data_9EJ5
# 
_entry.id   9EJ5 
# 
_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   9EJ5         pdb_00009ej5 10.2210/pdb9ej5/pdb 
WWPDB D_1000290514 ?            ?                   
# 
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                        9EJ5 
_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    220 ?        ? ? ? 
# 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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  198 HOH HOH A . 
G 5 HOH 2   802  177 HOH HOH A . 
G 5 HOH 3   803  82  HOH HOH A . 
G 5 HOH 4   804  67  HOH HOH A . 
G 5 HOH 5   805  111 HOH HOH A . 
G 5 HOH 6   806  36  HOH HOH A . 
G 5 HOH 7   807  80  HOH HOH A . 
G 5 HOH 8   808  147 HOH HOH A . 
G 5 HOH 9   809  172 HOH HOH A . 
G 5 HOH 10  810  161 HOH HOH A . 
G 5 HOH 11  811  63  HOH HOH A . 
G 5 HOH 12  812  62  HOH HOH A . 
G 5 HOH 13  813  206 HOH HOH A . 
G 5 HOH 14  814  215 HOH HOH A . 
G 5 HOH 15  815  96  HOH HOH A . 
G 5 HOH 16  816  181 HOH HOH A . 
G 5 HOH 17  817  207 HOH HOH A . 
G 5 HOH 18  818  112 HOH HOH A . 
G 5 HOH 19  819  129 HOH HOH A . 
G 5 HOH 20  820  30  HOH HOH A . 
G 5 HOH 21  821  165 HOH HOH A . 
G 5 HOH 22  822  89  HOH HOH A . 
G 5 HOH 23  823  49  HOH HOH A . 
G 5 HOH 24  824  97  HOH HOH A . 
G 5 HOH 25  825  151 HOH HOH A . 
G 5 HOH 26  826  115 HOH HOH A . 
G 5 HOH 27  827  156 HOH HOH A . 
G 5 HOH 28  828  7   HOH HOH A . 
G 5 HOH 29  829  72  HOH HOH A . 
G 5 HOH 30  830  108 HOH HOH A . 
G 5 HOH 31  831  86  HOH HOH A . 
G 5 HOH 32  832  217 HOH HOH A . 
G 5 HOH 33  833  46  HOH HOH A . 
G 5 HOH 34  834  167 HOH HOH A . 
G 5 HOH 35  835  22  HOH HOH A . 
G 5 HOH 36  836  105 HOH HOH A . 
G 5 HOH 37  837  14  HOH HOH A . 
G 5 HOH 38  838  121 HOH HOH A . 
G 5 HOH 39  839  1   HOH HOH A . 
G 5 HOH 40  840  32  HOH HOH A . 
G 5 HOH 41  841  150 HOH HOH A . 
G 5 HOH 42  842  15  HOH HOH A . 
G 5 HOH 43  843  59  HOH HOH A . 
G 5 HOH 44  844  6   HOH HOH A . 
G 5 HOH 45  845  103 HOH HOH A . 
G 5 HOH 46  846  144 HOH HOH A . 
G 5 HOH 47  847  178 HOH HOH A . 
G 5 HOH 48  848  213 HOH HOH A . 
G 5 HOH 49  849  189 HOH HOH A . 
G 5 HOH 50  850  13  HOH HOH A . 
G 5 HOH 51  851  55  HOH HOH A . 
G 5 HOH 52  852  11  HOH HOH A . 
G 5 HOH 53  853  107 HOH HOH A . 
G 5 HOH 54  854  69  HOH HOH A . 
G 5 HOH 55  855  39  HOH HOH A . 
G 5 HOH 56  856  23  HOH HOH A . 
G 5 HOH 57  857  164 HOH HOH A . 
G 5 HOH 58  858  54  HOH HOH A . 
G 5 HOH 59  859  35  HOH HOH A . 
G 5 HOH 60  860  25  HOH HOH A . 
G 5 HOH 61  861  145 HOH HOH A . 
G 5 HOH 62  862  136 HOH HOH A . 
G 5 HOH 63  863  28  HOH HOH A . 
G 5 HOH 64  864  57  HOH HOH A . 
G 5 HOH 65  865  21  HOH HOH A . 
G 5 HOH 66  866  79  HOH HOH A . 
G 5 HOH 67  867  42  HOH HOH A . 
G 5 HOH 68  868  192 HOH HOH A . 
G 5 HOH 69  869  8   HOH HOH A . 
G 5 HOH 70  870  152 HOH HOH A . 
G 5 HOH 71  871  113 HOH HOH A . 
G 5 HOH 72  872  176 HOH HOH A . 
G 5 HOH 73  873  200 HOH HOH A . 
G 5 HOH 74  874  38  HOH HOH A . 
G 5 HOH 75  875  40  HOH HOH A . 
G 5 HOH 76  876  27  HOH HOH A . 
G 5 HOH 77  877  52  HOH HOH A . 
G 5 HOH 78  878  3   HOH HOH A . 
G 5 HOH 79  879  24  HOH HOH A . 
G 5 HOH 80  880  9   HOH HOH A . 
G 5 HOH 81  881  216 HOH HOH A . 
G 5 HOH 82  882  100 HOH HOH A . 
G 5 HOH 83  883  208 HOH HOH A . 
G 5 HOH 84  884  60  HOH HOH A . 
G 5 HOH 85  885  137 HOH HOH A . 
G 5 HOH 86  886  58  HOH HOH A . 
G 5 HOH 87  887  5   HOH HOH A . 
G 5 HOH 88  888  195 HOH HOH A . 
G 5 HOH 89  889  163 HOH HOH A . 
G 5 HOH 90  890  33  HOH HOH A . 
G 5 HOH 91  891  119 HOH HOH A . 
G 5 HOH 92  892  65  HOH HOH A . 
G 5 HOH 93  893  127 HOH HOH A . 
G 5 HOH 94  894  124 HOH HOH A . 
G 5 HOH 95  895  93  HOH HOH A . 
G 5 HOH 96  896  135 HOH HOH A . 
G 5 HOH 97  897  205 HOH HOH A . 
G 5 HOH 98  898  19  HOH HOH A . 
G 5 HOH 99  899  31  HOH HOH A . 
G 5 HOH 100 900  56  HOH HOH A . 
G 5 HOH 101 901  17  HOH HOH A . 
G 5 HOH 102 902  102 HOH HOH A . 
G 5 HOH 103 903  50  HOH HOH A . 
G 5 HOH 104 904  77  HOH HOH A . 
G 5 HOH 105 905  81  HOH HOH A . 
G 5 HOH 106 906  118 HOH HOH A . 
G 5 HOH 107 907  94  HOH HOH A . 
G 5 HOH 108 908  175 HOH HOH A . 
G 5 HOH 109 909  168 HOH HOH A . 
G 5 HOH 110 910  2   HOH HOH A . 
G 5 HOH 111 911  87  HOH HOH A . 
G 5 HOH 112 912  91  HOH HOH A . 
G 5 HOH 113 913  18  HOH HOH A . 
G 5 HOH 114 914  98  HOH HOH A . 
G 5 HOH 115 915  88  HOH HOH A . 
G 5 HOH 116 916  134 HOH HOH A . 
G 5 HOH 117 917  138 HOH HOH A . 
G 5 HOH 118 918  64  HOH HOH A . 
G 5 HOH 119 919  4   HOH HOH A . 
G 5 HOH 120 920  169 HOH HOH A . 
G 5 HOH 121 921  10  HOH HOH A . 
G 5 HOH 122 922  133 HOH HOH A . 
G 5 HOH 123 923  61  HOH HOH A . 
G 5 HOH 124 924  44  HOH HOH A . 
G 5 HOH 125 925  12  HOH HOH A . 
G 5 HOH 126 926  74  HOH HOH A . 
G 5 HOH 127 927  123 HOH HOH A . 
G 5 HOH 128 928  43  HOH HOH A . 
G 5 HOH 129 929  126 HOH HOH A . 
G 5 HOH 130 930  104 HOH HOH A . 
G 5 HOH 131 931  48  HOH HOH A . 
G 5 HOH 132 932  83  HOH HOH A . 
G 5 HOH 133 933  139 HOH HOH A . 
G 5 HOH 134 934  120 HOH HOH A . 
G 5 HOH 135 935  174 HOH HOH A . 
G 5 HOH 136 936  153 HOH HOH A . 
G 5 HOH 137 937  85  HOH HOH A . 
G 5 HOH 138 938  170 HOH HOH A . 
G 5 HOH 139 939  141 HOH HOH A . 
G 5 HOH 140 940  26  HOH HOH A . 
G 5 HOH 141 941  95  HOH HOH A . 
G 5 HOH 142 942  155 HOH HOH A . 
G 5 HOH 143 943  51  HOH HOH A . 
G 5 HOH 144 944  76  HOH HOH A . 
G 5 HOH 145 945  99  HOH HOH A . 
G 5 HOH 146 946  187 HOH HOH A . 
G 5 HOH 147 947  125 HOH HOH A . 
G 5 HOH 148 948  90  HOH HOH A . 
G 5 HOH 149 949  47  HOH HOH A . 
G 5 HOH 150 950  29  HOH HOH A . 
G 5 HOH 151 951  45  HOH HOH A . 
G 5 HOH 152 952  211 HOH HOH A . 
G 5 HOH 153 953  68  HOH HOH A . 
G 5 HOH 154 954  16  HOH HOH A . 
G 5 HOH 155 955  190 HOH HOH A . 
G 5 HOH 156 956  34  HOH HOH A . 
G 5 HOH 157 957  173 HOH HOH A . 
G 5 HOH 158 958  41  HOH HOH A . 
G 5 HOH 159 959  114 HOH HOH A . 
G 5 HOH 160 960  66  HOH HOH A . 
G 5 HOH 161 961  180 HOH HOH A . 
G 5 HOH 162 962  117 HOH HOH A . 
G 5 HOH 163 963  162 HOH HOH A . 
G 5 HOH 164 964  199 HOH HOH A . 
G 5 HOH 165 965  92  HOH HOH A . 
G 5 HOH 166 966  157 HOH HOH A . 
G 5 HOH 167 967  132 HOH HOH A . 
G 5 HOH 168 968  209 HOH HOH A . 
G 5 HOH 169 969  106 HOH HOH A . 
G 5 HOH 170 970  131 HOH HOH A . 
G 5 HOH 171 971  140 HOH HOH A . 
G 5 HOH 172 972  37  HOH HOH A . 
G 5 HOH 173 973  166 HOH HOH A . 
G 5 HOH 174 974  158 HOH HOH A . 
G 5 HOH 175 975  122 HOH HOH A . 
G 5 HOH 176 976  110 HOH HOH A . 
G 5 HOH 177 977  75  HOH HOH A . 
G 5 HOH 178 978  142 HOH HOH A . 
G 5 HOH 179 979  78  HOH HOH A . 
G 5 HOH 180 980  184 HOH HOH A . 
G 5 HOH 181 981  116 HOH HOH A . 
G 5 HOH 182 982  73  HOH HOH A . 
G 5 HOH 183 983  182 HOH HOH A . 
G 5 HOH 184 984  160 HOH HOH A . 
G 5 HOH 185 985  171 HOH HOH A . 
G 5 HOH 186 986  210 HOH HOH A . 
G 5 HOH 187 987  143 HOH HOH A . 
G 5 HOH 188 988  53  HOH HOH A . 
G 5 HOH 189 989  212 HOH HOH A . 
G 5 HOH 190 990  20  HOH HOH A . 
G 5 HOH 191 991  196 HOH HOH A . 
G 5 HOH 192 992  214 HOH HOH A . 
G 5 HOH 193 993  219 HOH HOH A . 
G 5 HOH 194 994  183 HOH HOH A . 
G 5 HOH 195 995  218 HOH HOH A . 
G 5 HOH 196 996  193 HOH HOH A . 
G 5 HOH 197 997  149 HOH HOH A . 
G 5 HOH 198 998  130 HOH HOH A . 
G 5 HOH 199 999  194 HOH HOH A . 
G 5 HOH 200 1000 203 HOH HOH A . 
G 5 HOH 201 1001 70  HOH HOH A . 
G 5 HOH 202 1002 159 HOH HOH A . 
G 5 HOH 203 1003 179 HOH HOH A . 
G 5 HOH 204 1004 204 HOH HOH A . 
G 5 HOH 205 1005 109 HOH HOH A . 
G 5 HOH 206 1006 191 HOH HOH A . 
G 5 HOH 207 1007 146 HOH HOH A . 
G 5 HOH 208 1008 202 HOH HOH A . 
G 5 HOH 209 1009 128 HOH HOH A . 
G 5 HOH 210 1010 148 HOH HOH A . 
G 5 HOH 211 1011 220 HOH HOH A . 
G 5 HOH 212 1012 201 HOH HOH A . 
G 5 HOH 213 1013 71  HOH HOH A . 
G 5 HOH 214 1014 188 HOH HOH A . 
G 5 HOH 215 1015 185 HOH HOH A . 
G 5 HOH 216 1016 186 HOH HOH A . 
G 5 HOH 217 1017 197 HOH HOH A . 
G 5 HOH 218 1018 84  HOH HOH A . 
G 5 HOH 219 1019 101 HOH HOH A . 
G 5 HOH 220 1020 154 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                   111.39 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EJ5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.818 
_cell.length_a_esd                 ? 
_cell.length_b                     119.735 
_cell.length_b_esd                 ? 
_cell.length_c                     60.552 
_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                         9EJ5 
_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                   9EJ5 
_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             2.18 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.49 
_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 pH 7.5, 0.5 uL of 100 mM MnCl2, 10 mM GTP, and 18-28% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_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                          ? 
_reflns.entry_id                                       9EJ5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.94 
_reflns.d_resolution_low                               120.46 
_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                                     43355 
_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                           98.51 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.97 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.4 
_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                                0.167 
_reflns.pdbx_Rpim_I_all                                0.063 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.155 
_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                                    1.95 
_reflns_shell.d_res_low                                     1.98 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2140 
_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                               7.16 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               1.716 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.618 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.27 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.592 
_reflns_shell.pdbx_Rsym_value                               0.637 
_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                                 9EJ5 
_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                            1.94 
_refine.ls_d_res_low                             51.01 
_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                     43195 
_refine.ls_number_reflns_R_free                  2196 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.64 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1703 
_refine.ls_R_factor_R_free                       0.2025 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1685 
_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                          1.36 
_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                 22.57 
_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                            0.22 
_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.pdbx_number_atoms_protein        4869 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         45 
_refine_hist.number_atoms_solvent             220 
_refine_hist.number_atoms_total               5134 
_refine_hist.d_res_high                       1.94 
_refine_hist.d_res_low                        51.01 
# 
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' ? 0.006  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.884  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.173 ? 1918 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052  ? 723  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 900  ? 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' 1.94 1.98  . . 128 2331 90.00  . . . . 0.2879 . . . . . . . . . . . 0.3303 
'X-RAY DIFFRACTION' 1.98 2.02  . . 134 2553 97.00  . . . . 0.2520 . . . . . . . . . . . 0.2823 
'X-RAY DIFFRACTION' 2.02 2.07  . . 135 2513 97.00  . . . . 0.2273 . . . . . . . . . . . 0.2521 
'X-RAY DIFFRACTION' 2.07 2.13  . . 147 2590 98.00  . . . . 0.2200 . . . . . . . . . . . 0.2566 
'X-RAY DIFFRACTION' 2.13 2.19  . . 133 2504 97.00  . . . . 0.2113 . . . . . . . . . . . 0.2754 
'X-RAY DIFFRACTION' 2.19 2.26  . . 135 2561 98.00  . . . . 0.1962 . . . . . . . . . . . 0.2496 
'X-RAY DIFFRACTION' 2.26 2.34  . . 130 2594 98.00  . . . . 0.1814 . . . . . . . . . . . 0.2066 
'X-RAY DIFFRACTION' 2.34 2.44  . . 141 2571 98.00  . . . . 0.1665 . . . . . . . . . . . 0.2151 
'X-RAY DIFFRACTION' 2.44 2.55  . . 141 2543 98.00  . . . . 0.1726 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 2.55 2.68  . . 123 2606 99.00  . . . . 0.1682 . . . . . . . . . . . 0.2250 
'X-RAY DIFFRACTION' 2.68 2.85  . . 122 2589 98.00  . . . . 0.1666 . . . . . . . . . . . 0.2016 
'X-RAY DIFFRACTION' 2.85 3.07  . . 154 2567 99.00  . . . . 0.1625 . . . . . . . . . . . 0.2460 
'X-RAY DIFFRACTION' 3.07 3.38  . . 119 2634 99.00  . . . . 0.1507 . . . . . . . . . . . 0.1644 
'X-RAY DIFFRACTION' 3.38 3.87  . . 141 2587 99.00  . . . . 0.1394 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 3.87 4.87  . . 160 2603 99.00  . . . . 0.1335 . . . . . . . . . . . 0.1622 
'X-RAY DIFFRACTION' 4.88 51.01 . . 153 2653 100.00 . . . . 0.1646 . . . . . . . . . . . 0.1806 
# 
_struct.entry_id                     9EJ5 
_struct.title                        'Rat cytosolic PEPCK in complex with GTP and beta-sulfopyruvate (293K)' 
_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        9EJ5 
_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              9EJ5 
_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_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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   none 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 PRO A 223 ? ARG A 225 ? PRO A 223 ARG A 225 5 ? 3  
HELX_P HELX_P12 AB3 TYR A 235 ? LEU A 240 ? TYR A 235 LEU A 240 1 ? 6  
HELX_P HELX_P13 AB4 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P14 AB5 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P15 AB6 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P16 AB7 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P17 AB8 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P18 AB9 PRO A 479 ? PHE A 486 ? PRO A 479 PHE A 486 5 ? 8  
HELX_P HELX_P19 AC1 ASN A 489 ? MET A 500 ? ASN A 489 MET A 500 1 ? 12 
HELX_P HELX_P20 AC2 ALA A 501 ? ARG A 503 ? ALA A 501 ARG A 503 5 ? 3  
HELX_P HELX_P21 AC3 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P22 AC4 ASN A 533 ? GLU A 545 ? ASN A 533 GLU A 545 1 ? 13 
HELX_P HELX_P23 AC5 ASN A 573 ? GLY A 579 ? ASN A 573 GLY A 579 1 ? 7  
HELX_P HELX_P24 AC6 SER A 581 ? ASN A 601 ? SER A 581 ASN A 601 1 ? 21 
HELX_P HELX_P25 AC7 ALA A 602 ? LEU A 604 ? ALA A 602 LEU A 604 5 ? 3  
HELX_P HELX_P26 AC8 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 GLU 63  OE1 ? ? ? 1_555 D MN  . MN  ? ? A GLU 63  A MN  703 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc2  metalc ? ? A LYS 244 NZ  ? ? ? 1_555 B MN  . MN  ? ? A LYS 244 A MN  701 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc3  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 B MN  . MN  ? ? A HIS 264 A MN  701 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc4  metalc ? ? A THR 291 OG1 ? ? ? 1_555 C MN  . MN  ? ? A THR 291 A MN  702 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc5  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 B MN  . MN  ? ? A ASP 311 A MN  701 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc6  metalc ? ? A HIS 502 NE2 ? ? ? 1_555 D MN  . MN  ? ? A HIS 502 A MN  703 2_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc7  metalc ? ? A GLU 607 OE2 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 2_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc8  metalc ? ? B MN  .   MN  ? ? ? 1_555 E SPV . O1  ? ? A MN  701 A SPV 704 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 E SPV . O2  ? ? A MN  701 A SPV 704 1_555 ? ? ? ? ? ? ? 2.426 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O1G A ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc11 metalc ? ? B MN  .   MN  ? ? ? 1_555 F GTP . O2G B ? A MN  701 A GTP 705 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc12 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O1G B ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O3G A ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc14 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O2B A ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc15 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GTP . O2B B ? A MN  702 A GTP 705 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc16 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 816 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc17 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 827 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc18 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 833 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc19 metalc ? ? D MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  703 A HOH 832 1_555 ? ? ? ? ? ? ? 2.750 ? ? 
metalc20 metalc ? ? D MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  703 A HOH 881 1_555 ? ? ? ? ? ? ? 2.260 ? ? 
metalc21 metalc ? ? D MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  703 A HOH 895 2_545 ? ? ? ? ? ? ? 2.476 ? ? 
# 
_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  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 49.3  ? 
2  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 48.4  ? 
3  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 4.1   ? 
4  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 832 ? 1_555 60.4  ? 
5  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 832 ? 1_555 108.9 ? 
6  OE2 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 832 ? 1_555 108.6 ? 
7  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 881 ? 1_555 104.8 ? 
8  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 881 ? 1_555 58.5  ? 
9  OE2 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 881 ? 1_555 57.9  ? 
10 O   ? G HOH .   ? A HOH 832 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 881 ? 1_555 163.3 ? 
11 OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 895 ? 2_545 165.2 ? 
12 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 895 ? 2_545 145.5 ? 
13 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 895 ? 2_545 146.3 ? 
14 O   ? G HOH .   ? A HOH 832 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 895 ? 2_545 105.1 ? 
15 O   ? G HOH .   ? A HOH 881 ? 1_555 MN ? D MN . ? A MN 703 ? 1_555 O   ? G HOH .   ? A HOH 895 ? 2_545 89.1  ? 
16 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  ? 
17 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 99.9  ? 
18 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 94.9  ? 
19 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 88.2  ? 
20 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 98.0  ? 
21 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1  ? E SPV .   ? A SPV 704 ? 1_555 165.7 ? 
22 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 92.0  ? 
23 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2  ? E SPV .   ? A SPV 704 ? 1_555 168.8 ? 
24 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 95.5  ? 
25 O1  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2  ? E SPV .   ? A SPV 704 ? 1_555 72.2  ? 
26 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_555 173.7 ? 
27 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 95.2  ? 
28 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 86.0  ? 
29 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 86.4  ? 
30 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 89.5  ? 
31 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2G B F GTP .   ? A GTP 705 ? 1_555 170.0 ? 
32 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2G B F GTP .   ? A GTP 705 ? 1_555 106.7 ? 
33 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2G B F GTP .   ? A GTP 705 ? 1_555 84.0  ? 
34 O1  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2G B F GTP .   ? A GTP 705 ? 1_555 86.2  ? 
35 O2  ? E SPV .   ? A SPV 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2G B F GTP .   ? A GTP 705 ? 1_555 78.4  ? 
36 O1G A F GTP .   ? A GTP 705 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O2G B F GTP .   ? A GTP 705 ? 1_555 11.6  ? 
37 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O1G B F GTP .   ? A GTP 705 ? 1_555 158.6 ? 
38 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_555 173.2 ? 
39 O1G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3G A F GTP .   ? A GTP 705 ? 1_555 25.1  ? 
40 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 88.2  ? 
41 O1G 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  ? 
42 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 97.7  ? 
43 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 92.5  ? 
44 O1G 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 80.9  ? 
45 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 94.3  ? 
46 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 23.9  ? 
47 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 816 ? 1_555 99.4  ? 
48 O1G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 816 ? 1_555 101.7 ? 
49 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 816 ? 1_555 78.6  ? 
50 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 816 ? 1_555 76.7  ? 
51 O2B B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 816 ? 1_555 99.1  ? 
52 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 827 ? 1_555 83.7  ? 
53 O1G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 827 ? 1_555 75.1  ? 
54 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 827 ? 1_555 98.6  ? 
55 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 827 ? 1_555 100.4 ? 
56 O2B B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 827 ? 1_555 77.5  ? 
57 O   ? G HOH .   ? A HOH 816 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 827 ? 1_555 175.6 ? 
58 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 82.4  ? 
59 O1G B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 102.8 ? 
60 O3G A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 90.9  ? 
61 O2B A F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 157.6 ? 
62 O2B B F GTP .   ? A GTP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 174.0 ? 
63 O   ? G HOH .   ? A HOH 816 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 84.8  ? 
64 O   ? G HOH .   ? A HOH 827 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 833 ? 1_555 98.8  ? 
# 
_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       1.16 
# 
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 GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
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 LEU A 160 ? N LEU A 160 O CYS A 192 ? O CYS A 192 
AA1 5 6 N LEU A 193 ? N LEU A 193 O SER A 230 ? O SER A 230 
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 GLN A 17  ? N GLN A 17  O ILE A 45  ? O ILE A 45  
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 LYS A 316 ? N LYS A 316 O ARG A 324 ? O ARG A 324 
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 LYS A 316 ? N LYS A 316 O ARG A 324 ? O ARG A 324 
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                   9EJ5 
_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_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   ? ? -132.48 -135.87 
2  1 SER A 108 ? ? -143.43 -37.06  
3  1 LEU A 149 ? ? -62.38  83.31   
4  1 LYS A 243 ? ? -89.69  -82.27  
5  1 ASP A 311 ? ? -152.31 -41.63  
6  1 PHE A 333 ? ? -116.76 77.55   
7  1 PRO A 393 ? ? -63.80  11.71   
8  1 THR A 465 ? ? -106.20 -165.84 
9  1 ALA A 468 ? ? -96.72  -112.73 
10 1 GLU A 469 ? ? -144.60 32.10   
11 1 ALA A 505 ? ? 58.14   15.85   
12 1 PHE A 530 ? ? 53.64   -125.83 
13 1 ASP A 571 ? ? -103.85 40.47   
14 1 ASN A 601 ? ? 51.58   -118.17 
# 
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                    9EJ5 
_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]   0.022312 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008740 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008352 
_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]   0.017736 
_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   ? 2.486   -13.308 -32.391 1.00 89.49  ? 3    PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 3.269   -14.169 -33.283 1.00 86.62  ? 3    PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 4.510   -14.729 -32.602 1.00 84.04  ? 3    PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 4.840   -14.311 -31.493 1.00 84.90  ? 3    PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 3.657   -13.226 -34.418 1.00 84.08  ? 3    PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 3.760   -11.895 -33.755 1.00 83.24  ? 3    PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 2.685   -11.879 -32.694 1.00 85.88  ? 3    PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 5.182   -15.666 -33.265 1.00 57.40  ? 4    GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 6.412   -16.256 -32.753 1.00 57.07  ? 4    GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 7.005   -17.144 -33.839 1.00 43.95  ? 4    GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 6.309   -17.582 -34.758 1.00 36.34  ? 4    GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 6.176   -17.055 -31.457 1.00 59.71  ? 4    GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 5.096   -18.129 -31.552 1.00 59.36  ? 4    GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 4.922   -18.932 -30.263 1.00 67.38  ? 4    GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 5.754   -18.876 -29.353 1.00 61.56  ? 4    GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 3.834   -19.692 -30.189 1.00 61.28  ? 4    GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 8.310   -17.383 -33.730 1.00 38.26  ? 5    LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 9.018   -18.268 -34.651 1.00 37.89  ? 5    LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 9.152   -19.688 -34.125 1.00 37.63  ? 5    LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 9.461   -20.598 -34.904 1.00 35.15  ? 5    LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 10.416  -17.717 -34.948 1.00 35.47  ? 5    LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 10.433  -16.484 -35.850 1.00 37.25  ? 5    LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 11.831  -15.898 -35.901 1.00 38.54  ? 5    LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 9.933   -16.852 -37.244 1.00 39.32  ? 5    LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 8.947   -19.884 -32.826 1.00 37.35  ? 6    HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 8.985   -21.198 -32.201 1.00 50.68  ? 6    HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 7.763   -21.372 -31.301 1.00 60.33  ? 6    HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 6.649   -21.023 -31.701 1.00 53.31  ? 6    HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 10.296  -21.366 -31.436 1.00 37.56  ? 6    HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 11.503  -21.316 -32.318 1.00 47.12  ? 6    HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 12.182  -20.145 -32.584 1.00 44.49  ? 6    HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 12.129  -22.284 -33.031 1.00 35.26  ? 6    HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 13.191  -20.400 -33.399 1.00 36.37  ? 6    HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 13.178  -21.689 -33.688 1.00 40.95  ? 6    HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 7.944   -21.905 -30.096 1.00 83.81  ? 7    ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 6.829   -22.069 -29.164 1.00 85.61  ? 7    ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 7.247   -21.666 -27.759 1.00 85.30  ? 7    ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 6.934   -22.346 -26.775 1.00 85.66  ? 7    ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 6.299   -23.501 -29.180 1.00 86.35  ? 7    ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 5.501   -23.807 -30.428 1.00 94.34  ? 7    ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 4.272   -23.717 -30.430 1.00 97.14  ? 7    ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 6.197   -24.162 -31.505 1.00 94.38  ? 7    ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 7.950   -20.544 -27.647 1.00 63.16  ? 8    GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 8.510   -20.150 -26.375 1.00 59.04  ? 8    GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 7.731   -19.068 -25.662 1.00 47.15  ? 8    GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 7.890   -18.895 -24.450 1.00 54.16  ? 8    GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 6.877   -18.346 -26.387 1.00 42.66  ? 9    LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 6.227   -17.159 -25.837 1.00 48.28  ? 9    LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 4.760   -17.358 -25.485 1.00 42.15  ? 9    LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 4.239   -16.624 -24.638 1.00 45.91  ? 9    LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 6.343   -15.992 -26.819 1.00 48.16  ? 9    LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 7.783   -15.674 -27.211 1.00 49.79  ? 9    LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 7.814   -14.483 -28.160 1.00 48.18  ? 9    LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 8.625   -15.416 -25.966 1.00 46.41  ? 9    LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 4.075   -18.306 -26.120 1.00 40.45  ? 10   ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 2.673   -18.572 -25.810 1.00 46.07  ? 10   ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 2.576   -19.516 -24.612 1.00 37.01  ? 10   ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 2.987   -20.679 -24.695 1.00 31.77  ? 10   ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 1.969   -19.168 -27.027 1.00 48.02  ? 10   ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 0.459   -19.203 -26.875 1.00 45.40  ? 10   ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? -0.036  -19.223 -25.730 1.00 45.54  ? 10   ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? -0.244  -19.215 -27.909 1.00 57.99  ? 10   ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 2.010   -19.027 -23.507 1.00 33.35  ? 11   PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 1.916   -19.808 -22.283 1.00 28.41  ? 11   PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 0.576   -20.509 -22.130 1.00 29.46  ? 11   PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 0.277   -21.005 -21.037 1.00 25.82  ? 11   PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 2.194   -18.929 -21.062 1.00 32.19  ? 11   PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 3.646   -18.863 -20.691 1.00 33.11  ? 11   PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 4.528   -18.081 -21.425 1.00 31.35  ? 11   PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 4.135   -19.593 -19.618 1.00 33.80  ? 11   PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 5.869   -18.031 -21.094 1.00 32.32  ? 11   PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 5.471   -19.539 -19.276 1.00 32.23  ? 11   PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 6.339   -18.754 -20.018 1.00 29.30  ? 11   PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? -0.219  -20.579 -23.205 1.00 26.10  ? 12   SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? -1.553  -21.172 -23.130 1.00 33.00  ? 12   SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? -1.512  -22.601 -22.601 1.00 33.64  ? 12   SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? -2.392  -23.009 -21.830 1.00 31.60  ? 12   SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? -2.218  -21.144 -24.509 1.00 36.67  ? 12   SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? -2.580  -19.822 -24.878 1.00 37.70  ? 12   SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? -0.510  -23.383 -23.013 1.00 26.24  ? 13   ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? -0.476  -24.785 -22.617 1.00 29.15  ? 13   ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? -0.182  -24.968 -21.137 1.00 29.17  ? 13   ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? -0.335  -26.082 -20.630 1.00 30.50  ? 13   ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 0.558   -25.551 -23.446 1.00 26.56  ? 13   ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 0.242   -23.920 -20.435 1.00 27.52  ? 14   LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 0.502   -24.020 -19.006 1.00 30.88  ? 14   LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? -0.633  -23.476 -18.143 1.00 25.28  ? 14   LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? -0.493  -23.453 -16.917 1.00 23.30  ? 14   LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 1.806   -23.301 -18.653 1.00 30.15  ? 14   LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 3.042   -24.001 -19.198 1.00 37.53  ? 14   LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 4.327   -23.332 -18.718 1.00 36.11  ? 14   LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 5.560   -24.115 -19.146 1.00 39.75  ? 14   LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 5.937   -23.836 -20.570 1.00 53.68  ? 14   LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? -1.752  -23.069 -18.740 1.00 24.86  ? 15   VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? -2.857  -22.465 -17.992 1.00 24.42  ? 15   VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? -3.733  -23.581 -17.432 1.00 25.72  ? 15   VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? -4.383  -24.311 -18.184 1.00 29.79  ? 15   VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? -3.678  -21.515 -18.868 1.00 27.44  ? 15   VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? -4.909  -21.035 -18.101 1.00 24.09  ? 15   VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? -2.826  -20.332 -19.324 1.00 25.94  ? 15   VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? -3.763  -23.715 -16.106 1.00 22.66  ? 16   ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? -4.551  -24.770 -15.477 1.00 20.56  ? 16   ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? -5.910  -24.287 -15.003 1.00 24.73  ? 16   ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? -6.715  -25.114 -14.552 1.00 24.99  ? 16   ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? -3.789  -25.419 -14.305 1.00 24.01  ? 16   ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? -3.433  -24.388 -13.238 1.00 26.98  ? 16   ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? -2.530  -26.109 -14.822 1.00 20.96  ? 16   ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? -2.667  -24.968 -12.067 1.00 28.98  ? 16   ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? -6.185  -22.983 -15.062 1.00 24.39  ? 17   GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? -7.539  -22.477 -14.858 1.00 24.67  ? 17   GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? -7.691  -21.158 -15.597 1.00 30.56  ? 17   GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? -6.823  -20.283 -15.502 1.00 24.57  ? 17   GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? -7.885  -22.283 -13.370 1.00 26.25  ? 17   GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? -9.278  -21.686 -13.198 1.00 21.24  ? 17   GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? -9.761  -21.626 -11.764 1.00 31.74  ? 17   GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? -9.807  -22.633 -11.061 1.00 32.31  ? 17   GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? -10.143 -20.434 -11.328 1.00 29.28  ? 17   GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? -8.794  -21.017 -16.324 1.00 26.95  ? 18   GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? -9.022  -19.827 -17.108 1.00 29.52  ? 18   GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? -8.425  -19.918 -18.495 1.00 34.69  ? 18   GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? -7.989  -20.973 -18.968 1.00 34.45  ? 18   GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? -8.408  -18.767 -19.161 1.00 36.51  ? 19   SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? -7.940  -18.668 -20.535 1.00 37.60  ? 19   SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? -7.157  -17.379 -20.720 1.00 36.28  ? 19   SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? -7.654  -16.304 -20.369 1.00 36.60  ? 19   SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? -9.121  -18.702 -21.514 1.00 33.78  ? 19   SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? -8.680  -18.485 -22.843 1.00 50.68  ? 19   SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? -5.944  -17.481 -21.281 1.00 34.18  ? 20   LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? -5.222  -16.270 -21.678 1.00 36.44  ? 20   LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? -5.989  -15.493 -22.740 1.00 38.25  ? 20   LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? -5.965  -14.257 -22.744 1.00 42.05  ? 20   LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? -3.820  -16.615 -22.192 1.00 30.60  ? 20   LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? -2.772  -17.148 -21.208 1.00 32.56  ? 20   LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? -1.450  -17.466 -21.915 1.00 34.16  ? 20   LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? -2.543  -16.167 -20.066 1.00 30.85  ? 20   LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? -6.701  -16.199 -23.625 1.00 44.27  ? 21   ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? -7.456  -15.547 -24.691 1.00 54.00  ? 21   ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? -8.553  -14.639 -24.150 1.00 52.95  ? 21   ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? -8.858  -13.607 -24.756 1.00 68.42  ? 21   ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? -8.068  -16.601 -25.617 1.00 58.51  ? 21   ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? -7.040  -17.560 -26.170 1.00 62.91  ? 21   ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? -5.961  -17.097 -26.594 1.00 61.85  ? 21   ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? -7.307  -18.781 -26.178 1.00 70.55  ? 21   ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? -9.165  -15.002 -23.025 1.00 46.49  ? 22   SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? -10.274 -14.225 -22.489 1.00 44.00  ? 22   SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? -9.828  -12.987 -21.721 1.00 45.36  ? 22   SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? -10.686 -12.199 -21.308 1.00 52.98  ? 22   SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? -11.131 -15.098 -21.577 1.00 43.02  ? 22   SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? -10.414 -15.438 -20.406 1.00 48.16  ? 22   SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? -8.521  -12.795 -21.517 1.00 38.63  ? 23   LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? -8.025  -11.636 -20.791 1.00 38.01  ? 23   LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? -7.992  -10.401 -21.690 1.00 43.69  ? 23   LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? -7.697  -10.502 -22.885 1.00 40.97  ? 23   LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? -6.617  -11.896 -20.264 1.00 39.28  ? 23   LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? -6.372  -13.013 -19.251 1.00 36.51  ? 23   LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? -4.880  -13.091 -18.946 1.00 31.67  ? 23   LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? -7.169  -12.775 -17.977 1.00 41.61  ? 23   LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? -8.277  -9.224  -21.131 1.00 39.56  ? 24   PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? -7.992  -7.979  -21.856 1.00 39.23  ? 24   PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? -6.534  -7.942  -22.293 1.00 38.81  ? 24   PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? -5.640  -8.372  -21.560 1.00 40.79  ? 24   PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? -8.299  -6.888  -20.827 1.00 39.18  ? 24   PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? -9.226  -7.537  -19.842 1.00 43.07  ? 24   PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? -8.820  -8.977  -19.785 1.00 42.16  ? 24   PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? -6.305  -7.415  -23.501 1.00 36.58  ? 25   GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? -4.993  -7.515  -24.143 1.00 40.40  ? 25   GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? -3.864  -7.030  -23.238 1.00 35.28  ? 25   GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? -2.832  -7.694  -23.114 1.00 35.71  ? 25   GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? -4.990  -6.742  -25.467 1.00 50.37  ? 25   GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? -5.609  -7.504  -26.642 1.00 63.05  ? 25   GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? -5.296  -6.872  -27.998 1.00 76.91  ? 25   GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? -4.721  -5.781  -28.073 1.00 75.37  ? 25   GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? -5.672  -7.561  -29.076 1.00 72.60  ? 25   GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? -4.036  -5.872  -22.593 1.00 35.92  ? 26   GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? -2.971  -5.383  -21.719 1.00 36.06  ? 26   GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? -2.767  -6.293  -20.513 1.00 33.85  ? 26   GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? -1.637  -6.429  -20.027 1.00 31.24  ? 26   GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? -3.266  -3.954  -21.259 1.00 43.15  ? 26   GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? -3.161  -2.912  -22.365 1.00 48.16  ? 26   GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? -1.812  -2.930  -23.065 1.00 49.51  ? 26   GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? -0.774  -3.074  -22.381 1.00 50.43  ? 26   GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? -1.790  -2.805  -24.308 1.00 59.58  ? 26   GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? -3.836  -6.916  -20.010 1.00 31.75  ? 27   VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? -3.675  -7.869  -18.915 1.00 28.10  ? 27   VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? -2.918  -9.096  -19.396 1.00 27.11  ? 27   VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? -2.003  -9.584  -18.718 1.00 27.90  ? 27   VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? -5.045  -8.239  -18.313 1.00 33.75  ? 27   VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? -4.897  -9.313  -17.235 1.00 26.29  ? 27   VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? -5.713  -6.997  -17.738 1.00 29.80  ? 27   VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? -3.266  -9.605  -20.579 1.00 26.85  ? 28   ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? -2.551  -10.769 -21.096 1.00 31.86  ? 28   ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? -1.065  -10.472 -21.246 1.00 26.72  ? 28   ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? -0.215  -11.270 -20.833 1.00 28.08  ? 28   ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? -3.138  -11.231 -22.431 1.00 29.23  ? 28   ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? -2.327  -12.406 -22.975 1.00 33.36  ? 28   ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? -2.847  -13.011 -24.260 1.00 36.88  ? 28   ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? -2.046  -14.185 -24.600 1.00 36.39  ? 28   ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? -2.491  -15.225 -25.290 1.00 39.33  ? 28   ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? -3.714  -15.245 -25.796 1.00 41.92  ? 28   ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? -1.696  -16.281 -25.458 1.00 41.20  ? 28   ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? -0.731  -9.319  -21.826 1.00 27.08  ? 29   LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 0.671   -8.945  -21.978 1.00 29.17  ? 29   LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 1.388   -8.937  -20.636 1.00 27.05  ? 29   LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 2.526   -9.402  -20.530 1.00 24.71  ? 29   LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 0.780   -7.560  -22.630 1.00 36.10  ? 29   LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 0.265   -7.459  -24.061 1.00 44.23  ? 29   LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 0.466   -6.037  -24.592 1.00 47.23  ? 29   LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? -0.260  -5.799  -25.910 1.00 63.47  ? 29   LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? 0.482   -6.340  -27.092 1.00 77.53  ? 29   LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 0.745   -8.374  -19.607 1.00 28.17  ? 30   PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 1.331   -8.336  -18.270 1.00 28.03  ? 30   PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 1.576   -9.743  -17.731 1.00 25.45  ? 30   PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 2.640   -10.025 -17.167 1.00 26.12  ? 30   PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 0.407   -7.524  -17.346 1.00 25.48  ? 30   PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 0.852   -7.448  -15.907 1.00 24.09  ? 30   PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 2.075   -6.907  -15.569 1.00 20.36  ? 30   PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? -0.006  -7.854  -14.884 1.00 23.63  ? 30   PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 2.478   -6.834  -14.234 1.00 24.20  ? 30   PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 0.375   -7.761  -13.555 1.00 23.19  ? 30   PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 1.614   -7.247  -13.226 1.00 21.23  ? 30   PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 0.611   -10.647 -17.911 1.00 26.74  ? 31   VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 0.778   -12.013 -17.423 1.00 19.83  ? 31   VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 1.892   -12.727 -18.188 1.00 27.76  ? 31   VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 2.829   -13.279 -17.591 1.00 22.56  ? 31   VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? -0.549  -12.794 -17.525 1.00 28.13  ? 31   VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? -0.328  -14.266 -17.171 1.00 23.23  ? 31   VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? -1.639  -12.170 -16.632 1.00 21.93  ? 31   VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 1.809   -12.724 -19.521 1.00 24.03  ? 32   GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 2.730   -13.531 -20.322 1.00 31.81  ? 32   GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 4.154   -12.994 -20.261 1.00 29.16  ? 32   GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 5.109   -13.775 -20.170 1.00 30.73  ? 32   GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 2.242   -13.612 -21.769 1.00 32.81  ? 32   GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 1.250   -14.742 -21.987 1.00 39.15  ? 32   GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 0.931   -15.003 -23.452 1.00 39.81  ? 32   GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 0.762   -14.027 -24.206 1.00 30.87  ? 32   GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 0.836   -16.193 -23.838 1.00 39.57  ? 32   GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 4.320   -11.669 -20.314 1.00 26.97  ? 33   GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 5.655   -11.097 -20.198 1.00 24.85  ? 33   GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 6.341   -11.478 -18.900 1.00 27.03  ? 33   GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 7.528   -11.812 -18.883 1.00 23.04  ? 33   GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 5.600   -11.460 -17.795 1.00 27.20  ? 34   ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 6.209   -11.857 -16.536 1.00 23.77  ? 34   ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 6.342   -13.365 -16.415 1.00 22.03  ? 34   ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 7.244   -13.850 -15.722 1.00 24.72  ? 34   ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 5.400   -11.293 -15.375 1.00 27.05  ? 34   ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 5.703   -9.856  -15.150 1.00 27.97  ? 34   ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 6.833   -9.506  -14.798 1.00 26.99  ? 34   ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 4.727   -8.998  -15.402 1.00 27.34  ? 34   ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 5.454   -14.122 -17.058 1.00 21.96  ? 35   ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 5.628   -15.572 -17.074 1.00 21.16  ? 35   ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 6.898   -15.943 -17.825 1.00 27.12  ? 35   ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 7.629   -16.849 -17.412 1.00 26.63  ? 35   ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 4.413   -16.253 -17.698 1.00 24.83  ? 35   ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 7.184   -15.235 -18.922 1.00 29.20  ? 36   GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 8.438   -15.457 -19.641 1.00 27.38  ? 36   GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 9.631   -15.145 -18.747 1.00 29.88  ? 36   GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 10.624  -15.880 -18.739 1.00 27.25  ? 36   GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 8.462   -14.604 -20.914 1.00 31.44  ? 36   GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 7.397   -15.005 -21.936 1.00 38.33  ? 36   GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 7.111   -13.928 -22.971 1.00 47.91  ? 36   GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 7.900   -12.997 -23.163 1.00 47.95  ? 36   GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 5.969   -14.052 -23.645 1.00 46.97  ? 36   GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 9.526   -14.080 -17.952 1.00 25.12  ? 37   LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 10.612  -13.686 -17.060 1.00 26.22  ? 37   LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 10.750  -14.630 -15.869 1.00 26.77  ? 37   LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 11.862  -15.056 -15.527 1.00 24.68  ? 37   LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 10.376  -12.248 -16.585 1.00 29.45  ? 37   LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 11.239  -11.760 -15.426 1.00 34.88  ? 37   LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 12.624  -11.387 -15.914 1.00 36.27  ? 37   LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 10.562  -10.587 -14.738 1.00 33.50  ? 37   LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 9.635   -14.955 -15.202 1.00 24.85  ? 38   CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 9.700   -15.696 -13.951 1.00 22.50  ? 38   CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 9.653   -17.205 -14.135 1.00 25.38  ? 38   CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 9.990   -17.936 -13.196 1.00 25.19  ? 38   CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 8.551   -15.277 -13.022 1.00 24.01  ? 38   CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 8.487   -13.522 -12.652 1.00 28.27  ? 38   CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 9.235   -17.685 -15.305 0.48 27.14  ? 39   GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 9.211   -17.678 -15.298 0.52 27.13  ? 39   GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 9.216   -19.106 -15.656 0.48 29.32  ? 39   GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 9.192   -19.090 -15.679 0.52 29.33  ? 39   GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 8.408   -19.967 -14.686 0.48 28.60  ? 39   GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 8.400   -19.970 -14.712 0.52 28.61  ? 39   GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 8.927   -20.970 -14.175 0.48 25.90  ? 39   GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 8.921   -20.987 -14.230 0.52 25.87  ? 39   GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 10.646  -19.645 -15.749 0.48 31.02  ? 39   GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 10.627  -19.605 -15.811 0.52 31.05  ? 39   GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 11.383  -19.217 -17.009 0.48 32.96  ? 39   GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 11.493  -18.737 -16.716 0.52 32.38  ? 39   GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 10.738  -19.764 -18.264 0.48 33.30  ? 39   GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 12.866  -19.321 -16.936 0.52 33.77  ? 39   GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 10.826  -20.960 -18.551 0.48 37.62  ? 39   GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 13.060  -20.166 -17.810 0.52 40.28  ? 39   GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 10.077  -18.894 -19.016 0.48 32.84  ? 39   GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 13.830  -18.884 -16.135 0.52 30.87  ? 39   GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 7.139   -19.645 -14.429 1.00 26.80  ? 40   PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 6.321   -20.538 -13.603 1.00 24.72  ? 40   PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 6.012   -21.813 -14.373 1.00 25.70  ? 40   PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 5.998   -21.837 -15.607 1.00 24.53  ? 40   PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 5.050   -19.719 -13.353 1.00 24.33  ? 40   PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 4.908   -18.950 -14.625 1.00 25.34  ? 40   PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 6.322   -18.547 -14.988 1.00 23.85  ? 40   PRO A CD    1 
ATOM   302  N  N     A GLU A 1 41  ? 5.775   -22.891 -13.620 0.64 25.08  ? 41   GLU A N     1 
ATOM   303  N  N     B GLU A 1 41  ? 5.755   -22.885 -13.625 0.36 25.08  ? 41   GLU A N     1 
ATOM   304  C  CA    A GLU A 1 41  ? 5.388   -24.152 -14.238 0.64 25.18  ? 41   GLU A CA    1 
ATOM   305  C  CA    B GLU A 1 41  ? 5.381   -24.135 -14.271 0.36 25.19  ? 41   GLU A CA    1 
ATOM   306  C  C     A GLU A 1 41  ? 3.930   -24.139 -14.682 0.64 28.54  ? 41   GLU A C     1 
ATOM   307  C  C     B GLU A 1 41  ? 3.916   -24.143 -14.688 0.36 28.45  ? 41   GLU A C     1 
ATOM   308  O  O     A GLU A 1 41  ? 3.604   -24.729 -15.717 0.64 25.69  ? 41   GLU A O     1 
ATOM   309  O  O     B GLU A 1 41  ? 3.571   -24.760 -15.700 0.36 25.77  ? 41   GLU A O     1 
ATOM   310  C  CB    A GLU A 1 41  ? 5.648   -25.311 -13.271 0.64 26.96  ? 41   GLU A CB    1 
ATOM   311  C  CB    B GLU A 1 41  ? 5.673   -25.316 -13.349 0.36 26.99  ? 41   GLU A CB    1 
ATOM   312  C  CG    A GLU A 1 41  ? 5.570   -26.722 -13.895 0.64 29.51  ? 41   GLU A CG    1 
ATOM   313  C  CG    B GLU A 1 41  ? 5.591   -26.667 -14.046 0.36 29.48  ? 41   GLU A CG    1 
ATOM   314  C  CD    A GLU A 1 41  ? 6.819   -27.113 -14.679 0.64 31.29  ? 41   GLU A CD    1 
ATOM   315  C  CD    B GLU A 1 41  ? 5.971   -27.807 -13.134 0.36 29.12  ? 41   GLU A CD    1 
ATOM   316  O  OE1   A GLU A 1 41  ? 7.723   -26.262 -14.851 0.64 28.85  ? 41   GLU A OE1   1 
ATOM   317  O  OE1   B GLU A 1 41  ? 6.209   -27.551 -11.935 0.36 29.08  ? 41   GLU A OE1   1 
ATOM   318  O  OE2   A GLU A 1 41  ? 6.897   -28.282 -15.121 0.64 32.37  ? 41   GLU A OE2   1 
ATOM   319  O  OE2   B GLU A 1 41  ? 6.038   -28.959 -13.616 0.36 33.56  ? 41   GLU A OE2   1 
ATOM   320  N  N     . TYR A 1 42  ? 3.049   -23.470 -13.931 1.00 20.11  ? 42   TYR A N     1 
ATOM   321  C  CA    . TYR A 1 42  ? 1.627   -23.391 -14.250 1.00 23.88  ? 42   TYR A CA    1 
ATOM   322  C  C     . TYR A 1 42  ? 1.150   -21.957 -14.074 1.00 21.90  ? 42   TYR A C     1 
ATOM   323  O  O     . TYR A 1 42  ? 1.753   -21.173 -13.342 1.00 19.63  ? 42   TYR A O     1 
ATOM   324  C  CB    . TYR A 1 42  ? 0.758   -24.277 -13.345 1.00 23.62  ? 42   TYR A CB    1 
ATOM   325  C  CG    . TYR A 1 42  ? 1.351   -25.619 -13.038 1.00 28.27  ? 42   TYR A CG    1 
ATOM   326  C  CD1   . TYR A 1 42  ? 1.157   -26.694 -13.892 1.00 30.57  ? 42   TYR A CD1   1 
ATOM   327  C  CD2   . TYR A 1 42  ? 2.095   -25.814 -11.882 1.00 32.14  ? 42   TYR A CD2   1 
ATOM   328  C  CE1   . TYR A 1 42  ? 1.695   -27.939 -13.610 1.00 33.41  ? 42   TYR A CE1   1 
ATOM   329  C  CE2   . TYR A 1 42  ? 2.640   -27.047 -11.592 1.00 35.00  ? 42   TYR A CE2   1 
ATOM   330  C  CZ    . TYR A 1 42  ? 2.431   -28.108 -12.456 1.00 30.99  ? 42   TYR A CZ    1 
ATOM   331  O  OH    . TYR A 1 42  ? 2.979   -29.336 -12.169 1.00 37.59  ? 42   TYR A OH    1 
ATOM   332  N  N     . ILE A 1 43  ? 0.046   -21.629 -14.740 1.00 24.10  ? 43   ILE A N     1 
ATOM   333  C  CA    . ILE A 1 43  ? -0.620  -20.336 -14.585 1.00 21.48  ? 43   ILE A CA    1 
ATOM   334  C  C     . ILE A 1 43  ? -2.077  -20.573 -14.210 1.00 21.18  ? 43   ILE A C     1 
ATOM   335  O  O     . ILE A 1 43  ? -2.815  -21.246 -14.939 1.00 22.49  ? 43   ILE A O     1 
ATOM   336  C  CB    . ILE A 1 43  ? -0.537  -19.487 -15.863 1.00 21.26  ? 43   ILE A CB    1 
ATOM   337  C  CG1   . ILE A 1 43  ? 0.921   -19.174 -16.185 1.00 21.49  ? 43   ILE A CG1   1 
ATOM   338  C  CG2   . ILE A 1 43  ? -1.349  -18.212 -15.681 1.00 21.10  ? 43   ILE A CG2   1 
ATOM   339  C  CD1   . ILE A 1 43  ? 1.106   -18.455 -17.489 1.00 26.90  ? 43   ILE A CD1   1 
ATOM   340  N  N     . HIS A 1 44  ? -2.503  -19.966 -13.109 1.00 18.08  ? 44   HIS A N     1 
ATOM   341  C  CA    . HIS A 1 44  ? -3.846  -20.128 -12.578 1.00 16.05  ? 44   HIS A CA    1 
ATOM   342  C  C     . HIS A 1 44  ? -4.483  -18.742 -12.554 1.00 18.70  ? 44   HIS A C     1 
ATOM   343  O  O     . HIS A 1 44  ? -4.069  -17.888 -11.773 1.00 18.17  ? 44   HIS A O     1 
ATOM   344  C  CB    . HIS A 1 44  ? -3.783  -20.748 -11.183 1.00 18.60  ? 44   HIS A CB    1 
ATOM   345  C  CG    . HIS A 1 44  ? -5.108  -20.885 -10.502 1.00 20.60  ? 44   HIS A CG    1 
ATOM   346  N  ND1   . HIS A 1 44  ? -5.635  -22.105 -10.139 1.00 23.17  ? 44   HIS A ND1   1 
ATOM   347  C  CD2   . HIS A 1 44  ? -6.006  -19.952 -10.093 1.00 18.67  ? 44   HIS A CD2   1 
ATOM   348  C  CE1   . HIS A 1 44  ? -6.801  -21.924 -9.541  1.00 20.74  ? 44   HIS A CE1   1 
ATOM   349  N  NE2   . HIS A 1 44  ? -7.049  -20.626 -9.503  1.00 20.21  ? 44   HIS A NE2   1 
ATOM   350  N  N     . ILE A 1 45  ? -5.460  -18.508 -13.421 1.00 19.03  ? 45   ILE A N     1 
ATOM   351  C  CA    . ILE A 1 45  ? -6.194  -17.250 -13.429 1.00 20.20  ? 45   ILE A CA    1 
ATOM   352  C  C     . ILE A 1 45  ? -7.331  -17.382 -12.425 1.00 19.01  ? 45   ILE A C     1 
ATOM   353  O  O     . ILE A 1 45  ? -8.254  -18.177 -12.619 1.00 22.86  ? 45   ILE A O     1 
ATOM   354  C  CB    . ILE A 1 45  ? -6.716  -16.907 -14.826 1.00 21.23  ? 45   ILE A CB    1 
ATOM   355  C  CG1   . ILE A 1 45  ? -5.560  -16.933 -15.836 1.00 24.77  ? 45   ILE A CG1   1 
ATOM   356  C  CG2   . ILE A 1 45  ? -7.373  -15.526 -14.804 1.00 24.00  ? 45   ILE A CG2   1 
ATOM   357  C  CD1   . ILE A 1 45  ? -5.974  -16.681 -17.250 1.00 28.47  ? 45   ILE A CD1   1 
ATOM   358  N  N     . CYS A 1 46  ? -7.262  -16.614 -11.345 1.00 23.60  ? 46   CYS A N     1 
ATOM   359  C  CA    . CYS A 1 46  ? -8.240  -16.752 -10.271 1.00 20.36  ? 46   CYS A CA    1 
ATOM   360  C  C     . CYS A 1 46  ? -9.611  -16.263 -10.711 1.00 22.23  ? 46   CYS A C     1 
ATOM   361  O  O     . CYS A 1 46  ? -9.735  -15.229 -11.367 1.00 23.15  ? 46   CYS A O     1 
ATOM   362  C  CB    . CYS A 1 46  ? -7.794  -15.973 -9.042  1.00 19.35  ? 46   CYS A CB    1 
ATOM   363  S  SG    . CYS A 1 46  ? -6.277  -16.575 -8.330  1.00 20.59  ? 46   CYS A SG    1 
ATOM   364  N  N     . ASP A 1 47  ? -10.651 -17.010 -10.335 1.00 21.58  ? 47   ASP A N     1 
ATOM   365  C  CA    . ASP A 1 47  ? -12.016 -16.561 -10.558 1.00 24.76  ? 47   ASP A CA    1 
ATOM   366  C  C     . ASP A 1 47  ? -12.723 -16.138 -9.277  1.00 20.33  ? 47   ASP A C     1 
ATOM   367  O  O     . ASP A 1 47  ? -13.845 -15.644 -9.349  1.00 25.00  ? 47   ASP A O     1 
ATOM   368  C  CB    . ASP A 1 47  ? -12.834 -17.636 -11.295 1.00 24.12  ? 47   ASP A CB    1 
ATOM   369  C  CG    . ASP A 1 47  ? -13.029 -18.930 -10.499 1.00 26.21  ? 47   ASP A CG    1 
ATOM   370  O  OD1   . ASP A 1 47  ? -12.862 -18.990 -9.259  1.00 25.57  ? 47   ASP A OD1   1 
ATOM   371  O  OD2   . ASP A 1 47  ? -13.376 -19.922 -11.161 1.00 30.69  ? 47   ASP A OD2   1 
ATOM   372  N  N     . GLY A 1 48  ? -12.092 -16.293 -8.117  1.00 20.70  ? 48   GLY A N     1 
ATOM   373  C  CA    . GLY A 1 48  ? -12.712 -15.855 -6.879  1.00 23.84  ? 48   GLY A CA    1 
ATOM   374  C  C     . GLY A 1 48  ? -13.839 -16.728 -6.380  1.00 24.95  ? 48   GLY A C     1 
ATOM   375  O  O     . GLY A 1 48  ? -14.521 -16.342 -5.423  1.00 25.19  ? 48   GLY A O     1 
ATOM   376  N  N     . SER A 1 49  ? -14.052 -17.897 -6.980  1.00 27.89  ? 49   SER A N     1 
ATOM   377  C  CA    . SER A 1 49  ? -15.176 -18.747 -6.607  1.00 26.36  ? 49   SER A CA    1 
ATOM   378  C  C     . SER A 1 49  ? -14.919 -19.464 -5.283  1.00 27.56  ? 49   SER A C     1 
ATOM   379  O  O     . SER A 1 49  ? -13.784 -19.616 -4.836  1.00 25.89  ? 49   SER A O     1 
ATOM   380  C  CB    . SER A 1 49  ? -15.447 -19.785 -7.695  1.00 27.06  ? 49   SER A CB    1 
ATOM   381  O  OG    . SER A 1 49  ? -14.393 -20.737 -7.755  1.00 25.31  ? 49   SER A OG    1 
ATOM   382  N  N     . GLU A 1 50  ? -16.008 -19.924 -4.657  1.00 30.43  ? 50   GLU A N     1 
ATOM   383  C  CA    . GLU A 1 50  ? -15.868 -20.735 -3.451  1.00 26.50  ? 50   GLU A CA    1 
ATOM   384  C  C     . GLU A 1 50  ? -15.157 -22.051 -3.750  1.00 30.98  ? 50   GLU A C     1 
ATOM   385  O  O     . GLU A 1 50  ? -14.354 -22.531 -2.938  1.00 28.48  ? 50   GLU A O     1 
ATOM   386  C  CB    . GLU A 1 50  ? -17.243 -20.991 -2.826  1.00 29.04  ? 50   GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 50  ? -17.839 -19.775 -2.138  1.00 37.98  ? 50   GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 50  ? -16.996 -19.322 -0.956  1.00 53.42  ? 50   GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 50  ? -16.329 -20.185 -0.339  1.00 55.33  ? 50   GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 50  ? -16.993 -18.109 -0.649  1.00 57.48  ? 50   GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 51  ? -15.430 -22.646 -4.917  1.00 27.16  ? 51   GLU A N     1 
ATOM   392  C  CA    . GLU A 1 51  ? -14.767 -23.893 -5.298  1.00 31.25  ? 51   GLU A CA    1 
ATOM   393  C  C     . GLU A 1 51  ? -13.262 -23.708 -5.364  1.00 33.76  ? 51   GLU A C     1 
ATOM   394  O  O     . GLU A 1 51  ? -12.496 -24.531 -4.851  1.00 29.38  ? 51   GLU A O     1 
ATOM   395  C  CB    . GLU A 1 51  ? -15.286 -24.391 -6.651  1.00 32.50  ? 51   GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 51  ? -16.737 -24.845 -6.675  1.00 46.39  ? 51   GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 51  ? -17.738 -23.699 -6.561  1.00 54.65  ? 51   GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 51  ? -17.363 -22.531 -6.821  1.00 42.30  ? 51   GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 51  ? -18.908 -23.977 -6.206  1.00 63.05  ? 51   GLU A OE2   1 
ATOM   400  N  N     . GLU A 1 52  ? -12.819 -22.626 -6.005  1.00 29.25  ? 52   GLU A N     1 
ATOM   401  C  CA    . GLU A 1 52  ? -11.394 -22.359 -6.105  1.00 26.88  ? 52   GLU A CA    1 
ATOM   402  C  C     . GLU A 1 52  ? -10.773 -22.181 -4.725  1.00 26.73  ? 52   GLU A C     1 
ATOM   403  O  O     . GLU A 1 52  ? -9.706  -22.734 -4.433  1.00 25.08  ? 52   GLU A O     1 
ATOM   404  C  CB    . GLU A 1 52  ? -11.185 -21.119 -6.973  1.00 26.56  ? 52   GLU A CB    1 
ATOM   405  C  CG    . GLU A 1 52  ? -9.901  -20.399 -6.733  1.00 21.10  ? 52   GLU A CG    1 
ATOM   406  C  CD    . GLU A 1 52  ? -9.792  -19.159 -7.589  1.00 24.89  ? 52   GLU A CD    1 
ATOM   407  O  OE1   . GLU A 1 52  ? -9.450  -19.296 -8.784  1.00 24.69  ? 52   GLU A OE1   1 
ATOM   408  O  OE2   . GLU A 1 52  ? -10.055 -18.057 -7.068  1.00 27.61  ? 52   GLU A OE2   1 
ATOM   409  N  N     . TYR A 1 53  ? -11.446 -21.425 -3.859  1.00 27.77  ? 53   TYR A N     1 
ATOM   410  C  CA    . TYR A 1 53  ? -10.948 -21.198 -2.509  1.00 27.78  ? 53   TYR A CA    1 
ATOM   411  C  C     . TYR A 1 53  ? -10.802 -22.509 -1.756  1.00 27.09  ? 53   TYR A C     1 
ATOM   412  O  O     . TYR A 1 53  ? -9.783  -22.740 -1.096  1.00 24.71  ? 53   TYR A O     1 
ATOM   413  C  CB    . TYR A 1 53  ? -11.898 -20.244 -1.778  1.00 28.77  ? 53   TYR A CB    1 
ATOM   414  C  CG    . TYR A 1 53  ? -11.418 -19.728 -0.442  1.00 29.78  ? 53   TYR A CG    1 
ATOM   415  C  CD1   . TYR A 1 53  ? -10.226 -19.033 -0.329  1.00 30.79  ? 53   TYR A CD1   1 
ATOM   416  C  CD2   . TYR A 1 53  ? -12.184 -19.898 0.699   1.00 36.75  ? 53   TYR A CD2   1 
ATOM   417  C  CE1   . TYR A 1 53  ? -9.798  -18.549 0.884   1.00 29.57  ? 53   TYR A CE1   1 
ATOM   418  C  CE2   . TYR A 1 53  ? -11.765 -19.417 1.912   1.00 37.64  ? 53   TYR A CE2   1 
ATOM   419  C  CZ    . TYR A 1 53  ? -10.571 -18.742 1.999   1.00 33.52  ? 53   TYR A CZ    1 
ATOM   420  O  OH    . TYR A 1 53  ? -10.152 -18.257 3.215   1.00 38.77  ? 53   TYR A OH    1 
ATOM   421  N  N     . GLY A 1 54  ? -11.807 -23.386 -1.856  1.00 28.96  ? 54   GLY A N     1 
ATOM   422  C  CA    . GLY A 1 54  ? -11.702 -24.691 -1.223  1.00 30.22  ? 54   GLY A CA    1 
ATOM   423  C  C     . GLY A 1 54  ? -10.500 -25.474 -1.715  1.00 32.58  ? 54   GLY A C     1 
ATOM   424  O  O     . GLY A 1 54  ? -9.789  -26.097 -0.923  1.00 34.85  ? 54   GLY A O     1 
ATOM   425  N  N     . ARG A 1 55  ? -10.242 -25.432 -3.029  1.00 29.53  ? 55   ARG A N     1 
ATOM   426  C  CA    . ARG A 1 55  ? -9.085  -26.123 -3.594  1.00 27.55  ? 55   ARG A CA    1 
ATOM   427  C  C     . ARG A 1 55  ? -7.769  -25.553 -3.072  1.00 36.17  ? 55   ARG A C     1 
ATOM   428  O  O     . ARG A 1 55  ? -6.851  -26.319 -2.749  1.00 34.56  ? 55   ARG A O     1 
ATOM   429  C  CB    . ARG A 1 55  ? -9.117  -26.054 -5.122  1.00 37.56  ? 55   ARG A CB    1 
ATOM   430  C  CG    . ARG A 1 55  ? -10.200 -26.905 -5.746  1.00 44.09  ? 55   ARG A CG    1 
ATOM   431  C  CD    . ARG A 1 55  ? -10.127 -26.929 -7.273  1.00 54.95  ? 55   ARG A CD    1 
ATOM   432  N  NE    . ARG A 1 55  ? -11.200 -27.760 -7.813  1.00 64.15  ? 55   ARG A NE    1 
ATOM   433  C  CZ    . ARG A 1 55  ? -12.415 -27.315 -8.106  1.00 61.38  ? 55   ARG A CZ    1 
ATOM   434  N  NH1   . ARG A 1 55  ? -12.724 -26.032 -8.002  1.00 56.25  ? 55   ARG A NH1   1 
ATOM   435  N  NH2   . ARG A 1 55  ? -13.343 -28.178 -8.510  1.00 65.38  ? 55   ARG A NH2   1 
ATOM   436  N  N     . LEU A 1 56  ? -7.643  -24.219 -3.004  1.00 25.90  ? 56   LEU A N     1 
ATOM   437  C  CA    . LEU A 1 56  ? -6.416  -23.619 -2.480  1.00 27.18  ? 56   LEU A CA    1 
ATOM   438  C  C     . LEU A 1 56  ? -6.164  -24.046 -1.039  1.00 25.66  ? 56   LEU A C     1 
ATOM   439  O  O     . LEU A 1 56  ? -5.041  -24.411 -0.675  1.00 29.25  ? 56   LEU A O     1 
ATOM   440  C  CB    . LEU A 1 56  ? -6.483  -22.093 -2.551  1.00 32.42  ? 56   LEU A CB    1 
ATOM   441  C  CG    . LEU A 1 56  ? -6.794  -21.325 -3.826  1.00 38.52  ? 56   LEU A CG    1 
ATOM   442  C  CD1   . LEU A 1 56  ? -7.178  -19.912 -3.428  1.00 40.72  ? 56   LEU A CD1   1 
ATOM   443  C  CD2   . LEU A 1 56  ? -5.599  -21.300 -4.748  1.00 35.32  ? 56   LEU A CD2   1 
ATOM   444  N  N     . LEU A 1 57  ? -7.182  -23.914 -0.183  1.00 27.82  ? 57   LEU A N     1 
ATOM   445  C  CA    . LEU A 1 57  ? -7.080  -24.393 1.193   1.00 32.33  ? 57   LEU A CA    1 
ATOM   446  C  C     . LEU A 1 57  ? -6.655  -25.859 1.245   1.00 29.88  ? 57   LEU A C     1 
ATOM   447  O  O     . LEU A 1 57  ? -5.699  -26.217 1.943   1.00 33.84  ? 57   LEU A O     1 
ATOM   448  C  CB    . LEU A 1 57  ? -8.417  -24.209 1.908   1.00 26.81  ? 57   LEU A CB    1 
ATOM   449  C  CG    . LEU A 1 57  ? -8.813  -22.750 2.071   1.00 24.71  ? 57   LEU A CG    1 
ATOM   450  C  CD1   . LEU A 1 57  ? -10.213 -22.662 2.645   1.00 33.30  ? 57   LEU A CD1   1 
ATOM   451  C  CD2   . LEU A 1 57  ? -7.811  -22.057 2.969   1.00 28.55  ? 57   LEU A CD2   1 
ATOM   452  N  N     . ALA A 1 58  ? -7.373  -26.725 0.525   1.00 30.36  ? 58   ALA A N     1 
ATOM   453  C  CA    . ALA A 1 58  ? -7.015  -28.146 0.492   1.00 31.25  ? 58   ALA A CA    1 
ATOM   454  C  C     . ALA A 1 58  ? -5.565  -28.340 0.068   1.00 29.14  ? 58   ALA A C     1 
ATOM   455  O  O     . ALA A 1 58  ? -4.823  -29.107 0.690   1.00 29.81  ? 58   ALA A O     1 
ATOM   456  C  CB    . ALA A 1 58  ? -7.947  -28.903 -0.453  1.00 31.87  ? 58   ALA A CB    1 
ATOM   457  N  N     . HIS A 1 59  ? -5.138  -27.626 -0.973  1.00 25.59  ? 59   HIS A N     1 
ATOM   458  C  CA    . HIS A 1 59  ? -3.757  -27.714 -1.441  1.00 27.01  ? 59   HIS A CA    1 
ATOM   459  C  C     . HIS A 1 59  ? -2.767  -27.308 -0.356  1.00 36.01  ? 59   HIS A C     1 
ATOM   460  O  O     . HIS A 1 59  ? -1.785  -28.018 -0.091  1.00 29.24  ? 59   HIS A O     1 
ATOM   461  C  CB    . HIS A 1 59  ? -3.583  -26.828 -2.671  1.00 28.12  ? 59   HIS A CB    1 
ATOM   462  C  CG    . HIS A 1 59  ? -2.173  -26.747 -3.173  1.00 37.05  ? 59   HIS A CG    1 
ATOM   463  N  ND1   . HIS A 1 59  ? -1.434  -27.864 -3.507  1.00 35.66  ? 59   HIS A ND1   1 
ATOM   464  C  CD2   . HIS A 1 59  ? -1.378  -25.679 -3.423  1.00 38.14  ? 59   HIS A CD2   1 
ATOM   465  C  CE1   . HIS A 1 59  ? -0.239  -27.487 -3.926  1.00 38.07  ? 59   HIS A CE1   1 
ATOM   466  N  NE2   . HIS A 1 59  ? -0.181  -26.166 -3.889  1.00 44.04  ? 59   HIS A NE2   1 
ATOM   467  N  N     . MET A 1 60  ? -2.990  -26.139 0.258   1.00 32.50  ? 60   MET A N     1 
ATOM   468  C  CA    . MET A 1 60  ? -2.075  -25.639 1.278   1.00 24.82  ? 60   MET A CA    1 
ATOM   469  C  C     . MET A 1 60  ? -2.026  -26.564 2.477   1.00 25.01  ? 60   MET A C     1 
ATOM   470  O  O     . MET A 1 60  ? -0.988  -26.667 3.139   1.00 30.22  ? 60   MET A O     1 
ATOM   471  C  CB    . MET A 1 60  ? -2.495  -24.229 1.716   1.00 25.72  ? 60   MET A CB    1 
ATOM   472  C  CG    . MET A 1 60  ? -1.973  -23.138 0.787   1.00 24.65  ? 60   MET A CG    1 
ATOM   473  S  SD    . MET A 1 60  ? -2.404  -21.491 1.376   1.00 27.73  ? 60   MET A SD    1 
ATOM   474  C  CE    . MET A 1 60  ? -4.172  -21.426 1.067   1.00 21.54  ? 60   MET A CE    1 
ATOM   475  N  N     . GLN A 1 61  ? -3.141  -27.222 2.788   1.00 25.05  ? 61   GLN A N     1 
ATOM   476  C  CA    . GLN A 1 61  ? -3.145  -28.163 3.899   1.00 32.35  ? 61   GLN A CA    1 
ATOM   477  C  C     . GLN A 1 61  ? -2.339  -29.405 3.548   1.00 38.28  ? 61   GLN A C     1 
ATOM   478  O  O     . GLN A 1 61  ? -1.590  -29.929 4.384   1.00 34.77  ? 61   GLN A O     1 
ATOM   479  C  CB    . GLN A 1 61  ? -4.579  -28.536 4.263   1.00 31.72  ? 61   GLN A CB    1 
ATOM   480  C  CG    . GLN A 1 61  ? -4.731  -29.163 5.635   1.00 39.18  ? 61   GLN A CG    1 
ATOM   481  C  CD    . GLN A 1 61  ? -6.171  -29.537 5.933   1.00 39.64  ? 61   GLN A CD    1 
ATOM   482  O  OE1   . GLN A 1 61  ? -7.005  -29.586 5.027   1.00 45.82  ? 61   GLN A OE1   1 
ATOM   483  N  NE2   . GLN A 1 61  ? -6.473  -29.794 7.206   1.00 40.83  ? 61   GLN A NE2   1 
ATOM   484  N  N     . GLU A 1 62  ? -2.468  -29.874 2.305   1.00 35.53  ? 62   GLU A N     1 
ATOM   485  C  CA    . GLU A 1 62  ? -1.689  -31.024 1.855   1.00 39.81  ? 62   GLU A CA    1 
ATOM   486  C  C     . GLU A 1 62  ? -0.194  -30.711 1.804   1.00 39.29  ? 62   GLU A C     1 
ATOM   487  O  O     . GLU A 1 62  ? 0.626   -31.605 2.039   1.00 46.01  ? 62   GLU A O     1 
ATOM   488  C  CB    . GLU A 1 62  ? -2.220  -31.497 0.496   1.00 30.22  ? 62   GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 62  ? -3.632  -32.105 0.587   1.00 34.00  ? 62   GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 62  ? -4.382  -32.155 -0.744  1.00 36.43  ? 62   GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 62  ? -3.776  -31.872 -1.794  1.00 30.32  ? 62   GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 62  ? -5.592  -32.472 -0.733  1.00 42.66  ? 62   GLU A OE2   1 
ATOM   493  N  N     . GLU A 1 63  ? 0.184   -29.456 1.540   1.00 35.61  ? 63   GLU A N     1 
ATOM   494  C  CA    . GLU A 1 63  ? 1.595   -29.067 1.510   1.00 36.58  ? 63   GLU A CA    1 
ATOM   495  C  C     . GLU A 1 63  ? 2.142   -28.676 2.878   1.00 37.94  ? 63   GLU A C     1 
ATOM   496  O  O     . GLU A 1 63  ? 3.304   -28.268 2.971   1.00 43.22  ? 63   GLU A O     1 
ATOM   497  C  CB    . GLU A 1 63  ? 1.819   -27.894 0.552   1.00 30.23  ? 63   GLU A CB    1 
ATOM   498  C  CG    . GLU A 1 63  ? 1.381   -28.129 -0.877  1.00 39.85  ? 63   GLU A CG    1 
ATOM   499  C  CD    . GLU A 1 63  ? 2.327   -29.042 -1.621  1.00 43.38  ? 63   GLU A CD    1 
ATOM   500  O  OE1   . GLU A 1 63  ? 2.274   -30.256 -1.361  1.00 39.57  ? 63   GLU A OE1   1 
ATOM   501  O  OE2   . GLU A 1 63  ? 3.124   -28.539 -2.442  1.00 47.02  ? 63   GLU A OE2   1 
ATOM   502  N  N     . GLY A 1 64  ? 1.335   -28.757 3.930   1.00 37.04  ? 64   GLY A N     1 
ATOM   503  C  CA    . GLY A 1 64  ? 1.781   -28.323 5.237   1.00 40.58  ? 64   GLY A CA    1 
ATOM   504  C  C     . GLY A 1 64  ? 1.916   -26.826 5.412   1.00 36.54  ? 64   GLY A C     1 
ATOM   505  O  O     . GLY A 1 64  ? 2.581   -26.386 6.353   1.00 37.71  ? 64   GLY A O     1 
ATOM   506  N  N     . VAL A 1 65  ? 1.313   -26.022 4.536   1.00 28.98  ? 65   VAL A N     1 
ATOM   507  C  CA    . VAL A 1 65  ? 1.423   -24.574 4.697   1.00 36.44  ? 65   VAL A CA    1 
ATOM   508  C  C     . VAL A 1 65  ? 0.439   -24.068 5.748   1.00 36.53  ? 65   VAL A C     1 
ATOM   509  O  O     . VAL A 1 65  ? 0.770   -23.180 6.544   1.00 38.23  ? 65   VAL A O     1 
ATOM   510  C  CB    . VAL A 1 65  ? 1.230   -23.861 3.346   1.00 30.16  ? 65   VAL A CB    1 
ATOM   511  C  CG1   . VAL A 1 65  ? 1.381   -22.361 3.521   1.00 31.39  ? 65   VAL A CG1   1 
ATOM   512  C  CG2   . VAL A 1 65  ? 2.240   -24.370 2.339   1.00 34.83  ? 65   VAL A CG2   1 
ATOM   513  N  N     . ILE A 1 66  ? -0.782  -24.609 5.772   1.00 27.05  ? 66   ILE A N     1 
ATOM   514  C  CA    . ILE A 1 66  ? -1.777  -24.208 6.759   1.00 25.74  ? 66   ILE A CA    1 
ATOM   515  C  C     . ILE A 1 66  ? -2.304  -25.443 7.467   1.00 30.85  ? 66   ILE A C     1 
ATOM   516  O  O     . ILE A 1 66  ? -2.223  -26.565 6.962   1.00 27.30  ? 66   ILE A O     1 
ATOM   517  C  CB    . ILE A 1 66  ? -2.963  -23.427 6.155   1.00 27.78  ? 66   ILE A CB    1 
ATOM   518  C  CG1   . ILE A 1 66  ? -3.741  -24.307 5.182   1.00 26.23  ? 66   ILE A CG1   1 
ATOM   519  C  CG2   . ILE A 1 66  ? -2.497  -22.147 5.475   1.00 29.77  ? 66   ILE A CG2   1 
ATOM   520  C  CD1   . ILE A 1 66  ? -4.942  -23.610 4.604   1.00 32.72  ? 66   ILE A CD1   1 
ATOM   521  N  N     . ARG A 1 67  ? -2.865  -25.205 8.648   1.00 23.47  ? 67   ARG A N     1 
ATOM   522  C  CA    . ARG A 1 67  ? -3.539  -26.212 9.455   1.00 29.60  ? 67   ARG A CA    1 
ATOM   523  C  C     . ARG A 1 67  ? -4.986  -25.803 9.683   1.00 31.70  ? 67   ARG A C     1 
ATOM   524  O  O     . ARG A 1 67  ? -5.280  -24.620 9.899   1.00 23.91  ? 67   ARG A O     1 
ATOM   525  C  CB    . ARG A 1 67  ? -2.866  -26.371 10.816  1.00 34.52  ? 67   ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 67  ? -1.467  -26.924 10.786  1.00 38.51  ? 67   ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 67  ? -0.894  -26.985 12.201  1.00 50.76  ? 67   ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 67  ? -1.872  -27.470 13.173  1.00 54.04  ? 67   ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 67  ? -2.157  -28.749 13.393  1.00 59.89  ? 67   ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 67  ? -1.568  -29.720 12.709  1.00 69.42  ? 67   ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 67  ? -3.053  -29.064 14.326  1.00 48.63  ? 67   ARG A NH2   1 
ATOM   532  N  N     . LYS A 1 68  ? -5.885  -26.784 9.674   1.00 26.34  ? 68   LYS A N     1 
ATOM   533  C  CA    . LYS A 1 68  ? -7.273  -26.520 10.014  1.00 26.93  ? 68   LYS A CA    1 
ATOM   534  C  C     . LYS A 1 68  ? -7.424  -26.375 11.521  1.00 24.21  ? 68   LYS A C     1 
ATOM   535  O  O     . LYS A 1 68  ? -6.852  -27.147 12.293  1.00 33.15  ? 68   LYS A O     1 
ATOM   536  C  CB    . LYS A 1 68  ? -8.181  -27.638 9.506   1.00 34.35  ? 68   LYS A CB    1 
ATOM   537  C  CG    . LYS A 1 68  ? -9.633  -27.231 9.338   1.00 33.71  ? 68   LYS A CG    1 
ATOM   538  C  CD    . LYS A 1 68  ? -10.362 -28.271 8.498   1.00 39.64  ? 68   LYS A CD    1 
ATOM   539  C  CE    . LYS A 1 68  ? -11.685 -27.760 7.964   1.00 41.14  ? 68   LYS A CE    1 
ATOM   540  N  NZ    . LYS A 1 68  ? -12.657 -27.482 9.047   1.00 48.11  ? 68   LYS A NZ    1 
ATOM   541  N  N     . LEU A 1 69  ? -8.183  -25.360 11.932  1.00 27.05  ? 69   LEU A N     1 
ATOM   542  C  CA    . LEU A 1 69  ? -8.524  -25.106 13.334  1.00 31.65  ? 69   LEU A CA    1 
ATOM   543  C  C     . LEU A 1 69  ? -9.906  -25.715 13.552  1.00 32.68  ? 69   LEU A C     1 
ATOM   544  O  O     . LEU A 1 69  ? -10.933 -25.077 13.311  1.00 31.61  ? 69   LEU A O     1 
ATOM   545  C  CB    . LEU A 1 69  ? -8.496  -23.612 13.652  1.00 23.61  ? 69   LEU A CB    1 
ATOM   546  C  CG    . LEU A 1 69  ? -7.128  -22.925 13.532  1.00 22.25  ? 69   LEU A CG    1 
ATOM   547  C  CD1   . LEU A 1 69  ? -7.245  -21.403 13.473  1.00 24.84  ? 69   LEU A CD1   1 
ATOM   548  C  CD2   . LEU A 1 69  ? -6.206  -23.350 14.661  1.00 27.83  ? 69   LEU A CD2   1 
ATOM   549  N  N     . LYS A 1 70  ? -9.925  -26.971 14.007  1.00 31.62  ? 70   LYS A N     1 
ATOM   550  C  CA    . LYS A 1 70  ? -11.170 -27.735 14.030  1.00 30.72  ? 70   LYS A CA    1 
ATOM   551  C  C     . LYS A 1 70  ? -12.200 -27.175 15.005  1.00 32.26  ? 70   LYS A C     1 
ATOM   552  O  O     . LYS A 1 70  ? -13.396 -27.434 14.840  1.00 32.37  ? 70   LYS A O     1 
ATOM   553  C  CB    . LYS A 1 70  ? -10.880 -29.204 14.355  1.00 40.28  ? 70   LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 70  ? -9.942  -29.419 15.531  1.00 47.50  ? 70   LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 70  ? -9.954  -30.869 16.017  1.00 53.92  ? 70   LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 70  ? -8.803  -31.140 16.987  1.00 57.26  ? 70   LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 70  ? -8.917  -32.479 17.631  1.00 60.96  ? 70   LYS A NZ    1 
ATOM   558  N  N     . LYS A 1 71  ? -11.780 -26.403 16.001  1.00 25.29  ? 71   LYS A N     1 
ATOM   559  C  CA    . LYS A 1 71  ? -12.744 -25.839 16.932  1.00 19.39  ? 71   LYS A CA    1 
ATOM   560  C  C     . LYS A 1 71  ? -13.708 -24.860 16.267  1.00 31.78  ? 71   LYS A C     1 
ATOM   561  O  O     . LYS A 1 71  ? -14.805 -24.653 16.789  1.00 26.62  ? 71   LYS A O     1 
ATOM   562  C  CB    . LYS A 1 71  ? -11.999 -25.158 18.073  1.00 29.97  ? 71   LYS A CB    1 
ATOM   563  C  CG    . LYS A 1 71  ? -12.849 -24.689 19.232  1.00 26.41  ? 71   LYS A CG    1 
ATOM   564  C  CD    . LYS A 1 71  ? -11.925 -24.438 20.404  1.00 30.27  ? 71   LYS A CD    1 
ATOM   565  C  CE    . LYS A 1 71  ? -12.682 -24.055 21.630  1.00 42.53  ? 71   LYS A CE    1 
ATOM   566  N  NZ    . LYS A 1 71  ? -12.020 -24.647 22.824  1.00 47.71  ? 71   LYS A NZ    1 
ATOM   567  N  N     . TYR A 1 72  ? -13.340 -24.257 15.133  1.00 28.60  ? 72   TYR A N     1 
ATOM   568  C  CA    . TYR A 1 72  ? -14.150 -23.208 14.524  1.00 23.13  ? 72   TYR A CA    1 
ATOM   569  C  C     . TYR A 1 72  ? -14.636 -23.642 13.138  1.00 25.69  ? 72   TYR A C     1 
ATOM   570  O  O     . TYR A 1 72  ? -14.320 -24.726 12.637  1.00 34.16  ? 72   TYR A O     1 
ATOM   571  C  CB    . TYR A 1 72  ? -13.370 -21.884 14.462  1.00 24.05  ? 72   TYR A CB    1 
ATOM   572  C  CG    . TYR A 1 72  ? -12.680 -21.545 15.770  1.00 23.50  ? 72   TYR A CG    1 
ATOM   573  C  CD1   . TYR A 1 72  ? -13.417 -21.271 16.921  1.00 28.11  ? 72   TYR A CD1   1 
ATOM   574  C  CD2   . TYR A 1 72  ? -11.293 -21.521 15.860  1.00 25.21  ? 72   TYR A CD2   1 
ATOM   575  C  CE1   . TYR A 1 72  ? -12.788 -20.981 18.122  1.00 28.87  ? 72   TYR A CE1   1 
ATOM   576  C  CE2   . TYR A 1 72  ? -10.655 -21.234 17.055  1.00 25.02  ? 72   TYR A CE2   1 
ATOM   577  C  CZ    . TYR A 1 72  ? -11.411 -20.966 18.183  1.00 24.87  ? 72   TYR A CZ    1 
ATOM   578  O  OH    . TYR A 1 72  ? -10.779 -20.669 19.365  1.00 27.78  ? 72   TYR A OH    1 
ATOM   579  N  N     . ASP A 1 73  ? -15.422 -22.772 12.533  1.00 23.97  ? 73   ASP A N     1 
ATOM   580  C  CA    . ASP A 1 73  ? -16.071 -23.001 11.246  1.00 24.61  ? 73   ASP A CA    1 
ATOM   581  C  C     . ASP A 1 73  ? -15.195 -22.395 10.150  1.00 26.32  ? 73   ASP A C     1 
ATOM   582  O  O     . ASP A 1 73  ? -15.177 -21.174 9.966   1.00 25.90  ? 73   ASP A O     1 
ATOM   583  C  CB    . ASP A 1 73  ? -17.461 -22.369 11.279  1.00 32.85  ? 73   ASP A CB    1 
ATOM   584  C  CG    . ASP A 1 73  ? -18.283 -22.663 10.044  1.00 41.77  ? 73   ASP A CG    1 
ATOM   585  O  OD1   . ASP A 1 73  ? -17.706 -23.038 9.007   1.00 41.00  ? 73   ASP A OD1   1 
ATOM   586  O  OD2   . ASP A 1 73  ? -19.525 -22.509 10.116  1.00 54.46  ? 73   ASP A OD2   1 
ATOM   587  N  N     . ASN A 1 74  ? -14.459 -23.243 9.425   1.00 22.68  ? 74   ASN A N     1 
ATOM   588  C  CA    . ASN A 1 74  ? -13.663 -22.810 8.266   1.00 23.83  ? 74   ASN A CA    1 
ATOM   589  C  C     . ASN A 1 74  ? -12.608 -21.766 8.656   1.00 23.15  ? 74   ASN A C     1 
ATOM   590  O  O     . ASN A 1 74  ? -12.464 -20.719 8.021   1.00 25.67  ? 74   ASN A O     1 
ATOM   591  C  CB    . ASN A 1 74  ? -14.576 -22.283 7.150   1.00 22.48  ? 74   ASN A CB    1 
ATOM   592  C  CG    . ASN A 1 74  ? -13.832 -22.036 5.829   1.00 27.95  ? 74   ASN A CG    1 
ATOM   593  O  OD1   . ASN A 1 74  ? -12.932 -22.791 5.447   1.00 33.10  ? 74   ASN A OD1   1 
ATOM   594  N  ND2   . ASN A 1 74  ? -14.203 -20.961 5.138   1.00 30.50  ? 74   ASN A ND2   1 
ATOM   595  N  N     . CYS A 1 75  ? -11.855 -22.056 9.710   1.00 22.60  ? 75   CYS A N     1 
ATOM   596  C  CA    . CYS A 1 75  ? -10.739 -21.213 10.115  1.00 26.36  ? 75   CYS A CA    1 
ATOM   597  C  C     . CYS A 1 75  ? -9.455  -22.015 9.999   1.00 26.16  ? 75   CYS A C     1 
ATOM   598  O  O     . CYS A 1 75  ? -9.460  -23.239 10.141  1.00 23.80  ? 75   CYS A O     1 
ATOM   599  C  CB    . CYS A 1 75  ? -10.890 -20.695 11.547  1.00 21.63  ? 75   CYS A CB    1 
ATOM   600  S  SG    . CYS A 1 75  ? -12.260 -19.595 11.805  1.00 22.77  ? 75   CYS A SG    1 
ATOM   601  N  N     . TRP A 1 76  ? -8.357  -21.313 9.738   1.00 21.30  ? 76   TRP A N     1 
ATOM   602  C  CA    . TRP A 1 76  ? -7.098  -21.930 9.351   1.00 20.01  ? 76   TRP A CA    1 
ATOM   603  C  C     . TRP A 1 76  ? -5.947  -21.166 9.978   1.00 25.04  ? 76   TRP A C     1 
ATOM   604  O  O     . TRP A 1 76  ? -6.025  -19.952 10.189  1.00 20.90  ? 76   TRP A O     1 
ATOM   605  C  CB    . TRP A 1 76  ? -6.933  -21.944 7.830   1.00 22.46  ? 76   TRP A CB    1 
ATOM   606  C  CG    . TRP A 1 76  ? -8.071  -22.577 7.135   1.00 20.97  ? 76   TRP A CG    1 
ATOM   607  C  CD1   . TRP A 1 76  ? -9.241  -21.990 6.781   1.00 21.26  ? 76   TRP A CD1   1 
ATOM   608  C  CD2   . TRP A 1 76  ? -8.154  -23.937 6.702   1.00 25.36  ? 76   TRP A CD2   1 
ATOM   609  N  NE1   . TRP A 1 76  ? -10.064 -22.899 6.156   1.00 22.44  ? 76   TRP A NE1   1 
ATOM   610  C  CE2   . TRP A 1 76  ? -9.416  -24.106 6.097   1.00 28.03  ? 76   TRP A CE2   1 
ATOM   611  C  CE3   . TRP A 1 76  ? -7.289  -25.033 6.779   1.00 31.69  ? 76   TRP A CE3   1 
ATOM   612  C  CZ2   . TRP A 1 76  ? -9.830  -25.325 5.564   1.00 32.57  ? 76   TRP A CZ2   1 
ATOM   613  C  CZ3   . TRP A 1 76  ? -7.697  -26.246 6.239   1.00 33.49  ? 76   TRP A CZ3   1 
ATOM   614  C  CH2   . TRP A 1 76  ? -8.956  -26.382 5.645   1.00 29.17  ? 76   TRP A CH2   1 
ATOM   615  N  N     . LEU A 1 77  ? -4.872  -21.885 10.258  1.00 22.99  ? 77   LEU A N     1 
ATOM   616  C  CA    . LEU A 1 77  ? -3.683  -21.321 10.884  1.00 22.94  ? 77   LEU A CA    1 
ATOM   617  C  C     . LEU A 1 77  ? -2.481  -21.490 9.964   1.00 25.88  ? 77   LEU A C     1 
ATOM   618  O  O     . LEU A 1 77  ? -2.229  -22.589 9.456   1.00 23.69  ? 77   LEU A O     1 
ATOM   619  C  CB    . LEU A 1 77  ? -3.408  -22.005 12.226  1.00 25.06  ? 77   LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 77  ? -2.146  -21.527 12.944  1.00 26.02  ? 77   LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 77  ? -2.293  -20.055 13.305  1.00 25.17  ? 77   LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 77  ? -1.886  -22.360 14.184  1.00 32.94  ? 77   LEU A CD2   1 
ATOM   623  N  N     . ALA A 1 78  ? -1.734  -20.414 9.765   1.00 21.91  ? 78   ALA A N     1 
ATOM   624  C  CA    . ALA A 1 78  ? -0.472  -20.460 9.039   1.00 24.31  ? 78   ALA A CA    1 
ATOM   625  C  C     . ALA A 1 78  ? 0.643   -19.986 9.958   1.00 24.14  ? 78   ALA A C     1 
ATOM   626  O  O     . ALA A 1 78  ? 0.486   -18.985 10.660  1.00 24.93  ? 78   ALA A O     1 
ATOM   627  C  CB    . ALA A 1 78  ? -0.531  -19.587 7.779   1.00 21.66  ? 78   ALA A CB    1 
ATOM   628  N  N     . LEU A 1 79  ? 1.766   -20.704 9.953   1.00 22.63  ? 79   LEU A N     1 
ATOM   629  C  CA    . LEU A 1 79  ? 2.955   -20.335 10.714  1.00 23.60  ? 79   LEU A CA    1 
ATOM   630  C  C     . LEU A 1 79  ? 4.064   -19.967 9.737   1.00 26.62  ? 79   LEU A C     1 
ATOM   631  O  O     . LEU A 1 79  ? 4.315   -20.704 8.779   1.00 34.22  ? 79   LEU A O     1 
ATOM   632  C  CB    . LEU A 1 79  ? 3.411   -21.478 11.619  1.00 25.55  ? 79   LEU A CB    1 
ATOM   633  C  CG    . LEU A 1 79  ? 2.337   -21.960 12.606  1.00 31.30  ? 79   LEU A CG    1 
ATOM   634  C  CD1   . LEU A 1 79  ? 2.872   -23.056 13.528  1.00 36.11  ? 79   LEU A CD1   1 
ATOM   635  C  CD2   . LEU A 1 79  ? 1.766   -20.784 13.406  1.00 25.30  ? 79   LEU A CD2   1 
ATOM   636  N  N     . THR A 1 80  ? 4.726   -18.841 9.979   1.00 23.58  ? 80   THR A N     1 
ATOM   637  C  CA    . THR A 1 80  ? 5.734   -18.340 9.057   1.00 27.38  ? 80   THR A CA    1 
ATOM   638  C  C     . THR A 1 80  ? 7.146   -18.635 9.557   1.00 33.58  ? 80   THR A C     1 
ATOM   639  O  O     . THR A 1 80  ? 7.375   -18.982 10.720  1.00 28.36  ? 80   THR A O     1 
ATOM   640  C  CB    . THR A 1 80  ? 5.587   -16.820 8.840   1.00 28.80  ? 80   THR A CB    1 
ATOM   641  O  OG1   . THR A 1 80  ? 6.063   -16.111 9.992   1.00 27.07  ? 80   THR A OG1   1 
ATOM   642  C  CG2   . THR A 1 80  ? 4.133   -16.424 8.565   1.00 22.23  ? 80   THR A CG2   1 
ATOM   643  N  N     . ASP A 1 81  ? 8.099   -18.474 8.647   1.00 29.35  ? 81   ASP A N     1 
ATOM   644  C  CA    . ASP A 1 81  ? 9.493   -18.335 9.027   1.00 33.25  ? 81   ASP A CA    1 
ATOM   645  C  C     . ASP A 1 81  ? 9.608   -17.182 10.017  1.00 29.51  ? 81   ASP A C     1 
ATOM   646  O  O     . ASP A 1 81  ? 9.052   -16.103 9.771   1.00 32.22  ? 81   ASP A O     1 
ATOM   647  C  CB    . ASP A 1 81  ? 10.346  -18.068 7.779   1.00 31.00  ? 81   ASP A CB    1 
ATOM   648  C  CG    . ASP A 1 81  ? 11.848  -18.171 8.037   1.00 37.21  ? 81   ASP A CG    1 
ATOM   649  O  OD1   . ASP A 1 81  ? 12.375  -17.406 8.870   1.00 32.71  ? 81   ASP A OD1   1 
ATOM   650  O  OD2   . ASP A 1 81  ? 12.503  -19.013 7.379   1.00 33.55  ? 81   ASP A OD2   1 
ATOM   651  N  N     . PRO A 1 82  ? 10.300  -17.361 11.143  1.00 31.92  ? 82   PRO A N     1 
ATOM   652  C  CA    . PRO A 1 82  ? 10.401  -16.265 12.118  1.00 32.68  ? 82   PRO A CA    1 
ATOM   653  C  C     . PRO A 1 82  ? 11.137  -15.031 11.599  1.00 36.51  ? 82   PRO A C     1 
ATOM   654  O  O     . PRO A 1 82  ? 11.083  -13.990 12.263  1.00 37.41  ? 82   PRO A O     1 
ATOM   655  C  CB    . PRO A 1 82  ? 11.133  -16.910 13.304  1.00 39.26  ? 82   PRO A CB    1 
ATOM   656  C  CG    . PRO A 1 82  ? 11.814  -18.118 12.736  1.00 40.84  ? 82   PRO A CG    1 
ATOM   657  C  CD    . PRO A 1 82  ? 10.947  -18.598 11.614  1.00 37.44  ? 82   PRO A CD    1 
ATOM   658  N  N     . ARG A 1 83  ? 11.796  -15.095 10.435  1.00 35.09  ? 83   ARG A N     1 
ATOM   659  C  CA    . ARG A 1 83  ? 12.396  -13.908 9.827   1.00 37.08  ? 83   ARG A CA    1 
ATOM   660  C  C     . ARG A 1 83  ? 11.424  -13.131 8.945   1.00 37.26  ? 83   ARG A C     1 
ATOM   661  O  O     . ARG A 1 83  ? 11.794  -12.073 8.425   1.00 33.20  ? 83   ARG A O     1 
ATOM   662  C  CB    . ARG A 1 83  ? 13.622  -14.294 8.990   1.00 37.01  ? 83   ARG A CB    1 
ATOM   663  C  CG    . ARG A 1 83  ? 14.734  -14.966 9.764   1.00 37.07  ? 83   ARG A CG    1 
ATOM   664  C  CD    . ARG A 1 83  ? 15.723  -15.623 8.814   1.00 36.12  ? 83   ARG A CD    1 
ATOM   665  N  NE    . ARG A 1 83  ? 15.111  -16.705 8.050   1.00 37.30  ? 83   ARG A NE    1 
ATOM   666  C  CZ    . ARG A 1 83  ? 15.718  -17.370 7.073   1.00 47.96  ? 83   ARG A CZ    1 
ATOM   667  N  NH1   . ARG A 1 83  ? 16.964  -17.096 6.721   1.00 52.91  ? 83   ARG A NH1   1 
ATOM   668  N  NH2   . ARG A 1 83  ? 15.060  -18.332 6.430   1.00 37.60  ? 83   ARG A NH2   1 
ATOM   669  N  N     . ASP A 1 84  ? 10.191  -13.623 8.769   1.00 29.05  ? 84   ASP A N     1 
ATOM   670  C  CA    . ASP A 1 84  ? 9.220   -13.054 7.833   1.00 32.17  ? 84   ASP A CA    1 
ATOM   671  C  C     . ASP A 1 84  ? 7.905   -12.826 8.583   1.00 30.93  ? 84   ASP A C     1 
ATOM   672  O  O     . ASP A 1 84  ? 6.941   -13.573 8.393   1.00 29.67  ? 84   ASP A O     1 
ATOM   673  C  CB    . ASP A 1 84  ? 9.016   -13.986 6.628   1.00 28.04  ? 84   ASP A CB    1 
ATOM   674  C  CG    . ASP A 1 84  ? 8.261   -13.321 5.501   1.00 27.89  ? 84   ASP A CG    1 
ATOM   675  O  OD1   . ASP A 1 84  ? 8.271   -12.076 5.472   1.00 32.30  ? 84   ASP A OD1   1 
ATOM   676  O  OD2   . ASP A 1 84  ? 7.654   -14.026 4.651   1.00 26.12  ? 84   ASP A OD2   1 
ATOM   677  N  N     . VAL A 1 85  ? 7.861   -11.792 9.429   1.00 28.45  ? 85   VAL A N     1 
ATOM   678  C  CA    . VAL A 1 85  ? 6.781   -11.645 10.396  1.00 28.55  ? 85   VAL A CA    1 
ATOM   679  C  C     . VAL A 1 85  ? 6.165   -10.253 10.420  1.00 32.78  ? 85   VAL A C     1 
ATOM   680  O  O     . VAL A 1 85  ? 5.300   -9.997  11.260  1.00 30.08  ? 85   VAL A O     1 
ATOM   681  C  CB    . VAL A 1 85  ? 7.253   -12.030 11.813  1.00 33.17  ? 85   VAL A CB    1 
ATOM   682  C  CG1   . VAL A 1 85  ? 7.632   -13.503 11.877  1.00 32.91  ? 85   VAL A CG1   1 
ATOM   683  C  CG2   . VAL A 1 85  ? 8.419   -11.144 12.237  1.00 32.38  ? 85   VAL A CG2   1 
ATOM   684  N  N     . ALA A 1 86  ? 6.566   -9.344  9.531   1.00 26.39  ? 86   ALA A N     1 
ATOM   685  C  CA    . ALA A 1 86  ? 6.085   -7.965  9.571   1.00 31.55  ? 86   ALA A CA    1 
ATOM   686  C  C     . ALA A 1 86  ? 6.508   -7.244  8.298   1.00 30.21  ? 86   ALA A C     1 
ATOM   687  O  O     . ALA A 1 86  ? 7.344   -7.731  7.532   1.00 25.33  ? 86   ALA A O     1 
ATOM   688  C  CB    . ALA A 1 86  ? 6.626   -7.215  10.792  1.00 31.52  ? 86   ALA A CB    1 
ATOM   689  N  N     . ARG A 1 87  ? 5.913   -6.067  8.088   1.00 32.64  ? 87   ARG A N     1 
ATOM   690  C  CA    . ARG A 1 87  ? 6.451   -5.114  7.129   1.00 30.52  ? 87   ARG A CA    1 
ATOM   691  C  C     . ARG A 1 87  ? 7.917   -4.852  7.431   1.00 38.54  ? 87   ARG A C     1 
ATOM   692  O  O     . ARG A 1 87  ? 8.326   -4.801  8.594   1.00 37.86  ? 87   ARG A O     1 
ATOM   693  C  CB    . ARG A 1 87  ? 5.689   -3.778  7.186   1.00 33.05  ? 87   ARG A CB    1 
ATOM   694  C  CG    . ARG A 1 87  ? 4.619   -3.590  6.115   1.00 26.82  ? 87   ARG A CG    1 
ATOM   695  C  CD    . ARG A 1 87  ? 3.993   -2.194  6.141   1.00 23.49  ? 87   ARG A CD    1 
ATOM   696  N  NE    . ARG A 1 87  ? 3.581   -1.777  7.476   1.00 24.89  ? 87   ARG A NE    1 
ATOM   697  C  CZ    . ARG A 1 87  ? 4.279   -0.956  8.253   1.00 30.73  ? 87   ARG A CZ    1 
ATOM   698  N  NH1   . ARG A 1 87  ? 5.443   -0.456  7.861   1.00 23.66  ? 87   ARG A NH1   1 
ATOM   699  N  NH2   . ARG A 1 87  ? 3.793   -0.625  9.450   1.00 25.48  ? 87   ARG A NH2   1 
ATOM   700  N  N     . ILE A 1 88  ? 8.699   -4.653  6.377   1.00 33.35  ? 88   ILE A N     1 
ATOM   701  C  CA    . ILE A 1 88  ? 10.112  -4.303  6.492   1.00 39.88  ? 88   ILE A CA    1 
ATOM   702  C  C     . ILE A 1 88  ? 10.261  -2.913  5.889   1.00 35.69  ? 88   ILE A C     1 
ATOM   703  O  O     . ILE A 1 88  ? 10.407  -2.753  4.675   1.00 34.93  ? 88   ILE A O     1 
ATOM   704  C  CB    . ILE A 1 88  ? 11.020  -5.316  5.796   1.00 43.30  ? 88   ILE A CB    1 
ATOM   705  C  CG1   . ILE A 1 88  ? 10.683  -6.722  6.286   1.00 36.67  ? 88   ILE A CG1   1 
ATOM   706  C  CG2   . ILE A 1 88  ? 12.474  -4.964  6.060   1.00 45.18  ? 88   ILE A CG2   1 
ATOM   707  C  CD1   . ILE A 1 88  ? 11.178  -7.821  5.388   1.00 42.87  ? 88   ILE A CD1   1 
ATOM   708  N  N     . GLU A 1 89  ? 10.226  -1.892  6.744   1.00 34.01  ? 89   GLU A N     1 
ATOM   709  C  CA    . GLU A 1 89  ? 10.263  -0.517  6.263   1.00 30.57  ? 89   GLU A CA    1 
ATOM   710  C  C     . GLU A 1 89  ? 11.582  -0.207  5.565   1.00 36.71  ? 89   GLU A C     1 
ATOM   711  O  O     . GLU A 1 89  ? 11.614  0.603   4.633   1.00 35.32  ? 89   GLU A O     1 
ATOM   712  C  CB    . GLU A 1 89  ? 10.016  0.433   7.444   1.00 32.44  ? 89   GLU A CB    1 
ATOM   713  C  CG    . GLU A 1 89  ? 9.977   1.925   7.120   1.00 39.22  ? 89   GLU A CG    1 
ATOM   714  C  CD    . GLU A 1 89  ? 9.402   2.760   8.277   1.00 46.60  ? 89   GLU A CD    1 
ATOM   715  O  OE1   . GLU A 1 89  ? 8.860   2.160   9.242   1.00 40.05  ? 89   GLU A OE1   1 
ATOM   716  O  OE2   . GLU A 1 89  ? 9.485   4.014   8.216   1.00 43.25  ? 89   GLU A OE2   1 
ATOM   717  N  N     . SER A 1 90  ? 12.672  -0.854  5.985   1.00 37.94  ? 90   SER A N     1 
ATOM   718  C  CA    . SER A 1 90  ? 13.993  -0.518  5.457   1.00 41.77  ? 90   SER A CA    1 
ATOM   719  C  C     . SER A 1 90  ? 14.229  -1.078  4.061   1.00 42.24  ? 90   SER A C     1 
ATOM   720  O  O     . SER A 1 90  ? 15.162  -0.633  3.383   1.00 44.86  ? 90   SER A O     1 
ATOM   721  C  CB    . SER A 1 90  ? 15.083  -1.021  6.406   1.00 39.44  ? 90   SER A CB    1 
ATOM   722  O  OG    . SER A 1 90  ? 14.911  -2.402  6.698   1.00 49.35  ? 90   SER A OG    1 
ATOM   723  N  N     . LYS A 1 91  ? 13.418  -2.043  3.624   1.00 34.30  ? 91   LYS A N     1 
ATOM   724  C  CA    . LYS A 1 91  ? 13.514  -2.629  2.293   1.00 33.49  ? 91   LYS A CA    1 
ATOM   725  C  C     . LYS A 1 91  ? 12.345  -2.221  1.396   1.00 30.19  ? 91   LYS A C     1 
ATOM   726  O  O     . LYS A 1 91  ? 12.118  -2.833  0.347   1.00 33.56  ? 91   LYS A O     1 
ATOM   727  C  CB    . LYS A 1 91  ? 13.621  -4.146  2.417   1.00 34.68  ? 91   LYS A CB    1 
ATOM   728  C  CG    . LYS A 1 91  ? 14.930  -4.569  3.065   1.00 43.73  ? 91   LYS A CG    1 
ATOM   729  C  CD    . LYS A 1 91  ? 14.946  -6.024  3.485   1.00 49.42  ? 91   LYS A CD    1 
ATOM   730  C  CE    . LYS A 1 91  ? 16.379  -6.534  3.581   1.00 54.18  ? 91   LYS A CE    1 
ATOM   731  N  NZ    . LYS A 1 91  ? 17.285  -5.485  4.138   1.00 65.17  ? 91   LYS A NZ    1 
ATOM   732  N  N     . THR A 1 92  ? 11.616  -1.183  1.780   1.00 25.56  ? 92   THR A N     1 
ATOM   733  C  CA    . THR A 1 92  ? 10.500  -0.655  1.007   1.00 28.22  ? 92   THR A CA    1 
ATOM   734  C  C     . THR A 1 92  ? 10.941  0.647   0.354   1.00 26.77  ? 92   THR A C     1 
ATOM   735  O  O     . THR A 1 92  ? 11.289  1.602   1.055   1.00 29.92  ? 92   THR A O     1 
ATOM   736  C  CB    . THR A 1 92  ? 9.282   -0.411  1.898   1.00 27.36  ? 92   THR A CB    1 
ATOM   737  O  OG1   . THR A 1 92  ? 8.927   -1.630  2.554   1.00 30.31  ? 92   THR A OG1   1 
ATOM   738  C  CG2   . THR A 1 92  ? 8.105   0.060   1.059   1.00 24.54  ? 92   THR A CG2   1 
ATOM   739  N  N     . VAL A 1 93  ? 10.918  0.685   -0.984  1.00 22.49  ? 93   VAL A N     1 
ATOM   740  C  CA    . VAL A 1 93  ? 11.480  1.793   -1.745  1.00 24.66  ? 93   VAL A CA    1 
ATOM   741  C  C     . VAL A 1 93  ? 10.466  2.289   -2.765  1.00 26.57  ? 93   VAL A C     1 
ATOM   742  O  O     . VAL A 1 93  ? 9.563   1.564   -3.195  1.00 23.63  ? 93   VAL A O     1 
ATOM   743  C  CB    . VAL A 1 93  ? 12.793  1.396   -2.452  1.00 28.26  ? 93   VAL A CB    1 
ATOM   744  C  CG1   . VAL A 1 93  ? 13.853  1.056   -1.424  1.00 27.60  ? 93   VAL A CG1   1 
ATOM   745  C  CG2   . VAL A 1 93  ? 12.555  0.193   -3.379  1.00 23.13  ? 93   VAL A CG2   1 
ATOM   746  N  N     . ILE A 1 94  ? 10.644  3.549   -3.151  1.00 24.38  ? 94   ILE A N     1 
ATOM   747  C  CA    . ILE A 1 94  ? 9.863   4.211   -4.188  1.00 20.15  ? 94   ILE A CA    1 
ATOM   748  C  C     . ILE A 1 94  ? 10.843  4.679   -5.255  1.00 31.12  ? 94   ILE A C     1 
ATOM   749  O  O     . ILE A 1 94  ? 11.879  5.270   -4.929  1.00 29.32  ? 94   ILE A O     1 
ATOM   750  C  CB    . ILE A 1 94  ? 9.065   5.401   -3.620  1.00 20.38  ? 94   ILE A CB    1 
ATOM   751  C  CG1   . ILE A 1 94  ? 8.128   4.936   -2.499  1.00 26.23  ? 94   ILE A CG1   1 
ATOM   752  C  CG2   . ILE A 1 94  ? 8.277   6.125   -4.728  1.00 22.35  ? 94   ILE A CG2   1 
ATOM   753  C  CD1   . ILE A 1 94  ? 7.359   6.062   -1.873  1.00 30.67  ? 94   ILE A CD1   1 
ATOM   754  N  N     . ILE A 1 95  ? 10.519  4.426   -6.520  1.00 29.73  ? 95   ILE A N     1 
ATOM   755  C  CA    . ILE A 1 95  ? 11.391  4.773   -7.637  1.00 25.60  ? 95   ILE A CA    1 
ATOM   756  C  C     . ILE A 1 95  ? 10.750  5.909   -8.412  1.00 29.90  ? 95   ILE A C     1 
ATOM   757  O  O     . ILE A 1 95  ? 9.640   5.764   -8.941  1.00 29.85  ? 95   ILE A O     1 
ATOM   758  C  CB    . ILE A 1 95  ? 11.668  3.564   -8.542  1.00 31.48  ? 95   ILE A CB    1 
ATOM   759  C  CG1   . ILE A 1 95  ? 12.569  2.571   -7.817  1.00 27.81  ? 95   ILE A CG1   1 
ATOM   760  C  CG2   . ILE A 1 95  ? 12.314  4.006   -9.852  1.00 36.95  ? 95   ILE A CG2   1 
ATOM   761  C  CD1   . ILE A 1 95  ? 11.842  1.441   -7.185  1.00 29.10  ? 95   ILE A CD1   1 
ATOM   762  N  N     . THR A 1 96  ? 11.441  7.050   -8.446  1.00 26.12  ? 96   THR A N     1 
ATOM   763  C  CA    . THR A 1 96  ? 11.105  8.193   -9.280  1.00 31.48  ? 96   THR A CA    1 
ATOM   764  C  C     . THR A 1 96  ? 12.389  8.689   -9.942  1.00 32.21  ? 96   THR A C     1 
ATOM   765  O  O     . THR A 1 96  ? 13.495  8.452   -9.447  1.00 30.30  ? 96   THR A O     1 
ATOM   766  C  CB    . THR A 1 96  ? 10.457  9.332   -8.463  1.00 31.71  ? 96   THR A CB    1 
ATOM   767  O  OG1   . THR A 1 96  ? 11.342  9.711   -7.404  1.00 32.01  ? 96   THR A OG1   1 
ATOM   768  C  CG2   . THR A 1 96  ? 9.119   8.880   -7.864  1.00 36.48  ? 96   THR A CG2   1 
ATOM   769  N  N     . GLN A 1 97  ? 12.247  9.373   -11.076 1.00 39.28  ? 97   GLN A N     1 
ATOM   770  C  CA    . GLN A 1 97  ? 13.442  9.906   -11.728 1.00 41.13  ? 97   GLN A CA    1 
ATOM   771  C  C     . GLN A 1 97  ? 14.150  10.917  -10.829 1.00 41.22  ? 97   GLN A C     1 
ATOM   772  O  O     . GLN A 1 97  ? 15.373  10.853  -10.664 1.00 39.91  ? 97   GLN A O     1 
ATOM   773  C  CB    . GLN A 1 97  ? 13.091  10.515  -13.086 1.00 51.19  ? 97   GLN A CB    1 
ATOM   774  C  CG    . GLN A 1 97  ? 11.962  11.519  -13.074 1.00 59.00  ? 97   GLN A CG    1 
ATOM   775  C  CD    . GLN A 1 97  ? 11.658  12.060  -14.458 1.00 76.74  ? 97   GLN A CD    1 
ATOM   776  O  OE1   . GLN A 1 97  ? 12.292  11.673  -15.445 1.00 71.57  ? 97   GLN A OE1   1 
ATOM   777  N  NE2   . GLN A 1 97  ? 10.686  12.964  -14.539 1.00 74.32  ? 97   GLN A NE2   1 
ATOM   778  N  N     . GLU A 1 98  ? 13.392  11.810  -10.189 1.00 39.83  ? 98   GLU A N     1 
ATOM   779  C  CA    . GLU A 1 98  ? 13.929  12.808  -9.267  1.00 41.17  ? 98   GLU A CA    1 
ATOM   780  C  C     . GLU A 1 98  ? 13.554  12.466  -7.829  1.00 37.75  ? 98   GLU A C     1 
ATOM   781  O  O     . GLU A 1 98  ? 12.385  12.200  -7.533  1.00 31.03  ? 98   GLU A O     1 
ATOM   782  C  CB    . GLU A 1 98  ? 13.419  14.204  -9.622  1.00 46.56  ? 98   GLU A CB    1 
ATOM   783  C  CG    . GLU A 1 98  ? 13.926  14.696  -10.967 1.00 55.22  ? 98   GLU A CG    1 
ATOM   784  C  CD    . GLU A 1 98  ? 13.497  16.111  -11.264 1.00 68.96  ? 98   GLU A CD    1 
ATOM   785  O  OE1   . GLU A 1 98  ? 13.040  16.804  -10.328 1.00 70.50  ? 98   GLU A OE1   1 
ATOM   786  O  OE2   . GLU A 1 98  ? 13.611  16.527  -12.435 1.00 77.54  ? 98   GLU A OE2   1 
ATOM   787  N  N     . GLN A 1 99  ? 14.551  12.492  -6.940  1.00 28.70  ? 99   GLN A N     1 
ATOM   788  C  CA    . GLN A 1 99  ? 14.332  12.116  -5.547  1.00 36.67  ? 99   GLN A CA    1 
ATOM   789  C  C     . GLN A 1 99  ? 13.338  13.044  -4.851  1.00 35.67  ? 99   GLN A C     1 
ATOM   790  O  O     . GLN A 1 99  ? 12.595  12.604  -3.965  1.00 30.08  ? 99   GLN A O     1 
ATOM   791  C  CB    . GLN A 1 99  ? 15.665  12.105  -4.802  1.00 34.97  ? 99   GLN A CB    1 
ATOM   792  C  CG    . GLN A 1 99  ? 15.521  11.837  -3.323  1.00 38.96  ? 99   GLN A CG    1 
ATOM   793  C  CD    . GLN A 1 99  ? 16.847  11.785  -2.609  1.00 46.69  ? 99   GLN A CD    1 
ATOM   794  O  OE1   . GLN A 1 99  ? 17.843  12.327  -3.088  1.00 48.22  ? 99   GLN A OE1   1 
ATOM   795  N  NE2   . GLN A 1 99  ? 16.870  11.123  -1.452  1.00 45.80  ? 99   GLN A NE2   1 
ATOM   796  N  N     . ARG A 1 100 ? 13.297  14.316  -5.251  1.00 31.60  ? 100  ARG A N     1 
ATOM   797  C  CA    . ARG A 1 100 ? 12.417  15.301  -4.632  1.00 35.87  ? 100  ARG A CA    1 
ATOM   798  C  C     . ARG A 1 100 ? 10.940  15.000  -4.876  1.00 31.89  ? 100  ARG A C     1 
ATOM   799  O  O     . ARG A 1 100 ? 10.084  15.547  -4.170  1.00 30.13  ? 100  ARG A O     1 
ATOM   800  C  CB    . ARG A 1 100 ? 12.774  16.702  -5.153  1.00 33.45  ? 100  ARG A CB    1 
ATOM   801  C  CG    . ARG A 1 100 ? 12.216  17.852  -4.324  1.00 41.65  ? 100  ARG A CG    1 
ATOM   802  C  CD    . ARG A 1 100 ? 12.799  19.191  -4.755  1.00 44.75  ? 100  ARG A CD    1 
ATOM   803  N  NE    . ARG A 1 100 ? 12.448  20.257  -3.823  1.00 55.11  ? 100  ARG A NE    1 
ATOM   804  C  CZ    . ARG A 1 100 ? 12.861  21.514  -3.922  1.00 57.27  ? 100  ARG A CZ    1 
ATOM   805  N  NH1   . ARG A 1 100 ? 13.638  21.912  -4.917  1.00 60.38  ? 100  ARG A NH1   1 
ATOM   806  N  NH2   . ARG A 1 100 ? 12.482  22.396  -3.000  1.00 57.90  ? 100  ARG A NH2   1 
ATOM   807  N  N     . ASP A 1 101 ? 10.622  14.153  -5.863  1.00 34.13  ? 101  ASP A N     1 
ATOM   808  C  CA    . ASP A 1 101 ? 9.242   13.701  -6.027  1.00 36.36  ? 101  ASP A CA    1 
ATOM   809  C  C     . ASP A 1 101 ? 8.827   12.766  -4.900  1.00 27.36  ? 101  ASP A C     1 
ATOM   810  O  O     . ASP A 1 101 ? 7.642   12.690  -4.567  1.00 36.30  ? 101  ASP A O     1 
ATOM   811  C  CB    . ASP A 1 101 ? 9.052   12.964  -7.358  1.00 38.65  ? 101  ASP A CB    1 
ATOM   812  C  CG    . ASP A 1 101 ? 9.471   13.781  -8.555  1.00 51.99  ? 101  ASP A CG    1 
ATOM   813  O  OD1   . ASP A 1 101 ? 9.377   15.027  -8.495  1.00 54.63  ? 101  ASP A OD1   1 
ATOM   814  O  OD2   . ASP A 1 101 ? 9.889   13.160  -9.561  1.00 52.80  ? 101  ASP A OD2   1 
ATOM   815  N  N     . THR A 1 102 ? 9.780   12.043  -4.319  1.00 30.83  ? 102  THR A N     1 
ATOM   816  C  CA    . THR A 1 102 ? 9.509   10.998  -3.343  1.00 31.45  ? 102  THR A CA    1 
ATOM   817  C  C     . THR A 1 102 ? 9.690   11.471  -1.907  1.00 31.99  ? 102  THR A C     1 
ATOM   818  O  O     . THR A 1 102 ? 8.866   11.157  -1.041  1.00 29.17  ? 102  THR A O     1 
ATOM   819  C  CB    . THR A 1 102 ? 10.408  9.788   -3.628  1.00 28.43  ? 102  THR A CB    1 
ATOM   820  O  OG1   . THR A 1 102 ? 9.953   9.153   -4.826  1.00 31.80  ? 102  THR A OG1   1 
ATOM   821  C  CG2   . THR A 1 102 ? 10.367  8.766   -2.471  1.00 27.68  ? 102  THR A CG2   1 
ATOM   822  N  N     . VAL A 1 103 ? 10.759  12.215  -1.634  1.00 24.64  ? 103  VAL A N     1 
ATOM   823  C  CA    . VAL A 1 103 ? 10.992  12.773  -0.302  1.00 24.71  ? 103  VAL A CA    1 
ATOM   824  C  C     . VAL A 1 103 ? 11.466  14.201  -0.439  1.00 32.80  ? 103  VAL A C     1 
ATOM   825  O  O     . VAL A 1 103 ? 12.084  14.581  -1.449  1.00 30.34  ? 103  VAL A O     1 
ATOM   826  C  CB    . VAL A 1 103 ? 12.039  11.957  0.481   1.00 25.81  ? 103  VAL A CB    1 
ATOM   827  C  CG1   . VAL A 1 103 ? 11.458  10.620  0.918   1.00 23.81  ? 103  VAL A CG1   1 
ATOM   828  C  CG2   . VAL A 1 103 ? 13.307  11.753  -0.373  1.00 27.40  ? 103  VAL A CG2   1 
ATOM   829  N  N     . PRO A 1 104 ? 11.191  15.039  0.563   1.00 28.18  ? 104  PRO A N     1 
ATOM   830  C  CA    . PRO A 1 104 ? 11.848  16.347  0.603   1.00 29.35  ? 104  PRO A CA    1 
ATOM   831  C  C     . PRO A 1 104 ? 13.335  16.144  0.819   1.00 28.73  ? 104  PRO A C     1 
ATOM   832  O  O     . PRO A 1 104 ? 13.759  15.205  1.498   1.00 26.22  ? 104  PRO A O     1 
ATOM   833  C  CB    . PRO A 1 104 ? 11.192  17.064  1.795   1.00 28.31  ? 104  PRO A CB    1 
ATOM   834  C  CG    . PRO A 1 104 ? 9.993   16.202  2.184   1.00 26.55  ? 104  PRO A CG    1 
ATOM   835  C  CD    . PRO A 1 104 ? 10.322  14.809  1.736   1.00 24.85  ? 104  PRO A CD    1 
ATOM   836  N  N     . ILE A 1 105 ? 14.135  17.006  0.201   1.00 26.85  ? 105  ILE A N     1 
ATOM   837  C  CA    . ILE A 1 105 ? 15.579  16.907  0.374   1.00 32.91  ? 105  ILE A CA    1 
ATOM   838  C  C     . ILE A 1 105 ? 15.903  17.382  1.782   1.00 29.03  ? 105  ILE A C     1 
ATOM   839  O  O     . ILE A 1 105 ? 15.673  18.558  2.095   1.00 30.42  ? 105  ILE A O     1 
ATOM   840  C  CB    . ILE A 1 105 ? 16.336  17.726  -0.685  1.00 38.85  ? 105  ILE A CB    1 
ATOM   841  C  CG1   . ILE A 1 105 ? 16.003  17.207  -2.086  1.00 36.28  ? 105  ILE A CG1   1 
ATOM   842  C  CG2   . ILE A 1 105 ? 17.834  17.686  -0.406  1.00 35.74  ? 105  ILE A CG2   1 
ATOM   843  C  CD1   . ILE A 1 105 ? 16.126  15.701  -2.214  1.00 36.15  ? 105  ILE A CD1   1 
ATOM   844  N  N     . PRO A 1 106 ? 16.425  16.525  2.655   1.00 28.49  ? 106  PRO A N     1 
ATOM   845  C  CA    . PRO A 1 106 ? 16.641  16.943  4.042   1.00 33.81  ? 106  PRO A CA    1 
ATOM   846  C  C     . PRO A 1 106 ? 17.761  17.969  4.137   1.00 37.15  ? 106  PRO A C     1 
ATOM   847  O  O     . PRO A 1 106 ? 18.645  18.052  3.282   1.00 33.34  ? 106  PRO A O     1 
ATOM   848  C  CB    . PRO A 1 106 ? 17.016  15.642  4.767   1.00 33.83  ? 106  PRO A CB    1 
ATOM   849  C  CG    . PRO A 1 106 ? 16.835  14.533  3.753   1.00 34.72  ? 106  PRO A CG    1 
ATOM   850  C  CD    . PRO A 1 106 ? 16.944  15.169  2.407   1.00 27.58  ? 106  PRO A CD    1 
ATOM   851  N  N     . LYS A 1 107 ? 17.709  18.754  5.212   1.00 34.02  ? 107  LYS A N     1 
ATOM   852  C  CA    . LYS A 1 107 ? 18.720  19.781  5.435   1.00 39.02  ? 107  LYS A CA    1 
ATOM   853  C  C     . LYS A 1 107 ? 20.079  19.160  5.740   1.00 42.67  ? 107  LYS A C     1 
ATOM   854  O  O     . LYS A 1 107 ? 21.099  19.563  5.167   1.00 44.02  ? 107  LYS A O     1 
ATOM   855  C  CB    . LYS A 1 107 ? 18.277  20.709  6.565   1.00 37.72  ? 107  LYS A CB    1 
ATOM   856  C  CG    . LYS A 1 107 ? 18.882  22.101  6.527   1.00 46.41  ? 107  LYS A CG    1 
ATOM   857  C  CD    . LYS A 1 107 ? 18.075  23.057  7.399   1.00 47.87  ? 107  LYS A CD    1 
ATOM   858  C  CE    . LYS A 1 107 ? 18.608  24.477  7.327   1.00 61.10  ? 107  LYS A CE    1 
ATOM   859  N  NZ    . LYS A 1 107 ? 17.817  25.404  8.190   1.00 62.93  ? 107  LYS A NZ    1 
ATOM   860  N  N     . SER A 1 108 ? 20.122  18.168  6.628   1.00 39.07  ? 108  SER A N     1 
ATOM   861  C  CA    . SER A 1 108 ? 21.424  17.616  6.976   1.00 40.37  ? 108  SER A CA    1 
ATOM   862  C  C     . SER A 1 108 ? 21.381  16.111  7.205   1.00 44.78  ? 108  SER A C     1 
ATOM   863  O  O     . SER A 1 108 ? 22.325  15.404  6.842   1.00 38.97  ? 108  SER A O     1 
ATOM   864  C  CB    . SER A 1 108 ? 21.992  18.329  8.207   1.00 45.52  ? 108  SER A CB    1 
ATOM   865  O  OG    . SER A 1 108 ? 21.227  18.063  9.367   1.00 48.77  ? 108  SER A OG    1 
ATOM   866  N  N     . GLY A 1 109 ? 20.303  15.607  7.802   1.00 40.00  ? 109  GLY A N     1 
ATOM   867  C  CA    . GLY A 1 109 ? 20.203  14.192  8.067   1.00 40.60  ? 109  GLY A CA    1 
ATOM   868  C  C     . GLY A 1 109 ? 19.760  13.382  6.859   1.00 39.55  ? 109  GLY A C     1 
ATOM   869  O  O     . GLY A 1 109 ? 19.525  13.887  5.760   1.00 35.41  ? 109  GLY A O     1 
ATOM   870  N  N     . GLN A 1 110 ? 19.679  12.077  7.080   1.00 37.06  ? 110  GLN A N     1 
ATOM   871  C  CA    . GLN A 1 110 ? 19.001  11.183  6.157   1.00 32.50  ? 110  GLN A CA    1 
ATOM   872  C  C     . GLN A 1 110 ? 17.490  11.400  6.271   1.00 31.63  ? 110  GLN A C     1 
ATOM   873  O  O     . GLN A 1 110 ? 16.985  11.754  7.335   1.00 33.70  ? 110  GLN A O     1 
ATOM   874  C  CB    . GLN A 1 110 ? 19.390  9.749   6.505   1.00 36.93  ? 110  GLN A CB    1 
ATOM   875  C  CG    . GLN A 1 110 ? 18.793  8.646   5.679   1.00 37.24  ? 110  GLN A CG    1 
ATOM   876  C  CD    . GLN A 1 110 ? 19.228  7.298   6.205   1.00 42.23  ? 110  GLN A CD    1 
ATOM   877  O  OE1   . GLN A 1 110 ? 18.703  6.816   7.211   1.00 42.93  ? 110  GLN A OE1   1 
ATOM   878  N  NE2   . GLN A 1 110 ? 20.209  6.688   5.544   1.00 41.25  ? 110  GLN A NE2   1 
ATOM   879  N  N     . SER A 1 111 ? 16.763  11.193  5.170   1.00 28.45  ? 111  SER A N     1 
ATOM   880  C  CA    . SER A 1 111 ? 15.308  11.319  5.223   1.00 29.57  ? 111  SER A CA    1 
ATOM   881  C  C     . SER A 1 111 ? 14.669  10.119  5.914   1.00 31.26  ? 111  SER A C     1 
ATOM   882  O  O     . SER A 1 111 ? 15.027  8.966   5.653   1.00 26.84  ? 111  SER A O     1 
ATOM   883  C  CB    . SER A 1 111 ? 14.709  11.457  3.824   1.00 29.67  ? 111  SER A CB    1 
ATOM   884  O  OG    . SER A 1 111 ? 13.282  11.532  3.914   1.00 28.40  ? 111  SER A OG    1 
ATOM   885  N  N     . GLN A 1 112 ? 13.698  10.400  6.786   1.00 26.48  ? 112  GLN A N     1 
ATOM   886  C  CA    . GLN A 1 112 ? 12.848  9.389   7.406   1.00 25.63  ? 112  GLN A CA    1 
ATOM   887  C  C     . GLN A 1 112 ? 11.485  9.266   6.749   1.00 29.65  ? 112  GLN A C     1 
ATOM   888  O  O     . GLN A 1 112 ? 10.644  8.509   7.246   1.00 32.51  ? 112  GLN A O     1 
ATOM   889  C  CB    . GLN A 1 112 ? 12.592  9.701   8.881   1.00 29.65  ? 112  GLN A CB    1 
ATOM   890  C  CG    . GLN A 1 112 ? 13.772  9.803   9.783   1.00 30.78  ? 112  GLN A CG    1 
ATOM   891  C  CD    . GLN A 1 112 ? 13.324  10.112  11.198  1.00 34.49  ? 112  GLN A CD    1 
ATOM   892  O  OE1   . GLN A 1 112 ? 12.128  10.029  11.514  1.00 29.75  ? 112  GLN A OE1   1 
ATOM   893  N  NE2   . GLN A 1 112 ? 14.273  10.459  12.060  1.00 29.87  ? 112  GLN A NE2   1 
ATOM   894  N  N     . LEU A 1 113 ? 11.217  10.022  5.692   1.00 22.98  ? 113  LEU A N     1 
ATOM   895  C  CA    . LEU A 1 113 ? 9.870   10.115  5.149   1.00 26.88  ? 113  LEU A CA    1 
ATOM   896  C  C     . LEU A 1 113 ? 9.688   9.255   3.909   1.00 25.58  ? 113  LEU A C     1 
ATOM   897  O  O     . LEU A 1 113 ? 8.668   9.377   3.223   1.00 31.92  ? 113  LEU A O     1 
ATOM   898  C  CB    . LEU A 1 113 ? 9.528   11.572  4.845   1.00 27.55  ? 113  LEU A CB    1 
ATOM   899  C  CG    . LEU A 1 113 ? 9.468   12.472  6.079   1.00 30.39  ? 113  LEU A CG    1 
ATOM   900  C  CD1   . LEU A 1 113 ? 9.469   13.933  5.651   1.00 29.24  ? 113  LEU A CD1   1 
ATOM   901  C  CD2   . LEU A 1 113 ? 8.220   12.141  6.877   1.00 25.61  ? 113  LEU A CD2   1 
ATOM   902  N  N     . GLY A 1 114 ? 10.648  8.392   3.622   1.00 27.64  ? 114  GLY A N     1 
ATOM   903  C  CA    . GLY A 1 114 ? 10.603  7.493   2.484   1.00 29.59  ? 114  GLY A CA    1 
ATOM   904  C  C     . GLY A 1 114 ? 12.003  7.039   2.150   1.00 32.53  ? 114  GLY A C     1 
ATOM   905  O  O     . GLY A 1 114 ? 12.991  7.588   2.633   1.00 34.83  ? 114  GLY A O     1 
ATOM   906  N  N     . ARG A 1 115 ? 12.084  5.994   1.332   1.00 28.75  ? 115  ARG A N     1 
ATOM   907  C  CA    . ARG A 1 115 ? 13.369  5.544   0.803   1.00 31.65  ? 115  ARG A CA    1 
ATOM   908  C  C     . ARG A 1 115 ? 13.281  5.620   -0.711  1.00 33.80  ? 115  ARG A C     1 
ATOM   909  O  O     . ARG A 1 115 ? 12.460  4.933   -1.324  1.00 30.48  ? 115  ARG A O     1 
ATOM   910  C  CB    . ARG A 1 115 ? 13.724  4.140   1.288   1.00 34.54  ? 115  ARG A CB    1 
ATOM   911  C  CG    . ARG A 1 115 ? 13.893  4.063   2.801   1.00 39.91  ? 115  ARG A CG    1 
ATOM   912  C  CD    . ARG A 1 115 ? 14.872  2.963   3.215   1.00 52.71  ? 115  ARG A CD    1 
ATOM   913  N  NE    . ARG A 1 115 ? 14.863  2.744   4.659   1.00 60.32  ? 115  ARG A NE    1 
ATOM   914  C  CZ    . ARG A 1 115 ? 15.754  3.238   5.513   1.00 62.06  ? 115  ARG A CZ    1 
ATOM   915  N  NH1   . ARG A 1 115 ? 16.781  3.970   5.100   1.00 54.88  ? 115  ARG A NH1   1 
ATOM   916  N  NH2   . ARG A 1 115 ? 15.615  2.986   6.814   1.00 55.64  ? 115  ARG A NH2   1 
ATOM   917  N  N     . TRP A 1 116 ? 14.087  6.489   -1.304  1.00 30.52  ? 116  TRP A N     1 
ATOM   918  C  CA    . TRP A 1 116 ? 14.081  6.676   -2.744  1.00 33.67  ? 116  TRP A CA    1 
ATOM   919  C  C     . TRP A 1 116 ? 15.131  5.777   -3.373  1.00 33.69  ? 116  TRP A C     1 
ATOM   920  O  O     . TRP A 1 116 ? 16.168  5.484   -2.771  1.00 35.54  ? 116  TRP A O     1 
ATOM   921  C  CB    . TRP A 1 116 ? 14.341  8.143   -3.101  1.00 32.65  ? 116  TRP A CB    1 
ATOM   922  C  CG    . TRP A 1 116 ? 14.455  8.400   -4.569  1.00 36.21  ? 116  TRP A CG    1 
ATOM   923  C  CD1   . TRP A 1 116 ? 13.434  8.545   -5.464  1.00 36.36  ? 116  TRP A CD1   1 
ATOM   924  C  CD2   . TRP A 1 116 ? 15.667  8.550   -5.313  1.00 32.01  ? 116  TRP A CD2   1 
ATOM   925  N  NE1   . TRP A 1 116 ? 13.937  8.776   -6.725  1.00 34.03  ? 116  TRP A NE1   1 
ATOM   926  C  CE2   . TRP A 1 116 ? 15.307  8.785   -6.657  1.00 34.98  ? 116  TRP A CE2   1 
ATOM   927  C  CE3   . TRP A 1 116 ? 17.021  8.519   -4.972  1.00 35.63  ? 116  TRP A CE3   1 
ATOM   928  C  CZ2   . TRP A 1 116 ? 16.254  8.983   -7.659  1.00 39.00  ? 116  TRP A CZ2   1 
ATOM   929  C  CZ3   . TRP A 1 116 ? 17.964  8.709   -5.972  1.00 38.51  ? 116  TRP A CZ3   1 
ATOM   930  C  CH2   . TRP A 1 116 ? 17.573  8.940   -7.297  1.00 35.47  ? 116  TRP A CH2   1 
ATOM   931  N  N     . MET A 1 117 ? 14.830  5.290   -4.573  1.00 33.08  ? 117  MET A N     1 
ATOM   932  C  CA    . MET A 1 117 ? 15.770  4.463   -5.322  1.00 35.19  ? 117  MET A CA    1 
ATOM   933  C  C     . MET A 1 117 ? 15.720  4.911   -6.770  1.00 33.64  ? 117  MET A C     1 
ATOM   934  O  O     . MET A 1 117 ? 14.633  5.134   -7.313  1.00 32.86  ? 117  MET A O     1 
ATOM   935  C  CB    . MET A 1 117 ? 15.434  2.966   -5.206  1.00 34.70  ? 117  MET A CB    1 
ATOM   936  C  CG    . MET A 1 117 ? 16.577  2.033   -5.582  1.00 32.33  ? 117  MET A CG    1 
ATOM   937  S  SD    . MET A 1 117 ? 16.227  0.253   -5.475  1.00 43.44  ? 117  MET A SD    1 
ATOM   938  C  CE    . MET A 1 117 ? 16.648  -0.118  -3.771  1.00 46.94  ? 117  MET A CE    1 
ATOM   939  N  N     . SER A 1 118 ? 16.885  5.064   -7.391  1.00 39.28  ? 118  SER A N     1 
ATOM   940  C  CA    . SER A 1 118 ? 16.894  5.460   -8.788  1.00 38.03  ? 118  SER A CA    1 
ATOM   941  C  C     . SER A 1 118 ? 16.462  4.287   -9.659  1.00 30.22  ? 118  SER A C     1 
ATOM   942  O  O     . SER A 1 118 ? 16.627  3.118   -9.299  1.00 32.12  ? 118  SER A O     1 
ATOM   943  C  CB    . SER A 1 118 ? 18.279  5.951   -9.215  1.00 34.08  ? 118  SER A CB    1 
ATOM   944  O  OG    . SER A 1 118 ? 19.206  4.878   -9.213  1.00 33.67  ? 118  SER A OG    1 
ATOM   945  N  N     . GLU A 1 119 ? 15.891  4.624   -10.815 1.00 36.19  ? 119  GLU A N     1 
ATOM   946  C  CA    . GLU A 1 119 ? 15.424  3.607   -11.745 1.00 41.82  ? 119  GLU A CA    1 
ATOM   947  C  C     . GLU A 1 119 ? 16.564  2.687   -12.181 1.00 43.58  ? 119  GLU A C     1 
ATOM   948  O  O     . GLU A 1 119 ? 16.383  1.467   -12.285 1.00 34.64  ? 119  GLU A O     1 
ATOM   949  C  CB    . GLU A 1 119 ? 14.766  4.288   -12.946 1.00 50.32  ? 119  GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 119 ? 14.315  3.334   -14.026 1.00 58.96  ? 119  GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 119 ? 13.514  2.184   -13.463 1.00 71.69  ? 119  GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 119 ? 12.520  2.455   -12.757 1.00 74.58  ? 119  GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 119 ? 13.889  1.011   -13.702 1.00 68.50  ? 119  GLU A OE2   1 
ATOM   954  N  N     . GLU A 1 120 ? 17.751  3.253   -12.417 1.00 41.90  ? 120  GLU A N     1 
ATOM   955  C  CA    . GLU A 1 120 ? 18.894  2.438   -12.818 1.00 44.00  ? 120  GLU A CA    1 
ATOM   956  C  C     . GLU A 1 120 ? 19.307  1.485   -11.706 1.00 37.43  ? 120  GLU A C     1 
ATOM   957  O  O     . GLU A 1 120 ? 19.654  0.327   -11.967 1.00 37.50  ? 120  GLU A O     1 
ATOM   958  C  CB    . GLU A 1 120 ? 20.066  3.335   -13.223 1.00 44.14  ? 120  GLU A CB    1 
ATOM   959  C  CG    . GLU A 1 120 ? 19.797  4.212   -14.446 1.00 55.31  ? 120  GLU A CG    1 
ATOM   960  C  CD    . GLU A 1 120 ? 19.058  5.498   -14.114 1.00 60.20  ? 120  GLU A CD    1 
ATOM   961  O  OE1   . GLU A 1 120 ? 18.680  5.686   -12.939 1.00 54.47  ? 120  GLU A OE1   1 
ATOM   962  O  OE2   . GLU A 1 120 ? 18.859  6.327   -15.029 1.00 72.20  ? 120  GLU A OE2   1 
ATOM   963  N  N     . ASP A 1 121 ? 19.263  1.946   -10.457 1.00 36.73  ? 121  ASP A N     1 
ATOM   964  C  CA    . ASP A 1 121 ? 19.596  1.055   -9.351  1.00 37.47  ? 121  ASP A CA    1 
ATOM   965  C  C     . ASP A 1 121 ? 18.537  -0.028  -9.173  1.00 36.22  ? 121  ASP A C     1 
ATOM   966  O  O     . ASP A 1 121 ? 18.873  -1.178  -8.872  1.00 31.51  ? 121  ASP A O     1 
ATOM   967  C  CB    . ASP A 1 121 ? 19.780  1.857   -8.067  1.00 35.21  ? 121  ASP A CB    1 
ATOM   968  C  CG    . ASP A 1 121 ? 20.978  2.791   -8.138  1.00 43.40  ? 121  ASP A CG    1 
ATOM   969  O  OD1   . ASP A 1 121 ? 21.990  2.415   -8.762  1.00 53.03  ? 121  ASP A OD1   1 
ATOM   970  O  OD2   . ASP A 1 121 ? 20.903  3.903   -7.588  1.00 40.78  ? 121  ASP A OD2   1 
ATOM   971  N  N     . PHE A 1 122 ? 17.254  0.317   -9.360  1.00 34.71  ? 122  PHE A N     1 
ATOM   972  C  CA    . PHE A 1 122 ? 16.209  -0.701  -9.260  1.00 34.98  ? 122  PHE A CA    1 
ATOM   973  C  C     . PHE A 1 122 ? 16.368  -1.765  -10.340 1.00 31.89  ? 122  PHE A C     1 
ATOM   974  O  O     . PHE A 1 122 ? 16.245  -2.965  -10.060 1.00 33.60  ? 122  PHE A O     1 
ATOM   975  C  CB    . PHE A 1 122 ? 14.814  -0.083  -9.350  1.00 32.31  ? 122  PHE A CB    1 
ATOM   976  C  CG    . PHE A 1 122 ? 13.707  -1.118  -9.334  1.00 31.64  ? 122  PHE A CG    1 
ATOM   977  C  CD1   . PHE A 1 122 ? 13.552  -1.960  -8.242  1.00 28.85  ? 122  PHE A CD1   1 
ATOM   978  C  CD2   . PHE A 1 122 ? 12.848  -1.264  -10.416 1.00 29.13  ? 122  PHE A CD2   1 
ATOM   979  C  CE1   . PHE A 1 122 ? 12.552  -2.925  -8.217  1.00 30.35  ? 122  PHE A CE1   1 
ATOM   980  C  CE2   . PHE A 1 122 ? 11.842  -2.230  -10.400 1.00 31.31  ? 122  PHE A CE2   1 
ATOM   981  C  CZ    . PHE A 1 122 ? 11.694  -3.057  -9.299  1.00 27.20  ? 122  PHE A CZ    1 
ATOM   982  N  N     . GLU A 1 123 ? 16.632  -1.342  -11.581 1.00 29.99  ? 123  GLU A N     1 
ATOM   983  C  CA    . GLU A 1 123 ? 16.808  -2.289  -12.682 1.00 33.82  ? 123  GLU A CA    1 
ATOM   984  C  C     . GLU A 1 123 ? 17.833  -3.367  -12.336 1.00 32.59  ? 123  GLU A C     1 
ATOM   985  O  O     . GLU A 1 123 ? 17.636  -4.551  -12.640 1.00 29.25  ? 123  GLU A O     1 
ATOM   986  C  CB    . GLU A 1 123 ? 17.209  -1.525  -13.945 1.00 39.78  ? 123  GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 123 ? 17.257  -2.347  -15.221 1.00 60.32  ? 123  GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 123 ? 17.853  -1.563  -16.389 1.00 69.53  ? 123  GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 123 ? 18.182  -0.370  -16.204 1.00 62.70  ? 123  GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 123 ? 17.998  -2.141  -17.489 1.00 74.06  ? 123  GLU A OE2   1 
ATOM   991  N  N     . LYS A 1 124 ? 18.914  -2.987  -11.655 1.00 33.63  ? 124  LYS A N     1 
ATOM   992  C  CA    . LYS A 1 124 ? 19.899  -3.978  -11.229 1.00 30.20  ? 124  LYS A CA    1 
ATOM   993  C  C     . LYS A 1 124 ? 19.349  -4.876  -10.130 1.00 30.81  ? 124  LYS A C     1 
ATOM   994  O  O     . LYS A 1 124 ? 19.570  -6.093  -10.147 1.00 31.96  ? 124  LYS A O     1 
ATOM   995  C  CB    . LYS A 1 124 ? 21.173  -3.278  -10.756 1.00 32.42  ? 124  LYS A CB    1 
ATOM   996  C  CG    . LYS A 1 124 ? 21.804  -2.397  -11.833 1.00 44.99  ? 124  LYS A CG    1 
ATOM   997  C  CD    . LYS A 1 124 ? 22.966  -1.555  -11.317 1.00 54.72  ? 124  LYS A CD    1 
ATOM   998  C  CE    . LYS A 1 124 ? 23.395  -0.540  -12.384 1.00 64.38  ? 124  LYS A CE    1 
ATOM   999  N  NZ    . LYS A 1 124 ? 24.500  0.356   -11.945 1.00 70.04  ? 124  LYS A NZ    1 
ATOM   1000 N  N     . ALA A 1 125 ? 18.653  -4.292  -9.148  1.00 27.01  ? 125  ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 125 ? 18.058  -5.093  -8.079  1.00 28.05  ? 125  ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 125 ? 17.026  -6.067  -8.629  1.00 25.81  ? 125  ALA A C     1 
ATOM   1003 O  O     . ALA A 1 125 ? 16.920  -7.203  -8.161  1.00 31.34  ? 125  ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 125 ? 17.421  -4.173  -7.034  1.00 29.69  ? 125  ALA A CB    1 
ATOM   1005 N  N     . PHE A 1 126 ? 16.248  -5.630  -9.617  1.00 26.66  ? 126  PHE A N     1 
ATOM   1006 C  CA    . PHE A 1 126 ? 15.211  -6.475  -10.194 1.00 28.20  ? 126  PHE A CA    1 
ATOM   1007 C  C     . PHE A 1 126 ? 15.824  -7.669  -10.919 1.00 30.54  ? 126  PHE A C     1 
ATOM   1008 O  O     . PHE A 1 126 ? 15.412  -8.821  -10.717 1.00 30.61  ? 126  PHE A O     1 
ATOM   1009 C  CB    . PHE A 1 126 ? 14.363  -5.620  -11.136 1.00 26.39  ? 126  PHE A CB    1 
ATOM   1010 C  CG    . PHE A 1 126 ? 13.251  -6.358  -11.811 1.00 31.96  ? 126  PHE A CG    1 
ATOM   1011 C  CD1   . PHE A 1 126 ? 12.016  -6.470  -11.206 1.00 25.37  ? 126  PHE A CD1   1 
ATOM   1012 C  CD2   . PHE A 1 126 ? 13.427  -6.909  -13.069 1.00 33.63  ? 126  PHE A CD2   1 
ATOM   1013 C  CE1   . PHE A 1 126 ? 10.979  -7.135  -11.830 1.00 27.70  ? 126  PHE A CE1   1 
ATOM   1014 C  CE2   . PHE A 1 126 ? 12.392  -7.585  -13.698 1.00 36.72  ? 126  PHE A CE2   1 
ATOM   1015 C  CZ    . PHE A 1 126 ? 11.162  -7.694  -13.072 1.00 30.57  ? 126  PHE A CZ    1 
ATOM   1016 N  N     . ASN A 1 127 ? 16.836  -7.411  -11.751 1.00 30.13  ? 127  ASN A N     1 
ATOM   1017 C  CA    . ASN A 1 127 ? 17.425  -8.477  -12.551 1.00 30.75  ? 127  ASN A CA    1 
ATOM   1018 C  C     . ASN A 1 127 ? 18.157  -9.487  -11.691 1.00 26.52  ? 127  ASN A C     1 
ATOM   1019 O  O     . ASN A 1 127 ? 18.265  -10.652 -12.074 1.00 32.96  ? 127  ASN A O     1 
ATOM   1020 C  CB    . ASN A 1 127 ? 18.362  -7.880  -13.597 1.00 32.85  ? 127  ASN A CB    1 
ATOM   1021 C  CG    . ASN A 1 127 ? 17.618  -7.101  -14.644 1.00 37.18  ? 127  ASN A CG    1 
ATOM   1022 O  OD1   . ASN A 1 127 ? 16.475  -7.429  -14.978 1.00 39.79  ? 127  ASN A OD1   1 
ATOM   1023 N  ND2   . ASN A 1 127 ? 18.250  -6.052  -15.170 1.00 49.01  ? 127  ASN A ND2   1 
ATOM   1024 N  N     . ALA A 1 128 ? 18.654  -9.073  -10.528 1.00 32.35  ? 128  ALA A N     1 
ATOM   1025 C  CA    . ALA A 1 128 ? 19.266  -10.019 -9.609  1.00 28.96  ? 128  ALA A CA    1 
ATOM   1026 C  C     . ALA A 1 128 ? 18.246  -10.913 -8.912  1.00 35.64  ? 128  ALA A C     1 
ATOM   1027 O  O     . ALA A 1 128 ? 18.644  -11.901 -8.292  1.00 38.44  ? 128  ALA A O     1 
ATOM   1028 C  CB    . ALA A 1 128 ? 20.093  -9.274  -8.559  1.00 26.46  ? 128  ALA A CB    1 
ATOM   1029 N  N     . ARG A 1 129 ? 16.951  -10.609 -9.009  1.00 27.78  ? 129  ARG A N     1 
ATOM   1030 C  CA    . ARG A 1 129 ? 15.939  -11.301 -8.215  1.00 22.80  ? 129  ARG A CA    1 
ATOM   1031 C  C     . ARG A 1 129 ? 14.942  -12.083 -9.051  1.00 22.13  ? 129  ARG A C     1 
ATOM   1032 O  O     . ARG A 1 129 ? 14.724  -13.276 -8.800  1.00 24.41  ? 129  ARG A O     1 
ATOM   1033 C  CB    . ARG A 1 129 ? 15.185  -10.282 -7.342  1.00 28.18  ? 129  ARG A CB    1 
ATOM   1034 C  CG    . ARG A 1 129 ? 15.946  -9.838  -6.106  1.00 27.62  ? 129  ARG A CG    1 
ATOM   1035 C  CD    . ARG A 1 129 ? 15.384  -8.537  -5.550  1.00 30.86  ? 129  ARG A CD    1 
ATOM   1036 N  NE    . ARG A 1 129 ? 16.046  -8.184  -4.300  1.00 34.40  ? 129  ARG A NE    1 
ATOM   1037 C  CZ    . ARG A 1 129 ? 17.185  -7.511  -4.222  1.00 41.67  ? 129  ARG A CZ    1 
ATOM   1038 N  NH1   . ARG A 1 129 ? 17.787  -7.044  -5.305  1.00 38.84  ? 129  ARG A NH1   1 
ATOM   1039 N  NH2   . ARG A 1 129 ? 17.737  -7.304  -3.029  1.00 37.35  ? 129  ARG A NH2   1 
ATOM   1040 N  N     . PHE A 1 130 ? 14.325  -11.455 -10.032 1.00 23.74  ? 130  PHE A N     1 
ATOM   1041 C  CA    . PHE A 1 130 ? 13.139  -12.061 -10.619 1.00 26.10  ? 130  PHE A CA    1 
ATOM   1042 C  C     . PHE A 1 130 ? 13.352  -13.092 -11.722 1.00 29.63  ? 130  PHE A C     1 
ATOM   1043 O  O     . PHE A 1 130 ? 12.532  -14.013 -11.828 1.00 26.44  ? 130  PHE A O     1 
ATOM   1044 C  CB    . PHE A 1 130 ? 12.215  -10.963 -11.120 1.00 26.56  ? 130  PHE A CB    1 
ATOM   1045 C  CG    . PHE A 1 130 ? 11.362  -10.413 -10.027 1.00 27.91  ? 130  PHE A CG    1 
ATOM   1046 C  CD1   . PHE A 1 130 ? 10.183  -11.052 -9.666  1.00 28.30  ? 130  PHE A CD1   1 
ATOM   1047 C  CD2   . PHE A 1 130 ? 11.789  -9.333  -9.282  1.00 28.48  ? 130  PHE A CD2   1 
ATOM   1048 C  CE1   . PHE A 1 130 ? 9.418   -10.570 -8.622  1.00 24.74  ? 130  PHE A CE1   1 
ATOM   1049 C  CE2   . PHE A 1 130 ? 11.015  -8.859  -8.231  1.00 25.75  ? 130  PHE A CE2   1 
ATOM   1050 C  CZ    . PHE A 1 130 ? 9.841   -9.478  -7.914  1.00 22.02  ? 130  PHE A CZ    1 
ATOM   1051 N  N     . PRO A 1 131 ? 14.396  -12.982 -12.581 1.00 29.68  ? 131  PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 131 ? 14.595  -14.025 -13.599 1.00 24.98  ? 131  PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 131 ? 14.571  -15.433 -13.023 1.00 22.17  ? 131  PRO A C     1 
ATOM   1054 O  O     . PRO A 1 131 ? 15.378  -15.780 -12.154 1.00 31.56  ? 131  PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 131 ? 15.969  -13.677 -14.188 1.00 29.73  ? 131  PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 131 ? 16.023  -12.198 -14.095 1.00 29.13  ? 131  PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 131 ? 15.311  -11.839 -12.799 1.00 26.27  ? 131  PRO A CD    1 
ATOM   1058 N  N     . GLY A 1 132 ? 13.629  -16.251 -13.487 1.00 28.03  ? 132  GLY A N     1 
ATOM   1059 C  CA    . GLY A 1 132 ? 13.540  -17.629 -13.052 1.00 22.22  ? 132  GLY A CA    1 
ATOM   1060 C  C     . GLY A 1 132 ? 13.026  -17.851 -11.647 1.00 27.36  ? 132  GLY A C     1 
ATOM   1061 O  O     . GLY A 1 132 ? 13.104  -18.980 -11.156 1.00 25.84  ? 132  GLY A O     1 
ATOM   1062 N  N     . CYS A 1 133 ? 12.470  -16.829 -10.987 1.00 25.71  ? 133  CYS A N     1 
ATOM   1063 C  CA    . CYS A 1 133 ? 12.189  -16.954 -9.555  1.00 22.70  ? 133  CYS A CA    1 
ATOM   1064 C  C     . CYS A 1 133 ? 11.011  -17.870 -9.242  1.00 24.50  ? 133  CYS A C     1 
ATOM   1065 O  O     . CYS A 1 133 ? 10.933  -18.369 -8.114  1.00 25.93  ? 133  CYS A O     1 
ATOM   1066 C  CB    . CYS A 1 133 ? 11.944  -15.571 -8.929  1.00 21.56  ? 133  CYS A CB    1 
ATOM   1067 S  SG    . CYS A 1 133 ? 10.469  -14.732 -9.518  1.00 25.45  ? 133  CYS A SG    1 
ATOM   1068 N  N     . MET A 1 134 ? 10.101  -18.116 -10.192 1.00 21.49  ? 134  MET A N     1 
ATOM   1069 C  CA    . MET A 1 134 ? 8.930   -18.957 -9.936  1.00 22.32  ? 134  MET A CA    1 
ATOM   1070 C  C     . MET A 1 134 ? 9.067   -20.367 -10.512 1.00 27.11  ? 134  MET A C     1 
ATOM   1071 O  O     . MET A 1 134 ? 8.054   -21.060 -10.681 1.00 23.73  ? 134  MET A O     1 
ATOM   1072 C  CB    . MET A 1 134 ? 7.659   -18.309 -10.495 1.00 24.79  ? 134  MET A CB    1 
ATOM   1073 C  CG    . MET A 1 134 ? 7.292   -16.942 -9.899  1.00 21.15  ? 134  MET A CG    1 
ATOM   1074 S  SD    . MET A 1 134 ? 5.709   -16.418 -10.606 1.00 21.63  ? 134  MET A SD    1 
ATOM   1075 C  CE    . MET A 1 134 ? 5.511   -14.782 -9.880  1.00 20.48  ? 134  MET A CE    1 
ATOM   1076 N  N     . LYS A 1 135 ? 10.288  -20.806 -10.819 1.00 28.86  ? 135  LYS A N     1 
ATOM   1077 C  CA    . LYS A 1 135 ? 10.481  -22.126 -11.416 1.00 27.48  ? 135  LYS A CA    1 
ATOM   1078 C  C     . LYS A 1 135 ? 9.870   -23.221 -10.551 1.00 28.20  ? 135  LYS A C     1 
ATOM   1079 O  O     . LYS A 1 135 ? 10.115  -23.284 -9.342  1.00 31.15  ? 135  LYS A O     1 
ATOM   1080 C  CB    . LYS A 1 135 ? 11.972  -22.400 -11.619 1.00 31.02  ? 135  LYS A CB    1 
ATOM   1081 C  CG    . LYS A 1 135 ? 12.275  -23.315 -12.798 1.00 40.83  ? 135  LYS A CG    1 
ATOM   1082 C  CD    . LYS A 1 135 ? 12.286  -22.522 -14.096 1.00 45.48  ? 135  LYS A CD    1 
ATOM   1083 C  CE    . LYS A 1 135 ? 12.719  -23.372 -15.291 1.00 47.20  ? 135  LYS A CE    1 
ATOM   1084 N  NZ    . LYS A 1 135 ? 12.979  -22.507 -16.488 1.00 54.39  ? 135  LYS A NZ    1 
ATOM   1085 N  N     . GLY A 1 136 ? 9.089   -24.102 -11.186 1.00 27.32  ? 136  GLY A N     1 
ATOM   1086 C  CA    . GLY A 1 136 ? 8.430   -25.191 -10.497 1.00 23.75  ? 136  GLY A CA    1 
ATOM   1087 C  C     . GLY A 1 136 ? 7.188   -24.809 -9.711  1.00 26.62  ? 136  GLY A C     1 
ATOM   1088 O  O     . GLY A 1 136 ? 6.605   -25.680 -9.051  1.00 31.33  ? 136  GLY A O     1 
ATOM   1089 N  N     . ARG A 1 137 ? 6.777   -23.540 -9.737  1.00 28.51  ? 137  ARG A N     1 
ATOM   1090 C  CA    . ARG A 1 137 ? 5.631   -23.059 -8.971  1.00 25.05  ? 137  ARG A CA    1 
ATOM   1091 C  C     . ARG A 1 137 ? 4.518   -22.588 -9.901  1.00 20.20  ? 137  ARG A C     1 
ATOM   1092 O  O     . ARG A 1 137 ? 4.705   -22.408 -11.108 1.00 23.09  ? 137  ARG A O     1 
ATOM   1093 C  CB    . ARG A 1 137 ? 6.033   -21.920 -8.021  1.00 26.96  ? 137  ARG A CB    1 
ATOM   1094 C  CG    . ARG A 1 137 ? 7.001   -22.332 -6.931  1.00 29.30  ? 137  ARG A CG    1 
ATOM   1095 C  CD    . ARG A 1 137 ? 7.225   -21.216 -5.932  1.00 29.02  ? 137  ARG A CD    1 
ATOM   1096 N  NE    . ARG A 1 137 ? 8.300   -21.521 -4.992  1.00 33.09  ? 137  ARG A NE    1 
ATOM   1097 C  CZ    . ARG A 1 137 ? 8.162   -22.297 -3.925  1.00 30.34  ? 137  ARG A CZ    1 
ATOM   1098 N  NH1   . ARG A 1 137 ? 7.011   -22.871 -3.636  1.00 31.33  ? 137  ARG A NH1   1 
ATOM   1099 N  NH2   . ARG A 1 137 ? 9.206   -22.493 -3.125  1.00 36.34  ? 137  ARG A NH2   1 
ATOM   1100 N  N     . THR A 1 138 ? 3.343   -22.392 -9.316  1.00 21.85  ? 138  THR A N     1 
ATOM   1101 C  CA    . THR A 1 138 ? 2.195   -21.831 -10.017 1.00 24.65  ? 138  THR A CA    1 
ATOM   1102 C  C     . THR A 1 138 ? 2.196   -20.310 -9.885  1.00 23.13  ? 138  THR A C     1 
ATOM   1103 O  O     . THR A 1 138 ? 2.345   -19.776 -8.779  1.00 24.37  ? 138  THR A O     1 
ATOM   1104 C  CB    . THR A 1 138 ? 0.895   -22.402 -9.446  1.00 23.56  ? 138  THR A CB    1 
ATOM   1105 O  OG1   . THR A 1 138 ? 0.825   -23.802 -9.715  1.00 24.11  ? 138  THR A OG1   1 
ATOM   1106 C  CG2   . THR A 1 138 ? -0.306  -21.742 -10.068 1.00 21.69  ? 138  THR A CG2   1 
ATOM   1107 N  N     . MET A 1 139 ? 2.036   -19.613 -11.007 1.00 20.84  ? 139  MET A N     1 
ATOM   1108 C  CA    . MET A 1 139 ? 1.793   -18.175 -10.988 1.00 24.33  ? 139  MET A CA    1 
ATOM   1109 C  C     . MET A 1 139 ? 0.289   -17.951 -10.931 1.00 22.67  ? 139  MET A C     1 
ATOM   1110 O  O     . MET A 1 139 ? -0.434  -18.276 -11.884 1.00 23.52  ? 139  MET A O     1 
ATOM   1111 C  CB    . MET A 1 139 ? 2.393   -17.486 -12.211 1.00 21.46  ? 139  MET A CB    1 
ATOM   1112 C  CG    . MET A 1 139 ? 1.813   -16.085 -12.440 1.00 23.01  ? 139  MET A CG    1 
ATOM   1113 S  SD    . MET A 1 139 ? 2.511   -15.245 -13.884 1.00 27.62  ? 139  MET A SD    1 
ATOM   1114 C  CE    . MET A 1 139 ? 4.159   -14.899 -13.303 1.00 24.60  ? 139  MET A CE    1 
ATOM   1115 N  N     . TYR A 1 140 ? -0.182  -17.390 -9.822  1.00 20.37  ? 140  TYR A N     1 
ATOM   1116 C  CA    . TYR A 1 140 ? -1.583  -17.041 -9.668  1.00 18.00  ? 140  TYR A CA    1 
ATOM   1117 C  C     . TYR A 1 140 ? -1.826  -15.628 -10.177 1.00 21.46  ? 140  TYR A C     1 
ATOM   1118 O  O     . TYR A 1 140 ? -1.038  -14.715 -9.915  1.00 18.89  ? 140  TYR A O     1 
ATOM   1119 C  CB    . TYR A 1 140 ? -2.007  -17.144 -8.198  1.00 19.51  ? 140  TYR A CB    1 
ATOM   1120 C  CG    . TYR A 1 140 ? -1.898  -18.546 -7.644  1.00 19.43  ? 140  TYR A CG    1 
ATOM   1121 C  CD1   . TYR A 1 140 ? -2.931  -19.459 -7.810  1.00 20.27  ? 140  TYR A CD1   1 
ATOM   1122 C  CD2   . TYR A 1 140 ? -0.756  -18.962 -6.963  1.00 19.65  ? 140  TYR A CD2   1 
ATOM   1123 C  CE1   . TYR A 1 140 ? -2.833  -20.764 -7.296  1.00 23.01  ? 140  TYR A CE1   1 
ATOM   1124 C  CE2   . TYR A 1 140 ? -0.649  -20.266 -6.460  1.00 22.54  ? 140  TYR A CE2   1 
ATOM   1125 C  CZ    . TYR A 1 140 ? -1.686  -21.156 -6.632  1.00 25.40  ? 140  TYR A CZ    1 
ATOM   1126 O  OH    . TYR A 1 140 ? -1.575  -22.444 -6.131  1.00 30.41  ? 140  TYR A OH    1 
ATOM   1127 N  N     . VAL A 1 141 ? -2.905  -15.460 -10.932 1.00 18.74  ? 141  VAL A N     1 
ATOM   1128 C  CA    . VAL A 1 141 ? -3.285  -14.164 -11.479 1.00 23.61  ? 141  VAL A CA    1 
ATOM   1129 C  C     . VAL A 1 141 ? -4.528  -13.711 -10.719 1.00 20.78  ? 141  VAL A C     1 
ATOM   1130 O  O     . VAL A 1 141 ? -5.619  -14.247 -10.937 1.00 19.50  ? 141  VAL A O     1 
ATOM   1131 C  CB    . VAL A 1 141 ? -3.536  -14.235 -12.992 1.00 19.00  ? 141  VAL A CB    1 
ATOM   1132 C  CG1   . VAL A 1 141 ? -3.923  -12.863 -13.549 1.00 20.31  ? 141  VAL A CG1   1 
ATOM   1133 C  CG2   . VAL A 1 141 ? -2.298  -14.775 -13.711 1.00 16.79  ? 141  VAL A CG2   1 
ATOM   1134 N  N     . ILE A 1 142 ? -4.366  -12.709 -9.853  1.00 20.39  ? 142  ILE A N     1 
ATOM   1135 C  CA    . ILE A 1 142 ? -5.425  -12.217 -8.963  1.00 16.16  ? 142  ILE A CA    1 
ATOM   1136 C  C     . ILE A 1 142 ? -6.004  -10.910 -9.492  1.00 21.71  ? 142  ILE A C     1 
ATOM   1137 O  O     . ILE A 1 142 ? -5.372  -9.854  -9.339  1.00 17.73  ? 142  ILE A O     1 
ATOM   1138 C  CB    . ILE A 1 142 ? -4.897  -11.976 -7.539  1.00 17.16  ? 142  ILE A CB    1 
ATOM   1139 C  CG1   . ILE A 1 142 ? -4.199  -13.219 -6.974  1.00 21.18  ? 142  ILE A CG1   1 
ATOM   1140 C  CG2   . ILE A 1 142 ? -6.049  -11.474 -6.630  1.00 17.41  ? 142  ILE A CG2   1 
ATOM   1141 C  CD1   . ILE A 1 142 ? -3.426  -12.949 -5.671  1.00 19.54  ? 142  ILE A CD1   1 
ATOM   1142 N  N     . PRO A 1 143 ? -7.185  -10.905 -10.093 1.00 18.97  ? 143  PRO A N     1 
ATOM   1143 C  CA    . PRO A 1 143 ? -7.801  -9.619  -10.439 1.00 20.71  ? 143  PRO A CA    1 
ATOM   1144 C  C     . PRO A 1 143 ? -8.607  -9.108  -9.256  1.00 20.41  ? 143  PRO A C     1 
ATOM   1145 O  O     . PRO A 1 143 ? -9.466  -9.835  -8.736  1.00 22.57  ? 143  PRO A O     1 
ATOM   1146 C  CB    . PRO A 1 143 ? -8.690  -9.963  -11.643 1.00 21.60  ? 143  PRO A CB    1 
ATOM   1147 C  CG    . PRO A 1 143 ? -8.760  -11.516 -11.673 1.00 25.20  ? 143  PRO A CG    1 
ATOM   1148 C  CD    . PRO A 1 143 ? -8.058  -12.030 -10.444 1.00 22.15  ? 143  PRO A CD    1 
ATOM   1149 N  N     . PHE A 1 144 ? -8.332  -7.891  -8.785  1.00 20.95  ? 144  PHE A N     1 
ATOM   1150 C  CA    . PHE A 1 144 ? -8.981  -7.442  -7.563  1.00 19.35  ? 144  PHE A CA    1 
ATOM   1151 C  C     . PHE A 1 144 ? -9.348  -5.971  -7.668  1.00 20.46  ? 144  PHE A C     1 
ATOM   1152 O  O     . PHE A 1 144 ? -8.707  -5.195  -8.383  1.00 20.26  ? 144  PHE A O     1 
ATOM   1153 C  CB    . PHE A 1 144 ? -8.101  -7.689  -6.311  1.00 21.08  ? 144  PHE A CB    1 
ATOM   1154 C  CG    . PHE A 1 144 ? -6.843  -6.860  -6.267  1.00 22.87  ? 144  PHE A CG    1 
ATOM   1155 C  CD1   . PHE A 1 144 ? -5.689  -7.284  -6.910  1.00 22.50  ? 144  PHE A CD1   1 
ATOM   1156 C  CD2   . PHE A 1 144 ? -6.811  -5.662  -5.564  1.00 21.57  ? 144  PHE A CD2   1 
ATOM   1157 C  CE1   . PHE A 1 144 ? -4.534  -6.528  -6.869  1.00 24.92  ? 144  PHE A CE1   1 
ATOM   1158 C  CE2   . PHE A 1 144 ? -5.659  -4.890  -5.524  1.00 22.94  ? 144  PHE A CE2   1 
ATOM   1159 C  CZ    . PHE A 1 144 ? -4.519  -5.318  -6.171  1.00 21.12  ? 144  PHE A CZ    1 
ATOM   1160 N  N     . SER A 1 145 ? -10.391 -5.602  -6.934  1.00 21.66  ? 145  SER A N     1 
ATOM   1161 C  CA    . SER A 1 145 ? -10.887 -4.239  -6.894  1.00 27.96  ? 145  SER A CA    1 
ATOM   1162 C  C     . SER A 1 145 ? -10.695 -3.686  -5.492  1.00 24.07  ? 145  SER A C     1 
ATOM   1163 O  O     . SER A 1 145 ? -11.063 -4.341  -4.511  1.00 24.03  ? 145  SER A O     1 
ATOM   1164 C  CB    . SER A 1 145 ? -12.366 -4.185  -7.281  1.00 26.29  ? 145  SER A CB    1 
ATOM   1165 O  OG    . SER A 1 145 ? -12.840 -2.860  -7.144  1.00 31.09  ? 145  SER A OG    1 
ATOM   1166 N  N     . MET A 1 146 ? -10.098 -2.500  -5.398  1.00 23.07  ? 146  MET A N     1 
ATOM   1167 C  CA    . MET A 1 146 ? -10.039 -1.751  -4.147  1.00 24.52  ? 146  MET A CA    1 
ATOM   1168 C  C     . MET A 1 146 ? -11.199 -0.767  -4.167  1.00 30.98  ? 146  MET A C     1 
ATOM   1169 O  O     . MET A 1 146 ? -11.233 0.140   -5.007  1.00 27.72  ? 146  MET A O     1 
ATOM   1170 C  CB    . MET A 1 146 ? -8.709  -1.017  -3.984  1.00 25.60  ? 146  MET A CB    1 
ATOM   1171 C  CG    . MET A 1 146 ? -7.489  -1.925  -4.014  1.00 25.31  ? 146  MET A CG    1 
ATOM   1172 S  SD    . MET A 1 146 ? -7.628  -3.202  -2.777  1.00 27.44  ? 146  MET A SD    1 
ATOM   1173 C  CE    . MET A 1 146 ? -7.491  -2.285  -1.241  1.00 26.63  ? 146  MET A CE    1 
ATOM   1174 N  N     . GLY A 1 147 ? -12.151 -0.951  -3.256  1.00 29.25  ? 147  GLY A N     1 
ATOM   1175 C  CA    . GLY A 1 147 ? -13.379 -0.199  -3.291  1.00 28.75  ? 147  GLY A CA    1 
ATOM   1176 C  C     . GLY A 1 147 ? -14.492 -1.006  -3.929  1.00 41.19  ? 147  GLY A C     1 
ATOM   1177 O  O     . GLY A 1 147 ? -14.246 -1.986  -4.643  1.00 32.25  ? 147  GLY A O     1 
ATOM   1178 N  N     . PRO A 1 148 ? -15.742 -0.620  -3.662  1.00 47.32  ? 148  PRO A N     1 
ATOM   1179 C  CA    . PRO A 1 148 ? -16.882 -1.346  -4.241  1.00 47.15  ? 148  PRO A CA    1 
ATOM   1180 C  C     . PRO A 1 148 ? -16.789 -1.397  -5.758  1.00 52.67  ? 148  PRO A C     1 
ATOM   1181 O  O     . PRO A 1 148 ? -16.513 -0.393  -6.417  1.00 57.30  ? 148  PRO A O     1 
ATOM   1182 C  CB    . PRO A 1 148 ? -18.094 -0.530  -3.774  1.00 48.11  ? 148  PRO A CB    1 
ATOM   1183 C  CG    . PRO A 1 148 ? -17.632 0.139   -2.527  1.00 41.60  ? 148  PRO A CG    1 
ATOM   1184 C  CD    . PRO A 1 148 ? -16.174 0.446   -2.738  1.00 38.62  ? 148  PRO A CD    1 
ATOM   1185 N  N     . LEU A 1 149 ? -17.021 -2.587  -6.307  1.00 51.04  ? 149  LEU A N     1 
ATOM   1186 C  CA    . LEU A 1 149 ? -16.851 -2.818  -7.734  1.00 56.59  ? 149  LEU A CA    1 
ATOM   1187 C  C     . LEU A 1 149 ? -17.805 -1.953  -8.548  1.00 68.81  ? 149  LEU A C     1 
ATOM   1188 O  O     . LEU A 1 149 ? -18.882 -2.407  -8.949  1.00 71.75  ? 149  LEU A O     1 
ATOM   1189 C  CB    . LEU A 1 149 ? -17.056 -4.296  -8.048  1.00 54.74  ? 149  LEU A CB    1 
ATOM   1190 C  CG    . LEU A 1 149 ? -16.624 -4.763  -9.433  1.00 51.07  ? 149  LEU A CG    1 
ATOM   1191 C  CD1   . LEU A 1 149 ? -15.173 -4.381  -9.704  1.00 50.10  ? 149  LEU A CD1   1 
ATOM   1192 C  CD2   . LEU A 1 149 ? -16.830 -6.262  -9.539  1.00 48.07  ? 149  LEU A CD2   1 
ATOM   1193 N  N     . GLY A 1 150 ? -17.415 -0.705  -8.790  1.00 71.82  ? 150  GLY A N     1 
ATOM   1194 C  CA    . GLY A 1 150 ? -18.252 0.229   -9.513  1.00 73.07  ? 150  GLY A CA    1 
ATOM   1195 C  C     . GLY A 1 150 ? -18.222 1.620   -8.918  1.00 82.36  ? 150  GLY A C     1 
ATOM   1196 O  O     . GLY A 1 150 ? -18.655 2.584   -9.556  1.00 88.36  ? 150  GLY A O     1 
ATOM   1197 N  N     . SER A 1 151 ? -17.716 1.731   -7.687  1.00 84.96  ? 151  SER A N     1 
ATOM   1198 C  CA    . SER A 1 151 ? -17.537 3.001   -6.992  1.00 85.88  ? 151  SER A CA    1 
ATOM   1199 C  C     . SER A 1 151 ? -16.734 3.974   -7.850  1.00 89.72  ? 151  SER A C     1 
ATOM   1200 O  O     . SER A 1 151 ? -15.885 3.546   -8.644  1.00 91.48  ? 151  SER A O     1 
ATOM   1201 C  CB    . SER A 1 151 ? -16.842 2.772   -5.645  1.00 83.72  ? 151  SER A CB    1 
ATOM   1202 O  OG    . SER A 1 151 ? -16.459 3.991   -5.029  1.00 80.64  ? 151  SER A OG    1 
ATOM   1203 N  N     . PRO A 1 152 ? -16.977 5.284   -7.737  1.00 94.85  ? 152  PRO A N     1 
ATOM   1204 C  CA    . PRO A 1 152 ? -16.154 6.234   -8.505  1.00 97.91  ? 152  PRO A CA    1 
ATOM   1205 C  C     . PRO A 1 152 ? -14.692 6.199   -8.109  1.00 91.08  ? 152  PRO A C     1 
ATOM   1206 O  O     . PRO A 1 152 ? -13.815 6.199   -8.981  1.00 92.16  ? 152  PRO A O     1 
ATOM   1207 C  CB    . PRO A 1 152 ? -16.802 7.591   -8.192  1.00 102.20 ? 152  PRO A CB    1 
ATOM   1208 C  CG    . PRO A 1 152 ? -17.494 7.386   -6.887  1.00 96.76  ? 152  PRO A CG    1 
ATOM   1209 C  CD    . PRO A 1 152 ? -17.995 5.971   -6.925  1.00 94.15  ? 152  PRO A CD    1 
ATOM   1210 N  N     . LEU A 1 153 ? -14.403 6.159   -6.810  1.00 74.15  ? 153  LEU A N     1 
ATOM   1211 C  CA    . LEU A 1 153 ? -13.030 6.094   -6.332  1.00 69.96  ? 153  LEU A CA    1 
ATOM   1212 C  C     . LEU A 1 153 ? -12.430 4.683   -6.419  1.00 56.71  ? 153  LEU A C     1 
ATOM   1213 O  O     . LEU A 1 153 ? -11.322 4.478   -5.919  1.00 46.76  ? 153  LEU A O     1 
ATOM   1214 C  CB    . LEU A 1 153 ? -12.947 6.625   -4.888  1.00 57.72  ? 153  LEU A CB    1 
ATOM   1215 C  CG    . LEU A 1 153 ? -13.034 8.152   -4.660  1.00 57.98  ? 153  LEU A CG    1 
ATOM   1216 C  CD1   . LEU A 1 153 ? -12.975 8.537   -3.173  1.00 38.02  ? 153  LEU A CD1   1 
ATOM   1217 C  CD2   . LEU A 1 153 ? -11.960 8.899   -5.441  1.00 40.03  ? 153  LEU A CD2   1 
ATOM   1218 N  N     . ALA A 1 154 ? -13.106 3.724   -7.054  1.00 49.73  ? 154  ALA A N     1 
ATOM   1219 C  CA    . ALA A 1 154 ? -12.622 2.346   -7.084  1.00 54.61  ? 154  ALA A CA    1 
ATOM   1220 C  C     . ALA A 1 154 ? -11.504 2.171   -8.105  1.00 42.56  ? 154  ALA A C     1 
ATOM   1221 O  O     . ALA A 1 154 ? -11.604 2.635   -9.244  1.00 39.08  ? 154  ALA A O     1 
ATOM   1222 C  CB    . ALA A 1 154 ? -13.763 1.378   -7.400  1.00 49.94  ? 154  ALA A CB    1 
ATOM   1223 N  N     . LYS A 1 155 ? -10.444 1.475   -7.696  1.00 38.45  ? 155  LYS A N     1 
ATOM   1224 C  CA    . LYS A 1 155 ? -9.309  1.172   -8.557  1.00 29.30  ? 155  LYS A CA    1 
ATOM   1225 C  C     . LYS A 1 155 ? -9.120  -0.341  -8.653  1.00 30.93  ? 155  LYS A C     1 
ATOM   1226 O  O     . LYS A 1 155 ? -9.360  -1.072  -7.688  1.00 25.28  ? 155  LYS A O     1 
ATOM   1227 C  CB    . LYS A 1 155 ? -8.033  1.828   -8.030  1.00 28.87  ? 155  LYS A CB    1 
ATOM   1228 C  CG    . LYS A 1 155 ? -8.157  3.311   -7.747  1.00 36.68  ? 155  LYS A CG    1 
ATOM   1229 C  CD    . LYS A 1 155 ? -8.301  4.115   -9.016  1.00 40.44  ? 155  LYS A CD    1 
ATOM   1230 C  CE    . LYS A 1 155 ? -8.231  5.607   -8.700  1.00 43.61  ? 155  LYS A CE    1 
ATOM   1231 N  NZ    . LYS A 1 155 ? -8.297  6.412   -9.937  1.00 49.20  ? 155  LYS A NZ    1 
ATOM   1232 N  N     . ILE A 1 156 ? -8.693  -0.810  -9.819  1.00 25.75  ? 156  ILE A N     1 
ATOM   1233 C  CA    . ILE A 1 156 ? -8.541  -2.238  -10.079 1.00 29.31  ? 156  ILE A CA    1 
ATOM   1234 C  C     . ILE A 1 156 ? -7.058  -2.558  -10.199 1.00 26.81  ? 156  ILE A C     1 
ATOM   1235 O  O     . ILE A 1 156 ? -6.290  -1.776  -10.765 1.00 26.49  ? 156  ILE A O     1 
ATOM   1236 C  CB    . ILE A 1 156 ? -9.320  -2.654  -11.346 1.00 27.81  ? 156  ILE A CB    1 
ATOM   1237 C  CG1   . ILE A 1 156 ? -10.819 -2.659  -11.049 1.00 26.28  ? 156  ILE A CG1   1 
ATOM   1238 C  CG2   . ILE A 1 156 ? -8.861  -4.023  -11.860 1.00 22.39  ? 156  ILE A CG2   1 
ATOM   1239 C  CD1   . ILE A 1 156 ? -11.698 -2.870  -12.252 1.00 35.40  ? 156  ILE A CD1   1 
ATOM   1240 N  N     . GLY A 1 157 ? -6.648  -3.698  -9.639  1.00 25.66  ? 157  GLY A N     1 
ATOM   1241 C  CA    . GLY A 1 157 ? -5.284  -4.153  -9.773  1.00 21.25  ? 157  GLY A CA    1 
ATOM   1242 C  C     . GLY A 1 157 ? -5.243  -5.612  -10.190 1.00 22.95  ? 157  GLY A C     1 
ATOM   1243 O  O     . GLY A 1 157 ? -6.209  -6.354  -10.034 1.00 19.06  ? 157  GLY A O     1 
ATOM   1244 N  N     . ILE A 1 158 ? -4.105  -6.005  -10.753 1.00 21.47  ? 158  ILE A N     1 
ATOM   1245 C  CA    . ILE A 1 158 ? -3.804  -7.405  -11.040 1.00 20.04  ? 158  ILE A CA    1 
ATOM   1246 C  C     . ILE A 1 158 ? -2.555  -7.747  -10.247 1.00 21.29  ? 158  ILE A C     1 
ATOM   1247 O  O     . ILE A 1 158 ? -1.517  -7.103  -10.430 1.00 23.61  ? 158  ILE A O     1 
ATOM   1248 C  CB    . ILE A 1 158 ? -3.562  -7.656  -12.538 1.00 19.36  ? 158  ILE A CB    1 
ATOM   1249 C  CG1   . ILE A 1 158 ? -4.710  -7.124  -13.399 1.00 24.18  ? 158  ILE A CG1   1 
ATOM   1250 C  CG2   . ILE A 1 158 ? -3.291  -9.138  -12.805 1.00 18.96  ? 158  ILE A CG2   1 
ATOM   1251 C  CD1   . ILE A 1 158 ? -5.971  -7.921  -13.331 1.00 21.35  ? 158  ILE A CD1   1 
ATOM   1252 N  N     . GLU A 1 159 ? -2.639  -8.746  -9.368  1.00 17.65  ? 159  GLU A N     1 
ATOM   1253 C  CA    . GLU A 1 159 ? -1.449  -9.225  -8.671  1.00 15.16  ? 159  GLU A CA    1 
ATOM   1254 C  C     . GLU A 1 159 ? -1.061  -10.599 -9.202  1.00 19.87  ? 159  GLU A C     1 
ATOM   1255 O  O     . GLU A 1 159 ? -1.881  -11.522 -9.218  1.00 18.30  ? 159  GLU A O     1 
ATOM   1256 C  CB    . GLU A 1 159 ? -1.620  -9.297  -7.152  1.00 14.11  ? 159  GLU A CB    1 
ATOM   1257 C  CG    . GLU A 1 159 ? -0.327  -9.851  -6.480  1.00 18.62  ? 159  GLU A CG    1 
ATOM   1258 C  CD    . GLU A 1 159 ? -0.242  -9.635  -4.977  1.00 20.74  ? 159  GLU A CD    1 
ATOM   1259 O  OE1   . GLU A 1 159 ? -1.008  -8.811  -4.460  1.00 21.93  ? 159  GLU A OE1   1 
ATOM   1260 O  OE2   . GLU A 1 159 ? 0.616   -10.263 -4.311  1.00 18.47  ? 159  GLU A OE2   1 
ATOM   1261 N  N     . LEU A 1 160 ? 0.189   -10.722 -9.627  1.00 17.03  ? 160  LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 160 ? 0.796   -12.007 -9.932  1.00 17.92  ? 160  LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 160 ? 1.569   -12.451 -8.702  1.00 22.22  ? 160  LEU A C     1 
ATOM   1264 O  O     . LEU A 1 160 ? 2.285   -11.647 -8.100  1.00 20.96  ? 160  LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 160 ? 1.734   -11.908 -11.135 1.00 14.78  ? 160  LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 160 ? 1.199   -11.121 -12.319 1.00 19.50  ? 160  LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 160 ? 2.259   -11.082 -13.429 1.00 21.48  ? 160  LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 160 ? -0.133  -11.687 -12.814 1.00 23.82  ? 160  LEU A CD2   1 
ATOM   1269 N  N     . THR A 1 161 ? 1.411   -13.717 -8.317  1.00 17.68  ? 161  THR A N     1 
ATOM   1270 C  CA    . THR A 1 161 ? 2.098   -14.214 -7.136  1.00 18.54  ? 161  THR A CA    1 
ATOM   1271 C  C     . THR A 1 161 ? 2.297   -15.715 -7.272  1.00 19.30  ? 161  THR A C     1 
ATOM   1272 O  O     . THR A 1 161 ? 1.555   -16.392 -7.985  1.00 19.48  ? 161  THR A O     1 
ATOM   1273 C  CB    . THR A 1 161 ? 1.317   -13.902 -5.850  1.00 20.37  ? 161  THR A CB    1 
ATOM   1274 O  OG1   . THR A 1 161 ? 2.025   -14.438 -4.727  1.00 18.23  ? 161  THR A OG1   1 
ATOM   1275 C  CG2   . THR A 1 161 ? -0.082  -14.530 -5.882  1.00 17.72  ? 161  THR A CG2   1 
ATOM   1276 N  N     . ASP A 1 162 ? 3.311   -16.237 -6.587  1.00 17.38  ? 162  ASP A N     1 
ATOM   1277 C  CA    . ASP A 1 162 ? 3.512   -17.681 -6.557  1.00 19.35  ? 162  ASP A CA    1 
ATOM   1278 C  C     . ASP A 1 162 ? 3.105   -18.277 -5.219  1.00 22.27  ? 162  ASP A C     1 
ATOM   1279 O  O     . ASP A 1 162 ? 3.487   -19.404 -4.905  1.00 23.79  ? 162  ASP A O     1 
ATOM   1280 C  CB    . ASP A 1 162 ? 4.961   -18.052 -6.892  1.00 18.22  ? 162  ASP A CB    1 
ATOM   1281 C  CG    . ASP A 1 162 ? 5.987   -17.234 -6.110  1.00 21.92  ? 162  ASP A CG    1 
ATOM   1282 O  OD1   . ASP A 1 162 ? 5.611   -16.529 -5.143  1.00 18.66  ? 162  ASP A OD1   1 
ATOM   1283 O  OD2   . ASP A 1 162 ? 7.188   -17.290 -6.487  1.00 24.69  ? 162  ASP A OD2   1 
ATOM   1284 N  N     . SER A 1 163 ? 2.320   -17.542 -4.430  1.00 22.55  ? 163  SER A N     1 
ATOM   1285 C  CA    . SER A 1 163 ? 1.963   -17.956 -3.082  1.00 17.76  ? 163  SER A CA    1 
ATOM   1286 C  C     . SER A 1 163 ? 0.460   -18.141 -2.970  1.00 16.88  ? 163  SER A C     1 
ATOM   1287 O  O     . SER A 1 163 ? -0.285  -17.150 -3.059  1.00 20.74  ? 163  SER A O     1 
ATOM   1288 C  CB    . SER A 1 163 ? 2.434   -16.918 -2.062  1.00 22.73  ? 163  SER A CB    1 
ATOM   1289 O  OG    . SER A 1 163 ? 1.803   -17.161 -0.816  1.00 21.73  ? 163  SER A OG    1 
ATOM   1290 N  N     . PRO A 1 164 ? -0.030  -19.366 -2.751  1.00 17.79  ? 164  PRO A N     1 
ATOM   1291 C  CA    . PRO A 1 164 ? -1.467  -19.544 -2.517  1.00 19.61  ? 164  PRO A CA    1 
ATOM   1292 C  C     . PRO A 1 164 ? -1.943  -18.880 -1.232  1.00 19.96  ? 164  PRO A C     1 
ATOM   1293 O  O     . PRO A 1 164 ? -3.119  -18.511 -1.146  1.00 18.95  ? 164  PRO A O     1 
ATOM   1294 C  CB    . PRO A 1 164 ? -1.630  -21.075 -2.477  1.00 19.03  ? 164  PRO A CB    1 
ATOM   1295 C  CG    . PRO A 1 164 ? -0.289  -21.573 -2.064  1.00 25.45  ? 164  PRO A CG    1 
ATOM   1296 C  CD    . PRO A 1 164 ? 0.710   -20.642 -2.699  1.00 18.94  ? 164  PRO A CD    1 
ATOM   1297 N  N     . TYR A 1 165 ? -1.055  -18.686 -0.250  1.00 17.38  ? 165  TYR A N     1 
ATOM   1298 C  CA    . TYR A 1 165 ? -1.420  -17.943 0.954   1.00 20.59  ? 165  TYR A CA    1 
ATOM   1299 C  C     . TYR A 1 165 ? -1.795  -16.502 0.622   1.00 20.85  ? 165  TYR A C     1 
ATOM   1300 O  O     . TYR A 1 165 ? -2.718  -15.935 1.218   1.00 20.25  ? 165  TYR A O     1 
ATOM   1301 C  CB    . TYR A 1 165 ? -0.265  -17.993 1.954   1.00 20.56  ? 165  TYR A CB    1 
ATOM   1302 C  CG    . TYR A 1 165 ? -0.434  -17.063 3.155   1.00 21.50  ? 165  TYR A CG    1 
ATOM   1303 C  CD1   . TYR A 1 165 ? -1.095  -17.489 4.312   1.00 19.48  ? 165  TYR A CD1   1 
ATOM   1304 C  CD2   . TYR A 1 165 ? 0.086   -15.778 3.135   1.00 22.45  ? 165  TYR A CD2   1 
ATOM   1305 C  CE1   . TYR A 1 165 ? -1.239  -16.636 5.408   1.00 21.62  ? 165  TYR A CE1   1 
ATOM   1306 C  CE2   . TYR A 1 165 ? -0.048  -14.924 4.216   1.00 22.50  ? 165  TYR A CE2   1 
ATOM   1307 C  CZ    . TYR A 1 165 ? -0.707  -15.360 5.348   1.00 19.70  ? 165  TYR A CZ    1 
ATOM   1308 O  OH    . TYR A 1 165 ? -0.829  -14.497 6.414   1.00 21.04  ? 165  TYR A OH    1 
ATOM   1309 N  N     . VAL A 1 166 ? -1.076  -15.891 -0.324  1.00 16.28  ? 166  VAL A N     1 
ATOM   1310 C  CA    . VAL A 1 166 ? -1.436  -14.559 -0.787  1.00 21.17  ? 166  VAL A CA    1 
ATOM   1311 C  C     . VAL A 1 166 ? -2.796  -14.593 -1.464  1.00 19.11  ? 166  VAL A C     1 
ATOM   1312 O  O     . VAL A 1 166 ? -3.632  -13.714 -1.245  1.00 18.51  ? 166  VAL A O     1 
ATOM   1313 C  CB    . VAL A 1 166 ? -0.339  -14.014 -1.730  1.00 19.14  ? 166  VAL A CB    1 
ATOM   1314 C  CG1   . VAL A 1 166 ? -0.822  -12.750 -2.473  1.00 15.79  ? 166  VAL A CG1   1 
ATOM   1315 C  CG2   . VAL A 1 166 ? 0.929   -13.735 -0.943  1.00 20.16  ? 166  VAL A CG2   1 
ATOM   1316 N  N     . VAL A 1 167 ? -3.040  -15.603 -2.303  1.00 16.76  ? 167  VAL A N     1 
ATOM   1317 C  CA    . VAL A 1 167 ? -4.314  -15.671 -3.024  1.00 18.06  ? 167  VAL A CA    1 
ATOM   1318 C  C     . VAL A 1 167 ? -5.478  -15.732 -2.047  1.00 18.79  ? 167  VAL A C     1 
ATOM   1319 O  O     . VAL A 1 167 ? -6.466  -14.991 -2.168  1.00 23.05  ? 167  VAL A O     1 
ATOM   1320 C  CB    . VAL A 1 167 ? -4.337  -16.880 -3.973  1.00 18.92  ? 167  VAL A CB    1 
ATOM   1321 C  CG1   . VAL A 1 167 ? -5.697  -16.954 -4.683  1.00 22.98  ? 167  VAL A CG1   1 
ATOM   1322 C  CG2   . VAL A 1 167 ? -3.203  -16.793 -4.966  1.00 18.70  ? 167  VAL A CG2   1 
ATOM   1323 N  N     . ALA A 1 168 ? -5.374  -16.620 -1.060  1.00 17.92  ? 168  ALA A N     1 
ATOM   1324 C  CA    . ALA A 1 168 ? -6.455  -16.817 -0.106  1.00 15.95  ? 168  ALA A CA    1 
ATOM   1325 C  C     . ALA A 1 168 ? -6.705  -15.558 0.712   1.00 21.77  ? 168  ALA A C     1 
ATOM   1326 O  O     . ALA A 1 168 ? -7.859  -15.167 0.936   1.00 21.84  ? 168  ALA A O     1 
ATOM   1327 C  CB    . ALA A 1 168 ? -6.118  -17.993 0.809   1.00 17.09  ? 168  ALA A CB    1 
ATOM   1328 N  N     . SER A 1 169 ? -5.630  -14.914 1.172   1.00 19.13  ? 169  SER A N     1 
ATOM   1329 C  CA    . SER A 1 169 ? -5.772  -13.693 1.954   1.00 18.03  ? 169  SER A CA    1 
ATOM   1330 C  C     . SER A 1 169 ? -6.336  -12.552 1.106   1.00 22.10  ? 169  SER A C     1 
ATOM   1331 O  O     . SER A 1 169 ? -7.173  -11.772 1.581   1.00 18.47  ? 169  SER A O     1 
ATOM   1332 C  CB    . SER A 1 169 ? -4.414  -13.304 2.547   1.00 20.57  ? 169  SER A CB    1 
ATOM   1333 O  OG    . SER A 1 169 ? -3.850  -14.376 3.285   1.00 21.17  ? 169  SER A OG    1 
ATOM   1334 N  N     . MET A 1 170 ? -5.891  -12.441 -0.149  1.00 14.72  ? 170  MET A N     1 
ATOM   1335 C  CA    . MET A 1 170 ? -6.427  -11.424 -1.054  1.00 16.16  ? 170  MET A CA    1 
ATOM   1336 C  C     . MET A 1 170 ? -7.910  -11.637 -1.333  1.00 19.62  ? 170  MET A C     1 
ATOM   1337 O  O     . MET A 1 170 ? -8.650  -10.670 -1.547  1.00 19.79  ? 170  MET A O     1 
ATOM   1338 C  CB    . MET A 1 170 ? -5.630  -11.420 -2.363  1.00 16.16  ? 170  MET A CB    1 
ATOM   1339 C  CG    . MET A 1 170 ? -4.235  -10.790 -2.232  1.00 15.73  ? 170  MET A CG    1 
ATOM   1340 S  SD    . MET A 1 170 ? -4.274  -8.993  -1.952  1.00 21.89  ? 170  MET A SD    1 
ATOM   1341 C  CE    . MET A 1 170 ? -4.609  -8.419  -3.615  1.00 14.42  ? 170  MET A CE    1 
ATOM   1342 N  N     . ARG A 1 171 ? -8.370  -12.888 -1.327  1.00 19.45  ? 171  ARG A N     1 
ATOM   1343 C  CA    . ARG A 1 171 ? -9.801  -13.128 -1.472  1.00 20.78  ? 171  ARG A CA    1 
ATOM   1344 C  C     . ARG A 1 171 ? -10.582 -12.527 -0.310  1.00 19.31  ? 171  ARG A C     1 
ATOM   1345 O  O     . ARG A 1 171 ? -11.714 -12.072 -0.495  1.00 19.01  ? 171  ARG A O     1 
ATOM   1346 C  CB    . ARG A 1 171 ? -10.092 -14.629 -1.591  1.00 20.68  ? 171  ARG A CB    1 
ATOM   1347 C  CG    . ARG A 1 171 ? -11.587 -14.931 -1.770  1.00 24.10  ? 171  ARG A CG    1 
ATOM   1348 C  CD    . ARG A 1 171 ? -11.888 -16.430 -1.859  1.00 31.72  ? 171  ARG A CD    1 
ATOM   1349 N  NE    . ARG A 1 171 ? -13.185 -16.662 -2.490  1.00 30.79  ? 171  ARG A NE    1 
ATOM   1350 C  CZ    . ARG A 1 171 ? -14.329 -16.834 -1.839  1.00 40.93  ? 171  ARG A CZ    1 
ATOM   1351 N  NH1   . ARG A 1 171 ? -14.374 -16.889 -0.516  1.00 35.51  ? 171  ARG A NH1   1 
ATOM   1352 N  NH2   . ARG A 1 171 ? -15.459 -16.947 -2.533  1.00 37.34  ? 171  ARG A NH2   1 
ATOM   1353 N  N     . ILE A 1 172 ? -9.989  -12.493 0.884   1.00 16.75  ? 172  ILE A N     1 
ATOM   1354 C  CA    . ILE A 1 172 ? -10.679 -11.912 2.027   1.00 19.79  ? 172  ILE A CA    1 
ATOM   1355 C  C     . ILE A 1 172 ? -10.522 -10.397 2.037   1.00 20.54  ? 172  ILE A C     1 
ATOM   1356 O  O     . ILE A 1 172 ? -11.483 -9.655  2.269   1.00 18.80  ? 172  ILE A O     1 
ATOM   1357 C  CB    . ILE A 1 172 ? -10.152 -12.540 3.328   1.00 20.41  ? 172  ILE A CB    1 
ATOM   1358 C  CG1   . ILE A 1 172 ? -10.457 -14.043 3.359   1.00 20.66  ? 172  ILE A CG1   1 
ATOM   1359 C  CG2   . ILE A 1 172 ? -10.739 -11.825 4.524   1.00 20.75  ? 172  ILE A CG2   1 
ATOM   1360 C  CD1   . ILE A 1 172 ? -9.704  -14.776 4.434   1.00 21.45  ? 172  ILE A CD1   1 
ATOM   1361 N  N     . MET A 1 173 ? -9.313  -9.921  1.760   1.00 19.37  ? 173  MET A N     1 
ATOM   1362 C  CA    . MET A 1 173 ? -8.976  -8.525  1.967   1.00 20.61  ? 173  MET A CA    1 
ATOM   1363 C  C     . MET A 1 173 ? -9.415  -7.622  0.829   1.00 18.96  ? 173  MET A C     1 
ATOM   1364 O  O     . MET A 1 173 ? -9.471  -6.401  1.018   1.00 20.03  ? 173  MET A O     1 
ATOM   1365 C  CB    . MET A 1 173 ? -7.470  -8.401  2.197   1.00 18.85  ? 173  MET A CB    1 
ATOM   1366 C  CG    . MET A 1 173 ? -7.026  -8.984  3.543   1.00 16.56  ? 173  MET A CG    1 
ATOM   1367 S  SD    . MET A 1 173 ? -7.993  -8.301  4.944   1.00 18.48  ? 173  MET A SD    1 
ATOM   1368 C  CE    . MET A 1 173 ? -7.501  -6.581  4.877   1.00 19.10  ? 173  MET A CE    1 
ATOM   1369 N  N     . THR A 1 174 ? -9.724  -8.175  -0.339  1.00 18.67  ? 174  THR A N     1 
ATOM   1370 C  CA    . THR A 1 174 ? -10.123 -7.386  -1.491  1.00 18.83  ? 174  THR A CA    1 
ATOM   1371 C  C     . THR A 1 174 ? -11.355 -8.019  -2.114  1.00 19.37  ? 174  THR A C     1 
ATOM   1372 O  O     . THR A 1 174 ? -11.805 -9.094  -1.703  1.00 19.60  ? 174  THR A O     1 
ATOM   1373 C  CB    . THR A 1 174 ? -8.993  -7.287  -2.528  1.00 22.34  ? 174  THR A CB    1 
ATOM   1374 O  OG1   . THR A 1 174 ? -8.775  -8.578  -3.139  1.00 19.86  ? 174  THR A OG1   1 
ATOM   1375 C  CG2   . THR A 1 174 ? -7.693  -6.824  -1.859  1.00 19.18  ? 174  THR A CG2   1 
ATOM   1376 N  N     . ARG A 1 175 ? -11.898 -7.338  -3.117  1.00 20.03  ? 175  ARG A N     1 
ATOM   1377 C  CA    . ARG A 1 175 ? -12.932 -7.888  -3.983  1.00 20.82  ? 175  ARG A CA    1 
ATOM   1378 C  C     . ARG A 1 175 ? -12.256 -8.483  -5.216  1.00 22.31  ? 175  ARG A C     1 
ATOM   1379 O  O     . ARG A 1 175 ? -11.639 -7.759  -6.005  1.00 21.03  ? 175  ARG A O     1 
ATOM   1380 C  CB    . ARG A 1 175 ? -13.938 -6.804  -4.348  1.00 22.18  ? 175  ARG A CB    1 
ATOM   1381 C  CG    . ARG A 1 175 ? -14.669 -6.276  -3.084  1.00 24.18  ? 175  ARG A CG    1 
ATOM   1382 C  CD    . ARG A 1 175 ? -15.314 -4.948  -3.296  1.00 36.58  ? 175  ARG A CD    1 
ATOM   1383 N  NE    . ARG A 1 175 ? -16.129 -4.584  -2.145  1.00 32.32  ? 175  ARG A NE    1 
ATOM   1384 C  CZ    . ARG A 1 175 ? -15.724 -3.826  -1.134  1.00 35.26  ? 175  ARG A CZ    1 
ATOM   1385 N  NH1   . ARG A 1 175 ? -14.506 -3.309  -1.099  1.00 22.36  ? 175  ARG A NH1   1 
ATOM   1386 N  NH2   . ARG A 1 175 ? -16.570 -3.567  -0.139  1.00 34.59  ? 175  ARG A NH2   1 
ATOM   1387 N  N     . MET A 1 176 ? -12.382 -9.796  -5.383  1.00 21.92  ? 176  MET A N     1 
ATOM   1388 C  CA    . MET A 1 176 ? -11.448 -10.555 -6.212  1.00 26.40  ? 176  MET A CA    1 
ATOM   1389 C  C     . MET A 1 176 ? -12.190 -11.529 -7.114  1.00 23.88  ? 176  MET A C     1 
ATOM   1390 O  O     . MET A 1 176 ? -13.130 -12.191 -6.666  1.00 23.95  ? 176  MET A O     1 
ATOM   1391 C  CB    . MET A 1 176 ? -10.472 -11.335 -5.316  1.00 24.36  ? 176  MET A CB    1 
ATOM   1392 C  CG    . MET A 1 176 ? -9.322  -11.933 -6.037  1.00 27.37  ? 176  MET A CG    1 
ATOM   1393 S  SD    . MET A 1 176 ? -9.510  -13.654 -6.513  1.00 33.70  ? 176  MET A SD    1 
ATOM   1394 C  CE    . MET A 1 176 ? -8.941  -14.443 -5.018  1.00 25.63  ? 176  MET A CE    1 
ATOM   1395 N  N     . GLY A 1 177 ? -11.761 -11.616 -8.387  1.00 26.04  ? 177  GLY A N     1 
ATOM   1396 C  CA    . GLY A 1 177 ? -12.133 -12.709 -9.260  1.00 27.77  ? 177  GLY A CA    1 
ATOM   1397 C  C     . GLY A 1 177 ? -12.671 -12.231 -10.594 1.00 28.23  ? 177  GLY A C     1 
ATOM   1398 O  O     . GLY A 1 177 ? -12.407 -11.105 -11.030 1.00 30.75  ? 177  GLY A O     1 
ATOM   1399 N  N     . THR A 1 178 ? -13.474 -13.103 -11.218 1.00 29.60  ? 178  THR A N     1 
ATOM   1400 C  CA    . THR A 1 178 ? -13.859 -12.918 -12.618 1.00 31.37  ? 178  THR A CA    1 
ATOM   1401 C  C     . THR A 1 178 ? -14.615 -11.616 -12.836 1.00 31.63  ? 178  THR A C     1 
ATOM   1402 O  O     . THR A 1 178 ? -14.416 -10.941 -13.852 1.00 32.58  ? 178  THR A O     1 
ATOM   1403 C  CB    . THR A 1 178 ? -14.716 -14.094 -13.093 1.00 31.52  ? 178  THR A CB    1 
ATOM   1404 O  OG1   . THR A 1 178 ? -13.966 -15.303 -12.987 1.00 30.38  ? 178  THR A OG1   1 
ATOM   1405 C  CG2   . THR A 1 178 ? -15.138 -13.895 -14.547 1.00 36.13  ? 178  THR A CG2   1 
ATOM   1406 N  N     . SER A 1 179 ? -15.490 -11.245 -11.897 1.00 29.37  ? 179  SER A N     1 
ATOM   1407 C  CA    . SER A 1 179 ? -16.298 -10.051 -12.105 1.00 32.23  ? 179  SER A CA    1 
ATOM   1408 C  C     . SER A 1 179 ? -15.451 -8.782  -12.151 1.00 34.30  ? 179  SER A C     1 
ATOM   1409 O  O     . SER A 1 179 ? -15.880 -7.789  -12.751 1.00 36.89  ? 179  SER A O     1 
ATOM   1410 C  CB    . SER A 1 179 ? -17.373 -9.952  -11.021 1.00 34.76  ? 179  SER A CB    1 
ATOM   1411 O  OG    . SER A 1 179 ? -16.791 -9.716  -9.754  1.00 42.53  ? 179  SER A OG    1 
ATOM   1412 N  N     . VAL A 1 180 ? -14.255 -8.791  -11.552 1.00 29.90  ? 180  VAL A N     1 
ATOM   1413 C  CA    . VAL A 1 180 ? -13.373 -7.631  -11.667 1.00 28.82  ? 180  VAL A CA    1 
ATOM   1414 C  C     . VAL A 1 180 ? -12.847 -7.506  -13.093 1.00 32.71  ? 180  VAL A C     1 
ATOM   1415 O  O     . VAL A 1 180 ? -12.762 -6.403  -13.646 1.00 32.75  ? 180  VAL A O     1 
ATOM   1416 C  CB    . VAL A 1 180 ? -12.222 -7.719  -10.644 1.00 23.63  ? 180  VAL A CB    1 
ATOM   1417 C  CG1   . VAL A 1 180 ? -11.255 -6.538  -10.823 1.00 25.46  ? 180  VAL A CG1   1 
ATOM   1418 C  CG2   . VAL A 1 180 ? -12.764 -7.727  -9.241  1.00 25.63  ? 180  VAL A CG2   1 
ATOM   1419 N  N     . LEU A 1 181 ? -12.485 -8.636  -13.711 1.00 30.98  ? 181  LEU A N     1 
ATOM   1420 C  CA    . LEU A 1 181 ? -12.027 -8.611  -15.098 1.00 33.87  ? 181  LEU A CA    1 
ATOM   1421 C  C     . LEU A 1 181 ? -13.094 -8.037  -16.022 1.00 33.55  ? 181  LEU A C     1 
ATOM   1422 O  O     . LEU A 1 181 ? -12.781 -7.296  -16.960 1.00 38.18  ? 181  LEU A O     1 
ATOM   1423 C  CB    . LEU A 1 181 ? -11.634 -10.020 -15.548 1.00 34.50  ? 181  LEU A CB    1 
ATOM   1424 C  CG    . LEU A 1 181 ? -10.300 -10.573 -15.045 1.00 35.78  ? 181  LEU A CG    1 
ATOM   1425 C  CD1   . LEU A 1 181 ? -10.187 -12.046 -15.363 1.00 31.22  ? 181  LEU A CD1   1 
ATOM   1426 C  CD2   . LEU A 1 181 ? -9.154  -9.807  -15.674 1.00 37.70  ? 181  LEU A CD2   1 
ATOM   1427 N  N     . GLU A 1 182 ? -14.360 -8.375  -15.780 1.00 36.20  ? 182  GLU A N     1 
ATOM   1428 C  CA    . GLU A 1 182 ? -15.426 -7.832  -16.614 1.00 40.53  ? 182  GLU A CA    1 
ATOM   1429 C  C     . GLU A 1 182 ? -15.570 -6.327  -16.418 1.00 43.43  ? 182  GLU A C     1 
ATOM   1430 O  O     . GLU A 1 182 ? -15.755 -5.586  -17.391 1.00 49.59  ? 182  GLU A O     1 
ATOM   1431 C  CB    . GLU A 1 182 ? -16.737 -8.553  -16.316 1.00 41.90  ? 182  GLU A CB    1 
ATOM   1432 C  CG    . GLU A 1 182 ? -16.759 -9.972  -16.837 1.00 51.97  ? 182  GLU A CG    1 
ATOM   1433 C  CD    . GLU A 1 182 ? -17.978 -10.742 -16.386 1.00 65.37  ? 182  GLU A CD    1 
ATOM   1434 O  OE1   . GLU A 1 182 ? -18.606 -10.332 -15.385 1.00 60.72  ? 182  GLU A OE1   1 
ATOM   1435 O  OE2   . GLU A 1 182 ? -18.305 -11.761 -17.035 1.00 79.55  ? 182  GLU A OE2   1 
ATOM   1436 N  N     . ALA A 1 183 ? -15.477 -5.855  -15.171 1.00 41.11  ? 183  ALA A N     1 
ATOM   1437 C  CA    . ALA A 1 183 ? -15.532 -4.422  -14.906 1.00 36.54  ? 183  ALA A CA    1 
ATOM   1438 C  C     . ALA A 1 183 ? -14.317 -3.694  -15.465 1.00 40.84  ? 183  ALA A C     1 
ATOM   1439 O  O     . ALA A 1 183 ? -14.406 -2.507  -15.803 1.00 44.62  ? 183  ALA A O     1 
ATOM   1440 C  CB    . ALA A 1 183 ? -15.647 -4.168  -13.402 1.00 33.94  ? 183  ALA A CB    1 
ATOM   1441 N  N     . LEU A 1 184 ? -13.176 -4.376  -15.566 1.00 39.81  ? 184  LEU A N     1 
ATOM   1442 C  CA    . LEU A 1 184 ? -11.965 -3.707  -16.025 1.00 39.90  ? 184  LEU A CA    1 
ATOM   1443 C  C     . LEU A 1 184 ? -12.026 -3.417  -17.520 1.00 36.70  ? 184  LEU A C     1 
ATOM   1444 O  O     . LEU A 1 184 ? -11.752 -2.294  -17.953 1.00 37.84  ? 184  LEU A O     1 
ATOM   1445 C  CB    . LEU A 1 184 ? -10.739 -4.554  -15.684 1.00 37.66  ? 184  LEU A CB    1 
ATOM   1446 C  CG    . LEU A 1 184 ? -9.399  -4.074  -16.236 1.00 35.34  ? 184  LEU A CG    1 
ATOM   1447 C  CD1   . LEU A 1 184 ? -9.054  -2.698  -15.675 1.00 35.58  ? 184  LEU A CD1   1 
ATOM   1448 C  CD2   . LEU A 1 184 ? -8.304  -5.083  -15.925 1.00 32.20  ? 184  LEU A CD2   1 
ATOM   1449 N  N     . GLY A 1 185 ? -12.388 -4.414  -18.322 1.00 44.35  ? 185  GLY A N     1 
ATOM   1450 C  CA    . GLY A 1 185 ? -12.352 -4.241  -19.766 1.00 43.94  ? 185  GLY A CA    1 
ATOM   1451 C  C     . GLY A 1 185 ? -10.961 -3.833  -20.205 1.00 39.50  ? 185  GLY A C     1 
ATOM   1452 O  O     . GLY A 1 185 ? -9.956  -4.387  -19.751 1.00 45.99  ? 185  GLY A O     1 
ATOM   1453 N  N     . ASP A 1 186 ? -10.889 -2.823  -21.073 1.00 44.47  ? 186  ASP A N     1 
ATOM   1454 C  CA    . ASP A 1 186 ? -9.616  -2.269  -21.522 1.00 49.49  ? 186  ASP A CA    1 
ATOM   1455 C  C     . ASP A 1 186 ? -9.198  -1.037  -20.718 1.00 49.60  ? 186  ASP A C     1 
ATOM   1456 O  O     . ASP A 1 186 ? -8.429  -0.206  -21.213 1.00 43.61  ? 186  ASP A O     1 
ATOM   1457 C  CB    . ASP A 1 186 ? -9.671  -1.938  -23.015 1.00 51.18  ? 186  ASP A CB    1 
ATOM   1458 C  CG    . ASP A 1 186 ? -9.204  -3.094  -23.892 1.00 61.68  ? 186  ASP A CG    1 
ATOM   1459 O  OD1   . ASP A 1 186 ? -8.859  -4.170  -23.347 1.00 54.16  ? 186  ASP A OD1   1 
ATOM   1460 O  OD2   . ASP A 1 186 ? -9.173  -2.921  -25.131 1.00 70.38  ? 186  ASP A OD2   1 
ATOM   1461 N  N     . GLY A 1 187 ? -9.678  -0.907  -19.481 1.00 41.77  ? 187  GLY A N     1 
ATOM   1462 C  CA    . GLY A 1 187 ? -9.280  0.189   -18.628 1.00 42.27  ? 187  GLY A CA    1 
ATOM   1463 C  C     . GLY A 1 187 ? -7.898  -0.003  -18.021 1.00 44.90  ? 187  GLY A C     1 
ATOM   1464 O  O     . GLY A 1 187 ? -7.252  -1.042  -18.165 1.00 40.64  ? 187  GLY A O     1 
ATOM   1465 N  N     . GLU A 1 188 ? -7.444  1.037   -17.323 1.00 43.34  ? 188  GLU A N     1 
ATOM   1466 C  CA    . GLU A 1 188 ? -6.147  1.016   -16.658 1.00 47.79  ? 188  GLU A CA    1 
ATOM   1467 C  C     . GLU A 1 188 ? -6.206  0.188   -15.376 1.00 40.17  ? 188  GLU A C     1 
ATOM   1468 O  O     . GLU A 1 188 ? -7.229  0.142   -14.688 1.00 36.29  ? 188  GLU A O     1 
ATOM   1469 C  CB    . GLU A 1 188 ? -5.689  2.438   -16.321 1.00 48.56  ? 188  GLU A CB    1 
ATOM   1470 C  CG    . GLU A 1 188 ? -5.683  3.408   -17.494 1.00 58.05  ? 188  GLU A CG    1 
ATOM   1471 C  CD    . GLU A 1 188 ? -4.515  3.185   -18.440 1.00 76.22  ? 188  GLU A CD    1 
ATOM   1472 O  OE1   . GLU A 1 188 ? -3.586  2.431   -18.073 1.00 76.84  ? 188  GLU A OE1   1 
ATOM   1473 O  OE2   . GLU A 1 188 ? -4.525  3.767   -19.549 1.00 78.46  ? 188  GLU A OE2   1 
ATOM   1474 N  N     . PHE A 1 189 ? -5.086  -0.454  -15.046 1.00 28.32  ? 189  PHE A N     1 
ATOM   1475 C  CA    . PHE A 1 189 ? -4.977  -1.190  -13.800 1.00 30.20  ? 189  PHE A CA    1 
ATOM   1476 C  C     . PHE A 1 189 ? -3.592  -0.991  -13.202 1.00 25.91  ? 189  PHE A C     1 
ATOM   1477 O  O     . PHE A 1 189 ? -2.636  -0.636  -13.894 1.00 25.95  ? 189  PHE A O     1 
ATOM   1478 C  CB    . PHE A 1 189 ? -5.273  -2.691  -13.999 1.00 23.29  ? 189  PHE A CB    1 
ATOM   1479 C  CG    . PHE A 1 189 ? -4.402  -3.369  -15.030 1.00 28.44  ? 189  PHE A CG    1 
ATOM   1480 C  CD1   . PHE A 1 189 ? -4.726  -3.315  -16.379 1.00 28.92  ? 189  PHE A CD1   1 
ATOM   1481 C  CD2   . PHE A 1 189 ? -3.288  -4.104  -14.645 1.00 26.18  ? 189  PHE A CD2   1 
ATOM   1482 C  CE1   . PHE A 1 189 ? -3.948  -3.956  -17.328 1.00 31.04  ? 189  PHE A CE1   1 
ATOM   1483 C  CE2   . PHE A 1 189 ? -2.499  -4.747  -15.596 1.00 26.11  ? 189  PHE A CE2   1 
ATOM   1484 C  CZ    . PHE A 1 189 ? -2.831  -4.671  -16.936 1.00 29.31  ? 189  PHE A CZ    1 
ATOM   1485 N  N     . ILE A 1 190 ? -3.506  -1.212  -11.893 1.00 24.19  ? 190  ILE A N     1 
ATOM   1486 C  CA    . ILE A 1 190 ? -2.231  -1.234  -11.185 1.00 22.04  ? 190  ILE A CA    1 
ATOM   1487 C  C     . ILE A 1 190 ? -1.611  -2.614  -11.340 1.00 27.28  ? 190  ILE A C     1 
ATOM   1488 O  O     . ILE A 1 190 ? -2.264  -3.633  -11.076 1.00 23.54  ? 190  ILE A O     1 
ATOM   1489 C  CB    . ILE A 1 190 ? -2.426  -0.891  -9.700  1.00 26.94  ? 190  ILE A CB    1 
ATOM   1490 C  CG1   . ILE A 1 190 ? -3.131  0.459   -9.541  1.00 30.94  ? 190  ILE A CG1   1 
ATOM   1491 C  CG2   . ILE A 1 190 ? -1.086  -0.954  -8.949  1.00 26.26  ? 190  ILE A CG2   1 
ATOM   1492 C  CD1   . ILE A 1 190 ? -2.467  1.602   -10.244 1.00 32.92  ? 190  ILE A CD1   1 
ATOM   1493 N  N     . LYS A 1 191 ? -0.340  -2.651  -11.740 1.00 21.44  ? 191  LYS A N     1 
ATOM   1494 C  CA    . LYS A 1 191 ? 0.372   -3.901  -11.977 1.00 23.32  ? 191  LYS A CA    1 
ATOM   1495 C  C     . LYS A 1 191 ? 1.133   -4.290  -10.718 1.00 23.06  ? 191  LYS A C     1 
ATOM   1496 O  O     . LYS A 1 191 ? 1.982   -3.532  -10.239 1.00 22.82  ? 191  LYS A O     1 
ATOM   1497 C  CB    . LYS A 1 191 ? 1.316   -3.753  -13.170 1.00 20.00  ? 191  LYS A CB    1 
ATOM   1498 C  CG    . LYS A 1 191 ? 0.586   -3.327  -14.421 1.00 25.92  ? 191  LYS A CG    1 
ATOM   1499 C  CD    . LYS A 1 191 ? 1.534   -2.910  -15.537 1.00 28.15  ? 191  LYS A CD    1 
ATOM   1500 C  CE    . LYS A 1 191 ? 0.752   -2.172  -16.619 1.00 41.05  ? 191  LYS A CE    1 
ATOM   1501 N  NZ    . LYS A 1 191 ? 1.522   -1.963  -17.876 1.00 51.31  ? 191  LYS A NZ    1 
ATOM   1502 N  N     . CYS A 1 192 ? 0.809   -5.456  -10.169 1.00 17.57  ? 192  CYS A N     1 
ATOM   1503 C  CA    . CYS A 1 192 ? 1.400   -5.941  -8.930  1.00 18.62  ? 192  CYS A CA    1 
ATOM   1504 C  C     . CYS A 1 192 ? 2.112   -7.254  -9.219  1.00 21.04  ? 192  CYS A C     1 
ATOM   1505 O  O     . CYS A 1 192 ? 1.490   -8.204  -9.696  1.00 21.99  ? 192  CYS A O     1 
ATOM   1506 C  CB    . CYS A 1 192 ? 0.322   -6.119  -7.856  1.00 17.43  ? 192  CYS A CB    1 
ATOM   1507 S  SG    . CYS A 1 192 ? -0.617  -4.594  -7.562  1.00 22.79  ? 192  CYS A SG    1 
ATOM   1508 N  N     . LEU A 1 193 ? 3.409   -7.303  -8.940  1.00 15.41  ? 193  LEU A N     1 
ATOM   1509 C  CA    . LEU A 1 193 ? 4.209   -8.497  -9.161  1.00 20.80  ? 193  LEU A CA    1 
ATOM   1510 C  C     . LEU A 1 193 ? 4.787   -8.915  -7.824  1.00 24.05  ? 193  LEU A C     1 
ATOM   1511 O  O     . LEU A 1 193 ? 5.452   -8.117  -7.154  1.00 21.10  ? 193  LEU A O     1 
ATOM   1512 C  CB    . LEU A 1 193 ? 5.323   -8.237  -10.188 1.00 18.74  ? 193  LEU A CB    1 
ATOM   1513 C  CG    . LEU A 1 193 ? 6.284   -9.399  -10.412 1.00 23.68  ? 193  LEU A CG    1 
ATOM   1514 C  CD1   . LEU A 1 193 ? 5.540   -10.579 -10.948 1.00 20.73  ? 193  LEU A CD1   1 
ATOM   1515 C  CD2   . LEU A 1 193 ? 7.415   -8.980  -11.373 1.00 26.43  ? 193  LEU A CD2   1 
ATOM   1516 N  N     . HIS A 1 194 ? 4.516   -10.150 -7.426  1.00 19.43  ? 194  HIS A N     1 
ATOM   1517 C  CA    . HIS A 1 194 ? 5.012   -10.665 -6.165  1.00 23.62  ? 194  HIS A CA    1 
ATOM   1518 C  C     . HIS A 1 194 ? 5.656   -12.025 -6.373  1.00 21.48  ? 194  HIS A C     1 
ATOM   1519 O  O     . HIS A 1 194 ? 5.135   -12.853 -7.121  1.00 19.72  ? 194  HIS A O     1 
ATOM   1520 C  CB    . HIS A 1 194 ? 3.880   -10.779 -5.139  1.00 17.08  ? 194  HIS A CB    1 
ATOM   1521 C  CG    . HIS A 1 194 ? 4.301   -11.423 -3.862  1.00 18.97  ? 194  HIS A CG    1 
ATOM   1522 N  ND1   . HIS A 1 194 ? 3.892   -12.688 -3.502  1.00 18.20  ? 194  HIS A ND1   1 
ATOM   1523 C  CD2   . HIS A 1 194 ? 5.099   -10.983 -2.861  1.00 19.16  ? 194  HIS A CD2   1 
ATOM   1524 C  CE1   . HIS A 1 194 ? 4.426   -13.000 -2.334  1.00 21.52  ? 194  HIS A CE1   1 
ATOM   1525 N  NE2   . HIS A 1 194 ? 5.166   -11.985 -1.927  1.00 20.17  ? 194  HIS A NE2   1 
ATOM   1526 N  N     . SER A 1 195 ? 6.780   -12.259 -5.694  1.00 17.96  ? 195  SER A N     1 
ATOM   1527 C  CA    . SER A 1 195 ? 7.319   -13.606 -5.587  1.00 20.26  ? 195  SER A CA    1 
ATOM   1528 C  C     . SER A 1 195 ? 7.922   -13.824 -4.208  1.00 22.12  ? 195  SER A C     1 
ATOM   1529 O  O     . SER A 1 195 ? 8.586   -12.932 -3.671  1.00 22.40  ? 195  SER A O     1 
ATOM   1530 C  CB    . SER A 1 195 ? 8.397   -13.877 -6.654  1.00 22.32  ? 195  SER A CB    1 
ATOM   1531 O  OG    . SER A 1 195 ? 8.946   -15.164 -6.460  1.00 22.07  ? 195  SER A OG    1 
ATOM   1532 N  N     . VAL A 1 196 ? 7.706   -15.020 -3.645  1.00 22.43  ? 196  VAL A N     1 
ATOM   1533 C  CA    . VAL A 1 196 ? 8.394   -15.384 -2.409  1.00 26.38  ? 196  VAL A CA    1 
ATOM   1534 C  C     . VAL A 1 196 ? 9.877   -15.642 -2.628  1.00 26.15  ? 196  VAL A C     1 
ATOM   1535 O  O     . VAL A 1 196 ? 10.635  -15.724 -1.650  1.00 29.01  ? 196  VAL A O     1 
ATOM   1536 C  CB    . VAL A 1 196 ? 7.745   -16.615 -1.748  1.00 25.81  ? 196  VAL A CB    1 
ATOM   1537 C  CG1   . VAL A 1 196 ? 6.282   -16.323 -1.392  1.00 30.29  ? 196  VAL A CG1   1 
ATOM   1538 C  CG2   . VAL A 1 196 ? 7.865   -17.856 -2.645  1.00 24.32  ? 196  VAL A CG2   1 
ATOM   1539 N  N     . GLY A 1 197 ? 10.308  -15.764 -3.882  1.00 27.56  ? 197  GLY A N     1 
ATOM   1540 C  CA    . GLY A 1 197 ? 11.722  -15.862 -4.214  1.00 30.88  ? 197  GLY A CA    1 
ATOM   1541 C  C     . GLY A 1 197 ? 12.363  -17.193 -3.880  1.00 32.68  ? 197  GLY A C     1 
ATOM   1542 O  O     . GLY A 1 197 ? 13.525  -17.224 -3.450  1.00 34.26  ? 197  GLY A O     1 
ATOM   1543 N  N     . CYS A 1 198 ? 11.633  -18.295 -4.059  1.00 27.76  ? 198  CYS A N     1 
ATOM   1544 C  CA    . CYS A 1 198 ? 12.121  -19.639 -3.742  1.00 33.16  ? 198  CYS A CA    1 
ATOM   1545 C  C     . CYS A 1 198 ? 11.817  -20.572 -4.899  1.00 29.49  ? 198  CYS A C     1 
ATOM   1546 O  O     . CYS A 1 198 ? 10.981  -21.478 -4.777  1.00 31.10  ? 198  CYS A O     1 
ATOM   1547 C  CB    . CYS A 1 198 ? 11.492  -20.170 -2.453  1.00 36.65  ? 198  CYS A CB    1 
ATOM   1548 S  SG    . CYS A 1 198 ? 12.029  -19.306 -0.991  1.00 41.33  ? 198  CYS A SG    1 
ATOM   1549 N  N     . PRO A 1 199 ? 12.484  -20.382 -6.040  1.00 31.73  ? 199  PRO A N     1 
ATOM   1550 C  CA    . PRO A 1 199 ? 12.288  -21.294 -7.171  1.00 30.68  ? 199  PRO A CA    1 
ATOM   1551 C  C     . PRO A 1 199 ? 12.662  -22.715 -6.789  1.00 39.26  ? 199  PRO A C     1 
ATOM   1552 O  O     . PRO A 1 199 ? 13.542  -22.947 -5.957  1.00 41.33  ? 199  PRO A O     1 
ATOM   1553 C  CB    . PRO A 1 199 ? 13.232  -20.739 -8.242  1.00 34.61  ? 199  PRO A CB    1 
ATOM   1554 C  CG    . PRO A 1 199 ? 14.289  -20.028 -7.461  1.00 34.18  ? 199  PRO A CG    1 
ATOM   1555 C  CD    . PRO A 1 199 ? 13.550  -19.404 -6.305  1.00 31.29  ? 199  PRO A CD    1 
ATOM   1556 N  N     . LEU A 1 200 ? 11.958  -23.671 -7.386  1.00 37.38  ? 200  LEU A N     1 
ATOM   1557 C  CA    . LEU A 1 200 ? 12.299  -25.059 -7.115  1.00 41.21  ? 200  LEU A CA    1 
ATOM   1558 C  C     . LEU A 1 200 ? 13.260  -25.574 -8.182  1.00 47.87  ? 200  LEU A C     1 
ATOM   1559 O  O     . LEU A 1 200 ? 13.269  -25.067 -9.307  1.00 46.15  ? 200  LEU A O     1 
ATOM   1560 C  CB    . LEU A 1 200 ? 11.042  -25.922 -7.091  1.00 37.03  ? 200  LEU A CB    1 
ATOM   1561 C  CG    . LEU A 1 200 ? 9.892   -25.377 -6.252  1.00 36.94  ? 200  LEU A CG    1 
ATOM   1562 C  CD1   . LEU A 1 200 ? 8.643   -26.192 -6.494  1.00 37.77  ? 200  LEU A CD1   1 
ATOM   1563 C  CD2   . LEU A 1 200 ? 10.265  -25.389 -4.779  1.00 44.01  ? 200  LEU A CD2   1 
ATOM   1564 N  N     . PRO A 1 201 ? 14.110  -26.573 -7.875  1.00 58.44  ? 201  PRO A N     1 
ATOM   1565 C  CA    . PRO A 1 201 ? 14.249  -27.302 -6.603  1.00 55.33  ? 201  PRO A CA    1 
ATOM   1566 C  C     . PRO A 1 201 ? 14.837  -26.424 -5.506  1.00 56.47  ? 201  PRO A C     1 
ATOM   1567 O  O     . PRO A 1 201 ? 15.601  -25.496 -5.776  1.00 53.25  ? 201  PRO A O     1 
ATOM   1568 C  CB    . PRO A 1 201 ? 15.185  -28.461 -6.975  1.00 57.13  ? 201  PRO A CB    1 
ATOM   1569 C  CG    . PRO A 1 201 ? 16.058  -27.880 -8.050  1.00 60.28  ? 201  PRO A CG    1 
ATOM   1570 C  CD    . PRO A 1 201 ? 15.142  -26.981 -8.849  1.00 58.41  ? 201  PRO A CD    1 
ATOM   1571 N  N     . LEU A 1 202 ? 14.489  -26.698 -4.252  1.00 57.83  ? 202  LEU A N     1 
ATOM   1572 C  CA    . LEU A 1 202 ? 14.933  -25.851 -3.156  1.00 61.89  ? 202  LEU A CA    1 
ATOM   1573 C  C     . LEU A 1 202 ? 16.412  -26.069 -2.869  1.00 75.20  ? 202  LEU A C     1 
ATOM   1574 O  O     . LEU A 1 202 ? 16.871  -27.206 -2.721  1.00 75.24  ? 202  LEU A O     1 
ATOM   1575 C  CB    . LEU A 1 202 ? 14.102  -26.127 -1.905  1.00 61.38  ? 202  LEU A CB    1 
ATOM   1576 C  CG    . LEU A 1 202 ? 12.681  -25.563 -1.961  1.00 52.75  ? 202  LEU A CG    1 
ATOM   1577 C  CD1   . LEU A 1 202 ? 11.930  -25.831 -0.676  1.00 47.23  ? 202  LEU A CD1   1 
ATOM   1578 C  CD2   . LEU A 1 202 ? 12.722  -24.071 -2.267  1.00 47.80  ? 202  LEU A CD2   1 
ATOM   1579 N  N     . LYS A 1 203 ? 17.160  -24.968 -2.808  1.00 83.48  ? 203  LYS A N     1 
ATOM   1580 C  CA    . LYS A 1 203 ? 18.516  -25.025 -2.282  1.00 88.79  ? 203  LYS A CA    1 
ATOM   1581 C  C     . LYS A 1 203 ? 18.501  -25.003 -0.759  1.00 95.23  ? 203  LYS A C     1 
ATOM   1582 O  O     . LYS A 1 203 ? 19.201  -25.793 -0.115  1.00 97.70  ? 203  LYS A O     1 
ATOM   1583 C  CB    . LYS A 1 203 ? 19.342  -23.859 -2.827  1.00 98.99  ? 203  LYS A CB    1 
ATOM   1584 C  CG    . LYS A 1 203 ? 18.946  -23.418 -4.230  1.00 95.86  ? 203  LYS A CG    1 
ATOM   1585 C  CD    . LYS A 1 203 ? 19.781  -22.238 -4.695  1.00 101.76 ? 203  LYS A CD    1 
ATOM   1586 C  CE    . LYS A 1 203 ? 19.171  -21.580 -5.923  1.00 103.69 ? 203  LYS A CE    1 
ATOM   1587 N  NZ    . LYS A 1 203 ? 17.846  -20.967 -5.622  1.00 90.02  ? 203  LYS A NZ    1 
ATOM   1588 N  N     . LYS A 1 204 ? 17.687  -24.118 -0.173  1.00 97.92  ? 204  LYS A N     1 
ATOM   1589 C  CA    . LYS A 1 204 ? 17.553  -24.007 1.273   1.00 90.89  ? 204  LYS A CA    1 
ATOM   1590 C  C     . LYS A 1 204 ? 16.268  -24.684 1.716   1.00 86.50  ? 204  LYS A C     1 
ATOM   1591 O  O     . LYS A 1 204 ? 15.191  -24.326 1.212   1.00 79.85  ? 204  LYS A O     1 
ATOM   1592 C  CB    . LYS A 1 204 ? 17.542  -22.542 1.697   1.00 90.00  ? 204  LYS A CB    1 
ATOM   1593 C  CG    . LYS A 1 204 ? 18.548  -21.670 0.966   1.00 97.55  ? 204  LYS A CG    1 
ATOM   1594 C  CD    . LYS A 1 204 ? 18.387  -20.204 1.337   1.00 103.43 ? 204  LYS A CD    1 
ATOM   1595 C  CE    . LYS A 1 204 ? 19.391  -19.337 0.592   1.00 104.08 ? 204  LYS A CE    1 
ATOM   1596 N  NZ    . LYS A 1 204 ? 19.294  -17.904 0.981   1.00 95.47  ? 204  LYS A NZ    1 
ATOM   1597 N  N     . PRO A 1 205 ? 16.317  -25.661 2.623   1.00 84.04  ? 205  PRO A N     1 
ATOM   1598 C  CA    . PRO A 1 205 ? 15.077  -26.153 3.237   1.00 78.08  ? 205  PRO A CA    1 
ATOM   1599 C  C     . PRO A 1 205 ? 14.346  -25.031 3.966   1.00 65.70  ? 205  PRO A C     1 
ATOM   1600 O  O     . PRO A 1 205 ? 14.944  -24.033 4.379   1.00 60.81  ? 205  PRO A O     1 
ATOM   1601 C  CB    . PRO A 1 205 ? 15.563  -27.237 4.207   1.00 71.55  ? 205  PRO A CB    1 
ATOM   1602 C  CG    . PRO A 1 205 ? 16.862  -27.699 3.622   1.00 77.24  ? 205  PRO A CG    1 
ATOM   1603 C  CD    . PRO A 1 205 ? 17.485  -26.477 2.999   1.00 80.07  ? 205  PRO A CD    1 
ATOM   1604 N  N     . LEU A 1 206 ? 13.036  -25.204 4.121   1.00 57.79  ? 206  LEU A N     1 
ATOM   1605 C  CA    . LEU A 1 206 ? 12.160  -24.142 4.599   1.00 46.66  ? 206  LEU A CA    1 
ATOM   1606 C  C     . LEU A 1 206 ? 11.848  -24.305 6.082   1.00 53.07  ? 206  LEU A C     1 
ATOM   1607 O  O     . LEU A 1 206 ? 11.652  -25.422 6.574   1.00 56.49  ? 206  LEU A O     1 
ATOM   1608 C  CB    . LEU A 1 206 ? 10.855  -24.111 3.799   1.00 44.99  ? 206  LEU A CB    1 
ATOM   1609 C  CG    . LEU A 1 206 ? 10.971  -23.831 2.296   1.00 45.61  ? 206  LEU A CG    1 
ATOM   1610 C  CD1   . LEU A 1 206 ? 9.595   -23.789 1.649   1.00 41.03  ? 206  LEU A CD1   1 
ATOM   1611 C  CD2   . LEU A 1 206 ? 11.727  -22.540 2.044   1.00 38.14  ? 206  LEU A CD2   1 
ATOM   1612 N  N     . VAL A 1 207 ? 11.804  -23.180 6.789   1.00 42.55  ? 207  VAL A N     1 
ATOM   1613 C  CA    . VAL A 1 207 ? 11.367  -23.149 8.178   1.00 39.52  ? 207  VAL A CA    1 
ATOM   1614 C  C     . VAL A 1 207 ? 9.852   -23.001 8.199   1.00 40.81  ? 207  VAL A C     1 
ATOM   1615 O  O     . VAL A 1 207 ? 9.301   -22.079 7.581   1.00 37.60  ? 207  VAL A O     1 
ATOM   1616 C  CB    . VAL A 1 207 ? 12.046  -22.005 8.948   1.00 41.46  ? 207  VAL A CB    1 
ATOM   1617 C  CG1   . VAL A 1 207 ? 11.578  -21.995 10.398  1.00 41.74  ? 207  VAL A CG1   1 
ATOM   1618 C  CG2   . VAL A 1 207 ? 13.554  -22.144 8.874   1.00 44.80  ? 207  VAL A CG2   1 
ATOM   1619 N  N     . ASN A 1 208 ? 9.184   -23.927 8.896   1.00 37.96  ? 208  ASN A N     1 
ATOM   1620 C  CA    . ASN A 1 208 ? 7.728   -23.954 9.056   1.00 43.95  ? 208  ASN A CA    1 
ATOM   1621 C  C     . ASN A 1 208 ? 7.000   -24.048 7.719   1.00 40.96  ? 208  ASN A C     1 
ATOM   1622 O  O     . ASN A 1 208 ? 5.874   -23.562 7.587   1.00 41.46  ? 208  ASN A O     1 
ATOM   1623 C  CB    . ASN A 1 208 ? 7.226   -22.741 9.847   1.00 39.84  ? 208  ASN A CB    1 
ATOM   1624 C  CG    . ASN A 1 208 ? 7.090   -23.023 11.328  1.00 42.61  ? 208  ASN A CG    1 
ATOM   1625 O  OD1   . ASN A 1 208 ? 6.930   -24.174 11.745  1.00 48.89  ? 208  ASN A OD1   1 
ATOM   1626 N  ND2   . ASN A 1 208 ? 7.135   -21.964 12.138  1.00 47.18  ? 208  ASN A ND2   1 
ATOM   1627 N  N     . ASN A 1 209 ? 7.626   -24.681 6.723   1.00 40.12  ? 209  ASN A N     1 
ATOM   1628 C  CA    . ASN A 1 209 ? 7.057   -24.799 5.377   1.00 41.92  ? 209  ASN A CA    1 
ATOM   1629 C  C     . ASN A 1 209 ? 6.745   -23.437 4.757   1.00 36.44  ? 209  ASN A C     1 
ATOM   1630 O  O     . ASN A 1 209 ? 5.840   -23.323 3.929   1.00 39.73  ? 209  ASN A O     1 
ATOM   1631 C  CB    . ASN A 1 209 ? 5.788   -25.656 5.375   1.00 39.43  ? 209  ASN A CB    1 
ATOM   1632 C  CG    . ASN A 1 209 ? 6.071   -27.123 5.539   1.00 49.10  ? 209  ASN A CG    1 
ATOM   1633 O  OD1   . ASN A 1 209 ? 7.045   -27.643 4.996   1.00 53.58  ? 209  ASN A OD1   1 
ATOM   1634 N  ND2   . ASN A 1 209 ? 5.205   -27.809 6.283   1.00 38.07  ? 209  ASN A ND2   1 
ATOM   1635 N  N     . TRP A 1 210 ? 7.475   -22.393 5.136   1.00 29.74  ? 210  TRP A N     1 
ATOM   1636 C  CA    . TRP A 1 210 ? 7.146   -21.030 4.725   1.00 30.11  ? 210  TRP A CA    1 
ATOM   1637 C  C     . TRP A 1 210 ? 8.232   -20.515 3.789   1.00 29.14  ? 210  TRP A C     1 
ATOM   1638 O  O     . TRP A 1 210 ? 9.348   -20.220 4.229   1.00 29.81  ? 210  TRP A O     1 
ATOM   1639 C  CB    . TRP A 1 210 ? 6.998   -20.124 5.940   1.00 30.12  ? 210  TRP A CB    1 
ATOM   1640 C  CG    . TRP A 1 210 ? 6.585   -18.720 5.611   1.00 25.56  ? 210  TRP A CG    1 
ATOM   1641 C  CD1   . TRP A 1 210 ? 7.405   -17.638 5.435   1.00 29.69  ? 210  TRP A CD1   1 
ATOM   1642 C  CD2   . TRP A 1 210 ? 5.245   -18.242 5.439   1.00 30.41  ? 210  TRP A CD2   1 
ATOM   1643 N  NE1   . TRP A 1 210 ? 6.655   -16.509 5.169   1.00 27.21  ? 210  TRP A NE1   1 
ATOM   1644 C  CE2   . TRP A 1 210 ? 5.326   -16.855 5.165   1.00 29.79  ? 210  TRP A CE2   1 
ATOM   1645 C  CE3   . TRP A 1 210 ? 3.983   -18.851 5.488   1.00 29.28  ? 210  TRP A CE3   1 
ATOM   1646 C  CZ2   . TRP A 1 210 ? 4.193   -16.069 4.941   1.00 30.50  ? 210  TRP A CZ2   1 
ATOM   1647 C  CZ3   . TRP A 1 210 ? 2.858   -18.067 5.270   1.00 27.97  ? 210  TRP A CZ3   1 
ATOM   1648 C  CH2   . TRP A 1 210 ? 2.971   -16.688 4.995   1.00 22.24  ? 210  TRP A CH2   1 
ATOM   1649 N  N     . ALA A 1 211 ? 7.902   -20.402 2.507   1.00 25.97  ? 211  ALA A N     1 
ATOM   1650 C  CA    . ALA A 1 211 ? 8.869   -19.960 1.513   1.00 27.48  ? 211  ALA A CA    1 
ATOM   1651 C  C     . ALA A 1 211 ? 9.051   -18.453 1.603   1.00 30.77  ? 211  ALA A C     1 
ATOM   1652 O  O     . ALA A 1 211 ? 8.073   -17.695 1.621   1.00 31.77  ? 211  ALA A O     1 
ATOM   1653 C  CB    . ALA A 1 211 ? 8.417   -20.357 0.110   1.00 27.75  ? 211  ALA A CB    1 
ATOM   1654 N  N     . CYS A 1 212 ? 10.306  -18.022 1.670   1.00 28.29  ? 212  CYS A N     1 
ATOM   1655 C  CA    . CYS A 1 212 ? 10.642  -16.611 1.756   1.00 26.84  ? 212  CYS A CA    1 
ATOM   1656 C  C     . CYS A 1 212 ? 12.131  -16.483 1.470   1.00 26.28  ? 212  CYS A C     1 
ATOM   1657 O  O     . CYS A 1 212 ? 12.873  -17.468 1.483   1.00 26.86  ? 212  CYS A O     1 
ATOM   1658 C  CB    . CYS A 1 212 ? 10.285  -16.028 3.127   1.00 31.17  ? 212  CYS A CB    1 
ATOM   1659 S  SG    . CYS A 1 212 ? 11.214  -16.741 4.494   1.00 33.10  ? 212  CYS A SG    1 
ATOM   1660 N  N     . ASN A 1 213 ? 12.558  -15.256 1.214   1.00 28.95  ? 213  ASN A N     1 
ATOM   1661 C  CA    . ASN A 1 213 ? 13.960  -14.963 0.912   1.00 29.99  ? 213  ASN A CA    1 
ATOM   1662 C  C     . ASN A 1 213 ? 14.310  -13.665 1.614   1.00 27.87  ? 213  ASN A C     1 
ATOM   1663 O  O     . ASN A 1 213 ? 14.301  -12.587 1.009   1.00 36.15  ? 213  ASN A O     1 
ATOM   1664 C  CB    . ASN A 1 213 ? 14.183  -14.886 -0.597  1.00 31.66  ? 213  ASN A CB    1 
ATOM   1665 C  CG    . ASN A 1 213 ? 15.650  -14.957 -0.978  1.00 34.49  ? 213  ASN A CG    1 
ATOM   1666 O  OD1   . ASN A 1 213 ? 16.513  -14.379 -0.310  1.00 35.93  ? 213  ASN A OD1   1 
ATOM   1667 N  ND2   . ASN A 1 213 ? 15.936  -15.669 -2.058  1.00 32.82  ? 213  ASN A ND2   1 
ATOM   1668 N  N     . PRO A 1 214 ? 14.602  -13.729 2.919   1.00 29.77  ? 214  PRO A N     1 
ATOM   1669 C  CA    . PRO A 1 214 ? 14.809  -12.489 3.685   1.00 34.19  ? 214  PRO A CA    1 
ATOM   1670 C  C     . PRO A 1 214 ? 15.983  -11.659 3.189   1.00 34.60  ? 214  PRO A C     1 
ATOM   1671 O  O     . PRO A 1 214 ? 15.888  -10.426 3.140   1.00 36.29  ? 214  PRO A O     1 
ATOM   1672 C  CB    . PRO A 1 214 ? 15.037  -13.000 5.115   1.00 37.12  ? 214  PRO A CB    1 
ATOM   1673 C  CG    . PRO A 1 214 ? 14.481  -14.387 5.135   1.00 36.91  ? 214  PRO A CG    1 
ATOM   1674 C  CD    . PRO A 1 214 ? 14.709  -14.930 3.764   1.00 33.44  ? 214  PRO A CD    1 
ATOM   1675 N  N     . GLU A 1 215 ? 17.087  -12.307 2.801   1.00 33.84  ? 215  GLU A N     1 
ATOM   1676 C  CA    . GLU A 1 215 ? 18.263  -11.565 2.353   1.00 38.97  ? 215  GLU A CA    1 
ATOM   1677 C  C     . GLU A 1 215 ? 17.953  -10.693 1.144   1.00 35.16  ? 215  GLU A C     1 
ATOM   1678 O  O     . GLU A 1 215 ? 18.512  -9.597  1.008   1.00 38.26  ? 215  GLU A O     1 
ATOM   1679 C  CB    . GLU A 1 215 ? 19.397  -12.540 2.028   1.00 49.09  ? 215  GLU A CB    1 
ATOM   1680 C  CG    . GLU A 1 215 ? 19.654  -13.557 3.130   1.00 60.81  ? 215  GLU A CG    1 
ATOM   1681 C  CD    . GLU A 1 215 ? 20.620  -14.651 2.715   1.00 82.68  ? 215  GLU A CD    1 
ATOM   1682 O  OE1   . GLU A 1 215 ? 21.018  -14.682 1.528   1.00 86.56  ? 215  GLU A OE1   1 
ATOM   1683 O  OE2   . GLU A 1 215 ? 20.980  -15.483 3.580   1.00 86.45  ? 215  GLU A OE2   1 
ATOM   1684 N  N     . LEU A 1 216 ? 17.066  -11.153 0.264   1.00 34.47  ? 216  LEU A N     1 
ATOM   1685 C  CA    . LEU A 1 216 ? 16.766  -10.464 -0.981  1.00 26.98  ? 216  LEU A CA    1 
ATOM   1686 C  C     . LEU A 1 216 ? 15.455  -9.702  -0.934  1.00 30.39  ? 216  LEU A C     1 
ATOM   1687 O  O     . LEU A 1 216 ? 15.014  -9.205  -1.972  1.00 31.86  ? 216  LEU A O     1 
ATOM   1688 C  CB    . LEU A 1 216 ? 16.745  -11.462 -2.145  1.00 31.03  ? 216  LEU A CB    1 
ATOM   1689 C  CG    . LEU A 1 216 ? 18.093  -12.110 -2.463  1.00 35.97  ? 216  LEU A CG    1 
ATOM   1690 C  CD1   . LEU A 1 216 ? 17.991  -13.012 -3.690  1.00 30.99  ? 216  LEU A CD1   1 
ATOM   1691 C  CD2   . LEU A 1 216 ? 19.155  -11.028 -2.657  1.00 39.40  ? 216  LEU A CD2   1 
ATOM   1692 N  N     . THR A 1 217 ? 14.836  -9.577  0.242   1.00 32.79  ? 217  THR A N     1 
ATOM   1693 C  CA    . THR A 1 217 ? 13.528  -8.937  0.334   1.00 34.27  ? 217  THR A CA    1 
ATOM   1694 C  C     . THR A 1 217 ? 13.594  -7.490  -0.133  1.00 32.91  ? 217  THR A C     1 
ATOM   1695 O  O     . THR A 1 217 ? 14.454  -6.717  0.299   1.00 32.21  ? 217  THR A O     1 
ATOM   1696 C  CB    . THR A 1 217 ? 12.986  -9.000  1.763   1.00 28.89  ? 217  THR A CB    1 
ATOM   1697 O  OG1   . THR A 1 217 ? 12.757  -10.363 2.123   1.00 33.41  ? 217  THR A OG1   1 
ATOM   1698 C  CG2   . THR A 1 217 ? 11.674  -8.232  1.871   1.00 29.73  ? 217  THR A CG2   1 
ATOM   1699 N  N     . LEU A 1 218 ? 12.670  -7.133  -1.023  1.00 25.25  ? 218  LEU A N     1 
ATOM   1700 C  CA    . LEU A 1 218 ? 12.605  -5.802  -1.596  1.00 25.85  ? 218  LEU A CA    1 
ATOM   1701 C  C     . LEU A 1 218 ? 11.166  -5.555  -2.019  1.00 29.63  ? 218  LEU A C     1 
ATOM   1702 O  O     . LEU A 1 218 ? 10.587  -6.368  -2.748  1.00 27.23  ? 218  LEU A O     1 
ATOM   1703 C  CB    . LEU A 1 218 ? 13.565  -5.672  -2.787  1.00 29.86  ? 218  LEU A CB    1 
ATOM   1704 C  CG    . LEU A 1 218 ? 13.755  -4.254  -3.320  1.00 33.84  ? 218  LEU A CG    1 
ATOM   1705 C  CD1   . LEU A 1 218 ? 14.380  -3.375  -2.244  1.00 26.86  ? 218  LEU A CD1   1 
ATOM   1706 C  CD2   . LEU A 1 218 ? 14.617  -4.252  -4.586  1.00 39.95  ? 218  LEU A CD2   1 
ATOM   1707 N  N     . ILE A 1 219 ? 10.587  -4.458  -1.534  1.00 24.96  ? 219  ILE A N     1 
ATOM   1708 C  CA    . ILE A 1 219 ? 9.228   -4.054  -1.867  1.00 23.80  ? 219  ILE A CA    1 
ATOM   1709 C  C     . ILE A 1 219 ? 9.351   -2.708  -2.563  1.00 27.84  ? 219  ILE A C     1 
ATOM   1710 O  O     . ILE A 1 219 ? 9.711   -1.709  -1.926  1.00 27.01  ? 219  ILE A O     1 
ATOM   1711 C  CB    . ILE A 1 219 ? 8.322   -3.957  -0.628  1.00 22.08  ? 219  ILE A CB    1 
ATOM   1712 C  CG1   . ILE A 1 219 ? 8.355   -5.251  0.186   1.00 26.37  ? 219  ILE A CG1   1 
ATOM   1713 C  CG2   . ILE A 1 219 ? 6.894   -3.693  -1.059  1.00 24.64  ? 219  ILE A CG2   1 
ATOM   1714 C  CD1   . ILE A 1 219 ? 9.361   -5.266  1.323   1.00 27.53  ? 219  ILE A CD1   1 
ATOM   1715 N  N     . ALA A 1 220 ? 9.053   -2.672  -3.860  1.00 22.52  ? 220  ALA A N     1 
ATOM   1716 C  CA    . ALA A 1 220 ? 9.344   -1.507  -4.685  1.00 25.19  ? 220  ALA A CA    1 
ATOM   1717 C  C     . ALA A 1 220 ? 8.064   -0.950  -5.289  1.00 24.24  ? 220  ALA A C     1 
ATOM   1718 O  O     . ALA A 1 220 ? 7.142   -1.700  -5.631  1.00 26.03  ? 220  ALA A O     1 
ATOM   1719 C  CB    . ALA A 1 220 ? 10.335  -1.852  -5.805  1.00 27.52  ? 220  ALA A CB    1 
ATOM   1720 N  N     . HIS A 1 221 ? 8.017   0.377   -5.409  1.00 21.26  ? 221  HIS A N     1 
ATOM   1721 C  CA    . HIS A 1 221 ? 6.886   1.083   -5.992  1.00 24.65  ? 221  HIS A CA    1 
ATOM   1722 C  C     . HIS A 1 221 ? 7.390   1.986   -7.101  1.00 25.85  ? 221  HIS A C     1 
ATOM   1723 O  O     . HIS A 1 221 ? 8.394   2.686   -6.936  1.00 27.70  ? 221  HIS A O     1 
ATOM   1724 C  CB    . HIS A 1 221 ? 6.126   1.924   -4.947  1.00 21.79  ? 221  HIS A CB    1 
ATOM   1725 C  CG    . HIS A 1 221 ? 5.787   1.165   -3.704  1.00 25.33  ? 221  HIS A CG    1 
ATOM   1726 N  ND1   . HIS A 1 221 ? 6.743   0.757   -2.797  1.00 23.37  ? 221  HIS A ND1   1 
ATOM   1727 C  CD2   . HIS A 1 221 ? 4.598   0.723   -3.225  1.00 20.50  ? 221  HIS A CD2   1 
ATOM   1728 C  CE1   . HIS A 1 221 ? 6.156   0.103   -1.808  1.00 22.61  ? 221  HIS A CE1   1 
ATOM   1729 N  NE2   . HIS A 1 221 ? 4.858   0.058   -2.053  1.00 22.80  ? 221  HIS A NE2   1 
ATOM   1730 N  N     . LEU A 1 222 ? 6.681   1.967   -8.226  1.00 24.99  ? 222  LEU A N     1 
ATOM   1731 C  CA    . LEU A 1 222 ? 7.032   2.747   -9.412  1.00 25.45  ? 222  LEU A CA    1 
ATOM   1732 C  C     . LEU A 1 222 ? 5.767   3.488   -9.822  1.00 29.66  ? 222  LEU A C     1 
ATOM   1733 O  O     . LEU A 1 222 ? 5.038   3.054   -10.730 1.00 28.43  ? 222  LEU A O     1 
ATOM   1734 C  CB    . LEU A 1 222 ? 7.580   1.854   -10.529 1.00 32.19  ? 222  LEU A CB    1 
ATOM   1735 C  CG    . LEU A 1 222 ? 8.913   1.155   -10.214 1.00 30.04  ? 222  LEU A CG    1 
ATOM   1736 C  CD1   . LEU A 1 222 ? 8.717   -0.211  -9.555  1.00 31.77  ? 222  LEU A CD1   1 
ATOM   1737 C  CD2   . LEU A 1 222 ? 9.782   1.038   -11.452 1.00 41.29  ? 222  LEU A CD2   1 
ATOM   1738 N  N     . PRO A 1 223 ? 5.468   4.613   -9.158  1.00 29.03  ? 223  PRO A N     1 
ATOM   1739 C  CA    . PRO A 1 223 ? 4.171   5.272   -9.372  1.00 30.88  ? 223  PRO A CA    1 
ATOM   1740 C  C     . PRO A 1 223 ? 3.963   5.767   -10.786 1.00 32.99  ? 223  PRO A C     1 
ATOM   1741 O  O     . PRO A 1 223 ? 2.823   5.776   -11.266 1.00 35.41  ? 223  PRO A O     1 
ATOM   1742 C  CB    . PRO A 1 223 ? 4.188   6.431   -8.359  1.00 31.82  ? 223  PRO A CB    1 
ATOM   1743 C  CG    . PRO A 1 223 ? 5.617   6.600   -7.952  1.00 35.80  ? 223  PRO A CG    1 
ATOM   1744 C  CD    . PRO A 1 223 ? 6.256   5.248   -8.087  1.00 28.89  ? 223  PRO A CD    1 
ATOM   1745 N  N     . ASP A 1 224 ? 5.030   6.168   -11.479 1.00 34.94  ? 224  ASP A N     1 
ATOM   1746 C  CA    . ASP A 1 224 ? 4.865   6.666   -12.839 1.00 42.45  ? 224  ASP A CA    1 
ATOM   1747 C  C     . ASP A 1 224 ? 4.415   5.565   -13.786 1.00 41.47  ? 224  ASP A C     1 
ATOM   1748 O  O     . ASP A 1 224 ? 3.703   5.840   -14.760 1.00 46.00  ? 224  ASP A O     1 
ATOM   1749 C  CB    . ASP A 1 224 ? 6.170   7.293   -13.330 1.00 49.72  ? 224  ASP A CB    1 
ATOM   1750 C  CG    . ASP A 1 224 ? 6.589   8.484   -12.493 1.00 52.39  ? 224  ASP A CG    1 
ATOM   1751 O  OD1   . ASP A 1 224 ? 5.728   9.345   -12.218 1.00 45.43  ? 224  ASP A OD1   1 
ATOM   1752 O  OD2   . ASP A 1 224 ? 7.774   8.551   -12.101 1.00 61.33  ? 224  ASP A OD2   1 
ATOM   1753 N  N     . ARG A 1 225 ? 4.811   4.321   -13.516 1.00 36.70  ? 225  ARG A N     1 
ATOM   1754 C  CA    . ARG A 1 225 ? 4.419   3.176   -14.321 1.00 37.51  ? 225  ARG A CA    1 
ATOM   1755 C  C     . ARG A 1 225 ? 3.258   2.395   -13.714 1.00 40.82  ? 225  ARG A C     1 
ATOM   1756 O  O     . ARG A 1 225 ? 2.849   1.375   -14.285 1.00 37.79  ? 225  ARG A O     1 
ATOM   1757 C  CB    . ARG A 1 225 ? 5.620   2.249   -14.517 1.00 43.85  ? 225  ARG A CB    1 
ATOM   1758 C  CG    . ARG A 1 225 ? 6.915   3.002   -14.782 1.00 55.53  ? 225  ARG A CG    1 
ATOM   1759 C  CD    . ARG A 1 225 ? 8.113   2.075   -14.733 1.00 60.09  ? 225  ARG A CD    1 
ATOM   1760 N  NE    . ARG A 1 225 ? 8.203   1.251   -15.929 1.00 62.90  ? 225  ARG A NE    1 
ATOM   1761 C  CZ    . ARG A 1 225 ? 8.880   1.594   -17.017 1.00 68.94  ? 225  ARG A CZ    1 
ATOM   1762 N  NH1   . ARG A 1 225 ? 9.552   2.733   -17.082 1.00 74.33  ? 225  ARG A NH1   1 
ATOM   1763 N  NH2   . ARG A 1 225 ? 8.880   0.777   -18.066 1.00 62.61  ? 225  ARG A NH2   1 
ATOM   1764 N  N     . ARG A 1 226 ? 2.729   2.843   -12.573 1.00 32.11  ? 226  ARG A N     1 
ATOM   1765 C  CA    . ARG A 1 226 ? 1.612   2.175   -11.905 1.00 35.40  ? 226  ARG A CA    1 
ATOM   1766 C  C     . ARG A 1 226 ? 1.950   0.717   -11.604 1.00 31.90  ? 226  ARG A C     1 
ATOM   1767 O  O     . ARG A 1 226 ? 1.139   -0.183  -11.827 1.00 29.79  ? 226  ARG A O     1 
ATOM   1768 C  CB    . ARG A 1 226 ? 0.333   2.266   -12.742 1.00 38.31  ? 226  ARG A CB    1 
ATOM   1769 C  CG    . ARG A 1 226 ? 0.066   3.629   -13.342 1.00 46.15  ? 226  ARG A CG    1 
ATOM   1770 C  CD    . ARG A 1 226 ? -0.446  4.577   -12.295 1.00 42.36  ? 226  ARG A CD    1 
ATOM   1771 N  NE    . ARG A 1 226 ? -1.013  5.790   -12.876 1.00 54.14  ? 226  ARG A NE    1 
ATOM   1772 C  CZ    . ARG A 1 226 ? -0.554  7.013   -12.647 1.00 52.78  ? 226  ARG A CZ    1 
ATOM   1773 N  NH1   . ARG A 1 226 ? 0.505   7.222   -11.881 1.00 42.93  ? 226  ARG A NH1   1 
ATOM   1774 N  NH2   . ARG A 1 226 ? -1.188  8.054   -13.180 1.00 55.18  ? 226  ARG A NH2   1 
ATOM   1775 N  N     . GLU A 1 227 ? 3.167   0.478   -11.124 1.00 27.99  ? 227  GLU A N     1 
ATOM   1776 C  CA    . GLU A 1 227 ? 3.656   -0.865  -10.862 1.00 30.31  ? 227  GLU A CA    1 
ATOM   1777 C  C     . GLU A 1 227 ? 4.127   -0.979  -9.426  1.00 23.27  ? 227  GLU A C     1 
ATOM   1778 O  O     . GLU A 1 227 ? 4.752   -0.056  -8.891  1.00 24.60  ? 227  GLU A O     1 
ATOM   1779 C  CB    . GLU A 1 227 ? 4.814   -1.247  -11.800 1.00 27.22  ? 227  GLU A CB    1 
ATOM   1780 C  CG    . GLU A 1 227 ? 4.416   -1.299  -13.252 1.00 35.77  ? 227  GLU A CG    1 
ATOM   1781 C  CD    . GLU A 1 227 ? 5.563   -1.698  -14.153 1.00 38.94  ? 227  GLU A CD    1 
ATOM   1782 O  OE1   . GLU A 1 227 ? 6.604   -2.151  -13.634 1.00 37.29  ? 227  GLU A OE1   1 
ATOM   1783 O  OE2   . GLU A 1 227 ? 5.415   -1.547  -15.382 1.00 52.21  ? 227  GLU A OE2   1 
ATOM   1784 N  N     . ILE A 1 228 ? 3.816   -2.117  -8.817  1.00 21.33  ? 228  ILE A N     1 
ATOM   1785 C  CA    . ILE A 1 228 ? 4.335   -2.512  -7.515  1.00 19.28  ? 228  ILE A CA    1 
ATOM   1786 C  C     . ILE A 1 228 ? 5.022   -3.851  -7.707  1.00 18.48  ? 228  ILE A C     1 
ATOM   1787 O  O     . ILE A 1 228 ? 4.420   -4.772  -8.261  1.00 19.84  ? 228  ILE A O     1 
ATOM   1788 C  CB    . ILE A 1 228 ? 3.213   -2.642  -6.470  1.00 17.83  ? 228  ILE A CB    1 
ATOM   1789 C  CG1   . ILE A 1 228 ? 2.432   -1.329  -6.328  1.00 22.02  ? 228  ILE A CG1   1 
ATOM   1790 C  CG2   . ILE A 1 228 ? 3.786   -3.125  -5.141  1.00 20.17  ? 228  ILE A CG2   1 
ATOM   1791 C  CD1   . ILE A 1 228 ? 1.104   -1.484  -5.576  1.00 21.38  ? 228  ILE A CD1   1 
ATOM   1792 N  N     . ILE A 1 229 ? 6.247   -3.977  -7.204  1.00 18.36  ? 229  ILE A N     1 
ATOM   1793 C  CA    . ILE A 1 229 ? 7.079   -5.153  -7.425  1.00 16.90  ? 229  ILE A CA    1 
ATOM   1794 C  C     . ILE A 1 229 ? 7.656   -5.572  -6.086  1.00 21.04  ? 229  ILE A C     1 
ATOM   1795 O  O     . ILE A 1 229 ? 8.437   -4.827  -5.487  1.00 22.04  ? 229  ILE A O     1 
ATOM   1796 C  CB    . ILE A 1 229 ? 8.205   -4.865  -8.433  1.00 22.45  ? 229  ILE A CB    1 
ATOM   1797 C  CG1   . ILE A 1 229 ? 7.609   -4.510  -9.796  1.00 24.81  ? 229  ILE A CG1   1 
ATOM   1798 C  CG2   . ILE A 1 229 ? 9.169   -6.046  -8.535  1.00 19.28  ? 229  ILE A CG2   1 
ATOM   1799 C  CD1   . ILE A 1 229 ? 8.643   -4.088  -10.825 1.00 30.90  ? 229  ILE A CD1   1 
ATOM   1800 N  N     . SER A 1 230 ? 7.300   -6.767  -5.627  1.00 16.70  ? 230  SER A N     1 
ATOM   1801 C  CA    . SER A 1 230 ? 7.652   -7.199  -4.282  1.00 19.77  ? 230  SER A CA    1 
ATOM   1802 C  C     . SER A 1 230 ? 8.271   -8.586  -4.311  1.00 21.30  ? 230  SER A C     1 
ATOM   1803 O  O     . SER A 1 230 ? 7.761   -9.481  -4.984  1.00 24.07  ? 230  SER A O     1 
ATOM   1804 C  CB    . SER A 1 230 ? 6.406   -7.201  -3.385  1.00 20.00  ? 230  SER A CB    1 
ATOM   1805 O  OG    . SER A 1 230 ? 6.737   -7.640  -2.096  1.00 21.25  ? 230  SER A OG    1 
ATOM   1806 N  N     . PHE A 1 231 ? 9.347   -8.776  -3.543  1.00 19.53  ? 231  PHE A N     1 
ATOM   1807 C  CA    . PHE A 1 231 ? 10.156  -9.987  -3.632  1.00 18.53  ? 231  PHE A CA    1 
ATOM   1808 C  C     . PHE A 1 231 ? 10.610  -10.436 -2.252  1.00 24.27  ? 231  PHE A C     1 
ATOM   1809 O  O     . PHE A 1 231 ? 11.134  -9.631  -1.482  1.00 27.15  ? 231  PHE A O     1 
ATOM   1810 C  CB    . PHE A 1 231 ? 11.392  -9.747  -4.515  1.00 23.24  ? 231  PHE A CB    1 
ATOM   1811 C  CG    . PHE A 1 231 ? 12.184  -10.990 -4.798  1.00 24.11  ? 231  PHE A CG    1 
ATOM   1812 C  CD1   . PHE A 1 231 ? 11.873  -11.785 -5.884  1.00 23.93  ? 231  PHE A CD1   1 
ATOM   1813 C  CD2   . PHE A 1 231 ? 13.233  -11.369 -3.975  1.00 24.09  ? 231  PHE A CD2   1 
ATOM   1814 C  CE1   . PHE A 1 231 ? 12.600  -12.948 -6.151  1.00 24.17  ? 231  PHE A CE1   1 
ATOM   1815 C  CE2   . PHE A 1 231 ? 13.959  -12.521 -4.234  1.00 24.35  ? 231  PHE A CE2   1 
ATOM   1816 C  CZ    . PHE A 1 231 ? 13.644  -13.308 -5.318  1.00 24.55  ? 231  PHE A CZ    1 
ATOM   1817 N  N     . GLY A 1 232 ? 10.419  -11.719 -1.941  1.00 20.52  ? 232  GLY A N     1 
ATOM   1818 C  CA    . GLY A 1 232 ? 11.112  -12.350 -0.844  1.00 25.43  ? 232  GLY A CA    1 
ATOM   1819 C  C     . GLY A 1 232 ? 10.321  -12.495 0.448   1.00 30.47  ? 232  GLY A C     1 
ATOM   1820 O  O     . GLY A 1 232 ? 10.728  -13.277 1.311   1.00 28.94  ? 232  GLY A O     1 
ATOM   1821 N  N     . SER A 1 233 ? 9.221   -11.761 0.615   1.00 26.85  ? 233  SER A N     1 
ATOM   1822 C  CA    . SER A 1 233 ? 8.404   -11.843 1.822   1.00 25.01  ? 233  SER A CA    1 
ATOM   1823 C  C     . SER A 1 233 ? 7.005   -12.332 1.480   1.00 25.12  ? 233  SER A C     1 
ATOM   1824 O  O     . SER A 1 233 ? 6.389   -11.854 0.524   1.00 25.61  ? 233  SER A O     1 
ATOM   1825 C  CB    . SER A 1 233 ? 8.304   -10.484 2.517   1.00 24.89  ? 233  SER A CB    1 
ATOM   1826 O  OG    . SER A 1 233 ? 7.397   -10.556 3.603   1.00 22.97  ? 233  SER A OG    1 
ATOM   1827 N  N     . GLY A 1 234 ? 6.500   -13.283 2.262   1.00 26.44  ? 234  GLY A N     1 
ATOM   1828 C  CA    . GLY A 1 234 ? 5.112   -13.655 2.086   1.00 25.34  ? 234  GLY A CA    1 
ATOM   1829 C  C     . GLY A 1 234 ? 4.141   -12.965 3.015   1.00 31.30  ? 234  GLY A C     1 
ATOM   1830 O  O     . GLY A 1 234 ? 2.941   -13.248 2.957   1.00 27.75  ? 234  GLY A O     1 
ATOM   1831 N  N     . TYR A 1 235 ? 4.615   -12.032 3.839   1.00 23.29  ? 235  TYR A N     1 
ATOM   1832 C  CA    . TYR A 1 235 ? 3.882   -11.559 5.005   1.00 27.91  ? 235  TYR A CA    1 
ATOM   1833 C  C     . TYR A 1 235 ? 3.132   -10.264 4.735   1.00 26.56  ? 235  TYR A C     1 
ATOM   1834 O  O     . TYR A 1 235 ? 3.696   -9.312  4.174   1.00 28.10  ? 235  TYR A O     1 
ATOM   1835 C  CB    . TYR A 1 235 ? 4.817   -11.336 6.193   1.00 29.55  ? 235  TYR A CB    1 
ATOM   1836 C  CG    . TYR A 1 235 ? 4.034   -11.273 7.476   1.00 29.35  ? 235  TYR A CG    1 
ATOM   1837 C  CD1   . TYR A 1 235 ? 3.754   -12.440 8.173   1.00 28.10  ? 235  TYR A CD1   1 
ATOM   1838 C  CD2   . TYR A 1 235 ? 3.522   -10.066 7.963   1.00 31.07  ? 235  TYR A CD2   1 
ATOM   1839 C  CE1   . TYR A 1 235 ? 3.020   -12.420 9.328   1.00 32.68  ? 235  TYR A CE1   1 
ATOM   1840 C  CE2   . TYR A 1 235 ? 2.766   -10.035 9.144   1.00 29.09  ? 235  TYR A CE2   1 
ATOM   1841 C  CZ    . TYR A 1 235 ? 2.523   -11.229 9.814   1.00 29.86  ? 235  TYR A CZ    1 
ATOM   1842 O  OH    . TYR A 1 235 ? 1.785   -11.275 10.983  1.00 33.31  ? 235  TYR A OH    1 
ATOM   1843 N  N     . GLY A 1 236 ? 1.869   -10.231 5.174   1.00 20.79  ? 236  GLY A N     1 
ATOM   1844 C  CA    . GLY A 1 236 ? 1.074   -9.028  5.354   1.00 21.89  ? 236  GLY A CA    1 
ATOM   1845 C  C     . GLY A 1 236 ? 1.287   -7.901  4.365   1.00 23.57  ? 236  GLY A C     1 
ATOM   1846 O  O     . GLY A 1 236 ? 1.061   -8.064  3.162   1.00 27.43  ? 236  GLY A O     1 
ATOM   1847 N  N     . GLY A 1 237 ? 1.727   -6.746  4.867   1.00 21.06  ? 237  GLY A N     1 
ATOM   1848 C  CA    . GLY A 1 237 ? 1.865   -5.580  4.020   1.00 20.92  ? 237  GLY A CA    1 
ATOM   1849 C  C     . GLY A 1 237 ? 2.889   -5.720  2.905   1.00 22.99  ? 237  GLY A C     1 
ATOM   1850 O  O     . GLY A 1 237 ? 2.912   -4.882  1.998   1.00 21.96  ? 237  GLY A O     1 
ATOM   1851 N  N     . ASN A 1 238 ? 3.728   -6.755  2.942   1.00 20.49  ? 238  ASN A N     1 
ATOM   1852 C  CA    . ASN A 1 238 ? 4.721   -6.960  1.885   1.00 26.60  ? 238  ASN A CA    1 
ATOM   1853 C  C     . ASN A 1 238 ? 4.181   -7.731  0.690   1.00 29.23  ? 238  ASN A C     1 
ATOM   1854 O  O     . ASN A 1 238 ? 4.730   -7.618  -0.416  1.00 25.61  ? 238  ASN A O     1 
ATOM   1855 C  CB    . ASN A 1 238 ? 5.928   -7.745  2.401   1.00 20.74  ? 238  ASN A CB    1 
ATOM   1856 C  CG    . ASN A 1 238 ? 6.600   -7.093  3.582   1.00 22.24  ? 238  ASN A CG    1 
ATOM   1857 O  OD1   . ASN A 1 238 ? 6.672   -5.866  3.687   1.00 25.21  ? 238  ASN A OD1   1 
ATOM   1858 N  ND2   . ASN A 1 238 ? 7.134   -7.920  4.469   1.00 23.53  ? 238  ASN A ND2   1 
ATOM   1859 N  N     . SER A 1 239 ? 3.164   -8.555  0.902   1.00 24.59  ? 239  SER A N     1 
ATOM   1860 C  CA    . SER A 1 239 ? 2.722   -9.531  -0.081  1.00 20.14  ? 239  SER A CA    1 
ATOM   1861 C  C     . SER A 1 239 ? 1.303   -9.298  -0.556  1.00 24.58  ? 239  SER A C     1 
ATOM   1862 O  O     . SER A 1 239 ? 1.000   -9.568  -1.719  1.00 20.64  ? 239  SER A O     1 
ATOM   1863 C  CB    . SER A 1 239 ? 2.811   -10.947 0.511   1.00 25.16  ? 239  SER A CB    1 
ATOM   1864 O  OG    . SER A 1 239 ? 1.775   -11.122 1.477   1.00 22.92  ? 239  SER A OG    1 
ATOM   1865 N  N     . LEU A 1 240 ? 0.424   -8.807  0.316   1.00 21.80  ? 240  LEU A N     1 
ATOM   1866 C  CA    . LEU A 1 240 ? -0.928  -8.411  -0.066  1.00 23.24  ? 240  LEU A CA    1 
ATOM   1867 C  C     . LEU A 1 240 ? -0.832  -7.002  -0.630  1.00 22.29  ? 240  LEU A C     1 
ATOM   1868 O  O     . LEU A 1 240 ? -1.027  -6.002  0.064   1.00 22.47  ? 240  LEU A O     1 
ATOM   1869 C  CB    . LEU A 1 240 ? -1.861  -8.476  1.135   1.00 22.61  ? 240  LEU A CB    1 
ATOM   1870 C  CG    . LEU A 1 240 ? -1.741  -9.739  2.003   1.00 26.03  ? 240  LEU A CG    1 
ATOM   1871 C  CD1   . LEU A 1 240 ? -2.741  -9.666  3.163   1.00 18.24  ? 240  LEU A CD1   1 
ATOM   1872 C  CD2   . LEU A 1 240 ? -1.954  -10.998 1.185   1.00 17.87  ? 240  LEU A CD2   1 
ATOM   1873 N  N     . LEU A 1 241 ? -0.522  -6.925  -1.926  1.00 22.60  ? 241  LEU A N     1 
ATOM   1874 C  CA    . LEU A 1 241 ? -0.066  -5.658  -2.485  1.00 21.67  ? 241  LEU A CA    1 
ATOM   1875 C  C     . LEU A 1 241 ? -1.184  -4.632  -2.630  1.00 23.35  ? 241  LEU A C     1 
ATOM   1876 O  O     . LEU A 1 241 ? -0.892  -3.446  -2.816  1.00 23.11  ? 241  LEU A O     1 
ATOM   1877 C  CB    . LEU A 1 241 ? 0.616   -5.890  -3.839  1.00 17.81  ? 241  LEU A CB    1 
ATOM   1878 C  CG    . LEU A 1 241 ? 1.878   -6.744  -3.785  1.00 18.36  ? 241  LEU A CG    1 
ATOM   1879 C  CD1   . LEU A 1 241 ? 2.597   -6.774  -5.152  1.00 17.37  ? 241  LEU A CD1   1 
ATOM   1880 C  CD2   . LEU A 1 241 ? 2.834   -6.265  -2.686  1.00 20.68  ? 241  LEU A CD2   1 
ATOM   1881 N  N     . GLY A 1 242 ? -2.451  -5.049  -2.561  1.00 24.49  ? 242  GLY A N     1 
ATOM   1882 C  CA    . GLY A 1 242 ? -3.535  -4.079  -2.640  1.00 24.46  ? 242  GLY A CA    1 
ATOM   1883 C  C     . GLY A 1 242 ? -3.633  -3.159  -1.434  1.00 22.92  ? 242  GLY A C     1 
ATOM   1884 O  O     . GLY A 1 242 ? -4.230  -2.085  -1.532  1.00 25.42  ? 242  GLY A O     1 
ATOM   1885 N  N     . LYS A 1 243 ? -3.013  -3.532  -0.322  1.00 23.89  ? 243  LYS A N     1 
ATOM   1886 C  CA    . LYS A 1 243 ? -3.303  -2.925  0.968   1.00 26.40  ? 243  LYS A CA    1 
ATOM   1887 C  C     . LYS A 1 243 ? -2.422  -1.710  1.241   1.00 26.98  ? 243  LYS A C     1 
ATOM   1888 O  O     . LYS A 1 243 ? -2.848  -0.570  1.026   1.00 28.58  ? 243  LYS A O     1 
ATOM   1889 C  CB    . LYS A 1 243 ? -3.142  -3.978  2.069   1.00 22.22  ? 243  LYS A CB    1 
ATOM   1890 C  CG    . LYS A 1 243 ? -3.472  -3.473  3.473   1.00 24.38  ? 243  LYS A CG    1 
ATOM   1891 C  CD    . LYS A 1 243 ? -3.602  -4.643  4.459   1.00 19.20  ? 243  LYS A CD    1 
ATOM   1892 C  CE    . LYS A 1 243 ? -3.866  -4.156  5.877   1.00 21.54  ? 243  LYS A CE    1 
ATOM   1893 N  NZ    . LYS A 1 243 ? -5.181  -3.455  6.030   1.00 21.99  ? 243  LYS A NZ    1 
ATOM   1894 N  N     . LYS A 1 244 ? -1.193  -1.926  1.717   1.00 23.19  ? 244  LYS A N     1 
ATOM   1895 C  CA    . LYS A 1 244 ? -0.325  -0.779  1.959   1.00 16.38  ? 244  LYS A CA    1 
ATOM   1896 C  C     . LYS A 1 244 ? 0.277   -0.258  0.656   1.00 21.80  ? 244  LYS A C     1 
ATOM   1897 O  O     . LYS A 1 244 ? 0.270   0.950   0.399   1.00 17.46  ? 244  LYS A O     1 
ATOM   1898 C  CB    . LYS A 1 244 ? 0.776   -1.160  2.946   1.00 20.11  ? 244  LYS A CB    1 
ATOM   1899 C  CG    . LYS A 1 244 ? 0.238   -1.686  4.266   1.00 21.41  ? 244  LYS A CG    1 
ATOM   1900 C  CD    . LYS A 1 244 ? -0.572  -0.605  4.979   1.00 19.66  ? 244  LYS A CD    1 
ATOM   1901 C  CE    . LYS A 1 244 ? -1.023  -1.043  6.381   1.00 17.89  ? 244  LYS A CE    1 
ATOM   1902 N  NZ    . LYS A 1 244 ? -1.628  0.150   7.105   1.00 20.09  ? 244  LYS A NZ    1 
ATOM   1903 N  N     . CYS A 1 245 ? 0.779   -1.157  -0.191  1.00 17.66  ? 245  CYS A N     1 
ATOM   1904 C  CA    . CYS A 1 245 ? 1.536   -0.715  -1.367  1.00 17.27  ? 245  CYS A CA    1 
ATOM   1905 C  C     . CYS A 1 245 ? 0.648   0.063   -2.333  1.00 21.83  ? 245  CYS A C     1 
ATOM   1906 O  O     . CYS A 1 245 ? 0.978   1.183   -2.741  1.00 20.61  ? 245  CYS A O     1 
ATOM   1907 C  CB    . CYS A 1 245 ? 2.169   -1.928  -2.055  1.00 16.96  ? 245  CYS A CB    1 
ATOM   1908 S  SG    . CYS A 1 245 ? 3.360   -2.769  -1.019  1.00 20.31  ? 245  CYS A SG    1 
ATOM   1909 N  N     . PHE A 1 246 ? -0.508  -0.506  -2.672  1.00 22.33  ? 246  PHE A N     1 
ATOM   1910 C  CA    . PHE A 1 246 ? -1.475  0.101   -3.587  1.00 20.89  ? 246  PHE A CA    1 
ATOM   1911 C  C     . PHE A 1 246 ? -2.308  1.185   -2.889  1.00 21.32  ? 246  PHE A C     1 
ATOM   1912 O  O     . PHE A 1 246 ? -2.271  2.354   -3.277  1.00 24.60  ? 246  PHE A O     1 
ATOM   1913 C  CB    . PHE A 1 246 ? -2.330  -1.050  -4.136  1.00 19.73  ? 246  PHE A CB    1 
ATOM   1914 C  CG    . PHE A 1 246 ? -3.415  -0.691  -5.135  1.00 27.95  ? 246  PHE A CG    1 
ATOM   1915 C  CD1   . PHE A 1 246 ? -3.963  0.579   -5.256  1.00 30.71  ? 246  PHE A CD1   1 
ATOM   1916 C  CD2   . PHE A 1 246 ? -3.941  -1.715  -5.926  1.00 27.22  ? 246  PHE A CD2   1 
ATOM   1917 C  CE1   . PHE A 1 246 ? -4.994  0.827   -6.158  1.00 32.71  ? 246  PHE A CE1   1 
ATOM   1918 C  CE2   . PHE A 1 246 ? -4.955  -1.472  -6.834  1.00 27.98  ? 246  PHE A CE2   1 
ATOM   1919 C  CZ    . PHE A 1 246 ? -5.485  -0.199  -6.946  1.00 33.33  ? 246  PHE A CZ    1 
ATOM   1920 N  N     . ALA A 1 247 ? -3.069  0.811   -1.855  1.00 22.26  ? 247  ALA A N     1 
ATOM   1921 C  CA    . ALA A 1 247 ? -4.109  1.692   -1.329  1.00 25.32  ? 247  ALA A CA    1 
ATOM   1922 C  C     . ALA A 1 247 ? -3.591  2.828   -0.458  1.00 20.11  ? 247  ALA A C     1 
ATOM   1923 O  O     . ALA A 1 247 ? -4.363  3.759   -0.187  1.00 23.21  ? 247  ALA A O     1 
ATOM   1924 C  CB    . ALA A 1 247 ? -5.130  0.881   -0.535  1.00 23.38  ? 247  ALA A CB    1 
ATOM   1925 N  N     . LEU A 1 248 ? -2.336  2.782   0.010   1.00 21.06  ? 248  LEU A N     1 
ATOM   1926 C  CA    . LEU A 1 248 ? -1.700  3.964   0.610   1.00 20.63  ? 248  LEU A CA    1 
ATOM   1927 C  C     . LEU A 1 248 ? -0.604  4.565   -0.266  1.00 21.55  ? 248  LEU A C     1 
ATOM   1928 O  O     . LEU A 1 248 ? -0.666  5.750   -0.620  1.00 25.98  ? 248  LEU A O     1 
ATOM   1929 C  CB    . LEU A 1 248 ? -1.142  3.613   1.994   1.00 19.16  ? 248  LEU A CB    1 
ATOM   1930 C  CG    . LEU A 1 248 ? -2.206  3.443   3.098   1.00 19.45  ? 248  LEU A CG    1 
ATOM   1931 C  CD1   . LEU A 1 248 ? -1.514  3.283   4.429   1.00 18.66  ? 248  LEU A CD1   1 
ATOM   1932 C  CD2   . LEU A 1 248 ? -3.175  4.638   3.136   1.00 18.10  ? 248  LEU A CD2   1 
ATOM   1933 N  N     . ARG A 1 249 ? 0.430   3.804   -0.622  1.00 21.30  ? 249  ARG A N     1 
ATOM   1934 C  CA    . ARG A 1 249 ? 1.581   4.452   -1.258  1.00 24.19  ? 249  ARG A CA    1 
ATOM   1935 C  C     . ARG A 1 249 ? 1.260   4.883   -2.681  1.00 24.20  ? 249  ARG A C     1 
ATOM   1936 O  O     . ARG A 1 249 ? 1.376   6.065   -3.027  1.00 22.33  ? 249  ARG A O     1 
ATOM   1937 C  CB    . ARG A 1 249 ? 2.804   3.544   -1.225  1.00 24.99  ? 249  ARG A CB    1 
ATOM   1938 C  CG    . ARG A 1 249 ? 3.291   3.311   0.181   1.00 27.80  ? 249  ARG A CG    1 
ATOM   1939 C  CD    . ARG A 1 249 ? 4.737   2.853   0.230   1.00 24.22  ? 249  ARG A CD    1 
ATOM   1940 N  NE    . ARG A 1 249 ? 4.991   2.245   1.530   1.00 26.81  ? 249  ARG A NE    1 
ATOM   1941 C  CZ    . ARG A 1 249 ? 4.744   0.974   1.812   1.00 24.99  ? 249  ARG A CZ    1 
ATOM   1942 N  NH1   . ARG A 1 249 ? 4.316   0.130   0.883   1.00 26.54  ? 249  ARG A NH1   1 
ATOM   1943 N  NH2   . ARG A 1 249 ? 4.953   0.530   3.047   1.00 28.78  ? 249  ARG A NH2   1 
ATOM   1944 N  N     . ILE A 1 250 ? 0.856   3.939   -3.531  1.00 26.12  ? 250  ILE A N     1 
ATOM   1945 C  CA    . ILE A 1 250 ? 0.518   4.311   -4.903  1.00 26.07  ? 250  ILE A CA    1 
ATOM   1946 C  C     . ILE A 1 250 ? -0.660  5.276   -4.912  1.00 26.58  ? 250  ILE A C     1 
ATOM   1947 O  O     . ILE A 1 250 ? -0.681  6.254   -5.668  1.00 23.09  ? 250  ILE A O     1 
ATOM   1948 C  CB    . ILE A 1 250 ? 0.240   3.049   -5.743  1.00 25.84  ? 250  ILE A CB    1 
ATOM   1949 C  CG1   . ILE A 1 250 ? 1.541   2.282   -5.957  1.00 25.23  ? 250  ILE A CG1   1 
ATOM   1950 C  CG2   . ILE A 1 250 ? -0.382  3.407   -7.085  1.00 28.46  ? 250  ILE A CG2   1 
ATOM   1951 C  CD1   . ILE A 1 250 ? 2.623   3.132   -6.567  1.00 25.17  ? 250  ILE A CD1   1 
ATOM   1952 N  N     . ALA A 1 251 ? -1.646  5.026   -4.047  1.00 24.75  ? 251  ALA A N     1 
ATOM   1953 C  CA    . ALA A 1 251 ? -2.890  5.783   -4.074  1.00 25.93  ? 251  ALA A CA    1 
ATOM   1954 C  C     . ALA A 1 251 ? -2.708  7.202   -3.567  1.00 21.33  ? 251  ALA A C     1 
ATOM   1955 O  O     . ALA A 1 251 ? -3.420  8.105   -4.010  1.00 22.65  ? 251  ALA A O     1 
ATOM   1956 C  CB    . ALA A 1 251 ? -3.959  5.074   -3.228  1.00 19.58  ? 251  ALA A CB    1 
ATOM   1957 N  N     . SER A 1 252 ? -1.796  7.424   -2.623  1.00 21.29  ? 252  SER A N     1 
ATOM   1958 C  CA    . SER A 1 252 ? -1.634  8.789   -2.134  1.00 20.73  ? 252  SER A CA    1 
ATOM   1959 C  C     . SER A 1 252 ? -1.066  9.679   -3.228  1.00 20.80  ? 252  SER A C     1 
ATOM   1960 O  O     . SER A 1 252 ? -1.452  10.847  -3.348  1.00 23.84  ? 252  SER A O     1 
ATOM   1961 C  CB    . SER A 1 252 ? -0.746  8.829   -0.887  1.00 21.35  ? 252  SER A CB    1 
ATOM   1962 O  OG    . SER A 1 252 ? 0.567   8.377   -1.146  1.00 20.40  ? 252  SER A OG    1 
ATOM   1963 N  N     . ARG A 1 253 ? -0.165  9.127   -4.044  1.00 24.81  ? 253  ARG A N     1 
ATOM   1964 C  CA    . ARG A 1 253 ? 0.334   9.838   -5.215  1.00 18.80  ? 253  ARG A CA    1 
ATOM   1965 C  C     . ARG A 1 253 ? -0.792  10.107  -6.213  1.00 26.57  ? 253  ARG A C     1 
ATOM   1966 O  O     . ARG A 1 253 ? -0.972  11.242  -6.668  1.00 30.99  ? 253  ARG A O     1 
ATOM   1967 C  CB    . ARG A 1 253 ? 1.469   9.024   -5.843  1.00 29.67  ? 253  ARG A CB    1 
ATOM   1968 C  CG    . ARG A 1 253 ? 1.783   9.328   -7.280  1.00 40.79  ? 253  ARG A CG    1 
ATOM   1969 C  CD    . ARG A 1 253 ? 2.701   10.509  -7.431  1.00 38.25  ? 253  ARG A CD    1 
ATOM   1970 N  NE    . ARG A 1 253 ? 3.280   10.517  -8.770  1.00 44.55  ? 253  ARG A NE    1 
ATOM   1971 C  CZ    . ARG A 1 253 ? 4.572   10.377  -9.041  1.00 42.07  ? 253  ARG A CZ    1 
ATOM   1972 N  NH1   . ARG A 1 253 ? 5.478   10.288  -8.080  1.00 40.18  ? 253  ARG A NH1   1 
ATOM   1973 N  NH2   . ARG A 1 253 ? 4.965   10.333  -10.311 1.00 49.75  ? 253  ARG A NH2   1 
ATOM   1974 N  N     . LEU A 1 254 ? -1.582  9.079   -6.549  1.00 28.20  ? 254  LEU A N     1 
ATOM   1975 C  CA    . LEU A 1 254 ? -2.751  9.297   -7.403  1.00 24.62  ? 254  LEU A CA    1 
ATOM   1976 C  C     . LEU A 1 254 ? -3.684  10.346  -6.810  1.00 26.26  ? 254  LEU A C     1 
ATOM   1977 O  O     . LEU A 1 254 ? -4.223  11.189  -7.535  1.00 30.66  ? 254  LEU A O     1 
ATOM   1978 C  CB    . LEU A 1 254 ? -3.518  7.991   -7.607  1.00 30.58  ? 254  LEU A CB    1 
ATOM   1979 C  CG    . LEU A 1 254 ? -2.810  6.776   -8.203  1.00 36.76  ? 254  LEU A CG    1 
ATOM   1980 C  CD1   . LEU A 1 254 ? -3.793  5.618   -8.288  1.00 31.08  ? 254  LEU A CD1   1 
ATOM   1981 C  CD2   . LEU A 1 254 ? -2.256  7.103   -9.570  1.00 34.82  ? 254  LEU A CD2   1 
ATOM   1982 N  N     . ALA A 1 255 ? -3.898  10.295  -5.489  1.00 27.10  ? 255  ALA A N     1 
ATOM   1983 C  CA    . ALA A 1 255 ? -4.819  11.223  -4.838  1.00 26.38  ? 255  ALA A CA    1 
ATOM   1984 C  C     . ALA A 1 255 ? -4.325  12.656  -4.958  1.00 26.07  ? 255  ALA A C     1 
ATOM   1985 O  O     . ALA A 1 255 ? -5.115  13.583  -5.186  1.00 28.94  ? 255  ALA A O     1 
ATOM   1986 C  CB    . ALA A 1 255 ? -4.992  10.837  -3.364  1.00 26.13  ? 255  ALA A CB    1 
ATOM   1987 N  N     . LYS A 1 256 ? -3.021  12.855  -4.778  1.00 29.77  ? 256  LYS A N     1 
ATOM   1988 C  CA    . LYS A 1 256 ? -2.422  14.160  -5.026  1.00 31.06  ? 256  LYS A CA    1 
ATOM   1989 C  C     . LYS A 1 256 ? -2.687  14.617  -6.456  1.00 28.89  ? 256  LYS A C     1 
ATOM   1990 O  O     . LYS A 1 256 ? -3.101  15.756  -6.680  1.00 35.35  ? 256  LYS A O     1 
ATOM   1991 C  CB    . LYS A 1 256 ? -0.921  14.091  -4.746  1.00 28.50  ? 256  LYS A CB    1 
ATOM   1992 C  CG    . LYS A 1 256 ? -0.159  15.364  -5.095  1.00 34.20  ? 256  LYS A CG    1 
ATOM   1993 C  CD    . LYS A 1 256 ? -0.576  16.514  -4.197  1.00 32.05  ? 256  LYS A CD    1 
ATOM   1994 C  CE    . LYS A 1 256 ? 0.215   17.781  -4.532  1.00 46.24  ? 256  LYS A CE    1 
ATOM   1995 N  NZ    . LYS A 1 256 ? 0.048   18.205  -5.952  1.00 48.36  ? 256  LYS A NZ    1 
ATOM   1996 N  N     . GLU A 1 257 ? -2.489  13.722  -7.432  1.00 32.28  ? 257  GLU A N     1 
ATOM   1997 C  CA    . GLU A 1 257 ? -2.692  14.061  -8.839  1.00 39.47  ? 257  GLU A CA    1 
ATOM   1998 C  C     . GLU A 1 257 ? -4.154  14.362  -9.150  1.00 36.57  ? 257  GLU A C     1 
ATOM   1999 O  O     . GLU A 1 257 ? -4.444  15.229  -9.983  1.00 35.78  ? 257  GLU A O     1 
ATOM   2000 C  CB    . GLU A 1 257 ? -2.215  12.913  -9.744  1.00 35.97  ? 257  GLU A CB    1 
ATOM   2001 C  CG    . GLU A 1 257 ? -0.729  12.563  -9.683  1.00 37.60  ? 257  GLU A CG    1 
ATOM   2002 C  CD    . GLU A 1 257 ? -0.386  11.296  -10.491 1.00 46.73  ? 257  GLU A CD    1 
ATOM   2003 O  OE1   . GLU A 1 257 ? -1.217  10.858  -11.322 1.00 46.76  ? 257  GLU A OE1   1 
ATOM   2004 O  OE2   . GLU A 1 257 ? 0.711   10.727  -10.283 1.00 50.73  ? 257  GLU A OE2   1 
ATOM   2005 N  N     . GLU A 1 258 ? -5.081  13.648  -8.512  1.00 31.68  ? 258  GLU A N     1 
ATOM   2006 C  CA    . GLU A 1 258 ? -6.490  13.679  -8.886  1.00 31.76  ? 258  GLU A CA    1 
ATOM   2007 C  C     . GLU A 1 258 ? -7.372  14.428  -7.893  1.00 33.39  ? 258  GLU A C     1 
ATOM   2008 O  O     . GLU A 1 258 ? -8.578  14.550  -8.132  1.00 40.61  ? 258  GLU A O     1 
ATOM   2009 C  CB    . GLU A 1 258 ? -7.010  12.241  -9.072  1.00 33.63  ? 258  GLU A CB    1 
ATOM   2010 C  CG    . GLU A 1 258 ? -6.297  11.468  -10.172 1.00 35.50  ? 258  GLU A CG    1 
ATOM   2011 C  CD    . GLU A 1 258 ? -6.530  9.968   -10.109 1.00 43.98  ? 258  GLU A CD    1 
ATOM   2012 O  OE1   . GLU A 1 258 ? -7.424  9.515   -9.359  1.00 36.01  ? 258  GLU A OE1   1 
ATOM   2013 O  OE2   . GLU A 1 258 ? -5.805  9.231   -10.814 1.00 48.05  ? 258  GLU A OE2   1 
ATOM   2014 N  N     . GLY A 1 259 ? -6.817  14.936  -6.794  1.00 30.73  ? 259  GLY A N     1 
ATOM   2015 C  CA    . GLY A 1 259 ? -7.578  15.782  -5.893  1.00 27.76  ? 259  GLY A CA    1 
ATOM   2016 C  C     . GLY A 1 259 ? -8.330  15.069  -4.783  1.00 33.21  ? 259  GLY A C     1 
ATOM   2017 O  O     . GLY A 1 259 ? -9.399  15.536  -4.371  1.00 33.80  ? 259  GLY A O     1 
ATOM   2018 N  N     . TRP A 1 260 ? -7.812  13.959  -4.275  1.00 28.13  ? 260  TRP A N     1 
ATOM   2019 C  CA    . TRP A 1 260 ? -8.445  13.275  -3.150  1.00 26.98  ? 260  TRP A CA    1 
ATOM   2020 C  C     . TRP A 1 260 ? -7.364  12.912  -2.132  1.00 23.11  ? 260  TRP A C     1 
ATOM   2021 O  O     . TRP A 1 260 ? -6.257  13.464  -2.130  1.00 23.19  ? 260  TRP A O     1 
ATOM   2022 C  CB    . TRP A 1 260 ? -9.285  12.085  -3.643  1.00 28.85  ? 260  TRP A CB    1 
ATOM   2023 C  CG    . TRP A 1 260 ? -8.638  11.086  -4.606  1.00 31.15  ? 260  TRP A CG    1 
ATOM   2024 C  CD1   . TRP A 1 260 ? -8.428  11.255  -5.948  1.00 30.25  ? 260  TRP A CD1   1 
ATOM   2025 C  CD2   . TRP A 1 260 ? -8.212  9.742   -4.306  1.00 28.14  ? 260  TRP A CD2   1 
ATOM   2026 N  NE1   . TRP A 1 260 ? -7.864  10.116  -6.489  1.00 25.67  ? 260  TRP A NE1   1 
ATOM   2027 C  CE2   . TRP A 1 260 ? -7.725  9.176   -5.504  1.00 30.09  ? 260  TRP A CE2   1 
ATOM   2028 C  CE3   . TRP A 1 260 ? -8.182  8.970   -3.139  1.00 25.28  ? 260  TRP A CE3   1 
ATOM   2029 C  CZ2   . TRP A 1 260 ? -7.207  7.876   -5.567  1.00 28.44  ? 260  TRP A CZ2   1 
ATOM   2030 C  CZ3   . TRP A 1 260 ? -7.668  7.679   -3.207  1.00 25.04  ? 260  TRP A CZ3   1 
ATOM   2031 C  CH2   . TRP A 1 260 ? -7.183  7.150   -4.412  1.00 26.04  ? 260  TRP A CH2   1 
ATOM   2032 N  N     . LEU A 1 261 ? -7.690  12.003  -1.215  1.00 21.40  ? 261  LEU A N     1 
ATOM   2033 C  CA    . LEU A 1 261 ? -6.802  11.658  -0.112  1.00 18.75  ? 261  LEU A CA    1 
ATOM   2034 C  C     . LEU A 1 261 ? -6.848  10.161  0.148   1.00 24.12  ? 261  LEU A C     1 
ATOM   2035 O  O     . LEU A 1 261 ? -7.927  9.560   0.163   1.00 23.05  ? 261  LEU A O     1 
ATOM   2036 C  CB    . LEU A 1 261 ? -7.197  12.406  1.178   1.00 19.60  ? 261  LEU A CB    1 
ATOM   2037 C  CG    . LEU A 1 261 ? -7.273  13.935  1.193   1.00 24.36  ? 261  LEU A CG    1 
ATOM   2038 C  CD1   . LEU A 1 261 ? -7.989  14.429  2.447   1.00 24.59  ? 261  LEU A CD1   1 
ATOM   2039 C  CD2   . LEU A 1 261 ? -5.869  14.545  1.112   1.00 24.76  ? 261  LEU A CD2   1 
ATOM   2040 N  N     . ALA A 1 262 ? -5.678  9.562   0.371   1.00 20.47  ? 262  ALA A N     1 
ATOM   2041 C  CA    . ALA A 1 262 ? -5.571  8.165   0.762   1.00 17.90  ? 262  ALA A CA    1 
ATOM   2042 C  C     . ALA A 1 262 ? -4.795  8.116   2.064   1.00 22.72  ? 262  ALA A C     1 
ATOM   2043 O  O     . ALA A 1 262 ? -3.627  8.511   2.098   1.00 16.92  ? 262  ALA A O     1 
ATOM   2044 C  CB    . ALA A 1 262 ? -4.872  7.331   -0.319  1.00 20.93  ? 262  ALA A CB    1 
ATOM   2045 N  N     . GLU A 1 263 ? -5.428  7.620   3.128   1.00 19.25  ? 263  GLU A N     1 
ATOM   2046 C  CA    . GLU A 1 263 ? -4.909  7.836   4.472   1.00 19.61  ? 263  GLU A CA    1 
ATOM   2047 C  C     . GLU A 1 263 ? -4.978  6.567   5.307   1.00 21.42  ? 263  GLU A C     1 
ATOM   2048 O  O     . GLU A 1 263 ? -5.827  5.698   5.090   1.00 19.52  ? 263  GLU A O     1 
ATOM   2049 C  CB    . GLU A 1 263 ? -5.687  8.964   5.191   1.00 16.94  ? 263  GLU A CB    1 
ATOM   2050 C  CG    . GLU A 1 263 ? -5.716  10.299  4.422   1.00 16.77  ? 263  GLU A CG    1 
ATOM   2051 C  CD    . GLU A 1 263 ? -4.349  10.966  4.337   1.00 19.07  ? 263  GLU A CD    1 
ATOM   2052 O  OE1   . GLU A 1 263 ? -3.449  10.626  5.144   1.00 18.01  ? 263  GLU A OE1   1 
ATOM   2053 O  OE2   . GLU A 1 263 ? -4.173  11.838  3.459   1.00 21.53  ? 263  GLU A OE2   1 
ATOM   2054 N  N     . HIS A 1 264 ? -4.072  6.491   6.287   1.00 15.12  ? 264  HIS A N     1 
ATOM   2055 C  CA    . HIS A 1 264 ? -3.987  5.398   7.252   1.00 19.73  ? 264  HIS A CA    1 
ATOM   2056 C  C     . HIS A 1 264 ? -5.001  5.615   8.382   1.00 19.90  ? 264  HIS A C     1 
ATOM   2057 O  O     . HIS A 1 264 ? -4.644  5.844   9.537   1.00 14.71  ? 264  HIS A O     1 
ATOM   2058 C  CB    . HIS A 1 264 ? -2.575  5.338   7.813   1.00 15.61  ? 264  HIS A CB    1 
ATOM   2059 C  CG    . HIS A 1 264 ? -2.273  4.084   8.566   1.00 14.71  ? 264  HIS A CG    1 
ATOM   2060 N  ND1   . HIS A 1 264 ? -1.217  3.985   9.444   1.00 15.60  ? 264  HIS A ND1   1 
ATOM   2061 C  CD2   . HIS A 1 264 ? -2.875  2.865   8.558   1.00 13.71  ? 264  HIS A CD2   1 
ATOM   2062 C  CE1   . HIS A 1 264 ? -1.169  2.756   9.936   1.00 20.21  ? 264  HIS A CE1   1 
ATOM   2063 N  NE2   . HIS A 1 264 ? -2.172  2.061   9.425   1.00 12.05  ? 264  HIS A NE2   1 
ATOM   2064 N  N     . MET A 1 265 ? -6.286  5.540   8.035   1.00 16.39  ? 265  MET A N     1 
ATOM   2065 C  CA    . MET A 1 265 ? -7.339  5.920   8.965   1.00 15.79  ? 265  MET A CA    1 
ATOM   2066 C  C     . MET A 1 265 ? -8.433  4.868   9.035   1.00 20.05  ? 265  MET A C     1 
ATOM   2067 O  O     . MET A 1 265 ? -8.846  4.329   8.004   1.00 19.87  ? 265  MET A O     1 
ATOM   2068 C  CB    . MET A 1 265 ? -8.001  7.242   8.568   1.00 17.31  ? 265  MET A CB    1 
ATOM   2069 C  CG    . MET A 1 265 ? -7.084  8.450   8.634   1.00 18.73  ? 265  MET A CG    1 
ATOM   2070 S  SD    . MET A 1 265 ? -7.977  9.887   8.065   1.00 21.19  ? 265  MET A SD    1 
ATOM   2071 C  CE    . MET A 1 265 ? -6.705  11.134  8.342   1.00 23.65  ? 265  MET A CE    1 
ATOM   2072 N  N     . LEU A 1 266 ? -8.934  4.627   10.249  1.00 17.20  ? 266  LEU A N     1 
ATOM   2073 C  CA    . LEU A 1 266 ? -10.224 3.966   10.418  1.00 17.88  ? 266  LEU A CA    1 
ATOM   2074 C  C     . LEU A 1 266 ? -11.372 4.918   10.071  1.00 22.62  ? 266  LEU A C     1 
ATOM   2075 O  O     . LEU A 1 266 ? -11.239 6.152   10.097  1.00 19.36  ? 266  LEU A O     1 
ATOM   2076 C  CB    . LEU A 1 266 ? -10.391 3.464   11.853  1.00 17.38  ? 266  LEU A CB    1 
ATOM   2077 C  CG    . LEU A 1 266 ? -10.543 4.540   12.948  1.00 21.35  ? 266  LEU A CG    1 
ATOM   2078 C  CD1   . LEU A 1 266 ? -11.999 4.848   13.238  1.00 22.09  ? 266  LEU A CD1   1 
ATOM   2079 C  CD2   . LEU A 1 266 ? -9.826  4.145   14.231  1.00 18.49  ? 266  LEU A CD2   1 
ATOM   2080 N  N     . ILE A 1 267 ? -12.525 4.329   9.763   1.00 15.35  ? 267  ILE A N     1 
ATOM   2081 C  CA    . ILE A 1 267 ? -13.766 5.075   9.583   1.00 17.15  ? 267  ILE A CA    1 
ATOM   2082 C  C     . ILE A 1 267 ? -14.834 4.421   10.455  1.00 20.82  ? 267  ILE A C     1 
ATOM   2083 O  O     . ILE A 1 267 ? -15.053 3.205   10.369  1.00 18.90  ? 267  ILE A O     1 
ATOM   2084 C  CB    . ILE A 1 267 ? -14.225 5.109   8.114   1.00 16.55  ? 267  ILE A CB    1 
ATOM   2085 C  CG1   . ILE A 1 267 ? -13.119 5.655   7.198   1.00 21.58  ? 267  ILE A CG1   1 
ATOM   2086 C  CG2   . ILE A 1 267 ? -15.453 5.977   7.969   1.00 22.24  ? 267  ILE A CG2   1 
ATOM   2087 C  CD1   . ILE A 1 267 ? -13.342 5.289   5.746   1.00 18.87  ? 267  ILE A CD1   1 
ATOM   2088 N  N     . LEU A 1 268 ? -15.491 5.215   11.291  1.00 15.75  ? 268  LEU A N     1 
ATOM   2089 C  CA    . LEU A 1 268 ? -16.555 4.674   12.127  1.00 17.46  ? 268  LEU A CA    1 
ATOM   2090 C  C     . LEU A 1 268 ? -17.748 5.614   12.086  1.00 24.40  ? 268  LEU A C     1 
ATOM   2091 O  O     . LEU A 1 268 ? -17.608 6.821   11.849  1.00 17.89  ? 268  LEU A O     1 
ATOM   2092 C  CB    . LEU A 1 268 ? -16.093 4.448   13.586  1.00 16.72  ? 268  LEU A CB    1 
ATOM   2093 C  CG    . LEU A 1 268 ? -15.588 5.630   14.433  1.00 23.43  ? 268  LEU A CG    1 
ATOM   2094 C  CD1   . LEU A 1 268 ? -16.729 6.512   14.941  1.00 25.85  ? 268  LEU A CD1   1 
ATOM   2095 C  CD2   . LEU A 1 268 ? -14.773 5.119   15.617  1.00 20.99  ? 268  LEU A CD2   1 
ATOM   2096 N  N     . GLY A 1 269 ? -18.923 5.048   12.323  1.00 19.29  ? 269  GLY A N     1 
ATOM   2097 C  CA    . GLY A 1 269 ? -20.143 5.814   12.468  1.00 18.43  ? 269  GLY A CA    1 
ATOM   2098 C  C     . GLY A 1 269 ? -20.578 5.661   13.913  1.00 20.95  ? 269  GLY A C     1 
ATOM   2099 O  O     . GLY A 1 269 ? -20.543 4.560   14.456  1.00 20.60  ? 269  GLY A O     1 
ATOM   2100 N  N     . ILE A 1 270 ? -20.962 6.766   14.529  1.00 20.42  ? 270  ILE A N     1 
ATOM   2101 C  CA    . ILE A 1 270 ? -21.374 6.756   15.924  1.00 22.21  ? 270  ILE A CA    1 
ATOM   2102 C  C     . ILE A 1 270 ? -22.737 7.431   16.034  1.00 21.27  ? 270  ILE A C     1 
ATOM   2103 O  O     . ILE A 1 270 ? -22.941 8.523   15.497  1.00 22.31  ? 270  ILE A O     1 
ATOM   2104 C  CB    . ILE A 1 270 ? -20.321 7.437   16.822  1.00 20.89  ? 270  ILE A CB    1 
ATOM   2105 C  CG1   . ILE A 1 270 ? -20.808 7.486   18.270  1.00 24.61  ? 270  ILE A CG1   1 
ATOM   2106 C  CG2   . ILE A 1 270 ? -19.962 8.829   16.292  1.00 26.92  ? 270  ILE A CG2   1 
ATOM   2107 C  CD1   . ILE A 1 270 ? -19.699 7.640   19.281  1.00 30.06  ? 270  ILE A CD1   1 
ATOM   2108 N  N     . THR A 1 271 ? -23.672 6.770   16.708  1.00 24.27  ? 271  THR A N     1 
ATOM   2109 C  CA    . THR A 1 271 ? -25.040 7.255   16.863  1.00 22.89  ? 271  THR A CA    1 
ATOM   2110 C  C     . THR A 1 271 ? -25.281 7.550   18.333  1.00 24.90  ? 271  THR A C     1 
ATOM   2111 O  O     . THR A 1 271 ? -24.866 6.776   19.194  1.00 19.63  ? 271  THR A O     1 
ATOM   2112 C  CB    . THR A 1 271 ? -26.058 6.210   16.370  1.00 24.26  ? 271  THR A CB    1 
ATOM   2113 O  OG1   . THR A 1 271 ? -25.791 5.892   15.003  1.00 23.22  ? 271  THR A OG1   1 
ATOM   2114 C  CG2   . THR A 1 271 ? -27.486 6.738   16.489  1.00 25.97  ? 271  THR A CG2   1 
ATOM   2115 N  N     . ASN A 1 272 ? -25.935 8.668   18.626  1.00 23.17  ? 272  ASN A N     1 
ATOM   2116 C  CA    . ASN A 1 272 ? -26.106 9.087   20.003  1.00 20.94  ? 272  ASN A CA    1 
ATOM   2117 C  C     . ASN A 1 272 ? -27.512 8.753   20.477  1.00 22.96  ? 272  ASN A C     1 
ATOM   2118 O  O     . ASN A 1 272 ? -28.347 8.273   19.702  1.00 23.07  ? 272  ASN A O     1 
ATOM   2119 C  CB    . ASN A 1 272 ? -25.772 10.591  20.144  1.00 22.60  ? 272  ASN A CB    1 
ATOM   2120 C  CG    . ASN A 1 272 ? -26.883 11.532  19.659  1.00 23.20  ? 272  ASN A CG    1 
ATOM   2121 O  OD1   . ASN A 1 272 ? -27.814 11.146  18.959  1.00 20.44  ? 272  ASN A OD1   1 
ATOM   2122 N  ND2   . ASN A 1 272 ? -26.742 12.810  20.007  1.00 28.34  ? 272  ASN A ND2   1 
ATOM   2123 N  N     . PRO A 1 273 ? -27.810 8.942   21.769  1.00 23.67  ? 273  PRO A N     1 
ATOM   2124 C  CA    . PRO A 1 273 ? -29.151 8.568   22.257  1.00 23.72  ? 273  PRO A CA    1 
ATOM   2125 C  C     . PRO A 1 273 ? -30.282 9.432   21.709  1.00 26.63  ? 273  PRO A C     1 
ATOM   2126 O  O     . PRO A 1 273 ? -31.449 9.067   21.901  1.00 26.87  ? 273  PRO A O     1 
ATOM   2127 C  CB    . PRO A 1 273 ? -29.029 8.714   23.781  1.00 23.97  ? 273  PRO A CB    1 
ATOM   2128 C  CG    . PRO A 1 273 ? -27.577 8.596   24.071  1.00 25.30  ? 273  PRO A CG    1 
ATOM   2129 C  CD    . PRO A 1 273 ? -26.892 9.235   22.888  1.00 22.91  ? 273  PRO A CD    1 
ATOM   2130 N  N     . GLU A 1 274 ? -29.991 10.552  21.044  1.00 23.15  ? 274  GLU A N     1 
ATOM   2131 C  CA    . GLU A 1 274 ? -31.017 11.364  20.393  1.00 24.24  ? 274  GLU A CA    1 
ATOM   2132 C  C     . GLU A 1 274 ? -31.251 10.969  18.941  1.00 26.55  ? 274  GLU A C     1 
ATOM   2133 O  O     . GLU A 1 274 ? -31.910 11.715  18.208  1.00 23.90  ? 274  GLU A O     1 
ATOM   2134 C  CB    . GLU A 1 274 ? -30.647 12.854  20.435  1.00 23.45  ? 274  GLU A CB    1 
ATOM   2135 C  CG    . GLU A 1 274 ? -30.343 13.410  21.812  1.00 27.89  ? 274  GLU A CG    1 
ATOM   2136 C  CD    . GLU A 1 274 ? -31.555 13.445  22.733  1.00 35.98  ? 274  GLU A CD    1 
ATOM   2137 O  OE1   . GLU A 1 274 ? -32.716 13.417  22.244  1.00 30.65  ? 274  GLU A OE1   1 
ATOM   2138 O  OE2   . GLU A 1 274 ? -31.334 13.504  23.959  1.00 38.11  ? 274  GLU A OE2   1 
ATOM   2139 N  N     . GLY A 1 275 ? -30.707 9.837   18.499  1.00 25.44  ? 275  GLY A N     1 
ATOM   2140 C  CA    . GLY A 1 275 ? -30.935 9.393   17.139  1.00 23.49  ? 275  GLY A CA    1 
ATOM   2141 C  C     . GLY A 1 275 ? -30.180 10.148  16.064  1.00 25.89  ? 275  GLY A C     1 
ATOM   2142 O  O     . GLY A 1 275 ? -30.617 10.149  14.909  1.00 26.67  ? 275  GLY A O     1 
ATOM   2143 N  N     . LYS A 1 276 ? -29.077 10.815  16.404  1.00 22.69  ? 276  LYS A N     1 
ATOM   2144 C  CA    . LYS A 1 276 ? -28.223 11.456  15.404  1.00 24.03  ? 276  LYS A CA    1 
ATOM   2145 C  C     . LYS A 1 276 ? -26.980 10.595  15.200  1.00 22.09  ? 276  LYS A C     1 
ATOM   2146 O  O     . LYS A 1 276 ? -26.458 10.012  16.154  1.00 22.70  ? 276  LYS A O     1 
ATOM   2147 C  CB    . LYS A 1 276 ? -27.812 12.873  15.823  1.00 28.68  ? 276  LYS A CB    1 
ATOM   2148 C  CG    . LYS A 1 276 ? -28.927 13.742  16.459  1.00 30.67  ? 276  LYS A CG    1 
ATOM   2149 C  CD    . LYS A 1 276 ? -30.005 14.178  15.465  1.00 27.54  ? 276  LYS A CD    1 
ATOM   2150 C  CE    . LYS A 1 276 ? -30.947 15.237  16.074  1.00 25.63  ? 276  LYS A CE    1 
ATOM   2151 N  NZ    . LYS A 1 276 ? -31.669 14.786  17.326  1.00 24.23  ? 276  LYS A NZ    1 
ATOM   2152 N  N     . LYS A 1 277 ? -26.506 10.524  13.961  1.00 20.14  ? 277  LYS A N     1 
ATOM   2153 C  CA    . LYS A 1 277 ? -25.349 9.705   13.615  1.00 21.39  ? 277  LYS A CA    1 
ATOM   2154 C  C     . LYS A 1 277 ? -24.325 10.558  12.876  1.00 24.17  ? 277  LYS A C     1 
ATOM   2155 O  O     . LYS A 1 277 ? -24.686 11.303  11.960  1.00 23.70  ? 277  LYS A O     1 
ATOM   2156 C  CB    . LYS A 1 277 ? -25.761 8.514   12.750  1.00 23.24  ? 277  LYS A CB    1 
ATOM   2157 C  CG    . LYS A 1 277 ? -24.585 7.638   12.314  1.00 22.63  ? 277  LYS A CG    1 
ATOM   2158 C  CD    . LYS A 1 277 ? -25.075 6.395   11.608  1.00 24.28  ? 277  LYS A CD    1 
ATOM   2159 C  CE    . LYS A 1 277 ? -23.904 5.492   11.223  1.00 25.23  ? 277  LYS A CE    1 
ATOM   2160 N  NZ    . LYS A 1 277 ? -24.404 4.171   10.742  1.00 21.80  ? 277  LYS A NZ    1 
ATOM   2161 N  N     . LYS A 1 278 ? -23.058 10.460  13.288  1.00 18.32  ? 278  LYS A N     1 
ATOM   2162 C  CA    . LYS A 1 278 ? -21.952 11.116  12.594  1.00 21.55  ? 278  LYS A CA    1 
ATOM   2163 C  C     . LYS A 1 278 ? -20.855 10.100  12.282  1.00 21.21  ? 278  LYS A C     1 
ATOM   2164 O  O     . LYS A 1 278 ? -20.724 9.079   12.953  1.00 20.19  ? 278  LYS A O     1 
ATOM   2165 C  CB    . LYS A 1 278 ? -21.380 12.259  13.431  1.00 22.25  ? 278  LYS A CB    1 
ATOM   2166 C  CG    . LYS A 1 278 ? -22.395 13.351  13.707  1.00 21.30  ? 278  LYS A CG    1 
ATOM   2167 C  CD    . LYS A 1 278 ? -21.780 14.527  14.453  1.00 27.48  ? 278  LYS A CD    1 
ATOM   2168 C  CE    . LYS A 1 278 ? -22.832 15.598  14.742  1.00 23.13  ? 278  LYS A CE    1 
ATOM   2169 N  NZ    . LYS A 1 278 ? -23.502 16.042  13.482  1.00 27.31  ? 278  LYS A NZ    1 
ATOM   2170 N  N     . TYR A 1 279 ? -20.054 10.393  11.261  1.00 20.36  ? 279  TYR A N     1 
ATOM   2171 C  CA    . TYR A 1 279 ? -18.908 9.565   10.911  1.00 18.42  ? 279  TYR A CA    1 
ATOM   2172 C  C     . TYR A 1 279 ? -17.621 10.309  11.227  1.00 19.73  ? 279  TYR A C     1 
ATOM   2173 O  O     . TYR A 1 279 ? -17.506 11.505  10.952  1.00 19.92  ? 279  TYR A O     1 
ATOM   2174 C  CB    . TYR A 1 279 ? -18.925 9.177   9.436   1.00 18.75  ? 279  TYR A CB    1 
ATOM   2175 C  CG    . TYR A 1 279 ? -19.997 8.186   9.068   1.00 24.31  ? 279  TYR A CG    1 
ATOM   2176 C  CD1   . TYR A 1 279 ? -21.270 8.617   8.713   1.00 25.50  ? 279  TYR A CD1   1 
ATOM   2177 C  CD2   . TYR A 1 279 ? -19.739 6.817   9.066   1.00 18.95  ? 279  TYR A CD2   1 
ATOM   2178 C  CE1   . TYR A 1 279 ? -22.259 7.721   8.362   1.00 26.48  ? 279  TYR A CE1   1 
ATOM   2179 C  CE2   . TYR A 1 279 ? -20.731 5.909   8.726   1.00 21.80  ? 279  TYR A CE2   1 
ATOM   2180 C  CZ    . TYR A 1 279 ? -21.988 6.371   8.364   1.00 25.37  ? 279  TYR A CZ    1 
ATOM   2181 O  OH    . TYR A 1 279 ? -22.986 5.489   8.005   1.00 25.26  ? 279  TYR A OH    1 
ATOM   2182 N  N     . LEU A 1 280 ? -16.662 9.588   11.799  1.00 20.02  ? 280  LEU A N     1 
ATOM   2183 C  CA    . LEU A 1 280 ? -15.351 10.104  12.162  1.00 18.37  ? 280  LEU A CA    1 
ATOM   2184 C  C     . LEU A 1 280 ? -14.283 9.210   11.549  1.00 17.88  ? 280  LEU A C     1 
ATOM   2185 O  O     . LEU A 1 280 ? -14.467 7.998   11.432  1.00 18.94  ? 280  LEU A O     1 
ATOM   2186 C  CB    . LEU A 1 280 ? -15.145 10.118  13.678  1.00 18.41  ? 280  LEU A CB    1 
ATOM   2187 C  CG    . LEU A 1 280 ? -16.257 10.657  14.583  1.00 28.29  ? 280  LEU A CG    1 
ATOM   2188 C  CD1   . LEU A 1 280 ? -15.980 10.261  16.027  1.00 26.81  ? 280  LEU A CD1   1 
ATOM   2189 C  CD2   . LEU A 1 280 ? -16.330 12.153  14.453  1.00 29.19  ? 280  LEU A CD2   1 
ATOM   2190 N  N     . ALA A 1 281 ? -13.152 9.809   11.182  1.00 19.42  ? 281  ALA A N     1 
ATOM   2191 C  CA    . ALA A 1 281 ? -11.972 9.070   10.773  1.00 17.39  ? 281  ALA A CA    1 
ATOM   2192 C  C     . ALA A 1 281 ? -10.863 9.305   11.793  1.00 21.35  ? 281  ALA A C     1 
ATOM   2193 O  O     . ALA A 1 281 ? -10.802 10.362  12.421  1.00 19.64  ? 281  ALA A O     1 
ATOM   2194 C  CB    . ALA A 1 281 ? -11.513 9.481   9.368   1.00 17.99  ? 281  ALA A CB    1 
ATOM   2195 N  N     . ALA A 1 282 ? -9.993  8.310   11.974  1.00 15.41  ? 282  ALA A N     1 
ATOM   2196 C  CA    . ALA A 1 282 ? -8.920  8.424   12.965  1.00 19.25  ? 282  ALA A CA    1 
ATOM   2197 C  C     . ALA A 1 282 ? -7.632  7.826   12.421  1.00 22.34  ? 282  ALA A C     1 
ATOM   2198 O  O     . ALA A 1 282 ? -7.606  6.653   12.032  1.00 17.10  ? 282  ALA A O     1 
ATOM   2199 C  CB    . ALA A 1 282 ? -9.290  7.724   14.279  1.00 15.89  ? 282  ALA A CB    1 
ATOM   2200 N  N     . ALA A 1 283 ? -6.554  8.613   12.436  1.00 16.58  ? 283  ALA A N     1 
ATOM   2201 C  CA    . ALA A 1 283 ? -5.236  8.143   12.018  1.00 17.48  ? 283  ALA A CA    1 
ATOM   2202 C  C     . ALA A 1 283 ? -4.374  7.901   13.253  1.00 16.02  ? 283  ALA A C     1 
ATOM   2203 O  O     . ALA A 1 283 ? -3.935  8.851   13.908  1.00 16.14  ? 283  ALA A O     1 
ATOM   2204 C  CB    . ALA A 1 283 ? -4.576  9.155   11.080  1.00 18.94  ? 283  ALA A CB    1 
ATOM   2205 N  N     . PHE A 1 284 ? -4.149  6.636   13.584  1.00 15.72  ? 284  PHE A N     1 
ATOM   2206 C  CA    . PHE A 1 284 ? -3.189  6.253   14.597  1.00 12.33  ? 284  PHE A CA    1 
ATOM   2207 C  C     . PHE A 1 284 ? -2.124  5.421   13.911  1.00 17.36  ? 284  PHE A C     1 
ATOM   2208 O  O     . PHE A 1 284 ? -2.428  4.772   12.906  1.00 18.36  ? 284  PHE A O     1 
ATOM   2209 C  CB    . PHE A 1 284 ? -3.814  5.405   15.716  1.00 14.74  ? 284  PHE A CB    1 
ATOM   2210 C  CG    . PHE A 1 284 ? -5.031  6.008   16.351  1.00 17.98  ? 284  PHE A CG    1 
ATOM   2211 C  CD1   . PHE A 1 284 ? -5.123  7.373   16.552  1.00 17.52  ? 284  PHE A CD1   1 
ATOM   2212 C  CD2   . PHE A 1 284 ? -6.082  5.189   16.765  1.00 20.67  ? 284  PHE A CD2   1 
ATOM   2213 C  CE1   . PHE A 1 284 ? -6.237  7.931   17.149  1.00 17.61  ? 284  PHE A CE1   1 
ATOM   2214 C  CE2   . PHE A 1 284 ? -7.213  5.736   17.366  1.00 23.07  ? 284  PHE A CE2   1 
ATOM   2215 C  CZ    . PHE A 1 284 ? -7.290  7.098   17.559  1.00 18.32  ? 284  PHE A CZ    1 
ATOM   2216 N  N     . PRO A 1 285 ? -0.892  5.387   14.426  1.00 17.83  ? 285  PRO A N     1 
ATOM   2217 C  CA    . PRO A 1 285 ? 0.144   4.553   13.801  1.00 19.53  ? 285  PRO A CA    1 
ATOM   2218 C  C     . PRO A 1 285 ? -0.197  3.085   13.977  1.00 25.54  ? 285  PRO A C     1 
ATOM   2219 O  O     . PRO A 1 285 ? -1.124  2.712   14.696  1.00 18.57  ? 285  PRO A O     1 
ATOM   2220 C  CB    . PRO A 1 285 ? 1.424   4.929   14.557  1.00 17.88  ? 285  PRO A CB    1 
ATOM   2221 C  CG    . PRO A 1 285 ? 1.104   6.306   15.166  1.00 20.82  ? 285  PRO A CG    1 
ATOM   2222 C  CD    . PRO A 1 285 ? -0.343  6.193   15.530  1.00 22.79  ? 285  PRO A CD    1 
ATOM   2223 N  N     A SER A 1 286 ? 0.572   2.238   13.299  0.62 22.45  ? 286  SER A N     1 
ATOM   2224 N  N     B SER A 1 286 ? 0.572   2.237   13.301  0.38 22.42  ? 286  SER A N     1 
ATOM   2225 C  CA    A SER A 1 286 ? 0.382   0.804   13.459  0.62 22.59  ? 286  SER A CA    1 
ATOM   2226 C  CA    B SER A 1 286 ? 0.370   0.806   13.462  0.38 22.27  ? 286  SER A CA    1 
ATOM   2227 C  C     A SER A 1 286 ? 0.553   0.420   14.924  0.62 22.01  ? 286  SER A C     1 
ATOM   2228 C  C     B SER A 1 286 ? 0.555   0.415   14.922  0.38 21.92  ? 286  SER A C     1 
ATOM   2229 O  O     A SER A 1 286 ? 1.396   0.973   15.634  0.62 24.39  ? 286  SER A O     1 
ATOM   2230 O  O     B SER A 1 286 ? 1.413   0.956   15.623  0.38 24.40  ? 286  SER A O     1 
ATOM   2231 C  CB    A SER A 1 286 ? 1.377   0.039   12.579  0.62 23.48  ? 286  SER A CB    1 
ATOM   2232 C  CB    B SER A 1 286 ? 1.338   0.023   12.576  0.38 23.49  ? 286  SER A CB    1 
ATOM   2233 O  OG    A SER A 1 286 ? 1.632   0.751   11.376  0.62 22.45  ? 286  SER A OG    1 
ATOM   2234 O  OG    B SER A 1 286 ? 1.025   -1.354  12.609  0.38 23.77  ? 286  SER A OG    1 
ATOM   2235 N  N     . ALA A 1 287 ? -0.279  -0.521  15.381  1.00 25.60  ? 287  ALA A N     1 
ATOM   2236 C  CA    . ALA A 1 287 ? -0.253  -1.016  16.760  1.00 24.83  ? 287  ALA A CA    1 
ATOM   2237 C  C     . ALA A 1 287 ? -0.629  0.060   17.783  1.00 27.45  ? 287  ALA A C     1 
ATOM   2238 O  O     . ALA A 1 287 ? -0.226  -0.006  18.949  1.00 32.25  ? 287  ALA A O     1 
ATOM   2239 C  CB    . ALA A 1 287 ? 1.094   -1.656  17.119  1.00 32.31  ? 287  ALA A CB    1 
ATOM   2240 N  N     . CYS A 1 288 ? -1.432  1.046   17.386  1.00 24.35  ? 288  CYS A N     1 
ATOM   2241 C  CA    . CYS A 1 288 ? -1.846  2.091   18.319  1.00 23.85  ? 288  CYS A CA    1 
ATOM   2242 C  C     . CYS A 1 288 ? -3.361  2.197   18.491  1.00 23.89  ? 288  CYS A C     1 
ATOM   2243 O  O     . CYS A 1 288 ? -3.838  3.174   19.087  1.00 20.99  ? 288  CYS A O     1 
ATOM   2244 C  CB    . CYS A 1 288 ? -1.237  3.432   17.894  1.00 22.31  ? 288  CYS A CB    1 
ATOM   2245 S  SG    . CYS A 1 288 ? 0.569   3.411   18.156  1.00 26.49  ? 288  CYS A SG    1 
ATOM   2246 N  N     . GLY A 1 289 ? -4.132  1.227   18.009  1.00 19.84  ? 289  GLY A N     1 
ATOM   2247 C  CA    . GLY A 1 289 ? -5.508  1.089   18.438  1.00 19.78  ? 289  GLY A CA    1 
ATOM   2248 C  C     . GLY A 1 289 ? -6.619  1.402   17.450  1.00 22.12  ? 289  GLY A C     1 
ATOM   2249 O  O     . GLY A 1 289 ? -7.768  1.551   17.882  1.00 23.18  ? 289  GLY A O     1 
ATOM   2250 N  N     . LYS A 1 290 ? -6.332  1.481   16.151  1.00 19.85  ? 290  LYS A N     1 
ATOM   2251 C  CA    . LYS A 1 290 ? -7.394  1.806   15.197  1.00 19.95  ? 290  LYS A CA    1 
ATOM   2252 C  C     . LYS A 1 290 ? -8.482  0.727   15.180  1.00 19.56  ? 290  LYS A C     1 
ATOM   2253 O  O     . LYS A 1 290 ? -9.682  1.028   15.215  1.00 19.81  ? 290  LYS A O     1 
ATOM   2254 C  CB    . LYS A 1 290 ? -6.808  1.999   13.797  1.00 20.46  ? 290  LYS A CB    1 
ATOM   2255 C  CG    . LYS A 1 290 ? -5.977  3.276   13.604  1.00 15.95  ? 290  LYS A CG    1 
ATOM   2256 C  CD    . LYS A 1 290 ? -5.550  3.451   12.144  1.00 17.35  ? 290  LYS A CD    1 
ATOM   2257 C  CE    . LYS A 1 290 ? -4.789  2.225   11.621  1.00 16.34  ? 290  LYS A CE    1 
ATOM   2258 N  NZ    . LYS A 1 290 ? -3.495  2.018   12.326  1.00 17.63  ? 290  LYS A NZ    1 
ATOM   2259 N  N     . THR A 1 291 ? -8.081  -0.541  15.103  1.00 20.66  ? 291  THR A N     1 
ATOM   2260 C  CA    . THR A 1 291 ? -9.080  -1.604  15.031  1.00 18.90  ? 291  THR A CA    1 
ATOM   2261 C  C     . THR A 1 291 ? -9.906  -1.677  16.309  1.00 18.41  ? 291  THR A C     1 
ATOM   2262 O  O     . THR A 1 291 ? -11.114 -1.943  16.259  1.00 18.06  ? 291  THR A O     1 
ATOM   2263 C  CB    . THR A 1 291 ? -8.422  -2.948  14.745  1.00 18.87  ? 291  THR A CB    1 
ATOM   2264 O  OG1   . THR A 1 291 ? -7.794  -2.900  13.460  1.00 17.85  ? 291  THR A OG1   1 
ATOM   2265 C  CG2   . THR A 1 291 ? -9.494  -4.059  14.718  1.00 18.18  ? 291  THR A CG2   1 
ATOM   2266 N  N     . ASN A 1 292 ? -9.272  -1.468  17.463  1.00 19.02  ? 292  ASN A N     1 
ATOM   2267 C  CA    . ASN A 1 292 ? -10.011 -1.466  18.720  1.00 19.36  ? 292  ASN A CA    1 
ATOM   2268 C  C     . ASN A 1 292 ? -11.035 -0.336  18.777  1.00 20.34  ? 292  ASN A C     1 
ATOM   2269 O  O     . ASN A 1 292 ? -12.101 -0.488  19.382  1.00 18.45  ? 292  ASN A O     1 
ATOM   2270 C  CB    . ASN A 1 292 ? -9.036  -1.346  19.886  1.00 27.34  ? 292  ASN A CB    1 
ATOM   2271 C  CG    . ASN A 1 292 ? -8.294  -2.634  20.133  1.00 31.29  ? 292  ASN A CG    1 
ATOM   2272 O  OD1   . ASN A 1 292 ? -8.708  -3.446  20.959  1.00 31.85  ? 292  ASN A OD1   1 
ATOM   2273 N  ND2   . ASN A 1 292 ? -7.220  -2.852  19.389  1.00 29.65  ? 292  ASN A ND2   1 
ATOM   2274 N  N     . LEU A 1 293 ? -10.718 0.812   18.177  1.00 17.73  ? 293  LEU A N     1 
ATOM   2275 C  CA    . LEU A 1 293 ? -11.653 1.935   18.210  1.00 20.16  ? 293  LEU A CA    1 
ATOM   2276 C  C     . LEU A 1 293 ? -12.759 1.754   17.176  1.00 21.68  ? 293  LEU A C     1 
ATOM   2277 O  O     . LEU A 1 293 ? -13.927 2.049   17.452  1.00 18.62  ? 293  LEU A O     1 
ATOM   2278 C  CB    . LEU A 1 293 ? -10.905 3.251   17.972  1.00 16.36  ? 293  LEU A CB    1 
ATOM   2279 C  CG    . LEU A 1 293 ? -11.710 4.552   18.169  1.00 18.53  ? 293  LEU A CG    1 
ATOM   2280 C  CD1   . LEU A 1 293 ? -12.098 4.707   19.619  1.00 18.80  ? 293  LEU A CD1   1 
ATOM   2281 C  CD2   . LEU A 1 293 ? -10.920 5.762   17.719  1.00 16.77  ? 293  LEU A CD2   1 
ATOM   2282 N  N     . ALA A 1 294 ? -12.403 1.261   15.987  1.00 17.65  ? 294  ALA A N     1 
ATOM   2283 C  CA    . ALA A 1 294 ? -13.361 1.106   14.899  1.00 19.68  ? 294  ALA A CA    1 
ATOM   2284 C  C     . ALA A 1 294 ? -14.447 0.079   15.236  1.00 21.72  ? 294  ALA A C     1 
ATOM   2285 O  O     . ALA A 1 294 ? -15.554 0.143   14.689  1.00 20.88  ? 294  ALA A O     1 
ATOM   2286 C  CB    . ALA A 1 294 ? -12.615 0.678   13.629  1.00 18.21  ? 294  ALA A CB    1 
ATOM   2287 N  N     . MET A 1 295 ? -14.140 -0.880  16.103  1.00 17.99  ? 295  MET A N     1 
ATOM   2288 C  CA    . MET A 1 295 ? -15.064 -1.955  16.459  1.00 22.89  ? 295  MET A CA    1 
ATOM   2289 C  C     . MET A 1 295 ? -15.562 -1.834  17.884  1.00 22.62  ? 295  MET A C     1 
ATOM   2290 O  O     . MET A 1 295 ? -16.118 -2.801  18.420  1.00 21.54  ? 295  MET A O     1 
ATOM   2291 C  CB    . MET A 1 295 ? -14.406 -3.325  16.286  1.00 19.16  ? 295  MET A CB    1 
ATOM   2292 C  CG    . MET A 1 295 ? -14.016 -3.626  14.909  1.00 24.58  ? 295  MET A CG    1 
ATOM   2293 S  SD    . MET A 1 295 ? -13.452 -5.326  14.812  1.00 28.93  ? 295  MET A SD    1 
ATOM   2294 C  CE    . MET A 1 295 ? -13.052 -5.336  13.084  1.00 29.09  ? 295  MET A CE    1 
ATOM   2295 N  N     . MET A 1 296 ? -15.381 -0.659  18.496  1.00 22.12  ? 296  MET A N     1 
ATOM   2296 C  CA    . MET A 1 296 ? -15.598 -0.488  19.925  1.00 24.73  ? 296  MET A CA    1 
ATOM   2297 C  C     . MET A 1 296 ? -17.013 -0.876  20.332  1.00 25.03  ? 296  MET A C     1 
ATOM   2298 O  O     . MET A 1 296 ? -17.981 -0.640  19.598  1.00 24.31  ? 296  MET A O     1 
ATOM   2299 C  CB    . MET A 1 296 ? -15.320 0.970   20.311  1.00 22.25  ? 296  MET A CB    1 
ATOM   2300 C  CG    . MET A 1 296 ? -16.190 1.524   21.400  1.00 33.43  ? 296  MET A CG    1 
ATOM   2301 S  SD    . MET A 1 296 ? -15.629 3.148   21.928  1.00 32.56  ? 296  MET A SD    1 
ATOM   2302 C  CE    . MET A 1 296 ? -15.492 3.969   20.357  1.00 38.02  ? 296  MET A CE    1 
ATOM   2303 N  N     . ASN A 1 297 ? -17.122 -1.473  21.519  1.00 23.37  ? 297  ASN A N     1 
ATOM   2304 C  CA    . ASN A 1 297 ? -18.388 -1.668  22.209  1.00 26.40  ? 297  ASN A CA    1 
ATOM   2305 C  C     . ASN A 1 297 ? -18.510 -0.559  23.256  1.00 19.41  ? 297  ASN A C     1 
ATOM   2306 O  O     . ASN A 1 297 ? -17.862 -0.634  24.310  1.00 21.14  ? 297  ASN A O     1 
ATOM   2307 C  CB    . ASN A 1 297 ? -18.443 -3.055  22.870  1.00 21.89  ? 297  ASN A CB    1 
ATOM   2308 C  CG    . ASN A 1 297 ? -19.802 -3.353  23.490  1.00 33.64  ? 297  ASN A CG    1 
ATOM   2309 O  OD1   . ASN A 1 297 ? -20.840 -3.007  22.928  1.00 36.26  ? 297  ASN A OD1   1 
ATOM   2310 N  ND2   . ASN A 1 297 ? -19.800 -3.991  24.655  1.00 32.39  ? 297  ASN A ND2   1 
ATOM   2311 N  N     . PRO A 1 298 ? -19.247 0.510   22.995  1.00 23.00  ? 298  PRO A N     1 
ATOM   2312 C  CA    . PRO A 1 298 ? -19.252 1.639   23.938  1.00 26.29  ? 298  PRO A CA    1 
ATOM   2313 C  C     . PRO A 1 298 ? -19.841 1.240   25.283  1.00 26.43  ? 298  PRO A C     1 
ATOM   2314 O  O     . PRO A 1 298 ? -20.799 0.472   25.352  1.00 25.85  ? 298  PRO A O     1 
ATOM   2315 C  CB    . PRO A 1 298 ? -20.120 2.697   23.236  1.00 25.67  ? 298  PRO A CB    1 
ATOM   2316 C  CG    . PRO A 1 298 ? -20.861 1.979   22.180  1.00 30.58  ? 298  PRO A CG    1 
ATOM   2317 C  CD    . PRO A 1 298 ? -20.033 0.783   21.780  1.00 25.06  ? 298  PRO A CD    1 
ATOM   2318 N  N     . THR A 1 299 ? -19.240 1.747   26.364  1.00 29.91  ? 299  THR A N     1 
ATOM   2319 C  CA    . THR A 1 299 ? -19.817 1.528   27.694  1.00 27.86  ? 299  THR A CA    1 
ATOM   2320 C  C     . THR A 1 299 ? -20.987 2.458   27.995  1.00 29.10  ? 299  THR A C     1 
ATOM   2321 O  O     . THR A 1 299 ? -21.792 2.147   28.878  1.00 33.96  ? 299  THR A O     1 
ATOM   2322 C  CB    . THR A 1 299 ? -18.761 1.710   28.789  1.00 26.28  ? 299  THR A CB    1 
ATOM   2323 O  OG1   . THR A 1 299 ? -18.157 3.004   28.651  1.00 26.28  ? 299  THR A OG1   1 
ATOM   2324 C  CG2   . THR A 1 299 ? -17.681 0.651   28.689  1.00 26.50  ? 299  THR A CG2   1 
ATOM   2325 N  N     . LEU A 1 300 ? -21.089 3.594   27.309  1.00 27.30  ? 300  LEU A N     1 
ATOM   2326 C  CA    . LEU A 1 300 ? -22.155 4.556   27.599  1.00 28.55  ? 300  LEU A CA    1 
ATOM   2327 C  C     . LEU A 1 300 ? -23.476 4.045   27.036  1.00 29.85  ? 300  LEU A C     1 
ATOM   2328 O  O     . LEU A 1 300 ? -23.543 3.700   25.851  1.00 25.70  ? 300  LEU A O     1 
ATOM   2329 C  CB    . LEU A 1 300 ? -21.837 5.930   26.986  1.00 29.95  ? 300  LEU A CB    1 
ATOM   2330 C  CG    . LEU A 1 300 ? -20.734 6.816   27.571  1.00 29.88  ? 300  LEU A CG    1 
ATOM   2331 C  CD1   . LEU A 1 300 ? -20.678 8.176   26.846  1.00 27.53  ? 300  LEU A CD1   1 
ATOM   2332 C  CD2   . LEU A 1 300 ? -20.936 7.012   29.060  1.00 30.02  ? 300  LEU A CD2   1 
ATOM   2333 N  N     . PRO A 1 301 ? -24.545 3.990   27.829  1.00 28.51  ? 301  PRO A N     1 
ATOM   2334 C  CA    . PRO A 1 301 ? -25.810 3.458   27.305  1.00 28.01  ? 301  PRO A CA    1 
ATOM   2335 C  C     . PRO A 1 301 ? -26.447 4.435   26.332  1.00 26.41  ? 301  PRO A C     1 
ATOM   2336 O  O     . PRO A 1 301 ? -26.313 5.653   26.461  1.00 30.10  ? 301  PRO A O     1 
ATOM   2337 C  CB    . PRO A 1 301 ? -26.670 3.263   28.564  1.00 32.00  ? 301  PRO A CB    1 
ATOM   2338 C  CG    . PRO A 1 301 ? -26.135 4.270   29.536  1.00 37.61  ? 301  PRO A CG    1 
ATOM   2339 C  CD    . PRO A 1 301 ? -24.651 4.415   29.236  1.00 32.63  ? 301  PRO A CD    1 
ATOM   2340 N  N     . GLY A 1 302 ? -27.117 3.884   25.325  1.00 21.29  ? 302  GLY A N     1 
ATOM   2341 C  CA    . GLY A 1 302 ? -27.739 4.677   24.289  1.00 25.14  ? 302  GLY A CA    1 
ATOM   2342 C  C     . GLY A 1 302 ? -26.827 5.060   23.139  1.00 31.83  ? 302  GLY A C     1 
ATOM   2343 O  O     . GLY A 1 302 ? -27.302 5.677   22.178  1.00 29.28  ? 302  GLY A O     1 
ATOM   2344 N  N     . TRP A 1 303 ? -25.542 4.714   23.204  1.00 23.96  ? 303  TRP A N     1 
ATOM   2345 C  CA    . TRP A 1 303 ? -24.570 5.019   22.159  1.00 24.64  ? 303  TRP A CA    1 
ATOM   2346 C  C     . TRP A 1 303 ? -24.265 3.764   21.344  1.00 26.40  ? 303  TRP A C     1 
ATOM   2347 O  O     . TRP A 1 303 ? -24.316 2.640   21.854  1.00 24.11  ? 303  TRP A O     1 
ATOM   2348 C  CB    . TRP A 1 303 ? -23.288 5.582   22.781  1.00 21.83  ? 303  TRP A CB    1 
ATOM   2349 C  CG    . TRP A 1 303 ? -23.458 6.988   23.283  1.00 24.31  ? 303  TRP A CG    1 
ATOM   2350 C  CD1   . TRP A 1 303 ? -24.004 7.389   24.480  1.00 23.22  ? 303  TRP A CD1   1 
ATOM   2351 C  CD2   . TRP A 1 303 ? -23.097 8.184   22.585  1.00 21.20  ? 303  TRP A CD2   1 
ATOM   2352 N  NE1   . TRP A 1 303 ? -23.997 8.770   24.563  1.00 26.96  ? 303  TRP A NE1   1 
ATOM   2353 C  CE2   . TRP A 1 303 ? -23.446 9.279   23.414  1.00 20.03  ? 303  TRP A CE2   1 
ATOM   2354 C  CE3   . TRP A 1 303 ? -22.513 8.436   21.338  1.00 20.00  ? 303  TRP A CE3   1 
ATOM   2355 C  CZ2   . TRP A 1 303 ? -23.225 10.603  23.032  1.00 26.36  ? 303  TRP A CZ2   1 
ATOM   2356 C  CZ3   . TRP A 1 303 ? -22.298 9.744   20.960  1.00 22.56  ? 303  TRP A CZ3   1 
ATOM   2357 C  CH2   . TRP A 1 303 ? -22.648 10.815  21.804  1.00 24.47  ? 303  TRP A CH2   1 
ATOM   2358 N  N     . LYS A 1 304 ? -23.981 3.955   20.059  1.00 23.61  ? 304  LYS A N     1 
ATOM   2359 C  CA    . LYS A 1 304 ? -23.690 2.823   19.188  1.00 24.74  ? 304  LYS A CA    1 
ATOM   2360 C  C     . LYS A 1 304 ? -22.562 3.195   18.238  1.00 21.18  ? 304  LYS A C     1 
ATOM   2361 O  O     . LYS A 1 304 ? -22.535 4.303   17.699  1.00 21.94  ? 304  LYS A O     1 
ATOM   2362 C  CB    . LYS A 1 304 ? -24.927 2.390   18.381  1.00 27.37  ? 304  LYS A CB    1 
ATOM   2363 C  CG    . LYS A 1 304 ? -24.654 1.256   17.383  1.00 35.92  ? 304  LYS A CG    1 
ATOM   2364 C  CD    . LYS A 1 304 ? -25.936 0.763   16.713  1.00 49.46  ? 304  LYS A CD    1 
ATOM   2365 C  CE    . LYS A 1 304 ? -25.684 -0.490  15.882  1.00 48.28  ? 304  LYS A CE    1 
ATOM   2366 N  NZ    . LYS A 1 304 ? -26.901 -1.348  15.761  1.00 56.98  ? 304  LYS A NZ    1 
ATOM   2367 N  N     . VAL A 1 305 ? -21.634 2.268   18.035  1.00 19.53  ? 305  VAL A N     1 
ATOM   2368 C  CA    . VAL A 1 305 ? -20.534 2.461   17.097  1.00 22.20  ? 305  VAL A CA    1 
ATOM   2369 C  C     . VAL A 1 305 ? -20.670 1.409   16.008  1.00 23.94  ? 305  VAL A C     1 
ATOM   2370 O  O     . VAL A 1 305 ? -20.925 0.237   16.300  1.00 22.10  ? 305  VAL A O     1 
ATOM   2371 C  CB    . VAL A 1 305 ? -19.163 2.365   17.793  1.00 26.80  ? 305  VAL A CB    1 
ATOM   2372 C  CG1   . VAL A 1 305 ? -18.025 2.418   16.753  1.00 24.89  ? 305  VAL A CG1   1 
ATOM   2373 C  CG2   . VAL A 1 305 ? -19.018 3.495   18.800  1.00 27.89  ? 305  VAL A CG2   1 
ATOM   2374 N  N     . GLU A 1 306 ? -20.549 1.833   14.762  1.00 21.30  ? 306  GLU A N     1 
ATOM   2375 C  CA    . GLU A 1 306 ? -20.540 0.919   13.634  1.00 19.70  ? 306  GLU A CA    1 
ATOM   2376 C  C     . GLU A 1 306 ? -19.263 1.133   12.839  1.00 20.21  ? 306  GLU A C     1 
ATOM   2377 O  O     . GLU A 1 306 ? -18.786 2.267   12.701  1.00 20.40  ? 306  GLU A O     1 
ATOM   2378 C  CB    . GLU A 1 306 ? -21.779 1.126   12.761  1.00 20.30  ? 306  GLU A CB    1 
ATOM   2379 C  CG    . GLU A 1 306 ? -23.075 0.762   13.519  1.00 25.67  ? 306  GLU A CG    1 
ATOM   2380 C  CD    . GLU A 1 306 ? -24.309 1.260   12.821  1.00 24.39  ? 306  GLU A CD    1 
ATOM   2381 O  OE1   . GLU A 1 306 ? -24.571 2.475   12.886  1.00 28.73  ? 306  GLU A OE1   1 
ATOM   2382 O  OE2   . GLU A 1 306 ? -25.016 0.443   12.199  1.00 32.12  ? 306  GLU A OE2   1 
ATOM   2383 N  N     . CYS A 1 307 ? -18.721 0.044   12.313  1.00 20.23  ? 307  CYS A N     1 
ATOM   2384 C  CA    . CYS A 1 307 ? -17.415 0.052   11.670  1.00 18.58  ? 307  CYS A CA    1 
ATOM   2385 C  C     . CYS A 1 307 ? -17.578 0.181   10.159  1.00 23.65  ? 307  CYS A C     1 
ATOM   2386 O  O     . CYS A 1 307 ? -18.274 -0.626  9.535   1.00 21.59  ? 307  CYS A O     1 
ATOM   2387 C  CB    . CYS A 1 307 ? -16.666 -1.230  12.022  1.00 22.00  ? 307  CYS A CB    1 
ATOM   2388 S  SG    . CYS A 1 307 ? -15.047 -1.334  11.306  1.00 23.89  ? 307  CYS A SG    1 
ATOM   2389 N  N     . VAL A 1 308 ? -16.939 1.193   9.570   1.00 19.44  ? 308  VAL A N     1 
ATOM   2390 C  CA    . VAL A 1 308 ? -16.865 1.251   8.113   1.00 18.95  ? 308  VAL A CA    1 
ATOM   2391 C  C     . VAL A 1 308 ? -15.565 0.623   7.615   1.00 23.93  ? 308  VAL A C     1 
ATOM   2392 O  O     . VAL A 1 308 ? -15.572 -0.153  6.661   1.00 24.85  ? 308  VAL A O     1 
ATOM   2393 C  CB    . VAL A 1 308 ? -17.027 2.708   7.626   1.00 19.91  ? 308  VAL A CB    1 
ATOM   2394 C  CG1   . VAL A 1 308 ? -16.878 2.802   6.104   1.00 22.13  ? 308  VAL A CG1   1 
ATOM   2395 C  CG2   . VAL A 1 308 ? -18.377 3.274   8.042   1.00 23.08  ? 308  VAL A CG2   1 
ATOM   2396 N  N     . GLY A 1 309 ? -14.447 0.938   8.268   1.00 21.51  ? 309  GLY A N     1 
ATOM   2397 C  CA    . GLY A 1 309 ? -13.163 0.325   7.979   1.00 22.50  ? 309  GLY A CA    1 
ATOM   2398 C  C     . GLY A 1 309 ? -12.241 0.583   9.148   1.00 21.20  ? 309  GLY A C     1 
ATOM   2399 O  O     . GLY A 1 309 ? -12.503 1.448   9.985   1.00 17.60  ? 309  GLY A O     1 
ATOM   2400 N  N     . ASP A 1 310 ? -11.161 -0.182  9.221   1.00 17.48  ? 310  ASP A N     1 
ATOM   2401 C  CA    . ASP A 1 310 ? -10.291 -0.061  10.382  1.00 19.28  ? 310  ASP A CA    1 
ATOM   2402 C  C     . ASP A 1 310 ? -8.866  0.362   10.059  1.00 15.86  ? 310  ASP A C     1 
ATOM   2403 O  O     . ASP A 1 310 ? -8.029  0.382   10.976  1.00 20.22  ? 310  ASP A O     1 
ATOM   2404 C  CB    . ASP A 1 310 ? -10.270 -1.373  11.163  1.00 17.87  ? 310  ASP A CB    1 
ATOM   2405 C  CG    . ASP A 1 310 ? -9.427  -2.468  10.487  1.00 19.35  ? 310  ASP A CG    1 
ATOM   2406 O  OD1   . ASP A 1 310 ? -9.278  -2.480  9.251   1.00 18.05  ? 310  ASP A OD1   1 
ATOM   2407 O  OD2   . ASP A 1 310 ? -8.918  -3.319  11.224  1.00 19.22  ? 310  ASP A OD2   1 
ATOM   2408 N  N     . ASP A 1 311 ? -8.560  0.707   8.805   1.00 14.93  ? 311  ASP A N     1 
ATOM   2409 C  CA    . ASP A 1 311 ? -7.152  0.833   8.431   1.00 19.02  ? 311  ASP A CA    1 
ATOM   2410 C  C     . ASP A 1 311 ? -6.855  1.804   7.300   1.00 15.81  ? 311  ASP A C     1 
ATOM   2411 O  O     . ASP A 1 311 ? -5.839  2.501   7.339   1.00 15.75  ? 311  ASP A O     1 
ATOM   2412 C  CB    . ASP A 1 311 ? -6.597  -0.541  8.039   1.00 15.19  ? 311  ASP A CB    1 
ATOM   2413 C  CG    . ASP A 1 311 ? -5.071  -0.575  8.038   1.00 17.27  ? 311  ASP A CG    1 
ATOM   2414 O  OD1   . ASP A 1 311 ? -4.465  -0.270  9.079   1.00 16.65  ? 311  ASP A OD1   1 
ATOM   2415 O  OD2   . ASP A 1 311 ? -4.479  -0.935  7.003   1.00 19.80  ? 311  ASP A OD2   1 
ATOM   2416 N  N     . ILE A 1 312 ? -7.671  1.816   6.250   1.00 14.85  ? 312  ILE A N     1 
ATOM   2417 C  CA    . ILE A 1 312 ? -7.397  2.635   5.079   1.00 18.31  ? 312  ILE A CA    1 
ATOM   2418 C  C     . ILE A 1 312 ? -8.664  3.380   4.703   1.00 20.95  ? 312  ILE A C     1 
ATOM   2419 O  O     . ILE A 1 312 ? -9.729  2.770   4.569   1.00 19.21  ? 312  ILE A O     1 
ATOM   2420 C  CB    . ILE A 1 312 ? -6.891  1.796   3.882   1.00 20.62  ? 312  ILE A CB    1 
ATOM   2421 C  CG1   . ILE A 1 312 ? -5.603  1.044   4.263   1.00 19.52  ? 312  ILE A CG1   1 
ATOM   2422 C  CG2   . ILE A 1 312 ? -6.673  2.700   2.668   1.00 20.42  ? 312  ILE A CG2   1 
ATOM   2423 C  CD1   . ILE A 1 312 ? -4.899  0.430   3.127   1.00 27.17  ? 312  ILE A CD1   1 
ATOM   2424 N  N     . ALA A 1 313 ? -8.546  4.694   4.512   1.00 17.62  ? 313  ALA A N     1 
ATOM   2425 C  CA    . ALA A 1 313 ? -9.651  5.524   4.060   1.00 20.14  ? 313  ALA A CA    1 
ATOM   2426 C  C     . ALA A 1 313 ? -9.243  6.230   2.781   1.00 21.17  ? 313  ALA A C     1 
ATOM   2427 O  O     . ALA A 1 313 ? -8.131  6.748   2.689   1.00 18.91  ? 313  ALA A O     1 
ATOM   2428 C  CB    . ALA A 1 313 ? -10.035 6.567   5.112   1.00 18.07  ? 313  ALA A CB    1 
ATOM   2429 N  N     . TRP A 1 314 ? -10.145 6.256   1.802   1.00 20.79  ? 314  TRP A N     1 
ATOM   2430 C  CA    . TRP A 1 314 ? -10.007 7.100   0.622   1.00 21.28  ? 314  TRP A CA    1 
ATOM   2431 C  C     . TRP A 1 314 ? -11.097 8.163   0.675   1.00 26.32  ? 314  TRP A C     1 
ATOM   2432 O  O     . TRP A 1 314 ? -12.276 7.832   0.850   1.00 24.47  ? 314  TRP A O     1 
ATOM   2433 C  CB    . TRP A 1 314 ? -10.135 6.294   -0.674  1.00 20.73  ? 314  TRP A CB    1 
ATOM   2434 C  CG    . TRP A 1 314 ? -8.996  5.343   -0.978  1.00 21.61  ? 314  TRP A CG    1 
ATOM   2435 C  CD1   . TRP A 1 314 ? -7.854  5.148   -0.250  1.00 18.84  ? 314  TRP A CD1   1 
ATOM   2436 C  CD2   . TRP A 1 314 ? -8.903  4.462   -2.111  1.00 21.84  ? 314  TRP A CD2   1 
ATOM   2437 N  NE1   . TRP A 1 314 ? -7.060  4.180   -0.863  1.00 19.00  ? 314  TRP A NE1   1 
ATOM   2438 C  CE2   . TRP A 1 314 ? -7.689  3.757   -2.002  1.00 16.94  ? 314  TRP A CE2   1 
ATOM   2439 C  CE3   . TRP A 1 314 ? -9.739  4.196   -3.199  1.00 24.13  ? 314  TRP A CE3   1 
ATOM   2440 C  CZ2   . TRP A 1 314 ? -7.287  2.818   -2.941  1.00 24.06  ? 314  TRP A CZ2   1 
ATOM   2441 C  CZ3   . TRP A 1 314 ? -9.332  3.249   -4.131  1.00 27.18  ? 314  TRP A CZ3   1 
ATOM   2442 C  CH2   . TRP A 1 314 ? -8.120  2.586   -3.999  1.00 25.88  ? 314  TRP A CH2   1 
ATOM   2443 N  N     . MET A 1 315 ? -10.716 9.432   0.503   1.00 21.53  ? 315  MET A N     1 
ATOM   2444 C  CA    . MET A 1 315 ? -11.628 10.529  0.801   1.00 24.30  ? 315  MET A CA    1 
ATOM   2445 C  C     . MET A 1 315 ? -11.540 11.622  -0.252  1.00 25.80  ? 315  MET A C     1 
ATOM   2446 O  O     . MET A 1 315 ? -10.490 11.854  -0.851  1.00 28.07  ? 315  MET A O     1 
ATOM   2447 C  CB    . MET A 1 315 ? -11.347 11.158  2.178   1.00 25.36  ? 315  MET A CB    1 
ATOM   2448 C  CG    . MET A 1 315 ? -11.182 10.162  3.301   1.00 30.70  ? 315  MET A CG    1 
ATOM   2449 S  SD    . MET A 1 315 ? -11.146 10.951  4.919   1.00 33.78  ? 315  MET A SD    1 
ATOM   2450 C  CE    . MET A 1 315 ? -9.614  11.865  4.860   1.00 31.99  ? 315  MET A CE    1 
ATOM   2451 N  N     . LYS A 1 316 ? -12.649 12.328  -0.428  1.00 28.10  ? 316  LYS A N     1 
ATOM   2452 C  CA    . LYS A 1 316 ? -12.751 13.343  -1.462  1.00 32.83  ? 316  LYS A CA    1 
ATOM   2453 C  C     . LYS A 1 316 ? -13.941 14.228  -1.142  1.00 29.81  ? 316  LYS A C     1 
ATOM   2454 O  O     . LYS A 1 316 ? -14.947 13.755  -0.617  1.00 29.61  ? 316  LYS A O     1 
ATOM   2455 C  CB    . LYS A 1 316 ? -12.913 12.696  -2.844  1.00 36.46  ? 316  LYS A CB    1 
ATOM   2456 C  CG    . LYS A 1 316 ? -12.886 13.662  -4.006  1.00 40.68  ? 316  LYS A CG    1 
ATOM   2457 C  CD    . LYS A 1 316 ? -12.889 12.924  -5.342  1.00 45.75  ? 316  LYS A CD    1 
ATOM   2458 C  CE    . LYS A 1 316 ? -13.984 11.864  -5.398  1.00 49.74  ? 316  LYS A CE    1 
ATOM   2459 N  NZ    . LYS A 1 316 ? -15.319 12.409  -5.054  1.00 54.02  ? 316  LYS A NZ    1 
ATOM   2460 N  N     . PHE A 1 317 ? -13.823 15.511  -1.440  1.00 31.74  ? 317  PHE A N     1 
ATOM   2461 C  CA    . PHE A 1 317 ? -15.001 16.358  -1.365  1.00 36.32  ? 317  PHE A CA    1 
ATOM   2462 C  C     . PHE A 1 317 ? -15.950 16.007  -2.501  1.00 37.68  ? 317  PHE A C     1 
ATOM   2463 O  O     . PHE A 1 317 ? -15.523 15.699  -3.618  1.00 37.24  ? 317  PHE A O     1 
ATOM   2464 C  CB    . PHE A 1 317 ? -14.601 17.832  -1.405  1.00 37.08  ? 317  PHE A CB    1 
ATOM   2465 C  CG    . PHE A 1 317 ? -13.881 18.272  -0.169  1.00 40.17  ? 317  PHE A CG    1 
ATOM   2466 C  CD1   . PHE A 1 317 ? -14.589 18.654  0.959   1.00 35.85  ? 317  PHE A CD1   1 
ATOM   2467 C  CD2   . PHE A 1 317 ? -12.498 18.255  -0.113  1.00 41.03  ? 317  PHE A CD2   1 
ATOM   2468 C  CE1   . PHE A 1 317 ? -13.933 19.041  2.112   1.00 35.84  ? 317  PHE A CE1   1 
ATOM   2469 C  CE2   . PHE A 1 317 ? -11.837 18.634  1.038   1.00 41.31  ? 317  PHE A CE2   1 
ATOM   2470 C  CZ    . PHE A 1 317 ? -12.557 19.032  2.151   1.00 41.41  ? 317  PHE A CZ    1 
ATOM   2471 N  N     . ASP A 1 318 ? -17.239 15.976  -2.189  1.00 33.86  ? 318  ASP A N     1 
ATOM   2472 C  CA    . ASP A 1 318 ? -18.254 15.867  -3.219  1.00 36.04  ? 318  ASP A CA    1 
ATOM   2473 C  C     . ASP A 1 318 ? -18.682 17.268  -3.652  1.00 37.45  ? 318  ASP A C     1 
ATOM   2474 O  O     . ASP A 1 318 ? -18.157 18.282  -3.179  1.00 34.23  ? 318  ASP A O     1 
ATOM   2475 C  CB    . ASP A 1 318 ? -19.444 15.031  -2.731  1.00 42.13  ? 318  ASP A CB    1 
ATOM   2476 C  CG    . ASP A 1 318 ? -20.222 15.688  -1.589  1.00 35.85  ? 318  ASP A CG    1 
ATOM   2477 O  OD1   . ASP A 1 318 ? -20.110 16.910  -1.358  1.00 36.77  ? 318  ASP A OD1   1 
ATOM   2478 O  OD2   . ASP A 1 318 ? -20.963 14.952  -0.899  1.00 34.02  ? 318  ASP A OD2   1 
ATOM   2479 N  N     . ALA A 1 319 ? -19.686 17.321  -4.530  1.00 41.59  ? 319  ALA A N     1 
ATOM   2480 C  CA    . ALA A 1 319 ? -20.152 18.599  -5.059  1.00 44.32  ? 319  ALA A CA    1 
ATOM   2481 C  C     . ALA A 1 319 ? -20.664 19.524  -3.960  1.00 49.88  ? 319  ALA A C     1 
ATOM   2482 O  O     . ALA A 1 319 ? -20.551 20.751  -4.079  1.00 48.24  ? 319  ALA A O     1 
ATOM   2483 C  CB    . ALA A 1 319 ? -21.244 18.354  -6.101  1.00 49.74  ? 319  ALA A CB    1 
ATOM   2484 N  N     . GLN A 1 320 ? -21.220 18.964  -2.885  1.00 36.82  ? 320  GLN A N     1 
ATOM   2485 C  CA    . GLN A 1 320 ? -21.780 19.766  -1.805  1.00 36.65  ? 320  GLN A CA    1 
ATOM   2486 C  C     . GLN A 1 320 ? -20.738 20.243  -0.802  1.00 41.05  ? 320  GLN A C     1 
ATOM   2487 O  O     . GLN A 1 320 ? -21.095 20.956  0.140   1.00 39.47  ? 320  GLN A O     1 
ATOM   2488 C  CB    . GLN A 1 320 ? -22.859 18.964  -1.069  1.00 45.01  ? 320  GLN A CB    1 
ATOM   2489 C  CG    . GLN A 1 320 ? -23.792 18.210  -1.997  1.00 44.58  ? 320  GLN A CG    1 
ATOM   2490 C  CD    . GLN A 1 320 ? -24.643 19.142  -2.834  1.00 51.59  ? 320  GLN A CD    1 
ATOM   2491 O  OE1   . GLN A 1 320 ? -24.984 20.243  -2.400  1.00 60.27  ? 320  GLN A OE1   1 
ATOM   2492 N  NE2   . GLN A 1 320 ? -24.989 18.708  -4.042  1.00 54.97  ? 320  GLN A NE2   1 
ATOM   2493 N  N     . GLY A 1 321 ? -19.471 19.869  -0.958  1.00 36.32  ? 321  GLY A N     1 
ATOM   2494 C  CA    . GLY A 1 321 ? -18.474 20.259  0.012   1.00 34.96  ? 321  GLY A CA    1 
ATOM   2495 C  C     . GLY A 1 321 ? -18.368 19.360  1.220   1.00 32.98  ? 321  GLY A C     1 
ATOM   2496 O  O     . GLY A 1 321 ? -17.688 19.730  2.185   1.00 35.18  ? 321  GLY A O     1 
ATOM   2497 N  N     . ASN A 1 322 ? -19.025 18.200  1.211   1.00 31.88  ? 322  ASN A N     1 
ATOM   2498 C  CA    . ASN A 1 322 ? -18.817 17.210  2.259   1.00 27.92  ? 322  ASN A CA    1 
ATOM   2499 C  C     . ASN A 1 322 ? -17.583 16.378  1.939   1.00 30.31  ? 322  ASN A C     1 
ATOM   2500 O  O     . ASN A 1 322 ? -17.371 15.977  0.790   1.00 31.48  ? 322  ASN A O     1 
ATOM   2501 C  CB    . ASN A 1 322 ? -20.041 16.298  2.399   1.00 34.26  ? 322  ASN A CB    1 
ATOM   2502 C  CG    . ASN A 1 322 ? -21.320 17.071  2.647   1.00 35.36  ? 322  ASN A CG    1 
ATOM   2503 O  OD1   . ASN A 1 322 ? -21.527 17.621  3.726   1.00 39.09  ? 322  ASN A OD1   1 
ATOM   2504 N  ND2   . ASN A 1 322 ? -22.185 17.118  1.642   1.00 38.89  ? 322  ASN A ND2   1 
ATOM   2505 N  N     . LEU A 1 323 ? -16.747 16.142  2.946   1.00 25.48  ? 323  LEU A N     1 
ATOM   2506 C  CA    . LEU A 1 323 ? -15.659 15.182  2.794   1.00 25.63  ? 323  LEU A CA    1 
ATOM   2507 C  C     . LEU A 1 323 ? -16.241 13.779  2.935   1.00 22.68  ? 323  LEU A C     1 
ATOM   2508 O  O     . LEU A 1 323 ? -16.802 13.443  3.984   1.00 28.09  ? 323  LEU A O     1 
ATOM   2509 C  CB    . LEU A 1 323 ? -14.573 15.431  3.837   1.00 22.51  ? 323  LEU A CB    1 
ATOM   2510 C  CG    . LEU A 1 323 ? -13.310 14.578  3.780   1.00 29.75  ? 323  LEU A CG    1 
ATOM   2511 C  CD1   . LEU A 1 323 ? -12.567 14.767  2.451   1.00 28.87  ? 323  LEU A CD1   1 
ATOM   2512 C  CD2   . LEU A 1 323 ? -12.416 14.915  4.969   1.00 27.80  ? 323  LEU A CD2   1 
ATOM   2513 N  N     . ARG A 1 324 ? -16.142 12.979  1.876   1.00 24.28  ? 324  ARG A N     1 
ATOM   2514 C  CA    . ARG A 1 324 ? -16.711 11.640  1.834   1.00 26.74  ? 324  ARG A CA    1 
ATOM   2515 C  C     . ARG A 1 324 ? -15.603 10.601  1.830   1.00 24.77  ? 324  ARG A C     1 
ATOM   2516 O  O     . ARG A 1 324 ? -14.635 10.722  1.072   1.00 23.65  ? 324  ARG A O     1 
ATOM   2517 C  CB    . ARG A 1 324 ? -17.595 11.458  0.601   1.00 31.86  ? 324  ARG A CB    1 
ATOM   2518 C  CG    . ARG A 1 324 ? -18.623 12.547  0.438   1.00 33.31  ? 324  ARG A CG    1 
ATOM   2519 C  CD    . ARG A 1 324 ? -19.779 12.082  -0.404  1.00 42.36  ? 324  ARG A CD    1 
ATOM   2520 N  NE    . ARG A 1 324 ? -20.630 11.131  0.300   1.00 37.64  ? 324  ARG A NE    1 
ATOM   2521 C  CZ    . ARG A 1 324 ? -21.707 11.469  0.995   1.00 36.79  ? 324  ARG A CZ    1 
ATOM   2522 N  NH1   . ARG A 1 324 ? -22.065 12.733  1.143   1.00 36.12  ? 324  ARG A NH1   1 
ATOM   2523 N  NH2   . ARG A 1 324 ? -22.448 10.515  1.548   1.00 30.60  ? 324  ARG A NH2   1 
ATOM   2524 N  N     . ALA A 1 325 ? -15.754 9.570   2.656   1.00 22.81  ? 325  ALA A N     1 
ATOM   2525 C  CA    . ALA A 1 325 ? -14.760 8.509   2.754   1.00 21.52  ? 325  ALA A CA    1 
ATOM   2526 C  C     . ALA A 1 325 ? -15.354 7.171   2.351   1.00 23.65  ? 325  ALA A C     1 
ATOM   2527 O  O     . ALA A 1 325 ? -16.516 6.884   2.647   1.00 24.02  ? 325  ALA A O     1 
ATOM   2528 C  CB    . ALA A 1 325 ? -14.208 8.388   4.174   1.00 19.64  ? 325  ALA A CB    1 
ATOM   2529 N  N     . ILE A 1 326 ? -14.547 6.342   1.692   1.00 23.33  ? 326  ILE A N     1 
ATOM   2530 C  CA    . ILE A 1 326 ? -14.872 4.931   1.563   1.00 21.28  ? 326  ILE A CA    1 
ATOM   2531 C  C     . ILE A 1 326 ? -13.731 4.135   2.165   1.00 22.09  ? 326  ILE A C     1 
ATOM   2532 O  O     . ILE A 1 326 ? -12.597 4.608   2.275   1.00 21.54  ? 326  ILE A O     1 
ATOM   2533 C  CB    . ILE A 1 326 ? -15.131 4.479   0.111   1.00 28.73  ? 326  ILE A CB    1 
ATOM   2534 C  CG1   . ILE A 1 326 ? -13.893 4.704   -0.751  1.00 25.64  ? 326  ILE A CG1   1 
ATOM   2535 C  CG2   . ILE A 1 326 ? -16.371 5.157   -0.467  1.00 25.09  ? 326  ILE A CG2   1 
ATOM   2536 C  CD1   . ILE A 1 326 ? -13.555 3.522   -1.630  1.00 28.96  ? 326  ILE A CD1   1 
ATOM   2537 N  N     . ASN A 1 327 ? -14.066 2.922   2.602   1.00 20.45  ? 327  ASN A N     1 
ATOM   2538 C  CA    . ASN A 1 327 ? -13.073 1.924   2.961   1.00 24.00  ? 327  ASN A CA    1 
ATOM   2539 C  C     . ASN A 1 327 ? -12.813 1.084   1.719   1.00 25.84  ? 327  ASN A C     1 
ATOM   2540 O  O     . ASN A 1 327 ? -13.732 0.402   1.247   1.00 20.80  ? 327  ASN A O     1 
ATOM   2541 C  CB    . ASN A 1 327 ? -13.583 1.055   4.105   1.00 23.60  ? 327  ASN A CB    1 
ATOM   2542 C  CG    . ASN A 1 327 ? -12.724 -0.187  4.349   1.00 23.67  ? 327  ASN A CG    1 
ATOM   2543 O  OD1   . ASN A 1 327 ? -11.539 -0.248  3.980   1.00 19.62  ? 327  ASN A OD1   1 
ATOM   2544 N  ND2   . ASN A 1 327 ? -13.324 -1.186  4.995   1.00 21.46  ? 327  ASN A ND2   1 
ATOM   2545 N  N     . PRO A 1 328 ? -11.613 1.127   1.131   1.00 22.03  ? 328  PRO A N     1 
ATOM   2546 C  CA    . PRO A 1 328 ? -11.371 0.348   -0.094  1.00 21.95  ? 328  PRO A CA    1 
ATOM   2547 C  C     . PRO A 1 328 ? -11.167 -1.147  0.140   1.00 22.80  ? 328  PRO A C     1 
ATOM   2548 O  O     . PRO A 1 328 ? -11.168 -1.908  -0.839  1.00 22.37  ? 328  PRO A O     1 
ATOM   2549 C  CB    . PRO A 1 328 ? -10.104 1.000   -0.672  1.00 22.70  ? 328  PRO A CB    1 
ATOM   2550 C  CG    . PRO A 1 328 ? -9.359  1.508   0.543   1.00 21.50  ? 328  PRO A CG    1 
ATOM   2551 C  CD    . PRO A 1 328 ? -10.423 1.873   1.576   1.00 17.48  ? 328  PRO A CD    1 
ATOM   2552 N  N     . GLU A 1 329 ? -11.007 -1.593  1.388   1.00 20.59  ? 329  GLU A N     1 
ATOM   2553 C  CA    . GLU A 1 329 ? -10.741 -2.990  1.706   1.00 21.41  ? 329  GLU A CA    1 
ATOM   2554 C  C     . GLU A 1 329 ? -12.039 -3.781  1.821   1.00 22.54  ? 329  GLU A C     1 
ATOM   2555 O  O     . GLU A 1 329 ? -13.129 -3.222  1.911   1.00 23.84  ? 329  GLU A O     1 
ATOM   2556 C  CB    . GLU A 1 329 ? -9.961  -3.119  3.016   1.00 21.48  ? 329  GLU A CB    1 
ATOM   2557 C  CG    . GLU A 1 329 ? -8.723  -2.230  3.107   1.00 20.34  ? 329  GLU A CG    1 
ATOM   2558 C  CD    . GLU A 1 329 ? -7.744  -2.741  4.149   1.00 20.13  ? 329  GLU A CD    1 
ATOM   2559 O  OE1   . GLU A 1 329 ? -7.907  -2.417  5.336   1.00 19.99  ? 329  GLU A OE1   1 
ATOM   2560 O  OE2   . GLU A 1 329 ? -6.825  -3.497  3.792   1.00 21.75  ? 329  GLU A OE2   1 
ATOM   2561 N  N     . ASN A 1 330 ? -11.897 -5.110  1.840   1.00 21.30  ? 330  ASN A N     1 
ATOM   2562 C  CA    . ASN A 1 330 ? -13.017 -6.033  1.949   1.00 19.34  ? 330  ASN A CA    1 
ATOM   2563 C  C     . ASN A 1 330 ? -12.965 -6.863  3.226   1.00 20.08  ? 330  ASN A C     1 
ATOM   2564 O  O     . ASN A 1 330 ? -13.834 -7.713  3.435   1.00 18.97  ? 330  ASN A O     1 
ATOM   2565 C  CB    . ASN A 1 330 ? -13.035 -6.956  0.718   1.00 23.12  ? 330  ASN A CB    1 
ATOM   2566 C  CG    . ASN A 1 330 ? -14.382 -7.628  0.496   1.00 27.86  ? 330  ASN A CG    1 
ATOM   2567 O  OD1   . ASN A 1 330 ? -15.420 -7.083  0.850   1.00 25.92  ? 330  ASN A OD1   1 
ATOM   2568 N  ND2   . ASN A 1 330 ? -14.362 -8.825  -0.094  1.00 25.72  ? 330  ASN A ND2   1 
ATOM   2569 N  N     . GLY A 1 331 ? -11.952 -6.669  4.067   1.00 17.00  ? 331  GLY A N     1 
ATOM   2570 C  CA    . GLY A 1 331 ? -11.836 -7.423  5.297   1.00 18.56  ? 331  GLY A CA    1 
ATOM   2571 C  C     . GLY A 1 331 ? -10.941 -6.686  6.267   1.00 20.24  ? 331  GLY A C     1 
ATOM   2572 O  O     . GLY A 1 331 ? -10.448 -5.593  5.977   1.00 21.75  ? 331  GLY A O     1 
ATOM   2573 N  N     . PHE A 1 332 ? -10.711 -7.313  7.420   1.00 17.64  ? 332  PHE A N     1 
ATOM   2574 C  CA    . PHE A 1 332 ? -9.828  -6.781  8.456   1.00 22.84  ? 332  PHE A CA    1 
ATOM   2575 C  C     . PHE A 1 332 ? -8.636  -7.701  8.650   1.00 17.50  ? 332  PHE A C     1 
ATOM   2576 O  O     . PHE A 1 332 ? -8.805  -8.914  8.791   1.00 19.20  ? 332  PHE A O     1 
ATOM   2577 C  CB    . PHE A 1 332 ? -10.552 -6.632  9.803   1.00 19.97  ? 332  PHE A CB    1 
ATOM   2578 C  CG    . PHE A 1 332 ? -11.882 -5.967  9.697   1.00 21.73  ? 332  PHE A CG    1 
ATOM   2579 C  CD1   . PHE A 1 332 ? -11.973 -4.632  9.332   1.00 19.55  ? 332  PHE A CD1   1 
ATOM   2580 C  CD2   . PHE A 1 332 ? -13.047 -6.676  9.974   1.00 22.97  ? 332  PHE A CD2   1 
ATOM   2581 C  CE1   . PHE A 1 332 ? -13.195 -4.015  9.224   1.00 24.88  ? 332  PHE A CE1   1 
ATOM   2582 C  CE2   . PHE A 1 332 ? -14.278 -6.055  9.885   1.00 26.14  ? 332  PHE A CE2   1 
ATOM   2583 C  CZ    . PHE A 1 332 ? -14.353 -4.730  9.514   1.00 21.81  ? 332  PHE A CZ    1 
ATOM   2584 N  N     . PHE A 1 333 ? -7.444  -7.110  8.702   1.00 15.90  ? 333  PHE A N     1 
ATOM   2585 C  CA    . PHE A 1 333 ? -6.173  -7.789  8.906   1.00 19.84  ? 333  PHE A CA    1 
ATOM   2586 C  C     . PHE A 1 333 ? -5.601  -7.272  10.224  1.00 19.36  ? 333  PHE A C     1 
ATOM   2587 O  O     . PHE A 1 333 ? -4.690  -6.433  10.246  1.00 18.33  ? 333  PHE A O     1 
ATOM   2588 C  CB    . PHE A 1 333 ? -5.231  -7.514  7.689   1.00 19.40  ? 333  PHE A CB    1 
ATOM   2589 C  CG    . PHE A 1 333 ? -3.950  -8.290  7.710   1.00 19.65  ? 333  PHE A CG    1 
ATOM   2590 C  CD1   . PHE A 1 333 ? -3.959  -9.681  7.633   1.00 21.20  ? 333  PHE A CD1   1 
ATOM   2591 C  CD2   . PHE A 1 333 ? -2.727  -7.628  7.755   1.00 22.58  ? 333  PHE A CD2   1 
ATOM   2592 C  CE1   . PHE A 1 333 ? -2.775  -10.401 7.636   1.00 19.30  ? 333  PHE A CE1   1 
ATOM   2593 C  CE2   . PHE A 1 333 ? -1.529  -8.335  7.749   1.00 20.03  ? 333  PHE A CE2   1 
ATOM   2594 C  CZ    . PHE A 1 333 ? -1.554  -9.730  7.694   1.00 21.91  ? 333  PHE A CZ    1 
ATOM   2595 N  N     . GLY A 1 334 ? -6.140  -7.780  11.326  1.00 18.87  ? 334  GLY A N     1 
ATOM   2596 C  CA    . GLY A 1 334 ? -5.964  -7.167  12.628  1.00 15.55  ? 334  GLY A CA    1 
ATOM   2597 C  C     . GLY A 1 334 ? -4.954  -7.888  13.500  1.00 17.04  ? 334  GLY A C     1 
ATOM   2598 O  O     . GLY A 1 334 ? -4.776  -9.101  13.403  1.00 19.21  ? 334  GLY A O     1 
ATOM   2599 N  N     . VAL A 1 335 ? -4.311  -7.117  14.378  1.00 19.12  ? 335  VAL A N     1 
ATOM   2600 C  CA    . VAL A 1 335 ? -3.409  -7.685  15.373  1.00 16.07  ? 335  VAL A CA    1 
ATOM   2601 C  C     . VAL A 1 335 ? -4.189  -8.582  16.326  1.00 18.36  ? 335  VAL A C     1 
ATOM   2602 O  O     . VAL A 1 335 ? -5.219  -8.184  16.883  1.00 21.95  ? 335  VAL A O     1 
ATOM   2603 C  CB    . VAL A 1 335 ? -2.681  -6.565  16.128  1.00 22.13  ? 335  VAL A CB    1 
ATOM   2604 C  CG1   . VAL A 1 335 ? -1.871  -7.125  17.301  1.00 19.97  ? 335  VAL A CG1   1 
ATOM   2605 C  CG2   . VAL A 1 335 ? -1.784  -5.800  15.155  1.00 22.37  ? 335  VAL A CG2   1 
ATOM   2606 N  N     . ALA A 1 336 ? -3.699  -9.799  16.513  1.00 21.81  ? 336  ALA A N     1 
ATOM   2607 C  CA    . ALA A 1 336 ? -4.381  -10.775 17.361  1.00 19.50  ? 336  ALA A CA    1 
ATOM   2608 C  C     . ALA A 1 336 ? -4.055  -10.591 18.849  1.00 18.86  ? 336  ALA A C     1 
ATOM   2609 O  O     . ALA A 1 336 ? -4.988  -10.474 19.648  1.00 23.62  ? 336  ALA A O     1 
ATOM   2610 C  CB    . ALA A 1 336 ? -4.056  -12.191 16.886  1.00 21.83  ? 336  ALA A CB    1 
ATOM   2611 N  N     . PRO A 1 337 ? -2.786  -10.566 19.280  1.00 23.52  ? 337  PRO A N     1 
ATOM   2612 C  CA    . PRO A 1 337 ? -2.517  -10.403 20.719  1.00 20.87  ? 337  PRO A CA    1 
ATOM   2613 C  C     . PRO A 1 337 ? -3.180  -9.148  21.271  1.00 27.58  ? 337  PRO A C     1 
ATOM   2614 O  O     . PRO A 1 337 ? -3.271  -8.120  20.592  1.00 27.06  ? 337  PRO A O     1 
ATOM   2615 C  CB    . PRO A 1 337 ? -0.986  -10.314 20.792  1.00 26.80  ? 337  PRO A CB    1 
ATOM   2616 C  CG    . PRO A 1 337 ? -0.516  -11.072 19.589  1.00 25.21  ? 337  PRO A CG    1 
ATOM   2617 C  CD    . PRO A 1 337 ? -1.532  -10.731 18.518  1.00 24.29  ? 337  PRO A CD    1 
ATOM   2618 N  N     . GLY A 1 338 ? -3.691  -9.263  22.504  1.00 22.84  ? 338  GLY A N     1 
ATOM   2619 C  CA    . GLY A 1 338 ? -4.453  -8.215  23.151  1.00 22.69  ? 338  GLY A CA    1 
ATOM   2620 C  C     . GLY A 1 338 ? -5.929  -8.205  22.822  1.00 26.59  ? 338  GLY A C     1 
ATOM   2621 O  O     . GLY A 1 338 ? -6.692  -7.479  23.472  1.00 32.75  ? 338  GLY A O     1 
ATOM   2622 N  N     . THR A 1 339 ? -6.354  -8.968  21.826  1.00 23.56  ? 339  THR A N     1 
ATOM   2623 C  CA    . THR A 1 339 ? -7.766  -9.077  21.490  1.00 22.39  ? 339  THR A CA    1 
ATOM   2624 C  C     . THR A 1 339 ? -8.448  -10.021 22.478  1.00 26.76  ? 339  THR A C     1 
ATOM   2625 O  O     . THR A 1 339 ? -8.067  -11.192 22.588  1.00 25.08  ? 339  THR A O     1 
ATOM   2626 C  CB    . THR A 1 339 ? -7.926  -9.613  20.072  1.00 22.80  ? 339  THR A CB    1 
ATOM   2627 O  OG1   . THR A 1 339 ? -7.193  -8.783  19.166  1.00 24.59  ? 339  THR A OG1   1 
ATOM   2628 C  CG2   . THR A 1 339 ? -9.381  -9.647  19.667  1.00 26.34  ? 339  THR A CG2   1 
ATOM   2629 N  N     . SER A 1 340 ? -9.468  -9.528  23.176  1.00 23.06  ? 340  SER A N     1 
ATOM   2630 C  CA    . SER A 1 340 ? -10.206 -10.364 24.109  1.00 30.49  ? 340  SER A CA    1 
ATOM   2631 C  C     . SER A 1 340 ? -11.644 -9.885  24.166  1.00 30.95  ? 340  SER A C     1 
ATOM   2632 O  O     . SER A 1 340 ? -11.996 -8.829  23.630  1.00 29.24  ? 340  SER A O     1 
ATOM   2633 C  CB    . SER A 1 340 ? -9.579  -10.340 25.503  1.00 28.82  ? 340  SER A CB    1 
ATOM   2634 O  OG    . SER A 1 340 ? -9.855  -9.105  26.132  1.00 34.51  ? 340  SER A OG    1 
ATOM   2635 N  N     . VAL A 1 341 ? -12.478 -10.675 24.845  1.00 28.12  ? 341  VAL A N     1 
ATOM   2636 C  CA    . VAL A 1 341 ? -13.864 -10.276 25.067  1.00 32.11  ? 341  VAL A CA    1 
ATOM   2637 C  C     . VAL A 1 341 ? -13.934 -8.922  25.759  1.00 24.44  ? 341  VAL A C     1 
ATOM   2638 O  O     . VAL A 1 341 ? -14.903 -8.177  25.582  1.00 31.57  ? 341  VAL A O     1 
ATOM   2639 C  CB    . VAL A 1 341 ? -14.598 -11.378 25.867  1.00 39.56  ? 341  VAL A CB    1 
ATOM   2640 C  CG1   . VAL A 1 341 ? -16.026 -10.970 26.183  1.00 46.52  ? 341  VAL A CG1   1 
ATOM   2641 C  CG2   . VAL A 1 341 ? -14.588 -12.669 25.078  1.00 43.51  ? 341  VAL A CG2   1 
ATOM   2642 N  N     . LYS A 1 342 ? -12.912 -8.573  26.545  1.00 28.36  ? 342  LYS A N     1 
ATOM   2643 C  CA    . LYS A 1 342 ? -12.903 -7.296  27.251  1.00 30.89  ? 342  LYS A CA    1 
ATOM   2644 C  C     . LYS A 1 342 ? -12.484 -6.139  26.345  1.00 38.62  ? 342  LYS A C     1 
ATOM   2645 O  O     . LYS A 1 342 ? -13.113 -5.073  26.353  1.00 37.48  ? 342  LYS A O     1 
ATOM   2646 C  CB    . LYS A 1 342 ? -11.966 -7.370  28.458  1.00 35.89  ? 342  LYS A CB    1 
ATOM   2647 C  CG    . LYS A 1 342 ? -12.435 -8.318  29.554  1.00 45.96  ? 342  LYS A CG    1 
ATOM   2648 C  CD    . LYS A 1 342 ? -11.639 -8.114  30.839  1.00 54.78  ? 342  LYS A CD    1 
ATOM   2649 C  CE    . LYS A 1 342 ? -12.074 -9.098  31.926  1.00 58.15  ? 342  LYS A CE    1 
ATOM   2650 N  NZ    . LYS A 1 342 ? -11.347 -8.863  33.204  1.00 61.99  ? 342  LYS A NZ    1 
ATOM   2651 N  N     . THR A 1 343 ? -11.402 -6.318  25.586  1.00 31.14  ? 343  THR A N     1 
ATOM   2652 C  CA    . THR A 1 343 ? -10.851 -5.219  24.798  1.00 30.12  ? 343  THR A CA    1 
ATOM   2653 C  C     . THR A 1 343 ? -11.590 -5.029  23.482  1.00 32.88  ? 343  THR A C     1 
ATOM   2654 O  O     . THR A 1 343 ? -11.818 -3.890  23.052  1.00 35.39  ? 343  THR A O     1 
ATOM   2655 C  CB    . THR A 1 343 ? -9.379  -5.463  24.506  1.00 29.92  ? 343  THR A CB    1 
ATOM   2656 O  OG1   . THR A 1 343 ? -9.235  -6.700  23.786  1.00 31.53  ? 343  THR A OG1   1 
ATOM   2657 C  CG2   . THR A 1 343 ? -8.577  -5.515  25.799  1.00 35.87  ? 343  THR A CG2   1 
ATOM   2658 N  N     . ASN A 1 344 ? -11.941 -6.120  22.805  1.00 23.71  ? 344  ASN A N     1 
ATOM   2659 C  CA    . ASN A 1 344 ? -12.532 -6.035  21.472  1.00 24.04  ? 344  ASN A CA    1 
ATOM   2660 C  C     . ASN A 1 344 ? -13.505 -7.187  21.265  1.00 27.49  ? 344  ASN A C     1 
ATOM   2661 O  O     . ASN A 1 344 ? -13.274 -8.083  20.438  1.00 25.99  ? 344  ASN A O     1 
ATOM   2662 C  CB    . ASN A 1 344 ? -11.437 -6.027  20.405  1.00 23.00  ? 344  ASN A CB    1 
ATOM   2663 C  CG    . ASN A 1 344 ? -11.920 -5.468  19.094  1.00 26.34  ? 344  ASN A CG    1 
ATOM   2664 O  OD1   . ASN A 1 344 ? -13.127 -5.368  18.860  1.00 26.51  ? 344  ASN A OD1   1 
ATOM   2665 N  ND2   . ASN A 1 344 ? -10.981 -5.109  18.217  1.00 21.68  ? 344  ASN A ND2   1 
ATOM   2666 N  N     . PRO A 1 345 ? -14.631 -7.180  21.995  1.00 27.95  ? 345  PRO A N     1 
ATOM   2667 C  CA    . PRO A 1 345 ? -15.621 -8.261  21.846  1.00 26.27  ? 345  PRO A CA    1 
ATOM   2668 C  C     . PRO A 1 345 ? -16.177 -8.395  20.438  1.00 30.45  ? 345  PRO A C     1 
ATOM   2669 O  O     . PRO A 1 345 ? -16.495 -9.516  20.012  1.00 26.23  ? 345  PRO A O     1 
ATOM   2670 C  CB    . PRO A 1 345 ? -16.724 -7.862  22.841  1.00 29.82  ? 345  PRO A CB    1 
ATOM   2671 C  CG    . PRO A 1 345 ? -16.576 -6.362  22.983  1.00 27.93  ? 345  PRO A CG    1 
ATOM   2672 C  CD    . PRO A 1 345 ? -15.098 -6.127  22.921  1.00 27.97  ? 345  PRO A CD    1 
ATOM   2673 N  N     . ASN A 1 346 ? -16.315 -7.290  19.697  1.00 22.93  ? 346  ASN A N     1 
ATOM   2674 C  CA    . ASN A 1 346 ? -16.879 -7.404  18.356  1.00 20.58  ? 346  ASN A CA    1 
ATOM   2675 C  C     . ASN A 1 346 ? -15.906 -8.092  17.407  1.00 22.58  ? 346  ASN A C     1 
ATOM   2676 O  O     . ASN A 1 346 ? -16.337 -8.717  16.433  1.00 25.95  ? 346  ASN A O     1 
ATOM   2677 C  CB    . ASN A 1 346 ? -17.291 -6.026  17.831  1.00 25.33  ? 346  ASN A CB    1 
ATOM   2678 C  CG    . ASN A 1 346 ? -18.597 -5.550  18.443  1.00 35.97  ? 346  ASN A CG    1 
ATOM   2679 O  OD1   . ASN A 1 346 ? -19.512 -6.350  18.645  1.00 25.75  ? 346  ASN A OD1   1 
ATOM   2680 N  ND2   . ASN A 1 346 ? -18.685 -4.257  18.766  1.00 22.60  ? 346  ASN A ND2   1 
ATOM   2681 N  N     . ALA A 1 347 ? -14.602 -8.011  17.691  1.00 20.08  ? 347  ALA A N     1 
ATOM   2682 C  CA    . ALA A 1 347 ? -13.620 -8.778  16.927  1.00 21.55  ? 347  ALA A CA    1 
ATOM   2683 C  C     . ALA A 1 347 ? -13.746 -10.267 17.218  1.00 23.99  ? 347  ALA A C     1 
ATOM   2684 O  O     . ALA A 1 347 ? -13.671 -11.089 16.300  1.00 20.60  ? 347  ALA A O     1 
ATOM   2685 C  CB    . ALA A 1 347 ? -12.204 -8.299  17.241  1.00 25.05  ? 347  ALA A CB    1 
ATOM   2686 N  N     . ILE A 1 348 ? -13.953 -10.623 18.490  1.00 23.41  ? 348  ILE A N     1 
ATOM   2687 C  CA    . ILE A 1 348 ? -14.117 -12.024 18.887  1.00 22.75  ? 348  ILE A CA    1 
ATOM   2688 C  C     . ILE A 1 348 ? -15.258 -12.674 18.112  1.00 26.72  ? 348  ILE A C     1 
ATOM   2689 O  O     . ILE A 1 348 ? -15.133 -13.800 17.605  1.00 31.08  ? 348  ILE A O     1 
ATOM   2690 C  CB    . ILE A 1 348 ? -14.343 -12.120 20.406  1.00 25.91  ? 348  ILE A CB    1 
ATOM   2691 C  CG1   . ILE A 1 348 ? -13.119 -11.586 21.155  1.00 27.64  ? 348  ILE A CG1   1 
ATOM   2692 C  CG2   . ILE A 1 348 ? -14.619 -13.556 20.816  1.00 35.39  ? 348  ILE A CG2   1 
ATOM   2693 C  CD1   . ILE A 1 348 ? -11.858 -12.347 20.887  1.00 29.26  ? 348  ILE A CD1   1 
ATOM   2694 N  N     . LYS A 1 349 ? -16.391 -11.982 18.020  1.00 24.28  ? 349  LYS A N     1 
ATOM   2695 C  CA    . LYS A 1 349 ? -17.535 -12.509 17.282  1.00 25.72  ? 349  LYS A CA    1 
ATOM   2696 C  C     . LYS A 1 349 ? -17.232 -12.672 15.801  1.00 28.36  ? 349  LYS A C     1 
ATOM   2697 O  O     . LYS A 1 349 ? -17.778 -13.566 15.149  1.00 35.02  ? 349  LYS A O     1 
ATOM   2698 C  CB    . LYS A 1 349 ? -18.743 -11.593 17.463  1.00 27.73  ? 349  LYS A CB    1 
ATOM   2699 C  CG    . LYS A 1 349 ? -19.227 -11.447 18.908  1.00 37.83  ? 349  LYS A CG    1 
ATOM   2700 C  CD    . LYS A 1 349 ? -20.407 -10.481 18.980  1.00 46.85  ? 349  LYS A CD    1 
ATOM   2701 C  CE    . LYS A 1 349 ? -20.984 -10.392 20.384  1.00 51.90  ? 349  LYS A CE    1 
ATOM   2702 N  NZ    . LYS A 1 349 ? -22.347 -9.782  20.385  1.00 61.91  ? 349  LYS A NZ    1 
ATOM   2703 N  N     . THR A 1 350 ? -16.365 -11.820 15.252  1.00 26.77  ? 350  THR A N     1 
ATOM   2704 C  CA    . THR A 1 350 ? -16.103 -11.806 13.822  1.00 22.85  ? 350  THR A CA    1 
ATOM   2705 C  C     . THR A 1 350 ? -15.207 -12.965 13.388  1.00 19.54  ? 350  THR A C     1 
ATOM   2706 O  O     . THR A 1 350 ? -15.380 -13.501 12.289  1.00 21.10  ? 350  THR A O     1 
ATOM   2707 C  CB    . THR A 1 350 ? -15.452 -10.469 13.440  1.00 21.97  ? 350  THR A CB    1 
ATOM   2708 O  OG1   . THR A 1 350 ? -16.266 -9.384  13.917  1.00 26.50  ? 350  THR A OG1   1 
ATOM   2709 C  CG2   . THR A 1 350 ? -15.290 -10.348 11.935  1.00 22.78  ? 350  THR A CG2   1 
ATOM   2710 N  N     . ILE A 1 351 ? -14.224 -13.337 14.211  1.00 16.92  ? 351  ILE A N     1 
ATOM   2711 C  CA    . ILE A 1 351 ? -13.112 -14.163 13.758  1.00 18.56  ? 351  ILE A CA    1 
ATOM   2712 C  C     . ILE A 1 351 ? -13.342 -15.653 14.008  1.00 24.20  ? 351  ILE A C     1 
ATOM   2713 O  O     . ILE A 1 351 ? -12.417 -16.452 13.842  1.00 22.16  ? 351  ILE A O     1 
ATOM   2714 C  CB    . ILE A 1 351 ? -11.794 -13.712 14.405  1.00 19.61  ? 351  ILE A CB    1 
ATOM   2715 C  CG1   . ILE A 1 351 ? -11.873 -13.825 15.928  1.00 20.02  ? 351  ILE A CG1   1 
ATOM   2716 C  CG2   . ILE A 1 351 ? -11.461 -12.277 13.972  1.00 18.57  ? 351  ILE A CG2   1 
ATOM   2717 C  CD1   . ILE A 1 351 ? -10.563 -13.446 16.638  1.00 23.33  ? 351  ILE A CD1   1 
ATOM   2718 N  N     . GLN A 1 352 ? -14.546 -16.051 14.380  1.00 26.01  ? 352  GLN A N     1 
ATOM   2719 C  CA    . GLN A 1 352 ? -14.786 -17.462 14.665  1.00 27.09  ? 352  GLN A CA    1 
ATOM   2720 C  C     . GLN A 1 352 ? -15.262 -18.252 13.457  1.00 28.38  ? 352  GLN A C     1 
ATOM   2721 O  O     . GLN A 1 352 ? -15.581 -19.438 13.595  1.00 33.42  ? 352  GLN A O     1 
ATOM   2722 C  CB    . GLN A 1 352 ? -15.790 -17.592 15.803  1.00 30.82  ? 352  GLN A CB    1 
ATOM   2723 C  CG    . GLN A 1 352 ? -15.288 -16.945 17.057  1.00 33.97  ? 352  GLN A CG    1 
ATOM   2724 C  CD    . GLN A 1 352 ? -16.115 -17.306 18.261  1.00 42.75  ? 352  GLN A CD    1 
ATOM   2725 O  OE1   . GLN A 1 352 ? -16.614 -18.424 18.373  1.00 51.47  ? 352  GLN A OE1   1 
ATOM   2726 N  NE2   . GLN A 1 352 ? -16.259 -16.364 19.177  1.00 45.81  ? 352  GLN A NE2   1 
ATOM   2727 N  N     . LYS A 1 353 ? -15.330 -17.637 12.285  1.00 23.16  ? 353  LYS A N     1 
ATOM   2728 C  CA    . LYS A 1 353 ? -15.541 -18.409 11.079  1.00 26.89  ? 353  LYS A CA    1 
ATOM   2729 C  C     . LYS A 1 353 ? -14.888 -17.706 9.901   1.00 30.23  ? 353  LYS A C     1 
ATOM   2730 O  O     . LYS A 1 353 ? -14.684 -16.484 9.912   1.00 25.27  ? 353  LYS A O     1 
ATOM   2731 C  CB    . LYS A 1 353 ? -17.026 -18.674 10.802  1.00 35.76  ? 353  LYS A CB    1 
ATOM   2732 C  CG    . LYS A 1 353 ? -17.910 -17.471 10.668  1.00 37.80  ? 353  LYS A CG    1 
ATOM   2733 C  CD    . LYS A 1 353 ? -19.375 -17.916 10.637  1.00 42.92  ? 353  LYS A CD    1 
ATOM   2734 C  CE    . LYS A 1 353 ? -20.330 -16.742 10.774  1.00 58.61  ? 353  LYS A CE    1 
ATOM   2735 N  NZ    . LYS A 1 353 ? -21.708 -17.205 11.123  1.00 68.82  ? 353  LYS A NZ    1 
ATOM   2736 N  N     . ASN A 1 354 ? -14.523 -18.513 8.902   1.00 23.92  ? 354  ASN A N     1 
ATOM   2737 C  CA    . ASN A 1 354 ? -14.020 -18.019 7.617   1.00 24.68  ? 354  ASN A CA    1 
ATOM   2738 C  C     . ASN A 1 354 ? -12.791 -17.127 7.777   1.00 20.58  ? 354  ASN A C     1 
ATOM   2739 O  O     . ASN A 1 354 ? -12.589 -16.185 7.008   1.00 21.29  ? 354  ASN A O     1 
ATOM   2740 C  CB    . ASN A 1 354 ? -15.117 -17.281 6.854   1.00 24.75  ? 354  ASN A CB    1 
ATOM   2741 C  CG    . ASN A 1 354 ? -16.362 -18.122 6.667   1.00 30.83  ? 354  ASN A CG    1 
ATOM   2742 O  OD1   . ASN A 1 354 ? -16.279 -19.303 6.325   1.00 32.23  ? 354  ASN A OD1   1 
ATOM   2743 N  ND2   . ASN A 1 354 ? -17.521 -17.519 6.886   1.00 32.69  ? 354  ASN A ND2   1 
ATOM   2744 N  N     . THR A 1 355 ? -11.930 -17.451 8.738   1.00 18.82  ? 355  THR A N     1 
ATOM   2745 C  CA    . THR A 1 355 ? -10.844 -16.551 9.118   1.00 18.61  ? 355  THR A CA    1 
ATOM   2746 C  C     . THR A 1 355 ? -9.509  -17.279 9.066   1.00 21.72  ? 355  THR A C     1 
ATOM   2747 O  O     . THR A 1 355 ? -9.404  -18.421 9.510   1.00 22.83  ? 355  THR A O     1 
ATOM   2748 C  CB    . THR A 1 355 ? -11.105 -15.987 10.524  1.00 21.33  ? 355  THR A CB    1 
ATOM   2749 O  OG1   . THR A 1 355 ? -12.243 -15.116 10.472  1.00 19.89  ? 355  THR A OG1   1 
ATOM   2750 C  CG2   . THR A 1 355 ? -9.895  -15.235 11.063  1.00 15.66  ? 355  THR A CG2   1 
ATOM   2751 N  N     . ILE A 1 356 ? -8.497  -16.637 8.485   1.00 20.82  ? 356  ILE A N     1 
ATOM   2752 C  CA    . ILE A 1 356 ? -7.139  -17.172 8.479   1.00 17.89  ? 356  ILE A CA    1 
ATOM   2753 C  C     . ILE A 1 356 ? -6.340  -16.471 9.565   1.00 18.12  ? 356  ILE A C     1 
ATOM   2754 O  O     . ILE A 1 356 ? -6.269  -15.242 9.591   1.00 19.23  ? 356  ILE A O     1 
ATOM   2755 C  CB    . ILE A 1 356 ? -6.467  -16.987 7.109   1.00 24.20  ? 356  ILE A CB    1 
ATOM   2756 C  CG1   . ILE A 1 356 ? -7.257  -17.727 6.028   1.00 25.92  ? 356  ILE A CG1   1 
ATOM   2757 C  CG2   . ILE A 1 356 ? -4.990  -17.482 7.149   1.00 21.55  ? 356  ILE A CG2   1 
ATOM   2758 C  CD1   . ILE A 1 356 ? -6.664  -17.580 4.642   1.00 30.44  ? 356  ILE A CD1   1 
ATOM   2759 N  N     . PHE A 1 357 ? -5.722  -17.243 10.442  1.00 16.52  ? 357  PHE A N     1 
ATOM   2760 C  CA    . PHE A 1 357 ? -4.837  -16.712 11.472  1.00 19.19  ? 357  PHE A CA    1 
ATOM   2761 C  C     . PHE A 1 357 ? -3.395  -16.978 11.064  1.00 23.31  ? 357  PHE A C     1 
ATOM   2762 O  O     . PHE A 1 357 ? -3.085  -18.053 10.547  1.00 23.08  ? 357  PHE A O     1 
ATOM   2763 C  CB    . PHE A 1 357 ? -5.101  -17.371 12.831  1.00 21.01  ? 357  PHE A CB    1 
ATOM   2764 C  CG    . PHE A 1 357 ? -6.488  -17.162 13.349  1.00 19.01  ? 357  PHE A CG    1 
ATOM   2765 C  CD1   . PHE A 1 357 ? -7.520  -17.992 12.951  1.00 19.91  ? 357  PHE A CD1   1 
ATOM   2766 C  CD2   . PHE A 1 357 ? -6.767  -16.112 14.213  1.00 22.20  ? 357  PHE A CD2   1 
ATOM   2767 C  CE1   . PHE A 1 357 ? -8.827  -17.795 13.435  1.00 21.49  ? 357  PHE A CE1   1 
ATOM   2768 C  CE2   . PHE A 1 357 ? -8.057  -15.915 14.704  1.00 19.90  ? 357  PHE A CE2   1 
ATOM   2769 C  CZ    . PHE A 1 357 ? -9.085  -16.752 14.304  1.00 21.10  ? 357  PHE A CZ    1 
ATOM   2770 N  N     . THR A 1 358 ? -2.509  -16.015 11.324  1.00 19.73  ? 358  THR A N     1 
ATOM   2771 C  CA    . THR A 1 358 ? -1.089  -16.171 11.026  1.00 22.40  ? 358  THR A CA    1 
ATOM   2772 C  C     . THR A 1 358 ? -0.276  -15.945 12.298  1.00 21.58  ? 358  THR A C     1 
ATOM   2773 O  O     . THR A 1 358 ? -0.345  -14.868 12.899  1.00 22.69  ? 358  THR A O     1 
ATOM   2774 C  CB    . THR A 1 358 ? -0.646  -15.209 9.912   1.00 18.54  ? 358  THR A CB    1 
ATOM   2775 O  OG1   . THR A 1 358 ? -1.459  -15.411 8.743   1.00 18.15  ? 358  THR A OG1   1 
ATOM   2776 C  CG2   . THR A 1 358 ? 0.797   -15.468 9.543   1.00 23.96  ? 358  THR A CG2   1 
ATOM   2777 N  N     . ASN A 1 359 ? 0.460   -16.977 12.722  1.00 21.27  ? 359  ASN A N     1 
ATOM   2778 C  CA    . ASN A 1 359 ? 1.460   -16.883 13.796  1.00 21.14  ? 359  ASN A CA    1 
ATOM   2779 C  C     . ASN A 1 359 ? 0.855   -16.724 15.193  1.00 23.79  ? 359  ASN A C     1 
ATOM   2780 O  O     . ASN A 1 359 ? 1.505   -16.184 16.092  1.00 26.59  ? 359  ASN A O     1 
ATOM   2781 C  CB    . ASN A 1 359 ? 2.468   -15.756 13.522  1.00 22.50  ? 359  ASN A CB    1 
ATOM   2782 C  CG    . ASN A 1 359 ? 3.471   -16.145 12.463  1.00 22.17  ? 359  ASN A CG    1 
ATOM   2783 O  OD1   . ASN A 1 359 ? 3.643   -17.332 12.184  1.00 23.07  ? 359  ASN A OD1   1 
ATOM   2784 N  ND2   . ASN A 1 359 ? 4.125   -15.164 11.862  1.00 24.60  ? 359  ASN A ND2   1 
ATOM   2785 N  N     . VAL A 1 360 ? -0.366  -17.193 15.420  1.00 21.69  ? 360  VAL A N     1 
ATOM   2786 C  CA    . VAL A 1 360 ? -0.895  -17.319 16.772  1.00 18.97  ? 360  VAL A CA    1 
ATOM   2787 C  C     . VAL A 1 360 ? -0.640  -18.741 17.262  1.00 26.28  ? 360  VAL A C     1 
ATOM   2788 O  O     . VAL A 1 360 ? -0.150  -19.597 16.528  1.00 23.02  ? 360  VAL A O     1 
ATOM   2789 C  CB    . VAL A 1 360 ? -2.407  -16.954 16.857  1.00 19.66  ? 360  VAL A CB    1 
ATOM   2790 C  CG1   . VAL A 1 360 ? -2.653  -15.532 16.351  1.00 21.97  ? 360  VAL A CG1   1 
ATOM   2791 C  CG2   . VAL A 1 360 ? -3.257  -17.974 16.091  1.00 21.21  ? 360  VAL A CG2   1 
ATOM   2792 N  N     . ALA A 1 361 ? -0.981  -19.004 18.524  1.00 26.23  ? 361  ALA A N     1 
ATOM   2793 C  CA    . ALA A 1 361 ? -0.829  -20.347 19.068  1.00 27.02  ? 361  ALA A CA    1 
ATOM   2794 C  C     . ALA A 1 361 ? -2.058  -21.189 18.768  1.00 24.77  ? 361  ALA A C     1 
ATOM   2795 O  O     . ALA A 1 361 ? -3.166  -20.675 18.589  1.00 23.58  ? 361  ALA A O     1 
ATOM   2796 C  CB    . ALA A 1 361 ? -0.597  -20.319 20.581  1.00 23.70  ? 361  ALA A CB    1 
ATOM   2797 N  N     . GLU A 1 362 ? -1.854  -22.504 18.731  1.00 26.36  ? 362  GLU A N     1 
ATOM   2798 C  CA    . GLU A 1 362 ? -2.942  -23.457 18.555  1.00 28.96  ? 362  GLU A CA    1 
ATOM   2799 C  C     . GLU A 1 362 ? -3.150  -24.243 19.845  1.00 28.04  ? 362  GLU A C     1 
ATOM   2800 O  O     . GLU A 1 362 ? -2.182  -24.714 20.452  1.00 30.03  ? 362  GLU A O     1 
ATOM   2801 C  CB    . GLU A 1 362 ? -2.651  -24.409 17.395  1.00 29.15  ? 362  GLU A CB    1 
ATOM   2802 C  CG    . GLU A 1 362 ? -3.807  -25.362 17.097  1.00 33.54  ? 362  GLU A CG    1 
ATOM   2803 C  CD    . GLU A 1 362 ? -3.472  -26.354 15.989  1.00 36.50  ? 362  GLU A CD    1 
ATOM   2804 O  OE1   . GLU A 1 362 ? -2.334  -26.323 15.484  1.00 34.98  ? 362  GLU A OE1   1 
ATOM   2805 O  OE2   . GLU A 1 362 ? -4.348  -27.160 15.620  1.00 37.52  ? 362  GLU A OE2   1 
ATOM   2806 N  N     . THR A 1 363 ? -4.400  -24.368 20.273  1.00 28.93  ? 363  THR A N     1 
ATOM   2807 C  CA    . THR A 1 363 ? -4.708  -25.228 21.406  1.00 29.46  ? 363  THR A CA    1 
ATOM   2808 C  C     . THR A 1 363 ? -5.017  -26.645 20.923  1.00 34.22  ? 363  THR A C     1 
ATOM   2809 O  O     . THR A 1 363 ? -5.486  -26.848 19.799  1.00 30.52  ? 363  THR A O     1 
ATOM   2810 C  CB    . THR A 1 363 ? -5.878  -24.676 22.214  1.00 27.61  ? 363  THR A CB    1 
ATOM   2811 O  OG1   . THR A 1 363 ? -7.056  -24.644 21.401  1.00 26.82  ? 363  THR A OG1   1 
ATOM   2812 C  CG2   . THR A 1 363 ? -5.560  -23.271 22.701  1.00 28.75  ? 363  THR A CG2   1 
ATOM   2813 N  N     . SER A 1 364 ? -4.761  -27.630 21.796  1.00 33.39  ? 364  SER A N     1 
ATOM   2814 C  CA    . SER A 1 364 ? -4.862  -29.031 21.388  1.00 36.63  ? 364  SER A CA    1 
ATOM   2815 C  C     . SER A 1 364 ? -6.270  -29.412 20.954  1.00 35.87  ? 364  SER A C     1 
ATOM   2816 O  O     . SER A 1 364 ? -6.436  -30.415 20.252  1.00 38.92  ? 364  SER A O     1 
ATOM   2817 C  CB    . SER A 1 364 ? -4.404  -29.957 22.519  1.00 32.31  ? 364  SER A CB    1 
ATOM   2818 O  OG    . SER A 1 364 ? -5.189  -29.755 23.676  1.00 31.94  ? 364  SER A OG    1 
ATOM   2819 N  N     . ASP A 1 365 ? -7.282  -28.633 21.328  1.00 31.52  ? 365  ASP A N     1 
ATOM   2820 C  CA    . ASP A 1 365 ? -8.643  -28.909 20.899  1.00 28.13  ? 365  ASP A CA    1 
ATOM   2821 C  C     . ASP A 1 365 ? -9.037  -28.124 19.654  1.00 29.32  ? 365  ASP A C     1 
ATOM   2822 O  O     . ASP A 1 365 ? -10.225 -28.045 19.333  1.00 27.48  ? 365  ASP A O     1 
ATOM   2823 C  CB    . ASP A 1 365 ? -9.632  -28.661 22.048  1.00 33.30  ? 365  ASP A CB    1 
ATOM   2824 C  CG    . ASP A 1 365 ? -9.643  -27.216 22.542  1.00 38.25  ? 365  ASP A CG    1 
ATOM   2825 O  OD1   . ASP A 1 365 ? -8.678  -26.463 22.296  1.00 31.51  ? 365  ASP A OD1   1 
ATOM   2826 O  OD2   . ASP A 1 365 ? -10.632 -26.841 23.207  1.00 34.99  ? 365  ASP A OD2   1 
ATOM   2827 N  N     . GLY A 1 366 ? -8.067  -27.568 18.931  1.00 28.79  ? 366  GLY A N     1 
ATOM   2828 C  CA    . GLY A 1 366 ? -8.337  -26.928 17.658  1.00 31.18  ? 366  GLY A CA    1 
ATOM   2829 C  C     . GLY A 1 366 ? -8.665  -25.457 17.716  1.00 34.55  ? 366  GLY A C     1 
ATOM   2830 O  O     . GLY A 1 366 ? -9.246  -24.931 16.760  1.00 29.87  ? 366  GLY A O     1 
ATOM   2831 N  N     . GLY A 1 367 ? -8.335  -24.775 18.813  1.00 26.63  ? 367  GLY A N     1 
ATOM   2832 C  CA    . GLY A 1 367 ? -8.585  -23.358 18.945  1.00 29.13  ? 367  GLY A CA    1 
ATOM   2833 C  C     . GLY A 1 367 ? -7.317  -22.536 18.796  1.00 25.77  ? 367  GLY A C     1 
ATOM   2834 O  O     . GLY A 1 367 ? -6.242  -23.040 18.475  1.00 23.83  ? 367  GLY A O     1 
ATOM   2835 N  N     . VAL A 1 368 ? -7.462  -21.238 19.049  1.00 24.84  ? 368  VAL A N     1 
ATOM   2836 C  CA    . VAL A 1 368 ? -6.368  -20.281 18.918  1.00 26.61  ? 368  VAL A CA    1 
ATOM   2837 C  C     . VAL A 1 368 ? -6.032  -19.743 20.296  1.00 27.67  ? 368  VAL A C     1 
ATOM   2838 O  O     . VAL A 1 368 ? -6.903  -19.616 21.160  1.00 27.22  ? 368  VAL A O     1 
ATOM   2839 C  CB    . VAL A 1 368 ? -6.716  -19.113 17.968  1.00 21.63  ? 368  VAL A CB    1 
ATOM   2840 C  CG1   . VAL A 1 368 ? -6.929  -19.624 16.549  1.00 24.16  ? 368  VAL A CG1   1 
ATOM   2841 C  CG2   . VAL A 1 368 ? -7.961  -18.392 18.454  1.00 23.27  ? 368  VAL A CG2   1 
ATOM   2842 N  N     . TYR A 1 369 ? -4.769  -19.382 20.492  1.00 25.07  ? 369  TYR A N     1 
ATOM   2843 C  CA    . TYR A 1 369 ? -4.395  -18.706 21.725  1.00 27.24  ? 369  TYR A CA    1 
ATOM   2844 C  C     . TYR A 1 369 ? -3.431  -17.568 21.422  1.00 22.59  ? 369  TYR A C     1 
ATOM   2845 O  O     . TYR A 1 369 ? -2.665  -17.620 20.455  1.00 25.20  ? 369  TYR A O     1 
ATOM   2846 C  CB    . TYR A 1 369 ? -3.776  -19.676 22.743  1.00 25.60  ? 369  TYR A CB    1 
ATOM   2847 C  CG    . TYR A 1 369 ? -4.209  -19.367 24.156  1.00 28.18  ? 369  TYR A CG    1 
ATOM   2848 C  CD1   . TYR A 1 369 ? -5.551  -19.428 24.506  1.00 28.00  ? 369  TYR A CD1   1 
ATOM   2849 C  CD2   . TYR A 1 369 ? -3.291  -18.999 25.133  1.00 29.46  ? 369  TYR A CD2   1 
ATOM   2850 C  CE1   . TYR A 1 369 ? -5.971  -19.148 25.785  1.00 34.82  ? 369  TYR A CE1   1 
ATOM   2851 C  CE2   . TYR A 1 369 ? -3.715  -18.706 26.436  1.00 31.28  ? 369  TYR A CE2   1 
ATOM   2852 C  CZ    . TYR A 1 369 ? -5.052  -18.785 26.747  1.00 35.89  ? 369  TYR A CZ    1 
ATOM   2853 O  OH    . TYR A 1 369 ? -5.498  -18.506 28.023  1.00 45.56  ? 369  TYR A OH    1 
ATOM   2854 N  N     . TRP A 1 370 ? -3.480  -16.536 22.260  1.00 24.94  ? 370  TRP A N     1 
ATOM   2855 C  CA    . TRP A 1 370 ? -2.473  -15.480 22.205  1.00 29.33  ? 370  TRP A CA    1 
ATOM   2856 C  C     . TRP A 1 370 ? -2.420  -14.764 23.543  1.00 28.64  ? 370  TRP A C     1 
ATOM   2857 O  O     . TRP A 1 370 ? -3.320  -14.894 24.379  1.00 26.78  ? 370  TRP A O     1 
ATOM   2858 C  CB    . TRP A 1 370 ? -2.742  -14.472 21.081  1.00 21.01  ? 370  TRP A CB    1 
ATOM   2859 C  CG    . TRP A 1 370 ? -4.137  -13.987 21.018  1.00 21.79  ? 370  TRP A CG    1 
ATOM   2860 C  CD1   . TRP A 1 370 ? -4.744  -13.099 21.863  1.00 19.84  ? 370  TRP A CD1   1 
ATOM   2861 C  CD2   . TRP A 1 370 ? -5.113  -14.335 20.036  1.00 18.97  ? 370  TRP A CD2   1 
ATOM   2862 N  NE1   . TRP A 1 370 ? -6.038  -12.887 21.473  1.00 17.87  ? 370  TRP A NE1   1 
ATOM   2863 C  CE2   . TRP A 1 370 ? -6.290  -13.633 20.351  1.00 16.48  ? 370  TRP A CE2   1 
ATOM   2864 C  CE3   . TRP A 1 370 ? -5.104  -15.179 18.919  1.00 19.23  ? 370  TRP A CE3   1 
ATOM   2865 C  CZ2   . TRP A 1 370 ? -7.455  -13.737 19.584  1.00 20.61  ? 370  TRP A CZ2   1 
ATOM   2866 C  CZ3   . TRP A 1 370 ? -6.255  -15.284 18.164  1.00 19.96  ? 370  TRP A CZ3   1 
ATOM   2867 C  CH2   . TRP A 1 370 ? -7.409  -14.561 18.492  1.00 17.85  ? 370  TRP A CH2   1 
ATOM   2868 N  N     . GLU A 1 371 ? -1.345  -14.003 23.726  1.00 32.16  ? 371  GLU A N     1 
ATOM   2869 C  CA    . GLU A 1 371 ? -1.215  -13.152 24.897  1.00 30.81  ? 371  GLU A CA    1 
ATOM   2870 C  C     . GLU A 1 371 ? -2.388  -12.181 24.979  1.00 29.21  ? 371  GLU A C     1 
ATOM   2871 O  O     . GLU A 1 371 ? -2.790  -11.580 23.978  1.00 30.99  ? 371  GLU A O     1 
ATOM   2872 C  CB    . GLU A 1 371 ? 0.112   -12.387 24.838  1.00 31.81  ? 371  GLU A CB    1 
ATOM   2873 C  CG    . GLU A 1 371 ? 1.328   -13.188 25.292  1.00 33.71  ? 371  GLU A CG    1 
ATOM   2874 C  CD    . GLU A 1 371 ? 1.596   -14.421 24.444  1.00 39.43  ? 371  GLU A CD    1 
ATOM   2875 O  OE1   . GLU A 1 371 ? 1.358   -14.379 23.214  1.00 34.59  ? 371  GLU A OE1   1 
ATOM   2876 O  OE2   . GLU A 1 371 ? 2.050   -15.435 25.016  1.00 39.54  ? 371  GLU A OE2   1 
ATOM   2877 N  N     . GLY A 1 372 ? -2.954  -12.043 26.179  1.00 31.79  ? 372  GLY A N     1 
ATOM   2878 C  CA    . GLY A 1 372 ? -4.019  -11.083 26.399  1.00 25.84  ? 372  GLY A CA    1 
ATOM   2879 C  C     . GLY A 1 372 ? -5.385  -11.551 25.969  1.00 26.96  ? 372  GLY A C     1 
ATOM   2880 O  O     . GLY A 1 372 ? -6.337  -10.768 26.011  1.00 30.46  ? 372  GLY A O     1 
ATOM   2881 N  N     . ILE A 1 373 ? -5.519  -12.809 25.554  1.00 25.88  ? 373  ILE A N     1 
ATOM   2882 C  CA    . ILE A 1 373 ? -6.827  -13.338 25.203  1.00 26.47  ? 373  ILE A CA    1 
ATOM   2883 C  C     . ILE A 1 373 ? -7.731  -13.425 26.428  1.00 27.89  ? 373  ILE A C     1 
ATOM   2884 O  O     . ILE A 1 373 ? -8.960  -13.423 26.293  1.00 23.46  ? 373  ILE A O     1 
ATOM   2885 C  CB    . ILE A 1 373 ? -6.635  -14.708 24.519  1.00 28.42  ? 373  ILE A CB    1 
ATOM   2886 C  CG1   . ILE A 1 373 ? -7.932  -15.196 23.871  1.00 27.95  ? 373  ILE A CG1   1 
ATOM   2887 C  CG2   . ILE A 1 373 ? -6.114  -15.730 25.523  1.00 27.39  ? 373  ILE A CG2   1 
ATOM   2888 C  CD1   . ILE A 1 373 ? -7.722  -16.439 22.997  1.00 26.97  ? 373  ILE A CD1   1 
ATOM   2889 N  N     . ASP A 1 374 ? -7.147  -13.495 27.625  1.00 27.70  ? 374  ASP A N     1 
ATOM   2890 C  CA    . ASP A 1 374 ? -7.890  -13.282 28.870  1.00 35.87  ? 374  ASP A CA    1 
ATOM   2891 C  C     . ASP A 1 374 ? -8.984  -14.328 29.047  1.00 33.92  ? 374  ASP A C     1 
ATOM   2892 O  O     . ASP A 1 374 ? -10.069 -14.055 29.557  1.00 37.44  ? 374  ASP A O     1 
ATOM   2893 C  CB    . ASP A 1 374 ? -8.470  -11.868 28.915  1.00 38.01  ? 374  ASP A CB    1 
ATOM   2894 C  CG    . ASP A 1 374 ? -8.800  -11.427 30.308  1.00 57.85  ? 374  ASP A CG    1 
ATOM   2895 O  OD1   . ASP A 1 374 ? -7.891  -11.463 31.165  1.00 66.54  ? 374  ASP A OD1   1 
ATOM   2896 O  OD2   . ASP A 1 374 ? -9.965  -11.044 30.548  1.00 68.52  ? 374  ASP A OD2   1 
ATOM   2897 N  N     . GLU A 1 375 ? -8.695  -15.526 28.626  1.00 36.38  ? 375  GLU A N     1 
ATOM   2898 C  CA    . GLU A 1 375 ? -9.704  -16.562 28.573  1.00 34.82  ? 375  GLU A CA    1 
ATOM   2899 C  C     . GLU A 1 375 ? -9.030  -17.862 28.977  1.00 35.38  ? 375  GLU A C     1 
ATOM   2900 O  O     . GLU A 1 375 ? -8.071  -18.294 28.322  1.00 34.41  ? 375  GLU A O     1 
ATOM   2901 C  CB    . GLU A 1 375 ? -10.309 -16.632 27.173  1.00 40.11  ? 375  GLU A CB    1 
ATOM   2902 C  CG    . GLU A 1 375 ? -11.410 -17.632 27.013  1.00 45.58  ? 375  GLU A CG    1 
ATOM   2903 C  CD    . GLU A 1 375 ? -12.244 -17.355 25.790  1.00 48.88  ? 375  GLU A CD    1 
ATOM   2904 O  OE1   . GLU A 1 375 ? -12.055 -16.287 25.164  1.00 44.45  ? 375  GLU A OE1   1 
ATOM   2905 O  OE2   . GLU A 1 375 ? -13.091 -18.205 25.460  1.00 47.49  ? 375  GLU A OE2   1 
ATOM   2906 N  N     . PRO A 1 376 ? -9.464  -18.480 30.072  1.00 36.74  ? 376  PRO A N     1 
ATOM   2907 C  CA    . PRO A 1 376 ? -8.788  -19.684 30.559  1.00 36.81  ? 376  PRO A CA    1 
ATOM   2908 C  C     . PRO A 1 376 ? -9.172  -20.913 29.752  1.00 33.83  ? 376  PRO A C     1 
ATOM   2909 O  O     . PRO A 1 376 ? -10.279 -21.026 29.221  1.00 37.67  ? 376  PRO A O     1 
ATOM   2910 C  CB    . PRO A 1 376 ? -9.275  -19.793 32.011  1.00 32.68  ? 376  PRO A CB    1 
ATOM   2911 C  CG    . PRO A 1 376 ? -10.640 -19.194 31.966  1.00 39.11  ? 376  PRO A CG    1 
ATOM   2912 C  CD    . PRO A 1 376 ? -10.529 -18.033 30.989  1.00 36.13  ? 376  PRO A CD    1 
ATOM   2913 N  N     . LEU A 1 377 ? -8.226  -21.837 29.661  1.00 40.07  ? 377  LEU A N     1 
ATOM   2914 C  CA    . LEU A 1 377 ? -8.436  -23.087 28.949  1.00 41.13  ? 377  LEU A CA    1 
ATOM   2915 C  C     . LEU A 1 377 ? -8.914  -24.185 29.902  1.00 41.30  ? 377  LEU A C     1 
ATOM   2916 O  O     . LEU A 1 377 ? -8.717  -24.118 31.116  1.00 37.82  ? 377  LEU A O     1 
ATOM   2917 C  CB    . LEU A 1 377 ? -7.149  -23.504 28.249  1.00 39.01  ? 377  LEU A CB    1 
ATOM   2918 C  CG    . LEU A 1 377 ? -6.706  -22.504 27.184  1.00 34.79  ? 377  LEU A CG    1 
ATOM   2919 C  CD1   . LEU A 1 377 ? -5.365  -22.899 26.607  1.00 31.67  ? 377  LEU A CD1   1 
ATOM   2920 C  CD2   . LEU A 1 377 ? -7.759  -22.421 26.092  1.00 35.97  ? 377  LEU A CD2   1 
ATOM   2921 N  N     . ALA A 1 378 ? -9.554  -25.200 29.331  1.00 43.06  ? 378  ALA A N     1 
ATOM   2922 C  CA    . ALA A 1 378 ? -10.061 -26.315 30.113  1.00 37.90  ? 378  ALA A CA    1 
ATOM   2923 C  C     . ALA A 1 378 ? -8.925  -27.254 30.507  1.00 38.00  ? 378  ALA A C     1 
ATOM   2924 O  O     . ALA A 1 378 ? -7.859  -27.249 29.884  1.00 34.14  ? 378  ALA A O     1 
ATOM   2925 C  CB    . ALA A 1 378 ? -11.121 -27.072 29.319  1.00 36.95  ? 378  ALA A CB    1 
ATOM   2926 N  N     . PRO A 1 379 ? -9.131  -28.073 31.543  1.00 46.91  ? 379  PRO A N     1 
ATOM   2927 C  CA    . PRO A 1 379 ? -8.104  -29.053 31.924  1.00 40.05  ? 379  PRO A CA    1 
ATOM   2928 C  C     . PRO A 1 379 ? -7.717  -29.949 30.761  1.00 31.16  ? 379  PRO A C     1 
ATOM   2929 O  O     . PRO A 1 379 ? -8.550  -30.320 29.929  1.00 34.41  ? 379  PRO A O     1 
ATOM   2930 C  CB    . PRO A 1 379 ? -8.781  -29.851 33.045  1.00 47.12  ? 379  PRO A CB    1 
ATOM   2931 C  CG    . PRO A 1 379 ? -9.747  -28.891 33.643  1.00 42.39  ? 379  PRO A CG    1 
ATOM   2932 C  CD    . PRO A 1 379 ? -10.258 -28.062 32.497  1.00 46.00  ? 379  PRO A CD    1 
ATOM   2933 N  N     . GLY A 1 380 ? -6.433  -30.291 30.701  1.00 27.75  ? 380  GLY A N     1 
ATOM   2934 C  CA    . GLY A 1 380 ? -5.944  -31.157 29.651  1.00 33.39  ? 380  GLY A CA    1 
ATOM   2935 C  C     . GLY A 1 380 ? -5.660  -30.478 28.325  1.00 38.22  ? 380  GLY A C     1 
ATOM   2936 O  O     . GLY A 1 380 ? -5.048  -31.101 27.448  1.00 32.12  ? 380  GLY A O     1 
ATOM   2937 N  N     . VAL A 1 381 ? -6.093  -29.235 28.138  1.00 37.60  ? 381  VAL A N     1 
ATOM   2938 C  CA    . VAL A 1 381 ? -5.795  -28.508 26.907  1.00 35.29  ? 381  VAL A CA    1 
ATOM   2939 C  C     . VAL A 1 381 ? -4.347  -28.041 26.960  1.00 29.58  ? 381  VAL A C     1 
ATOM   2940 O  O     . VAL A 1 381 ? -3.903  -27.468 27.960  1.00 32.77  ? 381  VAL A O     1 
ATOM   2941 C  CB    . VAL A 1 381 ? -6.765  -27.327 26.724  1.00 37.58  ? 381  VAL A CB    1 
ATOM   2942 C  CG1   . VAL A 1 381 ? -6.465  -26.571 25.434  1.00 37.32  ? 381  VAL A CG1   1 
ATOM   2943 C  CG2   . VAL A 1 381 ? -8.208  -27.821 26.717  1.00 31.40  ? 381  VAL A CG2   1 
ATOM   2944 N  N     . THR A 1 382 ? -3.600  -28.312 25.899  1.00 31.73  ? 382  THR A N     1 
ATOM   2945 C  CA    . THR A 1 382 ? -2.222  -27.864 25.771  1.00 35.72  ? 382  THR A CA    1 
ATOM   2946 C  C     . THR A 1 382 ? -2.130  -26.809 24.671  1.00 33.67  ? 382  THR A C     1 
ATOM   2947 O  O     . THR A 1 382 ? -3.071  -26.593 23.905  1.00 32.76  ? 382  THR A O     1 
ATOM   2948 C  CB    . THR A 1 382 ? -1.285  -29.040 25.466  1.00 32.05  ? 382  THR A CB    1 
ATOM   2949 O  OG1   . THR A 1 382 ? -1.790  -29.773 24.345  1.00 39.92  ? 382  THR A OG1   1 
ATOM   2950 C  CG2   . THR A 1 382 ? -1.170  -29.965 26.670  1.00 43.33  ? 382  THR A CG2   1 
ATOM   2951 N  N     . ILE A 1 383 ? -0.979  -26.150 24.598  1.00 33.42  ? 383  ILE A N     1 
ATOM   2952 C  CA    . ILE A 1 383 ? -0.754  -25.048 23.667  1.00 33.34  ? 383  ILE A CA    1 
ATOM   2953 C  C     . ILE A 1 383 ? 0.470   -25.362 22.820  1.00 37.00  ? 383  ILE A C     1 
ATOM   2954 O  O     . ILE A 1 383 ? 1.512   -25.765 23.352  1.00 45.57  ? 383  ILE A O     1 
ATOM   2955 C  CB    . ILE A 1 383 ? -0.569  -23.712 24.408  1.00 39.74  ? 383  ILE A CB    1 
ATOM   2956 C  CG1   . ILE A 1 383 ? -1.853  -23.336 25.146  1.00 36.48  ? 383  ILE A CG1   1 
ATOM   2957 C  CG2   . ILE A 1 383 ? -0.139  -22.612 23.439  1.00 30.60  ? 383  ILE A CG2   1 
ATOM   2958 C  CD1   . ILE A 1 383 ? -1.715  -22.105 26.023  1.00 41.13  ? 383  ILE A CD1   1 
ATOM   2959 N  N     . THR A 1 384 ? 0.342   -25.190 21.507  1.00 32.75  ? 384  THR A N     1 
ATOM   2960 C  CA    . THR A 1 384 ? 1.488   -25.161 20.602  1.00 35.14  ? 384  THR A CA    1 
ATOM   2961 C  C     . THR A 1 384 ? 1.736   -23.720 20.180  1.00 31.59  ? 384  THR A C     1 
ATOM   2962 O  O     . THR A 1 384 ? 0.835   -23.070 19.639  1.00 32.46  ? 384  THR A O     1 
ATOM   2963 C  CB    . THR A 1 384 ? 1.261   -26.026 19.367  1.00 33.01  ? 384  THR A CB    1 
ATOM   2964 O  OG1   . THR A 1 384 ? 0.995   -27.370 19.771  1.00 40.63  ? 384  THR A OG1   1 
ATOM   2965 C  CG2   . THR A 1 384 ? 2.501   -25.993 18.486  1.00 34.63  ? 384  THR A CG2   1 
ATOM   2966 N  N     . SER A 1 385 ? 2.949   -23.231 20.424  1.00 33.26  ? 385  SER A N     1 
ATOM   2967 C  CA    . SER A 1 385 ? 3.285   -21.849 20.126  1.00 36.43  ? 385  SER A CA    1 
ATOM   2968 C  C     . SER A 1 385 ? 3.380   -21.637 18.616  1.00 32.73  ? 385  SER A C     1 
ATOM   2969 O  O     . SER A 1 385 ? 3.383   -22.580 17.827  1.00 29.38  ? 385  SER A O     1 
ATOM   2970 C  CB    . SER A 1 385 ? 4.606   -21.466 20.791  1.00 36.83  ? 385  SER A CB    1 
ATOM   2971 O  OG    . SER A 1 385 ? 5.698   -22.078 20.127  1.00 38.13  ? 385  SER A OG    1 
ATOM   2972 N  N     . TRP A 1 386 ? 3.479   -20.369 18.215  1.00 33.98  ? 386  TRP A N     1 
ATOM   2973 C  CA    . TRP A 1 386 ? 3.638   -20.067 16.798  1.00 32.07  ? 386  TRP A CA    1 
ATOM   2974 C  C     . TRP A 1 386 ? 4.948   -20.605 16.224  1.00 38.69  ? 386  TRP A C     1 
ATOM   2975 O  O     . TRP A 1 386 ? 5.111   -20.618 14.997  1.00 37.05  ? 386  TRP A O     1 
ATOM   2976 C  CB    . TRP A 1 386 ? 3.550   -18.561 16.580  1.00 32.91  ? 386  TRP A CB    1 
ATOM   2977 C  CG    . TRP A 1 386 ? 4.759   -17.841 17.034  1.00 29.80  ? 386  TRP A CG    1 
ATOM   2978 C  CD1   . TRP A 1 386 ? 5.109   -17.554 18.321  1.00 31.71  ? 386  TRP A CD1   1 
ATOM   2979 C  CD2   . TRP A 1 386 ? 5.797   -17.313 16.204  1.00 35.03  ? 386  TRP A CD2   1 
ATOM   2980 N  NE1   . TRP A 1 386 ? 6.307   -16.884 18.345  1.00 35.33  ? 386  TRP A NE1   1 
ATOM   2981 C  CE2   . TRP A 1 386 ? 6.751   -16.723 17.056  1.00 37.16  ? 386  TRP A CE2   1 
ATOM   2982 C  CE3   . TRP A 1 386 ? 6.017   -17.291 14.823  1.00 33.94  ? 386  TRP A CE3   1 
ATOM   2983 C  CZ2   . TRP A 1 386 ? 7.902   -16.108 16.573  1.00 34.00  ? 386  TRP A CZ2   1 
ATOM   2984 C  CZ3   . TRP A 1 386 ? 7.161   -16.682 14.344  1.00 35.78  ? 386  TRP A CZ3   1 
ATOM   2985 C  CH2   . TRP A 1 386 ? 8.087   -16.093 15.218  1.00 36.88  ? 386  TRP A CH2   1 
ATOM   2986 N  N     . LYS A 1 387 ? 5.884   -21.040 17.067  1.00 36.86  ? 387  LYS A N     1 
ATOM   2987 C  CA    . LYS A 1 387 ? 7.109   -21.685 16.609  1.00 40.23  ? 387  LYS A CA    1 
ATOM   2988 C  C     . LYS A 1 387 ? 6.947   -23.189 16.440  1.00 43.90  ? 387  LYS A C     1 
ATOM   2989 O  O     . LYS A 1 387 ? 7.948   -23.887 16.244  1.00 50.40  ? 387  LYS A O     1 
ATOM   2990 C  CB    . LYS A 1 387 ? 8.257   -21.407 17.581  1.00 43.68  ? 387  LYS A CB    1 
ATOM   2991 C  CG    . LYS A 1 387 ? 8.749   -19.979 17.602  1.00 39.80  ? 387  LYS A CG    1 
ATOM   2992 C  CD    . LYS A 1 387 ? 9.584   -19.736 18.855  1.00 46.94  ? 387  LYS A CD    1 
ATOM   2993 C  CE    . LYS A 1 387 ? 10.203  -18.347 18.871  1.00 53.56  ? 387  LYS A CE    1 
ATOM   2994 N  NZ    . LYS A 1 387 ? 11.357  -18.239 17.925  1.00 56.01  ? 387  LYS A NZ    1 
ATOM   2995 N  N     . ASN A 1 388 ? 5.716   -23.697 16.528  1.00 42.01  ? 388  ASN A N     1 
ATOM   2996 C  CA    . ASN A 1 388 ? 5.420   -25.117 16.350  1.00 44.18  ? 388  ASN A CA    1 
ATOM   2997 C  C     . ASN A 1 388 ? 6.100   -25.957 17.429  1.00 51.80  ? 388  ASN A C     1 
ATOM   2998 O  O     . ASN A 1 388 ? 6.666   -27.016 17.154  1.00 55.00  ? 388  ASN A O     1 
ATOM   2999 C  CB    . ASN A 1 388 ? 5.812   -25.594 14.950  1.00 44.26  ? 388  ASN A CB    1 
ATOM   3000 C  CG    . ASN A 1 388 ? 4.875   -26.643 14.416  1.00 50.12  ? 388  ASN A CG    1 
ATOM   3001 O  OD1   . ASN A 1 388 ? 3.696   -26.664 14.758  1.00 46.80  ? 388  ASN A OD1   1 
ATOM   3002 N  ND2   . ASN A 1 388 ? 5.394   -27.529 13.574  1.00 63.59  ? 388  ASN A ND2   1 
ATOM   3003 N  N     . LYS A 1 389 ? 6.041   -25.471 18.668  1.00 44.73  ? 389  LYS A N     1 
ATOM   3004 C  CA    . LYS A 1 389 ? 6.652   -26.117 19.818  1.00 48.24  ? 389  LYS A CA    1 
ATOM   3005 C  C     . LYS A 1 389 ? 5.644   -26.162 20.953  1.00 51.82  ? 389  LYS A C     1 
ATOM   3006 O  O     . LYS A 1 389 ? 4.737   -25.328 21.028  1.00 45.48  ? 389  LYS A O     1 
ATOM   3007 C  CB    . LYS A 1 389 ? 7.909   -25.372 20.301  1.00 49.05  ? 389  LYS A CB    1 
ATOM   3008 C  CG    . LYS A 1 389 ? 9.033   -25.277 19.283  1.00 60.79  ? 389  LYS A CG    1 
ATOM   3009 C  CD    . LYS A 1 389 ? 10.200  -24.463 19.834  1.00 60.90  ? 389  LYS A CD    1 
ATOM   3010 C  CE    . LYS A 1 389 ? 11.319  -24.334 18.815  1.00 62.44  ? 389  LYS A CE    1 
ATOM   3011 N  NZ    . LYS A 1 389 ? 12.441  -23.506 19.340  1.00 73.51  ? 389  LYS A NZ    1 
ATOM   3012 N  N     . GLU A 1 390 ? 5.806   -27.149 21.832  1.00 55.61  ? 390  GLU A N     1 
ATOM   3013 C  CA    . GLU A 1 390 ? 5.012   -27.189 23.050  1.00 53.83  ? 390  GLU A CA    1 
ATOM   3014 C  C     . GLU A 1 390 ? 5.361   -25.996 23.928  1.00 55.26  ? 390  GLU A C     1 
ATOM   3015 O  O     . GLU A 1 390 ? 6.532   -25.646 24.097  1.00 56.94  ? 390  GLU A O     1 
ATOM   3016 C  CB    . GLU A 1 390 ? 5.251   -28.496 23.801  1.00 58.44  ? 390  GLU A CB    1 
ATOM   3017 C  CG    . GLU A 1 390 ? 4.380   -29.633 23.318  1.00 65.31  ? 390  GLU A CG    1 
ATOM   3018 C  CD    . GLU A 1 390 ? 2.962   -29.541 23.856  1.00 71.56  ? 390  GLU A CD    1 
ATOM   3019 O  OE1   . GLU A 1 390 ? 2.749   -29.913 25.031  1.00 64.86  ? 390  GLU A OE1   1 
ATOM   3020 O  OE2   . GLU A 1 390 ? 2.063   -29.092 23.108  1.00 68.44  ? 390  GLU A OE2   1 
ATOM   3021 N  N     . TRP A 1 391 ? 4.333   -25.361 24.481  1.00 54.27  ? 391  TRP A N     1 
ATOM   3022 C  CA    . TRP A 1 391 ? 4.494   -24.097 25.185  1.00 58.06  ? 391  TRP A CA    1 
ATOM   3023 C  C     . TRP A 1 391 ? 3.765   -24.174 26.517  1.00 63.11  ? 391  TRP A C     1 
ATOM   3024 O  O     . TRP A 1 391 ? 2.564   -24.462 26.555  1.00 53.04  ? 391  TRP A O     1 
ATOM   3025 C  CB    . TRP A 1 391 ? 3.960   -22.939 24.333  1.00 53.59  ? 391  TRP A CB    1 
ATOM   3026 C  CG    . TRP A 1 391 ? 4.073   -21.585 24.961  1.00 52.02  ? 391  TRP A CG    1 
ATOM   3027 C  CD1   . TRP A 1 391 ? 5.082   -20.682 24.786  1.00 52.21  ? 391  TRP A CD1   1 
ATOM   3028 C  CD2   . TRP A 1 391 ? 3.131   -20.970 25.845  1.00 54.20  ? 391  TRP A CD2   1 
ATOM   3029 N  NE1   . TRP A 1 391 ? 4.830   -19.548 25.514  1.00 49.97  ? 391  TRP A NE1   1 
ATOM   3030 C  CE2   . TRP A 1 391 ? 3.638   -19.699 26.174  1.00 51.74  ? 391  TRP A CE2   1 
ATOM   3031 C  CE3   . TRP A 1 391 ? 1.908   -21.374 26.394  1.00 56.63  ? 391  TRP A CE3   1 
ATOM   3032 C  CZ2   . TRP A 1 391 ? 2.968   -18.829 27.029  1.00 56.60  ? 391  TRP A CZ2   1 
ATOM   3033 C  CZ3   . TRP A 1 391 ? 1.243   -20.509 27.242  1.00 55.50  ? 391  TRP A CZ3   1 
ATOM   3034 C  CH2   . TRP A 1 391 ? 1.774   -19.251 27.553  1.00 58.19  ? 391  TRP A CH2   1 
ATOM   3035 N  N     . ARG A 1 392 ? 4.493   -23.936 27.602  1.00 70.58  ? 392  ARG A N     1 
ATOM   3036 C  CA    . ARG A 1 392 ? 3.891   -23.703 28.902  1.00 76.21  ? 392  ARG A CA    1 
ATOM   3037 C  C     . ARG A 1 392 ? 4.070   -22.241 29.295  1.00 82.31  ? 392  ARG A C     1 
ATOM   3038 O  O     . ARG A 1 392 ? 5.045   -21.601 28.888  1.00 81.32  ? 392  ARG A O     1 
ATOM   3039 C  CB    . ARG A 1 392 ? 4.508   -24.595 29.987  1.00 81.18  ? 392  ARG A CB    1 
ATOM   3040 C  CG    . ARG A 1 392 ? 3.954   -26.011 30.033  1.00 81.06  ? 392  ARG A CG    1 
ATOM   3041 C  CD    . ARG A 1 392 ? 4.422   -26.739 31.285  1.00 82.83  ? 392  ARG A CD    1 
ATOM   3042 N  NE    . ARG A 1 392 ? 5.833   -27.100 31.212  1.00 89.16  ? 392  ARG A NE    1 
ATOM   3043 C  CZ    . ARG A 1 392 ? 6.543   -27.558 32.234  1.00 95.33  ? 392  ARG A CZ    1 
ATOM   3044 N  NH1   . ARG A 1 392 ? 6.015   -27.688 33.441  1.00 91.68  ? 392  ARG A NH1   1 
ATOM   3045 N  NH2   . ARG A 1 392 ? 7.816   -27.895 32.042  1.00 94.37  ? 392  ARG A NH2   1 
ATOM   3046 N  N     . PRO A 1 393 ? 3.150   -21.677 30.091  1.00 84.66  ? 393  PRO A N     1 
ATOM   3047 C  CA    . PRO A 1 393 ? 3.340   -20.301 30.577  1.00 87.29  ? 393  PRO A CA    1 
ATOM   3048 C  C     . PRO A 1 393 ? 4.557   -20.141 31.480  1.00 102.61 ? 393  PRO A C     1 
ATOM   3049 O  O     . PRO A 1 393 ? 4.718   -19.106 32.133  1.00 105.56 ? 393  PRO A O     1 
ATOM   3050 C  CB    . PRO A 1 393 ? 2.038   -20.016 31.339  1.00 81.70  ? 393  PRO A CB    1 
ATOM   3051 C  CG    . PRO A 1 393 ? 1.033   -20.932 30.720  1.00 76.52  ? 393  PRO A CG    1 
ATOM   3052 C  CD    . PRO A 1 393 ? 1.798   -22.184 30.386  1.00 82.70  ? 393  PRO A CD    1 
ATOM   3053 N  N     . GLN A 1 394 ? 5.415   -21.160 31.526  1.00 117.76 ? 394  GLN A N     1 
ATOM   3054 C  CA    . GLN A 1 394 ? 6.671   -21.107 32.259  1.00 124.96 ? 394  GLN A CA    1 
ATOM   3055 C  C     . GLN A 1 394 ? 7.849   -20.689 31.388  1.00 125.28 ? 394  GLN A C     1 
ATOM   3056 O  O     . GLN A 1 394 ? 8.914   -20.369 31.927  1.00 133.02 ? 394  GLN A O     1 
ATOM   3057 C  CB    . GLN A 1 394 ? 6.963   -22.467 32.907  1.00 127.14 ? 394  GLN A CB    1 
ATOM   3058 C  CG    . GLN A 1 394 ? 6.229   -22.705 34.225  1.00 134.35 ? 394  GLN A CG    1 
ATOM   3059 C  CD    . GLN A 1 394 ? 4.717   -22.669 34.080  1.00 128.02 ? 394  GLN A CD    1 
ATOM   3060 O  OE1   . GLN A 1 394 ? 4.162   -23.198 33.117  1.00 122.71 ? 394  GLN A OE1   1 
ATOM   3061 N  NE2   . GLN A 1 394 ? 4.045   -22.036 35.036  1.00 131.62 ? 394  GLN A NE2   1 
ATOM   3062 N  N     . ASP A 1 395 ? 7.691   -20.688 30.068  1.00 115.25 ? 395  ASP A N     1 
ATOM   3063 C  CA    . ASP A 1 395 ? 8.721   -20.137 29.204  1.00 121.91 ? 395  ASP A CA    1 
ATOM   3064 C  C     . ASP A 1 395 ? 8.731   -18.613 29.313  1.00 125.07 ? 395  ASP A C     1 
ATOM   3065 O  O     . ASP A 1 395 ? 7.805   -17.991 29.841  1.00 124.02 ? 395  ASP A O     1 
ATOM   3066 C  CB    . ASP A 1 395 ? 8.496   -20.567 27.754  1.00 111.05 ? 395  ASP A CB    1 
ATOM   3067 C  CG    . ASP A 1 395 ? 8.487   -22.072 27.588  1.00 111.00 ? 395  ASP A CG    1 
ATOM   3068 O  OD1   . ASP A 1 395 ? 9.205   -22.757 28.347  1.00 121.39 ? 395  ASP A OD1   1 
ATOM   3069 O  OD2   . ASP A 1 395 ? 7.764   -22.570 26.698  1.00 94.27  ? 395  ASP A OD2   1 
ATOM   3070 N  N     . GLU A 1 396 ? 9.802   -18.008 28.810  1.00 140.69 ? 396  GLU A N     1 
ATOM   3071 C  CA    . GLU A 1 396 ? 9.887   -16.554 28.798  1.00 141.09 ? 396  GLU A CA    1 
ATOM   3072 C  C     . GLU A 1 396 ? 9.217   -15.947 27.574  1.00 140.48 ? 396  GLU A C     1 
ATOM   3073 O  O     . GLU A 1 396 ? 8.744   -14.805 27.635  1.00 140.26 ? 396  GLU A O     1 
ATOM   3074 C  CB    . GLU A 1 396 ? 11.351  -16.108 28.857  1.00 142.77 ? 396  GLU A CB    1 
ATOM   3075 C  CG    . GLU A 1 396 ? 11.544  -14.609 29.076  1.00 143.73 ? 396  GLU A CG    1 
ATOM   3076 C  CD    . GLU A 1 396 ? 12.941  -14.134 28.712  1.00 143.71 ? 396  GLU A CD    1 
ATOM   3077 O  OE1   . GLU A 1 396 ? 13.733  -14.947 28.190  1.00 144.24 ? 396  GLU A OE1   1 
ATOM   3078 O  OE2   . GLU A 1 396 ? 13.245  -12.943 28.943  1.00 143.32 ? 396  GLU A OE2   1 
ATOM   3079 N  N     . GLU A 1 397 ? 9.146   -16.703 26.459  1.00 95.30  ? 397  GLU A N     1 
ATOM   3080 C  CA    . GLU A 1 397 ? 8.681   -16.218 25.170  1.00 72.62  ? 397  GLU A CA    1 
ATOM   3081 C  C     . GLU A 1 397 ? 7.166   -16.336 25.047  1.00 58.93  ? 397  GLU A C     1 
ATOM   3082 O  O     . GLU A 1 397 ? 6.554   -17.229 25.640  1.00 53.26  ? 397  GLU A O     1 
ATOM   3083 C  CB    . GLU A 1 397 ? 9.343   -17.000 24.042  1.00 65.60  ? 397  GLU A CB    1 
ATOM   3084 C  CG    . GLU A 1 397 ? 9.147   -18.497 24.134  1.00 65.94  ? 397  GLU A CG    1 
ATOM   3085 C  CD    . GLU A 1 397 ? 9.746   -19.221 22.952  1.00 62.38  ? 397  GLU A CD    1 
ATOM   3086 O  OE1   . GLU A 1 397 ? 10.365  -18.545 22.104  1.00 63.00  ? 397  GLU A OE1   1 
ATOM   3087 O  OE2   . GLU A 1 397 ? 9.596   -20.459 22.868  1.00 72.23  ? 397  GLU A OE2   1 
ATOM   3088 N  N     . PRO A 1 398 ? 6.540   -15.446 24.282  1.00 53.95  ? 398  PRO A N     1 
ATOM   3089 C  CA    . PRO A 1 398 ? 5.092   -15.536 24.084  1.00 44.04  ? 398  PRO A CA    1 
ATOM   3090 C  C     . PRO A 1 398 ? 4.730   -16.707 23.187  1.00 40.66  ? 398  PRO A C     1 
ATOM   3091 O  O     . PRO A 1 398 ? 5.536   -17.197 22.397  1.00 38.81  ? 398  PRO A O     1 
ATOM   3092 C  CB    . PRO A 1 398 ? 4.744   -14.203 23.420  1.00 40.38  ? 398  PRO A CB    1 
ATOM   3093 C  CG    . PRO A 1 398 ? 5.996   -13.822 22.697  1.00 48.61  ? 398  PRO A CG    1 
ATOM   3094 C  CD    . PRO A 1 398 ? 7.122   -14.289 23.579  1.00 53.49  ? 398  PRO A CD    1 
ATOM   3095 N  N     . CYS A 1 399 ? 3.485   -17.160 23.323  1.00 38.45  ? 399  CYS A N     1 
ATOM   3096 C  CA    . CYS A 1 399 ? 3.002   -18.261 22.499  1.00 39.56  ? 399  CYS A CA    1 
ATOM   3097 C  C     . CYS A 1 399 ? 2.586   -17.807 21.105  1.00 34.03  ? 399  CYS A C     1 
ATOM   3098 O  O     . CYS A 1 399 ? 2.489   -18.643 20.202  1.00 30.25  ? 399  CYS A O     1 
ATOM   3099 C  CB    . CYS A 1 399 ? 1.831   -18.973 23.194  1.00 36.28  ? 399  CYS A CB    1 
ATOM   3100 S  SG    . CYS A 1 399 ? 0.348   -17.959 23.476  1.00 35.42  ? 399  CYS A SG    1 
ATOM   3101 N  N     . ALA A 1 400 ? 2.334   -16.512 20.912  1.00 32.32  ? 400  ALA A N     1 
ATOM   3102 C  CA    . ALA A 1 400 ? 1.977   -15.958 19.613  1.00 27.93  ? 400  ALA A CA    1 
ATOM   3103 C  C     . ALA A 1 400 ? 2.931   -14.823 19.290  1.00 34.61  ? 400  ALA A C     1 
ATOM   3104 O  O     . ALA A 1 400 ? 3.336   -14.079 20.188  1.00 36.76  ? 400  ALA A O     1 
ATOM   3105 C  CB    . ALA A 1 400 ? 0.527   -15.445 19.600  1.00 25.29  ? 400  ALA A CB    1 
ATOM   3106 N  N     . HIS A 1 401 ? 3.298   -14.686 18.017  1.00 29.40  ? 401  HIS A N     1 
ATOM   3107 C  CA    . HIS A 1 401 ? 4.157   -13.568 17.654  1.00 26.26  ? 401  HIS A CA    1 
ATOM   3108 C  C     . HIS A 1 401 ? 3.439   -12.246 17.938  1.00 27.98  ? 401  HIS A C     1 
ATOM   3109 O  O     . HIS A 1 401 ? 2.219   -12.150 17.747  1.00 25.28  ? 401  HIS A O     1 
ATOM   3110 C  CB    . HIS A 1 401 ? 4.569   -13.630 16.189  1.00 27.03  ? 401  HIS A CB    1 
ATOM   3111 C  CG    . HIS A 1 401 ? 5.616   -12.624 15.841  1.00 28.01  ? 401  HIS A CG    1 
ATOM   3112 N  ND1   . HIS A 1 401 ? 5.313   -11.317 15.535  1.00 26.71  ? 401  HIS A ND1   1 
ATOM   3113 C  CD2   . HIS A 1 401 ? 6.966   -12.715 15.814  1.00 29.27  ? 401  HIS A CD2   1 
ATOM   3114 C  CE1   . HIS A 1 401 ? 6.430   -10.650 15.304  1.00 28.40  ? 401  HIS A CE1   1 
ATOM   3115 N  NE2   . HIS A 1 401 ? 7.448   -11.477 15.467  1.00 26.75  ? 401  HIS A NE2   1 
ATOM   3116 N  N     . PRO A 1 402 ? 4.156   -11.214 18.405  1.00 33.02  ? 402  PRO A N     1 
ATOM   3117 C  CA    . PRO A 1 402 ? 3.482   -9.941  18.723  1.00 26.51  ? 402  PRO A CA    1 
ATOM   3118 C  C     . PRO A 1 402 ? 2.760   -9.309  17.543  1.00 27.16  ? 402  PRO A C     1 
ATOM   3119 O  O     . PRO A 1 402 ? 1.759   -8.606  17.742  1.00 26.63  ? 402  PRO A O     1 
ATOM   3120 C  CB    . PRO A 1 402 ? 4.629   -9.049  19.218  1.00 30.15  ? 402  PRO A CB    1 
ATOM   3121 C  CG    . PRO A 1 402 ? 5.676   -9.988  19.685  1.00 31.24  ? 402  PRO A CG    1 
ATOM   3122 C  CD    . PRO A 1 402 ? 5.578   -11.200 18.801  1.00 29.65  ? 402  PRO A CD    1 
ATOM   3123 N  N     . ASN A 1 403 ? 3.227   -9.526  16.319  1.00 23.89  ? 403  ASN A N     1 
ATOM   3124 C  CA    . ASN A 1 403 ? 2.549   -8.999  15.144  1.00 29.01  ? 403  ASN A CA    1 
ATOM   3125 C  C     . ASN A 1 403 ? 1.703   -10.064 14.458  1.00 29.29  ? 403  ASN A C     1 
ATOM   3126 O  O     . ASN A 1 403 ? 1.416   -9.946  13.263  1.00 22.91  ? 403  ASN A O     1 
ATOM   3127 C  CB    . ASN A 1 403 ? 3.565   -8.403  14.160  1.00 25.41  ? 403  ASN A CB    1 
ATOM   3128 C  CG    . ASN A 1 403 ? 2.907   -7.576  13.052  1.00 29.48  ? 403  ASN A CG    1 
ATOM   3129 O  OD1   . ASN A 1 403 ? 2.039   -6.729  13.306  1.00 26.13  ? 403  ASN A OD1   1 
ATOM   3130 N  ND2   . ASN A 1 403 ? 3.318   -7.827  11.813  1.00 27.57  ? 403  ASN A ND2   1 
ATOM   3131 N  N     . SER A 1 404 ? 1.303   -11.110 15.184  1.00 21.53  ? 404  SER A N     1 
ATOM   3132 C  CA    . SER A 1 404 ? 0.421   -12.091 14.582  1.00 24.67  ? 404  SER A CA    1 
ATOM   3133 C  C     . SER A 1 404 ? -0.932  -11.457 14.292  1.00 17.71  ? 404  SER A C     1 
ATOM   3134 O  O     . SER A 1 404 ? -1.334  -10.458 14.902  1.00 23.06  ? 404  SER A O     1 
ATOM   3135 C  CB    . SER A 1 404 ? 0.258   -13.315 15.483  1.00 21.37  ? 404  SER A CB    1 
ATOM   3136 O  OG    . SER A 1 404 ? -0.164  -12.913 16.769  1.00 25.18  ? 404  SER A OG    1 
ATOM   3137 N  N     . ARG A 1 405 ? -1.628  -12.031 13.319  1.00 20.51  ? 405  ARG A N     1 
ATOM   3138 C  CA    . ARG A 1 405 ? -2.755  -11.357 12.695  1.00 19.19  ? 405  ARG A CA    1 
ATOM   3139 C  C     . ARG A 1 405 ? -3.886  -12.342 12.487  1.00 19.21  ? 405  ARG A C     1 
ATOM   3140 O  O     . ARG A 1 405 ? -3.656  -13.536 12.310  1.00 19.46  ? 405  ARG A O     1 
ATOM   3141 C  CB    . ARG A 1 405 ? -2.361  -10.765 11.328  1.00 18.78  ? 405  ARG A CB    1 
ATOM   3142 C  CG    . ARG A 1 405 ? -1.261  -9.708  11.384  1.00 21.55  ? 405  ARG A CG    1 
ATOM   3143 C  CD    . ARG A 1 405 ? -1.871  -8.319  11.601  1.00 19.25  ? 405  ARG A CD    1 
ATOM   3144 N  NE    . ARG A 1 405 ? -0.888  -7.260  11.817  1.00 20.62  ? 405  ARG A NE    1 
ATOM   3145 C  CZ    . ARG A 1 405 ? -1.196  -5.968  11.857  1.00 21.88  ? 405  ARG A CZ    1 
ATOM   3146 N  NH1   . ARG A 1 405 ? -2.411  -5.539  11.567  1.00 18.58  ? 405  ARG A NH1   1 
ATOM   3147 N  NH2   . ARG A 1 405 ? -0.267  -5.089  12.215  1.00 18.49  ? 405  ARG A NH2   1 
ATOM   3148 N  N     . PHE A 1 406 ? -5.107  -11.826 12.482  1.00 19.18  ? 406  PHE A N     1 
ATOM   3149 C  CA    . PHE A 1 406 ? -6.223  -12.534 11.886  1.00 21.33  ? 406  PHE A CA    1 
ATOM   3150 C  C     . PHE A 1 406 ? -6.584  -11.852 10.577  1.00 20.80  ? 406  PHE A C     1 
ATOM   3151 O  O     . PHE A 1 406 ? -6.302  -10.672 10.380  1.00 20.15  ? 406  PHE A O     1 
ATOM   3152 C  CB    . PHE A 1 406 ? -7.445  -12.590 12.818  1.00 15.69  ? 406  PHE A CB    1 
ATOM   3153 C  CG    . PHE A 1 406 ? -7.904  -11.241 13.354  1.00 18.30  ? 406  PHE A CG    1 
ATOM   3154 C  CD1   . PHE A 1 406 ? -8.720  -10.414 12.603  1.00 16.08  ? 406  PHE A CD1   1 
ATOM   3155 C  CD2   . PHE A 1 406 ? -7.547  -10.835 14.631  1.00 16.06  ? 406  PHE A CD2   1 
ATOM   3156 C  CE1   . PHE A 1 406 ? -9.163  -9.199  13.115  1.00 18.81  ? 406  PHE A CE1   1 
ATOM   3157 C  CE2   . PHE A 1 406 ? -7.989  -9.639  15.150  1.00 20.18  ? 406  PHE A CE2   1 
ATOM   3158 C  CZ    . PHE A 1 406 ? -8.794  -8.812  14.392  1.00 20.96  ? 406  PHE A CZ    1 
ATOM   3159 N  N     . CYS A 1 407 ? -7.197  -12.608 9.677   1.00 16.51  ? 407  CYS A N     1 
ATOM   3160 C  CA    . CYS A 1 407 ? -7.580  -12.088 8.372   1.00 18.67  ? 407  CYS A CA    1 
ATOM   3161 C  C     . CYS A 1 407 ? -9.019  -12.517 8.145   1.00 20.42  ? 407  CYS A C     1 
ATOM   3162 O  O     . CYS A 1 407 ? -9.285  -13.704 7.939   1.00 18.40  ? 407  CYS A O     1 
ATOM   3163 C  CB    . CYS A 1 407 ? -6.650  -12.623 7.274   1.00 20.23  ? 407  CYS A CB    1 
ATOM   3164 S  SG    . CYS A 1 407 ? -6.955  -11.940 5.658   1.00 21.41  ? 407  CYS A SG    1 
ATOM   3165 N  N     . THR A 1 408 ? -9.950  -11.565 8.193   1.00 19.34  ? 408  THR A N     1 
ATOM   3166 C  CA    . THR A 1 408 ? -11.334 -11.950 8.354   1.00 18.45  ? 408  THR A CA    1 
ATOM   3167 C  C     . THR A 1 408 ? -12.239 -11.095 7.468   1.00 19.77  ? 408  THR A C     1 
ATOM   3168 O  O     . THR A 1 408 ? -11.945 -9.913  7.238   1.00 24.21  ? 408  THR A O     1 
ATOM   3169 C  CB    . THR A 1 408 ? -11.711 -11.826 9.852   1.00 19.58  ? 408  THR A CB    1 
ATOM   3170 O  OG1   . THR A 1 408 ? -12.906 -12.558 10.132  1.00 18.44  ? 408  THR A OG1   1 
ATOM   3171 C  CG2   . THR A 1 408 ? -11.913 -10.382 10.271  1.00 15.43  ? 408  THR A CG2   1 
ATOM   3172 N  N     . PRO A 1 409 ? -13.313 -11.671 6.926   1.00 21.03  ? 409  PRO A N     1 
ATOM   3173 C  CA    . PRO A 1 409 ? -14.229 -10.898 6.067   1.00 19.34  ? 409  PRO A CA    1 
ATOM   3174 C  C     . PRO A 1 409 ? -14.941 -9.794  6.843   1.00 23.11  ? 409  PRO A C     1 
ATOM   3175 O  O     . PRO A 1 409 ? -15.473 -10.029 7.932   1.00 19.30  ? 409  PRO A O     1 
ATOM   3176 C  CB    . PRO A 1 409 ? -15.226 -11.954 5.570   1.00 24.29  ? 409  PRO A CB    1 
ATOM   3177 C  CG    . PRO A 1 409 ? -14.535 -13.264 5.760   1.00 22.43  ? 409  PRO A CG    1 
ATOM   3178 C  CD    . PRO A 1 409 ? -13.666 -13.101 6.972   1.00 21.54  ? 409  PRO A CD    1 
ATOM   3179 N  N     . ALA A 1 410 ? -14.969 -8.588  6.260   1.00 18.93  ? 410  ALA A N     1 
ATOM   3180 C  CA    . ALA A 1 410 ? -15.626 -7.457  6.926   1.00 23.41  ? 410  ALA A CA    1 
ATOM   3181 C  C     . ALA A 1 410 ? -17.126 -7.661  7.057   1.00 25.29  ? 410  ALA A C     1 
ATOM   3182 O  O     . ALA A 1 410 ? -17.727 -7.204  8.038   1.00 24.41  ? 410  ALA A O     1 
ATOM   3183 C  CB    . ALA A 1 410 ? -15.367 -6.147  6.181   1.00 22.22  ? 410  ALA A CB    1 
ATOM   3184 N  N     . SER A 1 411 ? -17.750 -8.322  6.080   1.00 27.44  ? 411  SER A N     1 
ATOM   3185 C  CA    . SER A 1 411 ? -19.201 -8.484  6.121   1.00 30.28  ? 411  SER A CA    1 
ATOM   3186 C  C     . SER A 1 411 ? -19.658 -9.315  7.316   1.00 30.67  ? 411  SER A C     1 
ATOM   3187 O  O     . SER A 1 411 ? -20.832 -9.242  7.695   1.00 31.60  ? 411  SER A O     1 
ATOM   3188 C  CB    . SER A 1 411 ? -19.694 -9.117  4.821   1.00 32.43  ? 411  SER A CB    1 
ATOM   3189 O  OG    . SER A 1 411 ? -19.205 -10.438 4.699   1.00 32.30  ? 411  SER A OG    1 
ATOM   3190 N  N     . GLN A 1 412 ? -18.755 -10.070 7.942   1.00 30.45  ? 412  GLN A N     1 
ATOM   3191 C  CA    . GLN A 1 412 ? -19.094 -10.864 9.114   1.00 33.66  ? 412  GLN A CA    1 
ATOM   3192 C  C     . GLN A 1 412 ? -19.127 -10.065 10.401  1.00 31.43  ? 412  GLN A C     1 
ATOM   3193 O  O     . GLN A 1 412 ? -19.605 -10.587 11.407  1.00 30.22  ? 412  GLN A O     1 
ATOM   3194 C  CB    . GLN A 1 412 ? -18.095 -11.999 9.285   1.00 26.75  ? 412  GLN A CB    1 
ATOM   3195 C  CG    . GLN A 1 412 ? -18.233 -13.038 8.224   1.00 33.23  ? 412  GLN A CG    1 
ATOM   3196 C  CD    . GLN A 1 412 ? -17.233 -14.146 8.383   1.00 24.74  ? 412  GLN A CD    1 
ATOM   3197 O  OE1   . GLN A 1 412 ? -17.194 -15.064 7.573   1.00 35.11  ? 412  GLN A OE1   1 
ATOM   3198 N  NE2   . GLN A 1 412 ? -16.406 -14.067 9.429   1.00 27.29  ? 412  GLN A NE2   1 
ATOM   3199 N  N     . CYS A 1 413 ? -18.605 -8.843  10.407  1.00 28.45  ? 413  CYS A N     1 
ATOM   3200 C  CA    . CYS A 1 413 ? -18.570 -8.064  11.633  1.00 25.92  ? 413  CYS A CA    1 
ATOM   3201 C  C     . CYS A 1 413 ? -19.997 -7.746  12.074  1.00 26.07  ? 413  CYS A C     1 
ATOM   3202 O  O     . CYS A 1 413 ? -20.783 -7.232  11.268  1.00 24.16  ? 413  CYS A O     1 
ATOM   3203 C  CB    . CYS A 1 413 ? -17.781 -6.765  11.414  1.00 25.81  ? 413  CYS A CB    1 
ATOM   3204 S  SG    . CYS A 1 413 ? -17.469 -5.839  12.916  1.00 28.10  ? 413  CYS A SG    1 
ATOM   3205 N  N     . PRO A 1 414 ? -20.373 -8.036  13.324  1.00 28.15  ? 414  PRO A N     1 
ATOM   3206 C  CA    . PRO A 1 414 ? -21.761 -7.769  13.742  1.00 23.79  ? 414  PRO A CA    1 
ATOM   3207 C  C     . PRO A 1 414 ? -22.123 -6.298  13.743  1.00 25.57  ? 414  PRO A C     1 
ATOM   3208 O  O     . PRO A 1 414 ? -23.318 -5.979  13.685  1.00 22.89  ? 414  PRO A O     1 
ATOM   3209 C  CB    . PRO A 1 414 ? -21.829 -8.363  15.157  1.00 30.84  ? 414  PRO A CB    1 
ATOM   3210 C  CG    . PRO A 1 414 ? -20.407 -8.438  15.616  1.00 30.00  ? 414  PRO A CG    1 
ATOM   3211 C  CD    . PRO A 1 414 ? -19.598 -8.703  14.386  1.00 25.21  ? 414  PRO A CD    1 
ATOM   3212 N  N     . ILE A 1 415 ? -21.148 -5.391  13.778  1.00 23.79  ? 415  ILE A N     1 
ATOM   3213 C  CA    . ILE A 1 415 ? -21.430 -3.960  13.781  1.00 24.19  ? 415  ILE A CA    1 
ATOM   3214 C  C     . ILE A 1 415 ? -20.936 -3.282  12.502  1.00 26.84  ? 415  ILE A C     1 
ATOM   3215 O  O     . ILE A 1 415 ? -20.734 -2.081  12.485  1.00 21.50  ? 415  ILE A O     1 
ATOM   3216 C  CB    . ILE A 1 415 ? -20.831 -3.288  15.030  1.00 26.75  ? 415  ILE A CB    1 
ATOM   3217 C  CG1   . ILE A 1 415 ? -19.335 -3.607  15.118  1.00 31.73  ? 415  ILE A CG1   1 
ATOM   3218 C  CG2   . ILE A 1 415 ? -21.565 -3.756  16.281  1.00 26.29  ? 415  ILE A CG2   1 
ATOM   3219 C  CD1   . ILE A 1 415 ? -18.569 -2.729  16.061  1.00 32.59  ? 415  ILE A CD1   1 
ATOM   3220 N  N     . ILE A 1 416 ? -20.739 -4.043  11.422  1.00 22.62  ? 416  ILE A N     1 
ATOM   3221 C  CA    . ILE A 1 416 ? -20.367 -3.421  10.159  1.00 22.02  ? 416  ILE A CA    1 
ATOM   3222 C  C     . ILE A 1 416 ? -21.453 -2.422  9.774   1.00 28.81  ? 416  ILE A C     1 
ATOM   3223 O  O     . ILE A 1 416 ? -22.654 -2.684  9.927   1.00 25.23  ? 416  ILE A O     1 
ATOM   3224 C  CB    . ILE A 1 416 ? -20.124 -4.485  9.070   1.00 26.16  ? 416  ILE A CB    1 
ATOM   3225 C  CG1   . ILE A 1 416 ? -19.205 -3.931  7.976   1.00 25.88  ? 416  ILE A CG1   1 
ATOM   3226 C  CG2   . ILE A 1 416 ? -21.422 -4.985  8.450   1.00 28.95  ? 416  ILE A CG2   1 
ATOM   3227 C  CD1   . ILE A 1 416 ? -17.776 -3.717  8.459   1.00 25.42  ? 416  ILE A CD1   1 
ATOM   3228 N  N     . ASP A 1 417 ? -21.023 -1.245  9.326   1.00 23.05  ? 417  ASP A N     1 
ATOM   3229 C  CA    . ASP A 1 417 ? -21.944 -0.151  9.048   1.00 24.22  ? 417  ASP A CA    1 
ATOM   3230 C  C     . ASP A 1 417 ? -22.775 -0.468  7.808   1.00 26.18  ? 417  ASP A C     1 
ATOM   3231 O  O     . ASP A 1 417 ? -22.261 -1.060  6.852   1.00 24.31  ? 417  ASP A O     1 
ATOM   3232 C  CB    . ASP A 1 417 ? -21.172 1.162   8.819   1.00 22.71  ? 417  ASP A CB    1 
ATOM   3233 C  CG    . ASP A 1 417 ? -22.067 2.386   8.894   1.00 23.32  ? 417  ASP A CG    1 
ATOM   3234 O  OD1   . ASP A 1 417 ? -22.262 2.901   10.005  1.00 25.88  ? 417  ASP A OD1   1 
ATOM   3235 O  OD2   . ASP A 1 417 ? -22.613 2.802   7.858   1.00 24.69  ? 417  ASP A OD2   1 
ATOM   3236 N  N     . PRO A 1 418 ? -24.048 -0.072  7.783   1.00 27.59  ? 418  PRO A N     1 
ATOM   3237 C  CA    . PRO A 1 418 ? -24.872 -0.346  6.595   1.00 28.90  ? 418  PRO A CA    1 
ATOM   3238 C  C     . PRO A 1 418 ? -24.396 0.357   5.339   1.00 33.43  ? 418  PRO A C     1 
ATOM   3239 O  O     . PRO A 1 418 ? -24.767 -0.064  4.238   1.00 36.60  ? 418  PRO A O     1 
ATOM   3240 C  CB    . PRO A 1 418 ? -26.275 0.131   7.016   1.00 33.51  ? 418  PRO A CB    1 
ATOM   3241 C  CG    . PRO A 1 418 ? -26.053 1.014   8.203   1.00 33.90  ? 418  PRO A CG    1 
ATOM   3242 C  CD    . PRO A 1 418 ? -24.853 0.454   8.901   1.00 30.14  ? 418  PRO A CD    1 
ATOM   3243 N  N     . ALA A 1 419 ? -23.583 1.409   5.454   1.00 31.72  ? 419  ALA A N     1 
ATOM   3244 C  CA    . ALA A 1 419 ? -23.069 2.108   4.286   1.00 31.03  ? 419  ALA A CA    1 
ATOM   3245 C  C     . ALA A 1 419 ? -21.617 1.754   3.979   1.00 33.01  ? 419  ALA A C     1 
ATOM   3246 O  O     . ALA A 1 419 ? -20.964 2.481   3.221   1.00 33.14  ? 419  ALA A O     1 
ATOM   3247 C  CB    . ALA A 1 419 ? -23.202 3.624   4.465   1.00 25.24  ? 419  ALA A CB    1 
ATOM   3248 N  N     . TRP A 1 420 ? -21.088 0.661   4.551   1.00 28.08  ? 420  TRP A N     1 
ATOM   3249 C  CA    . TRP A 1 420 ? -19.667 0.369   4.347   1.00 33.69  ? 420  TRP A CA    1 
ATOM   3250 C  C     . TRP A 1 420 ? -19.332 -0.004  2.905   1.00 36.99  ? 420  TRP A C     1 
ATOM   3251 O  O     . TRP A 1 420 ? -18.163 0.105   2.516   1.00 30.18  ? 420  TRP A O     1 
ATOM   3252 C  CB    . TRP A 1 420 ? -19.181 -0.732  5.296   1.00 30.19  ? 420  TRP A CB    1 
ATOM   3253 C  CG    . TRP A 1 420 ? -19.446 -2.129  4.834   1.00 31.90  ? 420  TRP A CG    1 
ATOM   3254 C  CD1   . TRP A 1 420 ? -20.611 -2.821  4.962   1.00 31.98  ? 420  TRP A CD1   1 
ATOM   3255 C  CD2   . TRP A 1 420 ? -18.514 -3.023  4.195   1.00 33.65  ? 420  TRP A CD2   1 
ATOM   3256 N  NE1   . TRP A 1 420 ? -20.471 -4.083  4.432   1.00 28.53  ? 420  TRP A NE1   1 
ATOM   3257 C  CE2   . TRP A 1 420 ? -19.195 -4.234  3.960   1.00 32.29  ? 420  TRP A CE2   1 
ATOM   3258 C  CE3   . TRP A 1 420 ? -17.174 -2.913  3.796   1.00 31.41  ? 420  TRP A CE3   1 
ATOM   3259 C  CZ2   . TRP A 1 420 ? -18.588 -5.329  3.331   1.00 32.62  ? 420  TRP A CZ2   1 
ATOM   3260 C  CZ3   . TRP A 1 420 ? -16.571 -4.004  3.171   1.00 29.24  ? 420  TRP A CZ3   1 
ATOM   3261 C  CH2   . TRP A 1 420 ? -17.281 -5.193  2.947   1.00 29.48  ? 420  TRP A CH2   1 
ATOM   3262 N  N     . GLU A 1 421 ? -20.311 -0.416  2.095   1.00 34.96  ? 421  GLU A N     1 
ATOM   3263 C  CA    . GLU A 1 421 ? -20.077 -0.664  0.672   1.00 37.20  ? 421  GLU A CA    1 
ATOM   3264 C  C     . GLU A 1 421 ? -20.740 0.368   -0.222  1.00 42.02  ? 421  GLU A C     1 
ATOM   3265 O  O     . GLU A 1 421 ? -20.760 0.189   -1.445  1.00 44.11  ? 421  GLU A O     1 
ATOM   3266 C  CB    . GLU A 1 421 ? -20.573 -2.050  0.258   1.00 38.99  ? 421  GLU A CB    1 
ATOM   3267 C  CG    . GLU A 1 421 ? -19.994 -3.168  1.043   1.00 37.53  ? 421  GLU A CG    1 
ATOM   3268 C  CD    . GLU A 1 421 ? -20.229 -4.522  0.400   1.00 43.09  ? 421  GLU A CD    1 
ATOM   3269 O  OE1   . GLU A 1 421 ? -19.549 -4.839  -0.600  1.00 46.37  ? 421  GLU A OE1   1 
ATOM   3270 O  OE2   . GLU A 1 421 ? -21.095 -5.266  0.897   1.00 40.03  ? 421  GLU A OE2   1 
ATOM   3271 N  N     . SER A 1 422 ? -21.302 1.422   0.345   1.00 35.57  ? 422  SER A N     1 
ATOM   3272 C  CA    . SER A 1 422 ? -21.964 2.421   -0.476  1.00 40.97  ? 422  SER A CA    1 
ATOM   3273 C  C     . SER A 1 422 ? -20.928 3.104   -1.352  1.00 40.43  ? 422  SER A C     1 
ATOM   3274 O  O     . SER A 1 422 ? -19.922 3.604   -0.830  1.00 39.23  ? 422  SER A O     1 
ATOM   3275 C  CB    . SER A 1 422 ? -22.690 3.441   0.390   1.00 43.77  ? 422  SER A CB    1 
ATOM   3276 O  OG    . SER A 1 422 ? -23.608 2.786   1.252   1.00 51.79  ? 422  SER A OG    1 
ATOM   3277 N  N     . PRO A 1 423 ? -21.118 3.144   -2.671  1.00 46.65  ? 423  PRO A N     1 
ATOM   3278 C  CA    . PRO A 1 423 ? -20.091 3.739   -3.536  1.00 50.33  ? 423  PRO A CA    1 
ATOM   3279 C  C     . PRO A 1 423 ? -19.937 5.238   -3.353  1.00 46.64  ? 423  PRO A C     1 
ATOM   3280 O  O     . PRO A 1 423 ? -18.928 5.790   -3.805  1.00 49.57  ? 423  PRO A O     1 
ATOM   3281 C  CB    . PRO A 1 423 ? -20.576 3.389   -4.950  1.00 50.25  ? 423  PRO A CB    1 
ATOM   3282 C  CG    . PRO A 1 423 ? -22.060 3.232   -4.803  1.00 50.55  ? 423  PRO A CG    1 
ATOM   3283 C  CD    . PRO A 1 423 ? -22.274 2.641   -3.434  1.00 46.73  ? 423  PRO A CD    1 
ATOM   3284 N  N     . GLU A 1 424 ? -20.880 5.916   -2.694  1.00 42.86  ? 424  GLU A N     1 
ATOM   3285 C  CA    . GLU A 1 424 ? -20.775 7.362   -2.523  1.00 44.83  ? 424  GLU A CA    1 
ATOM   3286 C  C     . GLU A 1 424 ? -20.049 7.769   -1.244  1.00 39.02  ? 424  GLU A C     1 
ATOM   3287 O  O     . GLU A 1 424 ? -19.758 8.955   -1.067  1.00 38.08  ? 424  GLU A O     1 
ATOM   3288 C  CB    . GLU A 1 424 ? -22.165 8.010   -2.559  1.00 37.66  ? 424  GLU A CB    1 
ATOM   3289 C  CG    . GLU A 1 424 ? -22.927 7.986   -1.240  1.00 48.91  ? 424  GLU A CG    1 
ATOM   3290 C  CD    . GLU A 1 424 ? -23.562 6.641   -0.939  1.00 57.42  ? 424  GLU A CD    1 
ATOM   3291 O  OE1   . GLU A 1 424 ? -23.553 5.754   -1.827  1.00 57.89  ? 424  GLU A OE1   1 
ATOM   3292 O  OE2   . GLU A 1 424 ? -24.073 6.474   0.193   1.00 66.98  ? 424  GLU A OE2   1 
ATOM   3293 N  N     . GLY A 1 425 ? -19.738 6.826   -0.359  1.00 34.04  ? 425  GLY A N     1 
ATOM   3294 C  CA    . GLY A 1 425 ? -18.971 7.138   0.826   1.00 27.56  ? 425  GLY A CA    1 
ATOM   3295 C  C     . GLY A 1 425 ? -19.832 7.681   1.948   1.00 28.68  ? 425  GLY A C     1 
ATOM   3296 O  O     . GLY A 1 425 ? -21.033 7.897   1.814   1.00 31.98  ? 425  GLY A O     1 
ATOM   3297 N  N     . VAL A 1 426 ? -19.193 7.888   3.092   1.00 23.56  ? 426  VAL A N     1 
ATOM   3298 C  CA    . VAL A 1 426 ? -19.875 8.448   4.252   1.00 25.16  ? 426  VAL A CA    1 
ATOM   3299 C  C     . VAL A 1 426 ? -19.308 9.840   4.510   1.00 29.31  ? 426  VAL A C     1 
ATOM   3300 O  O     . VAL A 1 426 ? -18.110 10.076  4.296   1.00 23.74  ? 426  VAL A O     1 
ATOM   3301 C  CB    . VAL A 1 426 ? -19.736 7.534   5.477   1.00 24.35  ? 426  VAL A CB    1 
ATOM   3302 C  CG1   . VAL A 1 426 ? -20.519 6.252   5.255   1.00 25.77  ? 426  VAL A CG1   1 
ATOM   3303 C  CG2   . VAL A 1 426 ? -18.277 7.225   5.748   1.00 23.82  ? 426  VAL A CG2   1 
ATOM   3304 N  N     . PRO A 1 427 ? -20.129 10.792  4.951   1.00 27.99  ? 427  PRO A N     1 
ATOM   3305 C  CA    . PRO A 1 427 ? -19.629 12.151  5.189   1.00 28.15  ? 427  PRO A CA    1 
ATOM   3306 C  C     . PRO A 1 427 ? -18.878 12.212  6.513   1.00 26.79  ? 427  PRO A C     1 
ATOM   3307 O  O     . PRO A 1 427 ? -19.404 11.832  7.564   1.00 24.83  ? 427  PRO A O     1 
ATOM   3308 C  CB    . PRO A 1 427 ? -20.907 12.997  5.217   1.00 30.19  ? 427  PRO A CB    1 
ATOM   3309 C  CG    . PRO A 1 427 ? -21.970 12.035  5.710   1.00 28.68  ? 427  PRO A CG    1 
ATOM   3310 C  CD    . PRO A 1 427 ? -21.570 10.658  5.246   1.00 27.22  ? 427  PRO A CD    1 
ATOM   3311 N  N     . ILE A 1 428 ? -17.640 12.689  6.453   1.00 20.18  ? 428  ILE A N     1 
ATOM   3312 C  CA    . ILE A 1 428 ? -16.757 12.724  7.613   1.00 18.80  ? 428  ILE A CA    1 
ATOM   3313 C  C     . ILE A 1 428 ? -16.900 14.083  8.271   1.00 19.61  ? 428  ILE A C     1 
ATOM   3314 O  O     . ILE A 1 428 ? -16.736 15.117  7.610   1.00 25.40  ? 428  ILE A O     1 
ATOM   3315 C  CB    . ILE A 1 428 ? -15.297 12.469  7.197   1.00 16.60  ? 428  ILE A CB    1 
ATOM   3316 C  CG1   . ILE A 1 428 ? -15.139 11.072  6.598   1.00 19.57  ? 428  ILE A CG1   1 
ATOM   3317 C  CG2   . ILE A 1 428 ? -14.342 12.693  8.390   1.00 18.56  ? 428  ILE A CG2   1 
ATOM   3318 C  CD1   . ILE A 1 428 ? -15.439 9.902   7.609   1.00 16.79  ? 428  ILE A CD1   1 
ATOM   3319 N  N     . GLU A 1 429 ? -17.198 14.091  9.572   1.00 15.97  ? 429  GLU A N     1 
ATOM   3320 C  CA    . GLU A 1 429 ? -17.364 15.330  10.310  1.00 17.01  ? 429  GLU A CA    1 
ATOM   3321 C  C     . GLU A 1 429 ? -16.270 15.563  11.338  1.00 19.76  ? 429  GLU A C     1 
ATOM   3322 O  O     . GLU A 1 429 ? -16.205 16.654  11.917  1.00 20.84  ? 429  GLU A O     1 
ATOM   3323 C  CB    . GLU A 1 429 ? -18.734 15.354  11.009  1.00 21.09  ? 429  GLU A CB    1 
ATOM   3324 C  CG    . GLU A 1 429 ? -19.884 15.470  10.030  1.00 24.87  ? 429  GLU A CG    1 
ATOM   3325 C  CD    . GLU A 1 429 ? -21.226 15.494  10.719  1.00 29.69  ? 429  GLU A CD    1 
ATOM   3326 O  OE1   . GLU A 1 429 ? -21.455 16.413  11.535  1.00 28.52  ? 429  GLU A OE1   1 
ATOM   3327 O  OE2   . GLU A 1 429 ? -22.043 14.591  10.449  1.00 25.71  ? 429  GLU A OE2   1 
ATOM   3328 N  N     . GLY A 1 430 ? -15.424 14.578  11.587  1.00 17.14  ? 430  GLY A N     1 
ATOM   3329 C  CA    . GLY A 1 430 ? -14.313 14.779  12.491  1.00 18.44  ? 430  GLY A CA    1 
ATOM   3330 C  C     . GLY A 1 430 ? -13.165 13.867  12.129  1.00 21.21  ? 430  GLY A C     1 
ATOM   3331 O  O     . GLY A 1 430 ? -13.382 12.741  11.675  1.00 21.00  ? 430  GLY A O     1 
ATOM   3332 N  N     . ILE A 1 431 ? -11.941 14.354  12.304  1.00 15.58  ? 431  ILE A N     1 
ATOM   3333 C  CA    . ILE A 1 431 ? -10.733 13.583  12.057  1.00 17.13  ? 431  ILE A CA    1 
ATOM   3334 C  C     . ILE A 1 431 ? -9.959  13.549  13.362  1.00 17.88  ? 431  ILE A C     1 
ATOM   3335 O  O     . ILE A 1 431 ? -9.785  14.588  14.007  1.00 20.40  ? 431  ILE A O     1 
ATOM   3336 C  CB    . ILE A 1 431 ? -9.888  14.197  10.927  1.00 18.88  ? 431  ILE A CB    1 
ATOM   3337 C  CG1   . ILE A 1 431 ? -10.612 14.056  9.583   1.00 21.95  ? 431  ILE A CG1   1 
ATOM   3338 C  CG2   . ILE A 1 431 ? -8.517  13.543  10.881  1.00 20.81  ? 431  ILE A CG2   1 
ATOM   3339 C  CD1   . ILE A 1 431 ? -9.927  14.820  8.416   1.00 27.92  ? 431  ILE A CD1   1 
ATOM   3340 N  N     . ILE A 1 432 ? -9.524  12.359  13.767  1.00 15.88  ? 432  ILE A N     1 
ATOM   3341 C  CA    . ILE A 1 432 ? -8.811  12.171  15.023  1.00 18.80  ? 432  ILE A CA    1 
ATOM   3342 C  C     . ILE A 1 432 ? -7.379  11.776  14.710  1.00 18.53  ? 432  ILE A C     1 
ATOM   3343 O  O     . ILE A 1 432 ? -7.139  10.917  13.857  1.00 19.74  ? 432  ILE A O     1 
ATOM   3344 C  CB    . ILE A 1 432 ? -9.500  11.109  15.897  1.00 18.54  ? 432  ILE A CB    1 
ATOM   3345 C  CG1   . ILE A 1 432 ? -11.007 11.379  15.926  1.00 14.62  ? 432  ILE A CG1   1 
ATOM   3346 C  CG2   . ILE A 1 432 ? -8.899  11.090  17.291  1.00 15.05  ? 432  ILE A CG2   1 
ATOM   3347 C  CD1   . ILE A 1 432 ? -11.837 10.294  16.623  1.00 16.81  ? 432  ILE A CD1   1 
ATOM   3348 N  N     . PHE A 1 433 ? -6.431  12.397  15.402  1.00 15.83  ? 433  PHE A N     1 
ATOM   3349 C  CA    . PHE A 1 433 ? -5.032  12.002  15.361  1.00 20.13  ? 433  PHE A CA    1 
ATOM   3350 C  C     . PHE A 1 433 ? -4.617  11.499  16.737  1.00 16.53  ? 433  PHE A C     1 
ATOM   3351 O  O     . PHE A 1 433 ? -5.207  11.874  17.751  1.00 15.57  ? 433  PHE A O     1 
ATOM   3352 C  CB    . PHE A 1 433 ? -4.124  13.179  14.938  1.00 15.84  ? 433  PHE A CB    1 
ATOM   3353 C  CG    . PHE A 1 433 ? -4.339  13.644  13.520  1.00 18.97  ? 433  PHE A CG    1 
ATOM   3354 C  CD1   . PHE A 1 433 ? -4.184  12.761  12.451  1.00 20.73  ? 433  PHE A CD1   1 
ATOM   3355 C  CD2   . PHE A 1 433 ? -4.642  14.970  13.250  1.00 20.41  ? 433  PHE A CD2   1 
ATOM   3356 C  CE1   . PHE A 1 433 ? -4.359  13.183  11.145  1.00 22.37  ? 433  PHE A CE1   1 
ATOM   3357 C  CE2   . PHE A 1 433 ? -4.799  15.409  11.938  1.00 19.01  ? 433  PHE A CE2   1 
ATOM   3358 C  CZ    . PHE A 1 433 ? -4.670  14.514  10.888  1.00 20.03  ? 433  PHE A CZ    1 
ATOM   3359 N  N     . GLY A 1 434 ? -3.597  10.643  16.778  1.00 18.68  ? 434  GLY A N     1 
ATOM   3360 C  CA    . GLY A 1 434 ? -3.077  10.240  18.074  1.00 19.64  ? 434  GLY A CA    1 
ATOM   3361 C  C     . GLY A 1 434 ? -2.042  9.137   18.033  1.00 21.16  ? 434  GLY A C     1 
ATOM   3362 O  O     . GLY A 1 434 ? -1.902  8.452   17.027  1.00 19.99  ? 434  GLY A O     1 
ATOM   3363 N  N     . GLY A 1 435 ? -1.295  8.973   19.115  1.00 22.39  ? 435  GLY A N     1 
ATOM   3364 C  CA    . GLY A 1 435 ? -0.360  7.877   19.206  1.00 23.10  ? 435  GLY A CA    1 
ATOM   3365 C  C     . GLY A 1 435 ? -0.068  7.550   20.652  1.00 23.32  ? 435  GLY A C     1 
ATOM   3366 O  O     . GLY A 1 435 ? -0.742  8.023   21.569  1.00 19.85  ? 435  GLY A O     1 
ATOM   3367 N  N     . ARG A 1 436 ? 0.967   6.748   20.849  1.00 22.23  ? 436  ARG A N     1 
ATOM   3368 C  CA    . ARG A 1 436 ? 1.348   6.305   22.186  1.00 25.52  ? 436  ARG A CA    1 
ATOM   3369 C  C     . ARG A 1 436 ? 2.276   7.351   22.780  1.00 24.46  ? 436  ARG A C     1 
ATOM   3370 O  O     . ARG A 1 436 ? 3.449   7.441   22.405  1.00 24.40  ? 436  ARG A O     1 
ATOM   3371 C  CB    . ARG A 1 436 ? 2.018   4.937   22.134  1.00 24.73  ? 436  ARG A CB    1 
ATOM   3372 C  CG    . ARG A 1 436 ? 1.072   3.778   21.892  1.00 27.22  ? 436  ARG A CG    1 
ATOM   3373 C  CD    . ARG A 1 436 ? 1.871   2.530   21.555  1.00 24.42  ? 436  ARG A CD    1 
ATOM   3374 N  NE    . ARG A 1 436 ? 0.996   1.405   21.287  1.00 33.11  ? 436  ARG A NE    1 
ATOM   3375 C  CZ    . ARG A 1 436 ? 0.531   0.592   22.225  1.00 33.91  ? 436  ARG A CZ    1 
ATOM   3376 N  NH1   . ARG A 1 436 ? 0.887   0.724   23.494  1.00 30.59  ? 436  ARG A NH1   1 
ATOM   3377 N  NH2   . ARG A 1 436 ? -0.309  -0.376  21.880  1.00 32.10  ? 436  ARG A NH2   1 
ATOM   3378 N  N     . ARG A 1 437 ? 1.760   8.138   23.719  1.00 19.57  ? 437  ARG A N     1 
ATOM   3379 C  CA    . ARG A 1 437 ? 2.583   9.128   24.413  1.00 26.80  ? 437  ARG A CA    1 
ATOM   3380 C  C     . ARG A 1 437 ? 2.458   8.858   25.897  1.00 27.42  ? 437  ARG A C     1 
ATOM   3381 O  O     . ARG A 1 437 ? 1.420   9.185   26.506  1.00 23.99  ? 437  ARG A O     1 
ATOM   3382 C  CB    . ARG A 1 437 ? 2.182   10.572  24.095  1.00 23.40  ? 437  ARG A CB    1 
ATOM   3383 C  CG    . ARG A 1 437 ? 2.390   10.995  22.646  1.00 21.66  ? 437  ARG A CG    1 
ATOM   3384 C  CD    . ARG A 1 437 ? 3.839   10.852  22.195  1.00 30.82  ? 437  ARG A CD    1 
ATOM   3385 N  NE    . ARG A 1 437 ? 4.815   11.576  23.005  1.00 21.34  ? 437  ARG A NE    1 
ATOM   3386 C  CZ    . ARG A 1 437 ? 5.256   12.795  22.728  1.00 26.23  ? 437  ARG A CZ    1 
ATOM   3387 N  NH1   . ARG A 1 437 ? 4.709   13.523  21.774  1.00 20.22  ? 437  ARG A NH1   1 
ATOM   3388 N  NH2   . ARG A 1 437 ? 6.286   13.289  23.415  1.00 24.43  ? 437  ARG A NH2   1 
ATOM   3389 N  N     . PRO A 1 438 ? 3.485   8.267   26.517  1.00 28.73  ? 438  PRO A N     1 
ATOM   3390 C  CA    . PRO A 1 438 ? 3.395   7.944   27.951  1.00 32.20  ? 438  PRO A CA    1 
ATOM   3391 C  C     . PRO A 1 438 ? 3.366   9.167   28.849  1.00 29.48  ? 438  PRO A C     1 
ATOM   3392 O  O     . PRO A 1 438 ? 2.899   9.066   29.987  1.00 31.33  ? 438  PRO A O     1 
ATOM   3393 C  CB    . PRO A 1 438 ? 4.652   7.098   28.201  1.00 37.35  ? 438  PRO A CB    1 
ATOM   3394 C  CG    . PRO A 1 438 ? 5.610   7.510   27.097  1.00 35.82  ? 438  PRO A CG    1 
ATOM   3395 C  CD    . PRO A 1 438 ? 4.749   7.816   25.907  1.00 28.44  ? 438  PRO A CD    1 
ATOM   3396 N  N     . ALA A 1 439 ? 3.825   10.321  28.367  1.00 31.36  ? 439  ALA A N     1 
ATOM   3397 C  CA    . ALA A 1 439 ? 3.974   11.507  29.196  1.00 31.77  ? 439  ALA A CA    1 
ATOM   3398 C  C     . ALA A 1 439 ? 3.564   12.749  28.420  1.00 27.98  ? 439  ALA A C     1 
ATOM   3399 O  O     . ALA A 1 439 ? 3.674   12.795  27.191  1.00 25.47  ? 439  ALA A O     1 
ATOM   3400 C  CB    . ALA A 1 439 ? 5.423   11.683  29.679  1.00 30.32  ? 439  ALA A CB    1 
ATOM   3401 N  N     . GLY A 1 440 ? 3.097   13.758  29.162  1.00 29.14  ? 440  GLY A N     1 
ATOM   3402 C  CA    . GLY A 1 440 ? 2.973   15.112  28.650  1.00 25.52  ? 440  GLY A CA    1 
ATOM   3403 C  C     . GLY A 1 440 ? 1.724   15.447  27.860  1.00 28.82  ? 440  GLY A C     1 
ATOM   3404 O  O     . GLY A 1 440 ? 1.209   16.565  27.962  1.00 29.70  ? 440  GLY A O     1 
ATOM   3405 N  N     . VAL A 1 441 ? 1.222   14.507  27.070  1.00 23.40  ? 441  VAL A N     1 
ATOM   3406 C  CA    . VAL A 1 441 ? 0.182   14.781  26.084  1.00 20.04  ? 441  VAL A CA    1 
ATOM   3407 C  C     . VAL A 1 441 ? -1.175  14.436  26.702  1.00 20.66  ? 441  VAL A C     1 
ATOM   3408 O  O     . VAL A 1 441 ? -1.363  13.292  27.143  1.00 20.71  ? 441  VAL A O     1 
ATOM   3409 C  CB    . VAL A 1 441 ? 0.411   13.995  24.786  1.00 23.47  ? 441  VAL A CB    1 
ATOM   3410 C  CG1   . VAL A 1 441 ? -0.716  14.315  23.776  1.00 22.73  ? 441  VAL A CG1   1 
ATOM   3411 C  CG2   . VAL A 1 441 ? 1.785   14.328  24.229  1.00 27.33  ? 441  VAL A CG2   1 
ATOM   3412 N  N     . PRO A 1 442 ? -2.121  15.371  26.741  1.00 24.20  ? 442  PRO A N     1 
ATOM   3413 C  CA    . PRO A 1 442 ? -3.390  15.120  27.439  1.00 24.56  ? 442  PRO A CA    1 
ATOM   3414 C  C     . PRO A 1 442 ? -4.274  14.136  26.688  1.00 23.41  ? 442  PRO A C     1 
ATOM   3415 O  O     . PRO A 1 442 ? -4.027  13.776  25.540  1.00 20.18  ? 442  PRO A O     1 
ATOM   3416 C  CB    . PRO A 1 442 ? -4.044  16.505  27.511  1.00 23.54  ? 442  PRO A CB    1 
ATOM   3417 C  CG    . PRO A 1 442 ? -3.388  17.309  26.490  1.00 27.41  ? 442  PRO A CG    1 
ATOM   3418 C  CD    . PRO A 1 442 ? -2.012  16.760  26.265  1.00 24.66  ? 442  PRO A CD    1 
ATOM   3419 N  N     . LEU A 1 443 ? -5.346  13.726  27.374  1.00 21.01  ? 443  LEU A N     1 
ATOM   3420 C  CA    . LEU A 1 443 ? -6.234  12.685  26.872  1.00 18.64  ? 443  LEU A CA    1 
ATOM   3421 C  C     . LEU A 1 443 ? -6.881  13.079  25.553  1.00 21.85  ? 443  LEU A C     1 
ATOM   3422 O  O     . LEU A 1 443 ? -7.001  12.249  24.642  1.00 21.32  ? 443  LEU A O     1 
ATOM   3423 C  CB    . LEU A 1 443 ? -7.307  12.373  27.921  1.00 17.95  ? 443  LEU A CB    1 
ATOM   3424 C  CG    . LEU A 1 443 ? -8.484  11.477  27.504  1.00 20.48  ? 443  LEU A CG    1 
ATOM   3425 C  CD1   . LEU A 1 443 ? -8.034  10.063  27.169  1.00 21.21  ? 443  LEU A CD1   1 
ATOM   3426 C  CD2   . LEU A 1 443 ? -9.536  11.463  28.596  1.00 24.48  ? 443  LEU A CD2   1 
ATOM   3427 N  N     . VAL A 1 444 ? -7.314  14.329  25.427  1.00 18.36  ? 444  VAL A N     1 
ATOM   3428 C  CA    . VAL A 1 444 ? -7.929  14.782  24.185  1.00 19.17  ? 444  VAL A CA    1 
ATOM   3429 C  C     . VAL A 1 444 ? -7.790  16.299  24.116  1.00 16.69  ? 444  VAL A C     1 
ATOM   3430 O  O     . VAL A 1 444 ? -7.913  16.993  25.125  1.00 20.94  ? 444  VAL A O     1 
ATOM   3431 C  CB    . VAL A 1 444 ? -9.410  14.327  24.093  1.00 19.87  ? 444  VAL A CB    1 
ATOM   3432 C  CG1   . VAL A 1 444 ? -10.253 14.972  25.213  1.00 19.05  ? 444  VAL A CG1   1 
ATOM   3433 C  CG2   . VAL A 1 444 ? -10.010 14.663  22.719  1.00 19.88  ? 444  VAL A CG2   1 
ATOM   3434 N  N     . TYR A 1 445 ? -7.504  16.809  22.922  1.00 22.00  ? 445  TYR A N     1 
ATOM   3435 C  CA    . TYR A 1 445 ? -7.688  18.231  22.686  1.00 18.48  ? 445  TYR A CA    1 
ATOM   3436 C  C     . TYR A 1 445 ? -8.162  18.432  21.255  1.00 22.12  ? 445  TYR A C     1 
ATOM   3437 O  O     . TYR A 1 445 ? -8.126  17.517  20.432  1.00 21.50  ? 445  TYR A O     1 
ATOM   3438 C  CB    . TYR A 1 445 ? -6.424  19.038  23.004  1.00 17.70  ? 445  TYR A CB    1 
ATOM   3439 C  CG    . TYR A 1 445 ? -5.210  18.776  22.140  1.00 18.12  ? 445  TYR A CG    1 
ATOM   3440 C  CD1   . TYR A 1 445 ? -4.965  19.531  20.997  1.00 22.55  ? 445  TYR A CD1   1 
ATOM   3441 C  CD2   . TYR A 1 445 ? -4.285  17.814  22.496  1.00 18.52  ? 445  TYR A CD2   1 
ATOM   3442 C  CE1   . TYR A 1 445 ? -3.832  19.305  20.208  1.00 23.67  ? 445  TYR A CE1   1 
ATOM   3443 C  CE2   . TYR A 1 445 ? -3.153  17.581  21.725  1.00 20.15  ? 445  TYR A CE2   1 
ATOM   3444 C  CZ    . TYR A 1 445 ? -2.928  18.336  20.583  1.00 23.22  ? 445  TYR A CZ    1 
ATOM   3445 O  OH    . TYR A 1 445 ? -1.808  18.110  19.806  1.00 24.14  ? 445  TYR A OH    1 
ATOM   3446 N  N     . GLU A 1 446 ? -8.659  19.637  20.981  1.00 19.19  ? 446  GLU A N     1 
ATOM   3447 C  CA    . GLU A 1 446 ? -9.217  19.984  19.684  1.00 15.70  ? 446  GLU A CA    1 
ATOM   3448 C  C     . GLU A 1 446 ? -8.396  21.117  19.084  1.00 16.46  ? 446  GLU A C     1 
ATOM   3449 O  O     . GLU A 1 446 ? -7.997  22.047  19.790  1.00 20.36  ? 446  GLU A O     1 
ATOM   3450 C  CB    . GLU A 1 446 ? -10.699 20.386  19.813  1.00 18.44  ? 446  GLU A CB    1 
ATOM   3451 C  CG    . GLU A 1 446 ? -11.365 20.983  18.567  1.00 19.87  ? 446  GLU A CG    1 
ATOM   3452 C  CD    . GLU A 1 446 ? -12.720 21.621  18.904  1.00 24.68  ? 446  GLU A CD    1 
ATOM   3453 O  OE1   . GLU A 1 446 ? -13.377 21.157  19.849  1.00 26.20  ? 446  GLU A OE1   1 
ATOM   3454 O  OE2   . GLU A 1 446 ? -13.122 22.594  18.247  1.00 25.04  ? 446  GLU A OE2   1 
ATOM   3455 N  N     . ALA A 1 447 ? -8.141  21.023  17.784  1.00 18.08  ? 447  ALA A N     1 
ATOM   3456 C  CA    . ALA A 1 447 ? -7.331  22.008  17.080  1.00 16.82  ? 447  ALA A CA    1 
ATOM   3457 C  C     . ALA A 1 447 ? -8.070  23.336  16.945  1.00 16.98  ? 447  ALA A C     1 
ATOM   3458 O  O     . ALA A 1 447 ? -9.304  23.392  16.954  1.00 20.54  ? 447  ALA A O     1 
ATOM   3459 C  CB    . ALA A 1 447 ? -6.957  21.485  15.696  1.00 16.55  ? 447  ALA A CB    1 
ATOM   3460 N  N     . LEU A 1 448 ? -7.297  24.419  16.797  1.00 21.48  ? 448  LEU A N     1 
ATOM   3461 C  CA    . LEU A 1 448 ? -7.863  25.768  16.769  1.00 21.09  ? 448  LEU A CA    1 
ATOM   3462 C  C     . LEU A 1 448 ? -8.368  26.163  15.395  1.00 26.08  ? 448  LEU A C     1 
ATOM   3463 O  O     . LEU A 1 448 ? -9.197  27.068  15.290  1.00 28.43  ? 448  LEU A O     1 
ATOM   3464 C  CB    . LEU A 1 448 ? -6.821  26.785  17.222  1.00 21.94  ? 448  LEU A CB    1 
ATOM   3465 C  CG    . LEU A 1 448 ? -6.264  26.525  18.615  1.00 22.93  ? 448  LEU A CG    1 
ATOM   3466 C  CD1   . LEU A 1 448 ? -5.009  27.369  18.822  1.00 29.95  ? 448  LEU A CD1   1 
ATOM   3467 C  CD2   . LEU A 1 448 ? -7.329  26.831  19.677  1.00 19.00  ? 448  LEU A CD2   1 
ATOM   3468 N  N     . SER A 1 449 ? -7.892  25.507  14.348  1.00 20.62  ? 449  SER A N     1 
ATOM   3469 C  CA    . SER A 1 449 ? -8.226  25.873  12.981  1.00 20.74  ? 449  SER A CA    1 
ATOM   3470 C  C     . SER A 1 449 ? -7.790  24.712  12.112  1.00 20.24  ? 449  SER A C     1 
ATOM   3471 O  O     . SER A 1 449 ? -7.111  23.802  12.580  1.00 21.98  ? 449  SER A O     1 
ATOM   3472 C  CB    . SER A 1 449 ? -7.510  27.156  12.556  1.00 25.67  ? 449  SER A CB    1 
ATOM   3473 O  OG    . SER A 1 449 ? -6.113  26.915  12.507  1.00 23.84  ? 449  SER A OG    1 
ATOM   3474 N  N     . TRP A 1 450 ? -8.172  24.762  10.835  1.00 25.13  ? 450  TRP A N     1 
ATOM   3475 C  CA    . TRP A 1 450 ? -7.708  23.753  9.887   1.00 22.42  ? 450  TRP A CA    1 
ATOM   3476 C  C     . TRP A 1 450 ? -6.191  23.718  9.824   1.00 22.76  ? 450  TRP A C     1 
ATOM   3477 O  O     . TRP A 1 450 ? -5.580  22.642  9.848   1.00 22.51  ? 450  TRP A O     1 
ATOM   3478 C  CB    . TRP A 1 450 ? -8.281  24.022  8.500   1.00 23.00  ? 450  TRP A CB    1 
ATOM   3479 C  CG    . TRP A 1 450 ? -7.932  22.956  7.537   1.00 24.27  ? 450  TRP A CG    1 
ATOM   3480 C  CD1   . TRP A 1 450 ? -7.036  23.032  6.512   1.00 22.77  ? 450  TRP A CD1   1 
ATOM   3481 C  CD2   . TRP A 1 450 ? -8.455  21.625  7.521   1.00 21.14  ? 450  TRP A CD2   1 
ATOM   3482 N  NE1   . TRP A 1 450 ? -6.980  21.830  5.846   1.00 26.20  ? 450  TRP A NE1   1 
ATOM   3483 C  CE2   . TRP A 1 450 ? -7.850  20.952  6.443   1.00 27.56  ? 450  TRP A CE2   1 
ATOM   3484 C  CE3   . TRP A 1 450 ? -9.399  20.942  8.304   1.00 26.29  ? 450  TRP A CE3   1 
ATOM   3485 C  CZ2   . TRP A 1 450 ? -8.140  19.628  6.136   1.00 25.33  ? 450  TRP A CZ2   1 
ATOM   3486 C  CZ3   . TRP A 1 450 ? -9.687  19.627  7.995   1.00 22.56  ? 450  TRP A CZ3   1 
ATOM   3487 C  CH2   . TRP A 1 450 ? -9.057  18.982  6.925   1.00 26.38  ? 450  TRP A CH2   1 
ATOM   3488 N  N     . GLN A 1 451 ? -5.559  24.894  9.748   1.00 20.34  ? 451  GLN A N     1 
ATOM   3489 C  CA    . GLN A 1 451 ? -4.108  24.939  9.632   1.00 22.96  ? 451  GLN A CA    1 
ATOM   3490 C  C     . GLN A 1 451 ? -3.441  24.386  10.884  1.00 19.66  ? 451  GLN A C     1 
ATOM   3491 O  O     . GLN A 1 451 ? -2.491  23.596  10.791  1.00 20.16  ? 451  GLN A O     1 
ATOM   3492 C  CB    . GLN A 1 451 ? -3.651  26.371  9.340   1.00 25.67  ? 451  GLN A CB    1 
ATOM   3493 C  CG    . GLN A 1 451 ? -4.093  26.877  7.960   1.00 28.79  ? 451  GLN A CG    1 
ATOM   3494 C  CD    . GLN A 1 451 ? -5.553  27.333  7.914   1.00 35.42  ? 451  GLN A CD    1 
ATOM   3495 O  OE1   . GLN A 1 451 ? -6.118  27.770  8.918   1.00 30.44  ? 451  GLN A OE1   1 
ATOM   3496 N  NE2   . GLN A 1 451 ? -6.169  27.225  6.740   1.00 40.81  ? 451  GLN A NE2   1 
ATOM   3497 N  N     . HIS A 1 452 ? -3.953  24.749  12.059  1.00 17.81  ? 452  HIS A N     1 
ATOM   3498 C  CA    . HIS A 1 452 ? -3.445  24.151  13.289  1.00 20.67  ? 452  HIS A CA    1 
ATOM   3499 C  C     . HIS A 1 452 ? -3.665  22.634  13.308  1.00 18.48  ? 452  HIS A C     1 
ATOM   3500 O  O     . HIS A 1 452 ? -2.809  21.887  13.785  1.00 18.44  ? 452  HIS A O     1 
ATOM   3501 C  CB    . HIS A 1 452 ? -4.097  24.808  14.504  1.00 18.46  ? 452  HIS A CB    1 
ATOM   3502 C  CG    . HIS A 1 452 ? -3.596  24.267  15.810  1.00 21.04  ? 452  HIS A CG    1 
ATOM   3503 N  ND1   . HIS A 1 452 ? -4.437  23.822  16.807  1.00 20.97  ? 452  HIS A ND1   1 
ATOM   3504 C  CD2   . HIS A 1 452 ? -2.337  24.102  16.280  1.00 19.72  ? 452  HIS A CD2   1 
ATOM   3505 C  CE1   . HIS A 1 452 ? -3.716  23.401  17.834  1.00 25.00  ? 452  HIS A CE1   1 
ATOM   3506 N  NE2   . HIS A 1 452 ? -2.437  23.568  17.542  1.00 23.38  ? 452  HIS A NE2   1 
ATOM   3507 N  N     . GLY A 1 453 ? -4.787  22.160  12.763  1.00 18.42  ? 453  GLY A N     1 
ATOM   3508 C  CA    . GLY A 1 453 ? -5.047  20.723  12.763  1.00 15.62  ? 453  GLY A CA    1 
ATOM   3509 C  C     . GLY A 1 453 ? -4.098  19.968  11.855  1.00 19.39  ? 453  GLY A C     1 
ATOM   3510 O  O     . GLY A 1 453 ? -3.642  18.876  12.198  1.00 19.67  ? 453  GLY A O     1 
ATOM   3511 N  N     . VAL A 1 454 ? -3.750  20.560  10.705  1.00 17.01  ? 454  VAL A N     1 
ATOM   3512 C  CA    . VAL A 1 454 ? -2.756  19.953  9.826   1.00 17.61  ? 454  VAL A CA    1 
ATOM   3513 C  C     . VAL A 1 454 ? -1.409  19.906  10.525  1.00 20.38  ? 454  VAL A C     1 
ATOM   3514 O  O     . VAL A 1 454 ? -0.659  18.925  10.412  1.00 18.51  ? 454  VAL A O     1 
ATOM   3515 C  CB    . VAL A 1 454 ? -2.684  20.720  8.490   1.00 21.50  ? 454  VAL A CB    1 
ATOM   3516 C  CG1   . VAL A 1 454 ? -1.507  20.216  7.616   1.00 15.83  ? 454  VAL A CG1   1 
ATOM   3517 C  CG2   . VAL A 1 454 ? -4.015  20.594  7.748   1.00 20.90  ? 454  VAL A CG2   1 
ATOM   3518 N  N     . PHE A 1 455 ? -1.081  20.966  11.261  1.00 17.41  ? 455  PHE A N     1 
ATOM   3519 C  CA    . PHE A 1 455 ? 0.149   20.970  12.041  1.00 17.46  ? 455  PHE A CA    1 
ATOM   3520 C  C     . PHE A 1 455 ? 0.143   19.874  13.100  1.00 14.18  ? 455  PHE A C     1 
ATOM   3521 O  O     . PHE A 1 455 ? 1.166   19.221  13.327  1.00 18.85  ? 455  PHE A O     1 
ATOM   3522 C  CB    . PHE A 1 455 ? 0.347   22.327  12.709  1.00 19.02  ? 455  PHE A CB    1 
ATOM   3523 C  CG    . PHE A 1 455 ? 1.434   22.316  13.729  1.00 16.29  ? 455  PHE A CG    1 
ATOM   3524 C  CD1   . PHE A 1 455 ? 2.756   22.347  13.339  1.00 20.76  ? 455  PHE A CD1   1 
ATOM   3525 C  CD2   . PHE A 1 455 ? 1.139   22.231  15.067  1.00 17.91  ? 455  PHE A CD2   1 
ATOM   3526 C  CE1   . PHE A 1 455 ? 3.767   22.319  14.271  1.00 18.57  ? 455  PHE A CE1   1 
ATOM   3527 C  CE2   . PHE A 1 455 ? 2.144   22.188  16.001  1.00 22.00  ? 455  PHE A CE2   1 
ATOM   3528 C  CZ    . PHE A 1 455 ? 3.455   22.233  15.603  1.00 19.16  ? 455  PHE A CZ    1 
ATOM   3529 N  N     . VAL A 1 456 ? -0.985  19.685  13.782  1.00 15.55  ? 456  VAL A N     1 
ATOM   3530 C  CA    . VAL A 1 456 ? -1.095  18.610  14.781  1.00 15.22  ? 456  VAL A CA    1 
ATOM   3531 C  C     . VAL A 1 456 ? -0.821  17.246  14.147  1.00 16.60  ? 456  VAL A C     1 
ATOM   3532 O  O     . VAL A 1 456 ? -0.085  16.415  14.701  1.00 18.30  ? 456  VAL A O     1 
ATOM   3533 C  CB    . VAL A 1 456 ? -2.479  18.649  15.453  1.00 14.58  ? 456  VAL A CB    1 
ATOM   3534 C  CG1   . VAL A 1 456 ? -2.685  17.403  16.341  1.00 18.17  ? 456  VAL A CG1   1 
ATOM   3535 C  CG2   . VAL A 1 456 ? -2.644  19.930  16.269  1.00 14.68  ? 456  VAL A CG2   1 
ATOM   3536 N  N     . GLY A 1 457 ? -1.416  16.983  12.985  1.00 15.57  ? 457  GLY A N     1 
ATOM   3537 C  CA    . GLY A 1 457 ? -1.092  15.747  12.283  1.00 15.93  ? 457  GLY A CA    1 
ATOM   3538 C  C     . GLY A 1 457 ? 0.386   15.639  11.955  1.00 18.77  ? 457  GLY A C     1 
ATOM   3539 O  O     . GLY A 1 457 ? 0.993   14.581  12.133  1.00 17.64  ? 457  GLY A O     1 
ATOM   3540 N  N     . ALA A 1 458 ? 0.987   16.747  11.489  1.00 16.32  ? 458  ALA A N     1 
ATOM   3541 C  CA    . ALA A 1 458 ? 2.395   16.756  11.130  1.00 17.52  ? 458  ALA A CA    1 
ATOM   3542 C  C     . ALA A 1 458 ? 3.283   16.531  12.342  1.00 16.29  ? 458  ALA A C     1 
ATOM   3543 O  O     . ALA A 1 458 ? 4.372   15.961  12.211  1.00 19.94  ? 458  ALA A O     1 
ATOM   3544 C  CB    . ALA A 1 458 ? 2.764   18.089  10.447  1.00 16.49  ? 458  ALA A CB    1 
ATOM   3545 N  N     . ALA A 1 459 ? 2.840   16.966  13.515  1.00 14.11  ? 459  ALA A N     1 
ATOM   3546 C  CA    . ALA A 1 459 ? 3.609   16.888  14.749  1.00 17.83  ? 459  ALA A CA    1 
ATOM   3547 C  C     . ALA A 1 459 ? 3.457   15.556  15.480  1.00 16.58  ? 459  ALA A C     1 
ATOM   3548 O  O     . ALA A 1 459 ? 4.055   15.390  16.546  1.00 19.58  ? 459  ALA A O     1 
ATOM   3549 C  CB    . ALA A 1 459 ? 3.192   18.023  15.701  1.00 17.56  ? 459  ALA A CB    1 
ATOM   3550 N  N     . MET A 1 460 ? 2.695   14.606  14.939  1.00 16.82  ? 460  MET A N     1 
ATOM   3551 C  CA    . MET A 1 460 ? 2.459   13.336  15.637  1.00 18.02  ? 460  MET A CA    1 
ATOM   3552 C  C     . MET A 1 460 ? 3.750   12.595  15.958  1.00 19.72  ? 460  MET A C     1 
ATOM   3553 O  O     . MET A 1 460 ? 4.665   12.494  15.126  1.00 22.40  ? 460  MET A O     1 
ATOM   3554 C  CB    . MET A 1 460 ? 1.559   12.423  14.807  1.00 14.97  ? 460  MET A CB    1 
ATOM   3555 C  CG    . MET A 1 460 ? 0.098   12.804  14.915  1.00 20.94  ? 460  MET A CG    1 
ATOM   3556 S  SD    . MET A 1 460 ? -0.854  11.833  13.765  1.00 18.81  ? 460  MET A SD    1 
ATOM   3557 C  CE    . MET A 1 460 ? -0.609  10.174  14.400  1.00 18.87  ? 460  MET A CE    1 
ATOM   3558 N  N     . ARG A 1 461 ? 3.820   12.092  17.187  1.00 17.67  ? 461  ARG A N     1 
ATOM   3559 C  CA    . ARG A 1 461 ? 4.913   11.245  17.654  1.00 17.99  ? 461  ARG A CA    1 
ATOM   3560 C  C     . ARG A 1 461 ? 4.308   10.104  18.452  1.00 20.75  ? 461  ARG A C     1 
ATOM   3561 O  O     . ARG A 1 461 ? 3.207   10.225  18.975  1.00 20.75  ? 461  ARG A O     1 
ATOM   3562 C  CB    . ARG A 1 461 ? 5.905   12.028  18.516  1.00 17.80  ? 461  ARG A CB    1 
ATOM   3563 C  CG    . ARG A 1 461 ? 6.556   13.214  17.759  1.00 16.67  ? 461  ARG A CG    1 
ATOM   3564 C  CD    . ARG A 1 461 ? 7.400   14.019  18.718  1.00 21.30  ? 461  ARG A CD    1 
ATOM   3565 N  NE    . ARG A 1 461 ? 8.668   13.359  18.960  1.00 22.42  ? 461  ARG A NE    1 
ATOM   3566 C  CZ    . ARG A 1 461 ? 9.429   13.557  20.026  1.00 27.83  ? 461  ARG A CZ    1 
ATOM   3567 N  NH1   . ARG A 1 461 ? 9.017   14.290  21.043  1.00 21.48  ? 461  ARG A NH1   1 
ATOM   3568 N  NH2   . ARG A 1 461 ? 10.635  13.002  20.071  1.00 24.58  ? 461  ARG A NH2   1 
ATOM   3569 N  N     . SER A 1 462 ? 5.035   8.990   18.546  1.00 24.52  ? 462  SER A N     1 
ATOM   3570 C  CA    . SER A 1 462 ? 4.504   7.787   19.183  1.00 27.50  ? 462  SER A CA    1 
ATOM   3571 C  C     . SER A 1 462 ? 5.672   6.881   19.565  1.00 32.59  ? 462  SER A C     1 
ATOM   3572 O  O     . SER A 1 462 ? 6.655   6.790   18.824  1.00 25.46  ? 462  SER A O     1 
ATOM   3573 C  CB    . SER A 1 462 ? 3.541   7.046   18.238  1.00 21.46  ? 462  SER A CB    1 
ATOM   3574 O  OG    . SER A 1 462 ? 2.828   5.999   18.891  1.00 24.74  ? 462  SER A OG    1 
ATOM   3575 N  N     . GLU A 1 463 ? 5.570   6.217   20.716  1.00 28.12  ? 463  GLU A N     1 
ATOM   3576 C  CA    . GLU A 1 463 ? 6.657   5.328   21.102  1.00 41.15  ? 463  GLU A CA    1 
ATOM   3577 C  C     . GLU A 1 463 ? 6.660   4.091   20.205  1.00 43.50  ? 463  GLU A C     1 
ATOM   3578 O  O     . GLU A 1 463 ? 5.622   3.671   19.680  1.00 36.13  ? 463  GLU A O     1 
ATOM   3579 C  CB    . GLU A 1 463 ? 6.564   4.947   22.583  1.00 40.14  ? 463  GLU A CB    1 
ATOM   3580 C  CG    . GLU A 1 463 ? 5.313   4.230   22.983  1.00 47.33  ? 463  GLU A CG    1 
ATOM   3581 C  CD    . GLU A 1 463 ? 5.356   3.750   24.424  1.00 51.64  ? 463  GLU A CD    1 
ATOM   3582 O  OE1   . GLU A 1 463 ? 6.419   3.891   25.070  1.00 53.81  ? 463  GLU A OE1   1 
ATOM   3583 O  OE2   . GLU A 1 463 ? 4.322   3.235   24.907  1.00 63.51  ? 463  GLU A OE2   1 
ATOM   3584 N  N     . ALA A 1 464 ? 7.852   3.529   20.010  1.00 44.28  ? 464  ALA A N     1 
ATOM   3585 C  CA    . ALA A 1 464 ? 8.053   2.511   18.980  1.00 61.39  ? 464  ALA A CA    1 
ATOM   3586 C  C     . ALA A 1 464 ? 7.303   1.218   19.299  1.00 76.28  ? 464  ALA A C     1 
ATOM   3587 O  O     . ALA A 1 464 ? 7.311   0.733   20.434  1.00 69.18  ? 464  ALA A O     1 
ATOM   3588 C  CB    . ALA A 1 464 ? 9.543   2.221   18.809  1.00 61.08  ? 464  ALA A CB    1 
ATOM   3589 N  N     . THR A 1 465 ? 6.666   0.652   18.273  1.00 79.06  ? 465  THR A N     1 
ATOM   3590 C  CA    . THR A 1 465 ? 5.861   -0.556  18.373  1.00 82.83  ? 465  THR A CA    1 
ATOM   3591 C  C     . THR A 1 465 ? 6.604   -1.739  17.747  1.00 92.97  ? 465  THR A C     1 
ATOM   3592 O  O     . THR A 1 465 ? 7.809   -1.675  17.477  1.00 97.03  ? 465  THR A O     1 
ATOM   3593 C  CB    . THR A 1 465 ? 4.503   -0.336  17.702  1.00 77.37  ? 465  THR A CB    1 
ATOM   3594 O  OG1   . THR A 1 465 ? 4.699   -0.072  16.306  1.00 77.16  ? 465  THR A OG1   1 
ATOM   3595 C  CG2   . THR A 1 465 ? 3.765   0.842   18.342  1.00 69.06  ? 465  THR A CG2   1 
ATOM   3596 N  N     . ALA A 1 466 ? 5.871   -2.830  17.508  1.00 88.81  ? 466  ALA A N     1 
ATOM   3597 C  CA    . ALA A 1 466 ? 6.428   -4.059  16.954  1.00 92.08  ? 466  ALA A CA    1 
ATOM   3598 C  C     . ALA A 1 466 ? 5.903   -4.354  15.553  1.00 88.72  ? 466  ALA A C     1 
ATOM   3599 O  O     . ALA A 1 466 ? 5.898   -5.515  15.125  1.00 77.13  ? 466  ALA A O     1 
ATOM   3600 C  CB    . ALA A 1 466 ? 6.141   -5.241  17.882  1.00 87.17  ? 466  ALA A CB    1 
ATOM   3601 N  N     . ALA A 1 467 ? 5.476   -3.325  14.825  1.00 87.45  ? 467  ALA A N     1 
ATOM   3602 C  CA    . ALA A 1 467 ? 4.843   -3.512  13.527  1.00 72.63  ? 467  ALA A CA    1 
ATOM   3603 C  C     . ALA A 1 467 ? 5.765   -3.232  12.346  1.00 72.66  ? 467  ALA A C     1 
ATOM   3604 O  O     . ALA A 1 467 ? 5.521   -3.749  11.250  1.00 59.28  ? 467  ALA A O     1 
ATOM   3605 C  CB    . ALA A 1 467 ? 3.605   -2.623  13.427  1.00 52.87  ? 467  ALA A CB    1 
ATOM   3606 N  N     . ALA A 1 468 ? 6.805   -2.420  12.530  1.00 78.91  ? 468  ALA A N     1 
ATOM   3607 C  CA    . ALA A 1 468 ? 7.830   -2.273  11.505  1.00 80.89  ? 468  ALA A CA    1 
ATOM   3608 C  C     . ALA A 1 468 ? 8.999   -3.193  11.841  1.00 87.48  ? 468  ALA A C     1 
ATOM   3609 O  O     . ALA A 1 468 ? 8.857   -4.420  11.799  1.00 87.80  ? 468  ALA A O     1 
ATOM   3610 C  CB    . ALA A 1 468 ? 8.284   -0.817  11.387  1.00 76.47  ? 468  ALA A CB    1 
ATOM   3611 N  N     . GLU A 1 469 ? 10.162  -2.619  12.183  1.00 91.02  ? 469  GLU A N     1 
ATOM   3612 C  CA    . GLU A 1 469 ? 11.273  -3.423  12.688  1.00 91.49  ? 469  GLU A CA    1 
ATOM   3613 C  C     . GLU A 1 469 ? 12.070  -2.675  13.757  1.00 97.13  ? 469  GLU A C     1 
ATOM   3614 O  O     . GLU A 1 469 ? 13.281  -2.885  13.889  1.00 97.83  ? 469  GLU A O     1 
ATOM   3615 C  CB    . GLU A 1 469 ? 12.197  -3.880  11.540  1.00 84.11  ? 469  GLU A CB    1 
ATOM   3616 C  CG    . GLU A 1 469 ? 12.969  -2.777  10.826  1.00 77.94  ? 469  GLU A CG    1 
ATOM   3617 C  CD    . GLU A 1 469 ? 12.306  -2.321  9.542   1.00 65.24  ? 469  GLU A CD    1 
ATOM   3618 O  OE1   . GLU A 1 469 ? 11.064  -2.179  9.524   1.00 64.14  ? 469  GLU A OE1   1 
ATOM   3619 O  OE2   . GLU A 1 469 ? 13.031  -2.107  8.548   1.00 58.98  ? 469  GLU A OE2   1 
ATOM   3620 N  N     . HIS A 1 470 ? 11.408  -1.826  14.537  1.00 105.70 ? 470  HIS A N     1 
ATOM   3621 C  CA    . HIS A 1 470 ? 12.065  -0.978  15.520  1.00 108.13 ? 470  HIS A CA    1 
ATOM   3622 C  C     . HIS A 1 470 ? 12.018  -1.610  16.909  1.00 106.47 ? 470  HIS A C     1 
ATOM   3623 O  O     . HIS A 1 470 ? 11.204  -2.493  17.192  1.00 105.70 ? 470  HIS A O     1 
ATOM   3624 C  CB    . HIS A 1 470 ? 11.412  0.408   15.548  1.00 105.86 ? 470  HIS A CB    1 
ATOM   3625 C  CG    . HIS A 1 470 ? 11.292  1.043   14.197  1.00 103.70 ? 470  HIS A CG    1 
ATOM   3626 N  ND1   . HIS A 1 470 ? 10.084  1.199   13.551  1.00 96.44  ? 470  HIS A ND1   1 
ATOM   3627 C  CD2   . HIS A 1 470 ? 12.232  1.548   13.362  1.00 107.21 ? 470  HIS A CD2   1 
ATOM   3628 C  CE1   . HIS A 1 470 ? 10.284  1.782   12.382  1.00 91.50  ? 470  HIS A CE1   1 
ATOM   3629 N  NE2   . HIS A 1 470 ? 11.579  2.002   12.242  1.00 95.80  ? 470  HIS A NE2   1 
ATOM   3630 N  N     . LYS A 1 471 ? 12.916  -1.144  17.775  1.00 104.32 ? 471  LYS A N     1 
ATOM   3631 C  CA    . LYS A 1 471 ? 13.008  -1.619  19.152  1.00 99.14  ? 471  LYS A CA    1 
ATOM   3632 C  C     . LYS A 1 471 ? 13.347  -0.432  20.052  1.00 94.84  ? 471  LYS A C     1 
ATOM   3633 O  O     . LYS A 1 471 ? 13.377  0.722   19.610  1.00 84.65  ? 471  LYS A O     1 
ATOM   3634 C  CB    . LYS A 1 471 ? 14.041  -2.748  19.277  1.00 95.77  ? 471  LYS A CB    1 
ATOM   3635 C  CG    . LYS A 1 471 ? 13.597  -4.086  18.703  1.00 94.84  ? 471  LYS A CG    1 
ATOM   3636 C  CD    . LYS A 1 471 ? 14.691  -5.133  18.854  1.00 91.76  ? 471  LYS A CD    1 
ATOM   3637 C  CE    . LYS A 1 471 ? 14.318  -6.440  18.175  1.00 88.37  ? 471  LYS A CE    1 
ATOM   3638 N  NZ    . LYS A 1 471 ? 15.479  -7.370  18.119  1.00 88.72  ? 471  LYS A NZ    1 
ATOM   3639 N  N     . GLY A 1 472 ? 13.602  -0.723  21.328  1.00 95.26  ? 472  GLY A N     1 
ATOM   3640 C  CA    . GLY A 1 472 ? 13.951  0.295   22.302  1.00 90.69  ? 472  GLY A CA    1 
ATOM   3641 C  C     . GLY A 1 472 ? 12.784  1.162   22.736  1.00 88.11  ? 472  GLY A C     1 
ATOM   3642 O  O     . GLY A 1 472 ? 11.739  1.178   22.078  1.00 86.17  ? 472  GLY A O     1 
ATOM   3643 N  N     . LYS A 1 473 ? 12.944  1.885   23.849  1.00 85.20  ? 473  LYS A N     1 
ATOM   3644 C  CA    . LYS A 1 473 ? 11.937  2.848   24.300  1.00 80.92  ? 473  LYS A CA    1 
ATOM   3645 C  C     . LYS A 1 473 ? 12.306  4.209   23.722  1.00 73.37  ? 473  LYS A C     1 
ATOM   3646 O  O     . LYS A 1 473 ? 12.991  5.022   24.348  1.00 64.89  ? 473  LYS A O     1 
ATOM   3647 C  CB    . LYS A 1 473 ? 11.833  2.870   25.820  1.00 88.37  ? 473  LYS A CB    1 
ATOM   3648 C  CG    . LYS A 1 473 ? 11.004  1.720   26.403  1.00 91.65  ? 473  LYS A CG    1 
ATOM   3649 C  CD    . LYS A 1 473 ? 9.568   1.722   25.876  1.00 82.59  ? 473  LYS A CD    1 
ATOM   3650 C  CE    . LYS A 1 473 ? 8.784   0.513   26.387  1.00 86.29  ? 473  LYS A CE    1 
ATOM   3651 N  NZ    . LYS A 1 473 ? 7.372   0.476   25.893  1.00 82.24  ? 473  LYS A NZ    1 
ATOM   3652 N  N     . VAL A 1 474 ? 11.837  4.450   22.502  1.00 61.56  ? 474  VAL A N     1 
ATOM   3653 C  CA    . VAL A 1 474 ? 12.141  5.649   21.738  1.00 50.07  ? 474  VAL A CA    1 
ATOM   3654 C  C     . VAL A 1 474 ? 10.828  6.280   21.299  1.00 43.26  ? 474  VAL A C     1 
ATOM   3655 O  O     . VAL A 1 474 ? 9.888   5.574   20.918  1.00 41.78  ? 474  VAL A O     1 
ATOM   3656 C  CB    . VAL A 1 474 ? 13.027  5.308   20.521  1.00 45.90  ? 474  VAL A CB    1 
ATOM   3657 C  CG1   . VAL A 1 474 ? 13.326  6.544   19.676  1.00 35.91  ? 474  VAL A CG1   1 
ATOM   3658 C  CG2   . VAL A 1 474 ? 14.310  4.647   20.986  1.00 51.11  ? 474  VAL A CG2   1 
ATOM   3659 N  N     . ILE A 1 475 ? 10.757  7.604   21.369  1.00 36.04  ? 475  ILE A N     1 
ATOM   3660 C  CA    . ILE A 1 475 ? 9.623   8.352   20.834  1.00 32.84  ? 475  ILE A CA    1 
ATOM   3661 C  C     . ILE A 1 475 ? 9.995   8.791   19.426  1.00 31.27  ? 475  ILE A C     1 
ATOM   3662 O  O     . ILE A 1 475 ? 10.952  9.548   19.237  1.00 31.10  ? 475  ILE A O     1 
ATOM   3663 C  CB    . ILE A 1 475 ? 9.280   9.561   21.720  1.00 32.35  ? 475  ILE A CB    1 
ATOM   3664 C  CG1   . ILE A 1 475 ? 9.006   9.118   23.161  1.00 32.69  ? 475  ILE A CG1   1 
ATOM   3665 C  CG2   . ILE A 1 475 ? 8.083   10.317  21.154  1.00 28.04  ? 475  ILE A CG2   1 
ATOM   3666 C  CD1   . ILE A 1 475 ? 7.688   8.377   23.344  1.00 35.14  ? 475  ILE A CD1   1 
ATOM   3667 N  N     . MET A 1 476 ? 9.263   8.306   18.431  1.00 23.19  ? 476  MET A N     1 
ATOM   3668 C  CA    . MET A 1 476 ? 9.581   8.646   17.057  1.00 27.34  ? 476  MET A CA    1 
ATOM   3669 C  C     . MET A 1 476 ? 8.466   9.462   16.425  1.00 28.58  ? 476  MET A C     1 
ATOM   3670 O  O     . MET A 1 476 ? 7.317   9.458   16.882  1.00 24.90  ? 476  MET A O     1 
ATOM   3671 C  CB    . MET A 1 476 ? 9.850   7.404   16.216  1.00 26.96  ? 476  MET A CB    1 
ATOM   3672 C  CG    . MET A 1 476 ? 8.647   6.574   15.892  1.00 39.00  ? 476  MET A CG    1 
ATOM   3673 S  SD    . MET A 1 476 ? 9.228   4.958   15.333  1.00 66.40  ? 476  MET A SD    1 
ATOM   3674 C  CE    . MET A 1 476 ? 10.591  5.442   14.272  1.00 52.37  ? 476  MET A CE    1 
ATOM   3675 N  N     . HIS A 1 477 ? 8.835   10.170  15.363  1.00 22.77  ? 477  HIS A N     1 
ATOM   3676 C  CA    . HIS A 1 477 ? 7.888   10.983  14.617  1.00 21.24  ? 477  HIS A CA    1 
ATOM   3677 C  C     . HIS A 1 477 ? 7.136   10.101  13.634  1.00 25.15  ? 477  HIS A C     1 
ATOM   3678 O  O     . HIS A 1 477 ? 7.744   9.272   12.946  1.00 22.59  ? 477  HIS A O     1 
ATOM   3679 C  CB    . HIS A 1 477 ? 8.625   12.091  13.870  1.00 21.71  ? 477  HIS A CB    1 
ATOM   3680 C  CG    . HIS A 1 477 ? 9.202   13.141  14.766  1.00 23.31  ? 477  HIS A CG    1 
ATOM   3681 N  ND1   . HIS A 1 477 ? 8.544   14.322  15.039  1.00 20.68  ? 477  HIS A ND1   1 
ATOM   3682 C  CD2   . HIS A 1 477 ? 10.357  13.181  15.472  1.00 22.14  ? 477  HIS A CD2   1 
ATOM   3683 C  CE1   . HIS A 1 477 ? 9.287   15.060  15.846  1.00 22.20  ? 477  HIS A CE1   1 
ATOM   3684 N  NE2   . HIS A 1 477 ? 10.387  14.389  16.132  1.00 22.53  ? 477  HIS A NE2   1 
ATOM   3685 N  N     . ASP A 1 478 ? 5.815   10.264  13.570  1.00 17.98  ? 478  ASP A N     1 
ATOM   3686 C  CA    . ASP A 1 478 ? 4.992   9.531   12.604  1.00 21.11  ? 478  ASP A CA    1 
ATOM   3687 C  C     . ASP A 1 478 ? 3.858   10.439  12.160  1.00 19.69  ? 478  ASP A C     1 
ATOM   3688 O  O     . ASP A 1 478 ? 2.694   10.264  12.556  1.00 20.61  ? 478  ASP A O     1 
ATOM   3689 C  CB    . ASP A 1 478 ? 4.473   8.217   13.201  1.00 20.03  ? 478  ASP A CB    1 
ATOM   3690 C  CG    . ASP A 1 478 ? 3.936   7.253   12.144  1.00 19.31  ? 478  ASP A CG    1 
ATOM   3691 O  OD1   . ASP A 1 478 ? 3.656   7.684   11.011  1.00 23.35  ? 478  ASP A OD1   1 
ATOM   3692 O  OD2   . ASP A 1 478 ? 3.756   6.062   12.456  1.00 21.58  ? 478  ASP A OD2   1 
ATOM   3693 N  N     . PRO A 1 479 ? 4.170   11.436  11.339  1.00 18.19  ? 479  PRO A N     1 
ATOM   3694 C  CA    . PRO A 1 479 ? 3.158   12.431  10.962  1.00 21.39  ? 479  PRO A CA    1 
ATOM   3695 C  C     . PRO A 1 479 ? 2.020   11.772  10.207  1.00 18.04  ? 479  PRO A C     1 
ATOM   3696 O  O     . PRO A 1 479 ? 2.246   10.998  9.271   1.00 17.59  ? 479  PRO A O     1 
ATOM   3697 C  CB    . PRO A 1 479 ? 3.932   13.417  10.068  1.00 18.91  ? 479  PRO A CB    1 
ATOM   3698 C  CG    . PRO A 1 479 ? 5.143   12.681  9.628   1.00 20.78  ? 479  PRO A CG    1 
ATOM   3699 C  CD    . PRO A 1 479 ? 5.473   11.679  10.689  1.00 21.08  ? 479  PRO A CD    1 
ATOM   3700 N  N     . PHE A 1 480 ? 0.797   12.078  10.639  1.00 17.74  ? 480  PHE A N     1 
ATOM   3701 C  CA    . PHE A 1 480 ? -0.442  11.597  10.032  1.00 19.57  ? 480  PHE A CA    1 
ATOM   3702 C  C     . PHE A 1 480 ? -0.578  10.082  10.095  1.00 19.79  ? 480  PHE A C     1 
ATOM   3703 O  O     . PHE A 1 480 ? -1.418  9.502   9.389   1.00 16.36  ? 480  PHE A O     1 
ATOM   3704 C  CB    . PHE A 1 480 ? -0.568  12.082  8.590   1.00 19.42  ? 480  PHE A CB    1 
ATOM   3705 C  CG    . PHE A 1 480 ? -0.902  13.538  8.486   1.00 22.01  ? 480  PHE A CG    1 
ATOM   3706 C  CD1   . PHE A 1 480 ? 0.086   14.500  8.639   1.00 21.34  ? 480  PHE A CD1   1 
ATOM   3707 C  CD2   . PHE A 1 480 ? -2.205  13.948  8.256   1.00 20.32  ? 480  PHE A CD2   1 
ATOM   3708 C  CE1   . PHE A 1 480 ? -0.210  15.832  8.548   1.00 19.39  ? 480  PHE A CE1   1 
ATOM   3709 C  CE2   . PHE A 1 480 ? -2.512  15.298  8.170   1.00 22.50  ? 480  PHE A CE2   1 
ATOM   3710 C  CZ    . PHE A 1 480 ? -1.515  16.237  8.318   1.00 20.71  ? 480  PHE A CZ    1 
ATOM   3711 N  N     . ALA A 1 481 ? 0.246   9.439   10.924  1.00 14.02  ? 481  ALA A N     1 
ATOM   3712 C  CA    . ALA A 1 481 ? 0.351   7.971   10.973  1.00 17.98  ? 481  ALA A CA    1 
ATOM   3713 C  C     . ALA A 1 481 ? 0.761   7.401   9.614   1.00 21.26  ? 481  ALA A C     1 
ATOM   3714 O  O     . ALA A 1 481 ? 0.480   6.240   9.301   1.00 16.64  ? 481  ALA A O     1 
ATOM   3715 C  CB    . ALA A 1 481 ? -0.948  7.323   11.463  1.00 21.86  ? 481  ALA A CB    1 
ATOM   3716 N  N     . MET A 1 482 ? 1.435   8.216   8.795   1.00 15.15  ? 482  MET A N     1 
ATOM   3717 C  CA    . MET A 1 482 ? 1.732   7.847   7.413   1.00 16.58  ? 482  MET A CA    1 
ATOM   3718 C  C     . MET A 1 482 ? 3.213   7.716   7.130   1.00 18.70  ? 482  MET A C     1 
ATOM   3719 O  O     . MET A 1 482 ? 3.587   7.543   5.963   1.00 21.24  ? 482  MET A O     1 
ATOM   3720 C  CB    . MET A 1 482 ? 1.146   8.871   6.443   1.00 20.08  ? 482  MET A CB    1 
ATOM   3721 C  CG    . MET A 1 482 ? -0.347  8.757   6.264   1.00 24.87  ? 482  MET A CG    1 
ATOM   3722 S  SD    . MET A 1 482 ? -0.733  7.397   5.160   1.00 20.23  ? 482  MET A SD    1 
ATOM   3723 C  CE    . MET A 1 482 ? -0.057  8.005   3.621   1.00 23.74  ? 482  MET A CE    1 
ATOM   3724 N  N     . ARG A 1 483 ? 4.073   7.788   8.144   1.00 19.31  ? 483  ARG A N     1 
ATOM   3725 C  CA    . ARG A 1 483 ? 5.508   7.780   7.874   1.00 16.78  ? 483  ARG A CA    1 
ATOM   3726 C  C     . ARG A 1 483 ? 5.965   6.606   6.999   1.00 20.73  ? 483  ARG A C     1 
ATOM   3727 O  O     . ARG A 1 483 ? 6.735   6.841   6.054   1.00 19.46  ? 483  ARG A O     1 
ATOM   3728 C  CB    . ARG A 1 483 ? 6.282   7.822   9.198   1.00 21.13  ? 483  ARG A CB    1 
ATOM   3729 C  CG    . ARG A 1 483 ? 7.777   8.084   8.980   1.00 25.12  ? 483  ARG A CG    1 
ATOM   3730 C  CD    . ARG A 1 483 ? 8.651   7.472   10.056  1.00 22.37  ? 483  ARG A CD    1 
ATOM   3731 N  NE    . ARG A 1 483 ? 8.467   6.031   10.153  1.00 33.50  ? 483  ARG A NE    1 
ATOM   3732 C  CZ    . ARG A 1 483 ? 7.920   5.424   11.196  1.00 36.54  ? 483  ARG A CZ    1 
ATOM   3733 N  NH1   . ARG A 1 483 ? 7.516   6.108   12.252  1.00 32.23  ? 483  ARG A NH1   1 
ATOM   3734 N  NH2   . ARG A 1 483 ? 7.787   4.096   11.182  1.00 37.46  ? 483  ARG A NH2   1 
ATOM   3735 N  N     . PRO A 1 484 ? 5.536   5.354   7.223   1.00 21.49  ? 484  PRO A N     1 
ATOM   3736 C  CA    . PRO A 1 484 ? 5.973   4.270   6.329   1.00 19.87  ? 484  PRO A CA    1 
ATOM   3737 C  C     . PRO A 1 484 ? 5.258   4.243   4.991   1.00 19.91  ? 484  PRO A C     1 
ATOM   3738 O  O     . PRO A 1 484 ? 5.611   3.413   4.142   1.00 22.93  ? 484  PRO A O     1 
ATOM   3739 C  CB    . PRO A 1 484 ? 5.641   2.988   7.131   1.00 23.45  ? 484  PRO A CB    1 
ATOM   3740 C  CG    . PRO A 1 484 ? 5.155   3.450   8.492   1.00 24.89  ? 484  PRO A CG    1 
ATOM   3741 C  CD    . PRO A 1 484 ? 4.659   4.838   8.296   1.00 21.26  ? 484  PRO A CD    1 
ATOM   3742 N  N     . PHE A 1 485 ? 4.257   5.093   4.781   1.00 19.46  ? 485  PHE A N     1 
ATOM   3743 C  CA    . PHE A 1 485 ? 3.327   4.935   3.673   1.00 21.32  ? 485  PHE A CA    1 
ATOM   3744 C  C     . PHE A 1 485 ? 3.267   6.109   2.705   1.00 21.30  ? 485  PHE A C     1 
ATOM   3745 O  O     . PHE A 1 485 ? 2.464   6.069   1.764   1.00 21.76  ? 485  PHE A O     1 
ATOM   3746 C  CB    . PHE A 1 485 ? 1.918   4.652   4.227   1.00 21.99  ? 485  PHE A CB    1 
ATOM   3747 C  CG    . PHE A 1 485 ? 1.886   3.519   5.221   1.00 19.92  ? 485  PHE A CG    1 
ATOM   3748 C  CD1   . PHE A 1 485 ? 2.302   2.240   4.852   1.00 19.64  ? 485  PHE A CD1   1 
ATOM   3749 C  CD2   . PHE A 1 485 ? 1.447   3.726   6.522   1.00 18.50  ? 485  PHE A CD2   1 
ATOM   3750 C  CE1   . PHE A 1 485 ? 2.284   1.189   5.770   1.00 19.56  ? 485  PHE A CE1   1 
ATOM   3751 C  CE2   . PHE A 1 485 ? 1.436   2.682   7.445   1.00 20.16  ? 485  PHE A CE2   1 
ATOM   3752 C  CZ    . PHE A 1 485 ? 1.836   1.416   7.072   1.00 20.79  ? 485  PHE A CZ    1 
ATOM   3753 N  N     . PHE A 1 486 ? 4.084   7.146   2.874   1.00 16.91  ? 486  PHE A N     1 
ATOM   3754 C  CA    . PHE A 1 486 ? 4.016   8.250   1.925   1.00 21.81  ? 486  PHE A CA    1 
ATOM   3755 C  C     . PHE A 1 486 ? 4.399   7.786   0.528   1.00 17.56  ? 486  PHE A C     1 
ATOM   3756 O  O     . PHE A 1 486 ? 5.408   7.112   0.342   1.00 26.70  ? 486  PHE A O     1 
ATOM   3757 C  CB    . PHE A 1 486 ? 4.917   9.407   2.355   1.00 21.66  ? 486  PHE A CB    1 
ATOM   3758 C  CG    . PHE A 1 486 ? 4.430   10.112  3.564   1.00 16.96  ? 486  PHE A CG    1 
ATOM   3759 C  CD1   . PHE A 1 486 ? 3.237   10.805  3.534   1.00 19.64  ? 486  PHE A CD1   1 
ATOM   3760 C  CD2   . PHE A 1 486 ? 5.157   10.076  4.742   1.00 19.15  ? 486  PHE A CD2   1 
ATOM   3761 C  CE1   . PHE A 1 486 ? 2.782   11.462  4.654   1.00 18.71  ? 486  PHE A CE1   1 
ATOM   3762 C  CE2   . PHE A 1 486 ? 4.702   10.736  5.864   1.00 17.27  ? 486  PHE A CE2   1 
ATOM   3763 C  CZ    . PHE A 1 486 ? 3.520   11.430  5.821   1.00 17.49  ? 486  PHE A CZ    1 
ATOM   3764 N  N     . GLY A 1 487 ? 3.571   8.136   -0.452  1.00 21.38  ? 487  GLY A N     1 
ATOM   3765 C  CA    . GLY A 1 487 ? 3.877   7.830   -1.831  1.00 21.41  ? 487  GLY A CA    1 
ATOM   3766 C  C     . GLY A 1 487 ? 4.662   8.905   -2.539  1.00 27.19  ? 487  GLY A C     1 
ATOM   3767 O  O     . GLY A 1 487 ? 5.169   8.666   -3.638  1.00 25.92  ? 487  GLY A O     1 
ATOM   3768 N  N     . TYR A 1 488 ? 4.775   10.083  -1.925  1.00 24.03  ? 488  TYR A N     1 
ATOM   3769 C  CA    . TYR A 1 488 ? 5.439   11.228  -2.535  1.00 25.93  ? 488  TYR A CA    1 
ATOM   3770 C  C     . TYR A 1 488 ? 5.888   12.181  -1.433  1.00 28.61  ? 488  TYR A C     1 
ATOM   3771 O  O     . TYR A 1 488 ? 5.650   11.952  -0.242  1.00 23.68  ? 488  TYR A O     1 
ATOM   3772 C  CB    . TYR A 1 488 ? 4.519   11.929  -3.543  1.00 24.77  ? 488  TYR A CB    1 
ATOM   3773 C  CG    . TYR A 1 488 ? 3.288   12.543  -2.924  1.00 23.35  ? 488  TYR A CG    1 
ATOM   3774 C  CD1   . TYR A 1 488 ? 2.231   11.750  -2.479  1.00 25.23  ? 488  TYR A CD1   1 
ATOM   3775 C  CD2   . TYR A 1 488 ? 3.179   13.926  -2.777  1.00 24.06  ? 488  TYR A CD2   1 
ATOM   3776 C  CE1   . TYR A 1 488 ? 1.098   12.329  -1.900  1.00 23.60  ? 488  TYR A CE1   1 
ATOM   3777 C  CE2   . TYR A 1 488 ? 2.056   14.508  -2.218  1.00 25.37  ? 488  TYR A CE2   1 
ATOM   3778 C  CZ    . TYR A 1 488 ? 1.020   13.708  -1.777  1.00 27.24  ? 488  TYR A CZ    1 
ATOM   3779 O  OH    . TYR A 1 488 ? -0.085  14.310  -1.215  1.00 22.72  ? 488  TYR A OH    1 
ATOM   3780 N  N     . ASN A 1 489 ? 6.543   13.261  -1.863  1.00 24.00  ? 489  ASN A N     1 
ATOM   3781 C  CA    . ASN A 1 489 ? 7.117   14.296  -1.010  1.00 23.79  ? 489  ASN A CA    1 
ATOM   3782 C  C     . ASN A 1 489 ? 6.151   14.750  0.089   1.00 19.30  ? 489  ASN A C     1 
ATOM   3783 O  O     . ASN A 1 489 ? 5.059   15.237  -0.194  1.00 22.32  ? 489  ASN A O     1 
ATOM   3784 C  CB    . ASN A 1 489 ? 7.512   15.473  -1.917  1.00 21.01  ? 489  ASN A CB    1 
ATOM   3785 C  CG    . ASN A 1 489 ? 8.255   16.566  -1.193  1.00 28.30  ? 489  ASN A CG    1 
ATOM   3786 O  OD1   . ASN A 1 489 ? 7.774   17.115  -0.209  1.00 27.36  ? 489  ASN A OD1   1 
ATOM   3787 N  ND2   . ASN A 1 489 ? 9.436   16.916  -1.705  1.00 27.25  ? 489  ASN A ND2   1 
ATOM   3788 N  N     . PHE A 1 490 ? 6.568   14.578  1.347   1.00 22.70  ? 490  PHE A N     1 
ATOM   3789 C  CA    . PHE A 1 490 ? 5.706   14.892  2.485   1.00 23.00  ? 490  PHE A CA    1 
ATOM   3790 C  C     . PHE A 1 490 ? 5.393   16.380  2.559   1.00 21.49  ? 490  PHE A C     1 
ATOM   3791 O  O     . PHE A 1 490 ? 4.278   16.764  2.933   1.00 21.20  ? 490  PHE A O     1 
ATOM   3792 C  CB    . PHE A 1 490 ? 6.378   14.400  3.769   1.00 22.85  ? 490  PHE A CB    1 
ATOM   3793 C  CG    . PHE A 1 490 ? 5.723   14.885  5.041   1.00 24.46  ? 490  PHE A CG    1 
ATOM   3794 C  CD1   . PHE A 1 490 ? 4.423   14.514  5.358   1.00 18.27  ? 490  PHE A CD1   1 
ATOM   3795 C  CD2   . PHE A 1 490 ? 6.427   15.673  5.940   1.00 20.43  ? 490  PHE A CD2   1 
ATOM   3796 C  CE1   . PHE A 1 490 ? 3.813   14.953  6.537   1.00 19.92  ? 490  PHE A CE1   1 
ATOM   3797 C  CE2   . PHE A 1 490 ? 5.829   16.109  7.124   1.00 26.23  ? 490  PHE A CE2   1 
ATOM   3798 C  CZ    . PHE A 1 490 ? 4.516   15.737  7.427   1.00 18.68  ? 490  PHE A CZ    1 
ATOM   3799 N  N     . GLY A 1 491 ? 6.348   17.237  2.187   1.00 23.71  ? 491  GLY A N     1 
ATOM   3800 C  CA    . GLY A 1 491 ? 6.051   18.664  2.135   1.00 19.42  ? 491  GLY A CA    1 
ATOM   3801 C  C     . GLY A 1 491 ? 4.904   18.971  1.191   1.00 20.13  ? 491  GLY A C     1 
ATOM   3802 O  O     . GLY A 1 491 ? 4.025   19.784  1.503   1.00 21.92  ? 491  GLY A O     1 
ATOM   3803 N  N     . LYS A 1 492 ? 4.890   18.316  0.029   1.00 19.36  ? 492  LYS A N     1 
ATOM   3804 C  CA    . LYS A 1 492 ? 3.772   18.478  -0.900  1.00 18.53  ? 492  LYS A CA    1 
ATOM   3805 C  C     . LYS A 1 492 ? 2.488   17.854  -0.350  1.00 19.32  ? 492  LYS A C     1 
ATOM   3806 O  O     . LYS A 1 492 ? 1.397   18.341  -0.645  1.00 24.57  ? 492  LYS A O     1 
ATOM   3807 C  CB    . LYS A 1 492 ? 4.108   17.850  -2.251  1.00 20.50  ? 492  LYS A CB    1 
ATOM   3808 C  CG    . LYS A 1 492 ? 5.365   18.431  -2.936  1.00 28.46  ? 492  LYS A CG    1 
ATOM   3809 C  CD    . LYS A 1 492 ? 5.327   19.962  -2.924  1.00 33.09  ? 492  LYS A CD    1 
ATOM   3810 C  CE    . LYS A 1 492 ? 6.684   20.559  -3.313  1.00 42.38  ? 492  LYS A CE    1 
ATOM   3811 N  NZ    . LYS A 1 492 ? 6.926   21.854  -2.615  1.00 41.29  ? 492  LYS A NZ    1 
ATOM   3812 N  N     . TYR A 1 493 ? 2.602   16.758  0.403   1.00 18.07  ? 493  TYR A N     1 
ATOM   3813 C  CA    . TYR A 1 493 ? 1.440   16.187  1.087   1.00 20.34  ? 493  TYR A CA    1 
ATOM   3814 C  C     . TYR A 1 493 ? 0.820   17.193  2.056   1.00 18.71  ? 493  TYR A C     1 
ATOM   3815 O  O     . TYR A 1 493 ? -0.406  17.357  2.092   1.00 20.41  ? 493  TYR A O     1 
ATOM   3816 C  CB    . TYR A 1 493 ? 1.873   14.897  1.797   1.00 21.97  ? 493  TYR A CB    1 
ATOM   3817 C  CG    . TYR A 1 493 ? 0.884   14.247  2.753   1.00 19.98  ? 493  TYR A CG    1 
ATOM   3818 C  CD1   . TYR A 1 493 ? 0.822   14.636  4.089   1.00 20.13  ? 493  TYR A CD1   1 
ATOM   3819 C  CD2   . TYR A 1 493 ? 0.066   13.201  2.334   1.00 21.99  ? 493  TYR A CD2   1 
ATOM   3820 C  CE1   . TYR A 1 493 ? -0.047  14.033  4.973   1.00 20.36  ? 493  TYR A CE1   1 
ATOM   3821 C  CE2   . TYR A 1 493 ? -0.815  12.577  3.222   1.00 22.05  ? 493  TYR A CE2   1 
ATOM   3822 C  CZ    . TYR A 1 493 ? -0.861  13.003  4.535   1.00 20.41  ? 493  TYR A CZ    1 
ATOM   3823 O  OH    . TYR A 1 493 ? -1.725  12.407  5.419   1.00 18.88  ? 493  TYR A OH    1 
ATOM   3824 N  N     . LEU A 1 494 ? 1.649   17.900  2.830   1.00 20.34  ? 494  LEU A N     1 
ATOM   3825 C  CA    . LEU A 1 494 ? 1.124   18.939  3.718   1.00 20.09  ? 494  LEU A CA    1 
ATOM   3826 C  C     . LEU A 1 494 ? 0.431   20.048  2.936   1.00 18.55  ? 494  LEU A C     1 
ATOM   3827 O  O     . LEU A 1 494 ? -0.646  20.510  3.328   1.00 20.40  ? 494  LEU A O     1 
ATOM   3828 C  CB    . LEU A 1 494 ? 2.245   19.520  4.580   1.00 17.74  ? 494  LEU A CB    1 
ATOM   3829 C  CG    . LEU A 1 494 ? 2.825   18.562  5.620   1.00 20.70  ? 494  LEU A CG    1 
ATOM   3830 C  CD1   . LEU A 1 494 ? 4.106   19.137  6.211   1.00 22.51  ? 494  LEU A CD1   1 
ATOM   3831 C  CD2   . LEU A 1 494 ? 1.793   18.304  6.716   1.00 18.03  ? 494  LEU A CD2   1 
ATOM   3832 N  N     . ALA A 1 495 ? 1.035   20.504  1.826   1.00 22.33  ? 495  ALA A N     1 
ATOM   3833 C  CA    . ALA A 1 495 ? 0.388   21.548  1.032   1.00 21.94  ? 495  ALA A CA    1 
ATOM   3834 C  C     . ALA A 1 495 ? -0.937  21.055  0.473   1.00 19.43  ? 495  ALA A C     1 
ATOM   3835 O  O     . ALA A 1 495 ? -1.896  21.824  0.358   1.00 26.57  ? 495  ALA A O     1 
ATOM   3836 C  CB    . ALA A 1 495 ? 1.317   22.008  -0.106  1.00 24.51  ? 495  ALA A CB    1 
ATOM   3837 N  N     . HIS A 1 496 ? -1.009  19.762  0.159   1.00 23.91  ? 496  HIS A N     1 
ATOM   3838 C  CA    . HIS A 1 496 ? -2.247  19.153  -0.314  1.00 26.09  ? 496  HIS A CA    1 
ATOM   3839 C  C     . HIS A 1 496 ? -3.347  19.250  0.743   1.00 24.36  ? 496  HIS A C     1 
ATOM   3840 O  O     . HIS A 1 496 ? -4.461  19.706  0.459   1.00 21.90  ? 496  HIS A O     1 
ATOM   3841 C  CB    . HIS A 1 496 ? -1.959  17.695  -0.702  1.00 22.56  ? 496  HIS A CB    1 
ATOM   3842 C  CG    . HIS A 1 496 ? -3.061  17.032  -1.464  1.00 29.72  ? 496  HIS A CG    1 
ATOM   3843 N  ND1   . HIS A 1 496 ? -3.610  17.578  -2.603  1.00 29.03  ? 496  HIS A ND1   1 
ATOM   3844 C  CD2   . HIS A 1 496 ? -3.711  15.862  -1.255  1.00 25.45  ? 496  HIS A CD2   1 
ATOM   3845 C  CE1   . HIS A 1 496 ? -4.557  16.776  -3.060  1.00 30.49  ? 496  HIS A CE1   1 
ATOM   3846 N  NE2   . HIS A 1 496 ? -4.635  15.726  -2.262  1.00 29.93  ? 496  HIS A NE2   1 
ATOM   3847 N  N     . TRP A 1 497 ? -3.046  18.829  1.975   1.00 22.26  ? 497  TRP A N     1 
ATOM   3848 C  CA    . TRP A 1 497 ? -4.011  18.954  3.065   1.00 19.67  ? 497  TRP A CA    1 
ATOM   3849 C  C     . TRP A 1 497 ? -4.401  20.408  3.302   1.00 23.98  ? 497  TRP A C     1 
ATOM   3850 O  O     . TRP A 1 497 ? -5.583  20.723  3.482   1.00 25.33  ? 497  TRP A O     1 
ATOM   3851 C  CB    . TRP A 1 497 ? -3.433  18.351  4.343   1.00 17.43  ? 497  TRP A CB    1 
ATOM   3852 C  CG    . TRP A 1 497 ? -3.743  16.913  4.518   1.00 18.87  ? 497  TRP A CG    1 
ATOM   3853 C  CD1   . TRP A 1 497 ? -3.098  15.863  3.934   1.00 20.06  ? 497  TRP A CD1   1 
ATOM   3854 C  CD2   . TRP A 1 497 ? -4.780  16.350  5.331   1.00 21.02  ? 497  TRP A CD2   1 
ATOM   3855 N  NE1   . TRP A 1 497 ? -3.668  14.683  4.334   1.00 21.98  ? 497  TRP A NE1   1 
ATOM   3856 C  CE2   . TRP A 1 497 ? -4.701  14.951  5.193   1.00 22.50  ? 497  TRP A CE2   1 
ATOM   3857 C  CE3   . TRP A 1 497 ? -5.764  16.894  6.168   1.00 18.54  ? 497  TRP A CE3   1 
ATOM   3858 C  CZ2   . TRP A 1 497 ? -5.561  14.076  5.873   1.00 18.40  ? 497  TRP A CZ2   1 
ATOM   3859 C  CZ3   . TRP A 1 497 ? -6.630  16.033  6.835   1.00 20.84  ? 497  TRP A CZ3   1 
ATOM   3860 C  CH2   . TRP A 1 497 ? -6.524  14.632  6.675   1.00 23.20  ? 497  TRP A CH2   1 
ATOM   3861 N  N     . LEU A 1 498 ? -3.416  21.312  3.309   1.00 24.62  ? 498  LEU A N     1 
ATOM   3862 C  CA    . LEU A 1 498 ? -3.713  22.719  3.576   1.00 22.75  ? 498  LEU A CA    1 
ATOM   3863 C  C     . LEU A 1 498 ? -4.594  23.311  2.491   1.00 21.19  ? 498  LEU A C     1 
ATOM   3864 O  O     . LEU A 1 498 ? -5.448  24.158  2.778   1.00 26.57  ? 498  LEU A O     1 
ATOM   3865 C  CB    . LEU A 1 498 ? -2.417  23.518  3.689   1.00 20.22  ? 498  LEU A CB    1 
ATOM   3866 C  CG    . LEU A 1 498 ? -1.568  23.249  4.931   1.00 21.34  ? 498  LEU A CG    1 
ATOM   3867 C  CD1   . LEU A 1 498 ? -0.148  23.742  4.708   1.00 25.17  ? 498  LEU A CD1   1 
ATOM   3868 C  CD2   . LEU A 1 498 ? -2.187  23.943  6.130   1.00 21.41  ? 498  LEU A CD2   1 
ATOM   3869 N  N     . SER A 1 499 ? -4.420  22.849  1.249   1.00 24.76  ? 499  SER A N     1 
ATOM   3870 C  CA    . SER A 1 499 ? -5.196  23.361  0.126   1.00 26.77  ? 499  SER A CA    1 
ATOM   3871 C  C     . SER A 1 499 ? -6.671  23.019  0.227   1.00 31.68  ? 499  SER A C     1 
ATOM   3872 O  O     . SER A 1 499 ? -7.481  23.615  -0.494  1.00 33.61  ? 499  SER A O     1 
ATOM   3873 C  CB    . SER A 1 499 ? -4.634  22.831  -1.194  1.00 28.51  ? 499  SER A CB    1 
ATOM   3874 O  OG    . SER A 1 499 ? -4.960  21.466  -1.393  1.00 36.34  ? 499  SER A OG    1 
ATOM   3875 N  N     A MET A 1 500 ? -7.049  22.086  1.103   0.52 28.37  ? 500  MET A N     1 
ATOM   3876 N  N     B MET A 1 500 ? -7.043  22.074  1.095   0.48 28.37  ? 500  MET A N     1 
ATOM   3877 C  CA    A MET A 1 500 ? -8.465  21.764  1.247   0.52 28.94  ? 500  MET A CA    1 
ATOM   3878 C  CA    B MET A 1 500 ? -8.457  21.758  1.278   0.48 28.95  ? 500  MET A CA    1 
ATOM   3879 C  C     A MET A 1 500 ? -9.252  22.930  1.834   0.52 31.04  ? 500  MET A C     1 
ATOM   3880 C  C     B MET A 1 500 ? -9.233  22.965  1.787   0.48 31.02  ? 500  MET A C     1 
ATOM   3881 O  O     A MET A 1 500 ? -10.447 23.074  1.550   0.52 35.24  ? 500  MET A O     1 
ATOM   3882 O  O     B MET A 1 500 ? -10.393 23.172  1.411   0.48 35.08  ? 500  MET A O     1 
ATOM   3883 C  CB    A MET A 1 500 ? -8.627  20.508  2.098   0.52 27.23  ? 500  MET A CB    1 
ATOM   3884 C  CB    B MET A 1 500 ? -8.609  20.578  2.234   0.48 27.15  ? 500  MET A CB    1 
ATOM   3885 C  CG    A MET A 1 500 ? -7.977  19.272  1.474   0.52 28.02  ? 500  MET A CG    1 
ATOM   3886 C  CG    B MET A 1 500 ? -8.208  19.245  1.622   0.48 28.11  ? 500  MET A CG    1 
ATOM   3887 S  SD    A MET A 1 500 ? -8.598  18.894  -0.182  0.52 35.12  ? 500  MET A SD    1 
ATOM   3888 S  SD    B MET A 1 500 ? -7.914  17.958  2.848   0.48 24.22  ? 500  MET A SD    1 
ATOM   3889 C  CE    A MET A 1 500 ? -7.330  17.794  -0.804  0.52 27.37  ? 500  MET A CE    1 
ATOM   3890 C  CE    B MET A 1 500 ? -9.551  17.739  3.536   0.48 26.33  ? 500  MET A CE    1 
ATOM   3891 N  N     . ALA A 1 501 ? -8.603  23.784  2.628   1.00 25.54  ? 501  ALA A N     1 
ATOM   3892 C  CA    . ALA A 1 501 ? -9.254  24.973  3.166   1.00 30.57  ? 501  ALA A CA    1 
ATOM   3893 C  C     . ALA A 1 501 ? -9.490  26.065  2.117   1.00 38.39  ? 501  ALA A C     1 
ATOM   3894 O  O     . ALA A 1 501 ? -10.182 27.044  2.417   1.00 32.52  ? 501  ALA A O     1 
ATOM   3895 C  CB    . ALA A 1 501 ? -8.417  25.538  4.317   1.00 32.94  ? 501  ALA A CB    1 
ATOM   3896 N  N     . HIS A 1 502 ? -8.935  25.930  0.908   1.00 40.12  ? 502  HIS A N     1 
ATOM   3897 C  CA    . HIS A 1 502 ? -9.139  26.900  -0.165  1.00 42.96  ? 502  HIS A CA    1 
ATOM   3898 C  C     . HIS A 1 502 ? -10.350 26.589  -1.038  1.00 50.63  ? 502  HIS A C     1 
ATOM   3899 O  O     . HIS A 1 502 ? -10.748 27.441  -1.841  1.00 58.31  ? 502  HIS A O     1 
ATOM   3900 C  CB    . HIS A 1 502 ? -7.903  26.968  -1.074  1.00 41.68  ? 502  HIS A CB    1 
ATOM   3901 C  CG    . HIS A 1 502 ? -6.639  27.330  -0.361  1.00 42.86  ? 502  HIS A CG    1 
ATOM   3902 N  ND1   . HIS A 1 502 ? -5.408  27.320  -0.982  1.00 51.90  ? 502  HIS A ND1   1 
ATOM   3903 C  CD2   . HIS A 1 502 ? -6.413  27.712  0.918   1.00 37.71  ? 502  HIS A CD2   1 
ATOM   3904 C  CE1   . HIS A 1 502 ? -4.478  27.682  -0.115  1.00 48.07  ? 502  HIS A CE1   1 
ATOM   3905 N  NE2   . HIS A 1 502 ? -5.062  27.926  1.044   1.00 44.15  ? 502  HIS A NE2   1 
ATOM   3906 N  N     . ARG A 1 503 ? -10.929 25.390  -0.920  1.00 50.31  ? 503  ARG A N     1 
ATOM   3907 C  CA    . ARG A 1 503 ? -12.015 24.974  -1.797  1.00 60.38  ? 503  ARG A CA    1 
ATOM   3908 C  C     . ARG A 1 503 ? -13.317 25.677  -1.415  1.00 71.63  ? 503  ARG A C     1 
ATOM   3909 O  O     . ARG A 1 503 ? -13.568 25.923  -0.231  1.00 61.04  ? 503  ARG A O     1 
ATOM   3910 C  CB    . ARG A 1 503 ? -12.211 23.469  -1.725  1.00 56.32  ? 503  ARG A CB    1 
ATOM   3911 C  CG    . ARG A 1 503 ? -10.977 22.673  -2.067  1.00 57.16  ? 503  ARG A CG    1 
ATOM   3912 C  CD    . ARG A 1 503 ? -11.250 21.208  -1.850  1.00 55.26  ? 503  ARG A CD    1 
ATOM   3913 N  NE    . ARG A 1 503 ? -12.338 20.728  -2.692  1.00 63.13  ? 503  ARG A NE    1 
ATOM   3914 C  CZ    . ARG A 1 503 ? -12.167 19.970  -3.767  1.00 68.80  ? 503  ARG A CZ    1 
ATOM   3915 N  NH1   . ARG A 1 503 ? -10.959 19.600  -4.167  1.00 62.87  ? 503  ARG A NH1   1 
ATOM   3916 N  NH2   . ARG A 1 503 ? -13.234 19.564  -4.452  1.00 66.67  ? 503  ARG A NH2   1 
ATOM   3917 N  N     . PRO A 1 504 ? -14.156 26.005  -2.397  1.00 92.83  ? 504  PRO A N     1 
ATOM   3918 C  CA    . PRO A 1 504 ? -15.434 26.656  -2.088  1.00 94.45  ? 504  PRO A CA    1 
ATOM   3919 C  C     . PRO A 1 504 ? -16.429 25.666  -1.503  1.00 95.07  ? 504  PRO A C     1 
ATOM   3920 O  O     . PRO A 1 504 ? -16.485 24.501  -1.905  1.00 95.99  ? 504  PRO A O     1 
ATOM   3921 C  CB    . PRO A 1 504 ? -15.907 27.185  -3.449  1.00 101.08 ? 504  PRO A CB    1 
ATOM   3922 C  CG    . PRO A 1 504 ? -14.714 27.069  -4.367  1.00 100.69 ? 504  PRO A CG    1 
ATOM   3923 C  CD    . PRO A 1 504 ? -13.921 25.917  -3.846  1.00 94.04  ? 504  PRO A CD    1 
ATOM   3924 N  N     . ALA A 1 505 ? -17.214 26.148  -0.539  1.00 81.45  ? 505  ALA A N     1 
ATOM   3925 C  CA    . ALA A 1 505 ? -18.234 25.359  0.150   1.00 70.43  ? 505  ALA A CA    1 
ATOM   3926 C  C     . ALA A 1 505 ? -17.655 24.124  0.834   1.00 57.13  ? 505  ALA A C     1 
ATOM   3927 O  O     . ALA A 1 505 ? -18.402 23.212  1.197   1.00 54.25  ? 505  ALA A O     1 
ATOM   3928 C  CB    . ALA A 1 505 ? -19.367 24.951  -0.802  1.00 65.40  ? 505  ALA A CB    1 
ATOM   3929 N  N     . ALA A 1 506 ? -16.336 24.070  1.015   1.00 54.41  ? 506  ALA A N     1 
ATOM   3930 C  CA    . ALA A 1 506 ? -15.717 22.949  1.709   1.00 48.81  ? 506  ALA A CA    1 
ATOM   3931 C  C     . ALA A 1 506 ? -16.183 22.927  3.159   1.00 44.61  ? 506  ALA A C     1 
ATOM   3932 O  O     . ALA A 1 506 ? -15.990 23.900  3.895   1.00 43.10  ? 506  ALA A O     1 
ATOM   3933 C  CB    . ALA A 1 506 ? -14.196 23.050  1.633   1.00 47.20  ? 506  ALA A CB    1 
ATOM   3934 N  N     . LYS A 1 507 ? -16.829 21.833  3.564   1.00 41.55  ? 507  LYS A N     1 
ATOM   3935 C  CA    . LYS A 1 507 ? -17.236 21.656  4.959   1.00 34.38  ? 507  LYS A CA    1 
ATOM   3936 C  C     . LYS A 1 507 ? -16.122 20.886  5.651   1.00 35.46  ? 507  LYS A C     1 
ATOM   3937 O  O     . LYS A 1 507 ? -16.105 19.655  5.671   1.00 35.69  ? 507  LYS A O     1 
ATOM   3938 C  CB    . LYS A 1 507 ? -18.574 20.933  5.052   1.00 35.31  ? 507  LYS A CB    1 
ATOM   3939 C  CG    . LYS A 1 507 ? -19.711 21.652  4.342   1.00 41.77  ? 507  LYS A CG    1 
ATOM   3940 C  CD    . LYS A 1 507 ? -20.870 20.704  4.099   1.00 44.75  ? 507  LYS A CD    1 
ATOM   3941 C  CE    . LYS A 1 507 ? -21.980 21.361  3.301   1.00 45.68  ? 507  LYS A CE    1 
ATOM   3942 N  NZ    . LYS A 1 507 ? -22.961 20.331  2.847   1.00 52.12  ? 507  LYS A NZ    1 
ATOM   3943 N  N     . LEU A 1 508 ? -15.185 21.625  6.225   1.00 28.32  ? 508  LEU A N     1 
ATOM   3944 C  CA    . LEU A 1 508 ? -13.982 21.036  6.806   1.00 28.96  ? 508  LEU A CA    1 
ATOM   3945 C  C     . LEU A 1 508 ? -14.317 20.375  8.139   1.00 30.73  ? 508  LEU A C     1 
ATOM   3946 O  O     . LEU A 1 508 ? -14.942 21.007  8.990   1.00 25.56  ? 508  LEU A O     1 
ATOM   3947 C  CB    . LEU A 1 508 ? -12.931 22.117  7.011   1.00 26.62  ? 508  LEU A CB    1 
ATOM   3948 C  CG    . LEU A 1 508 ? -12.458 22.792  5.719   1.00 29.19  ? 508  LEU A CG    1 
ATOM   3949 C  CD1   . LEU A 1 508 ? -11.499 23.923  6.030   1.00 31.01  ? 508  LEU A CD1   1 
ATOM   3950 C  CD2   . LEU A 1 508 ? -11.808 21.769  4.829   1.00 24.96  ? 508  LEU A CD2   1 
ATOM   3951 N  N     . PRO A 1 509 ? -13.914 19.126  8.364   1.00 26.83  ? 509  PRO A N     1 
ATOM   3952 C  CA    . PRO A 1 509 ? -14.226 18.482  9.645   1.00 23.12  ? 509  PRO A CA    1 
ATOM   3953 C  C     . PRO A 1 509 ? -13.410 19.089  10.779  1.00 25.93  ? 509  PRO A C     1 
ATOM   3954 O  O     . PRO A 1 509 ? -12.373 19.725  10.567  1.00 21.25  ? 509  PRO A O     1 
ATOM   3955 C  CB    . PRO A 1 509 ? -13.848 17.015  9.410   1.00 21.35  ? 509  PRO A CB    1 
ATOM   3956 C  CG    . PRO A 1 509 ? -12.786 17.069  8.355   1.00 20.99  ? 509  PRO A CG    1 
ATOM   3957 C  CD    . PRO A 1 509 ? -13.140 18.246  7.467   1.00 22.07  ? 509  PRO A CD    1 
ATOM   3958 N  N     . LYS A 1 510 ? -13.898 18.893  12.002  1.00 20.48  ? 510  LYS A N     1 
ATOM   3959 C  CA    . LYS A 1 510 ? -13.100 19.246  13.170  1.00 20.09  ? 510  LYS A CA    1 
ATOM   3960 C  C     . LYS A 1 510 ? -11.938 18.271  13.285  1.00 23.57  ? 510  LYS A C     1 
ATOM   3961 O  O     . LYS A 1 510 ? -12.024 17.125  12.841  1.00 21.26  ? 510  LYS A O     1 
ATOM   3962 C  CB    . LYS A 1 510 ? -13.939 19.201  14.446  1.00 19.05  ? 510  LYS A CB    1 
ATOM   3963 C  CG    . LYS A 1 510 ? -14.580 20.526  14.849  1.00 30.02  ? 510  LYS A CG    1 
ATOM   3964 C  CD    . LYS A 1 510 ? -15.514 20.285  16.029  1.00 31.86  ? 510  LYS A CD    1 
ATOM   3965 C  CE    . LYS A 1 510 ? -15.606 21.486  16.935  1.00 41.05  ? 510  LYS A CE    1 
ATOM   3966 N  NZ    . LYS A 1 510 ? -15.686 22.742  16.186  1.00 31.30  ? 510  LYS A NZ    1 
ATOM   3967 N  N     . ILE A 1 511 ? -10.839 18.730  13.878  1.00 18.48  ? 511  ILE A N     1 
ATOM   3968 C  CA    . ILE A 1 511 ? -9.643  17.909  14.037  1.00 17.59  ? 511  ILE A CA    1 
ATOM   3969 C  C     . ILE A 1 511 ? -9.316  17.810  15.521  1.00 22.24  ? 511  ILE A C     1 
ATOM   3970 O  O     . ILE A 1 511 ? -9.228  18.834  16.213  1.00 18.74  ? 511  ILE A O     1 
ATOM   3971 C  CB    . ILE A 1 511 ? -8.454  18.475  13.237  1.00 19.00  ? 511  ILE A CB    1 
ATOM   3972 C  CG1   . ILE A 1 511 ? -8.642  18.189  11.746  1.00 18.90  ? 511  ILE A CG1   1 
ATOM   3973 C  CG2   . ILE A 1 511 ? -7.130  17.916  13.752  1.00 18.66  ? 511  ILE A CG2   1 
ATOM   3974 C  CD1   . ILE A 1 511 ? -7.605  18.895  10.848  1.00 20.47  ? 511  ILE A CD1   1 
ATOM   3975 N  N     . PHE A 1 512 ? -9.180  16.575  16.014  1.00 16.45  ? 512  PHE A N     1 
ATOM   3976 C  CA    . PHE A 1 512 ? -8.874  16.281  17.405  1.00 15.56  ? 512  PHE A CA    1 
ATOM   3977 C  C     . PHE A 1 512 ? -7.581  15.485  17.487  1.00 17.03  ? 512  PHE A C     1 
ATOM   3978 O  O     . PHE A 1 512 ? -7.202  14.793  16.536  1.00 20.94  ? 512  PHE A O     1 
ATOM   3979 C  CB    . PHE A 1 512 ? -9.997  15.453  18.070  1.00 16.93  ? 512  PHE A CB    1 
ATOM   3980 C  CG    . PHE A 1 512 ? -11.368 16.076  17.981  1.00 18.55  ? 512  PHE A CG    1 
ATOM   3981 C  CD1   . PHE A 1 512 ? -11.808 16.973  18.951  1.00 15.42  ? 512  PHE A CD1   1 
ATOM   3982 C  CD2   . PHE A 1 512 ? -12.226 15.748  16.943  1.00 17.61  ? 512  PHE A CD2   1 
ATOM   3983 C  CE1   . PHE A 1 512 ? -13.083 17.537  18.880  1.00 19.75  ? 512  PHE A CE1   1 
ATOM   3984 C  CE2   . PHE A 1 512 ? -13.503 16.314  16.864  1.00 17.53  ? 512  PHE A CE2   1 
ATOM   3985 C  CZ    . PHE A 1 512 ? -13.934 17.197  17.830  1.00 15.40  ? 512  PHE A CZ    1 
ATOM   3986 N  N     . HIS A 1 513 ? -6.910  15.571  18.638  1.00 15.87  ? 513  HIS A N     1 
ATOM   3987 C  CA    . HIS A 1 513 ? -5.789  14.696  18.976  1.00 17.94  ? 513  HIS A CA    1 
ATOM   3988 C  C     . HIS A 1 513 ? -6.115  13.978  20.288  1.00 19.95  ? 513  HIS A C     1 
ATOM   3989 O  O     . HIS A 1 513 ? -6.575  14.607  21.249  1.00 16.81  ? 513  HIS A O     1 
ATOM   3990 C  CB    . HIS A 1 513 ? -4.466  15.481  19.098  1.00 15.56  ? 513  HIS A CB    1 
ATOM   3991 C  CG    . HIS A 1 513 ? -3.239  14.618  19.234  1.00 16.78  ? 513  HIS A CG    1 
ATOM   3992 N  ND1   . HIS A 1 513 ? -2.798  14.126  20.448  1.00 18.04  ? 513  HIS A ND1   1 
ATOM   3993 C  CD2   . HIS A 1 513 ? -2.335  14.197  18.312  1.00 18.44  ? 513  HIS A CD2   1 
ATOM   3994 C  CE1   . HIS A 1 513 ? -1.702  13.410  20.263  1.00 19.67  ? 513  HIS A CE1   1 
ATOM   3995 N  NE2   . HIS A 1 513 ? -1.391  13.448  18.977  1.00 20.45  ? 513  HIS A NE2   1 
ATOM   3996 N  N     . VAL A 1 514 ? -5.880  12.668  20.331  1.00 16.88  ? 514  VAL A N     1 
ATOM   3997 C  CA    . VAL A 1 514 ? -6.123  11.887  21.543  1.00 20.65  ? 514  VAL A CA    1 
ATOM   3998 C  C     . VAL A 1 514 ? -4.840  11.209  21.992  1.00 19.70  ? 514  VAL A C     1 
ATOM   3999 O  O     . VAL A 1 514 ? -3.906  10.995  21.212  1.00 17.80  ? 514  VAL A O     1 
ATOM   4000 C  CB    . VAL A 1 514 ? -7.223  10.828  21.366  1.00 18.07  ? 514  VAL A CB    1 
ATOM   4001 C  CG1   . VAL A 1 514 ? -8.520  11.481  20.974  1.00 15.66  ? 514  VAL A CG1   1 
ATOM   4002 C  CG2   . VAL A 1 514 ? -6.792  9.772   20.332  1.00 18.92  ? 514  VAL A CG2   1 
ATOM   4003 N  N     . ASN A 1 515 ? -4.818  10.835  23.270  1.00 15.96  ? 515  ASN A N     1 
ATOM   4004 C  CA    . ASN A 1 515 ? -3.733  10.022  23.818  1.00 15.72  ? 515  ASN A CA    1 
ATOM   4005 C  C     . ASN A 1 515 ? -4.358  9.065   24.831  1.00 21.60  ? 515  ASN A C     1 
ATOM   4006 O  O     . ASN A 1 515 ? -4.682  9.464   25.955  1.00 19.07  ? 515  ASN A O     1 
ATOM   4007 C  CB    . ASN A 1 515 ? -2.647  10.881  24.454  1.00 18.74  ? 515  ASN A CB    1 
ATOM   4008 C  CG    . ASN A 1 515 ? -1.522  10.050  25.042  1.00 20.37  ? 515  ASN A CG    1 
ATOM   4009 O  OD1   . ASN A 1 515 ? -1.270  8.921   24.607  1.00 21.56  ? 515  ASN A OD1   1 
ATOM   4010 N  ND2   . ASN A 1 515 ? -0.851  10.595  26.041  1.00 21.74  ? 515  ASN A ND2   1 
ATOM   4011 N  N     . TRP A 1 516 ? -4.541  7.805   24.424  1.00 21.93  ? 516  TRP A N     1 
ATOM   4012 C  CA    . TRP A 1 516 ? -5.058  6.790   25.335  1.00 23.05  ? 516  TRP A CA    1 
ATOM   4013 C  C     . TRP A 1 516 ? -3.995  6.267   26.281  1.00 24.33  ? 516  TRP A C     1 
ATOM   4014 O  O     . TRP A 1 516 ? -4.314  5.440   27.144  1.00 23.53  ? 516  TRP A O     1 
ATOM   4015 C  CB    . TRP A 1 516 ? -5.622  5.579   24.581  1.00 19.62  ? 516  TRP A CB    1 
ATOM   4016 C  CG    . TRP A 1 516 ? -6.592  5.802   23.445  1.00 20.90  ? 516  TRP A CG    1 
ATOM   4017 C  CD1   . TRP A 1 516 ? -6.664  5.062   22.292  1.00 20.97  ? 516  TRP A CD1   1 
ATOM   4018 C  CD2   . TRP A 1 516 ? -7.648  6.772   23.360  1.00 18.70  ? 516  TRP A CD2   1 
ATOM   4019 N  NE1   . TRP A 1 516 ? -7.686  5.521   21.493  1.00 20.44  ? 516  TRP A NE1   1 
ATOM   4020 C  CE2   . TRP A 1 516 ? -8.317  6.557   22.135  1.00 19.82  ? 516  TRP A CE2   1 
ATOM   4021 C  CE3   . TRP A 1 516 ? -8.105  7.799   24.206  1.00 24.49  ? 516  TRP A CE3   1 
ATOM   4022 C  CZ2   . TRP A 1 516 ? -9.399  7.344   21.724  1.00 17.83  ? 516  TRP A CZ2   1 
ATOM   4023 C  CZ3   . TRP A 1 516 ? -9.181  8.571   23.797  1.00 22.74  ? 516  TRP A CZ3   1 
ATOM   4024 C  CH2   . TRP A 1 516 ? -9.816  8.340   22.570  1.00 17.65  ? 516  TRP A CH2   1 
ATOM   4025 N  N     . PHE A 1 517 ? -2.746  6.703   26.131  1.00 19.94  ? 517  PHE A N     1 
ATOM   4026 C  CA    . PHE A 1 517 ? -1.608  5.951   26.638  1.00 19.92  ? 517  PHE A CA    1 
ATOM   4027 C  C     . PHE A 1 517 ? -0.803  6.687   27.692  1.00 24.37  ? 517  PHE A C     1 
ATOM   4028 O  O     . PHE A 1 517 ? 0.314   6.253   28.000  1.00 26.75  ? 517  PHE A O     1 
ATOM   4029 C  CB    . PHE A 1 517 ? -0.700  5.536   25.470  1.00 22.32  ? 517  PHE A CB    1 
ATOM   4030 C  CG    . PHE A 1 517 ? -1.369  4.615   24.492  1.00 24.84  ? 517  PHE A CG    1 
ATOM   4031 C  CD1   . PHE A 1 517 ? -1.424  3.250   24.734  1.00 23.99  ? 517  PHE A CD1   1 
ATOM   4032 C  CD2   . PHE A 1 517 ? -1.969  5.112   23.345  1.00 22.57  ? 517  PHE A CD2   1 
ATOM   4033 C  CE1   . PHE A 1 517 ? -2.041  2.407   23.844  1.00 24.92  ? 517  PHE A CE1   1 
ATOM   4034 C  CE2   . PHE A 1 517 ? -2.588  4.270   22.453  1.00 24.05  ? 517  PHE A CE2   1 
ATOM   4035 C  CZ    . PHE A 1 517 ? -2.628  2.910   22.702  1.00 24.60  ? 517  PHE A CZ    1 
ATOM   4036 N  N     . ARG A 1 518 ? -1.332  7.772   28.262  1.00 22.30  ? 518  ARG A N     1 
ATOM   4037 C  CA    . ARG A 1 518 ? -0.578  8.525   29.255  1.00 34.17  ? 518  ARG A CA    1 
ATOM   4038 C  C     . ARG A 1 518 ? -0.438  7.702   30.530  1.00 36.40  ? 518  ARG A C     1 
ATOM   4039 O  O     . ARG A 1 518 ? -1.378  7.024   30.959  1.00 36.60  ? 518  ARG A O     1 
ATOM   4040 C  CB    . ARG A 1 518 ? -1.248  9.876   29.556  1.00 30.78  ? 518  ARG A CB    1 
ATOM   4041 C  CG    . ARG A 1 518 ? -0.300  10.924  30.179  1.00 29.82  ? 518  ARG A CG    1 
ATOM   4042 C  CD    . ARG A 1 518 ? -1.014  12.243  30.521  1.00 35.54  ? 518  ARG A CD    1 
ATOM   4043 N  NE    . ARG A 1 518 ? -0.088  13.288  30.952  1.00 34.78  ? 518  ARG A NE    1 
ATOM   4044 C  CZ    . ARG A 1 518 ? -0.342  14.595  30.908  1.00 38.96  ? 518  ARG A CZ    1 
ATOM   4045 N  NH1   . ARG A 1 518 ? -1.498  15.068  30.464  1.00 32.42  ? 518  ARG A NH1   1 
ATOM   4046 N  NH2   . ARG A 1 518 ? 0.594   15.455  31.309  1.00 37.14  ? 518  ARG A NH2   1 
ATOM   4047 N  N     . LYS A 1 519 ? 0.753   7.745   31.122  1.00 39.53  ? 519  LYS A N     1 
ATOM   4048 C  CA    . LYS A 1 519 ? 1.066   6.975   32.315  1.00 43.19  ? 519  LYS A CA    1 
ATOM   4049 C  C     . LYS A 1 519 ? 1.384   7.902   33.477  1.00 46.94  ? 519  LYS A C     1 
ATOM   4050 O  O     . LYS A 1 519 ? 1.845   9.033   33.288  1.00 47.92  ? 519  LYS A O     1 
ATOM   4051 C  CB    . LYS A 1 519 ? 2.248   6.026   32.071  1.00 47.53  ? 519  LYS A CB    1 
ATOM   4052 C  CG    . LYS A 1 519 ? 1.956   4.916   31.074  1.00 41.54  ? 519  LYS A CG    1 
ATOM   4053 C  CD    . LYS A 1 519 ? 3.156   4.007   30.886  1.00 43.12  ? 519  LYS A CD    1 
ATOM   4054 C  CE    . LYS A 1 519 ? 2.763   2.729   30.167  1.00 46.82  ? 519  LYS A CE    1 
ATOM   4055 N  NZ    . LYS A 1 519 ? 3.946   1.851   29.939  1.00 56.31  ? 519  LYS A NZ    1 
ATOM   4056 N  N     . ASP A 1 520 ? 1.119   7.413   34.687  1.00 59.82  ? 520  ASP A N     1 
ATOM   4057 C  CA    . ASP A 1 520 ? 1.511   8.102   35.904  1.00 64.97  ? 520  ASP A CA    1 
ATOM   4058 C  C     . ASP A 1 520 ? 2.956   7.748   36.248  1.00 73.94  ? 520  ASP A C     1 
ATOM   4059 O  O     . ASP A 1 520 ? 3.640   7.029   35.514  1.00 72.35  ? 520  ASP A O     1 
ATOM   4060 C  CB    . ASP A 1 520 ? 0.563   7.751   37.055  1.00 71.23  ? 520  ASP A CB    1 
ATOM   4061 C  CG    . ASP A 1 520 ? 0.526   6.251   37.368  1.00 70.76  ? 520  ASP A CG    1 
ATOM   4062 O  OD1   . ASP A 1 520 ? 1.215   5.454   36.694  1.00 71.79  ? 520  ASP A OD1   1 
ATOM   4063 O  OD2   . ASP A 1 520 ? -0.207  5.868   38.304  1.00 76.64  ? 520  ASP A OD2   1 
ATOM   4064 N  N     . LYS A 1 521 ? 3.427   8.248   37.392  1.00 81.20  ? 521  LYS A N     1 
ATOM   4065 C  CA    . LYS A 1 521 ? 4.770   7.910   37.847  1.00 84.04  ? 521  LYS A CA    1 
ATOM   4066 C  C     . LYS A 1 521 ? 4.925   6.419   38.142  1.00 83.68  ? 521  LYS A C     1 
ATOM   4067 O  O     . LYS A 1 521 ? 6.056   5.926   38.202  1.00 85.98  ? 521  LYS A O     1 
ATOM   4068 C  CB    . LYS A 1 521 ? 5.118   8.739   39.084  1.00 86.63  ? 521  LYS A CB    1 
ATOM   4069 C  CG    . LYS A 1 521 ? 4.942   10.235  38.887  1.00 89.35  ? 521  LYS A CG    1 
ATOM   4070 C  CD    . LYS A 1 521 ? 5.301   10.998  40.149  1.00 97.61  ? 521  LYS A CD    1 
ATOM   4071 C  CE    . LYS A 1 521 ? 5.143   12.497  39.949  1.00 104.60 ? 521  LYS A CE    1 
ATOM   4072 N  NZ    . LYS A 1 521 ? 5.519   13.268  41.166  1.00 104.50 ? 521  LYS A NZ    1 
ATOM   4073 N  N     . ASN A 1 522 ? 3.817   5.689   38.313  1.00 79.62  ? 522  ASN A N     1 
ATOM   4074 C  CA    . ASN A 1 522 ? 3.897   4.255   38.579  1.00 78.81  ? 522  ASN A CA    1 
ATOM   4075 C  C     . ASN A 1 522 ? 4.283   3.463   37.337  1.00 75.51  ? 522  ASN A C     1 
ATOM   4076 O  O     . ASN A 1 522 ? 4.832   2.363   37.452  1.00 77.45  ? 522  ASN A O     1 
ATOM   4077 C  CB    . ASN A 1 522 ? 2.559   3.730   39.111  1.00 82.27  ? 522  ASN A CB    1 
ATOM   4078 C  CG    . ASN A 1 522 ? 2.250   4.207   40.520  1.00 84.98  ? 522  ASN A CG    1 
ATOM   4079 O  OD1   . ASN A 1 522 ? 3.149   4.381   41.344  1.00 90.23  ? 522  ASN A OD1   1 
ATOM   4080 N  ND2   . ASN A 1 522 ? 0.967   4.412   40.806  1.00 77.92  ? 522  ASN A ND2   1 
ATOM   4081 N  N     . GLY A 1 523 ? 3.999   3.991   36.151  1.00 74.83  ? 523  GLY A N     1 
ATOM   4082 C  CA    . GLY A 1 523 ? 4.077   3.199   34.944  1.00 66.55  ? 523  GLY A CA    1 
ATOM   4083 C  C     . GLY A 1 523 ? 2.785   2.508   34.575  1.00 61.27  ? 523  GLY A C     1 
ATOM   4084 O  O     . GLY A 1 523 ? 2.788   1.656   33.677  1.00 57.75  ? 523  GLY A O     1 
ATOM   4085 N  N     . LYS A 1 524 ? 1.687   2.840   35.244  1.00 61.11  ? 524  LYS A N     1 
ATOM   4086 C  CA    . LYS A 1 524 ? 0.370   2.314   34.927  1.00 65.16  ? 524  LYS A CA    1 
ATOM   4087 C  C     . LYS A 1 524 ? -0.455  3.385   34.222  1.00 54.42  ? 524  LYS A C     1 
ATOM   4088 O  O     . LYS A 1 524 ? -0.316  4.582   34.495  1.00 53.58  ? 524  LYS A O     1 
ATOM   4089 C  CB    . LYS A 1 524 ? -0.353  1.845   36.193  1.00 72.59  ? 524  LYS A CB    1 
ATOM   4090 C  CG    . LYS A 1 524 ? 0.413   0.817   37.022  1.00 78.20  ? 524  LYS A CG    1 
ATOM   4091 C  CD    . LYS A 1 524 ? -0.370  0.420   38.268  1.00 78.46  ? 524  LYS A CD    1 
ATOM   4092 C  CE    . LYS A 1 524 ? 0.399   -0.579  39.120  1.00 79.85  ? 524  LYS A CE    1 
ATOM   4093 N  NZ    . LYS A 1 524 ? -0.380  -1.002  40.324  1.00 76.02  ? 524  LYS A NZ    1 
ATOM   4094 N  N     . PHE A 1 525 ? -1.324  2.939   33.316  1.00 49.88  ? 525  PHE A N     1 
ATOM   4095 C  CA    . PHE A 1 525 ? -2.121  3.863   32.518  1.00 43.75  ? 525  PHE A CA    1 
ATOM   4096 C  C     . PHE A 1 525 ? -3.057  4.683   33.397  1.00 43.75  ? 525  PHE A C     1 
ATOM   4097 O  O     . PHE A 1 525 ? -3.551  4.213   34.424  1.00 48.48  ? 525  PHE A O     1 
ATOM   4098 C  CB    . PHE A 1 525 ? -2.920  3.093   31.461  1.00 41.68  ? 525  PHE A CB    1 
ATOM   4099 C  CG    . PHE A 1 525 ? -2.057  2.448   30.405  1.00 42.37  ? 525  PHE A CG    1 
ATOM   4100 C  CD1   . PHE A 1 525 ? -1.458  3.216   29.417  1.00 38.03  ? 525  PHE A CD1   1 
ATOM   4101 C  CD2   . PHE A 1 525 ? -1.841  1.082   30.402  1.00 43.60  ? 525  PHE A CD2   1 
ATOM   4102 C  CE1   . PHE A 1 525 ? -0.667  2.635   28.452  1.00 35.41  ? 525  PHE A CE1   1 
ATOM   4103 C  CE2   . PHE A 1 525 ? -1.046  0.491   29.429  1.00 43.03  ? 525  PHE A CE2   1 
ATOM   4104 C  CZ    . PHE A 1 525 ? -0.460  1.270   28.452  1.00 37.86  ? 525  PHE A CZ    1 
ATOM   4105 N  N     . LEU A 1 526 ? -3.283  5.932   32.994  1.00 35.72  ? 526  LEU A N     1 
ATOM   4106 C  CA    . LEU A 1 526 ? -4.218  6.806   33.692  1.00 34.68  ? 526  LEU A CA    1 
ATOM   4107 C  C     . LEU A 1 526 ? -5.652  6.631   33.209  1.00 37.58  ? 526  LEU A C     1 
ATOM   4108 O  O     . LEU A 1 526 ? -6.587  7.003   33.925  1.00 35.90  ? 526  LEU A O     1 
ATOM   4109 C  CB    . LEU A 1 526 ? -3.801  8.267   33.511  1.00 37.35  ? 526  LEU A CB    1 
ATOM   4110 C  CG    . LEU A 1 526 ? -2.568  8.796   34.247  1.00 44.23  ? 526  LEU A CG    1 
ATOM   4111 C  CD1   . LEU A 1 526 ? -2.035  10.023  33.538  1.00 47.19  ? 526  LEU A CD1   1 
ATOM   4112 C  CD2   . LEU A 1 526 ? -2.916  9.132   35.693  1.00 47.66  ? 526  LEU A CD2   1 
ATOM   4113 N  N     . TRP A 1 527 ? -5.842  6.079   32.016  1.00 30.40  ? 527  TRP A N     1 
ATOM   4114 C  CA    . TRP A 1 527 ? -7.135  6.013   31.370  1.00 27.34  ? 527  TRP A CA    1 
ATOM   4115 C  C     . TRP A 1 527 ? -7.460  4.564   31.042  1.00 31.04  ? 527  TRP A C     1 
ATOM   4116 O  O     . TRP A 1 527 ? -6.602  3.847   30.504  1.00 27.65  ? 527  TRP A O     1 
ATOM   4117 C  CB    . TRP A 1 527 ? -7.142  6.858   30.091  1.00 25.28  ? 527  TRP A CB    1 
ATOM   4118 C  CG    . TRP A 1 527 ? -8.427  6.877   29.334  1.00 20.36  ? 527  TRP A CG    1 
ATOM   4119 C  CD1   . TRP A 1 527 ? -8.656  6.328   28.108  1.00 20.86  ? 527  TRP A CD1   1 
ATOM   4120 C  CD2   . TRP A 1 527 ? -9.659  7.498   29.734  1.00 21.65  ? 527  TRP A CD2   1 
ATOM   4121 N  NE1   . TRP A 1 527 ? -9.958  6.559   27.719  1.00 25.34  ? 527  TRP A NE1   1 
ATOM   4122 C  CE2   . TRP A 1 527 ? -10.594 7.274   28.699  1.00 22.07  ? 527  TRP A CE2   1 
ATOM   4123 C  CE3   . TRP A 1 527 ? -10.066 8.215   30.867  1.00 26.59  ? 527  TRP A CE3   1 
ATOM   4124 C  CZ2   . TRP A 1 527 ? -11.904 7.748   28.760  1.00 22.31  ? 527  TRP A CZ2   1 
ATOM   4125 C  CZ3   . TRP A 1 527 ? -11.369 8.686   30.920  1.00 24.90  ? 527  TRP A CZ3   1 
ATOM   4126 C  CH2   . TRP A 1 527 ? -12.273 8.444   29.876  1.00 23.56  ? 527  TRP A CH2   1 
ATOM   4127 N  N     . PRO A 1 528 ? -8.669  4.093   31.361  1.00 34.16  ? 528  PRO A N     1 
ATOM   4128 C  CA    . PRO A 1 528 ? -8.986  2.677   31.113  1.00 30.68  ? 528  PRO A CA    1 
ATOM   4129 C  C     . PRO A 1 528 ? -9.046  2.319   29.639  1.00 33.42  ? 528  PRO A C     1 
ATOM   4130 O  O     . PRO A 1 528 ? -8.753  1.172   29.280  1.00 30.49  ? 528  PRO A O     1 
ATOM   4131 C  CB    . PRO A 1 528 ? -10.347 2.495   31.808  1.00 28.51  ? 528  PRO A CB    1 
ATOM   4132 C  CG    . PRO A 1 528 ? -10.914 3.856   31.950  1.00 31.96  ? 528  PRO A CG    1 
ATOM   4133 C  CD    . PRO A 1 528 ? -9.741  4.791   32.091  1.00 30.60  ? 528  PRO A CD    1 
ATOM   4134 N  N     . GLY A 1 529 ? -9.419  3.263   28.770  1.00 30.52  ? 529  GLY A N     1 
ATOM   4135 C  CA    . GLY A 1 529 ? -9.401  2.976   27.349  1.00 26.59  ? 529  GLY A CA    1 
ATOM   4136 C  C     . GLY A 1 529 ? -10.478 1.999   26.881  1.00 25.92  ? 529  GLY A C     1 
ATOM   4137 O  O     . GLY A 1 529 ? -11.469 1.725   27.565  1.00 25.22  ? 529  GLY A O     1 
ATOM   4138 N  N     . PHE A 1 530 ? -10.263 1.498   25.664  1.00 20.05  ? 530  PHE A N     1 
ATOM   4139 C  CA    . PHE A 1 530 ? -11.124 0.522   24.984  1.00 28.70  ? 530  PHE A CA    1 
ATOM   4140 C  C     . PHE A 1 530 ? -12.553 1.068   24.973  1.00 30.65  ? 530  PHE A C     1 
ATOM   4141 O  O     . PHE A 1 530 ? -12.772 2.192   24.499  1.00 24.19  ? 530  PHE A O     1 
ATOM   4142 C  CB    . PHE A 1 530 ? -10.937 -0.851  25.638  1.00 23.46  ? 530  PHE A CB    1 
ATOM   4143 C  CG    . PHE A 1 530 ? -9.521  -1.339  25.582  1.00 21.57  ? 530  PHE A CG    1 
ATOM   4144 C  CD1   . PHE A 1 530 ? -9.022  -1.908  24.429  1.00 20.82  ? 530  PHE A CD1   1 
ATOM   4145 C  CD2   . PHE A 1 530 ? -8.678  -1.178  26.660  1.00 21.48  ? 530  PHE A CD2   1 
ATOM   4146 C  CE1   . PHE A 1 530 ? -7.702  -2.336  24.362  1.00 27.77  ? 530  PHE A CE1   1 
ATOM   4147 C  CE2   . PHE A 1 530 ? -7.368  -1.597  26.601  1.00 24.51  ? 530  PHE A CE2   1 
ATOM   4148 C  CZ    . PHE A 1 530 ? -6.878  -2.177  25.452  1.00 23.81  ? 530  PHE A CZ    1 
ATOM   4149 N  N     . GLY A 1 531 ? -13.541 0.319   25.462  1.00 25.81  ? 531  GLY A N     1 
ATOM   4150 C  CA    . GLY A 1 531 ? -14.905 0.784   25.387  1.00 22.47  ? 531  GLY A CA    1 
ATOM   4151 C  C     . GLY A 1 531 ? -15.149 2.075   26.126  1.00 20.16  ? 531  GLY A C     1 
ATOM   4152 O  O     . GLY A 1 531 ? -16.098 2.789   25.792  1.00 23.96  ? 531  GLY A O     1 
ATOM   4153 N  N     . GLU A 1 532 ? -14.314 2.398   27.127  1.00 20.11  ? 532  GLU A N     1 
ATOM   4154 C  CA    . GLU A 1 532 ? -14.465 3.674   27.826  1.00 19.30  ? 532  GLU A CA    1 
ATOM   4155 C  C     . GLU A 1 532 ? -14.076 4.866   26.956  1.00 22.34  ? 532  GLU A C     1 
ATOM   4156 O  O     . GLU A 1 532 ? -14.384 6.004   27.323  1.00 21.12  ? 532  GLU A O     1 
ATOM   4157 C  CB    . GLU A 1 532 ? -13.623 3.719   29.112  1.00 23.47  ? 532  GLU A CB    1 
ATOM   4158 C  CG    . GLU A 1 532 ? -13.916 2.611   30.163  1.00 29.29  ? 532  GLU A CG    1 
ATOM   4159 C  CD    . GLU A 1 532 ? -15.364 2.537   30.646  1.00 29.11  ? 532  GLU A CD    1 
ATOM   4160 O  OE1   . GLU A 1 532 ? -16.166 3.462   30.399  1.00 27.50  ? 532  GLU A OE1   1 
ATOM   4161 O  OE2   . GLU A 1 532 ? -15.705 1.519   31.282  1.00 35.16  ? 532  GLU A OE2   1 
ATOM   4162 N  N     . ASN A 1 533 ? -13.394 4.638   25.830  1.00 23.18  ? 533  ASN A N     1 
ATOM   4163 C  CA    . ASN A 1 533 ? -13.103 5.743   24.916  1.00 22.47  ? 533  ASN A CA    1 
ATOM   4164 C  C     . ASN A 1 533 ? -14.372 6.346   24.326  1.00 24.52  ? 533  ASN A C     1 
ATOM   4165 O  O     . ASN A 1 533 ? -14.310 7.430   23.734  1.00 18.47  ? 533  ASN A O     1 
ATOM   4166 C  CB    . ASN A 1 533 ? -12.164 5.268   23.794  1.00 16.61  ? 533  ASN A CB    1 
ATOM   4167 C  CG    . ASN A 1 533 ? -10.775 4.921   24.308  1.00 20.58  ? 533  ASN A CG    1 
ATOM   4168 O  OD1   . ASN A 1 533 ? -10.344 5.421   25.354  1.00 22.53  ? 533  ASN A OD1   1 
ATOM   4169 N  ND2   . ASN A 1 533 ? -10.064 4.060   23.573  1.00 22.89  ? 533  ASN A ND2   1 
ATOM   4170 N  N     . SER A 1 534 ? -15.522 5.683   24.497  1.00 26.39  ? 534  SER A N     1 
ATOM   4171 C  CA    . SER A 1 534 ? -16.789 6.265   24.064  1.00 22.94  ? 534  SER A CA    1 
ATOM   4172 C  C     . SER A 1 534 ? -17.090 7.579   24.784  1.00 21.29  ? 534  SER A C     1 
ATOM   4173 O  O     . SER A 1 534 ? -17.809 8.426   24.243  1.00 19.61  ? 534  SER A O     1 
ATOM   4174 C  CB    . SER A 1 534 ? -17.923 5.262   24.286  1.00 29.60  ? 534  SER A CB    1 
ATOM   4175 O  OG    . SER A 1 534 ? -18.077 4.941   25.659  1.00 20.36  ? 534  SER A OG    1 
ATOM   4176 N  N     . ARG A 1 535 ? -16.546 7.771   25.992  1.00 19.09  ? 535  ARG A N     1 
ATOM   4177 C  CA    . ARG A 1 535 ? -16.747 9.027   26.712  1.00 20.68  ? 535  ARG A CA    1 
ATOM   4178 C  C     . ARG A 1 535 ? -15.995 10.181  26.051  1.00 20.19  ? 535  ARG A C     1 
ATOM   4179 O  O     . ARG A 1 535 ? -16.429 11.338  26.129  1.00 18.06  ? 535  ARG A O     1 
ATOM   4180 C  CB    . ARG A 1 535 ? -16.282 8.881   28.160  1.00 21.97  ? 535  ARG A CB    1 
ATOM   4181 C  CG    . ARG A 1 535 ? -16.996 7.800   28.962  1.00 21.20  ? 535  ARG A CG    1 
ATOM   4182 C  CD    . ARG A 1 535 ? -16.168 7.430   30.190  1.00 26.38  ? 535  ARG A CD    1 
ATOM   4183 N  NE    . ARG A 1 535 ? -16.659 6.217   30.836  1.00 30.82  ? 535  ARG A NE    1 
ATOM   4184 C  CZ    . ARG A 1 535 ? -17.583 6.202   31.787  1.00 36.53  ? 535  ARG A CZ    1 
ATOM   4185 N  NH1   . ARG A 1 535 ? -18.152 7.317   32.213  1.00 31.29  ? 535  ARG A NH1   1 
ATOM   4186 N  NH2   . ARG A 1 535 ? -17.941 5.039   32.328  1.00 31.40  ? 535  ARG A NH2   1 
ATOM   4187 N  N     . VAL A 1 536 ? -14.850 9.894   25.439  1.00 19.27  ? 536  VAL A N     1 
ATOM   4188 C  CA    . VAL A 1 536 ? -14.149 10.925  24.675  1.00 19.10  ? 536  VAL A CA    1 
ATOM   4189 C  C     . VAL A 1 536 ? -14.878 11.190  23.362  1.00 22.00  ? 536  VAL A C     1 
ATOM   4190 O  O     . VAL A 1 536 ? -15.028 12.342  22.938  1.00 20.46  ? 536  VAL A O     1 
ATOM   4191 C  CB    . VAL A 1 536 ? -12.680 10.514  24.457  1.00 19.20  ? 536  VAL A CB    1 
ATOM   4192 C  CG1   . VAL A 1 536 ? -11.974 11.474  23.495  1.00 18.91  ? 536  VAL A CG1   1 
ATOM   4193 C  CG2   . VAL A 1 536 ? -11.944 10.473  25.787  1.00 22.45  ? 536  VAL A CG2   1 
ATOM   4194 N  N     . LEU A 1 537 ? -15.350 10.137  22.694  1.00 17.97  ? 537  LEU A N     1 
ATOM   4195 C  CA    . LEU A 1 537 ? -16.113 10.372  21.471  1.00 20.03  ? 537  LEU A CA    1 
ATOM   4196 C  C     . LEU A 1 537 ? -17.389 11.163  21.745  1.00 23.16  ? 537  LEU A C     1 
ATOM   4197 O  O     . LEU A 1 537 ? -17.815 11.952  20.894  1.00 20.78  ? 537  LEU A O     1 
ATOM   4198 C  CB    . LEU A 1 537 ? -16.467 9.064   20.782  1.00 24.01  ? 537  LEU A CB    1 
ATOM   4199 C  CG    . LEU A 1 537 ? -15.350 8.132   20.311  1.00 26.78  ? 537  LEU A CG    1 
ATOM   4200 C  CD1   . LEU A 1 537 ? -15.904 7.290   19.189  1.00 35.73  ? 537  LEU A CD1   1 
ATOM   4201 C  CD2   . LEU A 1 537 ? -14.130 8.875   19.853  1.00 23.14  ? 537  LEU A CD2   1 
ATOM   4202 N  N     . GLU A 1 538 ? -18.024 10.959  22.907  1.00 19.65  ? 538  GLU A N     1 
ATOM   4203 C  CA    . GLU A 1 538 ? -19.207 11.752  23.231  1.00 20.87  ? 538  GLU A CA    1 
ATOM   4204 C  C     . GLU A 1 538 ? -18.880 13.244  23.252  1.00 22.80  ? 538  GLU A C     1 
ATOM   4205 O  O     . GLU A 1 538 ? -19.636 14.060  22.713  1.00 20.45  ? 538  GLU A O     1 
ATOM   4206 C  CB    . GLU A 1 538 ? -19.795 11.317  24.574  1.00 24.26  ? 538  GLU A CB    1 
ATOM   4207 C  CG    . GLU A 1 538 ? -20.841 12.303  25.101  1.00 28.20  ? 538  GLU A CG    1 
ATOM   4208 C  CD    . GLU A 1 538 ? -21.519 11.834  26.376  1.00 31.82  ? 538  GLU A CD    1 
ATOM   4209 O  OE1   . GLU A 1 538 ? -20.816 11.487  27.345  1.00 28.23  ? 538  GLU A OE1   1 
ATOM   4210 O  OE2   . GLU A 1 538 ? -22.765 11.809  26.402  1.00 33.59  ? 538  GLU A OE2   1 
ATOM   4211 N  N     . TRP A 1 539 ? -17.750 13.612  23.865  1.00 19.68  ? 539  TRP A N     1 
ATOM   4212 C  CA    . TRP A 1 539 ? -17.339 15.009  23.901  1.00 22.25  ? 539  TRP A CA    1 
ATOM   4213 C  C     . TRP A 1 539 ? -17.110 15.546  22.496  1.00 23.01  ? 539  TRP A C     1 
ATOM   4214 O  O     . TRP A 1 539 ? -17.511 16.672  22.180  1.00 22.57  ? 539  TRP A O     1 
ATOM   4215 C  CB    . TRP A 1 539 ? -16.070 15.162  24.738  1.00 20.71  ? 539  TRP A CB    1 
ATOM   4216 C  CG    . TRP A 1 539 ? -15.637 16.593  24.876  1.00 22.57  ? 539  TRP A CG    1 
ATOM   4217 C  CD1   . TRP A 1 539 ? -16.223 17.544  25.667  1.00 23.36  ? 539  TRP A CD1   1 
ATOM   4218 C  CD2   . TRP A 1 539 ? -14.534 17.244  24.213  1.00 21.31  ? 539  TRP A CD2   1 
ATOM   4219 N  NE1   . TRP A 1 539 ? -15.562 18.743  25.529  1.00 22.86  ? 539  TRP A NE1   1 
ATOM   4220 C  CE2   . TRP A 1 539 ? -14.519 18.586  24.653  1.00 20.09  ? 539  TRP A CE2   1 
ATOM   4221 C  CE3   . TRP A 1 539 ? -13.561 16.821  23.291  1.00 19.62  ? 539  TRP A CE3   1 
ATOM   4222 C  CZ2   . TRP A 1 539 ? -13.573 19.521  24.194  1.00 23.39  ? 539  TRP A CZ2   1 
ATOM   4223 C  CZ3   . TRP A 1 539 ? -12.619 17.744  22.841  1.00 21.37  ? 539  TRP A CZ3   1 
ATOM   4224 C  CH2   . TRP A 1 539 ? -12.631 19.081  23.299  1.00 25.09  ? 539  TRP A CH2   1 
ATOM   4225 N  N     . MET A 1 540 ? -16.447 14.753  21.647  1.00 19.13  ? 540  MET A N     1 
ATOM   4226 C  CA    . MET A 1 540 ? -16.205 15.148  20.266  1.00 20.57  ? 540  MET A CA    1 
ATOM   4227 C  C     . MET A 1 540 ? -17.505 15.349  19.516  1.00 21.93  ? 540  MET A C     1 
ATOM   4228 O  O     . MET A 1 540 ? -17.641 16.292  18.729  1.00 19.50  ? 540  MET A O     1 
ATOM   4229 C  CB    . MET A 1 540 ? -15.372 14.075  19.560  1.00 16.06  ? 540  MET A CB    1 
ATOM   4230 C  CG    . MET A 1 540 ? -13.987 13.912  20.107  1.00 19.07  ? 540  MET A CG    1 
ATOM   4231 S  SD    . MET A 1 540 ? -13.170 12.580  19.190  1.00 19.31  ? 540  MET A SD    1 
ATOM   4232 C  CE    . MET A 1 540 ? -11.578 12.653  19.989  1.00 15.56  ? 540  MET A CE    1 
ATOM   4233 N  N     . PHE A 1 541 ? -18.454 14.437  19.718  1.00 16.68  ? 541  PHE A N     1 
ATOM   4234 C  CA    . PHE A 1 541 ? -19.761 14.538  19.081  1.00 21.40  ? 541  PHE A CA    1 
ATOM   4235 C  C     . PHE A 1 541 ? -20.423 15.868  19.415  1.00 20.81  ? 541  PHE A C     1 
ATOM   4236 O  O     . PHE A 1 541 ? -20.983 16.531  18.533  1.00 22.94  ? 541  PHE A O     1 
ATOM   4237 C  CB    . PHE A 1 541 ? -20.636 13.355  19.545  1.00 17.63  ? 541  PHE A CB    1 
ATOM   4238 C  CG    . PHE A 1 541 ? -21.841 13.098  18.677  1.00 23.58  ? 541  PHE A CG    1 
ATOM   4239 C  CD1   . PHE A 1 541 ? -22.963 13.918  18.751  1.00 24.57  ? 541  PHE A CD1   1 
ATOM   4240 C  CD2   . PHE A 1 541 ? -21.865 12.008  17.812  1.00 20.67  ? 541  PHE A CD2   1 
ATOM   4241 C  CE1   . PHE A 1 541 ? -24.068 13.676  17.949  1.00 24.63  ? 541  PHE A CE1   1 
ATOM   4242 C  CE2   . PHE A 1 541 ? -22.965 11.762  17.010  1.00 21.69  ? 541  PHE A CE2   1 
ATOM   4243 C  CZ    . PHE A 1 541 ? -24.069 12.595  17.080  1.00 22.44  ? 541  PHE A CZ    1 
ATOM   4244 N  N     . GLY A 1 542 ? -20.363 16.275  20.685  1.00 21.12  ? 542  GLY A N     1 
ATOM   4245 C  CA    . GLY A 1 542 ? -20.998 17.526  21.085  1.00 22.59  ? 542  GLY A CA    1 
ATOM   4246 C  C     . GLY A 1 542 ? -20.277 18.747  20.546  1.00 22.71  ? 542  GLY A C     1 
ATOM   4247 O  O     . GLY A 1 542 ? -20.909 19.748  20.186  1.00 23.55  ? 542  GLY A O     1 
ATOM   4248 N  N     . ARG A 1 543 ? -18.946 18.692  20.497  1.00 21.65  ? 543  ARG A N     1 
ATOM   4249 C  CA    . ARG A 1 543 ? -18.177 19.786  19.905  1.00 19.21  ? 543  ARG A CA    1 
ATOM   4250 C  C     . ARG A 1 543 ? -18.496 19.954  18.425  1.00 23.32  ? 543  ARG A C     1 
ATOM   4251 O  O     . ARG A 1 543 ? -18.562 21.079  17.921  1.00 24.80  ? 543  ARG A O     1 
ATOM   4252 C  CB    . ARG A 1 543 ? -16.686 19.533  20.108  1.00 20.02  ? 543  ARG A CB    1 
ATOM   4253 C  CG    . ARG A 1 543 ? -16.220 19.810  21.534  1.00 21.51  ? 543  ARG A CG    1 
ATOM   4254 C  CD    . ARG A 1 543 ? -16.405 21.291  21.879  1.00 24.35  ? 543  ARG A CD    1 
ATOM   4255 N  NE    . ARG A 1 543 ? -15.561 22.142  21.051  1.00 22.40  ? 543  ARG A NE    1 
ATOM   4256 C  CZ    . ARG A 1 543 ? -15.723 23.449  20.923  1.00 31.56  ? 543  ARG A CZ    1 
ATOM   4257 N  NH1   . ARG A 1 543 ? -16.721 24.083  21.525  1.00 30.35  ? 543  ARG A NH1   1 
ATOM   4258 N  NH2   . ARG A 1 543 ? -14.864 24.139  20.176  1.00 26.64  ? 543  ARG A NH2   1 
ATOM   4259 N  N     . ILE A 1 544 ? -18.674 18.849  17.702  1.00 20.68  ? 544  ILE A N     1 
ATOM   4260 C  CA    . ILE A 1 544 ? -19.062 18.952  16.297  1.00 25.66  ? 544  ILE A CA    1 
ATOM   4261 C  C     . ILE A 1 544 ? -20.432 19.601  16.165  1.00 24.83  ? 544  ILE A C     1 
ATOM   4262 O  O     . ILE A 1 544 ? -20.683 20.352  15.214  1.00 24.97  ? 544  ILE A O     1 
ATOM   4263 C  CB    . ILE A 1 544 ? -19.022 17.562  15.628  1.00 25.08  ? 544  ILE A CB    1 
ATOM   4264 C  CG1   . ILE A 1 544 ? -17.571 17.103  15.474  1.00 20.46  ? 544  ILE A CG1   1 
ATOM   4265 C  CG2   . ILE A 1 544 ? -19.719 17.590  14.279  1.00 23.87  ? 544  ILE A CG2   1 
ATOM   4266 C  CD1   . ILE A 1 544 ? -17.439 15.576  15.231  1.00 22.83  ? 544  ILE A CD1   1 
ATOM   4267 N  N     . GLU A 1 545 ? -21.334 19.336  17.110  1.00 23.41  ? 545  GLU A N     1 
ATOM   4268 C  CA    . GLU A 1 545 ? -22.654 19.960  17.098  1.00 26.99  ? 545  GLU A CA    1 
ATOM   4269 C  C     . GLU A 1 545 ? -22.632 21.404  17.588  1.00 33.40  ? 545  GLU A C     1 
ATOM   4270 O  O     . GLU A 1 545 ? -23.664 22.082  17.525  1.00 32.73  ? 545  GLU A O     1 
ATOM   4271 C  CB    . GLU A 1 545 ? -23.628 19.152  17.963  1.00 24.84  ? 545  GLU A CB    1 
ATOM   4272 C  CG    . GLU A 1 545 ? -24.043 17.809  17.394  1.00 24.81  ? 545  GLU A CG    1 
ATOM   4273 C  CD    . GLU A 1 545 ? -25.202 17.197  18.181  1.00 31.33  ? 545  GLU A CD    1 
ATOM   4274 O  OE1   . GLU A 1 545 ? -25.230 17.339  19.423  1.00 35.12  ? 545  GLU A OE1   1 
ATOM   4275 O  OE2   . GLU A 1 545 ? -26.106 16.603  17.557  1.00 34.55  ? 545  GLU A OE2   1 
ATOM   4276 N  N     . GLY A 1 546 ? -21.499 21.878  18.097  1.00 30.21  ? 546  GLY A N     1 
ATOM   4277 C  CA    . GLY A 1 546 ? -21.387 23.243  18.550  1.00 32.38  ? 546  GLY A CA    1 
ATOM   4278 C  C     . GLY A 1 546 ? -21.578 23.467  20.031  1.00 31.83  ? 546  GLY A C     1 
ATOM   4279 O  O     . GLY A 1 546 ? -21.795 24.610  20.440  1.00 32.10  ? 546  GLY A O     1 
ATOM   4280 N  N     . GLU A 1 547 ? -21.491 22.434  20.859  1.00 26.60  ? 547  GLU A N     1 
ATOM   4281 C  CA    . GLU A 1 547 ? -21.685 22.645  22.286  1.00 31.34  ? 547  GLU A CA    1 
ATOM   4282 C  C     . GLU A 1 547 ? -20.528 23.445  22.877  1.00 32.67  ? 547  GLU A C     1 
ATOM   4283 O  O     . GLU A 1 547 ? -19.383 23.328  22.439  1.00 26.90  ? 547  GLU A O     1 
ATOM   4284 C  CB    . GLU A 1 547 ? -21.855 21.311  23.012  1.00 25.55  ? 547  GLU A CB    1 
ATOM   4285 C  CG    . GLU A 1 547 ? -23.315 20.879  23.053  1.00 45.04  ? 547  GLU A CG    1 
ATOM   4286 C  CD    . GLU A 1 547 ? -23.505 19.411  23.391  1.00 54.87  ? 547  GLU A CD    1 
ATOM   4287 O  OE1   . GLU A 1 547 ? -22.557 18.787  23.921  1.00 49.80  ? 547  GLU A OE1   1 
ATOM   4288 O  OE2   . GLU A 1 547 ? -24.608 18.879  23.118  1.00 60.78  ? 547  GLU A OE2   1 
ATOM   4289 N  N     . ASP A 1 548 ? -20.848 24.279  23.868  1.00 31.41  ? 548  ASP A N     1 
ATOM   4290 C  CA    . ASP A 1 548 ? -19.886 25.166  24.528  1.00 36.53  ? 548  ASP A CA    1 
ATOM   4291 C  C     . ASP A 1 548 ? -19.218 24.410  25.681  1.00 37.22  ? 548  ASP A C     1 
ATOM   4292 O  O     . ASP A 1 548 ? -19.352 24.732  26.865  1.00 34.20  ? 548  ASP A O     1 
ATOM   4293 C  CB    . ASP A 1 548 ? -20.597 26.430  25.004  1.00 39.64  ? 548  ASP A CB    1 
ATOM   4294 C  CG    . ASP A 1 548 ? -19.657 27.440  25.622  1.00 42.88  ? 548  ASP A CG    1 
ATOM   4295 O  OD1   . ASP A 1 548 ? -18.713 27.881  24.928  1.00 47.71  ? 548  ASP A OD1   1 
ATOM   4296 O  OD2   . ASP A 1 548 ? -19.883 27.808  26.795  1.00 48.85  ? 548  ASP A OD2   1 
ATOM   4297 N  N     . SER A 1 549 ? -18.486 23.363  25.307  1.00 30.86  ? 549  SER A N     1 
ATOM   4298 C  CA    . SER A 1 549 ? -17.972 22.408  26.280  1.00 26.80  ? 549  SER A CA    1 
ATOM   4299 C  C     . SER A 1 549 ? -16.448 22.396  26.350  1.00 26.06  ? 549  SER A C     1 
ATOM   4300 O  O     . SER A 1 549 ? -15.877 21.464  26.927  1.00 25.84  ? 549  SER A O     1 
ATOM   4301 C  CB    . SER A 1 549 ? -18.488 21.011  25.940  1.00 28.67  ? 549  SER A CB    1 
ATOM   4302 O  OG    . SER A 1 549 ? -18.056 20.675  24.630  1.00 24.47  ? 549  SER A OG    1 
ATOM   4303 N  N     . ALA A 1 550 ? -15.775 23.401  25.793  1.00 27.83  ? 550  ALA A N     1 
ATOM   4304 C  CA    . ALA A 1 550 ? -14.322 23.416  25.731  1.00 27.52  ? 550  ALA A CA    1 
ATOM   4305 C  C     . ALA A 1 550 ? -13.758 24.662  26.404  1.00 28.28  ? 550  ALA A C     1 
ATOM   4306 O  O     . ALA A 1 550 ? -14.425 25.696  26.496  1.00 26.30  ? 550  ALA A O     1 
ATOM   4307 C  CB    . ALA A 1 550 ? -13.836 23.357  24.283  1.00 28.71  ? 550  ALA A CB    1 
ATOM   4308 N  N     . LYS A 1 551 ? -12.518 24.547  26.879  1.00 24.01  ? 551  LYS A N     1 
ATOM   4309 C  CA    . LYS A 1 551 ? -11.750 25.695  27.329  1.00 28.28  ? 551  LYS A CA    1 
ATOM   4310 C  C     . LYS A 1 551 ? -10.443 25.795  26.546  1.00 25.95  ? 551  LYS A C     1 
ATOM   4311 O  O     . LYS A 1 551 ? -9.880  24.793  26.088  1.00 22.25  ? 551  LYS A O     1 
ATOM   4312 C  CB    . LYS A 1 551 ? -11.478 25.638  28.837  1.00 29.54  ? 551  LYS A CB    1 
ATOM   4313 C  CG    . LYS A 1 551 ? -10.575 24.531  29.301  1.00 34.82  ? 551  LYS A CG    1 
ATOM   4314 C  CD    . LYS A 1 551 ? -10.493 24.526  30.826  1.00 42.97  ? 551  LYS A CD    1 
ATOM   4315 C  CE    . LYS A 1 551 ? -9.454  23.525  31.321  1.00 54.40  ? 551  LYS A CE    1 
ATOM   4316 N  NZ    . LYS A 1 551 ? -9.798  22.968  32.667  1.00 61.27  ? 551  LYS A NZ    1 
ATOM   4317 N  N     . LEU A 1 552 ? -9.965  27.022  26.400  1.00 22.38  ? 552  LEU A N     1 
ATOM   4318 C  CA    . LEU A 1 552 ? -8.788  27.310  25.595  1.00 26.31  ? 552  LEU A CA    1 
ATOM   4319 C  C     . LEU A 1 552 ? -7.518  27.077  26.404  1.00 28.64  ? 552  LEU A C     1 
ATOM   4320 O  O     . LEU A 1 552 ? -7.411  27.532  27.547  1.00 25.46  ? 552  LEU A O     1 
ATOM   4321 C  CB    . LEU A 1 552 ? -8.851  28.754  25.099  1.00 25.35  ? 552  LEU A CB    1 
ATOM   4322 C  CG    . LEU A 1 552 ? -7.691  29.192  24.213  1.00 27.45  ? 552  LEU A CG    1 
ATOM   4323 C  CD1   . LEU A 1 552 ? -7.593  28.289  23.000  1.00 29.29  ? 552  LEU A CD1   1 
ATOM   4324 C  CD2   . LEU A 1 552 ? -7.866  30.655  23.797  1.00 25.08  ? 552  LEU A CD2   1 
ATOM   4325 N  N     . THR A 1 553 ? -6.563  26.354  25.823  1.00 23.38  ? 553  THR A N     1 
ATOM   4326 C  CA    . THR A 1 553 ? -5.244  26.145  26.389  1.00 23.19  ? 553  THR A CA    1 
ATOM   4327 C  C     . THR A 1 553 ? -4.214  26.525  25.339  1.00 23.26  ? 553  THR A C     1 
ATOM   4328 O  O     . THR A 1 553 ? -4.569  26.767  24.181  1.00 20.72  ? 553  THR A O     1 
ATOM   4329 C  CB    . THR A 1 553 ? -5.037  24.683  26.841  1.00 24.82  ? 553  THR A CB    1 
ATOM   4330 O  OG1   . THR A 1 553 ? -4.809  23.834  25.706  1.00 21.97  ? 553  THR A OG1   1 
ATOM   4331 C  CG2   . THR A 1 553 ? -6.257  24.186  27.631  1.00 24.52  ? 553  THR A CG2   1 
ATOM   4332 N  N     . PRO A 1 554 ? -2.930  26.613  25.710  1.00 20.28  ? 554  PRO A N     1 
ATOM   4333 C  CA    . PRO A 1 554 ? -1.897  26.890  24.699  1.00 25.12  ? 554  PRO A CA    1 
ATOM   4334 C  C     . PRO A 1 554 ? -1.814  25.858  23.596  1.00 24.71  ? 554  PRO A C     1 
ATOM   4335 O  O     . PRO A 1 554 ? -1.352  26.198  22.504  1.00 24.19  ? 554  PRO A O     1 
ATOM   4336 C  CB    . PRO A 1 554 ? -0.599  26.927  25.519  1.00 25.27  ? 554  PRO A CB    1 
ATOM   4337 C  CG    . PRO A 1 554 ? -1.036  27.349  26.870  1.00 30.37  ? 554  PRO A CG    1 
ATOM   4338 C  CD    . PRO A 1 554 ? -2.377  26.691  27.077  1.00 27.16  ? 554  PRO A CD    1 
ATOM   4339 N  N     . ILE A 1 555 ? -2.252  24.615  23.819  1.00 18.63  ? 555  ILE A N     1 
ATOM   4340 C  CA    . ILE A 1 555 ? -2.121  23.593  22.784  1.00 20.73  ? 555  ILE A CA    1 
ATOM   4341 C  C     . ILE A 1 555 ? -3.414  23.377  22.013  1.00 22.32  ? 555  ILE A C     1 
ATOM   4342 O  O     . ILE A 1 555 ? -3.410  22.624  21.030  1.00 20.59  ? 555  ILE A O     1 
ATOM   4343 C  CB    . ILE A 1 555 ? -1.609  22.255  23.357  1.00 22.13  ? 555  ILE A CB    1 
ATOM   4344 C  CG1   . ILE A 1 555 ? -2.614  21.680  24.362  1.00 23.63  ? 555  ILE A CG1   1 
ATOM   4345 C  CG2   . ILE A 1 555 ? -0.231  22.456  23.994  1.00 26.56  ? 555  ILE A CG2   1 
ATOM   4346 C  CD1   . ILE A 1 555 ? -2.453  20.185  24.627  1.00 27.42  ? 555  ILE A CD1   1 
ATOM   4347 N  N     . GLY A 1 556 ? -4.510  24.051  22.397  1.00 22.46  ? 556  GLY A N     1 
ATOM   4348 C  CA    . GLY A 1 556 ? -5.802  23.901  21.760  1.00 21.24  ? 556  GLY A CA    1 
ATOM   4349 C  C     . GLY A 1 556 ? -6.909  23.814  22.798  1.00 24.20  ? 556  GLY A C     1 
ATOM   4350 O  O     . GLY A 1 556 ? -6.705  24.098  23.973  1.00 24.69  ? 556  GLY A O     1 
ATOM   4351 N  N     . TYR A 1 557 ? -8.102  23.402  22.359  1.00 17.78  ? 557  TYR A N     1 
ATOM   4352 C  CA    . TYR A 1 557 ? -9.260  23.294  23.246  1.00 24.15  ? 557  TYR A CA    1 
ATOM   4353 C  C     . TYR A 1 557 ? -9.265  21.952  23.967  1.00 24.94  ? 557  TYR A C     1 
ATOM   4354 O  O     . TYR A 1 557 ? -9.065  20.911  23.337  1.00 22.97  ? 557  TYR A O     1 
ATOM   4355 C  CB    . TYR A 1 557 ? -10.565 23.429  22.461  1.00 20.15  ? 557  TYR A CB    1 
ATOM   4356 C  CG    . TYR A 1 557 ? -10.765 24.776  21.832  1.00 26.64  ? 557  TYR A CG    1 
ATOM   4357 C  CD1   . TYR A 1 557 ? -11.048 25.892  22.614  1.00 28.45  ? 557  TYR A CD1   1 
ATOM   4358 C  CD2   . TYR A 1 557 ? -10.689 24.931  20.453  1.00 27.42  ? 557  TYR A CD2   1 
ATOM   4359 C  CE1   . TYR A 1 557 ? -11.236 27.147  22.035  1.00 29.59  ? 557  TYR A CE1   1 
ATOM   4360 C  CE2   . TYR A 1 557 ? -10.872 26.168  19.861  1.00 25.84  ? 557  TYR A CE2   1 
ATOM   4361 C  CZ    . TYR A 1 557 ? -11.148 27.277  20.667  1.00 35.00  ? 557  TYR A CZ    1 
ATOM   4362 O  OH    . TYR A 1 557 ? -11.339 28.510  20.093  1.00 40.44  ? 557  TYR A OH    1 
ATOM   4363 N  N     . VAL A 1 558 ? -9.526  21.976  25.267  1.00 21.70  ? 558  VAL A N     1 
ATOM   4364 C  CA    . VAL A 1 558 ? -9.695  20.752  26.049  1.00 21.73  ? 558  VAL A CA    1 
ATOM   4365 C  C     . VAL A 1 558 ? -11.085 20.801  26.670  1.00 23.96  ? 558  VAL A C     1 
ATOM   4366 O  O     . VAL A 1 558 ? -11.701 21.876  26.751  1.00 22.11  ? 558  VAL A O     1 
ATOM   4367 C  CB    . VAL A 1 558 ? -8.581  20.592  27.111  1.00 23.96  ? 558  VAL A CB    1 
ATOM   4368 C  CG1   . VAL A 1 558 ? -7.202  20.642  26.463  1.00 24.31  ? 558  VAL A CG1   1 
ATOM   4369 C  CG2   . VAL A 1 558 ? -8.718  21.649  28.206  1.00 28.06  ? 558  VAL A CG2   1 
ATOM   4370 N  N     . PRO A 1 559 ? -11.630 19.654  27.095  1.00 25.48  ? 559  PRO A N     1 
ATOM   4371 C  CA    . PRO A 1 559 ? -12.956 19.673  27.724  1.00 21.05  ? 559  PRO A CA    1 
ATOM   4372 C  C     . PRO A 1 559 ? -12.965 20.532  28.979  1.00 25.99  ? 559  PRO A C     1 
ATOM   4373 O  O     . PRO A 1 559 ? -12.004 20.551  29.752  1.00 26.13  ? 559  PRO A O     1 
ATOM   4374 C  CB    . PRO A 1 559 ? -13.224 18.200  28.061  1.00 23.80  ? 559  PRO A CB    1 
ATOM   4375 C  CG    . PRO A 1 559 ? -12.295 17.422  27.204  1.00 24.62  ? 559  PRO A CG    1 
ATOM   4376 C  CD    . PRO A 1 559 ? -11.087 18.290  26.989  1.00 22.50  ? 559  PRO A CD    1 
ATOM   4377 N  N     . LYS A 1 560 ? -14.070 21.245  29.178  1.00 26.28  ? 560  LYS A N     1 
ATOM   4378 C  CA    . LYS A 1 560 ? -14.293 21.893  30.463  1.00 33.55  ? 560  LYS A CA    1 
ATOM   4379 C  C     . LYS A 1 560 ? -14.384 20.839  31.556  1.00 42.08  ? 560  LYS A C     1 
ATOM   4380 O  O     . LYS A 1 560 ? -14.846 19.718  31.328  1.00 33.34  ? 560  LYS A O     1 
ATOM   4381 C  CB    . LYS A 1 560 ? -15.585 22.711  30.457  1.00 32.33  ? 560  LYS A CB    1 
ATOM   4382 C  CG    . LYS A 1 560 ? -15.617 23.878  29.519  1.00 30.75  ? 560  LYS A CG    1 
ATOM   4383 C  CD    . LYS A 1 560 ? -16.961 24.573  29.606  1.00 33.64  ? 560  LYS A CD    1 
ATOM   4384 C  CE    . LYS A 1 560 ? -17.012 25.749  28.664  1.00 35.51  ? 560  LYS A CE    1 
ATOM   4385 N  NZ    . LYS A 1 560 ? -18.222 26.605  28.865  1.00 33.32  ? 560  LYS A NZ    1 
ATOM   4386 N  N     . GLU A 1 561 ? -13.929 21.205  32.751  1.00 55.37  ? 561  GLU A N     1 
ATOM   4387 C  CA    . GLU A 1 561 ? -14.211 20.397  33.927  1.00 58.50  ? 561  GLU A CA    1 
ATOM   4388 C  C     . GLU A 1 561 ? -15.703 20.107  33.987  1.00 57.88  ? 561  GLU A C     1 
ATOM   4389 O  O     . GLU A 1 561 ? -16.530 21.019  33.890  1.00 61.70  ? 561  GLU A O     1 
ATOM   4390 C  CB    . GLU A 1 561 ? -13.748 21.121  35.193  1.00 66.86  ? 561  GLU A CB    1 
ATOM   4391 C  CG    . GLU A 1 561 ? -12.280 21.528  35.160  1.00 78.65  ? 561  GLU A CG    1 
ATOM   4392 C  CD    . GLU A 1 561 ? -11.924 22.561  36.215  1.00 89.23  ? 561  GLU A CD    1 
ATOM   4393 O  OE1   . GLU A 1 561 ? -12.807 22.921  37.026  1.00 97.15  ? 561  GLU A OE1   1 
ATOM   4394 O  OE2   . GLU A 1 561 ? -10.758 23.014  36.230  1.00 81.71  ? 561  GLU A OE2   1 
ATOM   4395 N  N     . ASP A 1 562 ? -16.036 18.825  34.088  1.00 45.68  ? 562  ASP A N     1 
ATOM   4396 C  CA    . ASP A 1 562 ? -17.391 18.279  34.107  1.00 57.01  ? 562  ASP A CA    1 
ATOM   4397 C  C     . ASP A 1 562 ? -18.046 18.247  32.729  1.00 47.15  ? 562  ASP A C     1 
ATOM   4398 O  O     . ASP A 1 562 ? -19.241 17.931  32.637  1.00 42.20  ? 562  ASP A O     1 
ATOM   4399 C  CB    . ASP A 1 562 ? -18.309 19.027  35.085  1.00 69.40  ? 562  ASP A CB    1 
ATOM   4400 C  CG    . ASP A 1 562 ? -17.799 18.980  36.521  1.00 77.17  ? 562  ASP A CG    1 
ATOM   4401 O  OD1   . ASP A 1 562 ? -17.226 17.939  36.922  1.00 75.66  ? 562  ASP A OD1   1 
ATOM   4402 O  OD2   . ASP A 1 562 ? -17.968 19.987  37.246  1.00 80.00  ? 562  ASP A OD2   1 
ATOM   4403 N  N     . ALA A 1 563 ? -17.322 18.542  31.649  1.00 41.76  ? 563  ALA A N     1 
ATOM   4404 C  CA    . ALA A 1 563 ? -17.889 18.311  30.326  1.00 35.98  ? 563  ALA A CA    1 
ATOM   4405 C  C     . ALA A 1 563 ? -17.702 16.872  29.859  1.00 35.13  ? 563  ALA A C     1 
ATOM   4406 O  O     . ALA A 1 563 ? -18.317 16.477  28.864  1.00 36.50  ? 563  ALA A O     1 
ATOM   4407 C  CB    . ALA A 1 563 ? -17.283 19.273  29.300  1.00 33.13  ? 563  ALA A CB    1 
ATOM   4408 N  N     . LEU A 1 564 ? -16.874 16.093  30.549  1.00 33.33  ? 564  LEU A N     1 
ATOM   4409 C  CA    . LEU A 1 564 ? -16.643 14.685  30.241  1.00 36.75  ? 564  LEU A CA    1 
ATOM   4410 C  C     . LEU A 1 564 ? -17.450 13.813  31.192  1.00 35.00  ? 564  LEU A C     1 
ATOM   4411 O  O     . LEU A 1 564 ? -17.374 13.990  32.410  1.00 36.41  ? 564  LEU A O     1 
ATOM   4412 C  CB    . LEU A 1 564 ? -15.159 14.333  30.371  1.00 40.36  ? 564  LEU A CB    1 
ATOM   4413 C  CG    . LEU A 1 564 ? -14.244 14.335  29.147  1.00 38.73  ? 564  LEU A CG    1 
ATOM   4414 C  CD1   . LEU A 1 564 ? -13.029 13.454  29.414  1.00 45.52  ? 564  LEU A CD1   1 
ATOM   4415 C  CD2   . LEU A 1 564 ? -14.984 13.848  27.924  1.00 36.12  ? 564  LEU A CD2   1 
ATOM   4416 N  N     . ASN A 1 565 ? -18.218 12.874  30.643  1.00 37.94  ? 565  ASN A N     1 
ATOM   4417 C  CA    . ASN A 1 565 ? -18.946 11.916  31.476  1.00 32.80  ? 565  ASN A CA    1 
ATOM   4418 C  C     . ASN A 1 565 ? -17.946 10.926  32.055  1.00 37.13  ? 565  ASN A C     1 
ATOM   4419 O  O     . ASN A 1 565 ? -17.553 9.962   31.395  1.00 33.05  ? 565  ASN A O     1 
ATOM   4420 C  CB    . ASN A 1 565 ? -20.025 11.200  30.670  1.00 33.14  ? 565  ASN A CB    1 
ATOM   4421 C  CG    . ASN A 1 565 ? -20.901 10.292  31.531  1.00 41.38  ? 565  ASN A CG    1 
ATOM   4422 O  OD1   . ASN A 1 565 ? -20.584 10.011  32.686  1.00 42.55  ? 565  ASN A OD1   1 
ATOM   4423 N  ND2   . ASN A 1 565 ? -22.001 9.818   30.960  1.00 37.75  ? 565  ASN A ND2   1 
ATOM   4424 N  N     . LEU A 1 566 ? -17.529 11.157  33.298  1.00 37.77  ? 566  LEU A N     1 
ATOM   4425 C  CA    . LEU A 1 566 ? -16.636 10.246  34.003  1.00 42.87  ? 566  LEU A CA    1 
ATOM   4426 C  C     . LEU A 1 566 ? -17.364 9.374   35.022  1.00 46.15  ? 566  LEU A C     1 
ATOM   4427 O  O     . LEU A 1 566 ? -16.712 8.731   35.853  1.00 52.86  ? 566  LEU A O     1 
ATOM   4428 C  CB    . LEU A 1 566 ? -15.519 11.032  34.691  1.00 36.14  ? 566  LEU A CB    1 
ATOM   4429 C  CG    . LEU A 1 566 ? -14.557 11.720  33.727  1.00 44.40  ? 566  LEU A CG    1 
ATOM   4430 C  CD1   . LEU A 1 566 ? -13.448 12.428  34.483  1.00 49.40  ? 566  LEU A CD1   1 
ATOM   4431 C  CD2   . LEU A 1 566 ? -13.989 10.697  32.749  1.00 44.21  ? 566  LEU A CD2   1 
ATOM   4432 N  N     . LYS A 1 567 ? -18.693 9.328   34.967  1.00 44.97  ? 567  LYS A N     1 
ATOM   4433 C  CA    . LYS A 1 567 ? -19.464 8.598   35.962  1.00 51.99  ? 567  LYS A CA    1 
ATOM   4434 C  C     . LYS A 1 567 ? -19.257 7.099   35.801  1.00 56.08  ? 567  LYS A C     1 
ATOM   4435 O  O     . LYS A 1 567 ? -19.458 6.545   34.715  1.00 51.41  ? 567  LYS A O     1 
ATOM   4436 C  CB    . LYS A 1 567 ? -20.944 8.956   35.839  1.00 57.64  ? 567  LYS A CB    1 
ATOM   4437 C  CG    . LYS A 1 567 ? -21.208 10.452  36.032  1.00 70.57  ? 567  LYS A CG    1 
ATOM   4438 C  CD    . LYS A 1 567 ? -22.660 10.833  35.788  1.00 74.54  ? 567  LYS A CD    1 
ATOM   4439 C  CE    . LYS A 1 567 ? -22.855 12.337  35.923  1.00 71.02  ? 567  LYS A CE    1 
ATOM   4440 N  NZ    . LYS A 1 567 ? -24.287 12.732  35.797  1.00 74.68  ? 567  LYS A NZ    1 
ATOM   4441 N  N     . GLY A 1 568 ? -18.850 6.445   36.890  1.00 54.89  ? 568  GLY A N     1 
ATOM   4442 C  CA    . GLY A 1 568 ? -18.591 5.030   36.904  1.00 56.23  ? 568  GLY A CA    1 
ATOM   4443 C  C     . GLY A 1 568 ? -17.120 4.669   36.925  1.00 59.42  ? 568  GLY A C     1 
ATOM   4444 O  O     . GLY A 1 568 ? -16.768 3.579   37.387  1.00 66.14  ? 568  GLY A O     1 
ATOM   4445 N  N     . LEU A 1 569 ? -16.253 5.552   36.430  1.00 59.73  ? 569  LEU A N     1 
ATOM   4446 C  CA    . LEU A 1 569 ? -14.822 5.276   36.453  1.00 60.96  ? 569  LEU A CA    1 
ATOM   4447 C  C     . LEU A 1 569 ? -14.209 5.531   37.821  1.00 66.40  ? 569  LEU A C     1 
ATOM   4448 O  O     . LEU A 1 569 ? -13.160 4.958   38.137  1.00 66.24  ? 569  LEU A O     1 
ATOM   4449 C  CB    . LEU A 1 569 ? -14.107 6.114   35.392  1.00 51.26  ? 569  LEU A CB    1 
ATOM   4450 C  CG    . LEU A 1 569 ? -14.624 5.909   33.970  1.00 43.84  ? 569  LEU A CG    1 
ATOM   4451 C  CD1   . LEU A 1 569 ? -13.889 6.815   33.001  1.00 39.85  ? 569  LEU A CD1   1 
ATOM   4452 C  CD2   . LEU A 1 569 ? -14.479 4.447   33.563  1.00 43.53  ? 569  LEU A CD2   1 
ATOM   4453 N  N     . GLY A 1 570 ? -14.836 6.380   38.630  1.00 71.48  ? 570  GLY A N     1 
ATOM   4454 C  CA    . GLY A 1 570 ? -14.424 6.556   40.004  1.00 71.25  ? 570  GLY A CA    1 
ATOM   4455 C  C     . GLY A 1 570 ? -13.239 7.472   40.217  1.00 79.99  ? 570  GLY A C     1 
ATOM   4456 O  O     . GLY A 1 570 ? -13.394 8.696   40.296  1.00 79.46  ? 570  GLY A O     1 
ATOM   4457 N  N     . ASP A 1 571 ? -12.046 6.888   40.309  1.00 84.43  ? 571  ASP A N     1 
ATOM   4458 C  CA    . ASP A 1 571 ? -10.864 7.583   40.813  1.00 84.44  ? 571  ASP A CA    1 
ATOM   4459 C  C     . ASP A 1 571 ? -9.910  7.993   39.701  1.00 80.87  ? 571  ASP A C     1 
ATOM   4460 O  O     . ASP A 1 571 ? -8.690  7.894   39.855  1.00 82.44  ? 571  ASP A O     1 
ATOM   4461 C  CB    . ASP A 1 571 ? -10.149 6.707   41.837  1.00 88.01  ? 571  ASP A CB    1 
ATOM   4462 C  CG    . ASP A 1 571 ? -11.119 5.969   42.747  1.00 89.04  ? 571  ASP A CG    1 
ATOM   4463 O  OD1   . ASP A 1 571 ? -12.128 6.575   43.171  1.00 89.04  ? 571  ASP A OD1   1 
ATOM   4464 O  OD2   . ASP A 1 571 ? -10.879 4.776   43.026  1.00 89.98  ? 571  ASP A OD2   1 
ATOM   4465 N  N     . VAL A 1 572 ? -10.438 8.468   38.573  1.00 79.44  ? 572  VAL A N     1 
ATOM   4466 C  CA    . VAL A 1 572 ? -9.590  8.888   37.463  1.00 71.16  ? 572  VAL A CA    1 
ATOM   4467 C  C     . VAL A 1 572 ? -8.940  10.225  37.792  1.00 66.30  ? 572  VAL A C     1 
ATOM   4468 O  O     . VAL A 1 572 ? -9.618  11.192  38.165  1.00 62.34  ? 572  VAL A O     1 
ATOM   4469 C  CB    . VAL A 1 572 ? -10.402 8.966   36.163  1.00 67.80  ? 572  VAL A CB    1 
ATOM   4470 C  CG1   . VAL A 1 572 ? -9.678  9.814   35.140  1.00 61.46  ? 572  VAL A CG1   1 
ATOM   4471 C  CG2   . VAL A 1 572 ? -10.645 7.573   35.610  1.00 61.07  ? 572  VAL A CG2   1 
ATOM   4472 N  N     . ASN A 1 573 ? -7.619  10.288  37.643  1.00 64.69  ? 573  ASN A N     1 
ATOM   4473 C  CA    . ASN A 1 573 ? -6.845  11.476  37.998  1.00 60.12  ? 573  ASN A CA    1 
ATOM   4474 C  C     . ASN A 1 573 ? -6.953  12.493  36.867  1.00 61.46  ? 573  ASN A C     1 
ATOM   4475 O  O     . ASN A 1 573 ? -6.104  12.561  35.975  1.00 57.05  ? 573  ASN A O     1 
ATOM   4476 C  CB    . ASN A 1 573 ? -5.397  11.098  38.281  1.00 59.63  ? 573  ASN A CB    1 
ATOM   4477 C  CG    . ASN A 1 573 ? -4.565  12.276  38.746  1.00 63.43  ? 573  ASN A CG    1 
ATOM   4478 O  OD1   . ASN A 1 573 ? -5.073  13.389  38.916  1.00 64.89  ? 573  ASN A OD1   1 
ATOM   4479 N  ND2   . ASN A 1 573 ? -3.277  12.035  38.970  1.00 58.95  ? 573  ASN A ND2   1 
ATOM   4480 N  N     . VAL A 1 574 ? -8.005  13.314  36.928  1.00 58.65  ? 574  VAL A N     1 
ATOM   4481 C  CA    . VAL A 1 574 ? -8.271  14.305  35.889  1.00 57.12  ? 574  VAL A CA    1 
ATOM   4482 C  C     . VAL A 1 574 ? -7.153  15.335  35.808  1.00 54.22  ? 574  VAL A C     1 
ATOM   4483 O  O     . VAL A 1 574 ? -6.856  15.859  34.727  1.00 46.05  ? 574  VAL A O     1 
ATOM   4484 C  CB    . VAL A 1 574 ? -9.634  14.976  36.147  1.00 56.55  ? 574  VAL A CB    1 
ATOM   4485 C  CG1   . VAL A 1 574 ? -9.994  15.931  35.015  1.00 54.63  ? 574  VAL A CG1   1 
ATOM   4486 C  CG2   . VAL A 1 574 ? -10.710 13.922  36.335  1.00 60.28  ? 574  VAL A CG2   1 
ATOM   4487 N  N     . GLU A 1 575 ? -6.521  15.645  36.942  1.00 61.04  ? 575  GLU A N     1 
ATOM   4488 C  CA    . GLU A 1 575 ? -5.422  16.605  36.952  1.00 57.72  ? 575  GLU A CA    1 
ATOM   4489 C  C     . GLU A 1 575 ? -4.267  16.127  36.084  1.00 51.45  ? 575  GLU A C     1 
ATOM   4490 O  O     . GLU A 1 575 ? -3.693  16.903  35.311  1.00 47.83  ? 575  GLU A O     1 
ATOM   4491 C  CB    . GLU A 1 575 ? -4.948  16.838  38.388  1.00 63.71  ? 575  GLU A CB    1 
ATOM   4492 C  CG    . GLU A 1 575 ? -5.675  17.946  39.129  1.00 75.03  ? 575  GLU A CG    1 
ATOM   4493 C  CD    . GLU A 1 575 ? -5.231  19.327  38.686  1.00 81.60  ? 575  GLU A CD    1 
ATOM   4494 O  OE1   . GLU A 1 575 ? -5.599  19.745  37.566  1.00 80.58  ? 575  GLU A OE1   1 
ATOM   4495 O  OE2   . GLU A 1 575 ? -4.502  19.991  39.455  1.00 84.03  ? 575  GLU A OE2   1 
ATOM   4496 N  N     . GLU A 1 576 ? -3.907  14.847  36.210  1.00 51.57  ? 576  GLU A N     1 
ATOM   4497 C  CA    . GLU A 1 576 ? -2.790  14.284  35.460  1.00 49.24  ? 576  GLU A CA    1 
ATOM   4498 C  C     . GLU A 1 576 ? -3.171  13.970  34.018  1.00 46.93  ? 576  GLU A C     1 
ATOM   4499 O  O     . GLU A 1 576 ? -2.331  14.097  33.120  1.00 44.14  ? 576  GLU A O     1 
ATOM   4500 C  CB    . GLU A 1 576 ? -2.277  13.025  36.167  1.00 54.30  ? 576  GLU A CB    1 
ATOM   4501 C  CG    . GLU A 1 576 ? -0.793  12.722  35.975  1.00 62.63  ? 576  GLU A CG    1 
ATOM   4502 C  CD    . GLU A 1 576 ? -0.259  11.711  36.991  1.00 71.36  ? 576  GLU A CD    1 
ATOM   4503 O  OE1   . GLU A 1 576 ? -0.979  11.398  37.965  1.00 71.10  ? 576  GLU A OE1   1 
ATOM   4504 O  OE2   . GLU A 1 576 ? 0.885   11.231  36.816  1.00 73.57  ? 576  GLU A OE2   1 
ATOM   4505 N  N     . LEU A 1 577 ? -4.425  13.572  33.772  1.00 45.85  ? 577  LEU A N     1 
ATOM   4506 C  CA    . LEU A 1 577 ? -4.853  13.275  32.409  1.00 44.58  ? 577  LEU A CA    1 
ATOM   4507 C  C     . LEU A 1 577 ? -4.849  14.514  31.521  1.00 36.76  ? 577  LEU A C     1 
ATOM   4508 O  O     . LEU A 1 577 ? -4.573  14.402  30.325  1.00 33.45  ? 577  LEU A O     1 
ATOM   4509 C  CB    . LEU A 1 577 ? -6.247  12.647  32.397  1.00 33.62  ? 577  LEU A CB    1 
ATOM   4510 C  CG    . LEU A 1 577 ? -6.344  11.124  32.320  1.00 45.21  ? 577  LEU A CG    1 
ATOM   4511 C  CD1   . LEU A 1 577 ? -6.400  10.524  33.707  1.00 57.54  ? 577  LEU A CD1   1 
ATOM   4512 C  CD2   . LEU A 1 577 ? -7.564  10.701  31.526  1.00 43.73  ? 577  LEU A CD2   1 
ATOM   4513 N  N     . PHE A 1 578 ? -5.172  15.690  32.070  1.00 28.32  ? 578  PHE A N     1 
ATOM   4514 C  CA    . PHE A 1 578 ? -5.226  16.916  31.282  1.00 30.28  ? 578  PHE A CA    1 
ATOM   4515 C  C     . PHE A 1 578 ? -4.180  17.938  31.690  1.00 29.80  ? 578  PHE A C     1 
ATOM   4516 O  O     . PHE A 1 578 ? -4.219  19.069  31.205  1.00 35.04  ? 578  PHE A O     1 
ATOM   4517 C  CB    . PHE A 1 578 ? -6.616  17.537  31.348  1.00 33.74  ? 578  PHE A CB    1 
ATOM   4518 C  CG    . PHE A 1 578 ? -7.641  16.776  30.579  1.00 30.61  ? 578  PHE A CG    1 
ATOM   4519 C  CD1   . PHE A 1 578 ? -7.769  16.965  29.215  1.00 28.47  ? 578  PHE A CD1   1 
ATOM   4520 C  CD2   . PHE A 1 578 ? -8.464  15.862  31.217  1.00 32.22  ? 578  PHE A CD2   1 
ATOM   4521 C  CE1   . PHE A 1 578 ? -8.711  16.273  28.495  1.00 25.35  ? 578  PHE A CE1   1 
ATOM   4522 C  CE2   . PHE A 1 578 ? -9.418  15.154  30.506  1.00 33.58  ? 578  PHE A CE2   1 
ATOM   4523 C  CZ    . PHE A 1 578 ? -9.546  15.362  29.143  1.00 30.72  ? 578  PHE A CZ    1 
ATOM   4524 N  N     . GLY A 1 579 ? -3.231  17.558  32.538  1.00 34.75  ? 579  GLY A N     1 
ATOM   4525 C  CA    . GLY A 1 579 ? -2.171  18.479  32.899  1.00 35.70  ? 579  GLY A CA    1 
ATOM   4526 C  C     . GLY A 1 579 ? -1.320  18.835  31.693  1.00 37.87  ? 579  GLY A C     1 
ATOM   4527 O  O     . GLY A 1 579 ? -0.980  17.980  30.871  1.00 37.34  ? 579  GLY A O     1 
ATOM   4528 N  N     . ILE A 1 580 ? -0.974  20.112  31.599  1.00 34.58  ? 580  ILE A N     1 
ATOM   4529 C  CA    . ILE A 1 580 ? -0.158  20.654  30.522  1.00 34.19  ? 580  ILE A CA    1 
ATOM   4530 C  C     . ILE A 1 580 ? 1.001   21.378  31.182  1.00 33.07  ? 580  ILE A C     1 
ATOM   4531 O  O     . ILE A 1 580 ? 0.810   22.410  31.833  1.00 33.38  ? 580  ILE A O     1 
ATOM   4532 C  CB    . ILE A 1 580 ? -0.970  21.583  29.609  1.00 38.72  ? 580  ILE A CB    1 
ATOM   4533 C  CG1   . ILE A 1 580 ? -1.911  20.736  28.741  1.00 31.68  ? 580  ILE A CG1   1 
ATOM   4534 C  CG2   . ILE A 1 580 ? -0.055  22.475  28.758  1.00 36.91  ? 580  ILE A CG2   1 
ATOM   4535 C  CD1   . ILE A 1 580 ? -3.273  21.352  28.536  1.00 34.12  ? 580  ILE A CD1   1 
ATOM   4536 N  N     . SER A 1 581 ? 2.192   20.817  31.067  1.00 31.26  ? 581  SER A N     1 
ATOM   4537 C  CA    . SER A 1 581 ? 3.366   21.362  31.729  1.00 31.99  ? 581  SER A CA    1 
ATOM   4538 C  C     . SER A 1 581 ? 4.168   22.182  30.728  1.00 32.73  ? 581  SER A C     1 
ATOM   4539 O  O     . SER A 1 581 ? 4.438   21.723  29.612  1.00 29.86  ? 581  SER A O     1 
ATOM   4540 C  CB    . SER A 1 581 ? 4.214   20.237  32.323  1.00 35.85  ? 581  SER A CB    1 
ATOM   4541 O  OG    . SER A 1 581 ? 5.562   20.333  31.910  1.00 37.50  ? 581  SER A OG    1 
ATOM   4542 N  N     . LYS A 1 582 ? 4.524   23.404  31.121  1.00 32.25  ? 582  LYS A N     1 
ATOM   4543 C  CA    . LYS A 1 582 ? 5.336   24.251  30.253  1.00 29.90  ? 582  LYS A CA    1 
ATOM   4544 C  C     . LYS A 1 582 ? 6.672   23.594  29.936  1.00 32.83  ? 582  LYS A C     1 
ATOM   4545 O  O     . LYS A 1 582 ? 7.157   23.665  28.800  1.00 31.80  ? 582  LYS A O     1 
ATOM   4546 C  CB    . LYS A 1 582 ? 5.549   25.611  30.915  1.00 36.72  ? 582  LYS A CB    1 
ATOM   4547 C  CG    . LYS A 1 582 ? 6.442   26.549  30.141  1.00 31.27  ? 582  LYS A CG    1 
ATOM   4548 C  CD    . LYS A 1 582 ? 6.494   27.907  30.822  1.00 37.55  ? 582  LYS A CD    1 
ATOM   4549 C  CE    . LYS A 1 582 ? 7.286   28.914  29.996  1.00 38.49  ? 582  LYS A CE    1 
ATOM   4550 N  NZ    . LYS A 1 582 ? 7.072   30.291  30.538  1.00 45.48  ? 582  LYS A NZ    1 
ATOM   4551 N  N     . GLU A 1 583 ? 7.280   22.949  30.932  1.00 33.48  ? 583  GLU A N     1 
ATOM   4552 C  CA    . GLU A 1 583 ? 8.569   22.306  30.718  1.00 33.12  ? 583  GLU A CA    1 
ATOM   4553 C  C     . GLU A 1 583 ? 8.473   21.227  29.649  1.00 31.53  ? 583  GLU A C     1 
ATOM   4554 O  O     . GLU A 1 583 ? 9.352   21.123  28.785  1.00 33.04  ? 583  GLU A O     1 
ATOM   4555 C  CB    . GLU A 1 583 ? 9.090   21.714  32.031  1.00 36.16  ? 583  GLU A CB    1 
ATOM   4556 C  CG    . GLU A 1 583 ? 9.280   22.732  33.154  1.00 51.26  ? 583  GLU A CG    1 
ATOM   4557 C  CD    . GLU A 1 583 ? 7.990   23.054  33.912  1.00 58.35  ? 583  GLU A CD    1 
ATOM   4558 O  OE1   . GLU A 1 583 ? 6.940   22.446  33.611  1.00 53.15  ? 583  GLU A OE1   1 
ATOM   4559 O  OE2   . GLU A 1 583 ? 8.030   23.921  34.816  1.00 76.52  ? 583  GLU A OE2   1 
ATOM   4560 N  N     . PHE A 1 584 ? 7.422   20.403  29.694  1.00 29.60  ? 584  PHE A N     1 
ATOM   4561 C  CA    . PHE A 1 584 ? 7.303   19.331  28.709  1.00 29.15  ? 584  PHE A CA    1 
ATOM   4562 C  C     . PHE A 1 584 ? 7.125   19.898  27.305  1.00 28.90  ? 584  PHE A C     1 
ATOM   4563 O  O     . PHE A 1 584 ? 7.746   19.429  26.343  1.00 24.87  ? 584  PHE A O     1 
ATOM   4564 C  CB    . PHE A 1 584 ? 6.138   18.404  29.060  1.00 33.13  ? 584  PHE A CB    1 
ATOM   4565 C  CG    . PHE A 1 584 ? 5.842   17.401  27.986  1.00 29.72  ? 584  PHE A CG    1 
ATOM   4566 C  CD1   . PHE A 1 584 ? 6.531   16.201  27.939  1.00 31.02  ? 584  PHE A CD1   1 
ATOM   4567 C  CD2   . PHE A 1 584 ? 4.904   17.673  27.000  1.00 28.36  ? 584  PHE A CD2   1 
ATOM   4568 C  CE1   . PHE A 1 584 ? 6.286   15.282  26.935  1.00 31.01  ? 584  PHE A CE1   1 
ATOM   4569 C  CE2   . PHE A 1 584 ? 4.656   16.757  25.988  1.00 27.41  ? 584  PHE A CE2   1 
ATOM   4570 C  CZ    . PHE A 1 584 ? 5.349   15.561  25.960  1.00 26.80  ? 584  PHE A CZ    1 
ATOM   4571 N  N     . TRP A 1 585 ? 6.272   20.910  27.168  1.00 26.06  ? 585  TRP A N     1 
ATOM   4572 C  CA    . TRP A 1 585 ? 5.914   21.402  25.847  1.00 28.28  ? 585  TRP A CA    1 
ATOM   4573 C  C     . TRP A 1 585 ? 6.987   22.291  25.237  1.00 26.13  ? 585  TRP A C     1 
ATOM   4574 O  O     . TRP A 1 585 ? 7.022   22.432  24.010  1.00 25.72  ? 585  TRP A O     1 
ATOM   4575 C  CB    . TRP A 1 585 ? 4.558   22.116  25.919  1.00 26.83  ? 585  TRP A CB    1 
ATOM   4576 C  CG    . TRP A 1 585 ? 3.465   21.110  25.941  1.00 29.68  ? 585  TRP A CG    1 
ATOM   4577 C  CD1   . TRP A 1 585 ? 2.842   20.588  27.046  1.00 30.10  ? 585  TRP A CD1   1 
ATOM   4578 C  CD2   . TRP A 1 585 ? 2.920   20.419  24.810  1.00 30.13  ? 585  TRP A CD2   1 
ATOM   4579 N  NE1   . TRP A 1 585 ? 1.915   19.642  26.666  1.00 27.81  ? 585  TRP A NE1   1 
ATOM   4580 C  CE2   . TRP A 1 585 ? 1.944   19.514  25.302  1.00 27.97  ? 585  TRP A CE2   1 
ATOM   4581 C  CE3   . TRP A 1 585 ? 3.147   20.489  23.430  1.00 26.60  ? 585  TRP A CE3   1 
ATOM   4582 C  CZ2   . TRP A 1 585 ? 1.192   18.691  24.461  1.00 27.19  ? 585  TRP A CZ2   1 
ATOM   4583 C  CZ3   . TRP A 1 585 ? 2.396   19.672  22.595  1.00 30.35  ? 585  TRP A CZ3   1 
ATOM   4584 C  CH2   . TRP A 1 585 ? 1.433   18.778  23.117  1.00 31.07  ? 585  TRP A CH2   1 
ATOM   4585 N  N     . GLU A 1 586 ? 7.875   22.866  26.055  1.00 27.51  ? 586  GLU A N     1 
ATOM   4586 C  CA    . GLU A 1 586 ? 9.016   23.593  25.508  1.00 29.58  ? 586  GLU A CA    1 
ATOM   4587 C  C     . GLU A 1 586 ? 9.990   22.645  24.828  1.00 29.16  ? 586  GLU A C     1 
ATOM   4588 O  O     . GLU A 1 586 ? 10.548  22.969  23.773  1.00 28.49  ? 586  GLU A O     1 
ATOM   4589 C  CB    . GLU A 1 586 ? 9.732   24.364  26.613  1.00 31.50  ? 586  GLU A CB    1 
ATOM   4590 C  CG    . GLU A 1 586 ? 9.022   25.632  27.028  1.00 42.61  ? 586  GLU A CG    1 
ATOM   4591 C  CD    . GLU A 1 586 ? 9.890   26.502  27.910  1.00 52.53  ? 586  GLU A CD    1 
ATOM   4592 O  OE1   . GLU A 1 586 ? 10.765  25.941  28.600  1.00 52.25  ? 586  GLU A OE1   1 
ATOM   4593 O  OE2   . GLU A 1 586 ? 9.703   27.738  27.902  1.00 56.43  ? 586  GLU A OE2   1 
ATOM   4594 N  N     . LYS A 1 587 ? 10.232  21.485  25.442  1.00 23.87  ? 587  LYS A N     1 
ATOM   4595 C  CA    . LYS A 1 587 ? 11.039  20.456  24.796  1.00 25.68  ? 587  LYS A CA    1 
ATOM   4596 C  C     . LYS A 1 587 ? 10.322  19.903  23.575  1.00 25.50  ? 587  LYS A C     1 
ATOM   4597 O  O     . LYS A 1 587 ? 10.949  19.640  22.544  1.00 27.77  ? 587  LYS A O     1 
ATOM   4598 C  CB    . LYS A 1 587 ? 11.347  19.341  25.793  1.00 29.04  ? 587  LYS A CB    1 
ATOM   4599 C  CG    . LYS A 1 587 ? 12.011  18.104  25.178  1.00 30.86  ? 587  LYS A CG    1 
ATOM   4600 C  CD    . LYS A 1 587 ? 13.387  18.430  24.597  1.00 40.80  ? 587  LYS A CD    1 
ATOM   4601 C  CE    . LYS A 1 587 ? 14.174  17.144  24.317  1.00 43.25  ? 587  LYS A CE    1 
ATOM   4602 N  NZ    . LYS A 1 587 ? 15.489  17.386  23.642  1.00 45.74  ? 587  LYS A NZ    1 
ATOM   4603 N  N     . GLU A 1 588 ? 9.004   19.716  23.677  1.00 26.75  ? 588  GLU A N     1 
ATOM   4604 C  CA    . GLU A 1 588 ? 8.257   19.120  22.574  1.00 25.40  ? 588  GLU A CA    1 
ATOM   4605 C  C     . GLU A 1 588 ? 8.316   20.004  21.330  1.00 24.25  ? 588  GLU A C     1 
ATOM   4606 O  O     . GLU A 1 588 ? 8.583   19.515  20.231  1.00 23.07  ? 588  GLU A O     1 
ATOM   4607 C  CB    . GLU A 1 588 ? 6.815   18.857  23.005  1.00 24.65  ? 588  GLU A CB    1 
ATOM   4608 C  CG    . GLU A 1 588 ? 5.984   18.008  22.030  1.00 24.50  ? 588  GLU A CG    1 
ATOM   4609 C  CD    . GLU A 1 588 ? 6.417   16.537  21.947  1.00 26.50  ? 588  GLU A CD    1 
ATOM   4610 O  OE1   . GLU A 1 588 ? 7.136   16.033  22.835  1.00 22.33  ? 588  GLU A OE1   1 
ATOM   4611 O  OE2   . GLU A 1 588 ? 6.028   15.881  20.967  1.00 25.87  ? 588  GLU A OE2   1 
ATOM   4612 N  N     . VAL A 1 589 ? 8.087   21.313  21.478  1.00 20.34  ? 589  VAL A N     1 
ATOM   4613 C  CA    . VAL A 1 589 ? 8.104   22.187  20.298  1.00 23.42  ? 589  VAL A CA    1 
ATOM   4614 C  C     . VAL A 1 589 ? 9.491   22.229  19.669  1.00 23.68  ? 589  VAL A C     1 
ATOM   4615 O  O     . VAL A 1 589 ? 9.629   22.300  18.446  1.00 23.71  ? 589  VAL A O     1 
ATOM   4616 C  CB    . VAL A 1 589 ? 7.614   23.608  20.638  1.00 27.31  ? 589  VAL A CB    1 
ATOM   4617 C  CG1   . VAL A 1 589 ? 6.146   23.584  20.952  1.00 31.80  ? 589  VAL A CG1   1 
ATOM   4618 C  CG2   . VAL A 1 589 ? 8.406   24.187  21.789  1.00 32.34  ? 589  VAL A CG2   1 
ATOM   4619 N  N     . GLU A 1 590 ? 10.535  22.207  20.497  1.00 22.93  ? 590  GLU A N     1 
ATOM   4620 C  CA    . GLU A 1 590 ? 11.895  22.152  19.985  1.00 22.45  ? 590  GLU A CA    1 
ATOM   4621 C  C     . GLU A 1 590 ? 12.132  20.882  19.170  1.00 25.01  ? 590  GLU A C     1 
ATOM   4622 O  O     . GLU A 1 590 ? 12.759  20.928  18.106  1.00 27.47  ? 590  GLU A O     1 
ATOM   4623 C  CB    . GLU A 1 590 ? 12.865  22.243  21.160  1.00 27.05  ? 590  GLU A CB    1 
ATOM   4624 C  CG    . GLU A 1 590 ? 14.315  22.010  20.805  1.00 37.34  ? 590  GLU A CG    1 
ATOM   4625 C  CD    . GLU A 1 590 ? 15.218  22.104  22.020  1.00 46.06  ? 590  GLU A CD    1 
ATOM   4626 O  OE1   . GLU A 1 590 ? 14.799  22.723  23.027  1.00 50.84  ? 590  GLU A OE1   1 
ATOM   4627 O  OE2   . GLU A 1 590 ? 16.337  21.548  21.965  1.00 56.59  ? 590  GLU A OE2   1 
ATOM   4628 N  N     . GLU A 1 591 ? 11.636  19.732  19.650  1.00 21.74  ? 591  GLU A N     1 
ATOM   4629 C  CA    . GLU A 1 591 ? 11.823  18.496  18.889  1.00 22.75  ? 591  GLU A CA    1 
ATOM   4630 C  C     . GLU A 1 591 ? 11.054  18.545  17.578  1.00 19.93  ? 591  GLU A C     1 
ATOM   4631 O  O     . GLU A 1 591 ? 11.532  18.049  16.554  1.00 20.37  ? 591  GLU A O     1 
ATOM   4632 C  CB    . GLU A 1 591 ? 11.394  17.271  19.708  1.00 20.49  ? 591  GLU A CB    1 
ATOM   4633 C  CG    . GLU A 1 591 ? 12.335  16.945  20.859  1.00 21.72  ? 591  GLU A CG    1 
ATOM   4634 C  CD    . GLU A 1 591 ? 13.778  16.746  20.404  1.00 31.96  ? 591  GLU A CD    1 
ATOM   4635 O  OE1   . GLU A 1 591 ? 14.008  16.053  19.381  1.00 30.09  ? 591  GLU A OE1   1 
ATOM   4636 O  OE2   . GLU A 1 591 ? 14.688  17.295  21.067  1.00 32.34  ? 591  GLU A OE2   1 
ATOM   4637 N  N     . ILE A 1 592 ? 9.857   19.132  17.595  1.00 17.75  ? 592  ILE A N     1 
ATOM   4638 C  CA    . ILE A 1 592 ? 9.098   19.278  16.359  1.00 19.70  ? 592  ILE A CA    1 
ATOM   4639 C  C     . ILE A 1 592 ? 9.817   20.238  15.415  1.00 21.28  ? 592  ILE A C     1 
ATOM   4640 O  O     . ILE A 1 592 ? 9.916   19.998  14.206  1.00 20.68  ? 592  ILE A O     1 
ATOM   4641 C  CB    . ILE A 1 592 ? 7.666   19.750  16.680  1.00 22.23  ? 592  ILE A CB    1 
ATOM   4642 C  CG1   . ILE A 1 592 ? 6.941   18.690  17.533  1.00 22.83  ? 592  ILE A CG1   1 
ATOM   4643 C  CG2   . ILE A 1 592 ? 6.896   20.044  15.395  1.00 22.17  ? 592  ILE A CG2   1 
ATOM   4644 C  CD1   . ILE A 1 592 ? 5.755   19.232  18.304  1.00 25.52  ? 592  ILE A CD1   1 
ATOM   4645 N  N     . ASP A 1 593 ? 10.334  21.333  15.959  1.00 21.47  ? 593  ASP A N     1 
ATOM   4646 C  CA    . ASP A 1 593 ? 11.044  22.311  15.142  1.00 19.73  ? 593  ASP A CA    1 
ATOM   4647 C  C     . ASP A 1 593 ? 12.243  21.663  14.450  1.00 23.06  ? 593  ASP A C     1 
ATOM   4648 O  O     . ASP A 1 593 ? 12.383  21.749  13.225  1.00 24.62  ? 593  ASP A O     1 
ATOM   4649 C  CB    . ASP A 1 593 ? 11.456  23.485  16.030  1.00 21.43  ? 593  ASP A CB    1 
ATOM   4650 C  CG    . ASP A 1 593 ? 12.097  24.631  15.253  1.00 35.26  ? 593  ASP A CG    1 
ATOM   4651 O  OD1   . ASP A 1 593 ? 11.804  24.813  14.055  1.00 31.34  ? 593  ASP A OD1   1 
ATOM   4652 O  OD2   . ASP A 1 593 ? 12.904  25.353  15.860  1.00 40.59  ? 593  ASP A OD2   1 
ATOM   4653 N  N     . LYS A 1 594 ? 13.079  20.948  15.218  1.00 22.48  ? 594  LYS A N     1 
ATOM   4654 C  CA    . LYS A 1 594 ? 14.257  20.292  14.651  1.00 26.65  ? 594  LYS A CA    1 
ATOM   4655 C  C     . LYS A 1 594 ? 13.876  19.281  13.581  1.00 27.86  ? 594  LYS A C     1 
ATOM   4656 O  O     . LYS A 1 594 ? 14.554  19.162  12.553  1.00 26.83  ? 594  LYS A O     1 
ATOM   4657 C  CB    . LYS A 1 594 ? 15.059  19.604  15.758  1.00 23.26  ? 594  LYS A CB    1 
ATOM   4658 C  CG    . LYS A 1 594 ? 15.676  20.576  16.734  1.00 30.28  ? 594  LYS A CG    1 
ATOM   4659 C  CD    . LYS A 1 594 ? 16.713  19.912  17.640  1.00 29.66  ? 594  LYS A CD    1 
ATOM   4660 C  CE    . LYS A 1 594 ? 16.084  18.955  18.624  1.00 26.29  ? 594  LYS A CE    1 
ATOM   4661 N  NZ    . LYS A 1 594 ? 16.975  18.757  19.821  1.00 25.07  ? 594  LYS A NZ    1 
ATOM   4662 N  N     . TYR A 1 595 ? 12.803  18.526  13.820  1.00 26.78  ? 595  TYR A N     1 
ATOM   4663 C  CA    . TYR A 1 595 ? 12.388  17.497  12.879  1.00 24.25  ? 595  TYR A CA    1 
ATOM   4664 C  C     . TYR A 1 595 ? 11.881  18.107  11.578  1.00 25.36  ? 595  TYR A C     1 
ATOM   4665 O  O     . TYR A 1 595 ? 12.287  17.689  10.487  1.00 25.35  ? 595  TYR A O     1 
ATOM   4666 C  CB    . TYR A 1 595 ? 11.322  16.620  13.540  1.00 22.47  ? 595  TYR A CB    1 
ATOM   4667 C  CG    . TYR A 1 595 ? 10.707  15.596  12.635  1.00 24.84  ? 595  TYR A CG    1 
ATOM   4668 C  CD1   . TYR A 1 595 ? 11.320  14.371  12.419  1.00 20.68  ? 595  TYR A CD1   1 
ATOM   4669 C  CD2   . TYR A 1 595 ? 9.487   15.845  12.018  1.00 26.51  ? 595  TYR A CD2   1 
ATOM   4670 C  CE1   . TYR A 1 595 ? 10.735  13.419  11.596  1.00 22.80  ? 595  TYR A CE1   1 
ATOM   4671 C  CE2   . TYR A 1 595 ? 8.901   14.913  11.200  1.00 25.20  ? 595  TYR A CE2   1 
ATOM   4672 C  CZ    . TYR A 1 595 ? 9.525   13.710  10.988  1.00 22.38  ? 595  TYR A CZ    1 
ATOM   4673 O  OH    . TYR A 1 595 ? 8.906   12.793  10.173  1.00 30.03  ? 595  TYR A OH    1 
ATOM   4674 N  N     . LEU A 1 596 ? 11.010  19.116  11.667  1.00 23.49  ? 596  LEU A N     1 
ATOM   4675 C  CA    . LEU A 1 596 ? 10.446  19.686  10.446  1.00 25.68  ? 596  LEU A CA    1 
ATOM   4676 C  C     . LEU A 1 596 ? 11.497  20.471  9.666   1.00 32.45  ? 596  LEU A C     1 
ATOM   4677 O  O     . LEU A 1 596 ? 11.483  20.472  8.428   1.00 28.05  ? 596  LEU A O     1 
ATOM   4678 C  CB    . LEU A 1 596 ? 9.245   20.577  10.770  1.00 26.90  ? 596  LEU A CB    1 
ATOM   4679 C  CG    . LEU A 1 596 ? 7.957   19.981  11.361  1.00 26.38  ? 596  LEU A CG    1 
ATOM   4680 C  CD1   . LEU A 1 596 ? 7.048   21.107  11.850  1.00 29.63  ? 596  LEU A CD1   1 
ATOM   4681 C  CD2   . LEU A 1 596 ? 7.227   19.108  10.336  1.00 26.22  ? 596  LEU A CD2   1 
ATOM   4682 N  N     . GLU A 1 597 ? 12.419  21.141  10.366  1.00 29.70  ? 597  GLU A N     1 
ATOM   4683 C  CA    . GLU A 1 597 ? 13.477  21.873  9.673   1.00 34.26  ? 597  GLU A CA    1 
ATOM   4684 C  C     . GLU A 1 597 ? 14.363  20.925  8.880   1.00 29.39  ? 597  GLU A C     1 
ATOM   4685 O  O     . GLU A 1 597 ? 14.649  21.158  7.700   1.00 33.19  ? 597  GLU A O     1 
ATOM   4686 C  CB    . GLU A 1 597 ? 14.321  22.665  10.671  1.00 32.25  ? 597  GLU A CB    1 
ATOM   4687 C  CG    . GLU A 1 597 ? 15.558  23.275  10.041  1.00 44.02  ? 597  GLU A CG    1 
ATOM   4688 C  CD    . GLU A 1 597 ? 16.483  23.912  11.053  1.00 57.34  ? 597  GLU A CD    1 
ATOM   4689 O  OE1   . GLU A 1 597 ? 16.583  23.383  12.182  1.00 60.83  ? 597  GLU A OE1   1 
ATOM   4690 O  OE2   . GLU A 1 597 ? 17.107  24.942  10.719  1.00 62.28  ? 597  GLU A OE2   1 
ATOM   4691 N  N     . ASP A 1 598 ? 14.813  19.850  9.523   1.00 28.11  ? 598  ASP A N     1 
ATOM   4692 C  CA    . ASP A 1 598 ? 15.689  18.893  8.859   1.00 25.25  ? 598  ASP A CA    1 
ATOM   4693 C  C     . ASP A 1 598 ? 14.938  18.099  7.798   1.00 32.15  ? 598  ASP A C     1 
ATOM   4694 O  O     . ASP A 1 598 ? 15.383  17.996  6.647   1.00 27.67  ? 598  ASP A O     1 
ATOM   4695 C  CB    . ASP A 1 598 ? 16.303  17.953  9.901   1.00 27.74  ? 598  ASP A CB    1 
ATOM   4696 C  CG    . ASP A 1 598 ? 17.267  16.958  9.289   1.00 38.28  ? 598  ASP A CG    1 
ATOM   4697 O  OD1   . ASP A 1 598 ? 18.045  17.377  8.408   1.00 43.50  ? 598  ASP A OD1   1 
ATOM   4698 O  OD2   . ASP A 1 598 ? 17.259  15.768  9.693   1.00 37.24  ? 598  ASP A OD2   1 
ATOM   4699 N  N     . GLN A 1 599 ? 13.798  17.522  8.169   1.00 27.77  ? 599  GLN A N     1 
ATOM   4700 C  CA    . GLN A 1 599 ? 13.192  16.500  7.331   1.00 20.97  ? 599  GLN A CA    1 
ATOM   4701 C  C     . GLN A 1 599 ? 12.367  17.096  6.202   1.00 21.79  ? 599  GLN A C     1 
ATOM   4702 O  O     . GLN A 1 599 ? 12.263  16.489  5.135   1.00 27.03  ? 599  GLN A O     1 
ATOM   4703 C  CB    . GLN A 1 599 ? 12.337  15.575  8.201   1.00 20.67  ? 599  GLN A CB    1 
ATOM   4704 C  CG    . GLN A 1 599 ? 13.175  14.699  9.102   1.00 26.30  ? 599  GLN A CG    1 
ATOM   4705 C  CD    . GLN A 1 599 ? 13.971  13.686  8.295   1.00 29.10  ? 599  GLN A CD    1 
ATOM   4706 O  OE1   . GLN A 1 599 ? 13.410  12.981  7.457   1.00 27.07  ? 599  GLN A OE1   1 
ATOM   4707 N  NE2   . GLN A 1 599 ? 15.283  13.629  8.521   1.00 30.06  ? 599  GLN A NE2   1 
ATOM   4708 N  N     . VAL A 1 600 ? 11.766  18.269  6.394   1.00 27.10  ? 600  VAL A N     1 
ATOM   4709 C  CA    . VAL A 1 600 ? 10.957  18.862  5.346   1.00 19.72  ? 600  VAL A CA    1 
ATOM   4710 C  C     . VAL A 1 600 ? 11.648  20.054  4.691   1.00 28.77  ? 600  VAL A C     1 
ATOM   4711 O  O     . VAL A 1 600 ? 11.412  20.305  3.505   1.00 26.02  ? 600  VAL A O     1 
ATOM   4712 C  CB    . VAL A 1 600 ? 9.563   19.256  5.866   1.00 23.62  ? 600  VAL A CB    1 
ATOM   4713 C  CG1   . VAL A 1 600 ? 8.599   19.467  4.706   1.00 23.30  ? 600  VAL A CG1   1 
ATOM   4714 C  CG2   . VAL A 1 600 ? 8.988   18.156  6.804   1.00 23.33  ? 600  VAL A CG2   1 
ATOM   4715 N  N     . ASN A 1 601 ? 12.493  20.786  5.425   1.00 29.08  ? 601  ASN A N     1 
ATOM   4716 C  CA    . ASN A 1 601 ? 13.422  21.767  4.851   1.00 27.02  ? 601  ASN A CA    1 
ATOM   4717 C  C     . ASN A 1 601 ? 12.722  22.752  3.923   1.00 26.93  ? 601  ASN A C     1 
ATOM   4718 O  O     . ASN A 1 601 ? 11.829  23.479  4.358   1.00 24.48  ? 601  ASN A O     1 
ATOM   4719 C  CB    . ASN A 1 601 ? 14.552  21.040  4.112   1.00 28.96  ? 601  ASN A CB    1 
ATOM   4720 C  CG    . ASN A 1 601 ? 15.771  21.908  3.915   1.00 36.33  ? 601  ASN A CG    1 
ATOM   4721 O  OD1   . ASN A 1 601 ? 15.854  23.016  4.448   1.00 36.95  ? 601  ASN A OD1   1 
ATOM   4722 N  ND2   . ASN A 1 601 ? 16.724  21.411  3.140   1.00 30.17  ? 601  ASN A ND2   1 
ATOM   4723 N  N     . ALA A 1 602 ? 13.101  22.769  2.640   1.00 30.34  ? 602  ALA A N     1 
ATOM   4724 C  CA    . ALA A 1 602 ? 12.604  23.788  1.715   1.00 30.08  ? 602  ALA A CA    1 
ATOM   4725 C  C     . ALA A 1 602 ? 11.178  23.533  1.240   1.00 31.12  ? 602  ALA A C     1 
ATOM   4726 O  O     . ALA A 1 602 ? 10.566  24.440  0.664   1.00 29.31  ? 602  ALA A O     1 
ATOM   4727 C  CB    . ALA A 1 602 ? 13.529  23.899  0.497   1.00 33.70  ? 602  ALA A CB    1 
ATOM   4728 N  N     . ASP A 1 603 ? 10.631  22.339  1.470   1.00 28.41  ? 603  ASP A N     1 
ATOM   4729 C  CA    . ASP A 1 603 ? 9.275   22.003  1.054   1.00 27.59  ? 603  ASP A CA    1 
ATOM   4730 C  C     . ASP A 1 603 ? 8.255   22.186  2.173   1.00 26.16  ? 603  ASP A C     1 
ATOM   4731 O  O     . ASP A 1 603 ? 7.086   21.819  2.004   1.00 25.77  ? 603  ASP A O     1 
ATOM   4732 C  CB    . ASP A 1 603 ? 9.233   20.564  0.529   1.00 25.98  ? 603  ASP A CB    1 
ATOM   4733 C  CG    . ASP A 1 603 ? 9.890   20.427  -0.838  1.00 38.29  ? 603  ASP A CG    1 
ATOM   4734 O  OD1   . ASP A 1 603 ? 9.588   21.257  -1.722  1.00 37.47  ? 603  ASP A OD1   1 
ATOM   4735 O  OD2   . ASP A 1 603 ? 10.703  19.498  -1.026  1.00 36.83  ? 603  ASP A OD2   1 
ATOM   4736 N  N     . LEU A 1 604 ? 8.672   22.729  3.306   1.00 22.43  ? 604  LEU A N     1 
ATOM   4737 C  CA    . LEU A 1 604 ? 7.757   22.962  4.416   1.00 22.42  ? 604  LEU A CA    1 
ATOM   4738 C  C     . LEU A 1 604 ? 6.860   24.150  4.099   1.00 25.76  ? 604  LEU A C     1 
ATOM   4739 O  O     . LEU A 1 604 ? 7.373   25.254  3.882   1.00 24.17  ? 604  LEU A O     1 
ATOM   4740 C  CB    . LEU A 1 604 ? 8.537   23.221  5.696   1.00 24.40  ? 604  LEU A CB    1 
ATOM   4741 C  CG    . LEU A 1 604 ? 7.667   23.488  6.920   1.00 24.85  ? 604  LEU A CG    1 
ATOM   4742 C  CD1   . LEU A 1 604 ? 6.846   22.255  7.221   1.00 31.46  ? 604  LEU A CD1   1 
ATOM   4743 C  CD2   . LEU A 1 604 ? 8.535   23.861  8.105   1.00 29.72  ? 604  LEU A CD2   1 
ATOM   4744 N  N     . PRO A 1 605 ? 5.542   23.977  4.039   1.00 25.15  ? 605  PRO A N     1 
ATOM   4745 C  CA    . PRO A 1 605 ? 4.672   25.117  3.738   1.00 25.71  ? 605  PRO A CA    1 
ATOM   4746 C  C     . PRO A 1 605 ? 4.768   26.166  4.832   1.00 25.44  ? 605  PRO A C     1 
ATOM   4747 O  O     . PRO A 1 605 ? 4.949   25.850  6.010   1.00 23.30  ? 605  PRO A O     1 
ATOM   4748 C  CB    . PRO A 1 605 ? 3.276   24.489  3.671   1.00 26.75  ? 605  PRO A CB    1 
ATOM   4749 C  CG    . PRO A 1 605 ? 3.530   23.034  3.371   1.00 22.01  ? 605  PRO A CG    1 
ATOM   4750 C  CD    . PRO A 1 605 ? 4.790   22.707  4.108   1.00 25.20  ? 605  PRO A CD    1 
ATOM   4751 N  N     . TYR A 1 606 ? 4.682   27.430  4.428   1.00 22.25  ? 606  TYR A N     1 
ATOM   4752 C  CA    . TYR A 1 606 ? 4.799   28.506  5.410   1.00 24.78  ? 606  TYR A CA    1 
ATOM   4753 C  C     . TYR A 1 606 ? 3.695   28.438  6.463   1.00 21.70  ? 606  TYR A C     1 
ATOM   4754 O  O     . TYR A 1 606 ? 3.928   28.765  7.629   1.00 21.99  ? 606  TYR A O     1 
ATOM   4755 C  CB    . TYR A 1 606 ? 4.785   29.877  4.729   1.00 22.60  ? 606  TYR A CB    1 
ATOM   4756 C  CG    . TYR A 1 606 ? 4.726   30.992  5.753   1.00 24.16  ? 606  TYR A CG    1 
ATOM   4757 C  CD1   . TYR A 1 606 ? 5.821   31.268  6.568   1.00 30.56  ? 606  TYR A CD1   1 
ATOM   4758 C  CD2   . TYR A 1 606 ? 3.565   31.729  5.941   1.00 27.87  ? 606  TYR A CD2   1 
ATOM   4759 C  CE1   . TYR A 1 606 ? 5.762   32.273  7.529   1.00 36.39  ? 606  TYR A CE1   1 
ATOM   4760 C  CE2   . TYR A 1 606 ? 3.500   32.740  6.896   1.00 34.01  ? 606  TYR A CE2   1 
ATOM   4761 C  CZ    . TYR A 1 606 ? 4.598   33.003  7.685   1.00 30.71  ? 606  TYR A CZ    1 
ATOM   4762 O  OH    . TYR A 1 606 ? 4.530   34.000  8.631   1.00 44.89  ? 606  TYR A OH    1 
ATOM   4763 N  N     . GLU A 1 607 ? 2.482   28.035  6.075   1.00 22.19  ? 607  GLU A N     1 
ATOM   4764 C  CA    . GLU A 1 607 ? 1.411   27.935  7.062   1.00 24.99  ? 607  GLU A CA    1 
ATOM   4765 C  C     . GLU A 1 607 ? 1.763   26.977  8.191   1.00 23.51  ? 607  GLU A C     1 
ATOM   4766 O  O     . GLU A 1 607 ? 1.333   27.192  9.326   1.00 20.89  ? 607  GLU A O     1 
ATOM   4767 C  CB    . GLU A 1 607 ? 0.106   27.503  6.398   1.00 27.10  ? 607  GLU A CB    1 
ATOM   4768 C  CG    . GLU A 1 607 ? -0.507  28.596  5.543   1.00 35.62  ? 607  GLU A CG    1 
ATOM   4769 C  CD    . GLU A 1 607 ? -1.894  28.251  5.061   1.00 32.75  ? 607  GLU A CD    1 
ATOM   4770 O  OE1   . GLU A 1 607 ? -2.248  27.060  5.067   1.00 40.06  ? 607  GLU A OE1   1 
ATOM   4771 O  OE2   . GLU A 1 607 ? -2.642  29.175  4.694   1.00 47.64  ? 607  GLU A OE2   1 
ATOM   4772 N  N     . ILE A 1 608 ? 2.548   25.927  7.911   1.00 23.74  ? 608  ILE A N     1 
ATOM   4773 C  CA    . ILE A 1 608 ? 2.949   24.992  8.966   1.00 24.40  ? 608  ILE A CA    1 
ATOM   4774 C  C     . ILE A 1 608 ? 4.011   25.617  9.858   1.00 22.14  ? 608  ILE A C     1 
ATOM   4775 O  O     . ILE A 1 608 ? 3.979   25.465  11.087  1.00 22.93  ? 608  ILE A O     1 
ATOM   4776 C  CB    . ILE A 1 608 ? 3.441   23.661  8.362   1.00 24.85  ? 608  ILE A CB    1 
ATOM   4777 C  CG1   . ILE A 1 608 ? 2.305   22.955  7.624   1.00 22.92  ? 608  ILE A CG1   1 
ATOM   4778 C  CG2   . ILE A 1 608 ? 3.963   22.749  9.458   1.00 23.68  ? 608  ILE A CG2   1 
ATOM   4779 C  CD1   . ILE A 1 608 ? 1.227   22.392  8.580   1.00 23.41  ? 608  ILE A CD1   1 
ATOM   4780 N  N     . GLU A 1 609 ? 4.959   26.343  9.264   1.00 22.27  ? 609  GLU A N     1 
ATOM   4781 C  CA    . GLU A 1 609 ? 5.942   27.048  10.077  1.00 22.26  ? 609  GLU A CA    1 
ATOM   4782 C  C     . GLU A 1 609 ? 5.272   28.110  10.931  1.00 19.38  ? 609  GLU A C     1 
ATOM   4783 O  O     . GLU A 1 609 ? 5.674   28.338  12.076  1.00 22.98  ? 609  GLU A O     1 
ATOM   4784 C  CB    . GLU A 1 609 ? 7.024   27.692  9.198   1.00 28.82  ? 609  GLU A CB    1 
ATOM   4785 C  CG    . GLU A 1 609 ? 7.848   28.705  9.981   1.00 28.75  ? 609  GLU A CG    1 
ATOM   4786 C  CD    . GLU A 1 609 ? 8.955   29.351  9.183   1.00 35.81  ? 609  GLU A CD    1 
ATOM   4787 O  OE1   . GLU A 1 609 ? 9.260   28.876  8.069   1.00 46.33  ? 609  GLU A OE1   1 
ATOM   4788 O  OE2   . GLU A 1 609 ? 9.525   30.336  9.689   1.00 45.02  ? 609  GLU A OE2   1 
ATOM   4789 N  N     . ARG A 1 610 ? 4.248   28.774  10.386  1.00 18.84  ? 610  ARG A N     1 
ATOM   4790 C  CA    . ARG A 1 610 ? 3.527   29.783  11.150  1.00 19.62  ? 610  ARG A CA    1 
ATOM   4791 C  C     . ARG A 1 610 ? 2.847   29.174  12.368  1.00 20.91  ? 610  ARG A C     1 
ATOM   4792 O  O     . ARG A 1 610 ? 2.806   29.797  13.436  1.00 21.60  ? 610  ARG A O     1 
ATOM   4793 C  CB    . ARG A 1 610 ? 2.492   30.478  10.268  1.00 24.43  ? 610  ARG A CB    1 
ATOM   4794 C  CG    . ARG A 1 610 ? 1.615   31.466  11.041  1.00 26.95  ? 610  ARG A CG    1 
ATOM   4795 C  CD    . ARG A 1 610 ? 0.737   32.289  10.112  1.00 30.06  ? 610  ARG A CD    1 
ATOM   4796 N  NE    . ARG A 1 610 ? -0.278  31.476  9.456   1.00 28.64  ? 610  ARG A NE    1 
ATOM   4797 C  CZ    . ARG A 1 610 ? -1.006  31.894  8.431   1.00 35.59  ? 610  ARG A CZ    1 
ATOM   4798 N  NH1   . ARG A 1 610 ? -0.811  33.085  7.889   1.00 41.99  ? 610  ARG A NH1   1 
ATOM   4799 N  NH2   . ARG A 1 610 ? -1.956  31.101  7.942   1.00 33.20  ? 610  ARG A NH2   1 
ATOM   4800 N  N     . GLU A 1 611 ? 2.291   27.958  12.225  1.00 18.97  ? 611  GLU A N     1 
ATOM   4801 C  CA    . GLU A 1 611 ? 1.660   27.300  13.373  1.00 21.24  ? 611  GLU A CA    1 
ATOM   4802 C  C     . GLU A 1 611 ? 2.700   26.887  14.403  1.00 19.31  ? 611  GLU A C     1 
ATOM   4803 O  O     . GLU A 1 611 ? 2.467   26.991  15.616  1.00 19.69  ? 611  GLU A O     1 
ATOM   4804 C  CB    . GLU A 1 611 ? 0.842   26.083  12.929  1.00 19.83  ? 611  GLU A CB    1 
ATOM   4805 C  CG    . GLU A 1 611 ? -0.402  26.413  12.112  1.00 21.50  ? 611  GLU A CG    1 
ATOM   4806 C  CD    . GLU A 1 611 ? -1.341  27.379  12.822  1.00 25.19  ? 611  GLU A CD    1 
ATOM   4807 O  OE1   . GLU A 1 611 ? -1.587  27.205  14.036  1.00 22.58  ? 611  GLU A OE1   1 
ATOM   4808 O  OE2   . GLU A 1 611 ? -1.826  28.328  12.165  1.00 29.17  ? 611  GLU A OE2   1 
ATOM   4809 N  N     . LEU A 1 612 ? 3.859   26.434  13.944  1.00 20.36  ? 612  LEU A N     1 
ATOM   4810 C  CA    . LEU A 1 612 ? 4.927   26.108  14.877  1.00 18.03  ? 612  LEU A CA    1 
ATOM   4811 C  C     . LEU A 1 612 ? 5.355   27.338  15.666  1.00 23.07  ? 612  LEU A C     1 
ATOM   4812 O  O     . LEU A 1 612 ? 5.538   27.267  16.890  1.00 21.72  ? 612  LEU A O     1 
ATOM   4813 C  CB    . LEU A 1 612 ? 6.093   25.501  14.112  1.00 21.49  ? 612  LEU A CB    1 
ATOM   4814 C  CG    . LEU A 1 612 ? 7.369   25.219  14.888  1.00 25.96  ? 612  LEU A CG    1 
ATOM   4815 C  CD1   . LEU A 1 612 ? 7.081   24.263  16.017  1.00 26.85  ? 612  LEU A CD1   1 
ATOM   4816 C  CD2   . LEU A 1 612 ? 8.409   24.645  13.925  1.00 26.99  ? 612  LEU A CD2   1 
ATOM   4817 N  N     . ARG A 1 613 ? 5.494   28.488  14.982  1.00 23.29  ? 613  ARG A N     1 
ATOM   4818 C  CA    . ARG A 1 613 ? 5.822   29.733  15.668  1.00 24.03  ? 613  ARG A CA    1 
ATOM   4819 C  C     . ARG A 1 613 ? 4.732   30.126  16.645  1.00 19.27  ? 613  ARG A C     1 
ATOM   4820 O  O     . ARG A 1 613 ? 5.023   30.578  17.758  1.00 22.01  ? 613  ARG A O     1 
ATOM   4821 C  CB    . ARG A 1 613 ? 6.022   30.875  14.663  1.00 22.60  ? 613  ARG A CB    1 
ATOM   4822 C  CG    . ARG A 1 613 ? 7.216   30.740  13.756  1.00 32.62  ? 613  ARG A CG    1 
ATOM   4823 C  CD    . ARG A 1 613 ? 7.132   31.810  12.689  1.00 38.44  ? 613  ARG A CD    1 
ATOM   4824 N  NE    . ARG A 1 613 ? 8.339   31.895  11.883  1.00 37.55  ? 613  ARG A NE    1 
ATOM   4825 C  CZ    . ARG A 1 613 ? 9.086   32.986  11.777  1.00 49.34  ? 613  ARG A CZ    1 
ATOM   4826 N  NH1   . ARG A 1 613 ? 8.789   34.096  12.442  1.00 35.81  ? 613  ARG A NH1   1 
ATOM   4827 N  NH2   . ARG A 1 613 ? 10.145  32.969  10.973  1.00 48.68  ? 613  ARG A NH2   1 
ATOM   4828 N  N     . ALA A 1 614 ? 3.468   30.009  16.232  1.00 16.75  ? 614  ALA A N     1 
ATOM   4829 C  CA    . ALA A 1 614 ? 2.379   30.406  17.126  1.00 20.06  ? 614  ALA A CA    1 
ATOM   4830 C  C     . ALA A 1 614 ? 2.348   29.531  18.374  1.00 22.94  ? 614  ALA A C     1 
ATOM   4831 O  O     . ALA A 1 614 ? 2.170   30.031  19.488  1.00 21.85  ? 614  ALA A O     1 
ATOM   4832 C  CB    . ALA A 1 614 ? 1.037   30.349  16.390  1.00 18.92  ? 614  ALA A CB    1 
ATOM   4833 N  N     . LEU A 1 615 ? 2.531   28.217  18.213  1.00 21.92  ? 615  LEU A N     1 
ATOM   4834 C  CA    . LEU A 1 615 ? 2.540   27.338  19.382  1.00 19.60  ? 615  LEU A CA    1 
ATOM   4835 C  C     . LEU A 1 615 ? 3.692   27.689  20.318  1.00 22.04  ? 615  LEU A C     1 
ATOM   4836 O  O     . LEU A 1 615 ? 3.513   27.764  21.539  1.00 21.38  ? 615  LEU A O     1 
ATOM   4837 C  CB    . LEU A 1 615 ? 2.645   25.878  18.944  1.00 20.98  ? 615  LEU A CB    1 
ATOM   4838 C  CG    . LEU A 1 615 ? 2.677   24.854  20.089  1.00 22.07  ? 615  LEU A CG    1 
ATOM   4839 C  CD1   . LEU A 1 615 ? 1.460   25.019  20.993  1.00 19.66  ? 615  LEU A CD1   1 
ATOM   4840 C  CD2   . LEU A 1 615 ? 2.741   23.453  19.534  1.00 23.58  ? 615  LEU A CD2   1 
ATOM   4841 N  N     . LYS A 1 616 ? 4.880   27.921  19.753  1.00 22.47  ? 616  LYS A N     1 
ATOM   4842 C  CA    . LYS A 1 616 ? 6.025   28.334  20.560  1.00 26.82  ? 616  LYS A CA    1 
ATOM   4843 C  C     . LYS A 1 616 ? 5.708   29.587  21.371  1.00 25.08  ? 616  LYS A C     1 
ATOM   4844 O  O     . LYS A 1 616 ? 6.075   29.691  22.548  1.00 24.56  ? 616  LYS A O     1 
ATOM   4845 C  CB    . LYS A 1 616 ? 7.235   28.573  19.655  1.00 23.92  ? 616  LYS A CB    1 
ATOM   4846 C  CG    . LYS A 1 616 ? 8.513   28.837  20.414  1.00 36.34  ? 616  LYS A CG    1 
ATOM   4847 C  CD    . LYS A 1 616 ? 9.616   27.907  19.940  1.00 50.49  ? 616  LYS A CD    1 
ATOM   4848 C  CE    . LYS A 1 616 ? 10.927  28.150  20.689  1.00 57.05  ? 616  LYS A CE    1 
ATOM   4849 N  NZ    . LYS A 1 616 ? 11.959  27.119  20.345  1.00 57.66  ? 616  LYS A NZ    1 
ATOM   4850 N  N     . GLN A 1 617 ? 5.001   30.539  20.760  1.00 24.00  ? 617  GLN A N     1 
ATOM   4851 C  CA    . GLN A 1 617 ? 4.673   31.773  21.458  1.00 26.34  ? 617  GLN A CA    1 
ATOM   4852 C  C     . GLN A 1 617 ? 3.662   31.531  22.574  1.00 28.02  ? 617  GLN A C     1 
ATOM   4853 O  O     . GLN A 1 617 ? 3.821   32.058  23.680  1.00 25.64  ? 617  GLN A O     1 
ATOM   4854 C  CB    . GLN A 1 617 ? 4.151   32.810  20.459  1.00 26.90  ? 617  GLN A CB    1 
ATOM   4855 C  CG    . GLN A 1 617 ? 3.912   34.191  21.063  1.00 27.34  ? 617  GLN A CG    1 
ATOM   4856 C  CD    . GLN A 1 617 ? 5.204   34.901  21.441  1.00 30.40  ? 617  GLN A CD    1 
ATOM   4857 O  OE1   . GLN A 1 617 ? 6.280   34.559  20.953  1.00 36.58  ? 617  GLN A OE1   1 
ATOM   4858 N  NE2   . GLN A 1 617 ? 5.100   35.886  22.315  1.00 36.68  ? 617  GLN A NE2   1 
ATOM   4859 N  N     . ARG A 1 618 ? 2.609   30.750  22.304  1.00 24.91  ? 618  ARG A N     1 
ATOM   4860 C  CA    . ARG A 1 618 ? 1.615   30.467  23.339  1.00 27.47  ? 618  ARG A CA    1 
ATOM   4861 C  C     . ARG A 1 618 ? 2.228   29.735  24.525  1.00 28.13  ? 618  ARG A C     1 
ATOM   4862 O  O     . ARG A 1 618 ? 1.825   29.964  25.666  1.00 29.18  ? 618  ARG A O     1 
ATOM   4863 C  CB    . ARG A 1 618 ? 0.453   29.650  22.768  1.00 22.64  ? 618  ARG A CB    1 
ATOM   4864 C  CG    . ARG A 1 618 ? -0.444  30.426  21.805  1.00 26.13  ? 618  ARG A CG    1 
ATOM   4865 C  CD    . ARG A 1 618 ? -1.681  29.621  21.415  1.00 23.92  ? 618  ARG A CD    1 
ATOM   4866 N  NE    . ARG A 1 618 ? -1.376  28.300  20.860  1.00 27.48  ? 618  ARG A NE    1 
ATOM   4867 C  CZ    . ARG A 1 618 ? -1.247  28.029  19.566  1.00 28.05  ? 618  ARG A CZ    1 
ATOM   4868 N  NH1   . ARG A 1 618 ? -1.289  28.989  18.650  1.00 22.48  ? 618  ARG A NH1   1 
ATOM   4869 N  NH2   . ARG A 1 618 ? -1.085  26.759  19.177  1.00 21.82  ? 618  ARG A NH2   1 
ATOM   4870 N  N     . ILE A 1 619 ? 3.215   28.873  24.280  1.00 26.98  ? 619  ILE A N     1 
ATOM   4871 C  CA    . ILE A 1 619 ? 3.849   28.136  25.370  1.00 30.30  ? 619  ILE A CA    1 
ATOM   4872 C  C     . ILE A 1 619 ? 4.772   29.045  26.172  1.00 30.24  ? 619  ILE A C     1 
ATOM   4873 O  O     . ILE A 1 619 ? 4.821   28.970  27.403  1.00 29.53  ? 619  ILE A O     1 
ATOM   4874 C  CB    . ILE A 1 619 ? 4.605   26.916  24.812  1.00 29.51  ? 619  ILE A CB    1 
ATOM   4875 C  CG1   . ILE A 1 619 ? 3.608   25.844  24.371  1.00 31.65  ? 619  ILE A CG1   1 
ATOM   4876 C  CG2   . ILE A 1 619 ? 5.593   26.365  25.845  1.00 31.05  ? 619  ILE A CG2   1 
ATOM   4877 C  CD1   . ILE A 1 619 ? 4.241   24.730  23.600  1.00 39.72  ? 619  ILE A CD1   1 
ATOM   4878 N  N     . SER A 1 620 ? 5.523   29.910  25.487  1.00 29.57  ? 620  SER A N     1 
ATOM   4879 C  CA    . SER A 1 620 ? 6.414   30.835  26.181  1.00 30.78  ? 620  SER A CA    1 
ATOM   4880 C  C     . SER A 1 620 ? 5.653   31.750  27.137  1.00 34.73  ? 620  SER A C     1 
ATOM   4881 O  O     . SER A 1 620 ? 6.189   32.146  28.181  1.00 37.21  ? 620  SER A O     1 
ATOM   4882 C  CB    . SER A 1 620 ? 7.179   31.668  25.158  1.00 31.91  ? 620  SER A CB    1 
ATOM   4883 O  OG    . SER A 1 620 ? 6.302   32.616  24.569  1.00 38.22  ? 620  SER A OG    1 
ATOM   4884 N  N     . GLN A 1 621 ? 4.410   32.092  26.804  1.00 27.27  ? 621  GLN A N     1 
ATOM   4885 C  CA    . GLN A 1 621 ? 3.591   32.965  27.634  1.00 33.87  ? 621  GLN A CA    1 
ATOM   4886 C  C     . GLN A 1 621 ? 2.932   32.249  28.806  1.00 38.07  ? 621  GLN A C     1 
ATOM   4887 O  O     . GLN A 1 621 ? 2.197   32.892  29.560  1.00 40.89  ? 621  GLN A O     1 
ATOM   4888 C  CB    . GLN A 1 621 ? 2.517   33.636  26.777  1.00 34.83  ? 621  GLN A CB    1 
ATOM   4889 C  CG    . GLN A 1 621 ? 3.105   34.510  25.683  1.00 33.37  ? 621  GLN A CG    1 
ATOM   4890 C  CD    . GLN A 1 621 ? 3.919   35.652  26.250  1.00 38.96  ? 621  GLN A CD    1 
ATOM   4891 O  OE1   . GLN A 1 621 ? 3.454   36.386  27.122  1.00 42.52  ? 621  GLN A OE1   1 
ATOM   4892 N  NE2   . GLN A 1 621 ? 5.145   35.801  25.769  1.00 40.73  ? 621  GLN A NE2   1 
ATOM   4893 N  N     . MET A 1 622 ? 3.164   30.948  28.974  1.00 37.48  ? 622  MET A N     1 
ATOM   4894 C  CA    . MET A 1 622 ? 2.663   30.204  30.132  1.00 37.20  ? 622  MET A CA    1 
ATOM   4895 C  C     . MET A 1 622 ? 3.417   30.554  31.401  1.00 40.40  ? 622  MET A C     1 
ATOM   4896 O  O     . MET A 1 622 ? 4.571   30.979  31.351  1.00 45.83  ? 622  MET A O     1 
ATOM   4897 C  CB    . MET A 1 622 ? 2.785   28.695  29.916  1.00 36.40  ? 622  MET A CB    1 
ATOM   4898 C  CG    . MET A 1 622 ? 1.871   28.109  28.879  1.00 35.97  ? 622  MET A CG    1 
ATOM   4899 S  SD    . MET A 1 622 ? 2.223   26.347  28.744  1.00 38.08  ? 622  MET A SD    1 
ATOM   4900 C  CE    . MET A 1 622 ? 1.460   25.704  30.241  1.00 35.89  ? 622  MET A CE    1 
ATOM   4901 O  OXT   . MET A 1 622 ? 2.903   30.369  32.501  1.00 49.12  ? 622  MET A OXT   1 
HETATM 4902 MN MN    . MN  B 2 .   ? -2.299  -0.215  9.341   1.00 18.55  ? 701  MN  A MN    1 
HETATM 4903 MN MN    . MN  C 2 .   ? -5.631  -2.728  12.715  1.00 20.46  ? 702  MN  A MN    1 
HETATM 4904 MN MN    . MN  D 2 .   ? 3.597   -31.487 -2.772  1.00 49.14  ? 703  MN  A MN    1 
HETATM 4905 C  C1    . SPV E 3 .   ? 0.246   -1.757  9.614   1.00 23.30  ? 704  SPV A C1    1 
HETATM 4906 O  O1    . SPV E 3 .   ? -0.262  -0.642  9.812   1.00 21.42  ? 704  SPV A O1    1 
HETATM 4907 O  "O2'" . SPV E 3 .   ? 1.439   -2.074  9.711   1.00 25.60  ? 704  SPV A "O2'" 1 
HETATM 4908 C  C2    . SPV E 3 .   ? -0.797  -2.880  9.239   1.00 22.81  ? 704  SPV A C2    1 
HETATM 4909 C  C3    . SPV E 3 .   ? -0.264  -4.276  9.018   1.00 18.73  ? 704  SPV A C3    1 
HETATM 4910 O  O2    . SPV E 3 .   ? -1.977  -2.611  9.136   1.00 17.28  ? 704  SPV A O2    1 
HETATM 4911 S  S     . SPV E 3 .   ? 0.432   -4.572  7.389   1.00 22.46  ? 704  SPV A S     1 
HETATM 4912 O  O1S   . SPV E 3 .   ? 1.148   -5.860  7.494   1.00 20.05  ? 704  SPV A O1S   1 
HETATM 4913 O  O2S   . SPV E 3 .   ? 1.314   -3.412  7.170   1.00 23.63  ? 704  SPV A O2S   1 
HETATM 4914 O  O3S   . SPV E 3 .   ? -0.750  -4.595  6.502   1.00 23.56  ? 704  SPV A O3S   1 
HETATM 4915 P  PG    A GTP F 4 .   ? -2.644  -1.676  12.259  0.60 20.01  ? 705  GTP A PG    1 
HETATM 4916 P  PG    B GTP F 4 .   ? -2.453  -1.959  12.619  0.40 20.41  ? 705  GTP A PG    1 
HETATM 4917 O  O1G   A GTP F 4 .   ? -2.680  -0.457  11.354  0.60 21.08  ? 705  GTP A O1G   1 
HETATM 4918 O  O1G   B GTP F 4 .   ? -3.456  -3.095  12.612  0.40 23.06  ? 705  GTP A O1G   1 
HETATM 4919 O  O2G   A GTP F 4 .   ? -1.289  -2.355  12.232  0.60 18.82  ? 705  GTP A O2G   1 
HETATM 4920 O  O2G   B GTP F 4 .   ? -2.798  -0.953  11.540  0.40 20.82  ? 705  GTP A O2G   1 
HETATM 4921 O  O3G   A GTP F 4 .   ? -3.689  -2.669  11.799  0.60 22.24  ? 705  GTP A O3G   1 
HETATM 4922 O  O3G   B GTP F 4 .   ? -1.067  -2.516  12.394  0.40 17.96  ? 705  GTP A O3G   1 
HETATM 4923 O  O3B   A GTP F 4 .   ? -2.800  -1.199  13.799  0.60 20.28  ? 705  GTP A O3B   1 
HETATM 4924 O  O3B   B GTP F 4 .   ? -2.437  -1.228  14.061  0.40 20.41  ? 705  GTP A O3B   1 
HETATM 4925 P  PB    A GTP F 4 .   ? -4.128  -0.680  14.555  0.60 20.53  ? 705  GTP A PB    1 
HETATM 4926 P  PB    B GTP F 4 .   ? -3.733  -0.910  14.973  0.40 19.58  ? 705  GTP A PB    1 
HETATM 4927 O  O1B   A GTP F 4 .   ? -4.038  0.833   14.655  0.60 21.60  ? 705  GTP A O1B   1 
HETATM 4928 O  O1B   B GTP F 4 .   ? -3.945  0.591   14.949  0.40 21.35  ? 705  GTP A O1B   1 
HETATM 4929 O  O2B   A GTP F 4 .   ? -5.422  -1.084  13.904  0.60 21.59  ? 705  GTP A O2B   1 
HETATM 4930 O  O2B   B GTP F 4 .   ? -4.997  -1.589  14.520  0.40 21.33  ? 705  GTP A O2B   1 
HETATM 4931 O  O3A   A GTP F 4 .   ? -3.882  -1.245  16.044  0.60 21.33  ? 705  GTP A O3A   1 
HETATM 4932 O  O3A   B GTP F 4 .   ? -3.334  -1.301  16.483  0.40 21.99  ? 705  GTP A O3A   1 
HETATM 4933 P  PA    A GTP F 4 .   ? -4.888  -2.154  16.939  0.60 19.12  ? 705  GTP A PA    1 
HETATM 4934 P  PA    B GTP F 4 .   ? -3.216  -2.767  17.158  0.40 22.91  ? 705  GTP A PA    1 
HETATM 4935 O  O1A   A GTP F 4 .   ? -6.298  -1.637  16.941  0.60 20.86  ? 705  GTP A O1A   1 
HETATM 4936 O  O1A   B GTP F 4 .   ? -4.340  -3.685  16.746  0.40 22.79  ? 705  GTP A O1A   1 
HETATM 4937 O  O2A   A GTP F 4 .   ? -4.769  -3.592  16.479  0.60 24.62  ? 705  GTP A O2A   1 
HETATM 4938 O  O2A   B GTP F 4 .   ? -1.900  -3.437  16.929  0.40 23.08  ? 705  GTP A O2A   1 
HETATM 4939 O  "O5'" A GTP F 4 .   ? -4.275  -2.002  18.412  0.60 19.95  ? 705  GTP A "O5'" 1 
HETATM 4940 O  "O5'" B GTP F 4 .   ? -3.271  -2.360  18.711  0.40 23.95  ? 705  GTP A "O5'" 1 
HETATM 4941 C  "C5'" A GTP F 4 .   ? -2.981  -2.467  18.730  0.60 24.09  ? 705  GTP A "C5'" 1 
HETATM 4942 C  "C5'" B GTP F 4 .   ? -3.171  -3.321  19.730  0.40 24.59  ? 705  GTP A "C5'" 1 
HETATM 4943 C  "C4'" A GTP F 4 .   ? -2.847  -2.670  20.238  0.60 23.91  ? 705  GTP A "C4'" 1 
HETATM 4944 C  "C4'" B GTP F 4 .   ? -2.630  -2.647  20.987  0.40 25.44  ? 705  GTP A "C4'" 1 
HETATM 4945 O  "O4'" A GTP F 4 .   ? -3.213  -1.469  20.884  0.60 24.77  ? 705  GTP A "O4'" 1 
HETATM 4946 O  "O4'" B GTP F 4 .   ? -3.306  -1.429  21.241  0.40 25.10  ? 705  GTP A "O4'" 1 
HETATM 4947 C  "C3'" A GTP F 4 .   ? -3.759  -3.754  20.798  0.60 27.71  ? 705  GTP A "C3'" 1 
HETATM 4948 C  "C3'" B GTP F 4 .   ? -2.817  -3.515  22.216  0.40 24.35  ? 705  GTP A "C3'" 1 
HETATM 4949 O  "O3'" A GTP F 4 .   ? -3.044  -4.921  21.165  0.60 30.49  ? 705  GTP A "O3'" 1 
HETATM 4950 O  "O3'" B GTP F 4 .   ? -1.565  -3.728  22.810  0.40 28.66  ? 705  GTP A "O3'" 1 
HETATM 4951 C  "C2'" A GTP F 4 .   ? -4.433  -3.146  22.014  0.60 26.81  ? 705  GTP A "C2'" 1 
HETATM 4952 C  "C2'" B GTP F 4 .   ? -3.654  -2.690  23.166  0.40 27.04  ? 705  GTP A "C2'" 1 
HETATM 4953 O  "O2'" A GTP F 4 .   ? -4.209  -3.887  23.198  0.60 33.87  ? 705  GTP A "O2'" 1 
HETATM 4954 O  "O2'" B GTP F 4 .   ? -3.163  -2.820  24.479  0.40 27.88  ? 705  GTP A "O2'" 1 
HETATM 4955 C  "C1'" A GTP F 4 .   ? -3.850  -1.746  22.114  0.60 26.50  ? 705  GTP A "C1'" 1 
HETATM 4956 C  "C1'" B GTP F 4 .   ? -3.504  -1.272  22.636  0.40 24.95  ? 705  GTP A "C1'" 1 
HETATM 4957 N  N9    A GTP F 4 .   ? -4.959  -0.811  22.331  0.60 23.89  ? 705  GTP A N9    1 
HETATM 4958 N  N9    B GTP F 4 .   ? -4.702  -0.450  22.891  0.40 21.81  ? 705  GTP A N9    1 
HETATM 4959 C  C8    A GTP F 4 .   ? -6.001  -0.539  21.481  0.60 24.41  ? 705  GTP A C8    1 
HETATM 4960 C  C8    B GTP F 4 .   ? -5.761  -0.258  22.043  0.40 23.58  ? 705  GTP A C8    1 
HETATM 4961 N  N7    A GTP F 4 .   ? -6.803  0.372   22.075  0.60 21.98  ? 705  GTP A N7    1 
HETATM 4962 N  N7    B GTP F 4 .   ? -6.644  0.582   22.631  0.40 23.11  ? 705  GTP A N7    1 
HETATM 4963 C  C5    A GTP F 4 .   ? -6.273  0.678   23.282  0.60 22.98  ? 705  GTP A C5    1 
HETATM 4964 C  C5    B GTP F 4 .   ? -6.154  0.947   23.838  0.40 22.11  ? 705  GTP A C5    1 
HETATM 4965 C  C6    A GTP F 4 .   ? -6.669  1.540   24.290  0.60 22.21  ? 705  GTP A C6    1 
HETATM 4966 C  C6    B GTP F 4 .   ? -6.638  1.785   24.837  0.40 23.58  ? 705  GTP A C6    1 
HETATM 4967 O  O6    A GTP F 4 .   ? -7.698  2.207   24.161  0.60 23.38  ? 705  GTP A O6    1 
HETATM 4968 O  O6    B GTP F 4 .   ? -7.721  2.361   24.707  0.40 22.64  ? 705  GTP A O6    1 
HETATM 4969 N  N1    A GTP F 4 .   ? -5.896  1.638   25.430  0.60 23.76  ? 705  GTP A N1    1 
HETATM 4970 N  N1    B GTP F 4 .   ? -5.895  1.968   25.985  0.40 24.28  ? 705  GTP A N1    1 
HETATM 4971 C  C2    A GTP F 4 .   ? -4.752  0.878   25.573  0.60 23.20  ? 705  GTP A C2    1 
HETATM 4972 C  C2    B GTP F 4 .   ? -4.683  1.323   26.131  0.40 24.93  ? 705  GTP A C2    1 
HETATM 4973 N  N2    A GTP F 4 .   ? -4.005  0.974   26.669  0.60 26.52  ? 705  GTP A N2    1 
HETATM 4974 N  N2    B GTP F 4 .   ? -3.968  1.505   27.236  0.40 25.70  ? 705  GTP A N2    1 
HETATM 4975 N  N3    A GTP F 4 .   ? -4.362  0.028   24.569  0.60 22.97  ? 705  GTP A N3    1 
HETATM 4976 N  N3    B GTP F 4 .   ? -4.209  0.492   25.138  0.40 23.43  ? 705  GTP A N3    1 
HETATM 4977 C  C4    A GTP F 4 .   ? -5.112  -0.062  23.450  0.60 22.39  ? 705  GTP A C4    1 
HETATM 4978 C  C4    B GTP F 4 .   ? -4.930  0.310   24.007  0.40 23.45  ? 705  GTP A C4    1 
HETATM 4979 O  O     . HOH G 5 .   ? 9.648   9.778   -12.005 1.00 53.73  ? 801  HOH A O     1 
HETATM 4980 O  O     . HOH G 5 .   ? 16.608  -23.899 -7.024  1.00 55.96  ? 802  HOH A O     1 
HETATM 4981 O  O     . HOH G 5 .   ? 16.723  14.633  11.590  1.00 33.00  ? 803  HOH A O     1 
HETATM 4982 O  O     . HOH G 5 .   ? -10.554 -30.570 28.719  1.00 32.27  ? 804  HOH A O     1 
HETATM 4983 O  O     . HOH G 5 .   ? -5.101  -29.748 9.141   1.00 38.79  ? 805  HOH A O     1 
HETATM 4984 O  O     . HOH G 5 .   ? 7.496   6.639   3.800   1.00 29.10  ? 806  HOH A O     1 
HETATM 4985 O  O     . HOH G 5 .   ? -5.871  3.359   27.928  1.00 28.35  ? 807  HOH A O     1 
HETATM 4986 O  O     . HOH G 5 .   ? 1.101   11.315  33.167  1.00 48.96  ? 808  HOH A O     1 
HETATM 4987 O  O     . HOH G 5 .   ? -4.793  -28.748 17.382  1.00 42.19  ? 809  HOH A O     1 
HETATM 4988 O  O     . HOH G 5 .   ? 20.798  15.132  4.080   1.00 40.02  ? 810  HOH A O     1 
HETATM 4989 O  O     . HOH G 5 .   ? -4.805  -6.375  19.788  1.00 31.34  ? 811  HOH A O     1 
HETATM 4990 O  O     . HOH G 5 .   ? -1.014  -6.290  20.836  1.00 38.07  ? 812  HOH A O     1 
HETATM 4991 O  O     . HOH G 5 .   ? -27.635 4.982   19.827  1.00 38.70  ? 813  HOH A O     1 
HETATM 4992 O  O     . HOH G 5 .   ? -9.744  20.489  32.917  1.00 62.58  ? 814  HOH A O     1 
HETATM 4993 O  O     . HOH G 5 .   ? 9.582   10.445  10.669  1.00 32.75  ? 815  HOH A O     1 
HETATM 4994 O  O     . HOH G 5 .   ? -5.843  -1.216  11.447  1.00 23.31  ? 816  HOH A O     1 
HETATM 4995 O  O     . HOH G 5 .   ? 5.909   34.524  10.648  1.00 46.51  ? 817  HOH A O     1 
HETATM 4996 O  O     . HOH G 5 .   ? 1.391   -22.571 -25.043 1.00 33.60  ? 818  HOH A O     1 
HETATM 4997 O  O     . HOH G 5 .   ? 8.026   5.877   -10.867 1.00 40.01  ? 819  HOH A O     1 
HETATM 4998 O  O     . HOH G 5 .   ? -1.187  10.500  21.566  1.00 20.16  ? 820  HOH A O     1 
HETATM 4999 O  O     . HOH G 5 .   ? 6.402   9.739   -5.804  1.00 28.62  ? 821  HOH A O     1 
HETATM 5000 O  O     . HOH G 5 .   ? 13.212  19.304  -1.230  1.00 36.64  ? 822  HOH A O     1 
HETATM 5001 O  O     . HOH G 5 .   ? -4.277  8.910   28.390  1.00 25.12  ? 823  HOH A O     1 
HETATM 5002 O  O     . HOH G 5 .   ? -11.815 23.699  16.381  1.00 30.91  ? 824  HOH A O     1 
HETATM 5003 O  O     . HOH G 5 .   ? 15.249  -20.213 -11.747 1.00 42.89  ? 825  HOH A O     1 
HETATM 5004 O  O     . HOH G 5 .   ? -10.962 -14.994 -13.583 1.00 33.59  ? 826  HOH A O     1 
HETATM 5005 O  O     . HOH G 5 .   ? -5.286  -4.199  14.063  1.00 21.11  ? 827  HOH A O     1 
HETATM 5006 O  O     . HOH G 5 .   ? -15.600 -4.526  20.227  1.00 26.38  ? 828  HOH A O     1 
HETATM 5007 O  O     . HOH G 5 .   ? -21.077 -2.957  20.388  1.00 33.82  ? 829  HOH A O     1 
HETATM 5008 O  O     . HOH G 5 .   ? 20.970  7.430   3.215   1.00 40.14  ? 830  HOH A O     1 
HETATM 5009 O  O     . HOH G 5 .   ? -0.924  28.900  9.838   1.00 26.02  ? 831  HOH A O     1 
HETATM 5010 O  O     . HOH G 5 .   ? 1.735   -32.761 -1.199  1.00 46.84  ? 832  HOH A O     1 
HETATM 5011 O  O     . HOH G 5 .   ? -6.464  -4.045  10.953  1.00 24.34  ? 833  HOH A O     1 
HETATM 5012 O  O     . HOH G 5 .   ? 3.007   -4.087  10.807  1.00 40.98  ? 834  HOH A O     1 
HETATM 5013 O  O     . HOH G 5 .   ? -16.784 2.287   2.417   1.00 24.43  ? 835  HOH A O     1 
HETATM 5014 O  O     . HOH G 5 .   ? -1.421  -29.030 7.065   1.00 39.01  ? 836  HOH A O     1 
HETATM 5015 O  O     . HOH G 5 .   ? -11.746 -4.271  -1.754  1.00 24.79  ? 837  HOH A O     1 
HETATM 5016 O  O     . HOH G 5 .   ? -11.314 -13.335 25.191  1.00 33.39  ? 838  HOH A O     1 
HETATM 5017 O  O     . HOH G 5 .   ? -9.625  -0.577  6.032   1.00 15.57  ? 839  HOH A O     1 
HETATM 5018 O  O     . HOH G 5 .   ? 0.524   15.875  17.187  1.00 21.92  ? 840  HOH A O     1 
HETATM 5019 O  O     . HOH G 5 .   ? 4.613   -31.044 -14.300 1.00 35.72  ? 841  HOH A O     1 
HETATM 5020 O  O     . HOH G 5 .   ? 11.717  -20.484 5.313   1.00 32.24  ? 842  HOH A O     1 
HETATM 5021 O  O     . HOH G 5 .   ? -19.041 3.762   1.987   1.00 32.83  ? 843  HOH A O     1 
HETATM 5022 O  O     . HOH G 5 .   ? -21.247 12.253  9.549   1.00 23.64  ? 844  HOH A O     1 
HETATM 5023 O  O     . HOH G 5 .   ? 8.925   -23.991 -14.296 1.00 31.75  ? 845  HOH A O     1 
HETATM 5024 O  O     . HOH G 5 .   ? -23.004 -1.083  2.570   1.00 39.73  ? 846  HOH A O     1 
HETATM 5025 O  O     . HOH G 5 .   ? -17.011 -2.305  26.159  1.00 37.98  ? 847  HOH A O     1 
HETATM 5026 O  O     . HOH G 5 .   ? 7.562   -7.468  14.526  1.00 48.65  ? 848  HOH A O     1 
HETATM 5027 O  O     . HOH G 5 .   ? -1.516  -32.098 -3.131  1.00 42.02  ? 849  HOH A O     1 
HETATM 5028 O  O     . HOH G 5 .   ? -3.316  11.076  1.084   1.00 21.01  ? 850  HOH A O     1 
HETATM 5029 O  O     . HOH G 5 .   ? 8.845   16.436  24.806  1.00 33.03  ? 851  HOH A O     1 
HETATM 5030 O  O     . HOH G 5 .   ? -23.775 4.205   14.750  1.00 22.51  ? 852  HOH A O     1 
HETATM 5031 O  O     . HOH G 5 .   ? -24.816 10.308  27.124  1.00 36.30  ? 853  HOH A O     1 
HETATM 5032 O  O     . HOH G 5 .   ? 13.170  14.219  3.883   1.00 26.87  ? 854  HOH A O     1 
HETATM 5033 O  O     . HOH G 5 .   ? 20.798  11.152  9.294   1.00 32.44  ? 855  HOH A O     1 
HETATM 5034 O  O     . HOH G 5 .   ? 2.492   13.696  20.322  1.00 23.81  ? 856  HOH A O     1 
HETATM 5035 O  O     . HOH G 5 .   ? -14.294 -2.793  25.672  1.00 35.54  ? 857  HOH A O     1 
HETATM 5036 O  O     . HOH G 5 .   ? -16.177 26.131  24.546  1.00 29.36  ? 858  HOH A O     1 
HETATM 5037 O  O     . HOH G 5 .   ? -7.782  -4.053  7.717   1.00 17.62  ? 859  HOH A O     1 
HETATM 5038 O  O     . HOH G 5 .   ? 6.715   -2.971  3.177   1.00 28.47  ? 860  HOH A O     1 
HETATM 5039 O  O     . HOH G 5 .   ? -0.485  31.175  26.237  1.00 35.15  ? 861  HOH A O     1 
HETATM 5040 O  O     . HOH G 5 .   ? -6.489  -4.251  -22.102 1.00 41.50  ? 862  HOH A O     1 
HETATM 5041 O  O     . HOH G 5 .   ? 0.899   -12.157 6.764   1.00 22.30  ? 863  HOH A O     1 
HETATM 5042 O  O     . HOH G 5 .   ? -12.029 -24.787 10.880  1.00 27.05  ? 864  HOH A O     1 
HETATM 5043 O  O     . HOH G 5 .   ? 7.784   1.868   4.475   1.00 26.11  ? 865  HOH A O     1 
HETATM 5044 O  O     . HOH G 5 .   ? 17.366  -7.257  -0.368  1.00 41.77  ? 866  HOH A O     1 
HETATM 5045 O  O     . HOH G 5 .   ? -0.416  26.719  16.408  1.00 30.01  ? 867  HOH A O     1 
HETATM 5046 O  O     . HOH G 5 .   ? -16.165 -18.217 1.908   1.00 50.74  ? 868  HOH A O     1 
HETATM 5047 O  O     . HOH G 5 .   ? 6.155   14.357  13.803  1.00 17.46  ? 869  HOH A O     1 
HETATM 5048 O  O     . HOH G 5 .   ? 10.689  -13.478 14.880  1.00 43.14  ? 870  HOH A O     1 
HETATM 5049 O  O     . HOH G 5 .   ? 8.298   -9.050  -0.410  1.00 29.01  ? 871  HOH A O     1 
HETATM 5050 O  O     . HOH G 5 .   ? 12.932  -28.847 -3.765  1.00 53.47  ? 872  HOH A O     1 
HETATM 5051 O  O     . HOH G 5 .   ? 10.529  -0.359  -19.875 1.00 51.41  ? 873  HOH A O     1 
HETATM 5052 O  O     . HOH G 5 .   ? -18.987 18.226  23.980  1.00 20.33  ? 874  HOH A O     1 
HETATM 5053 O  O     . HOH G 5 .   ? -18.287 12.441  27.749  1.00 30.59  ? 875  HOH A O     1 
HETATM 5054 O  O     . HOH G 5 .   ? -11.461 -17.951 -4.762  1.00 22.02  ? 876  HOH A O     1 
HETATM 5055 O  O     . HOH G 5 .   ? 3.015   -5.902  9.462   1.00 26.37  ? 877  HOH A O     1 
HETATM 5056 O  O     . HOH G 5 .   ? 0.636   -3.963  0.753   1.00 17.56  ? 878  HOH A O     1 
HETATM 5057 O  O     . HOH G 5 .   ? -3.786  6.147   29.717  1.00 29.08  ? 879  HOH A O     1 
HETATM 5058 O  O     . HOH G 5 .   ? 3.907   16.090  19.274  1.00 21.42  ? 880  HOH A O     1 
HETATM 5059 O  O     . HOH G 5 .   ? 5.123   -30.018 -3.561  1.00 44.48  ? 881  HOH A O     1 
HETATM 5060 O  O     . HOH G 5 .   ? -25.672 14.433  13.103  1.00 40.06  ? 882  HOH A O     1 
HETATM 5061 O  O     . HOH G 5 .   ? -17.633 4.703   -10.943 1.00 78.67  ? 883  HOH A O     1 
HETATM 5062 O  O     . HOH G 5 .   ? 2.170   18.371  29.849  1.00 31.74  ? 884  HOH A O     1 
HETATM 5063 O  O     . HOH G 5 .   ? -12.076 -22.902 28.363  1.00 50.03  ? 885  HOH A O     1 
HETATM 5064 O  O     . HOH G 5 .   ? -17.490 19.029  11.467  1.00 28.94  ? 886  HOH A O     1 
HETATM 5065 O  O     . HOH G 5 .   ? -4.259  14.423  22.746  1.00 19.57  ? 887  HOH A O     1 
HETATM 5066 O  O     . HOH G 5 .   ? -4.225  5.860   19.496  1.00 26.60  ? 888  HOH A O     1 
HETATM 5067 O  O     . HOH G 5 .   ? -14.883 -2.145  22.959  1.00 28.22  ? 889  HOH A O     1 
HETATM 5068 O  O     . HOH G 5 .   ? -3.869  -14.086 8.680   1.00 21.54  ? 890  HOH A O     1 
HETATM 5069 O  O     . HOH G 5 .   ? -2.492  19.410  -4.326  1.00 42.04  ? 891  HOH A O     1 
HETATM 5070 O  O     . HOH G 5 .   ? -16.031 -1.102  1.076   1.00 34.02  ? 892  HOH A O     1 
HETATM 5071 O  O     . HOH G 5 .   ? -17.822 2.144   32.927  1.00 44.47  ? 893  HOH A O     1 
HETATM 5072 O  O     . HOH G 5 .   ? -17.521 -21.019 14.744  1.00 40.63  ? 894  HOH A O     1 
HETATM 5073 O  O     . HOH G 5 .   ? -4.789  26.564  3.960   1.00 35.98  ? 895  HOH A O     1 
HETATM 5074 O  O     . HOH G 5 .   ? -2.423  28.968  15.989  1.00 35.81  ? 896  HOH A O     1 
HETATM 5075 O  O     . HOH G 5 .   ? -9.345  -16.352 -18.027 1.00 48.28  ? 897  HOH A O     1 
HETATM 5076 O  O     . HOH G 5 .   ? 9.502   -18.772 -5.783  1.00 26.73  ? 898  HOH A O     1 
HETATM 5077 O  O     . HOH G 5 .   ? -8.276  2.406   20.463  1.00 24.22  ? 899  HOH A O     1 
HETATM 5078 O  O     . HOH G 5 .   ? -6.895  -6.132  16.088  1.00 24.91  ? 900  HOH A O     1 
HETATM 5079 O  O     . HOH G 5 .   ? 1.059   12.181  18.751  1.00 22.17  ? 901  HOH A O     1 
HETATM 5080 O  O     . HOH G 5 .   ? 18.532  4.459   8.662   1.00 41.57  ? 902  HOH A O     1 
HETATM 5081 O  O     . HOH G 5 .   ? -20.561 18.940  10.820  1.00 42.18  ? 903  HOH A O     1 
HETATM 5082 O  O     . HOH G 5 .   ? -14.215 -13.752 -4.464  1.00 29.71  ? 904  HOH A O     1 
HETATM 5083 O  O     . HOH G 5 .   ? -10.406 -17.854 -14.347 1.00 32.35  ? 905  HOH A O     1 
HETATM 5084 O  O     . HOH G 5 .   ? 5.466   22.360  -0.305  1.00 38.41  ? 906  HOH A O     1 
HETATM 5085 O  O     . HOH G 5 .   ? -20.726 -0.822  18.866  1.00 33.21  ? 907  HOH A O     1 
HETATM 5086 O  O     . HOH G 5 .   ? 5.398   5.142   14.515  1.00 36.80  ? 908  HOH A O     1 
HETATM 5087 O  O     . HOH G 5 .   ? -15.078 -26.094 9.195   1.00 35.20  ? 909  HOH A O     1 
HETATM 5088 O  O     . HOH G 5 .   ? -3.483  9.173   7.534   1.00 19.27  ? 910  HOH A O     1 
HETATM 5089 O  O     . HOH G 5 .   ? 2.201   4.270   10.973  1.00 27.66  ? 911  HOH A O     1 
HETATM 5090 O  O     . HOH G 5 .   ? 0.049   20.143  19.283  1.00 33.66  ? 912  HOH A O     1 
HETATM 5091 O  O     . HOH G 5 .   ? 5.408   11.151  25.725  1.00 27.46  ? 913  HOH A O     1 
HETATM 5092 O  O     . HOH G 5 .   ? 2.104   -12.094 21.769  1.00 32.89  ? 914  HOH A O     1 
HETATM 5093 O  O     . HOH G 5 .   ? -24.522 -2.313  12.007  1.00 29.72  ? 915  HOH A O     1 
HETATM 5094 O  O     . HOH G 5 .   ? -7.230  -28.163 14.884  1.00 39.98  ? 916  HOH A O     1 
HETATM 5095 O  O     . HOH G 5 .   ? 24.585  16.935  6.175   1.00 33.78  ? 917  HOH A O     1 
HETATM 5096 O  O     . HOH G 5 .   ? -10.998 2.212   21.672  1.00 28.66  ? 918  HOH A O     1 
HETATM 5097 O  O     . HOH G 5 .   ? 0.188   16.363  20.744  1.00 23.48  ? 919  HOH A O     1 
HETATM 5098 O  O     . HOH G 5 .   ? 3.816   2.308   15.050  1.00 34.42  ? 920  HOH A O     1 
HETATM 5099 O  O     . HOH G 5 .   ? -2.214  12.472  -1.046  1.00 21.09  ? 921  HOH A O     1 
HETATM 5100 O  O     . HOH G 5 .   ? -24.171 1.327   24.467  1.00 35.65  ? 922  HOH A O     1 
HETATM 5101 O  O     . HOH G 5 .   ? -33.321 9.642   14.287  1.00 26.52  ? 923  HOH A O     1 
HETATM 5102 O  O     . HOH G 5 .   ? -3.693  -13.592 5.993   1.00 26.44  ? 924  HOH A O     1 
HETATM 5103 O  O     . HOH G 5 .   ? -3.801  7.494   21.711  1.00 21.57  ? 925  HOH A O     1 
HETATM 5104 O  O     . HOH G 5 .   ? 6.619   5.053   1.863   1.00 30.03  ? 926  HOH A O     1 
HETATM 5105 O  O     . HOH G 5 .   ? 17.114  13.212  -7.908  1.00 46.36  ? 927  HOH A O     1 
HETATM 5106 O  O     . HOH G 5 .   ? 14.291  20.734  0.917   1.00 35.93  ? 928  HOH A O     1 
HETATM 5107 O  O     . HOH G 5 .   ? 4.135   6.311   -4.829  1.00 34.95  ? 929  HOH A O     1 
HETATM 5108 O  O     . HOH G 5 .   ? 16.639  11.991  11.755  1.00 32.44  ? 930  HOH A O     1 
HETATM 5109 O  O     . HOH G 5 .   ? 7.777   11.800  1.628   1.00 25.01  ? 931  HOH A O     1 
HETATM 5110 O  O     . HOH G 5 .   ? -26.710 16.951  14.807  1.00 32.84  ? 932  HOH A O     1 
HETATM 5111 O  O     . HOH G 5 .   ? -7.191  -3.765  -19.578 1.00 39.30  ? 933  HOH A O     1 
HETATM 5112 O  O     . HOH G 5 .   ? 9.713   -9.722  8.839   1.00 36.22  ? 934  HOH A O     1 
HETATM 5113 O  O     . HOH G 5 .   ? 3.155   -23.268 8.351   1.00 43.85  ? 935  HOH A O     1 
HETATM 5114 O  O     . HOH G 5 .   ? 3.085   -22.003 -5.995  1.00 37.50  ? 936  HOH A O     1 
HETATM 5115 O  O     . HOH G 5 .   ? -11.129 2.531   7.044   1.00 19.02  ? 937  HOH A O     1 
HETATM 5116 O  O     . HOH G 5 .   ? -12.113 -1.198  22.146  1.00 38.93  ? 938  HOH A O     1 
HETATM 5117 O  O     . HOH G 5 .   ? -28.036 15.290  19.434  1.00 25.49  ? 939  HOH A O     1 
HETATM 5118 O  O     . HOH G 5 .   ? -4.755  -3.909  8.911   1.00 20.11  ? 940  HOH A O     1 
HETATM 5119 O  O     . HOH G 5 .   ? -1.382  31.841  18.776  1.00 26.69  ? 941  HOH A O     1 
HETATM 5120 O  O     . HOH G 5 .   ? 15.237  -21.814 -3.949  1.00 54.77  ? 942  HOH A O     1 
HETATM 5121 O  O     . HOH G 5 .   ? 5.243   -17.837 2.023   1.00 33.71  ? 943  HOH A O     1 
HETATM 5122 O  O     . HOH G 5 .   ? 10.220  2.970   3.331   1.00 34.41  ? 944  HOH A O     1 
HETATM 5123 O  O     . HOH G 5 .   ? -17.341 17.071  5.596   1.00 31.38  ? 945  HOH A O     1 
HETATM 5124 O  O     . HOH G 5 .   ? -8.454  0.942   -12.078 1.00 38.51  ? 946  HOH A O     1 
HETATM 5125 O  O     . HOH G 5 .   ? 15.869  7.659   3.242   1.00 42.69  ? 947  HOH A O     1 
HETATM 5126 O  O     . HOH G 5 .   ? -21.823 20.636  12.593  1.00 45.20  ? 948  HOH A O     1 
HETATM 5127 O  O     . HOH G 5 .   ? -14.106 -10.732 2.738   1.00 21.39  ? 949  HOH A O     1 
HETATM 5128 O  O     . HOH G 5 .   ? -0.863  22.271  19.746  1.00 26.11  ? 950  HOH A O     1 
HETATM 5129 O  O     . HOH G 5 .   ? -8.297  -6.304  18.217  1.00 26.51  ? 951  HOH A O     1 
HETATM 5130 O  O     . HOH G 5 .   ? -12.196 -20.080 -13.786 1.00 45.48  ? 952  HOH A O     1 
HETATM 5131 O  O     . HOH G 5 .   ? 17.098  20.516  12.425  1.00 39.13  ? 953  HOH A O     1 
HETATM 5132 O  O     . HOH G 5 .   ? -6.872  -4.960  1.303   1.00 19.66  ? 954  HOH A O     1 
HETATM 5133 O  O     . HOH G 5 .   ? -11.124 5.685   -9.904  1.00 49.08  ? 955  HOH A O     1 
HETATM 5134 O  O     . HOH G 5 .   ? 3.720   -12.303 12.869  1.00 31.04  ? 956  HOH A O     1 
HETATM 5135 O  O     . HOH G 5 .   ? 5.670   -22.135 -22.893 1.00 46.87  ? 957  HOH A O     1 
HETATM 5136 O  O     . HOH G 5 .   ? -10.729 16.316  -1.918  1.00 35.45  ? 958  HOH A O     1 
HETATM 5137 O  O     . HOH G 5 .   ? 1.335   -7.114  20.192  1.00 35.27  ? 959  HOH A O     1 
HETATM 5138 O  O     . HOH G 5 .   ? 4.339   -2.272  2.616   1.00 24.51  ? 960  HOH A O     1 
HETATM 5139 O  O     . HOH G 5 .   ? 7.665   -21.721 -21.558 1.00 45.74  ? 961  HOH A O     1 
HETATM 5140 O  O     . HOH G 5 .   ? 1.007   -23.480 -5.289  1.00 38.34  ? 962  HOH A O     1 
HETATM 5141 O  O     . HOH G 5 .   ? 2.424   4.313   26.832  1.00 42.82  ? 963  HOH A O     1 
HETATM 5142 O  O     . HOH G 5 .   ? -22.561 -10.027 23.283  1.00 57.71  ? 964  HOH A O     1 
HETATM 5143 O  O     . HOH G 5 .   ? -11.379 -2.648  6.618   1.00 22.59  ? 965  HOH A O     1 
HETATM 5144 O  O     . HOH G 5 .   ? 10.982  25.716  22.834  1.00 48.18  ? 966  HOH A O     1 
HETATM 5145 O  O     . HOH G 5 .   ? 3.119   13.587  32.101  1.00 45.03  ? 967  HOH A O     1 
HETATM 5146 O  O     . HOH G 5 .   ? -25.430 -3.479  14.357  1.00 43.32  ? 968  HOH A O     1 
HETATM 5147 O  O     . HOH G 5 .   ? -10.057 26.850  9.957   1.00 33.09  ? 969  HOH A O     1 
HETATM 5148 O  O     . HOH G 5 .   ? 5.020   -21.510 1.747   1.00 41.55  ? 970  HOH A O     1 
HETATM 5149 O  O     . HOH G 5 .   ? 9.554   4.462   1.332   1.00 35.74  ? 971  HOH A O     1 
HETATM 5150 O  O     . HOH G 5 .   ? -16.436 -9.118  3.522   1.00 27.14  ? 972  HOH A O     1 
HETATM 5151 O  O     . HOH G 5 .   ? -4.917  -20.078 -22.270 1.00 39.05  ? 973  HOH A O     1 
HETATM 5152 O  O     . HOH G 5 .   ? 6.742   -0.661  5.088   1.00 28.16  ? 974  HOH A O     1 
HETATM 5153 O  O     . HOH G 5 .   ? 7.808   -24.542 -1.318  1.00 46.21  ? 975  HOH A O     1 
HETATM 5154 O  O     . HOH G 5 .   ? -18.653 -18.838 -5.464  1.00 42.99  ? 976  HOH A O     1 
HETATM 5155 O  O     . HOH G 5 .   ? -13.347 -11.632 -2.944  1.00 27.49  ? 977  HOH A O     1 
HETATM 5156 O  O     . HOH G 5 .   ? -1.546  -24.826 -8.232  1.00 35.00  ? 978  HOH A O     1 
HETATM 5157 O  O     . HOH G 5 .   ? -14.299 -12.674 0.861   1.00 36.12  ? 979  HOH A O     1 
HETATM 5158 O  O     . HOH G 5 .   ? -24.958 15.102  11.050  1.00 39.95  ? 980  HOH A O     1 
HETATM 5159 O  O     . HOH G 5 .   ? 15.598  15.471  -6.782  1.00 29.49  ? 981  HOH A O     1 
HETATM 5160 O  O     . HOH G 5 .   ? 15.891  16.578  13.315  1.00 31.70  ? 982  HOH A O     1 
HETATM 5161 O  O     . HOH G 5 .   ? -1.578  24.811  0.132   1.00 37.88  ? 983  HOH A O     1 
HETATM 5162 O  O     . HOH G 5 .   ? 20.210  12.908  2.994   1.00 49.78  ? 984  HOH A O     1 
HETATM 5163 O  O     . HOH G 5 .   ? -5.520  -21.458 30.943  1.00 47.21  ? 985  HOH A O     1 
HETATM 5164 O  O     . HOH G 5 .   ? -23.765 24.681  24.611  1.00 48.06  ? 986  HOH A O     1 
HETATM 5165 O  O     . HOH G 5 .   ? 17.373  15.898  21.779  1.00 36.20  ? 987  HOH A O     1 
HETATM 5166 O  O     . HOH G 5 .   ? 0.654   -22.666 16.487  1.00 35.03  ? 988  HOH A O     1 
HETATM 5167 O  O     . HOH G 5 .   ? -26.435 1.117   23.441  1.00 44.25  ? 989  HOH A O     1 
HETATM 5168 O  O     . HOH G 5 .   ? -10.660 21.770  14.190  1.00 24.73  ? 990  HOH A O     1 
HETATM 5169 O  O     . HOH G 5 .   ? -23.689 19.110  13.444  1.00 38.32  ? 991  HOH A O     1 
HETATM 5170 O  O     . HOH G 5 .   ? 0.403   36.760  27.497  1.00 47.12  ? 992  HOH A O     1 
HETATM 5171 O  O     . HOH G 5 .   ? -11.269 -22.764 -17.069 1.00 41.16  ? 993  HOH A O     1 
HETATM 5172 O  O     . HOH G 5 .   ? -22.661 14.856  22.886  1.00 39.40  ? 994  HOH A O     1 
HETATM 5173 O  O     . HOH G 5 .   ? 18.192  10.375  2.475   1.00 42.87  ? 995  HOH A O     1 
HETATM 5174 O  O     . HOH G 5 .   ? 6.433   -30.239 3.286   1.00 43.56  ? 996  HOH A O     1 
HETATM 5175 O  O     . HOH G 5 .   ? 15.407  8.643   0.615   1.00 43.75  ? 997  HOH A O     1 
HETATM 5176 O  O     . HOH G 5 .   ? 5.396   0.932   11.717  1.00 43.74  ? 998  HOH A O     1 
HETATM 5177 O  O     . HOH G 5 .   ? -13.244 24.257  33.358  1.00 54.01  ? 999  HOH A O     1 
HETATM 5178 O  O     . HOH G 5 .   ? 2.984   -27.610 -17.051 1.00 43.00  ? 1000 HOH A O     1 
HETATM 5179 O  O     . HOH G 5 .   ? -4.807  -6.250  -0.192  1.00 23.40  ? 1001 HOH A O     1 
HETATM 5180 O  O     . HOH G 5 .   ? 4.632   -25.679 -22.982 1.00 49.27  ? 1002 HOH A O     1 
HETATM 5181 O  O     . HOH G 5 .   ? 4.579   -26.409 -6.481  1.00 44.11  ? 1003 HOH A O     1 
HETATM 5182 O  O     . HOH G 5 .   ? -17.156 10.286  -3.173  1.00 41.51  ? 1004 HOH A O     1 
HETATM 5183 O  O     . HOH G 5 .   ? -20.125 17.231  25.763  1.00 42.69  ? 1005 HOH A O     1 
HETATM 5184 O  O     . HOH G 5 .   ? -9.893  -1.858  30.492  1.00 45.77  ? 1006 HOH A O     1 
HETATM 5185 O  O     . HOH G 5 .   ? -12.040 -0.951  29.735  1.00 48.66  ? 1007 HOH A O     1 
HETATM 5186 O  O     . HOH G 5 .   ? -11.440 22.782  12.029  1.00 34.79  ? 1008 HOH A O     1 
HETATM 5187 O  O     . HOH G 5 .   ? -3.176  35.314  6.399   1.00 39.71  ? 1009 HOH A O     1 
HETATM 5188 O  O     . HOH G 5 .   ? -4.038  -35.659 0.168   1.00 42.91  ? 1010 HOH A O     1 
HETATM 5189 O  O     . HOH G 5 .   ? 7.681   33.120  17.864  1.00 44.13  ? 1011 HOH A O     1 
HETATM 5190 O  O     . HOH G 5 .   ? 9.481   -2.334  -20.112 1.00 68.21  ? 1012 HOH A O     1 
HETATM 5191 O  O     . HOH G 5 .   ? 1.956   17.620  19.258  1.00 30.41  ? 1013 HOH A O     1 
HETATM 5192 O  O     . HOH G 5 .   ? 10.363  -3.199  -14.545 1.00 44.44  ? 1014 HOH A O     1 
HETATM 5193 O  O     . HOH G 5 .   ? 4.378   16.171  32.448  1.00 44.03  ? 1015 HOH A O     1 
HETATM 5194 O  O     . HOH G 5 .   ? 7.495   11.150  26.647  1.00 44.95  ? 1016 HOH A O     1 
HETATM 5195 O  O     . HOH G 5 .   ? -2.533  30.751  25.011  1.00 38.89  ? 1017 HOH A O     1 
HETATM 5196 O  O     . HOH G 5 .   ? -25.862 19.617  14.399  1.00 41.65  ? 1018 HOH A O     1 
HETATM 5197 O  O     . HOH G 5 .   ? 2.184   -9.894  22.555  1.00 42.43  ? 1019 HOH A O     1 
HETATM 5198 O  O     . HOH G 5 .   ? -2.552  -35.258 2.122   1.00 46.70  ? 1020 HOH A O     1 
# 
