE A 572 ? ASP A 571 ILE A 572 
G 1  ILE A 369 ? SER A 370 ? ILE A 369 SER A 370 
G 2  GLY A 408 ? VAL A 411 ? GLY A 408 VAL A 411 
G 3  GLY A 403 ? VAL A 405 ? GLY A 403 VAL A 405 
H 1  VAL A 487 ? GLN A 488 ? VAL A 487 GLN A 488 
H 2  GLY A 491 ? LYS A 492 ? GLY A 491 LYS A 492 
I 1  ALA A 652 ? ARG A 653 ? ALA A 652 ARG A 653 
I 2  PHE A 672 ? TRP A 674 ? PHE A 672 TRP A 674 
I 3  LEU A 678 ? THR A 681 ? LEU A 678 THR A 681 
I 4  GLY A 726 ? ARG A 730 ? GLY A 726 ARG A 730 
I 5  TRP A 700 ? ASP A 702 ? TRP A 700 ASP A 702 
J 1  LYS A 690 ? VAL A 695 ? LYS A 690 VAL A 695 
J 2  GLN A 714 ? GLU A 719 ? GLN A 714 GLU A 719 
K 1  VAL A 834 ? PRO A 835 ? VAL A 834 PRO A 835 
K 2  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
K 3  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
K 4  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
K 5  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
K 6  GLU A 763 ? TRP A 770 ? GLU A 763 TRP A 770 
K 7  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
K 8  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
K 9  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
K 10 VAL A 850 ? THR A 854 ? VAL A 850 THR A 854 
K 11 THR A 841 ? ASP A 845 ? THR A 841 ASP A 845 
L 1  VAL A 834 ? PRO A 835 ? VAL A 834 PRO A 835 
L 2  SER A 825 ? HIS A 831 ? SER A 825 HIS A 831 
L 3  TYR A 864 ? ALA A 869 ? TYR A 864 ALA A 869 
L 4  ARG A 795 ? SER A 803 ? ARG A 795 SER A 803 
L 5  LEU A 785 ? THR A 792 ? LEU A 785 THR A 792 
L 6  GLU A 763 ? TRP A 770 ? GLU A 763 TRP A 770 
L 7  TYR A 733 ? GLN A 738 ? TYR A 733 GLN A 738 
L 8  LEU A 752 ? ALA A 757 ? LEU A 752 ALA A 757 
L 9  ALA A 812 ? LEU A 819 ? ALA A 812 LEU A 819 
L 10 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  O THR A 66  ? O THR A 66  N VAL A 59  ? N VAL A 59  
C 1  2  N HIS A 53  ? N HIS A 53  O LYS A 70  ? O LYS A 70  
C 2  3  N LEU A 69  ? N LEU A 69  O VAL A 85  ? O VAL A 85  
C 3  4  N GLU A 90  ? N GLU A 90  O HIS A 98  ? O HIS A 98  
C 4  5  N PHE A 99  ? N PHE A 99  O PHE A 262 ? O PHE A 262 
C 5  6  O GLY A 267 ? O GLY A 267 N SER A 230 ? N SER A 230 
C 6  7  O PHE A 231 ? O PHE A 231 N CYS A 222 ? N CYS A 222 
C 7  8  O GLN A 217 ? O GLN A 217 N GLY A 181 ? N GLY A 181 
D 1  2  N GLN A 130 ? N GLN A 130 O THR A 143 ? O THR A 143 
D 2  3  N VAL A 142 ? N VAL A 142 O LEU A 151 ? O LEU A 151 
E 1  2  N ALA A 162 ? N ALA A 162 O PHE A 165 ? O PHE A 165 
E 2  3  N LEU A 166 ? N LEU A 166 O THR A 255 ? O THR A 255 
E 3  4  O THR A 252 ? O THR A 252 N VAL A 244 ? N VAL A 244 
E 4  5  O LEU A 245 ? O LEU A 245 N LYS A 195 ? N LYS A 195 
F 1  2  O GLY A 569 ? O GLY A 569 N HIS A 538 ? N HIS A 538 
F 2  3  O ALA A 537 ? O ALA A 537 N ILE A 523 ? N ILE A 523 
F 3  4  O LEU A 524 ? O LEU A 524 N ILE A 442 ? N ILE A 442 
F 4  5  O TRP A 441 ? O TRP A 441 N ILE A 363 ? N ILE A 363 
F 5  6  O VAL A 362 ? O VAL A 362 N GLN A 324 ? N GLN A 324 
F 6  7  O VAL A 323 ? O VAL A 323 N LEU A 296 ? N LEU A 296 
F 7  8  N HIS A 295 ? N HIS A 295 O SER A 597 ? O SER A 597 
F 8  9  O ARG A 598 ? O ARG A 598 N ILE A 572 ? N ILE A 572 
G 1  2  N ILE A 369 ? N ILE A 369 O VAL A 411 ? O VAL A 411 
G 2  3  O THR A 410 ? O THR A 410 N GLY A 403 ? N GLY A 403 
H 1  2  N GLN A 488 ? N GLN A 488 O GLY A 491 ? O GLY A 491 
I 1  2  N ARG A 653 ? N ARG A 653 O LEU A 673 ? O LEU A 673 
I 2  3  N PHE A 672 ? N PHE A 672 O ILE A 680 ? O ILE A 680 
I 3  4  N LEU A 679 ? N LEU A 679 O HIS A 728 ? O HIS A 728 
I 4  5  O LEU A 729 ? O LEU A 729 N TYR A 701 ? N TYR A 701 
J 1  2  N VAL A 691 ? N VAL A 691 O MET A 718 ? O MET A 718 
K 1  2  O VAL A 834 ? O VAL A 834 N HIS A 831 ? N HIS A 831 
K 2  3  N SER A 825 ? N SER A 825 O ALA A 869 ? O ALA A 869 
K 3  4  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
K 4  5  O GLU A 797 ? O GLU A 797 N SER A 790 ? N SER A 790 
K 5  6  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
K 6  7  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
K 7  8  N TYR A 733 ? N TYR A 733 O ALA A 757 ? O ALA A 757 
K 8  9  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
K 9  10 N ILE A 818 ? N ILE A 818 O ALA A 851 ? O ALA A 851 
K 10 11 O THR A 854 ? O THR A 854 N THR A 841 ? N THR A 841 
L 1  2  O VAL A 834 ? O VAL A 834 N HIS A 831 ? N HIS A 831 
L 2  3  N SER A 825 ? N SER A 825 O ALA A 869 ? O ALA A 869 
L 3  4  O VAL A 866 ? O VAL A 866 N LEU A 796 ? N LEU A 796 
L 4  5  O GLU A 797 ? O GLU A 797 N SER A 790 ? N SER A 790 
L 5  6  O LEU A 785 ? O LEU A 785 N TRP A 770 ? N TRP A 770 
L 6  7  O LYS A 765 ? O LYS A 765 N ILE A 734 ? N ILE A 734 
L 7  8  N TYR A 733 ? N TYR A 733 O ALA A 757 ? O ALA A 757 
L 8  9  N ILE A 756 ? N ILE A 756 O LYS A 817 ? O LYS A 817 
L 9  10 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE NAG A 2001' 
AC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 2002' 
AC3 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG A 2003' 
AC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 2004' 
AC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 2005' 
AC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE GOL A 3001' 
AC7 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE GOL A 3002' 
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE GOL A 3003' 
AC9 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE GOL A 3004' 
BC1 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE GOL A 3005' 
BC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE GOL A 3006' 
BC3 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE GOL A 3007' 
BC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE GOL A 3008' 
BC5 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE GOL A 3009' 
BC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE GOL A 3010' 
BC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE GOL A 3011' 
# 
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 10 ARG A 145 ? ARG A 145  . ? 2_675 ? 
2  AC1 10 SER A 146 ? SER A 146  . ? 2_675 ? 
3  AC1 10 ASN A 147 ? ASN A 147  . ? 2_675 ? 
4  AC1 10 ASN A 148 ? ASN A 148  . ? 2_675 ? 
5  AC1 10 ASN A 741 ? ASN A 741  . ? 1_555 ? 
6  AC1 10 ASN A 750 ? ASN A 750  . ? 1_555 ? 
7  AC1 10 NAG C .   ? NAG A 2002 . ? 1_555 ? 
8  AC1 10 HOH R .   ? HOH A 3105 . ? 2_675 ? 
9  AC1 10 HOH R .   ? HOH A 3273 . ? 1_555 ? 
10 AC1 10 HOH R .   ? HOH A 3477 . ? 1_555 ? 
11 AC2 3  ASN A 147 ? ASN A 147  . ? 2_675 ? 
12 AC2 3  NAG B .   ? NAG A 2001 . ? 1_555 ? 
13 AC2 3  HOH R .   ? HOH A 3477 . ? 1_555 ? 
14 AC3 9  LYS A 389 ? LYS A 389  . ? 1_555 ? 
15 AC3 9  ASN A 393 ? ASN A 393  . ? 1_555 ? 
16 AC3 9  GLY A 397 ? GLY A 397  . ? 1_555 ? 
17 AC3 9  VAL A 398 ? VAL A 398  . ? 1_555 ? 
18 AC3 9  GLN A 488 ? GLN A 488  . ? 1_555 ? 
19 AC3 9  HIS A 489 ? HIS A 489  . ? 1_555 ? 
20 AC3 9  NAG E .   ? NAG A 2004 . ? 1_555 ? 
21 AC3 9  HOH R .   ? HOH A 3042 . ? 1_555 ? 
22 AC3 9  HOH R .   ? HOH A 3044 . ? 1_555 ? 
23 AC4 4  LYS A 389 ? LYS A 389  . ? 1_555 ? 
24 AC4 4  NAG D .   ? NAG A 2003 . ? 1_555 ? 
25 AC4 4  HOH R .   ? HOH A 3047 . ? 1_555 ? 
26 AC4 4  HOH R .   ? HOH A 3048 . ? 1_555 ? 
27 AC5 3  ASN A 207 ? ASN A 207  . ? 1_555 ? 
28 AC5 3  GLY A 208 ? GLY A 208  . ? 1_555 ? 
29 AC5 3  ASN A 209 ? ASN A 209  . ? 1_555 ? 
30 AC6 6  GLN A 92  ? GLN A 92   . ? 1_555 ? 
31 AC6 6  ARG A 96  ? ARG A 96   . ? 1_555 ? 
32 AC6 6  GLN A 117 ? GLN A 117  . ? 1_555 ? 
33 AC6 6  PHE A 119 ? PHE A 119  . ? 1_555 ? 
34 AC6 6  HOH R .   ? HOH A 3081 . ? 1_555 ? 
35 AC6 6  HOH R .   ? HOH A 3082 . ? 1_555 ? 
36 AC7 8  ALA A 285 ? ALA A 285  . ? 1_555 ? 
37 AC7 8  PRO A 287 ? PRO A 287  . ? 1_555 ? 
38 AC7 8  PHE A 522 ? PHE A 522  . ? 1_555 ? 
39 AC7 8  ILE A 523 ? ILE A 523  . ? 1_555 ? 
40 AC7 8  PHE A 535 ? PHE A 535  . ? 1_555 ? 
41 AC7 8  ALA A 536 ? ALA A 536  . ? 1_555 ? 
42 AC7 8  ALA A 537 ? ALA A 537  . ? 1_555 ? 
43 AC7 8  HOH R .   ? HOH A 3203 . ? 1_555 ? 
44 AC8 5  ASN A 306 ? ASN A 306  . ? 1_555 ? 
45 AC8 5  GLU A 309 ? GLU A 309  . ? 1_555 ? 
46 AC8 5  ARG A 313 ? ARG A 313  . ? 1_555 ? 
47 AC8 5  ASP A 607 ? ASP A 607  . ? 1_555 ? 
48 AC8 5  HOH R .   ? HOH A 3442 . ? 1_555 ? 
49 AC9 1  LEU A 618 ? LEU A 618  . ? 1_555 ? 
50 BC1 3  ARG A 145 ? ARG A 145  . ? 2_675 ? 
51 BC1 3  PRO A 740 ? PRO A 740  . ? 1_555 ? 
52 BC1 3  HOH R .   ? HOH A 3265 . ? 1_555 ? 
53 BC2 6  LEU A 58  ? LEU A 58   . ? 1_555 ? 
54 BC2 6  VAL A 131 ? VAL A 131  . ? 1_555 ? 
55 BC2 6  GLU A 132 ? GLU A 132  . ? 1_555 ? 
56 BC2 6  ILE A 133 ? ILE A 133  . ? 1_555 ? 
57 BC2 6  THR A 843 ? THR A 843  . ? 2_674 ? 
58 BC2 6  THR A 854 ? THR A 854  . ? 2_674 ? 
59 BC3 3  SER A 126 ? SER A 126  . ? 2_675 ? 
60 BC3 3  HIS A 625 ? HIS A 625  . ? 1_555 ? 
61 BC3 3  ASN A 628 ? ASN A 628  . ? 1_555 ? 
62 BC4 6  TYR A 626 ? TYR A 626  . ? 1_555 ? 
63 BC4 6  ASP A 702 ? ASP A 702  . ? 1_555 ? 
64 BC4 6  GLU A 704 ? GLU A 704  . ? 1_555 ? 
65 BC4 6  ILE A 725 ? ILE A 725  . ? 1_555 ? 
66 BC4 6  GLY A 726 ? GLY A 726  . ? 1_555 ? 
67 BC4 6  LEU A 727 ? LEU A 727  . ? 1_555 ? 
68 BC5 9  ASP A 327 ? ASP A 327  . ? 1_555 ? 
69 BC5 9  ILE A 328 ? ILE A 328  . ? 1_555 ? 
70 BC5 9  ILE A 364 ? ILE A 364  . ? 1_555 ? 
71 BC5 9  TRP A 441 ? TRP A 441  . ? 1_555 ? 
72 BC5 9  ASP A 443 ? ASP A 443  . ? 1_555 ? 
73 BC5 9  PHE A 575 ? PHE A 575  . ? 1_555 ? 
74 BC5 9  HIS A 600 ? HIS A 600  . ? 1_555 ? 
75 BC5 9  HOH R .   ? HOH A 3434 . ? 1_555 ? 
76 BC5 9  HOH R .   ? HOH A 3533 . ? 1_555 ? 
77 BC6 3  ASP A 203 ? ASP A 203  . ? 1_555 ? 
78 BC6 3  TRP A 406 ? TRP A 406  . ? 1_555 ? 
79 BC6 3  HOH R .   ? HOH A 3535 . ? 1_555 ? 
80 BC7 4  THR A 416 ? THR A 416  . ? 1_555 ? 
81 BC7 4  TRP A 490 ? TRP A 490  . ? 1_555 ? 
82 BC7 4  HOH R .   ? HOH A 3394 . ? 1_555 ? 
83 BC7 4  HOH R .   ? HOH A 3543 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2QLY 
_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                    2QLY 
_atom_sites.fract_transf_matrix[1][1]   0.010733 
_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]   0.009290 
_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]   0.008931 
_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   ? 60.392 70.479  -7.763  1.00 51.82 ? 7    VAL A N   1 
ATOM   2    C CA  . VAL A 1 7   ? 60.320 71.635  -6.806  1.00 51.42 ? 7    VAL A CA  1 
ATOM   3    C C   . VAL A 1 7   ? 61.354 71.415  -5.711  1.00 50.79 ? 7    VAL A C   1 
ATOM   4    O O   . VAL A 1 7   ? 61.577 70.280  -5.264  1.00 51.88 ? 7    VAL A O   1 
ATOM   5    C CB  . VAL A 1 7   ? 58.907 71.841  -6.160  1.00 52.18 ? 7    VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 7   ? 58.835 73.182  -5.362  1.00 51.87 ? 7    VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 7   ? 57.810 71.825  -7.209  1.00 51.99 ? 7    VAL A CG2 1 
ATOM   8    N N   . ASN A 1 8   ? 62.025 72.495  -5.320  1.00 48.54 ? 8    ASN A N   1 
ATOM   9    C CA  . ASN A 1 8   ? 62.805 72.493  -4.106  1.00 46.16 ? 8    ASN A CA  1 
ATOM   10   C C   . ASN A 1 8   ? 61.819 72.364  -2.937  1.00 43.26 ? 8    ASN A C   1 
ATOM   11   O O   . ASN A 1 8   ? 60.830 73.096  -2.872  1.00 41.39 ? 8    ASN A O   1 
ATOM   12   C CB  . ASN A 1 8   ? 63.622 73.781  -3.988  1.00 46.52 ? 8    ASN A CB  1 
ATOM   13   C CG  . ASN A 1 8   ? 64.557 73.754  -2.793  1.00 49.89 ? 8    ASN A CG  1 
ATOM   14   O OD1 . ASN A 1 8   ? 64.182 74.171  -1.706  1.00 51.70 ? 8    ASN A OD1 1 
ATOM   15   N ND2 . ASN A 1 8   ? 65.771 73.214  -2.980  1.00 52.50 ? 8    ASN A ND2 1 
ATOM   16   N N   . GLU A 1 9   ? 62.075 71.438  -2.027  1.00 40.29 ? 9    GLU A N   1 
ATOM   17   C CA  . GLU A 1 9   ? 61.129 71.222  -0.953  1.00 39.60 ? 9    GLU A CA  1 
ATOM   18   C C   . GLU A 1 9   ? 60.937 72.441  -0.021  1.00 36.22 ? 9    GLU A C   1 
ATOM   19   O O   . GLU A 1 9   ? 59.922 72.554  0.630   1.00 33.64 ? 9    GLU A O   1 
ATOM   20   C CB  . GLU A 1 9   ? 61.379 69.894  -0.214  1.00 39.71 ? 9    GLU A CB  1 
ATOM   21   C CG  . GLU A 1 9   ? 62.718 69.709  0.456   1.00 43.35 ? 9    GLU A CG  1 
ATOM   22   C CD  . GLU A 1 9   ? 62.895 68.268  1.013   1.00 44.95 ? 9    GLU A CD  1 
ATOM   23   O OE1 . GLU A 1 9   ? 62.813 67.287  0.209   1.00 52.52 ? 9    GLU A OE1 1 
ATOM   24   O OE2 . GLU A 1 9   ? 63.129 68.113  2.247   1.00 47.74 ? 9    GLU A OE2 1 
ATOM   25   N N   . LEU A 1 10  ? 61.903 73.364  0.000   1.00 33.41 ? 10   LEU A N   1 
ATOM   26   C CA  . LEU A 1 10  ? 61.792 74.544  0.871   1.00 32.24 ? 10   LEU A CA  1 
ATOM   27   C C   . LEU A 1 10  ? 60.826 75.593  0.322   1.00 30.64 ? 10   LEU A C   1 
ATOM   28   O O   . LEU A 1 10  ? 60.476 76.531  1.040   1.00 29.22 ? 10   LEU A O   1 
ATOM   29   C CB  . LEU A 1 10  ? 63.155 75.172  1.167   1.00 31.78 ? 10   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 10  ? 64.286 74.273  1.666   1.00 32.87 ? 10   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 10  ? 65.627 75.077  1.753   1.00 32.64 ? 10   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 10  ? 63.946 73.644  2.993   1.00 32.15 ? 10   LEU A CD2 1 
ATOM   33   N N   . GLU A 1 11  ? 60.424 75.411  -0.946  1.00 28.71 ? 11   GLU A N   1 
ATOM   34   C CA  . GLU A 1 11  ? 59.558 76.301  -1.669  1.00 28.45 ? 11   GLU A CA  1 
ATOM   35   C C   . GLU A 1 11  ? 58.126 75.802  -1.801  1.00 27.73 ? 11   GLU A C   1 
ATOM   36   O O   . GLU A 1 11  ? 57.309 76.474  -2.436  1.00 27.49 ? 11   GLU A O   1 
ATOM   37   C CB  . GLU A 1 11  ? 60.117 76.533  -3.080  1.00 29.40 ? 11   GLU A CB  1 
ATOM   38   C CG  . GLU A 1 11  ? 61.340 77.406  -3.067  1.00 34.15 ? 11   GLU A CG  1 
ATOM   39   C CD  . GLU A 1 11  ? 61.837 77.698  -4.462  1.00 43.52 ? 11   GLU A CD  1 
ATOM   40   O OE1 . GLU A 1 11  ? 61.050 78.236  -5.289  1.00 46.44 ? 11   GLU A OE1 1 
ATOM   41   O OE2 . GLU A 1 11  ? 63.015 77.383  -4.725  1.00 46.11 ? 11   GLU A OE2 1 
ATOM   42   N N   . ARG A 1 12  ? 57.820 74.619  -1.255  1.00 26.71 ? 12   ARG A N   1 
ATOM   43   C CA  A ARG A 1 12  ? 56.454 74.086  -1.314  0.50 26.31 ? 12   ARG A CA  1 
ATOM   44   C CA  B ARG A 1 12  ? 56.451 74.100  -1.353  0.50 26.49 ? 12   ARG A CA  1 
ATOM   45   C C   . ARG A 1 12  ? 55.546 74.923  -0.446  1.00 25.95 ? 12   ARG A C   1 
ATOM   46   O O   . ARG A 1 12  ? 55.879 75.215  0.728   1.00 25.16 ? 12   ARG A O   1 
ATOM   47   C CB  A ARG A 1 12  ? 56.408 72.664  -0.786  0.50 26.09 ? 12   ARG A CB  1 
ATOM   48   C CB  B ARG A 1 12  ? 56.373 72.600  -1.025  0.50 26.49 ? 12   ARG A CB  1 
ATOM   49   C CG  A ARG A 1 12  ? 57.150 71.645  -1.607  0.50 27.07 ? 12   ARG A CG  1 
ATOM   50   C CG  B ARG A 1 12  ? 57.610 71.817  -1.464  0.50 28.16 ? 12   ARG A CG  1 
ATOM   51   C CD  A ARG A 1 12  ? 57.092 70.353  -0.849  0.50 28.17 ? 12   ARG A CD  1 
ATOM   52   C CD  B ARG A 1 12  ? 57.364 70.446  -2.065  0.50 30.10 ? 12   ARG A CD  1 
ATOM   53   N NE  A ARG A 1 12  ? 58.091 69.366  -1.245  0.50 28.43 ? 12   ARG A NE  1 
ATOM   54   N NE  B ARG A 1 12  ? 58.615 69.940  -2.621  0.50 29.75 ? 12   ARG A NE  1 
ATOM   55   C CZ  A ARG A 1 12  ? 58.024 68.079  -0.911  0.50 27.76 ? 12   ARG A CZ  1 
ATOM   56   C CZ  B ARG A 1 12  ? 58.964 68.662  -2.728  0.50 31.39 ? 12   ARG A CZ  1 
ATOM   57   N NH1 A ARG A 1 12  ? 56.969 67.598  -0.208  0.50 20.22 ? 12   ARG A NH1 1 
ATOM   58   N NH1 B ARG A 1 12  ? 58.135 67.708  -2.345  0.50 32.46 ? 12   ARG A NH1 1 
ATOM   59   N NH2 A ARG A 1 12  ? 59.011 67.277  -1.297  0.50 25.59 ? 12   ARG A NH2 1 
ATOM   60   N NH2 B ARG A 1 12  ? 60.159 68.342  -3.237  0.50 30.45 ? 12   ARG A NH2 1 
ATOM   61   N N   . ILE A 1 13  ? 54.407 75.309  -1.004  1.00 25.69 ? 13   ILE A N   1 
ATOM   62   C CA  . ILE A 1 13  ? 53.440 76.040  -0.255  1.00 25.07 ? 13   ILE A CA  1 
ATOM   63   C C   . ILE A 1 13  ? 52.334 75.049  0.104   1.00 26.14 ? 13   ILE A C   1 
ATOM   64   O O   . ILE A 1 13  ? 51.662 74.505  -0.781  1.00 25.27 ? 13   ILE A O   1 
ATOM   65   C CB  . ILE A 1 13  ? 52.924 77.267  -1.032  1.00 25.14 ? 13   ILE A CB  1 
ATOM   66   C CG1 . ILE A 1 13  ? 54.084 78.201  -1.447  1.00 22.23 ? 13   ILE A CG1 1 
ATOM   67   C CG2 . ILE A 1 13  ? 51.841 78.008  -0.217  1.00 25.14 ? 13   ILE A CG2 1 
ATOM   68   C CD1 . ILE A 1 13  ? 54.656 78.986  -0.286  1.00 20.44 ? 13   ILE A CD1 1 
ATOM   69   N N   . ASN A 1 14  ? 52.198 74.814  1.415   1.00 26.67 ? 14   ASN A N   1 
ATOM   70   C CA  . ASN A 1 14  ? 51.229 73.882  1.967   1.00 26.51 ? 14   ASN A CA  1 
ATOM   71   C C   . ASN A 1 14  ? 49.801 74.116  1.465   1.00 26.78 ? 14   ASN A C   1 
ATOM   72   O O   . ASN A 1 14  ? 49.228 75.196  1.642   1.00 25.38 ? 14   ASN A O   1 
ATOM   73   C CB  . ASN A 1 14  ? 51.312 73.933  3.503   1.00 26.85 ? 14   ASN A CB  1 
ATOM   74   C CG  . ASN A 1 14  ? 50.397 72.912  4.189   1.00 29.95 ? 14   ASN A CG  1 
ATOM   75   O OD1 . ASN A 1 14  ? 49.923 71.959  3.565   1.00 28.19 ? 14   ASN A OD1 1 
ATOM   76   N ND2 . ASN A 1 14  ? 50.110 73.146  5.481   1.00 31.71 ? 14   ASN A ND2 1 
ATOM   77   N N   . CYS A 1 15  ? 49.237 73.066  0.843   1.00 29.07 ? 15   CYS A N   1 
ATOM   78   C CA  . CYS A 1 15  ? 47.902 73.069  0.279   1.00 29.90 ? 15   CYS A CA  1 
ATOM   79   C C   . CYS A 1 15  ? 46.869 72.507  1.301   1.00 29.78 ? 15   CYS A C   1 
ATOM   80   O O   . CYS A 1 15  ? 45.657 72.613  1.099   1.00 29.61 ? 15   CYS A O   1 
ATOM   81   C CB  . CYS A 1 15  ? 47.944 72.217  -1.033  1.00 30.45 ? 15   CYS A CB  1 
ATOM   82   S SG  . CYS A 1 15  ? 46.358 71.913  -1.803  1.00 38.51 ? 15   CYS A SG  1 
ATOM   83   N N   . ILE A 1 16  ? 47.340 71.901  2.387   1.00 28.40 ? 16   ILE A N   1 
ATOM   84   C CA  . ILE A 1 16  ? 46.414 71.401  3.428   1.00 28.74 ? 16   ILE A CA  1 
ATOM   85   C C   . ILE A 1 16  ? 46.762 72.030  4.787   1.00 29.56 ? 16   ILE A C   1 
ATOM   86   O O   . ILE A 1 16  ? 47.435 71.406  5.638   1.00 29.86 ? 16   ILE A O   1 
ATOM   87   C CB  . ILE A 1 16  ? 46.350 69.824  3.481   1.00 28.22 ? 16   ILE A CB  1 
ATOM   88   C CG1 . ILE A 1 16  ? 45.866 69.261  2.126   1.00 27.15 ? 16   ILE A CG1 1 
ATOM   89   C CG2 . ILE A 1 16  ? 45.360 69.337  4.596   1.00 28.96 ? 16   ILE A CG2 1 
ATOM   90   C CD1 . ILE A 1 16  ? 45.973 67.728  1.988   1.00 28.37 ? 16   ILE A CD1 1 
ATOM   91   N N   . PRO A 1 17  ? 46.392 73.300  4.956   1.00 31.00 ? 17   PRO A N   1 
ATOM   92   C CA  . PRO A 1 17  ? 46.704 73.995  6.188   1.00 33.15 ? 17   PRO A CA  1 
ATOM   93   C C   . PRO A 1 17  ? 45.702 73.627  7.333   1.00 35.34 ? 17   PRO A C   1 
ATOM   94   O O   . PRO A 1 17  ? 45.972 73.918  8.511   1.00 36.63 ? 17   PRO A O   1 
ATOM   95   C CB  . PRO A 1 17  ? 46.533 75.463  5.779   1.00 33.21 ? 17   PRO A CB  1 
ATOM   96   C CG  . PRO A 1 17  ? 45.363 75.436  4.832   1.00 30.73 ? 17   PRO A CG  1 
ATOM   97   C CD  . PRO A 1 17  ? 45.634 74.169  4.015   1.00 31.84 ? 17   PRO A CD  1 
ATOM   98   N N   . ASP A 1 18  ? 44.608 72.953  6.971   1.00 35.60 ? 18   ASP A N   1 
ATOM   99   C CA  . ASP A 1 18  ? 43.421 72.784  7.808   1.00 37.74 ? 18   ASP A CA  1 
ATOM   100  C C   . ASP A 1 18  ? 43.217 71.372  8.412   1.00 39.30 ? 18   ASP A C   1 
ATOM   101  O O   . ASP A 1 18  ? 42.165 71.129  9.021   1.00 39.80 ? 18   ASP A O   1 
ATOM   102  C CB  . ASP A 1 18  ? 42.206 73.048  6.930   1.00 37.36 ? 18   ASP A CB  1 
ATOM   103  C CG  . ASP A 1 18  ? 42.191 72.144  5.654   1.00 39.14 ? 18   ASP A CG  1 
ATOM   104  O OD1 . ASP A 1 18  ? 43.238 72.022  4.971   1.00 39.42 ? 18   ASP A OD1 1 
ATOM   105  O OD2 . ASP A 1 18  ? 41.137 71.536  5.331   1.00 42.01 ? 18   ASP A OD2 1 
ATOM   106  N N   . GLN A 1 19  ? 44.150 70.441  8.213   1.00 39.58 ? 19   GLN A N   1 
ATOM   107  C CA  . GLN A 1 19  ? 43.932 69.044  8.637   1.00 40.84 ? 19   GLN A CA  1 
ATOM   108  C C   . GLN A 1 19  ? 45.219 68.253  8.439   1.00 40.73 ? 19   GLN A C   1 
ATOM   109  O O   . GLN A 1 19  ? 46.155 68.788  7.846   1.00 41.63 ? 19   GLN A O   1 
ATOM   110  C CB  . GLN A 1 19  ? 42.704 68.438  7.907   1.00 40.78 ? 19   GLN A CB  1 
ATOM   111  C CG  . GLN A 1 19  ? 42.907 67.896  6.524   1.00 40.69 ? 19   GLN A CG  1 
ATOM   112  C CD  . GLN A 1 19  ? 41.601 67.585  5.786   1.00 42.58 ? 19   GLN A CD  1 
ATOM   113  O OE1 . GLN A 1 19  ? 40.541 68.117  6.102   1.00 48.17 ? 19   GLN A OE1 1 
ATOM   114  N NE2 . GLN A 1 19  ? 41.685 66.741  4.792   1.00 42.29 ? 19   GLN A NE2 1 
ATOM   115  N N   . PRO A 1 20  ? 45.330 67.017  9.004   1.00 40.58 ? 20   PRO A N   1 
ATOM   116  C CA  . PRO A 1 20  ? 46.497 66.144  8.674   1.00 39.54 ? 20   PRO A CA  1 
ATOM   117  C C   . PRO A 1 20  ? 46.549 65.781  7.155   1.00 36.79 ? 20   PRO A C   1 
ATOM   118  O O   . PRO A 1 20  ? 45.537 65.347  6.623   1.00 35.96 ? 20   PRO A O   1 
ATOM   119  C CB  . PRO A 1 20  ? 46.237 64.885  9.529   1.00 39.78 ? 20   PRO A CB  1 
ATOM   120  C CG  . PRO A 1 20  ? 45.383 65.349  10.640  1.00 40.73 ? 20   PRO A CG  1 
ATOM   121  C CD  . PRO A 1 20  ? 44.460 66.377  10.012  1.00 41.36 ? 20   PRO A CD  1 
ATOM   122  N N   . PRO A 1 21  ? 47.709 65.949  6.480   1.00 35.42 ? 21   PRO A N   1 
ATOM   123  C CA  . PRO A 1 21  ? 47.719 65.784  5.008   1.00 34.19 ? 21   PRO A CA  1 
ATOM   124  C C   . PRO A 1 21  ? 47.446 64.338  4.560   1.00 32.84 ? 21   PRO A C   1 
ATOM   125  O O   . PRO A 1 21  ? 48.056 63.405  5.068   1.00 32.37 ? 21   PRO A O   1 
ATOM   126  C CB  . PRO A 1 21  ? 49.166 66.094  4.633   1.00 33.87 ? 21   PRO A CB  1 
ATOM   127  C CG  . PRO A 1 21  ? 49.927 65.712  5.859   1.00 35.58 ? 21   PRO A CG  1 
ATOM   128  C CD  . PRO A 1 21  ? 49.072 66.188  6.991   1.00 35.02 ? 21   PRO A CD  1 
ATOM   129  N N   . THR A 1 22  ? 46.598 64.186  3.561   1.00 32.17 ? 22   THR A N   1 
ATOM   130  C CA  . THR A 1 22  ? 46.380 62.878  2.932   1.00 32.14 ? 22   THR A CA  1 
ATOM   131  C C   . THR A 1 22  ? 46.228 63.028  1.426   1.00 32.88 ? 22   THR A C   1 
ATOM   132  O O   . THR A 1 22  ? 45.815 64.090  0.954   1.00 31.61 ? 22   THR A O   1 
ATOM   133  C CB  . THR A 1 22  ? 45.094 62.257  3.406   1.00 30.69 ? 22   THR A CB  1 
ATOM   134  O OG1 . THR A 1 22  ? 44.002 63.116  3.024   1.00 30.79 ? 22   THR A OG1 1 
ATOM   135  C CG2 . THR A 1 22  ? 45.133 62.038  4.932   1.00 30.65 ? 22   THR A CG2 1 
ATOM   136  N N   . LYS A 1 23  ? 46.524 61.950  0.698   1.00 34.35 ? 23   LYS A N   1 
ATOM   137  C CA  . LYS A 1 23  ? 46.450 61.950  -0.776  1.00 35.30 ? 23   LYS A CA  1 
ATOM   138  C C   . LYS A 1 23  ? 45.071 62.230  -1.304  1.00 36.24 ? 23   LYS A C   1 
ATOM   139  O O   . LYS A 1 23  ? 44.921 63.015  -2.246  1.00 36.67 ? 23   LYS A O   1 
ATOM   140  C CB  . LYS A 1 23  ? 47.012 60.662  -1.375  1.00 36.21 ? 23   LYS A CB  1 
ATOM   141  C CG  . LYS A 1 23  ? 47.145 60.714  -2.906  1.00 37.14 ? 23   LYS A CG  1 
ATOM   142  C CD  . LYS A 1 23  ? 48.132 59.657  -3.396  1.00 41.54 ? 23   LYS A CD  1 
ATOM   143  C CE  . LYS A 1 23  ? 48.331 59.676  -4.934  1.00 41.83 ? 23   LYS A CE  1 
ATOM   144  N NZ  . LYS A 1 23  ? 47.196 60.255  -5.723  1.00 45.20 ? 23   LYS A NZ  1 
ATOM   145  N N   . ALA A 1 24  ? 44.057 61.623  -0.704  1.00 36.76 ? 24   ALA A N   1 
ATOM   146  C CA  . ALA A 1 24  ? 42.687 61.820  -1.145  1.00 38.06 ? 24   ALA A CA  1 
ATOM   147  C C   . ALA A 1 24  ? 42.337 63.302  -1.168  1.00 38.69 ? 24   ALA A C   1 
ATOM   148  O O   . ALA A 1 24  ? 41.867 63.810  -2.199  1.00 39.59 ? 24   ALA A O   1 
ATOM   149  C CB  . ALA A 1 24  ? 41.695 61.036  -0.255  1.00 38.47 ? 24   ALA A CB  1 
ATOM   150  N N   . THR A 1 25  ? 42.576 64.004  -0.054  1.00 38.74 ? 25   THR A N   1 
ATOM   151  C CA  . THR A 1 25  ? 42.348 65.471  0.004   1.00 38.83 ? 25   THR A CA  1 
ATOM   152  C C   . THR A 1 25  ? 43.192 66.212  -1.034  1.00 38.24 ? 25   THR A C   1 
ATOM   153  O O   . THR A 1 25  ? 42.698 67.094  -1.705  1.00 38.07 ? 25   THR A O   1 
ATOM   154  C CB  . THR A 1 25  ? 42.674 66.068  1.386   1.00 38.61 ? 25   THR A CB  1 
ATOM   155  O OG1 . THR A 1 25  ? 42.064 65.278  2.414   1.00 41.45 ? 25   THR A OG1 1 
ATOM   156  C CG2 . THR A 1 25  ? 42.173 67.502  1.489   1.00 37.14 ? 25   THR A CG2 1 
ATOM   157  N N   . CYS A 1 26  ? 44.467 65.851  -1.118  1.00 39.79 ? 26   CYS A N   1 
ATOM   158  C CA  . CYS A 1 26  ? 45.392 66.419  -2.078  1.00 40.82 ? 26   CYS A CA  1 
ATOM   159  C C   . CYS A 1 26  ? 44.809 66.320  -3.490  1.00 41.66 ? 26   CYS A C   1 
ATOM   160  O O   . CYS A 1 26  ? 44.718 67.327  -4.198  1.00 41.18 ? 26   CYS A O   1 
ATOM   161  C CB  . CYS A 1 26  ? 46.720 65.685  -2.019  1.00 40.15 ? 26   CYS A CB  1 
ATOM   162  S SG  . CYS A 1 26  ? 47.964 66.255  -3.241  1.00 44.37 ? 26   CYS A SG  1 
ATOM   163  N N   . ASP A 1 27  ? 44.369 65.116  -3.870  1.00 43.24 ? 27   ASP A N   1 
ATOM   164  C CA  . ASP A 1 27  ? 43.826 64.841  -5.217  1.00 44.62 ? 27   ASP A CA  1 
ATOM   165  C C   . ASP A 1 27  ? 42.561 65.633  -5.465  1.00 45.27 ? 27   ASP A C   1 
ATOM   166  O O   . ASP A 1 27  ? 42.342 66.187  -6.553  1.00 45.81 ? 27   ASP A O   1 
ATOM   167  C CB  . ASP A 1 27  ? 43.539 63.345  -5.388  1.00 45.24 ? 27   ASP A CB  1 
ATOM   168  C CG  . ASP A 1 27  ? 44.802 62.530  -5.560  1.00 47.19 ? 27   ASP A CG  1 
ATOM   169  O OD1 . ASP A 1 27  ? 45.881 63.132  -5.795  1.00 49.59 ? 27   ASP A OD1 1 
ATOM   170  O OD2 . ASP A 1 27  ? 44.718 61.284  -5.476  1.00 51.22 ? 27   ASP A OD2 1 
ATOM   171  N N   . GLN A 1 28  ? 41.745 65.695  -4.427  1.00 44.97 ? 28   GLN A N   1 
ATOM   172  C CA  . GLN A 1 28  ? 40.493 66.413  -4.428  1.00 45.56 ? 28   GLN A CA  1 
ATOM   173  C C   . GLN A 1 28  ? 40.705 67.913  -4.673  1.00 45.18 ? 28   GLN A C   1 
ATOM   174  O O   . GLN A 1 28  ? 39.881 68.568  -5.306  1.00 45.51 ? 28   GLN A O   1 
ATOM   175  C CB  . GLN A 1 28  ? 39.859 66.147  -3.067  1.00 45.78 ? 28   GLN A CB  1 
ATOM   176  C CG  . GLN A 1 28  ? 38.516 66.744  -2.792  1.00 50.19 ? 28   GLN A CG  1 
ATOM   177  C CD  . GLN A 1 28  ? 37.889 66.119  -1.546  1.00 55.86 ? 28   GLN A CD  1 
ATOM   178  O OE1 . GLN A 1 28  ? 38.037 66.636  -0.427  1.00 58.45 ? 28   GLN A OE1 1 
ATOM   179  N NE2 . GLN A 1 28  ? 37.206 64.985  -1.730  1.00 57.37 ? 28   GLN A NE2 1 
ATOM   180  N N   . ARG A 1 29  ? 41.816 68.450  -4.153  1.00 45.19 ? 29   ARG A N   1 
ATOM   181  C CA  . ARG A 1 29  ? 42.118 69.879  -4.229  1.00 43.53 ? 29   ARG A CA  1 
ATOM   182  C C   . ARG A 1 29  ? 42.957 70.193  -5.456  1.00 43.23 ? 29   ARG A C   1 
ATOM   183  O O   . ARG A 1 29  ? 43.209 71.364  -5.762  1.00 43.30 ? 29   ARG A O   1 
ATOM   184  C CB  . ARG A 1 29  ? 42.837 70.341  -2.953  1.00 43.14 ? 29   ARG A CB  1 
ATOM   185  C CG  . ARG A 1 29  ? 41.926 70.327  -1.765  1.00 41.96 ? 29   ARG A CG  1 
ATOM   186  C CD  . ARG A 1 29  ? 42.507 70.896  -0.529  1.00 38.47 ? 29   ARG A CD  1 
ATOM   187  N NE  . ARG A 1 29  ? 41.524 70.738  0.531   1.00 37.65 ? 29   ARG A NE  1 
ATOM   188  C CZ  . ARG A 1 29  ? 41.714 71.091  1.792   1.00 38.76 ? 29   ARG A CZ  1 
ATOM   189  N NH1 . ARG A 1 29  ? 42.870 71.630  2.168   1.00 32.80 ? 29   ARG A NH1 1 
ATOM   190  N NH2 . ARG A 1 29  ? 40.745 70.892  2.679   1.00 37.67 ? 29   ARG A NH2 1 
ATOM   191  N N   . GLY A 1 30  ? 43.373 69.140  -6.159  1.00 42.52 ? 30   GLY A N   1 
ATOM   192  C CA  . GLY A 1 30  ? 44.219 69.276  -7.347  1.00 41.27 ? 30   GLY A CA  1 
ATOM   193  C C   . GLY A 1 30  ? 45.641 69.699  -7.075  1.00 40.94 ? 30   GLY A C   1 
ATOM   194  O O   . GLY A 1 30  ? 46.273 70.337  -7.926  1.00 41.48 ? 30   GLY A O   1 
ATOM   195  N N   . CYS A 1 31  ? 46.172 69.328  -5.905  1.00 39.47 ? 31   CYS A N   1 
ATOM   196  C CA  . CYS A 1 31  ? 47.510 69.749  -5.492  1.00 38.39 ? 31   CYS A CA  1 
ATOM   197  C C   . CYS A 1 31  ? 48.513 68.657  -5.756  1.00 38.35 ? 31   CYS A C   1 
ATOM   198  O O   . CYS A 1 31  ? 48.161 67.637  -6.349  1.00 38.90 ? 31   CYS A O   1 
ATOM   199  C CB  . CYS A 1 31  ? 47.496 70.153  -4.017  1.00 37.91 ? 31   CYS A CB  1 
ATOM   200  S SG  . CYS A 1 31  ? 46.663 71.717  -3.830  1.00 38.29 ? 31   CYS A SG  1 
ATOM   201  N N   . CYS A 1 32  ? 49.757 68.851  -5.337  1.00 37.57 ? 32   CYS A N   1 
ATOM   202  C CA  . CYS A 1 32  ? 50.797 67.886  -5.594  1.00 38.21 ? 32   CYS A CA  1 
ATOM   203  C C   . CYS A 1 32  ? 51.048 67.124  -4.321  1.00 38.35 ? 32   CYS A C   1 
ATOM   204  O O   . CYS A 1 32  ? 50.907 67.693  -3.254  1.00 36.64 ? 32   CYS A O   1 
ATOM   205  C CB  . CYS A 1 32  ? 52.082 68.576  -6.015  1.00 38.26 ? 32   CYS A CB  1 
ATOM   206  S SG  . CYS A 1 32  ? 51.836 69.745  -7.364  1.00 42.55 ? 32   CYS A SG  1 
ATOM   207  N N   . TRP A 1 33  ? 51.472 65.863  -4.448  1.00 37.63 ? 33   TRP A N   1 
ATOM   208  C CA  . TRP A 1 33  ? 51.589 64.979  -3.318  1.00 38.81 ? 33   TRP A CA  1 
ATOM   209  C C   . TRP A 1 33  ? 52.969 64.402  -3.306  1.00 39.60 ? 33   TRP A C   1 
ATOM   210  O O   . TRP A 1 33  ? 53.391 63.787  -4.285  1.00 40.38 ? 33   TRP A O   1 
ATOM   211  C CB  . TRP A 1 33  ? 50.560 63.829  -3.398  1.00 38.09 ? 33   TRP A CB  1 
ATOM   212  C CG  . TRP A 1 33  ? 50.695 62.848  -2.260  1.00 38.19 ? 33   TRP A CG  1 
ATOM   213  C CD1 . TRP A 1 33  ? 51.221 61.587  -2.324  1.00 38.36 ? 33   TRP A CD1 1 
ATOM   214  C CD2 . TRP A 1 33  ? 50.328 63.063  -0.882  1.00 38.50 ? 33   TRP A CD2 1 
ATOM   215  N NE1 . TRP A 1 33  ? 51.191 61.000  -1.075  1.00 38.94 ? 33   TRP A NE1 1 
ATOM   216  C CE2 . TRP A 1 33  ? 50.653 61.878  -0.174  1.00 38.59 ? 33   TRP A CE2 1 
ATOM   217  C CE3 . TRP A 1 33  ? 49.743 64.133  -0.183  1.00 37.71 ? 33   TRP A CE3 1 
ATOM   218  C CZ2 . TRP A 1 33  ? 50.421 61.734  1.209   1.00 38.88 ? 33   TRP A CZ2 1 
ATOM   219  C CZ3 . TRP A 1 33  ? 49.512 63.991  1.191   1.00 38.40 ? 33   TRP A CZ3 1 
ATOM   220  C CH2 . TRP A 1 33  ? 49.864 62.799  1.874   1.00 37.45 ? 33   TRP A CH2 1 
ATOM   221  N N   . ASN A 1 34  ? 53.676 64.578  -2.197  1.00 40.62 ? 34   ASN A N   1 
ATOM   222  C CA  . ASN A 1 34  ? 55.024 64.049  -2.078  1.00 42.56 ? 34   ASN A CA  1 
ATOM   223  C C   . ASN A 1 34  ? 55.386 63.954  -0.610  1.00 43.69 ? 34   ASN A C   1 
ATOM   224  O O   . ASN A 1 34  ? 55.986 64.873  -0.047  1.00 42.97 ? 34   ASN A O   1 
ATOM   225  C CB  . ASN A 1 34  ? 56.032 64.909  -2.877  1.00 42.92 ? 34   ASN A CB  1 
ATOM   226  C CG  . ASN A 1 34  ? 57.449 64.333  -2.886  1.00 45.06 ? 34   ASN A CG  1 
ATOM   227  O OD1 . ASN A 1 34  ? 57.774 63.417  -2.140  1.00 50.21 ? 34   ASN A OD1 1 
ATOM   228  N ND2 . ASN A 1 34  ? 58.299 64.888  -3.729  1.00 48.65 ? 34   ASN A ND2 1 
ATOM   229  N N   . PRO A 1 35  ? 55.036 62.824  0.023   1.00 44.87 ? 35   PRO A N   1 
ATOM   230  C CA  . PRO A 1 35  ? 55.360 62.679  1.430   1.00 46.45 ? 35   PRO A CA  1 
ATOM   231  C C   . PRO A 1 35  ? 56.808 62.320  1.717   1.00 48.38 ? 35   PRO A C   1 
ATOM   232  O O   . PRO A 1 35  ? 57.112 61.943  2.850   1.00 49.17 ? 35   PRO A O   1 
ATOM   233  C CB  . PRO A 1 35  ? 54.430 61.556  1.902   1.00 45.96 ? 35   PRO A CB  1 
ATOM   234  C CG  . PRO A 1 35  ? 54.102 60.775  0.680   1.00 46.01 ? 35   PRO A CG  1 
ATOM   235  C CD  . PRO A 1 35  ? 54.341 61.645  -0.526  1.00 45.48 ? 35   PRO A CD  1 
ATOM   236  N N   . GLN A 1 36  ? 57.701 62.462  0.745   1.00 50.53 ? 36   GLN A N   1 
ATOM   237  C CA  . GLN A 1 36  ? 59.078 61.998  0.948   1.00 53.41 ? 36   GLN A CA  1 
ATOM   238  C C   . GLN A 1 36  ? 60.029 63.083  1.485   1.00 53.98 ? 36   GLN A C   1 
ATOM   239  O O   . GLN A 1 36  ? 61.270 62.902  1.481   1.00 55.32 ? 36   GLN A O   1 
ATOM   240  C CB  . GLN A 1 36  ? 59.665 61.296  -0.305  1.00 53.93 ? 36   GLN A CB  1 
ATOM   241  C CG  . GLN A 1 36  ? 58.660 60.590  -1.272  1.00 57.89 ? 36   GLN A CG  1 
ATOM   242  C CD  . GLN A 1 36  ? 57.939 59.343  -0.712  1.00 61.87 ? 36   GLN A CD  1 
ATOM   243  O OE1 . GLN A 1 36  ? 58.122 58.942  0.452   1.00 62.97 ? 36   GLN A OE1 1 
ATOM   244  N NE2 . GLN A 1 36  ? 57.102 58.731  -1.561  1.00 62.14 ? 36   GLN A NE2 1 
ATOM   245  N N   . GLY A 1 37  ? 59.459 64.186  1.974   1.00 53.73 ? 37   GLY A N   1 
ATOM   246  C CA  . GLY A 1 37  ? 60.270 65.299  2.441   1.00 53.07 ? 37   GLY A CA  1 
ATOM   247  C C   . GLY A 1 37  ? 60.797 65.161  3.862   1.00 52.67 ? 37   GLY A C   1 
ATOM   248  O O   . GLY A 1 37  ? 60.406 64.236  4.598   1.00 53.57 ? 37   GLY A O   1 
ATOM   249  N N   . ALA A 1 38  ? 61.681 66.097  4.230   1.00 51.20 ? 38   ALA A N   1 
ATOM   250  C CA  . ALA A 1 38  ? 62.130 66.336  5.617   1.00 49.44 ? 38   ALA A CA  1 
ATOM   251  C C   . ALA A 1 38  ? 61.017 66.800  6.585   1.00 48.04 ? 38   ALA A C   1 
ATOM   252  O O   . ALA A 1 38  ? 59.931 67.182  6.167   1.00 47.20 ? 38   ALA A O   1 
ATOM   253  C CB  . ALA A 1 38  ? 63.253 67.361  5.597   1.00 49.69 ? 38   ALA A CB  1 
ATOM   254  N N   . VAL A 1 39  ? 61.293 66.788  7.886   1.00 46.27 ? 39   VAL A N   1 
ATOM   255  C CA  . VAL A 1 39  ? 60.293 67.210  8.863   1.00 44.84 ? 39   VAL A CA  1 
ATOM   256  C C   . VAL A 1 39  ? 59.695 68.609  8.575   1.00 43.07 ? 39   VAL A C   1 
ATOM   257  O O   . VAL A 1 39  ? 60.408 69.544  8.193   1.00 43.08 ? 39   VAL A O   1 
ATOM   258  C CB  . VAL A 1 39  ? 60.813 67.086  10.322  1.00 45.21 ? 39   VAL A CB  1 
ATOM   259  C CG1 . VAL A 1 39  ? 62.066 67.929  10.540  1.00 47.23 ? 39   VAL A CG1 1 
ATOM   260  C CG2 . VAL A 1 39  ? 59.721 67.456  11.318  1.00 46.36 ? 39   VAL A CG2 1 
ATOM   261  N N   . SER A 1 40  ? 58.378 68.705  8.738   1.00 40.72 ? 40   SER A N   1 
ATOM   262  C CA  . SER A 1 40  ? 57.579 69.925  8.526   1.00 38.93 ? 40   SER A CA  1 
ATOM   263  C C   . SER A 1 40  ? 57.436 70.368  7.065   1.00 35.64 ? 40   SER A C   1 
ATOM   264  O O   . SER A 1 40  ? 56.607 71.197  6.763   1.00 35.34 ? 40   SER A O   1 
ATOM   265  C CB  . SER A 1 40  ? 58.097 71.072  9.418   1.00 39.55 ? 40   SER A CB  1 
ATOM   266  O OG  . SER A 1 40  ? 57.596 70.930  10.742  1.00 42.13 ? 40   SER A OG  1 
ATOM   267  N N   . VAL A 1 41  ? 58.203 69.775  6.157   1.00 33.96 ? 41   VAL A N   1 
ATOM   268  C CA  . VAL A 1 41  ? 58.076 70.058  4.724   1.00 32.93 ? 41   VAL A CA  1 
ATOM   269  C C   . VAL A 1 41  ? 56.703 69.548  4.322   1.00 32.09 ? 41   VAL A C   1 
ATOM   270  O O   . VAL A 1 41  ? 56.393 68.405  4.646   1.00 32.32 ? 41   VAL A O   1 
ATOM   271  C CB  . VAL A 1 41  ? 59.154 69.353  3.900   1.00 32.28 ? 41   VAL A CB  1 
ATOM   272  C CG1 . VAL A 1 41  ? 58.828 69.462  2.449   1.00 33.38 ? 41   VAL A CG1 1 
ATOM   273  C CG2 . VAL A 1 41  ? 60.533 69.983  4.171   1.00 34.10 ? 41   VAL A CG2 1 
ATOM   274  N N   . PRO A 1 42  ? 55.866 70.397  3.675   1.00 31.07 ? 42   PRO A N   1 
ATOM   275  C CA  . PRO A 1 42  ? 54.499 70.003  3.332   1.00 30.88 ? 42   PRO A CA  1 
ATOM   276  C C   . PRO A 1 42  ? 54.417 68.815  2.381   1.00 31.15 ? 42   PRO A C   1 
ATOM   277  O O   . PRO A 1 42  ? 55.007 68.853  1.291   1.00 29.59 ? 42   PRO A O   1 
ATOM   278  C CB  . PRO A 1 42  ? 53.912 71.242  2.623   1.00 31.26 ? 42   PRO A CB  1 
ATOM   279  C CG  . PRO A 1 42  ? 54.837 72.347  2.910   1.00 30.17 ? 42   PRO A CG  1 
ATOM   280  C CD  . PRO A 1 42  ? 56.155 71.779  3.261   1.00 30.92 ? 42   PRO A CD  1 
ATOM   281  N N   . TRP A 1 43  ? 53.665 67.785  2.800   1.00 30.38 ? 43   TRP A N   1 
ATOM   282  C CA  . TRP A 1 43  ? 53.363 66.629  1.937   1.00 30.59 ? 43   TRP A CA  1 
ATOM   283  C C   . TRP A 1 43  ? 52.485 67.007  0.778   1.00 29.28 ? 43   TRP A C   1 
ATOM   284  O O   . TRP A 1 43  ? 52.593 66.455  -0.304  1.00 29.41 ? 43   TRP A O   1 
ATOM   285  C CB  . TRP A 1 43  ? 52.671 65.540  2.761   1.00 31.01 ? 43   TRP A CB  1 
ATOM   286  C CG  . TRP A 1 43  ? 53.608 64.869  3.660   1.00 31.66 ? 43   TRP A CG  1 
ATOM   287  C CD1 . TRP A 1 43  ? 54.934 65.168  3.842   1.00 34.28 ? 43   TRP A CD1 1 
ATOM   288  C CD2 . TRP A 1 43  ? 53.324 63.770  4.522   1.00 32.73 ? 43   TRP A CD2 1 
ATOM   289  N NE1 . TRP A 1 43  ? 55.478 64.337  4.779   1.00 33.41 ? 43   TRP A NE1 1 
ATOM   290  C CE2 . TRP A 1 43  ? 54.517 63.458  5.205   1.00 34.66 ? 43   TRP A CE2 1 
ATOM   291  C CE3 . TRP A 1 43  ? 52.173 63.009  4.782   1.00 34.13 ? 43   TRP A CE3 1 
ATOM   292  C CZ2 . TRP A 1 43  ? 54.596 62.416  6.144   1.00 35.90 ? 43   TRP A CZ2 1 
ATOM   293  C CZ3 . TRP A 1 43  ? 52.246 61.987  5.728   1.00 32.67 ? 43   TRP A CZ3 1 
ATOM   294  C CH2 . TRP A 1 43  ? 53.449 61.696  6.387   1.00 34.22 ? 43   TRP A CH2 1 
ATOM   295  N N   . CYS A 1 44  ? 51.573 67.933  1.003   1.00 30.44 ? 44   CYS A N   1 
ATOM   296  C CA  . CYS A 1 44  ? 50.665 68.314  -0.051  1.00 29.63 ? 44   CYS A CA  1 
ATOM   297  C C   . CYS A 1 44  ? 50.830 69.801  -0.317  1.00 29.28 ? 44   CYS A C   1 
ATOM   298  O O   . CYS A 1 44  ? 50.707 70.625  0.606   1.00 27.61 ? 44   CYS A O   1 
ATOM   299  C CB  . CYS A 1 44  ? 49.240 68.013  0.356   1.00 29.75 ? 44   CYS A CB  1 
ATOM   300  S SG  . CYS A 1 44  ? 48.122 68.625  -0.835  1.00 34.71 ? 44   CYS A SG  1 
ATOM   301  N N   . TYR A 1 45  ? 51.148 70.140  -1.565  1.00 29.02 ? 45   TYR A N   1 
ATOM   302  C CA  . TYR A 1 45  ? 51.524 71.511  -1.875  1.00 30.08 ? 45   TYR A CA  1 
ATOM   303  C C   . TYR A 1 45  ? 50.991 71.960  -3.232  1.00 30.23 ? 45   TYR A C   1 
ATOM   304  O O   . TYR A 1 45  ? 50.629 71.142  -4.072  1.00 29.83 ? 45   TYR A O   1 
ATOM   305  C CB  . TYR A 1 45  ? 53.038 71.666  -1.797  1.00 30.82 ? 45   TYR A CB  1 
ATOM   306  C CG  . TYR A 1 45  ? 53.777 70.805  -2.781  1.00 32.04 ? 45   TYR A CG  1 
ATOM   307  C CD1 . TYR A 1 45  ? 54.123 71.294  -4.041  1.00 33.39 ? 45   TYR A CD1 1 
ATOM   308  C CD2 . TYR A 1 45  ? 54.138 69.500  -2.455  1.00 31.21 ? 45   TYR A CD2 1 
ATOM   309  C CE1 . TYR A 1 45  ? 54.819 70.497  -4.957  1.00 33.98 ? 45   TYR A CE1 1 
ATOM   310  C CE2 . TYR A 1 45  ? 54.823 68.691  -3.355  1.00 33.31 ? 45   TYR A CE2 1 
ATOM   311  C CZ  . TYR A 1 45  ? 55.160 69.200  -4.603  1.00 34.83 ? 45   TYR A CZ  1 
ATOM   312  O OH  . TYR A 1 45  ? 55.845 68.410  -5.505  1.00 37.05 ? 45   TYR A OH  1 
ATOM   313  N N   . TYR A 1 46  ? 50.933 73.261  -3.431  1.00 30.81 ? 46   TYR A N   1 
ATOM   314  C CA  . TYR A 1 46  ? 50.253 73.807  -4.568  1.00 32.83 ? 46   TYR A CA  1 
ATOM   315  C C   . TYR A 1 46  ? 51.073 73.527  -5.822  1.00 34.94 ? 46   TYR A C   1 
ATOM   316  O O   . TYR A 1 46  ? 52.319 73.543  -5.793  1.00 33.30 ? 46   TYR A O   1 
ATOM   317  C CB  . TYR A 1 46  ? 50.042 75.290  -4.394  1.00 32.01 ? 46   TYR A CB  1 
ATOM   318  C CG  . TYR A 1 46  ? 48.976 75.601  -3.390  1.00 32.53 ? 46   TYR A CG  1 
ATOM   319  C CD1 . TYR A 1 46  ? 47.632 75.397  -3.683  1.00 29.12 ? 46   TYR A CD1 1 
ATOM   320  C CD2 . TYR A 1 46  ? 49.305 76.054  -2.121  1.00 32.05 ? 46   TYR A CD2 1 
ATOM   321  C CE1 . TYR A 1 46  ? 46.643 75.671  -2.727  1.00 29.91 ? 46   TYR A CE1 1 
ATOM   322  C CE2 . TYR A 1 46  ? 48.320 76.329  -1.177  1.00 33.27 ? 46   TYR A CE2 1 
ATOM   323  C CZ  . TYR A 1 46  ? 46.994 76.124  -1.498  1.00 30.52 ? 46   TYR A CZ  1 
ATOM   324  O OH  . TYR A 1 46  ? 46.035 76.398  -0.568  1.00 32.02 ? 46   TYR A OH  1 
ATOM   325  N N   . SER A 1 47  ? 50.360 73.230  -6.898  1.00 38.33 ? 47   SER A N   1 
ATOM   326  C CA  . SER A 1 47  ? 50.976 73.027  -8.207  1.00 42.96 ? 47   SER A CA  1 
ATOM   327  C C   . SER A 1 47  ? 51.364 74.369  -8.814  1.00 45.22 ? 47   SER A C   1 
ATOM   328  O O   . SER A 1 47  ? 51.092 75.426  -8.241  1.00 45.09 ? 47   SER A O   1 
ATOM   329  C CB  . SER A 1 47  ? 50.024 72.273  -9.136  1.00 42.38 ? 47   SER A CB  1 
ATOM   330  O OG  . SER A 1 47  ? 48.839 73.027  -9.337  1.00 44.93 ? 47   SER A OG  1 
ATOM   331  N N   . LYS A 1 48  ? 52.014 74.314  -9.972  1.00 49.23 ? 48   LYS A N   1 
ATOM   332  C CA  . LYS A 1 48  ? 52.590 75.504  -10.595 1.00 52.77 ? 48   LYS A CA  1 
ATOM   333  C C   . LYS A 1 48  ? 51.525 76.409  -11.221 1.00 53.84 ? 48   LYS A C   1 
ATOM   334  O O   . LYS A 1 48  ? 51.752 77.618  -11.346 1.00 54.71 ? 48   LYS A O   1 
ATOM   335  C CB  . LYS A 1 48  ? 53.654 75.114  -11.630 1.00 52.59 ? 48   LYS A CB  1 
ATOM   336  C CG  . LYS A 1 48  ? 54.807 74.277  -11.046 1.00 54.20 ? 48   LYS A CG  1 
ATOM   337  C CD  . LYS A 1 48  ? 55.706 73.656  -12.137 1.00 55.62 ? 48   LYS A CD  1 
ATOM   338  C CE  . LYS A 1 48  ? 56.439 74.737  -12.984 1.00 60.05 ? 48   LYS A CE  1 
ATOM   339  N NZ  . LYS A 1 48  ? 57.175 75.746  -12.141 1.00 61.10 ? 48   LYS A NZ  1 
ATOM   340  N N   . ASN A 1 49  ? 50.387 75.822  -11.596 1.00 55.50 ? 49   ASN A N   1 
ATOM   341  C CA  . ASN A 1 49  ? 49.252 76.554  -12.181 1.00 57.00 ? 49   ASN A CA  1 
ATOM   342  C C   . ASN A 1 49  ? 47.926 76.276  -11.452 1.00 57.33 ? 49   ASN A C   1 
ATOM   343  O O   . ASN A 1 49  ? 47.143 75.386  -11.841 1.00 58.53 ? 49   ASN A O   1 
ATOM   344  C CB  . ASN A 1 49  ? 49.121 76.236  -13.681 1.00 57.77 ? 49   ASN A CB  1 
ATOM   345  C CG  . ASN A 1 49  ? 48.707 77.459  -14.514 1.00 60.13 ? 49   ASN A CG  1 
ATOM   346  O OD1 . ASN A 1 49  ? 47.625 78.046  -14.308 1.00 61.70 ? 49   ASN A OD1 1 
ATOM   347  N ND2 . ASN A 1 49  ? 49.572 77.846  -15.463 1.00 61.83 ? 49   ASN A ND2 1 
ATOM   348  N N   . HIS A 1 50  ? 47.662 77.041  -10.396 1.00 56.95 ? 50   HIS A N   1 
ATOM   349  C CA  . HIS A 1 50  ? 46.514 76.751  -9.539  1.00 56.13 ? 50   HIS A CA  1 
ATOM   350  C C   . HIS A 1 50  ? 45.420 77.791  -9.746  1.00 54.41 ? 50   HIS A C   1 
ATOM   351  O O   . HIS A 1 50  ? 44.245 77.459  -9.962  1.00 55.33 ? 50   HIS A O   1 
ATOM   352  C CB  . HIS A 1 50  ? 46.949 76.702  -8.047  1.00 57.33 ? 50   HIS A CB  1 
ATOM   353  C CG  . HIS A 1 50  ? 45.955 76.035  -7.135  1.00 59.52 ? 50   HIS A CG  1 
ATOM   354  N ND1 . HIS A 1 50  ? 45.884 74.664  -6.982  1.00 61.17 ? 50   HIS A ND1 1 
ATOM   355  C CD2 . HIS A 1 50  ? 44.994 76.552  -6.326  1.00 62.05 ? 50   HIS A CD2 1 
ATOM   356  C CE1 . HIS A 1 50  ? 44.920 74.364  -6.126  1.00 62.75 ? 50   HIS A CE1 1 
ATOM   357  N NE2 . HIS A 1 50  ? 44.365 75.491  -5.711  1.00 63.57 ? 50   HIS A NE2 1 
ATOM   358  N N   . SER A 1 51  ? 45.831 79.050  -9.735  1.00 51.37 ? 51   SER A N   1 
ATOM   359  C CA  . SER A 1 51  ? 44.961 80.104  -9.272  1.00 48.21 ? 51   SER A CA  1 
ATOM   360  C C   . SER A 1 51  ? 44.452 81.032  -10.366 1.00 45.41 ? 51   SER A C   1 
ATOM   361  O O   . SER A 1 51  ? 43.678 80.630  -11.235 1.00 46.11 ? 51   SER A O   1 
ATOM   362  C CB  . SER A 1 51  ? 45.667 80.916  -8.161  1.00 48.82 ? 51   SER A CB  1 
ATOM   363  O OG  . SER A 1 51  ? 46.885 81.503  -8.631  1.00 48.28 ? 51   SER A OG  1 
ATOM   364  N N   . TYR A 1 52  ? 44.863 82.285  -10.284 1.00 41.07 ? 52   TYR A N   1 
ATOM   365  C CA  . TYR A 1 52  ? 44.310 83.324  -11.115 1.00 37.19 ? 52   TYR A CA  1 
ATOM   366  C C   . TYR A 1 52  ? 45.282 83.575  -12.239 1.00 35.03 ? 52   TYR A C   1 
ATOM   367  O O   . TYR A 1 52  ? 46.443 83.209  -12.158 1.00 33.94 ? 52   TYR A O   1 
ATOM   368  C CB  . TYR A 1 52  ? 44.075 84.589  -10.302 1.00 36.83 ? 52   TYR A CB  1 
ATOM   369  C CG  . TYR A 1 52  ? 42.930 84.495  -9.319  1.00 34.71 ? 52   TYR A CG  1 
ATOM   370  C CD1 . TYR A 1 52  ? 43.084 83.836  -8.119  1.00 35.66 ? 52   TYR A CD1 1 
ATOM   371  C CD2 . TYR A 1 52  ? 41.714 85.091  -9.582  1.00 36.44 ? 52   TYR A CD2 1 
ATOM   372  C CE1 . TYR A 1 52  ? 42.054 83.739  -7.215  1.00 34.83 ? 52   TYR A CE1 1 
ATOM   373  C CE2 . TYR A 1 52  ? 40.667 85.002  -8.687  1.00 34.85 ? 52   TYR A CE2 1 
ATOM   374  C CZ  . TYR A 1 52  ? 40.853 84.312  -7.501  1.00 35.85 ? 52   TYR A CZ  1 
ATOM   375  O OH  . TYR A 1 52  ? 39.848 84.216  -6.571  1.00 37.10 ? 52   TYR A OH  1 
ATOM   376  N N   . HIS A 1 53  ? 44.769 84.154  -13.302 1.00 33.18 ? 53   HIS A N   1 
ATOM   377  C CA  . HIS A 1 53  ? 45.584 84.634  -14.390 1.00 32.53 ? 53   HIS A CA  1 
ATOM   378  C C   . HIS A 1 53  ? 45.075 86.039  -14.701 1.00 31.55 ? 53   HIS A C   1 
ATOM   379  O O   . HIS A 1 53  ? 43.907 86.371  -14.426 1.00 30.37 ? 53   HIS A O   1 
ATOM   380  C CB  . HIS A 1 53  ? 45.466 83.704  -15.613 1.00 33.25 ? 53   HIS A CB  1 
ATOM   381  C CG  . HIS A 1 53  ? 44.077 83.635  -16.181 1.00 35.09 ? 53   HIS A CG  1 
ATOM   382  N ND1 . HIS A 1 53  ? 43.543 84.632  -16.977 1.00 39.82 ? 53   HIS A ND1 1 
ATOM   383  C CD2 . HIS A 1 53  ? 43.109 82.699  -16.057 1.00 37.23 ? 53   HIS A CD2 1 
ATOM   384  C CE1 . HIS A 1 53  ? 42.306 84.312  -17.319 1.00 39.08 ? 53   HIS A CE1 1 
ATOM   385  N NE2 . HIS A 1 53  ? 42.018 83.142  -16.776 1.00 38.68 ? 53   HIS A NE2 1 
ATOM   386  N N   . VAL A 1 54  ? 45.934 86.876  -15.271 1.00 29.62 ? 54   VAL A N   1 
ATOM   387  C CA  . VAL A 1 54  ? 45.464 88.179  -15.696 1.00 29.90 ? 54   VAL A CA  1 
ATOM   388  C C   . VAL A 1 54  ? 44.595 87.968  -16.940 1.00 30.61 ? 54   VAL A C   1 
ATOM   389  O O   . VAL A 1 54  ? 44.939 87.174  -17.818 1.00 29.81 ? 54   VAL A O   1 
ATOM   390  C CB  . VAL A 1 54  ? 46.653 89.142  -16.000 1.00 30.93 ? 54   VAL A CB  1 
ATOM   391  C CG1 . VAL A 1 54  ? 46.148 90.450  -16.519 1.00 27.11 ? 54   VAL A CG1 1 
ATOM   392  C CG2 . VAL A 1 54  ? 47.495 89.356  -14.719 1.00 29.89 ? 54   VAL A CG2 1 
ATOM   393  N N   . GLU A 1 55  ? 43.459 88.647  -16.963 1.00 32.47 ? 55   GLU A N   1 
ATOM   394  C CA  . GLU A 1 55  ? 42.544 88.638  -18.073 1.00 35.20 ? 55   GLU A CA  1 
ATOM   395  C C   . GLU A 1 55  ? 42.757 89.939  -18.829 1.00 35.06 ? 55   GLU A C   1 
ATOM   396  O O   . GLU A 1 55  ? 42.500 91.015  -18.296 1.00 36.41 ? 55   GLU A O   1 
ATOM   397  C CB  . GLU A 1 55  ? 41.107 88.579  -17.557 1.00 36.66 ? 55   GLU A CB  1 
ATOM   398  C CG  . GLU A 1 55  ? 40.022 88.579  -18.640 1.00 43.60 ? 55   GLU A CG  1 
ATOM   399  C CD  . GLU A 1 55  ? 39.953 87.273  -19.460 1.00 51.68 ? 55   GLU A CD  1 
ATOM   400  O OE1 . GLU A 1 55  ? 40.515 86.228  -19.031 1.00 54.48 ? 55   GLU A OE1 1 
ATOM   401  O OE2 . GLU A 1 55  ? 39.313 87.296  -20.550 1.00 56.20 ? 55   GLU A OE2 1 
ATOM   402  N N   . GLY A 1 56  ? 43.238 89.847  -20.062 1.00 34.47 ? 56   GLY A N   1 
ATOM   403  C CA  . GLY A 1 56  ? 43.348 91.041  -20.894 1.00 33.61 ? 56   GLY A CA  1 
ATOM   404  C C   . GLY A 1 56  ? 44.519 91.896  -20.456 1.00 32.50 ? 56   GLY A C   1 
ATOM   405  O O   . GLY A 1 56  ? 45.542 91.376  -20.002 1.00 32.43 ? 56   GLY A O   1 
ATOM   406  N N   . ASN A 1 57  ? 44.398 93.201  -20.598 1.00 31.40 ? 57   ASN A N   1 
ATOM   407  C CA  . ASN A 1 57  ? 45.582 94.035  -20.428 1.00 31.05 ? 57   ASN A CA  1 
ATOM   408  C C   . ASN A 1 57  ? 45.511 94.773  -19.114 1.00 31.04 ? 57   ASN A C   1 
ATOM   409  O O   . ASN A 1 57  ? 44.417 95.068  -18.617 1.00 31.25 ? 57   ASN A O   1 
ATOM   410  C CB  . ASN A 1 57  ? 45.726 95.070  -21.557 1.00 30.12 ? 57   ASN A CB  1 
ATOM   411  C CG  . ASN A 1 57  ? 45.934 94.437  -22.947 1.00 30.57 ? 57   ASN A CG  1 
ATOM   412  O OD1 . ASN A 1 57  ? 46.503 93.368  -23.097 1.00 30.89 ? 57   ASN A OD1 1 
ATOM   413  N ND2 . ASN A 1 57  ? 45.478 95.128  -23.949 1.00 31.07 ? 57   ASN A ND2 1 
ATOM   414  N N   . LEU A 1 58  ? 46.673 95.162  -18.611 1.00 28.94 ? 58   LEU A N   1 
ATOM   415  C CA  . LEU A 1 58  ? 46.734 96.090  -17.496 1.00 29.12 ? 58   LEU A CA  1 
ATOM   416  C C   . LEU A 1 58  ? 46.365 97.485  -17.983 1.00 29.04 ? 58   LEU A C   1 
ATOM   417  O O   . LEU A 1 58  ? 46.596 97.826  -19.156 1.00 28.33 ? 58   LEU A O   1 
ATOM   418  C CB  . LEU A 1 58  ? 48.132 96.075  -16.889 1.00 28.39 ? 58   LEU A CB  1 
ATOM   419  C CG  . LEU A 1 58  ? 48.431 94.948  -15.889 1.00 30.97 ? 58   LEU A CG  1 
ATOM   420  C CD1 . LEU A 1 58  ? 48.221 93.563  -16.423 1.00 28.97 ? 58   LEU A CD1 1 
ATOM   421  C CD2 . LEU A 1 58  ? 49.872 95.108  -15.463 1.00 31.05 ? 58   LEU A CD2 1 
ATOM   422  N N   . VAL A 1 59  ? 45.750 98.263  -17.102 1.00 28.10 ? 59   VAL A N   1 
ATOM   423  C CA  . VAL A 1 59  ? 45.306 99.617  -17.421 1.00 28.02 ? 59   VAL A CA  1 
ATOM   424  C C   . VAL A 1 59  ? 46.107 100.597 -16.601 1.00 28.49 ? 59   VAL A C   1 
ATOM   425  O O   . VAL A 1 59  ? 46.132 100.490 -15.365 1.00 27.68 ? 59   VAL A O   1 
ATOM   426  C CB  . VAL A 1 59  ? 43.835 99.789  -17.051 1.00 28.57 ? 59   VAL A CB  1 
ATOM   427  C CG1 . VAL A 1 59  ? 43.347 101.213 -17.362 1.00 30.58 ? 59   VAL A CG1 1 
ATOM   428  C CG2 . VAL A 1 59  ? 43.011 98.753  -17.785 1.00 29.79 ? 59   VAL A CG2 1 
ATOM   429  N N   . ASN A 1 60  ? 46.788 101.544 -17.264 1.00 27.67 ? 60   ASN A N   1 
ATOM   430  C CA  . ASN A 1 60  ? 47.440 102.620 -16.556 1.00 28.21 ? 60   ASN A CA  1 
ATOM   431  C C   . ASN A 1 60  ? 46.442 103.530 -15.917 1.00 29.05 ? 60   ASN A C   1 
ATOM   432  O O   . ASN A 1 60  ? 45.414 103.878 -16.526 1.00 29.93 ? 60   ASN A O   1 
ATOM   433  C CB  . ASN A 1 60  ? 48.314 103.448 -17.481 1.00 29.25 ? 60   ASN A CB  1 
ATOM   434  C CG  . ASN A 1 60  ? 49.531 102.729 -17.863 1.00 32.19 ? 60   ASN A CG  1 
ATOM   435  O OD1 . ASN A 1 60  ? 50.507 102.685 -17.109 1.00 36.16 ? 60   ASN A OD1 1 
ATOM   436  N ND2 . ASN A 1 60  ? 49.489 102.094 -19.023 1.00 33.33 ? 60   ASN A ND2 1 
ATOM   437  N N   . THR A 1 61  ? 46.717 103.923 -14.683 1.00 27.70 ? 61   THR A N   1 
ATOM   438  C CA  . THR A 1 61  ? 45.850 104.861 -13.995 1.00 28.59 ? 61   THR A CA  1 
ATOM   439  C C   . THR A 1 61  ? 46.743 106.023 -13.600 1.00 29.24 ? 61   THR A C   1 
ATOM   440  O O   . THR A 1 61  ? 47.964 105.915 -13.759 1.00 29.65 ? 61   THR A O   1 
ATOM   441  C CB  . THR A 1 61  ? 45.165 104.191 -12.755 1.00 29.66 ? 61   THR A CB  1 
ATOM   442  O OG1 . THR A 1 61  ? 46.165 103.840 -11.790 1.00 28.36 ? 61   THR A OG1 1 
ATOM   443  C CG2 . THR A 1 61  ? 44.425 102.896 -13.165 1.00 27.89 ? 61   THR A CG2 1 
ATOM   444  N N   . ASN A 1 62  ? 46.168 107.116 -13.097 1.00 28.92 ? 62   ASN A N   1 
ATOM   445  C CA  . ASN A 1 62  ? 46.944 108.226 -12.543 1.00 30.40 ? 62   ASN A CA  1 
ATOM   446  C C   . ASN A 1 62  ? 47.914 107.749 -11.424 1.00 30.09 ? 62   ASN A C   1 
ATOM   447  O O   . ASN A 1 62  ? 49.053 108.235 -11.336 1.00 29.81 ? 62   ASN A O   1 
ATOM   448  C CB  . ASN A 1 62  ? 46.021 109.339 -11.974 1.00 31.31 ? 62   ASN A CB  1 
ATOM   449  C CG  . ASN A 1 62  ? 45.298 110.163 -13.062 1.00 37.18 ? 62   ASN A CG  1 
ATOM   450  O OD1 . ASN A 1 62  ? 44.156 110.619 -12.849 1.00 43.78 ? 62   ASN A OD1 1 
ATOM   451  N ND2 . ASN A 1 62  ? 45.962 110.392 -14.202 1.00 36.43 ? 62   ASN A ND2 1 
ATOM   452  N N   . ALA A 1 63  ? 47.458 106.788 -10.612 1.00 29.08 ? 63   ALA A N   1 
ATOM   453  C CA  . ALA A 1 63  ? 48.136 106.387 -9.366  1.00 28.57 ? 63   ALA A CA  1 
ATOM   454  C C   . ALA A 1 63  ? 49.114 105.257 -9.588  1.00 27.84 ? 63   ALA A C   1 
ATOM   455  O O   . ALA A 1 63  ? 50.027 105.034 -8.767  1.00 28.51 ? 63   ALA A O   1 
ATOM   456  C CB  . ALA A 1 63  ? 47.098 105.931 -8.369  1.00 28.95 ? 63   ALA A CB  1 
ATOM   457  N N   . GLY A 1 64  ? 48.877 104.501 -10.657 1.00 26.74 ? 64   GLY A N   1 
ATOM   458  C CA  . GLY A 1 64  ? 49.608 103.293 -10.956 1.00 26.32 ? 64   GLY A CA  1 
ATOM   459  C C   . GLY A 1 64  ? 48.963 102.498 -12.057 1.00 26.77 ? 64   GLY A C   1 
ATOM   460  O O   . GLY A 1 64  ? 49.022 102.867 -13.242 1.00 26.42 ? 64   GLY A O   1 
ATOM   461  N N   . PHE A 1 65  ? 48.306 101.413 -11.694 1.00 25.99 ? 65   PHE A N   1 
ATOM   462  C CA  . PHE A 1 65  ? 47.685 100.558 -12.706 1.00 26.07 ? 65   PHE A CA  1 
ATOM   463  C C   . PHE A 1 65  ? 46.633 99.658  -12.054 1.00 26.64 ? 65   PHE A C   1 
ATOM   464  O O   . PHE A 1 65  ? 46.643 99.432  -10.835 1.00 26.37 ? 65   PHE A O   1 
ATOM   465  C CB  . PHE A 1 65  ? 48.727 99.730  -13.529 1.00 25.60 ? 65   PHE A CB  1 
ATOM   466  C CG  . PHE A 1 65  ? 49.522 98.729  -12.697 1.00 27.65 ? 65   PHE A CG  1 
ATOM   467  C CD1 . PHE A 1 65  ? 49.014 97.437  -12.451 1.00 24.31 ? 65   PHE A CD1 1 
ATOM   468  C CD2 . PHE A 1 65  ? 50.732 99.104  -12.117 1.00 26.42 ? 65   PHE A CD2 1 
ATOM   469  C CE1 . PHE A 1 65  ? 49.701 96.549  -11.672 1.00 26.15 ? 65   PHE A CE1 1 
ATOM   470  C CE2 . PHE A 1 65  ? 51.450 98.209  -11.323 1.00 28.19 ? 65   PHE A CE2 1 
ATOM   471  C CZ  . PHE A 1 65  ? 50.936 96.937  -11.097 1.00 28.96 ? 65   PHE A CZ  1 
ATOM   472  N N   . THR A 1 66  ? 45.718 99.157  -12.861 1.00 26.95 ? 66   THR A N   1 
ATOM   473  C CA  . THR A 1 66  ? 44.815 98.105  -12.407 1.00 28.35 ? 66   THR A CA  1 
ATOM   474  C C   . THR A 1 66  ? 44.902 96.882  -13.306 1.00 29.07 ? 66   THR A C   1 
ATOM   475  O O   . THR A 1 66  ? 45.343 96.943  -14.478 1.00 28.25 ? 66   THR A O   1 
ATOM   476  C CB  . THR A 1 66  ? 43.373 98.607  -12.325 1.00 28.92 ? 66   THR A CB  1 
ATOM   477  O OG1 . THR A 1 66  ? 42.974 99.094  -13.608 1.00 31.07 ? 66   THR A OG1 1 
ATOM   478  C CG2 . THR A 1 66  ? 43.290 99.737  -11.348 1.00 30.69 ? 66   THR A CG2 1 
ATOM   479  N N   . ALA A 1 67  ? 44.498 95.741  -12.757 1.00 28.68 ? 67   ALA A N   1 
ATOM   480  C CA  . ALA A 1 67  ? 44.416 94.543  -13.539 1.00 29.07 ? 67   ALA A CA  1 
ATOM   481  C C   . ALA A 1 67  ? 43.175 93.775  -13.109 1.00 29.96 ? 67   ALA A C   1 
ATOM   482  O O   . ALA A 1 67  ? 42.785 93.806  -11.937 1.00 29.20 ? 67   ALA A O   1 
ATOM   483  C CB  . ALA A 1 67  ? 45.664 93.690  -13.345 1.00 28.53 ? 67   ALA A CB  1 
ATOM   484  N N   . ARG A 1 68  ? 42.580 93.069  -14.056 1.00 30.89 ? 68   ARG A N   1 
ATOM   485  C CA  . ARG A 1 68  ? 41.489 92.131  -13.755 1.00 32.56 ? 68   ARG A CA  1 
ATOM   486  C C   . ARG A 1 68  ? 42.067 90.747  -13.706 1.00 31.41 ? 68   ARG A C   1 
ATOM   487  O O   . ARG A 1 68  ? 42.751 90.354  -14.635 1.00 30.56 ? 68   ARG A O   1 
ATOM   488  C CB  . ARG A 1 68  ? 40.384 92.207  -14.819 1.00 32.47 ? 68   ARG A CB  1 
ATOM   489  C CG  . ARG A 1 68  ? 39.497 93.443  -14.632 1.00 39.39 ? 68   ARG A CG  1 
ATOM   490  C CD  . ARG A 1 68  ? 38.768 93.888  -15.924 1.00 48.63 ? 68   ARG A CD  1 
ATOM   491  N NE  . ARG A 1 68  ? 37.519 94.617  -15.658 1.00 54.26 ? 68   ARG A NE  1 
ATOM   492  C CZ  . ARG A 1 68  ? 36.780 95.249  -16.577 1.00 58.55 ? 68   ARG A CZ  1 
ATOM   493  N NH1 . ARG A 1 68  ? 37.155 95.289  -17.861 1.00 58.59 ? 68   ARG A NH1 1 
ATOM   494  N NH2 . ARG A 1 68  ? 35.657 95.869  -16.204 1.00 60.37 ? 68   ARG A NH2 1 
ATOM   495  N N   . LEU A 1 69  ? 41.776 90.010  -12.624 1.00 31.41 ? 69   LEU A N   1 
ATOM   496  C CA  . LEU A 1 69  ? 42.295 88.667  -12.440 1.00 32.90 ? 69   LEU A CA  1 
ATOM   497  C C   . LEU A 1 69  ? 41.143 87.690  -12.465 1.00 33.90 ? 69   LEU A C   1 
ATOM   498  O O   . LEU A 1 69  ? 40.105 87.940  -11.892 1.00 33.97 ? 69   LEU A O   1 
ATOM   499  C CB  . LEU A 1 69  ? 43.099 88.516  -11.135 1.00 32.14 ? 69   LEU A CB  1 
ATOM   500  C CG  . LEU A 1 69  ? 44.105 89.600  -10.743 1.00 33.12 ? 69   LEU A CG  1 
ATOM   501  C CD1 . LEU A 1 69  ? 44.789 89.165  -9.437  1.00 34.05 ? 69   LEU A CD1 1 
ATOM   502  C CD2 . LEU A 1 69  ? 45.160 89.816  -11.847 1.00 30.12 ? 69   LEU A CD2 1 
ATOM   503  N N   . LYS A 1 70  ? 41.329 86.580  -13.153 1.00 36.04 ? 70   LYS A N   1 
ATOM   504  C CA  . LYS A 1 70  ? 40.221 85.680  -13.377 1.00 39.22 ? 70   LYS A CA  1 
ATOM   505  C C   . LYS A 1 70  ? 40.643 84.334  -12.869 1.00 40.36 ? 70   LYS A C   1 
ATOM   506  O O   . LYS A 1 70  ? 41.730 83.860  -13.175 1.00 39.99 ? 70   LYS A O   1 
ATOM   507  C CB  . LYS A 1 70  ? 39.846 85.658  -14.872 1.00 39.70 ? 70   LYS A CB  1 
ATOM   508  C CG  . LYS A 1 70  ? 38.608 84.851  -15.232 1.00 44.50 ? 70   LYS A CG  1 
ATOM   509  C CD  . LYS A 1 70  ? 38.110 85.300  -16.627 1.00 51.30 ? 70   LYS A CD  1 
ATOM   510  C CE  . LYS A 1 70  ? 37.000 84.405  -17.186 1.00 54.70 ? 70   LYS A CE  1 
ATOM   511  N NZ  . LYS A 1 70  ? 36.706 84.737  -18.635 1.00 56.01 ? 70   LYS A NZ  1 
ATOM   512  N N   . ASN A 1 71  ? 39.789 83.733  -12.057 1.00 44.08 ? 71   ASN A N   1 
ATOM   513  C CA  . ASN A 1 71  ? 40.089 82.437  -11.481 1.00 48.28 ? 71   ASN A CA  1 
ATOM   514  C C   . ASN A 1 71  ? 39.886 81.331  -12.502 1.00 51.03 ? 71   ASN A C   1 
ATOM   515  O O   . ASN A 1 71  ? 38.883 81.299  -13.190 1.00 50.47 ? 71   ASN A O   1 
ATOM   516  C CB  . ASN A 1 71  ? 39.248 82.185  -10.219 1.00 48.26 ? 71   ASN A CB  1 
ATOM   517  C CG  . ASN A 1 71  ? 39.693 80.949  -9.448  1.00 49.98 ? 71   ASN A CG  1 
ATOM   518  O OD1 . ASN A 1 71  ? 40.876 80.539  -9.479  1.00 51.44 ? 71   ASN A OD1 1 
ATOM   519  N ND2 . ASN A 1 71  ? 38.737 80.333  -8.752  1.00 54.27 ? 71   ASN A ND2 1 
ATOM   520  N N   . LEU A 1 72  ? 40.886 80.462  -12.599 1.00 55.53 ? 72   LEU A N   1 
ATOM   521  C CA  . LEU A 1 72  ? 40.864 79.269  -13.431 1.00 59.64 ? 72   LEU A CA  1 
ATOM   522  C C   . LEU A 1 72  ? 40.081 78.230  -12.636 1.00 62.38 ? 72   LEU A C   1 
ATOM   523  O O   . LEU A 1 72  ? 40.578 77.758  -11.605 1.00 63.16 ? 72   LEU A O   1 
ATOM   524  C CB  . LEU A 1 72  ? 42.302 78.752  -13.659 1.00 59.95 ? 72   LEU A CB  1 
ATOM   525  C CG  . LEU A 1 72  ? 43.293 79.269  -14.726 1.00 60.95 ? 72   LEU A CG  1 
ATOM   526  C CD1 . LEU A 1 72  ? 42.634 79.425  -16.123 1.00 62.18 ? 72   LEU A CD1 1 
ATOM   527  C CD2 . LEU A 1 72  ? 44.045 80.528  -14.294 1.00 59.75 ? 72   LEU A CD2 1 
ATOM   528  N N   . PRO A 1 73  ? 38.878 77.842  -13.117 1.00 65.02 ? 73   PRO A N   1 
ATOM   529  C CA  . PRO A 1 73  ? 37.823 77.348  -12.205 1.00 66.71 ? 73   PRO A CA  1 
ATOM   530  C C   . PRO A 1 73  ? 38.220 76.187  -11.261 1.00 68.15 ? 73   PRO A C   1 
ATOM   531  O O   . PRO A 1 73  ? 39.184 75.447  -11.529 1.00 68.15 ? 73   PRO A O   1 
ATOM   532  C CB  . PRO A 1 73  ? 36.681 76.928  -13.159 1.00 67.30 ? 73   PRO A CB  1 
ATOM   533  C CG  . PRO A 1 73  ? 37.343 76.757  -14.520 1.00 66.88 ? 73   PRO A CG  1 
ATOM   534  C CD  . PRO A 1 73  ? 38.464 77.773  -14.536 1.00 65.33 ? 73   PRO A CD  1 
ATOM   535  N N   . SER A 1 74  ? 37.466 76.063  -10.164 1.00 69.45 ? 74   SER A N   1 
ATOM   536  C CA  . SER A 1 74  ? 37.669 75.058  -9.110  1.00 70.38 ? 74   SER A CA  1 
ATOM   537  C C   . SER A 1 74  ? 36.484 75.122  -8.157  1.00 71.08 ? 74   SER A C   1 
ATOM   538  O O   . SER A 1 74  ? 36.025 76.219  -7.788  1.00 71.68 ? 74   SER A O   1 
ATOM   539  C CB  . SER A 1 74  ? 38.960 75.311  -8.312  1.00 70.40 ? 74   SER A CB  1 
ATOM   540  O OG  . SER A 1 74  ? 40.044 74.524  -8.783  1.00 70.50 ? 74   SER A OG  1 
ATOM   541  N N   . SER A 1 75  ? 35.998 73.942  -7.768  1.00 71.63 ? 75   SER A N   1 
ATOM   542  C CA  . SER A 1 75  ? 34.965 73.779  -6.727  1.00 71.44 ? 75   SER A CA  1 
ATOM   543  C C   . SER A 1 75  ? 35.428 74.205  -5.295  1.00 71.42 ? 75   SER A C   1 
ATOM   544  O O   . SER A 1 75  ? 36.629 74.106  -4.964  1.00 71.41 ? 75   SER A O   1 
ATOM   545  C CB  . SER A 1 75  ? 34.410 72.337  -6.755  1.00 72.01 ? 75   SER A CB  1 
ATOM   546  O OG  . SER A 1 75  ? 35.113 71.498  -7.676  1.00 71.25 ? 75   SER A OG  1 
ATOM   547  N N   . PRO A 1 76  ? 34.473 74.681  -4.449  1.00 71.00 ? 76   PRO A N   1 
ATOM   548  C CA  . PRO A 1 76  ? 34.786 75.352  -3.161  1.00 70.53 ? 76   PRO A CA  1 
ATOM   549  C C   . PRO A 1 76  ? 35.427 74.472  -2.070  1.00 69.44 ? 76   PRO A C   1 
ATOM   550  O O   . PRO A 1 76  ? 34.952 73.363  -1.789  1.00 69.42 ? 76   PRO A O   1 
ATOM   551  C CB  . PRO A 1 76  ? 33.419 75.887  -2.683  1.00 70.72 ? 76   PRO A CB  1 
ATOM   552  C CG  . PRO A 1 76  ? 32.496 75.772  -3.878  1.00 71.11 ? 76   PRO A CG  1 
ATOM   553  C CD  . PRO A 1 76  ? 33.016 74.610  -4.672  1.00 71.08 ? 76   PRO A CD  1 
ATOM   554  N N   . VAL A 1 77  ? 36.506 74.991  -1.477  1.00 67.82 ? 77   VAL A N   1 
ATOM   555  C CA  . VAL A 1 77  ? 37.252 74.325  -0.409  1.00 65.62 ? 77   VAL A CA  1 
ATOM   556  C C   . VAL A 1 77  ? 36.908 75.024  0.899   1.00 64.18 ? 77   VAL A C   1 
ATOM   557  O O   . VAL A 1 77  ? 36.339 74.411  1.810   1.00 63.87 ? 77   VAL A O   1 
ATOM   558  C CB  . VAL A 1 77  ? 38.796 74.417  -0.627  1.00 65.68 ? 77   VAL A CB  1 
ATOM   559  C CG1 . VAL A 1 77  ? 39.531 73.723  0.508   1.00 65.17 ? 77   VAL A CG1 1 
ATOM   560  C CG2 . VAL A 1 77  ? 39.208 73.830  -1.975  1.00 65.98 ? 77   VAL A CG2 1 
ATOM   561  N N   . PHE A 1 78  ? 37.261 76.310  0.978   1.00 61.76 ? 78   PHE A N   1 
ATOM   562  C CA  . PHE A 1 78  ? 37.008 77.106  2.164   1.00 59.84 ? 78   PHE A CA  1 
ATOM   563  C C   . PHE A 1 78  ? 35.998 78.161  1.851   1.00 59.93 ? 78   PHE A C   1 
ATOM   564  O O   . PHE A 1 78  ? 36.226 79.354  2.070   1.00 59.87 ? 78   PHE A O   1 
ATOM   565  C CB  . PHE A 1 78  ? 38.284 77.739  2.676   1.00 58.41 ? 78   PHE A CB  1 
ATOM   566  C CG  . PHE A 1 78  ? 39.274 76.755  3.156   1.00 55.46 ? 78   PHE A CG  1 
ATOM   567  C CD1 . PHE A 1 78  ? 40.545 76.721  2.616   1.00 53.85 ? 78   PHE A CD1 1 
ATOM   568  C CD2 . PHE A 1 78  ? 38.928 75.829  4.134   1.00 52.88 ? 78   PHE A CD2 1 
ATOM   569  C CE1 . PHE A 1 78  ? 41.469 75.798  3.065   1.00 53.72 ? 78   PHE A CE1 1 
ATOM   570  C CE2 . PHE A 1 78  ? 39.838 74.912  4.581   1.00 52.18 ? 78   PHE A CE2 1 
ATOM   571  C CZ  . PHE A 1 78  ? 41.114 74.898  4.049   1.00 53.52 ? 78   PHE A CZ  1 
ATOM   572  N N   . GLY A 1 79  ? 34.871 77.700  1.330   1.00 59.86 ? 79   GLY A N   1 
ATOM   573  C CA  . GLY A 1 79  ? 33.744 78.565  1.040   1.00 59.82 ? 79   GLY A CA  1 
ATOM   574  C C   . GLY A 1 79  ? 33.776 79.163  -0.356  1.00 59.38 ? 79   GLY A C   1 
ATOM   575  O O   . GLY A 1 79  ? 34.603 78.784  -1.217  1.00 59.27 ? 79   GLY A O   1 
ATOM   576  N N   . SER A 1 80  ? 32.861 80.109  -0.558  1.00 58.77 ? 80   SER A N   1 
ATOM   577  C CA  . SER A 1 80  ? 32.602 80.697  -1.860  1.00 58.28 ? 80   SER A CA  1 
ATOM   578  C C   . SER A 1 80  ? 33.822 81.477  -2.377  1.00 56.89 ? 80   SER A C   1 
ATOM   579  O O   . SER A 1 80  ? 34.191 82.504  -1.811  1.00 56.44 ? 80   SER A O   1 
ATOM   580  C CB  . SER A 1 80  ? 31.356 81.590  -1.784  1.00 58.72 ? 80   SER A CB  1 
ATOM   581  O OG  . SER A 1 80  ? 30.654 81.586  -3.025  1.00 61.71 ? 80   SER A OG  1 
ATOM   582  N N   . ASN A 1 81  ? 34.437 80.942  -3.432  1.00 55.27 ? 81   ASN A N   1 
ATOM   583  C CA  . ASN A 1 81  ? 35.557 81.537  -4.126  1.00 54.01 ? 81   ASN A CA  1 
ATOM   584  C C   . ASN A 1 81  ? 35.163 82.811  -4.919  1.00 53.07 ? 81   ASN A C   1 
ATOM   585  O O   . ASN A 1 81  ? 33.979 83.022  -5.222  1.00 52.65 ? 81   ASN A O   1 
ATOM   586  C CB  . ASN A 1 81  ? 36.126 80.487  -5.063  1.00 54.76 ? 81   ASN A CB  1 
ATOM   587  C CG  . ASN A 1 81  ? 37.597 80.668  -5.327  1.00 57.03 ? 81   ASN A CG  1 
ATOM   588  O OD1 . ASN A 1 81  ? 38.052 81.739  -5.754  1.00 60.23 ? 81   ASN A OD1 1 
ATOM   589  N ND2 . ASN A 1 81  ? 38.360 79.602  -5.104  1.00 58.22 ? 81   ASN A ND2 1 
ATOM   590  N N   . VAL A 1 82  ? 36.143 83.667  -5.225  1.00 51.13 ? 82   VAL A N   1 
ATOM   591  C CA  . VAL A 1 82  ? 35.868 84.940  -5.897  1.00 49.60 ? 82   VAL A CA  1 
ATOM   592  C C   . VAL A 1 82  ? 36.459 84.841  -7.308  1.00 48.99 ? 82   VAL A C   1 
ATOM   593  O O   . VAL A 1 82  ? 37.667 84.860  -7.468  1.00 49.23 ? 82   VAL A O   1 
ATOM   594  C CB  . VAL A 1 82  ? 36.446 86.139  -5.090  1.00 50.26 ? 82   VAL A CB  1 
ATOM   595  C CG1 . VAL A 1 82  ? 36.396 87.456  -5.896  1.00 48.84 ? 82   VAL A CG1 1 
ATOM   596  C CG2 . VAL A 1 82  ? 35.733 86.286  -3.732  1.00 48.17 ? 82   VAL A CG2 1 
ATOM   597  N N   . ASP A 1 83  ? 35.610 84.700  -8.317  1.00 47.75 ? 83   ASP A N   1 
ATOM   598  C CA  . ASP A 1 83  ? 36.062 84.346  -9.672  1.00 47.08 ? 83   ASP A CA  1 
ATOM   599  C C   . ASP A 1 83  ? 36.790 85.506  -10.401 1.00 44.64 ? 83   ASP A C   1 
ATOM   600  O O   . ASP A 1 83  ? 37.685 85.273  -11.233 1.00 44.52 ? 83   ASP A O   1 
ATOM   601  C CB  . ASP A 1 83  ? 34.870 83.875  -10.532 1.00 48.48 ? 83   ASP A CB  1 
ATOM   602  C CG  . ASP A 1 83  ? 34.481 82.378  -10.309 1.00 53.14 ? 83   ASP A CG  1 
ATOM   603  O OD1 . ASP A 1 83  ? 34.621 81.838  -9.171  1.00 55.41 ? 83   ASP A OD1 1 
ATOM   604  O OD2 . ASP A 1 83  ? 34.005 81.755  -11.308 1.00 56.71 ? 83   ASP A OD2 1 
ATOM   605  N N   . ASN A 1 84  ? 36.373 86.730  -10.093 1.00 42.24 ? 84   ASN A N   1 
ATOM   606  C CA  . ASN A 1 84  ? 36.955 87.939  -10.636 1.00 40.50 ? 84   ASN A CA  1 
ATOM   607  C C   . ASN A 1 84  ? 37.461 88.896  -9.582  1.00 38.36 ? 84   ASN A C   1 
ATOM   608  O O   . ASN A 1 84  ? 36.703 89.496  -8.836  1.00 37.58 ? 84   ASN A O   1 
ATOM   609  C CB  . ASN A 1 84  ? 35.988 88.625  -11.589 1.00 41.44 ? 84   ASN A CB  1 
ATOM   610  C CG  . ASN A 1 84  ? 35.822 87.832  -12.867 1.00 44.04 ? 84   ASN A CG  1 
ATOM   611  O OD1 . ASN A 1 84  ? 34.925 86.985  -12.966 1.00 47.16 ? 84   ASN A OD1 1 
ATOM   612  N ND2 . ASN A 1 84  ? 36.762 88.008  -13.804 1.00 44.98 ? 84   ASN A ND2 1 
ATOM   613  N N   . VAL A 1 85  ? 38.778 89.018  -9.547  1.00 36.55 ? 85   VAL A N   1 
ATOM   614  C CA  . VAL A 1 85  ? 39.483 89.834  -8.573  1.00 34.55 ? 85   VAL A CA  1 
ATOM   615  C C   . VAL A 1 85  ? 40.008 91.091  -9.287  1.00 33.94 ? 85   VAL A C   1 
ATOM   616  O O   . VAL A 1 85  ? 40.458 91.015  -10.425 1.00 34.14 ? 85   VAL A O   1 
ATOM   617  C CB  . VAL A 1 85  ? 40.639 88.989  -7.939  1.00 34.70 ? 85   VAL A CB  1 
ATOM   618  C CG1 . VAL A 1 85  ? 41.624 89.854  -7.141  1.00 33.72 ? 85   VAL A CG1 1 
ATOM   619  C CG2 . VAL A 1 85  ? 40.057 87.881  -7.063  1.00 33.88 ? 85   VAL A CG2 1 
ATOM   620  N N   . LEU A 1 86  ? 39.952 92.226  -8.622  1.00 32.66 ? 86   LEU A N   1 
ATOM   621  C CA  . LEU A 1 86  ? 40.567 93.430  -9.126  1.00 32.26 ? 86   LEU A CA  1 
ATOM   622  C C   . LEU A 1 86  ? 41.887 93.723  -8.376  1.00 32.10 ? 86   LEU A C   1 
ATOM   623  O O   . LEU A 1 86  ? 41.917 93.759  -7.140  1.00 32.02 ? 86   LEU A O   1 
ATOM   624  C CB  . LEU A 1 86  ? 39.602 94.617  -9.021  1.00 31.96 ? 86   LEU A CB  1 
ATOM   625  C CG  . LEU A 1 86  ? 40.144 95.995  -9.468  1.00 33.26 ? 86   LEU A CG  1 
ATOM   626  C CD1 . LEU A 1 86  ? 39.982 96.160  -10.937 1.00 33.15 ? 86   LEU A CD1 1 
ATOM   627  C CD2 . LEU A 1 86  ? 39.418 97.093  -8.769  1.00 33.30 ? 86   LEU A CD2 1 
ATOM   628  N N   . LEU A 1 87  ? 42.977 93.927  -9.127  1.00 30.82 ? 87   LEU A N   1 
ATOM   629  C CA  . LEU A 1 87  ? 44.224 94.405  -8.535  1.00 29.82 ? 87   LEU A CA  1 
ATOM   630  C C   . LEU A 1 87  ? 44.349 95.891  -8.809  1.00 30.28 ? 87   LEU A C   1 
ATOM   631  O O   . LEU A 1 87  ? 44.203 96.353  -9.965  1.00 29.40 ? 87   LEU A O   1 
ATOM   632  C CB  . LEU A 1 87  ? 45.440 93.640  -9.078  1.00 30.23 ? 87   LEU A CB  1 
ATOM   633  C CG  . LEU A 1 87  ? 46.819 94.291  -8.762  1.00 31.31 ? 87   LEU A CG  1 
ATOM   634  C CD1 . LEU A 1 87  ? 47.252 94.111  -7.315  1.00 28.25 ? 87   LEU A CD1 1 
ATOM   635  C CD2 . LEU A 1 87  ? 47.831 93.695  -9.685  1.00 33.41 ? 87   LEU A CD2 1 
ATOM   636  N N   . THR A 1 88  ? 44.541 96.662  -7.741  1.00 29.07 ? 88   THR A N   1 
ATOM   637  C CA  . THR A 1 88  ? 44.727 98.077  -7.874  1.00 28.52 ? 88   THR A CA  1 
ATOM   638  C C   . THR A 1 88  ? 46.074 98.378  -7.257  1.00 28.37 ? 88   THR A C   1 
ATOM   639  O O   . THR A 1 88  ? 46.274 98.045  -6.099  1.00 25.90 ? 88   THR A O   1 
ATOM   640  C CB  . THR A 1 88  ? 43.687 98.833  -7.038  1.00 29.23 ? 88   THR A CB  1 
ATOM   641  O OG1 . THR A 1 88  ? 42.363 98.498  -7.492  1.00 31.01 ? 88   THR A OG1 1 
ATOM   642  C CG2 . THR A 1 88  ? 43.908 100.328 -7.156  1.00 29.57 ? 88   THR A CG2 1 
ATOM   643  N N   . ALA A 1 89  ? 46.959 99.032  -8.010  1.00 26.26 ? 89   ALA A N   1 
ATOM   644  C CA  . ALA A 1 89  ? 48.321 99.322  -7.557  1.00 26.21 ? 89   ALA A CA  1 
ATOM   645  C C   . ALA A 1 89  ? 48.552 100.819 -7.614  1.00 26.85 ? 89   ALA A C   1 
ATOM   646  O O   . ALA A 1 89  ? 48.138 101.486 -8.574  1.00 25.35 ? 89   ALA A O   1 
ATOM   647  C CB  . ALA A 1 89  ? 49.345 98.570  -8.400  1.00 25.94 ? 89   ALA A CB  1 
ATOM   648  N N   . GLU A 1 90  ? 49.158 101.346 -6.540  1.00 26.29 ? 90   GLU A N   1 
ATOM   649  C CA  . GLU A 1 90  ? 49.395 102.768 -6.364  1.00 26.53 ? 90   GLU A CA  1 
ATOM   650  C C   . GLU A 1 90  ? 50.859 102.970 -5.990  1.00 25.76 ? 90   GLU A C   1 
ATOM   651  O O   . GLU A 1 90  ? 51.327 102.463 -4.979  1.00 23.55 ? 90   GLU A O   1 
ATOM   652  C CB  . GLU A 1 90  ? 48.504 103.371 -5.267  1.00 26.11 ? 90   GLU A CB  1 
ATOM   653  C CG  . GLU A 1 90  ? 46.996 103.247 -5.570  1.00 28.22 ? 90   GLU A CG  1 
ATOM   654  C CD  . GLU A 1 90  ? 46.108 103.631 -4.407  1.00 30.18 ? 90   GLU A CD  1 
ATOM   655  O OE1 . GLU A 1 90  ? 46.580 103.686 -3.237  1.00 29.16 ? 90   GLU A OE1 1 
ATOM   656  O OE2 . GLU A 1 90  ? 44.900 103.896 -4.660  1.00 36.99 ? 90   GLU A OE2 1 
ATOM   657  N N   . TYR A 1 91  ? 51.552 103.745 -6.816  1.00 25.45 ? 91   TYR A N   1 
ATOM   658  C CA  . TYR A 1 91  ? 52.910 104.185 -6.562  1.00 25.91 ? 91   TYR A CA  1 
ATOM   659  C C   . TYR A 1 91  ? 52.820 105.384 -5.650  1.00 24.51 ? 91   TYR A C   1 
ATOM   660  O O   . TYR A 1 91  ? 52.941 106.511 -6.086  1.00 25.57 ? 91   TYR A O   1 
ATOM   661  C CB  . TYR A 1 91  ? 53.581 104.548 -7.900  1.00 26.68 ? 91   TYR A CB  1 
ATOM   662  C CG  . TYR A 1 91  ? 53.736 103.376 -8.852  1.00 29.15 ? 91   TYR A CG  1 
ATOM   663  C CD1 . TYR A 1 91  ? 54.590 102.322 -8.547  1.00 32.67 ? 91   TYR A CD1 1 
ATOM   664  C CD2 . TYR A 1 91  ? 53.101 103.349 -10.081 1.00 33.83 ? 91   TYR A CD2 1 
ATOM   665  C CE1 . TYR A 1 91  ? 54.783 101.254 -9.421  1.00 32.24 ? 91   TYR A CE1 1 
ATOM   666  C CE2 . TYR A 1 91  ? 53.285 102.265 -10.968 1.00 32.99 ? 91   TYR A CE2 1 
ATOM   667  C CZ  . TYR A 1 91  ? 54.124 101.221 -10.616 1.00 31.40 ? 91   TYR A CZ  1 
ATOM   668  O OH  . TYR A 1 91  ? 54.367 100.157 -11.469 1.00 31.94 ? 91   TYR A OH  1 
ATOM   669  N N   . GLN A 1 92  ? 52.594 105.158 -4.362  1.00 23.21 ? 92   GLN A N   1 
ATOM   670  C CA  . GLN A 1 92  ? 52.204 106.240 -3.480  1.00 22.11 ? 92   GLN A CA  1 
ATOM   671  C C   . GLN A 1 92  ? 53.348 107.236 -3.206  1.00 22.32 ? 92   GLN A C   1 
ATOM   672  O O   . GLN A 1 92  ? 53.144 108.460 -3.153  1.00 22.11 ? 92   GLN A O   1 
ATOM   673  C CB  . GLN A 1 92  ? 51.635 105.684 -2.170  1.00 21.71 ? 92   GLN A CB  1 
ATOM   674  C CG  . GLN A 1 92  ? 50.305 104.924 -2.378  1.00 24.01 ? 92   GLN A CG  1 
ATOM   675  C CD  . GLN A 1 92  ? 49.590 104.660 -1.073  1.00 25.14 ? 92   GLN A CD  1 
ATOM   676  O OE1 . GLN A 1 92  ? 50.163 104.811 -0.011  1.00 24.95 ? 92   GLN A OE1 1 
ATOM   677  N NE2 . GLN A 1 92  ? 48.333 104.281 -1.153  1.00 25.64 ? 92   GLN A NE2 1 
ATOM   678  N N   . THR A 1 93  ? 54.527 106.714 -2.965  1.00 22.27 ? 93   THR A N   1 
ATOM   679  C CA  . THR A 1 93  ? 55.689 107.574 -2.726  1.00 22.86 ? 93   THR A CA  1 
ATOM   680  C C   . THR A 1 93  ? 56.866 106.876 -3.354  1.00 22.72 ? 93   THR A C   1 
ATOM   681  O O   . THR A 1 93  ? 56.735 105.722 -3.777  1.00 22.16 ? 93   THR A O   1 
ATOM   682  C CB  . THR A 1 93  ? 55.986 107.852 -1.223  1.00 23.17 ? 93   THR A CB  1 
ATOM   683  O OG1 . THR A 1 93  ? 56.531 106.692 -0.631  1.00 22.09 ? 93   THR A OG1 1 
ATOM   684  C CG2 . THR A 1 93  ? 54.778 108.338 -0.422  1.00 25.11 ? 93   THR A CG2 1 
ATOM   685  N N   . SER A 1 94  ? 58.026 107.539 -3.402  1.00 23.04 ? 94   SER A N   1 
ATOM   686  C CA  . SER A 1 94  ? 59.256 106.900 -3.911  1.00 23.43 ? 94   SER A CA  1 
ATOM   687  C C   . SER A 1 94  ? 59.657 105.628 -3.205  1.00 22.57 ? 94   SER A C   1 
ATOM   688  O O   . SER A 1 94  ? 60.424 104.803 -3.756  1.00 22.71 ? 94   SER A O   1 
ATOM   689  C CB  . SER A 1 94  ? 60.457 107.875 -3.766  1.00 25.22 ? 94   SER A CB  1 
ATOM   690  O OG  . SER A 1 94  ? 60.237 109.023 -4.561  1.00 29.52 ? 94   SER A OG  1 
ATOM   691  N N   . ASN A 1 95  ? 59.228 105.493 -1.945  1.00 22.23 ? 95   ASN A N   1 
ATOM   692  C CA  . ASN A 1 95  ? 59.655 104.355 -1.161  1.00 22.29 ? 95   ASN A CA  1 
ATOM   693  C C   . ASN A 1 95  ? 58.487 103.535 -0.633  1.00 21.05 ? 95   ASN A C   1 
ATOM   694  O O   . ASN A 1 95  ? 58.685 102.665 0.203   1.00 21.51 ? 95   ASN A O   1 
ATOM   695  C CB  . ASN A 1 95  ? 60.492 104.820 0.029   1.00 22.13 ? 95   ASN A CB  1 
ATOM   696  C CG  . ASN A 1 95  ? 61.783 105.550 -0.411  1.00 29.09 ? 95   ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 95  ? 62.846 104.940 -0.574  1.00 35.32 ? 95   ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 95  ? 61.657 106.830 -0.650  1.00 30.59 ? 95   ASN A ND2 1 
ATOM   699  N N   . ARG A 1 96  ? 57.281 103.861 -1.048  1.00 20.84 ? 96   ARG A N   1 
ATOM   700  C CA  . ARG A 1 96  ? 56.118 103.094 -0.584  1.00 20.61 ? 96   ARG A CA  1 
ATOM   701  C C   . ARG A 1 96  ? 55.226 102.739 -1.733  1.00 20.61 ? 96   ARG A C   1 
ATOM   702  O O   . ARG A 1 96  ? 54.773 103.622 -2.482  1.00 21.14 ? 96   ARG A O   1 
ATOM   703  C CB  . ARG A 1 96  ? 55.304 103.904 0.430   1.00 20.90 ? 96   ARG A CB  1 
ATOM   704  C CG  . ARG A 1 96  ? 54.058 103.124 0.954   1.00 18.54 ? 96   ARG A CG  1 
ATOM   705  C CD  . ARG A 1 96  ? 53.441 103.896 2.106   1.00 19.15 ? 96   ARG A CD  1 
ATOM   706  N NE  . ARG A 1 96  ? 52.607 104.983 1.623   1.00 21.82 ? 96   ARG A NE  1 
ATOM   707  C CZ  . ARG A 1 96  ? 52.684 106.246 2.000   1.00 21.95 ? 96   ARG A CZ  1 
ATOM   708  N NH1 . ARG A 1 96  ? 53.585 106.665 2.851   1.00 22.94 ? 96   ARG A NH1 1 
ATOM   709  N NH2 . ARG A 1 96  ? 51.832 107.117 1.487   1.00 21.08 ? 96   ARG A NH2 1 
ATOM   710  N N   . PHE A 1 97  ? 54.939 101.456 -1.830  1.00 20.16 ? 97   PHE A N   1 
ATOM   711  C CA  . PHE A 1 97  ? 54.095 100.893 -2.866  1.00 21.62 ? 97   PHE A CA  1 
ATOM   712  C C   . PHE A 1 97  ? 52.881 100.305 -2.147  1.00 21.99 ? 97   PHE A C   1 
ATOM   713  O O   . PHE A 1 97  ? 53.003 99.701  -1.076  1.00 21.80 ? 97   PHE A O   1 
ATOM   714  C CB  . PHE A 1 97  ? 54.801 99.751  -3.590  1.00 20.50 ? 97   PHE A CB  1 
ATOM   715  C CG  . PHE A 1 97  ? 53.952 99.080  -4.677  1.00 24.27 ? 97   PHE A CG  1 
ATOM   716  C CD1 . PHE A 1 97  ? 53.359 99.838  -5.696  1.00 24.72 ? 97   PHE A CD1 1 
ATOM   717  C CD2 . PHE A 1 97  ? 53.776 97.699  -4.689  1.00 23.91 ? 97   PHE A CD2 1 
ATOM   718  C CE1 . PHE A 1 97  ? 52.553 99.241  -6.684  1.00 20.10 ? 97   PHE A CE1 1 
ATOM   719  C CE2 . PHE A 1 97  ? 53.036 97.090  -5.720  1.00 23.17 ? 97   PHE A CE2 1 
ATOM   720  C CZ  . PHE A 1 97  ? 52.438 97.859  -6.700  1.00 22.71 ? 97   PHE A CZ  1 
ATOM   721  N N   . HIS A 1 98  ? 51.734 100.445 -2.758  1.00 22.29 ? 98   HIS A N   1 
ATOM   722  C CA  . HIS A 1 98  ? 50.489 99.920  -2.195  1.00 22.21 ? 98   HIS A CA  1 
ATOM   723  C C   . HIS A 1 98  ? 49.826 99.125  -3.293  1.00 22.63 ? 98   HIS A C   1 
ATOM   724  O O   . HIS A 1 98  ? 49.794 99.571  -4.470  1.00 21.94 ? 98   HIS A O   1 
ATOM   725  C CB  . HIS A 1 98  ? 49.647 101.102 -1.766  1.00 22.72 ? 98   HIS A CB  1 
ATOM   726  C CG  . HIS A 1 98  ? 48.245 100.774 -1.367  1.00 26.09 ? 98   HIS A CG  1 
ATOM   727  N ND1 . HIS A 1 98  ? 47.929 99.776  -0.468  1.00 26.45 ? 98   HIS A ND1 1 
ATOM   728  C CD2 . HIS A 1 98  ? 47.078 101.377 -1.683  1.00 29.59 ? 98   HIS A CD2 1 
ATOM   729  C CE1 . HIS A 1 98  ? 46.628 99.782  -0.252  1.00 30.02 ? 98   HIS A CE1 1 
ATOM   730  N NE2 . HIS A 1 98  ? 46.087 100.740 -0.981  1.00 33.91 ? 98   HIS A NE2 1 
ATOM   731  N N   . PHE A 1 99  ? 49.370 97.918  -2.950  1.00 21.30 ? 99   PHE A N   1 
ATOM   732  C CA  . PHE A 1 99  ? 48.492 97.191  -3.855  1.00 23.51 ? 99   PHE A CA  1 
ATOM   733  C C   . PHE A 1 99  ? 47.419 96.465  -3.064  1.00 25.02 ? 99   PHE A C   1 
ATOM   734  O O   . PHE A 1 99  ? 47.640 96.003  -1.932  1.00 24.41 ? 99   PHE A O   1 
ATOM   735  C CB  . PHE A 1 99  ? 49.235 96.221  -4.809  1.00 21.98 ? 99   PHE A CB  1 
ATOM   736  C CG  . PHE A 1 99  ? 49.799 95.007  -4.145  1.00 25.76 ? 99   PHE A CG  1 
ATOM   737  C CD1 . PHE A 1 99  ? 49.080 93.789  -4.137  1.00 27.21 ? 99   PHE A CD1 1 
ATOM   738  C CD2 . PHE A 1 99  ? 51.045 95.059  -3.537  1.00 25.21 ? 99   PHE A CD2 1 
ATOM   739  C CE1 . PHE A 1 99  ? 49.604 92.678  -3.517  1.00 26.77 ? 99   PHE A CE1 1 
ATOM   740  C CE2 . PHE A 1 99  ? 51.602 93.929  -2.933  1.00 26.73 ? 99   PHE A CE2 1 
ATOM   741  C CZ  . PHE A 1 99  ? 50.874 92.738  -2.927  1.00 25.33 ? 99   PHE A CZ  1 
ATOM   742  N N   . LYS A 1 100 ? 46.239 96.413  -3.648  1.00 24.96 ? 100  LYS A N   1 
ATOM   743  C CA  . LYS A 1 100 ? 45.166 95.668  -3.029  1.00 27.14 ? 100  LYS A CA  1 
ATOM   744  C C   . LYS A 1 100 ? 44.466 94.788  -4.020  1.00 27.57 ? 100  LYS A C   1 
ATOM   745  O O   . LYS A 1 100 ? 44.403 95.093  -5.220  1.00 27.18 ? 100  LYS A O   1 
ATOM   746  C CB  . LYS A 1 100 ? 44.163 96.545  -2.261  1.00 26.79 ? 100  LYS A CB  1 
ATOM   747  C CG  . LYS A 1 100 ? 43.692 97.765  -2.907  1.00 30.76 ? 100  LYS A CG  1 
ATOM   748  C CD  . LYS A 1 100 ? 42.540 98.322  -2.075  1.00 37.70 ? 100  LYS A CD  1 
ATOM   749  C CE  . LYS A 1 100 ? 42.937 99.309  -0.989  1.00 41.14 ? 100  LYS A CE  1 
ATOM   750  N NZ  . LYS A 1 100 ? 41.686 99.907  -0.347  1.00 45.41 ? 100  LYS A NZ  1 
ATOM   751  N N   . LEU A 1 101 ? 43.997 93.663  -3.495  1.00 27.64 ? 101  LEU A N   1 
ATOM   752  C CA  . LEU A 1 101 ? 43.274 92.681  -4.252  1.00 28.13 ? 101  LEU A CA  1 
ATOM   753  C C   . LEU A 1 101 ? 41.887 92.704  -3.634  1.00 30.07 ? 101  LEU A C   1 
ATOM   754  O O   . LEU A 1 101 ? 41.750 92.501  -2.425  1.00 29.68 ? 101  LEU A O   1 
ATOM   755  C CB  . LEU A 1 101 ? 43.953 91.327  -4.096  1.00 28.46 ? 101  LEU A CB  1 
ATOM   756  C CG  . LEU A 1 101 ? 45.316 91.266  -4.817  1.00 29.22 ? 101  LEU A CG  1 
ATOM   757  C CD1 . LEU A 1 101 ? 46.344 90.351  -4.167  1.00 30.91 ? 101  LEU A CD1 1 
ATOM   758  C CD2 . LEU A 1 101 ? 45.104 90.923  -6.311  1.00 25.10 ? 101  LEU A CD2 1 
ATOM   759  N N   . THR A 1 102 ? 40.887 93.048  -4.450  1.00 31.06 ? 102  THR A N   1 
ATOM   760  C CA  . THR A 1 102 ? 39.486 93.152  -4.020  1.00 32.45 ? 102  THR A CA  1 
ATOM   761  C C   . THR A 1 102 ? 38.628 92.262  -4.907  1.00 33.42 ? 102  THR A C   1 
ATOM   762  O O   . THR A 1 102 ? 39.107 91.717  -5.906  1.00 32.27 ? 102  THR A O   1 
ATOM   763  C CB  . THR A 1 102 ? 38.958 94.610  -4.146  1.00 33.04 ? 102  THR A CB  1 
ATOM   764  O OG1 . THR A 1 102 ? 39.306 95.117  -5.439  1.00 32.77 ? 102  THR A OG1 1 
ATOM   765  C CG2 . THR A 1 102 ? 39.594 95.536  -3.110  1.00 32.49 ? 102  THR A CG2 1 
ATOM   766  N N   . ASP A 1 103 ? 37.352 92.124  -4.545  1.00 34.64 ? 103  ASP A N   1 
ATOM   767  C CA  . ASP A 1 103 ? 36.385 91.424  -5.386  1.00 36.99 ? 103  ASP A CA  1 
ATOM   768  C C   . ASP A 1 103 ? 35.887 92.443  -6.420  1.00 37.42 ? 103  ASP A C   1 
ATOM   769  O O   . ASP A 1 103 ? 35.349 93.493  -6.067  1.00 37.62 ? 103  ASP A O   1 
ATOM   770  C CB  . ASP A 1 103 ? 35.219 90.878  -4.516  1.00 36.74 ? 103  ASP A CB  1 
ATOM   771  C CG  . ASP A 1 103 ? 34.199 90.013  -5.313  1.00 41.30 ? 103  ASP A CG  1 
ATOM   772  O OD1 . ASP A 1 103 ? 34.143 90.088  -6.570  1.00 42.89 ? 103  ASP A OD1 1 
ATOM   773  O OD2 . ASP A 1 103 ? 33.403 89.273  -4.662  1.00 43.13 ? 103  ASP A OD2 1 
ATOM   774  N N   . GLN A 1 104 ? 36.066 92.139  -7.694  1.00 39.33 ? 104  GLN A N   1 
ATOM   775  C CA  . GLN A 1 104 ? 35.603 93.035  -8.760  1.00 42.37 ? 104  GLN A CA  1 
ATOM   776  C C   . GLN A 1 104 ? 34.149 93.450  -8.649  1.00 43.25 ? 104  GLN A C   1 
ATOM   777  O O   . GLN A 1 104 ? 33.808 94.610  -8.925  1.00 44.83 ? 104  GLN A O   1 
ATOM   778  C CB  . GLN A 1 104 ? 35.767 92.360  -10.103 1.00 42.95 ? 104  GLN A CB  1 
ATOM   779  C CG  . GLN A 1 104 ? 36.998 92.754  -10.791 1.00 45.55 ? 104  GLN A CG  1 
ATOM   780  C CD  . GLN A 1 104 ? 36.771 92.828  -12.260 1.00 49.86 ? 104  GLN A CD  1 
ATOM   781  O OE1 . GLN A 1 104 ? 36.620 91.794  -12.937 1.00 49.67 ? 104  GLN A OE1 1 
ATOM   782  N NE2 . GLN A 1 104 ? 36.729 94.060  -12.779 1.00 50.71 ? 104  GLN A NE2 1 
ATOM   783  N N   . THR A 1 105 ? 33.317 92.496  -8.232  1.00 43.93 ? 105  THR A N   1 
ATOM   784  C CA  . THR A 1 105 ? 31.860 92.594  -8.263  1.00 45.00 ? 105  THR A CA  1 
ATOM   785  C C   . THR A 1 105 ? 31.192 93.010  -6.948  1.00 44.68 ? 105  THR A C   1 
ATOM   786  O O   . THR A 1 105 ? 30.066 93.526  -6.947  1.00 45.50 ? 105  THR A O   1 
ATOM   787  C CB  . THR A 1 105 ? 31.243 91.258  -8.786  1.00 45.73 ? 105  THR A CB  1 
ATOM   788  O OG1 . THR A 1 105 ? 31.448 90.191  -7.831  1.00 48.46 ? 105  THR A OG1 1 
ATOM   789  C CG2 . THR A 1 105 ? 31.890 90.863  -10.118 1.00 45.78 ? 105  THR A CG2 1 
ATOM   790  N N   . ASN A 1 106 ? 31.894 92.814  -5.834  1.00 43.90 ? 106  ASN A N   1 
ATOM   791  C CA  . ASN A 1 106 ? 31.361 93.092  -4.515  1.00 42.82 ? 106  ASN A CA  1 
ATOM   792  C C   . ASN A 1 106 ? 32.344 93.860  -3.665  1.00 40.98 ? 106  ASN A C   1 
ATOM   793  O O   . ASN A 1 106 ? 33.538 93.562  -3.670  1.00 40.73 ? 106  ASN A O   1 
ATOM   794  C CB  . ASN A 1 106 ? 31.020 91.785  -3.779  1.00 43.33 ? 106  ASN A CB  1 
ATOM   795  C CG  . ASN A 1 106 ? 30.009 90.946  -4.522  1.00 47.02 ? 106  ASN A CG  1 
ATOM   796  O OD1 . ASN A 1 106 ? 30.350 89.873  -5.044  1.00 50.31 ? 106  ASN A OD1 1 
ATOM   797  N ND2 . ASN A 1 106 ? 28.754 91.430  -4.593  1.00 48.32 ? 106  ASN A ND2 1 
ATOM   798  N N   . ASN A 1 107 ? 31.834 94.831  -2.927  1.00 39.55 ? 107  ASN A N   1 
ATOM   799  C CA  . ASN A 1 107 ? 32.588 95.470  -1.877  1.00 39.33 ? 107  ASN A CA  1 
ATOM   800  C C   . ASN A 1 107 ? 32.735 94.497  -0.715  1.00 37.55 ? 107  ASN A C   1 
ATOM   801  O O   . ASN A 1 107 ? 31.842 93.681  -0.462  1.00 37.49 ? 107  ASN A O   1 
ATOM   802  C CB  . ASN A 1 107 ? 31.899 96.748  -1.395  1.00 40.55 ? 107  ASN A CB  1 
ATOM   803  C CG  . ASN A 1 107 ? 31.816 97.819  -2.481  1.00 44.49 ? 107  ASN A CG  1 
ATOM   804  O OD1 . ASN A 1 107 ? 30.812 98.532  -2.569  1.00 49.20 ? 107  ASN A OD1 1 
ATOM   805  N ND2 . ASN A 1 107 ? 32.852 97.922  -3.318  1.00 45.15 ? 107  ASN A ND2 1 
ATOM   806  N N   . ARG A 1 108 ? 33.875 94.579  -0.035  1.00 35.26 ? 108  ARG A N   1 
ATOM   807  C CA  . ARG A 1 108 ? 34.175 93.696  1.065   1.00 32.46 ? 108  ARG A CA  1 
ATOM   808  C C   . ARG A 1 108 ? 34.655 94.573  2.193   1.00 31.32 ? 108  ARG A C   1 
ATOM   809  O O   . ARG A 1 108 ? 34.948 95.749  1.991   1.00 30.95 ? 108  ARG A O   1 
ATOM   810  C CB  . ARG A 1 108 ? 35.224 92.655  0.678   1.00 32.37 ? 108  ARG A CB  1 
ATOM   811  C CG  . ARG A 1 108 ? 34.773 91.654  -0.369  1.00 29.74 ? 108  ARG A CG  1 
ATOM   812  C CD  . ARG A 1 108 ? 35.921 90.734  -0.767  1.00 29.20 ? 108  ARG A CD  1 
ATOM   813  N NE  . ARG A 1 108 ? 36.496 90.063  0.411   1.00 29.58 ? 108  ARG A NE  1 
ATOM   814  C CZ  . ARG A 1 108 ? 35.952 88.995  0.980   1.00 32.74 ? 108  ARG A CZ  1 
ATOM   815  N NH1 . ARG A 1 108 ? 34.863 88.462  0.431   1.00 29.93 ? 108  ARG A NH1 1 
ATOM   816  N NH2 . ARG A 1 108 ? 36.495 88.444  2.077   1.00 28.19 ? 108  ARG A NH2 1 
ATOM   817  N N   . PHE A 1 109 ? 34.713 94.007  3.383   1.00 28.99 ? 109  PHE A N   1 
ATOM   818  C CA  . PHE A 1 109 ? 35.206 94.739  4.516   1.00 28.65 ? 109  PHE A CA  1 
ATOM   819  C C   . PHE A 1 109 ? 36.639 95.244  4.280   1.00 28.13 ? 109  PHE A C   1 
ATOM   820  O O   . PHE A 1 109 ? 37.510 94.502  3.817   1.00 28.13 ? 109  PHE A O   1 
ATOM   821  C CB  . PHE A 1 109 ? 35.172 93.881  5.792   1.00 27.52 ? 109  PHE A CB  1 
ATOM   822  C CG  . PHE A 1 109 ? 35.622 94.638  7.007   1.00 27.90 ? 109  PHE A CG  1 
ATOM   823  C CD1 . PHE A 1 109 ? 34.769 95.526  7.646   1.00 29.23 ? 109  PHE A CD1 1 
ATOM   824  C CD2 . PHE A 1 109 ? 36.914 94.489  7.484   1.00 28.72 ? 109  PHE A CD2 1 
ATOM   825  C CE1 . PHE A 1 109 ? 35.205 96.252  8.743   1.00 29.02 ? 109  PHE A CE1 1 
ATOM   826  C CE2 . PHE A 1 109 ? 37.351 95.205  8.583   1.00 25.78 ? 109  PHE A CE2 1 
ATOM   827  C CZ  . PHE A 1 109 ? 36.521 96.083  9.202   1.00 27.99 ? 109  PHE A CZ  1 
ATOM   828  N N   . GLU A 1 110 ? 36.856 96.494  4.653   1.00 28.73 ? 110  GLU A N   1 
ATOM   829  C CA  . GLU A 1 110 ? 38.157 97.132  4.632   1.00 28.68 ? 110  GLU A CA  1 
ATOM   830  C C   . GLU A 1 110 ? 38.341 97.861  5.933   1.00 28.31 ? 110  GLU A C   1 
ATOM   831  O O   . GLU A 1 110 ? 37.416 98.542  6.416   1.00 26.88 ? 110  GLU A O   1 
ATOM   832  C CB  . GLU A 1 110 ? 38.241 98.124  3.465   1.00 29.32 ? 110  GLU A CB  1 
ATOM   833  C CG  . GLU A 1 110 ? 37.745 97.526  2.187   1.00 32.99 ? 110  GLU A CG  1 
ATOM   834  C CD  . GLU A 1 110 ? 38.214 98.262  0.951   1.00 42.32 ? 110  GLU A CD  1 
ATOM   835  O OE1 . GLU A 1 110 ? 39.039 99.201  1.074   1.00 47.09 ? 110  GLU A OE1 1 
ATOM   836  O OE2 . GLU A 1 110 ? 37.770 97.882  -0.157  1.00 43.29 ? 110  GLU A OE2 1 
ATOM   837  N N   . VAL A 1 111 ? 39.541 97.748  6.497   1.00 27.03 ? 111  VAL A N   1 
ATOM   838  C CA  . VAL A 1 111 ? 39.817 98.334  7.803   1.00 25.94 ? 111  VAL A CA  1 
ATOM   839  C C   . VAL A 1 111 ? 39.570 99.843  7.805   1.00 27.61 ? 111  VAL A C   1 
ATOM   840  O O   . VAL A 1 111 ? 40.198 100.559 7.014   1.00 27.44 ? 111  VAL A O   1 
ATOM   841  C CB  . VAL A 1 111 ? 41.236 97.984  8.277   1.00 25.39 ? 111  VAL A CB  1 
ATOM   842  C CG1 . VAL A 1 111 ? 41.548 98.617  9.632   1.00 22.47 ? 111  VAL A CG1 1 
ATOM   843  C CG2 . VAL A 1 111 ? 41.406 96.456  8.321   1.00 24.05 ? 111  VAL A CG2 1 
ATOM   844  N N   . PRO A 1 112 ? 38.676 100.337 8.712   1.00 28.63 ? 112  PRO A N   1 
ATOM   845  C CA  . PRO A 1 112 ? 38.460 101.784 8.795   1.00 29.30 ? 112  PRO A CA  1 
ATOM   846  C C   . PRO A 1 112 ? 39.503 102.468 9.694   1.00 29.56 ? 112  PRO A C   1 
ATOM   847  O O   . PRO A 1 112 ? 39.180 103.051 10.738  1.00 29.72 ? 112  PRO A O   1 
ATOM   848  C CB  . PRO A 1 112 ? 37.033 101.904 9.337   1.00 30.19 ? 112  PRO A CB  1 
ATOM   849  C CG  . PRO A 1 112 ? 36.910 100.684 10.223  1.00 29.86 ? 112  PRO A CG  1 
ATOM   850  C CD  . PRO A 1 112 ? 37.813 99.604  9.664   1.00 28.56 ? 112  PRO A CD  1 
ATOM   851  N N   . HIS A 1 113 ? 40.757 102.437 9.234   1.00 28.11 ? 113  HIS A N   1 
ATOM   852  C CA  . HIS A 1 113 ? 41.873 102.985 9.984   1.00 27.52 ? 113  HIS A CA  1 
ATOM   853  C C   . HIS A 1 113 ? 41.737 104.485 10.226  1.00 27.93 ? 113  HIS A C   1 
ATOM   854  O O   . HIS A 1 113 ? 41.343 105.219 9.341   1.00 29.50 ? 113  HIS A O   1 
ATOM   855  C CB  . HIS A 1 113 ? 43.210 102.619 9.294   1.00 25.39 ? 113  HIS A CB  1 
ATOM   856  C CG  . HIS A 1 113 ? 44.381 102.609 10.231  1.00 26.00 ? 113  HIS A CG  1 
ATOM   857  N ND1 . HIS A 1 113 ? 45.201 103.711 10.410  1.00 20.69 ? 113  HIS A ND1 1 
ATOM   858  C CD2 . HIS A 1 113 ? 44.852 101.644 11.067  1.00 22.37 ? 113  HIS A CD2 1 
ATOM   859  C CE1 . HIS A 1 113 ? 46.147 103.413 11.282  1.00 24.77 ? 113  HIS A CE1 1 
ATOM   860  N NE2 . HIS A 1 113 ? 45.948 102.177 11.714  1.00 24.41 ? 113  HIS A NE2 1 
ATOM   861  N N   . GLU A 1 114 ? 42.087 104.933 11.429  1.00 27.84 ? 114  GLU A N   1 
ATOM   862  C CA  . GLU A 1 114 ? 41.913 106.318 11.833  1.00 28.09 ? 114  GLU A CA  1 
ATOM   863  C C   . GLU A 1 114 ? 42.974 107.200 11.189  1.00 28.74 ? 114  GLU A C   1 
ATOM   864  O O   . GLU A 1 114 ? 42.748 108.389 10.992  1.00 29.21 ? 114  GLU A O   1 
ATOM   865  C CB  . GLU A 1 114 ? 41.933 106.431 13.354  1.00 28.41 ? 114  GLU A CB  1 
ATOM   866  C CG  . GLU A 1 114 ? 41.711 107.836 13.939  1.00 34.33 ? 114  GLU A CG  1 
ATOM   867  C CD  . GLU A 1 114 ? 42.980 108.736 13.964  1.00 41.01 ? 114  GLU A CD  1 
ATOM   868  O OE1 . GLU A 1 114 ? 44.138 108.264 13.793  1.00 37.25 ? 114  GLU A OE1 1 
ATOM   869  O OE2 . GLU A 1 114 ? 42.802 109.966 14.140  1.00 45.87 ? 114  GLU A OE2 1 
ATOM   870  N N   . HIS A 1 115 ? 44.122 106.622 10.835  1.00 26.25 ? 115  HIS A N   1 
ATOM   871  C CA  . HIS A 1 115 ? 45.190 107.446 10.318  1.00 26.17 ? 115  HIS A CA  1 
ATOM   872  C C   . HIS A 1 115 ? 45.456 107.312 8.820   1.00 27.08 ? 115  HIS A C   1 
ATOM   873  O O   . HIS A 1 115 ? 45.593 108.341 8.121   1.00 27.15 ? 115  HIS A O   1 
ATOM   874  C CB  . HIS A 1 115 ? 46.469 107.205 11.089  1.00 25.40 ? 115  HIS A CB  1 
ATOM   875  C CG  . HIS A 1 115 ? 47.566 108.135 10.710  1.00 24.59 ? 115  HIS A CG  1 
ATOM   876  N ND1 . HIS A 1 115 ? 47.709 109.371 11.288  1.00 27.66 ? 115  HIS A ND1 1 
ATOM   877  C CD2 . HIS A 1 115 ? 48.592 108.002 9.834   1.00 23.00 ? 115  HIS A CD2 1 
ATOM   878  C CE1 . HIS A 1 115 ? 48.784 109.969 10.786  1.00 27.60 ? 115  HIS A CE1 1 
ATOM   879  N NE2 . HIS A 1 115 ? 49.328 109.162 9.892   1.00 23.15 ? 115  HIS A NE2 1 
ATOM   880  N N   . VAL A 1 116 ? 45.536 106.077 8.325   1.00 26.08 ? 116  VAL A N   1 
ATOM   881  C CA  . VAL A 1 116 ? 45.725 105.851 6.902   1.00 27.15 ? 116  VAL A CA  1 
ATOM   882  C C   . VAL A 1 116 ? 44.526 106.440 6.161   1.00 28.88 ? 116  VAL A C   1 
ATOM   883  O O   . VAL A 1 116 ? 43.396 106.253 6.582   1.00 28.22 ? 116  VAL A O   1 
ATOM   884  C CB  . VAL A 1 116 ? 45.869 104.375 6.608   1.00 26.70 ? 116  VAL A CB  1 
ATOM   885  C CG1 . VAL A 1 116 ? 45.920 104.101 5.108   1.00 27.44 ? 116  VAL A CG1 1 
ATOM   886  C CG2 . VAL A 1 116 ? 47.085 103.828 7.342   1.00 26.34 ? 116  VAL A CG2 1 
ATOM   887  N N   . GLN A 1 117 ? 44.799 107.198 5.101   1.00 29.49 ? 117  GLN A N   1 
ATOM   888  C CA  . GLN A 1 117 ? 43.757 107.705 4.183   1.00 31.28 ? 117  GLN A CA  1 
ATOM   889  C C   . GLN A 1 117 ? 43.882 107.092 2.808   1.00 31.03 ? 117  GLN A C   1 
ATOM   890  O O   . GLN A 1 117 ? 44.912 106.516 2.485   1.00 30.72 ? 117  GLN A O   1 
ATOM   891  C CB  . GLN A 1 117 ? 43.893 109.204 4.026   1.00 31.49 ? 117  GLN A CB  1 
ATOM   892  C CG  . GLN A 1 117 ? 43.649 109.943 5.289   1.00 37.77 ? 117  GLN A CG  1 
ATOM   893  C CD  . GLN A 1 117 ? 43.847 111.424 5.093   1.00 46.91 ? 117  GLN A CD  1 
ATOM   894  O OE1 . GLN A 1 117 ? 44.955 111.891 4.776   1.00 47.65 ? 117  GLN A OE1 1 
ATOM   895  N NE2 . GLN A 1 117 ? 42.769 112.184 5.266   1.00 48.88 ? 117  GLN A NE2 1 
ATOM   896  N N   . SER A 1 118 ? 42.846 107.216 1.976   1.00 32.78 ? 118  SER A N   1 
ATOM   897  C CA  . SER A 1 118 ? 42.928 106.699 0.604   1.00 33.68 ? 118  SER A CA  1 
ATOM   898  C C   . SER A 1 118 ? 43.856 107.644 -0.166  1.00 34.21 ? 118  SER A C   1 
ATOM   899  O O   . SER A 1 118 ? 44.069 108.784 0.245   1.00 34.48 ? 118  SER A O   1 
ATOM   900  C CB  . SER A 1 118 ? 41.551 106.670 -0.060  1.00 34.73 ? 118  SER A CB  1 
ATOM   901  O OG  . SER A 1 118 ? 41.051 108.002 -0.088  1.00 36.73 ? 118  SER A OG  1 
ATOM   902  N N   . PHE A 1 119 ? 44.425 107.147 -1.255  1.00 34.55 ? 119  PHE A N   1 
ATOM   903  C CA  . PHE A 1 119 ? 45.313 107.896 -2.073  1.00 35.78 ? 119  PHE A CA  1 
ATOM   904  C C   . PHE A 1 119 ? 44.523 108.591 -3.180  1.00 37.98 ? 119  PHE A C   1 
ATOM   905  O O   . PHE A 1 119 ? 43.658 107.979 -3.823  1.00 37.17 ? 119  PHE A O   1 
ATOM   906  C CB  . PHE A 1 119 ? 46.297 106.924 -2.695  1.00 35.06 ? 119  PHE A CB  1 
ATOM   907  C CG  . PHE A 1 119 ? 47.397 107.563 -3.519  1.00 34.08 ? 119  PHE A CG  1 
ATOM   908  C CD1 . PHE A 1 119 ? 48.424 108.272 -2.912  1.00 34.21 ? 119  PHE A CD1 1 
ATOM   909  C CD2 . PHE A 1 119 ? 47.435 107.385 -4.887  1.00 33.35 ? 119  PHE A CD2 1 
ATOM   910  C CE1 . PHE A 1 119 ? 49.446 108.837 -3.661  1.00 34.38 ? 119  PHE A CE1 1 
ATOM   911  C CE2 . PHE A 1 119 ? 48.447 107.949 -5.646  1.00 36.78 ? 119  PHE A CE2 1 
ATOM   912  C CZ  . PHE A 1 119 ? 49.472 108.677 -5.022  1.00 35.24 ? 119  PHE A CZ  1 
ATOM   913  N N   . SER A 1 120 ? 44.844 109.859 -3.414  1.00 39.82 ? 120  SER A N   1 
ATOM   914  C CA  . SER A 1 120 ? 44.358 110.575 -4.606  1.00 41.96 ? 120  SER A CA  1 
ATOM   915  C C   . SER A 1 120 ? 45.529 111.201 -5.394  1.00 42.35 ? 120  SER A C   1 
ATOM   916  O O   . SER A 1 120 ? 46.637 111.371 -4.876  1.00 43.29 ? 120  SER A O   1 
ATOM   917  C CB  . SER A 1 120 ? 43.273 111.606 -4.229  1.00 42.38 ? 120  SER A CB  1 
ATOM   918  O OG  . SER A 1 120 ? 43.626 112.359 -3.070  1.00 45.45 ? 120  SER A OG  1 
ATOM   919  N N   . GLY A 1 121 ? 45.301 111.533 -6.655  1.00 42.98 ? 121  GLY A N   1 
ATOM   920  C CA  . GLY A 1 121 ? 46.396 112.054 -7.478  1.00 42.16 ? 121  GLY A CA  1 
ATOM   921  C C   . GLY A 1 121 ? 47.339 110.968 -8.032  1.00 41.83 ? 121  GLY A C   1 
ATOM   922  O O   . GLY A 1 121 ? 46.956 109.809 -8.225  1.00 41.11 ? 121  GLY A O   1 
ATOM   923  N N   . ASN A 1 122 ? 48.584 111.363 -8.265  1.00 40.92 ? 122  ASN A N   1 
ATOM   924  C CA  . ASN A 1 122 ? 49.399 110.751 -9.281  1.00 39.87 ? 122  ASN A CA  1 
ATOM   925  C C   . ASN A 1 122 ? 50.551 110.017 -8.714  1.00 38.16 ? 122  ASN A C   1 
ATOM   926  O O   . ASN A 1 122 ? 51.051 110.388 -7.663  1.00 38.76 ? 122  ASN A O   1 
ATOM   927  C CB  . ASN A 1 122 ? 49.939 111.847 -10.212 1.00 41.31 ? 122  ASN A CB  1 
ATOM   928  C CG  . ASN A 1 122 ? 48.828 112.619 -10.921 1.00 44.13 ? 122  ASN A CG  1 
ATOM   929  O OD1 . ASN A 1 122 ? 47.864 112.035 -11.410 1.00 46.51 ? 122  ASN A OD1 1 
ATOM   930  N ND2 . ASN A 1 122 ? 48.965 113.934 -10.970 1.00 46.37 ? 122  ASN A ND2 1 
ATOM   931  N N   . ALA A 1 123 ? 51.008 109.021 -9.458  1.00 35.90 ? 123  ALA A N   1 
ATOM   932  C CA  . ALA A 1 123 ? 52.100 108.155 -9.080  1.00 34.80 ? 123  ALA A CA  1 
ATOM   933  C C   . ALA A 1 123 ? 53.345 108.983 -8.808  1.00 35.69 ? 123  ALA A C   1 
ATOM   934  O O   . ALA A 1 123 ? 53.651 109.926 -9.565  1.00 34.53 ? 123  ALA A O   1 
ATOM   935  C CB  . ALA A 1 123 ? 52.357 107.188 -10.186 1.00 33.43 ? 123  ALA A CB  1 
ATOM   936  N N   . ALA A 1 124 ? 54.062 108.635 -7.740  1.00 34.08 ? 124  ALA A N   1 
ATOM   937  C CA  . ALA A 1 124 ? 55.215 109.398 -7.312  1.00 34.44 ? 124  ALA A CA  1 
ATOM   938  C C   . ALA A 1 124 ? 56.295 109.327 -8.386  1.00 34.61 ? 124  ALA A C   1 
ATOM   939  O O   . ALA A 1 124 ? 56.366 108.341 -9.142  1.00 34.44 ? 124  ALA A O   1 
ATOM   940  C CB  . ALA A 1 124 ? 55.745 108.851 -6.012  1.00 34.00 ? 124  ALA A CB  1 
ATOM   941  N N   . ALA A 1 125 ? 57.119 110.370 -8.465  1.00 34.51 ? 125  ALA A N   1 
ATOM   942  C CA  . ALA A 1 125 ? 58.271 110.347 -9.368  1.00 34.78 ? 125  ALA A CA  1 
ATOM   943  C C   . ALA A 1 125 ? 59.449 109.689 -8.636  1.00 35.01 ? 125  ALA A C   1 
ATOM   944  O O   . ALA A 1 125 ? 59.386 109.476 -7.413  1.00 35.55 ? 125  ALA A O   1 
ATOM   945  C CB  . ALA A 1 125 ? 58.619 111.758 -9.777  1.00 35.75 ? 125  ALA A CB  1 
ATOM   946  N N   . SER A 1 126 ? 60.506 109.344 -9.374  1.00 34.44 ? 126  SER A N   1 
ATOM   947  C CA  . SER A 1 126 ? 61.758 108.843 -8.779  1.00 33.67 ? 126  SER A CA  1 
ATOM   948  C C   . SER A 1 126 ? 61.552 107.620 -7.864  1.00 31.94 ? 126  SER A C   1 
ATOM   949  O O   . SER A 1 126 ? 62.001 107.615 -6.731  1.00 32.34 ? 126  SER A O   1 
ATOM   950  C CB  . SER A 1 126 ? 62.456 109.941 -7.978  1.00 34.55 ? 126  SER A CB  1 
ATOM   951  O OG  . SER A 1 126 ? 62.693 111.071 -8.778  1.00 38.14 ? 126  SER A OG  1 
ATOM   952  N N   . LEU A 1 127 ? 60.929 106.571 -8.380  1.00 29.67 ? 127  LEU A N   1 
ATOM   953  C CA  . LEU A 1 127 ? 60.705 105.392 -7.566  1.00 28.29 ? 127  LEU A CA  1 
ATOM   954  C C   . LEU A 1 127 ? 61.994 104.665 -7.267  1.00 27.53 ? 127  LEU A C   1 
ATOM   955  O O   . LEU A 1 127 ? 62.851 104.530 -8.144  1.00 26.46 ? 127  LEU A O   1 
ATOM   956  C CB  . LEU A 1 127 ? 59.715 104.456 -8.243  1.00 28.59 ? 127  LEU A CB  1 
ATOM   957  C CG  . LEU A 1 127 ? 58.369 105.124 -8.527  1.00 27.43 ? 127  LEU A CG  1 
ATOM   958  C CD1 . LEU A 1 127 ? 57.507 104.150 -9.262  1.00 31.07 ? 127  LEU A CD1 1 
ATOM   959  C CD2 . LEU A 1 127 ? 57.689 105.619 -7.234  1.00 28.99 ? 127  LEU A CD2 1 
ATOM   960  N N   . THR A 1 128 ? 62.115 104.156 -6.046  1.00 24.75 ? 128  THR A N   1 
ATOM   961  C CA  . THR A 1 128 ? 63.252 103.317 -5.685  1.00 24.32 ? 128  THR A CA  1 
ATOM   962  C C   . THR A 1 128 ? 62.995 101.838 -6.005  1.00 23.78 ? 128  THR A C   1 
ATOM   963  O O   . THR A 1 128 ? 63.877 101.004 -5.856  1.00 23.56 ? 128  THR A O   1 
ATOM   964  C CB  . THR A 1 128 ? 63.611 103.498 -4.187  1.00 24.30 ? 128  THR A CB  1 
ATOM   965  O OG1 . THR A 1 128 ? 62.524 103.017 -3.413  1.00 28.90 ? 128  THR A OG1 1 
ATOM   966  C CG2 . THR A 1 128 ? 63.748 104.975 -3.864  1.00 22.88 ? 128  THR A CG2 1 
ATOM   967  N N   . TYR A 1 129 ? 61.784 101.525 -6.451  1.00 22.86 ? 129  TYR A N   1 
ATOM   968  C CA  . TYR A 1 129 ? 61.365 100.142 -6.670  1.00 23.50 ? 129  TYR A CA  1 
ATOM   969  C C   . TYR A 1 129 ? 60.734 100.049 -8.066  1.00 24.46 ? 129  TYR A C   1 
ATOM   970  O O   . TYR A 1 129 ? 60.305 101.049 -8.635  1.00 25.49 ? 129  TYR A O   1 
ATOM   971  C CB  . TYR A 1 129 ? 60.361 99.651  -5.592  1.00 22.95 ? 129  TYR A CB  1 
ATOM   972  C CG  . TYR A 1 129 ? 59.142 100.524 -5.501  1.00 21.76 ? 129  TYR A CG  1 
ATOM   973  C CD1 . TYR A 1 129 ? 57.994 100.266 -6.281  1.00 22.37 ? 129  TYR A CD1 1 
ATOM   974  C CD2 . TYR A 1 129 ? 59.131 101.638 -4.684  1.00 22.56 ? 129  TYR A CD2 1 
ATOM   975  C CE1 . TYR A 1 129 ? 56.879 101.117 -6.232  1.00 21.97 ? 129  TYR A CE1 1 
ATOM   976  C CE2 . TYR A 1 129 ? 57.989 102.484 -4.619  1.00 21.22 ? 129  TYR A CE2 1 
ATOM   977  C CZ  . TYR A 1 129 ? 56.883 102.205 -5.397  1.00 21.83 ? 129  TYR A CZ  1 
ATOM   978  O OH  . TYR A 1 129 ? 55.778 103.044 -5.306  1.00 23.82 ? 129  TYR A OH  1 
ATOM   979  N N   . GLN A 1 130 ? 60.669 98.842  -8.593  1.00 25.60 ? 130  GLN A N   1 
ATOM   980  C CA  . GLN A 1 130 ? 59.988 98.598  -9.841  1.00 28.38 ? 130  GLN A CA  1 
ATOM   981  C C   . GLN A 1 130 ? 59.047 97.404  -9.614  1.00 26.63 ? 130  GLN A C   1 
ATOM   982  O O   . GLN A 1 130 ? 59.365 96.488  -8.863  1.00 26.53 ? 130  GLN A O   1 
ATOM   983  C CB  . GLN A 1 130 ? 61.000 98.191  -10.915 1.00 27.24 ? 130  GLN A CB  1 
ATOM   984  C CG  . GLN A 1 130 ? 60.308 97.694  -12.196 1.00 34.58 ? 130  GLN A CG  1 
ATOM   985  C CD  . GLN A 1 130 ? 61.205 96.900  -13.166 1.00 36.65 ? 130  GLN A CD  1 
ATOM   986  O OE1 . GLN A 1 130 ? 60.904 96.832  -14.380 1.00 46.40 ? 130  GLN A OE1 1 
ATOM   987  N NE2 . GLN A 1 130 ? 62.294 96.278  -12.639 1.00 45.30 ? 130  GLN A NE2 1 
ATOM   988  N N   . VAL A 1 131 ? 57.915 97.408  -10.290 1.00 25.76 ? 131  VAL A N   1 
ATOM   989  C CA  . VAL A 1 131 ? 56.887 96.383  -10.044 1.00 25.62 ? 131  VAL A CA  1 
ATOM   990  C C   . VAL A 1 131 ? 56.710 95.616  -11.349 1.00 28.01 ? 131  VAL A C   1 
ATOM   991  O O   . VAL A 1 131 ? 56.637 96.234  -12.437 1.00 27.97 ? 131  VAL A O   1 
ATOM   992  C CB  . VAL A 1 131 ? 55.567 97.009  -9.568  1.00 25.03 ? 131  VAL A CB  1 
ATOM   993  C CG1 . VAL A 1 131 ? 54.417 95.898  -9.460  1.00 25.04 ? 131  VAL A CG1 1 
ATOM   994  C CG2 . VAL A 1 131 ? 55.730 97.742  -8.226  1.00 22.89 ? 131  VAL A CG2 1 
ATOM   995  N N   A GLU A 1 132 ? 56.627 94.288  -11.250 0.50 28.34 ? 132  GLU A N   1 
ATOM   996  N N   B GLU A 1 132 ? 56.711 94.283  -11.275 0.50 27.87 ? 132  GLU A N   1 
ATOM   997  C CA  A GLU A 1 132 ? 56.427 93.449  -12.422 0.50 29.58 ? 132  GLU A CA  1 
ATOM   998  C CA  B GLU A 1 132 ? 56.368 93.466  -12.437 0.50 28.30 ? 132  GLU A CA  1 
ATOM   999  C C   A GLU A 1 132 ? 55.267 92.471  -12.188 0.50 28.74 ? 132  GLU A C   1 
ATOM   1000 C C   B GLU A 1 132 ? 55.166 92.601  -12.113 0.50 28.14 ? 132  GLU A C   1 
ATOM   1001 O O   A GLU A 1 132 ? 55.254 91.760  -11.191 0.50 27.37 ? 132  GLU A O   1 
ATOM   1002 O O   B GLU A 1 132 ? 55.042 92.081  -11.013 0.50 26.52 ? 132  GLU A O   1 
ATOM   1003 C CB  A GLU A 1 132 ? 57.715 92.697  -12.753 0.50 29.59 ? 132  GLU A CB  1 
ATOM   1004 C CB  B GLU A 1 132 ? 57.527 92.580  -12.893 0.50 28.76 ? 132  GLU A CB  1 
ATOM   1005 C CG  A GLU A 1 132 ? 57.936 92.517  -14.269 0.50 32.65 ? 132  GLU A CG  1 
ATOM   1006 C CG  B GLU A 1 132 ? 57.116 91.402  -13.861 0.50 31.11 ? 132  GLU A CG  1 
ATOM   1007 C CD  A GLU A 1 132 ? 58.918 91.385  -14.627 0.50 33.07 ? 132  GLU A CD  1 
ATOM   1008 C CD  B GLU A 1 132 ? 57.017 91.782  -15.357 0.50 32.99 ? 132  GLU A CD  1 
ATOM   1009 O OE1 A GLU A 1 132 ? 60.113 91.478  -14.250 0.50 39.53 ? 132  GLU A OE1 1 
ATOM   1010 O OE1 B GLU A 1 132 ? 56.179 92.636  -15.750 0.50 34.84 ? 132  GLU A OE1 1 
ATOM   1011 O OE2 A GLU A 1 132 ? 58.489 90.407  -15.292 0.50 37.42 ? 132  GLU A OE2 1 
ATOM   1012 O OE2 B GLU A 1 132 ? 57.768 91.189  -16.154 0.50 35.58 ? 132  GLU A OE2 1 
ATOM   1013 N N   . ILE A 1 133 ? 54.286 92.473  -13.100 1.00 28.86 ? 133  ILE A N   1 
ATOM   1014 C CA  . ILE A 1 133 ? 53.148 91.558  -13.062 1.00 28.76 ? 133  ILE A CA  1 
ATOM   1015 C C   . ILE A 1 133 ? 53.371 90.459  -14.099 1.00 30.45 ? 133  ILE A C   1 
ATOM   1016 O O   . ILE A 1 133 ? 53.803 90.726  -15.256 1.00 29.12 ? 133  ILE A O   1 
ATOM   1017 C CB  . ILE A 1 133 ? 51.816 92.299  -13.366 1.00 28.95 ? 133  ILE A CB  1 
ATOM   1018 C CG1 . ILE A 1 133 ? 51.636 93.490  -12.425 1.00 28.44 ? 133  ILE A CG1 1 
ATOM   1019 C CG2 . ILE A 1 133 ? 50.571 91.376  -13.265 1.00 29.94 ? 133  ILE A CG2 1 
ATOM   1020 C CD1 . ILE A 1 133 ? 51.377 93.088  -11.014 1.00 26.21 ? 133  ILE A CD1 1 
ATOM   1021 N N   . SER A 1 134 ? 53.121 89.225  -13.665 1.00 30.07 ? 134  SER A N   1 
ATOM   1022 C CA  A SER A 1 134 ? 53.080 88.096  -14.557 0.50 31.53 ? 134  SER A CA  1 
ATOM   1023 C CA  B SER A 1 134 ? 53.063 88.094  -14.569 0.50 31.77 ? 134  SER A CA  1 
ATOM   1024 C C   . SER A 1 134 ? 51.615 87.687  -14.673 1.00 32.87 ? 134  SER A C   1 
ATOM   1025 O O   . SER A 1 134 ? 50.847 87.831  -13.717 1.00 31.94 ? 134  SER A O   1 
ATOM   1026 C CB  A SER A 1 134 ? 53.951 86.973  -14.017 0.50 31.66 ? 134  SER A CB  1 
ATOM   1027 C CB  B SER A 1 134 ? 53.877 86.918  -14.072 0.50 31.88 ? 134  SER A CB  1 
ATOM   1028 O OG  A SER A 1 134 ? 55.317 87.395  -13.944 0.50 31.42 ? 134  SER A OG  1 
ATOM   1029 O OG  B SER A 1 134 ? 54.155 86.039  -15.154 0.50 33.21 ? 134  SER A OG  1 
ATOM   1030 N N   . ARG A 1 135 ? 51.215 87.204  -15.840 1.00 34.37 ? 135  ARG A N   1 
ATOM   1031 C CA  . ARG A 1 135 ? 49.815 86.963  -16.023 1.00 36.11 ? 135  ARG A CA  1 
ATOM   1032 C C   . ARG A 1 135 ? 49.381 85.519  -16.022 1.00 36.27 ? 135  ARG A C   1 
ATOM   1033 O O   . ARG A 1 135 ? 48.217 85.254  -15.747 1.00 35.87 ? 135  ARG A O   1 
ATOM   1034 C CB  . ARG A 1 135 ? 49.334 87.556  -17.337 1.00 39.15 ? 135  ARG A CB  1 
ATOM   1035 C CG  . ARG A 1 135 ? 49.993 88.851  -17.881 1.00 43.04 ? 135  ARG A CG  1 
ATOM   1036 C CD  . ARG A 1 135 ? 49.925 88.689  -19.394 1.00 48.96 ? 135  ARG A CD  1 
ATOM   1037 N NE  . ARG A 1 135 ? 48.547 88.531  -19.864 1.00 51.25 ? 135  ARG A NE  1 
ATOM   1038 C CZ  . ARG A 1 135 ? 47.741 89.542  -20.210 1.00 53.72 ? 135  ARG A CZ  1 
ATOM   1039 N NH1 . ARG A 1 135 ? 48.155 90.835  -20.131 1.00 50.49 ? 135  ARG A NH1 1 
ATOM   1040 N NH2 . ARG A 1 135 ? 46.503 89.251  -20.628 1.00 53.43 ? 135  ARG A NH2 1 
ATOM   1041 N N   . GLN A 1 136 ? 50.264 84.593  -16.382 1.00 36.34 ? 136  GLN A N   1 
ATOM   1042 C CA  . GLN A 1 136 ? 49.844 83.197  -16.562 1.00 37.73 ? 136  GLN A CA  1 
ATOM   1043 C C   . GLN A 1 136 ? 50.780 82.260  -15.824 1.00 37.04 ? 136  GLN A C   1 
ATOM   1044 O O   . GLN A 1 136 ? 51.758 81.795  -16.399 1.00 38.35 ? 136  GLN A O   1 
ATOM   1045 C CB  . GLN A 1 136 ? 49.814 82.814  -18.058 1.00 38.15 ? 136  GLN A CB  1 
ATOM   1046 C CG  . GLN A 1 136 ? 49.252 83.892  -19.030 1.00 42.78 ? 136  GLN A CG  1 
ATOM   1047 C CD  . GLN A 1 136 ? 47.757 84.216  -18.838 1.00 48.28 ? 136  GLN A CD  1 
ATOM   1048 O OE1 . GLN A 1 136 ? 46.918 83.309  -18.742 1.00 50.68 ? 136  GLN A OE1 1 
ATOM   1049 N NE2 . GLN A 1 136 ? 47.421 85.517  -18.807 1.00 48.70 ? 136  GLN A NE2 1 
ATOM   1050 N N   . PRO A 1 137 ? 50.518 81.998  -14.535 1.00 35.53 ? 137  PRO A N   1 
ATOM   1051 C CA  . PRO A 1 137 ? 49.488 82.547  -13.667 1.00 34.44 ? 137  PRO A CA  1 
ATOM   1052 C C   . PRO A 1 137 ? 49.882 83.892  -13.039 1.00 33.10 ? 137  PRO A C   1 
ATOM   1053 O O   . PRO A 1 137 ? 51.004 84.313  -13.162 1.00 32.98 ? 137  PRO A O   1 
ATOM   1054 C CB  . PRO A 1 137 ? 49.358 81.485  -12.580 1.00 33.88 ? 137  PRO A CB  1 
ATOM   1055 C CG  . PRO A 1 137 ? 50.712 80.878  -12.491 1.00 36.32 ? 137  PRO A CG  1 
ATOM   1056 C CD  . PRO A 1 137 ? 51.369 81.022  -13.837 1.00 35.62 ? 137  PRO A CD  1 
ATOM   1057 N N   . PHE A 1 138 ? 48.946 84.541  -12.369 1.00 31.84 ? 138  PHE A N   1 
ATOM   1058 C CA  . PHE A 1 138 ? 49.194 85.830  -11.799 1.00 30.53 ? 138  PHE A CA  1 
ATOM   1059 C C   . PHE A 1 138 ? 50.318 85.737  -10.773 1.00 30.97 ? 138  PHE A C   1 
ATOM   1060 O O   . PHE A 1 138 ? 50.317 84.860  -9.894  1.00 30.54 ? 138  PHE A O   1 
ATOM   1061 C CB  . PHE A 1 138 ? 47.936 86.352  -11.132 1.00 30.21 ? 138  PHE A CB  1 
ATOM   1062 C CG  . PHE A 1 138 ? 48.183 87.502  -10.236 1.00 30.43 ? 138  PHE A CG  1 
ATOM   1063 C CD1 . PHE A 1 138 ? 48.251 87.322  -8.859  1.00 29.53 ? 138  PHE A CD1 1 
ATOM   1064 C CD2 . PHE A 1 138 ? 48.403 88.773  -10.767 1.00 29.88 ? 138  PHE A CD2 1 
ATOM   1065 C CE1 . PHE A 1 138 ? 48.538 88.392  -8.021  1.00 29.18 ? 138  PHE A CE1 1 
ATOM   1066 C CE2 . PHE A 1 138 ? 48.642 89.863  -9.927  1.00 30.56 ? 138  PHE A CE2 1 
ATOM   1067 C CZ  . PHE A 1 138 ? 48.725 89.664  -8.554  1.00 30.39 ? 138  PHE A CZ  1 
ATOM   1068 N N   . SER A 1 139 ? 51.299 86.623  -10.908 1.00 30.33 ? 139  SER A N   1 
ATOM   1069 C CA  . SER A 1 139 ? 52.127 86.963  -9.767  1.00 29.68 ? 139  SER A CA  1 
ATOM   1070 C C   . SER A 1 139 ? 52.533 88.438  -9.816  1.00 28.59 ? 139  SER A C   1 
ATOM   1071 O O   . SER A 1 139 ? 52.466 89.076  -10.877 1.00 27.25 ? 139  SER A O   1 
ATOM   1072 C CB  . SER A 1 139 ? 53.311 86.018  -9.631  1.00 29.31 ? 139  SER A CB  1 
ATOM   1073 O OG  . SER A 1 139 ? 54.287 86.259  -10.604 1.00 34.71 ? 139  SER A OG  1 
ATOM   1074 N N   . ILE A 1 140 ? 52.903 88.963  -8.646  1.00 27.72 ? 140  ILE A N   1 
ATOM   1075 C CA  . ILE A 1 140 ? 53.352 90.343  -8.483  1.00 27.99 ? 140  ILE A CA  1 
ATOM   1076 C C   . ILE A 1 140 ? 54.730 90.283  -7.839  1.00 28.06 ? 140  ILE A C   1 
ATOM   1077 O O   . ILE A 1 140 ? 54.992 89.475  -6.909  1.00 26.40 ? 140  ILE A O   1 
ATOM   1078 C CB  . ILE A 1 140 ? 52.357 91.211  -7.654  1.00 28.41 ? 140  ILE A CB  1 
ATOM   1079 C CG1 . ILE A 1 140 ? 52.908 92.629  -7.400  1.00 29.21 ? 140  ILE A CG1 1 
ATOM   1080 C CG2 . ILE A 1 140 ? 52.050 90.573  -6.294  1.00 27.17 ? 140  ILE A CG2 1 
ATOM   1081 C CD1 . ILE A 1 140 ? 51.825 93.650  -7.133  1.00 31.36 ? 140  ILE A CD1 1 
ATOM   1082 N N   . LYS A 1 141 ? 55.612 91.147  -8.338  1.00 28.30 ? 141  LYS A N   1 
ATOM   1083 C CA  . LYS A 1 141 ? 56.992 91.198  -7.886  1.00 28.05 ? 141  LYS A CA  1 
ATOM   1084 C C   . LYS A 1 141 ? 57.442 92.651  -7.744  1.00 27.39 ? 141  LYS A C   1 
ATOM   1085 O O   . LYS A 1 141 ? 57.131 93.459  -8.593  1.00 26.19 ? 141  LYS A O   1 
ATOM   1086 C CB  . LYS A 1 141 ? 57.848 90.475  -8.915  1.00 29.53 ? 141  LYS A CB  1 
ATOM   1087 C CG  . LYS A 1 141 ? 59.278 90.402  -8.591  1.00 35.13 ? 141  LYS A CG  1 
ATOM   1088 C CD  . LYS A 1 141 ? 60.082 90.021  -9.858  1.00 39.83 ? 141  LYS A CD  1 
ATOM   1089 C CE  . LYS A 1 141 ? 59.905 88.538  -10.233 1.00 42.87 ? 141  LYS A CE  1 
ATOM   1090 N NZ  . LYS A 1 141 ? 61.050 87.979  -11.093 1.00 43.72 ? 141  LYS A NZ  1 
ATOM   1091 N N   . VAL A 1 142 ? 58.149 92.972  -6.653  1.00 25.32 ? 142  VAL A N   1 
ATOM   1092 C CA  . VAL A 1 142 ? 58.608 94.331  -6.382  1.00 23.46 ? 142  VAL A CA  1 
ATOM   1093 C C   . VAL A 1 142 ? 60.105 94.168  -6.279  1.00 24.18 ? 142  VAL A C   1 
ATOM   1094 O O   . VAL A 1 142 ? 60.573 93.306  -5.533  1.00 24.67 ? 142  VAL A O   1 
ATOM   1095 C CB  . VAL A 1 142 ? 57.997 94.886  -5.073  1.00 23.88 ? 142  VAL A CB  1 
ATOM   1096 C CG1 . VAL A 1 142 ? 58.506 96.321  -4.780  1.00 21.53 ? 142  VAL A CG1 1 
ATOM   1097 C CG2 . VAL A 1 142 ? 56.443 94.888  -5.176  1.00 20.65 ? 142  VAL A CG2 1 
ATOM   1098 N N   . THR A 1 143 ? 60.863 94.907  -7.078  1.00 23.93 ? 143  THR A N   1 
ATOM   1099 C CA  . THR A 1 143 ? 62.330 94.774  -6.970  1.00 25.14 ? 143  THR A CA  1 
ATOM   1100 C C   . THR A 1 143 ? 62.921 96.125  -6.669  1.00 24.41 ? 143  THR A C   1 
ATOM   1101 O O   . THR A 1 143 ? 62.300 97.155  -6.957  1.00 24.34 ? 143  THR A O   1 
ATOM   1102 C CB  . THR A 1 143 ? 62.992 94.176  -8.234  1.00 26.55 ? 143  THR A CB  1 
ATOM   1103 O OG1 . THR A 1 143 ? 62.911 95.135  -9.277  1.00 32.52 ? 143  THR A OG1 1 
ATOM   1104 C CG2 . THR A 1 143 ? 62.235 92.998  -8.703  1.00 25.09 ? 143  THR A CG2 1 
ATOM   1105 N N   . ARG A 1 144 ? 64.085 96.107  -6.030  1.00 22.98 ? 144  ARG A N   1 
ATOM   1106 C CA  . ARG A 1 144 ? 64.804 97.349  -5.752  1.00 23.87 ? 144  ARG A CA  1 
ATOM   1107 C C   . ARG A 1 144 ? 65.501 97.789  -7.044  1.00 24.04 ? 144  ARG A C   1 
ATOM   1108 O O   . ARG A 1 144 ? 66.229 97.009  -7.655  1.00 24.15 ? 144  ARG A O   1 
ATOM   1109 C CB  . ARG A 1 144 ? 65.812 97.105  -4.671  1.00 22.34 ? 144  ARG A CB  1 
ATOM   1110 C CG  . ARG A 1 144 ? 66.523 98.353  -4.238  1.00 24.06 ? 144  ARG A CG  1 
ATOM   1111 C CD  . ARG A 1 144 ? 67.484 97.980  -3.135  1.00 25.90 ? 144  ARG A CD  1 
ATOM   1112 N NE  . ARG A 1 144 ? 66.802 97.752  -1.851  1.00 24.13 ? 144  ARG A NE  1 
ATOM   1113 C CZ  . ARG A 1 144 ? 66.348 98.713  -1.050  1.00 23.99 ? 144  ARG A CZ  1 
ATOM   1114 N NH1 . ARG A 1 144 ? 66.471 99.997  -1.377  1.00 20.77 ? 144  ARG A NH1 1 
ATOM   1115 N NH2 . ARG A 1 144 ? 65.773 98.380  0.097   1.00 25.22 ? 144  ARG A NH2 1 
ATOM   1116 N N   . ARG A 1 145 ? 65.253 98.999  -7.492  1.00 24.51 ? 145  ARG A N   1 
ATOM   1117 C CA  . ARG A 1 145 ? 65.823 99.394  -8.794  1.00 26.64 ? 145  ARG A CA  1 
ATOM   1118 C C   . ARG A 1 145 ? 67.350 99.528  -8.819  1.00 26.04 ? 145  ARG A C   1 
ATOM   1119 O O   . ARG A 1 145 ? 67.960 99.274  -9.865  1.00 27.01 ? 145  ARG A O   1 
ATOM   1120 C CB  . ARG A 1 145 ? 65.252 100.720 -9.254  1.00 26.93 ? 145  ARG A CB  1 
ATOM   1121 C CG  . ARG A 1 145 ? 63.823 100.636 -9.613  1.00 33.33 ? 145  ARG A CG  1 
ATOM   1122 C CD  . ARG A 1 145 ? 63.311 101.996 -10.032 1.00 41.97 ? 145  ARG A CD  1 
ATOM   1123 N NE  . ARG A 1 145 ? 64.037 102.504 -11.191 1.00 47.77 ? 145  ARG A NE  1 
ATOM   1124 C CZ  . ARG A 1 145 ? 64.005 103.769 -11.613 1.00 51.28 ? 145  ARG A CZ  1 
ATOM   1125 N NH1 . ARG A 1 145 ? 63.266 104.694 -10.984 1.00 53.06 ? 145  ARG A NH1 1 
ATOM   1126 N NH2 . ARG A 1 145 ? 64.712 104.115 -12.681 1.00 51.27 ? 145  ARG A NH2 1 
ATOM   1127 N N   . SER A 1 146 ? 67.965 99.963  -7.715  1.00 25.09 ? 146  SER A N   1 
ATOM   1128 C CA  . SER A 1 146 ? 69.418 100.180 -7.689  1.00 24.66 ? 146  SER A CA  1 
ATOM   1129 C C   . SER A 1 146 ? 70.288 98.930  -7.900  1.00 24.77 ? 146  SER A C   1 
ATOM   1130 O O   . SER A 1 146 ? 71.428 99.026  -8.432  1.00 23.23 ? 146  SER A O   1 
ATOM   1131 C CB  . SER A 1 146 ? 69.853 100.887 -6.392  1.00 24.80 ? 146  SER A CB  1 
ATOM   1132 O OG  . SER A 1 146 ? 69.751 100.019 -5.265  1.00 24.98 ? 146  SER A OG  1 
ATOM   1133 N N   . ASN A 1 147 ? 69.812 97.762  -7.482  1.00 22.98 ? 147  ASN A N   1 
ATOM   1134 C CA  . ASN A 1 147 ? 70.642 96.573  -7.579  1.00 23.86 ? 147  ASN A CA  1 
ATOM   1135 C C   . ASN A 1 147 ? 69.840 95.353  -8.069  1.00 25.17 ? 147  ASN A C   1 
ATOM   1136 O O   . ASN A 1 147 ? 70.334 94.241  -8.015  1.00 24.77 ? 147  ASN A O   1 
ATOM   1137 C CB  . ASN A 1 147 ? 71.308 96.245  -6.223  1.00 24.49 ? 147  ASN A CB  1 
ATOM   1138 C CG  . ASN A 1 147 ? 70.277 95.915  -5.126  1.00 24.83 ? 147  ASN A CG  1 
ATOM   1139 O OD1 . ASN A 1 147 ? 69.099 95.928  -5.392  1.00 22.09 ? 147  ASN A OD1 1 
ATOM   1140 N ND2 . ASN A 1 147 ? 70.734 95.591  -3.939  1.00 25.71 ? 147  ASN A ND2 1 
ATOM   1141 N N   . ASN A 1 148 ? 68.596 95.587  -8.496  1.00 24.47 ? 148  ASN A N   1 
ATOM   1142 C CA  . ASN A 1 148 ? 67.678 94.532  -8.958  1.00 26.45 ? 148  ASN A CA  1 
ATOM   1143 C C   . ASN A 1 148 ? 67.331 93.457  -7.966  1.00 25.90 ? 148  ASN A C   1 
ATOM   1144 O O   . ASN A 1 148 ? 66.957 92.332  -8.371  1.00 27.02 ? 148  ASN A O   1 
ATOM   1145 C CB  . ASN A 1 148 ? 68.141 93.894  -10.272 1.00 27.20 ? 148  ASN A CB  1 
ATOM   1146 C CG  . ASN A 1 148 ? 68.263 94.901  -11.387 1.00 30.20 ? 148  ASN A CG  1 
ATOM   1147 O OD1 . ASN A 1 148 ? 69.373 95.128  -11.903 1.00 35.86 ? 148  ASN A OD1 1 
ATOM   1148 N ND2 . ASN A 1 148 ? 67.155 95.546  -11.745 1.00 30.80 ? 148  ASN A ND2 1 
ATOM   1149 N N   . ARG A 1 149 ? 67.429 93.778  -6.673  1.00 25.32 ? 149  ARG A N   1 
ATOM   1150 C CA  . ARG A 1 149 ? 67.129 92.779  -5.649  1.00 26.14 ? 149  ARG A CA  1 
ATOM   1151 C C   . ARG A 1 149 ? 65.624 92.573  -5.672  1.00 25.02 ? 149  ARG A C   1 
ATOM   1152 O O   . ARG A 1 149 ? 64.880 93.539  -5.605  1.00 23.68 ? 149  ARG A O   1 
ATOM   1153 C CB  . ARG A 1 149 ? 67.625 93.244  -4.295  1.00 26.78 ? 149  ARG A CB  1 
ATOM   1154 C CG  . ARG A 1 149 ? 67.295 92.299  -3.135  1.00 32.00 ? 149  ARG A CG  1 
ATOM   1155 C CD  . ARG A 1 149 ? 68.256 91.124  -3.055  1.00 39.01 ? 149  ARG A CD  1 
ATOM   1156 N NE  . ARG A 1 149 ? 69.601 91.613  -2.849  1.00 45.54 ? 149  ARG A NE  1 
ATOM   1157 C CZ  . ARG A 1 149 ? 70.370 91.254  -1.833  1.00 51.23 ? 149  ARG A CZ  1 
ATOM   1158 N NH1 . ARG A 1 149 ? 69.945 90.364  -0.928  1.00 53.05 ? 149  ARG A NH1 1 
ATOM   1159 N NH2 . ARG A 1 149 ? 71.584 91.762  -1.742  1.00 53.05 ? 149  ARG A NH2 1 
ATOM   1160 N N   . VAL A 1 150 ? 65.177 91.320  -5.771  1.00 25.38 ? 150  VAL A N   1 
ATOM   1161 C CA  . VAL A 1 150 ? 63.718 91.027  -5.741  1.00 25.49 ? 150  VAL A CA  1 
ATOM   1162 C C   . VAL A 1 150 ? 63.265 91.028  -4.273  1.00 24.91 ? 150  VAL A C   1 
ATOM   1163 O O   . VAL A 1 150 ? 63.793 90.281  -3.462  1.00 25.92 ? 150  VAL A O   1 
ATOM   1164 C CB  . VAL A 1 150 ? 63.364 89.700  -6.432  1.00 26.26 ? 150  VAL A CB  1 
ATOM   1165 C CG1 . VAL A 1 150 ? 61.838 89.377  -6.265  1.00 27.97 ? 150  VAL A CG1 1 
ATOM   1166 C CG2 . VAL A 1 150 ? 63.743 89.781  -7.923  1.00 26.42 ? 150  VAL A CG2 1 
ATOM   1167 N N   . LEU A 1 151 ? 62.350 91.913  -3.932  1.00 24.84 ? 151  LEU A N   1 
ATOM   1168 C CA  . LEU A 1 151 ? 61.971 92.111  -2.520  1.00 25.12 ? 151  LEU A CA  1 
ATOM   1169 C C   . LEU A 1 151 ? 60.732 91.284  -2.218  1.00 26.55 ? 151  LEU A C   1 
ATOM   1170 O O   . LEU A 1 151 ? 60.757 90.419  -1.332  1.00 28.33 ? 151  LEU A O   1 
ATOM   1171 C CB  . LEU A 1 151 ? 61.695 93.584  -2.246  1.00 23.28 ? 151  LEU A CB  1 
ATOM   1172 C CG  . LEU A 1 151 ? 62.905 94.501  -2.596  1.00 21.95 ? 151  LEU A CG  1 
ATOM   1173 C CD1 . LEU A 1 151 ? 62.591 95.871  -2.155  1.00 21.68 ? 151  LEU A CD1 1 
ATOM   1174 C CD2 . LEU A 1 151 ? 64.234 94.012  -1.937  1.00 21.94 ? 151  LEU A CD2 1 
ATOM   1175 N N   . PHE A 1 152 ? 59.657 91.618  -2.921  1.00 28.12 ? 152  PHE A N   1 
ATOM   1176 C CA  . PHE A 1 152 ? 58.374 90.936  -2.837  1.00 28.88 ? 152  PHE A CA  1 
ATOM   1177 C C   . PHE A 1 152 ? 58.251 90.136  -4.132  1.00 28.85 ? 152  PHE A C   1 
ATOM   1178 O O   . PHE A 1 152 ? 58.551 90.676  -5.194  1.00 29.12 ? 152  PHE A O   1 
ATOM   1179 C CB  . PHE A 1 152 ? 57.273 91.964  -2.799  1.00 29.55 ? 152  PHE A CB  1 
ATOM   1180 C CG  . PHE A 1 152 ? 55.934 91.407  -2.359  1.00 31.25 ? 152  PHE A CG  1 
ATOM   1181 C CD1 . PHE A 1 152 ? 55.504 91.554  -1.027  1.00 31.14 ? 152  PHE A CD1 1 
ATOM   1182 C CD2 . PHE A 1 152 ? 55.111 90.753  -3.278  1.00 31.74 ? 152  PHE A CD2 1 
ATOM   1183 C CE1 . PHE A 1 152 ? 54.238 91.062  -0.611  1.00 31.37 ? 152  PHE A CE1 1 
ATOM   1184 C CE2 . PHE A 1 152 ? 53.870 90.228  -2.884  1.00 29.52 ? 152  PHE A CE2 1 
ATOM   1185 C CZ  . PHE A 1 152 ? 53.438 90.371  -1.548  1.00 30.90 ? 152  PHE A CZ  1 
ATOM   1186 N N   . ASP A 1 153 ? 57.898 88.854  -4.047  1.00 28.50 ? 153  ASP A N   1 
ATOM   1187 C CA  . ASP A 1 153 ? 57.641 88.040  -5.237  1.00 28.34 ? 153  ASP A CA  1 
ATOM   1188 C C   . ASP A 1 153 ? 56.623 86.958  -4.896  1.00 26.78 ? 153  ASP A C   1 
ATOM   1189 O O   . ASP A 1 153 ? 56.942 85.977  -4.236  1.00 26.88 ? 153  ASP A O   1 
ATOM   1190 C CB  . ASP A 1 153 ? 58.907 87.375  -5.761  1.00 27.21 ? 153  ASP A CB  1 
ATOM   1191 C CG  . ASP A 1 153 ? 58.619 86.446  -6.946  1.00 32.33 ? 153  ASP A CG  1 
ATOM   1192 O OD1 . ASP A 1 153 ? 57.483 86.486  -7.519  1.00 35.26 ? 153  ASP A OD1 1 
ATOM   1193 O OD2 . ASP A 1 153 ? 59.517 85.668  -7.302  1.00 36.13 ? 153  ASP A OD2 1 
ATOM   1194 N N   . SER A 1 154 ? 55.408 87.116  -5.363  1.00 25.79 ? 154  SER A N   1 
ATOM   1195 C CA  . SER A 1 154 ? 54.366 86.203  -4.949  1.00 25.78 ? 154  SER A CA  1 
ATOM   1196 C C   . SER A 1 154 ? 54.382 84.892  -5.733  1.00 26.90 ? 154  SER A C   1 
ATOM   1197 O O   . SER A 1 154 ? 53.633 83.960  -5.399  1.00 26.15 ? 154  SER A O   1 
ATOM   1198 C CB  . SER A 1 154 ? 53.018 86.915  -5.060  1.00 24.83 ? 154  SER A CB  1 
ATOM   1199 O OG  . SER A 1 154 ? 52.607 87.038  -6.405  1.00 25.61 ? 154  SER A OG  1 
ATOM   1200 N N   . SER A 1 155 ? 55.248 84.785  -6.754  1.00 27.30 ? 155  SER A N   1 
ATOM   1201 C CA  . SER A 1 155 ? 55.165 83.666  -7.699  1.00 28.50 ? 155  SER A CA  1 
ATOM   1202 C C   . SER A 1 155 ? 55.441 82.315  -7.044  1.00 27.92 ? 155  SER A C   1 
ATOM   1203 O O   . SER A 1 155 ? 55.217 81.266  -7.650  1.00 28.96 ? 155  SER A O   1 
ATOM   1204 C CB  . SER A 1 155 ? 56.092 83.873  -8.908  1.00 28.93 ? 155  SER A CB  1 
ATOM   1205 O OG  . SER A 1 155 ? 57.460 83.779  -8.495  1.00 32.03 ? 155  SER A OG  1 
ATOM   1206 N N   . ILE A 1 156 ? 55.887 82.313  -5.800  1.00 27.35 ? 156  ILE A N   1 
ATOM   1207 C CA  . ILE A 1 156 ? 56.258 81.037  -5.113  1.00 26.76 ? 156  ILE A CA  1 
ATOM   1208 C C   . ILE A 1 156 ? 54.988 80.224  -4.820  1.00 25.87 ? 156  ILE A C   1 
ATOM   1209 O O   . ILE A 1 156 ? 54.994 78.987  -4.778  1.00 26.18 ? 156  ILE A O   1 
ATOM   1210 C CB  . ILE A 1 156 ? 57.042 81.297  -3.797  1.00 26.15 ? 156  ILE A CB  1 
ATOM   1211 C CG1 . ILE A 1 156 ? 57.538 79.984  -3.191  1.00 26.53 ? 156  ILE A CG1 1 
ATOM   1212 C CG2 . ILE A 1 156 ? 56.209 82.198  -2.830  1.00 26.17 ? 156  ILE A CG2 1 
ATOM   1213 C CD1 . ILE A 1 156 ? 58.370 80.147  -1.972  1.00 21.24 ? 156  ILE A CD1 1 
ATOM   1214 N N   . GLY A 1 157 ? 53.896 80.938  -4.679  1.00 25.24 ? 157  GLY A N   1 
ATOM   1215 C CA  . GLY A 1 157 ? 52.638 80.310  -4.367  1.00 25.66 ? 157  GLY A CA  1 
ATOM   1216 C C   . GLY A 1 157 ? 51.509 80.955  -5.115  1.00 26.51 ? 157  GLY A C   1 
ATOM   1217 O O   . GLY A 1 157 ? 51.686 81.953  -5.785  1.00 25.13 ? 157  GLY A O   1 
ATOM   1218 N N   . PRO A 1 158 ? 50.310 80.398  -4.958  1.00 26.77 ? 158  PRO A N   1 
ATOM   1219 C CA  . PRO A 1 158 ? 49.091 80.887  -5.557  1.00 26.86 ? 158  PRO A CA  1 
ATOM   1220 C C   . PRO A 1 158 ? 48.518 82.136  -4.821  1.00 27.29 ? 158  PRO A C   1 
ATOM   1221 O O   . PRO A 1 158 ? 48.890 82.389  -3.668  1.00 27.60 ? 158  PRO A O   1 
ATOM   1222 C CB  . PRO A 1 158 ? 48.141 79.675  -5.369  1.00 28.11 ? 158  PRO A CB  1 
ATOM   1223 C CG  . PRO A 1 158 ? 48.575 79.073  -4.065  1.00 26.56 ? 158  PRO A CG  1 
ATOM   1224 C CD  . PRO A 1 158 ? 50.105 79.163  -4.163  1.00 27.56 ? 158  PRO A CD  1 
ATOM   1225 N N   . LEU A 1 159 ? 47.661 82.909  -5.494  1.00 25.36 ? 159  LEU A N   1 
ATOM   1226 C CA  . LEU A 1 159 ? 46.747 83.824  -4.832  1.00 25.98 ? 159  LEU A CA  1 
ATOM   1227 C C   . LEU A 1 159 ? 45.478 82.999  -4.586  1.00 26.56 ? 159  LEU A C   1 
ATOM   1228 O O   . LEU A 1 159 ? 45.011 82.357  -5.506  1.00 26.05 ? 159  LEU A O   1 
ATOM   1229 C CB  . LEU A 1 159 ? 46.392 85.013  -5.733  1.00 25.91 ? 159  LEU A CB  1 
ATOM   1230 C CG  . LEU A 1 159 ? 45.149 85.865  -5.392  1.00 25.72 ? 159  LEU A CG  1 
ATOM   1231 C CD1 . LEU A 1 159 ? 45.257 86.651  -4.079  1.00 27.01 ? 159  LEU A CD1 1 
ATOM   1232 C CD2 . LEU A 1 159 ? 44.873 86.857  -6.502  1.00 26.39 ? 159  LEU A CD2 1 
ATOM   1233 N N   . LEU A 1 160 ? 44.991 82.974  -3.343  1.00 26.35 ? 160  LEU A N   1 
ATOM   1234 C CA  . LEU A 1 160 ? 43.674 82.378  -2.994  1.00 27.06 ? 160  LEU A CA  1 
ATOM   1235 C C   . LEU A 1 160 ? 42.792 83.462  -2.458  1.00 27.78 ? 160  LEU A C   1 
ATOM   1236 O O   . LEU A 1 160 ? 43.220 84.315  -1.656  1.00 27.37 ? 160  LEU A O   1 
ATOM   1237 C CB  . LEU A 1 160 ? 43.816 81.256  -1.959  1.00 27.29 ? 160  LEU A CB  1 
ATOM   1238 C CG  . LEU A 1 160 ? 44.879 80.254  -2.409  1.00 27.60 ? 160  LEU A CG  1 
ATOM   1239 C CD1 . LEU A 1 160 ? 45.273 79.413  -1.294  1.00 27.88 ? 160  LEU A CD1 1 
ATOM   1240 C CD2 . LEU A 1 160 ? 44.409 79.415  -3.591  1.00 25.79 ? 160  LEU A CD2 1 
ATOM   1241 N N   . PHE A 1 161 ? 41.565 83.500  -2.956  1.00 28.04 ? 161  PHE A N   1 
ATOM   1242 C CA  . PHE A 1 161 ? 40.689 84.573  -2.605  1.00 29.48 ? 161  PHE A CA  1 
ATOM   1243 C C   . PHE A 1 161 ? 39.282 84.012  -2.533  1.00 30.38 ? 161  PHE A C   1 
ATOM   1244 O O   . PHE A 1 161 ? 38.515 84.158  -3.476  1.00 30.57 ? 161  PHE A O   1 
ATOM   1245 C CB  . PHE A 1 161 ? 40.770 85.682  -3.656  1.00 30.30 ? 161  PHE A CB  1 
ATOM   1246 C CG  . PHE A 1 161 ? 40.354 87.031  -3.165  1.00 31.67 ? 161  PHE A CG  1 
ATOM   1247 C CD1 . PHE A 1 161 ? 41.215 88.113  -3.290  1.00 33.90 ? 161  PHE A CD1 1 
ATOM   1248 C CD2 . PHE A 1 161 ? 39.136 87.231  -2.534  1.00 34.41 ? 161  PHE A CD2 1 
ATOM   1249 C CE1 . PHE A 1 161 ? 40.855 89.368  -2.834  1.00 34.90 ? 161  PHE A CE1 1 
ATOM   1250 C CE2 . PHE A 1 161 ? 38.748 88.498  -2.080  1.00 36.01 ? 161  PHE A CE2 1 
ATOM   1251 C CZ  . PHE A 1 161 ? 39.616 89.579  -2.237  1.00 35.65 ? 161  PHE A CZ  1 
ATOM   1252 N N   . ALA A 1 162 ? 38.948 83.393  -1.406  1.00 29.81 ? 162  ALA A N   1 
ATOM   1253 C CA  . ALA A 1 162 ? 37.574 82.945  -1.132  1.00 29.63 ? 162  ALA A CA  1 
ATOM   1254 C C   . ALA A 1 162 ? 37.002 83.895  -0.098  1.00 29.60 ? 162  ALA A C   1 
ATOM   1255 O O   . ALA A 1 162 ? 37.760 84.646  0.559   1.00 28.17 ? 162  ALA A O   1 
ATOM   1256 C CB  . ALA A 1 162 ? 37.586 81.505  -0.623  1.00 29.00 ? 162  ALA A CB  1 
ATOM   1257 N N   . ASP A 1 163 ? 35.682 83.881  0.086   1.00 29.17 ? 163  ASP A N   1 
ATOM   1258 C CA  . ASP A 1 163 ? 35.082 84.842  1.000   1.00 29.49 ? 163  ASP A CA  1 
ATOM   1259 C C   . ASP A 1 163 ? 35.647 84.763  2.413   1.00 27.29 ? 163  ASP A C   1 
ATOM   1260 O O   . ASP A 1 163 ? 35.734 85.771  3.106   1.00 28.64 ? 163  ASP A O   1 
ATOM   1261 C CB  . ASP A 1 163 ? 33.555 84.734  1.019   1.00 30.38 ? 163  ASP A CB  1 
ATOM   1262 C CG  . ASP A 1 163 ? 32.897 85.808  1.896   1.00 36.52 ? 163  ASP A CG  1 
ATOM   1263 O OD1 . ASP A 1 163 ? 33.277 87.012  1.826   1.00 39.87 ? 163  ASP A OD1 1 
ATOM   1264 O OD2 . ASP A 1 163 ? 31.956 85.446  2.671   1.00 43.12 ? 163  ASP A OD2 1 
ATOM   1265 N N   . GLN A 1 164 ? 36.063 83.584  2.832   1.00 26.06 ? 164  GLN A N   1 
ATOM   1266 C CA  . GLN A 1 164 ? 36.587 83.418  4.197   1.00 26.11 ? 164  GLN A CA  1 
ATOM   1267 C C   . GLN A 1 164 ? 37.929 82.729  4.225   1.00 25.63 ? 164  GLN A C   1 
ATOM   1268 O O   . GLN A 1 164 ? 38.282 82.077  5.200   1.00 24.36 ? 164  GLN A O   1 
ATOM   1269 C CB  . GLN A 1 164 ? 35.577 82.646  5.056   1.00 26.66 ? 164  GLN A CB  1 
ATOM   1270 C CG  . GLN A 1 164 ? 34.383 83.521  5.430   1.00 27.19 ? 164  GLN A CG  1 
ATOM   1271 C CD  . GLN A 1 164 ? 33.412 82.799  6.345   1.00 28.05 ? 164  GLN A CD  1 
ATOM   1272 O OE1 . GLN A 1 164 ? 33.545 82.837  7.567   1.00 27.30 ? 164  GLN A OE1 1 
ATOM   1273 N NE2 . GLN A 1 164 ? 32.467 82.110  5.755   1.00 27.53 ? 164  GLN A NE2 1 
ATOM   1274 N N   . PHE A 1 165 ? 38.686 82.876  3.145   1.00 25.57 ? 165  PHE A N   1 
ATOM   1275 C CA  . PHE A 1 165 ? 40.024 82.337  3.058   1.00 24.97 ? 165  PHE A CA  1 
ATOM   1276 C C   . PHE A 1 165 ? 40.779 83.080  1.968   1.00 25.72 ? 165  PHE A C   1 
ATOM   1277 O O   . PHE A 1 165 ? 40.456 82.934  0.780   1.00 25.61 ? 165  PHE A O   1 
ATOM   1278 C CB  . PHE A 1 165 ? 40.036 80.865  2.763   1.00 25.52 ? 165  PHE A CB  1 
ATOM   1279 C CG  . PHE A 1 165 ? 41.392 80.205  2.979   1.00 29.05 ? 165  PHE A CG  1 
ATOM   1280 C CD1 . PHE A 1 165 ? 41.773 79.746  4.242   1.00 30.28 ? 165  PHE A CD1 1 
ATOM   1281 C CD2 . PHE A 1 165 ? 42.283 80.058  1.921   1.00 29.46 ? 165  PHE A CD2 1 
ATOM   1282 C CE1 . PHE A 1 165 ? 43.024 79.131  4.452   1.00 30.13 ? 165  PHE A CE1 1 
ATOM   1283 C CE2 . PHE A 1 165 ? 43.525 79.453  2.113   1.00 29.64 ? 165  PHE A CE2 1 
ATOM   1284 C CZ  . PHE A 1 165 ? 43.901 78.987  3.391   1.00 30.63 ? 165  PHE A CZ  1 
ATOM   1285 N N   . LEU A 1 166 ? 41.746 83.899  2.395   1.00 23.95 ? 166  LEU A N   1 
ATOM   1286 C CA  . LEU A 1 166 ? 42.533 84.751  1.478   1.00 23.64 ? 166  LEU A CA  1 
ATOM   1287 C C   . LEU A 1 166 ? 43.965 84.449  1.819   1.00 23.70 ? 166  LEU A C   1 
ATOM   1288 O O   . LEU A 1 166 ? 44.338 84.431  3.005   1.00 23.54 ? 166  LEU A O   1 
ATOM   1289 C CB  . LEU A 1 166 ? 42.231 86.250  1.651   1.00 23.52 ? 166  LEU A CB  1 
ATOM   1290 C CG  . LEU A 1 166 ? 40.800 86.689  1.317   1.00 23.90 ? 166  LEU A CG  1 
ATOM   1291 C CD1 . LEU A 1 166 ? 39.965 86.472  2.517   1.00 22.32 ? 166  LEU A CD1 1 
ATOM   1292 C CD2 . LEU A 1 166 ? 40.722 88.149  0.965   1.00 24.76 ? 166  LEU A CD2 1 
ATOM   1293 N N   . GLN A 1 167 ? 44.752 84.178  0.790   1.00 23.00 ? 167  GLN A N   1 
ATOM   1294 C CA  . GLN A 1 167 ? 46.150 83.829  0.957   1.00 21.96 ? 167  GLN A CA  1 
ATOM   1295 C C   . GLN A 1 167 ? 47.014 84.391  -0.154  1.00 22.88 ? 167  GLN A C   1 
ATOM   1296 O O   . GLN A 1 167 ? 46.680 84.281  -1.337  1.00 22.87 ? 167  GLN A O   1 
ATOM   1297 C CB  . GLN A 1 167 ? 46.329 82.313  0.971   1.00 21.72 ? 167  GLN A CB  1 
ATOM   1298 C CG  . GLN A 1 167 ? 47.759 81.914  1.337   1.00 23.16 ? 167  GLN A CG  1 
ATOM   1299 C CD  . GLN A 1 167 ? 47.887 80.435  1.492   1.00 28.02 ? 167  GLN A CD  1 
ATOM   1300 O OE1 . GLN A 1 167 ? 48.563 79.776  0.708   1.00 31.87 ? 167  GLN A OE1 1 
ATOM   1301 N NE2 . GLN A 1 167 ? 47.201 79.884  2.479   1.00 26.03 ? 167  GLN A NE2 1 
ATOM   1302 N N   . LEU A 1 168 ? 48.139 84.968  0.241   1.00 22.68 ? 168  LEU A N   1 
ATOM   1303 C CA  . LEU A 1 168 ? 49.218 85.346  -0.681  1.00 23.01 ? 168  LEU A CA  1 
ATOM   1304 C C   . LEU A 1 168 ? 50.537 85.072  0.009   1.00 23.59 ? 168  LEU A C   1 
ATOM   1305 O O   . LEU A 1 168 ? 50.654 85.273  1.218   1.00 24.27 ? 168  LEU A O   1 
ATOM   1306 C CB  . LEU A 1 168 ? 49.139 86.816  -1.064  1.00 23.38 ? 168  LEU A CB  1 
ATOM   1307 C CG  . LEU A 1 168 ? 49.951 87.204  -2.312  1.00 23.28 ? 168  LEU A CG  1 
ATOM   1308 C CD1 . LEU A 1 168 ? 49.429 86.483  -3.615  1.00 23.37 ? 168  LEU A CD1 1 
ATOM   1309 C CD2 . LEU A 1 168 ? 49.982 88.717  -2.450  1.00 21.89 ? 168  LEU A CD2 1 
ATOM   1310 N N   . SER A 1 169 ? 51.512 84.639  -0.784  1.00 24.10 ? 169  SER A N   1 
ATOM   1311 C CA  . SER A 1 169 ? 52.856 84.306  -0.335  1.00 23.96 ? 169  SER A CA  1 
ATOM   1312 C C   . SER A 1 169 ? 53.855 85.281  -0.982  1.00 24.57 ? 169  SER A C   1 
ATOM   1313 O O   . SER A 1 169 ? 53.557 85.872  -2.020  1.00 23.67 ? 169  SER A O   1 
ATOM   1314 C CB  . SER A 1 169 ? 53.206 82.898  -0.783  1.00 23.51 ? 169  SER A CB  1 
ATOM   1315 O OG  . SER A 1 169 ? 52.533 81.928  -0.051  1.00 24.45 ? 169  SER A OG  1 
ATOM   1316 N N   . THR A 1 170 ? 55.008 85.457  -0.355  1.00 25.18 ? 170  THR A N   1 
ATOM   1317 C CA  . THR A 1 170 ? 56.134 86.144  -0.987  1.00 25.79 ? 170  THR A CA  1 
ATOM   1318 C C   . THR A 1 170 ? 57.477 85.473  -0.656  1.00 25.14 ? 170  THR A C   1 
ATOM   1319 O O   . THR A 1 170 ? 57.729 85.113  0.481   1.00 24.29 ? 170  THR A O   1 
ATOM   1320 C CB  . THR A 1 170 ? 56.150 87.673  -0.672  1.00 26.45 ? 170  THR A CB  1 
ATOM   1321 O OG1 . THR A 1 170 ? 57.264 88.285  -1.312  1.00 28.33 ? 170  THR A OG1 1 
ATOM   1322 C CG2 . THR A 1 170 ? 56.219 87.990  0.827   1.00 28.76 ? 170  THR A CG2 1 
ATOM   1323 N N   . ARG A 1 171 ? 58.328 85.308  -1.663  1.00 24.71 ? 171  ARG A N   1 
ATOM   1324 C CA  . ARG A 1 171 ? 59.731 84.976  -1.432  1.00 26.20 ? 171  ARG A CA  1 
ATOM   1325 C C   . ARG A 1 171 ? 60.337 86.173  -0.721  1.00 26.37 ? 171  ARG A C   1 
ATOM   1326 O O   . ARG A 1 171 ? 59.814 87.295  -0.812  1.00 27.17 ? 171  ARG A O   1 
ATOM   1327 C CB  . ARG A 1 171 ? 60.486 84.816  -2.739  1.00 27.01 ? 171  ARG A CB  1 
ATOM   1328 C CG  . ARG A 1 171 ? 59.896 83.802  -3.674  1.00 28.80 ? 171  ARG A CG  1 
ATOM   1329 C CD  . ARG A 1 171 ? 60.879 83.555  -4.805  1.00 34.55 ? 171  ARG A CD  1 
ATOM   1330 N NE  . ARG A 1 171 ? 60.160 83.013  -5.938  1.00 36.08 ? 171  ARG A NE  1 
ATOM   1331 C CZ  . ARG A 1 171 ? 60.092 81.728  -6.221  1.00 38.53 ? 171  ARG A CZ  1 
ATOM   1332 N NH1 . ARG A 1 171 ? 60.741 80.841  -5.475  1.00 37.22 ? 171  ARG A NH1 1 
ATOM   1333 N NH2 . ARG A 1 171 ? 59.363 81.349  -7.262  1.00 40.82 ? 171  ARG A NH2 1 
ATOM   1334 N N   . LEU A 1 172 ? 61.424 85.911  -0.012  1.00 26.47 ? 172  LEU A N   1 
ATOM   1335 C CA  . LEU A 1 172 ? 62.200 86.940  0.683   1.00 26.97 ? 172  LEU A CA  1 
ATOM   1336 C C   . LEU A 1 172 ? 63.654 86.861  0.234   1.00 27.56 ? 172  LEU A C   1 
ATOM   1337 O O   . LEU A 1 172 ? 64.109 85.772  -0.088  1.00 27.57 ? 172  LEU A O   1 
ATOM   1338 C CB  . LEU A 1 172 ? 62.081 86.707  2.206   1.00 26.05 ? 172  LEU A CB  1 
ATOM   1339 C CG  . LEU A 1 172 ? 60.653 86.886  2.756   1.00 25.79 ? 172  LEU A CG  1 
ATOM   1340 C CD1 . LEU A 1 172 ? 60.616 86.399  4.197   1.00 28.18 ? 172  LEU A CD1 1 
ATOM   1341 C CD2 . LEU A 1 172 ? 60.182 88.326  2.669   1.00 26.63 ? 172  LEU A CD2 1 
ATOM   1342 N N   . PRO A 1 173 ? 64.370 88.016  0.207   1.00 27.78 ? 173  PRO A N   1 
ATOM   1343 C CA  . PRO A 1 173 ? 65.787 88.109  -0.161  1.00 28.31 ? 173  PRO A CA  1 
ATOM   1344 C C   . PRO A 1 173 ? 66.770 87.565  0.872   1.00 28.78 ? 173  PRO A C   1 
ATOM   1345 O O   . PRO A 1 173 ? 67.928 87.258  0.518   1.00 29.89 ? 173  PRO A O   1 
ATOM   1346 C CB  . PRO A 1 173 ? 66.008 89.613  -0.419  1.00 28.84 ? 173  PRO A CB  1 
ATOM   1347 C CG  . PRO A 1 173 ? 64.910 90.331  0.312   1.00 27.34 ? 173  PRO A CG  1 
ATOM   1348 C CD  . PRO A 1 173 ? 63.774 89.333  0.522   1.00 27.73 ? 173  PRO A CD  1 
ATOM   1349 N N   . SER A 1 174 ? 66.310 87.382  2.115   1.00 27.85 ? 174  SER A N   1 
ATOM   1350 C CA  . SER A 1 174 ? 67.153 86.948  3.226   1.00 27.28 ? 174  SER A CA  1 
ATOM   1351 C C   . SER A 1 174 ? 66.303 86.290  4.308   1.00 27.10 ? 174  SER A C   1 
ATOM   1352 O O   . SER A 1 174 ? 65.058 86.309  4.260   1.00 27.42 ? 174  SER A O   1 
ATOM   1353 C CB  . SER A 1 174 ? 67.937 88.135  3.846   1.00 26.70 ? 174  SER A CB  1 
ATOM   1354 O OG  . SER A 1 174 ? 67.071 88.989  4.620   1.00 27.87 ? 174  SER A OG  1 
ATOM   1355 N N   . THR A 1 175 ? 66.968 85.747  5.306   1.00 27.57 ? 175  THR A N   1 
ATOM   1356 C CA  . THR A 1 175 ? 66.281 85.221  6.507   1.00 27.64 ? 175  THR A CA  1 
ATOM   1357 C C   . THR A 1 175 ? 66.375 86.198  7.685   1.00 26.94 ? 175  THR A C   1 
ATOM   1358 O O   . THR A 1 175 ? 66.085 85.825  8.843   1.00 27.28 ? 175  THR A O   1 
ATOM   1359 C CB  . THR A 1 175 ? 66.902 83.865  6.927   1.00 29.87 ? 175  THR A CB  1 
ATOM   1360 O OG1 . THR A 1 175 ? 68.320 84.043  7.098   1.00 31.51 ? 175  THR A OG1 1 
ATOM   1361 C CG2 . THR A 1 175 ? 66.665 82.808  5.849   1.00 30.48 ? 175  THR A CG2 1 
ATOM   1362 N N   . ASN A 1 176 ? 66.807 87.437  7.416   1.00 23.75 ? 176  ASN A N   1 
ATOM   1363 C CA  . ASN A 1 176 ? 66.841 88.434  8.458   1.00 23.49 ? 176  ASN A CA  1 
ATOM   1364 C C   . ASN A 1 176 ? 65.512 89.136  8.506   1.00 22.46 ? 176  ASN A C   1 
ATOM   1365 O O   . ASN A 1 176 ? 65.382 90.174  7.906   1.00 19.42 ? 176  ASN A O   1 
ATOM   1366 C CB  . ASN A 1 176 ? 67.956 89.467  8.219   1.00 23.09 ? 176  ASN A CB  1 
ATOM   1367 C CG  . ASN A 1 176 ? 69.292 88.818  8.006   1.00 26.88 ? 176  ASN A CG  1 
ATOM   1368 O OD1 . ASN A 1 176 ? 69.696 87.949  8.788   1.00 27.73 ? 176  ASN A OD1 1 
ATOM   1369 N ND2 . ASN A 1 176 ? 69.996 89.241  6.953   1.00 28.84 ? 176  ASN A ND2 1 
ATOM   1370 N N   . VAL A 1 177 ? 64.551 88.535  9.225   1.00 21.59 ? 177  VAL A N   1 
ATOM   1371 C CA  . VAL A 1 177 ? 63.174 88.903  9.177   1.00 21.92 ? 177  VAL A CA  1 
ATOM   1372 C C   . VAL A 1 177 ? 62.763 89.194  10.662  1.00 21.30 ? 177  VAL A C   1 
ATOM   1373 O O   . VAL A 1 177 ? 63.061 88.414  11.582  1.00 19.61 ? 177  VAL A O   1 
ATOM   1374 C CB  . VAL A 1 177 ? 62.303 87.754  8.510   1.00 22.56 ? 177  VAL A CB  1 
ATOM   1375 C CG1 . VAL A 1 177 ? 60.810 88.064  8.650   1.00 22.78 ? 177  VAL A CG1 1 
ATOM   1376 C CG2 . VAL A 1 177 ? 62.597 87.615  7.013   1.00 23.01 ? 177  VAL A CG2 1 
ATOM   1377 N N   . TYR A 1 178 ? 62.095 90.316  10.889  1.00 20.57 ? 178  TYR A N   1 
ATOM   1378 C CA  . TYR A 1 178 ? 61.841 90.800  12.263  1.00 20.33 ? 178  TYR A CA  1 
ATOM   1379 C C   . TYR A 1 178 ? 60.434 91.342  12.244  1.00 21.27 ? 178  TYR A C   1 
ATOM   1380 O O   . TYR A 1 178 ? 60.085 91.997  11.306  1.00 20.19 ? 178  TYR A O   1 
ATOM   1381 C CB  . TYR A 1 178 ? 62.825 91.945  12.629  1.00 20.35 ? 178  TYR A CB  1 
ATOM   1382 C CG  . TYR A 1 178 ? 64.273 91.585  12.351  1.00 20.10 ? 178  TYR A CG  1 
ATOM   1383 C CD1 . TYR A 1 178 ? 65.002 90.866  13.274  1.00 19.98 ? 178  TYR A CD1 1 
ATOM   1384 C CD2 . TYR A 1 178 ? 64.885 91.942  11.153  1.00 19.52 ? 178  TYR A CD2 1 
ATOM   1385 C CE1 . TYR A 1 178 ? 66.295 90.521  13.054  1.00 19.02 ? 178  TYR A CE1 1 
ATOM   1386 C CE2 . TYR A 1 178 ? 66.201 91.573  10.906  1.00 20.78 ? 178  TYR A CE2 1 
ATOM   1387 C CZ  . TYR A 1 178 ? 66.879 90.853  11.860  1.00 20.15 ? 178  TYR A CZ  1 
ATOM   1388 O OH  . TYR A 1 178 ? 68.176 90.482  11.649  1.00 23.87 ? 178  TYR A OH  1 
ATOM   1389 N N   . GLY A 1 179 ? 59.631 91.082  13.277  1.00 20.87 ? 179  GLY A N   1 
ATOM   1390 C CA  . GLY A 1 179 ? 58.337 91.734  13.360  1.00 21.54 ? 179  GLY A CA  1 
ATOM   1391 C C   . GLY A 1 179 ? 57.272 90.672  13.543  1.00 21.37 ? 179  GLY A C   1 
ATOM   1392 O O   . GLY A 1 179 ? 57.557 89.557  13.986  1.00 21.01 ? 179  GLY A O   1 
ATOM   1393 N N   . LEU A 1 180 ? 56.057 91.027  13.167  1.00 21.61 ? 180  LEU A N   1 
ATOM   1394 C CA  . LEU A 1 180 ? 54.834 90.246  13.456  1.00 21.36 ? 180  LEU A CA  1 
ATOM   1395 C C   . LEU A 1 180 ? 54.504 90.227  14.960  1.00 21.06 ? 180  LEU A C   1 
ATOM   1396 O O   . LEU A 1 180 ? 55.385 90.268  15.847  1.00 21.49 ? 180  LEU A O   1 
ATOM   1397 C CB  . LEU A 1 180 ? 54.922 88.801  12.918  1.00 21.65 ? 180  LEU A CB  1 
ATOM   1398 C CG  . LEU A 1 180 ? 55.382 88.612  11.477  1.00 22.33 ? 180  LEU A CG  1 
ATOM   1399 C CD1 . LEU A 1 180 ? 55.544 87.109  11.134  1.00 23.75 ? 180  LEU A CD1 1 
ATOM   1400 C CD2 . LEU A 1 180 ? 54.438 89.312  10.493  1.00 20.27 ? 180  LEU A CD2 1 
ATOM   1401 N N   . GLY A 1 181 ? 53.232 90.185  15.281  1.00 20.33 ? 181  GLY A N   1 
ATOM   1402 C CA  . GLY A 1 181 ? 52.893 90.220  16.695  1.00 20.49 ? 181  GLY A CA  1 
ATOM   1403 C C   . GLY A 1 181 ? 51.413 90.117  16.800  1.00 20.70 ? 181  GLY A C   1 
ATOM   1404 O O   . GLY A 1 181 ? 50.741 90.167  15.768  1.00 19.98 ? 181  GLY A O   1 
ATOM   1405 N N   . GLU A 1 182 ? 50.904 90.012  18.026  1.00 20.22 ? 182  GLU A N   1 
ATOM   1406 C CA  . GLU A 1 182 ? 51.728 90.027  19.217  1.00 22.87 ? 182  GLU A CA  1 
ATOM   1407 C C   . GLU A 1 182 ? 51.953 88.586  19.651  1.00 22.76 ? 182  GLU A C   1 
ATOM   1408 O O   . GLU A 1 182 ? 50.978 87.822  19.861  1.00 23.16 ? 182  GLU A O   1 
ATOM   1409 C CB  . GLU A 1 182 ? 51.031 90.814  20.344  1.00 23.05 ? 182  GLU A CB  1 
ATOM   1410 C CG  . GLU A 1 182 ? 51.856 90.857  21.644  1.00 23.54 ? 182  GLU A CG  1 
ATOM   1411 C CD  . GLU A 1 182 ? 51.321 91.840  22.666  1.00 26.34 ? 182  GLU A CD  1 
ATOM   1412 O OE1 . GLU A 1 182 ? 50.192 92.333  22.409  1.00 32.23 ? 182  GLU A OE1 1 
ATOM   1413 O OE2 . GLU A 1 182 ? 52.008 92.131  23.709  1.00 27.38 ? 182  GLU A OE2 1 
ATOM   1414 N N   . HIS A 1 183 ? 53.214 88.207  19.774  1.00 23.49 ? 183  HIS A N   1 
ATOM   1415 C CA  . HIS A 1 183 ? 53.563 86.858  20.234  1.00 23.47 ? 183  HIS A CA  1 
ATOM   1416 C C   . HIS A 1 183 ? 54.766 86.965  21.148  1.00 24.28 ? 183  HIS A C   1 
ATOM   1417 O O   . HIS A 1 183 ? 55.425 88.010  21.199  1.00 24.36 ? 183  HIS A O   1 
ATOM   1418 C CB  . HIS A 1 183 ? 53.951 85.937  19.060  1.00 23.76 ? 183  HIS A CB  1 
ATOM   1419 C CG  . HIS A 1 183 ? 53.148 86.133  17.818  1.00 21.23 ? 183  HIS A CG  1 
ATOM   1420 N ND1 . HIS A 1 183 ? 51.864 85.661  17.680  1.00 24.42 ? 183  HIS A ND1 1 
ATOM   1421 C CD2 . HIS A 1 183 ? 53.493 86.641  16.613  1.00 18.97 ? 183  HIS A CD2 1 
ATOM   1422 C CE1 . HIS A 1 183 ? 51.419 85.947  16.474  1.00 19.69 ? 183  HIS A CE1 1 
ATOM   1423 N NE2 . HIS A 1 183 ? 52.384 86.558  15.814  1.00 23.05 ? 183  HIS A NE2 1 
ATOM   1424 N N   . VAL A 1 184 ? 55.080 85.853  21.829  1.00 24.01 ? 184  VAL A N   1 
ATOM   1425 C CA  . VAL A 1 184 ? 56.363 85.658  22.435  1.00 24.20 ? 184  VAL A CA  1 
ATOM   1426 C C   . VAL A 1 184 ? 57.193 84.814  21.467  1.00 24.36 ? 184  VAL A C   1 
ATOM   1427 O O   . VAL A 1 184 ? 57.097 83.568  21.429  1.00 24.08 ? 184  VAL A O   1 
ATOM   1428 C CB  . VAL A 1 184 ? 56.185 84.986  23.819  1.00 25.14 ? 184  VAL A CB  1 
ATOM   1429 C CG1 . VAL A 1 184 ? 57.519 84.632  24.397  1.00 23.36 ? 184  VAL A CG1 1 
ATOM   1430 C CG2 . VAL A 1 184 ? 55.444 85.953  24.735  1.00 22.70 ? 184  VAL A CG2 1 
ATOM   1431 N N   . HIS A 1 185 ? 57.995 85.464  20.630  1.00 23.25 ? 185  HIS A N   1 
ATOM   1432 C CA  . HIS A 1 185 ? 58.768 84.721  19.633  1.00 23.84 ? 185  HIS A CA  1 
ATOM   1433 C C   . HIS A 1 185 ? 59.949 84.019  20.300  1.00 24.48 ? 185  HIS A C   1 
ATOM   1434 O O   . HIS A 1 185 ? 60.485 83.088  19.735  1.00 23.71 ? 185  HIS A O   1 
ATOM   1435 C CB  . HIS A 1 185 ? 59.275 85.629  18.472  1.00 23.13 ? 185  HIS A CB  1 
ATOM   1436 C CG  . HIS A 1 185 ? 58.165 86.265  17.694  1.00 25.17 ? 185  HIS A CG  1 
ATOM   1437 N ND1 . HIS A 1 185 ? 58.148 87.604  17.363  1.00 25.50 ? 185  HIS A ND1 1 
ATOM   1438 C CD2 . HIS A 1 185 ? 56.993 85.748  17.239  1.00 23.79 ? 185  HIS A CD2 1 
ATOM   1439 C CE1 . HIS A 1 185 ? 57.023 87.884  16.718  1.00 24.90 ? 185  HIS A CE1 1 
ATOM   1440 N NE2 . HIS A 1 185 ? 56.309 86.777  16.623  1.00 24.05 ? 185  HIS A NE2 1 
ATOM   1441 N N   . GLN A 1 186 ? 60.368 84.516  21.463  1.00 25.39 ? 186  GLN A N   1 
ATOM   1442 C CA  . GLN A 1 186 ? 61.572 84.001  22.188  1.00 27.89 ? 186  GLN A CA  1 
ATOM   1443 C C   . GLN A 1 186 ? 62.914 84.363  21.584  1.00 29.25 ? 186  GLN A C   1 
ATOM   1444 O O   . GLN A 1 186 ? 63.950 84.188  22.212  1.00 32.11 ? 186  GLN A O   1 
ATOM   1445 C CB  . GLN A 1 186 ? 61.496 82.461  22.441  1.00 25.64 ? 186  GLN A CB  1 
ATOM   1446 C CG  . GLN A 1 186 ? 60.130 82.050  23.051  1.00 28.57 ? 186  GLN A CG  1 
ATOM   1447 C CD  . GLN A 1 186 ? 59.928 80.546  23.286  1.00 29.43 ? 186  GLN A CD  1 
ATOM   1448 O OE1 . GLN A 1 186 ? 60.863 79.829  23.500  1.00 30.54 ? 186  GLN A OE1 1 
ATOM   1449 N NE2 . GLN A 1 186 ? 58.675 80.100  23.265  1.00 33.43 ? 186  GLN A NE2 1 
ATOM   1450 N N   . GLN A 1 187 ? 62.925 84.810  20.353  1.00 30.16 ? 187  GLN A N   1 
ATOM   1451 C CA  . GLN A 1 187 ? 64.122 85.348  19.748  1.00 29.63 ? 187  GLN A CA  1 
ATOM   1452 C C   . GLN A 1 187 ? 63.676 86.507  18.895  1.00 28.49 ? 187  GLN A C   1 
ATOM   1453 O O   . GLN A 1 187 ? 62.503 86.595  18.572  1.00 30.65 ? 187  GLN A O   1 
ATOM   1454 C CB  . GLN A 1 187 ? 64.802 84.304  18.892  1.00 29.71 ? 187  GLN A CB  1 
ATOM   1455 C CG  . GLN A 1 187 ? 63.993 83.734  17.758  1.00 34.52 ? 187  GLN A CG  1 
ATOM   1456 C CD  . GLN A 1 187 ? 64.530 82.394  17.307  1.00 41.08 ? 187  GLN A CD  1 
ATOM   1457 O OE1 . GLN A 1 187 ? 65.002 82.257  16.171  1.00 43.84 ? 187  GLN A OE1 1 
ATOM   1458 N NE2 . GLN A 1 187 ? 64.496 81.397  18.209  1.00 41.03 ? 187  GLN A NE2 1 
ATOM   1459 N N   . TYR A 1 188 ? 64.599 87.357  18.481  1.00 26.12 ? 188  TYR A N   1 
ATOM   1460 C CA  . TYR A 1 188 ? 64.240 88.524  17.708  1.00 23.70 ? 188  TYR A CA  1 
ATOM   1461 C C   . TYR A 1 188 ? 64.201 88.246  16.190  1.00 23.85 ? 188  TYR A C   1 
ATOM   1462 O O   . TYR A 1 188 ? 63.170 88.485  15.513  1.00 22.08 ? 188  TYR A O   1 
ATOM   1463 C CB  . TYR A 1 188 ? 65.180 89.698  18.070  1.00 23.35 ? 188  TYR A CB  1 
ATOM   1464 C CG  . TYR A 1 188 ? 64.798 90.968  17.384  1.00 22.19 ? 188  TYR A CG  1 
ATOM   1465 C CD1 . TYR A 1 188 ? 63.486 91.478  17.509  1.00 22.05 ? 188  TYR A CD1 1 
ATOM   1466 C CD2 . TYR A 1 188 ? 65.711 91.655  16.605  1.00 24.08 ? 188  TYR A CD2 1 
ATOM   1467 C CE1 . TYR A 1 188 ? 63.090 92.624  16.842  1.00 20.70 ? 188  TYR A CE1 1 
ATOM   1468 C CE2 . TYR A 1 188 ? 65.338 92.822  15.942  1.00 20.89 ? 188  TYR A CE2 1 
ATOM   1469 C CZ  . TYR A 1 188 ? 64.031 93.285  16.082  1.00 22.00 ? 188  TYR A CZ  1 
ATOM   1470 O OH  . TYR A 1 188 ? 63.661 94.403  15.416  1.00 23.62 ? 188  TYR A OH  1 
ATOM   1471 N N   . ARG A 1 189 ? 65.290 87.699  15.654  1.00 20.90 ? 189  ARG A N   1 
ATOM   1472 C CA  . ARG A 1 189 ? 65.314 87.284  14.266  1.00 21.07 ? 189  ARG A CA  1 
ATOM   1473 C C   . ARG A 1 189 ? 64.473 86.010  14.062  1.00 22.37 ? 189  ARG A C   1 
ATOM   1474 O O   . ARG A 1 189 ? 64.595 85.047  14.834  1.00 22.87 ? 189  ARG A O   1 
ATOM   1475 C CB  . ARG A 1 189 ? 66.763 87.020  13.761  1.00 18.93 ? 189  ARG A CB  1 
ATOM   1476 C CG  . ARG A 1 189 ? 66.698 86.842  12.235  1.00 21.30 ? 189  ARG A CG  1 
ATOM   1477 C CD  . ARG A 1 189 ? 68.006 86.722  11.633  1.00 22.68 ? 189  ARG A CD  1 
ATOM   1478 N NE  . ARG A 1 189 ? 68.687 85.517  12.099  1.00 26.43 ? 189  ARG A NE  1 
ATOM   1479 C CZ  . ARG A 1 189 ? 69.936 85.257  11.755  1.00 30.81 ? 189  ARG A CZ  1 
ATOM   1480 N NH1 . ARG A 1 189 ? 70.580 86.120  10.949  1.00 28.98 ? 189  ARG A NH1 1 
ATOM   1481 N NH2 . ARG A 1 189 ? 70.542 84.165  12.216  1.00 33.44 ? 189  ARG A NH2 1 
ATOM   1482 N N   . HIS A 1 190 ? 63.588 86.016  13.083  1.00 23.07 ? 190  HIS A N   1 
ATOM   1483 C CA  . HIS A 1 190 ? 62.651 84.917  12.948  1.00 25.92 ? 190  HIS A CA  1 
ATOM   1484 C C   . HIS A 1 190 ? 63.254 83.567  12.655  1.00 28.83 ? 190  HIS A C   1 
ATOM   1485 O O   . HIS A 1 190 ? 64.161 83.456  11.856  1.00 28.58 ? 190  HIS A O   1 
ATOM   1486 C CB  . HIS A 1 190 ? 61.531 85.247  11.962  1.00 25.62 ? 190  HIS A CB  1 
ATOM   1487 C CG  . HIS A 1 190 ? 60.365 85.878  12.642  1.00 29.13 ? 190  HIS A CG  1 
ATOM   1488 N ND1 . HIS A 1 190 ? 60.246 87.246  12.821  1.00 30.21 ? 190  HIS A ND1 1 
ATOM   1489 C CD2 . HIS A 1 190 ? 59.333 85.319  13.317  1.00 30.68 ? 190  HIS A CD2 1 
ATOM   1490 C CE1 . HIS A 1 190 ? 59.139 87.498  13.506  1.00 28.34 ? 190  HIS A CE1 1 
ATOM   1491 N NE2 . HIS A 1 190 ? 58.573 86.348  13.823  1.00 33.24 ? 190  HIS A NE2 1 
ATOM   1492 N N   . ASP A 1 191 ? 62.761 82.560  13.394  1.00 31.72 ? 191  ASP A N   1 
ATOM   1493 C CA  . ASP A 1 191 ? 62.875 81.160  13.010  1.00 34.37 ? 191  ASP A CA  1 
ATOM   1494 C C   . ASP A 1 191 ? 62.057 80.943  11.721  1.00 34.16 ? 191  ASP A C   1 
ATOM   1495 O O   . ASP A 1 191 ? 60.816 81.018  11.726  1.00 33.56 ? 191  ASP A O   1 
ATOM   1496 C CB  . ASP A 1 191 ? 62.355 80.241  14.145  1.00 35.16 ? 191  ASP A CB  1 
ATOM   1497 C CG  . ASP A 1 191 ? 62.716 78.766  13.929  1.00 39.19 ? 191  ASP A CG  1 
ATOM   1498 O OD1 . ASP A 1 191 ? 63.185 78.408  12.827  1.00 42.51 ? 191  ASP A OD1 1 
ATOM   1499 O OD2 . ASP A 1 191 ? 62.541 77.959  14.876  1.00 45.04 ? 191  ASP A OD2 1 
ATOM   1500 N N   . MET A 1 192 ? 62.759 80.666  10.616  1.00 35.51 ? 192  MET A N   1 
ATOM   1501 C CA  . MET A 1 192 ? 62.094 80.512  9.316   1.00 34.96 ? 192  MET A CA  1 
ATOM   1502 C C   . MET A 1 192 ? 61.851 79.041  9.016   1.00 35.42 ? 192  MET A C   1 
ATOM   1503 O O   . MET A 1 192 ? 61.564 78.688  7.883   1.00 35.63 ? 192  MET A O   1 
ATOM   1504 C CB  . MET A 1 192 ? 62.907 81.155  8.181   1.00 35.16 ? 192  MET A CB  1 
ATOM   1505 C CG  . MET A 1 192 ? 63.170 82.691  8.275   1.00 36.60 ? 192  MET A CG  1 
ATOM   1506 S SD  . MET A 1 192 ? 61.683 83.704  8.107   1.00 37.43 ? 192  MET A SD  1 
ATOM   1507 C CE  . MET A 1 192 ? 61.326 83.521  6.374   1.00 31.72 ? 192  MET A CE  1 
ATOM   1508 N N   . ASN A 1 193 ? 61.956 78.178  10.018  1.00 34.84 ? 193  ASN A N   1 
ATOM   1509 C CA  . ASN A 1 193 ? 61.810 76.747  9.770   1.00 35.44 ? 193  ASN A CA  1 
ATOM   1510 C C   . ASN A 1 193 ? 60.415 76.246  9.948   1.00 33.40 ? 193  ASN A C   1 
ATOM   1511 O O   . ASN A 1 193 ? 60.114 75.524  10.908  1.00 34.71 ? 193  ASN A O   1 
ATOM   1512 C CB  . ASN A 1 193 ? 62.732 75.911  10.666  1.00 36.85 ? 193  ASN A CB  1 
ATOM   1513 C CG  . ASN A 1 193 ? 64.185 76.185  10.395  1.00 41.20 ? 193  ASN A CG  1 
ATOM   1514 O OD1 . ASN A 1 193 ? 64.911 76.629  11.293  1.00 47.64 ? 193  ASN A OD1 1 
ATOM   1515 N ND2 . ASN A 1 193 ? 64.619 75.965  9.143   1.00 45.16 ? 193  ASN A ND2 1 
ATOM   1516 N N   . TRP A 1 194 ? 59.567 76.629  9.029   1.00 30.79 ? 194  TRP A N   1 
ATOM   1517 C CA  . TRP A 1 194 ? 58.230 76.143  9.022   1.00 29.15 ? 194  TRP A CA  1 
ATOM   1518 C C   . TRP A 1 194 ? 57.670 76.546  10.355  1.00 29.61 ? 194  TRP A C   1 
ATOM   1519 O O   . TRP A 1 194 ? 57.608 75.718  11.259  1.00 30.97 ? 194  TRP A O   1 
ATOM   1520 C CB  . TRP A 1 194 ? 58.250 74.623  8.861   1.00 27.06 ? 194  TRP A CB  1 
ATOM   1521 C CG  . TRP A 1 194 ? 59.029 74.186  7.645   1.00 24.49 ? 194  TRP A CG  1 
ATOM   1522 C CD1 . TRP A 1 194 ? 60.283 73.643  7.611   1.00 25.43 ? 194  TRP A CD1 1 
ATOM   1523 C CD2 . TRP A 1 194 ? 58.602 74.305  6.292   1.00 22.19 ? 194  TRP A CD2 1 
ATOM   1524 N NE1 . TRP A 1 194 ? 60.640 73.381  6.295   1.00 23.12 ? 194  TRP A NE1 1 
ATOM   1525 C CE2 . TRP A 1 194 ? 59.618 73.776  5.478   1.00 21.99 ? 194  TRP A CE2 1 
ATOM   1526 C CE3 . TRP A 1 194 ? 57.433 74.785  5.683   1.00 22.09 ? 194  TRP A CE3 1 
ATOM   1527 C CZ2 . TRP A 1 194 ? 59.513 73.732  4.086   1.00 21.41 ? 194  TRP A CZ2 1 
ATOM   1528 C CZ3 . TRP A 1 194 ? 57.334 74.741  4.296   1.00 21.91 ? 194  TRP A CZ3 1 
ATOM   1529 C CH2 . TRP A 1 194 ? 58.381 74.227  3.517   1.00 23.78 ? 194  TRP A CH2 1 
ATOM   1530 N N   . LYS A 1 195 ? 57.298 77.819  10.500  1.00 27.95 ? 195  LYS A N   1 
ATOM   1531 C CA  . LYS A 1 195 ? 56.646 78.287  11.721  1.00 28.25 ? 195  LYS A CA  1 
ATOM   1532 C C   . LYS A 1 195 ? 55.358 79.014  11.337  1.00 27.23 ? 195  LYS A C   1 
ATOM   1533 O O   . LYS A 1 195 ? 55.327 79.707  10.333  1.00 27.60 ? 195  LYS A O   1 
ATOM   1534 C CB  . LYS A 1 195 ? 57.540 79.216  12.560  1.00 28.39 ? 195  LYS A CB  1 
ATOM   1535 C CG  . LYS A 1 195 ? 58.728 78.537  13.247  1.00 34.13 ? 195  LYS A CG  1 
ATOM   1536 C CD  . LYS A 1 195 ? 58.362 77.292  14.096  1.00 39.99 ? 195  LYS A CD  1 
ATOM   1537 C CE  . LYS A 1 195 ? 59.405 77.080  15.222  1.00 47.79 ? 195  LYS A CE  1 
ATOM   1538 N NZ  . LYS A 1 195 ? 60.009 75.679  15.337  1.00 48.58 ? 195  LYS A NZ  1 
ATOM   1539 N N   . THR A 1 196 ? 54.290 78.801  12.096  1.00 26.07 ? 196  THR A N   1 
ATOM   1540 C CA  . THR A 1 196 ? 52.997 79.481  11.848  1.00 24.56 ? 196  THR A CA  1 
ATOM   1541 C C   . THR A 1 196 ? 52.683 80.271  13.099  1.00 24.61 ? 196  THR A C   1 
ATOM   1542 O O   . THR A 1 196 ? 52.893 79.773  14.231  1.00 24.71 ? 196  THR A O   1 
ATOM   1543 C CB  . THR A 1 196 ? 51.875 78.467  11.476  1.00 24.99 ? 196  THR A CB  1 
ATOM   1544 O OG1 . THR A 1 196 ? 52.242 77.723  10.316  1.00 25.50 ? 196  THR A OG1 1 
ATOM   1545 C CG2 . THR A 1 196 ? 50.539 79.137  11.148  1.00 24.57 ? 196  THR A CG2 1 
ATOM   1546 N N   . TRP A 1 197 ? 52.282 81.523  12.902  1.00 22.79 ? 197  TRP A N   1 
ATOM   1547 C CA  . TRP A 1 197 ? 52.012 82.445  13.977  1.00 22.54 ? 197  TRP A CA  1 
ATOM   1548 C C   . TRP A 1 197 ? 50.607 82.945  13.787  1.00 22.73 ? 197  TRP A C   1 
ATOM   1549 O O   . TRP A 1 197 ? 50.339 83.693  12.833  1.00 21.37 ? 197  TRP A O   1 
ATOM   1550 C CB  . TRP A 1 197 ? 52.988 83.649  13.946  1.00 23.51 ? 197  TRP A CB  1 
ATOM   1551 C CG  . TRP A 1 197 ? 54.341 83.250  14.300  1.00 23.40 ? 197  TRP A CG  1 
ATOM   1552 C CD1 . TRP A 1 197 ? 55.386 83.033  13.451  1.00 26.05 ? 197  TRP A CD1 1 
ATOM   1553 C CD2 . TRP A 1 197 ? 54.806 82.908  15.613  1.00 25.18 ? 197  TRP A CD2 1 
ATOM   1554 N NE1 . TRP A 1 197 ? 56.472 82.609  14.158  1.00 23.86 ? 197  TRP A NE1 1 
ATOM   1555 C CE2 . TRP A 1 197 ? 56.156 82.556  15.490  1.00 22.49 ? 197  TRP A CE2 1 
ATOM   1556 C CE3 . TRP A 1 197 ? 54.210 82.915  16.893  1.00 22.13 ? 197  TRP A CE3 1 
ATOM   1557 C CZ2 . TRP A 1 197 ? 56.950 82.187  16.607  1.00 26.50 ? 197  TRP A CZ2 1 
ATOM   1558 C CZ3 . TRP A 1 197 ? 54.995 82.573  18.000  1.00 24.67 ? 197  TRP A CZ3 1 
ATOM   1559 C CH2 . TRP A 1 197 ? 56.331 82.200  17.847  1.00 23.77 ? 197  TRP A CH2 1 
ATOM   1560 N N   . PRO A 1 198 ? 49.701 82.515  14.666  1.00 23.28 ? 198  PRO A N   1 
ATOM   1561 C CA  . PRO A 1 198 ? 48.365 83.065  14.452  1.00 22.46 ? 198  PRO A CA  1 
ATOM   1562 C C   . PRO A 1 198 ? 48.282 84.480  15.033  1.00 21.71 ? 198  PRO A C   1 
ATOM   1563 O O   . PRO A 1 198 ? 48.937 84.817  16.019  1.00 21.34 ? 198  PRO A O   1 
ATOM   1564 C CB  . PRO A 1 198 ? 47.490 82.064  15.204  1.00 22.26 ? 198  PRO A CB  1 
ATOM   1565 C CG  . PRO A 1 198 ? 48.335 81.694  16.403  1.00 23.51 ? 198  PRO A CG  1 
ATOM   1566 C CD  . PRO A 1 198 ? 49.729 81.562  15.815  1.00 23.04 ? 198  PRO A CD  1 
ATOM   1567 N N   . ILE A 1 199 ? 47.441 85.295  14.447  1.00 22.09 ? 199  ILE A N   1 
ATOM   1568 C CA  . ILE A 1 199 ? 47.211 86.625  14.949  1.00 22.94 ? 199  ILE A CA  1 
ATOM   1569 C C   . ILE A 1 199 ? 45.684 86.846  15.135  1.00 22.65 ? 199  ILE A C   1 
ATOM   1570 O O   . ILE A 1 199 ? 44.935 86.812  14.185  1.00 20.18 ? 199  ILE A O   1 
ATOM   1571 C CB  . ILE A 1 199 ? 47.781 87.649  13.917  1.00 22.84 ? 199  ILE A CB  1 
ATOM   1572 C CG1 . ILE A 1 199 ? 49.297 87.447  13.820  1.00 22.86 ? 199  ILE A CG1 1 
ATOM   1573 C CG2 . ILE A 1 199 ? 47.355 89.061  14.315  1.00 23.99 ? 199  ILE A CG2 1 
ATOM   1574 C CD1 . ILE A 1 199 ? 50.054 88.274  12.672  1.00 25.69 ? 199  ILE A CD1 1 
ATOM   1575 N N   . PHE A 1 200 ? 45.264 87.042  16.387  1.00 22.89 ? 200  PHE A N   1 
ATOM   1576 C CA  . PHE A 1 200 ? 43.897 87.264  16.724  1.00 23.47 ? 200  PHE A CA  1 
ATOM   1577 C C   . PHE A 1 200 ? 43.867 87.657  18.183  1.00 22.57 ? 200  PHE A C   1 
ATOM   1578 O O   . PHE A 1 200 ? 44.328 86.901  19.035  1.00 22.61 ? 200  PHE A O   1 
ATOM   1579 C CB  . PHE A 1 200 ? 43.088 85.985  16.468  1.00 24.40 ? 200  PHE A CB  1 
ATOM   1580 C CG  . PHE A 1 200 ? 41.613 86.162  16.641  1.00 25.22 ? 200  PHE A CG  1 
ATOM   1581 C CD1 . PHE A 1 200 ? 40.869 86.919  15.718  1.00 26.13 ? 200  PHE A CD1 1 
ATOM   1582 C CD2 . PHE A 1 200 ? 40.970 85.584  17.732  1.00 29.34 ? 200  PHE A CD2 1 
ATOM   1583 C CE1 . PHE A 1 200 ? 39.507 87.059  15.853  1.00 30.02 ? 200  PHE A CE1 1 
ATOM   1584 C CE2 . PHE A 1 200 ? 39.610 85.745  17.910  1.00 29.64 ? 200  PHE A CE2 1 
ATOM   1585 C CZ  . PHE A 1 200 ? 38.870 86.466  16.968  1.00 27.96 ? 200  PHE A CZ  1 
ATOM   1586 N N   . ASN A 1 201 ? 43.399 88.871  18.467  1.00 21.61 ? 201  ASN A N   1 
ATOM   1587 C CA  . ASN A 1 201 ? 43.616 89.455  19.790  1.00 21.18 ? 201  ASN A CA  1 
ATOM   1588 C C   . ASN A 1 201 ? 42.899 88.585  20.814  1.00 21.18 ? 201  ASN A C   1 
ATOM   1589 O O   . ASN A 1 201 ? 41.738 88.213  20.630  1.00 20.32 ? 201  ASN A O   1 
ATOM   1590 C CB  . ASN A 1 201 ? 43.100 90.869  19.829  1.00 20.37 ? 201  ASN A CB  1 
ATOM   1591 C CG  . ASN A 1 201 ? 43.875 91.770  18.877  1.00 21.14 ? 201  ASN A CG  1 
ATOM   1592 O OD1 . ASN A 1 201 ? 44.830 91.312  18.224  1.00 24.25 ? 201  ASN A OD1 1 
ATOM   1593 N ND2 . ASN A 1 201 ? 43.545 93.041  18.861  1.00 20.08 ? 201  ASN A ND2 1 
ATOM   1594 N N   . ARG A 1 202 ? 43.615 88.290  21.875  1.00 22.81 ? 202  ARG A N   1 
ATOM   1595 C CA  A ARG A 1 202 ? 43.202 87.300  22.853  0.50 23.57 ? 202  ARG A CA  1 
ATOM   1596 C CA  B ARG A 1 202 ? 43.234 87.250  22.838  0.50 22.66 ? 202  ARG A CA  1 
ATOM   1597 C C   . ARG A 1 202 ? 43.967 87.460  24.152  1.00 23.90 ? 202  ARG A C   1 
ATOM   1598 O O   . ARG A 1 202 ? 45.202 87.668  24.178  1.00 22.38 ? 202  ARG A O   1 
ATOM   1599 C CB  A ARG A 1 202 ? 43.382 85.872  22.324  0.50 23.90 ? 202  ARG A CB  1 
ATOM   1600 C CB  B ARG A 1 202 ? 43.531 85.838  22.281  0.50 22.32 ? 202  ARG A CB  1 
ATOM   1601 C CG  A ARG A 1 202 ? 42.582 84.863  23.157  0.50 26.39 ? 202  ARG A CG  1 
ATOM   1602 C CG  B ARG A 1 202 ? 43.358 84.665  23.298  0.50 20.64 ? 202  ARG A CG  1 
ATOM   1603 C CD  A ARG A 1 202 ? 43.333 83.636  23.396  0.50 27.75 ? 202  ARG A CD  1 
ATOM   1604 C CD  B ARG A 1 202 ? 41.878 84.438  23.693  0.50 16.04 ? 202  ARG A CD  1 
ATOM   1605 N NE  A ARG A 1 202 ? 42.776 82.891  24.521  0.50 30.48 ? 202  ARG A NE  1 
ATOM   1606 N NE  B ARG A 1 202 ? 41.744 83.654  24.915  0.50 15.70 ? 202  ARG A NE  1 
ATOM   1607 C CZ  A ARG A 1 202 ? 41.984 81.826  24.412  0.50 29.98 ? 202  ARG A CZ  1 
ATOM   1608 C CZ  B ARG A 1 202 ? 41.522 82.349  24.947  0.50 14.50 ? 202  ARG A CZ  1 
ATOM   1609 N NH1 A ARG A 1 202 ? 41.632 81.347  23.219  0.50 30.52 ? 202  ARG A NH1 1 
ATOM   1610 N NH1 B ARG A 1 202 ? 41.396 81.666  23.823  0.50 18.38 ? 202  ARG A NH1 1 
ATOM   1611 N NH2 A ARG A 1 202 ? 41.557 81.223  25.512  0.50 29.34 ? 202  ARG A NH2 1 
ATOM   1612 N NH2 B ARG A 1 202 ? 41.465 81.716  26.114  0.50 17.77 ? 202  ARG A NH2 1 
ATOM   1613 N N   . ASP A 1 203 ? 43.204 87.395  25.232  1.00 24.89 ? 203  ASP A N   1 
ATOM   1614 C CA  . ASP A 1 203 ? 43.695 87.462  26.571  1.00 27.04 ? 203  ASP A CA  1 
ATOM   1615 C C   . ASP A 1 203 ? 44.280 86.091  26.862  1.00 28.16 ? 203  ASP A C   1 
ATOM   1616 O O   . ASP A 1 203 ? 43.542 85.141  27.142  1.00 28.18 ? 203  ASP A O   1 
ATOM   1617 C CB  . ASP A 1 203 ? 42.513 87.679  27.527  1.00 27.26 ? 203  ASP A CB  1 
ATOM   1618 C CG  . ASP A 1 203 ? 42.966 87.871  28.961  1.00 30.87 ? 203  ASP A CG  1 
ATOM   1619 O OD1 . ASP A 1 203 ? 44.169 87.654  29.217  1.00 32.24 ? 203  ASP A OD1 1 
ATOM   1620 O OD2 . ASP A 1 203 ? 42.131 88.284  29.813  1.00 36.56 ? 203  ASP A OD2 1 
ATOM   1621 N N   . THR A 1 204 ? 45.591 85.967  26.760  1.00 29.03 ? 204  THR A N   1 
ATOM   1622 C CA  . THR A 1 204 ? 46.246 84.719  27.117  1.00 31.59 ? 204  THR A CA  1 
ATOM   1623 C C   . THR A 1 204 ? 47.559 85.060  27.707  1.00 31.60 ? 204  THR A C   1 
ATOM   1624 O O   . THR A 1 204 ? 48.033 86.173  27.531  1.00 31.85 ? 204  THR A O   1 
ATOM   1625 C CB  . THR A 1 204 ? 46.577 83.933  25.915  1.00 32.09 ? 204  THR A CB  1 
ATOM   1626 O OG1 . THR A 1 204 ? 47.065 84.806  24.894  1.00 38.80 ? 204  THR A OG1 1 
ATOM   1627 C CG2 . THR A 1 204 ? 45.404 83.291  25.419  1.00 36.50 ? 204  THR A CG2 1 
ATOM   1628 N N   . THR A 1 205 ? 48.198 84.077  28.324  1.00 31.32 ? 205  THR A N   1 
ATOM   1629 C CA  . THR A 1 205 ? 49.492 84.261  28.946  1.00 30.45 ? 205  THR A CA  1 
ATOM   1630 C C   . THR A 1 205 ? 50.632 84.294  27.950  1.00 30.22 ? 205  THR A C   1 
ATOM   1631 O O   . THR A 1 205 ? 50.755 83.395  27.136  1.00 29.58 ? 205  THR A O   1 
ATOM   1632 C CB  . THR A 1 205 ? 49.714 83.116  29.952  1.00 31.00 ? 205  THR A CB  1 
ATOM   1633 O OG1 . THR A 1 205 ? 48.592 83.100  30.840  1.00 33.16 ? 205  THR A OG1 1 
ATOM   1634 C CG2 . THR A 1 205 ? 50.983 83.307  30.753  1.00 28.42 ? 205  THR A CG2 1 
ATOM   1635 N N   . PRO A 1 206 ? 51.511 85.317  28.053  1.00 30.23 ? 206  PRO A N   1 
ATOM   1636 C CA  . PRO A 1 206 ? 52.677 85.359  27.219  1.00 30.69 ? 206  PRO A CA  1 
ATOM   1637 C C   . PRO A 1 206 ? 53.744 84.335  27.685  1.00 31.46 ? 206  PRO A C   1 
ATOM   1638 O O   . PRO A 1 206 ? 54.716 84.708  28.360  1.00 33.88 ? 206  PRO A O   1 
ATOM   1639 C CB  . PRO A 1 206 ? 53.195 86.797  27.401  1.00 30.04 ? 206  PRO A CB  1 
ATOM   1640 C CG  . PRO A 1 206 ? 52.147 87.518  28.274  1.00 31.85 ? 206  PRO A CG  1 
ATOM   1641 C CD  . PRO A 1 206 ? 51.432 86.473  28.983  1.00 29.55 ? 206  PRO A CD  1 
ATOM   1642 N N   . ASN A 1 207 ? 53.603 83.083  27.263  1.00 31.29 ? 207  ASN A N   1 
ATOM   1643 C CA  . ASN A 1 207 ? 54.471 81.989  27.716  1.00 30.20 ? 207  ASN A CA  1 
ATOM   1644 C C   . ASN A 1 207 ? 55.209 81.384  26.526  1.00 29.66 ? 207  ASN A C   1 
ATOM   1645 O O   . ASN A 1 207 ? 55.241 81.979  25.440  1.00 29.38 ? 207  ASN A O   1 
ATOM   1646 C CB  . ASN A 1 207 ? 53.606 80.938  28.433  1.00 31.20 ? 207  ASN A CB  1 
ATOM   1647 C CG  . ASN A 1 207 ? 52.494 80.395  27.543  1.00 31.35 ? 207  ASN A CG  1 
ATOM   1648 O OD1 . ASN A 1 207 ? 52.603 80.438  26.323  1.00 32.59 ? 207  ASN A OD1 1 
ATOM   1649 N ND2 . ASN A 1 207 ? 51.426 79.884  28.147  1.00 33.19 ? 207  ASN A ND2 1 
ATOM   1650 N N   . GLY A 1 208 ? 55.782 80.192  26.712  1.00 28.24 ? 208  GLY A N   1 
ATOM   1651 C CA  . GLY A 1 208 ? 56.521 79.505  25.669  1.00 28.76 ? 208  GLY A CA  1 
ATOM   1652 C C   . GLY A 1 208 ? 55.717 78.845  24.567  1.00 28.13 ? 208  GLY A C   1 
ATOM   1653 O O   . GLY A 1 208 ? 56.302 78.271  23.672  1.00 28.33 ? 208  GLY A O   1 
ATOM   1654 N N   . ASN A 1 209 ? 54.390 78.915  24.622  1.00 28.02 ? 209  ASN A N   1 
ATOM   1655 C CA  . ASN A 1 209 ? 53.546 78.195  23.660  1.00 27.99 ? 209  ASN A CA  1 
ATOM   1656 C C   . ASN A 1 209 ? 53.322 78.807  22.310  1.00 27.54 ? 209  ASN A C   1 
ATOM   1657 O O   . ASN A 1 209 ? 52.620 78.203  21.496  1.00 28.04 ? 209  ASN A O   1 
ATOM   1658 C CB  . ASN A 1 209 ? 52.179 77.915  24.247  1.00 28.31 ? 209  ASN A CB  1 
ATOM   1659 C CG  . ASN A 1 209 ? 52.234 76.885  25.335  1.00 34.30 ? 209  ASN A CG  1 
ATOM   1660 O OD1 . ASN A 1 209 ? 52.664 75.748  25.096  1.00 39.54 ? 209  ASN A OD1 1 
ATOM   1661 N ND2 . ASN A 1 209 ? 51.840 77.277  26.540  1.00 40.89 ? 209  ASN A ND2 1 
ATOM   1662 N N   . GLY A 1 210 ? 53.828 80.010  22.062  1.00 26.11 ? 210  GLY A N   1 
ATOM   1663 C CA  . GLY A 1 210 ? 53.730 80.545  20.688  1.00 25.56 ? 210  GLY A CA  1 
ATOM   1664 C C   . GLY A 1 210 ? 52.325 80.902  20.221  1.00 25.38 ? 210  GLY A C   1 
ATOM   1665 O O   . GLY A 1 210 ? 52.039 80.864  19.016  1.00 26.49 ? 210  GLY A O   1 
ATOM   1666 N N   . THR A 1 211 ? 51.436 81.268  21.148  1.00 25.49 ? 211  THR A N   1 
ATOM   1667 C CA  . THR A 1 211 ? 50.059 81.602  20.770  1.00 25.93 ? 211  THR A CA  1 
ATOM   1668 C C   . THR A 1 211 ? 49.882 83.068  20.315  1.00 24.84 ? 211  THR A C   1 
ATOM   1669 O O   . THR A 1 211 ? 50.759 83.918  20.530  1.00 24.61 ? 211  THR A O   1 
ATOM   1670 C CB  . THR A 1 211 ? 49.016 81.265  21.880  1.00 26.22 ? 211  THR A CB  1 
ATOM   1671 O OG1 . THR A 1 211 ? 49.013 82.282  22.899  1.00 26.89 ? 211  THR A OG1 1 
ATOM   1672 C CG2 . THR A 1 211 ? 49.334 79.907  22.537  1.00 25.37 ? 211  THR A CG2 1 
ATOM   1673 N N   . ASN A 1 212 ? 48.756 83.310  19.658  1.00 24.14 ? 212  ASN A N   1 
ATOM   1674 C CA  . ASN A 1 212 ? 48.178 84.636  19.524  1.00 22.96 ? 212  ASN A CA  1 
ATOM   1675 C C   . ASN A 1 212 ? 48.037 85.270  20.904  1.00 23.11 ? 212  ASN A C   1 
ATOM   1676 O O   . ASN A 1 212 ? 47.616 84.607  21.876  1.00 22.39 ? 212  ASN A O   1 
ATOM   1677 C CB  . ASN A 1 212 ? 46.832 84.572  18.777  1.00 22.41 ? 212  ASN A CB  1 
ATOM   1678 C CG  . ASN A 1 212 ? 45.836 83.590  19.402  1.00 23.55 ? 212  ASN A CG  1 
ATOM   1679 O OD1 . ASN A 1 212 ? 46.140 82.404  19.622  1.00 20.91 ? 212  ASN A OD1 1 
ATOM   1680 N ND2 . ASN A 1 212 ? 44.638 84.093  19.695  1.00 18.06 ? 212  ASN A ND2 1 
ATOM   1681 N N   . LEU A 1 213 ? 48.459 86.534  21.025  1.00 20.77 ? 213  LEU A N   1 
ATOM   1682 C CA  . LEU A 1 213 ? 48.299 87.255  22.266  1.00 21.27 ? 213  LEU A CA  1 
ATOM   1683 C C   . LEU A 1 213 ? 47.419 88.449  22.034  1.00 20.05 ? 213  LEU A C   1 
ATOM   1684 O O   . LEU A 1 213 ? 46.505 88.382  21.232  1.00 21.02 ? 213  LEU A O   1 
ATOM   1685 C CB  . LEU A 1 213 ? 49.655 87.657  22.869  1.00 20.75 ? 213  LEU A CB  1 
ATOM   1686 C CG  . LEU A 1 213 ? 50.581 86.447  23.160  1.00 23.60 ? 213  LEU A CG  1 
ATOM   1687 C CD1 . LEU A 1 213 ? 51.905 86.921  23.671  1.00 19.82 ? 213  LEU A CD1 1 
ATOM   1688 C CD2 . LEU A 1 213 ? 49.933 85.519  24.204  1.00 24.17 ? 213  LEU A CD2 1 
ATOM   1689 N N   . TYR A 1 214 ? 47.707 89.554  22.699  1.00 19.85 ? 214  TYR A N   1 
ATOM   1690 C CA  . TYR A 1 214 ? 46.662 90.573  22.928  1.00 21.73 ? 214  TYR A CA  1 
ATOM   1691 C C   . TYR A 1 214 ? 46.454 91.480  21.761  1.00 22.10 ? 214  TYR A C   1 
ATOM   1692 O O   . TYR A 1 214 ? 45.393 92.104  21.648  1.00 23.47 ? 214  TYR A O   1 
ATOM   1693 C CB  . TYR A 1 214 ? 47.040 91.459  24.089  1.00 22.63 ? 214  TYR A CB  1 
ATOM   1694 C CG  . TYR A 1 214 ? 47.486 90.715  25.308  1.00 23.96 ? 214  TYR A CG  1 
ATOM   1695 C CD1 . TYR A 1 214 ? 46.563 90.111  26.170  1.00 24.23 ? 214  TYR A CD1 1 
ATOM   1696 C CD2 . TYR A 1 214 ? 48.811 90.645  25.622  1.00 22.67 ? 214  TYR A CD2 1 
ATOM   1697 C CE1 . TYR A 1 214 ? 47.001 89.430  27.339  1.00 25.65 ? 214  TYR A CE1 1 
ATOM   1698 C CE2 . TYR A 1 214 ? 49.266 89.949  26.765  1.00 27.95 ? 214  TYR A CE2 1 
ATOM   1699 C CZ  . TYR A 1 214 ? 48.350 89.355  27.617  1.00 26.94 ? 214  TYR A CZ  1 
ATOM   1700 O OH  . TYR A 1 214 ? 48.821 88.724  28.774  1.00 26.21 ? 214  TYR A OH  1 
ATOM   1701 N N   . GLY A 1 215 ? 47.495 91.608  20.943  1.00 21.27 ? 215  GLY A N   1 
ATOM   1702 C CA  . GLY A 1 215 ? 47.497 92.551  19.826  1.00 20.45 ? 215  GLY A CA  1 
ATOM   1703 C C   . GLY A 1 215 ? 47.738 91.939  18.467  1.00 20.42 ? 215  GLY A C   1 
ATOM   1704 O O   . GLY A 1 215 ? 48.130 90.772  18.343  1.00 20.35 ? 215  GLY A O   1 
ATOM   1705 N N   . ALA A 1 216 ? 47.474 92.726  17.417  1.00 19.54 ? 216  ALA A N   1 
ATOM   1706 C CA  . ALA A 1 216 ? 47.558 92.215  16.070  1.00 18.50 ? 216  ALA A CA  1 
ATOM   1707 C C   . ALA A 1 216 ? 48.506 93.122  15.263  1.00 19.69 ? 216  ALA A C   1 
ATOM   1708 O O   . ALA A 1 216 ? 48.132 94.241  14.966  1.00 19.71 ? 216  ALA A O   1 
ATOM   1709 C CB  . ALA A 1 216 ? 46.210 92.268  15.411  1.00 18.51 ? 216  ALA A CB  1 
ATOM   1710 N N   . GLN A 1 217 ? 49.656 92.604  14.843  1.00 18.75 ? 217  GLN A N   1 
ATOM   1711 C CA  . GLN A 1 217 ? 50.641 93.413  14.135  1.00 19.11 ? 217  GLN A CA  1 
ATOM   1712 C C   . GLN A 1 217 ? 51.189 92.631  12.950  1.00 20.55 ? 217  GLN A C   1 
ATOM   1713 O O   . GLN A 1 217 ? 51.918 91.658  13.146  1.00 23.12 ? 217  GLN A O   1 
ATOM   1714 C CB  . GLN A 1 217 ? 51.795 93.800  15.102  1.00 17.36 ? 217  GLN A CB  1 
ATOM   1715 C CG  . GLN A 1 217 ? 51.402 94.566  16.368  1.00 18.57 ? 217  GLN A CG  1 
ATOM   1716 C CD  . GLN A 1 217 ? 51.002 96.016  16.130  1.00 23.15 ? 217  GLN A CD  1 
ATOM   1717 O OE1 . GLN A 1 217 ? 51.293 96.594  15.060  1.00 22.05 ? 217  GLN A OE1 1 
ATOM   1718 N NE2 . GLN A 1 217 ? 50.324 96.624  17.119  1.00 22.16 ? 217  GLN A NE2 1 
ATOM   1719 N N   . THR A 1 218 ? 50.862 93.025  11.727  1.00 19.97 ? 218  THR A N   1 
ATOM   1720 C CA  . THR A 1 218 ? 51.298 92.258  10.577  1.00 21.39 ? 218  THR A CA  1 
ATOM   1721 C C   . THR A 1 218 ? 52.617 92.777  9.949   1.00 21.02 ? 218  THR A C   1 
ATOM   1722 O O   . THR A 1 218 ? 53.180 92.146  9.069   1.00 22.34 ? 218  THR A O   1 
ATOM   1723 C CB  . THR A 1 218 ? 50.217 92.245  9.499   1.00 22.45 ? 218  THR A CB  1 
ATOM   1724 O OG1 . THR A 1 218 ? 49.952 93.592  9.131   1.00 24.90 ? 218  THR A OG1 1 
ATOM   1725 C CG2 . THR A 1 218 ? 48.884 91.632  10.026  1.00 21.26 ? 218  THR A CG2 1 
ATOM   1726 N N   . PHE A 1 219 ? 53.129 93.885  10.431  1.00 20.90 ? 219  PHE A N   1 
ATOM   1727 C CA  . PHE A 1 219 ? 54.356 94.443  9.845   1.00 19.82 ? 219  PHE A CA  1 
ATOM   1728 C C   . PHE A 1 219 ? 55.554 93.541  10.096  1.00 20.82 ? 219  PHE A C   1 
ATOM   1729 O O   . PHE A 1 219 ? 55.743 93.039  11.222  1.00 20.71 ? 219  PHE A O   1 
ATOM   1730 C CB  . PHE A 1 219 ? 54.632 95.770  10.496  1.00 19.77 ? 219  PHE A CB  1 
ATOM   1731 C CG  . PHE A 1 219 ? 55.907 96.405  10.034  1.00 19.52 ? 219  PHE A CG  1 
ATOM   1732 C CD1 . PHE A 1 219 ? 56.046 96.815  8.707   1.00 19.30 ? 219  PHE A CD1 1 
ATOM   1733 C CD2 . PHE A 1 219 ? 56.971 96.576  10.930  1.00 22.29 ? 219  PHE A CD2 1 
ATOM   1734 C CE1 . PHE A 1 219 ? 57.253 97.423  8.274   1.00 19.35 ? 219  PHE A CE1 1 
ATOM   1735 C CE2 . PHE A 1 219 ? 58.183 97.190  10.506  1.00 23.13 ? 219  PHE A CE2 1 
ATOM   1736 C CZ  . PHE A 1 219 ? 58.306 97.595  9.173   1.00 18.48 ? 219  PHE A CZ  1 
ATOM   1737 N N   . PHE A 1 220 ? 56.342 93.280  9.059   1.00 19.92 ? 220  PHE A N   1 
ATOM   1738 C CA  . PHE A 1 220 ? 57.710 92.826  9.310   1.00 21.18 ? 220  PHE A CA  1 
ATOM   1739 C C   . PHE A 1 220 ? 58.693 93.624  8.459   1.00 21.78 ? 220  PHE A C   1 
ATOM   1740 O O   . PHE A 1 220 ? 58.292 94.243  7.462   1.00 19.30 ? 220  PHE A O   1 
ATOM   1741 C CB  . PHE A 1 220 ? 57.903 91.328  9.021   1.00 22.39 ? 220  PHE A CB  1 
ATOM   1742 C CG  . PHE A 1 220 ? 57.843 90.994  7.577   1.00 25.30 ? 220  PHE A CG  1 
ATOM   1743 C CD1 . PHE A 1 220 ? 58.990 91.029  6.778   1.00 27.24 ? 220  PHE A CD1 1 
ATOM   1744 C CD2 . PHE A 1 220 ? 56.640 90.627  7.000   1.00 24.75 ? 220  PHE A CD2 1 
ATOM   1745 C CE1 . PHE A 1 220 ? 58.916 90.733  5.431   1.00 28.01 ? 220  PHE A CE1 1 
ATOM   1746 C CE2 . PHE A 1 220 ? 56.571 90.331  5.648   1.00 26.95 ? 220  PHE A CE2 1 
ATOM   1747 C CZ  . PHE A 1 220 ? 57.698 90.369  4.868   1.00 26.03 ? 220  PHE A CZ  1 
ATOM   1748 N N   . LEU A 1 221 ? 59.969 93.545  8.881   1.00 20.65 ? 221  LEU A N   1 
ATOM   1749 C CA  . LEU A 1 221 ? 61.104 94.267  8.312   1.00 22.24 ? 221  LEU A CA  1 
ATOM   1750 C C   . LEU A 1 221 ? 62.127 93.179  7.909   1.00 21.37 ? 221  LEU A C   1 
ATOM   1751 O O   . LEU A 1 221 ? 62.331 92.211  8.635   1.00 21.34 ? 221  LEU A O   1 
ATOM   1752 C CB  . LEU A 1 221 ? 61.747 95.156  9.391   1.00 22.07 ? 221  LEU A CB  1 
ATOM   1753 C CG  . LEU A 1 221 ? 62.917 96.049  8.954   1.00 24.89 ? 221  LEU A CG  1 
ATOM   1754 C CD1 . LEU A 1 221 ? 62.827 97.296  9.799   1.00 24.11 ? 221  LEU A CD1 1 
ATOM   1755 C CD2 . LEU A 1 221 ? 64.295 95.306  9.138   1.00 24.59 ? 221  LEU A CD2 1 
ATOM   1756 N N   . CYS A 1 222 ? 62.714 93.337  6.741   1.00 21.90 ? 222  CYS A N   1 
ATOM   1757 C CA  . CYS A 1 222 ? 63.709 92.391  6.226   1.00 22.24 ? 222  CYS A CA  1 
ATOM   1758 C C   . CYS A 1 222 ? 64.997 93.154  5.915   1.00 22.44 ? 222  CYS A C   1 
ATOM   1759 O O   . CYS A 1 222 ? 64.984 94.055  5.099   1.00 22.60 ? 222  CYS A O   1 
ATOM   1760 C CB  . CYS A 1 222 ? 63.160 91.697  4.977   1.00 21.75 ? 222  CYS A CB  1 
ATOM   1761 S SG  . CYS A 1 222 ? 64.437 90.573  4.295   1.00 25.98 ? 222  CYS A SG  1 
ATOM   1762 N N   . LEU A 1 223 ? 66.093 92.807  6.581   1.00 22.92 ? 223  LEU A N   1 
ATOM   1763 C CA  . LEU A 1 223 ? 67.408 93.375  6.262   1.00 22.98 ? 223  LEU A CA  1 
ATOM   1764 C C   . LEU A 1 223 ? 67.979 92.511  5.119   1.00 23.67 ? 223  LEU A C   1 
ATOM   1765 O O   . LEU A 1 223 ? 68.311 91.332  5.313   1.00 24.85 ? 223  LEU A O   1 
ATOM   1766 C CB  . LEU A 1 223 ? 68.318 93.266  7.470   1.00 22.77 ? 223  LEU A CB  1 
ATOM   1767 C CG  . LEU A 1 223 ? 69.817 93.581  7.240   1.00 21.81 ? 223  LEU A CG  1 
ATOM   1768 C CD1 . LEU A 1 223 ? 70.003 95.008  6.793   1.00 23.28 ? 223  LEU A CD1 1 
ATOM   1769 C CD2 . LEU A 1 223 ? 70.607 93.280  8.504   1.00 22.22 ? 223  LEU A CD2 1 
ATOM   1770 N N   . GLU A 1 224 ? 68.106 93.104  3.950   1.00 24.71 ? 224  GLU A N   1 
ATOM   1771 C CA  . GLU A 1 224 ? 68.407 92.349  2.731   1.00 27.57 ? 224  GLU A CA  1 
ATOM   1772 C C   . GLU A 1 224 ? 69.873 91.871  2.724   1.00 28.77 ? 224  GLU A C   1 
ATOM   1773 O O   . GLU A 1 224 ? 70.148 90.738  2.329   1.00 29.92 ? 224  GLU A O   1 
ATOM   1774 C CB  . GLU A 1 224 ? 68.107 93.191  1.477   1.00 26.52 ? 224  GLU A CB  1 
ATOM   1775 C CG  . GLU A 1 224 ? 66.657 93.744  1.386   1.00 30.16 ? 224  GLU A CG  1 
ATOM   1776 C CD  . GLU A 1 224 ? 66.553 94.993  0.481   1.00 28.73 ? 224  GLU A CD  1 
ATOM   1777 O OE1 . GLU A 1 224 ? 67.356 95.145  -0.488  1.00 31.01 ? 224  GLU A OE1 1 
ATOM   1778 O OE2 . GLU A 1 224 ? 65.657 95.830  0.721   1.00 32.49 ? 224  GLU A OE2 1 
ATOM   1779 N N   . ASP A 1 225 ? 70.800 92.723  3.180   1.00 29.39 ? 225  ASP A N   1 
ATOM   1780 C CA  . ASP A 1 225 ? 72.206 92.344  3.236   1.00 29.81 ? 225  ASP A CA  1 
ATOM   1781 C C   . ASP A 1 225 ? 72.994 93.335  4.113   1.00 28.72 ? 225  ASP A C   1 
ATOM   1782 O O   . ASP A 1 225 ? 72.445 94.318  4.617   1.00 26.92 ? 225  ASP A O   1 
ATOM   1783 C CB  . ASP A 1 225 ? 72.793 92.239  1.792   1.00 31.02 ? 225  ASP A CB  1 
ATOM   1784 C CG  . ASP A 1 225 ? 72.618 93.515  0.985   1.00 35.23 ? 225  ASP A CG  1 
ATOM   1785 O OD1 . ASP A 1 225 ? 73.139 94.574  1.402   1.00 40.89 ? 225  ASP A OD1 1 
ATOM   1786 O OD2 . ASP A 1 225 ? 71.898 93.515  -0.050  1.00 43.84 ? 225  ASP A OD2 1 
ATOM   1787 N N   . ALA A 1 226 ? 74.286 93.075  4.275   1.00 27.42 ? 226  ALA A N   1 
ATOM   1788 C CA  . ALA A 1 226 ? 75.181 93.910  5.086   1.00 27.41 ? 226  ALA A CA  1 
ATOM   1789 C C   . ALA A 1 226 ? 75.314 95.373  4.659   1.00 26.95 ? 226  ALA A C   1 
ATOM   1790 O O   . ALA A 1 226 ? 75.850 96.184  5.415   1.00 28.28 ? 226  ALA A O   1 
ATOM   1791 C CB  . ALA A 1 226 ? 76.572 93.267  5.164   1.00 26.79 ? 226  ALA A CB  1 
ATOM   1792 N N   . SER A 1 227 ? 74.901 95.738  3.462   1.00 26.34 ? 227  SER A N   1 
ATOM   1793 C CA  . SER A 1 227 ? 74.910 97.149  3.112   1.00 26.61 ? 227  SER A CA  1 
ATOM   1794 C C   . SER A 1 227 ? 73.821 97.937  3.886   1.00 26.18 ? 227  SER A C   1 
ATOM   1795 O O   . SER A 1 227 ? 73.864 99.158  3.952   1.00 26.98 ? 227  SER A O   1 
ATOM   1796 C CB  . SER A 1 227 ? 74.673 97.354  1.615   1.00 27.60 ? 227  SER A CB  1 
ATOM   1797 O OG  . SER A 1 227 ? 73.339 96.990  1.287   1.00 28.71 ? 227  SER A OG  1 
ATOM   1798 N N   . GLY A 1 228 ? 72.819 97.247  4.405   1.00 26.48 ? 228  GLY A N   1 
ATOM   1799 C CA  . GLY A 1 228 ? 71.829 97.896  5.265   1.00 25.15 ? 228  GLY A CA  1 
ATOM   1800 C C   . GLY A 1 228 ? 70.502 98.001  4.558   1.00 25.05 ? 228  GLY A C   1 
ATOM   1801 O O   . GLY A 1 228 ? 69.491 98.277  5.214   1.00 23.61 ? 228  GLY A O   1 
ATOM   1802 N N   . LEU A 1 229 ? 70.509 97.825  3.217   1.00 23.80 ? 229  LEU A N   1 
ATOM   1803 C CA  . LEU A 1 229 ? 69.311 97.968  2.401   1.00 22.92 ? 229  LEU A CA  1 
ATOM   1804 C C   . LEU A 1 229 ? 68.260 97.033  3.001   1.00 22.15 ? 229  LEU A C   1 
ATOM   1805 O O   . LEU A 1 229 ? 68.585 95.908  3.330   1.00 21.03 ? 229  LEU A O   1 
ATOM   1806 C CB  . LEU A 1 229 ? 69.591 97.574  0.955   1.00 22.80 ? 229  LEU A CB  1 
ATOM   1807 C CG  . LEU A 1 229 ? 70.554 98.467  0.160   1.00 24.13 ? 229  LEU A CG  1 
ATOM   1808 C CD1 . LEU A 1 229 ? 70.580 97.942  -1.284  1.00 24.02 ? 229  LEU A CD1 1 
ATOM   1809 C CD2 . LEU A 1 229 ? 70.144 99.902  0.150   1.00 24.91 ? 229  LEU A CD2 1 
ATOM   1810 N N   . SER A 1 230 ? 67.039 97.550  3.198   1.00 20.98 ? 230  SER A N   1 
ATOM   1811 C CA  . SER A 1 230 ? 66.041 96.827  3.930   1.00 21.56 ? 230  SER A CA  1 
ATOM   1812 C C   . SER A 1 230 ? 64.697 97.155  3.329   1.00 20.11 ? 230  SER A C   1 
ATOM   1813 O O   . SER A 1 230 ? 64.515 98.151  2.616   1.00 19.16 ? 230  SER A O   1 
ATOM   1814 C CB  . SER A 1 230 ? 66.048 97.209  5.449   1.00 20.46 ? 230  SER A CB  1 
ATOM   1815 O OG  . SER A 1 230 ? 67.307 96.924  6.044   1.00 25.77 ? 230  SER A OG  1 
ATOM   1816 N N   . PHE A 1 231 ? 63.742 96.312  3.614   1.00 20.06 ? 231  PHE A N   1 
ATOM   1817 C CA  . PHE A 1 231 ? 62.375 96.642  3.174   1.00 20.33 ? 231  PHE A CA  1 
ATOM   1818 C C   . PHE A 1 231 ? 61.409 96.118  4.200   1.00 20.44 ? 231  PHE A C   1 
ATOM   1819 O O   . PHE A 1 231 ? 61.837 95.391  5.085   1.00 19.53 ? 231  PHE A O   1 
ATOM   1820 C CB  . PHE A 1 231 ? 62.064 96.106  1.754   1.00 21.25 ? 231  PHE A CB  1 
ATOM   1821 C CG  . PHE A 1 231 ? 61.783 94.654  1.704   1.00 21.02 ? 231  PHE A CG  1 
ATOM   1822 C CD1 . PHE A 1 231 ? 60.487 94.195  1.563   1.00 22.25 ? 231  PHE A CD1 1 
ATOM   1823 C CD2 . PHE A 1 231 ? 62.824 93.742  1.746   1.00 24.19 ? 231  PHE A CD2 1 
ATOM   1824 C CE1 . PHE A 1 231 ? 60.219 92.835  1.516   1.00 24.47 ? 231  PHE A CE1 1 
ATOM   1825 C CE2 . PHE A 1 231 ? 62.576 92.398  1.679   1.00 25.09 ? 231  PHE A CE2 1 
ATOM   1826 C CZ  . PHE A 1 231 ? 61.287 91.929  1.569   1.00 21.95 ? 231  PHE A CZ  1 
ATOM   1827 N N   . GLY A 1 232 ? 60.135 96.549  4.110   1.00 19.53 ? 232  GLY A N   1 
ATOM   1828 C CA  . GLY A 1 232 ? 59.114 96.147  5.066   1.00 20.33 ? 232  GLY A CA  1 
ATOM   1829 C C   . GLY A 1 232 ? 57.862 95.829  4.303   1.00 19.48 ? 232  GLY A C   1 
ATOM   1830 O O   . GLY A 1 232 ? 57.648 96.338  3.195   1.00 19.52 ? 232  GLY A O   1 
ATOM   1831 N N   . VAL A 1 233 ? 57.039 95.005  4.894   1.00 19.45 ? 233  VAL A N   1 
ATOM   1832 C CA  . VAL A 1 233 ? 55.717 94.671  4.345   1.00 19.35 ? 233  VAL A CA  1 
ATOM   1833 C C   . VAL A 1 233 ? 54.688 94.810  5.469   1.00 21.81 ? 233  VAL A C   1 
ATOM   1834 O O   . VAL A 1 233 ? 54.949 94.357  6.572   1.00 21.56 ? 233  VAL A O   1 
ATOM   1835 C CB  . VAL A 1 233 ? 55.673 93.235  3.783   1.00 19.42 ? 233  VAL A CB  1 
ATOM   1836 C CG1 . VAL A 1 233 ? 54.231 92.828  3.399   1.00 19.56 ? 233  VAL A CG1 1 
ATOM   1837 C CG2 . VAL A 1 233 ? 56.530 93.124  2.545   1.00 20.78 ? 233  VAL A CG2 1 
ATOM   1838 N N   . PHE A 1 234 ? 53.567 95.484  5.174   1.00 19.58 ? 234  PHE A N   1 
ATOM   1839 C CA  . PHE A 1 234 ? 52.465 95.624  6.065   1.00 21.15 ? 234  PHE A CA  1 
ATOM   1840 C C   . PHE A 1 234 ? 51.174 95.148  5.349   1.00 20.71 ? 234  PHE A C   1 
ATOM   1841 O O   . PHE A 1 234 ? 50.905 95.526  4.204   1.00 20.55 ? 234  PHE A O   1 
ATOM   1842 C CB  . PHE A 1 234 ? 52.318 97.077  6.481   1.00 20.20 ? 234  PHE A CB  1 
ATOM   1843 C CG  . PHE A 1 234 ? 51.097 97.326  7.261   1.00 20.38 ? 234  PHE A CG  1 
ATOM   1844 C CD1 . PHE A 1 234 ? 50.871 96.639  8.461   1.00 18.73 ? 234  PHE A CD1 1 
ATOM   1845 C CD2 . PHE A 1 234 ? 50.185 98.249  6.826   1.00 19.66 ? 234  PHE A CD2 1 
ATOM   1846 C CE1 . PHE A 1 234 ? 49.733 96.866  9.171   1.00 22.06 ? 234  PHE A CE1 1 
ATOM   1847 C CE2 . PHE A 1 234 ? 49.019 98.480  7.564   1.00 23.42 ? 234  PHE A CE2 1 
ATOM   1848 C CZ  . PHE A 1 234 ? 48.799 97.787  8.710   1.00 20.50 ? 234  PHE A CZ  1 
ATOM   1849 N N   . LEU A 1 235 ? 50.415 94.298  6.027   1.00 20.32 ? 235  LEU A N   1 
ATOM   1850 C CA  . LEU A 1 235 ? 49.080 93.901  5.572   1.00 21.27 ? 235  LEU A CA  1 
ATOM   1851 C C   . LEU A 1 235 ? 47.990 94.606  6.393   1.00 21.41 ? 235  LEU A C   1 
ATOM   1852 O O   . LEU A 1 235 ? 47.871 94.399  7.623   1.00 21.98 ? 235  LEU A O   1 
ATOM   1853 C CB  . LEU A 1 235 ? 48.947 92.397  5.671   1.00 20.73 ? 235  LEU A CB  1 
ATOM   1854 C CG  . LEU A 1 235 ? 47.585 91.777  5.326   1.00 23.75 ? 235  LEU A CG  1 
ATOM   1855 C CD1 . LEU A 1 235 ? 47.053 92.160  3.924   1.00 21.23 ? 235  LEU A CD1 1 
ATOM   1856 C CD2 . LEU A 1 235 ? 47.684 90.243  5.545   1.00 23.71 ? 235  LEU A CD2 1 
ATOM   1857 N N   . MET A 1 236 ? 47.229 95.466  5.742   1.00 19.63 ? 236  MET A N   1 
ATOM   1858 C CA  . MET A 1 236 ? 46.121 96.144  6.404   1.00 21.89 ? 236  MET A CA  1 
ATOM   1859 C C   . MET A 1 236 ? 44.892 95.204  6.360   1.00 22.55 ? 236  MET A C   1 
ATOM   1860 O O   . MET A 1 236 ? 44.141 95.192  5.371   1.00 23.07 ? 236  MET A O   1 
ATOM   1861 C CB  . MET A 1 236 ? 45.811 97.442  5.667   1.00 22.82 ? 236  MET A CB  1 
ATOM   1862 C CG  . MET A 1 236 ? 44.639 98.239  6.272   1.00 23.52 ? 236  MET A CG  1 
ATOM   1863 S SD  . MET A 1 236 ? 44.934 98.916  7.927   1.00 30.68 ? 236  MET A SD  1 
ATOM   1864 C CE  . MET A 1 236 ? 45.868 100.389 7.459   1.00 30.01 ? 236  MET A CE  1 
ATOM   1865 N N   . ASN A 1 237 ? 44.723 94.391  7.409   1.00 23.06 ? 237  ASN A N   1 
ATOM   1866 C CA  . ASN A 1 237 ? 43.653 93.391  7.446   1.00 23.11 ? 237  ASN A CA  1 
ATOM   1867 C C   . ASN A 1 237 ? 43.468 93.095  8.943   1.00 23.56 ? 237  ASN A C   1 
ATOM   1868 O O   . ASN A 1 237 ? 44.448 92.969  9.688   1.00 24.65 ? 237  ASN A O   1 
ATOM   1869 C CB  . ASN A 1 237 ? 43.989 92.131  6.589   1.00 22.20 ? 237  ASN A CB  1 
ATOM   1870 C CG  . ASN A 1 237 ? 42.830 91.063  6.581   1.00 24.23 ? 237  ASN A CG  1 
ATOM   1871 O OD1 . ASN A 1 237 ? 42.621 90.396  7.579   1.00 26.15 ? 237  ASN A OD1 1 
ATOM   1872 N ND2 . ASN A 1 237 ? 42.144 90.884  5.446   1.00 20.71 ? 237  ASN A ND2 1 
ATOM   1873 N N   . SER A 1 238 ? 42.224 93.072  9.407   1.00 24.05 ? 238  SER A N   1 
ATOM   1874 C CA  . SER A 1 238 ? 41.931 92.912  10.833  1.00 22.65 ? 238  SER A CA  1 
ATOM   1875 C C   . SER A 1 238 ? 41.163 91.608  11.150  1.00 24.11 ? 238  SER A C   1 
ATOM   1876 O O   . SER A 1 238 ? 40.715 91.399  12.300  1.00 24.13 ? 238  SER A O   1 
ATOM   1877 C CB  . SER A 1 238 ? 41.158 94.147  11.318  1.00 22.80 ? 238  SER A CB  1 
ATOM   1878 O OG  . SER A 1 238 ? 39.964 94.305  10.572  1.00 24.11 ? 238  SER A OG  1 
ATOM   1879 N N   . ASN A 1 239 ? 41.003 90.740  10.156  1.00 22.74 ? 239  ASN A N   1 
ATOM   1880 C CA  . ASN A 1 239 ? 40.411 89.430  10.382  1.00 24.72 ? 239  ASN A CA  1 
ATOM   1881 C C   . ASN A 1 239 ? 41.428 88.482  11.031  1.00 25.24 ? 239  ASN A C   1 
ATOM   1882 O O   . ASN A 1 239 ? 42.654 88.755  11.002  1.00 23.86 ? 239  ASN A O   1 
ATOM   1883 C CB  . ASN A 1 239 ? 39.895 88.850  9.068   1.00 24.55 ? 239  ASN A CB  1 
ATOM   1884 C CG  . ASN A 1 239 ? 38.681 89.588  8.558   1.00 26.65 ? 239  ASN A CG  1 
ATOM   1885 O OD1 . ASN A 1 239 ? 37.532 89.207  8.812   1.00 29.42 ? 239  ASN A OD1 1 
ATOM   1886 N ND2 . ASN A 1 239 ? 38.920 90.650  7.831   1.00 23.80 ? 239  ASN A ND2 1 
ATOM   1887 N N   . ALA A 1 240 ? 40.938 87.390  11.631  1.00 23.64 ? 240  ALA A N   1 
ATOM   1888 C CA  . ALA A 1 240 ? 41.832 86.391  12.206  1.00 23.11 ? 240  ALA A CA  1 
ATOM   1889 C C   . ALA A 1 240 ? 42.745 85.918  11.113  1.00 23.37 ? 240  ALA A C   1 
ATOM   1890 O O   . ALA A 1 240 ? 42.339 85.751  9.974   1.00 23.17 ? 240  ALA A O   1 
ATOM   1891 C CB  . ALA A 1 240 ? 41.036 85.186  12.782  1.00 23.92 ? 240  ALA A CB  1 
ATOM   1892 N N   . MET A 1 241 ? 44.010 85.703  11.434  1.00 22.61 ? 241  MET A N   1 
ATOM   1893 C CA  . MET A 1 241 ? 44.903 85.369  10.359  1.00 25.07 ? 241  MET A CA  1 
ATOM   1894 C C   . MET A 1 241 ? 46.049 84.561  10.918  1.00 23.29 ? 241  MET A C   1 
ATOM   1895 O O   . MET A 1 241 ? 46.181 84.423  12.124  1.00 20.38 ? 241  MET A O   1 
ATOM   1896 C CB  . MET A 1 241 ? 45.386 86.651  9.657   1.00 24.86 ? 241  MET A CB  1 
ATOM   1897 C CG  . MET A 1 241 ? 46.433 87.388  10.445  1.00 26.73 ? 241  MET A CG  1 
ATOM   1898 S SD  . MET A 1 241 ? 47.140 88.613  9.321   1.00 31.14 ? 241  MET A SD  1 
ATOM   1899 C CE  . MET A 1 241 ? 45.752 89.733  9.112   1.00 21.11 ? 241  MET A CE  1 
ATOM   1900 N N   . GLU A 1 242 ? 46.809 83.941  10.036  1.00 23.55 ? 242  GLU A N   1 
ATOM   1901 C CA  . GLU A 1 242 ? 48.077 83.369  10.456  1.00 25.85 ? 242  GLU A CA  1 
ATOM   1902 C C   . GLU A 1 242 ? 49.142 83.655  9.419   1.00 25.95 ? 242  GLU A C   1 
ATOM   1903 O O   . GLU A 1 242 ? 48.835 83.861  8.235   1.00 25.61 ? 242  GLU A O   1 
ATOM   1904 C CB  . GLU A 1 242 ? 48.011 81.861  10.757  1.00 26.13 ? 242  GLU A CB  1 
ATOM   1905 C CG  . GLU A 1 242 ? 47.481 80.994  9.637   1.00 28.92 ? 242  GLU A CG  1 
ATOM   1906 C CD  . GLU A 1 242 ? 47.126 79.559  10.131  1.00 30.83 ? 242  GLU A CD  1 
ATOM   1907 O OE1 . GLU A 1 242 ? 47.179 79.308  11.364  1.00 34.30 ? 242  GLU A OE1 1 
ATOM   1908 O OE2 . GLU A 1 242 ? 46.836 78.686  9.278   1.00 35.23 ? 242  GLU A OE2 1 
ATOM   1909 N N   . VAL A 1 243 ? 50.394 83.681  9.880   1.00 24.04 ? 243  VAL A N   1 
ATOM   1910 C CA  . VAL A 1 243 ? 51.489 84.008  9.012   1.00 24.63 ? 243  VAL A CA  1 
ATOM   1911 C C   . VAL A 1 243 ? 52.407 82.815  9.058   1.00 23.16 ? 243  VAL A C   1 
ATOM   1912 O O   . VAL A 1 243 ? 52.719 82.320  10.118  1.00 22.74 ? 243  VAL A O   1 
ATOM   1913 C CB  . VAL A 1 243 ? 52.244 85.265  9.504   1.00 25.83 ? 243  VAL A CB  1 
ATOM   1914 C CG1 . VAL A 1 243 ? 53.419 85.531  8.594   1.00 27.50 ? 243  VAL A CG1 1 
ATOM   1915 C CG2 . VAL A 1 243 ? 51.322 86.478  9.509   1.00 24.74 ? 243  VAL A CG2 1 
ATOM   1916 N N   . VAL A 1 244 ? 52.791 82.311  7.908   1.00 22.94 ? 244  VAL A N   1 
ATOM   1917 C CA  . VAL A 1 244 ? 53.536 81.068  7.843   1.00 23.20 ? 244  VAL A CA  1 
ATOM   1918 C C   . VAL A 1 244 ? 54.908 81.358  7.284   1.00 22.97 ? 244  VAL A C   1 
ATOM   1919 O O   . VAL A 1 244 ? 55.007 81.842  6.160   1.00 23.71 ? 244  VAL A O   1 
ATOM   1920 C CB  . VAL A 1 244 ? 52.862 80.084  6.902   1.00 23.07 ? 244  VAL A CB  1 
ATOM   1921 C CG1 . VAL A 1 244 ? 53.664 78.762  6.833   1.00 24.60 ? 244  VAL A CG1 1 
ATOM   1922 C CG2 . VAL A 1 244 ? 51.352 79.883  7.275   1.00 26.84 ? 244  VAL A CG2 1 
ATOM   1923 N N   . LEU A 1 245 ? 55.945 80.987  8.027   1.00 22.75 ? 245  LEU A N   1 
ATOM   1924 C CA  . LEU A 1 245 ? 57.317 81.232  7.616   1.00 23.34 ? 245  LEU A CA  1 
ATOM   1925 C C   . LEU A 1 245 ? 57.981 79.929  7.228   1.00 23.09 ? 245  LEU A C   1 
ATOM   1926 O O   . LEU A 1 245 ? 57.867 78.929  7.940   1.00 22.92 ? 245  LEU A O   1 
ATOM   1927 C CB  . LEU A 1 245 ? 58.114 81.877  8.761   1.00 24.25 ? 245  LEU A CB  1 
ATOM   1928 C CG  . LEU A 1 245 ? 57.449 83.105  9.406   1.00 26.75 ? 245  LEU A CG  1 
ATOM   1929 C CD1 . LEU A 1 245 ? 58.257 83.486  10.662  1.00 32.95 ? 245  LEU A CD1 1 
ATOM   1930 C CD2 . LEU A 1 245 ? 57.511 84.188  8.466   1.00 27.53 ? 245  LEU A CD2 1 
ATOM   1931 N N   . GLN A 1 246 ? 58.701 79.945  6.119   1.00 23.20 ? 246  GLN A N   1 
ATOM   1932 C CA  . GLN A 1 246 ? 59.392 78.770  5.655   1.00 23.53 ? 246  GLN A CA  1 
ATOM   1933 C C   . GLN A 1 246 ? 60.744 79.085  5.095   1.00 24.60 ? 246  GLN A C   1 
ATOM   1934 O O   . GLN A 1 246 ? 60.998 80.227  4.734   1.00 23.84 ? 246  GLN A O   1 
ATOM   1935 C CB  . GLN A 1 246 ? 58.576 78.008  4.640   1.00 23.40 ? 246  GLN A CB  1 
ATOM   1936 C CG  . GLN A 1 246 ? 58.386 78.676  3.323   1.00 22.33 ? 246  GLN A CG  1 
ATOM   1937 C CD  . GLN A 1 246 ? 57.301 77.948  2.593   1.00 24.54 ? 246  GLN A CD  1 
ATOM   1938 O OE1 . GLN A 1 246 ? 56.127 78.085  2.929   1.00 25.18 ? 246  GLN A OE1 1 
ATOM   1939 N NE2 . GLN A 1 246 ? 57.687 77.093  1.647   1.00 22.23 ? 246  GLN A NE2 1 
ATOM   1940 N N   . PRO A 1 247 ? 61.635 78.070  5.048   1.00 25.47 ? 247  PRO A N   1 
ATOM   1941 C CA  . PRO A 1 247 ? 63.024 78.402  4.739   1.00 27.13 ? 247  PRO A CA  1 
ATOM   1942 C C   . PRO A 1 247 ? 63.465 78.611  3.273   1.00 27.71 ? 247  PRO A C   1 
ATOM   1943 O O   . PRO A 1 247 ? 64.660 78.750  3.027   1.00 29.38 ? 247  PRO A O   1 
ATOM   1944 C CB  . PRO A 1 247 ? 63.810 77.303  5.449   1.00 26.29 ? 247  PRO A CB  1 
ATOM   1945 C CG  . PRO A 1 247 ? 62.781 76.265  5.851   1.00 28.24 ? 247  PRO A CG  1 
ATOM   1946 C CD  . PRO A 1 247 ? 61.478 76.641  5.315   1.00 26.00 ? 247  PRO A CD  1 
ATOM   1947 N N   . ALA A 1 248 ? 62.522 78.723  2.344   1.00 28.50 ? 248  ALA A N   1 
ATOM   1948 C CA  . ALA A 1 248 ? 62.796 79.094  0.963   1.00 27.82 ? 248  ALA A CA  1 
ATOM   1949 C C   . ALA A 1 248 ? 63.914 80.134  0.811   1.00 28.91 ? 248  ALA A C   1 
ATOM   1950 O O   . ALA A 1 248 ? 64.881 79.859  0.065   1.00 29.45 ? 248  ALA A O   1 
ATOM   1951 C CB  . ALA A 1 248 ? 61.524 79.577  0.288   1.00 28.68 ? 248  ALA A CB  1 
ATOM   1952 N N   . PRO A 1 249 ? 63.831 81.299  1.522   1.00 27.69 ? 249  PRO A N   1 
ATOM   1953 C CA  . PRO A 1 249 ? 62.838 81.799  2.531   1.00 26.52 ? 249  PRO A CA  1 
ATOM   1954 C C   . PRO A 1 249 ? 61.602 82.482  1.957   1.00 26.04 ? 249  PRO A C   1 
ATOM   1955 O O   . PRO A 1 249 ? 61.638 83.062  0.891   1.00 26.24 ? 249  PRO A O   1 
ATOM   1956 C CB  . PRO A 1 249 ? 63.630 82.798  3.366   1.00 27.68 ? 249  PRO A CB  1 
ATOM   1957 C CG  . PRO A 1 249 ? 64.794 83.248  2.441   1.00 27.40 ? 249  PRO A CG  1 
ATOM   1958 C CD  . PRO A 1 249 ? 64.945 82.258  1.316   1.00 27.12 ? 249  PRO A CD  1 
ATOM   1959 N N   . ALA A 1 250 ? 60.491 82.367  2.656   1.00 23.85 ? 250  ALA A N   1 
ATOM   1960 C CA  . ALA A 1 250 ? 59.236 82.929  2.180   1.00 23.29 ? 250  ALA A CA  1 
ATOM   1961 C C   . ALA A 1 250 ? 58.314 83.132  3.362   1.00 22.70 ? 250  ALA A C   1 
ATOM   1962 O O   . ALA A 1 250 ? 58.434 82.458  4.384   1.00 21.04 ? 250  ALA A O   1 
ATOM   1963 C CB  . ALA A 1 250 ? 58.564 81.960  1.231   1.00 22.28 ? 250  ALA A CB  1 
ATOM   1964 N N   . ILE A 1 251 ? 57.335 83.994  3.158   1.00 23.23 ? 251  ILE A N   1 
ATOM   1965 C CA  . ILE A 1 251 ? 56.293 84.212  4.132   1.00 24.17 ? 251  ILE A CA  1 
ATOM   1966 C C   . ILE A 1 251 ? 54.945 84.157  3.407   1.00 24.55 ? 251  ILE A C   1 
ATOM   1967 O O   . ILE A 1 251 ? 54.827 84.611  2.267   1.00 24.55 ? 251  ILE A O   1 
ATOM   1968 C CB  . ILE A 1 251 ? 56.478 85.574  4.828   1.00 25.16 ? 251  ILE A CB  1 
ATOM   1969 C CG1 . ILE A 1 251 ? 55.352 85.847  5.838   1.00 25.05 ? 251  ILE A CG1 1 
ATOM   1970 C CG2 . ILE A 1 251 ? 56.476 86.739  3.807   1.00 26.98 ? 251  ILE A CG2 1 
ATOM   1971 C CD1 . ILE A 1 251 ? 55.773 86.905  6.857   1.00 29.76 ? 251  ILE A CD1 1 
ATOM   1972 N N   . THR A 1 252 ? 53.938 83.601  4.072   1.00 23.57 ? 252  THR A N   1 
ATOM   1973 C CA  . THR A 1 252 ? 52.598 83.509  3.559   1.00 23.51 ? 252  THR A CA  1 
ATOM   1974 C C   . THR A 1 252 ? 51.650 84.111  4.593   1.00 23.43 ? 252  THR A C   1 
ATOM   1975 O O   . THR A 1 252 ? 51.759 83.803  5.780   1.00 22.39 ? 252  THR A O   1 
ATOM   1976 C CB  . THR A 1 252 ? 52.211 82.020  3.376   1.00 24.26 ? 252  THR A CB  1 
ATOM   1977 O OG1 . THR A 1 252 ? 53.002 81.483  2.317   1.00 28.16 ? 252  THR A OG1 1 
ATOM   1978 C CG2 . THR A 1 252 ? 50.745 81.840  3.022   1.00 23.71 ? 252  THR A CG2 1 
ATOM   1979 N N   . TYR A 1 253 ? 50.733 84.943  4.120   1.00 21.33 ? 253  TYR A N   1 
ATOM   1980 C CA  . TYR A 1 253 ? 49.722 85.525  4.953   1.00 22.62 ? 253  TYR A CA  1 
ATOM   1981 C C   . TYR A 1 253 ? 48.444 84.758  4.585   1.00 23.63 ? 253  TYR A C   1 
ATOM   1982 O O   . TYR A 1 253 ? 48.133 84.612  3.403   1.00 22.11 ? 253  TYR A O   1 
ATOM   1983 C CB  . TYR A 1 253 ? 49.502 86.959  4.611   1.00 22.64 ? 253  TYR A CB  1 
ATOM   1984 C CG  . TYR A 1 253 ? 50.499 87.945  5.203   1.00 24.13 ? 253  TYR A CG  1 
ATOM   1985 C CD1 . TYR A 1 253 ? 50.371 88.406  6.500   1.00 26.47 ? 253  TYR A CD1 1 
ATOM   1986 C CD2 . TYR A 1 253 ? 51.587 88.394  4.452   1.00 30.63 ? 253  TYR A CD2 1 
ATOM   1987 C CE1 . TYR A 1 253 ? 51.315 89.302  7.060   1.00 27.91 ? 253  TYR A CE1 1 
ATOM   1988 C CE2 . TYR A 1 253 ? 52.525 89.309  4.980   1.00 28.12 ? 253  TYR A CE2 1 
ATOM   1989 C CZ  . TYR A 1 253 ? 52.364 89.765  6.277   1.00 28.54 ? 253  TYR A CZ  1 
ATOM   1990 O OH  . TYR A 1 253 ? 53.271 90.670  6.804   1.00 31.61 ? 253  TYR A OH  1 
ATOM   1991 N N   . ARG A 1 254 ? 47.701 84.322  5.587   1.00 23.12 ? 254  ARG A N   1 
ATOM   1992 C CA  . ARG A 1 254 ? 46.479 83.531  5.356   1.00 24.58 ? 254  ARG A CA  1 
ATOM   1993 C C   . ARG A 1 254 ? 45.414 84.146  6.263   1.00 25.44 ? 254  ARG A C   1 
ATOM   1994 O O   . ARG A 1 254 ? 45.544 84.083  7.461   1.00 26.45 ? 254  ARG A O   1 
ATOM   1995 C CB  . ARG A 1 254 ? 46.830 82.120  5.750   1.00 25.67 ? 254  ARG A CB  1 
ATOM   1996 C CG  . ARG A 1 254 ? 45.926 81.022  5.396   1.00 28.96 ? 254  ARG A CG  1 
ATOM   1997 C CD  . ARG A 1 254 ? 46.488 79.759  6.018   1.00 27.46 ? 254  ARG A CD  1 
ATOM   1998 N NE  . ARG A 1 254 ? 47.554 79.118  5.236   1.00 23.47 ? 254  ARG A NE  1 
ATOM   1999 C CZ  . ARG A 1 254 ? 48.459 78.318  5.786   1.00 24.51 ? 254  ARG A CZ  1 
ATOM   2000 N NH1 . ARG A 1 254 ? 48.403 78.067  7.088   1.00 26.29 ? 254  ARG A NH1 1 
ATOM   2001 N NH2 . ARG A 1 254 ? 49.399 77.720  5.055   1.00 25.55 ? 254  ARG A NH2 1 
ATOM   2002 N N   . THR A 1 255 ? 44.406 84.801  5.695   1.00 24.24 ? 255  THR A N   1 
ATOM   2003 C CA  . THR A 1 255 ? 43.370 85.465  6.499   1.00 24.54 ? 255  THR A CA  1 
ATOM   2004 C C   . THR A 1 255 ? 41.983 84.951  6.163   1.00 24.80 ? 255  THR A C   1 
ATOM   2005 O O   . THR A 1 255 ? 41.791 84.354  5.087   1.00 24.50 ? 255  THR A O   1 
ATOM   2006 C CB  . THR A 1 255 ? 43.431 87.021  6.324   1.00 23.91 ? 255  THR A CB  1 
ATOM   2007 O OG1 . THR A 1 255 ? 42.555 87.648  7.248   1.00 27.28 ? 255  THR A OG1 1 
ATOM   2008 C CG2 . THR A 1 255 ? 43.050 87.452  4.955   1.00 22.48 ? 255  THR A CG2 1 
ATOM   2009 N N   . ILE A 1 256 ? 41.033 85.143  7.089   1.00 24.57 ? 256  ILE A N   1 
ATOM   2010 C CA  . ILE A 1 256 ? 39.671 84.546  6.959   1.00 23.82 ? 256  ILE A CA  1 
ATOM   2011 C C   . ILE A 1 256 ? 38.614 85.575  6.625   1.00 23.36 ? 256  ILE A C   1 
ATOM   2012 O O   . ILE A 1 256 ? 37.393 85.293  6.642   1.00 23.96 ? 256  ILE A O   1 
ATOM   2013 C CB  . ILE A 1 256 ? 39.253 83.627  8.167   1.00 24.19 ? 256  ILE A CB  1 
ATOM   2014 C CG1 . ILE A 1 256 ? 39.106 84.407  9.466   1.00 23.48 ? 256  ILE A CG1 1 
ATOM   2015 C CG2 . ILE A 1 256 ? 40.259 82.414  8.290   1.00 24.06 ? 256  ILE A CG2 1 
ATOM   2016 C CD1 . ILE A 1 256 ? 38.505 83.535  10.651  1.00 25.20 ? 256  ILE A CD1 1 
ATOM   2017 N N   . GLY A 1 257 ? 39.066 86.775  6.284   1.00 21.37 ? 257  GLY A N   1 
ATOM   2018 C CA  . GLY A 1 257 ? 38.182 87.739  5.715   1.00 22.36 ? 257  GLY A CA  1 
ATOM   2019 C C   . GLY A 1 257 ? 38.836 88.972  5.128   1.00 23.27 ? 257  GLY A C   1 
ATOM   2020 O O   . GLY A 1 257 ? 40.073 89.071  5.076   1.00 22.76 ? 257  GLY A O   1 
ATOM   2021 N N   . GLY A 1 258 ? 37.986 89.936  4.768   1.00 22.37 ? 258  GLY A N   1 
ATOM   2022 C CA  . GLY A 1 258 ? 38.413 91.248  4.372   1.00 22.35 ? 258  GLY A CA  1 
ATOM   2023 C C   . GLY A 1 258 ? 39.027 91.170  2.986   1.00 22.67 ? 258  GLY A C   1 
ATOM   2024 O O   . GLY A 1 258 ? 38.571 90.394  2.115   1.00 22.67 ? 258  GLY A O   1 
ATOM   2025 N N   . ILE A 1 259 ? 40.072 91.959  2.778   1.00 23.79 ? 259  ILE A N   1 
ATOM   2026 C CA  . ILE A 1 259 ? 40.775 91.967  1.496   1.00 24.83 ? 259  ILE A CA  1 
ATOM   2027 C C   . ILE A 1 259 ? 42.282 91.932  1.711   1.00 25.69 ? 259  ILE A C   1 
ATOM   2028 O O   . ILE A 1 259 ? 42.774 92.107  2.816   1.00 25.49 ? 259  ILE A O   1 
ATOM   2029 C CB  . ILE A 1 259 ? 40.435 93.218  0.652   1.00 25.83 ? 259  ILE A CB  1 
ATOM   2030 C CG1 . ILE A 1 259 ? 40.916 94.513  1.353   1.00 27.19 ? 259  ILE A CG1 1 
ATOM   2031 C CG2 . ILE A 1 259 ? 38.949 93.287  0.349   1.00 26.24 ? 259  ILE A CG2 1 
ATOM   2032 C CD1 . ILE A 1 259 ? 40.956 95.693  0.418   1.00 26.69 ? 259  ILE A CD1 1 
ATOM   2033 N N   . LEU A 1 260 ? 43.014 91.750  0.628   1.00 25.78 ? 260  LEU A N   1 
ATOM   2034 C CA  . LEU A 1 260 ? 44.443 91.732  0.748   1.00 26.92 ? 260  LEU A CA  1 
ATOM   2035 C C   . LEU A 1 260 ? 44.898 93.124  0.353   1.00 27.11 ? 260  LEU A C   1 
ATOM   2036 O O   . LEU A 1 260 ? 44.853 93.482  -0.833  1.00 29.12 ? 260  LEU A O   1 
ATOM   2037 C CB  . LEU A 1 260 ? 45.011 90.637  -0.135  1.00 26.00 ? 260  LEU A CB  1 
ATOM   2038 C CG  . LEU A 1 260 ? 44.708 89.188  0.265   1.00 26.09 ? 260  LEU A CG  1 
ATOM   2039 C CD1 . LEU A 1 260 ? 45.420 88.193  -0.740  1.00 24.70 ? 260  LEU A CD1 1 
ATOM   2040 C CD2 . LEU A 1 260 ? 45.125 88.939  1.728   1.00 25.27 ? 260  LEU A CD2 1 
ATOM   2041 N N   . ASP A 1 261 ? 45.236 93.924  1.361   1.00 26.16 ? 261  ASP A N   1 
ATOM   2042 C CA  . ASP A 1 261 ? 45.632 95.309  1.164   1.00 25.85 ? 261  ASP A CA  1 
ATOM   2043 C C   . ASP A 1 261 ? 47.077 95.435  1.667   1.00 24.52 ? 261  ASP A C   1 
ATOM   2044 O O   . ASP A 1 261 ? 47.312 95.525  2.870   1.00 22.84 ? 261  ASP A O   1 
ATOM   2045 C CB  . ASP A 1 261 ? 44.659 96.200  1.946   1.00 27.13 ? 261  ASP A CB  1 
ATOM   2046 C CG  . ASP A 1 261 ? 44.986 97.695  1.836   1.00 32.04 ? 261  ASP A CG  1 
ATOM   2047 O OD1 . ASP A 1 261 ? 45.989 98.025  1.175   1.00 37.54 ? 261  ASP A OD1 1 
ATOM   2048 O OD2 . ASP A 1 261 ? 44.236 98.547  2.398   1.00 35.74 ? 261  ASP A OD2 1 
ATOM   2049 N N   . PHE A 1 262 ? 48.045 95.438  0.752   1.00 21.98 ? 262  PHE A N   1 
ATOM   2050 C CA  . PHE A 1 262 ? 49.442 95.341  1.167   1.00 22.40 ? 262  PHE A CA  1 
ATOM   2051 C C   . PHE A 1 262 ? 50.170 96.643  0.894   1.00 21.84 ? 262  PHE A C   1 
ATOM   2052 O O   . PHE A 1 262 ? 49.901 97.305  -0.134  1.00 19.85 ? 262  PHE A O   1 
ATOM   2053 C CB  . PHE A 1 262 ? 50.165 94.258  0.354   1.00 22.08 ? 262  PHE A CB  1 
ATOM   2054 C CG  . PHE A 1 262 ? 49.953 92.883  0.832   1.00 24.27 ? 262  PHE A CG  1 
ATOM   2055 C CD1 . PHE A 1 262 ? 50.708 92.380  1.902   1.00 26.24 ? 262  PHE A CD1 1 
ATOM   2056 C CD2 . PHE A 1 262 ? 49.048 92.034  0.180   1.00 23.28 ? 262  PHE A CD2 1 
ATOM   2057 C CE1 . PHE A 1 262 ? 50.515 91.058  2.367   1.00 27.23 ? 262  PHE A CE1 1 
ATOM   2058 C CE2 . PHE A 1 262 ? 48.889 90.708  0.615   1.00 25.73 ? 262  PHE A CE2 1 
ATOM   2059 C CZ  . PHE A 1 262 ? 49.612 90.223  1.703   1.00 25.49 ? 262  PHE A CZ  1 
ATOM   2060 N N   . TYR A 1 263 ? 51.153 96.939  1.749   1.00 21.12 ? 263  TYR A N   1 
ATOM   2061 C CA  . TYR A 1 263 ? 52.095 98.032  1.546   1.00 20.70 ? 263  TYR A CA  1 
ATOM   2062 C C   . TYR A 1 263 ? 53.512 97.456  1.603   1.00 22.07 ? 263  TYR A C   1 
ATOM   2063 O O   . TYR A 1 263 ? 53.785 96.551  2.400   1.00 21.92 ? 263  TYR A O   1 
ATOM   2064 C CB  . TYR A 1 263 ? 51.967 99.085  2.625   1.00 19.55 ? 263  TYR A CB  1 
ATOM   2065 C CG  . TYR A 1 263 ? 50.644 99.827  2.604   1.00 22.49 ? 263  TYR A CG  1 
ATOM   2066 C CD1 . TYR A 1 263 ? 50.534 101.035 1.961   1.00 19.89 ? 263  TYR A CD1 1 
ATOM   2067 C CD2 . TYR A 1 263 ? 49.505 99.321  3.252   1.00 22.59 ? 263  TYR A CD2 1 
ATOM   2068 C CE1 . TYR A 1 263 ? 49.317 101.767 1.964   1.00 21.77 ? 263  TYR A CE1 1 
ATOM   2069 C CE2 . TYR A 1 263 ? 48.312 100.044 3.264   1.00 21.93 ? 263  TYR A CE2 1 
ATOM   2070 C CZ  . TYR A 1 263 ? 48.224 101.251 2.596   1.00 22.05 ? 263  TYR A CZ  1 
ATOM   2071 O OH  . TYR A 1 263 ? 47.050 102.023 2.600   1.00 23.50 ? 263  TYR A OH  1 
ATOM   2072 N N   . VAL A 1 264 ? 54.376 97.949  0.713   1.00 21.00 ? 264  VAL A N   1 
ATOM   2073 C CA  . VAL A 1 264 ? 55.770 97.519  0.652   1.00 20.51 ? 264  VAL A CA  1 
ATOM   2074 C C   . VAL A 1 264 ? 56.583 98.810  0.797   1.00 19.77 ? 264  VAL A C   1 
ATOM   2075 O O   . VAL A 1 264 ? 56.268 99.806  0.140   1.00 20.05 ? 264  VAL A O   1 
ATOM   2076 C CB  . VAL A 1 264 ? 56.052 96.761  -0.658  1.00 20.53 ? 264  VAL A CB  1 
ATOM   2077 C CG1 . VAL A 1 264 ? 57.485 96.226  -0.672  1.00 22.26 ? 264  VAL A CG1 1 
ATOM   2078 C CG2 . VAL A 1 264 ? 55.048 95.559  -0.847  1.00 20.99 ? 264  VAL A CG2 1 
ATOM   2079 N N   . PHE A 1 265 ? 57.579 98.787  1.681   1.00 18.83 ? 265  PHE A N   1 
ATOM   2080 C CA  . PHE A 1 265 ? 58.358 99.965  2.083   1.00 19.55 ? 265  PHE A CA  1 
ATOM   2081 C C   . PHE A 1 265 ? 59.826 99.652  1.810   1.00 19.76 ? 265  PHE A C   1 
ATOM   2082 O O   . PHE A 1 265 ? 60.264 98.561  2.163   1.00 20.38 ? 265  PHE A O   1 
ATOM   2083 C CB  . PHE A 1 265 ? 58.221 100.254 3.613   1.00 18.59 ? 265  PHE A CB  1 
ATOM   2084 C CG  . PHE A 1 265 ? 56.774 100.348 4.101   1.00 19.70 ? 265  PHE A CG  1 
ATOM   2085 C CD1 . PHE A 1 265 ? 56.064 101.527 3.960   1.00 18.40 ? 265  PHE A CD1 1 
ATOM   2086 C CD2 . PHE A 1 265 ? 56.172 99.259  4.743   1.00 20.90 ? 265  PHE A CD2 1 
ATOM   2087 C CE1 . PHE A 1 265 ? 54.729 101.632 4.423   1.00 18.92 ? 265  PHE A CE1 1 
ATOM   2088 C CE2 . PHE A 1 265 ? 54.870 99.314  5.211   1.00 16.74 ? 265  PHE A CE2 1 
ATOM   2089 C CZ  . PHE A 1 265 ? 54.118 100.504 5.030   1.00 17.84 ? 265  PHE A CZ  1 
ATOM   2090 N N   . LEU A 1 266 ? 60.578 100.580 1.198   1.00 20.04 ? 266  LEU A N   1 
ATOM   2091 C CA  . LEU A 1 266 ? 62.006 100.334 0.959   1.00 21.55 ? 266  LEU A CA  1 
ATOM   2092 C C   . LEU A 1 266 ? 62.794 101.347 1.752   1.00 21.63 ? 266  LEU A C   1 
ATOM   2093 O O   . LEU A 1 266 ? 62.379 102.475 1.856   1.00 21.45 ? 266  LEU A O   1 
ATOM   2094 C CB  . LEU A 1 266 ? 62.363 100.509 -0.537  1.00 21.11 ? 266  LEU A CB  1 
ATOM   2095 C CG  . LEU A 1 266 ? 62.175 99.329  -1.459  1.00 22.39 ? 266  LEU A CG  1 
ATOM   2096 C CD1 . LEU A 1 266 ? 60.652 99.088  -1.760  1.00 22.60 ? 266  LEU A CD1 1 
ATOM   2097 C CD2 . LEU A 1 266 ? 62.978 99.593  -2.762  1.00 21.91 ? 266  LEU A CD2 1 
ATOM   2098 N N   . GLY A 1 267 ? 63.962 100.972 2.262   1.00 22.54 ? 267  GLY A N   1 
ATOM   2099 C CA  . GLY A 1 267 ? 64.837 101.992 2.795   1.00 21.75 ? 267  GLY A CA  1 
ATOM   2100 C C   . GLY A 1 267 ? 66.277 101.608 2.678   1.00 22.55 ? 267  GLY A C   1 
ATOM   2101 O O   . GLY A 1 267 ? 66.613 100.469 2.317   1.00 20.69 ? 267  GLY A O   1 
ATOM   2102 N N   . ASN A 1 268 ? 67.149 102.575 2.960   1.00 21.97 ? 268  ASN A N   1 
ATOM   2103 C CA  . ASN A 1 268 ? 68.567 102.277 2.896   1.00 22.95 ? 268  ASN A CA  1 
ATOM   2104 C C   . ASN A 1 268 ? 69.113 101.617 4.093   1.00 22.52 ? 268  ASN A C   1 
ATOM   2105 O O   . ASN A 1 268 ? 70.252 101.125 4.060   1.00 23.22 ? 268  ASN A O   1 
ATOM   2106 C CB  . ASN A 1 268 ? 69.398 103.528 2.551   1.00 22.98 ? 268  ASN A CB  1 
ATOM   2107 C CG  . ASN A 1 268 ? 69.029 104.074 1.220   1.00 27.66 ? 268  ASN A CG  1 
ATOM   2108 O OD1 . ASN A 1 268 ? 68.656 103.319 0.328   1.00 32.08 ? 268  ASN A OD1 1 
ATOM   2109 N ND2 . ASN A 1 268 ? 69.057 105.390 1.082   1.00 29.68 ? 268  ASN A ND2 1 
ATOM   2110 N N   . THR A 1 269 ? 68.348 101.650 5.177   1.00 21.75 ? 269  THR A N   1 
ATOM   2111 C CA  . THR A 1 269 ? 68.762 101.073 6.448   1.00 22.82 ? 269  THR A CA  1 
ATOM   2112 C C   . THR A 1 269 ? 67.475 100.547 7.112   1.00 21.29 ? 269  THR A C   1 
ATOM   2113 O O   . THR A 1 269 ? 66.390 100.877 6.673   1.00 22.80 ? 269  THR A O   1 
ATOM   2114 C CB  . THR A 1 269 ? 69.422 102.117 7.390   1.00 23.41 ? 269  THR A CB  1 
ATOM   2115 O OG1 . THR A 1 269 ? 68.440 103.082 7.749   1.00 24.54 ? 269  THR A OG1 1 
ATOM   2116 C CG2 . THR A 1 269 ? 70.662 102.855 6.718   1.00 27.57 ? 269  THR A CG2 1 
ATOM   2117 N N   . PRO A 1 270 ? 67.600 99.660  8.096   1.00 20.91 ? 270  PRO A N   1 
ATOM   2118 C CA  . PRO A 1 270 ? 66.435 99.235  8.861   1.00 20.06 ? 270  PRO A CA  1 
ATOM   2119 C C   . PRO A 1 270 ? 65.643 100.384 9.493   1.00 19.48 ? 270  PRO A C   1 
ATOM   2120 O O   . PRO A 1 270 ? 64.433 100.360 9.423   1.00 18.91 ? 270  PRO A O   1 
ATOM   2121 C CB  . PRO A 1 270 ? 67.055 98.372  9.935   1.00 20.41 ? 270  PRO A CB  1 
ATOM   2122 C CG  . PRO A 1 270 ? 68.239 97.731  9.229   1.00 19.22 ? 270  PRO A CG  1 
ATOM   2123 C CD  . PRO A 1 270 ? 68.817 98.931  8.517   1.00 20.54 ? 270  PRO A CD  1 
ATOM   2124 N N   . GLU A 1 271 ? 66.325 101.386 10.069  1.00 19.75 ? 271  GLU A N   1 
ATOM   2125 C CA  . GLU A 1 271 ? 65.666 102.535 10.660  1.00 21.25 ? 271  GLU A CA  1 
ATOM   2126 C C   . GLU A 1 271 ? 64.819 103.268 9.632   1.00 20.10 ? 271  GLU A C   1 
ATOM   2127 O O   . GLU A 1 271 ? 63.727 103.751 9.954   1.00 19.85 ? 271  GLU A O   1 
ATOM   2128 C CB  . GLU A 1 271 ? 66.691 103.473 11.354  1.00 20.70 ? 271  GLU A CB  1 
ATOM   2129 C CG  . GLU A 1 271 ? 67.155 102.986 12.758  1.00 26.17 ? 271  GLU A CG  1 
ATOM   2130 C CD  . GLU A 1 271 ? 65.998 103.065 13.779  1.00 32.19 ? 271  GLU A CD  1 
ATOM   2131 O OE1 . GLU A 1 271 ? 65.440 104.196 14.005  1.00 33.07 ? 271  GLU A OE1 1 
ATOM   2132 O OE2 . GLU A 1 271 ? 65.615 101.981 14.297  1.00 29.71 ? 271  GLU A OE2 1 
ATOM   2133 N N   . GLN A 1 272 ? 65.293 103.358 8.383   1.00 20.84 ? 272  GLN A N   1 
ATOM   2134 C CA  . GLN A 1 272 ? 64.486 103.942 7.323   1.00 20.42 ? 272  GLN A CA  1 
ATOM   2135 C C   . GLN A 1 272 ? 63.201 103.189 6.950   1.00 20.89 ? 272  GLN A C   1 
ATOM   2136 O O   . GLN A 1 272 ? 62.175 103.816 6.591   1.00 19.61 ? 272  GLN A O   1 
ATOM   2137 C CB  . GLN A 1 272 ? 65.288 104.180 6.042   1.00 22.11 ? 272  GLN A CB  1 
ATOM   2138 C CG  . GLN A 1 272 ? 66.273 105.324 6.203   1.00 26.23 ? 272  GLN A CG  1 
ATOM   2139 C CD  . GLN A 1 272 ? 67.001 105.660 4.909   1.00 33.37 ? 272  GLN A CD  1 
ATOM   2140 O OE1 . GLN A 1 272 ? 66.605 105.235 3.796   1.00 32.96 ? 272  GLN A OE1 1 
ATOM   2141 N NE2 . GLN A 1 272 ? 68.080 106.424 5.050   1.00 34.58 ? 272  GLN A NE2 1 
ATOM   2142 N N   . VAL A 1 273 ? 63.251 101.880 6.970   1.00 19.68 ? 273  VAL A N   1 
ATOM   2143 C CA  . VAL A 1 273 ? 62.011 101.101 6.763   1.00 19.47 ? 273  VAL A CA  1 
ATOM   2144 C C   . VAL A 1 273 ? 60.981 101.428 7.878   1.00 19.70 ? 273  VAL A C   1 
ATOM   2145 O O   . VAL A 1 273 ? 59.823 101.663 7.579   1.00 19.47 ? 273  VAL A O   1 
ATOM   2146 C CB  . VAL A 1 273 ? 62.294 99.622  6.695   1.00 19.93 ? 273  VAL A CB  1 
ATOM   2147 C CG1 . VAL A 1 273 ? 60.961 98.776  6.578   1.00 15.78 ? 273  VAL A CG1 1 
ATOM   2148 C CG2 . VAL A 1 273 ? 63.140 99.355  5.469   1.00 18.61 ? 273  VAL A CG2 1 
ATOM   2149 N N   . VAL A 1 274 ? 61.426 101.446 9.143   1.00 19.66 ? 274  VAL A N   1 
ATOM   2150 C CA  . VAL A 1 274 ? 60.539 101.719 10.268  1.00 18.98 ? 274  VAL A CA  1 
ATOM   2151 C C   . VAL A 1 274 ? 59.974 103.111 10.041  1.00 19.90 ? 274  VAL A C   1 
ATOM   2152 O O   . VAL A 1 274 ? 58.784 103.323 10.225  1.00 18.77 ? 274  VAL A O   1 
ATOM   2153 C CB  . VAL A 1 274 ? 61.269 101.676 11.633  1.00 18.31 ? 274  VAL A CB  1 
ATOM   2154 C CG1 . VAL A 1 274 ? 60.334 102.114 12.762  1.00 18.12 ? 274  VAL A CG1 1 
ATOM   2155 C CG2 . VAL A 1 274 ? 61.747 100.235 11.927  1.00 17.43 ? 274  VAL A CG2 1 
ATOM   2156 N N   . GLN A 1 275 ? 60.842 104.069 9.688   1.00 18.95 ? 275  GLN A N   1 
ATOM   2157 C CA  . GLN A 1 275 ? 60.378 105.426 9.392   1.00 19.78 ? 275  GLN A CA  1 
ATOM   2158 C C   . GLN A 1 275 ? 59.280 105.480 8.298   1.00 19.23 ? 275  GLN A C   1 
ATOM   2159 O O   . GLN A 1 275 ? 58.272 106.196 8.403   1.00 19.82 ? 275  GLN A O   1 
ATOM   2160 C CB  . GLN A 1 275 ? 61.604 106.290 9.029   1.00 18.57 ? 275  GLN A CB  1 
ATOM   2161 C CG  . GLN A 1 275 ? 62.470 106.576 10.208  1.00 19.67 ? 275  GLN A CG  1 
ATOM   2162 C CD  . GLN A 1 275 ? 63.754 107.300 9.801   1.00 26.78 ? 275  GLN A CD  1 
ATOM   2163 O OE1 . GLN A 1 275 ? 64.054 107.409 8.631   1.00 26.64 ? 275  GLN A OE1 1 
ATOM   2164 N NE2 . GLN A 1 275 ? 64.513 107.776 10.772  1.00 26.74 ? 275  GLN A NE2 1 
ATOM   2165 N N   . GLU A 1 276 ? 59.467 104.718 7.236   1.00 19.48 ? 276  GLU A N   1 
ATOM   2166 C CA  . GLU A 1 276 ? 58.478 104.640 6.144   1.00 20.48 ? 276  GLU A CA  1 
ATOM   2167 C C   . GLU A 1 276 ? 57.152 104.006 6.604   1.00 19.26 ? 276  GLU A C   1 
ATOM   2168 O O   . GLU A 1 276 ? 56.061 104.512 6.314   1.00 18.63 ? 276  GLU A O   1 
ATOM   2169 C CB  . GLU A 1 276 ? 59.056 103.746 5.023   1.00 20.72 ? 276  GLU A CB  1 
ATOM   2170 C CG  . GLU A 1 276 ? 60.078 104.381 4.187   1.00 26.36 ? 276  GLU A CG  1 
ATOM   2171 C CD  . GLU A 1 276 ? 59.606 105.673 3.487   1.00 31.85 ? 276  GLU A CD  1 
ATOM   2172 O OE1 . GLU A 1 276 ? 58.386 105.827 3.175   1.00 34.72 ? 276  GLU A OE1 1 
ATOM   2173 O OE2 . GLU A 1 276 ? 60.494 106.524 3.231   1.00 34.93 ? 276  GLU A OE2 1 
ATOM   2174 N N   . TYR A 1 277 ? 57.261 102.924 7.345   1.00 17.10 ? 277  TYR A N   1 
ATOM   2175 C CA  . TYR A 1 277 ? 56.074 102.280 7.936   1.00 18.48 ? 277  TYR A CA  1 
ATOM   2176 C C   . TYR A 1 277 ? 55.265 103.228 8.830   1.00 19.01 ? 277  TYR A C   1 
ATOM   2177 O O   . TYR A 1 277 ? 54.048 103.296 8.710   1.00 20.84 ? 277  TYR A O   1 
ATOM   2178 C CB  . TYR A 1 277 ? 56.496 101.046 8.748   1.00 18.40 ? 277  TYR A CB  1 
ATOM   2179 C CG  . TYR A 1 277 ? 55.336 100.393 9.515   1.00 17.64 ? 277  TYR A CG  1 
ATOM   2180 C CD1 . TYR A 1 277 ? 54.213 99.927  8.848   1.00 18.16 ? 277  TYR A CD1 1 
ATOM   2181 C CD2 . TYR A 1 277 ? 55.381 100.266 10.896  1.00 19.05 ? 277  TYR A CD2 1 
ATOM   2182 C CE1 . TYR A 1 277 ? 53.154 99.344  9.563   1.00 18.13 ? 277  TYR A CE1 1 
ATOM   2183 C CE2 . TYR A 1 277 ? 54.304 99.678  11.620  1.00 17.68 ? 277  TYR A CE2 1 
ATOM   2184 C CZ  . TYR A 1 277 ? 53.254 99.194  10.951  1.00 17.19 ? 277  TYR A CZ  1 
ATOM   2185 O OH  . TYR A 1 277 ? 52.190 98.662  11.681  1.00 22.18 ? 277  TYR A OH  1 
ATOM   2186 N N   . LEU A 1 278 ? 55.946 103.949 9.716   1.00 18.82 ? 278  LEU A N   1 
ATOM   2187 C CA  . LEU A 1 278 ? 55.299 104.857 10.655  1.00 19.62 ? 278  LEU A CA  1 
ATOM   2188 C C   . LEU A 1 278 ? 54.763 106.123 9.997   1.00 20.45 ? 278  LEU A C   1 
ATOM   2189 O O   . LEU A 1 278 ? 53.742 106.682 10.437  1.00 23.10 ? 278  LEU A O   1 
ATOM   2190 C CB  . LEU A 1 278 ? 56.258 105.158 11.795  1.00 18.63 ? 278  LEU A CB  1 
ATOM   2191 C CG  . LEU A 1 278 ? 56.632 103.904 12.611  1.00 20.01 ? 278  LEU A CG  1 
ATOM   2192 C CD1 . LEU A 1 278 ? 57.443 104.285 13.822  1.00 19.85 ? 278  LEU A CD1 1 
ATOM   2193 C CD2 . LEU A 1 278 ? 55.421 103.074 13.039  1.00 19.70 ? 278  LEU A CD2 1 
ATOM   2194 N N   . GLU A 1 279 ? 55.426 106.576 8.940   1.00 21.92 ? 279  GLU A N   1 
ATOM   2195 C CA  . GLU A 1 279 ? 54.882 107.599 8.050   1.00 22.40 ? 279  GLU A CA  1 
ATOM   2196 C C   . GLU A 1 279 ? 53.499 107.182 7.530   1.00 22.89 ? 279  GLU A C   1 
ATOM   2197 O O   . GLU A 1 279 ? 52.555 108.011 7.485   1.00 23.54 ? 279  GLU A O   1 
ATOM   2198 C CB  . GLU A 1 279 ? 55.874 107.865 6.882   1.00 22.64 ? 279  GLU A CB  1 
ATOM   2199 C CG  . GLU A 1 279 ? 55.309 108.711 5.731   1.00 27.16 ? 279  GLU A CG  1 
ATOM   2200 C CD  . GLU A 1 279 ? 54.802 110.089 6.151   1.00 34.47 ? 279  GLU A CD  1 
ATOM   2201 O OE1 . GLU A 1 279 ? 55.373 110.665 7.117   1.00 33.69 ? 279  GLU A OE1 1 
ATOM   2202 O OE2 . GLU A 1 279 ? 53.812 110.595 5.508   1.00 36.88 ? 279  GLU A OE2 1 
ATOM   2203 N N   . LEU A 1 280 ? 53.361 105.932 7.103   1.00 21.41 ? 280  LEU A N   1 
ATOM   2204 C CA  . LEU A 1 280 ? 52.042 105.431 6.701   1.00 21.79 ? 280  LEU A CA  1 
ATOM   2205 C C   . LEU A 1 280 ? 51.018 105.274 7.878   1.00 21.68 ? 280  LEU A C   1 
ATOM   2206 O O   . LEU A 1 280 ? 49.936 105.888 7.873   1.00 20.57 ? 280  LEU A O   1 
ATOM   2207 C CB  . LEU A 1 280 ? 52.157 104.108 5.900   1.00 21.30 ? 280  LEU A CB  1 
ATOM   2208 C CG  . LEU A 1 280 ? 50.767 103.505 5.641   1.00 21.59 ? 280  LEU A CG  1 
ATOM   2209 C CD1 . LEU A 1 280 ? 50.084 104.228 4.468   1.00 17.12 ? 280  LEU A CD1 1 
ATOM   2210 C CD2 . LEU A 1 280 ? 50.740 101.982 5.420   1.00 21.96 ? 280  LEU A CD2 1 
ATOM   2211 N N   . ILE A 1 281 ? 51.341 104.492 8.904   1.00 22.25 ? 281  ILE A N   1 
ATOM   2212 C CA  . ILE A 1 281 ? 50.280 104.132 9.866   1.00 21.40 ? 281  ILE A CA  1 
ATOM   2213 C C   . ILE A 1 281 ? 50.129 105.114 11.018  1.00 21.81 ? 281  ILE A C   1 
ATOM   2214 O O   . ILE A 1 281 ? 49.159 105.006 11.772  1.00 21.03 ? 281  ILE A O   1 
ATOM   2215 C CB  . ILE A 1 281 ? 50.405 102.702 10.527  1.00 24.57 ? 281  ILE A CB  1 
ATOM   2216 C CG1 . ILE A 1 281 ? 51.825 102.443 10.925  1.00 23.41 ? 281  ILE A CG1 1 
ATOM   2217 C CG2 . ILE A 1 281 ? 49.587 101.554 9.790   1.00 25.44 ? 281  ILE A CG2 1 
ATOM   2218 C CD1 . ILE A 1 281 ? 51.995 102.723 12.297  1.00 25.11 ? 281  ILE A CD1 1 
ATOM   2219 N N   . GLY A 1 282 ? 51.089 106.034 11.196  1.00 19.93 ? 282  GLY A N   1 
ATOM   2220 C CA  . GLY A 1 282 ? 51.046 106.952 12.322  1.00 19.53 ? 282  GLY A CA  1 
ATOM   2221 C C   . GLY A 1 282 ? 52.243 106.799 13.237  1.00 21.22 ? 282  GLY A C   1 
ATOM   2222 O O   . GLY A 1 282 ? 52.498 105.715 13.758  1.00 21.16 ? 282  GLY A O   1 
ATOM   2223 N N   . ARG A 1 283 ? 52.976 107.900 13.429  1.00 20.13 ? 283  ARG A N   1 
ATOM   2224 C CA  . ARG A 1 283 ? 54.074 107.941 14.355  1.00 19.88 ? 283  ARG A CA  1 
ATOM   2225 C C   . ARG A 1 283 ? 53.581 107.982 15.780  1.00 19.57 ? 283  ARG A C   1 
ATOM   2226 O O   . ARG A 1 283 ? 52.451 108.416 16.043  1.00 20.56 ? 283  ARG A O   1 
ATOM   2227 C CB  . ARG A 1 283 ? 54.985 109.140 14.019  1.00 19.83 ? 283  ARG A CB  1 
ATOM   2228 C CG  . ARG A 1 283 ? 55.945 108.810 12.853  1.00 17.86 ? 283  ARG A CG  1 
ATOM   2229 C CD  . ARG A 1 283 ? 56.853 109.993 12.563  1.00 21.91 ? 283  ARG A CD  1 
ATOM   2230 N NE  . ARG A 1 283 ? 56.063 111.145 12.174  1.00 20.46 ? 283  ARG A NE  1 
ATOM   2231 C CZ  . ARG A 1 283 ? 55.721 111.396 10.915  1.00 24.14 ? 283  ARG A CZ  1 
ATOM   2232 N NH1 . ARG A 1 283 ? 56.126 110.590 9.947   1.00 24.32 ? 283  ARG A NH1 1 
ATOM   2233 N NH2 . ARG A 1 283 ? 54.954 112.455 10.622  1.00 26.14 ? 283  ARG A NH2 1 
ATOM   2234 N N   . PRO A 1 284 ? 54.356 107.424 16.708  1.00 18.61 ? 284  PRO A N   1 
ATOM   2235 C CA  . PRO A 1 284 ? 53.890 107.407 18.100  1.00 18.90 ? 284  PRO A CA  1 
ATOM   2236 C C   . PRO A 1 284 ? 53.720 108.744 18.740  1.00 19.20 ? 284  PRO A C   1 
ATOM   2237 O O   . PRO A 1 284 ? 54.402 109.690 18.380  1.00 20.65 ? 284  PRO A O   1 
ATOM   2238 C CB  . PRO A 1 284 ? 55.000 106.639 18.857  1.00 19.17 ? 284  PRO A CB  1 
ATOM   2239 C CG  . PRO A 1 284 ? 56.138 106.696 17.981  1.00 16.88 ? 284  PRO A CG  1 
ATOM   2240 C CD  . PRO A 1 284 ? 55.675 106.755 16.555  1.00 17.55 ? 284  PRO A CD  1 
ATOM   2241 N N   . ALA A 1 285 ? 52.812 108.805 19.709  1.00 20.47 ? 285  ALA A N   1 
ATOM   2242 C CA  . ALA A 1 285 ? 52.637 109.963 20.604  1.00 21.21 ? 285  ALA A CA  1 
ATOM   2243 C C   . ALA A 1 285 ? 53.937 110.248 21.295  1.00 22.50 ? 285  ALA A C   1 
ATOM   2244 O O   . ALA A 1 285 ? 54.693 109.300 21.633  1.00 21.89 ? 285  ALA A O   1 
ATOM   2245 C CB  . ALA A 1 285 ? 51.591 109.608 21.672  1.00 21.96 ? 285  ALA A CB  1 
ATOM   2246 N N   . LEU A 1 286 ? 54.195 111.528 21.542  1.00 21.30 ? 286  LEU A N   1 
ATOM   2247 C CA  . LEU A 1 286 ? 55.259 111.938 22.413  1.00 22.88 ? 286  LEU A CA  1 
ATOM   2248 C C   . LEU A 1 286 ? 54.761 111.766 23.862  1.00 22.35 ? 286  LEU A C   1 
ATOM   2249 O O   . LEU A 1 286 ? 53.748 112.349 24.219  1.00 23.72 ? 286  LEU A O   1 
ATOM   2250 C CB  . LEU A 1 286 ? 55.633 113.399 22.143  1.00 22.22 ? 286  LEU A CB  1 
ATOM   2251 C CG  . LEU A 1 286 ? 56.862 113.976 22.866  1.00 25.47 ? 286  LEU A CG  1 
ATOM   2252 C CD1 . LEU A 1 286 ? 58.121 113.187 22.548  1.00 29.11 ? 286  LEU A CD1 1 
ATOM   2253 C CD2 . LEU A 1 286 ? 57.016 115.515 22.545  1.00 24.02 ? 286  LEU A CD2 1 
ATOM   2254 N N   . PRO A 1 287 ? 55.445 110.948 24.688  1.00 21.30 ? 287  PRO A N   1 
ATOM   2255 C CA  . PRO A 1 287 ? 54.907 110.766 26.044  1.00 21.15 ? 287  PRO A CA  1 
ATOM   2256 C C   . PRO A 1 287 ? 55.039 111.983 26.928  1.00 20.42 ? 287  PRO A C   1 
ATOM   2257 O O   . PRO A 1 287 ? 55.828 112.898 26.631  1.00 19.50 ? 287  PRO A O   1 
ATOM   2258 C CB  . PRO A 1 287 ? 55.732 109.598 26.624  1.00 21.00 ? 287  PRO A CB  1 
ATOM   2259 C CG  . PRO A 1 287 ? 56.987 109.643 25.876  1.00 24.74 ? 287  PRO A CG  1 
ATOM   2260 C CD  . PRO A 1 287 ? 56.617 110.092 24.444  1.00 20.97 ? 287  PRO A CD  1 
ATOM   2261 N N   . SER A 1 288 ? 54.249 112.022 27.997  1.00 19.91 ? 288  SER A N   1 
ATOM   2262 C CA  . SER A 1 288 ? 54.518 112.988 29.040  1.00 19.66 ? 288  SER A CA  1 
ATOM   2263 C C   . SER A 1 288 ? 55.852 112.652 29.578  1.00 18.96 ? 288  SER A C   1 
ATOM   2264 O O   . SER A 1 288 ? 56.189 111.498 29.721  1.00 18.80 ? 288  SER A O   1 
ATOM   2265 C CB  . SER A 1 288 ? 53.488 112.948 30.203  1.00 19.62 ? 288  SER A CB  1 
ATOM   2266 O OG  . SER A 1 288 ? 52.199 113.284 29.686  1.00 19.86 ? 288  SER A OG  1 
ATOM   2267 N N   . TYR A 1 289 ? 56.623 113.662 29.915  1.00 19.44 ? 289  TYR A N   1 
ATOM   2268 C CA  . TYR A 1 289 ? 57.950 113.383 30.445  1.00 20.22 ? 289  TYR A CA  1 
ATOM   2269 C C   . TYR A 1 289 ? 57.849 112.556 31.735  1.00 21.18 ? 289  TYR A C   1 
ATOM   2270 O O   . TYR A 1 289 ? 58.656 111.666 31.972  1.00 21.31 ? 289  TYR A O   1 
ATOM   2271 C CB  . TYR A 1 289 ? 58.644 114.703 30.703  1.00 19.68 ? 289  TYR A CB  1 
ATOM   2272 C CG  . TYR A 1 289 ? 60.152 114.648 30.935  1.00 20.62 ? 289  TYR A CG  1 
ATOM   2273 C CD1 . TYR A 1 289 ? 61.052 114.844 29.875  1.00 17.85 ? 289  TYR A CD1 1 
ATOM   2274 C CD2 . TYR A 1 289 ? 60.681 114.495 32.226  1.00 20.84 ? 289  TYR A CD2 1 
ATOM   2275 C CE1 . TYR A 1 289 ? 62.444 114.858 30.110  1.00 21.15 ? 289  TYR A CE1 1 
ATOM   2276 C CE2 . TYR A 1 289 ? 62.089 114.481 32.459  1.00 19.32 ? 289  TYR A CE2 1 
ATOM   2277 C CZ  . TYR A 1 289 ? 62.938 114.699 31.406  1.00 19.69 ? 289  TYR A CZ  1 
ATOM   2278 O OH  . TYR A 1 289 ? 64.294 114.705 31.639  1.00 23.46 ? 289  TYR A OH  1 
ATOM   2279 N N   . TRP A 1 290 ? 56.855 112.822 32.573  1.00 21.72 ? 290  TRP A N   1 
ATOM   2280 C CA  . TRP A 1 290 ? 56.722 111.976 33.805  1.00 21.65 ? 290  TRP A CA  1 
ATOM   2281 C C   . TRP A 1 290 ? 56.486 110.499 33.538  1.00 21.72 ? 290  TRP A C   1 
ATOM   2282 O O   . TRP A 1 290 ? 56.881 109.652 34.367  1.00 23.14 ? 290  TRP A O   1 
ATOM   2283 C CB  . TRP A 1 290 ? 55.680 112.519 34.797  1.00 21.39 ? 290  TRP A CB  1 
ATOM   2284 C CG  . TRP A 1 290 ? 54.271 112.675 34.238  1.00 20.76 ? 290  TRP A CG  1 
ATOM   2285 C CD1 . TRP A 1 290 ? 53.693 113.833 33.763  1.00 21.25 ? 290  TRP A CD1 1 
ATOM   2286 C CD2 . TRP A 1 290 ? 53.270 111.640 34.111  1.00 19.51 ? 290  TRP A CD2 1 
ATOM   2287 N NE1 . TRP A 1 290 ? 52.360 113.568 33.370  1.00 18.81 ? 290  TRP A NE1 1 
ATOM   2288 C CE2 . TRP A 1 290 ? 52.097 112.239 33.589  1.00 19.11 ? 290  TRP A CE2 1 
ATOM   2289 C CE3 . TRP A 1 290 ? 53.242 110.265 34.426  1.00 18.62 ? 290  TRP A CE3 1 
ATOM   2290 C CZ2 . TRP A 1 290 ? 50.929 111.500 33.339  1.00 21.14 ? 290  TRP A CZ2 1 
ATOM   2291 C CZ3 . TRP A 1 290 ? 52.059 109.540 34.207  1.00 22.20 ? 290  TRP A CZ3 1 
ATOM   2292 C CH2 . TRP A 1 290 ? 50.929 110.170 33.667  1.00 18.86 ? 290  TRP A CH2 1 
ATOM   2293 N N   . ALA A 1 291 ? 55.892 110.164 32.395  1.00 20.25 ? 291  ALA A N   1 
ATOM   2294 C CA  . ALA A 1 291 ? 55.590 108.777 32.080  1.00 20.10 ? 291  ALA A CA  1 
ATOM   2295 C C   . ALA A 1 291 ? 56.892 107.986 31.785  1.00 20.05 ? 291  ALA A C   1 
ATOM   2296 O O   . ALA A 1 291 ? 56.907 106.765 31.822  1.00 20.73 ? 291  ALA A O   1 
ATOM   2297 C CB  . ALA A 1 291 ? 54.643 108.709 30.898  1.00 20.93 ? 291  ALA A CB  1 
ATOM   2298 N N   . LEU A 1 292 ? 58.002 108.698 31.615  1.00 21.01 ? 292  LEU A N   1 
ATOM   2299 C CA  . LEU A 1 292 ? 59.311 108.080 31.405  1.00 20.42 ? 292  LEU A CA  1 
ATOM   2300 C C   . LEU A 1 292 ? 59.974 107.727 32.744  1.00 20.87 ? 292  LEU A C   1 
ATOM   2301 O O   . LEU A 1 292 ? 61.019 107.099 32.765  1.00 21.16 ? 292  LEU A O   1 
ATOM   2302 C CB  . LEU A 1 292 ? 60.229 109.039 30.618  1.00 20.82 ? 292  LEU A CB  1 
ATOM   2303 C CG  . LEU A 1 292 ? 59.801 109.411 29.183  1.00 22.48 ? 292  LEU A CG  1 
ATOM   2304 C CD1 . LEU A 1 292 ? 60.889 110.315 28.644  1.00 29.25 ? 292  LEU A CD1 1 
ATOM   2305 C CD2 . LEU A 1 292 ? 59.747 108.205 28.374  1.00 28.10 ? 292  LEU A CD2 1 
ATOM   2306 N N   . GLY A 1 293 ? 59.405 108.183 33.851  1.00 20.42 ? 293  GLY A N   1 
ATOM   2307 C CA  . GLY A 1 293 ? 59.886 107.794 35.165  1.00 20.07 ? 293  GLY A CA  1 
ATOM   2308 C C   . GLY A 1 293 ? 59.533 106.339 35.500  1.00 20.31 ? 293  GLY A C   1 
ATOM   2309 O O   . GLY A 1 293 ? 59.044 105.567 34.638  1.00 22.33 ? 293  GLY A O   1 
ATOM   2310 N N   . PHE A 1 294 ? 59.772 105.946 36.746  1.00 19.43 ? 294  PHE A N   1 
ATOM   2311 C CA  . PHE A 1 294 ? 59.465 104.587 37.169  1.00 19.16 ? 294  PHE A CA  1 
ATOM   2312 C C   . PHE A 1 294 ? 58.065 104.498 37.671  1.00 19.40 ? 294  PHE A C   1 
ATOM   2313 O O   . PHE A 1 294 ? 57.557 105.411 38.361  1.00 20.74 ? 294  PHE A O   1 
ATOM   2314 C CB  . PHE A 1 294 ? 60.461 104.186 38.277  1.00 20.14 ? 294  PHE A CB  1 
ATOM   2315 C CG  . PHE A 1 294 ? 60.264 102.826 38.820  1.00 19.65 ? 294  PHE A CG  1 
ATOM   2316 C CD1 . PHE A 1 294 ? 60.468 101.697 38.024  1.00 21.78 ? 294  PHE A CD1 1 
ATOM   2317 C CD2 . PHE A 1 294 ? 59.919 102.658 40.180  1.00 21.89 ? 294  PHE A CD2 1 
ATOM   2318 C CE1 . PHE A 1 294 ? 60.289 100.401 38.545  1.00 23.15 ? 294  PHE A CE1 1 
ATOM   2319 C CE2 . PHE A 1 294 ? 59.730 101.357 40.711  1.00 21.88 ? 294  PHE A CE2 1 
ATOM   2320 C CZ  . PHE A 1 294 ? 59.920 100.239 39.900  1.00 22.68 ? 294  PHE A CZ  1 
ATOM   2321 N N   . HIS A 1 295 ? 57.414 103.405 37.299  1.00 20.14 ? 295  HIS A N   1 
ATOM   2322 C CA  . HIS A 1 295 ? 56.003 103.174 37.620  1.00 19.06 ? 295  HIS A CA  1 
ATOM   2323 C C   . HIS A 1 295 ? 55.957 101.994 38.591  1.00 19.51 ? 295  HIS A C   1 
ATOM   2324 O O   . HIS A 1 295 ? 56.668 100.985 38.395  1.00 19.49 ? 295  HIS A O   1 
ATOM   2325 C CB  . HIS A 1 295 ? 55.216 102.776 36.386  1.00 18.65 ? 295  HIS A CB  1 
ATOM   2326 C CG  . HIS A 1 295 ? 55.069 103.849 35.343  1.00 19.46 ? 295  HIS A CG  1 
ATOM   2327 N ND1 . HIS A 1 295 ? 56.132 104.356 34.613  1.00 21.88 ? 295  HIS A ND1 1 
ATOM   2328 C CD2 . HIS A 1 295 ? 53.957 104.443 34.847  1.00 12.81 ? 295  HIS A CD2 1 
ATOM   2329 C CE1 . HIS A 1 295 ? 55.677 105.236 33.735  1.00 16.06 ? 295  HIS A CE1 1 
ATOM   2330 N NE2 . HIS A 1 295 ? 54.358 105.309 33.868  1.00 21.43 ? 295  HIS A NE2 1 
ATOM   2331 N N   . LEU A 1 296 ? 55.127 102.080 39.627  1.00 21.70 ? 296  LEU A N   1 
ATOM   2332 C CA  . LEU A 1 296 ? 54.944 100.918 40.528  1.00 21.56 ? 296  LEU A CA  1 
ATOM   2333 C C   . LEU A 1 296 ? 53.466 100.565 40.617  1.00 23.02 ? 296  LEU A C   1 
ATOM   2334 O O   . LEU A 1 296 ? 52.614 101.445 40.576  1.00 23.15 ? 296  LEU A O   1 
ATOM   2335 C CB  . LEU A 1 296 ? 55.485 101.229 41.903  1.00 21.53 ? 296  LEU A CB  1 
ATOM   2336 C CG  . LEU A 1 296 ? 55.552 100.185 43.027  1.00 24.17 ? 296  LEU A CG  1 
ATOM   2337 C CD1 . LEU A 1 296 ? 56.428 99.055  42.624  1.00 21.84 ? 296  LEU A CD1 1 
ATOM   2338 C CD2 . LEU A 1 296 ? 56.127 100.870 44.297  1.00 23.57 ? 296  LEU A CD2 1 
ATOM   2339 N N   . SER A 1 297 ? 53.176 99.288  40.810  1.00 23.16 ? 297  SER A N   1 
ATOM   2340 C CA  . SER A 1 297 ? 51.813 98.802  40.692  1.00 25.66 ? 297  SER A CA  1 
ATOM   2341 C C   . SER A 1 297 ? 51.695 97.413  41.315  1.00 24.58 ? 297  SER A C   1 
ATOM   2342 O O   . SER A 1 297 ? 52.683 96.679  41.421  1.00 25.15 ? 297  SER A O   1 
ATOM   2343 C CB  . SER A 1 297 ? 51.496 98.695  39.178  1.00 25.08 ? 297  SER A CB  1 
ATOM   2344 O OG  . SER A 1 297 ? 50.141 98.344  38.933  1.00 30.26 ? 297  SER A OG  1 
ATOM   2345 N N   . ARG A 1 298 ? 50.481 97.026  41.695  1.00 24.49 ? 298  ARG A N   1 
ATOM   2346 C CA  . ARG A 1 298 ? 50.186 95.621  41.853  1.00 24.34 ? 298  ARG A CA  1 
ATOM   2347 C C   . ARG A 1 298 ? 48.701 95.411  41.750  1.00 24.55 ? 298  ARG A C   1 
ATOM   2348 O O   . ARG A 1 298 ? 47.911 96.328  41.993  1.00 24.87 ? 298  ARG A O   1 
ATOM   2349 C CB  . ARG A 1 298 ? 50.715 95.005  43.160  1.00 24.27 ? 298  ARG A CB  1 
ATOM   2350 C CG  . ARG A 1 298 ? 49.927 95.290  44.402  1.00 25.68 ? 298  ARG A CG  1 
ATOM   2351 C CD  . ARG A 1 298 ? 50.376 94.363  45.516  1.00 26.89 ? 298  ARG A CD  1 
ATOM   2352 N NE  . ARG A 1 298 ? 50.158 92.965  45.150  1.00 26.56 ? 298  ARG A NE  1 
ATOM   2353 C CZ  . ARG A 1 298 ? 50.705 91.949  45.793  1.00 27.82 ? 298  ARG A CZ  1 
ATOM   2354 N NH1 . ARG A 1 298 ? 51.513 92.195  46.805  1.00 25.80 ? 298  ARG A NH1 1 
ATOM   2355 N NH2 . ARG A 1 298 ? 50.465 90.706  45.405  1.00 26.39 ? 298  ARG A NH2 1 
ATOM   2356 N N   . TYR A 1 299 ? 48.351 94.199  41.369  1.00 23.94 ? 299  TYR A N   1 
ATOM   2357 C CA  . TYR A 1 299 ? 46.991 93.742  41.454  1.00 26.47 ? 299  TYR A CA  1 
ATOM   2358 C C   . TYR A 1 299 ? 46.733 93.335  42.918  1.00 27.46 ? 299  TYR A C   1 
ATOM   2359 O O   . TYR A 1 299 ? 47.453 92.518  43.487  1.00 28.00 ? 299  TYR A O   1 
ATOM   2360 C CB  . TYR A 1 299 ? 46.832 92.574  40.506  1.00 26.91 ? 299  TYR A CB  1 
ATOM   2361 C CG  . TYR A 1 299 ? 45.448 91.960  40.388  1.00 28.46 ? 299  TYR A CG  1 
ATOM   2362 C CD1 . TYR A 1 299 ? 45.296 90.731  39.751  1.00 28.96 ? 299  TYR A CD1 1 
ATOM   2363 C CD2 . TYR A 1 299 ? 44.316 92.571  40.926  1.00 29.63 ? 299  TYR A CD2 1 
ATOM   2364 C CE1 . TYR A 1 299 ? 44.062 90.117  39.625  1.00 31.25 ? 299  TYR A CE1 1 
ATOM   2365 C CE2 . TYR A 1 299 ? 43.047 91.959  40.796  1.00 30.92 ? 299  TYR A CE2 1 
ATOM   2366 C CZ  . TYR A 1 299 ? 42.949 90.724  40.153  1.00 30.03 ? 299  TYR A CZ  1 
ATOM   2367 O OH  . TYR A 1 299 ? 41.715 90.087  39.995  1.00 32.39 ? 299  TYR A OH  1 
ATOM   2368 N N   . GLU A 1 300 ? 45.745 93.981  43.522  1.00 29.02 ? 300  GLU A N   1 
ATOM   2369 C CA  . GLU A 1 300 ? 45.276 93.688  44.886  1.00 31.25 ? 300  GLU A CA  1 
ATOM   2370 C C   . GLU A 1 300 ? 46.245 94.098  45.997  1.00 31.32 ? 300  GLU A C   1 
ATOM   2371 O O   . GLU A 1 300 ? 46.825 93.240  46.712  1.00 31.50 ? 300  GLU A O   1 
ATOM   2372 C CB  . GLU A 1 300 ? 44.800 92.241  45.030  1.00 31.57 ? 300  GLU A CB  1 
ATOM   2373 C CG  . GLU A 1 300 ? 43.504 91.994  44.264  1.00 37.78 ? 300  GLU A CG  1 
ATOM   2374 C CD  . GLU A 1 300 ? 42.236 92.355  45.042  1.00 44.77 ? 300  GLU A CD  1 
ATOM   2375 O OE1 . GLU A 1 300 ? 42.364 92.627  46.277  1.00 45.59 ? 300  GLU A OE1 1 
ATOM   2376 O OE2 . GLU A 1 300 ? 41.121 92.386  44.397  1.00 47.36 ? 300  GLU A OE2 1 
ATOM   2377 N N   . TYR A 1 301 ? 46.435 95.419  46.134  1.00 30.91 ? 301  TYR A N   1 
ATOM   2378 C CA  . TYR A 1 301 ? 46.922 95.947  47.410  1.00 31.40 ? 301  TYR A CA  1 
ATOM   2379 C C   . TYR A 1 301 ? 45.829 95.621  48.427  1.00 31.55 ? 301  TYR A C   1 
ATOM   2380 O O   . TYR A 1 301 ? 46.115 95.358  49.586  1.00 33.22 ? 301  TYR A O   1 
ATOM   2381 C CB  . TYR A 1 301 ? 47.183 97.454  47.365  1.00 29.77 ? 301  TYR A CB  1 
ATOM   2382 C CG  . TYR A 1 301 ? 48.402 97.855  46.552  1.00 28.85 ? 301  TYR A CG  1 
ATOM   2383 C CD1 . TYR A 1 301 ? 49.715 97.647  47.039  1.00 27.15 ? 301  TYR A CD1 1 
ATOM   2384 C CD2 . TYR A 1 301 ? 48.245 98.456  45.300  1.00 28.79 ? 301  TYR A CD2 1 
ATOM   2385 C CE1 . TYR A 1 301 ? 50.821 98.047  46.300  1.00 25.83 ? 301  TYR A CE1 1 
ATOM   2386 C CE2 . TYR A 1 301 ? 49.371 98.842  44.543  1.00 25.95 ? 301  TYR A CE2 1 
ATOM   2387 C CZ  . TYR A 1 301 ? 50.620 98.645  45.037  1.00 27.35 ? 301  TYR A CZ  1 
ATOM   2388 O OH  . TYR A 1 301 ? 51.688 99.041  44.235  1.00 28.85 ? 301  TYR A OH  1 
ATOM   2389 N N   . GLY A 1 302 ? 44.586 95.617  47.963  1.00 32.48 ? 302  GLY A N   1 
ATOM   2390 C CA  . GLY A 1 302 ? 43.413 95.245  48.762  1.00 31.71 ? 302  GLY A CA  1 
ATOM   2391 C C   . GLY A 1 302 ? 42.766 96.431  49.457  1.00 30.80 ? 302  GLY A C   1 
ATOM   2392 O O   . GLY A 1 302 ? 41.548 96.611  49.430  1.00 29.55 ? 302  GLY A O   1 
ATOM   2393 N N   . THR A 1 303 ? 43.598 97.243  50.092  1.00 29.95 ? 303  THR A N   1 
ATOM   2394 C CA  . THR A 1 303 ? 43.095 98.399  50.827  1.00 29.00 ? 303  THR A CA  1 
ATOM   2395 C C   . THR A 1 303 ? 43.985 99.581  50.536  1.00 28.91 ? 303  THR A C   1 
ATOM   2396 O O   . THR A 1 303 ? 45.164 99.404  50.197  1.00 27.14 ? 303  THR A O   1 
ATOM   2397 C CB  . THR A 1 303 ? 43.123 98.197  52.375  1.00 28.49 ? 303  THR A CB  1 
ATOM   2398 O OG1 . THR A 1 303 ? 44.467 98.163  52.825  1.00 30.88 ? 303  THR A OG1 1 
ATOM   2399 C CG2 . THR A 1 303 ? 42.438 96.873  52.822  1.00 29.40 ? 303  THR A CG2 1 
ATOM   2400 N N   . LEU A 1 304 ? 43.439 100.778 50.679  1.00 27.66 ? 304  LEU A N   1 
ATOM   2401 C CA  . LEU A 1 304 ? 44.267 101.959 50.554  1.00 28.84 ? 304  LEU A CA  1 
ATOM   2402 C C   . LEU A 1 304 ? 45.416 102.003 51.568  1.00 29.88 ? 304  LEU A C   1 
ATOM   2403 O O   . LEU A 1 304 ? 46.503 102.437 51.237  1.00 28.61 ? 304  LEU A O   1 
ATOM   2404 C CB  . LEU A 1 304 ? 43.420 103.223 50.599  1.00 28.88 ? 304  LEU A CB  1 
ATOM   2405 C CG  . LEU A 1 304 ? 44.123 104.543 50.387  1.00 29.98 ? 304  LEU A CG  1 
ATOM   2406 C CD1 . LEU A 1 304 ? 44.728 104.565 48.978  1.00 28.32 ? 304  LEU A CD1 1 
ATOM   2407 C CD2 . LEU A 1 304 ? 43.076 105.624 50.566  1.00 30.34 ? 304  LEU A CD2 1 
ATOM   2408 N N   . ASP A 1 305 ? 45.183 101.551 52.801  1.00 30.53 ? 305  ASP A N   1 
ATOM   2409 C CA  . ASP A 1 305 ? 46.242 101.511 53.795  1.00 31.28 ? 305  ASP A CA  1 
ATOM   2410 C C   . ASP A 1 305 ? 47.442 100.700 53.327  1.00 30.29 ? 305  ASP A C   1 
ATOM   2411 O O   . ASP A 1 305 ? 48.606 101.111 53.542  1.00 29.65 ? 305  ASP A O   1 
ATOM   2412 C CB  . ASP A 1 305 ? 45.732 100.947 55.133  1.00 32.97 ? 305  ASP A CB  1 
ATOM   2413 C CG  . ASP A 1 305 ? 44.934 101.984 55.956  1.00 40.13 ? 305  ASP A CG  1 
ATOM   2414 O OD1 . ASP A 1 305 ? 44.674 103.119 55.449  1.00 46.92 ? 305  ASP A OD1 1 
ATOM   2415 O OD2 . ASP A 1 305 ? 44.547 101.649 57.118  1.00 46.36 ? 305  ASP A OD2 1 
ATOM   2416 N N   . ASN A 1 306 ? 47.180 99.540  52.722  1.00 28.88 ? 306  ASN A N   1 
ATOM   2417 C CA  . ASN A 1 306 ? 48.243 98.725  52.148  1.00 30.06 ? 306  ASN A CA  1 
ATOM   2418 C C   . ASN A 1 306 ? 48.964 99.452  50.991  1.00 29.24 ? 306  ASN A C   1 
ATOM   2419 O O   . ASN A 1 306 ? 50.170 99.372  50.887  1.00 28.88 ? 306  ASN A O   1 
ATOM   2420 C CB  . ASN A 1 306 ? 47.682 97.386  51.635  1.00 30.41 ? 306  ASN A CB  1 
ATOM   2421 C CG  . ASN A 1 306 ? 47.325 96.417  52.777  1.00 33.19 ? 306  ASN A CG  1 
ATOM   2422 O OD1 . ASN A 1 306 ? 47.718 96.635  53.940  1.00 31.05 ? 306  ASN A OD1 1 
ATOM   2423 N ND2 . ASN A 1 306 ? 46.586 95.351  52.441  1.00 32.51 ? 306  ASN A ND2 1 
ATOM   2424 N N   . MET A 1 307 ? 48.201 100.081 50.099  1.00 28.85 ? 307  MET A N   1 
ATOM   2425 C CA  . MET A 1 307 ? 48.789 100.804 48.976  1.00 30.35 ? 307  MET A CA  1 
ATOM   2426 C C   . MET A 1 307 ? 49.691 101.909 49.519  1.00 30.40 ? 307  MET A C   1 
ATOM   2427 O O   . MET A 1 307 ? 50.849 102.011 49.134  1.00 29.71 ? 307  MET A O   1 
ATOM   2428 C CB  . MET A 1 307 ? 47.727 101.405 48.070  1.00 29.77 ? 307  MET A CB  1 
ATOM   2429 C CG  . MET A 1 307 ? 48.338 102.107 46.844  1.00 30.90 ? 307  MET A CG  1 
ATOM   2430 S SD  . MET A 1 307 ? 47.088 102.813 45.756  1.00 34.92 ? 307  MET A SD  1 
ATOM   2431 C CE  . MET A 1 307 ? 46.317 101.401 44.967  1.00 33.72 ? 307  MET A CE  1 
ATOM   2432 N N   . ARG A 1 308 ? 49.160 102.709 50.444  1.00 30.84 ? 308  ARG A N   1 
ATOM   2433 C CA  . ARG A 1 308 ? 49.920 103.779 51.037  1.00 32.46 ? 308  ARG A CA  1 
ATOM   2434 C C   . ARG A 1 308 ? 51.150 103.277 51.764  1.00 31.89 ? 308  ARG A C   1 
ATOM   2435 O O   . ARG A 1 308 ? 52.213 103.947 51.743  1.00 31.62 ? 308  ARG A O   1 
ATOM   2436 C CB  . ARG A 1 308 ? 49.015 104.611 51.942  1.00 33.33 ? 308  ARG A CB  1 
ATOM   2437 C CG  . ARG A 1 308 ? 49.669 105.830 52.523  1.00 39.19 ? 308  ARG A CG  1 
ATOM   2438 C CD  . ARG A 1 308 ? 48.762 106.451 53.603  1.00 44.69 ? 308  ARG A CD  1 
ATOM   2439 N NE  . ARG A 1 308 ? 47.661 107.215 53.026  1.00 48.96 ? 308  ARG A NE  1 
ATOM   2440 C CZ  . ARG A 1 308 ? 46.374 106.982 53.257  1.00 53.60 ? 308  ARG A CZ  1 
ATOM   2441 N NH1 . ARG A 1 308 ? 45.996 105.991 54.068  1.00 54.74 ? 308  ARG A NH1 1 
ATOM   2442 N NH2 . ARG A 1 308 ? 45.460 107.764 52.686  1.00 55.03 ? 308  ARG A NH2 1 
ATOM   2443 N N   . GLU A 1 309 ? 51.073 102.085 52.368  1.00 30.91 ? 309  GLU A N   1 
ATOM   2444 C CA  . GLU A 1 309 ? 52.248 101.525 53.028  1.00 31.90 ? 309  GLU A CA  1 
ATOM   2445 C C   . GLU A 1 309 ? 53.379 101.276 52.017  1.00 29.89 ? 309  GLU A C   1 
ATOM   2446 O O   . GLU A 1 309 ? 54.543 101.530 52.299  1.00 29.42 ? 309  GLU A O   1 
ATOM   2447 C CB  . GLU A 1 309 ? 51.960 100.197 53.772  1.00 31.55 ? 309  GLU A CB  1 
ATOM   2448 C CG  . GLU A 1 309 ? 53.258 99.602  54.409  1.00 35.94 ? 309  GLU A CG  1 
ATOM   2449 C CD  . GLU A 1 309 ? 53.027 98.470  55.451  1.00 38.33 ? 309  GLU A CD  1 
ATOM   2450 O OE1 . GLU A 1 309 ? 52.029 98.534  56.209  1.00 48.03 ? 309  GLU A OE1 1 
ATOM   2451 O OE2 . GLU A 1 309 ? 53.869 97.534  55.541  1.00 47.35 ? 309  GLU A OE2 1 
ATOM   2452 N N   . VAL A 1 310 ? 53.028 100.729 50.855  1.00 27.83 ? 310  VAL A N   1 
ATOM   2453 C CA  . VAL A 1 310 ? 54.031 100.437 49.827  1.00 26.88 ? 310  VAL A CA  1 
ATOM   2454 C C   . VAL A 1 310 ? 54.622 101.747 49.271  1.00 25.52 ? 310  VAL A C   1 
ATOM   2455 O O   . VAL A 1 310 ? 55.792 101.874 49.116  1.00 23.55 ? 310  VAL A O   1 
ATOM   2456 C CB  . VAL A 1 310 ? 53.423 99.498  48.735  1.00 26.34 ? 310  VAL A CB  1 
ATOM   2457 C CG1 . VAL A 1 310 ? 54.351 99.288  47.555  1.00 26.43 ? 310  VAL A CG1 1 
ATOM   2458 C CG2 . VAL A 1 310 ? 53.068 98.119  49.386  1.00 25.35 ? 310  VAL A CG2 1 
ATOM   2459 N N   . VAL A 1 311 ? 53.762 102.721 48.992  1.00 25.56 ? 311  VAL A N   1 
ATOM   2460 C CA  . VAL A 1 311 ? 54.192 104.000 48.483  1.00 26.39 ? 311  VAL A CA  1 
ATOM   2461 C C   . VAL A 1 311 ? 55.190 104.593 49.423  1.00 27.82 ? 311  VAL A C   1 
ATOM   2462 O O   . VAL A 1 311 ? 56.280 105.015 49.024  1.00 25.31 ? 311  VAL A O   1 
ATOM   2463 C CB  . VAL A 1 311 ? 52.959 104.952 48.327  1.00 26.65 ? 311  VAL A CB  1 
ATOM   2464 C CG1 . VAL A 1 311 ? 53.385 106.406 48.199  1.00 25.55 ? 311  VAL A CG1 1 
ATOM   2465 C CG2 . VAL A 1 311 ? 52.145 104.504 47.157  1.00 24.26 ? 311  VAL A CG2 1 
ATOM   2466 N N   . GLU A 1 312 ? 54.831 104.589 50.705  1.00 28.82 ? 312  GLU A N   1 
ATOM   2467 C CA  . GLU A 1 312 ? 55.687 105.196 51.723  1.00 30.08 ? 312  GLU A CA  1 
ATOM   2468 C C   . GLU A 1 312 ? 57.022 104.520 51.954  1.00 28.73 ? 312  GLU A C   1 
ATOM   2469 O O   . GLU A 1 312 ? 58.005 105.205 52.065  1.00 30.11 ? 312  GLU A O   1 
ATOM   2470 C CB  . GLU A 1 312 ? 54.932 105.444 53.039  1.00 30.87 ? 312  GLU A CB  1 
ATOM   2471 C CG  . GLU A 1 312 ? 54.076 106.755 52.971  1.00 39.28 ? 312  GLU A CG  1 
ATOM   2472 C CD  . GLU A 1 312 ? 54.786 107.989 52.275  1.00 48.45 ? 312  GLU A CD  1 
ATOM   2473 O OE1 . GLU A 1 312 ? 55.898 108.396 52.723  1.00 52.02 ? 312  GLU A OE1 1 
ATOM   2474 O OE2 . GLU A 1 312 ? 54.203 108.582 51.309  1.00 50.26 ? 312  GLU A OE2 1 
ATOM   2475 N N   . ARG A 1 313 ? 57.103 103.203 51.996  1.00 27.94 ? 313  ARG A N   1 
ATOM   2476 C CA  . ARG A 1 313 ? 58.445 102.589 52.099  1.00 27.84 ? 313  ARG A CA  1 
ATOM   2477 C C   . ARG A 1 313 ? 59.363 102.827 50.875  1.00 27.05 ? 313  ARG A C   1 
ATOM   2478 O O   . ARG A 1 313 ? 60.551 102.984 51.005  1.00 26.85 ? 313  ARG A O   1 
ATOM   2479 C CB  . ARG A 1 313 ? 58.349 101.085 52.456  1.00 28.69 ? 313  ARG A CB  1 
ATOM   2480 C CG  . ARG A 1 313 ? 57.621 100.193 51.432  1.00 27.51 ? 313  ARG A CG  1 
ATOM   2481 C CD  . ARG A 1 313 ? 57.941 98.708  51.769  1.00 27.63 ? 313  ARG A CD  1 
ATOM   2482 N NE  . ARG A 1 313 ? 57.263 97.721  50.900  1.00 30.50 ? 313  ARG A NE  1 
ATOM   2483 C CZ  . ARG A 1 313 ? 56.281 96.904  51.305  1.00 31.20 ? 313  ARG A CZ  1 
ATOM   2484 N NH1 . ARG A 1 313 ? 55.837 96.965  52.556  1.00 31.56 ? 313  ARG A NH1 1 
ATOM   2485 N NH2 . ARG A 1 313 ? 55.720 96.034  50.464  1.00 30.23 ? 313  ARG A NH2 1 
ATOM   2486 N N   . ASN A 1 314 ? 58.793 102.888 49.685  1.00 26.90 ? 314  ASN A N   1 
ATOM   2487 C CA  . ASN A 1 314 ? 59.595 103.187 48.501  1.00 26.76 ? 314  ASN A CA  1 
ATOM   2488 C C   . ASN A 1 314 ? 60.012 104.643 48.417  1.00 26.55 ? 314  ASN A C   1 
ATOM   2489 O O   . ASN A 1 314 ? 61.125 104.906 48.040  1.00 26.30 ? 314  ASN A O   1 
ATOM   2490 C CB  . ASN A 1 314 ? 58.907 102.698 47.228  1.00 25.14 ? 314  ASN A CB  1 
ATOM   2491 C CG  . ASN A 1 314 ? 58.896 101.208 47.151  1.00 24.86 ? 314  ASN A CG  1 
ATOM   2492 O OD1 . ASN A 1 314 ? 59.871 100.601 46.733  1.00 24.76 ? 314  ASN A OD1 1 
ATOM   2493 N ND2 . ASN A 1 314 ? 57.819 100.596 47.617  1.00 21.58 ? 314  ASN A ND2 1 
ATOM   2494 N N   . ARG A 1 315 ? 59.149 105.588 48.797  1.00 26.55 ? 315  ARG A N   1 
ATOM   2495 C CA  . ARG A 1 315 ? 59.615 106.970 48.984  1.00 27.08 ? 315  ARG A CA  1 
ATOM   2496 C C   . ARG A 1 315 ? 60.716 107.124 50.081  1.00 28.08 ? 315  ARG A C   1 
ATOM   2497 O O   . ARG A 1 315 ? 61.692 107.867 49.903  1.00 27.41 ? 315  ARG A O   1 
ATOM   2498 C CB  . ARG A 1 315 ? 58.440 107.881 49.285  1.00 27.17 ? 315  ARG A CB  1 
ATOM   2499 C CG  . ARG A 1 315 ? 57.383 107.908 48.156  1.00 27.59 ? 315  ARG A CG  1 
ATOM   2500 C CD  . ARG A 1 315 ? 56.437 109.073 48.347  1.00 28.21 ? 315  ARG A CD  1 
ATOM   2501 N NE  . ARG A 1 315 ? 57.193 110.310 48.324  1.00 33.07 ? 315  ARG A NE  1 
ATOM   2502 C CZ  . ARG A 1 315 ? 57.349 111.108 49.373  1.00 38.88 ? 315  ARG A CZ  1 
ATOM   2503 N NH1 . ARG A 1 315 ? 56.768 110.802 50.540  1.00 42.33 ? 315  ARG A NH1 1 
ATOM   2504 N NH2 . ARG A 1 315 ? 58.069 112.227 49.244  1.00 37.83 ? 315  ARG A NH2 1 
ATOM   2505 N N   . ALA A 1 316 ? 60.560 106.422 51.209  1.00 28.68 ? 316  ALA A N   1 
ATOM   2506 C CA  . ALA A 1 316 ? 61.530 106.517 52.310  1.00 29.00 ? 316  ALA A CA  1 
ATOM   2507 C C   . ALA A 1 316 ? 62.891 105.959 51.874  1.00 28.24 ? 316  ALA A C   1 
ATOM   2508 O O   . ALA A 1 316 ? 63.938 106.420 52.347  1.00 27.59 ? 316  ALA A O   1 
ATOM   2509 C CB  . ALA A 1 316 ? 61.011 105.780 53.573  1.00 29.56 ? 316  ALA A CB  1 
ATOM   2510 N N   . ALA A 1 317 ? 62.864 105.015 50.931  1.00 26.86 ? 317  ALA A N   1 
ATOM   2511 C CA  . ALA A 1 317 ? 64.066 104.486 50.299  1.00 26.55 ? 317  ALA A CA  1 
ATOM   2512 C C   . ALA A 1 317 ? 64.734 105.461 49.318  1.00 26.83 ? 317  ALA A C   1 
ATOM   2513 O O   . ALA A 1 317 ? 65.822 105.168 48.814  1.00 27.19 ? 317  ALA A O   1 
ATOM   2514 C CB  . ALA A 1 317 ? 63.736 103.173 49.578  1.00 26.54 ? 317  ALA A CB  1 
ATOM   2515 N N   . GLN A 1 318 ? 64.073 106.574 49.002  1.00 25.48 ? 318  GLN A N   1 
ATOM   2516 C CA  . GLN A 1 318 ? 64.546 107.518 47.982  1.00 26.99 ? 318  GLN A CA  1 
ATOM   2517 C C   . GLN A 1 318 ? 64.633 106.859 46.599  1.00 26.51 ? 318  GLN A C   1 
ATOM   2518 O O   . GLN A 1 318 ? 65.552 107.121 45.812  1.00 26.36 ? 318  GLN A O   1 
ATOM   2519 C CB  . GLN A 1 318 ? 65.896 108.166 48.367  1.00 28.31 ? 318  GLN A CB  1 
ATOM   2520 C CG  . GLN A 1 318 ? 65.987 108.720 49.823  1.00 34.30 ? 318  GLN A CG  1 
ATOM   2521 C CD  . GLN A 1 318 ? 64.994 109.839 50.074  1.00 41.81 ? 318  GLN A CD  1 
ATOM   2522 O OE1 . GLN A 1 318 ? 64.854 110.750 49.249  1.00 46.60 ? 318  GLN A OE1 1 
ATOM   2523 N NE2 . GLN A 1 318 ? 64.277 109.773 51.203  1.00 43.66 ? 318  GLN A NE2 1 
ATOM   2524 N N   . LEU A 1 319 ? 63.676 105.996 46.293  1.00 24.71 ? 319  LEU A N   1 
ATOM   2525 C CA  . LEU A 1 319 ? 63.685 105.355 44.996  1.00 25.35 ? 319  LEU A CA  1 
ATOM   2526 C C   . LEU A 1 319 ? 63.094 106.351 43.965  1.00 25.59 ? 319  LEU A C   1 
ATOM   2527 O O   . LEU A 1 319 ? 62.060 106.962 44.250  1.00 26.53 ? 319  LEU A O   1 
ATOM   2528 C CB  . LEU A 1 319 ? 62.821 104.104 45.065  1.00 25.29 ? 319  LEU A CB  1 
ATOM   2529 C CG  . LEU A 1 319 ? 62.857 103.154 43.867  1.00 27.74 ? 319  LEU A CG  1 
ATOM   2530 C CD1 . LEU A 1 319 ? 64.073 102.210 43.995  1.00 29.45 ? 319  LEU A CD1 1 
ATOM   2531 C CD2 . LEU A 1 319 ? 61.542 102.382 43.794  1.00 28.48 ? 319  LEU A CD2 1 
ATOM   2532 N N   . PRO A 1 320 ? 63.744 106.525 42.788  1.00 24.81 ? 320  PRO A N   1 
ATOM   2533 C CA  . PRO A 1 320 ? 63.108 107.295 41.702  1.00 24.90 ? 320  PRO A CA  1 
ATOM   2534 C C   . PRO A 1 320 ? 61.791 106.617 41.362  1.00 24.78 ? 320  PRO A C   1 
ATOM   2535 O O   . PRO A 1 320 ? 61.772 105.422 41.121  1.00 25.92 ? 320  PRO A O   1 
ATOM   2536 C CB  . PRO A 1 320 ? 64.125 107.142 40.556  1.00 25.98 ? 320  PRO A CB  1 
ATOM   2537 C CG  . PRO A 1 320 ? 65.431 107.025 41.279  1.00 23.63 ? 320  PRO A CG  1 
ATOM   2538 C CD  . PRO A 1 320 ? 65.073 106.040 42.373  1.00 24.44 ? 320  PRO A CD  1 
ATOM   2539 N N   . TYR A 1 321 ? 60.692 107.350 41.367  1.00 23.03 ? 321  TYR A N   1 
ATOM   2540 C CA  . TYR A 1 321 ? 59.376 106.705 41.457  1.00 23.33 ? 321  TYR A CA  1 
ATOM   2541 C C   . TYR A 1 321 ? 58.349 107.790 41.154  1.00 22.70 ? 321  TYR A C   1 
ATOM   2542 O O   . TYR A 1 321 ? 58.070 108.608 42.022  1.00 22.71 ? 321  TYR A O   1 
ATOM   2543 C CB  . TYR A 1 321 ? 59.259 106.214 42.910  1.00 23.69 ? 321  TYR A CB  1 
ATOM   2544 C CG  . TYR A 1 321 ? 57.941 105.683 43.417  1.00 25.43 ? 321  TYR A CG  1 
ATOM   2545 C CD1 . TYR A 1 321 ? 56.937 105.219 42.558  1.00 22.19 ? 321  TYR A CD1 1 
ATOM   2546 C CD2 . TYR A 1 321 ? 57.730 105.590 44.806  1.00 26.05 ? 321  TYR A CD2 1 
ATOM   2547 C CE1 . TYR A 1 321 ? 55.731 104.758 43.078  1.00 25.39 ? 321  TYR A CE1 1 
ATOM   2548 C CE2 . TYR A 1 321 ? 56.536 105.110 45.321  1.00 28.66 ? 321  TYR A CE2 1 
ATOM   2549 C CZ  . TYR A 1 321 ? 55.551 104.695 44.467  1.00 26.89 ? 321  TYR A CZ  1 
ATOM   2550 O OH  . TYR A 1 321 ? 54.372 104.203 45.008  1.00 27.19 ? 321  TYR A OH  1 
ATOM   2551 N N   . ASP A 1 322 ? 57.877 107.863 39.905  1.00 21.96 ? 322  ASP A N   1 
ATOM   2552 C CA  . ASP A 1 322 ? 57.016 108.953 39.452  1.00 21.25 ? 322  ASP A CA  1 
ATOM   2553 C C   . ASP A 1 322 ? 55.569 108.599 39.534  1.00 20.75 ? 322  ASP A C   1 
ATOM   2554 O O   . ASP A 1 322 ? 54.721 109.462 39.760  1.00 22.62 ? 322  ASP A O   1 
ATOM   2555 C CB  . ASP A 1 322 ? 57.343 109.334 38.003  1.00 20.80 ? 322  ASP A CB  1 
ATOM   2556 C CG  . ASP A 1 322 ? 58.349 110.417 37.961  1.00 25.79 ? 322  ASP A CG  1 
ATOM   2557 O OD1 . ASP A 1 322 ? 58.007 111.560 37.611  1.00 27.84 ? 322  ASP A OD1 1 
ATOM   2558 O OD2 . ASP A 1 322 ? 59.463 110.137 38.422  1.00 24.54 ? 322  ASP A OD2 1 
ATOM   2559 N N   . VAL A 1 323 ? 55.288 107.319 39.358  1.00 20.43 ? 323  VAL A N   1 
ATOM   2560 C CA  . VAL A 1 323 ? 53.931 106.919 39.056  1.00 20.63 ? 323  VAL A CA  1 
ATOM   2561 C C   . VAL A 1 323 ? 53.482 105.714 39.874  1.00 21.29 ? 323  VAL A C   1 
ATOM   2562 O O   . VAL A 1 323 ? 54.166 104.670 39.951  1.00 19.87 ? 323  VAL A O   1 
ATOM   2563 C CB  . VAL A 1 323 ? 53.747 106.599 37.555  1.00 21.07 ? 323  VAL A CB  1 
ATOM   2564 C CG1 . VAL A 1 323 ? 52.304 106.562 37.186  1.00 17.74 ? 323  VAL A CG1 1 
ATOM   2565 C CG2 . VAL A 1 323 ? 54.589 107.529 36.628  1.00 20.49 ? 323  VAL A CG2 1 
ATOM   2566 N N   . GLN A 1 324 ? 52.284 105.871 40.448  1.00 22.21 ? 324  GLN A N   1 
ATOM   2567 C CA  . GLN A 1 324 ? 51.615 104.791 41.116  1.00 21.42 ? 324  GLN A CA  1 
ATOM   2568 C C   . GLN A 1 324 ? 50.361 104.392 40.349  1.00 22.01 ? 324  GLN A C   1 
ATOM   2569 O O   . GLN A 1 324 ? 49.561 105.246 39.932  1.00 23.10 ? 324  GLN A O   1 
ATOM   2570 C CB  . GLN A 1 324 ? 51.304 105.207 42.554  1.00 22.94 ? 324  GLN A CB  1 
ATOM   2571 C CG  . GLN A 1 324 ? 50.578 104.110 43.335  1.00 23.24 ? 324  GLN A CG  1 
ATOM   2572 C CD  . GLN A 1 324 ? 51.417 102.881 43.497  1.00 24.08 ? 324  GLN A CD  1 
ATOM   2573 O OE1 . GLN A 1 324 ? 52.619 102.957 43.806  1.00 22.74 ? 324  GLN A OE1 1 
ATOM   2574 N NE2 . GLN A 1 324 ? 50.791 101.724 43.335  1.00 23.97 ? 324  GLN A NE2 1 
ATOM   2575 N N   . HIS A 1 325 ? 50.223 103.105 40.059  1.00 21.99 ? 325  HIS A N   1 
ATOM   2576 C CA  . HIS A 1 325 ? 49.038 102.637 39.375  1.00 23.01 ? 325  HIS A CA  1 
ATOM   2577 C C   . HIS A 1 325 ? 48.095 102.006 40.411  1.00 24.55 ? 325  HIS A C   1 
ATOM   2578 O O   . HIS A 1 325 ? 48.527 101.459 41.433  1.00 24.91 ? 325  HIS A O   1 
ATOM   2579 C CB  . HIS A 1 325 ? 49.372 101.602 38.300  1.00 22.37 ? 325  HIS A CB  1 
ATOM   2580 C CG  . HIS A 1 325 ? 50.204 102.132 37.167  1.00 22.50 ? 325  HIS A CG  1 
ATOM   2581 N ND1 . HIS A 1 325 ? 50.027 101.720 35.873  1.00 21.99 ? 325  HIS A ND1 1 
ATOM   2582 C CD2 . HIS A 1 325 ? 51.269 102.977 37.149  1.00 20.14 ? 325  HIS A CD2 1 
ATOM   2583 C CE1 . HIS A 1 325 ? 50.906 102.327 35.090  1.00 24.77 ? 325  HIS A CE1 1 
ATOM   2584 N NE2 . HIS A 1 325 ? 51.679 103.086 35.841  1.00 19.37 ? 325  HIS A NE2 1 
ATOM   2585 N N   . ALA A 1 326 ? 46.809 102.124 40.135  1.00 25.23 ? 326  ALA A N   1 
ATOM   2586 C CA  . ALA A 1 326 ? 45.788 101.530 40.958  1.00 25.87 ? 326  ALA A CA  1 
ATOM   2587 C C   . ALA A 1 326 ? 45.039 100.567 40.083  1.00 25.65 ? 326  ALA A C   1 
ATOM   2588 O O   . ALA A 1 326 ? 44.434 100.977 39.081  1.00 25.61 ? 326  ALA A O   1 
ATOM   2589 C CB  . ALA A 1 326 ? 44.812 102.618 41.491  1.00 24.71 ? 326  ALA A CB  1 
ATOM   2590 N N   . ASP A 1 327 ? 45.006 99.303  40.508  1.00 25.98 ? 327  ASP A N   1 
ATOM   2591 C CA  . ASP A 1 327 ? 44.376 98.231  39.754  1.00 26.99 ? 327  ASP A CA  1 
ATOM   2592 C C   . ASP A 1 327 ? 42.940 98.072  40.287  1.00 27.62 ? 327  ASP A C   1 
ATOM   2593 O O   . ASP A 1 327 ? 42.489 98.880  41.110  1.00 28.42 ? 327  ASP A O   1 
ATOM   2594 C CB  . ASP A 1 327 ? 45.218 96.973  39.946  1.00 27.79 ? 327  ASP A CB  1 
ATOM   2595 C CG  . ASP A 1 327 ? 45.102 95.970  38.805  1.00 28.06 ? 327  ASP A CG  1 
ATOM   2596 O OD1 . ASP A 1 327 ? 44.040 95.842  38.189  1.00 27.63 ? 327  ASP A OD1 1 
ATOM   2597 O OD2 . ASP A 1 327 ? 46.118 95.263  38.561  1.00 29.51 ? 327  ASP A OD2 1 
ATOM   2598 N N   . ILE A 1 328 ? 42.231 97.029  39.853  1.00 27.23 ? 328  ILE A N   1 
ATOM   2599 C CA  . ILE A 1 328 ? 40.771 96.955  40.022  1.00 27.32 ? 328  ILE A CA  1 
ATOM   2600 C C   . ILE A 1 328 ? 40.334 96.886  41.487  1.00 27.30 ? 328  ILE A C   1 
ATOM   2601 O O   . ILE A 1 328 ? 39.156 97.142  41.798  1.00 27.75 ? 328  ILE A O   1 
ATOM   2602 C CB  . ILE A 1 328 ? 40.145 95.792  39.245  1.00 26.96 ? 328  ILE A CB  1 
ATOM   2603 C CG1 . ILE A 1 328 ? 40.713 94.441  39.711  1.00 27.19 ? 328  ILE A CG1 1 
ATOM   2604 C CG2 . ILE A 1 328 ? 40.312 96.010  37.673  1.00 26.40 ? 328  ILE A CG2 1 
ATOM   2605 C CD1 . ILE A 1 328 ? 40.300 93.288  38.779  1.00 28.34 ? 328  ILE A CD1 1 
ATOM   2606 N N   . ASP A 1 329 ? 41.275 96.578  42.377  1.00 26.58 ? 329  ASP A N   1 
ATOM   2607 C CA  . ASP A 1 329 ? 40.982 96.672  43.827  1.00 27.65 ? 329  ASP A CA  1 
ATOM   2608 C C   . ASP A 1 329 ? 40.491 98.035  44.336  1.00 26.13 ? 329  ASP A C   1 
ATOM   2609 O O   . ASP A 1 329 ? 39.860 98.094  45.386  1.00 25.78 ? 329  ASP A O   1 
ATOM   2610 C CB  . ASP A 1 329 ? 42.116 96.114  44.727  1.00 27.81 ? 329  ASP A CB  1 
ATOM   2611 C CG  . ASP A 1 329 ? 43.540 96.539  44.286  1.00 34.09 ? 329  ASP A CG  1 
ATOM   2612 O OD1 . ASP A 1 329 ? 43.913 96.363  43.078  1.00 34.90 ? 329  ASP A OD1 1 
ATOM   2613 O OD2 . ASP A 1 329 ? 44.319 96.973  45.194  1.00 36.86 ? 329  ASP A OD2 1 
ATOM   2614 N N   . TYR A 1 330 ? 40.797 99.132  43.626  1.00 25.41 ? 330  TYR A N   1 
ATOM   2615 C CA  . TYR A 1 330 ? 40.364 100.452 44.080  1.00 24.09 ? 330  TYR A CA  1 
ATOM   2616 C C   . TYR A 1 330 ? 38.861 100.629 43.910  1.00 24.87 ? 330  TYR A C   1 
ATOM   2617 O O   . TYR A 1 330 ? 38.282 101.443 44.620  1.00 24.99 ? 330  TYR A O   1 
ATOM   2618 C CB  . TYR A 1 330 ? 41.115 101.645 43.412  1.00 22.63 ? 330  TYR A CB  1 
ATOM   2619 C CG  . TYR A 1 330 ? 40.640 101.998 42.002  1.00 24.20 ? 330  TYR A CG  1 
ATOM   2620 C CD1 . TYR A 1 330 ? 39.492 102.756 41.788  1.00 24.09 ? 330  TYR A CD1 1 
ATOM   2621 C CD2 . TYR A 1 330 ? 41.353 101.566 40.886  1.00 23.37 ? 330  TYR A CD2 1 
ATOM   2622 C CE1 . TYR A 1 330 ? 39.055 103.072 40.464  1.00 24.52 ? 330  TYR A CE1 1 
ATOM   2623 C CE2 . TYR A 1 330 ? 40.941 101.860 39.598  1.00 23.46 ? 330  TYR A CE2 1 
ATOM   2624 C CZ  . TYR A 1 330 ? 39.809 102.620 39.385  1.00 25.10 ? 330  TYR A CZ  1 
ATOM   2625 O OH  . TYR A 1 330 ? 39.411 102.895 38.117  1.00 22.98 ? 330  TYR A OH  1 
ATOM   2626 N N   . MET A 1 331 ? 38.268 99.885  42.986  1.00 24.29 ? 331  MET A N   1 
ATOM   2627 C CA  . MET A 1 331 ? 36.875 100.053 42.577  1.00 27.04 ? 331  MET A CA  1 
ATOM   2628 C C   . MET A 1 331 ? 35.865 99.487  43.613  1.00 28.00 ? 331  MET A C   1 
ATOM   2629 O O   . MET A 1 331 ? 36.214 98.664  44.441  1.00 27.08 ? 331  MET A O   1 
ATOM   2630 C CB  . MET A 1 331 ? 36.640 99.300  41.278  1.00 25.75 ? 331  MET A CB  1 
ATOM   2631 C CG  . MET A 1 331 ? 37.402 99.883  40.063  1.00 26.86 ? 331  MET A CG  1 
ATOM   2632 S SD  . MET A 1 331 ? 37.178 98.804  38.657  1.00 29.19 ? 331  MET A SD  1 
ATOM   2633 C CE  . MET A 1 331 ? 38.246 99.568  37.407  1.00 26.31 ? 331  MET A CE  1 
ATOM   2634 N N   . ASP A 1 332 ? 34.614 99.907  43.514  1.00 28.91 ? 332  ASP A N   1 
ATOM   2635 C CA  . ASP A 1 332 ? 33.585 99.292  44.341  1.00 31.80 ? 332  ASP A CA  1 
ATOM   2636 C C   . ASP A 1 332 ? 33.068 98.030  43.658  1.00 31.47 ? 332  ASP A C   1 
ATOM   2637 O O   . ASP A 1 332 ? 32.255 98.121  42.722  1.00 32.52 ? 332  ASP A O   1 
ATOM   2638 C CB  . ASP A 1 332 ? 32.443 100.281 44.594  1.00 32.82 ? 332  ASP A CB  1 
ATOM   2639 C CG  . ASP A 1 332 ? 31.442 99.769  45.630  1.00 39.30 ? 332  ASP A CG  1 
ATOM   2640 O OD1 . ASP A 1 332 ? 30.952 98.630  45.495  1.00 43.07 ? 332  ASP A OD1 1 
ATOM   2641 O OD2 . ASP A 1 332 ? 31.165 100.516 46.595  1.00 49.13 ? 332  ASP A OD2 1 
ATOM   2642 N N   . GLU A 1 333 ? 33.505 96.867  44.155  1.00 30.77 ? 333  GLU A N   1 
ATOM   2643 C CA  . GLU A 1 333 ? 33.172 95.563  43.580  1.00 31.63 ? 333  GLU A CA  1 
ATOM   2644 C C   . GLU A 1 333 ? 33.584 95.450  42.078  1.00 29.90 ? 333  GLU A C   1 
ATOM   2645 O O   . GLU A 1 333 ? 32.813 94.951  41.248  1.00 28.89 ? 333  GLU A O   1 
ATOM   2646 C CB  . GLU A 1 333 ? 31.678 95.249  43.767  1.00 33.21 ? 333  GLU A CB  1 
ATOM   2647 C CG  . GLU A 1 333 ? 31.204 95.128  45.245  1.00 40.61 ? 333  GLU A CG  1 
ATOM   2648 C CD  . GLU A 1 333 ? 31.793 93.916  45.999  1.00 49.22 ? 333  GLU A CD  1 
ATOM   2649 O OE1 . GLU A 1 333 ? 32.257 92.937  45.352  1.00 54.00 ? 333  GLU A OE1 1 
ATOM   2650 O OE2 . GLU A 1 333 ? 31.782 93.933  47.257  1.00 53.92 ? 333  GLU A OE2 1 
ATOM   2651 N N   . ARG A 1 334 ? 34.770 95.985  41.751  1.00 29.33 ? 334  ARG A N   1 
ATOM   2652 C CA  . ARG A 1 334 ? 35.381 95.868  40.428  1.00 28.53 ? 334  ARG A CA  1 
ATOM   2653 C C   . ARG A 1 334 ? 34.533 96.524  39.365  1.00 28.53 ? 334  ARG A C   1 
ATOM   2654 O O   . ARG A 1 334 ? 34.521 96.066  38.225  1.00 29.26 ? 334  ARG A O   1 
ATOM   2655 C CB  . ARG A 1 334 ? 35.663 94.383  40.105  1.00 28.72 ? 334  ARG A CB  1 
ATOM   2656 C CG  . ARG A 1 334 ? 36.634 93.734  41.089  1.00 29.55 ? 334  ARG A CG  1 
ATOM   2657 C CD  . ARG A 1 334 ? 36.471 92.190  41.261  1.00 30.68 ? 334  ARG A CD  1 
ATOM   2658 N NE  . ARG A 1 334 ? 35.087 91.661  41.101  1.00 40.22 ? 334  ARG A NE  1 
ATOM   2659 C CZ  . ARG A 1 334 ? 34.190 91.440  42.086  1.00 43.31 ? 334  ARG A CZ  1 
ATOM   2660 N NH1 . ARG A 1 334 ? 34.467 91.728  43.365  1.00 41.95 ? 334  ARG A NH1 1 
ATOM   2661 N NH2 . ARG A 1 334 ? 32.985 90.927  41.790  1.00 45.64 ? 334  ARG A NH2 1 
ATOM   2662 N N   . ARG A 1 335 ? 33.807 97.585  39.731  1.00 27.55 ? 335  ARG A N   1 
ATOM   2663 C CA  . ARG A 1 335 ? 33.019 98.350  38.772  1.00 28.84 ? 335  ARG A CA  1 
ATOM   2664 C C   . ARG A 1 335 ? 33.696 99.658  38.373  1.00 28.62 ? 335  ARG A C   1 
ATOM   2665 O O   . ARG A 1 335 ? 34.173 100.381 39.240  1.00 28.52 ? 335  ARG A O   1 
ATOM   2666 C CB  . ARG A 1 335 ? 31.628 98.622  39.321  1.00 29.13 ? 335  ARG A CB  1 
ATOM   2667 C CG  . ARG A 1 335 ? 30.756 97.364  39.356  1.00 29.48 ? 335  ARG A CG  1 
ATOM   2668 C CD  . ARG A 1 335 ? 29.374 97.642  39.839  1.00 36.08 ? 335  ARG A CD  1 
ATOM   2669 N NE  . ARG A 1 335 ? 29.370 98.248  41.168  1.00 42.98 ? 335  ARG A NE  1 
ATOM   2670 C CZ  . ARG A 1 335 ? 28.315 98.860  41.693  1.00 47.23 ? 335  ARG A CZ  1 
ATOM   2671 N NH1 . ARG A 1 335 ? 27.161 98.937  41.004  1.00 47.41 ? 335  ARG A NH1 1 
ATOM   2672 N NH2 . ARG A 1 335 ? 28.411 99.393  42.906  1.00 48.16 ? 335  ARG A NH2 1 
ATOM   2673 N N   . ASP A 1 336 ? 33.779 99.935  37.060  1.00 29.43 ? 336  ASP A N   1 
ATOM   2674 C CA  . ASP A 1 336 ? 34.463 101.155 36.565  1.00 28.82 ? 336  ASP A CA  1 
ATOM   2675 C C   . ASP A 1 336 ? 33.821 102.378 37.201  1.00 29.51 ? 336  ASP A C   1 
ATOM   2676 O O   . ASP A 1 336 ? 32.600 102.367 37.416  1.00 27.93 ? 336  ASP A O   1 
ATOM   2677 C CB  . ASP A 1 336 ? 34.257 101.367 35.072  1.00 28.23 ? 336  ASP A CB  1 
ATOM   2678 C CG  . ASP A 1 336 ? 35.155 100.545 34.212  1.00 29.15 ? 336  ASP A CG  1 
ATOM   2679 O OD1 . ASP A 1 336 ? 36.199 100.001 34.692  1.00 28.57 ? 336  ASP A OD1 1 
ATOM   2680 O OD2 . ASP A 1 336 ? 34.759 100.427 33.019  1.00 31.05 ? 336  ASP A OD2 1 
ATOM   2681 N N   . PHE A 1 337 ? 34.625 103.433 37.438  1.00 27.98 ? 337  PHE A N   1 
ATOM   2682 C CA  . PHE A 1 337 ? 34.108 104.749 37.772  1.00 28.19 ? 337  PHE A CA  1 
ATOM   2683 C C   . PHE A 1 337 ? 33.478 104.772 39.183  1.00 29.00 ? 337  PHE A C   1 
ATOM   2684 O O   . PHE A 1 337 ? 32.529 105.507 39.454  1.00 28.32 ? 337  PHE A O   1 
ATOM   2685 C CB  . PHE A 1 337 ? 33.124 105.245 36.686  1.00 27.40 ? 337  PHE A CB  1 
ATOM   2686 C CG  . PHE A 1 337 ? 33.712 105.182 35.268  1.00 27.38 ? 337  PHE A CG  1 
ATOM   2687 C CD1 . PHE A 1 337 ? 34.917 105.840 34.982  1.00 25.10 ? 337  PHE A CD1 1 
ATOM   2688 C CD2 . PHE A 1 337 ? 33.119 104.401 34.281  1.00 22.83 ? 337  PHE A CD2 1 
ATOM   2689 C CE1 . PHE A 1 337 ? 35.493 105.765 33.677  1.00 24.45 ? 337  PHE A CE1 1 
ATOM   2690 C CE2 . PHE A 1 337 ? 33.693 104.283 32.952  1.00 21.92 ? 337  PHE A CE2 1 
ATOM   2691 C CZ  . PHE A 1 337 ? 34.932 104.990 32.693  1.00 24.93 ? 337  PHE A CZ  1 
ATOM   2692 N N   . THR A 1 338 ? 34.055 103.976 40.062  1.00 28.67 ? 338  THR A N   1 
ATOM   2693 C CA  . THR A 1 338 ? 33.681 103.967 41.453  1.00 29.65 ? 338  THR A CA  1 
ATOM   2694 C C   . THR A 1 338 ? 34.958 103.686 42.197  1.00 29.10 ? 338  THR A C   1 
ATOM   2695 O O   . THR A 1 338 ? 35.896 103.128 41.618  1.00 29.04 ? 338  THR A O   1 
ATOM   2696 C CB  . THR A 1 338 ? 32.705 102.820 41.794  1.00 28.90 ? 338  THR A CB  1 
ATOM   2697 O OG1 . THR A 1 338 ? 33.363 101.553 41.621  1.00 30.83 ? 338  THR A OG1 1 
ATOM   2698 C CG2 . THR A 1 338 ? 31.510 102.823 40.909  1.00 29.62 ? 338  THR A CG2 1 
ATOM   2699 N N   . TYR A 1 339 ? 35.007 104.069 43.468  1.00 28.73 ? 339  TYR A N   1 
ATOM   2700 C CA  . TYR A 1 339 ? 35.988 103.489 44.351  1.00 29.43 ? 339  TYR A CA  1 
ATOM   2701 C C   . TYR A 1 339 ? 35.313 102.912 45.603  1.00 29.88 ? 339  TYR A C   1 
ATOM   2702 O O   . TYR A 1 339 ? 34.212 103.288 45.946  1.00 29.60 ? 339  TYR A O   1 
ATOM   2703 C CB  . TYR A 1 339 ? 37.120 104.462 44.680  1.00 30.22 ? 339  TYR A CB  1 
ATOM   2704 C CG  . TYR A 1 339 ? 36.774 105.647 45.552  1.00 32.31 ? 339  TYR A CG  1 
ATOM   2705 C CD1 . TYR A 1 339 ? 36.986 105.600 46.921  1.00 32.08 ? 339  TYR A CD1 1 
ATOM   2706 C CD2 . TYR A 1 339 ? 36.267 106.838 44.993  1.00 32.94 ? 339  TYR A CD2 1 
ATOM   2707 C CE1 . TYR A 1 339 ? 36.690 106.694 47.730  1.00 34.96 ? 339  TYR A CE1 1 
ATOM   2708 C CE2 . TYR A 1 339 ? 35.976 107.953 45.796  1.00 34.49 ? 339  TYR A CE2 1 
ATOM   2709 C CZ  . TYR A 1 339 ? 36.187 107.866 47.159  1.00 33.78 ? 339  TYR A CZ  1 
ATOM   2710 O OH  . TYR A 1 339 ? 35.917 108.947 47.987  1.00 35.06 ? 339  TYR A OH  1 
ATOM   2711 N N   . ASP A 1 340 ? 35.990 101.970 46.228  1.00 30.64 ? 340  ASP A N   1 
ATOM   2712 C CA  . ASP A 1 340 ? 35.512 101.260 47.415  1.00 32.78 ? 340  ASP A CA  1 
ATOM   2713 C C   . ASP A 1 340 ? 35.592 102.202 48.622  1.00 32.62 ? 340  ASP A C   1 
ATOM   2714 O O   . ASP A 1 340 ? 36.665 102.459 49.143  1.00 32.96 ? 340  ASP A O   1 
ATOM   2715 C CB  . ASP A 1 340 ? 36.406 100.047 47.632  1.00 32.53 ? 340  ASP A CB  1 
ATOM   2716 C CG  . ASP A 1 340 ? 35.852 99.077  48.665  1.00 36.95 ? 340  ASP A CG  1 
ATOM   2717 O OD1 . ASP A 1 340 ? 35.077 99.503  49.560  1.00 40.65 ? 340  ASP A OD1 1 
ATOM   2718 O OD2 . ASP A 1 340 ? 36.210 97.884  48.580  1.00 41.46 ? 340  ASP A OD2 1 
ATOM   2719 N N   . SER A 1 341 ? 34.447 102.704 49.058  1.00 34.99 ? 341  SER A N   1 
ATOM   2720 C CA  . SER A 1 341 ? 34.388 103.668 50.164  1.00 36.24 ? 341  SER A CA  1 
ATOM   2721 C C   . SER A 1 341 ? 34.797 103.131 51.524  1.00 35.73 ? 341  SER A C   1 
ATOM   2722 O O   . SER A 1 341 ? 35.099 103.914 52.430  1.00 36.82 ? 341  SER A O   1 
ATOM   2723 C CB  . SER A 1 341 ? 33.006 104.316 50.249  1.00 37.05 ? 341  SER A CB  1 
ATOM   2724 O OG  . SER A 1 341 ? 31.994 103.329 50.398  1.00 41.17 ? 341  SER A OG  1 
ATOM   2725 N N   . VAL A 1 342 ? 34.858 101.816 51.686  1.00 35.04 ? 342  VAL A N   1 
ATOM   2726 C CA  . VAL A 1 342 ? 35.445 101.252 52.916  1.00 34.96 ? 342  VAL A CA  1 
ATOM   2727 C C   . VAL A 1 342 ? 36.931 100.940 52.733  1.00 33.53 ? 342  VAL A C   1 
ATOM   2728 O O   . VAL A 1 342 ? 37.782 101.525 53.406  1.00 34.02 ? 342  VAL A O   1 
ATOM   2729 C CB  . VAL A 1 342 ? 34.677 99.986  53.407  1.00 34.95 ? 342  VAL A CB  1 
ATOM   2730 C CG1 . VAL A 1 342 ? 35.422 99.317  54.573  1.00 37.44 ? 342  VAL A CG1 1 
ATOM   2731 C CG2 . VAL A 1 342 ? 33.274 100.356 53.814  1.00 37.85 ? 342  VAL A CG2 1 
ATOM   2732 N N   . ASP A 1 343 ? 37.276 100.042 51.813  1.00 32.16 ? 343  ASP A N   1 
ATOM   2733 C CA  . ASP A 1 343 ? 38.690 99.643  51.740  1.00 31.56 ? 343  ASP A CA  1 
ATOM   2734 C C   . ASP A 1 343 ? 39.542 100.752 51.154  1.00 30.36 ? 343  ASP A C   1 
ATOM   2735 O O   . ASP A 1 343 ? 40.740 100.827 51.464  1.00 30.38 ? 343  ASP A O   1 
ATOM   2736 C CB  . ASP A 1 343 ? 38.894 98.344  50.959  1.00 31.98 ? 343  ASP A CB  1 
ATOM   2737 C CG  . ASP A 1 343 ? 38.389 97.088  51.735  1.00 37.07 ? 343  ASP A CG  1 
ATOM   2738 O OD1 . ASP A 1 343 ? 38.346 97.113  52.993  1.00 40.86 ? 343  ASP A OD1 1 
ATOM   2739 O OD2 . ASP A 1 343 ? 38.023 96.086  51.069  1.00 41.48 ? 343  ASP A OD2 1 
ATOM   2740 N N   . PHE A 1 344 ? 38.931 101.583 50.319  1.00 29.24 ? 344  PHE A N   1 
ATOM   2741 C CA  . PHE A 1 344 ? 39.629 102.736 49.734  1.00 29.98 ? 344  PHE A CA  1 
ATOM   2742 C C   . PHE A 1 344 ? 39.099 104.063 50.243  1.00 30.17 ? 344  PHE A C   1 
ATOM   2743 O O   . PHE A 1 344 ? 39.066 105.064 49.535  1.00 29.95 ? 344  PHE A O   1 
ATOM   2744 C CB  . PHE A 1 344 ? 39.703 102.616 48.197  1.00 29.35 ? 344  PHE A CB  1 
ATOM   2745 C CG  . PHE A 1 344 ? 40.848 101.732 47.749  1.00 30.68 ? 344  PHE A CG  1 
ATOM   2746 C CD1 . PHE A 1 344 ? 40.750 100.342 47.850  1.00 29.86 ? 344  PHE A CD1 1 
ATOM   2747 C CD2 . PHE A 1 344 ? 42.048 102.297 47.284  1.00 30.52 ? 344  PHE A CD2 1 
ATOM   2748 C CE1 . PHE A 1 344 ? 41.834 99.506  47.448  1.00 30.32 ? 344  PHE A CE1 1 
ATOM   2749 C CE2 . PHE A 1 344 ? 43.120 101.481 46.894  1.00 32.00 ? 344  PHE A CE2 1 
ATOM   2750 C CZ  . PHE A 1 344 ? 43.011 100.091 46.975  1.00 30.43 ? 344  PHE A CZ  1 
ATOM   2751 N N   . LYS A 1 345 ? 38.682 104.059 51.508  1.00 31.23 ? 345  LYS A N   1 
ATOM   2752 C CA  . LYS A 1 345 ? 38.173 105.273 52.103  1.00 32.07 ? 345  LYS A CA  1 
ATOM   2753 C C   . LYS A 1 345 ? 39.340 106.245 52.166  1.00 31.16 ? 345  LYS A C   1 
ATOM   2754 O O   . LYS A 1 345 ? 40.463 105.870 52.556  1.00 31.66 ? 345  LYS A O   1 
ATOM   2755 C CB  . LYS A 1 345 ? 37.647 105.006 53.505  1.00 33.39 ? 345  LYS A CB  1 
ATOM   2756 C CG  . LYS A 1 345 ? 36.949 106.262 54.163  1.00 34.62 ? 345  LYS A CG  1 
ATOM   2757 C CD  . LYS A 1 345 ? 36.593 105.968 55.621  1.00 34.90 ? 345  LYS A CD  1 
ATOM   2758 C CE  . LYS A 1 345 ? 35.792 107.159 56.265  1.00 40.47 ? 345  LYS A CE  1 
ATOM   2759 N NZ  . LYS A 1 345 ? 35.844 107.082 57.803  1.00 43.70 ? 345  LYS A NZ  1 
ATOM   2760 N N   . GLY A 1 346 ? 39.100 107.478 51.757  1.00 30.50 ? 346  GLY A N   1 
ATOM   2761 C CA  . GLY A 1 346 ? 40.177 108.469 51.748  1.00 29.38 ? 346  GLY A CA  1 
ATOM   2762 C C   . GLY A 1 346 ? 40.970 108.458 50.452  1.00 29.34 ? 346  GLY A C   1 
ATOM   2763 O O   . GLY A 1 346 ? 42.088 109.026 50.386  1.00 28.32 ? 346  GLY A O   1 
ATOM   2764 N N   . PHE A 1 347 ? 40.427 107.812 49.430  1.00 28.93 ? 347  PHE A N   1 
ATOM   2765 C CA  . PHE A 1 347 ? 41.136 107.720 48.142  1.00 30.47 ? 347  PHE A CA  1 
ATOM   2766 C C   . PHE A 1 347 ? 41.487 109.140 47.626  1.00 30.56 ? 347  PHE A C   1 
ATOM   2767 O O   . PHE A 1 347 ? 42.630 109.369 47.279  1.00 30.62 ? 347  PHE A O   1 
ATOM   2768 C CB  . PHE A 1 347 ? 40.341 106.932 47.097  1.00 30.30 ? 347  PHE A CB  1 
ATOM   2769 C CG  . PHE A 1 347 ? 41.185 106.376 45.961  1.00 29.35 ? 347  PHE A CG  1 
ATOM   2770 C CD1 . PHE A 1 347 ? 42.542 106.087 46.137  1.00 30.07 ? 347  PHE A CD1 1 
ATOM   2771 C CD2 . PHE A 1 347 ? 40.603 106.090 44.748  1.00 29.12 ? 347  PHE A CD2 1 
ATOM   2772 C CE1 . PHE A 1 347 ? 43.314 105.534 45.058  1.00 31.09 ? 347  PHE A CE1 1 
ATOM   2773 C CE2 . PHE A 1 347 ? 41.360 105.547 43.666  1.00 30.33 ? 347  PHE A CE2 1 
ATOM   2774 C CZ  . PHE A 1 347 ? 42.706 105.289 43.830  1.00 28.77 ? 347  PHE A CZ  1 
ATOM   2775 N N   . PRO A 1 348 ? 40.518 110.102 47.620  1.00 30.69 ? 348  PRO A N   1 
ATOM   2776 C CA  . PRO A 1 348 ? 40.901 111.462 47.180  1.00 29.87 ? 348  PRO A CA  1 
ATOM   2777 C C   . PRO A 1 348 ? 42.041 112.122 47.941  1.00 29.33 ? 348  PRO A C   1 
ATOM   2778 O O   . PRO A 1 348 ? 42.863 112.796 47.301  1.00 29.57 ? 348  PRO A O   1 
ATOM   2779 C CB  . PRO A 1 348 ? 39.597 112.263 47.319  1.00 29.98 ? 348  PRO A CB  1 
ATOM   2780 C CG  . PRO A 1 348 ? 38.496 111.187 47.171  1.00 30.82 ? 348  PRO A CG  1 
ATOM   2781 C CD  . PRO A 1 348 ? 39.076 110.031 47.941  1.00 30.72 ? 348  PRO A CD  1 
ATOM   2782 N N   . GLU A 1 349 ? 42.112 111.958 49.266  1.00 29.32 ? 349  GLU A N   1 
ATOM   2783 C CA  . GLU A 1 349 ? 43.224 112.522 50.089  1.00 29.87 ? 349  GLU A CA  1 
ATOM   2784 C C   . GLU A 1 349 ? 44.571 111.916 49.695  1.00 28.45 ? 349  GLU A C   1 
ATOM   2785 O O   . GLU A 1 349 ? 45.610 112.605 49.644  1.00 27.55 ? 349  GLU A O   1 
ATOM   2786 C CB  . GLU A 1 349 ? 43.010 112.253 51.588  1.00 30.77 ? 349  GLU A CB  1 
ATOM   2787 C CG  . GLU A 1 349 ? 41.857 113.006 52.213  1.00 36.63 ? 349  GLU A CG  1 
ATOM   2788 C CD  . GLU A 1 349 ? 40.580 112.158 52.450  1.00 45.08 ? 349  GLU A CD  1 
ATOM   2789 O OE1 . GLU A 1 349 ? 39.807 111.907 51.457  1.00 48.61 ? 349  GLU A OE1 1 
ATOM   2790 O OE2 . GLU A 1 349 ? 40.337 111.785 53.640  1.00 43.78 ? 349  GLU A OE2 1 
ATOM   2791 N N   . PHE A 1 350 ? 44.569 110.605 49.490  1.00 27.73 ? 350  PHE A N   1 
ATOM   2792 C CA  . PHE A 1 350 ? 45.806 109.898 49.039  1.00 27.21 ? 350  PHE A CA  1 
ATOM   2793 C C   . PHE A 1 350 ? 46.347 110.467 47.704  1.00 26.23 ? 350  PHE A C   1 
ATOM   2794 O O   . PHE A 1 350 ? 47.547 110.625 47.497  1.00 27.88 ? 350  PHE A O   1 
ATOM   2795 C CB  . PHE A 1 350 ? 45.461 108.436 48.827  1.00 26.38 ? 350  PHE A CB  1 
ATOM   2796 C CG  . PHE A 1 350 ? 46.561 107.646 48.148  1.00 26.54 ? 350  PHE A CG  1 
ATOM   2797 C CD1 . PHE A 1 350 ? 47.728 107.349 48.823  1.00 27.63 ? 350  PHE A CD1 1 
ATOM   2798 C CD2 . PHE A 1 350 ? 46.401 107.194 46.849  1.00 26.13 ? 350  PHE A CD2 1 
ATOM   2799 C CE1 . PHE A 1 350 ? 48.724 106.602 48.205  1.00 28.08 ? 350  PHE A CE1 1 
ATOM   2800 C CE2 . PHE A 1 350 ? 47.380 106.451 46.234  1.00 26.71 ? 350  PHE A CE2 1 
ATOM   2801 C CZ  . PHE A 1 350 ? 48.546 106.166 46.905  1.00 26.81 ? 350  PHE A CZ  1 
ATOM   2802 N N   . VAL A 1 351 ? 45.444 110.736 46.802  1.00 26.44 ? 351  VAL A N   1 
ATOM   2803 C CA  . VAL A 1 351 ? 45.796 111.285 45.512  1.00 28.43 ? 351  VAL A CA  1 
ATOM   2804 C C   . VAL A 1 351 ? 46.373 112.673 45.690  1.00 27.30 ? 351  VAL A C   1 
ATOM   2805 O O   . VAL A 1 351 ? 47.322 113.004 45.018  1.00 26.52 ? 351  VAL A O   1 
ATOM   2806 C CB  . VAL A 1 351 ? 44.590 111.340 44.629  1.00 28.35 ? 351  VAL A CB  1 
ATOM   2807 C CG1 . VAL A 1 351 ? 44.908 112.056 43.363  1.00 30.95 ? 351  VAL A CG1 1 
ATOM   2808 C CG2 . VAL A 1 351 ? 44.151 109.900 44.325  1.00 29.84 ? 351  VAL A CG2 1 
ATOM   2809 N N   . ASN A 1 352 ? 45.789 113.497 46.575  1.00 26.47 ? 352  ASN A N   1 
ATOM   2810 C CA  . ASN A 1 352 ? 46.442 114.757 46.926  1.00 27.02 ? 352  ASN A CA  1 
ATOM   2811 C C   . ASN A 1 352 ? 47.859 114.546 47.444  1.00 25.58 ? 352  ASN A C   1 
ATOM   2812 O O   . ASN A 1 352 ? 48.744 115.317 47.114  1.00 25.23 ? 352  ASN A O   1 
ATOM   2813 C CB  . ASN A 1 352 ? 45.649 115.574 47.944  1.00 26.66 ? 352  ASN A CB  1 
ATOM   2814 C CG  . ASN A 1 352 ? 44.342 116.119 47.381  1.00 28.73 ? 352  ASN A CG  1 
ATOM   2815 O OD1 . ASN A 1 352 ? 44.023 115.969 46.203  1.00 28.86 ? 352  ASN A OD1 1 
ATOM   2816 N ND2 . ASN A 1 352 ? 43.569 116.763 48.247  1.00 30.02 ? 352  ASN A ND2 1 
ATOM   2817 N N   . GLU A 1 353 ? 48.055 113.548 48.303  1.00 26.40 ? 353  GLU A N   1 
ATOM   2818 C CA  . GLU A 1 353 ? 49.393 113.226 48.843  1.00 28.19 ? 353  GLU A CA  1 
ATOM   2819 C C   . GLU A 1 353 ? 50.375 112.814 47.730  1.00 25.93 ? 353  GLU A C   1 
ATOM   2820 O O   . GLU A 1 353 ? 51.500 113.314 47.680  1.00 25.78 ? 353  GLU A O   1 
ATOM   2821 C CB  . GLU A 1 353 ? 49.351 112.117 49.924  1.00 27.86 ? 353  GLU A CB  1 
ATOM   2822 C CG  . GLU A 1 353 ? 48.505 112.397 51.153  1.00 33.09 ? 353  GLU A CG  1 
ATOM   2823 C CD  . GLU A 1 353 ? 48.673 111.303 52.225  1.00 37.22 ? 353  GLU A CD  1 
ATOM   2824 O OE1 . GLU A 1 353 ? 49.809 111.234 52.801  1.00 46.23 ? 353  GLU A OE1 1 
ATOM   2825 O OE2 . GLU A 1 353 ? 47.697 110.512 52.473  1.00 45.34 ? 353  GLU A OE2 1 
ATOM   2826 N N   . LEU A 1 354 ? 49.978 111.903 46.854  1.00 26.03 ? 354  LEU A N   1 
ATOM   2827 C CA  . LEU A 1 354 ? 50.801 111.663 45.628  1.00 26.75 ? 354  LEU A CA  1 
ATOM   2828 C C   . LEU A 1 354 ? 51.182 112.958 44.909  1.00 26.61 ? 354  LEU A C   1 
ATOM   2829 O O   . LEU A 1 354 ? 52.340 113.207 44.677  1.00 26.86 ? 354  LEU A O   1 
ATOM   2830 C CB  . LEU A 1 354 ? 50.067 110.753 44.621  1.00 26.61 ? 354  LEU A CB  1 
ATOM   2831 C CG  . LEU A 1 354 ? 49.897 109.271 44.920  1.00 27.64 ? 354  LEU A CG  1 
ATOM   2832 C CD1 . LEU A 1 354 ? 49.001 108.660 43.827  1.00 26.56 ? 354  LEU A CD1 1 
ATOM   2833 C CD2 . LEU A 1 354 ? 51.262 108.550 45.021  1.00 26.93 ? 354  LEU A CD2 1 
ATOM   2834 N N   . HIS A 1 355 ? 50.190 113.784 44.548  1.00 27.30 ? 355  HIS A N   1 
ATOM   2835 C CA  . HIS A 1 355 ? 50.459 115.026 43.828  1.00 26.84 ? 355  HIS A CA  1 
ATOM   2836 C C   . HIS A 1 355 ? 51.396 115.945 44.586  1.00 27.59 ? 355  HIS A C   1 
ATOM   2837 O O   . HIS A 1 355 ? 52.301 116.521 44.006  1.00 26.42 ? 355  HIS A O   1 
ATOM   2838 C CB  . HIS A 1 355 ? 49.168 115.752 43.452  1.00 26.51 ? 355  HIS A CB  1 
ATOM   2839 C CG  . HIS A 1 355 ? 48.377 115.009 42.433  1.00 27.75 ? 355  HIS A CG  1 
ATOM   2840 N ND1 . HIS A 1 355 ? 47.049 115.253 42.199  1.00 25.62 ? 355  HIS A ND1 1 
ATOM   2841 C CD2 . HIS A 1 355 ? 48.736 114.005 41.592  1.00 27.13 ? 355  HIS A CD2 1 
ATOM   2842 C CE1 . HIS A 1 355 ? 46.612 114.443 41.249  1.00 30.45 ? 355  HIS A CE1 1 
ATOM   2843 N NE2 . HIS A 1 355 ? 47.616 113.661 40.878  1.00 32.12 ? 355  HIS A NE2 1 
ATOM   2844 N N   . ASN A 1 356 ? 51.207 116.037 45.896  1.00 27.89 ? 356  ASN A N   1 
ATOM   2845 C CA  A ASN A 1 356 ? 52.041 116.879 46.727  0.50 27.53 ? 356  ASN A CA  1 
ATOM   2846 C CA  B ASN A 1 356 ? 52.064 116.887 46.709  0.50 27.49 ? 356  ASN A CA  1 
ATOM   2847 C C   . ASN A 1 356 ? 53.488 116.401 46.737  1.00 27.59 ? 356  ASN A C   1 
ATOM   2848 O O   . ASN A 1 356 ? 54.404 117.197 46.921  1.00 27.43 ? 356  ASN A O   1 
ATOM   2849 C CB  A ASN A 1 356 ? 51.501 116.940 48.162  0.50 27.80 ? 356  ASN A CB  1 
ATOM   2850 C CB  B ASN A 1 356 ? 51.512 117.054 48.128  0.50 27.67 ? 356  ASN A CB  1 
ATOM   2851 C CG  A ASN A 1 356 ? 52.149 118.025 48.958  0.50 27.77 ? 356  ASN A CG  1 
ATOM   2852 C CG  B ASN A 1 356 ? 50.296 117.909 48.140  0.50 27.74 ? 356  ASN A CG  1 
ATOM   2853 O OD1 A ASN A 1 356 ? 52.286 119.145 48.476  0.50 30.36 ? 356  ASN A OD1 1 
ATOM   2854 O OD1 B ASN A 1 356 ? 49.998 118.548 47.134  0.50 31.15 ? 356  ASN A OD1 1 
ATOM   2855 N ND2 A ASN A 1 356 ? 52.592 117.704 50.162  0.50 31.29 ? 356  ASN A ND2 1 
ATOM   2856 N ND2 B ASN A 1 356 ? 49.562 117.914 49.233  0.50 27.55 ? 356  ASN A ND2 1 
ATOM   2857 N N   . ASN A 1 357 ? 53.684 115.105 46.536  1.00 26.77 ? 357  ASN A N   1 
ATOM   2858 C CA  . ASN A 1 357 ? 55.059 114.570 46.489  1.00 27.98 ? 357  ASN A CA  1 
ATOM   2859 C C   . ASN A 1 357 ? 55.610 114.496 45.055  1.00 27.64 ? 357  ASN A C   1 
ATOM   2860 O O   . ASN A 1 357 ? 56.634 113.842 44.807  1.00 28.58 ? 357  ASN A O   1 
ATOM   2861 C CB  . ASN A 1 357 ? 55.113 113.199 47.150  1.00 28.50 ? 357  ASN A CB  1 
ATOM   2862 C CG  . ASN A 1 357 ? 54.829 113.272 48.637  1.00 32.06 ? 357  ASN A CG  1 
ATOM   2863 O OD1 . ASN A 1 357 ? 54.118 112.440 49.170  1.00 37.93 ? 357  ASN A OD1 1 
ATOM   2864 N ND2 . ASN A 1 357 ? 55.356 114.299 49.306  1.00 36.69 ? 357  ASN A ND2 1 
ATOM   2865 N N   . GLY A 1 358 ? 54.913 115.125 44.127  1.00 26.22 ? 358  GLY A N   1 
ATOM   2866 C CA  . GLY A 1 358 ? 55.352 115.204 42.727  1.00 26.16 ? 358  GLY A CA  1 
ATOM   2867 C C   . GLY A 1 358 ? 55.097 113.957 41.914  1.00 25.70 ? 358  GLY A C   1 
ATOM   2868 O O   . GLY A 1 358 ? 55.725 113.751 40.865  1.00 26.20 ? 358  GLY A O   1 
ATOM   2869 N N   . GLN A 1 359 ? 54.183 113.116 42.378  1.00 23.79 ? 359  GLN A N   1 
ATOM   2870 C CA  . GLN A 1 359 ? 53.913 111.831 41.730  1.00 23.59 ? 359  GLN A CA  1 
ATOM   2871 C C   . GLN A 1 359 ? 52.560 111.867 41.068  1.00 23.01 ? 359  GLN A C   1 
ATOM   2872 O O   . GLN A 1 359 ? 51.832 112.818 41.250  1.00 22.24 ? 359  GLN A O   1 
ATOM   2873 C CB  . GLN A 1 359 ? 53.933 110.697 42.759  1.00 24.91 ? 359  GLN A CB  1 
ATOM   2874 C CG  . GLN A 1 359 ? 55.299 110.458 43.372  1.00 22.89 ? 359  GLN A CG  1 
ATOM   2875 C CD  . GLN A 1 359 ? 55.224 109.412 44.467  1.00 29.43 ? 359  GLN A CD  1 
ATOM   2876 O OE1 . GLN A 1 359 ? 54.470 109.578 45.466  1.00 28.12 ? 359  GLN A OE1 1 
ATOM   2877 N NE2 . GLN A 1 359 ? 56.018 108.330 44.312  1.00 25.23 ? 359  GLN A NE2 1 
ATOM   2878 N N   . LYS A 1 360 ? 52.211 110.798 40.350  1.00 21.55 ? 360  LYS A N   1 
ATOM   2879 C CA  . LYS A 1 360 ? 51.116 110.792 39.408  1.00 21.15 ? 360  LYS A CA  1 
ATOM   2880 C C   . LYS A 1 360 ? 50.347 109.527 39.728  1.00 21.69 ? 360  LYS A C   1 
ATOM   2881 O O   . LYS A 1 360 ? 50.919 108.562 40.216  1.00 22.42 ? 360  LYS A O   1 
ATOM   2882 C CB  . LYS A 1 360 ? 51.639 110.726 37.957  1.00 21.92 ? 360  LYS A CB  1 
ATOM   2883 C CG  . LYS A 1 360 ? 52.468 111.970 37.522  1.00 19.63 ? 360  LYS A CG  1 
ATOM   2884 C CD  . LYS A 1 360 ? 51.571 113.227 37.604  1.00 24.08 ? 360  LYS A CD  1 
ATOM   2885 C CE  . LYS A 1 360 ? 52.312 114.505 37.195  1.00 28.76 ? 360  LYS A CE  1 
ATOM   2886 N NZ  . LYS A 1 360 ? 51.300 115.617 36.963  1.00 32.18 ? 360  LYS A NZ  1 
ATOM   2887 N N   . LEU A 1 361 ? 49.060 109.536 39.456  1.00 22.37 ? 361  LEU A N   1 
ATOM   2888 C CA  . LEU A 1 361 ? 48.227 108.354 39.646  1.00 23.84 ? 361  LEU A CA  1 
ATOM   2889 C C   . LEU A 1 361 ? 47.656 107.920 38.329  1.00 24.02 ? 361  LEU A C   1 
ATOM   2890 O O   . LEU A 1 361 ? 47.022 108.727 37.606  1.00 25.16 ? 361  LEU A O   1 
ATOM   2891 C CB  . LEU A 1 361 ? 47.063 108.665 40.602  1.00 23.99 ? 361  LEU A CB  1 
ATOM   2892 C CG  . LEU A 1 361 ? 46.073 107.483 40.781  1.00 25.59 ? 361  LEU A CG  1 
ATOM   2893 C CD1 . LEU A 1 361 ? 46.608 106.378 41.691  1.00 24.63 ? 361  LEU A CD1 1 
ATOM   2894 C CD2 . LEU A 1 361 ? 44.754 108.037 41.286  1.00 25.64 ? 361  LEU A CD2 1 
ATOM   2895 N N   . VAL A 1 362 ? 47.892 106.654 38.002  1.00 23.40 ? 362  VAL A N   1 
ATOM   2896 C CA  . VAL A 1 362 ? 47.267 106.031 36.866  1.00 23.16 ? 362  VAL A CA  1 
ATOM   2897 C C   . VAL A 1 362 ? 46.276 104.974 37.364  1.00 24.12 ? 362  VAL A C   1 
ATOM   2898 O O   . VAL A 1 362 ? 46.624 104.138 38.190  1.00 25.78 ? 362  VAL A O   1 
ATOM   2899 C CB  . VAL A 1 362 ? 48.295 105.386 35.911  1.00 22.00 ? 362  VAL A CB  1 
ATOM   2900 C CG1 . VAL A 1 362 ? 47.571 104.504 34.837  1.00 20.81 ? 362  VAL A CG1 1 
ATOM   2901 C CG2 . VAL A 1 362 ? 49.112 106.470 35.211  1.00 20.61 ? 362  VAL A CG2 1 
ATOM   2902 N N   . ILE A 1 363 ? 45.058 105.010 36.844  1.00 23.92 ? 363  ILE A N   1 
ATOM   2903 C CA  . ILE A 1 363 ? 43.979 104.102 37.271  1.00 23.05 ? 363  ILE A CA  1 
ATOM   2904 C C   . ILE A 1 363 ? 43.645 103.196 36.127  1.00 23.16 ? 363  ILE A C   1 
ATOM   2905 O O   . ILE A 1 363 ? 43.747 103.623 34.957  1.00 21.93 ? 363  ILE A O   1 
ATOM   2906 C CB  . ILE A 1 363 ? 42.715 104.883 37.701  1.00 23.18 ? 363  ILE A CB  1 
ATOM   2907 C CG1 . ILE A 1 363 ? 42.177 105.765 36.539  1.00 24.01 ? 363  ILE A CG1 1 
ATOM   2908 C CG2 . ILE A 1 363 ? 43.037 105.600 39.033  1.00 21.67 ? 363  ILE A CG2 1 
ATOM   2909 C CD1 . ILE A 1 363 ? 40.695 106.243 36.718  1.00 23.70 ? 363  ILE A CD1 1 
ATOM   2910 N N   . ILE A 1 364 ? 43.299 101.941 36.452  1.00 22.49 ? 364  ILE A N   1 
ATOM   2911 C CA  . ILE A 1 364 ? 42.920 100.981 35.455  1.00 23.15 ? 364  ILE A CA  1 
ATOM   2912 C C   . ILE A 1 364 ? 41.469 101.247 35.161  1.00 24.84 ? 364  ILE A C   1 
ATOM   2913 O O   . ILE A 1 364 ? 40.700 101.659 36.074  1.00 25.10 ? 364  ILE A O   1 
ATOM   2914 C CB  . ILE A 1 364 ? 43.139 99.507  35.895  1.00 23.87 ? 364  ILE A CB  1 
ATOM   2915 C CG1 . ILE A 1 364 ? 42.986 98.530  34.710  1.00 25.01 ? 364  ILE A CG1 1 
ATOM   2916 C CG2 . ILE A 1 364 ? 42.156 99.049  37.025  1.00 22.54 ? 364  ILE A CG2 1 
ATOM   2917 C CD1 . ILE A 1 364 ? 43.601 97.106  35.046  1.00 24.37 ? 364  ILE A CD1 1 
ATOM   2918 N N   . VAL A 1 365 ? 41.085 101.026 33.912  1.00 24.05 ? 365  VAL A N   1 
ATOM   2919 C CA  . VAL A 1 365 ? 39.669 101.105 33.513  1.00 26.11 ? 365  VAL A CA  1 
ATOM   2920 C C   . VAL A 1 365 ? 39.449 99.979  32.527  1.00 26.04 ? 365  VAL A C   1 
ATOM   2921 O O   . VAL A 1 365 ? 40.194 99.823  31.563  1.00 27.48 ? 365  VAL A O   1 
ATOM   2922 C CB  . VAL A 1 365 ? 39.327 102.476 32.900  1.00 26.55 ? 365  VAL A CB  1 
ATOM   2923 C CG1 . VAL A 1 365 ? 37.853 102.564 32.553  1.00 28.76 ? 365  VAL A CG1 1 
ATOM   2924 C CG2 . VAL A 1 365 ? 39.649 103.615 33.938  1.00 25.79 ? 365  VAL A CG2 1 
ATOM   2925 N N   . ASP A 1 366 ? 38.470 99.139  32.784  1.00 26.11 ? 366  ASP A N   1 
ATOM   2926 C CA  . ASP A 1 366 ? 38.156 98.085  31.843  1.00 26.59 ? 366  ASP A CA  1 
ATOM   2927 C C   . ASP A 1 366 ? 37.059 98.524  30.891  1.00 25.97 ? 366  ASP A C   1 
ATOM   2928 O O   . ASP A 1 366 ? 36.273 99.400  31.205  1.00 25.84 ? 366  ASP A O   1 
ATOM   2929 C CB  . ASP A 1 366 ? 37.776 96.825  32.618  1.00 28.18 ? 366  ASP A CB  1 
ATOM   2930 C CG  . ASP A 1 366 ? 38.885 96.381  33.531  1.00 31.45 ? 366  ASP A CG  1 
ATOM   2931 O OD1 . ASP A 1 366 ? 40.007 96.191  33.040  1.00 34.68 ? 366  ASP A OD1 1 
ATOM   2932 O OD2 . ASP A 1 366 ? 38.642 96.275  34.752  1.00 38.30 ? 366  ASP A OD2 1 
ATOM   2933 N N   . PRO A 1 367 ? 36.968 97.894  29.733  1.00 25.46 ? 367  PRO A N   1 
ATOM   2934 C CA  . PRO A 1 367 ? 35.873 98.330  28.894  1.00 25.25 ? 367  PRO A CA  1 
ATOM   2935 C C   . PRO A 1 367 ? 34.494 97.824  29.384  1.00 26.81 ? 367  PRO A C   1 
ATOM   2936 O O   . PRO A 1 367 ? 33.533 98.595  29.309  1.00 28.34 ? 367  PRO A O   1 
ATOM   2937 C CB  . PRO A 1 367 ? 36.204 97.696  27.552  1.00 24.94 ? 367  PRO A CB  1 
ATOM   2938 C CG  . PRO A 1 367 ? 36.924 96.454  27.910  1.00 25.02 ? 367  PRO A CG  1 
ATOM   2939 C CD  . PRO A 1 367 ? 37.734 96.802  29.120  1.00 24.47 ? 367  PRO A CD  1 
ATOM   2940 N N   . ALA A 1 368 ? 34.389 96.598  29.906  1.00 26.56 ? 368  ALA A N   1 
ATOM   2941 C CA  . ALA A 1 368 ? 33.045 96.038  30.233  1.00 28.23 ? 368  ALA A CA  1 
ATOM   2942 C C   . ALA A 1 368 ? 32.374 96.732  31.436  1.00 28.13 ? 368  ALA A C   1 
ATOM   2943 O O   . ALA A 1 368 ? 33.016 97.018  32.450  1.00 29.45 ? 368  ALA A O   1 
ATOM   2944 C CB  . ALA A 1 368 ? 33.091 94.542  30.434  1.00 27.50 ? 368  ALA A CB  1 
ATOM   2945 N N   . ILE A 1 369 ? 31.075 96.981  31.301  1.00 27.40 ? 369  ILE A N   1 
ATOM   2946 C CA  . ILE A 1 369 ? 30.306 97.796  32.252  1.00 27.51 ? 369  ILE A CA  1 
ATOM   2947 C C   . ILE A 1 369 ? 29.229 96.870  32.909  1.00 27.58 ? 369  ILE A C   1 
ATOM   2948 O O   . ILE A 1 369 ? 28.441 96.219  32.214  1.00 25.95 ? 369  ILE A O   1 
ATOM   2949 C CB  . ILE A 1 369 ? 29.662 99.023  31.514  1.00 26.80 ? 369  ILE A CB  1 
ATOM   2950 C CG1 . ILE A 1 369 ? 30.728 99.987  30.913  1.00 26.16 ? 369  ILE A CG1 1 
ATOM   2951 C CG2 . ILE A 1 369 ? 28.706 99.801  32.410  1.00 29.68 ? 369  ILE A CG2 1 
ATOM   2952 C CD1 . ILE A 1 369 ? 31.697 100.690 31.947  1.00 24.82 ? 369  ILE A CD1 1 
ATOM   2953 N N   . SER A 1 370 ? 29.238 96.767  34.233  1.00 28.09 ? 370  SER A N   1 
ATOM   2954 C CA  . SER A 1 370 ? 28.170 95.990  34.938  1.00 28.76 ? 370  SER A CA  1 
ATOM   2955 C C   . SER A 1 370 ? 26.755 96.397  34.461  1.00 29.21 ? 370  SER A C   1 
ATOM   2956 O O   . SER A 1 370 ? 26.460 97.577  34.414  1.00 28.99 ? 370  SER A O   1 
ATOM   2957 C CB  . SER A 1 370 ? 28.318 96.212  36.439  1.00 28.86 ? 370  SER A CB  1 
ATOM   2958 O OG  . SER A 1 370 ? 27.293 95.572  37.171  1.00 31.09 ? 370  SER A OG  1 
ATOM   2959 N N   . ASN A 1 371 ? 25.898 95.430  34.107  1.00 29.89 ? 371  ASN A N   1 
ATOM   2960 C CA  . ASN A 1 371 ? 24.495 95.752  33.763  1.00 32.18 ? 371  ASN A CA  1 
ATOM   2961 C C   . ASN A 1 371 ? 23.535 95.650  34.972  1.00 33.30 ? 371  ASN A C   1 
ATOM   2962 O O   . ASN A 1 371 ? 22.341 95.540  34.801  1.00 33.40 ? 371  ASN A O   1 
ATOM   2963 C CB  . ASN A 1 371 ? 23.987 94.887  32.608  1.00 31.31 ? 371  ASN A CB  1 
ATOM   2964 C CG  . ASN A 1 371 ? 23.878 93.416  32.995  1.00 33.00 ? 371  ASN A CG  1 
ATOM   2965 O OD1 . ASN A 1 371 ? 24.332 93.037  34.063  1.00 35.54 ? 371  ASN A OD1 1 
ATOM   2966 N ND2 . ASN A 1 371 ? 23.322 92.583  32.115  1.00 30.43 ? 371  ASN A ND2 1 
ATOM   2967 N N   . ASN A 1 372 ? 24.093 95.674  36.172  1.00 34.83 ? 372  ASN A N   1 
ATOM   2968 C CA  . ASN A 1 372 ? 23.341 95.553  37.400  1.00 37.36 ? 372  ASN A CA  1 
ATOM   2969 C C   . ASN A 1 372 ? 23.023 96.911  37.948  1.00 38.32 ? 372  ASN A C   1 
ATOM   2970 O O   . ASN A 1 372 ? 23.840 97.532  38.628  1.00 38.59 ? 372  ASN A O   1 
ATOM   2971 C CB  . ASN A 1 372 ? 24.105 94.733  38.442  1.00 37.64 ? 372  ASN A CB  1 
ATOM   2972 C CG  . ASN A 1 372 ? 23.178 94.207  39.562  1.00 40.10 ? 372  ASN A CG  1 
ATOM   2973 O OD1 . ASN A 1 372 ? 22.252 94.906  39.992  1.00 43.73 ? 372  ASN A OD1 1 
ATOM   2974 N ND2 . ASN A 1 372 ? 23.422 92.997  40.014  1.00 41.63 ? 372  ASN A ND2 1 
ATOM   2975 N N   . SER A 1 373 ? 21.830 97.373  37.619  1.00 40.47 ? 373  SER A N   1 
ATOM   2976 C CA  . SER A 1 373 ? 21.366 98.705  38.003  1.00 42.80 ? 373  SER A CA  1 
ATOM   2977 C C   . SER A 1 373 ? 19.855 98.654  38.288  1.00 44.80 ? 373  SER A C   1 
ATOM   2978 O O   . SER A 1 373 ? 19.097 98.097  37.500  1.00 45.63 ? 373  SER A O   1 
ATOM   2979 C CB  . SER A 1 373 ? 21.647 99.697  36.872  1.00 41.27 ? 373  SER A CB  1 
ATOM   2980 O OG  . SER A 1 373 ? 21.342 101.013 37.275  1.00 41.98 ? 373  SER A OG  1 
ATOM   2981 N N   . SER A 1 374 ? 19.430 99.253  39.394  1.00 46.93 ? 374  SER A N   1 
ATOM   2982 C CA  . SER A 1 374 ? 18.015 99.347  39.742  1.00 49.93 ? 374  SER A CA  1 
ATOM   2983 C C   . SER A 1 374 ? 17.755 100.739 40.303  1.00 51.54 ? 374  SER A C   1 
ATOM   2984 O O   . SER A 1 374 ? 18.697 101.521 40.515  1.00 51.97 ? 374  SER A O   1 
ATOM   2985 C CB  . SER A 1 374 ? 17.630 98.271  40.762  1.00 49.60 ? 374  SER A CB  1 
ATOM   2986 O OG  . SER A 1 374 ? 18.441 98.360  41.929  1.00 50.70 ? 374  SER A OG  1 
ATOM   2987 N N   . SER A 1 375 ? 16.482 101.052 40.541  1.00 53.78 ? 375  SER A N   1 
ATOM   2988 C CA  . SER A 1 375 ? 16.073 102.337 41.132  1.00 55.05 ? 375  SER A CA  1 
ATOM   2989 C C   . SER A 1 375 ? 16.592 102.419 42.577  1.00 55.61 ? 375  SER A C   1 
ATOM   2990 O O   . SER A 1 375 ? 16.999 103.491 43.061  1.00 56.05 ? 375  SER A O   1 
ATOM   2991 C CB  . SER A 1 375 ? 14.549 102.454 41.081  1.00 55.90 ? 375  SER A CB  1 
ATOM   2992 O OG  . SER A 1 375 ? 14.041 101.908 39.862  1.00 57.38 ? 375  SER A OG  1 
ATOM   2993 N N   . SER A 1 376 ? 16.592 101.262 43.243  1.00 55.60 ? 376  SER A N   1 
ATOM   2994 C CA  . SER A 1 376 ? 17.163 101.099 44.567  1.00 55.59 ? 376  SER A CA  1 
ATOM   2995 C C   . SER A 1 376 ? 18.640 101.487 44.556  1.00 54.74 ? 376  SER A C   1 
ATOM   2996 O O   . SER A 1 376 ? 19.042 102.480 45.195  1.00 55.24 ? 376  SER A O   1 
ATOM   2997 C CB  . SER A 1 376 ? 16.987 99.645  45.026  1.00 56.33 ? 376  SER A CB  1 
ATOM   2998 O OG  . SER A 1 376 ? 18.002 99.276  45.958  1.00 58.03 ? 376  SER A OG  1 
ATOM   2999 N N   . LYS A 1 377 ? 19.443 100.715 43.815  1.00 53.44 ? 377  LYS A N   1 
ATOM   3000 C CA  . LYS A 1 377 ? 20.873 100.991 43.681  1.00 51.42 ? 377  LYS A CA  1 
ATOM   3001 C C   . LYS A 1 377 ? 21.281 101.174 42.203  1.00 49.40 ? 377  LYS A C   1 
ATOM   3002 O O   . LYS A 1 377 ? 21.564 100.204 41.499  1.00 48.21 ? 377  LYS A O   1 
ATOM   3003 C CB  . LYS A 1 377 ? 21.718 99.942  44.411  1.00 52.51 ? 377  LYS A CB  1 
ATOM   3004 C CG  . LYS A 1 377 ? 22.149 100.375 45.828  1.00 54.45 ? 377  LYS A CG  1 
ATOM   3005 C CD  . LYS A 1 377 ? 21.158 99.945  46.931  1.00 56.23 ? 377  LYS A CD  1 
ATOM   3006 C CE  . LYS A 1 377 ? 21.803 100.084 48.323  1.00 56.00 ? 377  LYS A CE  1 
ATOM   3007 N NZ  . LYS A 1 377 ? 20.876 99.787  49.468  1.00 57.57 ? 377  LYS A NZ  1 
ATOM   3008 N N   . PRO A 1 378 ? 21.261 102.428 41.723  1.00 47.10 ? 378  PRO A N   1 
ATOM   3009 C CA  . PRO A 1 378 ? 21.568 102.655 40.318  1.00 45.44 ? 378  PRO A CA  1 
ATOM   3010 C C   . PRO A 1 378 ? 23.081 102.578 40.087  1.00 42.99 ? 378  PRO A C   1 
ATOM   3011 O O   . PRO A 1 378 ? 23.871 102.840 40.996  1.00 42.54 ? 378  PRO A O   1 
ATOM   3012 C CB  . PRO A 1 378 ? 21.064 104.096 40.070  1.00 45.58 ? 378  PRO A CB  1 
ATOM   3013 C CG  . PRO A 1 378 ? 20.366 104.510 41.344  1.00 46.51 ? 378  PRO A CG  1 
ATOM   3014 C CD  . PRO A 1 378 ? 20.985 103.691 42.421  1.00 47.11 ? 378  PRO A CD  1 
ATOM   3015 N N   . TYR A 1 379 ? 23.470 102.194 38.875  1.00 40.49 ? 379  TYR A N   1 
ATOM   3016 C CA  . TYR A 1 379 ? 24.866 102.273 38.475  1.00 36.84 ? 379  TYR A CA  1 
ATOM   3017 C C   . TYR A 1 379 ? 24.899 103.197 37.252  1.00 35.31 ? 379  TYR A C   1 
ATOM   3018 O O   . TYR A 1 379 ? 24.470 102.814 36.149  1.00 33.84 ? 379  TYR A O   1 
ATOM   3019 C CB  . TYR A 1 379 ? 25.445 100.864 38.236  1.00 35.38 ? 379  TYR A CB  1 
ATOM   3020 C CG  . TYR A 1 379 ? 26.904 100.849 37.781  1.00 33.87 ? 379  TYR A CG  1 
ATOM   3021 C CD1 . TYR A 1 379 ? 27.924 101.490 38.528  1.00 31.09 ? 379  TYR A CD1 1 
ATOM   3022 C CD2 . TYR A 1 379 ? 27.256 100.194 36.601  1.00 32.58 ? 379  TYR A CD2 1 
ATOM   3023 C CE1 . TYR A 1 379 ? 29.268 101.459 38.073  1.00 31.97 ? 379  TYR A CE1 1 
ATOM   3024 C CE2 . TYR A 1 379 ? 28.576 100.166 36.140  1.00 31.09 ? 379  TYR A CE2 1 
ATOM   3025 C CZ  . TYR A 1 379 ? 29.570 100.796 36.869  1.00 32.90 ? 379  TYR A CZ  1 
ATOM   3026 O OH  . TYR A 1 379 ? 30.850 100.734 36.371  1.00 29.84 ? 379  TYR A OH  1 
ATOM   3027 N N   . GLY A 1 380 ? 25.349 104.431 37.497  1.00 33.74 ? 380  GLY A N   1 
ATOM   3028 C CA  . GLY A 1 380 ? 25.256 105.518 36.508  1.00 33.26 ? 380  GLY A CA  1 
ATOM   3029 C C   . GLY A 1 380 ? 25.837 105.237 35.121  1.00 32.13 ? 380  GLY A C   1 
ATOM   3030 O O   . GLY A 1 380 ? 25.188 105.520 34.114  1.00 32.94 ? 380  GLY A O   1 
ATOM   3031 N N   . PRO A 1 381 ? 27.088 104.699 35.047  1.00 30.88 ? 381  PRO A N   1 
ATOM   3032 C CA  . PRO A 1 381 ? 27.675 104.362 33.722  1.00 30.60 ? 381  PRO A CA  1 
ATOM   3033 C C   . PRO A 1 381 ? 26.816 103.445 32.860  1.00 30.00 ? 381  PRO A C   1 
ATOM   3034 O O   . PRO A 1 381 ? 26.717 103.669 31.653  1.00 29.06 ? 381  PRO A O   1 
ATOM   3035 C CB  . PRO A 1 381 ? 28.987 103.621 34.101  1.00 29.25 ? 381  PRO A CB  1 
ATOM   3036 C CG  . PRO A 1 381 ? 29.374 104.225 35.368  1.00 29.25 ? 381  PRO A CG  1 
ATOM   3037 C CD  . PRO A 1 381 ? 28.036 104.393 36.127  1.00 29.68 ? 381  PRO A CD  1 
ATOM   3038 N N   . TYR A 1 382 ? 26.238 102.400 33.456  1.00 30.31 ? 382  TYR A N   1 
ATOM   3039 C CA  . TYR A 1 382 ? 25.310 101.546 32.711  1.00 32.36 ? 382  TYR A CA  1 
ATOM   3040 C C   . TYR A 1 382 ? 24.082 102.343 32.291  1.00 32.95 ? 382  TYR A C   1 
ATOM   3041 O O   . TYR A 1 382 ? 23.648 102.266 31.147  1.00 34.06 ? 382  TYR A O   1 
ATOM   3042 C CB  . TYR A 1 382 ? 24.875 100.315 33.516  1.00 32.04 ? 382  TYR A CB  1 
ATOM   3043 C CG  . TYR A 1 382 ? 23.935 99.437  32.751  1.00 33.31 ? 382  TYR A CG  1 
ATOM   3044 C CD1 . TYR A 1 382 ? 24.375 98.714  31.650  1.00 29.93 ? 382  TYR A CD1 1 
ATOM   3045 C CD2 . TYR A 1 382 ? 22.598 99.333  33.122  1.00 32.93 ? 382  TYR A CD2 1 
ATOM   3046 C CE1 . TYR A 1 382 ? 23.543 97.929  30.938  1.00 32.12 ? 382  TYR A CE1 1 
ATOM   3047 C CE2 . TYR A 1 382 ? 21.738 98.552  32.420  1.00 34.29 ? 382  TYR A CE2 1 
ATOM   3048 C CZ  . TYR A 1 382 ? 22.205 97.840  31.329  1.00 35.18 ? 382  TYR A CZ  1 
ATOM   3049 O OH  . TYR A 1 382 ? 21.355 97.043  30.608  1.00 37.22 ? 382  TYR A OH  1 
ATOM   3050 N N   . ASP A 1 383 ? 23.524 103.102 33.218  1.00 33.95 ? 383  ASP A N   1 
ATOM   3051 C CA  . ASP A 1 383 ? 22.290 103.830 32.932  1.00 35.26 ? 383  ASP A CA  1 
ATOM   3052 C C   . ASP A 1 383 ? 22.538 104.829 31.816  1.00 34.65 ? 383  ASP A C   1 
ATOM   3053 O O   . ASP A 1 383 ? 21.787 104.894 30.866  1.00 35.14 ? 383  ASP A O   1 
ATOM   3054 C CB  . ASP A 1 383 ? 21.823 104.594 34.175  1.00 36.20 ? 383  ASP A CB  1 
ATOM   3055 C CG  . ASP A 1 383 ? 21.311 103.685 35.292  1.00 37.54 ? 383  ASP A CG  1 
ATOM   3056 O OD1 . ASP A 1 383 ? 20.892 102.533 35.029  1.00 39.37 ? 383  ASP A OD1 1 
ATOM   3057 O OD2 . ASP A 1 383 ? 21.330 104.166 36.449  1.00 40.25 ? 383  ASP A OD2 1 
ATOM   3058 N N   . ARG A 1 384 ? 23.605 105.618 31.948  1.00 34.75 ? 384  ARG A N   1 
ATOM   3059 C CA  . ARG A 1 384 ? 23.976 106.597 30.915  1.00 33.73 ? 384  ARG A CA  1 
ATOM   3060 C C   . ARG A 1 384 ? 24.325 105.984 29.567  1.00 33.38 ? 384  ARG A C   1 
ATOM   3061 O O   . ARG A 1 384 ? 23.999 106.546 28.521  1.00 33.44 ? 384  ARG A O   1 
ATOM   3062 C CB  . ARG A 1 384 ? 25.106 107.489 31.408  1.00 33.57 ? 384  ARG A CB  1 
ATOM   3063 C CG  . ARG A 1 384 ? 24.705 108.404 32.510  1.00 33.78 ? 384  ARG A CG  1 
ATOM   3064 C CD  . ARG A 1 384 ? 25.833 109.308 32.994  1.00 33.48 ? 384  ARG A CD  1 
ATOM   3065 N NE  . ARG A 1 384 ? 26.852 108.590 33.774  1.00 36.48 ? 384  ARG A NE  1 
ATOM   3066 C CZ  . ARG A 1 384 ? 26.928 108.579 35.098  1.00 35.22 ? 384  ARG A CZ  1 
ATOM   3067 N NH1 . ARG A 1 384 ? 26.035 109.238 35.828  1.00 36.29 ? 384  ARG A NH1 1 
ATOM   3068 N NH2 . ARG A 1 384 ? 27.908 107.921 35.700  1.00 35.07 ? 384  ARG A NH2 1 
ATOM   3069 N N   . GLY A 1 385 ? 24.970 104.819 29.572  1.00 33.47 ? 385  GLY A N   1 
ATOM   3070 C CA  . GLY A 1 385 ? 25.338 104.162 28.320  1.00 33.00 ? 385  GLY A CA  1 
ATOM   3071 C C   . GLY A 1 385 ? 24.125 103.602 27.643  1.00 33.37 ? 385  GLY A C   1 
ATOM   3072 O O   . GLY A 1 385 ? 24.023 103.585 26.415  1.00 31.50 ? 385  GLY A O   1 
ATOM   3073 N N   . SER A 1 386 ? 23.191 103.127 28.457  1.00 34.88 ? 386  SER A N   1 
ATOM   3074 C CA  . SER A 1 386 ? 21.974 102.525 27.897  1.00 37.12 ? 386  SER A CA  1 
ATOM   3075 C C   . SER A 1 386 ? 21.066 103.606 27.313  1.00 37.83 ? 386  SER A C   1 
ATOM   3076 O O   . SER A 1 386 ? 20.461 103.396 26.274  1.00 39.20 ? 386  SER A O   1 
ATOM   3077 C CB  . SER A 1 386 ? 21.235 101.680 28.939  1.00 37.06 ? 386  SER A CB  1 
ATOM   3078 O OG  . SER A 1 386 ? 22.118 100.770 29.570  1.00 37.32 ? 386  SER A OG  1 
ATOM   3079 N N   . ASP A 1 387 ? 20.992 104.758 27.965  1.00 39.37 ? 387  ASP A N   1 
ATOM   3080 C CA  . ASP A 1 387 ? 20.260 105.890 27.408  1.00 40.93 ? 387  ASP A CA  1 
ATOM   3081 C C   . ASP A 1 387 ? 20.853 106.315 26.058  1.00 41.25 ? 387  ASP A C   1 
ATOM   3082 O O   . ASP A 1 387 ? 20.126 106.738 25.152  1.00 41.23 ? 387  ASP A O   1 
ATOM   3083 C CB  . ASP A 1 387 ? 20.282 107.087 28.361  1.00 41.49 ? 387  ASP A CB  1 
ATOM   3084 C CG  . ASP A 1 387 ? 19.525 106.830 29.678  1.00 46.74 ? 387  ASP A CG  1 
ATOM   3085 O OD1 . ASP A 1 387 ? 18.749 105.830 29.777  1.00 48.17 ? 387  ASP A OD1 1 
ATOM   3086 O OD2 . ASP A 1 387 ? 19.733 107.649 30.629  1.00 51.37 ? 387  ASP A OD2 1 
ATOM   3087 N N   . MET A 1 388 ? 22.176 106.225 25.934  1.00 40.66 ? 388  MET A N   1 
ATOM   3088 C CA  . MET A 1 388 ? 22.856 106.634 24.701  1.00 40.86 ? 388  MET A CA  1 
ATOM   3089 C C   . MET A 1 388 ? 22.897 105.542 23.654  1.00 38.65 ? 388  MET A C   1 
ATOM   3090 O O   . MET A 1 388 ? 23.176 105.814 22.497  1.00 38.06 ? 388  MET A O   1 
ATOM   3091 C CB  . MET A 1 388 ? 24.242 107.151 25.028  1.00 40.19 ? 388  MET A CB  1 
ATOM   3092 C CG  . MET A 1 388 ? 24.155 108.402 25.814  1.00 42.70 ? 388  MET A CG  1 
ATOM   3093 S SD  . MET A 1 388 ? 25.768 109.137 26.023  1.00 47.37 ? 388  MET A SD  1 
ATOM   3094 C CE  . MET A 1 388 ? 25.950 109.830 24.364  1.00 49.12 ? 388  MET A CE  1 
ATOM   3095 N N   . LYS A 1 389 ? 22.551 104.326 24.067  1.00 37.43 ? 389  LYS A N   1 
ATOM   3096 C CA  . LYS A 1 389 ? 22.470 103.118 23.215  1.00 36.68 ? 389  LYS A CA  1 
ATOM   3097 C C   . LYS A 1 389 ? 23.814 102.794 22.512  1.00 35.15 ? 389  LYS A C   1 
ATOM   3098 O O   . LYS A 1 389 ? 23.865 102.517 21.311  1.00 34.31 ? 389  LYS A O   1 
ATOM   3099 C CB  . LYS A 1 389 ? 21.294 103.208 22.239  1.00 37.84 ? 389  LYS A CB  1 
ATOM   3100 C CG  . LYS A 1 389 ? 19.927 103.331 22.962  1.00 37.39 ? 389  LYS A CG  1 
ATOM   3101 C CD  . LYS A 1 389 ? 18.743 103.513 22.006  1.00 40.15 ? 389  LYS A CD  1 
ATOM   3102 C CE  . LYS A 1 389 ? 17.395 103.615 22.787  1.00 41.46 ? 389  LYS A CE  1 
ATOM   3103 N NZ  . LYS A 1 389 ? 17.051 102.390 23.594  1.00 45.38 ? 389  LYS A NZ  1 
ATOM   3104 N N   . ILE A 1 390 ? 24.878 102.807 23.306  1.00 32.94 ? 390  ILE A N   1 
ATOM   3105 C CA  . ILE A 1 390 ? 26.262 102.718 22.796  1.00 32.25 ? 390  ILE A CA  1 
ATOM   3106 C C   . ILE A 1 390 ? 26.959 101.376 23.041  1.00 31.06 ? 390  ILE A C   1 
ATOM   3107 O O   . ILE A 1 390 ? 28.176 101.283 22.873  1.00 29.87 ? 390  ILE A O   1 
ATOM   3108 C CB  . ILE A 1 390 ? 27.157 103.908 23.286  1.00 31.34 ? 390  ILE A CB  1 
ATOM   3109 C CG1 . ILE A 1 390 ? 27.074 104.117 24.791  1.00 32.75 ? 390  ILE A CG1 1 
ATOM   3110 C CG2 . ILE A 1 390 ? 26.798 105.191 22.529  1.00 31.38 ? 390  ILE A CG2 1 
ATOM   3111 C CD1 . ILE A 1 390 ? 27.779 103.053 25.623  1.00 33.61 ? 390  ILE A CD1 1 
ATOM   3112 N N   . TRP A 1 391 ? 26.180 100.348 23.382  1.00 29.89 ? 391  TRP A N   1 
ATOM   3113 C CA  . TRP A 1 391 ? 26.707 99.004  23.638  1.00 29.38 ? 391  TRP A CA  1 
ATOM   3114 C C   . TRP A 1 391 ? 26.930 98.226  22.342  1.00 28.77 ? 391  TRP A C   1 
ATOM   3115 O O   . TRP A 1 391 ? 26.324 98.524  21.330  1.00 31.09 ? 391  TRP A O   1 
ATOM   3116 C CB  . TRP A 1 391 ? 25.758 98.228  24.574  1.00 29.06 ? 391  TRP A CB  1 
ATOM   3117 C CG  . TRP A 1 391 ? 25.377 98.975  25.847  1.00 29.44 ? 391  TRP A CG  1 
ATOM   3118 C CD1 . TRP A 1 391 ? 24.079 99.247  26.308  1.00 29.12 ? 391  TRP A CD1 1 
ATOM   3119 C CD2 . TRP A 1 391 ? 26.270 99.547  26.828  1.00 31.24 ? 391  TRP A CD2 1 
ATOM   3120 N NE1 . TRP A 1 391 ? 24.144 99.939  27.501  1.00 29.69 ? 391  TRP A NE1 1 
ATOM   3121 C CE2 . TRP A 1 391 ? 25.463 100.132 27.847  1.00 29.96 ? 391  TRP A CE2 1 
ATOM   3122 C CE3 . TRP A 1 391 ? 27.671 99.606  26.956  1.00 27.70 ? 391  TRP A CE3 1 
ATOM   3123 C CZ2 . TRP A 1 391 ? 26.015 100.795 28.960  1.00 30.17 ? 391  TRP A CZ2 1 
ATOM   3124 C CZ3 . TRP A 1 391 ? 28.211 100.253 28.070  1.00 30.77 ? 391  TRP A CZ3 1 
ATOM   3125 C CH2 . TRP A 1 391 ? 27.387 100.842 29.053  1.00 29.40 ? 391  TRP A CH2 1 
ATOM   3126 N N   . VAL A 1 392 ? 27.809 97.237  22.365  1.00 27.28 ? 392  VAL A N   1 
ATOM   3127 C CA  . VAL A 1 392 ? 27.857 96.248  21.320  1.00 26.75 ? 392  VAL A CA  1 
ATOM   3128 C C   . VAL A 1 392 ? 26.543 95.427  21.426  1.00 27.56 ? 392  VAL A C   1 
ATOM   3129 O O   . VAL A 1 392 ? 26.078 95.106  22.546  1.00 26.79 ? 392  VAL A O   1 
ATOM   3130 C CB  . VAL A 1 392 ? 29.081 95.292  21.523  1.00 25.61 ? 392  VAL A CB  1 
ATOM   3131 C CG1 . VAL A 1 392 ? 29.081 94.166  20.551  1.00 25.06 ? 392  VAL A CG1 1 
ATOM   3132 C CG2 . VAL A 1 392 ? 30.404 96.071  21.532  1.00 24.95 ? 392  VAL A CG2 1 
ATOM   3133 N N   . ASN A 1 393 ? 25.943 95.135  20.274  1.00 29.22 ? 393  ASN A N   1 
ATOM   3134 C CA  . ASN A 1 393 ? 24.699 94.354  20.180  1.00 29.72 ? 393  ASN A CA  1 
ATOM   3135 C C   . ASN A 1 393 ? 24.915 92.927  19.710  1.00 31.88 ? 393  ASN A C   1 
ATOM   3136 O O   . ASN A 1 393 ? 25.839 92.650  18.938  1.00 29.64 ? 393  ASN A O   1 
ATOM   3137 C CB  . ASN A 1 393 ? 23.726 95.033  19.216  1.00 30.72 ? 393  ASN A CB  1 
ATOM   3138 C CG  . ASN A 1 393 ? 23.247 96.397  19.715  1.00 27.29 ? 393  ASN A CG  1 
ATOM   3139 O OD1 . ASN A 1 393 ? 23.334 96.717  20.905  1.00 29.44 ? 393  ASN A OD1 1 
ATOM   3140 N ND2 . ASN A 1 393 ? 22.780 97.206  18.779  1.00 30.04 ? 393  ASN A ND2 1 
ATOM   3141 N N   . SER A 1 394 ? 24.046 92.018  20.187  1.00 33.97 ? 394  SER A N   1 
ATOM   3142 C CA  . SER A 1 394 ? 23.916 90.667  19.655  1.00 36.66 ? 394  SER A CA  1 
ATOM   3143 C C   . SER A 1 394 ? 23.640 90.703  18.172  1.00 37.88 ? 394  SER A C   1 
ATOM   3144 O O   . SER A 1 394 ? 23.377 91.762  17.613  1.00 37.77 ? 394  SER A O   1 
ATOM   3145 C CB  . SER A 1 394 ? 22.695 89.973  20.284  1.00 37.06 ? 394  SER A CB  1 
ATOM   3146 O OG  . SER A 1 394 ? 22.982 89.556  21.600  1.00 42.38 ? 394  SER A OG  1 
ATOM   3147 N N   . SER A 1 395 ? 23.624 89.524  17.541  1.00 40.03 ? 395  SER A N   1 
ATOM   3148 C CA  . SER A 1 395 ? 23.428 89.433  16.092  1.00 42.27 ? 395  SER A CA  1 
ATOM   3149 C C   . SER A 1 395 ? 22.094 90.017  15.612  1.00 43.43 ? 395  SER A C   1 
ATOM   3150 O O   . SER A 1 395 ? 21.999 90.428  14.450  1.00 43.43 ? 395  SER A O   1 
ATOM   3151 C CB  . SER A 1 395 ? 23.642 88.013  15.577  1.00 42.28 ? 395  SER A CB  1 
ATOM   3152 O OG  . SER A 1 395 ? 22.569 87.157  15.936  1.00 44.89 ? 395  SER A OG  1 
ATOM   3153 N N   . ASP A 1 396 ? 21.091 90.097  16.504  1.00 44.72 ? 396  ASP A N   1 
ATOM   3154 C CA  . ASP A 1 396 ? 19.799 90.739  16.152  1.00 45.68 ? 396  ASP A CA  1 
ATOM   3155 C C   . ASP A 1 396 ? 19.938 92.223  15.835  1.00 45.17 ? 396  ASP A C   1 
ATOM   3156 O O   . ASP A 1 396 ? 19.001 92.850  15.354  1.00 45.73 ? 396  ASP A O   1 
ATOM   3157 C CB  . ASP A 1 396 ? 18.707 90.505  17.226  1.00 46.10 ? 396  ASP A CB  1 
ATOM   3158 C CG  . ASP A 1 396 ? 18.966 91.253  18.569  1.00 48.44 ? 396  ASP A CG  1 
ATOM   3159 O OD1 . ASP A 1 396 ? 19.941 92.056  18.702  1.00 47.79 ? 396  ASP A OD1 1 
ATOM   3160 O OD2 . ASP A 1 396 ? 18.161 91.022  19.520  1.00 50.16 ? 396  ASP A OD2 1 
ATOM   3161 N N   . GLY A 1 397 ? 21.102 92.790  16.136  1.00 43.84 ? 397  GLY A N   1 
ATOM   3162 C CA  . GLY A 1 397 ? 21.351 94.178  15.855  1.00 42.54 ? 397  GLY A CA  1 
ATOM   3163 C C   . GLY A 1 397 ? 20.789 95.165  16.851  1.00 42.07 ? 397  GLY A C   1 
ATOM   3164 O O   . GLY A 1 397 ? 21.164 96.305  16.776  1.00 42.80 ? 397  GLY A O   1 
ATOM   3165 N N   . VAL A 1 398 ? 19.918 94.756  17.782  1.00 41.38 ? 398  VAL A N   1 
ATOM   3166 C CA  . VAL A 1 398 ? 19.242 95.706  18.698  1.00 40.75 ? 398  VAL A CA  1 
ATOM   3167 C C   . VAL A 1 398 ? 19.335 95.422  20.221  1.00 39.74 ? 398  VAL A C   1 
ATOM   3168 O O   . VAL A 1 398 ? 19.043 96.292  21.039  1.00 39.84 ? 398  VAL A O   1 
ATOM   3169 C CB  . VAL A 1 398 ? 17.711 95.977  18.299  1.00 40.94 ? 398  VAL A CB  1 
ATOM   3170 C CG1 . VAL A 1 398 ? 17.595 96.660  16.947  1.00 42.06 ? 398  VAL A CG1 1 
ATOM   3171 C CG2 . VAL A 1 398 ? 16.889 94.686  18.300  1.00 41.74 ? 398  VAL A CG2 1 
ATOM   3172 N N   . THR A 1 399 ? 19.718 94.215  20.605  1.00 38.52 ? 399  THR A N   1 
ATOM   3173 C CA  . THR A 1 399 ? 19.818 93.886  22.021  1.00 37.82 ? 399  THR A CA  1 
ATOM   3174 C C   . THR A 1 399 ? 21.285 93.897  22.398  1.00 35.63 ? 399  THR A C   1 
ATOM   3175 O O   . THR A 1 399 ? 22.039 93.150  21.806  1.00 34.89 ? 399  THR A O   1 
ATOM   3176 C CB  . THR A 1 399 ? 19.355 92.465  22.300  1.00 37.94 ? 399  THR A CB  1 
ATOM   3177 O OG1 . THR A 1 399 ? 18.081 92.249  21.672  1.00 43.23 ? 399  THR A OG1 1 
ATOM   3178 C CG2 . THR A 1 399 ? 19.278 92.211  23.818  1.00 37.50 ? 399  THR A CG2 1 
ATOM   3179 N N   . PRO A 1 400 ? 21.681 94.718  23.381  1.00 35.56 ? 400  PRO A N   1 
ATOM   3180 C CA  . PRO A 1 400 ? 23.091 94.698  23.821  1.00 34.65 ? 400  PRO A CA  1 
ATOM   3181 C C   . PRO A 1 400 ? 23.552 93.309  24.200  1.00 34.71 ? 400  PRO A C   1 
ATOM   3182 O O   . PRO A 1 400 ? 22.829 92.570  24.903  1.00 34.25 ? 400  PRO A O   1 
ATOM   3183 C CB  . PRO A 1 400 ? 23.089 95.582  25.053  1.00 34.77 ? 400  PRO A CB  1 
ATOM   3184 C CG  . PRO A 1 400 ? 21.955 96.500  24.840  1.00 35.38 ? 400  PRO A CG  1 
ATOM   3185 C CD  . PRO A 1 400 ? 20.901 95.742  24.110  1.00 34.92 ? 400  PRO A CD  1 
ATOM   3186 N N   . LEU A 1 401 ? 24.743 92.944  23.728  1.00 33.09 ? 401  LEU A N   1 
ATOM   3187 C CA  . LEU A 1 401 ? 25.306 91.641  24.037  1.00 31.41 ? 401  LEU A CA  1 
ATOM   3188 C C   . LEU A 1 401 ? 25.736 91.537  25.499  1.00 30.68 ? 401  LEU A C   1 
ATOM   3189 O O   . LEU A 1 401 ? 26.306 92.478  26.056  1.00 29.93 ? 401  LEU A O   1 
ATOM   3190 C CB  . LEU A 1 401 ? 26.431 91.339  23.071  1.00 31.10 ? 401  LEU A CB  1 
ATOM   3191 C CG  . LEU A 1 401 ? 27.032 89.974  23.224  1.00 30.95 ? 401  LEU A CG  1 
ATOM   3192 C CD1 . LEU A 1 401 ? 27.469 89.522  21.865  1.00 32.70 ? 401  LEU A CD1 1 
ATOM   3193 C CD2 . LEU A 1 401 ? 28.226 90.135  24.161  1.00 33.72 ? 401  LEU A CD2 1 
ATOM   3194 N N   . ILE A 1 402 ? 25.423 90.407  26.144  1.00 30.19 ? 402  ILE A N   1 
ATOM   3195 C CA  . ILE A 1 402 ? 25.767 90.248  27.576  1.00 30.12 ? 402  ILE A CA  1 
ATOM   3196 C C   . ILE A 1 402 ? 26.899 89.250  27.744  1.00 28.44 ? 402  ILE A C   1 
ATOM   3197 O O   . ILE A 1 402 ? 26.798 88.152  27.291  1.00 28.92 ? 402  ILE A O   1 
ATOM   3198 C CB  . ILE A 1 402 ? 24.546 89.760  28.471  1.00 30.65 ? 402  ILE A CB  1 
ATOM   3199 C CG1 . ILE A 1 402 ? 23.336 90.684  28.354  1.00 34.36 ? 402  ILE A CG1 1 
ATOM   3200 C CG2 . ILE A 1 402 ? 24.916 89.656  29.945  1.00 29.85 ? 402  ILE A CG2 1 
ATOM   3201 C CD1 . ILE A 1 402 ? 23.554 92.007  28.909  1.00 37.84 ? 402  ILE A CD1 1 
ATOM   3202 N N   . GLY A 1 403 ? 27.965 89.645  28.430  1.00 28.00 ? 403  GLY A N   1 
ATOM   3203 C CA  . GLY A 1 403 ? 29.017 88.724  28.771  1.00 27.34 ? 403  GLY A CA  1 
ATOM   3204 C C   . GLY A 1 403 ? 29.349 88.862  30.241  1.00 27.95 ? 403  GLY A C   1 
ATOM   3205 O O   . GLY A 1 403 ? 28.546 89.346  31.046  1.00 27.37 ? 403  GLY A O   1 
ATOM   3206 N N   . GLU A 1 404 ? 30.554 88.467  30.615  1.00 29.12 ? 404  GLU A N   1 
ATOM   3207 C CA  . GLU A 1 404 ? 30.922 88.497  32.010  1.00 30.70 ? 404  GLU A CA  1 
ATOM   3208 C C   . GLU A 1 404 ? 32.390 88.869  32.174  1.00 30.11 ? 404  GLU A C   1 
ATOM   3209 O O   . GLU A 1 404 ? 33.249 88.249  31.565  1.00 29.80 ? 404  GLU A O   1 
ATOM   3210 C CB  . GLU A 1 404 ? 30.680 87.087  32.543  1.00 31.88 ? 404  GLU A CB  1 
ATOM   3211 C CG  . GLU A 1 404 ? 30.866 86.877  34.014  1.00 39.47 ? 404  GLU A CG  1 
ATOM   3212 C CD  . GLU A 1 404 ? 30.707 85.387  34.342  1.00 49.53 ? 404  GLU A CD  1 
ATOM   3213 O OE1 . GLU A 1 404 ? 29.547 84.872  34.192  1.00 52.17 ? 404  GLU A OE1 1 
ATOM   3214 O OE2 . GLU A 1 404 ? 31.737 84.746  34.708  1.00 50.92 ? 404  GLU A OE2 1 
ATOM   3215 N N   . VAL A 1 405 ? 32.685 89.844  33.015  1.00 29.12 ? 405  VAL A N   1 
ATOM   3216 C CA  . VAL A 1 405 ? 34.069 90.185  33.288  1.00 28.70 ? 405  VAL A CA  1 
ATOM   3217 C C   . VAL A 1 405 ? 34.218 90.431  34.775  1.00 28.95 ? 405  VAL A C   1 
ATOM   3218 O O   . VAL A 1 405 ? 33.623 89.718  35.551  1.00 28.89 ? 405  VAL A O   1 
ATOM   3219 C CB  . VAL A 1 405 ? 34.596 91.340  32.364  1.00 28.97 ? 405  VAL A CB  1 
ATOM   3220 C CG1 . VAL A 1 405 ? 36.081 91.236  32.244  1.00 26.01 ? 405  VAL A CG1 1 
ATOM   3221 C CG2 . VAL A 1 405 ? 34.017 91.217  30.962  1.00 26.11 ? 405  VAL A CG2 1 
ATOM   3222 N N   . TRP A 1 406 ? 35.012 91.395  35.205  1.00 29.17 ? 406  TRP A N   1 
ATOM   3223 C CA  . TRP A 1 406 ? 35.371 91.463  36.628  1.00 30.42 ? 406  TRP A CA  1 
ATOM   3224 C C   . TRP A 1 406 ? 34.175 91.714  37.532  1.00 31.10 ? 406  TRP A C   1 
ATOM   3225 O O   . TRP A 1 406 ? 34.094 91.108  38.590  1.00 31.86 ? 406  TRP A O   1 
ATOM   3226 C CB  . TRP A 1 406 ? 36.446 92.526  36.921  1.00 30.14 ? 406  TRP A CB  1 
ATOM   3227 C CG  . TRP A 1 406 ? 37.755 92.225  36.304  1.00 28.54 ? 406  TRP A CG  1 
ATOM   3228 C CD1 . TRP A 1 406 ? 38.394 92.966  35.359  1.00 27.99 ? 406  TRP A CD1 1 
ATOM   3229 C CD2 . TRP A 1 406 ? 38.603 91.111  36.591  1.00 28.86 ? 406  TRP A CD2 1 
ATOM   3230 N NE1 . TRP A 1 406 ? 39.578 92.369  35.025  1.00 31.33 ? 406  TRP A NE1 1 
ATOM   3231 C CE2 . TRP A 1 406 ? 39.740 91.235  35.769  1.00 27.90 ? 406  TRP A CE2 1 
ATOM   3232 C CE3 . TRP A 1 406 ? 38.510 90.012  37.466  1.00 28.99 ? 406  TRP A CE3 1 
ATOM   3233 C CZ2 . TRP A 1 406 ? 40.781 90.321  35.791  1.00 31.61 ? 406  TRP A CZ2 1 
ATOM   3234 C CZ3 . TRP A 1 406 ? 39.527 89.110  37.489  1.00 30.80 ? 406  TRP A CZ3 1 
ATOM   3235 C CH2 . TRP A 1 406 ? 40.680 89.283  36.669  1.00 29.05 ? 406  TRP A CH2 1 
ATOM   3236 N N   . PRO A 1 407 ? 33.253 92.610  37.133  1.00 31.83 ? 407  PRO A N   1 
ATOM   3237 C CA  . PRO A 1 407 ? 32.186 92.826  38.091  1.00 32.36 ? 407  PRO A CA  1 
ATOM   3238 C C   . PRO A 1 407 ? 31.015 91.827  38.013  1.00 32.82 ? 407  PRO A C   1 
ATOM   3239 O O   . PRO A 1 407 ? 30.082 91.979  38.788  1.00 34.10 ? 407  PRO A O   1 
ATOM   3240 C CB  . PRO A 1 407 ? 31.691 94.234  37.746  1.00 32.07 ? 407  PRO A CB  1 
ATOM   3241 C CG  . PRO A 1 407 ? 31.938 94.400  36.301  1.00 30.00 ? 407  PRO A CG  1 
ATOM   3242 C CD  . PRO A 1 407 ? 33.048 93.423  35.909  1.00 32.56 ? 407  PRO A CD  1 
ATOM   3243 N N   . GLY A 1 408 ? 31.068 90.824  37.133  1.00 32.24 ? 408  GLY A N   1 
ATOM   3244 C CA  . GLY A 1 408 ? 29.913 89.927  36.881  1.00 32.99 ? 408  GLY A CA  1 
ATOM   3245 C C   . GLY A 1 408 ? 29.351 90.162  35.493  1.00 33.32 ? 408  GLY A C   1 
ATOM   3246 O O   . GLY A 1 408 ? 30.125 90.529  34.604  1.00 33.88 ? 408  GLY A O   1 
ATOM   3247 N N   . GLN A 1 409 ? 28.029 90.004  35.289  1.00 33.40 ? 409  GLN A N   1 
ATOM   3248 C CA  . GLN A 1 409 ? 27.398 90.276  33.984  1.00 33.01 ? 409  GLN A CA  1 
ATOM   3249 C C   . GLN A 1 409 ? 27.648 91.711  33.540  1.00 31.58 ? 409  GLN A C   1 
ATOM   3250 O O   . GLN A 1 409 ? 27.576 92.656  34.317  1.00 30.19 ? 409  GLN A O   1 
ATOM   3251 C CB  . GLN A 1 409 ? 25.876 90.065  33.973  1.00 34.02 ? 409  GLN A CB  1 
ATOM   3252 C CG  . GLN A 1 409 ? 25.424 88.645  33.859  1.00 38.01 ? 409  GLN A CG  1 
ATOM   3253 C CD  . GLN A 1 409 ? 23.996 88.512  33.316  1.00 42.60 ? 409  GLN A CD  1 
ATOM   3254 O OE1 . GLN A 1 409 ? 23.239 89.509  33.113  1.00 44.95 ? 409  GLN A OE1 1 
ATOM   3255 N NE2 . GLN A 1 409 ? 23.631 87.279  33.041  1.00 42.84 ? 409  GLN A NE2 1 
ATOM   3256 N N   . THR A 1 410 ? 27.913 91.868  32.255  1.00 31.40 ? 410  THR A N   1 
ATOM   3257 C CA  . THR A 1 410 ? 28.344 93.154  31.769  1.00 31.78 ? 410  THR A CA  1 
ATOM   3258 C C   . THR A 1 410 ? 27.856 93.325  30.368  1.00 30.22 ? 410  THR A C   1 
ATOM   3259 O O   . THR A 1 410 ? 27.574 92.367  29.678  1.00 31.31 ? 410  THR A O   1 
ATOM   3260 C CB  . THR A 1 410 ? 29.928 93.307  31.745  1.00 31.21 ? 410  THR A CB  1 
ATOM   3261 O OG1 . THR A 1 410 ? 30.499 92.335  30.859  1.00 34.49 ? 410  THR A OG1 1 
ATOM   3262 C CG2 . THR A 1 410 ? 30.561 93.181  33.123  1.00 29.45 ? 410  THR A CG2 1 
ATOM   3263 N N   . VAL A 1 411 ? 27.803 94.569  29.949  1.00 28.76 ? 411  VAL A N   1 
ATOM   3264 C CA  . VAL A 1 411 ? 27.670 94.888  28.534  1.00 28.08 ? 411  VAL A CA  1 
ATOM   3265 C C   . VAL A 1 411 ? 28.990 95.571  28.092  1.00 27.26 ? 411  VAL A C   1 
ATOM   3266 O O   . VAL A 1 411 ? 29.799 95.976  28.920  1.00 25.74 ? 411  VAL A O   1 
ATOM   3267 C CB  . VAL A 1 411 ? 26.471 95.843  28.276  1.00 27.91 ? 411  VAL A CB  1 
ATOM   3268 C CG1 . VAL A 1 411 ? 25.119 95.056  28.374  1.00 30.99 ? 411  VAL A CG1 1 
ATOM   3269 C CG2 . VAL A 1 411 ? 26.500 97.010  29.239  1.00 26.08 ? 411  VAL A CG2 1 
ATOM   3270 N N   . PHE A 1 412 ? 29.174 95.696  26.783  1.00 26.83 ? 412  PHE A N   1 
ATOM   3271 C CA  . PHE A 1 412 ? 30.408 96.203  26.239  1.00 26.73 ? 412  PHE A CA  1 
ATOM   3272 C C   . PHE A 1 412 ? 30.181 97.428  25.382  1.00 25.43 ? 412  PHE A C   1 
ATOM   3273 O O   . PHE A 1 412 ? 29.420 97.366  24.441  1.00 25.69 ? 412  PHE A O   1 
ATOM   3274 C CB  . PHE A 1 412 ? 31.066 95.119  25.390  1.00 25.86 ? 412  PHE A CB  1 
ATOM   3275 C CG  . PHE A 1 412 ? 31.346 93.862  26.153  1.00 26.32 ? 412  PHE A CG  1 
ATOM   3276 C CD1 . PHE A 1 412 ? 32.570 93.677  26.769  1.00 23.92 ? 412  PHE A CD1 1 
ATOM   3277 C CD2 . PHE A 1 412 ? 30.379 92.865  26.267  1.00 23.84 ? 412  PHE A CD2 1 
ATOM   3278 C CE1 . PHE A 1 412 ? 32.857 92.517  27.485  1.00 25.90 ? 412  PHE A CE1 1 
ATOM   3279 C CE2 . PHE A 1 412 ? 30.645 91.706  27.009  1.00 25.91 ? 412  PHE A CE2 1 
ATOM   3280 C CZ  . PHE A 1 412 ? 31.883 91.523  27.617  1.00 26.65 ? 412  PHE A CZ  1 
ATOM   3281 N N   . PRO A 1 413 ? 30.928 98.506  25.646  1.00 26.09 ? 413  PRO A N   1 
ATOM   3282 C CA  . PRO A 1 413 ? 30.816 99.715  24.837  1.00 26.32 ? 413  PRO A CA  1 
ATOM   3283 C C   . PRO A 1 413 ? 31.304 99.481  23.381  1.00 26.95 ? 413  PRO A C   1 
ATOM   3284 O O   . PRO A 1 413 ? 32.220 98.661  23.123  1.00 26.88 ? 413  PRO A O   1 
ATOM   3285 C CB  . PRO A 1 413 ? 31.666 100.725 25.592  1.00 26.47 ? 413  PRO A CB  1 
ATOM   3286 C CG  . PRO A 1 413 ? 31.915 100.074 26.994  1.00 25.96 ? 413  PRO A CG  1 
ATOM   3287 C CD  . PRO A 1 413 ? 31.968 98.631  26.673  1.00 25.58 ? 413  PRO A CD  1 
ATOM   3288 N N   . ASP A 1 414 ? 30.625 100.116 22.442  1.00 27.01 ? 414  ASP A N   1 
ATOM   3289 C CA  . ASP A 1 414 ? 31.004 100.028 21.057  1.00 28.13 ? 414  ASP A CA  1 
ATOM   3290 C C   . ASP A 1 414 ? 31.794 101.291 20.770  1.00 28.69 ? 414  ASP A C   1 
ATOM   3291 O O   . ASP A 1 414 ? 31.228 102.338 20.468  1.00 28.78 ? 414  ASP A O   1 
ATOM   3292 C CB  . ASP A 1 414 ? 29.795 99.889  20.143  1.00 28.99 ? 414  ASP A CB  1 
ATOM   3293 C CG  . ASP A 1 414 ? 30.162 100.072 18.658  1.00 31.95 ? 414  ASP A CG  1 
ATOM   3294 O OD1 . ASP A 1 414 ? 31.374 99.952  18.301  1.00 31.79 ? 414  ASP A OD1 1 
ATOM   3295 O OD2 . ASP A 1 414 ? 29.236 100.333 17.857  1.00 31.49 ? 414  ASP A OD2 1 
ATOM   3296 N N   . TYR A 1 415 ? 33.113 101.200 20.934  1.00 27.49 ? 415  TYR A N   1 
ATOM   3297 C CA  . TYR A 1 415 ? 33.945 102.384 20.776  1.00 28.25 ? 415  TYR A CA  1 
ATOM   3298 C C   . TYR A 1 415 ? 34.086 102.825 19.309  1.00 28.89 ? 415  TYR A C   1 
ATOM   3299 O O   . TYR A 1 415 ? 34.568 103.916 19.077  1.00 31.51 ? 415  TYR A O   1 
ATOM   3300 C CB  . TYR A 1 415 ? 35.318 102.199 21.443  1.00 26.66 ? 415  TYR A CB  1 
ATOM   3301 C CG  . TYR A 1 415 ? 35.302 101.988 22.927  1.00 24.22 ? 415  TYR A CG  1 
ATOM   3302 C CD1 . TYR A 1 415 ? 35.151 103.054 23.802  1.00 22.81 ? 415  TYR A CD1 1 
ATOM   3303 C CD2 . TYR A 1 415 ? 35.481 100.714 23.460  1.00 23.53 ? 415  TYR A CD2 1 
ATOM   3304 C CE1 . TYR A 1 415 ? 35.179 102.858 25.177  1.00 24.14 ? 415  TYR A CE1 1 
ATOM   3305 C CE2 . TYR A 1 415 ? 35.491 100.511 24.821  1.00 24.82 ? 415  TYR A CE2 1 
ATOM   3306 C CZ  . TYR A 1 415 ? 35.330 101.572 25.662  1.00 23.87 ? 415  TYR A CZ  1 
ATOM   3307 O OH  . TYR A 1 415 ? 35.364 101.342 27.004  1.00 27.00 ? 415  TYR A OH  1 
ATOM   3308 N N   . THR A 1 416 ? 33.623 102.028 18.344  1.00 29.42 ? 416  THR A N   1 
ATOM   3309 C CA  . THR A 1 416 ? 33.601 102.430 16.934  1.00 30.29 ? 416  THR A CA  1 
ATOM   3310 C C   . THR A 1 416 ? 32.466 103.451 16.643  1.00 32.38 ? 416  THR A C   1 
ATOM   3311 O O   . THR A 1 416 ? 32.428 104.088 15.596  1.00 31.44 ? 416  THR A O   1 
ATOM   3312 C CB  . THR A 1 416 ? 33.481 101.197 15.990  1.00 29.62 ? 416  THR A CB  1 
ATOM   3313 O OG1 . THR A 1 416 ? 32.135 100.647 15.997  1.00 31.21 ? 416  THR A OG1 1 
ATOM   3314 C CG2 . THR A 1 416 ? 34.467 100.103 16.392  1.00 30.41 ? 416  THR A CG2 1 
ATOM   3315 N N   . ASN A 1 417 ? 31.538 103.589 17.591  1.00 34.19 ? 417  ASN A N   1 
ATOM   3316 C CA  . ASN A 1 417 ? 30.430 104.519 17.483  1.00 35.87 ? 417  ASN A CA  1 
ATOM   3317 C C   . ASN A 1 417 ? 30.890 105.868 18.044  1.00 37.23 ? 417  ASN A C   1 
ATOM   3318 O O   . ASN A 1 417 ? 31.237 105.950 19.200  1.00 37.08 ? 417  ASN A O   1 
ATOM   3319 C CB  . ASN A 1 417 ? 29.245 103.972 18.289  1.00 36.01 ? 417  ASN A CB  1 
ATOM   3320 C CG  . ASN A 1 417 ? 28.021 104.895 18.248  1.00 37.68 ? 417  ASN A CG  1 
ATOM   3321 O OD1 . ASN A 1 417 ? 28.142 106.089 17.972  1.00 39.46 ? 417  ASN A OD1 1 
ATOM   3322 N ND2 . ASN A 1 417 ? 26.847 104.343 18.535  1.00 38.38 ? 417  ASN A ND2 1 
ATOM   3323 N N   . PRO A 1 418 ? 30.862 106.950 17.229  1.00 39.46 ? 418  PRO A N   1 
ATOM   3324 C CA  . PRO A 1 418 ? 31.322 108.273 17.692  1.00 39.75 ? 418  PRO A CA  1 
ATOM   3325 C C   . PRO A 1 418 ? 30.680 108.757 19.005  1.00 39.50 ? 418  PRO A C   1 
ATOM   3326 O O   . PRO A 1 418 ? 31.361 109.385 19.836  1.00 38.23 ? 418  PRO A O   1 
ATOM   3327 C CB  . PRO A 1 418 ? 30.939 109.197 16.522  1.00 40.73 ? 418  PRO A CB  1 
ATOM   3328 C CG  . PRO A 1 418 ? 29.865 108.402 15.755  1.00 40.41 ? 418  PRO A CG  1 
ATOM   3329 C CD  . PRO A 1 418 ? 30.374 107.013 15.838  1.00 39.64 ? 418  PRO A CD  1 
ATOM   3330 N N   . ASN A 1 419 ? 29.400 108.444 19.201  1.00 38.61 ? 419  ASN A N   1 
ATOM   3331 C CA  . ASN A 1 419 ? 28.718 108.757 20.459  1.00 38.71 ? 419  ASN A CA  1 
ATOM   3332 C C   . ASN A 1 419 ? 29.206 107.973 21.658  1.00 37.56 ? 419  ASN A C   1 
ATOM   3333 O O   . ASN A 1 419 ? 28.965 108.367 22.785  1.00 37.39 ? 419  ASN A O   1 
ATOM   3334 C CB  . ASN A 1 419 ? 27.192 108.585 20.330  1.00 39.71 ? 419  ASN A CB  1 
ATOM   3335 C CG  . ASN A 1 419 ? 26.610 109.429 19.219  1.00 44.51 ? 419  ASN A CG  1 
ATOM   3336 O OD1 . ASN A 1 419 ? 27.001 110.591 19.035  1.00 49.01 ? 419  ASN A OD1 1 
ATOM   3337 N ND2 . ASN A 1 419 ? 25.676 108.846 18.449  1.00 47.80 ? 419  ASN A ND2 1 
ATOM   3338 N N   . CYS A 1 420 ? 29.885 106.847 21.433  1.00 36.35 ? 420  CYS A N   1 
ATOM   3339 C CA  . CYS A 1 420 ? 30.452 106.091 22.557  1.00 35.79 ? 420  CYS A CA  1 
ATOM   3340 C C   . CYS A 1 420 ? 31.593 106.873 23.212  1.00 35.36 ? 420  CYS A C   1 
ATOM   3341 O O   . CYS A 1 420 ? 31.680 106.964 24.438  1.00 35.91 ? 420  CYS A O   1 
ATOM   3342 C CB  . CYS A 1 420 ? 30.901 104.717 22.095  1.00 35.40 ? 420  CYS A CB  1 
ATOM   3343 S SG  . CYS A 1 420 ? 31.389 103.685 23.443  1.00 35.68 ? 420  CYS A SG  1 
ATOM   3344 N N   . ALA A 1 421 ? 32.418 107.526 22.401  1.00 35.44 ? 421  ALA A N   1 
ATOM   3345 C CA  . ALA A 1 421 ? 33.465 108.409 22.925  1.00 34.85 ? 421  ALA A CA  1 
ATOM   3346 C C   . ALA A 1 421 ? 32.907 109.594 23.733  1.00 34.26 ? 421  ALA A C   1 
ATOM   3347 O O   . ALA A 1 421 ? 33.546 110.054 24.687  1.00 35.22 ? 421  ALA A O   1 
ATOM   3348 C CB  . ALA A 1 421 ? 34.350 108.899 21.801  1.00 35.31 ? 421  ALA A CB  1 
ATOM   3349 N N   . VAL A 1 422 ? 31.742 110.091 23.359  1.00 33.23 ? 422  VAL A N   1 
ATOM   3350 C CA  . VAL A 1 422 ? 31.063 111.146 24.157  1.00 33.08 ? 422  VAL A CA  1 
ATOM   3351 C C   . VAL A 1 422 ? 30.509 110.566 25.488  1.00 31.30 ? 422  VAL A C   1 
ATOM   3352 O O   . VAL A 1 422 ? 30.688 111.151 26.548  1.00 32.37 ? 422  VAL A O   1 
ATOM   3353 C CB  . VAL A 1 422 ? 29.916 111.776 23.330  1.00 33.93 ? 422  VAL A CB  1 
ATOM   3354 C CG1 . VAL A 1 422 ? 29.040 112.711 24.189  1.00 34.30 ? 422  VAL A CG1 1 
ATOM   3355 C CG2 . VAL A 1 422 ? 30.488 112.505 22.101  1.00 35.10 ? 422  VAL A CG2 1 
ATOM   3356 N N   . TRP A 1 423 ? 29.881 109.399 25.444  1.00 29.56 ? 423  TRP A N   1 
ATOM   3357 C CA  . TRP A 1 423 ? 29.527 108.701 26.696  1.00 27.97 ? 423  TRP A CA  1 
ATOM   3358 C C   . TRP A 1 423 ? 30.795 108.449 27.576  1.00 27.18 ? 423  TRP A C   1 
ATOM   3359 O O   . TRP A 1 423 ? 30.863 108.767 28.754  1.00 25.98 ? 423  TRP A O   1 
ATOM   3360 C CB  . TRP A 1 423 ? 28.806 107.377 26.374  1.00 27.64 ? 423  TRP A CB  1 
ATOM   3361 C CG  . TRP A 1 423 ? 28.767 106.459 27.582  1.00 28.40 ? 423  TRP A CG  1 
ATOM   3362 C CD1 . TRP A 1 423 ? 27.963 106.583 28.686  1.00 28.85 ? 423  TRP A CD1 1 
ATOM   3363 C CD2 . TRP A 1 423 ? 29.633 105.329 27.839  1.00 30.01 ? 423  TRP A CD2 1 
ATOM   3364 N NE1 . TRP A 1 423 ? 28.260 105.595 29.598  1.00 29.35 ? 423  TRP A NE1 1 
ATOM   3365 C CE2 . TRP A 1 423 ? 29.271 104.803 29.106  1.00 29.87 ? 423  TRP A CE2 1 
ATOM   3366 C CE3 . TRP A 1 423 ? 30.659 104.704 27.114  1.00 29.94 ? 423  TRP A CE3 1 
ATOM   3367 C CZ2 . TRP A 1 423 ? 29.902 103.679 29.667  1.00 27.96 ? 423  TRP A CZ2 1 
ATOM   3368 C CZ3 . TRP A 1 423 ? 31.292 103.587 27.681  1.00 29.19 ? 423  TRP A CZ3 1 
ATOM   3369 C CH2 . TRP A 1 423 ? 30.900 103.083 28.938  1.00 28.79 ? 423  TRP A CH2 1 
ATOM   3370 N N   . TRP A 1 424 ? 31.816 107.868 26.971  1.00 26.98 ? 424  TRP A N   1 
ATOM   3371 C CA  . TRP A 1 424 ? 33.068 107.545 27.669  1.00 26.69 ? 424  TRP A CA  1 
ATOM   3372 C C   . TRP A 1 424 ? 33.744 108.763 28.287  1.00 25.86 ? 424  TRP A C   1 
ATOM   3373 O O   . TRP A 1 424 ? 34.188 108.728 29.440  1.00 25.91 ? 424  TRP A O   1 
ATOM   3374 C CB  . TRP A 1 424 ? 33.951 106.895 26.601  1.00 27.36 ? 424  TRP A CB  1 
ATOM   3375 C CG  . TRP A 1 424 ? 35.180 106.216 27.030  1.00 28.91 ? 424  TRP A CG  1 
ATOM   3376 C CD1 . TRP A 1 424 ? 36.425 106.462 26.560  1.00 28.70 ? 424  TRP A CD1 1 
ATOM   3377 C CD2 . TRP A 1 424 ? 35.299 105.097 27.934  1.00 26.73 ? 424  TRP A CD2 1 
ATOM   3378 N NE1 . TRP A 1 424 ? 37.322 105.592 27.118  1.00 25.45 ? 424  TRP A NE1 1 
ATOM   3379 C CE2 . TRP A 1 424 ? 36.660 104.729 27.950  1.00 28.35 ? 424  TRP A CE2 1 
ATOM   3380 C CE3 . TRP A 1 424 ? 34.393 104.356 28.691  1.00 27.01 ? 424  TRP A CE3 1 
ATOM   3381 C CZ2 . TRP A 1 424 ? 37.143 103.659 28.731  1.00 29.22 ? 424  TRP A CZ2 1 
ATOM   3382 C CZ3 . TRP A 1 424 ? 34.858 103.306 29.463  1.00 28.73 ? 424  TRP A CZ3 1 
ATOM   3383 C CH2 . TRP A 1 424 ? 36.217 102.960 29.482  1.00 28.13 ? 424  TRP A CH2 1 
ATOM   3384 N N   . THR A 1 425 ? 33.813 109.860 27.532  1.00 25.57 ? 425  THR A N   1 
ATOM   3385 C CA  . THR A 1 425 ? 34.386 111.101 28.040  1.00 26.93 ? 425  THR A CA  1 
ATOM   3386 C C   . THR A 1 425 ? 33.680 111.629 29.315  1.00 28.09 ? 425  THR A C   1 
ATOM   3387 O O   . THR A 1 425 ? 34.324 112.018 30.325  1.00 26.90 ? 425  THR A O   1 
ATOM   3388 C CB  . THR A 1 425 ? 34.251 112.167 26.985  1.00 27.10 ? 425  THR A CB  1 
ATOM   3389 O OG1 . THR A 1 425 ? 35.019 111.776 25.840  1.00 29.13 ? 425  THR A OG1 1 
ATOM   3390 C CG2 . THR A 1 425 ? 34.709 113.486 27.505  1.00 27.95 ? 425  THR A CG2 1 
ATOM   3391 N N   . LYS A 1 426 ? 32.354 111.661 29.228  1.00 27.93 ? 426  LYS A N   1 
ATOM   3392 C CA  . LYS A 1 426 ? 31.516 112.042 30.387  1.00 29.53 ? 426  LYS A CA  1 
ATOM   3393 C C   . LYS A 1 426 ? 31.732 111.151 31.603  1.00 27.82 ? 426  LYS A C   1 
ATOM   3394 O O   . LYS A 1 426 ? 31.725 111.654 32.730  1.00 28.95 ? 426  LYS A O   1 
ATOM   3395 C CB  . LYS A 1 426 ? 30.042 112.047 30.016  1.00 29.44 ? 426  LYS A CB  1 
ATOM   3396 C CG  . LYS A 1 426 ? 29.124 112.609 31.178  1.00 34.81 ? 426  LYS A CG  1 
ATOM   3397 C CD  . LYS A 1 426 ? 29.655 113.966 31.756  1.00 41.93 ? 426  LYS A CD  1 
ATOM   3398 C CE  . LYS A 1 426 ? 28.519 115.019 31.879  1.00 46.89 ? 426  LYS A CE  1 
ATOM   3399 N NZ  . LYS A 1 426 ? 28.997 116.433 31.617  1.00 47.90 ? 426  LYS A NZ  1 
ATOM   3400 N N   . GLU A 1 427 ? 31.932 109.841 31.393  1.00 27.93 ? 427  GLU A N   1 
ATOM   3401 C CA  . GLU A 1 427 ? 32.235 108.925 32.539  1.00 28.07 ? 427  GLU A CA  1 
ATOM   3402 C C   . GLU A 1 427 ? 33.534 109.325 33.240  1.00 27.46 ? 427  GLU A C   1 
ATOM   3403 O O   . GLU A 1 427 ? 33.636 109.333 34.455  1.00 27.45 ? 427  GLU A O   1 
ATOM   3404 C CB  . GLU A 1 427 ? 32.273 107.443 32.148  1.00 27.12 ? 427  GLU A CB  1 
ATOM   3405 C CG  . GLU A 1 427 ? 30.938 106.758 31.844  1.00 32.49 ? 427  GLU A CG  1 
ATOM   3406 C CD  . GLU A 1 427 ? 29.767 107.092 32.820  1.00 34.38 ? 427  GLU A CD  1 
ATOM   3407 O OE1 . GLU A 1 427 ? 29.970 107.229 34.058  1.00 36.74 ? 427  GLU A OE1 1 
ATOM   3408 O OE2 . GLU A 1 427 ? 28.617 107.205 32.328  1.00 39.69 ? 427  GLU A OE2 1 
ATOM   3409 N N   . PHE A 1 428 ? 34.535 109.675 32.455  1.00 28.16 ? 428  PHE A N   1 
ATOM   3410 C CA  . PHE A 1 428 ? 35.820 110.080 33.007  1.00 28.47 ? 428  PHE A CA  1 
ATOM   3411 C C   . PHE A 1 428 ? 35.769 111.434 33.683  1.00 28.58 ? 428  PHE A C   1 
ATOM   3412 O O   . PHE A 1 428 ? 36.342 111.614 34.736  1.00 27.74 ? 428  PHE A O   1 
ATOM   3413 C CB  . PHE A 1 428 ? 36.856 110.092 31.897  1.00 29.68 ? 428  PHE A CB  1 
ATOM   3414 C CG  . PHE A 1 428 ? 37.457 108.757 31.643  1.00 31.25 ? 428  PHE A CG  1 
ATOM   3415 C CD1 . PHE A 1 428 ? 38.311 108.183 32.588  1.00 34.64 ? 428  PHE A CD1 1 
ATOM   3416 C CD2 . PHE A 1 428 ? 37.173 108.067 30.490  1.00 33.01 ? 428  PHE A CD2 1 
ATOM   3417 C CE1 . PHE A 1 428 ? 38.881 106.930 32.371  1.00 36.83 ? 428  PHE A CE1 1 
ATOM   3418 C CE2 . PHE A 1 428 ? 37.763 106.795 30.251  1.00 35.86 ? 428  PHE A CE2 1 
ATOM   3419 C CZ  . PHE A 1 428 ? 38.612 106.241 31.194  1.00 33.79 ? 428  PHE A CZ  1 
ATOM   3420 N N   . GLU A 1 429 ? 35.109 112.404 33.057  1.00 29.37 ? 429  GLU A N   1 
ATOM   3421 C CA  . GLU A 1 429 ? 34.956 113.714 33.684  1.00 31.19 ? 429  GLU A CA  1 
ATOM   3422 C C   . GLU A 1 429 ? 34.230 113.606 35.039  1.00 30.24 ? 429  GLU A C   1 
ATOM   3423 O O   . GLU A 1 429 ? 34.683 114.175 36.022  1.00 30.30 ? 429  GLU A O   1 
ATOM   3424 C CB  . GLU A 1 429 ? 34.245 114.673 32.715  1.00 32.45 ? 429  GLU A CB  1 
ATOM   3425 C CG  . GLU A 1 429 ? 34.056 116.070 33.263  1.00 40.31 ? 429  GLU A CG  1 
ATOM   3426 C CD  . GLU A 1 429 ? 33.891 117.116 32.157  1.00 48.61 ? 429  GLU A CD  1 
ATOM   3427 O OE1 . GLU A 1 429 ? 33.427 116.729 31.050  1.00 51.51 ? 429  GLU A OE1 1 
ATOM   3428 O OE2 . GLU A 1 429 ? 34.253 118.309 32.408  1.00 51.79 ? 429  GLU A OE2 1 
ATOM   3429 N N   . LEU A 1 430 ? 33.139 112.844 35.097  1.00 30.37 ? 430  LEU A N   1 
ATOM   3430 C CA  . LEU A 1 430 ? 32.493 112.537 36.383  1.00 30.31 ? 430  LEU A CA  1 
ATOM   3431 C C   . LEU A 1 430 ? 33.406 111.882 37.396  1.00 30.37 ? 430  LEU A C   1 
ATOM   3432 O O   . LEU A 1 430 ? 33.436 112.291 38.564  1.00 30.31 ? 430  LEU A O   1 
ATOM   3433 C CB  . LEU A 1 430 ? 31.232 111.681 36.177  1.00 31.16 ? 430  LEU A CB  1 
ATOM   3434 C CG  . LEU A 1 430 ? 30.101 112.459 35.478  1.00 33.04 ? 430  LEU A CG  1 
ATOM   3435 C CD1 . LEU A 1 430 ? 29.017 111.539 34.976  1.00 32.83 ? 430  LEU A CD1 1 
ATOM   3436 C CD2 . LEU A 1 430 ? 29.536 113.551 36.413  1.00 33.03 ? 430  LEU A CD2 1 
ATOM   3437 N N   . PHE A 1 431 ? 34.177 110.866 36.988  1.00 29.84 ? 431  PHE A N   1 
ATOM   3438 C CA  . PHE A 1 431 ? 34.964 110.160 37.971  1.00 28.65 ? 431  PHE A CA  1 
ATOM   3439 C C   . PHE A 1 431 ? 36.142 111.013 38.392  1.00 28.81 ? 431  PHE A C   1 
ATOM   3440 O O   . PHE A 1 431 ? 36.520 111.010 39.530  1.00 27.89 ? 431  PHE A O   1 
ATOM   3441 C CB  . PHE A 1 431 ? 35.380 108.776 37.458  1.00 29.36 ? 431  PHE A CB  1 
ATOM   3442 C CG  . PHE A 1 431 ? 36.103 107.924 38.478  1.00 30.41 ? 431  PHE A CG  1 
ATOM   3443 C CD1 . PHE A 1 431 ? 35.530 107.671 39.745  1.00 29.58 ? 431  PHE A CD1 1 
ATOM   3444 C CD2 . PHE A 1 431 ? 37.343 107.351 38.175  1.00 29.84 ? 431  PHE A CD2 1 
ATOM   3445 C CE1 . PHE A 1 431 ? 36.184 106.890 40.672  1.00 31.07 ? 431  PHE A CE1 1 
ATOM   3446 C CE2 . PHE A 1 431 ? 38.011 106.577 39.117  1.00 30.64 ? 431  PHE A CE2 1 
ATOM   3447 C CZ  . PHE A 1 431 ? 37.438 106.329 40.365  1.00 31.18 ? 431  PHE A CZ  1 
ATOM   3448 N N   . HIS A 1 432 ? 36.699 111.783 37.460  1.00 30.55 ? 432  HIS A N   1 
ATOM   3449 C CA  . HIS A 1 432 ? 37.859 112.644 37.735  1.00 32.16 ? 432  HIS A CA  1 
ATOM   3450 C C   . HIS A 1 432 ? 37.624 113.728 38.778  1.00 33.30 ? 432  HIS A C   1 
ATOM   3451 O O   . HIS A 1 432 ? 38.556 114.135 39.504  1.00 34.46 ? 432  HIS A O   1 
ATOM   3452 C CB  . HIS A 1 432 ? 38.364 113.285 36.440  1.00 32.53 ? 432  HIS A CB  1 
ATOM   3453 C CG  . HIS A 1 432 ? 39.706 113.920 36.573  1.00 33.41 ? 432  HIS A CG  1 
ATOM   3454 N ND1 . HIS A 1 432 ? 39.871 115.270 36.773  1.00 36.44 ? 432  HIS A ND1 1 
ATOM   3455 C CD2 . HIS A 1 432 ? 40.949 113.382 36.569  1.00 34.30 ? 432  HIS A CD2 1 
ATOM   3456 C CE1 . HIS A 1 432 ? 41.162 115.543 36.875  1.00 38.91 ? 432  HIS A CE1 1 
ATOM   3457 N NE2 . HIS A 1 432 ? 41.838 114.412 36.759  1.00 36.11 ? 432  HIS A NE2 1 
ATOM   3458 N N   . ASN A 1 433 ? 36.395 114.224 38.826  1.00 34.69 ? 433  ASN A N   1 
ATOM   3459 C CA  . ASN A 1 433 ? 35.939 115.138 39.869  1.00 36.33 ? 433  ASN A CA  1 
ATOM   3460 C C   . ASN A 1 433 ? 36.026 114.527 41.246  1.00 36.58 ? 433  ASN A C   1 
ATOM   3461 O O   . ASN A 1 433 ? 36.252 115.227 42.217  1.00 37.86 ? 433  ASN A O   1 
ATOM   3462 C CB  . ASN A 1 433 ? 34.475 115.517 39.609  1.00 36.87 ? 433  ASN A CB  1 
ATOM   3463 C CG  . ASN A 1 433 ? 34.326 116.488 38.479  1.00 40.69 ? 433  ASN A CG  1 
ATOM   3464 O OD1 . ASN A 1 433 ? 35.210 117.313 38.247  1.00 43.43 ? 433  ASN A OD1 1 
ATOM   3465 N ND2 . ASN A 1 433 ? 33.193 116.410 37.756  1.00 45.49 ? 433  ASN A ND2 1 
ATOM   3466 N N   . GLN A 1 434 ? 35.853 113.223 41.347  1.00 37.01 ? 434  GLN A N   1 
ATOM   3467 C CA  . GLN A 1 434 ? 36.060 112.550 42.647  1.00 38.31 ? 434  GLN A CA  1 
ATOM   3468 C C   . GLN A 1 434 ? 37.509 112.133 42.903  1.00 37.58 ? 434  GLN A C   1 
ATOM   3469 O O   . GLN A 1 434 ? 37.987 112.264 44.021  1.00 37.49 ? 434  GLN A O   1 
ATOM   3470 C CB  . GLN A 1 434 ? 35.173 111.306 42.775  1.00 38.92 ? 434  GLN A CB  1 
ATOM   3471 C CG  . GLN A 1 434 ? 33.788 111.439 42.177  1.00 43.23 ? 434  GLN A CG  1 
ATOM   3472 C CD  . GLN A 1 434 ? 33.053 110.113 42.171  1.00 48.89 ? 434  GLN A CD  1 
ATOM   3473 O OE1 . GLN A 1 434 ? 32.447 109.727 41.156  1.00 53.18 ? 434  GLN A OE1 1 
ATOM   3474 N NE2 . GLN A 1 434 ? 33.112 109.395 43.297  1.00 50.83 ? 434  GLN A NE2 1 
ATOM   3475 N N   . VAL A 1 435 ? 38.161 111.547 41.883  1.00 36.60 ? 435  VAL A N   1 
ATOM   3476 C CA  . VAL A 1 435 ? 39.554 111.062 41.977  1.00 36.12 ? 435  VAL A CA  1 
ATOM   3477 C C   . VAL A 1 435 ? 40.336 111.736 40.852  1.00 35.24 ? 435  VAL A C   1 
ATOM   3478 O O   . VAL A 1 435 ? 40.025 111.535 39.683  1.00 34.36 ? 435  VAL A O   1 
ATOM   3479 C CB  . VAL A 1 435 ? 39.684 109.518 41.815  1.00 36.14 ? 435  VAL A CB  1 
ATOM   3480 C CG1 . VAL A 1 435 ? 41.104 109.055 42.210  1.00 37.43 ? 435  VAL A CG1 1 
ATOM   3481 C CG2 . VAL A 1 435 ? 38.631 108.786 42.661  1.00 37.94 ? 435  VAL A CG2 1 
ATOM   3482 N N   . GLU A 1 436 ? 41.316 112.558 41.211  1.00 34.63 ? 436  GLU A N   1 
ATOM   3483 C CA  . GLU A 1 436 ? 42.062 113.323 40.214  1.00 34.75 ? 436  GLU A CA  1 
ATOM   3484 C C   . GLU A 1 436 ? 43.203 112.461 39.681  1.00 31.91 ? 436  GLU A C   1 
ATOM   3485 O O   . GLU A 1 436 ? 44.366 112.756 39.928  1.00 31.76 ? 436  GLU A O   1 
ATOM   3486 C CB  . GLU A 1 436 ? 42.653 114.597 40.827  1.00 35.03 ? 436  GLU A CB  1 
ATOM   3487 C CG  . GLU A 1 436 ? 41.624 115.433 41.569  1.00 39.62 ? 436  GLU A CG  1 
ATOM   3488 C CD  . GLU A 1 436 ? 42.025 116.902 41.821  1.00 39.96 ? 436  GLU A CD  1 
ATOM   3489 O OE1 . GLU A 1 436 ? 43.221 117.225 42.060  1.00 46.63 ? 436  GLU A OE1 1 
ATOM   3490 O OE2 . GLU A 1 436 ? 41.096 117.742 41.803  1.00 46.88 ? 436  GLU A OE2 1 
ATOM   3491 N N   . PHE A 1 437 ? 42.873 111.403 38.953  1.00 28.82 ? 437  PHE A N   1 
ATOM   3492 C CA  . PHE A 1 437 ? 43.922 110.581 38.305  1.00 26.31 ? 437  PHE A CA  1 
ATOM   3493 C C   . PHE A 1 437 ? 44.644 111.383 37.196  1.00 25.57 ? 437  PHE A C   1 
ATOM   3494 O O   . PHE A 1 437 ? 44.089 112.367 36.662  1.00 25.04 ? 437  PHE A O   1 
ATOM   3495 C CB  . PHE A 1 437 ? 43.303 109.309 37.724  1.00 25.63 ? 437  PHE A CB  1 
ATOM   3496 C CG  . PHE A 1 437 ? 42.151 109.565 36.798  1.00 27.30 ? 437  PHE A CG  1 
ATOM   3497 C CD1 . PHE A 1 437 ? 42.349 109.740 35.435  1.00 25.96 ? 437  PHE A CD1 1 
ATOM   3498 C CD2 . PHE A 1 437 ? 40.847 109.655 37.303  1.00 29.11 ? 437  PHE A CD2 1 
ATOM   3499 C CE1 . PHE A 1 437 ? 41.273 109.999 34.571  1.00 31.64 ? 437  PHE A CE1 1 
ATOM   3500 C CE2 . PHE A 1 437 ? 39.773 109.908 36.436  1.00 28.79 ? 437  PHE A CE2 1 
ATOM   3501 C CZ  . PHE A 1 437 ? 39.986 110.077 35.081  1.00 27.89 ? 437  PHE A CZ  1 
ATOM   3502 N N   . ASP A 1 438 ? 45.836 110.925 36.821  1.00 22.86 ? 438  ASP A N   1 
ATOM   3503 C CA  . ASP A 1 438 ? 46.685 111.611 35.819  1.00 23.60 ? 438  ASP A CA  1 
ATOM   3504 C C   . ASP A 1 438 ? 46.765 110.927 34.469  1.00 22.42 ? 438  ASP A C   1 
ATOM   3505 O O   . ASP A 1 438 ? 47.130 111.547 33.470  1.00 24.88 ? 438  ASP A O   1 
ATOM   3506 C CB  . ASP A 1 438 ? 48.092 111.820 36.397  1.00 22.48 ? 438  ASP A CB  1 
ATOM   3507 C CG  . ASP A 1 438 ? 48.055 112.596 37.690  1.00 26.69 ? 438  ASP A CG  1 
ATOM   3508 O OD1 . ASP A 1 438 ? 47.822 113.837 37.623  1.00 31.71 ? 438  ASP A OD1 1 
ATOM   3509 O OD2 . ASP A 1 438 ? 48.212 111.986 38.771  1.00 24.88 ? 438  ASP A OD2 1 
ATOM   3510 N N   . GLY A 1 439 ? 46.414 109.651 34.428  1.00 21.77 ? 439  GLY A N   1 
ATOM   3511 C CA  . GLY A 1 439 ? 46.463 108.884 33.197  1.00 21.76 ? 439  GLY A CA  1 
ATOM   3512 C C   . GLY A 1 439 ? 45.660 107.631 33.384  1.00 21.54 ? 439  GLY A C   1 
ATOM   3513 O O   . GLY A 1 439 ? 45.168 107.371 34.496  1.00 21.48 ? 439  GLY A O   1 
ATOM   3514 N N   . ILE A 1 440 ? 45.542 106.848 32.322  1.00 21.28 ? 440  ILE A N   1 
ATOM   3515 C CA  . ILE A 1 440 ? 44.579 105.775 32.283  1.00 22.97 ? 440  ILE A CA  1 
ATOM   3516 C C   . ILE A 1 440 ? 45.236 104.529 31.735  1.00 22.89 ? 440  ILE A C   1 
ATOM   3517 O O   . ILE A 1 440 ? 45.899 104.577 30.714  1.00 23.60 ? 440  ILE A O   1 
ATOM   3518 C CB  . ILE A 1 440 ? 43.385 106.163 31.384  1.00 22.56 ? 440  ILE A CB  1 
ATOM   3519 C CG1 . ILE A 1 440 ? 42.721 107.420 31.965  1.00 24.52 ? 440  ILE A CG1 1 
ATOM   3520 C CG2 . ILE A 1 440 ? 42.357 105.014 31.369  1.00 23.73 ? 440  ILE A CG2 1 
ATOM   3521 C CD1 . ILE A 1 440 ? 41.862 108.255 30.933  1.00 24.82 ? 440  ILE A CD1 1 
ATOM   3522 N N   . TRP A 1 441 ? 45.026 103.416 32.414  1.00 21.36 ? 441  TRP A N   1 
ATOM   3523 C CA  . TRP A 1 441 ? 45.442 102.131 31.952  1.00 20.37 ? 441  TRP A CA  1 
ATOM   3524 C C   . TRP A 1 441 ? 44.196 101.302 31.478  1.00 22.02 ? 441  TRP A C   1 
ATOM   3525 O O   . TRP A 1 441 ? 43.330 100.955 32.281  1.00 20.98 ? 441  TRP A O   1 
ATOM   3526 C CB  . TRP A 1 441 ? 46.143 101.515 33.161  1.00 21.55 ? 441  TRP A CB  1 
ATOM   3527 C CG  . TRP A 1 441 ? 46.440 100.097 33.060  1.00 23.75 ? 441  TRP A CG  1 
ATOM   3528 C CD1 . TRP A 1 441 ? 46.513 99.345  31.940  1.00 23.98 ? 441  TRP A CD1 1 
ATOM   3529 C CD2 . TRP A 1 441 ? 46.753 99.243  34.155  1.00 24.09 ? 441  TRP A CD2 1 
ATOM   3530 N NE1 . TRP A 1 441 ? 46.824 98.030  32.274  1.00 25.34 ? 441  TRP A NE1 1 
ATOM   3531 C CE2 . TRP A 1 441 ? 46.991 97.954  33.626  1.00 25.24 ? 441  TRP A CE2 1 
ATOM   3532 C CE3 . TRP A 1 441 ? 46.830 99.443  35.536  1.00 26.01 ? 441  TRP A CE3 1 
ATOM   3533 C CZ2 . TRP A 1 441 ? 47.306 96.854  34.430  1.00 26.24 ? 441  TRP A CZ2 1 
ATOM   3534 C CZ3 . TRP A 1 441 ? 47.156 98.315  36.357  1.00 26.78 ? 441  TRP A CZ3 1 
ATOM   3535 C CH2 . TRP A 1 441 ? 47.374 97.053  35.780  1.00 26.39 ? 441  TRP A CH2 1 
ATOM   3536 N N   . ILE A 1 442 ? 44.097 101.025 30.183  1.00 21.60 ? 442  ILE A N   1 
ATOM   3537 C CA  . ILE A 1 442 ? 42.955 100.328 29.594  1.00 22.77 ? 442  ILE A CA  1 
ATOM   3538 C C   . ILE A 1 442 ? 43.375 98.884  29.415  1.00 24.07 ? 442  ILE A C   1 
ATOM   3539 O O   . ILE A 1 442 ? 44.411 98.571  28.799  1.00 24.02 ? 442  ILE A O   1 
ATOM   3540 C CB  . ILE A 1 442 ? 42.365 100.999 28.290  1.00 22.44 ? 442  ILE A CB  1 
ATOM   3541 C CG1 . ILE A 1 442 ? 43.402 101.240 27.219  1.00 23.33 ? 442  ILE A CG1 1 
ATOM   3542 C CG2 . ILE A 1 442 ? 41.776 102.398 28.581  1.00 24.66 ? 442  ILE A CG2 1 
ATOM   3543 C CD1 . ILE A 1 442 ? 42.806 101.844 25.934  1.00 24.49 ? 442  ILE A CD1 1 
ATOM   3544 N N   . ASP A 1 443 ? 42.613 98.004  30.056  1.00 23.89 ? 443  ASP A N   1 
ATOM   3545 C CA  . ASP A 1 443 ? 42.928 96.606  30.130  1.00 24.62 ? 443  ASP A CA  1 
ATOM   3546 C C   . ASP A 1 443 ? 41.721 95.821  29.645  1.00 24.15 ? 443  ASP A C   1 
ATOM   3547 O O   . ASP A 1 443 ? 40.687 96.420  29.387  1.00 24.36 ? 443  ASP A O   1 
ATOM   3548 C CB  . ASP A 1 443 ? 43.273 96.285  31.583  1.00 26.09 ? 443  ASP A CB  1 
ATOM   3549 C CG  . ASP A 1 443 ? 43.862 94.895  31.758  1.00 29.01 ? 443  ASP A CG  1 
ATOM   3550 O OD1 . ASP A 1 443 ? 44.541 94.404  30.827  1.00 32.32 ? 443  ASP A OD1 1 
ATOM   3551 O OD2 . ASP A 1 443 ? 43.638 94.301  32.846  1.00 31.67 ? 443  ASP A OD2 1 
ATOM   3552 N N   . MET A 1 444 ? 41.910 94.513  29.439  1.00 25.28 ? 444  MET A N   1 
ATOM   3553 C CA  . MET A 1 444 ? 40.873 93.532  29.045  1.00 25.59 ? 444  MET A CA  1 
ATOM   3554 C C   . MET A 1 444 ? 40.212 93.911  27.741  1.00 25.26 ? 444  MET A C   1 
ATOM   3555 O O   . MET A 1 444 ? 39.038 93.584  27.511  1.00 24.11 ? 444  MET A O   1 
ATOM   3556 C CB  . MET A 1 444 ? 39.802 93.411  30.139  1.00 26.29 ? 444  MET A CB  1 
ATOM   3557 C CG  . MET A 1 444 ? 40.303 93.250  31.543  1.00 28.10 ? 444  MET A CG  1 
ATOM   3558 S SD  . MET A 1 444 ? 41.286 91.745  31.836  1.00 35.52 ? 444  MET A SD  1 
ATOM   3559 C CE  . MET A 1 444 ? 39.982 90.511  31.804  1.00 28.19 ? 444  MET A CE  1 
ATOM   3560 N N   . ASN A 1 445 ? 40.947 94.629  26.885  1.00 23.92 ? 445  ASN A N   1 
ATOM   3561 C CA  . ASN A 1 445 ? 40.318 95.212  25.701  1.00 23.68 ? 445  ASN A CA  1 
ATOM   3562 C C   . ASN A 1 445 ? 40.558 94.460  24.400  1.00 24.75 ? 445  ASN A C   1 
ATOM   3563 O O   . ASN A 1 445 ? 40.565 95.051  23.352  1.00 22.11 ? 445  ASN A O   1 
ATOM   3564 C CB  . ASN A 1 445 ? 40.646 96.720  25.585  1.00 24.35 ? 445  ASN A CB  1 
ATOM   3565 C CG  . ASN A 1 445 ? 42.132 97.003  25.611  1.00 23.19 ? 445  ASN A CG  1 
ATOM   3566 O OD1 . ASN A 1 445 ? 42.927 96.117  25.841  1.00 23.55 ? 445  ASN A OD1 1 
ATOM   3567 N ND2 . ASN A 1 445 ? 42.506 98.249  25.365  1.00 23.42 ? 445  ASN A ND2 1 
ATOM   3568 N N   . GLU A 1 446 ? 40.718 93.140  24.485  1.00 25.89 ? 446  GLU A N   1 
ATOM   3569 C CA  . GLU A 1 446 ? 40.834 92.263  23.310  1.00 28.74 ? 446  GLU A CA  1 
ATOM   3570 C C   . GLU A 1 446 ? 39.610 92.140  22.360  1.00 29.43 ? 446  GLU A C   1 
ATOM   3571 O O   . GLU A 1 446 ? 39.802 92.103  21.145  1.00 30.45 ? 446  GLU A O   1 
ATOM   3572 C CB  . GLU A 1 446 ? 41.391 90.890  23.724  1.00 28.01 ? 446  GLU A CB  1 
ATOM   3573 C CG  . GLU A 1 446 ? 42.791 90.933  24.274  1.00 28.89 ? 446  GLU A CG  1 
ATOM   3574 C CD  . GLU A 1 446 ? 42.952 91.560  25.647  1.00 35.31 ? 446  GLU A CD  1 
ATOM   3575 O OE1 . GLU A 1 446 ? 42.063 91.396  26.523  1.00 33.33 ? 446  GLU A OE1 1 
ATOM   3576 O OE2 . GLU A 1 446 ? 44.027 92.218  25.873  1.00 39.04 ? 446  GLU A OE2 1 
ATOM   3577 N N   . VAL A 1 447 ? 38.356 92.115  22.818  1.00 31.61 ? 447  VAL A N   1 
ATOM   3578 C CA  . VAL A 1 447 ? 37.878 92.306  24.185  1.00 32.22 ? 447  VAL A CA  1 
ATOM   3579 C C   . VAL A 1 447 ? 37.783 90.952  24.931  1.00 32.35 ? 447  VAL A C   1 
ATOM   3580 O O   . VAL A 1 447 ? 37.483 89.897  24.344  1.00 33.73 ? 447  VAL A O   1 
ATOM   3581 C CB  . VAL A 1 447 ? 36.520 93.130  24.142  1.00 32.53 ? 447  VAL A CB  1 
ATOM   3582 C CG1 . VAL A 1 447 ? 35.478 92.346  23.523  1.00 32.98 ? 447  VAL A CG1 1 
ATOM   3583 C CG2 . VAL A 1 447 ? 36.074 93.593  25.512  1.00 32.84 ? 447  VAL A CG2 1 
ATOM   3584 N N   . SER A 1 448 ? 38.083 90.980  26.218  1.00 31.90 ? 448  SER A N   1 
ATOM   3585 C CA  . SER A 1 448 ? 38.313 89.761  26.971  1.00 32.38 ? 448  SER A CA  1 
ATOM   3586 C C   . SER A 1 448 ? 36.992 89.478  27.677  1.00 32.01 ? 448  SER A C   1 
ATOM   3587 O O   . SER A 1 448 ? 36.387 90.388  28.223  1.00 32.64 ? 448  SER A O   1 
ATOM   3588 C CB  . SER A 1 448 ? 39.477 89.969  27.928  1.00 31.32 ? 448  SER A CB  1 
ATOM   3589 O OG  . SER A 1 448 ? 39.635 88.888  28.811  1.00 36.14 ? 448  SER A OG  1 
ATOM   3590 N N   . ASN A 1 449 ? 36.521 88.234  27.598  1.00 30.52 ? 449  ASN A N   1 
ATOM   3591 C CA  . ASN A 1 449 ? 35.190 87.854  28.117  1.00 30.37 ? 449  ASN A CA  1 
ATOM   3592 C C   . ASN A 1 449 ? 35.406 86.602  28.963  1.00 29.93 ? 449  ASN A C   1 
ATOM   3593 O O   . ASN A 1 449 ? 36.152 85.703  28.553  1.00 30.43 ? 449  ASN A O   1 
ATOM   3594 C CB  . ASN A 1 449 ? 34.255 87.541  26.935  1.00 28.43 ? 449  ASN A CB  1 
ATOM   3595 C CG  . ASN A 1 449 ? 32.771 87.530  27.308  1.00 31.61 ? 449  ASN A CG  1 
ATOM   3596 O OD1 . ASN A 1 449 ? 32.378 87.798  28.462  1.00 30.79 ? 449  ASN A OD1 1 
ATOM   3597 N ND2 . ASN A 1 449 ? 31.926 87.214  26.318  1.00 28.57 ? 449  ASN A ND2 1 
ATOM   3598 N N   . PHE A 1 450 ? 34.818 86.542  30.153  1.00 29.75 ? 450  PHE A N   1 
ATOM   3599 C CA  . PHE A 1 450 ? 35.026 85.339  30.967  1.00 29.61 ? 450  PHE A CA  1 
ATOM   3600 C C   . PHE A 1 450 ? 34.100 84.189  30.514  1.00 29.96 ? 450  PHE A C   1 
ATOM   3601 O O   . PHE A 1 450 ? 34.301 83.053  30.924  1.00 30.91 ? 450  PHE A O   1 
ATOM   3602 C CB  . PHE A 1 450 ? 34.905 85.612  32.472  1.00 28.59 ? 450  PHE A CB  1 
ATOM   3603 C CG  . PHE A 1 450 ? 35.957 86.535  33.027  1.00 30.14 ? 450  PHE A CG  1 
ATOM   3604 C CD1 . PHE A 1 450 ? 37.143 86.805  32.324  1.00 29.46 ? 450  PHE A CD1 1 
ATOM   3605 C CD2 . PHE A 1 450 ? 35.786 87.101  34.285  1.00 28.82 ? 450  PHE A CD2 1 
ATOM   3606 C CE1 . PHE A 1 450 ? 38.124 87.655  32.878  1.00 30.81 ? 450  PHE A CE1 1 
ATOM   3607 C CE2 . PHE A 1 450 ? 36.732 87.936  34.833  1.00 29.34 ? 450  PHE A CE2 1 
ATOM   3608 C CZ  . PHE A 1 450 ? 37.913 88.225  34.127  1.00 30.16 ? 450  PHE A CZ  1 
ATOM   3609 N N   . VAL A 1 451 ? 33.091 84.486  29.697  1.00 29.40 ? 451  VAL A N   1 
ATOM   3610 C CA  . VAL A 1 451 ? 32.303 83.438  29.009  1.00 29.53 ? 451  VAL A CA  1 
ATOM   3611 C C   . VAL A 1 451 ? 32.688 83.427  27.523  1.00 30.34 ? 451  VAL A C   1 
ATOM   3612 O O   . VAL A 1 451 ? 33.190 84.426  27.001  1.00 29.72 ? 451  VAL A O   1 
ATOM   3613 C CB  . VAL A 1 451 ? 30.809 83.666  29.153  1.00 29.72 ? 451  VAL A CB  1 
ATOM   3614 C CG1 . VAL A 1 451 ? 30.390 83.510  30.652  1.00 30.40 ? 451  VAL A CG1 1 
ATOM   3615 C CG2 . VAL A 1 451 ? 30.391 85.032  28.591  1.00 27.25 ? 451  VAL A CG2 1 
ATOM   3616 N N   . ASP A 1 452 ? 32.454 82.319  26.839  1.00 29.89 ? 452  ASP A N   1 
ATOM   3617 C CA  . ASP A 1 452 ? 32.749 82.248  25.420  1.00 30.14 ? 452  ASP A CA  1 
ATOM   3618 C C   . ASP A 1 452 ? 31.617 82.855  24.636  1.00 30.69 ? 452  ASP A C   1 
ATOM   3619 O O   . ASP A 1 452 ? 30.533 82.270  24.574  1.00 30.50 ? 452  ASP A O   1 
ATOM   3620 C CB  . ASP A 1 452 ? 32.897 80.801  25.007  1.00 30.17 ? 452  ASP A CB  1 
ATOM   3621 C CG  . ASP A 1 452 ? 34.174 80.161  25.544  1.00 33.50 ? 452  ASP A CG  1 
ATOM   3622 O OD1 . ASP A 1 452 ? 35.159 80.880  25.881  1.00 30.67 ? 452  ASP A OD1 1 
ATOM   3623 O OD2 . ASP A 1 452 ? 34.202 78.909  25.632  1.00 37.82 ? 452  ASP A OD2 1 
ATOM   3624 N N   . GLY A 1 453 ? 31.847 84.010  24.024  1.00 29.05 ? 453  GLY A N   1 
ATOM   3625 C CA  . GLY A 1 453 ? 30.853 84.599  23.134  1.00 28.84 ? 453  GLY A CA  1 
ATOM   3626 C C   . GLY A 1 453 ? 29.882 85.498  23.842  1.00 30.29 ? 453  GLY A C   1 
ATOM   3627 O O   . GLY A 1 453 ? 29.916 86.711  23.668  1.00 29.37 ? 453  GLY A O   1 
ATOM   3628 N N   . SER A 1 454 ? 29.002 84.901  24.649  1.00 30.01 ? 454  SER A N   1 
ATOM   3629 C CA  . SER A 1 454 ? 28.095 85.667  25.495  1.00 31.81 ? 454  SER A CA  1 
ATOM   3630 C C   . SER A 1 454 ? 27.561 84.733  26.573  1.00 31.21 ? 454  SER A C   1 
ATOM   3631 O O   . SER A 1 454 ? 27.938 83.560  26.609  1.00 30.01 ? 454  SER A O   1 
ATOM   3632 C CB  . SER A 1 454 ? 26.940 86.284  24.697  1.00 31.73 ? 454  SER A CB  1 
ATOM   3633 O OG  . SER A 1 454 ? 25.961 85.307  24.293  1.00 38.69 ? 454  SER A OG  1 
ATOM   3634 N N   . VAL A 1 455 ? 26.724 85.260  27.464  1.00 32.11 ? 455  VAL A N   1 
ATOM   3635 C CA  . VAL A 1 455 ? 26.143 84.426  28.545  1.00 32.59 ? 455  VAL A CA  1 
ATOM   3636 C C   . VAL A 1 455 ? 25.236 83.327  27.969  1.00 34.50 ? 455  VAL A C   1 
ATOM   3637 O O   . VAL A 1 455 ? 25.051 82.292  28.586  1.00 35.17 ? 455  VAL A O   1 
ATOM   3638 C CB  . VAL A 1 455 ? 25.441 85.258  29.643  1.00 32.69 ? 455  VAL A CB  1 
ATOM   3639 C CG1 . VAL A 1 455 ? 26.469 86.078  30.401  1.00 30.48 ? 455  VAL A CG1 1 
ATOM   3640 C CG2 . VAL A 1 455 ? 24.357 86.156  29.041  1.00 30.87 ? 455  VAL A CG2 1 
ATOM   3641 N N   . SER A 1 456 ? 24.706 83.536  26.772  1.00 35.99 ? 456  SER A N   1 
ATOM   3642 C CA  . SER A 1 456 ? 23.968 82.478  26.089  1.00 38.08 ? 456  SER A CA  1 
ATOM   3643 C C   . SER A 1 456 ? 24.757 81.718  25.011  1.00 38.40 ? 456  SER A C   1 
ATOM   3644 O O   . SER A 1 456 ? 24.185 80.980  24.235  1.00 40.13 ? 456  SER A O   1 
ATOM   3645 C CB  . SER A 1 456 ? 22.618 83.009  25.574  1.00 38.08 ? 456  SER A CB  1 
ATOM   3646 O OG  . SER A 1 456 ? 22.720 84.277  24.941  1.00 40.62 ? 456  SER A OG  1 
ATOM   3647 N N   . GLY A 1 457 ? 26.081 81.856  25.000  1.00 38.87 ? 457  GLY A N   1 
ATOM   3648 C CA  . GLY A 1 457 ? 26.902 81.239  23.976  1.00 39.95 ? 457  GLY A CA  1 
ATOM   3649 C C   . GLY A 1 457 ? 26.714 81.906  22.623  1.00 40.15 ? 457  GLY A C   1 
ATOM   3650 O O   . GLY A 1 457 ? 26.286 83.052  22.538  1.00 41.69 ? 457  GLY A O   1 
ATOM   3651 N N   . CYS A 1 458 ? 27.014 81.166  21.574  1.00 40.15 ? 458  CYS A N   1 
ATOM   3652 C CA  . CYS A 1 458 ? 27.044 81.680  20.212  1.00 40.65 ? 458  CYS A CA  1 
ATOM   3653 C C   . CYS A 1 458 ? 26.248 80.764  19.299  1.00 39.64 ? 458  CYS A C   1 
ATOM   3654 O O   . CYS A 1 458 ? 26.339 79.556  19.418  1.00 40.74 ? 458  CYS A O   1 
ATOM   3655 C CB  . CYS A 1 458 ? 28.486 81.654  19.706  1.00 40.03 ? 458  CYS A CB  1 
ATOM   3656 S SG  . CYS A 1 458 ? 29.562 82.757  20.556  1.00 45.62 ? 458  CYS A SG  1 
ATOM   3657 N N   . SER A 1 459 ? 25.521 81.332  18.350  1.00 39.79 ? 459  SER A N   1 
ATOM   3658 C CA  . SER A 1 459 ? 24.832 80.521  17.339  1.00 39.88 ? 459  SER A CA  1 
ATOM   3659 C C   . SER A 1 459 ? 25.857 79.861  16.425  1.00 38.98 ? 459  SER A C   1 
ATOM   3660 O O   . SER A 1 459 ? 26.929 80.404  16.217  1.00 37.94 ? 459  SER A O   1 
ATOM   3661 C CB  . SER A 1 459 ? 23.931 81.410  16.486  1.00 40.09 ? 459  SER A CB  1 
ATOM   3662 O OG  . SER A 1 459 ? 22.995 82.102  17.304  1.00 44.58 ? 459  SER A OG  1 
ATOM   3663 N N   . THR A 1 460 ? 25.511 78.710  15.863  1.00 38.32 ? 460  THR A N   1 
ATOM   3664 C CA  . THR A 1 460 ? 26.350 78.038  14.869  1.00 38.20 ? 460  THR A CA  1 
ATOM   3665 C C   . THR A 1 460 ? 26.048 78.747  13.565  1.00 37.52 ? 460  THR A C   1 
ATOM   3666 O O   . THR A 1 460 ? 24.889 78.819  13.145  1.00 37.29 ? 460  THR A O   1 
ATOM   3667 C CB  . THR A 1 460 ? 26.036 76.533  14.770  1.00 38.93 ? 460  THR A CB  1 
ATOM   3668 O OG1 . THR A 1 460 ? 26.381 75.900  16.008  1.00 40.30 ? 460  THR A OG1 1 
ATOM   3669 C CG2 . THR A 1 460 ? 26.840 75.864  13.661  1.00 38.14 ? 460  THR A CG2 1 
ATOM   3670 N N   . ASN A 1 461 ? 27.075 79.364  12.983  1.00 35.90 ? 461  ASN A N   1 
ATOM   3671 C CA  . ASN A 1 461 ? 26.964 80.029  11.673  1.00 34.52 ? 461  ASN A CA  1 
ATOM   3672 C C   . ASN A 1 461 ? 28.380 80.208  11.116  1.00 34.36 ? 461  ASN A C   1 
ATOM   3673 O O   . ASN A 1 461 ? 29.367 79.906  11.818  1.00 32.71 ? 461  ASN A O   1 
ATOM   3674 C CB  . ASN A 1 461 ? 26.192 81.368  11.729  1.00 34.44 ? 461  ASN A CB  1 
ATOM   3675 C CG  . ASN A 1 461 ? 26.805 82.375  12.700  1.00 34.10 ? 461  ASN A CG  1 
ATOM   3676 O OD1 . ASN A 1 461 ? 28.019 82.554  12.741  1.00 36.54 ? 461  ASN A OD1 1 
ATOM   3677 N ND2 . ASN A 1 461 ? 25.965 83.056  13.453  1.00 33.19 ? 461  ASN A ND2 1 
ATOM   3678 N N   . ASN A 1 462 ? 28.475 80.659  9.867   1.00 33.47 ? 462  ASN A N   1 
ATOM   3679 C CA  . ASN A 1 462 ? 29.773 80.753  9.184   1.00 33.45 ? 462  ASN A CA  1 
ATOM   3680 C C   . ASN A 1 462 ? 30.746 81.786  9.832   1.00 31.49 ? 462  ASN A C   1 
ATOM   3681 O O   . ASN A 1 462 ? 31.933 81.790  9.516   1.00 31.38 ? 462  ASN A O   1 
ATOM   3682 C CB  . ASN A 1 462 ? 29.559 81.081  7.695   1.00 34.25 ? 462  ASN A CB  1 
ATOM   3683 C CG  . ASN A 1 462 ? 28.872 82.446  7.492   1.00 39.62 ? 462  ASN A CG  1 
ATOM   3684 O OD1 . ASN A 1 462 ? 27.782 82.711  8.049   1.00 47.12 ? 462  ASN A OD1 1 
ATOM   3685 N ND2 . ASN A 1 462 ? 29.516 83.334  6.702   1.00 46.24 ? 462  ASN A ND2 1 
ATOM   3686 N N   . LEU A 1 463 ? 30.248 82.650  10.712  1.00 30.71 ? 463  LEU A N   1 
ATOM   3687 C CA  . LEU A 1 463 ? 31.075 83.619  11.421  1.00 29.97 ? 463  LEU A CA  1 
ATOM   3688 C C   . LEU A 1 463 ? 31.656 83.065  12.715  1.00 30.99 ? 463  LEU A C   1 
ATOM   3689 O O   . LEU A 1 463 ? 32.861 83.183  12.974  1.00 30.40 ? 463  LEU A O   1 
ATOM   3690 C CB  . LEU A 1 463 ? 30.308 84.893  11.728  1.00 29.74 ? 463  LEU A CB  1 
ATOM   3691 C CG  . LEU A 1 463 ? 29.753 85.604  10.495  1.00 30.64 ? 463  LEU A CG  1 
ATOM   3692 C CD1 . LEU A 1 463 ? 29.199 86.953  10.892  1.00 27.33 ? 463  LEU A CD1 1 
ATOM   3693 C CD2 . LEU A 1 463 ? 30.817 85.721  9.425   1.00 27.07 ? 463  LEU A CD2 1 
ATOM   3694 N N   . ASN A 1 464 ? 30.792 82.498  13.564  1.00 30.81 ? 464  ASN A N   1 
ATOM   3695 C CA  . ASN A 1 464 ? 31.247 81.845  14.773  1.00 30.64 ? 464  ASN A CA  1 
ATOM   3696 C C   . ASN A 1 464 ? 32.018 80.582  14.515  1.00 30.52 ? 464  ASN A C   1 
ATOM   3697 O O   . ASN A 1 464 ? 32.878 80.218  15.316  1.00 30.74 ? 464  ASN A O   1 
ATOM   3698 C CB  . ASN A 1 464 ? 30.077 81.540  15.720  1.00 30.65 ? 464  ASN A CB  1 
ATOM   3699 C CG  . ASN A 1 464 ? 29.572 82.761  16.378  1.00 31.97 ? 464  ASN A CG  1 
ATOM   3700 O OD1 . ASN A 1 464 ? 28.368 83.004  16.430  1.00 37.50 ? 464  ASN A OD1 1 
ATOM   3701 N ND2 . ASN A 1 464 ? 30.488 83.588  16.839  1.00 31.63 ? 464  ASN A ND2 1 
ATOM   3702 N N   . ASN A 1 465 ? 31.677 79.913  13.411  1.00 30.44 ? 465  ASN A N   1 
ATOM   3703 C CA  . ASN A 1 465 ? 32.247 78.624  13.021  1.00 30.15 ? 465  ASN A CA  1 
ATOM   3704 C C   . ASN A 1 465 ? 32.648 78.650  11.550  1.00 30.10 ? 465  ASN A C   1 
ATOM   3705 O O   . ASN A 1 465 ? 32.019 77.996  10.723  1.00 29.21 ? 465  ASN A O   1 
ATOM   3706 C CB  . ASN A 1 465 ? 31.241 77.479  13.280  1.00 30.55 ? 465  ASN A CB  1 
ATOM   3707 C CG  . ASN A 1 465 ? 30.623 77.577  14.671  1.00 31.11 ? 465  ASN A CG  1 
ATOM   3708 O OD1 . ASN A 1 465 ? 31.209 77.115  15.657  1.00 35.21 ? 465  ASN A OD1 1 
ATOM   3709 N ND2 . ASN A 1 465 ? 29.489 78.230  14.762  1.00 30.08 ? 465  ASN A ND2 1 
ATOM   3710 N N   . PRO A 1 466 ? 33.737 79.383  11.227  1.00 29.97 ? 466  PRO A N   1 
ATOM   3711 C CA  . PRO A 1 466 ? 34.125 79.562  9.816   1.00 29.76 ? 466  PRO A CA  1 
ATOM   3712 C C   . PRO A 1 466 ? 34.692 78.293  9.172   1.00 30.18 ? 466  PRO A C   1 
ATOM   3713 O O   . PRO A 1 466 ? 35.095 77.366  9.882   1.00 30.64 ? 466  PRO A O   1 
ATOM   3714 C CB  . PRO A 1 466 ? 35.205 80.689  9.901   1.00 29.66 ? 466  PRO A CB  1 
ATOM   3715 C CG  . PRO A 1 466 ? 35.814 80.510  11.160  1.00 29.49 ? 466  PRO A CG  1 
ATOM   3716 C CD  . PRO A 1 466 ? 34.686 80.068  12.128  1.00 29.07 ? 466  PRO A CD  1 
ATOM   3717 N N   . PRO A 1 467 ? 34.761 78.259  7.814   1.00 30.81 ? 467  PRO A N   1 
ATOM   3718 C CA  . PRO A 1 467 ? 35.346 77.181  6.999   1.00 30.35 ? 467  PRO A CA  1 
ATOM   3719 C C   . PRO A 1 467 ? 36.782 76.801  7.394   1.00 30.79 ? 467  PRO A C   1 
ATOM   3720 O O   . PRO A 1 467 ? 37.123 75.616  7.413   1.00 30.25 ? 467  PRO A O   1 
ATOM   3721 C CB  . PRO A 1 467 ? 35.368 77.775  5.588   1.00 31.57 ? 467  PRO A CB  1 
ATOM   3722 C CG  . PRO A 1 467 ? 34.345 78.878  5.590   1.00 32.03 ? 467  PRO A CG  1 
ATOM   3723 C CD  . PRO A 1 467 ? 34.196 79.356  6.999   1.00 30.02 ? 467  PRO A CD  1 
ATOM   3724 N N   . PHE A 1 468 ? 37.613 77.818  7.659   1.00 28.95 ? 468  PHE A N   1 
ATOM   3725 C CA  . PHE A 1 468 ? 38.982 77.653  8.125   1.00 27.91 ? 468  PHE A CA  1 
ATOM   3726 C C   . PHE A 1 468 ? 39.179 78.491  9.400   1.00 26.83 ? 468  PHE A C   1 
ATOM   3727 O O   . PHE A 1 468 ? 38.774 79.657  9.438   1.00 25.73 ? 468  PHE A O   1 
ATOM   3728 C CB  . PHE A 1 468 ? 39.970 78.167  7.065   1.00 27.58 ? 468  PHE A CB  1 
ATOM   3729 C CG  . PHE A 1 468 ? 41.419 78.054  7.488   1.00 26.22 ? 468  PHE A CG  1 
ATOM   3730 C CD1 . PHE A 1 468 ? 42.035 76.817  7.517   1.00 28.17 ? 468  PHE A CD1 1 
ATOM   3731 C CD2 . PHE A 1 468 ? 42.156 79.193  7.894   1.00 24.52 ? 468  PHE A CD2 1 
ATOM   3732 C CE1 . PHE A 1 468 ? 43.379 76.696  7.936   1.00 26.65 ? 468  PHE A CE1 1 
ATOM   3733 C CE2 . PHE A 1 468 ? 43.474 79.086  8.328   1.00 24.69 ? 468  PHE A CE2 1 
ATOM   3734 C CZ  . PHE A 1 468 ? 44.094 77.859  8.338   1.00 26.97 ? 468  PHE A CZ  1 
ATOM   3735 N N   . THR A 1 469 ? 39.840 77.928  10.412  1.00 26.74 ? 469  THR A N   1 
ATOM   3736 C CA  . THR A 1 469 ? 40.180 78.680  11.629  1.00 26.68 ? 469  THR A CA  1 
ATOM   3737 C C   . THR A 1 469 ? 41.689 78.605  11.710  1.00 27.87 ? 469  THR A C   1 
ATOM   3738 O O   . THR A 1 469 ? 42.237 77.514  11.681  1.00 27.34 ? 469  THR A O   1 
ATOM   3739 C CB  . THR A 1 469 ? 39.542 78.038  12.924  1.00 27.77 ? 469  THR A CB  1 
ATOM   3740 O OG1 . THR A 1 469 ? 38.158 77.798  12.691  1.00 29.14 ? 469  THR A OG1 1 
ATOM   3741 C CG2 . THR A 1 469 ? 39.663 78.933  14.162  1.00 24.70 ? 469  THR A CG2 1 
ATOM   3742 N N   . PRO A 1 470 ? 42.375 79.774  11.800  1.00 27.95 ? 470  PRO A N   1 
ATOM   3743 C CA  . PRO A 1 470 ? 43.794 79.745  12.012  1.00 28.85 ? 470  PRO A CA  1 
ATOM   3744 C C   . PRO A 1 470 ? 44.045 79.096  13.366  1.00 29.69 ? 470  PRO A C   1 
ATOM   3745 O O   . PRO A 1 470 ? 43.091 78.948  14.151  1.00 31.11 ? 470  PRO A O   1 
ATOM   3746 C CB  . PRO A 1 470 ? 44.166 81.216  12.099  1.00 28.44 ? 470  PRO A CB  1 
ATOM   3747 C CG  . PRO A 1 470 ? 43.045 81.915  11.384  1.00 29.68 ? 470  PRO A CG  1 
ATOM   3748 C CD  . PRO A 1 470 ? 41.852 81.144  11.731  1.00 27.33 ? 470  PRO A CD  1 
ATOM   3749 N N   . ARG A 1 471 ? 45.312 78.777  13.638  1.00 29.70 ? 471  ARG A N   1 
ATOM   3750 C CA  . ARG A 1 471 ? 45.701 78.032  14.799  1.00 30.98 ? 471  ARG A CA  1 
ATOM   3751 C C   . ARG A 1 471 ? 45.728 78.835  16.103  1.00 29.41 ? 471  ARG A C   1 
ATOM   3752 O O   . ARG A 1 471 ? 46.667 78.775  16.873  1.00 30.46 ? 471  ARG A O   1 
ATOM   3753 C CB  . ARG A 1 471 ? 47.020 77.294  14.527  1.00 31.61 ? 471  ARG A CB  1 
ATOM   3754 C CG  . ARG A 1 471 ? 48.262 78.137  14.332  1.00 35.20 ? 471  ARG A CG  1 
ATOM   3755 C CD  . ARG A 1 471 ? 49.464 77.230  14.421  1.00 43.45 ? 471  ARG A CD  1 
ATOM   3756 N NE  . ARG A 1 471 ? 49.342 76.215  13.368  1.00 46.90 ? 471  ARG A NE  1 
ATOM   3757 C CZ  . ARG A 1 471 ? 50.266 75.298  13.076  1.00 48.97 ? 471  ARG A CZ  1 
ATOM   3758 N NH1 . ARG A 1 471 ? 51.416 75.247  13.769  1.00 48.96 ? 471  ARG A NH1 1 
ATOM   3759 N NH2 . ARG A 1 471 ? 50.025 74.427  12.092  1.00 46.46 ? 471  ARG A NH2 1 
ATOM   3760 N N   . ILE A 1 472 ? 44.671 79.583  16.325  1.00 28.21 ? 472  ILE A N   1 
ATOM   3761 C CA  . ILE A 1 472 ? 44.520 80.405  17.521  1.00 27.61 ? 472  ILE A CA  1 
ATOM   3762 C C   . ILE A 1 472 ? 44.289 79.518  18.758  1.00 28.17 ? 472  ILE A C   1 
ATOM   3763 O O   . ILE A 1 472 ? 43.723 78.405  18.659  1.00 27.42 ? 472  ILE A O   1 
ATOM   3764 C CB  . ILE A 1 472 ? 43.309 81.353  17.381  1.00 27.84 ? 472  ILE A CB  1 
ATOM   3765 C CG1 . ILE A 1 472 ? 42.044 80.530  17.135  1.00 28.48 ? 472  ILE A CG1 1 
ATOM   3766 C CG2 . ILE A 1 472 ? 43.514 82.385  16.215  1.00 24.99 ? 472  ILE A CG2 1 
ATOM   3767 C CD1 . ILE A 1 472 ? 40.810 81.331  17.261  1.00 28.62 ? 472  ILE A CD1 1 
ATOM   3768 N N   . LEU A 1 473 ? 44.698 80.028  19.909  1.00 27.39 ? 473  LEU A N   1 
ATOM   3769 C CA  . LEU A 1 473 ? 44.542 79.323  21.172  1.00 28.29 ? 473  LEU A CA  1 
ATOM   3770 C C   . LEU A 1 473 ? 43.085 78.867  21.376  1.00 29.00 ? 473  LEU A C   1 
ATOM   3771 O O   . LEU A 1 473 ? 42.165 79.661  21.256  1.00 28.46 ? 473  LEU A O   1 
ATOM   3772 C CB  . LEU A 1 473 ? 44.959 80.249  22.305  1.00 27.36 ? 473  LEU A CB  1 
ATOM   3773 C CG  . LEU A 1 473 ? 44.916 79.613  23.691  1.00 27.23 ? 473  LEU A CG  1 
ATOM   3774 C CD1 . LEU A 1 473 ? 45.836 78.382  23.752  1.00 27.51 ? 473  LEU A CD1 1 
ATOM   3775 C CD2 . LEU A 1 473 ? 45.349 80.650  24.662  1.00 29.52 ? 473  LEU A CD2 1 
ATOM   3776 N N   . ASP A 1 474 ? 42.913 77.573  21.683  1.00 31.41 ? 474  ASP A N   1 
ATOM   3777 C CA  . ASP A 1 474 ? 41.592 76.927  21.901  1.00 31.87 ? 474  ASP A CA  1 
ATOM   3778 C C   . ASP A 1 474 ? 40.781 76.633  20.653  1.00 32.26 ? 474  ASP A C   1 
ATOM   3779 O O   . ASP A 1 474 ? 39.779 75.944  20.752  1.00 32.28 ? 474  ASP A O   1 
ATOM   3780 C CB  . ASP A 1 474 ? 40.734 77.687  22.914  1.00 32.84 ? 474  ASP A CB  1 
ATOM   3781 C CG  . ASP A 1 474 ? 41.406 77.777  24.308  1.00 38.25 ? 474  ASP A CG  1 
ATOM   3782 O OD1 . ASP A 1 474 ? 41.906 76.737  24.842  1.00 41.97 ? 474  ASP A OD1 1 
ATOM   3783 O OD2 . ASP A 1 474 ? 41.423 78.896  24.886  1.00 43.24 ? 474  ASP A OD2 1 
ATOM   3784 N N   . GLY A 1 475 ? 41.191 77.133  19.487  1.00 30.43 ? 475  GLY A N   1 
ATOM   3785 C CA  . GLY A 1 475 ? 40.613 76.662  18.247  1.00 30.07 ? 475  GLY A CA  1 
ATOM   3786 C C   . GLY A 1 475 ? 39.218 77.136  17.888  1.00 29.31 ? 475  GLY A C   1 
ATOM   3787 O O   . GLY A 1 475 ? 38.618 76.619  16.943  1.00 31.00 ? 475  GLY A O   1 
ATOM   3788 N N   . TYR A 1 476 ? 38.679 78.091  18.631  1.00 28.50 ? 476  TYR A N   1 
ATOM   3789 C CA  A TYR A 1 476 ? 37.452 78.721  18.199  0.50 27.47 ? 476  TYR A CA  1 
ATOM   3790 C CA  B TYR A 1 476 ? 37.367 78.713  18.353  0.50 28.15 ? 476  TYR A CA  1 
ATOM   3791 C C   . TYR A 1 476 ? 37.543 80.216  18.435  1.00 27.03 ? 476  TYR A C   1 
ATOM   3792 O O   . TYR A 1 476 ? 38.150 80.679  19.384  1.00 26.75 ? 476  TYR A O   1 
ATOM   3793 C CB  A TYR A 1 476 ? 36.185 78.062  18.791  0.50 27.66 ? 476  TYR A CB  1 
ATOM   3794 C CB  B TYR A 1 476 ? 36.310 78.347  19.417  0.50 29.11 ? 476  TYR A CB  1 
ATOM   3795 C CG  A TYR A 1 476 ? 36.153 77.886  20.298  0.50 26.30 ? 476  TYR A CG  1 
ATOM   3796 C CG  B TYR A 1 476 ? 35.733 76.960  19.335  0.50 29.71 ? 476  TYR A CG  1 
ATOM   3797 C CD1 A TYR A 1 476 ? 36.910 76.898  20.929  0.50 27.87 ? 476  TYR A CD1 1 
ATOM   3798 C CD1 B TYR A 1 476 ? 34.604 76.689  18.552  0.50 30.32 ? 476  TYR A CD1 1 
ATOM   3799 C CD2 A TYR A 1 476 ? 35.339 78.682  21.084  0.50 25.62 ? 476  TYR A CD2 1 
ATOM   3800 C CD2 B TYR A 1 476 ? 36.285 75.918  20.072  0.50 31.11 ? 476  TYR A CD2 1 
ATOM   3801 C CE1 A TYR A 1 476 ? 36.868 76.734  22.334  0.50 26.42 ? 476  TYR A CE1 1 
ATOM   3802 C CE1 B TYR A 1 476 ? 34.068 75.402  18.494  0.50 30.57 ? 476  TYR A CE1 1 
ATOM   3803 C CE2 A TYR A 1 476 ? 35.269 78.522  22.475  0.50 24.42 ? 476  TYR A CE2 1 
ATOM   3804 C CE2 B TYR A 1 476 ? 35.749 74.632  20.013  0.50 30.77 ? 476  TYR A CE2 1 
ATOM   3805 C CZ  A TYR A 1 476 ? 36.036 77.556  23.094  0.50 26.35 ? 476  TYR A CZ  1 
ATOM   3806 C CZ  B TYR A 1 476 ? 34.664 74.392  19.231  0.50 29.61 ? 476  TYR A CZ  1 
ATOM   3807 O OH  A TYR A 1 476 ? 35.964 77.424  24.463  0.50 25.56 ? 476  TYR A OH  1 
ATOM   3808 O OH  B TYR A 1 476 ? 34.171 73.124  19.210  0.50 31.81 ? 476  TYR A OH  1 
ATOM   3809 N N   . LEU A 1 477 ? 36.960 80.960  17.503  1.00 26.41 ? 477  LEU A N   1 
ATOM   3810 C CA  . LEU A 1 477 ? 37.115 82.424  17.444  1.00 25.95 ? 477  LEU A CA  1 
ATOM   3811 C C   . LEU A 1 477 ? 36.525 83.131  18.644  1.00 26.72 ? 477  LEU A C   1 
ATOM   3812 O O   . LEU A 1 477 ? 37.162 84.029  19.206  1.00 25.64 ? 477  LEU A O   1 
ATOM   3813 C CB  . LEU A 1 477 ? 36.568 83.022  16.134  1.00 25.12 ? 477  LEU A CB  1 
ATOM   3814 C CG  . LEU A 1 477 ? 37.298 82.615  14.834  1.00 26.14 ? 477  LEU A CG  1 
ATOM   3815 C CD1 . LEU A 1 477 ? 36.483 83.248  13.716  1.00 22.80 ? 477  LEU A CD1 1 
ATOM   3816 C CD2 . LEU A 1 477 ? 38.784 83.166  14.824  1.00 23.91 ? 477  LEU A CD2 1 
ATOM   3817 N N   . PHE A 1 478 ? 35.364 82.675  19.104  1.00 26.04 ? 478  PHE A N   1 
ATOM   3818 C CA  . PHE A 1 478 ? 34.689 83.358  20.202  1.00 25.48 ? 478  PHE A CA  1 
ATOM   3819 C C   . PHE A 1 478 ? 35.159 82.940  21.592  1.00 26.24 ? 478  PHE A C   1 
ATOM   3820 O O   . PHE A 1 478 ? 34.597 83.387  22.595  1.00 25.92 ? 478  PHE A O   1 
ATOM   3821 C CB  . PHE A 1 478 ? 33.200 83.125  20.066  1.00 27.09 ? 478  PHE A CB  1 
ATOM   3822 C CG  . PHE A 1 478 ? 32.826 81.666  20.010  1.00 27.15 ? 478  PHE A CG  1 
ATOM   3823 C CD1 . PHE A 1 478 ? 32.533 80.972  21.170  1.00 29.06 ? 478  PHE A CD1 1 
ATOM   3824 C CD2 . PHE A 1 478 ? 32.770 80.992  18.782  1.00 29.77 ? 478  PHE A CD2 1 
ATOM   3825 C CE1 . PHE A 1 478 ? 32.176 79.613  21.122  1.00 28.10 ? 478  PHE A CE1 1 
ATOM   3826 C CE2 . PHE A 1 478 ? 32.409 79.624  18.718  1.00 29.46 ? 478  PHE A CE2 1 
ATOM   3827 C CZ  . PHE A 1 478 ? 32.138 78.938  19.890  1.00 27.50 ? 478  PHE A CZ  1 
ATOM   3828 N N   . CYS A 1 479 ? 36.195 82.111  21.678  1.00 26.67 ? 479  CYS A N   1 
ATOM   3829 C CA  A CYS A 1 479 ? 36.759 81.675  22.966  0.50 26.92 ? 479  CYS A CA  1 
ATOM   3830 C CA  B CYS A 1 479 ? 36.698 81.711  22.985  0.50 28.11 ? 479  CYS A CA  1 
ATOM   3831 C C   . CYS A 1 479 ? 37.258 82.864  23.808  1.00 27.74 ? 479  CYS A C   1 
ATOM   3832 O O   . CYS A 1 479 ? 38.180 83.573  23.379  1.00 27.27 ? 479  CYS A O   1 
ATOM   3833 C CB  A CYS A 1 479 ? 37.914 80.685  22.736  0.50 26.81 ? 479  CYS A CB  1 
ATOM   3834 C CB  B CYS A 1 479 ? 37.690 80.567  22.847  0.50 28.45 ? 479  CYS A CB  1 
ATOM   3835 S SG  A CYS A 1 479 ? 38.621 80.027  24.252  0.50 27.43 ? 479  CYS A SG  1 
ATOM   3836 S SG  B CYS A 1 479 ? 36.741 79.105  22.465  0.50 35.60 ? 479  CYS A SG  1 
ATOM   3837 N N   . LYS A 1 480 ? 36.653 83.072  24.987  1.00 27.03 ? 480  LYS A N   1 
ATOM   3838 C CA  . LYS A 1 480 ? 36.999 84.177  25.901  1.00 27.92 ? 480  LYS A CA  1 
ATOM   3839 C C   . LYS A 1 480 ? 36.908 85.589  25.269  1.00 27.44 ? 480  LYS A C   1 
ATOM   3840 O O   . LYS A 1 480 ? 37.631 86.526  25.674  1.00 25.77 ? 480  LYS A O   1 
ATOM   3841 C CB  . LYS A 1 480 ? 38.339 83.932  26.593  1.00 29.18 ? 480  LYS A CB  1 
ATOM   3842 C CG  . LYS A 1 480 ? 38.478 82.578  27.377  1.00 31.23 ? 480  LYS A CG  1 
ATOM   3843 C CD  . LYS A 1 480 ? 37.423 82.444  28.504  1.00 35.92 ? 480  LYS A CD  1 
ATOM   3844 C CE  . LYS A 1 480 ? 37.539 81.095  29.263  1.00 39.05 ? 480  LYS A CE  1 
ATOM   3845 N NZ  . LYS A 1 480 ? 36.181 80.347  29.290  1.00 43.38 ? 480  LYS A NZ  1 
ATOM   3846 N N   . THR A 1 481 ? 35.978 85.744  24.331  1.00 26.68 ? 481  THR A N   1 
ATOM   3847 C CA  . THR A 1 481 ? 35.691 87.036  23.716  1.00 27.79 ? 481  THR A CA  1 
ATOM   3848 C C   . THR A 1 481 ? 34.221 87.121  23.262  1.00 28.35 ? 481  THR A C   1 
ATOM   3849 O O   . THR A 1 481 ? 33.393 86.329  23.704  1.00 28.31 ? 481  THR A O   1 
ATOM   3850 C CB  . THR A 1 481 ? 36.695 87.376  22.532  1.00 27.34 ? 481  THR A CB  1 
ATOM   3851 O OG1 . THR A 1 481 ? 36.554 88.761  22.174  1.00 30.22 ? 481  THR A OG1 1 
ATOM   3852 C CG2 . THR A 1 481 ? 36.456 86.527  21.304  1.00 28.54 ? 481  THR A CG2 1 
ATOM   3853 N N   . LEU A 1 482 ? 33.903 88.065  22.380  1.00 28.76 ? 482  LEU A N   1 
ATOM   3854 C CA  . LEU A 1 482 ? 32.542 88.253  21.917  1.00 29.07 ? 482  LEU A CA  1 
ATOM   3855 C C   . LEU A 1 482 ? 32.145 87.328  20.781  1.00 30.22 ? 482  LEU A C   1 
ATOM   3856 O O   . LEU A 1 482 ? 33.007 86.829  20.029  1.00 29.75 ? 482  LEU A O   1 
ATOM   3857 C CB  . LEU A 1 482 ? 32.316 89.730  21.548  1.00 28.99 ? 482  LEU A CB  1 
ATOM   3858 C CG  . LEU A 1 482 ? 32.708 90.768  22.632  1.00 29.82 ? 482  LEU A CG  1 
ATOM   3859 C CD1 . LEU A 1 482 ? 32.194 92.153  22.240  1.00 31.85 ? 482  LEU A CD1 1 
ATOM   3860 C CD2 . LEU A 1 482 ? 32.244 90.412  24.073  1.00 28.75 ? 482  LEU A CD2 1 
ATOM   3861 N N   . CYS A 1 483 ? 30.835 87.083  20.646  1.00 29.95 ? 483  CYS A N   1 
ATOM   3862 C CA  . CYS A 1 483 ? 30.319 86.371  19.474  1.00 31.13 ? 483  CYS A CA  1 
ATOM   3863 C C   . CYS A 1 483 ? 30.833 87.071  18.210  1.00 29.15 ? 483  CYS A C   1 
ATOM   3864 O O   . CYS A 1 483 ? 30.891 88.286  18.149  1.00 27.74 ? 483  CYS A O   1 
ATOM   3865 C CB  . CYS A 1 483 ? 28.779 86.378  19.452  1.00 31.53 ? 483  CYS A CB  1 
ATOM   3866 S SG  . CYS A 1 483 ? 28.045 85.534  20.893  1.00 41.82 ? 483  CYS A SG  1 
ATOM   3867 N N   . MET A 1 484 ? 31.188 86.291  17.208  1.00 29.65 ? 484  MET A N   1 
ATOM   3868 C CA  . MET A 1 484 ? 31.711 86.834  15.956  1.00 28.86 ? 484  MET A CA  1 
ATOM   3869 C C   . MET A 1 484 ? 30.614 87.544  15.161  1.00 29.86 ? 484  MET A C   1 
ATOM   3870 O O   . MET A 1 484 ? 30.894 88.323  14.252  1.00 29.36 ? 484  MET A O   1 
ATOM   3871 C CB  . MET A 1 484 ? 32.326 85.732  15.130  1.00 27.93 ? 484  MET A CB  1 
ATOM   3872 C CG  . MET A 1 484 ? 33.626 85.219  15.687  1.00 28.07 ? 484  MET A CG  1 
ATOM   3873 S SD  . MET A 1 484 ? 34.866 86.564  15.792  1.00 30.56 ? 484  MET A SD  1 
ATOM   3874 C CE  . MET A 1 484 ? 35.025 86.755  17.572  1.00 29.49 ? 484  MET A CE  1 
ATOM   3875 N N   . ASP A 1 485 ? 29.357 87.265  15.497  1.00 29.98 ? 485  ASP A N   1 
ATOM   3876 C CA  . ASP A 1 485 ? 28.233 87.909  14.821  1.00 30.11 ? 485  ASP A CA  1 
ATOM   3877 C C   . ASP A 1 485 ? 27.674 89.068  15.614  1.00 29.59 ? 485  ASP A C   1 
ATOM   3878 O O   . ASP A 1 485 ? 26.738 89.719  15.176  1.00 30.77 ? 485  ASP A O   1 
ATOM   3879 C CB  . ASP A 1 485 ? 27.149 86.909  14.402  1.00 31.29 ? 485  ASP A CB  1 
ATOM   3880 C CG  . ASP A 1 485 ? 26.681 86.022  15.551  1.00 35.54 ? 485  ASP A CG  1 
ATOM   3881 O OD1 . ASP A 1 485 ? 27.028 86.275  16.746  1.00 39.74 ? 485  ASP A OD1 1 
ATOM   3882 O OD2 . ASP A 1 485 ? 25.931 85.068  15.252  1.00 40.02 ? 485  ASP A OD2 1 
ATOM   3883 N N   . ALA A 1 486 ? 28.302 89.388  16.737  1.00 28.50 ? 486  ALA A N   1 
ATOM   3884 C CA  . ALA A 1 486 ? 28.035 90.641  17.436  1.00 28.94 ? 486  ALA A CA  1 
ATOM   3885 C C   . ALA A 1 486 ? 28.262 91.839  16.509  1.00 29.78 ? 486  ALA A C   1 
ATOM   3886 O O   . ALA A 1 486 ? 29.058 91.764  15.551  1.00 28.69 ? 486  ALA A O   1 
ATOM   3887 C CB  . ALA A 1 486 ? 28.885 90.757  18.692  1.00 27.66 ? 486  ALA A CB  1 
ATOM   3888 N N   . VAL A 1 487 ? 27.550 92.929  16.785  1.00 29.61 ? 487  VAL A N   1 
ATOM   3889 C CA  . VAL A 1 487 ? 27.451 94.028  15.836  1.00 31.16 ? 487  VAL A CA  1 
ATOM   3890 C C   . VAL A 1 487 ? 27.858 95.334  16.458  1.00 30.08 ? 487  VAL A C   1 
ATOM   3891 O O   . VAL A 1 487 ? 27.378 95.696  17.534  1.00 30.63 ? 487  VAL A O   1 
ATOM   3892 C CB  . VAL A 1 487 ? 26.005 94.220  15.257  1.00 31.99 ? 487  VAL A CB  1 
ATOM   3893 C CG1 . VAL A 1 487 ? 26.062 95.205  14.152  1.00 36.65 ? 487  VAL A CG1 1 
ATOM   3894 C CG2 . VAL A 1 487 ? 25.446 92.939  14.683  1.00 33.16 ? 487  VAL A CG2 1 
ATOM   3895 N N   . GLN A 1 488 ? 28.711 96.061  15.740  1.00 29.04 ? 488  GLN A N   1 
ATOM   3896 C CA  . GLN A 1 488 ? 29.183 97.364  16.146  1.00 29.08 ? 488  GLN A CA  1 
ATOM   3897 C C   . GLN A 1 488 ? 29.005 98.330  14.981  1.00 28.93 ? 488  GLN A C   1 
ATOM   3898 O O   . GLN A 1 488 ? 28.766 97.919  13.849  1.00 29.40 ? 488  GLN A O   1 
ATOM   3899 C CB  . GLN A 1 488 ? 30.653 97.287  16.564  1.00 27.82 ? 488  GLN A CB  1 
ATOM   3900 C CG  . GLN A 1 488 ? 30.873 96.618  17.933  1.00 29.53 ? 488  GLN A CG  1 
ATOM   3901 C CD  . GLN A 1 488 ? 32.346 96.581  18.364  1.00 30.57 ? 488  GLN A CD  1 
ATOM   3902 O OE1 . GLN A 1 488 ? 32.922 97.578  18.822  1.00 33.35 ? 488  GLN A OE1 1 
ATOM   3903 N NE2 . GLN A 1 488 ? 32.941 95.421  18.236  1.00 30.31 ? 488  GLN A NE2 1 
ATOM   3904 N N   . HIS A 1 489 ? 29.156 99.604  15.252  1.00 29.31 ? 489  HIS A N   1 
ATOM   3905 C CA  . HIS A 1 489 ? 29.068 100.598 14.191  1.00 31.30 ? 489  HIS A CA  1 
ATOM   3906 C C   . HIS A 1 489 ? 29.976 100.332 12.944  1.00 32.03 ? 489  HIS A C   1 
ATOM   3907 O O   . HIS A 1 489 ? 29.518 100.468 11.792  1.00 31.56 ? 489  HIS A O   1 
ATOM   3908 C CB  . HIS A 1 489 ? 29.307 101.959 14.763  1.00 31.70 ? 489  HIS A CB  1 
ATOM   3909 C CG  . HIS A 1 489 ? 29.172 103.043 13.750  1.00 36.70 ? 489  HIS A CG  1 
ATOM   3910 N ND1 . HIS A 1 489 ? 30.192 103.924 13.464  1.00 41.38 ? 489  HIS A ND1 1 
ATOM   3911 C CD2 . HIS A 1 489 ? 28.156 103.348 12.906  1.00 38.94 ? 489  HIS A CD2 1 
ATOM   3912 C CE1 . HIS A 1 489 ? 29.801 104.753 12.508  1.00 41.67 ? 489  HIS A CE1 1 
ATOM   3913 N NE2 . HIS A 1 489 ? 28.572 104.420 12.150  1.00 43.44 ? 489  HIS A NE2 1 
ATOM   3914 N N   . TRP A 1 490 ? 31.217 99.885  13.162  1.00 32.19 ? 490  TRP A N   1 
ATOM   3915 C CA  . TRP A 1 490 ? 32.142 99.534  12.030  1.00 31.68 ? 490  TRP A CA  1 
ATOM   3916 C C   . TRP A 1 490 ? 31.886 98.209  11.371  1.00 31.38 ? 490  TRP A C   1 
ATOM   3917 O O   . TRP A 1 490 ? 32.407 97.943  10.303  1.00 31.66 ? 490  TRP A O   1 
ATOM   3918 C CB  . TRP A 1 490 ? 33.609 99.519  12.456  1.00 31.76 ? 490  TRP A CB  1 
ATOM   3919 C CG  . TRP A 1 490 ? 34.225 100.835 12.642  1.00 30.92 ? 490  TRP A CG  1 
ATOM   3920 C CD1 . TRP A 1 490 ? 33.686 102.025 12.339  1.00 30.90 ? 490  TRP A CD1 1 
ATOM   3921 C CD2 . TRP A 1 490 ? 35.521 101.102 13.223  1.00 32.10 ? 490  TRP A CD2 1 
ATOM   3922 N NE1 . TRP A 1 490 ? 34.538 103.038 12.708  1.00 31.95 ? 490  TRP A NE1 1 
ATOM   3923 C CE2 . TRP A 1 490 ? 35.686 102.500 13.231  1.00 32.56 ? 490  TRP A CE2 1 
ATOM   3924 C CE3 . TRP A 1 490 ? 36.562 100.289 13.709  1.00 32.20 ? 490  TRP A CE3 1 
ATOM   3925 C CZ2 . TRP A 1 490 ? 36.857 103.128 13.715  1.00 33.58 ? 490  TRP A CZ2 1 
ATOM   3926 C CZ3 . TRP A 1 490 ? 37.725 100.900 14.211  1.00 31.08 ? 490  TRP A CZ3 1 
ATOM   3927 C CH2 . TRP A 1 490 ? 37.858 102.315 14.209  1.00 32.82 ? 490  TRP A CH2 1 
ATOM   3928 N N   . GLY A 1 491 ? 31.153 97.324  12.032  1.00 30.63 ? 491  GLY A N   1 
ATOM   3929 C CA  . GLY A 1 491 ? 30.739 96.087  11.406  1.00 29.86 ? 491  GLY A CA  1 
ATOM   3930 C C   . GLY A 1 491 ? 30.652 94.927  12.391  1.00 30.24 ? 491  GLY A C   1 
ATOM   3931 O O   . GLY A 1 491 ? 30.607 95.115  13.622  1.00 30.68 ? 491  GLY A O   1 
ATOM   3932 N N   . LYS A 1 492 ? 30.679 93.726  11.854  1.00 30.41 ? 492  LYS A N   1 
ATOM   3933 C CA  . LYS A 1 492 ? 30.524 92.554  12.683  1.00 32.16 ? 492  LYS A CA  1 
ATOM   3934 C C   . LYS A 1 492 ? 31.836 92.252  13.363  1.00 31.24 ? 492  LYS A C   1 
ATOM   3935 O O   . LYS A 1 492 ? 32.928 92.546  12.820  1.00 28.78 ? 492  LYS A O   1 
ATOM   3936 C CB  . LYS A 1 492 ? 30.002 91.372  11.861  1.00 33.36 ? 492  LYS A CB  1 
ATOM   3937 C CG  . LYS A 1 492 ? 28.520 91.605  11.516  1.00 36.80 ? 492  LYS A CG  1 
ATOM   3938 C CD  . LYS A 1 492 ? 27.774 90.412  10.910  1.00 36.99 ? 492  LYS A CD  1 
ATOM   3939 C CE  . LYS A 1 492 ? 26.197 90.575  11.047  1.00 40.59 ? 492  LYS A CE  1 
ATOM   3940 N NZ  . LYS A 1 492 ? 25.668 89.990  12.383  1.00 44.10 ? 492  LYS A NZ  1 
ATOM   3941 N N   . GLN A 1 493 ? 31.724 91.677  14.559  1.00 28.25 ? 493  GLN A N   1 
ATOM   3942 C CA  . GLN A 1 493 ? 32.866 91.279  15.337  1.00 27.52 ? 493  GLN A CA  1 
ATOM   3943 C C   . GLN A 1 493 ? 33.880 90.475  14.527  1.00 26.66 ? 493  GLN A C   1 
ATOM   3944 O O   . GLN A 1 493 ? 35.089 90.636  14.706  1.00 25.49 ? 493  GLN A O   1 
ATOM   3945 C CB  . GLN A 1 493 ? 32.377 90.475  16.538  1.00 28.21 ? 493  GLN A CB  1 
ATOM   3946 C CG  . GLN A 1 493 ? 33.422 90.080  17.492  1.00 30.63 ? 493  GLN A CG  1 
ATOM   3947 C CD  . GLN A 1 493 ? 33.964 91.268  18.263  1.00 34.78 ? 493  GLN A CD  1 
ATOM   3948 O OE1 . GLN A 1 493 ? 33.398 92.367  18.241  1.00 36.76 ? 493  GLN A OE1 1 
ATOM   3949 N NE2 . GLN A 1 493 ? 35.070 91.045  18.950  1.00 32.53 ? 493  GLN A NE2 1 
ATOM   3950 N N   . TYR A 1 494 ? 33.406 89.587  13.666  1.00 24.38 ? 494  TYR A N   1 
ATOM   3951 C CA  . TYR A 1 494 ? 34.283 88.768  12.845  1.00 24.87 ? 494  TYR A CA  1 
ATOM   3952 C C   . TYR A 1 494 ? 35.316 89.628  12.089  1.00 25.71 ? 494  TYR A C   1 
ATOM   3953 O O   . TYR A 1 494 ? 36.442 89.196  11.878  1.00 24.38 ? 494  TYR A O   1 
ATOM   3954 C CB  . TYR A 1 494 ? 33.422 88.021  11.835  1.00 23.91 ? 494  TYR A CB  1 
ATOM   3955 C CG  . TYR A 1 494 ? 34.125 87.056  10.914  1.00 24.00 ? 494  TYR A CG  1 
ATOM   3956 C CD1 . TYR A 1 494 ? 34.298 85.723  11.283  1.00 23.87 ? 494  TYR A CD1 1 
ATOM   3957 C CD2 . TYR A 1 494 ? 34.564 87.463  9.643   1.00 22.65 ? 494  TYR A CD2 1 
ATOM   3958 C CE1 . TYR A 1 494 ? 34.902 84.821  10.457  1.00 25.11 ? 494  TYR A CE1 1 
ATOM   3959 C CE2 . TYR A 1 494 ? 35.179 86.532  8.789   1.00 23.01 ? 494  TYR A CE2 1 
ATOM   3960 C CZ  . TYR A 1 494 ? 35.349 85.231  9.212   1.00 24.02 ? 494  TYR A CZ  1 
ATOM   3961 O OH  . TYR A 1 494 ? 35.940 84.294  8.402   1.00 23.92 ? 494  TYR A OH  1 
ATOM   3962 N N   . ASP A 1 495 ? 34.892 90.798  11.630  1.00 26.49 ? 495  ASP A N   1 
ATOM   3963 C CA  . ASP A 1 495 ? 35.800 91.688  10.863  1.00 28.56 ? 495  ASP A CA  1 
ATOM   3964 C C   . ASP A 1 495 ? 36.550 92.650  11.769  1.00 28.29 ? 495  ASP A C   1 
ATOM   3965 O O   . ASP A 1 495 ? 37.651 93.052  11.452  1.00 28.21 ? 495  ASP A O   1 
ATOM   3966 C CB  . ASP A 1 495 ? 35.016 92.520  9.858   1.00 29.04 ? 495  ASP A CB  1 
ATOM   3967 C CG  . ASP A 1 495 ? 34.431 91.685  8.731   1.00 31.42 ? 495  ASP A CG  1 
ATOM   3968 O OD1 . ASP A 1 495 ? 35.154 90.802  8.181   1.00 34.15 ? 495  ASP A OD1 1 
ATOM   3969 O OD2 . ASP A 1 495 ? 33.260 91.963  8.361   1.00 32.62 ? 495  ASP A OD2 1 
ATOM   3970 N N   . ILE A 1 496 ? 35.937 93.065  12.876  1.00 27.79 ? 496  ILE A N   1 
ATOM   3971 C CA  . ILE A 1 496 ? 36.529 94.144  13.658  1.00 28.23 ? 496  ILE A CA  1 
ATOM   3972 C C   . ILE A 1 496 ? 37.084 93.757  15.045  1.00 27.08 ? 496  ILE A C   1 
ATOM   3973 O O   . ILE A 1 496 ? 37.555 94.614  15.807  1.00 26.81 ? 496  ILE A O   1 
ATOM   3974 C CB  . ILE A 1 496 ? 35.556 95.337  13.805  1.00 28.87 ? 496  ILE A CB  1 
ATOM   3975 C CG1 . ILE A 1 496 ? 34.354 94.952  14.652  1.00 30.56 ? 496  ILE A CG1 1 
ATOM   3976 C CG2 . ILE A 1 496 ? 35.139 95.910  12.422  1.00 28.09 ? 496  ILE A CG2 1 
ATOM   3977 C CD1 . ILE A 1 496 ? 33.577 96.121  15.049  1.00 35.10 ? 496  ILE A CD1 1 
ATOM   3978 N N   . HIS A 1 497 ? 37.034 92.465  15.373  1.00 25.82 ? 497  HIS A N   1 
ATOM   3979 C CA  . HIS A 1 497 ? 37.561 91.991  16.667  1.00 25.07 ? 497  HIS A CA  1 
ATOM   3980 C C   . HIS A 1 497 ? 38.962 92.601  16.992  1.00 23.32 ? 497  HIS A C   1 
ATOM   3981 O O   . HIS A 1 497 ? 39.243 93.088  18.105  1.00 23.36 ? 497  HIS A O   1 
ATOM   3982 C CB  . HIS A 1 497 ? 37.719 90.481  16.590  1.00 23.63 ? 497  HIS A CB  1 
ATOM   3983 C CG  . HIS A 1 497 ? 38.272 89.891  17.832  1.00 24.10 ? 497  HIS A CG  1 
ATOM   3984 N ND1 . HIS A 1 497 ? 39.590 89.505  17.952  1.00 26.55 ? 497  HIS A ND1 1 
ATOM   3985 C CD2 . HIS A 1 497 ? 37.696 89.652  19.032  1.00 23.71 ? 497  HIS A CD2 1 
ATOM   3986 C CE1 . HIS A 1 497 ? 39.796 89.032  19.170  1.00 21.03 ? 497  HIS A CE1 1 
ATOM   3987 N NE2 . HIS A 1 497 ? 38.661 89.106  19.838  1.00 26.72 ? 497  HIS A NE2 1 
ATOM   3988 N N   . ASN A 1 498 ? 39.849 92.530  16.016  1.00 24.01 ? 498  ASN A N   1 
ATOM   3989 C CA  . ASN A 1 498 ? 41.272 92.977  16.224  1.00 23.87 ? 498  ASN A CA  1 
ATOM   3990 C C   . ASN A 1 498 ? 41.427 94.473  16.400  1.00 23.62 ? 498  ASN A C   1 
ATOM   3991 O O   . ASN A 1 498 ? 42.528 94.993  16.671  1.00 25.66 ? 498  ASN A O   1 
ATOM   3992 C CB  . ASN A 1 498 ? 42.186 92.447  15.103  1.00 23.18 ? 498  ASN A CB  1 
ATOM   3993 C CG  . ASN A 1 498 ? 42.555 90.977  15.263  1.00 24.60 ? 498  ASN A CG  1 
ATOM   3994 O OD1 . ASN A 1 498 ? 43.032 90.333  14.317  1.00 28.85 ? 498  ASN A OD1 1 
ATOM   3995 N ND2 . ASN A 1 498 ? 42.345 90.432  16.435  1.00 21.78 ? 498  ASN A ND2 1 
ATOM   3996 N N   . LEU A 1 499 ? 40.328 95.185  16.229  1.00 23.23 ? 499  LEU A N   1 
ATOM   3997 C CA  . LEU A 1 499 ? 40.263 96.634  16.255  1.00 22.49 ? 499  LEU A CA  1 
ATOM   3998 C C   . LEU A 1 499 ? 39.604 97.167  17.514  1.00 23.04 ? 499  LEU A C   1 
ATOM   3999 O O   . LEU A 1 499 ? 39.467 98.377  17.652  1.00 23.08 ? 499  LEU A O   1 
ATOM   4000 C CB  . LEU A 1 499 ? 39.445 97.128  15.049  1.00 22.53 ? 499  LEU A CB  1 
ATOM   4001 C CG  . LEU A 1 499 ? 39.960 96.801  13.637  1.00 21.56 ? 499  LEU A CG  1 
ATOM   4002 C CD1 . LEU A 1 499 ? 39.061 97.502  12.636  1.00 21.69 ? 499  LEU A CD1 1 
ATOM   4003 C CD2 . LEU A 1 499 ? 41.352 97.332  13.491  1.00 24.06 ? 499  LEU A CD2 1 
ATOM   4004 N N   . TYR A 1 500 ? 39.173 96.283  18.432  1.00 22.50 ? 500  TYR A N   1 
ATOM   4005 C CA  . TYR A 1 500 ? 38.423 96.744  19.603  1.00 21.70 ? 500  TYR A CA  1 
ATOM   4006 C C   . TYR A 1 500 ? 39.329 97.599  20.483  1.00 21.63 ? 500  TYR A C   1 
ATOM   4007 O O   . TYR A 1 500 ? 38.943 98.698  20.855  1.00 22.56 ? 500  TYR A O   1 
ATOM   4008 C CB  . TYR A 1 500 ? 37.836 95.553  20.436  1.00 22.50 ? 500  TYR A CB  1 
ATOM   4009 C CG  . TYR A 1 500 ? 36.879 96.021  21.508  1.00 23.90 ? 500  TYR A CG  1 
ATOM   4010 C CD1 . TYR A 1 500 ? 35.512 95.978  21.305  1.00 25.93 ? 500  TYR A CD1 1 
ATOM   4011 C CD2 . TYR A 1 500 ? 37.348 96.583  22.690  1.00 24.33 ? 500  TYR A CD2 1 
ATOM   4012 C CE1 . TYR A 1 500 ? 34.616 96.447  22.307  1.00 24.70 ? 500  TYR A CE1 1 
ATOM   4013 C CE2 . TYR A 1 500 ? 36.493 97.062  23.655  1.00 22.74 ? 500  TYR A CE2 1 
ATOM   4014 C CZ  . TYR A 1 500 ? 35.127 96.964  23.457  1.00 23.61 ? 500  TYR A CZ  1 
ATOM   4015 O OH  . TYR A 1 500 ? 34.312 97.453  24.423  1.00 24.18 ? 500  TYR A OH  1 
ATOM   4016 N N   . GLY A 1 501 ? 40.507 97.092  20.854  1.00 19.19 ? 501  GLY A N   1 
ATOM   4017 C CA  . GLY A 1 501 ? 41.421 97.842  21.733  1.00 20.91 ? 501  GLY A CA  1 
ATOM   4018 C C   . GLY A 1 501 ? 41.947 99.121  21.065  1.00 22.17 ? 501  GLY A C   1 
ATOM   4019 O O   . GLY A 1 501 ? 42.122 100.164 21.731  1.00 23.32 ? 501  GLY A O   1 
ATOM   4020 N N   . TYR A 1 502 ? 42.185 99.037  19.751  1.00 21.31 ? 502  TYR A N   1 
ATOM   4021 C CA  . TYR A 1 502 ? 42.582 100.176 18.944  1.00 21.84 ? 502  TYR A CA  1 
ATOM   4022 C C   . TYR A 1 502 ? 41.509 101.301 19.066  1.00 22.32 ? 502  TYR A C   1 
ATOM   4023 O O   . TYR A 1 502 ? 41.818 102.441 19.372  1.00 21.98 ? 502  TYR A O   1 
ATOM   4024 C CB  . TYR A 1 502 ? 42.711 99.707  17.495  1.00 21.30 ? 502  TYR A CB  1 
ATOM   4025 C CG  . TYR A 1 502 ? 42.942 100.817 16.486  1.00 22.72 ? 502  TYR A CG  1 
ATOM   4026 C CD1 . TYR A 1 502 ? 44.174 101.495 16.420  1.00 25.16 ? 502  TYR A CD1 1 
ATOM   4027 C CD2 . TYR A 1 502 ? 41.966 101.156 15.563  1.00 22.96 ? 502  TYR A CD2 1 
ATOM   4028 C CE1 . TYR A 1 502 ? 44.405 102.501 15.457  1.00 23.69 ? 502  TYR A CE1 1 
ATOM   4029 C CE2 . TYR A 1 502 ? 42.173 102.172 14.606  1.00 26.38 ? 502  TYR A CE2 1 
ATOM   4030 C CZ  . TYR A 1 502 ? 43.404 102.825 14.559  1.00 26.94 ? 502  TYR A CZ  1 
ATOM   4031 O OH  . TYR A 1 502 ? 43.612 103.808 13.622  1.00 26.30 ? 502  TYR A OH  1 
ATOM   4032 N N   . SER A 1 503 ? 40.241 100.952 18.850  1.00 22.88 ? 503  SER A N   1 
ATOM   4033 C CA  . SER A 1 503 ? 39.136 101.952 18.927  1.00 25.10 ? 503  SER A CA  1 
ATOM   4034 C C   . SER A 1 503 ? 38.969 102.438 20.349  1.00 24.01 ? 503  SER A C   1 
ATOM   4035 O O   . SER A 1 503 ? 38.694 103.610 20.580  1.00 23.27 ? 503  SER A O   1 
ATOM   4036 C CB  . SER A 1 503 ? 37.818 101.364 18.387  1.00 25.18 ? 503  SER A CB  1 
ATOM   4037 O OG  . SER A 1 503 ? 37.289 100.306 19.234  1.00 29.74 ? 503  SER A OG  1 
ATOM   4038 N N   . MET A 1 504 ? 39.168 101.547 21.327  1.00 24.00 ? 504  MET A N   1 
ATOM   4039 C CA  . MET A 1 504 ? 39.154 101.989 22.708  1.00 24.17 ? 504  MET A CA  1 
ATOM   4040 C C   . MET A 1 504 ? 40.257 103.011 23.004  1.00 24.16 ? 504  MET A C   1 
ATOM   4041 O O   . MET A 1 504 ? 40.026 103.989 23.740  1.00 23.78 ? 504  MET A O   1 
ATOM   4042 C CB  . MET A 1 504 ? 39.234 100.813 23.664  1.00 23.94 ? 504  MET A CB  1 
ATOM   4043 C CG  . MET A 1 504 ? 38.838 101.207 25.041  1.00 24.57 ? 504  MET A CG  1 
ATOM   4044 S SD  . MET A 1 504 ? 39.036 99.818  26.143  1.00 26.18 ? 504  MET A SD  1 
ATOM   4045 C CE  . MET A 1 504 ? 38.569 100.627 27.704  1.00 25.48 ? 504  MET A CE  1 
ATOM   4046 N N   . ALA A 1 505 ? 41.449 102.799 22.453  1.00 23.45 ? 505  ALA A N   1 
ATOM   4047 C CA  . ALA A 1 505 ? 42.538 103.798 22.648  1.00 23.82 ? 505  ALA A CA  1 
ATOM   4048 C C   . ALA A 1 505 ? 42.220 105.145 21.979  1.00 22.33 ? 505  ALA A C   1 
ATOM   4049 O O   . ALA A 1 505 ? 42.447 106.169 22.569  1.00 22.51 ? 505  ALA A O   1 
ATOM   4050 C CB  . ALA A 1 505 ? 43.884 103.263 22.157  1.00 23.14 ? 505  ALA A CB  1 
ATOM   4051 N N   . VAL A 1 506 ? 41.713 105.116 20.756  1.00 23.00 ? 506  VAL A N   1 
ATOM   4052 C CA  . VAL A 1 506 ? 41.282 106.335 20.053  1.00 24.01 ? 506  VAL A CA  1 
ATOM   4053 C C   . VAL A 1 506 ? 40.243 107.106 20.893  1.00 24.72 ? 506  VAL A C   1 
ATOM   4054 O O   . VAL A 1 506 ? 40.413 108.303 21.146  1.00 26.32 ? 506  VAL A O   1 
ATOM   4055 C CB  . VAL A 1 506 ? 40.707 106.020 18.649  1.00 24.58 ? 506  VAL A CB  1 
ATOM   4056 C CG1 . VAL A 1 506 ? 40.172 107.329 17.944  1.00 23.60 ? 506  VAL A CG1 1 
ATOM   4057 C CG2 . VAL A 1 506 ? 41.733 105.292 17.778  1.00 25.64 ? 506  VAL A CG2 1 
ATOM   4058 N N   . ALA A 1 507 ? 39.192 106.412 21.356  1.00 25.79 ? 507  ALA A N   1 
ATOM   4059 C CA  . ALA A 1 507 ? 38.167 106.959 22.257  1.00 23.77 ? 507  ALA A CA  1 
ATOM   4060 C C   . ALA A 1 507 ? 38.739 107.457 23.550  1.00 23.64 ? 507  ALA A C   1 
ATOM   4061 O O   . ALA A 1 507 ? 38.394 108.539 23.991  1.00 24.13 ? 507  ALA A O   1 
ATOM   4062 C CB  . ALA A 1 507 ? 37.070 105.932 22.528  1.00 25.38 ? 507  ALA A CB  1 
ATOM   4063 N N   . THR A 1 508 ? 39.673 106.731 24.167  1.00 23.36 ? 508  THR A N   1 
ATOM   4064 C CA  . THR A 1 508 ? 40.260 107.198 25.414  1.00 23.06 ? 508  THR A CA  1 
ATOM   4065 C C   . THR A 1 508 ? 41.104 108.460 25.232  1.00 23.97 ? 508  THR A C   1 
ATOM   4066 O O   . THR A 1 508 ? 41.075 109.360 26.074  1.00 24.02 ? 508  THR A O   1 
ATOM   4067 C CB  . THR A 1 508 ? 41.053 106.071 26.128  1.00 23.68 ? 508  THR A CB  1 
ATOM   4068 O OG1 . THR A 1 508 ? 40.160 104.973 26.369  1.00 24.53 ? 508  THR A OG1 1 
ATOM   4069 C CG2 . THR A 1 508 ? 41.662 106.588 27.441  1.00 21.99 ? 508  THR A CG2 1 
ATOM   4070 N N   . ALA A 1 509 ? 41.851 108.506 24.136  1.00 24.41 ? 509  ALA A N   1 
ATOM   4071 C CA  . ALA A 1 509 ? 42.601 109.696 23.726  1.00 25.97 ? 509  ALA A CA  1 
ATOM   4072 C C   . ALA A 1 509 ? 41.632 110.839 23.498  1.00 26.48 ? 509  ALA A C   1 
ATOM   4073 O O   . ALA A 1 509 ? 41.918 111.955 23.863  1.00 26.68 ? 509  ALA A O   1 
ATOM   4074 C CB  . ALA A 1 509 ? 43.396 109.425 22.426  1.00 24.80 ? 509  ALA A CB  1 
ATOM   4075 N N   . GLU A 1 510 ? 40.476 110.544 22.910  1.00 29.20 ? 510  GLU A N   1 
ATOM   4076 C CA  . GLU A 1 510 ? 39.431 111.560 22.710  1.00 30.84 ? 510  GLU A CA  1 
ATOM   4077 C C   . GLU A 1 510 ? 38.905 112.114 24.057  1.00 30.79 ? 510  GLU A C   1 
ATOM   4078 O O   . GLU A 1 510 ? 38.793 113.340 24.229  1.00 30.58 ? 510  GLU A O   1 
ATOM   4079 C CB  . GLU A 1 510 ? 38.308 110.977 21.857  1.00 32.30 ? 510  GLU A CB  1 
ATOM   4080 C CG  . GLU A 1 510 ? 37.275 111.993 21.383  1.00 37.54 ? 510  GLU A CG  1 
ATOM   4081 C CD  . GLU A 1 510 ? 37.879 113.080 20.480  1.00 45.65 ? 510  GLU A CD  1 
ATOM   4082 O OE1 . GLU A 1 510 ? 39.041 112.910 20.003  1.00 47.27 ? 510  GLU A OE1 1 
ATOM   4083 O OE2 . GLU A 1 510 ? 37.180 114.105 20.256  1.00 49.55 ? 510  GLU A OE2 1 
ATOM   4084 N N   . ALA A 1 511 ? 38.630 111.217 25.022  1.00 30.44 ? 511  ALA A N   1 
ATOM   4085 C CA  . ALA A 1 511 ? 38.254 111.577 26.389  1.00 29.05 ? 511  ALA A CA  1 
ATOM   4086 C C   . ALA A 1 511 ? 39.264 112.497 27.054  1.00 29.28 ? 511  ALA A C   1 
ATOM   4087 O O   . ALA A 1 511 ? 38.892 113.418 27.780  1.00 26.83 ? 511  ALA A O   1 
ATOM   4088 C CB  . ALA A 1 511 ? 38.055 110.316 27.263  1.00 29.54 ? 511  ALA A CB  1 
ATOM   4089 N N   . ALA A 1 512 ? 40.558 112.225 26.830  1.00 28.31 ? 512  ALA A N   1 
ATOM   4090 C CA  . ALA A 1 512 ? 41.635 112.990 27.435  1.00 28.09 ? 512  ALA A CA  1 
ATOM   4091 C C   . ALA A 1 512 ? 41.654 114.447 26.927  1.00 28.28 ? 512  ALA A C   1 
ATOM   4092 O O   . ALA A 1 512 ? 42.193 115.309 27.597  1.00 27.13 ? 512  ALA A O   1 
ATOM   4093 C CB  . ALA A 1 512 ? 43.030 112.286 27.197  1.00 28.07 ? 512  ALA A CB  1 
ATOM   4094 N N   . LYS A 1 513 ? 41.062 114.729 25.769  1.00 28.58 ? 513  LYS A N   1 
ATOM   4095 C CA  . LYS A 1 513 ? 41.007 116.111 25.302  1.00 30.78 ? 513  LYS A CA  1 
ATOM   4096 C C   . LYS A 1 513 ? 40.161 116.965 26.254  1.00 30.98 ? 513  LYS A C   1 
ATOM   4097 O O   . LYS A 1 513 ? 40.419 118.162 26.401  1.00 31.47 ? 513  LYS A O   1 
ATOM   4098 C CB  . LYS A 1 513 ? 40.430 116.225 23.889  1.00 30.23 ? 513  LYS A CB  1 
ATOM   4099 C CG  . LYS A 1 513 ? 41.235 115.520 22.812  1.00 32.68 ? 513  LYS A CG  1 
ATOM   4100 C CD  . LYS A 1 513 ? 40.583 115.667 21.438  1.00 33.38 ? 513  LYS A CD  1 
ATOM   4101 C CE  . LYS A 1 513 ? 41.516 115.138 20.325  1.00 38.12 ? 513  LYS A CE  1 
ATOM   4102 N NZ  . LYS A 1 513 ? 40.774 114.931 19.011  1.00 40.16 ? 513  LYS A NZ  1 
ATOM   4103 N N   . THR A 1 514 ? 39.119 116.357 26.843  1.00 31.05 ? 514  THR A N   1 
ATOM   4104 C CA  . THR A 1 514 ? 38.230 117.041 27.807  1.00 30.15 ? 514  THR A CA  1 
ATOM   4105 C C   . THR A 1 514 ? 38.795 116.939 29.225  1.00 29.93 ? 514  THR A C   1 
ATOM   4106 O O   . THR A 1 514 ? 38.868 117.923 29.976  1.00 29.94 ? 514  THR A O   1 
ATOM   4107 C CB  . THR A 1 514 ? 36.834 116.445 27.711  1.00 29.90 ? 514  THR A CB  1 
ATOM   4108 O OG1 . THR A 1 514 ? 36.347 116.668 26.385  1.00 30.76 ? 514  THR A OG1 1 
ATOM   4109 C CG2 . THR A 1 514 ? 35.866 117.048 28.757  1.00 33.19 ? 514  THR A CG2 1 
ATOM   4110 N N   . VAL A 1 515 ? 39.258 115.756 29.598  1.00 29.13 ? 515  VAL A N   1 
ATOM   4111 C CA  . VAL A 1 515 ? 39.605 115.524 30.990  1.00 28.58 ? 515  VAL A CA  1 
ATOM   4112 C C   . VAL A 1 515 ? 40.927 116.186 31.328  1.00 28.90 ? 515  VAL A C   1 
ATOM   4113 O O   . VAL A 1 515 ? 41.098 116.697 32.447  1.00 28.60 ? 515  VAL A O   1 
ATOM   4114 C CB  . VAL A 1 515 ? 39.527 113.986 31.340  1.00 29.17 ? 515  VAL A CB  1 
ATOM   4115 C CG1 . VAL A 1 515 ? 39.753 113.731 32.813  1.00 28.93 ? 515  VAL A CG1 1 
ATOM   4116 C CG2 . VAL A 1 515 ? 38.182 113.461 30.942  1.00 28.92 ? 515  VAL A CG2 1 
ATOM   4117 N N   . PHE A 1 516 ? 41.863 116.216 30.367  1.00 28.59 ? 516  PHE A N   1 
ATOM   4118 C CA  . PHE A 1 516 ? 43.185 116.813 30.611  1.00 29.11 ? 516  PHE A CA  1 
ATOM   4119 C C   . PHE A 1 516 ? 43.479 117.829 29.512  1.00 29.46 ? 516  PHE A C   1 
ATOM   4120 O O   . PHE A 1 516 ? 44.298 117.543 28.630  1.00 28.92 ? 516  PHE A O   1 
ATOM   4121 C CB  . PHE A 1 516 ? 44.267 115.705 30.536  1.00 28.58 ? 516  PHE A CB  1 
ATOM   4122 C CG  . PHE A 1 516 ? 44.052 114.588 31.505  1.00 29.51 ? 516  PHE A CG  1 
ATOM   4123 C CD1 . PHE A 1 516 ? 44.292 114.779 32.867  1.00 29.60 ? 516  PHE A CD1 1 
ATOM   4124 C CD2 . PHE A 1 516 ? 43.631 113.343 31.054  1.00 25.72 ? 516  PHE A CD2 1 
ATOM   4125 C CE1 . PHE A 1 516 ? 44.118 113.721 33.762  1.00 29.34 ? 516  PHE A CE1 1 
ATOM   4126 C CE2 . PHE A 1 516 ? 43.437 112.285 31.961  1.00 29.97 ? 516  PHE A CE2 1 
ATOM   4127 C CZ  . PHE A 1 516 ? 43.691 112.484 33.289  1.00 28.74 ? 516  PHE A CZ  1 
ATOM   4128 N N   . PRO A 1 517 ? 42.784 118.987 29.521  1.00 30.21 ? 517  PRO A N   1 
ATOM   4129 C CA  . PRO A 1 517 ? 42.827 119.799 28.313  1.00 30.31 ? 517  PRO A CA  1 
ATOM   4130 C C   . PRO A 1 517 ? 44.240 120.303 28.001  1.00 29.87 ? 517  PRO A C   1 
ATOM   4131 O O   . PRO A 1 517 ? 44.934 120.807 28.868  1.00 31.00 ? 517  PRO A O   1 
ATOM   4132 C CB  . PRO A 1 517 ? 41.838 120.966 28.601  1.00 31.17 ? 517  PRO A CB  1 
ATOM   4133 C CG  . PRO A 1 517 ? 41.609 120.954 30.081  1.00 32.16 ? 517  PRO A CG  1 
ATOM   4134 C CD  . PRO A 1 517 ? 41.985 119.595 30.612  1.00 29.27 ? 517  PRO A CD  1 
ATOM   4135 N N   . ASN A 1 518 ? 44.640 120.092 26.760  1.00 29.47 ? 518  ASN A N   1 
ATOM   4136 C CA  . ASN A 1 518 ? 45.939 120.465 26.229  1.00 30.86 ? 518  ASN A CA  1 
ATOM   4137 C C   . ASN A 1 518 ? 47.114 119.615 26.724  1.00 28.86 ? 518  ASN A C   1 
ATOM   4138 O O   . ASN A 1 518 ? 48.245 119.977 26.475  1.00 29.55 ? 518  ASN A O   1 
ATOM   4139 C CB  . ASN A 1 518 ? 46.206 121.965 26.446  1.00 31.82 ? 518  ASN A CB  1 
ATOM   4140 C CG  . ASN A 1 518 ? 45.181 122.814 25.712  1.00 38.18 ? 518  ASN A CG  1 
ATOM   4141 O OD1 . ASN A 1 518 ? 44.786 122.473 24.576  1.00 42.58 ? 518  ASN A OD1 1 
ATOM   4142 N ND2 . ASN A 1 518 ? 44.694 123.870 26.368  1.00 41.55 ? 518  ASN A ND2 1 
ATOM   4143 N N   . LYS A 1 519 ? 46.838 118.512 27.413  1.00 26.79 ? 519  LYS A N   1 
ATOM   4144 C CA  . LYS A 1 519 ? 47.910 117.714 28.021  1.00 25.33 ? 519  LYS A CA  1 
ATOM   4145 C C   . LYS A 1 519 ? 48.002 116.384 27.320  1.00 24.40 ? 519  LYS A C   1 
ATOM   4146 O O   . LYS A 1 519 ? 47.033 115.898 26.728  1.00 23.67 ? 519  LYS A O   1 
ATOM   4147 C CB  . LYS A 1 519 ? 47.681 117.477 29.510  1.00 25.55 ? 519  LYS A CB  1 
ATOM   4148 C CG  . LYS A 1 519 ? 47.576 118.722 30.348  1.00 27.06 ? 519  LYS A CG  1 
ATOM   4149 C CD  . LYS A 1 519 ? 48.884 119.509 30.447  1.00 27.77 ? 519  LYS A CD  1 
ATOM   4150 C CE  . LYS A 1 519 ? 48.672 120.634 31.422  1.00 30.01 ? 519  LYS A CE  1 
ATOM   4151 N NZ  . LYS A 1 519 ? 49.805 121.596 31.473  1.00 35.47 ? 519  LYS A NZ  1 
ATOM   4152 N N   . ARG A 1 520 ? 49.186 115.797 27.344  1.00 21.60 ? 520  ARG A N   1 
ATOM   4153 C CA  . ARG A 1 520 ? 49.351 114.461 26.787  1.00 21.84 ? 520  ARG A CA  1 
ATOM   4154 C C   . ARG A 1 520 ? 48.752 113.415 27.721  1.00 22.08 ? 520  ARG A C   1 
ATOM   4155 O O   . ARG A 1 520 ? 48.326 112.363 27.234  1.00 21.95 ? 520  ARG A O   1 
ATOM   4156 C CB  . ARG A 1 520 ? 50.826 114.101 26.664  1.00 22.59 ? 520  ARG A CB  1 
ATOM   4157 C CG  . ARG A 1 520 ? 51.635 115.157 25.881  1.00 21.44 ? 520  ARG A CG  1 
ATOM   4158 C CD  . ARG A 1 520 ? 53.098 114.910 25.870  1.00 24.14 ? 520  ARG A CD  1 
ATOM   4159 N NE  . ARG A 1 520 ? 53.687 116.158 25.408  1.00 23.17 ? 520  ARG A NE  1 
ATOM   4160 C CZ  . ARG A 1 520 ? 54.954 116.483 25.498  1.00 25.40 ? 520  ARG A CZ  1 
ATOM   4161 N NH1 . ARG A 1 520 ? 55.840 115.596 25.988  1.00 21.99 ? 520  ARG A NH1 1 
ATOM   4162 N NH2 . ARG A 1 520 ? 55.318 117.706 25.087  1.00 22.72 ? 520  ARG A NH2 1 
ATOM   4163 N N   . SER A 1 521 ? 48.833 113.650 29.036  1.00 21.02 ? 521  SER A N   1 
ATOM   4164 C CA  . SER A 1 521 ? 48.418 112.627 30.014  1.00 21.40 ? 521  SER A CA  1 
ATOM   4165 C C   . SER A 1 521 ? 49.199 111.316 29.683  1.00 22.45 ? 521  SER A C   1 
ATOM   4166 O O   . SER A 1 521 ? 50.337 111.383 29.235  1.00 22.21 ? 521  SER A O   1 
ATOM   4167 C CB  . SER A 1 521 ? 46.911 112.367 29.889  1.00 20.17 ? 521  SER A CB  1 
ATOM   4168 O OG  . SER A 1 521 ? 46.474 111.407 30.871  1.00 21.79 ? 521  SER A OG  1 
ATOM   4169 N N   . PHE A 1 522 ? 48.559 110.145 29.838  1.00 21.11 ? 522  PHE A N   1 
ATOM   4170 C CA  . PHE A 1 522 ? 49.240 108.873 29.575  1.00 21.89 ? 522  PHE A CA  1 
ATOM   4171 C C   . PHE A 1 522 ? 48.186 107.825 29.406  1.00 20.51 ? 522  PHE A C   1 
ATOM   4172 O O   . PHE A 1 522 ? 47.297 107.709 30.291  1.00 20.88 ? 522  PHE A O   1 
ATOM   4173 C CB  . PHE A 1 522 ? 50.108 108.528 30.776  1.00 20.19 ? 522  PHE A CB  1 
ATOM   4174 C CG  . PHE A 1 522 ? 50.706 107.120 30.756  1.00 24.20 ? 522  PHE A CG  1 
ATOM   4175 C CD1 . PHE A 1 522 ? 51.837 106.817 29.980  1.00 25.35 ? 522  PHE A CD1 1 
ATOM   4176 C CD2 . PHE A 1 522 ? 50.147 106.114 31.545  1.00 23.64 ? 522  PHE A CD2 1 
ATOM   4177 C CE1 . PHE A 1 522 ? 52.410 105.503 29.975  1.00 25.32 ? 522  PHE A CE1 1 
ATOM   4178 C CE2 . PHE A 1 522 ? 50.699 104.824 31.571  1.00 26.81 ? 522  PHE A CE2 1 
ATOM   4179 C CZ  . PHE A 1 522 ? 51.845 104.512 30.800  1.00 23.06 ? 522  PHE A CZ  1 
ATOM   4180 N N   . ILE A 1 523 ? 48.243 107.059 28.317  1.00 19.11 ? 523  ILE A N   1 
ATOM   4181 C CA  . ILE A 1 523 ? 47.321 105.925 28.152  1.00 20.16 ? 523  ILE A CA  1 
ATOM   4182 C C   . ILE A 1 523 ? 48.174 104.688 27.949  1.00 20.46 ? 523  ILE A C   1 
ATOM   4183 O O   . ILE A 1 523 ? 49.091 104.692 27.095  1.00 20.24 ? 523  ILE A O   1 
ATOM   4184 C CB  . ILE A 1 523 ? 46.389 106.094 26.937  1.00 20.97 ? 523  ILE A CB  1 
ATOM   4185 C CG1 . ILE A 1 523 ? 45.461 107.300 27.110  1.00 23.70 ? 523  ILE A CG1 1 
ATOM   4186 C CG2 . ILE A 1 523 ? 45.433 104.872 26.778  1.00 24.42 ? 523  ILE A CG2 1 
ATOM   4187 C CD1 . ILE A 1 523 ? 45.003 107.875 25.753  1.00 27.77 ? 523  ILE A CD1 1 
ATOM   4188 N N   . LEU A 1 524 ? 47.881 103.637 28.693  1.00 18.51 ? 524  LEU A N   1 
ATOM   4189 C CA  . LEU A 1 524 ? 48.592 102.348 28.551  1.00 19.29 ? 524  LEU A CA  1 
ATOM   4190 C C   . LEU A 1 524 ? 47.566 101.326 28.148  1.00 19.75 ? 524  LEU A C   1 
ATOM   4191 O O   . LEU A 1 524 ? 46.526 101.238 28.788  1.00 21.21 ? 524  LEU A O   1 
ATOM   4192 C CB  . LEU A 1 524 ? 49.180 101.969 29.930  1.00 19.06 ? 524  LEU A CB  1 
ATOM   4193 C CG  . LEU A 1 524 ? 49.797 100.574 30.037  1.00 20.53 ? 524  LEU A CG  1 
ATOM   4194 C CD1 . LEU A 1 524 ? 51.033 100.515 29.206  1.00 18.34 ? 524  LEU A CD1 1 
ATOM   4195 C CD2 . LEU A 1 524 ? 50.128 100.348 31.487  1.00 17.25 ? 524  LEU A CD2 1 
ATOM   4196 N N   . THR A 1 525 ? 47.798 100.558 27.090  1.00 20.42 ? 525  THR A N   1 
ATOM   4197 C CA  . THR A 1 525 ? 46.768 99.651  26.614  1.00 21.43 ? 525  THR A CA  1 
ATOM   4198 C C   . THR A 1 525 ? 47.338 98.252  26.509  1.00 22.80 ? 525  THR A C   1 
ATOM   4199 O O   . THR A 1 525 ? 48.530 98.071  26.260  1.00 22.62 ? 525  THR A O   1 
ATOM   4200 C CB  . THR A 1 525 ? 46.217 100.074 25.250  1.00 22.14 ? 525  THR A CB  1 
ATOM   4201 O OG1 . THR A 1 525 ? 45.161 99.169  24.858  1.00 23.14 ? 525  THR A OG1 1 
ATOM   4202 C CG2 . THR A 1 525 ? 47.332 100.106 24.159  1.00 23.19 ? 525  THR A CG2 1 
ATOM   4203 N N   . ARG A 1 526 ? 46.474 97.267  26.696  1.00 23.40 ? 526  ARG A N   1 
ATOM   4204 C CA  . ARG A 1 526 ? 46.835 95.894  26.474  1.00 24.79 ? 526  ARG A CA  1 
ATOM   4205 C C   . ARG A 1 526 ? 46.677 95.498  25.025  1.00 22.68 ? 526  ARG A C   1 
ATOM   4206 O O   . ARG A 1 526 ? 47.600 95.072  24.409  1.00 23.92 ? 526  ARG A O   1 
ATOM   4207 C CB  . ARG A 1 526 ? 46.008 94.911  27.369  1.00 22.87 ? 526  ARG A CB  1 
ATOM   4208 C CG  . ARG A 1 526 ? 46.834 93.580  27.573  1.00 29.73 ? 526  ARG A CG  1 
ATOM   4209 C CD  . ARG A 1 526 ? 46.374 92.780  28.799  1.00 28.67 ? 526  ARG A CD  1 
ATOM   4210 N NE  . ARG A 1 526 ? 45.062 92.209  28.490  1.00 34.08 ? 526  ARG A NE  1 
ATOM   4211 C CZ  . ARG A 1 526 ? 44.420 91.364  29.306  1.00 33.99 ? 526  ARG A CZ  1 
ATOM   4212 N NH1 . ARG A 1 526 ? 44.979 91.032  30.464  1.00 34.80 ? 526  ARG A NH1 1 
ATOM   4213 N NH2 . ARG A 1 526 ? 43.231 90.892  28.977  1.00 26.98 ? 526  ARG A NH2 1 
ATOM   4214 N N   . SER A 1 527 ? 45.477 95.601  24.479  1.00 22.72 ? 527  SER A N   1 
ATOM   4215 C CA  . SER A 1 527 ? 45.306 95.166  23.114  1.00 22.74 ? 527  SER A CA  1 
ATOM   4216 C C   . SER A 1 527 ? 45.695 96.291  22.118  1.00 23.23 ? 527  SER A C   1 
ATOM   4217 O O   . SER A 1 527 ? 45.414 97.473  22.394  1.00 23.23 ? 527  SER A O   1 
ATOM   4218 C CB  . SER A 1 527 ? 43.884 94.709  22.894  1.00 21.54 ? 527  SER A CB  1 
ATOM   4219 O OG  . SER A 1 527 ? 43.774 94.363  21.538  1.00 28.13 ? 527  SER A OG  1 
ATOM   4220 N N   . THR A 1 528 ? 46.353 95.931  21.007  1.00 21.63 ? 528  THR A N   1 
ATOM   4221 C CA  . THR A 1 528 ? 46.837 96.920  20.005  1.00 22.22 ? 528  THR A CA  1 
ATOM   4222 C C   . THR A 1 528 ? 46.484 96.427  18.593  1.00 22.30 ? 528  THR A C   1 
ATOM   4223 O O   . THR A 1 528 ? 46.242 95.213  18.396  1.00 22.13 ? 528  THR A O   1 
ATOM   4224 C CB  . THR A 1 528 ? 48.385 97.182  20.042  1.00 22.68 ? 528  THR A CB  1 
ATOM   4225 O OG1 . THR A 1 528 ? 49.094 95.958  19.770  1.00 22.02 ? 528  THR A OG1 1 
ATOM   4226 C CG2 . THR A 1 528 ? 48.860 97.840  21.389  1.00 20.90 ? 528  THR A CG2 1 
ATOM   4227 N N   . PHE A 1 529 ? 46.437 97.389  17.632  1.00 21.65 ? 529  PHE A N   1 
ATOM   4228 C CA  . PHE A 1 529 ? 46.432 97.133  16.217  1.00 21.09 ? 529  PHE A CA  1 
ATOM   4229 C C   . PHE A 1 529 ? 47.510 98.059  15.655  1.00 20.88 ? 529  PHE A C   1 
ATOM   4230 O O   . PHE A 1 529 ? 48.037 98.859  16.383  1.00 21.91 ? 529  PHE A O   1 
ATOM   4231 C CB  . PHE A 1 529 ? 45.040 97.436  15.614  1.00 21.53 ? 529  PHE A CB  1 
ATOM   4232 C CG  . PHE A 1 529 ? 44.880 96.957  14.205  1.00 22.78 ? 529  PHE A CG  1 
ATOM   4233 C CD1 . PHE A 1 529 ? 44.735 95.596  13.921  1.00 23.70 ? 529  PHE A CD1 1 
ATOM   4234 C CD2 . PHE A 1 529 ? 44.920 97.875  13.141  1.00 23.80 ? 529  PHE A CD2 1 
ATOM   4235 C CE1 . PHE A 1 529 ? 44.627 95.163  12.615  1.00 26.56 ? 529  PHE A CE1 1 
ATOM   4236 C CE2 . PHE A 1 529 ? 44.793 97.462  11.850  1.00 23.67 ? 529  PHE A CE2 1 
ATOM   4237 C CZ  . PHE A 1 529 ? 44.640 96.100  11.569  1.00 25.18 ? 529  PHE A CZ  1 
ATOM   4238 N N   . ALA A 1 530 ? 47.881 97.877  14.399  1.00 19.53 ? 530  ALA A N   1 
ATOM   4239 C CA  . ALA A 1 530 ? 48.780 98.789  13.663  1.00 21.32 ? 530  ALA A CA  1 
ATOM   4240 C C   . ALA A 1 530 ? 48.329 100.235 13.819  1.00 20.69 ? 530  ALA A C   1 
ATOM   4241 O O   . ALA A 1 530 ? 47.167 100.598 13.548  1.00 22.28 ? 530  ALA A O   1 
ATOM   4242 C CB  . ALA A 1 530 ? 48.847 98.373  12.185  1.00 20.71 ? 530  ALA A CB  1 
ATOM   4243 N N   . GLY A 1 531 ? 49.204 101.063 14.351  1.00 20.76 ? 531  GLY A N   1 
ATOM   4244 C CA  . GLY A 1 531 ? 48.795 102.418 14.572  1.00 19.16 ? 531  GLY A CA  1 
ATOM   4245 C C   . GLY A 1 531 ? 48.483 102.789 16.006  1.00 18.61 ? 531  GLY A C   1 
ATOM   4246 O O   . GLY A 1 531 ? 48.358 103.966 16.299  1.00 17.85 ? 531  GLY A O   1 
ATOM   4247 N N   . SER A 1 532 ? 48.356 101.798 16.912  1.00 19.43 ? 532  SER A N   1 
ATOM   4248 C CA  . SER A 1 532 ? 47.966 102.080 18.301  1.00 19.36 ? 532  SER A CA  1 
ATOM   4249 C C   . SER A 1 532 ? 48.920 103.005 19.018  1.00 20.56 ? 532  SER A C   1 
ATOM   4250 O O   . SER A 1 532 ? 48.494 103.729 19.951  1.00 20.29 ? 532  SER A O   1 
ATOM   4251 C CB  . SER A 1 532 ? 47.761 100.805 19.157  1.00 19.58 ? 532  SER A CB  1 
ATOM   4252 O OG  . SER A 1 532 ? 46.562 100.135 18.810  1.00 19.65 ? 532  SER A OG  1 
ATOM   4253 N N   . GLY A 1 533 ? 50.198 102.973 18.625  1.00 19.61 ? 533  GLY A N   1 
ATOM   4254 C CA  . GLY A 1 533 ? 51.234 103.828 19.272  1.00 20.00 ? 533  GLY A CA  1 
ATOM   4255 C C   . GLY A 1 533 ? 50.968 105.322 19.151  1.00 20.71 ? 533  GLY A C   1 
ATOM   4256 O O   . GLY A 1 533 ? 51.525 106.117 19.894  1.00 21.54 ? 533  GLY A O   1 
ATOM   4257 N N   . LYS A 1 534 ? 50.107 105.719 18.223  1.00 20.73 ? 534  LYS A N   1 
ATOM   4258 C CA  . LYS A 1 534 ? 49.794 107.133 18.083  1.00 21.76 ? 534  LYS A CA  1 
ATOM   4259 C C   . LYS A 1 534 ? 49.021 107.629 19.312  1.00 22.13 ? 534  LYS A C   1 
ATOM   4260 O O   . LYS A 1 534 ? 49.035 108.811 19.618  1.00 22.21 ? 534  LYS A O   1 
ATOM   4261 C CB  . LYS A 1 534 ? 49.073 107.365 16.761  1.00 21.89 ? 534  LYS A CB  1 
ATOM   4262 C CG  . LYS A 1 534 ? 48.660 108.821 16.451  1.00 25.41 ? 534  LYS A CG  1 
ATOM   4263 C CD  . LYS A 1 534 ? 47.681 108.800 15.266  1.00 25.60 ? 534  LYS A CD  1 
ATOM   4264 C CE  . LYS A 1 534 ? 47.121 110.225 14.878  1.00 27.16 ? 534  LYS A CE  1 
ATOM   4265 N NZ  . LYS A 1 534 ? 46.155 110.051 13.727  1.00 27.63 ? 534  LYS A NZ  1 
ATOM   4266 N N   . PHE A 1 535 ? 48.393 106.697 20.042  1.00 21.85 ? 535  PHE A N   1 
ATOM   4267 C CA  . PHE A 1 535 ? 47.529 107.008 21.166  1.00 22.52 ? 535  PHE A CA  1 
ATOM   4268 C C   . PHE A 1 535 ? 47.996 106.494 22.523  1.00 23.26 ? 535  PHE A C   1 
ATOM   4269 O O   . PHE A 1 535 ? 47.631 107.059 23.560  1.00 24.46 ? 535  PHE A O   1 
ATOM   4270 C CB  . PHE A 1 535 ? 46.157 106.411 20.875  1.00 22.22 ? 535  PHE A CB  1 
ATOM   4271 C CG  . PHE A 1 535 ? 45.614 106.811 19.550  1.00 25.10 ? 535  PHE A CG  1 
ATOM   4272 C CD1 . PHE A 1 535 ? 45.085 108.078 19.370  1.00 27.14 ? 535  PHE A CD1 1 
ATOM   4273 C CD2 . PHE A 1 535 ? 45.622 105.924 18.483  1.00 26.11 ? 535  PHE A CD2 1 
ATOM   4274 C CE1 . PHE A 1 535 ? 44.618 108.476 18.151  1.00 25.79 ? 535  PHE A CE1 1 
ATOM   4275 C CE2 . PHE A 1 535 ? 45.127 106.317 17.245  1.00 27.35 ? 535  PHE A CE2 1 
ATOM   4276 C CZ  . PHE A 1 535 ? 44.627 107.588 17.086  1.00 24.75 ? 535  PHE A CZ  1 
ATOM   4277 N N   . ALA A 1 536 ? 48.785 105.417 22.544  1.00 21.56 ? 536  ALA A N   1 
ATOM   4278 C CA  . ALA A 1 536 ? 48.969 104.699 23.788  1.00 20.44 ? 536  ALA A CA  1 
ATOM   4279 C C   . ALA A 1 536 ? 50.330 104.007 23.881  1.00 20.30 ? 536  ALA A C   1 
ATOM   4280 O O   . ALA A 1 536 ? 50.867 103.562 22.860  1.00 20.78 ? 536  ALA A O   1 
ATOM   4281 C CB  . ALA A 1 536 ? 47.831 103.652 23.889  1.00 20.45 ? 536  ALA A CB  1 
ATOM   4282 N N   . ALA A 1 537 ? 50.847 103.896 25.099  1.00 19.67 ? 537  ALA A N   1 
ATOM   4283 C CA  . ALA A 1 537 ? 51.881 102.913 25.489  1.00 19.40 ? 537  ALA A CA  1 
ATOM   4284 C C   . ALA A 1 537 ? 51.323 101.489 25.562  1.00 20.98 ? 537  ALA A C   1 
ATOM   4285 O O   . ALA A 1 537 ? 50.098 101.281 25.612  1.00 19.32 ? 537  ALA A O   1 
ATOM   4286 C CB  . ALA A 1 537 ? 52.424 103.300 26.858  1.00 19.27 ? 537  ALA A CB  1 
ATOM   4287 N N   . HIS A 1 538 ? 52.213 100.481 25.629  1.00 20.91 ? 538  HIS A N   1 
ATOM   4288 C CA  . HIS A 1 538 ? 51.735 99.077  25.666  1.00 21.41 ? 538  HIS A CA  1 
ATOM   4289 C C   . HIS A 1 538 ? 52.521 98.371  26.739  1.00 21.46 ? 538  HIS A C   1 
ATOM   4290 O O   . HIS A 1 538 ? 53.641 98.731  27.017  1.00 21.10 ? 538  HIS A O   1 
ATOM   4291 C CB  . HIS A 1 538 ? 51.971 98.384  24.308  1.00 21.75 ? 538  HIS A CB  1 
ATOM   4292 C CG  . HIS A 1 538 ? 51.601 96.937  24.301  1.00 21.09 ? 538  HIS A CG  1 
ATOM   4293 N ND1 . HIS A 1 538 ? 50.333 96.487  24.635  1.00 23.97 ? 538  HIS A ND1 1 
ATOM   4294 C CD2 . HIS A 1 538 ? 52.341 95.833  24.062  1.00 25.46 ? 538  HIS A CD2 1 
ATOM   4295 C CE1 . HIS A 1 538 ? 50.308 95.167  24.576  1.00 29.10 ? 538  HIS A CE1 1 
ATOM   4296 N NE2 . HIS A 1 538 ? 51.506 94.744  24.214  1.00 25.13 ? 538  HIS A NE2 1 
ATOM   4297 N N   . TRP A 1 539 ? 51.913 97.436  27.424  1.00 22.46 ? 539  TRP A N   1 
ATOM   4298 C CA  . TRP A 1 539 ? 52.753 96.568  28.234  1.00 23.81 ? 539  TRP A CA  1 
ATOM   4299 C C   . TRP A 1 539 ? 52.557 95.143  27.810  1.00 23.85 ? 539  TRP A C   1 
ATOM   4300 O O   . TRP A 1 539 ? 51.472 94.767  27.330  1.00 23.34 ? 539  TRP A O   1 
ATOM   4301 C CB  . TRP A 1 539 ? 52.615 96.770  29.745  1.00 26.16 ? 539  TRP A CB  1 
ATOM   4302 C CG  . TRP A 1 539 ? 51.632 95.901  30.393  1.00 24.78 ? 539  TRP A CG  1 
ATOM   4303 C CD1 . TRP A 1 539 ? 51.875 94.848  31.242  1.00 26.82 ? 539  TRP A CD1 1 
ATOM   4304 C CD2 . TRP A 1 539 ? 50.244 96.038  30.294  1.00 27.51 ? 539  TRP A CD2 1 
ATOM   4305 N NE1 . TRP A 1 539 ? 50.679 94.308  31.665  1.00 30.30 ? 539  TRP A NE1 1 
ATOM   4306 C CE2 . TRP A 1 539 ? 49.658 95.011  31.083  1.00 27.04 ? 539  TRP A CE2 1 
ATOM   4307 C CE3 . TRP A 1 539 ? 49.414 96.926  29.598  1.00 27.85 ? 539  TRP A CE3 1 
ATOM   4308 C CZ2 . TRP A 1 539 ? 48.277 94.852  31.204  1.00 28.70 ? 539  TRP A CZ2 1 
ATOM   4309 C CZ3 . TRP A 1 539 ? 48.021 96.775  29.724  1.00 29.86 ? 539  TRP A CZ3 1 
ATOM   4310 C CH2 . TRP A 1 539 ? 47.471 95.730  30.519  1.00 28.66 ? 539  TRP A CH2 1 
ATOM   4311 N N   . LEU A 1 540 ? 53.615 94.357  28.001  1.00 23.24 ? 540  LEU A N   1 
ATOM   4312 C CA  . LEU A 1 540 ? 53.678 93.046  27.386  1.00 25.26 ? 540  LEU A CA  1 
ATOM   4313 C C   . LEU A 1 540 ? 52.757 92.004  28.066  1.00 25.95 ? 540  LEU A C   1 
ATOM   4314 O O   . LEU A 1 540 ? 52.704 90.888  27.629  1.00 26.64 ? 540  LEU A O   1 
ATOM   4315 C CB  . LEU A 1 540 ? 55.129 92.588  27.309  1.00 23.02 ? 540  LEU A CB  1 
ATOM   4316 C CG  . LEU A 1 540 ? 55.936 93.502  26.332  1.00 25.18 ? 540  LEU A CG  1 
ATOM   4317 C CD1 . LEU A 1 540 ? 57.408 93.040  26.353  1.00 24.43 ? 540  LEU A CD1 1 
ATOM   4318 C CD2 . LEU A 1 540 ? 55.447 93.398  24.905  1.00 21.33 ? 540  LEU A CD2 1 
ATOM   4319 N N   . GLY A 1 541 ? 52.043 92.403  29.115  1.00 26.21 ? 541  GLY A N   1 
ATOM   4320 C CA  . GLY A 1 541 ? 50.965 91.588  29.683  1.00 26.45 ? 541  GLY A CA  1 
ATOM   4321 C C   . GLY A 1 541 ? 51.379 90.831  30.923  1.00 27.08 ? 541  GLY A C   1 
ATOM   4322 O O   . GLY A 1 541 ? 52.394 91.156  31.593  1.00 27.67 ? 541  GLY A O   1 
ATOM   4323 N N   . ASP A 1 542 ? 50.631 89.767  31.174  1.00 28.24 ? 542  ASP A N   1 
ATOM   4324 C CA  . ASP A 1 542 ? 50.681 88.982  32.411  1.00 29.21 ? 542  ASP A CA  1 
ATOM   4325 C C   . ASP A 1 542 ? 51.767 87.913  32.291  1.00 28.19 ? 542  ASP A C   1 
ATOM   4326 O O   . ASP A 1 542 ? 51.493 86.729  32.070  1.00 29.57 ? 542  ASP A O   1 
ATOM   4327 C CB  . ASP A 1 542 ? 49.306 88.313  32.676  1.00 30.71 ? 542  ASP A CB  1 
ATOM   4328 C CG  . ASP A 1 542 ? 48.142 89.316  32.823  1.00 35.95 ? 542  ASP A CG  1 
ATOM   4329 O OD1 . ASP A 1 542 ? 48.381 90.539  33.039  1.00 40.59 ? 542  ASP A OD1 1 
ATOM   4330 O OD2 . ASP A 1 542 ? 46.954 88.880  32.736  1.00 41.36 ? 542  ASP A OD2 1 
ATOM   4331 N N   . ASN A 1 543 ? 53.002 88.326  32.461  1.00 26.58 ? 543  ASN A N   1 
ATOM   4332 C CA  . ASN A 1 543 ? 54.128 87.436  32.385  1.00 24.91 ? 543  ASN A CA  1 
ATOM   4333 C C   . ASN A 1 543 ? 54.245 86.716  33.747  1.00 25.65 ? 543  ASN A C   1 
ATOM   4334 O O   . ASN A 1 543 ? 53.328 86.793  34.604  1.00 25.22 ? 543  ASN A O   1 
ATOM   4335 C CB  . ASN A 1 543 ? 55.411 88.213  31.990  1.00 24.30 ? 543  ASN A CB  1 
ATOM   4336 C CG  . ASN A 1 543 ? 55.805 89.260  33.005  1.00 22.75 ? 543  ASN A CG  1 
ATOM   4337 O OD1 . ASN A 1 543 ? 55.084 89.481  33.956  1.00 27.56 ? 543  ASN A OD1 1 
ATOM   4338 N ND2 . ASN A 1 543 ? 56.950 89.929  32.799  1.00 20.16 ? 543  ASN A ND2 1 
ATOM   4339 N N   . THR A 1 544 ? 55.358 86.039  33.938  1.00 26.45 ? 544  THR A N   1 
ATOM   4340 C CA  . THR A 1 544 ? 55.576 85.163  35.061  1.00 27.84 ? 544  THR A CA  1 
ATOM   4341 C C   . THR A 1 544 ? 56.957 85.460  35.585  1.00 27.05 ? 544  THR A C   1 
ATOM   4342 O O   . THR A 1 544 ? 57.836 85.850  34.826  1.00 26.60 ? 544  THR A O   1 
ATOM   4343 C CB  . THR A 1 544 ? 55.517 83.711  34.584  1.00 28.78 ? 544  THR A CB  1 
ATOM   4344 O OG1 . THR A 1 544 ? 54.259 83.519  33.939  1.00 31.98 ? 544  THR A OG1 1 
ATOM   4345 C CG2 . THR A 1 544 ? 55.622 82.742  35.744  1.00 29.78 ? 544  THR A CG2 1 
ATOM   4346 N N   . ALA A 1 545 ? 57.150 85.283  36.885  1.00 26.55 ? 545  ALA A N   1 
ATOM   4347 C CA  . ALA A 1 545 ? 58.450 85.498  37.462  1.00 26.24 ? 545  ALA A CA  1 
ATOM   4348 C C   . ALA A 1 545 ? 59.382 84.309  37.191  1.00 27.84 ? 545  ALA A C   1 
ATOM   4349 O O   . ALA A 1 545 ? 59.703 83.540  38.094  1.00 27.02 ? 545  ALA A O   1 
ATOM   4350 C CB  . ALA A 1 545 ? 58.311 85.749  38.935  1.00 26.16 ? 545  ALA A CB  1 
ATOM   4351 N N   . THR A 1 546 ? 59.822 84.163  35.949  1.00 27.00 ? 546  THR A N   1 
ATOM   4352 C CA  . THR A 1 546 ? 60.823 83.155  35.606  1.00 27.61 ? 546  THR A CA  1 
ATOM   4353 C C   . THR A 1 546 ? 61.921 83.821  34.814  1.00 26.36 ? 546  THR A C   1 
ATOM   4354 O O   . THR A 1 546 ? 61.721 84.901  34.258  1.00 24.82 ? 546  THR A O   1 
ATOM   4355 C CB  . THR A 1 546 ? 60.240 81.985  34.739  1.00 27.32 ? 546  THR A CB  1 
ATOM   4356 O OG1 . THR A 1 546 ? 59.957 82.455  33.430  1.00 30.61 ? 546  THR A OG1 1 
ATOM   4357 C CG2 . THR A 1 546 ? 58.933 81.411  35.331  1.00 28.31 ? 546  THR A CG2 1 
ATOM   4358 N N   . TRP A 1 547 ? 63.064 83.150  34.729  1.00 24.75 ? 547  TRP A N   1 
ATOM   4359 C CA  . TRP A 1 547 ? 64.202 83.626  33.971  1.00 24.04 ? 547  TRP A CA  1 
ATOM   4360 C C   . TRP A 1 547 ? 63.911 83.609  32.492  1.00 24.40 ? 547  TRP A C   1 
ATOM   4361 O O   . TRP A 1 547 ? 64.466 84.451  31.747  1.00 23.64 ? 547  TRP A O   1 
ATOM   4362 C CB  . TRP A 1 547 ? 65.466 82.777  34.311  1.00 24.46 ? 547  TRP A CB  1 
ATOM   4363 C CG  . TRP A 1 547 ? 65.966 83.099  35.693  1.00 24.00 ? 547  TRP A CG  1 
ATOM   4364 C CD1 . TRP A 1 547 ? 65.558 82.515  36.879  1.00 23.78 ? 547  TRP A CD1 1 
ATOM   4365 C CD2 . TRP A 1 547 ? 66.931 84.103  36.048  1.00 24.27 ? 547  TRP A CD2 1 
ATOM   4366 N NE1 . TRP A 1 547 ? 66.240 83.091  37.938  1.00 25.34 ? 547  TRP A NE1 1 
ATOM   4367 C CE2 . TRP A 1 547 ? 67.077 84.067  37.460  1.00 23.62 ? 547  TRP A CE2 1 
ATOM   4368 C CE3 . TRP A 1 547 ? 67.667 85.048  35.315  1.00 27.26 ? 547  TRP A CE3 1 
ATOM   4369 C CZ2 . TRP A 1 547 ? 67.932 84.947  38.156  1.00 23.74 ? 547  TRP A CZ2 1 
ATOM   4370 C CZ3 . TRP A 1 547 ? 68.532 85.911  36.000  1.00 25.90 ? 547  TRP A CZ3 1 
ATOM   4371 C CH2 . TRP A 1 547 ? 68.673 85.835  37.417  1.00 23.91 ? 547  TRP A CH2 1 
ATOM   4372 N N   . ASP A 1 548 ? 63.056 82.672  32.048  1.00 22.42 ? 548  ASP A N   1 
ATOM   4373 C CA  . ASP A 1 548 ? 62.657 82.641  30.636  1.00 24.49 ? 548  ASP A CA  1 
ATOM   4374 C C   . ASP A 1 548 ? 61.883 83.940  30.293  1.00 23.40 ? 548  ASP A C   1 
ATOM   4375 O O   . ASP A 1 548 ? 62.095 84.520  29.240  1.00 23.79 ? 548  ASP A O   1 
ATOM   4376 C CB  . ASP A 1 548 ? 61.714 81.486  30.375  1.00 23.90 ? 548  ASP A CB  1 
ATOM   4377 C CG  . ASP A 1 548 ? 62.405 80.199  29.952  1.00 32.44 ? 548  ASP A CG  1 
ATOM   4378 O OD1 . ASP A 1 548 ? 63.614 80.189  29.610  1.00 32.68 ? 548  ASP A OD1 1 
ATOM   4379 O OD2 . ASP A 1 548 ? 61.664 79.184  29.949  1.00 35.21 ? 548  ASP A OD2 1 
ATOM   4380 N N   . ASP A 1 549 ? 60.975 84.356  31.176  1.00 22.45 ? 549  ASP A N   1 
ATOM   4381 C CA  . ASP A 1 549 ? 60.180 85.564  30.909  1.00 24.15 ? 549  ASP A CA  1 
ATOM   4382 C C   . ASP A 1 549 ? 61.055 86.804  30.849  1.00 23.16 ? 549  ASP A C   1 
ATOM   4383 O O   . ASP A 1 549 ? 60.790 87.715  30.041  1.00 22.63 ? 549  ASP A O   1 
ATOM   4384 C CB  . ASP A 1 549 ? 59.072 85.781  31.941  1.00 22.55 ? 549  ASP A CB  1 
ATOM   4385 C CG  . ASP A 1 549 ? 57.961 84.789  31.815  1.00 29.52 ? 549  ASP A CG  1 
ATOM   4386 O OD1 . ASP A 1 549 ? 56.800 85.179  31.448  1.00 30.17 ? 549  ASP A OD1 1 
ATOM   4387 O OD2 . ASP A 1 549 ? 58.221 83.628  32.179  1.00 32.47 ? 549  ASP A OD2 1 
ATOM   4388 N N   . LEU A 1 550 ? 62.088 86.850  31.684  1.00 23.30 ? 550  LEU A N   1 
ATOM   4389 C CA  . LEU A 1 550 ? 63.021 87.944  31.646  1.00 23.41 ? 550  LEU A CA  1 
ATOM   4390 C C   . LEU A 1 550 ? 63.702 88.026  30.262  1.00 23.39 ? 550  LEU A C   1 
ATOM   4391 O O   . LEU A 1 550 ? 63.777 89.083  29.596  1.00 23.46 ? 550  LEU A O   1 
ATOM   4392 C CB  . LEU A 1 550 ? 64.052 87.735  32.773  1.00 23.02 ? 550  LEU A CB  1 
ATOM   4393 C CG  . LEU A 1 550 ? 65.287 88.640  32.809  1.00 24.52 ? 550  LEU A CG  1 
ATOM   4394 C CD1 . LEU A 1 550 ? 64.994 90.081  32.931  1.00 24.25 ? 550  LEU A CD1 1 
ATOM   4395 C CD2 . LEU A 1 550 ? 66.154 88.271  34.013  1.00 26.09 ? 550  LEU A CD2 1 
ATOM   4396 N N   . ARG A 1 551 ? 64.257 86.897  29.833  1.00 24.01 ? 551  ARG A N   1 
ATOM   4397 C CA  . ARG A 1 551 ? 64.853 86.783  28.522  1.00 23.31 ? 551  ARG A CA  1 
ATOM   4398 C C   . ARG A 1 551 ? 63.895 87.137  27.360  1.00 23.13 ? 551  ARG A C   1 
ATOM   4399 O O   . ARG A 1 551 ? 64.287 87.832  26.448  1.00 24.37 ? 551  ARG A O   1 
ATOM   4400 C CB  . ARG A 1 551 ? 65.444 85.374  28.369  1.00 24.01 ? 551  ARG A CB  1 
ATOM   4401 C CG  . ARG A 1 551 ? 66.735 85.203  29.175  1.00 23.47 ? 551  ARG A CG  1 
ATOM   4402 C CD  . ARG A 1 551 ? 67.460 83.842  28.878  1.00 24.77 ? 551  ARG A CD  1 
ATOM   4403 N NE  . ARG A 1 551 ? 66.635 82.708  29.300  1.00 26.13 ? 551  ARG A NE  1 
ATOM   4404 C CZ  . ARG A 1 551 ? 66.703 82.082  30.475  1.00 26.75 ? 551  ARG A CZ  1 
ATOM   4405 N NH1 . ARG A 1 551 ? 67.564 82.469  31.415  1.00 30.09 ? 551  ARG A NH1 1 
ATOM   4406 N NH2 . ARG A 1 551 ? 65.881 81.065  30.713  1.00 25.78 ? 551  ARG A NH2 1 
ATOM   4407 N N   . TRP A 1 552 ? 62.650 86.671  27.407  1.00 22.70 ? 552  TRP A N   1 
ATOM   4408 C CA  . TRP A 1 552 ? 61.710 86.852  26.316  1.00 23.84 ? 552  TRP A CA  1 
ATOM   4409 C C   . TRP A 1 552 ? 61.214 88.297  26.182  1.00 23.42 ? 552  TRP A C   1 
ATOM   4410 O O   . TRP A 1 552 ? 60.699 88.697  25.132  1.00 24.53 ? 552  TRP A O   1 
ATOM   4411 C CB  . TRP A 1 552 ? 60.493 85.967  26.533  1.00 23.77 ? 552  TRP A CB  1 
ATOM   4412 C CG  . TRP A 1 552 ? 60.841 84.558  26.444  1.00 26.30 ? 552  TRP A CG  1 
ATOM   4413 C CD1 . TRP A 1 552 ? 61.963 84.015  25.865  1.00 26.93 ? 552  TRP A CD1 1 
ATOM   4414 C CD2 . TRP A 1 552 ? 60.083 83.475  26.941  1.00 28.63 ? 552  TRP A CD2 1 
ATOM   4415 N NE1 . TRP A 1 552 ? 61.949 82.658  25.995  1.00 26.10 ? 552  TRP A NE1 1 
ATOM   4416 C CE2 . TRP A 1 552 ? 60.818 82.297  26.669  1.00 26.87 ? 552  TRP A CE2 1 
ATOM   4417 C CE3 . TRP A 1 552 ? 58.866 83.378  27.635  1.00 25.83 ? 552  TRP A CE3 1 
ATOM   4418 C CZ2 . TRP A 1 552 ? 60.349 81.041  26.997  1.00 28.99 ? 552  TRP A CZ2 1 
ATOM   4419 C CZ3 . TRP A 1 552 ? 58.414 82.106  27.989  1.00 27.84 ? 552  TRP A CZ3 1 
ATOM   4420 C CH2 . TRP A 1 552 ? 59.157 80.963  27.648  1.00 25.92 ? 552  TRP A CH2 1 
ATOM   4421 N N   . SER A 1 553 ? 61.386 89.057  27.243  1.00 23.75 ? 553  SER A N   1 
ATOM   4422 C CA  . SER A 1 553 ? 61.001 90.478  27.270  1.00 24.12 ? 553  SER A CA  1 
ATOM   4423 C C   . SER A 1 553 ? 61.784 91.327  26.266  1.00 23.62 ? 553  SER A C   1 
ATOM   4424 O O   . SER A 1 553 ? 61.211 92.218  25.659  1.00 24.41 ? 553  SER A O   1 
ATOM   4425 C CB  . SER A 1 553 ? 61.115 91.044  28.677  1.00 23.63 ? 553  SER A CB  1 
ATOM   4426 O OG  . SER A 1 553 ? 62.438 91.349  29.062  1.00 24.95 ? 553  SER A OG  1 
ATOM   4427 N N   . ILE A 1 554 ? 63.081 91.050  26.083  1.00 23.93 ? 554  ILE A N   1 
ATOM   4428 C CA  . ILE A 1 554 ? 63.859 91.874  25.158  1.00 23.45 ? 554  ILE A CA  1 
ATOM   4429 C C   . ILE A 1 554 ? 63.357 91.856  23.699  1.00 23.43 ? 554  ILE A C   1 
ATOM   4430 O O   . ILE A 1 554 ? 63.135 92.908  23.147  1.00 24.52 ? 554  ILE A O   1 
ATOM   4431 C CB  . ILE A 1 554 ? 65.385 91.726  25.318  1.00 24.87 ? 554  ILE A CB  1 
ATOM   4432 C CG1 . ILE A 1 554 ? 65.792 92.071  26.761  1.00 24.37 ? 554  ILE A CG1 1 
ATOM   4433 C CG2 . ILE A 1 554 ? 66.151 92.639  24.279  1.00 20.96 ? 554  ILE A CG2 1 
ATOM   4434 C CD1 . ILE A 1 554 ? 67.337 91.827  27.045  1.00 25.37 ? 554  ILE A CD1 1 
ATOM   4435 N N   . PRO A 1 555 ? 63.168 90.675  23.066  1.00 24.29 ? 555  PRO A N   1 
ATOM   4436 C CA  . PRO A 1 555 ? 62.573 90.691  21.702  1.00 23.03 ? 555  PRO A CA  1 
ATOM   4437 C C   . PRO A 1 555 ? 61.198 91.371  21.678  1.00 22.32 ? 555  PRO A C   1 
ATOM   4438 O O   . PRO A 1 555 ? 60.859 92.020  20.694  1.00 21.77 ? 555  PRO A O   1 
ATOM   4439 C CB  . PRO A 1 555 ? 62.410 89.206  21.376  1.00 23.19 ? 555  PRO A CB  1 
ATOM   4440 C CG  . PRO A 1 555 ? 63.466 88.523  22.171  1.00 24.21 ? 555  PRO A CG  1 
ATOM   4441 C CD  . PRO A 1 555 ? 63.524 89.299  23.483  1.00 24.29 ? 555  PRO A CD  1 
ATOM   4442 N N   . GLY A 1 556 ? 60.426 91.220  22.748  1.00 22.25 ? 556  GLY A N   1 
ATOM   4443 C CA  . GLY A 1 556 ? 59.075 91.841  22.834  1.00 22.32 ? 556  GLY A CA  1 
ATOM   4444 C C   . GLY A 1 556 ? 59.122 93.369  22.774  1.00 21.79 ? 556  GLY A C   1 
ATOM   4445 O O   . GLY A 1 556 ? 58.338 94.016  22.051  1.00 22.41 ? 556  GLY A O   1 
ATOM   4446 N N   . VAL A 1 557 ? 60.035 93.962  23.535  1.00 20.37 ? 557  VAL A N   1 
ATOM   4447 C CA  . VAL A 1 557 ? 60.247 95.412  23.509  1.00 19.21 ? 557  VAL A CA  1 
ATOM   4448 C C   . VAL A 1 557 ? 60.737 95.869  22.131  1.00 19.68 ? 557  VAL A C   1 
ATOM   4449 O O   . VAL A 1 557 ? 60.242 96.850  21.568  1.00 19.07 ? 557  VAL A O   1 
ATOM   4450 C CB  . VAL A 1 557 ? 61.215 95.842  24.656  1.00 19.94 ? 557  VAL A CB  1 
ATOM   4451 C CG1 . VAL A 1 557 ? 61.817 97.303  24.452  1.00 18.45 ? 557  VAL A CG1 1 
ATOM   4452 C CG2 . VAL A 1 557 ? 60.501 95.646  26.014  1.00 20.21 ? 557  VAL A CG2 1 
ATOM   4453 N N   . LEU A 1 558 ? 61.687 95.150  21.558  1.00 19.60 ? 558  LEU A N   1 
ATOM   4454 C CA  . LEU A 1 558 ? 62.223 95.530  20.248  1.00 19.17 ? 558  LEU A CA  1 
ATOM   4455 C C   . LEU A 1 558 ? 61.217 95.488  19.161  1.00 18.48 ? 558  LEU A C   1 
ATOM   4456 O O   . LEU A 1 558 ? 61.218 96.395  18.345  1.00 18.60 ? 558  LEU A O   1 
ATOM   4457 C CB  . LEU A 1 558 ? 63.417 94.640  19.838  1.00 18.55 ? 558  LEU A CB  1 
ATOM   4458 C CG  . LEU A 1 558 ? 64.632 94.710  20.749  1.00 21.06 ? 558  LEU A CG  1 
ATOM   4459 C CD1 . LEU A 1 558 ? 65.748 93.733  20.295  1.00 20.65 ? 558  LEU A CD1 1 
ATOM   4460 C CD2 . LEU A 1 558 ? 65.144 96.170  20.828  1.00 18.26 ? 558  LEU A CD2 1 
ATOM   4461 N N   . GLU A 1 559 ? 60.344 94.462  19.158  1.00 19.18 ? 559  GLU A N   1 
ATOM   4462 C CA  . GLU A 1 559 ? 59.294 94.321  18.155  1.00 20.70 ? 559  GLU A CA  1 
ATOM   4463 C C   . GLU A 1 559 ? 58.297 95.466  18.285  1.00 19.42 ? 559  GLU A C   1 
ATOM   4464 O O   . GLU A 1 559 ? 57.905 96.008  17.283  1.00 19.25 ? 559  GLU A O   1 
ATOM   4465 C CB  . GLU A 1 559 ? 58.568 92.954  18.259  1.00 21.26 ? 559  GLU A CB  1 
ATOM   4466 C CG  . GLU A 1 559 ? 59.340 91.823  17.569  1.00 27.04 ? 559  GLU A CG  1 
ATOM   4467 C CD  . GLU A 1 559 ? 59.262 90.461  18.322  1.00 35.97 ? 559  GLU A CD  1 
ATOM   4468 O OE1 . GLU A 1 559 ? 58.439 90.380  19.283  1.00 36.31 ? 559  GLU A OE1 1 
ATOM   4469 O OE2 . GLU A 1 559 ? 59.997 89.479  17.923  1.00 34.42 ? 559  GLU A OE2 1 
ATOM   4470 N N   . PHE A 1 560 ? 57.921 95.854  19.510  1.00 18.81 ? 560  PHE A N   1 
ATOM   4471 C CA  . PHE A 1 560 ? 56.967 96.955  19.633  1.00 19.39 ? 560  PHE A CA  1 
ATOM   4472 C C   . PHE A 1 560 ? 57.565 98.286  19.217  1.00 19.42 ? 560  PHE A C   1 
ATOM   4473 O O   . PHE A 1 560 ? 56.869 99.193  18.765  1.00 20.11 ? 560  PHE A O   1 
ATOM   4474 C CB  . PHE A 1 560 ? 56.258 96.974  20.992  1.00 19.73 ? 560  PHE A CB  1 
ATOM   4475 C CG  . PHE A 1 560 ? 55.042 96.093  20.986  1.00 20.55 ? 560  PHE A CG  1 
ATOM   4476 C CD1 . PHE A 1 560 ? 55.162 94.750  21.263  1.00 22.47 ? 560  PHE A CD1 1 
ATOM   4477 C CD2 . PHE A 1 560 ? 53.810 96.587  20.584  1.00 22.57 ? 560  PHE A CD2 1 
ATOM   4478 C CE1 . PHE A 1 560 ? 54.008 93.908  21.171  1.00 25.13 ? 560  PHE A CE1 1 
ATOM   4479 C CE2 . PHE A 1 560 ? 52.667 95.757  20.469  1.00 22.18 ? 560  PHE A CE2 1 
ATOM   4480 C CZ  . PHE A 1 560 ? 52.772 94.448  20.777  1.00 23.59 ? 560  PHE A CZ  1 
ATOM   4481 N N   . ASN A 1 561 ? 58.866 98.382  19.313  1.00 19.30 ? 561  ASN A N   1 
ATOM   4482 C CA  . ASN A 1 561 ? 59.500 99.562  18.756  1.00 19.56 ? 561  ASN A CA  1 
ATOM   4483 C C   . ASN A 1 561 ? 59.417 99.602  17.226  1.00 19.73 ? 561  ASN A C   1 
ATOM   4484 O O   . ASN A 1 561 ? 59.175 100.692 16.655  1.00 21.20 ? 561  ASN A O   1 
ATOM   4485 C CB  . ASN A 1 561 ? 60.911 99.690  19.297  1.00 20.53 ? 561  ASN A CB  1 
ATOM   4486 C CG  . ASN A 1 561 ? 60.962 100.457 20.584  1.00 20.29 ? 561  ASN A CG  1 
ATOM   4487 O OD1 . ASN A 1 561 ? 61.410 101.627 20.596  1.00 21.50 ? 561  ASN A OD1 1 
ATOM   4488 N ND2 . ASN A 1 561 ? 60.498 99.843  21.684  1.00 17.37 ? 561  ASN A ND2 1 
ATOM   4489 N N   . LEU A 1 562 ? 59.539 98.457  16.537  1.00 19.86 ? 562  LEU A N   1 
ATOM   4490 C CA  . LEU A 1 562 ? 59.246 98.376  15.071  1.00 20.80 ? 562  LEU A CA  1 
ATOM   4491 C C   . LEU A 1 562 ? 57.809 98.791  14.754  1.00 21.33 ? 562  LEU A C   1 
ATOM   4492 O O   . LEU A 1 562 ? 57.531 99.441  13.764  1.00 21.18 ? 562  LEU A O   1 
ATOM   4493 C CB  . LEU A 1 562 ? 59.432 96.962  14.536  1.00 22.20 ? 562  LEU A CB  1 
ATOM   4494 C CG  . LEU A 1 562 ? 60.749 96.232  14.524  1.00 24.26 ? 562  LEU A CG  1 
ATOM   4495 C CD1 . LEU A 1 562 ? 60.534 94.881  13.787  1.00 23.40 ? 562  LEU A CD1 1 
ATOM   4496 C CD2 . LEU A 1 562 ? 61.788 97.138  13.805  1.00 21.73 ? 562  LEU A CD2 1 
ATOM   4497 N N   . PHE A 1 563 ? 56.903 98.435  15.647  1.00 20.74 ? 563  PHE A N   1 
ATOM   4498 C CA  . PHE A 1 563 ? 55.475 98.679  15.448  1.00 20.22 ? 563  PHE A CA  1 
ATOM   4499 C C   . PHE A 1 563 ? 55.036 100.123 15.745  1.00 20.28 ? 563  PHE A C   1 
ATOM   4500 O O   . PHE A 1 563 ? 53.855 100.443 15.628  1.00 22.37 ? 563  PHE A O   1 
ATOM   4501 C CB  . PHE A 1 563 ? 54.702 97.680  16.307  1.00 20.08 ? 563  PHE A CB  1 
ATOM   4502 C CG  . PHE A 1 563 ? 55.058 96.235  16.025  1.00 19.92 ? 563  PHE A CG  1 
ATOM   4503 C CD1 . PHE A 1 563 ? 55.409 95.838  14.723  1.00 18.35 ? 563  PHE A CD1 1 
ATOM   4504 C CD2 . PHE A 1 563 ? 54.949 95.274  17.045  1.00 21.65 ? 563  PHE A CD2 1 
ATOM   4505 C CE1 . PHE A 1 563 ? 55.719 94.505  14.449  1.00 20.68 ? 563  PHE A CE1 1 
ATOM   4506 C CE2 . PHE A 1 563 ? 55.191 93.946  16.792  1.00 21.59 ? 563  PHE A CE2 1 
ATOM   4507 C CZ  . PHE A 1 563 ? 55.597 93.563  15.479  1.00 21.22 ? 563  PHE A CZ  1 
ATOM   4508 N N   . GLY A 1 564 ? 55.961 100.991 16.158  1.00 20.97 ? 564  GLY A N   1 
ATOM   4509 C CA  . GLY A 1 564 ? 55.614 102.395 16.458  1.00 18.44 ? 564  GLY A CA  1 
ATOM   4510 C C   . GLY A 1 564 ? 55.013 102.561 17.834  1.00 18.38 ? 564  GLY A C   1 
ATOM   4511 O O   . GLY A 1 564 ? 54.273 103.521 18.067  1.00 19.09 ? 564  GLY A O   1 
ATOM   4512 N N   . ILE A 1 565 ? 55.251 101.586 18.721  1.00 16.43 ? 565  ILE A N   1 
ATOM   4513 C CA  . ILE A 1 565 ? 54.815 101.667 20.133  1.00 17.65 ? 565  ILE A CA  1 
ATOM   4514 C C   . ILE A 1 565 ? 56.110 101.612 20.983  1.00 18.56 ? 565  ILE A C   1 
ATOM   4515 O O   . ILE A 1 565 ? 56.393 100.624 21.595  1.00 20.11 ? 565  ILE A O   1 
ATOM   4516 C CB  . ILE A 1 565 ? 53.837 100.494 20.484  1.00 16.97 ? 565  ILE A CB  1 
ATOM   4517 C CG1 . ILE A 1 565 ? 52.756 100.457 19.411  1.00 16.99 ? 565  ILE A CG1 1 
ATOM   4518 C CG2 . ILE A 1 565 ? 53.276 100.703 21.846  1.00 22.40 ? 565  ILE A CG2 1 
ATOM   4519 C CD1 . ILE A 1 565 ? 51.745 99.384  19.551  1.00 24.21 ? 565  ILE A CD1 1 
ATOM   4520 N N   . PRO A 1 566 ? 56.915 102.681 20.971  1.00 17.92 ? 566  PRO A N   1 
ATOM   4521 C CA  . PRO A 1 566 ? 58.245 102.629 21.592  1.00 19.50 ? 566  PRO A CA  1 
ATOM   4522 C C   . PRO A 1 566 ? 58.153 102.562 23.109  1.00 20.35 ? 566  PRO A C   1 
ATOM   4523 O O   . PRO A 1 566 ? 59.085 102.038 23.748  1.00 19.49 ? 566  PRO A O   1 
ATOM   4524 C CB  . PRO A 1 566 ? 58.893 103.959 21.158  1.00 16.86 ? 566  PRO A CB  1 
ATOM   4525 C CG  . PRO A 1 566 ? 57.726 104.880 20.815  1.00 19.11 ? 566  PRO A CG  1 
ATOM   4526 C CD  . PRO A 1 566 ? 56.677 103.954 20.277  1.00 19.25 ? 566  PRO A CD  1 
ATOM   4527 N N   . MET A 1 567 ? 57.059 103.079 23.677  1.00 20.38 ? 567  MET A N   1 
ATOM   4528 C CA  . MET A 1 567 ? 56.852 103.017 25.119  1.00 23.44 ? 567  MET A CA  1 
ATOM   4529 C C   . MET A 1 567 ? 56.171 101.699 25.473  1.00 21.36 ? 567  MET A C   1 
ATOM   4530 O O   . MET A 1 567 ? 54.932 101.589 25.472  1.00 19.39 ? 567  MET A O   1 
ATOM   4531 C CB  . MET A 1 567 ? 56.063 104.215 25.664  1.00 22.38 ? 567  MET A CB  1 
ATOM   4532 C CG  . MET A 1 567 ? 56.236 104.269 27.179  1.00 28.09 ? 567  MET A CG  1 
ATOM   4533 S SD  . MET A 1 567 ? 55.723 105.800 27.958  1.00 32.56 ? 567  MET A SD  1 
ATOM   4534 C CE  . MET A 1 567 ? 57.376 106.479 28.079  1.00 35.76 ? 567  MET A CE  1 
ATOM   4535 N N   . VAL A 1 568 ? 57.005 100.696 25.750  1.00 19.40 ? 568  VAL A N   1 
ATOM   4536 C CA  . VAL A 1 568 ? 56.532 99.340  25.956  1.00 19.50 ? 568  VAL A CA  1 
ATOM   4537 C C   . VAL A 1 568 ? 57.480 98.732  26.985  1.00 19.49 ? 568  VAL A C   1 
ATOM   4538 O O   . VAL A 1 568 ? 58.650 99.082  27.046  1.00 19.63 ? 568  VAL A O   1 
ATOM   4539 C CB  . VAL A 1 568 ? 56.563 98.556  24.588  1.00 20.23 ? 568  VAL A CB  1 
ATOM   4540 C CG1 . VAL A 1 568 ? 57.960 98.623  24.026  1.00 18.20 ? 568  VAL A CG1 1 
ATOM   4541 C CG2 . VAL A 1 568 ? 56.140 97.073  24.753  1.00 20.73 ? 568  VAL A CG2 1 
ATOM   4542 N N   . GLY A 1 569 ? 56.968 97.854  27.850  1.00 20.09 ? 569  GLY A N   1 
ATOM   4543 C CA  . GLY A 1 569 ? 57.820 97.161  28.802  1.00 21.35 ? 569  GLY A CA  1 
ATOM   4544 C C   . GLY A 1 569 ? 56.980 95.993  29.320  1.00 22.64 ? 569  GLY A C   1 
ATOM   4545 O O   . GLY A 1 569 ? 55.796 95.969  29.092  1.00 23.29 ? 569  GLY A O   1 
ATOM   4546 N N   . PRO A 1 570 ? 57.592 95.000  29.980  1.00 24.27 ? 570  PRO A N   1 
ATOM   4547 C CA  . PRO A 1 570 ? 56.761 93.998  30.662  1.00 25.34 ? 570  PRO A CA  1 
ATOM   4548 C C   . PRO A 1 570 ? 56.487 94.438  32.132  1.00 27.04 ? 570  PRO A C   1 
ATOM   4549 O O   . PRO A 1 570 ? 56.869 95.545  32.562  1.00 28.71 ? 570  PRO A O   1 
ATOM   4550 C CB  . PRO A 1 570 ? 57.692 92.775  30.671  1.00 25.32 ? 570  PRO A CB  1 
ATOM   4551 C CG  . PRO A 1 570 ? 59.025 93.392  30.961  1.00 25.51 ? 570  PRO A CG  1 
ATOM   4552 C CD  . PRO A 1 570 ? 59.015 94.680  30.113  1.00 24.07 ? 570  PRO A CD  1 
ATOM   4553 N N   . ASP A 1 571 ? 55.901 93.537  32.920  1.00 28.10 ? 571  ASP A N   1 
ATOM   4554 C CA  . ASP A 1 571 ? 55.853 93.679  34.392  1.00 27.17 ? 571  ASP A CA  1 
ATOM   4555 C C   . ASP A 1 571 ? 57.224 93.267  34.920  1.00 26.12 ? 571  ASP A C   1 
ATOM   4556 O O   . ASP A 1 571 ? 57.552 92.089  34.931  1.00 25.30 ? 571  ASP A O   1 
ATOM   4557 C CB  . ASP A 1 571 ? 54.717 92.798  34.935  1.00 27.92 ? 571  ASP A CB  1 
ATOM   4558 C CG  . ASP A 1 571 ? 53.370 93.174  34.333  1.00 35.10 ? 571  ASP A CG  1 
ATOM   4559 O OD1 . ASP A 1 571 ? 53.190 94.377  33.997  1.00 41.08 ? 571  ASP A OD1 1 
ATOM   4560 O OD2 . ASP A 1 571 ? 52.468 92.307  34.194  1.00 42.96 ? 571  ASP A OD2 1 
ATOM   4561 N N   . ILE A 1 572 ? 58.037 94.248  35.318  1.00 24.36 ? 572  ILE A N   1 
ATOM   4562 C CA  . ILE A 1 572 ? 59.334 93.987  35.940  1.00 24.52 ? 572  ILE A CA  1 
ATOM   4563 C C   . ILE A 1 572 ? 59.098 93.124  37.190  1.00 25.50 ? 572  ILE A C   1 
ATOM   4564 O O   . ILE A 1 572 ? 58.150 93.367  37.967  1.00 23.77 ? 572  ILE A O   1 
ATOM   4565 C CB  . ILE A 1 572 ? 60.065 95.268  36.318  1.00 25.01 ? 572  ILE A CB  1 
ATOM   4566 C CG1 . ILE A 1 572 ? 60.408 96.087  35.073  1.00 23.60 ? 572  ILE A CG1 1 
ATOM   4567 C CG2 . ILE A 1 572 ? 61.326 94.925  37.082  1.00 24.18 ? 572  ILE A CG2 1 
ATOM   4568 C CD1 . ILE A 1 572 ? 60.987 97.490  35.487  1.00 24.11 ? 572  ILE A CD1 1 
ATOM   4569 N N   . CYS A 1 573 ? 59.959 92.109  37.318  1.00 25.15 ? 573  CYS A N   1 
ATOM   4570 C CA  . CYS A 1 573 ? 59.939 91.069  38.343  1.00 26.38 ? 573  CYS A CA  1 
ATOM   4571 C C   . CYS A 1 573 ? 58.910 89.967  38.093  1.00 26.04 ? 573  CYS A C   1 
ATOM   4572 O O   . CYS A 1 573 ? 58.961 88.914  38.737  1.00 26.07 ? 573  CYS A O   1 
ATOM   4573 C CB  . CYS A 1 573 ? 59.909 91.634  39.762  1.00 26.03 ? 573  CYS A CB  1 
ATOM   4574 S SG  . CYS A 1 573 ? 61.436 92.598  40.013  1.00 32.32 ? 573  CYS A SG  1 
ATOM   4575 N N   . GLY A 1 574 ? 57.981 90.191  37.172  1.00 23.93 ? 574  GLY A N   1 
ATOM   4576 C CA  . GLY A 1 574 ? 57.085 89.133  36.782  1.00 23.77 ? 574  GLY A CA  1 
ATOM   4577 C C   . GLY A 1 574 ? 55.785 89.237  37.547  1.00 24.79 ? 574  GLY A C   1 
ATOM   4578 O O   . GLY A 1 574 ? 55.743 89.338  38.763  1.00 25.61 ? 574  GLY A O   1 
ATOM   4579 N N   . PHE A 1 575 ? 54.708 89.258  36.804  1.00 24.99 ? 575  PHE A N   1 
ATOM   4580 C CA  . PHE A 1 575 ? 53.392 89.433  37.349  1.00 25.23 ? 575  PHE A CA  1 
ATOM   4581 C C   . PHE A 1 575 ? 52.963 88.168  38.162  1.00 26.12 ? 575  PHE A C   1 
ATOM   4582 O O   . PHE A 1 575 ? 52.743 88.250  39.363  1.00 27.24 ? 575  PHE A O   1 
ATOM   4583 C CB  . PHE A 1 575 ? 52.477 89.669  36.158  1.00 24.88 ? 575  PHE A CB  1 
ATOM   4584 C CG  . PHE A 1 575 ? 51.050 89.709  36.485  1.00 24.05 ? 575  PHE A CG  1 
ATOM   4585 C CD1 . PHE A 1 575 ? 50.480 90.861  37.010  1.00 26.53 ? 575  PHE A CD1 1 
ATOM   4586 C CD2 . PHE A 1 575 ? 50.261 88.624  36.239  1.00 28.94 ? 575  PHE A CD2 1 
ATOM   4587 C CE1 . PHE A 1 575 ? 49.136 90.912  37.277  1.00 25.10 ? 575  PHE A CE1 1 
ATOM   4588 C CE2 . PHE A 1 575 ? 48.918 88.664  36.507  1.00 27.03 ? 575  PHE A CE2 1 
ATOM   4589 C CZ  . PHE A 1 575 ? 48.368 89.824  37.024  1.00 27.50 ? 575  PHE A CZ  1 
ATOM   4590 N N   . ALA A 1 576 ? 52.911 87.015  37.514  1.00 25.91 ? 576  ALA A N   1 
ATOM   4591 C CA  . ALA A 1 576 ? 52.449 85.761  38.137  1.00 27.28 ? 576  ALA A CA  1 
ATOM   4592 C C   . ALA A 1 576 ? 53.614 85.187  38.909  1.00 27.71 ? 576  ALA A C   1 
ATOM   4593 O O   . ALA A 1 576 ? 54.728 85.248  38.431  1.00 27.54 ? 576  ALA A O   1 
ATOM   4594 C CB  . ALA A 1 576 ? 52.002 84.737  37.052  1.00 26.50 ? 576  ALA A CB  1 
ATOM   4595 N N   . LEU A 1 577 ? 53.356 84.620  40.088  1.00 28.99 ? 577  LEU A N   1 
ATOM   4596 C CA  . LEU A 1 577 ? 54.394 83.968  40.929  1.00 29.50 ? 577  LEU A CA  1 
ATOM   4597 C C   . LEU A 1 577 ? 55.141 84.911  41.884  1.00 29.96 ? 577  LEU A C   1 
ATOM   4598 O O   . LEU A 1 577 ? 55.317 86.121  41.634  1.00 27.55 ? 577  LEU A O   1 
ATOM   4599 C CB  . LEU A 1 577 ? 55.388 83.144  40.081  1.00 30.89 ? 577  LEU A CB  1 
ATOM   4600 C CG  . LEU A 1 577 ? 55.069 81.691  39.748  1.00 32.98 ? 577  LEU A CG  1 
ATOM   4601 C CD1 . LEU A 1 577 ? 53.643 81.513  39.367  1.00 33.14 ? 577  LEU A CD1 1 
ATOM   4602 C CD2 . LEU A 1 577 ? 56.016 81.113  38.697  1.00 31.11 ? 577  LEU A CD2 1 
ATOM   4603 N N   . ASP A 1 578 ? 55.572 84.343  43.007  1.00 30.80 ? 578  ASP A N   1 
ATOM   4604 C CA  . ASP A 1 578 ? 56.449 85.054  43.918  1.00 32.02 ? 578  ASP A CA  1 
ATOM   4605 C C   . ASP A 1 578 ? 57.764 85.155  43.194  1.00 31.81 ? 578  ASP A C   1 
ATOM   4606 O O   . ASP A 1 578 ? 58.229 84.159  42.641  1.00 31.90 ? 578  ASP A O   1 
ATOM   4607 C CB  . ASP A 1 578 ? 56.714 84.244  45.191  1.00 32.91 ? 578  ASP A CB  1 
ATOM   4608 C CG  . ASP A 1 578 ? 55.529 84.095  46.089  1.00 34.79 ? 578  ASP A CG  1 
ATOM   4609 O OD1 . ASP A 1 578 ? 54.481 84.783  45.967  1.00 33.74 ? 578  ASP A OD1 1 
ATOM   4610 O OD2 . ASP A 1 578 ? 55.707 83.262  46.996  1.00 40.42 ? 578  ASP A OD2 1 
ATOM   4611 N N   . THR A 1 579 ? 58.409 86.319  43.223  1.00 31.40 ? 579  THR A N   1 
ATOM   4612 C CA  . THR A 1 579 ? 59.698 86.448  42.534  1.00 30.59 ? 579  THR A CA  1 
ATOM   4613 C C   . THR A 1 579 ? 60.880 86.144  43.465  1.00 31.09 ? 579  THR A C   1 
ATOM   4614 O O   . THR A 1 579 ? 60.899 86.630  44.599  1.00 31.93 ? 579  THR A O   1 
ATOM   4615 C CB  . THR A 1 579 ? 59.833 87.887  41.934  1.00 31.06 ? 579  THR A CB  1 
ATOM   4616 O OG1 . THR A 1 579 ? 60.819 87.894  40.902  1.00 31.52 ? 579  THR A OG1 1 
ATOM   4617 C CG2 . THR A 1 579 ? 60.194 88.923  43.034  1.00 29.30 ? 579  THR A CG2 1 
ATOM   4618 N N   . PRO A 1 580 ? 61.874 85.361  43.002  1.00 30.56 ? 580  PRO A N   1 
ATOM   4619 C CA  . PRO A 1 580 ? 63.099 85.186  43.750  1.00 31.09 ? 580  PRO A CA  1 
ATOM   4620 C C   . PRO A 1 580 ? 63.895 86.491  43.785  1.00 32.06 ? 580  PRO A C   1 
ATOM   4621 O O   . PRO A 1 580 ? 63.821 87.290  42.837  1.00 32.06 ? 580  PRO A O   1 
ATOM   4622 C CB  . PRO A 1 580 ? 63.877 84.169  42.894  1.00 32.14 ? 580  PRO A CB  1 
ATOM   4623 C CG  . PRO A 1 580 ? 62.813 83.463  42.102  1.00 31.63 ? 580  PRO A CG  1 
ATOM   4624 C CD  . PRO A 1 580 ? 61.906 84.591  41.750  1.00 30.32 ? 580  PRO A CD  1 
ATOM   4625 N N   . GLU A 1 581 ? 64.667 86.708  44.842  1.00 30.76 ? 581  GLU A N   1 
ATOM   4626 C CA  . GLU A 1 581 ? 65.390 87.959  44.968  1.00 31.48 ? 581  GLU A CA  1 
ATOM   4627 C C   . GLU A 1 581 ? 66.384 88.153  43.827  1.00 30.85 ? 581  GLU A C   1 
ATOM   4628 O O   . GLU A 1 581 ? 66.519 89.267  43.342  1.00 31.34 ? 581  GLU A O   1 
ATOM   4629 C CB  . GLU A 1 581 ? 66.070 88.104  46.340  1.00 31.96 ? 581  GLU A CB  1 
ATOM   4630 C CG  . GLU A 1 581 ? 66.896 89.414  46.539  1.00 33.26 ? 581  GLU A CG  1 
ATOM   4631 C CD  . GLU A 1 581 ? 68.291 89.397  45.917  1.00 38.57 ? 581  GLU A CD  1 
ATOM   4632 O OE1 . GLU A 1 581 ? 68.765 88.295  45.506  1.00 39.06 ? 581  GLU A OE1 1 
ATOM   4633 O OE2 . GLU A 1 581 ? 68.938 90.504  45.846  1.00 37.30 ? 581  GLU A OE2 1 
ATOM   4634 N N   . GLU A 1 582 ? 67.084 87.094  43.404  1.00 28.88 ? 582  GLU A N   1 
ATOM   4635 C CA  . GLU A 1 582 ? 68.081 87.223  42.359  1.00 28.41 ? 582  GLU A CA  1 
ATOM   4636 C C   . GLU A 1 582 ? 67.407 87.606  41.018  1.00 27.56 ? 582  GLU A C   1 
ATOM   4637 O O   . GLU A 1 582 ? 67.887 88.477  40.321  1.00 26.64 ? 582  GLU A O   1 
ATOM   4638 C CB  . GLU A 1 582 ? 68.834 85.914  42.154  1.00 28.68 ? 582  GLU A CB  1 
ATOM   4639 C CG  . GLU A 1 582 ? 70.030 86.060  41.224  1.00 32.61 ? 582  GLU A CG  1 
ATOM   4640 C CD  . GLU A 1 582 ? 70.534 84.720  40.722  1.00 35.86 ? 582  GLU A CD  1 
ATOM   4641 O OE1 . GLU A 1 582 ? 70.024 83.670  41.188  1.00 38.37 ? 582  GLU A OE1 1 
ATOM   4642 O OE2 . GLU A 1 582 ? 71.401 84.716  39.831  1.00 36.15 ? 582  GLU A OE2 1 
ATOM   4643 N N   . LEU A 1 583 ? 66.307 86.939  40.672  1.00 27.12 ? 583  LEU A N   1 
ATOM   4644 C CA  . LEU A 1 583 ? 65.602 87.263  39.442  1.00 27.64 ? 583  LEU A CA  1 
ATOM   4645 C C   . LEU A 1 583 ? 65.103 88.709  39.513  1.00 27.90 ? 583  LEU A C   1 
ATOM   4646 O O   . LEU A 1 583 ? 65.311 89.472  38.591  1.00 27.69 ? 583  LEU A O   1 
ATOM   4647 C CB  . LEU A 1 583 ? 64.444 86.298  39.185  1.00 26.51 ? 583  LEU A CB  1 
ATOM   4648 C CG  . LEU A 1 583 ? 63.607 86.669  37.969  1.00 27.74 ? 583  LEU A CG  1 
ATOM   4649 C CD1 . LEU A 1 583 ? 64.482 86.603  36.688  1.00 26.44 ? 583  LEU A CD1 1 
ATOM   4650 C CD2 . LEU A 1 583 ? 62.452 85.793  37.826  1.00 24.39 ? 583  LEU A CD2 1 
ATOM   4651 N N   . CYS A 1 584 ? 64.446 89.085  40.606  1.00 29.31 ? 584  CYS A N   1 
ATOM   4652 C CA  . CYS A 1 584 ? 63.941 90.449  40.706  1.00 28.84 ? 584  CYS A CA  1 
ATOM   4653 C C   . CYS A 1 584 ? 65.052 91.532  40.673  1.00 28.29 ? 584  CYS A C   1 
ATOM   4654 O O   . CYS A 1 584 ? 64.844 92.595  40.094  1.00 27.06 ? 584  CYS A O   1 
ATOM   4655 C CB  . CYS A 1 584 ? 63.008 90.599  41.900  1.00 29.42 ? 584  CYS A CB  1 
ATOM   4656 S SG  . CYS A 1 584 ? 62.039 92.188  41.942  1.00 34.62 ? 584  CYS A SG  1 
ATOM   4657 N N   . ARG A 1 585 ? 66.221 91.251  41.263  1.00 26.26 ? 585  ARG A N   1 
ATOM   4658 C CA  . ARG A 1 585 ? 67.376 92.168  41.189  1.00 26.18 ? 585  ARG A CA  1 
ATOM   4659 C C   . ARG A 1 585 ? 67.849 92.353  39.729  1.00 25.36 ? 585  ARG A C   1 
ATOM   4660 O O   . ARG A 1 585 ? 67.990 93.469  39.286  1.00 24.22 ? 585  ARG A O   1 
ATOM   4661 C CB  . ARG A 1 585 ? 68.540 91.724  42.109  1.00 24.62 ? 585  ARG A CB  1 
ATOM   4662 C CG  . ARG A 1 585 ? 69.808 92.595  42.014  1.00 26.88 ? 585  ARG A CG  1 
ATOM   4663 C CD  . ARG A 1 585 ? 70.772 92.361  43.209  1.00 27.10 ? 585  ARG A CD  1 
ATOM   4664 N NE  . ARG A 1 585 ? 70.702 90.974  43.693  1.00 30.09 ? 585  ARG A NE  1 
ATOM   4665 C CZ  . ARG A 1 585 ? 71.334 89.943  43.117  1.00 30.10 ? 585  ARG A CZ  1 
ATOM   4666 N NH1 . ARG A 1 585 ? 72.105 90.127  42.050  1.00 30.23 ? 585  ARG A NH1 1 
ATOM   4667 N NH2 . ARG A 1 585 ? 71.207 88.728  43.615  1.00 26.09 ? 585  ARG A NH2 1 
ATOM   4668 N N   . ARG A 1 586 ? 68.070 91.250  39.001  1.00 24.92 ? 586  ARG A N   1 
ATOM   4669 C CA  . ARG A 1 586 ? 68.450 91.308  37.607  1.00 23.93 ? 586  ARG A CA  1 
ATOM   4670 C C   . ARG A 1 586 ? 67.410 92.001  36.723  1.00 23.99 ? 586  ARG A C   1 
ATOM   4671 O O   . ARG A 1 586 ? 67.770 92.725  35.802  1.00 24.05 ? 586  ARG A O   1 
ATOM   4672 C CB  . ARG A 1 586 ? 68.705 89.903  37.067  1.00 24.53 ? 586  ARG A CB  1 
ATOM   4673 C CG  . ARG A 1 586 ? 69.910 89.257  37.680  1.00 24.79 ? 586  ARG A CG  1 
ATOM   4674 C CD  . ARG A 1 586 ? 71.054 90.271  37.708  1.00 27.25 ? 586  ARG A CD  1 
ATOM   4675 N NE  . ARG A 1 586 ? 72.295 89.565  37.922  1.00 26.99 ? 586  ARG A NE  1 
ATOM   4676 C CZ  . ARG A 1 586 ? 73.504 90.096  37.950  1.00 27.13 ? 586  ARG A CZ  1 
ATOM   4677 N NH1 . ARG A 1 586 ? 73.691 91.406  37.840  1.00 22.82 ? 586  ARG A NH1 1 
ATOM   4678 N NH2 . ARG A 1 586 ? 74.528 89.286  38.128  1.00 22.40 ? 586  ARG A NH2 1 
ATOM   4679 N N   . TRP A 1 587 ? 66.144 91.720  36.999  1.00 22.51 ? 587  TRP A N   1 
ATOM   4680 C CA  . TRP A 1 587 ? 65.036 92.309  36.251  1.00 23.84 ? 587  TRP A CA  1 
ATOM   4681 C C   . TRP A 1 587 ? 64.876 93.792  36.525  1.00 22.56 ? 587  TRP A C   1 
ATOM   4682 O O   . TRP A 1 587 ? 64.539 94.540  35.608  1.00 23.35 ? 587  TRP A O   1 
ATOM   4683 C CB  . TRP A 1 587 ? 63.726 91.566  36.534  1.00 21.33 ? 587  TRP A CB  1 
ATOM   4684 C CG  . TRP A 1 587 ? 62.816 91.502  35.363  1.00 23.67 ? 587  TRP A CG  1 
ATOM   4685 C CD1 . TRP A 1 587 ? 62.728 92.391  34.312  1.00 21.65 ? 587  TRP A CD1 1 
ATOM   4686 C CD2 . TRP A 1 587 ? 61.829 90.486  35.118  1.00 22.42 ? 587  TRP A CD2 1 
ATOM   4687 N NE1 . TRP A 1 587 ? 61.784 91.946  33.416  1.00 22.01 ? 587  TRP A NE1 1 
ATOM   4688 C CE2 . TRP A 1 587 ? 61.220 90.785  33.887  1.00 19.95 ? 587  TRP A CE2 1 
ATOM   4689 C CE3 . TRP A 1 587 ? 61.494 89.287  35.766  1.00 24.95 ? 587  TRP A CE3 1 
ATOM   4690 C CZ2 . TRP A 1 587 ? 60.235 89.978  33.325  1.00 23.38 ? 587  TRP A CZ2 1 
ATOM   4691 C CZ3 . TRP A 1 587 ? 60.480 88.486  35.212  1.00 23.35 ? 587  TRP A CZ3 1 
ATOM   4692 C CH2 . TRP A 1 587 ? 59.873 88.834  34.002  1.00 22.38 ? 587  TRP A CH2 1 
ATOM   4693 N N   . MET A 1 588 ? 65.083 94.214  37.780  1.00 23.17 ? 588  MET A N   1 
ATOM   4694 C CA  . MET A 1 588 ? 65.108 95.642  38.112  1.00 23.17 ? 588  MET A CA  1 
ATOM   4695 C C   . MET A 1 588 ? 66.234 96.372  37.424  1.00 23.46 ? 588  MET A C   1 
ATOM   4696 O O   . MET A 1 588 ? 66.057 97.527  36.976  1.00 21.71 ? 588  MET A O   1 
ATOM   4697 C CB  . MET A 1 588 ? 65.082 95.923  39.639  1.00 23.91 ? 588  MET A CB  1 
ATOM   4698 C CG  . MET A 1 588 ? 63.669 95.740  40.308  1.00 22.70 ? 588  MET A CG  1 
ATOM   4699 S SD  . MET A 1 588 ? 62.480 97.007  39.738  1.00 26.00 ? 588  MET A SD  1 
ATOM   4700 C CE  . MET A 1 588 ? 63.318 98.498  40.284  1.00 24.34 ? 588  MET A CE  1 
ATOM   4701 N N   . GLN A 1 589 ? 67.394 95.705  37.307  1.00 23.31 ? 589  GLN A N   1 
ATOM   4702 C CA  . GLN A 1 589 ? 68.553 96.290  36.628  1.00 23.84 ? 589  GLN A CA  1 
ATOM   4703 C C   . GLN A 1 589 ? 68.269 96.499  35.123  1.00 23.50 ? 589  GLN A C   1 
ATOM   4704 O O   . GLN A 1 589 ? 68.480 97.606  34.574  1.00 23.10 ? 589  GLN A O   1 
ATOM   4705 C CB  . GLN A 1 589 ? 69.813 95.403  36.808  1.00 23.62 ? 589  GLN A CB  1 
ATOM   4706 C CG  . GLN A 1 589 ? 70.405 95.453  38.221  1.00 25.28 ? 589  GLN A CG  1 
ATOM   4707 C CD  . GLN A 1 589 ? 71.388 94.303  38.516  1.00 24.88 ? 589  GLN A CD  1 
ATOM   4708 O OE1 . GLN A 1 589 ? 71.576 93.405  37.695  1.00 25.78 ? 589  GLN A OE1 1 
ATOM   4709 N NE2 . GLN A 1 589 ? 71.988 94.329  39.692  1.00 25.12 ? 589  GLN A NE2 1 
ATOM   4710 N N   . LEU A 1 590 ? 67.749 95.461  34.478  1.00 22.19 ? 590  LEU A N   1 
ATOM   4711 C CA  . LEU A 1 590 ? 67.375 95.560  33.076  1.00 22.51 ? 590  LEU A CA  1 
ATOM   4712 C C   . LEU A 1 590 ? 66.243 96.556  32.967  1.00 22.24 ? 590  LEU A C   1 
ATOM   4713 O O   . LEU A 1 590 ? 66.231 97.381  32.048  1.00 22.96 ? 590  LEU A O   1 
ATOM   4714 C CB  . LEU A 1 590 ? 66.865 94.223  32.507  1.00 20.69 ? 590  LEU A CB  1 
ATOM   4715 C CG  . LEU A 1 590 ? 66.367 94.251  31.047  1.00 20.49 ? 590  LEU A CG  1 
ATOM   4716 C CD1 . LEU A 1 590 ? 67.410 94.835  30.102  1.00 22.93 ? 590  LEU A CD1 1 
ATOM   4717 C CD2 . LEU A 1 590 ? 66.000 92.863  30.610  1.00 24.87 ? 590  LEU A CD2 1 
ATOM   4718 N N   . GLY A 1 591 ? 65.310 96.446  33.910  1.00 22.10 ? 591  GLY A N   1 
ATOM   4719 C CA  . GLY A 1 591 ? 64.038 97.183  33.926  1.00 21.15 ? 591  GLY A CA  1 
ATOM   4720 C C   . GLY A 1 591 ? 64.182 98.667  34.012  1.00 20.71 ? 591  GLY A C   1 
ATOM   4721 O O   . GLY A 1 591 ? 63.334 99.402  33.537  1.00 19.82 ? 591  GLY A O   1 
ATOM   4722 N N   . ALA A 1 592 ? 65.275 99.113  34.605  1.00 18.98 ? 592  ALA A N   1 
ATOM   4723 C CA  . ALA A 1 592 ? 65.628 100.503 34.590  1.00 20.28 ? 592  ALA A CA  1 
ATOM   4724 C C   . ALA A 1 592 ? 65.819 101.014 33.185  1.00 20.34 ? 592  ALA A C   1 
ATOM   4725 O O   . ALA A 1 592 ? 65.802 102.205 32.984  1.00 19.69 ? 592  ALA A O   1 
ATOM   4726 C CB  . ALA A 1 592 ? 66.916 100.742 35.411  1.00 19.18 ? 592  ALA A CB  1 
ATOM   4727 N N   . PHE A 1 593 ? 66.018 100.114 32.216  1.00 20.41 ? 593  PHE A N   1 
ATOM   4728 C CA  . PHE A 1 593 ? 66.316 100.530 30.831  1.00 20.96 ? 593  PHE A CA  1 
ATOM   4729 C C   . PHE A 1 593 ? 65.270 100.156 29.788  1.00 20.75 ? 593  PHE A C   1 
ATOM   4730 O O   . PHE A 1 593 ? 65.488 100.364 28.587  1.00 21.91 ? 593  PHE A O   1 
ATOM   4731 C CB  . PHE A 1 593 ? 67.758 100.125 30.425  1.00 20.80 ? 593  PHE A CB  1 
ATOM   4732 C CG  . PHE A 1 593 ? 68.756 100.746 31.305  1.00 22.44 ? 593  PHE A CG  1 
ATOM   4733 C CD1 . PHE A 1 593 ? 69.155 102.076 31.089  1.00 21.30 ? 593  PHE A CD1 1 
ATOM   4734 C CD2 . PHE A 1 593 ? 69.194 100.062 32.451  1.00 22.27 ? 593  PHE A CD2 1 
ATOM   4735 C CE1 . PHE A 1 593 ? 69.991 102.694 32.024  1.00 22.18 ? 593  PHE A CE1 1 
ATOM   4736 C CE2 . PHE A 1 593 ? 70.038 100.669 33.368  1.00 20.60 ? 593  PHE A CE2 1 
ATOM   4737 C CZ  . PHE A 1 593 ? 70.434 101.991 33.147  1.00 19.85 ? 593  PHE A CZ  1 
ATOM   4738 N N   . TYR A 1 594 ? 64.127 99.608  30.231  1.00 21.39 ? 594  TYR A N   1 
ATOM   4739 C CA  . TYR A 1 594 ? 62.999 99.484  29.352  1.00 22.69 ? 594  TYR A CA  1 
ATOM   4740 C C   . TYR A 1 594 ? 62.354 100.867 29.105  1.00 24.11 ? 594  TYR A C   1 
ATOM   4741 O O   . TYR A 1 594 ? 62.283 101.681 30.033  1.00 23.62 ? 594  TYR A O   1 
ATOM   4742 C CB  . TYR A 1 594 ? 61.912 98.630  29.991  1.00 22.91 ? 594  TYR A CB  1 
ATOM   4743 C CG  . TYR A 1 594 ? 62.191 97.191  30.195  1.00 21.22 ? 594  TYR A CG  1 
ATOM   4744 C CD1 . TYR A 1 594 ? 62.669 96.390  29.157  1.00 21.01 ? 594  TYR A CD1 1 
ATOM   4745 C CD2 . TYR A 1 594 ? 61.852 96.597  31.409  1.00 25.24 ? 594  TYR A CD2 1 
ATOM   4746 C CE1 . TYR A 1 594 ? 62.820 94.978  29.336  1.00 25.04 ? 594  TYR A CE1 1 
ATOM   4747 C CE2 . TYR A 1 594 ? 62.008 95.241  31.618  1.00 26.22 ? 594  TYR A CE2 1 
ATOM   4748 C CZ  . TYR A 1 594 ? 62.501 94.438  30.594  1.00 25.88 ? 594  TYR A CZ  1 
ATOM   4749 O OH  . TYR A 1 594 ? 62.611 93.100  30.857  1.00 28.46 ? 594  TYR A OH  1 
ATOM   4750 N N   . PRO A 1 595 ? 61.825 101.109 27.873  1.00 24.58 ? 595  PRO A N   1 
ATOM   4751 C CA  . PRO A 1 595 ? 61.259 102.444 27.638  1.00 24.42 ? 595  PRO A CA  1 
ATOM   4752 C C   . PRO A 1 595 ? 60.100 102.725 28.545  1.00 24.91 ? 595  PRO A C   1 
ATOM   4753 O O   . PRO A 1 595 ? 60.056 103.817 29.113  1.00 25.94 ? 595  PRO A O   1 
ATOM   4754 C CB  . PRO A 1 595 ? 60.885 102.432 26.157  1.00 24.78 ? 595  PRO A CB  1 
ATOM   4755 C CG  . PRO A 1 595 ? 61.721 101.370 25.557  1.00 26.06 ? 595  PRO A CG  1 
ATOM   4756 C CD  . PRO A 1 595 ? 61.861 100.301 26.643  1.00 24.76 ? 595  PRO A CD  1 
ATOM   4757 N N   . PHE A 1 596 ? 59.190 101.749 28.712  1.00 23.34 ? 596  PHE A N   1 
ATOM   4758 C CA  . PHE A 1 596 ? 58.222 101.761 29.798  1.00 22.80 ? 596  PHE A CA  1 
ATOM   4759 C C   . PHE A 1 596 ? 58.717 100.902 30.979  1.00 22.23 ? 596  PHE A C   1 
ATOM   4760 O O   . PHE A 1 596 ? 58.882 99.701  30.818  1.00 23.13 ? 596  PHE A O   1 
ATOM   4761 C CB  . PHE A 1 596 ? 56.884 101.186 29.290  1.00 21.97 ? 596  PHE A CB  1 
ATOM   4762 C CG  . PHE A 1 596 ? 55.813 101.143 30.335  1.00 25.54 ? 596  PHE A CG  1 
ATOM   4763 C CD1 . PHE A 1 596 ? 55.493 102.290 31.073  1.00 26.30 ? 596  PHE A CD1 1 
ATOM   4764 C CD2 . PHE A 1 596 ? 55.109 99.961  30.574  1.00 24.59 ? 596  PHE A CD2 1 
ATOM   4765 C CE1 . PHE A 1 596 ? 54.503 102.254 32.038  1.00 27.66 ? 596  PHE A CE1 1 
ATOM   4766 C CE2 . PHE A 1 596 ? 54.120 99.907  31.573  1.00 27.75 ? 596  PHE A CE2 1 
ATOM   4767 C CZ  . PHE A 1 596 ? 53.801 101.065 32.282  1.00 25.30 ? 596  PHE A CZ  1 
ATOM   4768 N N   . SER A 1 597 ? 58.925 101.503 32.153  1.00 20.40 ? 597  SER A N   1 
ATOM   4769 C CA  . SER A 1 597 ? 59.519 100.791 33.303  1.00 21.13 ? 597  SER A CA  1 
ATOM   4770 C C   . SER A 1 597 ? 58.500 100.730 34.431  1.00 20.62 ? 597  SER A C   1 
ATOM   4771 O O   . SER A 1 597 ? 58.247 101.757 35.089  1.00 20.54 ? 597  SER A O   1 
ATOM   4772 C CB  . SER A 1 597 ? 60.733 101.606 33.752  1.00 20.50 ? 597  SER A CB  1 
ATOM   4773 O OG  . SER A 1 597 ? 61.454 100.946 34.726  1.00 24.04 ? 597  SER A OG  1 
ATOM   4774 N N   . ARG A 1 598 ? 57.843 99.576  34.584  1.00 20.33 ? 598  ARG A N   1 
ATOM   4775 C CA  . ARG A 1 598 ? 56.808 99.373  35.613  1.00 19.64 ? 598  ARG A CA  1 
ATOM   4776 C C   . ARG A 1 598 ? 57.021 98.045  36.338  1.00 19.04 ? 598  ARG A C   1 
ATOM   4777 O O   . ARG A 1 598 ? 57.097 97.028  35.694  1.00 19.00 ? 598  ARG A O   1 
ATOM   4778 C CB  . ARG A 1 598 ? 55.388 99.335  35.020  1.00 20.03 ? 598  ARG A CB  1 
ATOM   4779 C CG  . ARG A 1 598 ? 54.344 99.275  36.116  1.00 21.40 ? 598  ARG A CG  1 
ATOM   4780 C CD  . ARG A 1 598 ? 52.937 99.414  35.596  1.00 23.62 ? 598  ARG A CD  1 
ATOM   4781 N NE  . ARG A 1 598 ? 52.548 98.299  34.740  1.00 21.77 ? 598  ARG A NE  1 
ATOM   4782 C CZ  . ARG A 1 598 ? 51.289 97.992  34.482  1.00 26.85 ? 598  ARG A CZ  1 
ATOM   4783 N NH1 . ARG A 1 598 ? 50.314 98.758  34.965  1.00 27.29 ? 598  ARG A NH1 1 
ATOM   4784 N NH2 . ARG A 1 598 ? 50.996 96.961  33.716  1.00 24.24 ? 598  ARG A NH2 1 
ATOM   4785 N N   . ASN A 1 599 ? 57.167 98.093  37.650  1.00 19.68 ? 599  ASN A N   1 
ATOM   4786 C CA  . ASN A 1 599 ? 57.094 96.916  38.495  1.00 21.69 ? 599  ASN A CA  1 
ATOM   4787 C C   . ASN A 1 599 ? 55.636 96.690  38.836  1.00 21.85 ? 599  ASN A C   1 
ATOM   4788 O O   . ASN A 1 599 ? 54.982 97.566  39.367  1.00 22.71 ? 599  ASN A O   1 
ATOM   4789 C CB  . ASN A 1 599 ? 57.996 97.115  39.712  1.00 22.61 ? 599  ASN A CB  1 
ATOM   4790 C CG  . ASN A 1 599 ? 58.048 95.908  40.660  1.00 25.37 ? 599  ASN A CG  1 
ATOM   4791 O OD1 . ASN A 1 599 ? 57.013 95.300  41.014  1.00 28.55 ? 599  ASN A OD1 1 
ATOM   4792 N ND2 . ASN A 1 599 ? 59.236 95.644  41.179  1.00 23.61 ? 599  ASN A ND2 1 
ATOM   4793 N N   . HIS A 1 600 ? 55.115 95.544  38.416  1.00 22.91 ? 600  HIS A N   1 
ATOM   4794 C CA  . HIS A 1 600 ? 53.703 95.184  38.577  1.00 23.20 ? 600  HIS A CA  1 
ATOM   4795 C C   . HIS A 1 600 ? 53.630 93.720  39.027  1.00 24.32 ? 600  HIS A C   1 
ATOM   4796 O O   . HIS A 1 600 ? 54.454 92.904  38.595  1.00 26.29 ? 600  HIS A O   1 
ATOM   4797 C CB  . HIS A 1 600 ? 52.965 95.368  37.255  1.00 24.25 ? 600  HIS A CB  1 
ATOM   4798 C CG  . HIS A 1 600 ? 51.484 95.099  37.350  1.00 24.02 ? 600  HIS A CG  1 
ATOM   4799 N ND1 . HIS A 1 600 ? 50.691 95.655  38.331  1.00 24.59 ? 600  HIS A ND1 1 
ATOM   4800 C CD2 . HIS A 1 600 ? 50.655 94.363  36.571  1.00 23.90 ? 600  HIS A CD2 1 
ATOM   4801 C CE1 . HIS A 1 600 ? 49.442 95.237  38.186  1.00 24.78 ? 600  HIS A CE1 1 
ATOM   4802 N NE2 . HIS A 1 600 ? 49.393 94.452  37.121  1.00 25.20 ? 600  HIS A NE2 1 
ATOM   4803 N N   . ASN A 1 601 ? 52.673 93.369  39.890  1.00 24.54 ? 601  ASN A N   1 
ATOM   4804 C CA  . ASN A 1 601 ? 52.672 92.055  40.527  1.00 24.12 ? 601  ASN A CA  1 
ATOM   4805 C C   . ASN A 1 601 ? 51.255 91.580  40.558  1.00 24.30 ? 601  ASN A C   1 
ATOM   4806 O O   . ASN A 1 601 ? 50.335 92.403  40.629  1.00 24.97 ? 601  ASN A O   1 
ATOM   4807 C CB  . ASN A 1 601 ? 53.216 92.197  41.963  1.00 23.50 ? 601  ASN A CB  1 
ATOM   4808 C CG  . ASN A 1 601 ? 53.558 90.831  42.659  1.00 22.63 ? 601  ASN A CG  1 
ATOM   4809 O OD1 . ASN A 1 601 ? 53.586 89.764  42.055  1.00 21.16 ? 601  ASN A OD1 1 
ATOM   4810 N ND2 . ASN A 1 601 ? 53.814 90.902  43.945  1.00 21.54 ? 601  ASN A ND2 1 
ATOM   4811 N N   . GLY A 1 602 ? 51.061 90.261  40.472  1.00 25.73 ? 602  GLY A N   1 
ATOM   4812 C CA  . GLY A 1 602 ? 49.722 89.668  40.430  1.00 25.26 ? 602  GLY A CA  1 
ATOM   4813 C C   . GLY A 1 602 ? 49.078 89.571  41.816  1.00 28.12 ? 602  GLY A C   1 
ATOM   4814 O O   . GLY A 1 602 ? 49.677 89.930  42.831  1.00 28.82 ? 602  GLY A O   1 
ATOM   4815 N N   . GLN A 1 603 ? 47.833 89.122  41.848  1.00 30.79 ? 603  GLN A N   1 
ATOM   4816 C CA  . GLN A 1 603 ? 47.050 88.992  43.081  1.00 33.11 ? 603  GLN A CA  1 
ATOM   4817 C C   . GLN A 1 603 ? 47.656 87.893  43.952  1.00 33.67 ? 603  GLN A C   1 
ATOM   4818 O O   . GLN A 1 603 ? 47.880 86.776  43.488  1.00 33.96 ? 603  GLN A O   1 
ATOM   4819 C CB  . GLN A 1 603 ? 45.602 88.638  42.703  1.00 33.36 ? 603  GLN A CB  1 
ATOM   4820 C CG  . GLN A 1 603 ? 44.609 88.358  43.877  1.00 36.44 ? 603  GLN A CG  1 
ATOM   4821 C CD  . GLN A 1 603 ? 43.127 88.318  43.425  1.00 37.72 ? 603  GLN A CD  1 
ATOM   4822 O OE1 . GLN A 1 603 ? 42.740 87.591  42.496  1.00 42.22 ? 603  GLN A OE1 1 
ATOM   4823 N NE2 . GLN A 1 603 ? 42.296 89.101  44.106  1.00 44.64 ? 603  GLN A NE2 1 
ATOM   4824 N N   . GLY A 1 604 ? 47.971 88.239  45.197  1.00 34.14 ? 604  GLY A N   1 
ATOM   4825 C CA  . GLY A 1 604 ? 48.219 87.240  46.252  1.00 34.22 ? 604  GLY A CA  1 
ATOM   4826 C C   . GLY A 1 604 ? 49.668 86.893  46.482  1.00 34.02 ? 604  GLY A C   1 
ATOM   4827 O O   . GLY A 1 604 ? 49.999 86.345  47.515  1.00 35.13 ? 604  GLY A O   1 
ATOM   4828 N N   . TYR A 1 605 ? 50.539 87.249  45.532  1.00 33.02 ? 605  TYR A N   1 
ATOM   4829 C CA  . TYR A 1 605 ? 51.942 86.850  45.573  1.00 32.45 ? 605  TYR A CA  1 
ATOM   4830 C C   . TYR A 1 605 ? 52.711 87.780  46.500  1.00 32.40 ? 605  TYR A C   1 
ATOM   4831 O O   . TYR A 1 605 ? 52.260 88.881  46.755  1.00 32.15 ? 605  TYR A O   1 
ATOM   4832 C CB  . TYR A 1 605 ? 52.531 86.904  44.169  1.00 31.53 ? 605  TYR A CB  1 
ATOM   4833 C CG  . TYR A 1 605 ? 51.765 86.083  43.200  1.00 30.78 ? 605  TYR A CG  1 
ATOM   4834 C CD1 . TYR A 1 605 ? 51.707 84.701  43.330  1.00 31.30 ? 605  TYR A CD1 1 
ATOM   4835 C CD2 . TYR A 1 605 ? 51.084 86.682  42.136  1.00 28.54 ? 605  TYR A CD2 1 
ATOM   4836 C CE1 . TYR A 1 605 ? 50.988 83.915  42.397  1.00 31.51 ? 605  TYR A CE1 1 
ATOM   4837 C CE2 . TYR A 1 605 ? 50.358 85.917  41.231  1.00 32.05 ? 605  TYR A CE2 1 
ATOM   4838 C CZ  . TYR A 1 605 ? 50.324 84.531  41.371  1.00 31.90 ? 605  TYR A CZ  1 
ATOM   4839 O OH  . TYR A 1 605 ? 49.611 83.788  40.466  1.00 34.61 ? 605  TYR A OH  1 
ATOM   4840 N N   . LYS A 1 606 ? 53.876 87.341  46.975  1.00 32.22 ? 606  LYS A N   1 
ATOM   4841 C CA  . LYS A 1 606 ? 54.635 88.149  47.889  1.00 33.37 ? 606  LYS A CA  1 
ATOM   4842 C C   . LYS A 1 606 ? 55.056 89.465  47.244  1.00 32.46 ? 606  LYS A C   1 
ATOM   4843 O O   . LYS A 1 606 ? 55.245 89.554  46.019  1.00 32.60 ? 606  LYS A O   1 
ATOM   4844 C CB  . LYS A 1 606 ? 55.842 87.396  48.453  1.00 33.15 ? 606  LYS A CB  1 
ATOM   4845 C CG  . LYS A 1 606 ? 57.001 87.177  47.523  1.00 36.58 ? 606  LYS A CG  1 
ATOM   4846 C CD  . LYS A 1 606 ? 58.179 86.478  48.279  1.00 36.96 ? 606  LYS A CD  1 
ATOM   4847 C CE  . LYS A 1 606 ? 59.455 86.470  47.389  1.00 44.55 ? 606  LYS A CE  1 
ATOM   4848 N NZ  . LYS A 1 606 ? 60.399 85.284  47.548  1.00 46.29 ? 606  LYS A NZ  1 
ATOM   4849 N N   . ASP A 1 607 ? 55.208 90.474  48.074  1.00 30.91 ? 607  ASP A N   1 
ATOM   4850 C CA  . ASP A 1 607 ? 55.578 91.804  47.622  1.00 30.93 ? 607  ASP A CA  1 
ATOM   4851 C C   . ASP A 1 607 ? 56.802 91.772  46.742  1.00 29.50 ? 607  ASP A C   1 
ATOM   4852 O O   . ASP A 1 607 ? 57.725 90.990  46.993  1.00 28.95 ? 607  ASP A O   1 
ATOM   4853 C CB  . ASP A 1 607 ? 55.770 92.725  48.824  1.00 30.47 ? 607  ASP A CB  1 
ATOM   4854 C CG  . ASP A 1 607 ? 54.490 92.902  49.605  1.00 33.91 ? 607  ASP A CG  1 
ATOM   4855 O OD1 . ASP A 1 607 ? 53.421 92.507  49.061  1.00 38.61 ? 607  ASP A OD1 1 
ATOM   4856 O OD2 . ASP A 1 607 ? 54.517 93.437  50.746  1.00 36.01 ? 607  ASP A OD2 1 
ATOM   4857 N N   . GLN A 1 608 ? 56.789 92.567  45.661  1.00 28.75 ? 608  GLN A N   1 
ATOM   4858 C CA  . GLN A 1 608 ? 58.003 92.682  44.849  1.00 27.29 ? 608  GLN A CA  1 
ATOM   4859 C C   . GLN A 1 608 ? 58.426 94.128  44.528  1.00 26.73 ? 608  GLN A C   1 
ATOM   4860 O O   . GLN A 1 608 ? 59.246 94.342  43.648  1.00 25.32 ? 608  GLN A O   1 
ATOM   4861 C CB  . GLN A 1 608 ? 57.927 91.826  43.573  1.00 28.08 ? 608  GLN A CB  1 
ATOM   4862 C CG  . GLN A 1 608 ? 56.843 92.256  42.635  1.00 29.23 ? 608  GLN A CG  1 
ATOM   4863 C CD  . GLN A 1 608 ? 56.606 91.248  41.527  1.00 28.97 ? 608  GLN A CD  1 
ATOM   4864 O OE1 . GLN A 1 608 ? 56.570 90.046  41.756  1.00 29.59 ? 608  GLN A OE1 1 
ATOM   4865 N NE2 . GLN A 1 608 ? 56.412 91.740  40.324  1.00 29.64 ? 608  GLN A NE2 1 
ATOM   4866 N N   . ASP A 1 609 ? 57.856 95.102  45.241  1.00 25.38 ? 609  ASP A N   1 
ATOM   4867 C CA  . ASP A 1 609 ? 58.345 96.465  45.208  1.00 26.18 ? 609  ASP A CA  1 
ATOM   4868 C C   . ASP A 1 609 ? 59.781 96.498  45.737  1.00 26.30 ? 609  ASP A C   1 
ATOM   4869 O O   . ASP A 1 609 ? 60.125 95.741  46.638  1.00 26.51 ? 609  ASP A O   1 
ATOM   4870 C CB  . ASP A 1 609 ? 57.395 97.446  45.950  1.00 25.43 ? 609  ASP A CB  1 
ATOM   4871 C CG  . ASP A 1 609 ? 57.148 97.066  47.439  1.00 29.02 ? 609  ASP A CG  1 
ATOM   4872 O OD1 . ASP A 1 609 ? 56.331 96.135  47.722  1.00 27.34 ? 609  ASP A OD1 1 
ATOM   4873 O OD2 . ASP A 1 609 ? 57.729 97.755  48.303  1.00 28.42 ? 609  ASP A OD2 1 
ATOM   4874 N N   . PRO A 1 610 ? 60.643 97.359  45.164  1.00 25.90 ? 610  PRO A N   1 
ATOM   4875 C CA  . PRO A 1 610 ? 62.030 97.344  45.540  1.00 25.58 ? 610  PRO A CA  1 
ATOM   4876 C C   . PRO A 1 610 ? 62.277 97.457  47.041  1.00 26.32 ? 610  PRO A C   1 
ATOM   4877 O O   . PRO A 1 610 ? 63.146 96.745  47.569  1.00 27.46 ? 610  PRO A O   1 
ATOM   4878 C CB  . PRO A 1 610 ? 62.576 98.571  44.795  1.00 24.95 ? 610  PRO A CB  1 
ATOM   4879 C CG  . PRO A 1 610 ? 61.782 98.542  43.546  1.00 25.59 ? 610  PRO A CG  1 
ATOM   4880 C CD  . PRO A 1 610 ? 60.411 98.328  44.078  1.00 25.40 ? 610  PRO A CD  1 
ATOM   4881 N N   . ALA A 1 611 ? 61.547 98.340  47.726  1.00 26.21 ? 611  ALA A N   1 
ATOM   4882 C CA  . ALA A 1 611 ? 61.779 98.534  49.179  1.00 27.17 ? 611  ALA A CA  1 
ATOM   4883 C C   . ALA A 1 611 ? 61.373 97.350  50.051  1.00 27.24 ? 611  ALA A C   1 
ATOM   4884 O O   . ALA A 1 611 ? 61.870 97.213  51.187  1.00 27.79 ? 611  ALA A O   1 
ATOM   4885 C CB  . ALA A 1 611 ? 61.145 99.814  49.675  1.00 25.09 ? 611  ALA A CB  1 
ATOM   4886 N N   . SER A 1 612 ? 60.466 96.511  49.538  1.00 28.00 ? 612  SER A N   1 
ATOM   4887 C CA  . SER A 1 612 ? 60.036 95.294  50.216  1.00 28.52 ? 612  SER A CA  1 
ATOM   4888 C C   . SER A 1 612 ? 61.172 94.273  50.447  1.00 29.99 ? 612  SER A C   1 
ATOM   4889 O O   . SER A 1 612 ? 61.024 93.330  51.239  1.00 30.41 ? 612  SER A O   1 
ATOM   4890 C CB  . SER A 1 612 ? 58.868 94.646  49.459  1.00 28.44 ? 612  SER A CB  1 
ATOM   4891 O OG  . SER A 1 612 ? 59.310 93.847  48.355  1.00 28.55 ? 612  SER A OG  1 
ATOM   4892 N N   . PHE A 1 613 ? 62.299 94.449  49.757  1.00 30.53 ? 613  PHE A N   1 
ATOM   4893 C CA  . PHE A 1 613 ? 63.398 93.518  49.894  1.00 30.86 ? 613  PHE A CA  1 
ATOM   4894 C C   . PHE A 1 613 ? 64.309 93.902  51.053  1.00 32.35 ? 613  PHE A C   1 
ATOM   4895 O O   . PHE A 1 613 ? 65.192 93.144  51.434  1.00 32.84 ? 613  PHE A O   1 
ATOM   4896 C CB  . PHE A 1 613 ? 64.150 93.382  48.579  1.00 30.06 ? 613  PHE A CB  1 
ATOM   4897 C CG  . PHE A 1 613 ? 63.385 92.600  47.530  1.00 30.33 ? 613  PHE A CG  1 
ATOM   4898 C CD1 . PHE A 1 613 ? 63.533 91.206  47.429  1.00 32.94 ? 613  PHE A CD1 1 
ATOM   4899 C CD2 . PHE A 1 613 ? 62.483 93.243  46.690  1.00 29.54 ? 613  PHE A CD2 1 
ATOM   4900 C CE1 . PHE A 1 613 ? 62.804 90.472  46.483  1.00 31.52 ? 613  PHE A CE1 1 
ATOM   4901 C CE2 . PHE A 1 613 ? 61.761 92.540  45.736  1.00 31.05 ? 613  PHE A CE2 1 
ATOM   4902 C CZ  . PHE A 1 613 ? 61.923 91.150  45.621  1.00 31.54 ? 613  PHE A CZ  1 
ATOM   4903 N N   . GLY A 1 614 ? 64.085 95.075  51.631  1.00 33.45 ? 614  GLY A N   1 
ATOM   4904 C CA  . GLY A 1 614 ? 64.919 95.509  52.744  1.00 35.19 ? 614  GLY A CA  1 
ATOM   4905 C C   . GLY A 1 614 ? 65.530 96.863  52.478  1.00 36.04 ? 614  GLY A C   1 
ATOM   4906 O O   . GLY A 1 614 ? 66.183 97.072  51.441  1.00 36.44 ? 614  GLY A O   1 
ATOM   4907 N N   . ALA A 1 615 ? 65.322 97.776  53.425  1.00 36.63 ? 615  ALA A N   1 
ATOM   4908 C CA  . ALA A 1 615 ? 65.930 99.122  53.401  1.00 37.25 ? 615  ALA A CA  1 
ATOM   4909 C C   . ALA A 1 615 ? 67.423 99.162  53.023  1.00 37.74 ? 615  ALA A C   1 
ATOM   4910 O O   . ALA A 1 615 ? 67.887 100.122 52.382  1.00 38.30 ? 615  ALA A O   1 
ATOM   4911 C CB  . ALA A 1 615 ? 65.677 99.858  54.734  1.00 37.36 ? 615  ALA A CB  1 
ATOM   4912 N N   . ASP A 1 616 ? 68.184 98.144  53.407  1.00 37.92 ? 616  ASP A N   1 
ATOM   4913 C CA  . ASP A 1 616 ? 69.595 98.099  53.014  1.00 38.70 ? 616  ASP A CA  1 
ATOM   4914 C C   . ASP A 1 616 ? 69.964 96.877  52.160  1.00 37.05 ? 616  ASP A C   1 
ATOM   4915 O O   . ASP A 1 616 ? 71.116 96.455  52.117  1.00 36.97 ? 616  ASP A O   1 
ATOM   4916 C CB  . ASP A 1 616 ? 70.514 98.240  54.247  1.00 40.64 ? 616  ASP A CB  1 
ATOM   4917 C CG  . ASP A 1 616 ? 70.593 99.707  54.779  1.00 46.31 ? 616  ASP A CG  1 
ATOM   4918 O OD1 . ASP A 1 616 ? 70.564 99.918  56.024  1.00 52.80 ? 616  ASP A OD1 1 
ATOM   4919 O OD2 . ASP A 1 616 ? 70.712 100.657 53.959  1.00 51.21 ? 616  ASP A OD2 1 
ATOM   4920 N N   . SER A 1 617 ? 68.977 96.325  51.464  1.00 34.95 ? 617  SER A N   1 
ATOM   4921 C CA  . SER A 1 617 ? 69.190 95.162  50.644  1.00 33.20 ? 617  SER A CA  1 
ATOM   4922 C C   . SER A 1 617 ? 69.962 95.516  49.377  1.00 32.16 ? 617  SER A C   1 
ATOM   4923 O O   . SER A 1 617 ? 69.973 96.666  48.938  1.00 31.68 ? 617  SER A O   1 
ATOM   4924 C CB  . SER A 1 617 ? 67.852 94.526  50.303  1.00 33.94 ? 617  SER A CB  1 
ATOM   4925 O OG  . SER A 1 617 ? 67.123 95.325  49.391  1.00 31.76 ? 617  SER A OG  1 
ATOM   4926 N N   . LEU A 1 618 ? 70.625 94.519  48.811  1.00 30.88 ? 618  LEU A N   1 
ATOM   4927 C CA  . LEU A 1 618 ? 71.332 94.681  47.564  1.00 30.09 ? 618  LEU A CA  1 
ATOM   4928 C C   . LEU A 1 618 ? 70.381 95.051  46.418  1.00 28.29 ? 618  LEU A C   1 
ATOM   4929 O O   . LEU A 1 618 ? 70.757 95.834  45.572  1.00 26.36 ? 618  LEU A O   1 
ATOM   4930 C CB  . LEU A 1 618 ? 72.135 93.430  47.201  1.00 30.76 ? 618  LEU A CB  1 
ATOM   4931 C CG  . LEU A 1 618 ? 72.944 93.578  45.906  1.00 32.61 ? 618  LEU A CG  1 
ATOM   4932 C CD1 . LEU A 1 618 ? 74.095 94.627  46.004  1.00 33.27 ? 618  LEU A CD1 1 
ATOM   4933 C CD2 . LEU A 1 618 ? 73.461 92.215  45.517  1.00 33.28 ? 618  LEU A CD2 1 
ATOM   4934 N N   . LEU A 1 619 ? 69.186 94.451  46.397  1.00 27.11 ? 619  LEU A N   1 
ATOM   4935 C CA  . LEU A 1 619 ? 68.211 94.694  45.367  1.00 27.04 ? 619  LEU A CA  1 
ATOM   4936 C C   . LEU A 1 619 ? 67.805 96.152  45.419  1.00 26.99 ? 619  LEU A C   1 
ATOM   4937 O O   . LEU A 1 619 ? 67.729 96.788  44.383  1.00 26.74 ? 619  LEU A O   1 
ATOM   4938 C CB  . LEU A 1 619 ? 66.971 93.795  45.512  1.00 26.65 ? 619  LEU A CB  1 
ATOM   4939 C CG  . LEU A 1 619 ? 65.909 93.943  44.403  1.00 28.20 ? 619  LEU A CG  1 
ATOM   4940 C CD1 . LEU A 1 619 ? 65.120 92.661  44.214  1.00 24.77 ? 619  LEU A CD1 1 
ATOM   4941 C CD2 . LEU A 1 619 ? 64.914 95.040  44.779  1.00 27.70 ? 619  LEU A CD2 1 
ATOM   4942 N N   . LEU A 1 620 ? 67.553 96.687  46.616  1.00 26.58 ? 620  LEU A N   1 
ATOM   4943 C CA  . LEU A 1 620 ? 67.099 98.068  46.713  1.00 26.73 ? 620  LEU A CA  1 
ATOM   4944 C C   . LEU A 1 620 ? 68.232 99.011  46.317  1.00 27.53 ? 620  LEU A C   1 
ATOM   4945 O O   . LEU A 1 620 ? 68.013 99.948  45.572  1.00 27.90 ? 620  LEU A O   1 
ATOM   4946 C CB  . LEU A 1 620 ? 66.555 98.397  48.112  1.00 26.78 ? 620  LEU A CB  1 
ATOM   4947 C CG  . LEU A 1 620 ? 66.181 99.863  48.355  1.00 26.93 ? 620  LEU A CG  1 
ATOM   4948 C CD1 . LEU A 1 620 ? 65.040 100.323 47.419  1.00 22.07 ? 620  LEU A CD1 1 
ATOM   4949 C CD2 . LEU A 1 620 ? 65.752 100.061 49.793  1.00 27.25 ? 620  LEU A CD2 1 
ATOM   4950 N N   . ASN A 1 621 ? 69.443 98.761  46.785  1.00 26.64 ? 621  ASN A N   1 
ATOM   4951 C CA  . ASN A 1 621 ? 70.603 99.612  46.452  1.00 26.96 ? 621  ASN A CA  1 
ATOM   4952 C C   . ASN A 1 621 ? 70.886 99.647  44.948  1.00 26.98 ? 621  ASN A C   1 
ATOM   4953 O O   . ASN A 1 621 ? 71.188 100.706 44.384  1.00 26.30 ? 621  ASN A O   1 
ATOM   4954 C CB  . ASN A 1 621 ? 71.854 99.138  47.221  1.00 27.97 ? 621  ASN A CB  1 
ATOM   4955 C CG  . ASN A 1 621 ? 71.794 99.499  48.732  1.00 30.50 ? 621  ASN A CG  1 
ATOM   4956 O OD1 . ASN A 1 621 ? 71.001 100.331 49.139  1.00 36.19 ? 621  ASN A OD1 1 
ATOM   4957 N ND2 . ASN A 1 621 ? 72.643 98.893  49.533  1.00 35.42 ? 621  ASN A ND2 1 
ATOM   4958 N N   . SER A 1 622 ? 70.770 98.494  44.315  1.00 27.15 ? 622  SER A N   1 
ATOM   4959 C CA  . SER A 1 622 ? 71.084 98.337  42.911  1.00 28.93 ? 622  SER A CA  1 
ATOM   4960 C C   . SER A 1 622 ? 69.978 98.957  42.077  1.00 28.12 ? 622  SER A C   1 
ATOM   4961 O O   . SER A 1 622 ? 70.249 99.618  41.111  1.00 27.77 ? 622  SER A O   1 
ATOM   4962 C CB  . SER A 1 622 ? 71.200 96.854  42.563  1.00 29.46 ? 622  SER A CB  1 
ATOM   4963 O OG  . SER A 1 622 ? 71.684 96.749  41.234  1.00 34.04 ? 622  SER A OG  1 
ATOM   4964 N N   . SER A 1 623 ? 68.737 98.722  42.488  1.00 28.32 ? 623  SER A N   1 
ATOM   4965 C CA  . SER A 1 623 ? 67.532 99.364  41.920  1.00 28.92 ? 623  SER A CA  1 
ATOM   4966 C C   . SER A 1 623 ? 67.576 100.887 41.919  1.00 27.83 ? 623  SER A C   1 
ATOM   4967 O O   . SER A 1 623 ? 67.418 101.528 40.878  1.00 27.18 ? 623  SER A O   1 
ATOM   4968 C CB  . SER A 1 623 ? 66.286 98.894  42.666  1.00 28.61 ? 623  SER A CB  1 
ATOM   4969 O OG  . SER A 1 623 ? 66.031 97.518  42.379  1.00 32.10 ? 623  SER A OG  1 
ATOM   4970 N N   . ARG A 1 624 ? 67.753 101.474 43.094  1.00 27.06 ? 624  ARG A N   1 
ATOM   4971 C CA  . ARG A 1 624 ? 67.942 102.904 43.201  1.00 26.12 ? 624  ARG A CA  1 
ATOM   4972 C C   . ARG A 1 624 ? 69.119 103.382 42.342  1.00 25.37 ? 624  ARG A C   1 
ATOM   4973 O O   . ARG A 1 624 ? 68.991 104.369 41.660  1.00 25.88 ? 624  ARG A O   1 
ATOM   4974 C CB  . ARG A 1 624 ? 68.168 103.316 44.662  1.00 24.86 ? 624  ARG A CB  1 
ATOM   4975 C CG  . ARG A 1 624 ? 68.238 104.821 44.940  1.00 24.48 ? 624  ARG A CG  1 
ATOM   4976 C CD  . ARG A 1 624 ? 68.261 105.102 46.484  1.00 28.19 ? 624  ARG A CD  1 
ATOM   4977 N NE  . ARG A 1 624 ? 69.262 104.271 47.101  1.00 38.44 ? 624  ARG A NE  1 
ATOM   4978 C CZ  . ARG A 1 624 ? 69.103 103.472 48.146  1.00 36.23 ? 624  ARG A CZ  1 
ATOM   4979 N NH1 . ARG A 1 624 ? 67.974 103.410 48.880  1.00 33.68 ? 624  ARG A NH1 1 
ATOM   4980 N NH2 . ARG A 1 624 ? 70.146 102.764 48.476  1.00 37.05 ? 624  ARG A NH2 1 
ATOM   4981 N N   . HIS A 1 625 ? 70.234 102.671 42.367  1.00 24.06 ? 625  HIS A N   1 
ATOM   4982 C CA  . HIS A 1 625 ? 71.414 103.026 41.550  1.00 23.83 ? 625  HIS A CA  1 
ATOM   4983 C C   . HIS A 1 625 ? 71.099 103.134 40.035  1.00 21.80 ? 625  HIS A C   1 
ATOM   4984 O O   . HIS A 1 625 ? 71.425 104.131 39.397  1.00 20.19 ? 625  HIS A O   1 
ATOM   4985 C CB  . HIS A 1 625 ? 72.546 102.003 41.757  1.00 23.61 ? 625  HIS A CB  1 
ATOM   4986 C CG  . HIS A 1 625 ? 73.830 102.392 41.088  1.00 28.20 ? 625  HIS A CG  1 
ATOM   4987 N ND1 . HIS A 1 625 ? 74.288 101.790 39.929  1.00 30.82 ? 625  HIS A ND1 1 
ATOM   4988 C CD2 . HIS A 1 625 ? 74.723 103.374 41.379  1.00 29.69 ? 625  HIS A CD2 1 
ATOM   4989 C CE1 . HIS A 1 625 ? 75.414 102.366 39.551  1.00 29.75 ? 625  HIS A CE1 1 
ATOM   4990 N NE2 . HIS A 1 625 ? 75.701 103.328 40.418  1.00 35.17 ? 625  HIS A NE2 1 
ATOM   4991 N N   . TYR A 1 626 ? 70.457 102.105 39.479  1.00 21.36 ? 626  TYR A N   1 
ATOM   4992 C CA  . TYR A 1 626 ? 70.202 102.075 38.042  1.00 21.53 ? 626  TYR A CA  1 
ATOM   4993 C C   . TYR A 1 626 ? 68.990 102.926 37.653  1.00 21.20 ? 626  TYR A C   1 
ATOM   4994 O O   . TYR A 1 626 ? 68.921 103.460 36.553  1.00 22.43 ? 626  TYR A O   1 
ATOM   4995 C CB  . TYR A 1 626 ? 70.090 100.651 37.535  1.00 22.08 ? 626  TYR A CB  1 
ATOM   4996 C CG  . TYR A 1 626 ? 71.460 100.070 37.437  1.00 23.66 ? 626  TYR A CG  1 
ATOM   4997 C CD1 . TYR A 1 626 ? 71.888 99.069  38.307  1.00 24.41 ? 626  TYR A CD1 1 
ATOM   4998 C CD2 . TYR A 1 626 ? 72.371 100.610 36.554  1.00 23.14 ? 626  TYR A CD2 1 
ATOM   4999 C CE1 . TYR A 1 626 ? 73.218 98.589  38.251  1.00 21.54 ? 626  TYR A CE1 1 
ATOM   5000 C CE2 . TYR A 1 626 ? 73.669 100.166 36.514  1.00 24.23 ? 626  TYR A CE2 1 
ATOM   5001 C CZ  . TYR A 1 626 ? 74.072 99.141  37.352  1.00 23.37 ? 626  TYR A CZ  1 
ATOM   5002 O OH  . TYR A 1 626 ? 75.374 98.708  37.244  1.00 26.56 ? 626  TYR A OH  1 
ATOM   5003 N N   . LEU A 1 627 ? 68.049 103.081 38.567  1.00 20.69 ? 627  LEU A N   1 
ATOM   5004 C CA  . LEU A 1 627 ? 66.976 104.046 38.316  1.00 20.65 ? 627  LEU A CA  1 
ATOM   5005 C C   . LEU A 1 627 ? 67.511 105.477 38.344  1.00 20.89 ? 627  LEU A C   1 
ATOM   5006 O O   . LEU A 1 627 ? 67.070 106.299 37.563  1.00 22.17 ? 627  LEU A O   1 
ATOM   5007 C CB  . LEU A 1 627 ? 65.777 103.805 39.239  1.00 20.77 ? 627  LEU A CB  1 
ATOM   5008 C CG  . LEU A 1 627 ? 64.939 102.598 38.893  1.00 18.56 ? 627  LEU A CG  1 
ATOM   5009 C CD1 . LEU A 1 627 ? 63.942 102.377 40.072  1.00 19.25 ? 627  LEU A CD1 1 
ATOM   5010 C CD2 . LEU A 1 627 ? 64.235 102.788 37.509  1.00 18.31 ? 627  LEU A CD2 1 
ATOM   5011 N N   . ASN A 1 628 ? 68.478 105.786 39.206  1.00 21.74 ? 628  ASN A N   1 
ATOM   5012 C CA  . ASN A 1 628 ? 69.100 107.104 39.147  1.00 22.72 ? 628  ASN A CA  1 
ATOM   5013 C C   . ASN A 1 628 ? 69.842 107.367 37.834  1.00 22.31 ? 628  ASN A C   1 
ATOM   5014 O O   . ASN A 1 628 ? 69.822 108.504 37.299  1.00 22.11 ? 628  ASN A O   1 
ATOM   5015 C CB  . ASN A 1 628 ? 70.017 107.363 40.343  1.00 23.78 ? 628  ASN A CB  1 
ATOM   5016 C CG  . ASN A 1 628 ? 69.248 107.955 41.541  1.00 26.29 ? 628  ASN A CG  1 
ATOM   5017 O OD1 . ASN A 1 628 ? 69.390 107.478 42.672  1.00 32.04 ? 628  ASN A OD1 1 
ATOM   5018 N ND2 . ASN A 1 628 ? 68.376 108.922 41.279  1.00 24.87 ? 628  ASN A ND2 1 
ATOM   5019 N N   . ILE A 1 629 ? 70.469 106.315 37.292  1.00 22.07 ? 629  ILE A N   1 
ATOM   5020 C CA  . ILE A 1 629 ? 71.102 106.401 35.949  1.00 22.54 ? 629  ILE A CA  1 
ATOM   5021 C C   . ILE A 1 629 ? 70.056 106.628 34.877  1.00 20.79 ? 629  ILE A C   1 
ATOM   5022 O O   . ILE A 1 629 ? 70.208 107.526 34.065  1.00 21.19 ? 629  ILE A O   1 
ATOM   5023 C CB  . ILE A 1 629 ? 72.038 105.189 35.638  1.00 22.77 ? 629  ILE A CB  1 
ATOM   5024 C CG1 . ILE A 1 629 ? 73.244 105.218 36.595  1.00 22.62 ? 629  ILE A CG1 1 
ATOM   5025 C CG2 . ILE A 1 629 ? 72.387 105.143 34.124  1.00 21.66 ? 629  ILE A CG2 1 
ATOM   5026 C CD1 . ILE A 1 629 ? 74.118 103.949 36.570  1.00 24.38 ? 629  ILE A CD1 1 
ATOM   5027 N N   . ARG A 1 630 ? 68.974 105.839 34.883  1.00 20.25 ? 630  ARG A N   1 
ATOM   5028 C CA  . ARG A 1 630 ? 67.875 106.092 33.998  1.00 19.54 ? 630  ARG A CA  1 
ATOM   5029 C C   . ARG A 1 630 ? 67.403 107.544 34.074  1.00 18.89 ? 630  ARG A C   1 
ATOM   5030 O O   . ARG A 1 630 ? 67.185 108.201 33.032  1.00 17.91 ? 630  ARG A O   1 
ATOM   5031 C CB  . ARG A 1 630 ? 66.671 105.137 34.247  1.00 19.89 ? 630  ARG A CB  1 
ATOM   5032 C CG  . ARG A 1 630 ? 65.450 105.584 33.401  1.00 19.02 ? 630  ARG A CG  1 
ATOM   5033 C CD  . ARG A 1 630 ? 64.132 104.970 33.943  1.00 20.44 ? 630  ARG A CD  1 
ATOM   5034 N NE  . ARG A 1 630 ? 63.014 105.120 33.005  1.00 18.16 ? 630  ARG A NE  1 
ATOM   5035 C CZ  . ARG A 1 630 ? 62.797 104.282 31.996  1.00 18.37 ? 630  ARG A CZ  1 
ATOM   5036 N NH1 . ARG A 1 630 ? 63.643 103.263 31.761  1.00 18.77 ? 630  ARG A NH1 1 
ATOM   5037 N NH2 . ARG A 1 630 ? 61.767 104.484 31.190  1.00 18.07 ? 630  ARG A NH2 1 
ATOM   5038 N N   . TYR A 1 631 ? 67.248 108.069 35.288  1.00 18.48 ? 631  TYR A N   1 
ATOM   5039 C CA  . TYR A 1 631 ? 66.716 109.414 35.424  1.00 19.73 ? 631  TYR A CA  1 
ATOM   5040 C C   . TYR A 1 631 ? 67.776 110.419 34.921  1.00 20.26 ? 631  TYR A C   1 
ATOM   5041 O O   . TYR A 1 631 ? 67.451 111.455 34.353  1.00 21.17 ? 631  TYR A O   1 
ATOM   5042 C CB  . TYR A 1 631 ? 66.317 109.712 36.896  1.00 19.74 ? 631  TYR A CB  1 
ATOM   5043 C CG  . TYR A 1 631 ? 64.885 109.302 37.218  1.00 21.43 ? 631  TYR A CG  1 
ATOM   5044 C CD1 . TYR A 1 631 ? 64.424 108.029 36.902  1.00 24.10 ? 631  TYR A CD1 1 
ATOM   5045 C CD2 . TYR A 1 631 ? 64.009 110.193 37.844  1.00 23.09 ? 631  TYR A CD2 1 
ATOM   5046 C CE1 . TYR A 1 631 ? 63.150 107.638 37.164  1.00 23.28 ? 631  TYR A CE1 1 
ATOM   5047 C CE2 . TYR A 1 631 ? 62.693 109.826 38.110  1.00 21.07 ? 631  TYR A CE2 1 
ATOM   5048 C CZ  . TYR A 1 631 ? 62.282 108.565 37.793  1.00 21.66 ? 631  TYR A CZ  1 
ATOM   5049 O OH  . TYR A 1 631 ? 61.021 108.177 38.077  1.00 21.32 ? 631  TYR A OH  1 
ATOM   5050 N N   . THR A 1 632 ? 69.047 110.139 35.129  1.00 20.30 ? 632  THR A N   1 
ATOM   5051 C CA  . THR A 1 632 ? 70.085 111.051 34.692  1.00 20.08 ? 632  THR A CA  1 
ATOM   5052 C C   . THR A 1 632 ? 70.003 111.180 33.146  1.00 20.57 ? 632  THR A C   1 
ATOM   5053 O O   . THR A 1 632 ? 70.261 112.251 32.582  1.00 20.63 ? 632  THR A O   1 
ATOM   5054 C CB  . THR A 1 632 ? 71.444 110.480 35.070  1.00 21.54 ? 632  THR A CB  1 
ATOM   5055 O OG1 . THR A 1 632 ? 71.516 110.385 36.499  1.00 22.56 ? 632  THR A OG1 1 
ATOM   5056 C CG2 . THR A 1 632 ? 72.573 111.369 34.568  1.00 22.26 ? 632  THR A CG2 1 
ATOM   5057 N N   . LEU A 1 633 ? 69.620 110.092 32.497  1.00 19.23 ? 633  LEU A N   1 
ATOM   5058 C CA  . LEU A 1 633 ? 69.640 109.995 31.036  1.00 20.77 ? 633  LEU A CA  1 
ATOM   5059 C C   . LEU A 1 633 ? 68.291 110.304 30.456  1.00 18.62 ? 633  LEU A C   1 
ATOM   5060 O O   . LEU A 1 633 ? 68.071 110.111 29.285  1.00 19.17 ? 633  LEU A O   1 
ATOM   5061 C CB  . LEU A 1 633 ? 70.104 108.597 30.576  1.00 20.15 ? 633  LEU A CB  1 
ATOM   5062 C CG  . LEU A 1 633 ? 71.603 108.330 30.859  1.00 24.04 ? 633  LEU A CG  1 
ATOM   5063 C CD1 . LEU A 1 633 ? 71.915 106.888 30.579  1.00 24.18 ? 633  LEU A CD1 1 
ATOM   5064 C CD2 . LEU A 1 633 ? 72.460 109.197 30.001  1.00 25.72 ? 633  LEU A CD2 1 
ATOM   5065 N N   . LEU A 1 634 ? 67.367 110.788 31.268  1.00 19.77 ? 634  LEU A N   1 
ATOM   5066 C CA  . LEU A 1 634 ? 66.067 111.116 30.724  1.00 20.20 ? 634  LEU A CA  1 
ATOM   5067 C C   . LEU A 1 634 ? 66.069 112.126 29.591  1.00 19.71 ? 634  LEU A C   1 
ATOM   5068 O O   . LEU A 1 634 ? 65.275 111.996 28.680  1.00 21.02 ? 634  LEU A O   1 
ATOM   5069 C CB  . LEU A 1 634 ? 65.036 111.470 31.835  1.00 20.10 ? 634  LEU A CB  1 
ATOM   5070 C CG  . LEU A 1 634 ? 64.407 110.307 32.618  1.00 22.97 ? 634  LEU A CG  1 
ATOM   5071 C CD1 . LEU A 1 634 ? 63.308 110.870 33.542  1.00 26.05 ? 634  LEU A CD1 1 
ATOM   5072 C CD2 . LEU A 1 634 ? 63.818 109.165 31.790  1.00 23.70 ? 634  LEU A CD2 1 
ATOM   5073 N N   . PRO A 1 635 ? 66.890 113.196 29.651  1.00 19.81 ? 635  PRO A N   1 
ATOM   5074 C CA  . PRO A 1 635 ? 66.921 114.070 28.439  1.00 19.56 ? 635  PRO A CA  1 
ATOM   5075 C C   . PRO A 1 635 ? 67.290 113.395 27.129  1.00 18.40 ? 635  PRO A C   1 
ATOM   5076 O O   . PRO A 1 635 ? 66.784 113.762 26.087  1.00 17.71 ? 635  PRO A O   1 
ATOM   5077 C CB  . PRO A 1 635 ? 67.999 115.121 28.783  1.00 19.97 ? 635  PRO A CB  1 
ATOM   5078 C CG  . PRO A 1 635 ? 67.903 115.215 30.286  1.00 20.58 ? 635  PRO A CG  1 
ATOM   5079 C CD  . PRO A 1 635 ? 67.665 113.786 30.759  1.00 19.70 ? 635  PRO A CD  1 
ATOM   5080 N N   . TYR A 1 636 ? 68.171 112.420 27.182  1.00 18.33 ? 636  TYR A N   1 
ATOM   5081 C CA  . TYR A 1 636 ? 68.550 111.637 26.013  1.00 19.30 ? 636  TYR A CA  1 
ATOM   5082 C C   . TYR A 1 636 ? 67.393 110.721 25.609  1.00 18.89 ? 636  TYR A C   1 
ATOM   5083 O O   . TYR A 1 636 ? 66.996 110.676 24.427  1.00 18.52 ? 636  TYR A O   1 
ATOM   5084 C CB  . TYR A 1 636 ? 69.817 110.798 26.355  1.00 20.27 ? 636  TYR A CB  1 
ATOM   5085 C CG  . TYR A 1 636 ? 70.212 109.773 25.299  1.00 20.39 ? 636  TYR A CG  1 
ATOM   5086 C CD1 . TYR A 1 636 ? 70.609 110.174 24.038  1.00 21.51 ? 636  TYR A CD1 1 
ATOM   5087 C CD2 . TYR A 1 636 ? 70.225 108.408 25.591  1.00 20.76 ? 636  TYR A CD2 1 
ATOM   5088 C CE1 . TYR A 1 636 ? 70.965 109.227 23.064  1.00 21.15 ? 636  TYR A CE1 1 
ATOM   5089 C CE2 . TYR A 1 636 ? 70.625 107.467 24.651  1.00 19.51 ? 636  TYR A CE2 1 
ATOM   5090 C CZ  . TYR A 1 636 ? 70.971 107.898 23.384  1.00 21.13 ? 636  TYR A CZ  1 
ATOM   5091 O OH  . TYR A 1 636 ? 71.382 106.994 22.418  1.00 25.36 ? 636  TYR A OH  1 
ATOM   5092 N N   . LEU A 1 637 ? 66.790 110.044 26.586  1.00 19.38 ? 637  LEU A N   1 
ATOM   5093 C CA  . LEU A 1 637 ? 65.647 109.162 26.276  1.00 17.41 ? 637  LEU A CA  1 
ATOM   5094 C C   . LEU A 1 637 ? 64.472 109.979 25.698  1.00 17.88 ? 637  LEU A C   1 
ATOM   5095 O O   . LEU A 1 637 ? 63.819 109.594 24.747  1.00 17.71 ? 637  LEU A O   1 
ATOM   5096 C CB  . LEU A 1 637 ? 65.153 108.483 27.558  1.00 17.55 ? 637  LEU A CB  1 
ATOM   5097 C CG  . LEU A 1 637 ? 64.072 107.432 27.329  1.00 17.33 ? 637  LEU A CG  1 
ATOM   5098 C CD1 . LEU A 1 637 ? 64.554 106.278 26.409  1.00 15.74 ? 637  LEU A CD1 1 
ATOM   5099 C CD2 . LEU A 1 637 ? 63.747 106.839 28.645  1.00 19.66 ? 637  LEU A CD2 1 
ATOM   5100 N N   . TYR A 1 638 ? 64.181 111.107 26.318  1.00 16.78 ? 638  TYR A N   1 
ATOM   5101 C CA  . TYR A 1 638 ? 63.106 111.970 25.804  1.00 16.96 ? 638  TYR A CA  1 
ATOM   5102 C C   . TYR A 1 638 ? 63.364 112.454 24.393  1.00 17.76 ? 638  TYR A C   1 
ATOM   5103 O O   . TYR A 1 638 ? 62.468 112.582 23.597  1.00 17.77 ? 638  TYR A O   1 
ATOM   5104 C CB  . TYR A 1 638 ? 62.971 113.161 26.744  1.00 17.57 ? 638  TYR A CB  1 
ATOM   5105 C CG  . TYR A 1 638 ? 61.748 114.014 26.528  1.00 18.98 ? 638  TYR A CG  1 
ATOM   5106 C CD1 . TYR A 1 638 ? 60.449 113.443 26.583  1.00 19.19 ? 638  TYR A CD1 1 
ATOM   5107 C CD2 . TYR A 1 638 ? 61.871 115.398 26.377  1.00 18.23 ? 638  TYR A CD2 1 
ATOM   5108 C CE1 . TYR A 1 638 ? 59.323 114.247 26.461  1.00 21.21 ? 638  TYR A CE1 1 
ATOM   5109 C CE2 . TYR A 1 638 ? 60.728 116.211 26.252  1.00 17.85 ? 638  TYR A CE2 1 
ATOM   5110 C CZ  . TYR A 1 638 ? 59.476 115.626 26.297  1.00 19.94 ? 638  TYR A CZ  1 
ATOM   5111 O OH  . TYR A 1 638 ? 58.323 116.438 26.167  1.00 21.27 ? 638  TYR A OH  1 
ATOM   5112 N N   . THR A 1 639 ? 64.607 112.795 24.087  1.00 18.23 ? 639  THR A N   1 
ATOM   5113 C CA  . THR A 1 639 ? 64.936 113.185 22.736  1.00 18.39 ? 639  THR A CA  1 
ATOM   5114 C C   . THR A 1 639 ? 64.755 112.045 21.733  1.00 16.91 ? 639  THR A C   1 
ATOM   5115 O O   . THR A 1 639 ? 64.430 112.288 20.601  1.00 18.72 ? 639  THR A O   1 
ATOM   5116 C CB  . THR A 1 639 ? 66.388 113.729 22.663  1.00 18.45 ? 639  THR A CB  1 
ATOM   5117 O OG1 . THR A 1 639 ? 66.509 114.799 23.605  1.00 19.16 ? 639  THR A OG1 1 
ATOM   5118 C CG2 . THR A 1 639 ? 66.706 114.305 21.228  1.00 19.75 ? 639  THR A CG2 1 
ATOM   5119 N N   . LEU A 1 640 ? 64.997 110.812 22.143  1.00 16.45 ? 640  LEU A N   1 
ATOM   5120 C CA  . LEU A 1 640 ? 64.764 109.671 21.278  1.00 17.10 ? 640  LEU A CA  1 
ATOM   5121 C C   . LEU A 1 640 ? 63.295 109.537 20.996  1.00 17.13 ? 640  LEU A C   1 
ATOM   5122 O O   . LEU A 1 640 ? 62.891 109.221 19.881  1.00 17.55 ? 640  LEU A O   1 
ATOM   5123 C CB  . LEU A 1 640 ? 65.292 108.385 21.951  1.00 16.71 ? 640  LEU A CB  1 
ATOM   5124 C CG  . LEU A 1 640 ? 66.818 108.296 22.115  1.00 18.47 ? 640  LEU A CG  1 
ATOM   5125 C CD1 . LEU A 1 640 ? 67.156 106.948 22.774  1.00 17.49 ? 640  LEU A CD1 1 
ATOM   5126 C CD2 . LEU A 1 640 ? 67.523 108.435 20.754  1.00 21.69 ? 640  LEU A CD2 1 
ATOM   5127 N N   . PHE A 1 641 ? 62.491 109.780 22.023  1.00 17.31 ? 641  PHE A N   1 
ATOM   5128 C CA  . PHE A 1 641 ? 61.011 109.770 21.831  1.00 18.32 ? 641  PHE A CA  1 
ATOM   5129 C C   . PHE A 1 641 ? 60.556 110.893 20.917  1.00 17.94 ? 641  PHE A C   1 
ATOM   5130 O O   . PHE A 1 641 ? 59.638 110.714 20.177  1.00 18.89 ? 641  PHE A O   1 
ATOM   5131 C CB  . PHE A 1 641 ? 60.276 109.865 23.161  1.00 18.95 ? 641  PHE A CB  1 
ATOM   5132 C CG  . PHE A 1 641 ? 60.080 108.532 23.818  1.00 18.83 ? 641  PHE A CG  1 
ATOM   5133 C CD1 . PHE A 1 641 ? 59.077 107.658 23.373  1.00 16.79 ? 641  PHE A CD1 1 
ATOM   5134 C CD2 . PHE A 1 641 ? 60.892 108.155 24.866  1.00 18.10 ? 641  PHE A CD2 1 
ATOM   5135 C CE1 . PHE A 1 641 ? 58.924 106.407 23.981  1.00 16.52 ? 641  PHE A CE1 1 
ATOM   5136 C CE2 . PHE A 1 641 ? 60.742 106.924 25.474  1.00 19.45 ? 641  PHE A CE2 1 
ATOM   5137 C CZ  . PHE A 1 641 ? 59.752 106.034 25.024  1.00 17.87 ? 641  PHE A CZ  1 
ATOM   5138 N N   . PHE A 1 642 ? 61.180 112.058 21.011  1.00 18.64 ? 642  PHE A N   1 
ATOM   5139 C CA  . PHE A 1 642 ? 60.929 113.135 20.086  1.00 19.18 ? 642  PHE A CA  1 
ATOM   5140 C C   . PHE A 1 642 ? 61.211 112.696 18.651  1.00 19.21 ? 642  PHE A C   1 
ATOM   5141 O O   . PHE A 1 642 ? 60.458 112.982 17.720  1.00 20.75 ? 642  PHE A O   1 
ATOM   5142 C CB  . PHE A 1 642 ? 61.865 114.332 20.424  1.00 18.99 ? 642  PHE A CB  1 
ATOM   5143 C CG  . PHE A 1 642 ? 61.927 115.316 19.314  1.00 22.16 ? 642  PHE A CG  1 
ATOM   5144 C CD1 . PHE A 1 642 ? 60.737 116.021 18.907  1.00 19.58 ? 642  PHE A CD1 1 
ATOM   5145 C CD2 . PHE A 1 642 ? 63.126 115.518 18.628  1.00 20.55 ? 642  PHE A CD2 1 
ATOM   5146 C CE1 . PHE A 1 642 ? 60.799 116.958 17.808  1.00 22.57 ? 642  PHE A CE1 1 
ATOM   5147 C CE2 . PHE A 1 642 ? 63.203 116.431 17.535  1.00 23.18 ? 642  PHE A CE2 1 
ATOM   5148 C CZ  . PHE A 1 642 ? 62.052 117.153 17.130  1.00 22.01 ? 642  PHE A CZ  1 
ATOM   5149 N N   . ARG A 1 643 ? 62.316 111.994 18.443  1.00 19.43 ? 643  ARG A N   1 
ATOM   5150 C CA  . ARG A 1 643 ? 62.631 111.526 17.077  1.00 19.00 ? 643  ARG A CA  1 
ATOM   5151 C C   . ARG A 1 643 ? 61.682 110.432 16.616  1.00 17.72 ? 643  ARG A C   1 
ATOM   5152 O O   . ARG A 1 643 ? 61.342 110.384 15.445  1.00 18.24 ? 643  ARG A O   1 
ATOM   5153 C CB  . ARG A 1 643 ? 64.068 111.066 17.005  1.00 18.73 ? 643  ARG A CB  1 
ATOM   5154 C CG  . ARG A 1 643 ? 65.099 112.268 17.158  1.00 19.31 ? 643  ARG A CG  1 
ATOM   5155 C CD  . ARG A 1 643 ? 64.962 113.297 16.061  1.00 24.13 ? 643  ARG A CD  1 
ATOM   5156 N NE  . ARG A 1 643 ? 66.156 114.165 15.949  1.00 28.43 ? 643  ARG A NE  1 
ATOM   5157 C CZ  . ARG A 1 643 ? 66.232 115.212 15.134  1.00 29.22 ? 643  ARG A CZ  1 
ATOM   5158 N NH1 . ARG A 1 643 ? 65.226 115.508 14.358  1.00 30.89 ? 643  ARG A NH1 1 
ATOM   5159 N NH2 . ARG A 1 643 ? 67.332 115.949 15.065  1.00 34.40 ? 643  ARG A NH2 1 
ATOM   5160 N N   . ALA A 1 644 ? 61.219 109.584 17.542  1.00 17.80 ? 644  ALA A N   1 
ATOM   5161 C CA  . ALA A 1 644 ? 60.188 108.575 17.188  1.00 17.19 ? 644  ALA A CA  1 
ATOM   5162 C C   . ALA A 1 644 ? 58.917 109.276 16.733  1.00 17.86 ? 644  ALA A C   1 
ATOM   5163 O O   . ALA A 1 644 ? 58.294 108.905 15.747  1.00 18.78 ? 644  ALA A O   1 
ATOM   5164 C CB  . ALA A 1 644 ? 59.888 107.650 18.427  1.00 16.26 ? 644  ALA A CB  1 
ATOM   5165 N N   . HIS A 1 645 ? 58.534 110.282 17.496  1.00 18.55 ? 645  HIS A N   1 
ATOM   5166 C CA  . HIS A 1 645 ? 57.321 111.001 17.264  1.00 19.44 ? 645  HIS A CA  1 
ATOM   5167 C C   . HIS A 1 645 ? 57.386 111.832 15.978  1.00 19.60 ? 645  HIS A C   1 
ATOM   5168 O O   . HIS A 1 645 ? 56.421 111.856 15.220  1.00 19.70 ? 645  HIS A O   1 
ATOM   5169 C CB  . HIS A 1 645 ? 57.020 111.901 18.469  1.00 18.52 ? 645  HIS A CB  1 
ATOM   5170 C CG  . HIS A 1 645 ? 55.856 112.823 18.236  1.00 24.26 ? 645  HIS A CG  1 
ATOM   5171 N ND1 . HIS A 1 645 ? 54.579 112.352 17.996  1.00 24.57 ? 645  HIS A ND1 1 
ATOM   5172 C CD2 . HIS A 1 645 ? 55.773 114.180 18.197  1.00 25.45 ? 645  HIS A CD2 1 
ATOM   5173 C CE1 . HIS A 1 645 ? 53.758 113.376 17.818  1.00 27.92 ? 645  HIS A CE1 1 
ATOM   5174 N NE2 . HIS A 1 645 ? 54.453 114.494 17.945  1.00 29.56 ? 645  HIS A NE2 1 
ATOM   5175 N N   . SER A 1 646 ? 58.534 112.476 15.721  1.00 20.63 ? 646  SER A N   1 
ATOM   5176 C CA  . SER A 1 646 ? 58.621 113.423 14.621  1.00 21.64 ? 646  SER A CA  1 
ATOM   5177 C C   . SER A 1 646 ? 59.164 112.819 13.340  1.00 21.64 ? 646  SER A C   1 
ATOM   5178 O O   . SER A 1 646 ? 58.847 113.280 12.266  1.00 21.40 ? 646  SER A O   1 
ATOM   5179 C CB  . SER A 1 646 ? 59.485 114.605 15.019  1.00 21.07 ? 646  SER A CB  1 
ATOM   5180 O OG  . SER A 1 646 ? 60.783 114.128 15.379  1.00 23.41 ? 646  SER A OG  1 
ATOM   5181 N N   . ARG A 1 647 ? 59.989 111.794 13.465  1.00 21.35 ? 647  ARG A N   1 
ATOM   5182 C CA  . ARG A 1 647 ? 60.680 111.246 12.315  1.00 22.10 ? 647  ARG A CA  1 
ATOM   5183 C C   . ARG A 1 647 ? 60.384 109.775 12.120  1.00 20.88 ? 647  ARG A C   1 
ATOM   5184 O O   . ARG A 1 647 ? 60.476 109.239 10.999  1.00 21.63 ? 647  ARG A O   1 
ATOM   5185 C CB  . ARG A 1 647 ? 62.187 111.424 12.548  1.00 23.08 ? 647  ARG A CB  1 
ATOM   5186 C CG  . ARG A 1 647 ? 63.018 111.166 11.327  1.00 25.69 ? 647  ARG A CG  1 
ATOM   5187 C CD  . ARG A 1 647 ? 64.361 111.887 11.496  1.00 26.85 ? 647  ARG A CD  1 
ATOM   5188 N NE  . ARG A 1 647 ? 65.171 111.220 12.497  1.00 26.20 ? 647  ARG A NE  1 
ATOM   5189 C CZ  . ARG A 1 647 ? 66.321 111.686 12.977  1.00 28.54 ? 647  ARG A CZ  1 
ATOM   5190 N NH1 . ARG A 1 647 ? 66.799 112.838 12.532  1.00 29.87 ? 647  ARG A NH1 1 
ATOM   5191 N NH2 . ARG A 1 647 ? 66.988 111.006 13.897  1.00 26.41 ? 647  ARG A NH2 1 
ATOM   5192 N N   . GLY A 1 648 ? 60.048 109.086 13.211  1.00 20.87 ? 648  GLY A N   1 
ATOM   5193 C CA  . GLY A 1 648 ? 59.705 107.662 13.120  1.00 21.96 ? 648  GLY A CA  1 
ATOM   5194 C C   . GLY A 1 648 ? 60.832 106.706 13.570  1.00 22.61 ? 648  GLY A C   1 
ATOM   5195 O O   . GLY A 1 648 ? 60.714 105.513 13.389  1.00 25.16 ? 648  GLY A O   1 
ATOM   5196 N N   . ASP A 1 649 ? 61.924 107.205 14.123  1.00 23.33 ? 649  ASP A N   1 
ATOM   5197 C CA  . ASP A 1 649 ? 63.010 106.355 14.690  1.00 23.96 ? 649  ASP A CA  1 
ATOM   5198 C C   . ASP A 1 649 ? 62.558 105.355 15.786  1.00 24.07 ? 649  ASP A C   1 
ATOM   5199 O O   . ASP A 1 649 ? 61.628 105.636 16.502  1.00 27.75 ? 649  ASP A O   1 
ATOM   5200 C CB  . ASP A 1 649 ? 64.076 107.269 15.366  1.00 24.00 ? 649  ASP A CB  1 
ATOM   5201 C CG  . ASP A 1 649 ? 64.753 108.261 14.409  1.00 29.00 ? 649  ASP A CG  1 
ATOM   5202 O OD1 . ASP A 1 649 ? 64.140 108.660 13.396  1.00 29.29 ? 649  ASP A OD1 1 
ATOM   5203 O OD2 . ASP A 1 649 ? 65.916 108.702 14.712  1.00 30.63 ? 649  ASP A OD2 1 
ATOM   5204 N N   . THR A 1 650 ? 63.249 104.222 16.008  1.00 23.60 ? 650  THR A N   1 
ATOM   5205 C CA  . THR A 1 650 ? 62.961 103.381 17.189  1.00 22.00 ? 650  THR A CA  1 
ATOM   5206 C C   . THR A 1 650 ? 63.572 104.055 18.426  1.00 21.54 ? 650  THR A C   1 
ATOM   5207 O O   . THR A 1 650 ? 64.453 104.919 18.308  1.00 19.78 ? 650  THR A O   1 
ATOM   5208 C CB  . THR A 1 650 ? 63.607 101.967 17.026  1.00 22.10 ? 650  THR A CB  1 
ATOM   5209 O OG1 . THR A 1 650 ? 64.987 102.163 16.638  1.00 23.29 ? 650  THR A OG1 1 
ATOM   5210 C CG2 . THR A 1 650 ? 62.928 101.197 15.899  1.00 23.38 ? 650  THR A CG2 1 
ATOM   5211 N N   . VAL A 1 651 ? 63.134 103.663 19.613  1.00 18.68 ? 651  VAL A N   1 
ATOM   5212 C CA  . VAL A 1 651 ? 63.746 104.158 20.840  1.00 19.05 ? 651  VAL A CA  1 
ATOM   5213 C C   . VAL A 1 651 ? 64.617 103.032 21.429  1.00 19.26 ? 651  VAL A C   1 
ATOM   5214 O O   . VAL A 1 651 ? 65.812 103.179 21.510  1.00 19.80 ? 651  VAL A O   1 
ATOM   5215 C CB  . VAL A 1 651 ? 62.713 104.629 21.832  1.00 16.83 ? 651  VAL A CB  1 
ATOM   5216 C CG1 . VAL A 1 651 ? 63.304 104.916 23.221  1.00 18.36 ? 651  VAL A CG1 1 
ATOM   5217 C CG2 . VAL A 1 651 ? 61.960 105.860 21.247  1.00 20.66 ? 651  VAL A CG2 1 
ATOM   5218 N N   . ALA A 1 652 ? 64.029 101.910 21.836  1.00 19.10 ? 652  ALA A N   1 
ATOM   5219 C CA  . ALA A 1 652 ? 64.874 100.755 22.183  1.00 18.85 ? 652  ALA A CA  1 
ATOM   5220 C C   . ALA A 1 652 ? 65.137 100.086 20.801  1.00 19.97 ? 652  ALA A C   1 
ATOM   5221 O O   . ALA A 1 652 ? 64.215 99.810  20.023  1.00 19.80 ? 652  ALA A O   1 
ATOM   5222 C CB  . ALA A 1 652 ? 64.167 99.800  23.133  1.00 18.19 ? 652  ALA A CB  1 
ATOM   5223 N N   . ARG A 1 653 ? 66.398 99.825  20.509  1.00 20.04 ? 653  ARG A N   1 
ATOM   5224 C CA  . ARG A 1 653 ? 66.809 99.618  19.134  1.00 19.15 ? 653  ARG A CA  1 
ATOM   5225 C C   . ARG A 1 653 ? 67.659 98.344  19.103  1.00 19.20 ? 653  ARG A C   1 
ATOM   5226 O O   . ARG A 1 653 ? 68.506 98.153  19.986  1.00 20.81 ? 653  ARG A O   1 
ATOM   5227 C CB  . ARG A 1 653 ? 67.570 100.886 18.672  1.00 18.33 ? 653  ARG A CB  1 
ATOM   5228 C CG  . ARG A 1 653 ? 68.063 100.832 17.289  1.00 19.65 ? 653  ARG A CG  1 
ATOM   5229 C CD  . ARG A 1 653 ? 68.693 102.194 16.914  1.00 24.50 ? 653  ARG A CD  1 
ATOM   5230 N NE  . ARG A 1 653 ? 67.704 103.264 17.100  1.00 21.56 ? 653  ARG A NE  1 
ATOM   5231 C CZ  . ARG A 1 653 ? 67.883 104.538 16.801  1.00 23.16 ? 653  ARG A CZ  1 
ATOM   5232 N NH1 . ARG A 1 653 ? 69.031 104.923 16.277  1.00 20.93 ? 653  ARG A NH1 1 
ATOM   5233 N NH2 . ARG A 1 653 ? 66.914 105.425 17.042  1.00 22.36 ? 653  ARG A NH2 1 
ATOM   5234 N N   . PRO A 1 654 ? 67.437 97.456  18.109  1.00 18.79 ? 654  PRO A N   1 
ATOM   5235 C CA  . PRO A 1 654 ? 68.270 96.280  17.986  1.00 19.06 ? 654  PRO A CA  1 
ATOM   5236 C C   . PRO A 1 654 ? 69.708 96.699  17.600  1.00 18.42 ? 654  PRO A C   1 
ATOM   5237 O O   . PRO A 1 654 ? 69.925 97.690  16.891  1.00 18.62 ? 654  PRO A O   1 
ATOM   5238 C CB  . PRO A 1 654 ? 67.619 95.493  16.806  1.00 19.57 ? 654  PRO A CB  1 
ATOM   5239 C CG  . PRO A 1 654 ? 66.220 96.060  16.689  1.00 19.66 ? 654  PRO A CG  1 
ATOM   5240 C CD  . PRO A 1 654 ? 66.429 97.514  17.039  1.00 19.77 ? 654  PRO A CD  1 
ATOM   5241 N N   . LEU A 1 655 ? 70.692 95.941  18.024  1.00 18.93 ? 655  LEU A N   1 
ATOM   5242 C CA  . LEU A 1 655 ? 72.077 96.272  17.614  1.00 20.87 ? 655  LEU A CA  1 
ATOM   5243 C C   . LEU A 1 655 ? 72.205 96.360  16.096  1.00 19.48 ? 655  LEU A C   1 
ATOM   5244 O O   . LEU A 1 655 ? 72.961 97.191  15.555  1.00 20.78 ? 655  LEU A O   1 
ATOM   5245 C CB  . LEU A 1 655 ? 73.056 95.199  18.160  1.00 19.75 ? 655  LEU A CB  1 
ATOM   5246 C CG  . LEU A 1 655 ? 73.680 95.518  19.496  1.00 22.78 ? 655  LEU A CG  1 
ATOM   5247 C CD1 . LEU A 1 655 ? 72.657 95.716  20.578  1.00 24.04 ? 655  LEU A CD1 1 
ATOM   5248 C CD2 . LEU A 1 655 ? 74.644 94.344  19.883  1.00 22.89 ? 655  LEU A CD2 1 
ATOM   5249 N N   . LEU A 1 656 ? 71.422 95.546  15.396  1.00 20.37 ? 656  LEU A N   1 
ATOM   5250 C CA  . LEU A 1 656 ? 71.537 95.434  13.946  1.00 20.54 ? 656  LEU A CA  1 
ATOM   5251 C C   . LEU A 1 656 ? 71.064 96.685  13.232  1.00 21.13 ? 656  LEU A C   1 
ATOM   5252 O O   . LEU A 1 656 ? 71.465 96.927  12.100  1.00 21.00 ? 656  LEU A O   1 
ATOM   5253 C CB  . LEU A 1 656 ? 70.794 94.175  13.432  1.00 22.58 ? 656  LEU A CB  1 
ATOM   5254 C CG  . LEU A 1 656 ? 69.267 94.173  13.384  1.00 20.45 ? 656  LEU A CG  1 
ATOM   5255 C CD1 . LEU A 1 656 ? 68.771 94.366  11.939  1.00 23.29 ? 656  LEU A CD1 1 
ATOM   5256 C CD2 . LEU A 1 656 ? 68.690 92.895  13.986  1.00 21.93 ? 656  LEU A CD2 1 
ATOM   5257 N N   . HIS A 1 657 ? 70.189 97.485  13.861  1.00 19.29 ? 657  HIS A N   1 
ATOM   5258 C CA  . HIS A 1 657 ? 69.806 98.721  13.233  1.00 18.93 ? 657  HIS A CA  1 
ATOM   5259 C C   . HIS A 1 657 ? 70.959 99.725  13.153  1.00 19.85 ? 657  HIS A C   1 
ATOM   5260 O O   . HIS A 1 657 ? 70.965 100.591 12.277  1.00 21.00 ? 657  HIS A O   1 
ATOM   5261 C CB  . HIS A 1 657 ? 68.619 99.341  14.011  1.00 20.15 ? 657  HIS A CB  1 
ATOM   5262 C CG  . HIS A 1 657 ? 67.313 98.671  13.701  1.00 19.69 ? 657  HIS A CG  1 
ATOM   5263 N ND1 . HIS A 1 657 ? 66.117 99.350  13.594  1.00 22.46 ? 657  HIS A ND1 1 
ATOM   5264 C CD2 . HIS A 1 657 ? 67.042 97.385  13.388  1.00 22.89 ? 657  HIS A CD2 1 
ATOM   5265 C CE1 . HIS A 1 657 ? 65.153 98.491  13.297  1.00 21.92 ? 657  HIS A CE1 1 
ATOM   5266 N NE2 . HIS A 1 657 ? 65.692 97.290  13.160  1.00 18.29 ? 657  HIS A NE2 1 
ATOM   5267 N N   . GLU A 1 658 ? 71.937 99.618  14.050  1.00 19.67 ? 658  GLU A N   1 
ATOM   5268 C CA  . GLU A 1 658 ? 73.126 100.494 13.960  1.00 20.98 ? 658  GLU A CA  1 
ATOM   5269 C C   . GLU A 1 658 ? 74.316 99.771  13.339  1.00 21.27 ? 658  GLU A C   1 
ATOM   5270 O O   . GLU A 1 658 ? 75.215 100.408 12.778  1.00 22.51 ? 658  GLU A O   1 
ATOM   5271 C CB  . GLU A 1 658 ? 73.517 101.003 15.367  1.00 21.41 ? 658  GLU A CB  1 
ATOM   5272 C CG  . GLU A 1 658 ? 72.417 101.939 15.912  1.00 19.98 ? 658  GLU A CG  1 
ATOM   5273 C CD  . GLU A 1 658 ? 72.320 103.215 15.107  1.00 26.25 ? 658  GLU A CD  1 
ATOM   5274 O OE1 . GLU A 1 658 ? 73.411 103.790 14.712  1.00 31.44 ? 658  GLU A OE1 1 
ATOM   5275 O OE2 . GLU A 1 658 ? 71.169 103.665 14.880  1.00 29.04 ? 658  GLU A OE2 1 
ATOM   5276 N N   . PHE A 1 659 ? 74.313 98.453  13.425  1.00 21.71 ? 659  PHE A N   1 
ATOM   5277 C CA  . PHE A 1 659 ? 75.538 97.650  13.135  1.00 22.70 ? 659  PHE A CA  1 
ATOM   5278 C C   . PHE A 1 659 ? 75.351 96.558  12.100  1.00 22.84 ? 659  PHE A C   1 
ATOM   5279 O O   . PHE A 1 659 ? 76.080 95.520  12.129  1.00 23.89 ? 659  PHE A O   1 
ATOM   5280 C CB  . PHE A 1 659 ? 76.034 97.052  14.436  1.00 21.80 ? 659  PHE A CB  1 
ATOM   5281 C CG  . PHE A 1 659 ? 76.504 98.133  15.416  1.00 24.00 ? 659  PHE A CG  1 
ATOM   5282 C CD1 . PHE A 1 659 ? 77.635 98.922  15.105  1.00 20.89 ? 659  PHE A CD1 1 
ATOM   5283 C CD2 . PHE A 1 659 ? 75.796 98.387  16.590  1.00 19.63 ? 659  PHE A CD2 1 
ATOM   5284 C CE1 . PHE A 1 659 ? 78.043 99.930  15.958  1.00 18.63 ? 659  PHE A CE1 1 
ATOM   5285 C CE2 . PHE A 1 659 ? 76.205 99.414  17.460  1.00 19.24 ? 659  PHE A CE2 1 
ATOM   5286 C CZ  . PHE A 1 659 ? 77.340 100.164 17.139  1.00 21.03 ? 659  PHE A CZ  1 
ATOM   5287 N N   . TYR A 1 660 ? 74.405 96.809  11.207  1.00 23.53 ? 660  TYR A N   1 
ATOM   5288 C CA  . TYR A 1 660 ? 73.944 95.850  10.181  1.00 24.51 ? 660  TYR A CA  1 
ATOM   5289 C C   . TYR A 1 660 ? 75.088 95.378  9.265   1.00 24.60 ? 660  TYR A C   1 
ATOM   5290 O O   . TYR A 1 660 ? 74.962 94.331  8.651   1.00 24.62 ? 660  TYR A O   1 
ATOM   5291 C CB  . TYR A 1 660 ? 72.867 96.481  9.290   1.00 23.38 ? 660  TYR A CB  1 
ATOM   5292 C CG  . TYR A 1 660 ? 73.141 97.891  8.881   1.00 23.99 ? 660  TYR A CG  1 
ATOM   5293 C CD1 . TYR A 1 660 ? 74.008 98.190  7.809   1.00 20.77 ? 660  TYR A CD1 1 
ATOM   5294 C CD2 . TYR A 1 660 ? 72.504 98.953  9.546   1.00 25.28 ? 660  TYR A CD2 1 
ATOM   5295 C CE1 . TYR A 1 660 ? 74.282 99.479  7.453   1.00 21.85 ? 660  TYR A CE1 1 
ATOM   5296 C CE2 . TYR A 1 660 ? 72.735 100.229 9.188   1.00 26.10 ? 660  TYR A CE2 1 
ATOM   5297 C CZ  . TYR A 1 660 ? 73.605 100.498 8.132   1.00 27.92 ? 660  TYR A CZ  1 
ATOM   5298 O OH  . TYR A 1 660 ? 73.781 101.804 7.822   1.00 29.09 ? 660  TYR A OH  1 
ATOM   5299 N N   . GLU A 1 661 ? 76.160 96.166  9.134   1.00 25.29 ? 661  GLU A N   1 
ATOM   5300 C CA  . GLU A 1 661 ? 77.299 95.763  8.288   1.00 28.28 ? 661  GLU A CA  1 
ATOM   5301 C C   . GLU A 1 661 ? 77.998 94.560  8.887   1.00 27.17 ? 661  GLU A C   1 
ATOM   5302 O O   . GLU A 1 661 ? 78.788 93.888  8.224   1.00 27.12 ? 661  GLU A O   1 
ATOM   5303 C CB  . GLU A 1 661 ? 78.303 96.919  8.077   1.00 27.22 ? 661  GLU A CB  1 
ATOM   5304 C CG  . GLU A 1 661 ? 77.769 98.111  7.315   1.00 32.24 ? 661  GLU A CG  1 
ATOM   5305 C CD  . GLU A 1 661 ? 78.853 99.175  6.947   1.00 36.68 ? 661  GLU A CD  1 
ATOM   5306 O OE1 . GLU A 1 661 ? 80.068 98.988  7.293   1.00 43.58 ? 661  GLU A OE1 1 
ATOM   5307 O OE2 . GLU A 1 661 ? 78.462 100.202 6.299   1.00 46.23 ? 661  GLU A OE2 1 
ATOM   5308 N N   . ASP A 1 662 ? 77.701 94.285  10.152  1.00 25.97 ? 662  ASP A N   1 
ATOM   5309 C CA  . ASP A 1 662 ? 78.293 93.206  10.897  1.00 25.38 ? 662  ASP A CA  1 
ATOM   5310 C C   . ASP A 1 662 ? 77.258 92.116  11.077  1.00 26.16 ? 662  ASP A C   1 
ATOM   5311 O O   . ASP A 1 662 ? 76.318 92.251  11.867  1.00 25.53 ? 662  ASP A O   1 
ATOM   5312 C CB  . ASP A 1 662 ? 78.772 93.769  12.249  1.00 25.08 ? 662  ASP A CB  1 
ATOM   5313 C CG  . ASP A 1 662 ? 79.480 92.759  13.108  1.00 28.53 ? 662  ASP A CG  1 
ATOM   5314 O OD1 . ASP A 1 662 ? 79.552 91.575  12.721  1.00 27.78 ? 662  ASP A OD1 1 
ATOM   5315 O OD2 . ASP A 1 662 ? 79.990 93.160  14.193  1.00 33.08 ? 662  ASP A OD2 1 
ATOM   5316 N N   . ASN A 1 663 ? 77.409 91.012  10.352  1.00 25.14 ? 663  ASN A N   1 
ATOM   5317 C CA  . ASN A 1 663 ? 76.420 89.936  10.451  1.00 25.15 ? 663  ASN A CA  1 
ATOM   5318 C C   . ASN A 1 663 ? 76.367 89.299  11.812  1.00 24.08 ? 663  ASN A C   1 
ATOM   5319 O O   . ASN A 1 663 ? 75.393 88.648  12.142  1.00 22.73 ? 663  ASN A O   1 
ATOM   5320 C CB  . ASN A 1 663 ? 76.529 88.918  9.283   1.00 25.97 ? 663  ASN A CB  1 
ATOM   5321 C CG  . ASN A 1 663 ? 77.810 88.064  9.311   1.00 31.88 ? 663  ASN A CG  1 
ATOM   5322 O OD1 . ASN A 1 663 ? 78.525 87.990  10.309  1.00 32.86 ? 663  ASN A OD1 1 
ATOM   5323 N ND2 . ASN A 1 663 ? 78.073 87.370  8.179   1.00 35.22 ? 663  ASN A ND2 1 
ATOM   5324 N N   . SER A 1 664 ? 77.369 89.547  12.669  1.00 23.60 ? 664  SER A N   1 
ATOM   5325 C CA  . SER A 1 664 ? 77.245 89.024  14.038  1.00 25.36 ? 664  SER A CA  1 
ATOM   5326 C C   . SER A 1 664 ? 76.116 89.670  14.858  1.00 25.01 ? 664  SER A C   1 
ATOM   5327 O O   . SER A 1 664 ? 75.717 89.118  15.876  1.00 25.39 ? 664  SER A O   1 
ATOM   5328 C CB  . SER A 1 664 ? 78.570 89.103  14.818  1.00 26.72 ? 664  SER A CB  1 
ATOM   5329 O OG  . SER A 1 664 ? 79.480 88.137  14.288  1.00 29.69 ? 664  SER A OG  1 
ATOM   5330 N N   . THR A 1 665 ? 75.595 90.815  14.408  1.00 24.27 ? 665  THR A N   1 
ATOM   5331 C CA  . THR A 1 665 ? 74.569 91.507  15.160  1.00 24.21 ? 665  THR A CA  1 
ATOM   5332 C C   . THR A 1 665 ? 73.149 91.104  14.737  1.00 24.46 ? 665  THR A C   1 
ATOM   5333 O O   . THR A 1 665 ? 72.190 91.479  15.416  1.00 24.30 ? 665  THR A O   1 
ATOM   5334 C CB  . THR A 1 665 ? 74.671 93.011  14.982  1.00 24.61 ? 665  THR A CB  1 
ATOM   5335 O OG1 . THR A 1 665 ? 74.400 93.363  13.625  1.00 22.61 ? 665  THR A OG1 1 
ATOM   5336 C CG2 . THR A 1 665 ? 76.053 93.561  15.453  1.00 23.71 ? 665  THR A CG2 1 
ATOM   5337 N N   . TRP A 1 666 ? 73.022 90.317  13.664  1.00 23.93 ? 666  TRP A N   1 
ATOM   5338 C CA  . TRP A 1 666 ? 71.717 90.111  13.001  1.00 25.22 ? 666  TRP A CA  1 
ATOM   5339 C C   . TRP A 1 666 ? 70.712 89.341  13.813  1.00 25.18 ? 666  TRP A C   1 
ATOM   5340 O O   . TRP A 1 666 ? 69.491 89.447  13.567  1.00 26.32 ? 666  TRP A O   1 
ATOM   5341 C CB  . TRP A 1 666 ? 71.864 89.433  11.627  1.00 24.30 ? 666  TRP A CB  1 
ATOM   5342 C CG  . TRP A 1 666 ? 72.556 90.292  10.630  1.00 24.83 ? 666  TRP A CG  1 
ATOM   5343 C CD1 . TRP A 1 666 ? 72.931 91.575  10.791  1.00 23.22 ? 666  TRP A CD1 1 
ATOM   5344 C CD2 . TRP A 1 666 ? 72.932 89.916  9.305   1.00 26.33 ? 666  TRP A CD2 1 
ATOM   5345 N NE1 . TRP A 1 666 ? 73.536 92.056  9.640   1.00 27.11 ? 666  TRP A NE1 1 
ATOM   5346 C CE2 . TRP A 1 666 ? 73.558 91.043  8.713   1.00 27.06 ? 666  TRP A CE2 1 
ATOM   5347 C CE3 . TRP A 1 666 ? 72.829 88.720  8.567   1.00 28.35 ? 666  TRP A CE3 1 
ATOM   5348 C CZ2 . TRP A 1 666 ? 74.078 91.024  7.398   1.00 26.19 ? 666  TRP A CZ2 1 
ATOM   5349 C CZ3 . TRP A 1 666 ? 73.338 88.697  7.239   1.00 27.12 ? 666  TRP A CZ3 1 
ATOM   5350 C CH2 . TRP A 1 666 ? 73.944 89.839  6.674   1.00 26.44 ? 666  TRP A CH2 1 
ATOM   5351 N N   . ASP A 1 667 ? 71.198 88.567  14.759  1.00 26.73 ? 667  ASP A N   1 
ATOM   5352 C CA  . ASP A 1 667 ? 70.310 87.801  15.619  1.00 30.26 ? 667  ASP A CA  1 
ATOM   5353 C C   . ASP A 1 667 ? 70.504 88.122  17.104  1.00 30.53 ? 667  ASP A C   1 
ATOM   5354 O O   . ASP A 1 667 ? 69.972 87.426  17.957  1.00 32.54 ? 667  ASP A O   1 
ATOM   5355 C CB  . ASP A 1 667 ? 70.434 86.292  15.326  1.00 32.38 ? 667  ASP A CB  1 
ATOM   5356 C CG  . ASP A 1 667 ? 71.673 85.672  15.936  1.00 40.53 ? 667  ASP A CG  1 
ATOM   5357 O OD1 . ASP A 1 667 ? 72.585 86.431  16.350  1.00 46.31 ? 667  ASP A OD1 1 
ATOM   5358 O OD2 . ASP A 1 667 ? 71.735 84.411  16.016  1.00 49.21 ? 667  ASP A OD2 1 
ATOM   5359 N N   . VAL A 1 668 ? 71.236 89.190  17.426  1.00 29.99 ? 668  VAL A N   1 
ATOM   5360 C CA  . VAL A 1 668 ? 71.435 89.567  18.834  1.00 29.26 ? 668  VAL A CA  1 
ATOM   5361 C C   . VAL A 1 668 ? 70.141 90.093  19.446  1.00 29.63 ? 668  VAL A C   1 
ATOM   5362 O O   . VAL A 1 668 ? 69.519 91.041  18.901  1.00 29.73 ? 668  VAL A O   1 
ATOM   5363 C CB  . VAL A 1 668 ? 72.547 90.628  18.997  1.00 29.42 ? 668  VAL A CB  1 
ATOM   5364 C CG1 . VAL A 1 668 ? 72.534 91.185  20.432  1.00 28.60 ? 668  VAL A CG1 1 
ATOM   5365 C CG2 . VAL A 1 668 ? 73.893 90.009  18.682  1.00 29.47 ? 668  VAL A CG2 1 
ATOM   5366 N N   . HIS A 1 669 ? 69.717 89.454  20.545  1.00 29.58 ? 669  HIS A N   1 
ATOM   5367 C CA  . HIS A 1 669 ? 68.482 89.807  21.229  1.00 30.15 ? 669  HIS A CA  1 
ATOM   5368 C C   . HIS A 1 669 ? 68.596 89.763  22.767  1.00 29.38 ? 669  HIS A C   1 
ATOM   5369 O O   . HIS A 1 669 ? 67.599 89.912  23.472  1.00 29.78 ? 669  HIS A O   1 
ATOM   5370 C CB  . HIS A 1 669 ? 67.313 88.917  20.766  1.00 30.43 ? 669  HIS A CB  1 
ATOM   5371 C CG  . HIS A 1 669 ? 67.509 87.468  21.060  1.00 32.23 ? 669  HIS A CG  1 
ATOM   5372 N ND1 . HIS A 1 669 ? 66.900 86.837  22.122  1.00 35.77 ? 669  HIS A ND1 1 
ATOM   5373 C CD2 . HIS A 1 669 ? 68.295 86.537  20.470  1.00 35.77 ? 669  HIS A CD2 1 
ATOM   5374 C CE1 . HIS A 1 669 ? 67.294 85.577  22.165  1.00 37.34 ? 669  HIS A CE1 1 
ATOM   5375 N NE2 . HIS A 1 669 ? 68.148 85.372  21.177  1.00 37.71 ? 669  HIS A NE2 1 
ATOM   5376 N N   . GLN A 1 670 ? 69.784 89.548  23.288  1.00 27.14 ? 670  GLN A N   1 
ATOM   5377 C CA  . GLN A 1 670 ? 69.953 89.573  24.722  1.00 27.58 ? 670  GLN A CA  1 
ATOM   5378 C C   . GLN A 1 670 ? 70.611 90.913  25.148  1.00 26.31 ? 670  GLN A C   1 
ATOM   5379 O O   . GLN A 1 670 ? 70.967 91.106  26.299  1.00 26.70 ? 670  GLN A O   1 
ATOM   5380 C CB  . GLN A 1 670 ? 70.760 88.327  25.181  1.00 28.78 ? 670  GLN A CB  1 
ATOM   5381 C CG  . GLN A 1 670 ? 70.155 86.956  24.749  1.00 35.37 ? 670  GLN A CG  1 
ATOM   5382 C CD  . GLN A 1 670 ? 69.584 86.036  25.894  1.00 44.72 ? 670  GLN A CD  1 
ATOM   5383 O OE1 . GLN A 1 670 ? 70.345 85.400  26.690  1.00 45.37 ? 670  GLN A OE1 1 
ATOM   5384 N NE2 . GLN A 1 670 ? 68.239 85.913  25.925  1.00 43.94 ? 670  GLN A NE2 1 
ATOM   5385 N N   . GLN A 1 671 ? 70.813 91.799  24.183  1.00 24.88 ? 671  GLN A N   1 
ATOM   5386 C CA  . GLN A 1 671 ? 71.368 93.123  24.396  1.00 24.61 ? 671  GLN A CA  1 
ATOM   5387 C C   . GLN A 1 671 ? 70.512 94.034  23.504  1.00 23.73 ? 671  GLN A C   1 
ATOM   5388 O O   . GLN A 1 671 ? 69.869 93.542  22.539  1.00 24.63 ? 671  GLN A O   1 
ATOM   5389 C CB  . GLN A 1 671 ? 72.790 93.210  23.869  1.00 24.42 ? 671  GLN A CB  1 
ATOM   5390 C CG  . GLN A 1 671 ? 73.876 92.571  24.743  1.00 27.75 ? 671  GLN A CG  1 
ATOM   5391 C CD  . GLN A 1 671 ? 75.172 92.422  23.962  1.00 30.13 ? 671  GLN A CD  1 
ATOM   5392 O OE1 . GLN A 1 671 ? 75.272 91.575  23.063  1.00 31.85 ? 671  GLN A OE1 1 
ATOM   5393 N NE2 . GLN A 1 671 ? 76.142 93.302  24.237  1.00 24.58 ? 671  GLN A NE2 1 
ATOM   5394 N N   . PHE A 1 672 ? 70.530 95.322  23.801  1.00 20.95 ? 672  PHE A N   1 
ATOM   5395 C CA  . PHE A 1 672 ? 69.882 96.317  22.954  1.00 21.83 ? 672  PHE A CA  1 
ATOM   5396 C C   . PHE A 1 672 ? 70.497 97.698  23.134  1.00 20.28 ? 672  PHE A C   1 
ATOM   5397 O O   . PHE A 1 672 ? 71.313 97.876  23.996  1.00 20.84 ? 672  PHE A O   1 
ATOM   5398 C CB  . PHE A 1 672 ? 68.370 96.323  23.181  1.00 21.58 ? 672  PHE A CB  1 
ATOM   5399 C CG  . PHE A 1 672 ? 67.939 96.744  24.553  1.00 23.55 ? 672  PHE A CG  1 
ATOM   5400 C CD1 . PHE A 1 672 ? 67.265 97.948  24.735  1.00 25.68 ? 672  PHE A CD1 1 
ATOM   5401 C CD2 . PHE A 1 672 ? 68.098 95.897  25.657  1.00 24.76 ? 672  PHE A CD2 1 
ATOM   5402 C CE1 . PHE A 1 672 ? 66.836 98.346  26.010  1.00 25.08 ? 672  PHE A CE1 1 
ATOM   5403 C CE2 . PHE A 1 672 ? 67.685 96.283  26.916  1.00 26.33 ? 672  PHE A CE2 1 
ATOM   5404 C CZ  . PHE A 1 672 ? 67.027 97.501  27.104  1.00 26.07 ? 672  PHE A CZ  1 
ATOM   5405 N N   . LEU A 1 673 ? 70.074 98.661  22.319  1.00 19.21 ? 673  LEU A N   1 
ATOM   5406 C CA  . LEU A 1 673 ? 70.496 100.052 22.426  1.00 19.27 ? 673  LEU A CA  1 
ATOM   5407 C C   . LEU A 1 673 ? 69.339 100.943 22.868  1.00 20.14 ? 673  LEU A C   1 
ATOM   5408 O O   . LEU A 1 673 ? 68.183 100.666 22.548  1.00 20.28 ? 673  LEU A O   1 
ATOM   5409 C CB  . LEU A 1 673 ? 70.923 100.554 21.063  1.00 19.06 ? 673  LEU A CB  1 
ATOM   5410 C CG  . LEU A 1 673 ? 71.929 99.639  20.377  1.00 21.26 ? 673  LEU A CG  1 
ATOM   5411 C CD1 . LEU A 1 673 ? 72.098 100.108 18.941  1.00 21.81 ? 673  LEU A CD1 1 
ATOM   5412 C CD2 . LEU A 1 673 ? 73.255 99.769  21.113  1.00 24.26 ? 673  LEU A CD2 1 
ATOM   5413 N N   . TRP A 1 674 ? 69.660 101.987 23.612  1.00 20.35 ? 674  TRP A N   1 
ATOM   5414 C CA  . TRP A 1 674 ? 68.843 103.208 23.603  1.00 21.15 ? 674  TRP A CA  1 
ATOM   5415 C C   . TRP A 1 674 ? 69.350 104.069 22.480  1.00 21.25 ? 674  TRP A C   1 
ATOM   5416 O O   . TRP A 1 674 ? 70.423 104.670 22.598  1.00 24.42 ? 674  TRP A O   1 
ATOM   5417 C CB  . TRP A 1 674 ? 69.043 103.989 24.885  1.00 20.90 ? 674  TRP A CB  1 
ATOM   5418 C CG  . TRP A 1 674 ? 68.191 103.580 26.027  1.00 23.23 ? 674  TRP A CG  1 
ATOM   5419 C CD1 . TRP A 1 674 ? 67.524 102.410 26.187  1.00 23.35 ? 674  TRP A CD1 1 
ATOM   5420 C CD2 . TRP A 1 674 ? 67.929 104.366 27.189  1.00 23.54 ? 674  TRP A CD2 1 
ATOM   5421 N NE1 . TRP A 1 674 ? 66.823 102.427 27.382  1.00 26.86 ? 674  TRP A NE1 1 
ATOM   5422 C CE2 . TRP A 1 674 ? 67.067 103.621 28.013  1.00 24.11 ? 674  TRP A CE2 1 
ATOM   5423 C CE3 . TRP A 1 674 ? 68.331 105.654 27.602  1.00 22.78 ? 674  TRP A CE3 1 
ATOM   5424 C CZ2 . TRP A 1 674 ? 66.579 104.121 29.232  1.00 25.29 ? 674  TRP A CZ2 1 
ATOM   5425 C CZ3 . TRP A 1 674 ? 67.895 106.129 28.828  1.00 24.21 ? 674  TRP A CZ3 1 
ATOM   5426 C CH2 . TRP A 1 674 ? 67.030 105.360 29.637  1.00 24.36 ? 674  TRP A CH2 1 
ATOM   5427 N N   . GLY A 1 675 ? 68.579 104.175 21.415  1.00 22.16 ? 675  GLY A N   1 
ATOM   5428 C CA  . GLY A 1 675 ? 68.961 105.046 20.298  1.00 21.73 ? 675  GLY A CA  1 
ATOM   5429 C C   . GLY A 1 675 ? 70.245 104.510 19.705  1.00 21.70 ? 675  GLY A C   1 
ATOM   5430 O O   . GLY A 1 675 ? 70.469 103.323 19.712  1.00 19.19 ? 675  GLY A O   1 
ATOM   5431 N N   . PRO A 1 676 ? 71.071 105.398 19.152  1.00 22.62 ? 676  PRO A N   1 
ATOM   5432 C CA  . PRO A 1 676 ? 72.292 104.930 18.488  1.00 23.74 ? 676  PRO A CA  1 
ATOM   5433 C C   . PRO A 1 676 ? 73.429 104.675 19.443  1.00 24.16 ? 676  PRO A C   1 
ATOM   5434 O O   . PRO A 1 676 ? 74.371 103.984 19.088  1.00 24.39 ? 676  PRO A O   1 
ATOM   5435 C CB  . PRO A 1 676 ? 72.634 106.098 17.533  1.00 24.50 ? 676  PRO A CB  1 
ATOM   5436 C CG  . PRO A 1 676 ? 72.039 107.326 18.213  1.00 24.63 ? 676  PRO A CG  1 
ATOM   5437 C CD  . PRO A 1 676 ? 70.818 106.844 18.987  1.00 20.53 ? 676  PRO A CD  1 
ATOM   5438 N N   . GLY A 1 677 ? 73.305 105.170 20.680  1.00 24.32 ? 677  GLY A N   1 
ATOM   5439 C CA  . GLY A 1 677 ? 74.482 105.411 21.510  1.00 21.55 ? 677  GLY A CA  1 
ATOM   5440 C C   . GLY A 1 677 ? 74.723 104.654 22.774  1.00 21.85 ? 677  GLY A C   1 
ATOM   5441 O O   . GLY A 1 677 ? 75.828 104.698 23.303  1.00 22.51 ? 677  GLY A O   1 
ATOM   5442 N N   . LEU A 1 678 ? 73.726 103.963 23.309  1.00 22.03 ? 678  LEU A N   1 
ATOM   5443 C CA  . LEU A 1 678 ? 73.888 103.360 24.638  1.00 22.95 ? 678  LEU A CA  1 
ATOM   5444 C C   . LEU A 1 678 ? 73.577 101.889 24.522  1.00 22.32 ? 678  LEU A C   1 
ATOM   5445 O O   . LEU A 1 678 ? 72.487 101.510 24.110  1.00 22.67 ? 678  LEU A O   1 
ATOM   5446 C CB  . LEU A 1 678 ? 72.976 104.043 25.688  1.00 22.10 ? 678  LEU A CB  1 
ATOM   5447 C CG  . LEU A 1 678 ? 72.802 103.325 27.039  1.00 24.25 ? 678  LEU A CG  1 
ATOM   5448 C CD1 . LEU A 1 678 ? 74.087 103.295 27.869  1.00 21.71 ? 678  LEU A CD1 1 
ATOM   5449 C CD2 . LEU A 1 678 ? 71.719 103.984 27.868  1.00 24.63 ? 678  LEU A CD2 1 
ATOM   5450 N N   . LEU A 1 679 ? 74.570 101.074 24.842  1.00 21.86 ? 679  LEU A N   1 
ATOM   5451 C CA  . LEU A 1 679 ? 74.468 99.652  24.806  1.00 21.42 ? 679  LEU A CA  1 
ATOM   5452 C C   . LEU A 1 679 ? 74.187 99.082  26.179  1.00 20.88 ? 679  LEU A C   1 
ATOM   5453 O O   . LEU A 1 679 ? 74.910 99.336  27.129  1.00 21.18 ? 679  LEU A O   1 
ATOM   5454 C CB  . LEU A 1 679 ? 75.778 99.064  24.247  1.00 21.92 ? 679  LEU A CB  1 
ATOM   5455 C CG  . LEU A 1 679 ? 75.862 97.541  24.155  1.00 23.21 ? 679  LEU A CG  1 
ATOM   5456 C CD1 . LEU A 1 679 ? 74.904 96.967  23.136  1.00 18.46 ? 679  LEU A CD1 1 
ATOM   5457 C CD2 . LEU A 1 679 ? 77.331 97.162  23.793  1.00 20.83 ? 679  LEU A CD2 1 
ATOM   5458 N N   . ILE A 1 680 ? 73.154 98.254  26.275  1.00 19.79 ? 680  ILE A N   1 
ATOM   5459 C CA  . ILE A 1 680 ? 72.720 97.688  27.531  1.00 20.80 ? 680  ILE A CA  1 
ATOM   5460 C C   . ILE A 1 680 ? 72.910 96.171  27.417  1.00 20.61 ? 680  ILE A C   1 
ATOM   5461 O O   . ILE A 1 680 ? 72.447 95.562  26.453  1.00 20.90 ? 680  ILE A O   1 
ATOM   5462 C CB  . ILE A 1 680 ? 71.208 98.012  27.801  1.00 20.14 ? 680  ILE A CB  1 
ATOM   5463 C CG1 . ILE A 1 680 ? 70.992 99.530  27.868  1.00 23.43 ? 680  ILE A CG1 1 
ATOM   5464 C CG2 . ILE A 1 680 ? 70.698 97.318  29.076  1.00 21.05 ? 680  ILE A CG2 1 
ATOM   5465 C CD1 . ILE A 1 680 ? 70.019 100.015 26.919  1.00 24.95 ? 680  ILE A CD1 1 
ATOM   5466 N N   . THR A 1 681 ? 73.593 95.602  28.401  1.00 22.10 ? 681  THR A N   1 
ATOM   5467 C CA  . THR A 1 681 ? 74.027 94.203  28.425  1.00 22.61 ? 681  THR A CA  1 
ATOM   5468 C C   . THR A 1 681 ? 73.639 93.644  29.797  1.00 23.17 ? 681  THR A C   1 
ATOM   5469 O O   . THR A 1 681 ? 74.396 93.703  30.778  1.00 24.14 ? 681  THR A O   1 
ATOM   5470 C CB  . THR A 1 681 ? 75.549 94.094  28.125  1.00 23.76 ? 681  THR A CB  1 
ATOM   5471 O OG1 . THR A 1 681 ? 75.784 94.700  26.853  1.00 26.16 ? 681  THR A OG1 1 
ATOM   5472 C CG2 . THR A 1 681 ? 76.046 92.597  28.039  1.00 25.28 ? 681  THR A CG2 1 
ATOM   5473 N N   . PRO A 1 682 ? 72.426 93.104  29.894  1.00 23.19 ? 682  PRO A N   1 
ATOM   5474 C CA  . PRO A 1 682 ? 71.995 92.553  31.162  1.00 24.26 ? 682  PRO A CA  1 
ATOM   5475 C C   . PRO A 1 682 ? 72.496 91.131  31.408  1.00 25.74 ? 682  PRO A C   1 
ATOM   5476 O O   . PRO A 1 682 ? 72.831 90.427  30.464  1.00 26.76 ? 682  PRO A O   1 
ATOM   5477 C CB  . PRO A 1 682 ? 70.472 92.478  31.016  1.00 22.92 ? 682  PRO A CB  1 
ATOM   5478 C CG  . PRO A 1 682 ? 70.266 92.282  29.535  1.00 24.02 ? 682  PRO A CG  1 
ATOM   5479 C CD  . PRO A 1 682 ? 71.395 93.027  28.851  1.00 23.55 ? 682  PRO A CD  1 
ATOM   5480 N N   . VAL A 1 683 ? 72.476 90.723  32.677  1.00 26.23 ? 683  VAL A N   1 
ATOM   5481 C CA  . VAL A 1 683 ? 72.680 89.330  33.047  1.00 27.55 ? 683  VAL A CA  1 
ATOM   5482 C C   . VAL A 1 683 ? 71.299 88.737  33.031  1.00 27.96 ? 683  VAL A C   1 
ATOM   5483 O O   . VAL A 1 683 ? 70.358 89.302  33.624  1.00 27.52 ? 683  VAL A O   1 
ATOM   5484 C CB  . VAL A 1 683 ? 73.325 89.194  34.445  1.00 27.25 ? 683  VAL A CB  1 
ATOM   5485 C CG1 . VAL A 1 683 ? 73.254 87.730  34.964  1.00 26.37 ? 683  VAL A CG1 1 
ATOM   5486 C CG2 . VAL A 1 683 ? 74.753 89.698  34.395  1.00 26.74 ? 683  VAL A CG2 1 
ATOM   5487 N N   . LEU A 1 684 ? 71.166 87.623  32.322  1.00 27.69 ? 684  LEU A N   1 
ATOM   5488 C CA  . LEU A 1 684 ? 69.840 87.056  32.023  1.00 28.22 ? 684  LEU A CA  1 
ATOM   5489 C C   . LEU A 1 684 ? 69.765 85.578  32.425  1.00 29.13 ? 684  LEU A C   1 
ATOM   5490 O O   . LEU A 1 684 ? 68.790 84.909  32.116  1.00 28.26 ? 684  LEU A O   1 
ATOM   5491 C CB  . LEU A 1 684 ? 69.502 87.208  30.521  1.00 27.88 ? 684  LEU A CB  1 
ATOM   5492 C CG  . LEU A 1 684 ? 69.374 88.640  29.972  1.00 26.71 ? 684  LEU A CG  1 
ATOM   5493 C CD1 . LEU A 1 684 ? 69.152 88.637  28.461  1.00 24.94 ? 684  LEU A CD1 1 
ATOM   5494 C CD2 . LEU A 1 684 ? 68.271 89.416  30.692  1.00 25.22 ? 684  LEU A CD2 1 
ATOM   5495 N N   . ASP A 1 685 ? 70.801 85.100  33.134  1.00 31.21 ? 685  ASP A N   1 
ATOM   5496 C CA  . ASP A 1 685 ? 70.916 83.683  33.576  1.00 32.24 ? 685  ASP A CA  1 
ATOM   5497 C C   . ASP A 1 685 ? 70.993 83.548  35.086  1.00 31.53 ? 685  ASP A C   1 
ATOM   5498 O O   . ASP A 1 685 ? 71.736 84.267  35.747  1.00 30.15 ? 685  ASP A O   1 
ATOM   5499 C CB  . ASP A 1 685 ? 72.192 83.035  33.038  1.00 33.53 ? 685  ASP A CB  1 
ATOM   5500 C CG  . ASP A 1 685 ? 72.230 82.967  31.537  1.00 39.00 ? 685  ASP A CG  1 
ATOM   5501 O OD1 . ASP A 1 685 ? 71.225 82.540  30.899  1.00 42.83 ? 685  ASP A OD1 1 
ATOM   5502 O OD2 . ASP A 1 685 ? 73.302 83.328  30.998  1.00 44.19 ? 685  ASP A OD2 1 
ATOM   5503 N N   . GLU A 1 686 ? 70.267 82.580  35.610  1.00 31.84 ? 686  GLU A N   1 
ATOM   5504 C CA  . GLU A 1 686 ? 70.242 82.328  37.044  1.00 34.00 ? 686  GLU A CA  1 
ATOM   5505 C C   . GLU A 1 686 ? 71.614 81.882  37.496  1.00 34.39 ? 686  GLU A C   1 
ATOM   5506 O O   . GLU A 1 686 ? 72.254 81.063  36.832  1.00 33.44 ? 686  GLU A O   1 
ATOM   5507 C CB  . GLU A 1 686 ? 69.189 81.268  37.374  1.00 34.11 ? 686  GLU A CB  1 
ATOM   5508 C CG  . GLU A 1 686 ? 69.128 80.843  38.841  1.00 36.01 ? 686  GLU A CG  1 
ATOM   5509 C CD  . GLU A 1 686 ? 67.939 79.906  39.114  1.00 36.96 ? 686  GLU A CD  1 
ATOM   5510 O OE1 . GLU A 1 686 ? 67.303 79.409  38.148  1.00 41.12 ? 686  GLU A OE1 1 
ATOM   5511 O OE2 . GLU A 1 686 ? 67.609 79.697  40.295  1.00 40.89 ? 686  GLU A OE2 1 
ATOM   5512 N N   . GLY A 1 687 ? 72.082 82.494  38.583  1.00 35.05 ? 687  GLY A N   1 
ATOM   5513 C CA  . GLY A 1 687 ? 73.375 82.160  39.168  1.00 35.80 ? 687  GLY A CA  1 
ATOM   5514 C C   . GLY A 1 687 ? 74.530 82.953  38.590  1.00 36.58 ? 687  GLY A C   1 
ATOM   5515 O O   . GLY A 1 687 ? 75.589 83.045  39.221  1.00 38.07 ? 687  GLY A O   1 
ATOM   5516 N N   . ALA A 1 688 ? 74.319 83.568  37.427  1.00 35.77 ? 688  ALA A N   1 
ATOM   5517 C CA  . ALA A 1 688 ? 75.401 84.177  36.655  1.00 35.46 ? 688  ALA A CA  1 
ATOM   5518 C C   . ALA A 1 688 ? 75.933 85.520  37.151  1.00 35.33 ? 688  ALA A C   1 
ATOM   5519 O O   . ALA A 1 688 ? 75.174 86.376  37.638  1.00 34.84 ? 688  ALA A O   1 
ATOM   5520 C CB  . ALA A 1 688 ? 74.995 84.279  35.199  1.00 35.54 ? 688  ALA A CB  1 
ATOM   5521 N N   . GLU A 1 689 ? 77.247 85.698  37.000  1.00 34.80 ? 689  GLU A N   1 
ATOM   5522 C CA  . GLU A 1 689 ? 77.934 86.940  37.333  1.00 35.87 ? 689  GLU A CA  1 
ATOM   5523 C C   . GLU A 1 689 ? 78.752 87.426  36.144  1.00 36.37 ? 689  GLU A C   1 
ATOM   5524 O O   . GLU A 1 689 ? 79.719 88.196  36.256  1.00 35.42 ? 689  GLU A O   1 
ATOM   5525 C CB  . GLU A 1 689 ? 78.759 86.775  38.598  1.00 36.26 ? 689  GLU A CB  1 
ATOM   5526 C CG  . GLU A 1 689 ? 77.861 86.704  39.807  1.00 40.48 ? 689  GLU A CG  1 
ATOM   5527 C CD  . GLU A 1 689 ? 78.599 86.509  41.136  1.00 50.00 ? 689  GLU A CD  1 
ATOM   5528 O OE1 . GLU A 1 689 ? 79.720 85.917  41.169  1.00 52.94 ? 689  GLU A OE1 1 
ATOM   5529 O OE2 . GLU A 1 689 ? 78.028 86.943  42.164  1.00 53.60 ? 689  GLU A OE2 1 
ATOM   5530 N N   . LYS A 1 690 ? 78.302 86.999  34.975  1.00 37.51 ? 690  LYS A N   1 
ATOM   5531 C CA  . LYS A 1 690 ? 78.990 87.240  33.713  1.00 40.09 ? 690  LYS A CA  1 
ATOM   5532 C C   . LYS A 1 690 ? 77.917 87.126  32.655  1.00 39.71 ? 690  LYS A C   1 
ATOM   5533 O O   . LYS A 1 690 ? 76.885 86.490  32.860  1.00 39.32 ? 690  LYS A O   1 
ATOM   5534 C CB  . LYS A 1 690 ? 80.063 86.165  33.436  1.00 40.11 ? 690  LYS A CB  1 
ATOM   5535 C CG  . LYS A 1 690 ? 81.382 86.371  34.173  1.00 43.40 ? 690  LYS A CG  1 
ATOM   5536 C CD  . LYS A 1 690 ? 82.181 85.068  34.312  1.00 43.84 ? 690  LYS A CD  1 
ATOM   5537 C CE  . LYS A 1 690 ? 83.242 85.196  35.424  1.00 50.13 ? 690  LYS A CE  1 
ATOM   5538 N NZ  . LYS A 1 690 ? 84.438 84.316  35.178  1.00 52.86 ? 690  LYS A NZ  1 
ATOM   5539 N N   . VAL A 1 691 ? 78.151 87.765  31.522  1.00 39.99 ? 691  VAL A N   1 
ATOM   5540 C CA  . VAL A 1 691 ? 77.254 87.559  30.412  1.00 40.71 ? 691  VAL A CA  1 
ATOM   5541 C C   . VAL A 1 691 ? 78.079 87.486  29.150  1.00 39.86 ? 691  VAL A C   1 
ATOM   5542 O O   . VAL A 1 691 ? 79.020 88.262  28.981  1.00 39.43 ? 691  VAL A O   1 
ATOM   5543 C CB  . VAL A 1 691 ? 76.140 88.634  30.369  1.00 40.18 ? 691  VAL A CB  1 
ATOM   5544 C CG1 . VAL A 1 691 ? 76.749 90.006  30.275  1.00 43.23 ? 691  VAL A CG1 1 
ATOM   5545 C CG2 . VAL A 1 691 ? 75.207 88.418  29.198  1.00 43.76 ? 691  VAL A CG2 1 
ATOM   5546 N N   . MET A 1 692 ? 77.783 86.488  28.316  1.00 40.43 ? 692  MET A N   1 
ATOM   5547 C CA  . MET A 1 692 ? 78.372 86.425  26.982  1.00 40.62 ? 692  MET A CA  1 
ATOM   5548 C C   . MET A 1 692 ? 77.652 87.494  26.153  1.00 38.06 ? 692  MET A C   1 
ATOM   5549 O O   . MET A 1 692 ? 76.453 87.460  25.985  1.00 37.78 ? 692  MET A O   1 
ATOM   5550 C CB  . MET A 1 692 ? 78.288 85.020  26.350  1.00 42.06 ? 692  MET A CB  1 
ATOM   5551 C CG  . MET A 1 692 ? 79.228 83.976  27.020  1.00 47.21 ? 692  MET A CG  1 
ATOM   5552 S SD  . MET A 1 692 ? 81.031 84.371  26.983  1.00 56.22 ? 692  MET A SD  1 
ATOM   5553 C CE  . MET A 1 692 ? 81.697 83.162  28.160  1.00 52.34 ? 692  MET A CE  1 
ATOM   5554 N N   . ALA A 1 693 ? 78.416 88.453  25.662  1.00 36.21 ? 693  ALA A N   1 
ATOM   5555 C CA  . ALA A 1 693 ? 77.843 89.601  25.000  1.00 34.39 ? 693  ALA A CA  1 
ATOM   5556 C C   . ALA A 1 693 ? 78.604 89.837  23.737  1.00 32.58 ? 693  ALA A C   1 
ATOM   5557 O O   . ALA A 1 693 ? 79.779 89.491  23.641  1.00 32.65 ? 693  ALA A O   1 
ATOM   5558 C CB  . ALA A 1 693 ? 77.967 90.835  25.906  1.00 34.26 ? 693  ALA A CB  1 
ATOM   5559 N N   . TYR A 1 694 ? 77.950 90.494  22.790  1.00 29.77 ? 694  TYR A N   1 
ATOM   5560 C CA  . TYR A 1 694 ? 78.621 91.004  21.617  1.00 27.63 ? 694  TYR A CA  1 
ATOM   5561 C C   . TYR A 1 694 ? 78.947 92.471  21.789  1.00 27.35 ? 694  TYR A C   1 
ATOM   5562 O O   . TYR A 1 694 ? 78.095 93.292  22.221  1.00 26.56 ? 694  TYR A O   1 
ATOM   5563 C CB  . TYR A 1 694 ? 77.737 90.810  20.362  1.00 27.51 ? 694  TYR A CB  1 
ATOM   5564 C CG  . TYR A 1 694 ? 78.557 91.007  19.130  1.00 26.98 ? 694  TYR A CG  1 
ATOM   5565 C CD1 . TYR A 1 694 ? 79.574 90.094  18.820  1.00 27.91 ? 694  TYR A CD1 1 
ATOM   5566 C CD2 . TYR A 1 694 ? 78.371 92.119  18.303  1.00 25.67 ? 694  TYR A CD2 1 
ATOM   5567 C CE1 . TYR A 1 694 ? 80.382 90.288  17.700  1.00 26.85 ? 694  TYR A CE1 1 
ATOM   5568 C CE2 . TYR A 1 694 ? 79.143 92.299  17.174  1.00 26.42 ? 694  TYR A CE2 1 
ATOM   5569 C CZ  . TYR A 1 694 ? 80.157 91.367  16.895  1.00 27.38 ? 694  TYR A CZ  1 
ATOM   5570 O OH  . TYR A 1 694 ? 80.961 91.560  15.810  1.00 26.68 ? 694  TYR A OH  1 
ATOM   5571 N N   . VAL A 1 695 ? 80.174 92.822  21.439  1.00 26.01 ? 695  VAL A N   1 
ATOM   5572 C CA  . VAL A 1 695 ? 80.598 94.177  21.403  1.00 25.30 ? 695  VAL A CA  1 
ATOM   5573 C C   . VAL A 1 695 ? 80.771 94.551  19.947  1.00 26.86 ? 695  VAL A C   1 
ATOM   5574 O O   . VAL A 1 695 ? 81.706 94.055  19.256  1.00 27.17 ? 695  VAL A O   1 
ATOM   5575 C CB  . VAL A 1 695 ? 81.942 94.383  22.138  1.00 27.20 ? 695  VAL A CB  1 
ATOM   5576 C CG1 . VAL A 1 695 ? 82.318 95.826  22.068  1.00 24.83 ? 695  VAL A CG1 1 
ATOM   5577 C CG2 . VAL A 1 695 ? 81.810 93.943  23.614  1.00 26.71 ? 695  VAL A CG2 1 
ATOM   5578 N N   . PRO A 1 696 ? 79.883 95.426  19.455  1.00 24.79 ? 696  PRO A N   1 
ATOM   5579 C CA  . PRO A 1 696 ? 79.934 95.817  18.066  1.00 24.78 ? 696  PRO A CA  1 
ATOM   5580 C C   . PRO A 1 696 ? 81.177 96.620  17.720  1.00 25.76 ? 696  PRO A C   1 
ATOM   5581 O O   . PRO A 1 696 ? 81.941 97.070  18.582  1.00 27.46 ? 696  PRO A O   1 
ATOM   5582 C CB  . PRO A 1 696 ? 78.674 96.711  17.893  1.00 24.59 ? 696  PRO A CB  1 
ATOM   5583 C CG  . PRO A 1 696 ? 77.755 96.313  19.054  1.00 24.40 ? 696  PRO A CG  1 
ATOM   5584 C CD  . PRO A 1 696 ? 78.747 96.031  20.181  1.00 23.85 ? 696  PRO A CD  1 
ATOM   5585 N N   . ASP A 1 697 ? 81.292 96.880  16.447  1.00 26.47 ? 697  ASP A N   1 
ATOM   5586 C CA  . ASP A 1 697 ? 82.431 97.533  15.876  1.00 27.90 ? 697  ASP A CA  1 
ATOM   5587 C C   . ASP A 1 697 ? 82.329 99.044  16.036  1.00 26.69 ? 697  ASP A C   1 
ATOM   5588 O O   . ASP A 1 697 ? 82.025 99.763  15.106  1.00 28.67 ? 697  ASP A O   1 
ATOM   5589 C CB  . ASP A 1 697 ? 82.545 97.072  14.417  1.00 28.29 ? 697  ASP A CB  1 
ATOM   5590 C CG  . ASP A 1 697 ? 83.708 97.704  13.675  1.00 32.80 ? 697  ASP A CG  1 
ATOM   5591 O OD1 . ASP A 1 697 ? 84.670 98.194  14.313  1.00 33.77 ? 697  ASP A OD1 1 
ATOM   5592 O OD2 . ASP A 1 697 ? 83.642 97.707  12.418  1.00 39.91 ? 697  ASP A OD2 1 
ATOM   5593 N N   . ALA A 1 698 ? 82.569 99.511  17.250  1.00 25.75 ? 698  ALA A N   1 
ATOM   5594 C CA  . ALA A 1 698 ? 82.652 100.920 17.544  1.00 25.71 ? 698  ALA A CA  1 
ATOM   5595 C C   . ALA A 1 698 ? 83.606 101.066 18.711  1.00 25.13 ? 698  ALA A C   1 
ATOM   5596 O O   . ALA A 1 698 ? 84.012 100.100 19.322  1.00 26.26 ? 698  ALA A O   1 
ATOM   5597 C CB  . ALA A 1 698 ? 81.232 101.488 17.944  1.00 24.95 ? 698  ALA A CB  1 
ATOM   5598 N N   . VAL A 1 699 ? 83.949 102.288 19.046  1.00 25.35 ? 699  VAL A N   1 
ATOM   5599 C CA  . VAL A 1 699 ? 84.611 102.546 20.308  1.00 24.78 ? 699  VAL A CA  1 
ATOM   5600 C C   . VAL A 1 699 ? 83.520 102.557 21.398  1.00 25.11 ? 699  VAL A C   1 
ATOM   5601 O O   . VAL A 1 699 ? 82.473 103.179 21.186  1.00 24.97 ? 699  VAL A O   1 
ATOM   5602 C CB  . VAL A 1 699 ? 85.252 103.953 20.290  1.00 25.27 ? 699  VAL A CB  1 
ATOM   5603 C CG1 . VAL A 1 699 ? 85.731 104.304 21.685  1.00 26.02 ? 699  VAL A CG1 1 
ATOM   5604 C CG2 . VAL A 1 699 ? 86.349 104.057 19.248  1.00 25.93 ? 699  VAL A CG2 1 
ATOM   5605 N N   . TRP A 1 700 ? 83.752 101.891 22.523  1.00 23.62 ? 700  TRP A N   1 
ATOM   5606 C CA  . TRP A 1 700 ? 82.795 101.861 23.632  1.00 24.34 ? 700  TRP A CA  1 
ATOM   5607 C C   . TRP A 1 700 ? 83.461 102.312 24.920  1.00 25.13 ? 700  TRP A C   1 
ATOM   5608 O O   . TRP A 1 700 ? 84.619 101.935 25.158  1.00 23.95 ? 700  TRP A O   1 
ATOM   5609 C CB  . TRP A 1 700 ? 82.271 100.455 23.871  1.00 23.69 ? 700  TRP A CB  1 
ATOM   5610 C CG  . TRP A 1 700 ? 81.472 99.954  22.671  1.00 23.71 ? 700  TRP A CG  1 
ATOM   5611 C CD1 . TRP A 1 700 ? 81.928 99.165  21.677  1.00 24.32 ? 700  TRP A CD1 1 
ATOM   5612 C CD2 . TRP A 1 700 ? 80.114 100.306 22.314  1.00 26.33 ? 700  TRP A CD2 1 
ATOM   5613 N NE1 . TRP A 1 700 ? 80.944 98.949  20.731  1.00 23.68 ? 700  TRP A NE1 1 
ATOM   5614 C CE2 . TRP A 1 700 ? 79.817 99.641  21.098  1.00 24.03 ? 700  TRP A CE2 1 
ATOM   5615 C CE3 . TRP A 1 700 ? 79.131 101.099 22.906  1.00 22.36 ? 700  TRP A CE3 1 
ATOM   5616 C CZ2 . TRP A 1 700 ? 78.588 99.756  20.468  1.00 23.58 ? 700  TRP A CZ2 1 
ATOM   5617 C CZ3 . TRP A 1 700 ? 77.903 101.210 22.287  1.00 23.07 ? 700  TRP A CZ3 1 
ATOM   5618 C CH2 . TRP A 1 700 ? 77.635 100.553 21.081  1.00 24.42 ? 700  TRP A CH2 1 
ATOM   5619 N N   . TYR A 1 701 ? 82.690 103.007 25.772  1.00 24.03 ? 701  TYR A N   1 
ATOM   5620 C CA  . TYR A 1 701 ? 83.151 103.427 27.093  1.00 24.24 ? 701  TYR A CA  1 
ATOM   5621 C C   . TYR A 1 701 ? 82.224 102.933 28.158  1.00 25.49 ? 701  TYR A C   1 
ATOM   5622 O O   . TYR A 1 701 ? 80.988 103.126 28.038  1.00 24.59 ? 701  TYR A O   1 
ATOM   5623 C CB  . TYR A 1 701 ? 83.146 104.939 27.188  1.00 23.25 ? 701  TYR A CB  1 
ATOM   5624 C CG  . TYR A 1 701 ? 83.962 105.598 26.138  1.00 23.60 ? 701  TYR A CG  1 
ATOM   5625 C CD1 . TYR A 1 701 ? 85.333 105.810 26.346  1.00 23.24 ? 701  TYR A CD1 1 
ATOM   5626 C CD2 . TYR A 1 701 ? 83.386 105.990 24.925  1.00 23.22 ? 701  TYR A CD2 1 
ATOM   5627 C CE1 . TYR A 1 701 ? 86.135 106.388 25.363  1.00 23.73 ? 701  TYR A CE1 1 
ATOM   5628 C CE2 . TYR A 1 701 ? 84.143 106.590 23.949  1.00 24.24 ? 701  TYR A CE2 1 
ATOM   5629 C CZ  . TYR A 1 701 ? 85.521 106.788 24.169  1.00 24.93 ? 701  TYR A CZ  1 
ATOM   5630 O OH  . TYR A 1 701 ? 86.265 107.399 23.188  1.00 24.06 ? 701  TYR A OH  1 
ATOM   5631 N N   . ASP A 1 702 ? 82.796 102.376 29.220  1.00 25.47 ? 702  ASP A N   1 
ATOM   5632 C CA  . ASP A 1 702 ? 82.063 102.097 30.436  1.00 27.81 ? 702  ASP A CA  1 
ATOM   5633 C C   . ASP A 1 702 ? 81.308 103.332 30.959  1.00 27.52 ? 702  ASP A C   1 
ATOM   5634 O O   . ASP A 1 702 ? 81.893 104.401 31.115  1.00 27.55 ? 702  ASP A O   1 
ATOM   5635 C CB  . ASP A 1 702 ? 83.011 101.545 31.489  1.00 28.51 ? 702  ASP A CB  1 
ATOM   5636 C CG  . ASP A 1 702 ? 82.277 101.002 32.684  1.00 32.86 ? 702  ASP A CG  1 
ATOM   5637 O OD1 . ASP A 1 702 ? 82.017 99.800  32.694  1.00 42.45 ? 702  ASP A OD1 1 
ATOM   5638 O OD2 . ASP A 1 702 ? 81.907 101.761 33.599  1.00 38.32 ? 702  ASP A OD2 1 
ATOM   5639 N N   . TYR A 1 703 ? 80.000 103.209 31.187  1.00 28.43 ? 703  TYR A N   1 
ATOM   5640 C CA  . TYR A 1 703 ? 79.211 104.394 31.514  1.00 28.93 ? 703  TYR A CA  1 
ATOM   5641 C C   . TYR A 1 703 ? 79.693 104.992 32.848  1.00 30.27 ? 703  TYR A C   1 
ATOM   5642 O O   . TYR A 1 703 ? 79.972 106.201 32.940  1.00 30.19 ? 703  TYR A O   1 
ATOM   5643 C CB  . TYR A 1 703 ? 77.708 104.087 31.562  1.00 29.86 ? 703  TYR A CB  1 
ATOM   5644 C CG  . TYR A 1 703 ? 76.889 105.234 32.133  1.00 31.40 ? 703  TYR A CG  1 
ATOM   5645 C CD1 . TYR A 1 703 ? 76.463 106.295 31.320  1.00 31.53 ? 703  TYR A CD1 1 
ATOM   5646 C CD2 . TYR A 1 703 ? 76.592 105.288 33.500  1.00 30.33 ? 703  TYR A CD2 1 
ATOM   5647 C CE1 . TYR A 1 703 ? 75.750 107.343 31.839  1.00 28.18 ? 703  TYR A CE1 1 
ATOM   5648 C CE2 . TYR A 1 703 ? 75.875 106.361 34.032  1.00 28.46 ? 703  TYR A CE2 1 
ATOM   5649 C CZ  . TYR A 1 703 ? 75.455 107.365 33.198  1.00 30.69 ? 703  TYR A CZ  1 
ATOM   5650 O OH  . TYR A 1 703 ? 74.715 108.405 33.731  1.00 32.66 ? 703  TYR A OH  1 
ATOM   5651 N N   . GLU A 1 704 ? 79.807 104.162 33.875  1.00 30.04 ? 704  GLU A N   1 
ATOM   5652 C CA  . GLU A 1 704 ? 80.198 104.674 35.173  1.00 32.61 ? 704  GLU A CA  1 
ATOM   5653 C C   . GLU A 1 704 ? 81.636 105.188 35.291  1.00 32.23 ? 704  GLU A C   1 
ATOM   5654 O O   . GLU A 1 704 ? 81.827 106.274 35.817  1.00 32.27 ? 704  GLU A O   1 
ATOM   5655 C CB  . GLU A 1 704 ? 79.854 103.698 36.290  1.00 33.89 ? 704  GLU A CB  1 
ATOM   5656 C CG  . GLU A 1 704 ? 78.331 103.679 36.518  1.00 38.95 ? 704  GLU A CG  1 
ATOM   5657 C CD  . GLU A 1 704 ? 77.925 102.917 37.743  1.00 45.61 ? 704  GLU A CD  1 
ATOM   5658 O OE1 . GLU A 1 704 ? 78.291 103.370 38.874  1.00 50.77 ? 704  GLU A OE1 1 
ATOM   5659 O OE2 . GLU A 1 704 ? 77.235 101.873 37.572  1.00 44.71 ? 704  GLU A OE2 1 
ATOM   5660 N N   . THR A 1 705 ? 82.630 104.464 34.782  1.00 31.53 ? 705  THR A N   1 
ATOM   5661 C CA  . THR A 1 705 ? 84.005 104.929 34.941  1.00 31.82 ? 705  THR A CA  1 
ATOM   5662 C C   . THR A 1 705 ? 84.443 105.834 33.827  1.00 30.55 ? 705  THR A C   1 
ATOM   5663 O O   . THR A 1 705 ? 85.398 106.595 33.990  1.00 30.60 ? 705  THR A O   1 
ATOM   5664 C CB  . THR A 1 705 ? 85.020 103.764 35.064  1.00 31.37 ? 705  THR A CB  1 
ATOM   5665 O OG1 . THR A 1 705 ? 85.102 103.077 33.825  1.00 33.46 ? 705  THR A OG1 1 
ATOM   5666 C CG2 . THR A 1 705 ? 84.569 102.783 36.118  1.00 34.56 ? 705  THR A CG2 1 
ATOM   5667 N N   . GLY A 1 706 ? 83.783 105.713 32.672  1.00 29.50 ? 706  GLY A N   1 
ATOM   5668 C CA  . GLY A 1 706 ? 84.194 106.444 31.492  1.00 28.03 ? 706  GLY A CA  1 
ATOM   5669 C C   . GLY A 1 706 ? 85.354 105.792 30.743  1.00 28.47 ? 706  GLY A C   1 
ATOM   5670 O O   . GLY A 1 706 ? 85.789 106.322 29.711  1.00 28.64 ? 706  GLY A O   1 
ATOM   5671 N N   . SER A 1 707 ? 85.874 104.664 31.216  1.00 28.41 ? 707  SER A N   1 
ATOM   5672 C CA  . SER A 1 707 ? 87.037 104.096 30.505  1.00 30.68 ? 707  SER A CA  1 
ATOM   5673 C C   . SER A 1 707 ? 86.736 103.322 29.221  1.00 29.95 ? 707  SER A C   1 
ATOM   5674 O O   . SER A 1 707 ? 85.750 102.606 29.120  1.00 29.56 ? 707  SER A O   1 
ATOM   5675 C CB  . SER A 1 707 ? 87.986 103.311 31.417  1.00 31.13 ? 707  SER A CB  1 
ATOM   5676 O OG  . SER A 1 707 ? 87.618 101.955 31.513  1.00 37.61 ? 707  SER A OG  1 
ATOM   5677 N N   . GLN A 1 708 ? 87.635 103.449 28.257  1.00 30.04 ? 708  GLN A N   1 
ATOM   5678 C CA  . GLN A 1 708 ? 87.482 102.775 26.989  1.00 30.93 ? 708  GLN A CA  1 
ATOM   5679 C C   . GLN A 1 708 ? 87.730 101.288 27.145  1.00 32.39 ? 708  GLN A C   1 
ATOM   5680 O O   . GLN A 1 708 ? 88.740 100.883 27.704  1.00 33.09 ? 708  GLN A O   1 
ATOM   5681 C CB  . GLN A 1 708 ? 88.399 103.403 25.959  1.00 31.13 ? 708  GLN A CB  1 
ATOM   5682 C CG  . GLN A 1 708 ? 88.204 102.793 24.590  1.00 32.38 ? 708  GLN A CG  1 
ATOM   5683 C CD  . GLN A 1 708 ? 89.021 103.423 23.522  1.00 36.20 ? 708  GLN A CD  1 
ATOM   5684 O OE1 . GLN A 1 708 ? 89.585 104.510 23.693  1.00 36.42 ? 708  GLN A OE1 1 
ATOM   5685 N NE2 . GLN A 1 708 ? 89.084 102.745 22.374  1.00 36.64 ? 708  GLN A NE2 1 
ATOM   5686 N N   . VAL A 1 709 ? 86.786 100.457 26.703  1.00 33.04 ? 709  VAL A N   1 
ATOM   5687 C CA  . VAL A 1 709 ? 86.961 99.030  26.811  1.00 34.22 ? 709  VAL A CA  1 
ATOM   5688 C C   . VAL A 1 709 ? 87.926 98.601  25.698  1.00 35.29 ? 709  VAL A C   1 
ATOM   5689 O O   . VAL A 1 709 ? 88.012 99.251  24.652  1.00 33.19 ? 709  VAL A O   1 
ATOM   5690 C CB  . VAL A 1 709 ? 85.609 98.261  26.717  1.00 34.92 ? 709  VAL A CB  1 
ATOM   5691 C CG1 . VAL A 1 709 ? 84.631 98.809  27.722  1.00 36.46 ? 709  VAL A CG1 1 
ATOM   5692 C CG2 . VAL A 1 709 ? 85.023 98.357  25.316  1.00 34.57 ? 709  VAL A CG2 1 
ATOM   5693 N N   . ARG A 1 710 ? 88.660 97.513  25.924  1.00 37.46 ? 710  ARG A N   1 
ATOM   5694 C CA  . ARG A 1 710 ? 89.592 97.035  24.896  1.00 40.14 ? 710  ARG A CA  1 
ATOM   5695 C C   . ARG A 1 710 ? 88.835 96.355  23.732  1.00 39.99 ? 710  ARG A C   1 
ATOM   5696 O O   . ARG A 1 710 ? 89.246 96.439  22.570  1.00 41.55 ? 710  ARG A O   1 
ATOM   5697 C CB  . ARG A 1 710 ? 90.647 96.113  25.506  1.00 41.25 ? 710  ARG A CB  1 
ATOM   5698 C CG  . ARG A 1 710 ? 91.806 96.861  26.209  1.00 48.30 ? 710  ARG A CG  1 
ATOM   5699 C CD  . ARG A 1 710 ? 92.624 97.708  25.203  1.00 58.60 ? 710  ARG A CD  1 
ATOM   5700 N NE  . ARG A 1 710 ? 93.642 98.579  25.814  1.00 65.32 ? 710  ARG A NE  1 
ATOM   5701 C CZ  . ARG A 1 710 ? 94.155 99.662  25.214  1.00 68.92 ? 710  ARG A CZ  1 
ATOM   5702 N NH1 . ARG A 1 710 ? 93.725 100.022 24.002  1.00 70.60 ? 710  ARG A NH1 1 
ATOM   5703 N NH2 . ARG A 1 710 ? 95.087 100.399 25.823  1.00 69.55 ? 710  ARG A NH2 1 
ATOM   5704 N N   . TRP A 1 711 ? 87.696 95.754  24.059  1.00 39.34 ? 711  TRP A N   1 
ATOM   5705 C CA  . TRP A 1 711 ? 86.801 95.084  23.117  1.00 37.96 ? 711  TRP A CA  1 
ATOM   5706 C C   . TRP A 1 711 ? 86.326 95.910  21.917  1.00 37.32 ? 711  TRP A C   1 
ATOM   5707 O O   . TRP A 1 711 ? 86.063 97.132  22.036  1.00 36.76 ? 711  TRP A O   1 
ATOM   5708 C CB  . TRP A 1 711 ? 85.576 94.664  23.875  1.00 38.79 ? 711  TRP A CB  1 
ATOM   5709 C CG  . TRP A 1 711 ? 85.830 93.919  25.137  1.00 40.19 ? 711  TRP A CG  1 
ATOM   5710 C CD1 . TRP A 1 711 ? 86.725 92.911  25.334  1.00 40.38 ? 711  TRP A CD1 1 
ATOM   5711 C CD2 . TRP A 1 711 ? 85.112 94.068  26.365  1.00 40.01 ? 711  TRP A CD2 1 
ATOM   5712 N NE1 . TRP A 1 711 ? 86.623 92.438  26.611  1.00 40.85 ? 711  TRP A NE1 1 
ATOM   5713 C CE2 . TRP A 1 711 ? 85.646 93.134  27.271  1.00 39.82 ? 711  TRP A CE2 1 
ATOM   5714 C CE3 . TRP A 1 711 ? 84.082 94.917  26.789  1.00 40.03 ? 711  TRP A CE3 1 
ATOM   5715 C CZ2 . TRP A 1 711 ? 85.176 93.004  28.582  1.00 40.61 ? 711  TRP A CZ2 1 
ATOM   5716 C CZ3 . TRP A 1 711 ? 83.612 94.798  28.097  1.00 40.46 ? 711  TRP A CZ3 1 
ATOM   5717 C CH2 . TRP A 1 711 ? 84.167 93.850  28.982  1.00 41.18 ? 711  TRP A CH2 1 
ATOM   5718 N N   . ARG A 1 712 ? 86.187 95.234  20.766  1.00 35.36 ? 712  ARG A N   1 
ATOM   5719 C CA  . ARG A 1 712 ? 85.642 95.847  19.543  1.00 33.79 ? 712  ARG A CA  1 
ATOM   5720 C C   . ARG A 1 712 ? 85.312 94.760  18.549  1.00 34.22 ? 712  ARG A C   1 
ATOM   5721 O O   . ARG A 1 712 ? 86.177 93.956  18.208  1.00 34.80 ? 712  ARG A O   1 
ATOM   5722 C CB  . ARG A 1 712 ? 86.622 96.802  18.895  1.00 33.62 ? 712  ARG A CB  1 
ATOM   5723 C CG  . ARG A 1 712 ? 86.059 97.484  17.685  1.00 32.34 ? 712  ARG A CG  1 
ATOM   5724 C CD  . ARG A 1 712 ? 86.847 98.711  17.282  1.00 34.63 ? 712  ARG A CD  1 
ATOM   5725 N NE  . ARG A 1 712 ? 86.110 99.394  16.241  1.00 36.92 ? 712  ARG A NE  1 
ATOM   5726 C CZ  . ARG A 1 712 ? 86.147 100.695 15.991  1.00 39.58 ? 712  ARG A CZ  1 
ATOM   5727 N NH1 . ARG A 1 712 ? 86.926 101.503 16.696  1.00 41.61 ? 712  ARG A NH1 1 
ATOM   5728 N NH2 . ARG A 1 712 ? 85.381 101.191 15.029  1.00 40.99 ? 712  ARG A NH2 1 
ATOM   5729 N N   . LYS A 1 713 ? 84.073 94.745  18.060  1.00 33.38 ? 713  LYS A N   1 
ATOM   5730 C CA  . LYS A 1 713 ? 83.664 93.756  17.039  1.00 33.08 ? 713  LYS A CA  1 
ATOM   5731 C C   . LYS A 1 713 ? 83.967 92.293  17.428  1.00 33.79 ? 713  LYS A C   1 
ATOM   5732 O O   . LYS A 1 713 ? 84.526 91.535  16.639  1.00 33.62 ? 713  LYS A O   1 
ATOM   5733 C CB  . LYS A 1 713 ? 84.263 94.100  15.655  1.00 32.62 ? 713  LYS A CB  1 
ATOM   5734 C CG  . LYS A 1 713 ? 83.409 93.532  14.509  1.00 32.30 ? 713  LYS A CG  1 
ATOM   5735 C CD  . LYS A 1 713 ? 83.887 93.851  13.122  1.00 31.83 ? 713  LYS A CD  1 
ATOM   5736 C CE  . LYS A 1 713 ? 82.884 93.232  12.083  1.00 31.08 ? 713  LYS A CE  1 
ATOM   5737 N NZ  . LYS A 1 713 ? 83.180 93.324  10.598  1.00 34.52 ? 713  LYS A NZ  1 
ATOM   5738 N N   . GLN A 1 714 ? 83.565 91.890  18.627  1.00 34.18 ? 714  GLN A N   1 
ATOM   5739 C CA  . GLN A 1 714 ? 83.881 90.556  19.143  1.00 35.13 ? 714  GLN A CA  1 
ATOM   5740 C C   . GLN A 1 714 ? 82.936 90.140  20.264  1.00 36.16 ? 714  GLN A C   1 
ATOM   5741 O O   . GLN A 1 714 ? 82.358 91.007  20.952  1.00 35.05 ? 714  GLN A O   1 
ATOM   5742 C CB  . GLN A 1 714 ? 85.334 90.550  19.675  1.00 35.67 ? 714  GLN A CB  1 
ATOM   5743 C CG  . GLN A 1 714 ? 85.574 91.500  20.833  1.00 33.66 ? 714  GLN A CG  1 
ATOM   5744 C CD  . GLN A 1 714 ? 87.056 91.629  21.179  1.00 37.18 ? 714  GLN A CD  1 
ATOM   5745 O OE1 . GLN A 1 714 ? 87.625 90.763  21.848  1.00 41.10 ? 714  GLN A OE1 1 
ATOM   5746 N NE2 . GLN A 1 714 ? 87.680 92.697  20.718  1.00 36.55 ? 714  GLN A NE2 1 
ATOM   5747 N N   . LYS A 1 715 ? 82.753 88.826  20.431  1.00 36.72 ? 715  LYS A N   1 
ATOM   5748 C CA  . LYS A 1 715 ? 82.104 88.269  21.594  1.00 39.53 ? 715  LYS A CA  1 
ATOM   5749 C C   . LYS A 1 715 ? 83.049 88.412  22.778  1.00 39.61 ? 715  LYS A C   1 
ATOM   5750 O O   . LYS A 1 715 ? 84.267 88.237  22.624  1.00 40.34 ? 715  LYS A O   1 
ATOM   5751 C CB  . LYS A 1 715 ? 81.773 86.789  21.412  1.00 39.18 ? 715  LYS A CB  1 
ATOM   5752 C CG  . LYS A 1 715 ? 80.526 86.539  20.592  1.00 42.64 ? 715  LYS A CG  1 
ATOM   5753 C CD  . LYS A 1 715 ? 80.170 85.063  20.462  1.00 43.08 ? 715  LYS A CD  1 
ATOM   5754 C CE  . LYS A 1 715 ? 79.097 84.856  19.364  1.00 48.99 ? 715  LYS A CE  1 
ATOM   5755 N NZ  . LYS A 1 715 ? 79.243 85.786  18.149  1.00 50.68 ? 715  LYS A NZ  1 
ATOM   5756 N N   . VAL A 1 716 ? 82.493 88.729  23.942  1.00 39.45 ? 716  VAL A N   1 
ATOM   5757 C CA  . VAL A 1 716 ? 83.268 88.877  25.164  1.00 41.12 ? 716  VAL A CA  1 
ATOM   5758 C C   . VAL A 1 716 ? 82.478 88.217  26.286  1.00 42.27 ? 716  VAL A C   1 
ATOM   5759 O O   . VAL A 1 716 ? 81.257 88.070  26.168  1.00 42.71 ? 716  VAL A O   1 
ATOM   5760 C CB  . VAL A 1 716 ? 83.526 90.377  25.499  1.00 41.64 ? 716  VAL A CB  1 
ATOM   5761 C CG1 . VAL A 1 716 ? 84.063 91.117  24.287  1.00 41.47 ? 716  VAL A CG1 1 
ATOM   5762 C CG2 . VAL A 1 716 ? 82.255 91.067  25.947  1.00 40.18 ? 716  VAL A CG2 1 
ATOM   5763 N N   . GLU A 1 717 ? 83.144 87.791  27.361  1.00 43.11 ? 717  GLU A N   1 
ATOM   5764 C CA  . GLU A 1 717 ? 82.403 87.523  28.592  1.00 44.67 ? 717  GLU A CA  1 
ATOM   5765 C C   . GLU A 1 717 ? 82.609 88.714  29.486  1.00 43.23 ? 717  GLU A C   1 
ATOM   5766 O O   . GLU A 1 717 ? 83.725 89.030  29.922  1.00 44.01 ? 717  GLU A O   1 
ATOM   5767 C CB  . GLU A 1 717 ? 82.705 86.154  29.263  1.00 45.12 ? 717  GLU A CB  1 
ATOM   5768 C CG  . GLU A 1 717 ? 83.849 86.085  30.283  1.00 48.40 ? 717  GLU A CG  1 
ATOM   5769 C CD  . GLU A 1 717 ? 84.079 84.650  30.850  1.00 49.90 ? 717  GLU A CD  1 
ATOM   5770 O OE1 . GLU A 1 717 ? 83.106 83.823  30.899  1.00 55.61 ? 717  GLU A OE1 1 
ATOM   5771 O OE2 . GLU A 1 717 ? 85.242 84.361  31.246  1.00 54.89 ? 717  GLU A OE2 1 
ATOM   5772 N N   . MET A 1 718 ? 81.520 89.439  29.660  1.00 42.26 ? 718  MET A N   1 
ATOM   5773 C CA  . MET A 1 718 ? 81.524 90.685  30.390  1.00 40.67 ? 718  MET A CA  1 
ATOM   5774 C C   . MET A 1 718 ? 81.274 90.317  31.825  1.00 39.33 ? 718  MET A C   1 
ATOM   5775 O O   . MET A 1 718 ? 80.316 89.625  32.116  1.00 39.26 ? 718  MET A O   1 
ATOM   5776 C CB  . MET A 1 718 ? 80.404 91.576  29.818  1.00 40.50 ? 718  MET A CB  1 
ATOM   5777 C CG  . MET A 1 718 ? 80.545 93.039  30.133  1.00 41.08 ? 718  MET A CG  1 
ATOM   5778 S SD  . MET A 1 718 ? 79.118 93.895  29.438  1.00 40.86 ? 718  MET A SD  1 
ATOM   5779 C CE  . MET A 1 718 ? 79.611 94.031  27.714  1.00 36.73 ? 718  MET A CE  1 
ATOM   5780 N N   . GLU A 1 719 ? 82.141 90.773  32.721  1.00 39.50 ? 719  GLU A N   1 
ATOM   5781 C CA  . GLU A 1 719 ? 82.051 90.432  34.142  1.00 40.16 ? 719  GLU A CA  1 
ATOM   5782 C C   . GLU A 1 719 ? 80.971 91.334  34.788  1.00 37.54 ? 719  GLU A C   1 
ATOM   5783 O O   . GLU A 1 719 ? 81.115 92.553  34.814  1.00 37.16 ? 719  GLU A O   1 
ATOM   5784 C CB  . GLU A 1 719 ? 83.413 90.656  34.803  1.00 40.51 ? 719  GLU A CB  1 
ATOM   5785 C CG  . GLU A 1 719 ? 83.535 90.052  36.219  1.00 45.83 ? 719  GLU A CG  1 
ATOM   5786 C CD  . GLU A 1 719 ? 84.621 90.733  37.084  1.00 46.74 ? 719  GLU A CD  1 
ATOM   5787 O OE1 . GLU A 1 719 ? 85.800 90.792  36.632  1.00 54.07 ? 719  GLU A OE1 1 
ATOM   5788 O OE2 . GLU A 1 719 ? 84.292 91.190  38.224  1.00 54.42 ? 719  GLU A OE2 1 
ATOM   5789 N N   . LEU A 1 720 ? 79.893 90.742  35.294  1.00 34.27 ? 720  LEU A N   1 
ATOM   5790 C CA  . LEU A 1 720 ? 78.811 91.537  35.854  1.00 32.43 ? 720  LEU A CA  1 
ATOM   5791 C C   . LEU A 1 720 ? 78.305 90.958  37.165  1.00 31.22 ? 720  LEU A C   1 
ATOM   5792 O O   . LEU A 1 720 ? 77.384 90.122  37.171  1.00 30.98 ? 720  LEU A O   1 
ATOM   5793 C CB  . LEU A 1 720 ? 77.670 91.714  34.822  1.00 31.26 ? 720  LEU A CB  1 
ATOM   5794 C CG  . LEU A 1 720 ? 77.994 92.379  33.490  1.00 30.18 ? 720  LEU A CG  1 
ATOM   5795 C CD1 . LEU A 1 720 ? 76.878 92.134  32.445  1.00 31.30 ? 720  LEU A CD1 1 
ATOM   5796 C CD2 . LEU A 1 720 ? 78.214 93.846  33.664  1.00 31.78 ? 720  LEU A CD2 1 
ATOM   5797 N N   . PRO A 1 721 ? 78.915 91.387  38.286  1.00 30.79 ? 721  PRO A N   1 
ATOM   5798 C CA  . PRO A 1 721 ? 78.539 90.896  39.602  1.00 30.54 ? 721  PRO A CA  1 
ATOM   5799 C C   . PRO A 1 721 ? 77.069 91.239  39.916  1.00 31.14 ? 721  PRO A C   1 
ATOM   5800 O O   . PRO A 1 721 ? 76.400 91.933  39.119  1.00 30.04 ? 721  PRO A O   1 
ATOM   5801 C CB  . PRO A 1 721 ? 79.439 91.671  40.553  1.00 31.71 ? 721  PRO A CB  1 
ATOM   5802 C CG  . PRO A 1 721 ? 80.528 92.265  39.699  1.00 31.92 ? 721  PRO A CG  1 
ATOM   5803 C CD  . PRO A 1 721 ? 80.011 92.368  38.319  1.00 30.67 ? 721  PRO A CD  1 
ATOM   5804 N N   . GLY A 1 722 ? 76.606 90.772  41.069  1.00 29.94 ? 722  GLY A N   1 
ATOM   5805 C CA  . GLY A 1 722 ? 75.207 90.861  41.472  1.00 30.44 ? 722  GLY A CA  1 
ATOM   5806 C C   . GLY A 1 722 ? 74.613 92.255  41.383  1.00 30.65 ? 722  GLY A C   1 
ATOM   5807 O O   . GLY A 1 722 ? 73.400 92.401  41.268  1.00 29.79 ? 722  GLY A O   1 
ATOM   5808 N N   . ASP A 1 723 ? 75.456 93.276  41.483  1.00 30.58 ? 723  ASP A N   1 
ATOM   5809 C CA  . ASP A 1 723 ? 74.956 94.625  41.562  1.00 31.19 ? 723  ASP A CA  1 
ATOM   5810 C C   . ASP A 1 723 ? 75.128 95.386  40.262  1.00 30.72 ? 723  ASP A C   1 
ATOM   5811 O O   . ASP A 1 723 ? 74.833 96.574  40.259  1.00 31.37 ? 723  ASP A O   1 
ATOM   5812 C CB  . ASP A 1 723 ? 75.601 95.406  42.723  1.00 33.01 ? 723  ASP A CB  1 
ATOM   5813 C CG  . ASP A 1 723 ? 77.141 95.545  42.583  1.00 37.13 ? 723  ASP A CG  1 
ATOM   5814 O OD1 . ASP A 1 723 ? 77.786 94.715  41.890  1.00 40.72 ? 723  ASP A OD1 1 
ATOM   5815 O OD2 . ASP A 1 723 ? 77.734 96.471  43.204  1.00 44.58 ? 723  ASP A OD2 1 
ATOM   5816 N N   . LYS A 1 724 ? 75.597 94.728  39.185  1.00 28.89 ? 724  LYS A N   1 
ATOM   5817 C CA  . LYS A 1 724 ? 75.921 95.398  37.905  1.00 27.64 ? 724  LYS A CA  1 
ATOM   5818 C C   . LYS A 1 724 ? 75.128 94.926  36.656  1.00 27.11 ? 724  LYS A C   1 
ATOM   5819 O O   . LYS A 1 724 ? 74.782 93.759  36.532  1.00 27.25 ? 724  LYS A O   1 
ATOM   5820 C CB  . LYS A 1 724 ? 77.426 95.331  37.624  1.00 28.48 ? 724  LYS A CB  1 
ATOM   5821 C CG  . LYS A 1 724 ? 78.319 96.046  38.675  1.00 30.13 ? 724  LYS A CG  1 
ATOM   5822 C CD  . LYS A 1 724 ? 78.135 97.562  38.657  1.00 32.94 ? 724  LYS A CD  1 
ATOM   5823 C CE  . LYS A 1 724 ? 78.917 98.319  39.761  1.00 35.97 ? 724  LYS A CE  1 
ATOM   5824 N NZ  . LYS A 1 724 ? 78.058 99.473  40.315  1.00 38.35 ? 724  LYS A NZ  1 
ATOM   5825 N N   . ILE A 1 725 ? 74.823 95.880  35.775  1.00 26.11 ? 725  ILE A N   1 
ATOM   5826 C CA  . ILE A 1 725 ? 74.373 95.636  34.415  1.00 25.01 ? 725  ILE A CA  1 
ATOM   5827 C C   . ILE A 1 725 ? 75.356 96.326  33.480  1.00 24.24 ? 725  ILE A C   1 
ATOM   5828 O O   . ILE A 1 725 ? 75.898 97.374  33.822  1.00 24.80 ? 725  ILE A O   1 
ATOM   5829 C CB  . ILE A 1 725 ? 72.881 96.105  34.190  1.00 25.30 ? 725  ILE A CB  1 
ATOM   5830 C CG1 . ILE A 1 725 ? 72.440 95.945  32.729  1.00 24.89 ? 725  ILE A CG1 1 
ATOM   5831 C CG2 . ILE A 1 725 ? 72.651 97.580  34.687  1.00 23.14 ? 725  ILE A CG2 1 
ATOM   5832 C CD1 . ILE A 1 725 ? 70.953 95.850  32.598  1.00 26.76 ? 725  ILE A CD1 1 
ATOM   5833 N N   . GLY A 1 726 ? 75.617 95.746  32.307  1.00 23.72 ? 726  GLY A N   1 
ATOM   5834 C CA  . GLY A 1 726 ? 76.563 96.384  31.385  1.00 22.88 ? 726  GLY A CA  1 
ATOM   5835 C C   . GLY A 1 726 ? 75.913 97.590  30.720  1.00 23.47 ? 726  GLY A C   1 
ATOM   5836 O O   . GLY A 1 726 ? 74.815 97.478  30.177  1.00 22.96 ? 726  GLY A O   1 
ATOM   5837 N N   . LEU A 1 727 ? 76.584 98.732  30.779  1.00 22.38 ? 727  LEU A N   1 
ATOM   5838 C CA  . LEU A 1 727 ? 76.162 99.967  30.148  1.00 23.54 ? 727  LEU A CA  1 
ATOM   5839 C C   . LEU A 1 727 ? 77.373 100.637 29.524  1.00 23.47 ? 727  LEU A C   1 
ATOM   5840 O O   . LEU A 1 727 ? 78.300 101.051 30.242  1.00 24.17 ? 727  LEU A O   1 
ATOM   5841 C CB  . LEU A 1 727 ? 75.520 100.941 31.170  1.00 23.63 ? 727  LEU A CB  1 
ATOM   5842 C CG  . LEU A 1 727 ? 74.259 100.518 31.936  1.00 23.58 ? 727  LEU A CG  1 
ATOM   5843 C CD1 . LEU A 1 727 ? 73.892 101.541 33.016  1.00 22.76 ? 727  LEU A CD1 1 
ATOM   5844 C CD2 . LEU A 1 727 ? 73.150 100.343 30.933  1.00 22.26 ? 727  LEU A CD2 1 
ATOM   5845 N N   . HIS A 1 728 ? 77.336 100.799 28.207  1.00 21.73 ? 728  HIS A N   1 
ATOM   5846 C CA  . HIS A 1 728 ? 78.462 101.347 27.471  1.00 21.66 ? 728  HIS A CA  1 
ATOM   5847 C C   . HIS A 1 728 ? 77.994 102.402 26.509  1.00 22.09 ? 728  HIS A C   1 
ATOM   5848 O O   . HIS A 1 728 ? 76.931 102.260 25.879  1.00 21.64 ? 728  HIS A O   1 
ATOM   5849 C CB  . HIS A 1 728 ? 79.197 100.233 26.701  1.00 22.32 ? 728  HIS A CB  1 
ATOM   5850 C CG  . HIS A 1 728 ? 79.875 99.287  27.615  1.00 21.78 ? 728  HIS A CG  1 
ATOM   5851 N ND1 . HIS A 1 728 ? 79.241 98.186  28.125  1.00 25.09 ? 728  HIS A ND1 1 
ATOM   5852 C CD2 . HIS A 1 728 ? 81.099 99.326  28.199  1.00 23.55 ? 728  HIS A CD2 1 
ATOM   5853 C CE1 . HIS A 1 728 ? 80.045 97.572  28.980  1.00 26.12 ? 728  HIS A CE1 1 
ATOM   5854 N NE2 . HIS A 1 728 ? 81.184 98.242  29.034  1.00 24.65 ? 728  HIS A NE2 1 
ATOM   5855 N N   . LEU A 1 729 ? 78.803 103.432 26.387  1.00 20.38 ? 729  LEU A N   1 
ATOM   5856 C CA  . LEU A 1 729 ? 78.491 104.555 25.531  1.00 20.69 ? 729  LEU A CA  1 
ATOM   5857 C C   . LEU A 1 729 ? 79.347 104.461 24.289  1.00 21.23 ? 729  LEU A C   1 
ATOM   5858 O O   . LEU A 1 729 ? 80.491 104.084 24.378  1.00 19.67 ? 729  LEU A O   1 
ATOM   5859 C CB  . LEU A 1 729 ? 78.820 105.840 26.236  1.00 20.87 ? 729  LEU A CB  1 
ATOM   5860 C CG  . LEU A 1 729 ? 78.065 106.107 27.550  1.00 23.37 ? 729  LEU A CG  1 
ATOM   5861 C CD1 . LEU A 1 729 ? 78.644 107.321 28.204  1.00 22.88 ? 729  LEU A CD1 1 
ATOM   5862 C CD2 . LEU A 1 729 ? 76.577 106.278 27.232  1.00 22.67 ? 729  LEU A CD2 1 
ATOM   5863 N N   . ARG A 1 730 ? 78.753 104.794 23.168  1.00 20.35 ? 730  ARG A N   1 
ATOM   5864 C CA  . ARG A 1 730 ? 79.322 104.647 21.870  1.00 21.21 ? 730  ARG A CA  1 
ATOM   5865 C C   . ARG A 1 730 ? 80.066 105.888 21.512  1.00 21.82 ? 730  ARG A C   1 
ATOM   5866 O O   . ARG A 1 730 ? 79.531 107.007 21.587  1.00 21.99 ? 730  ARG A O   1 
ATOM   5867 C CB  . ARG A 1 730 ? 78.216 104.368 20.851  1.00 20.17 ? 730  ARG A CB  1 
ATOM   5868 C CG  . ARG A 1 730 ? 78.718 104.135 19.441  1.00 20.14 ? 730  ARG A CG  1 
ATOM   5869 C CD  . ARG A 1 730 ? 77.553 103.773 18.567  1.00 18.78 ? 730  ARG A CD  1 
ATOM   5870 N NE  . ARG A 1 730 ? 77.856 103.690 17.135  1.00 20.52 ? 730  ARG A NE  1 
ATOM   5871 C CZ  . ARG A 1 730 ? 76.906 103.601 16.206  1.00 19.51 ? 730  ARG A CZ  1 
ATOM   5872 N NH1 . ARG A 1 730 ? 75.636 103.625 16.577  1.00 21.76 ? 730  ARG A NH1 1 
ATOM   5873 N NH2 . ARG A 1 730 ? 77.216 103.481 14.921  1.00 22.68 ? 730  ARG A NH2 1 
ATOM   5874 N N   . GLY A 1 731 ? 81.325 105.685 21.153  1.00 21.25 ? 731  GLY A N   1 
ATOM   5875 C CA  . GLY A 1 731 ? 82.162 106.762 20.631  1.00 22.90 ? 731  GLY A CA  1 
ATOM   5876 C C   . GLY A 1 731 ? 81.567 107.364 19.390  1.00 23.29 ? 731  GLY A C   1 
ATOM   5877 O O   . GLY A 1 731 ? 81.080 106.664 18.485  1.00 24.05 ? 731  GLY A O   1 
ATOM   5878 N N   . GLY A 1 732 ? 81.614 108.674 19.332  1.00 22.62 ? 732  GLY A N   1 
ATOM   5879 C CA  . GLY A 1 732 ? 80.959 109.397 18.286  1.00 23.22 ? 732  GLY A CA  1 
ATOM   5880 C C   . GLY A 1 732 ? 79.706 110.110 18.684  1.00 22.39 ? 732  GLY A C   1 
ATOM   5881 O O   . GLY A 1 732 ? 79.140 110.795 17.864  1.00 22.72 ? 732  GLY A O   1 
ATOM   5882 N N   . TYR A 1 733 ? 79.283 109.979 19.944  1.00 21.77 ? 733  TYR A N   1 
ATOM   5883 C CA  . TYR A 1 733 ? 77.963 110.466 20.374  1.00 22.07 ? 733  TYR A CA  1 
ATOM   5884 C C   . TYR A 1 733 ? 78.057 111.317 21.619  1.00 21.74 ? 733  TYR A C   1 
ATOM   5885 O O   . TYR A 1 733 ? 78.886 111.061 22.482  1.00 22.16 ? 733  TYR A O   1 
ATOM   5886 C CB  . TYR A 1 733 ? 76.990 109.260 20.647  1.00 22.51 ? 733  TYR A CB  1 
ATOM   5887 C CG  . TYR A 1 733 ? 76.672 108.615 19.331  1.00 24.67 ? 733  TYR A CG  1 
ATOM   5888 C CD1 . TYR A 1 733 ? 75.573 109.033 18.579  1.00 22.60 ? 733  TYR A CD1 1 
ATOM   5889 C CD2 . TYR A 1 733 ? 77.567 107.691 18.762  1.00 25.95 ? 733  TYR A CD2 1 
ATOM   5890 C CE1 . TYR A 1 733 ? 75.325 108.471 17.309  1.00 25.80 ? 733  TYR A CE1 1 
ATOM   5891 C CE2 . TYR A 1 733 ? 77.347 107.155 17.484  1.00 25.59 ? 733  TYR A CE2 1 
ATOM   5892 C CZ  . TYR A 1 733 ? 76.218 107.541 16.784  1.00 25.65 ? 733  TYR A CZ  1 
ATOM   5893 O OH  . TYR A 1 733 ? 76.017 106.968 15.535  1.00 25.96 ? 733  TYR A OH  1 
ATOM   5894 N N   . ILE A 1 734 ? 77.179 112.305 21.690  1.00 22.02 ? 734  ILE A N   1 
ATOM   5895 C CA  . ILE A 1 734 ? 77.074 113.200 22.829  1.00 20.53 ? 734  ILE A CA  1 
ATOM   5896 C C   . ILE A 1 734 ? 75.702 112.981 23.504  1.00 22.36 ? 734  ILE A C   1 
ATOM   5897 O O   . ILE A 1 734 ? 74.674 113.005 22.825  1.00 23.34 ? 734  ILE A O   1 
ATOM   5898 C CB  . ILE A 1 734 ? 77.266 114.623 22.395  1.00 20.03 ? 734  ILE A CB  1 
ATOM   5899 C CG1 . ILE A 1 734 ? 78.709 114.778 21.800  1.00 17.19 ? 734  ILE A CG1 1 
ATOM   5900 C CG2 . ILE A 1 734 ? 77.084 115.582 23.615  1.00 14.76 ? 734  ILE A CG2 1 
ATOM   5901 C CD1 . ILE A 1 734 ? 78.944 116.109 21.089  1.00 17.10 ? 734  ILE A CD1 1 
ATOM   5902 N N   . PHE A 1 735 ? 75.701 112.767 24.815  1.00 21.13 ? 735  PHE A N   1 
ATOM   5903 C CA  . PHE A 1 735 ? 74.495 112.382 25.513  1.00 22.16 ? 735  PHE A CA  1 
ATOM   5904 C C   . PHE A 1 735 ? 74.171 113.501 26.492  1.00 22.15 ? 735  PHE A C   1 
ATOM   5905 O O   . PHE A 1 735 ? 74.965 113.799 27.360  1.00 22.87 ? 735  PHE A O   1 
ATOM   5906 C CB  . PHE A 1 735 ? 74.723 111.069 26.279  1.00 21.30 ? 735  PHE A CB  1 
ATOM   5907 C CG  . PHE A 1 735 ? 75.241 109.919 25.397  1.00 23.20 ? 735  PHE A CG  1 
ATOM   5908 C CD1 . PHE A 1 735 ? 74.390 108.909 24.976  1.00 22.52 ? 735  PHE A CD1 1 
ATOM   5909 C CD2 . PHE A 1 735 ? 76.598 109.834 25.036  1.00 20.83 ? 735  PHE A CD2 1 
ATOM   5910 C CE1 . PHE A 1 735 ? 74.866 107.855 24.131  1.00 22.24 ? 735  PHE A CE1 1 
ATOM   5911 C CE2 . PHE A 1 735 ? 77.061 108.769 24.199  1.00 18.64 ? 735  PHE A CE2 1 
ATOM   5912 C CZ  . PHE A 1 735 ? 76.198 107.813 23.757  1.00 22.13 ? 735  PHE A CZ  1 
ATOM   5913 N N   . PRO A 1 736 ? 73.009 114.133 26.339  1.00 21.57 ? 736  PRO A N   1 
ATOM   5914 C CA  . PRO A 1 736 ? 72.620 115.132 27.361  1.00 21.33 ? 736  PRO A CA  1 
ATOM   5915 C C   . PRO A 1 736 ? 72.062 114.455 28.612  1.00 22.06 ? 736  PRO A C   1 
ATOM   5916 O O   . PRO A 1 736 ? 71.390 113.413 28.524  1.00 22.50 ? 736  PRO A O   1 
ATOM   5917 C CB  . PRO A 1 736 ? 71.520 115.931 26.677  1.00 20.51 ? 736  PRO A CB  1 
ATOM   5918 C CG  . PRO A 1 736 ? 70.929 114.976 25.665  1.00 21.54 ? 736  PRO A CG  1 
ATOM   5919 C CD  . PRO A 1 736 ? 72.012 113.968 25.270  1.00 20.35 ? 736  PRO A CD  1 
ATOM   5920 N N   . THR A 1 737 ? 72.337 115.033 29.778  1.00 20.69 ? 737  THR A N   1 
ATOM   5921 C CA  . THR A 1 737 ? 71.934 114.427 31.027  1.00 22.01 ? 737  THR A CA  1 
ATOM   5922 C C   . THR A 1 737 ? 71.393 115.523 31.944  1.00 20.75 ? 737  THR A C   1 
ATOM   5923 O O   . THR A 1 737 ? 71.658 116.693 31.730  1.00 18.76 ? 737  THR A O   1 
ATOM   5924 C CB  . THR A 1 737 ? 73.122 113.757 31.758  1.00 22.91 ? 737  THR A CB  1 
ATOM   5925 O OG1 . THR A 1 737 ? 74.093 114.755 32.097  1.00 27.40 ? 737  THR A OG1 1 
ATOM   5926 C CG2 . THR A 1 737 ? 73.837 112.702 30.864  1.00 24.81 ? 737  THR A CG2 1 
ATOM   5927 N N   . GLN A 1 738 ? 70.631 115.137 32.963  1.00 20.24 ? 738  GLN A N   1 
ATOM   5928 C CA  . GLN A 1 738 ? 70.166 116.097 33.933  1.00 21.47 ? 738  GLN A CA  1 
ATOM   5929 C C   . GLN A 1 738 ? 70.305 115.428 35.291  1.00 23.51 ? 738  GLN A C   1 
ATOM   5930 O O   . GLN A 1 738 ? 69.865 114.288 35.456  1.00 24.54 ? 738  GLN A O   1 
ATOM   5931 C CB  . GLN A 1 738 ? 68.707 116.500 33.664  1.00 21.90 ? 738  GLN A CB  1 
ATOM   5932 C CG  . GLN A 1 738 ? 68.158 117.600 34.605  1.00 18.52 ? 738  GLN A CG  1 
ATOM   5933 C CD  . GLN A 1 738 ? 66.893 118.229 34.052  1.00 22.16 ? 738  GLN A CD  1 
ATOM   5934 O OE1 . GLN A 1 738 ? 65.999 117.517 33.566  1.00 20.76 ? 738  GLN A OE1 1 
ATOM   5935 N NE2 . GLN A 1 738 ? 66.808 119.569 34.107  1.00 19.30 ? 738  GLN A NE2 1 
ATOM   5936 N N   . GLN A 1 739 ? 70.818 116.150 36.292  1.00 22.59 ? 739  GLN A N   1 
ATOM   5937 C CA  . GLN A 1 739 ? 70.969 115.564 37.604  1.00 23.94 ? 739  GLN A CA  1 
ATOM   5938 C C   . GLN A 1 739 ? 69.641 115.020 38.105  1.00 22.88 ? 739  GLN A C   1 
ATOM   5939 O O   . GLN A 1 739 ? 68.657 115.702 38.065  1.00 22.60 ? 739  GLN A O   1 
ATOM   5940 C CB  . GLN A 1 739 ? 71.532 116.551 38.629  1.00 23.59 ? 739  GLN A CB  1 
ATOM   5941 C CG  . GLN A 1 739 ? 72.671 117.323 38.049  1.00 30.59 ? 739  GLN A CG  1 
ATOM   5942 C CD  . GLN A 1 739 ? 73.456 118.078 39.117  1.00 38.18 ? 739  GLN A CD  1 
ATOM   5943 O OE1 . GLN A 1 739 ? 72.935 118.334 40.224  1.00 37.82 ? 739  GLN A OE1 1 
ATOM   5944 N NE2 . GLN A 1 739 ? 74.718 118.435 38.791  1.00 37.36 ? 739  GLN A NE2 1 
ATOM   5945 N N   . PRO A 1 740 ? 69.653 113.793 38.611  1.00 22.93 ? 740  PRO A N   1 
ATOM   5946 C CA  . PRO A 1 740 ? 68.443 113.060 38.915  1.00 23.32 ? 740  PRO A CA  1 
ATOM   5947 C C   . PRO A 1 740 ? 67.821 113.560 40.241  1.00 24.09 ? 740  PRO A C   1 
ATOM   5948 O O   . PRO A 1 740 ? 68.482 114.188 41.061  1.00 24.53 ? 740  PRO A O   1 
ATOM   5949 C CB  . PRO A 1 740 ? 68.955 111.628 39.081  1.00 22.88 ? 740  PRO A CB  1 
ATOM   5950 C CG  . PRO A 1 740 ? 70.370 111.782 39.537  1.00 22.72 ? 740  PRO A CG  1 
ATOM   5951 C CD  . PRO A 1 740 ? 70.875 112.998 38.847  1.00 22.70 ? 740  PRO A CD  1 
ATOM   5952 N N   . ASN A 1 741 ? 66.580 113.197 40.458  1.00 22.77 ? 741  ASN A N   1 
ATOM   5953 C CA  . ASN A 1 741 ? 65.945 113.391 41.739  1.00 22.92 ? 741  ASN A CA  1 
ATOM   5954 C C   . ASN A 1 741 ? 64.909 112.292 41.707  1.00 22.46 ? 741  ASN A C   1 
ATOM   5955 O O   . ASN A 1 741 ? 64.864 111.534 40.745  1.00 23.52 ? 741  ASN A O   1 
ATOM   5956 C CB  . ASN A 1 741 ? 65.337 114.786 41.833  1.00 21.67 ? 741  ASN A CB  1 
ATOM   5957 C CG  . ASN A 1 741 ? 65.124 115.223 43.276  1.00 23.39 ? 741  ASN A CG  1 
ATOM   5958 O OD1 . ASN A 1 741 ? 64.937 114.386 44.178  1.00 25.29 ? 741  ASN A OD1 1 
ATOM   5959 N ND2 . ASN A 1 741 ? 65.101 116.508 43.483  1.00 23.33 ? 741  ASN A ND2 1 
ATOM   5960 N N   . THR A 1 742 ? 64.064 112.195 42.701  1.00 22.92 ? 742  THR A N   1 
ATOM   5961 C CA  . THR A 1 742 ? 63.184 111.026 42.841  1.00 23.09 ? 742  THR A CA  1 
ATOM   5962 C C   . THR A 1 742 ? 61.892 111.151 42.064  1.00 22.68 ? 742  THR A C   1 
ATOM   5963 O O   . THR A 1 742 ? 61.099 110.198 42.010  1.00 23.96 ? 742  THR A O   1 
ATOM   5964 C CB  . THR A 1 742 ? 62.900 110.761 44.331  1.00 23.43 ? 742  THR A CB  1 
ATOM   5965 O OG1 . THR A 1 742 ? 62.282 111.914 44.888  1.00 24.89 ? 742  THR A OG1 1 
ATOM   5966 C CG2 . THR A 1 742 ? 64.214 110.498 45.097  1.00 23.20 ? 742  THR A CG2 1 
ATOM   5967 N N   . THR A 1 743 ? 61.630 112.345 41.530  1.00 22.19 ? 743  THR A N   1 
ATOM   5968 C CA  . THR A 1 743 ? 60.507 112.563 40.585  1.00 21.10 ? 743  THR A CA  1 
ATOM   5969 C C   . THR A 1 743 ? 61.031 113.408 39.412  1.00 21.29 ? 743  THR A C   1 
ATOM   5970 O O   . THR A 1 743 ? 61.996 114.192 39.581  1.00 20.93 ? 743  THR A O   1 
ATOM   5971 C CB  . THR A 1 743 ? 59.275 113.328 41.211  1.00 21.93 ? 743  THR A CB  1 
ATOM   5972 O OG1 . THR A 1 743 ? 59.696 114.619 41.620  1.00 24.99 ? 743  THR A OG1 1 
ATOM   5973 C CG2 . THR A 1 743 ? 58.677 112.576 42.409  1.00 23.51 ? 743  THR A CG2 1 
ATOM   5974 N N   . THR A 1 744 ? 60.417 113.246 38.243  1.00 20.44 ? 744  THR A N   1 
ATOM   5975 C CA  . THR A 1 744 ? 60.727 114.067 37.083  1.00 21.38 ? 744  THR A CA  1 
ATOM   5976 C C   . THR A 1 744 ? 60.266 115.487 37.294  1.00 23.35 ? 744  THR A C   1 
ATOM   5977 O O   . THR A 1 744 ? 60.891 116.427 36.772  1.00 23.25 ? 744  THR A O   1 
ATOM   5978 C CB  . THR A 1 744 ? 60.198 113.470 35.790  1.00 21.83 ? 744  THR A CB  1 
ATOM   5979 O OG1 . THR A 1 744 ? 58.776 113.482 35.808  1.00 21.94 ? 744  THR A OG1 1 
ATOM   5980 C CG2 . THR A 1 744 ? 60.681 112.028 35.629  1.00 19.35 ? 744  THR A CG2 1 
ATOM   5981 N N   . LEU A 1 745 ? 59.234 115.688 38.125  1.00 22.95 ? 745  LEU A N   1 
ATOM   5982 C CA  . LEU A 1 745 ? 58.812 117.056 38.423  1.00 23.82 ? 745  LEU A CA  1 
ATOM   5983 C C   . LEU A 1 745 ? 60.004 117.838 38.999  1.00 24.08 ? 745  LEU A C   1 
ATOM   5984 O O   . LEU A 1 745 ? 60.335 118.972 38.583  1.00 24.90 ? 745  LEU A O   1 
ATOM   5985 C CB  . LEU A 1 745 ? 57.613 117.061 39.400  1.00 23.90 ? 745  LEU A CB  1 
ATOM   5986 C CG  . LEU A 1 745 ? 57.265 118.437 39.957  1.00 25.77 ? 745  LEU A CG  1 
ATOM   5987 C CD1 . LEU A 1 745 ? 56.483 119.156 38.918  1.00 28.58 ? 745  LEU A CD1 1 
ATOM   5988 C CD2 . LEU A 1 745 ? 56.453 118.328 41.246  1.00 31.98 ? 745  LEU A CD2 1 
ATOM   5989 N N   . ALA A 1 746 ? 60.715 117.189 39.912  1.00 23.37 ? 746  ALA A N   1 
ATOM   5990 C CA  . ALA A 1 746 ? 61.847 117.802 40.541  1.00 22.14 ? 746  ALA A CA  1 
ATOM   5991 C C   . ALA A 1 746 ? 63.140 117.698 39.668  1.00 22.23 ? 746  ALA A C   1 
ATOM   5992 O O   . ALA A 1 746 ? 63.863 118.644 39.558  1.00 20.66 ? 746  ALA A O   1 
ATOM   5993 C CB  . ALA A 1 746 ? 62.058 117.147 41.921  1.00 21.34 ? 746  ALA A CB  1 
ATOM   5994 N N   . SER A 1 747 ? 63.397 116.546 39.043  1.00 21.85 ? 747  SER A N   1 
ATOM   5995 C CA  . SER A 1 747 ? 64.604 116.380 38.242  1.00 22.45 ? 747  SER A CA  1 
ATOM   5996 C C   . SER A 1 747 ? 64.686 117.390 37.083  1.00 22.49 ? 747  SER A C   1 
ATOM   5997 O O   . SER A 1 747 ? 65.763 117.927 36.802  1.00 21.78 ? 747  SER A O   1 
ATOM   5998 C CB  . SER A 1 747 ? 64.772 114.925 37.783  1.00 22.25 ? 747  SER A CB  1 
ATOM   5999 O OG  . SER A 1 747 ? 63.949 114.712 36.675  1.00 26.42 ? 747  SER A OG  1 
ATOM   6000 N N   . ARG A 1 748 ? 63.556 117.705 36.455  1.00 22.11 ? 748  ARG A N   1 
ATOM   6001 C CA  . ARG A 1 748 ? 63.525 118.718 35.367  1.00 22.82 ? 748  ARG A CA  1 
ATOM   6002 C C   . ARG A 1 748 ? 63.999 120.126 35.740  1.00 22.54 ? 748  ARG A C   1 
ATOM   6003 O O   . ARG A 1 748 ? 64.231 120.946 34.846  1.00 21.81 ? 748  ARG A O   1 
ATOM   6004 C CB  . ARG A 1 748 ? 62.138 118.789 34.755  1.00 22.74 ? 748  ARG A CB  1 
ATOM   6005 C CG  . ARG A 1 748 ? 61.832 117.631 33.866  1.00 23.63 ? 748  ARG A CG  1 
ATOM   6006 C CD  . ARG A 1 748 ? 60.358 117.798 33.362  1.00 26.19 ? 748  ARG A CD  1 
ATOM   6007 N NE  . ARG A 1 748 ? 60.223 119.046 32.631  1.00 25.39 ? 748  ARG A NE  1 
ATOM   6008 C CZ  . ARG A 1 748 ? 60.431 119.180 31.312  1.00 27.11 ? 748  ARG A CZ  1 
ATOM   6009 N NH1 . ARG A 1 748 ? 60.708 118.134 30.546  1.00 23.00 ? 748  ARG A NH1 1 
ATOM   6010 N NH2 . ARG A 1 748 ? 60.329 120.372 30.734  1.00 25.74 ? 748  ARG A NH2 1 
ATOM   6011 N N   . LYS A 1 749 ? 64.178 120.395 37.038  1.00 21.79 ? 749  LYS A N   1 
ATOM   6012 C CA  . LYS A 1 749 ? 64.661 121.701 37.474  1.00 22.48 ? 749  LYS A CA  1 
ATOM   6013 C C   . LYS A 1 749 ? 66.164 121.731 37.696  1.00 22.76 ? 749  LYS A C   1 
ATOM   6014 O O   . LYS A 1 749 ? 66.678 122.756 38.100  1.00 22.84 ? 749  LYS A O   1 
ATOM   6015 C CB  . LYS A 1 749 ? 64.004 122.051 38.804  1.00 23.52 ? 749  LYS A CB  1 
ATOM   6016 C CG  . LYS A 1 749 ? 62.445 122.127 38.723  1.00 27.62 ? 749  LYS A CG  1 
ATOM   6017 C CD  . LYS A 1 749 ? 61.892 122.538 40.089  1.00 35.23 ? 749  LYS A CD  1 
ATOM   6018 C CE  . LYS A 1 749 ? 60.366 122.330 40.183  1.00 34.30 ? 749  LYS A CE  1 
ATOM   6019 N NZ  . LYS A 1 749 ? 59.980 122.269 41.662  1.00 42.00 ? 749  LYS A NZ  1 
ATOM   6020 N N   . ASN A 1 750 ? 66.836 120.596 37.514  1.00 21.73 ? 750  ASN A N   1 
ATOM   6021 C CA  . ASN A 1 750 ? 68.254 120.453 37.922  1.00 22.25 ? 750  ASN A CA  1 
ATOM   6022 C C   . ASN A 1 750 ? 69.201 120.835 36.792  1.00 22.63 ? 750  ASN A C   1 
ATOM   6023 O O   . ASN A 1 750 ? 68.772 120.891 35.626  1.00 22.13 ? 750  ASN A O   1 
ATOM   6024 C CB  . ASN A 1 750 ? 68.548 119.032 38.337  1.00 20.83 ? 750  ASN A CB  1 
ATOM   6025 C CG  . ASN A 1 750 ? 68.079 118.718 39.720  1.00 20.17 ? 750  ASN A CG  1 
ATOM   6026 O OD1 . ASN A 1 750 ? 67.736 119.591 40.496  1.00 22.05 ? 750  ASN A OD1 1 
ATOM   6027 N ND2 . ASN A 1 750 ? 68.041 117.463 40.029  1.00 17.06 ? 750  ASN A ND2 1 
ATOM   6028 N N   . PRO A 1 751 ? 70.495 121.063 37.131  1.00 24.52 ? 751  PRO A N   1 
ATOM   6029 C CA  . PRO A 1 751 ? 71.500 121.339 36.124  1.00 25.05 ? 751  PRO A CA  1 
ATOM   6030 C C   . PRO A 1 751 ? 71.635 120.194 35.117  1.00 24.74 ? 751  PRO A C   1 
ATOM   6031 O O   . PRO A 1 751 ? 71.293 119.046 35.414  1.00 24.72 ? 751  PRO A O   1 
ATOM   6032 C CB  . PRO A 1 751 ? 72.789 121.465 36.946  1.00 25.61 ? 751  PRO A CB  1 
ATOM   6033 C CG  . PRO A 1 751 ? 72.341 121.942 38.288  1.00 26.55 ? 751  PRO A CG  1 
ATOM   6034 C CD  . PRO A 1 751 ? 71.062 121.160 38.496  1.00 25.16 ? 751  PRO A CD  1 
ATOM   6035 N N   . LEU A 1 752 ? 72.127 120.532 33.941  1.00 23.57 ? 752  LEU A N   1 
ATOM   6036 C CA  . LEU A 1 752 ? 72.302 119.557 32.878  1.00 23.61 ? 752  LEU A CA  1 
ATOM   6037 C C   . LEU A 1 752 ? 73.769 119.250 32.740  1.00 23.05 ? 752  LEU A C   1 
ATOM   6038 O O   . LEU A 1 752 ? 74.616 120.006 33.231  1.00 23.00 ? 752  LEU A O   1 
ATOM   6039 C CB  . LEU A 1 752 ? 71.752 120.105 31.559  1.00 23.37 ? 752  LEU A CB  1 
ATOM   6040 C CG  . LEU A 1 752 ? 70.357 120.734 31.663  1.00 25.86 ? 752  LEU A CG  1 
ATOM   6041 C CD1 . LEU A 1 752 ? 70.159 121.641 30.443  1.00 29.38 ? 752  LEU A CD1 1 
ATOM   6042 C CD2 . LEU A 1 752 ? 69.335 119.659 31.717  1.00 27.75 ? 752  LEU A CD2 1 
ATOM   6043 N N   . GLY A 1 753 ? 74.071 118.176 32.026  1.00 22.98 ? 753  GLY A N   1 
ATOM   6044 C CA  . GLY A 1 753 ? 75.476 117.810 31.755  1.00 23.46 ? 753  GLY A CA  1 
ATOM   6045 C C   . GLY A 1 753 ? 75.584 117.309 30.316  1.00 24.45 ? 753  GLY A C   1 
ATOM   6046 O O   . GLY A 1 753 ? 74.558 117.032 29.684  1.00 24.00 ? 753  GLY A O   1 
ATOM   6047 N N   . LEU A 1 754 ? 76.796 117.239 29.765  1.00 23.94 ? 754  LEU A N   1 
ATOM   6048 C CA  . LEU A 1 754 ? 76.953 116.551 28.478  1.00 23.85 ? 754  LEU A CA  1 
ATOM   6049 C C   . LEU A 1 754 ? 77.939 115.457 28.763  1.00 24.19 ? 754  LEU A C   1 
ATOM   6050 O O   . LEU A 1 754 ? 78.847 115.666 29.526  1.00 24.82 ? 754  LEU A O   1 
ATOM   6051 C CB  . LEU A 1 754 ? 77.476 117.476 27.387  1.00 23.45 ? 754  LEU A CB  1 
ATOM   6052 C CG  . LEU A 1 754 ? 76.614 118.587 26.808  1.00 25.88 ? 754  LEU A CG  1 
ATOM   6053 C CD1 . LEU A 1 754 ? 77.402 119.425 25.759  1.00 29.43 ? 754  LEU A CD1 1 
ATOM   6054 C CD2 . LEU A 1 754 ? 75.390 117.942 26.176  1.00 21.76 ? 754  LEU A CD2 1 
ATOM   6055 N N   . ILE A 1 755 ? 77.736 114.275 28.206  1.00 23.66 ? 755  ILE A N   1 
ATOM   6056 C CA  . ILE A 1 755 ? 78.818 113.292 28.177  1.00 23.35 ? 755  ILE A CA  1 
ATOM   6057 C C   . ILE A 1 755 ? 79.220 113.177 26.682  1.00 24.41 ? 755  ILE A C   1 
ATOM   6058 O O   . ILE A 1 755 ? 78.414 112.801 25.842  1.00 23.53 ? 755  ILE A O   1 
ATOM   6059 C CB  . ILE A 1 755 ? 78.418 111.913 28.716  1.00 24.02 ? 755  ILE A CB  1 
ATOM   6060 C CG1 . ILE A 1 755 ? 77.919 111.959 30.171  1.00 22.50 ? 755  ILE A CG1 1 
ATOM   6061 C CG2 . ILE A 1 755 ? 79.607 110.912 28.608  1.00 23.26 ? 755  ILE A CG2 1 
ATOM   6062 C CD1 . ILE A 1 755 ? 77.103 110.690 30.519  1.00 25.39 ? 755  ILE A CD1 1 
ATOM   6063 N N   . ILE A 1 756 ? 80.475 113.499 26.376  1.00 23.26 ? 756  ILE A N   1 
ATOM   6064 C CA  . ILE A 1 756 ? 80.978 113.417 25.020  1.00 23.66 ? 756  ILE A CA  1 
ATOM   6065 C C   . ILE A 1 756 ? 81.801 112.159 24.927  1.00 24.52 ? 756  ILE A C   1 
ATOM   6066 O O   . ILE A 1 756 ? 82.845 112.067 25.549  1.00 24.72 ? 756  ILE A O   1 
ATOM   6067 C CB  . ILE A 1 756 ? 81.791 114.668 24.722  1.00 24.50 ? 756  ILE A CB  1 
ATOM   6068 C CG1 . ILE A 1 756 ? 80.838 115.873 24.805  1.00 20.37 ? 756  ILE A CG1 1 
ATOM   6069 C CG2 . ILE A 1 756 ? 82.564 114.532 23.374  1.00 23.53 ? 756  ILE A CG2 1 
ATOM   6070 C CD1 . ILE A 1 756 ? 81.472 117.209 24.834  1.00 29.12 ? 756  ILE A CD1 1 
ATOM   6071 N N   . ALA A 1 757 ? 81.307 111.159 24.199  1.00 24.35 ? 757  ALA A N   1 
ATOM   6072 C CA  . ALA A 1 757 ? 82.087 109.946 23.955  1.00 23.54 ? 757  ALA A CA  1 
ATOM   6073 C C   . ALA A 1 757 ? 82.775 110.087 22.583  1.00 24.14 ? 757  ALA A C   1 
ATOM   6074 O O   . ALA A 1 757 ? 82.140 109.934 21.552  1.00 23.01 ? 757  ALA A O   1 
ATOM   6075 C CB  . ALA A 1 757 ? 81.184 108.737 23.971  1.00 23.14 ? 757  ALA A CB  1 
ATOM   6076 N N   . LEU A 1 758 ? 84.075 110.367 22.570  1.00 24.08 ? 758  LEU A N   1 
ATOM   6077 C CA  . LEU A 1 758 ? 84.807 110.603 21.314  1.00 24.75 ? 758  LEU A CA  1 
ATOM   6078 C C   . LEU A 1 758 ? 84.987 109.346 20.479  1.00 24.59 ? 758  LEU A C   1 
ATOM   6079 O O   . LEU A 1 758 ? 85.230 108.277 21.016  1.00 23.38 ? 758  LEU A O   1 
ATOM   6080 C CB  . LEU A 1 758 ? 86.194 111.237 21.584  1.00 24.35 ? 758  LEU A CB  1 
ATOM   6081 C CG  . LEU A 1 758 ? 86.103 112.623 22.203  1.00 25.06 ? 758  LEU A CG  1 
ATOM   6082 C CD1 . LEU A 1 758 ? 87.532 113.168 22.611  1.00 25.78 ? 758  LEU A CD1 1 
ATOM   6083 C CD2 . LEU A 1 758 ? 85.400 113.561 21.269  1.00 23.40 ? 758  LEU A CD2 1 
ATOM   6084 N N   . ASP A 1 759 ? 84.864 109.496 19.159  1.00 26.97 ? 759  ASP A N   1 
ATOM   6085 C CA  . ASP A 1 759 ? 85.147 108.378 18.250  1.00 30.03 ? 759  ASP A CA  1 
ATOM   6086 C C   . ASP A 1 759 ? 86.647 108.394 17.918  1.00 31.67 ? 759  ASP A C   1 
ATOM   6087 O O   . ASP A 1 759 ? 87.403 109.217 18.480  1.00 30.94 ? 759  ASP A O   1 
ATOM   6088 C CB  . ASP A 1 759 ? 84.255 108.418 16.997  1.00 29.95 ? 759  ASP A CB  1 
ATOM   6089 C CG  . ASP A 1 759 ? 84.535 109.611 16.059  1.00 32.99 ? 759  ASP A CG  1 
ATOM   6090 O OD1 . ASP A 1 759 ? 85.603 110.281 16.124  1.00 37.96 ? 759  ASP A OD1 1 
ATOM   6091 O OD2 . ASP A 1 759 ? 83.650 109.894 15.205  1.00 35.49 ? 759  ASP A OD2 1 
ATOM   6092 N N   . GLU A 1 760 ? 87.062 107.504 17.015  1.00 34.29 ? 760  GLU A N   1 
ATOM   6093 C CA  . GLU A 1 760 ? 88.467 107.302 16.683  1.00 36.52 ? 760  GLU A CA  1 
ATOM   6094 C C   . GLU A 1 760 ? 89.110 108.592 16.181  1.00 36.47 ? 760  GLU A C   1 
ATOM   6095 O O   . GLU A 1 760 ? 90.276 108.839 16.459  1.00 38.31 ? 760  GLU A O   1 
ATOM   6096 C CB  . GLU A 1 760 ? 88.622 106.148 15.655  1.00 38.48 ? 760  GLU A CB  1 
ATOM   6097 C CG  . GLU A 1 760 ? 87.775 104.857 15.963  1.00 43.88 ? 760  GLU A CG  1 
ATOM   6098 C CD  . GLU A 1 760 ? 86.418 104.719 15.173  1.00 51.53 ? 760  GLU A CD  1 
ATOM   6099 O OE1 . GLU A 1 760 ? 86.417 103.956 14.168  1.00 54.89 ? 760  GLU A OE1 1 
ATOM   6100 O OE2 . GLU A 1 760 ? 85.360 105.316 15.557  1.00 51.66 ? 760  GLU A OE2 1 
ATOM   6101 N N   . ASN A 1 761 ? 88.344 109.426 15.484  1.00 35.88 ? 761  ASN A N   1 
ATOM   6102 C CA  . ASN A 1 761 ? 88.786 110.736 15.027  1.00 36.15 ? 761  ASN A CA  1 
ATOM   6103 C C   . ASN A 1 761 ? 88.650 111.884 16.023  1.00 35.26 ? 761  ASN A C   1 
ATOM   6104 O O   . ASN A 1 761 ? 88.808 113.052 15.635  1.00 36.17 ? 761  ASN A O   1 
ATOM   6105 C CB  . ASN A 1 761 ? 88.007 111.153 13.784  1.00 36.16 ? 761  ASN A CB  1 
ATOM   6106 C CG  . ASN A 1 761 ? 88.147 110.155 12.659  1.00 41.35 ? 761  ASN A CG  1 
ATOM   6107 O OD1 . ASN A 1 761 ? 89.143 109.416 12.585  1.00 43.78 ? 761  ASN A OD1 1 
ATOM   6108 N ND2 . ASN A 1 761 ? 87.147 110.115 11.773  1.00 44.07 ? 761  ASN A ND2 1 
ATOM   6109 N N   . LYS A 1 762 ? 88.375 111.564 17.289  1.00 34.12 ? 762  LYS A N   1 
ATOM   6110 C CA  . LYS A 1 762 ? 88.169 112.583 18.332  1.00 32.47 ? 762  LYS A CA  1 
ATOM   6111 C C   . LYS A 1 762 ? 87.009 113.542 17.965  1.00 30.83 ? 762  LYS A C   1 
ATOM   6112 O O   . LYS A 1 762 ? 87.051 114.742 18.254  1.00 30.12 ? 762  LYS A O   1 
ATOM   6113 C CB  . LYS A 1 762 ? 89.451 113.353 18.646  1.00 33.84 ? 762  LYS A CB  1 
ATOM   6114 C CG  . LYS A 1 762 ? 90.683 112.456 18.844  1.00 34.87 ? 762  LYS A CG  1 
ATOM   6115 C CD  . LYS A 1 762 ? 90.762 111.791 20.212  1.00 39.86 ? 762  LYS A CD  1 
ATOM   6116 C CE  . LYS A 1 762 ? 92.041 110.936 20.325  1.00 42.25 ? 762  LYS A CE  1 
ATOM   6117 N NZ  . LYS A 1 762 ? 91.835 109.616 19.670  1.00 46.76 ? 762  LYS A NZ  1 
ATOM   6118 N N   . GLU A 1 763 ? 85.997 112.975 17.317  1.00 28.72 ? 763  GLU A N   1 
ATOM   6119 C CA  . GLU A 1 763 ? 84.732 113.677 17.008  1.00 28.39 ? 763  GLU A CA  1 
ATOM   6120 C C   . GLU A 1 763 ? 83.553 112.985 17.691  1.00 26.06 ? 763  GLU A C   1 
ATOM   6121 O O   . GLU A 1 763 ? 83.657 111.832 18.081  1.00 24.14 ? 763  GLU A O   1 
ATOM   6122 C CB  . GLU A 1 763 ? 84.487 113.727 15.497  1.00 28.32 ? 763  GLU A CB  1 
ATOM   6123 C CG  . GLU A 1 763 ? 85.517 114.595 14.833  1.00 35.86 ? 763  GLU A CG  1 
ATOM   6124 C CD  . GLU A 1 763 ? 85.547 114.520 13.316  1.00 45.65 ? 763  GLU A CD  1 
ATOM   6125 O OE1 . GLU A 1 763 ? 84.703 113.810 12.708  1.00 49.09 ? 763  GLU A OE1 1 
ATOM   6126 O OE2 . GLU A 1 763 ? 86.425 115.210 12.733  1.00 50.24 ? 763  GLU A OE2 1 
ATOM   6127 N N   . ALA A 1 764 ? 82.437 113.716 17.770  1.00 23.51 ? 764  ALA A N   1 
ATOM   6128 C CA  . ALA A 1 764 ? 81.227 113.246 18.363  1.00 23.36 ? 764  ALA A CA  1 
ATOM   6129 C C   . ALA A 1 764 ? 80.136 114.244 18.006  1.00 21.66 ? 764  ALA A C   1 
ATOM   6130 O O   . ALA A 1 764 ? 80.414 115.414 17.691  1.00 21.47 ? 764  ALA A O   1 
ATOM   6131 C CB  . ALA A 1 764 ? 81.361 113.062 19.918  1.00 21.15 ? 764  ALA A CB  1 
ATOM   6132 N N   . LYS A 1 765 ? 78.911 113.742 17.966  1.00 22.63 ? 765  LYS A N   1 
ATOM   6133 C CA  . LYS A 1 765 ? 77.716 114.548 17.718  1.00 23.06 ? 765  LYS A CA  1 
ATOM   6134 C C   . LYS A 1 765 ? 76.525 114.100 18.606  1.00 22.28 ? 765  LYS A C   1 
ATOM   6135 O O   . LYS A 1 765 ? 76.378 112.940 18.956  1.00 20.90 ? 765  LYS A O   1 
ATOM   6136 C CB  . LYS A 1 765 ? 77.257 114.492 16.228  1.00 23.60 ? 765  LYS A CB  1 
ATOM   6137 C CG  . LYS A 1 765 ? 78.177 115.233 15.309  1.00 30.51 ? 765  LYS A CG  1 
ATOM   6138 C CD  . LYS A 1 765 ? 77.545 115.622 13.984  1.00 38.65 ? 765  LYS A CD  1 
ATOM   6139 C CE  . LYS A 1 765 ? 78.331 116.810 13.336  1.00 44.26 ? 765  LYS A CE  1 
ATOM   6140 N NZ  . LYS A 1 765 ? 77.551 117.538 12.242  1.00 46.70 ? 765  LYS A NZ  1 
ATOM   6141 N N   . GLY A 1 766 ? 75.640 115.045 18.896  1.00 22.04 ? 766  GLY A N   1 
ATOM   6142 C CA  . GLY A 1 766 ? 74.468 114.706 19.646  1.00 21.15 ? 766  GLY A CA  1 
ATOM   6143 C C   . GLY A 1 766 ? 73.485 115.831 19.513  1.00 21.81 ? 766  GLY A C   1 
ATOM   6144 O O   . GLY A 1 766 ? 73.740 116.827 18.812  1.00 21.08 ? 766  GLY A O   1 
ATOM   6145 N N   . GLU A 1 767 ? 72.369 115.695 20.229  1.00 20.39 ? 767  GLU A N   1 
ATOM   6146 C CA  . GLU A 1 767 ? 71.275 116.679 20.132  1.00 22.39 ? 767  GLU A CA  1 
ATOM   6147 C C   . GLU A 1 767 ? 70.424 116.613 21.374  1.00 19.69 ? 767  GLU A C   1 
ATOM   6148 O O   . GLU A 1 767 ? 70.454 115.618 22.120  1.00 18.99 ? 767  GLU A O   1 
ATOM   6149 C CB  . GLU A 1 767 ? 70.402 116.391 18.902  1.00 22.85 ? 767  GLU A CB  1 
ATOM   6150 C CG  . GLU A 1 767 ? 69.704 115.026 18.947  1.00 26.42 ? 767  GLU A CG  1 
ATOM   6151 C CD  . GLU A 1 767 ? 68.960 114.710 17.663  1.00 30.29 ? 767  GLU A CD  1 
ATOM   6152 O OE1 . GLU A 1 767 ? 69.108 115.485 16.668  1.00 36.58 ? 767  GLU A OE1 1 
ATOM   6153 O OE2 . GLU A 1 767 ? 68.195 113.703 17.646  1.00 33.27 ? 767  GLU A OE2 1 
ATOM   6154 N N   . LEU A 1 768 ? 69.668 117.681 21.611  1.00 21.18 ? 768  LEU A N   1 
ATOM   6155 C CA  . LEU A 1 768 ? 68.765 117.716 22.731  1.00 20.68 ? 768  LEU A CA  1 
ATOM   6156 C C   . LEU A 1 768 ? 67.477 118.432 22.306  1.00 19.61 ? 768  LEU A C   1 
ATOM   6157 O O   . LEU A 1 768 ? 67.511 119.520 21.767  1.00 19.64 ? 768  LEU A O   1 
ATOM   6158 C CB  . LEU A 1 768 ? 69.395 118.444 23.911  1.00 19.97 ? 768  LEU A CB  1 
ATOM   6159 C CG  . LEU A 1 768 ? 68.529 118.709 25.156  1.00 20.32 ? 768  LEU A CG  1 
ATOM   6160 C CD1 . LEU A 1 768 ? 67.992 117.428 25.790  1.00 17.10 ? 768  LEU A CD1 1 
ATOM   6161 C CD2 . LEU A 1 768 ? 69.395 119.481 26.161  1.00 23.63 ? 768  LEU A CD2 1 
ATOM   6162 N N   . PHE A 1 769 ? 66.356 117.747 22.507  1.00 19.51 ? 769  PHE A N   1 
ATOM   6163 C CA  . PHE A 1 769 ? 65.051 118.302 22.374  1.00 19.57 ? 769  PHE A CA  1 
ATOM   6164 C C   . PHE A 1 769 ? 64.588 118.714 23.791  1.00 20.39 ? 769  PHE A C   1 
ATOM   6165 O O   . PHE A 1 769 ? 64.810 117.969 24.767  1.00 18.36 ? 769  PHE A O   1 
ATOM   6166 C CB  . PHE A 1 769 ? 64.123 117.199 21.802  1.00 20.21 ? 769  PHE A CB  1 
ATOM   6167 C CG  . PHE A 1 769 ? 62.666 117.539 21.903  1.00 20.88 ? 769  PHE A CG  1 
ATOM   6168 C CD1 . PHE A 1 769 ? 62.098 118.417 21.007  1.00 20.88 ? 769  PHE A CD1 1 
ATOM   6169 C CD2 . PHE A 1 769 ? 61.874 116.995 22.932  1.00 20.72 ? 769  PHE A CD2 1 
ATOM   6170 C CE1 . PHE A 1 769 ? 60.793 118.741 21.075  1.00 20.55 ? 769  PHE A CE1 1 
ATOM   6171 C CE2 . PHE A 1 769 ? 60.550 117.337 23.016  1.00 22.01 ? 769  PHE A CE2 1 
ATOM   6172 C CZ  . PHE A 1 769 ? 60.015 118.203 22.101  1.00 23.14 ? 769  PHE A CZ  1 
ATOM   6173 N N   . TRP A 1 770 ? 63.957 119.887 23.926  1.00 20.91 ? 770  TRP A N   1 
ATOM   6174 C CA  . TRP A 1 770 ? 63.414 120.285 25.227  1.00 21.63 ? 770  TRP A CA  1 
ATOM   6175 C C   . TRP A 1 770 ? 62.111 121.086 24.996  1.00 21.91 ? 770  TRP A C   1 
ATOM   6176 O O   . TRP A 1 770 ? 62.048 121.984 24.169  1.00 22.03 ? 770  TRP A O   1 
ATOM   6177 C CB  . TRP A 1 770 ? 64.445 121.143 26.010  1.00 22.59 ? 770  TRP A CB  1 
ATOM   6178 C CG  . TRP A 1 770 ? 64.192 121.199 27.479  1.00 22.82 ? 770  TRP A CG  1 
ATOM   6179 C CD1 . TRP A 1 770 ? 63.753 122.274 28.181  1.00 26.03 ? 770  TRP A CD1 1 
ATOM   6180 C CD2 . TRP A 1 770 ? 64.336 120.128 28.422  1.00 23.12 ? 770  TRP A CD2 1 
ATOM   6181 N NE1 . TRP A 1 770 ? 63.608 121.947 29.534  1.00 27.89 ? 770  TRP A NE1 1 
ATOM   6182 C CE2 . TRP A 1 770 ? 63.980 120.641 29.703  1.00 25.59 ? 770  TRP A CE2 1 
ATOM   6183 C CE3 . TRP A 1 770 ? 64.757 118.787 28.320  1.00 25.80 ? 770  TRP A CE3 1 
ATOM   6184 C CZ2 . TRP A 1 770 ? 64.009 119.852 30.872  1.00 24.46 ? 770  TRP A CZ2 1 
ATOM   6185 C CZ3 . TRP A 1 770 ? 64.802 117.993 29.486  1.00 25.80 ? 770  TRP A CZ3 1 
ATOM   6186 C CH2 . TRP A 1 770 ? 64.431 118.540 30.748  1.00 25.14 ? 770  TRP A CH2 1 
ATOM   6187 N N   . ASP A 1 771 ? 61.066 120.707 25.696  1.00 21.33 ? 771  ASP A N   1 
ATOM   6188 C CA  . ASP A 1 771 ? 59.802 121.427 25.610  1.00 21.74 ? 771  ASP A CA  1 
ATOM   6189 C C   . ASP A 1 771 ? 59.271 121.346 27.076  1.00 22.50 ? 771  ASP A C   1 
ATOM   6190 O O   . ASP A 1 771 ? 60.030 121.003 28.012  1.00 20.45 ? 771  ASP A O   1 
ATOM   6191 C CB  . ASP A 1 771 ? 58.913 120.804 24.510  1.00 19.44 ? 771  ASP A CB  1 
ATOM   6192 C CG  . ASP A 1 771 ? 58.308 119.446 24.891  1.00 21.20 ? 771  ASP A CG  1 
ATOM   6193 O OD1 . ASP A 1 771 ? 58.743 118.812 25.883  1.00 20.78 ? 771  ASP A OD1 1 
ATOM   6194 O OD2 . ASP A 1 771 ? 57.383 118.990 24.173  1.00 19.00 ? 771  ASP A OD2 1 
ATOM   6195 N N   . ASP A 1 772 ? 58.016 121.690 27.292  1.00 21.64 ? 772  ASP A N   1 
ATOM   6196 C CA  . ASP A 1 772 ? 57.498 121.766 28.653  1.00 24.04 ? 772  ASP A CA  1 
ATOM   6197 C C   . ASP A 1 772 ? 57.109 120.401 29.213  1.00 23.61 ? 772  ASP A C   1 
ATOM   6198 O O   . ASP A 1 772 ? 56.674 120.313 30.341  1.00 24.01 ? 772  ASP A O   1 
ATOM   6199 C CB  . ASP A 1 772 ? 56.293 122.744 28.729  1.00 23.95 ? 772  ASP A CB  1 
ATOM   6200 C CG  . ASP A 1 772 ? 55.047 122.170 28.150  1.00 28.08 ? 772  ASP A CG  1 
ATOM   6201 O OD1 . ASP A 1 772 ? 55.046 120.949 27.807  1.00 27.20 ? 772  ASP A OD1 1 
ATOM   6202 O OD2 . ASP A 1 772 ? 54.040 122.933 28.011  1.00 30.66 ? 772  ASP A OD2 1 
ATOM   6203 N N   . GLY A 1 773 ? 57.248 119.342 28.410  1.00 23.12 ? 773  GLY A N   1 
ATOM   6204 C CA  . GLY A 1 773 ? 57.195 117.977 28.940  1.00 22.36 ? 773  GLY A CA  1 
ATOM   6205 C C   . GLY A 1 773 ? 55.763 117.440 29.096  1.00 22.07 ? 773  GLY A C   1 
ATOM   6206 O O   . GLY A 1 773 ? 55.587 116.296 29.474  1.00 20.82 ? 773  GLY A O   1 
ATOM   6207 N N   . GLU A 1 774 ? 54.741 118.267 28.839  1.00 21.81 ? 774  GLU A N   1 
ATOM   6208 C CA  . GLU A 1 774 ? 53.368 117.814 29.036  1.00 24.78 ? 774  GLU A CA  1 
ATOM   6209 C C   . GLU A 1 774 ? 52.315 118.322 28.066  1.00 25.20 ? 774  GLU A C   1 
ATOM   6210 O O   . GLU A 1 774 ? 51.258 117.705 27.928  1.00 23.53 ? 774  GLU A O   1 
ATOM   6211 C CB  . GLU A 1 774 ? 52.895 118.145 30.459  1.00 26.32 ? 774  GLU A CB  1 
ATOM   6212 C CG  . GLU A 1 774 ? 53.354 119.435 31.012  1.00 32.65 ? 774  GLU A CG  1 
ATOM   6213 C CD  . GLU A 1 774 ? 52.835 119.624 32.438  1.00 41.82 ? 774  GLU A CD  1 
ATOM   6214 O OE1 . GLU A 1 774 ? 53.180 118.808 33.322  1.00 46.36 ? 774  GLU A OE1 1 
ATOM   6215 O OE2 . GLU A 1 774 ? 52.056 120.568 32.664  1.00 45.89 ? 774  GLU A OE2 1 
ATOM   6216 N N   . THR A 1 775 ? 52.584 119.433 27.390  1.00 25.35 ? 775  THR A N   1 
ATOM   6217 C CA  . THR A 1 775 ? 51.591 119.975 26.480  1.00 25.74 ? 775  THR A CA  1 
ATOM   6218 C C   . THR A 1 775 ? 51.505 119.168 25.201  1.00 26.93 ? 775  THR A C   1 
ATOM   6219 O O   . THR A 1 775 ? 52.508 118.767 24.606  1.00 26.64 ? 775  THR A O   1 
ATOM   6220 C CB  . THR A 1 775 ? 51.838 121.474 26.238  1.00 26.14 ? 775  THR A CB  1 
ATOM   6221 O OG1 . THR A 1 775 ? 51.830 122.128 27.511  1.00 23.06 ? 775  THR A OG1 1 
ATOM   6222 C CG2 . THR A 1 775 ? 50.753 122.069 25.377  1.00 28.45 ? 775  THR A CG2 1 
ATOM   6223 N N   . LYS A 1 776 ? 50.294 118.869 24.798  1.00 27.79 ? 776  LYS A N   1 
ATOM   6224 C CA  . LYS A 1 776 ? 50.086 118.069 23.619  1.00 30.65 ? 776  LYS A CA  1 
ATOM   6225 C C   . LYS A 1 776 ? 50.387 118.956 22.417  1.00 31.57 ? 776  LYS A C   1 
ATOM   6226 O O   . LYS A 1 776 ? 50.103 120.162 22.431  1.00 31.25 ? 776  LYS A O   1 
ATOM   6227 C CB  . LYS A 1 776 ? 48.653 117.466 23.575  1.00 29.53 ? 776  LYS A CB  1 
ATOM   6228 C CG  . LYS A 1 776 ? 48.493 116.271 22.620  1.00 33.06 ? 776  LYS A CG  1 
ATOM   6229 C CD  . LYS A 1 776 ? 47.038 115.686 22.624  1.00 34.80 ? 776  LYS A CD  1 
ATOM   6230 C CE  . LYS A 1 776 ? 46.872 114.509 23.597  1.00 38.30 ? 776  LYS A CE  1 
ATOM   6231 N NZ  . LYS A 1 776 ? 45.544 113.691 23.503  1.00 39.56 ? 776  LYS A NZ  1 
ATOM   6232 N N   . ASP A 1 777 ? 51.019 118.356 21.410  1.00 32.90 ? 777  ASP A N   1 
ATOM   6233 C CA  . ASP A 1 777 ? 51.321 119.044 20.138  1.00 34.41 ? 777  ASP A CA  1 
ATOM   6234 C C   . ASP A 1 777 ? 52.283 120.243 20.191  1.00 32.87 ? 777  ASP A C   1 
ATOM   6235 O O   . ASP A 1 777 ? 52.203 121.132 19.331  1.00 31.96 ? 777  ASP A O   1 
ATOM   6236 C CB  . ASP A 1 777 ? 50.023 119.411 19.409  1.00 35.52 ? 777  ASP A CB  1 
ATOM   6237 C CG  . ASP A 1 777 ? 49.329 118.187 18.846  1.00 42.41 ? 777  ASP A CG  1 
ATOM   6238 O OD1 . ASP A 1 777 ? 50.053 117.281 18.316  1.00 48.11 ? 777  ASP A OD1 1 
ATOM   6239 O OD2 . ASP A 1 777 ? 48.072 118.117 18.944  1.00 48.35 ? 777  ASP A OD2 1 
ATOM   6240 N N   . THR A 1 778 ? 53.212 120.238 21.150  1.00 31.14 ? 778  THR A N   1 
ATOM   6241 C CA  . THR A 1 778 ? 54.296 121.211 21.171  1.00 29.34 ? 778  THR A CA  1 
ATOM   6242 C C   . THR A 1 778 ? 55.146 121.048 19.897  1.00 29.03 ? 778  THR A C   1 
ATOM   6243 O O   . THR A 1 778 ? 55.797 121.992 19.455  1.00 27.75 ? 778  THR A O   1 
ATOM   6244 C CB  . THR A 1 778 ? 55.236 121.012 22.398  1.00 29.62 ? 778  THR A CB  1 
ATOM   6245 O OG1 . THR A 1 778 ? 55.685 119.646 22.446  1.00 27.26 ? 778  THR A OG1 1 
ATOM   6246 C CG2 . THR A 1 778 ? 54.514 121.308 23.690  1.00 26.60 ? 778  THR A CG2 1 
ATOM   6247 N N   . VAL A 1 779 ? 55.173 119.843 19.334  1.00 28.71 ? 779  VAL A N   1 
ATOM   6248 C CA  . VAL A 1 779 ? 55.984 119.576 18.137  1.00 28.31 ? 779  VAL A CA  1 
ATOM   6249 C C   . VAL A 1 779 ? 55.271 120.076 16.883  1.00 29.13 ? 779  VAL A C   1 
ATOM   6250 O O   . VAL A 1 779 ? 55.844 120.841 16.103  1.00 28.52 ? 779  VAL A O   1 
ATOM   6251 C CB  . VAL A 1 779 ? 56.426 118.114 17.992  1.00 28.80 ? 779  VAL A CB  1 
ATOM   6252 C CG1 . VAL A 1 779 ? 57.211 117.925 16.679  1.00 26.10 ? 779  VAL A CG1 1 
ATOM   6253 C CG2 . VAL A 1 779 ? 57.314 117.678 19.206  1.00 27.78 ? 779  VAL A CG2 1 
ATOM   6254 N N   . ALA A 1 780 ? 54.028 119.654 16.694  1.00 29.78 ? 780  ALA A N   1 
ATOM   6255 C CA  . ALA A 1 780 ? 53.219 120.176 15.572  1.00 32.08 ? 780  ALA A CA  1 
ATOM   6256 C C   . ALA A 1 780 ? 53.151 121.708 15.592  1.00 32.19 ? 780  ALA A C   1 
ATOM   6257 O O   . ALA A 1 780 ? 53.175 122.362 14.547  1.00 32.30 ? 780  ALA A O   1 
ATOM   6258 C CB  . ALA A 1 780 ? 51.789 119.580 15.601  1.00 31.21 ? 780  ALA A CB  1 
ATOM   6259 N N   . ASN A 1 781 ? 53.064 122.285 16.780  1.00 33.17 ? 781  ASN A N   1 
ATOM   6260 C CA  . ASN A 1 781 ? 52.856 123.723 16.892  1.00 34.12 ? 781  ASN A CA  1 
ATOM   6261 C C   . ASN A 1 781 ? 54.183 124.463 17.044  1.00 33.06 ? 781  ASN A C   1 
ATOM   6262 O O   . ASN A 1 781 ? 54.200 125.669 17.281  1.00 32.69 ? 781  ASN A O   1 
ATOM   6263 C CB  . ASN A 1 781 ? 51.914 124.089 18.057  1.00 34.83 ? 781  ASN A CB  1 
ATOM   6264 C CG  . ASN A 1 781 ? 50.494 123.533 17.884  1.00 40.33 ? 781  ASN A CG  1 
ATOM   6265 O OD1 . ASN A 1 781 ? 49.934 122.941 18.819  1.00 43.61 ? 781  ASN A OD1 1 
ATOM   6266 N ND2 . ASN A 1 781 ? 49.907 123.722 16.708  1.00 42.09 ? 781  ASN A ND2 1 
ATOM   6267 N N   . LYS A 1 782 ? 55.286 123.725 16.912  1.00 31.97 ? 782  LYS A N   1 
ATOM   6268 C CA  . LYS A 1 782 ? 56.636 124.246 17.062  1.00 31.82 ? 782  LYS A CA  1 
ATOM   6269 C C   . LYS A 1 782 ? 56.898 125.092 18.286  1.00 29.96 ? 782  LYS A C   1 
ATOM   6270 O O   . LYS A 1 782 ? 57.439 126.190 18.185  1.00 29.57 ? 782  LYS A O   1 
ATOM   6271 C CB  . LYS A 1 782 ? 57.100 125.029 15.818  1.00 33.76 ? 782  LYS A CB  1 
ATOM   6272 C CG  . LYS A 1 782 ? 56.813 124.360 14.485  1.00 37.97 ? 782  LYS A CG  1 
ATOM   6273 C CD  . LYS A 1 782 ? 57.920 123.470 14.025  1.00 43.39 ? 782  LYS A CD  1 
ATOM   6274 C CE  . LYS A 1 782 ? 57.686 123.037 12.578  1.00 47.14 ? 782  LYS A CE  1 
ATOM   6275 N NZ  . LYS A 1 782 ? 58.807 122.117 12.123  1.00 52.33 ? 782  LYS A NZ  1 
ATOM   6276 N N   . VAL A 1 783 ? 56.574 124.577 19.452  1.00 27.28 ? 783  VAL A N   1 
ATOM   6277 C CA  . VAL A 1 783 ? 57.005 125.245 20.662  1.00 25.71 ? 783  VAL A CA  1 
ATOM   6278 C C   . VAL A 1 783 ? 57.968 124.337 21.391  1.00 24.81 ? 783  VAL A C   1 
ATOM   6279 O O   . VAL A 1 783 ? 57.570 123.612 22.302  1.00 24.50 ? 783  VAL A O   1 
ATOM   6280 C CB  . VAL A 1 783 ? 55.809 125.593 21.588  1.00 25.57 ? 783  VAL A CB  1 
ATOM   6281 C CG1 . VAL A 1 783 ? 56.278 126.354 22.846  1.00 22.36 ? 783  VAL A CG1 1 
ATOM   6282 C CG2 . VAL A 1 783 ? 54.731 126.359 20.801  1.00 27.88 ? 783  VAL A CG2 1 
ATOM   6283 N N   . TYR A 1 784 ? 59.234 124.380 20.972  1.00 24.76 ? 784  TYR A N   1 
ATOM   6284 C CA  . TYR A 1 784 ? 60.269 123.597 21.591  1.00 22.74 ? 784  TYR A CA  1 
ATOM   6285 C C   . TYR A 1 784 ? 61.657 124.161 21.311  1.00 23.10 ? 784  TYR A C   1 
ATOM   6286 O O   . TYR A 1 784 ? 61.834 125.042 20.485  1.00 24.22 ? 784  TYR A O   1 
ATOM   6287 C CB  . TYR A 1 784 ? 60.181 122.141 21.161  1.00 22.55 ? 784  TYR A CB  1 
ATOM   6288 C CG  . TYR A 1 784 ? 60.326 121.851 19.660  1.00 23.38 ? 784  TYR A CG  1 
ATOM   6289 C CD1 . TYR A 1 784 ? 61.564 121.520 19.110  1.00 22.33 ? 784  TYR A CD1 1 
ATOM   6290 C CD2 . TYR A 1 784 ? 59.200 121.787 18.824  1.00 23.67 ? 784  TYR A CD2 1 
ATOM   6291 C CE1 . TYR A 1 784 ? 61.692 121.173 17.737  1.00 23.00 ? 784  TYR A CE1 1 
ATOM   6292 C CE2 . TYR A 1 784 ? 59.322 121.460 17.479  1.00 26.26 ? 784  TYR A CE2 1 
ATOM   6293 C CZ  . TYR A 1 784 ? 60.566 121.175 16.943  1.00 24.51 ? 784  TYR A CZ  1 
ATOM   6294 O OH  . TYR A 1 784 ? 60.661 120.818 15.611  1.00 24.53 ? 784  TYR A OH  1 
ATOM   6295 N N   . LEU A 1 785 ? 62.630 123.583 21.985  1.00 22.01 ? 785  LEU A N   1 
ATOM   6296 C CA  . LEU A 1 785 ? 64.013 123.882 21.783  1.00 23.04 ? 785  LEU A CA  1 
ATOM   6297 C C   . LEU A 1 785 ? 64.649 122.650 21.147  1.00 23.26 ? 785  LEU A C   1 
ATOM   6298 O O   . LEU A 1 785 ? 64.409 121.530 21.600  1.00 21.92 ? 785  LEU A O   1 
ATOM   6299 C CB  . LEU A 1 785 ? 64.666 124.148 23.120  1.00 22.19 ? 785  LEU A CB  1 
ATOM   6300 C CG  . LEU A 1 785 ? 66.191 124.182 23.109  1.00 26.39 ? 785  LEU A CG  1 
ATOM   6301 C CD1 . LEU A 1 785 ? 66.709 125.444 22.362  1.00 28.06 ? 785  LEU A CD1 1 
ATOM   6302 C CD2 . LEU A 1 785 ? 66.741 124.135 24.499  1.00 28.47 ? 785  LEU A CD2 1 
ATOM   6303 N N   . LEU A 1 786 ? 65.467 122.839 20.122  1.00 23.74 ? 786  LEU A N   1 
ATOM   6304 C CA  . LEU A 1 786 ? 66.255 121.719 19.625  1.00 24.53 ? 786  LEU A CA  1 
ATOM   6305 C C   . LEU A 1 786 ? 67.667 122.208 19.425  1.00 26.25 ? 786  LEU A C   1 
ATOM   6306 O O   . LEU A 1 786 ? 67.913 123.160 18.674  1.00 25.43 ? 786  LEU A O   1 
ATOM   6307 C CB  . LEU A 1 786 ? 65.656 121.115 18.340  1.00 22.85 ? 786  LEU A CB  1 
ATOM   6308 C CG  . LEU A 1 786 ? 66.343 119.877 17.728  1.00 24.03 ? 786  LEU A CG  1 
ATOM   6309 C CD1 . LEU A 1 786 ? 66.368 118.642 18.640  1.00 23.16 ? 786  LEU A CD1 1 
ATOM   6310 C CD2 . LEU A 1 786 ? 65.634 119.494 16.394  1.00 27.15 ? 786  LEU A CD2 1 
ATOM   6311 N N   . CYS A 1 787 ? 68.603 121.600 20.120  1.00 27.79 ? 787  CYS A N   1 
ATOM   6312 C CA  . CYS A 1 787 ? 69.975 121.971 19.819  1.00 30.63 ? 787  CYS A CA  1 
ATOM   6313 C C   . CYS A 1 787 ? 70.846 120.791 19.385  1.00 30.38 ? 787  CYS A C   1 
ATOM   6314 O O   . CYS A 1 787 ? 70.464 119.620 19.547  1.00 28.35 ? 787  CYS A O   1 
ATOM   6315 C CB  . CYS A 1 787 ? 70.578 122.790 20.937  1.00 31.13 ? 787  CYS A CB  1 
ATOM   6316 S SG  . CYS A 1 787 ? 70.443 122.024 22.448  1.00 38.88 ? 787  CYS A SG  1 
ATOM   6317 N N   . GLU A 1 788 ? 71.974 121.130 18.773  1.00 30.12 ? 788  GLU A N   1 
ATOM   6318 C CA  . GLU A 1 788 ? 72.888 120.172 18.208  1.00 31.90 ? 788  GLU A CA  1 
ATOM   6319 C C   . GLU A 1 788 ? 74.216 120.414 18.896  1.00 29.06 ? 788  GLU A C   1 
ATOM   6320 O O   . GLU A 1 788 ? 74.592 121.568 19.145  1.00 27.66 ? 788  GLU A O   1 
ATOM   6321 C CB  . GLU A 1 788 ? 73.097 120.406 16.702  1.00 32.42 ? 788  GLU A CB  1 
ATOM   6322 C CG  . GLU A 1 788 ? 71.886 120.751 15.827  1.00 37.56 ? 788  GLU A CG  1 
ATOM   6323 C CD  . GLU A 1 788 ? 72.338 121.359 14.445  1.00 40.93 ? 788  GLU A CD  1 
ATOM   6324 O OE1 . GLU A 1 788 ? 71.509 121.392 13.477  1.00 50.15 ? 788  GLU A OE1 1 
ATOM   6325 O OE2 . GLU A 1 788 ? 73.543 121.772 14.311  1.00 48.01 ? 788  GLU A OE2 1 
ATOM   6326 N N   . PHE A 1 789 ? 74.914 119.330 19.213  1.00 27.52 ? 789  PHE A N   1 
ATOM   6327 C CA  . PHE A 1 789 ? 76.227 119.406 19.846  1.00 27.02 ? 789  PHE A CA  1 
ATOM   6328 C C   . PHE A 1 789 ? 77.111 118.718 18.832  1.00 27.73 ? 789  PHE A C   1 
ATOM   6329 O O   . PHE A 1 789 ? 76.714 117.709 18.243  1.00 25.65 ? 789  PHE A O   1 
ATOM   6330 C CB  . PHE A 1 789 ? 76.275 118.631 21.169  1.00 27.14 ? 789  PHE A CB  1 
ATOM   6331 C CG  . PHE A 1 789 ? 75.121 118.919 22.098  1.00 26.80 ? 789  PHE A CG  1 
ATOM   6332 C CD1 . PHE A 1 789 ? 74.961 120.176 22.678  1.00 28.22 ? 789  PHE A CD1 1 
ATOM   6333 C CD2 . PHE A 1 789 ? 74.192 117.911 22.399  1.00 26.09 ? 789  PHE A CD2 1 
ATOM   6334 C CE1 . PHE A 1 789 ? 73.884 120.451 23.545  1.00 28.95 ? 789  PHE A CE1 1 
ATOM   6335 C CE2 . PHE A 1 789 ? 73.146 118.159 23.269  1.00 29.32 ? 789  PHE A CE2 1 
ATOM   6336 C CZ  . PHE A 1 789 ? 72.975 119.429 23.830  1.00 30.30 ? 789  PHE A CZ  1 
ATOM   6337 N N   . SER A 1 790 ? 78.281 119.296 18.577  1.00 27.90 ? 790  SER A N   1 
ATOM   6338 C CA  . SER A 1 790 ? 79.272 118.639 17.735  1.00 29.82 ? 790  SER A CA  1 
ATOM   6339 C C   . SER A 1 790 ? 80.651 118.996 18.216  1.00 28.94 ? 790  SER A C   1 
ATOM   6340 O O   . SER A 1 790 ? 80.921 120.128 18.597  1.00 29.48 ? 790  SER A O   1 
ATOM   6341 C CB  . SER A 1 790 ? 79.124 118.951 16.239  1.00 30.26 ? 790  SER A CB  1 
ATOM   6342 O OG  . SER A 1 790 ? 78.488 120.196 16.001  1.00 36.45 ? 790  SER A OG  1 
ATOM   6343 N N   . VAL A 1 791 ? 81.478 117.978 18.261  1.00 29.32 ? 791  VAL A N   1 
ATOM   6344 C CA  . VAL A 1 791 ? 82.856 118.093 18.711  1.00 30.55 ? 791  VAL A CA  1 
ATOM   6345 C C   . VAL A 1 791 ? 83.670 117.670 17.522  1.00 32.70 ? 791  VAL A C   1 
ATOM   6346 O O   . VAL A 1 791 ? 83.405 116.624 16.915  1.00 29.58 ? 791  VAL A O   1 
ATOM   6347 C CB  . VAL A 1 791 ? 83.163 117.159 19.911  1.00 29.59 ? 791  VAL A CB  1 
ATOM   6348 C CG1 . VAL A 1 791 ? 84.686 117.004 20.104  1.00 30.11 ? 791  VAL A CG1 1 
ATOM   6349 C CG2 . VAL A 1 791 ? 82.548 117.726 21.174  1.00 29.11 ? 791  VAL A CG2 1 
ATOM   6350 N N   . THR A 1 792 ? 84.630 118.516 17.171  1.00 36.68 ? 792  THR A N   1 
ATOM   6351 C CA  . THR A 1 792 ? 85.601 118.231 16.119  1.00 41.17 ? 792  THR A CA  1 
ATOM   6352 C C   . THR A 1 792 ? 86.890 118.916 16.527  1.00 42.32 ? 792  THR A C   1 
ATOM   6353 O O   . THR A 1 792 ? 86.946 120.149 16.556  1.00 42.50 ? 792  THR A O   1 
ATOM   6354 C CB  . THR A 1 792 ? 85.104 118.620 14.680  1.00 41.43 ? 792  THR A CB  1 
ATOM   6355 O OG1 . THR A 1 792 ? 86.029 118.100 13.709  1.00 46.49 ? 792  THR A OG1 1 
ATOM   6356 C CG2 . THR A 1 792 ? 85.011 120.126 14.503  1.00 43.93 ? 792  THR A CG2 1 
ATOM   6357 N N   . GLN A 1 793 ? 87.898 118.074 16.815  1.00 43.86 ? 793  GLN A N   1 
ATOM   6358 C CA  . GLN A 1 793 ? 89.026 118.329 17.756  1.00 45.61 ? 793  GLN A CA  1 
ATOM   6359 C C   . GLN A 1 793 ? 89.268 119.769 18.209  1.00 43.44 ? 793  GLN A C   1 
ATOM   6360 O O   . GLN A 1 793 ? 89.202 120.737 17.403  1.00 43.24 ? 793  GLN A O   1 
ATOM   6361 C CB  . GLN A 1 793 ? 90.383 117.732 17.264  1.00 45.82 ? 793  GLN A CB  1 
ATOM   6362 C CG  . GLN A 1 793 ? 90.274 116.579 16.194  1.00 48.54 ? 793  GLN A CG  1 
ATOM   6363 C CD  . GLN A 1 793 ? 91.583 115.783 16.136  1.00 49.84 ? 793  GLN A CD  1 
ATOM   6364 O OE1 . GLN A 1 793 ? 92.299 115.676 17.154  1.00 57.00 ? 793  GLN A OE1 1 
ATOM   6365 N NE2 . GLN A 1 793 ? 91.892 115.184 14.955  1.00 50.58 ? 793  GLN A NE2 1 
ATOM   6366 N N   . ASN A 1 794 ? 89.586 119.883 19.497  1.00 42.17 ? 794  ASN A N   1 
ATOM   6367 C CA  . ASN A 1 794 ? 89.820 121.170 20.122  1.00 40.44 ? 794  ASN A CA  1 
ATOM   6368 C C   . ASN A 1 794 ? 88.548 122.005 20.265  1.00 38.66 ? 794  ASN A C   1 
ATOM   6369 O O   . ASN A 1 794 ? 88.617 123.156 20.701  1.00 37.57 ? 794  ASN A O   1 
ATOM   6370 C CB  . ASN A 1 794 ? 90.862 121.982 19.321  1.00 41.94 ? 794  ASN A CB  1 
ATOM   6371 C CG  . ASN A 1 794 ? 92.218 121.263 19.195  1.00 44.79 ? 794  ASN A CG  1 
ATOM   6372 O OD1 . ASN A 1 794 ? 92.351 120.265 18.483  1.00 47.64 ? 794  ASN A OD1 1 
ATOM   6373 N ND2 . ASN A 1 794 ? 93.229 121.787 19.888  1.00 49.48 ? 794  ASN A ND2 1 
ATOM   6374 N N   . ARG A 1 795 ? 87.399 121.484 19.845  1.00 35.66 ? 795  ARG A N   1 
ATOM   6375 C CA  . ARG A 1 795 ? 86.208 122.349 19.829  1.00 35.51 ? 795  ARG A CA  1 
ATOM   6376 C C   . ARG A 1 795 ? 84.884 121.594 20.009  1.00 34.36 ? 795  ARG A C   1 
ATOM   6377 O O   . ARG A 1 795 ? 84.632 120.627 19.303  1.00 33.94 ? 795  ARG A O   1 
ATOM   6378 C CB  . ARG A 1 795 ? 86.191 123.136 18.528  1.00 35.26 ? 795  ARG A CB  1 
ATOM   6379 C CG  . ARG A 1 795 ? 85.135 124.181 18.361  1.00 40.19 ? 795  ARG A CG  1 
ATOM   6380 C CD  . ARG A 1 795 ? 85.136 124.631 16.883  1.00 48.76 ? 795  ARG A CD  1 
ATOM   6381 N NE  . ARG A 1 795 ? 84.415 125.891 16.691  1.00 57.99 ? 795  ARG A NE  1 
ATOM   6382 C CZ  . ARG A 1 795 ? 84.964 127.049 16.308  1.00 62.07 ? 795  ARG A CZ  1 
ATOM   6383 N NH1 . ARG A 1 795 ? 86.273 127.130 16.035  1.00 63.36 ? 795  ARG A NH1 1 
ATOM   6384 N NH2 . ARG A 1 795 ? 84.188 128.132 16.178  1.00 63.37 ? 795  ARG A NH2 1 
ATOM   6385 N N   . LEU A 1 796 ? 84.060 122.078 20.941  1.00 33.05 ? 796  LEU A N   1 
ATOM   6386 C CA  . LEU A 1 796 ? 82.681 121.677 21.122  1.00 31.99 ? 796  LEU A CA  1 
ATOM   6387 C C   . LEU A 1 796 ? 81.840 122.852 20.654  1.00 32.65 ? 796  LEU A C   1 
ATOM   6388 O O   . LEU A 1 796 ? 82.070 123.964 21.092  1.00 33.33 ? 796  LEU A O   1 
ATOM   6389 C CB  . LEU A 1 796 ? 82.378 121.422 22.602  1.00 31.55 ? 796  LEU A CB  1 
ATOM   6390 C CG  . LEU A 1 796 ? 80.897 121.353 22.964  1.00 31.28 ? 796  LEU A CG  1 
ATOM   6391 C CD1 . LEU A 1 796 ? 80.193 120.171 22.205  1.00 26.92 ? 796  LEU A CD1 1 
ATOM   6392 C CD2 . LEU A 1 796 ? 80.752 121.211 24.492  1.00 31.41 ? 796  LEU A CD2 1 
ATOM   6393 N N   . GLU A 1 797 ? 80.894 122.619 19.756  1.00 31.62 ? 797  GLU A N   1 
ATOM   6394 C CA  . GLU A 1 797 ? 79.950 123.662 19.373  1.00 32.95 ? 797  GLU A CA  1 
ATOM   6395 C C   . GLU A 1 797 ? 78.563 123.289 19.840  1.00 32.79 ? 797  GLU A C   1 
ATOM   6396 O O   . GLU A 1 797 ? 78.104 122.160 19.587  1.00 30.08 ? 797  GLU A O   1 
ATOM   6397 C CB  . GLU A 1 797 ? 79.916 123.842 17.863  1.00 34.07 ? 797  GLU A CB  1 
ATOM   6398 C CG  . GLU A 1 797 ? 81.213 124.392 17.305  1.00 42.39 ? 797  GLU A CG  1 
ATOM   6399 C CD  . GLU A 1 797 ? 81.091 124.769 15.834  1.00 53.64 ? 797  GLU A CD  1 
ATOM   6400 O OE1 . GLU A 1 797 ? 79.983 124.554 15.244  1.00 56.46 ? 797  GLU A OE1 1 
ATOM   6401 O OE2 . GLU A 1 797 ? 82.111 125.278 15.275  1.00 58.12 ? 797  GLU A OE2 1 
ATOM   6402 N N   . VAL A 1 798 ? 77.907 124.240 20.522  1.00 31.98 ? 798  VAL A N   1 
ATOM   6403 C CA  . VAL A 1 798 ? 76.504 124.113 20.832  1.00 32.14 ? 798  VAL A CA  1 
ATOM   6404 C C   . VAL A 1 798 ? 75.728 125.072 19.902  1.00 33.10 ? 798  VAL A C   1 
ATOM   6405 O O   . VAL A 1 798 ? 75.896 126.281 19.974  1.00 31.20 ? 798  VAL A O   1 
ATOM   6406 C CB  . VAL A 1 798 ? 76.195 124.357 22.351  1.00 32.41 ? 798  VAL A CB  1 
ATOM   6407 C CG1 . VAL A 1 798 ? 74.742 124.015 22.637  1.00 31.23 ? 798  VAL A CG1 1 
ATOM   6408 C CG2 . VAL A 1 798 ? 77.107 123.509 23.246  1.00 30.04 ? 798  VAL A CG2 1 
ATOM   6409 N N   . ASN A 1 799 ? 74.884 124.487 19.053  1.00 32.61 ? 799  ASN A N   1 
ATOM   6410 C CA  . ASN A 1 799 ? 74.257 125.125 17.913  1.00 34.18 ? 799  ASN A CA  1 
ATOM   6411 C C   . ASN A 1 799 ? 72.750 124.938 18.098  1.00 33.41 ? 799  ASN A C   1 
ATOM   6412 O O   . ASN A 1 799 ? 72.320 123.848 18.404  1.00 32.99 ? 799  ASN A O   1 
ATOM   6413 C CB  . ASN A 1 799 ? 74.720 124.333 16.674  1.00 35.00 ? 799  ASN A CB  1 
ATOM   6414 C CG  . ASN A 1 799 ? 74.526 125.074 15.383  1.00 40.71 ? 799  ASN A CG  1 
ATOM   6415 O OD1 . ASN A 1 799 ? 73.554 125.818 15.208  1.00 49.49 ? 799  ASN A OD1 1 
ATOM   6416 N ND2 . ASN A 1 799 ? 75.449 124.861 14.431  1.00 48.10 ? 799  ASN A ND2 1 
ATOM   6417 N N   . ILE A 1 800 ? 71.942 125.979 17.916  1.00 32.72 ? 800  ILE A N   1 
ATOM   6418 C CA  . ILE A 1 800 ? 70.504 125.895 18.194  1.00 32.79 ? 800  ILE A CA  1 
ATOM   6419 C C   . ILE A 1 800 ? 69.702 125.879 16.901  1.00 32.47 ? 800  ILE A C   1 
ATOM   6420 O O   . ILE A 1 800 ? 69.880 126.751 16.060  1.00 31.22 ? 800  ILE A O   1 
ATOM   6421 C CB  . ILE A 1 800 ? 70.050 127.105 19.047  1.00 32.93 ? 800  ILE A CB  1 
ATOM   6422 C CG1 . ILE A 1 800 ? 70.968 127.298 20.246  1.00 33.65 ? 800  ILE A CG1 1 
ATOM   6423 C CG2 . ILE A 1 800 ? 68.612 126.980 19.451  1.00 34.71 ? 800  ILE A CG2 1 
ATOM   6424 C CD1 . ILE A 1 800 ? 71.012 126.118 21.260  1.00 30.99 ? 800  ILE A CD1 1 
ATOM   6425 N N   . SER A 1 801 ? 68.810 124.905 16.717  1.00 31.65 ? 801  SER A N   1 
ATOM   6426 C CA  . SER A 1 801 ? 68.093 124.874 15.453  1.00 33.06 ? 801  SER A CA  1 
ATOM   6427 C C   . SER A 1 801 ? 66.609 125.298 15.501  1.00 33.26 ? 801  SER A C   1 
ATOM   6428 O O   . SER A 1 801 ? 66.071 125.764 14.495  1.00 33.77 ? 801  SER A O   1 
ATOM   6429 C CB  . SER A 1 801 ? 68.292 123.559 14.718  1.00 33.62 ? 801  SER A CB  1 
ATOM   6430 O OG  . SER A 1 801 ? 67.605 122.514 15.341  1.00 37.84 ? 801  SER A OG  1 
ATOM   6431 N N   . GLN A 1 802 ? 65.970 125.121 16.652  1.00 31.75 ? 802  GLN A N   1 
ATOM   6432 C CA  . GLN A 1 802 ? 64.587 125.558 16.884  1.00 31.97 ? 802  GLN A CA  1 
ATOM   6433 C C   . GLN A 1 802 ? 64.597 126.104 18.279  1.00 31.08 ? 802  GLN A C   1 
ATOM   6434 O O   . GLN A 1 802 ? 65.051 125.449 19.208  1.00 30.24 ? 802  GLN A O   1 
ATOM   6435 C CB  . GLN A 1 802 ? 63.597 124.393 16.776  1.00 31.52 ? 802  GLN A CB  1 
ATOM   6436 C CG  . GLN A 1 802 ? 62.163 124.736 17.143  1.00 31.77 ? 802  GLN A CG  1 
ATOM   6437 C CD  . GLN A 1 802 ? 61.459 125.516 16.099  1.00 34.05 ? 802  GLN A CD  1 
ATOM   6438 O OE1 . GLN A 1 802 ? 60.651 126.404 16.401  1.00 38.37 ? 802  GLN A OE1 1 
ATOM   6439 N NE2 . GLN A 1 802 ? 61.733 125.213 14.869  1.00 28.52 ? 802  GLN A NE2 1 
ATOM   6440 N N   . SER A 1 803 ? 64.108 127.313 18.447  1.00 31.24 ? 803  SER A N   1 
ATOM   6441 C CA  . SER A 1 803 ? 64.307 127.974 19.725  1.00 33.18 ? 803  SER A CA  1 
ATOM   6442 C C   . SER A 1 803 ? 63.022 128.682 20.082  1.00 33.75 ? 803  SER A C   1 
ATOM   6443 O O   . SER A 1 803 ? 63.026 129.894 20.282  1.00 35.51 ? 803  SER A O   1 
ATOM   6444 C CB  . SER A 1 803 ? 65.463 128.977 19.592  1.00 34.10 ? 803  SER A CB  1 
ATOM   6445 O OG  . SER A 1 803 ? 65.812 129.508 20.864  1.00 38.55 ? 803  SER A OG  1 
ATOM   6446 N N   . THR A 1 804 ? 61.920 127.942 20.160  1.00 31.82 ? 804  THR A N   1 
ATOM   6447 C CA  . THR A 1 804 ? 60.640 128.539 20.470  1.00 30.97 ? 804  THR A CA  1 
ATOM   6448 C C   . THR A 1 804 ? 60.132 128.092 21.847  1.00 30.30 ? 804  THR A C   1 
ATOM   6449 O O   . THR A 1 804 ? 58.993 128.323 22.181  1.00 29.54 ? 804  THR A O   1 
ATOM   6450 C CB  . THR A 1 804 ? 59.589 128.185 19.429  1.00 31.51 ? 804  THR A CB  1 
ATOM   6451 O OG1 . THR A 1 804 ? 59.780 126.819 19.031  1.00 29.17 ? 804  THR A OG1 1 
ATOM   6452 C CG2 . THR A 1 804 ? 59.739 129.086 18.183  1.00 33.66 ? 804  THR A CG2 1 
ATOM   6453 N N   . TYR A 1 805 ? 60.976 127.453 22.630  1.00 27.20 ? 805  TYR A N   1 
ATOM   6454 C CA  . TYR A 1 805 ? 60.664 127.249 24.037  1.00 27.83 ? 805  TYR A CA  1 
ATOM   6455 C C   . TYR A 1 805 ? 61.829 127.645 24.900  1.00 27.81 ? 805  TYR A C   1 
ATOM   6456 O O   . TYR A 1 805 ? 62.931 127.152 24.713  1.00 27.81 ? 805  TYR A O   1 
ATOM   6457 C CB  . TYR A 1 805 ? 60.310 125.794 24.338  1.00 26.31 ? 805  TYR A CB  1 
ATOM   6458 C CG  . TYR A 1 805 ? 59.880 125.562 25.751  1.00 25.28 ? 805  TYR A CG  1 
ATOM   6459 C CD1 . TYR A 1 805 ? 58.653 126.074 26.223  1.00 26.72 ? 805  TYR A CD1 1 
ATOM   6460 C CD2 . TYR A 1 805 ? 60.681 124.843 26.620  1.00 22.32 ? 805  TYR A CD2 1 
ATOM   6461 C CE1 . TYR A 1 805 ? 58.255 125.888 27.526  1.00 27.36 ? 805  TYR A CE1 1 
ATOM   6462 C CE2 . TYR A 1 805 ? 60.294 124.627 27.927  1.00 23.04 ? 805  TYR A CE2 1 
ATOM   6463 C CZ  . TYR A 1 805 ? 59.076 125.154 28.380  1.00 25.78 ? 805  TYR A CZ  1 
ATOM   6464 O OH  . TYR A 1 805 ? 58.677 124.947 29.676  1.00 24.63 ? 805  TYR A OH  1 
ATOM   6465 N N   . LYS A 1 806 ? 61.565 128.495 25.883  1.00 28.80 ? 806  LYS A N   1 
ATOM   6466 C CA  . LYS A 1 806 ? 62.580 128.816 26.856  1.00 29.64 ? 806  LYS A CA  1 
ATOM   6467 C C   . LYS A 1 806 ? 62.101 128.410 28.235  1.00 29.63 ? 806  LYS A C   1 
ATOM   6468 O O   . LYS A 1 806 ? 61.190 129.018 28.812  1.00 29.81 ? 806  LYS A O   1 
ATOM   6469 C CB  . LYS A 1 806 ? 62.986 130.298 26.794  1.00 30.74 ? 806  LYS A CB  1 
ATOM   6470 C CG  . LYS A 1 806 ? 63.954 130.657 27.913  1.00 35.68 ? 806  LYS A CG  1 
ATOM   6471 C CD  . LYS A 1 806 ? 65.194 131.350 27.419  1.00 42.00 ? 806  LYS A CD  1 
ATOM   6472 C CE  . LYS A 1 806 ? 66.137 131.699 28.598  1.00 44.26 ? 806  LYS A CE  1 
ATOM   6473 N NZ  . LYS A 1 806 ? 67.490 132.142 28.139  1.00 46.59 ? 806  LYS A NZ  1 
ATOM   6474 N N   . ASP A 1 807 ? 62.711 127.362 28.775  1.00 28.88 ? 807  ASP A N   1 
ATOM   6475 C CA  . ASP A 1 807 ? 62.322 126.865 30.073  1.00 27.76 ? 807  ASP A CA  1 
ATOM   6476 C C   . ASP A 1 807 ? 62.527 127.983 31.127  1.00 28.47 ? 807  ASP A C   1 
ATOM   6477 O O   . ASP A 1 807 ? 63.646 128.488 31.283  1.00 26.60 ? 807  ASP A O   1 
ATOM   6478 C CB  . ASP A 1 807 ? 63.179 125.647 30.432  1.00 28.46 ? 807  ASP A CB  1 
ATOM   6479 C CG  . ASP A 1 807 ? 62.634 124.890 31.620  1.00 28.17 ? 807  ASP A CG  1 
ATOM   6480 O OD1 . ASP A 1 807 ? 62.455 125.516 32.668  1.00 30.85 ? 807  ASP A OD1 1 
ATOM   6481 O OD2 . ASP A 1 807 ? 62.350 123.691 31.489  1.00 29.29 ? 807  ASP A OD2 1 
ATOM   6482 N N   . PRO A 1 808 ? 61.455 128.344 31.879  1.00 29.23 ? 808  PRO A N   1 
ATOM   6483 C CA  . PRO A 1 808 ? 61.546 129.403 32.888  1.00 30.44 ? 808  PRO A CA  1 
ATOM   6484 C C   . PRO A 1 808 ? 62.348 129.007 34.115  1.00 31.09 ? 808  PRO A C   1 
ATOM   6485 O O   . PRO A 1 808 ? 62.585 129.838 34.980  1.00 32.53 ? 808  PRO A O   1 
ATOM   6486 C CB  . PRO A 1 808 ? 60.090 129.594 33.323  1.00 30.35 ? 808  PRO A CB  1 
ATOM   6487 C CG  . PRO A 1 808 ? 59.500 128.224 33.159  1.00 31.19 ? 808  PRO A CG  1 
ATOM   6488 C CD  . PRO A 1 808 ? 60.112 127.737 31.848  1.00 29.20 ? 808  PRO A CD  1 
ATOM   6489 N N   . ASN A 1 809 ? 62.769 127.758 34.212  1.00 32.30 ? 809  ASN A N   1 
ATOM   6490 C CA  . ASN A 1 809 ? 63.593 127.358 35.348  1.00 34.02 ? 809  ASN A CA  1 
ATOM   6491 C C   . ASN A 1 809 ? 65.046 127.679 35.152  1.00 34.53 ? 809  ASN A C   1 
ATOM   6492 O O   . ASN A 1 809 ? 65.875 127.302 35.975  1.00 37.19 ? 809  ASN A O   1 
ATOM   6493 C CB  . ASN A 1 809 ? 63.391 125.883 35.711  1.00 33.68 ? 809  ASN A CB  1 
ATOM   6494 C CG  . ASN A 1 809 ? 62.029 125.613 36.261  1.00 34.34 ? 809  ASN A CG  1 
ATOM   6495 O OD1 . ASN A 1 809 ? 61.336 124.681 35.842  1.00 34.80 ? 809  ASN A OD1 1 
ATOM   6496 N ND2 . ASN A 1 809 ? 61.614 126.444 37.191  1.00 33.91 ? 809  ASN A ND2 1 
ATOM   6497 N N   . ASN A 1 810 ? 65.372 128.364 34.056  1.00 35.98 ? 810  ASN A N   1 
ATOM   6498 C CA  . ASN A 1 810 ? 66.762 128.878 33.830  1.00 36.94 ? 810  ASN A CA  1 
ATOM   6499 C C   . ASN A 1 810 ? 67.861 127.749 33.877  1.00 35.10 ? 810  ASN A C   1 
ATOM   6500 O O   . ASN A 1 810 ? 68.848 127.834 34.602  1.00 35.40 ? 810  ASN A O   1 
ATOM   6501 C CB  . ASN A 1 810 ? 67.081 130.030 34.817  1.00 38.63 ? 810  ASN A CB  1 
ATOM   6502 C CG  . ASN A 1 810 ? 67.919 131.169 34.188  1.00 43.06 ? 810  ASN A CG  1 
ATOM   6503 O OD1 . ASN A 1 810 ? 68.056 131.300 32.953  1.00 48.88 ? 810  ASN A OD1 1 
ATOM   6504 N ND2 . ASN A 1 810 ? 68.471 132.003 35.050  1.00 47.67 ? 810  ASN A ND2 1 
ATOM   6505 N N   . LEU A 1 811 ? 67.644 126.696 33.088  1.00 32.43 ? 811  LEU A N   1 
ATOM   6506 C CA  . LEU A 1 811 ? 68.521 125.519 33.059  1.00 28.82 ? 811  LEU A CA  1 
ATOM   6507 C C   . LEU A 1 811 ? 69.859 125.779 32.354  1.00 27.20 ? 811  LEU A C   1 
ATOM   6508 O O   . LEU A 1 811 ? 69.921 126.523 31.399  1.00 26.15 ? 811  LEU A O   1 
ATOM   6509 C CB  . LEU A 1 811 ? 67.777 124.409 32.316  1.00 28.10 ? 811  LEU A CB  1 
ATOM   6510 C CG  . LEU A 1 811 ? 66.483 123.921 32.949  1.00 25.72 ? 811  LEU A CG  1 
ATOM   6511 C CD1 . LEU A 1 811 ? 65.989 122.696 32.231  1.00 24.42 ? 811  LEU A CD1 1 
ATOM   6512 C CD2 . LEU A 1 811 ? 66.652 123.630 34.438  1.00 23.84 ? 811  LEU A CD2 1 
ATOM   6513 N N   . ALA A 1 812 ? 70.921 125.110 32.793  1.00 26.65 ? 812  ALA A N   1 
ATOM   6514 C CA  . ALA A 1 812 ? 72.217 125.276 32.165  1.00 26.85 ? 812  ALA A CA  1 
ATOM   6515 C C   . ALA A 1 812 ? 73.028 123.993 32.295  1.00 26.51 ? 812  ALA A C   1 
ATOM   6516 O O   . ALA A 1 812 ? 72.848 123.234 33.237  1.00 25.54 ? 812  ALA A O   1 
ATOM   6517 C CB  . ALA A 1 812 ? 72.980 126.471 32.816  1.00 26.26 ? 812  ALA A CB  1 
ATOM   6518 N N   . PHE A 1 813 ? 73.896 123.761 31.323  1.00 26.58 ? 813  PHE A N   1 
ATOM   6519 C CA  . PHE A 1 813 ? 74.909 122.706 31.403  1.00 27.05 ? 813  PHE A CA  1 
ATOM   6520 C C   . PHE A 1 813 ? 75.961 123.203 32.332  1.00 27.92 ? 813  PHE A C   1 
ATOM   6521 O O   . PHE A 1 813 ? 76.540 124.265 32.100  1.00 28.12 ? 813  PHE A O   1 
ATOM   6522 C CB  . PHE A 1 813 ? 75.511 122.433 30.011  1.00 26.97 ? 813  PHE A CB  1 
ATOM   6523 C CG  . PHE A 1 813 ? 74.517 121.956 29.022  1.00 26.86 ? 813  PHE A CG  1 
ATOM   6524 C CD1 . PHE A 1 813 ? 74.175 120.606 28.961  1.00 26.37 ? 813  PHE A CD1 1 
ATOM   6525 C CD2 . PHE A 1 813 ? 73.858 122.864 28.193  1.00 28.40 ? 813  PHE A CD2 1 
ATOM   6526 C CE1 . PHE A 1 813 ? 73.211 120.176 28.054  1.00 24.74 ? 813  PHE A CE1 1 
ATOM   6527 C CE2 . PHE A 1 813 ? 72.899 122.451 27.274  1.00 26.95 ? 813  PHE A CE2 1 
ATOM   6528 C CZ  . PHE A 1 813 ? 72.580 121.109 27.199  1.00 28.72 ? 813  PHE A CZ  1 
ATOM   6529 N N   . ASN A 1 814 ? 76.207 122.479 33.419  1.00 29.05 ? 814  ASN A N   1 
ATOM   6530 C CA  . ASN A 1 814 ? 77.231 122.933 34.312  1.00 29.84 ? 814  ASN A CA  1 
ATOM   6531 C C   . ASN A 1 814 ? 78.350 121.899 34.423  1.00 29.73 ? 814  ASN A C   1 
ATOM   6532 O O   . ASN A 1 814 ? 79.250 122.055 35.230  1.00 29.60 ? 814  ASN A O   1 
ATOM   6533 C CB  . ASN A 1 814 ? 76.667 123.310 35.698  1.00 30.26 ? 814  ASN A CB  1 
ATOM   6534 C CG  . ASN A 1 814 ? 76.275 122.105 36.514  1.00 34.90 ? 814  ASN A CG  1 
ATOM   6535 O OD1 . ASN A 1 814 ? 76.076 121.011 35.971  1.00 41.97 ? 814  ASN A OD1 1 
ATOM   6536 N ND2 . ASN A 1 814 ? 76.160 122.280 37.841  1.00 41.53 ? 814  ASN A ND2 1 
ATOM   6537 N N   . GLU A 1 815 ? 78.292 120.850 33.607  1.00 29.51 ? 815  GLU A N   1 
ATOM   6538 C CA  . GLU A 1 815 ? 79.369 119.838 33.557  1.00 30.07 ? 815  GLU A CA  1 
ATOM   6539 C C   . GLU A 1 815 ? 79.437 119.227 32.170  1.00 29.89 ? 815  GLU A C   1 
ATOM   6540 O O   . GLU A 1 815 ? 78.393 118.924 31.554  1.00 28.67 ? 815  GLU A O   1 
ATOM   6541 C CB  . GLU A 1 815 ? 79.131 118.714 34.542  1.00 30.41 ? 815  GLU A CB  1 
ATOM   6542 C CG  . GLU A 1 815 ? 80.281 117.719 34.612  1.00 38.69 ? 815  GLU A CG  1 
ATOM   6543 C CD  . GLU A 1 815 ? 79.954 116.500 35.479  1.00 50.93 ? 815  GLU A CD  1 
ATOM   6544 O OE1 . GLU A 1 815 ? 79.655 116.693 36.698  1.00 55.20 ? 815  GLU A OE1 1 
ATOM   6545 O OE2 . GLU A 1 815 ? 80.014 115.346 34.947  1.00 55.93 ? 815  GLU A OE2 1 
ATOM   6546 N N   . ILE A 1 816 ? 80.660 119.031 31.695  1.00 27.96 ? 816  ILE A N   1 
ATOM   6547 C CA  . ILE A 1 816 ? 80.909 118.342 30.430  1.00 27.40 ? 816  ILE A CA  1 
ATOM   6548 C C   . ILE A 1 816 ? 81.977 117.283 30.727  1.00 27.52 ? 816  ILE A C   1 
ATOM   6549 O O   . ILE A 1 816 ? 83.059 117.611 31.199  1.00 26.27 ? 816  ILE A O   1 
ATOM   6550 C CB  . ILE A 1 816 ? 81.400 119.310 29.330  1.00 27.16 ? 816  ILE A CB  1 
ATOM   6551 C CG1 . ILE A 1 816 ? 80.373 120.413 29.071  1.00 27.36 ? 816  ILE A CG1 1 
ATOM   6552 C CG2 . ILE A 1 816 ? 81.721 118.522 28.029  1.00 25.64 ? 816  ILE A CG2 1 
ATOM   6553 C CD1 . ILE A 1 816 ? 80.886 121.527 28.176  1.00 27.59 ? 816  ILE A CD1 1 
ATOM   6554 N N   . LYS A 1 817 ? 81.641 116.016 30.509  1.00 25.82 ? 817  LYS A N   1 
ATOM   6555 C CA  . LYS A 1 817 ? 82.561 114.920 30.667  1.00 27.67 ? 817  LYS A CA  1 
ATOM   6556 C C   . LYS A 1 817 ? 82.999 114.472 29.267  1.00 27.24 ? 817  LYS A C   1 
ATOM   6557 O O   . LYS A 1 817 ? 82.149 114.160 28.431  1.00 28.83 ? 817  LYS A O   1 
ATOM   6558 C CB  . LYS A 1 817 ? 81.867 113.772 31.419  1.00 26.95 ? 817  LYS A CB  1 
ATOM   6559 C CG  . LYS A 1 817 ? 82.729 112.552 31.756  1.00 29.93 ? 817  LYS A CG  1 
ATOM   6560 C CD  . LYS A 1 817 ? 81.893 111.617 32.637  1.00 31.30 ? 817  LYS A CD  1 
ATOM   6561 C CE  . LYS A 1 817 ? 82.713 110.601 33.370  1.00 38.03 ? 817  LYS A CE  1 
ATOM   6562 N NZ  . LYS A 1 817 ? 81.928 109.350 33.673  1.00 39.93 ? 817  LYS A NZ  1 
ATOM   6563 N N   . ILE A 1 818 ? 84.303 114.453 29.009  1.00 26.46 ? 818  ILE A N   1 
ATOM   6564 C CA  . ILE A 1 818 ? 84.820 114.006 27.708  1.00 25.81 ? 818  ILE A CA  1 
ATOM   6565 C C   . ILE A 1 818 ? 85.563 112.702 27.910  1.00 25.46 ? 818  ILE A C   1 
ATOM   6566 O O   . ILE A 1 818 ? 86.451 112.613 28.765  1.00 23.62 ? 818  ILE A O   1 
ATOM   6567 C CB  . ILE A 1 818 ? 85.710 115.072 27.010  1.00 25.42 ? 818  ILE A CB  1 
ATOM   6568 C CG1 . ILE A 1 818 ? 85.059 116.446 27.063  1.00 26.51 ? 818  ILE A CG1 1 
ATOM   6569 C CG2 . ILE A 1 818 ? 85.945 114.685 25.537  1.00 23.94 ? 818  ILE A CG2 1 
ATOM   6570 C CD1 . ILE A 1 818 ? 86.023 117.597 26.758  1.00 28.66 ? 818  ILE A CD1 1 
ATOM   6571 N N   . LEU A 1 819 ? 85.166 111.683 27.130  1.00 24.25 ? 819  LEU A N   1 
ATOM   6572 C CA  . LEU A 1 819 ? 85.728 110.365 27.231  1.00 24.98 ? 819  LEU A CA  1 
ATOM   6573 C C   . LEU A 1 819 ? 86.698 110.115 26.056  1.00 25.31 ? 819  LEU A C   1 
ATOM   6574 O O   . LEU A 1 819 ? 86.461 110.544 24.956  1.00 25.41 ? 819  LEU A O   1 
ATOM   6575 C CB  . LEU A 1 819 ? 84.594 109.332 27.199  1.00 24.15 ? 819  LEU A CB  1 
ATOM   6576 C CG  . LEU A 1 819 ? 83.413 109.565 28.156  1.00 25.94 ? 819  LEU A CG  1 
ATOM   6577 C CD1 . LEU A 1 819 ? 82.382 108.421 28.053  1.00 26.13 ? 819  LEU A CD1 1 
ATOM   6578 C CD2 . LEU A 1 819 ? 83.975 109.636 29.573  1.00 23.89 ? 819  LEU A CD2 1 
ATOM   6579 N N   . GLY A 1 820 ? 87.771 109.398 26.308  1.00 26.31 ? 820  GLY A N   1 
ATOM   6580 C CA  . GLY A 1 820 ? 88.693 109.012 25.247  1.00 26.69 ? 820  GLY A CA  1 
ATOM   6581 C C   . GLY A 1 820 ? 89.432 110.214 24.734  1.00 27.97 ? 820  GLY A C   1 
ATOM   6582 O O   . GLY A 1 820 ? 89.626 110.357 23.547  1.00 28.97 ? 820  GLY A O   1 
ATOM   6583 N N   . THR A 1 821 ? 89.831 111.099 25.630  1.00 27.78 ? 821  THR A N   1 
ATOM   6584 C CA  . THR A 1 821 ? 90.501 112.313 25.222  1.00 29.67 ? 821  THR A CA  1 
ATOM   6585 C C   . THR A 1 821 ? 91.890 112.417 25.866  1.00 30.40 ? 821  THR A C   1 
ATOM   6586 O O   . THR A 1 821 ? 92.119 111.938 26.985  1.00 29.34 ? 821  THR A O   1 
ATOM   6587 C CB  . THR A 1 821 ? 89.703 113.573 25.596  1.00 28.97 ? 821  THR A CB  1 
ATOM   6588 O OG1 . THR A 1 821 ? 90.375 114.739 25.090  1.00 29.68 ? 821  THR A OG1 1 
ATOM   6589 C CG2 . THR A 1 821 ? 89.510 113.708 27.144  1.00 27.42 ? 821  THR A CG2 1 
ATOM   6590 N N   . GLU A 1 822 ? 92.801 113.084 25.166  1.00 32.85 ? 822  GLU A N   1 
ATOM   6591 C CA  . GLU A 1 822 ? 94.105 113.451 25.756  1.00 34.37 ? 822  GLU A CA  1 
ATOM   6592 C C   . GLU A 1 822 ? 93.861 114.712 26.597  1.00 34.67 ? 822  GLU A C   1 
ATOM   6593 O O   . GLU A 1 822 ? 92.821 115.362 26.455  1.00 33.78 ? 822  GLU A O   1 
ATOM   6594 C CB  . GLU A 1 822 ? 95.125 113.724 24.643  1.00 35.15 ? 822  GLU A CB  1 
ATOM   6595 C CG  . GLU A 1 822 ? 95.536 112.457 23.856  1.00 39.45 ? 822  GLU A CG  1 
ATOM   6596 C CD  . GLU A 1 822 ? 96.180 111.365 24.742  1.00 46.34 ? 822  GLU A CD  1 
ATOM   6597 O OE1 . GLU A 1 822 ? 97.042 111.697 25.586  1.00 46.80 ? 822  GLU A OE1 1 
ATOM   6598 O OE2 . GLU A 1 822 ? 95.839 110.155 24.592  1.00 49.87 ? 822  GLU A OE2 1 
ATOM   6599 N N   . GLU A 1 823 ? 94.814 115.084 27.447  1.00 36.46 ? 823  GLU A N   1 
ATOM   6600 C CA  . GLU A 1 823 ? 94.570 116.166 28.414  1.00 38.39 ? 823  GLU A CA  1 
ATOM   6601 C C   . GLU A 1 823 ? 94.202 117.474 27.745  1.00 39.36 ? 823  GLU A C   1 
ATOM   6602 O O   . GLU A 1 823 ? 95.012 118.009 26.992  1.00 39.79 ? 823  GLU A O   1 
ATOM   6603 C CB  . GLU A 1 823 ? 95.776 116.385 29.336  1.00 38.42 ? 823  GLU A CB  1 
ATOM   6604 C CG  . GLU A 1 823 ? 95.589 117.595 30.219  1.00 42.37 ? 823  GLU A CG  1 
ATOM   6605 C CD  . GLU A 1 823 ? 96.327 117.518 31.516  1.00 47.62 ? 823  GLU A CD  1 
ATOM   6606 O OE1 . GLU A 1 823 ? 97.382 116.858 31.550  1.00 51.04 ? 823  GLU A OE1 1 
ATOM   6607 O OE2 . GLU A 1 823 ? 95.845 118.129 32.506  1.00 50.67 ? 823  GLU A OE2 1 
ATOM   6608 N N   . PRO A 1 824 ? 92.991 118.009 28.034  1.00 39.90 ? 824  PRO A N   1 
ATOM   6609 C CA  . PRO A 1 824 ? 92.644 119.293 27.445  1.00 40.70 ? 824  PRO A CA  1 
ATOM   6610 C C   . PRO A 1 824 ? 93.338 120.383 28.227  1.00 41.68 ? 824  PRO A C   1 
ATOM   6611 O O   . PRO A 1 824 ? 93.454 120.294 29.466  1.00 41.85 ? 824  PRO A O   1 
ATOM   6612 C CB  . PRO A 1 824 ? 91.131 119.410 27.663  1.00 41.05 ? 824  PRO A CB  1 
ATOM   6613 C CG  . PRO A 1 824 ? 90.706 118.155 28.373  1.00 40.94 ? 824  PRO A CG  1 
ATOM   6614 C CD  . PRO A 1 824 ? 91.932 117.519 28.928  1.00 40.15 ? 824  PRO A CD  1 
ATOM   6615 N N   . SER A 1 825 ? 93.814 121.400 27.528  1.00 41.83 ? 825  SER A N   1 
ATOM   6616 C CA  . SER A 1 825 ? 94.359 122.527 28.237  1.00 42.11 ? 825  SER A CA  1 
ATOM   6617 C C   . SER A 1 825 ? 93.774 123.810 27.721  1.00 42.20 ? 825  SER A C   1 
ATOM   6618 O O   . SER A 1 825 ? 93.241 123.872 26.624  1.00 41.64 ? 825  SER A O   1 
ATOM   6619 C CB  . SER A 1 825 ? 95.886 122.511 28.233  1.00 42.58 ? 825  SER A CB  1 
ATOM   6620 O OG  . SER A 1 825 ? 96.434 122.600 26.933  1.00 43.49 ? 825  SER A OG  1 
ATOM   6621 N N   . ASN A 1 826 ? 93.820 124.822 28.572  1.00 43.23 ? 826  ASN A N   1 
ATOM   6622 C CA  . ASN A 1 826 ? 93.453 126.176 28.199  1.00 43.88 ? 826  ASN A CA  1 
ATOM   6623 C C   . ASN A 1 826 ? 92.066 126.235 27.529  1.00 42.46 ? 826  ASN A C   1 
ATOM   6624 O O   . ASN A 1 826 ? 91.892 126.703 26.388  1.00 42.42 ? 826  ASN A O   1 
ATOM   6625 C CB  . ASN A 1 826 ? 94.606 126.817 27.402  1.00 45.26 ? 826  ASN A CB  1 
ATOM   6626 C CG  . ASN A 1 826 ? 95.943 126.845 28.218  1.00 49.31 ? 826  ASN A CG  1 
ATOM   6627 O OD1 . ASN A 1 826 ? 95.976 127.333 29.364  1.00 53.67 ? 826  ASN A OD1 1 
ATOM   6628 N ND2 . ASN A 1 826 ? 97.029 126.314 27.631  1.00 51.69 ? 826  ASN A ND2 1 
ATOM   6629 N N   . VAL A 1 827 ? 91.097 125.711 28.279  1.00 40.88 ? 827  VAL A N   1 
ATOM   6630 C CA  . VAL A 1 827 ? 89.705 125.655 27.880  1.00 39.61 ? 827  VAL A CA  1 
ATOM   6631 C C   . VAL A 1 827 ? 89.089 127.043 27.869  1.00 39.44 ? 827  VAL A C   1 
ATOM   6632 O O   . VAL A 1 827 ? 89.131 127.780 28.866  1.00 39.53 ? 827  VAL A O   1 
ATOM   6633 C CB  . VAL A 1 827 ? 88.882 124.680 28.798  1.00 39.09 ? 827  VAL A CB  1 
ATOM   6634 C CG1 . VAL A 1 827 ? 87.433 124.672 28.404  1.00 38.90 ? 827  VAL A CG1 1 
ATOM   6635 C CG2 . VAL A 1 827 ? 89.413 123.308 28.695  1.00 36.63 ? 827  VAL A CG2 1 
ATOM   6636 N N   . THR A 1 828 ? 88.532 127.401 26.723  1.00 39.93 ? 828  THR A N   1 
ATOM   6637 C CA  . THR A 1 828 ? 87.838 128.670 26.541  1.00 40.91 ? 828  THR A CA  1 
ATOM   6638 C C   . THR A 1 828 ? 86.378 128.446 26.238  1.00 40.33 ? 828  THR A C   1 
ATOM   6639 O O   . THR A 1 828 ? 86.011 127.470 25.586  1.00 40.68 ? 828  THR A O   1 
ATOM   6640 C CB  . THR A 1 828 ? 88.402 129.456 25.320  1.00 41.07 ? 828  THR A CB  1 
ATOM   6641 O OG1 . THR A 1 828 ? 89.823 129.569 25.421  1.00 44.88 ? 828  THR A OG1 1 
ATOM   6642 C CG2 . THR A 1 828 ? 87.805 130.866 25.246  1.00 42.52 ? 828  THR A CG2 1 
ATOM   6643 N N   . VAL A 1 829 ? 85.553 129.392 26.668  1.00 40.06 ? 829  VAL A N   1 
ATOM   6644 C CA  . VAL A 1 829 ? 84.129 129.399 26.355  1.00 39.56 ? 829  VAL A CA  1 
ATOM   6645 C C   . VAL A 1 829 ? 83.770 130.690 25.640  1.00 39.99 ? 829  VAL A C   1 
ATOM   6646 O O   . VAL A 1 829 ? 84.035 131.768 26.139  1.00 40.31 ? 829  VAL A O   1 
ATOM   6647 C CB  . VAL A 1 829 ? 83.263 129.251 27.632  1.00 38.87 ? 829  VAL A CB  1 
ATOM   6648 C CG1 . VAL A 1 829 ? 81.801 129.152 27.269  1.00 37.37 ? 829  VAL A CG1 1 
ATOM   6649 C CG2 . VAL A 1 829 ? 83.706 128.048 28.436  1.00 37.87 ? 829  VAL A CG2 1 
ATOM   6650 N N   . LYS A 1 830 ? 83.164 130.581 24.472  1.00 40.20 ? 830  LYS A N   1 
ATOM   6651 C CA  . LYS A 1 830 ? 82.633 131.730 23.774  1.00 41.08 ? 830  LYS A CA  1 
ATOM   6652 C C   . LYS A 1 830 ? 81.130 131.603 23.713  1.00 41.25 ? 830  LYS A C   1 
ATOM   6653 O O   . LYS A 1 830 ? 80.604 130.506 23.545  1.00 39.94 ? 830  LYS A O   1 
ATOM   6654 C CB  . LYS A 1 830 ? 83.181 131.807 22.344  1.00 40.98 ? 830  LYS A CB  1 
ATOM   6655 C CG  . LYS A 1 830 ? 84.664 132.147 22.221  1.00 43.10 ? 830  LYS A CG  1 
ATOM   6656 C CD  . LYS A 1 830 ? 85.061 132.252 20.723  1.00 42.65 ? 830  LYS A CD  1 
ATOM   6657 C CE  . LYS A 1 830 ? 86.573 132.592 20.534  1.00 45.02 ? 830  LYS A CE  1 
ATOM   6658 N NZ  . LYS A 1 830 ? 87.120 132.125 19.185  1.00 46.75 ? 830  LYS A NZ  1 
ATOM   6659 N N   . HIS A 1 831 ? 80.445 132.728 23.824  1.00 41.65 ? 831  HIS A N   1 
ATOM   6660 C CA  . HIS A 1 831 ? 79.002 132.763 23.746  1.00 44.54 ? 831  HIS A CA  1 
ATOM   6661 C C   . HIS A 1 831 ? 78.654 133.661 22.578  1.00 46.43 ? 831  HIS A C   1 
ATOM   6662 O O   . HIS A 1 831 ? 79.148 134.783 22.516  1.00 46.60 ? 831  HIS A O   1 
ATOM   6663 C CB  . HIS A 1 831 ? 78.429 133.295 25.068  1.00 44.38 ? 831  HIS A CB  1 
ATOM   6664 C CG  . HIS A 1 831 ? 76.948 133.489 25.064  1.00 45.51 ? 831  HIS A CG  1 
ATOM   6665 N ND1 . HIS A 1 831 ? 76.329 134.479 25.798  1.00 48.66 ? 831  HIS A ND1 1 
ATOM   6666 C CD2 . HIS A 1 831 ? 75.956 132.822 24.421  1.00 47.36 ? 831  HIS A CD2 1 
ATOM   6667 C CE1 . HIS A 1 831 ? 75.020 134.412 25.609  1.00 49.03 ? 831  HIS A CE1 1 
ATOM   6668 N NE2 . HIS A 1 831 ? 74.770 133.419 24.773  1.00 47.74 ? 831  HIS A NE2 1 
ATOM   6669 N N   . ASN A 1 832 ? 77.825 133.171 21.648  1.00 48.86 ? 832  ASN A N   1 
ATOM   6670 C CA  . ASN A 1 832 ? 77.619 133.822 20.331  1.00 51.37 ? 832  ASN A CA  1 
ATOM   6671 C C   . ASN A 1 832 ? 78.924 134.276 19.673  1.00 52.06 ? 832  ASN A C   1 
ATOM   6672 O O   . ASN A 1 832 ? 78.969 135.331 19.037  1.00 52.51 ? 832  ASN A O   1 
ATOM   6673 C CB  . ASN A 1 832 ? 76.660 135.023 20.408  1.00 51.81 ? 832  ASN A CB  1 
ATOM   6674 C CG  . ASN A 1 832 ? 75.296 134.655 20.950  1.00 54.03 ? 832  ASN A CG  1 
ATOM   6675 O OD1 . ASN A 1 832 ? 74.697 133.648 20.540  1.00 56.26 ? 832  ASN A OD1 1 
ATOM   6676 N ND2 . ASN A 1 832 ? 74.780 135.486 21.869  1.00 55.13 ? 832  ASN A ND2 1 
ATOM   6677 N N   . GLY A 1 833 ? 79.979 133.482 19.840  1.00 53.20 ? 833  GLY A N   1 
ATOM   6678 C CA  . GLY A 1 833 ? 81.295 133.827 19.325  1.00 54.56 ? 833  GLY A CA  1 
ATOM   6679 C C   . GLY A 1 833 ? 82.079 134.887 20.094  1.00 55.47 ? 833  GLY A C   1 
ATOM   6680 O O   . GLY A 1 833 ? 83.150 135.295 19.655  1.00 55.71 ? 833  GLY A O   1 
ATOM   6681 N N   . VAL A 1 834 ? 81.560 135.314 21.244  1.00 56.26 ? 834  VAL A N   1 
ATOM   6682 C CA  . VAL A 1 834 ? 82.211 136.314 22.098  1.00 56.92 ? 834  VAL A CA  1 
ATOM   6683 C C   . VAL A 1 834 ? 82.785 135.629 23.348  1.00 57.91 ? 834  VAL A C   1 
ATOM   6684 O O   . VAL A 1 834 ? 82.051 135.019 24.117  1.00 57.37 ? 834  VAL A O   1 
ATOM   6685 C CB  . VAL A 1 834 ? 81.207 137.448 22.518  1.00 56.74 ? 834  VAL A CB  1 
ATOM   6686 C CG1 . VAL A 1 834 ? 81.891 138.556 23.315  1.00 56.63 ? 834  VAL A CG1 1 
ATOM   6687 C CG2 . VAL A 1 834 ? 80.477 138.026 21.301  1.00 56.58 ? 834  VAL A CG2 1 
ATOM   6688 N N   . PRO A 1 835 ? 84.112 135.708 23.549  1.00 59.25 ? 835  PRO A N   1 
ATOM   6689 C CA  . PRO A 1 835 ? 84.614 135.287 24.865  1.00 60.28 ? 835  PRO A CA  1 
ATOM   6690 C C   . PRO A 1 835 ? 84.385 136.439 25.841  1.00 61.49 ? 835  PRO A C   1 
ATOM   6691 O O   . PRO A 1 835 ? 84.588 137.601 25.434  1.00 62.59 ? 835  PRO A O   1 
ATOM   6692 C CB  . PRO A 1 835 ? 86.117 135.067 24.628  1.00 60.15 ? 835  PRO A CB  1 
ATOM   6693 C CG  . PRO A 1 835 ? 86.463 135.823 23.373  1.00 59.78 ? 835  PRO A CG  1 
ATOM   6694 C CD  . PRO A 1 835 ? 85.182 136.155 22.630  1.00 59.69 ? 835  PRO A CD  1 
ATOM   6695 N N   . SER A 1 836 ? 83.958 136.225 27.093  1.00 62.25 ? 836  SER A N   1 
ATOM   6696 C CA  . SER A 1 836 ? 83.635 134.995 27.821  1.00 62.30 ? 836  SER A CA  1 
ATOM   6697 C C   . SER A 1 836 ? 83.746 135.395 29.297  1.00 62.88 ? 836  SER A C   1 
ATOM   6698 O O   . SER A 1 836 ? 84.859 135.451 29.849  1.00 62.62 ? 836  SER A O   1 
ATOM   6699 C CB  . SER A 1 836 ? 84.626 133.876 27.610  1.00 62.73 ? 836  SER A CB  1 
ATOM   6700 O OG  . SER A 1 836 ? 84.327 132.841 28.539  1.00 62.47 ? 836  SER A OG  1 
ATOM   6701 N N   . THR A 1 838 ? 85.553 134.405 32.916  1.00 55.78 ? 838  THR A N   1 
ATOM   6702 C CA  . THR A 1 838 ? 85.205 132.988 33.102  1.00 55.00 ? 838  THR A CA  1 
ATOM   6703 C C   . THR A 1 838 ? 86.219 132.052 32.448  1.00 53.17 ? 838  THR A C   1 
ATOM   6704 O O   . THR A 1 838 ? 86.400 132.083 31.232  1.00 53.72 ? 838  THR A O   1 
ATOM   6705 C CB  . THR A 1 838 ? 83.799 132.632 32.530  1.00 55.62 ? 838  THR A CB  1 
ATOM   6706 O OG1 . THR A 1 838 ? 83.894 132.424 31.108  1.00 57.46 ? 838  THR A OG1 1 
ATOM   6707 C CG2 . THR A 1 838 ? 82.753 133.735 32.844  1.00 55.81 ? 838  THR A CG2 1 
ATOM   6708 N N   . SER A 1 839 ? 86.875 131.249 33.278  1.00 50.69 ? 839  SER A N   1 
ATOM   6709 C CA  . SER A 1 839 ? 87.697 130.114 32.865  1.00 48.36 ? 839  SER A CA  1 
ATOM   6710 C C   . SER A 1 839 ? 87.245 128.889 33.699  1.00 45.53 ? 839  SER A C   1 
ATOM   6711 O O   . SER A 1 839 ? 87.279 128.940 34.939  1.00 46.05 ? 839  SER A O   1 
ATOM   6712 C CB  . SER A 1 839 ? 89.187 130.398 33.085  1.00 48.75 ? 839  SER A CB  1 
ATOM   6713 O OG  . SER A 1 839 ? 89.974 129.220 32.862  1.00 50.61 ? 839  SER A OG  1 
ATOM   6714 N N   . PRO A 1 840 ? 86.775 127.815 33.031  1.00 42.06 ? 840  PRO A N   1 
ATOM   6715 C CA  . PRO A 1 840 ? 86.283 126.640 33.751  1.00 39.44 ? 840  PRO A CA  1 
ATOM   6716 C C   . PRO A 1 840 ? 87.357 125.788 34.424  1.00 37.08 ? 840  PRO A C   1 
ATOM   6717 O O   . PRO A 1 840 ? 88.510 125.802 34.004  1.00 36.75 ? 840  PRO A O   1 
ATOM   6718 C CB  . PRO A 1 840 ? 85.605 125.812 32.644  1.00 39.36 ? 840  PRO A CB  1 
ATOM   6719 C CG  . PRO A 1 840 ? 86.257 126.234 31.407  1.00 40.56 ? 840  PRO A CG  1 
ATOM   6720 C CD  . PRO A 1 840 ? 86.612 127.672 31.576  1.00 41.68 ? 840  PRO A CD  1 
ATOM   6721 N N   . THR A 1 841 ? 86.940 125.013 35.421  1.00 33.46 ? 841  THR A N   1 
ATOM   6722 C CA  . THR A 1 841 ? 87.786 124.018 36.087  1.00 32.17 ? 841  THR A CA  1 
ATOM   6723 C C   . THR A 1 841 ? 87.819 122.761 35.248  1.00 31.26 ? 841  THR A C   1 
ATOM   6724 O O   . THR A 1 841 ? 86.770 122.299 34.764  1.00 30.64 ? 841  THR A O   1 
ATOM   6725 C CB  . THR A 1 841 ? 87.233 123.712 37.517  1.00 32.23 ? 841  THR A CB  1 
ATOM   6726 O OG1 . THR A 1 841 ? 87.234 124.918 38.278  1.00 34.69 ? 841  THR A OG1 1 
ATOM   6727 C CG2 . THR A 1 841 ? 88.004 122.626 38.280  1.00 31.73 ? 841  THR A CG2 1 
ATOM   6728 N N   . VAL A 1 842 ? 89.010 122.205 35.056  1.00 29.49 ? 842  VAL A N   1 
ATOM   6729 C CA  . VAL A 1 842 ? 89.107 120.951 34.357  1.00 29.22 ? 842  VAL A CA  1 
ATOM   6730 C C   . VAL A 1 842 ? 89.821 119.961 35.228  1.00 29.23 ? 842  VAL A C   1 
ATOM   6731 O O   . VAL A 1 842 ? 90.887 120.264 35.767  1.00 27.87 ? 842  VAL A O   1 
ATOM   6732 C CB  . VAL A 1 842 ? 89.892 121.118 33.028  1.00 29.66 ? 842  VAL A CB  1 
ATOM   6733 C CG1 . VAL A 1 842 ? 90.002 119.780 32.301  1.00 29.71 ? 842  VAL A CG1 1 
ATOM   6734 C CG2 . VAL A 1 842 ? 89.273 122.227 32.199  1.00 29.11 ? 842  VAL A CG2 1 
ATOM   6735 N N   . THR A 1 843 ? 89.216 118.782 35.388  1.00 28.08 ? 843  THR A N   1 
ATOM   6736 C CA  . THR A 1 843 ? 89.844 117.675 36.060  1.00 28.32 ? 843  THR A CA  1 
ATOM   6737 C C   . THR A 1 843 ? 90.200 116.632 34.994  1.00 27.84 ? 843  THR A C   1 
ATOM   6738 O O   . THR A 1 843 ? 89.426 116.373 34.096  1.00 28.16 ? 843  THR A O   1 
ATOM   6739 C CB  . THR A 1 843 ? 88.858 117.094 37.077  1.00 29.07 ? 843  THR A CB  1 
ATOM   6740 O OG1 . THR A 1 843 ? 88.321 118.195 37.835  1.00 32.96 ? 843  THR A OG1 1 
ATOM   6741 C CG2 . THR A 1 843 ? 89.553 116.138 38.021  1.00 28.13 ? 843  THR A CG2 1 
ATOM   6742 N N   . TYR A 1 844 ? 91.377 116.050 35.079  1.00 27.79 ? 844  TYR A N   1 
ATOM   6743 C CA  . TYR A 1 844 ? 91.789 115.070 34.070  1.00 27.44 ? 844  TYR A CA  1 
ATOM   6744 C C   . TYR A 1 844 ? 92.280 113.826 34.753  1.00 27.27 ? 844  TYR A C   1 
ATOM   6745 O O   . TYR A 1 844 ? 92.982 113.905 35.785  1.00 26.08 ? 844  TYR A O   1 
ATOM   6746 C CB  . TYR A 1 844 ? 92.824 115.687 33.097  1.00 27.89 ? 844  TYR A CB  1 
ATOM   6747 C CG  . TYR A 1 844 ? 93.161 114.731 32.003  1.00 28.90 ? 844  TYR A CG  1 
ATOM   6748 C CD1 . TYR A 1 844 ? 92.167 114.323 31.111  1.00 26.67 ? 844  TYR A CD1 1 
ATOM   6749 C CD2 . TYR A 1 844 ? 94.463 114.229 31.856  1.00 27.17 ? 844  TYR A CD2 1 
ATOM   6750 C CE1 . TYR A 1 844 ? 92.430 113.456 30.096  1.00 29.62 ? 844  TYR A CE1 1 
ATOM   6751 C CE2 . TYR A 1 844 ? 94.742 113.315 30.836  1.00 30.56 ? 844  TYR A CE2 1 
ATOM   6752 C CZ  . TYR A 1 844 ? 93.700 112.942 29.968  1.00 28.63 ? 844  TYR A CZ  1 
ATOM   6753 O OH  . TYR A 1 844 ? 93.928 112.059 28.975  1.00 30.13 ? 844  TYR A OH  1 
ATOM   6754 N N   . ASP A 1 845 ? 91.802 112.675 34.269  1.00 26.57 ? 845  ASP A N   1 
ATOM   6755 C CA  . ASP A 1 845 ? 92.251 111.400 34.719  1.00 28.96 ? 845  ASP A CA  1 
ATOM   6756 C C   . ASP A 1 845 ? 93.051 110.833 33.554  1.00 30.65 ? 845  ASP A C   1 
ATOM   6757 O O   . ASP A 1 845 ? 92.490 110.466 32.514  1.00 28.85 ? 845  ASP A O   1 
ATOM   6758 C CB  . ASP A 1 845 ? 91.065 110.482 35.062  1.00 28.83 ? 845  ASP A CB  1 
ATOM   6759 C CG  . ASP A 1 845 ? 91.496 109.131 35.613  1.00 31.47 ? 845  ASP A CG  1 
ATOM   6760 O OD1 . ASP A 1 845 ? 92.511 108.556 35.154  1.00 32.94 ? 845  ASP A OD1 1 
ATOM   6761 O OD2 . ASP A 1 845 ? 90.780 108.590 36.479  1.00 35.36 ? 845  ASP A OD2 1 
ATOM   6762 N N   . SER A 1 846 ? 94.358 110.764 33.733  1.00 32.50 ? 846  SER A N   1 
ATOM   6763 C CA  . SER A 1 846 ? 95.266 110.371 32.637  1.00 35.15 ? 846  SER A CA  1 
ATOM   6764 C C   . SER A 1 846 ? 95.292 108.865 32.409  1.00 35.54 ? 846  SER A C   1 
ATOM   6765 O O   . SER A 1 846 ? 95.582 108.395 31.307  1.00 37.29 ? 846  SER A O   1 
ATOM   6766 C CB  . SER A 1 846 ? 96.672 110.915 32.904  1.00 35.05 ? 846  SER A CB  1 
ATOM   6767 O OG  . SER A 1 846 ? 97.249 110.142 33.938  1.00 39.39 ? 846  SER A OG  1 
ATOM   6768 N N   . ASN A 1 847 ? 94.982 108.102 33.445  1.00 35.71 ? 847  ASN A N   1 
ATOM   6769 C CA  . ASN A 1 847 ? 94.883 106.665 33.328  1.00 36.88 ? 847  ASN A CA  1 
ATOM   6770 C C   . ASN A 1 847 ? 93.671 106.253 32.484  1.00 36.10 ? 847  ASN A C   1 
ATOM   6771 O O   . ASN A 1 847 ? 93.784 105.353 31.667  1.00 36.67 ? 847  ASN A O   1 
ATOM   6772 C CB  . ASN A 1 847 ? 94.869 106.022 34.720  1.00 37.67 ? 847  ASN A CB  1 
ATOM   6773 C CG  . ASN A 1 847 ? 94.766 104.486 34.681  1.00 44.06 ? 847  ASN A CG  1 
ATOM   6774 O OD1 . ASN A 1 847 ? 93.928 103.901 35.389  1.00 48.34 ? 847  ASN A OD1 1 
ATOM   6775 N ND2 . ASN A 1 847 ? 95.653 103.819 33.896  1.00 48.56 ? 847  ASN A ND2 1 
ATOM   6776 N N   . LEU A 1 848 ? 92.536 106.932 32.665  1.00 34.47 ? 848  LEU A N   1 
ATOM   6777 C CA  . LEU A 1 848 ? 91.280 106.584 31.995  1.00 32.88 ? 848  LEU A CA  1 
ATOM   6778 C C   . LEU A 1 848 ? 91.015 107.417 30.757  1.00 31.31 ? 848  LEU A C   1 
ATOM   6779 O O   . LEU A 1 848 ? 90.115 107.093 29.975  1.00 30.94 ? 848  LEU A O   1 
ATOM   6780 C CB  . LEU A 1 848 ? 90.116 106.785 32.955  1.00 33.38 ? 848  LEU A CB  1 
ATOM   6781 C CG  . LEU A 1 848 ? 89.654 105.649 33.871  1.00 33.82 ? 848  LEU A CG  1 
ATOM   6782 C CD1 . LEU A 1 848 ? 90.757 104.784 34.346  1.00 37.20 ? 848  LEU A CD1 1 
ATOM   6783 C CD2 . LEU A 1 848 ? 88.834 106.211 35.032  1.00 33.76 ? 848  LEU A CD2 1 
ATOM   6784 N N   . LYS A 1 849 ? 91.769 108.505 30.604  1.00 28.55 ? 849  LYS A N   1 
ATOM   6785 C CA  . LYS A 1 849 ? 91.621 109.423 29.505  1.00 27.84 ? 849  LYS A CA  1 
ATOM   6786 C C   . LYS A 1 849 ? 90.244 110.139 29.535  1.00 27.08 ? 849  LYS A C   1 
ATOM   6787 O O   . LYS A 1 849 ? 89.585 110.284 28.528  1.00 25.84 ? 849  LYS A O   1 
ATOM   6788 C CB  . LYS A 1 849 ? 91.886 108.698 28.152  1.00 28.79 ? 849  LYS A CB  1 
ATOM   6789 C CG  . LYS A 1 849 ? 93.264 108.043 28.035  1.00 29.35 ? 849  LYS A CG  1 
ATOM   6790 C CD  . LYS A 1 849 ? 94.367 109.083 28.133  1.00 32.68 ? 849  LYS A CD  1 
ATOM   6791 C CE  . LYS A 1 849 ? 95.801 108.570 27.710  1.00 33.39 ? 849  LYS A CE  1 
ATOM   6792 N NZ  . LYS A 1 849 ? 96.847 109.530 28.312  1.00 35.04 ? 849  LYS A NZ  1 
ATOM   6793 N N   . VAL A 1 850 ? 89.849 110.605 30.714  1.00 26.32 ? 850  VAL A N   1 
ATOM   6794 C CA  . VAL A 1 850 ? 88.571 111.292 30.930  1.00 26.30 ? 850  VAL A CA  1 
ATOM   6795 C C   . VAL A 1 850 ? 88.816 112.693 31.463  1.00 25.95 ? 850  VAL A C   1 
ATOM   6796 O O   . VAL A 1 850 ? 89.524 112.857 32.446  1.00 26.15 ? 850  VAL A O   1 
ATOM   6797 C CB  . VAL A 1 850 ? 87.689 110.528 31.962  1.00 25.55 ? 850  VAL A CB  1 
ATOM   6798 C CG1 . VAL A 1 850 ? 86.381 111.288 32.216  1.00 26.66 ? 850  VAL A CG1 1 
ATOM   6799 C CG2 . VAL A 1 850 ? 87.402 109.084 31.483  1.00 25.87 ? 850  VAL A CG2 1 
ATOM   6800 N N   . ALA A 1 851 ? 88.284 113.694 30.785  1.00 25.77 ? 851  ALA A N   1 
ATOM   6801 C CA  . ALA A 1 851 ? 88.326 115.072 31.252  1.00 27.10 ? 851  ALA A CA  1 
ATOM   6802 C C   . ALA A 1 851 ? 86.958 115.477 31.697  1.00 27.37 ? 851  ALA A C   1 
ATOM   6803 O O   . ALA A 1 851 ? 85.973 115.181 31.002  1.00 28.98 ? 851  ALA A O   1 
ATOM   6804 C CB  . ALA A 1 851 ? 88.790 116.004 30.151  1.00 26.27 ? 851  ALA A CB  1 
ATOM   6805 N N   . ILE A 1 852 ? 86.870 116.170 32.830  1.00 27.24 ? 852  ILE A N   1 
ATOM   6806 C CA  . ILE A 1 852 ? 85.579 116.738 33.268  1.00 28.69 ? 852  ILE A CA  1 
ATOM   6807 C C   . ILE A 1 852 ? 85.695 118.226 33.402  1.00 28.74 ? 852  ILE A C   1 
ATOM   6808 O O   . ILE A 1 852 ? 86.547 118.710 34.126  1.00 28.80 ? 852  ILE A O   1 
ATOM   6809 C CB  . ILE A 1 852 ? 85.052 116.115 34.614  1.00 28.70 ? 852  ILE A CB  1 
ATOM   6810 C CG1 . ILE A 1 852 ? 84.855 114.613 34.442  1.00 29.14 ? 852  ILE A CG1 1 
ATOM   6811 C CG2 . ILE A 1 852 ? 83.777 116.807 35.046  1.00 29.64 ? 852  ILE A CG2 1 
ATOM   6812 C CD1 . ILE A 1 852 ? 84.357 113.848 35.673  1.00 30.68 ? 852  ILE A CD1 1 
ATOM   6813 N N   . ILE A 1 853 ? 84.844 118.952 32.705  1.00 29.31 ? 853  ILE A N   1 
ATOM   6814 C CA  . ILE A 1 853 ? 84.852 120.396 32.744  1.00 30.90 ? 853  ILE A CA  1 
ATOM   6815 C C   . ILE A 1 853 ? 83.695 120.867 33.615  1.00 32.56 ? 853  ILE A C   1 
ATOM   6816 O O   . ILE A 1 853 ? 82.532 120.518 33.387  1.00 30.38 ? 853  ILE A O   1 
ATOM   6817 C CB  . ILE A 1 853 ? 84.724 121.018 31.353  1.00 30.65 ? 853  ILE A CB  1 
ATOM   6818 C CG1 . ILE A 1 853 ? 85.778 120.424 30.382  1.00 32.48 ? 853  ILE A CG1 1 
ATOM   6819 C CG2 . ILE A 1 853 ? 84.764 122.536 31.439  1.00 32.36 ? 853  ILE A CG2 1 
ATOM   6820 C CD1 . ILE A 1 853 ? 85.608 120.924 28.929  1.00 29.68 ? 853  ILE A CD1 1 
ATOM   6821 N N   . THR A 1 854 ? 84.036 121.691 34.599  1.00 33.38 ? 854  THR A N   1 
ATOM   6822 C CA  . THR A 1 854 ? 83.106 122.075 35.640  1.00 36.20 ? 854  THR A CA  1 
ATOM   6823 C C   . THR A 1 854 ? 83.276 123.598 35.894  1.00 36.77 ? 854  THR A C   1 
ATOM   6824 O O   . THR A 1 854 ? 84.046 124.223 35.171  1.00 36.10 ? 854  THR A O   1 
ATOM   6825 C CB  . THR A 1 854 ? 83.382 121.082 36.781  1.00 36.55 ? 854  THR A CB  1 
ATOM   6826 O OG1 . THR A 1 854 ? 82.182 120.693 37.461  1.00 41.33 ? 854  THR A OG1 1 
ATOM   6827 C CG2 . THR A 1 854 ? 84.571 121.436 37.663  1.00 32.86 ? 854  THR A CG2 1 
ATOM   6828 N N   . ASP A 1 855 ? 82.534 124.231 36.824  1.00 38.39 ? 855  ASP A N   1 
ATOM   6829 C CA  . ASP A 1 855 ? 82.728 125.693 37.064  1.00 39.24 ? 855  ASP A CA  1 
ATOM   6830 C C   . ASP A 1 855 ? 82.329 126.388 35.753  1.00 39.30 ? 855  ASP A C   1 
ATOM   6831 O O   . ASP A 1 855 ? 82.947 127.362 35.317  1.00 38.35 ? 855  ASP A O   1 
ATOM   6832 C CB  . ASP A 1 855 ? 84.220 125.957 37.438  1.00 39.94 ? 855  ASP A CB  1 
ATOM   6833 C CG  . ASP A 1 855 ? 84.480 127.332 38.061  1.00 45.54 ? 855  ASP A CG  1 
ATOM   6834 O OD1 . ASP A 1 855 ? 83.528 127.945 38.589  1.00 49.03 ? 855  ASP A OD1 1 
ATOM   6835 O OD2 . ASP A 1 855 ? 85.676 127.783 38.036  1.00 49.77 ? 855  ASP A OD2 1 
ATOM   6836 N N   . ILE A 1 856 ? 81.303 125.837 35.099  1.00 38.38 ? 856  ILE A N   1 
ATOM   6837 C CA  . ILE A 1 856 ? 80.877 126.311 33.794  1.00 38.32 ? 856  ILE A CA  1 
ATOM   6838 C C   . ILE A 1 856 ? 79.354 126.499 33.840  1.00 38.56 ? 856  ILE A C   1 
ATOM   6839 O O   . ILE A 1 856 ? 78.680 125.912 34.699  1.00 38.41 ? 856  ILE A O   1 
ATOM   6840 C CB  . ILE A 1 856 ? 81.345 125.325 32.655  1.00 38.81 ? 856  ILE A CB  1 
ATOM   6841 C CG1 . ILE A 1 856 ? 81.353 125.997 31.286  1.00 37.74 ? 856  ILE A CG1 1 
ATOM   6842 C CG2 . ILE A 1 856 ? 80.516 124.006 32.630  1.00 37.07 ? 856  ILE A CG2 1 
ATOM   6843 C CD1 . ILE A 1 856 ? 82.195 125.191 30.222  1.00 39.68 ? 856  ILE A CD1 1 
ATOM   6844 N N   . ASP A 1 857 ? 78.817 127.325 32.952  1.00 38.59 ? 857  ASP A N   1 
ATOM   6845 C CA  . ASP A 1 857 ? 77.380 127.579 32.933  1.00 39.60 ? 857  ASP A CA  1 
ATOM   6846 C C   . ASP A 1 857 ? 76.821 127.919 31.563  1.00 38.19 ? 857  ASP A C   1 
ATOM   6847 O O   . ASP A 1 857 ? 76.568 129.093 31.246  1.00 38.53 ? 857  ASP A O   1 
ATOM   6848 C CB  . ASP A 1 857 ? 77.002 128.683 33.920  1.00 41.04 ? 857  ASP A CB  1 
ATOM   6849 C CG  . ASP A 1 857 ? 75.648 128.438 34.545  1.00 46.46 ? 857  ASP A CG  1 
ATOM   6850 O OD1 . ASP A 1 857 ? 75.449 127.343 35.130  1.00 53.89 ? 857  ASP A OD1 1 
ATOM   6851 O OD2 . ASP A 1 857 ? 74.774 129.328 34.458  1.00 54.91 ? 857  ASP A OD2 1 
ATOM   6852 N N   . LEU A 1 858 ? 76.598 126.890 30.752  1.00 35.90 ? 858  LEU A N   1 
ATOM   6853 C CA  . LEU A 1 858 ? 76.087 127.105 29.421  1.00 33.50 ? 858  LEU A CA  1 
ATOM   6854 C C   . LEU A 1 858 ? 74.569 127.073 29.410  1.00 31.98 ? 858  LEU A C   1 
ATOM   6855 O O   . LEU A 1 858 ? 73.958 126.012 29.485  1.00 30.89 ? 858  LEU A O   1 
ATOM   6856 C CB  . LEU A 1 858 ? 76.653 126.074 28.443  1.00 33.77 ? 858  LEU A CB  1 
ATOM   6857 C CG  . LEU A 1 858 ? 78.144 125.784 28.459  1.00 34.32 ? 858  LEU A CG  1 
ATOM   6858 C CD1 . LEU A 1 858 ? 78.448 124.782 27.365  1.00 34.83 ? 858  LEU A CD1 1 
ATOM   6859 C CD2 . LEU A 1 858 ? 78.912 127.078 28.254  1.00 35.31 ? 858  LEU A CD2 1 
ATOM   6860 N N   . LEU A 1 859 ? 73.964 128.234 29.256  1.00 31.08 ? 859  LEU A N   1 
ATOM   6861 C CA  . LEU A 1 859 ? 72.520 128.341 29.339  1.00 31.37 ? 859  LEU A CA  1 
ATOM   6862 C C   . LEU A 1 859 ? 71.856 127.501 28.289  1.00 30.55 ? 859  LEU A C   1 
ATOM   6863 O O   . LEU A 1 859 ? 72.252 127.534 27.139  1.00 30.18 ? 859  LEU A O   1 
ATOM   6864 C CB  . LEU A 1 859 ? 72.077 129.791 29.176  1.00 32.21 ? 859  LEU A CB  1 
ATOM   6865 C CG  . LEU A 1 859 ? 72.532 130.701 30.328  1.00 33.67 ? 859  LEU A CG  1 
ATOM   6866 C CD1 . LEU A 1 859 ? 72.080 132.102 30.046  1.00 36.30 ? 859  LEU A CD1 1 
ATOM   6867 C CD2 . LEU A 1 859 ? 71.971 130.169 31.657  1.00 33.19 ? 859  LEU A CD2 1 
ATOM   6868 N N   . LEU A 1 860 ? 70.813 126.773 28.676  1.00 31.06 ? 860  LEU A N   1 
ATOM   6869 C CA  . LEU A 1 860 ? 70.036 126.048 27.711  1.00 30.56 ? 860  LEU A CA  1 
ATOM   6870 C C   . LEU A 1 860 ? 69.364 126.976 26.687  1.00 31.43 ? 860  LEU A C   1 
ATOM   6871 O O   . LEU A 1 860 ? 68.660 127.923 27.045  1.00 30.94 ? 860  LEU A O   1 
ATOM   6872 C CB  . LEU A 1 860 ? 68.999 125.197 28.430  1.00 30.82 ? 860  LEU A CB  1 
ATOM   6873 C CG  . LEU A 1 860 ? 68.167 124.282 27.577  1.00 30.04 ? 860  LEU A CG  1 
ATOM   6874 C CD1 . LEU A 1 860 ? 69.053 123.154 27.094  1.00 31.36 ? 860  LEU A CD1 1 
ATOM   6875 C CD2 . LEU A 1 860 ? 67.020 123.713 28.408  1.00 29.88 ? 860  LEU A CD2 1 
ATOM   6876 N N   . GLY A 1 861 ? 69.557 126.674 25.403  1.00 30.28 ? 861  GLY A N   1 
ATOM   6877 C CA  . GLY A 1 861 ? 68.968 127.487 24.358  1.00 31.21 ? 861  GLY A CA  1 
ATOM   6878 C C   . GLY A 1 861 ? 69.897 128.561 23.786  1.00 31.39 ? 861  GLY A C   1 
ATOM   6879 O O   . GLY A 1 861 ? 69.470 129.338 22.913  1.00 32.68 ? 861  GLY A O   1 
ATOM   6880 N N   . GLU A 1 862 ? 71.146 128.604 24.244  1.00 31.36 ? 862  GLU A N   1 
ATOM   6881 C CA  . GLU A 1 862 ? 72.113 129.598 23.758  1.00 32.22 ? 862  GLU A CA  1 
ATOM   6882 C C   . GLU A 1 862 ? 73.240 128.900 23.033  1.00 32.46 ? 862  GLU A C   1 
ATOM   6883 O O   . GLU A 1 862 ? 73.611 127.786 23.404  1.00 31.18 ? 862  GLU A O   1 
ATOM   6884 C CB  . GLU A 1 862 ? 72.719 130.358 24.936  1.00 34.06 ? 862  GLU A CB  1 
ATOM   6885 C CG  . GLU A 1 862 ? 71.755 131.231 25.688  1.00 37.13 ? 862  GLU A CG  1 
ATOM   6886 C CD  . GLU A 1 862 ? 71.272 132.362 24.845  1.00 42.77 ? 862  GLU A CD  1 
ATOM   6887 O OE1 . GLU A 1 862 ? 72.119 133.168 24.391  1.00 46.09 ? 862  GLU A OE1 1 
ATOM   6888 O OE2 . GLU A 1 862 ? 70.046 132.439 24.623  1.00 48.52 ? 862  GLU A OE2 1 
ATOM   6889 N N   . ALA A 1 863 ? 73.834 129.578 22.043  1.00 32.42 ? 863  ALA A N   1 
ATOM   6890 C CA  . ALA A 1 863 ? 74.920 129.016 21.255  1.00 32.33 ? 863  ALA A CA  1 
ATOM   6891 C C   . ALA A 1 863 ? 76.272 129.305 21.882  1.00 32.63 ? 863  ALA A C   1 
ATOM   6892 O O   . ALA A 1 863 ? 76.586 130.469 22.213  1.00 33.37 ? 863  ALA A O   1 
ATOM   6893 C CB  . ALA A 1 863 ? 74.866 129.568 19.837  1.00 32.71 ? 863  ALA A CB  1 
ATOM   6894 N N   . TYR A 1 864 ? 77.074 128.253 22.057  1.00 31.48 ? 864  TYR A N   1 
ATOM   6895 C CA  . TYR A 1 864 ? 78.383 128.372 22.687  1.00 30.41 ? 864  TYR A CA  1 
ATOM   6896 C C   . TYR A 1 864 ? 79.393 127.589 21.864  1.00 30.98 ? 864  TYR A C   1 
ATOM   6897 O O   . TYR A 1 864 ? 79.015 126.657 21.106  1.00 29.44 ? 864  TYR A O   1 
ATOM   6898 C CB  . TYR A 1 864 ? 78.421 127.829 24.111  1.00 30.03 ? 864  TYR A CB  1 
ATOM   6899 C CG  . TYR A 1 864 ? 77.572 128.549 25.111  1.00 31.85 ? 864  TYR A CG  1 
ATOM   6900 C CD1 . TYR A 1 864 ? 78.062 129.648 25.816  1.00 31.29 ? 864  TYR A CD1 1 
ATOM   6901 C CD2 . TYR A 1 864 ? 76.269 128.112 25.377  1.00 30.31 ? 864  TYR A CD2 1 
ATOM   6902 C CE1 . TYR A 1 864 ? 77.254 130.316 26.769  1.00 32.09 ? 864  TYR A CE1 1 
ATOM   6903 C CE2 . TYR A 1 864 ? 75.461 128.772 26.310  1.00 31.26 ? 864  TYR A CE2 1 
ATOM   6904 C CZ  . TYR A 1 864 ? 75.965 129.841 27.020  1.00 32.36 ? 864  TYR A CZ  1 
ATOM   6905 O OH  . TYR A 1 864 ? 75.148 130.482 27.920  1.00 33.06 ? 864  TYR A OH  1 
ATOM   6906 N N   . THR A 1 865 ? 80.658 128.000 22.004  1.00 29.69 ? 865  THR A N   1 
ATOM   6907 C CA  . THR A 1 865 ? 81.790 127.257 21.486  1.00 30.70 ? 865  THR A CA  1 
ATOM   6908 C C   . THR A 1 865 ? 82.636 127.013 22.686  1.00 29.52 ? 865  THR A C   1 
ATOM   6909 O O   . THR A 1 865 ? 82.838 127.914 23.468  1.00 31.26 ? 865  THR A O   1 
ATOM   6910 C CB  . THR A 1 865 ? 82.549 128.031 20.355  1.00 31.12 ? 865  THR A CB  1 
ATOM   6911 O OG1 . THR A 1 865 ? 81.624 128.340 19.307  1.00 33.47 ? 865  THR A OG1 1 
ATOM   6912 C CG2 . THR A 1 865 ? 83.592 127.145 19.736  1.00 31.28 ? 865  THR A CG2 1 
ATOM   6913 N N   . VAL A 1 866 ? 83.083 125.797 22.880  1.00 30.38 ? 866  VAL A N   1 
ATOM   6914 C CA  . VAL A 1 866 ? 84.070 125.491 23.920  1.00 31.75 ? 866  VAL A CA  1 
ATOM   6915 C C   . VAL A 1 866 ? 85.244 124.918 23.177  1.00 33.58 ? 866  VAL A C   1 
ATOM   6916 O O   . VAL A 1 866 ? 85.052 124.065 22.300  1.00 33.43 ? 866  VAL A O   1 
ATOM   6917 C CB  . VAL A 1 866 ? 83.535 124.498 24.972  1.00 31.41 ? 866  VAL A CB  1 
ATOM   6918 C CG1 . VAL A 1 866 ? 84.631 124.076 25.967  1.00 32.99 ? 866  VAL A CG1 1 
ATOM   6919 C CG2 . VAL A 1 866 ? 82.369 125.096 25.702  1.00 30.66 ? 866  VAL A CG2 1 
ATOM   6920 N N   . GLU A 1 867 ? 86.454 125.398 23.508  1.00 34.67 ? 867  GLU A N   1 
ATOM   6921 C CA  . GLU A 1 867 ? 87.654 125.086 22.765  1.00 35.84 ? 867  GLU A CA  1 
ATOM   6922 C C   . GLU A 1 867 ? 88.765 124.786 23.727  1.00 35.39 ? 867  GLU A C   1 
ATOM   6923 O O   . GLU A 1 867 ? 88.808 125.326 24.812  1.00 35.45 ? 867  GLU A O   1 
ATOM   6924 C CB  . GLU A 1 867 ? 88.069 126.262 21.874  1.00 36.87 ? 867  GLU A CB  1 
ATOM   6925 C CG  . GLU A 1 867 ? 87.090 126.539 20.759  1.00 41.74 ? 867  GLU A CG  1 
ATOM   6926 C CD  . GLU A 1 867 ? 87.373 127.850 20.040  1.00 49.43 ? 867  GLU A CD  1 
ATOM   6927 O OE1 . GLU A 1 867 ? 87.177 128.929 20.657  1.00 51.77 ? 867  GLU A OE1 1 
ATOM   6928 O OE2 . GLU A 1 867 ? 87.781 127.786 18.855  1.00 50.76 ? 867  GLU A OE2 1 
ATOM   6929 N N   . TRP A 1 868 ? 89.626 123.864 23.343  1.00 35.46 ? 868  TRP A N   1 
ATOM   6930 C CA  . TRP A 1 868 ? 90.763 123.492 24.159  1.00 36.44 ? 868  TRP A CA  1 
ATOM   6931 C C   . TRP A 1 868 ? 91.949 123.201 23.255  1.00 38.09 ? 868  TRP A C   1 
ATOM   6932 O O   . TRP A 1 868 ? 91.804 122.964 22.055  1.00 37.50 ? 868  TRP A O   1 
ATOM   6933 C CB  . TRP A 1 868 ? 90.465 122.275 25.020  1.00 34.63 ? 868  TRP A CB  1 
ATOM   6934 C CG  . TRP A 1 868 ? 89.900 121.121 24.279  1.00 35.96 ? 868  TRP A CG  1 
ATOM   6935 C CD1 . TRP A 1 868 ? 90.571 120.045 23.775  1.00 33.64 ? 868  TRP A CD1 1 
ATOM   6936 C CD2 . TRP A 1 868 ? 88.509 120.906 23.980  1.00 34.21 ? 868  TRP A CD2 1 
ATOM   6937 N NE1 . TRP A 1 868 ? 89.690 119.181 23.189  1.00 36.39 ? 868  TRP A NE1 1 
ATOM   6938 C CE2 . TRP A 1 868 ? 88.420 119.697 23.278  1.00 35.94 ? 868  TRP A CE2 1 
ATOM   6939 C CE3 . TRP A 1 868 ? 87.333 121.644 24.233  1.00 35.62 ? 868  TRP A CE3 1 
ATOM   6940 C CZ2 . TRP A 1 868 ? 87.187 119.166 22.838  1.00 35.54 ? 868  TRP A CZ2 1 
ATOM   6941 C CZ3 . TRP A 1 868 ? 86.142 121.146 23.799  1.00 34.95 ? 868  TRP A CZ3 1 
ATOM   6942 C CH2 . TRP A 1 868 ? 86.072 119.910 23.083  1.00 35.29 ? 868  TRP A CH2 1 
ATOM   6943 N N   . ALA A 1 869 ? 93.126 123.198 23.852  1.00 40.56 ? 869  ALA A N   1 
ATOM   6944 C CA  . ALA A 1 869 ? 94.294 122.758 23.151  1.00 42.88 ? 869  ALA A CA  1 
ATOM   6945 C C   . ALA A 1 869 ? 94.744 121.427 23.736  1.00 44.37 ? 869  ALA A C   1 
ATOM   6946 O O   . ALA A 1 869 ? 94.262 120.998 24.808  1.00 44.27 ? 869  ALA A O   1 
ATOM   6947 C CB  . ALA A 1 869 ? 95.387 123.823 23.251  1.00 43.18 ? 869  ALA A CB  1 
ATOM   6948 N N   . HIS A 1 870 ? 95.634 120.765 22.996  1.00 46.21 ? 870  HIS A N   1 
ATOM   6949 C CA  . HIS A 1 870 ? 96.389 119.597 23.440  1.00 48.53 ? 870  HIS A CA  1 
ATOM   6950 C C   . HIS A 1 870 ? 97.878 119.883 23.222  1.00 49.49 ? 870  HIS A C   1 
ATOM   6951 O O   . HIS A 1 870 ? 98.503 120.600 24.000  1.00 51.57 ? 870  HIS A O   1 
ATOM   6952 C CB  . HIS A 1 870 ? 96.030 118.355 22.617  1.00 49.26 ? 870  HIS A CB  1 
ATOM   6953 C CG  . HIS A 1 870 ? 94.603 117.928 22.736  1.00 49.75 ? 870  HIS A CG  1 
ATOM   6954 N ND1 . HIS A 1 870 ? 94.083 117.371 23.886  1.00 49.73 ? 870  HIS A ND1 1 
ATOM   6955 C CD2 . HIS A 1 870 ? 93.593 117.943 21.833  1.00 50.54 ? 870  HIS A CD2 1 
ATOM   6956 C CE1 . HIS A 1 870 ? 92.812 117.072 23.691  1.00 49.78 ? 870  HIS A CE1 1 
ATOM   6957 N NE2 . HIS A 1 870 ? 92.488 117.414 22.455  1.00 51.42 ? 870  HIS A NE2 1 
HETATM 6958 C C1  . NAG B 2 .   ? 65.048 116.893 44.869  1.00 30.55 ? 2001 NAG A C1  1 
HETATM 6959 C C2  . NAG B 2 .   ? 66.035 118.027 45.192  1.00 31.75 ? 2001 NAG A C2  1 
HETATM 6960 C C3  . NAG B 2 .   ? 65.743 118.606 46.580  1.00 33.67 ? 2001 NAG A C3  1 
HETATM 6961 C C4  . NAG B 2 .   ? 64.353 119.200 46.652  1.00 37.25 ? 2001 NAG A C4  1 
HETATM 6962 C C5  . NAG B 2 .   ? 63.305 118.427 45.791  1.00 39.90 ? 2001 NAG A C5  1 
HETATM 6963 C C6  . NAG B 2 .   ? 61.883 118.395 46.405  1.00 42.15 ? 2001 NAG A C6  1 
HETATM 6964 C C7  . NAG B 2 .   ? 68.171 117.434 44.046  1.00 30.72 ? 2001 NAG A C7  1 
HETATM 6965 C C8  . NAG B 2 .   ? 69.438 116.615 44.151  1.00 27.35 ? 2001 NAG A C8  1 
HETATM 6966 N N2  . NAG B 2 .   ? 67.420 117.575 45.157  1.00 28.67 ? 2001 NAG A N2  1 
HETATM 6967 O O3  . NAG B 2 .   ? 66.637 119.683 46.742  1.00 31.00 ? 2001 NAG A O3  1 
HETATM 6968 O O4  . NAG B 2 .   ? 63.977 119.361 48.014  1.00 44.75 ? 2001 NAG A O4  1 
HETATM 6969 O O5  . NAG B 2 .   ? 63.716 117.166 45.256  1.00 34.63 ? 2001 NAG A O5  1 
HETATM 6970 O O6  . NAG B 2 .   ? 61.320 117.071 46.510  1.00 47.20 ? 2001 NAG A O6  1 
HETATM 6971 O O7  . NAG B 2 .   ? 67.882 117.936 42.963  1.00 32.21 ? 2001 NAG A O7  1 
HETATM 6972 C C1  . NAG C 2 .   ? 63.949 120.772 48.368  1.00 49.85 ? 2002 NAG A C1  1 
HETATM 6973 C C2  . NAG C 2 .   ? 63.267 120.935 49.738  1.00 53.05 ? 2002 NAG A C2  1 
HETATM 6974 C C3  . NAG C 2 .   ? 63.166 122.415 50.081  1.00 54.16 ? 2002 NAG A C3  1 
HETATM 6975 C C4  . NAG C 2 .   ? 64.568 123.023 50.171  1.00 55.52 ? 2002 NAG A C4  1 
HETATM 6976 C C5  . NAG C 2 .   ? 65.494 122.633 49.004  1.00 54.01 ? 2002 NAG A C5  1 
HETATM 6977 C C6  . NAG C 2 .   ? 66.897 122.563 49.593  1.00 54.50 ? 2002 NAG A C6  1 
HETATM 6978 C C7  . NAG C 2 .   ? 61.650 119.113 50.264  1.00 54.16 ? 2002 NAG A C7  1 
HETATM 6979 C C8  . NAG C 2 .   ? 62.682 118.179 50.832  1.00 54.39 ? 2002 NAG A C8  1 
HETATM 6980 N N2  . NAG C 2 .   ? 61.946 120.321 49.785  1.00 52.81 ? 2002 NAG A N2  1 
HETATM 6981 O O3  . NAG C 2 .   ? 62.514 122.554 51.323  1.00 54.76 ? 2002 NAG A O3  1 
HETATM 6982 O O4  . NAG C 2 .   ? 64.501 124.445 50.291  1.00 56.86 ? 2002 NAG A O4  1 
HETATM 6983 O O5  . NAG C 2 .   ? 65.233 121.386 48.347  1.00 50.88 ? 2002 NAG A O5  1 
HETATM 6984 O O6  . NAG C 2 .   ? 67.842 122.960 48.624  1.00 56.85 ? 2002 NAG A O6  1 
HETATM 6985 O O7  . NAG C 2 .   ? 60.494 118.727 50.242  1.00 58.23 ? 2002 NAG A O7  1 
HETATM 6986 C C1  . NAG D 2 .   ? 22.357 98.536  19.130  1.00 37.08 ? 2003 NAG A C1  1 
HETATM 6987 C C2  . NAG D 2 .   ? 22.525 99.342  17.840  1.00 38.54 ? 2003 NAG A C2  1 
HETATM 6988 C C3  . NAG D 2 .   ? 21.990 100.770 17.984  1.00 39.42 ? 2003 NAG A C3  1 
HETATM 6989 C C4  . NAG D 2 .   ? 20.528 100.742 18.490  1.00 41.91 ? 2003 NAG A C4  1 
HETATM 6990 C C5  . NAG D 2 .   ? 20.462 99.821  19.711  1.00 41.55 ? 2003 NAG A C5  1 
HETATM 6991 C C6  . NAG D 2 .   ? 19.041 99.606  20.217  1.00 43.40 ? 2003 NAG A C6  1 
HETATM 6992 C C7  . NAG D 2 .   ? 24.314 98.759  16.286  1.00 39.36 ? 2003 NAG A C7  1 
HETATM 6993 C C8  . NAG D 2 .   ? 25.762 98.929  15.894  1.00 40.41 ? 2003 NAG A C8  1 
HETATM 6994 N N2  . NAG D 2 .   ? 23.908 99.357  17.401  1.00 39.19 ? 2003 NAG A N2  1 
HETATM 6995 O O3  . NAG D 2 .   ? 22.123 101.389 16.711  1.00 38.03 ? 2003 NAG A O3  1 
HETATM 6996 O O4  . NAG D 2 .   ? 20.059 101.998 18.944  1.00 44.38 ? 2003 NAG A O4  1 
HETATM 6997 O O5  . NAG D 2 .   ? 20.970 98.547  19.395  1.00 40.03 ? 2003 NAG A O5  1 
HETATM 6998 O O6  . NAG D 2 .   ? 19.080 99.128  21.553  1.00 45.54 ? 2003 NAG A O6  1 
HETATM 6999 O O7  . NAG D 2 .   ? 23.575 98.088  15.576  1.00 42.12 ? 2003 NAG A O7  1 
HETATM 7000 C C1  . NAG E 2 .   ? 19.683 102.938 17.927  1.00 50.54 ? 2004 NAG A C1  1 
HETATM 7001 C C2  . NAG E 2 .   ? 18.172 103.249 17.930  1.00 53.62 ? 2004 NAG A C2  1 
HETATM 7002 C C3  . NAG E 2 .   ? 17.969 104.263 16.797  1.00 55.76 ? 2004 NAG A C3  1 
HETATM 7003 C C4  . NAG E 2 .   ? 18.792 105.522 17.084  1.00 54.77 ? 2004 NAG A C4  1 
HETATM 7004 C C5  . NAG E 2 .   ? 20.263 105.095 17.056  1.00 54.84 ? 2004 NAG A C5  1 
HETATM 7005 C C6  . NAG E 2 .   ? 21.229 106.254 17.267  1.00 56.05 ? 2004 NAG A C6  1 
HETATM 7006 C C7  . NAG E 2 .   ? 16.464 101.549 18.673  1.00 57.52 ? 2004 NAG A C7  1 
HETATM 7007 C C8  . NAG E 2 .   ? 15.718 100.306 18.265  1.00 57.98 ? 2004 NAG A C8  1 
HETATM 7008 N N2  . NAG E 2 .   ? 17.319 102.068 17.758  1.00 54.99 ? 2004 NAG A N2  1 
HETATM 7009 O O3  . NAG E 2 .   ? 16.615 104.591 16.633  1.00 57.99 ? 2004 NAG A O3  1 
HETATM 7010 O O4  . NAG E 2 .   ? 18.491 106.581 16.193  1.00 55.73 ? 2004 NAG A O4  1 
HETATM 7011 O O5  . NAG E 2 .   ? 20.435 104.142 18.093  1.00 52.54 ? 2004 NAG A O5  1 
HETATM 7012 O O6  . NAG E 2 .   ? 20.958 106.828 18.529  1.00 58.24 ? 2004 NAG A O6  1 
HETATM 7013 O O7  . NAG E 2 .   ? 16.243 102.004 19.802  1.00 58.03 ? 2004 NAG A O7  1 
HETATM 7014 C C1  . NAG F 2 .   ? 51.790 76.222  27.527  1.00 49.82 ? 2005 NAG A C1  1 
HETATM 7015 C C2  . NAG F 2 .   ? 52.944 76.271  28.538  1.00 53.57 ? 2005 NAG A C2  1 
HETATM 7016 C C3  . NAG F 2 .   ? 52.693 75.290  29.699  1.00 56.10 ? 2005 NAG A C3  1 
HETATM 7017 C C4  . NAG F 2 .   ? 51.290 75.456  30.290  1.00 57.88 ? 2005 NAG A C4  1 
HETATM 7018 C C5  . NAG F 2 .   ? 50.337 75.238  29.115  1.00 58.15 ? 2005 NAG A C5  1 
HETATM 7019 C C6  . NAG F 2 .   ? 48.841 75.185  29.409  1.00 60.73 ? 2005 NAG A C6  1 
HETATM 7020 C C7  . NAG F 2 .   ? 55.315 76.714  27.854  1.00 53.61 ? 2005 NAG A C7  1 
HETATM 7021 C C8  . NAG F 2 .   ? 56.411 76.166  26.992  1.00 53.44 ? 2005 NAG A C8  1 
HETATM 7022 N N2  . NAG F 2 .   ? 54.196 75.971  27.855  1.00 52.03 ? 2005 NAG A N2  1 
HETATM 7023 O O3  . NAG F 2 .   ? 53.670 75.429  30.706  1.00 56.30 ? 2005 NAG A O3  1 
HETATM 7024 O O4  . NAG F 2 .   ? 51.094 74.517  31.338  1.00 59.95 ? 2005 NAG A O4  1 
HETATM 7025 O O5  . NAG F 2 .   ? 50.556 76.287  28.200  1.00 53.98 ? 2005 NAG A O5  1 
HETATM 7026 O O6  . NAG F 2 .   ? 48.220 74.727  28.210  1.00 63.52 ? 2005 NAG A O6  1 
HETATM 7027 O O7  . NAG F 2 .   ? 55.503 77.767  28.490  1.00 54.10 ? 2005 NAG A O7  1 
HETATM 7028 C C1  . GOL G 3 .   ? 47.970 107.164 2.940   1.00 31.15 ? 3001 GOL A C1  1 
HETATM 7029 O O1  . GOL G 3 .   ? 47.808 107.523 4.313   1.00 31.19 ? 3001 GOL A O1  1 
HETATM 7030 C C2  . GOL G 3 .   ? 47.540 108.313 2.031   1.00 33.14 ? 3001 GOL A C2  1 
HETATM 7031 O O2  . GOL G 3 .   ? 48.169 109.520 2.415   1.00 35.55 ? 3001 GOL A O2  1 
HETATM 7032 C C3  . GOL G 3 .   ? 47.918 108.014 0.588   1.00 34.07 ? 3001 GOL A C3  1 
HETATM 7033 O O3  . GOL G 3 .   ? 49.329 107.880 0.507   1.00 32.16 ? 3001 GOL A O3  1 
HETATM 7034 C C1  . GOL H 3 .   ? 50.687 107.387 25.218  1.00 42.32 ? 3002 GOL A C1  1 
HETATM 7035 O O1  . GOL H 3 .   ? 50.046 108.181 26.209  1.00 36.18 ? 3002 GOL A O1  1 
HETATM 7036 C C2  . GOL H 3 .   ? 52.190 107.670 25.102  1.00 42.68 ? 3002 GOL A C2  1 
HETATM 7037 O O2  . GOL H 3 .   ? 52.713 107.740 26.400  1.00 43.90 ? 3002 GOL A O2  1 
HETATM 7038 C C3  . GOL H 3 .   ? 52.998 106.620 24.340  1.00 39.88 ? 3002 GOL A C3  1 
HETATM 7039 O O3  . GOL H 3 .   ? 54.189 107.191 23.741  1.00 40.30 ? 3002 GOL A O3  1 
HETATM 7040 C C1  . GOL I 3 .   ? 52.365 95.822  53.227  1.00 48.53 ? 3003 GOL A C1  1 
HETATM 7041 O O1  . GOL I 3 .   ? 53.714 95.450  53.439  1.00 49.02 ? 3003 GOL A O1  1 
HETATM 7042 C C2  . GOL I 3 .   ? 51.996 95.435  51.809  1.00 47.16 ? 3003 GOL A C2  1 
HETATM 7043 O O2  . GOL I 3 .   ? 52.160 94.040  51.698  1.00 49.70 ? 3003 GOL A O2  1 
HETATM 7044 C C3  . GOL I 3 .   ? 50.546 95.780  51.521  1.00 48.55 ? 3003 GOL A C3  1 
HETATM 7045 O O3  . GOL I 3 .   ? 50.214 95.484  50.171  1.00 46.16 ? 3003 GOL A O3  1 
HETATM 7046 C C1  . GOL J 3 .   ? 73.651 89.129  47.484  1.00 81.07 ? 3004 GOL A C1  1 
HETATM 7047 O O1  . GOL J 3 .   ? 74.429 88.437  46.524  1.00 81.06 ? 3004 GOL A O1  1 
HETATM 7048 C C2  . GOL J 3 .   ? 72.236 88.556  47.522  1.00 80.40 ? 3004 GOL A C2  1 
HETATM 7049 O O2  . GOL J 3 .   ? 72.333 87.150  47.573  1.00 79.80 ? 3004 GOL A O2  1 
HETATM 7050 C C3  . GOL J 3 .   ? 71.504 89.078  48.758  1.00 80.67 ? 3004 GOL A C3  1 
HETATM 7051 O O3  . GOL J 3 .   ? 70.268 88.410  48.942  1.00 80.08 ? 3004 GOL A O3  1 
HETATM 7052 C C1  . GOL K 3 .   ? 71.861 111.430 42.787  1.00 74.81 ? 3005 GOL A C1  1 
HETATM 7053 O O1  . GOL K 3 .   ? 72.168 110.204 42.139  1.00 73.28 ? 3005 GOL A O1  1 
HETATM 7054 C C2  . GOL K 3 .   ? 70.793 111.233 43.866  1.00 74.59 ? 3005 GOL A C2  1 
HETATM 7055 O O2  . GOL K 3 .   ? 71.278 110.393 44.899  1.00 73.75 ? 3005 GOL A O2  1 
HETATM 7056 C C3  . GOL K 3 .   ? 70.331 112.583 44.421  1.00 74.90 ? 3005 GOL A C3  1 
HETATM 7057 O O3  . GOL K 3 .   ? 68.922 112.581 44.618  1.00 75.27 ? 3005 GOL A O3  1 
HETATM 7058 C C1  . GOL L 3 .   ? 52.520 97.338  -15.277 1.00 53.50 ? 3006 GOL A C1  1 
HETATM 7059 O O1  . GOL L 3 .   ? 52.519 98.749  -15.373 1.00 54.79 ? 3006 GOL A O1  1 
HETATM 7060 C C2  . GOL L 3 .   ? 53.948 96.812  -15.176 1.00 52.69 ? 3006 GOL A C2  1 
HETATM 7061 O O2  . GOL L 3 .   ? 54.686 97.696  -14.359 1.00 52.10 ? 3006 GOL A O2  1 
HETATM 7062 C C3  . GOL L 3 .   ? 53.908 95.388  -14.617 1.00 50.47 ? 3006 GOL A C3  1 
HETATM 7063 O O3  . GOL L 3 .   ? 54.454 94.405  -15.491 1.00 45.58 ? 3006 GOL A O3  1 
HETATM 7064 C C1  . GOL M 3 .   ? 73.059 106.093 43.224  1.00 58.56 ? 3007 GOL A C1  1 
HETATM 7065 O O1  . GOL M 3 .   ? 71.832 105.930 43.916  1.00 54.58 ? 3007 GOL A O1  1 
HETATM 7066 C C2  . GOL M 3 .   ? 74.245 106.134 44.201  1.00 62.36 ? 3007 GOL A C2  1 
HETATM 7067 O O2  . GOL M 3 .   ? 74.715 104.835 44.536  1.00 61.84 ? 3007 GOL A O2  1 
HETATM 7068 C C3  . GOL M 3 .   ? 75.360 107.056 43.669  1.00 64.00 ? 3007 GOL A C3  1 
HETATM 7069 O O3  . GOL M 3 .   ? 76.658 106.477 43.710  1.00 65.85 ? 3007 GOL A O3  1 
HETATM 7070 C C1  . GOL N 3 .   ? 76.880 100.237 34.724  1.00 47.44 ? 3008 GOL A C1  1 
HETATM 7071 O O1  . GOL N 3 .   ? 77.041 100.126 36.111  1.00 44.75 ? 3008 GOL A O1  1 
HETATM 7072 C C2  . GOL N 3 .   ? 78.225 100.114 34.023  1.00 49.94 ? 3008 GOL A C2  1 
HETATM 7073 O O2  . GOL N 3 .   ? 79.109 101.071 34.569  1.00 51.91 ? 3008 GOL A O2  1 
HETATM 7074 C C3  . GOL N 3 .   ? 78.771 98.679  34.111  1.00 50.28 ? 3008 GOL A C3  1 
HETATM 7075 O O3  . GOL N 3 .   ? 79.164 98.229  32.826  1.00 48.36 ? 3008 GOL A O3  1 
HETATM 7076 C C1  . GOL O 3 .   ? 46.060 92.459  36.421  1.00 40.91 ? 3009 GOL A C1  1 
HETATM 7077 O O1  . GOL O 3 .   ? 46.893 93.587  36.588  1.00 35.83 ? 3009 GOL A O1  1 
HETATM 7078 C C2  . GOL O 3 .   ? 44.759 92.780  35.728  1.00 37.83 ? 3009 GOL A C2  1 
HETATM 7079 O O2  . GOL O 3 .   ? 44.498 91.980  34.600  1.00 37.47 ? 3009 GOL A O2  1 
HETATM 7080 C C3  . GOL O 3 .   ? 43.558 92.798  36.667  1.00 35.97 ? 3009 GOL A C3  1 
HETATM 7081 O O3  . GOL O 3 .   ? 42.965 94.066  36.453  1.00 27.36 ? 3009 GOL A O3  1 
HETATM 7082 C C1  . GOL P 3 .   ? 41.468 85.515  34.295  1.00 65.70 ? 3010 GOL A C1  1 
HETATM 7083 O O1  . GOL P 3 .   ? 40.917 85.271  35.581  1.00 64.92 ? 3010 GOL A O1  1 
HETATM 7084 C C2  . GOL P 3 .   ? 41.849 86.988  34.152  1.00 65.48 ? 3010 GOL A C2  1 
HETATM 7085 O O2  . GOL P 3 .   ? 43.017 87.301  34.888  1.00 67.12 ? 3010 GOL A O2  1 
HETATM 7086 C C3  . GOL P 3 .   ? 42.007 87.404  32.695  1.00 64.32 ? 3010 GOL A C3  1 
HETATM 7087 O O3  . GOL P 3 .   ? 43.093 88.297  32.567  1.00 63.69 ? 3010 GOL A O3  1 
HETATM 7088 C C1  . GOL Q 3 .   ? 35.103 106.619 14.719  1.00 75.50 ? 3011 GOL A C1  1 
HETATM 7089 O O1  . GOL Q 3 .   ? 33.834 106.072 14.397  1.00 73.95 ? 3011 GOL A O1  1 
HETATM 7090 C C2  . GOL Q 3 .   ? 35.510 106.405 16.184  1.00 75.50 ? 3011 GOL A C2  1 
HETATM 7091 O O2  . GOL Q 3 .   ? 36.811 105.850 16.231  1.00 76.09 ? 3011 GOL A O2  1 
HETATM 7092 C C3  . GOL Q 3 .   ? 35.554 107.730 16.949  1.00 75.37 ? 3011 GOL A C3  1 
HETATM 7093 O O3  . GOL Q 3 .   ? 35.871 107.514 18.311  1.00 74.45 ? 3011 GOL A O3  1 
HETATM 7094 O O   . HOH R 4 .   ? 37.369 80.795  7.345   1.00 27.79 ? 3012 HOH A O   1 
HETATM 7095 O O   . HOH R 4 .   ? 36.981 76.122  11.010  1.00 43.74 ? 3013 HOH A O   1 
HETATM 7096 O O   . HOH R 4 .   ? 40.441 75.090  10.199  1.00 35.42 ? 3014 HOH A O   1 
HETATM 7097 O O   . HOH R 4 .   ? 42.640 74.098  10.946  1.00 48.52 ? 3015 HOH A O   1 
HETATM 7098 O O   . HOH R 4 .   ? 44.284 75.853  11.694  1.00 40.25 ? 3016 HOH A O   1 
HETATM 7099 O O   . HOH R 4 .   ? 47.211 76.057  10.277  1.00 46.56 ? 3017 HOH A O   1 
HETATM 7100 O O   . HOH R 4 .   ? 50.187 76.625  8.777   1.00 27.73 ? 3018 HOH A O   1 
HETATM 7101 O O   . HOH R 4 .   ? 51.067 75.798  6.204   1.00 31.91 ? 3019 HOH A O   1 
HETATM 7102 O O   . HOH R 4 .   ? 53.566 75.245  5.826   1.00 28.19 ? 3020 HOH A O   1 
HETATM 7103 O O   . HOH R 4 .   ? 53.720 72.576  6.343   1.00 41.10 ? 3021 HOH A O   1 
HETATM 7104 O O   . HOH R 4 .   ? 54.866 75.953  8.105   1.00 48.50 ? 3022 HOH A O   1 
HETATM 7105 O O   . HOH R 4 .   ? 53.924 75.803  10.416  1.00 28.55 ? 3023 HOH A O   1 
HETATM 7106 O O   . HOH R 4 .   ? 54.491 76.463  14.081  1.00 35.78 ? 3024 HOH A O   1 
HETATM 7107 O O   . HOH R 4 .   ? 55.551 78.396  16.819  1.00 43.64 ? 3025 HOH A O   1 
HETATM 7108 O O   . HOH R 4 .   ? 53.525 79.401  17.111  1.00 42.03 ? 3026 HOH A O   1 
HETATM 7109 O O   . HOH R 4 .   ? 50.618 78.583  17.847  1.00 54.96 ? 3027 HOH A O   1 
HETATM 7110 O O   . HOH R 4 .   ? 48.060 79.085  19.441  1.00 37.44 ? 3028 HOH A O   1 
HETATM 7111 O O   . HOH R 4 .   ? 44.680 75.632  21.465  1.00 38.74 ? 3029 HOH A O   1 
HETATM 7112 O O   . HOH R 4 .   ? 43.882 76.177  17.117  1.00 34.34 ? 3030 HOH A O   1 
HETATM 7113 O O   . HOH R 4 .   ? 42.113 76.210  15.024  1.00 41.25 ? 3031 HOH A O   1 
HETATM 7114 O O   . HOH R 4 .   ? 39.951 74.904  15.123  1.00 41.38 ? 3032 HOH A O   1 
HETATM 7115 O O   . HOH R 4 .   ? 36.367 77.262  14.750  1.00 35.61 ? 3033 HOH A O   1 
HETATM 7116 O O   . HOH R 4 .   ? 35.484 79.574  15.600  1.00 31.56 ? 3034 HOH A O   1 
HETATM 7117 O O   . HOH R 4 .   ? 29.967 76.513  18.270  1.00 44.19 ? 3035 HOH A O   1 
HETATM 7118 O O   . HOH R 4 .   ? 31.950 77.771  25.801  1.00 35.83 ? 3036 HOH A O   1 
HETATM 7119 O O   . HOH R 4 .   ? 31.486 80.003  28.146  1.00 30.85 ? 3037 HOH A O   1 
HETATM 7120 O O   . HOH R 4 .   ? 23.642 88.433  24.880  1.00 40.05 ? 3038 HOH A O   1 
HETATM 7121 O O   . HOH R 4 .   ? 21.034 93.226  27.036  1.00 36.92 ? 3039 HOH A O   1 
HETATM 7122 O O   . HOH R 4 .   ? 21.655 94.515  29.228  1.00 56.11 ? 3040 HOH A O   1 
HETATM 7123 O O   . HOH R 4 .   ? 20.945 98.386  27.852  1.00 43.57 ? 3041 HOH A O   1 
HETATM 7124 O O   . HOH R 4 .   ? 20.967 99.890  23.362  1.00 44.18 ? 3042 HOH A O   1 
HETATM 7125 O O   . HOH R 4 .   ? 23.372 99.644  22.425  1.00 32.82 ? 3043 HOH A O   1 
HETATM 7126 O O   . HOH R 4 .   ? 25.145 100.460 19.921  1.00 30.85 ? 3044 HOH A O   1 
HETATM 7127 O O   . HOH R 4 .   ? 27.063 101.509 18.410  1.00 36.14 ? 3045 HOH A O   1 
HETATM 7128 O O   . HOH R 4 .   ? 25.183 102.560 15.746  1.00 56.39 ? 3046 HOH A O   1 
HETATM 7129 O O   . HOH R 4 .   ? 23.367 104.045 18.952  1.00 40.87 ? 3047 HOH A O   1 
HETATM 7130 O O   . HOH R 4 .   ? 18.209 100.487 15.490  1.00 47.13 ? 3048 HOH A O   1 
HETATM 7131 O O   . HOH R 4 .   ? 20.347 97.742  14.272  1.00 48.18 ? 3049 HOH A O   1 
HETATM 7132 O O   . HOH R 4 .   ? 25.415 87.504  18.619  1.00 37.94 ? 3050 HOH A O   1 
HETATM 7133 O O   . HOH R 4 .   ? 25.727 84.122  18.095  1.00 45.02 ? 3051 HOH A O   1 
HETATM 7134 O O   . HOH R 4 .   ? 22.832 82.520  13.348  1.00 43.94 ? 3052 HOH A O   1 
HETATM 7135 O O   . HOH R 4 .   ? 31.396 86.825  5.602   1.00 60.13 ? 3053 HOH A O   1 
HETATM 7136 O O   . HOH R 4 .   ? 34.418 87.223  5.247   1.00 29.74 ? 3054 HOH A O   1 
HETATM 7137 O O   . HOH R 4 .   ? 35.122 89.755  5.584   1.00 30.69 ? 3055 HOH A O   1 
HETATM 7138 O O   . HOH R 4 .   ? 33.987 91.131  3.632   1.00 32.30 ? 3056 HOH A O   1 
HETATM 7139 O O   . HOH R 4 .   ? 31.986 89.590  2.301   1.00 45.23 ? 3057 HOH A O   1 
HETATM 7140 O O   . HOH R 4 .   ? 31.505 90.294  -0.908  1.00 39.73 ? 3058 HOH A O   1 
HETATM 7141 O O   . HOH R 4 .   ? 33.217 88.865  -1.923  1.00 33.58 ? 3059 HOH A O   1 
HETATM 7142 O O   . HOH R 4 .   ? 32.406 87.119  -5.843  1.00 51.93 ? 3060 HOH A O   1 
HETATM 7143 O O   . HOH R 4 .   ? 36.053 93.798  -2.529  1.00 26.08 ? 3061 HOH A O   1 
HETATM 7144 O O   . HOH R 4 .   ? 36.062 96.017  -1.048  1.00 32.88 ? 3062 HOH A O   1 
HETATM 7145 O O   . HOH R 4 .   ? 34.361 98.358  5.229   1.00 38.93 ? 3063 HOH A O   1 
HETATM 7146 O O   . HOH R 4 .   ? 33.590 100.052 8.685   1.00 37.36 ? 3064 HOH A O   1 
HETATM 7147 O O   . HOH R 4 .   ? 31.447 96.173  7.996   1.00 43.75 ? 3065 HOH A O   1 
HETATM 7148 O O   . HOH R 4 .   ? 31.643 93.827  9.069   1.00 35.18 ? 3066 HOH A O   1 
HETATM 7149 O O   . HOH R 4 .   ? 40.033 92.884  7.444   1.00 24.15 ? 3067 HOH A O   1 
HETATM 7150 O O   . HOH R 4 .   ? 40.083 94.111  4.926   1.00 24.46 ? 3068 HOH A O   1 
HETATM 7151 O O   . HOH R 4 .   ? 41.526 96.191  4.781   1.00 25.52 ? 3069 HOH A O   1 
HETATM 7152 O O   . HOH R 4 .   ? 41.900 98.119  3.179   1.00 27.14 ? 3070 HOH A O   1 
HETATM 7153 O O   . HOH R 4 .   ? 41.042 100.490 4.650   1.00 35.30 ? 3071 HOH A O   1 
HETATM 7154 O O   . HOH R 4 .   ? 43.244 102.034 4.965   1.00 41.36 ? 3072 HOH A O   1 
HETATM 7155 O O   . HOH R 4 .   ? 45.060 100.777 3.542   1.00 30.07 ? 3073 HOH A O   1 
HETATM 7156 O O   . HOH R 4 .   ? 46.549 104.116 1.120   1.00 30.01 ? 3074 HOH A O   1 
HETATM 7157 O O   . HOH R 4 .   ? 41.648 104.027 6.053   1.00 33.96 ? 3075 HOH A O   1 
HETATM 7158 O O   . HOH R 4 .   ? 39.488 104.795 6.978   1.00 41.27 ? 3076 HOH A O   1 
HETATM 7159 O O   . HOH R 4 .   ? 39.104 107.224 9.176   1.00 52.80 ? 3077 HOH A O   1 
HETATM 7160 O O   . HOH R 4 .   ? 41.382 107.698 7.901   1.00 39.11 ? 3078 HOH A O   1 
HETATM 7161 O O   . HOH R 4 .   ? 43.528 110.545 9.071   1.00 49.38 ? 3079 HOH A O   1 
HETATM 7162 O O   . HOH R 4 .   ? 47.464 109.868 7.296   1.00 38.43 ? 3080 HOH A O   1 
HETATM 7163 O O   . HOH R 4 .   ? 47.262 111.029 4.760   1.00 37.52 ? 3081 HOH A O   1 
HETATM 7164 O O   . HOH R 4 .   ? 49.437 107.930 6.250   1.00 27.38 ? 3082 HOH A O   1 
HETATM 7165 O O   . HOH R 4 .   ? 51.332 109.669 5.273   1.00 31.79 ? 3083 HOH A O   1 
HETATM 7166 O O   . HOH R 4 .   ? 54.075 109.831 2.920   1.00 31.64 ? 3084 HOH A O   1 
HETATM 7167 O O   . HOH R 4 .   ? 56.523 109.867 2.345   1.00 31.15 ? 3085 HOH A O   1 
HETATM 7168 O O   . HOH R 4 .   ? 57.725 107.649 1.636   1.00 40.07 ? 3086 HOH A O   1 
HETATM 7169 O O   . HOH R 4 .   ? 59.778 108.744 -0.050  1.00 33.96 ? 3087 HOH A O   1 
HETATM 7170 O O   . HOH R 4 .   ? 57.519 110.390 -2.946  1.00 34.51 ? 3088 HOH A O   1 
HETATM 7171 O O   . HOH R 4 .   ? 55.357 111.850 -1.942  1.00 47.24 ? 3089 HOH A O   1 
HETATM 7172 O O   . HOH R 4 .   ? 52.484 110.770 1.068   1.00 48.56 ? 3090 HOH A O   1 
HETATM 7173 O O   . HOH R 4 .   ? 50.843 112.146 -3.953  1.00 46.84 ? 3091 HOH A O   1 
HETATM 7174 O O   . HOH R 4 .   ? 52.519 110.423 -5.061  1.00 36.64 ? 3092 HOH A O   1 
HETATM 7175 O O   . HOH R 4 .   ? 53.272 112.704 -8.286  1.00 48.96 ? 3093 HOH A O   1 
HETATM 7176 O O   . HOH R 4 .   ? 52.612 110.615 -12.238 1.00 42.37 ? 3094 HOH A O   1 
HETATM 7177 O O   . HOH R 4 .   ? 50.207 109.820 -13.228 1.00 46.05 ? 3095 HOH A O   1 
HETATM 7178 O O   . HOH R 4 .   ? 50.814 104.697 -14.138 1.00 46.10 ? 3096 HOH A O   1 
HETATM 7179 O O   . HOH R 4 .   ? 43.478 107.159 -13.608 1.00 42.21 ? 3097 HOH A O   1 
HETATM 7180 O O   . HOH R 4 .   ? 42.465 104.929 -16.175 1.00 44.21 ? 3098 HOH A O   1 
HETATM 7181 O O   . HOH R 4 .   ? 44.743 104.115 -19.200 1.00 37.85 ? 3099 HOH A O   1 
HETATM 7182 O O   . HOH R 4 .   ? 51.305 102.128 -20.834 1.00 28.28 ? 3100 HOH A O   1 
HETATM 7183 O O   . HOH R 4 .   ? 57.182 99.702  -11.866 1.00 32.14 ? 3101 HOH A O   1 
HETATM 7184 O O   . HOH R 4 .   ? 59.874 93.661  -10.175 1.00 35.52 ? 3102 HOH A O   1 
HETATM 7185 O O   . HOH R 4 .   ? 80.212 121.415 39.523  1.00 67.28 ? 3103 HOH A O   1 
HETATM 7186 O O   . HOH R 4 .   ? 78.301 119.942 39.003  1.00 60.26 ? 3104 HOH A O   1 
HETATM 7187 O O   . HOH R 4 .   ? 72.069 93.855  -11.507 1.00 45.18 ? 3105 HOH A O   1 
HETATM 7188 O O   . HOH R 4 .   ? 66.993 113.574 46.874  1.00 55.16 ? 3106 HOH A O   1 
HETATM 7189 O O   . HOH R 4 .   ? 72.177 99.393  -4.317  1.00 35.31 ? 3107 HOH A O   1 
HETATM 7190 O O   . HOH R 4 .   ? 68.044 101.260 -3.550  1.00 29.44 ? 3108 HOH A O   1 
HETATM 7191 O O   . HOH R 4 .   ? 69.469 103.060 -2.430  1.00 37.28 ? 3109 HOH A O   1 
HETATM 7192 O O   . HOH R 4 .   ? 65.819 102.503 -0.353  1.00 32.43 ? 3110 HOH A O   1 
HETATM 7193 O O   . HOH R 4 .   ? 65.398 105.465 -0.599  1.00 41.63 ? 3111 HOH A O   1 
HETATM 7194 O O   . HOH R 4 .   ? 63.678 108.095 -2.004  1.00 36.62 ? 3112 HOH A O   1 
HETATM 7195 O O   . HOH R 4 .   ? 63.561 108.763 -5.051  1.00 43.68 ? 3113 HOH A O   1 
HETATM 7196 O O   . HOH R 4 .   ? 66.970 103.997 -6.994  1.00 41.88 ? 3114 HOH A O   1 
HETATM 7197 O O   . HOH R 4 .   ? 66.467 101.756 -5.715  1.00 23.23 ? 3115 HOH A O   1 
HETATM 7198 O O   . HOH R 4 .   ? 69.478 94.460  -1.429  1.00 29.43 ? 3116 HOH A O   1 
HETATM 7199 O O   . HOH R 4 .   ? 73.762 94.605  -1.845  1.00 48.01 ? 3117 HOH A O   1 
HETATM 7200 O O   . HOH R 4 .   ? 75.600 90.684  3.231   1.00 37.84 ? 3118 HOH A O   1 
HETATM 7201 O O   . HOH R 4 .   ? 78.947 91.162  7.823   1.00 33.61 ? 3119 HOH A O   1 
HETATM 7202 O O   . HOH R 4 .   ? 81.509 96.507  10.953  1.00 33.45 ? 3120 HOH A O   1 
HETATM 7203 O O   . HOH R 4 .   ? 79.337 97.324  12.320  1.00 30.46 ? 3121 HOH A O   1 
HETATM 7204 O O   . HOH R 4 .   ? 80.461 99.717  12.831  1.00 45.35 ? 3122 HOH A O   1 
HETATM 7205 O O   . HOH R 4 .   ? 79.159 101.483 11.952  1.00 58.69 ? 3123 HOH A O   1 
HETATM 7206 O O   . HOH R 4 .   ? 81.917 102.703 14.185  1.00 40.61 ? 3124 HOH A O   1 
HETATM 7207 O O   . HOH R 4 .   ? 80.459 103.939 15.660  1.00 35.62 ? 3125 HOH A O   1 
HETATM 7208 O O   . HOH R 4 .   ? 80.557 106.615 15.591  1.00 50.98 ? 3126 HOH A O   1 
HETATM 7209 O O   . HOH R 4 .   ? 78.325 107.010 14.043  1.00 38.40 ? 3127 HOH A O   1 
HETATM 7210 O O   . HOH R 4 .   ? 73.836 106.509 14.496  1.00 40.46 ? 3128 HOH A O   1 
HETATM 7211 O O   . HOH R 4 .   ? 75.358 103.198 12.790  1.00 31.15 ? 3129 HOH A O   1 
HETATM 7212 O O   . HOH R 4 .   ? 73.070 103.886 9.341   1.00 38.53 ? 3130 HOH A O   1 
HETATM 7213 O O   . HOH R 4 .   ? 70.190 104.143 10.482  1.00 34.60 ? 3131 HOH A O   1 
HETATM 7214 O O   . HOH R 4 .   ? 68.861 105.532 8.883   1.00 31.83 ? 3132 HOH A O   1 
HETATM 7215 O O   . HOH R 4 .   ? 67.242 107.192 10.016  1.00 52.24 ? 3133 HOH A O   1 
HETATM 7216 O O   . HOH R 4 .   ? 67.165 109.637 9.974   1.00 51.00 ? 3134 HOH A O   1 
HETATM 7217 O O   . HOH R 4 .   ? 66.423 108.613 7.737   1.00 43.18 ? 3135 HOH A O   1 
HETATM 7218 O O   . HOH R 4 .   ? 60.763 110.365 8.610   1.00 43.73 ? 3136 HOH A O   1 
HETATM 7219 O O   . HOH R 4 .   ? 59.384 112.955 8.841   1.00 46.97 ? 3137 HOH A O   1 
HETATM 7220 O O   . HOH R 4 .   ? 61.980 114.971 10.693  1.00 42.48 ? 3138 HOH A O   1 
HETATM 7221 O O   . HOH R 4 .   ? 62.753 115.114 13.621  1.00 41.45 ? 3139 HOH A O   1 
HETATM 7222 O O   . HOH R 4 .   ? 62.730 118.129 13.141  1.00 45.05 ? 3140 HOH A O   1 
HETATM 7223 O O   . HOH R 4 .   ? 63.135 120.176 14.349  1.00 40.41 ? 3141 HOH A O   1 
HETATM 7224 O O   . HOH R 4 .   ? 64.986 122.105 13.931  1.00 32.93 ? 3142 HOH A O   1 
HETATM 7225 O O   . HOH R 4 .   ? 63.325 128.844 16.133  1.00 32.62 ? 3143 HOH A O   1 
HETATM 7226 O O   . HOH R 4 .   ? 58.941 128.005 14.447  1.00 49.21 ? 3144 HOH A O   1 
HETATM 7227 O O   . HOH R 4 .   ? 50.779 126.399 20.469  1.00 43.57 ? 3145 HOH A O   1 
HETATM 7228 O O   . HOH R 4 .   ? 52.231 124.008 22.013  1.00 41.69 ? 3146 HOH A O   1 
HETATM 7229 O O   . HOH R 4 .   ? 50.165 122.725 21.609  1.00 43.92 ? 3147 HOH A O   1 
HETATM 7230 O O   . HOH R 4 .   ? 54.448 124.746 25.867  1.00 29.30 ? 3148 HOH A O   1 
HETATM 7231 O O   . HOH R 4 .   ? 56.737 123.350 25.082  1.00 25.86 ? 3149 HOH A O   1 
HETATM 7232 O O   . HOH R 4 .   ? 55.190 127.436 26.487  1.00 48.26 ? 3150 HOH A O   1 
HETATM 7233 O O   . HOH R 4 .   ? 54.649 125.288 29.967  1.00 45.74 ? 3151 HOH A O   1 
HETATM 7234 O O   . HOH R 4 .   ? 56.759 126.300 30.579  1.00 28.83 ? 3152 HOH A O   1 
HETATM 7235 O O   . HOH R 4 .   ? 59.550 123.145 31.457  1.00 29.80 ? 3153 HOH A O   1 
HETATM 7236 O O   . HOH R 4 .   ? 58.110 123.231 33.438  1.00 33.72 ? 3154 HOH A O   1 
HETATM 7237 O O   . HOH R 4 .   ? 59.895 121.355 34.330  1.00 31.30 ? 3155 HOH A O   1 
HETATM 7238 O O   . HOH R 4 .   ? 59.293 120.401 36.631  1.00 28.55 ? 3156 HOH A O   1 
HETATM 7239 O O   . HOH R 4 .   ? 57.599 122.403 37.422  1.00 42.78 ? 3157 HOH A O   1 
HETATM 7240 O O   . HOH R 4 .   ? 57.150 118.676 35.030  1.00 34.70 ? 3158 HOH A O   1 
HETATM 7241 O O   . HOH R 4 .   ? 54.693 119.448 35.449  1.00 41.72 ? 3159 HOH A O   1 
HETATM 7242 O O   . HOH R 4 .   ? 57.407 115.723 34.831  1.00 37.18 ? 3160 HOH A O   1 
HETATM 7243 O O   . HOH R 4 .   ? 55.986 115.769 32.608  1.00 30.51 ? 3161 HOH A O   1 
HETATM 7244 O O   . HOH R 4 .   ? 50.474 115.672 32.731  1.00 39.28 ? 3162 HOH A O   1 
HETATM 7245 O O   . HOH R 4 .   ? 50.702 115.392 30.209  1.00 27.51 ? 3163 HOH A O   1 
HETATM 7246 O O   . HOH R 4 .   ? 47.874 114.190 33.117  1.00 34.18 ? 3164 HOH A O   1 
HETATM 7247 O O   . HOH R 4 .   ? 47.112 115.457 35.568  1.00 38.14 ? 3165 HOH A O   1 
HETATM 7248 O O   . HOH R 4 .   ? 44.395 115.471 36.924  1.00 55.67 ? 3166 HOH A O   1 
HETATM 7249 O O   . HOH R 4 .   ? 45.271 116.431 43.623  1.00 32.84 ? 3167 HOH A O   1 
HETATM 7250 O O   . HOH R 4 .   ? 41.469 113.280 44.129  1.00 40.88 ? 3168 HOH A O   1 
HETATM 7251 O O   . HOH R 4 .   ? 41.240 117.997 47.305  1.00 47.04 ? 3169 HOH A O   1 
HETATM 7252 O O   . HOH R 4 .   ? 37.166 112.365 50.706  1.00 47.68 ? 3170 HOH A O   1 
HETATM 7253 O O   . HOH R 4 .   ? 36.315 108.444 50.587  1.00 39.17 ? 3171 HOH A O   1 
HETATM 7254 O O   . HOH R 4 .   ? 34.647 110.961 46.717  1.00 49.77 ? 3172 HOH A O   1 
HETATM 7255 O O   . HOH R 4 .   ? 32.873 105.973 46.899  1.00 48.29 ? 3173 HOH A O   1 
HETATM 7256 O O   . HOH R 4 .   ? 32.289 105.548 44.174  1.00 33.41 ? 3174 HOH A O   1 
HETATM 7257 O O   . HOH R 4 .   ? 31.441 108.107 38.497  1.00 47.08 ? 3175 HOH A O   1 
HETATM 7258 O O   . HOH R 4 .   ? 31.682 108.124 35.781  1.00 29.05 ? 3176 HOH A O   1 
HETATM 7259 O O   . HOH R 4 .   ? 28.701 107.333 38.680  1.00 46.48 ? 3177 HOH A O   1 
HETATM 7260 O O   . HOH R 4 .   ? 26.267 109.312 39.847  1.00 51.32 ? 3178 HOH A O   1 
HETATM 7261 O O   . HOH R 4 .   ? 23.303 110.028 35.142  1.00 45.17 ? 3179 HOH A O   1 
HETATM 7262 O O   . HOH R 4 .   ? 25.457 112.544 31.140  1.00 43.61 ? 3180 HOH A O   1 
HETATM 7263 O O   . HOH R 4 .   ? 26.378 110.565 29.558  1.00 39.42 ? 3181 HOH A O   1 
HETATM 7264 O O   . HOH R 4 .   ? 28.297 109.083 30.294  1.00 31.65 ? 3182 HOH A O   1 
HETATM 7265 O O   . HOH R 4 .   ? 31.117 114.022 27.059  1.00 41.34 ? 3183 HOH A O   1 
HETATM 7266 O O   . HOH R 4 .   ? 32.319 115.215 24.732  1.00 42.39 ? 3184 HOH A O   1 
HETATM 7267 O O   . HOH R 4 .   ? 34.453 113.700 23.881  1.00 38.19 ? 3185 HOH A O   1 
HETATM 7268 O O   . HOH R 4 .   ? 34.218 113.356 21.219  1.00 40.89 ? 3186 HOH A O   1 
HETATM 7269 O O   . HOH R 4 .   ? 36.804 115.130 24.395  1.00 33.11 ? 3187 HOH A O   1 
HETATM 7270 O O   . HOH R 4 .   ? 42.402 119.817 24.837  1.00 44.88 ? 3188 HOH A O   1 
HETATM 7271 O O   . HOH R 4 .   ? 44.120 118.135 23.852  1.00 41.30 ? 3189 HOH A O   1 
HETATM 7272 O O   . HOH R 4 .   ? 44.591 116.244 26.023  1.00 29.26 ? 3190 HOH A O   1 
HETATM 7273 O O   . HOH R 4 .   ? 48.963 110.857 25.006  1.00 34.18 ? 3191 HOH A O   1 
HETATM 7274 O O   . HOH R 4 .   ? 47.149 109.789 23.502  1.00 34.42 ? 3192 HOH A O   1 
HETATM 7275 O O   . HOH R 4 .   ? 47.095 110.990 21.152  1.00 46.37 ? 3193 HOH A O   1 
HETATM 7276 O O   . HOH R 4 .   ? 49.908 111.046 18.432  1.00 37.50 ? 3194 HOH A O   1 
HETATM 7277 O O   . HOH R 4 .   ? 51.719 111.086 16.438  1.00 43.05 ? 3195 HOH A O   1 
HETATM 7278 O O   . HOH R 4 .   ? 52.311 110.355 11.843  1.00 30.94 ? 3196 HOH A O   1 
HETATM 7279 O O   . HOH R 4 .   ? 51.876 110.001 9.243   1.00 32.80 ? 3197 HOH A O   1 
HETATM 7280 O O   . HOH R 4 .   ? 54.593 114.084 13.456  1.00 43.20 ? 3198 HOH A O   1 
HETATM 7281 O O   . HOH R 4 .   ? 52.942 117.079 17.729  1.00 36.12 ? 3199 HOH A O   1 
HETATM 7282 O O   . HOH R 4 .   ? 54.157 117.279 21.011  1.00 38.27 ? 3200 HOH A O   1 
HETATM 7283 O O   . HOH R 4 .   ? 51.859 113.329 20.813  1.00 39.72 ? 3201 HOH A O   1 
HETATM 7284 O O   . HOH R 4 .   ? 51.083 112.149 24.034  1.00 39.47 ? 3202 HOH A O   1 
HETATM 7285 O O   . HOH R 4 .   ? 52.456 109.926 28.249  1.00 18.54 ? 3203 HOH A O   1 
HETATM 7286 O O   . HOH R 4 .   ? 54.321 104.348 22.358  1.00 36.86 ? 3204 HOH A O   1 
HETATM 7287 O O   . HOH R 4 .   ? 57.438 108.829 20.744  1.00 33.25 ? 3205 HOH A O   1 
HETATM 7288 O O   . HOH R 4 .   ? 58.948 103.336 17.582  1.00 29.36 ? 3206 HOH A O   1 
HETATM 7289 O O   . HOH R 4 .   ? 63.368 98.113  17.433  1.00 42.67 ? 3207 HOH A O   1 
HETATM 7290 O O   . HOH R 4 .   ? 64.829 94.851  13.192  1.00 26.73 ? 3208 HOH A O   1 
HETATM 7291 O O   . HOH R 4 .   ? 70.659 92.983  16.789  1.00 25.27 ? 3209 HOH A O   1 
HETATM 7292 O O   . HOH R 4 .   ? 69.572 93.792  19.796  1.00 25.08 ? 3210 HOH A O   1 
HETATM 7293 O O   . HOH R 4 .   ? 71.617 87.801  21.940  1.00 33.29 ? 3211 HOH A O   1 
HETATM 7294 O O   . HOH R 4 .   ? 74.000 89.227  23.174  1.00 36.18 ? 3212 HOH A O   1 
HETATM 7295 O O   . HOH R 4 .   ? 74.617 89.383  25.939  1.00 42.86 ? 3213 HOH A O   1 
HETATM 7296 O O   . HOH R 4 .   ? 72.850 90.007  27.808  1.00 24.23 ? 3214 HOH A O   1 
HETATM 7297 O O   . HOH R 4 .   ? 73.233 86.459  31.014  1.00 41.76 ? 3215 HOH A O   1 
HETATM 7298 O O   . HOH R 4 .   ? 75.226 84.864  31.636  1.00 37.81 ? 3216 HOH A O   1 
HETATM 7299 O O   . HOH R 4 .   ? 71.043 82.966  28.267  1.00 51.79 ? 3217 HOH A O   1 
HETATM 7300 O O   . HOH R 4 .   ? 64.890 81.600  27.589  1.00 43.18 ? 3218 HOH A O   1 
HETATM 7301 O O   . HOH R 4 .   ? 65.301 79.220  33.044  1.00 41.79 ? 3219 HOH A O   1 
HETATM 7302 O O   . HOH R 4 .   ? 62.767 79.937  33.466  1.00 36.84 ? 3220 HOH A O   1 
HETATM 7303 O O   . HOH R 4 .   ? 60.939 78.186  33.630  1.00 53.08 ? 3221 HOH A O   1 
HETATM 7304 O O   . HOH R 4 .   ? 59.025 79.042  30.909  1.00 41.44 ? 3222 HOH A O   1 
HETATM 7305 O O   . HOH R 4 .   ? 56.144 81.476  31.339  1.00 42.32 ? 3223 HOH A O   1 
HETATM 7306 O O   . HOH R 4 .   ? 54.556 83.836  31.253  1.00 32.17 ? 3224 HOH A O   1 
HETATM 7307 O O   . HOH R 4 .   ? 56.745 86.256  28.763  1.00 32.78 ? 3225 HOH A O   1 
HETATM 7308 O O   . HOH R 4 .   ? 56.856 88.822  27.662  1.00 42.56 ? 3226 HOH A O   1 
HETATM 7309 O O   . HOH R 4 .   ? 54.949 89.633  29.025  1.00 32.92 ? 3227 HOH A O   1 
HETATM 7310 O O   . HOH R 4 .   ? 54.908 91.751  31.007  1.00 32.74 ? 3228 HOH A O   1 
HETATM 7311 O O   . HOH R 4 .   ? 58.414 89.242  30.297  1.00 24.83 ? 3229 HOH A O   1 
HETATM 7312 O O   . HOH R 4 .   ? 57.863 89.273  25.297  1.00 38.05 ? 3230 HOH A O   1 
HETATM 7313 O O   . HOH R 4 .   ? 55.882 89.810  23.662  1.00 35.64 ? 3231 HOH A O   1 
HETATM 7314 O O   . HOH R 4 .   ? 53.467 90.106  24.934  1.00 31.78 ? 3232 HOH A O   1 
HETATM 7315 O O   . HOH R 4 .   ? 56.160 91.417  21.160  1.00 47.99 ? 3233 HOH A O   1 
HETATM 7316 O O   . HOH R 4 .   ? 55.267 90.253  18.858  1.00 24.82 ? 3234 HOH A O   1 
HETATM 7317 O O   . HOH R 4 .   ? 58.265 88.453  21.169  1.00 28.84 ? 3235 HOH A O   1 
HETATM 7318 O O   . HOH R 4 .   ? 59.925 87.164  22.910  1.00 28.60 ? 3236 HOH A O   1 
HETATM 7319 O O   . HOH R 4 .   ? 56.194 81.503  22.806  1.00 29.00 ? 3237 HOH A O   1 
HETATM 7320 O O   . HOH R 4 .   ? 56.870 78.480  20.464  1.00 50.78 ? 3238 HOH A O   1 
HETATM 7321 O O   . HOH R 4 .   ? 60.545 81.446  17.627  1.00 42.90 ? 3239 HOH A O   1 
HETATM 7322 O O   . HOH R 4 .   ? 60.677 83.222  15.554  1.00 34.87 ? 3240 HOH A O   1 
HETATM 7323 O O   . HOH R 4 .   ? 59.332 82.388  13.509  1.00 28.94 ? 3241 HOH A O   1 
HETATM 7324 O O   . HOH R 4 .   ? 61.171 86.092  16.095  1.00 26.11 ? 3242 HOH A O   1 
HETATM 7325 O O   . HOH R 4 .   ? 60.751 89.461  15.436  1.00 21.52 ? 3243 HOH A O   1 
HETATM 7326 O O   . HOH R 4 .   ? 67.422 86.851  17.325  1.00 23.19 ? 3244 HOH A O   1 
HETATM 7327 O O   . HOH R 4 .   ? 66.813 88.027  25.567  1.00 31.57 ? 3245 HOH A O   1 
HETATM 7328 O O   . HOH R 4 .   ? 70.149 92.118  34.438  1.00 27.36 ? 3246 HOH A O   1 
HETATM 7329 O O   . HOH R 4 .   ? 72.607 92.778  34.744  1.00 31.71 ? 3247 HOH A O   1 
HETATM 7330 O O   . HOH R 4 .   ? 72.158 86.550  38.432  1.00 34.56 ? 3248 HOH A O   1 
HETATM 7331 O O   . HOH R 4 .   ? 73.870 87.557  41.318  1.00 40.22 ? 3249 HOH A O   1 
HETATM 7332 O O   . HOH R 4 .   ? 73.212 86.338  43.273  1.00 40.92 ? 3250 HOH A O   1 
HETATM 7333 O O   . HOH R 4 .   ? 71.432 84.794  45.082  1.00 40.16 ? 3251 HOH A O   1 
HETATM 7334 O O   . HOH R 4 .   ? 69.150 85.683  45.983  1.00 35.88 ? 3252 HOH A O   1 
HETATM 7335 O O   . HOH R 4 .   ? 67.105 84.485  44.773  1.00 33.57 ? 3253 HOH A O   1 
HETATM 7336 O O   . HOH R 4 .   ? 64.566 84.298  46.999  1.00 44.83 ? 3254 HOH A O   1 
HETATM 7337 O O   . HOH R 4 .   ? 65.990 82.437  40.686  1.00 41.25 ? 3255 HOH A O   1 
HETATM 7338 O O   . HOH R 4 .   ? 62.868 80.447  36.144  1.00 39.76 ? 3256 HOH A O   1 
HETATM 7339 O O   . HOH R 4 .   ? 67.097 79.215  35.442  1.00 43.35 ? 3257 HOH A O   1 
HETATM 7340 O O   . HOH R 4 .   ? 68.485 80.989  33.815  1.00 34.84 ? 3258 HOH A O   1 
HETATM 7341 O O   . HOH R 4 .   ? 71.688 81.738  42.104  1.00 50.04 ? 3259 HOH A O   1 
HETATM 7342 O O   . HOH R 4 .   ? 78.865 83.450  36.127  1.00 41.15 ? 3260 HOH A O   1 
HETATM 7343 O O   . HOH R 4 .   ? 78.064 89.438  43.191  1.00 50.28 ? 3261 HOH A O   1 
HETATM 7344 O O   . HOH R 4 .   ? 74.313 98.626  41.699  1.00 37.41 ? 3262 HOH A O   1 
HETATM 7345 O O   . HOH R 4 .   ? 71.763 103.088 45.754  1.00 34.69 ? 3263 HOH A O   1 
HETATM 7346 O O   . HOH R 4 .   ? 73.375 105.905 40.078  1.00 38.56 ? 3264 HOH A O   1 
HETATM 7347 O O   . HOH R 4 .   ? 67.490 110.446 42.967  1.00 32.63 ? 3265 HOH A O   1 
HETATM 7348 O O   . HOH R 4 .   ? 67.463 108.544 44.975  1.00 25.35 ? 3266 HOH A O   1 
HETATM 7349 O O   . HOH R 4 .   ? 61.713 109.682 47.852  1.00 30.18 ? 3267 HOH A O   1 
HETATM 7350 O O   . HOH R 4 .   ? 60.720 108.229 46.078  1.00 25.29 ? 3268 HOH A O   1 
HETATM 7351 O O   . HOH R 4 .   ? 59.259 109.718 44.329  1.00 29.75 ? 3269 HOH A O   1 
HETATM 7352 O O   . HOH R 4 .   ? 57.948 111.468 45.913  1.00 31.55 ? 3270 HOH A O   1 
HETATM 7353 O O   . HOH R 4 .   ? 59.205 114.716 46.850  1.00 55.72 ? 3271 HOH A O   1 
HETATM 7354 O O   . HOH R 4 .   ? 61.406 114.458 43.939  1.00 41.44 ? 3272 HOH A O   1 
HETATM 7355 O O   . HOH R 4 .   ? 65.364 118.841 41.871  1.00 23.47 ? 3273 HOH A O   1 
HETATM 7356 O O   . HOH R 4 .   ? 67.503 121.959 42.148  1.00 48.17 ? 3274 HOH A O   1 
HETATM 7357 O O   . HOH R 4 .   ? 71.156 114.622 41.914  1.00 43.52 ? 3275 HOH A O   1 
HETATM 7358 O O   . HOH R 4 .   ? 74.274 120.609 41.449  1.00 51.27 ? 3276 HOH A O   1 
HETATM 7359 O O   . HOH R 4 .   ? 75.314 118.274 35.681  1.00 41.11 ? 3277 HOH A O   1 
HETATM 7360 O O   . HOH R 4 .   ? 78.042 114.922 32.603  1.00 47.59 ? 3278 HOH A O   1 
HETATM 7361 O O   . HOH R 4 .   ? 79.230 109.104 33.379  1.00 51.86 ? 3279 HOH A O   1 
HETATM 7362 O O   . HOH R 4 .   ? 86.066 107.261 36.663  1.00 35.16 ? 3280 HOH A O   1 
HETATM 7363 O O   . HOH R 4 .   ? 90.009 104.645 28.803  1.00 34.65 ? 3281 HOH A O   1 
HETATM 7364 O O   . HOH R 4 .   ? 90.435 106.136 25.998  1.00 38.25 ? 3282 HOH A O   1 
HETATM 7365 O O   . HOH R 4 .   ? 87.933 107.360 28.289  1.00 30.05 ? 3283 HOH A O   1 
HETATM 7366 O O   . HOH R 4 .   ? 89.357 108.124 21.255  1.00 44.59 ? 3284 HOH A O   1 
HETATM 7367 O O   . HOH R 4 .   ? 92.122 113.823 22.295  1.00 29.52 ? 3285 HOH A O   1 
HETATM 7368 O O   . HOH R 4 .   ? 89.952 115.711 22.604  1.00 43.91 ? 3286 HOH A O   1 
HETATM 7369 O O   . HOH R 4 .   ? 97.245 113.727 27.721  1.00 48.31 ? 3287 HOH A O   1 
HETATM 7370 O O   . HOH R 4 .   ? 86.410 119.491 36.839  1.00 32.17 ? 3288 HOH A O   1 
HETATM 7371 O O   . HOH R 4 .   ? 79.978 123.604 37.288  1.00 46.32 ? 3289 HOH A O   1 
HETATM 7372 O O   . HOH R 4 .   ? 80.673 129.400 31.342  1.00 53.41 ? 3290 HOH A O   1 
HETATM 7373 O O   . HOH R 4 .   ? 76.185 132.585 29.139  1.00 41.69 ? 3291 HOH A O   1 
HETATM 7374 O O   . HOH R 4 .   ? 73.383 125.836 25.484  1.00 29.88 ? 3292 HOH A O   1 
HETATM 7375 O O   . HOH R 4 .   ? 71.413 124.704 24.456  1.00 42.58 ? 3293 HOH A O   1 
HETATM 7376 O O   . HOH R 4 .   ? 64.459 125.764 27.221  1.00 38.56 ? 3294 HOH A O   1 
HETATM 7377 O O   . HOH R 4 .   ? 65.998 127.244 30.577  1.00 34.48 ? 3295 HOH A O   1 
HETATM 7378 O O   . HOH R 4 .   ? 67.951 128.668 29.914  1.00 43.39 ? 3296 HOH A O   1 
HETATM 7379 O O   . HOH R 4 .   ? 64.499 132.179 33.511  1.00 54.59 ? 3297 HOH A O   1 
HETATM 7380 O O   . HOH R 4 .   ? 65.621 125.211 38.514  1.00 42.97 ? 3298 HOH A O   1 
HETATM 7381 O O   . HOH R 4 .   ? 68.866 124.261 37.931  1.00 41.45 ? 3299 HOH A O   1 
HETATM 7382 O O   . HOH R 4 .   ? 70.556 124.542 35.878  1.00 36.88 ? 3300 HOH A O   1 
HETATM 7383 O O   . HOH R 4 .   ? 62.249 122.571 34.020  1.00 22.84 ? 3301 HOH A O   1 
HETATM 7384 O O   . HOH R 4 .   ? 61.532 118.730 28.274  1.00 37.26 ? 3302 HOH A O   1 
HETATM 7385 O O   . HOH R 4 .   ? 65.303 115.035 34.151  1.00 21.54 ? 3303 HOH A O   1 
HETATM 7386 O O   . HOH R 4 .   ? 67.002 113.723 35.321  1.00 19.16 ? 3304 HOH A O   1 
HETATM 7387 O O   . HOH R 4 .   ? 56.707 113.822 38.313  1.00 32.64 ? 3305 HOH A O   1 
HETATM 7388 O O   . HOH R 4 .   ? 53.583 110.391 47.967  1.00 40.86 ? 3306 HOH A O   1 
HETATM 7389 O O   . HOH R 4 .   ? 57.505 113.294 51.958  1.00 47.94 ? 3307 HOH A O   1 
HETATM 7390 O O   . HOH R 4 .   ? 56.908 116.421 49.694  1.00 46.91 ? 3308 HOH A O   1 
HETATM 7391 O O   . HOH R 4 .   ? 59.680 109.512 53.642  1.00 49.74 ? 3309 HOH A O   1 
HETATM 7392 O O   . HOH R 4 .   ? 57.917 107.799 53.578  1.00 45.16 ? 3310 HOH A O   1 
HETATM 7393 O O   . HOH R 4 .   ? 57.890 103.463 55.246  1.00 40.20 ? 3311 HOH A O   1 
HETATM 7394 O O   . HOH R 4 .   ? 60.471 102.415 55.351  1.00 44.37 ? 3312 HOH A O   1 
HETATM 7395 O O   . HOH R 4 .   ? 61.945 101.873 52.839  1.00 30.34 ? 3313 HOH A O   1 
HETATM 7396 O O   . HOH R 4 .   ? 64.194 102.945 53.319  1.00 44.20 ? 3314 HOH A O   1 
HETATM 7397 O O   . HOH R 4 .   ? 66.603 102.712 52.232  1.00 38.26 ? 3315 HOH A O   1 
HETATM 7398 O O   . HOH R 4 .   ? 62.315 98.967  53.090  1.00 32.71 ? 3316 HOH A O   1 
HETATM 7399 O O   . HOH R 4 .   ? 64.322 96.843  55.992  1.00 49.41 ? 3317 HOH A O   1 
HETATM 7400 O O   . HOH R 4 .   ? 68.048 95.439  54.889  1.00 62.57 ? 3318 HOH A O   1 
HETATM 7401 O O   . HOH R 4 .   ? 70.631 92.142  50.401  1.00 38.47 ? 3319 HOH A O   1 
HETATM 7402 O O   . HOH R 4 .   ? 68.458 91.821  48.034  1.00 27.56 ? 3320 HOH A O   1 
HETATM 7403 O O   . HOH R 4 .   ? 66.999 90.979  49.749  1.00 36.96 ? 3321 HOH A O   1 
HETATM 7404 O O   . HOH R 4 .   ? 82.652 94.333  34.029  1.00 51.57 ? 3322 HOH A O   1 
HETATM 7405 O O   . HOH R 4 .   ? 81.640 95.705  32.157  1.00 50.17 ? 3323 HOH A O   1 
HETATM 7406 O O   . HOH R 4 .   ? 83.359 97.911  30.978  1.00 39.39 ? 3324 HOH A O   1 
HETATM 7407 O O   . HOH R 4 .   ? 85.983 100.432 34.009  1.00 42.34 ? 3325 HOH A O   1 
HETATM 7408 O O   . HOH R 4 .   ? 88.252 96.346  28.693  1.00 45.73 ? 3326 HOH A O   1 
HETATM 7409 O O   . HOH R 4 .   ? 84.317 93.161  32.109  1.00 47.61 ? 3327 HOH A O   1 
HETATM 7410 O O   . HOH R 4 .   ? 76.800 97.190  27.620  1.00 24.18 ? 3328 HOH A O   1 
HETATM 7411 O O   . HOH R 4 .   ? 85.658 99.318  21.411  1.00 48.38 ? 3329 HOH A O   1 
HETATM 7412 O O   . HOH R 4 .   ? 88.731 100.993 18.965  1.00 44.19 ? 3330 HOH A O   1 
HETATM 7413 O O   . HOH R 4 .   ? 89.690 98.774  20.180  1.00 51.29 ? 3331 HOH A O   1 
HETATM 7414 O O   . HOH R 4 .   ? 82.889 104.465 17.694  1.00 31.65 ? 3332 HOH A O   1 
HETATM 7415 O O   . HOH R 4 .   ? 81.263 111.592 14.997  1.00 44.11 ? 3333 HOH A O   1 
HETATM 7416 O O   . HOH R 4 .   ? 81.262 113.609 13.391  1.00 46.48 ? 3334 HOH A O   1 
HETATM 7417 O O   . HOH R 4 .   ? 81.704 116.372 14.647  1.00 41.28 ? 3335 HOH A O   1 
HETATM 7418 O O   . HOH R 4 .   ? 82.749 121.307 16.550  1.00 36.46 ? 3336 HOH A O   1 
HETATM 7419 O O   . HOH R 4 .   ? 85.915 129.114 23.029  1.00 39.69 ? 3337 HOH A O   1 
HETATM 7420 O O   . HOH R 4 .   ? 86.696 131.072 28.799  1.00 50.21 ? 3338 HOH A O   1 
HETATM 7421 O O   . HOH R 4 .   ? 79.228 130.228 19.558  1.00 46.54 ? 3339 HOH A O   1 
HETATM 7422 O O   . HOH R 4 .   ? 77.792 127.241 18.265  1.00 43.79 ? 3340 HOH A O   1 
HETATM 7423 O O   . HOH R 4 .   ? 75.653 128.885 16.512  1.00 44.54 ? 3341 HOH A O   1 
HETATM 7424 O O   . HOH R 4 .   ? 72.948 128.547 17.037  1.00 32.59 ? 3342 HOH A O   1 
HETATM 7425 O O   . HOH R 4 .   ? 72.482 131.837 20.839  1.00 44.33 ? 3343 HOH A O   1 
HETATM 7426 O O   . HOH R 4 .   ? 77.900 126.219 13.487  1.00 57.89 ? 3344 HOH A O   1 
HETATM 7427 O O   . HOH R 4 .   ? 69.101 112.511 14.819  1.00 48.22 ? 3345 HOH A O   1 
HETATM 7428 O O   . HOH R 4 .   ? 68.767 109.658 17.624  1.00 33.19 ? 3346 HOH A O   1 
HETATM 7429 O O   . HOH R 4 .   ? 66.643 108.375 16.979  1.00 25.27 ? 3347 HOH A O   1 
HETATM 7430 O O   . HOH R 4 .   ? 64.509 107.676 18.583  1.00 20.45 ? 3348 HOH A O   1 
HETATM 7431 O O   . HOH R 4 .   ? 68.038 111.740 19.149  1.00 40.86 ? 3349 HOH A O   1 
HETATM 7432 O O   . HOH R 4 .   ? 68.649 111.458 21.808  1.00 32.04 ? 3350 HOH A O   1 
HETATM 7433 O O   . HOH R 4 .   ? 70.157 113.065 22.621  1.00 29.34 ? 3351 HOH A O   1 
HETATM 7434 O O   . HOH R 4 .   ? 72.353 112.946 21.456  1.00 24.85 ? 3352 HOH A O   1 
HETATM 7435 O O   . HOH R 4 .   ? 72.279 111.555 19.157  1.00 46.34 ? 3353 HOH A O   1 
HETATM 7436 O O   . HOH R 4 .   ? 69.810 107.544 15.398  1.00 32.97 ? 3354 HOH A O   1 
HETATM 7437 O O   . HOH R 4 .   ? 67.082 106.367 13.406  1.00 44.24 ? 3355 HOH A O   1 
HETATM 7438 O O   . HOH R 4 .   ? 70.279 105.037 12.907  1.00 39.92 ? 3356 HOH A O   1 
HETATM 7439 O O   . HOH R 4 .   ? 69.129 101.652 10.722  1.00 24.94 ? 3357 HOH A O   1 
HETATM 7440 O O   . HOH R 4 .   ? 76.749 98.999  10.303  1.00 37.81 ? 3358 HOH A O   1 
HETATM 7441 O O   . HOH R 4 .   ? 82.135 97.420  8.211   1.00 49.36 ? 3359 HOH A O   1 
HETATM 7442 O O   . HOH R 4 .   ? 79.563 95.818  14.758  1.00 25.55 ? 3360 HOH A O   1 
HETATM 7443 O O   . HOH R 4 .   ? 83.990 87.088  18.283  1.00 43.14 ? 3361 HOH A O   1 
HETATM 7444 O O   . HOH R 4 .   ? 76.710 85.303  11.264  1.00 51.12 ? 3362 HOH A O   1 
HETATM 7445 O O   . HOH R 4 .   ? 73.631 85.655  11.281  1.00 49.77 ? 3363 HOH A O   1 
HETATM 7446 O O   . HOH R 4 .   ? 65.501 80.819  9.935   1.00 50.01 ? 3364 HOH A O   1 
HETATM 7447 O O   . HOH R 4 .   ? 65.321 73.738  6.528   1.00 50.91 ? 3365 HOH A O   1 
HETATM 7448 O O   . HOH R 4 .   ? 63.124 71.902  6.017   1.00 34.66 ? 3366 HOH A O   1 
HETATM 7449 O O   . HOH R 4 .   ? 62.805 70.463  8.130   1.00 44.13 ? 3367 HOH A O   1 
HETATM 7450 O O   . HOH R 4 .   ? 64.520 70.135  3.634   1.00 63.04 ? 3368 HOH A O   1 
HETATM 7451 O O   . HOH R 4 .   ? 57.648 66.146  5.501   1.00 43.22 ? 3369 HOH A O   1 
HETATM 7452 O O   . HOH R 4 .   ? 52.952 67.825  5.856   1.00 36.91 ? 3370 HOH A O   1 
HETATM 7453 O O   . HOH R 4 .   ? 51.112 69.576  6.326   1.00 43.25 ? 3371 HOH A O   1 
HETATM 7454 O O   . HOH R 4 .   ? 50.702 69.304  3.296   1.00 25.82 ? 3372 HOH A O   1 
HETATM 7455 O O   . HOH R 4 .   ? 43.909 65.775  4.501   1.00 33.58 ? 3373 HOH A O   1 
HETATM 7456 O O   . HOH R 4 .   ? 47.091 59.646  2.191   1.00 32.95 ? 3374 HOH A O   1 
HETATM 7457 O O   . HOH R 4 .   ? 51.329 57.932  -0.806  1.00 45.59 ? 3375 HOH A O   1 
HETATM 7458 O O   . HOH R 4 .   ? 51.220 64.694  -7.204  1.00 43.34 ? 3376 HOH A O   1 
HETATM 7459 O O   . HOH R 4 .   ? 43.918 65.824  -8.971  1.00 48.93 ? 3377 HOH A O   1 
HETATM 7460 O O   . HOH R 4 .   ? 42.631 59.841  -4.726  1.00 54.38 ? 3378 HOH A O   1 
HETATM 7461 O O   . HOH R 4 .   ? 39.173 69.343  -0.138  1.00 46.33 ? 3379 HOH A O   1 
HETATM 7462 O O   . HOH R 4 .   ? 38.929 73.924  8.034   1.00 40.33 ? 3380 HOH A O   1 
HETATM 7463 O O   . HOH R 4 .   ? 34.758 81.254  1.970   1.00 38.79 ? 3381 HOH A O   1 
HETATM 7464 O O   . HOH R 4 .   ? 32.061 81.398  3.168   1.00 43.95 ? 3382 HOH A O   1 
HETATM 7465 O O   . HOH R 4 .   ? 37.985 87.089  11.395  1.00 27.25 ? 3383 HOH A O   1 
HETATM 7466 O O   . HOH R 4 .   ? 38.970 90.528  13.714  1.00 33.97 ? 3384 HOH A O   1 
HETATM 7467 O O   . HOH R 4 .   ? 44.479 91.033  11.772  1.00 38.55 ? 3385 HOH A O   1 
HETATM 7468 O O   . HOH R 4 .   ? 48.331 95.049  12.226  1.00 31.47 ? 3386 HOH A O   1 
HETATM 7469 O O   . HOH R 4 .   ? 51.899 95.930  12.303  1.00 20.07 ? 3387 HOH A O   1 
HETATM 7470 O O   . HOH R 4 .   ? 52.100 99.243  14.192  1.00 24.52 ? 3388 HOH A O   1 
HETATM 7471 O O   . HOH R 4 .   ? 51.416 101.906 16.351  1.00 21.31 ? 3389 HOH A O   1 
HETATM 7472 O O   . HOH R 4 .   ? 52.386 104.411 16.150  1.00 24.14 ? 3390 HOH A O   1 
HETATM 7473 O O   . HOH R 4 .   ? 47.775 105.491 14.039  1.00 27.99 ? 3391 HOH A O   1 
HETATM 7474 O O   . HOH R 4 .   ? 45.164 105.584 13.861  1.00 29.96 ? 3392 HOH A O   1 
HETATM 7475 O O   . HOH R 4 .   ? 37.706 105.471 11.111  1.00 43.54 ? 3393 HOH A O   1 
HETATM 7476 O O   . HOH R 4 .   ? 37.179 105.127 18.649  1.00 39.67 ? 3394 HOH A O   1 
HETATM 7477 O O   . HOH R 4 .   ? 41.606 110.315 19.509  1.00 39.48 ? 3395 HOH A O   1 
HETATM 7478 O O   . HOH R 4 .   ? 45.064 99.958  21.188  1.00 28.83 ? 3396 HOH A O   1 
HETATM 7479 O O   . HOH R 4 .   ? 43.000 96.372  18.793  1.00 21.77 ? 3397 HOH A O   1 
HETATM 7480 O O   . HOH R 4 .   ? 41.191 94.070  19.963  1.00 27.42 ? 3398 HOH A O   1 
HETATM 7481 O O   . HOH R 4 .   ? 37.035 92.432  20.190  1.00 32.19 ? 3399 HOH A O   1 
HETATM 7482 O O   . HOH R 4 .   ? 40.188 86.599  21.660  1.00 34.52 ? 3400 HOH A O   1 
HETATM 7483 O O   . HOH R 4 .   ? 40.286 87.281  24.728  1.00 31.93 ? 3401 HOH A O   1 
HETATM 7484 O O   . HOH R 4 .   ? 39.272 86.080  29.288  1.00 36.74 ? 3402 HOH A O   1 
HETATM 7485 O O   . HOH R 4 .   ? 44.271 81.666  28.238  1.00 49.61 ? 3403 HOH A O   1 
HETATM 7486 O O   . HOH R 4 .   ? 46.744 81.398  28.406  1.00 45.07 ? 3404 HOH A O   1 
HETATM 7487 O O   . HOH R 4 .   ? 48.980 79.318  26.457  1.00 33.55 ? 3405 HOH A O   1 
HETATM 7488 O O   . HOH R 4 .   ? 49.545 81.693  25.374  1.00 30.39 ? 3406 HOH A O   1 
HETATM 7489 O O   . HOH R 4 .   ? 52.487 82.470  24.218  1.00 31.09 ? 3407 HOH A O   1 
HETATM 7490 O O   . HOH R 4 .   ? 53.116 83.842  21.856  1.00 20.15 ? 3408 HOH A O   1 
HETATM 7491 O O   . HOH R 4 .   ? 47.034 88.116  18.471  1.00 21.55 ? 3409 HOH A O   1 
HETATM 7492 O O   . HOH R 4 .   ? 49.043 94.355  21.868  1.00 23.81 ? 3410 HOH A O   1 
HETATM 7493 O O   . HOH R 4 .   ? 46.531 87.383  30.162  1.00 41.95 ? 3411 HOH A O   1 
HETATM 7494 O O   . HOH R 4 .   ? 50.582 84.890  34.056  1.00 45.73 ? 3412 HOH A O   1 
HETATM 7495 O O   . HOH R 4 .   ? 48.643 85.025  35.617  1.00 37.29 ? 3413 HOH A O   1 
HETATM 7496 O O   . HOH R 4 .   ? 48.636 85.916  38.485  1.00 41.94 ? 3414 HOH A O   1 
HETATM 7497 O O   . HOH R 4 .   ? 46.947 87.536  39.502  1.00 30.61 ? 3415 HOH A O   1 
HETATM 7498 O O   . HOH R 4 .   ? 42.014 87.341  39.484  1.00 39.02 ? 3416 HOH A O   1 
HETATM 7499 O O   . HOH R 4 .   ? 39.339 91.018  41.885  1.00 44.69 ? 3417 HOH A O   1 
HETATM 7500 O O   . HOH R 4 .   ? 35.499 89.113  39.648  1.00 50.12 ? 3418 HOH A O   1 
HETATM 7501 O O   . HOH R 4 .   ? 33.071 87.640  37.069  1.00 41.59 ? 3419 HOH A O   1 
HETATM 7502 O O   . HOH R 4 .   ? 26.577 89.326  37.653  1.00 44.13 ? 3420 HOH A O   1 
HETATM 7503 O O   . HOH R 4 .   ? 23.529 91.665  36.281  1.00 38.15 ? 3421 HOH A O   1 
HETATM 7504 O O   . HOH R 4 .   ? 20.871 92.511  36.836  1.00 51.94 ? 3422 HOH A O   1 
HETATM 7505 O O   . HOH R 4 .   ? 22.193 90.872  40.536  1.00 51.93 ? 3423 HOH A O   1 
HETATM 7506 O O   . HOH R 4 .   ? 23.222 92.642  42.386  1.00 58.46 ? 3424 HOH A O   1 
HETATM 7507 O O   . HOH R 4 .   ? 22.320 90.571  43.835  1.00 51.89 ? 3425 HOH A O   1 
HETATM 7508 O O   . HOH R 4 .   ? 26.528 97.354  39.118  1.00 38.36 ? 3426 HOH A O   1 
HETATM 7509 O O   . HOH R 4 .   ? 30.478 93.977  40.982  1.00 31.68 ? 3427 HOH A O   1 
HETATM 7510 O O   . HOH R 4 .   ? 31.141 98.028  35.765  1.00 27.83 ? 3428 HOH A O   1 
HETATM 7511 O O   . HOH R 4 .   ? 33.786 97.752  34.898  1.00 29.74 ? 3429 HOH A O   1 
HETATM 7512 O O   . HOH R 4 .   ? 35.849 96.189  35.647  1.00 31.46 ? 3430 HOH A O   1 
HETATM 7513 O O   . HOH R 4 .   ? 35.297 94.678  33.632  1.00 38.24 ? 3431 HOH A O   1 
HETATM 7514 O O   . HOH R 4 .   ? 36.480 94.678  31.022  1.00 33.29 ? 3432 HOH A O   1 
HETATM 7515 O O   . HOH R 4 .   ? 36.666 92.996  28.787  1.00 25.33 ? 3433 HOH A O   1 
HETATM 7516 O O   . HOH R 4 .   ? 41.574 94.557  34.461  1.00 29.20 ? 3434 HOH A O   1 
HETATM 7517 O O   . HOH R 4 .   ? 49.929 92.516  33.721  1.00 34.70 ? 3435 HOH A O   1 
HETATM 7518 O O   . HOH R 4 .   ? 54.465 96.581  33.386  1.00 34.17 ? 3436 HOH A O   1 
HETATM 7519 O O   . HOH R 4 .   ? 58.594 97.627  32.461  1.00 25.34 ? 3437 HOH A O   1 
HETATM 7520 O O   . HOH R 4 .   ? 58.602 104.536 32.175  1.00 20.40 ? 3438 HOH A O   1 
HETATM 7521 O O   . HOH R 4 .   ? 54.856 95.393  42.569  1.00 21.46 ? 3439 HOH A O   1 
HETATM 7522 O O   . HOH R 4 .   ? 54.399 93.824  44.652  1.00 20.67 ? 3440 HOH A O   1 
HETATM 7523 O O   . HOH R 4 .   ? 53.939 95.594  46.673  1.00 23.89 ? 3441 HOH A O   1 
HETATM 7524 O O   . HOH R 4 .   ? 52.004 94.551  48.291  1.00 33.19 ? 3442 HOH A O   1 
HETATM 7525 O O   . HOH R 4 .   ? 53.835 97.503  44.546  1.00 24.47 ? 3443 HOH A O   1 
HETATM 7526 O O   . HOH R 4 .   ? 45.872 98.206  42.922  1.00 36.56 ? 3444 HOH A O   1 
HETATM 7527 O O   . HOH R 4 .   ? 40.322 93.745  47.120  1.00 49.70 ? 3445 HOH A O   1 
HETATM 7528 O O   . HOH R 4 .   ? 39.681 95.362  48.933  1.00 35.57 ? 3446 HOH A O   1 
HETATM 7529 O O   . HOH R 4 .   ? 38.416 96.954  47.426  1.00 32.03 ? 3447 HOH A O   1 
HETATM 7530 O O   . HOH R 4 .   ? 34.707 96.466  46.664  1.00 35.86 ? 3448 HOH A O   1 
HETATM 7531 O O   . HOH R 4 .   ? 37.198 96.464  43.586  1.00 25.46 ? 3449 HOH A O   1 
HETATM 7532 O O   . HOH R 4 .   ? 40.565 93.311  50.282  1.00 46.38 ? 3450 HOH A O   1 
HETATM 7533 O O   . HOH R 4 .   ? 42.472 91.880  49.196  1.00 45.63 ? 3451 HOH A O   1 
HETATM 7534 O O   . HOH R 4 .   ? 43.530 93.411  51.710  1.00 45.34 ? 3452 HOH A O   1 
HETATM 7535 O O   . HOH R 4 .   ? 47.390 90.494  46.850  1.00 29.68 ? 3453 HOH A O   1 
HETATM 7536 O O   . HOH R 4 .   ? 54.950 89.834  50.917  1.00 35.10 ? 3454 HOH A O   1 
HETATM 7537 O O   . HOH R 4 .   ? 56.321 92.992  52.391  1.00 43.31 ? 3455 HOH A O   1 
HETATM 7538 O O   . HOH R 4 .   ? 55.721 101.778 54.934  1.00 43.88 ? 3456 HOH A O   1 
HETATM 7539 O O   . HOH R 4 .   ? 48.619 98.122  55.986  1.00 55.14 ? 3457 HOH A O   1 
HETATM 7540 O O   . HOH R 4 .   ? 42.178 101.528 53.871  1.00 36.56 ? 3458 HOH A O   1 
HETATM 7541 O O   . HOH R 4 .   ? 39.624 98.584  55.355  1.00 50.78 ? 3459 HOH A O   1 
HETATM 7542 O O   . HOH R 4 .   ? 37.555 102.479 56.007  1.00 45.07 ? 3460 HOH A O   1 
HETATM 7543 O O   . HOH R 4 .   ? 35.058 102.238 56.732  1.00 56.31 ? 3461 HOH A O   1 
HETATM 7544 O O   . HOH R 4 .   ? 36.509 95.425  53.622  1.00 48.68 ? 3462 HOH A O   1 
HETATM 7545 O O   . HOH R 4 .   ? 32.734 98.798  50.395  1.00 44.53 ? 3463 HOH A O   1 
HETATM 7546 O O   . HOH R 4 .   ? 37.288 103.561 36.775  1.00 33.18 ? 3464 HOH A O   1 
HETATM 7547 O O   . HOH R 4 .   ? 34.948 99.047  20.200  1.00 32.93 ? 3465 HOH A O   1 
HETATM 7548 O O   . HOH R 4 .   ? 27.219 94.750  24.859  1.00 26.07 ? 3466 HOH A O   1 
HETATM 7549 O O   . HOH R 4 .   ? 39.442 83.735  20.911  1.00 32.19 ? 3467 HOH A O   1 
HETATM 7550 O O   . HOH R 4 .   ? 42.224 82.555  20.747  1.00 28.29 ? 3468 HOH A O   1 
HETATM 7551 O O   . HOH R 4 .   ? 43.298 78.656  27.296  1.00 45.82 ? 3469 HOH A O   1 
HETATM 7552 O O   . HOH R 4 .   ? 39.021 75.888  25.518  1.00 54.43 ? 3470 HOH A O   1 
HETATM 7553 O O   . HOH R 4 .   ? 39.194 73.873  22.316  1.00 42.91 ? 3471 HOH A O   1 
HETATM 7554 O O   . HOH R 4 .   ? 48.462 72.744  32.183  1.00 46.83 ? 3472 HOH A O   1 
HETATM 7555 O O   . HOH R 4 .   ? 54.659 81.495  43.752  1.00 38.39 ? 3473 HOH A O   1 
HETATM 7556 O O   . HOH R 4 .   ? 56.847 88.385  44.210  1.00 28.62 ? 3474 HOH A O   1 
HETATM 7557 O O   . HOH R 4 .   ? 55.036 88.382  40.875  1.00 18.69 ? 3475 HOH A O   1 
HETATM 7558 O O   . HOH R 4 .   ? 48.809 113.200 54.582  1.00 47.14 ? 3476 HOH A O   1 
HETATM 7559 O O   . HOH R 4 .   ? 65.301 117.643 50.186  1.00 62.36 ? 3477 HOH A O   1 
HETATM 7560 O O   . HOH R 4 .   ? 74.581 90.594  -2.181  1.00 52.24 ? 3478 HOH A O   1 
HETATM 7561 O O   . HOH R 4 .   ? 59.100 130.025 26.014  1.00 37.06 ? 3479 HOH A O   1 
HETATM 7562 O O   . HOH R 4 .   ? 58.194 108.448 9.922   1.00 21.70 ? 3480 HOH A O   1 
HETATM 7563 O O   . HOH R 4 .   ? 59.857 108.794 6.124   1.00 50.54 ? 3481 HOH A O   1 
HETATM 7564 O O   . HOH R 4 .   ? 62.794 105.902 3.418   1.00 52.35 ? 3482 HOH A O   1 
HETATM 7565 O O   . HOH R 4 .   ? 55.764 105.357 3.796   1.00 19.69 ? 3483 HOH A O   1 
HETATM 7566 O O   . HOH R 4 .   ? 46.936 111.130 -1.747  1.00 43.80 ? 3484 HOH A O   1 
HETATM 7567 O O   . HOH R 4 .   ? 44.649 108.667 -8.417  1.00 37.07 ? 3485 HOH A O   1 
HETATM 7568 O O   . HOH R 4 .   ? 44.225 106.575 -10.090 1.00 35.25 ? 3486 HOH A O   1 
HETATM 7569 O O   . HOH R 4 .   ? 44.006 104.200 -7.118  1.00 54.79 ? 3487 HOH A O   1 
HETATM 7570 O O   . HOH R 4 .   ? 45.827 102.484 -9.624  1.00 26.30 ? 3488 HOH A O   1 
HETATM 7571 O O   . HOH R 4 .   ? 40.905 100.407 -8.742  1.00 47.07 ? 3489 HOH A O   1 
HETATM 7572 O O   . HOH R 4 .   ? 39.074 100.115 -11.365 1.00 53.68 ? 3490 HOH A O   1 
HETATM 7573 O O   . HOH R 4 .   ? 35.722 96.748  -10.259 1.00 48.72 ? 3491 HOH A O   1 
HETATM 7574 O O   . HOH R 4 .   ? 41.653 96.357  -5.984  1.00 28.65 ? 3492 HOH A O   1 
HETATM 7575 O O   . HOH R 4 .   ? 41.444 96.843  -14.728 1.00 52.83 ? 3493 HOH A O   1 
HETATM 7576 O O   . HOH R 4 .   ? 41.655 95.564  -17.147 1.00 48.41 ? 3494 HOH A O   1 
HETATM 7577 O O   . HOH R 4 .   ? 43.495 93.146  -16.723 1.00 33.70 ? 3495 HOH A O   1 
HETATM 7578 O O   . HOH R 4 .   ? 47.109 80.923  -16.380 1.00 58.76 ? 3496 HOH A O   1 
HETATM 7579 O O   . HOH R 4 .   ? 48.619 82.879  -9.069  1.00 39.06 ? 3497 HOH A O   1 
HETATM 7580 O O   . HOH R 4 .   ? 51.010 84.887  -7.188  1.00 35.14 ? 3498 HOH A O   1 
HETATM 7581 O O   . HOH R 4 .   ? 51.403 83.847  -3.678  1.00 28.01 ? 3499 HOH A O   1 
HETATM 7582 O O   . HOH R 4 .   ? 50.048 81.336  -1.425  1.00 25.97 ? 3500 HOH A O   1 
HETATM 7583 O O   . HOH R 4 .   ? 49.741 77.693  2.368   1.00 29.96 ? 3501 HOH A O   1 
HETATM 7584 O O   . HOH R 4 .   ? 52.143 78.630  3.239   1.00 28.97 ? 3502 HOH A O   1 
HETATM 7585 O O   . HOH R 4 .   ? 53.832 76.413  3.326   1.00 27.50 ? 3503 HOH A O   1 
HETATM 7586 O O   . HOH R 4 .   ? 55.257 80.638  3.505   1.00 31.81 ? 3504 HOH A O   1 
HETATM 7587 O O   . HOH R 4 .   ? 56.616 77.071  -4.858  1.00 32.27 ? 3505 HOH A O   1 
HETATM 7588 O O   . HOH R 4 .   ? 54.114 74.816  -3.855  1.00 30.69 ? 3506 HOH A O   1 
HETATM 7589 O O   . HOH R 4 .   ? 53.047 77.106  -5.535  1.00 46.69 ? 3507 HOH A O   1 
HETATM 7590 O O   . HOH R 4 .   ? 47.823 73.191  -7.356  1.00 42.44 ? 3508 HOH A O   1 
HETATM 7591 O O   . HOH R 4 .   ? 46.844 77.141  2.009   1.00 26.27 ? 3509 HOH A O   1 
HETATM 7592 O O   . HOH R 4 .   ? 40.657 81.238  -4.790  1.00 36.60 ? 3510 HOH A O   1 
HETATM 7593 O O   . HOH R 4 .   ? 54.220 83.991  -12.438 1.00 53.50 ? 3511 HOH A O   1 
HETATM 7594 O O   . HOH R 4 .   ? 63.367 85.722  -6.517  1.00 46.34 ? 3512 HOH A O   1 
HETATM 7595 O O   . HOH R 4 .   ? 63.473 86.259  -4.062  1.00 38.79 ? 3513 HOH A O   1 
HETATM 7596 O O   . HOH R 4 .   ? 62.255 88.170  -2.538  1.00 28.18 ? 3514 HOH A O   1 
HETATM 7597 O O   . HOH R 4 .   ? 66.066 88.129  -3.855  1.00 41.80 ? 3515 HOH A O   1 
HETATM 7598 O O   . HOH R 4 .   ? 67.097 89.103  -6.040  1.00 36.31 ? 3516 HOH A O   1 
HETATM 7599 O O   . HOH R 4 .   ? 66.031 84.279  -1.346  1.00 51.33 ? 3517 HOH A O   1 
HETATM 7600 O O   . HOH R 4 .   ? 63.030 82.568  -1.556  1.00 42.68 ? 3518 HOH A O   1 
HETATM 7601 O O   . HOH R 4 .   ? 62.473 80.854  -3.557  1.00 41.17 ? 3519 HOH A O   1 
HETATM 7602 O O   . HOH R 4 .   ? 52.637 72.218  11.917  1.00 53.04 ? 3520 HOH A O   1 
HETATM 7603 O O   . HOH R 4 .   ? 39.071 101.571 3.011   1.00 41.68 ? 3521 HOH A O   1 
HETATM 7604 O O   . HOH R 4 .   ? 40.688 108.524 3.375   1.00 38.83 ? 3522 HOH A O   1 
HETATM 7605 O O   . HOH R 4 .   ? 43.074 110.654 -9.980  1.00 55.73 ? 3523 HOH A O   1 
HETATM 7606 O O   . HOH R 4 .   ? 56.763 107.379 -11.454 1.00 45.17 ? 3524 HOH A O   1 
HETATM 7607 O O   . HOH R 4 .   ? 60.420 106.529 -11.141 1.00 34.79 ? 3525 HOH A O   1 
HETATM 7608 O O   . HOH R 4 .   ? 72.648 101.029 2.798   1.00 34.96 ? 3526 HOH A O   1 
HETATM 7609 O O   . HOH R 4 .   ? 18.548 103.189 37.426  1.00 54.21 ? 3527 HOH A O   1 
HETATM 7610 O O   . HOH R 4 .   ? 52.576 115.837 21.807  1.00 39.90 ? 3528 HOH A O   1 
HETATM 7611 O O   . HOH R 4 .   ? 73.815 115.795 34.678  1.00 41.07 ? 3529 HOH A O   1 
HETATM 7612 O O   . HOH R 4 .   ? 53.151 116.208 38.703  1.00 53.74 ? 3530 HOH A O   1 
HETATM 7613 O O   . HOH R 4 .   ? 73.113 86.995  27.943  1.00 42.68 ? 3531 HOH A O   1 
HETATM 7614 O O   . HOH R 4 .   ? 53.425 66.744  7.815   1.00 49.55 ? 3532 HOH A O   1 
HETATM 7615 O O   . HOH R 4 .   ? 46.084 92.293  32.240  1.00 44.06 ? 3533 HOH A O   1 
HETATM 7616 O O   . HOH R 4 .   ? 46.776 94.667  9.985   1.00 42.79 ? 3534 HOH A O   1 
HETATM 7617 O O   . HOH R 4 .   ? 44.005 85.483  32.057  1.00 54.50 ? 3535 HOH A O   1 
HETATM 7618 O O   . HOH R 4 .   ? 20.286 99.745  26.117  1.00 51.48 ? 3536 HOH A O   1 
HETATM 7619 O O   . HOH R 4 .   ? 76.648 121.623 16.754  1.00 42.22 ? 3537 HOH A O   1 
HETATM 7620 O O   . HOH R 4 .   ? 51.424 82.455  34.496  1.00 48.87 ? 3538 HOH A O   1 
HETATM 7621 O O   . HOH R 4 .   ? 29.630 78.875  24.730  1.00 48.75 ? 3539 HOH A O   1 
HETATM 7622 O O   . HOH R 4 .   ? 43.657 109.009 52.867  1.00 51.37 ? 3540 HOH A O   1 
HETATM 7623 O O   . HOH R 4 .   ? 95.704 116.888 35.003  1.00 48.58 ? 3541 HOH A O   1 
HETATM 7624 O O   . HOH R 4 .   ? 44.808 110.104 29.371  1.00 52.17 ? 3542 HOH A O   1 
HETATM 7625 O O   . HOH R 4 .   ? 34.065 106.106 20.108  1.00 50.89 ? 3543 HOH A O   1 
HETATM 7626 O O   . HOH R 4 .   ? 57.617 69.366  -9.389  1.00 54.13 ? 3544 HOH A O   1 
HETATM 7627 O O   . HOH R 4 .   ? 66.672 98.231  -11.978 1.00 50.23 ? 3545 HOH A O   1 
HETATM 7628 O O   . HOH R 4 .   ? 67.650 84.008  16.668  1.00 48.57 ? 3546 HOH A O   1 
HETATM 7629 O O   . HOH R 4 .   ? 36.509 116.428 35.600  1.00 49.89 ? 3547 HOH A O   1 
HETATM 7630 O O   . HOH R 4 .   ? 91.343 100.859 25.394  1.00 55.99 ? 3548 HOH A O   1 
HETATM 7631 O O   . HOH R 4 .   ? 93.203 113.602 16.487  1.00 54.37 ? 3549 HOH A O   1 
HETATM 7632 O O   . HOH R 4 .   ? 88.079 116.221 20.476  1.00 56.56 ? 3550 HOH A O   1 
HETATM 7633 O O   . HOH R 4 .   ? 55.654 115.721 36.781  1.00 48.44 ? 3551 HOH A O   1 
HETATM 7634 O O   . HOH R 4 .   ? 62.237 87.040  48.025  1.00 63.85 ? 3552 HOH A O   1 
HETATM 7635 O O   . HOH R 4 .   ? 37.163 82.634  32.251  1.00 50.07 ? 3553 HOH A O   1 
HETATM 7636 O O   . HOH R 4 .   ? 40.081 84.402  30.991  1.00 53.80 ? 3554 HOH A O   1 
HETATM 7637 O O   . HOH R 4 .   ? 39.032 116.502 40.730  1.00 57.15 ? 3555 HOH A O   1 
HETATM 7638 O O   . HOH R 4 .   ? 56.621 120.338 13.306  1.00 52.83 ? 3556 HOH A O   1 
HETATM 7639 O O   . HOH R 4 .   ? 21.920 90.122  24.476  1.00 51.99 ? 3557 HOH A O   1 
HETATM 7640 O O   . HOH R 4 .   ? 38.040 89.757  -15.233 1.00 67.93 ? 3558 HOH A O   1 
HETATM 7641 O O   . HOH R 4 .   ? 54.439 116.534 14.332  1.00 59.37 ? 3559 HOH A O   1 
HETATM 7642 O O   . HOH R 4 .   ? 41.363 100.931 -13.979 1.00 44.13 ? 3560 HOH A O   1 
HETATM 7643 O O   . HOH R 4 .   ? 27.647 93.072  37.061  1.00 42.43 ? 3561 HOH A O   1 
HETATM 7644 O O   . HOH R 4 .   ? 44.854 97.037  55.443  1.00 46.87 ? 3562 HOH A O   1 
HETATM 7645 O O   . HOH R 4 .   ? 64.117 69.799  -2.545  1.00 51.73 ? 3563 HOH A O   1 
HETATM 7646 O O   . HOH R 4 .   ? 59.889 91.078  49.069  1.00 43.01 ? 3564 HOH A O   1 
HETATM 7647 O O   . HOH R 4 .   ? 40.720 100.580 -2.355  1.00 59.95 ? 3565 HOH A O   1 
HETATM 7648 O O   . HOH R 4 .   ? 23.526 109.345 28.967  1.00 55.96 ? 3566 HOH A O   1 
HETATM 7649 O O   . HOH R 4 .   ? 64.274 65.804  8.420   1.00 53.28 ? 3567 HOH A O   1 
HETATM 7650 O O   . HOH R 4 .   ? 56.247 89.109  -11.924 1.00 53.70 ? 3568 HOH A O   1 
HETATM 7651 O O   . HOH R 4 .   ? 54.813 119.134 44.407  1.00 54.07 ? 3569 HOH A O   1 
HETATM 7652 O O   . HOH R 4 .   ? 53.222 112.499 14.708  1.00 54.57 ? 3570 HOH A O   1 
HETATM 7653 O O   . HOH R 4 .   ? 45.120 91.844  50.222  1.00 50.77 ? 3571 HOH A O   1 
HETATM 7654 O O   . HOH R 4 .   ? 82.334 110.781 35.932  1.00 54.59 ? 3572 HOH A O   1 
HETATM 7655 O O   . HOH R 4 .   ? 42.656 117.666 34.286  1.00 43.70 ? 3573 HOH A O   1 
HETATM 7656 O O   . HOH R 4 .   ? 63.306 107.274 5.860   1.00 45.71 ? 3574 HOH A O   1 
HETATM 7657 O O   . HOH R 4 .   ? 77.979 89.646  5.505   1.00 47.29 ? 3575 HOH A O   1 
HETATM 7658 O O   . HOH R 4 .   ? 39.712 116.538 45.672  1.00 50.53 ? 3576 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 NAG 1   2001 2001 NAG NAG A . 
C 2 NAG 2   2002 2002 NAG NAG A . 
D 2 NAG 1   2003 2003 NAG NAG A . 
E 2 NAG 2   2004 2004 NAG NAG A . 
F 2 NAG 1   2005 2005 NAG NAG A . 
G 3 GOL 1   3001 3001 GOL GOL A . 
H 3 GOL 1   3002 3002 GOL GOL A . 
I 3 GOL 1   3003 3003 GOL GOL A . 
J 3 GOL 1   3004 3004 GOL GOL A . 
K 3 GOL 1   3005 3005 GOL GOL A . 
L 3 GOL 1   3006 3006 GOL GOL A . 
M 3 GOL 1   3007 3007 GOL GOL A . 
N 3 GOL 1   3008 3008 GOL GOL A . 
O 3 GOL 1   3009 3009 GOL GOL A . 
P 3 GOL 1   3010 3010 GOL GOL A . 
Q 3 GOL 1   3011 3011 GOL GOL A . 
R 4 HOH 1   3012 1    HOH HOH A . 
R 4 HOH 2   3013 2    HOH HOH A . 
R 4 HOH 3   3014 3    HOH HOH A . 
R 4 HOH 4   3015 4    HOH HOH A . 
R 4 HOH 5   3016 5    HOH HOH A . 
R 4 HOH 6   3017 6    HOH HOH A . 
R 4 HOH 7   3018 7    HOH HOH A . 
R 4 HOH 8   3019 8    HOH HOH A . 
R 4 HOH 9   3020 9    HOH HOH A . 
R 4 HOH 10  3021 10   HOH HOH A . 
R 4 HOH 11  3022 11   HOH HOH A . 
R 4 HOH 12  3023 12   HOH HOH A . 
R 4 HOH 13  3024 13   HOH HOH A . 
R 4 HOH 14  3025 14   HOH HOH A . 
R 4 HOH 15  3026 15   HOH HOH A . 
R 4 HOH 16  3027 16   HOH HOH A . 
R 4 HOH 17  3028 17   HOH HOH A . 
R 4 HOH 18  3029 18   HOH HOH A . 
R 4 HOH 19  3030 19   HOH HOH A . 
R 4 HOH 20  3031 20   HOH HOH A . 
R 4 HOH 21  3032 21   HOH HOH A . 
R 4 HOH 22  3033 22   HOH HOH A . 
R 4 HOH 23  3034 23   HOH HOH A . 
R 4 HOH 24  3035 24   HOH HOH A . 
R 4 HOH 25  3036 25   HOH HOH A . 
R 4 HOH 26  3037 26   HOH HOH A . 
R 4 HOH 27  3038 28   HOH HOH A . 
R 4 HOH 28  3039 29   HOH HOH A . 
R 4 HOH 29  3040 30   HOH HOH A . 
R 4 HOH 30  3041 31   HOH HOH A . 
R 4 HOH 31  3042 32   HOH HOH A . 
R 4 HOH 32  3043 33   HOH HOH A . 
R 4 HOH 33  3044 34   HOH HOH A . 
R 4 HOH 34  3045 35   HOH HOH A . 
R 4 HOH 35  3046 36   HOH HOH A . 
R 4 HOH 36  3047 37   HOH HOH A . 
R 4 HOH 37  3048 38   HOH HOH A . 
R 4 HOH 38  3049 40   HOH HOH A . 
R 4 HOH 39  3050 41   HOH HOH A . 
R 4 HOH 40  3051 42   HOH HOH A . 
R 4 HOH 41  3052 43   HOH HOH A . 
R 4 HOH 42  3053 45   HOH HOH A . 
R 4 HOH 43  3054 46   HOH HOH A . 
R 4 HOH 44  3055 47   HOH HOH A . 
R 4 HOH 45  3056 48   HOH HOH A . 
R 4 HOH 46  3057 49   HOH HOH A . 
R 4 HOH 47  3058 50   HOH HOH A . 
R 4 HOH 48  3059 51   HOH HOH A . 
R 4 HOH 49  3060 52   HOH HOH A . 
R 4 HOH 50  3061 53   HOH HOH A . 
R 4 HOH 51  3062 54   HOH HOH A . 
R 4 HOH 52  3063 55   HOH HOH A . 
R 4 HOH 53  3064 56   HOH HOH A . 
R 4 HOH 54  3065 57   HOH HOH A . 
R 4 HOH 55  3066 58   HOH HOH A . 
R 4 HOH 56  3067 59   HOH HOH A . 
R 4 HOH 57  3068 60   HOH HOH A . 
R 4 HOH 58  3069 62   HOH HOH A . 
R 4 HOH 59  3070 63   HOH HOH A . 
R 4 HOH 60  3071 64   HOH HOH A . 
R 4 HOH 61  3072 65   HOH HOH A . 
R 4 HOH 62  3073 66   HOH HOH A . 
R 4 HOH 63  3074 67   HOH HOH A . 
R 4 HOH 64  3075 68   HOH HOH A . 
R 4 HOH 65  3076 69   HOH HOH A . 
R 4 HOH 66  3077 71   HOH HOH A . 
R 4 HOH 67  3078 72   HOH HOH A . 
R 4 HOH 68  3079 73   HOH HOH A . 
R 4 HOH 69  3080 75   HOH HOH A . 
R 4 HOH 70  3081 76   HOH HOH A . 
R 4 HOH 71  3082 77   HOH HOH A . 
R 4 HOH 72  3083 79   HOH HOH A . 
R 4 HOH 73  3084 80   HOH HOH A . 
R 4 HOH 74  3085 81   HOH HOH A . 
R 4 HOH 75  3086 82   HOH HOH A . 
R 4 HOH 76  3087 83   HOH HOH A . 
R 4 HOH 77  3088 84   HOH HOH A . 
R 4 HOH 78  3089 85   HOH HOH A . 
R 4 HOH 79  3090 86   HOH HOH A . 
R 4 HOH 80  3091 87   HOH HOH A . 
R 4 HOH 81  3092 88   HOH HOH A . 
R 4 HOH 82  3093 89   HOH HOH A . 
R 4 HOH 83  3094 90   HOH HOH A . 
R 4 HOH 84  3095 91   HOH HOH A . 
R 4 HOH 85  3096 92   HOH HOH A . 
R 4 HOH 86  3097 95   HOH HOH A . 
R 4 HOH 87  3098 96   HOH HOH A . 
R 4 HOH 88  3099 97   HOH HOH A . 
R 4 HOH 89  3100 98   HOH HOH A . 
R 4 HOH 90  3101 99   HOH HOH A . 
R 4 HOH 91  3102 100  HOH HOH A . 
R 4 HOH 92  3103 101  HOH HOH A . 
R 4 HOH 93  3104 102  HOH HOH A . 
R 4 HOH 94  3105 103  HOH HOH A . 
R 4 HOH 95  3106 104  HOH HOH A . 
R 4 HOH 96  3107 105  HOH HOH A . 
R 4 HOH 97  3108 106  HOH HOH A . 
R 4 HOH 98  3109 107  HOH HOH A . 
R 4 HOH 99  3110 108  HOH HOH A . 
R 4 HOH 100 3111 109  HOH HOH A . 
R 4 HOH 101 3112 111  HOH HOH A . 
R 4 HOH 102 3113 112  HOH HOH A . 
R 4 HOH 103 3114 113  HOH HOH A . 
R 4 HOH 104 3115 114  HOH HOH A . 
R 4 HOH 105 3116 115  HOH HOH A . 
R 4 HOH 106 3117 117  HOH HOH A . 
R 4 HOH 107 3118 118  HOH HOH A . 
R 4 HOH 108 3119 121  HOH HOH A . 
R 4 HOH 109 3120 122  HOH HOH A . 
R 4 HOH 110 3121 123  HOH HOH A . 
R 4 HOH 111 3122 124  HOH HOH A . 
R 4 HOH 112 3123 125  HOH HOH A . 
R 4 HOH 113 3124 126  HOH HOH A . 
R 4 HOH 114 3125 127  HOH HOH A . 
R 4 HOH 115 3126 128  HOH HOH A . 
R 4 HOH 116 3127 129  HOH HOH A . 
R 4 HOH 117 3128 130  HOH HOH A . 
R 4 HOH 118 3129 131  HOH HOH A . 
R 4 HOH 119 3130 132  HOH HOH A . 
R 4 HOH 120 3131 133  HOH HOH A . 
R 4 HOH 121 3132 134  HOH HOH A . 
R 4 HOH 122 3133 135  HOH HOH A . 
R 4 HOH 123 3134 136  HOH HOH A . 
R 4 HOH 124 3135 137  HOH HOH A . 
R 4 HOH 125 3136 138  HOH HOH A . 
R 4 HOH 126 3137 139  HOH HOH A . 
R 4 HOH 127 3138 140  HOH HOH A . 
R 4 HOH 128 3139 141  HOH HOH A . 
R 4 HOH 129 3140 142  HOH HOH A . 
R 4 HOH 130 3141 144  HOH HOH A . 
R 4 HOH 131 3142 145  HOH HOH A . 
R 4 HOH 132 3143 146  HOH HOH A . 
R 4 HOH 133 3144 147  HOH HOH A . 
R 4 HOH 134 3145 148  HOH HOH A . 
R 4 HOH 135 3146 149  HOH HOH A . 
R 4 HOH 136 3147 150  HOH HOH A . 
R 4 HOH 137 3148 151  HOH HOH A . 
R 4 HOH 138 3149 152  HOH HOH A . 
R 4 HOH 139 3150 153  HOH HOH A . 
R 4 HOH 140 3151 154  HOH HOH A . 
R 4 HOH 141 3152 155  HOH HOH A . 
R 4 HOH 142 3153 156  HOH HOH A . 
R 4 HOH 143 3154 157  HOH HOH A . 
R 4 HOH 144 3155 158  HOH HOH A . 
R 4 HOH 145 3156 159  HOH HOH A . 
R 4 HOH 146 3157 160  HOH HOH A . 
R 4 HOH 147 3158 161  HOH HOH A . 
R 4 HOH 148 3159 162  HOH HOH A . 
R 4 HOH 149 3160 163  HOH HOH A . 
R 4 HOH 150 3161 164  HOH HOH A . 
R 4 HOH 151 3162 165  HOH HOH A . 
R 4 HOH 152 3163 166  HOH HOH A . 
R 4 HOH 153 3164 167  HOH HOH A . 
R 4 HOH 154 3165 168  HOH HOH A . 
R 4 HOH 155 3166 169  HOH HOH A . 
R 4 HOH 156 3167 170  HOH HOH A . 
R 4 HOH 157 3168 171  HOH HOH A . 
R 4 HOH 158 3169 172  HOH HOH A . 
R 4 HOH 159 3170 173  HOH HOH A . 
R 4 HOH 160 3171 174  HOH HOH A . 
R 4 HOH 161 3172 175  HOH HOH A . 
R 4 HOH 162 3173 176  HOH HOH A . 
R 4 HOH 163 3174 177  HOH HOH A . 
R 4 HOH 164 3175 178  HOH HOH A . 
R 4 HOH 165 3176 179  HOH HOH A . 
R 4 HOH 166 3177 180  HOH HOH A . 
R 4 HOH 167 3178 181  HOH HOH A . 
R 4 HOH 168 3179 182  HOH HOH A . 
R 4 HOH 169 3180 184  HOH HOH A . 
R 4 HOH 170 3181 185  HOH HOH A . 
R 4 HOH 171 3182 186  HOH HOH A . 
R 4 HOH 172 3183 187  HOH HOH A . 
R 4 HOH 173 3184 188  HOH HOH A . 
R 4 HOH 174 3185 189  HOH HOH A . 
R 4 HOH 175 3186 190  HOH HOH A . 
R 4 HOH 176 3187 191  HOH HOH A . 
R 4 HOH 177 3188 192  HOH HOH A . 
R 4 HOH 178 3189 193  HOH HOH A . 
R 4 HOH 179 3190 194  HOH HOH A . 
R 4 HOH 180 3191 195  HOH HOH A . 
R 4 HOH 181 3192 196  HOH HOH A . 
R 4 HOH 182 3193 197  HOH HOH A . 
R 4 HOH 183 3194 198  HOH HOH A . 
R 4 HOH 184 3195 199  HOH HOH A . 
R 4 HOH 185 3196 200  HOH HOH A . 
R 4 HOH 186 3197 201  HOH HOH A . 
R 4 HOH 187 3198 202  HOH HOH A . 
R 4 HOH 188 3199 203  HOH HOH A . 
R 4 HOH 189 3200 204  HOH HOH A . 
R 4 HOH 190 3201 206  HOH HOH A . 
R 4 HOH 191 3202 207  HOH HOH A . 
R 4 HOH 192 3203 208  HOH HOH A . 
R 4 HOH 193 3204 209  HOH HOH A . 
R 4 HOH 194 3205 210  HOH HOH A . 
R 4 HOH 195 3206 211  HOH HOH A . 
R 4 HOH 196 3207 212  HOH HOH A . 
R 4 HOH 197 3208 213  HOH HOH A . 
R 4 HOH 198 3209 214  HOH HOH A . 
R 4 HOH 199 3210 215  HOH HOH A . 
R 4 HOH 200 3211 216  HOH HOH A . 
R 4 HOH 201 3212 217  HOH HOH A . 
R 4 HOH 202 3213 218  HOH HOH A . 
R 4 HOH 203 3214 219  HOH HOH A . 
R 4 HOH 204 3215 220  HOH HOH A . 
R 4 HOH 205 3216 221  HOH HOH A . 
R 4 HOH 206 3217 222  HOH HOH A . 
R 4 HOH 207 3218 223  HOH HOH A . 
R 4 HOH 208 3219 224  HOH HOH A . 
R 4 HOH 209 3220 226  HOH HOH A . 
R 4 HOH 210 3221 227  HOH HOH A . 
R 4 HOH 211 3222 228  HOH HOH A . 
R 4 HOH 212 3223 229  HOH HOH A . 
R 4 HOH 213 3224 230  HOH HOH A . 
R 4 HOH 214 3225 231  HOH HOH A . 
R 4 HOH 215 3226 232  HOH HOH A . 
R 4 HOH 216 3227 233  HOH HOH A . 
R 4 HOH 217 3228 234  HOH HOH A . 
R 4 HOH 218 3229 235  HOH HOH A . 
R 4 HOH 219 3230 237  HOH HOH A . 
R 4 HOH 220 3231 238  HOH HOH A . 
R 4 HOH 221 3232 239  HOH HOH A . 
R 4 HOH 222 3233 242  HOH HOH A . 
R 4 HOH 223 3234 243  HOH HOH A . 
R 4 HOH 224 3235 244  HOH HOH A . 
R 4 HOH 225 3236 245  HOH HOH A . 
R 4 HOH 226 3237 246  HOH HOH A . 
R 4 HOH 227 3238 247  HOH HOH A . 
R 4 HOH 228 3239 248  HOH HOH A . 
R 4 HOH 229 3240 249  HOH HOH A . 
R 4 HOH 230 3241 250  HOH HOH A . 
R 4 HOH 231 3242 251  HOH HOH A . 
R 4 HOH 232 3243 252  HOH HOH A . 
R 4 HOH 233 3244 253  HOH HOH A . 
R 4 HOH 234 3245 254  HOH HOH A . 
R 4 HOH 235 3246 255  HOH HOH A . 
R 4 HOH 236 3247 256  HOH HOH A . 
R 4 HOH 237 3248 257  HOH HOH A . 
R 4 HOH 238 3249 258  HOH HOH A . 
R 4 HOH 239 3250 259  HOH HOH A . 
R 4 HOH 240 3251 260  HOH HOH A . 
R 4 HOH 241 3252 261  HOH HOH A . 
R 4 HOH 242 3253 263  HOH HOH A . 
R 4 HOH 243 3254 264  HOH HOH A . 
R 4 HOH 244 3255 266  HOH HOH A . 
R 4 HOH 245 3256 267  HOH HOH A . 
R 4 HOH 246 3257 268  HOH HOH A . 
R 4 HOH 247 3258 269  HOH HOH A . 
R 4 HOH 248 3259 270  HOH HOH A . 
R 4 HOH 249 3260 271  HOH HOH A . 
R 4 HOH 250 3261 272  HOH HOH A . 
R 4 HOH 251 3262 273  HOH HOH A . 
R 4 HOH 252 3263 274  HOH HOH A . 
R 4 HOH 253 3264 275  HOH HOH A . 
R 4 HOH 254 3265 276  HOH HOH A . 
R 4 HOH 255 3266 277  HOH HOH A . 
R 4 HOH 256 3267 278  HOH HOH A . 
R 4 HOH 257 3268 279  HOH HOH A . 
R 4 HOH 258 3269 280  HOH HOH A . 
R 4 HOH 259 3270 281  HOH HOH A . 
R 4 HOH 260 3271 282  HOH HOH A . 
R 4 HOH 261 3272 283  HOH HOH A . 
R 4 HOH 262 3273 284  HOH HOH A . 
R 4 HOH 263 3274 285  HOH HOH A . 
R 4 HOH 264 3275 288  HOH HOH A . 
R 4 HOH 265 3276 289  HOH HOH A . 
R 4 HOH 266 3277 290  HOH HOH A . 
R 4 HOH 267 3278 291  HOH HOH A . 
R 4 HOH 268 3279 292  HOH HOH A . 
R 4 HOH 269 3280 293  HOH HOH A . 
R 4 HOH 270 3281 295  HOH HOH A . 
R 4 HOH 271 3282 296  HOH HOH A . 
R 4 HOH 272 3283 297  HOH HOH A . 
R 4 HOH 273 3284 299  HOH HOH A . 
R 4 HOH 274 3285 300  HOH HOH A . 
R 4 HOH 275 3286 301  HOH HOH A . 
R 4 HOH 276 3287 303  HOH HOH A . 
R 4 HOH 277 3288 304  HOH HOH A . 
R 4 HOH 278 3289 305  HOH HOH A . 
R 4 HOH 279 3290 306  HOH HOH A . 
R 4 HOH 280 3291 307  HOH HOH A . 
R 4 HOH 281 3292 308  HOH HOH A . 
R 4 HOH 282 3293 309  HOH HOH A . 
R 4 HOH 283 3294 310  HOH HOH A . 
R 4 HOH 284 3295 311  HOH HOH A . 
R 4 HOH 285 3296 312  HOH HOH A . 
R 4 HOH 286 3297 313  HOH HOH A . 
R 4 HOH 287 3298 314  HOH HOH A . 
R 4 HOH 288 3299 315  HOH HOH A . 
R 4 HOH 289 3300 316  HOH HOH A . 
R 4 HOH 290 3301 317  HOH HOH A . 
R 4 HOH 291 3302 318  HOH HOH A . 
R 4 HOH 292 3303 319  HOH HOH A . 
R 4 HOH 293 3304 320  HOH HOH A . 
R 4 HOH 294 3305 321  HOH HOH A . 
R 4 HOH 295 3306 322  HOH HOH A . 
R 4 HOH 296 3307 323  HOH HOH A . 
R 4 HOH 297 3308 324  HOH HOH A . 
R 4 HOH 298 3309 325  HOH HOH A . 
R 4 HOH 299 3310 326  HOH HOH A . 
R 4 HOH 300 3311 327  HOH HOH A . 
R 4 HOH 301 3312 328  HOH HOH A . 
R 4 HOH 302 3313 329  HOH HOH A . 
R 4 HOH 303 3314 330  HOH HOH A . 
R 4 HOH 304 3315 331  HOH HOH A . 
R 4 HOH 305 3316 332  HOH HOH A . 
R 4 HOH 306 3317 333  HOH HOH A . 
R 4 HOH 307 3318 334  HOH HOH A . 
R 4 HOH 308 3319 335  HOH HOH A . 
R 4 HOH 309 3320 336  HOH HOH A . 
R 4 HOH 310 3321 337  HOH HOH A . 
R 4 HOH 311 3322 339  HOH HOH A . 
R 4 HOH 312 3323 340  HOH HOH A . 
R 4 HOH 313 3324 341  HOH HOH A . 
R 4 HOH 314 3325 342  HOH HOH A . 
R 4 HOH 315 3326 343  HOH HOH A . 
R 4 HOH 316 3327 344  HOH HOH A . 
R 4 HOH 317 3328 345  HOH HOH A . 
R 4 HOH 318 3329 346  HOH HOH A . 
R 4 HOH 319 3330 347  HOH HOH A . 
R 4 HOH 320 3331 348  HOH HOH A . 
R 4 HOH 321 3332 349  HOH HOH A . 
R 4 HOH 322 3333 350  HOH HOH A . 
R 4 HOH 323 3334 351  HOH HOH A . 
R 4 HOH 324 3335 352  HOH HOH A . 
R 4 HOH 325 3336 353  HOH HOH A . 
R 4 HOH 326 3337 355  HOH HOH A . 
R 4 HOH 327 3338 356  HOH HOH A . 
R 4 HOH 328 3339 357  HOH HOH A . 
R 4 HOH 329 3340 358  HOH HOH A . 
R 4 HOH 330 3341 359  HOH HOH A . 
R 4 HOH 331 3342 360  HOH HOH A . 
R 4 HOH 332 3343 361  HOH HOH A . 
R 4 HOH 333 3344 362  HOH HOH A . 
R 4 HOH 334 3345 363  HOH HOH A . 
R 4 HOH 335 3346 364  HOH HOH A . 
R 4 HOH 336 3347 365  HOH HOH A . 
R 4 HOH 337 3348 366  HOH HOH A . 
R 4 HOH 338 3349 367  HOH HOH A . 
R 4 HOH 339 3350 368  HOH HOH A . 
R 4 HOH 340 3351 369  HOH HOH A . 
R 4 HOH 341 3352 370  HOH HOH A . 
R 4 HOH 342 3353 371  HOH HOH A . 
R 4 HOH 343 3354 372  HOH HOH A . 
R 4 HOH 344 3355 373  HOH HOH A . 
R 4 HOH 345 3356 374  HOH HOH A . 
R 4 HOH 346 3357 377  HOH HOH A . 
R 4 HOH 347 3358 378  HOH HOH A . 
R 4 HOH 348 3359 379  HOH HOH A . 
R 4 HOH 349 3360 380  HOH HOH A . 
R 4 HOH 350 3361 381  HOH HOH A . 
R 4 HOH 351 3362 382  HOH HOH A . 
R 4 HOH 352 3363 383  HOH HOH A . 
R 4 HOH 353 3364 384  HOH HOH A . 
R 4 HOH 354 3365 386  HOH HOH A . 
R 4 HOH 355 3366 388  HOH HOH A . 
R 4 HOH 356 3367 389  HOH HOH A . 
R 4 HOH 357 3368 390  HOH HOH A . 
R 4 HOH 358 3369 391  HOH HOH A . 
R 4 HOH 359 3370 392  HOH HOH A . 
R 4 HOH 360 3371 393  HOH HOH A . 
R 4 HOH 361 3372 394  HOH HOH A . 
R 4 HOH 362 3373 395  HOH HOH A . 
R 4 HOH 363 3374 396  HOH HOH A . 
R 4 HOH 364 3375 397  HOH HOH A . 
R 4 HOH 365 3376 398  HOH HOH A . 
R 4 HOH 366 3377 399  HOH HOH A . 
R 4 HOH 367 3378 400  HOH HOH A . 
R 4 HOH 368 3379 401  HOH HOH A . 
R 4 HOH 369 3380 402  HOH HOH A . 
R 4 HOH 370 3381 403  HOH HOH A . 
R 4 HOH 371 3382 404  HOH HOH A . 
R 4 HOH 372 3383 405  HOH HOH A . 
R 4 HOH 373 3384 406  HOH HOH A . 
R 4 HOH 374 3385 407  HOH HOH A . 
R 4 HOH 375 3386 408  HOH HOH A . 
R 4 HOH 376 3387 409  HOH HOH A . 
R 4 HOH 377 3388 410  HOH HOH A . 
R 4 HOH 378 3389 411  HOH HOH A . 
R 4 HOH 379 3390 412  HOH HOH A . 
R 4 HOH 380 3391 414  HOH HOH A . 
R 4 HOH 381 3392 415  HOH HOH A . 
R 4 HOH 382 3393 416  HOH HOH A . 
R 4 HOH 383 3394 417  HOH HOH A . 
R 4 HOH 384 3395 419  HOH HOH A . 
R 4 HOH 385 3396 420  HOH HOH A . 
R 4 HOH 386 3397 422  HOH HOH A . 
R 4 HOH 387 3398 423  HOH HOH A . 
R 4 HOH 388 3399 424  HOH HOH A . 
R 4 HOH 389 3400 425  HOH HOH A . 
R 4 HOH 390 3401 426  HOH HOH A . 
R 4 HOH 391 3402 427  HOH HOH A . 
R 4 HOH 392 3403 428  HOH HOH A . 
R 4 HOH 393 3404 429  HOH HOH A . 
R 4 HOH 394 3405 430  HOH HOH A . 
R 4 HOH 395 3406 431  HOH HOH A . 
R 4 HOH 396 3407 432  HOH HOH A . 
R 4 HOH 397 3408 433  HOH HOH A . 
R 4 HOH 398 3409 434  HOH HOH A . 
R 4 HOH 399 3410 435  HOH HOH A . 
R 4 HOH 400 3411 436  HOH HOH A . 
R 4 HOH 401 3412 438  HOH HOH A . 
R 4 HOH 402 3413 439  HOH HOH A . 
R 4 HOH 403 3414 440  HOH HOH A . 
R 4 HOH 404 3415 441  HOH HOH A . 
R 4 HOH 405 3416 442  HOH HOH A . 
R 4 HOH 406 3417 443  HOH HOH A . 
R 4 HOH 407 3418 444  HOH HOH A . 
R 4 HOH 408 3419 445  HOH HOH A . 
R 4 HOH 409 3420 446  HOH HOH A . 
R 4 HOH 410 3421 447  HOH HOH A . 
R 4 HOH 411 3422 448  HOH HOH A . 
R 4 HOH 412 3423 449  HOH HOH A . 
R 4 HOH 413 3424 450  HOH HOH A . 
R 4 HOH 414 3425 451  HOH HOH A . 
R 4 HOH 415 3426 452  HOH HOH A . 
R 4 HOH 416 3427 453  HOH HOH A . 
R 4 HOH 417 3428 454  HOH HOH A . 
R 4 HOH 418 3429 455  HOH HOH A . 
R 4 HOH 419 3430 456  HOH HOH A . 
R 4 HOH 420 3431 457  HOH HOH A . 
R 4 HOH 421 3432 458  HOH HOH A . 
R 4 HOH 422 3433 459  HOH HOH A . 
R 4 HOH 423 3434 460  HOH HOH A . 
R 4 HOH 424 3435 461  HOH HOH A . 
R 4 HOH 425 3436 462  HOH HOH A . 
R 4 HOH 426 3437 463  HOH HOH A . 
R 4 HOH 427 3438 464  HOH HOH A . 
R 4 HOH 428 3439 465  HOH HOH A . 
R 4 HOH 429 3440 466  HOH HOH A . 
R 4 HOH 430 3441 467  HOH HOH A . 
R 4 HOH 431 3442 468  HOH HOH A . 
R 4 HOH 432 3443 469  HOH HOH A . 
R 4 HOH 433 3444 470  HOH HOH A . 
R 4 HOH 434 3445 471  HOH HOH A . 
R 4 HOH 435 3446 472  HOH HOH A . 
R 4 HOH 436 3447 473  HOH HOH A . 
R 4 HOH 437 3448 474  HOH HOH A . 
R 4 HOH 438 3449 475  HOH HOH A . 
R 4 HOH 439 3450 476  HOH HOH A . 
R 4 HOH 440 3451 477  HOH HOH A . 
R 4 HOH 441 3452 478  HOH HOH A . 
R 4 HOH 442 3453 479  HOH HOH A . 
R 4 HOH 443 3454 480  HOH HOH A . 
R 4 HOH 444 3455 481  HOH HOH A . 
R 4 HOH 445 3456 483  HOH HOH A . 
R 4 HOH 446 3457 484  HOH HOH A . 
R 4 HOH 447 3458 485  HOH HOH A . 
R 4 HOH 448 3459 486  HOH HOH A . 
R 4 HOH 449 3460 487  HOH HOH A . 
R 4 HOH 450 3461 488  HOH HOH A . 
R 4 HOH 451 3462 489  HOH HOH A . 
R 4 HOH 452 3463 490  HOH HOH A . 
R 4 HOH 453 3464 491  HOH HOH A . 
R 4 HOH 454 3465 492  HOH HOH A . 
R 4 HOH 455 3466 493  HOH HOH A . 
R 4 HOH 456 3467 494  HOH HOH A . 
R 4 HOH 457 3468 495  HOH HOH A . 
R 4 HOH 458 3469 496  HOH HOH A . 
R 4 HOH 459 3470 497  HOH HOH A . 
R 4 HOH 460 3471 498  HOH HOH A . 
R 4 HOH 461 3472 499  HOH HOH A . 
R 4 HOH 462 3473 500  HOH HOH A . 
R 4 HOH 463 3474 501  HOH HOH A . 
R 4 HOH 464 3475 502  HOH HOH A . 
R 4 HOH 465 3476 503  HOH HOH A . 
R 4 HOH 466 3477 505  HOH HOH A . 
R 4 HOH 467 3478 506  HOH HOH A . 
R 4 HOH 468 3479 507  HOH HOH A . 
R 4 HOH 469 3480 508  HOH HOH A . 
R 4 HOH 470 3481 509  HOH HOH A . 
R 4 HOH 471 3482 510  HOH HOH A . 
R 4 HOH 472 3483 511  HOH HOH A . 
R 4 HOH 473 3484 512  HOH HOH A . 
R 4 HOH 474 3485 513  HOH HOH A . 
R 4 HOH 475 3486 514  HOH HOH A . 
R 4 HOH 476 3487 515  HOH HOH A . 
R 4 HOH 477 3488 516  HOH HOH A . 
R 4 HOH 478 3489 517  HOH HOH A . 
R 4 HOH 479 3490 518  HOH HOH A . 
R 4 HOH 480 3491 519  HOH HOH A . 
R 4 HOH 481 3492 520  HOH HOH A . 
R 4 HOH 482 3493 521  HOH HOH A . 
R 4 HOH 483 3494 522  HOH HOH A . 
R 4 HOH 484 3495 523  HOH HOH A . 
R 4 HOH 485 3496 525  HOH HOH A . 
R 4 HOH 486 3497 526  HOH HOH A . 
R 4 HOH 487 3498 527  HOH HOH A . 
R 4 HOH 488 3499 528  HOH HOH A . 
R 4 HOH 489 3500 529  HOH HOH A . 
R 4 HOH 490 3501 530  HOH HOH A . 
R 4 HOH 491 3502 531  HOH HOH A . 
R 4 HOH 492 3503 532  HOH HOH A . 
R 4 HOH 493 3504 533  HOH HOH A . 
R 4 HOH 494 3505 534  HOH HOH A . 
R 4 HOH 495 3506 535  HOH HOH A . 
R 4 HOH 496 3507 536  HOH HOH A . 
R 4 HOH 497 3508 538  HOH HOH A . 
R 4 HOH 498 3509 539  HOH HOH A . 
R 4 HOH 499 3510 540  HOH HOH A . 
R 4 HOH 500 3511 541  HOH HOH A . 
R 4 HOH 501 3512 543  HOH HOH A . 
R 4 HOH 502 3513 544  HOH HOH A . 
R 4 HOH 503 3514 545  HOH HOH A . 
R 4 HOH 504 3515 551  HOH HOH A . 
R 4 HOH 505 3516 557  HOH HOH A . 
R 4 HOH 506 3517 559  HOH HOH A . 
R 4 HOH 507 3518 566  HOH HOH A . 
R 4 HOH 508 3519 567  HOH HOH A . 
R 4 HOH 509 3520 568  HOH HOH A . 
R 4 HOH 510 3521 575  HOH HOH A . 
R 4 HOH 511 3522 577  HOH HOH A . 
R 4 HOH 512 3523 578  HOH HOH A . 
R 4 HOH 513 3524 579  HOH HOH A . 
R 4 HOH 514 3525 580  HOH HOH A . 
R 4 HOH 515 3526 581  HOH HOH A . 
R 4 HOH 516 3527 582  HOH HOH A . 
R 4 HOH 517 3528 1    HOH HOH A . 
R 4 HOH 518 3529 3    HOH HOH A . 
R 4 HOH 519 3530 4    HOH HOH A . 
R 4 HOH 520 3531 6    HOH HOH A . 
R 4 HOH 521 3532 7    HOH HOH A . 
R 4 HOH 522 3533 9    HOH HOH A . 
R 4 HOH 523 3534 10   HOH HOH A . 
R 4 HOH 524 3535 11   HOH HOH A . 
R 4 HOH 525 3536 15   HOH HOH A . 
R 4 HOH 526 3537 16   HOH HOH A . 
R 4 HOH 527 3538 17   HOH HOH A . 
R 4 HOH 528 3539 18   HOH HOH A . 
R 4 HOH 529 3540 20   HOH HOH A . 
R 4 HOH 530 3541 21   HOH HOH A . 
R 4 HOH 531 3542 22   HOH HOH A . 
R 4 HOH 532 3543 23   HOH HOH A . 
R 4 HOH 533 3544 24   HOH HOH A . 
R 4 HOH 534 3545 25   HOH HOH A . 
R 4 HOH 535 3546 29   HOH HOH A . 
R 4 HOH 536 3547 30   HOH HOH A . 
R 4 HOH 537 3548 35   HOH HOH A . 
R 4 HOH 538 3549 37   HOH HOH A . 
R 4 HOH 539 3550 40   HOH HOH A . 
R 4 HOH 540 3551 42   HOH HOH A . 
R 4 HOH 541 3552 44   HOH HOH A . 
R 4 HOH 542 3553 45   HOH HOH A . 
R 4 HOH 543 3554 46   HOH HOH A . 
R 4 HOH 544 3555 47   HOH HOH A . 
R 4 HOH 545 3556 49   HOH HOH A . 
R 4 HOH 546 3557 53   HOH HOH A . 
R 4 HOH 547 3558 54   HOH HOH A . 
R 4 HOH 548 3559 55   HOH HOH A . 
R 4 HOH 549 3560 56   HOH HOH A . 
R 4 HOH 550 3561 57   HOH HOH A . 
R 4 HOH 551 3562 59   HOH HOH A . 
R 4 HOH 552 3563 60   HOH HOH A . 
R 4 HOH 553 3564 61   HOH HOH A . 
R 4 HOH 554 3565 62   HOH HOH A . 
R 4 HOH 555 3566 63   HOH HOH A . 
R 4 HOH 556 3567 66   HOH HOH A . 
R 4 HOH 557 3568 67   HOH HOH A . 
R 4 HOH 558 3569 68   HOH HOH A . 
R 4 HOH 559 3570 70   HOH HOH A . 
R 4 HOH 560 3571 71   HOH HOH A . 
R 4 HOH 561 3572 72   HOH HOH A . 
R 4 HOH 562 3573 74   HOH HOH A . 
R 4 HOH 563 3574 75   HOH HOH A . 
R 4 HOH 564 3575 2    HOH HOH A . 
R 4 HOH 565 3576 3    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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R 
# 
_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 
SHELXD   phasing           .        ? 5 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             787 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            SG 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            CYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             787 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.699 
_pdbx_validate_rmsd_bond.bond_target_value         1.812 
_pdbx_validate_rmsd_bond.bond_deviation            -0.113 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 624 ? ? CZ A ARG 624 ? ? NH1 A ARG 624 ? ? 123.89 120.30 3.59  0.50 N 
2 1 NE A ARG 624 ? ? CZ A ARG 624 ? ? NH2 A ARG 624 ? ? 115.55 120.30 -4.75 0.50 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 34  ? ? -159.98 87.17   
2  1 SER A 40  ? ? 70.14   -11.01  
3  1 SER A 51  ? ? -109.22 -114.94 
4  1 SER A 74  ? ? -171.59 137.16  
5  1 VAL A 77  ? ? -105.25 -62.89  
6  1 PHE A 78  ? ? -112.95 54.24   
7  1 LEU A 151 ? ? -95.92  -62.11  
8  1 LEU A 180 ? ? 67.35   147.34  
9  1 GLN A 186 ? ? 73.04   -15.35  
10 1 TRP A 194 ? ? 58.48   77.87   
11 1 PHE A 200 ? ? -171.13 117.88  
12 1 ASN A 207 ? ? -119.20 -164.40 
13 1 LEU A 213 ? ? -118.24 -143.54 
14 1 GLU A 300 ? ? 70.92   66.68   
15 1 TYR A 321 ? ? -168.78 97.16   
16 1 VAL A 342 ? ? -93.56  -61.82  
17 1 SER A 394 ? ? -55.40  173.94  
18 1 VAL A 405 ? ? -137.87 -142.00 
19 1 ARG A 471 ? ? -77.38  47.07   
20 1 ASP A 474 ? ? 75.82   -9.68   
21 1 SER A 521 ? ? 54.12   -143.15 
22 1 ILE A 565 ? ? -118.72 71.37   
23 1 CYS A 573 ? ? 78.47   -13.58  
24 1 LEU A 577 ? ? 87.10   150.19  
25 1 VAL A 651 ? ? -105.07 -64.00  
26 1 GLU A 774 ? ? -144.69 -20.90  
27 1 GLN A 793 ? ? -14.93  139.70  
28 1 ASP A 857 ? ? -150.58 79.93   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   HIS 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    50 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    51 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.54 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C5 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     2001 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
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 N-ACETYL-D-GLUCOSAMINE NAG 
3 GLYCEROL               GOL 
4 water                  HOH 
# 
