data_8RPG
# 
_entry.id   8RPG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8RPG         pdb_00008rpg 10.2210/pdb8rpg/pdb 
WWPDB D_1292135911 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RPG 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 mmartine@unizar.es   Marta    Martinez-Julvez ? 'principal investigator/group leader' 0000-0001-9047-0046 
3 ferreira@unizar.es   Patricia Ferreira        ? 'principal investigator/group leader' 0000-0003-4076-6118 
4 mangasjuan@uniovi.es Juan     Mangas-Sanchez  ? 'principal investigator/group leader' 0000-0002-3364-1512 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Martinez-Julvez, M.' 1 0000-0001-9047-0046 
'Ferreira, P.'        2 0000-0003-4076-6118 
'Cinca-Fernando, P.'  3 0000-0003-4929-9595 
# 
_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                   GW 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Appl.Microbiol.Biotechnol. 
_citation.journal_id_ASTM           AMBIDG 
_citation.journal_id_CSD            0786 
_citation.journal_id_ISSN           1432-0614 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            108 
_citation.language                  ? 
_citation.page_first                498 
_citation.page_last                 498 
_citation.title                     
'Discovery, characterization, and synthetic potential of two novel bacterial aryl-alcohol oxidases.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1007/s00253-024-13314-z 
_citation.pdbx_database_id_PubMed   39470785 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cinca-Fernando, P.'  1 ?                   
primary 'Ascaso-Alegre, C.'   2 ?                   
primary 'Sevilla, E.'         3 ?                   
primary 'Martinez-Julvez, M.' 4 ?                   
primary 'Mangas-Sanchez, J.'  5 ?                   
primary 'Ferreira, P.'        6 0000-0003-4076-6118 
# 
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 'Alcohol oxidase'             56729.574 1   1.1.3.7 ? ? ? 
2 non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE' 785.550   1   ?       ? ? ? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'          150.173   1   ?       ? ? ? 
4 non-polymer syn GLYCEROL                      92.094    6   ?       ? ? ? 
5 water       nat water                         18.015    304 ?       ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMSGTAFDYVIVGAGSAGCVLAARLSEDPEVRVALVEAGGADTDRAVRIPAAAAHLFGTGY
DWGYSTVPQAGLGGREVYWPRGRTLGGSSSVNFLMWVPGHAEDYEPWARAAGDLWSWDAVRPFLRGAEHWTGGPGAVYGT
EGPLWISPPRSPDPTTARFLQACGEAGLKEMTGGPGGPEHSGCALTPLNERNGARWSAADGYLRPAMDRGNLEVITGEQV
HRVLLEDGRATGVELAGRTLTARREVVLSAGTVGSAQLLMLSGIGDGPQLRAAGVEPRVQLPGVGRNLQDHVAVDVMMRA
TVAVPLADPDTPANRELYERERRGPLSSNIAEAVAFLRADGGTGAPDLELIWAPVADSEAVGGQGLTIAVVLLQPDSRGG
ITLAGADPSAAPLIDPGYLGAESDVRTLAAGVRFAERLFAAEALRGLVDGPAAPWPGPVGDDALERLVRERASTLFHPVG
TCRMGRAGDEQAVVDPWLRVHGVEGLRVADASVIPRVPRGHTHAHAVMIGERAAELIRPAG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMSGTAFDYVIVGAGSAGCVLAARLSEDPEVRVALVEAGGADTDRAVRIPAAAAHLFGTGY
DWGYSTVPQAGLGGREVYWPRGRTLGGSSSVNFLMWVPGHAEDYEPWARAAGDLWSWDAVRPFLRGAEHWTGGPGAVYGT
EGPLWISPPRSPDPTTARFLQACGEAGLKEMTGGPGGPEHSGCALTPLNERNGARWSAADGYLRPAMDRGNLEVITGEQV
HRVLLEDGRATGVELAGRTLTARREVVLSAGTVGSAQLLMLSGIGDGPQLRAAGVEPRVQLPGVGRNLQDHVAVDVMMRA
TVAVPLADPDTPANRELYERERRGPLSSNIAEAVAFLRADGGTGAPDLELIWAPVADSEAVGGQGLTIAVVLLQPDSRGG
ITLAGADPSAAPLIDPGYLGAESDVRTLAAGVRFAERLFAAEALRGLVDGPAAPWPGPVGDDALERLVRERASTLFHPVG
TCRMGRAGDEQAVVDPWLRVHGVEGLRVADASVIPRVPRGHTHAHAVMIGERAAELIRPAG
;
_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 'FLAVIN-ADENINE DINUCLEOTIDE' FAD 
3 'TRIETHYLENE GLYCOL'          PGE 
4 GLYCEROL                      GOL 
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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  SER n 
1 23  GLY n 
1 24  THR n 
1 25  ALA n 
1 26  PHE n 
1 27  ASP n 
1 28  TYR n 
1 29  VAL n 
1 30  ILE n 
1 31  VAL n 
1 32  GLY n 
1 33  ALA n 
1 34  GLY n 
1 35  SER n 
1 36  ALA n 
1 37  GLY n 
1 38  CYS n 
1 39  VAL n 
1 40  LEU n 
1 41  ALA n 
1 42  ALA n 
1 43  ARG n 
1 44  LEU n 
1 45  SER n 
1 46  GLU n 
1 47  ASP n 
1 48  PRO n 
1 49  GLU n 
1 50  VAL n 
1 51  ARG n 
1 52  VAL n 
1 53  ALA n 
1 54  LEU n 
1 55  VAL n 
1 56  GLU n 
1 57  ALA n 
1 58  GLY n 
1 59  GLY n 
1 60  ALA n 
1 61  ASP n 
1 62  THR n 
1 63  ASP n 
1 64  ARG n 
1 65  ALA n 
1 66  VAL n 
1 67  ARG n 
1 68  ILE n 
1 69  PRO n 
1 70  ALA n 
1 71  ALA n 
1 72  ALA n 
1 73  ALA n 
1 74  HIS n 
1 75  LEU n 
1 76  PHE n 
1 77  GLY n 
1 78  THR n 
1 79  GLY n 
1 80  TYR n 
1 81  ASP n 
1 82  TRP n 
1 83  GLY n 
1 84  TYR n 
1 85  SER n 
1 86  THR n 
1 87  VAL n 
1 88  PRO n 
1 89  GLN n 
1 90  ALA n 
1 91  GLY n 
1 92  LEU n 
1 93  GLY n 
1 94  GLY n 
1 95  ARG n 
1 96  GLU n 
1 97  VAL n 
1 98  TYR n 
1 99  TRP n 
1 100 PRO n 
1 101 ARG n 
1 102 GLY n 
1 103 ARG n 
1 104 THR n 
1 105 LEU n 
1 106 GLY n 
1 107 GLY n 
1 108 SER n 
1 109 SER n 
1 110 SER n 
1 111 VAL n 
1 112 ASN n 
1 113 PHE n 
1 114 LEU n 
1 115 MET n 
1 116 TRP n 
1 117 VAL n 
1 118 PRO n 
1 119 GLY n 
1 120 HIS n 
1 121 ALA n 
1 122 GLU n 
1 123 ASP n 
1 124 TYR n 
1 125 GLU n 
1 126 PRO n 
1 127 TRP n 
1 128 ALA n 
1 129 ARG n 
1 130 ALA n 
1 131 ALA n 
1 132 GLY n 
1 133 ASP n 
1 134 LEU n 
1 135 TRP n 
1 136 SER n 
1 137 TRP n 
1 138 ASP n 
1 139 ALA n 
1 140 VAL n 
1 141 ARG n 
1 142 PRO n 
1 143 PHE n 
1 144 LEU n 
1 145 ARG n 
1 146 GLY n 
1 147 ALA n 
1 148 GLU n 
1 149 HIS n 
1 150 TRP n 
1 151 THR n 
1 152 GLY n 
1 153 GLY n 
1 154 PRO n 
1 155 GLY n 
1 156 ALA n 
1 157 VAL n 
1 158 TYR n 
1 159 GLY n 
1 160 THR n 
1 161 GLU n 
1 162 GLY n 
1 163 PRO n 
1 164 LEU n 
1 165 TRP n 
1 166 ILE n 
1 167 SER n 
1 168 PRO n 
1 169 PRO n 
1 170 ARG n 
1 171 SER n 
1 172 PRO n 
1 173 ASP n 
1 174 PRO n 
1 175 THR n 
1 176 THR n 
1 177 ALA n 
1 178 ARG n 
1 179 PHE n 
1 180 LEU n 
1 181 GLN n 
1 182 ALA n 
1 183 CYS n 
1 184 GLY n 
1 185 GLU n 
1 186 ALA n 
1 187 GLY n 
1 188 LEU n 
1 189 LYS n 
1 190 GLU n 
1 191 MET n 
1 192 THR n 
1 193 GLY n 
1 194 GLY n 
1 195 PRO n 
1 196 GLY n 
1 197 GLY n 
1 198 PRO n 
1 199 GLU n 
1 200 HIS n 
1 201 SER n 
1 202 GLY n 
1 203 CYS n 
1 204 ALA n 
1 205 LEU n 
1 206 THR n 
1 207 PRO n 
1 208 LEU n 
1 209 ASN n 
1 210 GLU n 
1 211 ARG n 
1 212 ASN n 
1 213 GLY n 
1 214 ALA n 
1 215 ARG n 
1 216 TRP n 
1 217 SER n 
1 218 ALA n 
1 219 ALA n 
1 220 ASP n 
1 221 GLY n 
1 222 TYR n 
1 223 LEU n 
1 224 ARG n 
1 225 PRO n 
1 226 ALA n 
1 227 MET n 
1 228 ASP n 
1 229 ARG n 
1 230 GLY n 
1 231 ASN n 
1 232 LEU n 
1 233 GLU n 
1 234 VAL n 
1 235 ILE n 
1 236 THR n 
1 237 GLY n 
1 238 GLU n 
1 239 GLN n 
1 240 VAL n 
1 241 HIS n 
1 242 ARG n 
1 243 VAL n 
1 244 LEU n 
1 245 LEU n 
1 246 GLU n 
1 247 ASP n 
1 248 GLY n 
1 249 ARG n 
1 250 ALA n 
1 251 THR n 
1 252 GLY n 
1 253 VAL n 
1 254 GLU n 
1 255 LEU n 
1 256 ALA n 
1 257 GLY n 
1 258 ARG n 
1 259 THR n 
1 260 LEU n 
1 261 THR n 
1 262 ALA n 
1 263 ARG n 
1 264 ARG n 
1 265 GLU n 
1 266 VAL n 
1 267 VAL n 
1 268 LEU n 
1 269 SER n 
1 270 ALA n 
1 271 GLY n 
1 272 THR n 
1 273 VAL n 
1 274 GLY n 
1 275 SER n 
1 276 ALA n 
1 277 GLN n 
1 278 LEU n 
1 279 LEU n 
1 280 MET n 
1 281 LEU n 
1 282 SER n 
1 283 GLY n 
1 284 ILE n 
1 285 GLY n 
1 286 ASP n 
1 287 GLY n 
1 288 PRO n 
1 289 GLN n 
1 290 LEU n 
1 291 ARG n 
1 292 ALA n 
1 293 ALA n 
1 294 GLY n 
1 295 VAL n 
1 296 GLU n 
1 297 PRO n 
1 298 ARG n 
1 299 VAL n 
1 300 GLN n 
1 301 LEU n 
1 302 PRO n 
1 303 GLY n 
1 304 VAL n 
1 305 GLY n 
1 306 ARG n 
1 307 ASN n 
1 308 LEU n 
1 309 GLN n 
1 310 ASP n 
1 311 HIS n 
1 312 VAL n 
1 313 ALA n 
1 314 VAL n 
1 315 ASP n 
1 316 VAL n 
1 317 MET n 
1 318 MET n 
1 319 ARG n 
1 320 ALA n 
1 321 THR n 
1 322 VAL n 
1 323 ALA n 
1 324 VAL n 
1 325 PRO n 
1 326 LEU n 
1 327 ALA n 
1 328 ASP n 
1 329 PRO n 
1 330 ASP n 
1 331 THR n 
1 332 PRO n 
1 333 ALA n 
1 334 ASN n 
1 335 ARG n 
1 336 GLU n 
1 337 LEU n 
1 338 TYR n 
1 339 GLU n 
1 340 ARG n 
1 341 GLU n 
1 342 ARG n 
1 343 ARG n 
1 344 GLY n 
1 345 PRO n 
1 346 LEU n 
1 347 SER n 
1 348 SER n 
1 349 ASN n 
1 350 ILE n 
1 351 ALA n 
1 352 GLU n 
1 353 ALA n 
1 354 VAL n 
1 355 ALA n 
1 356 PHE n 
1 357 LEU n 
1 358 ARG n 
1 359 ALA n 
1 360 ASP n 
1 361 GLY n 
1 362 GLY n 
1 363 THR n 
1 364 GLY n 
1 365 ALA n 
1 366 PRO n 
1 367 ASP n 
1 368 LEU n 
1 369 GLU n 
1 370 LEU n 
1 371 ILE n 
1 372 TRP n 
1 373 ALA n 
1 374 PRO n 
1 375 VAL n 
1 376 ALA n 
1 377 ASP n 
1 378 SER n 
1 379 GLU n 
1 380 ALA n 
1 381 VAL n 
1 382 GLY n 
1 383 GLY n 
1 384 GLN n 
1 385 GLY n 
1 386 LEU n 
1 387 THR n 
1 388 ILE n 
1 389 ALA n 
1 390 VAL n 
1 391 VAL n 
1 392 LEU n 
1 393 LEU n 
1 394 GLN n 
1 395 PRO n 
1 396 ASP n 
1 397 SER n 
1 398 ARG n 
1 399 GLY n 
1 400 GLY n 
1 401 ILE n 
1 402 THR n 
1 403 LEU n 
1 404 ALA n 
1 405 GLY n 
1 406 ALA n 
1 407 ASP n 
1 408 PRO n 
1 409 SER n 
1 410 ALA n 
1 411 ALA n 
1 412 PRO n 
1 413 LEU n 
1 414 ILE n 
1 415 ASP n 
1 416 PRO n 
1 417 GLY n 
1 418 TYR n 
1 419 LEU n 
1 420 GLY n 
1 421 ALA n 
1 422 GLU n 
1 423 SER n 
1 424 ASP n 
1 425 VAL n 
1 426 ARG n 
1 427 THR n 
1 428 LEU n 
1 429 ALA n 
1 430 ALA n 
1 431 GLY n 
1 432 VAL n 
1 433 ARG n 
1 434 PHE n 
1 435 ALA n 
1 436 GLU n 
1 437 ARG n 
1 438 LEU n 
1 439 PHE n 
1 440 ALA n 
1 441 ALA n 
1 442 GLU n 
1 443 ALA n 
1 444 LEU n 
1 445 ARG n 
1 446 GLY n 
1 447 LEU n 
1 448 VAL n 
1 449 ASP n 
1 450 GLY n 
1 451 PRO n 
1 452 ALA n 
1 453 ALA n 
1 454 PRO n 
1 455 TRP n 
1 456 PRO n 
1 457 GLY n 
1 458 PRO n 
1 459 VAL n 
1 460 GLY n 
1 461 ASP n 
1 462 ASP n 
1 463 ALA n 
1 464 LEU n 
1 465 GLU n 
1 466 ARG n 
1 467 LEU n 
1 468 VAL n 
1 469 ARG n 
1 470 GLU n 
1 471 ARG n 
1 472 ALA n 
1 473 SER n 
1 474 THR n 
1 475 LEU n 
1 476 PHE n 
1 477 HIS n 
1 478 PRO n 
1 479 VAL n 
1 480 GLY n 
1 481 THR n 
1 482 CYS n 
1 483 ARG n 
1 484 MET n 
1 485 GLY n 
1 486 ARG n 
1 487 ALA n 
1 488 GLY n 
1 489 ASP n 
1 490 GLU n 
1 491 GLN n 
1 492 ALA n 
1 493 VAL n 
1 494 VAL n 
1 495 ASP n 
1 496 PRO n 
1 497 TRP n 
1 498 LEU n 
1 499 ARG n 
1 500 VAL n 
1 501 HIS n 
1 502 GLY n 
1 503 VAL n 
1 504 GLU n 
1 505 GLY n 
1 506 LEU n 
1 507 ARG n 
1 508 VAL n 
1 509 ALA n 
1 510 ASP n 
1 511 ALA n 
1 512 SER n 
1 513 VAL n 
1 514 ILE n 
1 515 PRO n 
1 516 ARG n 
1 517 VAL n 
1 518 PRO n 
1 519 ARG n 
1 520 GLY n 
1 521 HIS n 
1 522 THR n 
1 523 HIS n 
1 524 ALA n 
1 525 HIS n 
1 526 ALA n 
1 527 VAL n 
1 528 MET n 
1 529 ILE n 
1 530 GLY n 
1 531 GLU n 
1 532 ARG n 
1 533 ALA n 
1 534 ALA n 
1 535 GLU n 
1 536 LEU n 
1 537 ILE n 
1 538 ARG n 
1 539 PRO n 
1 540 ALA n 
1 541 GLY 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                   541 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Streptomyces hiroshimensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     66424 
_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-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE' ?                               'C27 H33 N9 O15 P2' 785.550 
GLN 'L-peptide linking' y GLUTAMINE                     ?                               'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'               ?                               'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                       ?                               'C2 H5 N O2'        75.067  
GOL non-polymer         . GLYCEROL                      'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE                     ?                               'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                         ?                               'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                    ?                               'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                       ?                               'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                        ?                               'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                    ?                               'C5 H11 N O2 S'     149.211 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'          ?                               'C6 H14 O4'         150.173 
PHE 'L-peptide linking' y PHENYLALANINE                 ?                               'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                       ?                               'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                        ?                               'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                     ?                               'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                    ?                               'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                      ?                               'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                        ?                               'C5 H11 N O2'       117.146 
# 
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   -20 ?   ?   ?   A . n 
A 1 2   GLY 2   -19 ?   ?   ?   A . n 
A 1 3   SER 3   -18 ?   ?   ?   A . n 
A 1 4   SER 4   -17 ?   ?   ?   A . n 
A 1 5   HIS 5   -16 ?   ?   ?   A . n 
A 1 6   HIS 6   -15 ?   ?   ?   A . n 
A 1 7   HIS 7   -14 ?   ?   ?   A . n 
A 1 8   HIS 8   -13 ?   ?   ?   A . n 
A 1 9   HIS 9   -12 ?   ?   ?   A . n 
A 1 10  HIS 10  -11 ?   ?   ?   A . n 
A 1 11  SER 11  -10 ?   ?   ?   A . n 
A 1 12  SER 12  -9  ?   ?   ?   A . n 
A 1 13  GLY 13  -8  ?   ?   ?   A . n 
A 1 14  LEU 14  -7  ?   ?   ?   A . n 
A 1 15  VAL 15  -6  ?   ?   ?   A . n 
A 1 16  PRO 16  -5  ?   ?   ?   A . n 
A 1 17  ARG 17  -4  ?   ?   ?   A . n 
A 1 18  GLY 18  -3  ?   ?   ?   A . n 
A 1 19  SER 19  -2  ?   ?   ?   A . n 
A 1 20  HIS 20  -1  ?   ?   ?   A . n 
A 1 21  MET 21  0   ?   ?   ?   A . n 
A 1 22  SER 22  1   ?   ?   ?   A . n 
A 1 23  GLY 23  2   ?   ?   ?   A . n 
A 1 24  THR 24  3   3   THR THR A . n 
A 1 25  ALA 25  4   4   ALA ALA A . n 
A 1 26  PHE 26  5   5   PHE PHE A . n 
A 1 27  ASP 27  6   6   ASP ASP A . n 
A 1 28  TYR 28  7   7   TYR TYR A . n 
A 1 29  VAL 29  8   8   VAL VAL A . n 
A 1 30  ILE 30  9   9   ILE ILE A . n 
A 1 31  VAL 31  10  10  VAL VAL A . n 
A 1 32  GLY 32  11  11  GLY GLY A . n 
A 1 33  ALA 33  12  12  ALA ALA A . n 
A 1 34  GLY 34  13  13  GLY GLY A . n 
A 1 35  SER 35  14  14  SER SER A . n 
A 1 36  ALA 36  15  15  ALA ALA A . n 
A 1 37  GLY 37  16  16  GLY GLY A . n 
A 1 38  CYS 38  17  17  CYS CYS A . n 
A 1 39  VAL 39  18  18  VAL VAL A . n 
A 1 40  LEU 40  19  19  LEU LEU A . n 
A 1 41  ALA 41  20  20  ALA ALA A . n 
A 1 42  ALA 42  21  21  ALA ALA A . n 
A 1 43  ARG 43  22  22  ARG ARG A . n 
A 1 44  LEU 44  23  23  LEU LEU A . n 
A 1 45  SER 45  24  24  SER SER A . n 
A 1 46  GLU 46  25  25  GLU GLU A . n 
A 1 47  ASP 47  26  26  ASP ASP A . n 
A 1 48  PRO 48  27  27  PRO PRO A . n 
A 1 49  GLU 49  28  28  GLU GLU A . n 
A 1 50  VAL 50  29  29  VAL VAL A . n 
A 1 51  ARG 51  30  30  ARG ARG A . n 
A 1 52  VAL 52  31  31  VAL VAL A . n 
A 1 53  ALA 53  32  32  ALA ALA A . n 
A 1 54  LEU 54  33  33  LEU LEU A . n 
A 1 55  VAL 55  34  34  VAL VAL A . n 
A 1 56  GLU 56  35  35  GLU GLU A . n 
A 1 57  ALA 57  36  36  ALA ALA A . n 
A 1 58  GLY 58  37  37  GLY GLY A . n 
A 1 59  GLY 59  38  38  GLY GLY A . n 
A 1 60  ALA 60  39  39  ALA ALA A . n 
A 1 61  ASP 61  40  40  ASP ASP A . n 
A 1 62  THR 62  41  41  THR THR A . n 
A 1 63  ASP 63  42  42  ASP ASP A . n 
A 1 64  ARG 64  43  43  ARG ARG A . n 
A 1 65  ALA 65  44  44  ALA ALA A . n 
A 1 66  VAL 66  45  45  VAL VAL A . n 
A 1 67  ARG 67  46  46  ARG ARG A . n 
A 1 68  ILE 68  47  47  ILE ILE A . n 
A 1 69  PRO 69  48  48  PRO PRO A . n 
A 1 70  ALA 70  49  49  ALA ALA A . n 
A 1 71  ALA 71  50  50  ALA ALA A . n 
A 1 72  ALA 72  51  51  ALA ALA A . n 
A 1 73  ALA 73  52  52  ALA ALA A . n 
A 1 74  HIS 74  53  53  HIS HIS A . n 
A 1 75  LEU 75  54  54  LEU LEU A . n 
A 1 76  PHE 76  55  55  PHE PHE A . n 
A 1 77  GLY 77  56  56  GLY GLY A . n 
A 1 78  THR 78  57  57  THR THR A . n 
A 1 79  GLY 79  58  58  GLY GLY A . n 
A 1 80  TYR 80  59  59  TYR TYR A . n 
A 1 81  ASP 81  60  60  ASP ASP A . n 
A 1 82  TRP 82  61  61  TRP TRP A . n 
A 1 83  GLY 83  62  62  GLY GLY A . n 
A 1 84  TYR 84  63  63  TYR TYR A . n 
A 1 85  SER 85  64  64  SER SER A . n 
A 1 86  THR 86  65  65  THR THR A . n 
A 1 87  VAL 87  66  66  VAL VAL A . n 
A 1 88  PRO 88  67  67  PRO PRO A . n 
A 1 89  GLN 89  68  68  GLN GLN A . n 
A 1 90  ALA 90  69  69  ALA ALA A . n 
A 1 91  GLY 91  70  70  GLY GLY A . n 
A 1 92  LEU 92  71  71  LEU LEU A . n 
A 1 93  GLY 93  72  72  GLY GLY A . n 
A 1 94  GLY 94  73  73  GLY GLY A . n 
A 1 95  ARG 95  74  74  ARG ARG A . n 
A 1 96  GLU 96  75  75  GLU GLU A . n 
A 1 97  VAL 97  76  76  VAL VAL A . n 
A 1 98  TYR 98  77  77  TYR TYR A . n 
A 1 99  TRP 99  78  78  TRP TRP A . n 
A 1 100 PRO 100 79  79  PRO PRO A . n 
A 1 101 ARG 101 80  80  ARG ARG A . n 
A 1 102 GLY 102 81  81  GLY GLY A . n 
A 1 103 ARG 103 82  82  ARG ARG A . n 
A 1 104 THR 104 83  83  THR THR A . n 
A 1 105 LEU 105 84  84  LEU LEU A . n 
A 1 106 GLY 106 85  85  GLY GLY A . n 
A 1 107 GLY 107 86  86  GLY GLY A . n 
A 1 108 SER 108 87  87  SER SER A . n 
A 1 109 SER 109 88  88  SER SER A . n 
A 1 110 SER 110 89  89  SER SER A . n 
A 1 111 VAL 111 90  90  VAL VAL A . n 
A 1 112 ASN 112 91  91  ASN ASN A . n 
A 1 113 PHE 113 92  92  PHE PHE A . n 
A 1 114 LEU 114 93  93  LEU LEU A . n 
A 1 115 MET 115 94  94  MET MET A . n 
A 1 116 TRP 116 95  95  TRP TRP A . n 
A 1 117 VAL 117 96  96  VAL VAL A . n 
A 1 118 PRO 118 97  97  PRO PRO A . n 
A 1 119 GLY 119 98  98  GLY GLY A . n 
A 1 120 HIS 120 99  99  HIS HIS A . n 
A 1 121 ALA 121 100 100 ALA ALA A . n 
A 1 122 GLU 122 101 101 GLU GLU A . n 
A 1 123 ASP 123 102 102 ASP ASP A . n 
A 1 124 TYR 124 103 103 TYR TYR A . n 
A 1 125 GLU 125 104 104 GLU GLU A . n 
A 1 126 PRO 126 105 105 PRO PRO A . n 
A 1 127 TRP 127 106 106 TRP TRP A . n 
A 1 128 ALA 128 107 107 ALA ALA A . n 
A 1 129 ARG 129 108 108 ARG ARG A . n 
A 1 130 ALA 130 109 109 ALA ALA A . n 
A 1 131 ALA 131 110 110 ALA ALA A . n 
A 1 132 GLY 132 111 111 GLY GLY A . n 
A 1 133 ASP 133 112 112 ASP ASP A . n 
A 1 134 LEU 134 113 113 LEU LEU A . n 
A 1 135 TRP 135 114 114 TRP TRP A . n 
A 1 136 SER 136 115 115 SER SER A . n 
A 1 137 TRP 137 116 116 TRP TRP A . n 
A 1 138 ASP 138 117 117 ASP ASP A . n 
A 1 139 ALA 139 118 118 ALA ALA A . n 
A 1 140 VAL 140 119 119 VAL VAL A . n 
A 1 141 ARG 141 120 120 ARG ARG A . n 
A 1 142 PRO 142 121 121 PRO PRO A . n 
A 1 143 PHE 143 122 122 PHE PHE A . n 
A 1 144 LEU 144 123 123 LEU LEU A . n 
A 1 145 ARG 145 124 124 ARG ARG A . n 
A 1 146 GLY 146 125 125 GLY GLY A . n 
A 1 147 ALA 147 126 126 ALA ALA A . n 
A 1 148 GLU 148 127 127 GLU GLU A . n 
A 1 149 HIS 149 128 128 HIS HIS A . n 
A 1 150 TRP 150 129 129 TRP TRP A . n 
A 1 151 THR 151 130 130 THR THR A . n 
A 1 152 GLY 152 131 131 GLY GLY A . n 
A 1 153 GLY 153 132 132 GLY GLY A . n 
A 1 154 PRO 154 133 133 PRO PRO A . n 
A 1 155 GLY 155 134 134 GLY GLY A . n 
A 1 156 ALA 156 135 135 ALA ALA A . n 
A 1 157 VAL 157 136 136 VAL VAL A . n 
A 1 158 TYR 158 137 137 TYR TYR A . n 
A 1 159 GLY 159 138 138 GLY GLY A . n 
A 1 160 THR 160 139 139 THR THR A . n 
A 1 161 GLU 161 140 140 GLU GLU A . n 
A 1 162 GLY 162 141 141 GLY GLY A . n 
A 1 163 PRO 163 142 142 PRO PRO A . n 
A 1 164 LEU 164 143 143 LEU LEU A . n 
A 1 165 TRP 165 144 144 TRP TRP A . n 
A 1 166 ILE 166 145 145 ILE ILE A . n 
A 1 167 SER 167 146 146 SER SER A . n 
A 1 168 PRO 168 147 147 PRO PRO A . n 
A 1 169 PRO 169 148 148 PRO PRO A . n 
A 1 170 ARG 170 149 149 ARG ARG A . n 
A 1 171 SER 171 150 150 SER SER A . n 
A 1 172 PRO 172 151 151 PRO PRO A . n 
A 1 173 ASP 173 152 152 ASP ASP A . n 
A 1 174 PRO 174 153 153 PRO PRO A . n 
A 1 175 THR 175 154 154 THR THR A . n 
A 1 176 THR 176 155 155 THR THR A . n 
A 1 177 ALA 177 156 156 ALA ALA A . n 
A 1 178 ARG 178 157 157 ARG ARG A . n 
A 1 179 PHE 179 158 158 PHE PHE A . n 
A 1 180 LEU 180 159 159 LEU LEU A . n 
A 1 181 GLN 181 160 160 GLN GLN A . n 
A 1 182 ALA 182 161 161 ALA ALA A . n 
A 1 183 CYS 183 162 162 CYS CYS A . n 
A 1 184 GLY 184 163 163 GLY GLY A . n 
A 1 185 GLU 185 164 164 GLU GLU A . n 
A 1 186 ALA 186 165 165 ALA ALA A . n 
A 1 187 GLY 187 166 166 GLY GLY A . n 
A 1 188 LEU 188 167 167 LEU LEU A . n 
A 1 189 LYS 189 168 168 LYS LYS A . n 
A 1 190 GLU 190 169 169 GLU GLU A . n 
A 1 191 MET 191 170 170 MET MET A . n 
A 1 192 THR 192 171 171 THR THR A . n 
A 1 193 GLY 193 172 172 GLY GLY A . n 
A 1 194 GLY 194 173 173 GLY GLY A . n 
A 1 195 PRO 195 174 174 PRO PRO A . n 
A 1 196 GLY 196 175 175 GLY GLY A . n 
A 1 197 GLY 197 176 176 GLY GLY A . n 
A 1 198 PRO 198 177 177 PRO PRO A . n 
A 1 199 GLU 199 178 178 GLU GLU A . n 
A 1 200 HIS 200 179 179 HIS HIS A . n 
A 1 201 SER 201 180 180 SER SER A . n 
A 1 202 GLY 202 181 181 GLY GLY A . n 
A 1 203 CYS 203 182 182 CYS CYS A . n 
A 1 204 ALA 204 183 183 ALA ALA A . n 
A 1 205 LEU 205 184 184 LEU LEU A . n 
A 1 206 THR 206 185 185 THR THR A . n 
A 1 207 PRO 207 186 186 PRO PRO A . n 
A 1 208 LEU 208 187 187 LEU LEU A . n 
A 1 209 ASN 209 188 188 ASN ASN A . n 
A 1 210 GLU 210 189 189 GLU GLU A . n 
A 1 211 ARG 211 190 190 ARG ARG A . n 
A 1 212 ASN 212 191 191 ASN ASN A . n 
A 1 213 GLY 213 192 192 GLY GLY A . n 
A 1 214 ALA 214 193 193 ALA ALA A . n 
A 1 215 ARG 215 194 194 ARG ARG A . n 
A 1 216 TRP 216 195 195 TRP TRP A . n 
A 1 217 SER 217 196 196 SER SER A . n 
A 1 218 ALA 218 197 197 ALA ALA A . n 
A 1 219 ALA 219 198 198 ALA ALA A . n 
A 1 220 ASP 220 199 199 ASP ASP A . n 
A 1 221 GLY 221 200 200 GLY GLY A . n 
A 1 222 TYR 222 201 201 TYR TYR A . n 
A 1 223 LEU 223 202 202 LEU LEU A . n 
A 1 224 ARG 224 203 203 ARG ARG A . n 
A 1 225 PRO 225 204 204 PRO PRO A . n 
A 1 226 ALA 226 205 205 ALA ALA A . n 
A 1 227 MET 227 206 206 MET MET A . n 
A 1 228 ASP 228 207 207 ASP ASP A . n 
A 1 229 ARG 229 208 208 ARG ARG A . n 
A 1 230 GLY 230 209 209 GLY GLY A . n 
A 1 231 ASN 231 210 210 ASN ASN A . n 
A 1 232 LEU 232 211 211 LEU LEU A . n 
A 1 233 GLU 233 212 212 GLU GLU A . n 
A 1 234 VAL 234 213 213 VAL VAL A . n 
A 1 235 ILE 235 214 214 ILE ILE A . n 
A 1 236 THR 236 215 215 THR THR A . n 
A 1 237 GLY 237 216 216 GLY GLY A . n 
A 1 238 GLU 238 217 217 GLU GLU A . n 
A 1 239 GLN 239 218 218 GLN GLN A . n 
A 1 240 VAL 240 219 219 VAL VAL A . n 
A 1 241 HIS 241 220 220 HIS HIS A . n 
A 1 242 ARG 242 221 221 ARG ARG A . n 
A 1 243 VAL 243 222 222 VAL VAL A . n 
A 1 244 LEU 244 223 223 LEU LEU A . n 
A 1 245 LEU 245 224 224 LEU LEU A . n 
A 1 246 GLU 246 225 225 GLU GLU A . n 
A 1 247 ASP 247 226 226 ASP ASP A . n 
A 1 248 GLY 248 227 227 GLY GLY A . n 
A 1 249 ARG 249 228 228 ARG ARG A . n 
A 1 250 ALA 250 229 229 ALA ALA A . n 
A 1 251 THR 251 230 230 THR THR A . n 
A 1 252 GLY 252 231 231 GLY GLY A . n 
A 1 253 VAL 253 232 232 VAL VAL A . n 
A 1 254 GLU 254 233 233 GLU GLU A . n 
A 1 255 LEU 255 234 234 LEU LEU A . n 
A 1 256 ALA 256 235 235 ALA ALA A . n 
A 1 257 GLY 257 236 236 GLY GLY A . n 
A 1 258 ARG 258 237 237 ARG ARG A . n 
A 1 259 THR 259 238 238 THR THR A . n 
A 1 260 LEU 260 239 239 LEU LEU A . n 
A 1 261 THR 261 240 240 THR THR A . n 
A 1 262 ALA 262 241 241 ALA ALA A . n 
A 1 263 ARG 263 242 242 ARG ARG A . n 
A 1 264 ARG 264 243 243 ARG ARG A . n 
A 1 265 GLU 265 244 244 GLU GLU A . n 
A 1 266 VAL 266 245 245 VAL VAL A . n 
A 1 267 VAL 267 246 246 VAL VAL A . n 
A 1 268 LEU 268 247 247 LEU LEU A . n 
A 1 269 SER 269 248 248 SER SER A . n 
A 1 270 ALA 270 249 249 ALA ALA A . n 
A 1 271 GLY 271 250 250 GLY GLY A . n 
A 1 272 THR 272 251 251 THR THR A . n 
A 1 273 VAL 273 252 252 VAL VAL A . n 
A 1 274 GLY 274 253 253 GLY GLY A . n 
A 1 275 SER 275 254 254 SER SER A . n 
A 1 276 ALA 276 255 255 ALA ALA A . n 
A 1 277 GLN 277 256 256 GLN GLN A . n 
A 1 278 LEU 278 257 257 LEU LEU A . n 
A 1 279 LEU 279 258 258 LEU LEU A . n 
A 1 280 MET 280 259 259 MET MET A . n 
A 1 281 LEU 281 260 260 LEU LEU A . n 
A 1 282 SER 282 261 261 SER SER A . n 
A 1 283 GLY 283 262 262 GLY GLY A . n 
A 1 284 ILE 284 263 263 ILE ILE A . n 
A 1 285 GLY 285 264 264 GLY GLY A . n 
A 1 286 ASP 286 265 265 ASP ASP A . n 
A 1 287 GLY 287 266 266 GLY GLY A . n 
A 1 288 PRO 288 267 267 PRO PRO A . n 
A 1 289 GLN 289 268 268 GLN GLN A . n 
A 1 290 LEU 290 269 269 LEU LEU A . n 
A 1 291 ARG 291 270 270 ARG ARG A . n 
A 1 292 ALA 292 271 271 ALA ALA A . n 
A 1 293 ALA 293 272 272 ALA ALA A . n 
A 1 294 GLY 294 273 273 GLY GLY A . n 
A 1 295 VAL 295 274 274 VAL VAL A . n 
A 1 296 GLU 296 275 275 GLU GLU A . n 
A 1 297 PRO 297 276 276 PRO PRO A . n 
A 1 298 ARG 298 277 277 ARG ARG A . n 
A 1 299 VAL 299 278 278 VAL VAL A . n 
A 1 300 GLN 300 279 279 GLN GLN A . n 
A 1 301 LEU 301 280 280 LEU LEU A . n 
A 1 302 PRO 302 281 281 PRO PRO A . n 
A 1 303 GLY 303 282 282 GLY GLY A . n 
A 1 304 VAL 304 283 283 VAL VAL A . n 
A 1 305 GLY 305 284 284 GLY GLY A . n 
A 1 306 ARG 306 285 285 ARG ARG A . n 
A 1 307 ASN 307 286 286 ASN ASN A . n 
A 1 308 LEU 308 287 287 LEU LEU A . n 
A 1 309 GLN 309 288 288 GLN GLN A . n 
A 1 310 ASP 310 289 289 ASP ASP A . n 
A 1 311 HIS 311 290 290 HIS HIS A . n 
A 1 312 VAL 312 291 291 VAL VAL A . n 
A 1 313 ALA 313 292 292 ALA ALA A . n 
A 1 314 VAL 314 293 293 VAL VAL A . n 
A 1 315 ASP 315 294 294 ASP ASP A . n 
A 1 316 VAL 316 295 295 VAL VAL A . n 
A 1 317 MET 317 296 296 MET MET A . n 
A 1 318 MET 318 297 297 MET MET A . n 
A 1 319 ARG 319 298 298 ARG ARG A . n 
A 1 320 ALA 320 299 299 ALA ALA A . n 
A 1 321 THR 321 300 300 THR THR A . n 
A 1 322 VAL 322 301 301 VAL VAL A . n 
A 1 323 ALA 323 302 302 ALA ALA A . n 
A 1 324 VAL 324 303 303 VAL VAL A . n 
A 1 325 PRO 325 304 304 PRO PRO A . n 
A 1 326 LEU 326 305 305 LEU LEU A . n 
A 1 327 ALA 327 306 306 ALA ALA A . n 
A 1 328 ASP 328 307 307 ASP ASP A . n 
A 1 329 PRO 329 308 308 PRO PRO A . n 
A 1 330 ASP 330 309 309 ASP ASP A . n 
A 1 331 THR 331 310 310 THR THR A . n 
A 1 332 PRO 332 311 311 PRO PRO A . n 
A 1 333 ALA 333 312 312 ALA ALA A . n 
A 1 334 ASN 334 313 313 ASN ASN A . n 
A 1 335 ARG 335 314 314 ARG ARG A . n 
A 1 336 GLU 336 315 315 GLU GLU A . n 
A 1 337 LEU 337 316 316 LEU LEU A . n 
A 1 338 TYR 338 317 317 TYR TYR A . n 
A 1 339 GLU 339 318 318 GLU GLU A . n 
A 1 340 ARG 340 319 319 ARG ARG A . n 
A 1 341 GLU 341 320 320 GLU GLU A . n 
A 1 342 ARG 342 321 321 ARG ARG A . n 
A 1 343 ARG 343 322 322 ARG ARG A . n 
A 1 344 GLY 344 323 323 GLY GLY A . n 
A 1 345 PRO 345 324 324 PRO PRO A . n 
A 1 346 LEU 346 325 325 LEU LEU A . n 
A 1 347 SER 347 326 326 SER SER A . n 
A 1 348 SER 348 327 327 SER SER A . n 
A 1 349 ASN 349 328 328 ASN ASN A . n 
A 1 350 ILE 350 329 329 ILE ILE A . n 
A 1 351 ALA 351 330 330 ALA ALA A . n 
A 1 352 GLU 352 331 331 GLU GLU A . n 
A 1 353 ALA 353 332 332 ALA ALA A . n 
A 1 354 VAL 354 333 333 VAL VAL A . n 
A 1 355 ALA 355 334 334 ALA ALA A . n 
A 1 356 PHE 356 335 335 PHE PHE A . n 
A 1 357 LEU 357 336 336 LEU LEU A . n 
A 1 358 ARG 358 337 337 ARG ARG A . n 
A 1 359 ALA 359 338 338 ALA ALA A . n 
A 1 360 ASP 360 339 339 ASP ASP A . n 
A 1 361 GLY 361 340 340 GLY GLY A . n 
A 1 362 GLY 362 341 341 GLY GLY A . n 
A 1 363 THR 363 342 342 THR THR A . n 
A 1 364 GLY 364 343 343 GLY GLY A . n 
A 1 365 ALA 365 344 344 ALA ALA A . n 
A 1 366 PRO 366 345 345 PRO PRO A . n 
A 1 367 ASP 367 346 346 ASP ASP A . n 
A 1 368 LEU 368 347 347 LEU LEU A . n 
A 1 369 GLU 369 348 348 GLU GLU A . n 
A 1 370 LEU 370 349 349 LEU LEU A . n 
A 1 371 ILE 371 350 350 ILE ILE A . n 
A 1 372 TRP 372 351 351 TRP TRP A . n 
A 1 373 ALA 373 352 352 ALA ALA A . n 
A 1 374 PRO 374 353 353 PRO PRO A . n 
A 1 375 VAL 375 354 354 VAL VAL A . n 
A 1 376 ALA 376 355 355 ALA ALA A . n 
A 1 377 ASP 377 356 356 ASP ASP A . n 
A 1 378 SER 378 357 357 SER SER A . n 
A 1 379 GLU 379 358 358 GLU GLU A . n 
A 1 380 ALA 380 359 359 ALA ALA A . n 
A 1 381 VAL 381 360 360 VAL VAL A . n 
A 1 382 GLY 382 361 361 GLY GLY A . n 
A 1 383 GLY 383 362 362 GLY GLY A . n 
A 1 384 GLN 384 363 363 GLN GLN A . n 
A 1 385 GLY 385 364 364 GLY GLY A . n 
A 1 386 LEU 386 365 365 LEU LEU A . n 
A 1 387 THR 387 366 366 THR THR A . n 
A 1 388 ILE 388 367 367 ILE ILE A . n 
A 1 389 ALA 389 368 368 ALA ALA A . n 
A 1 390 VAL 390 369 369 VAL VAL A . n 
A 1 391 VAL 391 370 370 VAL VAL A . n 
A 1 392 LEU 392 371 371 LEU LEU A . n 
A 1 393 LEU 393 372 372 LEU LEU A . n 
A 1 394 GLN 394 373 373 GLN GLN A . n 
A 1 395 PRO 395 374 374 PRO PRO A . n 
A 1 396 ASP 396 375 375 ASP ASP A . n 
A 1 397 SER 397 376 376 SER SER A . n 
A 1 398 ARG 398 377 377 ARG ARG A . n 
A 1 399 GLY 399 378 378 GLY GLY A . n 
A 1 400 GLY 400 379 379 GLY GLY A . n 
A 1 401 ILE 401 380 380 ILE ILE A . n 
A 1 402 THR 402 381 381 THR THR A . n 
A 1 403 LEU 403 382 382 LEU LEU A . n 
A 1 404 ALA 404 383 383 ALA ALA A . n 
A 1 405 GLY 405 384 384 GLY GLY A . n 
A 1 406 ALA 406 385 385 ALA ALA A . n 
A 1 407 ASP 407 386 386 ASP ASP A . n 
A 1 408 PRO 408 387 387 PRO PRO A . n 
A 1 409 SER 409 388 388 SER SER A . n 
A 1 410 ALA 410 389 389 ALA ALA A . n 
A 1 411 ALA 411 390 390 ALA ALA A . n 
A 1 412 PRO 412 391 391 PRO PRO A . n 
A 1 413 LEU 413 392 392 LEU LEU A . n 
A 1 414 ILE 414 393 393 ILE ILE A . n 
A 1 415 ASP 415 394 394 ASP ASP A . n 
A 1 416 PRO 416 395 395 PRO PRO A . n 
A 1 417 GLY 417 396 396 GLY GLY A . n 
A 1 418 TYR 418 397 397 TYR TYR A . n 
A 1 419 LEU 419 398 398 LEU LEU A . n 
A 1 420 GLY 420 399 399 GLY GLY A . n 
A 1 421 ALA 421 400 400 ALA ALA A . n 
A 1 422 GLU 422 401 401 GLU GLU A . n 
A 1 423 SER 423 402 402 SER SER A . n 
A 1 424 ASP 424 403 403 ASP ASP A . n 
A 1 425 VAL 425 404 404 VAL VAL A . n 
A 1 426 ARG 426 405 405 ARG ARG A . n 
A 1 427 THR 427 406 406 THR THR A . n 
A 1 428 LEU 428 407 407 LEU LEU A . n 
A 1 429 ALA 429 408 408 ALA ALA A . n 
A 1 430 ALA 430 409 409 ALA ALA A . n 
A 1 431 GLY 431 410 410 GLY GLY A . n 
A 1 432 VAL 432 411 411 VAL VAL A . n 
A 1 433 ARG 433 412 412 ARG ARG A . n 
A 1 434 PHE 434 413 413 PHE PHE A . n 
A 1 435 ALA 435 414 414 ALA ALA A . n 
A 1 436 GLU 436 415 415 GLU GLU A . n 
A 1 437 ARG 437 416 416 ARG ARG A . n 
A 1 438 LEU 438 417 417 LEU LEU A . n 
A 1 439 PHE 439 418 418 PHE PHE A . n 
A 1 440 ALA 440 419 419 ALA ALA A . n 
A 1 441 ALA 441 420 420 ALA ALA A . n 
A 1 442 GLU 442 421 421 GLU GLU A . n 
A 1 443 ALA 443 422 422 ALA ALA A . n 
A 1 444 LEU 444 423 423 LEU LEU A . n 
A 1 445 ARG 445 424 424 ARG ARG A . n 
A 1 446 GLY 446 425 425 GLY GLY A . n 
A 1 447 LEU 447 426 426 LEU LEU A . n 
A 1 448 VAL 448 427 427 VAL VAL A . n 
A 1 449 ASP 449 428 428 ASP ASP A . n 
A 1 450 GLY 450 429 429 GLY GLY A . n 
A 1 451 PRO 451 430 430 PRO PRO A . n 
A 1 452 ALA 452 431 431 ALA ALA A . n 
A 1 453 ALA 453 432 432 ALA ALA A . n 
A 1 454 PRO 454 433 433 PRO PRO A . n 
A 1 455 TRP 455 434 434 TRP TRP A . n 
A 1 456 PRO 456 435 435 PRO PRO A . n 
A 1 457 GLY 457 436 436 GLY GLY A . n 
A 1 458 PRO 458 437 437 PRO PRO A . n 
A 1 459 VAL 459 438 438 VAL VAL A . n 
A 1 460 GLY 460 439 439 GLY GLY A . n 
A 1 461 ASP 461 440 440 ASP ASP A . n 
A 1 462 ASP 462 441 441 ASP ASP A . n 
A 1 463 ALA 463 442 442 ALA ALA A . n 
A 1 464 LEU 464 443 443 LEU LEU A . n 
A 1 465 GLU 465 444 444 GLU GLU A . n 
A 1 466 ARG 466 445 445 ARG ARG A . n 
A 1 467 LEU 467 446 446 LEU LEU A . n 
A 1 468 VAL 468 447 447 VAL VAL A . n 
A 1 469 ARG 469 448 448 ARG ARG A . n 
A 1 470 GLU 470 449 449 GLU GLU A . n 
A 1 471 ARG 471 450 450 ARG ARG A . n 
A 1 472 ALA 472 451 451 ALA ALA A . n 
A 1 473 SER 473 452 452 SER SER A . n 
A 1 474 THR 474 453 453 THR THR A . n 
A 1 475 LEU 475 454 454 LEU LEU A . n 
A 1 476 PHE 476 455 455 PHE PHE A . n 
A 1 477 HIS 477 456 456 HIS HIS A . n 
A 1 478 PRO 478 457 457 PRO PRO A . n 
A 1 479 VAL 479 458 458 VAL VAL A . n 
A 1 480 GLY 480 459 459 GLY GLY A . n 
A 1 481 THR 481 460 460 THR THR A . n 
A 1 482 CYS 482 461 461 CYS CYS A . n 
A 1 483 ARG 483 462 462 ARG ARG A . n 
A 1 484 MET 484 463 463 MET MET A . n 
A 1 485 GLY 485 464 464 GLY GLY A . n 
A 1 486 ARG 486 465 465 ARG ARG A . n 
A 1 487 ALA 487 466 466 ALA ALA A . n 
A 1 488 GLY 488 467 467 GLY GLY A . n 
A 1 489 ASP 489 468 468 ASP ASP A . n 
A 1 490 GLU 490 469 469 GLU GLU A . n 
A 1 491 GLN 491 470 470 GLN GLN A . n 
A 1 492 ALA 492 471 471 ALA ALA A . n 
A 1 493 VAL 493 472 472 VAL VAL A . n 
A 1 494 VAL 494 473 473 VAL VAL A . n 
A 1 495 ASP 495 474 474 ASP ASP A . n 
A 1 496 PRO 496 475 475 PRO PRO A . n 
A 1 497 TRP 497 476 476 TRP TRP A . n 
A 1 498 LEU 498 477 477 LEU LEU A . n 
A 1 499 ARG 499 478 478 ARG ARG A . n 
A 1 500 VAL 500 479 479 VAL VAL A . n 
A 1 501 HIS 501 480 480 HIS HIS A . n 
A 1 502 GLY 502 481 481 GLY GLY A . n 
A 1 503 VAL 503 482 482 VAL VAL A . n 
A 1 504 GLU 504 483 483 GLU GLU A . n 
A 1 505 GLY 505 484 484 GLY GLY A . n 
A 1 506 LEU 506 485 485 LEU LEU A . n 
A 1 507 ARG 507 486 486 ARG ARG A . n 
A 1 508 VAL 508 487 487 VAL VAL A . n 
A 1 509 ALA 509 488 488 ALA ALA A . n 
A 1 510 ASP 510 489 489 ASP ASP A . n 
A 1 511 ALA 511 490 490 ALA ALA A . n 
A 1 512 SER 512 491 491 SER SER A . n 
A 1 513 VAL 513 492 492 VAL VAL A . n 
A 1 514 ILE 514 493 493 ILE ILE A . n 
A 1 515 PRO 515 494 494 PRO PRO A . n 
A 1 516 ARG 516 495 495 ARG ARG A . n 
A 1 517 VAL 517 496 496 VAL VAL A . n 
A 1 518 PRO 518 497 497 PRO PRO A . n 
A 1 519 ARG 519 498 498 ARG ARG A . n 
A 1 520 GLY 520 499 499 GLY GLY A . n 
A 1 521 HIS 521 500 500 HIS HIS A . n 
A 1 522 THR 522 501 501 THR THR A . n 
A 1 523 HIS 523 502 502 HIS HIS A . n 
A 1 524 ALA 524 503 503 ALA ALA A . n 
A 1 525 HIS 525 504 504 HIS HIS A . n 
A 1 526 ALA 526 505 505 ALA ALA A . n 
A 1 527 VAL 527 506 506 VAL VAL A . n 
A 1 528 MET 528 507 507 MET MET A . n 
A 1 529 ILE 529 508 508 ILE ILE A . n 
A 1 530 GLY 530 509 509 GLY GLY A . n 
A 1 531 GLU 531 510 510 GLU GLU A . n 
A 1 532 ARG 532 511 511 ARG ARG A . n 
A 1 533 ALA 533 512 512 ALA ALA A . n 
A 1 534 ALA 534 513 513 ALA ALA A . n 
A 1 535 GLU 535 514 514 GLU GLU A . n 
A 1 536 LEU 536 515 515 LEU LEU A . n 
A 1 537 ILE 537 516 516 ILE ILE A . n 
A 1 538 ARG 538 517 517 ARG ARG A . n 
A 1 539 PRO 539 518 518 PRO PRO A . n 
A 1 540 ALA 540 519 519 ALA ALA A . n 
A 1 541 GLY 541 520 520 GLY GLY 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 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PGE ? ? PGE ? ? '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 FAD 1   601  601 FAD FAD A . 
C 3 PGE 1   602  602 PGE PGE A . 
D 4 GOL 1   603  603 GOL GOL A . 
E 4 GOL 1   604  604 GOL GOL A . 
F 4 GOL 1   605  605 GOL GOL A . 
G 4 GOL 1   606  606 GOL GOL A . 
H 4 GOL 1   607  607 GOL GOL A . 
I 4 GOL 1   608  608 GOL GOL A . 
J 5 HOH 1   701  302 HOH HOH A . 
J 5 HOH 2   702  28  HOH HOH A . 
J 5 HOH 3   703  279 HOH HOH A . 
J 5 HOH 4   704  289 HOH HOH A . 
J 5 HOH 5   705  235 HOH HOH A . 
J 5 HOH 6   706  270 HOH HOH A . 
J 5 HOH 7   707  164 HOH HOH A . 
J 5 HOH 8   708  90  HOH HOH A . 
J 5 HOH 9   709  52  HOH HOH A . 
J 5 HOH 10  710  130 HOH HOH A . 
J 5 HOH 11  711  274 HOH HOH A . 
J 5 HOH 12  712  132 HOH HOH A . 
J 5 HOH 13  713  290 HOH HOH A . 
J 5 HOH 14  714  37  HOH HOH A . 
J 5 HOH 15  715  141 HOH HOH A . 
J 5 HOH 16  716  222 HOH HOH A . 
J 5 HOH 17  717  303 HOH HOH A . 
J 5 HOH 18  718  259 HOH HOH A . 
J 5 HOH 19  719  218 HOH HOH A . 
J 5 HOH 20  720  193 HOH HOH A . 
J 5 HOH 21  721  31  HOH HOH A . 
J 5 HOH 22  722  269 HOH HOH A . 
J 5 HOH 23  723  101 HOH HOH A . 
J 5 HOH 24  724  293 HOH HOH A . 
J 5 HOH 25  725  174 HOH HOH A . 
J 5 HOH 26  726  63  HOH HOH A . 
J 5 HOH 27  727  140 HOH HOH A . 
J 5 HOH 28  728  69  HOH HOH A . 
J 5 HOH 29  729  92  HOH HOH A . 
J 5 HOH 30  730  97  HOH HOH A . 
J 5 HOH 31  731  172 HOH HOH A . 
J 5 HOH 32  732  126 HOH HOH A . 
J 5 HOH 33  733  16  HOH HOH A . 
J 5 HOH 34  734  2   HOH HOH A . 
J 5 HOH 35  735  106 HOH HOH A . 
J 5 HOH 36  736  127 HOH HOH A . 
J 5 HOH 37  737  296 HOH HOH A . 
J 5 HOH 38  738  225 HOH HOH A . 
J 5 HOH 39  739  150 HOH HOH A . 
J 5 HOH 40  740  32  HOH HOH A . 
J 5 HOH 41  741  294 HOH HOH A . 
J 5 HOH 42  742  187 HOH HOH A . 
J 5 HOH 43  743  154 HOH HOH A . 
J 5 HOH 44  744  61  HOH HOH A . 
J 5 HOH 45  745  11  HOH HOH A . 
J 5 HOH 46  746  47  HOH HOH A . 
J 5 HOH 47  747  100 HOH HOH A . 
J 5 HOH 48  748  188 HOH HOH A . 
J 5 HOH 49  749  108 HOH HOH A . 
J 5 HOH 50  750  62  HOH HOH A . 
J 5 HOH 51  751  118 HOH HOH A . 
J 5 HOH 52  752  186 HOH HOH A . 
J 5 HOH 53  753  68  HOH HOH A . 
J 5 HOH 54  754  35  HOH HOH A . 
J 5 HOH 55  755  210 HOH HOH A . 
J 5 HOH 56  756  143 HOH HOH A . 
J 5 HOH 57  757  280 HOH HOH A . 
J 5 HOH 58  758  167 HOH HOH A . 
J 5 HOH 59  759  96  HOH HOH A . 
J 5 HOH 60  760  261 HOH HOH A . 
J 5 HOH 61  761  48  HOH HOH A . 
J 5 HOH 62  762  155 HOH HOH A . 
J 5 HOH 63  763  219 HOH HOH A . 
J 5 HOH 64  764  196 HOH HOH A . 
J 5 HOH 65  765  36  HOH HOH A . 
J 5 HOH 66  766  65  HOH HOH A . 
J 5 HOH 67  767  72  HOH HOH A . 
J 5 HOH 68  768  104 HOH HOH A . 
J 5 HOH 69  769  23  HOH HOH A . 
J 5 HOH 70  770  19  HOH HOH A . 
J 5 HOH 71  771  139 HOH HOH A . 
J 5 HOH 72  772  117 HOH HOH A . 
J 5 HOH 73  773  44  HOH HOH A . 
J 5 HOH 74  774  102 HOH HOH A . 
J 5 HOH 75  775  84  HOH HOH A . 
J 5 HOH 76  776  215 HOH HOH A . 
J 5 HOH 77  777  51  HOH HOH A . 
J 5 HOH 78  778  258 HOH HOH A . 
J 5 HOH 79  779  14  HOH HOH A . 
J 5 HOH 80  780  39  HOH HOH A . 
J 5 HOH 81  781  10  HOH HOH A . 
J 5 HOH 82  782  45  HOH HOH A . 
J 5 HOH 83  783  149 HOH HOH A . 
J 5 HOH 84  784  5   HOH HOH A . 
J 5 HOH 85  785  183 HOH HOH A . 
J 5 HOH 86  786  25  HOH HOH A . 
J 5 HOH 87  787  40  HOH HOH A . 
J 5 HOH 88  788  178 HOH HOH A . 
J 5 HOH 89  789  214 HOH HOH A . 
J 5 HOH 90  790  206 HOH HOH A . 
J 5 HOH 91  791  60  HOH HOH A . 
J 5 HOH 92  792  109 HOH HOH A . 
J 5 HOH 93  793  128 HOH HOH A . 
J 5 HOH 94  794  257 HOH HOH A . 
J 5 HOH 95  795  267 HOH HOH A . 
J 5 HOH 96  796  29  HOH HOH A . 
J 5 HOH 97  797  175 HOH HOH A . 
J 5 HOH 98  798  134 HOH HOH A . 
J 5 HOH 99  799  292 HOH HOH A . 
J 5 HOH 100 800  266 HOH HOH A . 
J 5 HOH 101 801  213 HOH HOH A . 
J 5 HOH 102 802  224 HOH HOH A . 
J 5 HOH 103 803  286 HOH HOH A . 
J 5 HOH 104 804  71  HOH HOH A . 
J 5 HOH 105 805  211 HOH HOH A . 
J 5 HOH 106 806  43  HOH HOH A . 
J 5 HOH 107 807  3   HOH HOH A . 
J 5 HOH 108 808  260 HOH HOH A . 
J 5 HOH 109 809  179 HOH HOH A . 
J 5 HOH 110 810  120 HOH HOH A . 
J 5 HOH 111 811  198 HOH HOH A . 
J 5 HOH 112 812  64  HOH HOH A . 
J 5 HOH 113 813  176 HOH HOH A . 
J 5 HOH 114 814  91  HOH HOH A . 
J 5 HOH 115 815  220 HOH HOH A . 
J 5 HOH 116 816  228 HOH HOH A . 
J 5 HOH 117 817  17  HOH HOH A . 
J 5 HOH 118 818  153 HOH HOH A . 
J 5 HOH 119 819  26  HOH HOH A . 
J 5 HOH 120 820  22  HOH HOH A . 
J 5 HOH 121 821  255 HOH HOH A . 
J 5 HOH 122 822  199 HOH HOH A . 
J 5 HOH 123 823  144 HOH HOH A . 
J 5 HOH 124 824  110 HOH HOH A . 
J 5 HOH 125 825  77  HOH HOH A . 
J 5 HOH 126 826  1   HOH HOH A . 
J 5 HOH 127 827  38  HOH HOH A . 
J 5 HOH 128 828  195 HOH HOH A . 
J 5 HOH 129 829  124 HOH HOH A . 
J 5 HOH 130 830  256 HOH HOH A . 
J 5 HOH 131 831  107 HOH HOH A . 
J 5 HOH 132 832  15  HOH HOH A . 
J 5 HOH 133 833  112 HOH HOH A . 
J 5 HOH 134 834  264 HOH HOH A . 
J 5 HOH 135 835  99  HOH HOH A . 
J 5 HOH 136 836  41  HOH HOH A . 
J 5 HOH 137 837  67  HOH HOH A . 
J 5 HOH 138 838  93  HOH HOH A . 
J 5 HOH 139 839  8   HOH HOH A . 
J 5 HOH 140 840  74  HOH HOH A . 
J 5 HOH 141 841  76  HOH HOH A . 
J 5 HOH 142 842  87  HOH HOH A . 
J 5 HOH 143 843  4   HOH HOH A . 
J 5 HOH 144 844  185 HOH HOH A . 
J 5 HOH 145 845  21  HOH HOH A . 
J 5 HOH 146 846  121 HOH HOH A . 
J 5 HOH 147 847  42  HOH HOH A . 
J 5 HOH 148 848  122 HOH HOH A . 
J 5 HOH 149 849  34  HOH HOH A . 
J 5 HOH 150 850  75  HOH HOH A . 
J 5 HOH 151 851  119 HOH HOH A . 
J 5 HOH 152 852  160 HOH HOH A . 
J 5 HOH 153 853  304 HOH HOH A . 
J 5 HOH 154 854  85  HOH HOH A . 
J 5 HOH 155 855  184 HOH HOH A . 
J 5 HOH 156 856  18  HOH HOH A . 
J 5 HOH 157 857  58  HOH HOH A . 
J 5 HOH 158 858  173 HOH HOH A . 
J 5 HOH 159 859  204 HOH HOH A . 
J 5 HOH 160 860  94  HOH HOH A . 
J 5 HOH 161 861  163 HOH HOH A . 
J 5 HOH 162 862  137 HOH HOH A . 
J 5 HOH 163 863  221 HOH HOH A . 
J 5 HOH 164 864  202 HOH HOH A . 
J 5 HOH 165 865  203 HOH HOH A . 
J 5 HOH 166 866  78  HOH HOH A . 
J 5 HOH 167 867  133 HOH HOH A . 
J 5 HOH 168 868  298 HOH HOH A . 
J 5 HOH 169 869  80  HOH HOH A . 
J 5 HOH 170 870  151 HOH HOH A . 
J 5 HOH 171 871  33  HOH HOH A . 
J 5 HOH 172 872  146 HOH HOH A . 
J 5 HOH 173 873  81  HOH HOH A . 
J 5 HOH 174 874  229 HOH HOH A . 
J 5 HOH 175 875  295 HOH HOH A . 
J 5 HOH 176 876  53  HOH HOH A . 
J 5 HOH 177 877  230 HOH HOH A . 
J 5 HOH 178 878  30  HOH HOH A . 
J 5 HOH 179 879  138 HOH HOH A . 
J 5 HOH 180 880  171 HOH HOH A . 
J 5 HOH 181 881  200 HOH HOH A . 
J 5 HOH 182 882  156 HOH HOH A . 
J 5 HOH 183 883  73  HOH HOH A . 
J 5 HOH 184 884  212 HOH HOH A . 
J 5 HOH 185 885  192 HOH HOH A . 
J 5 HOH 186 886  66  HOH HOH A . 
J 5 HOH 187 887  231 HOH HOH A . 
J 5 HOH 188 888  114 HOH HOH A . 
J 5 HOH 189 889  136 HOH HOH A . 
J 5 HOH 190 890  50  HOH HOH A . 
J 5 HOH 191 891  83  HOH HOH A . 
J 5 HOH 192 892  98  HOH HOH A . 
J 5 HOH 193 893  131 HOH HOH A . 
J 5 HOH 194 894  86  HOH HOH A . 
J 5 HOH 195 895  125 HOH HOH A . 
J 5 HOH 196 896  129 HOH HOH A . 
J 5 HOH 197 897  12  HOH HOH A . 
J 5 HOH 198 898  194 HOH HOH A . 
J 5 HOH 199 899  79  HOH HOH A . 
J 5 HOH 200 900  103 HOH HOH A . 
J 5 HOH 201 901  95  HOH HOH A . 
J 5 HOH 202 902  158 HOH HOH A . 
J 5 HOH 203 903  88  HOH HOH A . 
J 5 HOH 204 904  271 HOH HOH A . 
J 5 HOH 205 905  55  HOH HOH A . 
J 5 HOH 206 906  182 HOH HOH A . 
J 5 HOH 207 907  115 HOH HOH A . 
J 5 HOH 208 908  263 HOH HOH A . 
J 5 HOH 209 909  142 HOH HOH A . 
J 5 HOH 210 910  13  HOH HOH A . 
J 5 HOH 211 911  288 HOH HOH A . 
J 5 HOH 212 912  169 HOH HOH A . 
J 5 HOH 213 913  46  HOH HOH A . 
J 5 HOH 214 914  232 HOH HOH A . 
J 5 HOH 215 915  180 HOH HOH A . 
J 5 HOH 216 916  273 HOH HOH A . 
J 5 HOH 217 917  283 HOH HOH A . 
J 5 HOH 218 918  152 HOH HOH A . 
J 5 HOH 219 919  297 HOH HOH A . 
J 5 HOH 220 920  159 HOH HOH A . 
J 5 HOH 221 921  272 HOH HOH A . 
J 5 HOH 222 922  49  HOH HOH A . 
J 5 HOH 223 923  161 HOH HOH A . 
J 5 HOH 224 924  54  HOH HOH A . 
J 5 HOH 225 925  6   HOH HOH A . 
J 5 HOH 226 926  135 HOH HOH A . 
J 5 HOH 227 927  116 HOH HOH A . 
J 5 HOH 228 928  7   HOH HOH A . 
J 5 HOH 229 929  70  HOH HOH A . 
J 5 HOH 230 930  208 HOH HOH A . 
J 5 HOH 231 931  249 HOH HOH A . 
J 5 HOH 232 932  145 HOH HOH A . 
J 5 HOH 233 933  24  HOH HOH A . 
J 5 HOH 234 934  191 HOH HOH A . 
J 5 HOH 235 935  20  HOH HOH A . 
J 5 HOH 236 936  287 HOH HOH A . 
J 5 HOH 237 937  276 HOH HOH A . 
J 5 HOH 238 938  82  HOH HOH A . 
J 5 HOH 239 939  170 HOH HOH A . 
J 5 HOH 240 940  239 HOH HOH A . 
J 5 HOH 241 941  59  HOH HOH A . 
J 5 HOH 242 942  177 HOH HOH A . 
J 5 HOH 243 943  111 HOH HOH A . 
J 5 HOH 244 944  291 HOH HOH A . 
J 5 HOH 245 945  285 HOH HOH A . 
J 5 HOH 246 946  57  HOH HOH A . 
J 5 HOH 247 947  9   HOH HOH A . 
J 5 HOH 248 948  234 HOH HOH A . 
J 5 HOH 249 949  189 HOH HOH A . 
J 5 HOH 250 950  252 HOH HOH A . 
J 5 HOH 251 951  162 HOH HOH A . 
J 5 HOH 252 952  56  HOH HOH A . 
J 5 HOH 253 953  241 HOH HOH A . 
J 5 HOH 254 954  246 HOH HOH A . 
J 5 HOH 255 955  299 HOH HOH A . 
J 5 HOH 256 956  233 HOH HOH A . 
J 5 HOH 257 957  201 HOH HOH A . 
J 5 HOH 258 958  217 HOH HOH A . 
J 5 HOH 259 959  240 HOH HOH A . 
J 5 HOH 260 960  251 HOH HOH A . 
J 5 HOH 261 961  282 HOH HOH A . 
J 5 HOH 262 962  277 HOH HOH A . 
J 5 HOH 263 963  181 HOH HOH A . 
J 5 HOH 264 964  278 HOH HOH A . 
J 5 HOH 265 965  165 HOH HOH A . 
J 5 HOH 266 966  105 HOH HOH A . 
J 5 HOH 267 967  300 HOH HOH A . 
J 5 HOH 268 968  245 HOH HOH A . 
J 5 HOH 269 969  268 HOH HOH A . 
J 5 HOH 270 970  243 HOH HOH A . 
J 5 HOH 271 971  265 HOH HOH A . 
J 5 HOH 272 972  197 HOH HOH A . 
J 5 HOH 273 973  281 HOH HOH A . 
J 5 HOH 274 974  27  HOH HOH A . 
J 5 HOH 275 975  237 HOH HOH A . 
J 5 HOH 276 976  113 HOH HOH A . 
J 5 HOH 277 977  168 HOH HOH A . 
J 5 HOH 278 978  226 HOH HOH A . 
J 5 HOH 279 979  244 HOH HOH A . 
J 5 HOH 280 980  284 HOH HOH A . 
J 5 HOH 281 981  123 HOH HOH A . 
J 5 HOH 282 982  238 HOH HOH A . 
J 5 HOH 283 983  207 HOH HOH A . 
J 5 HOH 284 984  216 HOH HOH A . 
J 5 HOH 285 985  301 HOH HOH A . 
J 5 HOH 286 986  242 HOH HOH A . 
J 5 HOH 287 987  209 HOH HOH A . 
J 5 HOH 288 988  247 HOH HOH A . 
J 5 HOH 289 989  205 HOH HOH A . 
J 5 HOH 290 990  236 HOH HOH A . 
J 5 HOH 291 991  147 HOH HOH A . 
J 5 HOH 292 992  157 HOH HOH A . 
J 5 HOH 293 993  262 HOH HOH A . 
J 5 HOH 294 994  254 HOH HOH A . 
J 5 HOH 295 995  275 HOH HOH A . 
J 5 HOH 296 996  148 HOH HOH A . 
J 5 HOH 297 997  223 HOH HOH A . 
J 5 HOH 298 998  253 HOH HOH A . 
J 5 HOH 299 999  190 HOH HOH A . 
J 5 HOH 300 1000 166 HOH HOH A . 
J 5 HOH 301 1001 89  HOH HOH A . 
J 5 HOH 302 1002 250 HOH HOH A . 
J 5 HOH 303 1003 248 HOH HOH A . 
J 5 HOH 304 1004 227 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RPG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     80.510 
_cell.length_a_esd                 ? 
_cell.length_b                     97.688 
_cell.length_b_esd                 ? 
_cell.length_c                     68.047 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8RPG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8RPG 
_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             2.41 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.86 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    
;30 % Polyethylene glycol 4000 
100 mM TRIS pH 8.5 
200 mM Magnesium chloride
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-26 
_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   0.979180 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979180 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RPG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2 
_reflns.d_resolution_low                               97.69 
_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                                     36978 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.4 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.057 
_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                                    2 
_reflns_shell.d_res_low                                     2.11 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           5.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5325 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.235 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.68 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -1.67 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.99 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.456 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8RPG 
_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                            2.00 
_refine.ls_d_res_low                             62.21 
_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                     35032 
_refine.ls_number_reflns_R_free                  1898 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15317 
_refine.ls_R_factor_R_free                       0.19324 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15102 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.148 
_refine.pdbx_overall_ESU_R_Free                  0.137 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             3.104 
_refine.overall_SU_ML                            0.088 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        62.21 
_refine_hist.number_atoms_solvent             304 
_refine_hist.number_atoms_total               4225 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3921 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  4010 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3747 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.651  1.820  5470 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.573  1.735  8590 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.689  5.000  517  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.949  5.000  46   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.120 10.000 552  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.081  0.200  598  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  4958 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  923  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.046  2.395  2071 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.043  2.393  2070 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.735  4.290  2587 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.737  4.292  2588 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.455  2.784  1939 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.455  2.784  1940 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.180  4.901  2884 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.338  27.34  4496 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.508  26.01  4434 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.052 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             130 
_refine_ls_shell.number_reflns_R_work             2545 
_refine_ls_shell.percent_reflns_obs               99.96 
_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                  0.165 
_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   20 
_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                  0.224 
# 
_struct.entry_id                     8RPG 
_struct.title                        'Crystal structure of an alcohol oxidase from Streptomyces hiroshimensis' 
_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        8RPG 
_struct_keywords.text            'ALCOHOL OXIDASE, STREPTOMYCES HIROSHIMENSIS, OXIDOREDUCTASE, FLAVOPROTEIN' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8RPG 
_struct_ref.pdbx_db_accession          8RPG 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_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              8RPG 
_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                 541 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             8RPG 
_struct_ref_seq.db_align_beg                  -20 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  520 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       -20 
_struct_ref_seq.pdbx_auth_seq_align_end       520 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2990  ? 
1 MORE         -4    ? 
1 'SSA (A^2)'  18530 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_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 GLY A 34  ? SER A 45  ? GLY A 13  SER A 24  1 ? 12 
HELX_P HELX_P2  AA2 ASP A 63  ? ILE A 68  ? ASP A 42  ILE A 47  1 ? 6  
HELX_P HELX_P3  AA3 PRO A 69  ? PHE A 76  ? PRO A 48  PHE A 55  5 ? 8  
HELX_P HELX_P4  AA4 GLN A 89  ? GLY A 93  ? GLN A 68  GLY A 72  5 ? 5  
HELX_P HELX_P5  AA5 GLY A 106 ? VAL A 111 ? GLY A 85  VAL A 90  5 ? 6  
HELX_P HELX_P6  AA6 HIS A 120 ? ASP A 123 ? HIS A 99  ASP A 102 5 ? 4  
HELX_P HELX_P7  AA7 TYR A 124 ? GLY A 132 ? TYR A 103 GLY A 111 1 ? 9  
HELX_P HELX_P8  AA8 ASP A 133 ? TRP A 135 ? ASP A 112 TRP A 114 5 ? 3  
HELX_P HELX_P9  AA9 SER A 136 ? GLY A 146 ? SER A 115 GLY A 125 1 ? 11 
HELX_P HELX_P10 AB1 ASP A 173 ? ALA A 186 ? ASP A 152 ALA A 165 1 ? 14 
HELX_P HELX_P11 AB2 SER A 217 ? TYR A 222 ? SER A 196 TYR A 201 1 ? 6  
HELX_P HELX_P12 AB3 TYR A 222 ? MET A 227 ? TYR A 201 MET A 206 1 ? 6  
HELX_P HELX_P13 AB4 ALA A 270 ? SER A 282 ? ALA A 249 SER A 261 1 ? 13 
HELX_P HELX_P14 AB5 ASP A 286 ? ALA A 293 ? ASP A 265 ALA A 272 1 ? 8  
HELX_P HELX_P15 AB6 VAL A 324 ? ASP A 328 ? VAL A 303 ASP A 307 5 ? 5  
HELX_P HELX_P16 AB7 THR A 331 ? ARG A 342 ? THR A 310 ARG A 321 1 ? 12 
HELX_P HELX_P17 AB8 GLY A 344 ? SER A 348 ? GLY A 323 SER A 327 5 ? 5  
HELX_P HELX_P18 AB9 SER A 378 ? GLY A 382 ? SER A 357 GLY A 361 5 ? 5  
HELX_P HELX_P19 AC1 ALA A 421 ? ALA A 441 ? ALA A 400 ALA A 420 1 ? 21 
HELX_P HELX_P20 AC2 ALA A 441 ? GLY A 446 ? ALA A 420 GLY A 425 1 ? 6  
HELX_P HELX_P21 AC3 GLY A 460 ? ALA A 472 ? GLY A 439 ALA A 451 1 ? 13 
HELX_P HELX_P22 AC4 ASP A 510 ? ILE A 514 ? ASP A 489 ILE A 493 5 ? 5  
HELX_P HELX_P23 AC5 THR A 522 ? ARG A 538 ? THR A 501 ARG A 517 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ALA 
_struct_mon_prot_cis.label_seq_id           453 
_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           ALA 
_struct_mon_prot_cis.auth_seq_id            432 
_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    454 
_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     433 
_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       4.21 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 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 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA9 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 LEU A 232 ? ILE A 235 ? LEU A 211 ILE A 214 
AA1 2 VAL A 52  ? VAL A 55  ? VAL A 31  VAL A 34  
AA1 3 ALA A 25  ? VAL A 31  ? ALA A 4   VAL A 10  
AA1 4 THR A 259 ? LEU A 268 ? THR A 238 LEU A 247 
AA1 5 ARG A 249 ? GLU A 254 ? ARG A 228 GLU A 233 
AA1 6 ARG A 242 ? GLU A 246 ? ARG A 221 GLU A 225 
AA2 1 LEU A 232 ? ILE A 235 ? LEU A 211 ILE A 214 
AA2 2 VAL A 52  ? VAL A 55  ? VAL A 31  VAL A 34  
AA2 3 ALA A 25  ? VAL A 31  ? ALA A 4   VAL A 10  
AA2 4 THR A 259 ? LEU A 268 ? THR A 238 LEU A 247 
AA2 5 LEU A 506 ? VAL A 508 ? LEU A 485 VAL A 487 
AA3 1 TYR A 84  ? SER A 85  ? TYR A 63  SER A 64  
AA3 2 TYR A 98  ? TRP A 99  ? TYR A 77  TRP A 78  
AA4 1 GLU A 148 ? TRP A 150 ? GLU A 127 TRP A 129 
AA4 2 LEU A 164 ? ILE A 166 ? LEU A 143 ILE A 145 
AA5 1 GLY A 202 ? LEU A 205 ? GLY A 181 LEU A 184 
AA5 2 ALA A 353 ? LEU A 357 ? ALA A 332 LEU A 336 
AA5 3 LEU A 368 ? ALA A 373 ? LEU A 347 ALA A 352 
AA5 4 GLY A 385 ? LEU A 392 ? GLY A 364 LEU A 371 
AA5 5 VAL A 312 ? ALA A 320 ? VAL A 291 ALA A 299 
AA5 6 VAL A 448 ? PRO A 451 ? VAL A 427 PRO A 430 
AA6 1 GLY A 202 ? LEU A 205 ? GLY A 181 LEU A 184 
AA6 2 ALA A 353 ? LEU A 357 ? ALA A 332 LEU A 336 
AA6 3 LEU A 368 ? ALA A 373 ? LEU A 347 ALA A 352 
AA6 4 GLY A 385 ? LEU A 392 ? GLY A 364 LEU A 371 
AA6 5 VAL A 312 ? ALA A 320 ? VAL A 291 ALA A 299 
AA6 6 SER A 473 ? THR A 474 ? SER A 452 THR A 453 
AA7 1 GLU A 210 ? ARG A 211 ? GLU A 189 ARG A 190 
AA7 2 ALA A 214 ? ARG A 215 ? ALA A 193 ARG A 194 
AA8 1 ILE A 284 ? GLY A 285 ? ILE A 263 GLY A 264 
AA8 2 VAL A 299 ? GLN A 300 ? VAL A 278 GLN A 279 
AA9 1 GLY A 400 ? THR A 402 ? GLY A 379 THR A 381 
AA9 2 LEU A 413 ? ASP A 415 ? LEU A 392 ASP A 394 
# 
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 O ILE A 235 ? O ILE A 214 N LEU A 54  ? N LEU A 33  
AA1 2 3 O ALA A 53  ? O ALA A 32  N ILE A 30  ? N ILE A 9   
AA1 3 4 N PHE A 26  ? N PHE A 5   O ARG A 263 ? O ARG A 242 
AA1 4 5 O ALA A 262 ? O ALA A 241 N THR A 251 ? N THR A 230 
AA1 5 6 O GLU A 254 ? O GLU A 233 N ARG A 242 ? N ARG A 221 
AA2 1 2 O ILE A 235 ? O ILE A 214 N LEU A 54  ? N LEU A 33  
AA2 2 3 O ALA A 53  ? O ALA A 32  N ILE A 30  ? N ILE A 9   
AA2 3 4 N PHE A 26  ? N PHE A 5   O ARG A 263 ? O ARG A 242 
AA2 4 5 N LEU A 268 ? N LEU A 247 O ARG A 507 ? O ARG A 486 
AA3 1 2 N TYR A 84  ? N TYR A 63  O TRP A 99  ? O TRP A 78  
AA4 1 2 N HIS A 149 ? N HIS A 128 O LEU A 164 ? O LEU A 143 
AA5 1 2 N GLY A 202 ? N GLY A 181 O PHE A 356 ? O PHE A 335 
AA5 2 3 N ALA A 355 ? N ALA A 334 O LEU A 370 ? O LEU A 349 
AA5 3 4 N ILE A 371 ? N ILE A 350 O ALA A 389 ? O ALA A 368 
AA5 4 5 O LEU A 392 ? O LEU A 371 N VAL A 312 ? N VAL A 291 
AA5 5 6 N ARG A 319 ? N ARG A 298 O GLY A 450 ? O GLY A 429 
AA6 1 2 N GLY A 202 ? N GLY A 181 O PHE A 356 ? O PHE A 335 
AA6 2 3 N ALA A 355 ? N ALA A 334 O LEU A 370 ? O LEU A 349 
AA6 3 4 N ILE A 371 ? N ILE A 350 O ALA A 389 ? O ALA A 368 
AA6 4 5 O LEU A 392 ? O LEU A 371 N VAL A 312 ? N VAL A 291 
AA6 5 6 N ALA A 313 ? N ALA A 292 O SER A 473 ? O SER A 452 
AA7 1 2 N ARG A 211 ? N ARG A 190 O ALA A 214 ? O ALA A 193 
AA8 1 2 N GLY A 285 ? N GLY A 264 O VAL A 299 ? O VAL A 278 
AA9 1 2 N THR A 402 ? N THR A 381 O LEU A 413 ? O LEU A 392 
# 
_pdbx_entry_details.entry_id                   8RPG 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 321 ? ? CZ A ARG 321 ? ? NH2 A ARG 321 ? ? 115.73 120.30 -4.57 0.50 N 
2 1 NE A ARG 462 ? ? CZ A ARG 462 ? ? NH2 A ARG 462 ? ? 116.22 120.30 -4.08 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 12  ? ? -94.51  55.98   
2 1 THR A 83  ? ? 179.31  173.61  
3 1 LEU A 280 ? ? -152.87 80.30   
4 1 ILE A 329 ? ? 81.74   -50.39  
5 1 ASP A 489 ? ? -175.41 -168.85 
6 1 ARG A 498 ? ? -88.84  48.94   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    458 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    459 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.86 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 120 ? ? 0.081 'SIDE CHAIN' 
2 1 ARG A 228 ? ? 0.074 'SIDE CHAIN' 
3 1 ARG A 285 ? ? 0.121 'SIDE CHAIN' 
4 1 ARG A 322 ? ? 0.080 'SIDE CHAIN' 
5 1 ARG A 511 ? ? 0.144 'SIDE CHAIN' 
# 
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 -20 ? A MET 1  
2  1 Y 1 A GLY -19 ? A GLY 2  
3  1 Y 1 A SER -18 ? A SER 3  
4  1 Y 1 A SER -17 ? A SER 4  
5  1 Y 1 A HIS -16 ? A HIS 5  
6  1 Y 1 A HIS -15 ? A HIS 6  
7  1 Y 1 A HIS -14 ? A HIS 7  
8  1 Y 1 A HIS -13 ? A HIS 8  
9  1 Y 1 A HIS -12 ? A HIS 9  
10 1 Y 1 A HIS -11 ? A HIS 10 
11 1 Y 1 A SER -10 ? A SER 11 
12 1 Y 1 A SER -9  ? A SER 12 
13 1 Y 1 A GLY -8  ? A GLY 13 
14 1 Y 1 A LEU -7  ? A LEU 14 
15 1 Y 1 A VAL -6  ? A VAL 15 
16 1 Y 1 A PRO -5  ? A PRO 16 
17 1 Y 1 A ARG -4  ? A ARG 17 
18 1 Y 1 A GLY -3  ? A GLY 18 
19 1 Y 1 A SER -2  ? A SER 19 
20 1 Y 1 A HIS -1  ? A HIS 20 
21 1 Y 1 A MET 0   ? A MET 21 
22 1 Y 1 A SER 1   ? A SER 22 
23 1 Y 1 A GLY 2   ? A GLY 23 
# 
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  
FAD PA     P N R 88  
FAD O1A    O N N 89  
FAD O2A    O N N 90  
FAD O5B    O N N 91  
FAD C5B    C N N 92  
FAD C4B    C N R 93  
FAD O4B    O N N 94  
FAD C3B    C N S 95  
FAD O3B    O N N 96  
FAD C2B    C N R 97  
FAD O2B    O N N 98  
FAD C1B    C N R 99  
FAD N9A    N Y N 100 
FAD C8A    C Y N 101 
FAD N7A    N Y N 102 
FAD C5A    C Y N 103 
FAD C6A    C Y N 104 
FAD N6A    N N N 105 
FAD N1A    N Y N 106 
FAD C2A    C Y N 107 
FAD N3A    N Y N 108 
FAD C4A    C Y N 109 
FAD N1     N N N 110 
FAD C2     C N N 111 
FAD O2     O N N 112 
FAD N3     N N N 113 
FAD C4     C N N 114 
FAD O4     O N N 115 
FAD C4X    C N N 116 
FAD N5     N N N 117 
FAD C5X    C Y N 118 
FAD C6     C Y N 119 
FAD C7     C Y N 120 
FAD C7M    C N N 121 
FAD C8     C Y N 122 
FAD C8M    C N N 123 
FAD C9     C Y N 124 
FAD C9A    C Y N 125 
FAD N10    N N N 126 
FAD C10    C N N 127 
FAD "C1'"  C N N 128 
FAD "C2'"  C N S 129 
FAD "O2'"  O N N 130 
FAD "C3'"  C N S 131 
FAD "O3'"  O N N 132 
FAD "C4'"  C N R 133 
FAD "O4'"  O N N 134 
FAD "C5'"  C N N 135 
FAD "O5'"  O N N 136 
FAD P      P N R 137 
FAD O1P    O N N 138 
FAD O2P    O N N 139 
FAD O3P    O N N 140 
FAD HOA2   H N N 141 
FAD H51A   H N N 142 
FAD H52A   H N N 143 
FAD H4B    H N N 144 
FAD H3B    H N N 145 
FAD HO3A   H N N 146 
FAD H2B    H N N 147 
FAD HO2A   H N N 148 
FAD H1B    H N N 149 
FAD H8A    H N N 150 
FAD H61A   H N N 151 
FAD H62A   H N N 152 
FAD H2A    H N N 153 
FAD HN3    H N N 154 
FAD H6     H N N 155 
FAD HM71   H N N 156 
FAD HM72   H N N 157 
FAD HM73   H N N 158 
FAD HM81   H N N 159 
FAD HM82   H N N 160 
FAD HM83   H N N 161 
FAD H9     H N N 162 
FAD "H1'1" H N N 163 
FAD "H1'2" H N N 164 
FAD "H2'"  H N N 165 
FAD "HO2'" H N N 166 
FAD "H3'"  H N N 167 
FAD "HO3'" H N N 168 
FAD "H4'"  H N N 169 
FAD "HO4'" H N N 170 
FAD "H5'1" H N N 171 
FAD "H5'2" H N N 172 
FAD HOP2   H N N 173 
GLN N      N N N 174 
GLN CA     C N S 175 
GLN C      C N N 176 
GLN O      O N N 177 
GLN CB     C N N 178 
GLN CG     C N N 179 
GLN CD     C N N 180 
GLN OE1    O N N 181 
GLN NE2    N N N 182 
GLN OXT    O N N 183 
GLN H      H N N 184 
GLN H2     H N N 185 
GLN HA     H N N 186 
GLN HB2    H N N 187 
GLN HB3    H N N 188 
GLN HG2    H N N 189 
GLN HG3    H N N 190 
GLN HE21   H N N 191 
GLN HE22   H N N 192 
GLN HXT    H N N 193 
GLU N      N N N 194 
GLU CA     C N S 195 
GLU C      C N N 196 
GLU O      O N N 197 
GLU CB     C N N 198 
GLU CG     C N N 199 
GLU CD     C N N 200 
GLU OE1    O N N 201 
GLU OE2    O N N 202 
GLU OXT    O N N 203 
GLU H      H N N 204 
GLU H2     H N N 205 
GLU HA     H N N 206 
GLU HB2    H N N 207 
GLU HB3    H N N 208 
GLU HG2    H N N 209 
GLU HG3    H N N 210 
GLU HE2    H N N 211 
GLU HXT    H N N 212 
GLY N      N N N 213 
GLY CA     C N N 214 
GLY C      C N N 215 
GLY O      O N N 216 
GLY OXT    O N N 217 
GLY H      H N N 218 
GLY H2     H N N 219 
GLY HA2    H N N 220 
GLY HA3    H N N 221 
GLY HXT    H N N 222 
GOL C1     C N N 223 
GOL O1     O N N 224 
GOL C2     C N N 225 
GOL O2     O N N 226 
GOL C3     C N N 227 
GOL O3     O N N 228 
GOL H11    H N N 229 
GOL H12    H N N 230 
GOL HO1    H N N 231 
GOL H2     H N N 232 
GOL HO2    H N N 233 
GOL H31    H N N 234 
GOL H32    H N N 235 
GOL HO3    H N N 236 
HIS N      N N N 237 
HIS CA     C N S 238 
HIS C      C N N 239 
HIS O      O N N 240 
HIS CB     C N N 241 
HIS CG     C Y N 242 
HIS ND1    N Y N 243 
HIS CD2    C Y N 244 
HIS CE1    C Y N 245 
HIS NE2    N Y N 246 
HIS OXT    O N N 247 
HIS H      H N N 248 
HIS H2     H N N 249 
HIS HA     H N N 250 
HIS HB2    H N N 251 
HIS HB3    H N N 252 
HIS HD1    H N N 253 
HIS HD2    H N N 254 
HIS HE1    H N N 255 
HIS HE2    H N N 256 
HIS HXT    H N N 257 
HOH O      O N N 258 
HOH H1     H N N 259 
HOH H2     H N N 260 
ILE N      N N N 261 
ILE CA     C N S 262 
ILE C      C N N 263 
ILE O      O N N 264 
ILE CB     C N S 265 
ILE CG1    C N N 266 
ILE CG2    C N N 267 
ILE CD1    C N N 268 
ILE OXT    O N N 269 
ILE H      H N N 270 
ILE H2     H N N 271 
ILE HA     H N N 272 
ILE HB     H N N 273 
ILE HG12   H N N 274 
ILE HG13   H N N 275 
ILE HG21   H N N 276 
ILE HG22   H N N 277 
ILE HG23   H N N 278 
ILE HD11   H N N 279 
ILE HD12   H N N 280 
ILE HD13   H N N 281 
ILE HXT    H N N 282 
LEU N      N N N 283 
LEU CA     C N S 284 
LEU C      C N N 285 
LEU O      O N N 286 
LEU CB     C N N 287 
LEU CG     C N N 288 
LEU CD1    C N N 289 
LEU CD2    C N N 290 
LEU OXT    O N N 291 
LEU H      H N N 292 
LEU H2     H N N 293 
LEU HA     H N N 294 
LEU HB2    H N N 295 
LEU HB3    H N N 296 
LEU HG     H N N 297 
LEU HD11   H N N 298 
LEU HD12   H N N 299 
LEU HD13   H N N 300 
LEU HD21   H N N 301 
LEU HD22   H N N 302 
LEU HD23   H N N 303 
LEU HXT    H N N 304 
LYS N      N N N 305 
LYS CA     C N S 306 
LYS C      C N N 307 
LYS O      O N N 308 
LYS CB     C N N 309 
LYS CG     C N N 310 
LYS CD     C N N 311 
LYS CE     C N N 312 
LYS NZ     N N N 313 
LYS OXT    O N N 314 
LYS H      H N N 315 
LYS H2     H N N 316 
LYS HA     H N N 317 
LYS HB2    H N N 318 
LYS HB3    H N N 319 
LYS HG2    H N N 320 
LYS HG3    H N N 321 
LYS HD2    H N N 322 
LYS HD3    H N N 323 
LYS HE2    H N N 324 
LYS HE3    H N N 325 
LYS HZ1    H N N 326 
LYS HZ2    H N N 327 
LYS HZ3    H N N 328 
LYS HXT    H N N 329 
MET N      N N N 330 
MET CA     C N S 331 
MET C      C N N 332 
MET O      O N N 333 
MET CB     C N N 334 
MET CG     C N N 335 
MET SD     S N N 336 
MET CE     C N N 337 
MET OXT    O N N 338 
MET H      H N N 339 
MET H2     H N N 340 
MET HA     H N N 341 
MET HB2    H N N 342 
MET HB3    H N N 343 
MET HG2    H N N 344 
MET HG3    H N N 345 
MET HE1    H N N 346 
MET HE2    H N N 347 
MET HE3    H N N 348 
MET HXT    H N N 349 
PGE C1     C N N 350 
PGE O1     O N N 351 
PGE C2     C N N 352 
PGE O2     O N N 353 
PGE C3     C N N 354 
PGE C4     C N N 355 
PGE O4     O N N 356 
PGE C6     C N N 357 
PGE C5     C N N 358 
PGE O3     O N N 359 
PGE H1     H N N 360 
PGE H12    H N N 361 
PGE HO1    H N N 362 
PGE H2     H N N 363 
PGE H22    H N N 364 
PGE H3     H N N 365 
PGE H32    H N N 366 
PGE H4     H N N 367 
PGE H42    H N N 368 
PGE HO4    H N N 369 
PGE H6     H N N 370 
PGE H62    H N N 371 
PGE H5     H N N 372 
PGE H52    H N N 373 
PHE N      N N N 374 
PHE CA     C N S 375 
PHE C      C N N 376 
PHE O      O N N 377 
PHE CB     C N N 378 
PHE CG     C Y N 379 
PHE CD1    C Y N 380 
PHE CD2    C Y N 381 
PHE CE1    C Y N 382 
PHE CE2    C Y N 383 
PHE CZ     C Y N 384 
PHE OXT    O N N 385 
PHE H      H N N 386 
PHE H2     H N N 387 
PHE HA     H N N 388 
PHE HB2    H N N 389 
PHE HB3    H N N 390 
PHE HD1    H N N 391 
PHE HD2    H N N 392 
PHE HE1    H N N 393 
PHE HE2    H N N 394 
PHE HZ     H N N 395 
PHE HXT    H N N 396 
PRO N      N N N 397 
PRO CA     C N S 398 
PRO C      C N N 399 
PRO O      O N N 400 
PRO CB     C N N 401 
PRO CG     C N N 402 
PRO CD     C N N 403 
PRO OXT    O N N 404 
PRO H      H N N 405 
PRO HA     H N N 406 
PRO HB2    H N N 407 
PRO HB3    H N N 408 
PRO HG2    H N N 409 
PRO HG3    H N N 410 
PRO HD2    H N N 411 
PRO HD3    H N N 412 
PRO HXT    H N N 413 
SER N      N N N 414 
SER CA     C N S 415 
SER C      C N N 416 
SER O      O N N 417 
SER CB     C N N 418 
SER OG     O N N 419 
SER OXT    O N N 420 
SER H      H N N 421 
SER H2     H N N 422 
SER HA     H N N 423 
SER HB2    H N N 424 
SER HB3    H N N 425 
SER HG     H N N 426 
SER HXT    H N N 427 
THR N      N N N 428 
THR CA     C N S 429 
THR C      C N N 430 
THR O      O N N 431 
THR CB     C N R 432 
THR OG1    O N N 433 
THR CG2    C N N 434 
THR OXT    O N N 435 
THR H      H N N 436 
THR H2     H N N 437 
THR HA     H N N 438 
THR HB     H N N 439 
THR HG1    H N N 440 
THR HG21   H N N 441 
THR HG22   H N N 442 
THR HG23   H N N 443 
THR HXT    H N N 444 
TRP N      N N N 445 
TRP CA     C N S 446 
TRP C      C N N 447 
TRP O      O N N 448 
TRP CB     C N N 449 
TRP CG     C Y N 450 
TRP CD1    C Y N 451 
TRP CD2    C Y N 452 
TRP NE1    N Y N 453 
TRP CE2    C Y N 454 
TRP CE3    C Y N 455 
TRP CZ2    C Y N 456 
TRP CZ3    C Y N 457 
TRP CH2    C Y N 458 
TRP OXT    O N N 459 
TRP H      H N N 460 
TRP H2     H N N 461 
TRP HA     H N N 462 
TRP HB2    H N N 463 
TRP HB3    H N N 464 
TRP HD1    H N N 465 
TRP HE1    H N N 466 
TRP HE3    H N N 467 
TRP HZ2    H N N 468 
TRP HZ3    H N N 469 
TRP HH2    H N N 470 
TRP HXT    H N N 471 
TYR N      N N N 472 
TYR CA     C N S 473 
TYR C      C N N 474 
TYR O      O N N 475 
TYR CB     C N N 476 
TYR CG     C Y N 477 
TYR CD1    C Y N 478 
TYR CD2    C Y N 479 
TYR CE1    C Y N 480 
TYR CE2    C Y N 481 
TYR CZ     C Y N 482 
TYR OH     O N N 483 
TYR OXT    O N N 484 
TYR H      H N N 485 
TYR H2     H N N 486 
TYR HA     H N N 487 
TYR HB2    H N N 488 
TYR HB3    H N N 489 
TYR HD1    H N N 490 
TYR HD2    H N N 491 
TYR HE1    H N N 492 
TYR HE2    H N N 493 
TYR HH     H N N 494 
TYR HXT    H N N 495 
VAL N      N N N 496 
VAL CA     C N S 497 
VAL C      C N N 498 
VAL O      O N N 499 
VAL CB     C N N 500 
VAL CG1    C N N 501 
VAL CG2    C N N 502 
VAL OXT    O N N 503 
VAL H      H N N 504 
VAL H2     H N N 505 
VAL HA     H N N 506 
VAL HB     H N N 507 
VAL HG11   H N N 508 
VAL HG12   H N N 509 
VAL HG13   H N N 510 
VAL HG21   H N N 511 
VAL HG22   H N N 512 
VAL HG23   H N N 513 
VAL HXT    H N N 514 
# 
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  
FAD PA    O1A    doub N N 83  
FAD PA    O2A    sing N N 84  
FAD PA    O5B    sing N N 85  
FAD PA    O3P    sing N N 86  
FAD O2A   HOA2   sing N N 87  
FAD O5B   C5B    sing N N 88  
FAD C5B   C4B    sing N N 89  
FAD C5B   H51A   sing N N 90  
FAD C5B   H52A   sing N N 91  
FAD C4B   O4B    sing N N 92  
FAD C4B   C3B    sing N N 93  
FAD C4B   H4B    sing N N 94  
FAD O4B   C1B    sing N N 95  
FAD C3B   O3B    sing N N 96  
FAD C3B   C2B    sing N N 97  
FAD C3B   H3B    sing N N 98  
FAD O3B   HO3A   sing N N 99  
FAD C2B   O2B    sing N N 100 
FAD C2B   C1B    sing N N 101 
FAD C2B   H2B    sing N N 102 
FAD O2B   HO2A   sing N N 103 
FAD C1B   N9A    sing N N 104 
FAD C1B   H1B    sing N N 105 
FAD N9A   C8A    sing Y N 106 
FAD N9A   C4A    sing Y N 107 
FAD C8A   N7A    doub Y N 108 
FAD C8A   H8A    sing N N 109 
FAD N7A   C5A    sing Y N 110 
FAD C5A   C6A    sing Y N 111 
FAD C5A   C4A    doub Y N 112 
FAD C6A   N6A    sing N N 113 
FAD C6A   N1A    doub Y N 114 
FAD N6A   H61A   sing N N 115 
FAD N6A   H62A   sing N N 116 
FAD N1A   C2A    sing Y N 117 
FAD C2A   N3A    doub Y N 118 
FAD C2A   H2A    sing N N 119 
FAD N3A   C4A    sing Y N 120 
FAD N1    C2     sing N N 121 
FAD N1    C10    doub N N 122 
FAD C2    O2     doub N N 123 
FAD C2    N3     sing N N 124 
FAD N3    C4     sing N N 125 
FAD N3    HN3    sing N N 126 
FAD C4    O4     doub N N 127 
FAD C4    C4X    sing N N 128 
FAD C4X   N5     doub N N 129 
FAD C4X   C10    sing N N 130 
FAD N5    C5X    sing N N 131 
FAD C5X   C6     doub Y N 132 
FAD C5X   C9A    sing Y N 133 
FAD C6    C7     sing Y N 134 
FAD C6    H6     sing N N 135 
FAD C7    C7M    sing N N 136 
FAD C7    C8     doub Y N 137 
FAD C7M   HM71   sing N N 138 
FAD C7M   HM72   sing N N 139 
FAD C7M   HM73   sing N N 140 
FAD C8    C8M    sing N N 141 
FAD C8    C9     sing Y N 142 
FAD C8M   HM81   sing N N 143 
FAD C8M   HM82   sing N N 144 
FAD C8M   HM83   sing N N 145 
FAD C9    C9A    doub Y N 146 
FAD C9    H9     sing N N 147 
FAD C9A   N10    sing N N 148 
FAD N10   C10    sing N N 149 
FAD N10   "C1'"  sing N N 150 
FAD "C1'" "C2'"  sing N N 151 
FAD "C1'" "H1'1" sing N N 152 
FAD "C1'" "H1'2" sing N N 153 
FAD "C2'" "O2'"  sing N N 154 
FAD "C2'" "C3'"  sing N N 155 
FAD "C2'" "H2'"  sing N N 156 
FAD "O2'" "HO2'" sing N N 157 
FAD "C3'" "O3'"  sing N N 158 
FAD "C3'" "C4'"  sing N N 159 
FAD "C3'" "H3'"  sing N N 160 
FAD "O3'" "HO3'" sing N N 161 
FAD "C4'" "O4'"  sing N N 162 
FAD "C4'" "C5'"  sing N N 163 
FAD "C4'" "H4'"  sing N N 164 
FAD "O4'" "HO4'" sing N N 165 
FAD "C5'" "O5'"  sing N N 166 
FAD "C5'" "H5'1" sing N N 167 
FAD "C5'" "H5'2" sing N N 168 
FAD "O5'" P      sing N N 169 
FAD P     O1P    doub N N 170 
FAD P     O2P    sing N N 171 
FAD P     O3P    sing N N 172 
FAD O2P   HOP2   sing N N 173 
GLN N     CA     sing N N 174 
GLN N     H      sing N N 175 
GLN N     H2     sing N N 176 
GLN CA    C      sing N N 177 
GLN CA    CB     sing N N 178 
GLN CA    HA     sing N N 179 
GLN C     O      doub N N 180 
GLN C     OXT    sing N N 181 
GLN CB    CG     sing N N 182 
GLN CB    HB2    sing N N 183 
GLN CB    HB3    sing N N 184 
GLN CG    CD     sing N N 185 
GLN CG    HG2    sing N N 186 
GLN CG    HG3    sing N N 187 
GLN CD    OE1    doub N N 188 
GLN CD    NE2    sing N N 189 
GLN NE2   HE21   sing N N 190 
GLN NE2   HE22   sing N N 191 
GLN OXT   HXT    sing N N 192 
GLU N     CA     sing N N 193 
GLU N     H      sing N N 194 
GLU N     H2     sing N N 195 
GLU CA    C      sing N N 196 
GLU CA    CB     sing N N 197 
GLU CA    HA     sing N N 198 
GLU C     O      doub N N 199 
GLU C     OXT    sing N N 200 
GLU CB    CG     sing N N 201 
GLU CB    HB2    sing N N 202 
GLU CB    HB3    sing N N 203 
GLU CG    CD     sing N N 204 
GLU CG    HG2    sing N N 205 
GLU CG    HG3    sing N N 206 
GLU CD    OE1    doub N N 207 
GLU CD    OE2    sing N N 208 
GLU OE2   HE2    sing N N 209 
GLU OXT   HXT    sing N N 210 
GLY N     CA     sing N N 211 
GLY N     H      sing N N 212 
GLY N     H2     sing N N 213 
GLY CA    C      sing N N 214 
GLY CA    HA2    sing N N 215 
GLY CA    HA3    sing N N 216 
GLY C     O      doub N N 217 
GLY C     OXT    sing N N 218 
GLY OXT   HXT    sing N N 219 
GOL C1    O1     sing N N 220 
GOL C1    C2     sing N N 221 
GOL C1    H11    sing N N 222 
GOL C1    H12    sing N N 223 
GOL O1    HO1    sing N N 224 
GOL C2    O2     sing N N 225 
GOL C2    C3     sing N N 226 
GOL C2    H2     sing N N 227 
GOL O2    HO2    sing N N 228 
GOL C3    O3     sing N N 229 
GOL C3    H31    sing N N 230 
GOL C3    H32    sing N N 231 
GOL O3    HO3    sing N N 232 
HIS N     CA     sing N N 233 
HIS N     H      sing N N 234 
HIS N     H2     sing N N 235 
HIS CA    C      sing N N 236 
HIS CA    CB     sing N N 237 
HIS CA    HA     sing N N 238 
HIS C     O      doub N N 239 
HIS C     OXT    sing N N 240 
HIS CB    CG     sing N N 241 
HIS CB    HB2    sing N N 242 
HIS CB    HB3    sing N N 243 
HIS CG    ND1    sing Y N 244 
HIS CG    CD2    doub Y N 245 
HIS ND1   CE1    doub Y N 246 
HIS ND1   HD1    sing N N 247 
HIS CD2   NE2    sing Y N 248 
HIS CD2   HD2    sing N N 249 
HIS CE1   NE2    sing Y N 250 
HIS CE1   HE1    sing N N 251 
HIS NE2   HE2    sing N N 252 
HIS OXT   HXT    sing N N 253 
HOH O     H1     sing N N 254 
HOH O     H2     sing N N 255 
ILE N     CA     sing N N 256 
ILE N     H      sing N N 257 
ILE N     H2     sing N N 258 
ILE CA    C      sing N N 259 
ILE CA    CB     sing N N 260 
ILE CA    HA     sing N N 261 
ILE C     O      doub N N 262 
ILE C     OXT    sing N N 263 
ILE CB    CG1    sing N N 264 
ILE CB    CG2    sing N N 265 
ILE CB    HB     sing N N 266 
ILE CG1   CD1    sing N N 267 
ILE CG1   HG12   sing N N 268 
ILE CG1   HG13   sing N N 269 
ILE CG2   HG21   sing N N 270 
ILE CG2   HG22   sing N N 271 
ILE CG2   HG23   sing N N 272 
ILE CD1   HD11   sing N N 273 
ILE CD1   HD12   sing N N 274 
ILE CD1   HD13   sing N N 275 
ILE OXT   HXT    sing N N 276 
LEU N     CA     sing N N 277 
LEU N     H      sing N N 278 
LEU N     H2     sing N N 279 
LEU CA    C      sing N N 280 
LEU CA    CB     sing N N 281 
LEU CA    HA     sing N N 282 
LEU C     O      doub N N 283 
LEU C     OXT    sing N N 284 
LEU CB    CG     sing N N 285 
LEU CB    HB2    sing N N 286 
LEU CB    HB3    sing N N 287 
LEU CG    CD1    sing N N 288 
LEU CG    CD2    sing N N 289 
LEU CG    HG     sing N N 290 
LEU CD1   HD11   sing N N 291 
LEU CD1   HD12   sing N N 292 
LEU CD1   HD13   sing N N 293 
LEU CD2   HD21   sing N N 294 
LEU CD2   HD22   sing N N 295 
LEU CD2   HD23   sing N N 296 
LEU OXT   HXT    sing N N 297 
LYS N     CA     sing N N 298 
LYS N     H      sing N N 299 
LYS N     H2     sing N N 300 
LYS CA    C      sing N N 301 
LYS CA    CB     sing N N 302 
LYS CA    HA     sing N N 303 
LYS C     O      doub N N 304 
LYS C     OXT    sing N N 305 
LYS CB    CG     sing N N 306 
LYS CB    HB2    sing N N 307 
LYS CB    HB3    sing N N 308 
LYS CG    CD     sing N N 309 
LYS CG    HG2    sing N N 310 
LYS CG    HG3    sing N N 311 
LYS CD    CE     sing N N 312 
LYS CD    HD2    sing N N 313 
LYS CD    HD3    sing N N 314 
LYS CE    NZ     sing N N 315 
LYS CE    HE2    sing N N 316 
LYS CE    HE3    sing N N 317 
LYS NZ    HZ1    sing N N 318 
LYS NZ    HZ2    sing N N 319 
LYS NZ    HZ3    sing N N 320 
LYS OXT   HXT    sing N N 321 
MET N     CA     sing N N 322 
MET N     H      sing N N 323 
MET N     H2     sing N N 324 
MET CA    C      sing N N 325 
MET CA    CB     sing N N 326 
MET CA    HA     sing N N 327 
MET C     O      doub N N 328 
MET C     OXT    sing N N 329 
MET CB    CG     sing N N 330 
MET CB    HB2    sing N N 331 
MET CB    HB3    sing N N 332 
MET CG    SD     sing N N 333 
MET CG    HG2    sing N N 334 
MET CG    HG3    sing N N 335 
MET SD    CE     sing N N 336 
MET CE    HE1    sing N N 337 
MET CE    HE2    sing N N 338 
MET CE    HE3    sing N N 339 
MET OXT   HXT    sing N N 340 
PGE C1    O1     sing N N 341 
PGE C1    C2     sing N N 342 
PGE C1    H1     sing N N 343 
PGE C1    H12    sing N N 344 
PGE O1    HO1    sing N N 345 
PGE C2    O2     sing N N 346 
PGE C2    H2     sing N N 347 
PGE C2    H22    sing N N 348 
PGE O2    C3     sing N N 349 
PGE C3    C4     sing N N 350 
PGE C3    H3     sing N N 351 
PGE C3    H32    sing N N 352 
PGE C4    O3     sing N N 353 
PGE C4    H4     sing N N 354 
PGE C4    H42    sing N N 355 
PGE O4    C6     sing N N 356 
PGE O4    HO4    sing N N 357 
PGE C6    C5     sing N N 358 
PGE C6    H6     sing N N 359 
PGE C6    H62    sing N N 360 
PGE C5    O3     sing N N 361 
PGE C5    H5     sing N N 362 
PGE C5    H52    sing N N 363 
PHE N     CA     sing N N 364 
PHE N     H      sing N N 365 
PHE N     H2     sing N N 366 
PHE CA    C      sing N N 367 
PHE CA    CB     sing N N 368 
PHE CA    HA     sing N N 369 
PHE C     O      doub N N 370 
PHE C     OXT    sing N N 371 
PHE CB    CG     sing N N 372 
PHE CB    HB2    sing N N 373 
PHE CB    HB3    sing N N 374 
PHE CG    CD1    doub Y N 375 
PHE CG    CD2    sing Y N 376 
PHE CD1   CE1    sing Y N 377 
PHE CD1   HD1    sing N N 378 
PHE CD2   CE2    doub Y N 379 
PHE CD2   HD2    sing N N 380 
PHE CE1   CZ     doub Y N 381 
PHE CE1   HE1    sing N N 382 
PHE CE2   CZ     sing Y N 383 
PHE CE2   HE2    sing N N 384 
PHE CZ    HZ     sing N N 385 
PHE OXT   HXT    sing N N 386 
PRO N     CA     sing N N 387 
PRO N     CD     sing N N 388 
PRO N     H      sing N N 389 
PRO CA    C      sing N N 390 
PRO CA    CB     sing N N 391 
PRO CA    HA     sing N N 392 
PRO C     O      doub N N 393 
PRO C     OXT    sing N N 394 
PRO CB    CG     sing N N 395 
PRO CB    HB2    sing N N 396 
PRO CB    HB3    sing N N 397 
PRO CG    CD     sing N N 398 
PRO CG    HG2    sing N N 399 
PRO CG    HG3    sing N N 400 
PRO CD    HD2    sing N N 401 
PRO CD    HD3    sing N N 402 
PRO OXT   HXT    sing N N 403 
SER N     CA     sing N N 404 
SER N     H      sing N N 405 
SER N     H2     sing N N 406 
SER CA    C      sing N N 407 
SER CA    CB     sing N N 408 
SER CA    HA     sing N N 409 
SER C     O      doub N N 410 
SER C     OXT    sing N N 411 
SER CB    OG     sing N N 412 
SER CB    HB2    sing N N 413 
SER CB    HB3    sing N N 414 
SER OG    HG     sing N N 415 
SER OXT   HXT    sing N N 416 
THR N     CA     sing N N 417 
THR N     H      sing N N 418 
THR N     H2     sing N N 419 
THR CA    C      sing N N 420 
THR CA    CB     sing N N 421 
THR CA    HA     sing N N 422 
THR C     O      doub N N 423 
THR C     OXT    sing N N 424 
THR CB    OG1    sing N N 425 
THR CB    CG2    sing N N 426 
THR CB    HB     sing N N 427 
THR OG1   HG1    sing N N 428 
THR CG2   HG21   sing N N 429 
THR CG2   HG22   sing N N 430 
THR CG2   HG23   sing N N 431 
THR OXT   HXT    sing N N 432 
TRP N     CA     sing N N 433 
TRP N     H      sing N N 434 
TRP N     H2     sing N N 435 
TRP CA    C      sing N N 436 
TRP CA    CB     sing N N 437 
TRP CA    HA     sing N N 438 
TRP C     O      doub N N 439 
TRP C     OXT    sing N N 440 
TRP CB    CG     sing N N 441 
TRP CB    HB2    sing N N 442 
TRP CB    HB3    sing N N 443 
TRP CG    CD1    doub Y N 444 
TRP CG    CD2    sing Y N 445 
TRP CD1   NE1    sing Y N 446 
TRP CD1   HD1    sing N N 447 
TRP CD2   CE2    doub Y N 448 
TRP CD2   CE3    sing Y N 449 
TRP NE1   CE2    sing Y N 450 
TRP NE1   HE1    sing N N 451 
TRP CE2   CZ2    sing Y N 452 
TRP CE3   CZ3    doub Y N 453 
TRP CE3   HE3    sing N N 454 
TRP CZ2   CH2    doub Y N 455 
TRP CZ2   HZ2    sing N N 456 
TRP CZ3   CH2    sing Y N 457 
TRP CZ3   HZ3    sing N N 458 
TRP CH2   HH2    sing N N 459 
TRP OXT   HXT    sing N N 460 
TYR N     CA     sing N N 461 
TYR N     H      sing N N 462 
TYR N     H2     sing N N 463 
TYR CA    C      sing N N 464 
TYR CA    CB     sing N N 465 
TYR CA    HA     sing N N 466 
TYR C     O      doub N N 467 
TYR C     OXT    sing N N 468 
TYR CB    CG     sing N N 469 
TYR CB    HB2    sing N N 470 
TYR CB    HB3    sing N N 471 
TYR CG    CD1    doub Y N 472 
TYR CG    CD2    sing Y N 473 
TYR CD1   CE1    sing Y N 474 
TYR CD1   HD1    sing N N 475 
TYR CD2   CE2    doub Y N 476 
TYR CD2   HD2    sing N N 477 
TYR CE1   CZ     doub Y N 478 
TYR CE1   HE1    sing N N 479 
TYR CE2   CZ     sing Y N 480 
TYR CE2   HE2    sing N N 481 
TYR CZ    OH     sing N N 482 
TYR OH    HH     sing N N 483 
TYR OXT   HXT    sing N N 484 
VAL N     CA     sing N N 485 
VAL N     H      sing N N 486 
VAL N     H2     sing N N 487 
VAL CA    C      sing N N 488 
VAL CA    CB     sing N N 489 
VAL CA    HA     sing N N 490 
VAL C     O      doub N N 491 
VAL C     OXT    sing N N 492 
VAL CB    CG1    sing N N 493 
VAL CB    CG2    sing N N 494 
VAL CB    HB     sing N N 495 
VAL CG1   HG11   sing N N 496 
VAL CG1   HG12   sing N N 497 
VAL CG1   HG13   sing N N 498 
VAL CG2   HG21   sing N N 499 
VAL CG2   HG22   sing N N 500 
VAL CG2   HG23   sing N N 501 
VAL OXT   HXT    sing N N 502 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministerio de Ciencia e Innovacion (MCIN)' Spain TED2021-130803B-I00            1 
'Other government'                          Spain 'Biologia Estructural E35_23R' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RPG 
_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]   0.012421 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010237 
_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]   0.014696 
_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 
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     . THR A 1 24  ? 4.251  36.909  37.696  1.00 48.31  ? 3    THR A N     1 
ATOM   2    C CA    . THR A 1 24  ? 5.094  36.346  38.780  1.00 46.06  ? 3    THR A CA    1 
ATOM   3    C C     . THR A 1 24  ? 6.554  36.542  38.380  1.00 41.39  ? 3    THR A C     1 
ATOM   4    O O     . THR A 1 24  ? 6.910  36.655  37.188  1.00 30.40  ? 3    THR A O     1 
ATOM   5    C CB    . THR A 1 24  ? 4.742  34.887  39.057  1.00 52.83  ? 3    THR A CB    1 
ATOM   6    O OG1   . THR A 1 24  ? 3.332  34.967  39.163  1.00 66.31  ? 3    THR A OG1   1 
ATOM   7    C CG2   . THR A 1 24  ? 5.284  34.331  40.362  1.00 46.35  ? 3    THR A CG2   1 
ATOM   8    N N     . ALA A 1 25  ? 7.366  36.723  39.421  1.00 34.09  ? 4    ALA A N     1 
ATOM   9    C CA    . ALA A 1 25  ? 8.705  37.253  39.261  1.00 36.90  ? 4    ALA A CA    1 
ATOM   10   C C     . ALA A 1 25  ? 9.725  36.180  39.620  1.00 34.24  ? 4    ALA A C     1 
ATOM   11   O O     . ALA A 1 25  ? 9.558  35.436  40.587  1.00 36.95  ? 4    ALA A O     1 
ATOM   12   C CB    . ALA A 1 25  ? 8.876  38.517  40.092  1.00 39.41  ? 4    ALA A CB    1 
ATOM   13   N N     . PHE A 1 26  ? 10.765 36.110  38.791  1.00 28.11  ? 5    PHE A N     1 
ATOM   14   C CA    . PHE A 1 26  ? 11.822 35.125  38.905  1.00 28.18  ? 5    PHE A CA    1 
ATOM   15   C C     . PHE A 1 26  ? 13.150 35.835  38.735  1.00 25.54  ? 5    PHE A C     1 
ATOM   16   O O     . PHE A 1 26  ? 13.162 36.977  38.295  1.00 25.72  ? 5    PHE A O     1 
ATOM   17   C CB    . PHE A 1 26  ? 11.579 34.135  37.766  1.00 27.00  ? 5    PHE A CB    1 
ATOM   18   C CG    . PHE A 1 26  ? 10.319 33.314  37.965  1.00 26.27  ? 5    PHE A CG    1 
ATOM   19   C CD1   . PHE A 1 26  ? 10.349 32.146  38.728  1.00 26.47  ? 5    PHE A CD1   1 
ATOM   20   C CD2   . PHE A 1 26  ? 9.118  33.697  37.371  1.00 27.79  ? 5    PHE A CD2   1 
ATOM   21   C CE1   . PHE A 1 26  ? 9.176  31.420  38.936  1.00 29.52  ? 5    PHE A CE1   1 
ATOM   22   C CE2   . PHE A 1 26  ? 7.965  32.954  37.558  1.00 28.42  ? 5    PHE A CE2   1 
ATOM   23   C CZ    . PHE A 1 26  ? 7.987  31.828  38.357  1.00 29.88  ? 5    PHE A CZ    1 
ATOM   24   N N     . ASP A 1 27  ? 14.249 35.161  39.079  1.00 25.33  ? 6    ASP A N     1 
ATOM   25   C CA    . ASP A 1 27  ? 15.571 35.619  38.701  1.00 26.07  ? 6    ASP A CA    1 
ATOM   26   C C     . ASP A 1 27  ? 15.892 35.275  37.243  1.00 26.00  ? 6    ASP A C     1 
ATOM   27   O O     . ASP A 1 27  ? 16.416 36.125  36.511  1.00 24.10  ? 6    ASP A O     1 
ATOM   28   C CB    . ASP A 1 27  ? 16.576 35.061  39.685  1.00 30.44  ? 6    ASP A CB    1 
ATOM   29   C CG    . ASP A 1 27  ? 16.333 35.658  41.065  1.00 32.66  ? 6    ASP A CG    1 
ATOM   30   O OD1   . ASP A 1 27  ? 16.353 36.888  41.157  1.00 30.85  ? 6    ASP A OD1   1 
ATOM   31   O OD2   . ASP A 1 27  ? 16.020 34.900  41.973  1.00 32.75  ? 6    ASP A OD2   1 
ATOM   32   N N     . TYR A 1 28  ? 15.622 34.008  36.877  1.00 24.77  ? 7    TYR A N     1 
ATOM   33   C CA    . TYR A 1 28  ? 15.839 33.483  35.529  1.00 24.15  ? 7    TYR A CA    1 
ATOM   34   C C     . TYR A 1 28  ? 14.537 32.919  34.984  1.00 22.34  ? 7    TYR A C     1 
ATOM   35   O O     . TYR A 1 28  ? 13.875 32.139  35.677  1.00 24.04  ? 7    TYR A O     1 
ATOM   36   C CB    . TYR A 1 28  ? 16.890 32.379  35.511  1.00 21.64  ? 7    TYR A CB    1 
ATOM   37   C CG    . TYR A 1 28  ? 18.252 32.870  35.984  1.00 24.88  ? 7    TYR A CG    1 
ATOM   38   C CD1   . TYR A 1 28  ? 19.056 33.594  35.122  1.00 26.77  ? 7    TYR A CD1   1 
ATOM   39   C CD2   . TYR A 1 28  ? 18.697 32.677  37.291  1.00 26.80  ? 7    TYR A CD2   1 
ATOM   40   C CE1   . TYR A 1 28  ? 20.282 34.071  35.518  1.00 28.53  ? 7    TYR A CE1   1 
ATOM   41   C CE2   . TYR A 1 28  ? 19.930 33.153  37.703  1.00 26.45  ? 7    TYR A CE2   1 
ATOM   42   C CZ    . TYR A 1 28  ? 20.710 33.861  36.809  1.00 27.55  ? 7    TYR A CZ    1 
ATOM   43   O OH    . TYR A 1 28  ? 21.924 34.387  37.087  1.00 30.41  ? 7    TYR A OH    1 
ATOM   44   N N     . VAL A 1 29  ? 14.203 33.312  33.737  1.00 21.78  ? 8    VAL A N     1 
ATOM   45   C CA    . VAL A 1 29  ? 13.102 32.722  32.993  1.00 21.45  ? 8    VAL A CA    1 
ATOM   46   C C     . VAL A 1 29  ? 13.704 31.995  31.789  1.00 22.78  ? 8    VAL A C     1 
ATOM   47   O O     . VAL A 1 29  ? 14.288 32.647  30.914  1.00 18.94  ? 8    VAL A O     1 
ATOM   48   C CB    . VAL A 1 29  ? 12.070 33.766  32.537  1.00 23.09  ? 8    VAL A CB    1 
ATOM   49   C CG1   . VAL A 1 29  ? 10.972 33.149  31.668  1.00 23.17  ? 8    VAL A CG1   1 
ATOM   50   C CG2   . VAL A 1 29  ? 11.444 34.510  33.708  1.00 22.78  ? 8    VAL A CG2   1 
ATOM   51   N N     . ILE A 1 30  ? 13.579 30.655  31.767  1.00 21.31  ? 9    ILE A N     1 
ATOM   52   C CA    . ILE A 1 30  ? 14.039 29.843  30.645  1.00 21.58  ? 9    ILE A CA    1 
ATOM   53   C C     . ILE A 1 30  ? 12.842 29.428  29.800  1.00 21.47  ? 9    ILE A C     1 
ATOM   54   O O     . ILE A 1 30  ? 11.936 28.790  30.319  1.00 20.92  ? 9    ILE A O     1 
ATOM   55   C CB    . ILE A 1 30  ? 14.814 28.609  31.121  1.00 21.93  ? 9    ILE A CB    1 
ATOM   56   C CG1   . ILE A 1 30  ? 15.978 29.019  32.048  1.00 24.84  ? 9    ILE A CG1   1 
ATOM   57   C CG2   . ILE A 1 30  ? 15.295 27.786  29.905  1.00 22.51  ? 9    ILE A CG2   1 
ATOM   58   C CD1   . ILE A 1 30  ? 16.350 27.945  33.064  1.00 28.02  ? 9    ILE A CD1   1 
ATOM   59   N N     . VAL A 1 31  ? 12.901 29.714  28.489  1.00 18.29  ? 10   VAL A N     1 
ATOM   60   C CA    . VAL A 1 31  ? 11.846 29.330  27.570  1.00 19.02  ? 10   VAL A CA    1 
ATOM   61   C C     . VAL A 1 31  ? 12.269 28.064  26.840  1.00 19.24  ? 10   VAL A C     1 
ATOM   62   O O     . VAL A 1 31  ? 13.234 28.093  26.073  1.00 17.60  ? 10   VAL A O     1 
ATOM   63   C CB    . VAL A 1 31  ? 11.547 30.436  26.557  1.00 20.49  ? 10   VAL A CB    1 
ATOM   64   C CG1   . VAL A 1 31  ? 10.425 30.044  25.596  1.00 20.45  ? 10   VAL A CG1   1 
ATOM   65   C CG2   . VAL A 1 31  ? 11.263 31.754  27.266  1.00 23.04  ? 10   VAL A CG2   1 
ATOM   66   N N     . GLY A 1 32  ? 11.547 26.977  27.119  1.00 18.61  ? 11   GLY A N     1 
ATOM   67   C CA    . GLY A 1 32  ? 11.619 25.737  26.362  1.00 17.83  ? 11   GLY A CA    1 
ATOM   68   C C     . GLY A 1 32  ? 12.294 24.656  27.181  1.00 16.60  ? 11   GLY A C     1 
ATOM   69   O O     . GLY A 1 32  ? 13.486 24.746  27.509  1.00 17.12  ? 11   GLY A O     1 
ATOM   70   N N     . ALA A 1 33  ? 11.518 23.609  27.478  1.00 17.30  ? 12   ALA A N     1 
ATOM   71   C CA    . ALA A 1 33  ? 11.981 22.517  28.324  1.00 17.91  ? 12   ALA A CA    1 
ATOM   72   C C     . ALA A 1 33  ? 12.532 21.391  27.453  1.00 17.65  ? 12   ALA A C     1 
ATOM   73   O O     . ALA A 1 33  ? 12.150 20.248  27.604  1.00 17.60  ? 12   ALA A O     1 
ATOM   74   C CB    . ALA A 1 33  ? 10.845 22.023  29.179  1.00 18.03  ? 12   ALA A CB    1 
ATOM   75   N N     . GLY A 1 34  ? 13.501 21.708  26.606  1.00 18.57  ? 13   GLY A N     1 
ATOM   76   C CA    . GLY A 1 34  ? 14.071 20.742  25.680  1.00 17.37  ? 13   GLY A CA    1 
ATOM   77   C C     . GLY A 1 34  ? 15.424 20.257  26.171  1.00 18.35  ? 13   GLY A C     1 
ATOM   78   O O     . GLY A 1 34  ? 15.753 20.318  27.374  1.00 18.10  ? 13   GLY A O     1 
ATOM   79   N N     . SER A 1 35  ? 16.226 19.790  25.214  1.00 16.64  ? 14   SER A N     1 
ATOM   80   C CA    . SER A 1 35  ? 17.523 19.237  25.554  1.00 18.37  ? 14   SER A CA    1 
ATOM   81   C C     . SER A 1 35  ? 18.333 20.229  26.393  1.00 19.32  ? 14   SER A C     1 
ATOM   82   O O     . SER A 1 35  ? 18.840 19.871  27.461  1.00 19.49  ? 14   SER A O     1 
ATOM   83   C CB    . SER A 1 35  ? 18.287 18.849  24.308  1.00 18.28  ? 14   SER A CB    1 
ATOM   84   O OG    . SER A 1 35  ? 17.669 17.801  23.581  1.00 17.59  ? 14   SER A OG    1 
ATOM   85   N N     . ALA A 1 36  ? 18.470 21.470  25.892  1.00 20.11  ? 15   ALA A N     1 
ATOM   86   C CA    . ALA A 1 36  ? 19.270 22.479  26.576  1.00 18.38  ? 15   ALA A CA    1 
ATOM   87   C C     . ALA A 1 36  ? 18.540 23.056  27.793  1.00 20.01  ? 15   ALA A C     1 
ATOM   88   O O     . ALA A 1 36  ? 19.178 23.280  28.821  1.00 18.28  ? 15   ALA A O     1 
ATOM   89   C CB    . ALA A 1 36  ? 19.698 23.563  25.626  1.00 18.42  ? 15   ALA A CB    1 
ATOM   90   N N     . GLY A 1 37  ? 17.232 23.348  27.650  1.00 19.02  ? 16   GLY A N     1 
ATOM   91   C CA    . GLY A 1 37  ? 16.468 24.084  28.651  1.00 16.91  ? 16   GLY A CA    1 
ATOM   92   C C     . GLY A 1 37  ? 16.290 23.280  29.936  1.00 18.60  ? 16   GLY A C     1 
ATOM   93   O O     . GLY A 1 37  ? 16.324 23.837  31.038  1.00 16.68  ? 16   GLY A O     1 
ATOM   94   N N     . CYS A 1 38  ? 16.120 21.956  29.798  1.00 18.65  ? 17   CYS A N     1 
ATOM   95   C CA    . CYS A 1 38  ? 16.068 21.072  30.956  1.00 19.01  ? 17   CYS A CA    1 
ATOM   96   C C     . CYS A 1 38  ? 17.378 21.164  31.762  1.00 21.94  ? 17   CYS A C     1 
ATOM   97   O O     . CYS A 1 38  ? 17.349 21.272  33.006  1.00 21.16  ? 17   CYS A O     1 
ATOM   98   C CB    . CYS A 1 38  ? 15.756 19.624  30.579  1.00 19.47  ? 17   CYS A CB    1 
ATOM   99   S SG    . CYS A 1 38  ? 14.027 19.325  30.136  1.00 22.07  ? 17   CYS A SG    1 
ATOM   100  N N     . VAL A 1 39  ? 18.518 21.126  31.052  1.00 21.75  ? 18   VAL A N     1 
ATOM   101  C CA    . VAL A 1 39  ? 19.813 21.165  31.706  1.00 22.35  ? 18   VAL A CA    1 
ATOM   102  C C     . VAL A 1 39  ? 19.915 22.481  32.475  1.00 22.54  ? 18   VAL A C     1 
ATOM   103  O O     . VAL A 1 39  ? 20.229 22.508  33.660  1.00 18.96  ? 18   VAL A O     1 
ATOM   104  C CB    . VAL A 1 39  ? 20.985 21.039  30.718  1.00 22.68  ? 18   VAL A CB    1 
ATOM   105  C CG1   . VAL A 1 39  ? 22.309 21.310  31.406  1.00 24.58  ? 18   VAL A CG1   1 
ATOM   106  C CG2   . VAL A 1 39  ? 21.002 19.698  30.000  1.00 22.10  ? 18   VAL A CG2   1 
ATOM   107  N N     . LEU A 1 40  ? 19.604 23.581  31.788  1.00 23.23  ? 19   LEU A N     1 
ATOM   108  C CA    . LEU A 1 40  ? 19.780 24.902  32.356  1.00 25.14  ? 19   LEU A CA    1 
ATOM   109  C C     . LEU A 1 40  ? 18.848 25.144  33.557  1.00 25.11  ? 19   LEU A C     1 
ATOM   110  O O     . LEU A 1 40  ? 19.248 25.755  34.542  1.00 23.63  ? 19   LEU A O     1 
ATOM   111  C CB    . LEU A 1 40  ? 19.627 25.903  31.210  1.00 28.04  ? 19   LEU A CB    1 
ATOM   112  C CG    . LEU A 1 40  ? 20.280 27.266  31.454  1.00 35.55  ? 19   LEU A CG    1 
ATOM   113  C CD1   . LEU A 1 40  ? 21.823 27.209  31.486  1.00 37.53  ? 19   LEU A CD1   1 
ATOM   114  C CD2   . LEU A 1 40  ? 19.830 28.249  30.413  1.00 36.53  ? 19   LEU A CD2   1 
ATOM   115  N N     . ALA A 1 41  ? 17.619 24.633  33.533  1.00 24.97  ? 20   ALA A N     1 
ATOM   116  C CA    . ALA A 1 41  ? 16.697 24.806  34.650  1.00 26.55  ? 20   ALA A CA    1 
ATOM   117  C C     . ALA A 1 41  ? 17.211 24.079  35.888  1.00 26.53  ? 20   ALA A C     1 
ATOM   118  O O     . ALA A 1 41  ? 17.196 24.625  37.009  1.00 22.07  ? 20   ALA A O     1 
ATOM   119  C CB    . ALA A 1 41  ? 15.308 24.331  34.258  1.00 31.51  ? 20   ALA A CB    1 
ATOM   120  N N     . ALA A 1 42  ? 17.718 22.867  35.655  1.00 25.23  ? 21   ALA A N     1 
ATOM   121  C CA    . ALA A 1 42  ? 18.244 22.039  36.719  1.00 26.66  ? 21   ALA A CA    1 
ATOM   122  C C     . ALA A 1 42  ? 19.476 22.715  37.317  1.00 27.74  ? 21   ALA A C     1 
ATOM   123  O O     . ALA A 1 42  ? 19.558 22.877  38.530  1.00 27.26  ? 21   ALA A O     1 
ATOM   124  C CB    . ALA A 1 42  ? 18.581 20.663  36.204  1.00 28.58  ? 21   ALA A CB    1 
ATOM   125  N N     . ARG A 1 43  ? 20.407 23.133  36.460  1.00 23.56  ? 22   ARG A N     1 
ATOM   126  C CA    . ARG A 1 43  ? 21.679 23.672  36.918  1.00 26.05  ? 22   ARG A CA    1 
ATOM   127  C C     . ARG A 1 43  ? 21.475 25.004  37.646  1.00 27.26  ? 22   ARG A C     1 
ATOM   128  O O     . ARG A 1 43  ? 22.050 25.212  38.714  1.00 25.95  ? 22   ARG A O     1 
ATOM   129  C CB    . ARG A 1 43  ? 22.720 23.848  35.805  1.00 25.79  ? 22   ARG A CB    1 
ATOM   130  C CG    . ARG A 1 43  ? 23.214 22.557  35.172  1.00 26.71  ? 22   ARG A CG    1 
ATOM   131  C CD    . ARG A 1 43  ? 23.653 21.534  36.204  1.00 25.78  ? 22   ARG A CD    1 
ATOM   132  N NE    . ARG A 1 43  ? 24.360 20.424  35.574  1.00 24.67  ? 22   ARG A NE    1 
ATOM   133  C CZ    . ARG A 1 43  ? 24.665 19.310  36.177  1.00 25.30  ? 22   ARG A CZ    1 
ATOM   134  N NH1   . ARG A 1 43  ? 24.342 19.142  37.449  1.00 25.56  ? 22   ARG A NH1   1 
ATOM   135  N NH2   . ARG A 1 43  ? 25.208 18.336  35.496  1.00 26.83  ? 22   ARG A NH2   1 
ATOM   136  N N     . LEU A 1 44  ? 20.653 25.898  37.089  1.00 23.18  ? 23   LEU A N     1 
ATOM   137  C CA    . LEU A 1 44  ? 20.512 27.223  37.671  1.00 26.44  ? 23   LEU A CA    1 
ATOM   138  C C     . LEU A 1 44  ? 19.774 27.156  39.006  1.00 29.83  ? 23   LEU A C     1 
ATOM   139  O O     . LEU A 1 44  ? 19.998 28.016  39.857  1.00 32.88  ? 23   LEU A O     1 
ATOM   140  C CB    . LEU A 1 44  ? 19.813 28.167  36.697  1.00 24.84  ? 23   LEU A CB    1 
ATOM   141  C CG    . LEU A 1 44  ? 20.656 28.545  35.478  1.00 24.98  ? 23   LEU A CG    1 
ATOM   142  C CD1   . LEU A 1 44  ? 19.853 29.548  34.692  1.00 25.79  ? 23   LEU A CD1   1 
ATOM   143  C CD2   . LEU A 1 44  ? 22.037 29.098  35.825  1.00 26.72  ? 23   LEU A CD2   1 
ATOM   144  N N     . SER A 1 45  ? 18.853 26.184  39.165  1.00 29.41  ? 24   SER A N     1 
ATOM   145  C CA    . SER A 1 45  ? 18.078 26.056  40.392  1.00 27.51  ? 24   SER A CA    1 
ATOM   146  C C     . SER A 1 45  ? 18.876 25.339  41.492  1.00 30.42  ? 24   SER A C     1 
ATOM   147  O O     . SER A 1 45  ? 18.385 25.184  42.605  1.00 27.44  ? 24   SER A O     1 
ATOM   148  C CB    . SER A 1 45  ? 16.749 25.388  40.139  1.00 26.46  ? 24   SER A CB    1 
ATOM   149  O OG    . SER A 1 45  ? 16.903 24.031  39.773  1.00 25.90  ? 24   SER A OG    1 
ATOM   150  N N     . GLU A 1 46  ? 20.109 24.916  41.205  1.00 29.36  ? 25   GLU A N     1 
ATOM   151  C CA    . GLU A 1 46  ? 20.926 24.271  42.212  1.00 30.91  ? 25   GLU A CA    1 
ATOM   152  C C     . GLU A 1 46  ? 21.243 25.238  43.351  1.00 36.11  ? 25   GLU A C     1 
ATOM   153  O O     . GLU A 1 46  ? 21.477 24.793  44.459  1.00 38.10  ? 25   GLU A O     1 
ATOM   154  C CB    . GLU A 1 46  ? 22.215 23.727  41.619  1.00 30.56  ? 25   GLU A CB    1 
ATOM   155  C CG    . GLU A 1 46  ? 21.964 22.460  40.816  1.00 30.54  ? 25   GLU A CG    1 
ATOM   156  C CD    . GLU A 1 46  ? 23.163 21.876  40.103  1.00 31.13  ? 25   GLU A CD    1 
ATOM   157  O OE1   . GLU A 1 46  ? 23.064 20.828  39.432  1.00 29.46  ? 25   GLU A OE1   1 
ATOM   158  O OE2   . GLU A 1 46  ? 24.213 22.494  40.226  1.00 34.74  ? 25   GLU A OE2   1 
ATOM   159  N N     . ASP A 1 47  ? 21.291 26.531  43.042  1.00 35.48  ? 26   ASP A N     1 
ATOM   160  C CA    . ASP A 1 47  ? 21.446 27.591  44.023  1.00 41.02  ? 26   ASP A CA    1 
ATOM   161  C C     . ASP A 1 47  ? 20.075 27.938  44.594  1.00 37.57  ? 26   ASP A C     1 
ATOM   162  O O     . ASP A 1 47  ? 19.267 28.586  43.938  1.00 32.77  ? 26   ASP A O     1 
ATOM   163  C CB    . ASP A 1 47  ? 22.102 28.809  43.384  1.00 44.85  ? 26   ASP A CB    1 
ATOM   164  C CG    . ASP A 1 47  ? 22.312 30.031  44.273  1.00 51.42  ? 26   ASP A CG    1 
ATOM   165  O OD1   . ASP A 1 47  ? 21.823 30.040  45.425  1.00 42.58  ? 26   ASP A OD1   1 
ATOM   166  O OD2   . ASP A 1 47  ? 22.954 30.985  43.785  1.00 55.21  ? 26   ASP A OD2   1 
ATOM   167  N N     . PRO A 1 48  ? 19.772 27.558  45.853  1.00 38.50  ? 27   PRO A N     1 
ATOM   168  C CA    . PRO A 1 48  ? 18.447 27.834  46.423  1.00 38.22  ? 27   PRO A CA    1 
ATOM   169  C C     . PRO A 1 48  ? 18.057 29.307  46.596  1.00 37.92  ? 27   PRO A C     1 
ATOM   170  O O     . PRO A 1 48  ? 16.895 29.601  46.842  1.00 47.82  ? 27   PRO A O     1 
ATOM   171  C CB    . PRO A 1 48  ? 18.508 27.078  47.765  1.00 39.03  ? 27   PRO A CB    1 
ATOM   172  C CG    . PRO A 1 48  ? 19.979 27.048  48.108  1.00 38.46  ? 27   PRO A CG    1 
ATOM   173  C CD    . PRO A 1 48  ? 20.678 26.846  46.773  1.00 39.80  ? 27   PRO A CD    1 
ATOM   174  N N     . GLU A 1 49  ? 18.991 30.244  46.409  1.00 38.38  ? 28   GLU A N     1 
ATOM   175  C CA    . GLU A 1 49  ? 18.651 31.651  46.555  1.00 42.86  ? 28   GLU A CA    1 
ATOM   176  C C     . GLU A 1 49  ? 18.224 32.263  45.222  1.00 40.25  ? 28   GLU A C     1 
ATOM   177  O O     . GLU A 1 49  ? 17.895 33.437  45.208  1.00 40.91  ? 28   GLU A O     1 
ATOM   178  C CB    . GLU A 1 49  ? 19.782 32.434  47.225  1.00 50.10  ? 28   GLU A CB    1 
ATOM   179  C CG    . GLU A 1 49  ? 19.846 32.176  48.733  1.00 60.20  ? 28   GLU A CG    1 
ATOM   180  C CD    . GLU A 1 49  ? 21.219 32.331  49.384  1.00 73.75  ? 28   GLU A CD    1 
ATOM   181  O OE1   . GLU A 1 49  ? 21.397 33.232  50.231  1.00 79.52  ? 28   GLU A OE1   1 
ATOM   182  O OE2   . GLU A 1 49  ? 22.125 31.534  49.063  1.00 81.71  ? 28   GLU A OE2   1 
ATOM   183  N N     . VAL A 1 50  ? 18.191 31.504  44.111  1.00 37.39  ? 29   VAL A N     1 
ATOM   184  C CA    . VAL A 1 50  ? 17.686 32.083  42.865  1.00 36.90  ? 29   VAL A CA    1 
ATOM   185  C C     . VAL A 1 50  ? 16.423 31.328  42.449  1.00 28.82  ? 29   VAL A C     1 
ATOM   186  O O     . VAL A 1 50  ? 16.363 30.116  42.494  1.00 35.02  ? 29   VAL A O     1 
ATOM   187  C CB    . VAL A 1 50  ? 18.694 32.163  41.698  1.00 39.93  ? 29   VAL A CB    1 
ATOM   188  C CG1   . VAL A 1 50  ? 19.986 32.873  42.094  1.00 40.69  ? 29   VAL A CG1   1 
ATOM   189  C CG2   . VAL A 1 50  ? 19.011 30.802  41.118  1.00 39.03  ? 29   VAL A CG2   1 
ATOM   190  N N     . ARG A 1 51  ? 15.423 32.062  42.009  1.00 25.35  ? 30   ARG A N     1 
ATOM   191  C CA    . ARG A 1 51  ? 14.178 31.460  41.589  1.00 30.28  ? 30   ARG A CA    1 
ATOM   192  C C     . ARG A 1 51  ? 14.195 31.362  40.060  1.00 28.17  ? 30   ARG A C     1 
ATOM   193  O O     . ARG A 1 51  ? 14.523 32.330  39.372  1.00 30.82  ? 30   ARG A O     1 
ATOM   194  C CB    . ARG A 1 51  ? 13.021 32.301  42.115  1.00 29.04  ? 30   ARG A CB    1 
ATOM   195  C CG    . ARG A 1 51  ? 11.704 31.534  42.174  1.00 32.50  ? 30   ARG A CG    1 
ATOM   196  C CD    . ARG A 1 51  ? 10.492 32.440  42.255  1.00 32.68  ? 30   ARG A CD    1 
ATOM   197  N NE    . ARG A 1 51  ? 9.225  31.698  42.289  1.00 34.07  ? 30   ARG A NE    1 
ATOM   198  C CZ    . ARG A 1 51  ? 8.001  32.159  41.967  1.00 39.61  ? 30   ARG A CZ    1 
ATOM   199  N NH1   . ARG A 1 51  ? 7.842  33.404  41.553  1.00 40.60  ? 30   ARG A NH1   1 
ATOM   200  N NH2   . ARG A 1 51  ? 6.938  31.359  42.032  1.00 39.88  ? 30   ARG A NH2   1 
ATOM   201  N N     . VAL A 1 52  ? 13.846 30.181  39.560  1.00 26.53  ? 31   VAL A N     1 
ATOM   202  C CA    . VAL A 1 52  ? 13.968 29.826  38.151  1.00 25.35  ? 31   VAL A CA    1 
ATOM   203  C C     . VAL A 1 52  ? 12.591 29.380  37.655  1.00 25.82  ? 31   VAL A C     1 
ATOM   204  O O     . VAL A 1 52  ? 11.944 28.539  38.295  1.00 24.16  ? 31   VAL A O     1 
ATOM   205  C CB    . VAL A 1 52  ? 14.996 28.698  37.992  1.00 26.35  ? 31   VAL A CB    1 
ATOM   206  C CG1   . VAL A 1 52  ? 15.129 28.251  36.532  1.00 28.96  ? 31   VAL A CG1   1 
ATOM   207  C CG2   . VAL A 1 52  ? 16.365 29.049  38.553  1.00 26.81  ? 31   VAL A CG2   1 
ATOM   208  N N     . ALA A 1 53  ? 12.151 29.970  36.537  1.00 24.45  ? 32   ALA A N     1 
ATOM   209  C CA    . ALA A 1 53  ? 10.992 29.515  35.789  1.00 23.97  ? 32   ALA A CA    1 
ATOM   210  C C     . ALA A 1 53  ? 11.424 28.800  34.495  1.00 25.28  ? 32   ALA A C     1 
ATOM   211  O O     . ALA A 1 53  ? 12.305 29.229  33.736  1.00 22.59  ? 32   ALA A O     1 
ATOM   212  C CB    . ALA A 1 53  ? 10.069 30.661  35.505  1.00 24.57  ? 32   ALA A CB    1 
ATOM   213  N N     . LEU A 1 54  ? 10.801 27.654  34.245  1.00 20.79  ? 33   LEU A N     1 
ATOM   214  C CA    . LEU A 1 54  ? 11.010 26.938  32.993  1.00 19.90  ? 33   LEU A CA    1 
ATOM   215  C C     . LEU A 1 54  ? 9.652  26.885  32.312  1.00 20.53  ? 33   LEU A C     1 
ATOM   216  O O     . LEU A 1 54  ? 8.716  26.306  32.862  1.00 23.37  ? 33   LEU A O     1 
ATOM   217  C CB    . LEU A 1 54  ? 11.602 25.549  33.246  1.00 19.20  ? 33   LEU A CB    1 
ATOM   218  C CG    . LEU A 1 54  ? 11.782 24.692  31.978  1.00 20.47  ? 33   LEU A CG    1 
ATOM   219  C CD1   . LEU A 1 54  ? 12.841 25.338  31.074  1.00 18.95  ? 33   LEU A CD1   1 
ATOM   220  C CD2   . LEU A 1 54  ? 12.167 23.254  32.245  1.00 22.32  ? 33   LEU A CD2   1 
ATOM   221  N N     . VAL A 1 55  ? 9.531  27.553  31.170  1.00 19.02  ? 34   VAL A N     1 
ATOM   222  C CA    . VAL A 1 55  ? 8.251  27.711  30.512  1.00 20.85  ? 34   VAL A CA    1 
ATOM   223  C C     . VAL A 1 55  ? 8.234  26.891  29.231  1.00 21.74  ? 34   VAL A C     1 
ATOM   224  O O     . VAL A 1 55  ? 9.076  27.114  28.341  1.00 23.12  ? 34   VAL A O     1 
ATOM   225  C CB    . VAL A 1 55  ? 7.969  29.181  30.156  1.00 22.70  ? 34   VAL A CB    1 
ATOM   226  C CG1   . VAL A 1 55  ? 6.498  29.375  29.780  1.00 24.60  ? 34   VAL A CG1   1 
ATOM   227  C CG2   . VAL A 1 55  ? 8.365  30.096  31.283  1.00 28.33  ? 34   VAL A CG2   1 
ATOM   228  N N     . GLU A 1 56  ? 7.206  26.052  29.093  1.00 20.06  ? 35   GLU A N     1 
ATOM   229  C CA    . GLU A 1 56  ? 7.132  25.067  28.020  1.00 20.50  ? 35   GLU A CA    1 
ATOM   230  C C     . GLU A 1 56  ? 5.740  25.112  27.383  1.00 21.41  ? 35   GLU A C     1 
ATOM   231  O O     . GLU A 1 56  ? 4.750  25.129  28.085  1.00 18.75  ? 35   GLU A O     1 
ATOM   232  C CB    . GLU A 1 56  ? 7.424  23.659  28.550  1.00 20.27  ? 35   GLU A CB    1 
ATOM   233  C CG    . GLU A 1 56  ? 7.140  22.531  27.549  1.00 21.17  ? 35   GLU A CG    1 
ATOM   234  C CD    . GLU A 1 56  ? 7.836  22.680  26.192  1.00 20.53  ? 35   GLU A CD    1 
ATOM   235  O OE1   . GLU A 1 56  ? 7.182  22.433  25.149  1.00 18.52  ? 35   GLU A OE1   1 
ATOM   236  O OE2   . GLU A 1 56  ? 9.044  23.046  26.180  1.00 20.83  ? 35   GLU A OE2   1 
ATOM   237  N N     . ALA A 1 57  ? 5.689  25.126  26.046  1.00 19.46  ? 36   ALA A N     1 
ATOM   238  C CA    . ALA A 1 57  ? 4.443  25.169  25.299  1.00 20.80  ? 36   ALA A CA    1 
ATOM   239  C C     . ALA A 1 57  ? 3.664  23.872  25.479  1.00 20.22  ? 36   ALA A C     1 
ATOM   240  O O     . ALA A 1 57  ? 2.429  23.934  25.572  1.00 18.71  ? 36   ALA A O     1 
ATOM   241  C CB    . ALA A 1 57  ? 4.718  25.407  23.819  1.00 20.76  ? 36   ALA A CB    1 
ATOM   242  N N     . GLY A 1 58  ? 4.385  22.731  25.485  1.00 18.71  ? 37   GLY A N     1 
ATOM   243  C CA    . GLY A 1 58  ? 3.744  21.421  25.547  1.00 19.92  ? 37   GLY A CA    1 
ATOM   244  C C     . GLY A 1 58  ? 3.416  21.028  26.989  1.00 22.11  ? 37   GLY A C     1 
ATOM   245  O O     . GLY A 1 58  ? 3.664  21.808  27.940  1.00 21.93  ? 37   GLY A O     1 
ATOM   246  N N     . GLY A 1 59  ? 2.857  19.822  27.151  1.00 22.96  ? 38   GLY A N     1 
ATOM   247  C CA    . GLY A 1 59  ? 2.470  19.332  28.473  1.00 23.43  ? 38   GLY A CA    1 
ATOM   248  C C     . GLY A 1 59  ? 3.513  18.366  29.026  1.00 23.10  ? 38   GLY A C     1 
ATOM   249  O O     . GLY A 1 59  ? 4.608  18.234  28.476  1.00 20.41  ? 38   GLY A O     1 
ATOM   250  N N     . ALA A 1 60  ? 3.182  17.710  30.144  1.00 20.13  ? 39   ALA A N     1 
ATOM   251  C CA    . ALA A 1 60  ? 4.024  16.656  30.681  1.00 22.21  ? 39   ALA A CA    1 
ATOM   252  C C     . ALA A 1 60  ? 4.203  15.522  29.671  1.00 20.32  ? 39   ALA A C     1 
ATOM   253  O O     . ALA A 1 60  ? 3.340  15.231  28.851  1.00 18.70  ? 39   ALA A O     1 
ATOM   254  C CB    . ALA A 1 60  ? 3.457  16.144  32.003  1.00 26.17  ? 39   ALA A CB    1 
ATOM   255  N N     . ASP A 1 61  ? 5.377  14.885  29.729  1.00 19.95  ? 40   ASP A N     1 
ATOM   256  C CA    . ASP A 1 61  ? 5.710  13.781  28.842  1.00 21.21  ? 40   ASP A CA    1 
ATOM   257  C C     . ASP A 1 61  ? 5.130  12.474  29.392  1.00 22.01  ? 40   ASP A C     1 
ATOM   258  O O     . ASP A 1 61  ? 5.903  11.646  29.853  1.00 22.11  ? 40   ASP A O     1 
ATOM   259  C CB    . ASP A 1 61  ? 7.223  13.671  28.676  1.00 19.66  ? 40   ASP A CB    1 
ATOM   260  C CG    . ASP A 1 61  ? 8.016  13.576  29.977  1.00 22.54  ? 40   ASP A CG    1 
ATOM   261  O OD1   . ASP A 1 61  ? 7.678  14.332  30.940  1.00 21.28  ? 40   ASP A OD1   1 
ATOM   262  O OD2   . ASP A 1 61  ? 8.966  12.760  30.032  1.00 20.89  ? 40   ASP A OD2   1 
ATOM   263  N N     . THR A 1 62  ? 3.805  12.247  29.273  1.00 22.72  ? 41   THR A N     1 
ATOM   264  C CA    . THR A 1 62  ? 3.155  11.167  30.015  1.00 24.54  ? 41   THR A CA    1 
ATOM   265  C C     . THR A 1 62  ? 2.869  9.951   29.137  1.00 22.53  ? 41   THR A C     1 
ATOM   266  O O     . THR A 1 62  ? 2.762  8.841   29.653  1.00 19.79  ? 41   THR A O     1 
ATOM   267  C CB    . THR A 1 62  ? 1.869  11.653  30.688  1.00 26.82  ? 41   THR A CB    1 
ATOM   268  O OG1   . THR A 1 62  ? 1.035  12.218  29.694  1.00 27.72  ? 41   THR A OG1   1 
ATOM   269  C CG2   . THR A 1 62  ? 2.084  12.804  31.648  1.00 27.27  ? 41   THR A CG2   1 
ATOM   270  N N     . ASP A 1 63  ? 2.755  10.124  27.819  1.00 20.79  ? 42   ASP A N     1 
ATOM   271  C CA    . ASP A 1 63  ? 2.358  9.002   26.981  1.00 21.29  ? 42   ASP A CA    1 
ATOM   272  C C     . ASP A 1 63  ? 3.410  7.888   26.940  1.00 21.16  ? 42   ASP A C     1 
ATOM   273  O O     . ASP A 1 63  ? 4.610  8.139   26.850  1.00 19.41  ? 42   ASP A O     1 
ATOM   274  C CB    . ASP A 1 63  ? 2.082  9.438   25.560  1.00 21.99  ? 42   ASP A CB    1 
ATOM   275  C CG    . ASP A 1 63  ? 1.415  8.345   24.737  1.00 20.28  ? 42   ASP A CG    1 
ATOM   276  O OD1   . ASP A 1 63  ? 0.244  8.063   25.019  1.00 19.84  ? 42   ASP A OD1   1 
ATOM   277  O OD2   . ASP A 1 63  ? 2.081  7.812   23.834  1.00 19.29  ? 42   ASP A OD2   1 
ATOM   278  N N     . ARG A 1 64  ? 2.908  6.650   26.859  1.00 20.16  ? 43   ARG A N     1 
ATOM   279  C CA    . ARG A 1 64  ? 3.673  5.427   26.683  1.00 22.64  ? 43   ARG A CA    1 
ATOM   280  C C     . ARG A 1 64  ? 4.688  5.490   25.545  1.00 20.21  ? 43   ARG A C     1 
ATOM   281  O O     . ARG A 1 64  ? 5.760  4.915   25.661  1.00 23.10  ? 43   ARG A O     1 
ATOM   282  C CB    . ARG A 1 64  ? 2.761  4.277   26.217  1.00 29.41  ? 43   ARG A CB    1 
ATOM   283  C CG    . ARG A 1 64  ? 2.501  3.172   27.214  1.00 35.87  ? 43   ARG A CG    1 
ATOM   284  C CD    . ARG A 1 64  ? 2.120  1.855   26.528  1.00 35.14  ? 43   ARG A CD    1 
ATOM   285  N NE    . ARG A 1 64  ? 1.035  1.841   25.543  1.00 30.10  ? 43   ARG A NE    1 
ATOM   286  C CZ    . ARG A 1 64  ? -0.264 1.776   25.784  1.00 28.89  ? 43   ARG A CZ    1 
ATOM   287  N NH1   . ARG A 1 64  ? -0.694 1.946   26.994  1.00 32.44  ? 43   ARG A NH1   1 
ATOM   288  N NH2   . ARG A 1 64  ? -1.143 1.557   24.825  1.00 31.87  ? 43   ARG A NH2   1 
ATOM   289  N N     . ALA A 1 65  ? 4.292  6.015   24.383  1.00 19.39  ? 44   ALA A N     1 
ATOM   290  C CA    . ALA A 1 65  ? 5.169  6.041   23.223  1.00 18.00  ? 44   ALA A CA    1 
ATOM   291  C C     . ALA A 1 65  ? 6.419  6.900   23.448  1.00 19.32  ? 44   ALA A C     1 
ATOM   292  O O     . ALA A 1 65  ? 7.331  6.847   22.624  1.00 20.99  ? 44   ALA A O     1 
ATOM   293  C CB    . ALA A 1 65  ? 4.410  6.519   22.009  1.00 19.13  ? 44   ALA A CB    1 
ATOM   294  N N     . VAL A 1 66  ? 6.422  7.738   24.498  1.00 18.12  ? 45   VAL A N     1 
ATOM   295  C CA    . VAL A 1 66  ? 7.608  8.475   24.901  1.00 19.22  ? 45   VAL A CA    1 
ATOM   296  C C     . VAL A 1 66  ? 8.610  7.503   25.519  1.00 18.69  ? 45   VAL A C     1 
ATOM   297  O O     . VAL A 1 66  ? 9.796  7.605   25.252  1.00 18.48  ? 45   VAL A O     1 
ATOM   298  C CB    . VAL A 1 66  ? 7.307  9.630   25.874  1.00 19.84  ? 45   VAL A CB    1 
ATOM   299  C CG1   . VAL A 1 66  ? 8.587  10.277  26.386  1.00 20.41  ? 45   VAL A CG1   1 
ATOM   300  C CG2   . VAL A 1 66  ? 6.444  10.704  25.229  1.00 21.68  ? 45   VAL A CG2   1 
ATOM   301  N N     . ARG A 1 67  ? 8.133  6.550   26.332  1.00 19.50  ? 46   ARG A N     1 
ATOM   302  C CA    . ARG A 1 67  ? 9.015  5.665   27.099  1.00 21.18  ? 46   ARG A CA    1 
ATOM   303  C C     . ARG A 1 67  ? 9.639  4.555   26.245  1.00 19.64  ? 46   ARG A C     1 
ATOM   304  O O     . ARG A 1 67  ? 10.793 4.139   26.468  1.00 17.73  ? 46   ARG A O     1 
ATOM   305  C CB    . ARG A 1 67  ? 8.196  4.913   28.153  1.00 26.48  ? 46   ARG A CB    1 
ATOM   306  C CG    . ARG A 1 67  ? 7.223  5.673   29.046  1.00 30.92  ? 46   ARG A CG    1 
ATOM   307  C CD    . ARG A 1 67  ? 7.913  6.283   30.261  1.00 28.98  ? 46   ARG A CD    1 
ATOM   308  N NE    . ARG A 1 67  ? 8.576  7.547   29.908  1.00 30.22  ? 46   ARG A NE    1 
ATOM   309  C CZ    . ARG A 1 67  ? 7.950  8.739   29.903  1.00 31.37  ? 46   ARG A CZ    1 
ATOM   310  N NH1   . ARG A 1 67  ? 6.610  8.817   29.971  1.00 30.17  ? 46   ARG A NH1   1 
ATOM   311  N NH2   . ARG A 1 67  ? 8.667  9.856   29.845  1.00 28.04  ? 46   ARG A NH2   1 
ATOM   312  N N     . ILE A 1 68  ? 8.844  4.031   25.298  1.00 18.11  ? 47   ILE A N     1 
ATOM   313  C CA    . ILE A 1 68  ? 9.190  2.819   24.567  1.00 19.28  ? 47   ILE A CA    1 
ATOM   314  C C     . ILE A 1 68  ? 10.037 3.187   23.340  1.00 19.51  ? 47   ILE A C     1 
ATOM   315  O O     . ILE A 1 68  ? 9.595  3.908   22.429  1.00 17.56  ? 47   ILE A O     1 
ATOM   316  C CB    . ILE A 1 68  ? 7.918  2.069   24.150  1.00 20.90  ? 47   ILE A CB    1 
ATOM   317  C CG1   . ILE A 1 68  ? 7.050  1.648   25.355  1.00 22.24  ? 47   ILE A CG1   1 
ATOM   318  C CG2   . ILE A 1 68  ? 8.285  0.885   23.259  1.00 20.85  ? 47   ILE A CG2   1 
ATOM   319  C CD1   . ILE A 1 68  ? 5.657  1.173   24.964  1.00 22.68  ? 47   ILE A CD1   1 
ATOM   320  N N     . PRO A 1 69  ? 11.299 2.725   23.272  1.00 18.25  ? 48   PRO A N     1 
ATOM   321  C CA    . PRO A 1 69  ? 12.213 3.188   22.217  1.00 18.62  ? 48   PRO A CA    1 
ATOM   322  C C     . PRO A 1 69  ? 11.663 2.990   20.808  1.00 18.41  ? 48   PRO A C     1 
ATOM   323  O O     . PRO A 1 69  ? 11.775 3.890   19.980  1.00 20.13  ? 48   PRO A O     1 
ATOM   324  C CB    . PRO A 1 69  ? 13.522 2.406   22.515  1.00 18.53  ? 48   PRO A CB    1 
ATOM   325  C CG    . PRO A 1 69  ? 13.450 2.165   24.029  1.00 20.08  ? 48   PRO A CG    1 
ATOM   326  C CD    . PRO A 1 69  ? 11.965 1.892   24.282  1.00 19.01  ? 48   PRO A CD    1 
ATOM   327  N N     . ALA A 1 70  ? 11.001 1.845   20.559  1.00 18.62  ? 49   ALA A N     1 
ATOM   328  C CA    . ALA A 1 70  ? 10.543 1.491   19.228  1.00 18.37  ? 49   ALA A CA    1 
ATOM   329  C C     . ALA A 1 70  ? 9.379  2.376   18.790  1.00 17.49  ? 49   ALA A C     1 
ATOM   330  O O     . ALA A 1 70  ? 9.115  2.463   17.604  1.00 18.18  ? 49   ALA A O     1 
ATOM   331  C CB    . ALA A 1 70  ? 10.108 0.042   19.176  1.00 20.25  ? 49   ALA A CB    1 
ATOM   332  N N     . ALA A 1 71  ? 8.763  3.106   19.723  1.00 17.86  ? 50   ALA A N     1 
ATOM   333  C CA    . ALA A 1 71  ? 7.506  3.786   19.435  1.00 18.22  ? 50   ALA A CA    1 
ATOM   334  C C     . ALA A 1 71  ? 7.692  5.241   19.013  1.00 18.98  ? 50   ALA A C     1 
ATOM   335  O O     . ALA A 1 71  ? 6.714  5.918   18.681  1.00 19.68  ? 50   ALA A O     1 
ATOM   336  C CB    . ALA A 1 71  ? 6.595  3.683   20.629  1.00 18.85  ? 50   ALA A CB    1 
ATOM   337  N N     . ALA A 1 72  ? 8.933  5.747   19.055  1.00 17.75  ? 51   ALA A N     1 
ATOM   338  C CA    . ALA A 1 72  ? 9.187  7.185   18.931  1.00 16.94  ? 51   ALA A CA    1 
ATOM   339  C C     . ALA A 1 72  ? 8.514  7.803   17.696  1.00 17.84  ? 51   ALA A C     1 
ATOM   340  O O     . ALA A 1 72  ? 7.897  8.861   17.758  1.00 18.78  ? 51   ALA A O     1 
ATOM   341  C CB    . ALA A 1 72  ? 10.700 7.423   18.925  1.00 16.82  ? 51   ALA A CB    1 
ATOM   342  N N     . ALA A 1 73  ? 8.610  7.144   16.552  1.00 19.38  ? 52   ALA A N     1 
ATOM   343  C CA    . ALA A 1 73  ? 8.073  7.718   15.321  1.00 22.12  ? 52   ALA A CA    1 
ATOM   344  C C     . ALA A 1 73  ? 6.548  7.846   15.366  1.00 22.89  ? 52   ALA A C     1 
ATOM   345  O O     . ALA A 1 73  ? 5.993  8.655   14.623  1.00 19.75  ? 52   ALA A O     1 
ATOM   346  C CB    . ALA A 1 73  ? 8.469  6.859   14.121  1.00 23.74  ? 52   ALA A CB    1 
ATOM   347  N N     . HIS A 1 74  ? 5.878  7.118   16.275  1.00 22.19  ? 53   HIS A N     1 
ATOM   348  C CA    . HIS A 1 74  ? 4.427  7.216   16.361  1.00 22.88  ? 53   HIS A CA    1 
ATOM   349  C C     . HIS A 1 74  ? 4.020  8.547   16.976  1.00 22.80  ? 53   HIS A C     1 
ATOM   350  O O     . HIS A 1 74  ? 2.831  8.861   17.003  1.00 21.76  ? 53   HIS A O     1 
ATOM   351  C CB    . HIS A 1 74  ? 3.824  6.031   17.127  1.00 26.54  ? 53   HIS A CB    1 
ATOM   352  C CG    . HIS A 1 74  ? 4.032  4.772   16.364  1.00 30.52  ? 53   HIS A CG    1 
ATOM   353  N ND1   . HIS A 1 74  ? 4.547  3.632   16.949  1.00 37.79  ? 53   HIS A ND1   1 
ATOM   354  C CD2   . HIS A 1 74  ? 3.836  4.469   15.079  1.00 30.48  ? 53   HIS A CD2   1 
ATOM   355  C CE1   . HIS A 1 74  ? 4.656  2.678   16.027  1.00 30.94  ? 53   HIS A CE1   1 
ATOM   356  N NE2   . HIS A 1 74  ? 4.227  3.160   14.887  1.00 36.68  ? 53   HIS A NE2   1 
ATOM   357  N N     . LEU A 1 75  ? 4.970  9.323   17.520  1.00 19.18  ? 54   LEU A N     1 
ATOM   358  C CA    . LEU A 1 75  ? 4.615  10.634  18.071  1.00 18.47  ? 54   LEU A CA    1 
ATOM   359  C C     . LEU A 1 75  ? 4.507  11.721  16.982  1.00 17.11  ? 54   LEU A C     1 
ATOM   360  O O     . LEU A 1 75  ? 3.973  12.799  17.218  1.00 17.11  ? 54   LEU A O     1 
ATOM   361  C CB    . LEU A 1 75  ? 5.641  11.013  19.145  1.00 17.92  ? 54   LEU A CB    1 
ATOM   362  C CG    . LEU A 1 75  ? 5.676  10.118  20.391  1.00 18.47  ? 54   LEU A CG    1 
ATOM   363  C CD1   . LEU A 1 75  ? 6.968  10.431  21.109  1.00 20.84  ? 54   LEU A CD1   1 
ATOM   364  C CD2   . LEU A 1 75  ? 4.533  10.318  21.338  1.00 19.76  ? 54   LEU A CD2   1 
ATOM   365  N N     . PHE A 1 76  ? 4.959  11.429  15.764  1.00 19.67  ? 55   PHE A N     1 
ATOM   366  C CA    . PHE A 1 76  ? 4.841  12.360  14.660  1.00 20.52  ? 55   PHE A CA    1 
ATOM   367  C C     . PHE A 1 76  ? 3.372  12.689  14.406  1.00 24.00  ? 55   PHE A C     1 
ATOM   368  O O     . PHE A 1 76  ? 2.526  11.791  14.355  1.00 20.25  ? 55   PHE A O     1 
ATOM   369  C CB    . PHE A 1 76  ? 5.301  11.827  13.309  1.00 23.77  ? 55   PHE A CB    1 
ATOM   370  C CG    . PHE A 1 76  ? 6.800  11.772  13.093  1.00 24.70  ? 55   PHE A CG    1 
ATOM   371  C CD1   . PHE A 1 76  ? 7.675  11.603  14.161  1.00 24.76  ? 55   PHE A CD1   1 
ATOM   372  C CD2   . PHE A 1 76  ? 7.321  11.890  11.806  1.00 25.10  ? 55   PHE A CD2   1 
ATOM   373  C CE1   . PHE A 1 76  ? 9.046  11.506  13.941  1.00 23.84  ? 55   PHE A CE1   1 
ATOM   374  C CE2   . PHE A 1 76  ? 8.684  11.826  11.592  1.00 25.76  ? 55   PHE A CE2   1 
ATOM   375  C CZ    . PHE A 1 76  ? 9.551  11.624  12.663  1.00 24.90  ? 55   PHE A CZ    1 
ATOM   376  N N     . GLY A 1 77  ? 3.096  13.986  14.298  1.00 22.12  ? 56   GLY A N     1 
ATOM   377  C CA    . GLY A 1 77  ? 1.771  14.480  13.956  1.00 22.64  ? 56   GLY A CA    1 
ATOM   378  C C     . GLY A 1 77  ? 0.832  14.504  15.159  1.00 24.06  ? 56   GLY A C     1 
ATOM   379  O O     . GLY A 1 77  ? -0.334 14.780  14.967  1.00 25.52  ? 56   GLY A O     1 
ATOM   380  N N     . THR A 1 78  ? 1.332  14.197  16.370  1.00 22.39  ? 57   THR A N     1 
ATOM   381  C CA    . THR A 1 78  ? 0.553  14.214  17.596  1.00 21.47  ? 57   THR A CA    1 
ATOM   382  C C     . THR A 1 78  ? 0.752  15.528  18.338  1.00 21.86  ? 57   THR A C     1 
ATOM   383  O O     . THR A 1 78  ? 1.470  16.402  17.867  1.00 20.40  ? 57   THR A O     1 
ATOM   384  C CB    . THR A 1 78  ? 0.920  13.050  18.532  1.00 22.21  ? 57   THR A CB    1 
ATOM   385  O OG1   . THR A 1 78  ? 2.177  13.279  19.180  1.00 21.06  ? 57   THR A OG1   1 
ATOM   386  C CG2   . THR A 1 78  ? 0.891  11.712  17.811  1.00 22.09  ? 57   THR A CG2   1 
ATOM   387  N N     . GLY A 1 79  ? 0.103  15.646  19.511  1.00 18.45  ? 58   GLY A N     1 
ATOM   388  C CA    . GLY A 1 79  ? 0.292  16.812  20.367  1.00 22.01  ? 58   GLY A CA    1 
ATOM   389  C C     . GLY A 1 79  ? 1.742  16.967  20.841  1.00 21.74  ? 58   GLY A C     1 
ATOM   390  O O     . GLY A 1 79  ? 2.144  18.046  21.308  1.00 21.52  ? 58   GLY A O     1 
ATOM   391  N N     . TYR A 1 80  ? 2.518  15.870  20.747  1.00 19.40  ? 59   TYR A N     1 
ATOM   392  C CA    . TYR A 1 80  ? 3.895  15.867  21.197  1.00 19.23  ? 59   TYR A CA    1 
ATOM   393  C C     . TYR A 1 80  ? 4.811  16.494  20.155  1.00 17.93  ? 59   TYR A C     1 
ATOM   394  O O     . TYR A 1 80  ? 6.012  16.565  20.392  1.00 18.52  ? 59   TYR A O     1 
ATOM   395  C CB    . TYR A 1 80  ? 4.345  14.439  21.540  1.00 20.17  ? 59   TYR A CB    1 
ATOM   396  C CG    . TYR A 1 80  ? 3.773  13.955  22.865  1.00 21.91  ? 59   TYR A CG    1 
ATOM   397  C CD1   . TYR A 1 80  ? 2.432  13.568  22.979  1.00 22.16  ? 59   TYR A CD1   1 
ATOM   398  C CD2   . TYR A 1 80  ? 4.561  13.918  24.018  1.00 21.28  ? 59   TYR A CD2   1 
ATOM   399  C CE1   . TYR A 1 80  ? 1.910  13.138  24.191  1.00 20.75  ? 59   TYR A CE1   1 
ATOM   400  C CE2   . TYR A 1 80  ? 4.044  13.509  25.237  1.00 20.13  ? 59   TYR A CE2   1 
ATOM   401  C CZ    . TYR A 1 80  ? 2.717  13.120  25.315  1.00 22.04  ? 59   TYR A CZ    1 
ATOM   402  O OH    . TYR A 1 80  ? 2.214  12.702  26.499  1.00 21.01  ? 59   TYR A OH    1 
ATOM   403  N N     . ASP A 1 81  ? 4.259  16.896  19.003  1.00 18.71  ? 60   ASP A N     1 
ATOM   404  C CA    . ASP A 1 81  ? 5.026  17.317  17.843  1.00 19.96  ? 60   ASP A CA    1 
ATOM   405  C C     . ASP A 1 81  ? 4.497  18.659  17.348  1.00 22.12  ? 60   ASP A C     1 
ATOM   406  O O     . ASP A 1 81  ? 3.301  18.803  17.119  1.00 18.84  ? 60   ASP A O     1 
ATOM   407  C CB    . ASP A 1 81  ? 4.939  16.231  16.770  1.00 21.54  ? 60   ASP A CB    1 
ATOM   408  C CG    . ASP A 1 81  ? 5.570  16.521  15.412  1.00 21.95  ? 60   ASP A CG    1 
ATOM   409  O OD1   . ASP A 1 81  ? 6.305  17.548  15.293  1.00 20.38  ? 60   ASP A OD1   1 
ATOM   410  O OD2   . ASP A 1 81  ? 5.270  15.723  14.474  1.00 20.80  ? 60   ASP A OD2   1 
ATOM   411  N N     . TRP A 1 82  ? 5.389  19.647  17.188  1.00 18.89  ? 61   TRP A N     1 
ATOM   412  C CA    . TRP A 1 82  ? 5.002  20.923  16.610  1.00 19.69  ? 61   TRP A CA    1 
ATOM   413  C C     . TRP A 1 82  ? 4.452  20.764  15.197  1.00 21.24  ? 61   TRP A C     1 
ATOM   414  O O     . TRP A 1 82  ? 3.603  21.544  14.793  1.00 19.02  ? 61   TRP A O     1 
ATOM   415  C CB    . TRP A 1 82  ? 6.175  21.911  16.573  1.00 19.73  ? 61   TRP A CB    1 
ATOM   416  C CG    . TRP A 1 82  ? 6.525  22.468  17.927  1.00 19.99  ? 61   TRP A CG    1 
ATOM   417  C CD1   . TRP A 1 82  ? 7.363  21.911  18.847  1.00 20.20  ? 61   TRP A CD1   1 
ATOM   418  C CD2   . TRP A 1 82  ? 6.031  23.694  18.524  1.00 19.08  ? 61   TRP A CD2   1 
ATOM   419  N NE1   . TRP A 1 82  ? 7.426  22.704  19.960  1.00 19.02  ? 61   TRP A NE1   1 
ATOM   420  C CE2   . TRP A 1 82  ? 6.630  23.801  19.796  1.00 18.23  ? 61   TRP A CE2   1 
ATOM   421  C CE3   . TRP A 1 82  ? 5.146  24.694  18.111  1.00 20.92  ? 61   TRP A CE3   1 
ATOM   422  C CZ2   . TRP A 1 82  ? 6.387  24.870  20.660  1.00 19.94  ? 61   TRP A CZ2   1 
ATOM   423  C CZ3   . TRP A 1 82  ? 4.898  25.758  18.962  1.00 21.51  ? 61   TRP A CZ3   1 
ATOM   424  C CH2   . TRP A 1 82  ? 5.543  25.866  20.203  1.00 21.67  ? 61   TRP A CH2   1 
ATOM   425  N N     . GLY A 1 83  ? 4.974  19.818  14.420  1.00 18.60  ? 62   GLY A N     1 
ATOM   426  C CA    . GLY A 1 83  ? 4.412  19.523  13.103  1.00 18.89  ? 62   GLY A CA    1 
ATOM   427  C C     . GLY A 1 83  ? 4.673  20.630  12.087  1.00 20.73  ? 62   GLY A C     1 
ATOM   428  O O     . GLY A 1 83  ? 3.812  20.958  11.267  1.00 19.58  ? 62   GLY A O     1 
ATOM   429  N N     . TYR A 1 84  ? 5.894  21.163  12.075  1.00 18.70  ? 63   TYR A N     1 
ATOM   430  C CA    . TYR A 1 84  ? 6.253  22.105  11.037  1.00 17.34  ? 63   TYR A CA    1 
ATOM   431  C C     . TYR A 1 84  ? 6.486  21.416  9.695   1.00 18.77  ? 63   TYR A C     1 
ATOM   432  O O     . TYR A 1 84  ? 6.733  20.214  9.615   1.00 19.28  ? 63   TYR A O     1 
ATOM   433  C CB    . TYR A 1 84  ? 7.519  22.841  11.455  1.00 18.55  ? 63   TYR A CB    1 
ATOM   434  C CG    . TYR A 1 84  ? 7.421  23.691  12.702  1.00 18.03  ? 63   TYR A CG    1 
ATOM   435  C CD1   . TYR A 1 84  ? 6.626  24.818  12.730  1.00 19.95  ? 63   TYR A CD1   1 
ATOM   436  C CD2   . TYR A 1 84  ? 8.191  23.420  13.816  1.00 18.83  ? 63   TYR A CD2   1 
ATOM   437  C CE1   . TYR A 1 84  ? 6.561  25.635  13.847  1.00 18.61  ? 63   TYR A CE1   1 
ATOM   438  C CE2   . TYR A 1 84  ? 8.149  24.237  14.942  1.00 19.52  ? 63   TYR A CE2   1 
ATOM   439  C CZ    . TYR A 1 84  ? 7.318  25.343  14.962  1.00 18.27  ? 63   TYR A CZ    1 
ATOM   440  O OH    . TYR A 1 84  ? 7.278  26.169  16.052  1.00 19.00  ? 63   TYR A OH    1 
ATOM   441  N N     . SER A 1 85  ? 6.489  22.231  8.632   1.00 20.06  ? 64   SER A N     1 
ATOM   442  C CA    . SER A 1 85  ? 6.931  21.814  7.306   1.00 22.25  ? 64   SER A CA    1 
ATOM   443  C C     . SER A 1 85  ? 7.704  22.953  6.646   1.00 23.22  ? 64   SER A C     1 
ATOM   444  O O     . SER A 1 85  ? 7.461  24.124  6.939   1.00 22.16  ? 64   SER A O     1 
ATOM   445  C CB    . SER A 1 85  ? 5.753  21.416  6.428   1.00 25.26  ? 64   SER A CB    1 
ATOM   446  O OG    . SER A 1 85  ? 5.302  20.116  6.761   1.00 29.66  ? 64   SER A OG    1 
ATOM   447  N N     . THR A 1 86  ? 8.637  22.602  5.752   1.00 20.81  ? 65   THR A N     1 
ATOM   448  C CA    . THR A 1 86  ? 9.371  23.619  5.017   1.00 21.02  ? 65   THR A CA    1 
ATOM   449  C C     . THR A 1 86  ? 8.479  24.169  3.919   1.00 18.93  ? 65   THR A C     1 
ATOM   450  O O     . THR A 1 86  ? 7.509  23.547  3.517   1.00 17.89  ? 65   THR A O     1 
ATOM   451  C CB    . THR A 1 86  ? 10.665 23.092  4.394   1.00 20.73  ? 65   THR A CB    1 
ATOM   452  O OG1   . THR A 1 86  ? 10.270 22.234  3.315   1.00 18.60  ? 65   THR A OG1   1 
ATOM   453  C CG2   . THR A 1 86  ? 11.501 22.356  5.423   1.00 19.58  ? 65   THR A CG2   1 
ATOM   454  N N     . VAL A 1 87  ? 8.904  25.319  3.414   1.00 21.10  ? 66   VAL A N     1 
ATOM   455  C CA    . VAL A 1 87  ? 8.393  25.848  2.158   1.00 22.46  ? 66   VAL A CA    1 
ATOM   456  C C     . VAL A 1 87  ? 8.837  24.899  1.048   1.00 20.65  ? 66   VAL A C     1 
ATOM   457  O O     . VAL A 1 87  ? 9.705  24.005  1.262   1.00 18.15  ? 66   VAL A O     1 
ATOM   458  C CB    . VAL A 1 87  ? 8.848  27.306  1.903   1.00 21.62  ? 66   VAL A CB    1 
ATOM   459  C CG1   . VAL A 1 87  ? 8.381  28.250  3.004   1.00 23.28  ? 66   VAL A CG1   1 
ATOM   460  C CG2   . VAL A 1 87  ? 10.347 27.431  1.669   1.00 22.17  ? 66   VAL A CG2   1 
ATOM   461  N N     . PRO A 1 88  ? 8.265  25.019  -0.182  1.00 25.35  ? 67   PRO A N     1 
ATOM   462  C CA    . PRO A 1 88  ? 8.726  24.166  -1.294  1.00 22.04  ? 67   PRO A CA    1 
ATOM   463  C C     . PRO A 1 88  ? 10.222 24.375  -1.531  1.00 20.86  ? 67   PRO A C     1 
ATOM   464  O O     . PRO A 1 88  ? 10.712 25.499  -1.477  1.00 20.88  ? 67   PRO A O     1 
ATOM   465  C CB    . PRO A 1 88  ? 7.838  24.588  -2.475  1.00 24.23  ? 67   PRO A CB    1 
ATOM   466  C CG    . PRO A 1 88  ? 6.578  25.082  -1.770  1.00 27.55  ? 67   PRO A CG    1 
ATOM   467  C CD    . PRO A 1 88  ? 7.088  25.847  -0.542  1.00 24.47  ? 67   PRO A CD    1 
ATOM   468  N N     . GLN A 1 89  ? 10.953 23.275  -1.693  1.00 19.49  ? 68   GLN A N     1 
ATOM   469  C CA    . GLN A 1 89  ? 12.402 23.314  -1.871  1.00 20.65  ? 68   GLN A CA    1 
ATOM   470  C C     . GLN A 1 89  ? 12.804 23.049  -3.327  1.00 24.38  ? 68   GLN A C     1 
ATOM   471  O O     . GLN A 1 89  ? 12.684 21.926  -3.816  1.00 24.39  ? 68   GLN A O     1 
ATOM   472  C CB    . GLN A 1 89  ? 13.040 22.193  -1.061  1.00 21.71  ? 68   GLN A CB    1 
ATOM   473  C CG    . GLN A 1 89  ? 12.822 22.323  0.449   1.00 19.60  ? 68   GLN A CG    1 
ATOM   474  C CD    . GLN A 1 89  ? 13.530 23.520  1.021   1.00 17.95  ? 68   GLN A CD    1 
ATOM   475  O OE1   . GLN A 1 89  ? 14.756 23.551  1.143   1.00 20.61  ? 68   GLN A OE1   1 
ATOM   476  N NE2   . GLN A 1 89  ? 12.772 24.551  1.347   1.00 19.09  ? 68   GLN A NE2   1 
ATOM   477  N N     . ALA A 1 90  ? 13.425 24.050  -3.964  1.00 26.20  ? 69   ALA A N     1 
ATOM   478  C CA    . ALA A 1 90  ? 13.779 23.968  -5.374  1.00 27.88  ? 69   ALA A CA    1 
ATOM   479  C C     . ALA A 1 90  ? 14.784 22.842  -5.588  1.00 26.74  ? 69   ALA A C     1 
ATOM   480  O O     . ALA A 1 90  ? 14.652 22.118  -6.562  1.00 28.92  ? 69   ALA A O     1 
ATOM   481  C CB    . ALA A 1 90  ? 14.331 25.292  -5.886  1.00 30.99  ? 69   ALA A CB    1 
ATOM   482  N N     . GLY A 1 91  ? 15.750 22.690  -4.670  1.00 22.44  ? 70   GLY A N     1 
ATOM   483  C CA    . GLY A 1 91  ? 16.743 21.630  -4.736  1.00 21.01  ? 70   GLY A CA    1 
ATOM   484  C C     . GLY A 1 91  ? 16.141 20.219  -4.621  1.00 21.06  ? 70   GLY A C     1 
ATOM   485  O O     . GLY A 1 91  ? 16.821 19.255  -4.964  1.00 22.92  ? 70   GLY A O     1 
ATOM   486  N N     . LEU A 1 92  ? 14.865 20.105  -4.219  1.00 21.70  ? 71   LEU A N     1 
ATOM   487  C CA    . LEU A 1 92  ? 14.159 18.832  -4.065  1.00 24.39  ? 71   LEU A CA    1 
ATOM   488  C C     . LEU A 1 92  ? 13.004 18.758  -5.058  1.00 26.88  ? 71   LEU A C     1 
ATOM   489  O O     . LEU A 1 92  ? 11.991 18.111  -4.785  1.00 25.37  ? 71   LEU A O     1 
ATOM   490  C CB    . LEU A 1 92  ? 13.599 18.671  -2.647  1.00 21.22  ? 71   LEU A CB    1 
ATOM   491  C CG    . LEU A 1 92  ? 14.619 18.745  -1.516  1.00 22.14  ? 71   LEU A CG    1 
ATOM   492  C CD1   . LEU A 1 92  ? 13.947 18.383  -0.178  1.00 22.58  ? 71   LEU A CD1   1 
ATOM   493  C CD2   . LEU A 1 92  ? 15.782 17.826  -1.817  1.00 22.57  ? 71   LEU A CD2   1 
ATOM   494  N N     . GLY A 1 93  ? 13.104 19.543  -6.132  1.00 29.04  ? 72   GLY A N     1 
ATOM   495  C CA    . GLY A 1 93  ? 12.080 19.530  -7.157  1.00 28.78  ? 72   GLY A CA    1 
ATOM   496  C C     . GLY A 1 93  ? 10.779 20.131  -6.659  1.00 28.39  ? 72   GLY A C     1 
ATOM   497  O O     . GLY A 1 93  ? 9.737  19.799  -7.177  1.00 31.77  ? 72   GLY A O     1 
ATOM   498  N N     . GLY A 1 94  ? 10.810 21.007  -5.653  1.00 27.05  ? 73   GLY A N     1 
ATOM   499  C CA    . GLY A 1 94  ? 9.575  21.624  -5.180  1.00 27.67  ? 73   GLY A CA    1 
ATOM   500  C C     . GLY A 1 94  ? 8.939  20.907  -3.982  1.00 27.28  ? 73   GLY A C     1 
ATOM   501  O O     . GLY A 1 94  ? 7.936  21.384  -3.449  1.00 28.54  ? 73   GLY A O     1 
ATOM   502  N N     . ARG A 1 95  ? 9.531  19.804  -3.506  1.00 25.94  ? 74   ARG A N     1 
ATOM   503  C CA    . ARG A 1 95  ? 8.964  19.096  -2.376  1.00 26.55  ? 74   ARG A CA    1 
ATOM   504  C C     . ARG A 1 95  ? 9.077  19.938  -1.109  1.00 24.19  ? 74   ARG A C     1 
ATOM   505  O O     . ARG A 1 95  ? 10.016 20.700  -0.930  1.00 23.05  ? 74   ARG A O     1 
ATOM   506  C CB    . ARG A 1 95  ? 9.641  17.762  -2.060  1.00 27.55  ? 74   ARG A CB    1 
ATOM   507  C CG    . ARG A 1 95  ? 9.167  16.637  -2.957  1.00 32.27  ? 74   ARG A CG    1 
ATOM   508  C CD    . ARG A 1 95  ? 9.692  15.279  -2.475  1.00 31.30  ? 74   ARG A CD    1 
ATOM   509  N NE    . ARG A 1 95  ? 11.150 15.269  -2.538  1.00 30.74  ? 74   ARG A NE    1 
ATOM   510  C CZ    . ARG A 1 95  ? 11.970 15.057  -1.519  1.00 26.79  ? 74   ARG A CZ    1 
ATOM   511  N NH1   . ARG A 1 95  ? 11.472 14.956  -0.314  1.00 25.06  ? 74   ARG A NH1   1 
ATOM   512  N NH2   . ARG A 1 95  ? 13.284 15.014  -1.710  1.00 24.57  ? 74   ARG A NH2   1 
ATOM   513  N N     . GLU A 1 96  ? 8.080  19.777  -0.244  1.00 24.35  ? 75   GLU A N     1 
ATOM   514  C CA    . GLU A 1 96  ? 8.106  20.321  1.099   1.00 23.88  ? 75   GLU A CA    1 
ATOM   515  C C     . GLU A 1 96  ? 8.539  19.176  2.023   1.00 22.67  ? 75   GLU A C     1 
ATOM   516  O O     . GLU A 1 96  ? 8.241  18.015  1.758   1.00 22.89  ? 75   GLU A O     1 
ATOM   517  C CB    . GLU A 1 96  ? 6.707  20.827  1.423   1.00 26.06  ? 75   GLU A CB    1 
ATOM   518  C CG    . GLU A 1 96  ? 6.306  22.085  0.653   1.00 28.06  ? 75   GLU A CG    1 
ATOM   519  C CD    . GLU A 1 96  ? 4.911  22.571  1.008   1.00 31.98  ? 75   GLU A CD    1 
ATOM   520  O OE1   . GLU A 1 96  ? 4.608  23.731  0.760   1.00 46.31  ? 75   GLU A OE1   1 
ATOM   521  O OE2   . GLU A 1 96  ? 4.136  21.812  1.583   1.00 34.45  ? 75   GLU A OE2   1 
ATOM   522  N N     . VAL A 1 97  ? 9.297  19.504  3.061   1.00 20.19  ? 76   VAL A N     1 
ATOM   523  C CA    . VAL A 1 97  ? 9.851  18.504  3.954   1.00 19.37  ? 76   VAL A CA    1 
ATOM   524  C C     . VAL A 1 97  ? 9.228  18.680  5.333   1.00 18.62  ? 76   VAL A C     1 
ATOM   525  O O     . VAL A 1 97  ? 9.145  19.785  5.853   1.00 17.61  ? 76   VAL A O     1 
ATOM   526  C CB    . VAL A 1 97  ? 11.372 18.666  3.970   1.00 20.84  ? 76   VAL A CB    1 
ATOM   527  C CG1   . VAL A 1 97  ? 12.036 17.812  5.038   1.00 21.84  ? 76   VAL A CG1   1 
ATOM   528  C CG2   . VAL A 1 97  ? 11.941 18.363  2.591   1.00 22.21  ? 76   VAL A CG2   1 
ATOM   529  N N     . TYR A 1 98  ? 8.758  17.572  5.896   1.00 19.35  ? 77   TYR A N     1 
ATOM   530  C CA    . TYR A 1 98  ? 8.135  17.579  7.206   1.00 20.56  ? 77   TYR A CA    1 
ATOM   531  C C     . TYR A 1 98  ? 9.217  17.774  8.266   1.00 18.95  ? 77   TYR A C     1 
ATOM   532  O O     . TYR A 1 98  ? 10.252 17.123  8.177   1.00 16.94  ? 77   TYR A O     1 
ATOM   533  C CB    . TYR A 1 98  ? 7.369  16.268  7.448   1.00 19.47  ? 77   TYR A CB    1 
ATOM   534  C CG    . TYR A 1 98  ? 6.560  16.315  8.736   1.00 17.59  ? 77   TYR A CG    1 
ATOM   535  C CD1   . TYR A 1 98  ? 5.540  17.240  8.897   1.00 19.67  ? 77   TYR A CD1   1 
ATOM   536  C CD2   . TYR A 1 98  ? 6.819  15.439  9.787   1.00 17.60  ? 77   TYR A CD2   1 
ATOM   537  C CE1   . TYR A 1 98  ? 4.821  17.302  10.084  1.00 20.47  ? 77   TYR A CE1   1 
ATOM   538  C CE2   . TYR A 1 98  ? 6.091  15.464  10.956  1.00 17.81  ? 77   TYR A CE2   1 
ATOM   539  C CZ    . TYR A 1 98  ? 5.089  16.400  11.108  1.00 20.83  ? 77   TYR A CZ    1 
ATOM   540  O OH    . TYR A 1 98  ? 4.391  16.444  12.280  1.00 19.70  ? 77   TYR A OH    1 
ATOM   541  N N     . TRP A 1 99  ? 8.940  18.641  9.254   1.00 17.91  ? 78   TRP A N     1 
ATOM   542  C CA    . TRP A 1 99  ? 9.867  18.991  10.320  1.00 18.34  ? 78   TRP A CA    1 
ATOM   543  C C     . TRP A 1 99  ? 9.205  18.712  11.673  1.00 20.03  ? 78   TRP A C     1 
ATOM   544  O O     . TRP A 1 99  ? 8.605  19.600  12.298  1.00 23.00  ? 78   TRP A O     1 
ATOM   545  C CB    . TRP A 1 99  ? 10.317 20.452  10.202  1.00 19.89  ? 78   TRP A CB    1 
ATOM   546  C CG    . TRP A 1 99  ? 11.596 20.691  9.444   1.00 18.71  ? 78   TRP A CG    1 
ATOM   547  C CD1   . TRP A 1 99  ? 12.080 20.096  8.316   1.00 19.89  ? 78   TRP A CD1   1 
ATOM   548  C CD2   . TRP A 1 99  ? 12.571 21.670  9.824   1.00 18.53  ? 78   TRP A CD2   1 
ATOM   549  N NE1   . TRP A 1 99  ? 13.304 20.627  7.974   1.00 19.98  ? 78   TRP A NE1   1 
ATOM   550  C CE2   . TRP A 1 99  ? 13.626 21.600  8.890   1.00 19.14  ? 78   TRP A CE2   1 
ATOM   551  C CE3   . TRP A 1 99  ? 12.652 22.574  10.889  1.00 18.53  ? 78   TRP A CE3   1 
ATOM   552  C CZ2   . TRP A 1 99  ? 14.736 22.429  8.983   1.00 19.26  ? 78   TRP A CZ2   1 
ATOM   553  C CZ3   . TRP A 1 99  ? 13.753 23.397  10.971  1.00 18.53  ? 78   TRP A CZ3   1 
ATOM   554  C CH2   . TRP A 1 99  ? 14.771 23.330  10.033  1.00 19.05  ? 78   TRP A CH2   1 
ATOM   555  N N     . PRO A 1 100 ? 9.276  17.465  12.175  1.00 16.49  ? 79   PRO A N     1 
ATOM   556  C CA    . PRO A 1 100 ? 8.831  17.209  13.532  1.00 17.60  ? 79   PRO A CA    1 
ATOM   557  C C     . PRO A 1 100 ? 9.748  17.951  14.504  1.00 16.40  ? 79   PRO A C     1 
ATOM   558  O O     . PRO A 1 100 ? 10.932 18.177  14.245  1.00 15.95  ? 79   PRO A O     1 
ATOM   559  C CB    . PRO A 1 100 ? 8.899  15.696  13.639  1.00 18.33  ? 79   PRO A CB    1 
ATOM   560  C CG    . PRO A 1 100 ? 10.017 15.314  12.706  1.00 18.98  ? 79   PRO A CG    1 
ATOM   561  C CD    . PRO A 1 100 ? 9.875  16.293  11.533  1.00 18.56  ? 79   PRO A CD    1 
ATOM   562  N N     . ARG A 1 101 ? 9.169  18.355  15.618  1.00 17.89  ? 80   ARG A N     1 
ATOM   563  C CA    . ARG A 1 101 ? 9.874  18.971  16.735  1.00 16.71  ? 80   ARG A CA    1 
ATOM   564  C C     . ARG A 1 101 ? 9.159  18.613  18.031  1.00 16.90  ? 80   ARG A C     1 
ATOM   565  O O     . ARG A 1 101 ? 7.941  18.679  18.091  1.00 18.03  ? 80   ARG A O     1 
ATOM   566  C CB    . ARG A 1 101 ? 9.870  20.499  16.629  1.00 17.14  ? 80   ARG A CB    1 
ATOM   567  C CG    . ARG A 1 101 ? 10.736 21.153  15.563  1.00 16.39  ? 80   ARG A CG    1 
ATOM   568  C CD    . ARG A 1 101 ? 12.237 21.086  15.836  1.00 17.90  ? 80   ARG A CD    1 
ATOM   569  N NE    . ARG A 1 101 ? 12.860 19.833  15.398  1.00 17.34  ? 80   ARG A NE    1 
ATOM   570  C CZ    . ARG A 1 101 ? 14.136 19.521  15.507  1.00 18.15  ? 80   ARG A CZ    1 
ATOM   571  N NH1   . ARG A 1 101 ? 14.976 20.259  16.209  1.00 19.44  ? 80   ARG A NH1   1 
ATOM   572  N NH2   . ARG A 1 101 ? 14.592 18.439  14.913  1.00 19.69  ? 80   ARG A NH2   1 
ATOM   573  N N     . GLY A 1 102 ? 9.905  18.237  19.080  1.00 16.72  ? 81   GLY A N     1 
ATOM   574  C CA    . GLY A 1 102 ? 9.250  17.845  20.325  1.00 17.03  ? 81   GLY A CA    1 
ATOM   575  C C     . GLY A 1 102 ? 8.549  19.012  21.018  1.00 16.59  ? 81   GLY A C     1 
ATOM   576  O O     . GLY A 1 102 ? 9.012  20.167  20.964  1.00 18.61  ? 81   GLY A O     1 
ATOM   577  N N     . ARG A 1 103 ? 7.384  18.690  21.599  1.00 16.41  ? 82   ARG A N     1 
ATOM   578  C CA    . ARG A 1 103 ? 6.504  19.664  22.178  1.00 16.38  ? 82   ARG A CA    1 
ATOM   579  C C     . ARG A 1 103 ? 5.958  19.074  23.465  1.00 18.43  ? 82   ARG A C     1 
ATOM   580  O O     . ARG A 1 103 ? 4.827  18.580  23.493  1.00 19.17  ? 82   ARG A O     1 
ATOM   581  C CB    . ARG A 1 103 ? 5.421  20.087  21.180  1.00 19.11  ? 82   ARG A CB    1 
ATOM   582  C CG    . ARG A 1 103 ? 4.702  21.363  21.615  1.00 20.62  ? 82   ARG A CG    1 
ATOM   583  C CD    . ARG A 1 103 ? 3.566  21.715  20.654  1.00 26.42  ? 82   ARG A CD    1 
ATOM   584  N NE    . ARG A 1 103 ? 3.207  23.143  20.717  1.00 32.93  ? 82   ARG A NE    1 
ATOM   585  C CZ    . ARG A 1 103 ? 2.227  23.645  21.470  1.00 32.25  ? 82   ARG A CZ    1 
ATOM   586  N NH1   . ARG A 1 103 ? 1.936  24.926  21.404  1.00 28.51  ? 82   ARG A NH1   1 
ATOM   587  N NH2   . ARG A 1 103 ? 1.518  22.854  22.257  1.00 30.06  ? 82   ARG A NH2   1 
ATOM   588  N N     . THR A 1 104 ? 6.806  19.092  24.500  1.00 17.40  ? 83   THR A N     1 
ATOM   589  C CA    . THR A 1 104 ? 6.526  18.421  25.764  1.00 18.59  ? 83   THR A CA    1 
ATOM   590  C C     . THR A 1 104 ? 7.725  18.654  26.675  1.00 19.31  ? 83   THR A C     1 
ATOM   591  O O     . THR A 1 104 ? 8.757  19.159  26.231  1.00 19.98  ? 83   THR A O     1 
ATOM   592  C CB    . THR A 1 104 ? 6.248  16.929  25.545  1.00 19.95  ? 83   THR A CB    1 
ATOM   593  O OG1   . THR A 1 104 ? 5.807  16.280  26.743  1.00 20.70  ? 83   THR A OG1   1 
ATOM   594  C CG2   . THR A 1 104 ? 7.455  16.176  25.004  1.00 20.03  ? 83   THR A CG2   1 
ATOM   595  N N     . LEU A 1 105 ? 7.623  18.231  27.944  1.00 19.55  ? 84   LEU A N     1 
ATOM   596  C CA    . LEU A 1 105 ? 8.807  18.287  28.796  1.00 18.67  ? 84   LEU A CA    1 
ATOM   597  C C     . LEU A 1 105 ? 9.859  17.363  28.219  1.00 17.82  ? 84   LEU A C     1 
ATOM   598  O O     . LEU A 1 105 ? 9.553  16.205  27.956  1.00 17.91  ? 84   LEU A O     1 
ATOM   599  C CB    . LEU A 1 105 ? 8.470  17.887  30.227  1.00 20.14  ? 84   LEU A CB    1 
ATOM   600  C CG    . LEU A 1 105 ? 7.524  18.848  30.951  1.00 19.86  ? 84   LEU A CG    1 
ATOM   601  C CD1   . LEU A 1 105 ? 7.250  18.257  32.345  1.00 23.01  ? 84   LEU A CD1   1 
ATOM   602  C CD2   . LEU A 1 105 ? 8.092  20.248  31.059  1.00 20.42  ? 84   LEU A CD2   1 
ATOM   603  N N     . GLY A 1 106 ? 11.092 17.888  28.085  1.00 16.40  ? 85   GLY A N     1 
ATOM   604  C CA    . GLY A 1 106 ? 12.189 17.194  27.445  1.00 15.75  ? 85   GLY A CA    1 
ATOM   605  C C     . GLY A 1 106 ? 12.354 17.592  25.977  1.00 16.65  ? 85   GLY A C     1 
ATOM   606  O O     . GLY A 1 106 ? 13.334 17.202  25.336  1.00 19.24  ? 85   GLY A O     1 
ATOM   607  N N     . GLY A 1 107 ? 11.394 18.336  25.443  1.00 16.20  ? 86   GLY A N     1 
ATOM   608  C CA    . GLY A 1 107 ? 11.464 18.778  24.067  1.00 16.19  ? 86   GLY A CA    1 
ATOM   609  C C     . GLY A 1 107 ? 11.695 17.622  23.114  1.00 16.26  ? 86   GLY A C     1 
ATOM   610  O O     . GLY A 1 107 ? 11.117 16.532  23.229  1.00 15.88  ? 86   GLY A O     1 
ATOM   611  N N     . SER A 1 108 ? 12.610 17.870  22.193  1.00 17.47  ? 87   SER A N     1 
ATOM   612  C CA    . SER A 1 108 ? 12.903 16.893  21.177  1.00 17.70  ? 87   SER A CA    1 
ATOM   613  C C     . SER A 1 108 ? 13.626 15.681  21.783  1.00 18.97  ? 87   SER A C     1 
ATOM   614  O O     . SER A 1 108 ? 13.618 14.627  21.147  1.00 17.68  ? 87   SER A O     1 
ATOM   615  C CB    . SER A 1 108 ? 13.668 17.534  20.019  1.00 17.12  ? 87   SER A CB    1 
ATOM   616  O OG    . SER A 1 108 ? 12.903 18.546  19.351  1.00 16.31  ? 87   SER A OG    1 
ATOM   617  N N     . SER A 1 109 ? 14.239 15.797  22.990  1.00 17.35  ? 88   SER A N     1 
ATOM   618  C CA    . SER A 1 109 ? 14.846 14.626  23.617  1.00 16.48  ? 88   SER A CA    1 
ATOM   619  C C     . SER A 1 109 ? 13.781 13.623  24.055  1.00 16.05  ? 88   SER A C     1 
ATOM   620  O O     . SER A 1 109 ? 14.125 12.483  24.341  1.00 18.63  ? 88   SER A O     1 
ATOM   621  C CB    . SER A 1 109 ? 15.756 14.957  24.805  1.00 17.28  ? 88   SER A CB    1 
ATOM   622  O OG    . SER A 1 109 ? 15.017 15.232  25.985  1.00 16.37  ? 88   SER A OG    1 
ATOM   623  N N     . SER A 1 110 ? 12.502 14.043  24.090  1.00 16.09  ? 89   SER A N     1 
ATOM   624  C CA    . SER A 1 110 ? 11.402 13.146  24.430  1.00 17.22  ? 89   SER A CA    1 
ATOM   625  C C     . SER A 1 110 ? 10.801 12.438  23.216  1.00 17.39  ? 89   SER A C     1 
ATOM   626  O O     . SER A 1 110 ? 9.970  11.555  23.404  1.00 17.41  ? 89   SER A O     1 
ATOM   627  C CB    . SER A 1 110 ? 10.315 13.874  25.192  1.00 16.19  ? 89   SER A CB    1 
ATOM   628  O OG    . SER A 1 110 ? 10.813 14.337  26.435  1.00 18.35  ? 89   SER A OG    1 
ATOM   629  N N     . VAL A 1 111 ? 11.141 12.841  21.976  1.00 18.52  ? 90   VAL A N     1 
ATOM   630  C CA    . VAL A 1 111 ? 10.498 12.285  20.795  1.00 16.79  ? 90   VAL A CA    1 
ATOM   631  C C     . VAL A 1 111 ? 11.531 11.760  19.792  1.00 18.48  ? 90   VAL A C     1 
ATOM   632  O O     . VAL A 1 111 ? 11.155 11.200  18.753  1.00 17.43  ? 90   VAL A O     1 
ATOM   633  C CB    . VAL A 1 111 ? 9.543  13.297  20.113  1.00 18.95  ? 90   VAL A CB    1 
ATOM   634  C CG1   . VAL A 1 111 ? 8.551  13.928  21.086  1.00 18.58  ? 90   VAL A CG1   1 
ATOM   635  C CG2   . VAL A 1 111 ? 10.307 14.361  19.332  1.00 19.16  ? 90   VAL A CG2   1 
ATOM   636  N N     . ASN A 1 112 ? 12.834 11.876  20.116  1.00 18.23  ? 91   ASN A N     1 
ATOM   637  C CA    . ASN A 1 112 ? 13.872 11.615  19.142  1.00 17.25  ? 91   ASN A CA    1 
ATOM   638  C C     . ASN A 1 112 ? 14.163 10.121  19.072  1.00 17.36  ? 91   ASN A C     1 
ATOM   639  O O     . ASN A 1 112 ? 13.535 9.332   19.773  1.00 18.16  ? 91   ASN A O     1 
ATOM   640  C CB    . ASN A 1 112 ? 15.083 12.510  19.400  1.00 17.50  ? 91   ASN A CB    1 
ATOM   641  C CG    . ASN A 1 112 ? 15.932 12.138  20.595  1.00 18.30  ? 91   ASN A CG    1 
ATOM   642  O OD1   . ASN A 1 112 ? 15.749 11.093  21.234  1.00 15.35  ? 91   ASN A OD1   1 
ATOM   643  N ND2   . ASN A 1 112 ? 16.938 12.963  20.861  1.00 17.49  ? 91   ASN A ND2   1 
ATOM   644  N N     . PHE A 1 113 ? 15.171 9.736   18.278  1.00 16.87  ? 92   PHE A N     1 
ATOM   645  C CA    . PHE A 1 113 ? 15.429 8.323   18.058  1.00 17.97  ? 92   PHE A CA    1 
ATOM   646  C C     . PHE A 1 113 ? 16.529 7.761   18.961  1.00 17.69  ? 92   PHE A C     1 
ATOM   647  O O     . PHE A 1 113 ? 17.054 6.665   18.680  1.00 17.48  ? 92   PHE A O     1 
ATOM   648  C CB    . PHE A 1 113 ? 15.690 8.089   16.572  1.00 19.65  ? 92   PHE A CB    1 
ATOM   649  C CG    . PHE A 1 113 ? 14.522 8.438   15.667  1.00 21.91  ? 92   PHE A CG    1 
ATOM   650  C CD1   . PHE A 1 113 ? 13.202 8.205   16.060  1.00 26.90  ? 92   PHE A CD1   1 
ATOM   651  C CD2   . PHE A 1 113 ? 14.735 9.059   14.442  1.00 26.35  ? 92   PHE A CD2   1 
ATOM   652  C CE1   . PHE A 1 113 ? 12.143 8.537   15.225  1.00 28.69  ? 92   PHE A CE1   1 
ATOM   653  C CE2   . PHE A 1 113 ? 13.667 9.360   13.603  1.00 25.82  ? 92   PHE A CE2   1 
ATOM   654  C CZ    . PHE A 1 113 ? 12.384 9.136   14.012  1.00 25.37  ? 92   PHE A CZ    1 
ATOM   655  N N     . LEU A 1 114 ? 16.770 8.451   20.083  1.00 16.55  ? 93   LEU A N     1 
ATOM   656  C CA    . LEU A 1 114 ? 17.588 7.973   21.191  1.00 16.71  ? 93   LEU A CA    1 
ATOM   657  C C     . LEU A 1 114 ? 19.062 7.731   20.846  1.00 18.33  ? 93   LEU A C     1 
ATOM   658  O O     . LEU A 1 114 ? 19.785 7.131   21.654  1.00 17.15  ? 93   LEU A O     1 
ATOM   659  C CB    . LEU A 1 114 ? 16.961 6.716   21.776  1.00 17.11  ? 93   LEU A CB    1 
ATOM   660  C CG    . LEU A 1 114 ? 15.519 6.857   22.255  1.00 17.25  ? 93   LEU A CG    1 
ATOM   661  C CD1   . LEU A 1 114 ? 14.493 6.420   21.199  1.00 18.45  ? 93   LEU A CD1   1 
ATOM   662  C CD2   . LEU A 1 114 ? 15.319 6.013   23.474  1.00 19.57  ? 93   LEU A CD2   1 
ATOM   663  N N     . MET A 1 115 ? 19.535 8.252   19.717  1.00 15.90  ? 94   MET A N     1 
ATOM   664  C CA    . MET A 1 115 ? 20.907 8.041   19.299  1.00 17.14  ? 94   MET A CA    1 
ATOM   665  C C     . MET A 1 115 ? 21.833 9.042   19.994  1.00 17.24  ? 94   MET A C     1 
ATOM   666  O O     . MET A 1 115 ? 21.593 10.239  19.952  1.00 18.63  ? 94   MET A O     1 
ATOM   667  C CB    . MET A 1 115 ? 21.043 8.173   17.782  1.00 17.99  ? 94   MET A CB    1 
ATOM   668  C CG    . MET A 1 115 ? 20.099 7.253   17.023  1.00 18.45  ? 94   MET A CG    1 
ATOM   669  S SD    . MET A 1 115 ? 20.200 7.515   15.247  1.00 20.23  ? 94   MET A SD    1 
ATOM   670  C CE    . MET A 1 115 ? 21.692 6.559   14.900  1.00 19.68  ? 94   MET A CE    1 
ATOM   671  N N     . TRP A 1 116 ? 22.830 8.524   20.727  1.00 16.52  ? 95   TRP A N     1 
ATOM   672  C CA    . TRP A 1 116 ? 23.844 9.385   21.299  1.00 17.42  ? 95   TRP A CA    1 
ATOM   673  C C     . TRP A 1 116 ? 25.107 9.199   20.476  1.00 17.89  ? 95   TRP A C     1 
ATOM   674  O O     . TRP A 1 116 ? 25.782 8.181   20.604  1.00 20.26  ? 95   TRP A O     1 
ATOM   675  C CB    . TRP A 1 116 ? 24.103 9.080   22.778  1.00 18.11  ? 95   TRP A CB    1 
ATOM   676  C CG    . TRP A 1 116 ? 25.045 10.044  23.459  1.00 17.22  ? 95   TRP A CG    1 
ATOM   677  C CD1   . TRP A 1 116 ? 26.379 9.875   23.660  1.00 18.27  ? 95   TRP A CD1   1 
ATOM   678  C CD2   . TRP A 1 116 ? 24.700 11.321  24.039  1.00 18.23  ? 95   TRP A CD2   1 
ATOM   679  N NE1   . TRP A 1 116 ? 26.889 10.954  24.334  1.00 20.85  ? 95   TRP A NE1   1 
ATOM   680  C CE2   . TRP A 1 116 ? 25.887 11.860  24.577  1.00 18.68  ? 95   TRP A CE2   1 
ATOM   681  C CE3   . TRP A 1 116 ? 23.513 12.059  24.152  1.00 18.41  ? 95   TRP A CE3   1 
ATOM   682  C CZ2   . TRP A 1 116 ? 25.911 13.069  25.262  1.00 19.40  ? 95   TRP A CZ2   1 
ATOM   683  C CZ3   . TRP A 1 116 ? 23.534 13.263  24.836  1.00 21.45  ? 95   TRP A CZ3   1 
ATOM   684  C CH2   . TRP A 1 116 ? 24.723 13.757  25.386  1.00 22.23  ? 95   TRP A CH2   1 
ATOM   685  N N     . VAL A 1 117 ? 25.349 10.172  19.610  1.00 18.75  ? 96   VAL A N     1 
ATOM   686  C CA    . VAL A 1 117 ? 26.370 10.114  18.578  1.00 20.14  ? 96   VAL A CA    1 
ATOM   687  C C     . VAL A 1 117 ? 27.005 11.498  18.556  1.00 19.28  ? 96   VAL A C     1 
ATOM   688  O O     . VAL A 1 117 ? 26.672 12.341  17.742  1.00 19.01  ? 96   VAL A O     1 
ATOM   689  C CB    . VAL A 1 117 ? 25.800 9.700   17.217  1.00 22.58  ? 96   VAL A CB    1 
ATOM   690  C CG1   . VAL A 1 117 ? 26.899 9.578   16.150  1.00 26.21  ? 96   VAL A CG1   1 
ATOM   691  C CG2   . VAL A 1 117 ? 25.042 8.393   17.334  1.00 23.56  ? 96   VAL A CG2   1 
ATOM   692  N N     . PRO A 1 118 ? 27.908 11.763  19.510  1.00 20.85  ? 97   PRO A N     1 
ATOM   693  C CA    . PRO A 1 118 ? 28.289 13.134  19.852  1.00 23.61  ? 97   PRO A CA    1 
ATOM   694  C C     . PRO A 1 118 ? 29.226 13.933  18.959  1.00 26.04  ? 97   PRO A C     1 
ATOM   695  O O     . PRO A 1 118 ? 29.536 15.079  19.292  1.00 31.13  ? 97   PRO A O     1 
ATOM   696  C CB    . PRO A 1 118 ? 28.911 12.952  21.265  1.00 25.56  ? 97   PRO A CB    1 
ATOM   697  C CG    . PRO A 1 118 ? 29.423 11.546  21.295  1.00 25.35  ? 97   PRO A CG    1 
ATOM   698  C CD    . PRO A 1 118 ? 28.493 10.754  20.399  1.00 21.13  ? 97   PRO A CD    1 
ATOM   699  N N     . GLY A 1 119 ? 29.640 13.391  17.810  1.00 22.29  ? 98   GLY A N     1 
ATOM   700  C CA    . GLY A 1 119 ? 30.393 14.241  16.910  1.00 23.79  ? 98   GLY A CA    1 
ATOM   701  C C     . GLY A 1 119 ? 31.910 14.032  17.010  1.00 25.99  ? 98   GLY A C     1 
ATOM   702  O O     . GLY A 1 119 ? 32.373 13.208  17.792  1.00 27.61  ? 98   GLY A O     1 
ATOM   703  N N     . HIS A 1 120 ? 32.648 14.796  16.185  1.00 27.42  ? 99   HIS A N     1 
ATOM   704  C CA    . HIS A 1 120 ? 34.095 14.708  16.036  1.00 30.79  ? 99   HIS A CA    1 
ATOM   705  C C     . HIS A 1 120 ? 34.769 15.967  16.594  1.00 27.60  ? 99   HIS A C     1 
ATOM   706  O O     . HIS A 1 120 ? 34.237 17.064  16.470  1.00 24.91  ? 99   HIS A O     1 
ATOM   707  C CB    . HIS A 1 120 ? 34.433 14.469  14.563  1.00 38.27  ? 99   HIS A CB    1 
ATOM   708  C CG    . HIS A 1 120 ? 35.860 14.105  14.349  1.00 52.43  ? 99   HIS A CG    1 
ATOM   709  N ND1   . HIS A 1 120 ? 36.896 15.025  14.298  1.00 50.99  ? 99   HIS A ND1   1 
ATOM   710  C CD2   . HIS A 1 120 ? 36.424 12.889  14.215  1.00 60.62  ? 99   HIS A CD2   1 
ATOM   711  C CE1   . HIS A 1 120 ? 38.045 14.381  14.156  1.00 56.76  ? 99   HIS A CE1   1 
ATOM   712  N NE2   . HIS A 1 120 ? 37.786 13.082  14.094  1.00 62.96  ? 99   HIS A NE2   1 
ATOM   713  N N     . ALA A 1 121 ? 35.969 15.821  17.188  1.00 28.13  ? 100  ALA A N     1 
ATOM   714  C CA    . ALA A 1 121 ? 36.665 16.925  17.837  1.00 27.33  ? 100  ALA A CA    1 
ATOM   715  C C     . ALA A 1 121 ? 36.914 18.088  16.874  1.00 24.85  ? 100  ALA A C     1 
ATOM   716  O O     . ALA A 1 121 ? 36.931 19.257  17.276  1.00 26.64  ? 100  ALA A O     1 
ATOM   717  C CB    . ALA A 1 121 ? 37.967 16.398  18.457  1.00 32.88  ? 100  ALA A CB    1 
ATOM   718  N N     . GLU A 1 122 ? 37.089 17.791  15.590  1.00 23.56  ? 101  GLU A N     1 
ATOM   719  C CA    . GLU A 1 122 ? 37.363 18.816  14.593  1.00 26.81  ? 101  GLU A CA    1 
ATOM   720  C C     . GLU A 1 122 ? 36.148 19.682  14.277  1.00 24.02  ? 101  GLU A C     1 
ATOM   721  O O     . GLU A 1 122 ? 36.277 20.728  13.647  1.00 25.99  ? 101  GLU A O     1 
ATOM   722  C CB    . GLU A 1 122 ? 37.851 18.135  13.322  1.00 28.82  ? 101  GLU A CB    1 
ATOM   723  C CG    . GLU A 1 122 ? 39.253 17.596  13.550  1.00 34.02  ? 101  GLU A CG    1 
ATOM   724  C CD    . GLU A 1 122 ? 39.812 16.844  12.366  1.00 39.74  ? 101  GLU A CD    1 
ATOM   725  O OE1   . GLU A 1 122 ? 40.464 15.782  12.615  1.00 48.07  ? 101  GLU A OE1   1 
ATOM   726  O OE2   . GLU A 1 122 ? 39.580 17.326  11.221  1.00 41.34  ? 101  GLU A OE2   1 
ATOM   727  N N     . ASP A 1 123 ? 34.962 19.249  14.717  1.00 24.93  ? 102  ASP A N     1 
ATOM   728  C CA    . ASP A 1 123 ? 33.734 19.996  14.486  1.00 22.28  ? 102  ASP A CA    1 
ATOM   729  C C     . ASP A 1 123 ? 33.822 21.353  15.160  1.00 21.24  ? 102  ASP A C     1 
ATOM   730  O O     . ASP A 1 123 ? 33.151 22.274  14.708  1.00 27.24  ? 102  ASP A O     1 
ATOM   731  C CB    . ASP A 1 123 ? 32.519 19.225  14.996  1.00 23.52  ? 102  ASP A CB    1 
ATOM   732  C CG    . ASP A 1 123 ? 32.247 17.886  14.310  1.00 25.13  ? 102  ASP A CG    1 
ATOM   733  O OD1   . ASP A 1 123 ? 32.902 17.597  13.262  1.00 27.48  ? 102  ASP A OD1   1 
ATOM   734  O OD2   . ASP A 1 123 ? 31.405 17.112  14.851  1.00 25.21  ? 102  ASP A OD2   1 
ATOM   735  N N     . TYR A 1 124 ? 34.632 21.457  16.230  1.00 20.21  ? 103  TYR A N     1 
ATOM   736  C CA    . TYR A 1 124 ? 34.734 22.669  17.032  1.00 22.75  ? 103  TYR A CA    1 
ATOM   737  C C     . TYR A 1 124 ? 35.687 23.712  16.451  1.00 23.43  ? 103  TYR A C     1 
ATOM   738  O O     . TYR A 1 124 ? 35.660 24.870  16.882  1.00 23.79  ? 103  TYR A O     1 
ATOM   739  C CB    . TYR A 1 124 ? 35.109 22.332  18.472  1.00 24.04  ? 103  TYR A CB    1 
ATOM   740  C CG    . TYR A 1 124 ? 33.986 21.527  19.103  1.00 25.06  ? 103  TYR A CG    1 
ATOM   741  C CD1   . TYR A 1 124 ? 32.803 22.128  19.528  1.00 25.15  ? 103  TYR A CD1   1 
ATOM   742  C CD2   . TYR A 1 124 ? 34.050 20.130  19.105  1.00 28.32  ? 103  TYR A CD2   1 
ATOM   743  C CE1   . TYR A 1 124 ? 31.735 21.365  19.994  1.00 27.42  ? 103  TYR A CE1   1 
ATOM   744  C CE2   . TYR A 1 124 ? 32.997 19.366  19.585  1.00 27.81  ? 103  TYR A CE2   1 
ATOM   745  C CZ    . TYR A 1 124 ? 31.851 19.980  20.059  1.00 27.00  ? 103  TYR A CZ    1 
ATOM   746  O OH    . TYR A 1 124 ? 30.863 19.159  20.526  1.00 25.63  ? 103  TYR A OH    1 
ATOM   747  N N     . GLU A 1 125 ? 36.433 23.352  15.408  1.00 24.66  ? 104  GLU A N     1 
ATOM   748  C CA    . GLU A 1 125 ? 37.327 24.310  14.769  1.00 26.74  ? 104  GLU A CA    1 
ATOM   749  C C     . GLU A 1 125 ? 36.541 25.518  14.265  1.00 26.49  ? 104  GLU A C     1 
ATOM   750  O O     . GLU A 1 125 ? 36.928 26.658  14.531  1.00 24.77  ? 104  GLU A O     1 
ATOM   751  C CB    . GLU A 1 125 ? 38.146 23.692  13.632  1.00 26.70  ? 104  GLU A CB    1 
ATOM   752  C CG    . GLU A 1 125 ? 39.118 22.626  14.114  1.00 29.88  ? 104  GLU A CG    1 
ATOM   753  C CD    . GLU A 1 125 ? 39.817 21.862  12.999  1.00 34.54  ? 104  GLU A CD    1 
ATOM   754  O OE1   . GLU A 1 125 ? 40.584 20.940  13.285  1.00 38.67  ? 104  GLU A OE1   1 
ATOM   755  O OE2   . GLU A 1 125 ? 39.589 22.186  11.828  1.00 42.26  ? 104  GLU A OE2   1 
ATOM   756  N N     . PRO A 1 126 ? 35.430 25.361  13.505  1.00 25.90  ? 105  PRO A N     1 
ATOM   757  C CA    . PRO A 1 126 ? 34.638 26.530  13.126  1.00 26.11  ? 105  PRO A CA    1 
ATOM   758  C C     . PRO A 1 126 ? 33.927 27.257  14.268  1.00 26.53  ? 105  PRO A C     1 
ATOM   759  O O     . PRO A 1 126 ? 33.622 28.440  14.118  1.00 25.70  ? 105  PRO A O     1 
ATOM   760  C CB    . PRO A 1 126 ? 33.672 26.017  12.034  1.00 26.81  ? 105  PRO A CB    1 
ATOM   761  C CG    . PRO A 1 126 ? 33.648 24.519  12.247  1.00 27.76  ? 105  PRO A CG    1 
ATOM   762  C CD    . PRO A 1 126 ? 34.983 24.130  12.842  1.00 28.89  ? 105  PRO A CD    1 
ATOM   763  N N     . TRP A 1 127 ? 33.697 26.582  15.409  1.00 24.91  ? 106  TRP A N     1 
ATOM   764  C CA    . TRP A 1 127 ? 33.160 27.272  16.575  1.00 25.81  ? 106  TRP A CA    1 
ATOM   765  C C     . TRP A 1 127 ? 34.216 28.176  17.196  1.00 23.92  ? 106  TRP A C     1 
ATOM   766  O O     . TRP A 1 127 ? 33.933 29.326  17.484  1.00 22.74  ? 106  TRP A O     1 
ATOM   767  C CB    . TRP A 1 127 ? 32.668 26.334  17.673  1.00 24.70  ? 106  TRP A CB    1 
ATOM   768  C CG    . TRP A 1 127 ? 31.598 25.361  17.302  1.00 26.82  ? 106  TRP A CG    1 
ATOM   769  C CD1   . TRP A 1 127 ? 31.437 24.677  16.130  1.00 28.62  ? 106  TRP A CD1   1 
ATOM   770  C CD2   . TRP A 1 127 ? 30.584 24.864  18.214  1.00 25.79  ? 106  TRP A CD2   1 
ATOM   771  N NE1   . TRP A 1 127 ? 30.402 23.778  16.260  1.00 31.90  ? 106  TRP A NE1   1 
ATOM   772  C CE2   . TRP A 1 127 ? 29.857 23.874  17.523  1.00 26.94  ? 106  TRP A CE2   1 
ATOM   773  C CE3   . TRP A 1 127 ? 30.210 25.176  19.518  1.00 24.45  ? 106  TRP A CE3   1 
ATOM   774  C CZ2   . TRP A 1 127 ? 28.790 23.194  18.111  1.00 26.57  ? 106  TRP A CZ2   1 
ATOM   775  C CZ3   . TRP A 1 127 ? 29.163 24.506  20.100  1.00 24.91  ? 106  TRP A CZ3   1 
ATOM   776  C CH2   . TRP A 1 127 ? 28.476 23.514  19.414  1.00 25.92  ? 106  TRP A CH2   1 
ATOM   777  N N     . ALA A 1 128 ? 35.418 27.633  17.418  1.00 27.07  ? 107  ALA A N     1 
ATOM   778  C CA    . ALA A 1 128 ? 36.538 28.431  17.909  1.00 28.37  ? 107  ALA A CA    1 
ATOM   779  C C     . ALA A 1 128 ? 36.869 29.570  16.928  1.00 28.32  ? 107  ALA A C     1 
ATOM   780  O O     . ALA A 1 128 ? 37.169 30.669  17.370  1.00 31.07  ? 107  ALA A O     1 
ATOM   781  C CB    . ALA A 1 128 ? 37.727 27.540  18.221  1.00 26.48  ? 107  ALA A CB    1 
ATOM   782  N N     . ARG A 1 129 ? 36.735 29.362  15.613  1.00 27.04  ? 108  ARG A N     1 
ATOM   783  C CA    . ARG A 1 129 ? 36.973 30.429  14.646  1.00 31.22  ? 108  ARG A CA    1 
ATOM   784  C C     . ARG A 1 129 ? 35.954 31.550  14.840  1.00 31.01  ? 108  ARG A C     1 
ATOM   785  O O     . ARG A 1 129 ? 36.311 32.724  14.807  1.00 28.73  ? 108  ARG A O     1 
ATOM   786  C CB    . ARG A 1 129 ? 36.957 29.987  13.172  1.00 36.13  ? 108  ARG A CB    1 
ATOM   787  C CG    . ARG A 1 129 ? 38.284 29.397  12.706  1.00 45.37  ? 108  ARG A CG    1 
ATOM   788  C CD    . ARG A 1 129 ? 38.466 29.362  11.189  1.00 49.46  ? 108  ARG A CD    1 
ATOM   789  N NE    . ARG A 1 129 ? 37.578 28.385  10.547  1.00 54.16  ? 108  ARG A NE    1 
ATOM   790  C CZ    . ARG A 1 129 ? 37.671 27.054  10.672  1.00 53.62  ? 108  ARG A CZ    1 
ATOM   791  N NH1   . ARG A 1 129 ? 38.703 26.491  11.284  1.00 53.56  ? 108  ARG A NH1   1 
ATOM   792  N NH2   . ARG A 1 129 ? 36.733 26.283  10.165  1.00 47.28  ? 108  ARG A NH2   1 
ATOM   793  N N     . ALA A 1 130 ? 34.696 31.191  15.102  1.00 25.54  ? 109  ALA A N     1 
ATOM   794  C CA    . ALA A 1 130 ? 33.633 32.178  15.261  1.00 26.00  ? 109  ALA A CA    1 
ATOM   795  C C     . ALA A 1 130 ? 33.713 32.887  16.615  1.00 27.12  ? 109  ALA A C     1 
ATOM   796  O O     . ALA A 1 130 ? 33.447 34.083  16.704  1.00 27.83  ? 109  ALA A O     1 
ATOM   797  C CB    . ALA A 1 130 ? 32.294 31.483  15.124  1.00 24.20  ? 109  ALA A CB    1 
ATOM   798  N N     . ALA A 1 131 ? 33.970 32.127  17.694  1.00 25.48  ? 110  ALA A N     1 
ATOM   799  C CA    . ALA A 1 131 ? 33.626 32.591  19.025  1.00 28.40  ? 110  ALA A CA    1 
ATOM   800  C C     . ALA A 1 131 ? 34.788 32.454  20.004  1.00 28.82  ? 110  ALA A C     1 
ATOM   801  O O     . ALA A 1 131 ? 34.613 32.761  21.171  1.00 26.38  ? 110  ALA A O     1 
ATOM   802  C CB    . ALA A 1 131 ? 32.386 31.878  19.538  1.00 27.03  ? 110  ALA A CB    1 
ATOM   803  N N     . GLY A 1 132 ? 35.951 31.998  19.524  1.00 31.08  ? 111  GLY A N     1 
ATOM   804  C CA    . GLY A 1 132 ? 37.153 31.959  20.334  1.00 30.65  ? 111  GLY A CA    1 
ATOM   805  C C     . GLY A 1 132 ? 37.322 30.630  21.064  1.00 35.27  ? 111  GLY A C     1 
ATOM   806  O O     . GLY A 1 132 ? 36.526 29.704  20.895  1.00 28.21  ? 111  GLY A O     1 
ATOM   807  N N     . ASP A 1 133 ? 38.353 30.596  21.922  1.00 36.79  ? 112  ASP A N     1 
ATOM   808  C CA    . ASP A 1 133 ? 38.842 29.380  22.551  1.00 39.01  ? 112  ASP A CA    1 
ATOM   809  C C     . ASP A 1 133 ? 37.912 28.881  23.642  1.00 31.01  ? 112  ASP A C     1 
ATOM   810  O O     . ASP A 1 133 ? 38.037 27.738  24.046  1.00 33.00  ? 112  ASP A O     1 
ATOM   811  C CB    . ASP A 1 133 ? 40.254 29.563  23.085  1.00 47.47  ? 112  ASP A CB    1 
ATOM   812  C CG    . ASP A 1 133 ? 41.329 29.247  22.059  1.00 54.12  ? 112  ASP A CG    1 
ATOM   813  O OD1   . ASP A 1 133 ? 41.020 28.483  21.107  1.00 56.12  ? 112  ASP A OD1   1 
ATOM   814  O OD2   . ASP A 1 133 ? 42.445 29.804  22.192  1.00 67.71  ? 112  ASP A OD2   1 
ATOM   815  N N     . LEU A 1 134 ? 36.977 29.717  24.087  1.00 32.17  ? 113  LEU A N     1 
ATOM   816  C CA    . LEU A 1 134 ? 35.873 29.272  24.914  1.00 32.28  ? 113  LEU A CA    1 
ATOM   817  C C     . LEU A 1 134 ? 35.120 28.098  24.286  1.00 28.93  ? 113  LEU A C     1 
ATOM   818  O O     . LEU A 1 134 ? 34.525 27.320  25.019  1.00 26.37  ? 113  LEU A O     1 
ATOM   819  C CB    . LEU A 1 134 ? 34.863 30.388  25.153  1.00 37.30  ? 113  LEU A CB    1 
ATOM   820  C CG    . LEU A 1 134 ? 34.978 31.168  26.463  1.00 40.67  ? 113  LEU A CG    1 
ATOM   821  C CD1   . LEU A 1 134 ? 33.778 32.114  26.541  1.00 39.47  ? 113  LEU A CD1   1 
ATOM   822  C CD2   . LEU A 1 134 ? 35.058 30.292  27.693  1.00 37.95  ? 113  LEU A CD2   1 
ATOM   823  N N     . TRP A 1 135 ? 35.120 28.012  22.953  1.00 26.60  ? 114  TRP A N     1 
ATOM   824  C CA    . TRP A 1 135 ? 34.334 27.017  22.244  1.00 24.70  ? 114  TRP A CA    1 
ATOM   825  C C     . TRP A 1 135 ? 35.245 26.111  21.426  1.00 25.15  ? 114  TRP A C     1 
ATOM   826  O O     . TRP A 1 135 ? 34.815 25.447  20.484  1.00 23.09  ? 114  TRP A O     1 
ATOM   827  C CB    . TRP A 1 135 ? 33.261 27.695  21.384  1.00 23.96  ? 114  TRP A CB    1 
ATOM   828  C CG    . TRP A 1 135 ? 32.191 28.324  22.234  1.00 23.79  ? 114  TRP A CG    1 
ATOM   829  C CD1   . TRP A 1 135 ? 32.120 29.637  22.583  1.00 25.05  ? 114  TRP A CD1   1 
ATOM   830  C CD2   . TRP A 1 135 ? 31.082 27.677  22.894  1.00 24.40  ? 114  TRP A CD2   1 
ATOM   831  N NE1   . TRP A 1 135 ? 31.062 29.865  23.415  1.00 23.27  ? 114  TRP A NE1   1 
ATOM   832  C CE2   . TRP A 1 135 ? 30.394 28.681  23.610  1.00 24.77  ? 114  TRP A CE2   1 
ATOM   833  C CE3   . TRP A 1 135 ? 30.588 26.371  22.941  1.00 24.46  ? 114  TRP A CE3   1 
ATOM   834  C CZ2   . TRP A 1 135 ? 29.251 28.407  24.363  1.00 24.57  ? 114  TRP A CZ2   1 
ATOM   835  C CZ3   . TRP A 1 135 ? 29.461 26.101  23.691  1.00 26.24  ? 114  TRP A CZ3   1 
ATOM   836  C CH2   . TRP A 1 135 ? 28.787 27.112  24.374  1.00 25.79  ? 114  TRP A CH2   1 
ATOM   837  N N     . SER A 1 136 ? 36.493 25.956  21.881  1.00 25.05  ? 115  SER A N     1 
ATOM   838  C CA    . SER A 1 136 ? 37.337 24.929  21.311  1.00 23.51  ? 115  SER A CA    1 
ATOM   839  C C     . SER A 1 136 ? 36.928 23.573  21.874  1.00 24.55  ? 115  SER A C     1 
ATOM   840  O O     . SER A 1 136 ? 36.294 23.502  22.930  1.00 24.02  ? 115  SER A O     1 
ATOM   841  C CB    . SER A 1 136 ? 38.783 25.197  21.647  1.00 27.67  ? 115  SER A CB    1 
ATOM   842  O OG    . SER A 1 136 ? 38.902 25.155  23.054  1.00 23.46  ? 115  SER A OG    1 
ATOM   843  N N     . TRP A 1 137 ? 37.423 22.506  21.239  1.00 23.15  ? 116  TRP A N     1 
ATOM   844  C CA    . TRP A 1 137 ? 37.155 21.159  21.718  1.00 26.01  ? 116  TRP A CA    1 
ATOM   845  C C     . TRP A 1 137 ? 37.632 20.985  23.157  1.00 25.98  ? 116  TRP A C     1 
ATOM   846  O O     . TRP A 1 137 ? 36.905 20.472  24.017  1.00 23.12  ? 116  TRP A O     1 
ATOM   847  C CB    . TRP A 1 137 ? 37.788 20.134  20.773  1.00 27.31  ? 116  TRP A CB    1 
ATOM   848  C CG    . TRP A 1 137 ? 37.826 18.747  21.343  1.00 28.09  ? 116  TRP A CG    1 
ATOM   849  C CD1   . TRP A 1 137 ? 38.927 17.958  21.444  1.00 30.11  ? 116  TRP A CD1   1 
ATOM   850  C CD2   . TRP A 1 137 ? 36.707 17.966  21.821  1.00 28.46  ? 116  TRP A CD2   1 
ATOM   851  N NE1   . TRP A 1 137 ? 38.584 16.756  22.004  1.00 31.74  ? 116  TRP A NE1   1 
ATOM   852  C CE2   . TRP A 1 137 ? 37.231 16.724  22.240  1.00 32.86  ? 116  TRP A CE2   1 
ATOM   853  C CE3   . TRP A 1 137 ? 35.328 18.188  21.944  1.00 28.36  ? 116  TRP A CE3   1 
ATOM   854  C CZ2   . TRP A 1 137 ? 36.418 15.704  22.740  1.00 28.65  ? 116  TRP A CZ2   1 
ATOM   855  C CZ3   . TRP A 1 137 ? 34.530 17.182  22.447  1.00 28.16  ? 116  TRP A CZ3   1 
ATOM   856  C CH2   . TRP A 1 137 ? 35.068 15.958  22.829  1.00 28.52  ? 116  TRP A CH2   1 
ATOM   857  N N     . ASP A 1 138 ? 38.859 21.456  23.434  1.00 25.89  ? 117  ASP A N     1 
ATOM   858  C CA    . ASP A 1 138 ? 39.406 21.329  24.768  1.00 25.94  ? 117  ASP A CA    1 
ATOM   859  C C     . ASP A 1 138 ? 38.458 21.977  25.770  1.00 23.92  ? 117  ASP A C     1 
ATOM   860  O O     . ASP A 1 138 ? 38.263 21.439  26.830  1.00 23.66  ? 117  ASP A O     1 
ATOM   861  C CB    . ASP A 1 138 ? 40.819 21.890  24.869  1.00 31.76  ? 117  ASP A CB    1 
ATOM   862  C CG    . ASP A 1 138 ? 41.875 21.016  24.217  1.00 37.12  ? 117  ASP A CG    1 
ATOM   863  O OD1   . ASP A 1 138 ? 41.623 19.808  24.099  1.00 36.19  ? 117  ASP A OD1   1 
ATOM   864  O OD2   . ASP A 1 138 ? 42.898 21.566  23.744  1.00 46.25  ? 117  ASP A OD2   1 
ATOM   865  N N     . ALA A 1 139 ? 37.831 23.103  25.440  1.00 25.48  ? 118  ALA A N     1 
ATOM   866  C CA    . ALA A 1 139 ? 36.933 23.733  26.397  1.00 26.38  ? 118  ALA A CA    1 
ATOM   867  C C     . ALA A 1 139 ? 35.635 22.942  26.565  1.00 24.47  ? 118  ALA A C     1 
ATOM   868  O O     . ALA A 1 139 ? 35.076 22.902  27.666  1.00 26.99  ? 118  ALA A O     1 
ATOM   869  C CB    . ALA A 1 139 ? 36.603 25.148  25.964  1.00 27.94  ? 118  ALA A CB    1 
ATOM   870  N N     . VAL A 1 140 ? 35.105 22.373  25.476  1.00 25.95  ? 119  VAL A N     1 
ATOM   871  C CA    . VAL A 1 140 ? 33.743 21.840  25.551  1.00 26.14  ? 119  VAL A CA    1 
ATOM   872  C C     . VAL A 1 140 ? 33.764 20.404  26.082  1.00 24.16  ? 119  VAL A C     1 
ATOM   873  O O     . VAL A 1 140 ? 32.786 19.943  26.675  1.00 24.05  ? 119  VAL A O     1 
ATOM   874  C CB    . VAL A 1 140 ? 32.917 21.912  24.248  1.00 30.02  ? 119  VAL A CB    1 
ATOM   875  C CG1   . VAL A 1 140 ? 32.940 23.282  23.581  1.00 29.34  ? 119  VAL A CG1   1 
ATOM   876  C CG2   . VAL A 1 140 ? 33.283 20.827  23.275  1.00 33.78  ? 119  VAL A CG2   1 
ATOM   877  N N     . ARG A 1 141 ? 34.854 19.677  25.822  1.00 23.51  ? 120  ARG A N     1 
ATOM   878  C CA    . ARG A 1 141 ? 34.950 18.253  26.078  1.00 22.56  ? 120  ARG A CA    1 
ATOM   879  C C     . ARG A 1 141 ? 34.405 17.903  27.466  1.00 24.64  ? 120  ARG A C     1 
ATOM   880  O O     . ARG A 1 141 ? 33.625 16.963  27.611  1.00 23.53  ? 120  ARG A O     1 
ATOM   881  C CB    . ARG A 1 141 ? 36.389 17.774  25.834  1.00 26.34  ? 120  ARG A CB    1 
ATOM   882  C CG    . ARG A 1 141 ? 36.660 16.353  26.316  1.00 27.97  ? 120  ARG A CG    1 
ATOM   883  C CD    . ARG A 1 141 ? 38.067 15.841  26.008  1.00 33.02  ? 120  ARG A CD    1 
ATOM   884  N NE    . ARG A 1 141 ? 39.044 16.625  26.762  1.00 38.50  ? 120  ARG A NE    1 
ATOM   885  C CZ    . ARG A 1 141 ? 39.913 17.502  26.257  1.00 45.70  ? 120  ARG A CZ    1 
ATOM   886  N NH1   . ARG A 1 141 ? 40.228 17.506  24.980  1.00 48.31  ? 120  ARG A NH1   1 
ATOM   887  N NH2   . ARG A 1 141 ? 40.500 18.368  27.054  1.00 45.93  ? 120  ARG A NH2   1 
ATOM   888  N N     . PRO A 1 142 ? 34.840 18.573  28.560  1.00 25.82  ? 121  PRO A N     1 
ATOM   889  C CA    . PRO A 1 142 ? 34.433 18.154  29.898  1.00 23.99  ? 121  PRO A CA    1 
ATOM   890  C C     . PRO A 1 142 ? 32.941 18.293  30.131  1.00 22.71  ? 121  PRO A C     1 
ATOM   891  O O     . PRO A 1 142 ? 32.374 17.578  30.948  1.00 23.56  ? 121  PRO A O     1 
ATOM   892  C CB    . PRO A 1 142 ? 35.200 19.063  30.883  1.00 28.12  ? 121  PRO A CB    1 
ATOM   893  C CG    . PRO A 1 142 ? 36.137 19.897  30.033  1.00 28.87  ? 121  PRO A CG    1 
ATOM   894  C CD    . PRO A 1 142 ? 35.856 19.640  28.564  1.00 29.00  ? 121  PRO A CD    1 
ATOM   895  N N     . PHE A 1 143 ? 32.353 19.303  29.493  1.00 21.29  ? 122  PHE A N     1 
ATOM   896  C CA    . PHE A 1 143 ? 30.921 19.528  29.568  1.00 21.61  ? 122  PHE A CA    1 
ATOM   897  C C     . PHE A 1 143 ? 30.175 18.381  28.881  1.00 20.40  ? 122  PHE A C     1 
ATOM   898  O O     . PHE A 1 143 ? 29.129 17.968  29.361  1.00 21.97  ? 122  PHE A O     1 
ATOM   899  C CB    . PHE A 1 143 ? 30.558 20.863  28.920  1.00 21.89  ? 122  PHE A CB    1 
ATOM   900  C CG    . PHE A 1 143 ? 31.073 22.023  29.745  1.00 26.80  ? 122  PHE A CG    1 
ATOM   901  C CD1   . PHE A 1 143 ? 30.477 22.344  30.961  1.00 25.88  ? 122  PHE A CD1   1 
ATOM   902  C CD2   . PHE A 1 143 ? 32.243 22.675  29.390  1.00 27.99  ? 122  PHE A CD2   1 
ATOM   903  C CE1   . PHE A 1 143 ? 30.983 23.373  31.743  1.00 27.70  ? 122  PHE A CE1   1 
ATOM   904  C CE2   . PHE A 1 143 ? 32.730 23.720  30.173  1.00 29.30  ? 122  PHE A CE2   1 
ATOM   905  C CZ    . PHE A 1 143 ? 32.113 24.054  31.349  1.00 26.14  ? 122  PHE A CZ    1 
ATOM   906  N N     . LEU A 1 144 ? 30.694 17.903  27.759  1.00 19.81  ? 123  LEU A N     1 
ATOM   907  C CA    . LEU A 1 144 ? 30.065 16.825  27.013  1.00 20.91  ? 123  LEU A CA    1 
ATOM   908  C C     . LEU A 1 144 ? 30.244 15.513  27.757  1.00 22.71  ? 123  LEU A C     1 
ATOM   909  O O     . LEU A 1 144 ? 29.256 14.825  28.003  1.00 23.18  ? 123  LEU A O     1 
ATOM   910  C CB    . LEU A 1 144 ? 30.627 16.768  25.605  1.00 22.46  ? 123  LEU A CB    1 
ATOM   911  C CG    . LEU A 1 144 ? 30.214 15.577  24.730  1.00 23.84  ? 123  LEU A CG    1 
ATOM   912  C CD1   . LEU A 1 144 ? 28.719 15.627  24.428  1.00 25.99  ? 123  LEU A CD1   1 
ATOM   913  C CD2   . LEU A 1 144 ? 31.016 15.596  23.440  1.00 25.59  ? 123  LEU A CD2   1 
ATOM   914  N N     . ARG A 1 145 ? 31.491 15.184  28.128  1.00 22.79  ? 124  ARG A N     1 
ATOM   915  C CA    . ARG A 1 145 ? 31.760 13.988  28.907  1.00 21.17  ? 124  ARG A CA    1 
ATOM   916  C C     . ARG A 1 145 ? 30.994 14.030  30.219  1.00 21.47  ? 124  ARG A C     1 
ATOM   917  O O     . ARG A 1 145 ? 30.523 13.002  30.701  1.00 25.03  ? 124  ARG A O     1 
ATOM   918  C CB    . ARG A 1 145 ? 33.263 13.816  29.148  1.00 21.55  ? 124  ARG A CB    1 
ATOM   919  C CG    . ARG A 1 145 ? 34.106 13.511  27.916  1.00 24.57  ? 124  ARG A CG    1 
ATOM   920  C CD    . ARG A 1 145 ? 33.942 12.149  27.266  1.00 25.51  ? 124  ARG A CD    1 
ATOM   921  N NE    . ARG A 1 145 ? 32.807 12.118  26.333  1.00 26.13  ? 124  ARG A NE    1 
ATOM   922  C CZ    . ARG A 1 145 ? 32.875 12.336  25.019  1.00 24.61  ? 124  ARG A CZ    1 
ATOM   923  N NH1   . ARG A 1 145 ? 31.788 12.242  24.253  1.00 24.18  ? 124  ARG A NH1   1 
ATOM   924  N NH2   . ARG A 1 145 ? 34.022 12.669  24.456  1.00 25.39  ? 124  ARG A NH2   1 
ATOM   925  N N     . GLY A 1 146 ? 30.853 15.232  30.799  1.00 21.59  ? 125  GLY A N     1 
ATOM   926  C CA    . GLY A 1 146 ? 30.172 15.390  32.075  1.00 21.24  ? 125  GLY A CA    1 
ATOM   927  C C     . GLY A 1 146 ? 28.677 15.069  32.023  1.00 22.54  ? 125  GLY A C     1 
ATOM   928  O O     . GLY A 1 146 ? 28.063 14.892  33.073  1.00 23.68  ? 125  GLY A O     1 
ATOM   929  N N     . ALA A 1 147 ? 28.067 15.071  30.823  1.00 20.66  ? 126  ALA A N     1 
ATOM   930  C CA    . ALA A 1 147 ? 26.637 14.828  30.709  1.00 21.38  ? 126  ALA A CA    1 
ATOM   931  C C     . ALA A 1 147 ? 26.335 13.326  30.713  1.00 21.31  ? 126  ALA A C     1 
ATOM   932  O O     . ALA A 1 147 ? 25.178 12.943  30.883  1.00 21.09  ? 126  ALA A O     1 
ATOM   933  C CB    . ALA A 1 147 ? 26.118 15.488  29.448  1.00 20.95  ? 126  ALA A CB    1 
ATOM   934  N N     . GLU A 1 148 ? 27.363 12.510  30.459  1.00 18.76  ? 127  GLU A N     1 
ATOM   935  C CA    . GLU A 1 148 ? 27.216 11.099  30.100  1.00 20.84  ? 127  GLU A CA    1 
ATOM   936  C C     . GLU A 1 148 ? 27.475 10.181  31.298  1.00 23.19  ? 127  GLU A C     1 
ATOM   937  O O     . GLU A 1 148 ? 28.410 10.411  32.090  1.00 21.80  ? 127  GLU A O     1 
ATOM   938  C CB    . GLU A 1 148 ? 28.268 10.748  29.049  1.00 20.00  ? 127  GLU A CB    1 
ATOM   939  C CG    . GLU A 1 148 ? 28.111 11.492  27.727  1.00 20.56  ? 127  GLU A CG    1 
ATOM   940  C CD    . GLU A 1 148 ? 29.343 11.465  26.825  1.00 21.46  ? 127  GLU A CD    1 
ATOM   941  O OE1   . GLU A 1 148 ? 29.264 11.642  25.595  1.00 20.62  ? 127  GLU A OE1   1 
ATOM   942  O OE2   . GLU A 1 148 ? 30.407 11.189  27.371  1.00 19.75  ? 127  GLU A OE2   1 
ATOM   943  N N     . HIS A 1 149 ? 26.635 9.141   31.415  1.00 20.73  ? 128  HIS A N     1 
ATOM   944  C CA    . HIS A 1 149 ? 26.876 7.981   32.264  1.00 20.72  ? 128  HIS A CA    1 
ATOM   945  C C     . HIS A 1 149 ? 26.750 6.679   31.469  1.00 19.75  ? 128  HIS A C     1 
ATOM   946  O O     . HIS A 1 149 ? 25.656 6.116   31.353  1.00 19.52  ? 128  HIS A O     1 
ATOM   947  C CB    . HIS A 1 149 ? 25.886 8.007   33.426  1.00 22.57  ? 128  HIS A CB    1 
ATOM   948  C CG    . HIS A 1 149 ? 26.273 7.133   34.555  1.00 26.09  ? 128  HIS A CG    1 
ATOM   949  N ND1   . HIS A 1 149 ? 25.916 7.445   35.852  1.00 28.49  ? 128  HIS A ND1   1 
ATOM   950  C CD2   . HIS A 1 149 ? 27.029 5.992   34.611  1.00 26.78  ? 128  HIS A CD2   1 
ATOM   951  C CE1   . HIS A 1 149 ? 26.386 6.485   36.659  1.00 30.55  ? 128  HIS A CE1   1 
ATOM   952  N NE2   . HIS A 1 149 ? 27.048 5.614   35.916  1.00 30.58  ? 128  HIS A NE2   1 
ATOM   953  N N     . TRP A 1 150 ? 27.871 6.194   30.938  1.00 19.86  ? 129  TRP A N     1 
ATOM   954  C CA    . TRP A 1 150 ? 27.954 4.986   30.121  1.00 21.24  ? 129  TRP A CA    1 
ATOM   955  C C     . TRP A 1 150 ? 27.737 3.742   30.983  1.00 25.44  ? 129  TRP A C     1 
ATOM   956  O O     . TRP A 1 150 ? 28.222 3.684   32.123  1.00 25.45  ? 129  TRP A O     1 
ATOM   957  C CB    . TRP A 1 150 ? 29.307 4.935   29.414  1.00 24.55  ? 129  TRP A CB    1 
ATOM   958  C CG    . TRP A 1 150 ? 29.585 3.703   28.588  1.00 24.39  ? 129  TRP A CG    1 
ATOM   959  C CD1   . TRP A 1 150 ? 30.566 2.780   28.844  1.00 27.84  ? 129  TRP A CD1   1 
ATOM   960  C CD2   . TRP A 1 150 ? 28.905 3.240   27.398  1.00 24.03  ? 129  TRP A CD2   1 
ATOM   961  N NE1   . TRP A 1 150 ? 30.576 1.808   27.874  1.00 25.15  ? 129  TRP A NE1   1 
ATOM   962  C CE2   . TRP A 1 150 ? 29.559 2.059   26.984  1.00 24.52  ? 129  TRP A CE2   1 
ATOM   963  C CE3   . TRP A 1 150 ? 27.835 3.713   26.624  1.00 22.17  ? 129  TRP A CE3   1 
ATOM   964  C CZ2   . TRP A 1 150 ? 29.151 1.338   25.863  1.00 24.92  ? 129  TRP A CZ2   1 
ATOM   965  C CZ3   . TRP A 1 150 ? 27.428 2.992   25.523  1.00 21.00  ? 129  TRP A CZ3   1 
ATOM   966  C CH2   . TRP A 1 150 ? 28.096 1.835   25.131  1.00 24.35  ? 129  TRP A CH2   1 
ATOM   967  N N     . THR A 1 151 ? 26.888 2.820   30.497  1.00 23.21  ? 130  THR A N     1 
ATOM   968  C CA    . THR A 1 151 ? 26.533 1.627   31.264  1.00 25.90  ? 130  THR A CA    1 
ATOM   969  C C     . THR A 1 151 ? 27.135 0.395   30.601  1.00 28.42  ? 130  THR A C     1 
ATOM   970  O O     . THR A 1 151 ? 26.838 -0.706  31.027  1.00 27.45  ? 130  THR A O     1 
ATOM   971  C CB    . THR A 1 151 ? 25.014 1.451   31.391  1.00 24.91  ? 130  THR A CB    1 
ATOM   972  O OG1   . THR A 1 151 ? 24.461 1.305   30.087  1.00 24.00  ? 130  THR A OG1   1 
ATOM   973  C CG2   . THR A 1 151 ? 24.330 2.655   31.997  1.00 27.00  ? 130  THR A CG2   1 
ATOM   974  N N     . GLY A 1 152 ? 27.894 0.568   29.515  1.00 29.33  ? 131  GLY A N     1 
ATOM   975  C CA    . GLY A 1 152 ? 28.403 -0.567  28.762  1.00 32.28  ? 131  GLY A CA    1 
ATOM   976  C C     . GLY A 1 152 ? 29.809 -0.964  29.214  1.00 34.51  ? 131  GLY A C     1 
ATOM   977  O O     . GLY A 1 152 ? 30.215 -0.669  30.346  1.00 36.36  ? 131  GLY A O     1 
ATOM   978  N N     . GLY A 1 153 ? 30.552 -1.589  28.294  1.00 42.49  ? 132  GLY A N     1 
ATOM   979  C CA    . GLY A 1 153 ? 31.880 -2.109  28.586  1.00 45.47  ? 132  GLY A CA    1 
ATOM   980  C C     . GLY A 1 153 ? 32.956 -1.020  28.623  1.00 47.75  ? 132  GLY A C     1 
ATOM   981  O O     . GLY A 1 153 ? 32.822 0.047   28.018  1.00 35.64  ? 132  GLY A O     1 
ATOM   982  N N     . PRO A 1 154 ? 34.116 -1.293  29.270  1.00 50.35  ? 133  PRO A N     1 
ATOM   983  C CA    . PRO A 1 154 ? 35.147 -0.273  29.429  1.00 47.50  ? 133  PRO A CA    1 
ATOM   984  C C     . PRO A 1 154 ? 35.707 -0.028  28.040  1.00 41.69  ? 133  PRO A C     1 
ATOM   985  O O     . PRO A 1 154 ? 35.431 -0.781  27.109  1.00 49.75  ? 133  PRO A O     1 
ATOM   986  C CB    . PRO A 1 154 ? 36.135 -0.942  30.378  1.00 54.14  ? 133  PRO A CB    1 
ATOM   987  C CG    . PRO A 1 154 ? 36.043 -2.404  29.973  1.00 55.32  ? 133  PRO A CG    1 
ATOM   988  C CD    . PRO A 1 154 ? 34.542 -2.611  29.777  1.00 56.54  ? 133  PRO A CD    1 
ATOM   989  N N     . GLY A 1 155 ? 36.492 1.028   27.898  1.00 38.10  ? 134  GLY A N     1 
ATOM   990  C CA    . GLY A 1 155 ? 37.065 1.341   26.604  1.00 38.20  ? 134  GLY A CA    1 
ATOM   991  C C     . GLY A 1 155 ? 36.156 2.238   25.765  1.00 36.02  ? 134  GLY A C     1 
ATOM   992  O O     . GLY A 1 155 ? 36.532 2.633   24.669  1.00 34.76  ? 134  GLY A O     1 
ATOM   993  N N     . ALA A 1 156 ? 34.953 2.561   26.256  1.00 36.88  ? 135  ALA A N     1 
ATOM   994  C CA    . ALA A 1 156 ? 34.112 3.507   25.542  1.00 33.85  ? 135  ALA A CA    1 
ATOM   995  C C     . ALA A 1 156 ? 34.632 4.904   25.851  1.00 31.56  ? 135  ALA A C     1 
ATOM   996  O O     . ALA A 1 156 ? 35.190 5.135   26.921  1.00 28.20  ? 135  ALA A O     1 
ATOM   997  C CB    . ALA A 1 156 ? 32.658 3.319   25.924  1.00 29.77  ? 135  ALA A CB    1 
ATOM   998  N N     . VAL A 1 157 ? 34.432 5.839   24.927  1.00 30.24  ? 136  VAL A N     1 
ATOM   999  C CA    . VAL A 1 157 ? 34.907 7.193   25.137  1.00 34.04  ? 136  VAL A CA    1 
ATOM   1000 C C     . VAL A 1 157 ? 34.037 7.920   26.162  1.00 31.81  ? 136  VAL A C     1 
ATOM   1001 O O     . VAL A 1 157 ? 34.451 8.954   26.686  1.00 28.65  ? 136  VAL A O     1 
ATOM   1002 C CB    . VAL A 1 157 ? 34.956 7.997   23.824  1.00 43.42  ? 136  VAL A CB    1 
ATOM   1003 C CG1   . VAL A 1 157 ? 35.594 7.198   22.692  1.00 52.98  ? 136  VAL A CG1   1 
ATOM   1004 C CG2   . VAL A 1 157 ? 33.576 8.479   23.407  1.00 42.99  ? 136  VAL A CG2   1 
ATOM   1005 N N     . TYR A 1 158 ? 32.815 7.431   26.420  1.00 28.21  ? 137  TYR A N     1 
ATOM   1006 C CA    . TYR A 1 158 ? 31.819 8.240   27.120  1.00 24.79  ? 137  TYR A CA    1 
ATOM   1007 C C     . TYR A 1 158 ? 32.177 8.382   28.606  1.00 26.42  ? 137  TYR A C     1 
ATOM   1008 O O     . TYR A 1 158 ? 32.899 7.572   29.195  1.00 25.61  ? 137  TYR A O     1 
ATOM   1009 C CB    . TYR A 1 158 ? 30.396 7.707   26.861  1.00 23.16  ? 137  TYR A CB    1 
ATOM   1010 C CG    . TYR A 1 158 ? 30.233 7.392   25.381  1.00 21.90  ? 137  TYR A CG    1 
ATOM   1011 C CD1   . TYR A 1 158 ? 30.284 8.399   24.420  1.00 21.02  ? 137  TYR A CD1   1 
ATOM   1012 C CD2   . TYR A 1 158 ? 30.094 6.071   24.945  1.00 22.32  ? 137  TYR A CD2   1 
ATOM   1013 C CE1   . TYR A 1 158 ? 30.206 8.097   23.068  1.00 21.23  ? 137  TYR A CE1   1 
ATOM   1014 C CE2   . TYR A 1 158 ? 30.037 5.758   23.597  1.00 22.52  ? 137  TYR A CE2   1 
ATOM   1015 C CZ    . TYR A 1 158 ? 30.094 6.774   22.656  1.00 21.23  ? 137  TYR A CZ    1 
ATOM   1016 O OH    . TYR A 1 158 ? 30.044 6.470   21.325  1.00 22.83  ? 137  TYR A OH    1 
ATOM   1017 N N     . GLY A 1 159 ? 31.611 9.429   29.202  1.00 23.83  ? 138  GLY A N     1 
ATOM   1018 C CA    . GLY A 1 159 ? 31.709 9.700   30.623  1.00 25.92  ? 138  GLY A CA    1 
ATOM   1019 C C     . GLY A 1 159 ? 30.982 8.641   31.432  1.00 25.13  ? 138  GLY A C     1 
ATOM   1020 O O     . GLY A 1 159 ? 30.137 7.937   30.890  1.00 21.70  ? 138  GLY A O     1 
ATOM   1021 N N     . THR A 1 160 ? 31.303 8.559   32.723  1.00 23.90  ? 139  THR A N     1 
ATOM   1022 C CA    . THR A 1 160 ? 30.785 7.506   33.581  1.00 28.23  ? 139  THR A CA    1 
ATOM   1023 C C     . THR A 1 160 ? 30.096 8.099   34.806  1.00 27.88  ? 139  THR A C     1 
ATOM   1024 O O     . THR A 1 160 ? 29.895 7.370   35.774  1.00 29.53  ? 139  THR A O     1 
ATOM   1025 C CB    . THR A 1 160 ? 31.967 6.634   34.031  1.00 30.96  ? 139  THR A CB    1 
ATOM   1026 O OG1   . THR A 1 160 ? 32.833 7.552   34.696  1.00 31.85  ? 139  THR A OG1   1 
ATOM   1027 C CG2   . THR A 1 160 ? 32.788 6.112   32.881  1.00 32.20  ? 139  THR A CG2   1 
ATOM   1028 N N     . GLU A 1 161 ? 29.747 9.392   34.809  1.00 26.03  ? 140  GLU A N     1 
ATOM   1029 C CA    . GLU A 1 161 ? 29.180 9.974   36.022  1.00 31.31  ? 140  GLU A CA    1 
ATOM   1030 C C     . GLU A 1 161 ? 28.048 10.979  35.812  1.00 28.27  ? 140  GLU A C     1 
ATOM   1031 O O     . GLU A 1 161 ? 27.509 11.505  36.778  1.00 26.05  ? 140  GLU A O     1 
ATOM   1032 C CB    . GLU A 1 161 ? 30.318 10.640  36.788  1.00 37.25  ? 140  GLU A CB    1 
ATOM   1033 C CG    . GLU A 1 161 ? 31.229 9.582   37.393  1.00 48.00  ? 140  GLU A CG    1 
ATOM   1034 C CD    . GLU A 1 161 ? 32.442 10.177  38.049  1.00 58.79  ? 140  GLU A CD    1 
ATOM   1035 O OE1   . GLU A 1 161 ? 33.395 9.405   38.292  1.00 74.38  ? 140  GLU A OE1   1 
ATOM   1036 O OE2   . GLU A 1 161 ? 32.410 11.393  38.330  1.00 65.32  ? 140  GLU A OE2   1 
ATOM   1037 N N     . GLY A 1 162 ? 27.635 11.223  34.575  1.00 24.77  ? 141  GLY A N     1 
ATOM   1038 C CA    . GLY A 1 162 ? 26.714 12.318  34.316  1.00 21.74  ? 141  GLY A CA    1 
ATOM   1039 C C     . GLY A 1 162 ? 25.234 11.934  34.435  1.00 20.85  ? 141  GLY A C     1 
ATOM   1040 O O     . GLY A 1 162 ? 24.859 10.796  34.700  1.00 22.72  ? 141  GLY A O     1 
ATOM   1041 N N     . PRO A 1 163 ? 24.325 12.915  34.287  1.00 21.24  ? 142  PRO A N     1 
ATOM   1042 C CA    . PRO A 1 163 ? 22.886 12.670  34.439  1.00 21.88  ? 142  PRO A CA    1 
ATOM   1043 C C     . PRO A 1 163 ? 22.237 11.778  33.374  1.00 21.47  ? 142  PRO A C     1 
ATOM   1044 O O     . PRO A 1 163 ? 21.162 11.222  33.624  1.00 24.06  ? 142  PRO A O     1 
ATOM   1045 C CB    . PRO A 1 163 ? 22.304 14.092  34.401  1.00 20.24  ? 142  PRO A CB    1 
ATOM   1046 C CG    . PRO A 1 163 ? 23.486 14.977  34.682  1.00 22.47  ? 142  PRO A CG    1 
ATOM   1047 C CD    . PRO A 1 163 ? 24.626 14.309  33.950  1.00 20.97  ? 142  PRO A CD    1 
ATOM   1048 N N     . LEU A 1 164 ? 22.864 11.663  32.190  1.00 20.35  ? 143  LEU A N     1 
ATOM   1049 C CA    . LEU A 1 164 ? 22.258 10.923  31.073  1.00 20.03  ? 143  LEU A CA    1 
ATOM   1050 C C     . LEU A 1 164 ? 22.865 9.536   30.920  1.00 19.93  ? 143  LEU A C     1 
ATOM   1051 O O     . LEU A 1 164 ? 24.007 9.386   30.492  1.00 17.92  ? 143  LEU A O     1 
ATOM   1052 C CB    . LEU A 1 164 ? 22.391 11.696  29.764  1.00 19.62  ? 143  LEU A CB    1 
ATOM   1053 C CG    . LEU A 1 164 ? 21.693 13.058  29.710  1.00 19.28  ? 143  LEU A CG    1 
ATOM   1054 C CD1   . LEU A 1 164 ? 21.852 13.646  28.308  1.00 21.42  ? 143  LEU A CD1   1 
ATOM   1055 C CD2   . LEU A 1 164 ? 20.228 12.971  30.053  1.00 20.24  ? 143  LEU A CD2   1 
ATOM   1056 N N     . TRP A 1 165 ? 22.065 8.523   31.232  1.00 18.51  ? 144  TRP A N     1 
ATOM   1057 C CA    . TRP A 1 165 ? 22.461 7.148   31.008  1.00 20.46  ? 144  TRP A CA    1 
ATOM   1058 C C     . TRP A 1 165 ? 22.618 6.903   29.507  1.00 21.59  ? 144  TRP A C     1 
ATOM   1059 O O     . TRP A 1 165 ? 21.703 7.242   28.744  1.00 21.97  ? 144  TRP A O     1 
ATOM   1060 C CB    . TRP A 1 165 ? 21.393 6.209   31.553  1.00 21.22  ? 144  TRP A CB    1 
ATOM   1061 C CG    . TRP A 1 165 ? 21.117 6.280   33.025  1.00 26.57  ? 144  TRP A CG    1 
ATOM   1062 C CD1   . TRP A 1 165 ? 19.983 6.750   33.618  1.00 29.34  ? 144  TRP A CD1   1 
ATOM   1063 C CD2   . TRP A 1 165 ? 21.941 5.760   34.081  1.00 24.70  ? 144  TRP A CD2   1 
ATOM   1064 N NE1   . TRP A 1 165 ? 20.063 6.611   34.976  1.00 29.05  ? 144  TRP A NE1   1 
ATOM   1065 C CE2   . TRP A 1 165 ? 21.242 5.996   35.290  1.00 28.26  ? 144  TRP A CE2   1 
ATOM   1066 C CE3   . TRP A 1 165 ? 23.203 5.166   34.128  1.00 27.16  ? 144  TRP A CE3   1 
ATOM   1067 C CZ2   . TRP A 1 165 ? 21.747 5.609   36.530  1.00 27.35  ? 144  TRP A CZ2   1 
ATOM   1068 C CZ3   . TRP A 1 165 ? 23.704 4.788   35.358  1.00 27.46  ? 144  TRP A CZ3   1 
ATOM   1069 C CH2   . TRP A 1 165 ? 22.985 5.012   36.534  1.00 25.70  ? 144  TRP A CH2   1 
ATOM   1070 N N     . ILE A 1 166 ? 23.778 6.359   29.109  1.00 20.65  ? 145  ILE A N     1 
ATOM   1071 C CA    . ILE A 1 166 ? 24.100 6.020   27.728  1.00 19.38  ? 145  ILE A CA    1 
ATOM   1072 C C     . ILE A 1 166 ? 24.363 4.515   27.737  1.00 21.01  ? 145  ILE A C     1 
ATOM   1073 O O     . ILE A 1 166 ? 25.147 4.061   28.581  1.00 23.23  ? 145  ILE A O     1 
ATOM   1074 C CB    . ILE A 1 166 ? 25.333 6.772   27.197  1.00 21.18  ? 145  ILE A CB    1 
ATOM   1075 C CG1   . ILE A 1 166 ? 25.354 8.294   27.479  1.00 24.71  ? 145  ILE A CG1   1 
ATOM   1076 C CG2   . ILE A 1 166 ? 25.522 6.491   25.713  1.00 19.95  ? 145  ILE A CG2   1 
ATOM   1077 C CD1   . ILE A 1 166 ? 24.148 9.023   26.961  1.00 24.91  ? 145  ILE A CD1   1 
ATOM   1078 N N     . SER A 1 167 ? 23.646 3.744   26.908  1.00 19.90  ? 146  SER A N     1 
ATOM   1079 C CA    . SER A 1 167 ? 23.689 2.292   26.988  1.00 21.35  ? 146  SER A CA    1 
ATOM   1080 C C     . SER A 1 167 ? 23.902 1.667   25.615  1.00 20.61  ? 146  SER A C     1 
ATOM   1081 O O     . SER A 1 167 ? 23.459 2.193   24.588  1.00 21.17  ? 146  SER A O     1 
ATOM   1082 C CB    . SER A 1 167 ? 22.451 1.699   27.671  1.00 22.20  ? 146  SER A CB    1 
ATOM   1083 O OG    . SER A 1 167 ? 22.226 2.282   28.944  1.00 25.43  ? 146  SER A OG    1 
ATOM   1084 N N     . PRO A 1 168 ? 24.568 0.493   25.561  1.00 21.01  ? 147  PRO A N     1 
ATOM   1085 C CA    . PRO A 1 168 ? 24.557 -0.344  24.366  1.00 20.71  ? 147  PRO A CA    1 
ATOM   1086 C C     . PRO A 1 168 ? 23.140 -0.894  24.226  1.00 19.72  ? 147  PRO A C     1 
ATOM   1087 O O     . PRO A 1 168 ? 22.396 -0.976  25.200  1.00 19.49  ? 147  PRO A O     1 
ATOM   1088 C CB    . PRO A 1 168 ? 25.563 -1.454  24.650  1.00 22.83  ? 147  PRO A CB    1 
ATOM   1089 C CG    . PRO A 1 168 ? 25.527 -1.562  26.153  1.00 25.92  ? 147  PRO A CG    1 
ATOM   1090 C CD    . PRO A 1 168 ? 25.227 -0.167  26.696  1.00 23.16  ? 147  PRO A CD    1 
ATOM   1091 N N     . PRO A 1 169 ? 22.747 -1.344  23.022  1.00 18.83  ? 148  PRO A N     1 
ATOM   1092 C CA    . PRO A 1 169 ? 21.430 -1.932  22.825  1.00 20.48  ? 148  PRO A CA    1 
ATOM   1093 C C     . PRO A 1 169 ? 21.301 -3.207  23.631  1.00 22.96  ? 148  PRO A C     1 
ATOM   1094 O O     . PRO A 1 169 ? 22.241 -3.982  23.687  1.00 20.20  ? 148  PRO A O     1 
ATOM   1095 C CB    . PRO A 1 169 ? 21.368 -2.215  21.350  1.00 18.26  ? 148  PRO A CB    1 
ATOM   1096 C CG    . PRO A 1 169 ? 22.802 -2.324  20.925  1.00 19.19  ? 148  PRO A CG    1 
ATOM   1097 C CD    . PRO A 1 169 ? 23.551 -1.330  21.790  1.00 18.97  ? 148  PRO A CD    1 
ATOM   1098 N N     . ARG A 1 170 ? 20.115 -3.423  24.200  1.00 22.93  ? 149  ARG A N     1 
ATOM   1099 C CA    . ARG A 1 170 ? 19.833 -4.648  24.925  1.00 23.17  ? 149  ARG A CA    1 
ATOM   1100 C C     . ARG A 1 170 ? 19.549 -5.790  23.973  1.00 22.91  ? 149  ARG A C     1 
ATOM   1101 O O     . ARG A 1 170 ? 19.911 -6.920  24.248  1.00 24.11  ? 149  ARG A O     1 
ATOM   1102 C CB    . ARG A 1 170 ? 18.658 -4.438  25.874  1.00 24.00  ? 149  ARG A CB    1 
ATOM   1103 C CG    . ARG A 1 170 ? 19.097 -3.544  27.018  1.00 27.00  ? 149  ARG A CG    1 
ATOM   1104 C CD    . ARG A 1 170 ? 17.913 -2.938  27.731  1.00 29.19  ? 149  ARG A CD    1 
ATOM   1105 N NE    . ARG A 1 170 ? 17.277 -3.951  28.565  1.00 30.90  ? 149  ARG A NE    1 
ATOM   1106 C CZ    . ARG A 1 170 ? 17.657 -4.285  29.782  1.00 34.76  ? 149  ARG A CZ    1 
ATOM   1107 N NH1   . ARG A 1 170 ? 18.697 -3.700  30.352  1.00 36.30  ? 149  ARG A NH1   1 
ATOM   1108 N NH2   . ARG A 1 170 ? 16.992 -5.232  30.418  1.00 34.89  ? 149  ARG A NH2   1 
ATOM   1109 N N     . SER A 1 171 ? 18.861 -5.520  22.873  1.00 21.28  ? 150  SER A N     1 
ATOM   1110 C CA    . SER A 1 171 ? 18.383 -6.618  22.050  1.00 22.75  ? 150  SER A CA    1 
ATOM   1111 C C     . SER A 1 171 ? 18.557 -6.242  20.594  1.00 20.84  ? 150  SER A C     1 
ATOM   1112 O O     . SER A 1 171 ? 17.561 -6.077  19.907  1.00 20.96  ? 150  SER A O     1 
ATOM   1113 C CB    . SER A 1 171 ? 16.931 -6.955  22.346  1.00 23.66  ? 150  SER A CB    1 
ATOM   1114 O OG    . SER A 1 171 ? 16.757 -7.282  23.716  1.00 24.41  ? 150  SER A OG    1 
ATOM   1115 N N     . PRO A 1 172 ? 19.791 -6.070  20.079  1.00 22.39  ? 151  PRO A N     1 
ATOM   1116 C CA    . PRO A 1 172 ? 19.960 -5.673  18.683  1.00 22.38  ? 151  PRO A CA    1 
ATOM   1117 C C     . PRO A 1 172 ? 19.420 -6.730  17.706  1.00 21.83  ? 151  PRO A C     1 
ATOM   1118 O O     . PRO A 1 172 ? 19.436 -7.927  17.978  1.00 21.92  ? 151  PRO A O     1 
ATOM   1119 C CB    . PRO A 1 172 ? 21.492 -5.503  18.529  1.00 21.80  ? 151  PRO A CB    1 
ATOM   1120 C CG    . PRO A 1 172 ? 22.096 -6.362  19.628  1.00 22.94  ? 151  PRO A CG    1 
ATOM   1121 C CD    . PRO A 1 172 ? 21.075 -6.320  20.771  1.00 23.63  ? 151  PRO A CD    1 
ATOM   1122 N N     . ASP A 1 173 ? 18.963 -6.280  16.545  1.00 20.26  ? 152  ASP A N     1 
ATOM   1123 C CA    . ASP A 1 173 ? 18.488 -7.196  15.524  1.00 21.00  ? 152  ASP A CA    1 
ATOM   1124 C C     . ASP A 1 173 ? 19.651 -8.057  15.051  1.00 22.13  ? 152  ASP A C     1 
ATOM   1125 O O     . ASP A 1 173 ? 20.785 -7.588  14.923  1.00 21.29  ? 152  ASP A O     1 
ATOM   1126 C CB    . ASP A 1 173 ? 17.861 -6.458  14.358  1.00 21.47  ? 152  ASP A CB    1 
ATOM   1127 C CG    . ASP A 1 173 ? 17.022 -7.324  13.432  1.00 24.69  ? 152  ASP A CG    1 
ATOM   1128 O OD1   . ASP A 1 173 ? 17.600 -7.904  12.462  1.00 27.35  ? 152  ASP A OD1   1 
ATOM   1129 O OD2   . ASP A 1 173 ? 15.817 -7.450  13.725  1.00 27.83  ? 152  ASP A OD2   1 
ATOM   1130 N N     . PRO A 1 174 ? 19.421 -9.354  14.773  1.00 24.89  ? 153  PRO A N     1 
ATOM   1131 C CA    . PRO A 1 174 ? 20.501 -10.187 14.236  1.00 25.66  ? 153  PRO A CA    1 
ATOM   1132 C C     . PRO A 1 174 ? 21.150 -9.630  12.969  1.00 24.17  ? 153  PRO A C     1 
ATOM   1133 O O     . PRO A 1 174 ? 22.339 -9.834  12.735  1.00 24.22  ? 153  PRO A O     1 
ATOM   1134 C CB    . PRO A 1 174 ? 19.818 -11.540 13.961  1.00 28.21  ? 153  PRO A CB    1 
ATOM   1135 C CG    . PRO A 1 174 ? 18.565 -11.525 14.834  1.00 30.09  ? 153  PRO A CG    1 
ATOM   1136 C CD    . PRO A 1 174 ? 18.146 -10.061 14.969  1.00 25.73  ? 153  PRO A CD    1 
ATOM   1137 N N     . THR A 1 175 ? 20.404 -8.885  12.144  1.00 22.12  ? 154  THR A N     1 
ATOM   1138 C CA    . THR A 1 175 ? 20.984 -8.360  10.908  1.00 22.07  ? 154  THR A CA    1 
ATOM   1139 C C     . THR A 1 175 ? 21.991 -7.253  11.209  1.00 22.89  ? 154  THR A C     1 
ATOM   1140 O O     . THR A 1 175 ? 22.810 -6.915  10.351  1.00 22.44  ? 154  THR A O     1 
ATOM   1141 C CB    . THR A 1 175 ? 19.912 -7.869  9.929   1.00 25.36  ? 154  THR A CB    1 
ATOM   1142 O OG1   . THR A 1 175 ? 19.323 -6.714  10.527  1.00 23.69  ? 154  THR A OG1   1 
ATOM   1143 C CG2   . THR A 1 175 ? 18.887 -8.945  9.607   1.00 28.57  ? 154  THR A CG2   1 
ATOM   1144 N N     . THR A 1 176 ? 21.898 -6.637  12.395  1.00 22.18  ? 155  THR A N     1 
ATOM   1145 C CA    . THR A 1 176 ? 22.764 -5.507  12.697  1.00 21.02  ? 155  THR A CA    1 
ATOM   1146 C C     . THR A 1 176 ? 24.231 -5.964  12.760  1.00 20.86  ? 155  THR A C     1 
ATOM   1147 O O     . THR A 1 176 ? 25.104 -5.268  12.268  1.00 19.20  ? 155  THR A O     1 
ATOM   1148 C CB    . THR A 1 176 ? 22.281 -4.827  13.979  1.00 19.72  ? 155  THR A CB    1 
ATOM   1149 O OG1   . THR A 1 176 ? 20.966 -4.328  13.695  1.00 20.25  ? 155  THR A OG1   1 
ATOM   1150 C CG2   . THR A 1 176 ? 23.150 -3.652  14.384  1.00 19.42  ? 155  THR A CG2   1 
ATOM   1151 N N     . ALA A 1 177 ? 24.514 -7.156  13.314  1.00 21.48  ? 156  ALA A N     1 
ATOM   1152 C CA    . ALA A 1 177 ? 25.878 -7.689  13.312  1.00 23.65  ? 156  ALA A CA    1 
ATOM   1153 C C     . ALA A 1 177 ? 26.366 -7.849  11.873  1.00 22.91  ? 156  ALA A C     1 
ATOM   1154 O O     . ALA A 1 177 ? 27.534 -7.633  11.590  1.00 23.85  ? 156  ALA A O     1 
ATOM   1155 C CB    . ALA A 1 177 ? 25.964 -9.029  14.024  1.00 25.81  ? 156  ALA A CB    1 
ATOM   1156 N N     . ARG A 1 178 ? 25.442 -8.211  10.972  1.00 21.63  ? 157  ARG A N     1 
ATOM   1157 C CA    . ARG A 1 178 ? 25.773 -8.427  9.575   1.00 24.45  ? 157  ARG A CA    1 
ATOM   1158 C C     . ARG A 1 178 ? 26.127 -7.113  8.881   1.00 24.16  ? 157  ARG A C     1 
ATOM   1159 O O     . ARG A 1 178 ? 26.994 -7.072  8.001   1.00 22.34  ? 157  ARG A O     1 
ATOM   1160 C CB    . ARG A 1 178 ? 24.615 -9.170  8.906   1.00 25.43  ? 157  ARG A CB    1 
ATOM   1161 C CG    . ARG A 1 178 ? 24.363 -10.543 9.521   1.00 27.77  ? 157  ARG A CG    1 
ATOM   1162 C CD    . ARG A 1 178 ? 25.415 -11.586 9.261   1.00 31.69  ? 157  ARG A CD    1 
ATOM   1163 N NE    . ARG A 1 178 ? 25.341 -12.027 7.863   1.00 37.35  ? 157  ARG A NE    1 
ATOM   1164 C CZ    . ARG A 1 178 ? 24.545 -12.970 7.357   1.00 43.80  ? 157  ARG A CZ    1 
ATOM   1165 N NH1   . ARG A 1 178 ? 23.858 -13.783 8.137   1.00 48.33  ? 157  ARG A NH1   1 
ATOM   1166 N NH2   . ARG A 1 178 ? 24.450 -13.140 6.054   1.00 41.87  ? 157  ARG A NH2   1 
ATOM   1167 N N     . PHE A 1 179 ? 25.441 -6.035  9.274   1.00 22.23  ? 158  PHE A N     1 
ATOM   1168 C CA    . PHE A 1 179 ? 25.756 -4.726  8.730   1.00 20.32  ? 158  PHE A CA    1 
ATOM   1169 C C     . PHE A 1 179 ? 27.178 -4.340  9.134   1.00 19.28  ? 158  PHE A C     1 
ATOM   1170 O O     . PHE A 1 179 ? 27.931 -3.824  8.314   1.00 22.07  ? 158  PHE A O     1 
ATOM   1171 C CB    . PHE A 1 179 ? 24.732 -3.682  9.206   1.00 22.00  ? 158  PHE A CB    1 
ATOM   1172 C CG    . PHE A 1 179 ? 25.198 -2.237  9.034   1.00 19.08  ? 158  PHE A CG    1 
ATOM   1173 C CD1   . PHE A 1 179 ? 25.089 -1.604  7.802   1.00 18.35  ? 158  PHE A CD1   1 
ATOM   1174 C CD2   . PHE A 1 179 ? 25.728 -1.524  10.102  1.00 19.12  ? 158  PHE A CD2   1 
ATOM   1175 C CE1   . PHE A 1 179 ? 25.538 -0.306  7.630   1.00 18.46  ? 158  PHE A CE1   1 
ATOM   1176 C CE2   . PHE A 1 179 ? 26.163 -0.209  9.939   1.00 19.43  ? 158  PHE A CE2   1 
ATOM   1177 C CZ    . PHE A 1 179 ? 26.064 0.393   8.695   1.00 19.47  ? 158  PHE A CZ    1 
ATOM   1178 N N     . LEU A 1 180 ? 27.512 -4.525  10.408  1.00 19.49  ? 159  LEU A N     1 
ATOM   1179 C CA    . LEU A 1 180 ? 28.841 -4.215  10.911  1.00 23.09  ? 159  LEU A CA    1 
ATOM   1180 C C     . LEU A 1 180 ? 29.900 -5.069  10.193  1.00 22.82  ? 159  LEU A C     1 
ATOM   1181 O O     . LEU A 1 180 ? 30.963 -4.569  9.860   1.00 22.83  ? 159  LEU A O     1 
ATOM   1182 C CB    . LEU A 1 180 ? 28.884 -4.406  12.429  1.00 23.12  ? 159  LEU A CB    1 
ATOM   1183 C CG    . LEU A 1 180 ? 28.000 -3.447  13.249  1.00 24.48  ? 159  LEU A CG    1 
ATOM   1184 C CD1   . LEU A 1 180 ? 28.014 -3.890  14.682  1.00 27.83  ? 159  LEU A CD1   1 
ATOM   1185 C CD2   . LEU A 1 180 ? 28.442 -1.983  13.131  1.00 26.27  ? 159  LEU A CD2   1 
ATOM   1186 N N     . GLN A 1 181 ? 29.600 -6.345  9.926   1.00 25.27  ? 160  GLN A N     1 
ATOM   1187 C CA    . GLN A 1 181 ? 30.535 -7.217  9.231   1.00 26.56  ? 160  GLN A CA    1 
ATOM   1188 C C     . GLN A 1 181 ? 30.762 -6.694  7.816   1.00 27.07  ? 160  GLN A C     1 
ATOM   1189 O O     . GLN A 1 181 ? 31.917 -6.572  7.392   1.00 27.23  ? 160  GLN A O     1 
ATOM   1190 C CB    . GLN A 1 181 ? 30.036 -8.662  9.181   1.00 31.11  ? 160  GLN A CB    1 
ATOM   1191 C CG    . GLN A 1 181 ? 30.035 -9.368  10.533  1.00 37.62  ? 160  GLN A CG    1 
ATOM   1192 C CD    . GLN A 1 181 ? 29.124 -10.583 10.559  1.00 42.79  ? 160  GLN A CD    1 
ATOM   1193 O OE1   . GLN A 1 181 ? 28.402 -10.843 11.533  1.00 48.29  ? 160  GLN A OE1   1 
ATOM   1194 N NE2   . GLN A 1 181 ? 29.143 -11.323 9.463   1.00 39.53  ? 160  GLN A NE2   1 
ATOM   1195 N N     . ALA A 1 182 ? 29.668 -6.300  7.136   1.00 25.34  ? 161  ALA A N     1 
ATOM   1196 C CA    . ALA A 1 182 ? 29.739 -5.736  5.789   1.00 24.20  ? 161  ALA A CA    1 
ATOM   1197 C C     . ALA A 1 182 ? 30.625 -4.492  5.759   1.00 26.63  ? 161  ALA A C     1 
ATOM   1198 O O     . ALA A 1 182 ? 31.471 -4.363  4.889   1.00 25.86  ? 161  ALA A O     1 
ATOM   1199 C CB    . ALA A 1 182 ? 28.349 -5.401  5.276   1.00 23.60  ? 161  ALA A CB    1 
ATOM   1200 N N     . CYS A 1 183 ? 30.410 -3.571  6.709   1.00 26.08  ? 162  CYS A N     1 
ATOM   1201 C CA    . CYS A 1 183 ? 31.248 -2.400  6.883   1.00 24.96  ? 162  CYS A CA    1 
ATOM   1202 C C     . CYS A 1 183 ? 32.727 -2.814  6.922   1.00 24.47  ? 162  CYS A C     1 
ATOM   1203 O O     . CYS A 1 183 ? 33.554 -2.213  6.227   1.00 26.30  ? 162  CYS A O     1 
ATOM   1204 C CB    . CYS A 1 183 ? 30.867 -1.646  8.151   1.00 24.49  ? 162  CYS A CB    1 
ATOM   1205 S SG    . CYS A 1 183 ? 29.308 -0.716  8.005   1.00 24.21  ? 162  CYS A SG    1 
ATOM   1206 N N     . GLY A 1 184 ? 33.022 -3.799  7.776   1.00 27.88  ? 163  GLY A N     1 
ATOM   1207 C CA    . GLY A 1 184 ? 34.335 -4.411  7.902   1.00 29.33  ? 163  GLY A CA    1 
ATOM   1208 C C     . GLY A 1 184 ? 34.874 -4.857  6.545   1.00 28.82  ? 163  GLY A C     1 
ATOM   1209 O O     . GLY A 1 184 ? 35.992 -4.520  6.164   1.00 32.96  ? 163  GLY A O     1 
ATOM   1210 N N     . GLU A 1 185 ? 34.049 -5.566  5.788   1.00 28.82  ? 164  GLU A N     1 
ATOM   1211 C CA    . GLU A 1 185 ? 34.454 -6.034  4.485   1.00 32.12  ? 164  GLU A CA    1 
ATOM   1212 C C     . GLU A 1 185 ? 34.782 -4.862  3.563   1.00 34.91  ? 164  GLU A C     1 
ATOM   1213 O O     . GLU A 1 185 ? 35.633 -5.023  2.686   1.00 30.95  ? 164  GLU A O     1 
ATOM   1214 C CB    . GLU A 1 185 ? 33.407 -6.973  3.883   1.00 35.36  ? 164  GLU A CB    1 
ATOM   1215 C CG    . GLU A 1 185 ? 33.363 -8.318  4.594   1.00 38.11  ? 164  GLU A CG    1 
ATOM   1216 C CD    . GLU A 1 185 ? 32.066 -9.128  4.572   1.00 49.58  ? 164  GLU A CD    1 
ATOM   1217 O OE1   . GLU A 1 185 ? 32.016 -10.091 5.401   1.00 52.59  ? 164  GLU A OE1   1 
ATOM   1218 O OE2   . GLU A 1 185 ? 31.136 -8.847  3.757   1.00 38.04  ? 164  GLU A OE2   1 
ATOM   1219 N N     . ALA A 1 186 ? 34.135 -3.696  3.749   1.00 29.63  ? 165  ALA A N     1 
ATOM   1220 C CA    . ALA A 1 186 ? 34.363 -2.545  2.876   1.00 31.35  ? 165  ALA A CA    1 
ATOM   1221 C C     . ALA A 1 186 ? 35.375 -1.551  3.454   1.00 31.24  ? 165  ALA A C     1 
ATOM   1222 O O     . ALA A 1 186 ? 35.475 -0.418  2.967   1.00 33.30  ? 165  ALA A O     1 
ATOM   1223 C CB    . ALA A 1 186 ? 33.053 -1.849  2.554   1.00 31.39  ? 165  ALA A CB    1 
ATOM   1224 N N     . GLY A 1 187 ? 36.129 -1.975  4.463   1.00 27.65  ? 166  GLY A N     1 
ATOM   1225 C CA    . GLY A 1 187 ? 37.247 -1.207  4.983   1.00 28.97  ? 166  GLY A CA    1 
ATOM   1226 C C     . GLY A 1 187 ? 36.863 -0.260  6.120   1.00 35.10  ? 166  GLY A C     1 
ATOM   1227 O O     . GLY A 1 187 ? 37.680 0.573   6.518   1.00 33.94  ? 166  GLY A O     1 
ATOM   1228 N N     . LEU A 1 188 ? 35.639 -0.384  6.659   1.00 28.49  ? 167  LEU A N     1 
ATOM   1229 C CA    . LEU A 1 188 ? 35.227 0.414   7.805   1.00 30.83  ? 167  LEU A CA    1 
ATOM   1230 C C     . LEU A 1 188 ? 35.229 -0.477  9.035   1.00 32.90  ? 167  LEU A C     1 
ATOM   1231 O O     . LEU A 1 188 ? 34.287 -1.246  9.243   1.00 34.77  ? 167  LEU A O     1 
ATOM   1232 C CB    . LEU A 1 188 ? 33.835 1.014   7.611   1.00 28.50  ? 167  LEU A CB    1 
ATOM   1233 C CG    . LEU A 1 188 ? 33.631 1.823   6.329   1.00 30.48  ? 167  LEU A CG    1 
ATOM   1234 C CD1   . LEU A 1 188 ? 32.173 2.264   6.189   1.00 33.25  ? 167  LEU A CD1   1 
ATOM   1235 C CD2   . LEU A 1 188 ? 34.543 3.015   6.253   1.00 30.69  ? 167  LEU A CD2   1 
ATOM   1236 N N     . LYS A 1 189 ? 36.257 -0.339  9.870   1.00 31.18  ? 168  LYS A N     1 
ATOM   1237 C CA    . LYS A 1 189 ? 36.418 -1.214  11.018  1.00 32.76  ? 168  LYS A CA    1 
ATOM   1238 C C     . LYS A 1 189 ? 35.615 -0.705  12.208  1.00 29.22  ? 168  LYS A C     1 
ATOM   1239 O O     . LYS A 1 189 ? 35.272 0.479   12.291  1.00 25.88  ? 168  LYS A O     1 
ATOM   1240 C CB    . LYS A 1 189 ? 37.896 -1.311  11.423  1.00 39.42  ? 168  LYS A CB    1 
ATOM   1241 C CG    . LYS A 1 189 ? 38.790 -1.862  10.292  1.00 46.26  ? 168  LYS A CG    1 
ATOM   1242 C CD    . LYS A 1 189 ? 38.165 -2.969  9.446   1.00 47.75  ? 168  LYS A CD    1 
ATOM   1243 C CE    . LYS A 1 189 ? 39.140 -3.637  8.551   1.00 51.62  ? 168  LYS A CE    1 
ATOM   1244 N NZ    . LYS A 1 189 ? 38.461 -4.663  7.756   1.00 52.91  ? 168  LYS A NZ    1 
ATOM   1245 N N     . GLU A 1 190 ? 35.308 -1.630  13.128  1.00 28.47  ? 169  GLU A N     1 
ATOM   1246 C CA    . GLU A 1 190 ? 34.461 -1.327  14.268  1.00 32.69  ? 169  GLU A CA    1 
ATOM   1247 C C     . GLU A 1 190 ? 35.247 -0.431  15.227  1.00 35.33  ? 169  GLU A C     1 
ATOM   1248 O O     . GLU A 1 190 ? 36.413 -0.692  15.497  1.00 35.14  ? 169  GLU A O     1 
ATOM   1249 C CB    . GLU A 1 190 ? 33.955 -2.622  14.910  1.00 37.31  ? 169  GLU A CB    1 
ATOM   1250 C CG    . GLU A 1 190 ? 32.643 -2.433  15.679  1.00 46.51  ? 169  GLU A CG    1 
ATOM   1251 C CD    . GLU A 1 190 ? 32.123 -3.613  16.496  1.00 48.29  ? 169  GLU A CD    1 
ATOM   1252 O OE1   . GLU A 1 190 ? 31.186 -3.431  17.307  1.00 44.43  ? 169  GLU A OE1   1 
ATOM   1253 O OE2   . GLU A 1 190 ? 32.646 -4.724  16.304  1.00 47.57  ? 169  GLU A OE2   1 
ATOM   1254 N N     . MET A 1 191 ? 34.620 0.659   15.677  1.00 30.13  ? 170  MET A N     1 
ATOM   1255 C CA    . MET A 1 191 ? 35.242 1.612   16.574  1.00 36.94  ? 170  MET A CA    1 
ATOM   1256 C C     . MET A 1 191 ? 35.253 1.018   17.982  1.00 41.26  ? 170  MET A C     1 
ATOM   1257 O O     . MET A 1 191 ? 34.249 0.543   18.486  1.00 44.33  ? 170  MET A O     1 
ATOM   1258 C CB    . MET A 1 191 ? 34.505 2.952   16.490  1.00 37.32  ? 170  MET A CB    1 
ATOM   1259 C CG    . MET A 1 191 ? 34.610 3.594   15.109  1.00 36.37  ? 170  MET A CG    1 
ATOM   1260 S SD    . MET A 1 191 ? 33.733 5.159   14.866  1.00 44.58  ? 170  MET A SD    1 
ATOM   1261 C CE    . MET A 1 191 ? 32.047 4.596   15.083  1.00 42.66  ? 170  MET A CE    1 
ATOM   1262 N N     . THR A 1 192 ? 36.407 1.026   18.634  1.00 44.23  ? 171  THR A N     1 
ATOM   1263 C CA    . THR A 1 192 ? 36.486 0.375   19.931  1.00 50.14  ? 171  THR A CA    1 
ATOM   1264 C C     . THR A 1 192 ? 35.839 1.258   21.000  1.00 45.28  ? 171  THR A C     1 
ATOM   1265 O O     . THR A 1 192 ? 35.242 0.735   21.925  1.00 47.68  ? 171  THR A O     1 
ATOM   1266 C CB    . THR A 1 192 ? 37.939 -0.019  20.205  1.00 53.93  ? 171  THR A CB    1 
ATOM   1267 O OG1   . THR A 1 192 ? 38.732 1.124   19.914  1.00 59.87  ? 171  THR A OG1   1 
ATOM   1268 C CG2   . THR A 1 192 ? 38.418 -1.106  19.257  1.00 57.16  ? 171  THR A CG2   1 
ATOM   1269 N N     . GLY A 1 193 ? 35.860 2.586   20.835  1.00 44.04  ? 172  GLY A N     1 
ATOM   1270 C CA    . GLY A 1 193 ? 35.288 3.489   21.827  1.00 45.20  ? 172  GLY A CA    1 
ATOM   1271 C C     . GLY A 1 193 ? 33.845 3.926   21.529  1.00 40.81  ? 172  GLY A C     1 
ATOM   1272 O O     . GLY A 1 193 ? 33.209 4.615   22.334  1.00 34.82  ? 172  GLY A O     1 
ATOM   1273 N N     . GLY A 1 194 ? 33.318 3.500   20.382  1.00 32.52  ? 173  GLY A N     1 
ATOM   1274 C CA    . GLY A 1 194 ? 32.073 4.037   19.875  1.00 29.60  ? 173  GLY A CA    1 
ATOM   1275 C C     . GLY A 1 194 ? 32.282 5.345   19.112  1.00 28.84  ? 173  GLY A C     1 
ATOM   1276 O O     . GLY A 1 194 ? 33.393 5.892   18.988  1.00 28.65  ? 173  GLY A O     1 
ATOM   1277 N N     . PRO A 1 195 ? 31.191 5.882   18.539  1.00 25.74  ? 174  PRO A N     1 
ATOM   1278 C CA    . PRO A 1 195 ? 31.271 7.159   17.830  1.00 26.30  ? 174  PRO A CA    1 
ATOM   1279 C C     . PRO A 1 195 ? 31.640 8.290   18.786  1.00 27.39  ? 174  PRO A C     1 
ATOM   1280 O O     . PRO A 1 195 ? 31.262 8.271   19.956  1.00 28.23  ? 174  PRO A O     1 
ATOM   1281 C CB    . PRO A 1 195 ? 29.860 7.358   17.260  1.00 25.47  ? 174  PRO A CB    1 
ATOM   1282 C CG    . PRO A 1 195 ? 28.978 6.465   18.099  1.00 24.86  ? 174  PRO A CG    1 
ATOM   1283 C CD    . PRO A 1 195 ? 29.826 5.303   18.576  1.00 23.62  ? 174  PRO A CD    1 
ATOM   1284 N N     . GLY A 1 196 ? 32.359 9.288   18.270  1.00 31.83  ? 175  GLY A N     1 
ATOM   1285 C CA    . GLY A 1 196 ? 32.833 10.396  19.088  1.00 31.09  ? 175  GLY A CA    1 
ATOM   1286 C C     . GLY A 1 196 ? 34.196 10.088  19.681  1.00 34.48  ? 175  GLY A C     1 
ATOM   1287 O O     . GLY A 1 196 ? 34.671 10.820  20.532  1.00 37.01  ? 175  GLY A O     1 
ATOM   1288 N N     . GLY A 1 197 ? 34.808 8.992   19.217  1.00 34.91  ? 176  GLY A N     1 
ATOM   1289 C CA    . GLY A 1 197 ? 36.154 8.606   19.597  1.00 37.73  ? 176  GLY A CA    1 
ATOM   1290 C C     . GLY A 1 197 ? 37.161 9.225   18.636  1.00 35.82  ? 176  GLY A C     1 
ATOM   1291 O O     . GLY A 1 197 ? 36.821 10.133  17.891  1.00 35.42  ? 176  GLY A O     1 
ATOM   1292 N N     . PRO A 1 198 ? 38.428 8.777   18.660  1.00 39.56  ? 177  PRO A N     1 
ATOM   1293 C CA    . PRO A 1 198 ? 39.457 9.346   17.786  1.00 44.57  ? 177  PRO A CA    1 
ATOM   1294 C C     . PRO A 1 198 ? 39.339 8.958   16.313  1.00 45.48  ? 177  PRO A C     1 
ATOM   1295 O O     . PRO A 1 198 ? 39.733 9.714   15.429  1.00 40.43  ? 177  PRO A O     1 
ATOM   1296 C CB    . PRO A 1 198 ? 40.758 8.787   18.399  1.00 48.65  ? 177  PRO A CB    1 
ATOM   1297 C CG    . PRO A 1 198 ? 40.350 8.114   19.703  1.00 47.72  ? 177  PRO A CG    1 
ATOM   1298 C CD    . PRO A 1 198 ? 38.917 7.700   19.534  1.00 41.92  ? 177  PRO A CD    1 
ATOM   1299 N N     . GLU A 1 199 ? 38.834 7.738   16.080  1.00 45.81  ? 178  GLU A N     1 
ATOM   1300 C CA    . GLU A 1 199 ? 38.654 7.166   14.751  1.00 42.17  ? 178  GLU A CA    1 
ATOM   1301 C C     . GLU A 1 199 ? 37.791 8.101   13.897  1.00 40.82  ? 178  GLU A C     1 
ATOM   1302 O O     . GLU A 1 199 ? 36.699 8.477   14.298  1.00 41.40  ? 178  GLU A O     1 
ATOM   1303 C CB    . GLU A 1 199 ? 38.162 5.749   15.066  1.00 48.89  ? 178  GLU A CB    1 
ATOM   1304 C CG    . GLU A 1 199 ? 37.206 5.723   16.268  1.00 61.73  ? 178  GLU A CG    1 
ATOM   1305 C CD    . GLU A 1 199 ? 37.438 4.743   17.417  1.00 62.13  ? 178  GLU A CD    1 
ATOM   1306 O OE1   . GLU A 1 199 ? 38.187 3.758   17.209  1.00 56.10  ? 178  GLU A OE1   1 
ATOM   1307 O OE2   . GLU A 1 199 ? 36.837 4.960   18.516  1.00 68.32  ? 178  GLU A OE2   1 
ATOM   1308 N N     . HIS A 1 200 ? 38.315 8.491   12.726  1.00 33.83  ? 179  HIS A N     1 
ATOM   1309 C CA    . HIS A 1 200 ? 37.631 9.311   11.747  1.00 38.44  ? 179  HIS A CA    1 
ATOM   1310 C C     . HIS A 1 200 ? 36.594 8.500   10.970  1.00 38.65  ? 179  HIS A C     1 
ATOM   1311 O O     . HIS A 1 200 ? 35.579 9.027   10.524  1.00 38.19  ? 179  HIS A O     1 
ATOM   1312 C CB    . HIS A 1 200 ? 38.650 9.834   10.731  1.00 39.94  ? 179  HIS A CB    1 
ATOM   1313 C CG    . HIS A 1 200 ? 39.476 10.950  11.269  1.00 51.74  ? 179  HIS A CG    1 
ATOM   1314 N ND1   . HIS A 1 200 ? 40.362 11.679  10.505  1.00 61.99  ? 179  HIS A ND1   1 
ATOM   1315 C CD2   . HIS A 1 200 ? 39.564 11.452  12.510  1.00 55.26  ? 179  HIS A CD2   1 
ATOM   1316 C CE1   . HIS A 1 200 ? 40.943 12.600  11.268  1.00 60.51  ? 179  HIS A CE1   1 
ATOM   1317 N NE2   . HIS A 1 200 ? 40.475 12.477  12.490  1.00 54.49  ? 179  HIS A NE2   1 
ATOM   1318 N N     . SER A 1 201 ? 36.907 7.225   10.759  1.00 35.01  ? 180  SER A N     1 
ATOM   1319 C CA    . SER A 1 201 ? 36.137 6.336   9.908   1.00 33.57  ? 180  SER A CA    1 
ATOM   1320 C C     . SER A 1 201 ? 35.824 5.102   10.735  1.00 28.30  ? 180  SER A C     1 
ATOM   1321 O O     . SER A 1 201 ? 36.574 4.809   11.655  1.00 26.59  ? 180  SER A O     1 
ATOM   1322 C CB    . SER A 1 201 ? 36.930 5.964   8.687   1.00 36.74  ? 180  SER A CB    1 
ATOM   1323 O OG    . SER A 1 201 ? 36.097 6.131   7.557   1.00 48.79  ? 180  SER A OG    1 
ATOM   1324 N N     . GLY A 1 202 ? 34.762 4.368   10.404  1.00 23.72  ? 181  GLY A N     1 
ATOM   1325 C CA    . GLY A 1 202 ? 34.470 3.164   11.166  1.00 23.11  ? 181  GLY A CA    1 
ATOM   1326 C C     . GLY A 1 202 ? 32.972 2.930   11.290  1.00 22.58  ? 181  GLY A C     1 
ATOM   1327 O O     . GLY A 1 202 ? 32.176 3.660   10.696  1.00 22.12  ? 181  GLY A O     1 
ATOM   1328 N N     . CYS A 1 203 ? 32.613 1.858   12.004  1.00 21.76  ? 182  CYS A N     1 
ATOM   1329 C CA    . CYS A 1 203 ? 31.223 1.531   12.276  1.00 21.36  ? 182  CYS A CA    1 
ATOM   1330 C C     . CYS A 1 203 ? 31.087 1.151   13.738  1.00 23.48  ? 182  CYS A C     1 
ATOM   1331 O O     . CYS A 1 203 ? 32.083 0.880   14.402  1.00 25.17  ? 182  CYS A O     1 
ATOM   1332 C CB    . CYS A 1 203 ? 30.757 0.406   11.367  1.00 24.74  ? 182  CYS A CB    1 
ATOM   1333 S SG    . CYS A 1 203 ? 31.606 -1.170  11.668  1.00 26.96  ? 182  CYS A SG    1 
ATOM   1334 N N     . ALA A 1 204 ? 29.844 1.172   14.244  1.00 20.60  ? 183  ALA A N     1 
ATOM   1335 C CA    . ALA A 1 204 ? 29.563 0.796   15.618  1.00 21.09  ? 183  ALA A CA    1 
ATOM   1336 C C     . ALA A 1 204 ? 28.059 0.630   15.806  1.00 22.31  ? 183  ALA A C     1 
ATOM   1337 O O     . ALA A 1 204 ? 27.273 1.283   15.116  1.00 18.02  ? 183  ALA A O     1 
ATOM   1338 C CB    . ALA A 1 204 ? 30.022 1.870   16.580  1.00 20.34  ? 183  ALA A CB    1 
ATOM   1339 N N     . LEU A 1 205 ? 27.711 -0.107  16.868  1.00 21.74  ? 184  LEU A N     1 
ATOM   1340 C CA    . LEU A 1 205 ? 26.378 -0.054  17.424  1.00 21.49  ? 184  LEU A CA    1 
ATOM   1341 C C     . LEU A 1 205 ? 26.128 1.358   17.918  1.00 20.26  ? 184  LEU A C     1 
ATOM   1342 O O     . LEU A 1 205 ? 27.008 1.990   18.508  1.00 22.34  ? 184  LEU A O     1 
ATOM   1343 C CB    . LEU A 1 205 ? 26.265 -1.048  18.569  1.00 22.00  ? 184  LEU A CB    1 
ATOM   1344 C CG    . LEU A 1 205 ? 26.397 -2.512  18.178  1.00 23.01  ? 184  LEU A CG    1 
ATOM   1345 C CD1   . LEU A 1 205 ? 26.342 -3.322  19.428  1.00 22.56  ? 184  LEU A CD1   1 
ATOM   1346 C CD2   . LEU A 1 205 ? 25.293 -2.892  17.187  1.00 22.46  ? 184  LEU A CD2   1 
ATOM   1347 N N     . THR A 1 206 ? 24.910 1.829   17.708  1.00 17.92  ? 185  THR A N     1 
ATOM   1348 C CA    . THR A 1 206 ? 24.503 3.122   18.220  1.00 18.24  ? 185  THR A CA    1 
ATOM   1349 C C     . THR A 1 206 ? 24.475 3.118   19.751  1.00 18.43  ? 185  THR A C     1 
ATOM   1350 O O     . THR A 1 206 ? 23.761 2.308   20.348  1.00 18.55  ? 185  THR A O     1 
ATOM   1351 C CB    . THR A 1 206 ? 23.114 3.472   17.678  1.00 18.52  ? 185  THR A CB    1 
ATOM   1352 O OG1   . THR A 1 206 ? 23.150 3.272   16.264  1.00 17.55  ? 185  THR A OG1   1 
ATOM   1353 C CG2   . THR A 1 206 ? 22.816 4.939   17.938  1.00 20.55  ? 185  THR A CG2   1 
ATOM   1354 N N     . PRO A 1 207 ? 25.204 4.039   20.428  1.00 18.59  ? 186  PRO A N     1 
ATOM   1355 C CA    . PRO A 1 207 ? 24.985 4.315   21.845  1.00 18.50  ? 186  PRO A CA    1 
ATOM   1356 C C     . PRO A 1 207 ? 23.604 4.948   22.017  1.00 17.24  ? 186  PRO A C     1 
ATOM   1357 O O     . PRO A 1 207 ? 23.218 5.805   21.228  1.00 17.05  ? 186  PRO A O     1 
ATOM   1358 C CB    . PRO A 1 207 ? 26.097 5.305   22.227  1.00 19.78  ? 186  PRO A CB    1 
ATOM   1359 C CG    . PRO A 1 207 ? 27.097 5.239   21.079  1.00 19.52  ? 186  PRO A CG    1 
ATOM   1360 C CD    . PRO A 1 207 ? 26.253 4.909   19.867  1.00 20.31  ? 186  PRO A CD    1 
ATOM   1361 N N     . LEU A 1 208 ? 22.885 4.561   23.068  1.00 17.01  ? 187  LEU A N     1 
ATOM   1362 C CA    . LEU A 1 208 ? 21.503 4.982   23.211  1.00 18.37  ? 187  LEU A CA    1 
ATOM   1363 C C     . LEU A 1 208 ? 21.270 5.799   24.471  1.00 19.12  ? 187  LEU A C     1 
ATOM   1364 O O     . LEU A 1 208 ? 21.794 5.464   25.536  1.00 19.03  ? 187  LEU A O     1 
ATOM   1365 C CB    . LEU A 1 208 ? 20.624 3.741   23.243  1.00 19.00  ? 187  LEU A CB    1 
ATOM   1366 C CG    . LEU A 1 208 ? 20.741 2.828   22.022  1.00 20.33  ? 187  LEU A CG    1 
ATOM   1367 C CD1   . LEU A 1 208 ? 20.034 1.532   22.274  1.00 21.05  ? 187  LEU A CD1   1 
ATOM   1368 C CD2   . LEU A 1 208 ? 20.204 3.473   20.757  1.00 21.64  ? 187  LEU A CD2   1 
ATOM   1369 N N     . ASN A 1 209 ? 20.343 6.767   24.361  1.00 17.50  ? 188  ASN A N     1 
ATOM   1370 C CA    . ASN A 1 209 ? 19.773 7.457   25.507  1.00 18.74  ? 188  ASN A CA    1 
ATOM   1371 C C     . ASN A 1 209 ? 18.678 6.616   26.160  1.00 19.10  ? 188  ASN A C     1 
ATOM   1372 O O     . ASN A 1 209 ? 17.493 6.962   26.106  1.00 18.62  ? 188  ASN A O     1 
ATOM   1373 C CB    . ASN A 1 209 ? 19.285 8.848   25.123  1.00 18.18  ? 188  ASN A CB    1 
ATOM   1374 C CG    . ASN A 1 209 ? 20.440 9.776   24.830  1.00 19.99  ? 188  ASN A CG    1 
ATOM   1375 O OD1   . ASN A 1 209 ? 20.714 10.118  23.664  1.00 19.64  ? 188  ASN A OD1   1 
ATOM   1376 N ND2   . ASN A 1 209 ? 21.149 10.144  25.883  1.00 21.85  ? 188  ASN A ND2   1 
ATOM   1377 N N     . GLU A 1 210 ? 19.101 5.526   26.812  1.00 20.53  ? 189  GLU A N     1 
ATOM   1378 C CA    . GLU A 1 210 ? 18.202 4.545   27.388  1.00 19.77  ? 189  GLU A CA    1 
ATOM   1379 C C     . GLU A 1 210 ? 18.728 4.107   28.739  1.00 21.34  ? 189  GLU A C     1 
ATOM   1380 O O     . GLU A 1 210 ? 19.945 3.963   28.914  1.00 20.76  ? 189  GLU A O     1 
ATOM   1381 C CB    . GLU A 1 210 ? 18.136 3.238   26.596  1.00 22.50  ? 189  GLU A CB    1 
ATOM   1382 C CG    . GLU A 1 210 ? 17.328 3.383   25.314  1.00 24.15  ? 189  GLU A CG    1 
ATOM   1383 C CD    . GLU A 1 210 ? 17.029 2.125   24.507  1.00 26.41  ? 189  GLU A CD    1 
ATOM   1384 O OE1   . GLU A 1 210 ? 17.058 1.002   25.062  1.00 26.99  ? 189  GLU A OE1   1 
ATOM   1385 O OE2   . GLU A 1 210 ? 16.779 2.307   23.290  1.00 30.45  ? 189  GLU A OE2   1 
ATOM   1386 N N     . ARG A 1 211 ? 17.790 3.868   29.661  1.00 20.77  ? 190  ARG A N     1 
ATOM   1387 C CA    . ARG A 1 211 ? 18.102 3.210   30.920  1.00 21.48  ? 190  ARG A CA    1 
ATOM   1388 C C     . ARG A 1 211 ? 17.103 2.060   31.071  1.00 21.96  ? 190  ARG A C     1 
ATOM   1389 O O     . ARG A 1 211 ? 15.895 2.286   30.941  1.00 18.16  ? 190  ARG A O     1 
ATOM   1390 C CB    . ARG A 1 211 ? 17.953 4.208   32.072  1.00 22.87  ? 190  ARG A CB    1 
ATOM   1391 C CG    . ARG A 1 211 ? 18.156 3.680   33.492  1.00 27.15  ? 190  ARG A CG    1 
ATOM   1392 C CD    . ARG A 1 211 ? 19.413 2.857   33.672  1.00 34.88  ? 190  ARG A CD    1 
ATOM   1393 N NE    . ARG A 1 211 ? 19.670 2.493   35.082  1.00 41.66  ? 190  ARG A NE    1 
ATOM   1394 C CZ    . ARG A 1 211 ? 20.812 1.985   35.528  1.00 42.38  ? 190  ARG A CZ    1 
ATOM   1395 N NH1   . ARG A 1 211 ? 21.782 1.664   34.687  1.00 44.54  ? 190  ARG A NH1   1 
ATOM   1396 N NH2   . ARG A 1 211 ? 20.980 1.799   36.818  1.00 51.25  ? 190  ARG A NH2   1 
ATOM   1397 N N     . ASN A 1 212 ? 17.609 0.832   31.279  1.00 23.30  ? 191  ASN A N     1 
ATOM   1398 C CA    . ASN A 1 212 ? 16.749 -0.348  31.413  1.00 24.97  ? 191  ASN A CA    1 
ATOM   1399 C C     . ASN A 1 212 ? 15.765 -0.474  30.244  1.00 23.00  ? 191  ASN A C     1 
ATOM   1400 O O     . ASN A 1 212 ? 14.625 -0.855  30.430  1.00 21.67  ? 191  ASN A O     1 
ATOM   1401 C CB    . ASN A 1 212 ? 16.037 -0.345  32.762  1.00 30.81  ? 191  ASN A CB    1 
ATOM   1402 C CG    . ASN A 1 212 ? 17.023 -0.494  33.906  1.00 41.81  ? 191  ASN A CG    1 
ATOM   1403 O OD1   . ASN A 1 212 ? 17.993 -1.260  33.816  1.00 50.58  ? 191  ASN A OD1   1 
ATOM   1404 N ND2   . ASN A 1 212 ? 16.843 0.267   34.976  1.00 50.23  ? 191  ASN A ND2   1 
ATOM   1405 N N     . GLY A 1 213 ? 16.193 -0.158  29.016  1.00 23.80  ? 192  GLY A N     1 
ATOM   1406 C CA    . GLY A 1 213 ? 15.369 -0.459  27.845  1.00 21.13  ? 192  GLY A CA    1 
ATOM   1407 C C     . GLY A 1 213 ? 14.250 0.559   27.589  1.00 20.90  ? 192  GLY A C     1 
ATOM   1408 O O     . GLY A 1 213 ? 13.363 0.320   26.755  1.00 19.87  ? 192  GLY A O     1 
ATOM   1409 N N     . ALA A 1 214 ? 14.281 1.684   28.314  1.00 18.18  ? 193  ALA A N     1 
ATOM   1410 C CA    . ALA A 1 214 ? 13.316 2.750   28.137  1.00 19.26  ? 193  ALA A CA    1 
ATOM   1411 C C     . ALA A 1 214 ? 14.062 4.068   27.901  1.00 19.68  ? 193  ALA A C     1 
ATOM   1412 O O     . ALA A 1 214 ? 15.196 4.252   28.335  1.00 17.67  ? 193  ALA A O     1 
ATOM   1413 C CB    . ALA A 1 214 ? 12.389 2.859   29.324  1.00 19.89  ? 193  ALA A CB    1 
ATOM   1414 N N     . ARG A 1 215 ? 13.412 4.997   27.196  1.00 19.55  ? 194  ARG A N     1 
ATOM   1415 C CA    . ARG A 1 215 ? 13.988 6.314   26.979  1.00 18.65  ? 194  ARG A CA    1 
ATOM   1416 C C     . ARG A 1 215 ? 14.468 6.901   28.307  1.00 19.12  ? 194  ARG A C     1 
ATOM   1417 O O     . ARG A 1 215 ? 13.741 6.835   29.302  1.00 17.43  ? 194  ARG A O     1 
ATOM   1418 C CB    . ARG A 1 215 ? 12.920 7.278   26.457  1.00 17.28  ? 194  ARG A CB    1 
ATOM   1419 C CG    . ARG A 1 215 ? 13.529 8.606   26.026  1.00 16.87  ? 194  ARG A CG    1 
ATOM   1420 C CD    . ARG A 1 215 ? 12.458 9.515   25.496  1.00 18.36  ? 194  ARG A CD    1 
ATOM   1421 N NE    . ARG A 1 215 ? 11.931 9.011   24.222  1.00 18.01  ? 194  ARG A NE    1 
ATOM   1422 C CZ    . ARG A 1 215 ? 12.447 9.235   23.023  1.00 18.53  ? 194  ARG A CZ    1 
ATOM   1423 N NH1   . ARG A 1 215 ? 13.506 10.030  22.851  1.00 18.06  ? 194  ARG A NH1   1 
ATOM   1424 N NH2   . ARG A 1 215 ? 11.901 8.658   21.973  1.00 18.28  ? 194  ARG A NH2   1 
ATOM   1425 N N     . TRP A 1 216 ? 15.665 7.510   28.276  1.00 19.26  ? 195  TRP A N     1 
ATOM   1426 C CA    . TRP A 1 216 ? 16.117 8.398   29.333  1.00 18.90  ? 195  TRP A CA    1 
ATOM   1427 C C     . TRP A 1 216 ? 16.440 9.772   28.739  1.00 17.27  ? 195  TRP A C     1 
ATOM   1428 O O     . TRP A 1 216 ? 17.531 9.989   28.205  1.00 15.52  ? 195  TRP A O     1 
ATOM   1429 C CB    . TRP A 1 216 ? 17.326 7.793   30.067  1.00 17.55  ? 195  TRP A CB    1 
ATOM   1430 C CG    . TRP A 1 216 ? 17.686 8.552   31.322  1.00 18.78  ? 195  TRP A CG    1 
ATOM   1431 C CD1   . TRP A 1 216 ? 18.704 9.447   31.488  1.00 19.35  ? 195  TRP A CD1   1 
ATOM   1432 C CD2   . TRP A 1 216 ? 17.093 8.389   32.619  1.00 18.38  ? 195  TRP A CD2   1 
ATOM   1433 N NE1   . TRP A 1 216 ? 18.729 9.904   32.778  1.00 17.88  ? 195  TRP A NE1   1 
ATOM   1434 C CE2   . TRP A 1 216 ? 17.764 9.269   33.495  1.00 18.06  ? 195  TRP A CE2   1 
ATOM   1435 C CE3   . TRP A 1 216 ? 16.032 7.610   33.113  1.00 19.05  ? 195  TRP A CE3   1 
ATOM   1436 C CZ2   . TRP A 1 216 ? 17.447 9.362   34.850  1.00 21.71  ? 195  TRP A CZ2   1 
ATOM   1437 C CZ3   . TRP A 1 216 ? 15.715 7.704   34.458  1.00 22.09  ? 195  TRP A CZ3   1 
ATOM   1438 C CH2   . TRP A 1 216 ? 16.423 8.553   35.312  1.00 24.55  ? 195  TRP A CH2   1 
ATOM   1439 N N     . SER A 1 217 ? 15.466 10.674  28.859  1.00 17.95  ? 196  SER A N     1 
ATOM   1440 C CA    . SER A 1 217 ? 15.483 11.979  28.206  1.00 18.33  ? 196  SER A CA    1 
ATOM   1441 C C     . SER A 1 217 ? 16.169 13.011  29.103  1.00 18.79  ? 196  SER A C     1 
ATOM   1442 O O     . SER A 1 217 ? 16.481 12.710  30.264  1.00 19.88  ? 196  SER A O     1 
ATOM   1443 C CB    . SER A 1 217 ? 14.072 12.404  27.911  1.00 17.19  ? 196  SER A CB    1 
ATOM   1444 O OG    . SER A 1 217 ? 13.431 12.866  29.095  1.00 15.22  ? 196  SER A OG    1 
ATOM   1445 N N     . ALA A 1 218 ? 16.315 14.248  28.602  1.00 17.83  ? 197  ALA A N     1 
ATOM   1446 C CA    . ALA A 1 218 ? 16.778 15.363  29.435  1.00 19.04  ? 197  ALA A CA    1 
ATOM   1447 C C     . ALA A 1 218 ? 15.800 15.674  30.580  1.00 19.01  ? 197  ALA A C     1 
ATOM   1448 O O     . ALA A 1 218 ? 16.184 16.279  31.586  1.00 21.05  ? 197  ALA A O     1 
ATOM   1449 C CB    . ALA A 1 218 ? 17.023 16.603  28.576  1.00 19.57  ? 197  ALA A CB    1 
ATOM   1450 N N     . ALA A 1 219 ? 14.513 15.364  30.389  1.00 17.72  ? 198  ALA A N     1 
ATOM   1451 C CA    . ALA A 1 219 ? 13.510 15.547  31.426  1.00 18.53  ? 198  ALA A CA    1 
ATOM   1452 C C     . ALA A 1 219 ? 13.726 14.528  32.542  1.00 21.38  ? 198  ALA A C     1 
ATOM   1453 O O     . ALA A 1 219 ? 13.557 14.856  33.713  1.00 21.18  ? 198  ALA A O     1 
ATOM   1454 C CB    . ALA A 1 219 ? 12.115 15.437  30.865  1.00 16.62  ? 198  ALA A CB    1 
ATOM   1455 N N     . ASP A 1 220 ? 14.099 13.311  32.164  1.00 19.90  ? 199  ASP A N     1 
ATOM   1456 C CA    . ASP A 1 220 ? 14.427 12.260  33.124  1.00 20.65  ? 199  ASP A CA    1 
ATOM   1457 C C     . ASP A 1 220 ? 15.697 12.598  33.894  1.00 21.60  ? 199  ASP A C     1 
ATOM   1458 O O     . ASP A 1 220 ? 15.697 12.521  35.123  1.00 20.59  ? 199  ASP A O     1 
ATOM   1459 C CB    . ASP A 1 220 ? 14.633 10.914  32.446  1.00 20.27  ? 199  ASP A CB    1 
ATOM   1460 C CG    . ASP A 1 220 ? 13.351 10.339  31.856  1.00 20.34  ? 199  ASP A CG    1 
ATOM   1461 O OD1   . ASP A 1 220 ? 12.344 10.424  32.572  1.00 20.91  ? 199  ASP A OD1   1 
ATOM   1462 O OD2   . ASP A 1 220 ? 13.344 9.890   30.681  1.00 21.36  ? 199  ASP A OD2   1 
ATOM   1463 N N     . GLY A 1 221 ? 16.764 12.951  33.156  1.00 19.58  ? 200  GLY A N     1 
ATOM   1464 C CA    . GLY A 1 221 ? 18.098 13.056  33.708  1.00 21.15  ? 200  GLY A CA    1 
ATOM   1465 C C     . GLY A 1 221 ? 18.306 14.358  34.482  1.00 22.39  ? 200  GLY A C     1 
ATOM   1466 O O     . GLY A 1 221 ? 18.988 14.349  35.498  1.00 21.15  ? 200  GLY A O     1 
ATOM   1467 N N     . TYR A 1 222 ? 17.779 15.473  33.951  1.00 22.16  ? 201  TYR A N     1 
ATOM   1468 C CA    . TYR A 1 222 ? 18.049 16.785  34.511  1.00 24.36  ? 201  TYR A CA    1 
ATOM   1469 C C     . TYR A 1 222 ? 16.843 17.335  35.260  1.00 23.15  ? 201  TYR A C     1 
ATOM   1470 O O     . TYR A 1 222 ? 16.957 17.744  36.410  1.00 26.52  ? 201  TYR A O     1 
ATOM   1471 C CB    . TYR A 1 222 ? 18.509 17.741  33.399  1.00 22.34  ? 201  TYR A CB    1 
ATOM   1472 C CG    . TYR A 1 222 ? 19.935 17.508  32.926  1.00 20.88  ? 201  TYR A CG    1 
ATOM   1473 C CD1   . TYR A 1 222 ? 20.196 16.603  31.902  1.00 19.00  ? 201  TYR A CD1   1 
ATOM   1474 C CD2   . TYR A 1 222 ? 21.022 18.183  33.492  1.00 17.83  ? 201  TYR A CD2   1 
ATOM   1475 C CE1   . TYR A 1 222 ? 21.486 16.380  31.456  1.00 20.05  ? 201  TYR A CE1   1 
ATOM   1476 C CE2   . TYR A 1 222 ? 22.321 17.945  33.051  1.00 16.89  ? 201  TYR A CE2   1 
ATOM   1477 C CZ    . TYR A 1 222 ? 22.542 17.083  32.005  1.00 17.39  ? 201  TYR A CZ    1 
ATOM   1478 O OH    . TYR A 1 222 ? 23.797 16.824  31.566  1.00 21.23  ? 201  TYR A OH    1 
ATOM   1479 N N     . LEU A 1 223 ? 15.691 17.393  34.593  1.00 23.00  ? 202  LEU A N     1 
ATOM   1480 C CA    . LEU A 1 223 ? 14.583 18.166  35.103  1.00 22.43  ? 202  LEU A CA    1 
ATOM   1481 C C     . LEU A 1 223 ? 13.938 17.469  36.291  1.00 22.10  ? 202  LEU A C     1 
ATOM   1482 O O     . LEU A 1 223 ? 13.721 18.098  37.330  1.00 22.72  ? 202  LEU A O     1 
ATOM   1483 C CB    . LEU A 1 223 ? 13.536 18.432  34.027  1.00 24.41  ? 202  LEU A CB    1 
ATOM   1484 C CG    . LEU A 1 223 ? 12.388 19.344  34.453  1.00 24.22  ? 202  LEU A CG    1 
ATOM   1485 C CD1   . LEU A 1 223 ? 12.927 20.710  34.866  1.00 24.59  ? 202  LEU A CD1   1 
ATOM   1486 C CD2   . LEU A 1 223 ? 11.345 19.510  33.368  1.00 24.66  ? 202  LEU A CD2   1 
ATOM   1487 N N     . ARG A 1 224 ? 13.532 16.209  36.114  1.00 22.47  ? 203  ARG A N     1 
ATOM   1488 C CA    . ARG A 1 224 ? 12.761 15.550  37.152  1.00 24.69  ? 203  ARG A CA    1 
ATOM   1489 C C     . ARG A 1 224 ? 13.463 15.600  38.507  1.00 24.26  ? 203  ARG A C     1 
ATOM   1490 O O     . ARG A 1 224 ? 12.821 15.968  39.466  1.00 23.18  ? 203  ARG A O     1 
ATOM   1491 C CB    . ARG A 1 224 ? 12.192 14.163  36.838  1.00 27.54  ? 203  ARG A CB    1 
ATOM   1492 C CG    . ARG A 1 224 ? 10.744 14.508  36.485  1.00 28.84  ? 203  ARG A CG    1 
ATOM   1493 C CD    . ARG A 1 224 ? 9.873  13.451  35.963  1.00 28.15  ? 203  ARG A CD    1 
ATOM   1494 N NE    . ARG A 1 224 ? 10.398 12.868  34.732  1.00 26.99  ? 203  ARG A NE    1 
ATOM   1495 C CZ    . ARG A 1 224 ? 9.933  13.210  33.528  1.00 26.66  ? 203  ARG A CZ    1 
ATOM   1496 N NH1   . ARG A 1 224 ? 10.346 12.535  32.472  1.00 25.16  ? 203  ARG A NH1   1 
ATOM   1497 N NH2   . ARG A 1 224 ? 9.081  14.221  33.391  1.00 25.12  ? 203  ARG A NH2   1 
ATOM   1498 N N     . PRO A 1 225 ? 14.749 15.253  38.655  1.00 25.04  ? 204  PRO A N     1 
ATOM   1499 C CA    . PRO A 1 225 ? 15.390 15.339  39.971  1.00 26.29  ? 204  PRO A CA    1 
ATOM   1500 C C     . PRO A 1 225 ? 15.326 16.737  40.604  1.00 30.82  ? 204  PRO A C     1 
ATOM   1501 O O     . PRO A 1 225 ? 15.388 16.854  41.819  1.00 32.30  ? 204  PRO A O     1 
ATOM   1502 C CB    . PRO A 1 225 ? 16.814 14.909  39.621  1.00 26.36  ? 204  PRO A CB    1 
ATOM   1503 C CG    . PRO A 1 225 ? 16.639 13.980  38.422  1.00 27.19  ? 204  PRO A CG    1 
ATOM   1504 C CD    . PRO A 1 225 ? 15.625 14.708  37.602  1.00 24.97  ? 204  PRO A CD    1 
ATOM   1505 N N     . ALA A 1 226 ? 15.158 17.796  39.785  1.00 27.10  ? 205  ALA A N     1 
ATOM   1506 C CA    . ALA A 1 226 ? 15.159 19.169  40.279  1.00 28.07  ? 205  ALA A CA    1 
ATOM   1507 C C     . ALA A 1 226 ? 13.766 19.655  40.674  1.00 28.79  ? 205  ALA A C     1 
ATOM   1508 O O     . ALA A 1 226 ? 13.635 20.722  41.259  1.00 24.83  ? 205  ALA A O     1 
ATOM   1509 C CB    . ALA A 1 226 ? 15.728 20.078  39.208  1.00 29.54  ? 205  ALA A CB    1 
ATOM   1510 N N     . MET A 1 227 ? 12.718 18.909  40.322  1.00 26.60  ? 206  MET A N     1 
ATOM   1511 C CA    . MET A 1 227 ? 11.384 19.479  40.360  1.00 28.44  ? 206  MET A CA    1 
ATOM   1512 C C     . MET A 1 227 ? 10.794 19.531  41.774  1.00 30.94  ? 206  MET A C     1 
ATOM   1513 O O     . MET A 1 227 ? 9.784  20.205  41.953  1.00 30.54  ? 206  MET A O     1 
ATOM   1514 C CB    . MET A 1 227 ? 10.445 18.756  39.399  1.00 27.88  ? 206  MET A CB    1 
ATOM   1515 C CG    . MET A 1 227 ? 10.665 19.202  37.967  1.00 31.71  ? 206  MET A CG    1 
ATOM   1516 S SD    . MET A 1 227 ? 9.671  18.288  36.777  1.00 36.32  ? 206  MET A SD    1 
ATOM   1517 C CE    . MET A 1 227 ? 8.081  18.872  37.393  1.00 36.16  ? 206  MET A CE    1 
ATOM   1518 N N     . ASP A 1 228 ? 11.435 18.889  42.764  1.00 32.16  ? 207  ASP A N     1 
ATOM   1519 C CA    . ASP A 1 228 ? 11.057 19.063  44.165  1.00 41.27  ? 207  ASP A CA    1 
ATOM   1520 C C     . ASP A 1 228 ? 11.629 20.344  44.762  1.00 40.14  ? 207  ASP A C     1 
ATOM   1521 O O     . ASP A 1 228 ? 11.260 20.713  45.879  1.00 41.20  ? 207  ASP A O     1 
ATOM   1522 C CB    . ASP A 1 228 ? 11.471 17.889  45.038  1.00 45.01  ? 207  ASP A CB    1 
ATOM   1523 C CG    . ASP A 1 228 ? 10.655 16.636  44.769  1.00 54.42  ? 207  ASP A CG    1 
ATOM   1524 O OD1   . ASP A 1 228 ? 9.420  16.770  44.672  1.00 56.26  ? 207  ASP A OD1   1 
ATOM   1525 O OD2   . ASP A 1 228 ? 11.260 15.555  44.622  1.00 67.27  ? 207  ASP A OD2   1 
ATOM   1526 N N     . ARG A 1 229 ? 12.531 21.015  44.033  1.00 32.02  ? 208  ARG A N     1 
ATOM   1527 C CA    . ARG A 1 229 ? 13.110 22.245  44.542  1.00 30.57  ? 208  ARG A CA    1 
ATOM   1528 C C     . ARG A 1 229 ? 12.039 23.316  44.666  1.00 31.24  ? 208  ARG A C     1 
ATOM   1529 O O     . ARG A 1 229 ? 11.288 23.585  43.730  1.00 29.59  ? 208  ARG A O     1 
ATOM   1530 C CB    . ARG A 1 229 ? 14.251 22.756  43.665  1.00 27.86  ? 208  ARG A CB    1 
ATOM   1531 C CG    . ARG A 1 229 ? 15.385 21.762  43.738  1.00 26.78  ? 208  ARG A CG    1 
ATOM   1532 C CD    . ARG A 1 229 ? 16.451 22.152  42.760  1.00 27.35  ? 208  ARG A CD    1 
ATOM   1533 N NE    . ARG A 1 229 ? 17.444 21.077  42.726  1.00 28.02  ? 208  ARG A NE    1 
ATOM   1534 C CZ    . ARG A 1 229 ? 18.329 20.912  41.771  1.00 32.70  ? 208  ARG A CZ    1 
ATOM   1535 N NH1   . ARG A 1 229 ? 18.451 21.831  40.804  1.00 33.35  ? 208  ARG A NH1   1 
ATOM   1536 N NH2   . ARG A 1 229 ? 19.121 19.862  41.823  1.00 31.43  ? 208  ARG A NH2   1 
ATOM   1537 N N     . GLY A 1 230 ? 12.053 23.997  45.819  1.00 28.46  ? 209  GLY A N     1 
ATOM   1538 C CA    . GLY A 1 230 ? 11.134 25.089  46.054  1.00 28.32  ? 209  GLY A CA    1 
ATOM   1539 C C     . GLY A 1 230 ? 11.376 26.297  45.140  1.00 27.78  ? 209  GLY A C     1 
ATOM   1540 O O     . GLY A 1 230 ? 10.474 27.090  44.934  1.00 27.88  ? 209  GLY A O     1 
ATOM   1541 N N     . ASN A 1 231 ? 12.575 26.449  44.585  1.00 26.99  ? 210  ASN A N     1 
ATOM   1542 C CA    . ASN A 1 231 ? 12.891 27.624  43.781  1.00 27.95  ? 210  ASN A CA    1 
ATOM   1543 C C     . ASN A 1 231 ? 12.773 27.387  42.267  1.00 28.12  ? 210  ASN A C     1 
ATOM   1544 O O     . ASN A 1 231 ? 13.204 28.241  41.483  1.00 27.22  ? 210  ASN A O     1 
ATOM   1545 C CB    . ASN A 1 231 ? 14.300 28.090  44.113  1.00 27.77  ? 210  ASN A CB    1 
ATOM   1546 C CG    . ASN A 1 231 ? 15.318 26.998  43.912  1.00 26.86  ? 210  ASN A CG    1 
ATOM   1547 O OD1   . ASN A 1 231 ? 15.077 25.845  44.285  1.00 33.55  ? 210  ASN A OD1   1 
ATOM   1548 N ND2   . ASN A 1 231 ? 16.477 27.336  43.375  1.00 28.32  ? 210  ASN A ND2   1 
ATOM   1549 N N     . LEU A 1 232 ? 12.186 26.261  41.842  1.00 27.91  ? 211  LEU A N     1 
ATOM   1550 C CA    . LEU A 1 232 ? 12.004 25.974  40.415  1.00 24.47  ? 211  LEU A CA    1 
ATOM   1551 C C     . LEU A 1 232 ? 10.520 25.858  40.127  1.00 25.55  ? 211  LEU A C     1 
ATOM   1552 O O     . LEU A 1 232 ? 9.850  25.023  40.728  1.00 24.23  ? 211  LEU A O     1 
ATOM   1553 C CB    . LEU A 1 232 ? 12.727 24.683  40.029  1.00 24.09  ? 211  LEU A CB    1 
ATOM   1554 C CG    . LEU A 1 232 ? 12.553 24.201  38.584  1.00 24.31  ? 211  LEU A CG    1 
ATOM   1555 C CD1   . LEU A 1 232 ? 13.047 25.250  37.578  1.00 26.38  ? 211  LEU A CD1   1 
ATOM   1556 C CD2   . LEU A 1 232 ? 13.263 22.862  38.375  1.00 22.86  ? 211  LEU A CD2   1 
ATOM   1557 N N     . GLU A 1 233 ? 10.026 26.641  39.160  1.00 22.28  ? 212  GLU A N     1 
ATOM   1558 C CA    . GLU A 1 233 ? 8.660  26.501  38.708  1.00 24.45  ? 212  GLU A CA    1 
ATOM   1559 C C     . GLU A 1 233 ? 8.701  26.035  37.260  1.00 24.10  ? 212  GLU A C     1 
ATOM   1560 O O     . GLU A 1 233 ? 9.311  26.669  36.408  1.00 23.70  ? 212  GLU A O     1 
ATOM   1561 C CB    . GLU A 1 233 ? 7.833  27.783  38.784  1.00 28.09  ? 212  GLU A CB    1 
ATOM   1562 C CG    . GLU A 1 233 ? 7.727  28.326  40.205  1.00 38.25  ? 212  GLU A CG    1 
ATOM   1563 C CD    . GLU A 1 233 ? 6.887  27.416  41.082  1.00 41.25  ? 212  GLU A CD    1 
ATOM   1564 O OE1   . GLU A 1 233 ? 6.124  26.624  40.486  1.00 38.18  ? 212  GLU A OE1   1 
ATOM   1565 O OE2   . GLU A 1 233 ? 7.049  27.431  42.329  1.00 53.28  ? 212  GLU A OE2   1 
ATOM   1566 N N     . VAL A 1 234 ? 8.066  24.901  37.013  1.00 21.41  ? 213  VAL A N     1 
ATOM   1567 C CA    . VAL A 1 234 ? 7.977  24.370  35.672  1.00 22.25  ? 213  VAL A CA    1 
ATOM   1568 C C     . VAL A 1 234 ? 6.574  24.681  35.219  1.00 22.16  ? 213  VAL A C     1 
ATOM   1569 O O     . VAL A 1 234 ? 5.621  24.175  35.805  1.00 21.56  ? 213  VAL A O     1 
ATOM   1570 C CB    . VAL A 1 234 ? 8.282  22.869  35.600  1.00 24.56  ? 213  VAL A CB    1 
ATOM   1571 C CG1   . VAL A 1 234 ? 8.034  22.312  34.214  1.00 28.34  ? 213  VAL A CG1   1 
ATOM   1572 C CG2   . VAL A 1 234 ? 9.693  22.549  36.068  1.00 24.12  ? 213  VAL A CG2   1 
ATOM   1573 N N     . ILE A 1 235 ? 6.464  25.532  34.197  1.00 19.21  ? 214  ILE A N     1 
ATOM   1574 C CA    . ILE A 1 235 ? 5.167  25.997  33.723  1.00 22.52  ? 214  ILE A CA    1 
ATOM   1575 C C     . ILE A 1 235 ? 4.884  25.413  32.338  1.00 21.76  ? 214  ILE A C     1 
ATOM   1576 O O     . ILE A 1 235 ? 5.552  25.800  31.374  1.00 24.75  ? 214  ILE A O     1 
ATOM   1577 C CB    . ILE A 1 235 ? 5.180  27.533  33.684  1.00 24.01  ? 214  ILE A CB    1 
ATOM   1578 C CG1   . ILE A 1 235 ? 5.585  28.100  35.051  1.00 25.66  ? 214  ILE A CG1   1 
ATOM   1579 C CG2   . ILE A 1 235 ? 3.851  28.095  33.143  1.00 25.82  ? 214  ILE A CG2   1 
ATOM   1580 C CD1   . ILE A 1 235 ? 5.882  29.586  35.054  1.00 28.07  ? 214  ILE A CD1   1 
ATOM   1581 N N     . THR A 1 236 ? 3.906  24.496  32.241  1.00 20.60  ? 215  THR A N     1 
ATOM   1582 C CA    . THR A 1 236 ? 3.611  23.795  30.995  1.00 22.93  ? 215  THR A CA    1 
ATOM   1583 C C     . THR A 1 236 ? 2.372  24.401  30.362  1.00 23.71  ? 215  THR A C     1 
ATOM   1584 O O     . THR A 1 236 ? 1.659  25.212  30.964  1.00 24.05  ? 215  THR A O     1 
ATOM   1585 C CB    . THR A 1 236 ? 3.434  22.285  31.196  1.00 25.25  ? 215  THR A CB    1 
ATOM   1586 O OG1   . THR A 1 236 ? 2.462  22.113  32.217  1.00 22.54  ? 215  THR A OG1   1 
ATOM   1587 C CG2   . THR A 1 236 ? 4.698  21.597  31.677  1.00 24.66  ? 215  THR A CG2   1 
ATOM   1588 N N     . GLY A 1 237 ? 2.165  24.066  29.101  1.00 22.35  ? 216  GLY A N     1 
ATOM   1589 C CA    . GLY A 1 237 ? 0.963  24.482  28.409  1.00 23.35  ? 216  GLY A CA    1 
ATOM   1590 C C     . GLY A 1 237 ? 1.005  25.975  28.123  1.00 24.99  ? 216  GLY A C     1 
ATOM   1591 O O     . GLY A 1 237 ? -0.050 26.576  27.955  1.00 24.42  ? 216  GLY A O     1 
ATOM   1592 N N     . GLU A 1 238 ? 2.206  26.578  28.050  1.00 21.19  ? 217  GLU A N     1 
ATOM   1593 C CA    . GLU A 1 238 ? 2.273  28.009  27.819  1.00 22.70  ? 217  GLU A CA    1 
ATOM   1594 C C     . GLU A 1 238 ? 3.278  28.353  26.719  1.00 21.66  ? 217  GLU A C     1 
ATOM   1595 O O     . GLU A 1 238 ? 4.479  28.322  26.966  1.00 21.63  ? 217  GLU A O     1 
ATOM   1596 C CB    . GLU A 1 238 ? 2.709  28.738  29.103  1.00 25.75  ? 217  GLU A CB    1 
ATOM   1597 C CG    . GLU A 1 238 ? 1.654  28.743  30.201  1.00 27.61  ? 217  GLU A CG    1 
ATOM   1598 C CD    . GLU A 1 238 ? 0.428  29.616  29.951  1.00 30.32  ? 217  GLU A CD    1 
ATOM   1599 O OE1   . GLU A 1 238 ? 0.306  30.356  28.939  1.00 27.16  ? 217  GLU A OE1   1 
ATOM   1600 O OE2   . GLU A 1 238 ? -0.465 29.507  30.812  1.00 35.24  ? 217  GLU A OE2   1 
ATOM   1601 N N     . GLN A 1 239 ? 2.764  28.708  25.537  1.00 21.87  ? 218  GLN A N     1 
ATOM   1602 C CA    . GLN A 1 239 ? 3.601  29.153  24.449  1.00 23.72  ? 218  GLN A CA    1 
ATOM   1603 C C     . GLN A 1 239 ? 3.953  30.610  24.714  1.00 21.92  ? 218  GLN A C     1 
ATOM   1604 O O     . GLN A 1 239 ? 3.073  31.427  24.972  1.00 21.02  ? 218  GLN A O     1 
ATOM   1605 C CB    . GLN A 1 239 ? 2.902  28.961  23.099  1.00 23.38  ? 218  GLN A CB    1 
ATOM   1606 C CG    . GLN A 1 239 ? 3.761  29.355  21.902  1.00 22.69  ? 218  GLN A CG    1 
ATOM   1607 C CD    . GLN A 1 239 ? 3.234  28.787  20.605  1.00 25.96  ? 218  GLN A CD    1 
ATOM   1608 O OE1   . GLN A 1 239 ? 2.487  27.802  20.606  1.00 28.23  ? 218  GLN A OE1   1 
ATOM   1609 N NE2   . GLN A 1 239 ? 3.697  29.325  19.487  1.00 28.67  ? 218  GLN A NE2   1 
ATOM   1610 N N     . VAL A 1 240 ? 5.249  30.908  24.689  1.00 20.51  ? 219  VAL A N     1 
ATOM   1611 C CA    . VAL A 1 240 ? 5.719  32.276  24.834  1.00 21.07  ? 219  VAL A CA    1 
ATOM   1612 C C     . VAL A 1 240 ? 5.518  33.029  23.518  1.00 23.43  ? 219  VAL A C     1 
ATOM   1613 O O     . VAL A 1 240 ? 5.753  32.476  22.429  1.00 23.19  ? 219  VAL A O     1 
ATOM   1614 C CB    . VAL A 1 240 ? 7.184  32.237  25.292  1.00 21.51  ? 219  VAL A CB    1 
ATOM   1615 C CG1   . VAL A 1 240 ? 7.837  33.618  25.269  1.00 21.86  ? 219  VAL A CG1   1 
ATOM   1616 C CG2   . VAL A 1 240 ? 7.308  31.577  26.655  1.00 22.36  ? 219  VAL A CG2   1 
ATOM   1617 N N     . HIS A 1 241 ? 5.061  34.289  23.616  1.00 20.90  ? 220  HIS A N     1 
ATOM   1618 C CA    . HIS A 1 241 ? 4.742  35.072  22.435  1.00 22.40  ? 220  HIS A CA    1 
ATOM   1619 C C     . HIS A 1 241 ? 5.897  35.987  22.048  1.00 22.10  ? 220  HIS A C     1 
ATOM   1620 O O     . HIS A 1 241 ? 6.066  36.248  20.863  1.00 21.77  ? 220  HIS A O     1 
ATOM   1621 C CB    . HIS A 1 241 ? 3.473  35.909  22.605  1.00 23.67  ? 220  HIS A CB    1 
ATOM   1622 C CG    . HIS A 1 241 ? 2.231  35.074  22.623  1.00 29.09  ? 220  HIS A CG    1 
ATOM   1623 N ND1   . HIS A 1 241 ? 0.960  35.612  22.644  1.00 30.23  ? 220  HIS A ND1   1 
ATOM   1624 C CD2   . HIS A 1 241 ? 2.066  33.747  22.633  1.00 32.99  ? 220  HIS A CD2   1 
ATOM   1625 C CE1   . HIS A 1 241 ? 0.064  34.650  22.645  1.00 31.93  ? 220  HIS A CE1   1 
ATOM   1626 N NE2   . HIS A 1 241 ? 0.703  33.504  22.653  1.00 34.81  ? 220  HIS A NE2   1 
ATOM   1627 N N     . ARG A 1 242 ? 6.631  36.499  23.040  1.00 22.39  ? 221  ARG A N     1 
ATOM   1628 C CA    . ARG A 1 242 ? 7.785  37.338  22.777  1.00 24.01  ? 221  ARG A CA    1 
ATOM   1629 C C     . ARG A 1 242 ? 8.520  37.662  24.071  1.00 21.90  ? 221  ARG A C     1 
ATOM   1630 O O     . ARG A 1 242 ? 8.051  37.386  25.180  1.00 23.69  ? 221  ARG A O     1 
ATOM   1631 C CB    . ARG A 1 242 ? 7.397  38.651  22.084  1.00 28.49  ? 221  ARG A CB    1 
ATOM   1632 C CG    . ARG A 1 242 ? 6.416  39.469  22.892  1.00 33.94  ? 221  ARG A CG    1 
ATOM   1633 C CD    . ARG A 1 242 ? 6.174  40.786  22.161  1.00 41.15  ? 221  ARG A CD    1 
ATOM   1634 N NE    . ARG A 1 242 ? 5.048  41.472  22.796  1.00 52.01  ? 221  ARG A NE    1 
ATOM   1635 C CZ    . ARG A 1 242 ? 5.011  42.726  23.264  1.00 62.68  ? 221  ARG A CZ    1 
ATOM   1636 N NH1   . ARG A 1 242 ? 6.056  43.531  23.164  1.00 65.87  ? 221  ARG A NH1   1 
ATOM   1637 N NH2   . ARG A 1 242 ? 3.901  43.170  23.834  1.00 60.83  ? 221  ARG A NH2   1 
ATOM   1638 N N     . VAL A 1 243 ? 9.713  38.223  23.884  1.00 21.00  ? 222  VAL A N     1 
ATOM   1639 C CA    . VAL A 1 243 ? 10.518 38.736  24.967  1.00 22.16  ? 222  VAL A CA    1 
ATOM   1640 C C     . VAL A 1 243 ? 10.178 40.219  25.085  1.00 22.37  ? 222  VAL A C     1 
ATOM   1641 O O     . VAL A 1 243 ? 10.133 40.910  24.075  1.00 24.32  ? 222  VAL A O     1 
ATOM   1642 C CB    . VAL A 1 243 ? 12.029 38.508  24.756  1.00 23.07  ? 222  VAL A CB    1 
ATOM   1643 C CG1   . VAL A 1 243 ? 12.873 38.971  25.945  1.00 22.49  ? 222  VAL A CG1   1 
ATOM   1644 C CG2   . VAL A 1 243 ? 12.338 37.043  24.440  1.00 24.51  ? 222  VAL A CG2   1 
ATOM   1645 N N     . LEU A 1 244 ? 9.966  40.664  26.334  1.00 26.29  ? 223  LEU A N     1 
ATOM   1646 C CA    . LEU A 1 244 ? 9.736  42.060  26.695  1.00 27.00  ? 223  LEU A CA    1 
ATOM   1647 C C     . LEU A 1 244 ? 11.092 42.729  26.895  1.00 25.11  ? 223  LEU A C     1 
ATOM   1648 O O     . LEU A 1 244 ? 11.975 42.181  27.577  1.00 25.01  ? 223  LEU A O     1 
ATOM   1649 C CB    . LEU A 1 244 ? 8.891  42.117  27.967  1.00 31.20  ? 223  LEU A CB    1 
ATOM   1650 C CG    . LEU A 1 244 ? 7.459  41.574  27.825  1.00 38.57  ? 223  LEU A CG    1 
ATOM   1651 C CD1   . LEU A 1 244 ? 6.734  41.634  29.163  1.00 44.05  ? 223  LEU A CD1   1 
ATOM   1652 C CD2   . LEU A 1 244 ? 6.625  42.293  26.752  1.00 40.83  ? 223  LEU A CD2   1 
ATOM   1653 N N     . LEU A 1 245 ? 11.257 43.867  26.214  1.00 23.49  ? 224  LEU A N     1 
ATOM   1654 C CA    . LEU A 1 245 ? 12.474 44.663  26.231  1.00 23.00  ? 224  LEU A CA    1 
ATOM   1655 C C     . LEU A 1 245 ? 12.151 46.034  26.812  1.00 23.13  ? 224  LEU A C     1 
ATOM   1656 O O     . LEU A 1 245 ? 11.171 46.640  26.403  1.00 22.82  ? 224  LEU A O     1 
ATOM   1657 C CB    . LEU A 1 245 ? 12.993 44.835  24.809  1.00 25.01  ? 224  LEU A CB    1 
ATOM   1658 C CG    . LEU A 1 245 ? 13.340 43.553  24.051  1.00 25.17  ? 224  LEU A CG    1 
ATOM   1659 C CD1   . LEU A 1 245 ? 13.751 43.940  22.638  1.00 26.83  ? 224  LEU A CD1   1 
ATOM   1660 C CD2   . LEU A 1 245 ? 14.402 42.748  24.757  1.00 25.56  ? 224  LEU A CD2   1 
ATOM   1661 N N     . GLU A 1 246 ? 12.987 46.506  27.732  1.00 23.05  ? 225  GLU A N     1 
ATOM   1662 C CA    . GLU A 1 246 ? 12.824 47.832  28.319  1.00 25.37  ? 225  GLU A CA    1 
ATOM   1663 C C     . GLU A 1 246 ? 14.207 48.401  28.574  1.00 24.47  ? 225  GLU A C     1 
ATOM   1664 O O     . GLU A 1 246 ? 15.033 47.736  29.211  1.00 25.72  ? 225  GLU A O     1 
ATOM   1665 C CB    . GLU A 1 246 ? 12.104 47.799  29.665  1.00 32.49  ? 225  GLU A CB    1 
ATOM   1666 C CG    . GLU A 1 246 ? 10.661 47.302  29.611  1.00 42.69  ? 225  GLU A CG    1 
ATOM   1667 C CD    . GLU A 1 246 ? 10.009 47.168  30.988  1.00 53.65  ? 225  GLU A CD    1 
ATOM   1668 O OE1   . GLU A 1 246 ? 9.618  46.039  31.366  1.00 56.71  ? 225  GLU A OE1   1 
ATOM   1669 O OE2   . GLU A 1 246 ? 9.904  48.198  31.696  1.00 65.16  ? 225  GLU A OE2   1 
ATOM   1670 N N     . ASP A 1 247 ? 14.460 49.592  28.032  1.00 26.99  ? 226  ASP A N     1 
ATOM   1671 C CA    . ASP A 1 247 ? 15.727 50.282  28.219  1.00 29.05  ? 226  ASP A CA    1 
ATOM   1672 C C     . ASP A 1 247 ? 16.906 49.344  27.930  1.00 28.49  ? 226  ASP A C     1 
ATOM   1673 O O     . ASP A 1 247 ? 17.888 49.311  28.680  1.00 29.20  ? 226  ASP A O     1 
ATOM   1674 C CB    . ASP A 1 247 ? 15.770 50.888  29.609  1.00 30.54  ? 226  ASP A CB    1 
ATOM   1675 C CG    . ASP A 1 247 ? 14.578 51.782  29.960  1.00 31.64  ? 226  ASP A CG    1 
ATOM   1676 O OD1   . ASP A 1 247 ? 14.230 52.641  29.149  1.00 33.54  ? 226  ASP A OD1   1 
ATOM   1677 O OD2   . ASP A 1 247 ? 13.982 51.571  31.020  1.00 31.59  ? 226  ASP A OD2   1 
ATOM   1678 N N     . GLY A 1 248 ? 16.801 48.593  26.835  1.00 30.62  ? 227  GLY A N     1 
ATOM   1679 C CA    . GLY A 1 248 ? 17.915 47.814  26.308  1.00 31.29  ? 227  GLY A CA    1 
ATOM   1680 C C     . GLY A 1 248 ? 18.129 46.480  27.031  1.00 28.36  ? 227  GLY A C     1 
ATOM   1681 O O     . GLY A 1 248 ? 19.127 45.793  26.805  1.00 29.86  ? 227  GLY A O     1 
ATOM   1682 N N     . ARG A 1 249 ? 17.176 46.076  27.871  1.00 26.45  ? 228  ARG A N     1 
ATOM   1683 C CA    . ARG A 1 249 ? 17.305 44.838  28.622  1.00 25.63  ? 228  ARG A CA    1 
ATOM   1684 C C     . ARG A 1 249 ? 16.046 43.993  28.434  1.00 23.35  ? 228  ARG A C     1 
ATOM   1685 O O     . ARG A 1 249 ? 14.956 44.535  28.374  1.00 22.37  ? 228  ARG A O     1 
ATOM   1686 C CB    . ARG A 1 249 ? 17.559 45.261  30.076  1.00 29.87  ? 228  ARG A CB    1 
ATOM   1687 C CG    . ARG A 1 249 ? 17.362 44.187  31.134  1.00 39.40  ? 228  ARG A CG    1 
ATOM   1688 C CD    . ARG A 1 249 ? 17.711 44.627  32.563  1.00 43.02  ? 228  ARG A CD    1 
ATOM   1689 N NE    . ARG A 1 249 ? 18.593 43.606  33.152  1.00 56.65  ? 228  ARG A NE    1 
ATOM   1690 C CZ    . ARG A 1 249 ? 19.936 43.586  33.052  1.00 61.57  ? 228  ARG A CZ    1 
ATOM   1691 N NH1   . ARG A 1 249 ? 20.585 44.683  32.693  1.00 63.28  ? 228  ARG A NH1   1 
ATOM   1692 N NH2   . ARG A 1 249 ? 20.632 42.499  33.364  1.00 58.71  ? 228  ARG A NH2   1 
ATOM   1693 N N     . ALA A 1 250 ? 16.203 42.672  28.452  1.00 21.50  ? 229  ALA A N     1 
ATOM   1694 C CA    . ALA A 1 250 ? 15.074 41.756  28.510  1.00 22.88  ? 229  ALA A CA    1 
ATOM   1695 C C     . ALA A 1 250 ? 14.546 41.730  29.935  1.00 22.95  ? 229  ALA A C     1 
ATOM   1696 O O     . ALA A 1 250 ? 15.275 41.317  30.819  1.00 24.79  ? 229  ALA A O     1 
ATOM   1697 C CB    . ALA A 1 250 ? 15.493 40.372  28.057  1.00 21.89  ? 229  ALA A CB    1 
ATOM   1698 N N     . THR A 1 251 ? 13.276 42.083  30.138  1.00 23.40  ? 230  THR A N     1 
ATOM   1699 C CA    . THR A 1 251 ? 12.728 42.201  31.481  1.00 27.22  ? 230  THR A CA    1 
ATOM   1700 C C     . THR A 1 251 ? 11.799 41.030  31.811  1.00 27.85  ? 230  THR A C     1 
ATOM   1701 O O     . THR A 1 251 ? 11.451 40.816  32.973  1.00 25.42  ? 230  THR A O     1 
ATOM   1702 C CB    . THR A 1 251 ? 12.016 43.543  31.611  1.00 28.43  ? 230  THR A CB    1 
ATOM   1703 O OG1   . THR A 1 251 ? 11.011 43.526  30.608  1.00 29.87  ? 230  THR A OG1   1 
ATOM   1704 C CG2   . THR A 1 251 ? 12.979 44.690  31.394  1.00 32.16  ? 230  THR A CG2   1 
ATOM   1705 N N     . GLY A 1 252 ? 11.432 40.247  30.800  1.00 26.52  ? 231  GLY A N     1 
ATOM   1706 C CA    . GLY A 1 252 ? 10.548 39.112  31.020  1.00 27.13  ? 231  GLY A CA    1 
ATOM   1707 C C     . GLY A 1 252 ? 10.082 38.524  29.699  1.00 23.48  ? 231  GLY A C     1 
ATOM   1708 O O     . GLY A 1 252 ? 10.664 38.829  28.655  1.00 22.97  ? 231  GLY A O     1 
ATOM   1709 N N     . VAL A 1 253 ? 9.032  37.695  29.758  1.00 21.65  ? 232  VAL A N     1 
ATOM   1710 C CA    . VAL A 1 253 ? 8.447  37.114  28.557  1.00 23.06  ? 232  VAL A CA    1 
ATOM   1711 C C     . VAL A 1 253 ? 6.945  37.251  28.653  1.00 22.47  ? 232  VAL A C     1 
ATOM   1712 O O     . VAL A 1 253 ? 6.402  37.224  29.755  1.00 26.97  ? 232  VAL A O     1 
ATOM   1713 C CB    . VAL A 1 253 ? 8.845  35.639  28.357  1.00 21.96  ? 232  VAL A CB    1 
ATOM   1714 C CG1   . VAL A 1 253 ? 10.353 35.512  28.332  1.00 24.29  ? 232  VAL A CG1   1 
ATOM   1715 C CG2   . VAL A 1 253 ? 8.281  34.701  29.432  1.00 24.41  ? 232  VAL A CG2   1 
ATOM   1716 N N     . GLU A 1 254 ? 6.304  37.368  27.499  1.00 23.67  ? 233  GLU A N     1 
ATOM   1717 C CA    . GLU A 1 254 ? 4.865  37.501  27.434  1.00 26.46  ? 233  GLU A CA    1 
ATOM   1718 C C     . GLU A 1 254 ? 4.269  36.167  27.024  1.00 27.20  ? 233  GLU A C     1 
ATOM   1719 O O     . GLU A 1 254 ? 4.692  35.594  26.017  1.00 23.95  ? 233  GLU A O     1 
ATOM   1720 C CB    . GLU A 1 254 ? 4.524  38.594  26.435  1.00 34.03  ? 233  GLU A CB    1 
ATOM   1721 C CG    . GLU A 1 254 ? 3.024  38.857  26.363  1.00 41.63  ? 233  GLU A CG    1 
ATOM   1722 C CD    . GLU A 1 254 ? 2.724  40.251  25.833  1.00 49.48  ? 233  GLU A CD    1 
ATOM   1723 O OE1   . GLU A 1 254 ? 3.418  40.671  24.888  1.00 47.92  ? 233  GLU A OE1   1 
ATOM   1724 O OE2   . GLU A 1 254 ? 1.808  40.910  26.366  1.00 57.37  ? 233  GLU A OE2   1 
ATOM   1725 N N     . LEU A 1 255 ? 3.359  35.657  27.868  1.00 25.03  ? 234  LEU A N     1 
ATOM   1726 C CA    . LEU A 1 255 ? 2.498  34.529  27.560  1.00 24.89  ? 234  LEU A CA    1 
ATOM   1727 C C     . LEU A 1 255 ? 1.196  35.098  27.001  1.00 29.88  ? 234  LEU A C     1 
ATOM   1728 O O     . LEU A 1 255 ? 1.056  36.313  26.893  1.00 29.95  ? 234  LEU A O     1 
ATOM   1729 C CB    . LEU A 1 255 ? 2.242  33.698  28.815  1.00 24.69  ? 234  LEU A CB    1 
ATOM   1730 C CG    . LEU A 1 255 ? 3.450  33.411  29.703  1.00 29.18  ? 234  LEU A CG    1 
ATOM   1731 C CD1   . LEU A 1 255 ? 3.077  32.482  30.852  1.00 30.27  ? 234  LEU A CD1   1 
ATOM   1732 C CD2   . LEU A 1 255 ? 4.602  32.834  28.883  1.00 29.91  ? 234  LEU A CD2   1 
ATOM   1733 N N     . ALA A 1 256 ? 0.253  34.228  26.645  1.00 27.87  ? 235  ALA A N     1 
ATOM   1734 C CA    . ALA A 1 256 ? -1.028 34.688  26.145  1.00 30.99  ? 235  ALA A CA    1 
ATOM   1735 C C     . ALA A 1 256 ? -1.704 35.569  27.196  1.00 32.55  ? 235  ALA A C     1 
ATOM   1736 O O     . ALA A 1 256 ? -2.223 36.624  26.880  1.00 36.61  ? 235  ALA A O     1 
ATOM   1737 C CB    . ALA A 1 256 ? -1.925 33.533  25.764  1.00 30.94  ? 235  ALA A CB    1 
ATOM   1738 N N     . GLY A 1 257 ? -1.716 35.146  28.448  1.00 33.23  ? 236  GLY A N     1 
ATOM   1739 C CA    . GLY A 1 257 ? -2.577 35.812  29.412  1.00 37.34  ? 236  GLY A CA    1 
ATOM   1740 C C     . GLY A 1 257 ? -1.819 36.638  30.445  1.00 38.38  ? 236  GLY A C     1 
ATOM   1741 O O     . GLY A 1 257 ? -2.444 37.358  31.208  1.00 39.44  ? 236  GLY A O     1 
ATOM   1742 N N     . ARG A 1 258 ? -0.489 36.524  30.508  1.00 37.19  ? 237  ARG A N     1 
ATOM   1743 C CA    . ARG A 1 258 ? 0.249  37.205  31.558  1.00 33.54  ? 237  ARG A CA    1 
ATOM   1744 C C     . ARG A 1 258 ? 1.720  37.286  31.181  1.00 33.09  ? 237  ARG A C     1 
ATOM   1745 O O     . ARG A 1 258 ? 2.137  36.693  30.182  1.00 29.72  ? 237  ARG A O     1 
ATOM   1746 C CB    . ARG A 1 258 ? 0.081  36.450  32.883  1.00 36.57  ? 237  ARG A CB    1 
ATOM   1747 C CG    . ARG A 1 258 ? 0.570  35.008  32.910  1.00 36.75  ? 237  ARG A CG    1 
ATOM   1748 C CD    . ARG A 1 258 ? 0.386  34.403  34.297  1.00 35.56  ? 237  ARG A CD    1 
ATOM   1749 N NE    . ARG A 1 258 ? 1.058  33.115  34.502  1.00 36.14  ? 237  ARG A NE    1 
ATOM   1750 C CZ    . ARG A 1 258 ? 0.866  31.998  33.815  1.00 35.11  ? 237  ARG A CZ    1 
ATOM   1751 N NH1   . ARG A 1 258 ? -0.019 31.968  32.843  1.00 34.65  ? 237  ARG A NH1   1 
ATOM   1752 N NH2   . ARG A 1 258 ? 1.566  30.898  34.091  1.00 38.49  ? 237  ARG A NH2   1 
ATOM   1753 N N     . THR A 1 259 ? 2.477  37.989  32.028  1.00 26.04  ? 238  THR A N     1 
ATOM   1754 C CA    . THR A 1 259 ? 3.891  38.194  31.859  1.00 28.63  ? 238  THR A CA    1 
ATOM   1755 C C     . THR A 1 259 ? 4.627  37.520  32.999  1.00 28.87  ? 238  THR A C     1 
ATOM   1756 O O     . THR A 1 259 ? 4.171  37.606  34.132  1.00 30.03  ? 238  THR A O     1 
ATOM   1757 C CB    . THR A 1 259 ? 4.152  39.695  31.854  1.00 32.20  ? 238  THR A CB    1 
ATOM   1758 O OG1   . THR A 1 259 ? 3.738  40.111  30.567  1.00 35.82  ? 238  THR A OG1   1 
ATOM   1759 C CG2   . THR A 1 259 ? 5.622  40.060  31.918  1.00 35.35  ? 238  THR A CG2   1 
ATOM   1760 N N     . LEU A 1 260 ? 5.767  36.896  32.697  1.00 26.79  ? 239  LEU A N     1 
ATOM   1761 C CA    . LEU A 1 260 ? 6.701  36.417  33.704  1.00 26.95  ? 239  LEU A CA    1 
ATOM   1762 C C     . LEU A 1 260 ? 7.878  37.366  33.704  1.00 28.34  ? 239  LEU A C     1 
ATOM   1763 O O     . LEU A 1 260 ? 8.387  37.645  32.626  1.00 28.65  ? 239  LEU A O     1 
ATOM   1764 C CB    . LEU A 1 260 ? 7.159  35.007  33.351  1.00 28.89  ? 239  LEU A CB    1 
ATOM   1765 C CG    . LEU A 1 260 ? 6.044  33.977  33.181  1.00 27.96  ? 239  LEU A CG    1 
ATOM   1766 C CD1   . LEU A 1 260 ? 6.613  32.649  32.773  1.00 27.66  ? 239  LEU A CD1   1 
ATOM   1767 C CD2   . LEU A 1 260 ? 5.220  33.837  34.428  1.00 27.90  ? 239  LEU A CD2   1 
ATOM   1768 N N     . THR A 1 261 ? 8.320  37.849  34.871  1.00 25.74  ? 240  THR A N     1 
ATOM   1769 C CA    . THR A 1 261 ? 9.424  38.802  34.883  1.00 26.97  ? 240  THR A CA    1 
ATOM   1770 C C     . THR A 1 261 ? 10.684 38.077  35.310  1.00 24.56  ? 240  THR A C     1 
ATOM   1771 O O     . THR A 1 261 ? 10.643 37.162  36.129  1.00 24.95  ? 240  THR A O     1 
ATOM   1772 C CB    . THR A 1 261 ? 9.144  40.018  35.782  1.00 30.86  ? 240  THR A CB    1 
ATOM   1773 O OG1   . THR A 1 261 ? 8.854  39.510  37.082  1.00 30.36  ? 240  THR A OG1   1 
ATOM   1774 C CG2   . THR A 1 261 ? 7.989  40.859  35.270  1.00 30.80  ? 240  THR A CG2   1 
ATOM   1775 N N     . ALA A 1 262 ? 11.816 38.551  34.789  1.00 27.17  ? 241  ALA A N     1 
ATOM   1776 C CA    . ALA A 1 262 ? 13.123 38.057  35.181  1.00 26.71  ? 241  ALA A CA    1 
ATOM   1777 C C     . ALA A 1 262 ? 13.948 39.222  35.720  1.00 30.44  ? 241  ALA A C     1 
ATOM   1778 O O     . ALA A 1 262 ? 14.168 40.194  35.012  1.00 32.66  ? 241  ALA A O     1 
ATOM   1779 C CB    . ALA A 1 262 ? 13.837 37.450  34.003  1.00 27.52  ? 241  ALA A CB    1 
ATOM   1780 N N     . ARG A 1 263 ? 14.413 39.115  36.958  1.00 31.07  ? 242  ARG A N     1 
ATOM   1781 C CA    . ARG A 1 263 ? 15.231 40.169  37.537  1.00 32.94  ? 242  ARG A CA    1 
ATOM   1782 C C     . ARG A 1 263 ? 16.646 40.051  37.002  1.00 32.20  ? 242  ARG A C     1 
ATOM   1783 O O     . ARG A 1 263 ? 17.380 41.030  36.980  1.00 33.08  ? 242  ARG A O     1 
ATOM   1784 C CB    . ARG A 1 263 ? 15.389 40.041  39.056  1.00 41.11  ? 242  ARG A CB    1 
ATOM   1785 C CG    . ARG A 1 263 ? 14.171 40.360  39.908  1.00 45.87  ? 242  ARG A CG    1 
ATOM   1786 C CD    . ARG A 1 263 ? 14.476 40.026  41.368  1.00 49.24  ? 242  ARG A CD    1 
ATOM   1787 N NE    . ARG A 1 263 ? 13.208 39.590  41.958  1.00 59.89  ? 242  ARG A NE    1 
ATOM   1788 C CZ    . ARG A 1 263 ? 12.803 38.334  42.161  1.00 61.71  ? 242  ARG A CZ    1 
ATOM   1789 N NH1   . ARG A 1 263 ? 13.588 37.304  41.922  1.00 65.17  ? 242  ARG A NH1   1 
ATOM   1790 N NH2   . ARG A 1 263 ? 11.591 38.112  42.619  1.00 60.17  ? 242  ARG A NH2   1 
ATOM   1791 N N     . ARG A 1 264 ? 17.056 38.843  36.587  1.00 30.28  ? 243  ARG A N     1 
ATOM   1792 C CA    . ARG A 1 264 ? 18.426 38.687  36.134  1.00 28.95  ? 243  ARG A CA    1 
ATOM   1793 C C     . ARG A 1 264 ? 18.508 38.453  34.635  1.00 27.77  ? 243  ARG A C     1 
ATOM   1794 O O     . ARG A 1 264 ? 19.069 39.298  33.951  1.00 26.43  ? 243  ARG A O     1 
ATOM   1795 C CB    . ARG A 1 264 ? 19.181 37.592  36.870  1.00 31.71  ? 243  ARG A CB    1 
ATOM   1796 C CG    . ARG A 1 264 ? 19.163 37.853  38.359  1.00 34.75  ? 243  ARG A CG    1 
ATOM   1797 C CD    . ARG A 1 264 ? 20.053 36.848  38.976  1.00 35.14  ? 243  ARG A CD    1 
ATOM   1798 N NE    . ARG A 1 264 ? 20.031 37.041  40.426  1.00 38.30  ? 243  ARG A NE    1 
ATOM   1799 C CZ    . ARG A 1 264 ? 20.888 36.479  41.253  1.00 38.92  ? 243  ARG A CZ    1 
ATOM   1800 N NH1   . ARG A 1 264 ? 21.928 35.827  40.800  1.00 42.28  ? 243  ARG A NH1   1 
ATOM   1801 N NH2   . ARG A 1 264 ? 20.715 36.597  42.545  1.00 46.18  ? 243  ARG A NH2   1 
ATOM   1802 N N     . GLU A 1 265 ? 18.042 37.290  34.138  1.00 26.74  ? 244  GLU A N     1 
ATOM   1803 C CA    . GLU A 1 265 ? 18.163 37.001  32.711  1.00 25.23  ? 244  GLU A CA    1 
ATOM   1804 C C     . GLU A 1 265 ? 17.014 36.143  32.179  1.00 22.65  ? 244  GLU A C     1 
ATOM   1805 O O     . GLU A 1 265 ? 16.422 35.329  32.897  1.00 22.98  ? 244  GLU A O     1 
ATOM   1806 C CB    . GLU A 1 265 ? 19.478 36.301  32.413  1.00 28.04  ? 244  GLU A CB    1 
ATOM   1807 C CG    . GLU A 1 265 ? 20.673 37.098  32.907  1.00 31.63  ? 244  GLU A CG    1 
ATOM   1808 C CD    . GLU A 1 265 ? 21.942 36.717  32.199  1.00 34.53  ? 244  GLU A CD    1 
ATOM   1809 O OE1   . GLU A 1 265 ? 22.893 36.311  32.896  1.00 30.09  ? 244  GLU A OE1   1 
ATOM   1810 O OE2   . GLU A 1 265 ? 21.929 36.798  30.941  1.00 32.16  ? 244  GLU A OE2   1 
ATOM   1811 N N     . VAL A 1 266 ? 16.670 36.413  30.919  1.00 21.45  ? 245  VAL A N     1 
ATOM   1812 C CA    . VAL A 1 266 ? 15.839 35.534  30.110  1.00 23.02  ? 245  VAL A CA    1 
ATOM   1813 C C     . VAL A 1 266 ? 16.784 34.713  29.242  1.00 22.79  ? 245  VAL A C     1 
ATOM   1814 O O     . VAL A 1 266 ? 17.744 35.268  28.676  1.00 21.69  ? 245  VAL A O     1 
ATOM   1815 C CB    . VAL A 1 266 ? 14.864 36.335  29.233  1.00 22.27  ? 245  VAL A CB    1 
ATOM   1816 C CG1   . VAL A 1 266 ? 14.137 35.446  28.231  1.00 21.69  ? 245  VAL A CG1   1 
ATOM   1817 C CG2   . VAL A 1 266 ? 13.897 37.188  30.062  1.00 23.62  ? 245  VAL A CG2   1 
ATOM   1818 N N     . VAL A 1 267 ? 16.523 33.401  29.189  1.00 19.22  ? 246  VAL A N     1 
ATOM   1819 C CA    . VAL A 1 267 ? 17.322 32.479  28.406  1.00 18.46  ? 246  VAL A CA    1 
ATOM   1820 C C     . VAL A 1 267 ? 16.361 31.766  27.465  1.00 18.13  ? 246  VAL A C     1 
ATOM   1821 O O     . VAL A 1 267 ? 15.372 31.153  27.906  1.00 18.62  ? 246  VAL A O     1 
ATOM   1822 C CB    . VAL A 1 267 ? 18.133 31.477  29.251  1.00 20.00  ? 246  VAL A CB    1 
ATOM   1823 C CG1   . VAL A 1 267 ? 18.971 30.529  28.400  1.00 21.47  ? 246  VAL A CG1   1 
ATOM   1824 C CG2   . VAL A 1 267 ? 19.014 32.191  30.262  1.00 22.45  ? 246  VAL A CG2   1 
ATOM   1825 N N     . LEU A 1 268 ? 16.584 31.934  26.167  1.00 17.56  ? 247  LEU A N     1 
ATOM   1826 C CA    . LEU A 1 268 ? 15.795 31.215  25.171  1.00 18.72  ? 247  LEU A CA    1 
ATOM   1827 C C     . LEU A 1 268 ? 16.454 29.863  24.913  1.00 16.23  ? 247  LEU A C     1 
ATOM   1828 O O     . LEU A 1 268 ? 17.607 29.793  24.492  1.00 17.80  ? 247  LEU A O     1 
ATOM   1829 C CB    . LEU A 1 268 ? 15.662 32.050  23.896  1.00 20.15  ? 247  LEU A CB    1 
ATOM   1830 C CG    . LEU A 1 268 ? 14.974 33.410  24.059  1.00 19.70  ? 247  LEU A CG    1 
ATOM   1831 C CD1   . LEU A 1 268 ? 14.931 34.114  22.717  1.00 22.60  ? 247  LEU A CD1   1 
ATOM   1832 C CD2   . LEU A 1 268 ? 13.561 33.303  24.635  1.00 20.04  ? 247  LEU A CD2   1 
ATOM   1833 N N     . SER A 1 269 ? 15.699 28.796  25.178  1.00 16.66  ? 248  SER A N     1 
ATOM   1834 C CA    . SER A 1 269 ? 16.117 27.437  24.881  1.00 16.44  ? 248  SER A CA    1 
ATOM   1835 C C     . SER A 1 269 ? 15.019 26.760  24.054  1.00 16.26  ? 248  SER A C     1 
ATOM   1836 O O     . SER A 1 269 ? 14.734 25.567  24.206  1.00 18.10  ? 248  SER A O     1 
ATOM   1837 C CB    . SER A 1 269 ? 16.433 26.680  26.152  1.00 19.74  ? 248  SER A CB    1 
ATOM   1838 O OG    . SER A 1 269 ? 17.488 27.283  26.909  1.00 19.16  ? 248  SER A OG    1 
ATOM   1839 N N     . ALA A 1 270 ? 14.452 27.528  23.122  1.00 15.09  ? 249  ALA A N     1 
ATOM   1840 C CA    . ALA A 1 270 ? 13.279 27.118  22.376  1.00 15.61  ? 249  ALA A CA    1 
ATOM   1841 C C     . ALA A 1 270 ? 13.658 26.409  21.073  1.00 16.45  ? 249  ALA A C     1 
ATOM   1842 O O     . ALA A 1 270 ? 12.788 25.989  20.307  1.00 18.89  ? 249  ALA A O     1 
ATOM   1843 C CB    . ALA A 1 270 ? 12.405 28.336  22.164  1.00 15.58  ? 249  ALA A CB    1 
ATOM   1844 N N     . GLY A 1 271 ? 14.966 26.227  20.858  1.00 16.74  ? 250  GLY A N     1 
ATOM   1845 C CA    . GLY A 1 271 ? 15.512 25.448  19.761  1.00 17.36  ? 250  GLY A CA    1 
ATOM   1846 C C     . GLY A 1 271 ? 15.634 26.270  18.479  1.00 17.23  ? 250  GLY A C     1 
ATOM   1847 O O     . GLY A 1 271 ? 15.315 27.451  18.445  1.00 19.06  ? 250  GLY A O     1 
ATOM   1848 N N     . THR A 1 272 ? 16.106 25.610  17.430  1.00 16.72  ? 251  THR A N     1 
ATOM   1849 C CA    . THR A 1 272 ? 16.503 26.232  16.179  1.00 17.96  ? 251  THR A CA    1 
ATOM   1850 C C     . THR A 1 272 ? 15.325 26.974  15.541  1.00 17.86  ? 251  THR A C     1 
ATOM   1851 O O     . THR A 1 272 ? 15.496 28.009  14.903  1.00 17.21  ? 251  THR A O     1 
ATOM   1852 C CB    . THR A 1 272 ? 17.065 25.141  15.259  1.00 17.94  ? 251  THR A CB    1 
ATOM   1853 O OG1   . THR A 1 272 ? 18.282 24.710  15.869  1.00 16.94  ? 251  THR A OG1   1 
ATOM   1854 C CG2   . THR A 1 272 ? 17.370 25.683  13.877  1.00 17.86  ? 251  THR A CG2   1 
ATOM   1855 N N     . VAL A 1 273 ? 14.112 26.444  15.691  1.00 17.33  ? 252  VAL A N     1 
ATOM   1856 C CA    . VAL A 1 273 ? 12.946 27.155  15.221  1.00 17.14  ? 252  VAL A CA    1 
ATOM   1857 C C     . VAL A 1 273 ? 12.512 28.224  16.219  1.00 19.08  ? 252  VAL A C     1 
ATOM   1858 O O     . VAL A 1 273 ? 12.390 29.406  15.863  1.00 17.86  ? 252  VAL A O     1 
ATOM   1859 C CB    . VAL A 1 273 ? 11.775 26.220  14.874  1.00 17.93  ? 252  VAL A CB    1 
ATOM   1860 C CG1   . VAL A 1 273 ? 10.597 27.011  14.337  1.00 18.24  ? 252  VAL A CG1   1 
ATOM   1861 C CG2   . VAL A 1 273 ? 12.181 25.152  13.863  1.00 19.67  ? 252  VAL A CG2   1 
ATOM   1862 N N     . GLY A 1 274 ? 12.159 27.781  17.427  1.00 17.39  ? 253  GLY A N     1 
ATOM   1863 C CA    . GLY A 1 274 ? 11.471 28.639  18.375  1.00 18.05  ? 253  GLY A CA    1 
ATOM   1864 C C     . GLY A 1 274 ? 12.335 29.801  18.861  1.00 17.44  ? 253  GLY A C     1 
ATOM   1865 O O     . GLY A 1 274 ? 11.817 30.899  19.074  1.00 18.79  ? 253  GLY A O     1 
ATOM   1866 N N     . SER A 1 275 ? 13.640 29.583  19.056  1.00 17.69  ? 254  SER A N     1 
ATOM   1867 C CA    . SER A 1 275 ? 14.481 30.673  19.550  1.00 18.01  ? 254  SER A CA    1 
ATOM   1868 C C     . SER A 1 275 ? 14.552 31.805  18.535  1.00 20.04  ? 254  SER A C     1 
ATOM   1869 O O     . SER A 1 275 ? 14.447 32.991  18.897  1.00 19.98  ? 254  SER A O     1 
ATOM   1870 C CB    . SER A 1 275 ? 15.852 30.213  19.978  1.00 17.80  ? 254  SER A CB    1 
ATOM   1871 O OG    . SER A 1 275 ? 15.730 29.496  21.217  1.00 17.00  ? 254  SER A OG    1 
ATOM   1872 N N     . ALA A 1 276 ? 14.719 31.442  17.266  1.00 18.11  ? 255  ALA A N     1 
ATOM   1873 C CA    . ALA A 1 276 ? 14.830 32.438  16.216  1.00 19.31  ? 255  ALA A CA    1 
ATOM   1874 C C     . ALA A 1 276 ? 13.491 33.138  16.042  1.00 17.90  ? 255  ALA A C     1 
ATOM   1875 O O     . ALA A 1 276 ? 13.446 34.355  15.907  1.00 18.78  ? 255  ALA A O     1 
ATOM   1876 C CB    . ALA A 1 276 ? 15.302 31.810  14.925  1.00 19.59  ? 255  ALA A CB    1 
ATOM   1877 N N     . GLN A 1 277 ? 12.394 32.387  16.133  1.00 17.29  ? 256  GLN A N     1 
ATOM   1878 C CA    . GLN A 1 277 ? 11.090 32.985  15.920  1.00 18.53  ? 256  GLN A CA    1 
ATOM   1879 C C     . GLN A 1 277 ? 10.782 33.973  17.048  1.00 19.30  ? 256  GLN A C     1 
ATOM   1880 O O     . GLN A 1 277 ? 10.268 35.066  16.802  1.00 17.30  ? 256  GLN A O     1 
ATOM   1881 C CB    . GLN A 1 277 ? 9.995  31.930  15.771  1.00 20.11  ? 256  GLN A CB    1 
ATOM   1882 C CG    . GLN A 1 277 ? 8.631  32.553  15.557  1.00 21.29  ? 256  GLN A CG    1 
ATOM   1883 C CD    . GLN A 1 277 ? 7.479  31.589  15.397  1.00 23.62  ? 256  GLN A CD    1 
ATOM   1884 O OE1   . GLN A 1 277 ? 7.481  30.422  15.807  1.00 27.45  ? 256  GLN A OE1   1 
ATOM   1885 N NE2   . GLN A 1 277 ? 6.443  32.138  14.811  1.00 23.13  ? 256  GLN A NE2   1 
ATOM   1886 N N     . LEU A 1 278 ? 11.152 33.607  18.280  1.00 20.56  ? 257  LEU A N     1 
ATOM   1887 C CA    . LEU A 1 278 ? 10.904 34.466  19.425  1.00 19.13  ? 257  LEU A CA    1 
ATOM   1888 C C     . LEU A 1 278 ? 11.740 35.733  19.330  1.00 20.67  ? 257  LEU A C     1 
ATOM   1889 O O     . LEU A 1 278 ? 11.256 36.810  19.699  1.00 21.68  ? 257  LEU A O     1 
ATOM   1890 C CB    . LEU A 1 278 ? 11.147 33.751  20.738  1.00 19.72  ? 257  LEU A CB    1 
ATOM   1891 C CG    . LEU A 1 278 ? 10.048 32.758  21.140  1.00 22.21  ? 257  LEU A CG    1 
ATOM   1892 C CD1   . LEU A 1 278 ? 10.450 31.886  22.334  1.00 25.31  ? 257  LEU A CD1   1 
ATOM   1893 C CD2   . LEU A 1 278 ? 8.758  33.515  21.443  1.00 23.05  ? 257  LEU A CD2   1 
ATOM   1894 N N     . LEU A 1 279 ? 12.987 35.625  18.873  1.00 17.84  ? 258  LEU A N     1 
ATOM   1895 C CA    . LEU A 1 279 ? 13.772 36.843  18.704  1.00 20.94  ? 258  LEU A CA    1 
ATOM   1896 C C     . LEU A 1 279 ? 13.072 37.812  17.741  1.00 19.08  ? 258  LEU A C     1 
ATOM   1897 O O     . LEU A 1 279 ? 12.910 39.000  18.066  1.00 18.72  ? 258  LEU A O     1 
ATOM   1898 C CB    . LEU A 1 279 ? 15.218 36.561  18.296  1.00 19.90  ? 258  LEU A CB    1 
ATOM   1899 C CG    . LEU A 1 279 ? 16.086 35.933  19.386  1.00 20.02  ? 258  LEU A CG    1 
ATOM   1900 C CD1   . LEU A 1 279 ? 17.449 35.672  18.818  1.00 22.13  ? 258  LEU A CD1   1 
ATOM   1901 C CD2   . LEU A 1 279 ? 16.175 36.822  20.660  1.00 19.10  ? 258  LEU A CD2   1 
ATOM   1902 N N     . MET A 1 280 ? 12.682 37.303  16.563  1.00 17.18  ? 259  MET A N     1 
ATOM   1903 C CA    . MET A 1 280 ? 12.051 38.119  15.538  1.00 19.79  ? 259  MET A CA    1 
ATOM   1904 C C     . MET A 1 280 ? 10.735 38.719  16.049  1.00 20.22  ? 259  MET A C     1 
ATOM   1905 O O     . MET A 1 280 ? 10.454 39.905  15.852  1.00 19.37  ? 259  MET A O     1 
ATOM   1906 C CB    . MET A 1 280 ? 11.828 37.286  14.268  1.00 20.36  ? 259  MET A CB    1 
ATOM   1907 C CG    . MET A 1 280 ? 13.146 36.861  13.678  1.00 22.64  ? 259  MET A CG    1 
ATOM   1908 S SD    . MET A 1 280 ? 13.007 36.054  12.073  1.00 26.17  ? 259  MET A SD    1 
ATOM   1909 C CE    . MET A 1 280 ? 12.351 34.452  12.535  1.00 27.32  ? 259  MET A CE    1 
ATOM   1910 N N     . LEU A 1 281 ? 9.955  37.925  16.778  1.00 21.08  ? 260  LEU A N     1 
ATOM   1911 C CA    . LEU A 1 281 ? 8.692  38.417  17.313  1.00 21.65  ? 260  LEU A CA    1 
ATOM   1912 C C     . LEU A 1 281 ? 8.930  39.518  18.346  1.00 23.19  ? 260  LEU A C     1 
ATOM   1913 O O     . LEU A 1 281 ? 8.055  40.329  18.578  1.00 21.66  ? 260  LEU A O     1 
ATOM   1914 C CB    . LEU A 1 281 ? 7.866  37.291  17.911  1.00 20.31  ? 260  LEU A CB    1 
ATOM   1915 C CG    . LEU A 1 281 ? 7.218  36.330  16.919  1.00 22.65  ? 260  LEU A CG    1 
ATOM   1916 C CD1   . LEU A 1 281 ? 6.768  35.049  17.630  1.00 21.48  ? 260  LEU A CD1   1 
ATOM   1917 C CD2   . LEU A 1 281 ? 6.044  36.969  16.222  1.00 21.77  ? 260  LEU A CD2   1 
ATOM   1918 N N     . SER A 1 282 ? 10.123 39.574  18.934  1.00 21.44  ? 261  SER A N     1 
ATOM   1919 C CA    . SER A 1 282 ? 10.459 40.548  19.953  1.00 22.69  ? 261  SER A CA    1 
ATOM   1920 C C     . SER A 1 282 ? 11.042 41.816  19.330  1.00 22.89  ? 261  SER A C     1 
ATOM   1921 O O     . SER A 1 282 ? 11.443 42.743  20.041  1.00 23.58  ? 261  SER A O     1 
ATOM   1922 C CB    . SER A 1 282 ? 11.451 39.902  20.929  1.00 22.17  ? 261  SER A CB    1 
ATOM   1923 O OG    . SER A 1 282 ? 10.868 38.768  21.569  1.00 23.23  ? 261  SER A OG    1 
ATOM   1924 N N     . GLY A 1 283 ? 11.144 41.824  17.991  1.00 22.42  ? 262  GLY A N     1 
ATOM   1925 C CA    . GLY A 1 283 ? 11.762 42.908  17.242  1.00 21.16  ? 262  GLY A CA    1 
ATOM   1926 C C     . GLY A 1 283 ? 13.283 42.799  17.121  1.00 21.19  ? 262  GLY A C     1 
ATOM   1927 O O     . GLY A 1 283 ? 13.930 43.780  16.751  1.00 20.64  ? 262  GLY A O     1 
ATOM   1928 N N     . ILE A 1 284 ? 13.861 41.626  17.433  1.00 18.57  ? 263  ILE A N     1 
ATOM   1929 C CA    . ILE A 1 284 ? 15.296 41.413  17.393  1.00 18.25  ? 263  ILE A CA    1 
ATOM   1930 C C     . ILE A 1 284 ? 15.601 40.636  16.115  1.00 21.37  ? 263  ILE A C     1 
ATOM   1931 O O     . ILE A 1 284 ? 15.146 39.500  15.955  1.00 20.33  ? 263  ILE A O     1 
ATOM   1932 C CB    . ILE A 1 284 ? 15.809 40.672  18.637  1.00 18.27  ? 263  ILE A CB    1 
ATOM   1933 C CG1   . ILE A 1 284 ? 15.450 41.454  19.919  1.00 20.16  ? 263  ILE A CG1   1 
ATOM   1934 C CG2   . ILE A 1 284 ? 17.303 40.419  18.517  1.00 19.30  ? 263  ILE A CG2   1 
ATOM   1935 C CD1   . ILE A 1 284 ? 15.635 40.695  21.218  1.00 19.27  ? 263  ILE A CD1   1 
ATOM   1936 N N     . GLY A 1 285 ? 16.329 41.283  15.185  1.00 21.79  ? 264  GLY A N     1 
ATOM   1937 C CA    . GLY A 1 285 ? 16.537 40.703  13.859  1.00 21.39  ? 264  GLY A CA    1 
ATOM   1938 C C     . GLY A 1 285 ? 16.779 41.774  12.801  1.00 20.51  ? 264  GLY A C     1 
ATOM   1939 O O     . GLY A 1 285 ? 17.136 42.904  13.119  1.00 19.59  ? 264  GLY A O     1 
ATOM   1940 N N     . ASP A 1 286 ? 16.530 41.424  11.542  1.00 20.69  ? 265  ASP A N     1 
ATOM   1941 C CA    . ASP A 1 286 ? 16.754 42.371  10.467  1.00 25.04  ? 265  ASP A CA    1 
ATOM   1942 C C     . ASP A 1 286 ? 15.539 43.293  10.340  1.00 23.87  ? 265  ASP A C     1 
ATOM   1943 O O     . ASP A 1 286 ? 14.448 42.866  9.926   1.00 23.05  ? 265  ASP A O     1 
ATOM   1944 C CB    . ASP A 1 286 ? 17.075 41.631  9.181   1.00 26.23  ? 265  ASP A CB    1 
ATOM   1945 C CG    . ASP A 1 286 ? 17.376 42.585  8.034   1.00 30.32  ? 265  ASP A CG    1 
ATOM   1946 O OD1   . ASP A 1 286 ? 18.120 43.559  8.279   1.00 26.04  ? 265  ASP A OD1   1 
ATOM   1947 O OD2   . ASP A 1 286 ? 16.837 42.353  6.939   1.00 33.80  ? 265  ASP A OD2   1 
ATOM   1948 N N     . GLY A 1 287 ? 15.742 44.568  10.668  1.00 22.65  ? 266  GLY A N     1 
ATOM   1949 C CA    . GLY A 1 287 ? 14.651 45.517  10.825  1.00 22.19  ? 266  GLY A CA    1 
ATOM   1950 C C     . GLY A 1 287 ? 13.706 45.544  9.630   1.00 21.85  ? 266  GLY A C     1 
ATOM   1951 O O     . GLY A 1 287 ? 12.486 45.396  9.795   1.00 20.70  ? 266  GLY A O     1 
ATOM   1952 N N     . PRO A 1 288 ? 14.238 45.650  8.391   1.00 23.06  ? 267  PRO A N     1 
ATOM   1953 C CA    . PRO A 1 288 ? 13.399 45.691  7.192   1.00 24.28  ? 267  PRO A CA    1 
ATOM   1954 C C     . PRO A 1 288 ? 12.508 44.465  7.017   1.00 21.17  ? 267  PRO A C     1 
ATOM   1955 O O     . PRO A 1 288 ? 11.361 44.563  6.591   1.00 22.09  ? 267  PRO A O     1 
ATOM   1956 C CB    . PRO A 1 288 ? 14.419 45.802  6.033   1.00 22.84  ? 267  PRO A CB    1 
ATOM   1957 C CG    . PRO A 1 288 ? 15.638 46.357  6.659   1.00 25.59  ? 267  PRO A CG    1 
ATOM   1958 C CD    . PRO A 1 288 ? 15.664 45.818  8.083   1.00 25.74  ? 267  PRO A CD    1 
ATOM   1959 N N     . GLN A 1 289 ? 13.053 43.290  7.324   1.00 20.97  ? 268  GLN A N     1 
ATOM   1960 C CA    . GLN A 1 289 ? 12.265 42.064  7.198   1.00 24.28  ? 268  GLN A CA    1 
ATOM   1961 C C     . GLN A 1 289 ? 11.183 42.007  8.267   1.00 21.19  ? 268  GLN A C     1 
ATOM   1962 O O     . GLN A 1 289 ? 10.057 41.595  7.991   1.00 23.00  ? 268  GLN A O     1 
ATOM   1963 C CB    . GLN A 1 289 ? 13.135 40.821  7.295   1.00 24.68  ? 268  GLN A CB    1 
ATOM   1964 C CG    . GLN A 1 289 ? 14.100 40.774  6.135   1.00 29.17  ? 268  GLN A CG    1 
ATOM   1965 C CD    . GLN A 1 289 ? 14.886 39.487  6.082   1.00 36.27  ? 268  GLN A CD    1 
ATOM   1966 O OE1   . GLN A 1 289 ? 14.316 38.397  6.114   1.00 36.64  ? 268  GLN A OE1   1 
ATOM   1967 N NE2   . GLN A 1 289 ? 16.198 39.622  6.029   1.00 43.82  ? 268  GLN A NE2   1 
ATOM   1968 N N     . LEU A 1 290 ? 11.538 42.385  9.495   1.00 21.78  ? 269  LEU A N     1 
ATOM   1969 C CA    . LEU A 1 290 ? 10.556 42.431  10.567  1.00 22.54  ? 269  LEU A CA    1 
ATOM   1970 C C     . LEU A 1 290 ? 9.443  43.424  10.239  1.00 23.02  ? 269  LEU A C     1 
ATOM   1971 O O     . LEU A 1 290 ? 8.260  43.137  10.443  1.00 21.94  ? 269  LEU A O     1 
ATOM   1972 C CB    . LEU A 1 290 ? 11.268 42.770  11.870  1.00 23.42  ? 269  LEU A CB    1 
ATOM   1973 C CG    . LEU A 1 290 ? 12.292 41.735  12.335  1.00 25.01  ? 269  LEU A CG    1 
ATOM   1974 C CD1   . LEU A 1 290 ? 12.713 42.102  13.720  1.00 26.51  ? 269  LEU A CD1   1 
ATOM   1975 C CD2   . LEU A 1 290 ? 11.781 40.324  12.278  1.00 26.75  ? 269  LEU A CD2   1 
ATOM   1976 N N     . ARG A 1 291 ? 9.816  44.589  9.685   1.00 24.21  ? 270  ARG A N     1 
ATOM   1977 C CA    . ARG A 1 291 ? 8.825  45.582  9.297   1.00 26.21  ? 270  ARG A CA    1 
ATOM   1978 C C     . ARG A 1 291 ? 7.879  44.953  8.280   1.00 23.48  ? 270  ARG A C     1 
ATOM   1979 O O     . ARG A 1 291 ? 6.679  45.124  8.368   1.00 25.22  ? 270  ARG A O     1 
ATOM   1980 C CB    . ARG A 1 291 ? 9.403  46.874  8.697   1.00 27.49  ? 270  ARG A CB    1 
ATOM   1981 C CG    . ARG A 1 291 ? 10.080 47.822  9.669   1.00 32.50  ? 270  ARG A CG    1 
ATOM   1982 C CD    . ARG A 1 291 ? 10.671 49.056  8.971   1.00 34.97  ? 270  ARG A CD    1 
ATOM   1983 N NE    . ARG A 1 291 ? 11.732 49.714  9.744   1.00 36.24  ? 270  ARG A NE    1 
ATOM   1984 C CZ    . ARG A 1 291 ? 11.555 50.524  10.779  1.00 42.24  ? 270  ARG A CZ    1 
ATOM   1985 N NH1   . ARG A 1 291 ? 10.331 50.883  11.169  1.00 45.14  ? 270  ARG A NH1   1 
ATOM   1986 N NH2   . ARG A 1 291 ? 12.624 50.966  11.416  1.00 40.98  ? 270  ARG A NH2   1 
ATOM   1987 N N     . ALA A 1 292 ? 8.423  44.236  7.305   1.00 26.97  ? 271  ALA A N     1 
ATOM   1988 C CA    . ALA A 1 292 ? 7.604  43.600  6.294   1.00 26.55  ? 271  ALA A CA    1 
ATOM   1989 C C     . ALA A 1 292 ? 6.702  42.522  6.888   1.00 28.42  ? 271  ALA A C     1 
ATOM   1990 O O     . ALA A 1 292 ? 5.664  42.277  6.312   1.00 29.76  ? 271  ALA A O     1 
ATOM   1991 C CB    . ALA A 1 292 ? 8.470  43.023  5.195   1.00 28.97  ? 271  ALA A CB    1 
ATOM   1992 N N     . ALA A 1 293 ? 7.067  41.892  8.014   1.00 26.45  ? 272  ALA A N     1 
ATOM   1993 C CA    . ALA A 1 293 ? 6.221  40.885  8.657   1.00 25.80  ? 272  ALA A CA    1 
ATOM   1994 C C     . ALA A 1 293 ? 5.228  41.493  9.640   1.00 27.36  ? 272  ALA A C     1 
ATOM   1995 O O     . ALA A 1 293 ? 4.493  40.768  10.325  1.00 29.49  ? 272  ALA A O     1 
ATOM   1996 C CB    . ALA A 1 293 ? 7.071  39.883  9.391   1.00 26.07  ? 272  ALA A CB    1 
ATOM   1997 N N     . GLY A 1 294 ? 5.231  42.821  9.741   1.00 26.94  ? 273  GLY A N     1 
ATOM   1998 C CA    . GLY A 1 294 ? 4.324  43.502  10.630  1.00 25.59  ? 273  GLY A CA    1 
ATOM   1999 C C     . GLY A 1 294 ? 4.837  43.623  12.064  1.00 25.04  ? 273  GLY A C     1 
ATOM   2000 O O     . GLY A 1 294 ? 4.040  43.889  12.956  1.00 26.65  ? 273  GLY A O     1 
ATOM   2001 N N     . VAL A 1 295 ? 6.140  43.474  12.302  1.00 22.73  ? 274  VAL A N     1 
ATOM   2002 C CA    . VAL A 1 295 ? 6.693  43.583  13.638  1.00 24.23  ? 274  VAL A CA    1 
ATOM   2003 C C     . VAL A 1 295 ? 7.537  44.847  13.731  1.00 25.97  ? 274  VAL A C     1 
ATOM   2004 O O     . VAL A 1 295 ? 8.331  45.106  12.841  1.00 28.22  ? 274  VAL A O     1 
ATOM   2005 C CB    . VAL A 1 295 ? 7.558  42.347  13.944  1.00 23.02  ? 274  VAL A CB    1 
ATOM   2006 C CG1   . VAL A 1 295 ? 8.294  42.470  15.276  1.00 22.99  ? 274  VAL A CG1   1 
ATOM   2007 C CG2   . VAL A 1 295 ? 6.730  41.078  13.885  1.00 26.76  ? 274  VAL A CG2   1 
ATOM   2008 N N     . GLU A 1 296 ? 7.442  45.562  14.853  1.00 25.87  ? 275  GLU A N     1 
ATOM   2009 C CA    . GLU A 1 296 ? 8.227  46.761  15.097  1.00 27.27  ? 275  GLU A CA    1 
ATOM   2010 C C     . GLU A 1 296 ? 9.677  46.389  15.415  1.00 27.10  ? 275  GLU A C     1 
ATOM   2011 O O     . GLU A 1 296 ? 9.957  45.676  16.360  1.00 27.33  ? 275  GLU A O     1 
ATOM   2012 C CB    . GLU A 1 296 ? 7.544  47.511  16.255  1.00 32.22  ? 275  GLU A CB    1 
ATOM   2013 C CG    . GLU A 1 296 ? 8.171  48.849  16.644  1.00 39.23  ? 275  GLU A CG    1 
ATOM   2014 C CD    . GLU A 1 296 ? 8.072  49.922  15.575  1.00 51.34  ? 275  GLU A CD    1 
ATOM   2015 O OE1   . GLU A 1 296 ? 9.015  50.742  15.467  1.00 65.88  ? 275  GLU A OE1   1 
ATOM   2016 O OE2   . GLU A 1 296 ? 7.057  49.931  14.831  1.00 59.31  ? 275  GLU A OE2   1 
ATOM   2017 N N     . PRO A 1 297 ? 10.673 46.861  14.637  1.00 28.64  ? 276  PRO A N     1 
ATOM   2018 C CA    . PRO A 1 297 ? 12.072 46.582  14.941  1.00 25.16  ? 276  PRO A CA    1 
ATOM   2019 C C     . PRO A 1 297 ? 12.479 47.209  16.262  1.00 28.60  ? 276  PRO A C     1 
ATOM   2020 O O     . PRO A 1 297 ? 12.090 48.336  16.566  1.00 27.27  ? 276  PRO A O     1 
ATOM   2021 C CB    . PRO A 1 297 ? 12.833 47.215  13.772  1.00 27.22  ? 276  PRO A CB    1 
ATOM   2022 C CG    . PRO A 1 297 ? 11.820 47.318  12.676  1.00 27.09  ? 276  PRO A CG    1 
ATOM   2023 C CD    . PRO A 1 297 ? 10.500 47.575  13.362  1.00 28.01  ? 276  PRO A CD    1 
ATOM   2024 N N     . ARG A 1 298 ? 13.282 46.484  17.046  1.00 24.94  ? 277  ARG A N     1 
ATOM   2025 C CA    . ARG A 1 298 ? 13.793 47.020  18.300  1.00 25.10  ? 277  ARG A CA    1 
ATOM   2026 C C     . ARG A 1 298 ? 15.312 46.938  18.325  1.00 26.76  ? 277  ARG A C     1 
ATOM   2027 O O     . ARG A 1 298 ? 15.958 47.854  18.802  1.00 25.56  ? 277  ARG A O     1 
ATOM   2028 C CB    . ARG A 1 298 ? 13.120 46.294  19.474  1.00 28.77  ? 277  ARG A CB    1 
ATOM   2029 C CG    . ARG A 1 298 ? 11.625 46.554  19.367  1.00 32.80  ? 277  ARG A CG    1 
ATOM   2030 C CD    . ARG A 1 298 ? 10.921 46.792  20.656  1.00 47.64  ? 277  ARG A CD    1 
ATOM   2031 N NE    . ARG A 1 298 ? 11.556 47.812  21.509  1.00 50.08  ? 277  ARG A NE    1 
ATOM   2032 C CZ    . ARG A 1 298 ? 11.308 47.823  22.818  1.00 53.75  ? 277  ARG A CZ    1 
ATOM   2033 N NH1   . ARG A 1 298 ? 12.029 48.544  23.665  1.00 50.49  ? 277  ARG A NH1   1 
ATOM   2034 N NH2   . ARG A 1 298 ? 10.364 47.018  23.273  1.00 56.12  ? 277  ARG A NH2   1 
ATOM   2035 N N     . VAL A 1 299 ? 15.877 45.832  17.825  1.00 24.42  ? 278  VAL A N     1 
ATOM   2036 C CA    . VAL A 1 299 ? 17.311 45.637  17.823  1.00 24.84  ? 278  VAL A CA    1 
ATOM   2037 C C     . VAL A 1 299 ? 17.719 45.075  16.463  1.00 25.55  ? 278  VAL A C     1 
ATOM   2038 O O     . VAL A 1 299 ? 17.262 44.016  16.060  1.00 22.46  ? 278  VAL A O     1 
ATOM   2039 C CB    . VAL A 1 299 ? 17.746 44.699  18.965  1.00 27.21  ? 278  VAL A CB    1 
ATOM   2040 C CG1   . VAL A 1 299 ? 19.227 44.371  18.903  1.00 27.88  ? 278  VAL A CG1   1 
ATOM   2041 C CG2   . VAL A 1 299 ? 17.380 45.250  20.342  1.00 29.10  ? 278  VAL A CG2   1 
ATOM   2042 N N     . GLN A 1 300 ? 18.589 45.811  15.766  1.00 24.21  ? 279  GLN A N     1 
ATOM   2043 C CA    . GLN A 1 300 ? 19.110 45.379  14.487  1.00 24.48  ? 279  GLN A CA    1 
ATOM   2044 C C     . GLN A 1 300 ? 20.127 44.262  14.712  1.00 22.36  ? 279  GLN A C     1 
ATOM   2045 O O     . GLN A 1 300 ? 21.183 44.471  15.271  1.00 24.25  ? 279  GLN A O     1 
ATOM   2046 C CB    . GLN A 1 300 ? 19.699 46.606  13.784  1.00 25.41  ? 279  GLN A CB    1 
ATOM   2047 C CG    . GLN A 1 300 ? 20.309 46.284  12.439  1.00 23.81  ? 279  GLN A CG    1 
ATOM   2048 C CD    . GLN A 1 300 ? 19.325 45.681  11.471  1.00 20.83  ? 279  GLN A CD    1 
ATOM   2049 O OE1   . GLN A 1 300 ? 18.111 45.884  11.552  1.00 21.45  ? 279  GLN A OE1   1 
ATOM   2050 N NE2   . GLN A 1 300 ? 19.847 44.948  10.499  1.00 21.19  ? 279  GLN A NE2   1 
ATOM   2051 N N     . LEU A 1 301 ? 19.806 43.066  14.230  1.00 20.20  ? 280  LEU A N     1 
ATOM   2052 C CA    . LEU A 1 301 ? 20.640 41.900  14.447  1.00 20.55  ? 280  LEU A CA    1 
ATOM   2053 C C     . LEU A 1 301 ? 20.373 40.978  13.270  1.00 19.20  ? 280  LEU A C     1 
ATOM   2054 O O     . LEU A 1 301 ? 19.533 40.076  13.327  1.00 20.58  ? 280  LEU A O     1 
ATOM   2055 C CB    . LEU A 1 301 ? 20.308 41.270  15.811  1.00 21.79  ? 280  LEU A CB    1 
ATOM   2056 C CG    . LEU A 1 301 ? 21.291 40.220  16.329  1.00 22.89  ? 280  LEU A CG    1 
ATOM   2057 C CD1   . LEU A 1 301 ? 22.680 40.781  16.549  1.00 23.69  ? 280  LEU A CD1   1 
ATOM   2058 C CD2   . LEU A 1 301 ? 20.783 39.620  17.632  1.00 22.20  ? 280  LEU A CD2   1 
ATOM   2059 N N     . PRO A 1 302 ? 20.995 41.229  12.107  1.00 20.33  ? 281  PRO A N     1 
ATOM   2060 C CA    . PRO A 1 302 ? 20.480 40.611  10.888  1.00 22.07  ? 281  PRO A CA    1 
ATOM   2061 C C     . PRO A 1 302 ? 20.668 39.101  10.799  1.00 19.92  ? 281  PRO A C     1 
ATOM   2062 O O     . PRO A 1 302 ? 20.059 38.463  9.956   1.00 22.42  ? 281  PRO A O     1 
ATOM   2063 C CB    . PRO A 1 302 ? 21.242 41.373  9.776   1.00 22.56  ? 281  PRO A CB    1 
ATOM   2064 C CG    . PRO A 1 302 ? 22.540 41.771  10.439  1.00 23.75  ? 281  PRO A CG    1 
ATOM   2065 C CD    . PRO A 1 302 ? 22.138 42.121  11.889  1.00 22.05  ? 281  PRO A CD    1 
ATOM   2066 N N     . GLY A 1 303 ? 21.521 38.538  11.650  1.00 21.36  ? 282  GLY A N     1 
ATOM   2067 C CA    . GLY A 1 303 ? 21.808 37.119  11.600  1.00 21.03  ? 282  GLY A CA    1 
ATOM   2068 C C     . GLY A 1 303 ? 20.677 36.239  12.134  1.00 21.23  ? 282  GLY A C     1 
ATOM   2069 O O     . GLY A 1 303 ? 20.719 35.028  11.949  1.00 19.93  ? 282  GLY A O     1 
ATOM   2070 N N     . VAL A 1 304 ? 19.638 36.830  12.750  1.00 20.19  ? 283  VAL A N     1 
ATOM   2071 C CA    . VAL A 1 304 ? 18.595 36.022  13.363  1.00 19.18  ? 283  VAL A CA    1 
ATOM   2072 C C     . VAL A 1 304 ? 17.810 35.269  12.278  1.00 19.11  ? 283  VAL A C     1 
ATOM   2073 O O     . VAL A 1 304 ? 17.249 35.875  11.371  1.00 18.16  ? 283  VAL A O     1 
ATOM   2074 C CB    . VAL A 1 304 ? 17.658 36.887  14.232  1.00 17.74  ? 283  VAL A CB    1 
ATOM   2075 C CG1   . VAL A 1 304 ? 16.510 36.035  14.756  1.00 19.78  ? 283  VAL A CG1   1 
ATOM   2076 C CG2   . VAL A 1 304 ? 18.373 37.626  15.358  1.00 18.14  ? 283  VAL A CG2   1 
ATOM   2077 N N     . GLY A 1 305 ? 17.743 33.930  12.390  1.00 18.65  ? 284  GLY A N     1 
ATOM   2078 C CA    . GLY A 1 305 ? 17.046 33.114  11.424  1.00 18.81  ? 284  GLY A CA    1 
ATOM   2079 C C     . GLY A 1 305 ? 17.936 32.707  10.251  1.00 20.48  ? 284  GLY A C     1 
ATOM   2080 O O     . GLY A 1 305 ? 17.467 31.957  9.408   1.00 21.90  ? 284  GLY A O     1 
ATOM   2081 N N     . ARG A 1 306 ? 19.180 33.222  10.177  1.00 21.12  ? 285  ARG A N     1 
ATOM   2082 C CA    . ARG A 1 306 ? 20.064 32.938  9.069   1.00 20.41  ? 285  ARG A CA    1 
ATOM   2083 C C     . ARG A 1 306 ? 20.989 31.786  9.449   1.00 20.13  ? 285  ARG A C     1 
ATOM   2084 O O     . ARG A 1 306 ? 20.941 31.314  10.586  1.00 17.68  ? 285  ARG A O     1 
ATOM   2085 C CB    . ARG A 1 306 ? 20.831 34.200  8.662   1.00 23.05  ? 285  ARG A CB    1 
ATOM   2086 C CG    . ARG A 1 306 ? 19.875 35.271  8.147   1.00 26.86  ? 285  ARG A CG    1 
ATOM   2087 C CD    . ARG A 1 306 ? 20.662 36.420  7.628   1.00 37.20  ? 285  ARG A CD    1 
ATOM   2088 N NE    . ARG A 1 306 ? 21.462 36.166  6.418   1.00 43.96  ? 285  ARG A NE    1 
ATOM   2089 C CZ    . ARG A 1 306 ? 20.971 36.173  5.164   1.00 49.59  ? 285  ARG A CZ    1 
ATOM   2090 N NH1   . ARG A 1 306 ? 19.704 35.898  4.925   1.00 51.37  ? 285  ARG A NH1   1 
ATOM   2091 N NH2   . ARG A 1 306 ? 21.763 36.415  4.131   1.00 47.95  ? 285  ARG A NH2   1 
ATOM   2092 N N     . ASN A 1 307 ? 21.787 31.312  8.465   1.00 19.52  ? 286  ASN A N     1 
ATOM   2093 C CA    . ASN A 1 307 ? 22.795 30.286  8.702   1.00 19.67  ? 286  ASN A CA    1 
ATOM   2094 C C     . ASN A 1 307 ? 22.153 28.939  9.103   1.00 19.10  ? 286  ASN A C     1 
ATOM   2095 O O     . ASN A 1 307 ? 22.813 28.088  9.709   1.00 18.86  ? 286  ASN A O     1 
ATOM   2096 C CB    . ASN A 1 307 ? 23.721 30.756  9.818   1.00 22.26  ? 286  ASN A CB    1 
ATOM   2097 C CG    . ASN A 1 307 ? 24.870 29.823  10.136  1.00 27.96  ? 286  ASN A CG    1 
ATOM   2098 O OD1   . ASN A 1 307 ? 25.665 29.556  9.235   1.00 31.53  ? 286  ASN A OD1   1 
ATOM   2099 N ND2   . ASN A 1 307 ? 25.000 29.363  11.389  1.00 31.53  ? 286  ASN A ND2   1 
ATOM   2100 N N     . LEU A 1 308 ? 20.893 28.718  8.722   1.00 18.91  ? 287  LEU A N     1 
ATOM   2101 C CA    . LEU A 1 308 ? 20.223 27.456  8.984   1.00 20.61  ? 287  LEU A CA    1 
ATOM   2102 C C     . LEU A 1 308 ? 20.963 26.331  8.265   1.00 19.64  ? 287  LEU A C     1 
ATOM   2103 O O     . LEU A 1 308 ? 21.137 26.394  7.050   1.00 19.43  ? 287  LEU A O     1 
ATOM   2104 C CB    . LEU A 1 308 ? 18.754 27.517  8.558   1.00 18.95  ? 287  LEU A CB    1 
ATOM   2105 C CG    . LEU A 1 308 ? 17.946 26.230  8.754   1.00 20.09  ? 287  LEU A CG    1 
ATOM   2106 C CD1   . LEU A 1 308 ? 17.906 25.733  10.198  1.00 19.50  ? 287  LEU A CD1   1 
ATOM   2107 C CD2   . LEU A 1 308 ? 16.536 26.357  8.211   1.00 20.07  ? 287  LEU A CD2   1 
ATOM   2108 N N     . GLN A 1 309 ? 21.319 25.293  9.019   1.00 16.88  ? 288  GLN A N     1 
ATOM   2109 C CA    . GLN A 1 309 ? 21.899 24.078  8.464   1.00 18.88  ? 288  GLN A CA    1 
ATOM   2110 C C     . GLN A 1 309 ? 21.206 22.857  9.055   1.00 18.49  ? 288  GLN A C     1 
ATOM   2111 O O     . GLN A 1 309 ? 20.706 22.918  10.174  1.00 16.16  ? 288  GLN A O     1 
ATOM   2112 C CB    . GLN A 1 309 ? 23.376 23.981  8.859   1.00 19.94  ? 288  GLN A CB    1 
ATOM   2113 C CG    . GLN A 1 309 ? 24.272 25.029  8.211   1.00 20.24  ? 288  GLN A CG    1 
ATOM   2114 C CD    . GLN A 1 309 ? 25.526 25.271  9.008   1.00 23.98  ? 288  GLN A CD    1 
ATOM   2115 O OE1   . GLN A 1 309 ? 26.420 24.426  9.089   1.00 22.41  ? 288  GLN A OE1   1 
ATOM   2116 N NE2   . GLN A 1 309 ? 25.596 26.433  9.642   1.00 26.61  ? 288  GLN A NE2   1 
ATOM   2117 N N     . ASP A 1 310 ? 21.259 21.751  8.304   1.00 17.26  ? 289  ASP A N     1 
ATOM   2118 C CA    . ASP A 1 310 ? 20.613 20.502  8.671   1.00 17.48  ? 289  ASP A CA    1 
ATOM   2119 C C     . ASP A 1 310 ? 21.283 19.342  7.937   1.00 18.31  ? 289  ASP A C     1 
ATOM   2120 O O     . ASP A 1 310 ? 21.838 19.487  6.837   1.00 21.72  ? 289  ASP A O     1 
ATOM   2121 C CB    . ASP A 1 310 ? 19.114 20.556  8.381   1.00 17.81  ? 289  ASP A CB    1 
ATOM   2122 C CG    . ASP A 1 310 ? 18.265 19.388  8.872   1.00 18.66  ? 289  ASP A CG    1 
ATOM   2123 O OD1   . ASP A 1 310 ? 18.722 18.661  9.821   1.00 17.80  ? 289  ASP A OD1   1 
ATOM   2124 O OD2   . ASP A 1 310 ? 17.171 19.169  8.246   1.00 19.24  ? 289  ASP A OD2   1 
ATOM   2125 N N     . HIS A 1 311 ? 21.231 18.158  8.554   1.00 17.94  ? 290  HIS A N     1 
ATOM   2126 C CA    . HIS A 1 311 ? 21.625 16.958  7.844   1.00 18.04  ? 290  HIS A CA    1 
ATOM   2127 C C     . HIS A 1 311 ? 20.461 16.533  6.954   1.00 22.13  ? 290  HIS A C     1 
ATOM   2128 O O     . HIS A 1 311 ? 19.287 16.669  7.342   1.00 25.66  ? 290  HIS A O     1 
ATOM   2129 C CB    . HIS A 1 311 ? 22.014 15.857  8.823   1.00 17.92  ? 290  HIS A CB    1 
ATOM   2130 C CG    . HIS A 1 311 ? 23.266 16.167  9.593   1.00 17.12  ? 290  HIS A CG    1 
ATOM   2131 N ND1   . HIS A 1 311 ? 23.462 15.765  10.895  1.00 15.36  ? 290  HIS A ND1   1 
ATOM   2132 C CD2   . HIS A 1 311 ? 24.401 16.758  9.208   1.00 15.29  ? 290  HIS A CD2   1 
ATOM   2133 C CE1   . HIS A 1 311 ? 24.672 16.156  11.287  1.00 17.71  ? 290  HIS A CE1   1 
ATOM   2134 N NE2   . HIS A 1 311 ? 25.250 16.805  10.293  1.00 14.89  ? 290  HIS A NE2   1 
ATOM   2135 N N     . VAL A 1 312 ? 20.818 15.965  5.803   1.00 21.13  ? 291  VAL A N     1 
ATOM   2136 C CA    . VAL A 1 312 ? 19.874 15.393  4.863   1.00 25.80  ? 291  VAL A CA    1 
ATOM   2137 C C     . VAL A 1 312 ? 20.317 13.956  4.615   1.00 23.66  ? 291  VAL A C     1 
ATOM   2138 O O     . VAL A 1 312 ? 21.518 13.660  4.623   1.00 21.30  ? 291  VAL A O     1 
ATOM   2139 C CB    . VAL A 1 312 ? 19.750 16.254  3.582   1.00 33.46  ? 291  VAL A CB    1 
ATOM   2140 C CG1   . VAL A 1 312 ? 21.003 17.029  3.268   1.00 38.69  ? 291  VAL A CG1   1 
ATOM   2141 C CG2   . VAL A 1 312 ? 19.377 15.468  2.342   1.00 38.78  ? 291  VAL A CG2   1 
ATOM   2142 N N     . ALA A 1 313 ? 19.324 13.071  4.458   1.00 21.82  ? 292  ALA A N     1 
ATOM   2143 C CA    . ALA A 1 313 ? 19.565 11.646  4.284   1.00 22.60  ? 292  ALA A CA    1 
ATOM   2144 C C     . ALA A 1 313 ? 18.738 11.127  3.110   1.00 20.99  ? 292  ALA A C     1 
ATOM   2145 O O     . ALA A 1 313 ? 17.653 11.630  2.870   1.00 20.98  ? 292  ALA A O     1 
ATOM   2146 C CB    . ALA A 1 313 ? 19.212 10.889  5.552   1.00 20.95  ? 292  ALA A CB    1 
ATOM   2147 N N     . VAL A 1 314 ? 19.271 10.104  2.451   1.00 21.61  ? 293  VAL A N     1 
ATOM   2148 C CA    . VAL A 1 314 ? 18.597 9.282   1.452   1.00 20.91  ? 293  VAL A CA    1 
ATOM   2149 C C     . VAL A 1 314 ? 18.563 7.836   1.948   1.00 19.82  ? 293  VAL A C     1 
ATOM   2150 O O     . VAL A 1 314 ? 19.607 7.254   2.251   1.00 20.95  ? 293  VAL A O     1 
ATOM   2151 C CB    . VAL A 1 314 ? 19.333 9.352   0.106   1.00 23.16  ? 293  VAL A CB    1 
ATOM   2152 C CG1   . VAL A 1 314 ? 18.766 8.338   -0.890  1.00 23.51  ? 293  VAL A CG1   1 
ATOM   2153 C CG2   . VAL A 1 314 ? 19.301 10.763  -0.465  1.00 23.92  ? 293  VAL A CG2   1 
ATOM   2154 N N     . ASP A 1 315 ? 17.360 7.253   2.029   1.00 20.21  ? 294  ASP A N     1 
ATOM   2155 C CA    . ASP A 1 315 ? 17.210 5.886   2.504   1.00 22.09  ? 294  ASP A CA    1 
ATOM   2156 C C     . ASP A 1 315 ? 17.305 4.894   1.335   1.00 20.71  ? 294  ASP A C     1 
ATOM   2157 O O     . ASP A 1 315 ? 16.468 4.910   0.437   1.00 20.58  ? 294  ASP A O     1 
ATOM   2158 C CB    . ASP A 1 315 ? 15.878 5.684   3.186   1.00 23.79  ? 294  ASP A CB    1 
ATOM   2159 C CG    . ASP A 1 315 ? 15.739 6.421   4.497   1.00 25.92  ? 294  ASP A CG    1 
ATOM   2160 O OD1   . ASP A 1 315 ? 16.755 6.825   5.039   1.00 27.44  ? 294  ASP A OD1   1 
ATOM   2161 O OD2   . ASP A 1 315 ? 14.601 6.606   4.909   1.00 30.99  ? 294  ASP A OD2   1 
ATOM   2162 N N     . VAL A 1 316 ? 18.314 4.021   1.399   1.00 19.47  ? 295  VAL A N     1 
ATOM   2163 C CA    . VAL A 1 316 ? 18.503 2.906   0.473   1.00 18.59  ? 295  VAL A CA    1 
ATOM   2164 C C     . VAL A 1 316 ? 17.825 1.708   1.132   1.00 18.68  ? 295  VAL A C     1 
ATOM   2165 O O     . VAL A 1 316 ? 18.274 1.245   2.187   1.00 19.99  ? 295  VAL A O     1 
ATOM   2166 C CB    . VAL A 1 316 ? 20.020 2.680   0.237   1.00 18.51  ? 295  VAL A CB    1 
ATOM   2167 C CG1   . VAL A 1 316 ? 20.302 1.582   -0.772  1.00 18.88  ? 295  VAL A CG1   1 
ATOM   2168 C CG2   . VAL A 1 316 ? 20.744 3.947   -0.204  1.00 19.21  ? 295  VAL A CG2   1 
ATOM   2169 N N     . MET A 1 317 ? 16.688 1.314   0.562   1.00 18.67  ? 296  MET A N     1 
ATOM   2170 C CA    . MET A 1 317 ? 15.803 0.313   1.122   1.00 20.01  ? 296  MET A CA    1 
ATOM   2171 C C     . MET A 1 317 ? 15.807 -0.932  0.235   1.00 21.01  ? 296  MET A C     1 
ATOM   2172 O O     . MET A 1 317 ? 15.557 -0.825  -0.961  1.00 23.09  ? 296  MET A O     1 
ATOM   2173 C CB    . MET A 1 317 ? 14.390 0.877   1.191   1.00 20.26  ? 296  MET A CB    1 
ATOM   2174 C CG    . MET A 1 317 ? 14.268 2.122   2.039   1.00 26.38  ? 296  MET A CG    1 
ATOM   2175 S SD    . MET A 1 317 ? 12.560 2.626   2.331   1.00 29.24  ? 296  MET A SD    1 
ATOM   2176 C CE    . MET A 1 317 ? 11.949 3.016   0.690   1.00 29.33  ? 296  MET A CE    1 
ATOM   2177 N N     . MET A 1 318 ? 16.023 -2.105  0.846   1.00 21.83  ? 297  MET A N     1 
ATOM   2178 C CA    . MET A 1 318 ? 16.043 -3.376  0.131   1.00 20.05  ? 297  MET A CA    1 
ATOM   2179 C C     . MET A 1 318 ? 15.013 -4.307  0.759   1.00 22.53  ? 297  MET A C     1 
ATOM   2180 O O     . MET A 1 318 ? 14.764 -4.251  1.965   1.00 20.01  ? 297  MET A O     1 
ATOM   2181 C CB    . MET A 1 318 ? 17.426 -4.041  0.187   1.00 19.80  ? 297  MET A CB    1 
ATOM   2182 C CG    . MET A 1 318 ? 18.568 -3.195  -0.376  1.00 21.19  ? 297  MET A CG    1 
ATOM   2183 S SD    . MET A 1 318 ? 18.405 -2.918  -2.148  1.00 25.48  ? 297  MET A SD    1 
ATOM   2184 C CE    . MET A 1 318 ? 18.897 -4.569  -2.681  1.00 28.14  ? 297  MET A CE    1 
ATOM   2185 N N     . ARG A 1 319 ? 14.370 -5.131  -0.082  1.00 22.57  ? 298  ARG A N     1 
ATOM   2186 C CA    . ARG A 1 319 ? 13.474 -6.165  0.407   1.00 24.55  ? 298  ARG A CA    1 
ATOM   2187 C C     . ARG A 1 319 ? 14.272 -7.247  1.135   1.00 22.21  ? 298  ARG A C     1 
ATOM   2188 O O     . ARG A 1 319 ? 15.283 -7.708  0.627   1.00 24.54  ? 298  ARG A O     1 
ATOM   2189 C CB    . ARG A 1 319 ? 12.708 -6.761  -0.785  1.00 29.96  ? 298  ARG A CB    1 
ATOM   2190 C CG    . ARG A 1 319 ? 11.913 -7.988  -0.346  1.00 37.88  ? 298  ARG A CG    1 
ATOM   2191 C CD    . ARG A 1 319 ? 10.777 -8.403  -1.277  1.00 47.21  ? 298  ARG A CD    1 
ATOM   2192 N NE    . ARG A 1 319 ? 11.213 -8.477  -2.672  1.00 57.94  ? 298  ARG A NE    1 
ATOM   2193 C CZ    . ARG A 1 319 ? 11.649 -9.588  -3.269  1.00 75.71  ? 298  ARG A CZ    1 
ATOM   2194 N NH1   . ARG A 1 319 ? 11.802 -10.702 -2.570  1.00 77.59  ? 298  ARG A NH1   1 
ATOM   2195 N NH2   . ARG A 1 319 ? 11.967 -9.583  -4.556  1.00 81.14  ? 298  ARG A NH2   1 
ATOM   2196 N N     . ALA A 1 320 ? 13.787 -7.693  2.297   1.00 21.91  ? 299  ALA A N     1 
ATOM   2197 C CA    . ALA A 1 320 ? 14.476 -8.679  3.119   1.00 23.28  ? 299  ALA A CA    1 
ATOM   2198 C C     . ALA A 1 320 ? 14.092 -10.114 2.718   1.00 24.46  ? 299  ALA A C     1 
ATOM   2199 O O     . ALA A 1 320 ? 12.956 -10.375 2.302   1.00 22.38  ? 299  ALA A O     1 
ATOM   2200 C CB    . ALA A 1 320 ? 14.130 -8.451  4.573   1.00 25.28  ? 299  ALA A CB    1 
ATOM   2201 N N     . THR A 1 321 ? 15.023 -11.047 2.922   1.00 24.66  ? 300  THR A N     1 
ATOM   2202 C CA    . THR A 1 321 ? 14.787 -12.465 2.679   1.00 28.62  ? 300  THR A CA    1 
ATOM   2203 C C     . THR A 1 321 ? 14.662 -13.188 4.007   1.00 33.40  ? 300  THR A C     1 
ATOM   2204 O O     . THR A 1 321 ? 14.577 -14.414 4.042   1.00 32.22  ? 300  THR A O     1 
ATOM   2205 C CB    . THR A 1 321 ? 15.935 -13.098 1.896   1.00 26.63  ? 300  THR A CB    1 
ATOM   2206 O OG1   . THR A 1 321 ? 17.105 -12.905 2.692   1.00 27.21  ? 300  THR A OG1   1 
ATOM   2207 C CG2   . THR A 1 321 ? 16.066 -12.516 0.506   1.00 28.92  ? 300  THR A CG2   1 
ATOM   2208 N N     . VAL A 1 322 ? 14.793 -12.426 5.089   1.00 30.76  ? 301  VAL A N     1 
ATOM   2209 C CA    . VAL A 1 322 ? 14.743 -12.970 6.429   1.00 30.37  ? 301  VAL A CA    1 
ATOM   2210 C C     . VAL A 1 322 ? 13.652 -12.231 7.184   1.00 29.42  ? 301  VAL A C     1 
ATOM   2211 O O     . VAL A 1 322 ? 13.101 -11.241 6.680   1.00 28.40  ? 301  VAL A O     1 
ATOM   2212 C CB    . VAL A 1 322 ? 16.087 -12.886 7.177   1.00 30.95  ? 301  VAL A CB    1 
ATOM   2213 C CG1   . VAL A 1 322 ? 17.109 -13.842 6.564   1.00 33.71  ? 301  VAL A CG1   1 
ATOM   2214 C CG2   . VAL A 1 322 ? 16.607 -11.449 7.270   1.00 30.39  ? 301  VAL A CG2   1 
ATOM   2215 N N     . ALA A 1 323 ? 13.324 -12.782 8.358   1.00 27.78  ? 302  ALA A N     1 
ATOM   2216 C CA    . ALA A 1 323 ? 12.395 -12.161 9.299   1.00 29.18  ? 302  ALA A CA    1 
ATOM   2217 C C     . ALA A 1 323 ? 12.875 -10.749 9.635   1.00 27.14  ? 302  ALA A C     1 
ATOM   2218 O O     . ALA A 1 323 ? 14.065 -10.523 9.869   1.00 25.21  ? 302  ALA A O     1 
ATOM   2219 C CB    . ALA A 1 323 ? 12.335 -13.005 10.565  1.00 32.27  ? 302  ALA A CB    1 
ATOM   2220 N N     . VAL A 1 324 ? 11.920 -9.819  9.715   1.00 26.83  ? 303  VAL A N     1 
ATOM   2221 C CA    . VAL A 1 324 ? 12.170 -8.439  10.080  1.00 25.90  ? 303  VAL A CA    1 
ATOM   2222 C C     . VAL A 1 324 ? 11.268 -8.122  11.272  1.00 24.28  ? 303  VAL A C     1 
ATOM   2223 O O     . VAL A 1 324 ? 10.182 -7.583  11.092  1.00 22.00  ? 303  VAL A O     1 
ATOM   2224 C CB    . VAL A 1 324 ? 11.922 -7.515  8.873   1.00 24.88  ? 303  VAL A CB    1 
ATOM   2225 C CG1   . VAL A 1 324 ? 12.202 -6.057  9.200   1.00 24.42  ? 303  VAL A CG1   1 
ATOM   2226 C CG2   . VAL A 1 324 ? 12.791 -7.927  7.688   1.00 27.15  ? 303  VAL A CG2   1 
ATOM   2227 N N     . PRO A 1 325 ? 11.691 -8.447  12.515  1.00 23.68  ? 304  PRO A N     1 
ATOM   2228 C CA    . PRO A 1 325 ? 10.892 -8.149  13.710  1.00 26.51  ? 304  PRO A CA    1 
ATOM   2229 C C     . PRO A 1 325 ? 10.448 -6.700  13.869  1.00 25.51  ? 304  PRO A C     1 
ATOM   2230 O O     . PRO A 1 325 ? 9.352  -6.441  14.370  1.00 25.03  ? 304  PRO A O     1 
ATOM   2231 C CB    . PRO A 1 325 ? 11.804 -8.593  14.863  1.00 27.26  ? 304  PRO A CB    1 
ATOM   2232 C CG    . PRO A 1 325 ? 12.701 -9.618  14.269  1.00 27.63  ? 304  PRO A CG    1 
ATOM   2233 C CD    . PRO A 1 325 ? 12.912 -9.193  12.834  1.00 25.66  ? 304  PRO A CD    1 
ATOM   2234 N N     . LEU A 1 326 ? 11.270 -5.746  13.395  1.00 22.14  ? 305  LEU A N     1 
ATOM   2235 C CA    . LEU A 1 326 ? 10.937 -4.339  13.599  1.00 23.35  ? 305  LEU A CA    1 
ATOM   2236 C C     . LEU A 1 326 ? 9.869  -3.836  12.623  1.00 23.08  ? 305  LEU A C     1 
ATOM   2237 O O     . LEU A 1 326 ? 9.435  -2.692  12.721  1.00 23.35  ? 305  LEU A O     1 
ATOM   2238 C CB    . LEU A 1 326 ? 12.208 -3.492  13.512  1.00 22.40  ? 305  LEU A CB    1 
ATOM   2239 C CG    . LEU A 1 326 ? 13.286 -3.834  14.546  1.00 24.93  ? 305  LEU A CG    1 
ATOM   2240 C CD1   . LEU A 1 326 ? 14.461 -2.902  14.463  1.00 25.86  ? 305  LEU A CD1   1 
ATOM   2241 C CD2   . LEU A 1 326 ? 12.741 -3.791  15.956  1.00 26.91  ? 305  LEU A CD2   1 
ATOM   2242 N N     . ALA A 1 327 ? 9.468  -4.653  11.654  1.00 23.21  ? 306  ALA A N     1 
ATOM   2243 C CA    . ALA A 1 327 ? 8.394  -4.292  10.756  1.00 24.65  ? 306  ALA A CA    1 
ATOM   2244 C C     . ALA A 1 327 ? 7.057  -4.298  11.504  1.00 25.71  ? 306  ALA A C     1 
ATOM   2245 O O     . ALA A 1 327 ? 6.146  -3.591  11.104  1.00 26.96  ? 306  ALA A O     1 
ATOM   2246 C CB    . ALA A 1 327 ? 8.352  -5.290  9.612   1.00 25.29  ? 306  ALA A CB    1 
ATOM   2247 N N     . ASP A 1 328 ? 6.943  -5.107  12.563  1.00 24.78  ? 307  ASP A N     1 
ATOM   2248 C CA    . ASP A 1 328 ? 5.709  -5.217  13.349  1.00 28.78  ? 307  ASP A CA    1 
ATOM   2249 C C     . ASP A 1 328 ? 6.098  -5.506  14.798  1.00 25.02  ? 307  ASP A C     1 
ATOM   2250 O O     . ASP A 1 328 ? 5.966  -6.642  15.242  1.00 28.17  ? 307  ASP A O     1 
ATOM   2251 C CB    . ASP A 1 328 ? 4.842  -6.357  12.822  1.00 31.33  ? 307  ASP A CB    1 
ATOM   2252 C CG    . ASP A 1 328 ? 3.445  -6.483  13.419  1.00 34.75  ? 307  ASP A CG    1 
ATOM   2253 O OD1   . ASP A 1 328 ? 2.989  -5.517  14.033  1.00 32.67  ? 307  ASP A OD1   1 
ATOM   2254 O OD2   . ASP A 1 328 ? 2.841  -7.561  13.285  1.00 40.09  ? 307  ASP A OD2   1 
ATOM   2255 N N     . PRO A 1 329 ? 6.716  -4.558  15.540  1.00 23.79  ? 308  PRO A N     1 
ATOM   2256 C CA    . PRO A 1 329 ? 7.263  -4.867  16.863  1.00 25.75  ? 308  PRO A CA    1 
ATOM   2257 C C     . PRO A 1 329 ? 6.244  -4.970  18.002  1.00 23.60  ? 308  PRO A C     1 
ATOM   2258 O O     . PRO A 1 329 ? 6.520  -5.596  19.026  1.00 23.18  ? 308  PRO A O     1 
ATOM   2259 C CB    . PRO A 1 329 ? 8.277  -3.748  17.128  1.00 25.61  ? 308  PRO A CB    1 
ATOM   2260 C CG    . PRO A 1 329 ? 7.718  -2.577  16.384  1.00 25.27  ? 308  PRO A CG    1 
ATOM   2261 C CD    . PRO A 1 329 ? 7.012  -3.172  15.144  1.00 26.93  ? 308  PRO A CD    1 
ATOM   2262 N N     . ASP A 1 330 ? 5.083  -4.363  17.823  1.00 20.50  ? 309  ASP A N     1 
ATOM   2263 C CA    . ASP A 1 330 ? 4.161  -4.209  18.928  1.00 21.98  ? 309  ASP A CA    1 
ATOM   2264 C C     . ASP A 1 330 ? 3.161  -5.367  18.892  1.00 20.51  ? 309  ASP A C     1 
ATOM   2265 O O     . ASP A 1 330 ? 2.056  -5.228  18.355  1.00 22.71  ? 309  ASP A O     1 
ATOM   2266 C CB    . ASP A 1 330 ? 3.553  -2.813  18.920  1.00 22.95  ? 309  ASP A CB    1 
ATOM   2267 C CG    . ASP A 1 330 ? 2.844  -2.484  20.224  1.00 23.74  ? 309  ASP A CG    1 
ATOM   2268 O OD1   . ASP A 1 330 ? 3.104  -3.187  21.241  1.00 22.42  ? 309  ASP A OD1   1 
ATOM   2269 O OD2   . ASP A 1 330 ? 1.997  -1.594  20.193  1.00 26.90  ? 309  ASP A OD2   1 
ATOM   2270 N N     . THR A 1 331 ? 3.567  -6.510  19.443  1.00 18.29  ? 310  THR A N     1 
ATOM   2271 C CA    . THR A 1 331 ? 2.787  -7.750  19.406  1.00 18.60  ? 310  THR A CA    1 
ATOM   2272 C C     . THR A 1 331 ? 2.648  -8.238  20.837  1.00 19.84  ? 310  THR A C     1 
ATOM   2273 O O     . THR A 1 331 ? 3.413  -7.848  21.700  1.00 20.01  ? 310  THR A O     1 
ATOM   2274 C CB    . THR A 1 331 ? 3.490  -8.843  18.598  1.00 20.32  ? 310  THR A CB    1 
ATOM   2275 O OG1   . THR A 1 331 ? 4.663  -9.207  19.339  1.00 18.80  ? 310  THR A OG1   1 
ATOM   2276 C CG2   . THR A 1 331 ? 3.816  -8.438  17.163  1.00 21.62  ? 310  THR A CG2   1 
ATOM   2277 N N     . PRO A 1 332 ? 1.686  -9.124  21.157  1.00 20.05  ? 311  PRO A N     1 
ATOM   2278 C CA    . PRO A 1 332 ? 1.614  -9.645  22.516  1.00 18.97  ? 311  PRO A CA    1 
ATOM   2279 C C     . PRO A 1 332 ? 2.927  -10.213 23.059  1.00 18.88  ? 311  PRO A C     1 
ATOM   2280 O O     . PRO A 1 332 ? 3.302  -9.943  24.205  1.00 16.10  ? 311  PRO A O     1 
ATOM   2281 C CB    . PRO A 1 332 ? 0.510  -10.690 22.415  1.00 19.38  ? 311  PRO A CB    1 
ATOM   2282 C CG    . PRO A 1 332 ? -0.399 -10.154 21.319  1.00 20.64  ? 311  PRO A CG    1 
ATOM   2283 C CD    . PRO A 1 332 ? 0.559  -9.532  20.286  1.00 19.27  ? 311  PRO A CD    1 
ATOM   2284 N N     . ALA A 1 333 ? 3.594  -11.024 22.236  1.00 19.92  ? 312  ALA A N     1 
ATOM   2285 C CA    . ALA A 1 333 ? 4.834  -11.674 22.649  1.00 24.75  ? 312  ALA A CA    1 
ATOM   2286 C C     . ALA A 1 333 ? 5.923  -10.652 22.994  1.00 20.95  ? 312  ALA A C     1 
ATOM   2287 O O     . ALA A 1 333 ? 6.607  -10.785 24.002  1.00 21.19  ? 312  ALA A O     1 
ATOM   2288 C CB    . ALA A 1 333 ? 5.273  -12.651 21.565  1.00 24.29  ? 312  ALA A CB    1 
ATOM   2289 N N     . ASN A 1 334 ? 6.098  -9.638  22.140  1.00 19.92  ? 313  ASN A N     1 
ATOM   2290 C CA    . ASN A 1 334 ? 7.078  -8.581  22.370  1.00 18.44  ? 313  ASN A CA    1 
ATOM   2291 C C     . ASN A 1 334 ? 6.674  -7.719  23.563  1.00 18.94  ? 313  ASN A C     1 
ATOM   2292 O O     . ASN A 1 334 ? 7.548  -7.278  24.313  1.00 20.71  ? 313  ASN A O     1 
ATOM   2293 C CB    . ASN A 1 334 ? 7.305  -7.759  21.111  1.00 17.36  ? 313  ASN A CB    1 
ATOM   2294 C CG    . ASN A 1 334 ? 7.918  -8.570  19.999  1.00 18.55  ? 313  ASN A CG    1 
ATOM   2295 O OD1   . ASN A 1 334 ? 8.485  -9.623  20.250  1.00 21.07  ? 313  ASN A OD1   1 
ATOM   2296 N ND2   . ASN A 1 334 ? 7.917  -8.058  18.783  1.00 20.49  ? 313  ASN A ND2   1 
ATOM   2297 N N     . ARG A 1 335 ? 5.367  -7.499  23.788  1.00 17.38  ? 314  ARG A N     1 
ATOM   2298 C CA    . ARG A 1 335 ? 4.947  -6.712  24.939  1.00 18.03  ? 314  ARG A CA    1 
ATOM   2299 C C     . ARG A 1 335 ? 5.262  -7.479  26.230  1.00 18.42  ? 314  ARG A C     1 
ATOM   2300 O O     . ARG A 1 335 ? 5.687  -6.891  27.207  1.00 20.92  ? 314  ARG A O     1 
ATOM   2301 C CB    . ARG A 1 335 ? 3.463  -6.305  24.869  1.00 20.71  ? 314  ARG A CB    1 
ATOM   2302 C CG    . ARG A 1 335 ? 3.076  -5.219  23.872  1.00 22.04  ? 314  ARG A CG    1 
ATOM   2303 C CD    . ARG A 1 335 ? 1.614  -4.789  24.057  1.00 21.36  ? 314  ARG A CD    1 
ATOM   2304 N NE    . ARG A 1 335 ? 0.672  -5.769  23.508  1.00 19.13  ? 314  ARG A NE    1 
ATOM   2305 C CZ    . ARG A 1 335 ? 0.313  -5.825  22.223  1.00 21.13  ? 314  ARG A CZ    1 
ATOM   2306 N NH1   . ARG A 1 335 ? -0.641 -6.661  21.867  1.00 18.63  ? 314  ARG A NH1   1 
ATOM   2307 N NH2   . ARG A 1 335 ? 0.853  -5.024  21.319  1.00 19.77  ? 314  ARG A NH2   1 
ATOM   2308 N N     . GLU A 1 336 ? 5.128  -8.801  26.220  1.00 20.29  ? 315  GLU A N     1 
ATOM   2309 C CA    . GLU A 1 336 ? 5.364  -9.609  27.408  1.00 22.64  ? 315  GLU A CA    1 
ATOM   2310 C C     . GLU A 1 336 ? 6.859  -9.643  27.730  1.00 20.80  ? 315  GLU A C     1 
ATOM   2311 O O     . GLU A 1 336 ? 7.268  -9.443  28.869  1.00 20.21  ? 315  GLU A O     1 
ATOM   2312 C CB    . GLU A 1 336 ? 4.716  -10.974 27.178  1.00 25.95  ? 315  GLU A CB    1 
ATOM   2313 C CG    . GLU A 1 336 ? 4.762  -11.875 28.402  1.00 30.92  ? 315  GLU A CG    1 
ATOM   2314 C CD    . GLU A 1 336 ? 6.135  -12.453 28.751  1.00 41.07  ? 315  GLU A CD    1 
ATOM   2315 O OE1   . GLU A 1 336 ? 6.983  -12.720 27.843  1.00 40.32  ? 315  GLU A OE1   1 
ATOM   2316 O OE2   . GLU A 1 336 ? 6.352  -12.659 29.973  1.00 43.49  ? 315  GLU A OE2   1 
ATOM   2317 N N     . LEU A 1 337 ? 7.681  -9.796  26.703  1.00 20.26  ? 316  LEU A N     1 
ATOM   2318 C CA    . LEU A 1 337 ? 9.124  -9.749  26.895  1.00 21.58  ? 316  LEU A CA    1 
ATOM   2319 C C     . LEU A 1 337 ? 9.591  -8.365  27.359  1.00 22.06  ? 316  LEU A C     1 
ATOM   2320 O O     . LEU A 1 337 ? 10.436 -8.278  28.257  1.00 23.03  ? 316  LEU A O     1 
ATOM   2321 C CB    . LEU A 1 337 ? 9.804  -10.171 25.602  1.00 21.68  ? 316  LEU A CB    1 
ATOM   2322 C CG    . LEU A 1 337 ? 11.331 -10.234 25.637  1.00 26.52  ? 316  LEU A CG    1 
ATOM   2323 C CD1   . LEU A 1 337 ? 11.856 -11.132 26.776  1.00 27.85  ? 316  LEU A CD1   1 
ATOM   2324 C CD2   . LEU A 1 337 ? 11.819 -10.681 24.258  1.00 26.86  ? 316  LEU A CD2   1 
ATOM   2325 N N     . TYR A 1 338 ? 9.004  -7.292  26.801  1.00 20.59  ? 317  TYR A N     1 
ATOM   2326 C CA    . TYR A 1 338 ? 9.373  -5.935  27.196  1.00 21.20  ? 317  TYR A CA    1 
ATOM   2327 C C     . TYR A 1 338 ? 9.008  -5.671  28.662  1.00 22.38  ? 317  TYR A C     1 
ATOM   2328 O O     . TYR A 1 338 ? 9.762  -5.039  29.412  1.00 19.79  ? 317  TYR A O     1 
ATOM   2329 C CB    . TYR A 1 338 ? 8.761  -4.907  26.227  1.00 19.82  ? 317  TYR A CB    1 
ATOM   2330 C CG    . TYR A 1 338 ? 9.285  -3.494  26.479  1.00 21.46  ? 317  TYR A CG    1 
ATOM   2331 C CD1   . TYR A 1 338 ? 10.561 -3.134  26.090  1.00 20.79  ? 317  TYR A CD1   1 
ATOM   2332 C CD2   . TYR A 1 338 ? 8.505  -2.523  27.092  1.00 21.09  ? 317  TYR A CD2   1 
ATOM   2333 C CE1   . TYR A 1 338 ? 11.071 -1.879  26.352  1.00 18.95  ? 317  TYR A CE1   1 
ATOM   2334 C CE2   . TYR A 1 338 ? 8.990  -1.256  27.348  1.00 22.38  ? 317  TYR A CE2   1 
ATOM   2335 C CZ    . TYR A 1 338 ? 10.280 -0.923  26.962  1.00 22.49  ? 317  TYR A CZ    1 
ATOM   2336 O OH    . TYR A 1 338 ? 10.808 0.316   27.203  1.00 18.80  ? 317  TYR A OH    1 
ATOM   2337 N N     . GLU A 1 339 ? 7.796  -6.080  29.053  1.00 24.84  ? 318  GLU A N     1 
ATOM   2338 C CA    . GLU A 1 339 ? 7.323  -5.885  30.414  1.00 26.08  ? 318  GLU A CA    1 
ATOM   2339 C C     . GLU A 1 339 ? 8.191  -6.658  31.403  1.00 24.81  ? 318  GLU A C     1 
ATOM   2340 O O     . GLU A 1 339 ? 8.502  -6.145  32.463  1.00 25.43  ? 318  GLU A O     1 
ATOM   2341 C CB    . GLU A 1 339 ? 5.882  -6.381  30.564  1.00 30.17  ? 318  GLU A CB    1 
ATOM   2342 C CG    . GLU A 1 339 ? 5.257  -6.049  31.921  1.00 40.95  ? 318  GLU A CG    1 
ATOM   2343 C CD    . GLU A 1 339 ? 3.764  -6.352  32.039  1.00 56.65  ? 318  GLU A CD    1 
ATOM   2344 O OE1   . GLU A 1 339 ? 3.158  -6.960  31.115  1.00 68.17  ? 318  GLU A OE1   1 
ATOM   2345 O OE2   . GLU A 1 339 ? 3.187  -5.956  33.079  1.00 70.29  ? 318  GLU A OE2   1 
ATOM   2346 N N     . ARG A 1 340 ? 8.539  -7.903  31.067  1.00 24.34  ? 319  ARG A N     1 
ATOM   2347 C CA    . ARG A 1 340 ? 9.230  -8.782  31.991  1.00 25.20  ? 319  ARG A CA    1 
ATOM   2348 C C     . ARG A 1 340 ? 10.722 -8.467  32.039  1.00 25.16  ? 319  ARG A C     1 
ATOM   2349 O O     . ARG A 1 340 ? 11.317 -8.554  33.098  1.00 25.94  ? 319  ARG A O     1 
ATOM   2350 C CB    . ARG A 1 340 ? 8.997  -10.256 31.631  1.00 29.28  ? 319  ARG A CB    1 
ATOM   2351 C CG    . ARG A 1 340 ? 9.626  -11.279 32.582  1.00 31.26  ? 319  ARG A CG    1 
ATOM   2352 C CD    . ARG A 1 340 ? 9.156  -12.732 32.361  1.00 32.05  ? 319  ARG A CD    1 
ATOM   2353 N NE    . ARG A 1 340 ? 8.959  -13.079 30.943  1.00 30.47  ? 319  ARG A NE    1 
ATOM   2354 C CZ    . ARG A 1 340 ? 9.912  -13.357 30.059  1.00 33.31  ? 319  ARG A CZ    1 
ATOM   2355 N NH1   . ARG A 1 340 ? 9.593  -13.550 28.806  1.00 32.55  ? 319  ARG A NH1   1 
ATOM   2356 N NH2   . ARG A 1 340 ? 11.193 -13.396 30.406  1.00 39.94  ? 319  ARG A NH2   1 
ATOM   2357 N N     . GLU A 1 341 ? 11.337 -8.178  30.898  1.00 24.90  ? 320  GLU A N     1 
ATOM   2358 C CA    . GLU A 1 341 ? 12.788 -8.099  30.806  1.00 26.48  ? 320  GLU A CA    1 
ATOM   2359 C C     . GLU A 1 341 ? 13.269 -6.791  30.174  1.00 22.77  ? 320  GLU A C     1 
ATOM   2360 O O     . GLU A 1 341 ? 14.468 -6.563  30.101  1.00 22.31  ? 320  GLU A O     1 
ATOM   2361 C CB    . GLU A 1 341 ? 13.353 -9.204  29.918  1.00 28.04  ? 320  GLU A CB    1 
ATOM   2362 C CG    . GLU A 1 341 ? 13.181 -10.604 30.485  1.00 37.67  ? 320  GLU A CG    1 
ATOM   2363 C CD    . GLU A 1 341 ? 13.949 -11.601 29.645  1.00 45.65  ? 320  GLU A CD    1 
ATOM   2364 O OE1   . GLU A 1 341 ? 13.324 -12.552 29.115  1.00 54.05  ? 320  GLU A OE1   1 
ATOM   2365 O OE2   . GLU A 1 341 ? 15.175 -11.401 29.517  1.00 50.33  ? 320  GLU A OE2   1 
ATOM   2366 N N     . ARG A 1 342 ? 12.367 -5.936  29.691  1.00 24.40  ? 321  ARG A N     1 
ATOM   2367 C CA    . ARG A 1 342 ? 12.779 -4.763  28.927  1.00 23.50  ? 321  ARG A CA    1 
ATOM   2368 C C     . ARG A 1 342 ? 13.704 -5.162  27.794  1.00 23.20  ? 321  ARG A C     1 
ATOM   2369 O O     . ARG A 1 342 ? 14.727 -4.519  27.543  1.00 26.45  ? 321  ARG A O     1 
ATOM   2370 C CB    . ARG A 1 342 ? 13.437 -3.753  29.876  1.00 24.92  ? 321  ARG A CB    1 
ATOM   2371 C CG    . ARG A 1 342 ? 12.415 -3.095  30.786  1.00 24.87  ? 321  ARG A CG    1 
ATOM   2372 C CD    . ARG A 1 342 ? 11.488 -2.207  29.931  1.00 25.97  ? 321  ARG A CD    1 
ATOM   2373 N NE    . ARG A 1 342 ? 10.497 -1.520  30.763  1.00 26.73  ? 321  ARG A NE    1 
ATOM   2374 C CZ    . ARG A 1 342 ? 10.667 -0.464  31.521  1.00 34.56  ? 321  ARG A CZ    1 
ATOM   2375 N NH1   . ARG A 1 342 ? 11.869 0.137   31.653  1.00 34.99  ? 321  ARG A NH1   1 
ATOM   2376 N NH2   . ARG A 1 342 ? 9.582  -0.011  32.126  1.00 37.66  ? 321  ARG A NH2   1 
ATOM   2377 N N     . ARG A 1 343 ? 13.372 -6.263  27.119  1.00 21.96  ? 322  ARG A N     1 
ATOM   2378 C CA    . ARG A 1 343 ? 14.150 -6.678  25.966  1.00 22.79  ? 322  ARG A CA    1 
ATOM   2379 C C     . ARG A 1 343 ? 13.226 -6.889  24.781  1.00 20.66  ? 322  ARG A C     1 
ATOM   2380 O O     . ARG A 1 343 ? 12.006 -6.709  24.886  1.00 24.10  ? 322  ARG A O     1 
ATOM   2381 C CB    . ARG A 1 343 ? 14.876 -8.011  26.224  1.00 24.92  ? 322  ARG A CB    1 
ATOM   2382 C CG    . ARG A 1 343 ? 16.034 -7.803  27.182  1.00 29.31  ? 322  ARG A CG    1 
ATOM   2383 C CD    . ARG A 1 343 ? 16.709 -9.109  27.619  1.00 33.40  ? 322  ARG A CD    1 
ATOM   2384 N NE    . ARG A 1 343 ? 17.777 -8.726  28.548  1.00 34.92  ? 322  ARG A NE    1 
ATOM   2385 C CZ    . ARG A 1 343 ? 18.877 -8.110  28.153  1.00 39.76  ? 322  ARG A CZ    1 
ATOM   2386 N NH1   . ARG A 1 343 ? 19.230 -8.125  26.881  1.00 40.11  ? 322  ARG A NH1   1 
ATOM   2387 N NH2   . ARG A 1 343 ? 19.658 -7.530  29.039  1.00 39.59  ? 322  ARG A NH2   1 
ATOM   2388 N N     . GLY A 1 344 ? 13.824 -7.355  23.688  1.00 19.16  ? 323  GLY A N     1 
ATOM   2389 C CA    . GLY A 1 344 ? 13.113 -7.656  22.453  1.00 19.08  ? 323  GLY A CA    1 
ATOM   2390 C C     . GLY A 1 344 ? 12.920 -6.408  21.610  1.00 18.71  ? 323  GLY A C     1 
ATOM   2391 O O     . GLY A 1 344 ? 13.417 -5.340  21.974  1.00 19.63  ? 323  GLY A O     1 
ATOM   2392 N N     . PRO A 1 345 ? 12.205 -6.524  20.473  1.00 19.61  ? 324  PRO A N     1 
ATOM   2393 C CA    . PRO A 1 345 ? 12.066 -5.437  19.513  1.00 21.89  ? 324  PRO A CA    1 
ATOM   2394 C C     . PRO A 1 345 ? 11.628 -4.089  20.082  1.00 21.82  ? 324  PRO A C     1 
ATOM   2395 O O     . PRO A 1 345 ? 12.076 -3.060  19.581  1.00 19.86  ? 324  PRO A O     1 
ATOM   2396 C CB    . PRO A 1 345 ? 11.048 -5.997  18.505  1.00 23.36  ? 324  PRO A CB    1 
ATOM   2397 C CG    . PRO A 1 345 ? 11.270 -7.470  18.546  1.00 23.40  ? 324  PRO A CG    1 
ATOM   2398 C CD    . PRO A 1 345 ? 11.539 -7.761  20.009  1.00 21.42  ? 324  PRO A CD    1 
ATOM   2399 N N     . LEU A 1 346 ? 10.799 -4.080  21.144  1.00 21.46  ? 325  LEU A N     1 
ATOM   2400 C CA    . LEU A 1 346 ? 10.266 -2.809  21.633  1.00 21.80  ? 325  LEU A CA    1 
ATOM   2401 C C     . LEU A 1 346 ? 11.368 -1.967  22.295  1.00 18.75  ? 325  LEU A C     1 
ATOM   2402 O O     . LEU A 1 346 ? 11.263 -0.742  22.360  1.00 18.06  ? 325  LEU A O     1 
ATOM   2403 C CB    . LEU A 1 346 ? 9.068  -3.063  22.547  1.00 21.77  ? 325  LEU A CB    1 
ATOM   2404 C CG    . LEU A 1 346 ? 7.792  -3.540  21.843  1.00 21.43  ? 325  LEU A CG    1 
ATOM   2405 C CD1   . LEU A 1 346 ? 6.820  -3.942  22.918  1.00 23.43  ? 325  LEU A CD1   1 
ATOM   2406 C CD2   . LEU A 1 346 ? 7.192  -2.448  20.944  1.00 22.41  ? 325  LEU A CD2   1 
ATOM   2407 N N     . SER A 1 347 ? 12.471 -2.605  22.718  1.00 18.70  ? 326  SER A N     1 
ATOM   2408 C CA    . SER A 1 347 ? 13.626 -1.921  23.271  1.00 19.22  ? 326  SER A CA    1 
ATOM   2409 C C     . SER A 1 347 ? 14.518 -1.295  22.200  1.00 18.41  ? 326  SER A C     1 
ATOM   2410 O O     . SER A 1 347 ? 15.411 -0.536  22.563  1.00 21.14  ? 326  SER A O     1 
ATOM   2411 C CB    . SER A 1 347 ? 14.468 -2.845  24.167  1.00 21.49  ? 326  SER A CB    1 
ATOM   2412 O OG    . SER A 1 347 ? 15.148 -3.815  23.389  1.00 19.97  ? 326  SER A OG    1 
ATOM   2413 N N     . SER A 1 348 ? 14.282 -1.593  20.918  1.00 17.70  ? 327  SER A N     1 
ATOM   2414 C CA    . SER A 1 348 ? 15.086 -1.036  19.847  1.00 18.61  ? 327  SER A CA    1 
ATOM   2415 C C     . SER A 1 348 ? 14.670 0.402   19.553  1.00 19.06  ? 327  SER A C     1 
ATOM   2416 O O     . SER A 1 348 ? 13.489 0.712   19.509  1.00 20.14  ? 327  SER A O     1 
ATOM   2417 C CB    . SER A 1 348 ? 14.971 -1.867  18.580  1.00 20.46  ? 327  SER A CB    1 
ATOM   2418 O OG    . SER A 1 348 ? 15.705 -1.264  17.515  1.00 18.98  ? 327  SER A OG    1 
ATOM   2419 N N     . ASN A 1 349 ? 15.656 1.267   19.273  1.00 18.69  ? 328  ASN A N     1 
ATOM   2420 C CA    . ASN A 1 349 ? 15.421 2.610   18.754  1.00 19.78  ? 328  ASN A CA    1 
ATOM   2421 C C     . ASN A 1 349 ? 15.310 2.610   17.228  1.00 18.39  ? 328  ASN A C     1 
ATOM   2422 O O     . ASN A 1 349 ? 15.207 3.691   16.628  1.00 21.30  ? 328  ASN A O     1 
ATOM   2423 C CB    . ASN A 1 349 ? 16.548 3.540   19.208  1.00 19.79  ? 328  ASN A CB    1 
ATOM   2424 C CG    . ASN A 1 349 ? 17.801 3.252   18.422  1.00 18.21  ? 328  ASN A CG    1 
ATOM   2425 O OD1   . ASN A 1 349 ? 18.159 2.080   18.267  1.00 19.81  ? 328  ASN A OD1   1 
ATOM   2426 N ND2   . ASN A 1 349 ? 18.392 4.291   17.831  1.00 19.79  ? 328  ASN A ND2   1 
ATOM   2427 N N     . ILE A 1 350 ? 15.410 1.417   16.613  1.00 17.55  ? 329  ILE A N     1 
ATOM   2428 C CA    . ILE A 1 350 ? 15.303 1.181   15.177  1.00 19.20  ? 329  ILE A CA    1 
ATOM   2429 C C     . ILE A 1 350 ? 16.623 1.477   14.466  1.00 20.49  ? 329  ILE A C     1 
ATOM   2430 O O     . ILE A 1 350 ? 17.076 0.644   13.690  1.00 21.94  ? 329  ILE A O     1 
ATOM   2431 C CB    . ILE A 1 350 ? 14.128 1.928   14.514  1.00 21.28  ? 329  ILE A CB    1 
ATOM   2432 C CG1   . ILE A 1 350 ? 12.824 1.783   15.307  1.00 24.01  ? 329  ILE A CG1   1 
ATOM   2433 C CG2   . ILE A 1 350 ? 13.934 1.397   13.100  1.00 22.62  ? 329  ILE A CG2   1 
ATOM   2434 C CD1   . ILE A 1 350 ? 12.464 0.352   15.633  1.00 23.71  ? 329  ILE A CD1   1 
ATOM   2435 N N     . ALA A 1 351 ? 17.216 2.652   14.713  1.00 19.08  ? 330  ALA A N     1 
ATOM   2436 C CA    . ALA A 1 351 ? 18.488 3.039   14.118  1.00 20.05  ? 330  ALA A CA    1 
ATOM   2437 C C     . ALA A 1 351 ? 19.657 2.462   14.920  1.00 19.54  ? 330  ALA A C     1 
ATOM   2438 O O     . ALA A 1 351 ? 20.277 3.155   15.727  1.00 17.98  ? 330  ALA A O     1 
ATOM   2439 C CB    . ALA A 1 351 ? 18.550 4.546   13.999  1.00 19.12  ? 330  ALA A CB    1 
ATOM   2440 N N     . GLU A 1 352 ? 19.944 1.170   14.694  1.00 18.20  ? 331  GLU A N     1 
ATOM   2441 C CA    . GLU A 1 352 ? 20.726 0.375   15.635  1.00 19.47  ? 331  GLU A CA    1 
ATOM   2442 C C     . GLU A 1 352 ? 22.243 0.476   15.434  1.00 19.00  ? 331  GLU A C     1 
ATOM   2443 O O     . GLU A 1 352 ? 22.980 0.125   16.347  1.00 16.85  ? 331  GLU A O     1 
ATOM   2444 C CB    . GLU A 1 352 ? 20.333 -1.098  15.537  1.00 18.82  ? 331  GLU A CB    1 
ATOM   2445 C CG    . GLU A 1 352 ? 18.881 -1.368  15.906  1.00 19.14  ? 331  GLU A CG    1 
ATOM   2446 C CD    . GLU A 1 352 ? 18.570 -2.828  16.171  1.00 19.47  ? 331  GLU A CD    1 
ATOM   2447 O OE1   . GLU A 1 352 ? 17.512 -3.106  16.792  1.00 22.23  ? 331  GLU A OE1   1 
ATOM   2448 O OE2   . GLU A 1 352 ? 19.381 -3.684  15.780  1.00 20.22  ? 331  GLU A OE2   1 
ATOM   2449 N N     . ALA A 1 353 ? 22.720 0.894   14.252  1.00 18.46  ? 332  ALA A N     1 
ATOM   2450 C CA    . ALA A 1 353 ? 24.159 0.994   14.026  1.00 19.46  ? 332  ALA A CA    1 
ATOM   2451 C C     . ALA A 1 353 ? 24.472 2.176   13.120  1.00 19.84  ? 332  ALA A C     1 
ATOM   2452 O O     . ALA A 1 353 ? 23.603 2.635   12.384  1.00 17.58  ? 332  ALA A O     1 
ATOM   2453 C CB    . ALA A 1 353 ? 24.687 -0.296  13.456  1.00 21.04  ? 332  ALA A CB    1 
ATOM   2454 N N     . VAL A 1 354 ? 25.729 2.653   13.173  1.00 19.65  ? 333  VAL A N     1 
ATOM   2455 C CA    . VAL A 1 354 ? 26.155 3.797   12.384  1.00 19.96  ? 333  VAL A CA    1 
ATOM   2456 C C     . VAL A 1 354 ? 27.524 3.499   11.769  1.00 20.88  ? 333  VAL A C     1 
ATOM   2457 O O     . VAL A 1 354 ? 28.272 2.676   12.287  1.00 20.36  ? 333  VAL A O     1 
ATOM   2458 C CB    . VAL A 1 354 ? 26.199 5.085   13.226  1.00 18.94  ? 333  VAL A CB    1 
ATOM   2459 C CG1   . VAL A 1 354 ? 24.813 5.536   13.660  1.00 19.94  ? 333  VAL A CG1   1 
ATOM   2460 C CG2   . VAL A 1 354 ? 27.116 4.945   14.441  1.00 19.82  ? 333  VAL A CG2   1 
ATOM   2461 N N     . ALA A 1 355 ? 27.830 4.166   10.660  1.00 21.63  ? 334  ALA A N     1 
ATOM   2462 C CA    . ALA A 1 355 ? 29.165 4.100   10.071  1.00 22.63  ? 334  ALA A CA    1 
ATOM   2463 C C     . ALA A 1 355 ? 29.543 5.486   9.563   1.00 21.54  ? 334  ALA A C     1 
ATOM   2464 O O     . ALA A 1 355 ? 28.673 6.283   9.203   1.00 21.81  ? 334  ALA A O     1 
ATOM   2465 C CB    . ALA A 1 355 ? 29.248 3.085   8.956   1.00 23.92  ? 334  ALA A CB    1 
ATOM   2466 N N     . PHE A 1 356 ? 30.847 5.767   9.559   1.00 20.60  ? 335  PHE A N     1 
ATOM   2467 C CA    . PHE A 1 356 ? 31.368 7.068   9.167   1.00 21.89  ? 335  PHE A CA    1 
ATOM   2468 C C     . PHE A 1 356 ? 32.479 6.851   8.142   1.00 23.44  ? 335  PHE A C     1 
ATOM   2469 O O     . PHE A 1 356 ? 33.252 5.908   8.317   1.00 22.88  ? 335  PHE A O     1 
ATOM   2470 C CB    . PHE A 1 356 ? 31.880 7.845   10.385  1.00 23.03  ? 335  PHE A CB    1 
ATOM   2471 C CG    . PHE A 1 356 ? 30.777 8.288   11.332  1.00 23.90  ? 335  PHE A CG    1 
ATOM   2472 C CD1   . PHE A 1 356 ? 30.320 7.460   12.348  1.00 25.05  ? 335  PHE A CD1   1 
ATOM   2473 C CD2   . PHE A 1 356 ? 30.162 9.523   11.162  1.00 27.72  ? 335  PHE A CD2   1 
ATOM   2474 C CE1   . PHE A 1 356 ? 29.273 7.871   13.165  1.00 25.59  ? 335  PHE A CE1   1 
ATOM   2475 C CE2   . PHE A 1 356 ? 29.170 9.948   12.026  1.00 26.79  ? 335  PHE A CE2   1 
ATOM   2476 C CZ    . PHE A 1 356 ? 28.705 9.101   13.000  1.00 27.59  ? 335  PHE A CZ    1 
ATOM   2477 N N     . LEU A 1 357 ? 32.517 7.714   7.109   1.00 22.73  ? 336  LEU A N     1 
ATOM   2478 C CA    . LEU A 1 357 ? 33.476 7.635   6.003   1.00 25.76  ? 336  LEU A CA    1 
ATOM   2479 C C     . LEU A 1 357 ? 33.521 8.972   5.274   1.00 24.52  ? 336  LEU A C     1 
ATOM   2480 O O     . LEU A 1 357 ? 32.733 9.867   5.577   1.00 22.33  ? 336  LEU A O     1 
ATOM   2481 C CB    . LEU A 1 357 ? 33.132 6.522   5.008   1.00 25.97  ? 336  LEU A CB    1 
ATOM   2482 C CG    . LEU A 1 357 ? 31.879 6.752   4.151   1.00 26.35  ? 336  LEU A CG    1 
ATOM   2483 C CD1   . LEU A 1 357 ? 31.967 5.942   2.888   1.00 26.59  ? 336  LEU A CD1   1 
ATOM   2484 C CD2   . LEU A 1 357 ? 30.589 6.401   4.925   1.00 28.69  ? 336  LEU A CD2   1 
ATOM   2485 N N     . ARG A 1 358 ? 34.467 9.109   4.330   1.00 23.52  ? 337  ARG A N     1 
ATOM   2486 C CA    . ARG A 1 358 ? 34.504 10.227  3.405   1.00 23.68  ? 337  ARG A CA    1 
ATOM   2487 C C     . ARG A 1 358 ? 34.111 9.804   1.990   1.00 25.25  ? 337  ARG A C     1 
ATOM   2488 O O     . ARG A 1 358 ? 34.511 8.753   1.493   1.00 24.77  ? 337  ARG A O     1 
ATOM   2489 C CB    . ARG A 1 358 ? 35.919 10.818  3.390   1.00 26.99  ? 337  ARG A CB    1 
ATOM   2490 C CG    . ARG A 1 358 ? 36.371 11.366  4.734   1.00 28.00  ? 337  ARG A CG    1 
ATOM   2491 C CD    . ARG A 1 358 ? 37.738 12.074  4.662   1.00 29.00  ? 337  ARG A CD    1 
ATOM   2492 N NE    . ARG A 1 358 ? 37.786 13.027  3.557   1.00 30.58  ? 337  ARG A NE    1 
ATOM   2493 C CZ    . ARG A 1 358 ? 37.700 14.351  3.685   1.00 36.38  ? 337  ARG A CZ    1 
ATOM   2494 N NH1   . ARG A 1 358 ? 37.536 14.908  4.868   1.00 38.93  ? 337  ARG A NH1   1 
ATOM   2495 N NH2   . ARG A 1 358 ? 37.734 15.126  2.629   1.00 36.95  ? 337  ARG A NH2   1 
ATOM   2496 N N     . ALA A 1 359 ? 33.329 10.647  1.321   1.00 26.11  ? 338  ALA A N     1 
ATOM   2497 C CA    . ALA A 1 359 ? 32.984 10.432  -0.077  1.00 26.83  ? 338  ALA A CA    1 
ATOM   2498 C C     . ALA A 1 359 ? 34.240 10.251  -0.936  1.00 32.97  ? 338  ALA A C     1 
ATOM   2499 O O     . ALA A 1 359 ? 34.217 9.467   -1.878  1.00 30.99  ? 338  ALA A O     1 
ATOM   2500 C CB    . ALA A 1 359 ? 32.147 11.573  -0.593  1.00 25.45  ? 338  ALA A CB    1 
ATOM   2501 N N     . ASP A 1 360 ? 35.328 10.972  -0.629  1.00 33.44  ? 339  ASP A N     1 
ATOM   2502 C CA    . ASP A 1 360 ? 36.556 10.870  -1.412  1.00 33.58  ? 339  ASP A CA    1 
ATOM   2503 C C     . ASP A 1 360 ? 37.471 9.732   -0.952  1.00 36.70  ? 339  ASP A C     1 
ATOM   2504 O O     . ASP A 1 360 ? 38.539 9.548   -1.508  1.00 37.89  ? 339  ASP A O     1 
ATOM   2505 C CB    . ASP A 1 360 ? 37.352 12.167  -1.351  1.00 33.17  ? 339  ASP A CB    1 
ATOM   2506 C CG    . ASP A 1 360 ? 37.912 12.552  0.007   1.00 32.29  ? 339  ASP A CG    1 
ATOM   2507 O OD1   . ASP A 1 360 ? 37.963 11.699  0.919   1.00 31.19  ? 339  ASP A OD1   1 
ATOM   2508 O OD2   . ASP A 1 360 ? 38.281 13.721  0.156   1.00 34.17  ? 339  ASP A OD2   1 
ATOM   2509 N N     . GLY A 1 361 ? 37.105 8.987   0.085   1.00 38.15  ? 340  GLY A N     1 
ATOM   2510 C CA    . GLY A 1 361 ? 37.875 7.826   0.479   1.00 38.51  ? 340  GLY A CA    1 
ATOM   2511 C C     . GLY A 1 361 ? 39.120 8.201   1.280   1.00 40.86  ? 340  GLY A C     1 
ATOM   2512 O O     . GLY A 1 361 ? 39.889 7.325   1.664   1.00 42.37  ? 340  GLY A O     1 
ATOM   2513 N N     . GLY A 1 362 ? 39.288 9.491   1.587   1.00 37.48  ? 341  GLY A N     1 
ATOM   2514 C CA    . GLY A 1 362 ? 40.495 9.980   2.233   1.00 38.66  ? 341  GLY A CA    1 
ATOM   2515 C C     . GLY A 1 362 ? 40.541 9.607   3.712   1.00 42.28  ? 341  GLY A C     1 
ATOM   2516 O O     . GLY A 1 362 ? 39.652 8.948   4.243   1.00 42.93  ? 341  GLY A O     1 
ATOM   2517 N N     . THR A 1 363 ? 41.624 10.001  4.378   1.00 41.10  ? 342  THR A N     1 
ATOM   2518 C CA    . THR A 1 363 ? 41.606 10.060  5.821   1.00 43.16  ? 342  THR A CA    1 
ATOM   2519 C C     . THR A 1 363 ? 41.205 11.496  6.152   1.00 42.70  ? 342  THR A C     1 
ATOM   2520 O O     . THR A 1 363 ? 40.997 12.344  5.263   1.00 45.52  ? 342  THR A O     1 
ATOM   2521 C CB    . THR A 1 363 ? 42.940 9.625   6.435   1.00 52.12  ? 342  THR A CB    1 
ATOM   2522 O OG1   . THR A 1 363 ? 43.905 10.581  6.024   1.00 53.49  ? 342  THR A OG1   1 
ATOM   2523 C CG2   . THR A 1 363 ? 43.411 8.264   5.955   1.00 51.34  ? 342  THR A CG2   1 
ATOM   2524 N N     . GLY A 1 364 ? 41.043 11.756  7.436   1.00 39.32  ? 343  GLY A N     1 
ATOM   2525 C CA    . GLY A 1 364 ? 40.425 13.012  7.821   1.00 37.94  ? 343  GLY A CA    1 
ATOM   2526 C C     . GLY A 1 364 ? 38.967 12.787  8.201   1.00 33.18  ? 343  GLY A C     1 
ATOM   2527 O O     . GLY A 1 364 ? 38.403 11.723  7.957   1.00 25.27  ? 343  GLY A O     1 
ATOM   2528 N N     . ALA A 1 365 ? 38.392 13.818  8.810   1.00 30.77  ? 344  ALA A N     1 
ATOM   2529 C CA    . ALA A 1 365 ? 37.072 13.773  9.398   1.00 26.48  ? 344  ALA A CA    1 
ATOM   2530 C C     . ALA A 1 365 ? 36.018 13.370  8.371   1.00 23.03  ? 344  ALA A C     1 
ATOM   2531 O O     . ALA A 1 365 ? 36.040 13.805  7.216   1.00 21.29  ? 344  ALA A O     1 
ATOM   2532 C CB    . ALA A 1 365 ? 36.797 15.142  9.985   1.00 28.09  ? 344  ALA A CB    1 
ATOM   2533 N N     . PRO A 1 366 ? 34.990 12.593  8.776   1.00 23.16  ? 345  PRO A N     1 
ATOM   2534 C CA    . PRO A 1 366 ? 33.984 12.112  7.820   1.00 21.79  ? 345  PRO A CA    1 
ATOM   2535 C C     . PRO A 1 366 ? 33.042 13.189  7.285   1.00 21.06  ? 345  PRO A C     1 
ATOM   2536 O O     . PRO A 1 366 ? 32.736 14.155  7.985   1.00 21.78  ? 345  PRO A O     1 
ATOM   2537 C CB    . PRO A 1 366 ? 33.265 11.018  8.648   1.00 23.10  ? 345  PRO A CB    1 
ATOM   2538 C CG    . PRO A 1 366 ? 33.442 11.411  10.089  1.00 23.55  ? 345  PRO A CG    1 
ATOM   2539 C CD    . PRO A 1 366 ? 34.757 12.150  10.149  1.00 23.75  ? 345  PRO A CD    1 
ATOM   2540 N N     . ASP A 1 367 ? 32.615 13.053  6.019   1.00 20.93  ? 346  ASP A N     1 
ATOM   2541 C CA    . ASP A 1 367 ? 31.550 13.880  5.484   1.00 22.51  ? 346  ASP A CA    1 
ATOM   2542 C C     . ASP A 1 367 ? 30.291 13.058  5.170   1.00 20.92  ? 346  ASP A C     1 
ATOM   2543 O O     . ASP A 1 367 ? 29.307 13.608  4.676   1.00 20.94  ? 346  ASP A O     1 
ATOM   2544 C CB    . ASP A 1 367 ? 31.988 14.654  4.260   1.00 26.35  ? 346  ASP A CB    1 
ATOM   2545 C CG    . ASP A 1 367 ? 32.479 13.817  3.087   1.00 27.50  ? 346  ASP A CG    1 
ATOM   2546 O OD1   . ASP A 1 367 ? 32.404 12.580  3.155   1.00 25.73  ? 346  ASP A OD1   1 
ATOM   2547 O OD2   . ASP A 1 367 ? 33.037 14.415  2.154   1.00 35.09  ? 346  ASP A OD2   1 
ATOM   2548 N N     . LEU A 1 368 ? 30.329 11.752  5.463   1.00 21.66  ? 347  LEU A N     1 
ATOM   2549 C CA    . LEU A 1 368 ? 29.185 10.864  5.276   1.00 21.71  ? 347  LEU A CA    1 
ATOM   2550 C C     . LEU A 1 368 ? 28.976 10.034  6.531   1.00 21.07  ? 347  LEU A C     1 
ATOM   2551 O O     . LEU A 1 368 ? 29.928 9.498   7.100   1.00 17.86  ? 347  LEU A O     1 
ATOM   2552 C CB    . LEU A 1 368 ? 29.418 9.929   4.089   1.00 22.56  ? 347  LEU A CB    1 
ATOM   2553 C CG    . LEU A 1 368 ? 29.195 10.520  2.698   1.00 23.82  ? 347  LEU A CG    1 
ATOM   2554 C CD1   . LEU A 1 368 ? 29.762 9.559   1.645   1.00 23.69  ? 347  LEU A CD1   1 
ATOM   2555 C CD2   . LEU A 1 368 ? 27.752 10.826  2.376   1.00 24.66  ? 347  LEU A CD2   1 
ATOM   2556 N N     . GLU A 1 369 ? 27.697 9.799   6.848   1.00 20.72  ? 348  GLU A N     1 
ATOM   2557 C CA    . GLU A 1 369 ? 27.323 8.811   7.839   1.00 20.69  ? 348  GLU A CA    1 
ATOM   2558 C C     . GLU A 1 369 ? 26.339 7.845   7.201   1.00 18.59  ? 348  GLU A C     1 
ATOM   2559 O O     . GLU A 1 369 ? 25.541 8.283   6.382   1.00 18.96  ? 348  GLU A O     1 
ATOM   2560 C CB    . GLU A 1 369 ? 26.663 9.483   9.046   1.00 22.20  ? 348  GLU A CB    1 
ATOM   2561 C CG    . GLU A 1 369 ? 26.227 8.513   10.144  1.00 25.24  ? 348  GLU A CG    1 
ATOM   2562 C CD    . GLU A 1 369 ? 25.538 9.212   11.325  1.00 31.21  ? 348  GLU A CD    1 
ATOM   2563 O OE1   . GLU A 1 369 ? 25.112 8.492   12.261  1.00 35.02  ? 348  GLU A OE1   1 
ATOM   2564 O OE2   . GLU A 1 369 ? 25.480 10.472  11.334  1.00 35.26  ? 348  GLU A OE2   1 
ATOM   2565 N N     . LEU A 1 370 ? 26.427 6.564   7.596   1.00 19.39  ? 349  LEU A N     1 
ATOM   2566 C CA    . LEU A 1 370 ? 25.480 5.538   7.185   1.00 20.78  ? 349  LEU A CA    1 
ATOM   2567 C C     . LEU A 1 370 ? 24.770 5.039   8.437   1.00 21.39  ? 349  LEU A C     1 
ATOM   2568 O O     . LEU A 1 370 ? 25.436 4.699   9.400   1.00 23.21  ? 349  LEU A O     1 
ATOM   2569 C CB    . LEU A 1 370 ? 26.195 4.400   6.464   1.00 24.19  ? 349  LEU A CB    1 
ATOM   2570 C CG    . LEU A 1 370 ? 27.119 4.815   5.316   1.00 27.17  ? 349  LEU A CG    1 
ATOM   2571 C CD1   . LEU A 1 370 ? 27.842 3.644   4.717   1.00 30.78  ? 349  LEU A CD1   1 
ATOM   2572 C CD2   . LEU A 1 370 ? 26.372 5.585   4.236   1.00 26.84  ? 349  LEU A CD2   1 
ATOM   2573 N N     . ILE A 1 371 ? 23.429 5.068   8.436   1.00 19.51  ? 350  ILE A N     1 
ATOM   2574 C CA    . ILE A 1 371 ? 22.648 4.586   9.565   1.00 19.58  ? 350  ILE A CA    1 
ATOM   2575 C C     . ILE A 1 371 ? 21.916 3.334   9.115   1.00 18.49  ? 350  ILE A C     1 
ATOM   2576 O O     . ILE A 1 371 ? 21.179 3.367   8.134   1.00 19.58  ? 350  ILE A O     1 
ATOM   2577 C CB    . ILE A 1 371 ? 21.654 5.647   10.086  1.00 20.71  ? 350  ILE A CB    1 
ATOM   2578 C CG1   . ILE A 1 371 ? 22.353 6.950   10.441  1.00 19.88  ? 350  ILE A CG1   1 
ATOM   2579 C CG2   . ILE A 1 371 ? 20.852 5.071   11.264  1.00 20.97  ? 350  ILE A CG2   1 
ATOM   2580 C CD1   . ILE A 1 371 ? 21.448 8.143   10.674  1.00 21.39  ? 350  ILE A CD1   1 
ATOM   2581 N N     . TRP A 1 372 ? 22.089 2.263   9.899   1.00 18.70  ? 351  TRP A N     1 
ATOM   2582 C CA    . TRP A 1 372 ? 21.433 0.987   9.713   1.00 17.78  ? 351  TRP A CA    1 
ATOM   2583 C C     . TRP A 1 372 ? 20.149 0.937   10.527  1.00 17.63  ? 351  TRP A C     1 
ATOM   2584 O O     . TRP A 1 372 ? 20.183 1.103   11.746  1.00 20.74  ? 351  TRP A O     1 
ATOM   2585 C CB    . TRP A 1 372 ? 22.358 -0.145  10.178  1.00 17.57  ? 351  TRP A CB    1 
ATOM   2586 C CG    . TRP A 1 372 ? 21.729 -1.506  10.076  1.00 18.19  ? 351  TRP A CG    1 
ATOM   2587 C CD1   . TRP A 1 372 ? 21.269 -2.285  11.099  1.00 19.35  ? 351  TRP A CD1   1 
ATOM   2588 C CD2   . TRP A 1 372 ? 21.524 -2.263  8.873   1.00 17.04  ? 351  TRP A CD2   1 
ATOM   2589 N NE1   . TRP A 1 372 ? 20.798 -3.469  10.606  1.00 19.13  ? 351  TRP A NE1   1 
ATOM   2590 C CE2   . TRP A 1 372 ? 20.951 -3.488  9.254   1.00 19.06  ? 351  TRP A CE2   1 
ATOM   2591 C CE3   . TRP A 1 372 ? 21.789 -2.028  7.518   1.00 17.82  ? 351  TRP A CE3   1 
ATOM   2592 C CZ2   . TRP A 1 372 ? 20.621 -4.471  8.328   1.00 20.04  ? 351  TRP A CZ2   1 
ATOM   2593 C CZ3   . TRP A 1 372 ? 21.452 -2.996  6.610   1.00 19.11  ? 351  TRP A CZ3   1 
ATOM   2594 C CH2   . TRP A 1 372 ? 20.914 -4.206  7.015   1.00 19.70  ? 351  TRP A CH2   1 
ATOM   2595 N N     . ALA A 1 373 ? 19.053 0.669   9.830   1.00 19.29  ? 352  ALA A N     1 
ATOM   2596 C CA    . ALA A 1 373 ? 17.759 0.412   10.439  1.00 19.54  ? 352  ALA A CA    1 
ATOM   2597 C C     . ALA A 1 373 ? 17.247 -0.902  9.859   1.00 20.80  ? 352  ALA A C     1 
ATOM   2598 O O     . ALA A 1 373 ? 17.035 -0.977  8.647   1.00 23.75  ? 352  ALA A O     1 
ATOM   2599 C CB    . ALA A 1 373 ? 16.847 1.579   10.175  1.00 17.85  ? 352  ALA A CB    1 
ATOM   2600 N N     . PRO A 1 374 ? 17.113 -1.994  10.647  1.00 20.07  ? 353  PRO A N     1 
ATOM   2601 C CA    . PRO A 1 374 ? 16.591 -3.247  10.089  1.00 20.88  ? 353  PRO A CA    1 
ATOM   2602 C C     . PRO A 1 374 ? 15.070 -3.244  9.928   1.00 20.85  ? 353  PRO A C     1 
ATOM   2603 O O     . PRO A 1 374 ? 14.345 -4.016  10.553  1.00 22.49  ? 353  PRO A O     1 
ATOM   2604 C CB    . PRO A 1 374 ? 17.167 -4.303  11.027  1.00 20.02  ? 353  PRO A CB    1 
ATOM   2605 C CG    . PRO A 1 374 ? 17.273 -3.598  12.360  1.00 21.13  ? 353  PRO A CG    1 
ATOM   2606 C CD    . PRO A 1 374 ? 17.542 -2.134  12.040  1.00 20.88  ? 353  PRO A CD    1 
ATOM   2607 N N     . VAL A 1 375 ? 14.615 -2.332  9.056   1.00 21.24  ? 354  VAL A N     1 
ATOM   2608 C CA    . VAL A 1 375 ? 13.215 -2.168  8.721   1.00 24.10  ? 354  VAL A CA    1 
ATOM   2609 C C     . VAL A 1 375 ? 13.217 -1.384  7.421   1.00 23.87  ? 354  VAL A C     1 
ATOM   2610 O O     . VAL A 1 375 ? 14.252 -0.824  7.070   1.00 23.43  ? 354  VAL A O     1 
ATOM   2611 C CB    . VAL A 1 375 ? 12.466 -1.429  9.847   1.00 24.48  ? 354  VAL A CB    1 
ATOM   2612 C CG1   . VAL A 1 375 ? 12.922 0.020   9.901   1.00 26.43  ? 354  VAL A CG1   1 
ATOM   2613 C CG2   . VAL A 1 375 ? 10.956 -1.540  9.717   1.00 26.77  ? 354  VAL A CG2   1 
ATOM   2614 N N     . ALA A 1 376 ? 12.069 -1.324  6.736   1.00 23.06  ? 355  ALA A N     1 
ATOM   2615 C CA    . ALA A 1 376 ? 11.915 -0.479  5.573   1.00 26.23  ? 355  ALA A CA    1 
ATOM   2616 C C     . ALA A 1 376 ? 10.579 0.236   5.686   1.00 26.97  ? 355  ALA A C     1 
ATOM   2617 O O     . ALA A 1 376 ? 9.575  -0.393  5.983   1.00 28.33  ? 355  ALA A O     1 
ATOM   2618 C CB    . ALA A 1 376 ? 12.008 -1.305  4.285   1.00 24.92  ? 355  ALA A CB    1 
ATOM   2619 N N     . ASP A 1 377 ? 10.593 1.542   5.411   1.00 27.06  ? 356  ASP A N     1 
ATOM   2620 C CA    . ASP A 1 377 ? 9.378  2.316   5.235   1.00 27.21  ? 356  ASP A CA    1 
ATOM   2621 C C     . ASP A 1 377 ? 8.842  2.115   3.825   1.00 26.05  ? 356  ASP A C     1 
ATOM   2622 O O     . ASP A 1 377 ? 9.104  2.908   2.913   1.00 27.58  ? 356  ASP A O     1 
ATOM   2623 C CB    . ASP A 1 377 ? 9.656  3.784   5.457   1.00 30.44  ? 356  ASP A CB    1 
ATOM   2624 C CG    . ASP A 1 377 ? 8.400  4.625   5.400   1.00 31.69  ? 356  ASP A CG    1 
ATOM   2625 O OD1   . ASP A 1 377 ? 7.305  4.026   5.304   1.00 34.83  ? 356  ASP A OD1   1 
ATOM   2626 O OD2   . ASP A 1 377 ? 8.551  5.837   5.450   1.00 38.97  ? 356  ASP A OD2   1 
ATOM   2627 N N     . SER A 1 378 ? 8.223  0.956   3.627   1.00 28.14  ? 357  SER A N     1 
ATOM   2628 C CA    . SER A 1 378 ? 7.848  0.485   2.300   1.00 28.90  ? 357  SER A CA    1 
ATOM   2629 C C     . SER A 1 378 ? 6.632  -0.423  2.449   1.00 28.08  ? 357  SER A C     1 
ATOM   2630 O O     . SER A 1 378 ? 6.759  -1.552  2.905   1.00 27.08  ? 357  SER A O     1 
ATOM   2631 C CB    . SER A 1 378 ? 8.970  -0.255  1.605   1.00 28.48  ? 357  SER A CB    1 
ATOM   2632 O OG    . SER A 1 378 ? 8.482  -1.072  0.530   1.00 27.49  ? 357  SER A OG    1 
ATOM   2633 N N     . GLU A 1 379 ? 5.485  0.055   2.002   1.00 30.39  ? 358  GLU A N     1 
ATOM   2634 C CA    . GLU A 1 379 ? 4.254  -0.724  2.062   1.00 33.00  ? 358  GLU A CA    1 
ATOM   2635 C C     . GLU A 1 379 ? 4.304  -1.906  1.099   1.00 32.65  ? 358  GLU A C     1 
ATOM   2636 O O     . GLU A 1 379 ? 3.747  -2.963  1.382   1.00 32.40  ? 358  GLU A O     1 
ATOM   2637 C CB    . GLU A 1 379 ? 3.089  0.207   1.731   1.00 38.10  ? 358  GLU A CB    1 
ATOM   2638 C CG    . GLU A 1 379 ? 2.912  1.279   2.801   1.00 47.56  ? 358  GLU A CG    1 
ATOM   2639 C CD    . GLU A 1 379 ? 1.445  1.542   3.086   1.00 61.46  ? 358  GLU A CD    1 
ATOM   2640 O OE1   . GLU A 1 379 ? 0.803  2.306   2.327   1.00 63.55  ? 358  GLU A OE1   1 
ATOM   2641 O OE2   . GLU A 1 379 ? 0.935  0.907   4.035   1.00 68.42  ? 358  GLU A OE2   1 
ATOM   2642 N N     . ALA A 1 380 ? 5.026  -1.746  -0.011  1.00 34.65  ? 359  ALA A N     1 
ATOM   2643 C CA    . ALA A 1 380 ? 5.176  -2.818  -0.981  1.00 37.03  ? 359  ALA A CA    1 
ATOM   2644 C C     . ALA A 1 380 ? 5.663  -4.100  -0.314  1.00 37.72  ? 359  ALA A C     1 
ATOM   2645 O O     . ALA A 1 380 ? 5.257  -5.183  -0.730  1.00 36.39  ? 359  ALA A O     1 
ATOM   2646 C CB    . ALA A 1 380 ? 6.117  -2.397  -2.108  1.00 38.66  ? 359  ALA A CB    1 
ATOM   2647 N N     . VAL A 1 381 ? 6.548  -4.003  0.691   1.00 31.80  ? 360  VAL A N     1 
ATOM   2648 C CA    . VAL A 1 381 ? 7.044  -5.212  1.339   1.00 29.64  ? 360  VAL A CA    1 
ATOM   2649 C C     . VAL A 1 381 ? 6.523  -5.343  2.768   1.00 28.54  ? 360  VAL A C     1 
ATOM   2650 O O     . VAL A 1 381 ? 7.023  -6.165  3.525   1.00 31.57  ? 360  VAL A O     1 
ATOM   2651 C CB    . VAL A 1 381 ? 8.584  -5.274  1.257   1.00 31.65  ? 360  VAL A CB    1 
ATOM   2652 C CG1   . VAL A 1 381 ? 9.045  -5.338  -0.199  1.00 33.34  ? 360  VAL A CG1   1 
ATOM   2653 C CG2   . VAL A 1 381 ? 9.268  -4.128  1.996   1.00 28.91  ? 360  VAL A CG2   1 
ATOM   2654 N N     . GLY A 1 382 ? 5.501  -4.561  3.135   1.00 30.76  ? 361  GLY A N     1 
ATOM   2655 C CA    . GLY A 1 382 ? 4.886  -4.654  4.451   1.00 28.87  ? 361  GLY A CA    1 
ATOM   2656 C C     . GLY A 1 382 ? 5.883  -4.283  5.556   1.00 29.11  ? 361  GLY A C     1 
ATOM   2657 O O     . GLY A 1 382 ? 5.864  -4.840  6.646   1.00 29.04  ? 361  GLY A O     1 
ATOM   2658 N N     . GLY A 1 383 ? 6.839  -3.400  5.233   1.00 29.43  ? 362  GLY A N     1 
ATOM   2659 C CA    . GLY A 1 383 ? 7.889  -3.049  6.178   1.00 29.87  ? 362  GLY A CA    1 
ATOM   2660 C C     . GLY A 1 383 ? 9.036  -4.061  6.266   1.00 26.79  ? 362  GLY A C     1 
ATOM   2661 O O     . GLY A 1 383 ? 10.031 -3.769  6.937   1.00 26.89  ? 362  GLY A O     1 
ATOM   2662 N N     . GLN A 1 384 ? 8.935  -5.206  5.572   1.00 26.36  ? 363  GLN A N     1 
ATOM   2663 C CA    . GLN A 1 384 ? 9.927  -6.262  5.683   1.00 24.86  ? 363  GLN A CA    1 
ATOM   2664 C C     . GLN A 1 384 ? 11.073 -6.029  4.705   1.00 25.53  ? 363  GLN A C     1 
ATOM   2665 O O     . GLN A 1 384 ? 11.226 -6.680  3.664   1.00 22.43  ? 363  GLN A O     1 
ATOM   2666 C CB    . GLN A 1 384 ? 9.225  -7.604  5.539   1.00 32.16  ? 363  GLN A CB    1 
ATOM   2667 C CG    . GLN A 1 384 ? 8.188  -7.794  6.645   1.00 37.94  ? 363  GLN A CG    1 
ATOM   2668 C CD    . GLN A 1 384 ? 7.405  -9.062  6.465   1.00 42.68  ? 363  GLN A CD    1 
ATOM   2669 O OE1   . GLN A 1 384 ? 6.798  -9.292  5.417   1.00 51.57  ? 363  GLN A OE1   1 
ATOM   2670 N NE2   . GLN A 1 384 ? 7.469  -9.914  7.466   1.00 51.47  ? 363  GLN A NE2   1 
ATOM   2671 N N     . GLY A 1 385 ? 11.875 -5.039  5.065   1.00 24.27  ? 364  GLY A N     1 
ATOM   2672 C CA    . GLY A 1 385 ? 13.046 -4.649  4.304   1.00 23.95  ? 364  GLY A CA    1 
ATOM   2673 C C     . GLY A 1 385 ? 14.097 -4.124  5.270   1.00 21.50  ? 364  GLY A C     1 
ATOM   2674 O O     . GLY A 1 385 ? 13.861 -4.136  6.481   1.00 21.83  ? 364  GLY A O     1 
ATOM   2675 N N     . LEU A 1 386 ? 15.254 -3.731  4.726   1.00 23.25  ? 365  LEU A N     1 
ATOM   2676 C CA    . LEU A 1 386 ? 16.403 -3.288  5.505   1.00 22.50  ? 365  LEU A CA    1 
ATOM   2677 C C     . LEU A 1 386 ? 16.882 -1.990  4.865   1.00 20.80  ? 365  LEU A C     1 
ATOM   2678 O O     . LEU A 1 386 ? 16.802 -1.873  3.637   1.00 20.16  ? 365  LEU A O     1 
ATOM   2679 C CB    . LEU A 1 386 ? 17.501 -4.344  5.536   1.00 21.44  ? 365  LEU A CB    1 
ATOM   2680 C CG    . LEU A 1 386 ? 17.094 -5.748  6.002   1.00 24.64  ? 365  LEU A CG    1 
ATOM   2681 C CD1   . LEU A 1 386 ? 18.246 -6.694  5.743   1.00 24.54  ? 365  LEU A CD1   1 
ATOM   2682 C CD2   . LEU A 1 386 ? 16.726 -5.828  7.469   1.00 24.38  ? 365  LEU A CD2   1 
ATOM   2683 N N     . THR A 1 387 ? 17.243 -1.007  5.716   1.00 20.18  ? 366  THR A N     1 
ATOM   2684 C CA    . THR A 1 387 ? 17.563 0.341   5.267   1.00 20.54  ? 366  THR A CA    1 
ATOM   2685 C C     . THR A 1 387 ? 18.977 0.725   5.726   1.00 19.64  ? 366  THR A C     1 
ATOM   2686 O O     . THR A 1 387 ? 19.327 0.564   6.886   1.00 19.31  ? 366  THR A O     1 
ATOM   2687 C CB    . THR A 1 387 ? 16.572 1.374   5.816   1.00 20.57  ? 366  THR A CB    1 
ATOM   2688 O OG1   . THR A 1 387 ? 15.291 0.980   5.346   1.00 20.32  ? 366  THR A OG1   1 
ATOM   2689 C CG2   . THR A 1 387 ? 16.902 2.784   5.342   1.00 21.51  ? 366  THR A CG2   1 
ATOM   2690 N N     . ILE A 1 388 ? 19.719 1.355   4.804   1.00 20.79  ? 367  ILE A N     1 
ATOM   2691 C CA    . ILE A 1 388 ? 20.902 2.146   5.107   1.00 20.92  ? 367  ILE A CA    1 
ATOM   2692 C C     . ILE A 1 388 ? 20.546 3.576   4.763   1.00 20.14  ? 367  ILE A C     1 
ATOM   2693 O O     . ILE A 1 388 ? 20.353 3.892   3.593   1.00 19.08  ? 367  ILE A O     1 
ATOM   2694 C CB    . ILE A 1 388 ? 22.153 1.687   4.333   1.00 21.41  ? 367  ILE A CB    1 
ATOM   2695 C CG1   . ILE A 1 388 ? 22.538 0.261   4.750   1.00 21.07  ? 367  ILE A CG1   1 
ATOM   2696 C CG2   . ILE A 1 388 ? 23.320 2.664   4.535   1.00 21.60  ? 367  ILE A CG2   1 
ATOM   2697 C CD1   . ILE A 1 388 ? 23.628 -0.382  3.902   1.00 21.13  ? 367  ILE A CD1   1 
ATOM   2698 N N     . ALA A 1 389 ? 20.418 4.414   5.799   1.00 18.85  ? 368  ALA A N     1 
ATOM   2699 C CA    . ALA A 1 389 ? 20.241 5.841   5.578   1.00 20.01  ? 368  ALA A CA    1 
ATOM   2700 C C     . ALA A 1 389 ? 21.604 6.475   5.300   1.00 19.26  ? 368  ALA A C     1 
ATOM   2701 O O     . ALA A 1 389 ? 22.539 6.323   6.082   1.00 18.31  ? 368  ALA A O     1 
ATOM   2702 C CB    . ALA A 1 389 ? 19.526 6.496   6.755   1.00 20.66  ? 368  ALA A CB    1 
ATOM   2703 N N     . VAL A 1 390 ? 21.707 7.179   4.167   1.00 18.46  ? 369  VAL A N     1 
ATOM   2704 C CA    . VAL A 1 390 ? 22.933 7.859   3.746   1.00 20.10  ? 369  VAL A CA    1 
ATOM   2705 C C     . VAL A 1 390 ? 22.815 9.345   4.080   1.00 19.16  ? 369  VAL A C     1 
ATOM   2706 O O     . VAL A 1 390 ? 21.959 10.038  3.528   1.00 18.94  ? 369  VAL A O     1 
ATOM   2707 C CB    . VAL A 1 390 ? 23.167 7.713   2.229   1.00 21.29  ? 369  VAL A CB    1 
ATOM   2708 C CG1   . VAL A 1 390 ? 24.392 8.497   1.763   1.00 22.22  ? 369  VAL A CG1   1 
ATOM   2709 C CG2   . VAL A 1 390 ? 23.261 6.251   1.813   1.00 22.70  ? 369  VAL A CG2   1 
ATOM   2710 N N     . VAL A 1 391 ? 23.760 9.839   4.889   1.00 20.42  ? 370  VAL A N     1 
ATOM   2711 C CA    . VAL A 1 391 ? 23.619 11.117  5.569   1.00 19.68  ? 370  VAL A CA    1 
ATOM   2712 C C     . VAL A 1 391 ? 24.728 12.067  5.111   1.00 19.79  ? 370  VAL A C     1 
ATOM   2713 O O     . VAL A 1 391 ? 25.908 11.756  5.244   1.00 20.15  ? 370  VAL A O     1 
ATOM   2714 C CB    . VAL A 1 391 ? 23.688 10.970  7.099   1.00 18.76  ? 370  VAL A CB    1 
ATOM   2715 C CG1   . VAL A 1 391 ? 23.548 12.324  7.780   1.00 20.02  ? 370  VAL A CG1   1 
ATOM   2716 C CG2   . VAL A 1 391 ? 22.688 9.986   7.671   1.00 16.89  ? 370  VAL A CG2   1 
ATOM   2717 N N     . LEU A 1 392 ? 24.329 13.245  4.630   1.00 20.48  ? 371  LEU A N     1 
ATOM   2718 C CA    . LEU A 1 392 ? 25.258 14.315  4.271   1.00 19.84  ? 371  LEU A CA    1 
ATOM   2719 C C     . LEU A 1 392 ? 25.601 15.067  5.545   1.00 21.29  ? 371  LEU A C     1 
ATOM   2720 O O     . LEU A 1 392 ? 24.749 15.812  6.040   1.00 20.58  ? 371  LEU A O     1 
ATOM   2721 C CB    . LEU A 1 392 ? 24.486 15.190  3.284   1.00 21.50  ? 371  LEU A CB    1 
ATOM   2722 C CG    . LEU A 1 392 ? 25.167 16.462  2.764   1.00 24.14  ? 371  LEU A CG    1 
ATOM   2723 C CD1   . LEU A 1 392 ? 26.161 16.102  1.668   1.00 24.94  ? 371  LEU A CD1   1 
ATOM   2724 C CD2   . LEU A 1 392 ? 24.129 17.452  2.264   1.00 26.54  ? 371  LEU A CD2   1 
ATOM   2725 N N     . LEU A 1 393 ? 26.809 14.848  6.080   1.00 21.65  ? 372  LEU A N     1 
ATOM   2726 C CA    . LEU A 1 393 ? 27.174 15.348  7.407   1.00 22.40  ? 372  LEU A CA    1 
ATOM   2727 C C     . LEU A 1 393 ? 27.630 16.793  7.361   1.00 20.93  ? 372  LEU A C     1 
ATOM   2728 O O     . LEU A 1 393 ? 27.568 17.477  8.380   1.00 20.89  ? 372  LEU A O     1 
ATOM   2729 C CB    . LEU A 1 393 ? 28.298 14.548  8.046   1.00 23.99  ? 372  LEU A CB    1 
ATOM   2730 C CG    . LEU A 1 393 ? 27.960 13.173  8.597   1.00 22.70  ? 372  LEU A CG    1 
ATOM   2731 C CD1   . LEU A 1 393 ? 29.279 12.610  9.086   1.00 24.08  ? 372  LEU A CD1   1 
ATOM   2732 C CD2   . LEU A 1 393 ? 26.894 13.212  9.694   1.00 22.86  ? 372  LEU A CD2   1 
ATOM   2733 N N     . GLN A 1 394 ? 28.155 17.238  6.219   1.00 21.70  ? 373  GLN A N     1 
ATOM   2734 C CA    . GLN A 1 394 ? 28.712 18.583  6.128   1.00 22.56  ? 373  GLN A CA    1 
ATOM   2735 C C     . GLN A 1 394 ? 28.156 19.298  4.909   1.00 22.06  ? 373  GLN A C     1 
ATOM   2736 O O     . GLN A 1 394 ? 28.875 19.603  3.968   1.00 22.48  ? 373  GLN A O     1 
ATOM   2737 C CB    . GLN A 1 394 ? 30.236 18.525  6.112   1.00 24.32  ? 373  GLN A CB    1 
ATOM   2738 C CG    . GLN A 1 394 ? 30.836 17.972  7.395   1.00 21.62  ? 373  GLN A CG    1 
ATOM   2739 C CD    . GLN A 1 394 ? 30.877 18.962  8.544   1.00 23.28  ? 373  GLN A CD    1 
ATOM   2740 O OE1   . GLN A 1 394 ? 31.828 19.736  8.699   1.00 22.81  ? 373  GLN A OE1   1 
ATOM   2741 N NE2   . GLN A 1 394 ? 29.872 18.916  9.414   1.00 21.97  ? 373  GLN A NE2   1 
ATOM   2742 N N     . PRO A 1 395 ? 26.858 19.667  4.908   1.00 21.14  ? 374  PRO A N     1 
ATOM   2743 C CA    . PRO A 1 395 ? 26.258 20.311  3.745   1.00 21.00  ? 374  PRO A CA    1 
ATOM   2744 C C     . PRO A 1 395 ? 26.897 21.665  3.450   1.00 22.94  ? 374  PRO A C     1 
ATOM   2745 O O     . PRO A 1 395 ? 27.288 22.366  4.382   1.00 21.89  ? 374  PRO A O     1 
ATOM   2746 C CB    . PRO A 1 395 ? 24.815 20.468  4.191   1.00 20.95  ? 374  PRO A CB    1 
ATOM   2747 C CG    . PRO A 1 395 ? 24.911 20.536  5.684   1.00 20.51  ? 374  PRO A CG    1 
ATOM   2748 C CD    . PRO A 1 395 ? 25.888 19.463  5.998   1.00 21.05  ? 374  PRO A CD    1 
ATOM   2749 N N     . ASP A 1 396 ? 26.998 22.006  2.165   1.00 23.64  ? 375  ASP A N     1 
ATOM   2750 C CA    . ASP A 1 396 ? 27.357 23.358  1.750   1.00 25.79  ? 375  ASP A CA    1 
ATOM   2751 C C     . ASP A 1 396 ? 26.103 24.210  1.603   1.00 23.47  ? 375  ASP A C     1 
ATOM   2752 O O     . ASP A 1 396 ? 26.183 25.423  1.665   1.00 25.65  ? 375  ASP A O     1 
ATOM   2753 C CB    . ASP A 1 396 ? 28.153 23.359  0.461   1.00 27.54  ? 375  ASP A CB    1 
ATOM   2754 C CG    . ASP A 1 396 ? 29.584 22.878  0.642   1.00 31.39  ? 375  ASP A CG    1 
ATOM   2755 O OD1   . ASP A 1 396 ? 30.111 23.001  1.756   1.00 32.34  ? 375  ASP A OD1   1 
ATOM   2756 O OD2   . ASP A 1 396 ? 30.105 22.292  -0.294  1.00 40.09  ? 375  ASP A OD2   1 
ATOM   2757 N N     . SER A 1 397 ? 24.947 23.574  1.426   1.00 21.30  ? 376  SER A N     1 
ATOM   2758 C CA    . SER A 1 397 ? 23.682 24.286  1.316   1.00 21.77  ? 376  SER A CA    1 
ATOM   2759 C C     . SER A 1 397 ? 23.375 25.031  2.616   1.00 22.34  ? 376  SER A C     1 
ATOM   2760 O O     . SER A 1 397 ? 23.755 24.577  3.703   1.00 22.50  ? 376  SER A O     1 
ATOM   2761 C CB    . SER A 1 397 ? 22.567 23.349  0.979   1.00 23.28  ? 376  SER A CB    1 
ATOM   2762 O OG    . SER A 1 397 ? 22.753 22.741  -0.292  1.00 22.94  ? 376  SER A OG    1 
ATOM   2763 N N     . ARG A 1 398 ? 22.713 26.180  2.492   1.00 22.81  ? 377  ARG A N     1 
ATOM   2764 C CA    . ARG A 1 398 ? 22.314 26.958  3.663   1.00 25.35  ? 377  ARG A CA    1 
ATOM   2765 C C     . ARG A 1 398 ? 20.922 27.511  3.435   1.00 23.37  ? 377  ARG A C     1 
ATOM   2766 O O     . ARG A 1 398 ? 20.546 27.691  2.290   1.00 22.55  ? 377  ARG A O     1 
ATOM   2767 C CB    . ARG A 1 398 ? 23.178 28.196  3.897   1.00 25.00  ? 377  ARG A CB    1 
ATOM   2768 C CG    . ARG A 1 398 ? 24.597 27.857  4.292   1.00 24.93  ? 377  ARG A CG    1 
ATOM   2769 C CD    . ARG A 1 398 ? 24.672 27.403  5.707   1.00 24.79  ? 377  ARG A CD    1 
ATOM   2770 N NE    . ARG A 1 398 ? 26.079 27.159  6.044   1.00 27.81  ? 377  ARG A NE    1 
ATOM   2771 C CZ    . ARG A 1 398 ? 26.805 26.106  5.614   1.00 32.55  ? 377  ARG A CZ    1 
ATOM   2772 N NH1   . ARG A 1 398 ? 26.228 25.102  4.926   1.00 29.68  ? 377  ARG A NH1   1 
ATOM   2773 N NH2   . ARG A 1 398 ? 28.093 26.047  5.921   1.00 31.55  ? 377  ARG A NH2   1 
ATOM   2774 N N     . GLY A 1 399 ? 20.202 27.802  4.525   1.00 20.08  ? 378  GLY A N     1 
ATOM   2775 C CA    . GLY A 1 399 ? 18.859 28.359  4.421   1.00 20.42  ? 378  GLY A CA    1 
ATOM   2776 C C     . GLY A 1 399 ? 18.561 29.326  5.554   1.00 19.39  ? 378  GLY A C     1 
ATOM   2777 O O     . GLY A 1 399 ? 19.468 29.873  6.195   1.00 19.11  ? 378  GLY A O     1 
ATOM   2778 N N     . GLY A 1 400 ? 17.277 29.522  5.819   1.00 20.88  ? 379  GLY A N     1 
ATOM   2779 C CA    . GLY A 1 400 ? 16.917 30.397  6.914   1.00 22.15  ? 379  GLY A CA    1 
ATOM   2780 C C     . GLY A 1 400 ? 15.481 30.203  7.355   1.00 19.49  ? 379  GLY A C     1 
ATOM   2781 O O     . GLY A 1 400 ? 14.703 29.524  6.703   1.00 19.27  ? 379  GLY A O     1 
ATOM   2782 N N     . ILE A 1 401 ? 15.138 30.894  8.444   1.00 20.34  ? 380  ILE A N     1 
ATOM   2783 C CA    . ILE A 1 401 ? 13.783 30.955  8.975   1.00 18.61  ? 380  ILE A CA    1 
ATOM   2784 C C     . ILE A 1 401 ? 13.371 32.424  9.071   1.00 19.78  ? 380  ILE A C     1 
ATOM   2785 O O     . ILE A 1 401 ? 14.139 33.240  9.608   1.00 21.55  ? 380  ILE A O     1 
ATOM   2786 C CB    . ILE A 1 401 ? 13.752 30.294  10.357  1.00 17.86  ? 380  ILE A CB    1 
ATOM   2787 C CG1   . ILE A 1 401 ? 14.260 28.833  10.270  1.00 19.76  ? 380  ILE A CG1   1 
ATOM   2788 C CG2   . ILE A 1 401 ? 12.342 30.406  10.941  1.00 19.12  ? 380  ILE A CG2   1 
ATOM   2789 C CD1   . ILE A 1 401 ? 14.069 28.005  11.511  1.00 21.38  ? 380  ILE A CD1   1 
ATOM   2790 N N     . THR A 1 402 ? 12.178 32.738  8.570   1.00 20.77  ? 381  THR A N     1 
ATOM   2791 C CA    . THR A 1 402 ? 11.641 34.093  8.636   1.00 22.52  ? 381  THR A CA    1 
ATOM   2792 C C     . THR A 1 402 ? 10.212 34.039  9.192   1.00 23.51  ? 381  THR A C     1 
ATOM   2793 O O     . THR A 1 402 ? 9.608  32.976  9.251   1.00 21.32  ? 381  THR A O     1 
ATOM   2794 C CB    . THR A 1 402 ? 11.698 34.764  7.253   1.00 22.79  ? 381  THR A CB    1 
ATOM   2795 O OG1   . THR A 1 402 ? 10.937 33.946  6.378   1.00 22.44  ? 381  THR A OG1   1 
ATOM   2796 C CG2   . THR A 1 402 ? 13.115 34.939  6.740   1.00 24.69  ? 381  THR A CG2   1 
ATOM   2797 N N     . LEU A 1 403 ? 9.659  35.200  9.564   1.00 21.60  ? 382  LEU A N     1 
ATOM   2798 C CA    . LEU A 1 403 ? 8.283  35.247  10.028  1.00 23.27  ? 382  LEU A CA    1 
ATOM   2799 C C     . LEU A 1 403 ? 7.333  35.240  8.847   1.00 22.74  ? 382  LEU A C     1 
ATOM   2800 O O     . LEU A 1 403 ? 7.615  35.857  7.834   1.00 22.88  ? 382  LEU A O     1 
ATOM   2801 C CB    . LEU A 1 403 ? 8.020  36.484  10.875  1.00 23.37  ? 382  LEU A CB    1 
ATOM   2802 C CG    . LEU A 1 403 ? 8.843  36.593  12.158  1.00 24.61  ? 382  LEU A CG    1 
ATOM   2803 C CD1   . LEU A 1 403 ? 8.417  37.846  12.886  1.00 25.54  ? 382  LEU A CD1   1 
ATOM   2804 C CD2   . LEU A 1 403 ? 8.645  35.353  13.032  1.00 24.24  ? 382  LEU A CD2   1 
ATOM   2805 N N     . ALA A 1 404 ? 6.206  34.553  9.004   1.00 24.88  ? 383  ALA A N     1 
ATOM   2806 C CA    . ALA A 1 404 ? 5.109  34.630  8.044   1.00 27.13  ? 383  ALA A CA    1 
ATOM   2807 C C     . ALA A 1 404 ? 4.311  35.904  8.299   1.00 27.98  ? 383  ALA A C     1 
ATOM   2808 O O     . ALA A 1 404 ? 3.688  36.438  7.401   1.00 27.39  ? 383  ALA A O     1 
ATOM   2809 C CB    . ALA A 1 404 ? 4.206  33.398  8.142   1.00 27.70  ? 383  ALA A CB    1 
ATOM   2810 N N     . GLY A 1 405 ? 4.340  36.381  9.539   1.00 24.79  ? 384  GLY A N     1 
ATOM   2811 C CA    . GLY A 1 405 ? 3.636  37.577  9.959   1.00 24.53  ? 384  GLY A CA    1 
ATOM   2812 C C     . GLY A 1 405 ? 3.806  37.734  11.466  1.00 26.12  ? 384  GLY A C     1 
ATOM   2813 O O     . GLY A 1 405 ? 4.581  36.991  12.074  1.00 29.79  ? 384  GLY A O     1 
ATOM   2814 N N     . ALA A 1 406 ? 3.065  38.671  12.068  1.00 23.84  ? 385  ALA A N     1 
ATOM   2815 C CA    . ALA A 1 406 ? 3.273  39.037  13.454  1.00 24.72  ? 385  ALA A CA    1 
ATOM   2816 C C     . ALA A 1 406 ? 2.500  38.152  14.425  1.00 24.91  ? 385  ALA A C     1 
ATOM   2817 O O     . ALA A 1 406 ? 2.646  38.301  15.637  1.00 24.38  ? 385  ALA A O     1 
ATOM   2818 C CB    . ALA A 1 406 ? 2.876  40.481  13.659  1.00 28.71  ? 385  ALA A CB    1 
ATOM   2819 N N     . ASP A 1 407 ? 1.656  37.243  13.945  1.00 27.89  ? 386  ASP A N     1 
ATOM   2820 C CA    . ASP A 1 407 ? 0.912  36.408  14.881  1.00 26.79  ? 386  ASP A CA    1 
ATOM   2821 C C     . ASP A 1 407 ? 1.857  35.425  15.593  1.00 26.82  ? 386  ASP A C     1 
ATOM   2822 O O     . ASP A 1 407 ? 2.471  34.564  14.969  1.00 27.69  ? 386  ASP A O     1 
ATOM   2823 C CB    . ASP A 1 407 ? -0.248 35.768  14.165  1.00 28.06  ? 386  ASP A CB    1 
ATOM   2824 C CG    . ASP A 1 407 ? -1.054 34.786  14.997  1.00 30.67  ? 386  ASP A CG    1 
ATOM   2825 O OD1   . ASP A 1 407 ? -0.756 34.615  16.195  1.00 30.19  ? 386  ASP A OD1   1 
ATOM   2826 O OD2   . ASP A 1 407 ? -1.938 34.174  14.409  1.00 36.57  ? 386  ASP A OD2   1 
ATOM   2827 N N     . PRO A 1 408 ? 1.985  35.487  16.937  1.00 29.24  ? 387  PRO A N     1 
ATOM   2828 C CA    . PRO A 1 408 ? 2.952  34.651  17.653  1.00 28.68  ? 387  PRO A CA    1 
ATOM   2829 C C     . PRO A 1 408 ? 2.620  33.167  17.647  1.00 28.05  ? 387  PRO A C     1 
ATOM   2830 O O     . PRO A 1 408 ? 3.469  32.335  17.946  1.00 28.66  ? 387  PRO A O     1 
ATOM   2831 C CB    . PRO A 1 408 ? 2.925  35.249  19.076  1.00 31.01  ? 387  PRO A CB    1 
ATOM   2832 C CG    . PRO A 1 408 ? 1.541  35.853  19.211  1.00 30.97  ? 387  PRO A CG    1 
ATOM   2833 C CD    . PRO A 1 408 ? 1.229  36.384  17.834  1.00 29.86  ? 387  PRO A CD    1 
ATOM   2834 N N     . SER A 1 409 ? 1.376  32.854  17.285  1.00 27.34  ? 388  SER A N     1 
ATOM   2835 C CA    . SER A 1 409 ? 0.907  31.493  17.189  1.00 28.23  ? 388  SER A CA    1 
ATOM   2836 C C     . SER A 1 409 ? 1.143  30.908  15.802  1.00 27.92  ? 388  SER A C     1 
ATOM   2837 O O     . SER A 1 409 ? 0.883  29.723  15.626  1.00 26.67  ? 388  SER A O     1 
ATOM   2838 C CB    . SER A 1 409 ? -0.576 31.424  17.506  1.00 33.01  ? 388  SER A CB    1 
ATOM   2839 O OG    . SER A 1 409 ? -0.770 31.840  18.842  1.00 37.68  ? 388  SER A OG    1 
ATOM   2840 N N     . ALA A 1 410 ? 1.468  31.734  14.799  1.00 26.22  ? 389  ALA A N     1 
ATOM   2841 C CA    . ALA A 1 410 ? 1.657  31.229  13.439  1.00 25.24  ? 389  ALA A CA    1 
ATOM   2842 C C     . ALA A 1 410 ? 3.051  30.588  13.306  1.00 22.92  ? 389  ALA A C     1 
ATOM   2843 O O     . ALA A 1 410 ? 4.006  31.093  13.874  1.00 24.07  ? 389  ALA A O     1 
ATOM   2844 C CB    . ALA A 1 410 ? 1.456  32.354  12.442  1.00 25.45  ? 389  ALA A CB    1 
ATOM   2845 N N     . ALA A 1 411 ? 3.178  29.492  12.550  1.00 20.57  ? 390  ALA A N     1 
ATOM   2846 C CA    . ALA A 1 411 ? 4.493  28.940  12.259  1.00 21.64  ? 390  ALA A CA    1 
ATOM   2847 C C     . ALA A 1 411 ? 5.300  29.945  11.438  1.00 23.71  ? 390  ALA A C     1 
ATOM   2848 O O     . ALA A 1 411 ? 4.741  30.711  10.640  1.00 21.82  ? 390  ALA A O     1 
ATOM   2849 C CB    . ALA A 1 411 ? 4.398  27.633  11.516  1.00 24.30  ? 390  ALA A CB    1 
ATOM   2850 N N     . PRO A 1 412 ? 6.640  29.927  11.579  1.00 20.97  ? 391  PRO A N     1 
ATOM   2851 C CA    . PRO A 1 412 ? 7.515  30.728  10.740  1.00 20.68  ? 391  PRO A CA    1 
ATOM   2852 C C     . PRO A 1 412 ? 7.709  29.973  9.436   1.00 22.59  ? 391  PRO A C     1 
ATOM   2853 O O     . PRO A 1 412 ? 7.293  28.814  9.323   1.00 22.86  ? 391  PRO A O     1 
ATOM   2854 C CB    . PRO A 1 412 ? 8.804  30.809  11.556  1.00 21.33  ? 391  PRO A CB    1 
ATOM   2855 C CG    . PRO A 1 412 ? 8.862  29.463  12.256  1.00 21.00  ? 391  PRO A CG    1 
ATOM   2856 C CD    . PRO A 1 412 ? 7.400  29.073  12.515  1.00 20.99  ? 391  PRO A CD    1 
ATOM   2857 N N     . LEU A 1 413 ? 8.329  30.671  8.477   1.00 20.19  ? 392  LEU A N     1 
ATOM   2858 C CA    . LEU A 1 413 ? 8.650  30.122  7.168   1.00 21.79  ? 392  LEU A CA    1 
ATOM   2859 C C     . LEU A 1 413 ? 10.054 29.527  7.195   1.00 20.63  ? 392  LEU A C     1 
ATOM   2860 O O     . LEU A 1 413 ? 11.036 30.247  7.376   1.00 20.76  ? 392  LEU A O     1 
ATOM   2861 C CB    . LEU A 1 413 ? 8.542  31.260  6.155   1.00 22.19  ? 392  LEU A CB    1 
ATOM   2862 C CG    . LEU A 1 413 ? 7.138  31.833  5.976   1.00 22.66  ? 392  LEU A CG    1 
ATOM   2863 C CD1   . LEU A 1 413 ? 7.155  33.013  5.039   1.00 26.26  ? 392  LEU A CD1   1 
ATOM   2864 C CD2   . LEU A 1 413 ? 6.151  30.769  5.493   1.00 26.18  ? 392  LEU A CD2   1 
ATOM   2865 N N     . ILE A 1 414 ? 10.118 28.206  7.011   1.00 21.12  ? 393  ILE A N     1 
ATOM   2866 C CA    . ILE A 1 414 ? 11.335 27.441  7.151   1.00 20.14  ? 393  ILE A CA    1 
ATOM   2867 C C     . ILE A 1 414 ? 11.788 27.052  5.743   1.00 19.93  ? 393  ILE A C     1 
ATOM   2868 O O     . ILE A 1 414 ? 11.097 26.301  5.042   1.00 18.54  ? 393  ILE A O     1 
ATOM   2869 C CB    . ILE A 1 414 ? 11.088 26.224  8.081   1.00 20.84  ? 393  ILE A CB    1 
ATOM   2870 C CG1   . ILE A 1 414 ? 10.559 26.640  9.466   1.00 21.32  ? 393  ILE A CG1   1 
ATOM   2871 C CG2   . ILE A 1 414 ? 12.358 25.394  8.221   1.00 20.57  ? 393  ILE A CG2   1 
ATOM   2872 C CD1   . ILE A 1 414 ? 9.911  25.501  10.264  1.00 21.50  ? 393  ILE A CD1   1 
ATOM   2873 N N     . ASP A 1 415 ? 12.950 27.577  5.336   1.00 20.10  ? 394  ASP A N     1 
ATOM   2874 C CA    . ASP A 1 415 ? 13.515 27.310  4.029   1.00 22.32  ? 394  ASP A CA    1 
ATOM   2875 C C     . ASP A 1 415 ? 14.955 26.843  4.193   1.00 20.36  ? 394  ASP A C     1 
ATOM   2876 O O     . ASP A 1 415 ? 15.853 27.672  4.189   1.00 20.38  ? 394  ASP A O     1 
ATOM   2877 C CB    . ASP A 1 415 ? 13.445 28.524  3.103   1.00 24.75  ? 394  ASP A CB    1 
ATOM   2878 C CG    . ASP A 1 415 ? 13.965 28.224  1.707   1.00 25.34  ? 394  ASP A CG    1 
ATOM   2879 O OD1   . ASP A 1 415 ? 14.133 27.033  1.373   1.00 25.15  ? 394  ASP A OD1   1 
ATOM   2880 O OD2   . ASP A 1 415 ? 14.255 29.165  0.989   1.00 29.11  ? 394  ASP A OD2   1 
ATOM   2881 N N     . PRO A 1 416 ? 15.231 25.521  4.352   1.00 19.13  ? 395  PRO A N     1 
ATOM   2882 C CA    . PRO A 1 416 ? 16.611 25.037  4.492   1.00 19.76  ? 395  PRO A CA    1 
ATOM   2883 C C     . PRO A 1 416 ? 17.541 25.144  3.289   1.00 20.87  ? 395  PRO A C     1 
ATOM   2884 O O     . PRO A 1 416 ? 18.761 24.985  3.417   1.00 19.37  ? 395  PRO A O     1 
ATOM   2885 C CB    . PRO A 1 416 ? 16.422 23.554  4.912   1.00 19.72  ? 395  PRO A CB    1 
ATOM   2886 C CG    . PRO A 1 416 ? 15.051 23.532  5.499   1.00 19.17  ? 395  PRO A CG    1 
ATOM   2887 C CD    . PRO A 1 416 ? 14.241 24.472  4.609   1.00 19.09  ? 395  PRO A CD    1 
ATOM   2888 N N     . GLY A 1 417 ? 16.958 25.384  2.112   1.00 21.81  ? 396  GLY A N     1 
ATOM   2889 C CA    . GLY A 1 417 ? 17.750 25.438  0.897   1.00 20.37  ? 396  GLY A CA    1 
ATOM   2890 C C     . GLY A 1 417 ? 18.369 24.083  0.571   1.00 20.47  ? 396  GLY A C     1 
ATOM   2891 O O     . GLY A 1 417 ? 19.494 24.042  0.085   1.00 21.53  ? 396  GLY A O     1 
ATOM   2892 N N     . TYR A 1 418 ? 17.659 22.983  0.869   1.00 20.04  ? 397  TYR A N     1 
ATOM   2893 C CA    . TYR A 1 418 ? 18.235 21.650  0.708   1.00 21.96  ? 397  TYR A CA    1 
ATOM   2894 C C     . TYR A 1 418 ? 18.714 21.435  -0.734  1.00 21.56  ? 397  TYR A C     1 
ATOM   2895 O O     . TYR A 1 418 ? 17.963 21.729  -1.682  1.00 20.66  ? 397  TYR A O     1 
ATOM   2896 C CB    . TYR A 1 418 ? 17.180 20.587  1.026   1.00 20.72  ? 397  TYR A CB    1 
ATOM   2897 C CG    . TYR A 1 418 ? 16.758 20.467  2.492   1.00 22.26  ? 397  TYR A CG    1 
ATOM   2898 C CD1   . TYR A 1 418 ? 17.699 20.263  3.502   1.00 21.41  ? 397  TYR A CD1   1 
ATOM   2899 C CD2   . TYR A 1 418 ? 15.422 20.520  2.855   1.00 20.76  ? 397  TYR A CD2   1 
ATOM   2900 C CE1   . TYR A 1 418 ? 17.321 20.087  4.828   1.00 20.33  ? 397  TYR A CE1   1 
ATOM   2901 C CE2   . TYR A 1 418 ? 15.029 20.341  4.181   1.00 21.09  ? 397  TYR A CE2   1 
ATOM   2902 C CZ    . TYR A 1 418 ? 15.980 20.138  5.170   1.00 21.44  ? 397  TYR A CZ    1 
ATOM   2903 O OH    . TYR A 1 418 ? 15.628 20.022  6.495   1.00 21.41  ? 397  TYR A OH    1 
ATOM   2904 N N     . LEU A 1 419 ? 19.943 20.900  -0.863  1.00 21.14  ? 398  LEU A N     1 
ATOM   2905 C CA    . LEU A 1 419 ? 20.552 20.549  -2.148  1.00 23.66  ? 398  LEU A CA    1 
ATOM   2906 C C     . LEU A 1 419 ? 20.606 21.754  -3.093  1.00 25.30  ? 398  LEU A C     1 
ATOM   2907 O O     . LEU A 1 419 ? 20.619 21.597  -4.322  1.00 25.94  ? 398  LEU A O     1 
ATOM   2908 C CB    . LEU A 1 419 ? 19.843 19.364  -2.797  1.00 21.77  ? 398  LEU A CB    1 
ATOM   2909 C CG    . LEU A 1 419 ? 19.772 18.096  -1.932  1.00 21.14  ? 398  LEU A CG    1 
ATOM   2910 C CD1   . LEU A 1 419 ? 19.188 16.927  -2.708  1.00 20.89  ? 398  LEU A CD1   1 
ATOM   2911 C CD2   . LEU A 1 419 ? 21.136 17.763  -1.292  1.00 20.06  ? 398  LEU A CD2   1 
ATOM   2912 N N     . GLY A 1 420 ? 20.718 22.947  -2.498  1.00 25.04  ? 399  GLY A N     1 
ATOM   2913 C CA    . GLY A 1 420 ? 20.962 24.151  -3.268  1.00 26.15  ? 399  GLY A CA    1 
ATOM   2914 C C     . GLY A 1 420 ? 22.371 24.081  -3.841  1.00 26.53  ? 399  GLY A C     1 
ATOM   2915 O O     . GLY A 1 420 ? 22.582 24.485  -4.971  1.00 31.91  ? 399  GLY A O     1 
ATOM   2916 N N     . ALA A 1 421 ? 23.314 23.570  -3.037  1.00 27.70  ? 400  ALA A N     1 
ATOM   2917 C CA    . ALA A 1 421 ? 24.677 23.301  -3.462  1.00 29.29  ? 400  ALA A CA    1 
ATOM   2918 C C     . ALA A 1 421 ? 24.789 21.951  -4.183  1.00 30.69  ? 400  ALA A C     1 
ATOM   2919 O O     . ALA A 1 421 ? 24.526 20.887  -3.622  1.00 24.29  ? 400  ALA A O     1 
ATOM   2920 C CB    . ALA A 1 421 ? 25.609 23.372  -2.274  1.00 28.60  ? 400  ALA A CB    1 
ATOM   2921 N N     . GLU A 1 422 ? 25.262 21.989  -5.440  1.00 30.56  ? 401  GLU A N     1 
ATOM   2922 C CA    . GLU A 1 422 ? 25.390 20.777  -6.229  1.00 30.92  ? 401  GLU A CA    1 
ATOM   2923 C C     . GLU A 1 422 ? 26.378 19.814  -5.599  1.00 27.53  ? 401  GLU A C     1 
ATOM   2924 O O     . GLU A 1 422 ? 26.224 18.621  -5.769  1.00 27.25  ? 401  GLU A O     1 
ATOM   2925 C CB    . GLU A 1 422 ? 25.787 21.027  -7.684  1.00 37.94  ? 401  GLU A CB    1 
ATOM   2926 C CG    . GLU A 1 422 ? 24.597 21.543  -8.484  1.00 48.90  ? 401  GLU A CG    1 
ATOM   2927 C CD    . GLU A 1 422 ? 24.572 21.178  -9.958  1.00 62.78  ? 401  GLU A CD    1 
ATOM   2928 O OE1   . GLU A 1 422 ? 24.643 22.154  -10.735 1.00 55.68  ? 401  GLU A OE1   1 
ATOM   2929 O OE2   . GLU A 1 422 ? 24.446 19.976  -10.328 1.00 72.45  ? 401  GLU A OE2   1 
ATOM   2930 N N     . SER A 1 423 ? 27.398 20.305  -4.897  1.00 27.78  ? 402  SER A N     1 
ATOM   2931 C CA    . SER A 1 423 ? 28.317 19.404  -4.216  1.00 30.55  ? 402  SER A CA    1 
ATOM   2932 C C     . SER A 1 423 ? 27.593 18.467  -3.236  1.00 29.19  ? 402  SER A C     1 
ATOM   2933 O O     . SER A 1 423 ? 28.026 17.332  -3.006  1.00 26.22  ? 402  SER A O     1 
ATOM   2934 C CB    . SER A 1 423 ? 29.354 20.185  -3.502  1.00 33.07  ? 402  SER A CB    1 
ATOM   2935 O OG    . SER A 1 423 ? 28.694 21.150  -2.696  1.00 32.29  ? 402  SER A OG    1 
ATOM   2936 N N     . ASP A 1 424 ? 26.503 18.949  -2.627  1.00 28.42  ? 403  ASP A N     1 
ATOM   2937 C CA    . ASP A 1 424 ? 25.767 18.139  -1.652  1.00 24.65  ? 403  ASP A CA    1 
ATOM   2938 C C     . ASP A 1 424 ? 25.145 16.936  -2.365  1.00 23.14  ? 403  ASP A C     1 
ATOM   2939 O O     . ASP A 1 424 ? 25.101 15.847  -1.791  1.00 22.71  ? 403  ASP A O     1 
ATOM   2940 C CB    . ASP A 1 424 ? 24.688 18.947  -0.940  1.00 23.99  ? 403  ASP A CB    1 
ATOM   2941 C CG    . ASP A 1 424 ? 25.195 20.016  0.026   1.00 24.37  ? 403  ASP A CG    1 
ATOM   2942 O OD1   . ASP A 1 424 ? 26.442 20.082  0.217   1.00 23.91  ? 403  ASP A OD1   1 
ATOM   2943 O OD2   . ASP A 1 424 ? 24.343 20.768  0.604   1.00 24.43  ? 403  ASP A OD2   1 
ATOM   2944 N N     . VAL A 1 425 ? 24.671 17.144  -3.607  1.00 22.38  ? 404  VAL A N     1 
ATOM   2945 C CA    . VAL A 1 425 ? 24.039 16.085  -4.371  1.00 26.59  ? 404  VAL A CA    1 
ATOM   2946 C C     . VAL A 1 425 ? 25.083 15.022  -4.709  1.00 26.78  ? 404  VAL A C     1 
ATOM   2947 O O     . VAL A 1 425 ? 24.825 13.813  -4.574  1.00 23.24  ? 404  VAL A O     1 
ATOM   2948 C CB    . VAL A 1 425 ? 23.322 16.597  -5.636  1.00 28.72  ? 404  VAL A CB    1 
ATOM   2949 C CG1   . VAL A 1 425 ? 22.803 15.440  -6.477  1.00 26.95  ? 404  VAL A CG1   1 
ATOM   2950 C CG2   . VAL A 1 425 ? 22.179 17.548  -5.297  1.00 29.36  ? 404  VAL A CG2   1 
ATOM   2951 N N     . ARG A 1 426 ? 26.275 15.489  -5.124  1.00 27.95  ? 405  ARG A N     1 
ATOM   2952 C CA    . ARG A 1 426 ? 27.343 14.589  -5.520  1.00 28.84  ? 405  ARG A CA    1 
ATOM   2953 C C     . ARG A 1 426 ? 27.808 13.785  -4.307  1.00 27.46  ? 405  ARG A C     1 
ATOM   2954 O O     . ARG A 1 426 ? 28.151 12.609  -4.437  1.00 26.83  ? 405  ARG A O     1 
ATOM   2955 C CB    . ARG A 1 426 ? 28.507 15.327  -6.198  1.00 32.79  ? 405  ARG A CB    1 
ATOM   2956 C CG    . ARG A 1 426 ? 28.135 15.816  -7.598  1.00 38.11  ? 405  ARG A CG    1 
ATOM   2957 C CD    . ARG A 1 426 ? 29.303 16.348  -8.423  1.00 38.32  ? 405  ARG A CD    1 
ATOM   2958 N NE    . ARG A 1 426 ? 30.044 17.349  -7.648  1.00 42.32  ? 405  ARG A NE    1 
ATOM   2959 C CZ    . ARG A 1 426 ? 29.798 18.666  -7.696  1.00 43.31  ? 405  ARG A CZ    1 
ATOM   2960 N NH1   . ARG A 1 426 ? 28.834 19.139  -8.467  1.00 43.25  ? 405  ARG A NH1   1 
ATOM   2961 N NH2   . ARG A 1 426 ? 30.514 19.498  -6.968  1.00 41.25  ? 405  ARG A NH2   1 
ATOM   2962 N N     . THR A 1 427 ? 27.873 14.421  -3.128  1.00 26.19  ? 406  THR A N     1 
ATOM   2963 C CA    . THR A 1 427 ? 28.334 13.716  -1.941  1.00 24.61  ? 406  THR A CA    1 
ATOM   2964 C C     . THR A 1 427 ? 27.342 12.606  -1.570  1.00 23.62  ? 406  THR A C     1 
ATOM   2965 O O     . THR A 1 427 ? 27.765 11.503  -1.243  1.00 22.31  ? 406  THR A O     1 
ATOM   2966 C CB    . THR A 1 427 ? 28.529 14.662  -0.762  1.00 24.99  ? 406  THR A CB    1 
ATOM   2967 O OG1   . THR A 1 427 ? 29.559 15.575  -1.107  1.00 24.98  ? 406  THR A OG1   1 
ATOM   2968 C CG2   . THR A 1 427 ? 29.018 13.943  0.475   1.00 24.63  ? 406  THR A CG2   1 
ATOM   2969 N N     . LEU A 1 428 ? 26.041 12.918  -1.608  1.00 20.54  ? 407  LEU A N     1 
ATOM   2970 C CA    . LEU A 1 428 ? 25.008 11.933  -1.338  1.00 21.34  ? 407  LEU A CA    1 
ATOM   2971 C C     . LEU A 1 428 ? 25.032 10.797  -2.359  1.00 21.09  ? 407  LEU A C     1 
ATOM   2972 O O     . LEU A 1 428 ? 24.877 9.649   -1.959  1.00 18.90  ? 407  LEU A O     1 
ATOM   2973 C CB    . LEU A 1 428 ? 23.653 12.603  -1.295  1.00 22.07  ? 407  LEU A CB    1 
ATOM   2974 C CG    . LEU A 1 428 ? 23.349 13.330  0.022   1.00 22.62  ? 407  LEU A CG    1 
ATOM   2975 C CD1   . LEU A 1 428 ? 22.129 14.233  -0.218  1.00 24.46  ? 407  LEU A CD1   1 
ATOM   2976 C CD2   . LEU A 1 428 ? 23.135 12.364  1.209   1.00 22.27  ? 407  LEU A CD2   1 
ATOM   2977 N N     . ALA A 1 429 ? 25.280 11.110  -3.641  1.00 22.05  ? 408  ALA A N     1 
ATOM   2978 C CA    . ALA A 1 429 ? 25.384 10.093  -4.688  1.00 21.71  ? 408  ALA A CA    1 
ATOM   2979 C C     . ALA A 1 429 ? 26.489 9.098   -4.352  1.00 22.41  ? 408  ALA A C     1 
ATOM   2980 O O     . ALA A 1 429 ? 26.306 7.880   -4.430  1.00 23.20  ? 408  ALA A O     1 
ATOM   2981 C CB    . ALA A 1 429 ? 25.591 10.764  -6.039  1.00 23.66  ? 408  ALA A CB    1 
ATOM   2982 N N     . ALA A 1 430 ? 27.625 9.620   -3.896  1.00 26.04  ? 409  ALA A N     1 
ATOM   2983 C CA    . ALA A 1 430 ? 28.752 8.797   -3.505  1.00 24.54  ? 409  ALA A CA    1 
ATOM   2984 C C     . ALA A 1 430 ? 28.401 7.911   -2.316  1.00 22.74  ? 409  ALA A C     1 
ATOM   2985 O O     . ALA A 1 430 ? 28.813 6.753   -2.227  1.00 21.27  ? 409  ALA A O     1 
ATOM   2986 C CB    . ALA A 1 430 ? 29.915 9.677   -3.166  1.00 27.40  ? 409  ALA A CB    1 
ATOM   2987 N N     . GLY A 1 431 ? 27.664 8.461   -1.363  1.00 19.88  ? 410  GLY A N     1 
ATOM   2988 C CA    . GLY A 1 431 ? 27.243 7.672   -0.225  1.00 18.91  ? 410  GLY A CA    1 
ATOM   2989 C C     . GLY A 1 431 ? 26.240 6.575   -0.600  1.00 18.43  ? 410  GLY A C     1 
ATOM   2990 O O     . GLY A 1 431 ? 26.300 5.491   -0.032  1.00 17.21  ? 410  GLY A O     1 
ATOM   2991 N N     . VAL A 1 432 ? 25.320 6.839   -1.536  1.00 19.27  ? 411  VAL A N     1 
ATOM   2992 C CA    . VAL A 1 432 ? 24.405 5.806   -2.007  1.00 20.54  ? 411  VAL A CA    1 
ATOM   2993 C C     . VAL A 1 432 ? 25.198 4.684   -2.693  1.00 24.57  ? 411  VAL A C     1 
ATOM   2994 O O     . VAL A 1 432 ? 24.864 3.510   -2.520  1.00 21.77  ? 411  VAL A O     1 
ATOM   2995 C CB    . VAL A 1 432 ? 23.342 6.385   -2.951  1.00 21.29  ? 411  VAL A CB    1 
ATOM   2996 C CG1   . VAL A 1 432 ? 22.612 5.315   -3.761  1.00 20.94  ? 411  VAL A CG1   1 
ATOM   2997 C CG2   . VAL A 1 432 ? 22.355 7.258   -2.203  1.00 21.29  ? 411  VAL A CG2   1 
ATOM   2998 N N     . ARG A 1 433 ? 26.255 5.029   -3.451  1.00 23.76  ? 412  ARG A N     1 
ATOM   2999 C CA    . ARG A 1 433 ? 27.103 3.998   -4.058  1.00 22.61  ? 412  ARG A CA    1 
ATOM   3000 C C     . ARG A 1 433 ? 27.747 3.120   -2.986  1.00 20.95  ? 412  ARG A C     1 
ATOM   3001 O O     . ARG A 1 433 ? 27.856 1.895   -3.132  1.00 22.77  ? 412  ARG A O     1 
ATOM   3002 C CB    . ARG A 1 433 ? 28.123 4.549   -5.057  1.00 24.34  ? 412  ARG A CB    1 
ATOM   3003 C CG    . ARG A 1 433 ? 27.501 5.080   -6.339  1.00 25.17  ? 412  ARG A CG    1 
ATOM   3004 C CD    . ARG A 1 433 ? 26.986 3.917   -7.158  1.00 28.29  ? 412  ARG A CD    1 
ATOM   3005 N NE    . ARG A 1 433 ? 26.608 4.381   -8.496  1.00 31.46  ? 412  ARG A NE    1 
ATOM   3006 C CZ    . ARG A 1 433 ? 25.409 4.411   -9.024  1.00 33.89  ? 412  ARG A CZ    1 
ATOM   3007 N NH1   . ARG A 1 433 ? 24.382 3.789   -8.437  1.00 36.45  ? 412  ARG A NH1   1 
ATOM   3008 N NH2   . ARG A 1 433 ? 25.251 5.056   -10.178 1.00 32.85  ? 412  ARG A NH2   1 
ATOM   3009 N N     . PHE A 1 434 ? 28.155 3.740   -1.873  1.00 19.55  ? 413  PHE A N     1 
ATOM   3010 C CA    . PHE A 1 434 ? 28.787 3.005   -0.809  1.00 19.27  ? 413  PHE A CA    1 
ATOM   3011 C C     . PHE A 1 434 ? 27.788 2.091   -0.088  1.00 22.02  ? 413  PHE A C     1 
ATOM   3012 O O     . PHE A 1 434 ? 28.123 0.941   0.226   1.00 22.31  ? 413  PHE A O     1 
ATOM   3013 C CB    . PHE A 1 434 ? 29.516 3.990   0.098   1.00 20.91  ? 413  PHE A CB    1 
ATOM   3014 C CG    . PHE A 1 434 ? 30.526 3.240   0.936   1.00 20.32  ? 413  PHE A CG    1 
ATOM   3015 C CD1   . PHE A 1 434 ? 30.155 2.704   2.144   1.00 22.08  ? 413  PHE A CD1   1 
ATOM   3016 C CD2   . PHE A 1 434 ? 31.817 3.028   0.477   1.00 23.62  ? 413  PHE A CD2   1 
ATOM   3017 C CE1   . PHE A 1 434 ? 31.043 1.951   2.869   1.00 23.05  ? 413  PHE A CE1   1 
ATOM   3018 C CE2   . PHE A 1 434 ? 32.711 2.300   1.227   1.00 23.62  ? 413  PHE A CE2   1 
ATOM   3019 C CZ    . PHE A 1 434 ? 32.329 1.792   2.432   1.00 23.11  ? 413  PHE A CZ    1 
ATOM   3020 N N     . ALA A 1 435 ? 26.573 2.599   0.183   1.00 20.55  ? 414  ALA A N     1 
ATOM   3021 C CA    . ALA A 1 435 ? 25.491 1.802   0.735   1.00 20.11  ? 414  ALA A CA    1 
ATOM   3022 C C     . ALA A 1 435 ? 25.235 0.604   -0.185  1.00 20.55  ? 414  ALA A C     1 
ATOM   3023 O O     . ALA A 1 435 ? 25.100 -0.534  0.278   1.00 19.01  ? 414  ALA A O     1 
ATOM   3024 C CB    . ALA A 1 435 ? 24.213 2.647   0.871   1.00 21.21  ? 414  ALA A CB    1 
ATOM   3025 N N     . GLU A 1 436 ? 25.217 0.857   -1.503  1.00 20.10  ? 415  GLU A N     1 
ATOM   3026 C CA    . GLU A 1 436 ? 24.989 -0.243  -2.430  1.00 22.28  ? 415  GLU A CA    1 
ATOM   3027 C C     . GLU A 1 436 ? 26.100 -1.285  -2.324  1.00 24.06  ? 415  GLU A C     1 
ATOM   3028 O O     . GLU A 1 436 ? 25.838 -2.486  -2.453  1.00 25.11  ? 415  GLU A O     1 
ATOM   3029 C CB    . GLU A 1 436 ? 24.841 0.268   -3.854  1.00 24.35  ? 415  GLU A CB    1 
ATOM   3030 C CG    . GLU A 1 436 ? 23.513 0.987   -4.045  1.00 22.55  ? 415  GLU A CG    1 
ATOM   3031 C CD    . GLU A 1 436 ? 23.354 1.724   -5.354  1.00 23.39  ? 415  GLU A CD    1 
ATOM   3032 O OE1   . GLU A 1 436 ? 22.201 2.100   -5.643  1.00 24.03  ? 415  GLU A OE1   1 
ATOM   3033 O OE2   . GLU A 1 436 ? 24.353 1.998   -6.041  1.00 24.34  ? 415  GLU A OE2   1 
ATOM   3034 N N     . ARG A 1 437 ? 27.338 -0.806  -2.144  1.00 24.25  ? 416  ARG A N     1 
ATOM   3035 C CA    . ARG A 1 437 ? 28.494 -1.660  -1.988  1.00 22.73  ? 416  ARG A CA    1 
ATOM   3036 C C     . ARG A 1 437 ? 28.279 -2.559  -0.773  1.00 23.82  ? 416  ARG A C     1 
ATOM   3037 O O     . ARG A 1 437 ? 28.599 -3.748  -0.796  1.00 21.74  ? 416  ARG A O     1 
ATOM   3038 C CB    . ARG A 1 437 ? 29.771 -0.838  -1.819  1.00 22.38  ? 416  ARG A CB    1 
ATOM   3039 C CG    . ARG A 1 437 ? 31.000 -1.700  -1.566  1.00 26.01  ? 416  ARG A CG    1 
ATOM   3040 C CD    . ARG A 1 437 ? 32.247 -0.831  -1.542  1.00 28.08  ? 416  ARG A CD    1 
ATOM   3041 N NE    . ARG A 1 437 ? 33.433 -1.647  -1.243  1.00 29.37  ? 416  ARG A NE    1 
ATOM   3042 C CZ    . ARG A 1 437 ? 34.616 -1.177  -0.848  1.00 31.00  ? 416  ARG A CZ    1 
ATOM   3043 N NH1   . ARG A 1 437 ? 34.828 0.117   -0.808  1.00 30.96  ? 416  ARG A NH1   1 
ATOM   3044 N NH2   . ARG A 1 437 ? 35.579 -2.002  -0.476  1.00 34.07  ? 416  ARG A NH2   1 
ATOM   3045 N N     . LEU A 1 438 ? 27.734 -1.975  0.298   1.00 22.70  ? 417  LEU A N     1 
ATOM   3046 C CA    . LEU A 1 438 ? 27.509 -2.721  1.511   1.00 20.58  ? 417  LEU A CA    1 
ATOM   3047 C C     . LEU A 1 438 ? 26.453 -3.797  1.292   1.00 21.06  ? 417  LEU A C     1 
ATOM   3048 O O     . LEU A 1 438 ? 26.638 -4.941  1.700   1.00 21.23  ? 417  LEU A O     1 
ATOM   3049 C CB    . LEU A 1 438 ? 27.167 -1.793  2.668   1.00 20.85  ? 417  LEU A CB    1 
ATOM   3050 C CG    . LEU A 1 438 ? 28.284 -0.878  3.168   1.00 22.46  ? 417  LEU A CG    1 
ATOM   3051 C CD1   . LEU A 1 438 ? 27.795 -0.000  4.319   1.00 24.61  ? 417  LEU A CD1   1 
ATOM   3052 C CD2   . LEU A 1 438 ? 29.482 -1.680  3.642   1.00 23.15  ? 417  LEU A CD2   1 
ATOM   3053 N N     . PHE A 1 439 ? 25.322 -3.436  0.701   1.00 20.80  ? 418  PHE A N     1 
ATOM   3054 C CA    . PHE A 1 439 ? 24.306 -4.435  0.416   1.00 20.98  ? 418  PHE A CA    1 
ATOM   3055 C C     . PHE A 1 439 ? 24.810 -5.515  -0.544  1.00 21.94  ? 418  PHE A C     1 
ATOM   3056 O O     . PHE A 1 439 ? 24.279 -6.633  -0.509  1.00 21.57  ? 418  PHE A O     1 
ATOM   3057 C CB    . PHE A 1 439 ? 22.995 -3.881  -0.124  1.00 22.30  ? 418  PHE A CB    1 
ATOM   3058 C CG    . PHE A 1 439 ? 22.109 -3.255  0.940   1.00 21.15  ? 418  PHE A CG    1 
ATOM   3059 C CD1   . PHE A 1 439 ? 21.554 -4.038  1.954   1.00 22.62  ? 418  PHE A CD1   1 
ATOM   3060 C CD2   . PHE A 1 439 ? 21.795 -1.897  0.891   1.00 20.98  ? 418  PHE A CD2   1 
ATOM   3061 C CE1   . PHE A 1 439 ? 20.685 -3.471  2.873   1.00 22.63  ? 418  PHE A CE1   1 
ATOM   3062 C CE2   . PHE A 1 439 ? 20.941 -1.332  1.828   1.00 20.31  ? 418  PHE A CE2   1 
ATOM   3063 C CZ    . PHE A 1 439 ? 20.387 -2.114  2.808   1.00 21.51  ? 418  PHE A CZ    1 
ATOM   3064 N N     . ALA A 1 440 ? 25.847 -5.210  -1.344  1.00 21.28  ? 419  ALA A N     1 
ATOM   3065 C CA    . ALA A 1 440 ? 26.448 -6.195  -2.222  1.00 23.35  ? 419  ALA A CA    1 
ATOM   3066 C C     . ALA A 1 440 ? 27.473 -7.054  -1.488  1.00 24.36  ? 419  ALA A C     1 
ATOM   3067 O O     . ALA A 1 440 ? 27.908 -8.064  -2.033  1.00 21.44  ? 419  ALA A O     1 
ATOM   3068 C CB    . ALA A 1 440 ? 27.068 -5.522  -3.418  1.00 23.62  ? 419  ALA A CB    1 
ATOM   3069 N N     . ALA A 1 441 ? 27.845 -6.679  -0.259  1.00 25.43  ? 420  ALA A N     1 
ATOM   3070 C CA    . ALA A 1 441 ? 28.860 -7.404  0.489   1.00 25.14  ? 420  ALA A CA    1 
ATOM   3071 C C     . ALA A 1 441 ? 28.392 -8.807  0.867   1.00 26.99  ? 420  ALA A C     1 
ATOM   3072 O O     . ALA A 1 441 ? 27.193 -9.061  0.960   1.00 21.10  ? 420  ALA A O     1 
ATOM   3073 C CB    . ALA A 1 441 ? 29.237 -6.662  1.739   1.00 25.18  ? 420  ALA A CB    1 
ATOM   3074 N N     . GLU A 1 442 ? 29.371 -9.695  1.147   1.00 27.08  ? 421  GLU A N     1 
ATOM   3075 C CA    . GLU A 1 442 ? 29.068 -11.075 1.471   1.00 30.45  ? 421  GLU A CA    1 
ATOM   3076 C C     . GLU A 1 442 ? 28.157 -11.132 2.693   1.00 29.60  ? 421  GLU A C     1 
ATOM   3077 O O     . GLU A 1 442 ? 27.271 -11.968 2.756   1.00 26.45  ? 421  GLU A O     1 
ATOM   3078 C CB    . GLU A 1 442 ? 30.282 -11.940 1.818   1.00 36.22  ? 421  GLU A CB    1 
ATOM   3079 C CG    . GLU A 1 442 ? 31.282 -12.123 0.685   1.00 45.09  ? 421  GLU A CG    1 
ATOM   3080 C CD    . GLU A 1 442 ? 30.691 -12.580 -0.637  1.00 53.08  ? 421  GLU A CD    1 
ATOM   3081 O OE1   . GLU A 1 442 ? 30.033 -13.640 -0.662  1.00 61.81  ? 421  GLU A OE1   1 
ATOM   3082 O OE2   . GLU A 1 442 ? 30.891 -11.874 -1.654  1.00 66.27  ? 421  GLU A OE2   1 
ATOM   3083 N N     . ALA A 1 443 ? 28.414 -10.271 3.679   1.00 27.86  ? 422  ALA A N     1 
ATOM   3084 C CA    . ALA A 1 443 ? 27.694 -10.340 4.933   1.00 27.55  ? 422  ALA A CA    1 
ATOM   3085 C C     . ALA A 1 443 ? 26.234 -9.898  4.776   1.00 24.98  ? 422  ALA A C     1 
ATOM   3086 O O     . ALA A 1 443 ? 25.424 -10.281 5.600   1.00 24.25  ? 422  ALA A O     1 
ATOM   3087 C CB    . ALA A 1 443 ? 28.422 -9.500  5.962   1.00 31.69  ? 422  ALA A CB    1 
ATOM   3088 N N     . LEU A 1 444 ? 25.882 -9.118  3.730   1.00 23.85  ? 423  LEU A N     1 
ATOM   3089 C CA    . LEU A 1 444 ? 24.517 -8.600  3.596   1.00 25.26  ? 423  LEU A CA    1 
ATOM   3090 C C     . LEU A 1 444 ? 23.758 -9.189  2.409   1.00 23.47  ? 423  LEU A C     1 
ATOM   3091 O O     . LEU A 1 444 ? 22.533 -9.284  2.475   1.00 22.32  ? 423  LEU A O     1 
ATOM   3092 C CB    . LEU A 1 444 ? 24.488 -7.074  3.534   1.00 23.84  ? 423  LEU A CB    1 
ATOM   3093 C CG    . LEU A 1 444 ? 24.715 -6.343  4.864   1.00 23.84  ? 423  LEU A CG    1 
ATOM   3094 C CD1   . LEU A 1 444 ? 24.675 -4.867  4.583   1.00 22.29  ? 423  LEU A CD1   1 
ATOM   3095 C CD2   . LEU A 1 444 ? 23.698 -6.696  5.945   1.00 24.74  ? 423  LEU A CD2   1 
ATOM   3096 N N     . ARG A 1 445 ? 24.437 -9.566  1.313   1.00 24.77  ? 424  ARG A N     1 
ATOM   3097 C CA    . ARG A 1 445 ? 23.712 -9.837  0.071   1.00 25.73  ? 424  ARG A CA    1 
ATOM   3098 C C     . ARG A 1 445 ? 22.717 -10.993 0.212   1.00 26.85  ? 424  ARG A C     1 
ATOM   3099 O O     . ARG A 1 445 ? 21.711 -11.030 -0.512  1.00 26.00  ? 424  ARG A O     1 
ATOM   3100 C CB    . ARG A 1 445 ? 24.610 -10.150 -1.131  1.00 29.15  ? 424  ARG A CB    1 
ATOM   3101 C CG    . ARG A 1 445 ? 25.522 -11.353 -0.968  1.00 32.70  ? 424  ARG A CG    1 
ATOM   3102 C CD    . ARG A 1 445 ? 26.507 -11.265 -2.155  1.00 37.26  ? 424  ARG A CD    1 
ATOM   3103 N NE    . ARG A 1 445 ? 27.404 -12.417 -2.222  1.00 38.54  ? 424  ARG A NE    1 
ATOM   3104 C CZ    . ARG A 1 445 ? 27.062 -13.627 -2.658  1.00 46.89  ? 424  ARG A CZ    1 
ATOM   3105 N NH1   . ARG A 1 445 ? 27.918 -14.617 -2.484  1.00 50.32  ? 424  ARG A NH1   1 
ATOM   3106 N NH2   . ARG A 1 445 ? 25.867 -13.875 -3.202  1.00 46.05  ? 424  ARG A NH2   1 
ATOM   3107 N N     . GLY A 1 446 ? 23.012 -11.934 1.121   1.00 28.20  ? 425  GLY A N     1 
ATOM   3108 C CA    . GLY A 1 446 ? 22.132 -13.066 1.388   1.00 28.61  ? 425  GLY A CA    1 
ATOM   3109 C C     . GLY A 1 446 ? 20.860 -12.651 2.128   1.00 29.81  ? 425  GLY A C     1 
ATOM   3110 O O     . GLY A 1 446 ? 19.894 -13.421 2.178   1.00 23.34  ? 425  GLY A O     1 
ATOM   3111 N N     . LEU A 1 447 ? 20.831 -11.426 2.689   1.00 26.25  ? 426  LEU A N     1 
ATOM   3112 C CA    . LEU A 1 447 ? 19.688 -11.015 3.494   1.00 26.88  ? 426  LEU A CA    1 
ATOM   3113 C C     . LEU A 1 447 ? 18.645 -10.257 2.674   1.00 27.04  ? 426  LEU A C     1 
ATOM   3114 O O     . LEU A 1 447 ? 17.601 -9.877  3.223   1.00 24.78  ? 426  LEU A O     1 
ATOM   3115 C CB    . LEU A 1 447 ? 20.158 -10.172 4.681   1.00 28.06  ? 426  LEU A CB    1 
ATOM   3116 C CG    . LEU A 1 447 ? 21.188 -10.838 5.591   1.00 30.19  ? 426  LEU A CG    1 
ATOM   3117 C CD1   . LEU A 1 447 ? 21.582 -9.905  6.732   1.00 28.29  ? 426  LEU A CD1   1 
ATOM   3118 C CD2   . LEU A 1 447 ? 20.730 -12.192 6.116   1.00 30.64  ? 426  LEU A CD2   1 
ATOM   3119 N N     . VAL A 1 448 ? 18.981 -9.916  1.415   1.00 24.48  ? 427  VAL A N     1 
ATOM   3120 C CA    . VAL A 1 448 ? 18.157 -9.011  0.631   1.00 23.04  ? 427  VAL A CA    1 
ATOM   3121 C C     . VAL A 1 448 ? 17.926 -9.609  -0.755  1.00 25.91  ? 427  VAL A C     1 
ATOM   3122 O O     . VAL A 1 448 ? 18.710 -10.429 -1.230  1.00 27.60  ? 427  VAL A O     1 
ATOM   3123 C CB    . VAL A 1 448 ? 18.760 -7.590  0.544   1.00 22.81  ? 427  VAL A CB    1 
ATOM   3124 C CG1   . VAL A 1 448 ? 18.818 -6.920  1.910   1.00 22.99  ? 427  VAL A CG1   1 
ATOM   3125 C CG2   . VAL A 1 448 ? 20.147 -7.536  -0.108  1.00 23.20  ? 427  VAL A CG2   1 
ATOM   3126 N N     . ASP A 1 449 ? 16.836 -9.175  -1.385  1.00 25.72  ? 428  ASP A N     1 
ATOM   3127 C CA    . ASP A 1 449 ? 16.467 -9.596  -2.727  1.00 28.53  ? 428  ASP A CA    1 
ATOM   3128 C C     . ASP A 1 449 ? 15.742 -8.450  -3.424  1.00 26.62  ? 428  ASP A C     1 
ATOM   3129 O O     . ASP A 1 449 ? 14.525 -8.358  -3.376  1.00 29.13  ? 428  ASP A O     1 
ATOM   3130 C CB    . ASP A 1 449 ? 15.613 -10.859 -2.702  1.00 32.12  ? 428  ASP A CB    1 
ATOM   3131 C CG    . ASP A 1 449 ? 15.228 -11.410 -4.077  1.00 40.04  ? 428  ASP A CG    1 
ATOM   3132 O OD1   . ASP A 1 449 ? 16.078 -11.355 -4.996  1.00 40.20  ? 428  ASP A OD1   1 
ATOM   3133 O OD2   . ASP A 1 449 ? 14.075 -11.874 -4.226  1.00 42.16  ? 428  ASP A OD2   1 
ATOM   3134 N N     . GLY A 1 450 ? 16.507 -7.560  -4.049  1.00 26.11  ? 429  GLY A N     1 
ATOM   3135 C CA    . GLY A 1 450 ? 15.958 -6.420  -4.742  1.00 24.98  ? 429  GLY A CA    1 
ATOM   3136 C C     . GLY A 1 450 ? 15.542 -5.283  -3.806  1.00 24.02  ? 429  GLY A C     1 
ATOM   3137 O O     . GLY A 1 450 ? 15.501 -5.404  -2.586  1.00 24.08  ? 429  GLY A O     1 
ATOM   3138 N N     . PRO A 1 451 ? 15.224 -4.127  -4.404  1.00 26.33  ? 430  PRO A N     1 
ATOM   3139 C CA    . PRO A 1 451 ? 14.916 -2.907  -3.657  1.00 25.00  ? 430  PRO A CA    1 
ATOM   3140 C C     . PRO A 1 451 ? 13.505 -2.972  -3.098  1.00 25.25  ? 430  PRO A C     1 
ATOM   3141 O O     . PRO A 1 451 ? 12.672 -3.749  -3.566  1.00 22.77  ? 430  PRO A O     1 
ATOM   3142 C CB    . PRO A 1 451 ? 15.073 -1.825  -4.747  1.00 24.89  ? 430  PRO A CB    1 
ATOM   3143 C CG    . PRO A 1 451 ? 14.641 -2.513  -6.032  1.00 25.41  ? 430  PRO A CG    1 
ATOM   3144 C CD    . PRO A 1 451 ? 15.184 -3.926  -5.865  1.00 26.94  ? 430  PRO A CD    1 
ATOM   3145 N N     . ALA A 1 452 ? 13.236 -2.129  -2.107  1.00 24.08  ? 431  ALA A N     1 
ATOM   3146 C CA    . ALA A 1 452 ? 11.884 -2.031  -1.562  1.00 26.35  ? 431  ALA A CA    1 
ATOM   3147 C C     . ALA A 1 452 ? 11.264 -0.713  -2.011  1.00 24.05  ? 431  ALA A C     1 
ATOM   3148 O O     . ALA A 1 452 ? 11.766 0.344   -1.624  1.00 22.29  ? 431  ALA A O     1 
ATOM   3149 C CB    . ALA A 1 452 ? 11.945 -2.148  -0.057  1.00 26.41  ? 431  ALA A CB    1 
ATOM   3150 N N     . ALA A 1 453 ? 10.195 -0.775  -2.828  1.00 25.29  ? 432  ALA A N     1 
ATOM   3151 C CA    . ALA A 1 453 ? 9.663  0.444   -3.430  1.00 28.20  ? 432  ALA A CA    1 
ATOM   3152 C C     . ALA A 1 453 ? 9.250  1.395   -2.312  1.00 26.60  ? 432  ALA A C     1 
ATOM   3153 O O     . ALA A 1 453 ? 8.792  0.954   -1.269  1.00 28.33  ? 432  ALA A O     1 
ATOM   3154 C CB    . ALA A 1 453 ? 8.473  0.158   -4.347  1.00 31.22  ? 432  ALA A CB    1 
ATOM   3155 N N     . PRO A 1 454 ? 9.357  2.725   -2.487  1.00 28.54  ? 433  PRO A N     1 
ATOM   3156 C CA    . PRO A 1 454 ? 9.775  3.325   -3.751  1.00 29.72  ? 433  PRO A CA    1 
ATOM   3157 C C     . PRO A 1 454 ? 11.275 3.501   -3.995  1.00 29.83  ? 433  PRO A C     1 
ATOM   3158 O O     . PRO A 1 454 ? 11.651 4.161   -4.954  1.00 28.17  ? 433  PRO A O     1 
ATOM   3159 C CB    . PRO A 1 454 ? 9.062  4.698   -3.605  1.00 31.05  ? 433  PRO A CB    1 
ATOM   3160 C CG    . PRO A 1 454 ? 9.237  5.030   -2.140  1.00 28.26  ? 433  PRO A CG    1 
ATOM   3161 C CD    . PRO A 1 454 ? 9.004  3.720   -1.462  1.00 28.60  ? 433  PRO A CD    1 
ATOM   3162 N N     . TRP A 1 455 ? 12.154 2.931   -3.160  1.00 27.99  ? 434  TRP A N     1 
ATOM   3163 C CA    . TRP A 1 455 ? 13.553 2.906   -3.565  1.00 25.56  ? 434  TRP A CA    1 
ATOM   3164 C C     . TRP A 1 455 ? 13.655 2.071   -4.841  1.00 24.81  ? 434  TRP A C     1 
ATOM   3165 O O     . TRP A 1 455 ? 13.180 0.942   -4.853  1.00 25.40  ? 434  TRP A O     1 
ATOM   3166 C CB    . TRP A 1 455 ? 14.450 2.350   -2.463  1.00 24.68  ? 434  TRP A CB    1 
ATOM   3167 C CG    . TRP A 1 455 ? 15.904 2.417   -2.844  1.00 23.50  ? 434  TRP A CG    1 
ATOM   3168 C CD1   . TRP A 1 455 ? 16.741 1.374   -3.154  1.00 21.62  ? 434  TRP A CD1   1 
ATOM   3169 C CD2   . TRP A 1 455 ? 16.677 3.618   -3.015  1.00 21.99  ? 434  TRP A CD2   1 
ATOM   3170 N NE1   . TRP A 1 455 ? 17.980 1.844   -3.488  1.00 22.41  ? 434  TRP A NE1   1 
ATOM   3171 C CE2   . TRP A 1 455 ? 17.968 3.211   -3.434  1.00 22.19  ? 434  TRP A CE2   1 
ATOM   3172 C CE3   . TRP A 1 455 ? 16.400 4.981   -2.887  1.00 23.48  ? 434  TRP A CE3   1 
ATOM   3173 C CZ2   . TRP A 1 455 ? 18.972 4.120   -3.701  1.00 24.33  ? 434  TRP A CZ2   1 
ATOM   3174 C CZ3   . TRP A 1 455 ? 17.406 5.880   -3.149  1.00 22.70  ? 434  TRP A CZ3   1 
ATOM   3175 C CH2   . TRP A 1 455 ? 18.650 5.453   -3.605  1.00 23.29  ? 434  TRP A CH2   1 
ATOM   3176 N N     . PRO A 1 456 ? 14.204 2.595   -5.966  1.00 24.08  ? 435  PRO A N     1 
ATOM   3177 C CA    . PRO A 1 456 ? 14.271 1.837   -7.221  1.00 24.58  ? 435  PRO A CA    1 
ATOM   3178 C C     . PRO A 1 456 ? 15.442 0.876   -7.408  1.00 26.24  ? 435  PRO A C     1 
ATOM   3179 O O     . PRO A 1 456 ? 15.522 0.174   -8.421  1.00 24.98  ? 435  PRO A O     1 
ATOM   3180 C CB    . PRO A 1 456 ? 14.362 2.962   -8.235  1.00 26.58  ? 435  PRO A CB    1 
ATOM   3181 C CG    . PRO A 1 456 ? 15.256 3.965   -7.547  1.00 26.76  ? 435  PRO A CG    1 
ATOM   3182 C CD    . PRO A 1 456 ? 14.720 3.963   -6.115  1.00 26.38  ? 435  PRO A CD    1 
ATOM   3183 N N     . GLY A 1 457 ? 16.370 0.898   -6.456  1.00 23.02  ? 436  GLY A N     1 
ATOM   3184 C CA    . GLY A 1 457 ? 17.574 0.103   -6.565  1.00 24.38  ? 436  GLY A CA    1 
ATOM   3185 C C     . GLY A 1 457 ? 18.593 0.832   -7.428  1.00 24.26  ? 436  GLY A C     1 
ATOM   3186 O O     . GLY A 1 457 ? 18.457 2.024   -7.665  1.00 25.33  ? 436  GLY A O     1 
ATOM   3187 N N     . PRO A 1 458 ? 19.676 0.160   -7.847  1.00 22.76  ? 437  PRO A N     1 
ATOM   3188 C CA    . PRO A 1 458 ? 20.769 0.822   -8.565  1.00 25.22  ? 437  PRO A CA    1 
ATOM   3189 C C     . PRO A 1 458 ? 20.297 1.432   -9.882  1.00 23.48  ? 437  PRO A C     1 
ATOM   3190 O O     . PRO A 1 458 ? 19.494 0.829   -10.600 1.00 26.16  ? 437  PRO A O     1 
ATOM   3191 C CB    . PRO A 1 458 ? 21.819 -0.312  -8.783  1.00 25.66  ? 437  PRO A CB    1 
ATOM   3192 C CG    . PRO A 1 458 ? 21.402 -1.432  -7.850  1.00 23.05  ? 437  PRO A CG    1 
ATOM   3193 C CD    . PRO A 1 458 ? 19.926 -1.267  -7.615  1.00 24.38  ? 437  PRO A CD    1 
ATOM   3194 N N     . VAL A 1 459 ? 20.747 2.670   -10.129 1.00 26.69  ? 438  VAL A N     1 
ATOM   3195 C CA    . VAL A 1 459 ? 20.489 3.403   -11.357 1.00 25.64  ? 438  VAL A CA    1 
ATOM   3196 C C     . VAL A 1 459 ? 21.837 3.960   -11.815 1.00 25.36  ? 438  VAL A C     1 
ATOM   3197 O O     . VAL A 1 459 ? 22.830 3.912   -11.071 1.00 24.22  ? 438  VAL A O     1 
ATOM   3198 C CB    . VAL A 1 459 ? 19.420 4.505   -11.172 1.00 27.25  ? 438  VAL A CB    1 
ATOM   3199 C CG1   . VAL A 1 459 ? 18.080 3.950   -10.695 1.00 26.15  ? 438  VAL A CG1   1 
ATOM   3200 C CG2   . VAL A 1 459 ? 19.908 5.601   -10.219 1.00 26.10  ? 438  VAL A CG2   1 
ATOM   3201 N N     . GLY A 1 460 ? 21.887 4.478   -13.050 1.00 27.08  ? 439  GLY A N     1 
ATOM   3202 C CA    . GLY A 1 460 ? 23.135 5.051   -13.556 1.00 28.76  ? 439  GLY A CA    1 
ATOM   3203 C C     . GLY A 1 460 ? 23.471 6.397   -12.899 1.00 30.17  ? 439  GLY A C     1 
ATOM   3204 O O     . GLY A 1 460 ? 22.694 6.958   -12.117 1.00 27.34  ? 439  GLY A O     1 
ATOM   3205 N N     . ASP A 1 461 ? 24.637 6.939   -13.245 1.00 31.13  ? 440  ASP A N     1 
ATOM   3206 C CA    . ASP A 1 461 ? 25.169 8.125   -12.584 1.00 36.34  ? 440  ASP A CA    1 
ATOM   3207 C C     . ASP A 1 461 ? 24.230 9.328   -12.662 1.00 36.43  ? 440  ASP A C     1 
ATOM   3208 O O     . ASP A 1 461 ? 23.911 9.917   -11.624 1.00 38.92  ? 440  ASP A O     1 
ATOM   3209 C CB    . ASP A 1 461 ? 26.590 8.387   -13.044 1.00 36.00  ? 440  ASP A CB    1 
ATOM   3210 C CG    . ASP A 1 461 ? 27.556 7.278   -12.671 1.00 39.32  ? 440  ASP A CG    1 
ATOM   3211 O OD1   . ASP A 1 461 ? 27.119 6.310   -12.026 1.00 43.71  ? 440  ASP A OD1   1 
ATOM   3212 O OD2   . ASP A 1 461 ? 28.741 7.386   -13.020 1.00 47.69  ? 440  ASP A OD2   1 
ATOM   3213 N N     . ASP A 1 462 ? 23.729 9.663   -13.857 1.00 39.70  ? 441  ASP A N     1 
ATOM   3214 C CA    . ASP A 1 462 ? 22.869 10.832  -13.998 1.00 40.78  ? 441  ASP A CA    1 
ATOM   3215 C C     . ASP A 1 462 ? 21.542 10.603  -13.292 1.00 38.76  ? 441  ASP A C     1 
ATOM   3216 O O     . ASP A 1 462 ? 21.032 11.507  -12.607 1.00 33.35  ? 441  ASP A O     1 
ATOM   3217 C CB    . ASP A 1 462 ? 22.697 11.287  -15.438 1.00 48.27  ? 441  ASP A CB    1 
ATOM   3218 C CG    . ASP A 1 462 ? 23.996 11.717  -16.114 1.00 56.31  ? 441  ASP A CG    1 
ATOM   3219 O OD1   . ASP A 1 462 ? 24.802 12.400  -15.456 1.00 58.04  ? 441  ASP A OD1   1 
ATOM   3220 O OD2   . ASP A 1 462 ? 24.216 11.347  -17.288 1.00 63.25  ? 441  ASP A OD2   1 
ATOM   3221 N N     . ALA A 1 463 ? 21.010 9.383   -13.452 1.00 32.39  ? 442  ALA A N     1 
ATOM   3222 C CA    . ALA A 1 463 ? 19.765 9.017   -12.800 1.00 29.74  ? 442  ALA A CA    1 
ATOM   3223 C C     . ALA A 1 463 ? 19.918 9.165   -11.281 1.00 27.22  ? 442  ALA A C     1 
ATOM   3224 O O     . ALA A 1 463 ? 18.943 9.471   -10.622 1.00 25.32  ? 442  ALA A O     1 
ATOM   3225 C CB    . ALA A 1 463 ? 19.336 7.600   -13.174 1.00 28.45  ? 442  ALA A CB    1 
ATOM   3226 N N     . LEU A 1 464 ? 21.124 8.912   -10.751 1.00 26.67  ? 443  LEU A N     1 
ATOM   3227 C CA    . LEU A 1 464 ? 21.326 8.842   -9.313  1.00 29.31  ? 443  LEU A CA    1 
ATOM   3228 C C     . LEU A 1 464 ? 21.199 10.250  -8.725  1.00 28.71  ? 443  LEU A C     1 
ATOM   3229 O O     . LEU A 1 464 ? 20.569 10.440  -7.694  1.00 26.99  ? 443  LEU A O     1 
ATOM   3230 C CB    . LEU A 1 464 ? 22.672 8.207   -8.975  1.00 28.09  ? 443  LEU A CB    1 
ATOM   3231 C CG    . LEU A 1 464 ? 22.982 8.110   -7.480  1.00 27.11  ? 443  LEU A CG    1 
ATOM   3232 C CD1   . LEU A 1 464 ? 21.813 7.463   -6.759  1.00 26.65  ? 443  LEU A CD1   1 
ATOM   3233 C CD2   . LEU A 1 464 ? 24.262 7.395   -7.242  1.00 27.48  ? 443  LEU A CD2   1 
ATOM   3234 N N     . GLU A 1 465 ? 21.712 11.240  -9.452  1.00 27.08  ? 444  GLU A N     1 
ATOM   3235 C CA    . GLU A 1 465 ? 21.613 12.613  -8.995  1.00 29.19  ? 444  GLU A CA    1 
ATOM   3236 C C     . GLU A 1 465 ? 20.147 13.009  -8.893  1.00 28.66  ? 444  GLU A C     1 
ATOM   3237 O O     . GLU A 1 465 ? 19.753 13.598  -7.881  1.00 29.99  ? 444  GLU A O     1 
ATOM   3238 C CB    . GLU A 1 465 ? 22.475 13.515  -9.864  1.00 29.94  ? 444  GLU A CB    1 
ATOM   3239 C CG    . GLU A 1 465 ? 23.954 13.204  -9.672  1.00 32.97  ? 444  GLU A CG    1 
ATOM   3240 C CD    . GLU A 1 465 ? 24.881 14.233  -10.289 1.00 40.11  ? 444  GLU A CD    1 
ATOM   3241 O OE1   . GLU A 1 465 ? 26.097 14.184  -10.008 1.00 46.99  ? 444  GLU A OE1   1 
ATOM   3242 O OE2   . GLU A 1 465 ? 24.366 15.088  -11.044 1.00 42.10  ? 444  GLU A OE2   1 
ATOM   3243 N N     . ARG A 1 466 ? 19.336 12.641  -9.899  1.00 28.14  ? 445  ARG A N     1 
ATOM   3244 C CA    . ARG A 1 466 ? 17.915 12.960  -9.883  1.00 30.64  ? 445  ARG A CA    1 
ATOM   3245 C C     . ARG A 1 466 ? 17.220 12.211  -8.749  1.00 28.28  ? 445  ARG A C     1 
ATOM   3246 O O     . ARG A 1 466 ? 16.358 12.785  -8.108  1.00 25.45  ? 445  ARG A O     1 
ATOM   3247 C CB    . ARG A 1 466 ? 17.145 12.664  -11.170 1.00 31.63  ? 445  ARG A CB    1 
ATOM   3248 C CG    . ARG A 1 466 ? 17.562 13.642  -12.260 1.00 38.79  ? 445  ARG A CG    1 
ATOM   3249 C CD    . ARG A 1 466 ? 16.941 13.382  -13.642 1.00 45.09  ? 445  ARG A CD    1 
ATOM   3250 N NE    . ARG A 1 466 ? 16.903 11.963  -14.029 1.00 46.28  ? 445  ARG A NE    1 
ATOM   3251 C CZ    . ARG A 1 466 ? 17.675 11.305  -14.892 1.00 47.58  ? 445  ARG A CZ    1 
ATOM   3252 N NH1   . ARG A 1 466 ? 18.747 11.871  -15.417 1.00 48.71  ? 445  ARG A NH1   1 
ATOM   3253 N NH2   . ARG A 1 466 ? 17.397 10.040  -15.167 1.00 52.67  ? 445  ARG A NH2   1 
ATOM   3254 N N     . LEU A 1 467 ? 17.587 10.943  -8.520  1.00 25.26  ? 446  LEU A N     1 
ATOM   3255 C CA    . LEU A 1 467 ? 17.004 10.148  -7.441  1.00 25.51  ? 446  LEU A CA    1 
ATOM   3256 C C     . LEU A 1 467 ? 17.298 10.761  -6.063  1.00 25.14  ? 446  LEU A C     1 
ATOM   3257 O O     . LEU A 1 467 ? 16.423 10.801  -5.206  1.00 26.16  ? 446  LEU A O     1 
ATOM   3258 C CB    . LEU A 1 467 ? 17.527 8.717   -7.525  1.00 26.13  ? 446  LEU A CB    1 
ATOM   3259 C CG    . LEU A 1 467 ? 16.999 7.743   -6.466  1.00 24.94  ? 446  LEU A CG    1 
ATOM   3260 C CD1   . LEU A 1 467 ? 15.495 7.573   -6.584  1.00 24.12  ? 446  LEU A CD1   1 
ATOM   3261 C CD2   . LEU A 1 467 ? 17.720 6.440   -6.597  1.00 26.75  ? 446  LEU A CD2   1 
ATOM   3262 N N     . VAL A 1 468 ? 18.542 11.193  -5.830  1.00 23.79  ? 447  VAL A N     1 
ATOM   3263 C CA    . VAL A 1 468 ? 18.900 11.890  -4.609  1.00 22.43  ? 447  VAL A CA    1 
ATOM   3264 C C     . VAL A 1 468 ? 17.947 13.066  -4.354  1.00 25.40  ? 447  VAL A C     1 
ATOM   3265 O O     . VAL A 1 468 ? 17.347 13.190  -3.276  1.00 21.60  ? 447  VAL A O     1 
ATOM   3266 C CB    . VAL A 1 468 ? 20.387 12.299  -4.658  1.00 23.43  ? 447  VAL A CB    1 
ATOM   3267 C CG1   . VAL A 1 468 ? 20.748 13.307  -3.580  1.00 25.17  ? 447  VAL A CG1   1 
ATOM   3268 C CG2   . VAL A 1 468 ? 21.283 11.092  -4.477  1.00 23.48  ? 447  VAL A CG2   1 
ATOM   3269 N N     . ARG A 1 469 ? 17.756 13.930  -5.355  1.00 22.49  ? 448  ARG A N     1 
ATOM   3270 C CA    . ARG A 1 469 ? 16.861 15.055  -5.183  1.00 22.50  ? 448  ARG A CA    1 
ATOM   3271 C C     . ARG A 1 469 ? 15.432 14.595  -4.923  1.00 26.31  ? 448  ARG A C     1 
ATOM   3272 O O     . ARG A 1 469 ? 14.661 15.312  -4.273  1.00 23.41  ? 448  ARG A O     1 
ATOM   3273 C CB    . ARG A 1 469 ? 16.847 15.982  -6.404  1.00 23.55  ? 448  ARG A CB    1 
ATOM   3274 C CG    . ARG A 1 469 ? 18.172 16.662  -6.683  1.00 22.56  ? 448  ARG A CG    1 
ATOM   3275 C CD    . ARG A 1 469 ? 18.031 17.733  -7.799  1.00 25.15  ? 448  ARG A CD    1 
ATOM   3276 N NE    . ARG A 1 469 ? 19.349 18.337  -8.030  1.00 25.01  ? 448  ARG A NE    1 
ATOM   3277 C CZ    . ARG A 1 469 ? 19.884 19.355  -7.345  1.00 27.55  ? 448  ARG A CZ    1 
ATOM   3278 N NH1   . ARG A 1 469 ? 19.288 19.844  -6.264  1.00 28.24  ? 448  ARG A NH1   1 
ATOM   3279 N NH2   . ARG A 1 469 ? 21.042 19.874  -7.721  1.00 28.56  ? 448  ARG A NH2   1 
ATOM   3280 N N     . GLU A 1 470 ? 15.034 13.452  -5.498  1.00 24.23  ? 449  GLU A N     1 
ATOM   3281 C CA    . GLU A 1 470 ? 13.665 13.002  -5.336  1.00 23.87  ? 449  GLU A CA    1 
ATOM   3282 C C     . GLU A 1 470 ? 13.434 12.388  -3.955  1.00 21.59  ? 449  GLU A C     1 
ATOM   3283 O O     . GLU A 1 470 ? 12.297 12.375  -3.500  1.00 25.51  ? 449  GLU A O     1 
ATOM   3284 C CB    . GLU A 1 470 ? 13.263 11.932  -6.361  1.00 29.04  ? 449  GLU A CB    1 
ATOM   3285 C CG    . GLU A 1 470 ? 13.178 12.458  -7.794  1.00 35.42  ? 449  GLU A CG    1 
ATOM   3286 C CD    . GLU A 1 470 ? 13.009 11.352  -8.837  1.00 40.82  ? 449  GLU A CD    1 
ATOM   3287 O OE1   . GLU A 1 470 ? 12.688 11.716  -9.975  1.00 43.32  ? 449  GLU A OE1   1 
ATOM   3288 O OE2   . GLU A 1 470 ? 13.194 10.150  -8.532  1.00 42.11  ? 449  GLU A OE2   1 
ATOM   3289 N N     . ARG A 1 471 ? 14.473 11.867  -3.298  1.00 22.26  ? 450  ARG A N     1 
ATOM   3290 C CA    . ARG A 1 471 ? 14.290 11.070  -2.085  1.00 22.36  ? 450  ARG A CA    1 
ATOM   3291 C C     . ARG A 1 471 ? 14.872 11.727  -0.828  1.00 21.62  ? 450  ARG A C     1 
ATOM   3292 O O     . ARG A 1 471 ? 14.599 11.299  0.289   1.00 19.36  ? 450  ARG A O     1 
ATOM   3293 C CB    . ARG A 1 471 ? 14.966 9.709   -2.213  1.00 22.38  ? 450  ARG A CB    1 
ATOM   3294 C CG    . ARG A 1 471 ? 14.471 8.866   -3.382  1.00 27.29  ? 450  ARG A CG    1 
ATOM   3295 C CD    . ARG A 1 471 ? 12.992 8.598   -3.321  1.00 30.18  ? 450  ARG A CD    1 
ATOM   3296 N NE    . ARG A 1 471 ? 12.694 7.892   -2.068  1.00 31.92  ? 450  ARG A NE    1 
ATOM   3297 C CZ    . ARG A 1 471 ? 11.501 7.753   -1.494  1.00 37.72  ? 450  ARG A CZ    1 
ATOM   3298 N NH1   . ARG A 1 471 ? 10.416 8.239   -2.055  1.00 34.40  ? 450  ARG A NH1   1 
ATOM   3299 N NH2   . ARG A 1 471 ? 11.385 7.107   -0.347  1.00 36.22  ? 450  ARG A NH2   1 
ATOM   3300 N N     . ALA A 1 472 ? 15.744 12.711  -0.971  1.00 22.20  ? 451  ALA A N     1 
ATOM   3301 C CA    . ALA A 1 472 ? 16.417 13.276  0.197   1.00 21.02  ? 451  ALA A CA    1 
ATOM   3302 C C     . ALA A 1 472 ? 15.404 13.916  1.145   1.00 21.90  ? 451  ALA A C     1 
ATOM   3303 O O     . ALA A 1 472 ? 14.424 14.502  0.713   1.00 19.43  ? 451  ALA A O     1 
ATOM   3304 C CB    . ALA A 1 472 ? 17.455 14.284  -0.224  1.00 22.39  ? 451  ALA A CB    1 
ATOM   3305 N N     . SER A 1 473 ? 15.666 13.819  2.461   1.00 19.53  ? 452  SER A N     1 
ATOM   3306 C CA    . SER A 1 473 ? 14.791 14.426  3.445   1.00 19.51  ? 452  SER A CA    1 
ATOM   3307 C C     . SER A 1 473 ? 15.596 14.804  4.687   1.00 19.20  ? 452  SER A C     1 
ATOM   3308 O O     . SER A 1 473 ? 16.759 14.399  4.809   1.00 20.94  ? 452  SER A O     1 
ATOM   3309 C CB    . SER A 1 473 ? 13.633 13.506  3.748   1.00 19.71  ? 452  SER A CB    1 
ATOM   3310 O OG    . SER A 1 473 ? 12.718 14.166  4.610   1.00 19.89  ? 452  SER A OG    1 
ATOM   3311 N N     . THR A 1 474 ? 14.996 15.571  5.609   1.00 19.42  ? 453  THR A N     1 
ATOM   3312 C CA    . THR A 1 474 ? 15.689 15.976  6.834   1.00 18.84  ? 453  THR A CA    1 
ATOM   3313 C C     . THR A 1 474 ? 16.112 14.765  7.654   1.00 19.57  ? 453  THR A C     1 
ATOM   3314 O O     . THR A 1 474 ? 15.376 13.785  7.737   1.00 18.87  ? 453  THR A O     1 
ATOM   3315 C CB    . THR A 1 474 ? 14.809 16.913  7.669   1.00 19.54  ? 453  THR A CB    1 
ATOM   3316 O OG1   . THR A 1 474 ? 15.575 17.444  8.762   1.00 17.34  ? 453  THR A OG1   1 
ATOM   3317 C CG2   . THR A 1 474 ? 13.490 16.300  8.116   1.00 19.86  ? 453  THR A CG2   1 
ATOM   3318 N N     . LEU A 1 475 ? 17.224 14.908  8.385   1.00 18.47  ? 454  LEU A N     1 
ATOM   3319 C CA    . LEU A 1 475 ? 17.573 13.951  9.423   1.00 18.62  ? 454  LEU A CA    1 
ATOM   3320 C C     . LEU A 1 475 ? 17.431 14.567  10.825  1.00 19.13  ? 454  LEU A C     1 
ATOM   3321 O O     . LEU A 1 475 ? 17.985 14.036  11.782  1.00 22.25  ? 454  LEU A O     1 
ATOM   3322 C CB    . LEU A 1 475 ? 18.972 13.377  9.207   1.00 17.60  ? 454  LEU A CB    1 
ATOM   3323 C CG    . LEU A 1 475 ? 19.290 12.167  10.082  1.00 19.76  ? 454  LEU A CG    1 
ATOM   3324 C CD1   . LEU A 1 475 ? 18.512 10.967  9.542   1.00 21.71  ? 454  LEU A CD1   1 
ATOM   3325 C CD2   . LEU A 1 475 ? 20.800 11.907  10.155  1.00 22.43  ? 454  LEU A CD2   1 
ATOM   3326 N N     . PHE A 1 476 ? 16.655 15.646  10.941  1.00 17.62  ? 455  PHE A N     1 
ATOM   3327 C CA    . PHE A 1 476 ? 16.133 16.154  12.197  1.00 17.82  ? 455  PHE A CA    1 
ATOM   3328 C C     . PHE A 1 476 ? 17.193 16.858  13.041  1.00 18.18  ? 455  PHE A C     1 
ATOM   3329 O O     . PHE A 1 476 ? 16.984 16.993  14.251  1.00 15.69  ? 455  PHE A O     1 
ATOM   3330 C CB    . PHE A 1 476 ? 15.479 15.061  13.063  1.00 20.32  ? 455  PHE A CB    1 
ATOM   3331 C CG    . PHE A 1 476 ? 14.625 14.094  12.259  1.00 21.15  ? 455  PHE A CG    1 
ATOM   3332 C CD1   . PHE A 1 476 ? 13.461 14.513  11.639  1.00 24.36  ? 455  PHE A CD1   1 
ATOM   3333 C CD2   . PHE A 1 476 ? 15.063 12.801  12.024  1.00 25.23  ? 455  PHE A CD2   1 
ATOM   3334 C CE1   . PHE A 1 476 ? 12.691 13.636  10.879  1.00 21.85  ? 455  PHE A CE1   1 
ATOM   3335 C CE2   . PHE A 1 476 ? 14.318 11.933  11.229  1.00 24.58  ? 455  PHE A CE2   1 
ATOM   3336 C CZ    . PHE A 1 476 ? 13.129 12.351  10.669  1.00 22.97  ? 455  PHE A CZ    1 
ATOM   3337 N N     . HIS A 1 477 ? 18.257 17.397  12.407  1.00 16.81  ? 456  HIS A N     1 
ATOM   3338 C CA    . HIS A 1 477 ? 19.361 18.002  13.130  1.00 17.30  ? 456  HIS A CA    1 
ATOM   3339 C C     . HIS A 1 477 ? 19.534 19.484  12.755  1.00 17.69  ? 456  HIS A C     1 
ATOM   3340 O O     . HIS A 1 477 ? 20.645 19.913  12.442  1.00 17.65  ? 456  HIS A O     1 
ATOM   3341 C CB    . HIS A 1 477 ? 20.653 17.238  12.827  1.00 15.83  ? 456  HIS A CB    1 
ATOM   3342 C CG    . HIS A 1 477 ? 20.652 15.825  13.268  1.00 16.85  ? 456  HIS A CG    1 
ATOM   3343 N ND1   . HIS A 1 477 ? 21.498 14.867  12.735  1.00 17.87  ? 456  HIS A ND1   1 
ATOM   3344 C CD2   . HIS A 1 477 ? 19.903 15.194  14.202  1.00 18.01  ? 456  HIS A CD2   1 
ATOM   3345 C CE1   . HIS A 1 477 ? 21.231 13.690  13.304  1.00 18.90  ? 456  HIS A CE1   1 
ATOM   3346 N NE2   . HIS A 1 477 ? 20.272 13.872  14.202  1.00 19.83  ? 456  HIS A NE2   1 
ATOM   3347 N N     . PRO A 1 478 ? 18.471 20.322  12.761  1.00 17.82  ? 457  PRO A N     1 
ATOM   3348 C CA    . PRO A 1 478 ? 18.609 21.726  12.381  1.00 18.61  ? 457  PRO A CA    1 
ATOM   3349 C C     . PRO A 1 478 ? 19.323 22.580  13.432  1.00 19.43  ? 457  PRO A C     1 
ATOM   3350 O O     . PRO A 1 478 ? 19.027 22.466  14.618  1.00 18.48  ? 457  PRO A O     1 
ATOM   3351 C CB    . PRO A 1 478 ? 17.148 22.157  12.177  1.00 18.05  ? 457  PRO A CB    1 
ATOM   3352 C CG    . PRO A 1 478 ? 16.360 21.296  13.148  1.00 17.75  ? 457  PRO A CG    1 
ATOM   3353 C CD    . PRO A 1 478 ? 17.061 19.967  13.077  1.00 18.25  ? 457  PRO A CD    1 
ATOM   3354 N N     . VAL A 1 479 ? 20.246 23.443  12.966  1.00 16.94  ? 458  VAL A N     1 
ATOM   3355 C CA    . VAL A 1 479 ? 21.058 24.263  13.859  1.00 18.93  ? 458  VAL A CA    1 
ATOM   3356 C C     . VAL A 1 479 ? 21.270 25.638  13.225  1.00 17.86  ? 458  VAL A C     1 
ATOM   3357 O O     . VAL A 1 479 ? 21.031 25.791  12.042  1.00 16.09  ? 458  VAL A O     1 
ATOM   3358 C CB    . VAL A 1 479 ? 22.417 23.597  14.109  1.00 19.14  ? 458  VAL A CB    1 
ATOM   3359 C CG1   . VAL A 1 479 ? 22.235 22.152  14.569  1.00 20.00  ? 458  VAL A CG1   1 
ATOM   3360 C CG2   . VAL A 1 479 ? 23.306 23.703  12.875  1.00 19.49  ? 458  VAL A CG2   1 
ATOM   3361 N N     . GLY A 1 480 ? 21.674 26.630  14.023  1.00 19.04  ? 459  GLY A N     1 
ATOM   3362 C CA    . GLY A 1 480 ? 22.519 27.714  13.520  1.00 19.34  ? 459  GLY A CA    1 
ATOM   3363 C C     . GLY A 1 480 ? 21.808 29.051  13.312  1.00 18.66  ? 459  GLY A C     1 
ATOM   3364 O O     . GLY A 1 480 ? 22.460 30.018  12.915  1.00 21.25  ? 459  GLY A O     1 
ATOM   3365 N N     . THR A 1 481 ? 20.501 29.125  13.617  1.00 17.92  ? 460  THR A N     1 
ATOM   3366 C CA    . THR A 1 481 ? 19.701 30.320  13.392  1.00 17.26  ? 460  THR A CA    1 
ATOM   3367 C C     . THR A 1 481 ? 19.951 31.451  14.402  1.00 19.40  ? 460  THR A C     1 
ATOM   3368 O O     . THR A 1 481 ? 19.438 32.555  14.182  1.00 18.20  ? 460  THR A O     1 
ATOM   3369 C CB    . THR A 1 481 ? 18.230 29.911  13.403  1.00 18.25  ? 460  THR A CB    1 
ATOM   3370 O OG1   . THR A 1 481 ? 18.011 29.138  14.596  1.00 16.10  ? 460  THR A OG1   1 
ATOM   3371 C CG2   . THR A 1 481 ? 17.893 29.082  12.179  1.00 19.31  ? 460  THR A CG2   1 
ATOM   3372 N N     . CYS A 1 482 ? 20.662 31.177  15.514  1.00 18.01  ? 461  CYS A N     1 
ATOM   3373 C CA    . CYS A 1 482 ? 21.049 32.200  16.479  1.00 18.35  ? 461  CYS A CA    1 
ATOM   3374 C C     . CYS A 1 482 ? 22.553 32.088  16.743  1.00 19.53  ? 461  CYS A C     1 
ATOM   3375 O O     . CYS A 1 482 ? 23.001 31.976  17.869  1.00 19.49  ? 461  CYS A O     1 
ATOM   3376 C CB    . CYS A 1 482 ? 20.295 32.042  17.787  1.00 19.20  ? 461  CYS A CB    1 
ATOM   3377 S SG    . CYS A 1 482 ? 18.499 32.251  17.613  1.00 18.89  ? 461  CYS A SG    1 
ATOM   3378 N N     . ARG A 1 483 ? 23.322 32.135  15.657  1.00 20.15  ? 462  ARG A N     1 
ATOM   3379 C CA    . ARG A 1 483 ? 24.718 31.743  15.657  1.00 21.76  ? 462  ARG A CA    1 
ATOM   3380 C C     . ARG A 1 483 ? 25.549 32.581  16.629  1.00 21.60  ? 462  ARG A C     1 
ATOM   3381 O O     . ARG A 1 483 ? 25.433 33.822  16.706  1.00 21.43  ? 462  ARG A O     1 
ATOM   3382 C CB    . ARG A 1 483 ? 25.262 31.925  14.238  1.00 23.46  ? 462  ARG A CB    1 
ATOM   3383 C CG    . ARG A 1 483 ? 26.751 31.674  14.141  1.00 31.05  ? 462  ARG A CG    1 
ATOM   3384 C CD    . ARG A 1 483 ? 27.318 31.700  12.743  1.00 33.03  ? 462  ARG A CD    1 
ATOM   3385 N NE    . ARG A 1 483 ? 27.445 33.001  12.105  1.00 32.29  ? 462  ARG A NE    1 
ATOM   3386 C CZ    . ARG A 1 483 ? 28.267 34.023  12.394  1.00 35.94  ? 462  ARG A CZ    1 
ATOM   3387 N NH1   . ARG A 1 483 ? 29.020 34.048  13.513  1.00 31.62  ? 462  ARG A NH1   1 
ATOM   3388 N NH2   . ARG A 1 483 ? 28.249 35.051  11.546  1.00 34.64  ? 462  ARG A NH2   1 
ATOM   3389 N N     . MET A 1 484 ? 26.465 31.893  17.298  1.00 19.59  ? 463  MET A N     1 
ATOM   3390 C CA    . MET A 1 484 ? 27.441 32.575  18.129  1.00 22.05  ? 463  MET A CA    1 
ATOM   3391 C C     . MET A 1 484 ? 28.512 33.253  17.271  1.00 21.46  ? 463  MET A C     1 
ATOM   3392 O O     . MET A 1 484 ? 28.927 32.753  16.214  1.00 22.81  ? 463  MET A O     1 
ATOM   3393 C CB    . MET A 1 484 ? 28.138 31.621  19.106  1.00 22.87  ? 463  MET A CB    1 
ATOM   3394 C CG    . MET A 1 484 ? 28.895 30.477  18.473  1.00 24.31  ? 463  MET A CG    1 
ATOM   3395 S SD    . MET A 1 484 ? 29.716 29.438  19.706  1.00 26.51  ? 463  MET A SD    1 
ATOM   3396 C CE    . MET A 1 484 ? 28.353 28.571  20.513  1.00 28.51  ? 463  MET A CE    1 
ATOM   3397 N N     . GLY A 1 485 ? 29.022 34.358  17.807  1.00 21.74  ? 464  GLY A N     1 
ATOM   3398 C CA    . GLY A 1 485 ? 30.164 35.025  17.223  1.00 23.13  ? 464  GLY A CA    1 
ATOM   3399 C C     . GLY A 1 485 ? 30.559 36.272  18.001  1.00 23.38  ? 464  GLY A C     1 
ATOM   3400 O O     . GLY A 1 485 ? 29.786 36.835  18.779  1.00 23.26  ? 464  GLY A O     1 
ATOM   3401 N N     . ARG A 1 486 ? 31.785 36.711  17.736  1.00 27.25  ? 465  ARG A N     1 
ATOM   3402 C CA    . ARG A 1 486 ? 32.391 37.841  18.428  1.00 27.71  ? 465  ARG A CA    1 
ATOM   3403 C C     . ARG A 1 486 ? 31.738 39.127  17.964  1.00 28.02  ? 465  ARG A C     1 
ATOM   3404 O O     . ARG A 1 486 ? 31.226 39.198  16.847  1.00 29.27  ? 465  ARG A O     1 
ATOM   3405 C CB    . ARG A 1 486 ? 33.888 37.928  18.122  1.00 30.41  ? 465  ARG A CB    1 
ATOM   3406 C CG    . ARG A 1 486 ? 34.711 36.974  18.971  1.00 39.22  ? 465  ARG A CG    1 
ATOM   3407 C CD    . ARG A 1 486 ? 36.163 37.449  19.021  1.00 46.37  ? 465  ARG A CD    1 
ATOM   3408 N NE    . ARG A 1 486 ? 37.048 36.290  18.933  1.00 50.34  ? 465  ARG A NE    1 
ATOM   3409 C CZ    . ARG A 1 486 ? 37.157 35.486  17.882  1.00 47.10  ? 465  ARG A CZ    1 
ATOM   3410 N NH1   . ARG A 1 486 ? 36.650 35.807  16.707  1.00 48.98  ? 465  ARG A NH1   1 
ATOM   3411 N NH2   . ARG A 1 486 ? 37.822 34.363  18.010  1.00 47.99  ? 465  ARG A NH2   1 
ATOM   3412 N N     . ALA A 1 487 ? 31.739 40.132  18.849  1.00 31.35  ? 466  ALA A N     1 
ATOM   3413 C CA    . ALA A 1 487 ? 31.395 41.490  18.467  1.00 32.00  ? 466  ALA A CA    1 
ATOM   3414 C C     . ALA A 1 487 ? 32.202 41.868  17.225  1.00 33.46  ? 466  ALA A C     1 
ATOM   3415 O O     . ALA A 1 487 ? 33.405 41.600  17.157  1.00 37.48  ? 466  ALA A O     1 
ATOM   3416 C CB    . ALA A 1 487 ? 31.689 42.441  19.626  1.00 33.00  ? 466  ALA A CB    1 
ATOM   3417 N N     . GLY A 1 488 ? 31.532 42.472  16.245  1.00 32.32  ? 467  GLY A N     1 
ATOM   3418 C CA    . GLY A 1 488 ? 32.176 42.849  14.997  1.00 31.49  ? 467  GLY A CA    1 
ATOM   3419 C C     . GLY A 1 488 ? 31.742 41.918  13.867  1.00 34.52  ? 467  GLY A C     1 
ATOM   3420 O O     . GLY A 1 488 ? 31.835 42.255  12.695  1.00 30.31  ? 467  GLY A O     1 
ATOM   3421 N N     . ASP A 1 489 ? 31.239 40.729  14.223  1.00 29.29  ? 468  ASP A N     1 
ATOM   3422 C CA    . ASP A 1 489 ? 30.814 39.768  13.217  1.00 28.36  ? 468  ASP A CA    1 
ATOM   3423 C C     . ASP A 1 489 ? 29.340 40.067  12.968  1.00 27.34  ? 468  ASP A C     1 
ATOM   3424 O O     . ASP A 1 489 ? 28.500 39.746  13.805  1.00 23.99  ? 468  ASP A O     1 
ATOM   3425 C CB    . ASP A 1 489 ? 31.201 38.381  13.721  1.00 28.69  ? 468  ASP A CB    1 
ATOM   3426 C CG    . ASP A 1 489 ? 30.658 37.168  12.988  1.00 27.87  ? 468  ASP A CG    1 
ATOM   3427 O OD1   . ASP A 1 489 ? 29.922 37.344  12.003  1.00 26.46  ? 468  ASP A OD1   1 
ATOM   3428 O OD2   . ASP A 1 489 ? 31.038 36.056  13.400  1.00 28.98  ? 468  ASP A OD2   1 
ATOM   3429 N N     . GLU A 1 490 ? 29.024 40.657  11.817  1.00 26.69  ? 469  GLU A N     1 
ATOM   3430 C CA    . GLU A 1 490 ? 27.744 41.334  11.607  1.00 36.51  ? 469  GLU A CA    1 
ATOM   3431 C C     . GLU A 1 490 ? 26.522 40.390  11.668  1.00 32.77  ? 469  GLU A C     1 
ATOM   3432 O O     . GLU A 1 490 ? 25.421 40.810  12.055  1.00 33.43  ? 469  GLU A O     1 
ATOM   3433 C CB    . GLU A 1 490 ? 27.809 42.057  10.257  1.00 39.52  ? 469  GLU A CB    1 
ATOM   3434 C CG    . GLU A 1 490 ? 26.547 42.850  9.921   1.00 42.88  ? 469  GLU A CG    1 
ATOM   3435 C CD    . GLU A 1 490 ? 26.140 43.914  10.941  1.00 52.48  ? 469  GLU A CD    1 
ATOM   3436 O OE1   . GLU A 1 490 ? 26.975 44.300  11.797  1.00 48.45  ? 469  GLU A OE1   1 
ATOM   3437 O OE2   . GLU A 1 490 ? 24.963 44.349  10.892  1.00 46.40  ? 469  GLU A OE2   1 
ATOM   3438 N N     . GLN A 1 491 ? 26.715 39.141  11.257  1.00 26.23  ? 470  GLN A N     1 
ATOM   3439 C CA    . GLN A 1 491 ? 25.664 38.143  11.240  1.00 33.05  ? 470  GLN A CA    1 
ATOM   3440 C C     . GLN A 1 491 ? 25.740 37.229  12.485  1.00 31.00  ? 470  GLN A C     1 
ATOM   3441 O O     . GLN A 1 491 ? 25.034 36.217  12.564  1.00 30.16  ? 470  GLN A O     1 
ATOM   3442 C CB    . GLN A 1 491 ? 25.752 37.391  9.898   1.00 34.09  ? 470  GLN A CB    1 
ATOM   3443 C CG    . GLN A 1 491 ? 25.648 38.264  8.641   1.00 37.56  ? 470  GLN A CG    1 
ATOM   3444 C CD    . GLN A 1 491 ? 24.283 38.876  8.401   1.00 38.40  ? 470  GLN A CD    1 
ATOM   3445 O OE1   . GLN A 1 491 ? 23.295 38.477  9.014   1.00 40.24  ? 470  GLN A OE1   1 
ATOM   3446 N NE2   . GLN A 1 491 ? 24.197 39.876  7.527   1.00 41.85  ? 470  GLN A NE2   1 
ATOM   3447 N N     . ALA A 1 492 ? 26.595 37.544  13.470  1.00 24.29  ? 471  ALA A N     1 
ATOM   3448 C CA    . ALA A 1 492 ? 26.517 36.850  14.744  1.00 24.97  ? 471  ALA A CA    1 
ATOM   3449 C C     . ALA A 1 492 ? 25.256 37.297  15.498  1.00 21.47  ? 471  ALA A C     1 
ATOM   3450 O O     . ALA A 1 492 ? 24.898 38.469  15.485  1.00 21.99  ? 471  ALA A O     1 
ATOM   3451 C CB    . ALA A 1 492 ? 27.760 37.076  15.562  1.00 26.09  ? 471  ALA A CB    1 
ATOM   3452 N N     . VAL A 1 493 ? 24.614 36.362  16.194  1.00 18.93  ? 472  VAL A N     1 
ATOM   3453 C CA    . VAL A 1 493 ? 23.428 36.660  16.984  1.00 19.01  ? 472  VAL A CA    1 
ATOM   3454 C C     . VAL A 1 493 ? 23.741 36.737  18.471  1.00 20.62  ? 472  VAL A C     1 
ATOM   3455 O O     . VAL A 1 493 ? 23.283 37.642  19.167  1.00 19.50  ? 472  VAL A O     1 
ATOM   3456 C CB    . VAL A 1 493 ? 22.342 35.613  16.706  1.00 19.52  ? 472  VAL A CB    1 
ATOM   3457 C CG1   . VAL A 1 493 ? 21.125 35.850  17.587  1.00 17.63  ? 472  VAL A CG1   1 
ATOM   3458 C CG2   . VAL A 1 493 ? 21.954 35.630  15.224  1.00 21.55  ? 472  VAL A CG2   1 
ATOM   3459 N N     . VAL A 1 494 ? 24.503 35.766  18.977  1.00 19.53  ? 473  VAL A N     1 
ATOM   3460 C CA    . VAL A 1 494 ? 24.920 35.809  20.363  1.00 18.54  ? 473  VAL A CA    1 
ATOM   3461 C C     . VAL A 1 494 ? 26.437 35.930  20.395  1.00 21.63  ? 473  VAL A C     1 
ATOM   3462 O O     . VAL A 1 494 ? 27.134 35.524  19.455  1.00 20.25  ? 473  VAL A O     1 
ATOM   3463 C CB    . VAL A 1 494 ? 24.422 34.582  21.156  1.00 18.96  ? 473  VAL A CB    1 
ATOM   3464 C CG1   . VAL A 1 494 ? 22.900 34.508  21.130  1.00 19.04  ? 473  VAL A CG1   1 
ATOM   3465 C CG2   . VAL A 1 494 ? 25.019 33.264  20.685  1.00 19.06  ? 473  VAL A CG2   1 
ATOM   3466 N N     . ASP A 1 495 ? 26.936 36.410  21.528  1.00 23.41  ? 474  ASP A N     1 
ATOM   3467 C CA    . ASP A 1 495 ? 28.372 36.521  21.742  1.00 23.85  ? 474  ASP A CA    1 
ATOM   3468 C C     . ASP A 1 495 ? 28.919 35.199  22.280  1.00 23.68  ? 474  ASP A C     1 
ATOM   3469 O O     . ASP A 1 495 ? 28.177 34.230  22.498  1.00 22.69  ? 474  ASP A O     1 
ATOM   3470 C CB    . ASP A 1 495 ? 28.691 37.752  22.594  1.00 23.18  ? 474  ASP A CB    1 
ATOM   3471 C CG    . ASP A 1 495 ? 28.369 37.649  24.081  1.00 25.88  ? 474  ASP A CG    1 
ATOM   3472 O OD1   . ASP A 1 495 ? 27.954 36.573  24.549  1.00 22.88  ? 474  ASP A OD1   1 
ATOM   3473 O OD2   . ASP A 1 495 ? 28.511 38.668  24.785  1.00 22.13  ? 474  ASP A OD2   1 
ATOM   3474 N N     . PRO A 1 496 ? 30.242 35.101  22.564  1.00 23.90  ? 475  PRO A N     1 
ATOM   3475 C CA    . PRO A 1 496 ? 30.818 33.834  23.023  1.00 21.93  ? 475  PRO A CA    1 
ATOM   3476 C C     . PRO A 1 496 ? 30.262 33.376  24.371  1.00 20.79  ? 475  PRO A C     1 
ATOM   3477 O O     . PRO A 1 496 ? 30.368 32.205  24.721  1.00 22.72  ? 475  PRO A O     1 
ATOM   3478 C CB    . PRO A 1 496 ? 32.341 34.121  23.070  1.00 22.48  ? 475  PRO A CB    1 
ATOM   3479 C CG    . PRO A 1 496 ? 32.515 35.293  22.114  1.00 23.68  ? 475  PRO A CG    1 
ATOM   3480 C CD    . PRO A 1 496 ? 31.276 36.137  22.341  1.00 25.24  ? 475  PRO A CD    1 
ATOM   3481 N N     . TRP A 1 497 ? 29.664 34.305  25.125  1.00 21.27  ? 476  TRP A N     1 
ATOM   3482 C CA    . TRP A 1 497 ? 28.993 33.992  26.381  1.00 21.67  ? 476  TRP A CA    1 
ATOM   3483 C C     . TRP A 1 497 ? 27.505 33.737  26.163  1.00 19.83  ? 476  TRP A C     1 
ATOM   3484 O O     . TRP A 1 497 ? 26.773 33.633  27.145  1.00 20.61  ? 476  TRP A O     1 
ATOM   3485 C CB    . TRP A 1 497 ? 29.249 35.114  27.403  1.00 26.50  ? 476  TRP A CB    1 
ATOM   3486 C CG    . TRP A 1 497 ? 30.718 35.185  27.693  1.00 29.18  ? 476  TRP A CG    1 
ATOM   3487 C CD1   . TRP A 1 497 ? 31.414 34.441  28.598  1.00 31.03  ? 476  TRP A CD1   1 
ATOM   3488 C CD2   . TRP A 1 497 ? 31.685 35.945  26.934  1.00 32.09  ? 476  TRP A CD2   1 
ATOM   3489 N NE1   . TRP A 1 497 ? 32.752 34.711  28.475  1.00 35.01  ? 476  TRP A NE1   1 
ATOM   3490 C CE2   . TRP A 1 497 ? 32.952 35.626  27.468  1.00 34.70  ? 476  TRP A CE2   1 
ATOM   3491 C CE3   . TRP A 1 497 ? 31.601 36.867  25.886  1.00 31.57  ? 476  TRP A CE3   1 
ATOM   3492 C CZ2   . TRP A 1 497 ? 34.124 36.203  26.979  1.00 38.23  ? 476  TRP A CZ2   1 
ATOM   3493 C CZ3   . TRP A 1 497 ? 32.760 37.442  25.410  1.00 34.78  ? 476  TRP A CZ3   1 
ATOM   3494 C CH2   . TRP A 1 497 ? 34.004 37.097  25.942  1.00 35.73  ? 476  TRP A CH2   1 
ATOM   3495 N N     . LEU A 1 498 ? 27.081 33.625  24.887  1.00 21.09  ? 477  LEU A N     1 
ATOM   3496 C CA    . LEU A 1 498 ? 25.709 33.291  24.495  1.00 22.66  ? 477  LEU A CA    1 
ATOM   3497 C C     . LEU A 1 498 ? 24.720 34.427  24.763  1.00 23.20  ? 477  LEU A C     1 
ATOM   3498 O O     . LEU A 1 498 ? 23.508 34.217  24.754  1.00 21.05  ? 477  LEU A O     1 
ATOM   3499 C CB    . LEU A 1 498 ? 25.252 31.997  25.167  1.00 22.41  ? 477  LEU A CB    1 
ATOM   3500 C CG    . LEU A 1 498 ? 26.053 30.745  24.791  1.00 23.98  ? 477  LEU A CG    1 
ATOM   3501 C CD1   . LEU A 1 498 ? 25.500 29.492  25.448  1.00 23.83  ? 477  LEU A CD1   1 
ATOM   3502 C CD2   . LEU A 1 498 ? 26.153 30.544  23.280  1.00 24.19  ? 477  LEU A CD2   1 
ATOM   3503 N N     . ARG A 1 499 ? 25.239 35.644  24.967  1.00 20.89  ? 478  ARG A N     1 
ATOM   3504 C CA    . ARG A 1 499 ? 24.421 36.825  25.157  1.00 20.33  ? 478  ARG A CA    1 
ATOM   3505 C C     . ARG A 1 499 ? 24.068 37.413  23.800  1.00 20.12  ? 478  ARG A C     1 
ATOM   3506 O O     . ARG A 1 499 ? 24.944 37.611  22.953  1.00 21.77  ? 478  ARG A O     1 
ATOM   3507 C CB    . ARG A 1 499 ? 25.170 37.893  25.966  1.00 23.33  ? 478  ARG A CB    1 
ATOM   3508 C CG    . ARG A 1 499 ? 25.526 37.379  27.350  1.00 23.08  ? 478  ARG A CG    1 
ATOM   3509 C CD    . ARG A 1 499 ? 26.314 38.388  28.204  1.00 27.94  ? 478  ARG A CD    1 
ATOM   3510 N NE    . ARG A 1 499 ? 27.579 38.695  27.524  1.00 30.48  ? 478  ARG A NE    1 
ATOM   3511 C CZ    . ARG A 1 499 ? 28.588 39.398  28.029  1.00 39.11  ? 478  ARG A CZ    1 
ATOM   3512 N NH1   . ARG A 1 499 ? 28.520 39.826  29.279  1.00 38.96  ? 478  ARG A NH1   1 
ATOM   3513 N NH2   . ARG A 1 499 ? 29.674 39.621  27.303  1.00 32.80  ? 478  ARG A NH2   1 
ATOM   3514 N N     . VAL A 1 500 ? 22.779 37.729  23.621  1.00 18.48  ? 479  VAL A N     1 
ATOM   3515 C CA    . VAL A 1 500 ? 22.315 38.359  22.403  1.00 18.61  ? 479  VAL A CA    1 
ATOM   3516 C C     . VAL A 1 500 ? 23.014 39.714  22.268  1.00 22.01  ? 479  VAL A C     1 
ATOM   3517 O O     . VAL A 1 500 ? 22.975 40.558  23.192  1.00 19.60  ? 479  VAL A O     1 
ATOM   3518 C CB    . VAL A 1 500 ? 20.779 38.465  22.406  1.00 18.50  ? 479  VAL A CB    1 
ATOM   3519 C CG1   . VAL A 1 500 ? 20.239 39.270  21.246  1.00 20.06  ? 479  VAL A CG1   1 
ATOM   3520 C CG2   . VAL A 1 500 ? 20.110 37.088  22.425  1.00 19.79  ? 479  VAL A CG2   1 
ATOM   3521 N N     . HIS A 1 501 ? 23.621 39.927  21.101  1.00 24.44  ? 480  HIS A N     1 
ATOM   3522 C CA    . HIS A 1 501 ? 24.329 41.173  20.835  1.00 24.66  ? 480  HIS A CA    1 
ATOM   3523 C C     . HIS A 1 501 ? 23.345 42.338  20.827  1.00 25.51  ? 480  HIS A C     1 
ATOM   3524 O O     . HIS A 1 501 ? 22.391 42.376  20.023  1.00 23.21  ? 480  HIS A O     1 
ATOM   3525 C CB    . HIS A 1 501 ? 25.073 41.122  19.502  1.00 23.61  ? 480  HIS A CB    1 
ATOM   3526 C CG    . HIS A 1 501 ? 26.292 40.250  19.450  1.00 24.47  ? 480  HIS A CG    1 
ATOM   3527 N ND1   . HIS A 1 501 ? 27.498 40.528  20.065  1.00 26.90  ? 480  HIS A ND1   1 
ATOM   3528 C CD2   . HIS A 1 501 ? 26.485 39.108  18.766  1.00 26.73  ? 480  HIS A CD2   1 
ATOM   3529 C CE1   . HIS A 1 501 ? 28.379 39.582  19.760  1.00 25.62  ? 480  HIS A CE1   1 
ATOM   3530 N NE2   . HIS A 1 501 ? 27.770 38.693  18.978  1.00 24.56  ? 480  HIS A NE2   1 
ATOM   3531 N N     . GLY A 1 502 ? 23.576 43.286  21.739  1.00 25.92  ? 481  GLY A N     1 
ATOM   3532 C CA    . GLY A 1 502 ? 22.830 44.548  21.718  1.00 28.30  ? 481  GLY A CA    1 
ATOM   3533 C C     . GLY A 1 502 ? 21.652 44.518  22.698  1.00 29.20  ? 481  GLY A C     1 
ATOM   3534 O O     . GLY A 1 502 ? 20.830 45.427  22.720  1.00 30.89  ? 481  GLY A O     1 
ATOM   3535 N N     . VAL A 1 503 ? 21.566 43.471  23.529  1.00 26.28  ? 482  VAL A N     1 
ATOM   3536 C CA    . VAL A 1 503 ? 20.519 43.381  24.538  1.00 27.54  ? 482  VAL A CA    1 
ATOM   3537 C C     . VAL A 1 503 ? 21.190 42.930  25.823  1.00 24.94  ? 482  VAL A C     1 
ATOM   3538 O O     . VAL A 1 503 ? 22.010 42.037  25.795  1.00 29.27  ? 482  VAL A O     1 
ATOM   3539 C CB    . VAL A 1 503 ? 19.394 42.394  24.166  1.00 26.98  ? 482  VAL A CB    1 
ATOM   3540 C CG1   . VAL A 1 503 ? 18.277 42.374  25.208  1.00 27.92  ? 482  VAL A CG1   1 
ATOM   3541 C CG2   . VAL A 1 503 ? 18.841 42.656  22.792  1.00 26.56  ? 482  VAL A CG2   1 
ATOM   3542 N N     . GLU A 1 504 ? 20.804 43.506  26.957  1.00 24.20  ? 483  GLU A N     1 
ATOM   3543 C CA    . GLU A 1 504 ? 21.274 42.998  28.233  1.00 25.25  ? 483  GLU A CA    1 
ATOM   3544 C C     . GLU A 1 504 ? 20.282 41.969  28.780  1.00 24.15  ? 483  GLU A C     1 
ATOM   3545 O O     . GLU A 1 504 ? 19.075 42.077  28.581  1.00 23.72  ? 483  GLU A O     1 
ATOM   3546 C CB    . GLU A 1 504 ? 21.404 44.170  29.212  1.00 28.12  ? 483  GLU A CB    1 
ATOM   3547 C CG    . GLU A 1 504 ? 22.246 45.337  28.674  1.00 34.90  ? 483  GLU A CG    1 
ATOM   3548 C CD    . GLU A 1 504 ? 23.737 45.107  28.705  1.00 45.55  ? 483  GLU A CD    1 
ATOM   3549 O OE1   . GLU A 1 504 ? 24.197 44.602  29.749  1.00 58.83  ? 483  GLU A OE1   1 
ATOM   3550 O OE2   . GLU A 1 504 ? 24.448 45.450  27.733  1.00 58.08  ? 483  GLU A OE2   1 
ATOM   3551 N N     . GLY A 1 505 ? 20.810 41.026  29.560  1.00 21.79  ? 484  GLY A N     1 
ATOM   3552 C CA    . GLY A 1 505 ? 19.991 40.108  30.327  1.00 24.41  ? 484  GLY A CA    1 
ATOM   3553 C C     . GLY A 1 505 ? 19.249 39.128  29.423  1.00 22.41  ? 484  GLY A C     1 
ATOM   3554 O O     . GLY A 1 505 ? 18.177 38.657  29.785  1.00 24.98  ? 484  GLY A O     1 
ATOM   3555 N N     . LEU A 1 506 ? 19.780 38.873  28.224  1.00 23.28  ? 485  LEU A N     1 
ATOM   3556 C CA    . LEU A 1 506 ? 19.130 37.933  27.313  1.00 20.09  ? 485  LEU A CA    1 
ATOM   3557 C C     . LEU A 1 506 ? 20.154 37.008  26.655  1.00 21.98  ? 485  LEU A C     1 
ATOM   3558 O O     . LEU A 1 506 ? 21.168 37.452  26.086  1.00 21.29  ? 485  LEU A O     1 
ATOM   3559 C CB    . LEU A 1 506 ? 18.327 38.691  26.283  1.00 19.85  ? 485  LEU A CB    1 
ATOM   3560 C CG    . LEU A 1 506 ? 17.631 37.824  25.222  1.00 21.76  ? 485  LEU A CG    1 
ATOM   3561 C CD1   . LEU A 1 506 ? 16.537 36.961  25.813  1.00 22.78  ? 485  LEU A CD1   1 
ATOM   3562 C CD2   . LEU A 1 506 ? 17.111 38.705  24.116  1.00 21.34  ? 485  LEU A CD2   1 
ATOM   3563 N N     . ARG A 1 507 ? 19.904 35.696  26.790  1.00 19.63  ? 486  ARG A N     1 
ATOM   3564 C CA    . ARG A 1 507 ? 20.783 34.701  26.202  1.00 21.05  ? 486  ARG A CA    1 
ATOM   3565 C C     . ARG A 1 507 ? 19.965 33.726  25.362  1.00 19.95  ? 486  ARG A C     1 
ATOM   3566 O O     . ARG A 1 507 ? 18.761 33.570  25.573  1.00 18.17  ? 486  ARG A O     1 
ATOM   3567 C CB    . ARG A 1 507 ? 21.593 33.898  27.222  1.00 22.35  ? 486  ARG A CB    1 
ATOM   3568 C CG    . ARG A 1 507 ? 22.360 34.810  28.174  1.00 26.14  ? 486  ARG A CG    1 
ATOM   3569 C CD    . ARG A 1 507 ? 23.575 34.184  28.795  1.00 27.67  ? 486  ARG A CD    1 
ATOM   3570 N NE    . ARG A 1 507 ? 24.051 35.029  29.900  1.00 26.49  ? 486  ARG A NE    1 
ATOM   3571 C CZ    . ARG A 1 507 ? 25.267 35.097  30.420  1.00 26.40  ? 486  ARG A CZ    1 
ATOM   3572 N NH1   . ARG A 1 507 ? 26.283 34.484  29.839  1.00 25.97  ? 486  ARG A NH1   1 
ATOM   3573 N NH2   . ARG A 1 507 ? 25.439 35.794  31.557  1.00 26.69  ? 486  ARG A NH2   1 
ATOM   3574 N N     . VAL A 1 508 ? 20.680 33.009  24.498  1.00 20.08  ? 487  VAL A N     1 
ATOM   3575 C CA    . VAL A 1 508 ? 20.129 31.865  23.775  1.00 19.24  ? 487  VAL A CA    1 
ATOM   3576 C C     . VAL A 1 508 ? 21.063 30.698  24.046  1.00 20.32  ? 487  VAL A C     1 
ATOM   3577 O O     . VAL A 1 508 ? 22.273 30.841  23.880  1.00 20.46  ? 487  VAL A O     1 
ATOM   3578 C CB    . VAL A 1 508 ? 19.990 32.107  22.254  1.00 18.36  ? 487  VAL A CB    1 
ATOM   3579 C CG1   . VAL A 1 508 ? 19.323 30.921  21.533  1.00 17.47  ? 487  VAL A CG1   1 
ATOM   3580 C CG2   . VAL A 1 508 ? 19.252 33.401  21.979  1.00 18.51  ? 487  VAL A CG2   1 
ATOM   3581 N N     . ALA A 1 509 ? 20.490 29.563  24.494  1.00 21.14  ? 488  ALA A N     1 
ATOM   3582 C CA    . ALA A 1 509 ? 21.247 28.344  24.754  1.00 22.12  ? 488  ALA A CA    1 
ATOM   3583 C C     . ALA A 1 509 ? 20.449 27.126  24.296  1.00 21.33  ? 488  ALA A C     1 
ATOM   3584 O O     . ALA A 1 509 ? 19.593 26.646  25.036  1.00 19.90  ? 488  ALA A O     1 
ATOM   3585 C CB    . ALA A 1 509 ? 21.549 28.229  26.228  1.00 23.14  ? 488  ALA A CB    1 
ATOM   3586 N N     . ASP A 1 510 ? 20.759 26.658  23.086  1.00 20.20  ? 489  ASP A N     1 
ATOM   3587 C CA    . ASP A 1 510 ? 20.143 25.502  22.469  1.00 20.47  ? 489  ASP A CA    1 
ATOM   3588 C C     . ASP A 1 510 ? 20.889 25.281  21.157  1.00 19.56  ? 489  ASP A C     1 
ATOM   3589 O O     . ASP A 1 510 ? 21.872 25.943  20.919  1.00 17.34  ? 489  ASP A O     1 
ATOM   3590 C CB    . ASP A 1 510 ? 18.653 25.737  22.286  1.00 20.63  ? 489  ASP A CB    1 
ATOM   3591 C CG    . ASP A 1 510 ? 18.292 26.984  21.494  1.00 20.22  ? 489  ASP A CG    1 
ATOM   3592 O OD1   . ASP A 1 510 ? 19.115 27.392  20.690  1.00 21.02  ? 489  ASP A OD1   1 
ATOM   3593 O OD2   . ASP A 1 510 ? 17.215 27.571  21.762  1.00 20.74  ? 489  ASP A OD2   1 
ATOM   3594 N N     . ALA A 1 511 ? 20.368 24.414  20.290  1.00 18.58  ? 490  ALA A N     1 
ATOM   3595 C CA    . ALA A 1 511 ? 21.042 24.087  19.047  1.00 18.40  ? 490  ALA A CA    1 
ATOM   3596 C C     . ALA A 1 511 ? 21.080 25.280  18.086  1.00 18.82  ? 490  ALA A C     1 
ATOM   3597 O O     . ALA A 1 511 ? 21.801 25.229  17.099  1.00 18.47  ? 490  ALA A O     1 
ATOM   3598 C CB    . ALA A 1 511 ? 20.360 22.916  18.410  1.00 18.62  ? 490  ALA A CB    1 
ATOM   3599 N N     . SER A 1 512 ? 20.312 26.349  18.340  1.00 17.89  ? 491  SER A N     1 
ATOM   3600 C CA    . SER A 1 512 ? 20.317 27.475  17.427  1.00 19.18  ? 491  SER A CA    1 
ATOM   3601 C C     . SER A 1 512 ? 21.674 28.175  17.356  1.00 18.44  ? 491  SER A C     1 
ATOM   3602 O O     . SER A 1 512 ? 21.942 28.851  16.365  1.00 18.73  ? 491  SER A O     1 
ATOM   3603 C CB    . SER A 1 512 ? 19.252 28.462  17.776  1.00 20.77  ? 491  SER A CB    1 
ATOM   3604 O OG    . SER A 1 512 ? 19.521 29.096  19.013  1.00 18.52  ? 491  SER A OG    1 
ATOM   3605 N N     . VAL A 1 513 ? 22.482 28.085  18.420  1.00 17.20  ? 492  VAL A N     1 
ATOM   3606 C CA    . VAL A 1 513 ? 23.694 28.896  18.526  1.00 18.23  ? 492  VAL A CA    1 
ATOM   3607 C C     . VAL A 1 513 ? 24.861 28.263  17.787  1.00 18.10  ? 492  VAL A C     1 
ATOM   3608 O O     . VAL A 1 513 ? 25.913 28.905  17.617  1.00 17.18  ? 492  VAL A O     1 
ATOM   3609 C CB    . VAL A 1 513 ? 24.142 29.210  19.963  1.00 17.51  ? 492  VAL A CB    1 
ATOM   3610 C CG1   . VAL A 1 513 ? 23.005 29.907  20.727  1.00 19.69  ? 492  VAL A CG1   1 
ATOM   3611 C CG2   . VAL A 1 513 ? 24.651 27.967  20.688  1.00 16.62  ? 492  VAL A CG2   1 
ATOM   3612 N N     . ILE A 1 514 ? 24.689 27.002  17.380  1.00 18.60  ? 493  ILE A N     1 
ATOM   3613 C CA    . ILE A 1 514 ? 25.762 26.229  16.757  1.00 19.42  ? 493  ILE A CA    1 
ATOM   3614 C C     . ILE A 1 514 ? 26.166 26.883  15.426  1.00 19.56  ? 493  ILE A C     1 
ATOM   3615 O O     . ILE A 1 514 ? 25.329 27.097  14.568  1.00 21.08  ? 493  ILE A O     1 
ATOM   3616 C CB    . ILE A 1 514 ? 25.296 24.775  16.554  1.00 18.64  ? 493  ILE A CB    1 
ATOM   3617 C CG1   . ILE A 1 514 ? 25.105 24.031  17.895  1.00 17.60  ? 493  ILE A CG1   1 
ATOM   3618 C CG2   . ILE A 1 514 ? 26.243 24.038  15.611  1.00 19.55  ? 493  ILE A CG2   1 
ATOM   3619 C CD1   . ILE A 1 514 ? 24.429 22.678  17.750  1.00 18.66  ? 493  ILE A CD1   1 
ATOM   3620 N N     . PRO A 1 515 ? 27.444 27.240  15.201  1.00 20.52  ? 494  PRO A N     1 
ATOM   3621 C CA    . PRO A 1 515 ? 27.843 27.858  13.934  1.00 22.41  ? 494  PRO A CA    1 
ATOM   3622 C C     . PRO A 1 515 ? 27.828 26.919  12.737  1.00 21.28  ? 494  PRO A C     1 
ATOM   3623 O O     . PRO A 1 515 ? 27.470 27.330  11.634  1.00 18.68  ? 494  PRO A O     1 
ATOM   3624 C CB    . PRO A 1 515 ? 29.266 28.427  14.185  1.00 23.24  ? 494  PRO A CB    1 
ATOM   3625 C CG    . PRO A 1 515 ? 29.503 28.269  15.650  1.00 24.43  ? 494  PRO A CG    1 
ATOM   3626 C CD    . PRO A 1 515 ? 28.533 27.211  16.192  1.00 22.35  ? 494  PRO A CD    1 
ATOM   3627 N N     . ARG A 1 516 ? 28.235 25.665  12.962  1.00 20.90  ? 495  ARG A N     1 
ATOM   3628 C CA    . ARG A 1 516 ? 28.373 24.701  11.883  1.00 23.40  ? 495  ARG A CA    1 
ATOM   3629 C C     . ARG A 1 516 ? 27.774 23.380  12.351  1.00 20.60  ? 495  ARG A C     1 
ATOM   3630 O O     . ARG A 1 516 ? 28.114 22.908  13.426  1.00 21.78  ? 495  ARG A O     1 
ATOM   3631 C CB    . ARG A 1 516 ? 29.836 24.533  11.447  1.00 24.36  ? 495  ARG A CB    1 
ATOM   3632 C CG    . ARG A 1 516 ? 30.067 23.632  10.247  1.00 24.00  ? 495  ARG A CG    1 
ATOM   3633 C CD    . ARG A 1 516 ? 29.781 24.368  8.968   1.00 26.23  ? 495  ARG A CD    1 
ATOM   3634 N NE    . ARG A 1 516 ? 30.123 23.492  7.854   1.00 23.40  ? 495  ARG A NE    1 
ATOM   3635 C CZ    . ARG A 1 516 ? 29.296 22.918  6.993   1.00 24.95  ? 495  ARG A CZ    1 
ATOM   3636 N NH1   . ARG A 1 516 ? 27.972 23.045  7.089   1.00 22.25  ? 495  ARG A NH1   1 
ATOM   3637 N NH2   . ARG A 1 516 ? 29.806 22.151  6.049   1.00 21.60  ? 495  ARG A NH2   1 
ATOM   3638 N N     . VAL A 1 517 ? 26.849 22.825  11.562  1.00 18.55  ? 496  VAL A N     1 
ATOM   3639 C CA    . VAL A 1 517 ? 26.264 21.533  11.888  1.00 18.94  ? 496  VAL A CA    1 
ATOM   3640 C C     . VAL A 1 517 ? 27.378 20.518  12.111  1.00 21.57  ? 496  VAL A C     1 
ATOM   3641 O O     . VAL A 1 517 ? 28.302 20.455  11.314  1.00 18.82  ? 496  VAL A O     1 
ATOM   3642 C CB    . VAL A 1 517 ? 25.291 21.073  10.797  1.00 19.54  ? 496  VAL A CB    1 
ATOM   3643 C CG1   . VAL A 1 517 ? 25.999 20.544  9.569   1.00 21.34  ? 496  VAL A CG1   1 
ATOM   3644 C CG2   . VAL A 1 517 ? 24.319 20.032  11.311  1.00 20.52  ? 496  VAL A CG2   1 
ATOM   3645 N N     . PRO A 1 518 ? 27.346 19.723  13.217  1.00 19.39  ? 497  PRO A N     1 
ATOM   3646 C CA    . PRO A 1 518 ? 28.395 18.741  13.473  1.00 20.62  ? 497  PRO A CA    1 
ATOM   3647 C C     . PRO A 1 518 ? 28.374 17.490  12.607  1.00 20.44  ? 497  PRO A C     1 
ATOM   3648 O O     . PRO A 1 518 ? 27.438 17.248  11.850  1.00 21.42  ? 497  PRO A O     1 
ATOM   3649 C CB    . PRO A 1 518 ? 28.163 18.344  14.924  1.00 18.13  ? 497  PRO A CB    1 
ATOM   3650 C CG    . PRO A 1 518 ? 26.670 18.551  15.126  1.00 18.26  ? 497  PRO A CG    1 
ATOM   3651 C CD    . PRO A 1 518 ? 26.339 19.769  14.289  1.00 18.09  ? 497  PRO A CD    1 
ATOM   3652 N N     . ARG A 1 519 ? 29.428 16.691  12.801  1.00 20.75  ? 498  ARG A N     1 
ATOM   3653 C CA    . ARG A 1 519 ? 29.516 15.331  12.286  1.00 21.96  ? 498  ARG A CA    1 
ATOM   3654 C C     . ARG A 1 519 ? 28.921 14.355  13.302  1.00 20.75  ? 498  ARG A C     1 
ATOM   3655 O O     . ARG A 1 519 ? 29.503 13.321  13.591  1.00 23.19  ? 498  ARG A O     1 
ATOM   3656 C CB    . ARG A 1 519 ? 30.978 14.994  11.972  1.00 21.35  ? 498  ARG A CB    1 
ATOM   3657 C CG    . ARG A 1 519 ? 31.572 15.890  10.906  1.00 21.00  ? 498  ARG A CG    1 
ATOM   3658 C CD    . ARG A 1 519 ? 33.070 15.611  10.779  1.00 22.77  ? 498  ARG A CD    1 
ATOM   3659 N NE    . ARG A 1 519 ? 33.616 16.395  9.679   1.00 22.88  ? 498  ARG A NE    1 
ATOM   3660 C CZ    . ARG A 1 519 ? 34.312 17.500  9.811   1.00 26.88  ? 498  ARG A CZ    1 
ATOM   3661 N NH1   . ARG A 1 519 ? 34.369 18.119  10.980  1.00 25.91  ? 498  ARG A NH1   1 
ATOM   3662 N NH2   . ARG A 1 519 ? 34.952 17.971  8.754   1.00 24.67  ? 498  ARG A NH2   1 
ATOM   3663 N N     . GLY A 1 520 ? 27.719 14.669  13.794  1.00 19.90  ? 499  GLY A N     1 
ATOM   3664 C CA    . GLY A 1 520 ? 27.033 13.817  14.752  1.00 20.89  ? 499  GLY A CA    1 
ATOM   3665 C C     . GLY A 1 520 ? 25.591 14.304  14.937  1.00 19.91  ? 499  GLY A C     1 
ATOM   3666 O O     . GLY A 1 520 ? 25.168 15.223  14.267  1.00 18.99  ? 499  GLY A O     1 
ATOM   3667 N N     . HIS A 1 521 ? 24.878 13.693  15.873  1.00 16.99  ? 500  HIS A N     1 
ATOM   3668 C CA    . HIS A 1 521 ? 23.455 13.896  16.068  1.00 18.29  ? 500  HIS A CA    1 
ATOM   3669 C C     . HIS A 1 521 ? 23.315 14.927  17.189  1.00 16.66  ? 500  HIS A C     1 
ATOM   3670 O O     . HIS A 1 521 ? 24.095 14.889  18.118  1.00 19.37  ? 500  HIS A O     1 
ATOM   3671 C CB    . HIS A 1 521 ? 22.822 12.546  16.399  1.00 16.77  ? 500  HIS A CB    1 
ATOM   3672 C CG    . HIS A 1 521 ? 22.937 11.563  15.300  1.00 18.92  ? 500  HIS A CG    1 
ATOM   3673 N ND1   . HIS A 1 521 ? 21.855 10.828  14.828  1.00 19.92  ? 500  HIS A ND1   1 
ATOM   3674 C CD2   . HIS A 1 521 ? 23.997 11.168  14.588  1.00 20.75  ? 500  HIS A CD2   1 
ATOM   3675 C CE1   . HIS A 1 521 ? 22.282 10.006  13.869  1.00 21.53  ? 500  HIS A CE1   1 
ATOM   3676 N NE2   . HIS A 1 521 ? 23.583 10.184  13.720  1.00 19.27  ? 500  HIS A NE2   1 
ATOM   3677 N N     . THR A 1 522 ? 22.407 15.892  17.043  1.00 16.32  ? 501  THR A N     1 
ATOM   3678 C CA    . THR A 1 522 ? 22.520 17.179  17.721  1.00 16.86  ? 501  THR A CA    1 
ATOM   3679 C C     . THR A 1 522 ? 21.941 17.212  19.141  1.00 16.40  ? 501  THR A C     1 
ATOM   3680 O O     . THR A 1 522 ? 22.085 18.225  19.815  1.00 16.27  ? 501  THR A O     1 
ATOM   3681 C CB    . THR A 1 522 ? 21.951 18.277  16.819  1.00 16.77  ? 501  THR A CB    1 
ATOM   3682 O OG1   . THR A 1 522 ? 20.678 17.909  16.280  1.00 16.16  ? 501  THR A OG1   1 
ATOM   3683 C CG2   . THR A 1 522 ? 22.918 18.576  15.692  1.00 16.65  ? 501  THR A CG2   1 
ATOM   3684 N N     . HIS A 1 523 ? 21.322 16.137  19.644  1.00 15.98  ? 502  HIS A N     1 
ATOM   3685 C CA    . HIS A 1 523 ? 20.891 16.140  21.045  1.00 17.09  ? 502  HIS A CA    1 
ATOM   3686 C C     . HIS A 1 523 ? 22.101 16.283  21.970  1.00 17.27  ? 502  HIS A C     1 
ATOM   3687 O O     . HIS A 1 523 ? 22.078 17.039  22.938  1.00 16.67  ? 502  HIS A O     1 
ATOM   3688 C CB    . HIS A 1 523 ? 20.123 14.859  21.406  1.00 17.56  ? 502  HIS A CB    1 
ATOM   3689 C CG    . HIS A 1 523 ? 19.753 14.754  22.840  1.00 16.31  ? 502  HIS A CG    1 
ATOM   3690 N ND1   . HIS A 1 523 ? 20.029 13.645  23.645  1.00 17.92  ? 502  HIS A ND1   1 
ATOM   3691 C CD2   . HIS A 1 523 ? 19.114 15.649  23.602  1.00 13.85  ? 502  HIS A CD2   1 
ATOM   3692 C CE1   . HIS A 1 523 ? 19.562 13.902  24.882  1.00 14.62  ? 502  HIS A CE1   1 
ATOM   3693 N NE2   . HIS A 1 523 ? 18.996 15.117  24.866  1.00 16.32  ? 502  HIS A NE2   1 
ATOM   3694 N N     . ALA A 1 524 ? 23.181 15.573  21.656  1.00 17.54  ? 503  ALA A N     1 
ATOM   3695 C CA    . ALA A 1 524 ? 24.401 15.704  22.432  1.00 18.03  ? 503  ALA A CA    1 
ATOM   3696 C C     . ALA A 1 524 ? 24.881 17.151  22.519  1.00 17.74  ? 503  ALA A C     1 
ATOM   3697 O O     . ALA A 1 524 ? 25.226 17.645  23.606  1.00 19.91  ? 503  ALA A O     1 
ATOM   3698 C CB    . ALA A 1 524 ? 25.458 14.787  21.876  1.00 21.42  ? 503  ALA A CB    1 
ATOM   3699 N N     . HIS A 1 525 ? 24.901 17.840  21.381  1.00 18.20  ? 504  HIS A N     1 
ATOM   3700 C CA    . HIS A 1 525 ? 25.364 19.222  21.319  1.00 18.01  ? 504  HIS A CA    1 
ATOM   3701 C C     . HIS A 1 525 ? 24.457 20.131  22.138  1.00 17.44  ? 504  HIS A C     1 
ATOM   3702 O O     . HIS A 1 525 ? 24.945 20.994  22.868  1.00 17.03  ? 504  HIS A O     1 
ATOM   3703 C CB    . HIS A 1 525 ? 25.505 19.690  19.871  1.00 18.53  ? 504  HIS A CB    1 
ATOM   3704 C CG    . HIS A 1 525 ? 26.368 18.778  19.113  1.00 19.28  ? 504  HIS A CG    1 
ATOM   3705 N ND1   . HIS A 1 525 ? 25.896 17.562  18.646  1.00 19.20  ? 504  HIS A ND1   1 
ATOM   3706 C CD2   . HIS A 1 525 ? 27.694 18.821  18.841  1.00 20.09  ? 504  HIS A CD2   1 
ATOM   3707 C CE1   . HIS A 1 525 ? 26.913 16.895  18.114  1.00 20.66  ? 504  HIS A CE1   1 
ATOM   3708 N NE2   . HIS A 1 525 ? 28.017 17.654  18.192  1.00 19.93  ? 504  HIS A NE2   1 
ATOM   3709 N N     . ALA A 1 526 ? 23.132 19.964  22.010  1.00 16.39  ? 505  ALA A N     1 
ATOM   3710 C CA    . ALA A 1 526 ? 22.214 20.800  22.763  1.00 16.91  ? 505  ALA A CA    1 
ATOM   3711 C C     . ALA A 1 526 ? 22.406 20.646  24.283  1.00 17.09  ? 505  ALA A C     1 
ATOM   3712 O O     . ALA A 1 526 ? 22.469 21.639  25.014  1.00 17.53  ? 505  ALA A O     1 
ATOM   3713 C CB    . ALA A 1 526 ? 20.774 20.548  22.329  1.00 18.12  ? 505  ALA A CB    1 
ATOM   3714 N N     . VAL A 1 527 ? 22.507 19.414  24.764  1.00 16.15  ? 506  VAL A N     1 
ATOM   3715 C CA    . VAL A 1 527 ? 22.766 19.158  26.179  1.00 17.07  ? 506  VAL A CA    1 
ATOM   3716 C C     . VAL A 1 527 ? 24.078 19.823  26.599  1.00 19.66  ? 506  VAL A C     1 
ATOM   3717 O O     . VAL A 1 527 ? 24.160 20.430  27.658  1.00 21.42  ? 506  VAL A O     1 
ATOM   3718 C CB    . VAL A 1 527 ? 22.853 17.648  26.414  1.00 18.56  ? 506  VAL A CB    1 
ATOM   3719 C CG1   . VAL A 1 527 ? 23.368 17.295  27.809  1.00 20.45  ? 506  VAL A CG1   1 
ATOM   3720 C CG2   . VAL A 1 527 ? 21.494 16.982  26.161  1.00 17.13  ? 506  VAL A CG2   1 
ATOM   3721 N N     . MET A 1 528 ? 25.108 19.646  25.782  1.00 18.17  ? 507  MET A N     1 
ATOM   3722 C CA    . MET A 1 528 ? 26.406 20.225  26.059  1.00 20.30  ? 507  MET A CA    1 
ATOM   3723 C C     . MET A 1 528 ? 26.284 21.750  26.174  1.00 19.99  ? 507  MET A C     1 
ATOM   3724 O O     . MET A 1 528 ? 26.842 22.325  27.108  1.00 18.85  ? 507  MET A O     1 
ATOM   3725 C CB    . MET A 1 528 ? 27.431 19.839  24.984  1.00 20.87  ? 507  MET A CB    1 
ATOM   3726 C CG    . MET A 1 528 ? 28.820 20.458  25.202  1.00 20.75  ? 507  MET A CG    1 
ATOM   3727 S SD    . MET A 1 528 ? 28.959 22.146  24.577  1.00 22.47  ? 507  MET A SD    1 
ATOM   3728 C CE    . MET A 1 528 ? 29.024 21.749  22.829  1.00 25.92  ? 507  MET A CE    1 
ATOM   3729 N N     . ILE A 1 529 ? 25.513 22.384  25.283  1.00 18.07  ? 508  ILE A N     1 
ATOM   3730 C CA    . ILE A 1 529 ? 25.341 23.828  25.309  1.00 18.83  ? 508  ILE A CA    1 
ATOM   3731 C C     . ILE A 1 529 ? 24.592 24.245  26.575  1.00 19.91  ? 508  ILE A C     1 
ATOM   3732 O O     . ILE A 1 529 ? 24.911 25.268  27.174  1.00 20.84  ? 508  ILE A O     1 
ATOM   3733 C CB    . ILE A 1 529 ? 24.658 24.303  24.018  1.00 19.93  ? 508  ILE A CB    1 
ATOM   3734 C CG1   . ILE A 1 529 ? 25.631 24.185  22.866  1.00 20.86  ? 508  ILE A CG1   1 
ATOM   3735 C CG2   . ILE A 1 529 ? 24.111 25.720  24.157  1.00 22.08  ? 508  ILE A CG2   1 
ATOM   3736 C CD1   . ILE A 1 529 ? 25.021 24.251  21.484  1.00 21.22  ? 508  ILE A CD1   1 
ATOM   3737 N N     . GLY A 1 530 ? 23.586 23.464  26.968  1.00 17.88  ? 509  GLY A N     1 
ATOM   3738 C CA    . GLY A 1 530 ? 22.895 23.698  28.213  1.00 20.03  ? 509  GLY A CA    1 
ATOM   3739 C C     . GLY A 1 530 ? 23.886 23.716  29.379  1.00 20.10  ? 509  GLY A C     1 
ATOM   3740 O O     . GLY A 1 530 ? 23.862 24.650  30.187  1.00 21.40  ? 509  GLY A O     1 
ATOM   3741 N N     . GLU A 1 531 ? 24.719 22.675  29.463  1.00 18.27  ? 510  GLU A N     1 
ATOM   3742 C CA    . GLU A 1 531 ? 25.704 22.582  30.547  1.00 21.71  ? 510  GLU A CA    1 
ATOM   3743 C C     . GLU A 1 531 ? 26.662 23.787  30.520  1.00 24.67  ? 510  GLU A C     1 
ATOM   3744 O O     . GLU A 1 531 ? 26.957 24.404  31.550  1.00 23.61  ? 510  GLU A O     1 
ATOM   3745 C CB    . GLU A 1 531 ? 26.571 21.337  30.402  1.00 20.81  ? 510  GLU A CB    1 
ATOM   3746 C CG    . GLU A 1 531 ? 25.891 20.021  30.767  1.00 22.00  ? 510  GLU A CG    1 
ATOM   3747 C CD    . GLU A 1 531 ? 25.602 19.781  32.241  1.00 23.68  ? 510  GLU A CD    1 
ATOM   3748 O OE1   . GLU A 1 531 ? 25.473 18.612  32.597  1.00 24.16  ? 510  GLU A OE1   1 
ATOM   3749 O OE2   . GLU A 1 531 ? 25.503 20.733  33.029  1.00 25.29  ? 510  GLU A OE2   1 
ATOM   3750 N N     . ARG A 1 532 ? 27.166 24.098  29.324  1.00 24.81  ? 511  ARG A N     1 
ATOM   3751 C CA    . ARG A 1 532 ? 28.124 25.180  29.123  1.00 26.89  ? 511  ARG A CA    1 
ATOM   3752 C C     . ARG A 1 532 ? 27.512 26.529  29.494  1.00 26.57  ? 511  ARG A C     1 
ATOM   3753 O O     . ARG A 1 532 ? 28.125 27.342  30.198  1.00 28.67  ? 511  ARG A O     1 
ATOM   3754 C CB    . ARG A 1 532 ? 28.509 25.086  27.649  1.00 32.61  ? 511  ARG A CB    1 
ATOM   3755 C CG    . ARG A 1 532 ? 29.589 26.075  27.266  1.00 42.87  ? 511  ARG A CG    1 
ATOM   3756 C CD    . ARG A 1 532 ? 30.868 25.389  27.476  1.00 40.37  ? 511  ARG A CD    1 
ATOM   3757 N NE    . ARG A 1 532 ? 31.866 26.383  27.066  1.00 50.64  ? 511  ARG A NE    1 
ATOM   3758 C CZ    . ARG A 1 532 ? 32.522 27.054  27.968  1.00 45.04  ? 511  ARG A CZ    1 
ATOM   3759 N NH1   . ARG A 1 532 ? 31.958 27.282  29.160  1.00 45.85  ? 511  ARG A NH1   1 
ATOM   3760 N NH2   . ARG A 1 532 ? 33.726 27.474  27.654  1.00 43.30  ? 511  ARG A NH2   1 
ATOM   3761 N N     . ALA A 1 533 ? 26.270 26.748  29.052  1.00 24.56  ? 512  ALA A N     1 
ATOM   3762 C CA    . ALA A 1 533 ? 25.544 27.956  29.362  1.00 24.18  ? 512  ALA A CA    1 
ATOM   3763 C C     . ALA A 1 533 ? 25.394 28.117  30.873  1.00 26.37  ? 512  ALA A C     1 
ATOM   3764 O O     . ALA A 1 533 ? 25.552 29.227  31.389  1.00 24.69  ? 512  ALA A O     1 
ATOM   3765 C CB    . ALA A 1 533 ? 24.204 27.967  28.665  1.00 25.24  ? 512  ALA A CB    1 
ATOM   3766 N N     . ALA A 1 534 ? 25.099 27.018  31.585  1.00 23.00  ? 513  ALA A N     1 
ATOM   3767 C CA    . ALA A 1 534 ? 24.861 27.135  33.018  1.00 25.62  ? 513  ALA A CA    1 
ATOM   3768 C C     . ALA A 1 534 ? 26.127 27.639  33.709  1.00 28.26  ? 513  ALA A C     1 
ATOM   3769 O O     . ALA A 1 534 ? 26.047 28.455  34.627  1.00 27.50  ? 513  ALA A O     1 
ATOM   3770 C CB    . ALA A 1 534 ? 24.431 25.832  33.592  1.00 26.51  ? 513  ALA A CB    1 
ATOM   3771 N N     . GLU A 1 535 ? 27.280 27.132  33.263  1.00 25.69  ? 514  GLU A N     1 
ATOM   3772 C CA    . GLU A 1 535 ? 28.563 27.516  33.831  1.00 31.10  ? 514  GLU A CA    1 
ATOM   3773 C C     . GLU A 1 535 ? 28.937 28.948  33.438  1.00 31.80  ? 514  GLU A C     1 
ATOM   3774 O O     . GLU A 1 535 ? 29.525 29.668  34.237  1.00 32.05  ? 514  GLU A O     1 
ATOM   3775 C CB    . GLU A 1 535 ? 29.609 26.493  33.395  1.00 33.95  ? 514  GLU A CB    1 
ATOM   3776 C CG    . GLU A 1 535 ? 30.706 26.287  34.428  1.00 44.73  ? 514  GLU A CG    1 
ATOM   3777 C CD    . GLU A 1 535 ? 31.783 27.325  34.324  1.00 52.01  ? 514  GLU A CD    1 
ATOM   3778 O OE1   . GLU A 1 535 ? 32.240 27.848  35.352  1.00 50.03  ? 514  GLU A OE1   1 
ATOM   3779 O OE2   . GLU A 1 535 ? 32.147 27.595  33.165  1.00 63.72  ? 514  GLU A OE2   1 
ATOM   3780 N N     . LEU A 1 536 ? 28.599 29.370  32.219  1.00 28.63  ? 515  LEU A N     1 
ATOM   3781 C CA    . LEU A 1 536 ? 28.841 30.745  31.810  1.00 30.31  ? 515  LEU A CA    1 
ATOM   3782 C C     . LEU A 1 536 ? 27.982 31.683  32.654  1.00 32.61  ? 515  LEU A C     1 
ATOM   3783 O O     . LEU A 1 536 ? 28.424 32.776  32.969  1.00 31.04  ? 515  LEU A O     1 
ATOM   3784 C CB    . LEU A 1 536 ? 28.603 31.021  30.326  1.00 27.93  ? 515  LEU A CB    1 
ATOM   3785 C CG    . LEU A 1 536 ? 29.535 30.278  29.368  1.00 32.49  ? 515  LEU A CG    1 
ATOM   3786 C CD1   . LEU A 1 536 ? 29.045 30.431  27.958  1.00 34.84  ? 515  LEU A CD1   1 
ATOM   3787 C CD2   . LEU A 1 536 ? 30.986 30.751  29.480  1.00 35.27  ? 515  LEU A CD2   1 
ATOM   3788 N N     . ILE A 1 537 ? 26.751 31.276  32.979  1.00 28.57  ? 516  ILE A N     1 
ATOM   3789 C CA    . ILE A 1 537 ? 25.823 32.148  33.669  1.00 30.89  ? 516  ILE A CA    1 
ATOM   3790 C C     . ILE A 1 537 ? 26.119 32.166  35.163  1.00 34.95  ? 516  ILE A C     1 
ATOM   3791 O O     . ILE A 1 537 ? 25.959 33.200  35.788  1.00 33.36  ? 516  ILE A O     1 
ATOM   3792 C CB    . ILE A 1 537 ? 24.369 31.725  33.417  1.00 30.52  ? 516  ILE A CB    1 
ATOM   3793 C CG1   . ILE A 1 537 ? 23.976 31.929  31.959  1.00 32.81  ? 516  ILE A CG1   1 
ATOM   3794 C CG2   . ILE A 1 537 ? 23.418 32.465  34.369  1.00 32.03  ? 516  ILE A CG2   1 
ATOM   3795 C CD1   . ILE A 1 537 ? 22.617 31.340  31.601  1.00 31.48  ? 516  ILE A CD1   1 
ATOM   3796 N N     . ARG A 1 538 ? 26.490 31.017  35.740  1.00 34.43  ? 517  ARG A N     1 
ATOM   3797 C CA    . ARG A 1 538 ? 26.773 30.950  37.165  1.00 40.36  ? 517  ARG A CA    1 
ATOM   3798 C C     . ARG A 1 538 ? 27.981 30.047  37.382  1.00 35.66  ? 517  ARG A C     1 
ATOM   3799 O O     . ARG A 1 538 ? 27.821 28.856  37.623  1.00 34.62  ? 517  ARG A O     1 
ATOM   3800 C CB    . ARG A 1 538 ? 25.503 30.484  37.885  1.00 45.77  ? 517  ARG A CB    1 
ATOM   3801 C CG    . ARG A 1 538 ? 25.411 30.915  39.341  1.00 60.58  ? 517  ARG A CG    1 
ATOM   3802 C CD    . ARG A 1 538 ? 25.890 29.887  40.363  1.00 64.74  ? 517  ARG A CD    1 
ATOM   3803 N NE    . ARG A 1 538 ? 25.256 28.568  40.236  1.00 77.64  ? 517  ARG A NE    1 
ATOM   3804 C CZ    . ARG A 1 538 ? 23.955 28.286  40.046  1.00 82.31  ? 517  ARG A CZ    1 
ATOM   3805 N NH1   . ARG A 1 538 ? 23.035 29.239  39.927  1.00 82.66  ? 517  ARG A NH1   1 
ATOM   3806 N NH2   . ARG A 1 538 ? 23.578 27.020  39.961  1.00 75.29  ? 517  ARG A NH2   1 
ATOM   3807 N N     . PRO A 1 539 ? 29.216 30.553  37.199  1.00 35.86  ? 518  PRO A N     1 
ATOM   3808 C CA    . PRO A 1 539 ? 30.414 29.725  37.345  1.00 43.90  ? 518  PRO A CA    1 
ATOM   3809 C C     . PRO A 1 539 ? 30.425 28.981  38.680  1.00 46.74  ? 518  PRO A C     1 
ATOM   3810 O O     . PRO A 1 539 ? 29.963 29.506  39.695  1.00 42.53  ? 518  PRO A O     1 
ATOM   3811 C CB    . PRO A 1 539 ? 31.610 30.696  37.216  1.00 43.38  ? 518  PRO A CB    1 
ATOM   3812 C CG    . PRO A 1 539 ? 31.028 31.974  36.654  1.00 41.98  ? 518  PRO A CG    1 
ATOM   3813 C CD    . PRO A 1 539 ? 29.520 31.932  36.804  1.00 38.78  ? 518  PRO A CD    1 
ATOM   3814 N N     . ALA A 1 540 ? 30.912 27.738  38.663  1.00 49.54  ? 519  ALA A N     1 
ATOM   3815 C CA    . ALA A 1 540 ? 30.973 26.924  39.873  1.00 58.83  ? 519  ALA A CA    1 
ATOM   3816 C C     . ALA A 1 540 ? 32.033 27.478  40.835  1.00 55.21  ? 519  ALA A C     1 
ATOM   3817 O O     . ALA A 1 540 ? 33.077 27.964  40.403  1.00 54.00  ? 519  ALA A O     1 
ATOM   3818 C CB    . ALA A 1 540 ? 31.248 25.472  39.501  1.00 56.86  ? 519  ALA A CB    1 
ATOM   3819 N N     . GLY A 1 541 ? 31.744 27.406  42.139  1.00 60.58  ? 520  GLY A N     1 
ATOM   3820 C CA    . GLY A 1 541 ? 32.711 27.718  43.181  1.00 65.96  ? 520  GLY A CA    1 
ATOM   3821 C C     . GLY A 1 541 ? 32.688 29.192  43.534  1.00 65.34  ? 520  GLY A C     1 
ATOM   3822 O O     . GLY A 1 541 ? 33.644 29.869  43.117  1.00 59.83  ? 520  GLY A O     1 
HETATM 3823 P PA    . FAD B 2 .   ? 14.328 21.064  21.675  1.00 16.79  ? 601  FAD A PA    1 
HETATM 3824 O O1A   . FAD B 2 .   ? 14.748 19.895  22.461  1.00 16.44  ? 601  FAD A O1A   1 
HETATM 3825 O O2A   . FAD B 2 .   ? 13.492 20.977  20.437  1.00 16.48  ? 601  FAD A O2A   1 
HETATM 3826 O O5B   . FAD B 2 .   ? 13.645 21.983  22.796  1.00 16.10  ? 601  FAD A O5B   1 
HETATM 3827 C C5B   . FAD B 2 .   ? 12.924 23.166  22.448  1.00 17.14  ? 601  FAD A C5B   1 
HETATM 3828 C C4B   . FAD B 2 .   ? 11.773 23.294  23.431  1.00 18.21  ? 601  FAD A C4B   1 
HETATM 3829 O O4B   . FAD B 2 .   ? 11.220 24.631  23.424  1.00 16.84  ? 601  FAD A O4B   1 
HETATM 3830 C C3B   . FAD B 2 .   ? 10.609 22.318  23.176  1.00 18.03  ? 601  FAD A C3B   1 
HETATM 3831 O O3B   . FAD B 2 .   ? 10.176 21.575  24.315  1.00 16.91  ? 601  FAD A O3B   1 
HETATM 3832 C C2B   . FAD B 2 .   ? 9.538  23.247  22.594  1.00 17.19  ? 601  FAD A C2B   1 
HETATM 3833 O O2B   . FAD B 2 .   ? 8.229  22.771  22.765  1.00 15.62  ? 601  FAD A O2B   1 
HETATM 3834 C C1B   . FAD B 2 .   ? 9.801  24.534  23.359  1.00 17.69  ? 601  FAD A C1B   1 
HETATM 3835 N N9A   . FAD B 2 .   ? 9.292  25.730  22.683  1.00 18.86  ? 601  FAD A N9A   1 
HETATM 3836 C C8A   . FAD B 2 .   ? 9.552  26.168  21.407  1.00 20.06  ? 601  FAD A C8A   1 
HETATM 3837 N N7A   . FAD B 2 .   ? 8.985  27.319  21.107  1.00 20.20  ? 601  FAD A N7A   1 
HETATM 3838 C C5A   . FAD B 2 .   ? 8.341  27.677  22.285  1.00 23.29  ? 601  FAD A C5A   1 
HETATM 3839 C C6A   . FAD B 2 .   ? 7.549  28.789  22.635  1.00 23.27  ? 601  FAD A C6A   1 
HETATM 3840 N N6A   . FAD B 2 .   ? 7.288  29.796  21.811  1.00 23.41  ? 601  FAD A N6A   1 
HETATM 3841 N N1A   . FAD B 2 .   ? 7.102  28.870  23.912  1.00 20.67  ? 601  FAD A N1A   1 
HETATM 3842 C C2A   . FAD B 2 .   ? 7.365  27.863  24.743  1.00 20.93  ? 601  FAD A C2A   1 
HETATM 3843 N N3A   . FAD B 2 .   ? 8.051  26.748  24.514  1.00 22.25  ? 601  FAD A N3A   1 
HETATM 3844 C C4A   . FAD B 2 .   ? 8.515  26.705  23.255  1.00 20.67  ? 601  FAD A C4A   1 
HETATM 3845 N N1    . FAD B 2 .   ? 19.330 14.011  17.924  1.00 17.69  ? 601  FAD A N1    1 
HETATM 3846 C C2    . FAD B 2 .   ? 20.169 13.035  18.373  1.00 18.38  ? 601  FAD A C2    1 
HETATM 3847 O O2    . FAD B 2 .   ? 21.256 13.288  18.911  1.00 20.58  ? 601  FAD A O2    1 
HETATM 3848 N N3    . FAD B 2 .   ? 19.743 11.717  18.274  1.00 18.97  ? 601  FAD A N3    1 
HETATM 3849 C C4    . FAD B 2 .   ? 18.596 11.257  17.611  1.00 17.27  ? 601  FAD A C4    1 
HETATM 3850 O O4    . FAD B 2 .   ? 18.280 10.085  17.665  1.00 16.43  ? 601  FAD A O4    1 
HETATM 3851 C C4X   . FAD B 2 .   ? 17.733 12.275  17.184  1.00 16.97  ? 601  FAD A C4X   1 
HETATM 3852 N N5    . FAD B 2 .   ? 16.595 11.929  16.618  1.00 18.96  ? 601  FAD A N5    1 
HETATM 3853 C C5X   . FAD B 2 .   ? 15.685 12.925  16.369  1.00 18.56  ? 601  FAD A C5X   1 
HETATM 3854 C C6    . FAD B 2 .   ? 14.388 12.582  15.929  1.00 19.10  ? 601  FAD A C6    1 
HETATM 3855 C C7    . FAD B 2 .   ? 13.396 13.537  15.818  1.00 20.94  ? 601  FAD A C7    1 
HETATM 3856 C C7M   . FAD B 2 .   ? 12.001 13.167  15.365  1.00 20.06  ? 601  FAD A C7M   1 
HETATM 3857 C C8    . FAD B 2 .   ? 13.698 14.878  16.133  1.00 18.99  ? 601  FAD A C8    1 
HETATM 3858 C C8M   . FAD B 2 .   ? 12.625 15.932  16.061  1.00 19.03  ? 601  FAD A C8M   1 
HETATM 3859 C C9    . FAD B 2 .   ? 14.998 15.233  16.436  1.00 16.59  ? 601  FAD A C9    1 
HETATM 3860 C C9A   . FAD B 2 .   ? 15.985 14.270  16.633  1.00 17.31  ? 601  FAD A C9A   1 
HETATM 3861 N N10   . FAD B 2 .   ? 17.280 14.603  17.024  1.00 17.91  ? 601  FAD A N10   1 
HETATM 3862 C C10   . FAD B 2 .   ? 18.168 13.637  17.397  1.00 17.61  ? 601  FAD A C10   1 
HETATM 3863 C "C1'" . FAD B 2 .   ? 17.664 16.019  17.234  1.00 17.62  ? 601  FAD A "C1'" 1 
HETATM 3864 C "C2'" . FAD B 2 .   ? 17.758 16.442  18.667  1.00 17.35  ? 601  FAD A "C2'" 1 
HETATM 3865 O "O2'" . FAD B 2 .   ? 16.764 15.754  19.432  1.00 15.48  ? 601  FAD A "O2'" 1 
HETATM 3866 C "C3'" . FAD B 2 .   ? 17.634 17.962  18.660  1.00 16.90  ? 601  FAD A "C3'" 1 
HETATM 3867 O "O3'" . FAD B 2 .   ? 18.581 18.585  17.793  1.00 14.60  ? 601  FAD A "O3'" 1 
HETATM 3868 C "C4'" . FAD B 2 .   ? 17.794 18.526  20.071  1.00 17.07  ? 601  FAD A "C4'" 1 
HETATM 3869 O "O4'" . FAD B 2 .   ? 16.881 17.879  20.961  1.00 16.04  ? 601  FAD A "O4'" 1 
HETATM 3870 C "C5'" . FAD B 2 .   ? 17.515 20.018  20.100  1.00 16.06  ? 601  FAD A "C5'" 1 
HETATM 3871 O "O5'" . FAD B 2 .   ? 17.658 20.522  21.447  1.00 17.17  ? 601  FAD A "O5'" 1 
HETATM 3872 P P     . FAD B 2 .   ? 17.164 21.975  21.756  1.00 17.94  ? 601  FAD A P     1 
HETATM 3873 O O1P   . FAD B 2 .   ? 17.804 22.941  20.823  1.00 16.08  ? 601  FAD A O1P   1 
HETATM 3874 O O2P   . FAD B 2 .   ? 17.239 22.211  23.221  1.00 17.64  ? 601  FAD A O2P   1 
HETATM 3875 O O3P   . FAD B 2 .   ? 15.594 22.023  21.330  1.00 16.16  ? 601  FAD A O3P   1 
HETATM 3876 C C1    . PGE C 3 .   ? 18.455 11.252  13.830  1.00 31.17  ? 602  PGE A C1    1 
HETATM 3877 O O1    . PGE C 3 .   ? 19.327 11.539  14.919  1.00 28.17  ? 602  PGE A O1    1 
HETATM 3878 C C2    . PGE C 3 .   ? 18.351 9.790   13.565  1.00 37.30  ? 602  PGE A C2    1 
HETATM 3879 O O2    . PGE C 3 .   ? 17.545 9.521   12.419  1.00 47.98  ? 602  PGE A O2    1 
HETATM 3880 C C3    . PGE C 3 .   ? 17.605 8.155   11.989  1.00 52.63  ? 602  PGE A C3    1 
HETATM 3881 C C4    . PGE C 3 .   ? 16.530 7.841   10.954  1.00 55.81  ? 602  PGE A C4    1 
HETATM 3882 O O4    . PGE C 3 .   ? 13.212 5.453   12.175  1.00 50.95  ? 602  PGE A O4    1 
HETATM 3883 C C6    . PGE C 3 .   ? 14.332 5.197   11.346  1.00 58.14  ? 602  PGE A C6    1 
HETATM 3884 C C5    . PGE C 3 .   ? 15.567 5.855   11.887  1.00 57.32  ? 602  PGE A C5    1 
HETATM 3885 O O3    . PGE C 3 .   ? 16.336 6.432   10.830  1.00 63.11  ? 602  PGE A O3    1 
HETATM 3886 C C1    . GOL D 4 .   ? 28.636 4.349   37.024  1.00 40.03  ? 603  GOL A C1    1 
HETATM 3887 O O1    . GOL D 4 .   ? 28.274 4.305   38.408  1.00 32.89  ? 603  GOL A O1    1 
HETATM 3888 C C2    . GOL D 4 .   ? 28.505 2.996   36.394  1.00 38.05  ? 603  GOL A C2    1 
HETATM 3889 O O2    . GOL D 4 .   ? 28.039 3.016   35.045  1.00 48.53  ? 603  GOL A O2    1 
HETATM 3890 C C3    . GOL D 4 .   ? 29.806 2.242   36.453  1.00 43.50  ? 603  GOL A C3    1 
HETATM 3891 O O3    . GOL D 4 .   ? 29.691 1.241   37.443  1.00 47.02  ? 603  GOL A O3    1 
HETATM 3892 C C1    . GOL E 4 .   ? 20.015 39.814  6.676   1.00 45.91  ? 604  GOL A C1    1 
HETATM 3893 O O1    . GOL E 4 .   ? 20.422 38.785  5.780   1.00 46.65  ? 604  GOL A O1    1 
HETATM 3894 C C2    . GOL E 4 .   ? 20.517 41.184  6.261   1.00 39.84  ? 604  GOL A C2    1 
HETATM 3895 O O2    . GOL E 4 .   ? 21.912 41.304  6.553   1.00 35.21  ? 604  GOL A O2    1 
HETATM 3896 C C3    . GOL E 4 .   ? 20.192 41.545  4.817   1.00 41.33  ? 604  GOL A C3    1 
HETATM 3897 O O3    . GOL E 4 .   ? 20.954 40.831  3.838   1.00 35.52  ? 604  GOL A O3    1 
HETATM 3898 C C1    . GOL F 4 .   ? 1.825  8.831   12.704  1.00 53.10  ? 605  GOL A C1    1 
HETATM 3899 O O1    . GOL F 4 .   ? 2.427  9.223   13.940  1.00 41.09  ? 605  GOL A O1    1 
HETATM 3900 C C2    . GOL F 4 .   ? 1.033  7.561   12.885  1.00 51.38  ? 605  GOL A C2    1 
HETATM 3901 O O2    . GOL F 4 .   ? 0.449  7.120   11.662  1.00 60.09  ? 605  GOL A O2    1 
HETATM 3902 C C3    . GOL F 4 .   ? 1.886  6.453   13.445  1.00 52.92  ? 605  GOL A C3    1 
HETATM 3903 O O3    . GOL F 4 .   ? 1.519  6.183   14.791  1.00 51.01  ? 605  GOL A O3    1 
HETATM 3904 C C1    . GOL G 4 .   ? 13.797 48.280  33.756  1.00 45.53  ? 606  GOL A C1    1 
HETATM 3905 O O1    . GOL G 4 .   ? 12.501 48.833  33.574  1.00 48.90  ? 606  GOL A O1    1 
HETATM 3906 C C2    . GOL G 4 .   ? 14.731 48.712  32.643  1.00 50.92  ? 606  GOL A C2    1 
HETATM 3907 O O2    . GOL G 4 .   ? 15.191 50.048  32.874  1.00 46.88  ? 606  GOL A O2    1 
HETATM 3908 C C3    . GOL G 4 .   ? 15.896 47.757  32.471  1.00 50.66  ? 606  GOL A C3    1 
HETATM 3909 O O3    . GOL G 4 .   ? 16.909 48.273  31.609  1.00 48.87  ? 606  GOL A O3    1 
HETATM 3910 C C1    . GOL H 4 .   ? 0.474  17.924  26.176  1.00 32.63  ? 607  GOL A C1    1 
HETATM 3911 O O1    . GOL H 4 .   ? 0.748  16.899  27.120  1.00 47.14  ? 607  GOL A O1    1 
HETATM 3912 C C2    . GOL H 4 .   ? 1.309  17.726  24.931  1.00 41.73  ? 607  GOL A C2    1 
HETATM 3913 O O2    . GOL H 4 .   ? 2.702  17.504  25.196  1.00 32.62  ? 607  GOL A O2    1 
HETATM 3914 C C3    . GOL H 4 .   ? 0.745  16.588  24.127  1.00 43.38  ? 607  GOL A C3    1 
HETATM 3915 O O3    . GOL H 4 .   ? -0.661 16.495  24.310  1.00 41.93  ? 607  GOL A O3    1 
HETATM 3916 C C1    . GOL I 4 .   ? -3.287 -2.573  21.578  1.00 39.01  ? 608  GOL A C1    1 
HETATM 3917 O O1    . GOL I 4 .   ? -3.140 -3.026  20.231  1.00 44.19  ? 608  GOL A O1    1 
HETATM 3918 C C2    . GOL I 4 .   ? -2.197 -1.600  21.935  1.00 37.63  ? 608  GOL A C2    1 
HETATM 3919 O O2    . GOL I 4 .   ? -2.429 -1.127  23.262  1.00 28.08  ? 608  GOL A O2    1 
HETATM 3920 C C3    . GOL I 4 .   ? -0.822 -2.237  21.769  1.00 37.66  ? 608  GOL A C3    1 
HETATM 3921 O O3    . GOL I 4 .   ? 0.254  -1.408  22.219  1.00 24.06  ? 608  GOL A O3    1 
HETATM 3922 O O     . HOH J 5 .   ? 3.517  39.939  17.079  1.00 40.78  ? 701  HOH A O     1 
HETATM 3923 O O     . HOH J 5 .   ? 32.155 -8.668  1.623   1.00 33.67  ? 702  HOH A O     1 
HETATM 3924 O O     . HOH J 5 .   ? 29.798 21.744  14.693  1.00 26.43  ? 703  HOH A O     1 
HETATM 3925 O O     . HOH J 5 .   ? 24.525 43.961  8.554   1.00 73.47  ? 704  HOH A O     1 
HETATM 3926 O O     . HOH J 5 .   ? 6.360  -8.939  14.512  1.00 41.96  ? 705  HOH A O     1 
HETATM 3927 O O     . HOH J 5 .   ? 31.508 16.464  19.873  1.00 26.18  ? 706  HOH A O     1 
HETATM 3928 O O     . HOH J 5 .   ? 12.171 8.684   -6.778  1.00 44.36  ? 707  HOH A O     1 
HETATM 3929 O O     . HOH J 5 .   ? 14.143 48.990  9.727   1.00 36.82  ? 708  HOH A O     1 
HETATM 3930 O O     . HOH J 5 .   ? 32.983 35.910  15.033  1.00 27.06  ? 709  HOH A O     1 
HETATM 3931 O O     . HOH J 5 .   ? 5.553  27.395  8.160   1.00 32.57  ? 710  HOH A O     1 
HETATM 3932 O O     . HOH J 5 .   ? 1.283  20.335  22.217  1.00 29.08  ? 711  HOH A O     1 
HETATM 3933 O O     . HOH J 5 .   ? 17.883 -9.431  24.444  1.00 33.02  ? 712  HOH A O     1 
HETATM 3934 O O     . HOH J 5 .   ? -1.389 9.651   26.134  1.00 19.24  ? 713  HOH A O     1 
HETATM 3935 O O     . HOH J 5 .   ? 3.692  -3.547  15.488  1.00 27.91  ? 714  HOH A O     1 
HETATM 3936 O O     . HOH J 5 .   ? 33.497 16.067  32.668  1.00 36.32  ? 715  HOH A O     1 
HETATM 3937 O O     . HOH J 5 .   ? 33.200 29.699  11.933  1.00 34.97  ? 716  HOH A O     1 
HETATM 3938 O O     . HOH J 5 .   ? 0.609  38.142  22.827  1.00 38.82  ? 717  HOH A O     1 
HETATM 3939 O O     . HOH J 5 .   ? 10.954 12.395  28.459  1.00 20.43  ? 718  HOH A O     1 
HETATM 3940 O O     . HOH J 5 .   ? 9.574  27.776  -1.767  1.00 38.96  ? 719  HOH A O     1 
HETATM 3941 O O     . HOH J 5 .   ? 36.233 23.753  29.789  1.00 32.79  ? 720  HOH A O     1 
HETATM 3942 O O     . HOH J 5 .   ? 14.051 18.128  43.598  1.00 42.30  ? 721  HOH A O     1 
HETATM 3943 O O     . HOH J 5 .   ? 35.382 20.950  11.250  1.00 27.03  ? 722  HOH A O     1 
HETATM 3944 O O     . HOH J 5 .   ? 14.516 11.087  36.899  1.00 27.66  ? 723  HOH A O     1 
HETATM 3945 O O     . HOH J 5 .   ? 30.964 5.820   -3.296  1.00 25.12  ? 724  HOH A O     1 
HETATM 3946 O O     . HOH J 5 .   ? 22.960 36.230  35.597  1.00 34.54  ? 725  HOH A O     1 
HETATM 3947 O O     . HOH J 5 .   ? 15.521 35.397  9.219   1.00 25.84  ? 726  HOH A O     1 
HETATM 3948 O O     . HOH J 5 .   ? 23.171 -8.002  15.862  1.00 23.51  ? 727  HOH A O     1 
HETATM 3949 O O     . HOH J 5 .   ? 11.427 -0.283  -6.333  1.00 30.60  ? 728  HOH A O     1 
HETATM 3950 O O     . HOH J 5 .   ? 34.980 13.455  0.714   1.00 30.18  ? 729  HOH A O     1 
HETATM 3951 O O     . HOH J 5 .   ? 24.218 9.227   36.702  1.00 35.73  ? 730  HOH A O     1 
HETATM 3952 O O     . HOH J 5 .   ? 36.676 1.850   2.501   1.00 44.08  ? 731  HOH A O     1 
HETATM 3953 O O     . HOH J 5 .   ? 32.886 21.480  10.327  1.00 30.81  ? 732  HOH A O     1 
HETATM 3954 O O     . HOH J 5 .   ? 23.971 12.580  11.637  1.00 32.34  ? 733  HOH A O     1 
HETATM 3955 O O     . HOH J 5 .   ? 15.656 23.313  25.151  1.00 16.29  ? 734  HOH A O     1 
HETATM 3956 O O     . HOH J 5 .   ? 26.248 22.310  38.587  1.00 40.55  ? 735  HOH A O     1 
HETATM 3957 O O     . HOH J 5 .   ? 29.917 -1.362  18.300  1.00 29.50  ? 736  HOH A O     1 
HETATM 3958 O O     . HOH J 5 .   ? 17.295 43.298  4.536   1.00 28.59  ? 737  HOH A O     1 
HETATM 3959 O O     . HOH J 5 .   ? 23.309 38.688  29.753  1.00 35.40  ? 738  HOH A O     1 
HETATM 3960 O O     . HOH J 5 .   ? 33.910 -8.031  8.284   1.00 35.46  ? 739  HOH A O     1 
HETATM 3961 O O     . HOH J 5 .   ? 30.676 17.651  17.317  1.00 23.41  ? 740  HOH A O     1 
HETATM 3962 O O     . HOH J 5 .   ? 21.156 3.761   -7.397  1.00 28.21  ? 741  HOH A O     1 
HETATM 3963 O O     . HOH J 5 .   ? 33.375 4.992   29.415  1.00 42.63  ? 742  HOH A O     1 
HETATM 3964 O O     . HOH J 5 .   ? 5.095  18.248  4.915   1.00 40.38  ? 743  HOH A O     1 
HETATM 3965 O O     . HOH J 5 .   ? 24.765 -12.556 3.320   1.00 28.68  ? 744  HOH A O     1 
HETATM 3966 O O     . HOH J 5 .   ? 23.455 39.636  13.364  1.00 20.81  ? 745  HOH A O     1 
HETATM 3967 O O     . HOH J 5 .   ? 25.412 12.982  37.403  1.00 37.33  ? 746  HOH A O     1 
HETATM 3968 O O     . HOH J 5 .   ? 7.678  26.708  6.432   1.00 19.74  ? 747  HOH A O     1 
HETATM 3969 O O     . HOH J 5 .   ? 20.591 19.930  39.188  1.00 28.53  ? 748  HOH A O     1 
HETATM 3970 O O     . HOH J 5 .   ? 39.454 26.981  15.243  1.00 36.33  ? 749  HOH A O     1 
HETATM 3971 O O     . HOH J 5 .   ? 17.992 -1.275  24.091  1.00 21.29  ? 750  HOH A O     1 
HETATM 3972 O O     . HOH J 5 .   ? 39.083 20.796  17.296  1.00 32.85  ? 751  HOH A O     1 
HETATM 3973 O O     . HOH J 5 .   ? 33.041 -3.885  -2.600  1.00 43.47  ? 752  HOH A O     1 
HETATM 3974 O O     . HOH J 5 .   ? 16.048 -5.128  17.672  1.00 20.92  ? 753  HOH A O     1 
HETATM 3975 O O     . HOH J 5 .   ? 12.733 13.172  7.064   1.00 20.10  ? 754  HOH A O     1 
HETATM 3976 O O     . HOH J 5 .   ? 29.163 11.517  -6.628  1.00 34.72  ? 755  HOH A O     1 
HETATM 3977 O O     . HOH J 5 .   ? 14.418 6.422   -0.293  1.00 25.45  ? 756  HOH A O     1 
HETATM 3978 O O     . HOH J 5 .   ? 18.512 -9.316  20.038  1.00 41.52  ? 757  HOH A O     1 
HETATM 3979 O O     . HOH J 5 .   ? 8.666  -0.194  13.167  1.00 41.74  ? 758  HOH A O     1 
HETATM 3980 O O     . HOH J 5 .   ? 0.890  31.356  26.553  1.00 27.55  ? 759  HOH A O     1 
HETATM 3981 O O     . HOH J 5 .   ? 9.031  11.291  17.165  1.00 23.42  ? 760  HOH A O     1 
HETATM 3982 O O     . HOH J 5 .   ? 11.950 10.527  35.196  1.00 25.04  ? 761  HOH A O     1 
HETATM 3983 O O     . HOH J 5 .   ? 35.186 -4.631  -0.465  1.00 50.35  ? 762  HOH A O     1 
HETATM 3984 O O     . HOH J 5 .   ? 12.091 42.435  34.982  1.00 35.89  ? 763  HOH A O     1 
HETATM 3985 O O     . HOH J 5 .   ? 1.392  43.934  12.715  1.00 40.55  ? 764  HOH A O     1 
HETATM 3986 O O     . HOH J 5 .   ? 36.227 32.704  23.284  1.00 39.92  ? 765  HOH A O     1 
HETATM 3987 O O     . HOH J 5 .   ? 9.798  42.906  22.349  1.00 25.19  ? 766  HOH A O     1 
HETATM 3988 O O     . HOH J 5 .   ? 26.887 22.890  33.749  1.00 25.52  ? 767  HOH A O     1 
HETATM 3989 O O     . HOH J 5 .   ? 24.286 34.088  11.150  1.00 20.80  ? 768  HOH A O     1 
HETATM 3990 O O     . HOH J 5 .   ? 14.175 22.295  18.223  1.00 16.16  ? 769  HOH A O     1 
HETATM 3991 O O     . HOH J 5 .   ? 28.380 18.314  31.897  1.00 22.79  ? 770  HOH A O     1 
HETATM 3992 O O     . HOH J 5 .   ? 18.669 0.839   -13.136 1.00 29.78  ? 771  HOH A O     1 
HETATM 3993 O O     . HOH J 5 .   ? 8.516  -3.614  33.317  1.00 46.54  ? 772  HOH A O     1 
HETATM 3994 O O     . HOH J 5 .   ? 3.816  -1.410  23.106  1.00 22.38  ? 773  HOH A O     1 
HETATM 3995 O O     . HOH J 5 .   ? 14.784 -7.036  16.156  1.00 18.80  ? 774  HOH A O     1 
HETATM 3996 O O     . HOH J 5 .   ? 1.096  -0.324  18.017  1.00 45.52  ? 775  HOH A O     1 
HETATM 3997 O O     . HOH J 5 .   ? 31.778 33.891  12.008  1.00 43.80  ? 776  HOH A O     1 
HETATM 3998 O O     . HOH J 5 .   ? 19.972 24.182  5.671   1.00 18.95  ? 777  HOH A O     1 
HETATM 3999 O O     . HOH J 5 .   ? 13.057 17.730  12.669  1.00 18.28  ? 778  HOH A O     1 
HETATM 4000 O O     . HOH J 5 .   ? 10.906 21.677  19.807  1.00 14.89  ? 779  HOH A O     1 
HETATM 4001 O O     . HOH J 5 .   ? 5.744  28.363  15.781  1.00 23.38  ? 780  HOH A O     1 
HETATM 4002 O O     . HOH J 5 .   ? 20.220 9.465   28.405  1.00 19.08  ? 781  HOH A O     1 
HETATM 4003 O O     . HOH J 5 .   ? 11.207 6.363   30.087  1.00 26.68  ? 782  HOH A O     1 
HETATM 4004 O O     . HOH J 5 .   ? 19.821 12.259  36.985  1.00 37.24  ? 783  HOH A O     1 
HETATM 4005 O O     . HOH J 5 .   ? 9.973  6.603   22.138  1.00 15.08  ? 784  HOH A O     1 
HETATM 4006 O O     . HOH J 5 .   ? 2.577  30.448  9.050   1.00 35.53  ? 785  HOH A O     1 
HETATM 4007 O O     . HOH J 5 .   ? 5.795  -11.111 17.794  1.00 25.49  ? 786  HOH A O     1 
HETATM 4008 O O     . HOH J 5 .   ? 28.560 0.504   -5.340  1.00 19.88  ? 787  HOH A O     1 
HETATM 4009 O O     . HOH J 5 .   ? 0.984  25.833  33.508  1.00 38.95  ? 788  HOH A O     1 
HETATM 4010 O O     . HOH J 5 .   ? 9.695  12.335  -4.237  1.00 43.10  ? 789  HOH A O     1 
HETATM 4011 O O     . HOH J 5 .   ? 22.433 -2.243  27.590  1.00 25.24  ? 790  HOH A O     1 
HETATM 4012 O O     . HOH J 5 .   ? 23.198 -7.473  -2.845  1.00 31.78  ? 791  HOH A O     1 
HETATM 4013 O O     . HOH J 5 .   ? 30.745 -5.063  -1.795  1.00 31.74  ? 792  HOH A O     1 
HETATM 4014 O O     . HOH J 5 .   ? 9.864  39.235  6.668   1.00 39.98  ? 793  HOH A O     1 
HETATM 4015 O O     . HOH J 5 .   ? 14.503 19.078  10.643  1.00 16.92  ? 794  HOH A O     1 
HETATM 4016 O O     . HOH J 5 .   ? 17.815 20.882  16.570  1.00 15.61  ? 795  HOH A O     1 
HETATM 4017 O O     . HOH J 5 .   ? 21.388 -9.712  -2.861  1.00 24.34  ? 796  HOH A O     1 
HETATM 4018 O O     . HOH J 5 .   ? 0.071  28.477  33.266  1.00 38.82  ? 797  HOH A O     1 
HETATM 4019 O O     . HOH J 5 .   ? 3.301  20.540  8.633   1.00 31.05  ? 798  HOH A O     1 
HETATM 4020 O O     . HOH J 5 .   ? 1.968  -7.288  28.696  1.00 47.61  ? 799  HOH A O     1 
HETATM 4021 O O     . HOH J 5 .   ? 23.708 12.590  19.848  1.00 14.57  ? 800  HOH A O     1 
HETATM 4022 O O     . HOH J 5 .   ? 9.459  22.410  40.098  1.00 39.20  ? 801  HOH A O     1 
HETATM 4023 O O     . HOH J 5 .   ? 5.927  -2.037  8.887   1.00 44.65  ? 802  HOH A O     1 
HETATM 4024 O O     . HOH J 5 .   ? 21.838 43.977  7.033   1.00 32.31  ? 803  HOH A O     1 
HETATM 4025 O O     . HOH J 5 .   ? 10.532 14.455  7.739   1.00 25.55  ? 804  HOH A O     1 
HETATM 4026 O O     . HOH J 5 .   ? 10.622 -11.124 5.567   1.00 41.36  ? 805  HOH A O     1 
HETATM 4027 O O     . HOH J 5 .   ? 22.384 39.684  27.118  1.00 29.25  ? 806  HOH A O     1 
HETATM 4028 O O     . HOH J 5 .   ? 16.940 22.858  18.238  1.00 16.45  ? 807  HOH A O     1 
HETATM 4029 O O     . HOH J 5 .   ? 11.283 9.596   28.913  1.00 22.16  ? 808  HOH A O     1 
HETATM 4030 O O     . HOH J 5 .   ? 35.296 7.989   30.437  1.00 46.31  ? 809  HOH A O     1 
HETATM 4031 O O     . HOH J 5 .   ? 7.078  -13.245 25.163  1.00 25.23  ? 810  HOH A O     1 
HETATM 4032 O O     . HOH J 5 .   ? 13.216 2.759   5.364   1.00 28.02  ? 811  HOH A O     1 
HETATM 4033 O O     . HOH J 5 .   ? 22.417 44.082  17.887  1.00 30.04  ? 812  HOH A O     1 
HETATM 4034 O O     . HOH J 5 .   ? 5.511  31.794  19.685  1.00 27.44  ? 813  HOH A O     1 
HETATM 4035 O O     . HOH J 5 .   ? 28.665 16.124  3.772   1.00 23.16  ? 814  HOH A O     1 
HETATM 4036 O O     . HOH J 5 .   ? 25.827 9.830   -9.672  1.00 38.53  ? 815  HOH A O     1 
HETATM 4037 O O     . HOH J 5 .   ? 18.367 49.119  19.097  1.00 48.43  ? 816  HOH A O     1 
HETATM 4038 O O     . HOH J 5 .   ? 17.528 -0.967  -9.966  1.00 21.59  ? 817  HOH A O     1 
HETATM 4039 O O     . HOH J 5 .   ? 36.952 13.285  17.504  1.00 36.45  ? 818  HOH A O     1 
HETATM 4040 O O     . HOH J 5 .   ? 12.792 24.696  17.893  1.00 16.17  ? 819  HOH A O     1 
HETATM 4041 O O     . HOH J 5 .   ? 17.630 -3.200  22.090  1.00 17.30  ? 820  HOH A O     1 
HETATM 4042 O O     . HOH J 5 .   ? 16.613 11.331  24.195  1.00 21.28  ? 821  HOH A O     1 
HETATM 4043 O O     . HOH J 5 .   ? 27.903 42.748  21.631  1.00 34.00  ? 822  HOH A O     1 
HETATM 4044 O O     . HOH J 5 .   ? 4.880  34.717  13.656  1.00 24.67  ? 823  HOH A O     1 
HETATM 4045 O O     . HOH J 5 .   ? -0.110 11.205  13.846  1.00 35.22  ? 824  HOH A O     1 
HETATM 4046 O O     . HOH J 5 .   ? 21.179 31.956  5.653   1.00 39.70  ? 825  HOH A O     1 
HETATM 4047 O O     . HOH J 5 .   ? 9.977  -6.401  23.056  1.00 20.43  ? 826  HOH A O     1 
HETATM 4048 O O     . HOH J 5 .   ? 20.079 0.486   -4.634  1.00 21.83  ? 827  HOH A O     1 
HETATM 4049 O O     . HOH J 5 .   ? 20.943 26.306  -0.499  1.00 39.48  ? 828  HOH A O     1 
HETATM 4050 O O     . HOH J 5 .   ? 34.853 28.234  9.690   1.00 45.46  ? 829  HOH A O     1 
HETATM 4051 O O     . HOH J 5 .   ? 18.218 11.914  26.360  1.00 17.34  ? 830  HOH A O     1 
HETATM 4052 O O     . HOH J 5 .   ? 15.006 8.943   1.664   1.00 25.07  ? 831  HOH A O     1 
HETATM 4053 O O     . HOH J 5 .   ? 22.301 32.772  12.875  1.00 17.71  ? 832  HOH A O     1 
HETATM 4054 O O     . HOH J 5 .   ? 13.601 0.234   -10.405 1.00 42.05  ? 833  HOH A O     1 
HETATM 4055 O O     . HOH J 5 .   ? 14.820 26.052  -1.117  1.00 26.10  ? 834  HOH A O     1 
HETATM 4056 O O     . HOH J 5 .   ? 4.472  6.793   30.373  1.00 35.57  ? 835  HOH A O     1 
HETATM 4057 O O     . HOH J 5 .   ? 19.565 -0.110  19.198  1.00 20.61  ? 836  HOH A O     1 
HETATM 4058 O O     . HOH J 5 .   ? -0.518 12.295  26.372  1.00 24.50  ? 837  HOH A O     1 
HETATM 4059 O O     . HOH J 5 .   ? 33.438 20.247  6.506   1.00 25.15  ? 838  HOH A O     1 
HETATM 4060 O O     . HOH J 5 .   ? 13.873 -6.248  12.157  1.00 16.42  ? 839  HOH A O     1 
HETATM 4061 O O     . HOH J 5 .   ? 12.181 31.629  5.261   1.00 24.25  ? 840  HOH A O     1 
HETATM 4062 O O     . HOH J 5 .   ? 12.740 4.921   17.591  1.00 22.78  ? 841  HOH A O     1 
HETATM 4063 O O     . HOH J 5 .   ? 0.621  18.243  31.071  1.00 28.49  ? 842  HOH A O     1 
HETATM 4064 O O     . HOH J 5 .   ? 19.101 11.020  21.592  1.00 20.23  ? 843  HOH A O     1 
HETATM 4065 O O     . HOH J 5 .   ? -1.467 32.479  29.193  1.00 31.56  ? 844  HOH A O     1 
HETATM 4066 O O     . HOH J 5 .   ? 9.072  26.164  18.174  1.00 18.36  ? 845  HOH A O     1 
HETATM 4067 O O     . HOH J 5 .   ? 8.465  44.817  18.550  1.00 36.67  ? 846  HOH A O     1 
HETATM 4068 O O     . HOH J 5 .   ? 23.362 -3.163  -3.536  1.00 20.12  ? 847  HOH A O     1 
HETATM 4069 O O     . HOH J 5 .   ? 28.947 18.988  -0.333  1.00 42.63  ? 848  HOH A O     1 
HETATM 4070 O O     . HOH J 5 .   ? 22.264 0.323   19.037  1.00 19.44  ? 849  HOH A O     1 
HETATM 4071 O O     . HOH J 5 .   ? 16.192 23.838  -2.136  1.00 24.87  ? 850  HOH A O     1 
HETATM 4072 O O     . HOH J 5 .   ? 9.230  44.736  24.412  1.00 31.34  ? 851  HOH A O     1 
HETATM 4073 O O     . HOH J 5 .   ? 28.939 1.863   20.521  1.00 38.92  ? 852  HOH A O     1 
HETATM 4074 O O     . HOH J 5 .   ? 19.837 -12.968 -1.549  1.00 33.08  ? 853  HOH A O     1 
HETATM 4075 O O     . HOH J 5 .   ? 26.459 0.521   -7.140  1.00 27.95  ? 854  HOH A O     1 
HETATM 4076 O O     . HOH J 5 .   ? 9.062  15.421  1.104   1.00 38.70  ? 855  HOH A O     1 
HETATM 4077 O O     . HOH J 5 .   ? 1.485  17.733  15.278  1.00 29.29  ? 856  HOH A O     1 
HETATM 4078 O O     . HOH J 5 .   ? 0.719  25.743  24.283  1.00 30.89  ? 857  HOH A O     1 
HETATM 4079 O O     . HOH J 5 .   ? 39.919 16.164  8.505   1.00 40.07  ? 858  HOH A O     1 
HETATM 4080 O O     . HOH J 5 .   ? 31.440 21.150  3.416   1.00 49.22  ? 859  HOH A O     1 
HETATM 4081 O O     . HOH J 5 .   ? 21.767 22.549  -6.852  1.00 39.67  ? 860  HOH A O     1 
HETATM 4082 O O     . HOH J 5 .   ? 20.506 -1.668  29.604  1.00 33.52  ? 861  HOH A O     1 
HETATM 4083 O O     . HOH J 5 .   ? 15.437 38.860  11.103  1.00 29.77  ? 862  HOH A O     1 
HETATM 4084 O O     . HOH J 5 .   ? 9.416  -3.296  -3.828  1.00 33.33  ? 863  HOH A O     1 
HETATM 4085 O O     . HOH J 5 .   ? 4.969  -4.179  27.526  1.00 27.58  ? 864  HOH A O     1 
HETATM 4086 O O     . HOH J 5 .   ? 28.278 22.988  -4.916  1.00 36.75  ? 865  HOH A O     1 
HETATM 4087 O O     . HOH J 5 .   ? 15.396 42.559  34.076  1.00 36.67  ? 866  HOH A O     1 
HETATM 4088 O O     . HOH J 5 .   ? 10.591 46.838  5.103   1.00 23.93  ? 867  HOH A O     1 
HETATM 4089 O O     . HOH J 5 .   ? 24.991 42.509  14.274  1.00 32.44  ? 868  HOH A O     1 
HETATM 4090 O O     . HOH J 5 .   ? 10.988 37.663  9.153   1.00 25.96  ? 869  HOH A O     1 
HETATM 4091 O O     . HOH J 5 .   ? 0.029  21.733  30.819  1.00 38.48  ? 870  HOH A O     1 
HETATM 4092 O O     . HOH J 5 .   ? 5.429  33.339  11.444  1.00 29.34  ? 871  HOH A O     1 
HETATM 4093 O O     . HOH J 5 .   ? 0.835  28.806  11.107  1.00 35.24  ? 872  HOH A O     1 
HETATM 4094 O O     . HOH J 5 .   ? 16.172 -10.256 11.772  1.00 28.89  ? 873  HOH A O     1 
HETATM 4095 O O     . HOH J 5 .   ? 1.468  40.363  10.442  1.00 31.81  ? 874  HOH A O     1 
HETATM 4096 O O     . HOH J 5 .   ? 19.419 44.760  6.056   1.00 36.49  ? 875  HOH A O     1 
HETATM 4097 O O     . HOH J 5 .   ? 21.670 20.123  1.319   1.00 21.27  ? 876  HOH A O     1 
HETATM 4098 O O     . HOH J 5 .   ? 31.304 21.412  12.728  1.00 38.03  ? 877  HOH A O     1 
HETATM 4099 O O     . HOH J 5 .   ? 15.207 44.733  14.124  1.00 26.49  ? 878  HOH A O     1 
HETATM 4100 O O     . HOH J 5 .   ? 34.661 16.184  6.496   1.00 28.57  ? 879  HOH A O     1 
HETATM 4101 O O     . HOH J 5 .   ? 28.847 15.492  35.748  1.00 39.41  ? 880  HOH A O     1 
HETATM 4102 O O     . HOH J 5 .   ? 7.834  8.646   -0.915  1.00 50.20  ? 881  HOH A O     1 
HETATM 4103 O O     . HOH J 5 .   ? 31.017 41.261  9.867   1.00 37.52  ? 882  HOH A O     1 
HETATM 4104 O O     . HOH J 5 .   ? 40.155 32.832  21.980  1.00 34.52  ? 883  HOH A O     1 
HETATM 4105 O O     . HOH J 5 .   ? 29.881 24.841  3.953   1.00 40.76  ? 884  HOH A O     1 
HETATM 4106 O O     . HOH J 5 .   ? 5.864  0.855   -0.923  1.00 35.06  ? 885  HOH A O     1 
HETATM 4107 O O     . HOH J 5 .   ? 30.616 11.850  33.352  1.00 23.31  ? 886  HOH A O     1 
HETATM 4108 O O     . HOH J 5 .   ? 23.137 27.703  0.070   1.00 45.48  ? 887  HOH A O     1 
HETATM 4109 O O     . HOH J 5 .   ? 3.346  28.342  16.789  1.00 30.17  ? 888  HOH A O     1 
HETATM 4110 O O     . HOH J 5 .   ? 25.955 24.495  -6.725  1.00 38.12  ? 889  HOH A O     1 
HETATM 4111 O O     . HOH J 5 .   ? 5.131  24.719  9.255   1.00 24.62  ? 890  HOH A O     1 
HETATM 4112 O O     . HOH J 5 .   ? 22.527 45.284  9.430   1.00 23.90  ? 891  HOH A O     1 
HETATM 4113 O O     . HOH J 5 .   ? 14.730 48.531  24.751  1.00 37.37  ? 892  HOH A O     1 
HETATM 4114 O O     . HOH J 5 .   ? 17.712 24.333  45.308  1.00 34.69  ? 893  HOH A O     1 
HETATM 4115 O O     . HOH J 5 .   ? 9.073  1.852   28.968  1.00 33.37  ? 894  HOH A O     1 
HETATM 4116 O O     . HOH J 5 .   ? 14.511 -15.299 9.219   1.00 38.55  ? 895  HOH A O     1 
HETATM 4117 O O     . HOH J 5 .   ? 33.468 10.354  33.497  1.00 38.75  ? 896  HOH A O     1 
HETATM 4118 O O     . HOH J 5 .   ? 19.835 0.181   25.987  1.00 23.16  ? 897  HOH A O     1 
HETATM 4119 O O     . HOH J 5 .   ? 23.581 41.651  30.249  1.00 42.48  ? 898  HOH A O     1 
HETATM 4120 O O     . HOH J 5 .   ? 9.128  14.986  4.563   1.00 28.95  ? 899  HOH A O     1 
HETATM 4121 O O     . HOH J 5 .   ? 19.625 48.297  16.943  1.00 28.70  ? 900  HOH A O     1 
HETATM 4122 O O     . HOH J 5 .   ? 20.538 0.601   31.399  1.00 31.48  ? 901  HOH A O     1 
HETATM 4123 O O     . HOH J 5 .   ? 7.180  15.337  35.342  1.00 35.31  ? 902  HOH A O     1 
HETATM 4124 O O     . HOH J 5 .   ? 10.343 4.781   16.203  1.00 23.15  ? 903  HOH A O     1 
HETATM 4125 O O     . HOH J 5 .   ? 33.378 14.960  19.944  1.00 39.09  ? 904  HOH A O     1 
HETATM 4126 O O     . HOH J 5 .   ? 33.666 2.396   -2.289  1.00 32.39  ? 905  HOH A O     1 
HETATM 4127 O O     . HOH J 5 .   ? 28.818 35.136  31.230  1.00 36.06  ? 906  HOH A O     1 
HETATM 4128 O O     . HOH J 5 .   ? 7.255  22.984  39.115  1.00 31.01  ? 907  HOH A O     1 
HETATM 4129 O O     . HOH J 5 .   ? 13.054 26.749  -2.807  1.00 27.06  ? 908  HOH A O     1 
HETATM 4130 O O     . HOH J 5 .   ? 5.839  18.103  -1.214  1.00 36.24  ? 909  HOH A O     1 
HETATM 4131 O O     . HOH J 5 .   ? 36.891 12.701  25.188  1.00 24.72  ? 910  HOH A O     1 
HETATM 4132 O O     . HOH J 5 .   ? 21.381 20.398  4.041   1.00 18.34  ? 911  HOH A O     1 
HETATM 4133 O O     . HOH J 5 .   ? 33.044 23.546  8.424   1.00 39.07  ? 912  HOH A O     1 
HETATM 4134 O O     . HOH J 5 .   ? 38.918 23.084  18.713  1.00 30.29  ? 913  HOH A O     1 
HETATM 4135 O O     . HOH J 5 .   ? 19.714 9.151   -16.858 1.00 49.99  ? 914  HOH A O     1 
HETATM 4136 O O     . HOH J 5 .   ? 24.659 1.522   -11.040 1.00 44.79  ? 915  HOH A O     1 
HETATM 4137 O O     . HOH J 5 .   ? 23.067 32.171  40.621  1.00 46.79  ? 916  HOH A O     1 
HETATM 4138 O O     . HOH J 5 .   ? -0.167 28.125  25.131  1.00 32.60  ? 917  HOH A O     1 
HETATM 4139 O O     . HOH J 5 .   ? 29.641 -2.198  25.484  1.00 33.45  ? 918  HOH A O     1 
HETATM 4140 O O     . HOH J 5 .   ? 19.416 4.228   -14.772 1.00 36.10  ? 919  HOH A O     1 
HETATM 4141 O O     . HOH J 5 .   ? 26.199 15.989  37.124  1.00 39.58  ? 920  HOH A O     1 
HETATM 4142 O O     . HOH J 5 .   ? 19.110 0.339   28.390  1.00 25.80  ? 921  HOH A O     1 
HETATM 4143 O O     . HOH J 5 .   ? 18.305 -2.452  19.643  1.00 20.56  ? 922  HOH A O     1 
HETATM 4144 O O     . HOH J 5 .   ? 38.007 2.093   9.366   1.00 32.52  ? 923  HOH A O     1 
HETATM 4145 O O     . HOH J 5 .   ? 21.785 7.625   -15.813 1.00 30.10  ? 924  HOH A O     1 
HETATM 4146 O O     . HOH J 5 .   ? 22.013 22.681  5.332   1.00 20.20  ? 925  HOH A O     1 
HETATM 4147 O O     . HOH J 5 .   ? 7.928  30.572  18.821  1.00 30.47  ? 926  HOH A O     1 
HETATM 4148 O O     . HOH J 5 .   ? 36.815 7.153   4.400   1.00 33.01  ? 927  HOH A O     1 
HETATM 4149 O O     . HOH J 5 .   ? 32.276 39.466  21.797  1.00 19.81  ? 928  HOH A O     1 
HETATM 4150 O O     . HOH J 5 .   ? 0.056  6.247   27.924  1.00 27.30  ? 929  HOH A O     1 
HETATM 4151 O O     . HOH J 5 .   ? 17.194 18.420  44.261  1.00 41.04  ? 930  HOH A O     1 
HETATM 4152 O O     . HOH J 5 .   ? 40.238 13.804  27.080  1.00 57.10  ? 931  HOH A O     1 
HETATM 4153 O O     . HOH J 5 .   ? 29.209 -17.373 -2.964  1.00 35.31  ? 932  HOH A O     1 
HETATM 4154 O O     . HOH J 5 .   ? 13.756 37.835  9.102   1.00 28.27  ? 933  HOH A O     1 
HETATM 4155 O O     . HOH J 5 .   ? 30.393 11.115  15.857  1.00 38.73  ? 934  HOH A O     1 
HETATM 4156 O O     . HOH J 5 .   ? 20.463 16.871  -10.519 1.00 46.90  ? 935  HOH A O     1 
HETATM 4157 O O     . HOH J 5 .   ? 27.640 34.165  8.640   1.00 42.31  ? 936  HOH A O     1 
HETATM 4158 O O     . HOH J 5 .   ? -1.585 14.281  21.724  1.00 23.75  ? 937  HOH A O     1 
HETATM 4159 O O     . HOH J 5 .   ? 25.515 -16.582 -4.678  1.00 26.45  ? 938  HOH A O     1 
HETATM 4160 O O     . HOH J 5 .   ? 9.588  3.034   31.347  1.00 36.65  ? 939  HOH A O     1 
HETATM 4161 O O     . HOH J 5 .   ? 5.628  44.528  17.204  1.00 37.06  ? 940  HOH A O     1 
HETATM 4162 O O     . HOH J 5 .   ? 13.513 12.495  39.553  1.00 40.05  ? 941  HOH A O     1 
HETATM 4163 O O     . HOH J 5 .   ? 2.400  24.217  34.998  1.00 37.30  ? 942  HOH A O     1 
HETATM 4164 O O     . HOH J 5 .   ? 15.860 9.113   -11.195 1.00 43.04  ? 943  HOH A O     1 
HETATM 4165 O O     . HOH J 5 .   ? -4.059 2.109   25.924  1.00 20.66  ? 944  HOH A O     1 
HETATM 4166 O O     . HOH J 5 .   ? 0.605  36.569  11.032  1.00 38.47  ? 945  HOH A O     1 
HETATM 4167 O O     . HOH J 5 .   ? 40.885 22.398  21.183  1.00 29.23  ? 946  HOH A O     1 
HETATM 4168 O O     . HOH J 5 .   ? 2.471  -12.527 19.678  1.00 23.42  ? 947  HOH A O     1 
HETATM 4169 O O     . HOH J 5 .   ? 36.433 -6.783  9.004   1.00 45.12  ? 948  HOH A O     1 
HETATM 4170 O O     . HOH J 5 .   ? 2.649  41.786  7.228   1.00 47.38  ? 949  HOH A O     1 
HETATM 4171 O O     . HOH J 5 .   ? 7.123  -0.162  8.050   1.00 46.27  ? 950  HOH A O     1 
HETATM 4172 O O     . HOH J 5 .   ? 30.112 17.481  1.782   1.00 36.00  ? 951  HOH A O     1 
HETATM 4173 O O     . HOH J 5 .   ? 30.158 31.154  11.617  1.00 41.31  ? 952  HOH A O     1 
HETATM 4174 O O     . HOH J 5 .   ? 31.078 3.043   -3.340  1.00 25.58  ? 953  HOH A O     1 
HETATM 4175 O O     . HOH J 5 .   ? 21.410 9.489   36.492  1.00 44.39  ? 954  HOH A O     1 
HETATM 4176 O O     . HOH J 5 .   ? 28.206 42.585  16.729  1.00 38.70  ? 955  HOH A O     1 
HETATM 4177 O O     . HOH J 5 .   ? 36.432 20.276  6.798   1.00 47.10  ? 956  HOH A O     1 
HETATM 4178 O O     . HOH J 5 .   ? 26.760 1.055   21.769  1.00 38.15  ? 957  HOH A O     1 
HETATM 4179 O O     . HOH J 5 .   ? 25.539 39.777  30.920  1.00 50.56  ? 958  HOH A O     1 
HETATM 4180 O O     . HOH J 5 .   ? 7.761  46.816  5.170   1.00 24.10  ? 959  HOH A O     1 
HETATM 4181 O O     . HOH J 5 .   ? 1.672  -10.055 15.307  1.00 43.88  ? 960  HOH A O     1 
HETATM 4182 O O     . HOH J 5 .   ? -2.755 33.752  31.809  1.00 39.50  ? 961  HOH A O     1 
HETATM 4183 O O     . HOH J 5 .   ? -2.167 13.410  24.368  1.00 25.21  ? 962  HOH A O     1 
HETATM 4184 O O     . HOH J 5 .   ? 35.912 34.070  29.685  1.00 51.76  ? 963  HOH A O     1 
HETATM 4185 O O     . HOH J 5 .   ? 30.285 20.442  17.242  1.00 28.66  ? 964  HOH A O     1 
HETATM 4186 O O     . HOH J 5 .   ? 3.200  24.461  10.722  1.00 41.36  ? 965  HOH A O     1 
HETATM 4187 O O     . HOH J 5 .   ? 17.708 25.617  -3.721  1.00 32.64  ? 966  HOH A O     1 
HETATM 4188 O O     . HOH J 5 .   ? 10.286 25.177  -5.456  1.00 32.90  ? 967  HOH A O     1 
HETATM 4189 O O     . HOH J 5 .   ? 30.868 27.997  10.456  1.00 29.66  ? 968  HOH A O     1 
HETATM 4190 O O     . HOH J 5 .   ? 6.949  10.817  33.265  1.00 41.28  ? 969  HOH A O     1 
HETATM 4191 O O     . HOH J 5 .   ? 29.227 8.844   -7.138  1.00 37.23  ? 970  HOH A O     1 
HETATM 4192 O O     . HOH J 5 .   ? 32.828 11.619  13.857  1.00 46.32  ? 971  HOH A O     1 
HETATM 4193 O O     . HOH J 5 .   ? 40.507 29.339  16.154  1.00 46.22  ? 972  HOH A O     1 
HETATM 4194 O O     . HOH J 5 .   ? 14.752 -10.309 21.480  1.00 39.84  ? 973  HOH A O     1 
HETATM 4195 O O     . HOH J 5 .   ? 10.473 23.725  17.891  1.00 16.21  ? 974  HOH A O     1 
HETATM 4196 O O     . HOH J 5 .   ? 30.741 1.949   -5.659  1.00 25.79  ? 975  HOH A O     1 
HETATM 4197 O O     . HOH J 5 .   ? 30.224 19.389  33.629  1.00 33.21  ? 976  HOH A O     1 
HETATM 4198 O O     . HOH J 5 .   ? 30.746 0.849   21.669  1.00 38.99  ? 977  HOH A O     1 
HETATM 4199 O O     . HOH J 5 .   ? 28.054 -14.655 5.871   1.00 50.24  ? 978  HOH A O     1 
HETATM 4200 O O     . HOH J 5 .   ? 8.696  11.712  -1.472  1.00 60.55  ? 979  HOH A O     1 
HETATM 4201 O O     . HOH J 5 .   ? 19.306 -2.089  -4.645  1.00 194.55 ? 980  HOH A O     1 
HETATM 4202 O O     . HOH J 5 .   ? 5.451  26.847  4.582   1.00 36.21  ? 981  HOH A O     1 
HETATM 4203 O O     . HOH J 5 .   ? 2.877  25.449  15.325  1.00 48.75  ? 982  HOH A O     1 
HETATM 4204 O O     . HOH J 5 .   ? 3.302  -12.236 17.084  1.00 41.88  ? 983  HOH A O     1 
HETATM 4205 O O     . HOH J 5 .   ? 37.884 12.936  27.870  1.00 43.01  ? 984  HOH A O     1 
HETATM 4206 O O     . HOH J 5 .   ? 5.669  -2.703  29.690  1.00 34.74  ? 985  HOH A O     1 
HETATM 4207 O O     . HOH J 5 .   ? -3.705 30.812  28.403  1.00 47.47  ? 986  HOH A O     1 
HETATM 4208 O O     . HOH J 5 .   ? 15.286 -12.022 13.508  1.00 35.33  ? 987  HOH A O     1 
HETATM 4209 O O     . HOH J 5 .   ? 9.573  52.994  7.706   1.00 35.45  ? 988  HOH A O     1 
HETATM 4210 O O     . HOH J 5 .   ? 26.283 23.963  36.492  1.00 47.48  ? 989  HOH A O     1 
HETATM 4211 O O     . HOH J 5 .   ? -1.068 30.352  25.033  1.00 42.51  ? 990  HOH A O     1 
HETATM 4212 O O     . HOH J 5 .   ? 3.204  28.499  7.486   1.00 42.80  ? 991  HOH A O     1 
HETATM 4213 O O     . HOH J 5 .   ? 24.915 34.106  8.559   1.00 35.57  ? 992  HOH A O     1 
HETATM 4214 O O     . HOH J 5 .   ? 24.808 46.904  14.299  1.00 41.18  ? 993  HOH A O     1 
HETATM 4215 O O     . HOH J 5 .   ? 30.925 6.712   -6.074  1.00 36.66  ? 994  HOH A O     1 
HETATM 4216 O O     . HOH J 5 .   ? 3.219  13.473  9.125   1.00 48.04  ? 995  HOH A O     1 
HETATM 4217 O O     . HOH J 5 .   ? -4.910 0.520   28.293  1.00 37.75  ? 996  HOH A O     1 
HETATM 4218 O O     . HOH J 5 .   ? 21.172 -1.597  -3.037  1.00 33.06  ? 997  HOH A O     1 
HETATM 4219 O O     . HOH J 5 .   ? 7.316  -3.220  -5.566  1.00 48.56  ? 998  HOH A O     1 
HETATM 4220 O O     . HOH J 5 .   ? 8.582  12.728  7.973   1.00 33.99  ? 999  HOH A O     1 
HETATM 4221 O O     . HOH J 5 .   ? 5.994  1.724   29.132  1.00 38.16  ? 1000 HOH A O     1 
HETATM 4222 O O     . HOH J 5 .   ? 40.322 25.007  17.731  1.00 37.29  ? 1001 HOH A O     1 
HETATM 4223 O O     . HOH J 5 .   ? 12.378 -10.785 17.777  1.00 36.37  ? 1002 HOH A O     1 
HETATM 4224 O O     . HOH J 5 .   ? 35.638 22.802  32.395  1.00 51.92  ? 1003 HOH A O     1 
HETATM 4225 O O     . HOH J 5 .   ? 15.145 -11.760 16.216  1.00 38.45  ? 1004 HOH A O     1 
# 
