data_9EJ3
# 
_entry.id   9EJ3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EJ3         pdb_00009ej3 10.2210/pdb9ej3/pdb 
WWPDB D_1000290512 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-09 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EJ3 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ret6@cornell.edu 
_pdbx_contact_author.name_first         Robert 
_pdbx_contact_author.name_last          Thorne 
_pdbx_contact_author.name_mi            E 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7489-8074 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McLeod, M.J.'    1 0000-0001-5540-916X 
'Barwell, S.A.E.' 2 0000-0002-5703-5525 
'Holyoak, T.'     3 0000-0002-7329-1115 
'Thorne, R.E.'    4 0000-0002-7489-8074 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            33 
_citation.language                  ? 
_citation.page_first                924 
_citation.page_last                 934.e2 
_citation.title                     'A structural perspective on the temperature dependent activity of enzymes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2025.02.013 
_citation.pdbx_database_id_PubMed   40120576 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McLeod, M.J.'    1 ? 
primary 'Barwell, S.A.E.' 2 ? 
primary 'Holyoak, T.'     3 ? 
primary 'Thorne, R.E.'    4 ? 
# 
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 'Phosphoenolpyruvate carboxykinase, cytosolic [GTP]' 69499.664 1   4.1.1.32 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                                 54.938    3   ?        ? ? ? 
3 non-polymer syn SULFOPYRUVATE                                        168.125   1   ?        ? ? ? 
4 non-polymer syn "GUANOSINE-5'-TRIPHOSPHATE"                          523.180   1   ?        ? ? ? 
5 water       nat water                                                18.015    344 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        PEPCK-C 
# 
_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       
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION'        MN  
3 SULFOPYRUVATE               SPV 
4 "GUANOSINE-5'-TRIPHOSPHATE" GTP 
5 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   PRO n 
1 4   GLN n 
1 5   LEU n 
1 6   HIS n 
1 7   ASN n 
1 8   GLY n 
1 9   LEU n 
1 10  ASP n 
1 11  PHE n 
1 12  SER n 
1 13  ALA n 
1 14  LYS n 
1 15  VAL n 
1 16  ILE n 
1 17  GLN n 
1 18  GLY n 
1 19  SER n 
1 20  LEU n 
1 21  ASP n 
1 22  SER n 
1 23  LEU n 
1 24  PRO n 
1 25  GLN n 
1 26  GLU n 
1 27  VAL n 
1 28  ARG n 
1 29  LYS n 
1 30  PHE n 
1 31  VAL n 
1 32  GLU n 
1 33  GLY n 
1 34  ASN n 
1 35  ALA n 
1 36  GLN n 
1 37  LEU n 
1 38  CYS n 
1 39  GLN n 
1 40  PRO n 
1 41  GLU n 
1 42  TYR n 
1 43  ILE n 
1 44  HIS n 
1 45  ILE n 
1 46  CYS n 
1 47  ASP n 
1 48  GLY n 
1 49  SER n 
1 50  GLU n 
1 51  GLU n 
1 52  GLU n 
1 53  TYR n 
1 54  GLY n 
1 55  ARG n 
1 56  LEU n 
1 57  LEU n 
1 58  ALA n 
1 59  HIS n 
1 60  MET n 
1 61  GLN n 
1 62  GLU n 
1 63  GLU n 
1 64  GLY n 
1 65  VAL n 
1 66  ILE n 
1 67  ARG n 
1 68  LYS n 
1 69  LEU n 
1 70  LYS n 
1 71  LYS n 
1 72  TYR n 
1 73  ASP n 
1 74  ASN n 
1 75  CYS n 
1 76  TRP n 
1 77  LEU n 
1 78  ALA n 
1 79  LEU n 
1 80  THR n 
1 81  ASP n 
1 82  PRO n 
1 83  ARG n 
1 84  ASP n 
1 85  VAL n 
1 86  ALA n 
1 87  ARG n 
1 88  ILE n 
1 89  GLU n 
1 90  SER n 
1 91  LYS n 
1 92  THR n 
1 93  VAL n 
1 94  ILE n 
1 95  ILE n 
1 96  THR n 
1 97  GLN n 
1 98  GLU n 
1 99  GLN n 
1 100 ARG n 
1 101 ASP n 
1 102 THR n 
1 103 VAL n 
1 104 PRO n 
1 105 ILE n 
1 106 PRO n 
1 107 LYS n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 SER n 
1 112 GLN n 
1 113 LEU n 
1 114 GLY n 
1 115 ARG n 
1 116 TRP n 
1 117 MET n 
1 118 SER n 
1 119 GLU n 
1 120 GLU n 
1 121 ASP n 
1 122 PHE n 
1 123 GLU n 
1 124 LYS n 
1 125 ALA n 
1 126 PHE n 
1 127 ASN n 
1 128 ALA n 
1 129 ARG n 
1 130 PHE n 
1 131 PRO n 
1 132 GLY n 
1 133 CYS n 
1 134 MET n 
1 135 LYS n 
1 136 GLY n 
1 137 ARG n 
1 138 THR n 
1 139 MET n 
1 140 TYR n 
1 141 VAL n 
1 142 ILE n 
1 143 PRO n 
1 144 PHE n 
1 145 SER n 
1 146 MET n 
1 147 GLY n 
1 148 PRO n 
1 149 LEU n 
1 150 GLY n 
1 151 SER n 
1 152 PRO n 
1 153 LEU n 
1 154 ALA n 
1 155 LYS n 
1 156 ILE n 
1 157 GLY n 
1 158 ILE n 
1 159 GLU n 
1 160 LEU n 
1 161 THR n 
1 162 ASP n 
1 163 SER n 
1 164 PRO n 
1 165 TYR n 
1 166 VAL n 
1 167 VAL n 
1 168 ALA n 
1 169 SER n 
1 170 MET n 
1 171 ARG n 
1 172 ILE n 
1 173 MET n 
1 174 THR n 
1 175 ARG n 
1 176 MET n 
1 177 GLY n 
1 178 THR n 
1 179 SER n 
1 180 VAL n 
1 181 LEU n 
1 182 GLU n 
1 183 ALA n 
1 184 LEU n 
1 185 GLY n 
1 186 ASP n 
1 187 GLY n 
1 188 GLU n 
1 189 PHE n 
1 190 ILE n 
1 191 LYS n 
1 192 CYS n 
1 193 LEU n 
1 194 HIS n 
1 195 SER n 
1 196 VAL n 
1 197 GLY n 
1 198 CYS n 
1 199 PRO n 
1 200 LEU n 
1 201 PRO n 
1 202 LEU n 
1 203 LYS n 
1 204 LYS n 
1 205 PRO n 
1 206 LEU n 
1 207 VAL n 
1 208 ASN n 
1 209 ASN n 
1 210 TRP n 
1 211 ALA n 
1 212 CYS n 
1 213 ASN n 
1 214 PRO n 
1 215 GLU n 
1 216 LEU n 
1 217 THR n 
1 218 LEU n 
1 219 ILE n 
1 220 ALA n 
1 221 HIS n 
1 222 LEU n 
1 223 PRO n 
1 224 ASP n 
1 225 ARG n 
1 226 ARG n 
1 227 GLU n 
1 228 ILE n 
1 229 ILE n 
1 230 SER n 
1 231 PHE n 
1 232 GLY n 
1 233 SER n 
1 234 GLY n 
1 235 TYR n 
1 236 GLY n 
1 237 GLY n 
1 238 ASN n 
1 239 SER n 
1 240 LEU n 
1 241 LEU n 
1 242 GLY n 
1 243 LYS n 
1 244 LYS n 
1 245 CYS n 
1 246 PHE n 
1 247 ALA n 
1 248 LEU n 
1 249 ARG n 
1 250 ILE n 
1 251 ALA n 
1 252 SER n 
1 253 ARG n 
1 254 LEU n 
1 255 ALA n 
1 256 LYS n 
1 257 GLU n 
1 258 GLU n 
1 259 GLY n 
1 260 TRP n 
1 261 LEU n 
1 262 ALA n 
1 263 GLU n 
1 264 HIS n 
1 265 MET n 
1 266 LEU n 
1 267 ILE n 
1 268 LEU n 
1 269 GLY n 
1 270 ILE n 
1 271 THR n 
1 272 ASN n 
1 273 PRO n 
1 274 GLU n 
1 275 GLY n 
1 276 LYS n 
1 277 LYS n 
1 278 LYS n 
1 279 TYR n 
1 280 LEU n 
1 281 ALA n 
1 282 ALA n 
1 283 ALA n 
1 284 PHE n 
1 285 PRO n 
1 286 SER n 
1 287 ALA n 
1 288 CYS n 
1 289 GLY n 
1 290 LYS n 
1 291 THR n 
1 292 ASN n 
1 293 LEU n 
1 294 ALA n 
1 295 MET n 
1 296 MET n 
1 297 ASN n 
1 298 PRO n 
1 299 THR n 
1 300 LEU n 
1 301 PRO n 
1 302 GLY n 
1 303 TRP n 
1 304 LYS n 
1 305 VAL n 
1 306 GLU n 
1 307 CYS n 
1 308 VAL n 
1 309 GLY n 
1 310 ASP n 
1 311 ASP n 
1 312 ILE n 
1 313 ALA n 
1 314 TRP n 
1 315 MET n 
1 316 LYS n 
1 317 PHE n 
1 318 ASP n 
1 319 ALA n 
1 320 GLN n 
1 321 GLY n 
1 322 ASN n 
1 323 LEU n 
1 324 ARG n 
1 325 ALA n 
1 326 ILE n 
1 327 ASN n 
1 328 PRO n 
1 329 GLU n 
1 330 ASN n 
1 331 GLY n 
1 332 PHE n 
1 333 PHE n 
1 334 GLY n 
1 335 VAL n 
1 336 ALA n 
1 337 PRO n 
1 338 GLY n 
1 339 THR n 
1 340 SER n 
1 341 VAL n 
1 342 LYS n 
1 343 THR n 
1 344 ASN n 
1 345 PRO n 
1 346 ASN n 
1 347 ALA n 
1 348 ILE n 
1 349 LYS n 
1 350 THR n 
1 351 ILE n 
1 352 GLN n 
1 353 LYS n 
1 354 ASN n 
1 355 THR n 
1 356 ILE n 
1 357 PHE n 
1 358 THR n 
1 359 ASN n 
1 360 VAL n 
1 361 ALA n 
1 362 GLU n 
1 363 THR n 
1 364 SER n 
1 365 ASP n 
1 366 GLY n 
1 367 GLY n 
1 368 VAL n 
1 369 TYR n 
1 370 TRP n 
1 371 GLU n 
1 372 GLY n 
1 373 ILE n 
1 374 ASP n 
1 375 GLU n 
1 376 PRO n 
1 377 LEU n 
1 378 ALA n 
1 379 PRO n 
1 380 GLY n 
1 381 VAL n 
1 382 THR n 
1 383 ILE n 
1 384 THR n 
1 385 SER n 
1 386 TRP n 
1 387 LYS n 
1 388 ASN n 
1 389 LYS n 
1 390 GLU n 
1 391 TRP n 
1 392 ARG n 
1 393 PRO n 
1 394 GLN n 
1 395 ASP n 
1 396 GLU n 
1 397 GLU n 
1 398 PRO n 
1 399 CYS n 
1 400 ALA n 
1 401 HIS n 
1 402 PRO n 
1 403 ASN n 
1 404 SER n 
1 405 ARG n 
1 406 PHE n 
1 407 CYS n 
1 408 THR n 
1 409 PRO n 
1 410 ALA n 
1 411 SER n 
1 412 GLN n 
1 413 CYS n 
1 414 PRO n 
1 415 ILE n 
1 416 ILE n 
1 417 ASP n 
1 418 PRO n 
1 419 ALA n 
1 420 TRP n 
1 421 GLU n 
1 422 SER n 
1 423 PRO n 
1 424 GLU n 
1 425 GLY n 
1 426 VAL n 
1 427 PRO n 
1 428 ILE n 
1 429 GLU n 
1 430 GLY n 
1 431 ILE n 
1 432 ILE n 
1 433 PHE n 
1 434 GLY n 
1 435 GLY n 
1 436 ARG n 
1 437 ARG n 
1 438 PRO n 
1 439 ALA n 
1 440 GLY n 
1 441 VAL n 
1 442 PRO n 
1 443 LEU n 
1 444 VAL n 
1 445 TYR n 
1 446 GLU n 
1 447 ALA n 
1 448 LEU n 
1 449 SER n 
1 450 TRP n 
1 451 GLN n 
1 452 HIS n 
1 453 GLY n 
1 454 VAL n 
1 455 PHE n 
1 456 VAL n 
1 457 GLY n 
1 458 ALA n 
1 459 ALA n 
1 460 MET n 
1 461 ARG n 
1 462 SER n 
1 463 GLU n 
1 464 ALA n 
1 465 THR n 
1 466 ALA n 
1 467 ALA n 
1 468 ALA n 
1 469 GLU n 
1 470 HIS n 
1 471 LYS n 
1 472 GLY n 
1 473 LYS n 
1 474 VAL n 
1 475 ILE n 
1 476 MET n 
1 477 HIS n 
1 478 ASP n 
1 479 PRO n 
1 480 PHE n 
1 481 ALA n 
1 482 MET n 
1 483 ARG n 
1 484 PRO n 
1 485 PHE n 
1 486 PHE n 
1 487 GLY n 
1 488 TYR n 
1 489 ASN n 
1 490 PHE n 
1 491 GLY n 
1 492 LYS n 
1 493 TYR n 
1 494 LEU n 
1 495 ALA n 
1 496 HIS n 
1 497 TRP n 
1 498 LEU n 
1 499 SER n 
1 500 MET n 
1 501 ALA n 
1 502 HIS n 
1 503 ARG n 
1 504 PRO n 
1 505 ALA n 
1 506 ALA n 
1 507 LYS n 
1 508 LEU n 
1 509 PRO n 
1 510 LYS n 
1 511 ILE n 
1 512 PHE n 
1 513 HIS n 
1 514 VAL n 
1 515 ASN n 
1 516 TRP n 
1 517 PHE n 
1 518 ARG n 
1 519 LYS n 
1 520 ASP n 
1 521 LYS n 
1 522 ASN n 
1 523 GLY n 
1 524 LYS n 
1 525 PHE n 
1 526 LEU n 
1 527 TRP n 
1 528 PRO n 
1 529 GLY n 
1 530 PHE n 
1 531 GLY n 
1 532 GLU n 
1 533 ASN n 
1 534 SER n 
1 535 ARG n 
1 536 VAL n 
1 537 LEU n 
1 538 GLU n 
1 539 TRP n 
1 540 MET n 
1 541 PHE n 
1 542 GLY n 
1 543 ARG n 
1 544 ILE n 
1 545 GLU n 
1 546 GLY n 
1 547 GLU n 
1 548 ASP n 
1 549 SER n 
1 550 ALA n 
1 551 LYS n 
1 552 LEU n 
1 553 THR n 
1 554 PRO n 
1 555 ILE n 
1 556 GLY n 
1 557 TYR n 
1 558 VAL n 
1 559 PRO n 
1 560 LYS n 
1 561 GLU n 
1 562 ASP n 
1 563 ALA n 
1 564 LEU n 
1 565 ASN n 
1 566 LEU n 
1 567 LYS n 
1 568 GLY n 
1 569 LEU n 
1 570 GLY n 
1 571 ASP n 
1 572 VAL n 
1 573 ASN n 
1 574 VAL n 
1 575 GLU n 
1 576 GLU n 
1 577 LEU n 
1 578 PHE n 
1 579 GLY n 
1 580 ILE n 
1 581 SER n 
1 582 LYS n 
1 583 GLU n 
1 584 PHE n 
1 585 TRP n 
1 586 GLU n 
1 587 LYS n 
1 588 GLU n 
1 589 VAL n 
1 590 GLU n 
1 591 GLU n 
1 592 ILE n 
1 593 ASP n 
1 594 LYS n 
1 595 TYR n 
1 596 LEU n 
1 597 GLU n 
1 598 ASP n 
1 599 GLN n 
1 600 VAL n 
1 601 ASN n 
1 602 ALA n 
1 603 ASP n 
1 604 LEU n 
1 605 PRO n 
1 606 TYR n 
1 607 GLU n 
1 608 ILE n 
1 609 GLU n 
1 610 ARG n 
1 611 GLU n 
1 612 LEU n 
1 613 ARG n 
1 614 ALA n 
1 615 LEU n 
1 616 LYS n 
1 617 GLN n 
1 618 ARG n 
1 619 ILE n 
1 620 SER n 
1 621 GLN n 
1 622 MET n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   622 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Pck1 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli K-12' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     83333 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pESUMOstar (KAN)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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  
GTP non-polymer         n "GUANOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O14 P3' 523.180 
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 
MN  non-polymer         . 'MANGANESE (II) ION'        ? 'Mn 2'              54.938  
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 
SPV non-polymer         . SULFOPYRUVATE               ? 'C3 H4 O6 S'        168.125 
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 
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   HIS 6   6   6   HIS HIS A . n 
A 1 7   ASN 7   7   7   ASN ASN A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  MET 60  60  60  MET MET A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  LYS 68  68  68  LYS LYS 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  LYS 71  71  71  LYS LYS A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  CYS 75  75  75  CYS CYS A . n 
A 1 76  TRP 76  76  76  TRP TRP A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 TRP 116 116 116 TRP TRP A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 MET 134 134 134 MET MET A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LYS 155 155 155 LYS LYS 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 ILE 158 158 158 ILE ILE A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 MET 170 170 170 MET MET A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 TRP 210 210 210 TRP TRP A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 ILE 229 229 229 ILE ILE 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 SER 233 233 233 SER SER A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 CYS 245 245 245 CYS CYS A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 TRP 260 260 260 TRP TRP A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 MET 265 265 265 MET MET A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 CYS 288 288 288 CYS CYS A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 ASN 292 292 292 ASN ASN A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 CYS 307 307 307 CYS CYS A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 TRP 314 314 314 TRP TRP A . n 
A 1 315 MET 315 315 315 MET MET A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ARG 324 324 324 ARG ARG A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 PRO 328 328 328 PRO PRO A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 ASN 330 330 330 ASN ASN A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 PHE 333 333 333 PHE PHE A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 LYS 342 342 342 LYS LYS A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 ASN 346 346 346 ASN ASN A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 GLN 352 352 352 GLN GLN A . n 
A 1 353 LYS 353 353 353 LYS LYS A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 ILE 356 356 356 ILE ILE A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 ASN 359 359 359 ASN ASN A . n 
A 1 360 VAL 360 360 360 VAL VAL A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 THR 363 363 363 THR THR A . n 
A 1 364 SER 364 364 364 SER SER A . n 
A 1 365 ASP 365 365 365 ASP ASP A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 TRP 370 370 370 TRP TRP A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 PRO 379 379 379 PRO PRO A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 TRP 386 386 386 TRP TRP A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 ARG 392 392 392 ARG ARG A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 GLN 394 394 394 GLN GLN A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 PRO 398 398 398 PRO PRO A . n 
A 1 399 CYS 399 399 399 CYS CYS A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 HIS 401 401 401 HIS HIS A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 ASN 403 403 403 ASN ASN A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 PHE 406 406 406 PHE PHE A . n 
A 1 407 CYS 407 407 407 CYS CYS A . n 
A 1 408 THR 408 408 408 THR THR A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 SER 411 411 411 SER SER A . n 
A 1 412 GLN 412 412 412 GLN GLN A . n 
A 1 413 CYS 413 413 413 CYS CYS A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 TRP 420 420 420 TRP TRP A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 SER 422 422 422 SER SER A . n 
A 1 423 PRO 423 423 423 PRO PRO A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 PRO 427 427 427 PRO PRO A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 PHE 433 433 433 PHE PHE A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 ARG 436 436 436 ARG ARG A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 PRO 438 438 438 PRO PRO A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 GLY 440 440 440 GLY GLY A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 VAL 444 444 444 VAL VAL A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 SER 449 449 449 SER SER A . n 
A 1 450 TRP 450 450 450 TRP TRP A . n 
A 1 451 GLN 451 451 451 GLN GLN A . n 
A 1 452 HIS 452 452 452 HIS HIS A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 MET 460 460 460 MET MET A . n 
A 1 461 ARG 461 461 461 ARG ARG A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 THR 465 465 465 THR THR A . n 
A 1 466 ALA 466 466 466 ALA ALA A . n 
A 1 467 ALA 467 467 467 ALA ALA A . n 
A 1 468 ALA 468 468 468 ALA ALA A . n 
A 1 469 GLU 469 469 469 GLU GLU A . n 
A 1 470 HIS 470 470 470 HIS HIS A . n 
A 1 471 LYS 471 471 471 LYS LYS A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 LYS 473 473 473 LYS LYS A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 ILE 475 475 475 ILE ILE A . n 
A 1 476 MET 476 476 476 MET MET A . n 
A 1 477 HIS 477 477 477 HIS HIS A . n 
A 1 478 ASP 478 478 478 ASP ASP A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 PHE 480 480 480 PHE PHE A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 MET 482 482 482 MET MET A . n 
A 1 483 ARG 483 483 483 ARG ARG A . n 
A 1 484 PRO 484 484 484 PRO PRO A . n 
A 1 485 PHE 485 485 485 PHE PHE A . n 
A 1 486 PHE 486 486 486 PHE PHE A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 TYR 488 488 488 TYR TYR A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 PHE 490 490 490 PHE PHE 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 TYR 493 493 493 TYR TYR A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 ALA 495 495 495 ALA ALA A . n 
A 1 496 HIS 496 496 496 HIS HIS A . n 
A 1 497 TRP 497 497 497 TRP TRP A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 MET 500 500 500 MET MET A . n 
A 1 501 ALA 501 501 501 ALA ALA A . n 
A 1 502 HIS 502 502 502 HIS HIS A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 PRO 504 504 504 PRO PRO A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 LYS 507 507 507 LYS LYS A . n 
A 1 508 LEU 508 508 508 LEU LEU A . n 
A 1 509 PRO 509 509 509 PRO PRO A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 ILE 511 511 511 ILE ILE A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 HIS 513 513 513 HIS HIS A . n 
A 1 514 VAL 514 514 514 VAL VAL A . n 
A 1 515 ASN 515 515 515 ASN ASN A . n 
A 1 516 TRP 516 516 516 TRP TRP A . n 
A 1 517 PHE 517 517 517 PHE PHE A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 ASP 520 520 520 ASP ASP A . n 
A 1 521 LYS 521 521 521 LYS LYS A . n 
A 1 522 ASN 522 522 522 ASN ASN A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 LYS 524 524 524 LYS LYS A . n 
A 1 525 PHE 525 525 525 PHE PHE A . n 
A 1 526 LEU 526 526 526 LEU LEU A . n 
A 1 527 TRP 527 527 527 TRP TRP A . n 
A 1 528 PRO 528 528 528 PRO PRO A . n 
A 1 529 GLY 529 529 529 GLY GLY A . n 
A 1 530 PHE 530 530 530 PHE PHE A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 GLU 532 532 532 GLU GLU A . n 
A 1 533 ASN 533 533 533 ASN ASN A . n 
A 1 534 SER 534 534 534 SER SER A . n 
A 1 535 ARG 535 535 535 ARG ARG A . n 
A 1 536 VAL 536 536 536 VAL VAL A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 TRP 539 539 539 TRP TRP A . n 
A 1 540 MET 540 540 540 MET MET A . n 
A 1 541 PHE 541 541 541 PHE PHE A . n 
A 1 542 GLY 542 542 542 GLY GLY A . n 
A 1 543 ARG 543 543 543 ARG ARG A . n 
A 1 544 ILE 544 544 544 ILE ILE A . n 
A 1 545 GLU 545 545 545 GLU GLU A . n 
A 1 546 GLY 546 546 546 GLY GLY A . n 
A 1 547 GLU 547 547 547 GLU GLU A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 SER 549 549 549 SER SER A . n 
A 1 550 ALA 550 550 550 ALA ALA A . n 
A 1 551 LYS 551 551 551 LYS LYS A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 THR 553 553 553 THR THR A . n 
A 1 554 PRO 554 554 554 PRO PRO A . n 
A 1 555 ILE 555 555 555 ILE ILE A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 TYR 557 557 557 TYR TYR A . n 
A 1 558 VAL 558 558 558 VAL VAL A . n 
A 1 559 PRO 559 559 559 PRO PRO A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 GLU 561 561 561 GLU GLU A . n 
A 1 562 ASP 562 562 562 ASP ASP A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 ASN 565 565 565 ASN ASN A . n 
A 1 566 LEU 566 566 566 LEU LEU A . n 
A 1 567 LYS 567 567 567 LYS LYS A . n 
A 1 568 GLY 568 568 568 GLY GLY A . n 
A 1 569 LEU 569 569 569 LEU LEU A . n 
A 1 570 GLY 570 570 570 GLY GLY A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 VAL 572 572 572 VAL VAL A . n 
A 1 573 ASN 573 573 573 ASN ASN A . n 
A 1 574 VAL 574 574 574 VAL VAL A . n 
A 1 575 GLU 575 575 575 GLU GLU A . n 
A 1 576 GLU 576 576 576 GLU GLU A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 PHE 578 578 578 PHE PHE A . n 
A 1 579 GLY 579 579 579 GLY GLY A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 SER 581 581 581 SER SER A . n 
A 1 582 LYS 582 582 582 LYS LYS A . n 
A 1 583 GLU 583 583 583 GLU GLU A . n 
A 1 584 PHE 584 584 584 PHE PHE A . n 
A 1 585 TRP 585 585 585 TRP TRP A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 LYS 587 587 587 LYS LYS A . n 
A 1 588 GLU 588 588 588 GLU GLU A . n 
A 1 589 VAL 589 589 589 VAL VAL A . n 
A 1 590 GLU 590 590 590 GLU GLU A . n 
A 1 591 GLU 591 591 591 GLU GLU A . n 
A 1 592 ILE 592 592 592 ILE ILE A . n 
A 1 593 ASP 593 593 593 ASP ASP A . n 
A 1 594 LYS 594 594 594 LYS LYS A . n 
A 1 595 TYR 595 595 595 TYR TYR A . n 
A 1 596 LEU 596 596 596 LEU LEU A . n 
A 1 597 GLU 597 597 597 GLU GLU A . n 
A 1 598 ASP 598 598 598 ASP ASP A . n 
A 1 599 GLN 599 599 599 GLN GLN A . n 
A 1 600 VAL 600 600 600 VAL VAL A . n 
A 1 601 ASN 601 601 601 ASN ASN A . n 
A 1 602 ALA 602 602 602 ALA ALA A . n 
A 1 603 ASP 603 603 603 ASP ASP A . n 
A 1 604 LEU 604 604 604 LEU LEU A . n 
A 1 605 PRO 605 605 605 PRO PRO A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLU 607 607 607 GLU GLU A . n 
A 1 608 ILE 608 608 608 ILE ILE A . n 
A 1 609 GLU 609 609 609 GLU GLU A . n 
A 1 610 ARG 610 610 610 ARG ARG A . n 
A 1 611 GLU 611 611 611 GLU GLU A . n 
A 1 612 LEU 612 612 612 LEU LEU A . n 
A 1 613 ARG 613 613 613 ARG ARG A . n 
A 1 614 ALA 614 614 614 ALA ALA A . n 
A 1 615 LEU 615 615 615 LEU LEU A . n 
A 1 616 LYS 616 616 616 LYS LYS A . n 
A 1 617 GLN 617 617 617 GLN GLN A . n 
A 1 618 ARG 618 618 618 ARG ARG A . n 
A 1 619 ILE 619 619 619 ILE ILE A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 GLN 621 621 621 GLN GLN A . n 
A 1 622 MET 622 622 622 MET MET A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GTP ? ? GTP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SPV ? ? SPV ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 MN  1   701  700 MN  MN  A . 
C 2 MN  1   702  701 MN  MN  A . 
D 2 MN  1   703  702 MN  MN  A . 
E 3 SPV 1   704  800 SPV SPV A . 
F 4 GTP 1   705  900 GTP GTP A . 
G 5 HOH 1   801  127 HOH HOH A . 
G 5 HOH 2   802  181 HOH HOH A . 
G 5 HOH 3   803  82  HOH HOH A . 
G 5 HOH 4   804  175 HOH HOH A . 
G 5 HOH 5   805  189 HOH HOH A . 
G 5 HOH 6   806  266 HOH HOH A . 
G 5 HOH 7   807  87  HOH HOH A . 
G 5 HOH 8   808  141 HOH HOH A . 
G 5 HOH 9   809  207 HOH HOH A . 
G 5 HOH 10  810  263 HOH HOH A . 
G 5 HOH 11  811  292 HOH HOH A . 
G 5 HOH 12  812  94  HOH HOH A . 
G 5 HOH 13  813  209 HOH HOH A . 
G 5 HOH 14  814  239 HOH HOH A . 
G 5 HOH 15  815  324 HOH HOH A . 
G 5 HOH 16  816  244 HOH HOH A . 
G 5 HOH 17  817  249 HOH HOH A . 
G 5 HOH 18  818  142 HOH HOH A . 
G 5 HOH 19  819  252 HOH HOH A . 
G 5 HOH 20  820  295 HOH HOH A . 
G 5 HOH 21  821  103 HOH HOH A . 
G 5 HOH 22  822  245 HOH HOH A . 
G 5 HOH 23  823  281 HOH HOH A . 
G 5 HOH 24  824  319 HOH HOH A . 
G 5 HOH 25  825  129 HOH HOH A . 
G 5 HOH 26  826  124 HOH HOH A . 
G 5 HOH 27  827  174 HOH HOH A . 
G 5 HOH 28  828  243 HOH HOH A . 
G 5 HOH 29  829  117 HOH HOH A . 
G 5 HOH 30  830  110 HOH HOH A . 
G 5 HOH 31  831  283 HOH HOH A . 
G 5 HOH 32  832  280 HOH HOH A . 
G 5 HOH 33  833  256 HOH HOH A . 
G 5 HOH 34  834  88  HOH HOH A . 
G 5 HOH 35  835  136 HOH HOH A . 
G 5 HOH 36  836  184 HOH HOH A . 
G 5 HOH 37  837  223 HOH HOH A . 
G 5 HOH 38  838  37  HOH HOH A . 
G 5 HOH 39  839  294 HOH HOH A . 
G 5 HOH 40  840  71  HOH HOH A . 
G 5 HOH 41  841  111 HOH HOH A . 
G 5 HOH 42  842  8   HOH HOH A . 
G 5 HOH 43  843  146 HOH HOH A . 
G 5 HOH 44  844  208 HOH HOH A . 
G 5 HOH 45  845  293 HOH HOH A . 
G 5 HOH 46  846  125 HOH HOH A . 
G 5 HOH 47  847  24  HOH HOH A . 
G 5 HOH 48  848  261 HOH HOH A . 
G 5 HOH 49  849  248 HOH HOH A . 
G 5 HOH 50  850  247 HOH HOH A . 
G 5 HOH 51  851  1   HOH HOH A . 
G 5 HOH 52  852  6   HOH HOH A . 
G 5 HOH 53  853  277 HOH HOH A . 
G 5 HOH 54  854  167 HOH HOH A . 
G 5 HOH 55  855  69  HOH HOH A . 
G 5 HOH 56  856  64  HOH HOH A . 
G 5 HOH 57  857  50  HOH HOH A . 
G 5 HOH 58  858  109 HOH HOH A . 
G 5 HOH 59  859  169 HOH HOH A . 
G 5 HOH 60  860  119 HOH HOH A . 
G 5 HOH 61  861  185 HOH HOH A . 
G 5 HOH 62  862  211 HOH HOH A . 
G 5 HOH 63  863  296 HOH HOH A . 
G 5 HOH 64  864  128 HOH HOH A . 
G 5 HOH 65  865  290 HOH HOH A . 
G 5 HOH 66  866  150 HOH HOH A . 
G 5 HOH 67  867  272 HOH HOH A . 
G 5 HOH 68  868  212 HOH HOH A . 
G 5 HOH 69  869  27  HOH HOH A . 
G 5 HOH 70  870  153 HOH HOH A . 
G 5 HOH 71  871  325 HOH HOH A . 
G 5 HOH 72  872  241 HOH HOH A . 
G 5 HOH 73  873  65  HOH HOH A . 
G 5 HOH 74  874  334 HOH HOH A . 
G 5 HOH 75  875  53  HOH HOH A . 
G 5 HOH 76  876  298 HOH HOH A . 
G 5 HOH 77  877  131 HOH HOH A . 
G 5 HOH 78  878  45  HOH HOH A . 
G 5 HOH 79  879  253 HOH HOH A . 
G 5 HOH 80  880  11  HOH HOH A . 
G 5 HOH 81  881  168 HOH HOH A . 
G 5 HOH 82  882  163 HOH HOH A . 
G 5 HOH 83  883  255 HOH HOH A . 
G 5 HOH 84  884  102 HOH HOH A . 
G 5 HOH 85  885  55  HOH HOH A . 
G 5 HOH 86  886  137 HOH HOH A . 
G 5 HOH 87  887  85  HOH HOH A . 
G 5 HOH 88  888  227 HOH HOH A . 
G 5 HOH 89  889  278 HOH HOH A . 
G 5 HOH 90  890  226 HOH HOH A . 
G 5 HOH 91  891  78  HOH HOH A . 
G 5 HOH 92  892  225 HOH HOH A . 
G 5 HOH 93  893  26  HOH HOH A . 
G 5 HOH 94  894  305 HOH HOH A . 
G 5 HOH 95  895  100 HOH HOH A . 
G 5 HOH 96  896  173 HOH HOH A . 
G 5 HOH 97  897  213 HOH HOH A . 
G 5 HOH 98  898  4   HOH HOH A . 
G 5 HOH 99  899  216 HOH HOH A . 
G 5 HOH 100 900  30  HOH HOH A . 
G 5 HOH 101 901  56  HOH HOH A . 
G 5 HOH 102 902  2   HOH HOH A . 
G 5 HOH 103 903  13  HOH HOH A . 
G 5 HOH 104 904  44  HOH HOH A . 
G 5 HOH 105 905  83  HOH HOH A . 
G 5 HOH 106 906  62  HOH HOH A . 
G 5 HOH 107 907  235 HOH HOH A . 
G 5 HOH 108 908  311 HOH HOH A . 
G 5 HOH 109 909  15  HOH HOH A . 
G 5 HOH 110 910  47  HOH HOH A . 
G 5 HOH 111 911  238 HOH HOH A . 
G 5 HOH 112 912  231 HOH HOH A . 
G 5 HOH 113 913  58  HOH HOH A . 
G 5 HOH 114 914  104 HOH HOH A . 
G 5 HOH 115 915  276 HOH HOH A . 
G 5 HOH 116 916  199 HOH HOH A . 
G 5 HOH 117 917  254 HOH HOH A . 
G 5 HOH 118 918  341 HOH HOH A . 
G 5 HOH 119 919  92  HOH HOH A . 
G 5 HOH 120 920  126 HOH HOH A . 
G 5 HOH 121 921  114 HOH HOH A . 
G 5 HOH 122 922  41  HOH HOH A . 
G 5 HOH 123 923  303 HOH HOH A . 
G 5 HOH 124 924  90  HOH HOH A . 
G 5 HOH 125 925  7   HOH HOH A . 
G 5 HOH 126 926  339 HOH HOH A . 
G 5 HOH 127 927  74  HOH HOH A . 
G 5 HOH 128 928  186 HOH HOH A . 
G 5 HOH 129 929  147 HOH HOH A . 
G 5 HOH 130 930  132 HOH HOH A . 
G 5 HOH 131 931  214 HOH HOH A . 
G 5 HOH 132 932  31  HOH HOH A . 
G 5 HOH 133 933  220 HOH HOH A . 
G 5 HOH 134 934  196 HOH HOH A . 
G 5 HOH 135 935  9   HOH HOH A . 
G 5 HOH 136 936  93  HOH HOH A . 
G 5 HOH 137 937  25  HOH HOH A . 
G 5 HOH 138 938  234 HOH HOH A . 
G 5 HOH 139 939  237 HOH HOH A . 
G 5 HOH 140 940  84  HOH HOH A . 
G 5 HOH 141 941  144 HOH HOH A . 
G 5 HOH 142 942  3   HOH HOH A . 
G 5 HOH 143 943  5   HOH HOH A . 
G 5 HOH 144 944  22  HOH HOH A . 
G 5 HOH 145 945  307 HOH HOH A . 
G 5 HOH 146 946  42  HOH HOH A . 
G 5 HOH 147 947  97  HOH HOH A . 
G 5 HOH 148 948  10  HOH HOH A . 
G 5 HOH 149 949  39  HOH HOH A . 
G 5 HOH 150 950  67  HOH HOH A . 
G 5 HOH 151 951  14  HOH HOH A . 
G 5 HOH 152 952  51  HOH HOH A . 
G 5 HOH 153 953  40  HOH HOH A . 
G 5 HOH 154 954  61  HOH HOH A . 
G 5 HOH 155 955  28  HOH HOH A . 
G 5 HOH 156 956  32  HOH HOH A . 
G 5 HOH 157 957  224 HOH HOH A . 
G 5 HOH 158 958  134 HOH HOH A . 
G 5 HOH 159 959  91  HOH HOH A . 
G 5 HOH 160 960  177 HOH HOH A . 
G 5 HOH 161 961  99  HOH HOH A . 
G 5 HOH 162 962  59  HOH HOH A . 
G 5 HOH 163 963  297 HOH HOH A . 
G 5 HOH 164 964  105 HOH HOH A . 
G 5 HOH 165 965  43  HOH HOH A . 
G 5 HOH 166 966  17  HOH HOH A . 
G 5 HOH 167 967  288 HOH HOH A . 
G 5 HOH 168 968  19  HOH HOH A . 
G 5 HOH 169 969  12  HOH HOH A . 
G 5 HOH 170 970  176 HOH HOH A . 
G 5 HOH 171 971  46  HOH HOH A . 
G 5 HOH 172 972  116 HOH HOH A . 
G 5 HOH 173 973  206 HOH HOH A . 
G 5 HOH 174 974  232 HOH HOH A . 
G 5 HOH 175 975  159 HOH HOH A . 
G 5 HOH 176 976  188 HOH HOH A . 
G 5 HOH 177 977  23  HOH HOH A . 
G 5 HOH 178 978  342 HOH HOH A . 
G 5 HOH 179 979  236 HOH HOH A . 
G 5 HOH 180 980  162 HOH HOH A . 
G 5 HOH 181 981  344 HOH HOH A . 
G 5 HOH 182 982  187 HOH HOH A . 
G 5 HOH 183 983  36  HOH HOH A . 
G 5 HOH 184 984  76  HOH HOH A . 
G 5 HOH 185 985  113 HOH HOH A . 
G 5 HOH 186 986  166 HOH HOH A . 
G 5 HOH 187 987  57  HOH HOH A . 
G 5 HOH 188 988  86  HOH HOH A . 
G 5 HOH 189 989  171 HOH HOH A . 
G 5 HOH 190 990  79  HOH HOH A . 
G 5 HOH 191 991  198 HOH HOH A . 
G 5 HOH 192 992  260 HOH HOH A . 
G 5 HOH 193 993  156 HOH HOH A . 
G 5 HOH 194 994  33  HOH HOH A . 
G 5 HOH 195 995  218 HOH HOH A . 
G 5 HOH 196 996  165 HOH HOH A . 
G 5 HOH 197 997  145 HOH HOH A . 
G 5 HOH 198 998  192 HOH HOH A . 
G 5 HOH 199 999  133 HOH HOH A . 
G 5 HOH 200 1000 258 HOH HOH A . 
G 5 HOH 201 1001 229 HOH HOH A . 
G 5 HOH 202 1002 219 HOH HOH A . 
G 5 HOH 203 1003 121 HOH HOH A . 
G 5 HOH 204 1004 18  HOH HOH A . 
G 5 HOH 205 1005 164 HOH HOH A . 
G 5 HOH 206 1006 155 HOH HOH A . 
G 5 HOH 207 1007 34  HOH HOH A . 
G 5 HOH 208 1008 21  HOH HOH A . 
G 5 HOH 209 1009 106 HOH HOH A . 
G 5 HOH 210 1010 265 HOH HOH A . 
G 5 HOH 211 1011 138 HOH HOH A . 
G 5 HOH 212 1012 197 HOH HOH A . 
G 5 HOH 213 1013 112 HOH HOH A . 
G 5 HOH 214 1014 180 HOH HOH A . 
G 5 HOH 215 1015 161 HOH HOH A . 
G 5 HOH 216 1016 202 HOH HOH A . 
G 5 HOH 217 1017 63  HOH HOH A . 
G 5 HOH 218 1018 172 HOH HOH A . 
G 5 HOH 219 1019 52  HOH HOH A . 
G 5 HOH 220 1020 170 HOH HOH A . 
G 5 HOH 221 1021 70  HOH HOH A . 
G 5 HOH 222 1022 308 HOH HOH A . 
G 5 HOH 223 1023 222 HOH HOH A . 
G 5 HOH 224 1024 77  HOH HOH A . 
G 5 HOH 225 1025 151 HOH HOH A . 
G 5 HOH 226 1026 250 HOH HOH A . 
G 5 HOH 227 1027 68  HOH HOH A . 
G 5 HOH 228 1028 29  HOH HOH A . 
G 5 HOH 229 1029 158 HOH HOH A . 
G 5 HOH 230 1030 118 HOH HOH A . 
G 5 HOH 231 1031 191 HOH HOH A . 
G 5 HOH 232 1032 16  HOH HOH A . 
G 5 HOH 233 1033 123 HOH HOH A . 
G 5 HOH 234 1034 154 HOH HOH A . 
G 5 HOH 235 1035 20  HOH HOH A . 
G 5 HOH 236 1036 314 HOH HOH A . 
G 5 HOH 237 1037 337 HOH HOH A . 
G 5 HOH 238 1038 38  HOH HOH A . 
G 5 HOH 239 1039 135 HOH HOH A . 
G 5 HOH 240 1040 80  HOH HOH A . 
G 5 HOH 241 1041 149 HOH HOH A . 
G 5 HOH 242 1042 182 HOH HOH A . 
G 5 HOH 243 1043 327 HOH HOH A . 
G 5 HOH 244 1044 194 HOH HOH A . 
G 5 HOH 245 1045 205 HOH HOH A . 
G 5 HOH 246 1046 273 HOH HOH A . 
G 5 HOH 247 1047 48  HOH HOH A . 
G 5 HOH 248 1048 201 HOH HOH A . 
G 5 HOH 249 1049 49  HOH HOH A . 
G 5 HOH 250 1050 66  HOH HOH A . 
G 5 HOH 251 1051 148 HOH HOH A . 
G 5 HOH 252 1052 333 HOH HOH A . 
G 5 HOH 253 1053 271 HOH HOH A . 
G 5 HOH 254 1054 115 HOH HOH A . 
G 5 HOH 255 1055 230 HOH HOH A . 
G 5 HOH 256 1056 98  HOH HOH A . 
G 5 HOH 257 1057 259 HOH HOH A . 
G 5 HOH 258 1058 95  HOH HOH A . 
G 5 HOH 259 1059 331 HOH HOH A . 
G 5 HOH 260 1060 130 HOH HOH A . 
G 5 HOH 261 1061 289 HOH HOH A . 
G 5 HOH 262 1062 140 HOH HOH A . 
G 5 HOH 263 1063 54  HOH HOH A . 
G 5 HOH 264 1064 233 HOH HOH A . 
G 5 HOH 265 1065 60  HOH HOH A . 
G 5 HOH 266 1066 262 HOH HOH A . 
G 5 HOH 267 1067 228 HOH HOH A . 
G 5 HOH 268 1068 299 HOH HOH A . 
G 5 HOH 269 1069 336 HOH HOH A . 
G 5 HOH 270 1070 35  HOH HOH A . 
G 5 HOH 271 1071 143 HOH HOH A . 
G 5 HOH 272 1072 269 HOH HOH A . 
G 5 HOH 273 1073 215 HOH HOH A . 
G 5 HOH 274 1074 107 HOH HOH A . 
G 5 HOH 275 1075 204 HOH HOH A . 
G 5 HOH 276 1076 81  HOH HOH A . 
G 5 HOH 277 1077 251 HOH HOH A . 
G 5 HOH 278 1078 101 HOH HOH A . 
G 5 HOH 279 1079 322 HOH HOH A . 
G 5 HOH 280 1080 309 HOH HOH A . 
G 5 HOH 281 1081 157 HOH HOH A . 
G 5 HOH 282 1082 210 HOH HOH A . 
G 5 HOH 283 1083 200 HOH HOH A . 
G 5 HOH 284 1084 286 HOH HOH A . 
G 5 HOH 285 1085 320 HOH HOH A . 
G 5 HOH 286 1086 326 HOH HOH A . 
G 5 HOH 287 1087 274 HOH HOH A . 
G 5 HOH 288 1088 246 HOH HOH A . 
G 5 HOH 289 1089 335 HOH HOH A . 
G 5 HOH 290 1090 315 HOH HOH A . 
G 5 HOH 291 1091 318 HOH HOH A . 
G 5 HOH 292 1092 270 HOH HOH A . 
G 5 HOH 293 1093 328 HOH HOH A . 
G 5 HOH 294 1094 190 HOH HOH A . 
G 5 HOH 295 1095 178 HOH HOH A . 
G 5 HOH 296 1096 282 HOH HOH A . 
G 5 HOH 297 1097 179 HOH HOH A . 
G 5 HOH 298 1098 96  HOH HOH A . 
G 5 HOH 299 1099 193 HOH HOH A . 
G 5 HOH 300 1100 323 HOH HOH A . 
G 5 HOH 301 1101 332 HOH HOH A . 
G 5 HOH 302 1102 75  HOH HOH A . 
G 5 HOH 303 1103 304 HOH HOH A . 
G 5 HOH 304 1104 257 HOH HOH A . 
G 5 HOH 305 1105 195 HOH HOH A . 
G 5 HOH 306 1106 302 HOH HOH A . 
G 5 HOH 307 1107 329 HOH HOH A . 
G 5 HOH 308 1108 221 HOH HOH A . 
G 5 HOH 309 1109 72  HOH HOH A . 
G 5 HOH 310 1110 306 HOH HOH A . 
G 5 HOH 311 1111 217 HOH HOH A . 
G 5 HOH 312 1112 317 HOH HOH A . 
G 5 HOH 313 1113 120 HOH HOH A . 
G 5 HOH 314 1114 330 HOH HOH A . 
G 5 HOH 315 1115 291 HOH HOH A . 
G 5 HOH 316 1116 338 HOH HOH A . 
G 5 HOH 317 1117 139 HOH HOH A . 
G 5 HOH 318 1118 242 HOH HOH A . 
G 5 HOH 319 1119 301 HOH HOH A . 
G 5 HOH 320 1120 285 HOH HOH A . 
G 5 HOH 321 1121 183 HOH HOH A . 
G 5 HOH 322 1122 321 HOH HOH A . 
G 5 HOH 323 1123 160 HOH HOH A . 
G 5 HOH 324 1124 340 HOH HOH A . 
G 5 HOH 325 1125 203 HOH HOH A . 
G 5 HOH 326 1126 152 HOH HOH A . 
G 5 HOH 327 1127 287 HOH HOH A . 
G 5 HOH 328 1128 300 HOH HOH A . 
G 5 HOH 329 1129 73  HOH HOH A . 
G 5 HOH 330 1130 316 HOH HOH A . 
G 5 HOH 331 1131 267 HOH HOH A . 
G 5 HOH 332 1132 313 HOH HOH A . 
G 5 HOH 333 1133 343 HOH HOH A . 
G 5 HOH 334 1134 310 HOH HOH A . 
G 5 HOH 335 1135 279 HOH HOH A . 
G 5 HOH 336 1136 312 HOH HOH A . 
G 5 HOH 337 1137 89  HOH HOH A . 
G 5 HOH 338 1138 275 HOH HOH A . 
G 5 HOH 339 1139 122 HOH HOH A . 
G 5 HOH 340 1140 240 HOH HOH A . 
G 5 HOH 341 1141 268 HOH HOH A . 
G 5 HOH 342 1142 264 HOH HOH A . 
G 5 HOH 343 1143 108 HOH HOH A . 
G 5 HOH 344 1144 284 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.12 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EJ3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.851 
_cell.length_a_esd                 ? 
_cell.length_b                     119.770 
_cell.length_b_esd                 ? 
_cell.length_c                     60.546 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EJ3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EJ3 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.89 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES-OH, 10 mM GTP, 100 mM MnCl2, 18-28% PEG 3350, 10 mg/mL rcPEPCK.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     253 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.1271 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CHESS BEAMLINE 7B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1271 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   7B2 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          59.23 
_reflns.entry_id                                       9EJ3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               119.55 
_reflns.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.number_all                                     ? 
_reflns.number_obs                                     49496 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.64 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.81 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.1900 
_reflns.pdbx_Rpim_I_all                                0.0730 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.987 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.1750 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.85 
_reflns_shell.d_res_low                                     1.88 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2430 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.84 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.703 
_reflns_shell.pdbx_Rpim_I_all                               0.647 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.626 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.59 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.574 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EJ3 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             59.88 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     49337 
_refine.ls_number_reflns_R_free                  2448 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.04 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1719 
_refine.ls_R_factor_R_free                       0.2096 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1699 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.27 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        59.88 
_refine_hist.number_atoms_solvent             344 
_refine_hist.number_atoms_total               5258 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4869 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.070  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.762 ? 1915 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064  ? 722  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 898  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.86 1.89  . . 135 2565 91.00 . . . . 0.2999 . . . . . . . . . . . 0.3628 
'X-RAY DIFFRACTION' 1.89 1.93  . . 162 2690 97.00 . . . . 0.2721 . . . . . . . . . . . 0.3144 
'X-RAY DIFFRACTION' 1.93 1.98  . . 150 2727 98.00 . . . . 0.2435 . . . . . . . . . . . 0.3147 
'X-RAY DIFFRACTION' 1.98 2.03  . . 113 2797 98.00 . . . . 0.2290 . . . . . . . . . . . 0.2983 
'X-RAY DIFFRACTION' 2.03 2.08  . . 127 2731 98.00 . . . . 0.2155 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 2.08 2.14  . . 145 2754 98.00 . . . . 0.1940 . . . . . . . . . . . 0.2429 
'X-RAY DIFFRACTION' 2.14 2.21  . . 146 2748 98.00 . . . . 0.1784 . . . . . . . . . . . 0.2381 
'X-RAY DIFFRACTION' 2.21 2.29  . . 168 2719 98.00 . . . . 0.1732 . . . . . . . . . . . 0.2168 
'X-RAY DIFFRACTION' 2.29 2.39  . . 130 2790 99.00 . . . . 0.1675 . . . . . . . . . . . 0.2323 
'X-RAY DIFFRACTION' 2.39 2.49  . . 147 2775 98.00 . . . . 0.1689 . . . . . . . . . . . 0.2258 
'X-RAY DIFFRACTION' 2.49 2.63  . . 138 2789 99.00 . . . . 0.1721 . . . . . . . . . . . 0.2311 
'X-RAY DIFFRACTION' 2.63 2.79  . . 126 2805 99.00 . . . . 0.1712 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 2.79 3.00  . . 134 2793 99.00 . . . . 0.1780 . . . . . . . . . . . 0.2122 
'X-RAY DIFFRACTION' 3.01 3.31  . . 166 2752 99.00 . . . . 0.1647 . . . . . . . . . . . 0.2178 
'X-RAY DIFFRACTION' 3.31 3.79  . . 155 2817 99.00 . . . . 0.1523 . . . . . . . . . . . 0.2022 
'X-RAY DIFFRACTION' 3.79 4.77  . . 153 2789 99.00 . . . . 0.1348 . . . . . . . . . . . 0.1501 
'X-RAY DIFFRACTION' 4.77 59.88 . . 153 2848 99.00 . . . . 0.1471 . . . . . . . . . . . 0.1686 
# 
_struct.entry_id                     9EJ3 
_struct.title                        'Rat cytosolic PEPCK in complex with GTP and beta-sulfopyruvate (253K)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EJ3 
_struct_keywords.text            'Inhibitor complex, Metabolic enzyme, Multi-temperature, Ambient temperature, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 3 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PCKGC_RAT 
_struct_ref.pdbx_db_accession          P07379 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EJ3 
_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                 622 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07379 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  622 
_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       622 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PHE A 11  ? ALA A 13  ? PHE A 11  ALA A 13  5 ? 3  
HELX_P HELX_P2  AA2 PRO A 24  ? GLN A 39  ? PRO A 24  GLN A 39  1 ? 16 
HELX_P HELX_P3  AA3 SER A 49  ? GLU A 63  ? SER A 49  GLU A 63  1 ? 15 
HELX_P HELX_P4  AA4 ILE A 88  ? SER A 90  ? ILE A 88  SER A 90  5 ? 3  
HELX_P HELX_P5  AA5 GLU A 98  ? THR A 102 ? GLU A 98  THR A 102 5 ? 5  
HELX_P HELX_P6  AA6 SER A 118 ? ALA A 128 ? SER A 118 ALA A 128 1 ? 11 
HELX_P HELX_P7  AA7 SER A 163 ? THR A 174 ? SER A 163 THR A 174 1 ? 12 
HELX_P HELX_P8  AA8 GLY A 177 ? GLY A 185 ? GLY A 177 GLY A 185 1 ? 9  
HELX_P HELX_P9  AA9 LEU A 206 ? TRP A 210 ? LEU A 206 TRP A 210 5 ? 5  
HELX_P HELX_P10 AB1 ASN A 213 ? THR A 217 ? ASN A 213 THR A 217 5 ? 5  
HELX_P HELX_P11 AB2 TYR A 235 ? LEU A 240 ? TYR A 235 LEU A 240 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P13 AB4 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P14 AB5 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P15 AB6 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P16 AB7 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P17 AB8 PRO A 479 ? MET A 482 ? PRO A 479 MET A 482 5 ? 4  
HELX_P HELX_P18 AB9 ASN A 489 ? MET A 500 ? ASN A 489 MET A 500 1 ? 12 
HELX_P HELX_P19 AC1 ALA A 501 ? ARG A 503 ? ALA A 501 ARG A 503 5 ? 3  
HELX_P HELX_P20 AC2 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P21 AC3 ASN A 533 ? GLY A 546 ? ASN A 533 GLY A 546 1 ? 14 
HELX_P HELX_P22 AC4 ASN A 573 ? PHE A 578 ? ASN A 573 PHE A 578 1 ? 6  
HELX_P HELX_P23 AC5 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P24 AC6 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P25 AC7 PRO A 605 ? GLN A 621 ? PRO A 605 GLN A 621 1 ? 17 
# 
_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 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A LYS 244 NZ  ? ? ? 1_555 B MN  . MN  ? ? A LYS 244 A MN  701  1_555 ? ? ? ? ? ? ? 2.396 ? ? 
metalc2  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 B MN  . MN  ? ? A HIS 264 A MN  701  1_555 ? ? ? ? ? ? ? 2.285 ? ? 
metalc3  metalc ? ? A THR 291 OG1 ? ? ? 1_555 C MN  . MN  ? ? A THR 291 A MN  702  1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc4  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 B MN  . MN  ? ? A ASP 311 A MN  701  1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc5  metalc ? ? A GLU 607 OE2 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703  1_555 ? ? ? ? ? ? ? 2.704 ? ? 
metalc6  metalc ? ? B MN  .   MN  ? ? ? 1_555 E SPV . O1  ? ? A MN  701 A SPV 704  1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc7  metalc ? ? B MN  .   MN  ? ? ? 1_555 E SPV . O2  ? ? A MN  701 A SPV 704  1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc8  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1G A ? A MN  701 A GTP 705  1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1G B ? A MN  701 A GTP 705  1_555 ? ? ? ? ? ? ? 2.146 ? ? 
metalc10 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O3G A ? A MN  702 A GTP 705  1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc11 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O3G B ? A MN  702 A GTP 705  1_555 ? ? ? ? ? ? ? 2.268 ? ? 
metalc12 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O2B A ? A MN  702 A GTP 705  1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O2B B ? A MN  702 A GTP 705  1_555 ? ? ? ? ? ? ? 2.152 ? ? 
metalc14 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 888  1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc15 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 910  1_555 ? ? ? ? ? ? ? 2.361 ? ? 
metalc16 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 921  1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc17 metalc ? ? D MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  703 A HOH 1061 1_555 ? ? ? ? ? ? ? 2.693 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 NE2 ? A HIS 264 ? A HIS 264  ? 1_555 82.2  ? 
2  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 OD1 ? A ASP 311 ? A ASP 311  ? 1_555 91.0  ? 
3  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 OD1 ? A ASP 311 ? A ASP 311  ? 1_555 92.1  ? 
4  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1  ? E SPV .   ? A SPV 704  ? 1_555 96.2  ? 
5  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1  ? E SPV .   ? A SPV 704  ? 1_555 98.1  ? 
6  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1  ? E SPV .   ? A SPV 704  ? 1_555 168.2 ? 
7  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2  ? E SPV .   ? A SPV 704  ? 1_555 93.0  ? 
8  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2  ? E SPV .   ? A SPV 704  ? 1_555 170.2 ? 
9  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2  ? E SPV .   ? A SPV 704  ? 1_555 96.5  ? 
10 O1  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2  ? E SPV .   ? A SPV 704  ? 1_555 73.8  ? 
11 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G A F GTP .   ? A GTP 705  ? 1_555 173.0 ? 
12 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G A F GTP .   ? A GTP 705  ? 1_555 103.2 ? 
13 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G A F GTP .   ? A GTP 705  ? 1_555 84.3  ? 
14 O1  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G A F GTP .   ? A GTP 705  ? 1_555 87.6  ? 
15 O2  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G A F GTP .   ? A GTP 705  ? 1_555 82.4  ? 
16 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G B F GTP .   ? A GTP 705  ? 1_555 178.0 ? 
17 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G B F GTP .   ? A GTP 705  ? 1_555 95.8  ? 
18 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G B F GTP .   ? A GTP 705  ? 1_555 89.4  ? 
19 O1  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G B F GTP .   ? A GTP 705  ? 1_555 83.7  ? 
20 O2  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G B F GTP .   ? A GTP 705  ? 1_555 89.0  ? 
21 O1G A F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1G B F GTP .   ? A GTP 705  ? 1_555 8.9   ? 
22 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G A F GTP .   ? A GTP 705  ? 1_555 170.8 ? 
23 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G B F GTP .   ? A GTP 705  ? 1_555 170.8 ? 
24 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G B F GTP .   ? A GTP 705  ? 1_555 17.3  ? 
25 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B A F GTP .   ? A GTP 705  ? 1_555 92.9  ? 
26 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B A F GTP .   ? A GTP 705  ? 1_555 86.7  ? 
27 O3G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B A F GTP .   ? A GTP 705  ? 1_555 93.5  ? 
28 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B B F GTP .   ? A GTP 705  ? 1_555 88.2  ? 
29 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B B F GTP .   ? A GTP 705  ? 1_555 89.4  ? 
30 O3G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B B F GTP .   ? A GTP 705  ? 1_555 99.5  ? 
31 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O2B B F GTP .   ? A GTP 705  ? 1_555 13.3  ? 
32 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 888  ? 1_555 84.4  ? 
33 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 888  ? 1_555 86.5  ? 
34 O3G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 888  ? 1_555 101.2 ? 
35 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 888  ? 1_555 98.3  ? 
36 O2B B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 888  ? 1_555 85.4  ? 
37 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 910  ? 1_555 84.2  ? 
38 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 910  ? 1_555 98.6  ? 
39 O3G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 910  ? 1_555 87.9  ? 
40 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 910  ? 1_555 164.7 ? 
41 O2B B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 910  ? 1_555 171.9 ? 
42 O   ? G HOH .   ? A HOH 888 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 910  ? 1_555 96.4  ? 
43 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 98.2  ? 
44 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 90.8  ? 
45 O3G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 76.5  ? 
46 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 79.1  ? 
47 O2B B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 92.1  ? 
48 O   ? G HOH .   ? A HOH 888 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 176.3 ? 
49 O   ? G HOH .   ? A HOH 910 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 921  ? 1_555 86.4  ? 
50 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 1061 ? 1_555 66.7  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           200 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            200 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    201 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     201 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.47 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 7 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA1 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA1 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA1 4 LYS A 155 ? THR A 161 ? LYS A 155 THR A 161 
AA1 5 ILE A 190 ? SER A 195 ? ILE A 190 SER A 195 
AA1 6 GLU A 227 ? PHE A 231 ? GLU A 227 PHE A 231 
AA1 7 LEU A 218 ? LEU A 222 ? LEU A 218 LEU A 222 
AA1 8 THR A 92  ? ILE A 95  ? THR A 92  ILE A 95  
AA1 9 TRP A 116 ? MET A 117 ? TRP A 116 MET A 117 
AA2 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA2 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA2 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA2 4 ARG A 175 ? MET A 176 ? ARG A 175 MET A 176 
AA3 1 ILE A 66  ? LYS A 68  ? ILE A 66  LYS A 68  
AA3 2 TRP A 76  ? ALA A 78  ? TRP A 76  ALA A 78  
AA3 3 ILE A 356 ? THR A 358 ? ILE A 356 THR A 358 
AA3 4 ARG A 405 ? PRO A 409 ? ARG A 405 PRO A 409 
AA3 5 GLY A 331 ? VAL A 335 ? GLY A 331 VAL A 335 
AA4 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA4 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA4 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA4 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA4 5 LYS A 277 ? ALA A 283 ? LYS A 277 ALA A 283 
AA4 6 LEU A 266 ? THR A 271 ? LEU A 266 THR A 271 
AA4 7 LYS A 304 ? GLY A 309 ? LYS A 304 GLY A 309 
AA5 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA5 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA5 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA5 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA5 5 LYS A 510 ? VAL A 514 ? LYS A 510 VAL A 514 
AA5 6 VAL A 444 ? GLU A 446 ? VAL A 444 GLU A 446 
AA6 1 VAL A 368 ? TYR A 369 ? VAL A 368 TYR A 369 
AA6 2 ALA A 361 ? THR A 363 ? ALA A 361 THR A 363 
AA6 3 ILE A 383 ? THR A 384 ? ILE A 383 THR A 384 
AA6 4 GLU A 390 ? TRP A 391 ? GLU A 390 TRP A 391 
AA7 1 ARG A 461 ? GLU A 463 ? ARG A 461 GLU A 463 
AA7 2 ILE A 475 ? HIS A 477 ? ILE A 475 HIS A 477 
AA8 1 ALA A 550 ? THR A 553 ? ALA A 550 THR A 553 
AA8 2 GLY A 556 ? PRO A 559 ? GLY A 556 PRO A 559 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 16  ? N ILE A 16  O ILE A 43  ? O ILE A 43  
AA1 2 3 N TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
AA1 3 4 N TYR A 140 ? N TYR A 140 O THR A 161 ? O THR A 161 
AA1 4 5 N ILE A 158 ? N ILE A 158 O CYS A 192 ? O CYS A 192 
AA1 5 6 N LYS A 191 ? N LYS A 191 O ILE A 228 ? O ILE A 228 
AA1 6 7 O ILE A 229 ? O ILE A 229 N ALA A 220 ? N ALA A 220 
AA1 7 8 O HIS A 221 ? O HIS A 221 N ILE A 95  ? N ILE A 95  
AA1 8 9 N ILE A 94  ? N ILE A 94  O MET A 117 ? O MET A 117 
AA2 1 2 N ILE A 16  ? N ILE A 16  O ILE A 43  ? O ILE A 43  
AA2 2 3 N TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
AA2 3 4 N SER A 145 ? N SER A 145 O ARG A 175 ? O ARG A 175 
AA3 1 2 N ARG A 67  ? N ARG A 67  O LEU A 77  ? O LEU A 77  
AA3 2 3 N TRP A 76  ? N TRP A 76  O PHE A 357 ? O PHE A 357 
AA3 3 4 N THR A 358 ? N THR A 358 O ARG A 405 ? O ARG A 405 
AA3 4 5 O THR A 408 ? O THR A 408 N PHE A 332 ? N PHE A 332 
AA4 1 2 N GLU A 263 ? N GLU A 263 O ALA A 313 ? O ALA A 313 
AA4 2 3 N TRP A 314 ? N TRP A 314 O ILE A 326 ? O ILE A 326 
AA4 3 4 N LEU A 323 ? N LEU A 323 O ILE A 428 ? O ILE A 428 
AA4 4 5 O ILE A 432 ? O ILE A 432 N ALA A 283 ? N ALA A 283 
AA4 5 6 O LYS A 278 ? O LYS A 278 N ILE A 270 ? N ILE A 270 
AA4 6 7 N GLY A 269 ? N GLY A 269 O GLU A 306 ? O GLU A 306 
AA5 1 2 N GLU A 263 ? N GLU A 263 O ALA A 313 ? O ALA A 313 
AA5 2 3 N TRP A 314 ? N TRP A 314 O ILE A 326 ? O ILE A 326 
AA5 3 4 N LEU A 323 ? N LEU A 323 O ILE A 428 ? O ILE A 428 
AA5 4 5 N PHE A 433 ? N PHE A 433 O VAL A 514 ? O VAL A 514 
AA5 5 6 O HIS A 513 ? O HIS A 513 N TYR A 445 ? N TYR A 445 
AA6 1 2 O TYR A 369 ? O TYR A 369 N ALA A 361 ? N ALA A 361 
AA6 2 3 N GLU A 362 ? N GLU A 362 O THR A 384 ? O THR A 384 
AA6 3 4 N ILE A 383 ? N ILE A 383 O TRP A 391 ? O TRP A 391 
AA7 1 2 N SER A 462 ? N SER A 462 O MET A 476 ? O MET A 476 
AA8 1 2 N LYS A 551 ? N LYS A 551 O VAL A 558 ? O VAL A 558 
# 
_pdbx_entry_details.entry_id                   9EJ3 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OH  A TYR 606  ? ? O A HOH 801  ? ? 2.04 
2 1 O   A HOH 1035 ? ? O A HOH 1127 ? ? 2.14 
3 1 O   A HOH 1053 ? ? O A HOH 1120 ? ? 2.15 
4 1 OE2 A GLU 586  ? ? O A HOH 802  ? ? 2.16 
5 1 NZ  A LYS 507  ? ? O A HOH 803  ? ? 2.17 
# 
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 HIS A 6   ? ? -133.43 -123.00 
2  1 ASN A 7   ? ? -152.35 38.52   
3  1 SER A 108 ? ? -131.87 -38.64  
4  1 LYS A 243 ? ? -85.57  -83.93  
5  1 ASP A 311 ? ? -152.15 -41.29  
6  1 PHE A 333 ? ? -113.58 77.09   
7  1 ASN A 344 ? ? -159.63 71.29   
8  1 THR A 465 ? ? -124.96 -123.40 
9  1 ALA A 466 ? ? -156.29 60.07   
10 1 ALA A 468 ? ? -102.44 -133.23 
11 1 LYS A 473 ? ? -107.17 63.20   
12 1 PHE A 480 ? ? 59.17   14.56   
13 1 ALA A 505 ? ? 58.89   19.66   
14 1 PHE A 530 ? ? 52.70   -127.01 
15 1 ASN A 565 ? ? -69.81  98.59   
16 1 ASN A 601 ? ? 52.74   -119.36 
# 
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 MET 1 ? A MET 1 
2 1 Y 1 A PRO 2 ? A PRO 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
GTP PG     P  N N 137 
GTP O1G    O  N N 138 
GTP O2G    O  N N 139 
GTP O3G    O  N N 140 
GTP O3B    O  N N 141 
GTP PB     P  N N 142 
GTP O1B    O  N N 143 
GTP O2B    O  N N 144 
GTP O3A    O  N N 145 
GTP PA     P  N N 146 
GTP O1A    O  N N 147 
GTP O2A    O  N N 148 
GTP "O5'"  O  N N 149 
GTP "C5'"  C  N N 150 
GTP "C4'"  C  N R 151 
GTP "O4'"  O  N N 152 
GTP "C3'"  C  N S 153 
GTP "O3'"  O  N N 154 
GTP "C2'"  C  N R 155 
GTP "O2'"  O  N N 156 
GTP "C1'"  C  N R 157 
GTP N9     N  Y N 158 
GTP C8     C  Y N 159 
GTP N7     N  Y N 160 
GTP C5     C  Y N 161 
GTP C6     C  N N 162 
GTP O6     O  N N 163 
GTP N1     N  N N 164 
GTP C2     C  N N 165 
GTP N2     N  N N 166 
GTP N3     N  N N 167 
GTP C4     C  Y N 168 
GTP HOG2   H  N N 169 
GTP HOG3   H  N N 170 
GTP HOB2   H  N N 171 
GTP HOA2   H  N N 172 
GTP "H5'"  H  N N 173 
GTP "H5''" H  N N 174 
GTP "H4'"  H  N N 175 
GTP "H3'"  H  N N 176 
GTP "HO3'" H  N N 177 
GTP "H2'"  H  N N 178 
GTP "HO2'" H  N N 179 
GTP "H1'"  H  N N 180 
GTP H8     H  N N 181 
GTP HN1    H  N N 182 
GTP HN21   H  N N 183 
GTP HN22   H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MN  MN     MN N N 298 
PHE N      N  N N 299 
PHE CA     C  N S 300 
PHE C      C  N N 301 
PHE O      O  N N 302 
PHE CB     C  N N 303 
PHE CG     C  Y N 304 
PHE CD1    C  Y N 305 
PHE CD2    C  Y N 306 
PHE CE1    C  Y N 307 
PHE CE2    C  Y N 308 
PHE CZ     C  Y N 309 
PHE OXT    O  N N 310 
PHE H      H  N N 311 
PHE H2     H  N N 312 
PHE HA     H  N N 313 
PHE HB2    H  N N 314 
PHE HB3    H  N N 315 
PHE HD1    H  N N 316 
PHE HD2    H  N N 317 
PHE HE1    H  N N 318 
PHE HE2    H  N N 319 
PHE HZ     H  N N 320 
PHE HXT    H  N N 321 
PRO N      N  N N 322 
PRO CA     C  N S 323 
PRO C      C  N N 324 
PRO O      O  N N 325 
PRO CB     C  N N 326 
PRO CG     C  N N 327 
PRO CD     C  N N 328 
PRO OXT    O  N N 329 
PRO H      H  N N 330 
PRO HA     H  N N 331 
PRO HB2    H  N N 332 
PRO HB3    H  N N 333 
PRO HG2    H  N N 334 
PRO HG3    H  N N 335 
PRO HD2    H  N N 336 
PRO HD3    H  N N 337 
PRO HXT    H  N N 338 
SER N      N  N N 339 
SER CA     C  N S 340 
SER C      C  N N 341 
SER O      O  N N 342 
SER CB     C  N N 343 
SER OG     O  N N 344 
SER OXT    O  N N 345 
SER H      H  N N 346 
SER H2     H  N N 347 
SER HA     H  N N 348 
SER HB2    H  N N 349 
SER HB3    H  N N 350 
SER HG     H  N N 351 
SER HXT    H  N N 352 
SPV C1     C  N N 353 
SPV O1     O  N N 354 
SPV "O2'"  O  N N 355 
SPV C2     C  N N 356 
SPV C3     C  N N 357 
SPV O2     O  N N 358 
SPV S      S  N N 359 
SPV O1S    O  N N 360 
SPV O2S    O  N N 361 
SPV O3S    O  N N 362 
SPV "H2'O" H  N N 363 
SPV H31    H  N N 364 
SPV H32    H  N N 365 
SPV H2SO   H  N N 366 
THR N      N  N N 367 
THR CA     C  N S 368 
THR C      C  N N 369 
THR O      O  N N 370 
THR CB     C  N R 371 
THR OG1    O  N N 372 
THR CG2    C  N N 373 
THR OXT    O  N N 374 
THR H      H  N N 375 
THR H2     H  N N 376 
THR HA     H  N N 377 
THR HB     H  N N 378 
THR HG1    H  N N 379 
THR HG21   H  N N 380 
THR HG22   H  N N 381 
THR HG23   H  N N 382 
THR HXT    H  N N 383 
TRP N      N  N N 384 
TRP CA     C  N S 385 
TRP C      C  N N 386 
TRP O      O  N N 387 
TRP CB     C  N N 388 
TRP CG     C  Y N 389 
TRP CD1    C  Y N 390 
TRP CD2    C  Y N 391 
TRP NE1    N  Y N 392 
TRP CE2    C  Y N 393 
TRP CE3    C  Y N 394 
TRP CZ2    C  Y N 395 
TRP CZ3    C  Y N 396 
TRP CH2    C  Y N 397 
TRP OXT    O  N N 398 
TRP H      H  N N 399 
TRP H2     H  N N 400 
TRP HA     H  N N 401 
TRP HB2    H  N N 402 
TRP HB3    H  N N 403 
TRP HD1    H  N N 404 
TRP HE1    H  N N 405 
TRP HE3    H  N N 406 
TRP HZ2    H  N N 407 
TRP HZ3    H  N N 408 
TRP HH2    H  N N 409 
TRP HXT    H  N N 410 
TYR N      N  N N 411 
TYR CA     C  N S 412 
TYR C      C  N N 413 
TYR O      O  N N 414 
TYR CB     C  N N 415 
TYR CG     C  Y N 416 
TYR CD1    C  Y N 417 
TYR CD2    C  Y N 418 
TYR CE1    C  Y N 419 
TYR CE2    C  Y N 420 
TYR CZ     C  Y N 421 
TYR OH     O  N N 422 
TYR OXT    O  N N 423 
TYR H      H  N N 424 
TYR H2     H  N N 425 
TYR HA     H  N N 426 
TYR HB2    H  N N 427 
TYR HB3    H  N N 428 
TYR HD1    H  N N 429 
TYR HD2    H  N N 430 
TYR HE1    H  N N 431 
TYR HE2    H  N N 432 
TYR HH     H  N N 433 
TYR HXT    H  N N 434 
VAL N      N  N N 435 
VAL CA     C  N S 436 
VAL C      C  N N 437 
VAL O      O  N N 438 
VAL CB     C  N N 439 
VAL CG1    C  N N 440 
VAL CG2    C  N N 441 
VAL OXT    O  N N 442 
VAL H      H  N N 443 
VAL H2     H  N N 444 
VAL HA     H  N N 445 
VAL HB     H  N N 446 
VAL HG11   H  N N 447 
VAL HG12   H  N N 448 
VAL HG13   H  N N 449 
VAL HG21   H  N N 450 
VAL HG22   H  N N 451 
VAL HG23   H  N N 452 
VAL HXT    H  N N 453 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
GTP PG    O1G    doub N N 129 
GTP PG    O2G    sing N N 130 
GTP PG    O3G    sing N N 131 
GTP PG    O3B    sing N N 132 
GTP O2G   HOG2   sing N N 133 
GTP O3G   HOG3   sing N N 134 
GTP O3B   PB     sing N N 135 
GTP PB    O1B    doub N N 136 
GTP PB    O2B    sing N N 137 
GTP PB    O3A    sing N N 138 
GTP O2B   HOB2   sing N N 139 
GTP O3A   PA     sing N N 140 
GTP PA    O1A    doub N N 141 
GTP PA    O2A    sing N N 142 
GTP PA    "O5'"  sing N N 143 
GTP O2A   HOA2   sing N N 144 
GTP "O5'" "C5'"  sing N N 145 
GTP "C5'" "C4'"  sing N N 146 
GTP "C5'" "H5'"  sing N N 147 
GTP "C5'" "H5''" sing N N 148 
GTP "C4'" "O4'"  sing N N 149 
GTP "C4'" "C3'"  sing N N 150 
GTP "C4'" "H4'"  sing N N 151 
GTP "O4'" "C1'"  sing N N 152 
GTP "C3'" "O3'"  sing N N 153 
GTP "C3'" "C2'"  sing N N 154 
GTP "C3'" "H3'"  sing N N 155 
GTP "O3'" "HO3'" sing N N 156 
GTP "C2'" "O2'"  sing N N 157 
GTP "C2'" "C1'"  sing N N 158 
GTP "C2'" "H2'"  sing N N 159 
GTP "O2'" "HO2'" sing N N 160 
GTP "C1'" N9     sing N N 161 
GTP "C1'" "H1'"  sing N N 162 
GTP N9    C8     sing Y N 163 
GTP N9    C4     sing Y N 164 
GTP C8    N7     doub Y N 165 
GTP C8    H8     sing N N 166 
GTP N7    C5     sing Y N 167 
GTP C5    C6     sing N N 168 
GTP C5    C4     doub Y N 169 
GTP C6    O6     doub N N 170 
GTP C6    N1     sing N N 171 
GTP N1    C2     sing N N 172 
GTP N1    HN1    sing N N 173 
GTP C2    N2     sing N N 174 
GTP C2    N3     doub N N 175 
GTP N2    HN21   sing N N 176 
GTP N2    HN22   sing N N 177 
GTP N3    C4     sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
SPV C1    O1     doub N N 340 
SPV C1    "O2'"  sing N N 341 
SPV C1    C2     sing N N 342 
SPV "O2'" "H2'O" sing N N 343 
SPV C2    C3     sing N N 344 
SPV C2    O2     doub N N 345 
SPV C3    S      sing N N 346 
SPV C3    H31    sing N N 347 
SPV C3    H32    sing N N 348 
SPV S     O1S    doub N N 349 
SPV S     O2S    sing N N 350 
SPV S     O3S    doub N N 351 
SPV O2S   H2SO   sing N N 352 
THR N     CA     sing N N 353 
THR N     H      sing N N 354 
THR N     H2     sing N N 355 
THR CA    C      sing N N 356 
THR CA    CB     sing N N 357 
THR CA    HA     sing N N 358 
THR C     O      doub N N 359 
THR C     OXT    sing N N 360 
THR CB    OG1    sing N N 361 
THR CB    CG2    sing N N 362 
THR CB    HB     sing N N 363 
THR OG1   HG1    sing N N 364 
THR CG2   HG21   sing N N 365 
THR CG2   HG22   sing N N 366 
THR CG2   HG23   sing N N 367 
THR OXT   HXT    sing N N 368 
TRP N     CA     sing N N 369 
TRP N     H      sing N N 370 
TRP N     H2     sing N N 371 
TRP CA    C      sing N N 372 
TRP CA    CB     sing N N 373 
TRP CA    HA     sing N N 374 
TRP C     O      doub N N 375 
TRP C     OXT    sing N N 376 
TRP CB    CG     sing N N 377 
TRP CB    HB2    sing N N 378 
TRP CB    HB3    sing N N 379 
TRP CG    CD1    doub Y N 380 
TRP CG    CD2    sing Y N 381 
TRP CD1   NE1    sing Y N 382 
TRP CD1   HD1    sing N N 383 
TRP CD2   CE2    doub Y N 384 
TRP CD2   CE3    sing Y N 385 
TRP NE1   CE2    sing Y N 386 
TRP NE1   HE1    sing N N 387 
TRP CE2   CZ2    sing Y N 388 
TRP CE3   CZ3    doub Y N 389 
TRP CE3   HE3    sing N N 390 
TRP CZ2   CH2    doub Y N 391 
TRP CZ2   HZ2    sing N N 392 
TRP CZ3   CH2    sing Y N 393 
TRP CZ3   HZ3    sing N N 394 
TRP CH2   HH2    sing N N 395 
TRP OXT   HXT    sing N N 396 
TYR N     CA     sing N N 397 
TYR N     H      sing N N 398 
TYR N     H2     sing N N 399 
TYR CA    C      sing N N 400 
TYR CA    CB     sing N N 401 
TYR CA    HA     sing N N 402 
TYR C     O      doub N N 403 
TYR C     OXT    sing N N 404 
TYR CB    CG     sing N N 405 
TYR CB    HB2    sing N N 406 
TYR CB    HB3    sing N N 407 
TYR CG    CD1    doub Y N 408 
TYR CG    CD2    sing Y N 409 
TYR CD1   CE1    sing Y N 410 
TYR CD1   HD1    sing N N 411 
TYR CD2   CE2    doub Y N 412 
TYR CD2   HD2    sing N N 413 
TYR CE1   CZ     doub Y N 414 
TYR CE1   HE1    sing N N 415 
TYR CE2   CZ     sing Y N 416 
TYR CE2   HE2    sing N N 417 
TYR CZ    OH     sing N N 418 
TYR OH    HH     sing N N 419 
TYR OXT   HXT    sing N N 420 
VAL N     CA     sing N N 421 
VAL N     H      sing N N 422 
VAL N     H2     sing N N 423 
VAL CA    C      sing N N 424 
VAL CA    CB     sing N N 425 
VAL CA    HA     sing N N 426 
VAL C     O      doub N N 427 
VAL C     OXT    sing N N 428 
VAL CB    CG1    sing N N 429 
VAL CB    CG2    sing N N 430 
VAL CB    HB     sing N N 431 
VAL CG1   HG11   sing N N 432 
VAL CG1   HG12   sing N N 433 
VAL CG1   HG13   sing N N 434 
VAL CG2   HG21   sing N N 435 
VAL CG2   HG22   sing N N 436 
VAL CG2   HG23   sing N N 437 
VAL OXT   HXT    sing N N 438 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' DBI-2210041     1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 5R01GM127528-02 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3DT2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EJ3 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.022296 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008612 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008349 
_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]   0.017706 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . PRO A 1 3   ? 2.921   -12.853 -32.152 1.00 51.58  ? 3    PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 3.549   -13.882 -32.991 1.00 46.50  ? 3    PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 4.711   -14.576 -32.286 1.00 46.51  ? 3    PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 5.020   -14.255 -31.135 1.00 48.60  ? 3    PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 4.039   -13.092 -34.212 1.00 46.22  ? 3    PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 4.283   -11.695 -33.694 1.00 51.21  ? 3    PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 3.274   -11.483 -32.579 1.00 50.79  ? 3    PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 5.317   -15.549 -32.959 1.00 40.14  ? 4    GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 6.473   -16.262 -32.430 1.00 42.75  ? 4    GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 7.054   -17.115 -33.550 1.00 36.68  ? 4    GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 6.331   -17.572 -34.438 1.00 38.71  ? 4    GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 6.112   -17.127 -31.202 1.00 51.41  ? 4    GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 4.864   -17.981 -31.358 1.00 49.79  ? 4    GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 4.560   -18.859 -30.133 1.00 60.53  ? 4    GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 5.305   -18.871 -29.142 1.00 52.09  ? 4    GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 3.457   -19.602 -30.210 1.00 52.05  ? 4    GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 8.367   -17.286 -33.526 1.00 36.06  ? 5    LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 9.014   -18.161 -34.502 1.00 37.94  ? 5    LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 9.122   -19.589 -34.007 1.00 37.25  ? 5    LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 9.429   -20.496 -34.794 1.00 33.04  ? 5    LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 10.411  -17.646 -34.838 1.00 36.51  ? 5    LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 10.430  -16.360 -35.650 1.00 34.40  ? 5    LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 11.812  -15.731 -35.560 1.00 35.11  ? 5    LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 10.049  -16.689 -37.083 1.00 36.60  ? 5    LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 8.894   -19.791 -32.715 1.00 37.83  ? 6    HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 8.946   -21.098 -32.083 1.00 46.56  ? 6    HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 7.716   -21.269 -31.196 1.00 49.08  ? 6    HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 6.581   -21.135 -31.672 1.00 48.73  ? 6    HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 10.248  -21.240 -31.288 1.00 36.79  ? 6    HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 11.475  -21.175 -32.143 1.00 44.87  ? 6    HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 12.188  -20.008 -32.331 1.00 40.77  ? 6    HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 12.098  -22.123 -32.887 1.00 36.25  ? 6    HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 13.207  -20.242 -33.140 1.00 38.15  ? 6    HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 13.177  -21.517 -33.494 1.00 41.07  ? 6    HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 7.930   -21.536 -29.908 1.00 52.19  ? 7    ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 6.825   -21.719 -28.971 1.00 67.97  ? 7    ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 7.256   -21.337 -27.563 1.00 73.35  ? 7    ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 6.881   -21.993 -26.585 1.00 71.37  ? 7    ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 6.303   -23.157 -28.991 1.00 63.02  ? 7    ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 5.220   -23.363 -30.020 1.00 68.43  ? 7    ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 4.034   -23.171 -29.733 1.00 70.70  ? 7    ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 5.618   -23.754 -31.234 1.00 67.38  ? 7    ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 8.054   -20.281 -27.445 1.00 121.05 ? 8    GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 8.565   -19.835 -26.168 1.00 120.20 ? 8    GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 7.865   -18.638 -25.568 1.00 120.20 ? 8    GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 8.328   -18.125 -24.541 1.00 120.79 ? 8    GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 6.762   -18.176 -26.159 1.00 65.84  ? 9    LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 6.086   -16.972 -25.692 1.00 60.06  ? 9    LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 4.615   -17.167 -25.347 1.00 48.83  ? 9    LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 4.096   -16.420 -24.510 1.00 48.62  ? 9    LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 6.200   -15.859 -26.743 1.00 53.50  ? 9    LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 7.626   -15.599 -27.231 1.00 55.87  ? 9    LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 7.626   -14.493 -28.266 1.00 49.16  ? 9    LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 8.568   -15.256 -26.079 1.00 56.58  ? 9    LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 3.929   -18.126 -25.970 1.00 44.46  ? 10   ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 2.514   -18.398 -25.708 1.00 44.96  ? 10   ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 2.399   -19.386 -24.544 1.00 36.14  ? 10   ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 2.725   -20.567 -24.697 1.00 32.05  ? 10   ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 1.843   -18.951 -26.967 1.00 41.01  ? 10   ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 0.332   -19.029 -26.849 1.00 43.83  ? 10   ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? -0.207  -18.895 -25.728 1.00 39.79  ? 10   ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? -0.328  -19.220 -27.891 1.00 48.33  ? 10   ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 1.912   -18.914 -23.384 1.00 33.03  ? 11   PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 1.817   -19.760 -22.194 1.00 30.77  ? 11   PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 0.463   -20.439 -22.042 1.00 26.90  ? 11   PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 0.170   -20.959 -20.955 1.00 24.87  ? 11   PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 2.134   -18.951 -20.929 1.00 29.03  ? 11   PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 3.604   -18.913 -20.579 1.00 32.92  ? 11   PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 4.489   -18.147 -21.330 1.00 31.71  ? 11   PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 4.099   -19.630 -19.495 1.00 35.44  ? 11   PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 5.840   -18.104 -21.018 1.00 34.13  ? 11   PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 5.453   -19.596 -19.179 1.00 32.34  ? 11   PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 6.320   -18.820 -19.943 1.00 31.46  ? 11   PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? -0.363  -20.444 -23.099 1.00 24.85  ? 12   SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? -1.692  -21.055 -23.027 1.00 27.19  ? 12   SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? -1.647  -22.503 -22.528 1.00 31.48  ? 12   SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? -2.538  -22.934 -21.776 1.00 30.30  ? 12   SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? -2.365  -21.015 -24.398 1.00 34.10  ? 12   SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? -2.698  -19.717 -24.796 1.00 33.96  ? 12   SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? -0.651  -23.291 -22.975 1.00 26.38  ? 13   ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? -0.617  -24.704 -22.592 1.00 26.95  ? 13   ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? -0.350  -24.914 -21.111 1.00 31.40  ? 13   ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? -0.482  -26.048 -20.635 1.00 27.49  ? 13   ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 0.440   -25.480 -23.396 1.00 29.40  ? 13   ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 0.012   -23.864 -20.373 1.00 27.40  ? 14   LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 0.306   -23.982 -18.953 1.00 26.80  ? 14   LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? -0.798  -23.417 -18.071 1.00 23.17  ? 14   LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? -0.611  -23.348 -16.862 1.00 23.53  ? 14   LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 1.617   -23.267 -18.622 1.00 27.60  ? 14   LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 2.861   -24.078 -18.898 1.00 32.74  ? 14   LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 4.122   -23.245 -18.668 1.00 38.59  ? 14   LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 5.377   -24.132 -18.684 1.00 43.54  ? 14   LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 5.388   -25.044 -19.870 1.00 49.43  ? 14   LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? -1.918  -22.985 -18.646 1.00 20.96  ? 15   VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? -3.008  -22.409 -17.855 1.00 21.43  ? 15   VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? -3.889  -23.536 -17.302 1.00 26.64  ? 15   VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? -4.552  -24.260 -18.057 1.00 28.69  ? 15   VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? -3.825  -21.412 -18.687 1.00 25.18  ? 15   VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? -4.931  -20.801 -17.829 1.00 24.95  ? 15   VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? -2.919  -20.300 -19.225 1.00 24.22  ? 15   VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? -3.915  -23.674 -15.975 1.00 18.24  ? 16   ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? -4.698  -24.717 -15.332 1.00 20.90  ? 16   ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? -6.038  -24.226 -14.808 1.00 26.32  ? 16   ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? -6.832  -25.051 -14.345 1.00 26.74  ? 16   ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? -3.888  -25.385 -14.204 1.00 27.16  ? 16   ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? -3.555  -24.393 -13.102 1.00 24.69  ? 16   ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? -2.605  -26.021 -14.794 1.00 25.60  ? 16   ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? -2.727  -24.961 -11.974 1.00 29.84  ? 16   ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? -6.303  -22.911 -14.838 1.00 26.10  ? 17   GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? -7.637  -22.373 -14.603 1.00 25.87  ? 17   GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? -7.821  -21.081 -15.379 1.00 29.99  ? 17   GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? -6.988  -20.173 -15.282 1.00 25.03  ? 17   GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? -7.909  -22.106 -13.118 1.00 26.40  ? 17   GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? -9.269  -21.463 -12.966 1.00 28.17  ? 17   GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? -9.805  -21.524 -11.574 1.00 34.85  ? 17   GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? -9.977  -22.602 -10.994 1.00 33.15  ? 17   GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? -10.070 -20.354 -11.012 1.00 29.36  ? 17   GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? -8.903  -20.997 -16.144 1.00 23.79  ? 18   GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? -9.166  -19.787 -16.914 1.00 30.40  ? 18   GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? -8.592  -19.838 -18.319 1.00 34.00  ? 18   GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? -8.212  -20.897 -18.839 1.00 36.08  ? 18   GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? -8.531  -18.661 -18.945 1.00 33.91  ? 19   SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? -8.074  -18.546 -20.326 1.00 36.80  ? 19   SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? -7.307  -17.245 -20.526 1.00 36.39  ? 19   SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? -7.806  -16.173 -20.161 1.00 34.12  ? 19   SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? -9.262  -18.591 -21.298 1.00 38.89  ? 19   SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? -8.813  -18.453 -22.636 1.00 46.23  ? 19   SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? -6.114  -17.333 -21.126 1.00 32.84  ? 20   LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? -5.413  -16.108 -21.510 1.00 34.94  ? 20   LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? -6.187  -15.333 -22.571 1.00 39.32  ? 20   LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? -6.154  -14.095 -22.586 1.00 37.74  ? 20   LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? -4.001  -16.423 -22.010 1.00 31.77  ? 20   LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? -2.999  -17.047 -21.028 1.00 31.23  ? 20   LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? -1.731  -17.431 -21.758 1.00 36.61  ? 20   LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? -2.676  -16.128 -19.855 1.00 26.57  ? 20   LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? -6.910  -16.042 -23.444 1.00 41.54  ? 21   ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? -7.712  -15.394 -24.482 1.00 45.92  ? 21   ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? -8.815  -14.512 -23.900 1.00 48.24  ? 21   ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? -9.169  -13.485 -24.498 1.00 52.84  ? 21   ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? -8.332  -16.455 -25.401 1.00 54.63  ? 21   ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? -7.293  -17.266 -26.148 1.00 54.99  ? 21   ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? -6.229  -16.706 -26.475 1.00 53.13  ? 21   ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? -7.542  -18.463 -26.413 1.00 66.82  ? 21   ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? -9.380  -14.898 -22.754 1.00 37.17  ? 22   SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? -10.481 -14.162 -22.136 1.00 41.87  ? 22   SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? -10.032 -12.908 -21.387 1.00 41.69  ? 22   SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? -10.888 -12.109 -20.991 1.00 42.99  ? 22   SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? -11.250 -15.084 -21.174 1.00 35.41  ? 22   SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? -10.455 -15.393 -20.044 1.00 43.52  ? 22   SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? -8.714  -12.716 -21.176 1.00 38.97  ? 23   LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? -8.190  -11.550 -20.477 1.00 39.59  ? 23   LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? -8.191  -10.307 -21.375 1.00 42.39  ? 23   LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? -7.968  -10.407 -22.587 1.00 37.30  ? 23   LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? -6.762  -11.819 -19.996 1.00 38.37  ? 23   LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? -6.570  -12.935 -18.960 1.00 35.27  ? 23   LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? -5.088  -13.094 -18.632 1.00 34.25  ? 23   LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? -7.387  -12.655 -17.683 1.00 35.82  ? 23   LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? -8.416  -9.122  -20.800 1.00 34.56  ? 24   PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? -8.170  -7.886  -21.553 1.00 37.01  ? 24   PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? -6.728  -7.845  -22.028 1.00 35.89  ? 24   PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? -5.826  -8.340  -21.353 1.00 37.97  ? 24   PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? -8.452  -6.777  -20.532 1.00 41.61  ? 24   PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? -9.248  -7.441  -19.445 1.00 44.42  ? 24   PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? -8.745  -8.850  -19.394 1.00 36.53  ? 24   PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? -6.525  -7.233  -23.201 1.00 37.46  ? 25   GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? -5.237  -7.272  -23.892 1.00 40.12  ? 25   GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? -4.067  -6.943  -22.972 1.00 38.09  ? 25   GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? -3.101  -7.705  -22.889 1.00 35.09  ? 25   GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? -5.269  -6.299  -25.074 1.00 49.87  ? 25   GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? -3.899  -5.823  -25.561 1.00 53.20  ? 25   GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? -3.243  -6.800  -26.511 1.00 64.15  ? 25   GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? -3.173  -8.006  -26.241 1.00 65.28  ? 25   GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? -2.762  -6.287  -27.641 1.00 65.18  ? 25   GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? -4.135  -5.806  -22.272 1.00 34.56  ? 26   GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? -3.024  -5.384  -21.422 1.00 39.85  ? 26   GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? -2.834  -6.286  -20.204 1.00 32.62  ? 26   GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? -1.717  -6.378  -19.685 1.00 34.50  ? 26   GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? -3.221  -3.934  -20.960 1.00 43.75  ? 26   GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? -3.076  -2.879  -22.073 1.00 49.45  ? 26   GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? -1.765  -2.998  -22.852 1.00 50.84  ? 26   GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? -0.693  -3.182  -22.229 1.00 48.22  ? 26   GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? -1.815  -2.927  -24.100 1.00 60.86  ? 26   GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? -3.892  -6.931  -19.721 1.00 36.50  ? 27   VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? -3.720  -7.921  -18.660 1.00 30.04  ? 27   VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? -2.984  -9.148  -19.197 1.00 25.53  ? 27   VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? -2.043  -9.657  -18.571 1.00 25.65  ? 27   VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? -5.084  -8.301  -18.054 1.00 32.12  ? 27   VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? -4.909  -9.326  -16.937 1.00 26.17  ? 27   VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? -5.819  -7.059  -17.517 1.00 29.59  ? 27   VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? -3.392  -9.645  -20.367 1.00 28.75  ? 28   ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? -2.652  -10.756 -20.959 1.00 29.33  ? 28   ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? -1.169  -10.431 -21.099 1.00 25.51  ? 28   ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? -0.317  -11.254 -20.749 1.00 30.84  ? 28   ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? -3.232  -11.154 -22.318 1.00 29.06  ? 28   ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? -2.402  -12.304 -22.921 1.00 32.02  ? 28   ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? -3.100  -13.090 -24.040 1.00 39.79  ? 28   ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? -2.193  -14.130 -24.517 1.00 36.48  ? 28   ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? -2.552  -15.189 -25.226 1.00 41.89  ? 28   ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? -3.796  -15.343 -25.657 1.00 40.64  ? 28   ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? -1.641  -16.122 -25.499 1.00 40.05  ? 28   ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? -0.834  -9.246  -21.620 1.00 28.14  ? 29   LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 0.576   -8.898  -21.802 1.00 26.94  ? 29   LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 1.321   -8.894  -20.478 1.00 23.87  ? 29   LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 2.476   -9.319  -20.404 1.00 24.67  ? 29   LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 0.712   -7.508  -22.463 1.00 32.50  ? 29   LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 0.236   -7.400  -23.910 1.00 45.04  ? 29   LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 0.486   -5.994  -24.465 1.00 48.92  ? 29   LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? 0.038   -5.847  -25.912 1.00 63.23  ? 29   LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? 0.995   -6.454  -26.896 1.00 70.29  ? 29   LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 0.693   -8.357  -19.428 1.00 29.74  ? 30   PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 1.329   -8.310  -18.113 1.00 23.54  ? 30   PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 1.536   -9.712  -17.557 1.00 25.12  ? 30   PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 2.593   -10.009 -16.989 1.00 21.70  ? 30   PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 0.458   -7.446  -17.168 1.00 25.98  ? 30   PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 0.903   -7.442  -15.739 1.00 20.45  ? 30   PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 2.147   -6.988  -15.393 1.00 19.80  ? 30   PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? 0.030   -7.866  -14.721 1.00 22.67  ? 30   PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 2.554   -7.003  -14.081 1.00 21.46  ? 30   PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 0.422   -7.850  -13.410 1.00 19.94  ? 30   PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 1.669   -7.414  -13.074 1.00 20.15  ? 30   PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 0.530   -10.586 -17.702 1.00 24.47  ? 31   VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 0.670   -11.984 -17.277 1.00 20.60  ? 31   VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 1.745   -12.686 -18.098 1.00 22.60  ? 31   VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 2.684   -13.283 -17.550 1.00 23.80  ? 31   VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? -0.677  -12.735 -17.390 1.00 24.36  ? 31   VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? -0.492  -14.247 -17.149 1.00 22.19  ? 31   VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? -1.688  -12.204 -16.411 1.00 19.80  ? 31   VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 1.631   -12.623 -19.429 1.00 26.71  ? 32   GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 2.511   -13.448 -20.265 1.00 30.98  ? 32   GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 3.958   -12.982 -20.188 1.00 25.88  ? 32   GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 4.881   -13.808 -20.166 1.00 29.61  ? 32   GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 2.012   -13.467 -21.709 1.00 31.61  ? 32   GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 1.184   -14.714 -21.991 1.00 38.02  ? 32   GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 0.800   -14.890 -23.454 1.00 42.45  ? 32   GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 0.660   -13.874 -24.172 1.00 35.11  ? 32   GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 0.618   -16.059 -23.867 1.00 42.60  ? 32   GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 4.180   -11.666 -20.129 1.00 25.35  ? 33   GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 5.535   -11.161 -20.033 1.00 21.54  ? 33   GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 6.219   -11.542 -18.737 1.00 23.51  ? 33   GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 7.416   -11.838 -18.712 1.00 21.96  ? 33   GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 5.481   -11.519 -17.627 1.00 22.54  ? 34   ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 6.100   -11.970 -16.392 1.00 19.61  ? 34   ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 6.162   -13.486 -16.300 1.00 23.16  ? 34   ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 7.034   -14.009 -15.610 1.00 24.76  ? 34   ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 5.361   -11.381 -15.191 1.00 23.93  ? 34   ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 5.718   -9.957  -14.987 1.00 24.53  ? 34   ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 6.847   -9.652  -14.596 1.00 28.82  ? 34   ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 4.797   -9.055  -15.315 1.00 26.70  ? 34   ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 5.274   -14.218 -16.984 1.00 21.08  ? 35   ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 5.457   -15.665 -17.033 1.00 21.95  ? 35   ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 6.742   -16.007 -17.781 1.00 23.71  ? 35   ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 7.481   -16.910 -17.369 1.00 25.82  ? 35   ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 4.257   -16.351 -17.689 1.00 20.49  ? 35   ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 7.040   -15.259 -18.857 1.00 24.44  ? 36   GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 8.282   -15.466 -19.604 1.00 23.73  ? 36   GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 9.487   -15.238 -18.711 1.00 29.39  ? 36   GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 10.452  -16.010 -18.737 1.00 25.19  ? 36   GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 8.329   -14.534 -20.822 1.00 29.10  ? 36   GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 7.216   -14.783 -21.843 1.00 32.34  ? 36   GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 7.159   -13.741 -22.954 1.00 47.43  ? 36   GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 8.108   -12.974 -23.163 1.00 43.74  ? 36   GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 6.037   -13.715 -23.679 1.00 45.95  ? 36   GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 9.419   -14.206 -17.873 1.00 28.20  ? 37   LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 10.529  -13.831 -17.007 1.00 21.61  ? 37   LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 10.688  -14.782 -15.828 1.00 26.61  ? 37   LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 11.798  -15.247 -15.544 1.00 23.89  ? 37   LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 10.301  -12.404 -16.498 1.00 23.18  ? 37   LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 11.198  -12.020 -15.323 1.00 26.90  ? 37   LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 12.565  -11.664 -15.861 1.00 31.16  ? 37   LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 10.583  -10.856 -14.541 1.00 33.55  ? 37   LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 9.587   -15.047 -15.098 1.00 25.37  ? 38   CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 9.663   -15.817 -13.870 1.00 26.47  ? 38   CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 9.640   -17.319 -14.109 1.00 21.06  ? 38   CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 10.052  -18.066 -13.223 1.00 24.15  ? 38   CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 8.512   -15.427 -12.923 1.00 24.49  ? 38   CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 8.518   -13.643 -12.544 1.00 25.96  ? 38   CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 9.172   -17.769 -15.269 0.51 23.02  ? 39   GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 9.157   -17.764 -15.264 0.49 23.02  ? 39   GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 9.144   -19.189 -15.631 0.51 25.43  ? 39   GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 9.130   -19.176 -15.650 0.49 25.43  ? 39   GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 8.342   -20.050 -14.651 0.51 24.70  ? 39   GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 8.340   -20.049 -14.666 0.49 24.70  ? 39   GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 8.862   -21.059 -14.159 0.51 24.50  ? 39   GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 8.867   -21.060 -14.185 0.49 24.51  ? 39   GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 10.572  -19.739 -15.742 0.51 26.80  ? 39   GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 10.563  -19.706 -15.795 0.49 26.81  ? 39   GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 11.266  -19.362 -17.043 0.51 30.01  ? 39   GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 11.456  -18.839 -16.699 0.49 28.76  ? 39   GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 10.641  -20.050 -18.233 0.51 30.39  ? 39   GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 12.888  -19.350 -16.778 0.49 29.43  ? 39   GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 10.013  -19.409 -19.074 0.51 32.90  ? 39   GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 13.123  -20.545 -16.943 0.49 33.05  ? 39   GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 10.801  -21.368 -18.306 0.51 32.01  ? 39   GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 13.848  -18.442 -16.654 0.49 34.04  ? 39   GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 7.085   -19.722 -14.355 1.00 23.87  ? 40   PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 6.279   -20.625 -13.520 1.00 24.04  ? 40   PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 5.975   -21.889 -14.309 1.00 27.04  ? 40   PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 6.020   -21.899 -15.539 1.00 25.11  ? 40   PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 5.002   -19.827 -13.257 1.00 21.19  ? 40   PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 4.859   -19.035 -14.506 1.00 23.20  ? 40   PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 6.270   -18.586 -14.821 1.00 22.01  ? 40   PRO A CD    1 
ATOM   302  N  N     A GLU A 1 41  ? 5.658   -22.965 -13.574 0.61 24.18  ? 41   GLU A N     1 
ATOM   303  N  N     B GLU A 1 41  ? 5.647   -22.956 -13.579 0.39 24.21  ? 41   GLU A N     1 
ATOM   304  C  CA    A GLU A 1 41  ? 5.243   -24.213 -14.209 0.61 24.91  ? 41   GLU A CA    1 
ATOM   305  C  CA    B GLU A 1 41  ? 5.242   -24.189 -14.238 0.39 24.96  ? 41   GLU A CA    1 
ATOM   306  C  C     A GLU A 1 41  ? 3.788   -24.161 -14.659 0.61 27.03  ? 41   GLU A C     1 
ATOM   307  C  C     B GLU A 1 41  ? 3.785   -24.145 -14.676 0.39 27.03  ? 41   GLU A C     1 
ATOM   308  O  O     A GLU A 1 41  ? 3.429   -24.787 -15.661 0.61 29.17  ? 41   GLU A O     1 
ATOM   309  O  O     B GLU A 1 41  ? 3.422   -24.765 -15.680 0.39 29.13  ? 41   GLU A O     1 
ATOM   310  C  CB    A GLU A 1 41  ? 5.465   -25.392 -13.246 0.61 28.05  ? 41   GLU A CB    1 
ATOM   311  C  CB    B GLU A 1 41  ? 5.478   -25.378 -13.307 0.39 28.06  ? 41   GLU A CB    1 
ATOM   312  C  CG    A GLU A 1 41  ? 5.362   -26.795 -13.882 0.61 28.79  ? 41   GLU A CG    1 
ATOM   313  C  CG    B GLU A 1 41  ? 5.302   -26.723 -13.979 0.39 28.82  ? 41   GLU A CG    1 
ATOM   314  C  CD    A GLU A 1 41  ? 6.619   -27.195 -14.646 0.61 31.30  ? 41   GLU A CD    1 
ATOM   315  C  CD    B GLU A 1 41  ? 5.499   -27.860 -13.018 0.39 30.69  ? 41   GLU A CD    1 
ATOM   316  O  OE1   A GLU A 1 41  ? 7.488   -26.323 -14.870 0.61 31.95  ? 41   GLU A OE1   1 
ATOM   317  O  OE1   B GLU A 1 41  ? 5.506   -27.612 -11.795 0.39 28.90  ? 41   GLU A OE1   1 
ATOM   318  O  OE2   A GLU A 1 41  ? 6.746   -28.384 -15.022 0.61 35.62  ? 41   GLU A OE2   1 
ATOM   319  O  OE2   B GLU A 1 41  ? 5.650   -29.007 -13.482 0.39 37.80  ? 41   GLU A OE2   1 
ATOM   320  N  N     . TYR A 1 42  ? 2.946   -23.409 -13.949 1.00 23.19  ? 42   TYR A N     1 
ATOM   321  C  CA    . TYR A 1 42  ? 1.507   -23.371 -14.190 1.00 23.60  ? 42   TYR A CA    1 
ATOM   322  C  C     . TYR A 1 42  ? 1.029   -21.952 -13.965 1.00 25.41  ? 42   TYR A C     1 
ATOM   323  O  O     . TYR A 1 42  ? 1.640   -21.212 -13.191 1.00 20.42  ? 42   TYR A O     1 
ATOM   324  C  CB    . TYR A 1 42  ? 0.716   -24.271 -13.220 1.00 24.83  ? 42   TYR A CB    1 
ATOM   325  C  CG    . TYR A 1 42  ? 1.095   -25.720 -13.225 1.00 29.51  ? 42   TYR A CG    1 
ATOM   326  C  CD1   . TYR A 1 42  ? 0.899   -26.497 -14.358 1.00 32.02  ? 42   TYR A CD1   1 
ATOM   327  C  CD2   . TYR A 1 42  ? 1.619   -26.317 -12.096 1.00 30.44  ? 42   TYR A CD2   1 
ATOM   328  C  CE1   . TYR A 1 42  ? 1.228   -27.827 -14.365 1.00 39.95  ? 42   TYR A CE1   1 
ATOM   329  C  CE2   . TYR A 1 42  ? 1.952   -27.661 -12.095 1.00 34.03  ? 42   TYR A CE2   1 
ATOM   330  C  CZ    . TYR A 1 42  ? 1.734   -28.402 -13.217 1.00 33.32  ? 42   TYR A CZ    1 
ATOM   331  O  OH    . TYR A 1 42  ? 2.072   -29.722 -13.241 1.00 44.35  ? 42   TYR A OH    1 
ATOM   332  N  N     . ILE A 1 43  ? -0.060  -21.584 -14.650 1.00 24.97  ? 43   ILE A N     1 
ATOM   333  C  CA    . ILE A 1 43  ? -0.726  -20.292 -14.482 1.00 21.70  ? 43   ILE A CA    1 
ATOM   334  C  C     . ILE A 1 43  ? -2.169  -20.556 -14.069 1.00 23.11  ? 43   ILE A C     1 
ATOM   335  O  O     . ILE A 1 43  ? -2.899  -21.285 -14.754 1.00 22.09  ? 43   ILE A O     1 
ATOM   336  C  CB    . ILE A 1 43  ? -0.676  -19.438 -15.757 1.00 21.79  ? 43   ILE A CB    1 
ATOM   337  C  CG1   . ILE A 1 43  ? 0.765   -19.173 -16.163 1.00 22.31  ? 43   ILE A CG1   1 
ATOM   338  C  CG2   . ILE A 1 43  ? -1.434  -18.105 -15.552 1.00 21.11  ? 43   ILE A CG2   1 
ATOM   339  C  CD1   . ILE A 1 43  ? 0.913   -18.376 -17.451 1.00 28.36  ? 43   ILE A CD1   1 
ATOM   340  N  N     . HIS A 1 44  ? -2.592  -19.944 -12.971 1.00 20.99  ? 44   HIS A N     1 
ATOM   341  C  CA    . HIS A 1 44  ? -3.942  -20.123 -12.453 1.00 20.84  ? 44   HIS A CA    1 
ATOM   342  C  C     . HIS A 1 44  ? -4.563  -18.730 -12.409 1.00 23.00  ? 44   HIS A C     1 
ATOM   343  O  O     . HIS A 1 44  ? -4.091  -17.866 -11.678 1.00 17.97  ? 44   HIS A O     1 
ATOM   344  C  CB    . HIS A 1 44  ? -3.881  -20.811 -11.084 1.00 20.68  ? 44   HIS A CB    1 
ATOM   345  C  CG    . HIS A 1 44  ? -5.195  -20.922 -10.358 1.00 21.92  ? 44   HIS A CG    1 
ATOM   346  N  ND1   . HIS A 1 44  ? -5.673  -22.123 -9.880  1.00 26.49  ? 44   HIS A ND1   1 
ATOM   347  C  CD2   . HIS A 1 44  ? -6.082  -19.980 -9.951  1.00 19.91  ? 44   HIS A CD2   1 
ATOM   348  C  CE1   . HIS A 1 44  ? -6.822  -21.928 -9.260  1.00 27.97  ? 44   HIS A CE1   1 
ATOM   349  N  NE2   . HIS A 1 44  ? -7.090  -20.634 -9.281  1.00 23.39  ? 44   HIS A NE2   1 
ATOM   350  N  N     . ILE A 1 45  ? -5.580  -18.502 -13.228 1.00 19.22  ? 45   ILE A N     1 
ATOM   351  C  CA    . ILE A 1 45  ? -6.259  -17.220 -13.264 1.00 20.09  ? 45   ILE A CA    1 
ATOM   352  C  C     . ILE A 1 45  ? -7.414  -17.325 -12.282 1.00 23.29  ? 45   ILE A C     1 
ATOM   353  O  O     . ILE A 1 45  ? -8.351  -18.104 -12.497 1.00 23.08  ? 45   ILE A O     1 
ATOM   354  C  CB    . ILE A 1 45  ? -6.746  -16.871 -14.669 1.00 23.35  ? 45   ILE A CB    1 
ATOM   355  C  CG1   . ILE A 1 45  ? -5.545  -16.758 -15.627 1.00 25.72  ? 45   ILE A CG1   1 
ATOM   356  C  CG2   . ILE A 1 45  ? -7.561  -15.567 -14.613 1.00 20.99  ? 45   ILE A CG2   1 
ATOM   357  C  CD1   . ILE A 1 45  ? -5.911  -16.642 -17.101 1.00 26.71  ? 45   ILE A CD1   1 
ATOM   358  N  N     . CYS A 1 46  ? -7.334  -16.566 -11.195 1.00 20.16  ? 46   CYS A N     1 
ATOM   359  C  CA    . CYS A 1 46  ? -8.298  -16.726 -10.101 1.00 20.06  ? 46   CYS A CA    1 
ATOM   360  C  C     . CYS A 1 46  ? -9.685  -16.271 -10.517 1.00 21.72  ? 46   CYS A C     1 
ATOM   361  O  O     . CYS A 1 46  ? -9.839  -15.280 -11.225 1.00 22.69  ? 46   CYS A O     1 
ATOM   362  C  CB    . CYS A 1 46  ? -7.846  -15.931 -8.883  1.00 21.50  ? 46   CYS A CB    1 
ATOM   363  S  SG    . CYS A 1 46  ? -6.335  -16.578 -8.146  1.00 21.94  ? 46   CYS A SG    1 
ATOM   364  N  N     . ASP A 1 47  ? -10.711 -17.001 -10.080 1.00 25.08  ? 47   ASP A N     1 
ATOM   365  C  CA    . ASP A 1 47  ? -12.070 -16.558 -10.346 1.00 24.65  ? 47   ASP A CA    1 
ATOM   366  C  C     . ASP A 1 47  ? -12.800 -16.046 -9.111  1.00 25.01  ? 47   ASP A C     1 
ATOM   367  O  O     . ASP A 1 47  ? -13.881 -15.481 -9.261  1.00 24.36  ? 47   ASP A O     1 
ATOM   368  C  CB    . ASP A 1 47  ? -12.900 -17.675 -11.006 1.00 25.67  ? 47   ASP A CB    1 
ATOM   369  C  CG    . ASP A 1 47  ? -13.090 -18.917 -10.125 1.00 28.02  ? 47   ASP A CG    1 
ATOM   370  O  OD1   . ASP A 1 47  ? -12.783 -18.961 -8.911  1.00 25.09  ? 47   ASP A OD1   1 
ATOM   371  O  OD2   . ASP A 1 47  ? -13.546 -19.919 -10.696 1.00 34.85  ? 47   ASP A OD2   1 
ATOM   372  N  N     . GLY A 1 48  ? -12.231 -16.206 -7.916  1.00 21.89  ? 48   GLY A N     1 
ATOM   373  C  CA    . GLY A 1 48  ? -12.818 -15.687 -6.700  1.00 23.60  ? 48   GLY A CA    1 
ATOM   374  C  C     . GLY A 1 48  ? -13.843 -16.601 -6.079  1.00 26.47  ? 48   GLY A C     1 
ATOM   375  O  O     . GLY A 1 48  ? -14.400 -16.255 -5.033  1.00 26.98  ? 48   GLY A O     1 
ATOM   376  N  N     . SER A 1 49  ? -14.097 -17.765 -6.682  1.00 25.51  ? 49   SER A N     1 
ATOM   377  C  CA    . SER A 1 49  ? -15.242 -18.597 -6.311  1.00 24.89  ? 49   SER A CA    1 
ATOM   378  C  C     . SER A 1 49  ? -15.002 -19.328 -4.993  1.00 25.54  ? 49   SER A C     1 
ATOM   379  O  O     . SER A 1 49  ? -13.865 -19.587 -4.585  1.00 24.87  ? 49   SER A O     1 
ATOM   380  C  CB    . SER A 1 49  ? -15.538 -19.608 -7.420  1.00 28.96  ? 49   SER A CB    1 
ATOM   381  O  OG    . SER A 1 49  ? -14.508 -20.587 -7.529  1.00 26.20  ? 49   SER A OG    1 
ATOM   382  N  N     . GLU A 1 50  ? -16.106 -19.688 -4.328  1.00 29.38  ? 50   GLU A N     1 
ATOM   383  C  CA    . GLU A 1 50  ? -15.999 -20.543 -3.149  1.00 26.11  ? 50   GLU A CA    1 
ATOM   384  C  C     . GLU A 1 50  ? -15.295 -21.854 -3.473  1.00 29.06  ? 50   GLU A C     1 
ATOM   385  O  O     . GLU A 1 50  ? -14.503 -22.364 -2.664  1.00 28.65  ? 50   GLU A O     1 
ATOM   386  C  CB    . GLU A 1 50  ? -17.389 -20.836 -2.576  1.00 34.00  ? 50   GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 50  ? -18.109 -19.625 -2.038  1.00 35.34  ? 50   GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 50  ? -17.393 -18.996 -0.845  1.00 52.42  ? 50   GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 50  ? -16.560 -19.684 -0.207  1.00 52.68  ? 50   GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 50  ? -17.660 -17.804 -0.554  1.00 60.03  ? 50   GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 51  ? -15.583 -22.432 -4.646  1.00 29.28  ? 51   GLU A N     1 
ATOM   392  C  CA    . GLU A 1 51  ? -14.974 -23.718 -5.006  1.00 29.76  ? 51   GLU A CA    1 
ATOM   393  C  C     . GLU A 1 51  ? -13.461 -23.597 -5.087  1.00 31.94  ? 51   GLU A C     1 
ATOM   394  O  O     . GLU A 1 51  ? -12.726 -24.415 -4.520  1.00 27.70  ? 51   GLU A O     1 
ATOM   395  C  CB    . GLU A 1 51  ? -15.523 -24.221 -6.343  1.00 34.35  ? 51   GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 51  ? -16.960 -24.714 -6.304  1.00 44.98  ? 51   GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 51  ? -17.991 -23.583 -6.222  1.00 52.87  ? 51   GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 51  ? -17.610 -22.379 -6.283  1.00 40.68  ? 51   GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 51  ? -19.194 -23.915 -6.099  1.00 60.44  ? 51   GLU A OE2   1 
ATOM   400  N  N     . GLU A 1 52  ? -12.984 -22.566 -5.798  1.00 28.44  ? 52   GLU A N     1 
ATOM   401  C  CA    . GLU A 1 52  ? -11.556 -22.292 -5.882  1.00 27.14  ? 52   GLU A CA    1 
ATOM   402  C  C     . GLU A 1 52  ? -10.937 -22.121 -4.504  1.00 23.94  ? 52   GLU A C     1 
ATOM   403  O  O     . GLU A 1 52  ? -9.864  -22.668 -4.213  1.00 24.39  ? 52   GLU A O     1 
ATOM   404  C  CB    . GLU A 1 52  ? -11.358 -21.033 -6.722  1.00 24.23  ? 52   GLU A CB    1 
ATOM   405  C  CG    . GLU A 1 52  ? -9.969  -20.465 -6.694  1.00 26.48  ? 52   GLU A CG    1 
ATOM   406  C  CD    . GLU A 1 52  ? -9.893  -19.185 -7.488  1.00 28.02  ? 52   GLU A CD    1 
ATOM   407  O  OE1   . GLU A 1 52  ? -10.260 -18.111 -6.952  1.00 23.95  ? 52   GLU A OE1   1 
ATOM   408  O  OE2   . GLU A 1 52  ? -9.504  -19.275 -8.671  1.00 25.03  ? 52   GLU A OE2   1 
ATOM   409  N  N     . TYR A 1 53  ? -11.602 -21.353 -3.641  1.00 23.67  ? 53   TYR A N     1 
ATOM   410  C  CA    . TYR A 1 53  ? -11.058 -21.083 -2.318  1.00 26.10  ? 53   TYR A CA    1 
ATOM   411  C  C     . TYR A 1 53  ? -10.935 -22.361 -1.511  1.00 25.07  ? 53   TYR A C     1 
ATOM   412  O  O     . TYR A 1 53  ? -9.920  -22.581 -0.845  1.00 23.90  ? 53   TYR A O     1 
ATOM   413  C  CB    . TYR A 1 53  ? -11.954 -20.060 -1.596  1.00 26.38  ? 53   TYR A CB    1 
ATOM   414  C  CG    . TYR A 1 53  ? -11.473 -19.589 -0.238  1.00 27.02  ? 53   TYR A CG    1 
ATOM   415  C  CD1   . TYR A 1 53  ? -10.237 -18.968 -0.089  1.00 31.60  ? 53   TYR A CD1   1 
ATOM   416  C  CD2   . TYR A 1 53  ? -12.284 -19.705 0.885   1.00 31.42  ? 53   TYR A CD2   1 
ATOM   417  C  CE1   . TYR A 1 53  ? -9.806  -18.513 1.151   1.00 29.80  ? 53   TYR A CE1   1 
ATOM   418  C  CE2   . TYR A 1 53  ? -11.862 -19.255 2.125   1.00 32.55  ? 53   TYR A CE2   1 
ATOM   419  C  CZ    . TYR A 1 53  ? -10.624 -18.656 2.255   1.00 35.94  ? 53   TYR A CZ    1 
ATOM   420  O  OH    . TYR A 1 53  ? -10.205 -18.199 3.492   1.00 35.86  ? 53   TYR A OH    1 
ATOM   421  N  N     . GLY A 1 54  ? -11.962 -23.216 -1.557  1.00 27.25  ? 54   GLY A N     1 
ATOM   422  C  CA    . GLY A 1 54  ? -11.892 -24.476 -0.827  1.00 30.67  ? 54   GLY A CA    1 
ATOM   423  C  C     . GLY A 1 54  ? -10.796 -25.377 -1.364  1.00 30.51  ? 54   GLY A C     1 
ATOM   424  O  O     . GLY A 1 54  ? -10.077 -26.026 -0.599  1.00 29.96  ? 54   GLY A O     1 
ATOM   425  N  N     . ARG A 1 55  ? -10.625 -25.394 -2.691  1.00 31.25  ? 55   ARG A N     1 
ATOM   426  C  CA    . ARG A 1 55  ? -9.575  -26.212 -3.283  1.00 31.31  ? 55   ARG A CA    1 
ATOM   427  C  C     . ARG A 1 55  ? -8.201  -25.714 -2.854  1.00 30.98  ? 55   ARG A C     1 
ATOM   428  O  O     . ARG A 1 55  ? -7.312  -26.511 -2.526  1.00 32.98  ? 55   ARG A O     1 
ATOM   429  C  CB    . ARG A 1 55  ? -9.718  -26.207 -4.806  1.00 36.36  ? 55   ARG A CB    1 
ATOM   430  C  CG    . ARG A 1 55  ? -9.143  -27.412 -5.518  1.00 46.55  ? 55   ARG A CG    1 
ATOM   431  C  CD    . ARG A 1 55  ? -10.177 -28.552 -5.671  1.00 60.84  ? 55   ARG A CD    1 
ATOM   432  N  NE    . ARG A 1 55  ? -10.880 -28.854 -4.425  1.00 62.81  ? 55   ARG A NE    1 
ATOM   433  C  CZ    . ARG A 1 55  ? -10.486 -29.751 -3.526  1.00 62.86  ? 55   ARG A CZ    1 
ATOM   434  N  NH1   . ARG A 1 55  ? -9.408  -30.506 -3.725  1.00 52.77  ? 55   ARG A NH1   1 
ATOM   435  N  NH2   . ARG A 1 55  ? -11.186 -29.885 -2.396  1.00 52.45  ? 55   ARG A NH2   1 
ATOM   436  N  N     . LEU A 1 56  ? -8.026  -24.388 -2.829  1.00 28.77  ? 56   LEU A N     1 
ATOM   437  C  CA    . LEU A 1 56  ? -6.761  -23.777 -2.437  1.00 25.30  ? 56   LEU A CA    1 
ATOM   438  C  C     . LEU A 1 56  ? -6.409  -24.097 -0.985  1.00 26.64  ? 56   LEU A C     1 
ATOM   439  O  O     . LEU A 1 56  ? -5.270  -24.460 -0.673  1.00 26.75  ? 56   LEU A O     1 
ATOM   440  C  CB    . LEU A 1 56  ? -6.882  -22.270 -2.661  1.00 29.78  ? 56   LEU A CB    1 
ATOM   441  C  CG    . LEU A 1 56  ? -5.724  -21.307 -2.609  1.00 34.98  ? 56   LEU A CG    1 
ATOM   442  C  CD1   . LEU A 1 56  ? -5.004  -21.344 -3.943  1.00 33.85  ? 56   LEU A CD1   1 
ATOM   443  C  CD2   . LEU A 1 56  ? -6.268  -19.896 -2.313  1.00 33.81  ? 56   LEU A CD2   1 
ATOM   444  N  N     . LEU A 1 57  ? -7.376  -23.926 -0.074  1.00 24.12  ? 57   LEU A N     1 
ATOM   445  C  CA    . LEU A 1 57  ? -7.177  -24.309 1.323   1.00 30.36  ? 57   LEU A CA    1 
ATOM   446  C  C     . LEU A 1 57  ? -6.838  -25.787 1.456   1.00 28.74  ? 57   LEU A C     1 
ATOM   447  O  O     . LEU A 1 57  ? -5.976  -26.159 2.259   1.00 30.19  ? 57   LEU A O     1 
ATOM   448  C  CB    . LEU A 1 57  ? -8.432  -24.000 2.140   1.00 25.48  ? 57   LEU A CB    1 
ATOM   449  C  CG    . LEU A 1 57  ? -8.770  -22.522 2.309   1.00 28.74  ? 57   LEU A CG    1 
ATOM   450  C  CD1   . LEU A 1 57  ? -10.193 -22.347 2.835   1.00 31.47  ? 57   LEU A CD1   1 
ATOM   451  C  CD2   . LEU A 1 57  ? -7.782  -21.885 3.270   1.00 27.85  ? 57   LEU A CD2   1 
ATOM   452  N  N     . ALA A 1 58  ? -7.523  -26.647 0.700   1.00 26.33  ? 58   ALA A N     1 
ATOM   453  C  CA    . ALA A 1 58  ? -7.175  -28.071 0.733   1.00 34.69  ? 58   ALA A CA    1 
ATOM   454  C  C     . ALA A 1 58  ? -5.752  -28.294 0.250   1.00 30.25  ? 58   ALA A C     1 
ATOM   455  O  O     . ALA A 1 58  ? -5.006  -29.082 0.841   1.00 33.27  ? 58   ALA A O     1 
ATOM   456  C  CB    . ALA A 1 58  ? -8.151  -28.894 -0.112  1.00 32.78  ? 58   ALA A CB    1 
ATOM   457  N  N     . HIS A 1 59  ? -5.347  -27.597 -0.818  1.00 25.94  ? 59   HIS A N     1 
ATOM   458  C  CA    . HIS A 1 59  ? -3.986  -27.759 -1.329  1.00 28.40  ? 59   HIS A CA    1 
ATOM   459  C  C     . HIS A 1 59  ? -2.952  -27.344 -0.288  1.00 31.95  ? 59   HIS A C     1 
ATOM   460  O  O     . HIS A 1 59  ? -1.927  -28.008 -0.114  1.00 31.08  ? 59   HIS A O     1 
ATOM   461  C  CB    . HIS A 1 59  ? -3.820  -26.948 -2.612  1.00 31.80  ? 59   HIS A CB    1 
ATOM   462  C  CG    . HIS A 1 59  ? -2.405  -26.811 -3.088  1.00 40.43  ? 59   HIS A CG    1 
ATOM   463  N  ND1   . HIS A 1 59  ? -1.599  -27.895 -3.382  1.00 40.30  ? 59   HIS A ND1   1 
ATOM   464  C  CD2   . HIS A 1 59  ? -1.665  -25.707 -3.365  1.00 42.16  ? 59   HIS A CD2   1 
ATOM   465  C  CE1   . HIS A 1 59  ? -0.421  -27.463 -3.803  1.00 37.98  ? 59   HIS A CE1   1 
ATOM   466  N  NE2   . HIS A 1 59  ? -0.436  -26.140 -3.804  1.00 46.48  ? 59   HIS A NE2   1 
ATOM   467  N  N     . MET A 1 60  ? -3.196  -26.245 0.420   1.00 30.11  ? 60   MET A N     1 
ATOM   468  C  CA    . MET A 1 60  ? -2.204  -25.796 1.392   1.00 28.16  ? 60   MET A CA    1 
ATOM   469  C  C     . MET A 1 60  ? -2.170  -26.725 2.585   1.00 24.25  ? 60   MET A C     1 
ATOM   470  O  O     . MET A 1 60  ? -1.121  -26.900 3.211   1.00 27.99  ? 60   MET A O     1 
ATOM   471  C  CB    . MET A 1 60  ? -2.504  -24.348 1.835   1.00 24.76  ? 60   MET A CB    1 
ATOM   472  C  CG    . MET A 1 60  ? -1.980  -23.277 0.861   1.00 24.64  ? 60   MET A CG    1 
ATOM   473  S  SD    . MET A 1 60  ? -2.399  -21.668 1.507   1.00 28.10  ? 60   MET A SD    1 
ATOM   474  C  CE    . MET A 1 60  ? -4.117  -21.542 1.047   1.00 19.88  ? 60   MET A CE    1 
ATOM   475  N  N     . GLN A 1 61  ? -3.309  -27.317 2.920   1.00 24.20  ? 61   GLN A N     1 
ATOM   476  C  CA    . GLN A 1 61  ? -3.359  -28.240 4.043   1.00 31.82  ? 61   GLN A CA    1 
ATOM   477  C  C     . GLN A 1 61  ? -2.564  -29.504 3.725   1.00 36.00  ? 61   GLN A C     1 
ATOM   478  O  O     . GLN A 1 61  ? -1.847  -30.032 4.587   1.00 31.39  ? 61   GLN A O     1 
ATOM   479  C  CB    . GLN A 1 61  ? -4.817  -28.566 4.368   1.00 26.44  ? 61   GLN A CB    1 
ATOM   480  C  CG    . GLN A 1 61  ? -5.038  -29.203 5.718   1.00 29.27  ? 61   GLN A CG    1 
ATOM   481  C  CD    . GLN A 1 61  ? -6.459  -29.727 5.870   1.00 33.22  ? 61   GLN A CD    1 
ATOM   482  O  OE1   . GLN A 1 61  ? -7.191  -29.861 4.882   1.00 40.90  ? 61   GLN A OE1   1 
ATOM   483  N  NE2   . GLN A 1 61  ? -6.854  -30.022 7.100   1.00 33.17  ? 61   GLN A NE2   1 
ATOM   484  N  N     . GLU A 1 62  ? -2.656  -29.966 2.469   1.00 33.79  ? 62   GLU A N     1 
ATOM   485  C  CA    . GLU A 1 62  ? -1.903  -31.128 1.995   1.00 32.74  ? 62   GLU A CA    1 
ATOM   486  C  C     . GLU A 1 62  ? -0.399  -30.858 1.964   1.00 36.30  ? 62   GLU A C     1 
ATOM   487  O  O     . GLU A 1 62  ? 0.403   -31.754 2.254   1.00 47.07  ? 62   GLU A O     1 
ATOM   488  C  CB    . GLU A 1 62  ? -2.409  -31.526 0.603   1.00 29.27  ? 62   GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 62  ? -3.838  -32.091 0.591   1.00 34.39  ? 62   GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 62  ? -4.442  -32.257 -0.818  1.00 35.37  ? 62   GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 62  ? -3.728  -32.085 -1.817  1.00 38.55  ? 62   GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 62  ? -5.653  -32.538 -0.912  1.00 39.03  ? 62   GLU A OE2   1 
ATOM   493  N  N     . GLU A 1 63  ? 0.013   -29.642 1.602   1.00 37.89  ? 63   GLU A N     1 
ATOM   494  C  CA    . GLU A 1 63  ? 1.441   -29.334 1.571   1.00 35.41  ? 63   GLU A CA    1 
ATOM   495  C  C     . GLU A 1 63  ? 2.002   -28.971 2.937   1.00 42.15  ? 63   GLU A C     1 
ATOM   496  O  O     . GLU A 1 63  ? 3.207   -28.744 3.048   1.00 45.17  ? 63   GLU A O     1 
ATOM   497  C  CB    . GLU A 1 63  ? 1.716   -28.185 0.612   1.00 43.43  ? 63   GLU A CB    1 
ATOM   498  C  CG    . GLU A 1 63  ? 1.179   -28.400 -0.782  1.00 46.39  ? 63   GLU A CG    1 
ATOM   499  C  CD    . GLU A 1 63  ? 2.153   -29.128 -1.671  1.00 50.30  ? 63   GLU A CD    1 
ATOM   500  O  OE1   . GLU A 1 63  ? 2.621   -30.219 -1.280  1.00 54.86  ? 63   GLU A OE1   1 
ATOM   501  O  OE2   . GLU A 1 63  ? 2.445   -28.603 -2.765  1.00 58.24  ? 63   GLU A OE2   1 
ATOM   502  N  N     . GLY A 1 64  ? 1.161   -28.891 3.965   1.00 36.89  ? 64   GLY A N     1 
ATOM   503  C  CA    . GLY A 1 64  ? 1.601   -28.462 5.275   1.00 40.33  ? 64   GLY A CA    1 
ATOM   504  C  C     . GLY A 1 64  ? 1.786   -26.970 5.441   1.00 33.99  ? 64   GLY A C     1 
ATOM   505  O  O     . GLY A 1 64  ? 2.432   -26.553 6.405   1.00 35.68  ? 64   GLY A O     1 
ATOM   506  N  N     . VAL A 1 65  ? 1.249   -26.151 4.533   1.00 28.36  ? 65   VAL A N     1 
ATOM   507  C  CA    . VAL A 1 65  ? 1.403   -24.697 4.642   1.00 28.90  ? 65   VAL A CA    1 
ATOM   508  C  C     . VAL A 1 65  ? 0.482   -24.122 5.720   1.00 29.97  ? 65   VAL A C     1 
ATOM   509  O  O     . VAL A 1 65  ? 0.867   -23.212 6.458   1.00 30.21  ? 65   VAL A O     1 
ATOM   510  C  CB    . VAL A 1 65  ? 1.161   -24.039 3.270   1.00 31.12  ? 65   VAL A CB    1 
ATOM   511  C  CG1   . VAL A 1 65  ? 1.470   -22.553 3.320   1.00 31.92  ? 65   VAL A CG1   1 
ATOM   512  C  CG2   . VAL A 1 65  ? 1.990   -24.729 2.209   1.00 35.96  ? 65   VAL A CG2   1 
ATOM   513  N  N     . ILE A 1 66  ? -0.737  -24.651 5.853   1.00 26.38  ? 66   ILE A N     1 
ATOM   514  C  CA    . ILE A 1 66  ? -1.679  -24.218 6.884   1.00 20.14  ? 66   ILE A CA    1 
ATOM   515  C  C     . ILE A 1 66  ? -2.216  -25.458 7.585   1.00 31.29  ? 66   ILE A C     1 
ATOM   516  O  O     . ILE A 1 66  ? -2.131  -26.575 7.069   1.00 23.96  ? 66   ILE A O     1 
ATOM   517  C  CB    . ILE A 1 66  ? -2.855  -23.399 6.327   1.00 26.01  ? 66   ILE A CB    1 
ATOM   518  C  CG1   . ILE A 1 66  ? -3.596  -24.213 5.277   1.00 23.62  ? 66   ILE A CG1   1 
ATOM   519  C  CG2   . ILE A 1 66  ? -2.376  -22.045 5.748   1.00 30.70  ? 66   ILE A CG2   1 
ATOM   520  C  CD1   . ILE A 1 66  ? -4.752  -23.477 4.656   1.00 28.97  ? 66   ILE A CD1   1 
ATOM   521  N  N     . ARG A 1 67  ? -2.772  -25.235 8.773   1.00 24.99  ? 67   ARG A N     1 
ATOM   522  C  CA    . ARG A 1 67  ? -3.451  -26.241 9.575   1.00 28.07  ? 67   ARG A CA    1 
ATOM   523  C  C     . ARG A 1 67  ? -4.890  -25.810 9.804   1.00 28.97  ? 67   ARG A C     1 
ATOM   524  O  O     . ARG A 1 67  ? -5.166  -24.616 9.974   1.00 25.99  ? 67   ARG A O     1 
ATOM   525  C  CB    . ARG A 1 67  ? -2.766  -26.431 10.937  1.00 30.83  ? 67   ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 67  ? -1.527  -27.274 10.904  1.00 37.94  ? 67   ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 67  ? -0.944  -27.432 12.301  1.00 42.28  ? 67   ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 67  ? -1.952  -27.787 13.298  1.00 42.50  ? 67   ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 67  ? -2.324  -29.027 13.599  1.00 44.96  ? 67   ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 67  ? -1.823  -30.078 12.967  1.00 49.78  ? 67   ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 67  ? -3.220  -29.218 14.557  1.00 47.00  ? 67   ARG A NH2   1 
ATOM   532  N  N     . LYS A 1 68  ? -5.814  -26.775 9.820   1.00 26.59  ? 68   LYS A N     1 
ATOM   533  C  CA    . LYS A 1 68  ? -7.203  -26.453 10.115  1.00 28.36  ? 68   LYS A CA    1 
ATOM   534  C  C     . LYS A 1 68  ? -7.383  -26.332 11.619  1.00 28.30  ? 68   LYS A C     1 
ATOM   535  O  O     . LYS A 1 68  ? -6.866  -27.156 12.376  1.00 30.10  ? 68   LYS A O     1 
ATOM   536  C  CB    . LYS A 1 68  ? -8.145  -27.515 9.555   1.00 33.56  ? 68   LYS A CB    1 
ATOM   537  C  CG    . LYS A 1 68  ? -9.632  -27.119 9.531   1.00 32.50  ? 68   LYS A CG    1 
ATOM   538  C  CD    . LYS A 1 68  ? -10.428 -28.130 8.694   1.00 39.09  ? 68   LYS A CD    1 
ATOM   539  C  CE    . LYS A 1 68  ? -11.774 -27.579 8.221   1.00 43.11  ? 68   LYS A CE    1 
ATOM   540  N  NZ    . LYS A 1 68  ? -12.657 -27.139 9.333   1.00 45.68  ? 68   LYS A NZ    1 
ATOM   541  N  N     . LEU A 1 69  ? -8.107  -25.295 12.047  1.00 25.58  ? 69   LEU A N     1 
ATOM   542  C  CA    . LEU A 1 69  ? -8.419  -25.061 13.459  1.00 33.37  ? 69   LEU A CA    1 
ATOM   543  C  C     . LEU A 1 69  ? -9.770  -25.707 13.727  1.00 30.21  ? 69   LEU A C     1 
ATOM   544  O  O     . LEU A 1 69  ? -10.818 -25.095 13.538  1.00 29.91  ? 69   LEU A O     1 
ATOM   545  C  CB    . LEU A 1 69  ? -8.441  -23.566 13.780  1.00 23.66  ? 69   LEU A CB    1 
ATOM   546  C  CG    . LEU A 1 69  ? -7.075  -22.881 13.695  1.00 25.21  ? 69   LEU A CG    1 
ATOM   547  C  CD1   . LEU A 1 69  ? -7.218  -21.366 13.723  1.00 24.54  ? 69   LEU A CD1   1 
ATOM   548  C  CD2   . LEU A 1 69  ? -6.195  -23.381 14.844  1.00 30.72  ? 69   LEU A CD2   1 
ATOM   549  N  N     . LYS A 1 70  ? -9.747  -26.956 14.191  1.00 32.45  ? 70   LYS A N     1 
ATOM   550  C  CA    . LYS A 1 70  ? -10.983 -27.743 14.224  1.00 30.19  ? 70   LYS A CA    1 
ATOM   551  C  C     . LYS A 1 70  ? -12.019 -27.215 15.216  1.00 38.28  ? 70   LYS A C     1 
ATOM   552  O  O     . LYS A 1 70  ? -13.193 -27.594 15.115  1.00 32.65  ? 70   LYS A O     1 
ATOM   553  C  CB    . LYS A 1 70  ? -10.659 -29.206 14.515  1.00 37.89  ? 70   LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 70  ? -9.831  -29.444 15.767  1.00 45.32  ? 70   LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 70  ? -9.947  -30.908 16.243  1.00 52.04  ? 70   LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 70  ? -9.825  -31.017 17.771  1.00 55.36  ? 70   LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 70  ? -10.334 -32.312 18.331  1.00 65.94  ? 70   LYS A NZ    1 
ATOM   558  N  N     . LYS A 1 71  ? -11.642 -26.318 16.130  1.00 26.03  ? 71   LYS A N     1 
ATOM   559  C  CA    . LYS A 1 71  ? -12.609 -25.845 17.117  1.00 24.67  ? 71   LYS A CA    1 
ATOM   560  C  C     . LYS A 1 71  ? -13.584 -24.844 16.530  1.00 34.07  ? 71   LYS A C     1 
ATOM   561  O  O     . LYS A 1 71  ? -14.659 -24.638 17.100  1.00 32.48  ? 71   LYS A O     1 
ATOM   562  C  CB    . LYS A 1 71  ? -11.873 -25.239 18.313  1.00 31.41  ? 71   LYS A CB    1 
ATOM   563  C  CG    . LYS A 1 71  ? -12.757 -24.761 19.454  1.00 31.88  ? 71   LYS A CG    1 
ATOM   564  C  CD    . LYS A 1 71  ? -11.895 -24.308 20.611  1.00 30.76  ? 71   LYS A CD    1 
ATOM   565  C  CE    . LYS A 1 71  ? -12.752 -23.794 21.758  1.00 43.66  ? 71   LYS A CE    1 
ATOM   566  N  NZ    . LYS A 1 71  ? -12.119 -24.127 23.064  1.00 45.19  ? 71   LYS A NZ    1 
ATOM   567  N  N     . TYR A 1 72  ? -13.233 -24.210 15.410  1.00 31.61  ? 72   TYR A N     1 
ATOM   568  C  CA    . TYR A 1 72  ? -14.033 -23.153 14.819  1.00 27.54  ? 72   TYR A CA    1 
ATOM   569  C  C     . TYR A 1 72  ? -14.518 -23.587 13.440  1.00 28.72  ? 72   TYR A C     1 
ATOM   570  O  O     . TYR A 1 72  ? -14.247 -24.696 12.962  1.00 36.71  ? 72   TYR A O     1 
ATOM   571  C  CB    . TYR A 1 72  ? -13.226 -21.844 14.754  1.00 26.87  ? 72   TYR A CB    1 
ATOM   572  C  CG    . TYR A 1 72  ? -12.514 -21.513 16.053  1.00 24.86  ? 72   TYR A CG    1 
ATOM   573  C  CD1   . TYR A 1 72  ? -13.228 -21.284 17.222  1.00 29.74  ? 72   TYR A CD1   1 
ATOM   574  C  CD2   . TYR A 1 72  ? -11.127 -21.432 16.111  1.00 27.68  ? 72   TYR A CD2   1 
ATOM   575  C  CE1   . TYR A 1 72  ? -12.586 -20.999 18.415  1.00 30.68  ? 72   TYR A CE1   1 
ATOM   576  C  CE2   . TYR A 1 72  ? -10.479 -21.143 17.304  1.00 28.40  ? 72   TYR A CE2   1 
ATOM   577  C  CZ    . TYR A 1 72  ? -11.215 -20.922 18.452  1.00 29.67  ? 72   TYR A CZ    1 
ATOM   578  O  OH    . TYR A 1 72  ? -10.576 -20.627 19.645  1.00 30.61  ? 72   TYR A OH    1 
ATOM   579  N  N     . ASP A 1 73  ? -15.247 -22.693 12.807  1.00 29.81  ? 73   ASP A N     1 
ATOM   580  C  CA    . ASP A 1 73  ? -15.923 -22.940 11.539  1.00 29.67  ? 73   ASP A CA    1 
ATOM   581  C  C     . ASP A 1 73  ? -15.056 -22.367 10.411  1.00 29.61  ? 73   ASP A C     1 
ATOM   582  O  O     . ASP A 1 73  ? -14.992 -21.148 10.225  1.00 27.32  ? 73   ASP A O     1 
ATOM   583  C  CB    . ASP A 1 73  ? -17.301 -22.294 11.609  1.00 33.00  ? 73   ASP A CB    1 
ATOM   584  C  CG    . ASP A 1 73  ? -18.026 -22.284 10.293  1.00 39.42  ? 73   ASP A CG    1 
ATOM   585  O  OD1   . ASP A 1 73  ? -17.598 -22.999 9.360   1.00 41.83  ? 73   ASP A OD1   1 
ATOM   586  O  OD2   . ASP A 1 73  ? -19.039 -21.549 10.202  1.00 42.75  ? 73   ASP A OD2   1 
ATOM   587  N  N     . ASN A 1 74  ? -14.381 -23.244 9.663   1.00 26.38  ? 74   ASN A N     1 
ATOM   588  C  CA    . ASN A 1 74  ? -13.572 -22.824 8.507   1.00 24.16  ? 74   ASN A CA    1 
ATOM   589  C  C     . ASN A 1 74  ? -12.490 -21.799 8.882   1.00 23.15  ? 74   ASN A C     1 
ATOM   590  O  O     . ASN A 1 74  ? -12.304 -20.777 8.220   1.00 27.74  ? 74   ASN A O     1 
ATOM   591  C  CB    . ASN A 1 74  ? -14.473 -22.281 7.390   1.00 20.81  ? 74   ASN A CB    1 
ATOM   592  C  CG    . ASN A 1 74  ? -13.720 -22.077 6.059   1.00 31.91  ? 74   ASN A CG    1 
ATOM   593  O  OD1   . ASN A 1 74  ? -12.825 -22.862 5.708   1.00 32.43  ? 74   ASN A OD1   1 
ATOM   594  N  ND2   . ASN A 1 74  ? -14.068 -21.008 5.334   1.00 37.14  ? 74   ASN A ND2   1 
ATOM   595  N  N     . CYS A 1 75  ? -11.728 -22.088 9.924   1.00 26.69  ? 75   CYS A N     1 
ATOM   596  C  CA    . CYS A 1 75  ? -10.624 -21.220 10.314  1.00 23.41  ? 75   CYS A CA    1 
ATOM   597  C  C     . CYS A 1 75  ? -9.322  -21.989 10.175  1.00 30.24  ? 75   CYS A C     1 
ATOM   598  O  O     . CYS A 1 75  ? -9.299  -23.218 10.295  1.00 26.01  ? 75   CYS A O     1 
ATOM   599  C  CB    . CYS A 1 75  ? -10.767 -20.720 11.755  1.00 20.99  ? 75   CYS A CB    1 
ATOM   600  S  SG    . CYS A 1 75  ? -12.105 -19.605 12.058  1.00 23.40  ? 75   CYS A SG    1 
ATOM   601  N  N     . TRP A 1 76  ? -8.238  -21.262 9.894   1.00 20.54  ? 76   TRP A N     1 
ATOM   602  C  CA    . TRP A 1 76  ? -6.978  -21.891 9.550   1.00 20.68  ? 76   TRP A CA    1 
ATOM   603  C  C     . TRP A 1 76  ? -5.826  -21.139 10.187  1.00 24.41  ? 76   TRP A C     1 
ATOM   604  O  O     . TRP A 1 76  ? -5.915  -19.936 10.459  1.00 23.02  ? 76   TRP A O     1 
ATOM   605  C  CB    . TRP A 1 76  ? -6.779  -21.926 8.038   1.00 20.56  ? 76   TRP A CB    1 
ATOM   606  C  CG    . TRP A 1 76  ? -7.917  -22.528 7.344   1.00 21.32  ? 76   TRP A CG    1 
ATOM   607  C  CD1   . TRP A 1 76  ? -9.077  -21.916 6.988   1.00 23.99  ? 76   TRP A CD1   1 
ATOM   608  C  CD2   . TRP A 1 76  ? -8.018  -23.886 6.896   1.00 22.32  ? 76   TRP A CD2   1 
ATOM   609  N  NE1   . TRP A 1 76  ? -9.909  -22.820 6.352   1.00 25.74  ? 76   TRP A NE1   1 
ATOM   610  C  CE2   . TRP A 1 76  ? -9.275  -24.031 6.281   1.00 23.27  ? 76   TRP A CE2   1 
ATOM   611  C  CE3   . TRP A 1 76  ? -7.164  -24.988 6.956   1.00 28.14  ? 76   TRP A CE3   1 
ATOM   612  C  CZ2   . TRP A 1 76  ? -9.702  -25.235 5.731   1.00 29.62  ? 76   TRP A CZ2   1 
ATOM   613  C  CZ3   . TRP A 1 76  ? -7.590  -26.197 6.400   1.00 31.88  ? 76   TRP A CZ3   1 
ATOM   614  C  CH2   . TRP A 1 76  ? -8.844  -26.305 5.798   1.00 27.16  ? 76   TRP A CH2   1 
ATOM   615  N  N     . LEU A 1 77  ? -4.736  -21.857 10.399  1.00 21.33  ? 77   LEU A N     1 
ATOM   616  C  CA    . LEU A 1 77  ? -3.527  -21.325 11.014  1.00 24.14  ? 77   LEU A CA    1 
ATOM   617  C  C     . LEU A 1 77  ? -2.340  -21.510 10.077  1.00 25.41  ? 77   LEU A C     1 
ATOM   618  O  O     . LEU A 1 77  ? -2.132  -22.608 9.550   1.00 24.28  ? 77   LEU A O     1 
ATOM   619  C  CB    . LEU A 1 77  ? -3.247  -22.037 12.334  1.00 23.56  ? 77   LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 77  ? -1.997  -21.596 13.076  1.00 26.47  ? 77   LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 77  ? -2.204  -20.146 13.479  1.00 24.98  ? 77   LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 77  ? -1.830  -22.469 14.310  1.00 33.02  ? 77   LEU A CD2   1 
ATOM   623  N  N     . ALA A 1 78  ? -1.556  -20.443 9.877   1.00 23.05  ? 78   ALA A N     1 
ATOM   624  C  CA    . ALA A 1 78  ? -0.258  -20.520 9.213   1.00 25.05  ? 78   ALA A CA    1 
ATOM   625  C  C     . ALA A 1 78  ? 0.832   -20.122 10.211  1.00 27.28  ? 78   ALA A C     1 
ATOM   626  O  O     . ALA A 1 78  ? 0.619   -19.248 11.052  1.00 27.17  ? 78   ALA A O     1 
ATOM   627  C  CB    . ALA A 1 78  ? -0.209  -19.599 7.966   1.00 20.97  ? 78   ALA A CB    1 
ATOM   628  N  N     . LEU A 1 79  ? 1.980   -20.784 10.151  1.00 21.79  ? 79   LEU A N     1 
ATOM   629  C  CA    . LEU A 1 79  ? 3.143   -20.421 10.954  1.00 23.22  ? 79   LEU A CA    1 
ATOM   630  C  C     . LEU A 1 79  ? 4.281   -20.095 9.998   1.00 28.02  ? 79   LEU A C     1 
ATOM   631  O  O     . LEU A 1 79  ? 4.548   -20.863 9.071   1.00 28.13  ? 79   LEU A O     1 
ATOM   632  C  CB    . LEU A 1 79  ? 3.559   -21.548 11.905  1.00 27.14  ? 79   LEU A CB    1 
ATOM   633  C  CG    . LEU A 1 79  ? 2.499   -22.072 12.886  1.00 31.31  ? 79   LEU A CG    1 
ATOM   634  C  CD1   . LEU A 1 79  ? 3.105   -23.152 13.792  1.00 32.48  ? 79   LEU A CD1   1 
ATOM   635  C  CD2   . LEU A 1 79  ? 1.890   -20.936 13.731  1.00 22.40  ? 79   LEU A CD2   1 
ATOM   636  N  N     . THR A 1 80  ? 4.956   -18.973 10.222  1.00 27.40  ? 80   THR A N     1 
ATOM   637  C  CA    . THR A 1 80  ? 5.960   -18.510 9.276   1.00 22.64  ? 80   THR A CA    1 
ATOM   638  C  C     . THR A 1 80  ? 7.378   -18.834 9.751   1.00 29.71  ? 80   THR A C     1 
ATOM   639  O  O     . THR A 1 80  ? 7.620   -19.163 10.918  1.00 25.07  ? 80   THR A O     1 
ATOM   640  C  CB    . THR A 1 80  ? 5.823   -16.990 9.037   1.00 25.26  ? 80   THR A CB    1 
ATOM   641  O  OG1   . THR A 1 80  ? 6.296   -16.250 10.173  1.00 26.32  ? 80   THR A OG1   1 
ATOM   642  C  CG2   . THR A 1 80  ? 4.360   -16.608 8.776   1.00 22.46  ? 80   THR A CG2   1 
ATOM   643  N  N     . ASP A 1 81  ? 8.310   -18.761 8.805   1.00 30.10  ? 81   ASP A N     1 
ATOM   644  C  CA    . ASP A 1 81  ? 9.728   -18.607 9.123   1.00 31.31  ? 81   ASP A CA    1 
ATOM   645  C  C     . ASP A 1 81  ? 9.888   -17.424 10.071  1.00 30.35  ? 81   ASP A C     1 
ATOM   646  O  O     . ASP A 1 81  ? 9.388   -16.334 9.774   1.00 27.96  ? 81   ASP A O     1 
ATOM   647  C  CB    . ASP A 1 81  ? 10.520  -18.359 7.837   1.00 30.68  ? 81   ASP A CB    1 
ATOM   648  C  CG    . ASP A 1 81  ? 12.033  -18.455 8.021   1.00 32.70  ? 81   ASP A CG    1 
ATOM   649  O  OD1   . ASP A 1 81  ? 12.592  -17.837 8.943   1.00 29.98  ? 81   ASP A OD1   1 
ATOM   650  O  OD2   . ASP A 1 81  ? 12.668  -19.133 7.193   1.00 30.74  ? 81   ASP A OD2   1 
ATOM   651  N  N     . PRO A 1 82  ? 10.570  -17.587 11.205  1.00 28.58  ? 82   PRO A N     1 
ATOM   652  C  CA    . PRO A 1 82  ? 10.704  -16.467 12.147  1.00 29.93  ? 82   PRO A CA    1 
ATOM   653  C  C     . PRO A 1 82  ? 11.517  -15.290 11.600  1.00 29.90  ? 82   PRO A C     1 
ATOM   654  O  O     . PRO A 1 82  ? 11.542  -14.244 12.250  1.00 28.84  ? 82   PRO A O     1 
ATOM   655  C  CB    . PRO A 1 82  ? 11.389  -17.105 13.369  1.00 32.12  ? 82   PRO A CB    1 
ATOM   656  C  CG    . PRO A 1 82  ? 12.078  -18.341 12.812  1.00 42.67  ? 82   PRO A CG    1 
ATOM   657  C  CD    . PRO A 1 82  ? 11.185  -18.832 11.706  1.00 37.25  ? 82   PRO A CD    1 
ATOM   658  N  N     . ARG A 1 83  ? 12.169  -15.420 10.441  1.00 29.02  ? 83   ARG A N     1 
ATOM   659  C  CA    . ARG A 1 83  ? 12.785  -14.265 9.794   1.00 29.44  ? 83   ARG A CA    1 
ATOM   660  C  C     . ARG A 1 83  ? 11.799  -13.461 8.959   1.00 28.45  ? 83   ARG A C     1 
ATOM   661  O  O     . ARG A 1 83  ? 12.172  -12.412 8.424   1.00 30.71  ? 83   ARG A O     1 
ATOM   662  C  CB    . ARG A 1 83  ? 13.941  -14.703 8.892   1.00 30.86  ? 83   ARG A CB    1 
ATOM   663  C  CG    . ARG A 1 83  ? 15.070  -15.402 9.617   1.00 31.75  ? 83   ARG A CG    1 
ATOM   664  C  CD    . ARG A 1 83  ? 16.019  -16.092 8.656   1.00 27.88  ? 83   ARG A CD    1 
ATOM   665  N  NE    . ARG A 1 83  ? 15.367  -17.134 7.869   1.00 35.66  ? 83   ARG A NE    1 
ATOM   666  C  CZ    . ARG A 1 83  ? 15.876  -17.677 6.769   1.00 38.52  ? 83   ARG A CZ    1 
ATOM   667  N  NH1   . ARG A 1 83  ? 17.052  -17.303 6.292   1.00 43.90  ? 83   ARG A NH1   1 
ATOM   668  N  NH2   . ARG A 1 83  ? 15.193  -18.627 6.136   1.00 36.17  ? 83   ARG A NH2   1 
ATOM   669  N  N     . ASP A 1 84  ? 10.557  -13.916 8.830   1.00 31.22  ? 84   ASP A N     1 
ATOM   670  C  CA    . ASP A 1 84  ? 9.555   -13.283 7.958   1.00 30.08  ? 84   ASP A CA    1 
ATOM   671  C  C     . ASP A 1 84  ? 8.272   -13.113 8.772   1.00 26.50  ? 84   ASP A C     1 
ATOM   672  O  O     . ASP A 1 84  ? 7.311   -13.882 8.640   1.00 29.48  ? 84   ASP A O     1 
ATOM   673  C  CB    . ASP A 1 84  ? 9.342   -14.142 6.706   1.00 27.90  ? 84   ASP A CB    1 
ATOM   674  C  CG    . ASP A 1 84  ? 8.549   -13.434 5.629   1.00 28.44  ? 84   ASP A CG    1 
ATOM   675  O  OD1   . ASP A 1 84  ? 8.465   -12.187 5.676   1.00 29.29  ? 84   ASP A OD1   1 
ATOM   676  O  OD2   . ASP A 1 84  ? 7.985   -14.130 4.748   1.00 27.30  ? 84   ASP A OD2   1 
ATOM   677  N  N     . VAL A 1 85  ? 8.244   -12.100 9.635   1.00 24.59  ? 85   VAL A N     1 
ATOM   678  C  CA    . VAL A 1 85  ? 7.167   -11.969 10.606  1.00 24.93  ? 85   VAL A CA    1 
ATOM   679  C  C     . VAL A 1 85  ? 6.510   -10.601 10.585  1.00 31.03  ? 85   VAL A C     1 
ATOM   680  O  O     . VAL A 1 85  ? 5.555   -10.386 11.320  1.00 27.40  ? 85   VAL A O     1 
ATOM   681  C  CB    . VAL A 1 85  ? 7.657   -12.290 12.029  1.00 26.07  ? 85   VAL A CB    1 
ATOM   682  C  CG1   . VAL A 1 85  ? 8.051   -13.760 12.133  1.00 28.47  ? 85   VAL A CG1   1 
ATOM   683  C  CG2   . VAL A 1 85  ? 8.827   -11.382 12.395  1.00 30.22  ? 85   VAL A CG2   1 
ATOM   684  N  N     . ALA A 1 86  ? 6.987   -9.662  9.764   1.00 24.36  ? 86   ALA A N     1 
ATOM   685  C  CA    . ALA A 1 86  ? 6.405   -8.330  9.747   1.00 23.60  ? 86   ALA A CA    1 
ATOM   686  C  C     . ALA A 1 86  ? 6.783   -7.633  8.448   1.00 27.03  ? 86   ALA A C     1 
ATOM   687  O  O     . ALA A 1 86  ? 7.740   -8.013  7.767   1.00 25.53  ? 86   ALA A O     1 
ATOM   688  C  CB    . ALA A 1 86  ? 6.875   -7.500  10.941  1.00 32.67  ? 86   ALA A CB    1 
ATOM   689  N  N     . ARG A 1 87  ? 5.975   -6.634  8.102   1.00 30.84  ? 87   ARG A N     1 
ATOM   690  C  CA    . ARG A 1 87  ? 6.388   -5.592  7.172   1.00 28.56  ? 87   ARG A CA    1 
ATOM   691  C  C     . ARG A 1 87  ? 7.783   -5.100  7.558   1.00 32.02  ? 87   ARG A C     1 
ATOM   692  O  O     . ARG A 1 87  ? 8.099   -4.995  8.745   1.00 32.74  ? 87   ARG A O     1 
ATOM   693  C  CB    . ARG A 1 87  ? 5.348   -4.462  7.254   1.00 28.46  ? 87   ARG A CB    1 
ATOM   694  C  CG    . ARG A 1 87  ? 5.429   -3.352  6.243   1.00 24.02  ? 87   ARG A CG    1 
ATOM   695  C  CD    . ARG A 1 87  ? 4.224   -2.408  6.289   1.00 19.14  ? 87   ARG A CD    1 
ATOM   696  N  NE    . ARG A 1 87  ? 3.858   -1.985  7.633   1.00 20.93  ? 87   ARG A NE    1 
ATOM   697  C  CZ    . ARG A 1 87  ? 4.534   -1.108  8.371   1.00 31.24  ? 87   ARG A CZ    1 
ATOM   698  N  NH1   . ARG A 1 87  ? 5.664   -0.566  7.943   1.00 24.75  ? 87   ARG A NH1   1 
ATOM   699  N  NH2   . ARG A 1 87  ? 4.056   -0.758  9.569   1.00 26.19  ? 87   ARG A NH2   1 
ATOM   700  N  N     . ILE A 1 88  ? 8.638   -4.833  6.557   1.00 33.65  ? 88   ILE A N     1 
ATOM   701  C  CA    . ILE A 1 88  ? 10.038  -4.440  6.778   1.00 34.43  ? 88   ILE A CA    1 
ATOM   702  C  C     . ILE A 1 88  ? 10.257  -3.073  6.143   1.00 34.70  ? 88   ILE A C     1 
ATOM   703  O  O     . ILE A 1 88  ? 10.490  -2.975  4.934   1.00 33.90  ? 88   ILE A O     1 
ATOM   704  C  CB    . ILE A 1 88  ? 11.035  -5.441  6.195   1.00 37.26  ? 88   ILE A CB    1 
ATOM   705  C  CG1   . ILE A 1 88  ? 10.480  -6.844  6.208   1.00 42.45  ? 88   ILE A CG1   1 
ATOM   706  C  CG2   . ILE A 1 88  ? 12.390  -5.342  6.913   1.00 42.98  ? 88   ILE A CG2   1 
ATOM   707  C  CD1   . ILE A 1 88  ? 11.400  -7.812  5.562   1.00 43.56  ? 88   ILE A CD1   1 
ATOM   708  N  N     . GLU A 1 89  ? 10.271  -2.027  6.964   1.00 35.63  ? 89   GLU A N     1 
ATOM   709  C  CA    . GLU A 1 89  ? 10.462  -0.672  6.452   1.00 36.16  ? 89   GLU A CA    1 
ATOM   710  C  C     . GLU A 1 89  ? 11.802  -0.522  5.736   1.00 34.25  ? 89   GLU A C     1 
ATOM   711  O  O     . GLU A 1 89  ? 11.884  0.154   4.707   1.00 36.93  ? 89   GLU A O     1 
ATOM   712  C  CB    . GLU A 1 89  ? 10.336  0.325   7.603   1.00 37.74  ? 89   GLU A CB    1 
ATOM   713  C  CG    . GLU A 1 89  ? 10.347  1.806   7.193   1.00 44.42  ? 89   GLU A CG    1 
ATOM   714  C  CD    . GLU A 1 89  ? 9.922   2.753   8.345   1.00 49.01  ? 89   GLU A CD    1 
ATOM   715  O  OE1   . GLU A 1 89  ? 9.587   2.252   9.448   1.00 49.23  ? 89   GLU A OE1   1 
ATOM   716  O  OE2   . GLU A 1 89  ? 9.915   3.998   8.141   1.00 49.60  ? 89   GLU A OE2   1 
ATOM   717  N  N     . SER A 1 90  ? 12.856  -1.171  6.237   1.00 36.73  ? 90   SER A N     1 
ATOM   718  C  CA    . SER A 1 90  ? 14.214  -0.893  5.768   1.00 43.40  ? 90   SER A CA    1 
ATOM   719  C  C     . SER A 1 90  ? 14.490  -1.442  4.373   1.00 43.09  ? 90   SER A C     1 
ATOM   720  O  O     . SER A 1 90  ? 15.457  -1.011  3.734   1.00 43.88  ? 90   SER A O     1 
ATOM   721  C  CB    . SER A 1 90  ? 15.245  -1.456  6.755   1.00 44.81  ? 90   SER A CB    1 
ATOM   722  O  OG    . SER A 1 90  ? 15.043  -2.844  6.973   1.00 48.16  ? 90   SER A OG    1 
ATOM   723  N  N     . LYS A 1 91  ? 13.669  -2.379  3.895   1.00 31.94  ? 91   LYS A N     1 
ATOM   724  C  CA    . LYS A 1 91  ? 13.778  -2.958  2.565   1.00 27.93  ? 91   LYS A CA    1 
ATOM   725  C  C     . LYS A 1 91  ? 12.651  -2.492  1.638   1.00 24.16  ? 91   LYS A C     1 
ATOM   726  O  O     . LYS A 1 91  ? 12.404  -3.103  0.600   1.00 26.24  ? 91   LYS A O     1 
ATOM   727  C  CB    . LYS A 1 91  ? 13.804  -4.487  2.681   1.00 32.37  ? 91   LYS A CB    1 
ATOM   728  C  CG    . LYS A 1 91  ? 15.132  -4.997  3.265   1.00 39.50  ? 91   LYS A CG    1 
ATOM   729  C  CD    . LYS A 1 91  ? 15.061  -6.385  3.842   1.00 44.68  ? 91   LYS A CD    1 
ATOM   730  C  CE    . LYS A 1 91  ? 16.460  -7.025  3.917   1.00 46.76  ? 91   LYS A CE    1 
ATOM   731  N  NZ    . LYS A 1 91  ? 17.487  -6.050  4.397   1.00 62.16  ? 91   LYS A NZ    1 
ATOM   732  N  N     . THR A 1 92  ? 11.959  -1.421  1.990   1.00 26.81  ? 92   THR A N     1 
ATOM   733  C  CA    . THR A 1 92  ? 10.872  -0.897  1.172   1.00 22.36  ? 92   THR A CA    1 
ATOM   734  C  C     . THR A 1 92  ? 11.303  0.416   0.537   1.00 27.58  ? 92   THR A C     1 
ATOM   735  O  O     . THR A 1 92  ? 11.701  1.344   1.253   1.00 28.21  ? 92   THR A O     1 
ATOM   736  C  CB    . THR A 1 92  ? 9.626   -0.699  2.018   1.00 24.00  ? 92   THR A CB    1 
ATOM   737  O  OG1   . THR A 1 92  ? 9.336   -1.946  2.670   1.00 24.09  ? 92   THR A OG1   1 
ATOM   738  C  CG2   . THR A 1 92  ? 8.465   -0.279  1.143   1.00 23.92  ? 92   THR A CG2   1 
ATOM   739  N  N     . VAL A 1 93  ? 11.207  0.494   -0.805  1.00 22.17  ? 93   VAL A N     1 
ATOM   740  C  CA    . VAL A 1 93  ? 11.743  1.620   -1.570  1.00 21.06  ? 93   VAL A CA    1 
ATOM   741  C  C     . VAL A 1 93  ? 10.696  2.127   -2.557  1.00 20.51  ? 93   VAL A C     1 
ATOM   742  O  O     . VAL A 1 93  ? 9.772   1.413   -2.952  1.00 21.22  ? 93   VAL A O     1 
ATOM   743  C  CB    . VAL A 1 93  ? 13.017  1.227   -2.349  1.00 21.90  ? 93   VAL A CB    1 
ATOM   744  C  CG1   . VAL A 1 93  ? 14.125  0.774   -1.405  1.00 22.94  ? 93   VAL A CG1   1 
ATOM   745  C  CG2   . VAL A 1 93  ? 12.690  0.139   -3.350  1.00 19.72  ? 93   VAL A CG2   1 
ATOM   746  N  N     . ILE A 1 94  ? 10.888  3.357   -2.997  1.00 18.98  ? 94   ILE A N     1 
ATOM   747  C  CA    . ILE A 1 94  ? 10.065  3.972   -4.035  1.00 17.09  ? 94   ILE A CA    1 
ATOM   748  C  C     . ILE A 1 94  ? 11.016  4.477   -5.109  1.00 21.45  ? 94   ILE A C     1 
ATOM   749  O  O     . ILE A 1 94  ? 12.067  5.038   -4.785  1.00 22.57  ? 94   ILE A O     1 
ATOM   750  C  CB    . ILE A 1 94  ? 9.206   5.125   -3.474  1.00 19.19  ? 94   ILE A CB    1 
ATOM   751  C  CG1   . ILE A 1 94  ? 8.167   4.567   -2.485  1.00 19.19  ? 94   ILE A CG1   1 
ATOM   752  C  CG2   . ILE A 1 94  ? 8.502   5.905   -4.595  1.00 23.99  ? 94   ILE A CG2   1 
ATOM   753  C  CD1   . ILE A 1 94  ? 7.243   5.607   -1.963  1.00 22.20  ? 94   ILE A CD1   1 
ATOM   754  N  N     . ILE A 1 95  ? 10.654  4.290   -6.376  1.00 22.53  ? 95   ILE A N     1 
ATOM   755  C  CA    . ILE A 1 95  ? 11.548  4.608   -7.494  1.00 19.01  ? 95   ILE A CA    1 
ATOM   756  C  C     . ILE A 1 95  ? 10.943  5.759   -8.271  1.00 23.33  ? 95   ILE A C     1 
ATOM   757  O  O     . ILE A 1 95  ? 9.820   5.657   -8.786  1.00 23.25  ? 95   ILE A O     1 
ATOM   758  C  CB    . ILE A 1 95  ? 11.795  3.381   -8.392  1.00 21.81  ? 95   ILE A CB    1 
ATOM   759  C  CG1   . ILE A 1 95  ? 12.786  2.418   -7.738  1.00 29.99  ? 95   ILE A CG1   1 
ATOM   760  C  CG2   . ILE A 1 95  ? 12.369  3.797   -9.743  1.00 26.32  ? 95   ILE A CG2   1 
ATOM   761  C  CD1   . ILE A 1 95  ? 12.166  1.360   -6.850  1.00 22.47  ? 95   ILE A CD1   1 
ATOM   762  N  N     . THR A 1 96  ? 11.662  6.877   -8.318  1.00 24.41  ? 96   THR A N     1 
ATOM   763  C  CA    . THR A 1 96  ? 11.276  8.017   -9.136  1.00 22.72  ? 96   THR A CA    1 
ATOM   764  C  C     . THR A 1 96  ? 12.539  8.520   -9.827  1.00 24.72  ? 96   THR A C     1 
ATOM   765  O  O     . THR A 1 96  ? 13.667  8.249   -9.388  1.00 25.44  ? 96   THR A O     1 
ATOM   766  C  CB    . THR A 1 96  ? 10.607  9.163   -8.326  1.00 24.03  ? 96   THR A CB    1 
ATOM   767  O  OG1   . THR A 1 96  ? 11.469  9.548   -7.257  1.00 25.73  ? 96   THR A OG1   1 
ATOM   768  C  CG2   . THR A 1 96  ? 9.243   8.715   -7.728  1.00 27.14  ? 96   THR A CG2   1 
ATOM   769  N  N     . GLN A 1 97  ? 12.341  9.239   -10.929 1.00 29.75  ? 97   GLN A N     1 
ATOM   770  C  CA    . GLN A 1 97  ? 13.486  9.808   -11.642 1.00 34.49  ? 97   GLN A CA    1 
ATOM   771  C  C     . GLN A 1 97  ? 14.291  10.730  -10.734 1.00 32.09  ? 97   GLN A C     1 
ATOM   772  O  O     . GLN A 1 97  ? 15.519  10.625  -10.660 1.00 33.63  ? 97   GLN A O     1 
ATOM   773  C  CB    . GLN A 1 97  ? 13.000  10.553  -12.878 1.00 39.69  ? 97   GLN A CB    1 
ATOM   774  C  CG    . GLN A 1 97  ? 14.113  11.204  -13.676 1.00 52.89  ? 97   GLN A CG    1 
ATOM   775  C  CD    . GLN A 1 97  ? 13.557  12.175  -14.685 1.00 62.80  ? 97   GLN A CD    1 
ATOM   776  O  OE1   . GLN A 1 97  ? 12.606  11.847  -15.399 1.00 65.53  ? 97   GLN A OE1   1 
ATOM   777  N  NE2   . GLN A 1 97  ? 14.111  13.395  -14.724 1.00 62.16  ? 97   GLN A NE2   1 
ATOM   778  N  N     . GLU A 1 98  ? 13.602  11.593  -9.986  1.00 30.24  ? 98   GLU A N     1 
ATOM   779  C  CA    . GLU A 1 98  ? 14.205  12.574  -9.089  1.00 28.95  ? 98   GLU A CA    1 
ATOM   780  C  C     . GLU A 1 98  ? 13.889  12.207  -7.642  1.00 28.45  ? 98   GLU A C     1 
ATOM   781  O  O     . GLU A 1 98  ? 12.727  11.975  -7.307  1.00 25.00  ? 98   GLU A O     1 
ATOM   782  C  CB    . GLU A 1 98  ? 13.667  13.967  -9.408  1.00 32.98  ? 98   GLU A CB    1 
ATOM   783  C  CG    . GLU A 1 98  ? 13.845  14.367  -10.860 1.00 44.51  ? 98   GLU A CG    1 
ATOM   784  C  CD    . GLU A 1 98  ? 15.090  15.197  -11.067 1.00 54.30  ? 98   GLU A CD    1 
ATOM   785  O  OE1   . GLU A 1 98  ? 15.289  16.153  -10.281 1.00 57.04  ? 98   GLU A OE1   1 
ATOM   786  O  OE2   . GLU A 1 98  ? 15.869  14.889  -12.003 1.00 63.56  ? 98   GLU A OE2   1 
ATOM   787  N  N     . GLN A 1 99  ? 14.926  12.156  -6.799  1.00 26.09  ? 99   GLN A N     1 
ATOM   788  C  CA    . GLN A 1 99  ? 14.754  11.784  -5.406  1.00 26.36  ? 99   GLN A CA    1 
ATOM   789  C  C     . GLN A 1 99  ? 13.754  12.683  -4.690  1.00 28.95  ? 99   GLN A C     1 
ATOM   790  O  O     . GLN A 1 99  ? 13.010  12.211  -3.824  1.00 23.56  ? 99   GLN A O     1 
ATOM   791  C  CB    . GLN A 1 99  ? 16.102  11.835  -4.682  1.00 28.21  ? 99   GLN A CB    1 
ATOM   792  C  CG    . GLN A 1 99  ? 15.939  11.542  -3.203  1.00 26.70  ? 99   GLN A CG    1 
ATOM   793  C  CD    . GLN A 1 99  ? 17.248  11.319  -2.475  1.00 36.10  ? 99   GLN A CD    1 
ATOM   794  O  OE1   . GLN A 1 99  ? 18.309  11.802  -2.896  1.00 41.58  ? 99   GLN A OE1   1 
ATOM   795  N  NE2   . GLN A 1 99  ? 17.183  10.580  -1.374  1.00 32.62  ? 99   GLN A NE2   1 
ATOM   796  N  N     . ARG A 1 100 ? 13.710  13.963  -5.059  1.00 23.63  ? 100  ARG A N     1 
ATOM   797  C  CA    . ARG A 1 100 ? 12.893  14.971  -4.397  1.00 23.38  ? 100  ARG A CA    1 
ATOM   798  C  C     . ARG A 1 100 ? 11.408  14.745  -4.617  1.00 26.07  ? 100  ARG A C     1 
ATOM   799  O  O     . ARG A 1 100 ? 10.585  15.304  -3.879  1.00 27.45  ? 100  ARG A O     1 
ATOM   800  C  CB    . ARG A 1 100 ? 13.289  16.371  -4.922  1.00 25.81  ? 100  ARG A CB    1 
ATOM   801  C  CG    . ARG A 1 100 ? 12.716  17.546  -4.141  1.00 38.04  ? 100  ARG A CG    1 
ATOM   802  C  CD    . ARG A 1 100 ? 13.007  18.900  -4.811  1.00 42.08  ? 100  ARG A CD    1 
ATOM   803  N  NE    . ARG A 1 100 ? 12.658  20.005  -3.920  1.00 52.18  ? 100  ARG A NE    1 
ATOM   804  C  CZ    . ARG A 1 100 ? 12.784  21.297  -4.211  1.00 51.90  ? 100  ARG A CZ    1 
ATOM   805  N  NH1   . ARG A 1 100 ? 13.246  21.704  -5.384  1.00 53.28  ? 100  ARG A NH1   1 
ATOM   806  N  NH2   . ARG A 1 100 ? 12.434  22.204  -3.300  1.00 49.13  ? 100  ARG A NH2   1 
ATOM   807  N  N     . ASP A 1 101 ? 11.045  13.985  -5.648  1.00 26.12  ? 101  ASP A N     1 
ATOM   808  C  CA    . ASP A 1 101 ? 9.647   13.642  -5.828  1.00 25.86  ? 101  ASP A CA    1 
ATOM   809  C  C     . ASP A 1 101 ? 9.196   12.615  -4.790  1.00 24.86  ? 101  ASP A C     1 
ATOM   810  O  O     . ASP A 1 101 ? 7.997   12.492  -4.531  1.00 28.18  ? 101  ASP A O     1 
ATOM   811  C  CB    . ASP A 1 101 ? 9.433   13.118  -7.246  1.00 26.56  ? 101  ASP A CB    1 
ATOM   812  C  CG    . ASP A 1 101 ? 9.654   14.194  -8.290  1.00 36.49  ? 101  ASP A CG    1 
ATOM   813  O  OD1   . ASP A 1 101 ? 9.342   15.360  -7.994  1.00 41.73  ? 101  ASP A OD1   1 
ATOM   814  O  OD2   . ASP A 1 101 ? 10.159  13.880  -9.378  1.00 45.49  ? 101  ASP A OD2   1 
ATOM   815  N  N     . THR A 1 102 ? 10.136  11.893  -4.188  1.00 23.71  ? 102  THR A N     1 
ATOM   816  C  CA    . THR A 1 102 ? 9.848   10.814  -3.248  1.00 24.68  ? 102  THR A CA    1 
ATOM   817  C  C     . THR A 1 102 ? 9.992   11.253  -1.798  1.00 26.64  ? 102  THR A C     1 
ATOM   818  O  O     . THR A 1 102 ? 9.130   10.939  -0.974  1.00 24.45  ? 102  THR A O     1 
ATOM   819  C  CB    . THR A 1 102 ? 10.753  9.614   -3.536  1.00 25.48  ? 102  THR A CB    1 
ATOM   820  O  OG1   . THR A 1 102 ? 10.302  8.993   -4.740  1.00 27.24  ? 102  THR A OG1   1 
ATOM   821  C  CG2   . THR A 1 102 ? 10.711  8.577   -2.397  1.00 26.08  ? 102  THR A CG2   1 
ATOM   822  N  N     . VAL A 1 103 ? 11.069  11.970  -1.481  1.00 23.58  ? 103  VAL A N     1 
ATOM   823  C  CA    . VAL A 1 103 ? 11.304  12.516  -0.141  1.00 18.68  ? 103  VAL A CA    1 
ATOM   824  C  C     . VAL A 1 103 ? 11.849  13.922  -0.285  1.00 21.66  ? 103  VAL A C     1 
ATOM   825  O  O     . VAL A 1 103 ? 12.559  14.232  -1.248  1.00 26.42  ? 103  VAL A O     1 
ATOM   826  C  CB    . VAL A 1 103 ? 12.319  11.670  0.656   1.00 25.25  ? 103  VAL A CB    1 
ATOM   827  C  CG1   . VAL A 1 103 ? 11.763  10.308  0.993   1.00 23.10  ? 103  VAL A CG1   1 
ATOM   828  C  CG2   . VAL A 1 103 ? 13.620  11.509  -0.146  1.00 23.71  ? 103  VAL A CG2   1 
ATOM   829  N  N     . PRO A 1 104 ? 11.544  14.797  0.676   1.00 21.92  ? 104  PRO A N     1 
ATOM   830  C  CA    . PRO A 1 104 ? 12.225  16.094  0.707   1.00 23.25  ? 104  PRO A CA    1 
ATOM   831  C  C     . PRO A 1 104 ? 13.698  15.869  0.961   1.00 24.35  ? 104  PRO A C     1 
ATOM   832  O  O     . PRO A 1 104 ? 14.086  14.919  1.630   1.00 23.03  ? 104  PRO A O     1 
ATOM   833  C  CB    . PRO A 1 104 ? 11.560  16.838  1.888   1.00 23.20  ? 104  PRO A CB    1 
ATOM   834  C  CG    . PRO A 1 104 ? 10.325  16.039  2.209   1.00 20.68  ? 104  PRO A CG    1 
ATOM   835  C  CD    . PRO A 1 104 ? 10.696  14.605  1.868   1.00 19.91  ? 104  PRO A CD    1 
ATOM   836  N  N     . ILE A 1 105 ? 14.525  16.756  0.418   1.00 23.88  ? 105  ILE A N     1 
ATOM   837  C  CA    . ILE A 1 105 ? 15.969  16.608  0.572   1.00 26.73  ? 105  ILE A CA    1 
ATOM   838  C  C     . ILE A 1 105 ? 16.293  17.152  1.955   1.00 21.42  ? 105  ILE A C     1 
ATOM   839  O  O     . ILE A 1 105 ? 16.062  18.346  2.213   1.00 23.36  ? 105  ILE A O     1 
ATOM   840  C  CB    . ILE A 1 105 ? 16.730  17.340  -0.551  1.00 29.31  ? 105  ILE A CB    1 
ATOM   841  C  CG1   . ILE A 1 105 ? 16.353  16.736  -1.900  1.00 31.65  ? 105  ILE A CG1   1 
ATOM   842  C  CG2   . ILE A 1 105 ? 18.246  17.316  -0.307  1.00 30.05  ? 105  ILE A CG2   1 
ATOM   843  C  CD1   . ILE A 1 105 ? 16.476  15.218  -1.934  1.00 32.07  ? 105  ILE A CD1   1 
ATOM   844  N  N     . PRO A 1 106 ? 16.772  16.329  2.884   1.00 27.08  ? 106  PRO A N     1 
ATOM   845  C  CA    . PRO A 1 106 ? 16.960  16.819  4.253   1.00 25.15  ? 106  PRO A CA    1 
ATOM   846  C  C     . PRO A 1 106 ? 18.078  17.845  4.298   1.00 30.64  ? 106  PRO A C     1 
ATOM   847  O  O     . PRO A 1 106 ? 18.932  17.910  3.413   1.00 28.50  ? 106  PRO A O     1 
ATOM   848  C  CB    . PRO A 1 106 ? 17.323  15.570  5.068   1.00 25.87  ? 106  PRO A CB    1 
ATOM   849  C  CG    . PRO A 1 106 ? 17.118  14.393  4.149   1.00 25.58  ? 106  PRO A CG    1 
ATOM   850  C  CD    . PRO A 1 106 ? 17.181  14.918  2.734   1.00 25.45  ? 106  PRO A CD    1 
ATOM   851  N  N     . LYS A 1 107 ? 18.053  18.649  5.364   1.00 21.79  ? 107  LYS A N     1 
ATOM   852  C  CA    . LYS A 1 107 ? 19.041  19.704  5.534   1.00 30.45  ? 107  LYS A CA    1 
ATOM   853  C  C     . LYS A 1 107 ? 20.391  19.136  5.936   1.00 32.63  ? 107  LYS A C     1 
ATOM   854  O  O     . LYS A 1 107 ? 21.434  19.544  5.400   1.00 32.91  ? 107  LYS A O     1 
ATOM   855  C  CB    . LYS A 1 107 ? 18.570  20.701  6.590   1.00 28.19  ? 107  LYS A CB    1 
ATOM   856  C  CG    . LYS A 1 107 ? 19.481  21.913  6.721   1.00 30.70  ? 107  LYS A CG    1 
ATOM   857  C  CD    . LYS A 1 107 ? 18.828  22.955  7.615   1.00 31.53  ? 107  LYS A CD    1 
ATOM   858  C  CE    . LYS A 1 107 ? 19.512  24.316  7.511   1.00 45.50  ? 107  LYS A CE    1 
ATOM   859  N  NZ    . LYS A 1 107 ? 18.799  25.345  8.334   1.00 52.33  ? 107  LYS A NZ    1 
ATOM   860  N  N     . SER A 1 108 ? 20.397  18.202  6.877   1.00 28.61  ? 108  SER A N     1 
ATOM   861  C  CA    . SER A 1 108 ? 21.667  17.706  7.391   1.00 32.59  ? 108  SER A CA    1 
ATOM   862  C  C     . SER A 1 108 ? 21.723  16.183  7.437   1.00 34.73  ? 108  SER A C     1 
ATOM   863  O  O     . SER A 1 108 ? 22.769  15.589  7.153   1.00 29.73  ? 108  SER A O     1 
ATOM   864  C  CB    . SER A 1 108 ? 21.927  18.299  8.777   1.00 35.64  ? 108  SER A CB    1 
ATOM   865  O  OG    . SER A 1 108 ? 20.939  17.880  9.706   1.00 39.93  ? 108  SER A OG    1 
ATOM   866  N  N     . GLY A 1 109 ? 20.620  15.529  7.799   1.00 28.20  ? 109  GLY A N     1 
ATOM   867  C  CA    . GLY A 1 109 ? 20.631  14.109  8.055   1.00 30.20  ? 109  GLY A CA    1 
ATOM   868  C  C     . GLY A 1 109 ? 20.130  13.271  6.887   1.00 26.07  ? 109  GLY A C     1 
ATOM   869  O  O     . GLY A 1 109 ? 19.922  13.745  5.767   1.00 28.10  ? 109  GLY A O     1 
ATOM   870  N  N     . GLN A 1 110 ? 19.937  11.983  7.178   1.00 23.93  ? 110  GLN A N     1 
ATOM   871  C  CA    . GLN A 1 110 ? 19.327  11.040  6.250   1.00 25.81  ? 110  GLN A CA    1 
ATOM   872  C  C     . GLN A 1 110 ? 17.815  11.124  6.409   1.00 25.54  ? 110  GLN A C     1 
ATOM   873  O  O     . GLN A 1 110 ? 17.315  11.277  7.526   1.00 24.95  ? 110  GLN A O     1 
ATOM   874  C  CB    . GLN A 1 110 ? 19.836  9.633   6.559   1.00 26.98  ? 110  GLN A CB    1 
ATOM   875  C  CG    . GLN A 1 110 ? 19.132  8.462   5.869   1.00 31.00  ? 110  GLN A CG    1 
ATOM   876  C  CD    . GLN A 1 110 ? 19.530  7.142   6.501   1.00 36.35  ? 110  GLN A CD    1 
ATOM   877  O  OE1   . GLN A 1 110 ? 18.988  6.729   7.540   1.00 39.03  ? 110  GLN A OE1   1 
ATOM   878  N  NE2   . GLN A 1 110 ? 20.498  6.474   5.895   1.00 41.14  ? 110  GLN A NE2   1 
ATOM   879  N  N     . SER A 1 111 ? 17.079  11.024  5.302   1.00 23.21  ? 111  SER A N     1 
ATOM   880  C  CA    . SER A 1 111 ? 15.627  11.126  5.407   1.00 21.21  ? 111  SER A CA    1 
ATOM   881  C  C     . SER A 1 111 ? 15.026  9.927   6.152   1.00 23.59  ? 111  SER A C     1 
ATOM   882  O  O     . SER A 1 111 ? 15.383  8.771   5.892   1.00 24.85  ? 111  SER A O     1 
ATOM   883  C  CB    . SER A 1 111 ? 14.996  11.242  4.017   1.00 24.00  ? 111  SER A CB    1 
ATOM   884  O  OG    . SER A 1 111 ? 13.587  11.395  4.152   1.00 22.15  ? 111  SER A OG    1 
ATOM   885  N  N     . GLN A 1 112 ? 14.101  10.212  7.068   1.00 22.48  ? 112  GLN A N     1 
ATOM   886  C  CA    . GLN A 1 112 ? 13.241  9.219   7.703   1.00 23.08  ? 112  GLN A CA    1 
ATOM   887  C  C     . GLN A 1 112 ? 11.884  9.087   7.044   1.00 22.64  ? 112  GLN A C     1 
ATOM   888  O  O     . GLN A 1 112 ? 11.031  8.374   7.585   1.00 29.44  ? 112  GLN A O     1 
ATOM   889  C  CB    . GLN A 1 112 ? 12.956  9.562   9.173   1.00 22.85  ? 112  GLN A CB    1 
ATOM   890  C  CG    . GLN A 1 112 ? 14.102  9.872   10.073  1.00 32.47  ? 112  GLN A CG    1 
ATOM   891  C  CD    . GLN A 1 112 ? 13.616  10.095  11.506  1.00 36.84  ? 112  GLN A CD    1 
ATOM   892  O  OE1   . GLN A 1 112 ? 12.413  9.972   11.798  1.00 29.54  ? 112  GLN A OE1   1 
ATOM   893  N  NE2   . GLN A 1 112 ? 14.547  10.400  12.407  1.00 28.05  ? 112  GLN A NE2   1 
ATOM   894  N  N     . LEU A 1 113 ? 11.636  9.774   5.940   1.00 20.21  ? 113  LEU A N     1 
ATOM   895  C  CA    . LEU A 1 113 ? 10.286  9.933   5.420   1.00 20.17  ? 113  LEU A CA    1 
ATOM   896  C  C     . LEU A 1 113 ? 10.028  9.080   4.207   1.00 20.17  ? 113  LEU A C     1 
ATOM   897  O  O     . LEU A 1 113 ? 9.011   9.262   3.530   1.00 26.90  ? 113  LEU A O     1 
ATOM   898  C  CB    . LEU A 1 113 ? 10.024  11.396  5.089   1.00 24.31  ? 113  LEU A CB    1 
ATOM   899  C  CG    . LEU A 1 113 ? 10.083  12.294  6.316   1.00 27.79  ? 113  LEU A CG    1 
ATOM   900  C  CD1   . LEU A 1 113 ? 10.021  13.759  5.892   1.00 26.95  ? 113  LEU A CD1   1 
ATOM   901  C  CD2   . LEU A 1 113 ? 8.932   11.917  7.204   1.00 26.73  ? 113  LEU A CD2   1 
ATOM   902  N  N     . GLY A 1 114 ? 10.916  8.152   3.929   1.00 24.14  ? 114  GLY A N     1 
ATOM   903  C  CA    . GLY A 1 114 ? 10.848  7.350   2.727   1.00 25.50  ? 114  GLY A CA    1 
ATOM   904  C  C     . GLY A 1 114 ? 12.231  6.848   2.396   1.00 28.63  ? 114  GLY A C     1 
ATOM   905  O  O     . GLY A 1 114 ? 13.220  7.224   3.014   1.00 30.02  ? 114  GLY A O     1 
ATOM   906  N  N     . ARG A 1 115 ? 12.286  5.968   1.410   1.00 24.92  ? 115  ARG A N     1 
ATOM   907  C  CA    . ARG A 1 115 ? 13.543  5.361   0.996   1.00 30.60  ? 115  ARG A CA    1 
ATOM   908  C  C     . ARG A 1 115 ? 13.533  5.357   -0.524  1.00 28.95  ? 115  ARG A C     1 
ATOM   909  O  O     . ARG A 1 115 ? 12.799  4.582   -1.139  1.00 25.17  ? 115  ARG A O     1 
ATOM   910  C  CB    . ARG A 1 115 ? 13.696  3.958   1.584   1.00 30.49  ? 115  ARG A CB    1 
ATOM   911  C  CG    . ARG A 1 115 ? 15.142  3.455   1.629   1.00 45.80  ? 115  ARG A CG    1 
ATOM   912  C  CD    . ARG A 1 115 ? 15.274  2.126   2.387   1.00 50.02  ? 115  ARG A CD    1 
ATOM   913  N  NE    . ARG A 1 115 ? 14.927  2.263   3.799   1.00 46.40  ? 115  ARG A NE    1 
ATOM   914  C  CZ    . ARG A 1 115 ? 15.812  2.402   4.779   1.00 58.06  ? 115  ARG A CZ    1 
ATOM   915  N  NH1   . ARG A 1 115 ? 17.117  2.430   4.535   1.00 58.77  ? 115  ARG A NH1   1 
ATOM   916  N  NH2   . ARG A 1 115 ? 15.379  2.515   6.037   1.00 49.95  ? 115  ARG A NH2   1 
ATOM   917  N  N     . TRP A 1 116 ? 14.305  6.255   -1.123  1.00 26.62  ? 116  TRP A N     1 
ATOM   918  C  CA    . TRP A 1 116 ? 14.354  6.399   -2.571  1.00 25.14  ? 116  TRP A CA    1 
ATOM   919  C  C     . TRP A 1 116 ? 15.386  5.453   -3.176  1.00 30.47  ? 116  TRP A C     1 
ATOM   920  O  O     . TRP A 1 116 ? 16.427  5.180   -2.574  1.00 28.18  ? 116  TRP A O     1 
ATOM   921  C  CB    . TRP A 1 116 ? 14.687  7.845   -2.933  1.00 26.79  ? 116  TRP A CB    1 
ATOM   922  C  CG    . TRP A 1 116 ? 14.844  8.084   -4.375  1.00 28.27  ? 116  TRP A CG    1 
ATOM   923  C  CD1   . TRP A 1 116 ? 13.854  8.211   -5.302  1.00 29.91  ? 116  TRP A CD1   1 
ATOM   924  C  CD2   . TRP A 1 116 ? 16.080  8.250   -5.076  1.00 26.13  ? 116  TRP A CD2   1 
ATOM   925  N  NE1   . TRP A 1 116 ? 14.403  8.435   -6.547  1.00 27.25  ? 116  TRP A NE1   1 
ATOM   926  C  CE2   . TRP A 1 116 ? 15.767  8.466   -6.431  1.00 27.43  ? 116  TRP A CE2   1 
ATOM   927  C  CE3   . TRP A 1 116 ? 17.423  8.232   -4.686  1.00 29.13  ? 116  TRP A CE3   1 
ATOM   928  C  CZ2   . TRP A 1 116 ? 16.751  8.670   -7.405  1.00 27.66  ? 116  TRP A CZ2   1 
ATOM   929  C  CZ3   . TRP A 1 116 ? 18.403  8.427   -5.657  1.00 29.83  ? 116  TRP A CZ3   1 
ATOM   930  C  CH2   . TRP A 1 116 ? 18.057  8.648   -6.994  1.00 30.39  ? 116  TRP A CH2   1 
ATOM   931  N  N     . MET A 1 117 ? 15.092  4.941   -4.367  1.00 25.93  ? 117  MET A N     1 
ATOM   932  C  CA    . MET A 1 117 ? 16.068  4.137   -5.107  1.00 28.13  ? 117  MET A CA    1 
ATOM   933  C  C     . MET A 1 117 ? 16.010  4.567   -6.557  1.00 27.80  ? 117  MET A C     1 
ATOM   934  O  O     . MET A 1 117 ? 14.920  4.737   -7.102  1.00 27.46  ? 117  MET A O     1 
ATOM   935  C  CB    . MET A 1 117 ? 15.786  2.633   -4.989  1.00 23.04  ? 117  MET A CB    1 
ATOM   936  C  CG    . MET A 1 117 ? 16.731  1.709   -5.755  1.00 26.96  ? 117  MET A CG    1 
ATOM   937  S  SD    . MET A 1 117 ? 16.249  -0.037  -5.586  1.00 36.05  ? 117  MET A SD    1 
ATOM   938  C  CE    . MET A 1 117 ? 17.213  -0.547  -4.169  1.00 34.15  ? 117  MET A CE    1 
ATOM   939  N  N     . SER A 1 118 ? 17.170  4.768   -7.183  1.00 30.74  ? 118  SER A N     1 
ATOM   940  C  CA    . SER A 1 118 ? 17.156  5.175   -8.583  1.00 34.40  ? 118  SER A CA    1 
ATOM   941  C  C     . SER A 1 118 ? 16.639  4.038   -9.463  1.00 29.14  ? 118  SER A C     1 
ATOM   942  O  O     . SER A 1 118 ? 16.707  2.864   -9.107  1.00 28.87  ? 118  SER A O     1 
ATOM   943  C  CB    . SER A 1 118 ? 18.563  5.563   -9.065  1.00 31.96  ? 118  SER A CB    1 
ATOM   944  O  OG    . SER A 1 118 ? 19.379  4.396   -9.082  1.00 29.74  ? 118  SER A OG    1 
ATOM   945  N  N     . GLU A 1 119 ? 16.118  4.414   -10.633 1.00 32.90  ? 119  GLU A N     1 
ATOM   946  C  CA    . GLU A 1 119 ? 15.691  3.420   -11.615 1.00 35.13  ? 119  GLU A CA    1 
ATOM   947  C  C     . GLU A 1 119 ? 16.836  2.481   -11.991 1.00 36.87  ? 119  GLU A C     1 
ATOM   948  O  O     . GLU A 1 119 ? 16.641  1.264   -12.110 1.00 31.21  ? 119  GLU A O     1 
ATOM   949  C  CB    . GLU A 1 119 ? 15.155  4.121   -12.868 1.00 43.73  ? 119  GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 119 ? 13.833  4.849   -12.676 1.00 49.54  ? 119  GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 119 ? 13.789  6.224   -13.337 1.00 57.59  ? 119  GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 119 ? 14.800  6.663   -13.946 1.00 61.54  ? 119  GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 119 ? 12.722  6.867   -13.240 1.00 59.49  ? 119  GLU A OE2   1 
ATOM   954  N  N     . GLU A 1 120 ? 18.039  3.035   -12.186 1.00 39.90  ? 120  GLU A N     1 
ATOM   955  C  CA    . GLU A 1 120 ? 19.190  2.225   -12.580 1.00 40.11  ? 120  GLU A CA    1 
ATOM   956  C  C     . GLU A 1 120 ? 19.542  1.206   -11.504 1.00 35.45  ? 120  GLU A C     1 
ATOM   957  O  O     . GLU A 1 120 ? 19.839  0.046   -11.809 1.00 32.29  ? 120  GLU A O     1 
ATOM   958  C  CB    . GLU A 1 120 ? 20.396  3.129   -12.879 1.00 40.20  ? 120  GLU A CB    1 
ATOM   959  C  CG    . GLU A 1 120 ? 20.187  4.138   -14.018 1.00 51.50  ? 120  GLU A CG    1 
ATOM   960  C  CD    . GLU A 1 120 ? 19.387  5.381   -13.604 1.00 56.82  ? 120  GLU A CD    1 
ATOM   961  O  OE1   . GLU A 1 120 ? 19.289  5.667   -12.393 1.00 50.69  ? 120  GLU A OE1   1 
ATOM   962  O  OE2   . GLU A 1 120 ? 18.849  6.072   -14.497 1.00 66.39  ? 120  GLU A OE2   1 
ATOM   963  N  N     . ASP A 1 121 ? 19.525  1.619   -10.237 1.00 34.17  ? 121  ASP A N     1 
ATOM   964  C  CA    . ASP A 1 121 ? 19.797  0.657   -9.176  1.00 32.45  ? 121  ASP A CA    1 
ATOM   965  C  C     . ASP A 1 121 ? 18.687  -0.379  -9.085  1.00 31.14  ? 121  ASP A C     1 
ATOM   966  O  O     . ASP A 1 121 ? 18.957  -1.562  -8.865  1.00 31.12  ? 121  ASP A O     1 
ATOM   967  C  CB    . ASP A 1 121 ? 19.974  1.370   -7.841  1.00 33.94  ? 121  ASP A CB    1 
ATOM   968  C  CG    . ASP A 1 121 ? 21.194  2.269   -7.832  1.00 44.18  ? 121  ASP A CG    1 
ATOM   969  O  OD1   . ASP A 1 121 ? 22.252  1.806   -8.311  1.00 48.86  ? 121  ASP A OD1   1 
ATOM   970  O  OD2   . ASP A 1 121 ? 21.086  3.431   -7.371  1.00 38.17  ? 121  ASP A OD2   1 
ATOM   971  N  N     . PHE A 1 122 ? 17.433  0.039   -9.261  1.00 29.56  ? 122  PHE A N     1 
ATOM   972  C  CA    . PHE A 1 122 ? 16.372  -0.948  -9.160  1.00 29.19  ? 122  PHE A CA    1 
ATOM   973  C  C     . PHE A 1 122 ? 16.449  -1.964  -10.290 1.00 27.93  ? 122  PHE A C     1 
ATOM   974  O  O     . PHE A 1 122 ? 16.146  -3.141  -10.079 1.00 29.47  ? 122  PHE A O     1 
ATOM   975  C  CB    . PHE A 1 122 ? 14.994  -0.294  -9.141  1.00 32.81  ? 122  PHE A CB    1 
ATOM   976  C  CG    . PHE A 1 122 ? 13.880  -1.303  -9.115  1.00 28.13  ? 122  PHE A CG    1 
ATOM   977  C  CD1   . PHE A 1 122 ? 13.709  -2.132  -8.012  1.00 24.74  ? 122  PHE A CD1   1 
ATOM   978  C  CD2   . PHE A 1 122 ? 13.057  -1.471  -10.212 1.00 26.93  ? 122  PHE A CD2   1 
ATOM   979  C  CE1   . PHE A 1 122 ? 12.711  -3.079  -7.990  1.00 28.03  ? 122  PHE A CE1   1 
ATOM   980  C  CE2   . PHE A 1 122 ? 12.064  -2.438  -10.203 1.00 22.44  ? 122  PHE A CE2   1 
ATOM   981  C  CZ    . PHE A 1 122 ? 11.883  -3.230  -9.099  1.00 23.11  ? 122  PHE A CZ    1 
ATOM   982  N  N     . GLU A 1 123 ? 16.839  -1.533  -11.492 1.00 25.28  ? 123  GLU A N     1 
ATOM   983  C  CA    . GLU A 1 123 ? 17.005  -2.479  -12.598 1.00 29.93  ? 123  GLU A CA    1 
ATOM   984  C  C     . GLU A 1 123 ? 18.009  -3.571  -12.237 1.00 27.78  ? 123  GLU A C     1 
ATOM   985  O  O     . GLU A 1 123 ? 17.785  -4.761  -12.495 1.00 29.47  ? 123  GLU A O     1 
ATOM   986  C  CB    . GLU A 1 123 ? 17.437  -1.702  -13.843 1.00 42.97  ? 123  GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 123 ? 17.581  -2.493  -15.130 1.00 50.24  ? 123  GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 123 ? 18.177  -1.636  -16.260 1.00 63.10  ? 123  GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 123 ? 18.776  -0.572  -15.967 1.00 56.65  ? 123  GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 123 ? 18.044  -2.025  -17.441 1.00 72.17  ? 123  GLU A OE2   1 
ATOM   991  N  N     . LYS A 1 124 ? 19.102  -3.192  -11.592 1.00 27.72  ? 124  LYS A N     1 
ATOM   992  C  CA    . LYS A 1 124 ? 20.061  -4.187  -11.139 1.00 28.48  ? 124  LYS A CA    1 
ATOM   993  C  C     . LYS A 1 124 ? 19.451  -5.093  -10.080 1.00 30.13  ? 124  LYS A C     1 
ATOM   994  O  O     . LYS A 1 124 ? 19.585  -6.323  -10.156 1.00 30.35  ? 124  LYS A O     1 
ATOM   995  C  CB    . LYS A 1 124 ? 21.311  -3.490  -10.607 1.00 27.93  ? 124  LYS A CB    1 
ATOM   996  C  CG    . LYS A 1 124 ? 22.001  -2.640  -11.684 1.00 39.02  ? 124  LYS A CG    1 
ATOM   997  C  CD    . LYS A 1 124 ? 23.075  -1.730  -11.091 1.00 50.91  ? 124  LYS A CD    1 
ATOM   998  C  CE    . LYS A 1 124 ? 23.520  -0.681  -12.099 1.00 58.40  ? 124  LYS A CE    1 
ATOM   999  N  NZ    . LYS A 1 124 ? 24.791  -0.039  -11.670 1.00 63.82  ? 124  LYS A NZ    1 
ATOM   1000 N  N     . ALA A 1 125 ? 18.761  -4.504  -9.097  1.00 25.94  ? 125  ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 125 ? 18.134  -5.299  -8.034  1.00 25.19  ? 125  ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 125 ? 17.113  -6.279  -8.595  1.00 21.62  ? 125  ALA A C     1 
ATOM   1003 O  O     . ALA A 1 125 ? 17.054  -7.440  -8.172  1.00 29.24  ? 125  ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 125 ? 17.478  -4.362  -7.016  1.00 24.71  ? 125  ALA A CB    1 
ATOM   1005 N  N     . PHE A 1 126 ? 16.295  -5.818  -9.546  1.00 24.34  ? 126  PHE A N     1 
ATOM   1006 C  CA    . PHE A 1 126 ? 15.251  -6.642  -10.149 1.00 20.93  ? 126  PHE A CA    1 
ATOM   1007 C  C     . PHE A 1 126 ? 15.866  -7.807  -10.910 1.00 28.18  ? 126  PHE A C     1 
ATOM   1008 O  O     . PHE A 1 126 ? 15.452  -8.963  -10.756 1.00 23.81  ? 126  PHE A O     1 
ATOM   1009 C  CB    . PHE A 1 126 ? 14.407  -5.754  -11.070 1.00 25.57  ? 126  PHE A CB    1 
ATOM   1010 C  CG    . PHE A 1 126 ? 13.282  -6.470  -11.784 1.00 30.16  ? 126  PHE A CG    1 
ATOM   1011 C  CD1   . PHE A 1 126 ? 12.041  -6.618  -11.181 1.00 28.03  ? 126  PHE A CD1   1 
ATOM   1012 C  CD2   . PHE A 1 126 ? 13.452  -6.952  -13.073 1.00 33.19  ? 126  PHE A CD2   1 
ATOM   1013 C  CE1   . PHE A 1 126 ? 10.998  -7.263  -11.841 1.00 30.63  ? 126  PHE A CE1   1 
ATOM   1014 C  CE2   . PHE A 1 126 ? 12.409  -7.603  -13.743 1.00 36.57  ? 126  PHE A CE2   1 
ATOM   1015 C  CZ    . PHE A 1 126 ? 11.178  -7.753  -13.127 1.00 31.71  ? 126  PHE A CZ    1 
ATOM   1016 N  N     . ASN A 1 127 ? 16.877  -7.523  -11.721 1.00 23.75  ? 127  ASN A N     1 
ATOM   1017 C  CA    . ASN A 1 127 ? 17.503  -8.582  -12.516 1.00 25.71  ? 127  ASN A CA    1 
ATOM   1018 C  C     . ASN A 1 127 ? 18.235  -9.588  -11.652 1.00 24.02  ? 127  ASN A C     1 
ATOM   1019 O  O     . ASN A 1 127 ? 18.388  -10.740 -12.057 1.00 29.41  ? 127  ASN A O     1 
ATOM   1020 C  CB    . ASN A 1 127 ? 18.456  -7.965  -13.535 1.00 26.81  ? 127  ASN A CB    1 
ATOM   1021 C  CG    . ASN A 1 127 ? 17.719  -7.300  -14.672 1.00 34.12  ? 127  ASN A CG    1 
ATOM   1022 O  OD1   . ASN A 1 127 ? 16.589  -7.672  -14.998 1.00 35.18  ? 127  ASN A OD1   1 
ATOM   1023 N  ND2   . ASN A 1 127 ? 18.349  -6.308  -15.284 1.00 43.09  ? 127  ASN A ND2   1 
ATOM   1024 N  N     . ALA A 1 128 ? 18.689  -9.184  -10.473 1.00 29.56  ? 128  ALA A N     1 
ATOM   1025 C  CA    . ALA A 1 128 ? 19.316  -10.121 -9.561  1.00 26.88  ? 128  ALA A CA    1 
ATOM   1026 C  C     . ALA A 1 128 ? 18.316  -11.071 -8.902  1.00 32.84  ? 128  ALA A C     1 
ATOM   1027 O  O     . ALA A 1 128 ? 18.739  -12.079 -8.332  1.00 36.34  ? 128  ALA A O     1 
ATOM   1028 C  CB    . ALA A 1 128 ? 20.087  -9.363  -8.476  1.00 32.77  ? 128  ALA A CB    1 
ATOM   1029 N  N     . ARG A 1 129 ? 17.013  -10.797 -8.994  1.00 27.54  ? 129  ARG A N     1 
ATOM   1030 C  CA    . ARG A 1 129 ? 16.006  -11.457 -8.174  1.00 24.22  ? 129  ARG A CA    1 
ATOM   1031 C  C     . ARG A 1 129 ? 15.012  -12.278 -8.980  1.00 23.07  ? 129  ARG A C     1 
ATOM   1032 O  O     . ARG A 1 129 ? 14.810  -13.455 -8.686  1.00 25.48  ? 129  ARG A O     1 
ATOM   1033 C  CB    . ARG A 1 129 ? 15.248  -10.406 -7.337  1.00 22.07  ? 129  ARG A CB    1 
ATOM   1034 C  CG    . ARG A 1 129 ? 15.959  -9.982  -6.065  1.00 24.91  ? 129  ARG A CG    1 
ATOM   1035 C  CD    . ARG A 1 129 ? 15.423  -8.641  -5.516  1.00 23.46  ? 129  ARG A CD    1 
ATOM   1036 N  NE    . ARG A 1 129 ? 16.099  -8.314  -4.265  1.00 26.86  ? 129  ARG A NE    1 
ATOM   1037 C  CZ    . ARG A 1 129 ? 17.328  -7.817  -4.198  1.00 31.60  ? 129  ARG A CZ    1 
ATOM   1038 N  NH1   . ARG A 1 129 ? 17.999  -7.497  -5.291  1.00 34.19  ? 129  ARG A NH1   1 
ATOM   1039 N  NH2   . ARG A 1 129 ? 17.896  -7.638  -3.009  1.00 31.13  ? 129  ARG A NH2   1 
ATOM   1040 N  N     . PHE A 1 130 ? 14.386  -11.694 -9.982  1.00 24.33  ? 130  PHE A N     1 
ATOM   1041 C  CA    . PHE A 1 130 ? 13.193  -12.293 -10.563 1.00 25.74  ? 130  PHE A CA    1 
ATOM   1042 C  C     . PHE A 1 130 ? 13.397  -13.331 -11.663 1.00 27.03  ? 130  PHE A C     1 
ATOM   1043 O  O     . PHE A 1 130 ? 12.575  -14.258 -11.777 1.00 25.18  ? 130  PHE A O     1 
ATOM   1044 C  CB    . PHE A 1 130 ? 12.286  -11.181 -11.076 1.00 21.79  ? 130  PHE A CB    1 
ATOM   1045 C  CG    . PHE A 1 130 ? 11.437  -10.580 -9.966  1.00 22.93  ? 130  PHE A CG    1 
ATOM   1046 C  CD1   . PHE A 1 130 ? 11.925  -9.547  -9.191  1.00 23.85  ? 130  PHE A CD1   1 
ATOM   1047 C  CD2   . PHE A 1 130 ? 10.199  -11.117 -9.662  1.00 23.58  ? 130  PHE A CD2   1 
ATOM   1048 C  CE1   . PHE A 1 130 ? 11.144  -8.999  -8.144  1.00 21.73  ? 130  PHE A CE1   1 
ATOM   1049 C  CE2   . PHE A 1 130 ? 9.410   -10.582 -8.626  1.00 23.00  ? 130  PHE A CE2   1 
ATOM   1050 C  CZ    . PHE A 1 130 ? 9.897   -9.524  -7.871  1.00 20.82  ? 130  PHE A CZ    1 
ATOM   1051 N  N     . PRO A 1 131 ? 14.422  -13.208 -12.526 1.00 26.78  ? 131  PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 131 ? 14.592  -14.231 -13.568 1.00 24.89  ? 131  PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 131 ? 14.573  -15.639 -13.005 1.00 23.17  ? 131  PRO A C     1 
ATOM   1054 O  O     . PRO A 1 131 ? 15.358  -15.992 -12.119 1.00 30.01  ? 131  PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 131 ? 15.952  -13.864 -14.188 1.00 22.82  ? 131  PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 131 ? 15.945  -12.376 -14.111 1.00 24.26  ? 131  PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 131 ? 15.409  -12.124 -12.692 1.00 25.84  ? 131  PRO A CD    1 
ATOM   1058 N  N     . GLY A 1 132 ? 13.625  -16.440 -13.482 1.00 26.01  ? 132  GLY A N     1 
ATOM   1059 C  CA    . GLY A 1 132 ? 13.497  -17.809 -13.028 1.00 22.02  ? 132  GLY A CA    1 
ATOM   1060 C  C     . GLY A 1 132 ? 12.937  -18.000 -11.638 1.00 26.28  ? 132  GLY A C     1 
ATOM   1061 O  O     . GLY A 1 132 ? 12.940  -19.133 -11.156 1.00 23.48  ? 132  GLY A O     1 
ATOM   1062 N  N     . CYS A 1 133 ? 12.430  -16.946 -10.977 1.00 26.18  ? 133  CYS A N     1 
ATOM   1063 C  CA    . CYS A 1 133 ? 12.152  -17.090 -9.543  1.00 22.92  ? 133  CYS A CA    1 
ATOM   1064 C  C     . CYS A 1 133 ? 10.961  -17.987 -9.243  1.00 22.32  ? 133  CYS A C     1 
ATOM   1065 O  O     . CYS A 1 133 ? 10.856  -18.471 -8.117  1.00 22.79  ? 133  CYS A O     1 
ATOM   1066 C  CB    . CYS A 1 133 ? 11.941  -15.729 -8.868  1.00 22.28  ? 133  CYS A CB    1 
ATOM   1067 S  SG    . CYS A 1 133 ? 10.516  -14.824 -9.417  1.00 25.13  ? 133  CYS A SG    1 
ATOM   1068 N  N     . MET A 1 134 ? 10.061  -18.232 -10.195 1.00 19.72  ? 134  MET A N     1 
ATOM   1069 C  CA    . MET A 1 134 ? 8.915   -19.092 -9.896  1.00 18.71  ? 134  MET A CA    1 
ATOM   1070 C  C     . MET A 1 134 ? 9.061   -20.488 -10.490 1.00 22.91  ? 134  MET A C     1 
ATOM   1071 O  O     . MET A 1 134 ? 8.059   -21.186 -10.665 1.00 24.11  ? 134  MET A O     1 
ATOM   1072 C  CB    . MET A 1 134 ? 7.627   -18.470 -10.413 1.00 20.62  ? 134  MET A CB    1 
ATOM   1073 C  CG    . MET A 1 134 ? 7.243   -17.116 -9.724  1.00 18.34  ? 134  MET A CG    1 
ATOM   1074 S  SD    . MET A 1 134 ? 5.728   -16.535 -10.477 1.00 22.40  ? 134  MET A SD    1 
ATOM   1075 C  CE    . MET A 1 134 ? 5.586   -14.920 -9.680  1.00 24.15  ? 134  MET A CE    1 
ATOM   1076 N  N     . LYS A 1 135 ? 10.276  -20.888 -10.842 1.00 28.50  ? 135  LYS A N     1 
ATOM   1077 C  CA    . LYS A 1 135 ? 10.472  -22.196 -11.459 1.00 26.16  ? 135  LYS A CA    1 
ATOM   1078 C  C     . LYS A 1 135 ? 9.874   -23.292 -10.581 1.00 25.99  ? 135  LYS A C     1 
ATOM   1079 O  O     . LYS A 1 135 ? 10.166  -23.372 -9.385  1.00 31.17  ? 135  LYS A O     1 
ATOM   1080 C  CB    . LYS A 1 135 ? 11.963  -22.447 -11.692 1.00 27.33  ? 135  LYS A CB    1 
ATOM   1081 C  CG    . LYS A 1 135 ? 12.234  -23.444 -12.805 1.00 35.10  ? 135  LYS A CG    1 
ATOM   1082 C  CD    . LYS A 1 135 ? 12.413  -22.716 -14.140 1.00 41.43  ? 135  LYS A CD    1 
ATOM   1083 C  CE    . LYS A 1 135 ? 12.492  -23.686 -15.320 1.00 54.95  ? 135  LYS A CE    1 
ATOM   1084 N  NZ    . LYS A 1 135 ? 13.516  -24.759 -15.100 1.00 61.13  ? 135  LYS A NZ    1 
ATOM   1085 N  N     . GLY A 1 136 ? 9.001   -24.110 -11.174 1.00 22.40  ? 136  GLY A N     1 
ATOM   1086 C  CA    . GLY A 1 136 ? 8.398   -25.237 -10.484 1.00 22.39  ? 136  GLY A CA    1 
ATOM   1087 C  C     . GLY A 1 136 ? 7.178   -24.914 -9.642  1.00 25.81  ? 136  GLY A C     1 
ATOM   1088 O  O     . GLY A 1 136 ? 6.636   -25.820 -9.001  1.00 27.28  ? 136  GLY A O     1 
ATOM   1089 N  N     . ARG A 1 137 ? 6.733   -23.656 -9.623  1.00 27.65  ? 137  ARG A N     1 
ATOM   1090 C  CA    . ARG A 1 137 ? 5.594   -23.199 -8.833  1.00 25.64  ? 137  ARG A CA    1 
ATOM   1091 C  C     . ARG A 1 137 ? 4.473   -22.717 -9.745  1.00 21.28  ? 137  ARG A C     1 
ATOM   1092 O  O     . ARG A 1 137 ? 4.643   -22.578 -10.954 1.00 24.94  ? 137  ARG A O     1 
ATOM   1093 C  CB    . ARG A 1 137 ? 6.004   -22.079 -7.884  1.00 25.64  ? 137  ARG A CB    1 
ATOM   1094 C  CG    . ARG A 1 137 ? 7.174   -22.407 -6.986  1.00 24.81  ? 137  ARG A CG    1 
ATOM   1095 C  CD    . ARG A 1 137 ? 7.256   -21.379 -5.870  1.00 25.80  ? 137  ARG A CD    1 
ATOM   1096 N  NE    . ARG A 1 137 ? 8.306   -21.697 -4.919  1.00 26.98  ? 137  ARG A NE    1 
ATOM   1097 C  CZ    . ARG A 1 137 ? 8.144   -22.481 -3.867  1.00 28.11  ? 137  ARG A CZ    1 
ATOM   1098 N  NH1   . ARG A 1 137 ? 6.984   -23.047 -3.606  1.00 30.33  ? 137  ARG A NH1   1 
ATOM   1099 N  NH2   . ARG A 1 137 ? 9.174   -22.702 -3.055  1.00 36.09  ? 137  ARG A NH2   1 
ATOM   1100 N  N     . THR A 1 138 ? 3.304   -22.461 -9.155  1.00 19.62  ? 138  THR A N     1 
ATOM   1101 C  CA    . THR A 1 138 ? 2.166   -21.923 -9.894  1.00 22.71  ? 138  THR A CA    1 
ATOM   1102 C  C     . THR A 1 138 ? 2.183   -20.406 -9.770  1.00 23.11  ? 138  THR A C     1 
ATOM   1103 O  O     . THR A 1 138 ? 2.384   -19.880 -8.669  1.00 24.25  ? 138  THR A O     1 
ATOM   1104 C  CB    . THR A 1 138 ? 0.838   -22.455 -9.339  1.00 25.98  ? 138  THR A CB    1 
ATOM   1105 O  OG1   . THR A 1 138 ? 0.724   -23.857 -9.588  1.00 25.64  ? 138  THR A OG1   1 
ATOM   1106 C  CG2   . THR A 1 138 ? -0.361  -21.757 -9.974  1.00 24.49  ? 138  THR A CG2   1 
ATOM   1107 N  N     . MET A 1 139 ? 1.977   -19.707 -10.890 1.00 19.66  ? 139  MET A N     1 
ATOM   1108 C  CA    . MET A 1 139 ? 1.739   -18.267 -10.872 1.00 18.38  ? 139  MET A CA    1 
ATOM   1109 C  C     . MET A 1 139 ? 0.237   -18.030 -10.814 1.00 21.63  ? 139  MET A C     1 
ATOM   1110 O  O     . MET A 1 139 ? -0.483  -18.332 -11.773 1.00 23.97  ? 139  MET A O     1 
ATOM   1111 C  CB    . MET A 1 139 ? 2.339   -17.588 -12.103 1.00 22.14  ? 139  MET A CB    1 
ATOM   1112 C  CG    . MET A 1 139 ? 1.787   -16.156 -12.297 1.00 23.57  ? 139  MET A CG    1 
ATOM   1113 S  SD    . MET A 1 139 ? 2.435   -15.250 -13.740 1.00 25.97  ? 139  MET A SD    1 
ATOM   1114 C  CE    . MET A 1 139 ? 4.062   -14.917 -13.154 1.00 23.04  ? 139  MET A CE    1 
ATOM   1115 N  N     . TYR A 1 140 ? -0.241  -17.486 -9.694  1.00 23.62  ? 140  TYR A N     1 
ATOM   1116 C  CA    . TYR A 1 140 ? -1.640  -17.120 -9.544  1.00 19.18  ? 140  TYR A CA    1 
ATOM   1117 C  C     . TYR A 1 140 ? -1.877  -15.690 -10.019 1.00 21.48  ? 140  TYR A C     1 
ATOM   1118 O  O     . TYR A 1 140 ? -1.082  -14.783 -9.747  1.00 19.67  ? 140  TYR A O     1 
ATOM   1119 C  CB    . TYR A 1 140 ? -2.081  -17.250 -8.076  1.00 21.43  ? 140  TYR A CB    1 
ATOM   1120 C  CG    . TYR A 1 140 ? -1.929  -18.640 -7.508  1.00 17.73  ? 140  TYR A CG    1 
ATOM   1121 C  CD1   . TYR A 1 140 ? -2.934  -19.590 -7.681  1.00 19.51  ? 140  TYR A CD1   1 
ATOM   1122 C  CD2   . TYR A 1 140 ? -0.787  -19.011 -6.806  1.00 18.17  ? 140  TYR A CD2   1 
ATOM   1123 C  CE1   . TYR A 1 140 ? -2.812  -20.882 -7.163  1.00 19.24  ? 140  TYR A CE1   1 
ATOM   1124 C  CE2   . TYR A 1 140 ? -0.654  -20.314 -6.297  1.00 20.08  ? 140  TYR A CE2   1 
ATOM   1125 C  CZ    . TYR A 1 140 ? -1.668  -21.241 -6.483  1.00 25.99  ? 140  TYR A CZ    1 
ATOM   1126 O  OH    . TYR A 1 140 ? -1.539  -22.540 -5.998  1.00 26.46  ? 140  TYR A OH    1 
ATOM   1127 N  N     . VAL A 1 141 ? -2.987  -15.486 -10.719 1.00 18.00  ? 141  VAL A N     1 
ATOM   1128 C  CA    . VAL A 1 141 ? -3.337  -14.174 -11.235 1.00 23.31  ? 141  VAL A CA    1 
ATOM   1129 C  C     . VAL A 1 141 ? -4.561  -13.709 -10.445 1.00 22.32  ? 141  VAL A C     1 
ATOM   1130 O  O     . VAL A 1 141 ? -5.651  -14.277 -10.576 1.00 21.75  ? 141  VAL A O     1 
ATOM   1131 C  CB    . VAL A 1 141 ? -3.599  -14.208 -12.747 1.00 22.34  ? 141  VAL A CB    1 
ATOM   1132 C  CG1   . VAL A 1 141 ? -4.011  -12.870 -13.232 1.00 19.18  ? 141  VAL A CG1   1 
ATOM   1133 C  CG2   . VAL A 1 141 ? -2.350  -14.650 -13.492 1.00 21.53  ? 141  VAL A CG2   1 
ATOM   1134 N  N     . ILE A 1 142 ? -4.390  -12.668 -9.641  1.00 18.95  ? 142  ILE A N     1 
ATOM   1135 C  CA    . ILE A 1 142 ? -5.446  -12.209 -8.729  1.00 18.06  ? 142  ILE A CA    1 
ATOM   1136 C  C     . ILE A 1 142 ? -6.023  -10.888 -9.236  1.00 20.14  ? 142  ILE A C     1 
ATOM   1137 O  O     . ILE A 1 142 ? -5.400  -9.838  -9.043  1.00 19.70  ? 142  ILE A O     1 
ATOM   1138 C  CB    . ILE A 1 142 ? -4.893  -12.019 -7.308  1.00 20.35  ? 142  ILE A CB    1 
ATOM   1139 C  CG1   . ILE A 1 142 ? -4.161  -13.262 -6.811  1.00 20.61  ? 142  ILE A CG1   1 
ATOM   1140 C  CG2   . ILE A 1 142 ? -5.998  -11.618 -6.335  1.00 22.20  ? 142  ILE A CG2   1 
ATOM   1141 C  CD1   . ILE A 1 142 ? -3.304  -12.998 -5.542  1.00 18.24  ? 142  ILE A CD1   1 
ATOM   1142 N  N     . PRO A 1 143 ? -7.192  -10.870 -9.878  1.00 18.91  ? 143  PRO A N     1 
ATOM   1143 C  CA    . PRO A 1 143 ? -7.816  -9.581  -10.204 1.00 16.71  ? 143  PRO A CA    1 
ATOM   1144 C  C     . PRO A 1 143 ? -8.580  -9.086  -8.985  1.00 20.07  ? 143  PRO A C     1 
ATOM   1145 O  O     . PRO A 1 143 ? -9.399  -9.817  -8.425  1.00 19.50  ? 143  PRO A O     1 
ATOM   1146 C  CB    . PRO A 1 143 ? -8.762  -9.923  -11.365 1.00 19.89  ? 143  PRO A CB    1 
ATOM   1147 C  CG    . PRO A 1 143 ? -8.803  -11.485 -11.448 1.00 27.05  ? 143  PRO A CG    1 
ATOM   1148 C  CD    . PRO A 1 143 ? -8.064  -12.008 -10.229 1.00 23.97  ? 143  PRO A CD    1 
ATOM   1149 N  N     . PHE A 1 144 ? -8.278  -7.874  -8.535  1.00 20.91  ? 144  PHE A N     1 
ATOM   1150 C  CA    . PHE A 1 144 ? -8.919  -7.403  -7.313  1.00 21.12  ? 144  PHE A CA    1 
ATOM   1151 C  C     . PHE A 1 144 ? -9.291  -5.928  -7.414  1.00 17.72  ? 144  PHE A C     1 
ATOM   1152 O  O     . PHE A 1 144 ? -8.660  -5.140  -8.128  1.00 21.47  ? 144  PHE A O     1 
ATOM   1153 C  CB    . PHE A 1 144 ? -8.043  -7.653  -6.055  1.00 19.21  ? 144  PHE A CB    1 
ATOM   1154 C  CG    . PHE A 1 144 ? -6.761  -6.862  -6.022  1.00 19.80  ? 144  PHE A CG    1 
ATOM   1155 C  CD1   . PHE A 1 144 ? -5.653  -7.294  -6.723  1.00 20.55  ? 144  PHE A CD1   1 
ATOM   1156 C  CD2   . PHE A 1 144 ? -6.660  -5.682  -5.277  1.00 19.45  ? 144  PHE A CD2   1 
ATOM   1157 C  CE1   . PHE A 1 144 ? -4.471  -6.589  -6.697  1.00 22.58  ? 144  PHE A CE1   1 
ATOM   1158 C  CE2   . PHE A 1 144 ? -5.468  -4.971  -5.248  1.00 21.09  ? 144  PHE A CE2   1 
ATOM   1159 C  CZ    . PHE A 1 144 ? -4.383  -5.421  -5.952  1.00 21.53  ? 144  PHE A CZ    1 
ATOM   1160 N  N     . SER A 1 145 ? -10.333 -5.568  -6.671  1.00 21.75  ? 145  SER A N     1 
ATOM   1161 C  CA    . SER A 1 145 ? -10.792 -4.190  -6.580  1.00 23.68  ? 145  SER A CA    1 
ATOM   1162 C  C     . SER A 1 145 ? -10.559 -3.677  -5.172  1.00 18.95  ? 145  SER A C     1 
ATOM   1163 O  O     . SER A 1 145 ? -10.885 -4.365  -4.193  1.00 19.69  ? 145  SER A O     1 
ATOM   1164 C  CB    . SER A 1 145 ? -12.282 -4.055  -6.908  1.00 25.00  ? 145  SER A CB    1 
ATOM   1165 O  OG    . SER A 1 145 ? -12.637 -2.691  -6.795  1.00 25.65  ? 145  SER A OG    1 
ATOM   1166 N  N     . MET A 1 146 ? -9.997  -2.477  -5.081  1.00 19.49  ? 146  MET A N     1 
ATOM   1167 C  CA    . MET A 1 146 ? -9.875  -1.755  -3.828  1.00 20.72  ? 146  MET A CA    1 
ATOM   1168 C  C     . MET A 1 146 ? -11.063 -0.808  -3.768  1.00 25.22  ? 146  MET A C     1 
ATOM   1169 O  O     . MET A 1 146 ? -11.185 0.082   -4.622  1.00 21.18  ? 146  MET A O     1 
ATOM   1170 C  CB    . MET A 1 146 ? -8.555  -0.981  -3.767  1.00 24.59  ? 146  MET A CB    1 
ATOM   1171 C  CG    . MET A 1 146 ? -7.306  -1.878  -3.831  1.00 24.68  ? 146  MET A CG    1 
ATOM   1172 S  SD    . MET A 1 146 ? -7.360  -3.180  -2.606  1.00 26.99  ? 146  MET A SD    1 
ATOM   1173 C  CE    . MET A 1 146 ? -7.248  -2.304  -1.045  1.00 25.90  ? 146  MET A CE    1 
ATOM   1174 N  N     . GLY A 1 147 ? -11.943 -1.013  -2.790  1.00 25.54  ? 147  GLY A N     1 
ATOM   1175 C  CA    . GLY A 1 147 ? -13.195 -0.302  -2.767  1.00 28.35  ? 147  GLY A CA    1 
ATOM   1176 C  C     . GLY A 1 147 ? -14.302 -1.106  -3.425  1.00 34.29  ? 147  GLY A C     1 
ATOM   1177 O  O     . GLY A 1 147 ? -14.057 -2.060  -4.180  1.00 28.53  ? 147  GLY A O     1 
ATOM   1178 N  N     . PRO A 1 148 ? -15.553 -0.737  -3.138  1.00 34.07  ? 148  PRO A N     1 
ATOM   1179 C  CA    . PRO A 1 148 ? -16.692 -1.414  -3.775  1.00 35.07  ? 148  PRO A CA    1 
ATOM   1180 C  C     . PRO A 1 148 ? -16.614 -1.342  -5.293  1.00 40.80  ? 148  PRO A C     1 
ATOM   1181 O  O     . PRO A 1 148 ? -16.258 -0.308  -5.865  1.00 42.67  ? 148  PRO A O     1 
ATOM   1182 C  CB    . PRO A 1 148 ? -17.901 -0.635  -3.238  1.00 34.62  ? 148  PRO A CB    1 
ATOM   1183 C  CG    . PRO A 1 148 ? -17.440 -0.135  -1.916  1.00 31.70  ? 148  PRO A CG    1 
ATOM   1184 C  CD    . PRO A 1 148 ? -15.990 0.234   -2.122  1.00 30.48  ? 148  PRO A CD    1 
ATOM   1185 N  N     . LEU A 1 149 ? -16.961 -2.456  -5.943  1.00 37.62  ? 149  LEU A N     1 
ATOM   1186 C  CA    . LEU A 1 149 ? -16.936 -2.517  -7.399  1.00 42.90  ? 149  LEU A CA    1 
ATOM   1187 C  C     . LEU A 1 149 ? -17.831 -1.445  -8.000  1.00 56.19  ? 149  LEU A C     1 
ATOM   1188 O  O     . LEU A 1 149 ? -19.047 -1.447  -7.791  1.00 57.91  ? 149  LEU A O     1 
ATOM   1189 C  CB    . LEU A 1 149 ? -17.377 -3.896  -7.872  1.00 46.05  ? 149  LEU A CB    1 
ATOM   1190 C  CG    . LEU A 1 149 ? -16.239 -4.868  -8.170  1.00 49.55  ? 149  LEU A CG    1 
ATOM   1191 C  CD1   . LEU A 1 149 ? -16.789 -6.200  -8.671  1.00 46.01  ? 149  LEU A CD1   1 
ATOM   1192 C  CD2   . LEU A 1 149 ? -15.302 -4.256  -9.181  1.00 45.99  ? 149  LEU A CD2   1 
ATOM   1193 N  N     . GLY A 1 150 ? -17.229 -0.529  -8.746  1.00 57.98  ? 150  GLY A N     1 
ATOM   1194 C  CA    . GLY A 1 150 ? -17.980 0.540   -9.351  1.00 56.30  ? 150  GLY A CA    1 
ATOM   1195 C  C     . GLY A 1 150 ? -18.097 1.801   -8.526  1.00 61.13  ? 150  GLY A C     1 
ATOM   1196 O  O     . GLY A 1 150 ? -18.722 2.762   -8.992  1.00 66.15  ? 150  GLY A O     1 
ATOM   1197 N  N     . SER A 1 151 ? -17.542 1.837   -7.317  1.00 49.54  ? 151  SER A N     1 
ATOM   1198 C  CA    . SER A 1 151 ? -17.459 3.111   -6.617  1.00 46.32  ? 151  SER A CA    1 
ATOM   1199 C  C     . SER A 1 151 ? -16.595 4.090   -7.418  1.00 50.32  ? 151  SER A C     1 
ATOM   1200 O  O     . SER A 1 151 ? -15.623 3.678   -8.064  1.00 46.16  ? 151  SER A O     1 
ATOM   1201 C  CB    . SER A 1 151 ? -16.874 2.935   -5.214  1.00 46.21  ? 151  SER A CB    1 
ATOM   1202 O  OG    . SER A 1 151 ? -16.550 4.203   -4.639  1.00 42.08  ? 151  SER A OG    1 
ATOM   1203 N  N     . PRO A 1 152 ? -16.915 5.390   -7.399  1.00 47.55  ? 152  PRO A N     1 
ATOM   1204 C  CA    . PRO A 1 152 ? -16.025 6.369   -8.046  1.00 51.17  ? 152  PRO A CA    1 
ATOM   1205 C  C     . PRO A 1 152 ? -14.622 6.368   -7.473  1.00 45.93  ? 152  PRO A C     1 
ATOM   1206 O  O     . PRO A 1 152 ? -13.664 6.714   -8.181  1.00 40.85  ? 152  PRO A O     1 
ATOM   1207 C  CB    . PRO A 1 152 ? -16.733 7.708   -7.784  1.00 49.91  ? 152  PRO A CB    1 
ATOM   1208 C  CG    . PRO A 1 152 ? -17.571 7.455   -6.572  1.00 53.62  ? 152  PRO A CG    1 
ATOM   1209 C  CD    . PRO A 1 152 ? -18.055 6.043   -6.737  1.00 49.37  ? 152  PRO A CD    1 
ATOM   1210 N  N     . LEU A 1 153 ? -14.474 6.000   -6.204  1.00 36.07  ? 153  LEU A N     1 
ATOM   1211 C  CA    . LEU A 1 153 ? -13.170 5.965   -5.570  1.00 43.51  ? 153  LEU A CA    1 
ATOM   1212 C  C     . LEU A 1 153 ? -12.474 4.608   -5.714  1.00 35.65  ? 153  LEU A C     1 
ATOM   1213 O  O     . LEU A 1 153 ? -11.367 4.445   -5.190  1.00 37.75  ? 153  LEU A O     1 
ATOM   1214 C  CB    . LEU A 1 153 ? -13.302 6.357   -4.096  1.00 34.90  ? 153  LEU A CB    1 
ATOM   1215 C  CG    . LEU A 1 153 ? -13.570 7.877   -3.912  1.00 52.01  ? 153  LEU A CG    1 
ATOM   1216 C  CD1   . LEU A 1 153 ? -14.040 8.243   -2.498  1.00 38.40  ? 153  LEU A CD1   1 
ATOM   1217 C  CD2   . LEU A 1 153 ? -12.354 8.731   -4.326  1.00 42.40  ? 153  LEU A CD2   1 
ATOM   1218 N  N     . ALA A 1 154 ? -13.079 3.646   -6.411  1.00 31.80  ? 154  ALA A N     1 
ATOM   1219 C  CA    . ALA A 1 154 ? -12.476 2.317   -6.503  1.00 32.15  ? 154  ALA A CA    1 
ATOM   1220 C  C     . ALA A 1 154 ? -11.400 2.279   -7.581  1.00 28.24  ? 154  ALA A C     1 
ATOM   1221 O  O     . ALA A 1 154 ? -11.464 2.987   -8.586  1.00 33.65  ? 154  ALA A O     1 
ATOM   1222 C  CB    . ALA A 1 154 ? -13.521 1.239   -6.794  1.00 33.34  ? 154  ALA A CB    1 
ATOM   1223 N  N     . LYS A 1 155 ? -10.408 1.424   -7.369  1.00 28.04  ? 155  LYS A N     1 
ATOM   1224 C  CA    . LYS A 1 155 ? -9.313  1.238   -8.305  1.00 18.23  ? 155  LYS A CA    1 
ATOM   1225 C  C     . LYS A 1 155 ? -8.982  -0.246  -8.355  1.00 27.03  ? 155  LYS A C     1 
ATOM   1226 O  O     . LYS A 1 155 ? -9.119  -0.950  -7.355  1.00 22.66  ? 155  LYS A O     1 
ATOM   1227 C  CB    . LYS A 1 155 ? -8.093  2.046   -7.879  1.00 31.05  ? 155  LYS A CB    1 
ATOM   1228 C  CG    . LYS A 1 155 ? -8.338  3.557   -7.862  1.00 31.87  ? 155  LYS A CG    1 
ATOM   1229 C  CD    . LYS A 1 155 ? -7.027  4.261   -8.017  1.00 45.42  ? 155  LYS A CD    1 
ATOM   1230 C  CE    . LYS A 1 155 ? -6.506  4.044   -9.439  1.00 55.24  ? 155  LYS A CE    1 
ATOM   1231 N  NZ    . LYS A 1 155 ? -7.401  4.675   -10.462 1.00 60.41  ? 155  LYS A NZ    1 
ATOM   1232 N  N     . ILE A 1 156 ? -8.562  -0.720  -9.526  1.00 28.17  ? 156  ILE A N     1 
ATOM   1233 C  CA    . ILE A 1 156 ? -8.417  -2.153  -9.780  1.00 25.24  ? 156  ILE A CA    1 
ATOM   1234 C  C     . ILE A 1 156 ? -6.937  -2.497  -9.863  1.00 24.56  ? 156  ILE A C     1 
ATOM   1235 O  O     . ILE A 1 156 ? -6.131  -1.719  -10.393 1.00 22.61  ? 156  ILE A O     1 
ATOM   1236 C  CB    . ILE A 1 156 ? -9.176  -2.564  -11.059 1.00 23.07  ? 156  ILE A CB    1 
ATOM   1237 C  CG1   . ILE A 1 156 ? -10.677 -2.516  -10.770 1.00 22.25  ? 156  ILE A CG1   1 
ATOM   1238 C  CG2   . ILE A 1 156 ? -8.763  -3.970  -11.529 1.00 25.46  ? 156  ILE A CG2   1 
ATOM   1239 C  CD1   . ILE A 1 156 ? -11.573 -2.689  -11.929 1.00 26.20  ? 156  ILE A CD1   1 
ATOM   1240 N  N     . GLY A 1 157 ? -6.575  -3.648  -9.300  1.00 28.14  ? 157  GLY A N     1 
ATOM   1241 C  CA    . GLY A 1 157 ? -5.225  -4.143  -9.407  1.00 19.47  ? 157  GLY A CA    1 
ATOM   1242 C  C     . GLY A 1 157 ? -5.212  -5.566  -9.925  1.00 21.49  ? 157  GLY A C     1 
ATOM   1243 O  O     . GLY A 1 157 ? -6.197  -6.302  -9.828  1.00 20.66  ? 157  GLY A O     1 
ATOM   1244 N  N     . ILE A 1 158 ? -4.068  -5.943  -10.495 1.00 20.49  ? 158  ILE A N     1 
ATOM   1245 C  CA    . ILE A 1 158 ? -3.785  -7.337  -10.828 1.00 20.63  ? 158  ILE A CA    1 
ATOM   1246 C  C     . ILE A 1 158 ? -2.542  -7.734  -10.052 1.00 19.93  ? 158  ILE A C     1 
ATOM   1247 O  O     . ILE A 1 158 ? -1.485  -7.128  -10.253 1.00 22.60  ? 158  ILE A O     1 
ATOM   1248 C  CB    . ILE A 1 158 ? -3.546  -7.543  -12.327 1.00 26.53  ? 158  ILE A CB    1 
ATOM   1249 C  CG1   . ILE A 1 158 ? -4.720  -7.035  -13.160 1.00 27.61  ? 158  ILE A CG1   1 
ATOM   1250 C  CG2   . ILE A 1 158 ? -3.236  -9.022  -12.595 1.00 19.82  ? 158  ILE A CG2   1 
ATOM   1251 C  CD1   . ILE A 1 158 ? -5.942  -7.885  -13.045 1.00 24.45  ? 158  ILE A CD1   1 
ATOM   1252 N  N     . GLU A 1 159 ? -2.655  -8.738  -9.166  1.00 18.17  ? 159  GLU A N     1 
ATOM   1253 C  CA    . GLU A 1 159 ? -1.479  -9.266  -8.469  1.00 18.59  ? 159  GLU A CA    1 
ATOM   1254 C  C     . GLU A 1 159 ? -1.107  -10.631 -9.053  1.00 20.20  ? 159  GLU A C     1 
ATOM   1255 O  O     . GLU A 1 159 ? -1.939  -11.545 -9.095  1.00 18.82  ? 159  GLU A O     1 
ATOM   1256 C  CB    . GLU A 1 159 ? -1.668  -9.389  -6.948  1.00 17.81  ? 159  GLU A CB    1 
ATOM   1257 C  CG    . GLU A 1 159 ? -0.340  -9.907  -6.279  1.00 16.46  ? 159  GLU A CG    1 
ATOM   1258 C  CD    . GLU A 1 159 ? -0.202  -9.716  -4.760  1.00 21.52  ? 159  GLU A CD    1 
ATOM   1259 O  OE1   . GLU A 1 159 ? -0.999  -8.955  -4.160  1.00 19.28  ? 159  GLU A OE1   1 
ATOM   1260 O  OE2   . GLU A 1 159 ? 0.738   -10.319 -4.163  1.00 16.46  ? 159  GLU A OE2   1 
ATOM   1261 N  N     . LEU A 1 160 ? 0.144   -10.756 -9.491  1.00 15.26  ? 160  LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 160 ? 0.760   -12.037 -9.817  1.00 17.49  ? 160  LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 160 ? 1.539   -12.502 -8.598  1.00 20.46  ? 160  LEU A C     1 
ATOM   1264 O  O     . LEU A 1 160 ? 2.301   -11.721 -8.029  1.00 20.65  ? 160  LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 160 ? 1.719   -11.915 -11.013 1.00 15.58  ? 160  LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 160 ? 1.191   -11.127 -12.200 1.00 19.82  ? 160  LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 160 ? 2.244   -11.023 -13.330 1.00 16.50  ? 160  LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 160 ? -0.115  -11.722 -12.679 1.00 20.99  ? 160  LEU A CD2   1 
ATOM   1269 N  N     . THR A 1 161 ? 1.337   -13.756 -8.184  1.00 18.73  ? 161  THR A N     1 
ATOM   1270 C  CA    . THR A 1 161 ? 2.035   -14.263 -7.008  1.00 19.32  ? 161  THR A CA    1 
ATOM   1271 C  C     . THR A 1 161 ? 2.267   -15.760 -7.158  1.00 16.98  ? 161  THR A C     1 
ATOM   1272 O  O     . THR A 1 161 ? 1.527   -16.454 -7.857  1.00 17.94  ? 161  THR A O     1 
ATOM   1273 C  CB    . THR A 1 161 ? 1.245   -13.973 -5.706  1.00 21.11  ? 161  THR A CB    1 
ATOM   1274 O  OG1   . THR A 1 161 ? 1.980   -14.444 -4.562  1.00 18.43  ? 161  THR A OG1   1 
ATOM   1275 C  CG2   . THR A 1 161 ? -0.123  -14.670 -5.725  1.00 16.22  ? 161  THR A CG2   1 
ATOM   1276 N  N     . ASP A 1 162 ? 3.302   -16.265 -6.490  1.00 14.49  ? 162  ASP A N     1 
ATOM   1277 C  CA    . ASP A 1 162 ? 3.504   -17.708 -6.432  1.00 20.85  ? 162  ASP A CA    1 
ATOM   1278 C  C     . ASP A 1 162 ? 3.139   -18.286 -5.061  1.00 21.15  ? 162  ASP A C     1 
ATOM   1279 O  O     . ASP A 1 162 ? 3.504   -19.413 -4.750  1.00 20.28  ? 162  ASP A O     1 
ATOM   1280 C  CB    . ASP A 1 162 ? 4.944   -18.063 -6.824  1.00 17.87  ? 162  ASP A CB    1 
ATOM   1281 C  CG    . ASP A 1 162 ? 5.989   -17.267 -6.035  1.00 22.07  ? 162  ASP A CG    1 
ATOM   1282 O  OD1   . ASP A 1 162 ? 5.598   -16.548 -5.079  1.00 19.94  ? 162  ASP A OD1   1 
ATOM   1283 O  OD2   . ASP A 1 162 ? 7.193   -17.339 -6.397  1.00 23.64  ? 162  ASP A OD2   1 
ATOM   1284 N  N     . SER A 1 163 ? 2.400   -17.538 -4.238  1.00 18.54  ? 163  SER A N     1 
ATOM   1285 C  CA    . SER A 1 163 ? 2.073   -17.980 -2.887  1.00 19.67  ? 163  SER A CA    1 
ATOM   1286 C  C     . SER A 1 163 ? 0.579   -18.227 -2.763  1.00 21.48  ? 163  SER A C     1 
ATOM   1287 O  O     . SER A 1 163 ? -0.200  -17.255 -2.785  1.00 18.59  ? 163  SER A O     1 
ATOM   1288 C  CB    . SER A 1 163 ? 2.503   -16.925 -1.863  1.00 22.63  ? 163  SER A CB    1 
ATOM   1289 O  OG    . SER A 1 163 ? 1.835   -17.156 -0.618  1.00 18.91  ? 163  SER A OG    1 
ATOM   1290 N  N     . PRO A 1 164 ? 0.119   -19.475 -2.570  1.00 18.90  ? 164  PRO A N     1 
ATOM   1291 C  CA    . PRO A 1 164 ? -1.328  -19.666 -2.345  1.00 19.84  ? 164  PRO A CA    1 
ATOM   1292 C  C     . PRO A 1 164 ? -1.837  -18.976 -1.082  1.00 20.39  ? 164  PRO A C     1 
ATOM   1293 O  O     . PRO A 1 164 ? -3.020  -18.621 -1.014  1.00 18.38  ? 164  PRO A O     1 
ATOM   1294 C  CB    . PRO A 1 164 ? -1.495  -21.190 -2.275  1.00 22.98  ? 164  PRO A CB    1 
ATOM   1295 C  CG    . PRO A 1 164 ? -0.122  -21.751 -2.075  1.00 27.81  ? 164  PRO A CG    1 
ATOM   1296 C  CD    . PRO A 1 164 ? 0.889   -20.733 -2.546  1.00 19.85  ? 164  PRO A CD    1 
ATOM   1297 N  N     . TYR A 1 165 ? -0.980  -18.779 -0.076  1.00 17.58  ? 165  TYR A N     1 
ATOM   1298 C  CA    . TYR A 1 165 ? -1.388  -18.050 1.122   1.00 19.74  ? 165  TYR A CA    1 
ATOM   1299 C  C     . TYR A 1 165 ? -1.772  -16.611 0.796   1.00 21.36  ? 165  TYR A C     1 
ATOM   1300 O  O     . TYR A 1 165 ? -2.729  -16.073 1.367   1.00 18.90  ? 165  TYR A O     1 
ATOM   1301 C  CB    . TYR A 1 165 ? -0.251  -18.105 2.144   1.00 20.92  ? 165  TYR A CB    1 
ATOM   1302 C  CG    . TYR A 1 165 ? -0.370  -17.168 3.337   1.00 21.46  ? 165  TYR A CG    1 
ATOM   1303 C  CD1   . TYR A 1 165 ? 0.139   -15.877 3.283   1.00 21.52  ? 165  TYR A CD1   1 
ATOM   1304 C  CD2   . TYR A 1 165 ? -0.946  -17.592 4.528   1.00 20.07  ? 165  TYR A CD2   1 
ATOM   1305 C  CE1   . TYR A 1 165 ? 0.065   -15.027 4.361   1.00 21.94  ? 165  TYR A CE1   1 
ATOM   1306 C  CE2   . TYR A 1 165 ? -1.032  -16.731 5.625   1.00 21.81  ? 165  TYR A CE2   1 
ATOM   1307 C  CZ    . TYR A 1 165 ? -0.525  -15.452 5.528   1.00 18.82  ? 165  TYR A CZ    1 
ATOM   1308 O  OH    . TYR A 1 165 ? -0.602  -14.605 6.607   1.00 20.00  ? 165  TYR A OH    1 
ATOM   1309 N  N     . VAL A 1 166 ? -1.019  -15.960 -0.105  1.00 17.48  ? 166  VAL A N     1 
ATOM   1310 C  CA    . VAL A 1 166 ? -1.379  -14.626 -0.560  1.00 18.01  ? 166  VAL A CA    1 
ATOM   1311 C  C     . VAL A 1 166 ? -2.729  -14.653 -1.265  1.00 21.03  ? 166  VAL A C     1 
ATOM   1312 O  O     . VAL A 1 166 ? -3.548  -13.751 -1.082  1.00 19.85  ? 166  VAL A O     1 
ATOM   1313 C  CB    . VAL A 1 166 ? -0.268  -14.054 -1.471  1.00 19.07  ? 166  VAL A CB    1 
ATOM   1314 C  CG1   . VAL A 1 166 ? -0.743  -12.814 -2.185  1.00 18.18  ? 166  VAL A CG1   1 
ATOM   1315 C  CG2   . VAL A 1 166 ? 0.982   -13.755 -0.633  1.00 19.23  ? 166  VAL A CG2   1 
ATOM   1316 N  N     . VAL A 1 167 ? -2.989  -15.679 -2.088  1.00 16.14  ? 167  VAL A N     1 
ATOM   1317 C  CA    . VAL A 1 167 ? -4.275  -15.739 -2.791  1.00 16.38  ? 167  VAL A CA    1 
ATOM   1318 C  C     . VAL A 1 167 ? -5.432  -15.803 -1.790  1.00 18.31  ? 167  VAL A C     1 
ATOM   1319 O  O     . VAL A 1 167 ? -6.410  -15.045 -1.885  1.00 17.76  ? 167  VAL A O     1 
ATOM   1320 C  CB    . VAL A 1 167 ? -4.302  -16.931 -3.760  1.00 19.37  ? 167  VAL A CB    1 
ATOM   1321 C  CG1   . VAL A 1 167 ? -5.667  -16.996 -4.438  1.00 19.32  ? 167  VAL A CG1   1 
ATOM   1322 C  CG2   . VAL A 1 167 ? -3.160  -16.789 -4.797  1.00 18.06  ? 167  VAL A CG2   1 
ATOM   1323 N  N     . ALA A 1 168 ? -5.313  -16.678 -0.793  1.00 17.30  ? 168  ALA A N     1 
ATOM   1324 C  CA    . ALA A 1 168 ? -6.399  -16.849 0.166   1.00 20.12  ? 168  ALA A CA    1 
ATOM   1325 C  C     . ALA A 1 168 ? -6.615  -15.575 0.969   1.00 20.21  ? 168  ALA A C     1 
ATOM   1326 O  O     . ALA A 1 168 ? -7.757  -15.160 1.203   1.00 19.66  ? 168  ALA A O     1 
ATOM   1327 C  CB    . ALA A 1 168 ? -6.095  -18.025 1.094   1.00 20.00  ? 168  ALA A CB    1 
ATOM   1328 N  N     . SER A 1 169 ? -5.519  -14.946 1.387   1.00 16.77  ? 169  SER A N     1 
ATOM   1329 C  CA    . SER A 1 169 ? -5.595  -13.722 2.178   1.00 16.25  ? 169  SER A CA    1 
ATOM   1330 C  C     . SER A 1 169 ? -6.171  -12.560 1.369   1.00 18.60  ? 169  SER A C     1 
ATOM   1331 O  O     . SER A 1 169 ? -6.950  -11.756 1.896   1.00 19.49  ? 169  SER A O     1 
ATOM   1332 C  CB    . SER A 1 169 ? -4.205  -13.380 2.704   1.00 20.02  ? 169  SER A CB    1 
ATOM   1333 O  OG    . SER A 1 169 ? -3.746  -14.386 3.589   1.00 21.34  ? 169  SER A OG    1 
ATOM   1334 N  N     . MET A 1 170 ? -5.791  -12.449 0.092   1.00 15.81  ? 170  MET A N     1 
ATOM   1335 C  CA    . MET A 1 170 ? -6.334  -11.417 -0.789  1.00 19.50  ? 170  MET A CA    1 
ATOM   1336 C  C     . MET A 1 170 ? -7.821  -11.627 -1.051  1.00 18.89  ? 170  MET A C     1 
ATOM   1337 O  O     . MET A 1 170 ? -8.552  -10.660 -1.305  1.00 21.02  ? 170  MET A O     1 
ATOM   1338 C  CB    . MET A 1 170 ? -5.556  -11.418 -2.123  1.00 17.10  ? 170  MET A CB    1 
ATOM   1339 C  CG    . MET A 1 170 ? -4.130  -10.893 -2.026  1.00 18.37  ? 170  MET A CG    1 
ATOM   1340 S  SD    . MET A 1 170 ? -4.123  -9.098  -1.703  1.00 19.70  ? 170  MET A SD    1 
ATOM   1341 C  CE    . MET A 1 170 ? -4.447  -8.412  -3.315  1.00 17.80  ? 170  MET A CE    1 
ATOM   1342 N  N     . ARG A 1 171 ? -8.279  -12.882 -1.039  1.00 18.05  ? 171  ARG A N     1 
ATOM   1343 C  CA    . ARG A 1 171 ? -9.715  -13.124 -1.179  1.00 17.05  ? 171  ARG A CA    1 
ATOM   1344 C  C     . ARG A 1 171 ? -10.482 -12.496 -0.025  1.00 19.33  ? 171  ARG A C     1 
ATOM   1345 O  O     . ARG A 1 171 ? -11.594 -12.002 -0.219  1.00 21.15  ? 171  ARG A O     1 
ATOM   1346 C  CB    . ARG A 1 171 ? -10.023 -14.630 -1.223  1.00 22.71  ? 171  ARG A CB    1 
ATOM   1347 C  CG    . ARG A 1 171 ? -11.488 -14.897 -1.605  1.00 24.33  ? 171  ARG A CG    1 
ATOM   1348 C  CD    . ARG A 1 171 ? -11.842 -16.411 -1.687  1.00 30.82  ? 171  ARG A CD    1 
ATOM   1349 N  NE    . ARG A 1 171 ? -13.166 -16.606 -2.279  1.00 27.71  ? 171  ARG A NE    1 
ATOM   1350 C  CZ    . ARG A 1 171 ? -14.308 -16.649 -1.597  1.00 32.30  ? 171  ARG A CZ    1 
ATOM   1351 N  NH1   . ARG A 1 171 ? -14.336 -16.570 -0.275  1.00 28.95  ? 171  ARG A NH1   1 
ATOM   1352 N  NH2   . ARG A 1 171 ? -15.455 -16.750 -2.260  1.00 34.22  ? 171  ARG A NH2   1 
ATOM   1353 N  N     . ILE A 1 172 ? -9.895  -12.503 1.171   1.00 15.10  ? 172  ILE A N     1 
ATOM   1354 C  CA    . ILE A 1 172 ? -10.522 -11.887 2.339   1.00 15.56  ? 172  ILE A CA    1 
ATOM   1355 C  C     . ILE A 1 172 ? -10.335 -10.371 2.329   1.00 18.45  ? 172  ILE A C     1 
ATOM   1356 O  O     . ILE A 1 172 ? -11.282 -9.598  2.560   1.00 20.70  ? 172  ILE A O     1 
ATOM   1357 C  CB    . ILE A 1 172 ? -9.946  -12.544 3.619   1.00 16.92  ? 172  ILE A CB    1 
ATOM   1358 C  CG1   . ILE A 1 172 ? -10.305 -14.042 3.648   1.00 20.06  ? 172  ILE A CG1   1 
ATOM   1359 C  CG2   . ILE A 1 172 ? -10.421 -11.839 4.889   1.00 17.01  ? 172  ILE A CG2   1 
ATOM   1360 C  CD1   . ILE A 1 172 ? -9.510  -14.839 4.679   1.00 21.54  ? 172  ILE A CD1   1 
ATOM   1361 N  N     . MET A 1 173 ? -9.129  -9.915  2.018   1.00 20.37  ? 173  MET A N     1 
ATOM   1362 C  CA    . MET A 1 173 ? -8.808  -8.512  2.195   1.00 19.50  ? 173  MET A CA    1 
ATOM   1363 C  C     . MET A 1 173 ? -9.256  -7.627  1.039   1.00 22.84  ? 173  MET A C     1 
ATOM   1364 O  O     . MET A 1 173 ? -9.343  -6.413  1.233   1.00 20.19  ? 173  MET A O     1 
ATOM   1365 C  CB    . MET A 1 173 ? -7.305  -8.368  2.451   1.00 22.01  ? 173  MET A CB    1 
ATOM   1366 C  CG    . MET A 1 173 ? -6.860  -8.979  3.812   1.00 16.05  ? 173  MET A CG    1 
ATOM   1367 S  SD    . MET A 1 173 ? -7.803  -8.342  5.250   1.00 18.60  ? 173  MET A SD    1 
ATOM   1368 C  CE    . MET A 1 173 ? -7.443  -6.576  5.069   1.00 16.42  ? 173  MET A CE    1 
ATOM   1369 N  N     . THR A 1 174 ? -9.551  -8.181  -0.145  1.00 17.82  ? 174  THR A N     1 
ATOM   1370 C  CA    . THR A 1 174 ? -9.984  -7.383  -1.282  1.00 18.19  ? 174  THR A CA    1 
ATOM   1371 C  C     . THR A 1 174 ? -11.254 -7.992  -1.868  1.00 17.11  ? 174  THR A C     1 
ATOM   1372 O  O     . THR A 1 174 ? -11.713 -9.050  -1.420  1.00 18.21  ? 174  THR A O     1 
ATOM   1373 C  CB    . THR A 1 174 ? -8.869  -7.274  -2.344  1.00 20.02  ? 174  THR A CB    1 
ATOM   1374 O  OG1   . THR A 1 174 ? -8.672  -8.560  -2.970  1.00 20.30  ? 174  THR A OG1   1 
ATOM   1375 C  CG2   . THR A 1 174 ? -7.557  -6.865  -1.678  1.00 16.29  ? 174  THR A CG2   1 
ATOM   1376 N  N     . ARG A 1 175 ? -11.853 -7.291  -2.842  1.00 17.35  ? 175  ARG A N     1 
ATOM   1377 C  CA    . ARG A 1 175 ? -12.830 -7.899  -3.743  1.00 21.08  ? 175  ARG A CA    1 
ATOM   1378 C  C     . ARG A 1 175 ? -12.084 -8.528  -4.919  1.00 18.46  ? 175  ARG A C     1 
ATOM   1379 O  O     . ARG A 1 175 ? -11.463 -7.816  -5.700  1.00 21.84  ? 175  ARG A O     1 
ATOM   1380 C  CB    . ARG A 1 175 ? -13.842 -6.888  -4.270  1.00 18.68  ? 175  ARG A CB    1 
ATOM   1381 C  CG    . ARG A 1 175 ? -14.967 -6.514  -3.266  1.00 29.52  ? 175  ARG A CG    1 
ATOM   1382 C  CD    . ARG A 1 175 ? -14.547 -5.380  -2.438  1.00 28.71  ? 175  ARG A CD    1 
ATOM   1383 N  NE    . ARG A 1 175 ? -15.654 -4.745  -1.717  1.00 28.89  ? 175  ARG A NE    1 
ATOM   1384 C  CZ    . ARG A 1 175 ? -15.478 -3.852  -0.752  1.00 27.26  ? 175  ARG A CZ    1 
ATOM   1385 N  NH1   . ARG A 1 175 ? -14.278 -3.368  -0.470  1.00 28.45  ? 175  ARG A NH1   1 
ATOM   1386 N  NH2   . ARG A 1 175 ? -16.524 -3.465  -0.024  1.00 26.69  ? 175  ARG A NH2   1 
ATOM   1387 N  N     . MET A 1 176 ? -12.216 -9.845  -5.083  1.00 21.15  ? 176  MET A N     1 
ATOM   1388 C  CA    . MET A 1 176 ? -11.349 -10.634 -5.965  1.00 24.41  ? 176  MET A CA    1 
ATOM   1389 C  C     . MET A 1 176 ? -12.145 -11.568 -6.879  1.00 25.64  ? 176  MET A C     1 
ATOM   1390 O  O     . MET A 1 176 ? -13.045 -12.269 -6.412  1.00 24.54  ? 176  MET A O     1 
ATOM   1391 C  CB    . MET A 1 176 ? -10.404 -11.491 -5.098  1.00 24.43  ? 176  MET A CB    1 
ATOM   1392 C  CG    . MET A 1 176 ? -9.276  -12.072 -5.848  1.00 30.76  ? 176  MET A CG    1 
ATOM   1393 S  SD    . MET A 1 176 ? -9.587  -13.744 -6.374  1.00 33.83  ? 176  MET A SD    1 
ATOM   1394 C  CE    . MET A 1 176 ? -9.073  -14.623 -4.898  1.00 28.88  ? 176  MET A CE    1 
ATOM   1395 N  N     . GLY A 1 177 ? -11.785 -11.613 -8.171  1.00 24.59  ? 177  GLY A N     1 
ATOM   1396 C  CA    . GLY A 1 177 ? -12.221 -12.679 -9.040  1.00 26.55  ? 177  GLY A CA    1 
ATOM   1397 C  C     . GLY A 1 177 ? -12.720 -12.171 -10.379 1.00 29.86  ? 177  GLY A C     1 
ATOM   1398 O  O     . GLY A 1 177 ? -12.443 -11.047 -10.796 1.00 28.27  ? 177  GLY A O     1 
ATOM   1399 N  N     . THR A 1 178 ? -13.500 -13.035 -11.033 1.00 31.33  ? 178  THR A N     1 
ATOM   1400 C  CA    . THR A 1 178 ? -13.912 -12.791 -12.412 1.00 32.48  ? 178  THR A CA    1 
ATOM   1401 C  C     . THR A 1 178 ? -14.693 -11.492 -12.560 1.00 31.79  ? 178  THR A C     1 
ATOM   1402 O  O     . THR A 1 178 ? -14.553 -10.806 -13.576 1.00 34.40  ? 178  THR A O     1 
ATOM   1403 C  CB    . THR A 1 178 ? -14.743 -13.973 -12.916 1.00 31.11  ? 178  THR A CB    1 
ATOM   1404 O  OG1   . THR A 1 178 ? -14.014 -15.168 -12.662 1.00 29.42  ? 178  THR A OG1   1 
ATOM   1405 C  CG2   . THR A 1 178 ? -14.988 -13.873 -14.416 1.00 34.95  ? 178  THR A CG2   1 
ATOM   1406 N  N     . SER A 1 179 ? -15.523 -11.137 -11.568 1.00 32.09  ? 179  SER A N     1 
ATOM   1407 C  CA    . SER A 1 179 ? -16.314 -9.904  -11.682 1.00 33.85  ? 179  SER A CA    1 
ATOM   1408 C  C     . SER A 1 179 ? -15.425 -8.669  -11.813 1.00 34.59  ? 179  SER A C     1 
ATOM   1409 O  O     . SER A 1 179 ? -15.826 -7.686  -12.454 1.00 36.48  ? 179  SER A O     1 
ATOM   1410 C  CB    . SER A 1 179 ? -17.257 -9.749  -10.485 1.00 35.33  ? 179  SER A CB    1 
ATOM   1411 O  OG    . SER A 1 179 ? -16.538 -9.636  -9.269  1.00 39.55  ? 179  SER A OG    1 
ATOM   1412 N  N     . VAL A 1 180 ? -14.218 -8.695  -11.230 1.00 32.14  ? 180  VAL A N     1 
ATOM   1413 C  CA    . VAL A 1 180 ? -13.310 -7.555  -11.369 1.00 28.08  ? 180  VAL A CA    1 
ATOM   1414 C  C     . VAL A 1 180 ? -12.835 -7.409  -12.817 1.00 35.25  ? 180  VAL A C     1 
ATOM   1415 O  O     . VAL A 1 180 ? -12.786 -6.293  -13.359 1.00 37.77  ? 180  VAL A O     1 
ATOM   1416 C  CB    . VAL A 1 180 ? -12.113 -7.679  -10.408 1.00 26.92  ? 180  VAL A CB    1 
ATOM   1417 C  CG1   . VAL A 1 180 ? -11.280 -6.376  -10.463 1.00 25.80  ? 180  VAL A CG1   1 
ATOM   1418 C  CG2   . VAL A 1 180 ? -12.574 -7.974  -8.995  1.00 25.73  ? 180  VAL A CG2   1 
ATOM   1419 N  N     . LEU A 1 181 ? -12.449 -8.525  -13.453 1.00 29.07  ? 181  LEU A N     1 
ATOM   1420 C  CA    . LEU A 1 181 ? -12.038 -8.489  -14.855 1.00 31.50  ? 181  LEU A CA    1 
ATOM   1421 C  C     . LEU A 1 181 ? -13.145 -7.949  -15.757 1.00 32.03  ? 181  LEU A C     1 
ATOM   1422 O  O     . LEU A 1 181 ? -12.883 -7.161  -16.672 1.00 36.92  ? 181  LEU A O     1 
ATOM   1423 C  CB    . LEU A 1 181 ? -11.612 -9.892  -15.311 1.00 34.68  ? 181  LEU A CB    1 
ATOM   1424 C  CG    . LEU A 1 181 ? -10.266 -10.386 -14.786 1.00 33.36  ? 181  LEU A CG    1 
ATOM   1425 C  CD1   . LEU A 1 181 ? -10.050 -11.878 -15.072 1.00 31.77  ? 181  LEU A CD1   1 
ATOM   1426 C  CD2   . LEU A 1 181 ? -9.149  -9.559  -15.387 1.00 36.02  ? 181  LEU A CD2   1 
ATOM   1427 N  N     . GLU A 1 182 ? -14.389 -8.372  -15.532 1.00 37.33  ? 182  GLU A N     1 
ATOM   1428 C  CA    . GLU A 1 182 ? -15.467 -7.849  -16.360 1.00 38.35  ? 182  GLU A CA    1 
ATOM   1429 C  C     . GLU A 1 182 ? -15.646 -6.347  -16.159 1.00 41.45  ? 182  GLU A C     1 
ATOM   1430 O  O     . GLU A 1 182 ? -15.910 -5.624  -17.126 1.00 46.28  ? 182  GLU A O     1 
ATOM   1431 C  CB    . GLU A 1 182 ? -16.758 -8.608  -16.069 1.00 41.19  ? 182  GLU A CB    1 
ATOM   1432 C  CG    . GLU A 1 182 ? -16.627 -10.092 -16.353 1.00 44.04  ? 182  GLU A CG    1 
ATOM   1433 C  CD    . GLU A 1 182 ? -17.867 -10.863 -15.953 1.00 60.09  ? 182  GLU A CD    1 
ATOM   1434 O  OE1   . GLU A 1 182 ? -18.813 -10.217 -15.443 1.00 59.64  ? 182  GLU A OE1   1 
ATOM   1435 O  OE2   . GLU A 1 182 ? -17.897 -12.107 -16.144 1.00 60.43  ? 182  GLU A OE2   1 
ATOM   1436 N  N     . ALA A 1 183 ? -15.463 -5.859  -14.928 1.00 35.02  ? 183  ALA A N     1 
ATOM   1437 C  CA    . ALA A 1 183 ? -15.524 -4.432  -14.638 1.00 32.79  ? 183  ALA A CA    1 
ATOM   1438 C  C     . ALA A 1 183 ? -14.332 -3.667  -15.188 1.00 33.95  ? 183  ALA A C     1 
ATOM   1439 O  O     . ALA A 1 183 ? -14.468 -2.489  -15.543 1.00 37.63  ? 183  ALA A O     1 
ATOM   1440 C  CB    . ALA A 1 183 ? -15.607 -4.203  -13.125 1.00 33.96  ? 183  ALA A CB    1 
ATOM   1441 N  N     . LEU A 1 184 ? -13.157 -4.292  -15.234 1.00 35.43  ? 184  LEU A N     1 
ATOM   1442 C  CA    . LEU A 1 184 ? -11.956 -3.581  -15.669 1.00 32.74  ? 184  LEU A CA    1 
ATOM   1443 C  C     . LEU A 1 184 ? -11.988 -3.310  -17.167 1.00 35.55  ? 184  LEU A C     1 
ATOM   1444 O  O     . LEU A 1 184 ? -11.563 -2.241  -17.628 1.00 39.03  ? 184  LEU A O     1 
ATOM   1445 C  CB    . LEU A 1 184 ? -10.716 -4.393  -15.296 1.00 33.45  ? 184  LEU A CB    1 
ATOM   1446 C  CG    . LEU A 1 184 ? -9.397  -3.888  -15.867 1.00 34.52  ? 184  LEU A CG    1 
ATOM   1447 C  CD1   . LEU A 1 184 ? -9.006  -2.583  -15.179 1.00 32.14  ? 184  LEU A CD1   1 
ATOM   1448 C  CD2   . LEU A 1 184 ? -8.308  -4.942  -15.718 1.00 32.33  ? 184  LEU A CD2   1 
ATOM   1449 N  N     . GLY A 1 185 ? -12.479 -4.275  -17.942 1.00 36.06  ? 185  GLY A N     1 
ATOM   1450 C  CA    . GLY A 1 185 ? -12.462 -4.151  -19.391 1.00 42.78  ? 185  GLY A CA    1 
ATOM   1451 C  C     . GLY A 1 185 ? -11.080 -3.774  -19.886 1.00 44.39  ? 185  GLY A C     1 
ATOM   1452 O  O     . GLY A 1 185 ? -10.078 -4.399  -19.526 1.00 40.09  ? 185  GLY A O     1 
ATOM   1453 N  N     . ASP A 1 186 ? -11.012 -2.713  -20.693 1.00 42.47  ? 186  ASP A N     1 
ATOM   1454 C  CA    . ASP A 1 186 ? -9.742  -2.201  -21.195 1.00 44.63  ? 186  ASP A CA    1 
ATOM   1455 C  C     . ASP A 1 186 ? -9.231  -1.015  -20.390 1.00 43.16  ? 186  ASP A C     1 
ATOM   1456 O  O     . ASP A 1 186 ? -8.390  -0.258  -20.884 1.00 43.50  ? 186  ASP A O     1 
ATOM   1457 C  CB    . ASP A 1 186 ? -9.857  -1.817  -22.670 1.00 50.98  ? 186  ASP A CB    1 
ATOM   1458 C  CG    . ASP A 1 186 ? -9.796  -3.022  -23.599 1.00 58.34  ? 186  ASP A CG    1 
ATOM   1459 O  OD1   . ASP A 1 186 ? -9.034  -3.979  -23.312 1.00 52.63  ? 186  ASP A OD1   1 
ATOM   1460 O  OD2   . ASP A 1 186 ? -10.515 -3.007  -24.624 1.00 72.25  ? 186  ASP A OD2   1 
ATOM   1461 N  N     . GLY A 1 187 ? -9.701  -0.847  -19.159 1.00 38.15  ? 187  GLY A N     1 
ATOM   1462 C  CA    . GLY A 1 187 ? -9.271  0.267   -18.342 1.00 38.53  ? 187  GLY A CA    1 
ATOM   1463 C  C     . GLY A 1 187 ? -7.883  0.056   -17.768 1.00 35.81  ? 187  GLY A C     1 
ATOM   1464 O  O     . GLY A 1 187 ? -7.252  -0.987  -17.937 1.00 36.68  ? 187  GLY A O     1 
ATOM   1465 N  N     . GLU A 1 188 ? -7.401  1.076   -17.065 1.00 36.84  ? 188  GLU A N     1 
ATOM   1466 C  CA    . GLU A 1 188 ? -6.099  0.978   -16.418 1.00 41.33  ? 188  GLU A CA    1 
ATOM   1467 C  C     . GLU A 1 188 ? -6.198  0.186   -15.114 1.00 37.78  ? 188  GLU A C     1 
ATOM   1468 O  O     . GLU A 1 188 ? -7.256  0.124   -14.476 1.00 33.74  ? 188  GLU A O     1 
ATOM   1469 C  CB    . GLU A 1 188 ? -5.530  2.363   -16.127 1.00 41.73  ? 188  GLU A CB    1 
ATOM   1470 C  CG    . GLU A 1 188 ? -5.149  3.148   -17.368 1.00 58.40  ? 188  GLU A CG    1 
ATOM   1471 C  CD    . GLU A 1 188 ? -4.549  4.503   -17.043 1.00 66.64  ? 188  GLU A CD    1 
ATOM   1472 O  OE1   . GLU A 1 188 ? -4.461  4.854   -15.840 1.00 63.56  ? 188  GLU A OE1   1 
ATOM   1473 O  OE2   . GLU A 1 188 ? -4.161  5.216   -17.997 1.00 80.63  ? 188  GLU A OE2   1 
ATOM   1474 N  N     . PHE A 1 189 ? -5.066  -0.394  -14.713 1.00 30.91  ? 189  PHE A N     1 
ATOM   1475 C  CA    . PHE A 1 189 ? -4.963  -1.150  -13.470 1.00 29.58  ? 189  PHE A CA    1 
ATOM   1476 C  C     . PHE A 1 189 ? -3.553  -1.001  -12.905 1.00 24.95  ? 189  PHE A C     1 
ATOM   1477 O  O     . PHE A 1 189 ? -2.606  -0.683  -13.622 1.00 25.23  ? 189  PHE A O     1 
ATOM   1478 C  CB    . PHE A 1 189 ? -5.318  -2.637  -13.688 1.00 28.16  ? 189  PHE A CB    1 
ATOM   1479 C  CG    . PHE A 1 189 ? -4.443  -3.347  -14.693 1.00 32.02  ? 189  PHE A CG    1 
ATOM   1480 C  CD1   . PHE A 1 189 ? -4.747  -3.315  -16.051 1.00 33.39  ? 189  PHE A CD1   1 
ATOM   1481 C  CD2   . PHE A 1 189 ? -3.328  -4.079  -14.277 1.00 25.45  ? 189  PHE A CD2   1 
ATOM   1482 C  CE1   . PHE A 1 189 ? -3.947  -3.993  -16.982 1.00 31.30  ? 189  PHE A CE1   1 
ATOM   1483 C  CE2   . PHE A 1 189 ? -2.532  -4.756  -15.200 1.00 27.84  ? 189  PHE A CE2   1 
ATOM   1484 C  CZ    . PHE A 1 189 ? -2.843  -4.708  -16.552 1.00 31.56  ? 189  PHE A CZ    1 
ATOM   1485 N  N     . ILE A 1 190 ? -3.429  -1.198  -11.605 1.00 22.33  ? 190  ILE A N     1 
ATOM   1486 C  CA    . ILE A 1 190 ? -2.125  -1.203  -10.954 1.00 20.95  ? 190  ILE A CA    1 
ATOM   1487 C  C     . ILE A 1 190 ? -1.535  -2.596  -11.100 1.00 20.64  ? 190  ILE A C     1 
ATOM   1488 O  O     . ILE A 1 190 ? -2.192  -3.592  -10.758 1.00 23.19  ? 190  ILE A O     1 
ATOM   1489 C  CB    . ILE A 1 190 ? -2.256  -0.818  -9.473  1.00 25.07  ? 190  ILE A CB    1 
ATOM   1490 C  CG1   . ILE A 1 190 ? -2.971  0.529   -9.312  1.00 25.20  ? 190  ILE A CG1   1 
ATOM   1491 C  CG2   . ILE A 1 190 ? -0.876  -0.871  -8.761  1.00 25.73  ? 190  ILE A CG2   1 
ATOM   1492 C  CD1   . ILE A 1 190 ? -2.329  1.692   -10.049 1.00 30.91  ? 190  ILE A CD1   1 
ATOM   1493 N  N     . LYS A 1 191 ? -0.303  -2.673  -11.611 1.00 19.74  ? 191  LYS A N     1 
ATOM   1494 C  CA    . LYS A 1 191 ? 0.397   -3.937  -11.818 1.00 18.47  ? 191  LYS A CA    1 
ATOM   1495 C  C     . LYS A 1 191 ? 1.156   -4.323  -10.557 1.00 23.41  ? 191  LYS A C     1 
ATOM   1496 O  O     . LYS A 1 191 ? 2.029   -3.574  -10.106 1.00 24.71  ? 191  LYS A O     1 
ATOM   1497 C  CB    . LYS A 1 191 ? 1.358   -3.808  -12.994 1.00 17.56  ? 191  LYS A CB    1 
ATOM   1498 C  CG    . LYS A 1 191 ? 0.648   -3.521  -14.288 1.00 23.98  ? 191  LYS A CG    1 
ATOM   1499 C  CD    . LYS A 1 191 ? 1.658   -3.141  -15.361 1.00 24.85  ? 191  LYS A CD    1 
ATOM   1500 C  CE    . LYS A 1 191 ? 0.981   -2.580  -16.584 1.00 37.19  ? 191  LYS A CE    1 
ATOM   1501 N  NZ    . LYS A 1 191 ? 2.013   -2.400  -17.668 1.00 36.83  ? 191  LYS A NZ    1 
ATOM   1502 N  N     . CYS A 1 192 ? 0.806   -5.470  -9.967  1.00 18.43  ? 192  CYS A N     1 
ATOM   1503 C  CA    . CYS A 1 192 ? 1.437   -5.940  -8.735  1.00 19.30  ? 192  CYS A CA    1 
ATOM   1504 C  C     . CYS A 1 192 ? 2.106   -7.275  -9.015  1.00 21.30  ? 192  CYS A C     1 
ATOM   1505 O  O     . CYS A 1 192 ? 1.436   -8.213  -9.445  1.00 19.88  ? 192  CYS A O     1 
ATOM   1506 C  CB    . CYS A 1 192 ? 0.410   -6.115  -7.620  1.00 18.40  ? 192  CYS A CB    1 
ATOM   1507 S  SG    . CYS A 1 192 ? -0.593  -4.633  -7.340  1.00 23.21  ? 192  CYS A SG    1 
ATOM   1508 N  N     . LEU A 1 193 ? 3.408   -7.370  -8.735  1.00 15.21  ? 193  LEU A N     1 
ATOM   1509 C  CA    . LEU A 1 193 ? 4.170   -8.586  -8.991  1.00 19.58  ? 193  LEU A CA    1 
ATOM   1510 C  C     . LEU A 1 193 ? 4.828   -9.004  -7.691  1.00 20.61  ? 193  LEU A C     1 
ATOM   1511 O  O     . LEU A 1 193 ? 5.497   -8.189  -7.045  1.00 19.34  ? 193  LEU A O     1 
ATOM   1512 C  CB    . LEU A 1 193 ? 5.233   -8.358  -10.088 1.00 15.40  ? 193  LEU A CB    1 
ATOM   1513 C  CG    . LEU A 1 193 ? 6.234   -9.481  -10.350 1.00 21.60  ? 193  LEU A CG    1 
ATOM   1514 C  CD1   . LEU A 1 193 ? 5.568   -10.754 -10.771 1.00 21.98  ? 193  LEU A CD1   1 
ATOM   1515 C  CD2   . LEU A 1 193 ? 7.260   -8.986  -11.415 1.00 20.26  ? 193  LEU A CD2   1 
ATOM   1516 N  N     . HIS A 1 194 ? 4.583   -10.249 -7.282  1.00 19.43  ? 194  HIS A N     1 
ATOM   1517 C  CA    . HIS A 1 194 ? 5.108   -10.778 -6.032  1.00 20.70  ? 194  HIS A CA    1 
ATOM   1518 C  C     . HIS A 1 194 ? 5.732   -12.146 -6.249  1.00 24.09  ? 194  HIS A C     1 
ATOM   1519 O  O     . HIS A 1 194 ? 5.178   -12.963 -6.991  1.00 19.53  ? 194  HIS A O     1 
ATOM   1520 C  CB    . HIS A 1 194 ? 3.990   -10.881 -4.968  1.00 18.05  ? 194  HIS A CB    1 
ATOM   1521 C  CG    . HIS A 1 194 ? 4.447   -11.475 -3.680  1.00 21.17  ? 194  HIS A CG    1 
ATOM   1522 N  ND1   . HIS A 1 194 ? 4.069   -12.737 -3.278  1.00 19.22  ? 194  HIS A ND1   1 
ATOM   1523 C  CD2   . HIS A 1 194 ? 5.284   -11.005 -2.721  1.00 18.60  ? 194  HIS A CD2   1 
ATOM   1524 C  CE1   . HIS A 1 194 ? 4.648   -13.016 -2.122  1.00 21.59  ? 194  HIS A CE1   1 
ATOM   1525 N  NE2   . HIS A 1 194 ? 5.367   -11.972 -1.750  1.00 22.74  ? 194  HIS A NE2   1 
ATOM   1526 N  N     . SER A 1 195 ? 6.858   -12.410 -5.567  1.00 18.82  ? 195  SER A N     1 
ATOM   1527 C  CA    . SER A 1 195 ? 7.405   -13.763 -5.485  1.00 22.19  ? 195  SER A CA    1 
ATOM   1528 C  C     . SER A 1 195 ? 8.034   -13.961 -4.120  1.00 23.74  ? 195  SER A C     1 
ATOM   1529 O  O     . SER A 1 195 ? 8.659   -13.037 -3.584  1.00 23.61  ? 195  SER A O     1 
ATOM   1530 C  CB    . SER A 1 195 ? 8.458   -14.053 -6.583  1.00 20.41  ? 195  SER A CB    1 
ATOM   1531 O  OG    . SER A 1 195 ? 9.015   -15.333 -6.394  1.00 23.33  ? 195  SER A OG    1 
ATOM   1532 N  N     . VAL A 1 196 ? 7.822   -15.151 -3.541  1.00 19.42  ? 196  VAL A N     1 
ATOM   1533 C  CA    . VAL A 1 196 ? 8.514   -15.505 -2.313  1.00 21.35  ? 196  VAL A CA    1 
ATOM   1534 C  C     . VAL A 1 196 ? 9.995   -15.753 -2.537  1.00 23.15  ? 196  VAL A C     1 
ATOM   1535 O  O     . VAL A 1 196 ? 10.745  -15.810 -1.562  1.00 27.94  ? 196  VAL A O     1 
ATOM   1536 C  CB    . VAL A 1 196 ? 7.886   -16.750 -1.639  1.00 27.73  ? 196  VAL A CB    1 
ATOM   1537 C  CG1   . VAL A 1 196 ? 6.400   -16.517 -1.369  1.00 28.00  ? 196  VAL A CG1   1 
ATOM   1538 C  CG2   . VAL A 1 196 ? 8.094   -17.985 -2.490  1.00 21.46  ? 196  VAL A CG2   1 
ATOM   1539 N  N     . GLY A 1 197 ? 10.432  -15.910 -3.788  1.00 24.78  ? 197  GLY A N     1 
ATOM   1540 C  CA    . GLY A 1 197 ? 11.852  -15.960 -4.088  1.00 28.82  ? 197  GLY A CA    1 
ATOM   1541 C  C     . GLY A 1 197 ? 12.515  -17.309 -3.864  1.00 30.80  ? 197  GLY A C     1 
ATOM   1542 O  O     . GLY A 1 197 ? 13.696  -17.359 -3.486  1.00 30.57  ? 197  GLY A O     1 
ATOM   1543 N  N     . CYS A 1 198 ? 11.793  -18.408 -4.069  1.00 25.17  ? 198  CYS A N     1 
ATOM   1544 C  CA    . CYS A 1 198 ? 12.271  -19.750 -3.722  1.00 28.47  ? 198  CYS A CA    1 
ATOM   1545 C  C     . CYS A 1 198 ? 11.984  -20.703 -4.867  1.00 28.57  ? 198  CYS A C     1 
ATOM   1546 O  O     . CYS A 1 198 ? 11.215  -21.667 -4.706  1.00 27.23  ? 198  CYS A O     1 
ATOM   1547 C  CB    . CYS A 1 198 ? 11.607  -20.264 -2.441  1.00 28.29  ? 198  CYS A CB    1 
ATOM   1548 S  SG    . CYS A 1 198 ? 12.137  -19.449 -0.949  1.00 36.46  ? 198  CYS A SG    1 
ATOM   1549 N  N     . PRO A 1 199 ? 12.581  -20.462 -6.038  1.00 25.46  ? 199  PRO A N     1 
ATOM   1550 C  CA    . PRO A 1 199 ? 12.370  -21.365 -7.169  1.00 29.25  ? 199  PRO A CA    1 
ATOM   1551 C  C     . PRO A 1 199 ? 12.763  -22.771 -6.775  1.00 32.12  ? 199  PRO A C     1 
ATOM   1552 O  O     . PRO A 1 199 ? 13.658  -22.967 -5.950  1.00 33.86  ? 199  PRO A O     1 
ATOM   1553 C  CB    . PRO A 1 199 ? 13.306  -20.810 -8.245  1.00 27.97  ? 199  PRO A CB    1 
ATOM   1554 C  CG    . PRO A 1 199 ? 14.400  -20.140 -7.445  1.00 32.53  ? 199  PRO A CG    1 
ATOM   1555 C  CD    . PRO A 1 199 ? 13.634  -19.470 -6.332  1.00 29.83  ? 199  PRO A CD    1 
ATOM   1556 N  N     . LEU A 1 200 ? 12.047  -23.739 -7.320  1.00 32.58  ? 200  LEU A N     1 
ATOM   1557 C  CA    . LEU A 1 200 ? 12.437  -25.119 -7.057  1.00 35.34  ? 200  LEU A CA    1 
ATOM   1558 C  C     . LEU A 1 200 ? 13.444  -25.584 -8.107  1.00 37.97  ? 200  LEU A C     1 
ATOM   1559 O  O     . LEU A 1 200 ? 13.439  -25.090 -9.238  1.00 33.56  ? 200  LEU A O     1 
ATOM   1560 C  CB    . LEU A 1 200 ? 11.212  -26.035 -7.072  1.00 33.53  ? 200  LEU A CB    1 
ATOM   1561 C  CG    . LEU A 1 200 ? 10.046  -25.665 -6.156  1.00 35.13  ? 200  LEU A CG    1 
ATOM   1562 C  CD1   . LEU A 1 200 ? 8.879   -26.618 -6.339  1.00 34.12  ? 200  LEU A CD1   1 
ATOM   1563 C  CD2   . LEU A 1 200 ? 10.513  -25.661 -4.713  1.00 39.66  ? 200  LEU A CD2   1 
ATOM   1564 N  N     . PRO A 1 201 ? 14.343  -26.535 -7.778  1.00 43.97  ? 201  PRO A N     1 
ATOM   1565 C  CA    . PRO A 1 201 ? 14.510  -27.218 -6.489  1.00 45.66  ? 201  PRO A CA    1 
ATOM   1566 C  C     . PRO A 1 201 ? 15.111  -26.281 -5.450  1.00 40.35  ? 201  PRO A C     1 
ATOM   1567 O  O     . PRO A 1 201 ? 15.918  -25.406 -5.765  1.00 42.41  ? 201  PRO A O     1 
ATOM   1568 C  CB    . PRO A 1 201 ? 15.441  -28.396 -6.840  1.00 42.62  ? 201  PRO A CB    1 
ATOM   1569 C  CG    . PRO A 1 201 ? 16.283  -27.874 -7.960  1.00 39.66  ? 201  PRO A CG    1 
ATOM   1570 C  CD    . PRO A 1 201 ? 15.359  -26.968 -8.760  1.00 48.68  ? 201  PRO A CD    1 
ATOM   1571 N  N     . LEU A 1 202 ? 14.725  -26.456 -4.193  1.00 40.75  ? 202  LEU A N     1 
ATOM   1572 C  CA    . LEU A 1 202 ? 15.153  -25.536 -3.156  1.00 46.72  ? 202  LEU A CA    1 
ATOM   1573 C  C     . LEU A 1 202 ? 16.657  -25.612 -2.962  1.00 52.55  ? 202  LEU A C     1 
ATOM   1574 O  O     . LEU A 1 202 ? 17.234  -26.698 -2.901  1.00 61.91  ? 202  LEU A O     1 
ATOM   1575 C  CB    . LEU A 1 202 ? 14.433  -25.854 -1.848  1.00 46.35  ? 202  LEU A CB    1 
ATOM   1576 C  CG    . LEU A 1 202 ? 12.924  -25.608 -1.842  1.00 43.07  ? 202  LEU A CG    1 
ATOM   1577 C  CD1   . LEU A 1 202 ? 12.323  -26.150 -0.562  1.00 36.60  ? 202  LEU A CD1   1 
ATOM   1578 C  CD2   . LEU A 1 202 ? 12.618  -24.128 -1.993  1.00 41.69  ? 202  LEU A CD2   1 
ATOM   1579 N  N     . LYS A 1 203 ? 17.290  -24.448 -2.882  1.00 63.90  ? 203  LYS A N     1 
ATOM   1580 C  CA    . LYS A 1 203 ? 18.700  -24.361 -2.531  1.00 72.05  ? 203  LYS A CA    1 
ATOM   1581 C  C     . LYS A 1 203 ? 18.896  -24.321 -1.021  1.00 77.16  ? 203  LYS A C     1 
ATOM   1582 O  O     . LYS A 1 203 ? 19.830  -24.938 -0.500  1.00 79.14  ? 203  LYS A O     1 
ATOM   1583 C  CB    . LYS A 1 203 ? 19.324  -23.126 -3.188  1.00 72.69  ? 203  LYS A CB    1 
ATOM   1584 C  CG    . LYS A 1 203 ? 19.041  -23.035 -4.680  1.00 69.04  ? 203  LYS A CG    1 
ATOM   1585 C  CD    . LYS A 1 203 ? 19.714  -21.830 -5.304  1.00 78.41  ? 203  LYS A CD    1 
ATOM   1586 C  CE    . LYS A 1 203 ? 19.358  -21.700 -6.783  1.00 83.27  ? 203  LYS A CE    1 
ATOM   1587 N  NZ    . LYS A 1 203 ? 17.918  -21.362 -7.001  1.00 65.15  ? 203  LYS A NZ    1 
ATOM   1588 N  N     . LYS A 1 204 ? 18.018  -23.609 -0.307  1.00 78.96  ? 204  LYS A N     1 
ATOM   1589 C  CA    . LYS A 1 204 ? 17.988  -23.552 1.144   1.00 79.13  ? 204  LYS A CA    1 
ATOM   1590 C  C     . LYS A 1 204 ? 16.759  -24.288 1.661   1.00 72.33  ? 204  LYS A C     1 
ATOM   1591 O  O     . LYS A 1 204 ? 15.677  -24.169 1.074   1.00 68.50  ? 204  LYS A O     1 
ATOM   1592 C  CB    . LYS A 1 204 ? 17.958  -22.101 1.645   1.00 76.64  ? 204  LYS A CB    1 
ATOM   1593 C  CG    . LYS A 1 204 ? 18.884  -21.157 0.889   1.00 77.41  ? 204  LYS A CG    1 
ATOM   1594 C  CD    . LYS A 1 204 ? 18.582  -19.706 1.233   1.00 77.77  ? 204  LYS A CD    1 
ATOM   1595 C  CE    . LYS A 1 204 ? 19.379  -18.735 0.371   1.00 74.68  ? 204  LYS A CE    1 
ATOM   1596 N  NZ    . LYS A 1 204 ? 18.977  -17.319 0.633   1.00 65.99  ? 204  LYS A NZ    1 
ATOM   1597 N  N     . PRO A 1 205 ? 16.889  -25.066 2.735   1.00 78.78  ? 205  PRO A N     1 
ATOM   1598 C  CA    . PRO A 1 205 ? 15.713  -25.746 3.292   1.00 72.76  ? 205  PRO A CA    1 
ATOM   1599 C  C     . PRO A 1 205 ? 14.713  -24.741 3.845   1.00 62.33  ? 205  PRO A C     1 
ATOM   1600 O  O     . PRO A 1 205 ? 15.072  -23.634 4.257   1.00 63.46  ? 205  PRO A O     1 
ATOM   1601 C  CB    . PRO A 1 205 ? 16.300  -26.628 4.400   1.00 74.00  ? 205  PRO A CB    1 
ATOM   1602 C  CG    . PRO A 1 205 ? 17.751  -26.767 4.053   1.00 80.03  ? 205  PRO A CG    1 
ATOM   1603 C  CD    . PRO A 1 205 ? 18.128  -25.460 3.424   1.00 81.13  ? 205  PRO A CD    1 
ATOM   1604 N  N     . LEU A 1 206 ? 13.442  -25.138 3.832   1.00 52.17  ? 206  LEU A N     1 
ATOM   1605 C  CA    . LEU A 1 206 ? 12.350  -24.272 4.248   1.00 45.00  ? 206  LEU A CA    1 
ATOM   1606 C  C     . LEU A 1 206 ? 12.072  -24.461 5.728   1.00 44.10  ? 206  LEU A C     1 
ATOM   1607 O  O     . LEU A 1 206 ? 11.873  -25.589 6.194   1.00 54.47  ? 206  LEU A O     1 
ATOM   1608 C  CB    . LEU A 1 206 ? 11.080  -24.558 3.446   1.00 36.70  ? 206  LEU A CB    1 
ATOM   1609 C  CG    . LEU A 1 206 ? 10.966  -23.996 2.026   1.00 40.55  ? 206  LEU A CG    1 
ATOM   1610 C  CD1   . LEU A 1 206 ? 9.485   -23.812 1.689   1.00 38.09  ? 206  LEU A CD1   1 
ATOM   1611 C  CD2   . LEU A 1 206 ? 11.740  -22.689 1.822   1.00 43.97  ? 206  LEU A CD2   1 
ATOM   1612 N  N     . VAL A 1 207 ? 12.043  -23.365 6.455   1.00 34.97  ? 207  VAL A N     1 
ATOM   1613 C  CA    . VAL A 1 207 ? 11.698  -23.390 7.866   1.00 36.64  ? 207  VAL A CA    1 
ATOM   1614 C  C     . VAL A 1 207 ? 10.193  -23.216 7.999   1.00 41.06  ? 207  VAL A C     1 
ATOM   1615 O  O     . VAL A 1 207 ? 9.608   -22.292 7.419   1.00 40.94  ? 207  VAL A O     1 
ATOM   1616 C  CB    . VAL A 1 207 ? 12.464  -22.301 8.627   1.00 39.83  ? 207  VAL A CB    1 
ATOM   1617 C  CG1   . VAL A 1 207 ? 12.095  -22.329 10.097  1.00 39.14  ? 207  VAL A CG1   1 
ATOM   1618 C  CG2   . VAL A 1 207 ? 13.960  -22.512 8.423   1.00 38.18  ? 207  VAL A CG2   1 
ATOM   1619 N  N     . ASN A 1 208 ? 9.564   -24.133 8.736   1.00 39.08  ? 208  ASN A N     1 
ATOM   1620 C  CA    . ASN A 1 208 ? 8.128   -24.124 9.009   1.00 37.15  ? 208  ASN A CA    1 
ATOM   1621 C  C     . ASN A 1 208 ? 7.281   -24.187 7.740   1.00 33.62  ? 208  ASN A C     1 
ATOM   1622 O  O     . ASN A 1 208 ? 6.166   -23.665 7.713   1.00 35.20  ? 208  ASN A O     1 
ATOM   1623 C  CB    . ASN A 1 208 ? 7.727   -22.913 9.853   1.00 34.96  ? 208  ASN A CB    1 
ATOM   1624 C  CG    . ASN A 1 208 ? 6.984   -23.314 11.099  1.00 39.91  ? 208  ASN A CG    1 
ATOM   1625 O  OD1   . ASN A 1 208 ? 7.254   -22.799 12.184  1.00 53.59  ? 208  ASN A OD1   1 
ATOM   1626 N  ND2   . ASN A 1 208 ? 6.054   -24.268 10.964  1.00 47.60  ? 208  ASN A ND2   1 
ATOM   1627 N  N     . ASN A 1 209 ? 7.786   -24.868 6.706   1.00 36.94  ? 209  ASN A N     1 
ATOM   1628 C  CA    . ASN A 1 209 ? 7.137   -24.943 5.388   1.00 35.26  ? 209  ASN A CA    1 
ATOM   1629 C  C     . ASN A 1 209 ? 6.723   -23.571 4.872   1.00 36.62  ? 209  ASN A C     1 
ATOM   1630 O  O     . ASN A 1 209 ? 5.688   -23.435 4.218   1.00 32.37  ? 209  ASN A O     1 
ATOM   1631 C  CB    . ASN A 1 209 ? 5.924   -25.869 5.398   1.00 40.15  ? 209  ASN A CB    1 
ATOM   1632 C  CG    . ASN A 1 209 ? 6.298   -27.295 5.656   1.00 47.90  ? 209  ASN A CG    1 
ATOM   1633 O  OD1   . ASN A 1 209 ? 7.253   -27.810 5.074   1.00 54.11  ? 209  ASN A OD1   1 
ATOM   1634 N  ND2   . ASN A 1 209 ? 5.559   -27.948 6.547   1.00 55.46  ? 209  ASN A ND2   1 
ATOM   1635 N  N     . TRP A 1 210 ? 7.533   -22.553 5.152   1.00 26.23  ? 210  TRP A N     1 
ATOM   1636 C  CA    . TRP A 1 210 ? 7.205   -21.174 4.806   1.00 25.37  ? 210  TRP A CA    1 
ATOM   1637 C  C     . TRP A 1 210 ? 8.259   -20.641 3.840   1.00 29.41  ? 210  TRP A C     1 
ATOM   1638 O  O     . TRP A 1 210 ? 9.372   -20.295 4.249   1.00 27.48  ? 210  TRP A O     1 
ATOM   1639 C  CB    . TRP A 1 210 ? 7.127   -20.318 6.060   1.00 27.98  ? 210  TRP A CB    1 
ATOM   1640 C  CG    . TRP A 1 210 ? 6.793   -18.890 5.786   1.00 24.63  ? 210  TRP A CG    1 
ATOM   1641 C  CD1   . TRP A 1 210 ? 7.669   -17.847 5.615   1.00 25.66  ? 210  TRP A CD1   1 
ATOM   1642 C  CD2   . TRP A 1 210 ? 5.484   -18.351 5.644   1.00 25.72  ? 210  TRP A CD2   1 
ATOM   1643 N  NE1   . TRP A 1 210 ? 6.970   -16.674 5.388   1.00 25.93  ? 210  TRP A NE1   1 
ATOM   1644 C  CE2   . TRP A 1 210 ? 5.625   -16.962 5.401   1.00 26.42  ? 210  TRP A CE2   1 
ATOM   1645 C  CE3   . TRP A 1 210 ? 4.193   -18.909 5.708   1.00 27.58  ? 210  TRP A CE3   1 
ATOM   1646 C  CZ2   . TRP A 1 210 ? 4.526   -16.117 5.235   1.00 27.74  ? 210  TRP A CZ2   1 
ATOM   1647 C  CZ3   . TRP A 1 210 ? 3.096   -18.064 5.539   1.00 25.61  ? 210  TRP A CZ3   1 
ATOM   1648 C  CH2   . TRP A 1 210 ? 3.272   -16.686 5.298   1.00 27.01  ? 210  TRP A CH2   1 
ATOM   1649 N  N     . ALA A 1 211 ? 7.905   -20.544 2.564   1.00 27.00  ? 211  ALA A N     1 
ATOM   1650 C  CA    . ALA A 1 211 ? 8.861   -20.085 1.563   1.00 24.30  ? 211  ALA A CA    1 
ATOM   1651 C  C     . ALA A 1 211 ? 9.104   -18.582 1.692   1.00 27.27  ? 211  ALA A C     1 
ATOM   1652 O  O     . ALA A 1 211 ? 8.160   -17.775 1.754   1.00 25.48  ? 211  ALA A O     1 
ATOM   1653 C  CB    . ALA A 1 211 ? 8.365   -20.423 0.165   1.00 30.02  ? 211  ALA A CB    1 
ATOM   1654 N  N     . CYS A 1 212 ? 10.378  -18.209 1.737   1.00 28.12  ? 212  CYS A N     1 
ATOM   1655 C  CA    . CYS A 1 212 ? 10.764  -16.806 1.845   1.00 29.83  ? 212  CYS A CA    1 
ATOM   1656 C  C     . CYS A 1 212 ? 12.255  -16.711 1.553   1.00 30.22  ? 212  CYS A C     1 
ATOM   1657 O  O     . CYS A 1 212 ? 12.983  -17.706 1.621   1.00 30.17  ? 212  CYS A O     1 
ATOM   1658 C  CB    . CYS A 1 212 ? 10.427  -16.237 3.228   1.00 28.49  ? 212  CYS A CB    1 
ATOM   1659 S  SG    . CYS A 1 212 ? 11.400  -16.934 4.588   1.00 28.89  ? 212  CYS A SG    1 
ATOM   1660 N  N     . ASN A 1 213 ? 12.700  -15.510 1.199   1.00 30.61  ? 213  ASN A N     1 
ATOM   1661 C  CA    . ASN A 1 213 ? 14.109  -15.257 0.892   1.00 33.26  ? 213  ASN A CA    1 
ATOM   1662 C  C     . ASN A 1 213 ? 14.504  -13.988 1.631   1.00 30.88  ? 213  ASN A C     1 
ATOM   1663 O  O     . ASN A 1 213 ? 14.517  -12.896 1.048   1.00 33.27  ? 213  ASN A O     1 
ATOM   1664 C  CB    . ASN A 1 213 ? 14.347  -15.153 -0.618  1.00 29.40  ? 213  ASN A CB    1 
ATOM   1665 C  CG    . ASN A 1 213 ? 15.825  -15.160 -0.982  1.00 34.62  ? 213  ASN A CG    1 
ATOM   1666 O  OD1   . ASN A 1 213 ? 16.669  -14.722 -0.201  1.00 34.43  ? 213  ASN A OD1   1 
ATOM   1667 N  ND2   . ASN A 1 213 ? 16.142  -15.670 -2.168  1.00 29.33  ? 213  ASN A ND2   1 
ATOM   1668 N  N     . PRO A 1 214 ? 14.822  -14.095 2.928   1.00 30.90  ? 214  PRO A N     1 
ATOM   1669 C  CA    . PRO A 1 214 ? 15.066  -12.880 3.730   1.00 32.32  ? 214  PRO A CA    1 
ATOM   1670 C  C     . PRO A 1 214 ? 16.240  -12.046 3.257   1.00 34.76  ? 214  PRO A C     1 
ATOM   1671 O  O     . PRO A 1 214 ? 16.204  -10.811 3.375   1.00 36.06  ? 214  PRO A O     1 
ATOM   1672 C  CB    . PRO A 1 214 ? 15.315  -13.438 5.137   1.00 36.23  ? 214  PRO A CB    1 
ATOM   1673 C  CG    . PRO A 1 214 ? 14.631  -14.756 5.138   1.00 32.73  ? 214  PRO A CG    1 
ATOM   1674 C  CD    . PRO A 1 214 ? 14.819  -15.306 3.760   1.00 37.16  ? 214  PRO A CD    1 
ATOM   1675 N  N     . GLU A 1 215 ? 17.279  -12.691 2.728   1.00 31.93  ? 215  GLU A N     1 
ATOM   1676 C  CA    . GLU A 1 215 ? 18.469  -11.976 2.286   1.00 36.21  ? 215  GLU A CA    1 
ATOM   1677 C  C     . GLU A 1 215 ? 18.164  -11.040 1.124   1.00 36.79  ? 215  GLU A C     1 
ATOM   1678 O  O     . GLU A 1 215 ? 18.768  -9.967  1.009   1.00 36.93  ? 215  GLU A O     1 
ATOM   1679 C  CB    . GLU A 1 215 ? 19.549  -12.984 1.886   1.00 39.75  ? 215  GLU A CB    1 
ATOM   1680 C  CG    . GLU A 1 215 ? 20.044  -13.880 3.027   1.00 51.48  ? 215  GLU A CG    1 
ATOM   1681 C  CD    . GLU A 1 215 ? 19.131  -15.085 3.330   1.00 58.13  ? 215  GLU A CD    1 
ATOM   1682 O  OE1   . GLU A 1 215 ? 18.060  -15.248 2.685   1.00 46.73  ? 215  GLU A OE1   1 
ATOM   1683 O  OE2   . GLU A 1 215 ? 19.500  -15.877 4.231   1.00 64.97  ? 215  GLU A OE2   1 
ATOM   1684 N  N     . LEU A 1 216 ? 17.243  -11.434 0.244   1.00 30.71  ? 216  LEU A N     1 
ATOM   1685 C  CA    . LEU A 1 216 ? 16.959  -10.696 -0.978  1.00 22.51  ? 216  LEU A CA    1 
ATOM   1686 C  C     . LEU A 1 216 ? 15.637  -9.951  -0.914  1.00 25.39  ? 216  LEU A C     1 
ATOM   1687 O  O     . LEU A 1 216 ? 15.159  -9.477  -1.948  1.00 30.12  ? 216  LEU A O     1 
ATOM   1688 C  CB    . LEU A 1 216 ? 16.967  -11.637 -2.185  1.00 27.31  ? 216  LEU A CB    1 
ATOM   1689 C  CG    . LEU A 1 216 ? 18.313  -12.263 -2.560  1.00 32.76  ? 216  LEU A CG    1 
ATOM   1690 C  CD1   . LEU A 1 216 ? 18.163  -13.202 -3.746  1.00 32.03  ? 216  LEU A CD1   1 
ATOM   1691 C  CD2   . LEU A 1 216 ? 19.342  -11.187 -2.866  1.00 34.01  ? 216  LEU A CD2   1 
ATOM   1692 N  N     . THR A 1 217 ? 15.037  -9.840  0.276   1.00 27.18  ? 217  THR A N     1 
ATOM   1693 C  CA    . THR A 1 217 ? 13.747  -9.167  0.399   1.00 27.11  ? 217  THR A CA    1 
ATOM   1694 C  C     . THR A 1 217 ? 13.848  -7.715  -0.061  1.00 31.92  ? 217  THR A C     1 
ATOM   1695 O  O     . THR A 1 217 ? 14.737  -6.968  0.368   1.00 23.97  ? 217  THR A O     1 
ATOM   1696 C  CB    . THR A 1 217 ? 13.236  -9.240  1.840   1.00 30.97  ? 217  THR A CB    1 
ATOM   1697 O  OG1   . THR A 1 217 ? 12.861  -10.592 2.141   1.00 27.37  ? 217  THR A OG1   1 
ATOM   1698 C  CG2   . THR A 1 217 ? 12.024  -8.309  2.042   1.00 30.79  ? 217  THR A CG2   1 
ATOM   1699 N  N     . LEU A 1 218 ? 12.925  -7.327  -0.942  1.00 23.69  ? 218  LEU A N     1 
ATOM   1700 C  CA    . LEU A 1 218 ? 12.866  -5.983  -1.479  1.00 22.62  ? 218  LEU A CA    1 
ATOM   1701 C  C     . LEU A 1 218 ? 11.428  -5.722  -1.877  1.00 22.36  ? 218  LEU A C     1 
ATOM   1702 O  O     . LEU A 1 218 ? 10.867  -6.514  -2.639  1.00 19.95  ? 218  LEU A O     1 
ATOM   1703 C  CB    . LEU A 1 218 ? 13.800  -5.850  -2.687  1.00 24.71  ? 218  LEU A CB    1 
ATOM   1704 C  CG    . LEU A 1 218 ? 13.964  -4.449  -3.273  1.00 23.94  ? 218  LEU A CG    1 
ATOM   1705 C  CD1   . LEU A 1 218 ? 14.572  -3.500  -2.255  1.00 24.16  ? 218  LEU A CD1   1 
ATOM   1706 C  CD2   . LEU A 1 218 ? 14.825  -4.541  -4.534  1.00 28.94  ? 218  LEU A CD2   1 
ATOM   1707 N  N     . ILE A 1 219 ? 10.826  -4.655  -1.332  1.00 22.20  ? 219  ILE A N     1 
ATOM   1708 C  CA    . ILE A 1 219 ? 9.461   -4.248  -1.664  1.00 19.72  ? 219  ILE A CA    1 
ATOM   1709 C  C     . ILE A 1 219 ? 9.539   -2.898  -2.375  1.00 21.50  ? 219  ILE A C     1 
ATOM   1710 O  O     . ILE A 1 219 ? 9.817   -1.882  -1.730  1.00 25.86  ? 219  ILE A O     1 
ATOM   1711 C  CB    . ILE A 1 219 ? 8.569   -4.152  -0.412  1.00 19.12  ? 219  ILE A CB    1 
ATOM   1712 C  CG1   . ILE A 1 219 ? 8.600   -5.464  0.387   1.00 23.09  ? 219  ILE A CG1   1 
ATOM   1713 C  CG2   . ILE A 1 219 ? 7.172   -3.814  -0.847  1.00 17.52  ? 219  ILE A CG2   1 
ATOM   1714 C  CD1   . ILE A 1 219 ? 9.694   -5.519  1.470   1.00 23.49  ? 219  ILE A CD1   1 
ATOM   1715 N  N     . ALA A 1 220 ? 9.254   -2.861  -3.686  1.00 19.49  ? 220  ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 220 ? 9.521   -1.669  -4.496  1.00 21.51  ? 220  ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 220 ? 8.246   -1.084  -5.104  1.00 21.98  ? 220  ALA A C     1 
ATOM   1718 O  O     . ALA A 1 220 ? 7.303   -1.813  -5.440  1.00 22.02  ? 220  ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 220 ? 10.528  -1.998  -5.624  1.00 21.21  ? 220  ALA A CB    1 
ATOM   1720 N  N     . HIS A 1 221 ? 8.211   0.247   -5.221  1.00 19.46  ? 221  HIS A N     1 
ATOM   1721 C  CA    . HIS A 1 221 ? 7.071   0.957   -5.782  1.00 16.29  ? 221  HIS A CA    1 
ATOM   1722 C  C     . HIS A 1 221 ? 7.556   1.857   -6.907  1.00 21.05  ? 221  HIS A C     1 
ATOM   1723 O  O     . HIS A 1 221 ? 8.551   2.570   -6.743  1.00 23.60  ? 221  HIS A O     1 
ATOM   1724 C  CB    . HIS A 1 221 ? 6.352   1.786   -4.710  1.00 18.64  ? 221  HIS A CB    1 
ATOM   1725 C  CG    . HIS A 1 221 ? 6.017   0.995   -3.482  1.00 20.36  ? 221  HIS A CG    1 
ATOM   1726 N  ND1   . HIS A 1 221 ? 6.974   0.610   -2.559  1.00 19.61  ? 221  HIS A ND1   1 
ATOM   1727 C  CD2   . HIS A 1 221 ? 4.843   0.465   -3.057  1.00 20.16  ? 221  HIS A CD2   1 
ATOM   1728 C  CE1   . HIS A 1 221 ? 6.388   -0.095  -1.598  1.00 22.72  ? 221  HIS A CE1   1 
ATOM   1729 N  NE2   . HIS A 1 221 ? 5.100   -0.206  -1.883  1.00 21.05  ? 221  HIS A NE2   1 
ATOM   1730 N  N     . LEU A 1 222 ? 6.842   1.841   -8.038  1.00 21.94  ? 222  LEU A N     1 
ATOM   1731 C  CA    . LEU A 1 222 ? 7.182   2.651   -9.213  1.00 23.77  ? 222  LEU A CA    1 
ATOM   1732 C  C     . LEU A 1 222 ? 5.927   3.406   -9.643  1.00 22.54  ? 222  LEU A C     1 
ATOM   1733 O  O     . LEU A 1 222 ? 5.223   2.995   -10.580 1.00 24.87  ? 222  LEU A O     1 
ATOM   1734 C  CB    . LEU A 1 222 ? 7.752   1.778   -10.337 1.00 26.65  ? 222  LEU A CB    1 
ATOM   1735 C  CG    . LEU A 1 222 ? 9.027   0.971   -10.018 1.00 24.85  ? 222  LEU A CG    1 
ATOM   1736 C  CD1   . LEU A 1 222 ? 8.731   -0.416  -9.458  1.00 27.91  ? 222  LEU A CD1   1 
ATOM   1737 C  CD2   . LEU A 1 222 ? 9.907   0.880   -11.246 1.00 34.11  ? 222  LEU A CD2   1 
ATOM   1738 N  N     . PRO A 1 223 ? 5.617   4.518   -8.970  1.00 26.31  ? 223  PRO A N     1 
ATOM   1739 C  CA    . PRO A 1 223 ? 4.338   5.208   -9.219  1.00 27.89  ? 223  PRO A CA    1 
ATOM   1740 C  C     . PRO A 1 223 ? 4.135   5.683   -10.644 1.00 28.19  ? 223  PRO A C     1 
ATOM   1741 O  O     . PRO A 1 223 ? 2.988   5.728   -11.101 1.00 30.54  ? 223  PRO A O     1 
ATOM   1742 C  CB    . PRO A 1 223 ? 4.377   6.400   -8.244  1.00 28.74  ? 223  PRO A CB    1 
ATOM   1743 C  CG    . PRO A 1 223 ? 5.768   6.451   -7.686  1.00 27.84  ? 223  PRO A CG    1 
ATOM   1744 C  CD    . PRO A 1 223 ? 6.366   5.099   -7.838  1.00 24.02  ? 223  PRO A CD    1 
ATOM   1745 N  N     . ASP A 1 224 ? 5.200   6.052   -11.362 1.00 31.66  ? 224  ASP A N     1 
ATOM   1746 C  CA    . ASP A 1 224 ? 5.029   6.521   -12.730 1.00 36.23  ? 224  ASP A CA    1 
ATOM   1747 C  C     . ASP A 1 224 ? 4.610   5.401   -13.665 1.00 37.96  ? 224  ASP A C     1 
ATOM   1748 O  O     . ASP A 1 224 ? 3.870   5.647   -14.625 1.00 37.64  ? 224  ASP A O     1 
ATOM   1749 C  CB    . ASP A 1 224 ? 6.320   7.162   -13.225 1.00 42.25  ? 224  ASP A CB    1 
ATOM   1750 C  CG    . ASP A 1 224 ? 6.715   8.346   -12.392 1.00 49.94  ? 224  ASP A CG    1 
ATOM   1751 O  OD1   . ASP A 1 224 ? 5.833   9.179   -12.095 1.00 45.62  ? 224  ASP A OD1   1 
ATOM   1752 O  OD2   . ASP A 1 224 ? 7.902   8.437   -12.013 1.00 60.20  ? 224  ASP A OD2   1 
ATOM   1753 N  N     . ARG A 1 225 ? 5.075   4.175   -13.409 1.00 29.67  ? 225  ARG A N     1 
ATOM   1754 C  CA    . ARG A 1 225 ? 4.665   3.006   -14.170 1.00 31.23  ? 225  ARG A CA    1 
ATOM   1755 C  C     . ARG A 1 225 ? 3.432   2.325   -13.584 1.00 30.51  ? 225  ARG A C     1 
ATOM   1756 O  O     . ARG A 1 225 ? 2.971   1.322   -14.145 1.00 29.14  ? 225  ARG A O     1 
ATOM   1757 C  CB    . ARG A 1 225 ? 5.811   1.995   -14.244 1.00 35.78  ? 225  ARG A CB    1 
ATOM   1758 C  CG    . ARG A 1 225 ? 7.050   2.538   -14.916 1.00 41.52  ? 225  ARG A CG    1 
ATOM   1759 C  CD    . ARG A 1 225 ? 8.135   1.494   -14.980 1.00 44.25  ? 225  ARG A CD    1 
ATOM   1760 N  NE    . ARG A 1 225 ? 9.253   1.975   -15.779 1.00 63.71  ? 225  ARG A NE    1 
ATOM   1761 C  CZ    . ARG A 1 225 ? 10.311  1.245   -16.096 1.00 70.01  ? 225  ARG A CZ    1 
ATOM   1762 N  NH1   . ARG A 1 225 ? 10.439  -0.004  -15.669 1.00 76.74  ? 225  ARG A NH1   1 
ATOM   1763 N  NH2   . ARG A 1 225 ? 11.263  1.780   -16.863 1.00 67.62  ? 225  ARG A NH2   1 
ATOM   1764 N  N     . ARG A 1 226 ? 2.906   2.838   -12.474 1.00 25.61  ? 226  ARG A N     1 
ATOM   1765 C  CA    . ARG A 1 226 ? 1.814   2.186   -11.758 1.00 28.23  ? 226  ARG A CA    1 
ATOM   1766 C  C     . ARG A 1 226 ? 2.143   0.724   -11.462 1.00 28.17  ? 226  ARG A C     1 
ATOM   1767 O  O     . ARG A 1 226 ? 1.318   -0.167  -11.676 1.00 30.59  ? 226  ARG A O     1 
ATOM   1768 C  CB    . ARG A 1 226 ? 0.506   2.286   -12.547 1.00 30.43  ? 226  ARG A CB    1 
ATOM   1769 C  CG    . ARG A 1 226 ? 0.219   3.659   -13.142 1.00 41.46  ? 226  ARG A CG    1 
ATOM   1770 C  CD    . ARG A 1 226 ? -0.424  4.570   -12.130 1.00 38.32  ? 226  ARG A CD    1 
ATOM   1771 N  NE    . ARG A 1 226 ? -0.915  5.808   -12.741 1.00 48.41  ? 226  ARG A NE    1 
ATOM   1772 C  CZ    . ARG A 1 226 ? -0.451  7.020   -12.464 1.00 46.53  ? 226  ARG A CZ    1 
ATOM   1773 N  NH1   . ARG A 1 226 ? 0.551   7.202   -11.618 1.00 42.72  ? 226  ARG A NH1   1 
ATOM   1774 N  NH2   . ARG A 1 226 ? -1.022  8.081   -13.031 1.00 48.31  ? 226  ARG A NH2   1 
ATOM   1775 N  N     . GLU A 1 227 ? 3.355   0.463   -10.969 1.00 24.84  ? 227  GLU A N     1 
ATOM   1776 C  CA    . GLU A 1 227 ? 3.807   -0.903  -10.694 1.00 24.95  ? 227  GLU A CA    1 
ATOM   1777 C  C     . GLU A 1 227 ? 4.257   -1.051  -9.252  1.00 20.84  ? 227  GLU A C     1 
ATOM   1778 O  O     . GLU A 1 227 ? 4.901   -0.160  -8.699  1.00 24.22  ? 227  GLU A O     1 
ATOM   1779 C  CB    . GLU A 1 227 ? 4.977   -1.339  -11.609 1.00 26.92  ? 227  GLU A CB    1 
ATOM   1780 C  CG    . GLU A 1 227 ? 4.604   -1.462  -13.056 1.00 33.99  ? 227  GLU A CG    1 
ATOM   1781 C  CD    . GLU A 1 227 ? 5.788   -1.797  -13.960 1.00 38.48  ? 227  GLU A CD    1 
ATOM   1782 O  OE1   . GLU A 1 227 ? 6.869   -2.174  -13.457 1.00 35.22  ? 227  GLU A OE1   1 
ATOM   1783 O  OE2   . GLU A 1 227 ? 5.614   -1.664  -15.185 1.00 35.35  ? 227  GLU A OE2   1 
ATOM   1784 N  N     . ILE A 1 228 ? 3.904   -2.181  -8.646  1.00 18.13  ? 228  ILE A N     1 
ATOM   1785 C  CA    . ILE A 1 228 ? 4.417   -2.604  -7.345  1.00 18.41  ? 228  ILE A CA    1 
ATOM   1786 C  C     . ILE A 1 228 ? 5.134   -3.932  -7.553  1.00 16.78  ? 228  ILE A C     1 
ATOM   1787 O  O     . ILE A 1 228 ? 4.588   -4.827  -8.197  1.00 16.33  ? 228  ILE A O     1 
ATOM   1788 C  CB    . ILE A 1 228 ? 3.276   -2.775  -6.325  1.00 14.76  ? 228  ILE A CB    1 
ATOM   1789 C  CG1   . ILE A 1 228 ? 2.548   -1.426  -6.106  1.00 21.05  ? 228  ILE A CG1   1 
ATOM   1790 C  CG2   . ILE A 1 228 ? 3.829   -3.333  -5.042  1.00 16.85  ? 228  ILE A CG2   1 
ATOM   1791 C  CD1   . ILE A 1 228 ? 1.239   -1.601  -5.380  1.00 18.18  ? 228  ILE A CD1   1 
ATOM   1792 N  N     . ILE A 1 229 ? 6.346   -4.072  -7.011  1.00 15.19  ? 229  ILE A N     1 
ATOM   1793 C  CA    . ILE A 1 229 ? 7.180   -5.234  -7.318  1.00 17.28  ? 229  ILE A CA    1 
ATOM   1794 C  C     . ILE A 1 229 ? 7.813   -5.662  -6.006  1.00 19.22  ? 229  ILE A C     1 
ATOM   1795 O  O     . ILE A 1 229 ? 8.594   -4.906  -5.426  1.00 20.66  ? 229  ILE A O     1 
ATOM   1796 C  CB    . ILE A 1 229 ? 8.261   -4.927  -8.384  1.00 15.65  ? 229  ILE A CB    1 
ATOM   1797 C  CG1   . ILE A 1 229 ? 7.609   -4.573  -9.724  1.00 21.99  ? 229  ILE A CG1   1 
ATOM   1798 C  CG2   . ILE A 1 229 ? 9.180   -6.152  -8.587  1.00 18.43  ? 229  ILE A CG2   1 
ATOM   1799 C  CD1   . ILE A 1 229 ? 8.588   -4.090  -10.841 1.00 19.58  ? 229  ILE A CD1   1 
ATOM   1800 N  N     . SER A 1 230 ? 7.452   -6.853  -5.513  1.00 16.99  ? 230  SER A N     1 
ATOM   1801 C  CA    . SER A 1 230 ? 7.842   -7.272  -4.174  1.00 19.89  ? 230  SER A CA    1 
ATOM   1802 C  C     . SER A 1 230 ? 8.385   -8.697  -4.211  1.00 21.47  ? 230  SER A C     1 
ATOM   1803 O  O     . SER A 1 230 ? 7.812   -9.575  -4.853  1.00 19.22  ? 230  SER A O     1 
ATOM   1804 C  CB    . SER A 1 230 ? 6.651   -7.158  -3.191  1.00 22.37  ? 230  SER A CB    1 
ATOM   1805 O  OG    . SER A 1 230 ? 6.967   -7.774  -1.967  1.00 22.24  ? 230  SER A OG    1 
ATOM   1806 N  N     . PHE A 1 231 ? 9.485   -8.928  -3.498  1.00 18.81  ? 231  PHE A N     1 
ATOM   1807 C  CA    . PHE A 1 231 ? 10.270  -10.153 -3.614  1.00 18.23  ? 231  PHE A CA    1 
ATOM   1808 C  C     . PHE A 1 231 ? 10.731  -10.581 -2.239  1.00 23.38  ? 231  PHE A C     1 
ATOM   1809 O  O     . PHE A 1 231 ? 11.285  -9.764  -1.501  1.00 26.17  ? 231  PHE A O     1 
ATOM   1810 C  CB    . PHE A 1 231 ? 11.497  -9.923  -4.515  1.00 21.53  ? 231  PHE A CB    1 
ATOM   1811 C  CG    . PHE A 1 231 ? 12.314  -11.155 -4.779  1.00 23.35  ? 231  PHE A CG    1 
ATOM   1812 C  CD1   . PHE A 1 231 ? 13.334  -11.532 -3.919  1.00 25.56  ? 231  PHE A CD1   1 
ATOM   1813 C  CD2   . PHE A 1 231 ? 12.074  -11.927 -5.896  1.00 22.86  ? 231  PHE A CD2   1 
ATOM   1814 C  CE1   . PHE A 1 231 ? 14.097  -12.683 -4.177  1.00 23.21  ? 231  PHE A CE1   1 
ATOM   1815 C  CE2   . PHE A 1 231 ? 12.833  -13.095 -6.155  1.00 23.47  ? 231  PHE A CE2   1 
ATOM   1816 C  CZ    . PHE A 1 231 ? 13.844  -13.449 -5.288  1.00 22.85  ? 231  PHE A CZ    1 
ATOM   1817 N  N     . GLY A 1 232 ? 10.498  -11.850 -1.884  1.00 18.33  ? 232  GLY A N     1 
ATOM   1818 C  CA    . GLY A 1 232 ? 11.238  -12.485 -0.812  1.00 24.62  ? 232  GLY A CA    1 
ATOM   1819 C  C     . GLY A 1 232 ? 10.499  -12.638 0.508   1.00 27.99  ? 232  GLY A C     1 
ATOM   1820 O  O     . GLY A 1 232 ? 10.946  -13.421 1.357   1.00 25.54  ? 232  GLY A O     1 
ATOM   1821 N  N     . SER A 1 233 ? 9.391   -11.923 0.709   1.00 25.56  ? 233  SER A N     1 
ATOM   1822 C  CA    . SER A 1 233 ? 8.586   -12.054 1.922   1.00 21.85  ? 233  SER A CA    1 
ATOM   1823 C  C     . SER A 1 233 ? 7.198   -12.537 1.541   1.00 24.92  ? 233  SER A C     1 
ATOM   1824 O  O     . SER A 1 233 ? 6.634   -12.077 0.541   1.00 21.90  ? 233  SER A O     1 
ATOM   1825 C  CB    . SER A 1 233 ? 8.445   -10.715 2.687   1.00 26.59  ? 233  SER A CB    1 
ATOM   1826 O  OG    . SER A 1 233 ? 7.481   -10.868 3.757   1.00 21.90  ? 233  SER A OG    1 
ATOM   1827 N  N     . GLY A 1 234 ? 6.653   -13.467 2.332   1.00 26.48  ? 234  GLY A N     1 
ATOM   1828 C  CA    . GLY A 1 234 ? 5.264   -13.848 2.215   1.00 22.32  ? 234  GLY A CA    1 
ATOM   1829 C  C     . GLY A 1 234 ? 4.305   -13.151 3.159   1.00 28.48  ? 234  GLY A C     1 
ATOM   1830 O  O     . GLY A 1 234 ? 3.106   -13.450 3.117   1.00 26.09  ? 234  GLY A O     1 
ATOM   1831 N  N     . TYR A 1 235 ? 4.781   -12.197 3.967   1.00 26.73  ? 235  TYR A N     1 
ATOM   1832 C  CA    . TYR A 1 235 ? 4.080   -11.706 5.145   1.00 26.89  ? 235  TYR A CA    1 
ATOM   1833 C  C     . TYR A 1 235 ? 3.329   -10.413 4.881   1.00 25.65  ? 235  TYR A C     1 
ATOM   1834 O  O     . TYR A 1 235 ? 3.913   -9.450  4.354   1.00 22.44  ? 235  TYR A O     1 
ATOM   1835 C  CB    . TYR A 1 235 ? 5.046   -11.446 6.306   1.00 26.47  ? 235  TYR A CB    1 
ATOM   1836 C  CG    . TYR A 1 235 ? 4.282   -11.434 7.609   1.00 25.85  ? 235  TYR A CG    1 
ATOM   1837 C  CD1   . TYR A 1 235 ? 3.985   -12.638 8.241   1.00 22.41  ? 235  TYR A CD1   1 
ATOM   1838 C  CD2   . TYR A 1 235 ? 3.791   -10.243 8.170   1.00 28.73  ? 235  TYR A CD2   1 
ATOM   1839 C  CE1   . TYR A 1 235 ? 3.263   -12.671 9.423   1.00 27.70  ? 235  TYR A CE1   1 
ATOM   1840 C  CE2   . TYR A 1 235 ? 3.043   -10.264 9.369   1.00 26.28  ? 235  TYR A CE2   1 
ATOM   1841 C  CZ    . TYR A 1 235 ? 2.793   -11.496 9.985   1.00 25.97  ? 235  TYR A CZ    1 
ATOM   1842 O  OH    . TYR A 1 235 ? 2.058   -11.597 11.163  1.00 30.58  ? 235  TYR A OH    1 
ATOM   1843 N  N     . GLY A 1 236 ? 2.053   -10.384 5.301   1.00 17.85  ? 236  GLY A N     1 
ATOM   1844 C  CA    . GLY A 1 236 ? 1.241   -9.176  5.437   1.00 20.54  ? 236  GLY A CA    1 
ATOM   1845 C  C     . GLY A 1 236 ? 1.487   -8.061  4.432   1.00 21.99  ? 236  GLY A C     1 
ATOM   1846 O  O     . GLY A 1 236 ? 1.338   -8.263  3.227   1.00 24.80  ? 236  GLY A O     1 
ATOM   1847 N  N     . GLY A 1 237 ? 1.877   -6.886  4.920   1.00 18.12  ? 237  GLY A N     1 
ATOM   1848 C  CA    . GLY A 1 237 ? 2.060   -5.737  4.058   1.00 20.06  ? 237  GLY A CA    1 
ATOM   1849 C  C     . GLY A 1 237 ? 3.132   -5.900  2.995   1.00 20.48  ? 237  GLY A C     1 
ATOM   1850 O  O     . GLY A 1 237 ? 3.197   -5.079  2.065   1.00 23.06  ? 237  GLY A O     1 
ATOM   1851 N  N     . ASN A 1 238 ? 4.008   -6.900  3.127   1.00 20.12  ? 238  ASN A N     1 
ATOM   1852 C  CA    . ASN A 1 238 ? 4.994   -7.153  2.076   1.00 19.98  ? 238  ASN A CA    1 
ATOM   1853 C  C     . ASN A 1 238 ? 4.415   -7.888  0.870   1.00 23.87  ? 238  ASN A C     1 
ATOM   1854 O  O     . ASN A 1 238 ? 4.953   -7.753  -0.233  1.00 22.33  ? 238  ASN A O     1 
ATOM   1855 C  CB    . ASN A 1 238 ? 6.162   -7.991  2.592   1.00 22.53  ? 238  ASN A CB    1 
ATOM   1856 C  CG    . ASN A 1 238 ? 6.883   -7.347  3.723   1.00 23.53  ? 238  ASN A CG    1 
ATOM   1857 O  OD1   . ASN A 1 238 ? 6.975   -6.117  3.801   1.00 23.25  ? 238  ASN A OD1   1 
ATOM   1858 N  ND2   . ASN A 1 238 ? 7.433   -8.168  4.604   1.00 23.32  ? 238  ASN A ND2   1 
ATOM   1859 N  N     . SER A 1 239 ? 3.358   -8.686  1.053   1.00 20.22  ? 239  SER A N     1 
ATOM   1860 C  CA    . SER A 1 239 ? 2.894   -9.629  0.038   1.00 20.56  ? 239  SER A CA    1 
ATOM   1861 C  C     . SER A 1 239 ? 1.460   -9.402  -0.405  1.00 20.14  ? 239  SER A C     1 
ATOM   1862 O  O     . SER A 1 239 ? 1.133   -9.671  -1.563  1.00 18.93  ? 239  SER A O     1 
ATOM   1863 C  CB    . SER A 1 239 ? 3.011   -11.067 0.566   1.00 20.59  ? 239  SER A CB    1 
ATOM   1864 O  OG    . SER A 1 239 ? 2.145   -11.265 1.693   1.00 23.23  ? 239  SER A OG    1 
ATOM   1865 N  N     . LEU A 1 240 ? 0.591   -8.938  0.491   1.00 21.61  ? 240  LEU A N     1 
ATOM   1866 C  CA    . LEU A 1 240 ? -0.776  -8.538  0.149   1.00 21.37  ? 240  LEU A CA    1 
ATOM   1867 C  C     . LEU A 1 240 ? -0.682  -7.148  -0.451  1.00 18.69  ? 240  LEU A C     1 
ATOM   1868 O  O     . LEU A 1 240 ? -0.816  -6.141  0.239   1.00 19.98  ? 240  LEU A O     1 
ATOM   1869 C  CB    . LEU A 1 240 ? -1.675  -8.532  1.390   1.00 24.20  ? 240  LEU A CB    1 
ATOM   1870 C  CG    . LEU A 1 240 ? -1.591  -9.778  2.295   1.00 22.56  ? 240  LEU A CG    1 
ATOM   1871 C  CD1   . LEU A 1 240 ? -2.649  -9.707  3.399   1.00 20.94  ? 240  LEU A CD1   1 
ATOM   1872 C  CD2   . LEU A 1 240 ? -1.749  -11.071 1.521   1.00 22.38  ? 240  LEU A CD2   1 
ATOM   1873 N  N     . LEU A 1 241 ? -0.433  -7.089  -1.761  1.00 17.78  ? 241  LEU A N     1 
ATOM   1874 C  CA    . LEU A 1 241 ? 0.021   -5.824  -2.325  1.00 19.93  ? 241  LEU A CA    1 
ATOM   1875 C  C     . LEU A 1 241 ? -1.087  -4.780  -2.420  1.00 18.44  ? 241  LEU A C     1 
ATOM   1876 O  O     . LEU A 1 241 ? -0.790  -3.605  -2.657  1.00 19.93  ? 241  LEU A O     1 
ATOM   1877 C  CB    . LEU A 1 241 ? 0.671   -6.054  -3.707  1.00 15.21  ? 241  LEU A CB    1 
ATOM   1878 C  CG    . LEU A 1 241 ? 1.941   -6.893  -3.563  1.00 19.66  ? 241  LEU A CG    1 
ATOM   1879 C  CD1   . LEU A 1 241 ? 2.679   -7.062  -4.909  1.00 14.85  ? 241  LEU A CD1   1 
ATOM   1880 C  CD2   . LEU A 1 241 ? 2.867   -6.295  -2.512  1.00 21.38  ? 241  LEU A CD2   1 
ATOM   1881 N  N     . GLY A 1 242 ? -2.351  -5.166  -2.241  1.00 22.47  ? 242  GLY A N     1 
ATOM   1882 C  CA    . GLY A 1 242 ? -3.423  -4.188  -2.261  1.00 22.18  ? 242  GLY A CA    1 
ATOM   1883 C  C     . GLY A 1 242 ? -3.440  -3.276  -1.058  1.00 19.94  ? 242  GLY A C     1 
ATOM   1884 O  O     . GLY A 1 242 ? -3.969  -2.161  -1.135  1.00 29.12  ? 242  GLY A O     1 
ATOM   1885 N  N     . LYS A 1 243 ? -2.823  -3.688  0.025   1.00 21.73  ? 243  LYS A N     1 
ATOM   1886 C  CA    . LYS A 1 243 ? -3.064  -3.043  1.308   1.00 22.53  ? 243  LYS A CA    1 
ATOM   1887 C  C     . LYS A 1 243 ? -2.182  -1.814  1.523   1.00 25.10  ? 243  LYS A C     1 
ATOM   1888 O  O     . LYS A 1 243 ? -2.614  -0.682  1.283   1.00 29.49  ? 243  LYS A O     1 
ATOM   1889 C  CB    . LYS A 1 243 ? -2.839  -4.062  2.420   1.00 21.51  ? 243  LYS A CB    1 
ATOM   1890 C  CG    . LYS A 1 243 ? -3.247  -3.569  3.810   1.00 22.26  ? 243  LYS A CG    1 
ATOM   1891 C  CD    . LYS A 1 243 ? -3.308  -4.737  4.842   1.00 18.41  ? 243  LYS A CD    1 
ATOM   1892 C  CE    . LYS A 1 243 ? -3.690  -4.174  6.227   1.00 23.30  ? 243  LYS A CE    1 
ATOM   1893 N  NZ    . LYS A 1 243 ? -5.008  -3.470  6.208   1.00 22.87  ? 243  LYS A NZ    1 
ATOM   1894 N  N     . LYS A 1 244 ? -0.946  -2.007  1.994   1.00 22.00  ? 244  LYS A N     1 
ATOM   1895 C  CA    . LYS A 1 244 ? -0.100  -0.835  2.191   1.00 14.11  ? 244  LYS A CA    1 
ATOM   1896 C  C     . LYS A 1 244 ? 0.515   -0.361  0.878   1.00 20.70  ? 244  LYS A C     1 
ATOM   1897 O  O     . LYS A 1 244 ? 0.592   0.846   0.625   1.00 16.57  ? 244  LYS A O     1 
ATOM   1898 C  CB    . LYS A 1 244 ? 1.004   -1.135  3.208   1.00 21.18  ? 244  LYS A CB    1 
ATOM   1899 C  CG    . LYS A 1 244 ? 0.499   -1.646  4.538   1.00 21.20  ? 244  LYS A CG    1 
ATOM   1900 C  CD    . LYS A 1 244 ? -0.329  -0.568  5.248   1.00 17.17  ? 244  LYS A CD    1 
ATOM   1901 C  CE    . LYS A 1 244 ? -0.752  -1.005  6.647   1.00 20.47  ? 244  LYS A CE    1 
ATOM   1902 N  NZ    . LYS A 1 244 ? -1.610  0.060   7.266   1.00 17.61  ? 244  LYS A NZ    1 
ATOM   1903 N  N     . CYS A 1 245 ? 0.963   -1.284  0.025   1.00 17.38  ? 245  CYS A N     1 
ATOM   1904 C  CA    . CYS A 1 245 ? 1.723   -0.856  -1.157  1.00 16.27  ? 245  CYS A CA    1 
ATOM   1905 C  C     . CYS A 1 245 ? 0.842   -0.082  -2.123  1.00 17.81  ? 245  CYS A C     1 
ATOM   1906 O  O     . CYS A 1 245 ? 1.187   1.023   -2.553  1.00 18.99  ? 245  CYS A O     1 
ATOM   1907 C  CB    . CYS A 1 245 ? 2.339   -2.081  -1.857  1.00 16.16  ? 245  CYS A CB    1 
ATOM   1908 S  SG    . CYS A 1 245 ? 3.564   -2.904  -0.879  1.00 19.82  ? 245  CYS A SG    1 
ATOM   1909 N  N     . PHE A 1 246 ? -0.317  -0.634  -2.452  1.00 16.15  ? 246  PHE A N     1 
ATOM   1910 C  CA    . PHE A 1 246 ? -1.280  0.022   -3.341  1.00 18.65  ? 246  PHE A CA    1 
ATOM   1911 C  C     . PHE A 1 246 ? -2.083  1.109   -2.605  1.00 20.26  ? 246  PHE A C     1 
ATOM   1912 O  O     . PHE A 1 246 ? -2.063  2.284   -2.980  1.00 22.44  ? 246  PHE A O     1 
ATOM   1913 C  CB    . PHE A 1 246 ? -2.166  -1.100  -3.894  1.00 17.22  ? 246  PHE A CB    1 
ATOM   1914 C  CG    . PHE A 1 246 ? -3.256  -0.711  -4.876  1.00 21.26  ? 246  PHE A CG    1 
ATOM   1915 C  CD1   . PHE A 1 246 ? -3.746  0.568   -5.017  1.00 25.28  ? 246  PHE A CD1   1 
ATOM   1916 C  CD2   . PHE A 1 246 ? -3.833  -1.731  -5.644  1.00 27.11  ? 246  PHE A CD2   1 
ATOM   1917 C  CE1   . PHE A 1 246 ? -4.791  0.840   -5.914  1.00 26.81  ? 246  PHE A CE1   1 
ATOM   1918 C  CE2   . PHE A 1 246 ? -4.853  -1.472  -6.538  1.00 22.50  ? 246  PHE A CE2   1 
ATOM   1919 C  CZ    . PHE A 1 246 ? -5.335  -0.171  -6.672  1.00 27.64  ? 246  PHE A CZ    1 
ATOM   1920 N  N     . ALA A 1 247 ? -2.810  0.725   -1.562  1.00 22.03  ? 247  ALA A N     1 
ATOM   1921 C  CA    . ALA A 1 247 ? -3.835  1.602   -1.000  1.00 22.30  ? 247  ALA A CA    1 
ATOM   1922 C  C     . ALA A 1 247 ? -3.292  2.747   -0.152  1.00 18.97  ? 247  ALA A C     1 
ATOM   1923 O  O     . ALA A 1 247 ? -4.047  3.689   0.113   1.00 23.11  ? 247  ALA A O     1 
ATOM   1924 C  CB    . ALA A 1 247 ? -4.812  0.776   -0.172  1.00 22.52  ? 247  ALA A CB    1 
ATOM   1925 N  N     . LEU A 1 248 ? -2.037  2.693   0.310   1.00 22.63  ? 248  LEU A N     1 
ATOM   1926 C  CA    . LEU A 1 248 ? -1.381  3.887   0.858   1.00 19.42  ? 248  LEU A CA    1 
ATOM   1927 C  C     . LEU A 1 248 ? -0.295  4.450   -0.057  1.00 21.02  ? 248  LEU A C     1 
ATOM   1928 O  O     . LEU A 1 248 ? -0.343  5.636   -0.413  1.00 24.18  ? 248  LEU A O     1 
ATOM   1929 C  CB    . LEU A 1 248 ? -0.797  3.586   2.242   1.00 18.12  ? 248  LEU A CB    1 
ATOM   1930 C  CG    . LEU A 1 248 ? -1.890  3.285   3.297   1.00 18.76  ? 248  LEU A CG    1 
ATOM   1931 C  CD1   . LEU A 1 248 ? -1.217  3.174   4.639   1.00 20.35  ? 248  LEU A CD1   1 
ATOM   1932 C  CD2   . LEU A 1 248 ? -2.917  4.398   3.305   1.00 18.27  ? 248  LEU A CD2   1 
ATOM   1933 N  N     . ARG A 1 249 ? 0.724   3.664   -0.427  1.00 21.98  ? 249  ARG A N     1 
ATOM   1934 C  CA    . ARG A 1 249 ? 1.860   4.279   -1.121  1.00 19.59  ? 249  ARG A CA    1 
ATOM   1935 C  C     . ARG A 1 249 ? 1.500   4.707   -2.540  1.00 21.83  ? 249  ARG A C     1 
ATOM   1936 O  O     . ARG A 1 249 ? 1.639   5.879   -2.904  1.00 23.02  ? 249  ARG A O     1 
ATOM   1937 C  CB    . ARG A 1 249 ? 3.064   3.334   -1.122  1.00 21.99  ? 249  ARG A CB    1 
ATOM   1938 C  CG    . ARG A 1 249 ? 3.592   3.114   0.285   1.00 21.86  ? 249  ARG A CG    1 
ATOM   1939 C  CD    . ARG A 1 249 ? 5.059   2.715   0.341   1.00 22.21  ? 249  ARG A CD    1 
ATOM   1940 N  NE    . ARG A 1 249 ? 5.327   2.135   1.650   1.00 23.73  ? 249  ARG A NE    1 
ATOM   1941 C  CZ    . ARG A 1 249 ? 5.045   0.890   2.024   1.00 23.12  ? 249  ARG A CZ    1 
ATOM   1942 N  NH1   . ARG A 1 249 ? 4.623   -0.031  1.154   1.00 23.87  ? 249  ARG A NH1   1 
ATOM   1943 N  NH2   . ARG A 1 249 ? 5.209   0.547   3.299   1.00 23.45  ? 249  ARG A NH2   1 
ATOM   1944 N  N     . ILE A 1 250 ? 1.064   3.774   -3.380  1.00 24.30  ? 250  ILE A N     1 
ATOM   1945 C  CA    . ILE A 1 250 ? 0.719   4.184   -4.737  1.00 25.60  ? 250  ILE A CA    1 
ATOM   1946 C  C     . ILE A 1 250 ? -0.477  5.132   -4.710  1.00 23.71  ? 250  ILE A C     1 
ATOM   1947 O  O     . ILE A 1 250 ? -0.531  6.114   -5.456  1.00 21.78  ? 250  ILE A O     1 
ATOM   1948 C  CB    . ILE A 1 250 ? 0.454   2.950   -5.618  1.00 22.64  ? 250  ILE A CB    1 
ATOM   1949 C  CG1   . ILE A 1 250 ? 1.759   2.167   -5.844  1.00 17.19  ? 250  ILE A CG1   1 
ATOM   1950 C  CG2   . ILE A 1 250 ? -0.211  3.368   -6.929  1.00 28.60  ? 250  ILE A CG2   1 
ATOM   1951 C  CD1   . ILE A 1 250 ? 2.803   2.944   -6.676  1.00 16.64  ? 250  ILE A CD1   1 
ATOM   1952 N  N     . ALA A 1 251 ? -1.461  4.833   -3.868  1.00 23.37  ? 251  ALA A N     1 
ATOM   1953 C  CA    . ALA A 1 251 ? -2.684  5.623   -3.839  1.00 23.34  ? 251  ALA A CA    1 
ATOM   1954 C  C     . ALA A 1 251 ? -2.445  7.030   -3.321  1.00 17.42  ? 251  ALA A C     1 
ATOM   1955 O  O     . ALA A 1 251 ? -3.163  7.943   -3.719  1.00 19.18  ? 251  ALA A O     1 
ATOM   1956 C  CB    . ALA A 1 251 ? -3.744  4.930   -2.975  1.00 20.33  ? 251  ALA A CB    1 
ATOM   1957 N  N     . SER A 1 252 ? -1.505  7.231   -2.392  1.00 17.19  ? 252  SER A N     1 
ATOM   1958 C  CA    . SER A 1 252 ? -1.345  8.593   -1.893  1.00 16.41  ? 252  SER A CA    1 
ATOM   1959 C  C     . SER A 1 252 ? -0.789  9.486   -2.987  1.00 20.14  ? 252  SER A C     1 
ATOM   1960 O  O     . SER A 1 252 ? -1.151  10.664  -3.072  1.00 20.58  ? 252  SER A O     1 
ATOM   1961 C  CB    . SER A 1 252 ? -0.446  8.650   -0.650  1.00 19.00  ? 252  SER A CB    1 
ATOM   1962 O  OG    . SER A 1 252 ? 0.884   8.253   -0.916  1.00 18.64  ? 252  SER A OG    1 
ATOM   1963 N  N     . ARG A 1 253 ? 0.056   8.921   -3.852  1.00 18.03  ? 253  ARG A N     1 
ATOM   1964 C  CA    . ARG A 1 253 ? 0.543   9.651   -5.011  1.00 19.69  ? 253  ARG A CA    1 
ATOM   1965 C  C     . ARG A 1 253 ? -0.588  9.918   -6.003  1.00 24.29  ? 253  ARG A C     1 
ATOM   1966 O  O     . ARG A 1 253 ? -0.760  11.052  -6.459  1.00 28.30  ? 253  ARG A O     1 
ATOM   1967 C  CB    . ARG A 1 253 ? 1.692   8.856   -5.655  1.00 24.08  ? 253  ARG A CB    1 
ATOM   1968 C  CG    . ARG A 1 253 ? 1.910   9.103   -7.122  1.00 39.77  ? 253  ARG A CG    1 
ATOM   1969 C  CD    . ARG A 1 253 ? 2.707   10.353  -7.360  1.00 33.80  ? 253  ARG A CD    1 
ATOM   1970 N  NE    . ARG A 1 253 ? 3.291   10.294  -8.694  1.00 40.67  ? 253  ARG A NE    1 
ATOM   1971 C  CZ    . ARG A 1 253 ? 4.591   10.252  -8.952  1.00 45.64  ? 253  ARG A CZ    1 
ATOM   1972 N  NH1   . ARG A 1 253 ? 5.497   10.332  -7.985  1.00 41.57  ? 253  ARG A NH1   1 
ATOM   1973 N  NH2   . ARG A 1 253 ? 4.993   10.135  -10.213 1.00 51.71  ? 253  ARG A NH2   1 
ATOM   1974 N  N     . LEU A 1 254 ? -1.394  8.897   -6.327  1.00 26.16  ? 254  LEU A N     1 
ATOM   1975 C  CA    . LEU A 1 254 ? -2.553  9.139   -7.193  1.00 22.09  ? 254  LEU A CA    1 
ATOM   1976 C  C     . LEU A 1 254 ? -3.477  10.190  -6.594  1.00 26.09  ? 254  LEU A C     1 
ATOM   1977 O  O     . LEU A 1 254 ? -4.033  11.021  -7.319  1.00 29.44  ? 254  LEU A O     1 
ATOM   1978 C  CB    . LEU A 1 254 ? -3.338  7.859   -7.431  1.00 25.18  ? 254  LEU A CB    1 
ATOM   1979 C  CG    . LEU A 1 254 ? -2.606  6.675   -8.073  1.00 25.76  ? 254  LEU A CG    1 
ATOM   1980 C  CD1   . LEU A 1 254 ? -3.559  5.521   -8.166  1.00 32.51  ? 254  LEU A CD1   1 
ATOM   1981 C  CD2   . LEU A 1 254 ? -2.088  7.093   -9.424  1.00 32.28  ? 254  LEU A CD2   1 
ATOM   1982 N  N     . ALA A 1 255 ? -3.689  10.129  -5.274  1.00 23.70  ? 255  ALA A N     1 
ATOM   1983 C  CA    . ALA A 1 255 ? -4.556  11.091  -4.594  1.00 26.51  ? 255  ALA A CA    1 
ATOM   1984 C  C     . ALA A 1 255 ? -4.047  12.518  -4.759  1.00 25.06  ? 255  ALA A C     1 
ATOM   1985 O  O     . ALA A 1 255 ? -4.828  13.452  -5.026  1.00 22.55  ? 255  ALA A O     1 
ATOM   1986 C  CB    . ALA A 1 255 ? -4.645  10.725  -3.108  1.00 24.90  ? 255  ALA A CB    1 
ATOM   1987 N  N     . LYS A 1 256 ? -2.742  12.711  -4.551  1.00 27.12  ? 256  LYS A N     1 
ATOM   1988 C  CA    . LYS A 1 256 ? -2.121  14.008  -4.802  1.00 26.28  ? 256  LYS A CA    1 
ATOM   1989 C  C     . LYS A 1 256 ? -2.426  14.497  -6.213  1.00 27.55  ? 256  LYS A C     1 
ATOM   1990 O  O     . LYS A 1 256 ? -2.814  15.654  -6.403  1.00 33.65  ? 256  LYS A O     1 
ATOM   1991 C  CB    . LYS A 1 256 ? -0.610  13.901  -4.591  1.00 25.32  ? 256  LYS A CB    1 
ATOM   1992 C  CG    . LYS A 1 256 ? 0.215   15.097  -5.077  1.00 33.54  ? 256  LYS A CG    1 
ATOM   1993 C  CD    . LYS A 1 256 ? 0.017   16.262  -4.135  1.00 26.68  ? 256  LYS A CD    1 
ATOM   1994 C  CE    . LYS A 1 256 ? 0.800   17.503  -4.608  1.00 42.50  ? 256  LYS A CE    1 
ATOM   1995 N  NZ    . LYS A 1 256 ? 0.223   18.110  -5.845  1.00 44.18  ? 256  LYS A NZ    1 
ATOM   1996 N  N     . GLU A 1 257 ? -2.279  13.621  -7.208  1.00 31.01  ? 257  GLU A N     1 
ATOM   1997 C  CA    . GLU A 1 257 ? -2.478  14.020  -8.599  1.00 31.56  ? 257  GLU A CA    1 
ATOM   1998 C  C     . GLU A 1 257 ? -3.941  14.294  -8.912  1.00 37.36  ? 257  GLU A C     1 
ATOM   1999 O  O     . GLU A 1 257 ? -4.241  15.102  -9.792  1.00 32.15  ? 257  GLU A O     1 
ATOM   2000 C  CB    . GLU A 1 257 ? -1.972  12.924  -9.546  1.00 31.99  ? 257  GLU A CB    1 
ATOM   2001 C  CG    . GLU A 1 257 ? -0.513  12.600  -9.394  1.00 35.42  ? 257  GLU A CG    1 
ATOM   2002 C  CD    . GLU A 1 257 ? -0.093  11.347  -10.167 1.00 43.12  ? 257  GLU A CD    1 
ATOM   2003 O  OE1   . GLU A 1 257 ? -0.946  10.697  -10.818 1.00 43.50  ? 257  GLU A OE1   1 
ATOM   2004 O  OE2   . GLU A 1 257 ? 1.105   11.006  -10.112 1.00 52.50  ? 257  GLU A OE2   1 
ATOM   2005 N  N     . GLU A 1 258 ? -4.860  13.614  -8.235  1.00 31.32  ? 258  GLU A N     1 
ATOM   2006 C  CA    . GLU A 1 258 ? -6.269  13.604  -8.619  1.00 30.15  ? 258  GLU A CA    1 
ATOM   2007 C  C     . GLU A 1 258 ? -7.172  14.347  -7.635  1.00 31.62  ? 258  GLU A C     1 
ATOM   2008 O  O     . GLU A 1 258 ? -8.377  14.461  -7.881  1.00 32.86  ? 258  GLU A O     1 
ATOM   2009 C  CB    . GLU A 1 258 ? -6.738  12.146  -8.788  1.00 33.04  ? 258  GLU A CB    1 
ATOM   2010 C  CG    . GLU A 1 258 ? -5.985  11.417  -9.894  1.00 33.03  ? 258  GLU A CG    1 
ATOM   2011 C  CD    . GLU A 1 258 ? -6.200  9.924   -9.894  1.00 35.12  ? 258  GLU A CD    1 
ATOM   2012 O  OE1   . GLU A 1 258 ? -7.063  9.427   -9.140  1.00 36.07  ? 258  GLU A OE1   1 
ATOM   2013 O  OE2   . GLU A 1 258 ? -5.491  9.226   -10.657 1.00 43.94  ? 258  GLU A OE2   1 
ATOM   2014 N  N     . GLY A 1 259 ? -6.628  14.866  -6.542  1.00 25.63  ? 259  GLY A N     1 
ATOM   2015 C  CA    . GLY A 1 259 ? -7.398  15.708  -5.656  1.00 25.57  ? 259  GLY A CA    1 
ATOM   2016 C  C     . GLY A 1 259 ? -8.112  14.994  -4.527  1.00 25.42  ? 259  GLY A C     1 
ATOM   2017 O  O     . GLY A 1 259 ? -9.143  15.482  -4.059  1.00 29.32  ? 259  GLY A O     1 
ATOM   2018 N  N     . TRP A 1 260 ? -7.600  13.862  -4.060  1.00 21.57  ? 260  TRP A N     1 
ATOM   2019 C  CA    . TRP A 1 260 ? -8.206  13.176  -2.930  1.00 23.30  ? 260  TRP A CA    1 
ATOM   2020 C  C     . TRP A 1 260 ? -7.120  12.828  -1.918  1.00 19.51  ? 260  TRP A C     1 
ATOM   2021 O  O     . TRP A 1 260 ? -6.008  13.366  -1.942  1.00 22.20  ? 260  TRP A O     1 
ATOM   2022 C  CB    . TRP A 1 260 ? -9.045  11.975  -3.390  1.00 23.01  ? 260  TRP A CB    1 
ATOM   2023 C  CG    . TRP A 1 260 ? -8.409  10.984  -4.373  1.00 26.42  ? 260  TRP A CG    1 
ATOM   2024 C  CD1   . TRP A 1 260 ? -8.240  11.157  -5.720  1.00 27.55  ? 260  TRP A CD1   1 
ATOM   2025 C  CD2   . TRP A 1 260 ? -7.957  9.651   -4.083  1.00 24.97  ? 260  TRP A CD2   1 
ATOM   2026 N  NE1   . TRP A 1 260 ? -7.675  10.030  -6.278  1.00 30.11  ? 260  TRP A NE1   1 
ATOM   2027 C  CE2   . TRP A 1 260 ? -7.505  9.086   -5.298  1.00 24.82  ? 260  TRP A CE2   1 
ATOM   2028 C  CE3   . TRP A 1 260 ? -7.892  8.874   -2.914  1.00 23.16  ? 260  TRP A CE3   1 
ATOM   2029 C  CZ2   . TRP A 1 260 ? -6.970  7.805   -5.366  1.00 28.28  ? 260  TRP A CZ2   1 
ATOM   2030 C  CZ3   . TRP A 1 260 ? -7.346  7.603   -2.994  1.00 23.15  ? 260  TRP A CZ3   1 
ATOM   2031 C  CH2   . TRP A 1 260 ? -6.912  7.078   -4.205  1.00 24.20  ? 260  TRP A CH2   1 
ATOM   2032 N  N     . LEU A 1 261 ? -7.451  11.942  -0.982  1.00 20.22  ? 261  LEU A N     1 
ATOM   2033 C  CA    . LEU A 1 261 ? -6.570  11.575  0.125   1.00 19.62  ? 261  LEU A CA    1 
ATOM   2034 C  C     . LEU A 1 261 ? -6.625  10.067  0.348   1.00 24.68  ? 261  LEU A C     1 
ATOM   2035 O  O     . LEU A 1 261 ? -7.703  9.477   0.280   1.00 24.03  ? 261  LEU A O     1 
ATOM   2036 C  CB    . LEU A 1 261 ? -6.984  12.308  1.429   1.00 21.19  ? 261  LEU A CB    1 
ATOM   2037 C  CG    . LEU A 1 261 ? -6.990  13.854  1.430   1.00 20.78  ? 261  LEU A CG    1 
ATOM   2038 C  CD1   . LEU A 1 261 ? -7.676  14.414  2.701   1.00 25.62  ? 261  LEU A CD1   1 
ATOM   2039 C  CD2   . LEU A 1 261 ? -5.587  14.430  1.351   1.00 20.98  ? 261  LEU A CD2   1 
ATOM   2040 N  N     . ALA A 1 262 ? -5.467  9.452   0.626   1.00 21.07  ? 262  ALA A N     1 
ATOM   2041 C  CA    . ALA A 1 262 ? -5.357  8.049   1.003   1.00 14.84  ? 262  ALA A CA    1 
ATOM   2042 C  C     . ALA A 1 262 ? -4.544  7.968   2.287   1.00 19.44  ? 262  ALA A C     1 
ATOM   2043 O  O     . ALA A 1 262 ? -3.372  8.349   2.299   1.00 16.95  ? 262  ALA A O     1 
ATOM   2044 C  CB    . ALA A 1 262 ? -4.670  7.218   -0.096  1.00 18.00  ? 262  ALA A CB    1 
ATOM   2045 N  N     . GLU A 1 263 ? -5.147  7.469   3.366   1.00 15.52  ? 263  GLU A N     1 
ATOM   2046 C  CA    . GLU A 1 263 ? -4.628  7.723   4.708   1.00 14.13  ? 263  GLU A CA    1 
ATOM   2047 C  C     . GLU A 1 263 ? -4.758  6.479   5.565   1.00 15.49  ? 263  GLU A C     1 
ATOM   2048 O  O     . GLU A 1 263 ? -5.651  5.665   5.365   1.00 16.75  ? 263  GLU A O     1 
ATOM   2049 C  CB    . GLU A 1 263 ? -5.390  8.899   5.427   1.00 13.93  ? 263  GLU A CB    1 
ATOM   2050 C  CG    . GLU A 1 263 ? -5.368  10.243  4.600   1.00 15.35  ? 263  GLU A CG    1 
ATOM   2051 C  CD    . GLU A 1 263 ? -4.008  10.900  4.533   1.00 19.20  ? 263  GLU A CD    1 
ATOM   2052 O  OE1   . GLU A 1 263 ? -3.108  10.565  5.331   1.00 20.67  ? 263  GLU A OE1   1 
ATOM   2053 O  OE2   . GLU A 1 263 ? -3.832  11.773  3.657   1.00 17.94  ? 263  GLU A OE2   1 
ATOM   2054 N  N     . HIS A 1 264 ? -3.835  6.355   6.519   1.00 13.64  ? 264  HIS A N     1 
ATOM   2055 C  CA    . HIS A 1 264 ? -3.751  5.279   7.488   1.00 17.16  ? 264  HIS A CA    1 
ATOM   2056 C  C     . HIS A 1 264 ? -4.764  5.553   8.611   1.00 19.76  ? 264  HIS A C     1 
ATOM   2057 O  O     . HIS A 1 264 ? -4.409  5.831   9.756   1.00 15.43  ? 264  HIS A O     1 
ATOM   2058 C  CB    . HIS A 1 264 ? -2.333  5.239   8.039   1.00 15.29  ? 264  HIS A CB    1 
ATOM   2059 C  CG    . HIS A 1 264 ? -2.008  3.993   8.800   1.00 14.92  ? 264  HIS A CG    1 
ATOM   2060 N  ND1   . HIS A 1 264 ? -0.935  3.915   9.665   1.00 14.41  ? 264  HIS A ND1   1 
ATOM   2061 C  CD2   . HIS A 1 264 ? -2.589  2.764   8.807   1.00 15.01  ? 264  HIS A CD2   1 
ATOM   2062 C  CE1   . HIS A 1 264 ? -0.866  2.698   10.179  1.00 14.55  ? 264  HIS A CE1   1 
ATOM   2063 N  NE2   . HIS A 1 264 ? -1.850  1.974   9.665   1.00 16.69  ? 264  HIS A NE2   1 
ATOM   2064 N  N     . MET A 1 265 ? -6.047  5.496   8.262   1.00 15.07  ? 265  MET A N     1 
ATOM   2065 C  CA    . MET A 1 265 ? -7.095  5.860   9.215   1.00 15.22  ? 265  MET A CA    1 
ATOM   2066 C  C     . MET A 1 265 ? -8.181  4.798   9.295   1.00 17.74  ? 265  MET A C     1 
ATOM   2067 O  O     . MET A 1 265 ? -8.597  4.242   8.276   1.00 18.51  ? 265  MET A O     1 
ATOM   2068 C  CB    . MET A 1 265 ? -7.764  7.180   8.825   1.00 17.70  ? 265  MET A CB    1 
ATOM   2069 C  CG    . MET A 1 265 ? -6.841  8.378   8.925   1.00 16.80  ? 265  MET A CG    1 
ATOM   2070 S  SD    . MET A 1 265 ? -7.649  9.816   8.235   1.00 20.94  ? 265  MET A SD    1 
ATOM   2071 C  CE    . MET A 1 265 ? -6.338  11.009  8.470   1.00 20.80  ? 265  MET A CE    1 
ATOM   2072 N  N     . LEU A 1 266 ? -8.647  4.540   10.508  1.00 17.43  ? 266  LEU A N     1 
ATOM   2073 C  CA    . LEU A 1 266 ? -9.937  3.883   10.675  1.00 19.30  ? 266  LEU A CA    1 
ATOM   2074 C  C     . LEU A 1 266 ? -11.090 4.847   10.340  1.00 22.81  ? 266  LEU A C     1 
ATOM   2075 O  O     . LEU A 1 266 ? -10.947 6.081   10.347  1.00 19.29  ? 266  LEU A O     1 
ATOM   2076 C  CB    . LEU A 1 266 ? -10.083 3.373   12.108  1.00 18.69  ? 266  LEU A CB    1 
ATOM   2077 C  CG    . LEU A 1 266 ? -10.209 4.463   13.199  1.00 16.89  ? 266  LEU A CG    1 
ATOM   2078 C  CD1   . LEU A 1 266 ? -11.671 4.916   13.434  1.00 22.05  ? 266  LEU A CD1   1 
ATOM   2079 C  CD2   . LEU A 1 266 ? -9.630  4.035   14.506  1.00 17.90  ? 266  LEU A CD2   1 
ATOM   2080 N  N     . ILE A 1 267 ? -12.257 4.265   10.070  1.00 17.62  ? 267  ILE A N     1 
ATOM   2081 C  CA    . ILE A 1 267 ? -13.493 5.000   9.861   1.00 17.52  ? 267  ILE A CA    1 
ATOM   2082 C  C     . ILE A 1 267 ? -14.550 4.359   10.760  1.00 17.93  ? 267  ILE A C     1 
ATOM   2083 O  O     . ILE A 1 267 ? -14.723 3.135   10.728  1.00 18.89  ? 267  ILE A O     1 
ATOM   2084 C  CB    . ILE A 1 267 ? -13.959 4.954   8.396   1.00 16.14  ? 267  ILE A CB    1 
ATOM   2085 C  CG1   . ILE A 1 267 ? -12.911 5.548   7.434   1.00 19.19  ? 267  ILE A CG1   1 
ATOM   2086 C  CG2   . ILE A 1 267 ? -15.243 5.740   8.244   1.00 17.93  ? 267  ILE A CG2   1 
ATOM   2087 C  CD1   . ILE A 1 267 ? -13.231 5.241   5.965   1.00 17.13  ? 267  ILE A CD1   1 
ATOM   2088 N  N     . LEU A 1 268 ? -15.236 5.166   11.566  1.00 18.38  ? 268  LEU A N     1 
ATOM   2089 C  CA    . LEU A 1 268 ? -16.318 4.624   12.398  1.00 19.69  ? 268  LEU A CA    1 
ATOM   2090 C  C     . LEU A 1 268 ? -17.499 5.582   12.358  1.00 23.75  ? 268  LEU A C     1 
ATOM   2091 O  O     . LEU A 1 268 ? -17.354 6.780   12.070  1.00 19.64  ? 268  LEU A O     1 
ATOM   2092 C  CB    . LEU A 1 268 ? -15.874 4.382   13.865  1.00 21.61  ? 268  LEU A CB    1 
ATOM   2093 C  CG    . LEU A 1 268 ? -15.423 5.588   14.718  1.00 21.32  ? 268  LEU A CG    1 
ATOM   2094 C  CD1   . LEU A 1 268 ? -16.615 6.334   15.286  1.00 27.65  ? 268  LEU A CD1   1 
ATOM   2095 C  CD2   . LEU A 1 268 ? -14.525 5.131   15.871  1.00 19.77  ? 268  LEU A CD2   1 
ATOM   2096 N  N     . GLY A 1 269 ? -18.674 5.035   12.645  1.00 18.74  ? 269  GLY A N     1 
ATOM   2097 C  CA    . GLY A 1 269 ? -19.895 5.816   12.782  1.00 19.96  ? 269  GLY A CA    1 
ATOM   2098 C  C     . GLY A 1 269 ? -20.357 5.701   14.221  1.00 20.36  ? 269  GLY A C     1 
ATOM   2099 O  O     . GLY A 1 269 ? -20.327 4.616   14.794  1.00 21.06  ? 269  GLY A O     1 
ATOM   2100 N  N     . ILE A 1 270 ? -20.764 6.816   14.802  1.00 20.56  ? 270  ILE A N     1 
ATOM   2101 C  CA    . ILE A 1 270 ? -21.167 6.845   16.199  1.00 23.41  ? 270  ILE A CA    1 
ATOM   2102 C  C     . ILE A 1 270 ? -22.527 7.528   16.296  1.00 21.06  ? 270  ILE A C     1 
ATOM   2103 O  O     . ILE A 1 270 ? -22.740 8.574   15.686  1.00 19.84  ? 270  ILE A O     1 
ATOM   2104 C  CB    . ILE A 1 270 ? -20.123 7.559   17.081  1.00 26.19  ? 270  ILE A CB    1 
ATOM   2105 C  CG1   . ILE A 1 270 ? -20.585 7.602   18.537  1.00 24.18  ? 270  ILE A CG1   1 
ATOM   2106 C  CG2   . ILE A 1 270 ? -19.813 8.991   16.561  1.00 24.00  ? 270  ILE A CG2   1 
ATOM   2107 C  CD1   . ILE A 1 270 ? -19.443 7.832   19.520  1.00 24.66  ? 270  ILE A CD1   1 
ATOM   2108 N  N     . THR A 1 271 ? -23.457 6.916   17.038  1.00 22.04  ? 271  THR A N     1 
ATOM   2109 C  CA    . THR A 1 271 ? -24.824 7.409   17.171  1.00 20.09  ? 271  THR A CA    1 
ATOM   2110 C  C     . THR A 1 271 ? -25.062 7.723   18.640  1.00 20.60  ? 271  THR A C     1 
ATOM   2111 O  O     . THR A 1 271 ? -24.688 6.932   19.505  1.00 20.15  ? 271  THR A O     1 
ATOM   2112 C  CB    . THR A 1 271 ? -25.843 6.365   16.694  1.00 24.60  ? 271  THR A CB    1 
ATOM   2113 O  OG1   . THR A 1 271 ? -25.527 5.949   15.356  1.00 22.89  ? 271  THR A OG1   1 
ATOM   2114 C  CG2   . THR A 1 271 ? -27.265 6.917   16.746  1.00 21.37  ? 271  THR A CG2   1 
ATOM   2115 N  N     . ASN A 1 272 ? -25.623 8.883   18.930  1.00 21.93  ? 272  ASN A N     1 
ATOM   2116 C  CA    . ASN A 1 272 ? -25.801 9.297   20.312  1.00 20.73  ? 272  ASN A CA    1 
ATOM   2117 C  C     . ASN A 1 272 ? -27.196 8.911   20.802  1.00 22.41  ? 272  ASN A C     1 
ATOM   2118 O  O     . ASN A 1 272 ? -28.004 8.359   20.047  1.00 22.22  ? 272  ASN A O     1 
ATOM   2119 C  CB    . ASN A 1 272 ? -25.524 10.804  20.443  1.00 20.83  ? 272  ASN A CB    1 
ATOM   2120 C  CG    . ASN A 1 272 ? -26.645 11.682  19.912  1.00 19.81  ? 272  ASN A CG    1 
ATOM   2121 O  OD1   . ASN A 1 272 ? -27.578 11.217  19.271  1.00 20.31  ? 272  ASN A OD1   1 
ATOM   2122 N  ND2   . ASN A 1 272 ? -26.521 12.978  20.149  1.00 23.79  ? 272  ASN A ND2   1 
ATOM   2123 N  N     . PRO A 1 273 ? -27.521 9.185   22.074  1.00 21.15  ? 273  PRO A N     1 
ATOM   2124 C  CA    . PRO A 1 273 ? -28.858 8.807   22.575  1.00 24.64  ? 273  PRO A CA    1 
ATOM   2125 C  C     . PRO A 1 273 ? -29.997 9.639   21.999  1.00 25.93  ? 273  PRO A C     1 
ATOM   2126 O  O     . PRO A 1 273 ? -31.160 9.281   22.200  1.00 27.00  ? 273  PRO A O     1 
ATOM   2127 C  CB    . PRO A 1 273 ? -28.733 9.007   24.085  1.00 25.65  ? 273  PRO A CB    1 
ATOM   2128 C  CG    . PRO A 1 273 ? -27.281 8.794   24.375  1.00 22.42  ? 273  PRO A CG    1 
ATOM   2129 C  CD    . PRO A 1 273 ? -26.586 9.442   23.186  1.00 24.22  ? 273  PRO A CD    1 
ATOM   2130 N  N     . GLU A 1 274 ? -29.715 10.748  21.310  1.00 24.95  ? 274  GLU A N     1 
ATOM   2131 C  CA    . GLU A 1 274 ? -30.755 11.532  20.652  1.00 23.25  ? 274  GLU A CA    1 
ATOM   2132 C  C     . GLU A 1 274 ? -30.972 11.102  19.208  1.00 27.10  ? 274  GLU A C     1 
ATOM   2133 O  O     . GLU A 1 274 ? -31.614 11.833  18.442  1.00 24.62  ? 274  GLU A O     1 
ATOM   2134 C  CB    . GLU A 1 274 ? -30.415 13.019  20.690  1.00 26.73  ? 274  GLU A CB    1 
ATOM   2135 C  CG    . GLU A 1 274 ? -29.996 13.539  22.047  1.00 25.33  ? 274  GLU A CG    1 
ATOM   2136 C  CD    . GLU A 1 274 ? -31.169 13.692  23.004  1.00 35.99  ? 274  GLU A CD    1 
ATOM   2137 O  OE1   . GLU A 1 274 ? -32.337 13.516  22.583  1.00 32.04  ? 274  GLU A OE1   1 
ATOM   2138 O  OE2   . GLU A 1 274 ? -30.914 13.979  24.186  1.00 34.44  ? 274  GLU A OE2   1 
ATOM   2139 N  N     . GLY A 1 275 ? -30.439 9.944   18.821  1.00 24.04  ? 275  GLY A N     1 
ATOM   2140 C  CA    . GLY A 1 275 ? -30.611 9.434   17.478  1.00 24.86  ? 275  GLY A CA    1 
ATOM   2141 C  C     . GLY A 1 275 ? -29.864 10.175  16.383  1.00 26.40  ? 275  GLY A C     1 
ATOM   2142 O  O     . GLY A 1 275 ? -30.305 10.142  15.233  1.00 27.46  ? 275  GLY A O     1 
ATOM   2143 N  N     . LYS A 1 276 ? -28.763 10.859  16.696  1.00 22.95  ? 276  LYS A N     1 
ATOM   2144 C  CA    . LYS A 1 276 ? -27.946 11.514  15.667  1.00 21.33  ? 276  LYS A CA    1 
ATOM   2145 C  C     . LYS A 1 276 ? -26.680 10.690  15.450  1.00 18.01  ? 276  LYS A C     1 
ATOM   2146 O  O     . LYS A 1 276 ? -26.098 10.186  16.409  1.00 23.02  ? 276  LYS A O     1 
ATOM   2147 C  CB    . LYS A 1 276 ? -27.550 12.946  16.040  1.00 24.02  ? 276  LYS A CB    1 
ATOM   2148 C  CG    . LYS A 1 276 ? -28.665 13.882  16.659  1.00 30.03  ? 276  LYS A CG    1 
ATOM   2149 C  CD    . LYS A 1 276 ? -29.754 14.267  15.669  1.00 32.21  ? 276  LYS A CD    1 
ATOM   2150 C  CE    . LYS A 1 276 ? -30.727 15.336  16.234  1.00 22.69  ? 276  LYS A CE    1 
ATOM   2151 N  NZ    . LYS A 1 276 ? -31.565 14.836  17.362  1.00 26.52  ? 276  LYS A NZ    1 
ATOM   2152 N  N     . LYS A 1 277 ? -26.217 10.608  14.209  1.00 15.73  ? 277  LYS A N     1 
ATOM   2153 C  CA    . LYS A 1 277 ? -25.078 9.757   13.865  1.00 18.82  ? 277  LYS A CA    1 
ATOM   2154 C  C     . LYS A 1 277 ? -24.027 10.582  13.133  1.00 18.38  ? 277  LYS A C     1 
ATOM   2155 O  O     . LYS A 1 277 ? -24.367 11.335  12.220  1.00 19.75  ? 277  LYS A O     1 
ATOM   2156 C  CB    . LYS A 1 277 ? -25.518 8.583   12.990  1.00 18.45  ? 277  LYS A CB    1 
ATOM   2157 C  CG    . LYS A 1 277 ? -24.381 7.702   12.489  1.00 18.20  ? 277  LYS A CG    1 
ATOM   2158 C  CD    . LYS A 1 277 ? -24.930 6.410   11.837  1.00 26.41  ? 277  LYS A CD    1 
ATOM   2159 C  CE    . LYS A 1 277 ? -23.812 5.409   11.573  1.00 24.26  ? 277  LYS A CE    1 
ATOM   2160 N  NZ    . LYS A 1 277 ? -24.302 4.189   10.928  1.00 19.33  ? 277  LYS A NZ    1 
ATOM   2161 N  N     . LYS A 1 278 ? -22.764 10.463  13.558  1.00 16.81  ? 278  LYS A N     1 
ATOM   2162 C  CA    . LYS A 1 278 ? -21.654 11.120  12.863  1.00 22.46  ? 278  LYS A CA    1 
ATOM   2163 C  C     . LYS A 1 278 ? -20.576 10.101  12.505  1.00 20.44  ? 278  LYS A C     1 
ATOM   2164 O  O     . LYS A 1 278 ? -20.454 9.057   13.145  1.00 18.43  ? 278  LYS A O     1 
ATOM   2165 C  CB    . LYS A 1 278 ? -21.059 12.232  13.715  1.00 20.77  ? 278  LYS A CB    1 
ATOM   2166 C  CG    . LYS A 1 278 ? -22.037 13.380  13.905  1.00 18.62  ? 278  LYS A CG    1 
ATOM   2167 C  CD    . LYS A 1 278 ? -21.437 14.503  14.708  1.00 23.16  ? 278  LYS A CD    1 
ATOM   2168 C  CE    . LYS A 1 278 ? -22.470 15.596  14.972  1.00 22.87  ? 278  LYS A CE    1 
ATOM   2169 N  NZ    . LYS A 1 278 ? -23.027 16.129  13.717  1.00 24.76  ? 278  LYS A NZ    1 
ATOM   2170 N  N     . TYR A 1 279 ? -19.788 10.414  11.482  1.00 21.67  ? 279  TYR A N     1 
ATOM   2171 C  CA    . TYR A 1 279 ? -18.665 9.571   11.089  1.00 15.93  ? 279  TYR A CA    1 
ATOM   2172 C  C     . TYR A 1 279 ? -17.363 10.286  11.388  1.00 18.45  ? 279  TYR A C     1 
ATOM   2173 O  O     . TYR A 1 279 ? -17.232 11.489  11.124  1.00 21.58  ? 279  TYR A O     1 
ATOM   2174 C  CB    . TYR A 1 279 ? -18.747 9.199   9.619   1.00 17.50  ? 279  TYR A CB    1 
ATOM   2175 C  CG    . TYR A 1 279 ? -19.822 8.146   9.281   1.00 21.48  ? 279  TYR A CG    1 
ATOM   2176 C  CD1   . TYR A 1 279 ? -19.545 6.780   9.354   1.00 17.77  ? 279  TYR A CD1   1 
ATOM   2177 C  CD2   . TYR A 1 279 ? -21.095 8.540   8.886   1.00 21.56  ? 279  TYR A CD2   1 
ATOM   2178 C  CE1   . TYR A 1 279 ? -20.539 5.803   9.045   1.00 17.68  ? 279  TYR A CE1   1 
ATOM   2179 C  CE2   . TYR A 1 279 ? -22.077 7.599   8.561   1.00 19.59  ? 279  TYR A CE2   1 
ATOM   2180 C  CZ    . TYR A 1 279 ? -21.780 6.236   8.616   1.00 20.90  ? 279  TYR A CZ    1 
ATOM   2181 O  OH    . TYR A 1 279 ? -22.761 5.334   8.278   1.00 24.09  ? 279  TYR A OH    1 
ATOM   2182 N  N     . LEU A 1 280 ? -16.424 9.551   11.981  1.00 19.79  ? 280  LEU A N     1 
ATOM   2183 C  CA    . LEU A 1 280 ? -15.106 10.064  12.341  1.00 18.58  ? 280  LEU A CA    1 
ATOM   2184 C  C     . LEU A 1 280 ? -14.045 9.158   11.727  1.00 20.11  ? 280  LEU A C     1 
ATOM   2185 O  O     . LEU A 1 280 ? -14.254 7.951   11.595  1.00 16.86  ? 280  LEU A O     1 
ATOM   2186 C  CB    . LEU A 1 280 ? -14.920 10.086  13.842  1.00 21.20  ? 280  LEU A CB    1 
ATOM   2187 C  CG    . LEU A 1 280 ? -16.127 10.661  14.620  1.00 25.00  ? 280  LEU A CG    1 
ATOM   2188 C  CD1   . LEU A 1 280 ? -15.971 10.437  16.106  1.00 21.62  ? 280  LEU A CD1   1 
ATOM   2189 C  CD2   . LEU A 1 280 ? -16.153 12.094  14.330  1.00 22.55  ? 280  LEU A CD2   1 
ATOM   2190 N  N     . ALA A 1 281 ? -12.887 9.742   11.399  1.00 14.90  ? 281  ALA A N     1 
ATOM   2191 C  CA    . ALA A 1 281 ? -11.717 8.994   10.975  1.00 16.15  ? 281  ALA A CA    1 
ATOM   2192 C  C     . ALA A 1 281 ? -10.619 9.234   12.004  1.00 18.46  ? 281  ALA A C     1 
ATOM   2193 O  O     . ALA A 1 281 ? -10.579 10.291  12.642  1.00 17.95  ? 281  ALA A O     1 
ATOM   2194 C  CB    . ALA A 1 281 ? -11.270 9.419   9.573   1.00 18.32  ? 281  ALA A CB    1 
ATOM   2195 N  N     . ALA A 1 282 ? -9.729  8.264   12.181  1.00 15.79  ? 282  ALA A N     1 
ATOM   2196 C  CA    . ALA A 1 282 ? -8.656  8.410   13.170  1.00 17.40  ? 282  ALA A CA    1 
ATOM   2197 C  C     . ALA A 1 282 ? -7.370  7.818   12.628  1.00 19.79  ? 282  ALA A C     1 
ATOM   2198 O  O     . ALA A 1 282 ? -7.355  6.656   12.237  1.00 15.78  ? 282  ALA A O     1 
ATOM   2199 C  CB    . ALA A 1 282 ? -9.002  7.715   14.499  1.00 17.89  ? 282  ALA A CB    1 
ATOM   2200 N  N     . ALA A 1 283 ? -6.279  8.587   12.667  1.00 17.51  ? 283  ALA A N     1 
ATOM   2201 C  CA    . ALA A 1 283 ? -4.968  8.103   12.255  1.00 18.42  ? 283  ALA A CA    1 
ATOM   2202 C  C     . ALA A 1 283 ? -4.114  7.881   13.501  1.00 19.79  ? 283  ALA A C     1 
ATOM   2203 O  O     . ALA A 1 283 ? -3.711  8.851   14.153  1.00 17.17  ? 283  ALA A O     1 
ATOM   2204 C  CB    . ALA A 1 283 ? -4.305  9.120   11.311  1.00 16.28  ? 283  ALA A CB    1 
ATOM   2205 N  N     . PHE A 1 284 ? -3.830  6.607   13.827  1.00 15.16  ? 284  PHE A N     1 
ATOM   2206 C  CA    . PHE A 1 284 ? -2.866  6.233   14.849  1.00 14.27  ? 284  PHE A CA    1 
ATOM   2207 C  C     . PHE A 1 284 ? -1.829  5.353   14.179  1.00 19.37  ? 284  PHE A C     1 
ATOM   2208 O  O     . PHE A 1 284 ? -2.164  4.630   13.237  1.00 20.49  ? 284  PHE A O     1 
ATOM   2209 C  CB    . PHE A 1 284 ? -3.466  5.413   16.010  1.00 16.85  ? 284  PHE A CB    1 
ATOM   2210 C  CG    . PHE A 1 284 ? -4.710  5.959   16.596  1.00 17.68  ? 284  PHE A CG    1 
ATOM   2211 C  CD1   . PHE A 1 284 ? -4.894  7.337   16.729  1.00 16.79  ? 284  PHE A CD1   1 
ATOM   2212 C  CD2   . PHE A 1 284 ? -5.692  5.087   17.080  1.00 21.08  ? 284  PHE A CD2   1 
ATOM   2213 C  CE1   . PHE A 1 284 ? -6.069  7.857   17.311  1.00 17.73  ? 284  PHE A CE1   1 
ATOM   2214 C  CE2   . PHE A 1 284 ? -6.859  5.590   17.678  1.00 19.44  ? 284  PHE A CE2   1 
ATOM   2215 C  CZ    . PHE A 1 284 ? -7.043  6.975   17.787  1.00 19.20  ? 284  PHE A CZ    1 
ATOM   2216 N  N     . PRO A 1 285 ? -0.587  5.350   14.661  1.00 18.26  ? 285  PRO A N     1 
ATOM   2217 C  CA    . PRO A 1 285 ? 0.422   4.441   14.105  1.00 20.66  ? 285  PRO A CA    1 
ATOM   2218 C  C     . PRO A 1 285 ? 0.075   2.975   14.374  1.00 23.78  ? 285  PRO A C     1 
ATOM   2219 O  O     . PRO A 1 285 ? -0.805  2.639   15.168  1.00 18.96  ? 285  PRO A O     1 
ATOM   2220 C  CB    . PRO A 1 285 ? 1.718   4.861   14.816  1.00 20.11  ? 285  PRO A CB    1 
ATOM   2221 C  CG    . PRO A 1 285 ? 1.445   6.286   15.334  1.00 23.33  ? 285  PRO A CG    1 
ATOM   2222 C  CD    . PRO A 1 285 ? -0.020  6.333   15.607  1.00 18.80  ? 285  PRO A CD    1 
ATOM   2223 N  N     . SER A 1 286 ? 0.775   2.074   13.682  1.00 21.37  ? 286  SER A N     1 
ATOM   2224 C  CA    . SER A 1 286 ? 0.569   0.663   13.983  1.00 21.28  ? 286  SER A CA    1 
ATOM   2225 C  C     . SER A 1 286 ? 0.835   0.421   15.464  1.00 22.24  ? 286  SER A C     1 
ATOM   2226 O  O     . SER A 1 286 ? 1.682   1.084   16.072  1.00 24.73  ? 286  SER A O     1 
ATOM   2227 C  CB    . SER A 1 286 ? 1.491   -0.220  13.120  1.00 29.45  ? 286  SER A CB    1 
ATOM   2228 O  OG    . SER A 1 286 ? 1.693   0.360   11.835  1.00 36.89  ? 286  SER A OG    1 
ATOM   2229 N  N     . ALA A 1 287 ? 0.077   -0.506  16.057  1.00 23.48  ? 287  ALA A N     1 
ATOM   2230 C  CA    . ALA A 1 287 ? 0.225   -0.911  17.457  1.00 25.83  ? 287  ALA A CA    1 
ATOM   2231 C  C     . ALA A 1 287 ? -0.248  0.145   18.448  1.00 24.79  ? 287  ALA A C     1 
ATOM   2232 O  O     . ALA A 1 287 ? 0.148   0.110   19.629  1.00 27.12  ? 287  ALA A O     1 
ATOM   2233 C  CB    . ALA A 1 287 ? 1.665   -1.311  17.806  1.00 33.92  ? 287  ALA A CB    1 
ATOM   2234 N  N     . CYS A 1 288 ? -1.084  1.088   18.001  1.00 24.71  ? 288  CYS A N     1 
ATOM   2235 C  CA    . CYS A 1 288 ? -1.566  2.182   18.847  1.00 21.18  ? 288  CYS A CA    1 
ATOM   2236 C  C     . CYS A 1 288 ? -3.085  2.214   18.931  1.00 20.42  ? 288  CYS A C     1 
ATOM   2237 O  O     . CYS A 1 288 ? -3.654  3.195   19.430  1.00 21.67  ? 288  CYS A O     1 
ATOM   2238 C  CB    . CYS A 1 288 ? -1.013  3.533   18.331  1.00 21.04  ? 288  CYS A CB    1 
ATOM   2239 S  SG    . CYS A 1 288 ? 0.779   3.621   18.595  1.00 25.21  ? 288  CYS A SG    1 
ATOM   2240 N  N     . GLY A 1 289 ? -3.757  1.150   18.493  1.00 23.85  ? 289  GLY A N     1 
ATOM   2241 C  CA    . GLY A 1 289 ? -5.151  0.925   18.842  1.00 21.43  ? 289  GLY A CA    1 
ATOM   2242 C  C     . GLY A 1 289 ? -6.209  1.341   17.840  1.00 20.26  ? 289  GLY A C     1 
ATOM   2243 O  O     . GLY A 1 289 ? -7.346  1.584   18.247  1.00 21.70  ? 289  GLY A O     1 
ATOM   2244 N  N     . LYS A 1 290 ? -5.888  1.457   16.558  1.00 18.26  ? 290  LYS A N     1 
ATOM   2245 C  CA    . LYS A 1 290 ? -6.954  1.779   15.610  1.00 18.36  ? 290  LYS A CA    1 
ATOM   2246 C  C     . LYS A 1 290 ? -8.032  0.696   15.632  1.00 20.38  ? 290  LYS A C     1 
ATOM   2247 O  O     . LYS A 1 290 ? -9.233  0.987   15.646  1.00 21.61  ? 290  LYS A O     1 
ATOM   2248 C  CB    . LYS A 1 290 ? -6.386  1.930   14.201  1.00 18.21  ? 290  LYS A CB    1 
ATOM   2249 C  CG    . LYS A 1 290 ? -5.558  3.220   13.974  1.00 16.31  ? 290  LYS A CG    1 
ATOM   2250 C  CD    . LYS A 1 290 ? -5.230  3.394   12.481  1.00 17.15  ? 290  LYS A CD    1 
ATOM   2251 C  CE    . LYS A 1 290 ? -4.483  2.183   11.922  1.00 14.79  ? 290  LYS A CE    1 
ATOM   2252 N  NZ    . LYS A 1 290 ? -3.200  1.915   12.636  1.00 17.74  ? 290  LYS A NZ    1 
ATOM   2253 N  N     . THR A 1 291 ? -7.623  -0.566  15.617  1.00 18.36  ? 291  THR A N     1 
ATOM   2254 C  CA    . THR A 1 291 ? -8.636  -1.612  15.491  1.00 18.72  ? 291  THR A CA    1 
ATOM   2255 C  C     . THR A 1 291 ? -9.532  -1.669  16.735  1.00 17.26  ? 291  THR A C     1 
ATOM   2256 O  O     . THR A 1 291 ? -10.744 -1.877  16.608  1.00 17.64  ? 291  THR A O     1 
ATOM   2257 C  CB    . THR A 1 291 ? -7.980  -2.962  15.171  1.00 17.02  ? 291  THR A CB    1 
ATOM   2258 O  OG1   . THR A 1 291 ? -7.467  -2.881  13.856  1.00 19.57  ? 291  THR A OG1   1 
ATOM   2259 C  CG2   . THR A 1 291 ? -9.036  -4.091  15.144  1.00 19.22  ? 291  THR A CG2   1 
ATOM   2260 N  N     . ASN A 1 292 ? -8.975  -1.431  17.930  1.00 20.60  ? 292  ASN A N     1 
ATOM   2261 C  CA    . ASN A 1 292 ? -9.815  -1.374  19.140  1.00 21.08  ? 292  ASN A CA    1 
ATOM   2262 C  C     . ASN A 1 292 ? -10.850 -0.273  19.058  1.00 22.27  ? 292  ASN A C     1 
ATOM   2263 O  O     . ASN A 1 292 ? -11.981 -0.442  19.533  1.00 19.31  ? 292  ASN A O     1 
ATOM   2264 C  CB    . ASN A 1 292 ? -8.973  -1.151  20.401  1.00 22.93  ? 292  ASN A CB    1 
ATOM   2265 C  CG    . ASN A 1 292 ? -7.907  -2.219  20.571  1.00 29.50  ? 292  ASN A CG    1 
ATOM   2266 O  OD1   . ASN A 1 292 ? -6.873  -2.159  19.927  1.00 27.80  ? 292  ASN A OD1   1 
ATOM   2267 N  ND2   . ASN A 1 292 ? -8.166  -3.205  21.426  1.00 27.31  ? 292  ASN A ND2   1 
ATOM   2268 N  N     . LEU A 1 293 ? -10.464 0.905   18.522  1.00 18.89  ? 293  LEU A N     1 
ATOM   2269 C  CA    . LEU A 1 293 ? -11.408 2.018   18.494  1.00 17.40  ? 293  LEU A CA    1 
ATOM   2270 C  C     . LEU A 1 293 ? -12.458 1.805   17.411  1.00 19.64  ? 293  LEU A C     1 
ATOM   2271 O  O     . LEU A 1 293 ? -13.639 2.099   17.621  1.00 19.80  ? 293  LEU A O     1 
ATOM   2272 C  CB    . LEU A 1 293 ? -10.671 3.346   18.259  1.00 17.07  ? 293  LEU A CB    1 
ATOM   2273 C  CG    . LEU A 1 293 ? -11.557 4.589   18.303  1.00 21.85  ? 293  LEU A CG    1 
ATOM   2274 C  CD1   . LEU A 1 293 ? -12.106 4.707   19.678  1.00 21.35  ? 293  LEU A CD1   1 
ATOM   2275 C  CD2   . LEU A 1 293 ? -10.782 5.835   17.958  1.00 17.80  ? 293  LEU A CD2   1 
ATOM   2276 N  N     . ALA A 1 294 ? -12.042 1.294   16.248  1.00 18.27  ? 294  ALA A N     1 
ATOM   2277 C  CA    . ALA A 1 294 ? -12.971 1.101   15.140  1.00 17.96  ? 294  ALA A CA    1 
ATOM   2278 C  C     . ALA A 1 294 ? -14.086 0.118   15.500  1.00 20.42  ? 294  ALA A C     1 
ATOM   2279 O  O     . ALA A 1 294 ? -15.193 0.193   14.951  1.00 20.05  ? 294  ALA A O     1 
ATOM   2280 C  CB    . ALA A 1 294 ? -12.196 0.598   13.906  1.00 14.66  ? 294  ALA A CB    1 
ATOM   2281 N  N     . MET A 1 295 ? -13.818 -0.814  16.406  1.00 18.24  ? 295  MET A N     1 
ATOM   2282 C  CA    . MET A 1 295 ? -14.798 -1.842  16.737  1.00 21.39  ? 295  MET A CA    1 
ATOM   2283 C  C     . MET A 1 295 ? -15.291 -1.710  18.153  1.00 23.02  ? 295  MET A C     1 
ATOM   2284 O  O     . MET A 1 295 ? -15.815 -2.696  18.706  1.00 23.13  ? 295  MET A O     1 
ATOM   2285 C  CB    . MET A 1 295 ? -14.219 -3.252  16.558  1.00 22.08  ? 295  MET A CB    1 
ATOM   2286 C  CG    . MET A 1 295 ? -13.825 -3.555  15.197  1.00 25.39  ? 295  MET A CG    1 
ATOM   2287 S  SD    . MET A 1 295 ? -13.172 -5.206  15.164  1.00 26.75  ? 295  MET A SD    1 
ATOM   2288 C  CE    . MET A 1 295 ? -12.871 -5.281  13.403  1.00 27.66  ? 295  MET A CE    1 
ATOM   2289 N  N     . MET A 1 296 ? -15.148 -0.508  18.734  1.00 24.09  ? 296  MET A N     1 
ATOM   2290 C  CA    . MET A 1 296 ? -15.346 -0.322  20.169  1.00 22.54  ? 296  MET A CA    1 
ATOM   2291 C  C     . MET A 1 296 ? -16.732 -0.779  20.605  1.00 26.31  ? 296  MET A C     1 
ATOM   2292 O  O     . MET A 1 296 ? -17.719 -0.587  19.889  1.00 27.24  ? 296  MET A O     1 
ATOM   2293 C  CB    . MET A 1 296 ? -15.186 1.160   20.513  1.00 24.99  ? 296  MET A CB    1 
ATOM   2294 C  CG    . MET A 1 296 ? -14.926 1.470   21.974  1.00 36.12  ? 296  MET A CG    1 
ATOM   2295 S  SD    . MET A 1 296 ? -15.170 3.235   22.215  1.00 36.68  ? 296  MET A SD    1 
ATOM   2296 C  CE    . MET A 1 296 ? -16.825 3.246   21.584  1.00 26.69  ? 296  MET A CE    1 
ATOM   2297 N  N     . ASN A 1 297 ? -16.810 -1.352  21.807  1.00 21.73  ? 297  ASN A N     1 
ATOM   2298 C  CA    . ASN A 1 297 ? -18.098 -1.513  22.464  1.00 26.29  ? 297  ASN A CA    1 
ATOM   2299 C  C     . ASN A 1 297 ? -18.222 -0.400  23.503  1.00 21.38  ? 297  ASN A C     1 
ATOM   2300 O  O     . ASN A 1 297 ? -17.494 -0.424  24.504  1.00 20.62  ? 297  ASN A O     1 
ATOM   2301 C  CB    . ASN A 1 297 ? -18.203 -2.893  23.119  1.00 24.50  ? 297  ASN A CB    1 
ATOM   2302 C  CG    . ASN A 1 297 ? -19.540 -3.117  23.789  1.00 33.38  ? 297  ASN A CG    1 
ATOM   2303 O  OD1   . ASN A 1 297 ? -20.572 -2.665  23.302  1.00 37.51  ? 297  ASN A OD1   1 
ATOM   2304 N  ND2   . ASN A 1 297 ? -19.530 -3.811  24.919  1.00 36.10  ? 297  ASN A ND2   1 
ATOM   2305 N  N     . PRO A 1 298 ? -19.034 0.626   23.283  1.00 21.49  ? 298  PRO A N     1 
ATOM   2306 C  CA    . PRO A 1 298 ? -19.016 1.779   24.204  1.00 24.82  ? 298  PRO A CA    1 
ATOM   2307 C  C     . PRO A 1 298 ? -19.581 1.416   25.563  1.00 27.86  ? 298  PRO A C     1 
ATOM   2308 O  O     . PRO A 1 298 ? -20.553 0.667   25.662  1.00 23.79  ? 298  PRO A O     1 
ATOM   2309 C  CB    . PRO A 1 298 ? -19.902 2.823   23.509  1.00 22.53  ? 298  PRO A CB    1 
ATOM   2310 C  CG    . PRO A 1 298 ? -20.709 2.076   22.529  1.00 27.91  ? 298  PRO A CG    1 
ATOM   2311 C  CD    . PRO A 1 298 ? -19.939 0.826   22.143  1.00 25.70  ? 298  PRO A CD    1 
ATOM   2312 N  N     . THR A 1 299 ? -18.971 1.968   26.618  1.00 26.14  ? 299  THR A N     1 
ATOM   2313 C  CA    . THR A 1 299 ? -19.513 1.763   27.959  1.00 28.07  ? 299  THR A CA    1 
ATOM   2314 C  C     . THR A 1 299 ? -20.698 2.675   28.276  1.00 33.00  ? 299  THR A C     1 
ATOM   2315 O  O     . THR A 1 299 ? -21.504 2.324   29.138  1.00 26.38  ? 299  THR A O     1 
ATOM   2316 C  CB    . THR A 1 299 ? -18.418 1.961   29.018  1.00 25.04  ? 299  THR A CB    1 
ATOM   2317 O  OG1   . THR A 1 299 ? -17.859 3.283   28.899  1.00 21.90  ? 299  THR A OG1   1 
ATOM   2318 C  CG2   . THR A 1 299 ? -17.322 0.900   28.856  1.00 23.83  ? 299  THR A CG2   1 
ATOM   2319 N  N     . LEU A 1 300 ? -20.831 3.826   27.608  1.00 27.43  ? 300  LEU A N     1 
ATOM   2320 C  CA    . LEU A 1 300 ? -21.905 4.766   27.934  1.00 22.92  ? 300  LEU A CA    1 
ATOM   2321 C  C     . LEU A 1 300 ? -23.234 4.288   27.359  1.00 29.69  ? 300  LEU A C     1 
ATOM   2322 O  O     . LEU A 1 300 ? -23.308 3.966   26.166  1.00 25.66  ? 300  LEU A O     1 
ATOM   2323 C  CB    . LEU A 1 300 ? -21.598 6.166   27.371  1.00 24.10  ? 300  LEU A CB    1 
ATOM   2324 C  CG    . LEU A 1 300 ? -20.390 6.919   27.894  1.00 25.57  ? 300  LEU A CG    1 
ATOM   2325 C  CD1   . LEU A 1 300 ? -20.217 8.183   27.071  1.00 22.76  ? 300  LEU A CD1   1 
ATOM   2326 C  CD2   . LEU A 1 300 ? -20.557 7.267   29.356  1.00 28.55  ? 300  LEU A CD2   1 
ATOM   2327 N  N     . PRO A 1 301 ? -24.316 4.284   28.140  1.00 31.07  ? 301  PRO A N     1 
ATOM   2328 C  CA    . PRO A 1 301 ? -25.582 3.753   27.621  1.00 28.36  ? 301  PRO A CA    1 
ATOM   2329 C  C     . PRO A 1 301 ? -26.201 4.678   26.583  1.00 21.19  ? 301  PRO A C     1 
ATOM   2330 O  O     . PRO A 1 301 ? -26.112 5.900   26.674  1.00 24.50  ? 301  PRO A O     1 
ATOM   2331 C  CB    . PRO A 1 301 ? -26.464 3.629   28.877  1.00 31.47  ? 301  PRO A CB    1 
ATOM   2332 C  CG    . PRO A 1 301 ? -25.915 4.643   29.823  1.00 38.35  ? 301  PRO A CG    1 
ATOM   2333 C  CD    . PRO A 1 301 ? -24.417 4.681   29.555  1.00 36.98  ? 301  PRO A CD    1 
ATOM   2334 N  N     . GLY A 1 302 ? -26.854 4.073   25.597  1.00 18.80  ? 302  GLY A N     1 
ATOM   2335 C  CA    . GLY A 1 302 ? -27.508 4.810   24.542  1.00 24.87  ? 302  GLY A CA    1 
ATOM   2336 C  C     . GLY A 1 302 ? -26.589 5.249   23.417  1.00 23.70  ? 302  GLY A C     1 
ATOM   2337 O  O     . GLY A 1 302 ? -27.043 5.965   22.516  1.00 25.95  ? 302  GLY A O     1 
ATOM   2338 N  N     . TRP A 1 303 ? -25.312 4.872   23.462  1.00 25.08  ? 303  TRP A N     1 
ATOM   2339 C  CA    . TRP A 1 303 ? -24.324 5.190   22.434  1.00 23.49  ? 303  TRP A CA    1 
ATOM   2340 C  C     . TRP A 1 303 ? -24.023 3.941   21.626  1.00 26.12  ? 303  TRP A C     1 
ATOM   2341 O  O     . TRP A 1 303 ? -23.971 2.837   22.180  1.00 25.94  ? 303  TRP A O     1 
ATOM   2342 C  CB    . TRP A 1 303 ? -23.038 5.744   23.078  1.00 20.16  ? 303  TRP A CB    1 
ATOM   2343 C  CG    . TRP A 1 303 ? -23.213 7.165   23.542  1.00 20.34  ? 303  TRP A CG    1 
ATOM   2344 C  CD1   . TRP A 1 303 ? -23.757 7.584   24.726  1.00 25.63  ? 303  TRP A CD1   1 
ATOM   2345 C  CD2   . TRP A 1 303 ? -22.866 8.350   22.816  1.00 22.44  ? 303  TRP A CD2   1 
ATOM   2346 N  NE1   . TRP A 1 303 ? -23.772 8.973   24.779  1.00 24.86  ? 303  TRP A NE1   1 
ATOM   2347 C  CE2   . TRP A 1 303 ? -23.223 9.460   23.621  1.00 24.23  ? 303  TRP A CE2   1 
ATOM   2348 C  CE3   . TRP A 1 303 ? -22.274 8.586   21.561  1.00 18.64  ? 303  TRP A CE3   1 
ATOM   2349 C  CZ2   . TRP A 1 303 ? -23.015 10.777  23.209  1.00 21.41  ? 303  TRP A CZ2   1 
ATOM   2350 C  CZ3   . TRP A 1 303 ? -22.077 9.893   21.155  1.00 22.38  ? 303  TRP A CZ3   1 
ATOM   2351 C  CH2   . TRP A 1 303 ? -22.446 10.975  21.979  1.00 22.14  ? 303  TRP A CH2   1 
ATOM   2352 N  N     . LYS A 1 304 ? -23.845 4.103   20.312  1.00 22.85  ? 304  LYS A N     1 
ATOM   2353 C  CA    . LYS A 1 304 ? -23.570 2.959   19.460  1.00 19.68  ? 304  LYS A CA    1 
ATOM   2354 C  C     . LYS A 1 304 ? -22.415 3.295   18.536  1.00 21.56  ? 304  LYS A C     1 
ATOM   2355 O  O     . LYS A 1 304 ? -22.402 4.372   17.952  1.00 22.11  ? 304  LYS A O     1 
ATOM   2356 C  CB    . LYS A 1 304 ? -24.791 2.578   18.622  1.00 23.31  ? 304  LYS A CB    1 
ATOM   2357 C  CG    . LYS A 1 304 ? -24.535 1.345   17.740  1.00 35.42  ? 304  LYS A CG    1 
ATOM   2358 C  CD    . LYS A 1 304 ? -25.828 0.752   17.156  1.00 41.42  ? 304  LYS A CD    1 
ATOM   2359 C  CE    . LYS A 1 304 ? -25.535 -0.493  16.325  1.00 49.57  ? 304  LYS A CE    1 
ATOM   2360 N  NZ    . LYS A 1 304 ? -26.766 -1.297  16.030  1.00 51.76  ? 304  LYS A NZ    1 
ATOM   2361 N  N     . VAL A 1 305 ? -21.465 2.375   18.373  1.00 18.20  ? 305  VAL A N     1 
ATOM   2362 C  CA    . VAL A 1 305 ? -20.385 2.573   17.412  1.00 19.94  ? 305  VAL A CA    1 
ATOM   2363 C  C     . VAL A 1 305 ? -20.489 1.482   16.359  1.00 25.12  ? 305  VAL A C     1 
ATOM   2364 O  O     . VAL A 1 305 ? -20.732 0.314   16.688  1.00 22.78  ? 305  VAL A O     1 
ATOM   2365 C  CB    . VAL A 1 305 ? -19.002 2.539   18.091  1.00 29.05  ? 305  VAL A CB    1 
ATOM   2366 C  CG1   . VAL A 1 305 ? -17.874 2.425   17.025  1.00 22.01  ? 305  VAL A CG1   1 
ATOM   2367 C  CG2   . VAL A 1 305 ? -18.821 3.769   18.910  1.00 24.32  ? 305  VAL A CG2   1 
ATOM   2368 N  N     . GLU A 1 306 ? -20.343 1.868   15.096  1.00 21.22  ? 306  GLU A N     1 
ATOM   2369 C  CA    . GLU A 1 306 ? -20.306 0.924   13.997  1.00 19.36  ? 306  GLU A CA    1 
ATOM   2370 C  C     . GLU A 1 306 ? -19.023 1.118   13.203  1.00 20.78  ? 306  GLU A C     1 
ATOM   2371 O  O     . GLU A 1 306 ? -18.486 2.228   13.104  1.00 19.73  ? 306  GLU A O     1 
ATOM   2372 C  CB    . GLU A 1 306 ? -21.557 1.087   13.108  1.00 23.00  ? 306  GLU A CB    1 
ATOM   2373 C  CG    . GLU A 1 306 ? -22.872 0.803   13.890  1.00 24.27  ? 306  GLU A CG    1 
ATOM   2374 C  CD    . GLU A 1 306 ? -24.094 1.299   13.148  1.00 25.60  ? 306  GLU A CD    1 
ATOM   2375 O  OE1   . GLU A 1 306 ? -24.340 2.514   13.165  1.00 27.30  ? 306  GLU A OE1   1 
ATOM   2376 O  OE2   . GLU A 1 306 ? -24.787 0.484   12.515  1.00 29.35  ? 306  GLU A OE2   1 
ATOM   2377 N  N     . CYS A 1 307 ? -18.524 0.024   12.633  1.00 18.90  ? 307  CYS A N     1 
ATOM   2378 C  CA    . CYS A 1 307 ? -17.222 0.018   11.969  1.00 21.03  ? 307  CYS A CA    1 
ATOM   2379 C  C     . CYS A 1 307 ? -17.363 0.098   10.446  1.00 25.48  ? 307  CYS A C     1 
ATOM   2380 O  O     . CYS A 1 307 ? -17.997 -0.766  9.843   1.00 22.91  ? 307  CYS A O     1 
ATOM   2381 C  CB    . CYS A 1 307 ? -16.462 -1.257  12.341  1.00 26.36  ? 307  CYS A CB    1 
ATOM   2382 S  SG    . CYS A 1 307 ? -14.874 -1.335  11.525  1.00 26.43  ? 307  CYS A SG    1 
ATOM   2383 N  N     . VAL A 1 308 ? -16.756 1.113   9.823   1.00 22.81  ? 308  VAL A N     1 
ATOM   2384 C  CA    . VAL A 1 308 ? -16.651 1.156   8.362   1.00 18.28  ? 308  VAL A CA    1 
ATOM   2385 C  C     . VAL A 1 308 ? -15.337 0.529   7.895   1.00 22.95  ? 308  VAL A C     1 
ATOM   2386 O  O     . VAL A 1 308 ? -15.327 -0.241  6.939   1.00 20.77  ? 308  VAL A O     1 
ATOM   2387 C  CB    . VAL A 1 308 ? -16.805 2.607   7.845   1.00 19.00  ? 308  VAL A CB    1 
ATOM   2388 C  CG1   . VAL A 1 308 ? -16.508 2.717   6.313   1.00 20.19  ? 308  VAL A CG1   1 
ATOM   2389 C  CG2   . VAL A 1 308 ? -18.193 3.197   8.173   1.00 21.55  ? 308  VAL A CG2   1 
ATOM   2390 N  N     . GLY A 1 309 ? -14.215 0.836   8.562   1.00 18.88  ? 309  GLY A N     1 
ATOM   2391 C  CA    . GLY A 1 309 ? -12.930 0.183   8.312   1.00 18.63  ? 309  GLY A CA    1 
ATOM   2392 C  C     . GLY A 1 309 ? -11.995 0.481   9.466   1.00 19.96  ? 309  GLY A C     1 
ATOM   2393 O  O     . GLY A 1 309 ? -12.245 1.382   10.276  1.00 17.40  ? 309  GLY A O     1 
ATOM   2394 N  N     . ASP A 1 310 ? -10.910 -0.282  9.558   1.00 14.79  ? 310  ASP A N     1 
ATOM   2395 C  CA    . ASP A 1 310 ? -10.017 -0.154  10.704  1.00 17.72  ? 310  ASP A CA    1 
ATOM   2396 C  C     . ASP A 1 310 ? -8.593  0.286   10.379  1.00 17.30  ? 310  ASP A C     1 
ATOM   2397 O  O     . ASP A 1 310 ? -7.770  0.311   11.313  1.00 19.30  ? 310  ASP A O     1 
ATOM   2398 C  CB    . ASP A 1 310 ? -9.972  -1.463  11.502  1.00 17.65  ? 310  ASP A CB    1 
ATOM   2399 C  CG    . ASP A 1 310 ? -9.111  -2.543  10.850  1.00 21.57  ? 310  ASP A CG    1 
ATOM   2400 O  OD1   . ASP A 1 310 ? -8.903  -2.513  9.623   1.00 18.35  ? 310  ASP A OD1   1 
ATOM   2401 O  OD2   . ASP A 1 310 ? -8.631  -3.389  11.602  1.00 21.88  ? 310  ASP A OD2   1 
ATOM   2402 N  N     . ASP A 1 311 ? -8.263  0.631   9.112   1.00 17.48  ? 311  ASP A N     1 
ATOM   2403 C  CA    . ASP A 1 311 ? -6.847  0.776   8.738   1.00 17.87  ? 311  ASP A CA    1 
ATOM   2404 C  C     . ASP A 1 311 ? -6.569  1.744   7.608   1.00 15.64  ? 311  ASP A C     1 
ATOM   2405 O  O     . ASP A 1 311 ? -5.569  2.451   7.653   1.00 16.81  ? 311  ASP A O     1 
ATOM   2406 C  CB    . ASP A 1 311 ? -6.245  -0.590  8.317   1.00 17.43  ? 311  ASP A CB    1 
ATOM   2407 C  CG    . ASP A 1 311 ? -4.718  -0.597  8.313   1.00 16.83  ? 311  ASP A CG    1 
ATOM   2408 O  OD1   . ASP A 1 311 ? -4.089  -0.247  9.308   1.00 20.40  ? 311  ASP A OD1   1 
ATOM   2409 O  OD2   . ASP A 1 311 ? -4.137  -1.036  7.319   1.00 19.79  ? 311  ASP A OD2   1 
ATOM   2410 N  N     . ILE A 1 312 ? -7.390  1.745   6.560   1.00 14.04  ? 312  ILE A N     1 
ATOM   2411 C  CA    . ILE A 1 312 ? -7.125  2.532   5.371   1.00 16.79  ? 312  ILE A CA    1 
ATOM   2412 C  C     . ILE A 1 312 ? -8.391  3.291   5.005   1.00 19.34  ? 312  ILE A C     1 
ATOM   2413 O  O     . ILE A 1 312 ? -9.474  2.703   4.959   1.00 19.23  ? 312  ILE A O     1 
ATOM   2414 C  CB    . ILE A 1 312 ? -6.644  1.656   4.193   1.00 20.32  ? 312  ILE A CB    1 
ATOM   2415 C  CG1   . ILE A 1 312 ? -5.306  1.005   4.581   1.00 18.48  ? 312  ILE A CG1   1 
ATOM   2416 C  CG2   . ILE A 1 312 ? -6.466  2.517   2.901   1.00 20.99  ? 312  ILE A CG2   1 
ATOM   2417 C  CD1   . ILE A 1 312 ? -4.771  0.074   3.602   1.00 28.56  ? 312  ILE A CD1   1 
ATOM   2418 N  N     . ALA A 1 313 ? -8.255  4.592   4.752   1.00 16.25  ? 313  ALA A N     1 
ATOM   2419 C  CA    . ALA A 1 313 ? -9.368  5.411   4.290   1.00 16.82  ? 313  ALA A CA    1 
ATOM   2420 C  C     . ALA A 1 313 ? -8.959  6.118   3.012   1.00 18.60  ? 313  ALA A C     1 
ATOM   2421 O  O     . ALA A 1 313 ? -7.852  6.651   2.942   1.00 18.44  ? 313  ALA A O     1 
ATOM   2422 C  CB    . ALA A 1 313 ? -9.760  6.469   5.341   1.00 15.28  ? 313  ALA A CB    1 
ATOM   2423 N  N     . TRP A 1 314 ? -9.856  6.138   2.021   1.00 18.09  ? 314  TRP A N     1 
ATOM   2424 C  CA    . TRP A 1 314 ? -9.744  6.974   0.836   1.00 21.44  ? 314  TRP A CA    1 
ATOM   2425 C  C     . TRP A 1 314 ? -10.836 8.032   0.903   1.00 23.23  ? 314  TRP A C     1 
ATOM   2426 O  O     . TRP A 1 314 ? -12.008 7.703   1.091   1.00 23.68  ? 314  TRP A O     1 
ATOM   2427 C  CB    . TRP A 1 314 ? -9.891  6.152   -0.449  1.00 21.07  ? 314  TRP A CB    1 
ATOM   2428 C  CG    . TRP A 1 314 ? -8.734  5.231   -0.724  1.00 16.79  ? 314  TRP A CG    1 
ATOM   2429 C  CD1   . TRP A 1 314 ? -7.599  5.049   0.038   1.00 19.11  ? 314  TRP A CD1   1 
ATOM   2430 C  CD2   . TRP A 1 314 ? -8.600  4.348   -1.856  1.00 20.93  ? 314  TRP A CD2   1 
ATOM   2431 N  NE1   . TRP A 1 314 ? -6.773  4.088   -0.567  1.00 16.56  ? 314  TRP A NE1   1 
ATOM   2432 C  CE2   . TRP A 1 314 ? -7.370  3.680   -1.734  1.00 16.96  ? 314  TRP A CE2   1 
ATOM   2433 C  CE3   . TRP A 1 314 ? -9.396  4.090   -2.975  1.00 21.12  ? 314  TRP A CE3   1 
ATOM   2434 C  CZ2   . TRP A 1 314 ? -6.935  2.743   -2.670  1.00 20.15  ? 314  TRP A CZ2   1 
ATOM   2435 C  CZ3   . TRP A 1 314 ? -8.938  3.138   -3.919  1.00 21.49  ? 314  TRP A CZ3   1 
ATOM   2436 C  CH2   . TRP A 1 314 ? -7.732  2.502   -3.749  1.00 22.87  ? 314  TRP A CH2   1 
ATOM   2437 N  N     . MET A 1 315 ? -10.471 9.286   0.725   1.00 19.90  ? 315  MET A N     1 
ATOM   2438 C  CA    . MET A 1 315 ? -11.402 10.376  1.002   1.00 18.34  ? 315  MET A CA    1 
ATOM   2439 C  C     . MET A 1 315 ? -11.339 11.442  -0.076  1.00 24.58  ? 315  MET A C     1 
ATOM   2440 O  O     . MET A 1 315 ? -10.263 11.745  -0.601  1.00 27.37  ? 315  MET A O     1 
ATOM   2441 C  CB    . MET A 1 315 ? -11.096 11.014  2.363   1.00 22.31  ? 315  MET A CB    1 
ATOM   2442 C  CG    . MET A 1 315 ? -11.059 10.026  3.518   1.00 27.30  ? 315  MET A CG    1 
ATOM   2443 S  SD    . MET A 1 315 ? -10.868 10.811  5.135   1.00 28.97  ? 315  MET A SD    1 
ATOM   2444 C  CE    . MET A 1 315 ? -9.418  11.800  4.914   1.00 30.45  ? 315  MET A CE    1 
ATOM   2445 N  N     . LYS A 1 316 ? -12.487 12.061  -0.349  1.00 27.07  ? 316  LYS A N     1 
ATOM   2446 C  CA    . LYS A 1 316 ? -12.580 13.080  -1.381  1.00 28.47  ? 316  LYS A CA    1 
ATOM   2447 C  C     . LYS A 1 316 ? -13.728 14.016  -1.045  1.00 29.01  ? 316  LYS A C     1 
ATOM   2448 O  O     . LYS A 1 316 ? -14.794 13.561  -0.633  1.00 29.41  ? 316  LYS A O     1 
ATOM   2449 C  CB    . LYS A 1 316 ? -12.790 12.444  -2.760  1.00 27.99  ? 316  LYS A CB    1 
ATOM   2450 C  CG    . LYS A 1 316 ? -12.960 13.460  -3.878  1.00 33.74  ? 316  LYS A CG    1 
ATOM   2451 C  CD    . LYS A 1 316 ? -12.838 12.819  -5.250  1.00 40.14  ? 316  LYS A CD    1 
ATOM   2452 C  CE    . LYS A 1 316 ? -13.958 11.806  -5.482  1.00 44.62  ? 316  LYS A CE    1 
ATOM   2453 N  NZ    . LYS A 1 316 ? -15.305 12.442  -5.376  1.00 49.11  ? 316  LYS A NZ    1 
ATOM   2454 N  N     . PHE A 1 317 ? -13.499 15.320  -1.191  1.00 31.13  ? 317  PHE A N     1 
ATOM   2455 C  CA    . PHE A 1 317 ? -14.603 16.265  -1.116  1.00 35.62  ? 317  PHE A CA    1 
ATOM   2456 C  C     . PHE A 1 317 ? -15.539 16.052  -2.298  1.00 36.67  ? 317  PHE A C     1 
ATOM   2457 O  O     . PHE A 1 317 ? -15.096 15.833  -3.427  1.00 42.56  ? 317  PHE A O     1 
ATOM   2458 C  CB    . PHE A 1 317 ? -14.075 17.706  -1.078  1.00 32.01  ? 317  PHE A CB    1 
ATOM   2459 C  CG    . PHE A 1 317 ? -13.476 18.073  0.241   1.00 31.06  ? 317  PHE A CG    1 
ATOM   2460 C  CD1   . PHE A 1 317 ? -14.289 18.402  1.319   1.00 32.55  ? 317  PHE A CD1   1 
ATOM   2461 C  CD2   . PHE A 1 317 ? -12.107 18.058  0.423   1.00 35.31  ? 317  PHE A CD2   1 
ATOM   2462 C  CE1   . PHE A 1 317 ? -13.747 18.728  2.559   1.00 34.13  ? 317  PHE A CE1   1 
ATOM   2463 C  CE2   . PHE A 1 317 ? -11.558 18.368  1.649   1.00 34.31  ? 317  PHE A CE2   1 
ATOM   2464 C  CZ    . PHE A 1 317 ? -12.380 18.709  2.729   1.00 34.56  ? 317  PHE A CZ    1 
ATOM   2465 N  N     . ASP A 1 318 ? -16.842 16.054  -2.030  1.00 34.33  ? 318  ASP A N     1 
ATOM   2466 C  CA    . ASP A 1 318 ? -17.808 15.892  -3.104  1.00 30.30  ? 318  ASP A CA    1 
ATOM   2467 C  C     . ASP A 1 318 ? -18.250 17.277  -3.593  1.00 31.02  ? 318  ASP A C     1 
ATOM   2468 O  O     . ASP A 1 318 ? -17.752 18.311  -3.136  1.00 26.57  ? 318  ASP A O     1 
ATOM   2469 C  CB    . ASP A 1 318 ? -18.966 14.992  -2.648  1.00 34.47  ? 318  ASP A CB    1 
ATOM   2470 C  CG    . ASP A 1 318 ? -19.839 15.622  -1.560  1.00 31.16  ? 318  ASP A CG    1 
ATOM   2471 O  OD1   . ASP A 1 318 ? -19.727 16.831  -1.326  1.00 30.32  ? 318  ASP A OD1   1 
ATOM   2472 O  OD2   . ASP A 1 318 ? -20.641 14.880  -0.934  1.00 33.78  ? 318  ASP A OD2   1 
ATOM   2473 N  N     . ALA A 1 319 ? -19.215 17.301  -4.519  1.00 35.52  ? 319  ALA A N     1 
ATOM   2474 C  CA    . ALA A 1 319 ? -19.675 18.563  -5.089  1.00 40.37  ? 319  ALA A CA    1 
ATOM   2475 C  C     . ALA A 1 319 ? -20.297 19.462  -4.028  1.00 41.07  ? 319  ALA A C     1 
ATOM   2476 O  O     . ALA A 1 319 ? -20.251 20.696  -4.145  1.00 37.69  ? 319  ALA A O     1 
ATOM   2477 C  CB    . ALA A 1 319 ? -20.682 18.285  -6.208  1.00 43.80  ? 319  ALA A CB    1 
ATOM   2478 N  N     . GLN A 1 320 ? -20.876 18.862  -2.985  1.00 34.98  ? 320  GLN A N     1 
ATOM   2479 C  CA    . GLN A 1 320 ? -21.506 19.605  -1.902  1.00 33.70  ? 320  GLN A CA    1 
ATOM   2480 C  C     . GLN A 1 320 ? -20.509 20.083  -0.857  1.00 33.78  ? 320  GLN A C     1 
ATOM   2481 O  O     . GLN A 1 320 ? -20.900 20.796  0.071   1.00 37.04  ? 320  GLN A O     1 
ATOM   2482 C  CB    . GLN A 1 320 ? -22.567 18.729  -1.228  1.00 38.79  ? 320  GLN A CB    1 
ATOM   2483 C  CG    . GLN A 1 320 ? -23.457 17.992  -2.209  1.00 37.96  ? 320  GLN A CG    1 
ATOM   2484 C  CD    . GLN A 1 320 ? -24.280 18.933  -3.060  1.00 44.23  ? 320  GLN A CD    1 
ATOM   2485 O  OE1   . GLN A 1 320 ? -24.799 19.938  -2.570  1.00 48.48  ? 320  GLN A OE1   1 
ATOM   2486 N  NE2   . GLN A 1 320 ? -24.411 18.609  -4.344  1.00 49.69  ? 320  GLN A NE2   1 
ATOM   2487 N  N     . GLY A 1 321 ? -19.242 19.694  -0.962  1.00 35.60  ? 321  GLY A N     1 
ATOM   2488 C  CA    . GLY A 1 321 ? -18.257 20.100  0.016   1.00 32.90  ? 321  GLY A CA    1 
ATOM   2489 C  C     . GLY A 1 321 ? -18.090 19.170  1.196   1.00 31.77  ? 321  GLY A C     1 
ATOM   2490 O  O     . GLY A 1 321 ? -17.309 19.484  2.106   1.00 29.89  ? 321  GLY A O     1 
ATOM   2491 N  N     . ASN A 1 322 ? -18.794 18.042  1.225   1.00 29.17  ? 322  ASN A N     1 
ATOM   2492 C  CA    . ASN A 1 322 ? -18.596 17.091  2.307   1.00 27.32  ? 322  ASN A CA    1 
ATOM   2493 C  C     . ASN A 1 322 ? -17.362 16.246  2.016   1.00 23.83  ? 322  ASN A C     1 
ATOM   2494 O  O     . ASN A 1 322 ? -17.109 15.870  0.868   1.00 27.24  ? 322  ASN A O     1 
ATOM   2495 C  CB    . ASN A 1 322 ? -19.836 16.209  2.479   1.00 30.41  ? 322  ASN A CB    1 
ATOM   2496 C  CG    . ASN A 1 322 ? -21.101 17.030  2.699   1.00 29.81  ? 322  ASN A CG    1 
ATOM   2497 O  OD1   . ASN A 1 322 ? -21.291 17.608  3.757   1.00 36.56  ? 322  ASN A OD1   1 
ATOM   2498 N  ND2   . ASN A 1 322 ? -21.950 17.102  1.683   1.00 32.49  ? 322  ASN A ND2   1 
ATOM   2499 N  N     . LEU A 1 323 ? -16.572 15.981  3.053   1.00 24.44  ? 323  LEU A N     1 
ATOM   2500 C  CA    . LEU A 1 323 ? -15.458 15.035  2.936   1.00 20.82  ? 323  LEU A CA    1 
ATOM   2501 C  C     . LEU A 1 323 ? -16.018 13.627  3.068   1.00 24.27  ? 323  LEU A C     1 
ATOM   2502 O  O     . LEU A 1 323 ? -16.436 13.235  4.158   1.00 28.88  ? 323  LEU A O     1 
ATOM   2503 C  CB    . LEU A 1 323 ? -14.420 15.310  4.022   1.00 20.58  ? 323  LEU A CB    1 
ATOM   2504 C  CG    . LEU A 1 323 ? -13.142 14.479  3.967   1.00 29.36  ? 323  LEU A CG    1 
ATOM   2505 C  CD1   . LEU A 1 323 ? -12.348 14.779  2.670   1.00 25.35  ? 323  LEU A CD1   1 
ATOM   2506 C  CD2   . LEU A 1 323 ? -12.329 14.790  5.219   1.00 22.92  ? 323  LEU A CD2   1 
ATOM   2507 N  N     . ARG A 1 324 ? -16.082 12.891  1.957   1.00 20.98  ? 324  ARG A N     1 
ATOM   2508 C  CA    . ARG A 1 324 ? -16.652 11.546  1.908   1.00 23.48  ? 324  ARG A CA    1 
ATOM   2509 C  C     . ARG A 1 324 ? -15.535 10.509  1.922   1.00 24.82  ? 324  ARG A C     1 
ATOM   2510 O  O     . ARG A 1 324 ? -14.562 10.637  1.173   1.00 24.57  ? 324  ARG A O     1 
ATOM   2511 C  CB    . ARG A 1 324 ? -17.504 11.358  0.645   1.00 28.79  ? 324  ARG A CB    1 
ATOM   2512 C  CG    . ARG A 1 324 ? -18.731 12.285  0.548   1.00 28.70  ? 324  ARG A CG    1 
ATOM   2513 C  CD    . ARG A 1 324 ? -20.042 11.520  0.253   1.00 31.46  ? 324  ARG A CD    1 
ATOM   2514 N  NE    . ARG A 1 324 ? -21.190 12.165  0.893   1.00 37.09  ? 324  ARG A NE    1 
ATOM   2515 C  CZ    . ARG A 1 324 ? -22.072 11.533  1.655   1.00 36.48  ? 324  ARG A CZ    1 
ATOM   2516 N  NH1   . ARG A 1 324 ? -22.008 10.223  1.844   1.00 31.96  ? 324  ARG A NH1   1 
ATOM   2517 N  NH2   . ARG A 1 324 ? -23.055 12.230  2.228   1.00 49.69  ? 324  ARG A NH2   1 
ATOM   2518 N  N     . ALA A 1 325 ? -15.674 9.481   2.755   1.00 21.89  ? 325  ALA A N     1 
ATOM   2519 C  CA    . ALA A 1 325 ? -14.646 8.445   2.860   1.00 20.58  ? 325  ALA A CA    1 
ATOM   2520 C  C     . ALA A 1 325 ? -15.175 7.067   2.505   1.00 23.24  ? 325  ALA A C     1 
ATOM   2521 O  O     . ALA A 1 325 ? -16.327 6.733   2.808   1.00 20.60  ? 325  ALA A O     1 
ATOM   2522 C  CB    . ALA A 1 325 ? -14.057 8.386   4.270   1.00 17.98  ? 325  ALA A CB    1 
ATOM   2523 N  N     . ILE A 1 326 ? -14.311 6.248   1.864   1.00 21.52  ? 326  ILE A N     1 
ATOM   2524 C  CA    . ILE A 1 326 ? -14.570 4.822   1.795   1.00 19.61  ? 326  ILE A CA    1 
ATOM   2525 C  C     . ILE A 1 326 ? -13.410 4.056   2.414   1.00 22.38  ? 326  ILE A C     1 
ATOM   2526 O  O     . ILE A 1 326 ? -12.268 4.527   2.497   1.00 19.88  ? 326  ILE A O     1 
ATOM   2527 C  CB    . ILE A 1 326 ? -14.831 4.314   0.361   1.00 25.59  ? 326  ILE A CB    1 
ATOM   2528 C  CG1   . ILE A 1 326 ? -13.613 4.559   -0.539  1.00 24.40  ? 326  ILE A CG1   1 
ATOM   2529 C  CG2   . ILE A 1 326 ? -16.075 4.973   -0.206  1.00 21.65  ? 326  ILE A CG2   1 
ATOM   2530 C  CD1   . ILE A 1 326 ? -13.412 3.410   -1.529  1.00 30.94  ? 326  ILE A CD1   1 
ATOM   2531 N  N     . ASN A 1 327 ? -13.748 2.867   2.890   1.00 19.01  ? 327  ASN A N     1 
ATOM   2532 C  CA    . ASN A 1 327 ? -12.773 1.860   3.254   1.00 21.98  ? 327  ASN A CA    1 
ATOM   2533 C  C     . ASN A 1 327 ? -12.506 1.021   2.009   1.00 24.23  ? 327  ASN A C     1 
ATOM   2534 O  O     . ASN A 1 327 ? -13.423 0.326   1.537   1.00 21.94  ? 327  ASN A O     1 
ATOM   2535 C  CB    . ASN A 1 327 ? -13.311 0.991   4.379   1.00 21.19  ? 327  ASN A CB    1 
ATOM   2536 C  CG    . ASN A 1 327 ? -12.451 -0.253  4.638   1.00 22.03  ? 327  ASN A CG    1 
ATOM   2537 O  OD1   . ASN A 1 327 ? -11.269 -0.334  4.257   1.00 20.13  ? 327  ASN A OD1   1 
ATOM   2538 N  ND2   . ASN A 1 327 ? -13.043 -1.226  5.301   1.00 18.04  ? 327  ASN A ND2   1 
ATOM   2539 N  N     . PRO A 1 328 ? -11.302 1.073   1.426   1.00 19.22  ? 328  PRO A N     1 
ATOM   2540 C  CA    . PRO A 1 328 ? -11.039 0.289   0.215   1.00 19.93  ? 328  PRO A CA    1 
ATOM   2541 C  C     . PRO A 1 328 ? -10.812 -1.200  0.457   1.00 24.06  ? 328  PRO A C     1 
ATOM   2542 O  O     . PRO A 1 328 ? -10.699 -1.944  -0.529  1.00 24.81  ? 328  PRO A O     1 
ATOM   2543 C  CB    . PRO A 1 328 ? -9.769  0.961   -0.353  1.00 21.07  ? 328  PRO A CB    1 
ATOM   2544 C  CG    . PRO A 1 328 ? -9.036  1.407   0.863   1.00 20.04  ? 328  PRO A CG    1 
ATOM   2545 C  CD    . PRO A 1 328 ? -10.140 1.904   1.798   1.00 17.50  ? 328  PRO A CD    1 
ATOM   2546 N  N     . GLU A 1 329 ? -10.709 -1.660  1.710   1.00 19.98  ? 329  GLU A N     1 
ATOM   2547 C  CA    . GLU A 1 329 ? -10.470 -3.062  1.994   1.00 21.99  ? 329  GLU A CA    1 
ATOM   2548 C  C     . GLU A 1 329 ? -11.787 -3.827  2.074   1.00 25.68  ? 329  GLU A C     1 
ATOM   2549 O  O     . GLU A 1 329 ? -12.883 -3.255  2.003   1.00 21.68  ? 329  GLU A O     1 
ATOM   2550 C  CB    . GLU A 1 329 ? -9.679  -3.243  3.289   1.00 23.35  ? 329  GLU A CB    1 
ATOM   2551 C  CG    . GLU A 1 329 ? -8.415  -2.378  3.372   1.00 21.82  ? 329  GLU A CG    1 
ATOM   2552 C  CD    . GLU A 1 329 ? -7.464  -2.852  4.455   1.00 18.78  ? 329  GLU A CD    1 
ATOM   2553 O  OE1   . GLU A 1 329 ? -7.617  -2.400  5.600   1.00 23.42  ? 329  GLU A OE1   1 
ATOM   2554 O  OE2   . GLU A 1 329 ? -6.572  -3.691  4.181   1.00 21.04  ? 329  GLU A OE2   1 
ATOM   2555 N  N     . ASN A 1 330 ? -11.655 -5.154  2.187   1.00 21.14  ? 330  ASN A N     1 
ATOM   2556 C  CA    . ASN A 1 330 ? -12.784 -6.062  2.267   1.00 17.50  ? 330  ASN A CA    1 
ATOM   2557 C  C     . ASN A 1 330 ? -12.778 -6.887  3.543   1.00 18.27  ? 330  ASN A C     1 
ATOM   2558 O  O     . ASN A 1 330 ? -13.677 -7.710  3.742   1.00 18.95  ? 330  ASN A O     1 
ATOM   2559 C  CB    . ASN A 1 330 ? -12.788 -6.968  1.029   1.00 20.07  ? 330  ASN A CB    1 
ATOM   2560 C  CG    . ASN A 1 330 ? -14.143 -7.629  0.788   1.00 27.05  ? 330  ASN A CG    1 
ATOM   2561 O  OD1   . ASN A 1 330 ? -15.183 -7.074  1.142   1.00 24.50  ? 330  ASN A OD1   1 
ATOM   2562 N  ND2   . ASN A 1 330 ? -14.128 -8.809  0.174   1.00 21.83  ? 330  ASN A ND2   1 
ATOM   2563 N  N     . GLY A 1 331 ? -11.785 -6.709  4.408   1.00 17.65  ? 331  GLY A N     1 
ATOM   2564 C  CA    . GLY A 1 331 ? -11.667 -7.503  5.616   1.00 16.14  ? 331  GLY A CA    1 
ATOM   2565 C  C     . GLY A 1 331 ? -10.729 -6.795  6.574   1.00 20.47  ? 331  GLY A C     1 
ATOM   2566 O  O     . GLY A 1 331 ? -10.298 -5.669  6.313   1.00 19.97  ? 331  GLY A O     1 
ATOM   2567 N  N     . PHE A 1 332 ? -10.429 -7.454  7.700   1.00 21.97  ? 332  PHE A N     1 
ATOM   2568 C  CA    . PHE A 1 332 ? -9.588  -6.883  8.752   1.00 21.39  ? 332  PHE A CA    1 
ATOM   2569 C  C     . PHE A 1 332 ? -8.362  -7.749  8.965   1.00 19.93  ? 332  PHE A C     1 
ATOM   2570 O  O     . PHE A 1 332 ? -8.489  -8.949  9.189   1.00 23.34  ? 332  PHE A O     1 
ATOM   2571 C  CB    . PHE A 1 332 ? -10.324 -6.761  10.101  1.00 19.58  ? 332  PHE A CB    1 
ATOM   2572 C  CG    . PHE A 1 332 ? -11.633 -6.053  10.012  1.00 22.48  ? 332  PHE A CG    1 
ATOM   2573 C  CD1   . PHE A 1 332 ? -11.695 -4.715  9.660   1.00 20.22  ? 332  PHE A CD1   1 
ATOM   2574 C  CD2   . PHE A 1 332 ? -12.808 -6.720  10.303  1.00 25.35  ? 332  PHE A CD2   1 
ATOM   2575 C  CE1   . PHE A 1 332 ? -12.910 -4.062  9.579   1.00 21.82  ? 332  PHE A CE1   1 
ATOM   2576 C  CE2   . PHE A 1 332 ? -14.035 -6.057  10.245  1.00 26.34  ? 332  PHE A CE2   1 
ATOM   2577 C  CZ    . PHE A 1 332 ? -14.086 -4.744  9.871   1.00 27.56  ? 332  PHE A CZ    1 
ATOM   2578 N  N     . PHE A 1 333 ? -7.185  -7.124  8.936   1.00 16.78  ? 333  PHE A N     1 
ATOM   2579 C  CA    . PHE A 1 333 ? -5.915  -7.802  9.138   1.00 15.75  ? 333  PHE A CA    1 
ATOM   2580 C  C     . PHE A 1 333 ? -5.336  -7.274  10.446  1.00 18.96  ? 333  PHE A C     1 
ATOM   2581 O  O     . PHE A 1 333 ? -4.437  -6.425  10.461  1.00 15.78  ? 333  PHE A O     1 
ATOM   2582 C  CB    . PHE A 1 333 ? -4.989  -7.552  7.912   1.00 18.87  ? 333  PHE A CB    1 
ATOM   2583 C  CG    . PHE A 1 333 ? -3.729  -8.344  7.927   1.00 17.37  ? 333  PHE A CG    1 
ATOM   2584 C  CD1   . PHE A 1 333 ? -3.755  -9.732  7.818   1.00 23.06  ? 333  PHE A CD1   1 
ATOM   2585 C  CD2   . PHE A 1 333 ? -2.499  -7.701  8.013   1.00 21.67  ? 333  PHE A CD2   1 
ATOM   2586 C  CE1   . PHE A 1 333 ? -2.569  -10.488 7.798   1.00 22.01  ? 333  PHE A CE1   1 
ATOM   2587 C  CE2   . PHE A 1 333 ? -1.303  -8.450  8.008   1.00 21.56  ? 333  PHE A CE2   1 
ATOM   2588 C  CZ    . PHE A 1 333 ? -1.346  -9.848  7.894   1.00 22.82  ? 333  PHE A CZ    1 
ATOM   2589 N  N     . GLY A 1 334 ? -5.881  -7.769  11.552  1.00 19.67  ? 334  GLY A N     1 
ATOM   2590 C  CA    . GLY A 1 334 ? -5.700  -7.147  12.851  1.00 16.76  ? 334  GLY A CA    1 
ATOM   2591 C  C     . GLY A 1 334 ? -4.680  -7.878  13.704  1.00 18.92  ? 334  GLY A C     1 
ATOM   2592 O  O     . GLY A 1 334 ? -4.507  -9.089  13.592  1.00 19.70  ? 334  GLY A O     1 
ATOM   2593 N  N     . VAL A 1 335 ? -4.009  -7.121  14.575  1.00 18.06  ? 335  VAL A N     1 
ATOM   2594 C  CA    . VAL A 1 335 ? -3.071  -7.731  15.519  1.00 14.60  ? 335  VAL A CA    1 
ATOM   2595 C  C     . VAL A 1 335 ? -3.839  -8.649  16.465  1.00 19.72  ? 335  VAL A C     1 
ATOM   2596 O  O     . VAL A 1 335 ? -4.861  -8.252  17.030  1.00 20.82  ? 335  VAL A O     1 
ATOM   2597 C  CB    . VAL A 1 335 ? -2.314  -6.649  16.298  1.00 20.20  ? 335  VAL A CB    1 
ATOM   2598 C  CG1   . VAL A 1 335 ? -1.443  -7.270  17.379  1.00 17.81  ? 335  VAL A CG1   1 
ATOM   2599 C  CG2   . VAL A 1 335 ? -1.467  -5.849  15.335  1.00 19.70  ? 335  VAL A CG2   1 
ATOM   2600 N  N     . ALA A 1 336 ? -3.353  -9.888  16.632  1.00 18.13  ? 336  ALA A N     1 
ATOM   2601 C  CA    . ALA A 1 336 ? -4.070  -10.826 17.520  1.00 19.60  ? 336  ALA A CA    1 
ATOM   2602 C  C     . ALA A 1 336 ? -3.751  -10.591 18.999  1.00 17.95  ? 336  ALA A C     1 
ATOM   2603 O  O     . ALA A 1 336 ? -4.678  -10.415 19.789  1.00 24.36  ? 336  ALA A O     1 
ATOM   2604 C  CB    . ALA A 1 336 ? -3.771  -12.269 17.119  1.00 21.88  ? 336  ALA A CB    1 
ATOM   2605 N  N     . PRO A 1 337 ? -2.487  -10.584 19.423  1.00 19.89  ? 337  PRO A N     1 
ATOM   2606 C  CA    . PRO A 1 337 ? -2.206  -10.527 20.863  1.00 23.77  ? 337  PRO A CA    1 
ATOM   2607 C  C     . PRO A 1 337 ? -2.759  -9.259  21.488  1.00 25.62  ? 337  PRO A C     1 
ATOM   2608 O  O     . PRO A 1 337 ? -2.727  -8.180  20.892  1.00 27.61  ? 337  PRO A O     1 
ATOM   2609 C  CB    . PRO A 1 337 ? -0.671  -10.561 20.931  1.00 20.36  ? 337  PRO A CB    1 
ATOM   2610 C  CG    . PRO A 1 337 ? -0.247  -11.174 19.634  1.00 25.12  ? 337  PRO A CG    1 
ATOM   2611 C  CD    . PRO A 1 337 ? -1.233  -10.623 18.645  1.00 23.75  ? 337  PRO A CD    1 
ATOM   2612 N  N     . GLY A 1 338 ? -3.298  -9.407  22.696  1.00 23.22  ? 338  GLY A N     1 
ATOM   2613 C  CA    . GLY A 1 338 ? -3.995  -8.339  23.359  1.00 21.35  ? 338  GLY A CA    1 
ATOM   2614 C  C     . GLY A 1 338 ? -5.461  -8.254  23.030  1.00 23.91  ? 338  GLY A C     1 
ATOM   2615 O  O     . GLY A 1 338 ? -6.188  -7.476  23.668  1.00 29.78  ? 338  GLY A O     1 
ATOM   2616 N  N     . THR A 1 339 ? -5.925  -9.016  22.052  1.00 22.30  ? 339  THR A N     1 
ATOM   2617 C  CA    . THR A 1 339 ? -7.350  -9.058  21.753  1.00 22.94  ? 339  THR A CA    1 
ATOM   2618 C  C     . THR A 1 339 ? -8.034  -10.034 22.723  1.00 25.87  ? 339  THR A C     1 
ATOM   2619 O  O     . THR A 1 339 ? -7.641  -11.193 22.822  1.00 26.02  ? 339  THR A O     1 
ATOM   2620 C  CB    . THR A 1 339 ? -7.572  -9.491  20.310  1.00 25.66  ? 339  THR A CB    1 
ATOM   2621 O  OG1   . THR A 1 339 ? -6.820  -8.634  19.436  1.00 25.71  ? 339  THR A OG1   1 
ATOM   2622 C  CG2   . THR A 1 339 ? -9.046  -9.436  19.959  1.00 23.84  ? 339  THR A CG2   1 
ATOM   2623 N  N     . SER A 1 340 ? -9.056  -9.552  23.424  1.00 23.67  ? 340  SER A N     1 
ATOM   2624 C  CA    . SER A 1 340 ? -9.736  -10.290 24.470  1.00 28.11  ? 340  SER A CA    1 
ATOM   2625 C  C     . SER A 1 340 ? -11.144 -9.736  24.568  1.00 28.94  ? 340  SER A C     1 
ATOM   2626 O  O     . SER A 1 340 ? -11.447 -8.672  24.032  1.00 26.48  ? 340  SER A O     1 
ATOM   2627 C  CB    . SER A 1 340 ? -9.007  -10.163 25.812  1.00 28.79  ? 340  SER A CB    1 
ATOM   2628 O  OG    . SER A 1 340 ? -9.232  -8.882  26.379  1.00 29.68  ? 340  SER A OG    1 
ATOM   2629 N  N     . VAL A 1 341 ? -12.015 -10.472 25.264  1.00 28.18  ? 341  VAL A N     1 
ATOM   2630 C  CA    . VAL A 1 341 ? -13.394 -10.009 25.443  1.00 29.16  ? 341  VAL A CA    1 
ATOM   2631 C  C     . VAL A 1 341 ? -13.437 -8.623  26.062  1.00 25.99  ? 341  VAL A C     1 
ATOM   2632 O  O     . VAL A 1 341 ? -14.378 -7.855  25.818  1.00 36.83  ? 341  VAL A O     1 
ATOM   2633 C  CB    . VAL A 1 341 ? -14.195 -11.034 26.284  1.00 36.03  ? 341  VAL A CB    1 
ATOM   2634 C  CG1   . VAL A 1 341 ? -15.605 -10.505 26.577  1.00 42.40  ? 341  VAL A CG1   1 
ATOM   2635 C  CG2   . VAL A 1 341 ? -14.268 -12.347 25.542  1.00 36.03  ? 341  VAL A CG2   1 
ATOM   2636 N  N     . LYS A 1 342 ? -12.422 -8.252  26.842  1.00 32.57  ? 342  LYS A N     1 
ATOM   2637 C  CA    . LYS A 1 342 ? -12.468 -6.941  27.478  1.00 32.02  ? 342  LYS A CA    1 
ATOM   2638 C  C     . LYS A 1 342 ? -11.810 -5.836  26.651  1.00 37.08  ? 342  LYS A C     1 
ATOM   2639 O  O     . LYS A 1 342 ? -12.225 -4.675  26.769  1.00 32.03  ? 342  LYS A O     1 
ATOM   2640 C  CB    . LYS A 1 342 ? -11.851 -7.011  28.886  1.00 43.31  ? 342  LYS A CB    1 
ATOM   2641 C  CG    . LYS A 1 342 ? -10.386 -6.665  28.989  1.00 50.25  ? 342  LYS A CG    1 
ATOM   2642 C  CD    . LYS A 1 342 ? -9.921  -6.695  30.457  1.00 62.32  ? 342  LYS A CD    1 
ATOM   2643 C  CE    . LYS A 1 342 ? -8.424  -6.327  30.600  1.00 67.05  ? 342  LYS A CE    1 
ATOM   2644 N  NZ    . LYS A 1 342 ? -8.059  -4.947  30.127  1.00 57.37  ? 342  LYS A NZ    1 
ATOM   2645 N  N     . THR A 1 343 ? -10.836 -6.154  25.792  1.00 30.15  ? 343  THR A N     1 
ATOM   2646 C  CA    . THR A 1 343 ? -10.229 -5.121  24.949  1.00 29.04  ? 343  THR A CA    1 
ATOM   2647 C  C     . THR A 1 343 ? -10.876 -4.991  23.576  1.00 30.75  ? 343  THR A C     1 
ATOM   2648 O  O     . THR A 1 343 ? -10.807 -3.908  22.982  1.00 30.27  ? 343  THR A O     1 
ATOM   2649 C  CB    . THR A 1 343 ? -8.739  -5.377  24.732  1.00 29.36  ? 343  THR A CB    1 
ATOM   2650 O  OG1   . THR A 1 343 ? -8.555  -6.659  24.090  1.00 30.13  ? 343  THR A OG1   1 
ATOM   2651 C  CG2   . THR A 1 343 ? -7.970  -5.335  26.065  1.00 29.28  ? 343  THR A CG2   1 
ATOM   2652 N  N     . ASN A 1 344 ? -11.472 -6.070  23.031  1.00 23.86  ? 344  ASN A N     1 
ATOM   2653 C  CA    . ASN A 1 344 ? -12.119 -5.971  21.725  1.00 20.92  ? 344  ASN A CA    1 
ATOM   2654 C  C     . ASN A 1 344 ? -13.124 -7.098  21.529  1.00 22.47  ? 344  ASN A C     1 
ATOM   2655 O  O     . ASN A 1 344 ? -12.886 -8.033  20.737  1.00 25.28  ? 344  ASN A O     1 
ATOM   2656 C  CB    . ASN A 1 344 ? -11.064 -5.975  20.604  1.00 19.41  ? 344  ASN A CB    1 
ATOM   2657 C  CG    . ASN A 1 344 ? -11.598 -5.425  19.303  1.00 28.52  ? 344  ASN A CG    1 
ATOM   2658 O  OD1   . ASN A 1 344 ? -12.821 -5.339  19.111  1.00 27.04  ? 344  ASN A OD1   1 
ATOM   2659 N  ND2   . ASN A 1 344 ? -10.682 -5.062  18.376  1.00 23.79  ? 344  ASN A ND2   1 
ATOM   2660 N  N     . PRO A 1 345 ? -14.253 -7.050  22.242  1.00 27.01  ? 345  PRO A N     1 
ATOM   2661 C  CA    . PRO A 1 345 ? -15.238 -8.137  22.130  1.00 24.63  ? 345  PRO A CA    1 
ATOM   2662 C  C     . PRO A 1 345 ? -15.851 -8.262  20.750  1.00 27.17  ? 345  PRO A C     1 
ATOM   2663 O  O     . PRO A 1 345 ? -16.186 -9.377  20.338  1.00 24.50  ? 345  PRO A O     1 
ATOM   2664 C  CB    . PRO A 1 345 ? -16.297 -7.759  23.180  1.00 28.46  ? 345  PRO A CB    1 
ATOM   2665 C  CG    . PRO A 1 345 ? -16.164 -6.273  23.318  1.00 28.54  ? 345  PRO A CG    1 
ATOM   2666 C  CD    . PRO A 1 345 ? -14.702 -5.977  23.150  1.00 28.22  ? 345  PRO A CD    1 
ATOM   2667 N  N     . ASN A 1 346 ? -15.989 -7.168  19.994  1.00 22.88  ? 346  ASN A N     1 
ATOM   2668 C  CA    . ASN A 1 346 ? -16.557 -7.327  18.655  1.00 25.13  ? 346  ASN A CA    1 
ATOM   2669 C  C     . ASN A 1 346 ? -15.590 -8.029  17.706  1.00 26.93  ? 346  ASN A C     1 
ATOM   2670 O  O     . ASN A 1 346 ? -16.035 -8.667  16.748  1.00 26.95  ? 346  ASN A O     1 
ATOM   2671 C  CB    . ASN A 1 346 ? -16.999 -5.982  18.093  1.00 25.15  ? 346  ASN A CB    1 
ATOM   2672 C  CG    . ASN A 1 346 ? -18.282 -5.503  18.744  1.00 32.42  ? 346  ASN A CG    1 
ATOM   2673 O  OD1   . ASN A 1 346 ? -19.201 -6.308  18.949  1.00 28.96  ? 346  ASN A OD1   1 
ATOM   2674 N  ND2   . ASN A 1 346 ? -18.334 -4.224  19.139  1.00 22.61  ? 346  ASN A ND2   1 
ATOM   2675 N  N     . ALA A 1 347 ? -14.277 -7.939  17.951  1.00 24.73  ? 347  ALA A N     1 
ATOM   2676 C  CA    . ALA A 1 347 ? -13.345 -8.758  17.176  1.00 25.39  ? 347  ALA A CA    1 
ATOM   2677 C  C     . ALA A 1 347 ? -13.492 -10.238 17.528  1.00 27.22  ? 347  ALA A C     1 
ATOM   2678 O  O     . ALA A 1 347 ? -13.472 -11.108 16.638  1.00 24.62  ? 347  ALA A O     1 
ATOM   2679 C  CB    . ALA A 1 347 ? -11.911 -8.302  17.411  1.00 26.59  ? 347  ALA A CB    1 
ATOM   2680 N  N     . ILE A 1 348 ? -13.582 -10.545 18.826  1.00 24.14  ? 348  ILE A N     1 
ATOM   2681 C  CA    . ILE A 1 348 ? -13.737 -11.939 19.257  1.00 28.25  ? 348  ILE A CA    1 
ATOM   2682 C  C     . ILE A 1 348 ? -14.901 -12.586 18.523  1.00 27.56  ? 348  ILE A C     1 
ATOM   2683 O  O     . ILE A 1 348 ? -14.799 -13.719 18.035  1.00 29.98  ? 348  ILE A O     1 
ATOM   2684 C  CB    . ILE A 1 348 ? -13.916 -12.012 20.782  1.00 27.97  ? 348  ILE A CB    1 
ATOM   2685 C  CG1   . ILE A 1 348 ? -12.683 -11.437 21.484  1.00 24.78  ? 348  ILE A CG1   1 
ATOM   2686 C  CG2   . ILE A 1 348 ? -14.190 -13.454 21.232  1.00 28.57  ? 348  ILE A CG2   1 
ATOM   2687 C  CD1   . ILE A 1 348 ? -11.459 -12.311 21.426  1.00 30.43  ? 348  ILE A CD1   1 
ATOM   2688 N  N     . LYS A 1 349 ? -16.007 -11.864 18.394  1.00 24.14  ? 349  LYS A N     1 
ATOM   2689 C  CA    . LYS A 1 349 ? -17.164 -12.404 17.683  1.00 28.31  ? 349  LYS A CA    1 
ATOM   2690 C  C     . LYS A 1 349 ? -16.887 -12.608 16.203  1.00 33.68  ? 349  LYS A C     1 
ATOM   2691 O  O     . LYS A 1 349 ? -17.426 -13.540 15.604  1.00 35.12  ? 349  LYS A O     1 
ATOM   2692 C  CB    . LYS A 1 349 ? -18.363 -11.484 17.851  1.00 27.00  ? 349  LYS A CB    1 
ATOM   2693 C  CG    . LYS A 1 349 ? -18.843 -11.339 19.289  1.00 36.60  ? 349  LYS A CG    1 
ATOM   2694 C  CD    . LYS A 1 349 ? -20.018 -10.363 19.332  1.00 39.73  ? 349  LYS A CD    1 
ATOM   2695 C  CE    . LYS A 1 349 ? -20.729 -10.387 20.652  1.00 44.30  ? 349  LYS A CE    1 
ATOM   2696 N  NZ    . LYS A 1 349 ? -21.849 -9.405  20.634  1.00 58.83  ? 349  LYS A NZ    1 
ATOM   2697 N  N     . THR A 1 350 ? -16.075 -11.737 15.591  1.00 26.07  ? 350  THR A N     1 
ATOM   2698 C  CA    . THR A 1 350 ? -15.903 -11.756 14.148  1.00 25.32  ? 350  THR A CA    1 
ATOM   2699 C  C     . THR A 1 350 ? -15.050 -12.931 13.685  1.00 20.48  ? 350  THR A C     1 
ATOM   2700 O  O     . THR A 1 350 ? -15.266 -13.441 12.584  1.00 21.70  ? 350  THR A O     1 
ATOM   2701 C  CB    . THR A 1 350 ? -15.252 -10.434 13.681  1.00 24.21  ? 350  THR A CB    1 
ATOM   2702 O  OG1   . THR A 1 350 ? -16.092 -9.319  14.024  1.00 26.25  ? 350  THR A OG1   1 
ATOM   2703 C  CG2   . THR A 1 350 ? -15.002 -10.421 12.161  1.00 25.62  ? 350  THR A CG2   1 
ATOM   2704 N  N     . ILE A 1 351 ? -14.052 -13.327 14.475  1.00 19.30  ? 351  ILE A N     1 
ATOM   2705 C  CA    . ILE A 1 351 ? -12.950 -14.140 13.980  1.00 20.81  ? 351  ILE A CA    1 
ATOM   2706 C  C     . ILE A 1 351 ? -13.157 -15.627 14.219  1.00 30.28  ? 351  ILE A C     1 
ATOM   2707 O  O     . ILE A 1 351 ? -12.234 -16.430 14.034  1.00 25.85  ? 351  ILE A O     1 
ATOM   2708 C  CB    . ILE A 1 351 ? -11.626 -13.693 14.625  1.00 25.09  ? 351  ILE A CB    1 
ATOM   2709 C  CG1   . ILE A 1 351 ? -11.696 -13.862 16.141  1.00 24.61  ? 351  ILE A CG1   1 
ATOM   2710 C  CG2   . ILE A 1 351 ? -11.324 -12.217 14.246  1.00 20.76  ? 351  ILE A CG2   1 
ATOM   2711 C  CD1   . ILE A 1 351 ? -10.392 -13.525 16.880  1.00 24.68  ? 351  ILE A CD1   1 
ATOM   2712 N  N     . GLN A 1 352 ? -14.351 -16.018 14.620  1.00 28.05  ? 352  GLN A N     1 
ATOM   2713 C  CA    . GLN A 1 352 ? -14.560 -17.422 14.921  1.00 30.83  ? 352  GLN A CA    1 
ATOM   2714 C  C     . GLN A 1 352 ? -15.093 -18.219 13.748  1.00 30.71  ? 352  GLN A C     1 
ATOM   2715 O  O     . GLN A 1 352 ? -15.406 -19.405 13.915  1.00 29.66  ? 352  GLN A O     1 
ATOM   2716 C  CB    . GLN A 1 352 ? -15.476 -17.553 16.121  1.00 31.65  ? 352  GLN A CB    1 
ATOM   2717 C  CG    . GLN A 1 352 ? -14.687 -17.304 17.369  1.00 36.00  ? 352  GLN A CG    1 
ATOM   2718 C  CD    . GLN A 1 352 ? -15.519 -17.461 18.596  1.00 47.00  ? 352  GLN A CD    1 
ATOM   2719 O  OE1   . GLN A 1 352 ? -16.130 -18.508 18.813  1.00 45.91  ? 352  GLN A OE1   1 
ATOM   2720 N  NE2   . GLN A 1 352 ? -15.555 -16.426 19.415  1.00 38.92  ? 352  GLN A NE2   1 
ATOM   2721 N  N     . LYS A 1 353 ? -15.189 -17.612 12.568  1.00 23.02  ? 353  LYS A N     1 
ATOM   2722 C  CA    . LYS A 1 353 ? -15.417 -18.383 11.361  1.00 26.71  ? 353  LYS A CA    1 
ATOM   2723 C  C     . LYS A 1 353 ? -14.728 -17.718 10.182  1.00 28.02  ? 353  LYS A C     1 
ATOM   2724 O  O     . LYS A 1 353 ? -14.476 -16.507 10.187  1.00 25.05  ? 353  LYS A O     1 
ATOM   2725 C  CB    . LYS A 1 353 ? -16.899 -18.577 11.057  1.00 32.69  ? 353  LYS A CB    1 
ATOM   2726 C  CG    . LYS A 1 353 ? -17.710 -17.345 10.926  1.00 36.62  ? 353  LYS A CG    1 
ATOM   2727 C  CD    . LYS A 1 353 ? -19.193 -17.733 10.756  1.00 42.48  ? 353  LYS A CD    1 
ATOM   2728 C  CE    . LYS A 1 353 ? -20.018 -16.604 10.143  1.00 56.57  ? 353  LYS A CE    1 
ATOM   2729 N  NZ    . LYS A 1 353 ? -21.466 -16.964 10.091  1.00 62.04  ? 353  LYS A NZ    1 
ATOM   2730 N  N     . ASN A 1 354 ? -14.410 -18.540 9.182   1.00 23.94  ? 354  ASN A N     1 
ATOM   2731 C  CA    . ASN A 1 354 ? -13.878 -18.075 7.896   1.00 25.58  ? 354  ASN A CA    1 
ATOM   2732 C  C     . ASN A 1 354 ? -12.666 -17.165 8.058   1.00 19.58  ? 354  ASN A C     1 
ATOM   2733 O  O     . ASN A 1 354 ? -12.468 -16.241 7.277   1.00 22.39  ? 354  ASN A O     1 
ATOM   2734 C  CB    . ASN A 1 354 ? -14.951 -17.370 7.071   1.00 20.92  ? 354  ASN A CB    1 
ATOM   2735 C  CG    . ASN A 1 354 ? -16.178 -18.250 6.837   1.00 32.63  ? 354  ASN A CG    1 
ATOM   2736 O  OD1   . ASN A 1 354 ? -16.054 -19.440 6.595   1.00 32.27  ? 354  ASN A OD1   1 
ATOM   2737 N  ND2   . ASN A 1 354 ? -17.359 -17.659 6.918   1.00 37.74  ? 354  ASN A ND2   1 
ATOM   2738 N  N     . THR A 1 355 ? -11.801 -17.475 9.015   1.00 20.28  ? 355  THR A N     1 
ATOM   2739 C  CA    . THR A 1 355 ? -10.714 -16.566 9.370   1.00 21.95  ? 355  THR A CA    1 
ATOM   2740 C  C     . THR A 1 355 ? -9.377  -17.283 9.317   1.00 24.24  ? 355  THR A C     1 
ATOM   2741 O  O     . THR A 1 355 ? -9.266  -18.403 9.804   1.00 22.42  ? 355  THR A O     1 
ATOM   2742 C  CB    . THR A 1 355 ? -10.958 -16.007 10.780  1.00 23.37  ? 355  THR A CB    1 
ATOM   2743 O  OG1   . THR A 1 355 ? -12.108 -15.167 10.748  1.00 19.04  ? 355  THR A OG1   1 
ATOM   2744 C  CG2   . THR A 1 355 ? -9.765  -15.264 11.308  1.00 23.42  ? 355  THR A CG2   1 
ATOM   2745 N  N     . ILE A 1 356 ? -8.356  -16.629 8.746   1.00 19.85  ? 356  ILE A N     1 
ATOM   2746 C  CA    . ILE A 1 356 ? -6.994  -17.153 8.716   1.00 21.50  ? 356  ILE A CA    1 
ATOM   2747 C  C     . ILE A 1 356 ? -6.166  -16.475 9.797   1.00 20.27  ? 356  ILE A C     1 
ATOM   2748 O  O     . ILE A 1 356 ? -6.080  -15.250 9.833   1.00 22.31  ? 356  ILE A O     1 
ATOM   2749 C  CB    . ILE A 1 356 ? -6.343  -16.939 7.333   1.00 20.63  ? 356  ILE A CB    1 
ATOM   2750 C  CG1   . ILE A 1 356 ? -7.207  -17.566 6.235   1.00 24.76  ? 356  ILE A CG1   1 
ATOM   2751 C  CG2   . ILE A 1 356 ? -4.915  -17.568 7.293   1.00 21.47  ? 356  ILE A CG2   1 
ATOM   2752 C  CD1   . ILE A 1 356 ? -6.565  -17.551 4.850   1.00 27.06  ? 356  ILE A CD1   1 
ATOM   2753 N  N     . PHE A 1 357 ? -5.508  -17.262 10.644  1.00 19.80  ? 357  PHE A N     1 
ATOM   2754 C  CA    . PHE A 1 357 ? -4.599  -16.743 11.655  1.00 21.34  ? 357  PHE A CA    1 
ATOM   2755 C  C     . PHE A 1 357 ? -3.170  -17.042 11.247  1.00 24.58  ? 357  PHE A C     1 
ATOM   2756 O  O     . PHE A 1 357 ? -2.893  -18.116 10.705  1.00 24.13  ? 357  PHE A O     1 
ATOM   2757 C  CB    . PHE A 1 357 ? -4.854  -17.373 13.033  1.00 20.25  ? 357  PHE A CB    1 
ATOM   2758 C  CG    . PHE A 1 357 ? -6.235  -17.152 13.557  1.00 22.41  ? 357  PHE A CG    1 
ATOM   2759 C  CD1   . PHE A 1 357 ? -7.274  -17.970 13.144  1.00 21.03  ? 357  PHE A CD1   1 
ATOM   2760 C  CD2   . PHE A 1 357 ? -6.507  -16.117 14.468  1.00 20.58  ? 357  PHE A CD2   1 
ATOM   2761 C  CE1   . PHE A 1 357 ? -8.571  -17.781 13.628  1.00 25.32  ? 357  PHE A CE1   1 
ATOM   2762 C  CE2   . PHE A 1 357 ? -7.801  -15.925 14.969  1.00 22.68  ? 357  PHE A CE2   1 
ATOM   2763 C  CZ    . PHE A 1 357 ? -8.838  -16.758 14.538  1.00 22.14  ? 357  PHE A CZ    1 
ATOM   2764 N  N     . THR A 1 358 ? -2.253  -16.115 11.551  1.00 19.64  ? 358  THR A N     1 
ATOM   2765 C  CA    . THR A 1 358 ? -0.839  -16.307 11.260  1.00 18.74  ? 358  THR A CA    1 
ATOM   2766 C  C     . THR A 1 358 ? -0.025  -16.056 12.520  1.00 19.97  ? 358  THR A C     1 
ATOM   2767 O  O     . THR A 1 358 ? -0.109  -14.974 13.109  1.00 25.06  ? 358  THR A O     1 
ATOM   2768 C  CB    . THR A 1 358 ? -0.358  -15.357 10.135  1.00 16.35  ? 358  THR A CB    1 
ATOM   2769 O  OG1   . THR A 1 358 ? -1.156  -15.563 8.957   1.00 20.77  ? 358  THR A OG1   1 
ATOM   2770 C  CG2   . THR A 1 358 ? 1.040   -15.664 9.805   1.00 20.15  ? 358  THR A CG2   1 
ATOM   2771 N  N     . ASN A 1 359 ? 0.775   -17.041 12.908  1.00 21.46  ? 359  ASN A N     1 
ATOM   2772 C  CA    . ASN A 1 359 ? 1.756   -16.958 13.999  1.00 21.14  ? 359  ASN A CA    1 
ATOM   2773 C  C     . ASN A 1 359 ? 1.139   -16.822 15.397  1.00 23.55  ? 359  ASN A C     1 
ATOM   2774 O  O     . ASN A 1 359 ? 1.802   -16.349 16.323  1.00 27.70  ? 359  ASN A O     1 
ATOM   2775 C  CB    . ASN A 1 359 ? 2.790   -15.855 13.725  1.00 24.95  ? 359  ASN A CB    1 
ATOM   2776 C  CG    . ASN A 1 359 ? 3.739   -16.260 12.609  1.00 24.97  ? 359  ASN A CG    1 
ATOM   2777 O  OD1   . ASN A 1 359 ? 3.817   -17.456 12.278  1.00 24.00  ? 359  ASN A OD1   1 
ATOM   2778 N  ND2   . ASN A 1 359 ? 4.447   -15.292 12.010  1.00 23.38  ? 359  ASN A ND2   1 
ATOM   2779 N  N     . VAL A 1 360 ? -0.084  -17.295 15.606  1.00 21.54  ? 360  VAL A N     1 
ATOM   2780 C  CA    . VAL A 1 360 ? -0.650  -17.401 16.957  1.00 22.71  ? 360  VAL A CA    1 
ATOM   2781 C  C     . VAL A 1 360 ? -0.415  -18.821 17.455  1.00 27.24  ? 360  VAL A C     1 
ATOM   2782 O  O     . VAL A 1 360 ? 0.032   -19.698 16.715  1.00 23.64  ? 360  VAL A O     1 
ATOM   2783 C  CB    . VAL A 1 360 ? -2.158  -17.007 17.016  1.00 23.33  ? 360  VAL A CB    1 
ATOM   2784 C  CG1   . VAL A 1 360 ? -2.372  -15.585 16.546  1.00 20.40  ? 360  VAL A CG1   1 
ATOM   2785 C  CG2   . VAL A 1 360 ? -3.015  -17.959 16.196  1.00 22.93  ? 360  VAL A CG2   1 
ATOM   2786 N  N     . ALA A 1 361 ? -0.696  -19.056 18.734  1.00 28.46  ? 361  ALA A N     1 
ATOM   2787 C  CA    . ALA A 1 361 ? -0.571  -20.400 19.294  1.00 27.25  ? 361  ALA A CA    1 
ATOM   2788 C  C     . ALA A 1 361 ? -1.839  -21.199 19.054  1.00 25.32  ? 361  ALA A C     1 
ATOM   2789 O  O     . ALA A 1 361 ? -2.932  -20.646 18.921  1.00 24.81  ? 361  ALA A O     1 
ATOM   2790 C  CB    . ALA A 1 361 ? -0.266  -20.364 20.795  1.00 26.50  ? 361  ALA A CB    1 
ATOM   2791 N  N     . GLU A 1 362 ? -1.689  -22.523 19.030  1.00 31.27  ? 362  GLU A N     1 
ATOM   2792 C  CA    . GLU A 1 362 ? -2.808  -23.442 18.843  1.00 31.48  ? 362  GLU A CA    1 
ATOM   2793 C  C     . GLU A 1 362 ? -3.043  -24.246 20.120  1.00 28.97  ? 362  GLU A C     1 
ATOM   2794 O  O     . GLU A 1 362 ? -2.091  -24.772 20.713  1.00 29.62  ? 362  GLU A O     1 
ATOM   2795 C  CB    . GLU A 1 362 ? -2.543  -24.389 17.666  1.00 31.38  ? 362  GLU A CB    1 
ATOM   2796 C  CG    . GLU A 1 362 ? -3.684  -25.378 17.397  1.00 32.00  ? 362  GLU A CG    1 
ATOM   2797 C  CD    . GLU A 1 362 ? -3.354  -26.370 16.280  1.00 38.77  ? 362  GLU A CD    1 
ATOM   2798 O  OE1   . GLU A 1 362 ? -2.272  -26.239 15.669  1.00 35.97  ? 362  GLU A OE1   1 
ATOM   2799 O  OE2   . GLU A 1 362 ? -4.170  -27.288 16.031  1.00 40.63  ? 362  GLU A OE2   1 
ATOM   2800 N  N     . THR A 1 363 ? -4.297  -24.336 20.547  1.00 29.07  ? 363  THR A N     1 
ATOM   2801 C  CA    . THR A 1 363 ? -4.611  -25.220 21.666  1.00 30.84  ? 363  THR A CA    1 
ATOM   2802 C  C     . THR A 1 363 ? -4.885  -26.654 21.185  1.00 35.54  ? 363  THR A C     1 
ATOM   2803 O  O     . THR A 1 363 ? -5.316  -26.887 20.055  1.00 33.60  ? 363  THR A O     1 
ATOM   2804 C  CB    . THR A 1 363 ? -5.811  -24.721 22.443  1.00 23.65  ? 363  THR A CB    1 
ATOM   2805 O  OG1   . THR A 1 363 ? -6.949  -24.682 21.573  1.00 31.08  ? 363  THR A OG1   1 
ATOM   2806 C  CG2   . THR A 1 363 ? -5.562  -23.326 23.021  1.00 26.86  ? 363  THR A CG2   1 
ATOM   2807 N  N     . SER A 1 364 ? -4.689  -27.623 22.092  1.00 36.63  ? 364  SER A N     1 
ATOM   2808 C  CA    . SER A 1 364 ? -4.824  -29.033 21.714  1.00 31.40  ? 364  SER A CA    1 
ATOM   2809 C  C     . SER A 1 364 ? -6.233  -29.387 21.250  1.00 33.04  ? 364  SER A C     1 
ATOM   2810 O  O     . SER A 1 364 ? -6.405  -30.364 20.520  1.00 35.52  ? 364  SER A O     1 
ATOM   2811 C  CB    . SER A 1 364 ? -4.430  -29.928 22.883  1.00 28.41  ? 364  SER A CB    1 
ATOM   2812 O  OG    . SER A 1 364 ? -5.188  -29.589 24.022  1.00 31.92  ? 364  SER A OG    1 
ATOM   2813 N  N     . ASP A 1 365 ? -7.247  -28.615 21.629  1.00 31.95  ? 365  ASP A N     1 
ATOM   2814 C  CA    . ASP A 1 365 ? -8.594  -28.872 21.150  1.00 25.39  ? 365  ASP A CA    1 
ATOM   2815 C  C     . ASP A 1 365 ? -8.927  -28.110 19.867  1.00 31.49  ? 365  ASP A C     1 
ATOM   2816 O  O     . ASP A 1 365 ? -10.109 -27.988 19.524  1.00 29.98  ? 365  ASP A O     1 
ATOM   2817 C  CB    . ASP A 1 365 ? -9.618  -28.570 22.249  1.00 34.05  ? 365  ASP A CB    1 
ATOM   2818 C  CG    . ASP A 1 365 ? -9.554  -27.145 22.746  1.00 37.96  ? 365  ASP A CG    1 
ATOM   2819 O  OD1   . ASP A 1 365 ? -8.577  -26.426 22.422  1.00 35.27  ? 365  ASP A OD1   1 
ATOM   2820 O  OD2   . ASP A 1 365 ? -10.495 -26.748 23.460  1.00 34.03  ? 365  ASP A OD2   1 
ATOM   2821 N  N     . GLY A 1 366 ? -7.918  -27.613 19.149  1.00 28.03  ? 366  GLY A N     1 
ATOM   2822 C  CA    . GLY A 1 366 ? -8.145  -26.970 17.873  1.00 32.07  ? 366  GLY A CA    1 
ATOM   2823 C  C     . GLY A 1 366 ? -8.449  -25.488 17.925  1.00 38.96  ? 366  GLY A C     1 
ATOM   2824 O  O     . GLY A 1 366 ? -8.990  -24.958 16.947  1.00 33.84  ? 366  GLY A O     1 
ATOM   2825 N  N     . GLY A 1 367 ? -8.146  -24.806 19.037  1.00 32.48  ? 367  GLY A N     1 
ATOM   2826 C  CA    . GLY A 1 367 ? -8.412  -23.390 19.180  1.00 28.64  ? 367  GLY A CA    1 
ATOM   2827 C  C     . GLY A 1 367 ? -7.161  -22.540 19.013  1.00 25.09  ? 367  GLY A C     1 
ATOM   2828 O  O     . GLY A 1 367 ? -6.106  -23.006 18.577  1.00 22.96  ? 367  GLY A O     1 
ATOM   2829 N  N     . VAL A 1 368 ? -7.301  -21.251 19.356  1.00 31.17  ? 368  VAL A N     1 
ATOM   2830 C  CA    . VAL A 1 368 ? -6.235  -20.252 19.184  1.00 27.51  ? 368  VAL A CA    1 
ATOM   2831 C  C     . VAL A 1 368 ? -5.896  -19.650 20.541  1.00 31.95  ? 368  VAL A C     1 
ATOM   2832 O  O     . VAL A 1 368 ? -6.765  -19.502 21.414  1.00 25.76  ? 368  VAL A O     1 
ATOM   2833 C  CB    . VAL A 1 368 ? -6.594  -19.111 18.188  1.00 25.24  ? 368  VAL A CB    1 
ATOM   2834 C  CG1   . VAL A 1 368 ? -6.688  -19.613 16.769  1.00 22.86  ? 368  VAL A CG1   1 
ATOM   2835 C  CG2   . VAL A 1 368 ? -7.870  -18.429 18.586  1.00 22.47  ? 368  VAL A CG2   1 
ATOM   2836 N  N     . TYR A 1 369 ? -4.619  -19.312 20.725  1.00 26.17  ? 369  TYR A N     1 
ATOM   2837 C  CA    . TYR A 1 369 ? -4.195  -18.652 21.953  1.00 29.04  ? 369  TYR A CA    1 
ATOM   2838 C  C     . TYR A 1 369 ? -3.167  -17.562 21.657  1.00 24.27  ? 369  TYR A C     1 
ATOM   2839 O  O     . TYR A 1 369 ? -2.436  -17.616 20.661  1.00 23.91  ? 369  TYR A O     1 
ATOM   2840 C  CB    . TYR A 1 369 ? -3.616  -19.643 22.965  1.00 26.95  ? 369  TYR A CB    1 
ATOM   2841 C  CG    . TYR A 1 369 ? -4.042  -19.334 24.393  1.00 25.00  ? 369  TYR A CG    1 
ATOM   2842 C  CD1   . TYR A 1 369 ? -5.373  -19.359 24.755  1.00 27.64  ? 369  TYR A CD1   1 
ATOM   2843 C  CD2   . TYR A 1 369 ? -3.107  -19.034 25.367  1.00 28.48  ? 369  TYR A CD2   1 
ATOM   2844 C  CE1   . TYR A 1 369 ? -5.766  -19.089 26.046  1.00 36.16  ? 369  TYR A CE1   1 
ATOM   2845 C  CE2   . TYR A 1 369 ? -3.493  -18.775 26.667  1.00 26.09  ? 369  TYR A CE2   1 
ATOM   2846 C  CZ    . TYR A 1 369 ? -4.812  -18.798 26.999  1.00 34.09  ? 369  TYR A CZ    1 
ATOM   2847 O  OH    . TYR A 1 369 ? -5.193  -18.525 28.298  1.00 38.96  ? 369  TYR A OH    1 
ATOM   2848 N  N     . TRP A 1 370 ? -3.103  -16.583 22.557  1.00 26.16  ? 370  TRP A N     1 
ATOM   2849 C  CA    . TRP A 1 370 ? -2.129  -15.493 22.449  1.00 22.89  ? 370  TRP A CA    1 
ATOM   2850 C  C     . TRP A 1 370 ? -2.067  -14.744 23.772  1.00 29.10  ? 370  TRP A C     1 
ATOM   2851 O  O     . TRP A 1 370 ? -2.980  -14.833 24.596  1.00 24.26  ? 370  TRP A O     1 
ATOM   2852 C  CB    . TRP A 1 370 ? -2.458  -14.512 21.312  1.00 20.58  ? 370  TRP A CB    1 
ATOM   2853 C  CG    . TRP A 1 370 ? -3.827  -14.014 21.255  1.00 18.88  ? 370  TRP A CG    1 
ATOM   2854 C  CD1   . TRP A 1 370 ? -4.398  -13.092 22.091  1.00 18.44  ? 370  TRP A CD1   1 
ATOM   2855 C  CD2   . TRP A 1 370 ? -4.828  -14.334 20.271  1.00 18.22  ? 370  TRP A CD2   1 
ATOM   2856 N  NE1   . TRP A 1 370 ? -5.689  -12.834 21.700  1.00 21.26  ? 370  TRP A NE1   1 
ATOM   2857 C  CE2   . TRP A 1 370 ? -5.979  -13.584 20.587  1.00 19.05  ? 370  TRP A CE2   1 
ATOM   2858 C  CE3   . TRP A 1 370 ? -4.866  -15.196 19.168  1.00 18.80  ? 370  TRP A CE3   1 
ATOM   2859 C  CZ2   . TRP A 1 370 ? -7.163  -13.668 19.832  1.00 17.62  ? 370  TRP A CZ2   1 
ATOM   2860 C  CZ3   . TRP A 1 370 ? -6.031  -15.284 18.421  1.00 19.89  ? 370  TRP A CZ3   1 
ATOM   2861 C  CH2   . TRP A 1 370 ? -7.164  -14.528 18.752  1.00 18.90  ? 370  TRP A CH2   1 
ATOM   2862 N  N     . GLU A 1 371 ? -0.965  -14.018 23.965  1.00 30.97  ? 371  GLU A N     1 
ATOM   2863 C  CA    . GLU A 1 371 ? -0.830  -13.164 25.136  1.00 34.36  ? 371  GLU A CA    1 
ATOM   2864 C  C     . GLU A 1 371 ? -2.008  -12.203 25.211  1.00 28.43  ? 371  GLU A C     1 
ATOM   2865 O  O     . GLU A 1 371 ? -2.473  -11.694 24.189  1.00 30.89  ? 371  GLU A O     1 
ATOM   2866 C  CB    . GLU A 1 371 ? 0.492   -12.401 25.074  1.00 31.27  ? 371  GLU A CB    1 
ATOM   2867 C  CG    . GLU A 1 371 ? 1.722   -13.204 25.525  1.00 33.99  ? 371  GLU A CG    1 
ATOM   2868 C  CD    . GLU A 1 371 ? 2.025   -14.451 24.679  1.00 40.91  ? 371  GLU A CD    1 
ATOM   2869 O  OE1   . GLU A 1 371 ? 1.775   -14.463 23.445  1.00 31.43  ? 371  GLU A OE1   1 
ATOM   2870 O  OE2   . GLU A 1 371 ? 2.529   -15.424 25.277  1.00 35.55  ? 371  GLU A OE2   1 
ATOM   2871 N  N     . GLY A 1 372 ? -2.548  -12.021 26.418  1.00 28.86  ? 372  GLY A N     1 
ATOM   2872 C  CA    . GLY A 1 372 ? -3.605  -11.047 26.644  1.00 26.64  ? 372  GLY A CA    1 
ATOM   2873 C  C     . GLY A 1 372 ? -4.983  -11.486 26.220  1.00 26.12  ? 372  GLY A C     1 
ATOM   2874 O  O     . GLY A 1 372 ? -5.927  -10.693 26.294  1.00 33.17  ? 372  GLY A O     1 
ATOM   2875 N  N     . ILE A 1 373 ? -5.143  -12.739 25.800  1.00 28.19  ? 373  ILE A N     1 
ATOM   2876 C  CA    . ILE A 1 373 ? -6.468  -13.242 25.459  1.00 25.27  ? 373  ILE A CA    1 
ATOM   2877 C  C     . ILE A 1 373 ? -7.396  -13.287 26.681  1.00 26.06  ? 373  ILE A C     1 
ATOM   2878 O  O     . ILE A 1 373 ? -8.628  -13.305 26.530  1.00 26.02  ? 373  ILE A O     1 
ATOM   2879 C  CB    . ILE A 1 373 ? -6.272  -14.622 24.802  1.00 25.74  ? 373  ILE A CB    1 
ATOM   2880 C  CG1   . ILE A 1 373 ? -7.552  -15.110 24.130  1.00 25.97  ? 373  ILE A CG1   1 
ATOM   2881 C  CG2   . ILE A 1 373 ? -5.727  -15.616 25.827  1.00 23.01  ? 373  ILE A CG2   1 
ATOM   2882 C  CD1   . ILE A 1 373 ? -7.291  -16.307 23.228  1.00 29.54  ? 373  ILE A CD1   1 
ATOM   2883 N  N     . ASP A 1 374 ? -6.833  -13.313 27.889  1.00 30.29  ? 374  ASP A N     1 
ATOM   2884 C  CA    . ASP A 1 374 ? -7.613  -13.143 29.125  1.00 33.91  ? 374  ASP A CA    1 
ATOM   2885 C  C     . ASP A 1 374 ? -8.659  -14.241 29.287  1.00 35.82  ? 374  ASP A C     1 
ATOM   2886 O  O     . ASP A 1 374 ? -9.766  -14.006 29.767  1.00 38.63  ? 374  ASP A O     1 
ATOM   2887 C  CB    . ASP A 1 374 ? -8.289  -11.776 29.159  1.00 37.53  ? 374  ASP A CB    1 
ATOM   2888 C  CG    . ASP A 1 374 ? -8.174  -11.120 30.495  1.00 48.53  ? 374  ASP A CG    1 
ATOM   2889 O  OD1   . ASP A 1 374 ? -8.100  -11.857 31.507  1.00 44.00  ? 374  ASP A OD1   1 
ATOM   2890 O  OD2   . ASP A 1 374 ? -8.131  -9.872  30.523  1.00 55.64  ? 374  ASP A OD2   1 
ATOM   2891 N  N     . GLU A 1 375 ? -8.326  -15.429 28.858  1.00 36.02  ? 375  GLU A N     1 
ATOM   2892 C  CA    . GLU A 1 375 ? -9.365  -16.436 28.819  1.00 38.45  ? 375  GLU A CA    1 
ATOM   2893 C  C     . GLU A 1 375 ? -8.772  -17.749 29.292  1.00 40.25  ? 375  GLU A C     1 
ATOM   2894 O  O     . GLU A 1 375 ? -7.827  -18.257 28.679  1.00 37.51  ? 375  GLU A O     1 
ATOM   2895 C  CB    . GLU A 1 375 ? -9.935  -16.546 27.410  1.00 37.00  ? 375  GLU A CB    1 
ATOM   2896 C  CG    . GLU A 1 375 ? -11.115 -17.446 27.306  1.00 48.54  ? 375  GLU A CG    1 
ATOM   2897 C  CD    . GLU A 1 375 ? -11.874 -17.208 26.038  1.00 43.68  ? 375  GLU A CD    1 
ATOM   2898 O  OE1   . GLU A 1 375 ? -11.621 -16.177 25.386  1.00 45.39  ? 375  GLU A OE1   1 
ATOM   2899 O  OE2   . GLU A 1 375 ? -12.724 -18.043 25.697  1.00 49.23  ? 375  GLU A OE2   1 
ATOM   2900 N  N     . PRO A 1 376 ? -9.277  -18.306 30.394  1.00 42.48  ? 376  PRO A N     1 
ATOM   2901 C  CA    . PRO A 1 376 ? -8.687  -19.532 30.937  1.00 42.80  ? 376  PRO A CA    1 
ATOM   2902 C  C     . PRO A 1 376 ? -9.008  -20.726 30.061  1.00 36.39  ? 376  PRO A C     1 
ATOM   2903 O  O     . PRO A 1 376 ? -10.051 -20.787 29.405  1.00 38.91  ? 376  PRO A O     1 
ATOM   2904 C  CB    . PRO A 1 376 ? -9.342  -19.667 32.317  1.00 41.52  ? 376  PRO A CB    1 
ATOM   2905 C  CG    . PRO A 1 376 ? -9.994  -18.354 32.588  1.00 51.64  ? 376  PRO A CG    1 
ATOM   2906 C  CD    . PRO A 1 376 ? -10.346 -17.780 31.255  1.00 47.71  ? 376  PRO A CD    1 
ATOM   2907 N  N     . LEU A 1 377 ? -8.088  -21.674 30.052  1.00 36.51  ? 377  LEU A N     1 
ATOM   2908 C  CA    . LEU A 1 377 ? -8.252  -22.906 29.298  1.00 42.70  ? 377  LEU A CA    1 
ATOM   2909 C  C     . LEU A 1 377 ? -8.719  -24.038 30.219  1.00 40.63  ? 377  LEU A C     1 
ATOM   2910 O  O     . LEU A 1 377 ? -8.417  -24.047 31.410  1.00 40.96  ? 377  LEU A O     1 
ATOM   2911 C  CB    . LEU A 1 377 ? -6.939  -23.273 28.613  1.00 38.36  ? 377  LEU A CB    1 
ATOM   2912 C  CG    . LEU A 1 377 ? -6.554  -22.336 27.467  1.00 34.18  ? 377  LEU A CG    1 
ATOM   2913 C  CD1   . LEU A 1 377 ? -5.237  -22.742 26.875  1.00 32.36  ? 377  LEU A CD1   1 
ATOM   2914 C  CD2   . LEU A 1 377 ? -7.642  -22.340 26.412  1.00 36.49  ? 377  LEU A CD2   1 
ATOM   2915 N  N     . ALA A 1 378 ? -9.454  -24.997 29.649  1.00 39.03  ? 378  ALA A N     1 
ATOM   2916 C  CA    . ALA A 1 378 ? -9.952  -26.133 30.414  1.00 44.93  ? 378  ALA A CA    1 
ATOM   2917 C  C     . ALA A 1 378 ? -8.803  -27.001 30.914  1.00 36.09  ? 378  ALA A C     1 
ATOM   2918 O  O     . ALA A 1 378 ? -7.726  -27.033 30.313  1.00 35.60  ? 378  ALA A O     1 
ATOM   2919 C  CB    . ALA A 1 378 ? -10.902 -26.983 29.568  1.00 36.71  ? 378  ALA A CB    1 
ATOM   2920 N  N     . PRO A 1 379 ? -9.011  -27.724 32.017  1.00 46.27  ? 379  PRO A N     1 
ATOM   2921 C  CA    . PRO A 1 379 ? -8.016  -28.715 32.441  1.00 42.68  ? 379  PRO A CA    1 
ATOM   2922 C  C     . PRO A 1 379 ? -7.714  -29.690 31.318  1.00 29.35  ? 379  PRO A C     1 
ATOM   2923 O  O     . PRO A 1 379 ? -8.605  -30.104 30.573  1.00 37.15  ? 379  PRO A O     1 
ATOM   2924 C  CB    . PRO A 1 379 ? -8.698  -29.413 33.626  1.00 44.29  ? 379  PRO A CB    1 
ATOM   2925 C  CG    . PRO A 1 379 ? -9.630  -28.413 34.153  1.00 42.90  ? 379  PRO A CG    1 
ATOM   2926 C  CD    . PRO A 1 379 ? -10.148 -27.667 32.956  1.00 44.73  ? 379  PRO A CD    1 
ATOM   2927 N  N     . GLY A 1 380 ? -6.435  -30.021 31.169  1.00 27.62  ? 380  GLY A N     1 
ATOM   2928 C  CA    . GLY A 1 380 ? -6.003  -30.894 30.111  1.00 26.13  ? 380  GLY A CA    1 
ATOM   2929 C  C     . GLY A 1 380 ? -5.644  -30.215 28.799  1.00 36.43  ? 380  GLY A C     1 
ATOM   2930 O  O     . GLY A 1 380 ? -4.953  -30.826 27.977  1.00 32.53  ? 380  GLY A O     1 
ATOM   2931 N  N     . VAL A 1 381 ? -6.112  -28.989 28.557  1.00 36.43  ? 381  VAL A N     1 
ATOM   2932 C  CA    . VAL A 1 381 ? -5.838  -28.344 27.272  1.00 35.41  ? 381  VAL A CA    1 
ATOM   2933 C  C     . VAL A 1 381 ? -4.413  -27.815 27.265  1.00 32.35  ? 381  VAL A C     1 
ATOM   2934 O  O     . VAL A 1 381 ? -4.000  -27.103 28.185  1.00 39.21  ? 381  VAL A O     1 
ATOM   2935 C  CB    . VAL A 1 381 ? -6.851  -27.226 26.998  1.00 35.96  ? 381  VAL A CB    1 
ATOM   2936 C  CG1   . VAL A 1 381 ? -6.347  -26.293 25.867  1.00 26.96  ? 381  VAL A CG1   1 
ATOM   2937 C  CG2   . VAL A 1 381 ? -8.205  -27.832 26.646  1.00 28.52  ? 381  VAL A CG2   1 
ATOM   2938 N  N     . THR A 1 382 ? -3.657  -28.160 26.233  1.00 33.02  ? 382  THR A N     1 
ATOM   2939 C  CA    . THR A 1 382 ? -2.267  -27.745 26.103  1.00 34.55  ? 382  THR A CA    1 
ATOM   2940 C  C     . THR A 1 382 ? -2.102  -26.787 24.923  1.00 30.16  ? 382  THR A C     1 
ATOM   2941 O  O     . THR A 1 382 ? -2.980  -26.649 24.072  1.00 29.69  ? 382  THR A O     1 
ATOM   2942 C  CB    . THR A 1 382 ? -1.353  -28.962 25.927  1.00 32.78  ? 382  THR A CB    1 
ATOM   2943 O  OG1   . THR A 1 382 ? -1.779  -29.708 24.784  1.00 37.84  ? 382  THR A OG1   1 
ATOM   2944 C  CG2   . THR A 1 382 ? -1.413  -29.844 27.168  1.00 37.19  ? 382  THR A CG2   1 
ATOM   2945 N  N     . ILE A 1 383 ? -0.942  -26.147 24.861  1.00 30.41  ? 383  ILE A N     1 
ATOM   2946 C  CA    . ILE A 1 383 ? -0.696  -25.070 23.897  1.00 30.89  ? 383  ILE A CA    1 
ATOM   2947 C  C     . ILE A 1 383 ? 0.543   -25.407 23.072  1.00 32.86  ? 383  ILE A C     1 
ATOM   2948 O  O     . ILE A 1 383 ? 1.592   -25.770 23.623  1.00 36.81  ? 383  ILE A O     1 
ATOM   2949 C  CB    . ILE A 1 383 ? -0.545  -23.710 24.607  1.00 35.96  ? 383  ILE A CB    1 
ATOM   2950 C  CG1   . ILE A 1 383 ? -1.849  -23.334 25.300  1.00 33.45  ? 383  ILE A CG1   1 
ATOM   2951 C  CG2   . ILE A 1 383 ? -0.161  -22.610 23.623  1.00 34.43  ? 383  ILE A CG2   1 
ATOM   2952 C  CD1   . ILE A 1 383 ? -1.697  -22.246 26.326  1.00 42.92  ? 383  ILE A CD1   1 
ATOM   2953 N  N     . THR A 1 384 ? 0.414   -25.313 21.748  1.00 33.65  ? 384  THR A N     1 
ATOM   2954 C  CA    . THR A 1 384 ? 1.557   -25.322 20.840  1.00 33.41  ? 384  THR A CA    1 
ATOM   2955 C  C     . THR A 1 384 ? 1.825   -23.888 20.401  1.00 32.47  ? 384  THR A C     1 
ATOM   2956 O  O     . THR A 1 384 ? 0.936   -23.237 19.844  1.00 29.14  ? 384  THR A O     1 
ATOM   2957 C  CB    . THR A 1 384 ? 1.301   -26.191 19.609  1.00 29.62  ? 384  THR A CB    1 
ATOM   2958 O  OG1   . THR A 1 384 ? 1.001   -27.527 20.012  1.00 33.62  ? 384  THR A OG1   1 
ATOM   2959 C  CG2   . THR A 1 384 ? 2.541   -26.191 18.700  1.00 32.44  ? 384  THR A CG2   1 
ATOM   2960 N  N     . SER A 1 385 ? 3.045   -23.416 20.636  1.00 30.82  ? 385  SER A N     1 
ATOM   2961 C  CA    . SER A 1 385 ? 3.413   -22.039 20.326  1.00 37.09  ? 385  SER A CA    1 
ATOM   2962 C  C     . SER A 1 385 ? 3.505   -21.826 18.817  1.00 30.88  ? 385  SER A C     1 
ATOM   2963 O  O     . SER A 1 385 ? 3.478   -22.762 18.017  1.00 29.07  ? 385  SER A O     1 
ATOM   2964 C  CB    . SER A 1 385 ? 4.751   -21.682 20.969  1.00 34.24  ? 385  SER A CB    1 
ATOM   2965 O  OG    . SER A 1 385 ? 5.816   -22.234 20.217  1.00 34.18  ? 385  SER A OG    1 
ATOM   2966 N  N     . TRP A 1 386 ? 3.631   -20.554 18.427  1.00 33.86  ? 386  TRP A N     1 
ATOM   2967 C  CA    . TRP A 1 386 ? 3.845   -20.242 17.018  1.00 30.84  ? 386  TRP A CA    1 
ATOM   2968 C  C     . TRP A 1 386 ? 5.178   -20.773 16.500  1.00 34.84  ? 386  TRP A C     1 
ATOM   2969 O  O     . TRP A 1 386 ? 5.379   -20.833 15.280  1.00 34.24  ? 386  TRP A O     1 
ATOM   2970 C  CB    . TRP A 1 386 ? 3.762   -18.731 16.804  1.00 30.91  ? 386  TRP A CB    1 
ATOM   2971 C  CG    . TRP A 1 386 ? 4.986   -18.021 17.237  1.00 31.94  ? 386  TRP A CG    1 
ATOM   2972 C  CD1   . TRP A 1 386 ? 5.377   -17.744 18.514  1.00 32.65  ? 386  TRP A CD1   1 
ATOM   2973 C  CD2   . TRP A 1 386 ? 5.987   -17.476 16.379  1.00 30.68  ? 386  TRP A CD2   1 
ATOM   2974 N  NE1   . TRP A 1 386 ? 6.574   -17.058 18.503  1.00 35.07  ? 386  TRP A NE1   1 
ATOM   2975 C  CE2   . TRP A 1 386 ? 6.970   -16.890 17.201  1.00 36.07  ? 386  TRP A CE2   1 
ATOM   2976 C  CE3   . TRP A 1 386 ? 6.152   -17.437 14.992  1.00 32.01  ? 386  TRP A CE3   1 
ATOM   2977 C  CZ2   . TRP A 1 386 ? 8.103   -16.265 16.679  1.00 33.78  ? 386  TRP A CZ2   1 
ATOM   2978 C  CZ3   . TRP A 1 386 ? 7.276   -16.816 14.479  1.00 33.09  ? 386  TRP A CZ3   1 
ATOM   2979 C  CH2   . TRP A 1 386 ? 8.235   -16.240 15.321  1.00 33.41  ? 386  TRP A CH2   1 
ATOM   2980 N  N     . LYS A 1 387 ? 6.102   -21.145 17.383  1.00 32.96  ? 387  LYS A N     1 
ATOM   2981 C  CA    . LYS A 1 387 ? 7.312   -21.808 16.906  1.00 35.62  ? 387  LYS A CA    1 
ATOM   2982 C  C     . LYS A 1 387 ? 7.121   -23.316 16.747  1.00 43.77  ? 387  LYS A C     1 
ATOM   2983 O  O     . LYS A 1 387 ? 8.105   -24.044 16.568  1.00 42.60  ? 387  LYS A O     1 
ATOM   2984 C  CB    . LYS A 1 387 ? 8.478   -21.518 17.847  1.00 40.32  ? 387  LYS A CB    1 
ATOM   2985 C  CG    . LYS A 1 387 ? 8.980   -20.086 17.777  1.00 44.12  ? 387  LYS A CG    1 
ATOM   2986 C  CD    . LYS A 1 387 ? 10.145  -19.893 18.729  1.00 50.78  ? 387  LYS A CD    1 
ATOM   2987 C  CE    . LYS A 1 387 ? 10.676  -18.477 18.685  1.00 52.28  ? 387  LYS A CE    1 
ATOM   2988 N  NZ    . LYS A 1 387 ? 11.169  -18.160 17.312  1.00 56.07  ? 387  LYS A NZ    1 
ATOM   2989 N  N     . ASN A 1 388 ? 5.869   -23.781 16.811  1.00 40.93  ? 388  ASN A N     1 
ATOM   2990 C  CA    . ASN A 1 388 ? 5.519   -25.190 16.661  1.00 44.69  ? 388  ASN A CA    1 
ATOM   2991 C  C     . ASN A 1 388 ? 6.141   -26.019 17.782  1.00 45.85  ? 388  ASN A C     1 
ATOM   2992 O  O     . ASN A 1 388 ? 6.756   -27.055 17.550  1.00 44.72  ? 388  ASN A O     1 
ATOM   2993 C  CB    . ASN A 1 388 ? 5.927   -25.711 15.281  1.00 41.42  ? 388  ASN A CB    1 
ATOM   2994 C  CG    . ASN A 1 388 ? 5.120   -26.898 14.859  1.00 50.56  ? 388  ASN A CG    1 
ATOM   2995 O  OD1   . ASN A 1 388 ? 3.957   -27.035 15.238  1.00 47.72  ? 388  ASN A OD1   1 
ATOM   2996 N  ND2   . ASN A 1 388 ? 5.734   -27.785 14.084  1.00 55.03  ? 388  ASN A ND2   1 
ATOM   2997 N  N     . LYS A 1 389 ? 5.978   -25.547 19.017  1.00 41.64  ? 389  LYS A N     1 
ATOM   2998 C  CA    . LYS A 1 389 ? 6.651   -26.146 20.159  1.00 43.59  ? 389  LYS A CA    1 
ATOM   2999 C  C     . LYS A 1 389 ? 5.701   -26.188 21.338  1.00 45.87  ? 389  LYS A C     1 
ATOM   3000 O  O     . LYS A 1 389 ? 4.891   -25.277 21.532  1.00 42.19  ? 389  LYS A O     1 
ATOM   3001 C  CB    . LYS A 1 389 ? 7.918   -25.363 20.566  1.00 44.34  ? 389  LYS A CB    1 
ATOM   3002 C  CG    . LYS A 1 389 ? 9.032   -25.356 19.534  1.00 54.56  ? 389  LYS A CG    1 
ATOM   3003 C  CD    . LYS A 1 389 ? 10.264  -24.599 20.042  1.00 63.31  ? 389  LYS A CD    1 
ATOM   3004 C  CE    . LYS A 1 389 ? 11.380  -24.578 18.996  1.00 60.56  ? 389  LYS A CE    1 
ATOM   3005 N  NZ    . LYS A 1 389 ? 12.567  -23.774 19.423  1.00 68.99  ? 389  LYS A NZ    1 
ATOM   3006 N  N     . GLU A 1 390 ? 5.824   -27.246 22.139  1.00 46.90  ? 390  GLU A N     1 
ATOM   3007 C  CA    . GLU A 1 390 ? 5.054   -27.337 23.371  1.00 51.99  ? 390  GLU A CA    1 
ATOM   3008 C  C     . GLU A 1 390 ? 5.420   -26.178 24.283  1.00 49.18  ? 390  GLU A C     1 
ATOM   3009 O  O     . GLU A 1 390 ? 6.603   -25.914 24.514  1.00 53.80  ? 390  GLU A O     1 
ATOM   3010 C  CB    . GLU A 1 390 ? 5.311   -28.673 24.067  1.00 52.16  ? 390  GLU A CB    1 
ATOM   3011 C  CG    . GLU A 1 390 ? 4.647   -29.832 23.359  1.00 61.56  ? 390  GLU A CG    1 
ATOM   3012 C  CD    . GLU A 1 390 ? 3.181   -29.552 23.054  1.00 64.75  ? 390  GLU A CD    1 
ATOM   3013 O  OE1   . GLU A 1 390 ? 2.376   -29.471 24.015  1.00 57.38  ? 390  GLU A OE1   1 
ATOM   3014 O  OE2   . GLU A 1 390 ? 2.846   -29.390 21.852  1.00 62.89  ? 390  GLU A OE2   1 
ATOM   3015 N  N     . TRP A 1 391 ? 4.406   -25.489 24.805  1.00 45.53  ? 391  TRP A N     1 
ATOM   3016 C  CA    . TRP A 1 391 ? 4.617   -24.213 25.475  1.00 51.70  ? 391  TRP A CA    1 
ATOM   3017 C  C     . TRP A 1 391 ? 3.773   -24.131 26.738  1.00 52.79  ? 391  TRP A C     1 
ATOM   3018 O  O     . TRP A 1 391 ? 2.563   -24.369 26.693  1.00 50.03  ? 391  TRP A O     1 
ATOM   3019 C  CB    . TRP A 1 391 ? 4.270   -23.054 24.530  1.00 47.23  ? 391  TRP A CB    1 
ATOM   3020 C  CG    . TRP A 1 391 ? 4.439   -21.687 25.134  1.00 50.60  ? 391  TRP A CG    1 
ATOM   3021 C  CD1   . TRP A 1 391 ? 5.537   -20.881 25.038  1.00 51.19  ? 391  TRP A CD1   1 
ATOM   3022 C  CD2   . TRP A 1 391 ? 3.480   -20.967 25.918  1.00 50.59  ? 391  TRP A CD2   1 
ATOM   3023 N  NE1   . TRP A 1 391 ? 5.319   -19.710 25.712  1.00 51.22  ? 391  TRP A NE1   1 
ATOM   3024 C  CE2   . TRP A 1 391 ? 4.064   -19.737 26.262  1.00 48.55  ? 391  TRP A CE2   1 
ATOM   3025 C  CE3   . TRP A 1 391 ? 2.181   -21.244 26.362  1.00 52.59  ? 391  TRP A CE3   1 
ATOM   3026 C  CZ2   . TRP A 1 391 ? 3.398   -18.784 27.032  1.00 54.51  ? 391  TRP A CZ2   1 
ATOM   3027 C  CZ3   . TRP A 1 391 ? 1.522   -20.297 27.126  1.00 54.56  ? 391  TRP A CZ3   1 
ATOM   3028 C  CH2   . TRP A 1 391 ? 2.129   -19.083 27.452  1.00 52.80  ? 391  TRP A CH2   1 
ATOM   3029 N  N     . ARG A 1 392 ? 4.414   -23.774 27.865  1.00 55.64  ? 392  ARG A N     1 
ATOM   3030 C  CA    . ARG A 1 392 ? 3.722   -23.533 29.125  1.00 68.53  ? 392  ARG A CA    1 
ATOM   3031 C  C     . ARG A 1 392 ? 3.793   -22.054 29.506  1.00 72.96  ? 392  ARG A C     1 
ATOM   3032 O  O     . ARG A 1 392 ? 4.740   -21.352 29.133  1.00 70.02  ? 392  ARG A O     1 
ATOM   3033 C  CB    . ARG A 1 392 ? 4.312   -24.373 30.268  1.00 73.26  ? 392  ARG A CB    1 
ATOM   3034 C  CG    . ARG A 1 392 ? 3.961   -25.862 30.206  1.00 76.15  ? 392  ARG A CG    1 
ATOM   3035 C  CD    . ARG A 1 392 ? 4.498   -26.637 31.415  1.00 77.28  ? 392  ARG A CD    1 
ATOM   3036 N  NE    . ARG A 1 392 ? 5.953   -26.742 31.404  1.00 83.45  ? 392  ARG A NE    1 
ATOM   3037 C  CZ    . ARG A 1 392 ? 6.672   -27.378 32.322  1.00 84.57  ? 392  ARG A CZ    1 
ATOM   3038 N  NH1   . ARG A 1 392 ? 6.102   -27.985 33.351  1.00 84.35  ? 392  ARG A NH1   1 
ATOM   3039 N  NH2   . ARG A 1 392 ? 7.998   -27.404 32.204  1.00 81.57  ? 392  ARG A NH2   1 
ATOM   3040 N  N     . PRO A 1 393 ? 2.806   -21.548 30.260  1.00 76.26  ? 393  PRO A N     1 
ATOM   3041 C  CA    . PRO A 1 393 ? 2.856   -20.144 30.702  1.00 79.96  ? 393  PRO A CA    1 
ATOM   3042 C  C     . PRO A 1 393 ? 4.055   -19.826 31.584  1.00 90.34  ? 393  PRO A C     1 
ATOM   3043 O  O     . PRO A 1 393 ? 4.242   -18.675 31.988  1.00 92.10  ? 393  PRO A O     1 
ATOM   3044 C  CB    . PRO A 1 393 ? 1.538   -19.972 31.468  1.00 81.97  ? 393  PRO A CB    1 
ATOM   3045 C  CG    . PRO A 1 393 ? 0.623   -20.998 30.871  1.00 80.69  ? 393  PRO A CG    1 
ATOM   3046 C  CD    . PRO A 1 393 ? 1.508   -22.176 30.561  1.00 75.32  ? 393  PRO A CD    1 
ATOM   3047 N  N     . GLN A 1 394 ? 4.873   -20.834 31.883  1.00 102.75 ? 394  GLN A N     1 
ATOM   3048 C  CA    . GLN A 1 394 ? 6.075   -20.637 32.681  1.00 108.08 ? 394  GLN A CA    1 
ATOM   3049 C  C     . GLN A 1 394 ? 7.301   -20.292 31.845  1.00 106.44 ? 394  GLN A C     1 
ATOM   3050 O  O     . GLN A 1 394 ? 8.273   -19.758 32.390  1.00 107.91 ? 394  GLN A O     1 
ATOM   3051 C  CB    . GLN A 1 394 ? 6.361   -21.889 33.523  1.00 113.90 ? 394  GLN A CB    1 
ATOM   3052 C  CG    . GLN A 1 394 ? 5.516   -22.003 34.798  1.00 124.17 ? 394  GLN A CG    1 
ATOM   3053 C  CD    . GLN A 1 394 ? 4.055   -22.314 34.524  1.00 117.68 ? 394  GLN A CD    1 
ATOM   3054 O  OE1   . GLN A 1 394 ? 3.706   -22.821 33.459  1.00 111.93 ? 394  GLN A OE1   1 
ATOM   3055 N  NE2   . GLN A 1 394 ? 3.194   -22.012 35.491  1.00 120.35 ? 394  GLN A NE2   1 
ATOM   3056 N  N     . ASP A 1 395 ? 7.284   -20.579 30.546  1.00 95.42  ? 395  ASP A N     1 
ATOM   3057 C  CA    . ASP A 1 395 ? 8.403   -20.213 29.693  1.00 93.25  ? 395  ASP A CA    1 
ATOM   3058 C  C     . ASP A 1 395 ? 8.464   -18.697 29.515  1.00 94.73  ? 395  ASP A C     1 
ATOM   3059 O  O     . ASP A 1 395 ? 7.472   -17.982 29.692  1.00 91.74  ? 395  ASP A O     1 
ATOM   3060 C  CB    . ASP A 1 395 ? 8.285   -20.898 28.331  1.00 83.17  ? 395  ASP A CB    1 
ATOM   3061 C  CG    . ASP A 1 395 ? 8.105   -22.402 28.449  1.00 83.20  ? 395  ASP A CG    1 
ATOM   3062 O  OD1   . ASP A 1 395 ? 8.074   -22.911 29.591  1.00 86.28  ? 395  ASP A OD1   1 
ATOM   3063 O  OD2   . ASP A 1 395 ? 7.995   -23.074 27.400  1.00 73.41  ? 395  ASP A OD2   1 
ATOM   3064 N  N     . GLU A 1 396 ? 9.656   -18.201 29.171  1.00 95.66  ? 396  GLU A N     1 
ATOM   3065 C  CA    . GLU A 1 396 ? 9.781   -16.772 28.896  1.00 97.71  ? 396  GLU A CA    1 
ATOM   3066 C  C     . GLU A 1 396 ? 9.202   -16.422 27.532  1.00 90.81  ? 396  GLU A C     1 
ATOM   3067 O  O     . GLU A 1 396 ? 8.709   -15.305 27.338  1.00 88.32  ? 396  GLU A O     1 
ATOM   3068 C  CB    . GLU A 1 396 ? 11.246  -16.338 28.980  1.00 99.46  ? 396  GLU A CB    1 
ATOM   3069 C  CG    . GLU A 1 396 ? 11.455  -14.821 28.907  1.00 102.46 ? 396  GLU A CG    1 
ATOM   3070 C  CD    . GLU A 1 396 ? 12.883  -14.433 28.530  1.00 101.67 ? 396  GLU A CD    1 
ATOM   3071 O  OE1   . GLU A 1 396 ? 13.643  -15.325 28.086  1.00 101.45 ? 396  GLU A OE1   1 
ATOM   3072 O  OE2   . GLU A 1 396 ? 13.240  -13.239 28.675  1.00 96.28  ? 396  GLU A OE2   1 
ATOM   3073 N  N     . GLU A 1 397 ? 9.241   -17.366 26.596  1.00 79.53  ? 397  GLU A N     1 
ATOM   3074 C  CA    . GLU A 1 397 ? 8.761   -17.132 25.243  1.00 68.08  ? 397  GLU A CA    1 
ATOM   3075 C  C     . GLU A 1 397 ? 7.290   -16.727 25.257  1.00 58.33  ? 397  GLU A C     1 
ATOM   3076 O  O     . GLU A 1 397 ? 6.505   -17.284 26.030  1.00 56.64  ? 397  GLU A O     1 
ATOM   3077 C  CB    . GLU A 1 397 ? 8.921   -18.407 24.413  1.00 67.43  ? 397  GLU A CB    1 
ATOM   3078 C  CG    . GLU A 1 397 ? 10.337  -18.883 24.274  1.00 68.53  ? 397  GLU A CG    1 
ATOM   3079 C  CD    . GLU A 1 397 ? 10.861  -18.634 22.888  1.00 72.48  ? 397  GLU A CD    1 
ATOM   3080 O  OE1   . GLU A 1 397 ? 10.071  -18.816 21.935  1.00 68.03  ? 397  GLU A OE1   1 
ATOM   3081 O  OE2   . GLU A 1 397 ? 12.045  -18.244 22.748  1.00 81.62  ? 397  GLU A OE2   1 
ATOM   3082 N  N     . PRO A 1 398 ? 6.872   -15.777 24.420  1.00 47.62  ? 398  PRO A N     1 
ATOM   3083 C  CA    . PRO A 1 398 ? 5.441   -15.658 24.140  1.00 43.86  ? 398  PRO A CA    1 
ATOM   3084 C  C     . PRO A 1 398 ? 4.984   -16.831 23.284  1.00 44.04  ? 398  PRO A C     1 
ATOM   3085 O  O     . PRO A 1 398 ? 5.748   -17.395 22.496  1.00 45.12  ? 398  PRO A O     1 
ATOM   3086 C  CB    . PRO A 1 398 ? 5.322   -14.324 23.396  1.00 39.54  ? 398  PRO A CB    1 
ATOM   3087 C  CG    . PRO A 1 398 ? 6.645   -14.119 22.786  1.00 41.77  ? 398  PRO A CG    1 
ATOM   3088 C  CD    . PRO A 1 398 ? 7.653   -14.737 23.733  1.00 44.56  ? 398  PRO A CD    1 
ATOM   3089 N  N     . CYS A 1 399 ? 3.733   -17.237 23.486  1.00 36.14  ? 399  CYS A N     1 
ATOM   3090 C  CA    . CYS A 1 399 ? 3.204   -18.333 22.688  1.00 41.55  ? 399  CYS A CA    1 
ATOM   3091 C  C     . CYS A 1 399 ? 2.823   -17.873 21.289  1.00 33.23  ? 399  CYS A C     1 
ATOM   3092 O  O     . CYS A 1 399 ? 2.703   -18.700 20.379  1.00 27.92  ? 399  CYS A O     1 
ATOM   3093 C  CB    . CYS A 1 399 ? 2.005   -18.974 23.404  1.00 34.03  ? 399  CYS A CB    1 
ATOM   3094 S  SG    . CYS A 1 399 ? 0.548   -17.958 23.610  1.00 31.04  ? 399  CYS A SG    1 
ATOM   3095 N  N     . ALA A 1 400 ? 2.643   -16.573 21.105  1.00 33.76  ? 400  ALA A N     1 
ATOM   3096 C  CA    . ALA A 1 400 ? 2.286   -15.997 19.824  1.00 25.82  ? 400  ALA A CA    1 
ATOM   3097 C  C     . ALA A 1 400 ? 3.293   -14.909 19.497  1.00 28.91  ? 400  ALA A C     1 
ATOM   3098 O  O     . ALA A 1 400 ? 3.753   -14.197 20.395  1.00 33.88  ? 400  ALA A O     1 
ATOM   3099 C  CB    . ALA A 1 400 ? 0.870   -15.431 19.879  1.00 23.10  ? 400  ALA A CB    1 
ATOM   3100 N  N     . HIS A 1 401 ? 3.655   -14.785 18.223  1.00 26.58  ? 401  HIS A N     1 
ATOM   3101 C  CA    . HIS A 1 401 ? 4.516   -13.660 17.843  1.00 21.07  ? 401  HIS A CA    1 
ATOM   3102 C  C     . HIS A 1 401 ? 3.800   -12.342 18.145  1.00 23.25  ? 401  HIS A C     1 
ATOM   3103 O  O     . HIS A 1 401 ? 2.581   -12.247 17.953  1.00 25.04  ? 401  HIS A O     1 
ATOM   3104 C  CB    . HIS A 1 401 ? 4.883   -13.707 16.381  1.00 23.20  ? 401  HIS A CB    1 
ATOM   3105 C  CG    . HIS A 1 401 ? 5.924   -12.697 16.003  1.00 25.36  ? 401  HIS A CG    1 
ATOM   3106 N  ND1   . HIS A 1 401 ? 5.606   -11.419 15.609  1.00 26.11  ? 401  HIS A ND1   1 
ATOM   3107 C  CD2   . HIS A 1 401 ? 7.275   -12.761 16.013  1.00 24.84  ? 401  HIS A CD2   1 
ATOM   3108 C  CE1   . HIS A 1 401 ? 6.716   -10.748 15.360  1.00 25.84  ? 401  HIS A CE1   1 
ATOM   3109 N  NE2   . HIS A 1 401 ? 7.743   -11.538 15.606  1.00 28.55  ? 401  HIS A NE2   1 
ATOM   3110 N  N     . PRO A 1 402 ? 4.522   -11.312 18.618  1.00 26.04  ? 402  PRO A N     1 
ATOM   3111 C  CA    . PRO A 1 402 ? 3.857   -10.025 18.933  1.00 24.32  ? 402  PRO A CA    1 
ATOM   3112 C  C     . PRO A 1 402 ? 3.125   -9.397  17.764  1.00 21.66  ? 402  PRO A C     1 
ATOM   3113 O  O     . PRO A 1 402 ? 2.177   -8.641  17.979  1.00 26.08  ? 402  PRO A O     1 
ATOM   3114 C  CB    . PRO A 1 402 ? 5.015   -9.131  19.393  1.00 26.64  ? 402  PRO A CB    1 
ATOM   3115 C  CG    . PRO A 1 402 ? 6.032   -10.078 19.901  1.00 30.85  ? 402  PRO A CG    1 
ATOM   3116 C  CD    . PRO A 1 402 ? 5.916   -11.334 19.089  1.00 25.29  ? 402  PRO A CD    1 
ATOM   3117 N  N     . ASN A 1 403 ? 3.515   -9.692  16.532  1.00 23.64  ? 403  ASN A N     1 
ATOM   3118 C  CA    . ASN A 1 403 ? 2.833   -9.147  15.366  1.00 28.89  ? 403  ASN A CA    1 
ATOM   3119 C  C     . ASN A 1 403 ? 1.981   -10.192 14.654  1.00 28.90  ? 403  ASN A C     1 
ATOM   3120 O  O     . ASN A 1 403 ? 1.634   -10.010 13.484  1.00 21.58  ? 403  ASN A O     1 
ATOM   3121 C  CB    . ASN A 1 403 ? 3.855   -8.534  14.398  1.00 26.81  ? 403  ASN A CB    1 
ATOM   3122 C  CG    . ASN A 1 403 ? 3.196   -7.741  13.264  1.00 30.18  ? 403  ASN A CG    1 
ATOM   3123 O  OD1   . ASN A 1 403 ? 2.295   -6.936  13.503  1.00 30.22  ? 403  ASN A OD1   1 
ATOM   3124 N  ND2   . ASN A 1 403 ? 3.628   -7.997  12.019  1.00 26.38  ? 403  ASN A ND2   1 
ATOM   3125 N  N     . SER A 1 404 ? 1.638   -11.289 15.334  1.00 22.47  ? 404  SER A N     1 
ATOM   3126 C  CA    . SER A 1 404 ? 0.735   -12.248 14.733  1.00 20.44  ? 404  SER A CA    1 
ATOM   3127 C  C     . SER A 1 404 ? -0.611  -11.586 14.465  1.00 21.45  ? 404  SER A C     1 
ATOM   3128 O  O     . SER A 1 404 ? -0.996  -10.608 15.112  1.00 23.99  ? 404  SER A O     1 
ATOM   3129 C  CB    . SER A 1 404 ? 0.587   -13.467 15.640  1.00 22.44  ? 404  SER A CB    1 
ATOM   3130 O  OG    . SER A 1 404 ? 0.250   -13.077 16.969  1.00 24.39  ? 404  SER A OG    1 
ATOM   3131 N  N     . ARG A 1 405 ? -1.327  -12.113 13.482  1.00 20.72  ? 405  ARG A N     1 
ATOM   3132 C  CA    . ARG A 1 405 ? -2.471  -11.419 12.905  1.00 19.32  ? 405  ARG A CA    1 
ATOM   3133 C  C     . ARG A 1 405 ? -3.613  -12.396 12.714  1.00 21.12  ? 405  ARG A C     1 
ATOM   3134 O  O     . ARG A 1 405 ? -3.394  -13.585 12.520  1.00 21.20  ? 405  ARG A O     1 
ATOM   3135 C  CB    . ARG A 1 405 ? -2.120  -10.829 11.527  1.00 17.51  ? 405  ARG A CB    1 
ATOM   3136 C  CG    . ARG A 1 405 ? -0.994  -9.793  11.584  1.00 19.84  ? 405  ARG A CG    1 
ATOM   3137 C  CD    . ARG A 1 405 ? -1.576  -8.405  11.805  1.00 21.34  ? 405  ARG A CD    1 
ATOM   3138 N  NE    . ARG A 1 405 ? -0.577  -7.339  11.963  1.00 18.93  ? 405  ARG A NE    1 
ATOM   3139 C  CZ    . ARG A 1 405 ? -0.903  -6.059  12.053  1.00 21.60  ? 405  ARG A CZ    1 
ATOM   3140 N  NH1   . ARG A 1 405 ? -2.128  -5.636  11.768  1.00 16.27  ? 405  ARG A NH1   1 
ATOM   3141 N  NH2   . ARG A 1 405 ? 0.018   -5.182  12.431  1.00 19.10  ? 405  ARG A NH2   1 
ATOM   3142 N  N     . PHE A 1 406 ? -4.826  -11.869 12.697  1.00 19.80  ? 406  PHE A N     1 
ATOM   3143 C  CA    . PHE A 1 406 ? -5.957  -12.560 12.109  1.00 20.66  ? 406  PHE A CA    1 
ATOM   3144 C  C     . PHE A 1 406 ? -6.355  -11.858 10.823  1.00 20.49  ? 406  PHE A C     1 
ATOM   3145 O  O     . PHE A 1 406 ? -6.133  -10.657 10.650  1.00 20.42  ? 406  PHE A O     1 
ATOM   3146 C  CB    . PHE A 1 406 ? -7.168  -12.629 13.076  1.00 19.77  ? 406  PHE A CB    1 
ATOM   3147 C  CG    . PHE A 1 406 ? -7.648  -11.293 13.587  1.00 21.31  ? 406  PHE A CG    1 
ATOM   3148 C  CD1   . PHE A 1 406 ? -8.482  -10.491 12.823  1.00 19.46  ? 406  PHE A CD1   1 
ATOM   3149 C  CD2   . PHE A 1 406 ? -7.298  -10.866 14.857  1.00 20.19  ? 406  PHE A CD2   1 
ATOM   3150 C  CE1   . PHE A 1 406 ? -8.918  -9.255  13.295  1.00 23.49  ? 406  PHE A CE1   1 
ATOM   3151 C  CE2   . PHE A 1 406 ? -7.760  -9.654  15.354  1.00 20.85  ? 406  PHE A CE2   1 
ATOM   3152 C  CZ    . PHE A 1 406 ? -8.564  -8.843  14.578  1.00 26.81  ? 406  PHE A CZ    1 
ATOM   3153 N  N     . CYS A 1 407 ? -6.941  -12.615 9.916   1.00 18.23  ? 407  CYS A N     1 
ATOM   3154 C  CA    . CYS A 1 407 ? -7.359  -12.096 8.625   1.00 17.57  ? 407  CYS A CA    1 
ATOM   3155 C  C     . CYS A 1 407 ? -8.813  -12.511 8.465   1.00 18.19  ? 407  CYS A C     1 
ATOM   3156 O  O     . CYS A 1 407 ? -9.094  -13.694 8.252   1.00 19.40  ? 407  CYS A O     1 
ATOM   3157 C  CB    . CYS A 1 407 ? -6.481  -12.675 7.501   1.00 18.67  ? 407  CYS A CB    1 
ATOM   3158 S  SG    . CYS A 1 407 ? -6.797  -11.973 5.892   1.00 21.12  ? 407  CYS A SG    1 
ATOM   3159 N  N     . THR A 1 408 ? -9.735  -11.556 8.550   1.00 19.42  ? 408  THR A N     1 
ATOM   3160 C  CA    . THR A 1 408 ? -11.127 -11.934 8.725   1.00 17.43  ? 408  THR A CA    1 
ATOM   3161 C  C     . THR A 1 408 ? -12.019 -11.088 7.832   1.00 18.73  ? 408  THR A C     1 
ATOM   3162 O  O     . THR A 1 408 ? -11.706 -9.918  7.572   1.00 18.13  ? 408  THR A O     1 
ATOM   3163 C  CB    . THR A 1 408 ? -11.524 -11.781 10.212  1.00 23.04  ? 408  THR A CB    1 
ATOM   3164 O  OG1   . THR A 1 408 ? -12.699 -12.554 10.469  1.00 20.42  ? 408  THR A OG1   1 
ATOM   3165 C  CG2   . THR A 1 408 ? -11.764 -10.301 10.596  1.00 17.67  ? 408  THR A CG2   1 
ATOM   3166 N  N     . PRO A 1 409 ? -13.108 -11.662 7.305   1.00 18.44  ? 409  PRO A N     1 
ATOM   3167 C  CA    . PRO A 1 409 ? -13.999 -10.892 6.419   1.00 17.48  ? 409  PRO A CA    1 
ATOM   3168 C  C     . PRO A 1 409 ? -14.732 -9.778  7.159   1.00 25.51  ? 409  PRO A C     1 
ATOM   3169 O  O     . PRO A 1 409 ? -15.273 -9.986  8.248   1.00 20.51  ? 409  PRO A O     1 
ATOM   3170 C  CB    . PRO A 1 409 ? -14.992 -11.948 5.903   1.00 21.10  ? 409  PRO A CB    1 
ATOM   3171 C  CG    . PRO A 1 409 ? -14.300 -13.269 6.092   1.00 23.81  ? 409  PRO A CG    1 
ATOM   3172 C  CD    . PRO A 1 409 ? -13.473 -13.093 7.355   1.00 19.49  ? 409  PRO A CD    1 
ATOM   3173 N  N     . ALA A 1 410 ? -14.756 -8.586  6.546   1.00 20.56  ? 410  ALA A N     1 
ATOM   3174 C  CA    . ALA A 1 410 ? -15.409 -7.428  7.177   1.00 22.10  ? 410  ALA A CA    1 
ATOM   3175 C  C     . ALA A 1 410 ? -16.913 -7.627  7.341   1.00 24.82  ? 410  ALA A C     1 
ATOM   3176 O  O     . ALA A 1 410 ? -17.508 -7.145  8.326   1.00 22.31  ? 410  ALA A O     1 
ATOM   3177 C  CB    . ALA A 1 410 ? -15.147 -6.160  6.370   1.00 19.93  ? 410  ALA A CB    1 
ATOM   3178 N  N     . SER A 1 411 ? -17.531 -8.346  6.397   1.00 29.64  ? 411  SER A N     1 
ATOM   3179 C  CA    . SER A 1 411 ? -18.977 -8.553  6.393   1.00 31.53  ? 411  SER A CA    1 
ATOM   3180 C  C     . SER A 1 411 ? -19.481 -9.277  7.637   1.00 30.37  ? 411  SER A C     1 
ATOM   3181 O  O     . SER A 1 411 ? -20.658 -9.128  7.985   1.00 35.95  ? 411  SER A O     1 
ATOM   3182 C  CB    . SER A 1 411 ? -19.372 -9.333  5.146   1.00 34.54  ? 411  SER A CB    1 
ATOM   3183 O  OG    . SER A 1 411 ? -18.905 -10.665 5.259   1.00 37.86  ? 411  SER A OG    1 
ATOM   3184 N  N     . GLN A 1 412 ? -18.615 -10.018 8.332   1.00 28.30  ? 412  GLN A N     1 
ATOM   3185 C  CA    . GLN A 1 412 ? -18.975 -10.794 9.511   1.00 31.41  ? 412  GLN A CA    1 
ATOM   3186 C  C     . GLN A 1 412 ? -18.961 -9.989  10.795  1.00 32.16  ? 412  GLN A C     1 
ATOM   3187 O  O     . GLN A 1 412 ? -19.442 -10.488 11.810  1.00 29.60  ? 412  GLN A O     1 
ATOM   3188 C  CB    . GLN A 1 412 ? -18.017 -11.968 9.691   1.00 30.52  ? 412  GLN A CB    1 
ATOM   3189 C  CG    . GLN A 1 412 ? -18.145 -12.983 8.607   1.00 33.04  ? 412  GLN A CG    1 
ATOM   3190 C  CD    . GLN A 1 412 ? -17.114 -14.072 8.685   1.00 28.23  ? 412  GLN A CD    1 
ATOM   3191 O  OE1   . GLN A 1 412 ? -17.105 -14.959 7.836   1.00 36.25  ? 412  GLN A OE1   1 
ATOM   3192 N  NE2   . GLN A 1 412 ? -16.237 -14.025 9.697   1.00 26.39  ? 412  GLN A NE2   1 
ATOM   3193 N  N     . CYS A 1 413 ? -18.372 -8.801  10.795  1.00 25.67  ? 413  CYS A N     1 
ATOM   3194 C  CA    . CYS A 1 413 ? -18.327 -8.000  12.003  1.00 26.05  ? 413  CYS A CA    1 
ATOM   3195 C  C     . CYS A 1 413 ? -19.753 -7.689  12.457  1.00 26.14  ? 413  CYS A C     1 
ATOM   3196 O  O     . CYS A 1 413 ? -20.550 -7.173  11.656  1.00 25.84  ? 413  CYS A O     1 
ATOM   3197 C  CB    . CYS A 1 413 ? -17.571 -6.694  11.732  1.00 22.97  ? 413  CYS A CB    1 
ATOM   3198 S  SG    . CYS A 1 413 ? -17.243 -5.753  13.224  1.00 31.02  ? 413  CYS A SG    1 
ATOM   3199 N  N     . PRO A 1 414 ? -20.125 -7.993  13.707  1.00 28.60  ? 414  PRO A N     1 
ATOM   3200 C  CA    . PRO A 1 414 ? -21.521 -7.768  14.107  1.00 25.50  ? 414  PRO A CA    1 
ATOM   3201 C  C     . PRO A 1 414 ? -21.912 -6.304  14.111  1.00 30.13  ? 414  PRO A C     1 
ATOM   3202 O  O     . PRO A 1 414 ? -23.111 -6.014  14.036  1.00 27.38  ? 414  PRO A O     1 
ATOM   3203 C  CB    . PRO A 1 414 ? -21.598 -8.379  15.516  1.00 30.95  ? 414  PRO A CB    1 
ATOM   3204 C  CG    . PRO A 1 414 ? -20.205 -8.389  16.019  1.00 31.69  ? 414  PRO A CG    1 
ATOM   3205 C  CD    . PRO A 1 414 ? -19.317 -8.553  14.809  1.00 26.99  ? 414  PRO A CD    1 
ATOM   3206 N  N     . ILE A 1 415 ? -20.949 -5.378  14.150  1.00 28.47  ? 415  ILE A N     1 
ATOM   3207 C  CA    . ILE A 1 415 ? -21.231 -3.943  14.143  1.00 24.99  ? 415  ILE A CA    1 
ATOM   3208 C  C     . ILE A 1 415 ? -20.748 -3.278  12.852  1.00 27.21  ? 415  ILE A C     1 
ATOM   3209 O  O     . ILE A 1 415 ? -20.574 -2.075  12.821  1.00 19.96  ? 415  ILE A O     1 
ATOM   3210 C  CB    . ILE A 1 415 ? -20.625 -3.256  15.376  1.00 23.38  ? 415  ILE A CB    1 
ATOM   3211 C  CG1   . ILE A 1 415 ? -19.115 -3.555  15.455  1.00 27.26  ? 415  ILE A CG1   1 
ATOM   3212 C  CG2   . ILE A 1 415 ? -21.312 -3.714  16.634  1.00 25.98  ? 415  ILE A CG2   1 
ATOM   3213 C  CD1   . ILE A 1 415 ? -18.373 -2.701  16.467  1.00 34.95  ? 415  ILE A CD1   1 
ATOM   3214 N  N     . ILE A 1 416 ? -20.529 -4.046  11.782  1.00 21.63  ? 416  ILE A N     1 
ATOM   3215 C  CA    . ILE A 1 416 ? -20.178 -3.441  10.508  1.00 22.66  ? 416  ILE A CA    1 
ATOM   3216 C  C     . ILE A 1 416 ? -21.270 -2.450  10.118  1.00 29.67  ? 416  ILE A C     1 
ATOM   3217 O  O     . ILE A 1 416 ? -22.469 -2.684  10.323  1.00 24.74  ? 416  ILE A O     1 
ATOM   3218 C  CB    . ILE A 1 416 ? -19.924 -4.503  9.418   1.00 24.19  ? 416  ILE A CB    1 
ATOM   3219 C  CG1   . ILE A 1 416 ? -19.088 -3.898  8.278   1.00 24.10  ? 416  ILE A CG1   1 
ATOM   3220 C  CG2   . ILE A 1 416 ? -21.214 -5.103  8.876   1.00 30.32  ? 416  ILE A CG2   1 
ATOM   3221 C  CD1   . ILE A 1 416 ? -17.631 -3.738  8.643   1.00 20.96  ? 416  ILE A CD1   1 
ATOM   3222 N  N     . ASP A 1 417 ? -20.839 -1.302  9.618   1.00 22.21  ? 417  ASP A N     1 
ATOM   3223 C  CA    . ASP A 1 417 ? -21.739 -0.186  9.370   1.00 22.76  ? 417  ASP A CA    1 
ATOM   3224 C  C     . ASP A 1 417 ? -22.594 -0.490  8.143   1.00 28.97  ? 417  ASP A C     1 
ATOM   3225 O  O     . ASP A 1 417 ? -22.094 -1.068  7.170   1.00 24.84  ? 417  ASP A O     1 
ATOM   3226 C  CB    . ASP A 1 417 ? -20.919 1.106   9.130   1.00 21.31  ? 417  ASP A CB    1 
ATOM   3227 C  CG    . ASP A 1 417 ? -21.762 2.354   9.158   1.00 21.64  ? 417  ASP A CG    1 
ATOM   3228 O  OD1   . ASP A 1 417 ? -21.987 2.867   10.262  1.00 27.25  ? 417  ASP A OD1   1 
ATOM   3229 O  OD2   . ASP A 1 417 ? -22.221 2.816   8.099   1.00 23.71  ? 417  ASP A OD2   1 
ATOM   3230 N  N     . PRO A 1 418 ? -23.883 -0.135  8.164   1.00 29.25  ? 418  PRO A N     1 
ATOM   3231 C  CA    . PRO A 1 418 ? -24.733 -0.400  6.989   1.00 28.68  ? 418  PRO A CA    1 
ATOM   3232 C  C     . PRO A 1 418 ? -24.292 0.327   5.730   1.00 31.43  ? 418  PRO A C     1 
ATOM   3233 O  O     . PRO A 1 418 ? -24.698 -0.083  4.632   1.00 33.91  ? 418  PRO A O     1 
ATOM   3234 C  CB    . PRO A 1 418 ? -26.128 0.069   7.444   1.00 29.04  ? 418  PRO A CB    1 
ATOM   3235 C  CG    . PRO A 1 418 ? -25.850 1.017   8.584   1.00 31.73  ? 418  PRO A CG    1 
ATOM   3236 C  CD    . PRO A 1 418 ? -24.655 0.419   9.288   1.00 26.32  ? 418  PRO A CD    1 
ATOM   3237 N  N     . ALA A 1 419 ? -23.481 1.384   5.838   1.00 27.13  ? 419  ALA A N     1 
ATOM   3238 C  CA    . ALA A 1 419 ? -22.968 2.097   4.675   1.00 26.77  ? 419  ALA A CA    1 
ATOM   3239 C  C     . ALA A 1 419 ? -21.516 1.734   4.348   1.00 31.43  ? 419  ALA A C     1 
ATOM   3240 O  O     . ALA A 1 419 ? -20.852 2.483   3.613   1.00 29.72  ? 419  ALA A O     1 
ATOM   3241 C  CB    . ALA A 1 419 ? -23.078 3.612   4.888   1.00 25.48  ? 419  ALA A CB    1 
ATOM   3242 N  N     . TRP A 1 420 ? -21.005 0.616   4.879   1.00 25.11  ? 420  TRP A N     1 
ATOM   3243 C  CA    . TRP A 1 420 ? -19.577 0.319   4.723   1.00 25.89  ? 420  TRP A CA    1 
ATOM   3244 C  C     . TRP A 1 420 ? -19.193 -0.055  3.300   1.00 29.99  ? 420  TRP A C     1 
ATOM   3245 O  O     . TRP A 1 420 ? -18.014 0.058   2.950   1.00 29.06  ? 420  TRP A O     1 
ATOM   3246 C  CB    . TRP A 1 420 ? -19.119 -0.781  5.676   1.00 23.42  ? 420  TRP A CB    1 
ATOM   3247 C  CG    . TRP A 1 420 ? -19.342 -2.197  5.221   1.00 26.79  ? 420  TRP A CG    1 
ATOM   3248 C  CD1   . TRP A 1 420 ? -20.484 -2.943  5.367   1.00 31.25  ? 420  TRP A CD1   1 
ATOM   3249 C  CD2   . TRP A 1 420 ? -18.371 -3.066  4.587   1.00 28.22  ? 420  TRP A CD2   1 
ATOM   3250 N  NE1   . TRP A 1 420 ? -20.288 -4.219  4.838   1.00 24.30  ? 420  TRP A NE1   1 
ATOM   3251 C  CE2   . TRP A 1 420 ? -19.000 -4.316  4.373   1.00 29.74  ? 420  TRP A CE2   1 
ATOM   3252 C  CE3   . TRP A 1 420 ? -17.032 -2.902  4.192   1.00 25.99  ? 420  TRP A CE3   1 
ATOM   3253 C  CZ2   . TRP A 1 420 ? -18.342 -5.398  3.760   1.00 31.02  ? 420  TRP A CZ2   1 
ATOM   3254 C  CZ3   . TRP A 1 420 ? -16.380 -3.968  3.571   1.00 26.25  ? 420  TRP A CZ3   1 
ATOM   3255 C  CH2   . TRP A 1 420 ? -17.043 -5.208  3.369   1.00 28.00  ? 420  TRP A CH2   1 
ATOM   3256 N  N     . GLU A 1 421 ? -20.148 -0.450  2.461   1.00 30.05  ? 421  GLU A N     1 
ATOM   3257 C  CA    . GLU A 1 421 ? -19.880 -0.707  1.053   1.00 26.44  ? 421  GLU A CA    1 
ATOM   3258 C  C     . GLU A 1 421 ? -20.591 0.265   0.147   1.00 33.57  ? 421  GLU A C     1 
ATOM   3259 O  O     . GLU A 1 421 ? -20.673 0.006   -1.058  1.00 38.33  ? 421  GLU A O     1 
ATOM   3260 C  CB    . GLU A 1 421 ? -20.310 -2.115  0.654   1.00 32.63  ? 421  GLU A CB    1 
ATOM   3261 C  CG    . GLU A 1 421 ? -19.672 -3.183  1.432   1.00 30.94  ? 421  GLU A CG    1 
ATOM   3262 C  CD    . GLU A 1 421 ? -19.848 -4.529  0.774   1.00 38.57  ? 421  GLU A CD    1 
ATOM   3263 O  OE1   . GLU A 1 421 ? -20.928 -5.118  0.953   1.00 36.35  ? 421  GLU A OE1   1 
ATOM   3264 O  OE2   . GLU A 1 421 ? -18.912 -4.969  0.070   1.00 34.95  ? 421  GLU A OE2   1 
ATOM   3265 N  N     . SER A 1 422 ? -21.146 1.349   0.690   1.00 29.38  ? 422  SER A N     1 
ATOM   3266 C  CA    . SER A 1 422 ? -21.817 2.312   -0.166  1.00 28.75  ? 422  SER A CA    1 
ATOM   3267 C  C     . SER A 1 422 ? -20.789 2.963   -1.078  1.00 33.33  ? 422  SER A C     1 
ATOM   3268 O  O     . SER A 1 422 ? -19.721 3.371   -0.607  1.00 33.05  ? 422  SER A O     1 
ATOM   3269 C  CB    . SER A 1 422 ? -22.551 3.375   0.641   1.00 32.98  ? 422  SER A CB    1 
ATOM   3270 O  OG    . SER A 1 422 ? -23.535 2.749   1.466   1.00 42.48  ? 422  SER A OG    1 
ATOM   3271 N  N     . PRO A 1 423 ? -21.064 3.064   -2.375  1.00 35.68  ? 423  PRO A N     1 
ATOM   3272 C  CA    . PRO A 1 423 ? -20.053 3.590   -3.299  1.00 37.39  ? 423  PRO A CA    1 
ATOM   3273 C  C     . PRO A 1 423 ? -19.801 5.075   -3.139  1.00 36.81  ? 423  PRO A C     1 
ATOM   3274 O  O     . PRO A 1 423 ? -18.747 5.546   -3.576  1.00 39.24  ? 423  PRO A O     1 
ATOM   3275 C  CB    . PRO A 1 423 ? -20.635 3.259   -4.678  1.00 41.77  ? 423  PRO A CB    1 
ATOM   3276 C  CG    . PRO A 1 423 ? -22.132 3.161   -4.434  1.00 38.53  ? 423  PRO A CG    1 
ATOM   3277 C  CD    . PRO A 1 423 ? -22.263 2.564   -3.069  1.00 38.14  ? 423  PRO A CD    1 
ATOM   3278 N  N     . GLU A 1 424 ? -20.714 5.829   -2.516  1.00 33.84  ? 424  GLU A N     1 
ATOM   3279 C  CA    . GLU A 1 424 ? -20.536 7.266   -2.355  1.00 34.58  ? 424  GLU A CA    1 
ATOM   3280 C  C     . GLU A 1 424 ? -19.758 7.639   -1.092  1.00 27.96  ? 424  GLU A C     1 
ATOM   3281 O  O     . GLU A 1 424 ? -19.327 8.784   -0.972  1.00 33.20  ? 424  GLU A O     1 
ATOM   3282 C  CB    . GLU A 1 424 ? -21.904 7.981   -2.382  1.00 29.42  ? 424  GLU A CB    1 
ATOM   3283 C  CG    . GLU A 1 424 ? -22.711 7.901   -1.102  1.00 39.71  ? 424  GLU A CG    1 
ATOM   3284 C  CD    . GLU A 1 424 ? -23.288 6.513   -0.807  1.00 50.56  ? 424  GLU A CD    1 
ATOM   3285 O  OE1   . GLU A 1 424 ? -23.266 5.621   -1.699  1.00 42.65  ? 424  GLU A OE1   1 
ATOM   3286 O  OE2   . GLU A 1 424 ? -23.769 6.321   0.343   1.00 58.68  ? 424  GLU A OE2   1 
ATOM   3287 N  N     . GLY A 1 425 ? -19.511 6.700   -0.188  1.00 27.09  ? 425  GLY A N     1 
ATOM   3288 C  CA    . GLY A 1 425 ? -18.712 6.972   0.984   1.00 21.45  ? 425  GLY A CA    1 
ATOM   3289 C  C     . GLY A 1 425 ? -19.541 7.606   2.089   1.00 26.49  ? 425  GLY A C     1 
ATOM   3290 O  O     . GLY A 1 425 ? -20.714 7.927   1.925   1.00 29.00  ? 425  GLY A O     1 
ATOM   3291 N  N     . VAL A 1 426 ? -18.908 7.780   3.242   1.00 20.26  ? 426  VAL A N     1 
ATOM   3292 C  CA    . VAL A 1 426 ? -19.596 8.333   4.402   1.00 24.66  ? 426  VAL A CA    1 
ATOM   3293 C  C     . VAL A 1 426 ? -19.018 9.713   4.673   1.00 25.66  ? 426  VAL A C     1 
ATOM   3294 O  O     . VAL A 1 426 ? -17.839 9.958   4.383   1.00 23.70  ? 426  VAL A O     1 
ATOM   3295 C  CB    . VAL A 1 426 ? -19.493 7.401   5.617   1.00 20.32  ? 426  VAL A CB    1 
ATOM   3296 C  CG1   . VAL A 1 426 ? -20.234 6.083   5.330   1.00 22.09  ? 426  VAL A CG1   1 
ATOM   3297 C  CG2   . VAL A 1 426 ? -18.055 7.127   6.027   1.00 21.21  ? 426  VAL A CG2   1 
ATOM   3298 N  N     . PRO A 1 427 ? -19.816 10.657  5.179   1.00 24.38  ? 427  PRO A N     1 
ATOM   3299 C  CA    . PRO A 1 427 ? -19.330 12.039  5.319   1.00 24.51  ? 427  PRO A CA    1 
ATOM   3300 C  C     . PRO A 1 427 ? -18.589 12.181  6.640   1.00 23.86  ? 427  PRO A C     1 
ATOM   3301 O  O     . PRO A 1 427 ? -19.134 11.869  7.703   1.00 23.29  ? 427  PRO A O     1 
ATOM   3302 C  CB    . PRO A 1 427 ? -20.618 12.876  5.292   1.00 23.77  ? 427  PRO A CB    1 
ATOM   3303 C  CG    . PRO A 1 427 ? -21.682 11.935  5.854   1.00 19.88  ? 427  PRO A CG    1 
ATOM   3304 C  CD    . PRO A 1 427 ? -21.257 10.518  5.470   1.00 23.12  ? 427  PRO A CD    1 
ATOM   3305 N  N     . ILE A 1 428 ? -17.337 12.637  6.573   1.00 21.21  ? 428  ILE A N     1 
ATOM   3306 C  CA    . ILE A 1 428 ? -16.458 12.659  7.738   1.00 18.07  ? 428  ILE A CA    1 
ATOM   3307 C  C     . ILE A 1 428 ? -16.603 14.011  8.411   1.00 19.20  ? 428  ILE A C     1 
ATOM   3308 O  O     . ILE A 1 428 ? -16.399 15.051  7.766   1.00 22.26  ? 428  ILE A O     1 
ATOM   3309 C  CB    . ILE A 1 428 ? -14.990 12.404  7.356   1.00 19.55  ? 428  ILE A CB    1 
ATOM   3310 C  CG1   . ILE A 1 428 ? -14.784 11.001  6.749   1.00 17.74  ? 428  ILE A CG1   1 
ATOM   3311 C  CG2   . ILE A 1 428 ? -14.087 12.624  8.581   1.00 19.49  ? 428  ILE A CG2   1 
ATOM   3312 C  CD1   . ILE A 1 428 ? -15.172 9.800   7.723   1.00 17.96  ? 428  ILE A CD1   1 
ATOM   3313 N  N     . GLU A 1 429 ? -16.907 14.003  9.714   1.00 16.96  ? 429  GLU A N     1 
ATOM   3314 C  CA    . GLU A 1 429 ? -17.091 15.246  10.441  1.00 19.59  ? 429  GLU A CA    1 
ATOM   3315 C  C     . GLU A 1 429 ? -16.005 15.523  11.456  1.00 20.52  ? 429  GLU A C     1 
ATOM   3316 O  O     . GLU A 1 429 ? -15.929 16.653  11.964  1.00 20.50  ? 429  GLU A O     1 
ATOM   3317 C  CB    . GLU A 1 429 ? -18.457 15.248  11.145  1.00 23.04  ? 429  GLU A CB    1 
ATOM   3318 C  CG    . GLU A 1 429 ? -19.585 15.292  10.149  1.00 22.87  ? 429  GLU A CG    1 
ATOM   3319 C  CD    . GLU A 1 429 ? -20.911 15.399  10.848  1.00 25.50  ? 429  GLU A CD    1 
ATOM   3320 O  OE1   . GLU A 1 429 ? -21.065 16.361  11.618  1.00 24.03  ? 429  GLU A OE1   1 
ATOM   3321 O  OE2   . GLU A 1 429 ? -21.763 14.507  10.636  1.00 22.79  ? 429  GLU A OE2   1 
ATOM   3322 N  N     . GLY A 1 430 ? -15.162 14.543  11.750  1.00 20.12  ? 430  GLY A N     1 
ATOM   3323 C  CA    . GLY A 1 430 ? -14.023 14.776  12.613  1.00 20.33  ? 430  GLY A CA    1 
ATOM   3324 C  C     . GLY A 1 430 ? -12.873 13.859  12.244  1.00 22.00  ? 430  GLY A C     1 
ATOM   3325 O  O     . GLY A 1 430 ? -13.091 12.727  11.799  1.00 20.57  ? 430  GLY A O     1 
ATOM   3326 N  N     . ILE A 1 431 ? -11.645 14.341  12.413  1.00 13.43  ? 431  ILE A N     1 
ATOM   3327 C  CA    . ILE A 1 431 ? -10.448 13.560  12.164  1.00 17.20  ? 431  ILE A CA    1 
ATOM   3328 C  C     . ILE A 1 431 ? -9.677  13.544  13.468  1.00 20.16  ? 431  ILE A C     1 
ATOM   3329 O  O     . ILE A 1 431 ? -9.546  14.584  14.120  1.00 19.85  ? 431  ILE A O     1 
ATOM   3330 C  CB    . ILE A 1 431 ? -9.595  14.162  11.024  1.00 17.45  ? 431  ILE A CB    1 
ATOM   3331 C  CG1   . ILE A 1 431 ? -10.294 13.989  9.671   1.00 17.03  ? 431  ILE A CG1   1 
ATOM   3332 C  CG2   . ILE A 1 431 ? -8.202  13.483  11.008  1.00 17.44  ? 431  ILE A CG2   1 
ATOM   3333 C  CD1   . ILE A 1 431 ? -9.642  14.809  8.484   1.00 23.25  ? 431  ILE A CD1   1 
ATOM   3334 N  N     . ILE A 1 432 ? -9.200  12.370  13.869  1.00 19.90  ? 432  ILE A N     1 
ATOM   3335 C  CA    . ILE A 1 432 ? -8.519  12.203  15.141  1.00 17.56  ? 432  ILE A CA    1 
ATOM   3336 C  C     . ILE A 1 432 ? -7.100  11.752  14.873  1.00 19.95  ? 432  ILE A C     1 
ATOM   3337 O  O     . ILE A 1 432 ? -6.884  10.858  14.053  1.00 20.35  ? 432  ILE A O     1 
ATOM   3338 C  CB    . ILE A 1 432 ? -9.231  11.171  16.038  1.00 15.97  ? 432  ILE A CB    1 
ATOM   3339 C  CG1   . ILE A 1 432 ? -10.738 11.434  16.080  1.00 19.37  ? 432  ILE A CG1   1 
ATOM   3340 C  CG2   . ILE A 1 432 ? -8.649  11.256  17.426  1.00 19.45  ? 432  ILE A CG2   1 
ATOM   3341 C  CD1   . ILE A 1 432 ? -11.537 10.373  16.888  1.00 18.27  ? 432  ILE A CD1   1 
ATOM   3342 N  N     . PHE A 1 433 ? -6.146  12.349  15.578  1.00 18.19  ? 433  PHE A N     1 
ATOM   3343 C  CA    . PHE A 1 433 ? -4.755  11.924  15.559  1.00 18.79  ? 433  PHE A CA    1 
ATOM   3344 C  C     . PHE A 1 433 ? -4.368  11.470  16.957  1.00 17.85  ? 433  PHE A C     1 
ATOM   3345 O  O     . PHE A 1 433 ? -4.964  11.901  17.946  1.00 16.58  ? 433  PHE A O     1 
ATOM   3346 C  CB    . PHE A 1 433 ? -3.794  13.078  15.121  1.00 14.69  ? 433  PHE A CB    1 
ATOM   3347 C  CG    . PHE A 1 433 ? -4.009  13.539  13.728  1.00 16.12  ? 433  PHE A CG    1 
ATOM   3348 C  CD1   . PHE A 1 433 ? -3.944  12.631  12.671  1.00 21.35  ? 433  PHE A CD1   1 
ATOM   3349 C  CD2   . PHE A 1 433 ? -4.290  14.879  13.455  1.00 18.99  ? 433  PHE A CD2   1 
ATOM   3350 C  CE1   . PHE A 1 433 ? -4.137  13.030  11.373  1.00 21.23  ? 433  PHE A CE1   1 
ATOM   3351 C  CE2   . PHE A 1 433 ? -4.485  15.291  12.149  1.00 18.50  ? 433  PHE A CE2   1 
ATOM   3352 C  CZ    . PHE A 1 433 ? -4.414  14.362  11.106  1.00 17.81  ? 433  PHE A CZ    1 
ATOM   3353 N  N     . GLY A 1 434 ? -3.325  10.639  17.043  1.00 16.25  ? 434  GLY A N     1 
ATOM   3354 C  CA    . GLY A 1 434 ? -2.867  10.221  18.355  1.00 20.09  ? 434  GLY A CA    1 
ATOM   3355 C  C     . GLY A 1 434 ? -1.783  9.174   18.327  1.00 18.20  ? 434  GLY A C     1 
ATOM   3356 O  O     . GLY A 1 434 ? -1.591  8.518   17.316  1.00 19.15  ? 434  GLY A O     1 
ATOM   3357 N  N     . GLY A 1 435 ? -1.037  9.031   19.404  1.00 23.96  ? 435  GLY A N     1 
ATOM   3358 C  CA    . GLY A 1 435 ? -0.116  7.919   19.511  1.00 23.80  ? 435  GLY A CA    1 
ATOM   3359 C  C     . GLY A 1 435 ? 0.156   7.606   20.960  1.00 21.13  ? 435  GLY A C     1 
ATOM   3360 O  O     . GLY A 1 435 ? -0.556  8.067   21.856  1.00 20.36  ? 435  GLY A O     1 
ATOM   3361 N  N     . ARG A 1 436 ? 1.233   6.860   21.190  1.00 19.68  ? 436  ARG A N     1 
ATOM   3362 C  CA    . ARG A 1 436 ? 1.636   6.489   22.544  1.00 22.61  ? 436  ARG A CA    1 
ATOM   3363 C  C     . ARG A 1 436 ? 2.557   7.560   23.118  1.00 21.35  ? 436  ARG A C     1 
ATOM   3364 O  O     . ARG A 1 436 ? 3.730   7.657   22.729  1.00 20.80  ? 436  ARG A O     1 
ATOM   3365 C  CB    . ARG A 1 436 ? 2.321   5.119   22.544  1.00 25.01  ? 436  ARG A CB    1 
ATOM   3366 C  CG    . ARG A 1 436 ? 1.387   3.938   22.420  1.00 20.78  ? 436  ARG A CG    1 
ATOM   3367 C  CD    . ARG A 1 436 ? 2.237   2.750   22.032  1.00 24.78  ? 436  ARG A CD    1 
ATOM   3368 N  NE    . ARG A 1 436 ? 1.413   1.569   21.850  1.00 29.18  ? 436  ARG A NE    1 
ATOM   3369 C  CZ    . ARG A 1 436 ? 1.004   0.782   22.830  1.00 27.51  ? 436  ARG A CZ    1 
ATOM   3370 N  NH1   . ARG A 1 436 ? 1.408   0.961   24.076  1.00 29.84  ? 436  ARG A NH1   1 
ATOM   3371 N  NH2   . ARG A 1 436 ? 0.179   -0.217  22.549  1.00 27.42  ? 436  ARG A NH2   1 
ATOM   3372 N  N     . ARG A 1 437 ? 2.038   8.364   24.040  1.00 19.71  ? 437  ARG A N     1 
ATOM   3373 C  CA    . ARG A 1 437 ? 2.864   9.348   24.743  1.00 24.53  ? 437  ARG A CA    1 
ATOM   3374 C  C     . ARG A 1 437 ? 2.766   9.131   26.246  1.00 25.22  ? 437  ARG A C     1 
ATOM   3375 O  O     . ARG A 1 437 ? 1.774   9.547   26.876  1.00 24.54  ? 437  ARG A O     1 
ATOM   3376 C  CB    . ARG A 1 437 ? 2.468   10.791  24.399  1.00 19.25  ? 437  ARG A CB    1 
ATOM   3377 C  CG    . ARG A 1 437 ? 2.633   11.154  22.946  1.00 21.41  ? 437  ARG A CG    1 
ATOM   3378 C  CD    . ARG A 1 437 ? 4.073   11.102  22.481  1.00 22.97  ? 437  ARG A CD    1 
ATOM   3379 N  NE    . ARG A 1 437 ? 5.037   11.864  23.265  1.00 22.82  ? 437  ARG A NE    1 
ATOM   3380 C  CZ    . ARG A 1 437 ? 5.502   13.059  22.922  1.00 24.15  ? 437  ARG A CZ    1 
ATOM   3381 N  NH1   . ARG A 1 437 ? 4.949   13.757  21.949  1.00 19.66  ? 437  ARG A NH1   1 
ATOM   3382 N  NH2   . ARG A 1 437 ? 6.548   13.564  23.575  1.00 19.79  ? 437  ARG A NH2   1 
ATOM   3383 N  N     . PRO A 1 438 ? 3.779   8.517   26.868  1.00 27.85  ? 438  PRO A N     1 
ATOM   3384 C  CA    . PRO A 1 438 ? 3.694   8.237   28.319  1.00 30.22  ? 438  PRO A CA    1 
ATOM   3385 C  C     . PRO A 1 438 ? 3.606   9.493   29.192  1.00 26.54  ? 438  PRO A C     1 
ATOM   3386 O  O     . PRO A 1 438 ? 3.132   9.423   30.333  1.00 28.15  ? 438  PRO A O     1 
ATOM   3387 C  CB    . PRO A 1 438 ? 4.985   7.443   28.600  1.00 30.38  ? 438  PRO A CB    1 
ATOM   3388 C  CG    . PRO A 1 438 ? 5.901   7.730   27.432  1.00 34.18  ? 438  PRO A CG    1 
ATOM   3389 C  CD    . PRO A 1 438 ? 5.006   7.993   26.246  1.00 27.27  ? 438  PRO A CD    1 
ATOM   3390 N  N     . ALA A 1 439 ? 4.003   10.650  28.679  1.00 26.15  ? 439  ALA A N     1 
ATOM   3391 C  CA    . ALA A 1 439 ? 4.130   11.832  29.511  1.00 29.10  ? 439  ALA A CA    1 
ATOM   3392 C  C     . ALA A 1 439 ? 3.722   13.049  28.706  1.00 27.47  ? 439  ALA A C     1 
ATOM   3393 O  O     . ALA A 1 439 ? 3.785   13.045  27.471  1.00 24.93  ? 439  ALA A O     1 
ATOM   3394 C  CB    . ALA A 1 439 ? 5.572   12.009  30.027  1.00 25.49  ? 439  ALA A CB    1 
ATOM   3395 N  N     . GLY A 1 440 ? 3.297   14.081  29.434  1.00 23.39  ? 440  GLY A N     1 
ATOM   3396 C  CA    . GLY A 1 440 ? 3.222   15.441  28.909  1.00 28.83  ? 440  GLY A CA    1 
ATOM   3397 C  C     . GLY A 1 440 ? 1.999   15.790  28.078  1.00 29.43  ? 440  GLY A C     1 
ATOM   3398 O  O     . GLY A 1 440 ? 1.527   16.934  28.123  1.00 26.22  ? 440  GLY A O     1 
ATOM   3399 N  N     . VAL A 1 441 ? 1.473   14.823  27.332  1.00 25.35  ? 441  VAL A N     1 
ATOM   3400 C  CA    . VAL A 1 441 ? 0.420   15.060  26.340  1.00 21.22  ? 441  VAL A CA    1 
ATOM   3401 C  C     . VAL A 1 441 ? -0.926  14.687  26.951  1.00 23.72  ? 441  VAL A C     1 
ATOM   3402 O  O     . VAL A 1 441 ? -1.103  13.530  27.370  1.00 23.85  ? 441  VAL A O     1 
ATOM   3403 C  CB    . VAL A 1 441 ? 0.670   14.260  25.056  1.00 25.08  ? 441  VAL A CB    1 
ATOM   3404 C  CG1   . VAL A 1 441 ? -0.418  14.568  24.039  1.00 23.03  ? 441  VAL A CG1   1 
ATOM   3405 C  CG2   . VAL A 1 441 ? 2.066   14.560  24.500  1.00 23.72  ? 441  VAL A CG2   1 
ATOM   3406 N  N     . PRO A 1 442 ? -1.908  15.592  26.981  1.00 25.25  ? 442  PRO A N     1 
ATOM   3407 C  CA    . PRO A 1 442 ? -3.170  15.297  27.664  1.00 23.71  ? 442  PRO A CA    1 
ATOM   3408 C  C     . PRO A 1 442 ? -4.066  14.340  26.883  1.00 22.48  ? 442  PRO A C     1 
ATOM   3409 O  O     . PRO A 1 442 ? -3.819  13.968  25.730  1.00 20.13  ? 442  PRO A O     1 
ATOM   3410 C  CB    . PRO A 1 442 ? -3.830  16.678  27.829  1.00 27.38  ? 442  PRO A CB    1 
ATOM   3411 C  CG    . PRO A 1 442 ? -3.189  17.546  26.873  1.00 27.08  ? 442  PRO A CG    1 
ATOM   3412 C  CD    . PRO A 1 442 ? -1.827  17.008  26.551  1.00 23.09  ? 442  PRO A CD    1 
ATOM   3413 N  N     . LEU A 1 443 ? -5.110  13.906  27.584  1.00 20.26  ? 443  LEU A N     1 
ATOM   3414 C  CA    . LEU A 1 443 ? -6.023  12.883  27.075  1.00 18.93  ? 443  LEU A CA    1 
ATOM   3415 C  C     . LEU A 1 443 ? -6.654  13.295  25.756  1.00 19.90  ? 443  LEU A C     1 
ATOM   3416 O  O     . LEU A 1 443 ? -6.764  12.478  24.825  1.00 22.83  ? 443  LEU A O     1 
ATOM   3417 C  CB    . LEU A 1 443 ? -7.127  12.589  28.103  1.00 19.23  ? 443  LEU A CB    1 
ATOM   3418 C  CG    . LEU A 1 443 ? -8.215  11.596  27.668  1.00 20.68  ? 443  LEU A CG    1 
ATOM   3419 C  CD1   . LEU A 1 443 ? -7.615  10.188  27.506  1.00 16.92  ? 443  LEU A CD1   1 
ATOM   3420 C  CD2   . LEU A 1 443 ? -9.385  11.542  28.628  1.00 23.54  ? 443  LEU A CD2   1 
ATOM   3421 N  N     . VAL A 1 444 ? -7.085  14.543  25.648  1.00 19.06  ? 444  VAL A N     1 
ATOM   3422 C  CA    . VAL A 1 444 ? -7.701  14.980  24.406  1.00 19.85  ? 444  VAL A CA    1 
ATOM   3423 C  C     . VAL A 1 444 ? -7.554  16.491  24.287  1.00 22.04  ? 444  VAL A C     1 
ATOM   3424 O  O     . VAL A 1 444 ? -7.647  17.236  25.279  1.00 21.14  ? 444  VAL A O     1 
ATOM   3425 C  CB    . VAL A 1 444 ? -9.178  14.521  24.297  1.00 19.29  ? 444  VAL A CB    1 
ATOM   3426 C  CG1   . VAL A 1 444 ? -10.047 15.114  25.420  1.00 18.94  ? 444  VAL A CG1   1 
ATOM   3427 C  CG2   . VAL A 1 444 ? -9.755  14.894  22.899  1.00 18.55  ? 444  VAL A CG2   1 
ATOM   3428 N  N     . TYR A 1 445 ? -7.303  16.941  23.058  1.00 20.22  ? 445  TYR A N     1 
ATOM   3429 C  CA    . TYR A 1 445 ? -7.438  18.367  22.767  1.00 20.62  ? 445  TYR A CA    1 
ATOM   3430 C  C     . TYR A 1 445 ? -7.908  18.537  21.322  1.00 23.55  ? 445  TYR A C     1 
ATOM   3431 O  O     . TYR A 1 445 ? -7.856  17.605  20.516  1.00 22.74  ? 445  TYR A O     1 
ATOM   3432 C  CB    . TYR A 1 445 ? -6.142  19.137  23.059  1.00 16.66  ? 445  TYR A CB    1 
ATOM   3433 C  CG    . TYR A 1 445 ? -4.913  18.808  22.219  1.00 17.81  ? 445  TYR A CG    1 
ATOM   3434 C  CD1   . TYR A 1 445 ? -4.034  17.807  22.600  1.00 15.35  ? 445  TYR A CD1   1 
ATOM   3435 C  CD2   . TYR A 1 445 ? -4.592  19.559  21.092  1.00 22.23  ? 445  TYR A CD2   1 
ATOM   3436 C  CE1   . TYR A 1 445 ? -2.892  17.529  21.858  1.00 18.10  ? 445  TYR A CE1   1 
ATOM   3437 C  CE2   . TYR A 1 445 ? -3.443  19.286  20.332  1.00 18.54  ? 445  TYR A CE2   1 
ATOM   3438 C  CZ    . TYR A 1 445 ? -2.592  18.287  20.737  1.00 20.68  ? 445  TYR A CZ    1 
ATOM   3439 O  OH    . TYR A 1 445 ? -1.461  18.001  19.991  1.00 23.27  ? 445  TYR A OH    1 
ATOM   3440 N  N     . GLU A 1 446 ? -8.443  19.718  21.026  1.00 21.12  ? 446  GLU A N     1 
ATOM   3441 C  CA    . GLU A 1 446 ? -8.999  20.044  19.718  1.00 18.12  ? 446  GLU A CA    1 
ATOM   3442 C  C     . GLU A 1 446 ? -8.176  21.171  19.100  1.00 20.29  ? 446  GLU A C     1 
ATOM   3443 O  O     . GLU A 1 446 ? -7.815  22.126  19.793  1.00 18.92  ? 446  GLU A O     1 
ATOM   3444 C  CB    . GLU A 1 446 ? -10.463 20.469  19.851  1.00 16.25  ? 446  GLU A CB    1 
ATOM   3445 C  CG    . GLU A 1 446 ? -11.114 21.078  18.617  1.00 21.62  ? 446  GLU A CG    1 
ATOM   3446 C  CD    . GLU A 1 446 ? -12.459 21.707  18.960  1.00 27.37  ? 446  GLU A CD    1 
ATOM   3447 O  OE1   . GLU A 1 446 ? -13.050 21.286  19.962  1.00 25.70  ? 446  GLU A OE1   1 
ATOM   3448 O  OE2   . GLU A 1 446 ? -12.929 22.614  18.251  1.00 23.31  ? 446  GLU A OE2   1 
ATOM   3449 N  N     . ALA A 1 447 ? -7.870  21.044  17.812  1.00 19.08  ? 447  ALA A N     1 
ATOM   3450 C  CA    . ALA A 1 447 ? -7.000  22.000  17.134  1.00 16.41  ? 447  ALA A CA    1 
ATOM   3451 C  C     . ALA A 1 447 ? -7.736  23.328  16.938  1.00 22.14  ? 447  ALA A C     1 
ATOM   3452 O  O     . ALA A 1 447 ? -8.968  23.385  16.935  1.00 21.90  ? 447  ALA A O     1 
ATOM   3453 C  CB    . ALA A 1 447 ? -6.524  21.416  15.787  1.00 18.68  ? 447  ALA A CB    1 
ATOM   3454 N  N     . LEU A 1 448 ? -6.960  24.417  16.767  1.00 18.97  ? 448  LEU A N     1 
ATOM   3455 C  CA    . LEU A 1 448 ? -7.544  25.762  16.729  1.00 23.21  ? 448  LEU A CA    1 
ATOM   3456 C  C     . LEU A 1 448 ? -8.067  26.146  15.359  1.00 23.65  ? 448  LEU A C     1 
ATOM   3457 O  O     . LEU A 1 448 ? -8.860  27.076  15.268  1.00 22.40  ? 448  LEU A O     1 
ATOM   3458 C  CB    . LEU A 1 448 ? -6.529  26.814  17.160  1.00 20.50  ? 448  LEU A CB    1 
ATOM   3459 C  CG    . LEU A 1 448 ? -5.836  26.586  18.499  1.00 22.09  ? 448  LEU A CG    1 
ATOM   3460 C  CD1   . LEU A 1 448 ? -4.622  27.517  18.565  1.00 25.75  ? 448  LEU A CD1   1 
ATOM   3461 C  CD2   . LEU A 1 448 ? -6.811  26.845  19.646  1.00 22.39  ? 448  LEU A CD2   1 
ATOM   3462 N  N     . SER A 1 449 ? -7.675  25.440  14.309  1.00 19.21  ? 449  SER A N     1 
ATOM   3463 C  CA    . SER A 1 449 ? -8.050  25.783  12.946  1.00 20.57  ? 449  SER A CA    1 
ATOM   3464 C  C     . SER A 1 449 ? -7.570  24.643  12.063  1.00 21.38  ? 449  SER A C     1 
ATOM   3465 O  O     . SER A 1 449 ? -6.871  23.740  12.525  1.00 19.89  ? 449  SER A O     1 
ATOM   3466 C  CB    . SER A 1 449 ? -7.401  27.097  12.500  1.00 23.56  ? 449  SER A CB    1 
ATOM   3467 O  OG    . SER A 1 449 ? -5.988  26.898  12.426  1.00 20.86  ? 449  SER A OG    1 
ATOM   3468 N  N     . TRP A 1 450 ? -7.935  24.701  10.781  1.00 21.92  ? 450  TRP A N     1 
ATOM   3469 C  CA    . TRP A 1 450 ? -7.442  23.690  9.843   1.00 20.89  ? 450  TRP A CA    1 
ATOM   3470 C  C     . TRP A 1 450 ? -5.923  23.662  9.815   1.00 21.81  ? 450  TRP A C     1 
ATOM   3471 O  O     . TRP A 1 450 ? -5.308  22.591  9.891   1.00 22.45  ? 450  TRP A O     1 
ATOM   3472 C  CB    . TRP A 1 450 ? -7.990  23.943  8.442   1.00 20.95  ? 450  TRP A CB    1 
ATOM   3473 C  CG    . TRP A 1 450 ? -7.650  22.856  7.492   1.00 19.55  ? 450  TRP A CG    1 
ATOM   3474 C  CD1   . TRP A 1 450 ? -6.776  22.927  6.451   1.00 21.12  ? 450  TRP A CD1   1 
ATOM   3475 C  CD2   . TRP A 1 450 ? -8.183  21.523  7.482   1.00 17.92  ? 450  TRP A CD2   1 
ATOM   3476 N  NE1   . TRP A 1 450 ? -6.727  21.726  5.789   1.00 22.02  ? 450  TRP A NE1   1 
ATOM   3477 C  CE2   . TRP A 1 450 ? -7.573  20.842  6.409   1.00 21.50  ? 450  TRP A CE2   1 
ATOM   3478 C  CE3   . TRP A 1 450 ? -9.108  20.838  8.287   1.00 21.83  ? 450  TRP A CE3   1 
ATOM   3479 C  CZ2   . TRP A 1 450 ? -7.856  19.512  6.109   1.00 23.58  ? 450  TRP A CZ2   1 
ATOM   3480 C  CZ3   . TRP A 1 450 ? -9.395  19.500  7.987   1.00 20.90  ? 450  TRP A CZ3   1 
ATOM   3481 C  CH2   . TRP A 1 450 ? -8.771  18.859  6.905   1.00 24.72  ? 450  TRP A CH2   1 
ATOM   3482 N  N     . GLN A 1 451 ? -5.293  24.837  9.696   1.00 20.90  ? 451  GLN A N     1 
ATOM   3483 C  CA    . GLN A 1 451 ? -3.844  24.865  9.582   1.00 21.35  ? 451  GLN A CA    1 
ATOM   3484 C  C     . GLN A 1 451 ? -3.184  24.343  10.851  1.00 17.87  ? 451  GLN A C     1 
ATOM   3485 O  O     . GLN A 1 451 ? -2.195  23.601  10.782  1.00 17.65  ? 451  GLN A O     1 
ATOM   3486 C  CB    . GLN A 1 451 ? -3.372  26.299  9.254   1.00 22.10  ? 451  GLN A CB    1 
ATOM   3487 C  CG    . GLN A 1 451 ? -3.877  26.773  7.893   1.00 25.76  ? 451  GLN A CG    1 
ATOM   3488 C  CD    . GLN A 1 451 ? -5.345  27.218  7.882   1.00 33.25  ? 451  GLN A CD    1 
ATOM   3489 O  OE1   . GLN A 1 451 ? -5.912  27.628  8.914   1.00 28.28  ? 451  GLN A OE1   1 
ATOM   3490 N  NE2   . GLN A 1 451 ? -5.976  27.122  6.705   1.00 30.49  ? 451  GLN A NE2   1 
ATOM   3491 N  N     . HIS A 1 452 ? -3.709  24.725  12.013  1.00 17.96  ? 452  HIS A N     1 
ATOM   3492 C  CA    . HIS A 1 452 ? -3.201  24.148  13.251  1.00 18.41  ? 452  HIS A CA    1 
ATOM   3493 C  C     . HIS A 1 452 ? -3.422  22.633  13.268  1.00 18.00  ? 452  HIS A C     1 
ATOM   3494 O  O     . HIS A 1 452 ? -2.573  21.884  13.749  1.00 17.26  ? 452  HIS A O     1 
ATOM   3495 C  CB    . HIS A 1 452 ? -3.872  24.813  14.457  1.00 17.00  ? 452  HIS A CB    1 
ATOM   3496 C  CG    . HIS A 1 452 ? -3.380  24.290  15.772  1.00 20.98  ? 452  HIS A CG    1 
ATOM   3497 N  ND1   . HIS A 1 452 ? -4.228  23.877  16.783  1.00 21.65  ? 452  HIS A ND1   1 
ATOM   3498 C  CD2   . HIS A 1 452 ? -2.122  24.082  16.231  1.00 20.76  ? 452  HIS A CD2   1 
ATOM   3499 C  CE1   . HIS A 1 452 ? -3.512  23.461  17.814  1.00 19.83  ? 452  HIS A CE1   1 
ATOM   3500 N  NE2   . HIS A 1 452 ? -2.231  23.588  17.512  1.00 19.86  ? 452  HIS A NE2   1 
ATOM   3501 N  N     . GLY A 1 453 ? -4.573  22.177  12.765  1.00 19.21  ? 453  GLY A N     1 
ATOM   3502 C  CA    . GLY A 1 453 ? -4.858  20.758  12.731  1.00 15.23  ? 453  GLY A CA    1 
ATOM   3503 C  C     . GLY A 1 453 ? -3.859  20.001  11.884  1.00 17.67  ? 453  GLY A C     1 
ATOM   3504 O  O     . GLY A 1 453 ? -3.369  18.947  12.296  1.00 21.13  ? 453  GLY A O     1 
ATOM   3505 N  N     . VAL A 1 454 ? -3.507  20.557  10.712  1.00 18.72  ? 454  VAL A N     1 
ATOM   3506 C  CA    . VAL A 1 454 ? -2.482  19.952  9.863   1.00 18.02  ? 454  VAL A CA    1 
ATOM   3507 C  C     . VAL A 1 454 ? -1.141  19.917  10.591  1.00 20.65  ? 454  VAL A C     1 
ATOM   3508 O  O     . VAL A 1 454 ? -0.428  18.909  10.552  1.00 19.38  ? 454  VAL A O     1 
ATOM   3509 C  CB    . VAL A 1 454 ? -2.380  20.693  8.510   1.00 18.10  ? 454  VAL A CB    1 
ATOM   3510 C  CG1   . VAL A 1 454 ? -1.316  20.017  7.621   1.00 17.96  ? 454  VAL A CG1   1 
ATOM   3511 C  CG2   . VAL A 1 454 ? -3.716  20.654  7.785   1.00 19.22  ? 454  VAL A CG2   1 
ATOM   3512 N  N     . PHE A 1 455 ? -0.789  20.999  11.291  1.00 19.13  ? 455  PHE A N     1 
ATOM   3513 C  CA    . PHE A 1 455 ? 0.433   20.979  12.107  1.00 20.15  ? 455  PHE A CA    1 
ATOM   3514 C  C     . PHE A 1 455 ? 0.395   19.869  13.175  1.00 18.03  ? 455  PHE A C     1 
ATOM   3515 O  O     . PHE A 1 455 ? 1.403   19.195  13.419  1.00 19.39  ? 455  PHE A O     1 
ATOM   3516 C  CB    . PHE A 1 455 ? 0.649   22.361  12.749  1.00 17.60  ? 455  PHE A CB    1 
ATOM   3517 C  CG    . PHE A 1 455 ? 1.671   22.360  13.852  1.00 18.85  ? 455  PHE A CG    1 
ATOM   3518 C  CD1   . PHE A 1 455 ? 3.017   22.475  13.566  1.00 20.64  ? 455  PHE A CD1   1 
ATOM   3519 C  CD2   . PHE A 1 455 ? 1.275   22.202  15.184  1.00 19.64  ? 455  PHE A CD2   1 
ATOM   3520 C  CE1   . PHE A 1 455 ? 3.968   22.443  14.585  1.00 18.23  ? 455  PHE A CE1   1 
ATOM   3521 C  CE2   . PHE A 1 455 ? 2.204   22.171  16.196  1.00 22.22  ? 455  PHE A CE2   1 
ATOM   3522 C  CZ    . PHE A 1 455 ? 3.551   22.306  15.904  1.00 21.82  ? 455  PHE A CZ    1 
ATOM   3523 N  N     . VAL A 1 456 ? -0.733  19.710  13.867  1.00 17.37  ? 456  VAL A N     1 
ATOM   3524 C  CA    . VAL A 1 456 ? -0.871  18.632  14.866  1.00 17.08  ? 456  VAL A CA    1 
ATOM   3525 C  C     . VAL A 1 456 ? -0.558  17.264  14.252  1.00 18.01  ? 456  VAL A C     1 
ATOM   3526 O  O     . VAL A 1 456 ? 0.198   16.460  14.823  1.00 18.54  ? 456  VAL A O     1 
ATOM   3527 C  CB    . VAL A 1 456 ? -2.274  18.670  15.487  1.00 18.12  ? 456  VAL A CB    1 
ATOM   3528 C  CG1   . VAL A 1 456 ? -2.529  17.457  16.414  1.00 19.73  ? 456  VAL A CG1   1 
ATOM   3529 C  CG2   . VAL A 1 456 ? -2.443  19.987  16.252  1.00 16.45  ? 456  VAL A CG2   1 
ATOM   3530 N  N     . GLY A 1 457 ? -1.121  16.979  13.079  1.00 14.97  ? 457  GLY A N     1 
ATOM   3531 C  CA    . GLY A 1 457 ? -0.764  15.735  12.389  1.00 15.81  ? 457  GLY A CA    1 
ATOM   3532 C  C     . GLY A 1 457 ? 0.715   15.640  12.077  1.00 16.89  ? 457  GLY A C     1 
ATOM   3533 O  O     . GLY A 1 457 ? 1.327   14.593  12.285  1.00 15.57  ? 457  GLY A O     1 
ATOM   3534 N  N     . ALA A 1 458 ? 1.325   16.753  11.613  1.00 14.97  ? 458  ALA A N     1 
ATOM   3535 C  CA    . ALA A 1 458 ? 2.717   16.749  11.214  1.00 18.67  ? 458  ALA A CA    1 
ATOM   3536 C  C     . ALA A 1 458 ? 3.628   16.514  12.405  1.00 16.88  ? 458  ALA A C     1 
ATOM   3537 O  O     . ALA A 1 458 ? 4.706   15.932  12.258  1.00 18.57  ? 458  ALA A O     1 
ATOM   3538 C  CB    . ALA A 1 458 ? 3.074   18.094  10.533  1.00 14.38  ? 458  ALA A CB    1 
ATOM   3539 N  N     . ALA A 1 459 ? 3.197   16.937  13.580  1.00 13.82  ? 459  ALA A N     1 
ATOM   3540 C  CA    . ALA A 1 459 ? 3.992   16.873  14.795  1.00 18.21  ? 459  ALA A CA    1 
ATOM   3541 C  C     . ALA A 1 459 ? 3.816   15.564  15.570  1.00 19.61  ? 459  ALA A C     1 
ATOM   3542 O  O     . ALA A 1 459 ? 4.414   15.421  16.643  1.00 20.80  ? 459  ALA A O     1 
ATOM   3543 C  CB    . ALA A 1 459 ? 3.622   18.040  15.703  1.00 16.97  ? 459  ALA A CB    1 
ATOM   3544 N  N     . MET A 1 460 ? 3.029   14.617  15.070  1.00 19.76  ? 460  MET A N     1 
ATOM   3545 C  CA    . MET A 1 460 ? 2.777   13.381  15.829  1.00 20.01  ? 460  MET A CA    1 
ATOM   3546 C  C     . MET A 1 460 ? 4.070   12.655  16.160  1.00 18.67  ? 460  MET A C     1 
ATOM   3547 O  O     . MET A 1 460 ? 4.975   12.538  15.321  1.00 20.65  ? 460  MET A O     1 
ATOM   3548 C  CB    . MET A 1 460 ? 1.860   12.420  15.054  1.00 15.74  ? 460  MET A CB    1 
ATOM   3549 C  CG    . MET A 1 460 ? 0.447   12.891  15.026  1.00 17.96  ? 460  MET A CG    1 
ATOM   3550 S  SD    . MET A 1 460 ? -0.561  11.882  13.939  1.00 20.55  ? 460  MET A SD    1 
ATOM   3551 C  CE    . MET A 1 460 ? -0.330  10.272  14.650  1.00 17.89  ? 460  MET A CE    1 
ATOM   3552 N  N     . ARG A 1 461 ? 4.138   12.169  17.389  1.00 16.20  ? 461  ARG A N     1 
ATOM   3553 C  CA    . ARG A 1 461 ? 5.222   11.357  17.894  1.00 19.25  ? 461  ARG A CA    1 
ATOM   3554 C  C     . ARG A 1 461 ? 4.629   10.240  18.733  1.00 22.20  ? 461  ARG A C     1 
ATOM   3555 O  O     . ARG A 1 461 ? 3.549   10.379  19.303  1.00 18.70  ? 461  ARG A O     1 
ATOM   3556 C  CB    . ARG A 1 461 ? 6.192   12.166  18.739  1.00 19.66  ? 461  ARG A CB    1 
ATOM   3557 C  CG    . ARG A 1 461 ? 6.873   13.311  17.943  1.00 18.44  ? 461  ARG A CG    1 
ATOM   3558 C  CD    . ARG A 1 461 ? 7.631   14.160  18.901  1.00 19.97  ? 461  ARG A CD    1 
ATOM   3559 N  NE    . ARG A 1 461 ? 8.888   13.545  19.265  1.00 23.62  ? 461  ARG A NE    1 
ATOM   3560 C  CZ    . ARG A 1 461 ? 9.607   13.884  20.325  1.00 26.94  ? 461  ARG A CZ    1 
ATOM   3561 N  NH1   . ARG A 1 461 ? 9.161   14.756  21.216  1.00 22.11  ? 461  ARG A NH1   1 
ATOM   3562 N  NH2   . ARG A 1 461 ? 10.801  13.324  20.502  1.00 24.98  ? 461  ARG A NH2   1 
ATOM   3563 N  N     . SER A 1 462 ? 5.371   9.153   18.863  1.00 17.94  ? 462  SER A N     1 
ATOM   3564 C  CA    . SER A 1 462 ? 4.806   7.984   19.542  1.00 22.03  ? 462  SER A CA    1 
ATOM   3565 C  C     . SER A 1 462 ? 5.947   7.077   20.002  1.00 26.31  ? 462  SER A C     1 
ATOM   3566 O  O     . SER A 1 462 ? 6.947   6.948   19.305  1.00 26.52  ? 462  SER A O     1 
ATOM   3567 C  CB    . SER A 1 462 ? 3.861   7.247   18.580  1.00 18.56  ? 462  SER A CB    1 
ATOM   3568 O  OG    . SER A 1 462 ? 3.162   6.178   19.185  1.00 22.39  ? 462  SER A OG    1 
ATOM   3569 N  N     . GLU A 1 463 ? 5.810   6.463   21.177  1.00 25.92  ? 463  GLU A N     1 
ATOM   3570 C  CA    . GLU A 1 463 ? 6.915   5.659   21.683  1.00 34.59  ? 463  GLU A CA    1 
ATOM   3571 C  C     . GLU A 1 463 ? 7.021   4.376   20.871  1.00 29.80  ? 463  GLU A C     1 
ATOM   3572 O  O     . GLU A 1 463 ? 6.012   3.804   20.446  1.00 35.36  ? 463  GLU A O     1 
ATOM   3573 C  CB    . GLU A 1 463 ? 6.746   5.345   23.176  1.00 34.85  ? 463  GLU A CB    1 
ATOM   3574 C  CG    . GLU A 1 463 ? 5.708   4.335   23.486  1.00 43.01  ? 463  GLU A CG    1 
ATOM   3575 C  CD    . GLU A 1 463 ? 5.678   3.967   24.967  1.00 47.97  ? 463  GLU A CD    1 
ATOM   3576 O  OE1   . GLU A 1 463 ? 6.618   4.372   25.704  1.00 46.02  ? 463  GLU A OE1   1 
ATOM   3577 O  OE2   . GLU A 1 463 ? 4.706   3.283   25.383  1.00 57.35  ? 463  GLU A OE2   1 
ATOM   3578 N  N     . ALA A 1 464 ? 8.253   3.951   20.620  1.00 39.22  ? 464  ALA A N     1 
ATOM   3579 C  CA    . ALA A 1 464 ? 8.493   2.795   19.759  1.00 56.32  ? 464  ALA A CA    1 
ATOM   3580 C  C     . ALA A 1 464 ? 7.908   1.519   20.362  1.00 66.30  ? 464  ALA A C     1 
ATOM   3581 O  O     . ALA A 1 464 ? 7.953   1.312   21.579  1.00 64.40  ? 464  ALA A O     1 
ATOM   3582 C  CB    . ALA A 1 464 ? 9.992   2.620   19.515  1.00 67.43  ? 464  ALA A CB    1 
ATOM   3583 N  N     . THR A 1 465 ? 7.360   0.658   19.493  1.00 74.87  ? 465  THR A N     1 
ATOM   3584 C  CA    . THR A 1 465 ? 6.696   -0.579  19.901  1.00 87.82  ? 465  THR A CA    1 
ATOM   3585 C  C     . THR A 1 465 ? 7.282   -1.810  19.215  1.00 112.21 ? 465  THR A C     1 
ATOM   3586 O  O     . THR A 1 465 ? 8.484   -2.073  19.319  1.00 112.27 ? 465  THR A O     1 
ATOM   3587 C  CB    . THR A 1 465 ? 5.197   -0.517  19.599  1.00 80.43  ? 465  THR A CB    1 
ATOM   3588 O  OG1   . THR A 1 465 ? 4.996   -0.035  18.261  1.00 78.71  ? 465  THR A OG1   1 
ATOM   3589 C  CG2   . THR A 1 465 ? 4.472   0.374   20.600  1.00 59.20  ? 465  THR A CG2   1 
ATOM   3590 N  N     . ALA A 1 466 ? 6.438   -2.573  18.521  1.00 148.96 ? 466  ALA A N     1 
ATOM   3591 C  CA    . ALA A 1 466 ? 6.843   -3.824  17.879  1.00 152.41 ? 466  ALA A CA    1 
ATOM   3592 C  C     . ALA A 1 466 ? 5.902   -4.164  16.722  1.00 151.65 ? 466  ALA A C     1 
ATOM   3593 O  O     . ALA A 1 466 ? 5.254   -5.210  16.694  1.00 151.19 ? 466  ALA A O     1 
ATOM   3594 C  CB    . ALA A 1 466 ? 6.894   -4.957  18.902  1.00 154.65 ? 466  ALA A CB    1 
ATOM   3595 N  N     . ALA A 1 467 ? 5.829   -3.271  15.731  1.00 131.33 ? 467  ALA A N     1 
ATOM   3596 C  CA    . ALA A 1 467 ? 5.086   -3.496  14.490  1.00 115.35 ? 467  ALA A CA    1 
ATOM   3597 C  C     . ALA A 1 467 ? 5.980   -3.617  13.264  1.00 110.63 ? 467  ALA A C     1 
ATOM   3598 O  O     . ALA A 1 467 ? 5.695   -4.425  12.375  1.00 98.06  ? 467  ALA A O     1 
ATOM   3599 C  CB    . ALA A 1 467 ? 4.074   -2.369  14.264  1.00 91.98  ? 467  ALA A CB    1 
ATOM   3600 N  N     . ALA A 1 468 ? 7.049   -2.821  13.187  1.00 119.25 ? 468  ALA A N     1 
ATOM   3601 C  CA    . ALA A 1 468 ? 8.071   -2.999  12.162  1.00 112.20 ? 468  ALA A CA    1 
ATOM   3602 C  C     . ALA A 1 468 ? 9.296   -3.684  12.760  1.00 120.44 ? 468  ALA A C     1 
ATOM   3603 O  O     . ALA A 1 468 ? 9.168   -4.682  13.480  1.00 119.97 ? 468  ALA A O     1 
ATOM   3604 C  CB    . ALA A 1 468 ? 8.460   -1.657  11.542  1.00 105.08 ? 468  ALA A CB    1 
ATOM   3605 N  N     . GLU A 1 469 ? 10.488  -3.158  12.474  1.00 120.36 ? 469  GLU A N     1 
ATOM   3606 C  CA    . GLU A 1 469 ? 11.718  -3.645  13.083  1.00 118.50 ? 469  GLU A CA    1 
ATOM   3607 C  C     . GLU A 1 469 ? 12.210  -2.735  14.205  1.00 125.33 ? 469  GLU A C     1 
ATOM   3608 O  O     . GLU A 1 469 ? 13.317  -2.937  14.715  1.00 120.46 ? 469  GLU A O     1 
ATOM   3609 C  CB    . GLU A 1 469 ? 12.805  -3.817  12.017  1.00 103.24 ? 469  GLU A CB    1 
ATOM   3610 C  CG    . GLU A 1 469 ? 13.192  -2.541  11.284  1.00 95.61  ? 469  GLU A CG    1 
ATOM   3611 C  CD    . GLU A 1 469 ? 12.456  -2.365  9.968   1.00 73.64  ? 469  GLU A CD    1 
ATOM   3612 O  OE1   . GLU A 1 469 ? 11.207  -2.362  9.965   1.00 71.12  ? 469  GLU A OE1   1 
ATOM   3613 O  OE2   . GLU A 1 469 ? 13.137  -2.234  8.931   1.00 59.09  ? 469  GLU A OE2   1 
ATOM   3614 N  N     . HIS A 1 470 ? 11.406  -1.751  14.607  1.00 138.95 ? 470  HIS A N     1 
ATOM   3615 C  CA    . HIS A 1 470 ? 11.784  -0.835  15.674  1.00 144.62 ? 470  HIS A CA    1 
ATOM   3616 C  C     . HIS A 1 470 ? 11.470  -1.445  17.036  1.00 144.31 ? 470  HIS A C     1 
ATOM   3617 O  O     . HIS A 1 470 ? 10.445  -2.109  17.215  1.00 141.65 ? 470  HIS A O     1 
ATOM   3618 C  CB    . HIS A 1 470 ? 11.060  0.505   15.503  1.00 140.20 ? 470  HIS A CB    1 
ATOM   3619 C  CG    . HIS A 1 470 ? 11.250  1.126   14.152  1.00 137.25 ? 470  HIS A CG    1 
ATOM   3620 N  ND1   . HIS A 1 470 ? 12.285  1.991   13.868  1.00 141.17 ? 470  HIS A ND1   1 
ATOM   3621 C  CD2   . HIS A 1 470 ? 10.543  0.997   13.004  1.00 131.89 ? 470  HIS A CD2   1 
ATOM   3622 C  CE1   . HIS A 1 470 ? 12.206  2.372   12.605  1.00 134.50 ? 470  HIS A CE1   1 
ATOM   3623 N  NE2   . HIS A 1 470 ? 11.158  1.783   12.058  1.00 129.42 ? 470  HIS A NE2   1 
ATOM   3624 N  N     . LYS A 1 471 ? 12.372  -1.230  17.995  1.00 137.89 ? 471  LYS A N     1 
ATOM   3625 C  CA    . LYS A 1 471 ? 12.231  -1.769  19.342  1.00 133.34 ? 471  LYS A CA    1 
ATOM   3626 C  C     . LYS A 1 471 ? 12.694  -0.724  20.352  1.00 132.24 ? 471  LYS A C     1 
ATOM   3627 O  O     . LYS A 1 471 ? 13.382  0.241   20.007  1.00 125.22 ? 471  LYS A O     1 
ATOM   3628 C  CB    . LYS A 1 471 ? 13.025  -3.080  19.513  1.00 131.65 ? 471  LYS A CB    1 
ATOM   3629 C  CG    . LYS A 1 471 ? 12.623  -4.202  18.551  1.00 127.22 ? 471  LYS A CG    1 
ATOM   3630 C  CD    . LYS A 1 471 ? 13.561  -5.398  18.653  1.00 125.27 ? 471  LYS A CD    1 
ATOM   3631 C  CE    . LYS A 1 471 ? 13.197  -6.483  17.647  1.00 117.71 ? 471  LYS A CE    1 
ATOM   3632 N  NZ    . LYS A 1 471 ? 14.112  -7.654  17.741  1.00 113.55 ? 471  LYS A NZ    1 
ATOM   3633 N  N     . GLY A 1 472 ? 12.295  -0.920  21.611  1.00 131.08 ? 472  GLY A N     1 
ATOM   3634 C  CA    . GLY A 1 472 ? 12.697  -0.049  22.704  1.00 121.64 ? 472  GLY A CA    1 
ATOM   3635 C  C     . GLY A 1 472 ? 11.657  1.012   23.023  1.00 118.73 ? 472  GLY A C     1 
ATOM   3636 O  O     . GLY A 1 472 ? 10.618  1.139   22.367  1.00 116.63 ? 472  GLY A O     1 
ATOM   3637 N  N     . LYS A 1 473 ? 11.956  1.791   24.065  1.00 98.38  ? 473  LYS A N     1 
ATOM   3638 C  CA    . LYS A 1 473 ? 11.082  2.885   24.504  1.00 83.59  ? 473  LYS A CA    1 
ATOM   3639 C  C     . LYS A 1 473 ? 11.697  4.238   24.140  1.00 73.24  ? 473  LYS A C     1 
ATOM   3640 O  O     . LYS A 1 473 ? 12.052  5.062   24.982  1.00 70.16  ? 473  LYS A O     1 
ATOM   3641 C  CB    . LYS A 1 473 ? 10.801  2.777   26.003  1.00 83.83  ? 473  LYS A CB    1 
ATOM   3642 C  CG    . LYS A 1 473 ? 10.475  1.363   26.489  1.00 86.62  ? 473  LYS A CG    1 
ATOM   3643 C  CD    . LYS A 1 473 ? 9.275   0.739   25.768  1.00 89.38  ? 473  LYS A CD    1 
ATOM   3644 C  CE    . LYS A 1 473 ? 7.944   1.147   26.398  1.00 83.51  ? 473  LYS A CE    1 
ATOM   3645 N  NZ    . LYS A 1 473 ? 6.778   0.411   25.813  1.00 74.61  ? 473  LYS A NZ    1 
ATOM   3646 N  N     . VAL A 1 474 ? 11.830  4.429   22.836  1.00 65.69  ? 474  VAL A N     1 
ATOM   3647 C  CA    . VAL A 1 474 ? 12.260  5.665   22.201  1.00 43.85  ? 474  VAL A CA    1 
ATOM   3648 C  C     . VAL A 1 474 ? 11.008  6.373   21.711  1.00 34.04  ? 474  VAL A C     1 
ATOM   3649 O  O     . VAL A 1 474 ? 10.015  5.729   21.363  1.00 40.43  ? 474  VAL A O     1 
ATOM   3650 C  CB    . VAL A 1 474 ? 13.232  5.339   21.042  1.00 36.50  ? 474  VAL A CB    1 
ATOM   3651 C  CG1   . VAL A 1 474 ? 13.513  6.542   20.135  1.00 30.84  ? 474  VAL A CG1   1 
ATOM   3652 C  CG2   . VAL A 1 474 ? 14.528  4.769   21.600  1.00 51.26  ? 474  VAL A CG2   1 
ATOM   3653 N  N     . ILE A 1 475 ? 11.030  7.696   21.675  1.00 31.71  ? 475  ILE A N     1 
ATOM   3654 C  CA    . ILE A 1 475 ? 9.895   8.445   21.145  1.00 26.90  ? 475  ILE A CA    1 
ATOM   3655 C  C     . ILE A 1 475 ? 10.264  8.909   19.740  1.00 31.25  ? 475  ILE A C     1 
ATOM   3656 O  O     . ILE A 1 475 ? 11.201  9.690   19.551  1.00 32.15  ? 475  ILE A O     1 
ATOM   3657 C  CB    . ILE A 1 475 ? 9.492   9.593   22.081  1.00 29.46  ? 475  ILE A CB    1 
ATOM   3658 C  CG1   . ILE A 1 475 ? 9.118   8.960   23.436  1.00 32.31  ? 475  ILE A CG1   1 
ATOM   3659 C  CG2   . ILE A 1 475 ? 8.362   10.376  21.481  1.00 25.66  ? 475  ILE A CG2   1 
ATOM   3660 C  CD1   . ILE A 1 475 ? 8.083   9.652   24.257  1.00 33.26  ? 475  ILE A CD1   1 
ATOM   3661 N  N     . MET A 1 476 ? 9.561   8.390   18.743  1.00 21.50  ? 476  MET A N     1 
ATOM   3662 C  CA    . MET A 1 476 ? 9.877   8.683   17.359  1.00 26.92  ? 476  MET A CA    1 
ATOM   3663 C  C     . MET A 1 476 ? 8.759   9.494   16.730  1.00 26.86  ? 476  MET A C     1 
ATOM   3664 O  O     . MET A 1 476 ? 7.625   9.514   17.210  1.00 23.45  ? 476  MET A O     1 
ATOM   3665 C  CB    . MET A 1 476 ? 10.114  7.405   16.554  1.00 29.76  ? 476  MET A CB    1 
ATOM   3666 C  CG    . MET A 1 476 ? 8.912   6.509   16.458  1.00 40.16  ? 476  MET A CG    1 
ATOM   3667 S  SD    . MET A 1 476 ? 9.441   4.869   15.955  1.00 69.38  ? 476  MET A SD    1 
ATOM   3668 C  CE    . MET A 1 476 ? 10.514  5.301   14.579  1.00 64.50  ? 476  MET A CE    1 
ATOM   3669 N  N     . HIS A 1 477 ? 9.120   10.189  15.656  1.00 20.02  ? 477  HIS A N     1 
ATOM   3670 C  CA    . HIS A 1 477 ? 8.169   10.957  14.880  1.00 20.46  ? 477  HIS A CA    1 
ATOM   3671 C  C     . HIS A 1 477 ? 7.417   10.066  13.920  1.00 20.25  ? 477  HIS A C     1 
ATOM   3672 O  O     . HIS A 1 477 ? 8.023   9.247   13.222  1.00 21.79  ? 477  HIS A O     1 
ATOM   3673 C  CB    . HIS A 1 477 ? 8.909   12.024  14.087  1.00 19.40  ? 477  HIS A CB    1 
ATOM   3674 C  CG    . HIS A 1 477 ? 9.417   13.137  14.938  1.00 23.36  ? 477  HIS A CG    1 
ATOM   3675 N  ND1   . HIS A 1 477 ? 8.665   14.254  15.222  1.00 19.04  ? 477  HIS A ND1   1 
ATOM   3676 C  CD2   . HIS A 1 477 ? 10.575  13.272  15.628  1.00 25.91  ? 477  HIS A CD2   1 
ATOM   3677 C  CE1   . HIS A 1 477 ? 9.360   15.055  16.012  1.00 27.61  ? 477  HIS A CE1   1 
ATOM   3678 N  NE2   . HIS A 1 477 ? 10.517  14.479  16.281  1.00 22.98  ? 477  HIS A NE2   1 
ATOM   3679 N  N     . ASP A 1 478 ? 6.105   10.281  13.811  1.00 18.19  ? 478  ASP A N     1 
ATOM   3680 C  CA    . ASP A 1 478 ? 5.283   9.533   12.851  1.00 19.63  ? 478  ASP A CA    1 
ATOM   3681 C  C     . ASP A 1 478 ? 4.163   10.424  12.343  1.00 18.46  ? 478  ASP A C     1 
ATOM   3682 O  O     . ASP A 1 478 ? 2.986   10.248  12.701  1.00 19.58  ? 478  ASP A O     1 
ATOM   3683 C  CB    . ASP A 1 478 ? 4.722   8.254   13.484  1.00 22.44  ? 478  ASP A CB    1 
ATOM   3684 C  CG    . ASP A 1 478 ? 4.231   7.252   12.438  1.00 21.15  ? 478  ASP A CG    1 
ATOM   3685 O  OD1   . ASP A 1 478 ? 3.979   7.642   11.278  1.00 19.53  ? 478  ASP A OD1   1 
ATOM   3686 O  OD2   . ASP A 1 478 ? 4.102   6.067   12.777  1.00 21.61  ? 478  ASP A OD2   1 
ATOM   3687 N  N     . PRO A 1 479 ? 4.492   11.404  11.503  1.00 16.39  ? 479  PRO A N     1 
ATOM   3688 C  CA    . PRO A 1 479 ? 3.484   12.383  11.084  1.00 19.43  ? 479  PRO A CA    1 
ATOM   3689 C  C     . PRO A 1 479 ? 2.318   11.698  10.389  1.00 15.57  ? 479  PRO A C     1 
ATOM   3690 O  O     . PRO A 1 479 ? 2.516   10.875  9.504   1.00 18.13  ? 479  PRO A O     1 
ATOM   3691 C  CB    . PRO A 1 479 ? 4.250   13.294  10.106  1.00 15.47  ? 479  PRO A CB    1 
ATOM   3692 C  CG    . PRO A 1 479 ? 5.470   12.580  9.754   1.00 22.04  ? 479  PRO A CG    1 
ATOM   3693 C  CD    . PRO A 1 479 ? 5.814   11.677  10.896  1.00 18.84  ? 479  PRO A CD    1 
ATOM   3694 N  N     . PHE A 1 480 ? 1.104   12.044  10.809  1.00 16.25  ? 480  PHE A N     1 
ATOM   3695 C  CA    . PHE A 1 480 ? -0.144  11.536  10.237  1.00 19.97  ? 480  PHE A CA    1 
ATOM   3696 C  C     . PHE A 1 480 ? -0.273  10.017  10.319  1.00 18.50  ? 480  PHE A C     1 
ATOM   3697 O  O     . PHE A 1 480 ? -1.135  9.428   9.623   1.00 13.19  ? 480  PHE A O     1 
ATOM   3698 C  CB    . PHE A 1 480 ? -0.298  11.984  8.785   1.00 19.37  ? 480  PHE A CB    1 
ATOM   3699 C  CG    . PHE A 1 480 ? -0.622  13.432  8.652   1.00 21.24  ? 480  PHE A CG    1 
ATOM   3700 C  CD1   . PHE A 1 480 ? 0.393   14.398  8.752   1.00 20.89  ? 480  PHE A CD1   1 
ATOM   3701 C  CD2   . PHE A 1 480 ? -1.921  13.847  8.432   1.00 19.56  ? 480  PHE A CD2   1 
ATOM   3702 C  CE1   . PHE A 1 480 ? 0.102   15.735  8.640   1.00 22.97  ? 480  PHE A CE1   1 
ATOM   3703 C  CE2   . PHE A 1 480 ? -2.211  15.216  8.312   1.00 21.97  ? 480  PHE A CE2   1 
ATOM   3704 C  CZ    . PHE A 1 480 ? -1.202  16.146  8.422   1.00 18.68  ? 480  PHE A CZ    1 
ATOM   3705 N  N     . ALA A 1 481 ? 0.566   9.367   11.133  1.00 14.45  ? 481  ALA A N     1 
ATOM   3706 C  CA    . ALA A 1 481 ? 0.648   7.896   11.177  1.00 16.75  ? 481  ALA A CA    1 
ATOM   3707 C  C     . ALA A 1 481 ? 1.048   7.311   9.821   1.00 19.28  ? 481  ALA A C     1 
ATOM   3708 O  O     . ALA A 1 481 ? 0.707   6.163   9.500   1.00 17.21  ? 481  ALA A O     1 
ATOM   3709 C  CB    . ALA A 1 481 ? -0.655  7.265   11.675  1.00 19.59  ? 481  ALA A CB    1 
ATOM   3710 N  N     . MET A 1 482 ? 1.747   8.102   8.992   1.00 15.55  ? 482  MET A N     1 
ATOM   3711 C  CA    . MET A 1 482 ? 2.046   7.701   7.618   1.00 13.61  ? 482  MET A CA    1 
ATOM   3712 C  C     . MET A 1 482 ? 3.537   7.577   7.343   1.00 18.15  ? 482  MET A C     1 
ATOM   3713 O  O     . MET A 1 482 ? 3.920   7.405   6.180   1.00 16.71  ? 482  MET A O     1 
ATOM   3714 C  CB    . MET A 1 482 ? 1.448   8.696   6.628   1.00 20.04  ? 482  MET A CB    1 
ATOM   3715 C  CG    . MET A 1 482 ? -0.053  8.628   6.525   1.00 21.18  ? 482  MET A CG    1 
ATOM   3716 S  SD    . MET A 1 482 ? -0.518  7.344   5.373   1.00 19.68  ? 482  MET A SD    1 
ATOM   3717 C  CE    . MET A 1 482 ? -0.208  8.153   3.810   1.00 26.04  ? 482  MET A CE    1 
ATOM   3718 N  N     . ARG A 1 483 ? 4.385   7.690   8.357   1.00 16.82  ? 483  ARG A N     1 
ATOM   3719 C  CA    . ARG A 1 483 ? 5.822   7.688   8.108   1.00 17.94  ? 483  ARG A CA    1 
ATOM   3720 C  C     . ARG A 1 483 ? 6.304   6.503   7.260   1.00 21.91  ? 483  ARG A C     1 
ATOM   3721 O  O     . ARG A 1 483 ? 7.148   6.717   6.369   1.00 18.40  ? 483  ARG A O     1 
ATOM   3722 C  CB    . ARG A 1 483 ? 6.582   7.720   9.443   1.00 21.09  ? 483  ARG A CB    1 
ATOM   3723 C  CG    . ARG A 1 483 ? 8.102   7.836   9.242   1.00 23.77  ? 483  ARG A CG    1 
ATOM   3724 C  CD    . ARG A 1 483 ? 8.931   7.300   10.407  1.00 28.08  ? 483  ARG A CD    1 
ATOM   3725 N  NE    . ARG A 1 483 ? 8.785   5.856   10.558  1.00 37.22  ? 483  ARG A NE    1 
ATOM   3726 C  CZ    . ARG A 1 483 ? 8.175   5.285   11.589  1.00 46.21  ? 483  ARG A CZ    1 
ATOM   3727 N  NH1   . ARG A 1 483 ? 7.675   6.013   12.583  1.00 35.19  ? 483  ARG A NH1   1 
ATOM   3728 N  NH2   . ARG A 1 483 ? 8.058   3.954   11.625  1.00 43.66  ? 483  ARG A NH2   1 
ATOM   3729 N  N     . PRO A 1 484 ? 5.833   5.270   7.450   1.00 19.42  ? 484  PRO A N     1 
ATOM   3730 C  CA    . PRO A 1 484 ? 6.265   4.176   6.563   1.00 19.81  ? 484  PRO A CA    1 
ATOM   3731 C  C     . PRO A 1 484 ? 5.521   4.121   5.234   1.00 17.93  ? 484  PRO A C     1 
ATOM   3732 O  O     . PRO A 1 484 ? 5.817   3.240   4.406   1.00 20.85  ? 484  PRO A O     1 
ATOM   3733 C  CB    . PRO A 1 484 ? 5.970   2.900   7.400   1.00 21.96  ? 484  PRO A CB    1 
ATOM   3734 C  CG    . PRO A 1 484 ? 5.528   3.360   8.743   1.00 24.89  ? 484  PRO A CG    1 
ATOM   3735 C  CD    . PRO A 1 484 ? 4.998   4.761   8.553   1.00 20.71  ? 484  PRO A CD    1 
ATOM   3736 N  N     . PHE A 1 485 ? 4.590   5.035   4.976   1.00 20.83  ? 485  PHE A N     1 
ATOM   3737 C  CA    . PHE A 1 485 ? 3.660   4.864   3.862   1.00 20.44  ? 485  PHE A CA    1 
ATOM   3738 C  C     . PHE A 1 485 ? 3.540   6.046   2.906   1.00 20.20  ? 485  PHE A C     1 
ATOM   3739 O  O     . PHE A 1 485 ? 2.735   5.968   1.973   1.00 22.09  ? 485  PHE A O     1 
ATOM   3740 C  CB    . PHE A 1 485 ? 2.245   4.526   4.403   1.00 18.55  ? 485  PHE A CB    1 
ATOM   3741 C  CG    . PHE A 1 485 ? 2.233   3.408   5.429   1.00 19.63  ? 485  PHE A CG    1 
ATOM   3742 C  CD1   . PHE A 1 485 ? 2.588   2.118   5.078   1.00 18.17  ? 485  PHE A CD1   1 
ATOM   3743 C  CD2   . PHE A 1 485 ? 1.826   3.648   6.746   1.00 19.66  ? 485  PHE A CD2   1 
ATOM   3744 C  CE1   . PHE A 1 485 ? 2.565   1.081   6.037   1.00 18.01  ? 485  PHE A CE1   1 
ATOM   3745 C  CE2   . PHE A 1 485 ? 1.789   2.626   7.692   1.00 17.27  ? 485  PHE A CE2   1 
ATOM   3746 C  CZ    . PHE A 1 485 ? 2.155   1.343   7.336   1.00 21.36  ? 485  PHE A CZ    1 
ATOM   3747 N  N     . PHE A 1 486 ? 4.310   7.120   3.070   1.00 19.03  ? 486  PHE A N     1 
ATOM   3748 C  CA    . PHE A 1 486 ? 4.246   8.205   2.089   1.00 19.26  ? 486  PHE A CA    1 
ATOM   3749 C  C     . PHE A 1 486 ? 4.655   7.722   0.699   1.00 18.02  ? 486  PHE A C     1 
ATOM   3750 O  O     . PHE A 1 486 ? 5.701   7.104   0.531   1.00 26.86  ? 486  PHE A O     1 
ATOM   3751 C  CB    . PHE A 1 486 ? 5.140   9.379   2.511   1.00 19.24  ? 486  PHE A CB    1 
ATOM   3752 C  CG    . PHE A 1 486 ? 4.691   10.049  3.751   1.00 15.79  ? 486  PHE A CG    1 
ATOM   3753 C  CD1   . PHE A 1 486 ? 3.470   10.668  3.787   1.00 16.35  ? 486  PHE A CD1   1 
ATOM   3754 C  CD2   . PHE A 1 486 ? 5.471   10.054  4.894   1.00 16.68  ? 486  PHE A CD2   1 
ATOM   3755 C  CE1   . PHE A 1 486 ? 3.002   11.297  4.939   1.00 19.86  ? 486  PHE A CE1   1 
ATOM   3756 C  CE2   . PHE A 1 486 ? 4.983   10.697  6.066   1.00 14.52  ? 486  PHE A CE2   1 
ATOM   3757 C  CZ    . PHE A 1 486 ? 3.777   11.319  6.074   1.00 20.18  ? 486  PHE A CZ    1 
ATOM   3758 N  N     . GLY A 1 487 ? 3.800   7.978   -0.292  1.00 19.33  ? 487  GLY A N     1 
ATOM   3759 C  CA    . GLY A 1 487 ? 4.087   7.628   -1.668  1.00 19.88  ? 487  GLY A CA    1 
ATOM   3760 C  C     . GLY A 1 487 ? 4.889   8.677   -2.401  1.00 21.31  ? 487  GLY A C     1 
ATOM   3761 O  O     . GLY A 1 487 ? 5.316   8.433   -3.533  1.00 23.80  ? 487  GLY A O     1 
ATOM   3762 N  N     . TYR A 1 488 ? 5.095   9.829   -1.760  1.00 19.25  ? 488  TYR A N     1 
ATOM   3763 C  CA    . TYR A 1 488 ? 5.745   10.989  -2.370  1.00 24.52  ? 488  TYR A CA    1 
ATOM   3764 C  C     . TYR A 1 488 ? 6.200   11.947  -1.265  1.00 21.66  ? 488  TYR A C     1 
ATOM   3765 O  O     . TYR A 1 488 ? 5.951   11.736  -0.074  1.00 20.15  ? 488  TYR A O     1 
ATOM   3766 C  CB    . TYR A 1 488 ? 4.806   11.666  -3.388  1.00 20.89  ? 488  TYR A CB    1 
ATOM   3767 C  CG    . TYR A 1 488 ? 3.569   12.324  -2.770  1.00 19.59  ? 488  TYR A CG    1 
ATOM   3768 C  CD1   . TYR A 1 488 ? 2.485   11.561  -2.357  1.00 22.44  ? 488  TYR A CD1   1 
ATOM   3769 C  CD2   . TYR A 1 488 ? 3.499   13.705  -2.598  1.00 20.44  ? 488  TYR A CD2   1 
ATOM   3770 C  CE1   . TYR A 1 488 ? 1.363   12.145  -1.788  1.00 20.60  ? 488  TYR A CE1   1 
ATOM   3771 C  CE2   . TYR A 1 488 ? 2.385   14.315  -2.053  1.00 22.01  ? 488  TYR A CE2   1 
ATOM   3772 C  CZ    . TYR A 1 488 ? 1.308   13.518  -1.638  1.00 20.03  ? 488  TYR A CZ    1 
ATOM   3773 O  OH    . TYR A 1 488 ? 0.177   14.088  -1.096  1.00 19.43  ? 488  TYR A OH    1 
ATOM   3774 N  N     . ASN A 1 489 ? 6.885   13.008  -1.687  1.00 21.09  ? 489  ASN A N     1 
ATOM   3775 C  CA    . ASN A 1 489 ? 7.470   14.045  -0.841  1.00 19.52  ? 489  ASN A CA    1 
ATOM   3776 C  C     . ASN A 1 489 ? 6.497   14.559  0.214   1.00 19.17  ? 489  ASN A C     1 
ATOM   3777 O  O     . ASN A 1 489 ? 5.416   15.041  -0.114  1.00 18.22  ? 489  ASN A O     1 
ATOM   3778 C  CB    . ASN A 1 489 ? 7.915   15.196  -1.780  1.00 20.31  ? 489  ASN A CB    1 
ATOM   3779 C  CG    . ASN A 1 489 ? 8.596   16.345  -1.071  1.00 23.50  ? 489  ASN A CG    1 
ATOM   3780 O  OD1   . ASN A 1 489 ? 8.069   16.897  -0.111  1.00 21.17  ? 489  ASN A OD1   1 
ATOM   3781 N  ND2   . ASN A 1 489 ? 9.761   16.770  -1.602  1.00 22.06  ? 489  ASN A ND2   1 
ATOM   3782 N  N     . PHE A 1 490 ? 6.905   14.449  1.487   1.00 17.83  ? 490  PHE A N     1 
ATOM   3783 C  CA    . PHE A 1 490 ? 6.033   14.761  2.615   1.00 19.32  ? 490  PHE A CA    1 
ATOM   3784 C  C     . PHE A 1 490 ? 5.702   16.241  2.670   1.00 19.03  ? 490  PHE A C     1 
ATOM   3785 O  O     . PHE A 1 490 ? 4.592   16.607  3.070   1.00 19.66  ? 490  PHE A O     1 
ATOM   3786 C  CB    . PHE A 1 490 ? 6.691   14.297  3.931   1.00 18.72  ? 490  PHE A CB    1 
ATOM   3787 C  CG    . PHE A 1 490 ? 5.969   14.752  5.186   1.00 22.11  ? 490  PHE A CG    1 
ATOM   3788 C  CD1   . PHE A 1 490 ? 4.612   14.436  5.402   1.00 21.72  ? 490  PHE A CD1   1 
ATOM   3789 C  CD2   . PHE A 1 490 ? 6.654   15.452  6.172   1.00 21.41  ? 490  PHE A CD2   1 
ATOM   3790 C  CE1   . PHE A 1 490 ? 3.949   14.863  6.558   1.00 17.92  ? 490  PHE A CE1   1 
ATOM   3791 C  CE2   . PHE A 1 490 ? 5.997   15.884  7.343   1.00 22.44  ? 490  PHE A CE2   1 
ATOM   3792 C  CZ    . PHE A 1 490 ? 4.647   15.570  7.540   1.00 18.83  ? 490  PHE A CZ    1 
ATOM   3793 N  N     . GLY A 1 491 ? 6.641   17.106  2.260   1.00 18.61  ? 491  GLY A N     1 
ATOM   3794 C  CA    . GLY A 1 491 ? 6.318   18.528  2.173   1.00 18.96  ? 491  GLY A CA    1 
ATOM   3795 C  C     . GLY A 1 491 ? 5.160   18.798  1.229   1.00 18.83  ? 491  GLY A C     1 
ATOM   3796 O  O     . GLY A 1 491 ? 4.267   19.602  1.533   1.00 20.39  ? 491  GLY A O     1 
ATOM   3797 N  N     . LYS A 1 492 ? 5.186   18.171  0.050   1.00 19.20  ? 492  LYS A N     1 
ATOM   3798 C  CA    . LYS A 1 492 ? 4.081   18.297  -0.903  1.00 21.22  ? 492  LYS A CA    1 
ATOM   3799 C  C     . LYS A 1 492 ? 2.784   17.693  -0.334  1.00 23.31  ? 492  LYS A C     1 
ATOM   3800 O  O     . LYS A 1 492 ? 1.685   18.185  -0.632  1.00 17.39  ? 492  LYS A O     1 
ATOM   3801 C  CB    . LYS A 1 492 ? 4.452   17.601  -2.224  1.00 20.47  ? 492  LYS A CB    1 
ATOM   3802 C  CG    . LYS A 1 492 ? 5.759   18.112  -2.875  1.00 23.59  ? 492  LYS A CG    1 
ATOM   3803 C  CD    . LYS A 1 492 ? 5.718   19.626  -3.032  1.00 31.43  ? 492  LYS A CD    1 
ATOM   3804 C  CE    . LYS A 1 492 ? 7.036   20.178  -3.604  1.00 45.12  ? 492  LYS A CE    1 
ATOM   3805 N  NZ    . LYS A 1 492 ? 7.253   21.602  -3.153  1.00 46.24  ? 492  LYS A NZ    1 
ATOM   3806 N  N     . TYR A 1 493 ? 2.914   16.638  0.476   1.00 16.47  ? 493  TYR A N     1 
ATOM   3807 C  CA    . TYR A 1 493 ? 1.776   16.059  1.194   1.00 17.38  ? 493  TYR A CA    1 
ATOM   3808 C  C     . TYR A 1 493 ? 1.151   17.064  2.155   1.00 19.38  ? 493  TYR A C     1 
ATOM   3809 O  O     . TYR A 1 493 ? -0.071  17.217  2.179   1.00 17.55  ? 493  TYR A O     1 
ATOM   3810 C  CB    . TYR A 1 493 ? 2.237   14.805  1.922   1.00 15.98  ? 493  TYR A CB    1 
ATOM   3811 C  CG    . TYR A 1 493 ? 1.245   14.143  2.874   1.00 17.95  ? 493  TYR A CG    1 
ATOM   3812 C  CD1   . TYR A 1 493 ? 1.157   14.555  4.193   1.00 20.04  ? 493  TYR A CD1   1 
ATOM   3813 C  CD2   . TYR A 1 493 ? 0.465   13.067  2.462   1.00 20.07  ? 493  TYR A CD2   1 
ATOM   3814 C  CE1   . TYR A 1 493 ? 0.300   13.933  5.089   1.00 19.08  ? 493  TYR A CE1   1 
ATOM   3815 C  CE2   . TYR A 1 493 ? -0.413  12.432  3.351   1.00 19.83  ? 493  TYR A CE2   1 
ATOM   3816 C  CZ    . TYR A 1 493 ? -0.483  12.860  4.661   1.00 20.99  ? 493  TYR A CZ    1 
ATOM   3817 O  OH    . TYR A 1 493 ? -1.344  12.233  5.556   1.00 20.95  ? 493  TYR A OH    1 
ATOM   3818 N  N     . LEU A 1 494 ? 1.975   17.777  2.946   1.00 16.50  ? 494  LEU A N     1 
ATOM   3819 C  CA    . LEU A 1 494 ? 1.441   18.831  3.817   1.00 17.38  ? 494  LEU A CA    1 
ATOM   3820 C  C     . LEU A 1 494 ? 0.749   19.916  3.016   1.00 18.19  ? 494  LEU A C     1 
ATOM   3821 O  O     . LEU A 1 494 ? -0.320  20.392  3.404   1.00 19.66  ? 494  LEU A O     1 
ATOM   3822 C  CB    . LEU A 1 494 ? 2.546   19.454  4.659   1.00 19.33  ? 494  LEU A CB    1 
ATOM   3823 C  CG    . LEU A 1 494 ? 3.177   18.480  5.643   1.00 19.75  ? 494  LEU A CG    1 
ATOM   3824 C  CD1   . LEU A 1 494 ? 4.354   19.157  6.327   1.00 18.02  ? 494  LEU A CD1   1 
ATOM   3825 C  CD2   . LEU A 1 494 ? 2.140   18.109  6.660   1.00 17.31  ? 494  LEU A CD2   1 
ATOM   3826 N  N     . ALA A 1 495 ? 1.366   20.361  1.905   1.00 19.60  ? 495  ALA A N     1 
ATOM   3827 C  CA    . ALA A 1 495 ? 0.740   21.400  1.092   1.00 21.28  ? 495  ALA A CA    1 
ATOM   3828 C  C     . ALA A 1 495 ? -0.597  20.928  0.531   1.00 17.04  ? 495  ALA A C     1 
ATOM   3829 O  O     . ALA A 1 495 ? -1.562  21.699  0.439   1.00 21.36  ? 495  ALA A O     1 
ATOM   3830 C  CB    . ALA A 1 495 ? 1.691   21.808  -0.056  1.00 21.45  ? 495  ALA A CB    1 
ATOM   3831 N  N     . HIS A 1 496 ? -0.662  19.665  0.138   1.00 17.55  ? 496  HIS A N     1 
ATOM   3832 C  CA    . HIS A 1 496 ? -1.910  19.064  -0.330  1.00 19.26  ? 496  HIS A CA    1 
ATOM   3833 C  C     . HIS A 1 496 ? -2.996  19.125  0.755   1.00 22.11  ? 496  HIS A C     1 
ATOM   3834 O  O     . HIS A 1 496 ? -4.131  19.540  0.497   1.00 19.45  ? 496  HIS A O     1 
ATOM   3835 C  CB    . HIS A 1 496 ? -1.599  17.619  -0.767  1.00 18.21  ? 496  HIS A CB    1 
ATOM   3836 C  CG    . HIS A 1 496 ? -2.726  16.919  -1.456  1.00 21.19  ? 496  HIS A CG    1 
ATOM   3837 N  ND1   . HIS A 1 496 ? -3.409  17.465  -2.522  1.00 21.50  ? 496  HIS A ND1   1 
ATOM   3838 C  CD2   . HIS A 1 496 ? -3.295  15.709  -1.221  1.00 20.69  ? 496  HIS A CD2   1 
ATOM   3839 C  CE1   . HIS A 1 496 ? -4.351  16.621  -2.918  1.00 23.51  ? 496  HIS A CE1   1 
ATOM   3840 N  NE2   . HIS A 1 496 ? -4.302  15.546  -2.145  1.00 22.92  ? 496  HIS A NE2   1 
ATOM   3841 N  N     . TRP A 1 497 ? -2.654  18.757  1.990   1.00 21.80  ? 497  TRP A N     1 
ATOM   3842 C  CA    . TRP A 1 497 ? -3.631  18.854  3.078   1.00 18.31  ? 497  TRP A CA    1 
ATOM   3843 C  C     . TRP A 1 497 ? -4.037  20.293  3.317   1.00 22.44  ? 497  TRP A C     1 
ATOM   3844 O  O     . TRP A 1 497 ? -5.223  20.591  3.512   1.00 23.83  ? 497  TRP A O     1 
ATOM   3845 C  CB    . TRP A 1 497 ? -3.054  18.273  4.359   1.00 15.76  ? 497  TRP A CB    1 
ATOM   3846 C  CG    . TRP A 1 497 ? -3.352  16.841  4.551   1.00 21.30  ? 497  TRP A CG    1 
ATOM   3847 C  CD1   . TRP A 1 497 ? -2.697  15.797  3.985   1.00 19.46  ? 497  TRP A CD1   1 
ATOM   3848 C  CD2   . TRP A 1 497 ? -4.380  16.279  5.391   1.00 19.59  ? 497  TRP A CD2   1 
ATOM   3849 N  NE1   . TRP A 1 497 ? -3.270  14.608  4.403   1.00 19.91  ? 497  TRP A NE1   1 
ATOM   3850 C  CE2   . TRP A 1 497 ? -4.289  14.883  5.275   1.00 19.87  ? 497  TRP A CE2   1 
ATOM   3851 C  CE3   . TRP A 1 497 ? -5.373  16.830  6.220   1.00 22.52  ? 497  TRP A CE3   1 
ATOM   3852 C  CZ2   . TRP A 1 497 ? -5.148  14.005  5.967   1.00 22.39  ? 497  TRP A CZ2   1 
ATOM   3853 C  CZ3   . TRP A 1 497 ? -6.229  15.957  6.920   1.00 21.96  ? 497  TRP A CZ3   1 
ATOM   3854 C  CH2   . TRP A 1 497 ? -6.104  14.558  6.773   1.00 23.07  ? 497  TRP A CH2   1 
ATOM   3855 N  N     . LEU A 1 498 ? -3.060  21.209  3.305   1.00 21.43  ? 498  LEU A N     1 
ATOM   3856 C  CA    . LEU A 1 498 ? -3.374  22.618  3.519   1.00 22.28  ? 498  LEU A CA    1 
ATOM   3857 C  C     . LEU A 1 498 ? -4.285  23.152  2.428   1.00 21.85  ? 498  LEU A C     1 
ATOM   3858 O  O     . LEU A 1 498 ? -5.162  23.976  2.700   1.00 27.27  ? 498  LEU A O     1 
ATOM   3859 C  CB    . LEU A 1 498 ? -2.081  23.431  3.579   1.00 18.08  ? 498  LEU A CB    1 
ATOM   3860 C  CG    . LEU A 1 498 ? -1.298  23.122  4.861   1.00 19.74  ? 498  LEU A CG    1 
ATOM   3861 C  CD1   . LEU A 1 498 ? 0.128   23.604  4.744   1.00 24.28  ? 498  LEU A CD1   1 
ATOM   3862 C  CD2   . LEU A 1 498 ? -1.993  23.753  6.090   1.00 19.04  ? 498  LEU A CD2   1 
ATOM   3863 N  N     . SER A 1 499 ? -4.095  22.684  1.199   1.00 23.07  ? 499  SER A N     1 
ATOM   3864 C  CA    . SER A 1 499 ? -4.866  23.179  0.064   1.00 25.72  ? 499  SER A CA    1 
ATOM   3865 C  C     . SER A 1 499 ? -6.353  22.863  0.163   1.00 30.78  ? 499  SER A C     1 
ATOM   3866 O  O     . SER A 1 499 ? -7.148  23.503  -0.534  1.00 28.81  ? 499  SER A O     1 
ATOM   3867 C  CB    . SER A 1 499 ? -4.302  22.613  -1.250  1.00 28.15  ? 499  SER A CB    1 
ATOM   3868 O  OG    . SER A 1 499 ? -4.781  21.306  -1.570  1.00 24.37  ? 499  SER A OG    1 
ATOM   3869 N  N     A MET A 1 500 ? -6.750  21.898  1.002   0.68 27.08  ? 500  MET A N     1 
ATOM   3870 N  N     B MET A 1 500 ? -6.748  21.898  1.003   0.32 27.05  ? 500  MET A N     1 
ATOM   3871 C  CA    A MET A 1 500 ? -8.169  21.578  1.121   0.68 26.94  ? 500  MET A CA    1 
ATOM   3872 C  CA    B MET A 1 500 ? -8.167  21.582  1.152   0.32 26.97  ? 500  MET A CA    1 
ATOM   3873 C  C     A MET A 1 500 ? -8.977  22.735  1.704   0.68 30.43  ? 500  MET A C     1 
ATOM   3874 C  C     B MET A 1 500 ? -8.962  22.778  1.650   0.32 30.44  ? 500  MET A C     1 
ATOM   3875 O  O     A MET A 1 500 ? -10.172 22.845  1.414   0.68 34.62  ? 500  MET A O     1 
ATOM   3876 O  O     B MET A 1 500 ? -10.128 22.950  1.276   0.32 34.44  ? 500  MET A O     1 
ATOM   3877 C  CB    A MET A 1 500 ? -8.350  20.306  1.961   0.68 25.74  ? 500  MET A CB    1 
ATOM   3878 C  CB    B MET A 1 500 ? -8.352  20.405  2.109   0.32 25.81  ? 500  MET A CB    1 
ATOM   3879 C  CG    A MET A 1 500 ? -7.654  19.072  1.371   0.68 25.65  ? 500  MET A CG    1 
ATOM   3880 C  CG    B MET A 1 500 ? -7.924  19.077  1.536   0.32 25.89  ? 500  MET A CG    1 
ATOM   3881 S  SD    A MET A 1 500 ? -8.299  18.527  -0.236  0.68 32.58  ? 500  MET A SD    1 
ATOM   3882 S  SD    B MET A 1 500 ? -7.474  17.919  2.834   0.32 22.83  ? 500  MET A SD    1 
ATOM   3883 C  CE    A MET A 1 500 ? -6.989  17.468  -0.837  0.68 24.89  ? 500  MET A CE    1 
ATOM   3884 C  CE    B MET A 1 500 ? -9.045  17.563  3.600   0.32 22.07  ? 500  MET A CE    1 
ATOM   3885 N  N     . ALA A 1 501 ? -8.354  23.614  2.489   1.00 24.77  ? 501  ALA A N     1 
ATOM   3886 C  CA    . ALA A 1 501 ? -9.047  24.788  3.017   1.00 24.38  ? 501  ALA A CA    1 
ATOM   3887 C  C     . ALA A 1 501 ? -9.374  25.842  1.951   1.00 36.40  ? 501  ALA A C     1 
ATOM   3888 O  O     . ALA A 1 501 ? -10.136 26.772  2.245   1.00 39.82  ? 501  ALA A O     1 
ATOM   3889 C  CB    . ALA A 1 501 ? -8.201  25.416  4.119   1.00 28.49  ? 501  ALA A CB    1 
ATOM   3890 N  N     . HIS A 1 502 ? -8.828  25.730  0.734   1.00 38.62  ? 502  HIS A N     1 
ATOM   3891 C  CA    . HIS A 1 502 ? -9.128  26.662  -0.356  1.00 42.77  ? 502  HIS A CA    1 
ATOM   3892 C  C     . HIS A 1 502 ? -10.246 26.184  -1.278  1.00 45.39  ? 502  HIS A C     1 
ATOM   3893 O  O     . HIS A 1 502 ? -10.571 26.885  -2.241  1.00 61.19  ? 502  HIS A O     1 
ATOM   3894 C  CB    . HIS A 1 502 ? -7.888  26.920  -1.215  1.00 38.24  ? 502  HIS A CB    1 
ATOM   3895 C  CG    . HIS A 1 502 ? -6.637  27.147  -0.430  1.00 44.52  ? 502  HIS A CG    1 
ATOM   3896 N  ND1   . HIS A 1 502 ? -5.388  26.824  -0.920  1.00 49.86  ? 502  HIS A ND1   1 
ATOM   3897 C  CD2   . HIS A 1 502 ? -6.436  27.669  0.803   1.00 43.93  ? 502  HIS A CD2   1 
ATOM   3898 C  CE1   . HIS A 1 502 ? -4.473  27.135  -0.020  1.00 46.76  ? 502  HIS A CE1   1 
ATOM   3899 N  NE2   . HIS A 1 502 ? -5.082  27.642  1.038   1.00 48.67  ? 502  HIS A NE2   1 
ATOM   3900 N  N     . ARG A 1 503 ? -10.816 25.027  -1.033  1.00 47.06  ? 503  ARG A N     1 
ATOM   3901 C  CA    . ARG A 1 503 ? -11.811 24.476  -1.938  1.00 56.03  ? 503  ARG A CA    1 
ATOM   3902 C  C     . ARG A 1 503 ? -13.165 25.152  -1.733  1.00 72.77  ? 503  ARG A C     1 
ATOM   3903 O  O     . ARG A 1 503 ? -13.481 25.610  -0.628  1.00 62.84  ? 503  ARG A O     1 
ATOM   3904 C  CB    . ARG A 1 503 ? -11.945 22.973  -1.729  1.00 52.82  ? 503  ARG A CB    1 
ATOM   3905 C  CG    . ARG A 1 503 ? -10.801 22.183  -2.317  1.00 48.75  ? 503  ARG A CG    1 
ATOM   3906 C  CD    . ARG A 1 503 ? -10.979 20.712  -2.054  1.00 53.99  ? 503  ARG A CD    1 
ATOM   3907 N  NE    . ARG A 1 503 ? -12.055 20.126  -2.846  1.00 62.18  ? 503  ARG A NE    1 
ATOM   3908 C  CZ    . ARG A 1 503 ? -11.865 19.350  -3.905  1.00 61.38  ? 503  ARG A CZ    1 
ATOM   3909 N  NH1   . ARG A 1 503 ? -10.647 19.082  -4.357  1.00 60.71  ? 503  ARG A NH1   1 
ATOM   3910 N  NH2   . ARG A 1 503 ? -12.923 18.818  -4.518  1.00 60.29  ? 503  ARG A NH2   1 
ATOM   3911 N  N     . PRO A 1 504 ? -13.972 25.241  -2.793  1.00 91.51  ? 504  PRO A N     1 
ATOM   3912 C  CA    . PRO A 1 504 ? -15.283 25.895  -2.676  1.00 92.66  ? 504  PRO A CA    1 
ATOM   3913 C  C     . PRO A 1 504 ? -16.247 25.068  -1.837  1.00 92.55  ? 504  PRO A C     1 
ATOM   3914 O  O     . PRO A 1 504 ? -16.431 23.871  -2.071  1.00 94.07  ? 504  PRO A O     1 
ATOM   3915 C  CB    . PRO A 1 504 ? -15.759 26.005  -4.132  1.00 97.26  ? 504  PRO A CB    1 
ATOM   3916 C  CG    . PRO A 1 504 ? -14.525 25.862  -4.960  1.00 99.45  ? 504  PRO A CG    1 
ATOM   3917 C  CD    . PRO A 1 504 ? -13.639 24.927  -4.193  1.00 93.49  ? 504  PRO A CD    1 
ATOM   3918 N  N     . ALA A 1 505 ? -16.862 25.723  -0.853  1.00 73.62  ? 505  ALA A N     1 
ATOM   3919 C  CA    . ALA A 1 505 ? -17.882 25.129  0.005   1.00 65.53  ? 505  ALA A CA    1 
ATOM   3920 C  C     . ALA A 1 505 ? -17.376 23.904  0.764   1.00 49.57  ? 505  ALA A C     1 
ATOM   3921 O  O     . ALA A 1 505 ? -18.183 23.094  1.234   1.00 42.89  ? 505  ALA A O     1 
ATOM   3922 C  CB    . ALA A 1 505 ? -19.145 24.774  -0.794  1.00 65.18  ? 505  ALA A CB    1 
ATOM   3923 N  N     . ALA A 1 506 ? -16.056 23.753  0.897   1.00 48.63  ? 506  ALA A N     1 
ATOM   3924 C  CA    . ALA A 1 506 ? -15.503 22.663  1.688   1.00 41.19  ? 506  ALA A CA    1 
ATOM   3925 C  C     . ALA A 1 506 ? -15.966 22.771  3.129   1.00 37.21  ? 506  ALA A C     1 
ATOM   3926 O  O     . ALA A 1 506 ? -15.820 23.815  3.767   1.00 36.41  ? 506  ALA A O     1 
ATOM   3927 C  CB    . ALA A 1 506 ? -13.979 22.670  1.639   1.00 39.23  ? 506  ALA A CB    1 
ATOM   3928 N  N     . LYS A 1 507 ? -16.531 21.685  3.641   1.00 32.51  ? 507  LYS A N     1 
ATOM   3929 C  CA    . LYS A 1 507 ? -16.950 21.602  5.042   1.00 36.47  ? 507  LYS A CA    1 
ATOM   3930 C  C     . LYS A 1 507 ? -15.827 20.884  5.782   1.00 33.20  ? 507  LYS A C     1 
ATOM   3931 O  O     . LYS A 1 507 ? -15.815 19.662  5.889   1.00 27.63  ? 507  LYS A O     1 
ATOM   3932 C  CB    . LYS A 1 507 ? -18.280 20.869  5.166   1.00 34.29  ? 507  LYS A CB    1 
ATOM   3933 C  CG    . LYS A 1 507 ? -19.441 21.670  4.595   1.00 38.45  ? 507  LYS A CG    1 
ATOM   3934 C  CD    . LYS A 1 507 ? -20.617 20.787  4.258   1.00 40.46  ? 507  LYS A CD    1 
ATOM   3935 C  CE    . LYS A 1 507 ? -21.705 21.616  3.623   1.00 42.32  ? 507  LYS A CE    1 
ATOM   3936 N  NZ    . LYS A 1 507 ? -22.824 20.787  3.132   1.00 43.90  ? 507  LYS A NZ    1 
ATOM   3937 N  N     . LEU A 1 508 ? -14.868 21.649  6.286   1.00 26.80  ? 508  LEU A N     1 
ATOM   3938 C  CA    . LEU A 1 508 ? -13.689 21.023  6.873   1.00 23.89  ? 508  LEU A CA    1 
ATOM   3939 C  C     . LEU A 1 508 ? -14.032 20.362  8.208   1.00 26.60  ? 508  LEU A C     1 
ATOM   3940 O  O     . LEU A 1 508 ? -14.635 21.003  9.072   1.00 25.15  ? 508  LEU A O     1 
ATOM   3941 C  CB    . LEU A 1 508 ? -12.602 22.048  7.082   1.00 24.80  ? 508  LEU A CB    1 
ATOM   3942 C  CG    . LEU A 1 508 ? -12.158 22.808  5.830   1.00 25.94  ? 508  LEU A CG    1 
ATOM   3943 C  CD1   . LEU A 1 508 ? -11.167 23.880  6.311   1.00 25.66  ? 508  LEU A CD1   1 
ATOM   3944 C  CD2   . LEU A 1 508 ? -11.535 21.867  4.830   1.00 24.34  ? 508  LEU A CD2   1 
ATOM   3945 N  N     . PRO A 1 509 ? -13.639 19.111  8.426   1.00 23.64  ? 509  PRO A N     1 
ATOM   3946 C  CA    . PRO A 1 509 ? -13.912 18.472  9.719   1.00 23.56  ? 509  PRO A CA    1 
ATOM   3947 C  C     . PRO A 1 509 ? -13.064 19.044  10.855  1.00 29.61  ? 509  PRO A C     1 
ATOM   3948 O  O     . PRO A 1 509 ? -11.981 19.597  10.651  1.00 20.23  ? 509  PRO A O     1 
ATOM   3949 C  CB    . PRO A 1 509 ? -13.579 17.000  9.462   1.00 22.82  ? 509  PRO A CB    1 
ATOM   3950 C  CG    . PRO A 1 509 ? -12.694 16.985  8.286   1.00 23.16  ? 509  PRO A CG    1 
ATOM   3951 C  CD    . PRO A 1 509 ? -13.090 18.163  7.438   1.00 24.46  ? 509  PRO A CD    1 
ATOM   3952 N  N     . LYS A 1 510 ? -13.571 18.888  12.082  1.00 20.43  ? 510  LYS A N     1 
ATOM   3953 C  CA    . LYS A 1 510 ? -12.789 19.280  13.253  1.00 17.12  ? 510  LYS A CA    1 
ATOM   3954 C  C     . LYS A 1 510 ? -11.640 18.298  13.418  1.00 18.60  ? 510  LYS A C     1 
ATOM   3955 O  O     . LYS A 1 510 ? -11.739 17.151  13.008  1.00 23.29  ? 510  LYS A O     1 
ATOM   3956 C  CB    . LYS A 1 510 ? -13.651 19.293  14.513  1.00 22.64  ? 510  LYS A CB    1 
ATOM   3957 C  CG    . LYS A 1 510 ? -14.592 20.440  14.613  1.00 30.39  ? 510  LYS A CG    1 
ATOM   3958 C  CD    . LYS A 1 510 ? -15.222 20.490  15.995  1.00 25.94  ? 510  LYS A CD    1 
ATOM   3959 C  CE    . LYS A 1 510 ? -15.764 21.892  16.250  1.00 34.85  ? 510  LYS A CE    1 
ATOM   3960 N  NZ    . LYS A 1 510 ? -14.696 22.860  16.422  1.00 32.60  ? 510  LYS A NZ    1 
ATOM   3961 N  N     . ILE A 1 511 ? -10.533 18.743  14.020  1.00 20.14  ? 511  ILE A N     1 
ATOM   3962 C  CA    . ILE A 1 511 ? -9.348  17.895  14.152  1.00 17.96  ? 511  ILE A CA    1 
ATOM   3963 C  C     . ILE A 1 511 ? -8.986  17.821  15.623  1.00 20.35  ? 511  ILE A C     1 
ATOM   3964 O  O     . ILE A 1 511 ? -8.957  18.854  16.311  1.00 19.58  ? 511  ILE A O     1 
ATOM   3965 C  CB    . ILE A 1 511 ? -8.162  18.402  13.311  1.00 22.22  ? 511  ILE A CB    1 
ATOM   3966 C  CG1   . ILE A 1 511 ? -8.365  18.073  11.835  1.00 24.92  ? 511  ILE A CG1   1 
ATOM   3967 C  CG2   . ILE A 1 511 ? -6.821  17.756  13.770  1.00 15.74  ? 511  ILE A CG2   1 
ATOM   3968 C  CD1   . ILE A 1 511 ? -7.325  18.762  10.936  1.00 20.43  ? 511  ILE A CD1   1 
ATOM   3969 N  N     . PHE A 1 512 ? -8.842  16.593  16.126  1.00 15.31  ? 512  PHE A N     1 
ATOM   3970 C  CA    . PHE A 1 512 ? -8.574  16.309  17.527  1.00 14.45  ? 512  PHE A CA    1 
ATOM   3971 C  C     . PHE A 1 512 ? -7.288  15.520  17.644  1.00 16.94  ? 512  PHE A C     1 
ATOM   3972 O  O     . PHE A 1 512 ? -6.898  14.789  16.724  1.00 20.71  ? 512  PHE A O     1 
ATOM   3973 C  CB    . PHE A 1 512 ? -9.702  15.464  18.191  1.00 18.04  ? 512  PHE A CB    1 
ATOM   3974 C  CG    . PHE A 1 512 ? -11.068 16.095  18.115  1.00 13.94  ? 512  PHE A CG    1 
ATOM   3975 C  CD1   . PHE A 1 512 ? -11.482 17.018  19.058  1.00 16.72  ? 512  PHE A CD1   1 
ATOM   3976 C  CD2   . PHE A 1 512 ? -11.943 15.728  17.107  1.00 19.50  ? 512  PHE A CD2   1 
ATOM   3977 C  CE1   . PHE A 1 512 ? -12.735 17.599  18.976  1.00 21.87  ? 512  PHE A CE1   1 
ATOM   3978 C  CE2   . PHE A 1 512 ? -13.209 16.288  17.031  1.00 18.56  ? 512  PHE A CE2   1 
ATOM   3979 C  CZ    . PHE A 1 512 ? -13.608 17.231  17.964  1.00 18.66  ? 512  PHE A CZ    1 
ATOM   3980 N  N     . HIS A 1 513 ? -6.643  15.641  18.793  1.00 17.41  ? 513  HIS A N     1 
ATOM   3981 C  CA    . HIS A 1 513 ? -5.541  14.760  19.155  1.00 17.56  ? 513  HIS A CA    1 
ATOM   3982 C  C     . HIS A 1 513 ? -5.861  14.057  20.476  1.00 18.47  ? 513  HIS A C     1 
ATOM   3983 O  O     . HIS A 1 513 ? -6.239  14.722  21.451  1.00 17.54  ? 513  HIS A O     1 
ATOM   3984 C  CB    . HIS A 1 513 ? -4.257  15.555  19.305  1.00 18.23  ? 513  HIS A CB    1 
ATOM   3985 C  CG    . HIS A 1 513 ? -3.018  14.713  19.327  1.00 16.14  ? 513  HIS A CG    1 
ATOM   3986 N  ND1   . HIS A 1 513 ? -2.463  14.246  20.500  1.00 17.93  ? 513  HIS A ND1   1 
ATOM   3987 C  CD2   . HIS A 1 513 ? -2.188  14.318  18.330  1.00 16.86  ? 513  HIS A CD2   1 
ATOM   3988 C  CE1   . HIS A 1 513 ? -1.360  13.579  20.223  1.00 20.15  ? 513  HIS A CE1   1 
ATOM   3989 N  NE2   . HIS A 1 513 ? -1.165  13.615  18.917  1.00 16.52  ? 513  HIS A NE2   1 
ATOM   3990 N  N     . VAL A 1 514 ? -5.675  12.730  20.523  1.00 20.29  ? 514  VAL A N     1 
ATOM   3991 C  CA    . VAL A 1 514 ? -5.903  11.945  21.747  1.00 18.15  ? 514  VAL A CA    1 
ATOM   3992 C  C     . VAL A 1 514 ? -4.594  11.304  22.192  1.00 19.24  ? 514  VAL A C     1 
ATOM   3993 O  O     . VAL A 1 514 ? -3.639  11.141  21.416  1.00 19.95  ? 514  VAL A O     1 
ATOM   3994 C  CB    . VAL A 1 514 ? -6.969  10.858  21.582  1.00 18.21  ? 514  VAL A CB    1 
ATOM   3995 C  CG1   . VAL A 1 514 ? -8.268  11.470  21.132  1.00 17.84  ? 514  VAL A CG1   1 
ATOM   3996 C  CG2   . VAL A 1 514 ? -6.464  9.764   20.580  1.00 14.88  ? 514  VAL A CG2   1 
ATOM   3997 N  N     . ASN A 1 515 ? -4.566  10.935  23.468  1.00 14.45  ? 515  ASN A N     1 
ATOM   3998 C  CA    . ASN A 1 515 ? -3.472  10.181  24.074  1.00 14.93  ? 515  ASN A CA    1 
ATOM   3999 C  C     . ASN A 1 515 ? -4.115  9.210   25.070  1.00 18.78  ? 515  ASN A C     1 
ATOM   4000 O  O     . ASN A 1 515 ? -4.532  9.614   26.171  1.00 19.01  ? 515  ASN A O     1 
ATOM   4001 C  CB    . ASN A 1 515 ? -2.472  11.088  24.769  1.00 13.80  ? 515  ASN A CB    1 
ATOM   4002 C  CG    . ASN A 1 515 ? -1.310  10.322  25.340  1.00 18.60  ? 515  ASN A CG    1 
ATOM   4003 O  OD1   . ASN A 1 515 ? -1.037  9.209   24.908  1.00 23.07  ? 515  ASN A OD1   1 
ATOM   4004 N  ND2   . ASN A 1 515 ? -0.598  10.917  26.291  1.00 20.51  ? 515  ASN A ND2   1 
ATOM   4005 N  N     . TRP A 1 516 ? -4.206  7.937   24.682  1.00 19.75  ? 516  TRP A N     1 
ATOM   4006 C  CA    . TRP A 1 516 ? -4.715  6.928   25.596  1.00 19.63  ? 516  TRP A CA    1 
ATOM   4007 C  C     . TRP A 1 516 ? -3.656  6.467   26.589  1.00 24.27  ? 516  TRP A C     1 
ATOM   4008 O  O     . TRP A 1 516 ? -3.971  5.692   27.504  1.00 22.53  ? 516  TRP A O     1 
ATOM   4009 C  CB    . TRP A 1 516 ? -5.223  5.684   24.858  1.00 21.29  ? 516  TRP A CB    1 
ATOM   4010 C  CG    . TRP A 1 516 ? -6.229  5.851   23.707  1.00 18.56  ? 516  TRP A CG    1 
ATOM   4011 C  CD1   . TRP A 1 516 ? -6.280  5.059   22.565  1.00 21.42  ? 516  TRP A CD1   1 
ATOM   4012 C  CD2   . TRP A 1 516 ? -7.307  6.793   23.582  1.00 16.79  ? 516  TRP A CD2   1 
ATOM   4013 N  NE1   . TRP A 1 516 ? -7.326  5.451   21.763  1.00 21.59  ? 516  TRP A NE1   1 
ATOM   4014 C  CE2   . TRP A 1 516 ? -7.985  6.493   22.376  1.00 18.48  ? 516  TRP A CE2   1 
ATOM   4015 C  CE3   . TRP A 1 516 ? -7.795  7.843   24.388  1.00 16.01  ? 516  TRP A CE3   1 
ATOM   4016 C  CZ2   . TRP A 1 516 ? -9.078  7.235   21.927  1.00 17.96  ? 516  TRP A CZ2   1 
ATOM   4017 C  CZ3   . TRP A 1 516 ? -8.897  8.563   23.948  1.00 19.32  ? 516  TRP A CZ3   1 
ATOM   4018 C  CH2   . TRP A 1 516 ? -9.536  8.257   22.736  1.00 17.05  ? 516  TRP A CH2   1 
ATOM   4019 N  N     . PHE A 1 517 ? -2.425  6.952   26.461  1.00 20.48  ? 517  PHE A N     1 
ATOM   4020 C  CA    . PHE A 1 517 ? -1.267  6.231   26.976  1.00 19.80  ? 517  PHE A CA    1 
ATOM   4021 C  C     . PHE A 1 517 ? -0.488  7.008   28.013  1.00 23.25  ? 517  PHE A C     1 
ATOM   4022 O  O     . PHE A 1 517 ? 0.621   6.607   28.360  1.00 26.52  ? 517  PHE A O     1 
ATOM   4023 C  CB    . PHE A 1 517 ? -0.367  5.827   25.815  1.00 23.07  ? 517  PHE A CB    1 
ATOM   4024 C  CG    . PHE A 1 517 ? -1.014  4.841   24.893  1.00 22.28  ? 517  PHE A CG    1 
ATOM   4025 C  CD1   . PHE A 1 517 ? -0.992  3.481   25.201  1.00 27.63  ? 517  PHE A CD1   1 
ATOM   4026 C  CD2   . PHE A 1 517 ? -1.707  5.260   23.769  1.00 23.95  ? 517  PHE A CD2   1 
ATOM   4027 C  CE1   . PHE A 1 517 ? -1.601  2.545   24.382  1.00 24.74  ? 517  PHE A CE1   1 
ATOM   4028 C  CE2   . PHE A 1 517 ? -2.329  4.326   22.939  1.00 22.25  ? 517  PHE A CE2   1 
ATOM   4029 C  CZ    . PHE A 1 517 ? -2.271  2.959   23.250  1.00 25.89  ? 517  PHE A CZ    1 
ATOM   4030 N  N     . ARG A 1 518 ? -1.049  8.083   28.547  1.00 24.08  ? 518  ARG A N     1 
ATOM   4031 C  CA    . ARG A 1 518 ? -0.329  8.848   29.547  1.00 29.52  ? 518  ARG A CA    1 
ATOM   4032 C  C     . ARG A 1 518 ? -0.238  8.034   30.834  1.00 31.34  ? 518  ARG A C     1 
ATOM   4033 O  O     . ARG A 1 518 ? -1.200  7.380   31.245  1.00 28.00  ? 518  ARG A O     1 
ATOM   4034 C  CB    . ARG A 1 518 ? -1.014  10.208  29.785  1.00 24.66  ? 518  ARG A CB    1 
ATOM   4035 C  CG    . ARG A 1 518 ? -0.080  11.258  30.365  1.00 27.76  ? 518  ARG A CG    1 
ATOM   4036 C  CD    . ARG A 1 518 ? -0.819  12.584  30.612  1.00 27.99  ? 518  ARG A CD    1 
ATOM   4037 N  NE    . ARG A 1 518 ? 0.073   13.567  31.206  1.00 28.10  ? 518  ARG A NE    1 
ATOM   4038 C  CZ    . ARG A 1 518 ? -0.136  14.879  31.174  1.00 28.25  ? 518  ARG A CZ    1 
ATOM   4039 N  NH1   . ARG A 1 518 ? -1.215  15.395  30.606  1.00 24.65  ? 518  ARG A NH1   1 
ATOM   4040 N  NH2   . ARG A 1 518 ? 0.783   15.696  31.691  1.00 27.29  ? 518  ARG A NH2   1 
ATOM   4041 N  N     . LYS A 1 519 ? 0.949   8.031   31.436  1.00 28.47  ? 519  LYS A N     1 
ATOM   4042 C  CA    . LYS A 1 519 ? 1.210   7.282   32.657  1.00 35.72  ? 519  LYS A CA    1 
ATOM   4043 C  C     . LYS A 1 519 ? 1.555   8.233   33.795  1.00 41.54  ? 519  LYS A C     1 
ATOM   4044 O  O     . LYS A 1 519 ? 2.096   9.320   33.573  1.00 37.06  ? 519  LYS A O     1 
ATOM   4045 C  CB    . LYS A 1 519 ? 2.354   6.279   32.458  1.00 36.28  ? 519  LYS A CB    1 
ATOM   4046 C  CG    . LYS A 1 519 ? 2.052   5.173   31.463  1.00 32.37  ? 519  LYS A CG    1 
ATOM   4047 C  CD    . LYS A 1 519 ? 3.249   4.259   31.297  1.00 32.69  ? 519  LYS A CD    1 
ATOM   4048 C  CE    . LYS A 1 519 ? 2.893   3.046   30.443  1.00 36.64  ? 519  LYS A CE    1 
ATOM   4049 N  NZ    . LYS A 1 519 ? 4.104   2.261   30.101  1.00 38.55  ? 519  LYS A NZ    1 
ATOM   4050 N  N     . ASP A 1 520 ? 1.234   7.825   35.021  1.00 43.07  ? 520  ASP A N     1 
ATOM   4051 C  CA    . ASP A 1 520 ? 1.633   8.591   36.195  1.00 54.01  ? 520  ASP A CA    1 
ATOM   4052 C  C     . ASP A 1 520 ? 3.067   8.217   36.579  1.00 56.29  ? 520  ASP A C     1 
ATOM   4053 O  O     . ASP A 1 520 ? 3.727   7.420   35.902  1.00 51.51  ? 520  ASP A O     1 
ATOM   4054 C  CB    . ASP A 1 520 ? 0.643   8.369   37.341  1.00 56.57  ? 520  ASP A CB    1 
ATOM   4055 C  CG    . ASP A 1 520 ? 0.553   6.901   37.779  1.00 55.66  ? 520  ASP A CG    1 
ATOM   4056 O  OD1   . ASP A 1 520 ? 1.421   6.081   37.389  1.00 55.58  ? 520  ASP A OD1   1 
ATOM   4057 O  OD2   . ASP A 1 520 ? -0.400  6.565   38.525  1.00 62.38  ? 520  ASP A OD2   1 
ATOM   4058 N  N     . LYS A 1 521 ? 3.555   8.776   37.693  1.00 60.35  ? 521  LYS A N     1 
ATOM   4059 C  CA    . LYS A 1 521 ? 4.915   8.481   38.139  1.00 62.80  ? 521  LYS A CA    1 
ATOM   4060 C  C     . LYS A 1 521 ? 5.129   6.988   38.382  1.00 63.30  ? 521  LYS A C     1 
ATOM   4061 O  O     . LYS A 1 521 ? 6.256   6.499   38.257  1.00 65.30  ? 521  LYS A O     1 
ATOM   4062 C  CB    . LYS A 1 521 ? 5.234   9.277   39.404  1.00 66.49  ? 521  LYS A CB    1 
ATOM   4063 C  CG    . LYS A 1 521 ? 5.239   10.782  39.205  1.00 74.83  ? 521  LYS A CG    1 
ATOM   4064 C  CD    . LYS A 1 521 ? 5.778   11.503  40.437  1.00 83.60  ? 521  LYS A CD    1 
ATOM   4065 C  CE    . LYS A 1 521 ? 5.942   13.002  40.193  1.00 82.48  ? 521  LYS A CE    1 
ATOM   4066 N  NZ    . LYS A 1 521 ? 6.515   13.695  41.383  1.00 76.74  ? 521  LYS A NZ    1 
ATOM   4067 N  N     . ASN A 1 522 ? 4.068   6.247   38.718  1.00 62.27  ? 522  ASN A N     1 
ATOM   4068 C  CA    . ASN A 1 522 ? 4.180   4.809   38.946  1.00 58.84  ? 522  ASN A CA    1 
ATOM   4069 C  C     . ASN A 1 522 ? 4.412   4.018   37.668  1.00 60.06  ? 522  ASN A C     1 
ATOM   4070 O  O     . ASN A 1 522 ? 4.683   2.812   37.749  1.00 53.89  ? 522  ASN A O     1 
ATOM   4071 C  CB    . ASN A 1 522 ? 2.913   4.255   39.614  1.00 63.53  ? 522  ASN A CB    1 
ATOM   4072 C  CG    . ASN A 1 522 ? 2.692   4.792   41.019  1.00 70.15  ? 522  ASN A CG    1 
ATOM   4073 O  OD1   . ASN A 1 522 ? 3.642   5.039   41.767  1.00 74.72  ? 522  ASN A OD1   1 
ATOM   4074 N  ND2   . ASN A 1 522 ? 1.423   4.962   41.388  1.00 63.96  ? 522  ASN A ND2   1 
ATOM   4075 N  N     . GLY A 1 523 ? 4.298   4.648   36.502  1.00 56.13  ? 523  GLY A N     1 
ATOM   4076 C  CA    . GLY A 1 523 ? 4.223   3.887   35.274  1.00 47.56  ? 523  GLY A CA    1 
ATOM   4077 C  C     . GLY A 1 523 ? 2.901   3.184   35.079  1.00 42.93  ? 523  GLY A C     1 
ATOM   4078 O  O     . GLY A 1 523 ? 2.834   2.196   34.340  1.00 45.05  ? 523  GLY A O     1 
ATOM   4079 N  N     . LYS A 1 524 ? 1.842   3.669   35.722  1.00 44.62  ? 524  LYS A N     1 
ATOM   4080 C  CA    . LYS A 1 524 ? 0.496   3.134   35.575  1.00 45.49  ? 524  LYS A CA    1 
ATOM   4081 C  C     . LYS A 1 524 ? -0.328  4.054   34.682  1.00 37.25  ? 524  LYS A C     1 
ATOM   4082 O  O     . LYS A 1 524 ? -0.238  5.277   34.805  1.00 41.84  ? 524  LYS A O     1 
ATOM   4083 C  CB    . LYS A 1 524 ? -0.164  3.001   36.952  1.00 47.69  ? 524  LYS A CB    1 
ATOM   4084 C  CG    . LYS A 1 524 ? -1.645  2.624   36.941  1.00 53.66  ? 524  LYS A CG    1 
ATOM   4085 C  CD    . LYS A 1 524 ? -2.215  2.598   38.368  1.00 57.76  ? 524  LYS A CD    1 
ATOM   4086 C  CE    . LYS A 1 524 ? -3.715  2.334   38.383  1.00 58.45  ? 524  LYS A CE    1 
ATOM   4087 N  NZ    . LYS A 1 524 ? -4.288  2.538   39.752  1.00 61.35  ? 524  LYS A NZ    1 
ATOM   4088 N  N     . PHE A 1 525 ? -1.141  3.463   33.796  1.00 34.64  ? 525  PHE A N     1 
ATOM   4089 C  CA    . PHE A 1 525 ? -1.999  4.245   32.903  1.00 32.61  ? 525  PHE A CA    1 
ATOM   4090 C  C     . PHE A 1 525 ? -2.996  5.088   33.688  1.00 37.31  ? 525  PHE A C     1 
ATOM   4091 O  O     . PHE A 1 525 ? -3.717  4.583   34.555  1.00 41.06  ? 525  PHE A O     1 
ATOM   4092 C  CB    . PHE A 1 525 ? -2.758  3.338   31.932  1.00 26.41  ? 525  PHE A CB    1 
ATOM   4093 C  CG    . PHE A 1 525 ? -1.907  2.779   30.815  1.00 31.60  ? 525  PHE A CG    1 
ATOM   4094 C  CD1   . PHE A 1 525 ? -1.141  3.613   30.021  1.00 32.28  ? 525  PHE A CD1   1 
ATOM   4095 C  CD2   . PHE A 1 525 ? -1.867  1.418   30.568  1.00 31.71  ? 525  PHE A CD2   1 
ATOM   4096 C  CE1   . PHE A 1 525 ? -0.354  3.095   28.992  1.00 32.78  ? 525  PHE A CE1   1 
ATOM   4097 C  CE2   . PHE A 1 525 ? -1.086  0.909   29.549  1.00 28.72  ? 525  PHE A CE2   1 
ATOM   4098 C  CZ    . PHE A 1 525 ? -0.332  1.758   28.766  1.00 27.96  ? 525  PHE A CZ    1 
ATOM   4099 N  N     . LEU A 1 526 ? -3.046  6.379   33.361  1.00 28.07  ? 526  LEU A N     1 
ATOM   4100 C  CA    . LEU A 1 526 ? -3.997  7.297   33.984  1.00 28.31  ? 526  LEU A CA    1 
ATOM   4101 C  C     . LEU A 1 526 ? -5.424  7.083   33.501  1.00 33.37  ? 526  LEU A C     1 
ATOM   4102 O  O     . LEU A 1 526 ? -6.368  7.447   34.203  1.00 33.39  ? 526  LEU A O     1 
ATOM   4103 C  CB    . LEU A 1 526 ? -3.588  8.745   33.701  1.00 30.06  ? 526  LEU A CB    1 
ATOM   4104 C  CG    . LEU A 1 526 ? -2.377  9.301   34.453  1.00 34.71  ? 526  LEU A CG    1 
ATOM   4105 C  CD1   . LEU A 1 526 ? -1.894  10.579  33.774  1.00 35.22  ? 526  LEU A CD1   1 
ATOM   4106 C  CD2   . LEU A 1 526 ? -2.748  9.590   35.903  1.00 36.86  ? 526  LEU A CD2   1 
ATOM   4107 N  N     . TRP A 1 527 ? -5.603  6.520   32.318  1.00 28.35  ? 527  TRP A N     1 
ATOM   4108 C  CA    . TRP A 1 527 ? -6.903  6.409   31.683  1.00 25.57  ? 527  TRP A CA    1 
ATOM   4109 C  C     . TRP A 1 527 ? -7.211  4.939   31.431  1.00 29.18  ? 527  TRP A C     1 
ATOM   4110 O  O     . TRP A 1 527 ? -6.357  4.217   30.882  1.00 27.67  ? 527  TRP A O     1 
ATOM   4111 C  CB    . TRP A 1 527 ? -6.906  7.179   30.358  1.00 24.19  ? 527  TRP A CB    1 
ATOM   4112 C  CG    . TRP A 1 527 ? -8.188  7.193   29.635  1.00 21.45  ? 527  TRP A CG    1 
ATOM   4113 C  CD1   . TRP A 1 527 ? -8.448  6.632   28.432  1.00 20.44  ? 527  TRP A CD1   1 
ATOM   4114 C  CD2   . TRP A 1 527 ? -9.397  7.816   30.067  1.00 23.95  ? 527  TRP A CD2   1 
ATOM   4115 N  NE1   . TRP A 1 527 ? -9.762  6.861   28.081  1.00 19.82  ? 527  TRP A NE1   1 
ATOM   4116 C  CE2   . TRP A 1 527 ? -10.364 7.585   29.073  1.00 21.21  ? 527  TRP A CE2   1 
ATOM   4117 C  CE3   . TRP A 1 527 ? -9.768  8.521   31.221  1.00 21.55  ? 527  TRP A CE3   1 
ATOM   4118 C  CZ2   . TRP A 1 527 ? -11.662 8.073   29.165  1.00 22.29  ? 527  TRP A CZ2   1 
ATOM   4119 C  CZ3   . TRP A 1 527 ? -11.062 9.009   31.310  1.00 24.16  ? 527  TRP A CZ3   1 
ATOM   4120 C  CH2   . TRP A 1 527 ? -11.996 8.780   30.291  1.00 23.17  ? 527  TRP A CH2   1 
ATOM   4121 N  N     . PRO A 1 528 ? -8.406  4.455   31.798  1.00 28.09  ? 528  PRO A N     1 
ATOM   4122 C  CA    . PRO A 1 528 ? -8.716  3.029   31.569  1.00 31.69  ? 528  PRO A CA    1 
ATOM   4123 C  C     . PRO A 1 528 ? -8.743  2.625   30.103  1.00 32.56  ? 528  PRO A C     1 
ATOM   4124 O  O     . PRO A 1 528 ? -8.423  1.464   29.789  1.00 24.61  ? 528  PRO A O     1 
ATOM   4125 C  CB    . PRO A 1 528 ? -10.099 2.846   32.229  1.00 26.79  ? 528  PRO A CB    1 
ATOM   4126 C  CG    . PRO A 1 528 ? -10.644 4.207   32.430  1.00 28.48  ? 528  PRO A CG    1 
ATOM   4127 C  CD    . PRO A 1 528 ? -9.458  5.144   32.560  1.00 26.10  ? 528  PRO A CD    1 
ATOM   4128 N  N     . GLY A 1 529 ? -9.144  3.530   29.198  1.00 26.93  ? 529  GLY A N     1 
ATOM   4129 C  CA    . GLY A 1 529 ? -9.106  3.224   27.778  1.00 23.52  ? 529  GLY A CA    1 
ATOM   4130 C  C     . GLY A 1 529 ? -10.188 2.258   27.294  1.00 26.23  ? 529  GLY A C     1 
ATOM   4131 O  O     . GLY A 1 529 ? -11.188 1.998   27.968  1.00 26.02  ? 529  GLY A O     1 
ATOM   4132 N  N     . PHE A 1 530 ? -9.946  1.715   26.092  1.00 23.29  ? 530  PHE A N     1 
ATOM   4133 C  CA    . PHE A 1 530 ? -10.809 0.740   25.423  1.00 25.49  ? 530  PHE A CA    1 
ATOM   4134 C  C     . PHE A 1 530 ? -12.232 1.291   25.371  1.00 28.68  ? 530  PHE A C     1 
ATOM   4135 O  O     . PHE A 1 530 ? -12.417 2.412   24.884  1.00 24.60  ? 530  PHE A O     1 
ATOM   4136 C  CB    . PHE A 1 530 ? -10.644 -0.616  26.118  1.00 24.74  ? 530  PHE A CB    1 
ATOM   4137 C  CG    . PHE A 1 530 ? -9.239  -1.100  26.088  1.00 18.24  ? 530  PHE A CG    1 
ATOM   4138 C  CD1   . PHE A 1 530 ? -8.708  -1.616  24.918  1.00 20.98  ? 530  PHE A CD1   1 
ATOM   4139 C  CD2   . PHE A 1 530 ? -8.432  -0.985  27.204  1.00 21.92  ? 530  PHE A CD2   1 
ATOM   4140 C  CE1   . PHE A 1 530 ? -7.398  -2.040  24.861  1.00 21.73  ? 530  PHE A CE1   1 
ATOM   4141 C  CE2   . PHE A 1 530 ? -7.102  -1.403  27.162  1.00 25.88  ? 530  PHE A CE2   1 
ATOM   4142 C  CZ    . PHE A 1 530 ? -6.590  -1.938  25.992  1.00 23.15  ? 530  PHE A CZ    1 
ATOM   4143 N  N     . GLY A 1 531 ? -13.242 0.548   25.838  1.00 26.10  ? 531  GLY A N     1 
ATOM   4144 C  CA    . GLY A 1 531 ? -14.612 0.995   25.728  1.00 23.83  ? 531  GLY A CA    1 
ATOM   4145 C  C     . GLY A 1 531 ? -14.888 2.293   26.447  1.00 19.76  ? 531  GLY A C     1 
ATOM   4146 O  O     . GLY A 1 531 ? -15.866 2.970   26.116  1.00 19.08  ? 531  GLY A O     1 
ATOM   4147 N  N     . GLU A 1 532 ? -14.052 2.661   27.427  1.00 18.16  ? 532  GLU A N     1 
ATOM   4148 C  CA    . GLU A 1 532 ? -14.273 3.929   28.107  1.00 18.84  ? 532  GLU A CA    1 
ATOM   4149 C  C     . GLU A 1 532 ? -13.899 5.115   27.225  1.00 20.27  ? 532  GLU A C     1 
ATOM   4150 O  O     . GLU A 1 532 ? -14.257 6.255   27.540  1.00 18.54  ? 532  GLU A O     1 
ATOM   4151 C  CB    . GLU A 1 532 ? -13.470 3.991   29.416  1.00 22.26  ? 532  GLU A CB    1 
ATOM   4152 C  CG    . GLU A 1 532 ? -13.749 2.820   30.393  1.00 21.87  ? 532  GLU A CG    1 
ATOM   4153 C  CD    . GLU A 1 532 ? -15.163 2.812   30.934  1.00 28.97  ? 532  GLU A CD    1 
ATOM   4154 O  OE1   . GLU A 1 532 ? -15.958 3.710   30.597  1.00 27.07  ? 532  GLU A OE1   1 
ATOM   4155 O  OE2   . GLU A 1 532 ? -15.485 1.890   31.722  1.00 30.76  ? 532  GLU A OE2   1 
ATOM   4156 N  N     . ASN A 1 533 ? -13.196 4.874   26.124  1.00 20.16  ? 533  ASN A N     1 
ATOM   4157 C  CA    . ASN A 1 533 ? -12.904 5.965   25.191  1.00 18.61  ? 533  ASN A CA    1 
ATOM   4158 C  C     . ASN A 1 533 ? -14.163 6.524   24.548  1.00 19.64  ? 533  ASN A C     1 
ATOM   4159 O  O     . ASN A 1 533 ? -14.112 7.610   23.954  1.00 22.23  ? 533  ASN A O     1 
ATOM   4160 C  CB    . ASN A 1 533 ? -11.940 5.446   24.114  1.00 15.79  ? 533  ASN A CB    1 
ATOM   4161 C  CG    . ASN A 1 533 ? -10.594 5.152   24.682  1.00 18.78  ? 533  ASN A CG    1 
ATOM   4162 O  OD1   . ASN A 1 533 ? -10.229 5.739   25.703  1.00 22.42  ? 533  ASN A OD1   1 
ATOM   4163 N  ND2   . ASN A 1 533 ? -9.814  4.260   24.019  1.00 20.74  ? 533  ASN A ND2   1 
ATOM   4164 N  N     . SER A 1 534 ? -15.289 5.814   24.658  1.00 24.44  ? 534  SER A N     1 
ATOM   4165 C  CA    . SER A 1 534 ? -16.572 6.394   24.288  1.00 23.60  ? 534  SER A CA    1 
ATOM   4166 C  C     . SER A 1 534 ? -16.841 7.710   25.018  1.00 20.94  ? 534  SER A C     1 
ATOM   4167 O  O     . SER A 1 534 ? -17.599 8.538   24.514  1.00 20.66  ? 534  SER A O     1 
ATOM   4168 C  CB    . SER A 1 534 ? -17.710 5.414   24.582  1.00 24.72  ? 534  SER A CB    1 
ATOM   4169 O  OG    . SER A 1 534 ? -17.801 5.120   25.966  1.00 20.98  ? 534  SER A OG    1 
ATOM   4170 N  N     . ARG A 1 535 ? -16.245 7.926   26.195  1.00 19.52  ? 535  ARG A N     1 
ATOM   4171 C  CA    . ARG A 1 535 ? -16.484 9.191   26.896  1.00 18.51  ? 535  ARG A CA    1 
ATOM   4172 C  C     . ARG A 1 535 ? -15.747 10.346  26.223  1.00 20.70  ? 535  ARG A C     1 
ATOM   4173 O  O     . ARG A 1 535 ? -16.223 11.489  26.262  1.00 20.76  ? 535  ARG A O     1 
ATOM   4174 C  CB    . ARG A 1 535 ? -16.068 9.101   28.364  1.00 24.42  ? 535  ARG A CB    1 
ATOM   4175 C  CG    . ARG A 1 535 ? -16.751 7.965   29.137  1.00 23.30  ? 535  ARG A CG    1 
ATOM   4176 C  CD    . ARG A 1 535 ? -15.944 7.595   30.375  1.00 27.94  ? 535  ARG A CD    1 
ATOM   4177 N  NE    . ARG A 1 535 ? -16.482 6.404   31.027  1.00 27.97  ? 535  ARG A NE    1 
ATOM   4178 C  CZ    . ARG A 1 535 ? -17.429 6.425   31.956  1.00 35.52  ? 535  ARG A CZ    1 
ATOM   4179 N  NH1   . ARG A 1 535 ? -17.994 7.558   32.343  1.00 29.88  ? 535  ARG A NH1   1 
ATOM   4180 N  NH2   . ARG A 1 535 ? -17.824 5.277   32.503  1.00 35.30  ? 535  ARG A NH2   1 
ATOM   4181 N  N     . VAL A 1 536 ? -14.600 10.064  25.607  1.00 17.78  ? 536  VAL A N     1 
ATOM   4182 C  CA    . VAL A 1 536 ? -13.900 11.079  24.810  1.00 17.77  ? 536  VAL A CA    1 
ATOM   4183 C  C     . VAL A 1 536 ? -14.653 11.346  23.511  1.00 21.22  ? 536  VAL A C     1 
ATOM   4184 O  O     . VAL A 1 536 ? -14.803 12.503  23.075  1.00 18.86  ? 536  VAL A O     1 
ATOM   4185 C  CB    . VAL A 1 536 ? -12.448 10.629  24.562  1.00 18.84  ? 536  VAL A CB    1 
ATOM   4186 C  CG1   . VAL A 1 536 ? -11.721 11.562  23.557  1.00 20.66  ? 536  VAL A CG1   1 
ATOM   4187 C  CG2   . VAL A 1 536 ? -11.681 10.600  25.878  1.00 18.12  ? 536  VAL A CG2   1 
ATOM   4188 N  N     . LEU A 1 537 ? -15.137 10.288  22.863  1.00 18.27  ? 537  LEU A N     1 
ATOM   4189 C  CA    . LEU A 1 537 ? -15.930 10.481  21.651  1.00 16.82  ? 537  LEU A CA    1 
ATOM   4190 C  C     . LEU A 1 537 ? -17.164 11.340  21.915  1.00 20.32  ? 537  LEU A C     1 
ATOM   4191 O  O     . LEU A 1 537 ? -17.525 12.190  21.091  1.00 21.00  ? 537  LEU A O     1 
ATOM   4192 C  CB    . LEU A 1 537 ? -16.336 9.132   21.079  1.00 21.50  ? 537  LEU A CB    1 
ATOM   4193 C  CG    . LEU A 1 537 ? -15.155 8.229   20.666  1.00 25.43  ? 537  LEU A CG    1 
ATOM   4194 C  CD1   . LEU A 1 537 ? -15.688 6.899   20.157  1.00 29.48  ? 537  LEU A CD1   1 
ATOM   4195 C  CD2   . LEU A 1 537 ? -14.290 8.871   19.637  1.00 19.85  ? 537  LEU A CD2   1 
ATOM   4196 N  N     . GLU A 1 538 ? -17.841 11.124  23.049  1.00 22.76  ? 538  GLU A N     1 
ATOM   4197 C  CA    . GLU A 1 538 ? -18.998 11.963  23.369  1.00 20.92  ? 538  GLU A CA    1 
ATOM   4198 C  C     . GLU A 1 538 ? -18.622 13.443  23.382  1.00 22.29  ? 538  GLU A C     1 
ATOM   4199 O  O     . GLU A 1 538 ? -19.342 14.285  22.836  1.00 18.58  ? 538  GLU A O     1 
ATOM   4200 C  CB    . GLU A 1 538 ? -19.584 11.545  24.717  1.00 21.59  ? 538  GLU A CB    1 
ATOM   4201 C  CG    . GLU A 1 538 ? -20.540 12.540  25.331  1.00 22.26  ? 538  GLU A CG    1 
ATOM   4202 C  CD    . GLU A 1 538 ? -21.248 11.962  26.563  1.00 35.02  ? 538  GLU A CD    1 
ATOM   4203 O  OE1   . GLU A 1 538 ? -20.558 11.662  27.554  1.00 27.56  ? 538  GLU A OE1   1 
ATOM   4204 O  OE2   . GLU A 1 538 ? -22.481 11.791  26.518  1.00 33.15  ? 538  GLU A OE2   1 
ATOM   4205 N  N     . TRP A 1 539 ? -17.476 13.775  23.973  1.00 17.00  ? 539  TRP A N     1 
ATOM   4206 C  CA    . TRP A 1 539 ? -17.051 15.163  23.987  1.00 17.81  ? 539  TRP A CA    1 
ATOM   4207 C  C     . TRP A 1 539 ? -16.805 15.682  22.569  1.00 21.84  ? 539  TRP A C     1 
ATOM   4208 O  O     . TRP A 1 539 ? -17.232 16.793  22.229  1.00 18.68  ? 539  TRP A O     1 
ATOM   4209 C  CB    . TRP A 1 539 ? -15.791 15.318  24.852  1.00 20.21  ? 539  TRP A CB    1 
ATOM   4210 C  CG    . TRP A 1 539 ? -15.378 16.764  24.966  1.00 21.81  ? 539  TRP A CG    1 
ATOM   4211 C  CD1   . TRP A 1 539 ? -15.982 17.725  25.757  1.00 22.75  ? 539  TRP A CD1   1 
ATOM   4212 C  CD2   . TRP A 1 539 ? -14.319 17.426  24.263  1.00 20.40  ? 539  TRP A CD2   1 
ATOM   4213 N  NE1   . TRP A 1 539 ? -15.350 18.934  25.586  1.00 23.18  ? 539  TRP A NE1   1 
ATOM   4214 C  CE2   . TRP A 1 539 ? -14.324 18.783  24.686  1.00 18.83  ? 539  TRP A CE2   1 
ATOM   4215 C  CE3   . TRP A 1 539 ? -13.341 17.002  23.330  1.00 20.34  ? 539  TRP A CE3   1 
ATOM   4216 C  CZ2   . TRP A 1 539 ? -13.408 19.743  24.190  1.00 16.59  ? 539  TRP A CZ2   1 
ATOM   4217 C  CZ3   . TRP A 1 539 ? -12.427 17.953  22.843  1.00 24.67  ? 539  TRP A CZ3   1 
ATOM   4218 C  CH2   . TRP A 1 539 ? -12.469 19.313  23.289  1.00 24.80  ? 539  TRP A CH2   1 
ATOM   4219 N  N     . MET A 1 540 ? -16.124 14.890  21.722  1.00 18.58  ? 540  MET A N     1 
ATOM   4220 C  CA    . MET A 1 540 ? -15.893 15.297  20.339  1.00 22.15  ? 540  MET A CA    1 
ATOM   4221 C  C     . MET A 1 540 ? -17.204 15.488  19.603  1.00 17.57  ? 540  MET A C     1 
ATOM   4222 O  O     . MET A 1 540 ? -17.346 16.412  18.808  1.00 19.33  ? 540  MET A O     1 
ATOM   4223 C  CB    . MET A 1 540 ? -15.052 14.235  19.599  1.00 14.86  ? 540  MET A CB    1 
ATOM   4224 C  CG    . MET A 1 540 ? -13.761 13.920  20.264  1.00 15.54  ? 540  MET A CG    1 
ATOM   4225 S  SD    . MET A 1 540 ? -12.947 12.617  19.297  1.00 21.38  ? 540  MET A SD    1 
ATOM   4226 C  CE    . MET A 1 540 ? -11.349 12.635  20.107  1.00 15.97  ? 540  MET A CE    1 
ATOM   4227 N  N     . PHE A 1 541 ? -18.166 14.607  19.854  1.00 15.60  ? 541  PHE A N     1 
ATOM   4228 C  CA    . PHE A 1 541 ? -19.472 14.686  19.201  1.00 15.98  ? 541  PHE A CA    1 
ATOM   4229 C  C     . PHE A 1 541 ? -20.159 15.996  19.560  1.00 20.37  ? 541  PHE A C     1 
ATOM   4230 O  O     . PHE A 1 541 ? -20.740 16.670  18.697  1.00 22.92  ? 541  PHE A O     1 
ATOM   4231 C  CB    . PHE A 1 541 ? -20.328 13.484  19.660  1.00 18.91  ? 541  PHE A CB    1 
ATOM   4232 C  CG    . PHE A 1 541 ? -21.542 13.207  18.802  1.00 18.54  ? 541  PHE A CG    1 
ATOM   4233 C  CD1   . PHE A 1 541 ? -22.630 14.075  18.800  1.00 23.44  ? 541  PHE A CD1   1 
ATOM   4234 C  CD2   . PHE A 1 541 ? -21.601 12.059  18.025  1.00 21.29  ? 541  PHE A CD2   1 
ATOM   4235 C  CE1   . PHE A 1 541 ? -23.746 13.823  18.007  1.00 23.25  ? 541  PHE A CE1   1 
ATOM   4236 C  CE2   . PHE A 1 541 ? -22.728 11.798  17.237  1.00 20.22  ? 541  PHE A CE2   1 
ATOM   4237 C  CZ    . PHE A 1 541 ? -23.795 12.681  17.244  1.00 22.79  ? 541  PHE A CZ    1 
ATOM   4238 N  N     . GLY A 1 542 ? -20.101 16.366  20.837  1.00 22.37  ? 542  GLY A N     1 
ATOM   4239 C  CA    . GLY A 1 542 ? -20.692 17.630  21.260  1.00 22.21  ? 542  GLY A CA    1 
ATOM   4240 C  C     . GLY A 1 542 ? -19.980 18.824  20.655  1.00 20.78  ? 542  GLY A C     1 
ATOM   4241 O  O     . GLY A 1 542 ? -20.614 19.817  20.278  1.00 22.10  ? 542  GLY A O     1 
ATOM   4242 N  N     . ARG A 1 543 ? -18.649 18.757  20.564  1.00 22.92  ? 543  ARG A N     1 
ATOM   4243 C  CA    . ARG A 1 543 ? -17.903 19.863  19.960  1.00 19.61  ? 543  ARG A CA    1 
ATOM   4244 C  C     . ARG A 1 543 ? -18.243 20.026  18.481  1.00 22.76  ? 543  ARG A C     1 
ATOM   4245 O  O     . ARG A 1 543 ? -18.301 21.152  17.969  1.00 25.04  ? 543  ARG A O     1 
ATOM   4246 C  CB    . ARG A 1 543 ? -16.396 19.647  20.165  1.00 18.47  ? 543  ARG A CB    1 
ATOM   4247 C  CG    . ARG A 1 543 ? -15.915 19.932  21.593  1.00 20.99  ? 543  ARG A CG    1 
ATOM   4248 C  CD    . ARG A 1 543 ? -16.153 21.397  21.963  1.00 23.07  ? 543  ARG A CD    1 
ATOM   4249 N  NE    . ARG A 1 543 ? -15.308 22.268  21.139  1.00 21.00  ? 543  ARG A NE    1 
ATOM   4250 C  CZ    . ARG A 1 543 ? -15.547 23.546  20.931  1.00 32.86  ? 543  ARG A CZ    1 
ATOM   4251 N  NH1   . ARG A 1 543 ? -16.591 24.143  21.489  1.00 29.38  ? 543  ARG A NH1   1 
ATOM   4252 N  NH2   . ARG A 1 543 ? -14.711 24.245  20.160  1.00 26.17  ? 543  ARG A NH2   1 
ATOM   4253 N  N     . ILE A 1 544 ? -18.433 18.921  17.754  1.00 23.51  ? 544  ILE A N     1 
ATOM   4254 C  CA    . ILE A 1 544 ? -18.806 19.047  16.342  1.00 21.76  ? 544  ILE A CA    1 
ATOM   4255 C  C     . ILE A 1 544 ? -20.177 19.709  16.213  1.00 24.96  ? 544  ILE A C     1 
ATOM   4256 O  O     . ILE A 1 544 ? -20.422 20.504  15.295  1.00 24.93  ? 544  ILE A O     1 
ATOM   4257 C  CB    . ILE A 1 544 ? -18.755 17.674  15.645  1.00 18.90  ? 544  ILE A CB    1 
ATOM   4258 C  CG1   . ILE A 1 544 ? -17.310 17.234  15.505  1.00 20.46  ? 544  ILE A CG1   1 
ATOM   4259 C  CG2   . ILE A 1 544 ? -19.478 17.718  14.301  1.00 21.89  ? 544  ILE A CG2   1 
ATOM   4260 C  CD1   . ILE A 1 544 ? -17.163 15.671  15.347  1.00 22.85  ? 544  ILE A CD1   1 
ATOM   4261 N  N     . GLU A 1 545 ? -21.078 19.415  17.142  1.00 22.54  ? 545  GLU A N     1 
ATOM   4262 C  CA    . GLU A 1 545 ? -22.408 20.035  17.141  1.00 25.48  ? 545  GLU A CA    1 
ATOM   4263 C  C     . GLU A 1 545 ? -22.394 21.475  17.630  1.00 29.89  ? 545  GLU A C     1 
ATOM   4264 O  O     . GLU A 1 545 ? -23.417 22.156  17.524  1.00 27.04  ? 545  GLU A O     1 
ATOM   4265 C  CB    . GLU A 1 545 ? -23.375 19.243  18.019  1.00 24.39  ? 545  GLU A CB    1 
ATOM   4266 C  CG    . GLU A 1 545 ? -23.802 17.897  17.451  1.00 20.85  ? 545  GLU A CG    1 
ATOM   4267 C  CD    . GLU A 1 545 ? -25.009 17.342  18.195  1.00 31.27  ? 545  GLU A CD    1 
ATOM   4268 O  OE1   . GLU A 1 545 ? -25.132 17.577  19.419  1.00 34.86  ? 545  GLU A OE1   1 
ATOM   4269 O  OE2   . GLU A 1 545 ? -25.855 16.724  17.542  1.00 32.24  ? 545  GLU A OE2   1 
ATOM   4270 N  N     . GLY A 1 546 ? -21.296 21.933  18.207  1.00 27.17  ? 546  GLY A N     1 
ATOM   4271 C  CA    . GLY A 1 546 ? -21.166 23.308  18.605  1.00 29.99  ? 546  GLY A CA    1 
ATOM   4272 C  C     . GLY A 1 546 ? -21.344 23.572  20.074  1.00 34.81  ? 546  GLY A C     1 
ATOM   4273 O  O     . GLY A 1 546 ? -21.610 24.717  20.437  1.00 30.43  ? 546  GLY A O     1 
ATOM   4274 N  N     . GLU A 1 547 ? -21.202 22.564  20.933  1.00 28.71  ? 547  GLU A N     1 
ATOM   4275 C  CA    . GLU A 1 547 ? -21.404 22.792  22.357  1.00 29.07  ? 547  GLU A CA    1 
ATOM   4276 C  C     . GLU A 1 547 ? -20.260 23.601  22.962  1.00 31.70  ? 547  GLU A C     1 
ATOM   4277 O  O     . GLU A 1 547 ? -19.098 23.476  22.571  1.00 28.94  ? 547  GLU A O     1 
ATOM   4278 C  CB    . GLU A 1 547 ? -21.574 21.469  23.105  1.00 28.80  ? 547  GLU A CB    1 
ATOM   4279 C  CG    . GLU A 1 547 ? -23.003 21.018  23.135  1.00 42.90  ? 547  GLU A CG    1 
ATOM   4280 C  CD    . GLU A 1 547 ? -23.160 19.636  23.742  1.00 52.72  ? 547  GLU A CD    1 
ATOM   4281 O  OE1   . GLU A 1 547 ? -22.186 19.144  24.362  1.00 50.72  ? 547  GLU A OE1   1 
ATOM   4282 O  OE2   . GLU A 1 547 ? -24.253 19.040  23.589  1.00 62.30  ? 547  GLU A OE2   1 
ATOM   4283 N  N     . ASP A 1 548 ? -20.610 24.439  23.932  1.00 29.40  ? 548  ASP A N     1 
ATOM   4284 C  CA    . ASP A 1 548 ? -19.665 25.326  24.606  1.00 33.83  ? 548  ASP A CA    1 
ATOM   4285 C  C     . ASP A 1 548 ? -18.974 24.571  25.745  1.00 32.41  ? 548  ASP A C     1 
ATOM   4286 O  O     . ASP A 1 548 ? -19.100 24.892  26.927  1.00 35.32  ? 548  ASP A O     1 
ATOM   4287 C  CB    . ASP A 1 548 ? -20.419 26.554  25.102  1.00 38.53  ? 548  ASP A CB    1 
ATOM   4288 C  CG    . ASP A 1 548 ? -19.505 27.657  25.569  1.00 40.89  ? 548  ASP A CG    1 
ATOM   4289 O  OD1   . ASP A 1 548 ? -18.369 27.763  25.061  1.00 42.72  ? 548  ASP A OD1   1 
ATOM   4290 O  OD2   . ASP A 1 548 ? -19.939 28.431  26.447  1.00 43.78  ? 548  ASP A OD2   1 
ATOM   4291 N  N     . SER A 1 549 ? -18.254 23.512  25.363  1.00 25.27  ? 549  SER A N     1 
ATOM   4292 C  CA    . SER A 1 549 ? -17.733 22.554  26.331  1.00 25.84  ? 549  SER A CA    1 
ATOM   4293 C  C     . SER A 1 549 ? -16.210 22.537  26.374  1.00 25.99  ? 549  SER A C     1 
ATOM   4294 O  O     . SER A 1 549 ? -15.637 21.597  26.939  1.00 24.89  ? 549  SER A O     1 
ATOM   4295 C  CB    . SER A 1 549 ? -18.252 21.159  25.995  1.00 25.04  ? 549  SER A CB    1 
ATOM   4296 O  OG    . SER A 1 549 ? -17.781 20.832  24.706  1.00 25.14  ? 549  SER A OG    1 
ATOM   4297 N  N     . ALA A 1 550 ? -15.551 23.545  25.785  1.00 25.86  ? 550  ALA A N     1 
ATOM   4298 C  CA    . ALA A 1 550 ? -14.102 23.631  25.674  1.00 23.88  ? 550  ALA A CA    1 
ATOM   4299 C  C     . ALA A 1 550 ? -13.546 24.861  26.381  1.00 28.60  ? 550  ALA A C     1 
ATOM   4300 O  O     . ALA A 1 550 ? -14.186 25.918  26.441  1.00 25.91  ? 550  ALA A O     1 
ATOM   4301 C  CB    . ALA A 1 550 ? -13.650 23.690  24.207  1.00 23.35  ? 550  ALA A CB    1 
ATOM   4302 N  N     . LYS A 1 551 ? -12.325 24.699  26.887  1.00 25.15  ? 551  LYS A N     1 
ATOM   4303 C  CA    . LYS A 1 551 ? -11.502 25.766  27.433  1.00 26.03  ? 551  LYS A CA    1 
ATOM   4304 C  C     . LYS A 1 551 ? -10.250 25.939  26.571  1.00 25.01  ? 551  LYS A C     1 
ATOM   4305 O  O     . LYS A 1 551 ? -9.688  24.967  26.073  1.00 21.46  ? 551  LYS A O     1 
ATOM   4306 C  CB    . LYS A 1 551 ? -11.136 25.409  28.871  1.00 33.23  ? 551  LYS A CB    1 
ATOM   4307 C  CG    . LYS A 1 551 ? -10.013 26.182  29.493  1.00 36.73  ? 551  LYS A CG    1 
ATOM   4308 C  CD    . LYS A 1 551 ? -9.814  25.698  30.930  1.00 46.38  ? 551  LYS A CD    1 
ATOM   4309 C  CE    . LYS A 1 551 ? -9.638  24.194  30.972  1.00 42.05  ? 551  LYS A CE    1 
ATOM   4310 N  NZ    . LYS A 1 551 ? -9.362  23.689  32.354  1.00 56.15  ? 551  LYS A NZ    1 
ATOM   4311 N  N     . LEU A 1 552 ? -9.778  27.174  26.414  1.00 24.03  ? 552  LEU A N     1 
ATOM   4312 C  CA    . LEU A 1 552 ? -8.618  27.408  25.569  1.00 25.17  ? 552  LEU A CA    1 
ATOM   4313 C  C     . LEU A 1 552 ? -7.337  27.185  26.364  1.00 24.51  ? 552  LEU A C     1 
ATOM   4314 O  O     . LEU A 1 552 ? -7.212  27.660  27.492  1.00 26.81  ? 552  LEU A O     1 
ATOM   4315 C  CB    . LEU A 1 552 ? -8.668  28.835  25.009  1.00 28.66  ? 552  LEU A CB    1 
ATOM   4316 C  CG    . LEU A 1 552 ? -7.523  29.282  24.103  1.00 28.07  ? 552  LEU A CG    1 
ATOM   4317 C  CD1   . LEU A 1 552 ? -7.530  28.489  22.774  1.00 27.84  ? 552  LEU A CD1   1 
ATOM   4318 C  CD2   . LEU A 1 552 ? -7.585  30.795  23.845  1.00 31.81  ? 552  LEU A CD2   1 
ATOM   4319 N  N     . THR A 1 553 ? -6.392  26.444  25.797  1.00 21.92  ? 553  THR A N     1 
ATOM   4320 C  CA    . THR A 1 553 ? -5.064  26.285  26.373  1.00 21.41  ? 553  THR A CA    1 
ATOM   4321 C  C     . THR A 1 553 ? -4.045  26.665  25.313  1.00 27.54  ? 553  THR A C     1 
ATOM   4322 O  O     . THR A 1 553 ? -4.408  26.928  24.163  1.00 21.07  ? 553  THR A O     1 
ATOM   4323 C  CB    . THR A 1 553 ? -4.827  24.841  26.873  1.00 24.10  ? 553  THR A CB    1 
ATOM   4324 O  OG1   . THR A 1 553 ? -4.536  23.963  25.778  1.00 22.44  ? 553  THR A OG1   1 
ATOM   4325 C  CG2   . THR A 1 553 ? -6.035  24.329  27.674  1.00 21.20  ? 553  THR A CG2   1 
ATOM   4326 N  N     . PRO A 1 554 ? -2.756  26.731  25.665  1.00 22.91  ? 554  PRO A N     1 
ATOM   4327 C  CA    . PRO A 1 554 ? -1.744  27.009  24.636  1.00 30.48  ? 554  PRO A CA    1 
ATOM   4328 C  C     . PRO A 1 554 ? -1.627  25.934  23.558  1.00 27.07  ? 554  PRO A C     1 
ATOM   4329 O  O     . PRO A 1 554 ? -1.111  26.249  22.478  1.00 26.07  ? 554  PRO A O     1 
ATOM   4330 C  CB    . PRO A 1 554 ? -0.438  27.127  25.444  1.00 25.64  ? 554  PRO A CB    1 
ATOM   4331 C  CG    . PRO A 1 554 ? -0.876  27.485  26.816  1.00 28.66  ? 554  PRO A CG    1 
ATOM   4332 C  CD    . PRO A 1 554 ? -2.178  26.795  27.020  1.00 28.83  ? 554  PRO A CD    1 
ATOM   4333 N  N     . ILE A 1 555 ? -2.070  24.688  23.790  1.00 18.67  ? 555  ILE A N     1 
ATOM   4334 C  CA    . ILE A 1 555 ? -1.917  23.649  22.768  1.00 24.55  ? 555  ILE A CA    1 
ATOM   4335 C  C     . ILE A 1 555 ? -3.197  23.409  21.984  1.00 26.32  ? 555  ILE A C     1 
ATOM   4336 O  O     . ILE A 1 555 ? -3.193  22.587  21.045  1.00 22.15  ? 555  ILE A O     1 
ATOM   4337 C  CB    . ILE A 1 555 ? -1.409  22.323  23.369  1.00 25.79  ? 555  ILE A CB    1 
ATOM   4338 C  CG1   . ILE A 1 555 ? -2.479  21.744  24.303  1.00 21.89  ? 555  ILE A CG1   1 
ATOM   4339 C  CG2   . ILE A 1 555 ? -0.108  22.578  24.117  1.00 23.37  ? 555  ILE A CG2   1 
ATOM   4340 C  CD1   . ILE A 1 555 ? -2.248  20.322  24.717  1.00 22.80  ? 555  ILE A CD1   1 
ATOM   4341 N  N     . GLY A 1 556 ? -4.273  24.154  22.291  1.00 22.06  ? 556  GLY A N     1 
ATOM   4342 C  CA    . GLY A 1 556 ? -5.596  24.019  21.708  1.00 23.94  ? 556  GLY A CA    1 
ATOM   4343 C  C     . GLY A 1 556 ? -6.668  23.889  22.790  1.00 26.49  ? 556  GLY A C     1 
ATOM   4344 O  O     . GLY A 1 556 ? -6.443  24.186  23.974  1.00 26.28  ? 556  GLY A O     1 
ATOM   4345 N  N     . TYR A 1 557 ? -7.866  23.468  22.378  1.00 18.65  ? 557  TYR A N     1 
ATOM   4346 C  CA    . TYR A 1 557 ? -9.017  23.420  23.275  1.00 23.84  ? 557  TYR A CA    1 
ATOM   4347 C  C     . TYR A 1 557 ? -9.054  22.080  23.983  1.00 25.38  ? 557  TYR A C     1 
ATOM   4348 O  O     . TYR A 1 557 ? -8.853  21.043  23.348  1.00 21.62  ? 557  TYR A O     1 
ATOM   4349 C  CB    . TYR A 1 557 ? -10.339 23.594  22.520  1.00 22.86  ? 557  TYR A CB    1 
ATOM   4350 C  CG    . TYR A 1 557 ? -10.534 24.927  21.837  1.00 26.43  ? 557  TYR A CG    1 
ATOM   4351 C  CD1   . TYR A 1 557 ? -10.797 26.072  22.569  1.00 26.46  ? 557  TYR A CD1   1 
ATOM   4352 C  CD2   . TYR A 1 557 ? -10.495 25.022  20.454  1.00 28.01  ? 557  TYR A CD2   1 
ATOM   4353 C  CE1   . TYR A 1 557 ? -10.984 27.301  21.933  1.00 35.53  ? 557  TYR A CE1   1 
ATOM   4354 C  CE2   . TYR A 1 557 ? -10.675 26.231  19.802  1.00 31.98  ? 557  TYR A CE2   1 
ATOM   4355 C  CZ    . TYR A 1 557 ? -10.922 27.371  20.551  1.00 35.93  ? 557  TYR A CZ    1 
ATOM   4356 O  OH    . TYR A 1 557 ? -11.110 28.568  19.903  1.00 45.79  ? 557  TYR A OH    1 
ATOM   4357 N  N     . VAL A 1 558 ? -9.330  22.108  25.282  1.00 22.20  ? 558  VAL A N     1 
ATOM   4358 C  CA    . VAL A 1 558 ? -9.514  20.900  26.088  1.00 21.74  ? 558  VAL A CA    1 
ATOM   4359 C  C     . VAL A 1 558 ? -10.905 20.962  26.707  1.00 18.73  ? 558  VAL A C     1 
ATOM   4360 O  O     . VAL A 1 558 ? -11.534 22.028  26.736  1.00 20.99  ? 558  VAL A O     1 
ATOM   4361 C  CB    . VAL A 1 558 ? -8.432  20.765  27.186  1.00 25.25  ? 558  VAL A CB    1 
ATOM   4362 C  CG1   . VAL A 1 558 ? -7.042  20.757  26.602  1.00 22.96  ? 558  VAL A CG1   1 
ATOM   4363 C  CG2   . VAL A 1 558 ? -8.612  21.858  28.276  1.00 26.88  ? 558  VAL A CG2   1 
ATOM   4364 N  N     . PRO A 1 559 ? -11.419 19.833  27.218  1.00 23.63  ? 559  PRO A N     1 
ATOM   4365 C  CA    . PRO A 1 559 ? -12.732 19.870  27.878  1.00 20.93  ? 559  PRO A CA    1 
ATOM   4366 C  C     . PRO A 1 559 ? -12.710 20.786  29.095  1.00 24.22  ? 559  PRO A C     1 
ATOM   4367 O  O     . PRO A 1 559 ? -11.746 20.803  29.870  1.00 20.60  ? 559  PRO A O     1 
ATOM   4368 C  CB    . PRO A 1 559 ? -12.982 18.412  28.288  1.00 22.51  ? 559  PRO A CB    1 
ATOM   4369 C  CG    . PRO A 1 559 ? -12.039 17.600  27.466  1.00 20.12  ? 559  PRO A CG    1 
ATOM   4370 C  CD    . PRO A 1 559 ? -10.880 18.460  27.106  1.00 20.71  ? 559  PRO A CD    1 
ATOM   4371 N  N     . LYS A 1 560 ? -13.789 21.548  29.256  1.00 26.73  ? 560  LYS A N     1 
ATOM   4372 C  CA    . LYS A 1 560 ? -14.011 22.274  30.499  1.00 29.99  ? 560  LYS A CA    1 
ATOM   4373 C  C     . LYS A 1 560 ? -14.115 21.307  31.665  1.00 38.41  ? 560  LYS A C     1 
ATOM   4374 O  O     . LYS A 1 560 ? -14.458 20.134  31.502  1.00 30.88  ? 560  LYS A O     1 
ATOM   4375 C  CB    . LYS A 1 560 ? -15.312 23.079  30.467  1.00 28.04  ? 560  LYS A CB    1 
ATOM   4376 C  CG    . LYS A 1 560 ? -15.404 24.102  29.400  1.00 29.36  ? 560  LYS A CG    1 
ATOM   4377 C  CD    . LYS A 1 560 ? -16.620 24.940  29.669  1.00 30.60  ? 560  LYS A CD    1 
ATOM   4378 C  CE    . LYS A 1 560 ? -16.780 26.015  28.649  1.00 32.88  ? 560  LYS A CE    1 
ATOM   4379 N  NZ    . LYS A 1 560 ? -18.055 26.794  28.824  1.00 34.01  ? 560  LYS A NZ    1 
ATOM   4380 N  N     . GLU A 1 561 ? -13.817 21.828  32.857  1.00 41.45  ? 561  GLU A N     1 
ATOM   4381 C  CA    . GLU A 1 561 ? -14.164 21.146  34.098  1.00 50.99  ? 561  GLU A CA    1 
ATOM   4382 C  C     . GLU A 1 561 ? -15.591 20.628  34.012  1.00 44.17  ? 561  GLU A C     1 
ATOM   4383 O  O     . GLU A 1 561 ? -16.503 21.352  33.595  1.00 46.72  ? 561  GLU A O     1 
ATOM   4384 C  CB    . GLU A 1 561 ? -14.022 22.106  35.291  1.00 53.06  ? 561  GLU A CB    1 
ATOM   4385 C  CG    . GLU A 1 561 ? -14.464 21.512  36.645  1.00 66.97  ? 561  GLU A CG    1 
ATOM   4386 C  CD    . GLU A 1 561 ? -14.806 22.572  37.704  1.00 66.77  ? 561  GLU A CD    1 
ATOM   4387 O  OE1   . GLU A 1 561 ? -14.602 23.773  37.438  1.00 69.01  ? 561  GLU A OE1   1 
ATOM   4388 O  OE2   . GLU A 1 561 ? -15.287 22.197  38.799  1.00 72.62  ? 561  GLU A OE2   1 
ATOM   4389 N  N     . ASP A 1 562 ? -15.772 19.364  34.380  1.00 38.72  ? 562  ASP A N     1 
ATOM   4390 C  CA    . ASP A 1 562 ? -17.066 18.693  34.395  1.00 44.80  ? 562  ASP A CA    1 
ATOM   4391 C  C     . ASP A 1 562 ? -17.651 18.483  33.001  1.00 42.01  ? 562  ASP A C     1 
ATOM   4392 O  O     . ASP A 1 562 ? -18.782 18.009  32.896  1.00 37.80  ? 562  ASP A O     1 
ATOM   4393 C  CB    . ASP A 1 562 ? -18.118 19.438  35.244  1.00 53.37  ? 562  ASP A CB    1 
ATOM   4394 C  CG    . ASP A 1 562 ? -17.660 19.692  36.683  1.00 63.46  ? 562  ASP A CG    1 
ATOM   4395 O  OD1   . ASP A 1 562 ? -16.908 18.859  37.246  1.00 59.97  ? 562  ASP A OD1   1 
ATOM   4396 O  OD2   . ASP A 1 562 ? -18.062 20.735  37.255  1.00 70.56  ? 562  ASP A OD2   1 
ATOM   4397 N  N     . ALA A 1 563 ? -16.938 18.816  31.922  1.00 40.36  ? 563  ALA A N     1 
ATOM   4398 C  CA    . ALA A 1 563 ? -17.541 18.584  30.612  1.00 34.29  ? 563  ALA A CA    1 
ATOM   4399 C  C     . ALA A 1 563 ? -17.406 17.123  30.165  1.00 33.11  ? 563  ALA A C     1 
ATOM   4400 O  O     . ALA A 1 563 ? -18.212 16.655  29.352  1.00 29.87  ? 563  ALA A O     1 
ATOM   4401 C  CB    . ALA A 1 563 ? -16.944 19.542  29.575  1.00 29.16  ? 563  ALA A CB    1 
ATOM   4402 N  N     . LEU A 1 564 ? -16.430 16.382  30.690  1.00 27.62  ? 564  LEU A N     1 
ATOM   4403 C  CA    . LEU A 1 564 ? -16.302 14.958  30.377  1.00 29.73  ? 564  LEU A CA    1 
ATOM   4404 C  C     . LEU A 1 564 ? -17.145 14.130  31.339  1.00 31.81  ? 564  LEU A C     1 
ATOM   4405 O  O     . LEU A 1 564 ? -17.053 14.301  32.556  1.00 34.98  ? 564  LEU A O     1 
ATOM   4406 C  CB    . LEU A 1 564 ? -14.850 14.501  30.471  1.00 30.68  ? 564  LEU A CB    1 
ATOM   4407 C  CG    . LEU A 1 564 ? -13.925 14.551  29.267  1.00 32.13  ? 564  LEU A CG    1 
ATOM   4408 C  CD1   . LEU A 1 564 ? -12.694 13.752  29.616  1.00 29.82  ? 564  LEU A CD1   1 
ATOM   4409 C  CD2   . LEU A 1 564 ? -14.617 13.971  28.066  1.00 30.40  ? 564  LEU A CD2   1 
ATOM   4410 N  N     . ASN A 1 565 ? -17.960 13.240  30.786  1.00 28.07  ? 565  ASN A N     1 
ATOM   4411 C  CA    . ASN A 1 565 ? -18.773 12.289  31.547  1.00 31.76  ? 565  ASN A CA    1 
ATOM   4412 C  C     . ASN A 1 565 ? -17.843 11.264  32.177  1.00 33.13  ? 565  ASN A C     1 
ATOM   4413 O  O     . ASN A 1 565 ? -17.394 10.320  31.520  1.00 31.79  ? 565  ASN A O     1 
ATOM   4414 C  CB    . ASN A 1 565 ? -19.790 11.638  30.615  1.00 32.13  ? 565  ASN A CB    1 
ATOM   4415 C  CG    . ASN A 1 565 ? -20.812 10.751  31.327  1.00 43.06  ? 565  ASN A CG    1 
ATOM   4416 O  OD1   . ASN A 1 565 ? -20.608 10.282  32.449  1.00 42.83  ? 565  ASN A OD1   1 
ATOM   4417 N  ND2   . ASN A 1 565 ? -21.924 10.498  30.642  1.00 42.83  ? 565  ASN A ND2   1 
ATOM   4418 N  N     . LEU A 1 566 ? -17.521 11.464  33.453  1.00 26.85  ? 566  LEU A N     1 
ATOM   4419 C  CA    . LEU A 1 566 ? -16.693 10.536  34.210  1.00 36.74  ? 566  LEU A CA    1 
ATOM   4420 C  C     . LEU A 1 566 ? -17.505 9.678   35.187  1.00 44.99  ? 566  LEU A C     1 
ATOM   4421 O  O     . LEU A 1 566 ? -16.929 9.077   36.099  1.00 49.23  ? 566  LEU A O     1 
ATOM   4422 C  CB    . LEU A 1 566 ? -15.608 11.300  34.962  1.00 31.34  ? 566  LEU A CB    1 
ATOM   4423 C  CG    . LEU A 1 566 ? -14.652 12.076  34.070  1.00 40.30  ? 566  LEU A CG    1 
ATOM   4424 C  CD1   . LEU A 1 566 ? -13.534 12.679  34.897  1.00 41.75  ? 566  LEU A CD1   1 
ATOM   4425 C  CD2   . LEU A 1 566 ? -14.096 11.162  32.999  1.00 36.85  ? 566  LEU A CD2   1 
ATOM   4426 N  N     . LYS A 1 567 ? -18.826 9.603   35.016  1.00 46.41  ? 567  LYS A N     1 
ATOM   4427 C  CA    . LYS A 1 567 ? -19.663 8.829   35.931  1.00 49.44  ? 567  LYS A CA    1 
ATOM   4428 C  C     . LYS A 1 567 ? -19.330 7.347   35.817  1.00 54.61  ? 567  LYS A C     1 
ATOM   4429 O  O     . LYS A 1 567 ? -19.422 6.761   34.730  1.00 44.76  ? 567  LYS A O     1 
ATOM   4430 C  CB    . LYS A 1 567 ? -21.140 9.073   35.640  1.00 47.66  ? 567  LYS A CB    1 
ATOM   4431 C  CG    . LYS A 1 567 ? -21.506 10.559  35.633  1.00 63.79  ? 567  LYS A CG    1 
ATOM   4432 C  CD    . LYS A 1 567 ? -22.959 10.799  35.253  1.00 70.80  ? 567  LYS A CD    1 
ATOM   4433 C  CE    . LYS A 1 567 ? -23.248 12.286  35.105  1.00 67.50  ? 567  LYS A CE    1 
ATOM   4434 N  NZ    . LYS A 1 567 ? -24.709 12.547  34.965  1.00 69.62  ? 567  LYS A NZ    1 
ATOM   4435 N  N     . GLY A 1 568 ? -18.952 6.744   36.941  1.00 53.41  ? 568  GLY A N     1 
ATOM   4436 C  CA    . GLY A 1 568 ? -18.529 5.362   36.959  1.00 53.97  ? 568  GLY A CA    1 
ATOM   4437 C  C     . GLY A 1 568 ? -17.101 5.261   37.445  1.00 59.80  ? 568  GLY A C     1 
ATOM   4438 O  O     . GLY A 1 568 ? -16.833 4.732   38.527  1.00 65.64  ? 568  GLY A O     1 
ATOM   4439 N  N     . LEU A 1 569 ? -16.171 5.783   36.648  1.00 58.83  ? 569  LEU A N     1 
ATOM   4440 C  CA    . LEU A 1 569 ? -14.765 5.875   37.039  1.00 61.65  ? 569  LEU A CA    1 
ATOM   4441 C  C     . LEU A 1 569 ? -14.575 7.173   37.826  1.00 73.50  ? 569  LEU A C     1 
ATOM   4442 O  O     . LEU A 1 569 ? -14.090 8.185   37.313  1.00 71.76  ? 569  LEU A O     1 
ATOM   4443 C  CB    . LEU A 1 569 ? -13.858 5.823   35.811  1.00 56.56  ? 569  LEU A CB    1 
ATOM   4444 C  CG    . LEU A 1 569 ? -14.499 5.936   34.419  1.00 44.27  ? 569  LEU A CG    1 
ATOM   4445 C  CD1   . LEU A 1 569 ? -13.704 6.793   33.436  1.00 33.48  ? 569  LEU A CD1   1 
ATOM   4446 C  CD2   . LEU A 1 569 ? -14.665 4.552   33.849  1.00 39.26  ? 569  LEU A CD2   1 
ATOM   4447 N  N     . GLY A 1 570 ? -14.980 7.145   39.101  1.00 70.52  ? 570  GLY A N     1 
ATOM   4448 C  CA    . GLY A 1 570 ? -14.768 8.303   39.956  1.00 67.11  ? 570  GLY A CA    1 
ATOM   4449 C  C     . GLY A 1 570 ? -13.349 8.479   40.443  1.00 66.33  ? 570  GLY A C     1 
ATOM   4450 O  O     . GLY A 1 570 ? -13.019 9.492   41.072  1.00 64.83  ? 570  GLY A O     1 
ATOM   4451 N  N     . ASP A 1 571 ? -12.493 7.509   40.129  1.00 68.86  ? 571  ASP A N     1 
ATOM   4452 C  CA    . ASP A 1 571 ? -11.110 7.426   40.577  1.00 66.83  ? 571  ASP A CA    1 
ATOM   4453 C  C     . ASP A 1 571 ? -10.126 8.223   39.724  1.00 61.50  ? 571  ASP A C     1 
ATOM   4454 O  O     . ASP A 1 571 ? -8.958  8.337   40.111  1.00 64.26  ? 571  ASP A O     1 
ATOM   4455 C  CB    . ASP A 1 571 ? -10.685 5.955   40.583  1.00 67.60  ? 571  ASP A CB    1 
ATOM   4456 C  CG    . ASP A 1 571 ? -11.177 5.208   39.352  1.00 69.57  ? 571  ASP A CG    1 
ATOM   4457 O  OD1   . ASP A 1 571 ? -12.406 5.219   39.100  1.00 63.47  ? 571  ASP A OD1   1 
ATOM   4458 O  OD2   . ASP A 1 571 ? -10.338 4.634   38.620  1.00 77.80  ? 571  ASP A OD2   1 
ATOM   4459 N  N     . VAL A 1 572 ? -10.563 8.779   38.591  1.00 63.42  ? 572  VAL A N     1 
ATOM   4460 C  CA    . VAL A 1 572 ? -9.641  9.274   37.568  1.00 53.09  ? 572  VAL A CA    1 
ATOM   4461 C  C     . VAL A 1 572 ? -8.957  10.554  38.027  1.00 58.29  ? 572  VAL A C     1 
ATOM   4462 O  O     . VAL A 1 572 ? -9.606  11.487  38.524  1.00 47.91  ? 572  VAL A O     1 
ATOM   4463 C  CB    . VAL A 1 572 ? -10.383 9.510   36.248  1.00 51.26  ? 572  VAL A CB    1 
ATOM   4464 C  CG1   . VAL A 1 572 ? -9.408  9.969   35.178  1.00 51.03  ? 572  VAL A CG1   1 
ATOM   4465 C  CG2   . VAL A 1 572 ? -11.099 8.251   35.816  1.00 56.00  ? 572  VAL A CG2   1 
ATOM   4466 N  N     . ASN A 1 573 ? -7.646  10.625  37.802  1.00 52.18  ? 573  ASN A N     1 
ATOM   4467 C  CA    . ASN A 1 573 ? -6.828  11.780  38.175  1.00 49.45  ? 573  ASN A CA    1 
ATOM   4468 C  C     . ASN A 1 573 ? -6.888  12.805  37.049  1.00 50.69  ? 573  ASN A C     1 
ATOM   4469 O  O     . ASN A 1 573 ? -6.046  12.837  36.145  1.00 44.11  ? 573  ASN A O     1 
ATOM   4470 C  CB    . ASN A 1 573 ? -5.400  11.343  38.469  1.00 49.42  ? 573  ASN A CB    1 
ATOM   4471 C  CG    . ASN A 1 573 ? -4.554  12.464  39.024  1.00 57.81  ? 573  ASN A CG    1 
ATOM   4472 O  OD1   . ASN A 1 573 ? -5.047  13.571  39.265  1.00 58.07  ? 573  ASN A OD1   1 
ATOM   4473 N  ND2   . ASN A 1 573 ? -3.265  12.182  39.243  1.00 56.81  ? 573  ASN A ND2   1 
ATOM   4474 N  N     . VAL A 1 574 ? -7.902  13.662  37.117  1.00 47.72  ? 574  VAL A N     1 
ATOM   4475 C  CA    . VAL A 1 574 ? -8.173  14.591  36.030  1.00 49.84  ? 574  VAL A CA    1 
ATOM   4476 C  C     . VAL A 1 574 ? -7.066  15.629  35.914  1.00 44.01  ? 574  VAL A C     1 
ATOM   4477 O  O     . VAL A 1 574 ? -6.673  16.015  34.807  1.00 42.77  ? 574  VAL A O     1 
ATOM   4478 C  CB    . VAL A 1 574 ? -9.549  15.237  36.245  1.00 52.23  ? 574  VAL A CB    1 
ATOM   4479 C  CG1   . VAL A 1 574 ? -10.625 14.262  35.850  1.00 50.27  ? 574  VAL A CG1   1 
ATOM   4480 C  CG2   . VAL A 1 574 ? -9.712  15.643  37.716  1.00 57.29  ? 574  VAL A CG2   1 
ATOM   4481 N  N     . GLU A 1 575 ? -6.536  16.087  37.052  1.00 54.71  ? 575  GLU A N     1 
ATOM   4482 C  CA    . GLU A 1 575 ? -5.477  17.090  37.027  1.00 54.73  ? 575  GLU A CA    1 
ATOM   4483 C  C     . GLU A 1 575 ? -4.290  16.600  36.212  1.00 45.07  ? 575  GLU A C     1 
ATOM   4484 O  O     . GLU A 1 575 ? -3.792  17.313  35.329  1.00 39.26  ? 575  GLU A O     1 
ATOM   4485 C  CB    . GLU A 1 575 ? -5.047  17.440  38.454  1.00 56.60  ? 575  GLU A CB    1 
ATOM   4486 C  CG    . GLU A 1 575 ? -6.077  18.239  39.242  1.00 68.27  ? 575  GLU A CG    1 
ATOM   4487 C  CD    . GLU A 1 575 ? -6.033  19.730  38.929  1.00 85.66  ? 575  GLU A CD    1 
ATOM   4488 O  OE1   . GLU A 1 575 ? -5.282  20.138  38.010  1.00 85.19  ? 575  GLU A OE1   1 
ATOM   4489 O  OE2   . GLU A 1 575 ? -6.747  20.499  39.613  1.00 92.84  ? 575  GLU A OE2   1 
ATOM   4490 N  N     . GLU A 1 576 ? -3.838  15.370  36.483  1.00 39.57  ? 576  GLU A N     1 
ATOM   4491 C  CA    . GLU A 1 576 ? -2.674  14.818  35.794  1.00 45.63  ? 576  GLU A CA    1 
ATOM   4492 C  C     . GLU A 1 576 ? -3.000  14.414  34.359  1.00 40.23  ? 576  GLU A C     1 
ATOM   4493 O  O     . GLU A 1 576 ? -2.136  14.518  33.480  1.00 41.53  ? 576  GLU A O     1 
ATOM   4494 C  CB    . GLU A 1 576 ? -2.118  13.621  36.575  1.00 45.70  ? 576  GLU A CB    1 
ATOM   4495 C  CG    . GLU A 1 576 ? -0.653  13.290  36.286  1.00 55.40  ? 576  GLU A CG    1 
ATOM   4496 C  CD    . GLU A 1 576 ? -0.041  12.325  37.308  1.00 64.06  ? 576  GLU A CD    1 
ATOM   4497 O  OE1   . GLU A 1 576 ? -0.752  11.910  38.258  1.00 66.13  ? 576  GLU A OE1   1 
ATOM   4498 O  OE2   . GLU A 1 576 ? 1.157   11.984  37.161  1.00 61.92  ? 576  GLU A OE2   1 
ATOM   4499 N  N     . LEU A 1 577 ? -4.236  13.977  34.104  1.00 38.63  ? 577  LEU A N     1 
ATOM   4500 C  CA    . LEU A 1 577 ? -4.616  13.559  32.759  1.00 37.08  ? 577  LEU A CA    1 
ATOM   4501 C  C     . LEU A 1 577 ? -4.609  14.728  31.786  1.00 32.79  ? 577  LEU A C     1 
ATOM   4502 O  O     . LEU A 1 577 ? -4.286  14.547  30.606  1.00 28.82  ? 577  LEU A O     1 
ATOM   4503 C  CB    . LEU A 1 577 ? -5.996  12.904  32.763  1.00 33.12  ? 577  LEU A CB    1 
ATOM   4504 C  CG    . LEU A 1 577 ? -6.102  11.441  32.336  1.00 32.51  ? 577  LEU A CG    1 
ATOM   4505 C  CD1   . LEU A 1 577 ? -7.558  11.036  32.186  1.00 35.88  ? 577  LEU A CD1   1 
ATOM   4506 C  CD2   . LEU A 1 577 ? -5.281  11.116  31.063  1.00 32.40  ? 577  LEU A CD2   1 
ATOM   4507 N  N     . PHE A 1 578 ? -4.996  15.926  32.244  1.00 29.19  ? 578  PHE A N     1 
ATOM   4508 C  CA    . PHE A 1 578 ? -5.010  17.116  31.399  1.00 28.16  ? 578  PHE A CA    1 
ATOM   4509 C  C     . PHE A 1 578 ? -3.986  18.153  31.809  1.00 31.13  ? 578  PHE A C     1 
ATOM   4510 O  O     . PHE A 1 578 ? -4.049  19.284  31.326  1.00 36.47  ? 578  PHE A O     1 
ATOM   4511 C  CB    . PHE A 1 578 ? -6.393  17.755  31.375  1.00 32.94  ? 578  PHE A CB    1 
ATOM   4512 C  CG    . PHE A 1 578 ? -7.397  16.989  30.577  1.00 31.87  ? 578  PHE A CG    1 
ATOM   4513 C  CD1   . PHE A 1 578 ? -7.491  17.173  29.201  1.00 28.68  ? 578  PHE A CD1   1 
ATOM   4514 C  CD2   . PHE A 1 578 ? -8.256  16.090  31.200  1.00 32.73  ? 578  PHE A CD2   1 
ATOM   4515 C  CE1   . PHE A 1 578 ? -8.419  16.480  28.457  1.00 26.26  ? 578  PHE A CE1   1 
ATOM   4516 C  CE2   . PHE A 1 578 ? -9.198  15.382  30.476  1.00 30.37  ? 578  PHE A CE2   1 
ATOM   4517 C  CZ    . PHE A 1 578 ? -9.290  15.571  29.101  1.00 27.48  ? 578  PHE A CZ    1 
ATOM   4518 N  N     . GLY A 1 579 ? -3.027  17.796  32.653  1.00 31.42  ? 579  GLY A N     1 
ATOM   4519 C  CA    . GLY A 1 579 ? -1.983  18.743  32.996  1.00 32.00  ? 579  GLY A CA    1 
ATOM   4520 C  C     . GLY A 1 579 ? -1.136  19.101  31.784  1.00 34.22  ? 579  GLY A C     1 
ATOM   4521 O  O     . GLY A 1 579 ? -0.832  18.258  30.935  1.00 33.03  ? 579  GLY A O     1 
ATOM   4522 N  N     . ILE A 1 580 ? -0.745  20.369  31.716  1.00 31.78  ? 580  ILE A N     1 
ATOM   4523 C  CA    . ILE A 1 580 ? 0.070   20.907  30.630  1.00 32.82  ? 580  ILE A CA    1 
ATOM   4524 C  C     . ILE A 1 580 ? 1.222   21.661  31.271  1.00 33.10  ? 580  ILE A C     1 
ATOM   4525 O  O     . ILE A 1 580 ? 1.003   22.642  31.992  1.00 34.62  ? 580  ILE A O     1 
ATOM   4526 C  CB    . ILE A 1 580 ? -0.755  21.817  29.708  1.00 32.42  ? 580  ILE A CB    1 
ATOM   4527 C  CG1   . ILE A 1 580 ? -1.801  20.970  28.969  1.00 30.91  ? 580  ILE A CG1   1 
ATOM   4528 C  CG2   . ILE A 1 580 ? 0.150   22.596  28.741  1.00 36.61  ? 580  ILE A CG2   1 
ATOM   4529 C  CD1   . ILE A 1 580 ? -2.913  21.793  28.336  1.00 32.93  ? 580  ILE A CD1   1 
ATOM   4530 N  N     . SER A 1 581 ? 2.434   21.186  31.055  1.00 28.89  ? 581  SER A N     1 
ATOM   4531 C  CA    . SER A 1 581 ? 3.598   21.727  31.735  1.00 32.27  ? 581  SER A CA    1 
ATOM   4532 C  C     . SER A 1 581 ? 4.422   22.545  30.756  1.00 35.71  ? 581  SER A C     1 
ATOM   4533 O  O     . SER A 1 581 ? 4.780   22.053  29.681  1.00 28.38  ? 581  SER A O     1 
ATOM   4534 C  CB    . SER A 1 581 ? 4.432   20.600  32.335  1.00 36.68  ? 581  SER A CB    1 
ATOM   4535 O  OG    . SER A 1 581 ? 5.799   20.949  32.356  1.00 44.42  ? 581  SER A OG    1 
ATOM   4536 N  N     . LYS A 1 582 ? 4.710   23.799  31.126  1.00 31.56  ? 582  LYS A N     1 
ATOM   4537 C  CA    . LYS A 1 582 ? 5.545   24.641  30.277  1.00 31.32  ? 582  LYS A CA    1 
ATOM   4538 C  C     . LYS A 1 582 ? 6.864   23.954  29.957  1.00 32.76  ? 582  LYS A C     1 
ATOM   4539 O  O     . LYS A 1 582 ? 7.356   24.027  28.825  1.00 33.66  ? 582  LYS A O     1 
ATOM   4540 C  CB    . LYS A 1 582 ? 5.798   25.984  30.962  1.00 30.85  ? 582  LYS A CB    1 
ATOM   4541 C  CG    . LYS A 1 582 ? 6.675   26.921  30.159  1.00 31.72  ? 582  LYS A CG    1 
ATOM   4542 C  CD    . LYS A 1 582 ? 6.790   28.292  30.819  1.00 33.60  ? 582  LYS A CD    1 
ATOM   4543 C  CE    . LYS A 1 582 ? 7.647   29.242  29.963  1.00 38.41  ? 582  LYS A CE    1 
ATOM   4544 N  NZ    . LYS A 1 582 ? 7.758   30.565  30.614  1.00 47.13  ? 582  LYS A NZ    1 
ATOM   4545 N  N     . GLU A 1 583 ? 7.445   23.272  30.947  1.00 34.77  ? 583  GLU A N     1 
ATOM   4546 C  CA    . GLU A 1 583 ? 8.754   22.668  30.769  1.00 28.84  ? 583  GLU A CA    1 
ATOM   4547 C  C     . GLU A 1 583 ? 8.687   21.543  29.751  1.00 31.47  ? 583  GLU A C     1 
ATOM   4548 O  O     . GLU A 1 583 ? 9.571   21.412  28.899  1.00 32.13  ? 583  GLU A O     1 
ATOM   4549 C  CB    . GLU A 1 583 ? 9.281   22.147  32.112  1.00 36.70  ? 583  GLU A CB    1 
ATOM   4550 C  CG    . GLU A 1 583 ? 9.535   23.221  33.164  1.00 46.07  ? 583  GLU A CG    1 
ATOM   4551 C  CD    . GLU A 1 583 ? 8.253   23.783  33.784  1.00 58.77  ? 583  GLU A CD    1 
ATOM   4552 O  OE1   . GLU A 1 583 ? 7.297   23.002  34.042  1.00 54.18  ? 583  GLU A OE1   1 
ATOM   4553 O  OE2   . GLU A 1 583 ? 8.202   25.019  34.005  1.00 70.85  ? 583  GLU A OE2   1 
ATOM   4554 N  N     . PHE A 1 584 ? 7.640   20.727  29.817  1.00 30.43  ? 584  PHE A N     1 
ATOM   4555 C  CA    . PHE A 1 584 ? 7.502   19.662  28.834  1.00 30.74  ? 584  PHE A CA    1 
ATOM   4556 C  C     . PHE A 1 584 ? 7.319   20.228  27.428  1.00 27.70  ? 584  PHE A C     1 
ATOM   4557 O  O     . PHE A 1 584 ? 7.936   19.751  26.470  1.00 22.62  ? 584  PHE A O     1 
ATOM   4558 C  CB    . PHE A 1 584 ? 6.330   18.761  29.182  1.00 28.34  ? 584  PHE A CB    1 
ATOM   4559 C  CG    . PHE A 1 584 ? 6.075   17.708  28.140  1.00 27.31  ? 584  PHE A CG    1 
ATOM   4560 C  CD1   . PHE A 1 584 ? 6.792   16.530  28.148  1.00 30.02  ? 584  PHE A CD1   1 
ATOM   4561 C  CD2   . PHE A 1 584 ? 5.135   17.911  27.147  1.00 24.38  ? 584  PHE A CD2   1 
ATOM   4562 C  CE1   . PHE A 1 584 ? 6.567   15.564  27.183  1.00 29.07  ? 584  PHE A CE1   1 
ATOM   4563 C  CE2   . PHE A 1 584 ? 4.908   16.953  26.184  1.00 26.42  ? 584  PHE A CE2   1 
ATOM   4564 C  CZ    . PHE A 1 584 ? 5.619   15.781  26.209  1.00 24.53  ? 584  PHE A CZ    1 
ATOM   4565 N  N     . TRP A 1 585 ? 6.425   21.208  27.279  1.00 26.97  ? 585  TRP A N     1 
ATOM   4566 C  CA    . TRP A 1 585 ? 6.073   21.682  25.947  1.00 26.19  ? 585  TRP A CA    1 
ATOM   4567 C  C     . TRP A 1 585 ? 7.166   22.551  25.318  1.00 28.02  ? 585  TRP A C     1 
ATOM   4568 O  O     . TRP A 1 585 ? 7.296   22.568  24.080  1.00 26.81  ? 585  TRP A O     1 
ATOM   4569 C  CB    . TRP A 1 585 ? 4.707   22.391  26.018  1.00 25.61  ? 585  TRP A CB    1 
ATOM   4570 C  CG    . TRP A 1 585 ? 3.605   21.366  25.996  1.00 27.60  ? 585  TRP A CG    1 
ATOM   4571 C  CD1   . TRP A 1 585 ? 2.927   20.835  27.069  1.00 28.82  ? 585  TRP A CD1   1 
ATOM   4572 C  CD2   . TRP A 1 585 ? 3.118   20.683  24.835  1.00 27.44  ? 585  TRP A CD2   1 
ATOM   4573 N  NE1   . TRP A 1 585 ? 2.020   19.886  26.637  1.00 25.01  ? 585  TRP A NE1   1 
ATOM   4574 C  CE2   . TRP A 1 585 ? 2.128   19.759  25.275  1.00 25.34  ? 585  TRP A CE2   1 
ATOM   4575 C  CE3   . TRP A 1 585 ? 3.420   20.765  23.461  1.00 23.89  ? 585  TRP A CE3   1 
ATOM   4576 C  CZ2   . TRP A 1 585 ? 1.436   18.927  24.391  1.00 24.73  ? 585  TRP A CZ2   1 
ATOM   4577 C  CZ3   . TRP A 1 585 ? 2.720   19.957  22.580  1.00 24.38  ? 585  TRP A CZ3   1 
ATOM   4578 C  CH2   . TRP A 1 585 ? 1.745   19.028  23.058  1.00 26.73  ? 585  TRP A CH2   1 
ATOM   4579 N  N     . GLU A 1 586 ? 7.987   23.233  26.128  1.00 28.12  ? 586  GLU A N     1 
ATOM   4580 C  CA    . GLU A 1 586 ? 9.174   23.902  25.583  1.00 30.93  ? 586  GLU A CA    1 
ATOM   4581 C  C     . GLU A 1 586 ? 10.119  22.907  24.922  1.00 33.84  ? 586  GLU A C     1 
ATOM   4582 O  O     . GLU A 1 586 ? 10.670  23.175  23.837  1.00 27.72  ? 586  GLU A O     1 
ATOM   4583 C  CB    . GLU A 1 586 ? 9.918   24.651  26.690  1.00 31.22  ? 586  GLU A CB    1 
ATOM   4584 C  CG    . GLU A 1 586 ? 9.249   25.919  27.098  1.00 30.76  ? 586  GLU A CG    1 
ATOM   4585 C  CD    . GLU A 1 586 ? 10.053  26.678  28.140  1.00 44.75  ? 586  GLU A CD    1 
ATOM   4586 O  OE1   . GLU A 1 586 ? 10.703  26.033  28.992  1.00 46.42  ? 586  GLU A OE1   1 
ATOM   4587 O  OE2   . GLU A 1 586 ? 10.034  27.919  28.104  1.00 49.56  ? 586  GLU A OE2   1 
ATOM   4588 N  N     . LYS A 1 587 ? 10.347  21.761  25.581  1.00 26.70  ? 587  LYS A N     1 
ATOM   4589 C  CA    . LYS A 1 587 ? 11.163  20.718  24.967  1.00 24.47  ? 587  LYS A CA    1 
ATOM   4590 C  C     . LYS A 1 587 ? 10.464  20.152  23.741  1.00 23.23  ? 587  LYS A C     1 
ATOM   4591 O  O     . LYS A 1 587 ? 11.110  19.858  22.724  1.00 26.03  ? 587  LYS A O     1 
ATOM   4592 C  CB    . LYS A 1 587 ? 11.468  19.620  25.991  1.00 27.11  ? 587  LYS A CB    1 
ATOM   4593 C  CG    . LYS A 1 587 ? 12.161  18.364  25.411  1.00 30.66  ? 587  LYS A CG    1 
ATOM   4594 C  CD    . LYS A 1 587 ? 13.508  18.680  24.763  1.00 35.33  ? 587  LYS A CD    1 
ATOM   4595 C  CE    . LYS A 1 587 ? 14.189  17.401  24.254  1.00 41.41  ? 587  LYS A CE    1 
ATOM   4596 N  NZ    . LYS A 1 587 ? 15.548  17.651  23.657  1.00 43.08  ? 587  LYS A NZ    1 
ATOM   4597 N  N     . GLU A 1 588 ? 9.136   20.007  23.812  1.00 26.01  ? 588  GLU A N     1 
ATOM   4598 C  CA    . GLU A 1 588 ? 8.406   19.378  22.713  1.00 27.53  ? 588  GLU A CA    1 
ATOM   4599 C  C     . GLU A 1 588 ? 8.484   20.214  21.434  1.00 23.62  ? 588  GLU A C     1 
ATOM   4600 O  O     . GLU A 1 588 ? 8.760   19.677  20.363  1.00 20.58  ? 588  GLU A O     1 
ATOM   4601 C  CB    . GLU A 1 588 ? 6.954   19.131  23.109  1.00 21.89  ? 588  GLU A CB    1 
ATOM   4602 C  CG    . GLU A 1 588 ? 6.188   18.219  22.148  1.00 24.24  ? 588  GLU A CG    1 
ATOM   4603 C  CD    . GLU A 1 588 ? 6.667   16.772  22.152  1.00 29.11  ? 588  GLU A CD    1 
ATOM   4604 O  OE1   . GLU A 1 588 ? 7.318   16.336  23.142  1.00 26.85  ? 588  GLU A OE1   1 
ATOM   4605 O  OE2   . GLU A 1 588 ? 6.402   16.057  21.148  1.00 21.90  ? 588  GLU A OE2   1 
ATOM   4606 N  N     . VAL A 1 589 ? 8.224   21.524  21.522  1.00 24.39  ? 589  VAL A N     1 
ATOM   4607 C  CA    . VAL A 1 589 ? 8.313   22.384  20.333  1.00 22.55  ? 589  VAL A CA    1 
ATOM   4608 C  C     . VAL A 1 589 ? 9.726   22.377  19.759  1.00 24.87  ? 589  VAL A C     1 
ATOM   4609 O  O     . VAL A 1 589 ? 9.916   22.398  18.542  1.00 24.21  ? 589  VAL A O     1 
ATOM   4610 C  CB    . VAL A 1 589 ? 7.848   23.822  20.646  1.00 31.05  ? 589  VAL A CB    1 
ATOM   4611 C  CG1   . VAL A 1 589 ? 6.378   23.861  20.854  1.00 28.43  ? 589  VAL A CG1   1 
ATOM   4612 C  CG2   . VAL A 1 589 ? 8.550   24.369  21.862  1.00 28.75  ? 589  VAL A CG2   1 
ATOM   4613 N  N     . GLU A 1 590 ? 10.742  22.359  20.621  1.00 24.94  ? 590  GLU A N     1 
ATOM   4614 C  CA    . GLU A 1 590 ? 12.110  22.287  20.128  1.00 22.71  ? 590  GLU A CA    1 
ATOM   4615 C  C     . GLU A 1 590 ? 12.339  21.027  19.291  1.00 31.28  ? 590  GLU A C     1 
ATOM   4616 O  O     . GLU A 1 590 ? 12.958  21.090  18.218  1.00 27.20  ? 590  GLU A O     1 
ATOM   4617 C  CB    . GLU A 1 590 ? 13.088  22.358  21.311  1.00 30.79  ? 590  GLU A CB    1 
ATOM   4618 C  CG    . GLU A 1 590 ? 14.570  22.356  20.926  1.00 43.58  ? 590  GLU A CG    1 
ATOM   4619 C  CD    . GLU A 1 590 ? 14.997  23.644  20.183  1.00 60.89  ? 590  GLU A CD    1 
ATOM   4620 O  OE1   . GLU A 1 590 ? 14.299  24.681  20.331  1.00 55.65  ? 590  GLU A OE1   1 
ATOM   4621 O  OE2   . GLU A 1 590 ? 16.023  23.610  19.450  1.00 60.94  ? 590  GLU A OE2   1 
ATOM   4622 N  N     . GLU A 1 591 ? 11.829  19.865  19.748  1.00 24.18  ? 591  GLU A N     1 
ATOM   4623 C  CA    . GLU A 1 591 ? 12.066  18.631  18.998  1.00 21.68  ? 591  GLU A CA    1 
ATOM   4624 C  C     . GLU A 1 591 ? 11.299  18.633  17.688  1.00 20.57  ? 591  GLU A C     1 
ATOM   4625 O  O     . GLU A 1 591 ? 11.785  18.117  16.676  1.00 19.50  ? 591  GLU A O     1 
ATOM   4626 C  CB    . GLU A 1 591 ? 11.675  17.389  19.822  1.00 23.78  ? 591  GLU A CB    1 
ATOM   4627 C  CG    . GLU A 1 591 ? 12.617  17.112  20.959  1.00 23.76  ? 591  GLU A CG    1 
ATOM   4628 C  CD    . GLU A 1 591 ? 14.065  16.953  20.496  1.00 29.69  ? 591  GLU A CD    1 
ATOM   4629 O  OE1   . GLU A 1 591 ? 14.329  16.197  19.512  1.00 27.60  ? 591  GLU A OE1   1 
ATOM   4630 O  OE2   . GLU A 1 591 ? 14.944  17.577  21.131  1.00 27.97  ? 591  GLU A OE2   1 
ATOM   4631 N  N     . ILE A 1 592 ? 10.090  19.192  17.694  1.00 18.92  ? 592  ILE A N     1 
ATOM   4632 C  CA    . ILE A 1 592 ? 9.332   19.316  16.453  1.00 18.40  ? 592  ILE A CA    1 
ATOM   4633 C  C     . ILE A 1 592 ? 10.058  20.252  15.487  1.00 22.72  ? 592  ILE A C     1 
ATOM   4634 O  O     . ILE A 1 592 ? 10.169  19.984  14.290  1.00 22.84  ? 592  ILE A O     1 
ATOM   4635 C  CB    . ILE A 1 592 ? 7.919   19.840  16.751  1.00 18.44  ? 592  ILE A CB    1 
ATOM   4636 C  CG1   . ILE A 1 592 ? 7.151   18.864  17.676  1.00 20.96  ? 592  ILE A CG1   1 
ATOM   4637 C  CG2   . ILE A 1 592 ? 7.174   20.109  15.457  1.00 22.98  ? 592  ILE A CG2   1 
ATOM   4638 C  CD1   . ILE A 1 592 ? 5.969   19.522  18.414  1.00 22.02  ? 592  ILE A CD1   1 
ATOM   4639 N  N     . ASP A 1 593 ? 10.546  21.370  16.001  1.00 18.83  ? 593  ASP A N     1 
ATOM   4640 C  CA    . ASP A 1 593 ? 11.254  22.332  15.151  1.00 19.94  ? 593  ASP A CA    1 
ATOM   4641 C  C     . ASP A 1 593 ? 12.465  21.683  14.482  1.00 24.27  ? 593  ASP A C     1 
ATOM   4642 O  O     . ASP A 1 593 ? 12.622  21.738  13.260  1.00 22.58  ? 593  ASP A O     1 
ATOM   4643 C  CB    . ASP A 1 593 ? 11.646  23.508  16.032  1.00 22.30  ? 593  ASP A CB    1 
ATOM   4644 C  CG    . ASP A 1 593 ? 12.332  24.636  15.264  1.00 36.45  ? 593  ASP A CG    1 
ATOM   4645 O  OD1   . ASP A 1 593 ? 12.094  24.808  14.058  1.00 33.04  ? 593  ASP A OD1   1 
ATOM   4646 O  OD2   . ASP A 1 593 ? 13.134  25.323  15.904  1.00 42.22  ? 593  ASP A OD2   1 
ATOM   4647 N  N     . LYS A 1 594 ? 13.320  21.029  15.275  1.00 19.68  ? 594  LYS A N     1 
ATOM   4648 C  CA    . LYS A 1 594 ? 14.493  20.355  14.734  1.00 23.70  ? 594  LYS A CA    1 
ATOM   4649 C  C     . LYS A 1 594 ? 14.114  19.315  13.693  1.00 23.67  ? 594  LYS A C     1 
ATOM   4650 O  O     . LYS A 1 594 ? 14.795  19.162  12.670  1.00 23.05  ? 594  LYS A O     1 
ATOM   4651 C  CB    . LYS A 1 594 ? 15.275  19.706  15.875  1.00 23.62  ? 594  LYS A CB    1 
ATOM   4652 C  CG    . LYS A 1 594 ? 15.875  20.724  16.823  1.00 28.90  ? 594  LYS A CG    1 
ATOM   4653 C  CD    . LYS A 1 594 ? 16.876  20.061  17.771  1.00 34.24  ? 594  LYS A CD    1 
ATOM   4654 C  CE    . LYS A 1 594 ? 16.221  18.994  18.639  1.00 26.54  ? 594  LYS A CE    1 
ATOM   4655 N  NZ    . LYS A 1 594 ? 17.042  18.784  19.890  1.00 30.95  ? 594  LYS A NZ    1 
ATOM   4656 N  N     . TYR A 1 595 ? 13.039  18.571  13.944  1.00 21.50  ? 595  TYR A N     1 
ATOM   4657 C  CA    . TYR A 1 595 ? 12.643  17.521  13.019  1.00 20.70  ? 595  TYR A CA    1 
ATOM   4658 C  C     . TYR A 1 595 ? 12.135  18.106  11.705  1.00 22.51  ? 595  TYR A C     1 
ATOM   4659 O  O     . TYR A 1 595 ? 12.607  17.743  10.622  1.00 21.20  ? 595  TYR A O     1 
ATOM   4660 C  CB    . TYR A 1 595 ? 11.581  16.650  13.708  1.00 21.43  ? 595  TYR A CB    1 
ATOM   4661 C  CG    . TYR A 1 595 ? 10.938  15.650  12.809  1.00 20.07  ? 595  TYR A CG    1 
ATOM   4662 C  CD1   . TYR A 1 595 ? 11.541  14.415  12.560  1.00 20.79  ? 595  TYR A CD1   1 
ATOM   4663 C  CD2   . TYR A 1 595 ? 9.704   15.919  12.228  1.00 26.36  ? 595  TYR A CD2   1 
ATOM   4664 C  CE1   . TYR A 1 595 ? 10.932  13.470  11.749  1.00 26.22  ? 595  TYR A CE1   1 
ATOM   4665 C  CE2   . TYR A 1 595 ? 9.089   14.984  11.419  1.00 24.75  ? 595  TYR A CE2   1 
ATOM   4666 C  CZ    . TYR A 1 595 ? 9.708   13.770  11.180  1.00 25.27  ? 595  TYR A CZ    1 
ATOM   4667 O  OH    . TYR A 1 595 ? 9.085   12.846  10.371  1.00 28.02  ? 595  TYR A OH    1 
ATOM   4668 N  N     . LEU A 1 596 ? 11.197  19.048  11.781  1.00 19.57  ? 596  LEU A N     1 
ATOM   4669 C  CA    . LEU A 1 596 ? 10.682  19.682  10.567  1.00 22.96  ? 596  LEU A CA    1 
ATOM   4670 C  C     . LEU A 1 596 ? 11.785  20.398  9.775   1.00 23.33  ? 596  LEU A C     1 
ATOM   4671 O  O     . LEU A 1 596 ? 11.821  20.320  8.542   1.00 23.36  ? 596  LEU A O     1 
ATOM   4672 C  CB    . LEU A 1 596 ? 9.571   20.666  10.916  1.00 20.92  ? 596  LEU A CB    1 
ATOM   4673 C  CG    . LEU A 1 596 ? 8.291   20.058  11.506  1.00 25.05  ? 596  LEU A CG    1 
ATOM   4674 C  CD1   . LEU A 1 596 ? 7.302   21.161  11.906  1.00 28.21  ? 596  LEU A CD1   1 
ATOM   4675 C  CD2   . LEU A 1 596 ? 7.681   19.130  10.480  1.00 27.64  ? 596  LEU A CD2   1 
ATOM   4676 N  N     . GLU A 1 597 ? 12.700  21.086  10.459  1.00 21.52  ? 597  GLU A N     1 
ATOM   4677 C  CA    . GLU A 1 597 ? 13.772  21.777  9.734   1.00 24.67  ? 597  GLU A CA    1 
ATOM   4678 C  C     . GLU A 1 597 ? 14.665  20.797  8.983   1.00 25.26  ? 597  GLU A C     1 
ATOM   4679 O  O     . GLU A 1 597 ? 15.004  21.016  7.811   1.00 22.81  ? 597  GLU A O     1 
ATOM   4680 C  CB    . GLU A 1 597 ? 14.618  22.613  10.694  1.00 28.44  ? 597  GLU A CB    1 
ATOM   4681 C  CG    . GLU A 1 597 ? 15.772  23.296  9.990   1.00 29.62  ? 597  GLU A CG    1 
ATOM   4682 C  CD    . GLU A 1 597 ? 16.824  23.829  10.936  1.00 42.23  ? 597  GLU A CD    1 
ATOM   4683 O  OE1   . GLU A 1 597 ? 16.848  23.404  12.110  1.00 43.51  ? 597  GLU A OE1   1 
ATOM   4684 O  OE2   . GLU A 1 597 ? 17.637  24.669  10.497  1.00 49.75  ? 597  GLU A OE2   1 
ATOM   4685 N  N     . ASP A 1 598 ? 15.099  19.726  9.653   1.00 23.55  ? 598  ASP A N     1 
ATOM   4686 C  CA    . ASP A 1 598 ? 15.979  18.772  8.977   1.00 22.45  ? 598  ASP A CA    1 
ATOM   4687 C  C     . ASP A 1 598 ? 15.220  17.995  7.914   1.00 23.46  ? 598  ASP A C     1 
ATOM   4688 O  O     . ASP A 1 598 ? 15.639  17.940  6.749   1.00 22.96  ? 598  ASP A O     1 
ATOM   4689 C  CB    . ASP A 1 598 ? 16.612  17.818  9.989   1.00 24.00  ? 598  ASP A CB    1 
ATOM   4690 C  CG    . ASP A 1 598 ? 17.523  16.780  9.320   1.00 31.18  ? 598  ASP A CG    1 
ATOM   4691 O  OD1   . ASP A 1 598 ? 18.270  17.138  8.382   1.00 28.83  ? 598  ASP A OD1   1 
ATOM   4692 O  OD2   . ASP A 1 598 ? 17.474  15.607  9.726   1.00 30.74  ? 598  ASP A OD2   1 
ATOM   4693 N  N     . GLN A 1 599 ? 14.069  17.423  8.288   1.00 20.96  ? 599  GLN A N     1 
ATOM   4694 C  CA    . GLN A 1 599 ? 13.473  16.388  7.462   1.00 21.72  ? 599  GLN A CA    1 
ATOM   4695 C  C     . GLN A 1 599 ? 12.607  16.946  6.354   1.00 20.00  ? 599  GLN A C     1 
ATOM   4696 O  O     . GLN A 1 599 ? 12.426  16.275  5.332   1.00 23.74  ? 599  GLN A O     1 
ATOM   4697 C  CB    . GLN A 1 599 ? 12.653  15.433  8.333   1.00 20.97  ? 599  GLN A CB    1 
ATOM   4698 C  CG    . GLN A 1 599 ? 13.530  14.633  9.266   1.00 21.92  ? 599  GLN A CG    1 
ATOM   4699 C  CD    . GLN A 1 599 ? 14.263  13.558  8.535   1.00 22.68  ? 599  GLN A CD    1 
ATOM   4700 O  OE1   . GLN A 1 599 ? 13.659  12.794  7.780   1.00 23.35  ? 599  GLN A OE1   1 
ATOM   4701 N  NE2   . GLN A 1 599 ? 15.570  13.485  8.739   1.00 24.42  ? 599  GLN A NE2   1 
ATOM   4702 N  N     . VAL A 1 600 ? 12.058  18.146  6.509   1.00 22.50  ? 600  VAL A N     1 
ATOM   4703 C  CA    . VAL A 1 600 ? 11.243  18.721  5.451   1.00 17.19  ? 600  VAL A CA    1 
ATOM   4704 C  C     . VAL A 1 600 ? 11.926  19.912  4.780   1.00 21.33  ? 600  VAL A C     1 
ATOM   4705 O  O     . VAL A 1 600 ? 11.743  20.111  3.574   1.00 22.84  ? 600  VAL A O     1 
ATOM   4706 C  CB    . VAL A 1 600 ? 9.837   19.104  5.953   1.00 17.68  ? 600  VAL A CB    1 
ATOM   4707 C  CG1   . VAL A 1 600 ? 8.899   19.292  4.781   1.00 19.18  ? 600  VAL A CG1   1 
ATOM   4708 C  CG2   . VAL A 1 600 ? 9.266   17.966  6.880   1.00 21.67  ? 600  VAL A CG2   1 
ATOM   4709 N  N     . ASN A 1 601 ? 12.719  20.682  5.513   1.00 19.88  ? 601  ASN A N     1 
ATOM   4710 C  CA    . ASN A 1 601 ? 13.687  21.599  4.907   1.00 22.10  ? 601  ASN A CA    1 
ATOM   4711 C  C     . ASN A 1 601 ? 13.010  22.510  3.880   1.00 23.04  ? 601  ASN A C     1 
ATOM   4712 O  O     . ASN A 1 601 ? 12.068  23.244  4.218   1.00 20.92  ? 601  ASN A O     1 
ATOM   4713 C  CB    . ASN A 1 601 ? 14.837  20.794  4.292   1.00 20.62  ? 601  ASN A CB    1 
ATOM   4714 C  CG    . ASN A 1 601 ? 16.030  21.664  3.916   1.00 26.79  ? 601  ASN A CG    1 
ATOM   4715 O  OD1   . ASN A 1 601 ? 16.109  22.802  4.340   1.00 26.62  ? 601  ASN A OD1   1 
ATOM   4716 N  ND2   . ASN A 1 601 ? 16.960  21.117  3.127   1.00 22.55  ? 601  ASN A ND2   1 
ATOM   4717 N  N     . ALA A 1 602 ? 13.431  22.448  2.620   1.00 23.09  ? 602  ALA A N     1 
ATOM   4718 C  CA    . ALA A 1 602 ? 12.959  23.481  1.698   1.00 23.79  ? 602  ALA A CA    1 
ATOM   4719 C  C     . ALA A 1 602 ? 11.524  23.260  1.243   1.00 27.30  ? 602  ALA A C     1 
ATOM   4720 O  O     . ALA A 1 602 ? 10.961  24.148  0.611   1.00 24.81  ? 602  ALA A O     1 
ATOM   4721 C  CB    . ALA A 1 602 ? 13.870  23.564  0.469   1.00 26.03  ? 602  ALA A CB    1 
ATOM   4722 N  N     . ASP A 1 603 ? 10.912  22.116  1.550   1.00 23.52  ? 603  ASP A N     1 
ATOM   4723 C  CA    . ASP A 1 603 ? 9.554   21.822  1.116   1.00 24.82  ? 603  ASP A CA    1 
ATOM   4724 C  C     . ASP A 1 603 ? 8.522   21.993  2.246   1.00 22.94  ? 603  ASP A C     1 
ATOM   4725 O  O     . ASP A 1 603 ? 7.340   21.691  2.054   1.00 20.86  ? 603  ASP A O     1 
ATOM   4726 C  CB    . ASP A 1 603 ? 9.506   20.404  0.531   1.00 22.32  ? 603  ASP A CB    1 
ATOM   4727 C  CG    . ASP A 1 603 ? 10.259  20.288  -0.796  1.00 29.62  ? 603  ASP A CG    1 
ATOM   4728 O  OD1   . ASP A 1 603 ? 10.026  21.132  -1.665  1.00 30.02  ? 603  ASP A OD1   1 
ATOM   4729 O  OD2   . ASP A 1 603 ? 11.051  19.336  -0.970  1.00 30.24  ? 603  ASP A OD2   1 
ATOM   4730 N  N     . LEU A 1 604 ? 8.939   22.510  3.392   1.00 22.76  ? 604  LEU A N     1 
ATOM   4731 C  CA    . LEU A 1 604 ? 8.008   22.823  4.490   1.00 22.00  ? 604  LEU A CA    1 
ATOM   4732 C  C     . LEU A 1 604 ? 7.099   23.995  4.119   1.00 23.94  ? 604  LEU A C     1 
ATOM   4733 O  O     . LEU A 1 604 ? 7.602   25.110  3.900   1.00 23.85  ? 604  LEU A O     1 
ATOM   4734 C  CB    . LEU A 1 604 ? 8.800   23.151  5.756   1.00 20.29  ? 604  LEU A CB    1 
ATOM   4735 C  CG    . LEU A 1 604 ? 7.957   23.166  7.036   1.00 26.35  ? 604  LEU A CG    1 
ATOM   4736 C  CD1   . LEU A 1 604 ? 7.511   21.746  7.375   1.00 25.01  ? 604  LEU A CD1   1 
ATOM   4737 C  CD2   . LEU A 1 604 ? 8.720   23.783  8.195   1.00 25.80  ? 604  LEU A CD2   1 
ATOM   4738 N  N     . PRO A 1 605 ? 5.777   23.806  4.036   1.00 25.95  ? 605  PRO A N     1 
ATOM   4739 C  CA    . PRO A 1 605 ? 4.889   24.944  3.756   1.00 22.37  ? 605  PRO A CA    1 
ATOM   4740 C  C     . PRO A 1 605 ? 5.010   26.022  4.815   1.00 24.34  ? 605  PRO A C     1 
ATOM   4741 O  O     . PRO A 1 605 ? 5.175   25.742  6.005   1.00 21.23  ? 605  PRO A O     1 
ATOM   4742 C  CB    . PRO A 1 605 ? 3.488   24.317  3.766   1.00 22.79  ? 605  PRO A CB    1 
ATOM   4743 C  CG    . PRO A 1 605 ? 3.732   22.859  3.488   1.00 23.73  ? 605  PRO A CG    1 
ATOM   4744 C  CD    . PRO A 1 605 ? 5.023   22.536  4.160   1.00 20.03  ? 605  PRO A CD    1 
ATOM   4745 N  N     . TYR A 1 606 ? 4.916   27.271  4.368   1.00 23.63  ? 606  TYR A N     1 
ATOM   4746 C  CA    . TYR A 1 606 ? 5.013   28.385  5.303   1.00 25.75  ? 606  TYR A CA    1 
ATOM   4747 C  C     . TYR A 1 606 ? 3.935   28.316  6.391   1.00 22.91  ? 606  TYR A C     1 
ATOM   4748 O  O     . TYR A 1 606 ? 4.167   28.736  7.523   1.00 21.38  ? 606  TYR A O     1 
ATOM   4749 C  CB    . TYR A 1 606 ? 4.914   29.716  4.555   1.00 23.31  ? 606  TYR A CB    1 
ATOM   4750 C  CG    . TYR A 1 606 ? 4.826   30.848  5.527   1.00 27.24  ? 606  TYR A CG    1 
ATOM   4751 C  CD1   . TYR A 1 606 ? 5.923   31.198  6.305   1.00 35.77  ? 606  TYR A CD1   1 
ATOM   4752 C  CD2   . TYR A 1 606 ? 3.629   31.509  5.737   1.00 31.52  ? 606  TYR A CD2   1 
ATOM   4753 C  CE1   . TYR A 1 606 ? 5.830   32.219  7.242   1.00 46.56  ? 606  TYR A CE1   1 
ATOM   4754 C  CE2   . TYR A 1 606 ? 3.534   32.536  6.647   1.00 36.12  ? 606  TYR A CE2   1 
ATOM   4755 C  CZ    . TYR A 1 606 ? 4.624   32.879  7.397   1.00 35.58  ? 606  TYR A CZ    1 
ATOM   4756 O  OH    . TYR A 1 606 ? 4.501   33.887  8.314   1.00 51.85  ? 606  TYR A OH    1 
ATOM   4757 N  N     . GLU A 1 607 ? 2.739   27.830  6.059   1.00 23.48  ? 607  GLU A N     1 
ATOM   4758 C  CA    . GLU A 1 607 ? 1.687   27.754  7.072   1.00 22.76  ? 607  GLU A CA    1 
ATOM   4759 C  C     . GLU A 1 607 ? 2.063   26.815  8.212   1.00 22.55  ? 607  GLU A C     1 
ATOM   4760 O  O     . GLU A 1 607 ? 1.614   27.016  9.343   1.00 22.00  ? 607  GLU A O     1 
ATOM   4761 C  CB    . GLU A 1 607 ? 0.368   27.333  6.415   1.00 22.83  ? 607  GLU A CB    1 
ATOM   4762 C  CG    . GLU A 1 607 ? -0.317  28.509  5.673   1.00 33.73  ? 607  GLU A CG    1 
ATOM   4763 C  CD    . GLU A 1 607 ? -1.687  28.175  5.090   1.00 40.08  ? 607  GLU A CD    1 
ATOM   4764 O  OE1   . GLU A 1 607 ? -1.880  27.058  4.582   1.00 40.97  ? 607  GLU A OE1   1 
ATOM   4765 O  OE2   . GLU A 1 607 ? -2.588  29.031  5.159   1.00 45.97  ? 607  GLU A OE2   1 
ATOM   4766 N  N     . ILE A 1 608 ? 2.886   25.794  7.945   1.00 18.09  ? 608  ILE A N     1 
ATOM   4767 C  CA    . ILE A 1 608 ? 3.267   24.851  9.009   1.00 20.78  ? 608  ILE A CA    1 
ATOM   4768 C  C     . ILE A 1 608 ? 4.314   25.486  9.916   1.00 20.67  ? 608  ILE A C     1 
ATOM   4769 O  O     . ILE A 1 608 ? 4.246   25.385  11.149  1.00 22.02  ? 608  ILE A O     1 
ATOM   4770 C  CB    . ILE A 1 608 ? 3.786   23.531  8.410   1.00 18.06  ? 608  ILE A CB    1 
ATOM   4771 C  CG1   . ILE A 1 608 ? 2.672   22.829  7.640   1.00 18.12  ? 608  ILE A CG1   1 
ATOM   4772 C  CG2   . ILE A 1 608 ? 4.279   22.631  9.535   1.00 19.30  ? 608  ILE A CG2   1 
ATOM   4773 C  CD1   . ILE A 1 608 ? 1.541   22.445  8.589   1.00 22.03  ? 608  ILE A CD1   1 
ATOM   4774 N  N     . GLU A 1 609 ? 5.292   26.157  9.312   1.00 20.50  ? 609  GLU A N     1 
ATOM   4775 C  CA    . GLU A 1 609 ? 6.280   26.903  10.076  1.00 21.53  ? 609  GLU A CA    1 
ATOM   4776 C  C     . GLU A 1 609 ? 5.617   28.013  10.886  1.00 20.61  ? 609  GLU A C     1 
ATOM   4777 O  O     . GLU A 1 609 ? 6.056   28.307  11.998  1.00 25.12  ? 609  GLU A O     1 
ATOM   4778 C  CB    . GLU A 1 609 ? 7.324   27.488  9.123   1.00 24.72  ? 609  GLU A CB    1 
ATOM   4779 C  CG    . GLU A 1 609 ? 8.285   28.467  9.763   1.00 38.37  ? 609  GLU A CG    1 
ATOM   4780 C  CD    . GLU A 1 609 ? 9.207   29.119  8.740   1.00 49.96  ? 609  GLU A CD    1 
ATOM   4781 O  OE1   . GLU A 1 609 ? 9.274   28.639  7.578   1.00 48.25  ? 609  GLU A OE1   1 
ATOM   4782 O  OE2   . GLU A 1 609 ? 9.861   30.117  9.108   1.00 62.79  ? 609  GLU A OE2   1 
ATOM   4783 N  N     . ARG A 1 610 ? 4.546   28.608  10.362  1.00 18.17  ? 610  ARG A N     1 
ATOM   4784 C  CA    . ARG A 1 610 ? 3.830   29.639  11.104  1.00 18.85  ? 610  ARG A CA    1 
ATOM   4785 C  C     . ARG A 1 610 ? 3.132   29.068  12.342  1.00 19.99  ? 610  ARG A C     1 
ATOM   4786 O  O     . ARG A 1 610 ? 3.146   29.692  13.412  1.00 20.55  ? 610  ARG A O     1 
ATOM   4787 C  CB    . ARG A 1 610 ? 2.808   30.335  10.198  1.00 22.91  ? 610  ARG A CB    1 
ATOM   4788 C  CG    . ARG A 1 610 ? 2.026   31.468  10.935  1.00 24.68  ? 610  ARG A CG    1 
ATOM   4789 C  CD    . ARG A 1 610 ? 1.117   32.211  9.948   1.00 28.63  ? 610  ARG A CD    1 
ATOM   4790 N  NE    . ARG A 1 610 ? 0.042   31.382  9.408   1.00 27.37  ? 610  ARG A NE    1 
ATOM   4791 C  CZ    . ARG A 1 610 ? -0.688  31.717  8.350   1.00 32.86  ? 610  ARG A CZ    1 
ATOM   4792 N  NH1   . ARG A 1 610 ? -0.466  32.838  7.687   1.00 36.20  ? 610  ARG A NH1   1 
ATOM   4793 N  NH2   . ARG A 1 610 ? -1.671  30.913  7.952   1.00 31.33  ? 610  ARG A NH2   1 
ATOM   4794 N  N     . GLU A 1 611 ? 2.498   27.895  12.216  1.00 22.20  ? 611  GLU A N     1 
ATOM   4795 C  CA    . GLU A 1 611 ? 1.891   27.246  13.387  1.00 21.89  ? 611  GLU A CA    1 
ATOM   4796 C  C     . GLU A 1 611 ? 2.939   26.826  14.414  1.00 19.97  ? 611  GLU A C     1 
ATOM   4797 O  O     . GLU A 1 611 ? 2.691   26.882  15.624  1.00 19.61  ? 611  GLU A O     1 
ATOM   4798 C  CB    . GLU A 1 611 ? 1.062   26.029  12.961  1.00 18.10  ? 611  GLU A CB    1 
ATOM   4799 C  CG    . GLU A 1 611 ? -0.173  26.366  12.105  1.00 18.09  ? 611  GLU A CG    1 
ATOM   4800 C  CD    . GLU A 1 611 ? -1.155  27.279  12.832  1.00 25.18  ? 611  GLU A CD    1 
ATOM   4801 O  OE1   . GLU A 1 611 ? -1.408  27.070  14.038  1.00 23.78  ? 611  GLU A OE1   1 
ATOM   4802 O  OE2   . GLU A 1 611 ? -1.668  28.226  12.201  1.00 29.25  ? 611  GLU A OE2   1 
ATOM   4803 N  N     . LEU A 1 612 ? 4.119   26.424  13.968  1.00 19.19  ? 612  LEU A N     1 
ATOM   4804 C  CA    . LEU A 1 612 ? 5.163   26.107  14.932  1.00 22.16  ? 612  LEU A CA    1 
ATOM   4805 C  C     . LEU A 1 612 ? 5.571   27.349  15.714  1.00 21.54  ? 612  LEU A C     1 
ATOM   4806 O  O     . LEU A 1 612 ? 5.703   27.303  16.948  1.00 22.90  ? 612  LEU A O     1 
ATOM   4807 C  CB    . LEU A 1 612 ? 6.355   25.502  14.213  1.00 19.43  ? 612  LEU A CB    1 
ATOM   4808 C  CG    . LEU A 1 612 ? 7.565   25.216  15.084  1.00 28.83  ? 612  LEU A CG    1 
ATOM   4809 C  CD1   . LEU A 1 612 ? 7.242   24.095  16.059  1.00 25.31  ? 612  LEU A CD1   1 
ATOM   4810 C  CD2   . LEU A 1 612 ? 8.705   24.800  14.167  1.00 38.37  ? 612  LEU A CD2   1 
ATOM   4811 N  N     . ARG A 1 613 ? 5.794   28.474  15.002  1.00 23.20  ? 613  ARG A N     1 
ATOM   4812 C  CA    . ARG A 1 613 ? 6.100   29.734  15.676  1.00 23.78  ? 613  ARG A CA    1 
ATOM   4813 C  C     . ARG A 1 613 ? 4.984   30.149  16.619  1.00 21.21  ? 613  ARG A C     1 
ATOM   4814 O  O     . ARG A 1 613 ? 5.251   30.656  17.711  1.00 23.13  ? 613  ARG A O     1 
ATOM   4815 C  CB    . ARG A 1 613 ? 6.344   30.864  14.661  1.00 25.31  ? 613  ARG A CB    1 
ATOM   4816 C  CG    . ARG A 1 613 ? 7.537   30.657  13.724  1.00 30.64  ? 613  ARG A CG    1 
ATOM   4817 C  CD    . ARG A 1 613 ? 7.716   31.954  12.950  1.00 38.39  ? 613  ARG A CD    1 
ATOM   4818 N  NE    . ARG A 1 613 ? 8.731   31.865  11.921  1.00 42.69  ? 613  ARG A NE    1 
ATOM   4819 C  CZ    . ARG A 1 613 ? 9.407   32.911  11.458  1.00 56.85  ? 613  ARG A CZ    1 
ATOM   4820 N  NH1   . ARG A 1 613 ? 9.238   34.129  11.963  1.00 42.13  ? 613  ARG A NH1   1 
ATOM   4821 N  NH2   . ARG A 1 613 ? 10.282  32.729  10.472  1.00 54.16  ? 613  ARG A NH2   1 
ATOM   4822 N  N     . ALA A 1 614 ? 3.729   29.992  16.198  1.00 19.10  ? 614  ALA A N     1 
ATOM   4823 C  CA    . ALA A 1 614 ? 2.613   30.368  17.068  1.00 21.35  ? 614  ALA A CA    1 
ATOM   4824 C  C     . ALA A 1 614 ? 2.572   29.496  18.321  1.00 26.05  ? 614  ALA A C     1 
ATOM   4825 O  O     . ALA A 1 614 ? 2.357   30.002  19.428  1.00 25.12  ? 614  ALA A O     1 
ATOM   4826 C  CB    . ALA A 1 614 ? 1.286   30.263  16.311  1.00 20.75  ? 614  ALA A CB    1 
ATOM   4827 N  N     . LEU A 1 615 ? 2.770   28.182  18.177  1.00 20.28  ? 615  LEU A N     1 
ATOM   4828 C  CA    . LEU A 1 615 ? 2.786   27.341  19.373  1.00 19.98  ? 615  LEU A CA    1 
ATOM   4829 C  C     . LEU A 1 615 ? 3.941   27.743  20.288  1.00 25.32  ? 615  LEU A C     1 
ATOM   4830 O  O     . LEU A 1 615 ? 3.771   27.850  21.510  1.00 23.47  ? 615  LEU A O     1 
ATOM   4831 C  CB    . LEU A 1 615 ? 2.891   25.860  18.994  1.00 21.76  ? 615  LEU A CB    1 
ATOM   4832 C  CG    . LEU A 1 615 ? 2.943   24.889  20.188  1.00 22.28  ? 615  LEU A CG    1 
ATOM   4833 C  CD1   . LEU A 1 615 ? 1.780   25.109  21.122  1.00 22.76  ? 615  LEU A CD1   1 
ATOM   4834 C  CD2   . LEU A 1 615 ? 2.995   23.442  19.719  1.00 25.22  ? 615  LEU A CD2   1 
ATOM   4835 N  N     . LYS A 1 616 ? 5.113   28.016  19.708  1.00 25.27  ? 616  LYS A N     1 
ATOM   4836 C  CA    . LYS A 1 616 ? 6.253   28.417  20.528  1.00 26.04  ? 616  LYS A CA    1 
ATOM   4837 C  C     . LYS A 1 616 ? 5.920   29.655  21.339  1.00 27.12  ? 616  LYS A C     1 
ATOM   4838 O  O     . LYS A 1 616 ? 6.275   29.749  22.526  1.00 27.06  ? 616  LYS A O     1 
ATOM   4839 C  CB    . LYS A 1 616 ? 7.481   28.668  19.659  1.00 24.43  ? 616  LYS A CB    1 
ATOM   4840 C  CG    . LYS A 1 616 ? 8.693   29.068  20.477  1.00 31.89  ? 616  LYS A CG    1 
ATOM   4841 C  CD    . LYS A 1 616 ? 9.980   28.777  19.732  1.00 48.08  ? 616  LYS A CD    1 
ATOM   4842 C  CE    . LYS A 1 616 ? 11.190  29.172  20.578  1.00 61.64  ? 616  LYS A CE    1 
ATOM   4843 N  NZ    . LYS A 1 616 ? 12.485  28.826  19.908  1.00 69.51  ? 616  LYS A NZ    1 
ATOM   4844 N  N     . GLN A 1 617 ? 5.180   30.587  20.727  1.00 25.48  ? 617  GLN A N     1 
ATOM   4845 C  CA    . GLN A 1 617 ? 4.868   31.848  21.386  1.00 27.13  ? 617  GLN A CA    1 
ATOM   4846 C  C     . GLN A 1 617 ? 3.848   31.657  22.504  1.00 27.88  ? 617  GLN A C     1 
ATOM   4847 O  O     . GLN A 1 617 ? 4.017   32.207  23.600  1.00 28.28  ? 617  GLN A O     1 
ATOM   4848 C  CB    . GLN A 1 617 ? 4.362   32.856  20.349  1.00 27.76  ? 617  GLN A CB    1 
ATOM   4849 C  CG    . GLN A 1 617 ? 4.079   34.249  20.905  1.00 29.29  ? 617  GLN A CG    1 
ATOM   4850 C  CD    . GLN A 1 617 ? 5.345   34.972  21.322  1.00 34.40  ? 617  GLN A CD    1 
ATOM   4851 O  OE1   . GLN A 1 617 ? 6.449   34.606  20.911  1.00 37.15  ? 617  GLN A OE1   1 
ATOM   4852 N  NE2   . GLN A 1 617 ? 5.191   35.999  22.145  1.00 38.18  ? 617  GLN A NE2   1 
ATOM   4853 N  N     . ARG A 1 618 ? 2.770   30.907  22.242  1.00 26.14  ? 618  ARG A N     1 
ATOM   4854 C  CA    . ARG A 1 618 ? 1.800   30.620  23.299  1.00 26.88  ? 618  ARG A CA    1 
ATOM   4855 C  C     . ARG A 1 618 ? 2.450   29.902  24.476  1.00 26.70  ? 618  ARG A C     1 
ATOM   4856 O  O     . ARG A 1 618 ? 2.078   30.148  25.625  1.00 32.37  ? 618  ARG A O     1 
ATOM   4857 C  CB    . ARG A 1 618 ? 0.628   29.789  22.751  1.00 27.47  ? 618  ARG A CB    1 
ATOM   4858 C  CG    . ARG A 1 618 ? -0.205  30.501  21.696  1.00 25.48  ? 618  ARG A CG    1 
ATOM   4859 C  CD    . ARG A 1 618 ? -1.476  29.737  21.294  1.00 22.51  ? 618  ARG A CD    1 
ATOM   4860 N  NE    . ARG A 1 618 ? -1.215  28.398  20.756  1.00 26.60  ? 618  ARG A NE    1 
ATOM   4861 C  CZ    . ARG A 1 618 ? -1.089  28.095  19.469  1.00 24.05  ? 618  ARG A CZ    1 
ATOM   4862 N  NH1   . ARG A 1 618 ? -1.091  29.031  18.530  1.00 23.51  ? 618  ARG A NH1   1 
ATOM   4863 N  NH2   . ARG A 1 618 ? -0.952  26.811  19.107  1.00 22.98  ? 618  ARG A NH2   1 
ATOM   4864 N  N     . ILE A 1 619 ? 3.427   29.028  24.226  1.00 25.97  ? 619  ILE A N     1 
ATOM   4865 C  CA    . ILE A 1 619 ? 4.058   28.327  25.340  1.00 28.52  ? 619  ILE A CA    1 
ATOM   4866 C  C     . ILE A 1 619 ? 4.947   29.268  26.128  1.00 32.65  ? 619  ILE A C     1 
ATOM   4867 O  O     . ILE A 1 619 ? 5.011   29.191  27.361  1.00 28.93  ? 619  ILE A O     1 
ATOM   4868 C  CB    . ILE A 1 619 ? 4.861   27.112  24.847  1.00 29.69  ? 619  ILE A CB    1 
ATOM   4869 C  CG1   . ILE A 1 619 ? 3.922   26.005  24.371  1.00 27.11  ? 619  ILE A CG1   1 
ATOM   4870 C  CG2   . ILE A 1 619 ? 5.777   26.582  25.960  1.00 29.31  ? 619  ILE A CG2   1 
ATOM   4871 C  CD1   . ILE A 1 619 ? 4.663   24.969  23.612  1.00 32.95  ? 619  ILE A CD1   1 
ATOM   4872 N  N     . SER A 1 620 ? 5.674   30.144  25.430  1.00 30.73  ? 620  SER A N     1 
ATOM   4873 C  CA    . SER A 1 620 ? 6.538   31.098  26.112  1.00 32.10  ? 620  SER A CA    1 
ATOM   4874 C  C     . SER A 1 620 ? 5.749   32.041  27.024  1.00 31.92  ? 620  SER A C     1 
ATOM   4875 O  O     . SER A 1 620 ? 6.311   32.559  27.996  1.00 36.93  ? 620  SER A O     1 
ATOM   4876 C  CB    . SER A 1 620 ? 7.337   31.894  25.075  1.00 33.26  ? 620  SER A CB    1 
ATOM   4877 O  OG    . SER A 1 620 ? 6.516   32.906  24.507  1.00 38.54  ? 620  SER A OG    1 
ATOM   4878 N  N     . GLN A 1 621 ? 4.469   32.269  26.748  1.00 27.08  ? 621  GLN A N     1 
ATOM   4879 C  CA    . GLN A 1 621 ? 3.641   33.136  27.573  1.00 30.14  ? 621  GLN A CA    1 
ATOM   4880 C  C     . GLN A 1 621 ? 3.031   32.434  28.784  1.00 41.03  ? 621  GLN A C     1 
ATOM   4881 O  O     . GLN A 1 621 ? 2.327   33.081  29.561  1.00 42.56  ? 621  GLN A O     1 
ATOM   4882 C  CB    . GLN A 1 621 ? 2.532   33.738  26.721  1.00 32.93  ? 621  GLN A CB    1 
ATOM   4883 C  CG    . GLN A 1 621 ? 3.085   34.621  25.615  1.00 39.07  ? 621  GLN A CG    1 
ATOM   4884 C  CD    . GLN A 1 621 ? 3.833   35.832  26.156  1.00 40.58  ? 621  GLN A CD    1 
ATOM   4885 O  OE1   . GLN A 1 621 ? 3.299   36.607  26.969  1.00 38.13  ? 621  GLN A OE1   1 
ATOM   4886 N  NE2   . GLN A 1 621 ? 5.083   35.991  25.721  1.00 42.87  ? 621  GLN A NE2   1 
ATOM   4887 N  N     . MET A 1 622 ? 3.278   31.138  28.965  1.00 32.77  ? 622  MET A N     1 
ATOM   4888 C  CA    . MET A 1 622 ? 2.847   30.423  30.168  1.00 34.75  ? 622  MET A CA    1 
ATOM   4889 C  C     . MET A 1 622 ? 3.644   30.818  31.403  1.00 40.00  ? 622  MET A C     1 
ATOM   4890 O  O     . MET A 1 622 ? 4.776   31.301  31.322  1.00 39.05  ? 622  MET A O     1 
ATOM   4891 C  CB    . MET A 1 622 ? 2.976   28.904  29.983  1.00 35.89  ? 622  MET A CB    1 
ATOM   4892 C  CG    . MET A 1 622 ? 2.144   28.322  28.882  1.00 32.20  ? 622  MET A CG    1 
ATOM   4893 S  SD    . MET A 1 622 ? 2.516   26.557  28.778  1.00 33.96  ? 622  MET A SD    1 
ATOM   4894 C  CE    . MET A 1 622 ? 1.591   25.923  30.188  1.00 36.84  ? 622  MET A CE    1 
ATOM   4895 O  OXT   . MET A 1 622 ? 3.169   30.617  32.522  1.00 44.53  ? 622  MET A OXT   1 
HETATM 4896 MN MN    . MN  B 2 .   ? -1.991  -0.306  9.603   1.00 19.17  ? 701  MN  A MN    1 
HETATM 4897 MN MN    . MN  C 2 .   ? -5.294  -2.829  13.153  1.00 24.38  ? 702  MN  A MN    1 
HETATM 4898 MN MN    . MN  D 2 .   ? -4.856  29.548  3.781   1.00 90.41  ? 703  MN  A MN    1 
HETATM 4899 C  C1    . SPV E 3 .   ? 0.520   -1.850  9.865   1.00 23.28  ? 704  SPV A C1    1 
HETATM 4900 O  O1    . SPV E 3 .   ? 0.020   -0.744  10.096  1.00 22.49  ? 704  SPV A O1    1 
HETATM 4901 O  "O2'" . SPV E 3 .   ? 1.724   -2.162  9.955   1.00 25.91  ? 704  SPV A "O2'" 1 
HETATM 4902 C  C2    . SPV E 3 .   ? -0.560  -2.948  9.476   1.00 23.82  ? 704  SPV A C2    1 
HETATM 4903 C  C3    . SPV E 3 .   ? -0.057  -4.362  9.231   1.00 18.82  ? 704  SPV A C3    1 
HETATM 4904 O  O2    . SPV E 3 .   ? -1.759  -2.647  9.400   1.00 19.85  ? 704  SPV A O2    1 
HETATM 4905 S  S     . SPV E 3 .   ? 0.664   -4.699  7.615   1.00 21.82  ? 704  SPV A S     1 
HETATM 4906 O  O1S   . SPV E 3 .   ? 1.449   -5.954  7.737   1.00 21.68  ? 704  SPV A O1S   1 
HETATM 4907 O  O2S   . SPV E 3 .   ? 1.574   -3.570  7.341   1.00 24.03  ? 704  SPV A O2S   1 
HETATM 4908 O  O3S   . SPV E 3 .   ? -0.527  -4.737  6.712   1.00 20.45  ? 704  SPV A O3S   1 
HETATM 4909 P  PG    A GTP F 4 .   ? -2.237  -1.888  12.834  0.27 20.96  ? 705  GTP A PG    1 
HETATM 4910 P  PG    B GTP F 4 .   ? -2.244  -1.797  12.591  0.73 20.32  ? 705  GTP A PG    1 
HETATM 4911 O  O1G   A GTP F 4 .   ? -2.540  -0.856  11.767  0.27 22.60  ? 705  GTP A O1G   1 
HETATM 4912 O  O1G   B GTP F 4 .   ? -2.316  -0.560  11.709  0.73 24.09  ? 705  GTP A O1G   1 
HETATM 4913 O  O2G   A GTP F 4 .   ? -0.883  -2.495  12.608  0.27 21.37  ? 705  GTP A O2G   1 
HETATM 4914 O  O2G   B GTP F 4 .   ? -0.897  -2.431  12.585  0.73 21.31  ? 705  GTP A O2G   1 
HETATM 4915 O  O3G   A GTP F 4 .   ? -3.279  -2.982  12.778  0.27 22.36  ? 705  GTP A O3G   1 
HETATM 4916 O  O3G   B GTP F 4 .   ? -3.275  -2.804  12.120  0.73 21.46  ? 705  GTP A O3G   1 
HETATM 4917 O  O3B   A GTP F 4 .   ? -2.199  -1.174  14.284  0.27 22.20  ? 705  GTP A O3B   1 
HETATM 4918 O  O3B   B GTP F 4 .   ? -2.330  -1.339  14.141  0.73 21.90  ? 705  GTP A O3B   1 
HETATM 4919 P  PB    A GTP F 4 .   ? -3.492  -0.601  15.061  0.27 23.13  ? 705  GTP A PB    1 
HETATM 4920 P  PB    B GTP F 4 .   ? -3.537  -0.853  15.091  0.73 23.56  ? 705  GTP A PB    1 
HETATM 4921 O  O1B   A GTP F 4 .   ? -3.454  0.915   15.032  0.27 20.47  ? 705  GTP A O1B   1 
HETATM 4922 O  O1B   B GTP F 4 .   ? -3.669  0.665   15.076  0.73 20.82  ? 705  GTP A O1B   1 
HETATM 4923 O  O2B   A GTP F 4 .   ? -4.787  -1.118  14.485  0.27 21.04  ? 705  GTP A O2B   1 
HETATM 4924 O  O2B   B GTP F 4 .   ? -4.865  -1.514  14.802  0.73 22.15  ? 705  GTP A O2B   1 
HETATM 4925 O  O3A   A GTP F 4 .   ? -3.277  -1.023  16.604  0.27 21.44  ? 705  GTP A O3A   1 
HETATM 4926 O  O3A   B GTP F 4 .   ? -2.879  -1.237  16.532  0.73 21.84  ? 705  GTP A O3A   1 
HETATM 4927 P  PA    A GTP F 4 .   ? -4.069  -2.170  17.430  0.27 22.39  ? 705  GTP A PA    1 
HETATM 4928 P  PA    B GTP F 4 .   ? -2.854  -2.653  17.363  0.73 24.66  ? 705  GTP A PA    1 
HETATM 4929 O  O1A   A GTP F 4 .   ? -5.550  -1.960  17.335  0.27 22.18  ? 705  GTP A O1A   1 
HETATM 4930 O  O1A   B GTP F 4 .   ? -4.014  -3.540  16.919  0.73 22.84  ? 705  GTP A O1A   1 
HETATM 4931 O  O2A   A GTP F 4 .   ? -3.673  -3.562  16.979  0.27 22.64  ? 705  GTP A O2A   1 
HETATM 4932 O  O2A   B GTP F 4 .   ? -1.551  -3.380  17.414  0.73 24.20  ? 705  GTP A O2A   1 
HETATM 4933 O  "O5'" A GTP F 4 .   ? -3.544  -1.867  18.923  0.27 22.08  ? 705  GTP A "O5'" 1 
HETATM 4934 O  "O5'" B GTP F 4 .   ? -3.100  -2.131  18.859  0.73 22.65  ? 705  GTP A "O5'" 1 
HETATM 4935 C  "C5'" A GTP F 4 .   ? -2.904  -2.822  19.743  0.27 24.22  ? 705  GTP A "C5'" 1 
HETATM 4936 C  "C5'" B GTP F 4 .   ? -3.229  -3.025  19.942  0.73 24.16  ? 705  GTP A "C5'" 1 
HETATM 4937 C  "C4'" A GTP F 4 .   ? -2.315  -2.127  20.970  0.27 23.80  ? 705  GTP A "C4'" 1 
HETATM 4938 C  "C4'" B GTP F 4 .   ? -2.488  -2.430  21.129  0.73 24.00  ? 705  GTP A "C4'" 1 
HETATM 4939 O  "O4'" A GTP F 4 .   ? -3.033  -0.945  21.295  0.27 22.94  ? 705  GTP A "O4'" 1 
HETATM 4940 O  "O4'" B GTP F 4 .   ? -3.001  -1.151  21.517  0.73 22.97  ? 705  GTP A "O4'" 1 
HETATM 4941 C  "C3'" A GTP F 4 .   ? -2.379  -3.010  22.198  0.27 25.06  ? 705  GTP A "C3'" 1 
HETATM 4942 C  "C3'" B GTP F 4 .   ? -2.633  -3.341  22.314  0.73 25.93  ? 705  GTP A "C3'" 1 
HETATM 4943 O  "O3'" A GTP F 4 .   ? -1.153  -2.854  22.862  0.27 25.86  ? 705  GTP A "O3'" 1 
HETATM 4944 O  "O3'" B GTP F 4 .   ? -1.373  -3.280  22.921  0.73 27.84  ? 705  GTP A "O3'" 1 
HETATM 4945 C  "C2'" A GTP F 4 .   ? -3.465  -2.389  23.047  0.27 25.56  ? 705  GTP A "C2'" 1 
HETATM 4946 C  "C2'" B GTP F 4 .   ? -3.629  -2.620  23.184  0.73 26.43  ? 705  GTP A "C2'" 1 
HETATM 4947 O  "O2'" A GTP F 4 .   ? -3.225  -2.598  24.422  0.27 26.96  ? 705  GTP A "O2'" 1 
HETATM 4948 O  "O2'" B GTP F 4 .   ? -3.413  -2.952  24.543  0.73 27.83  ? 705  GTP A "O2'" 1 
HETATM 4949 C  "C1'" A GTP F 4 .   ? -3.331  -0.926  22.676  0.27 21.61  ? 705  GTP A "C1'" 1 
HETATM 4950 C  "C1'" B GTP F 4 .   ? -3.327  -1.157  22.887  0.73 20.46  ? 705  GTP A "C1'" 1 
HETATM 4951 N  N9    A GTP F 4 .   ? -4.574  -0.171  22.900  0.27 22.98  ? 705  GTP A N9    1 
HETATM 4952 N  N9    B GTP F 4 .   ? -4.524  -0.331  23.079  0.73 22.72  ? 705  GTP A N9    1 
HETATM 4953 C  C8    A GTP F 4 .   ? -5.615  -0.006  22.023  0.27 23.30  ? 705  GTP A C8    1 
HETATM 4954 C  C8    B GTP F 4 .   ? -5.586  -0.151  22.223  0.73 23.36  ? 705  GTP A C8    1 
HETATM 4955 N  N7    A GTP F 4 .   ? -6.548  0.778   22.606  0.27 23.99  ? 705  GTP A N7    1 
HETATM 4956 N  N7    B GTP F 4 .   ? -6.453  0.708   22.803  0.73 24.20  ? 705  GTP A N7    1 
HETATM 4957 C  C5    A GTP F 4 .   ? -6.110  1.123   23.835  0.27 21.15  ? 705  GTP A C5    1 
HETATM 4958 C  C5    B GTP F 4 .   ? -5.957  1.076   24.004  0.73 20.44  ? 705  GTP A C5    1 
HETATM 4959 C  C6    A GTP F 4 .   ? -6.663  1.901   24.834  0.27 22.02  ? 705  GTP A C6    1 
HETATM 4960 C  C6    B GTP F 4 .   ? -6.417  1.920   24.991  0.73 21.70  ? 705  GTP A C6    1 
HETATM 4961 O  O6    A GTP F 4 .   ? -7.767  2.417   24.661  0.27 22.67  ? 705  GTP A O6    1 
HETATM 4962 O  O6    B GTP F 4 .   ? -7.495  2.503   24.863  0.73 22.08  ? 705  GTP A O6    1 
HETATM 4963 N  N1    A GTP F 4 .   ? -5.964  2.076   26.011  0.27 23.49  ? 705  GTP A N1    1 
HETATM 4964 N  N1    B GTP F 4 .   ? -5.648  2.071   26.123  0.73 23.54  ? 705  GTP A N1    1 
HETATM 4965 C  C2    A GTP F 4 .   ? -4.728  1.480   26.182  0.27 23.93  ? 705  GTP A C2    1 
HETATM 4966 C  C2    B GTP F 4 .   ? -4.443  1.410   26.275  0.73 24.28  ? 705  GTP A C2    1 
HETATM 4967 N  N2    A GTP F 4 .   ? -4.035  1.645   27.306  0.27 24.95  ? 705  GTP A N2    1 
HETATM 4968 N  N2    B GTP F 4 .   ? -3.680  1.575   27.359  0.73 24.61  ? 705  GTP A N2    1 
HETATM 4969 N  N3    A GTP F 4 .   ? -4.188  0.709   25.181  0.27 23.83  ? 705  GTP A N3    1 
HETATM 4970 N  N3    B GTP F 4 .   ? -3.994  0.579   25.286  0.73 23.65  ? 705  GTP A N3    1 
HETATM 4971 C  C4    A GTP F 4 .   ? -4.870  0.535   24.029  0.27 22.59  ? 705  GTP A C4    1 
HETATM 4972 C  C4    B GTP F 4 .   ? -4.747  0.422   24.180  0.73 22.34  ? 705  GTP A C4    1 
HETATM 4973 O  O     . HOH G 5 .   ? 4.296   35.770  9.071   1.00 32.04  ? 801  HOH A O     1 
HETATM 4974 O  O     . HOH G 5 .   ? 9.249   29.219  26.566  1.00 39.70  ? 802  HOH A O     1 
HETATM 4975 O  O     . HOH G 5 .   ? -23.980 19.340  2.000   1.00 36.72  ? 803  HOH A O     1 
HETATM 4976 O  O     . HOH G 5 .   ? 9.973   9.246   -12.164 1.00 44.47  ? 804  HOH A O     1 
HETATM 4977 O  O     . HOH G 5 .   ? -1.977  -32.280 -3.192  1.00 38.93  ? 805  HOH A O     1 
HETATM 4978 O  O     . HOH G 5 .   ? -19.851 -8.926  -13.920 1.00 49.21  ? 806  HOH A O     1 
HETATM 4979 O  O     . HOH G 5 .   ? 16.893  14.819  11.790  1.00 30.94  ? 807  HOH A O     1 
HETATM 4980 O  O     . HOH G 5 .   ? -4.186  -5.082  24.839  1.00 35.02  ? 808  HOH A O     1 
HETATM 4981 O  O     . HOH G 5 .   ? 1.852   -26.753 14.314  1.00 40.10  ? 809  HOH A O     1 
HETATM 4982 O  O     . HOH G 5 .   ? 10.028  -26.983 5.992   1.00 45.02  ? 810  HOH A O     1 
HETATM 4983 O  O     . HOH G 5 .   ? -22.587 -8.361  6.916   1.00 36.22  ? 811  HOH A O     1 
HETATM 4984 O  O     . HOH G 5 .   ? 13.385  19.205  -1.165  1.00 28.42  ? 812  HOH A O     1 
HETATM 4985 O  O     . HOH G 5 .   ? 4.479   -30.769 -14.502 1.00 40.02  ? 813  HOH A O     1 
HETATM 4986 O  O     . HOH G 5 .   ? 4.364   3.834   18.769  1.00 27.76  ? 814  HOH A O     1 
HETATM 4987 O  O     . HOH G 5 .   ? -8.308  6.497   -9.277  1.00 43.37  ? 815  HOH A O     1 
HETATM 4988 O  O     . HOH G 5 .   ? -0.927  -30.103 -2.796  1.00 44.62  ? 816  HOH A O     1 
HETATM 4989 O  O     . HOH G 5 .   ? -4.214  -28.802 17.881  1.00 42.97  ? 817  HOH A O     1 
HETATM 4990 O  O     . HOH G 5 .   ? -10.874 -13.246 25.711  1.00 36.20  ? 818  HOH A O     1 
HETATM 4991 O  O     . HOH G 5 .   ? 16.767  -23.866 -7.387  1.00 47.25  ? 819  HOH A O     1 
HETATM 4992 O  O     . HOH G 5 .   ? -7.634  -32.205 -2.237  1.00 40.69  ? 820  HOH A O     1 
HETATM 4993 O  O     . HOH G 5 .   ? -11.300 23.985  16.795  1.00 32.61  ? 821  HOH A O     1 
HETATM 4994 O  O     . HOH G 5 .   ? 1.440   17.812  32.652  1.00 39.35  ? 822  HOH A O     1 
HETATM 4995 O  O     . HOH G 5 .   ? -1.795  18.317  -7.156  1.00 45.10  ? 823  HOH A O     1 
HETATM 4996 O  O     . HOH G 5 .   ? 21.109  7.218   3.665   1.00 41.66  ? 824  HOH A O     1 
HETATM 4997 O  O     . HOH G 5 .   ? 1.354   -22.574 -24.964 1.00 34.09  ? 825  HOH A O     1 
HETATM 4998 O  O     . HOH G 5 .   ? 19.270  4.361   -5.975  1.00 37.09  ? 826  HOH A O     1 
HETATM 4999 O  O     . HOH G 5 .   ? -7.777  -8.423  28.312  1.00 48.00  ? 827  HOH A O     1 
HETATM 5000 O  O     . HOH G 5 .   ? 2.192   -23.463 8.525   1.00 33.23  ? 828  HOH A O     1 
HETATM 5001 O  O     . HOH G 5 .   ? -6.097  -4.101  18.461  1.00 26.77  ? 829  HOH A O     1 
HETATM 5002 O  O     . HOH G 5 .   ? -25.961 4.584   9.124   1.00 37.36  ? 830  HOH A O     1 
HETATM 5003 O  O     . HOH G 5 .   ? -27.867 0.077   14.273  1.00 50.87  ? 831  HOH A O     1 
HETATM 5004 O  O     . HOH G 5 .   ? 5.132   -29.831 -10.734 1.00 41.70  ? 832  HOH A O     1 
HETATM 5005 O  O     . HOH G 5 .   ? 14.149  -16.052 -17.302 1.00 41.45  ? 833  HOH A O     1 
HETATM 5006 O  O     . HOH G 5 .   ? -26.287 17.000  15.100  1.00 26.76  ? 834  HOH A O     1 
HETATM 5007 O  O     . HOH G 5 .   ? 0.699   -23.493 -5.436  1.00 28.60  ? 835  HOH A O     1 
HETATM 5008 O  O     . HOH G 5 .   ? -9.504  1.209   -14.571 1.00 39.40  ? 836  HOH A O     1 
HETATM 5009 O  O     . HOH G 5 .   ? -0.387  27.039  2.576   1.00 39.37  ? 837  HOH A O     1 
HETATM 5010 O  O     . HOH G 5 .   ? 7.941   6.129   4.071   1.00 28.06  ? 838  HOH A O     1 
HETATM 5011 O  O     . HOH G 5 .   ? -4.383  17.602  -6.253  1.00 45.38  ? 839  HOH A O     1 
HETATM 5012 O  O     . HOH G 5 .   ? 13.381  13.889  3.991   1.00 27.21  ? 840  HOH A O     1 
HETATM 5013 O  O     . HOH G 5 .   ? -17.701 -7.165  -0.004  1.00 34.25  ? 841  HOH A O     1 
HETATM 5014 O  O     . HOH G 5 .   ? 6.482   14.246  13.980  1.00 20.74  ? 842  HOH A O     1 
HETATM 5015 O  O     . HOH G 5 .   ? -16.957 -20.993 15.091  1.00 36.72  ? 843  HOH A O     1 
HETATM 5016 O  O     . HOH G 5 .   ? 15.124  -15.810 -7.867  1.00 37.42  ? 844  HOH A O     1 
HETATM 5017 O  O     . HOH G 5 .   ? 11.109  24.042  11.873  1.00 44.70  ? 845  HOH A O     1 
HETATM 5018 O  O     . HOH G 5 .   ? -5.393  -29.559 9.099   1.00 32.65  ? 846  HOH A O     1 
HETATM 5019 O  O     . HOH G 5 .   ? -3.394  6.580   30.297  1.00 23.45  ? 847  HOH A O     1 
HETATM 5020 O  O     . HOH G 5 .   ? 12.327  26.253  20.375  1.00 48.14  ? 848  HOH A O     1 
HETATM 5021 O  O     . HOH G 5 .   ? 5.673   4.560   14.060  1.00 40.72  ? 849  HOH A O     1 
HETATM 5022 O  O     . HOH G 5 .   ? -6.557  8.498   36.974  1.00 43.11  ? 850  HOH A O     1 
HETATM 5023 O  O     . HOH G 5 .   ? -9.349  -0.671  6.258   1.00 20.11  ? 851  HOH A O     1 
HETATM 5024 O  O     . HOH G 5 .   ? -21.296 12.255  9.566   1.00 19.62  ? 852  HOH A O     1 
HETATM 5025 O  O     . HOH G 5 .   ? -19.787 -26.298 -5.463  1.00 51.38  ? 853  HOH A O     1 
HETATM 5026 O  O     . HOH G 5 .   ? 7.869   -21.890 21.672  1.00 44.84  ? 854  HOH A O     1 
HETATM 5027 O  O     . HOH G 5 .   ? -10.567 -30.567 29.017  1.00 28.16  ? 855  HOH A O     1 
HETATM 5028 O  O     . HOH G 5 .   ? -0.933  -6.351  21.020  1.00 31.40  ? 856  HOH A O     1 
HETATM 5029 O  O     . HOH G 5 .   ? -4.049  9.004   28.616  1.00 25.63  ? 857  HOH A O     1 
HETATM 5030 O  O     . HOH G 5 .   ? 9.330   -9.833  6.903   1.00 39.00  ? 858  HOH A O     1 
HETATM 5031 O  O     . HOH G 5 .   ? 3.288   -16.337 1.336   1.00 34.62  ? 859  HOH A O     1 
HETATM 5032 O  O     . HOH G 5 .   ? -24.501 10.356  27.208  1.00 33.17  ? 860  HOH A O     1 
HETATM 5033 O  O     . HOH G 5 .   ? 17.787  10.448  9.915   1.00 26.85  ? 861  HOH A O     1 
HETATM 5034 O  O     . HOH G 5 .   ? 23.340  4.515   -7.988  1.00 45.81  ? 862  HOH A O     1 
HETATM 5035 O  O     . HOH G 5 .   ? -17.810 -12.303 3.599   1.00 42.05  ? 863  HOH A O     1 
HETATM 5036 O  O     . HOH G 5 .   ? 2.588   -5.275  15.451  1.00 39.30  ? 864  HOH A O     1 
HETATM 5037 O  O     . HOH G 5 .   ? -0.393  0.171   -14.642 1.00 38.06  ? 865  HOH A O     1 
HETATM 5038 O  O     . HOH G 5 .   ? -17.592 2.536   33.072  1.00 42.47  ? 866  HOH A O     1 
HETATM 5039 O  O     . HOH G 5 .   ? -6.430  -11.479 -24.368 1.00 43.21  ? 867  HOH A O     1 
HETATM 5040 O  O     . HOH G 5 .   ? -17.773 -21.369 6.746   1.00 46.35  ? 868  HOH A O     1 
HETATM 5041 O  O     . HOH G 5 .   ? -11.568 -17.873 -4.729  1.00 23.77  ? 869  HOH A O     1 
HETATM 5042 O  O     . HOH G 5 .   ? 8.067   5.845   -10.690 1.00 34.46  ? 870  HOH A O     1 
HETATM 5043 O  O     . HOH G 5 .   ? 5.894   32.995  10.314  1.00 44.41  ? 871  HOH A O     1 
HETATM 5044 O  O     . HOH G 5 .   ? 3.413   -4.017  11.187  1.00 36.68  ? 872  HOH A O     1 
HETATM 5045 O  O     . HOH G 5 .   ? -4.216  -6.203  20.067  1.00 34.67  ? 873  HOH A O     1 
HETATM 5046 O  O     . HOH G 5 .   ? 2.969   -21.577 -6.106  1.00 26.91  ? 874  HOH A O     1 
HETATM 5047 O  O     . HOH G 5 .   ? 3.265   -6.264  9.587   1.00 26.44  ? 875  HOH A O     1 
HETATM 5048 O  O     . HOH G 5 .   ? -18.403 -14.541 5.601   1.00 42.74  ? 876  HOH A O     1 
HETATM 5049 O  O     . HOH G 5 .   ? 8.477   -9.165  -0.342  1.00 30.20  ? 877  HOH A O     1 
HETATM 5050 O  O     . HOH G 5 .   ? -3.618  -13.713 6.117   1.00 26.24  ? 878  HOH A O     1 
HETATM 5051 O  O     . HOH G 5 .   ? 0.856   36.656  27.914  1.00 44.27  ? 879  HOH A O     1 
HETATM 5052 O  O     . HOH G 5 .   ? -23.491 4.333   14.980  1.00 20.70  ? 880  HOH A O     1 
HETATM 5053 O  O     . HOH G 5 .   ? 24.809  17.027  6.325   1.00 34.86  ? 881  HOH A O     1 
HETATM 5054 O  O     . HOH G 5 .   ? -7.055  -28.034 14.850  1.00 35.86  ? 882  HOH A O     1 
HETATM 5055 O  O     . HOH G 5 .   ? -11.206 5.442   -9.502  1.00 45.41  ? 883  HOH A O     1 
HETATM 5056 O  O     . HOH G 5 .   ? 9.965   10.397  10.801  1.00 31.40  ? 884  HOH A O     1 
HETATM 5057 O  O     . HOH G 5 .   ? -16.109 26.156  24.651  1.00 25.46  ? 885  HOH A O     1 
HETATM 5058 O  O     . HOH G 5 .   ? 5.720   22.104  0.013   1.00 35.40  ? 886  HOH A O     1 
HETATM 5059 O  O     . HOH G 5 .   ? -5.778  3.695   28.204  1.00 26.57  ? 887  HOH A O     1 
HETATM 5060 O  O     . HOH G 5 .   ? -4.999  -4.524  14.668  1.00 20.10  ? 888  HOH A O     1 
HETATM 5061 O  O     . HOH G 5 .   ? 8.853   -24.206 -14.056 1.00 32.34  ? 889  HOH A O     1 
HETATM 5062 O  O     . HOH G 5 .   ? 8.434   -7.668  -15.365 1.00 44.37  ? 890  HOH A O     1 
HETATM 5063 O  O     . HOH G 5 .   ? 10.413  2.675   3.155   1.00 31.50  ? 891  HOH A O     1 
HETATM 5064 O  O     . HOH G 5 .   ? 16.583  24.279  16.938  1.00 49.15  ? 892  HOH A O     1 
HETATM 5065 O  O     . HOH G 5 .   ? -4.413  -4.005  9.359   1.00 24.94  ? 893  HOH A O     1 
HETATM 5066 O  O     . HOH G 5 .   ? -15.063 -26.017 9.491   1.00 35.50  ? 894  HOH A O     1 
HETATM 5067 O  O     . HOH G 5 .   ? -20.599 -0.581  19.190  1.00 33.86  ? 895  HOH A O     1 
HETATM 5068 O  O     . HOH G 5 .   ? 15.710  -17.386 -9.879  1.00 38.36  ? 896  HOH A O     1 
HETATM 5069 O  O     . HOH G 5 .   ? 7.204   -20.340 13.269  1.00 41.63  ? 897  HOH A O     1 
HETATM 5070 O  O     . HOH G 5 .   ? 0.504   16.458  20.918  1.00 18.73  ? 898  HOH A O     1 
HETATM 5071 O  O     . HOH G 5 .   ? 15.177  -20.546 -11.484 1.00 36.55  ? 899  HOH A O     1 
HETATM 5072 O  O     . HOH G 5 .   ? -0.877  10.714  21.825  1.00 21.09  ? 900  HOH A O     1 
HETATM 5073 O  O     . HOH G 5 .   ? 8.975   16.842  25.172  1.00 30.11  ? 901  HOH A O     1 
HETATM 5074 O  O     . HOH G 5 .   ? -3.111  9.121   7.851   1.00 14.25  ? 902  HOH A O     1 
HETATM 5075 O  O     . HOH G 5 .   ? -3.017  11.031  1.222   1.00 23.40  ? 903  HOH A O     1 
HETATM 5076 O  O     . HOH G 5 .   ? 14.801  20.433  1.118   1.00 27.38  ? 904  HOH A O     1 
HETATM 5077 O  O     . HOH G 5 .   ? 0.163   -4.337  19.229  1.00 25.92  ? 905  HOH A O     1 
HETATM 5078 O  O     . HOH G 5 .   ? 2.603   18.621  29.897  1.00 30.17  ? 906  HOH A O     1 
HETATM 5079 O  O     . HOH G 5 .   ? -14.593 -1.912  23.195  1.00 27.85  ? 907  HOH A O     1 
HETATM 5080 O  O     . HOH G 5 .   ? 6.300   14.413  -5.302  1.00 38.87  ? 908  HOH A O     1 
HETATM 5081 O  O     . HOH G 5 .   ? 11.809  -20.897 5.179   1.00 33.67  ? 909  HOH A O     1 
HETATM 5082 O  O     . HOH G 5 .   ? -6.084  -4.186  11.390  1.00 25.43  ? 910  HOH A O     1 
HETATM 5083 O  O     . HOH G 5 .   ? 6.839   9.480   -5.476  1.00 26.07  ? 911  HOH A O     1 
HETATM 5084 O  O     . HOH G 5 .   ? 20.953  15.192  3.755   1.00 34.53  ? 912  HOH A O     1 
HETATM 5085 O  O     . HOH G 5 .   ? -12.004 -24.791 11.149  1.00 29.11  ? 913  HOH A O     1 
HETATM 5086 O  O     . HOH G 5 .   ? 2.527   -12.322 21.878  1.00 30.35  ? 914  HOH A O     1 
HETATM 5087 O  O     . HOH G 5 .   ? -3.661  10.186  -12.378 1.00 42.74  ? 915  HOH A O     1 
HETATM 5088 O  O     . HOH G 5 .   ? 21.614  -7.424  -11.537 1.00 32.59  ? 916  HOH A O     1 
HETATM 5089 O  O     . HOH G 5 .   ? 4.053   2.343   15.870  1.00 38.93  ? 917  HOH A O     1 
HETATM 5090 O  O     . HOH G 5 .   ? 10.052  14.880  23.762  1.00 43.06  ? 918  HOH A O     1 
HETATM 5091 O  O     . HOH G 5 .   ? 2.686   4.297   11.309  1.00 28.31  ? 919  HOH A O     1 
HETATM 5092 O  O     . HOH G 5 .   ? -18.389 27.508  31.407  1.00 38.70  ? 920  HOH A O     1 
HETATM 5093 O  O     . HOH G 5 .   ? -5.450  -1.230  11.818  1.00 22.05  ? 921  HOH A O     1 
HETATM 5094 O  O     . HOH G 5 .   ? -18.006 12.536  28.010  1.00 26.71  ? 922  HOH A O     1 
HETATM 5095 O  O     . HOH G 5 .   ? -2.187  19.212  -4.196  1.00 40.66  ? 923  HOH A O     1 
HETATM 5096 O  O     . HOH G 5 .   ? -10.700 2.471   7.366   1.00 21.21  ? 924  HOH A O     1 
HETATM 5097 O  O     . HOH G 5 .   ? -14.972 -4.525  20.547  1.00 20.76  ? 925  HOH A O     1 
HETATM 5098 O  O     . HOH G 5 .   ? -13.237 -1.406  -21.531 1.00 53.26  ? 926  HOH A O     1 
HETATM 5099 O  O     . HOH G 5 .   ? -20.590 -3.106  20.624  1.00 30.75  ? 927  HOH A O     1 
HETATM 5100 O  O     . HOH G 5 .   ? 17.277  7.808   9.351   1.00 32.32  ? 928  HOH A O     1 
HETATM 5101 O  O     . HOH G 5 .   ? 15.856  7.097   3.659   1.00 34.37  ? 929  HOH A O     1 
HETATM 5102 O  O     . HOH G 5 .   ? 8.223   28.530  23.977  1.00 35.38  ? 930  HOH A O     1 
HETATM 5103 O  O     . HOH G 5 .   ? 0.301   16.954  -8.305  1.00 47.72  ? 931  HOH A O     1 
HETATM 5104 O  O     . HOH G 5 .   ? -8.050  2.589   20.674  1.00 25.07  ? 932  HOH A O     1 
HETATM 5105 O  O     . HOH G 5 .   ? -21.498 -1.184  -3.362  1.00 40.84  ? 933  HOH A O     1 
HETATM 5106 O  O     . HOH G 5 .   ? 1.695   11.989  33.211  1.00 41.30  ? 934  HOH A O     1 
HETATM 5107 O  O     . HOH G 5 .   ? 4.315   16.056  19.398  1.00 18.21  ? 935  HOH A O     1 
HETATM 5108 O  O     . HOH G 5 .   ? -24.156 -2.447  12.451  1.00 30.90  ? 936  HOH A O     1 
HETATM 5109 O  O     . HOH G 5 .   ? 6.935   -3.103  3.242   1.00 24.68  ? 937  HOH A O     1 
HETATM 5110 O  O     . HOH G 5 .   ? 7.349   0.530   9.786   1.00 42.62  ? 938  HOH A O     1 
HETATM 5111 O  O     . HOH G 5 .   ? -25.658 22.136  15.968  1.00 34.95  ? 939  HOH A O     1 
HETATM 5112 O  O     . HOH G 5 .   ? 17.370  -7.315  -0.351  1.00 35.07  ? 940  HOH A O     1 
HETATM 5113 O  O     . HOH G 5 .   ? 17.405  12.921  -7.648  1.00 40.71  ? 941  HOH A O     1 
HETATM 5114 O  O     . HOH G 5 .   ? 0.869   -4.095  1.033   1.00 17.66  ? 942  HOH A O     1 
HETATM 5115 O  O     . HOH G 5 .   ? -4.002  14.462  23.000  1.00 18.43  ? 943  HOH A O     1 
HETATM 5116 O  O     . HOH G 5 .   ? -16.522 2.332   2.668   1.00 25.73  ? 944  HOH A O     1 
HETATM 5117 O  O     . HOH G 5 .   ? 3.472   -27.131 -17.070 1.00 39.63  ? 945  HOH A O     1 
HETATM 5118 O  O     . HOH G 5 .   ? -10.759 16.220  -1.977  1.00 30.75  ? 946  HOH A O     1 
HETATM 5119 O  O     . HOH G 5 .   ? 0.322   19.969  19.324  1.00 25.58  ? 947  HOH A O     1 
HETATM 5120 O  O     . HOH G 5 .   ? -1.951  12.382  -0.853  1.00 18.67  ? 948  HOH A O     1 
HETATM 5121 O  O     . HOH G 5 .   ? -18.703 18.335  24.059  1.00 23.01  ? 949  HOH A O     1 
HETATM 5122 O  O     . HOH G 5 .   ? -15.771 -1.089  1.481   1.00 27.66  ? 950  HOH A O     1 
HETATM 5123 O  O     . HOH G 5 .   ? -11.631 -4.356  -1.446  1.00 21.35  ? 951  HOH A O     1 
HETATM 5124 O  O     . HOH G 5 .   ? -20.005 18.788  10.895  1.00 27.16  ? 952  HOH A O     1 
HETATM 5125 O  O     . HOH G 5 .   ? -23.775 11.095  9.550   1.00 25.89  ? 953  HOH A O     1 
HETATM 5126 O  O     . HOH G 5 .   ? -18.943 3.802   2.143   1.00 25.58  ? 954  HOH A O     1 
HETATM 5127 O  O     . HOH G 5 .   ? 1.130   -12.412 6.914   1.00 21.53  ? 955  HOH A O     1 
HETATM 5128 O  O     . HOH G 5 .   ? 0.927   16.068  17.447  1.00 19.48  ? 956  HOH A O     1 
HETATM 5129 O  O     . HOH G 5 .   ? 15.368  -21.866 -4.089  1.00 37.57  ? 957  HOH A O     1 
HETATM 5130 O  O     . HOH G 5 .   ? -11.283 -14.993 -13.556 1.00 33.81  ? 958  HOH A O     1 
HETATM 5131 O  O     . HOH G 5 .   ? -0.797  28.744  9.636   1.00 26.44  ? 959  HOH A O     1 
HETATM 5132 O  O     . HOH G 5 .   ? -18.443 -6.991  -12.992 1.00 44.73  ? 960  HOH A O     1 
HETATM 5133 O  O     . HOH G 5 .   ? -4.655  26.162  4.318   1.00 34.66  ? 961  HOH A O     1 
HETATM 5134 O  O     . HOH G 5 .   ? -17.266 19.052  11.623  1.00 25.36  ? 962  HOH A O     1 
HETATM 5135 O  O     . HOH G 5 .   ? -12.509 -28.132 24.761  1.00 44.42  ? 963  HOH A O     1 
HETATM 5136 O  O     . HOH G 5 .   ? -17.121 16.782  5.647   1.00 32.69  ? 964  HOH A O     1 
HETATM 5137 O  O     . HOH G 5 .   ? 0.041   26.704  16.414  1.00 23.99  ? 965  HOH A O     1 
HETATM 5138 O  O     . HOH G 5 .   ? 1.325   12.400  18.838  1.00 22.61  ? 966  HOH A O     1 
HETATM 5139 O  O     . HOH G 5 .   ? -9.858  -16.646 -17.571 1.00 40.46  ? 967  HOH A O     1 
HETATM 5140 O  O     . HOH G 5 .   ? 9.544   -18.815 -5.694  1.00 23.67  ? 968  HOH A O     1 
HETATM 5141 O  O     . HOH G 5 .   ? -3.511  7.550   22.021  1.00 22.25  ? 969  HOH A O     1 
HETATM 5142 O  O     . HOH G 5 .   ? -27.698 5.056   13.869  1.00 37.30  ? 970  HOH A O     1 
HETATM 5143 O  O     . HOH G 5 .   ? -7.921  -6.259  18.499  1.00 22.20  ? 971  HOH A O     1 
HETATM 5144 O  O     . HOH G 5 .   ? 5.549   4.030   28.515  1.00 42.22  ? 972  HOH A O     1 
HETATM 5145 O  O     . HOH G 5 .   ? 10.442  -10.870 15.670  1.00 40.33  ? 973  HOH A O     1 
HETATM 5146 O  O     . HOH G 5 .   ? -24.328 15.349  11.305  1.00 38.00  ? 974  HOH A O     1 
HETATM 5147 O  O     . HOH G 5 .   ? -18.744 15.259  27.005  1.00 31.98  ? 975  HOH A O     1 
HETATM 5148 O  O     . HOH G 5 .   ? -1.578  -24.666 -8.248  1.00 33.16  ? 976  HOH A O     1 
HETATM 5149 O  O     . HOH G 5 .   ? 2.635   14.117  20.438  1.00 20.79  ? 977  HOH A O     1 
HETATM 5150 O  O     . HOH G 5 .   ? 15.483  -18.941 1.626   1.00 47.96  ? 978  HOH A O     1 
HETATM 5151 O  O     . HOH G 5 .   ? -13.860 -2.665  25.738  1.00 33.26  ? 979  HOH A O     1 
HETATM 5152 O  O     . HOH G 5 .   ? -23.897 1.585   24.839  1.00 34.15  ? 980  HOH A O     1 
HETATM 5153 O  O     . HOH G 5 .   ? -16.165 21.603  11.326  1.00 42.61  ? 981  HOH A O     1 
HETATM 5154 O  O     . HOH G 5 .   ? 17.044  15.555  19.558  1.00 24.54  ? 982  HOH A O     1 
HETATM 5155 O  O     . HOH G 5 .   ? -7.288  -4.170  8.063   1.00 18.20  ? 983  HOH A O     1 
HETATM 5156 O  O     . HOH G 5 .   ? 6.824   4.967   1.931   1.00 26.25  ? 984  HOH A O     1 
HETATM 5157 O  O     . HOH G 5 .   ? -1.454  -29.274 7.289   1.00 35.30  ? 985  HOH A O     1 
HETATM 5158 O  O     . HOH G 5 .   ? -11.921 -22.658 28.511  1.00 46.90  ? 986  HOH A O     1 
HETATM 5159 O  O     . HOH G 5 .   ? -6.504  -6.255  15.975  1.00 23.43  ? 987  HOH A O     1 
HETATM 5160 O  O     . HOH G 5 .   ? -10.537 -17.978 -14.233 1.00 29.50  ? 988  HOH A O     1 
HETATM 5161 O  O     . HOH G 5 .   ? -22.701 -0.560  24.362  1.00 40.86  ? 989  HOH A O     1 
HETATM 5162 O  O     . HOH G 5 .   ? -14.020 -13.697 -3.967  1.00 28.09  ? 990  HOH A O     1 
HETATM 5163 O  O     . HOH G 5 .   ? -26.590 -2.117  4.276   1.00 39.43  ? 991  HOH A O     1 
HETATM 5164 O  O     . HOH G 5 .   ? -13.984 17.418  31.995  1.00 38.35  ? 992  HOH A O     1 
HETATM 5165 O  O     . HOH G 5 .   ? -24.669 -3.688  8.907   1.00 37.02  ? 993  HOH A O     1 
HETATM 5166 O  O     . HOH G 5 .   ? -3.878  5.966   19.792  1.00 23.70  ? 994  HOH A O     1 
HETATM 5167 O  O     . HOH G 5 .   ? -1.667  -27.872 20.801  1.00 39.86  ? 995  HOH A O     1 
HETATM 5168 O  O     . HOH G 5 .   ? -6.605  -4.144  -21.921 1.00 42.72  ? 996  HOH A O     1 
HETATM 5169 O  O     . HOH G 5 .   ? 0.333   -25.205 15.844  1.00 33.61  ? 997  HOH A O     1 
HETATM 5170 O  O     . HOH G 5 .   ? -23.042 -1.128  2.616   1.00 34.16  ? 998  HOH A O     1 
HETATM 5171 O  O     . HOH G 5 .   ? 1.793   -7.610  20.568  1.00 30.86  ? 999  HOH A O     1 
HETATM 5172 O  O     . HOH G 5 .   ? 12.298  24.204  6.859   1.00 39.53  ? 1000 HOH A O     1 
HETATM 5173 O  O     . HOH G 5 .   ? 11.127  25.814  22.948  1.00 36.55  ? 1001 HOH A O     1 
HETATM 5174 O  O     . HOH G 5 .   ? 11.016  -13.391 14.891  1.00 39.05  ? 1002 HOH A O     1 
HETATM 5175 O  O     . HOH G 5 .   ? -12.760 -15.257 1.674   1.00 35.67  ? 1003 HOH A O     1 
HETATM 5176 O  O     . HOH G 5 .   ? 5.617   11.362  26.122  1.00 24.64  ? 1004 HOH A O     1 
HETATM 5177 O  O     . HOH G 5 .   ? -2.309  28.948  15.956  1.00 34.10  ? 1005 HOH A O     1 
HETATM 5178 O  O     . HOH G 5 .   ? 18.277  10.745  2.750   1.00 37.42  ? 1006 HOH A O     1 
HETATM 5179 O  O     . HOH G 5 .   ? -3.649  -14.143 8.883   1.00 18.40  ? 1007 HOH A O     1 
HETATM 5180 O  O     . HOH G 5 .   ? 8.049   1.494   4.495   1.00 24.22  ? 1008 HOH A O     1 
HETATM 5181 O  O     . HOH G 5 .   ? 8.243   8.528   0.233   1.00 28.06  ? 1009 HOH A O     1 
HETATM 5182 O  O     . HOH G 5 .   ? -2.032  21.959  33.685  1.00 42.13  ? 1010 HOH A O     1 
HETATM 5183 O  O     . HOH G 5 .   ? 15.709  7.183   -11.113 1.00 37.16  ? 1011 HOH A O     1 
HETATM 5184 O  O     . HOH G 5 .   ? 14.731  -9.431  5.374   1.00 42.61  ? 1012 HOH A O     1 
HETATM 5185 O  O     . HOH G 5 .   ? 16.915  11.912  11.981  1.00 29.24  ? 1013 HOH A O     1 
HETATM 5186 O  O     . HOH G 5 .   ? 4.853   -20.147 -2.358  1.00 37.69  ? 1014 HOH A O     1 
HETATM 5187 O  O     . HOH G 5 .   ? 3.406   14.017  32.274  1.00 33.47  ? 1015 HOH A O     1 
HETATM 5188 O  O     . HOH G 5 .   ? 13.999  2.484   25.923  1.00 49.16  ? 1016 HOH A O     1 
HETATM 5189 O  O     . HOH G 5 .   ? 11.774  9.707   14.561  1.00 26.64  ? 1017 HOH A O     1 
HETATM 5190 O  O     . HOH G 5 .   ? -8.026  -21.899 -21.500 1.00 37.01  ? 1018 HOH A O     1 
HETATM 5191 O  O     . HOH G 5 .   ? 5.340   -17.938 2.130   1.00 29.63  ? 1019 HOH A O     1 
HETATM 5192 O  O     . HOH G 5 .   ? -7.309  -3.733  -19.366 1.00 39.91  ? 1020 HOH A O     1 
HETATM 5193 O  O     . HOH G 5 .   ? 17.395  20.334  12.517  1.00 29.80  ? 1021 HOH A O     1 
HETATM 5194 O  O     . HOH G 5 .   ? -13.794 -22.645 -9.867  1.00 41.47  ? 1022 HOH A O     1 
HETATM 5195 O  O     . HOH G 5 .   ? -9.534  3.874   -12.209 1.00 41.28  ? 1023 HOH A O     1 
HETATM 5196 O  O     . HOH G 5 .   ? -13.086 -11.490 -2.621  1.00 24.56  ? 1024 HOH A O     1 
HETATM 5197 O  O     . HOH G 5 .   ? -0.844  24.467  0.128   1.00 34.13  ? 1025 HOH A O     1 
HETATM 5198 O  O     . HOH G 5 .   ? -15.874 -19.612 2.586   1.00 46.40  ? 1026 HOH A O     1 
HETATM 5199 O  O     . HOH G 5 .   ? 4.560   -2.442  2.727   1.00 19.72  ? 1027 HOH A O     1 
HETATM 5200 O  O     . HOH G 5 .   ? -0.671  22.392  19.619  1.00 25.99  ? 1028 HOH A O     1 
HETATM 5201 O  O     . HOH G 5 .   ? 5.265   -21.577 1.991   1.00 35.12  ? 1029 HOH A O     1 
HETATM 5202 O  O     . HOH G 5 .   ? -9.867  26.645  9.855   1.00 31.58  ? 1030 HOH A O     1 
HETATM 5203 O  O     . HOH G 5 .   ? 4.271   24.807  33.802  1.00 36.67  ? 1031 HOH A O     1 
HETATM 5204 O  O     . HOH G 5 .   ? -6.565  -4.936  1.568   1.00 17.94  ? 1032 HOH A O     1 
HETATM 5205 O  O     . HOH G 5 .   ? -18.752 -18.917 -5.215  1.00 40.02  ? 1033 HOH A O     1 
HETATM 5206 O  O     . HOH G 5 .   ? 20.655  -6.340  -5.193  1.00 39.62  ? 1034 HOH A O     1 
HETATM 5207 O  O     . HOH G 5 .   ? -10.513 21.624  14.352  1.00 23.27  ? 1035 HOH A O     1 
HETATM 5208 O  O     . HOH G 5 .   ? 15.199  20.497  -2.610  1.00 47.51  ? 1036 HOH A O     1 
HETATM 5209 O  O     . HOH G 5 .   ? -12.866 24.534  33.297  1.00 46.55  ? 1037 HOH A O     1 
HETATM 5210 O  O     . HOH G 5 .   ? -16.285 -8.989  3.684   1.00 23.96  ? 1038 HOH A O     1 
HETATM 5211 O  O     . HOH G 5 .   ? 15.924  15.265  -6.419  1.00 29.88  ? 1039 HOH A O     1 
HETATM 5212 O  O     . HOH G 5 .   ? -27.454 5.043   19.790  1.00 32.11  ? 1040 HOH A O     1 
HETATM 5213 O  O     . HOH G 5 .   ? 7.421   32.593  17.853  1.00 39.46  ? 1041 HOH A O     1 
HETATM 5214 O  O     . HOH G 5 .   ? -8.184  -23.626 -6.406  1.00 30.50  ? 1042 HOH A O     1 
HETATM 5215 O  O     . HOH G 5 .   ? -2.066  -32.969 13.350  1.00 54.79  ? 1043 HOH A O     1 
HETATM 5216 O  O     . HOH G 5 .   ? -0.512  31.374  26.230  1.00 37.12  ? 1044 HOH A O     1 
HETATM 5217 O  O     . HOH G 5 .   ? -16.594 -13.062 -9.638  1.00 41.05  ? 1045 HOH A O     1 
HETATM 5218 O  O     . HOH G 5 .   ? -11.342 -26.963 1.872   1.00 43.33  ? 1046 HOH A O     1 
HETATM 5219 O  O     . HOH G 5 .   ? -13.904 -10.816 3.044   1.00 20.55  ? 1047 HOH A O     1 
HETATM 5220 O  O     . HOH G 5 .   ? 9.837   5.834   -0.204  1.00 31.22  ? 1048 HOH A O     1 
HETATM 5221 O  O     . HOH G 5 .   ? 8.183   11.671  1.833   1.00 21.41  ? 1049 HOH A O     1 
HETATM 5222 O  O     . HOH G 5 .   ? -10.664 2.349   21.950  1.00 29.47  ? 1050 HOH A O     1 
HETATM 5223 O  O     . HOH G 5 .   ? 4.084   5.892   -4.545  1.00 26.71  ? 1051 HOH A O     1 
HETATM 5224 O  O     . HOH G 5 .   ? 4.895   -27.793 -20.816 1.00 43.43  ? 1052 HOH A O     1 
HETATM 5225 O  O     . HOH G 5 .   ? -7.874  -23.791 -18.377 1.00 43.15  ? 1053 HOH A O     1 
HETATM 5226 O  O     . HOH G 5 .   ? -12.720 -16.616 4.361   1.00 30.49  ? 1054 HOH A O     1 
HETATM 5227 O  O     . HOH G 5 .   ? 7.069   -0.727  5.204   1.00 25.56  ? 1055 HOH A O     1 
HETATM 5228 O  O     . HOH G 5 .   ? -11.023 -2.581  6.976   1.00 23.01  ? 1056 HOH A O     1 
HETATM 5229 O  O     . HOH G 5 .   ? -4.077  29.833  23.741  1.00 38.20  ? 1057 HOH A O     1 
HETATM 5230 O  O     . HOH G 5 .   ? 11.519  -12.602 4.138   1.00 33.49  ? 1058 HOH A O     1 
HETATM 5231 O  O     . HOH G 5 .   ? 0.420   -1.141  25.904  1.00 36.73  ? 1059 HOH A O     1 
HETATM 5232 O  O     . HOH G 5 .   ? 19.324  20.307  10.219  1.00 38.29  ? 1060 HOH A O     1 
HETATM 5233 O  O     . HOH G 5 .   ? -4.930  30.435  6.323   1.00 48.26  ? 1061 HOH A O     1 
HETATM 5234 O  O     . HOH G 5 .   ? 10.280  -9.967  9.272   1.00 31.27  ? 1062 HOH A O     1 
HETATM 5235 O  O     . HOH G 5 .   ? 0.847   -22.633 16.639  1.00 26.87  ? 1063 HOH A O     1 
HETATM 5236 O  O     . HOH G 5 .   ? 2.675   4.713   27.343  1.00 39.68  ? 1064 HOH A O     1 
HETATM 5237 O  O     . HOH G 5 .   ? -23.469 19.071  13.658  1.00 28.68  ? 1065 HOH A O     1 
HETATM 5238 O  O     . HOH G 5 .   ? 9.637   31.383  28.449  1.00 46.88  ? 1066 HOH A O     1 
HETATM 5239 O  O     . HOH G 5 .   ? -5.828  -4.930  22.155  1.00 34.06  ? 1067 HOH A O     1 
HETATM 5240 O  O     . HOH G 5 .   ? 11.417  -6.099  -5.545  1.00 33.22  ? 1068 HOH A O     1 
HETATM 5241 O  O     . HOH G 5 .   ? -11.630 -0.569  22.498  1.00 40.79  ? 1069 HOH A O     1 
HETATM 5242 O  O     . HOH G 5 .   ? 4.022   -12.585 13.221  1.00 26.92  ? 1070 HOH A O     1 
HETATM 5243 O  O     . HOH G 5 .   ? 8.173   -24.863 -1.227  1.00 42.36  ? 1071 HOH A O     1 
HETATM 5244 O  O     . HOH G 5 .   ? -24.141 13.841  25.084  1.00 38.48  ? 1072 HOH A O     1 
HETATM 5245 O  O     . HOH G 5 .   ? 19.494  22.657  2.644   1.00 43.02  ? 1073 HOH A O     1 
HETATM 5246 O  O     . HOH G 5 .   ? -25.397 14.366  13.161  1.00 32.17  ? 1074 HOH A O     1 
HETATM 5247 O  O     . HOH G 5 .   ? 15.782  8.327   0.493   1.00 38.66  ? 1075 HOH A O     1 
HETATM 5248 O  O     . HOH G 5 .   ? -14.078 -12.776 1.305   1.00 28.37  ? 1076 HOH A O     1 
HETATM 5249 O  O     . HOH G 5 .   ? -9.160  3.514   -16.718 1.00 47.29  ? 1077 HOH A O     1 
HETATM 5250 O  O     . HOH G 5 .   ? -1.291  32.044  18.756  1.00 30.45  ? 1078 HOH A O     1 
HETATM 5251 O  O     . HOH G 5 .   ? -1.091  24.748  32.583  1.00 51.23  ? 1079 HOH A O     1 
HETATM 5252 O  O     . HOH G 5 .   ? -16.405 -14.663 -7.787  1.00 45.21  ? 1080 HOH A O     1 
HETATM 5253 O  O     . HOH G 5 .   ? 5.316   1.001   11.700  1.00 38.76  ? 1081 HOH A O     1 
HETATM 5254 O  O     . HOH G 5 .   ? 12.311  -10.760 5.875   1.00 38.18  ? 1082 HOH A O     1 
HETATM 5255 O  O     . HOH G 5 .   ? -17.719 10.011  -3.247  1.00 50.60  ? 1083 HOH A O     1 
HETATM 5256 O  O     . HOH G 5 .   ? 3.211   -23.126 -23.108 1.00 45.27  ? 1084 HOH A O     1 
HETATM 5257 O  O     . HOH G 5 .   ? -6.545  3.491   34.933  1.00 40.27  ? 1085 HOH A O     1 
HETATM 5258 O  O     . HOH G 5 .   ? -11.496 -11.875 28.422  1.00 44.80  ? 1086 HOH A O     1 
HETATM 5259 O  O     . HOH G 5 .   ? 6.816   -28.871 -9.070  1.00 47.76  ? 1087 HOH A O     1 
HETATM 5260 O  O     . HOH G 5 .   ? 7.790   11.379  -10.276 1.00 38.93  ? 1088 HOH A O     1 
HETATM 5261 O  O     . HOH G 5 .   ? -2.599  34.983  7.190   1.00 35.55  ? 1089 HOH A O     1 
HETATM 5262 O  O     . HOH G 5 .   ? -10.154 -30.115 5.636   1.00 43.05  ? 1090 HOH A O     1 
HETATM 5263 O  O     . HOH G 5 .   ? -24.818 -3.496  15.120  1.00 43.10  ? 1091 HOH A O     1 
HETATM 5264 O  O     . HOH G 5 .   ? -0.609  -34.557 1.466   1.00 39.16  ? 1092 HOH A O     1 
HETATM 5265 O  O     . HOH G 5 .   ? -23.593 24.879  24.586  1.00 37.87  ? 1093 HOH A O     1 
HETATM 5266 O  O     . HOH G 5 .   ? 17.784  16.029  22.280  1.00 33.89  ? 1094 HOH A O     1 
HETATM 5267 O  O     . HOH G 5 .   ? 1.503   -3.286  21.349  1.00 38.02  ? 1095 HOH A O     1 
HETATM 5268 O  O     . HOH G 5 .   ? -7.137  1.253   -11.428 1.00 36.88  ? 1096 HOH A O     1 
HETATM 5269 O  O     . HOH G 5 .   ? -22.382 14.839  23.051  1.00 32.54  ? 1097 HOH A O     1 
HETATM 5270 O  O     . HOH G 5 .   ? -21.561 20.776  12.419  1.00 37.98  ? 1098 HOH A O     1 
HETATM 5271 O  O     . HOH G 5 .   ? 1.969   -33.258 -0.989  1.00 47.32  ? 1099 HOH A O     1 
HETATM 5272 O  O     . HOH G 5 .   ? -5.152  -20.135 -22.142 1.00 38.28  ? 1100 HOH A O     1 
HETATM 5273 O  O     . HOH G 5 .   ? 5.653   -30.669 3.441   1.00 48.93  ? 1101 HOH A O     1 
HETATM 5274 O  O     . HOH G 5 .   ? 16.050  16.424  13.572  1.00 30.85  ? 1102 HOH A O     1 
HETATM 5275 O  O     . HOH G 5 .   ? -24.930 9.503   0.930   1.00 47.33  ? 1103 HOH A O     1 
HETATM 5276 O  O     . HOH G 5 .   ? -2.665  0.196   -16.660 1.00 43.39  ? 1104 HOH A O     1 
HETATM 5277 O  O     . HOH G 5 .   ? -11.454 -0.351  30.068  1.00 33.32  ? 1105 HOH A O     1 
HETATM 5278 O  O     . HOH G 5 .   ? 17.970  5.378   3.756   1.00 41.59  ? 1106 HOH A O     1 
HETATM 5279 O  O     . HOH G 5 .   ? -7.475  21.155  32.579  1.00 47.40  ? 1107 HOH A O     1 
HETATM 5280 O  O     . HOH G 5 .   ? -1.869  -1.171  26.904  1.00 39.67  ? 1108 HOH A O     1 
HETATM 5281 O  O     . HOH G 5 .   ? -4.557  -6.337  0.135   1.00 22.25  ? 1109 HOH A O     1 
HETATM 5282 O  O     . HOH G 5 .   ? 4.739   -26.436 -6.518  1.00 41.61  ? 1110 HOH A O     1 
HETATM 5283 O  O     . HOH G 5 .   ? 19.451  12.332  -5.825  1.00 41.84  ? 1111 HOH A O     1 
HETATM 5284 O  O     . HOH G 5 .   ? 7.775   -4.136  -15.819 1.00 43.82  ? 1112 HOH A O     1 
HETATM 5285 O  O     . HOH G 5 .   ? -20.177 16.958  25.666  1.00 36.70  ? 1113 HOH A O     1 
HETATM 5286 O  O     . HOH G 5 .   ? 8.638   12.676  25.890  1.00 30.62  ? 1114 HOH A O     1 
HETATM 5287 O  O     . HOH G 5 .   ? 7.993   -25.617 -21.739 1.00 45.26  ? 1115 HOH A O     1 
HETATM 5288 O  O     . HOH G 5 .   ? -10.567 -10.311 -24.568 1.00 48.69  ? 1116 HOH A O     1 
HETATM 5289 O  O     . HOH G 5 .   ? -13.760 -1.040  28.675  1.00 36.45  ? 1117 HOH A O     1 
HETATM 5290 O  O     . HOH G 5 .   ? 4.387   -25.830 -22.959 1.00 50.47  ? 1118 HOH A O     1 
HETATM 5291 O  O     . HOH G 5 .   ? 3.780   17.230  31.967  1.00 40.01  ? 1119 HOH A O     1 
HETATM 5292 O  O     . HOH G 5 .   ? -8.860  -25.163 -17.051 1.00 51.86  ? 1120 HOH A O     1 
HETATM 5293 O  O     . HOH G 5 .   ? 9.123   3.667   1.085   1.00 31.78  ? 1121 HOH A O     1 
HETATM 5294 O  O     . HOH G 5 .   ? 12.369  -2.415  -14.063 1.00 55.47  ? 1122 HOH A O     1 
HETATM 5295 O  O     . HOH G 5 .   ? -18.301 -8.591  1.652   1.00 40.85  ? 1123 HOH A O     1 
HETATM 5296 O  O     . HOH G 5 .   ? 4.679   13.610  -6.933  1.00 47.05  ? 1124 HOH A O     1 
HETATM 5297 O  O     . HOH G 5 .   ? -3.779  -35.404 0.088   1.00 39.89  ? 1125 HOH A O     1 
HETATM 5298 O  O     . HOH G 5 .   ? 16.877  21.505  -0.463  1.00 32.89  ? 1126 HOH A O     1 
HETATM 5299 O  O     . HOH G 5 .   ? -10.365 22.546  12.423  1.00 33.67  ? 1127 HOH A O     1 
HETATM 5300 O  O     . HOH G 5 .   ? 10.237  -3.408  -14.368 1.00 41.50  ? 1128 HOH A O     1 
HETATM 5301 O  O     . HOH G 5 .   ? 2.141   17.744  19.262  1.00 22.17  ? 1129 HOH A O     1 
HETATM 5302 O  O     . HOH G 5 .   ? 4.595   -5.043  -17.491 1.00 38.35  ? 1130 HOH A O     1 
HETATM 5303 O  O     . HOH G 5 .   ? -26.255 13.045  24.013  1.00 37.92  ? 1131 HOH A O     1 
HETATM 5304 O  O     . HOH G 5 .   ? -28.101 19.693  -4.879  1.00 48.02  ? 1132 HOH A O     1 
HETATM 5305 O  O     . HOH G 5 .   ? 5.225   14.152  -9.220  1.00 49.12  ? 1133 HOH A O     1 
HETATM 5306 O  O     . HOH G 5 .   ? 21.328  21.872  10.106  1.00 48.89  ? 1134 HOH A O     1 
HETATM 5307 O  O     . HOH G 5 .   ? 13.718  -13.603 -19.242 1.00 48.62  ? 1135 HOH A O     1 
HETATM 5308 O  O     . HOH G 5 .   ? -4.350  30.545  26.686  1.00 51.83  ? 1136 HOH A O     1 
HETATM 5309 O  O     . HOH G 5 .   ? -25.914 19.890  14.531  1.00 29.24  ? 1137 HOH A O     1 
HETATM 5310 O  O     . HOH G 5 .   ? -3.005  -2.633  28.890  1.00 47.07  ? 1138 HOH A O     1 
HETATM 5311 O  O     . HOH G 5 .   ? 25.083  19.192  8.210   1.00 39.81  ? 1139 HOH A O     1 
HETATM 5312 O  O     . HOH G 5 .   ? 12.253  25.355  9.386   1.00 40.20  ? 1140 HOH A O     1 
HETATM 5313 O  O     . HOH G 5 .   ? -2.749  -35.262 2.135   1.00 38.42  ? 1141 HOH A O     1 
HETATM 5314 O  O     . HOH G 5 .   ? -28.669 3.574   17.963  1.00 44.32  ? 1142 HOH A O     1 
HETATM 5315 O  O     . HOH G 5 .   ? 2.508   -9.688  22.633  1.00 32.90  ? 1143 HOH A O     1 
HETATM 5316 O  O     . HOH G 5 .   ? -1.136  -9.970  -30.766 1.00 57.10  ? 1144 HOH A O     1 
# 
