data_9G8A
# 
_entry.id   9G8A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9G8A         pdb_00009g8a 10.2210/pdb9g8a/pdb 
WWPDB D_1292140534 ?            ?                   
# 
_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       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9G8A 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-23 
_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_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9G88 unspecified 
PDB . 9G89 unspecified 
# 
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 jacek.plewka@uj.edu.pl       Jacek     Plewka         ? 'principal investigator/group leader' 0000-0002-0307-0907 
3 lukas.schober@tugraz.at      Lucas     Schober        ? 'principal investigator/group leader' 0000-0001-6546-6555 
4 k.magiera@uj.edu.pl          Katarzyna Magiera-Mularz ? 'principal investigator/group leader' 0000-0002-4826-6380 
5 florian.rudroff@tuwien.ac.at Florian   Rudroff        ? 'principal investigator/group leader' 0000-0002-6680-8200 
6 margit.winkler@tugraz.at     Margit    Winkler        ? 'principal investigator/group leader' 0000-0002-0754-9704 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Plewka, J.'         1 0000-0002-0307-0907 
'Schorber, L.'       2 0000-0001-6546-6555 
'Magiera-Mularz, K.' 3 0000-0002-4826-6380 
'Rudroff, F.'        4 0000-0002-6680-8200 
'Winkler, M.'        5 0000-0002-0754-9704 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Jacs Au' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2691-3704 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'structure of carotenoid cleavage oxygenase from Moesziomyces aphidis in apo and product bound forms' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacsau.5c00456 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Schorber, L.'       1 ? 
primary 'Plewka, J.'         2 ? 
primary 'Magiera-Mularz, K.' 3 ? 
primary 'Rudroff, F.'        4 ? 
primary 'Winkler, M.'        5 ? 
# 
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 'Lignostilbene dioxygenase' 62905.562 2   ? ? ? 'Aromatic dioxygenase' 
2 non-polymer syn P-HYDROXYBENZALDEHYDE       122.121   2   ? ? ? ?                      
3 non-polymer syn 'FE (II) ION'               55.845    2   ? ? ? ?                      
4 water       nat water                       18.015    874 ? ? ? ?                      
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carotenoid cleavage oxygenase, Aromatic dioxygenase' 
# 
_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       
;MWSHPQFEKAPTATQEPVPVPVTSKAAPSHGYVHPTDILPSGWPTATDLSGGAQPRRFEGTIFDVMTRGTIPKELHGTFY
RIMPDYAQPPTYYKGGELNAPIDGDGTVAAFRFKDGKVDYRQRFVETDRFKVERRARKSMYGLYRNPYTHHPCVRQTVES
TANTNVVMHAGRFLAMKENGNAYEMDPHTLKTLGYNPFNLPSKTMTAHPKQCSVTGNLVGFGYEAKGLATKDVYYFEVDP
SGKVVRDLWLEAPWCAFIHDCALTPNYLVLMLWPFEANLERMKAGGHHWAYDYTKPITWITIPRGAKSKDEVKYWHWKNG
MPIHTASGFEDEQGRIIIDSSLVHGNAFPFFPPDSDEQKKKQEADGTPKAQFVRWTIDPRKDNNEQLPDPEVILDTPSEF
PQIDNRFMGVEYSSAFINVFVPDRSDGNKNVFQGLNGLAHYKRKEGTTEWYYAGDNCLIQEPVFSPRSKDAPEGDGFVLA
IVDRLDLNRSEVVVIDTRDFTKAVAAVQLPFAIRSGIHGQWIPGEVTPDFETKGLVDLPKEEHWAPLSQSPYDPDA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MWSHPQFEKAPTATQEPVPVPVTSKAAPSHGYVHPTDILPSGWPTATDLSGGAQPRRFEGTIFDVMTRGTIPKELHGTFY
RIMPDYAQPPTYYKGGELNAPIDGDGTVAAFRFKDGKVDYRQRFVETDRFKVERRARKSMYGLYRNPYTHHPCVRQTVES
TANTNVVMHAGRFLAMKENGNAYEMDPHTLKTLGYNPFNLPSKTMTAHPKQCSVTGNLVGFGYEAKGLATKDVYYFEVDP
SGKVVRDLWLEAPWCAFIHDCALTPNYLVLMLWPFEANLERMKAGGHHWAYDYTKPITWITIPRGAKSKDEVKYWHWKNG
MPIHTASGFEDEQGRIIIDSSLVHGNAFPFFPPDSDEQKKKQEADGTPKAQFVRWTIDPRKDNNEQLPDPEVILDTPSEF
PQIDNRFMGVEYSSAFINVFVPDRSDGNKNVFQGLNGLAHYKRKEGTTEWYYAGDNCLIQEPVFSPRSKDAPEGDGFVLA
IVDRLDLNRSEVVVIDTRDFTKAVAAVQLPFAIRSGIHGQWIPGEVTPDFETKGLVDLPKEEHWAPLSQSPYDPDA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 P-HYDROXYBENZALDEHYDE HBA 
3 'FE (II) ION'         FE2 
4 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   TRP n 
1 3   SER n 
1 4   HIS n 
1 5   PRO n 
1 6   GLN n 
1 7   PHE n 
1 8   GLU n 
1 9   LYS n 
1 10  ALA n 
1 11  PRO n 
1 12  THR n 
1 13  ALA n 
1 14  THR n 
1 15  GLN n 
1 16  GLU n 
1 17  PRO n 
1 18  VAL n 
1 19  PRO n 
1 20  VAL n 
1 21  PRO n 
1 22  VAL n 
1 23  THR n 
1 24  SER n 
1 25  LYS n 
1 26  ALA n 
1 27  ALA n 
1 28  PRO n 
1 29  SER n 
1 30  HIS n 
1 31  GLY n 
1 32  TYR n 
1 33  VAL n 
1 34  HIS n 
1 35  PRO n 
1 36  THR n 
1 37  ASP n 
1 38  ILE n 
1 39  LEU n 
1 40  PRO n 
1 41  SER n 
1 42  GLY n 
1 43  TRP n 
1 44  PRO n 
1 45  THR n 
1 46  ALA n 
1 47  THR n 
1 48  ASP n 
1 49  LEU n 
1 50  SER n 
1 51  GLY n 
1 52  GLY n 
1 53  ALA n 
1 54  GLN n 
1 55  PRO n 
1 56  ARG n 
1 57  ARG n 
1 58  PHE n 
1 59  GLU n 
1 60  GLY n 
1 61  THR n 
1 62  ILE n 
1 63  PHE n 
1 64  ASP n 
1 65  VAL n 
1 66  MET n 
1 67  THR n 
1 68  ARG n 
1 69  GLY n 
1 70  THR n 
1 71  ILE n 
1 72  PRO n 
1 73  LYS n 
1 74  GLU n 
1 75  LEU n 
1 76  HIS n 
1 77  GLY n 
1 78  THR n 
1 79  PHE n 
1 80  TYR n 
1 81  ARG n 
1 82  ILE n 
1 83  MET n 
1 84  PRO n 
1 85  ASP n 
1 86  TYR n 
1 87  ALA n 
1 88  GLN n 
1 89  PRO n 
1 90  PRO n 
1 91  THR n 
1 92  TYR n 
1 93  TYR n 
1 94  LYS n 
1 95  GLY n 
1 96  GLY n 
1 97  GLU n 
1 98  LEU n 
1 99  ASN n 
1 100 ALA n 
1 101 PRO n 
1 102 ILE n 
1 103 ASP n 
1 104 GLY n 
1 105 ASP n 
1 106 GLY n 
1 107 THR n 
1 108 VAL n 
1 109 ALA n 
1 110 ALA n 
1 111 PHE n 
1 112 ARG n 
1 113 PHE n 
1 114 LYS n 
1 115 ASP n 
1 116 GLY n 
1 117 LYS n 
1 118 VAL n 
1 119 ASP n 
1 120 TYR n 
1 121 ARG n 
1 122 GLN n 
1 123 ARG n 
1 124 PHE n 
1 125 VAL n 
1 126 GLU n 
1 127 THR n 
1 128 ASP n 
1 129 ARG n 
1 130 PHE n 
1 131 LYS n 
1 132 VAL n 
1 133 GLU n 
1 134 ARG n 
1 135 ARG n 
1 136 ALA n 
1 137 ARG n 
1 138 LYS n 
1 139 SER n 
1 140 MET n 
1 141 TYR n 
1 142 GLY n 
1 143 LEU n 
1 144 TYR n 
1 145 ARG n 
1 146 ASN n 
1 147 PRO n 
1 148 TYR n 
1 149 THR n 
1 150 HIS n 
1 151 HIS n 
1 152 PRO n 
1 153 CYS n 
1 154 VAL n 
1 155 ARG n 
1 156 GLN n 
1 157 THR n 
1 158 VAL n 
1 159 GLU n 
1 160 SER n 
1 161 THR n 
1 162 ALA n 
1 163 ASN n 
1 164 THR n 
1 165 ASN n 
1 166 VAL n 
1 167 VAL n 
1 168 MET n 
1 169 HIS n 
1 170 ALA n 
1 171 GLY n 
1 172 ARG n 
1 173 PHE n 
1 174 LEU n 
1 175 ALA n 
1 176 MET n 
1 177 LYS n 
1 178 GLU n 
1 179 ASN n 
1 180 GLY n 
1 181 ASN n 
1 182 ALA n 
1 183 TYR n 
1 184 GLU n 
1 185 MET n 
1 186 ASP n 
1 187 PRO n 
1 188 HIS n 
1 189 THR n 
1 190 LEU n 
1 191 LYS n 
1 192 THR n 
1 193 LEU n 
1 194 GLY n 
1 195 TYR n 
1 196 ASN n 
1 197 PRO n 
1 198 PHE n 
1 199 ASN n 
1 200 LEU n 
1 201 PRO n 
1 202 SER n 
1 203 LYS n 
1 204 THR n 
1 205 MET n 
1 206 THR n 
1 207 ALA n 
1 208 HIS n 
1 209 PRO n 
1 210 LYS n 
1 211 GLN n 
1 212 CYS n 
1 213 SER n 
1 214 VAL n 
1 215 THR n 
1 216 GLY n 
1 217 ASN n 
1 218 LEU n 
1 219 VAL n 
1 220 GLY n 
1 221 PHE n 
1 222 GLY n 
1 223 TYR n 
1 224 GLU n 
1 225 ALA n 
1 226 LYS n 
1 227 GLY n 
1 228 LEU n 
1 229 ALA n 
1 230 THR n 
1 231 LYS n 
1 232 ASP n 
1 233 VAL n 
1 234 TYR n 
1 235 TYR n 
1 236 PHE n 
1 237 GLU n 
1 238 VAL n 
1 239 ASP n 
1 240 PRO n 
1 241 SER n 
1 242 GLY n 
1 243 LYS n 
1 244 VAL n 
1 245 VAL n 
1 246 ARG n 
1 247 ASP n 
1 248 LEU n 
1 249 TRP n 
1 250 LEU n 
1 251 GLU n 
1 252 ALA n 
1 253 PRO n 
1 254 TRP n 
1 255 CYS n 
1 256 ALA n 
1 257 PHE n 
1 258 ILE n 
1 259 HIS n 
1 260 ASP n 
1 261 CYS n 
1 262 ALA n 
1 263 LEU n 
1 264 THR n 
1 265 PRO n 
1 266 ASN n 
1 267 TYR n 
1 268 LEU n 
1 269 VAL n 
1 270 LEU n 
1 271 MET n 
1 272 LEU n 
1 273 TRP n 
1 274 PRO n 
1 275 PHE n 
1 276 GLU n 
1 277 ALA n 
1 278 ASN n 
1 279 LEU n 
1 280 GLU n 
1 281 ARG n 
1 282 MET n 
1 283 LYS n 
1 284 ALA n 
1 285 GLY n 
1 286 GLY n 
1 287 HIS n 
1 288 HIS n 
1 289 TRP n 
1 290 ALA n 
1 291 TYR n 
1 292 ASP n 
1 293 TYR n 
1 294 THR n 
1 295 LYS n 
1 296 PRO n 
1 297 ILE n 
1 298 THR n 
1 299 TRP n 
1 300 ILE n 
1 301 THR n 
1 302 ILE n 
1 303 PRO n 
1 304 ARG n 
1 305 GLY n 
1 306 ALA n 
1 307 LYS n 
1 308 SER n 
1 309 LYS n 
1 310 ASP n 
1 311 GLU n 
1 312 VAL n 
1 313 LYS n 
1 314 TYR n 
1 315 TRP n 
1 316 HIS n 
1 317 TRP n 
1 318 LYS n 
1 319 ASN n 
1 320 GLY n 
1 321 MET n 
1 322 PRO n 
1 323 ILE n 
1 324 HIS n 
1 325 THR n 
1 326 ALA n 
1 327 SER n 
1 328 GLY n 
1 329 PHE n 
1 330 GLU n 
1 331 ASP n 
1 332 GLU n 
1 333 GLN n 
1 334 GLY n 
1 335 ARG n 
1 336 ILE n 
1 337 ILE n 
1 338 ILE n 
1 339 ASP n 
1 340 SER n 
1 341 SER n 
1 342 LEU n 
1 343 VAL n 
1 344 HIS n 
1 345 GLY n 
1 346 ASN n 
1 347 ALA n 
1 348 PHE n 
1 349 PRO n 
1 350 PHE n 
1 351 PHE n 
1 352 PRO n 
1 353 PRO n 
1 354 ASP n 
1 355 SER n 
1 356 ASP n 
1 357 GLU n 
1 358 GLN n 
1 359 LYS n 
1 360 LYS n 
1 361 LYS n 
1 362 GLN n 
1 363 GLU n 
1 364 ALA n 
1 365 ASP n 
1 366 GLY n 
1 367 THR n 
1 368 PRO n 
1 369 LYS n 
1 370 ALA n 
1 371 GLN n 
1 372 PHE n 
1 373 VAL n 
1 374 ARG n 
1 375 TRP n 
1 376 THR n 
1 377 ILE n 
1 378 ASP n 
1 379 PRO n 
1 380 ARG n 
1 381 LYS n 
1 382 ASP n 
1 383 ASN n 
1 384 ASN n 
1 385 GLU n 
1 386 GLN n 
1 387 LEU n 
1 388 PRO n 
1 389 ASP n 
1 390 PRO n 
1 391 GLU n 
1 392 VAL n 
1 393 ILE n 
1 394 LEU n 
1 395 ASP n 
1 396 THR n 
1 397 PRO n 
1 398 SER n 
1 399 GLU n 
1 400 PHE n 
1 401 PRO n 
1 402 GLN n 
1 403 ILE n 
1 404 ASP n 
1 405 ASN n 
1 406 ARG n 
1 407 PHE n 
1 408 MET n 
1 409 GLY n 
1 410 VAL n 
1 411 GLU n 
1 412 TYR n 
1 413 SER n 
1 414 SER n 
1 415 ALA n 
1 416 PHE n 
1 417 ILE n 
1 418 ASN n 
1 419 VAL n 
1 420 PHE n 
1 421 VAL n 
1 422 PRO n 
1 423 ASP n 
1 424 ARG n 
1 425 SER n 
1 426 ASP n 
1 427 GLY n 
1 428 ASN n 
1 429 LYS n 
1 430 ASN n 
1 431 VAL n 
1 432 PHE n 
1 433 GLN n 
1 434 GLY n 
1 435 LEU n 
1 436 ASN n 
1 437 GLY n 
1 438 LEU n 
1 439 ALA n 
1 440 HIS n 
1 441 TYR n 
1 442 LYS n 
1 443 ARG n 
1 444 LYS n 
1 445 GLU n 
1 446 GLY n 
1 447 THR n 
1 448 THR n 
1 449 GLU n 
1 450 TRP n 
1 451 TYR n 
1 452 TYR n 
1 453 ALA n 
1 454 GLY n 
1 455 ASP n 
1 456 ASN n 
1 457 CYS n 
1 458 LEU n 
1 459 ILE n 
1 460 GLN n 
1 461 GLU n 
1 462 PRO n 
1 463 VAL n 
1 464 PHE n 
1 465 SER n 
1 466 PRO n 
1 467 ARG n 
1 468 SER n 
1 469 LYS n 
1 470 ASP n 
1 471 ALA n 
1 472 PRO n 
1 473 GLU n 
1 474 GLY n 
1 475 ASP n 
1 476 GLY n 
1 477 PHE n 
1 478 VAL n 
1 479 LEU n 
1 480 ALA n 
1 481 ILE n 
1 482 VAL n 
1 483 ASP n 
1 484 ARG n 
1 485 LEU n 
1 486 ASP n 
1 487 LEU n 
1 488 ASN n 
1 489 ARG n 
1 490 SER n 
1 491 GLU n 
1 492 VAL n 
1 493 VAL n 
1 494 VAL n 
1 495 ILE n 
1 496 ASP n 
1 497 THR n 
1 498 ARG n 
1 499 ASP n 
1 500 PHE n 
1 501 THR n 
1 502 LYS n 
1 503 ALA n 
1 504 VAL n 
1 505 ALA n 
1 506 ALA n 
1 507 VAL n 
1 508 GLN n 
1 509 LEU n 
1 510 PRO n 
1 511 PHE n 
1 512 ALA n 
1 513 ILE n 
1 514 ARG n 
1 515 SER n 
1 516 GLY n 
1 517 ILE n 
1 518 HIS n 
1 519 GLY n 
1 520 GLN n 
1 521 TRP n 
1 522 ILE n 
1 523 PRO n 
1 524 GLY n 
1 525 GLU n 
1 526 VAL n 
1 527 THR n 
1 528 PRO n 
1 529 ASP n 
1 530 PHE n 
1 531 GLU n 
1 532 THR n 
1 533 LYS n 
1 534 GLY n 
1 535 LEU n 
1 536 VAL n 
1 537 ASP n 
1 538 LEU n 
1 539 PRO n 
1 540 LYS n 
1 541 GLU n 
1 542 GLU n 
1 543 HIS n 
1 544 TRP n 
1 545 ALA n 
1 546 PRO n 
1 547 LEU n 
1 548 SER n 
1 549 GLN n 
1 550 SER n 
1 551 PRO n 
1 552 TYR n 
1 553 ASP n 
1 554 PRO n 
1 555 ASP n 
1 556 ALA 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                   556 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PaG_05861 
_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      'Moesziomyces aphidis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     84754 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
FE2 non-polymer         . 'FE (II) ION'         ? 'Fe 2'           55.845  
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  
HBA non-polymer         . P-HYDROXYBENZALDEHYDE ? 'C7 H6 O2'       122.121 
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 
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   -7  ?   ?   ?   A . n 
A 1 2   TRP 2   -6  ?   ?   ?   A . n 
A 1 3   SER 3   -5  ?   ?   ?   A . n 
A 1 4   HIS 4   -4  ?   ?   ?   A . n 
A 1 5   PRO 5   -3  ?   ?   ?   A . n 
A 1 6   GLN 6   -2  ?   ?   ?   A . n 
A 1 7   PHE 7   -1  ?   ?   ?   A . n 
A 1 8   GLU 8   0   ?   ?   ?   A . n 
A 1 9   LYS 9   1   ?   ?   ?   A . n 
A 1 10  ALA 10  2   ?   ?   ?   A . n 
A 1 11  PRO 11  3   ?   ?   ?   A . n 
A 1 12  THR 12  4   ?   ?   ?   A . n 
A 1 13  ALA 13  5   ?   ?   ?   A . n 
A 1 14  THR 14  6   ?   ?   ?   A . n 
A 1 15  GLN 15  7   ?   ?   ?   A . n 
A 1 16  GLU 16  8   ?   ?   ?   A . n 
A 1 17  PRO 17  9   ?   ?   ?   A . n 
A 1 18  VAL 18  10  ?   ?   ?   A . n 
A 1 19  PRO 19  11  ?   ?   ?   A . n 
A 1 20  VAL 20  12  ?   ?   ?   A . n 
A 1 21  PRO 21  13  ?   ?   ?   A . n 
A 1 22  VAL 22  14  ?   ?   ?   A . n 
A 1 23  THR 23  15  ?   ?   ?   A . n 
A 1 24  SER 24  16  ?   ?   ?   A . n 
A 1 25  LYS 25  17  ?   ?   ?   A . n 
A 1 26  ALA 26  18  ?   ?   ?   A . n 
A 1 27  ALA 27  19  ?   ?   ?   A . n 
A 1 28  PRO 28  20  ?   ?   ?   A . n 
A 1 29  SER 29  21  ?   ?   ?   A . n 
A 1 30  HIS 30  22  ?   ?   ?   A . n 
A 1 31  GLY 31  23  ?   ?   ?   A . n 
A 1 32  TYR 32  24  32  TYR TYR A . n 
A 1 33  VAL 33  25  33  VAL VAL A . n 
A 1 34  HIS 34  26  34  HIS HIS A . n 
A 1 35  PRO 35  27  35  PRO PRO A . n 
A 1 36  THR 36  28  36  THR THR A . n 
A 1 37  ASP 37  29  37  ASP ASP A . n 
A 1 38  ILE 38  30  38  ILE ILE A . n 
A 1 39  LEU 39  31  39  LEU LEU A . n 
A 1 40  PRO 40  32  40  PRO PRO A . n 
A 1 41  SER 41  33  41  SER SER A . n 
A 1 42  GLY 42  34  42  GLY GLY A . n 
A 1 43  TRP 43  35  43  TRP TRP A . n 
A 1 44  PRO 44  36  44  PRO PRO A . n 
A 1 45  THR 45  37  45  THR THR A . n 
A 1 46  ALA 46  38  46  ALA ALA A . n 
A 1 47  THR 47  39  47  THR THR A . n 
A 1 48  ASP 48  40  48  ASP ASP A . n 
A 1 49  LEU 49  41  49  LEU LEU A . n 
A 1 50  SER 50  42  50  SER SER A . n 
A 1 51  GLY 51  43  51  GLY GLY A . n 
A 1 52  GLY 52  44  52  GLY GLY A . n 
A 1 53  ALA 53  45  53  ALA ALA A . n 
A 1 54  GLN 54  46  54  GLN GLN A . n 
A 1 55  PRO 55  47  55  PRO PRO A . n 
A 1 56  ARG 56  48  56  ARG ARG A . n 
A 1 57  ARG 57  49  57  ARG ARG A . n 
A 1 58  PHE 58  50  58  PHE PHE A . n 
A 1 59  GLU 59  51  59  GLU GLU A . n 
A 1 60  GLY 60  52  60  GLY GLY A . n 
A 1 61  THR 61  53  61  THR THR A . n 
A 1 62  ILE 62  54  62  ILE ILE A . n 
A 1 63  PHE 63  55  63  PHE PHE A . n 
A 1 64  ASP 64  56  64  ASP ASP A . n 
A 1 65  VAL 65  57  65  VAL VAL A . n 
A 1 66  MET 66  58  66  MET MET A . n 
A 1 67  THR 67  59  67  THR THR A . n 
A 1 68  ARG 68  60  68  ARG ARG A . n 
A 1 69  GLY 69  61  69  GLY GLY A . n 
A 1 70  THR 70  62  70  THR THR A . n 
A 1 71  ILE 71  63  71  ILE ILE A . n 
A 1 72  PRO 72  64  72  PRO PRO A . n 
A 1 73  LYS 73  65  73  LYS LYS A . n 
A 1 74  GLU 74  66  74  GLU GLU A . n 
A 1 75  LEU 75  67  75  LEU LEU A . n 
A 1 76  HIS 76  68  76  HIS HIS A . n 
A 1 77  GLY 77  69  77  GLY GLY A . n 
A 1 78  THR 78  70  78  THR THR A . n 
A 1 79  PHE 79  71  79  PHE PHE A . n 
A 1 80  TYR 80  72  80  TYR TYR A . n 
A 1 81  ARG 81  73  81  ARG ARG A . n 
A 1 82  ILE 82  74  82  ILE ILE A . n 
A 1 83  MET 83  75  83  MET MET A . n 
A 1 84  PRO 84  76  84  PRO PRO A . n 
A 1 85  ASP 85  77  85  ASP ASP A . n 
A 1 86  TYR 86  78  86  TYR TYR A . n 
A 1 87  ALA 87  79  87  ALA ALA A . n 
A 1 88  GLN 88  80  88  GLN GLN A . n 
A 1 89  PRO 89  81  89  PRO PRO A . n 
A 1 90  PRO 90  82  90  PRO PRO A . n 
A 1 91  THR 91  83  91  THR THR A . n 
A 1 92  TYR 92  84  92  TYR TYR A . n 
A 1 93  TYR 93  85  93  TYR TYR A . n 
A 1 94  LYS 94  86  94  LYS LYS A . n 
A 1 95  GLY 95  87  95  GLY GLY A . n 
A 1 96  GLY 96  88  96  GLY GLY A . n 
A 1 97  GLU 97  89  97  GLU GLU A . n 
A 1 98  LEU 98  90  98  LEU LEU A . n 
A 1 99  ASN 99  91  99  ASN ASN A . n 
A 1 100 ALA 100 92  100 ALA ALA A . n 
A 1 101 PRO 101 93  101 PRO PRO A . n 
A 1 102 ILE 102 94  102 ILE ILE A . n 
A 1 103 ASP 103 95  103 ASP ASP A . n 
A 1 104 GLY 104 96  104 GLY GLY A . n 
A 1 105 ASP 105 97  105 ASP ASP A . n 
A 1 106 GLY 106 98  106 GLY GLY A . n 
A 1 107 THR 107 99  107 THR THR A . n 
A 1 108 VAL 108 100 108 VAL VAL A . n 
A 1 109 ALA 109 101 109 ALA ALA A . n 
A 1 110 ALA 110 102 110 ALA ALA A . n 
A 1 111 PHE 111 103 111 PHE PHE A . n 
A 1 112 ARG 112 104 112 ARG ARG A . n 
A 1 113 PHE 113 105 113 PHE PHE A . n 
A 1 114 LYS 114 106 114 LYS LYS A . n 
A 1 115 ASP 115 107 115 ASP ASP A . n 
A 1 116 GLY 116 108 116 GLY GLY A . n 
A 1 117 LYS 117 109 117 LYS LYS A . n 
A 1 118 VAL 118 110 118 VAL VAL A . n 
A 1 119 ASP 119 111 119 ASP ASP A . n 
A 1 120 TYR 120 112 120 TYR TYR A . n 
A 1 121 ARG 121 113 121 ARG ARG A . n 
A 1 122 GLN 122 114 122 GLN GLN A . n 
A 1 123 ARG 123 115 123 ARG ARG A . n 
A 1 124 PHE 124 116 124 PHE PHE A . n 
A 1 125 VAL 125 117 125 VAL VAL A . n 
A 1 126 GLU 126 118 126 GLU GLU A . n 
A 1 127 THR 127 119 127 THR THR A . n 
A 1 128 ASP 128 120 128 ASP ASP A . n 
A 1 129 ARG 129 121 129 ARG ARG A . n 
A 1 130 PHE 130 122 130 PHE PHE A . n 
A 1 131 LYS 131 123 131 LYS LYS A . n 
A 1 132 VAL 132 124 132 VAL VAL A . n 
A 1 133 GLU 133 125 133 GLU GLU A . n 
A 1 134 ARG 134 126 134 ARG ARG A . n 
A 1 135 ARG 135 127 135 ARG ARG A . n 
A 1 136 ALA 136 128 136 ALA ALA A . n 
A 1 137 ARG 137 129 137 ARG ARG A . n 
A 1 138 LYS 138 130 138 LYS LYS A . n 
A 1 139 SER 139 131 139 SER SER A . n 
A 1 140 MET 140 132 140 MET MET A . n 
A 1 141 TYR 141 133 141 TYR TYR A . n 
A 1 142 GLY 142 134 142 GLY GLY A . n 
A 1 143 LEU 143 135 143 LEU LEU A . n 
A 1 144 TYR 144 136 144 TYR TYR A . n 
A 1 145 ARG 145 137 145 ARG ARG A . n 
A 1 146 ASN 146 138 146 ASN ASN A . n 
A 1 147 PRO 147 139 147 PRO PRO A . n 
A 1 148 TYR 148 140 148 TYR TYR A . n 
A 1 149 THR 149 141 149 THR THR A . n 
A 1 150 HIS 150 142 150 HIS HIS A . n 
A 1 151 HIS 151 143 151 HIS HIS A . n 
A 1 152 PRO 152 144 152 PRO PRO A . n 
A 1 153 CYS 153 145 153 CYS CYS A . n 
A 1 154 VAL 154 146 154 VAL VAL A . n 
A 1 155 ARG 155 147 155 ARG ARG A . n 
A 1 156 GLN 156 148 156 GLN GLN A . n 
A 1 157 THR 157 149 157 THR THR A . n 
A 1 158 VAL 158 150 158 VAL VAL A . n 
A 1 159 GLU 159 151 159 GLU GLU A . n 
A 1 160 SER 160 152 160 SER SER A . n 
A 1 161 THR 161 153 161 THR THR A . n 
A 1 162 ALA 162 154 162 ALA ALA A . n 
A 1 163 ASN 163 155 163 ASN ASN A . n 
A 1 164 THR 164 156 164 THR THR A . n 
A 1 165 ASN 165 157 165 ASN ASN A . n 
A 1 166 VAL 166 158 166 VAL VAL A . n 
A 1 167 VAL 167 159 167 VAL VAL A . n 
A 1 168 MET 168 160 168 MET MET A . n 
A 1 169 HIS 169 161 169 HIS HIS A . n 
A 1 170 ALA 170 162 170 ALA ALA A . n 
A 1 171 GLY 171 163 171 GLY GLY A . n 
A 1 172 ARG 172 164 172 ARG ARG A . n 
A 1 173 PHE 173 165 173 PHE PHE A . n 
A 1 174 LEU 174 166 174 LEU LEU A . n 
A 1 175 ALA 175 167 175 ALA ALA A . n 
A 1 176 MET 176 168 176 MET MET A . n 
A 1 177 LYS 177 169 177 LYS LYS A . n 
A 1 178 GLU 178 170 178 GLU GLU A . n 
A 1 179 ASN 179 171 179 ASN ASN A . n 
A 1 180 GLY 180 172 180 GLY GLY A . n 
A 1 181 ASN 181 173 181 ASN ASN A . n 
A 1 182 ALA 182 174 182 ALA ALA A . n 
A 1 183 TYR 183 175 183 TYR TYR A . n 
A 1 184 GLU 184 176 184 GLU GLU A . n 
A 1 185 MET 185 177 185 MET MET A . n 
A 1 186 ASP 186 178 186 ASP ASP A . n 
A 1 187 PRO 187 179 187 PRO PRO A . n 
A 1 188 HIS 188 180 188 HIS HIS A . n 
A 1 189 THR 189 181 189 THR THR A . n 
A 1 190 LEU 190 182 190 LEU LEU A . n 
A 1 191 LYS 191 183 191 LYS LYS A . n 
A 1 192 THR 192 184 192 THR THR A . n 
A 1 193 LEU 193 185 193 LEU LEU A . n 
A 1 194 GLY 194 186 194 GLY GLY A . n 
A 1 195 TYR 195 187 195 TYR TYR A . n 
A 1 196 ASN 196 188 196 ASN ASN A . n 
A 1 197 PRO 197 189 197 PRO PRO A . n 
A 1 198 PHE 198 190 198 PHE PHE A . n 
A 1 199 ASN 199 191 199 ASN ASN A . n 
A 1 200 LEU 200 192 200 LEU LEU A . n 
A 1 201 PRO 201 193 201 PRO PRO A . n 
A 1 202 SER 202 194 202 SER SER A . n 
A 1 203 LYS 203 195 203 LYS LYS A . n 
A 1 204 THR 204 196 204 THR THR A . n 
A 1 205 MET 205 197 205 MET MET A . n 
A 1 206 THR 206 198 206 THR THR A . n 
A 1 207 ALA 207 199 207 ALA ALA A . n 
A 1 208 HIS 208 200 208 HIS HIS A . n 
A 1 209 PRO 209 201 209 PRO PRO A . n 
A 1 210 LYS 210 202 210 LYS LYS A . n 
A 1 211 GLN 211 203 211 GLN GLN A . n 
A 1 212 CYS 212 204 212 CYS CYS A . n 
A 1 213 SER 213 205 213 SER SER A . n 
A 1 214 VAL 214 206 214 VAL VAL A . n 
A 1 215 THR 215 207 215 THR THR A . n 
A 1 216 GLY 216 208 216 GLY GLY A . n 
A 1 217 ASN 217 209 217 ASN ASN A . n 
A 1 218 LEU 218 210 218 LEU LEU A . n 
A 1 219 VAL 219 211 219 VAL VAL A . n 
A 1 220 GLY 220 212 220 GLY GLY A . n 
A 1 221 PHE 221 213 221 PHE PHE A . n 
A 1 222 GLY 222 214 222 GLY GLY A . n 
A 1 223 TYR 223 215 223 TYR TYR A . n 
A 1 224 GLU 224 216 224 GLU GLU A . n 
A 1 225 ALA 225 217 225 ALA ALA A . n 
A 1 226 LYS 226 218 226 LYS LYS A . n 
A 1 227 GLY 227 219 227 GLY GLY A . n 
A 1 228 LEU 228 220 228 LEU LEU A . n 
A 1 229 ALA 229 221 229 ALA ALA A . n 
A 1 230 THR 230 222 230 THR THR A . n 
A 1 231 LYS 231 223 231 LYS LYS A . n 
A 1 232 ASP 232 224 232 ASP ASP A . n 
A 1 233 VAL 233 225 233 VAL VAL A . n 
A 1 234 TYR 234 226 234 TYR TYR A . n 
A 1 235 TYR 235 227 235 TYR TYR A . n 
A 1 236 PHE 236 228 236 PHE PHE A . n 
A 1 237 GLU 237 229 237 GLU GLU A . n 
A 1 238 VAL 238 230 238 VAL VAL A . n 
A 1 239 ASP 239 231 239 ASP ASP A . n 
A 1 240 PRO 240 232 240 PRO PRO A . n 
A 1 241 SER 241 233 241 SER SER A . n 
A 1 242 GLY 242 234 242 GLY GLY A . n 
A 1 243 LYS 243 235 243 LYS LYS A . n 
A 1 244 VAL 244 236 244 VAL VAL A . n 
A 1 245 VAL 245 237 245 VAL VAL A . n 
A 1 246 ARG 246 238 246 ARG ARG A . n 
A 1 247 ASP 247 239 247 ASP ASP A . n 
A 1 248 LEU 248 240 248 LEU LEU A . n 
A 1 249 TRP 249 241 249 TRP TRP A . n 
A 1 250 LEU 250 242 250 LEU LEU A . n 
A 1 251 GLU 251 243 251 GLU GLU A . n 
A 1 252 ALA 252 244 252 ALA ALA A . n 
A 1 253 PRO 253 245 253 PRO PRO A . n 
A 1 254 TRP 254 246 254 TRP TRP A . n 
A 1 255 CYS 255 247 255 CYS CYS A . n 
A 1 256 ALA 256 248 256 ALA ALA A . n 
A 1 257 PHE 257 249 257 PHE PHE A . n 
A 1 258 ILE 258 250 258 ILE ILE A . n 
A 1 259 HIS 259 251 259 HIS HIS A . n 
A 1 260 ASP 260 252 260 ASP ASP A . n 
A 1 261 CYS 261 253 261 CYS CYS A . n 
A 1 262 ALA 262 254 262 ALA ALA A . n 
A 1 263 LEU 263 255 263 LEU LEU A . n 
A 1 264 THR 264 256 264 THR THR A . n 
A 1 265 PRO 265 257 265 PRO PRO A . n 
A 1 266 ASN 266 258 266 ASN ASN A . n 
A 1 267 TYR 267 259 267 TYR TYR A . n 
A 1 268 LEU 268 260 268 LEU LEU A . n 
A 1 269 VAL 269 261 269 VAL VAL A . n 
A 1 270 LEU 270 262 270 LEU LEU A . n 
A 1 271 MET 271 263 271 MET MET A . n 
A 1 272 LEU 272 264 272 LEU LEU A . n 
A 1 273 TRP 273 265 273 TRP TRP A . n 
A 1 274 PRO 274 266 274 PRO PRO A . n 
A 1 275 PHE 275 267 275 PHE PHE A . n 
A 1 276 GLU 276 268 276 GLU GLU A . n 
A 1 277 ALA 277 269 277 ALA ALA A . n 
A 1 278 ASN 278 270 278 ASN ASN A . n 
A 1 279 LEU 279 271 279 LEU LEU A . n 
A 1 280 GLU 280 272 280 GLU GLU A . n 
A 1 281 ARG 281 273 281 ARG ARG A . n 
A 1 282 MET 282 274 282 MET MET A . n 
A 1 283 LYS 283 275 283 LYS LYS A . n 
A 1 284 ALA 284 276 284 ALA ALA A . n 
A 1 285 GLY 285 277 285 GLY GLY A . n 
A 1 286 GLY 286 278 286 GLY GLY A . n 
A 1 287 HIS 287 279 287 HIS HIS A . n 
A 1 288 HIS 288 280 288 HIS HIS A . n 
A 1 289 TRP 289 281 289 TRP TRP A . n 
A 1 290 ALA 290 282 290 ALA ALA A . n 
A 1 291 TYR 291 283 291 TYR TYR A . n 
A 1 292 ASP 292 284 292 ASP ASP A . n 
A 1 293 TYR 293 285 293 TYR TYR A . n 
A 1 294 THR 294 286 294 THR THR A . n 
A 1 295 LYS 295 287 295 LYS LYS A . n 
A 1 296 PRO 296 288 296 PRO PRO A . n 
A 1 297 ILE 297 289 297 ILE ILE A . n 
A 1 298 THR 298 290 298 THR THR A . n 
A 1 299 TRP 299 291 299 TRP TRP A . n 
A 1 300 ILE 300 292 300 ILE ILE A . n 
A 1 301 THR 301 293 301 THR THR A . n 
A 1 302 ILE 302 294 302 ILE ILE A . n 
A 1 303 PRO 303 295 303 PRO PRO A . n 
A 1 304 ARG 304 296 304 ARG ARG A . n 
A 1 305 GLY 305 297 305 GLY GLY A . n 
A 1 306 ALA 306 298 306 ALA ALA A . n 
A 1 307 LYS 307 299 307 LYS LYS A . n 
A 1 308 SER 308 300 308 SER SER A . n 
A 1 309 LYS 309 301 309 LYS LYS A . n 
A 1 310 ASP 310 302 310 ASP ASP A . n 
A 1 311 GLU 311 303 311 GLU GLU A . n 
A 1 312 VAL 312 304 312 VAL VAL A . n 
A 1 313 LYS 313 305 313 LYS LYS A . n 
A 1 314 TYR 314 306 314 TYR TYR A . n 
A 1 315 TRP 315 307 315 TRP TRP A . n 
A 1 316 HIS 316 308 316 HIS HIS A . n 
A 1 317 TRP 317 309 317 TRP TRP A . n 
A 1 318 LYS 318 310 318 LYS LYS A . n 
A 1 319 ASN 319 311 319 ASN ASN A . n 
A 1 320 GLY 320 312 320 GLY GLY A . n 
A 1 321 MET 321 313 321 MET MET A . n 
A 1 322 PRO 322 314 322 PRO PRO A . n 
A 1 323 ILE 323 315 323 ILE ILE A . n 
A 1 324 HIS 324 316 324 HIS HIS A . n 
A 1 325 THR 325 317 325 THR THR A . n 
A 1 326 ALA 326 318 326 ALA ALA A . n 
A 1 327 SER 327 319 327 SER SER A . n 
A 1 328 GLY 328 320 328 GLY GLY A . n 
A 1 329 PHE 329 321 329 PHE PHE A . n 
A 1 330 GLU 330 322 330 GLU GLU A . n 
A 1 331 ASP 331 323 331 ASP ASP A . n 
A 1 332 GLU 332 324 332 GLU GLU A . n 
A 1 333 GLN 333 325 333 GLN GLN A . n 
A 1 334 GLY 334 326 334 GLY GLY A . n 
A 1 335 ARG 335 327 335 ARG ARG A . n 
A 1 336 ILE 336 328 336 ILE ILE A . n 
A 1 337 ILE 337 329 337 ILE ILE A . n 
A 1 338 ILE 338 330 338 ILE ILE A . n 
A 1 339 ASP 339 331 339 ASP ASP A . n 
A 1 340 SER 340 332 340 SER SER A . n 
A 1 341 SER 341 333 341 SER SER A . n 
A 1 342 LEU 342 334 342 LEU LEU A . n 
A 1 343 VAL 343 335 343 VAL VAL A . n 
A 1 344 HIS 344 336 344 HIS HIS A . n 
A 1 345 GLY 345 337 345 GLY GLY A . n 
A 1 346 ASN 346 338 346 ASN ASN A . n 
A 1 347 ALA 347 339 347 ALA ALA A . n 
A 1 348 PHE 348 340 348 PHE PHE A . n 
A 1 349 PRO 349 341 349 PRO PRO A . n 
A 1 350 PHE 350 342 350 PHE PHE A . n 
A 1 351 PHE 351 343 351 PHE PHE A . n 
A 1 352 PRO 352 344 352 PRO PRO A . n 
A 1 353 PRO 353 345 353 PRO PRO A . n 
A 1 354 ASP 354 346 354 ASP ASP A . n 
A 1 355 SER 355 347 355 SER SER A . n 
A 1 356 ASP 356 348 356 ASP ASP A . n 
A 1 357 GLU 357 349 357 GLU GLU A . n 
A 1 358 GLN 358 350 358 GLN GLN A . n 
A 1 359 LYS 359 351 359 LYS LYS A . n 
A 1 360 LYS 360 352 360 LYS LYS A . n 
A 1 361 LYS 361 353 361 LYS LYS A . n 
A 1 362 GLN 362 354 362 GLN GLN A . n 
A 1 363 GLU 363 355 363 GLU GLU A . n 
A 1 364 ALA 364 356 364 ALA ALA A . n 
A 1 365 ASP 365 357 365 ASP ASP A . n 
A 1 366 GLY 366 358 366 GLY GLY A . n 
A 1 367 THR 367 359 367 THR THR A . n 
A 1 368 PRO 368 360 368 PRO PRO A . n 
A 1 369 LYS 369 361 369 LYS LYS A . n 
A 1 370 ALA 370 362 370 ALA ALA A . n 
A 1 371 GLN 371 363 371 GLN GLN A . n 
A 1 372 PHE 372 364 372 PHE PHE A . n 
A 1 373 VAL 373 365 373 VAL VAL A . n 
A 1 374 ARG 374 366 374 ARG ARG A . n 
A 1 375 TRP 375 367 375 TRP TRP A . n 
A 1 376 THR 376 368 376 THR THR A . n 
A 1 377 ILE 377 369 377 ILE ILE A . n 
A 1 378 ASP 378 370 378 ASP ASP A . n 
A 1 379 PRO 379 371 379 PRO PRO A . n 
A 1 380 ARG 380 372 380 ARG ARG A . n 
A 1 381 LYS 381 373 381 LYS LYS A . n 
A 1 382 ASP 382 374 382 ASP ASP A . n 
A 1 383 ASN 383 375 383 ASN ASN A . n 
A 1 384 ASN 384 376 384 ASN ASN A . n 
A 1 385 GLU 385 377 385 GLU GLU A . n 
A 1 386 GLN 386 378 386 GLN GLN A . n 
A 1 387 LEU 387 379 387 LEU LEU A . n 
A 1 388 PRO 388 380 388 PRO PRO A . n 
A 1 389 ASP 389 381 389 ASP ASP A . n 
A 1 390 PRO 390 382 390 PRO PRO A . n 
A 1 391 GLU 391 383 391 GLU GLU A . n 
A 1 392 VAL 392 384 392 VAL VAL A . n 
A 1 393 ILE 393 385 393 ILE ILE A . n 
A 1 394 LEU 394 386 394 LEU LEU A . n 
A 1 395 ASP 395 387 395 ASP ASP A . n 
A 1 396 THR 396 388 396 THR THR A . n 
A 1 397 PRO 397 389 397 PRO PRO A . n 
A 1 398 SER 398 390 398 SER SER A . n 
A 1 399 GLU 399 391 399 GLU GLU A . n 
A 1 400 PHE 400 392 400 PHE PHE A . n 
A 1 401 PRO 401 393 401 PRO PRO A . n 
A 1 402 GLN 402 394 402 GLN GLN A . n 
A 1 403 ILE 403 395 403 ILE ILE A . n 
A 1 404 ASP 404 396 404 ASP ASP A . n 
A 1 405 ASN 405 397 405 ASN ASN A . n 
A 1 406 ARG 406 398 406 ARG ARG A . n 
A 1 407 PHE 407 399 407 PHE PHE A . n 
A 1 408 MET 408 400 408 MET MET A . n 
A 1 409 GLY 409 401 409 GLY GLY A . n 
A 1 410 VAL 410 402 410 VAL VAL A . n 
A 1 411 GLU 411 403 411 GLU GLU A . n 
A 1 412 TYR 412 404 412 TYR TYR A . n 
A 1 413 SER 413 405 413 SER SER A . n 
A 1 414 SER 414 406 414 SER SER A . n 
A 1 415 ALA 415 407 415 ALA ALA A . n 
A 1 416 PHE 416 408 416 PHE PHE A . n 
A 1 417 ILE 417 409 417 ILE ILE A . n 
A 1 418 ASN 418 410 418 ASN ASN A . n 
A 1 419 VAL 419 411 419 VAL VAL A . n 
A 1 420 PHE 420 412 420 PHE PHE A . n 
A 1 421 VAL 421 413 421 VAL VAL A . n 
A 1 422 PRO 422 414 422 PRO PRO A . n 
A 1 423 ASP 423 415 423 ASP ASP A . n 
A 1 424 ARG 424 416 424 ARG ARG A . n 
A 1 425 SER 425 417 425 SER SER A . n 
A 1 426 ASP 426 418 426 ASP ASP A . n 
A 1 427 GLY 427 419 427 GLY GLY A . n 
A 1 428 ASN 428 420 428 ASN ASN A . n 
A 1 429 LYS 429 421 429 LYS LYS A . n 
A 1 430 ASN 430 422 430 ASN ASN A . n 
A 1 431 VAL 431 423 431 VAL VAL A . n 
A 1 432 PHE 432 424 432 PHE PHE A . n 
A 1 433 GLN 433 425 433 GLN GLN A . n 
A 1 434 GLY 434 426 434 GLY GLY A . n 
A 1 435 LEU 435 427 435 LEU LEU A . n 
A 1 436 ASN 436 428 436 ASN ASN A . n 
A 1 437 GLY 437 429 437 GLY GLY A . n 
A 1 438 LEU 438 430 438 LEU LEU A . n 
A 1 439 ALA 439 431 439 ALA ALA A . n 
A 1 440 HIS 440 432 440 HIS HIS A . n 
A 1 441 TYR 441 433 441 TYR TYR A . n 
A 1 442 LYS 442 434 442 LYS LYS A . n 
A 1 443 ARG 443 435 443 ARG ARG A . n 
A 1 444 LYS 444 436 444 LYS LYS A . n 
A 1 445 GLU 445 437 445 GLU GLU A . n 
A 1 446 GLY 446 438 446 GLY GLY A . n 
A 1 447 THR 447 439 447 THR THR A . n 
A 1 448 THR 448 440 448 THR THR A . n 
A 1 449 GLU 449 441 449 GLU GLU A . n 
A 1 450 TRP 450 442 450 TRP TRP A . n 
A 1 451 TYR 451 443 451 TYR TYR A . n 
A 1 452 TYR 452 444 452 TYR TYR A . n 
A 1 453 ALA 453 445 453 ALA ALA A . n 
A 1 454 GLY 454 446 454 GLY GLY A . n 
A 1 455 ASP 455 447 455 ASP ASP A . n 
A 1 456 ASN 456 448 456 ASN ASN A . n 
A 1 457 CYS 457 449 457 CYS CYS A . n 
A 1 458 LEU 458 450 458 LEU LEU A . n 
A 1 459 ILE 459 451 459 ILE ILE A . n 
A 1 460 GLN 460 452 460 GLN GLN A . n 
A 1 461 GLU 461 453 461 GLU GLU A . n 
A 1 462 PRO 462 454 462 PRO PRO A . n 
A 1 463 VAL 463 455 463 VAL VAL A . n 
A 1 464 PHE 464 456 464 PHE PHE A . n 
A 1 465 SER 465 457 465 SER SER A . n 
A 1 466 PRO 466 458 466 PRO PRO A . n 
A 1 467 ARG 467 459 467 ARG ARG A . n 
A 1 468 SER 468 460 468 SER SER A . n 
A 1 469 LYS 469 461 469 LYS LYS A . n 
A 1 470 ASP 470 462 470 ASP ASP A . n 
A 1 471 ALA 471 463 471 ALA ALA A . n 
A 1 472 PRO 472 464 472 PRO PRO A . n 
A 1 473 GLU 473 465 473 GLU GLU A . n 
A 1 474 GLY 474 466 474 GLY GLY A . n 
A 1 475 ASP 475 467 475 ASP ASP A . n 
A 1 476 GLY 476 468 476 GLY GLY A . n 
A 1 477 PHE 477 469 477 PHE PHE A . n 
A 1 478 VAL 478 470 478 VAL VAL A . n 
A 1 479 LEU 479 471 479 LEU LEU A . n 
A 1 480 ALA 480 472 480 ALA ALA A . n 
A 1 481 ILE 481 473 481 ILE ILE A . n 
A 1 482 VAL 482 474 482 VAL VAL A . n 
A 1 483 ASP 483 475 483 ASP ASP A . n 
A 1 484 ARG 484 476 484 ARG ARG A . n 
A 1 485 LEU 485 477 485 LEU LEU A . n 
A 1 486 ASP 486 478 486 ASP ASP A . n 
A 1 487 LEU 487 479 487 LEU LEU A . n 
A 1 488 ASN 488 480 488 ASN ASN A . n 
A 1 489 ARG 489 481 489 ARG ARG A . n 
A 1 490 SER 490 482 490 SER SER A . n 
A 1 491 GLU 491 483 491 GLU GLU A . n 
A 1 492 VAL 492 484 492 VAL VAL A . n 
A 1 493 VAL 493 485 493 VAL VAL A . n 
A 1 494 VAL 494 486 494 VAL VAL A . n 
A 1 495 ILE 495 487 495 ILE ILE A . n 
A 1 496 ASP 496 488 496 ASP ASP A . n 
A 1 497 THR 497 489 497 THR THR A . n 
A 1 498 ARG 498 490 498 ARG ARG A . n 
A 1 499 ASP 499 491 499 ASP ASP A . n 
A 1 500 PHE 500 492 500 PHE PHE A . n 
A 1 501 THR 501 493 501 THR THR A . n 
A 1 502 LYS 502 494 502 LYS LYS A . n 
A 1 503 ALA 503 495 503 ALA ALA A . n 
A 1 504 VAL 504 496 504 VAL VAL A . n 
A 1 505 ALA 505 497 505 ALA ALA A . n 
A 1 506 ALA 506 498 506 ALA ALA A . n 
A 1 507 VAL 507 499 507 VAL VAL A . n 
A 1 508 GLN 508 500 508 GLN GLN A . n 
A 1 509 LEU 509 501 509 LEU LEU A . n 
A 1 510 PRO 510 502 510 PRO PRO A . n 
A 1 511 PHE 511 503 511 PHE PHE A . n 
A 1 512 ALA 512 504 512 ALA ALA A . n 
A 1 513 ILE 513 505 513 ILE ILE A . n 
A 1 514 ARG 514 506 514 ARG ARG A . n 
A 1 515 SER 515 507 515 SER SER A . n 
A 1 516 GLY 516 508 516 GLY GLY A . n 
A 1 517 ILE 517 509 517 ILE ILE A . n 
A 1 518 HIS 518 510 518 HIS HIS A . n 
A 1 519 GLY 519 511 519 GLY GLY A . n 
A 1 520 GLN 520 512 520 GLN GLN A . n 
A 1 521 TRP 521 513 521 TRP TRP A . n 
A 1 522 ILE 522 514 522 ILE ILE A . n 
A 1 523 PRO 523 515 523 PRO PRO A . n 
A 1 524 GLY 524 516 524 GLY GLY A . n 
A 1 525 GLU 525 517 525 GLU GLU A . n 
A 1 526 VAL 526 518 526 VAL VAL A . n 
A 1 527 THR 527 519 527 THR THR A . n 
A 1 528 PRO 528 520 528 PRO PRO A . n 
A 1 529 ASP 529 521 529 ASP ASP A . n 
A 1 530 PHE 530 522 530 PHE PHE A . n 
A 1 531 GLU 531 523 531 GLU GLU A . n 
A 1 532 THR 532 524 532 THR THR A . n 
A 1 533 LYS 533 525 533 LYS LYS A . n 
A 1 534 GLY 534 526 534 GLY GLY A . n 
A 1 535 LEU 535 527 535 LEU LEU A . n 
A 1 536 VAL 536 528 536 VAL VAL A . n 
A 1 537 ASP 537 529 537 ASP ASP A . n 
A 1 538 LEU 538 530 538 LEU LEU A . n 
A 1 539 PRO 539 531 539 PRO PRO A . n 
A 1 540 LYS 540 532 540 LYS LYS A . n 
A 1 541 GLU 541 533 541 GLU GLU A . n 
A 1 542 GLU 542 534 542 GLU GLU A . n 
A 1 543 HIS 543 535 543 HIS HIS A . n 
A 1 544 TRP 544 536 544 TRP TRP A . n 
A 1 545 ALA 545 537 545 ALA ALA A . n 
A 1 546 PRO 546 538 546 PRO PRO A . n 
A 1 547 LEU 547 539 547 LEU LEU A . n 
A 1 548 SER 548 540 548 SER SER A . n 
A 1 549 GLN 549 541 549 GLN GLN A . n 
A 1 550 SER 550 542 550 SER SER A . n 
A 1 551 PRO 551 543 551 PRO PRO A . n 
A 1 552 TYR 552 544 552 TYR TYR A . n 
A 1 553 ASP 553 545 553 ASP ASP A . n 
A 1 554 PRO 554 546 554 PRO PRO A . n 
A 1 555 ASP 555 547 555 ASP ASP A . n 
A 1 556 ALA 556 548 556 ALA ALA A . n 
B 1 1   MET 1   -7  ?   ?   ?   B . n 
B 1 2   TRP 2   -6  ?   ?   ?   B . n 
B 1 3   SER 3   -5  ?   ?   ?   B . n 
B 1 4   HIS 4   -4  ?   ?   ?   B . n 
B 1 5   PRO 5   -3  ?   ?   ?   B . n 
B 1 6   GLN 6   -2  ?   ?   ?   B . n 
B 1 7   PHE 7   -1  ?   ?   ?   B . n 
B 1 8   GLU 8   0   ?   ?   ?   B . n 
B 1 9   LYS 9   1   ?   ?   ?   B . n 
B 1 10  ALA 10  2   ?   ?   ?   B . n 
B 1 11  PRO 11  3   ?   ?   ?   B . n 
B 1 12  THR 12  4   ?   ?   ?   B . n 
B 1 13  ALA 13  5   ?   ?   ?   B . n 
B 1 14  THR 14  6   ?   ?   ?   B . n 
B 1 15  GLN 15  7   ?   ?   ?   B . n 
B 1 16  GLU 16  8   ?   ?   ?   B . n 
B 1 17  PRO 17  9   ?   ?   ?   B . n 
B 1 18  VAL 18  10  ?   ?   ?   B . n 
B 1 19  PRO 19  11  ?   ?   ?   B . n 
B 1 20  VAL 20  12  ?   ?   ?   B . n 
B 1 21  PRO 21  13  ?   ?   ?   B . n 
B 1 22  VAL 22  14  ?   ?   ?   B . n 
B 1 23  THR 23  15  ?   ?   ?   B . n 
B 1 24  SER 24  16  ?   ?   ?   B . n 
B 1 25  LYS 25  17  ?   ?   ?   B . n 
B 1 26  ALA 26  18  ?   ?   ?   B . n 
B 1 27  ALA 27  19  ?   ?   ?   B . n 
B 1 28  PRO 28  20  ?   ?   ?   B . n 
B 1 29  SER 29  21  ?   ?   ?   B . n 
B 1 30  HIS 30  22  ?   ?   ?   B . n 
B 1 31  GLY 31  23  ?   ?   ?   B . n 
B 1 32  TYR 32  24  32  TYR TYR B . n 
B 1 33  VAL 33  25  33  VAL VAL B . n 
B 1 34  HIS 34  26  34  HIS HIS B . n 
B 1 35  PRO 35  27  35  PRO PRO B . n 
B 1 36  THR 36  28  36  THR THR B . n 
B 1 37  ASP 37  29  37  ASP ASP B . n 
B 1 38  ILE 38  30  38  ILE ILE B . n 
B 1 39  LEU 39  31  39  LEU LEU B . n 
B 1 40  PRO 40  32  40  PRO PRO B . n 
B 1 41  SER 41  33  41  SER SER B . n 
B 1 42  GLY 42  34  42  GLY GLY B . n 
B 1 43  TRP 43  35  43  TRP TRP B . n 
B 1 44  PRO 44  36  44  PRO PRO B . n 
B 1 45  THR 45  37  45  THR THR B . n 
B 1 46  ALA 46  38  46  ALA ALA B . n 
B 1 47  THR 47  39  47  THR THR B . n 
B 1 48  ASP 48  40  48  ASP ASP B . n 
B 1 49  LEU 49  41  49  LEU LEU B . n 
B 1 50  SER 50  42  50  SER SER B . n 
B 1 51  GLY 51  43  51  GLY GLY B . n 
B 1 52  GLY 52  44  52  GLY GLY B . n 
B 1 53  ALA 53  45  53  ALA ALA B . n 
B 1 54  GLN 54  46  54  GLN GLN B . n 
B 1 55  PRO 55  47  55  PRO PRO B . n 
B 1 56  ARG 56  48  56  ARG ARG B . n 
B 1 57  ARG 57  49  57  ARG ARG B . n 
B 1 58  PHE 58  50  58  PHE PHE B . n 
B 1 59  GLU 59  51  59  GLU GLU B . n 
B 1 60  GLY 60  52  60  GLY GLY B . n 
B 1 61  THR 61  53  61  THR THR B . n 
B 1 62  ILE 62  54  62  ILE ILE B . n 
B 1 63  PHE 63  55  63  PHE PHE B . n 
B 1 64  ASP 64  56  64  ASP ASP B . n 
B 1 65  VAL 65  57  65  VAL VAL B . n 
B 1 66  MET 66  58  66  MET MET B . n 
B 1 67  THR 67  59  67  THR THR B . n 
B 1 68  ARG 68  60  68  ARG ARG B . n 
B 1 69  GLY 69  61  69  GLY GLY B . n 
B 1 70  THR 70  62  70  THR THR B . n 
B 1 71  ILE 71  63  71  ILE ILE B . n 
B 1 72  PRO 72  64  72  PRO PRO B . n 
B 1 73  LYS 73  65  73  LYS LYS B . n 
B 1 74  GLU 74  66  74  GLU GLU B . n 
B 1 75  LEU 75  67  75  LEU LEU B . n 
B 1 76  HIS 76  68  76  HIS HIS B . n 
B 1 77  GLY 77  69  77  GLY GLY B . n 
B 1 78  THR 78  70  78  THR THR B . n 
B 1 79  PHE 79  71  79  PHE PHE B . n 
B 1 80  TYR 80  72  80  TYR TYR B . n 
B 1 81  ARG 81  73  81  ARG ARG B . n 
B 1 82  ILE 82  74  82  ILE ILE B . n 
B 1 83  MET 83  75  83  MET MET B . n 
B 1 84  PRO 84  76  84  PRO PRO B . n 
B 1 85  ASP 85  77  85  ASP ASP B . n 
B 1 86  TYR 86  78  86  TYR TYR B . n 
B 1 87  ALA 87  79  87  ALA ALA B . n 
B 1 88  GLN 88  80  88  GLN GLN B . n 
B 1 89  PRO 89  81  89  PRO PRO B . n 
B 1 90  PRO 90  82  90  PRO PRO B . n 
B 1 91  THR 91  83  91  THR THR B . n 
B 1 92  TYR 92  84  92  TYR TYR B . n 
B 1 93  TYR 93  85  93  TYR TYR B . n 
B 1 94  LYS 94  86  94  LYS LYS B . n 
B 1 95  GLY 95  87  95  GLY GLY B . n 
B 1 96  GLY 96  88  96  GLY GLY B . n 
B 1 97  GLU 97  89  97  GLU GLU B . n 
B 1 98  LEU 98  90  98  LEU LEU B . n 
B 1 99  ASN 99  91  99  ASN ASN B . n 
B 1 100 ALA 100 92  100 ALA ALA B . n 
B 1 101 PRO 101 93  101 PRO PRO B . n 
B 1 102 ILE 102 94  102 ILE ILE B . n 
B 1 103 ASP 103 95  103 ASP ASP B . n 
B 1 104 GLY 104 96  104 GLY GLY B . n 
B 1 105 ASP 105 97  105 ASP ASP B . n 
B 1 106 GLY 106 98  106 GLY GLY B . n 
B 1 107 THR 107 99  107 THR THR B . n 
B 1 108 VAL 108 100 108 VAL VAL B . n 
B 1 109 ALA 109 101 109 ALA ALA B . n 
B 1 110 ALA 110 102 110 ALA ALA B . n 
B 1 111 PHE 111 103 111 PHE PHE B . n 
B 1 112 ARG 112 104 112 ARG ARG B . n 
B 1 113 PHE 113 105 113 PHE PHE B . n 
B 1 114 LYS 114 106 114 LYS LYS B . n 
B 1 115 ASP 115 107 115 ASP ASP B . n 
B 1 116 GLY 116 108 116 GLY GLY B . n 
B 1 117 LYS 117 109 117 LYS LYS B . n 
B 1 118 VAL 118 110 118 VAL VAL B . n 
B 1 119 ASP 119 111 119 ASP ASP B . n 
B 1 120 TYR 120 112 120 TYR TYR B . n 
B 1 121 ARG 121 113 121 ARG ARG B . n 
B 1 122 GLN 122 114 122 GLN GLN B . n 
B 1 123 ARG 123 115 123 ARG ARG B . n 
B 1 124 PHE 124 116 124 PHE PHE B . n 
B 1 125 VAL 125 117 125 VAL VAL B . n 
B 1 126 GLU 126 118 126 GLU GLU B . n 
B 1 127 THR 127 119 127 THR THR B . n 
B 1 128 ASP 128 120 128 ASP ASP B . n 
B 1 129 ARG 129 121 129 ARG ARG B . n 
B 1 130 PHE 130 122 130 PHE PHE B . n 
B 1 131 LYS 131 123 131 LYS LYS B . n 
B 1 132 VAL 132 124 132 VAL VAL B . n 
B 1 133 GLU 133 125 133 GLU GLU B . n 
B 1 134 ARG 134 126 134 ARG ARG B . n 
B 1 135 ARG 135 127 135 ARG ARG B . n 
B 1 136 ALA 136 128 136 ALA ALA B . n 
B 1 137 ARG 137 129 137 ARG ARG B . n 
B 1 138 LYS 138 130 138 LYS LYS B . n 
B 1 139 SER 139 131 139 SER SER B . n 
B 1 140 MET 140 132 140 MET MET B . n 
B 1 141 TYR 141 133 141 TYR TYR B . n 
B 1 142 GLY 142 134 142 GLY GLY B . n 
B 1 143 LEU 143 135 143 LEU LEU B . n 
B 1 144 TYR 144 136 144 TYR TYR B . n 
B 1 145 ARG 145 137 145 ARG ARG B . n 
B 1 146 ASN 146 138 146 ASN ASN B . n 
B 1 147 PRO 147 139 147 PRO PRO B . n 
B 1 148 TYR 148 140 148 TYR TYR B . n 
B 1 149 THR 149 141 149 THR THR B . n 
B 1 150 HIS 150 142 150 HIS HIS B . n 
B 1 151 HIS 151 143 151 HIS HIS B . n 
B 1 152 PRO 152 144 152 PRO PRO B . n 
B 1 153 CYS 153 145 153 CYS CYS B . n 
B 1 154 VAL 154 146 154 VAL VAL B . n 
B 1 155 ARG 155 147 155 ARG ARG B . n 
B 1 156 GLN 156 148 156 GLN GLN B . n 
B 1 157 THR 157 149 157 THR THR B . n 
B 1 158 VAL 158 150 158 VAL VAL B . n 
B 1 159 GLU 159 151 159 GLU GLU B . n 
B 1 160 SER 160 152 160 SER SER B . n 
B 1 161 THR 161 153 161 THR THR B . n 
B 1 162 ALA 162 154 162 ALA ALA B . n 
B 1 163 ASN 163 155 163 ASN ASN B . n 
B 1 164 THR 164 156 164 THR THR B . n 
B 1 165 ASN 165 157 165 ASN ASN B . n 
B 1 166 VAL 166 158 166 VAL VAL B . n 
B 1 167 VAL 167 159 167 VAL VAL B . n 
B 1 168 MET 168 160 168 MET MET B . n 
B 1 169 HIS 169 161 169 HIS HIS B . n 
B 1 170 ALA 170 162 170 ALA ALA B . n 
B 1 171 GLY 171 163 171 GLY GLY B . n 
B 1 172 ARG 172 164 172 ARG ARG B . n 
B 1 173 PHE 173 165 173 PHE PHE B . n 
B 1 174 LEU 174 166 174 LEU LEU B . n 
B 1 175 ALA 175 167 175 ALA ALA B . n 
B 1 176 MET 176 168 176 MET MET B . n 
B 1 177 LYS 177 169 177 LYS LYS B . n 
B 1 178 GLU 178 170 178 GLU GLU B . n 
B 1 179 ASN 179 171 179 ASN ASN B . n 
B 1 180 GLY 180 172 180 GLY GLY B . n 
B 1 181 ASN 181 173 181 ASN ASN B . n 
B 1 182 ALA 182 174 182 ALA ALA B . n 
B 1 183 TYR 183 175 183 TYR TYR B . n 
B 1 184 GLU 184 176 184 GLU GLU B . n 
B 1 185 MET 185 177 185 MET MET B . n 
B 1 186 ASP 186 178 186 ASP ASP B . n 
B 1 187 PRO 187 179 187 PRO PRO B . n 
B 1 188 HIS 188 180 188 HIS HIS B . n 
B 1 189 THR 189 181 189 THR THR B . n 
B 1 190 LEU 190 182 190 LEU LEU B . n 
B 1 191 LYS 191 183 191 LYS LYS B . n 
B 1 192 THR 192 184 192 THR THR B . n 
B 1 193 LEU 193 185 193 LEU LEU B . n 
B 1 194 GLY 194 186 194 GLY GLY B . n 
B 1 195 TYR 195 187 195 TYR TYR B . n 
B 1 196 ASN 196 188 196 ASN ASN B . n 
B 1 197 PRO 197 189 197 PRO PRO B . n 
B 1 198 PHE 198 190 198 PHE PHE B . n 
B 1 199 ASN 199 191 199 ASN ASN B . n 
B 1 200 LEU 200 192 200 LEU LEU B . n 
B 1 201 PRO 201 193 201 PRO PRO B . n 
B 1 202 SER 202 194 202 SER SER B . n 
B 1 203 LYS 203 195 203 LYS LYS B . n 
B 1 204 THR 204 196 204 THR THR B . n 
B 1 205 MET 205 197 205 MET MET B . n 
B 1 206 THR 206 198 206 THR THR B . n 
B 1 207 ALA 207 199 207 ALA ALA B . n 
B 1 208 HIS 208 200 208 HIS HIS B . n 
B 1 209 PRO 209 201 209 PRO PRO B . n 
B 1 210 LYS 210 202 210 LYS LYS B . n 
B 1 211 GLN 211 203 211 GLN GLN B . n 
B 1 212 CYS 212 204 212 CYS CYS B . n 
B 1 213 SER 213 205 213 SER SER B . n 
B 1 214 VAL 214 206 214 VAL VAL B . n 
B 1 215 THR 215 207 215 THR THR B . n 
B 1 216 GLY 216 208 216 GLY GLY B . n 
B 1 217 ASN 217 209 217 ASN ASN B . n 
B 1 218 LEU 218 210 218 LEU LEU B . n 
B 1 219 VAL 219 211 219 VAL VAL B . n 
B 1 220 GLY 220 212 220 GLY GLY B . n 
B 1 221 PHE 221 213 221 PHE PHE B . n 
B 1 222 GLY 222 214 222 GLY GLY B . n 
B 1 223 TYR 223 215 223 TYR TYR B . n 
B 1 224 GLU 224 216 224 GLU GLU B . n 
B 1 225 ALA 225 217 225 ALA ALA B . n 
B 1 226 LYS 226 218 226 LYS LYS B . n 
B 1 227 GLY 227 219 227 GLY GLY B . n 
B 1 228 LEU 228 220 228 LEU LEU B . n 
B 1 229 ALA 229 221 229 ALA ALA B . n 
B 1 230 THR 230 222 230 THR THR B . n 
B 1 231 LYS 231 223 231 LYS LYS B . n 
B 1 232 ASP 232 224 232 ASP ASP B . n 
B 1 233 VAL 233 225 233 VAL VAL B . n 
B 1 234 TYR 234 226 234 TYR TYR B . n 
B 1 235 TYR 235 227 235 TYR TYR B . n 
B 1 236 PHE 236 228 236 PHE PHE B . n 
B 1 237 GLU 237 229 237 GLU GLU B . n 
B 1 238 VAL 238 230 238 VAL VAL B . n 
B 1 239 ASP 239 231 239 ASP ASP B . n 
B 1 240 PRO 240 232 240 PRO PRO B . n 
B 1 241 SER 241 233 241 SER SER B . n 
B 1 242 GLY 242 234 242 GLY GLY B . n 
B 1 243 LYS 243 235 243 LYS LYS B . n 
B 1 244 VAL 244 236 244 VAL VAL B . n 
B 1 245 VAL 245 237 245 VAL VAL B . n 
B 1 246 ARG 246 238 246 ARG ARG B . n 
B 1 247 ASP 247 239 247 ASP ASP B . n 
B 1 248 LEU 248 240 248 LEU LEU B . n 
B 1 249 TRP 249 241 249 TRP TRP B . n 
B 1 250 LEU 250 242 250 LEU LEU B . n 
B 1 251 GLU 251 243 251 GLU GLU B . n 
B 1 252 ALA 252 244 252 ALA ALA B . n 
B 1 253 PRO 253 245 253 PRO PRO B . n 
B 1 254 TRP 254 246 254 TRP TRP B . n 
B 1 255 CYS 255 247 255 CYS CYS B . n 
B 1 256 ALA 256 248 256 ALA ALA B . n 
B 1 257 PHE 257 249 257 PHE PHE B . n 
B 1 258 ILE 258 250 258 ILE ILE B . n 
B 1 259 HIS 259 251 259 HIS HIS B . n 
B 1 260 ASP 260 252 260 ASP ASP B . n 
B 1 261 CYS 261 253 261 CYS CYS B . n 
B 1 262 ALA 262 254 262 ALA ALA B . n 
B 1 263 LEU 263 255 263 LEU LEU B . n 
B 1 264 THR 264 256 264 THR THR B . n 
B 1 265 PRO 265 257 265 PRO PRO B . n 
B 1 266 ASN 266 258 266 ASN ASN B . n 
B 1 267 TYR 267 259 267 TYR TYR B . n 
B 1 268 LEU 268 260 268 LEU LEU B . n 
B 1 269 VAL 269 261 269 VAL VAL B . n 
B 1 270 LEU 270 262 270 LEU LEU B . n 
B 1 271 MET 271 263 271 MET MET B . n 
B 1 272 LEU 272 264 272 LEU LEU B . n 
B 1 273 TRP 273 265 273 TRP TRP B . n 
B 1 274 PRO 274 266 274 PRO PRO B . n 
B 1 275 PHE 275 267 275 PHE PHE B . n 
B 1 276 GLU 276 268 276 GLU GLU B . n 
B 1 277 ALA 277 269 277 ALA ALA B . n 
B 1 278 ASN 278 270 278 ASN ASN B . n 
B 1 279 LEU 279 271 279 LEU LEU B . n 
B 1 280 GLU 280 272 280 GLU GLU B . n 
B 1 281 ARG 281 273 281 ARG ARG B . n 
B 1 282 MET 282 274 282 MET MET B . n 
B 1 283 LYS 283 275 283 LYS LYS B . n 
B 1 284 ALA 284 276 284 ALA ALA B . n 
B 1 285 GLY 285 277 285 GLY GLY B . n 
B 1 286 GLY 286 278 286 GLY GLY B . n 
B 1 287 HIS 287 279 287 HIS HIS B . n 
B 1 288 HIS 288 280 288 HIS HIS B . n 
B 1 289 TRP 289 281 289 TRP TRP B . n 
B 1 290 ALA 290 282 290 ALA ALA B . n 
B 1 291 TYR 291 283 291 TYR TYR B . n 
B 1 292 ASP 292 284 292 ASP ASP B . n 
B 1 293 TYR 293 285 293 TYR TYR B . n 
B 1 294 THR 294 286 294 THR THR B . n 
B 1 295 LYS 295 287 295 LYS LYS B . n 
B 1 296 PRO 296 288 296 PRO PRO B . n 
B 1 297 ILE 297 289 297 ILE ILE B . n 
B 1 298 THR 298 290 298 THR THR B . n 
B 1 299 TRP 299 291 299 TRP TRP B . n 
B 1 300 ILE 300 292 300 ILE ILE B . n 
B 1 301 THR 301 293 301 THR THR B . n 
B 1 302 ILE 302 294 302 ILE ILE B . n 
B 1 303 PRO 303 295 303 PRO PRO B . n 
B 1 304 ARG 304 296 304 ARG ARG B . n 
B 1 305 GLY 305 297 305 GLY GLY B . n 
B 1 306 ALA 306 298 306 ALA ALA B . n 
B 1 307 LYS 307 299 307 LYS LYS B . n 
B 1 308 SER 308 300 308 SER SER B . n 
B 1 309 LYS 309 301 309 LYS LYS B . n 
B 1 310 ASP 310 302 310 ASP ASP B . n 
B 1 311 GLU 311 303 311 GLU GLU B . n 
B 1 312 VAL 312 304 312 VAL VAL B . n 
B 1 313 LYS 313 305 313 LYS LYS B . n 
B 1 314 TYR 314 306 314 TYR TYR B . n 
B 1 315 TRP 315 307 315 TRP TRP B . n 
B 1 316 HIS 316 308 316 HIS HIS B . n 
B 1 317 TRP 317 309 317 TRP TRP B . n 
B 1 318 LYS 318 310 318 LYS LYS B . n 
B 1 319 ASN 319 311 319 ASN ASN B . n 
B 1 320 GLY 320 312 320 GLY GLY B . n 
B 1 321 MET 321 313 321 MET MET B . n 
B 1 322 PRO 322 314 322 PRO PRO B . n 
B 1 323 ILE 323 315 323 ILE ILE B . n 
B 1 324 HIS 324 316 324 HIS HIS B . n 
B 1 325 THR 325 317 325 THR THR B . n 
B 1 326 ALA 326 318 326 ALA ALA B . n 
B 1 327 SER 327 319 327 SER SER B . n 
B 1 328 GLY 328 320 328 GLY GLY B . n 
B 1 329 PHE 329 321 329 PHE PHE B . n 
B 1 330 GLU 330 322 330 GLU GLU B . n 
B 1 331 ASP 331 323 331 ASP ASP B . n 
B 1 332 GLU 332 324 332 GLU GLU B . n 
B 1 333 GLN 333 325 333 GLN GLN B . n 
B 1 334 GLY 334 326 334 GLY GLY B . n 
B 1 335 ARG 335 327 335 ARG ARG B . n 
B 1 336 ILE 336 328 336 ILE ILE B . n 
B 1 337 ILE 337 329 337 ILE ILE B . n 
B 1 338 ILE 338 330 338 ILE ILE B . n 
B 1 339 ASP 339 331 339 ASP ASP B . n 
B 1 340 SER 340 332 340 SER SER B . n 
B 1 341 SER 341 333 341 SER SER B . n 
B 1 342 LEU 342 334 342 LEU LEU B . n 
B 1 343 VAL 343 335 343 VAL VAL B . n 
B 1 344 HIS 344 336 344 HIS HIS B . n 
B 1 345 GLY 345 337 345 GLY GLY B . n 
B 1 346 ASN 346 338 346 ASN ASN B . n 
B 1 347 ALA 347 339 347 ALA ALA B . n 
B 1 348 PHE 348 340 348 PHE PHE B . n 
B 1 349 PRO 349 341 349 PRO PRO B . n 
B 1 350 PHE 350 342 350 PHE PHE B . n 
B 1 351 PHE 351 343 351 PHE PHE B . n 
B 1 352 PRO 352 344 352 PRO PRO B . n 
B 1 353 PRO 353 345 353 PRO PRO B . n 
B 1 354 ASP 354 346 354 ASP ASP B . n 
B 1 355 SER 355 347 355 SER SER B . n 
B 1 356 ASP 356 348 356 ASP ASP B . n 
B 1 357 GLU 357 349 357 GLU GLU B . n 
B 1 358 GLN 358 350 358 GLN GLN B . n 
B 1 359 LYS 359 351 359 LYS LYS B . n 
B 1 360 LYS 360 352 360 LYS LYS B . n 
B 1 361 LYS 361 353 361 LYS LYS B . n 
B 1 362 GLN 362 354 362 GLN GLN B . n 
B 1 363 GLU 363 355 363 GLU GLU B . n 
B 1 364 ALA 364 356 364 ALA ALA B . n 
B 1 365 ASP 365 357 365 ASP ASP B . n 
B 1 366 GLY 366 358 366 GLY GLY B . n 
B 1 367 THR 367 359 367 THR THR B . n 
B 1 368 PRO 368 360 368 PRO PRO B . n 
B 1 369 LYS 369 361 369 LYS LYS B . n 
B 1 370 ALA 370 362 370 ALA ALA B . n 
B 1 371 GLN 371 363 371 GLN GLN B . n 
B 1 372 PHE 372 364 372 PHE PHE B . n 
B 1 373 VAL 373 365 373 VAL VAL B . n 
B 1 374 ARG 374 366 374 ARG ARG B . n 
B 1 375 TRP 375 367 375 TRP TRP B . n 
B 1 376 THR 376 368 376 THR THR B . n 
B 1 377 ILE 377 369 377 ILE ILE B . n 
B 1 378 ASP 378 370 378 ASP ASP B . n 
B 1 379 PRO 379 371 379 PRO PRO B . n 
B 1 380 ARG 380 372 380 ARG ARG B . n 
B 1 381 LYS 381 373 381 LYS LYS B . n 
B 1 382 ASP 382 374 382 ASP ASP B . n 
B 1 383 ASN 383 375 383 ASN ASN B . n 
B 1 384 ASN 384 376 384 ASN ASN B . n 
B 1 385 GLU 385 377 385 GLU GLU B . n 
B 1 386 GLN 386 378 386 GLN GLN B . n 
B 1 387 LEU 387 379 387 LEU LEU B . n 
B 1 388 PRO 388 380 388 PRO PRO B . n 
B 1 389 ASP 389 381 389 ASP ASP B . n 
B 1 390 PRO 390 382 390 PRO PRO B . n 
B 1 391 GLU 391 383 391 GLU GLU B . n 
B 1 392 VAL 392 384 392 VAL VAL B . n 
B 1 393 ILE 393 385 393 ILE ILE B . n 
B 1 394 LEU 394 386 394 LEU LEU B . n 
B 1 395 ASP 395 387 395 ASP ASP B . n 
B 1 396 THR 396 388 396 THR THR B . n 
B 1 397 PRO 397 389 397 PRO PRO B . n 
B 1 398 SER 398 390 398 SER SER B . n 
B 1 399 GLU 399 391 399 GLU GLU B . n 
B 1 400 PHE 400 392 400 PHE PHE B . n 
B 1 401 PRO 401 393 401 PRO PRO B . n 
B 1 402 GLN 402 394 402 GLN GLN B . n 
B 1 403 ILE 403 395 403 ILE ILE B . n 
B 1 404 ASP 404 396 404 ASP ASP B . n 
B 1 405 ASN 405 397 405 ASN ASN B . n 
B 1 406 ARG 406 398 406 ARG ARG B . n 
B 1 407 PHE 407 399 407 PHE PHE B . n 
B 1 408 MET 408 400 408 MET MET B . n 
B 1 409 GLY 409 401 409 GLY GLY B . n 
B 1 410 VAL 410 402 410 VAL VAL B . n 
B 1 411 GLU 411 403 411 GLU GLU B . n 
B 1 412 TYR 412 404 412 TYR TYR B . n 
B 1 413 SER 413 405 413 SER SER B . n 
B 1 414 SER 414 406 414 SER SER B . n 
B 1 415 ALA 415 407 415 ALA ALA B . n 
B 1 416 PHE 416 408 416 PHE PHE B . n 
B 1 417 ILE 417 409 417 ILE ILE B . n 
B 1 418 ASN 418 410 418 ASN ASN B . n 
B 1 419 VAL 419 411 419 VAL VAL B . n 
B 1 420 PHE 420 412 420 PHE PHE B . n 
B 1 421 VAL 421 413 421 VAL VAL B . n 
B 1 422 PRO 422 414 422 PRO PRO B . n 
B 1 423 ASP 423 415 423 ASP ASP B . n 
B 1 424 ARG 424 416 424 ARG ARG B . n 
B 1 425 SER 425 417 425 SER SER B . n 
B 1 426 ASP 426 418 426 ASP ASP B . n 
B 1 427 GLY 427 419 427 GLY GLY B . n 
B 1 428 ASN 428 420 428 ASN ASN B . n 
B 1 429 LYS 429 421 429 LYS LYS B . n 
B 1 430 ASN 430 422 430 ASN ASN B . n 
B 1 431 VAL 431 423 431 VAL VAL B . n 
B 1 432 PHE 432 424 432 PHE PHE B . n 
B 1 433 GLN 433 425 433 GLN GLN B . n 
B 1 434 GLY 434 426 434 GLY GLY B . n 
B 1 435 LEU 435 427 435 LEU LEU B . n 
B 1 436 ASN 436 428 436 ASN ASN B . n 
B 1 437 GLY 437 429 437 GLY GLY B . n 
B 1 438 LEU 438 430 438 LEU LEU B . n 
B 1 439 ALA 439 431 439 ALA ALA B . n 
B 1 440 HIS 440 432 440 HIS HIS B . n 
B 1 441 TYR 441 433 441 TYR TYR B . n 
B 1 442 LYS 442 434 442 LYS LYS B . n 
B 1 443 ARG 443 435 443 ARG ARG B . n 
B 1 444 LYS 444 436 444 LYS LYS B . n 
B 1 445 GLU 445 437 445 GLU GLU B . n 
B 1 446 GLY 446 438 446 GLY GLY B . n 
B 1 447 THR 447 439 447 THR THR B . n 
B 1 448 THR 448 440 448 THR THR B . n 
B 1 449 GLU 449 441 449 GLU GLU B . n 
B 1 450 TRP 450 442 450 TRP TRP B . n 
B 1 451 TYR 451 443 451 TYR TYR B . n 
B 1 452 TYR 452 444 452 TYR TYR B . n 
B 1 453 ALA 453 445 453 ALA ALA B . n 
B 1 454 GLY 454 446 454 GLY GLY B . n 
B 1 455 ASP 455 447 455 ASP ASP B . n 
B 1 456 ASN 456 448 456 ASN ASN B . n 
B 1 457 CYS 457 449 457 CYS CYS B . n 
B 1 458 LEU 458 450 458 LEU LEU B . n 
B 1 459 ILE 459 451 459 ILE ILE B . n 
B 1 460 GLN 460 452 460 GLN GLN B . n 
B 1 461 GLU 461 453 461 GLU GLU B . n 
B 1 462 PRO 462 454 462 PRO PRO B . n 
B 1 463 VAL 463 455 463 VAL VAL B . n 
B 1 464 PHE 464 456 464 PHE PHE B . n 
B 1 465 SER 465 457 465 SER SER B . n 
B 1 466 PRO 466 458 466 PRO PRO B . n 
B 1 467 ARG 467 459 467 ARG ARG B . n 
B 1 468 SER 468 460 468 SER SER B . n 
B 1 469 LYS 469 461 469 LYS LYS B . n 
B 1 470 ASP 470 462 470 ASP ASP B . n 
B 1 471 ALA 471 463 471 ALA ALA B . n 
B 1 472 PRO 472 464 472 PRO PRO B . n 
B 1 473 GLU 473 465 473 GLU GLU B . n 
B 1 474 GLY 474 466 474 GLY GLY B . n 
B 1 475 ASP 475 467 475 ASP ASP B . n 
B 1 476 GLY 476 468 476 GLY GLY B . n 
B 1 477 PHE 477 469 477 PHE PHE B . n 
B 1 478 VAL 478 470 478 VAL VAL B . n 
B 1 479 LEU 479 471 479 LEU LEU B . n 
B 1 480 ALA 480 472 480 ALA ALA B . n 
B 1 481 ILE 481 473 481 ILE ILE B . n 
B 1 482 VAL 482 474 482 VAL VAL B . n 
B 1 483 ASP 483 475 483 ASP ASP B . n 
B 1 484 ARG 484 476 484 ARG ARG B . n 
B 1 485 LEU 485 477 485 LEU LEU B . n 
B 1 486 ASP 486 478 486 ASP ASP B . n 
B 1 487 LEU 487 479 487 LEU LEU B . n 
B 1 488 ASN 488 480 488 ASN ASN B . n 
B 1 489 ARG 489 481 489 ARG ARG B . n 
B 1 490 SER 490 482 490 SER SER B . n 
B 1 491 GLU 491 483 491 GLU GLU B . n 
B 1 492 VAL 492 484 492 VAL VAL B . n 
B 1 493 VAL 493 485 493 VAL VAL B . n 
B 1 494 VAL 494 486 494 VAL VAL B . n 
B 1 495 ILE 495 487 495 ILE ILE B . n 
B 1 496 ASP 496 488 496 ASP ASP B . n 
B 1 497 THR 497 489 497 THR THR B . n 
B 1 498 ARG 498 490 498 ARG ARG B . n 
B 1 499 ASP 499 491 499 ASP ASP B . n 
B 1 500 PHE 500 492 500 PHE PHE B . n 
B 1 501 THR 501 493 501 THR THR B . n 
B 1 502 LYS 502 494 502 LYS LYS B . n 
B 1 503 ALA 503 495 503 ALA ALA B . n 
B 1 504 VAL 504 496 504 VAL VAL B . n 
B 1 505 ALA 505 497 505 ALA ALA B . n 
B 1 506 ALA 506 498 506 ALA ALA B . n 
B 1 507 VAL 507 499 507 VAL VAL B . n 
B 1 508 GLN 508 500 508 GLN GLN B . n 
B 1 509 LEU 509 501 509 LEU LEU B . n 
B 1 510 PRO 510 502 510 PRO PRO B . n 
B 1 511 PHE 511 503 511 PHE PHE B . n 
B 1 512 ALA 512 504 512 ALA ALA B . n 
B 1 513 ILE 513 505 513 ILE ILE B . n 
B 1 514 ARG 514 506 514 ARG ARG B . n 
B 1 515 SER 515 507 515 SER SER B . n 
B 1 516 GLY 516 508 516 GLY GLY B . n 
B 1 517 ILE 517 509 517 ILE ILE B . n 
B 1 518 HIS 518 510 518 HIS HIS B . n 
B 1 519 GLY 519 511 519 GLY GLY B . n 
B 1 520 GLN 520 512 520 GLN GLN B . n 
B 1 521 TRP 521 513 521 TRP TRP B . n 
B 1 522 ILE 522 514 522 ILE ILE B . n 
B 1 523 PRO 523 515 523 PRO PRO B . n 
B 1 524 GLY 524 516 524 GLY GLY B . n 
B 1 525 GLU 525 517 525 GLU GLU B . n 
B 1 526 VAL 526 518 526 VAL VAL B . n 
B 1 527 THR 527 519 527 THR THR B . n 
B 1 528 PRO 528 520 528 PRO PRO B . n 
B 1 529 ASP 529 521 529 ASP ASP B . n 
B 1 530 PHE 530 522 530 PHE PHE B . n 
B 1 531 GLU 531 523 531 GLU GLU B . n 
B 1 532 THR 532 524 532 THR THR B . n 
B 1 533 LYS 533 525 533 LYS LYS B . n 
B 1 534 GLY 534 526 534 GLY GLY B . n 
B 1 535 LEU 535 527 535 LEU LEU B . n 
B 1 536 VAL 536 528 536 VAL VAL B . n 
B 1 537 ASP 537 529 537 ASP ASP B . n 
B 1 538 LEU 538 530 538 LEU LEU B . n 
B 1 539 PRO 539 531 539 PRO PRO B . n 
B 1 540 LYS 540 532 540 LYS LYS B . n 
B 1 541 GLU 541 533 541 GLU GLU B . n 
B 1 542 GLU 542 534 542 GLU GLU B . n 
B 1 543 HIS 543 535 543 HIS HIS B . n 
B 1 544 TRP 544 536 544 TRP TRP B . n 
B 1 545 ALA 545 537 545 ALA ALA B . n 
B 1 546 PRO 546 538 546 PRO PRO B . n 
B 1 547 LEU 547 539 547 LEU LEU B . n 
B 1 548 SER 548 540 548 SER SER B . n 
B 1 549 GLN 549 541 549 GLN GLN B . n 
B 1 550 SER 550 542 550 SER SER B . n 
B 1 551 PRO 551 543 551 PRO PRO B . n 
B 1 552 TYR 552 544 552 TYR TYR B . n 
B 1 553 ASP 553 545 553 ASP ASP B . n 
B 1 554 PRO 554 546 554 PRO PRO B . n 
B 1 555 ASP 555 547 555 ASP ASP B . n 
B 1 556 ALA 556 548 556 ALA ALA B . 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 FE2 ? ? FE2 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 HBA ? ? HBA ? ? '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 
C 2 HBA 1   601  601 HBA HBA A . 
D 3 FE2 1   602  1   FE2 FE  A . 
E 2 HBA 1   601  601 HBA HBA B . 
F 3 FE2 1   602  2   FE2 FE  B . 
G 4 HOH 1   701  554 HOH HOH A . 
G 4 HOH 2   702  868 HOH HOH A . 
G 4 HOH 3   703  316 HOH HOH A . 
G 4 HOH 4   704  387 HOH HOH A . 
G 4 HOH 5   705  728 HOH HOH A . 
G 4 HOH 6   706  155 HOH HOH A . 
G 4 HOH 7   707  361 HOH HOH A . 
G 4 HOH 8   708  545 HOH HOH A . 
G 4 HOH 9   709  359 HOH HOH A . 
G 4 HOH 10  710  466 HOH HOH A . 
G 4 HOH 11  711  843 HOH HOH A . 
G 4 HOH 12  712  719 HOH HOH A . 
G 4 HOH 13  713  605 HOH HOH A . 
G 4 HOH 14  714  665 HOH HOH A . 
G 4 HOH 15  715  121 HOH HOH A . 
G 4 HOH 16  716  323 HOH HOH A . 
G 4 HOH 17  717  470 HOH HOH A . 
G 4 HOH 18  718  706 HOH HOH A . 
G 4 HOH 19  719  755 HOH HOH A . 
G 4 HOH 20  720  122 HOH HOH A . 
G 4 HOH 21  721  669 HOH HOH A . 
G 4 HOH 22  722  319 HOH HOH A . 
G 4 HOH 23  723  425 HOH HOH A . 
G 4 HOH 24  724  519 HOH HOH A . 
G 4 HOH 25  725  651 HOH HOH A . 
G 4 HOH 26  726  115 HOH HOH A . 
G 4 HOH 27  727  86  HOH HOH A . 
G 4 HOH 28  728  368 HOH HOH A . 
G 4 HOH 29  729  97  HOH HOH A . 
G 4 HOH 30  730  382 HOH HOH A . 
G 4 HOH 31  731  881 HOH HOH A . 
G 4 HOH 32  732  475 HOH HOH A . 
G 4 HOH 33  733  449 HOH HOH A . 
G 4 HOH 34  734  501 HOH HOH A . 
G 4 HOH 35  735  192 HOH HOH A . 
G 4 HOH 36  736  579 HOH HOH A . 
G 4 HOH 37  737  34  HOH HOH A . 
G 4 HOH 38  738  109 HOH HOH A . 
G 4 HOH 39  739  71  HOH HOH A . 
G 4 HOH 40  740  184 HOH HOH A . 
G 4 HOH 41  741  185 HOH HOH A . 
G 4 HOH 42  742  547 HOH HOH A . 
G 4 HOH 43  743  374 HOH HOH A . 
G 4 HOH 44  744  101 HOH HOH A . 
G 4 HOH 45  745  701 HOH HOH A . 
G 4 HOH 46  746  4   HOH HOH A . 
G 4 HOH 47  747  504 HOH HOH A . 
G 4 HOH 48  748  753 HOH HOH A . 
G 4 HOH 49  749  78  HOH HOH A . 
G 4 HOH 50  750  329 HOH HOH A . 
G 4 HOH 51  751  692 HOH HOH A . 
G 4 HOH 52  752  443 HOH HOH A . 
G 4 HOH 53  753  626 HOH HOH A . 
G 4 HOH 54  754  662 HOH HOH A . 
G 4 HOH 55  755  255 HOH HOH A . 
G 4 HOH 56  756  583 HOH HOH A . 
G 4 HOH 57  757  24  HOH HOH A . 
G 4 HOH 58  758  856 HOH HOH A . 
G 4 HOH 59  759  44  HOH HOH A . 
G 4 HOH 60  760  190 HOH HOH A . 
G 4 HOH 61  761  844 HOH HOH A . 
G 4 HOH 62  762  7   HOH HOH A . 
G 4 HOH 63  763  233 HOH HOH A . 
G 4 HOH 64  764  214 HOH HOH A . 
G 4 HOH 65  765  857 HOH HOH A . 
G 4 HOH 66  766  231 HOH HOH A . 
G 4 HOH 67  767  879 HOH HOH A . 
G 4 HOH 68  768  271 HOH HOH A . 
G 4 HOH 69  769  328 HOH HOH A . 
G 4 HOH 70  770  575 HOH HOH A . 
G 4 HOH 71  771  601 HOH HOH A . 
G 4 HOH 72  772  865 HOH HOH A . 
G 4 HOH 73  773  351 HOH HOH A . 
G 4 HOH 74  774  63  HOH HOH A . 
G 4 HOH 75  775  205 HOH HOH A . 
G 4 HOH 76  776  50  HOH HOH A . 
G 4 HOH 77  777  791 HOH HOH A . 
G 4 HOH 78  778  580 HOH HOH A . 
G 4 HOH 79  779  200 HOH HOH A . 
G 4 HOH 80  780  600 HOH HOH A . 
G 4 HOH 81  781  595 HOH HOH A . 
G 4 HOH 82  782  509 HOH HOH A . 
G 4 HOH 83  783  282 HOH HOH A . 
G 4 HOH 84  784  325 HOH HOH A . 
G 4 HOH 85  785  111 HOH HOH A . 
G 4 HOH 86  786  754 HOH HOH A . 
G 4 HOH 87  787  735 HOH HOH A . 
G 4 HOH 88  788  468 HOH HOH A . 
G 4 HOH 89  789  256 HOH HOH A . 
G 4 HOH 90  790  652 HOH HOH A . 
G 4 HOH 91  791  522 HOH HOH A . 
G 4 HOH 92  792  863 HOH HOH A . 
G 4 HOH 93  793  145 HOH HOH A . 
G 4 HOH 94  794  76  HOH HOH A . 
G 4 HOH 95  795  5   HOH HOH A . 
G 4 HOH 96  796  352 HOH HOH A . 
G 4 HOH 97  797  716 HOH HOH A . 
G 4 HOH 98  798  500 HOH HOH A . 
G 4 HOH 99  799  84  HOH HOH A . 
G 4 HOH 100 800  452 HOH HOH A . 
G 4 HOH 101 801  92  HOH HOH A . 
G 4 HOH 102 802  479 HOH HOH A . 
G 4 HOH 103 803  161 HOH HOH A . 
G 4 HOH 104 804  159 HOH HOH A . 
G 4 HOH 105 805  874 HOH HOH A . 
G 4 HOH 106 806  61  HOH HOH A . 
G 4 HOH 107 807  195 HOH HOH A . 
G 4 HOH 108 808  848 HOH HOH A . 
G 4 HOH 109 809  321 HOH HOH A . 
G 4 HOH 110 810  578 HOH HOH A . 
G 4 HOH 111 811  656 HOH HOH A . 
G 4 HOH 112 812  284 HOH HOH A . 
G 4 HOH 113 813  114 HOH HOH A . 
G 4 HOH 114 814  188 HOH HOH A . 
G 4 HOH 115 815  246 HOH HOH A . 
G 4 HOH 116 816  552 HOH HOH A . 
G 4 HOH 117 817  849 HOH HOH A . 
G 4 HOH 118 818  131 HOH HOH A . 
G 4 HOH 119 819  532 HOH HOH A . 
G 4 HOH 120 820  176 HOH HOH A . 
G 4 HOH 121 821  99  HOH HOH A . 
G 4 HOH 122 822  37  HOH HOH A . 
G 4 HOH 123 823  663 HOH HOH A . 
G 4 HOH 124 824  104 HOH HOH A . 
G 4 HOH 125 825  607 HOH HOH A . 
G 4 HOH 126 826  136 HOH HOH A . 
G 4 HOH 127 827  717 HOH HOH A . 
G 4 HOH 128 828  65  HOH HOH A . 
G 4 HOH 129 829  356 HOH HOH A . 
G 4 HOH 130 830  521 HOH HOH A . 
G 4 HOH 131 831  861 HOH HOH A . 
G 4 HOH 132 832  577 HOH HOH A . 
G 4 HOH 133 833  513 HOH HOH A . 
G 4 HOH 134 834  19  HOH HOH A . 
G 4 HOH 135 835  15  HOH HOH A . 
G 4 HOH 136 836  678 HOH HOH A . 
G 4 HOH 137 837  333 HOH HOH A . 
G 4 HOH 138 838  48  HOH HOH A . 
G 4 HOH 139 839  411 HOH HOH A . 
G 4 HOH 140 840  196 HOH HOH A . 
G 4 HOH 141 841  657 HOH HOH A . 
G 4 HOH 142 842  193 HOH HOH A . 
G 4 HOH 143 843  724 HOH HOH A . 
G 4 HOH 144 844  732 HOH HOH A . 
G 4 HOH 145 845  549 HOH HOH A . 
G 4 HOH 146 846  332 HOH HOH A . 
G 4 HOH 147 847  372 HOH HOH A . 
G 4 HOH 148 848  572 HOH HOH A . 
G 4 HOH 149 849  459 HOH HOH A . 
G 4 HOH 150 850  295 HOH HOH A . 
G 4 HOH 151 851  90  HOH HOH A . 
G 4 HOH 152 852  113 HOH HOH A . 
G 4 HOH 153 853  643 HOH HOH A . 
G 4 HOH 154 854  672 HOH HOH A . 
G 4 HOH 155 855  749 HOH HOH A . 
G 4 HOH 156 856  406 HOH HOH A . 
G 4 HOH 157 857  2   HOH HOH A . 
G 4 HOH 158 858  146 HOH HOH A . 
G 4 HOH 159 859  313 HOH HOH A . 
G 4 HOH 160 860  103 HOH HOH A . 
G 4 HOH 161 861  750 HOH HOH A . 
G 4 HOH 162 862  377 HOH HOH A . 
G 4 HOH 163 863  91  HOH HOH A . 
G 4 HOH 164 864  166 HOH HOH A . 
G 4 HOH 165 865  664 HOH HOH A . 
G 4 HOH 166 866  128 HOH HOH A . 
G 4 HOH 167 867  31  HOH HOH A . 
G 4 HOH 168 868  287 HOH HOH A . 
G 4 HOH 169 869  565 HOH HOH A . 
G 4 HOH 170 870  302 HOH HOH A . 
G 4 HOH 171 871  33  HOH HOH A . 
G 4 HOH 172 872  507 HOH HOH A . 
G 4 HOH 173 873  88  HOH HOH A . 
G 4 HOH 174 874  134 HOH HOH A . 
G 4 HOH 175 875  335 HOH HOH A . 
G 4 HOH 176 876  561 HOH HOH A . 
G 4 HOH 177 877  198 HOH HOH A . 
G 4 HOH 178 878  317 HOH HOH A . 
G 4 HOH 179 879  186 HOH HOH A . 
G 4 HOH 180 880  100 HOH HOH A . 
G 4 HOH 181 881  264 HOH HOH A . 
G 4 HOH 182 882  267 HOH HOH A . 
G 4 HOH 183 883  339 HOH HOH A . 
G 4 HOH 184 884  516 HOH HOH A . 
G 4 HOH 185 885  157 HOH HOH A . 
G 4 HOH 186 886  852 HOH HOH A . 
G 4 HOH 187 887  62  HOH HOH A . 
G 4 HOH 188 888  124 HOH HOH A . 
G 4 HOH 189 889  25  HOH HOH A . 
G 4 HOH 190 890  376 HOH HOH A . 
G 4 HOH 191 891  70  HOH HOH A . 
G 4 HOH 192 892  303 HOH HOH A . 
G 4 HOH 193 893  226 HOH HOH A . 
G 4 HOH 194 894  349 HOH HOH A . 
G 4 HOH 195 895  385 HOH HOH A . 
G 4 HOH 196 896  635 HOH HOH A . 
G 4 HOH 197 897  236 HOH HOH A . 
G 4 HOH 198 898  149 HOH HOH A . 
G 4 HOH 199 899  439 HOH HOH A . 
G 4 HOH 200 900  222 HOH HOH A . 
G 4 HOH 201 901  199 HOH HOH A . 
G 4 HOH 202 902  119 HOH HOH A . 
G 4 HOH 203 903  448 HOH HOH A . 
G 4 HOH 204 904  371 HOH HOH A . 
G 4 HOH 205 905  525 HOH HOH A . 
G 4 HOH 206 906  191 HOH HOH A . 
G 4 HOH 207 907  461 HOH HOH A . 
G 4 HOH 208 908  123 HOH HOH A . 
G 4 HOH 209 909  555 HOH HOH A . 
G 4 HOH 210 910  252 HOH HOH A . 
G 4 HOH 211 911  683 HOH HOH A . 
G 4 HOH 212 912  395 HOH HOH A . 
G 4 HOH 213 913  386 HOH HOH A . 
G 4 HOH 214 914  628 HOH HOH A . 
G 4 HOH 215 915  310 HOH HOH A . 
G 4 HOH 216 916  847 HOH HOH A . 
G 4 HOH 217 917  53  HOH HOH A . 
G 4 HOH 218 918  160 HOH HOH A . 
G 4 HOH 219 919  760 HOH HOH A . 
G 4 HOH 220 920  211 HOH HOH A . 
G 4 HOH 221 921  126 HOH HOH A . 
G 4 HOH 222 922  878 HOH HOH A . 
G 4 HOH 223 923  362 HOH HOH A . 
G 4 HOH 224 924  477 HOH HOH A . 
G 4 HOH 225 925  253 HOH HOH A . 
G 4 HOH 226 926  392 HOH HOH A . 
G 4 HOH 227 927  156 HOH HOH A . 
G 4 HOH 228 928  370 HOH HOH A . 
G 4 HOH 229 929  85  HOH HOH A . 
G 4 HOH 230 930  390 HOH HOH A . 
G 4 HOH 231 931  434 HOH HOH A . 
G 4 HOH 232 932  862 HOH HOH A . 
G 4 HOH 233 933  125 HOH HOH A . 
G 4 HOH 234 934  324 HOH HOH A . 
G 4 HOH 235 935  93  HOH HOH A . 
G 4 HOH 236 936  877 HOH HOH A . 
G 4 HOH 237 937  59  HOH HOH A . 
G 4 HOH 238 938  245 HOH HOH A . 
G 4 HOH 239 939  873 HOH HOH A . 
G 4 HOH 240 940  454 HOH HOH A . 
G 4 HOH 241 941  334 HOH HOH A . 
G 4 HOH 242 942  617 HOH HOH A . 
G 4 HOH 243 943  394 HOH HOH A . 
G 4 HOH 244 944  429 HOH HOH A . 
G 4 HOH 245 945  440 HOH HOH A . 
G 4 HOH 246 946  503 HOH HOH A . 
G 4 HOH 247 947  308 HOH HOH A . 
G 4 HOH 248 948  751 HOH HOH A . 
G 4 HOH 249 949  72  HOH HOH A . 
G 4 HOH 250 950  257 HOH HOH A . 
G 4 HOH 251 951  206 HOH HOH A . 
G 4 HOH 252 952  853 HOH HOH A . 
G 4 HOH 253 953  383 HOH HOH A . 
G 4 HOH 254 954  433 HOH HOH A . 
G 4 HOH 255 955  785 HOH HOH A . 
G 4 HOH 256 956  711 HOH HOH A . 
G 4 HOH 257 957  396 HOH HOH A . 
G 4 HOH 258 958  841 HOH HOH A . 
G 4 HOH 259 959  55  HOH HOH A . 
G 4 HOH 260 960  181 HOH HOH A . 
G 4 HOH 261 961  623 HOH HOH A . 
G 4 HOH 262 962  402 HOH HOH A . 
G 4 HOH 263 963  163 HOH HOH A . 
G 4 HOH 264 964  306 HOH HOH A . 
G 4 HOH 265 965  413 HOH HOH A . 
G 4 HOH 266 966  837 HOH HOH A . 
G 4 HOH 267 967  851 HOH HOH A . 
G 4 HOH 268 968  506 HOH HOH A . 
G 4 HOH 269 969  36  HOH HOH A . 
G 4 HOH 270 970  147 HOH HOH A . 
G 4 HOH 271 971  430 HOH HOH A . 
G 4 HOH 272 972  647 HOH HOH A . 
G 4 HOH 273 973  499 HOH HOH A . 
G 4 HOH 274 974  322 HOH HOH A . 
G 4 HOH 275 975  51  HOH HOH A . 
G 4 HOH 276 976  289 HOH HOH A . 
G 4 HOH 277 977  67  HOH HOH A . 
G 4 HOH 278 978  634 HOH HOH A . 
G 4 HOH 279 979  864 HOH HOH A . 
G 4 HOH 280 980  301 HOH HOH A . 
G 4 HOH 281 981  594 HOH HOH A . 
G 4 HOH 282 982  14  HOH HOH A . 
G 4 HOH 283 983  489 HOH HOH A . 
G 4 HOH 284 984  450 HOH HOH A . 
G 4 HOH 285 985  381 HOH HOH A . 
G 4 HOH 286 986  693 HOH HOH A . 
G 4 HOH 287 987  280 HOH HOH A . 
G 4 HOH 288 988  153 HOH HOH A . 
G 4 HOH 289 989  158 HOH HOH A . 
G 4 HOH 290 990  140 HOH HOH A . 
G 4 HOH 291 991  536 HOH HOH A . 
G 4 HOH 292 992  95  HOH HOH A . 
G 4 HOH 293 993  867 HOH HOH A . 
G 4 HOH 294 994  292 HOH HOH A . 
G 4 HOH 295 995  699 HOH HOH A . 
G 4 HOH 296 996  631 HOH HOH A . 
G 4 HOH 297 997  859 HOH HOH A . 
G 4 HOH 298 998  12  HOH HOH A . 
G 4 HOH 299 999  816 HOH HOH A . 
G 4 HOH 300 1000 235 HOH HOH A . 
G 4 HOH 301 1001 247 HOH HOH A . 
G 4 HOH 302 1002 281 HOH HOH A . 
G 4 HOH 303 1003 314 HOH HOH A . 
G 4 HOH 304 1004 455 HOH HOH A . 
G 4 HOH 305 1005 173 HOH HOH A . 
G 4 HOH 306 1006 544 HOH HOH A . 
G 4 HOH 307 1007 171 HOH HOH A . 
G 4 HOH 308 1008 451 HOH HOH A . 
G 4 HOH 309 1009 680 HOH HOH A . 
G 4 HOH 310 1010 79  HOH HOH A . 
G 4 HOH 311 1011 331 HOH HOH A . 
G 4 HOH 312 1012 496 HOH HOH A . 
G 4 HOH 313 1013 49  HOH HOH A . 
G 4 HOH 314 1014 642 HOH HOH A . 
G 4 HOH 315 1015 378 HOH HOH A . 
G 4 HOH 316 1016 690 HOH HOH A . 
G 4 HOH 317 1017 815 HOH HOH A . 
G 4 HOH 318 1018 139 HOH HOH A . 
G 4 HOH 319 1019 524 HOH HOH A . 
G 4 HOH 320 1020 46  HOH HOH A . 
G 4 HOH 321 1021 47  HOH HOH A . 
G 4 HOH 322 1022 743 HOH HOH A . 
G 4 HOH 323 1023 725 HOH HOH A . 
G 4 HOH 324 1024 364 HOH HOH A . 
G 4 HOH 325 1025 342 HOH HOH A . 
G 4 HOH 326 1026 127 HOH HOH A . 
G 4 HOH 327 1027 568 HOH HOH A . 
G 4 HOH 328 1028 338 HOH HOH A . 
G 4 HOH 329 1029 210 HOH HOH A . 
G 4 HOH 330 1030 531 HOH HOH A . 
G 4 HOH 331 1031 330 HOH HOH A . 
G 4 HOH 332 1032 762 HOH HOH A . 
G 4 HOH 333 1033 481 HOH HOH A . 
G 4 HOH 334 1034 684 HOH HOH A . 
G 4 HOH 335 1035 596 HOH HOH A . 
G 4 HOH 336 1036 539 HOH HOH A . 
G 4 HOH 337 1037 802 HOH HOH A . 
G 4 HOH 338 1038 148 HOH HOH A . 
G 4 HOH 339 1039 688 HOH HOH A . 
G 4 HOH 340 1040 170 HOH HOH A . 
G 4 HOH 341 1041 715 HOH HOH A . 
G 4 HOH 342 1042 54  HOH HOH A . 
G 4 HOH 343 1043 603 HOH HOH A . 
G 4 HOH 344 1044 614 HOH HOH A . 
G 4 HOH 345 1045 418 HOH HOH A . 
G 4 HOH 346 1046 248 HOH HOH A . 
G 4 HOH 347 1047 826 HOH HOH A . 
G 4 HOH 348 1048 789 HOH HOH A . 
G 4 HOH 349 1049 739 HOH HOH A . 
G 4 HOH 350 1050 673 HOH HOH A . 
G 4 HOH 351 1051 75  HOH HOH A . 
G 4 HOH 352 1052 415 HOH HOH A . 
G 4 HOH 353 1053 654 HOH HOH A . 
G 4 HOH 354 1054 400 HOH HOH A . 
G 4 HOH 355 1055 462 HOH HOH A . 
G 4 HOH 356 1056 403 HOH HOH A . 
G 4 HOH 357 1057 784 HOH HOH A . 
G 4 HOH 358 1058 636 HOH HOH A . 
G 4 HOH 359 1059 830 HOH HOH A . 
G 4 HOH 360 1060 648 HOH HOH A . 
G 4 HOH 361 1061 806 HOH HOH A . 
G 4 HOH 362 1062 819 HOH HOH A . 
G 4 HOH 363 1063 315 HOH HOH A . 
G 4 HOH 364 1064 653 HOH HOH A . 
G 4 HOH 365 1065 763 HOH HOH A . 
G 4 HOH 366 1066 661 HOH HOH A . 
G 4 HOH 367 1067 736 HOH HOH A . 
G 4 HOH 368 1068 597 HOH HOH A . 
G 4 HOH 369 1069 445 HOH HOH A . 
G 4 HOH 370 1070 691 HOH HOH A . 
G 4 HOH 371 1071 241 HOH HOH A . 
G 4 HOH 372 1072 769 HOH HOH A . 
G 4 HOH 373 1073 179 HOH HOH A . 
G 4 HOH 374 1074 677 HOH HOH A . 
G 4 HOH 375 1075 426 HOH HOH A . 
G 4 HOH 376 1076 355 HOH HOH A . 
G 4 HOH 377 1077 488 HOH HOH A . 
G 4 HOH 378 1078 781 HOH HOH A . 
G 4 HOH 379 1079 807 HOH HOH A . 
G 4 HOH 380 1080 495 HOH HOH A . 
G 4 HOH 381 1081 391 HOH HOH A . 
G 4 HOH 382 1082 788 HOH HOH A . 
G 4 HOH 383 1083 746 HOH HOH A . 
G 4 HOH 384 1084 804 HOH HOH A . 
G 4 HOH 385 1085 640 HOH HOH A . 
G 4 HOH 386 1086 838 HOH HOH A . 
G 4 HOH 387 1087 800 HOH HOH A . 
G 4 HOH 388 1088 606 HOH HOH A . 
G 4 HOH 389 1089 510 HOH HOH A . 
G 4 HOH 390 1090 582 HOH HOH A . 
G 4 HOH 391 1091 530 HOH HOH A . 
G 4 HOH 392 1092 774 HOH HOH A . 
G 4 HOH 393 1093 300 HOH HOH A . 
G 4 HOH 394 1094 369 HOH HOH A . 
G 4 HOH 395 1095 589 HOH HOH A . 
G 4 HOH 396 1096 512 HOH HOH A . 
G 4 HOH 397 1097 618 HOH HOH A . 
G 4 HOH 398 1098 794 HOH HOH A . 
G 4 HOH 399 1099 250 HOH HOH A . 
G 4 HOH 400 1100 174 HOH HOH A . 
G 4 HOH 401 1101 675 HOH HOH A . 
G 4 HOH 402 1102 703 HOH HOH A . 
G 4 HOH 403 1103 288 HOH HOH A . 
G 4 HOH 404 1104 625 HOH HOH A . 
G 4 HOH 405 1105 793 HOH HOH A . 
G 4 HOH 406 1106 268 HOH HOH A . 
G 4 HOH 407 1107 154 HOH HOH A . 
G 4 HOH 408 1108 491 HOH HOH A . 
G 4 HOH 409 1109 619 HOH HOH A . 
G 4 HOH 410 1110 266 HOH HOH A . 
G 4 HOH 411 1111 557 HOH HOH A . 
G 4 HOH 412 1112 834 HOH HOH A . 
G 4 HOH 413 1113 729 HOH HOH A . 
G 4 HOH 414 1114 341 HOH HOH A . 
G 4 HOH 415 1115 778 HOH HOH A . 
G 4 HOH 416 1116 511 HOH HOH A . 
G 4 HOH 417 1117 796 HOH HOH A . 
G 4 HOH 418 1118 828 HOH HOH A . 
G 4 HOH 419 1119 611 HOH HOH A . 
G 4 HOH 420 1120 637 HOH HOH A . 
G 4 HOH 421 1121 790 HOH HOH A . 
G 4 HOH 422 1122 783 HOH HOH A . 
G 4 HOH 423 1123 610 HOH HOH A . 
G 4 HOH 424 1124 798 HOH HOH A . 
G 4 HOH 425 1125 792 HOH HOH A . 
G 4 HOH 426 1126 832 HOH HOH A . 
G 4 HOH 427 1127 835 HOH HOH A . 
G 4 HOH 428 1128 831 HOH HOH A . 
G 4 HOH 429 1129 824 HOH HOH A . 
G 4 HOH 430 1130 695 HOH HOH A . 
G 4 HOH 431 1131 237 HOH HOH A . 
G 4 HOH 432 1132 486 HOH HOH A . 
G 4 HOH 433 1133 822 HOH HOH A . 
G 4 HOH 434 1134 632 HOH HOH A . 
G 4 HOH 435 1135 546 HOH HOH A . 
G 4 HOH 436 1136 612 HOH HOH A . 
G 4 HOH 437 1137 734 HOH HOH A . 
H 4 HOH 1   701  710 HOH HOH B . 
H 4 HOH 2   702  165 HOH HOH B . 
H 4 HOH 3   703  228 HOH HOH B . 
H 4 HOH 4   704  220 HOH HOH B . 
H 4 HOH 5   705  307 HOH HOH B . 
H 4 HOH 6   706  566 HOH HOH B . 
H 4 HOH 7   707  20  HOH HOH B . 
H 4 HOH 8   708  845 HOH HOH B . 
H 4 HOH 9   709  593 HOH HOH B . 
H 4 HOH 10  710  615 HOH HOH B . 
H 4 HOH 11  711  414 HOH HOH B . 
H 4 HOH 12  712  232 HOH HOH B . 
H 4 HOH 13  713  480 HOH HOH B . 
H 4 HOH 14  714  367 HOH HOH B . 
H 4 HOH 15  715  431 HOH HOH B . 
H 4 HOH 16  716  476 HOH HOH B . 
H 4 HOH 17  717  22  HOH HOH B . 
H 4 HOH 18  718  497 HOH HOH B . 
H 4 HOH 19  719  535 HOH HOH B . 
H 4 HOH 20  720  261 HOH HOH B . 
H 4 HOH 21  721  786 HOH HOH B . 
H 4 HOH 22  722  229 HOH HOH B . 
H 4 HOH 23  723  345 HOH HOH B . 
H 4 HOH 24  724  204 HOH HOH B . 
H 4 HOH 25  725  137 HOH HOH B . 
H 4 HOH 26  726  13  HOH HOH B . 
H 4 HOH 27  727  463 HOH HOH B . 
H 4 HOH 28  728  721 HOH HOH B . 
H 4 HOH 29  729  570 HOH HOH B . 
H 4 HOH 30  730  80  HOH HOH B . 
H 4 HOH 31  731  474 HOH HOH B . 
H 4 HOH 32  732  16  HOH HOH B . 
H 4 HOH 33  733  534 HOH HOH B . 
H 4 HOH 34  734  407 HOH HOH B . 
H 4 HOH 35  735  58  HOH HOH B . 
H 4 HOH 36  736  177 HOH HOH B . 
H 4 HOH 37  737  389 HOH HOH B . 
H 4 HOH 38  738  670 HOH HOH B . 
H 4 HOH 39  739  239 HOH HOH B . 
H 4 HOH 40  740  613 HOH HOH B . 
H 4 HOH 41  741  108 HOH HOH B . 
H 4 HOH 42  742  142 HOH HOH B . 
H 4 HOH 43  743  162 HOH HOH B . 
H 4 HOH 44  744  427 HOH HOH B . 
H 4 HOH 45  745  283 HOH HOH B . 
H 4 HOH 46  746  689 HOH HOH B . 
H 4 HOH 47  747  11  HOH HOH B . 
H 4 HOH 48  748  585 HOH HOH B . 
H 4 HOH 49  749  694 HOH HOH B . 
H 4 HOH 50  750  676 HOH HOH B . 
H 4 HOH 51  751  209 HOH HOH B . 
H 4 HOH 52  752  94  HOH HOH B . 
H 4 HOH 53  753  343 HOH HOH B . 
H 4 HOH 54  754  183 HOH HOH B . 
H 4 HOH 55  755  417 HOH HOH B . 
H 4 HOH 56  756  726 HOH HOH B . 
H 4 HOH 57  757  130 HOH HOH B . 
H 4 HOH 58  758  276 HOH HOH B . 
H 4 HOH 59  759  272 HOH HOH B . 
H 4 HOH 60  760  10  HOH HOH B . 
H 4 HOH 61  761  57  HOH HOH B . 
H 4 HOH 62  762  182 HOH HOH B . 
H 4 HOH 63  763  164 HOH HOH B . 
H 4 HOH 64  764  238 HOH HOH B . 
H 4 HOH 65  765  528 HOH HOH B . 
H 4 HOH 66  766  650 HOH HOH B . 
H 4 HOH 67  767  366 HOH HOH B . 
H 4 HOH 68  768  357 HOH HOH B . 
H 4 HOH 69  769  6   HOH HOH B . 
H 4 HOH 70  770  129 HOH HOH B . 
H 4 HOH 71  771  60  HOH HOH B . 
H 4 HOH 72  772  608 HOH HOH B . 
H 4 HOH 73  773  150 HOH HOH B . 
H 4 HOH 74  774  105 HOH HOH B . 
H 4 HOH 75  775  494 HOH HOH B . 
H 4 HOH 76  776  712 HOH HOH B . 
H 4 HOH 77  777  537 HOH HOH B . 
H 4 HOH 78  778  275 HOH HOH B . 
H 4 HOH 79  779  756 HOH HOH B . 
H 4 HOH 80  780  175 HOH HOH B . 
H 4 HOH 81  781  375 HOH HOH B . 
H 4 HOH 82  782  116 HOH HOH B . 
H 4 HOH 83  783  17  HOH HOH B . 
H 4 HOH 84  784  360 HOH HOH B . 
H 4 HOH 85  785  202 HOH HOH B . 
H 4 HOH 86  786  118 HOH HOH B . 
H 4 HOH 87  787  32  HOH HOH B . 
H 4 HOH 88  788  3   HOH HOH B . 
H 4 HOH 89  789  18  HOH HOH B . 
H 4 HOH 90  790  216 HOH HOH B . 
H 4 HOH 91  791  576 HOH HOH B . 
H 4 HOH 92  792  482 HOH HOH B . 
H 4 HOH 93  793  492 HOH HOH B . 
H 4 HOH 94  794  41  HOH HOH B . 
H 4 HOH 95  795  850 HOH HOH B . 
H 4 HOH 96  796  102 HOH HOH B . 
H 4 HOH 97  797  502 HOH HOH B . 
H 4 HOH 98  798  514 HOH HOH B . 
H 4 HOH 99  799  529 HOH HOH B . 
H 4 HOH 100 800  472 HOH HOH B . 
H 4 HOH 101 801  649 HOH HOH B . 
H 4 HOH 102 802  117 HOH HOH B . 
H 4 HOH 103 803  143 HOH HOH B . 
H 4 HOH 104 804  667 HOH HOH B . 
H 4 HOH 105 805  83  HOH HOH B . 
H 4 HOH 106 806  379 HOH HOH B . 
H 4 HOH 107 807  243 HOH HOH B . 
H 4 HOH 108 808  224 HOH HOH B . 
H 4 HOH 109 809  363 HOH HOH B . 
H 4 HOH 110 810  96  HOH HOH B . 
H 4 HOH 111 811  526 HOH HOH B . 
H 4 HOH 112 812  671 HOH HOH B . 
H 4 HOH 113 813  586 HOH HOH B . 
H 4 HOH 114 814  456 HOH HOH B . 
H 4 HOH 115 815  180 HOH HOH B . 
H 4 HOH 116 816  515 HOH HOH B . 
H 4 HOH 117 817  730 HOH HOH B . 
H 4 HOH 118 818  748 HOH HOH B . 
H 4 HOH 119 819  870 HOH HOH B . 
H 4 HOH 120 820  68  HOH HOH B . 
H 4 HOH 121 821  708 HOH HOH B . 
H 4 HOH 122 822  620 HOH HOH B . 
H 4 HOH 123 823  398 HOH HOH B . 
H 4 HOH 124 824  655 HOH HOH B . 
H 4 HOH 125 825  700 HOH HOH B . 
H 4 HOH 126 826  320 HOH HOH B . 
H 4 HOH 127 827  527 HOH HOH B . 
H 4 HOH 128 828  285 HOH HOH B . 
H 4 HOH 129 829  718 HOH HOH B . 
H 4 HOH 130 830  152 HOH HOH B . 
H 4 HOH 131 831  318 HOH HOH B . 
H 4 HOH 132 832  120 HOH HOH B . 
H 4 HOH 133 833  487 HOH HOH B . 
H 4 HOH 134 834  305 HOH HOH B . 
H 4 HOH 135 835  705 HOH HOH B . 
H 4 HOH 136 836  234 HOH HOH B . 
H 4 HOH 137 837  293 HOH HOH B . 
H 4 HOH 138 838  412 HOH HOH B . 
H 4 HOH 139 839  87  HOH HOH B . 
H 4 HOH 140 840  21  HOH HOH B . 
H 4 HOH 141 841  740 HOH HOH B . 
H 4 HOH 142 842  616 HOH HOH B . 
H 4 HOH 143 843  29  HOH HOH B . 
H 4 HOH 144 844  747 HOH HOH B . 
H 4 HOH 145 845  420 HOH HOH B . 
H 4 HOH 146 846  304 HOH HOH B . 
H 4 HOH 147 847  89  HOH HOH B . 
H 4 HOH 148 848  178 HOH HOH B . 
H 4 HOH 149 849  311 HOH HOH B . 
H 4 HOH 150 850  45  HOH HOH B . 
H 4 HOH 151 851  401 HOH HOH B . 
H 4 HOH 152 852  702 HOH HOH B . 
H 4 HOH 153 853  326 HOH HOH B . 
H 4 HOH 154 854  249 HOH HOH B . 
H 4 HOH 155 855  82  HOH HOH B . 
H 4 HOH 156 856  520 HOH HOH B . 
H 4 HOH 157 857  251 HOH HOH B . 
H 4 HOH 158 858  517 HOH HOH B . 
H 4 HOH 159 859  189 HOH HOH B . 
H 4 HOH 160 860  384 HOH HOH B . 
H 4 HOH 161 861  453 HOH HOH B . 
H 4 HOH 162 862  219 HOH HOH B . 
H 4 HOH 163 863  217 HOH HOH B . 
H 4 HOH 164 864  187 HOH HOH B . 
H 4 HOH 165 865  365 HOH HOH B . 
H 4 HOH 166 866  201 HOH HOH B . 
H 4 HOH 167 867  408 HOH HOH B . 
H 4 HOH 168 868  141 HOH HOH B . 
H 4 HOH 169 869  107 HOH HOH B . 
H 4 HOH 170 870  263 HOH HOH B . 
H 4 HOH 171 871  842 HOH HOH B . 
H 4 HOH 172 872  138 HOH HOH B . 
H 4 HOH 173 873  242 HOH HOH B . 
H 4 HOH 174 874  698 HOH HOH B . 
H 4 HOH 175 875  8   HOH HOH B . 
H 4 HOH 176 876  347 HOH HOH B . 
H 4 HOH 177 877  279 HOH HOH B . 
H 4 HOH 178 878  880 HOH HOH B . 
H 4 HOH 179 879  872 HOH HOH B . 
H 4 HOH 180 880  26  HOH HOH B . 
H 4 HOH 181 881  64  HOH HOH B . 
H 4 HOH 182 882  290 HOH HOH B . 
H 4 HOH 183 883  42  HOH HOH B . 
H 4 HOH 184 884  133 HOH HOH B . 
H 4 HOH 185 885  668 HOH HOH B . 
H 4 HOH 186 886  875 HOH HOH B . 
H 4 HOH 187 887  447 HOH HOH B . 
H 4 HOH 188 888  405 HOH HOH B . 
H 4 HOH 189 889  23  HOH HOH B . 
H 4 HOH 190 890  410 HOH HOH B . 
H 4 HOH 191 891  399 HOH HOH B . 
H 4 HOH 192 892  627 HOH HOH B . 
H 4 HOH 193 893  286 HOH HOH B . 
H 4 HOH 194 894  9   HOH HOH B . 
H 4 HOH 195 895  43  HOH HOH B . 
H 4 HOH 196 896  230 HOH HOH B . 
H 4 HOH 197 897  254 HOH HOH B . 
H 4 HOH 198 898  194 HOH HOH B . 
H 4 HOH 199 899  569 HOH HOH B . 
H 4 HOH 200 900  73  HOH HOH B . 
H 4 HOH 201 901  871 HOH HOH B . 
H 4 HOH 202 902  473 HOH HOH B . 
H 4 HOH 203 903  869 HOH HOH B . 
H 4 HOH 204 904  393 HOH HOH B . 
H 4 HOH 205 905  604 HOH HOH B . 
H 4 HOH 206 906  704 HOH HOH B . 
H 4 HOH 207 907  435 HOH HOH B . 
H 4 HOH 208 908  135 HOH HOH B . 
H 4 HOH 209 909  573 HOH HOH B . 
H 4 HOH 210 910  810 HOH HOH B . 
H 4 HOH 211 911  39  HOH HOH B . 
H 4 HOH 212 912  553 HOH HOH B . 
H 4 HOH 213 913  110 HOH HOH B . 
H 4 HOH 214 914  686 HOH HOH B . 
H 4 HOH 215 915  590 HOH HOH B . 
H 4 HOH 216 916  212 HOH HOH B . 
H 4 HOH 217 917  207 HOH HOH B . 
H 4 HOH 218 918  757 HOH HOH B . 
H 4 HOH 219 919  484 HOH HOH B . 
H 4 HOH 220 920  327 HOH HOH B . 
H 4 HOH 221 921  350 HOH HOH B . 
H 4 HOH 222 922  38  HOH HOH B . 
H 4 HOH 223 923  602 HOH HOH B . 
H 4 HOH 224 924  354 HOH HOH B . 
H 4 HOH 225 925  744 HOH HOH B . 
H 4 HOH 226 926  208 HOH HOH B . 
H 4 HOH 227 927  144 HOH HOH B . 
H 4 HOH 228 928  340 HOH HOH B . 
H 4 HOH 229 929  262 HOH HOH B . 
H 4 HOH 230 930  27  HOH HOH B . 
H 4 HOH 231 931  858 HOH HOH B . 
H 4 HOH 232 932  77  HOH HOH B . 
H 4 HOH 233 933  548 HOH HOH B . 
H 4 HOH 234 934  69  HOH HOH B . 
H 4 HOH 235 935  197 HOH HOH B . 
H 4 HOH 236 936  587 HOH HOH B . 
H 4 HOH 237 937  464 HOH HOH B . 
H 4 HOH 238 938  639 HOH HOH B . 
H 4 HOH 239 939  273 HOH HOH B . 
H 4 HOH 240 940  660 HOH HOH B . 
H 4 HOH 241 941  168 HOH HOH B . 
H 4 HOH 242 942  641 HOH HOH B . 
H 4 HOH 243 943  52  HOH HOH B . 
H 4 HOH 244 944  346 HOH HOH B . 
H 4 HOH 245 945  66  HOH HOH B . 
H 4 HOH 246 946  584 HOH HOH B . 
H 4 HOH 247 947  215 HOH HOH B . 
H 4 HOH 248 948  112 HOH HOH B . 
H 4 HOH 249 949  624 HOH HOH B . 
H 4 HOH 250 950  258 HOH HOH B . 
H 4 HOH 251 951  508 HOH HOH B . 
H 4 HOH 252 952  581 HOH HOH B . 
H 4 HOH 253 953  221 HOH HOH B . 
H 4 HOH 254 954  854 HOH HOH B . 
H 4 HOH 255 955  298 HOH HOH B . 
H 4 HOH 256 956  213 HOH HOH B . 
H 4 HOH 257 957  876 HOH HOH B . 
H 4 HOH 258 958  269 HOH HOH B . 
H 4 HOH 259 959  81  HOH HOH B . 
H 4 HOH 260 960  432 HOH HOH B . 
H 4 HOH 261 961  132 HOH HOH B . 
H 4 HOH 262 962  846 HOH HOH B . 
H 4 HOH 263 963  227 HOH HOH B . 
H 4 HOH 264 964  658 HOH HOH B . 
H 4 HOH 265 965  373 HOH HOH B . 
H 4 HOH 266 966  98  HOH HOH B . 
H 4 HOH 267 967  571 HOH HOH B . 
H 4 HOH 268 968  558 HOH HOH B . 
H 4 HOH 269 969  309 HOH HOH B . 
H 4 HOH 270 970  860 HOH HOH B . 
H 4 HOH 271 971  621 HOH HOH B . 
H 4 HOH 272 972  265 HOH HOH B . 
H 4 HOH 273 973  609 HOH HOH B . 
H 4 HOH 274 974  457 HOH HOH B . 
H 4 HOH 275 975  722 HOH HOH B . 
H 4 HOH 276 976  421 HOH HOH B . 
H 4 HOH 277 977  540 HOH HOH B . 
H 4 HOH 278 978  218 HOH HOH B . 
H 4 HOH 279 979  866 HOH HOH B . 
H 4 HOH 280 980  645 HOH HOH B . 
H 4 HOH 281 981  299 HOH HOH B . 
H 4 HOH 282 982  441 HOH HOH B . 
H 4 HOH 283 983  225 HOH HOH B . 
H 4 HOH 284 984  882 HOH HOH B . 
H 4 HOH 285 985  270 HOH HOH B . 
H 4 HOH 286 986  30  HOH HOH B . 
H 4 HOH 287 987  559 HOH HOH B . 
H 4 HOH 288 988  630 HOH HOH B . 
H 4 HOH 289 989  35  HOH HOH B . 
H 4 HOH 290 990  344 HOH HOH B . 
H 4 HOH 291 991  260 HOH HOH B . 
H 4 HOH 292 992  151 HOH HOH B . 
H 4 HOH 293 993  707 HOH HOH B . 
H 4 HOH 294 994  855 HOH HOH B . 
H 4 HOH 295 995  380 HOH HOH B . 
H 4 HOH 296 996  556 HOH HOH B . 
H 4 HOH 297 997  469 HOH HOH B . 
H 4 HOH 298 998  240 HOH HOH B . 
H 4 HOH 299 999  567 HOH HOH B . 
H 4 HOH 300 1000 28  HOH HOH B . 
H 4 HOH 301 1001 493 HOH HOH B . 
H 4 HOH 302 1002 106 HOH HOH B . 
H 4 HOH 303 1003 274 HOH HOH B . 
H 4 HOH 304 1004 336 HOH HOH B . 
H 4 HOH 305 1005 782 HOH HOH B . 
H 4 HOH 306 1006 523 HOH HOH B . 
H 4 HOH 307 1007 644 HOH HOH B . 
H 4 HOH 308 1008 761 HOH HOH B . 
H 4 HOH 309 1009 424 HOH HOH B . 
H 4 HOH 310 1010 574 HOH HOH B . 
H 4 HOH 311 1011 483 HOH HOH B . 
H 4 HOH 312 1012 821 HOH HOH B . 
H 4 HOH 313 1013 758 HOH HOH B . 
H 4 HOH 314 1014 169 HOH HOH B . 
H 4 HOH 315 1015 437 HOH HOH B . 
H 4 HOH 316 1016 538 HOH HOH B . 
H 4 HOH 317 1017 773 HOH HOH B . 
H 4 HOH 318 1018 436 HOH HOH B . 
H 4 HOH 319 1019 312 HOH HOH B . 
H 4 HOH 320 1020 766 HOH HOH B . 
H 4 HOH 321 1021 442 HOH HOH B . 
H 4 HOH 322 1022 1   HOH HOH B . 
H 4 HOH 323 1023 277 HOH HOH B . 
H 4 HOH 324 1024 720 HOH HOH B . 
H 4 HOH 325 1025 562 HOH HOH B . 
H 4 HOH 326 1026 172 HOH HOH B . 
H 4 HOH 327 1027 167 HOH HOH B . 
H 4 HOH 328 1028 467 HOH HOH B . 
H 4 HOH 329 1029 770 HOH HOH B . 
H 4 HOH 330 1030 353 HOH HOH B . 
H 4 HOH 331 1031 337 HOH HOH B . 
H 4 HOH 332 1032 294 HOH HOH B . 
H 4 HOH 333 1033 388 HOH HOH B . 
H 4 HOH 334 1034 759 HOH HOH B . 
H 4 HOH 335 1035 560 HOH HOH B . 
H 4 HOH 336 1036 74  HOH HOH B . 
H 4 HOH 337 1037 776 HOH HOH B . 
H 4 HOH 338 1038 836 HOH HOH B . 
H 4 HOH 339 1039 696 HOH HOH B . 
H 4 HOH 340 1040 679 HOH HOH B . 
H 4 HOH 341 1041 446 HOH HOH B . 
H 4 HOH 342 1042 498 HOH HOH B . 
H 4 HOH 343 1043 296 HOH HOH B . 
H 4 HOH 344 1044 505 HOH HOH B . 
H 4 HOH 345 1045 727 HOH HOH B . 
H 4 HOH 346 1046 542 HOH HOH B . 
H 4 HOH 347 1047 297 HOH HOH B . 
H 4 HOH 348 1048 460 HOH HOH B . 
H 4 HOH 349 1049 709 HOH HOH B . 
H 4 HOH 350 1050 795 HOH HOH B . 
H 4 HOH 351 1051 591 HOH HOH B . 
H 4 HOH 352 1052 775 HOH HOH B . 
H 4 HOH 353 1053 397 HOH HOH B . 
H 4 HOH 354 1054 291 HOH HOH B . 
H 4 HOH 355 1055 772 HOH HOH B . 
H 4 HOH 356 1056 598 HOH HOH B . 
H 4 HOH 357 1057 827 HOH HOH B . 
H 4 HOH 358 1058 674 HOH HOH B . 
H 4 HOH 359 1059 223 HOH HOH B . 
H 4 HOH 360 1060 40  HOH HOH B . 
H 4 HOH 361 1061 438 HOH HOH B . 
H 4 HOH 362 1062 764 HOH HOH B . 
H 4 HOH 363 1063 767 HOH HOH B . 
H 4 HOH 364 1064 825 HOH HOH B . 
H 4 HOH 365 1065 742 HOH HOH B . 
H 4 HOH 366 1066 799 HOH HOH B . 
H 4 HOH 367 1067 733 HOH HOH B . 
H 4 HOH 368 1068 745 HOH HOH B . 
H 4 HOH 369 1069 490 HOH HOH B . 
H 4 HOH 370 1070 659 HOH HOH B . 
H 4 HOH 371 1071 777 HOH HOH B . 
H 4 HOH 372 1072 533 HOH HOH B . 
H 4 HOH 373 1073 485 HOH HOH B . 
H 4 HOH 374 1074 685 HOH HOH B . 
H 4 HOH 375 1075 797 HOH HOH B . 
H 4 HOH 376 1076 358 HOH HOH B . 
H 4 HOH 377 1077 771 HOH HOH B . 
H 4 HOH 378 1078 737 HOH HOH B . 
H 4 HOH 379 1079 808 HOH HOH B . 
H 4 HOH 380 1080 404 HOH HOH B . 
H 4 HOH 381 1081 813 HOH HOH B . 
H 4 HOH 382 1082 444 HOH HOH B . 
H 4 HOH 383 1083 823 HOH HOH B . 
H 4 HOH 384 1084 666 HOH HOH B . 
H 4 HOH 385 1085 687 HOH HOH B . 
H 4 HOH 386 1086 803 HOH HOH B . 
H 4 HOH 387 1087 629 HOH HOH B . 
H 4 HOH 388 1088 840 HOH HOH B . 
H 4 HOH 389 1089 697 HOH HOH B . 
H 4 HOH 390 1090 244 HOH HOH B . 
H 4 HOH 391 1091 423 HOH HOH B . 
H 4 HOH 392 1092 592 HOH HOH B . 
H 4 HOH 393 1093 780 HOH HOH B . 
H 4 HOH 394 1094 259 HOH HOH B . 
H 4 HOH 395 1095 409 HOH HOH B . 
H 4 HOH 396 1096 428 HOH HOH B . 
H 4 HOH 397 1097 723 HOH HOH B . 
H 4 HOH 398 1098 419 HOH HOH B . 
H 4 HOH 399 1099 682 HOH HOH B . 
H 4 HOH 400 1100 551 HOH HOH B . 
H 4 HOH 401 1101 801 HOH HOH B . 
H 4 HOH 402 1102 713 HOH HOH B . 
H 4 HOH 403 1103 416 HOH HOH B . 
H 4 HOH 404 1104 638 HOH HOH B . 
H 4 HOH 405 1105 599 HOH HOH B . 
H 4 HOH 406 1106 817 HOH HOH B . 
H 4 HOH 407 1107 518 HOH HOH B . 
H 4 HOH 408 1108 564 HOH HOH B . 
H 4 HOH 409 1109 714 HOH HOH B . 
H 4 HOH 410 1110 203 HOH HOH B . 
H 4 HOH 411 1111 478 HOH HOH B . 
H 4 HOH 412 1112 588 HOH HOH B . 
H 4 HOH 413 1113 752 HOH HOH B . 
H 4 HOH 414 1114 278 HOH HOH B . 
H 4 HOH 415 1115 811 HOH HOH B . 
H 4 HOH 416 1116 820 HOH HOH B . 
H 4 HOH 417 1117 543 HOH HOH B . 
H 4 HOH 418 1118 731 HOH HOH B . 
H 4 HOH 419 1119 779 HOH HOH B . 
H 4 HOH 420 1120 458 HOH HOH B . 
H 4 HOH 421 1121 563 HOH HOH B . 
H 4 HOH 422 1122 787 HOH HOH B . 
H 4 HOH 423 1123 465 HOH HOH B . 
H 4 HOH 424 1124 812 HOH HOH B . 
H 4 HOH 425 1125 765 HOH HOH B . 
H 4 HOH 426 1126 471 HOH HOH B . 
H 4 HOH 427 1127 768 HOH HOH B . 
H 4 HOH 428 1128 839 HOH HOH B . 
H 4 HOH 429 1129 741 HOH HOH B . 
H 4 HOH 430 1130 633 HOH HOH B . 
H 4 HOH 431 1131 809 HOH HOH B . 
H 4 HOH 432 1132 814 HOH HOH B . 
H 4 HOH 433 1133 829 HOH HOH B . 
H 4 HOH 434 1134 422 HOH HOH B . 
H 4 HOH 435 1135 818 HOH HOH B . 
H 4 HOH 436 1136 833 HOH HOH B . 
H 4 HOH 437 1137 738 HOH HOH B . 
# 
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  ? ? ? 5.8.0430 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.498 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G8A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.836 
_cell.length_a_esd                 ? 
_cell.length_b                     83.808 
_cell.length_b_esd                 ? 
_cell.length_c                     98.117 
_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                         9G8A 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G8A 
_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             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.88 
_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              ? 
_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    '20% w/v Polyethyleneglycol 3,350 200mM Ammonium acetate 30% GOL' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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         2024-05-04 
_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   0.87313 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.87313 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G8A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               69.55 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     67761 
_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                           89.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.48 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.156 
_reflns.pdbx_Rpim_I_all                                0.110 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.989 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.111 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_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 
_reflns_shell.pdbx_diffrn_id 
_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 
_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 
9.38 69.55 ? 13.2 ? ? ? ? 727  ? ? ? ? ? ? ? ? ? ? ? 2.8 0.38 ? ? 0.047 0.033 ? 1 ? 0.996 ? ? 92.7 ? 0.033 ? ? ? ? ? ? ? ? ? 
2.00 2.05  ? 1.5  ? ? ? ? 4990 ? ? ? ? ? ? ? ? ? ? ? 3.1 0.43 ? ? 0.633 0.443 ? 2 ? 0.731 ? ? 97.1 ? 0.452 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -1.511 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            -1.167 
_refine.aniso_B[2][2]                            1.081 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.911 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.128 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.937 
_refine.details                                  'Hydrogens have not been used' 
_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                                 9G8A 
_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                            2.000 
_refine.ls_d_res_low                             69.548 
_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                     67740 
_refine.ls_number_reflns_R_free                  3363 
_refine.ls_number_reflns_R_work                  64377 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.916 
_refine.ls_percent_reflns_R_free                 4.965 
_refine.ls_R_factor_all                          0.182 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2181 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1799 
_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 BULK SOLVENT' 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.223 
_refine.pdbx_overall_ESU_R_Free                  0.176 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                             5.481 
_refine.overall_SU_ML                            0.144 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        69.548 
_refine_hist.number_atoms_solvent             874 
_refine_hist.number_atoms_total               9314 
_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        8420 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.012  8702  ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 2.193  1.821  11844 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.765  5.000  1048  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 8.730  5.000  58    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.855 10.000 1358  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.515 10.000 430   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.172  0.200  1216  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  6976  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.134  0.200  3876  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.260  0.200  5649  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.200  907   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200  2     ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.129  0.200  68    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.114  0.200  23    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 1.541  2.137  4198  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.357  3.864  5244  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 2.418  2.304  4504  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.729  4.157  6600  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.596  25.509 13380 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 0.045  0.050  17397 ? r_ncsr_local_group_1           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.04489 ? 0.05009 1 'Local ncs' ? A ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.04489 ? 0.05009 2 'Local ncs' ? B ? ? ? 1 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.000 2.052  5615 . 263 5182 96.9724 . 0.256 . . 0.255 . . . . . 0.251 . 20 . 0.951 0.950 0.263 
'X-RAY DIFFRACTION' 2.052 2.108  5430 . 152 3128 60.4052 . 0.234 . . 0.233 . . . . . 0.227 . 20 . 0.961 0.957 0.253 
'X-RAY DIFFRACTION' 2.108 2.169  5328 . 279 4884 96.9032 . 0.226 . . 0.225 . . . . . 0.219 . 20 . 0.966 0.957 0.250 
'X-RAY DIFFRACTION' 2.169 2.236  5130 . 249 4722 96.9006 . 0.218 . . 0.216 . . . . . 0.209 . 20 . 0.968 0.961 0.253 
'X-RAY DIFFRACTION' 2.236 2.309  5028 . 155 3443 71.5593 . 0.216 . . 0.214 . . . . . 0.206 . 20 . 0.969 0.947 0.272 
'X-RAY DIFFRACTION' 2.309 2.390  4866 . 205 4498 96.6502 . 0.202 . . 0.199 . . . . . 0.192 . 20 . 0.973 0.955 0.266 
'X-RAY DIFFRACTION' 2.390 2.480  4662 . 246 4276 96.9970 . 0.213 . . 0.210 . . . . . 0.202 . 20 . 0.971 0.953 0.262 
'X-RAY DIFFRACTION' 2.480 2.581  4500 . 198 4162 96.8889 . 0.203 . . 0.200 . . . . . 0.191 . 20 . 0.974 0.962 0.254 
'X-RAY DIFFRACTION' 2.581 2.696  4334 . 147 2973 71.9889 . 0.207 . . 0.204 . . . . . 0.195 . 20 . 0.975 0.959 0.257 
'X-RAY DIFFRACTION' 2.696 2.827  4113 . 183 3765 95.9883 . 0.187 . . 0.185 . . . . . 0.177 . 20 . 0.978 0.966 0.228 
'X-RAY DIFFRACTION' 2.827 2.980  3947 . 210 3591 96.3010 . 0.190 . . 0.186 . . . . . 0.181 . 20 . 0.979 0.958 0.248 
'X-RAY DIFFRACTION' 2.980 3.160  3728 . 181 3367 95.1717 . 0.177 . . 0.175 . . . . . 0.170 . 20 . 0.981 0.969 0.214 
'X-RAY DIFFRACTION' 3.160 3.378  3501 . 188 3152 95.4013 . 0.180 . . 0.179 . . . . . 0.177 . 20 . 0.981 0.972 0.208 
'X-RAY DIFFRACTION' 3.378 3.648  3270 . 120 2354 75.6575 . 0.166 . . 0.165 . . . . . 0.164 . 20 . 0.984 0.977 0.197 
'X-RAY DIFFRACTION' 3.648 3.995  3010 . 119 1940 68.4053 . 0.154 . . 0.152 . . . . . 0.153 . 20 . 0.986 0.983 0.189 
'X-RAY DIFFRACTION' 3.995 4.465  2728 . 140 2509 97.1041 . 0.133 . . 0.131 . . . . . 0.137 . 20 . 0.991 0.986 0.174 
'X-RAY DIFFRACTION' 4.465 5.152  2418 . 106 2261 97.8908 . 0.122 . . 0.121 . . . . . 0.127 . 20 . 0.992 0.988 0.155 
'X-RAY DIFFRACTION' 5.152 6.301  2028 . 96  1874 97.1400 . 0.147 . . 0.146 . . . . . 0.151 . 20 . 0.988 0.984 0.173 
'X-RAY DIFFRACTION' 6.301 8.875  1624 . 72  1493 96.3670 . 0.158 . . 0.157 . . . . . 0.164 . 20 . 0.986 0.974 0.200 
'X-RAY DIFFRACTION' 8.875 69.548 924  . 54  804  92.8571 . 0.195 . . 0.195 . . . . . 0.222 . 20 . 0.973 0.978 0.195 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 A 
2 1 B 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A TYR 32 . A ALA 556 . A TYR 24 A ALA 548 ? ? 
1 2 1 B TYR 32 . B ALA 556 . B TYR 24 B ALA 548 ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   'Local NCS retraints between domains:       1       2' 
# 
_struct.entry_id                     9G8A 
_struct.title                        'Carotenoid cleavage oxygenase from Moesziomyces aphidis bound to p-hydroxybenzaldehyde' 
_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        9G8A 
_struct_keywords.text            'oxygenase, Moesziomyces aphidi, p-hydroxybenzaldehyde, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
# 
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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    W3VHW6_MOEAP 
_struct_ref.pdbx_db_accession          W3VHW6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APTATQEPVPVPVTSKAAPSHGYVHPTDILPSGWPTATDLSGGAQPRRFEGTIFDVMTRGTIPKELHGTFYRIMPDYAQP
PTYYKGGELNAPIDGDGTVAAFRFKDGKVDYRQRFVETDRFKVERRARKSMYGLYRNPYTHHPCVRQTVESTANTNVVMH
AGRFLAMKENGNAYEMDPHTLKTLGYNPFNLPSKTMTAHPKQCSVTGNLVGFGYEAKGLATKDVYYFEVDPSGKVVRDLW
LEAPWCAFIHDCALTPNYLVLMLWPFEANLERMKAGGHHWAYDYTKPITWITIPRGAKSKDEVKYWHWKNGMPIHTASGF
EDEQGRIIIDSSLVHGNAFPFFPPDSDEQKKKQEADGTPKAQFVRWTIDPRKDNNEQLPDPEVILDTPSEFPQIDNRFMG
VEYSSAFINVFVPDRSDGNKNVFQGLNGLAHYKRKEGTTEWYYAGDNCLIQEPVFSPRSKDAPEGDGFVLAIVDRLDLNR
SEVVVIDTRDFTKAVAAVQLPFAIRSGIHGQWIPGEVTPDFETKGLVDLPKEEHWAPLSQSPYDPDA
;
_struct_ref.pdbx_align_begin           2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9G8A A 10 ? 556 ? W3VHW6 2 ? 548 ? 2 548 
2 1 9G8A B 10 ? 556 ? W3VHW6 2 ? 548 ? 2 548 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9G8A MET A 1 ? UNP W3VHW6 ? ? 'initiating methionine' -7 1  
1 9G8A TRP A 2 ? UNP W3VHW6 ? ? 'expression tag'        -6 2  
1 9G8A SER A 3 ? UNP W3VHW6 ? ? 'expression tag'        -5 3  
1 9G8A HIS A 4 ? UNP W3VHW6 ? ? 'expression tag'        -4 4  
1 9G8A PRO A 5 ? UNP W3VHW6 ? ? 'expression tag'        -3 5  
1 9G8A GLN A 6 ? UNP W3VHW6 ? ? 'expression tag'        -2 6  
1 9G8A PHE A 7 ? UNP W3VHW6 ? ? 'expression tag'        -1 7  
1 9G8A GLU A 8 ? UNP W3VHW6 ? ? 'expression tag'        0  8  
1 9G8A LYS A 9 ? UNP W3VHW6 ? ? 'expression tag'        1  9  
2 9G8A MET B 1 ? UNP W3VHW6 ? ? 'initiating methionine' -7 10 
2 9G8A TRP B 2 ? UNP W3VHW6 ? ? 'expression tag'        -6 11 
2 9G8A SER B 3 ? UNP W3VHW6 ? ? 'expression tag'        -5 12 
2 9G8A HIS B 4 ? UNP W3VHW6 ? ? 'expression tag'        -4 13 
2 9G8A PRO B 5 ? UNP W3VHW6 ? ? 'expression tag'        -3 14 
2 9G8A GLN B 6 ? UNP W3VHW6 ? ? 'expression tag'        -2 15 
2 9G8A PHE B 7 ? UNP W3VHW6 ? ? 'expression tag'        -1 16 
2 9G8A GLU B 8 ? UNP W3VHW6 ? ? 'expression tag'        0  17 
2 9G8A LYS B 9 ? UNP W3VHW6 ? ? 'expression tag'        1  18 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_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 HIS A 34  ? LEU A 39  ? HIS A 26  LEU A 31  5 ? 6  
HELX_P HELX_P2  AA2 TYR A 93  ? GLU A 97  ? TYR A 85  GLU A 89  5 ? 5  
HELX_P HELX_P3  AA3 THR A 127 ? ARG A 137 ? THR A 119 ARG A 129 1 ? 11 
HELX_P HELX_P4  AA4 ASN A 146 ? HIS A 150 ? ASN A 138 HIS A 142 5 ? 5  
HELX_P HELX_P5  AA5 HIS A 151 ? ARG A 155 ? HIS A 143 ARG A 147 5 ? 5  
HELX_P HELX_P6  AA6 ASN A 278 ? ALA A 284 ? ASN A 270 ALA A 276 1 ? 7  
HELX_P HELX_P7  AA7 SER A 308 ? VAL A 312 ? SER A 300 VAL A 304 5 ? 5  
HELX_P HELX_P8  AA8 SER A 355 ? GLY A 366 ? SER A 347 GLY A 358 1 ? 12 
HELX_P HELX_P9  AA9 ASN A 405 ? MET A 408 ? ASN A 397 MET A 400 5 ? 4  
HELX_P HELX_P10 AB1 ASP A 486 ? ASN A 488 ? ASP A 478 ASN A 480 5 ? 3  
HELX_P HELX_P11 AB2 ARG A 498 ? PHE A 500 ? ARG A 490 PHE A 492 5 ? 3  
HELX_P HELX_P12 AB3 GLU A 525 ? THR A 527 ? GLU A 517 THR A 519 5 ? 3  
HELX_P HELX_P13 AB4 PRO A 546 ? SER A 550 ? PRO A 538 SER A 542 5 ? 5  
HELX_P HELX_P14 AB5 HIS B 34  ? LEU B 39  ? HIS B 26  LEU B 31  5 ? 6  
HELX_P HELX_P15 AB6 TYR B 93  ? GLU B 97  ? TYR B 85  GLU B 89  5 ? 5  
HELX_P HELX_P16 AB7 THR B 127 ? ARG B 137 ? THR B 119 ARG B 129 1 ? 11 
HELX_P HELX_P17 AB8 ASN B 146 ? HIS B 150 ? ASN B 138 HIS B 142 5 ? 5  
HELX_P HELX_P18 AB9 HIS B 151 ? ARG B 155 ? HIS B 143 ARG B 147 5 ? 5  
HELX_P HELX_P19 AC1 ASN B 278 ? ALA B 284 ? ASN B 270 ALA B 276 1 ? 7  
HELX_P HELX_P20 AC2 SER B 308 ? VAL B 312 ? SER B 300 VAL B 304 5 ? 5  
HELX_P HELX_P21 AC3 SER B 355 ? ALA B 364 ? SER B 347 ALA B 356 1 ? 10 
HELX_P HELX_P22 AC4 ASN B 405 ? MET B 408 ? ASN B 397 MET B 400 5 ? 4  
HELX_P HELX_P23 AC5 ARG B 498 ? PHE B 500 ? ARG B 490 PHE B 492 5 ? 3  
HELX_P HELX_P24 AC6 GLU B 525 ? THR B 527 ? GLU B 517 THR B 519 5 ? 3  
HELX_P HELX_P25 AC7 PRO B 546 ? SER B 550 ? PRO B 538 SER B 542 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 208 NE2 ? ? ? 1_555 D FE2 . FE ? ? A HIS 200 A FE2 602 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
metalc2  metalc ? ? A HIS 259 NE2 ? ? ? 1_555 D FE2 . FE ? ? A HIS 251 A FE2 602 1_555 ? ? ? ? ? ? ? 2.246 ? ? 
metalc3  metalc ? ? A HIS 324 NE2 ? ? ? 1_555 D FE2 . FE ? ? A HIS 316 A FE2 602 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc4  metalc ? ? A HIS 518 NE2 ? ? ? 1_555 D FE2 . FE ? ? A HIS 510 A FE2 602 1_555 ? ? ? ? ? ? ? 2.181 ? ? 
metalc5  metalc ? ? D FE2 .   FE  ? ? ? 1_555 G HOH . O  ? ? A FE2 602 A HOH 733 1_555 ? ? ? ? ? ? ? 1.811 ? ? 
metalc6  metalc ? ? B HIS 208 NE2 ? ? ? 1_555 F FE2 . FE ? ? B HIS 200 B FE2 602 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc7  metalc ? ? B HIS 259 NE2 ? ? ? 1_555 F FE2 . FE ? ? B HIS 251 B FE2 602 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc8  metalc ? ? B HIS 324 NE2 ? ? ? 1_555 F FE2 . FE ? ? B HIS 316 B FE2 602 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc9  metalc ? ? B HIS 518 NE2 ? ? ? 1_555 F FE2 . FE ? ? B HIS 510 B FE2 602 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
metalc10 metalc ? ? F FE2 .   FE  ? ? ? 1_555 H HOH . O  ? ? B FE2 602 B HOH 899 1_555 ? ? ? ? ? ? ? 1.745 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 208 ? A HIS 200 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 NE2 ? A HIS 259 ? A HIS 251 ? 1_555 91.0  ? 
2  NE2 ? A HIS 208 ? A HIS 200 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 NE2 ? A HIS 324 ? A HIS 316 ? 1_555 102.2 ? 
3  NE2 ? A HIS 259 ? A HIS 251 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 NE2 ? A HIS 324 ? A HIS 316 ? 1_555 91.7  ? 
4  NE2 ? A HIS 208 ? A HIS 200 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 NE2 ? A HIS 518 ? A HIS 510 ? 1_555 90.3  ? 
5  NE2 ? A HIS 259 ? A HIS 251 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 NE2 ? A HIS 518 ? A HIS 510 ? 1_555 177.2 ? 
6  NE2 ? A HIS 324 ? A HIS 316 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 NE2 ? A HIS 518 ? A HIS 510 ? 1_555 90.4  ? 
7  NE2 ? A HIS 208 ? A HIS 200 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 O   ? G HOH .   ? A HOH 733 ? 1_555 138.5 ? 
8  NE2 ? A HIS 259 ? A HIS 251 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 O   ? G HOH .   ? A HOH 733 ? 1_555 89.6  ? 
9  NE2 ? A HIS 324 ? A HIS 316 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 O   ? G HOH .   ? A HOH 733 ? 1_555 119.2 ? 
10 NE2 ? A HIS 518 ? A HIS 510 ? 1_555 FE ? D FE2 . ? A FE2 602 ? 1_555 O   ? G HOH .   ? A HOH 733 ? 1_555 87.8  ? 
11 NE2 ? B HIS 208 ? B HIS 200 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 NE2 ? B HIS 259 ? B HIS 251 ? 1_555 92.0  ? 
12 NE2 ? B HIS 208 ? B HIS 200 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 NE2 ? B HIS 324 ? B HIS 316 ? 1_555 104.6 ? 
13 NE2 ? B HIS 259 ? B HIS 251 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 NE2 ? B HIS 324 ? B HIS 316 ? 1_555 91.6  ? 
14 NE2 ? B HIS 208 ? B HIS 200 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 NE2 ? B HIS 518 ? B HIS 510 ? 1_555 90.8  ? 
15 NE2 ? B HIS 259 ? B HIS 251 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 NE2 ? B HIS 518 ? B HIS 510 ? 1_555 176.7 ? 
16 NE2 ? B HIS 324 ? B HIS 316 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 NE2 ? B HIS 518 ? B HIS 510 ? 1_555 89.4  ? 
17 NE2 ? B HIS 208 ? B HIS 200 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 O   ? H HOH .   ? B HOH 899 ? 1_555 144.2 ? 
18 NE2 ? B HIS 259 ? B HIS 251 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 O   ? H HOH .   ? B HOH 899 ? 1_555 89.5  ? 
19 NE2 ? B HIS 324 ? B HIS 316 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 O   ? H HOH .   ? B HOH 899 ? 1_555 111.1 ? 
20 NE2 ? B HIS 518 ? B HIS 510 ? 1_555 FE ? F FE2 . ? B FE2 602 ? 1_555 O   ? H HOH .   ? B HOH 899 ? 1_555 87.2  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 5  ? 
AA3 ? 5  ? 
AA4 ? 4  ? 
AA5 ? 4  ? 
AA6 ? 3  ? 
AA7 ? 4  ? 
AA8 ? 4  ? 
AA9 ? 4  ? 
AB1 ? 5  ? 
AB2 ? 5  ? 
AB3 ? 4  ? 
AB4 ? 4  ? 
AB5 ? 3  ? 
AB6 ? 4  ? 
AB7 ? 4  ? 
AB8 ? 4  ? 
# 
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  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA1 6 7  ? anti-parallel 
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA4 1 2  ? anti-parallel 
AA4 2 3  ? anti-parallel 
AA4 3 4  ? anti-parallel 
AA5 1 2  ? anti-parallel 
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA7 1 2  ? anti-parallel 
AA7 2 3  ? anti-parallel 
AA7 3 4  ? anti-parallel 
AA8 1 2  ? anti-parallel 
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AB1 1 2  ? anti-parallel 
AB1 2 3  ? anti-parallel 
AB1 3 4  ? anti-parallel 
AB1 4 5  ? anti-parallel 
AB2 1 2  ? anti-parallel 
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB4 1 2  ? anti-parallel 
AB4 2 3  ? anti-parallel 
AB4 3 4  ? anti-parallel 
AB5 1 2  ? anti-parallel 
AB5 2 3  ? anti-parallel 
AB6 1 2  ? anti-parallel 
AB6 2 3  ? anti-parallel 
AB6 3 4  ? anti-parallel 
AB7 1 2  ? anti-parallel 
AB7 2 3  ? anti-parallel 
AB7 3 4  ? anti-parallel 
AB8 1 2  ? anti-parallel 
AB8 2 3  ? anti-parallel 
AB8 3 4  ? 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  GLY A 519 ? PRO A 523 ? GLY A 511 PRO A 515 
AA1 2  GLY A 77  ? PRO A 84  ? GLY A 69  PRO A 76  
AA1 3  GLY A 106 ? LYS A 114 ? GLY A 98  LYS A 106 
AA1 4  LYS A 117 ? PHE A 124 ? LYS A 109 PHE A 116 
AA1 5  GLU A 59  ? ILE A 62  ? GLU A 51  ILE A 54  
AA1 6  GLU B 59  ? ILE B 62  ? GLU B 51  ILE B 54  
AA1 7  LYS B 117 ? PHE B 124 ? LYS B 109 PHE B 116 
AA1 8  GLY B 106 ? LYS B 114 ? GLY B 98  LYS B 106 
AA1 9  GLY B 77  ? PRO B 84  ? GLY B 69  PRO B 76  
AA1 10 GLY B 519 ? PRO B 523 ? GLY B 511 PRO B 515 
AA2 1  MET A 66  ? GLY A 69  ? MET A 58  GLY A 61  
AA2 2  ALA A 503 ? GLN A 508 ? ALA A 495 GLN A 500 
AA2 3  ARG A 489 ? ASP A 496 ? ARG A 481 ASP A 488 
AA2 4  GLY A 476 ? ARG A 484 ? GLY A 468 ARG A 476 
AA2 5  CYS A 457 ? ILE A 459 ? CYS A 449 ILE A 451 
AA3 1  MET A 66  ? GLY A 69  ? MET A 58  GLY A 61  
AA3 2  ALA A 503 ? GLN A 508 ? ALA A 495 GLN A 500 
AA3 3  ARG A 489 ? ASP A 496 ? ARG A 481 ASP A 488 
AA3 4  GLY A 476 ? ARG A 484 ? GLY A 468 ARG A 476 
AA3 5  VAL A 463 ? PRO A 466 ? VAL A 455 PRO A 458 
AA4 1  ASN A 165 ? HIS A 169 ? ASN A 157 HIS A 161 
AA4 2  ARG A 172 ? MET A 176 ? ARG A 164 MET A 168 
AA4 3  TYR A 183 ? MET A 185 ? TYR A 175 MET A 177 
AA4 4  THR A 192 ? TYR A 195 ? THR A 184 TYR A 187 
AA5 1  LYS A 210 ? GLN A 211 ? LYS A 202 GLN A 203 
AA5 2  LEU A 218 ? TYR A 223 ? LEU A 210 TYR A 215 
AA5 3  ASP A 232 ? VAL A 238 ? ASP A 224 VAL A 230 
AA5 4  VAL A 244 ? GLU A 251 ? VAL A 236 GLU A 243 
AA6 1  ALA A 256 ? LEU A 263 ? ALA A 248 LEU A 255 
AA6 2  TYR A 267 ? ALA A 277 ? TYR A 259 ALA A 269 
AA6 3  TRP A 289 ? TYR A 291 ? TRP A 281 TYR A 283 
AA7 1  ALA A 256 ? LEU A 263 ? ALA A 248 LEU A 255 
AA7 2  TYR A 267 ? ALA A 277 ? TYR A 259 ALA A 269 
AA7 3  THR A 298 ? PRO A 303 ? THR A 290 PRO A 295 
AA7 4  LYS A 313 ? HIS A 316 ? LYS A 305 HIS A 308 
AA8 1  THR A 325 ? GLU A 330 ? THR A 317 GLU A 322 
AA8 2  ILE A 336 ? VAL A 343 ? ILE A 328 VAL A 335 
AA8 3  ALA A 370 ? ILE A 377 ? ALA A 362 ILE A 369 
AA8 4  GLU A 391 ? LEU A 394 ? GLU A 383 LEU A 386 
AA9 1  SER A 398 ? ILE A 403 ? SER A 390 ILE A 395 
AA9 2  SER A 414 ? VAL A 419 ? SER A 406 VAL A 411 
AA9 3  GLY A 437 ? LYS A 442 ? GLY A 429 LYS A 434 
AA9 4  THR A 447 ? TYR A 452 ? THR A 439 TYR A 444 
AB1 1  MET B 66  ? GLY B 69  ? MET B 58  GLY B 61  
AB1 2  ALA B 503 ? GLN B 508 ? ALA B 495 GLN B 500 
AB1 3  ARG B 489 ? ASP B 496 ? ARG B 481 ASP B 488 
AB1 4  GLY B 476 ? ARG B 484 ? GLY B 468 ARG B 476 
AB1 5  CYS B 457 ? ILE B 459 ? CYS B 449 ILE B 451 
AB2 1  MET B 66  ? GLY B 69  ? MET B 58  GLY B 61  
AB2 2  ALA B 503 ? GLN B 508 ? ALA B 495 GLN B 500 
AB2 3  ARG B 489 ? ASP B 496 ? ARG B 481 ASP B 488 
AB2 4  GLY B 476 ? ARG B 484 ? GLY B 468 ARG B 476 
AB2 5  VAL B 463 ? PRO B 466 ? VAL B 455 PRO B 458 
AB3 1  ASN B 165 ? HIS B 169 ? ASN B 157 HIS B 161 
AB3 2  ARG B 172 ? MET B 176 ? ARG B 164 MET B 168 
AB3 3  TYR B 183 ? MET B 185 ? TYR B 175 MET B 177 
AB3 4  THR B 192 ? TYR B 195 ? THR B 184 TYR B 187 
AB4 1  LYS B 210 ? GLN B 211 ? LYS B 202 GLN B 203 
AB4 2  LEU B 218 ? TYR B 223 ? LEU B 210 TYR B 215 
AB4 3  ASP B 232 ? VAL B 238 ? ASP B 224 VAL B 230 
AB4 4  VAL B 244 ? GLU B 251 ? VAL B 236 GLU B 243 
AB5 1  ALA B 256 ? LEU B 263 ? ALA B 248 LEU B 255 
AB5 2  TYR B 267 ? ALA B 277 ? TYR B 259 ALA B 269 
AB5 3  TRP B 289 ? TYR B 291 ? TRP B 281 TYR B 283 
AB6 1  ALA B 256 ? LEU B 263 ? ALA B 248 LEU B 255 
AB6 2  TYR B 267 ? ALA B 277 ? TYR B 259 ALA B 269 
AB6 3  THR B 298 ? PRO B 303 ? THR B 290 PRO B 295 
AB6 4  LYS B 313 ? HIS B 316 ? LYS B 305 HIS B 308 
AB7 1  THR B 325 ? GLU B 330 ? THR B 317 GLU B 322 
AB7 2  ILE B 336 ? VAL B 343 ? ILE B 328 VAL B 335 
AB7 3  ALA B 370 ? ILE B 377 ? ALA B 362 ILE B 369 
AB7 4  GLU B 391 ? LEU B 394 ? GLU B 383 LEU B 386 
AB8 1  SER B 398 ? ILE B 403 ? SER B 390 ILE B 395 
AB8 2  SER B 414 ? VAL B 419 ? SER B 406 VAL B 411 
AB8 3  GLY B 437 ? LYS B 442 ? GLY B 429 LYS B 434 
AB8 4  THR B 447 ? TYR B 452 ? THR B 439 TYR B 444 
# 
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 522 ? O ILE A 514 N THR A 78  ? N THR A 70  
AA1 2 3  N ARG A 81  ? N ARG A 73  O ALA A 109 ? O ALA A 101 
AA1 3 4  N VAL A 108 ? N VAL A 100 O ARG A 123 ? O ARG A 115 
AA1 4 5  O GLN A 122 ? O GLN A 114 N GLY A 60  ? N GLY A 52  
AA1 5 6  N THR A 61  ? N THR A 53  O GLU B 59  ? O GLU B 51  
AA1 6 7  N GLY B 60  ? N GLY B 52  O GLN B 122 ? O GLN B 114 
AA1 7 8  O ARG B 121 ? O ARG B 113 N ALA B 110 ? N ALA B 102 
AA1 8 9  O ALA B 109 ? O ALA B 101 N ARG B 81  ? N ARG B 73  
AA1 9 10 N THR B 78  ? N THR B 70  O ILE B 522 ? O ILE B 514 
AA2 1 2  N MET A 66  ? N MET A 58  O GLN A 508 ? O GLN A 500 
AA2 2 3  O VAL A 504 ? O VAL A 496 N VAL A 494 ? N VAL A 486 
AA2 3 4  O ARG A 489 ? O ARG A 481 N ARG A 484 ? N ARG A 476 
AA2 4 5  O ASP A 483 ? O ASP A 475 N LEU A 458 ? N LEU A 450 
AA3 1 2  N MET A 66  ? N MET A 58  O GLN A 508 ? O GLN A 500 
AA3 2 3  O VAL A 504 ? O VAL A 496 N VAL A 494 ? N VAL A 486 
AA3 3 4  O ARG A 489 ? O ARG A 481 N ARG A 484 ? N ARG A 476 
AA3 4 5  O PHE A 477 ? O PHE A 469 N SER A 465 ? N SER A 457 
AA4 1 2  N VAL A 167 ? N VAL A 159 O LEU A 174 ? O LEU A 166 
AA4 2 3  N ALA A 175 ? N ALA A 167 O TYR A 183 ? O TYR A 175 
AA4 3 4  N GLU A 184 ? N GLU A 176 O LEU A 193 ? O LEU A 185 
AA5 1 2  N LYS A 210 ? N LYS A 202 O VAL A 219 ? O VAL A 211 
AA5 2 3  N LEU A 218 ? N LEU A 210 O VAL A 238 ? O VAL A 230 
AA5 3 4  N TYR A 235 ? N TYR A 227 O LEU A 248 ? O LEU A 240 
AA6 1 2  N ALA A 262 ? N ALA A 254 O VAL A 269 ? O VAL A 261 
AA6 2 3  N GLU A 276 ? N GLU A 268 O ALA A 290 ? O ALA A 282 
AA7 1 2  N ALA A 262 ? N ALA A 254 O VAL A 269 ? O VAL A 261 
AA7 2 3  N LEU A 272 ? N LEU A 264 O THR A 298 ? O THR A 290 
AA7 3 4  N TRP A 299 ? N TRP A 291 O TRP A 315 ? O TRP A 307 
AA8 1 2  N PHE A 329 ? N PHE A 321 O ILE A 337 ? O ILE A 329 
AA8 2 3  N ILE A 338 ? N ILE A 330 O TRP A 375 ? O TRP A 367 
AA8 3 4  N PHE A 372 ? N PHE A 364 O ILE A 393 ? O ILE A 385 
AA9 1 2  N GLN A 402 ? N GLN A 394 O PHE A 416 ? O PHE A 408 
AA9 2 3  N ILE A 417 ? N ILE A 409 O ALA A 439 ? O ALA A 431 
AA9 3 4  N LEU A 438 ? N LEU A 430 O TYR A 451 ? O TYR A 443 
AB1 1 2  N MET B 66  ? N MET B 58  O GLN B 508 ? O GLN B 500 
AB1 2 3  O VAL B 507 ? O VAL B 499 N VAL B 492 ? N VAL B 484 
AB1 3 4  O ARG B 489 ? O ARG B 481 N ARG B 484 ? N ARG B 476 
AB1 4 5  O ASP B 483 ? O ASP B 475 N LEU B 458 ? N LEU B 450 
AB2 1 2  N MET B 66  ? N MET B 58  O GLN B 508 ? O GLN B 500 
AB2 2 3  O VAL B 507 ? O VAL B 499 N VAL B 492 ? N VAL B 484 
AB2 3 4  O ARG B 489 ? O ARG B 481 N ARG B 484 ? N ARG B 476 
AB2 4 5  O PHE B 477 ? O PHE B 469 N SER B 465 ? N SER B 457 
AB3 1 2  N VAL B 167 ? N VAL B 159 O LEU B 174 ? O LEU B 166 
AB3 2 3  N ALA B 175 ? N ALA B 167 O TYR B 183 ? O TYR B 175 
AB3 3 4  N GLU B 184 ? N GLU B 176 O LEU B 193 ? O LEU B 185 
AB4 1 2  N LYS B 210 ? N LYS B 202 O VAL B 219 ? O VAL B 211 
AB4 2 3  N LEU B 218 ? N LEU B 210 O VAL B 238 ? O VAL B 230 
AB4 3 4  N VAL B 233 ? N VAL B 225 O LEU B 250 ? O LEU B 242 
AB5 1 2  N ALA B 262 ? N ALA B 254 O VAL B 269 ? O VAL B 261 
AB5 2 3  N GLU B 276 ? N GLU B 268 O ALA B 290 ? O ALA B 282 
AB6 1 2  N ALA B 262 ? N ALA B 254 O VAL B 269 ? O VAL B 261 
AB6 2 3  N LEU B 272 ? N LEU B 264 O THR B 298 ? O THR B 290 
AB6 3 4  N TRP B 299 ? N TRP B 291 O TRP B 315 ? O TRP B 307 
AB7 1 2  N PHE B 329 ? N PHE B 321 O ILE B 337 ? O ILE B 329 
AB7 2 3  N ILE B 338 ? N ILE B 330 O TRP B 375 ? O TRP B 367 
AB7 3 4  N PHE B 372 ? N PHE B 364 O ILE B 393 ? O ILE B 385 
AB8 1 2  N GLN B 402 ? N GLN B 394 O PHE B 416 ? O PHE B 408 
AB8 2 3  N ILE B 417 ? N ILE B 409 O ALA B 439 ? O ALA B 431 
AB8 3 4  N LEU B 438 ? N LEU B 430 O TYR B 451 ? O TYR B 443 
# 
_pdbx_entry_details.entry_id                   9G8A 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 49  ? ? CZ A ARG 49  ? ? NH2 A ARG 49  ? ? 117.24 120.30 -3.06  0.50 N 
2  1 NE A ARG 164 ? ? CZ A ARG 164 ? ? NH2 A ARG 164 ? ? 116.42 120.30 -3.88  0.50 N 
3  1 NE A ARG 327 ? ? CZ A ARG 327 ? ? NH1 A ARG 327 ? ? 123.63 120.30 3.33   0.50 N 
4  1 NE A ARG 327 ? ? CZ A ARG 327 ? ? NH2 A ARG 327 ? ? 117.29 120.30 -3.01  0.50 N 
5  1 NE A ARG 416 ? ? CZ A ARG 416 ? ? NH1 A ARG 416 ? ? 123.66 120.30 3.36   0.50 N 
6  1 CB A ASP 418 ? ? CA A ASP 418 ? ? C   A ASP 418 ? ? 122.96 110.40 12.56  2.00 N 
7  1 NE B ARG 48  ? ? CZ B ARG 48  ? ? NH2 B ARG 48  ? ? 117.11 120.30 -3.19  0.50 N 
8  1 NE B ARG 49  ? ? CZ B ARG 49  ? ? NH2 B ARG 49  ? ? 116.31 120.30 -3.99  0.50 N 
9  1 CD B ARG 60  ? ? NE B ARG 60  ? ? CZ  B ARG 60  ? ? 132.24 123.60 8.64   1.40 N 
10 1 CG B ARG 73  ? ? CD B ARG 73  ? ? NE  B ARG 73  ? ? 98.22  111.80 -13.58 2.10 N 
11 1 NE B ARG 73  ? ? CZ B ARG 73  ? ? NH2 B ARG 73  ? ? 117.04 120.30 -3.26  0.50 N 
12 1 CB B LEU 220 ? ? CG B LEU 220 ? ? CD2 B LEU 220 ? ? 100.37 111.00 -10.63 1.70 N 
13 1 NE B ARG 238 ? ? CZ B ARG 238 ? ? NH1 B ARG 238 ? ? 123.47 120.30 3.17   0.50 N 
14 1 NE B ARG 327 ? ? CZ B ARG 327 ? ? NH1 B ARG 327 ? ? 123.57 120.30 3.27   0.50 N 
15 1 CD B ARG 416 ? ? NE B ARG 416 ? ? CZ  B ARG 416 ? ? 132.56 123.60 8.96   1.40 N 
16 1 NE B ARG 416 ? ? CZ B ARG 416 ? ? NH1 B ARG 416 ? ? 123.88 120.30 3.58   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 ARG A 48  ? ? -112.17 -80.18  
2  1 ASP A 56  ? ? 65.78   61.84   
3  1 ASP A 77  ? ? -151.12 78.86   
4  1 HIS A 200 ? ? -118.38 55.91   
5  1 ILE A 250 ? ? -102.46 78.05   
6  1 TRP A 309 ? ? -119.93 -108.53 
7  1 ALA A 318 ? ? -70.10  -75.48  
8  1 PHE A 340 ? ? -113.73 67.21   
9  1 PHE A 343 ? ? -109.43 74.37   
10 1 SER A 405 ? ? -132.43 -49.37  
11 1 ASP A 418 ? ? -74.22  -79.28  
12 1 ILE A 509 ? ? -109.83 -92.22  
13 1 ARG B 48  ? ? -110.71 -79.05  
14 1 ASP B 56  ? ? 62.93   62.82   
15 1 HIS B 200 ? ? -118.08 56.02   
16 1 ILE B 250 ? ? -102.11 78.68   
17 1 TRP B 309 ? ? -117.47 -109.62 
18 1 ALA B 318 ? ? -69.84  -75.78  
19 1 PHE B 340 ? ? -114.67 67.42   
20 1 PHE B 343 ? ? -109.46 73.37   
21 1 ASP B 387 ? ? -90.83  57.02   
22 1 ASP B 418 ? ? -73.86  -76.62  
23 1 ILE B 509 ? ? -110.28 -94.56  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    259 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    260 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.49 
# 
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 164 ? ? 0.090 'SIDE CHAIN' 
2 1 ARG A 416 ? ? 0.129 'SIDE CHAIN' 
3 1 ARG B 416 ? ? 0.098 'SIDE CHAIN' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1137 ? 5.86 . 
2 1 O ? B HOH 1136 ? 6.00 . 
3 1 O ? B HOH 1137 ? 6.27 . 
# 
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 -7 ? A MET 1  
2  1 Y 1 A TRP -6 ? A TRP 2  
3  1 Y 1 A SER -5 ? A SER 3  
4  1 Y 1 A HIS -4 ? A HIS 4  
5  1 Y 1 A PRO -3 ? A PRO 5  
6  1 Y 1 A GLN -2 ? A GLN 6  
7  1 Y 1 A PHE -1 ? A PHE 7  
8  1 Y 1 A GLU 0  ? A GLU 8  
9  1 Y 1 A LYS 1  ? A LYS 9  
10 1 Y 1 A ALA 2  ? A ALA 10 
11 1 Y 1 A PRO 3  ? A PRO 11 
12 1 Y 1 A THR 4  ? A THR 12 
13 1 Y 1 A ALA 5  ? A ALA 13 
14 1 Y 1 A THR 6  ? A THR 14 
15 1 Y 1 A GLN 7  ? A GLN 15 
16 1 Y 1 A GLU 8  ? A GLU 16 
17 1 Y 1 A PRO 9  ? A PRO 17 
18 1 Y 1 A VAL 10 ? A VAL 18 
19 1 Y 1 A PRO 11 ? A PRO 19 
20 1 Y 1 A VAL 12 ? A VAL 20 
21 1 Y 1 A PRO 13 ? A PRO 21 
22 1 Y 1 A VAL 14 ? A VAL 22 
23 1 Y 1 A THR 15 ? A THR 23 
24 1 Y 1 A SER 16 ? A SER 24 
25 1 Y 1 A LYS 17 ? A LYS 25 
26 1 Y 1 A ALA 18 ? A ALA 26 
27 1 Y 1 A ALA 19 ? A ALA 27 
28 1 Y 1 A PRO 20 ? A PRO 28 
29 1 Y 1 A SER 21 ? A SER 29 
30 1 Y 1 A HIS 22 ? A HIS 30 
31 1 Y 1 A GLY 23 ? A GLY 31 
32 1 Y 1 B MET -7 ? B MET 1  
33 1 Y 1 B TRP -6 ? B TRP 2  
34 1 Y 1 B SER -5 ? B SER 3  
35 1 Y 1 B HIS -4 ? B HIS 4  
36 1 Y 1 B PRO -3 ? B PRO 5  
37 1 Y 1 B GLN -2 ? B GLN 6  
38 1 Y 1 B PHE -1 ? B PHE 7  
39 1 Y 1 B GLU 0  ? B GLU 8  
40 1 Y 1 B LYS 1  ? B LYS 9  
41 1 Y 1 B ALA 2  ? B ALA 10 
42 1 Y 1 B PRO 3  ? B PRO 11 
43 1 Y 1 B THR 4  ? B THR 12 
44 1 Y 1 B ALA 5  ? B ALA 13 
45 1 Y 1 B THR 6  ? B THR 14 
46 1 Y 1 B GLN 7  ? B GLN 15 
47 1 Y 1 B GLU 8  ? B GLU 16 
48 1 Y 1 B PRO 9  ? B PRO 17 
49 1 Y 1 B VAL 10 ? B VAL 18 
50 1 Y 1 B PRO 11 ? B PRO 19 
51 1 Y 1 B VAL 12 ? B VAL 20 
52 1 Y 1 B PRO 13 ? B PRO 21 
53 1 Y 1 B VAL 14 ? B VAL 22 
54 1 Y 1 B THR 15 ? B THR 23 
55 1 Y 1 B SER 16 ? B SER 24 
56 1 Y 1 B LYS 17 ? B LYS 25 
57 1 Y 1 B ALA 18 ? B ALA 26 
58 1 Y 1 B ALA 19 ? B ALA 27 
59 1 Y 1 B PRO 20 ? B PRO 28 
60 1 Y 1 B SER 21 ? B SER 29 
61 1 Y 1 B HIS 22 ? B HIS 30 
62 1 Y 1 B GLY 23 ? B GLY 31 
# 
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  
FE2 FE    FE N N 88  
GLN N     N  N N 89  
GLN CA    C  N S 90  
GLN C     C  N N 91  
GLN O     O  N N 92  
GLN CB    C  N N 93  
GLN CG    C  N N 94  
GLN CD    C  N N 95  
GLN OE1   O  N N 96  
GLN NE2   N  N N 97  
GLN OXT   O  N N 98  
GLN H     H  N N 99  
GLN H2    H  N N 100 
GLN HA    H  N N 101 
GLN HB2   H  N N 102 
GLN HB3   H  N N 103 
GLN HG2   H  N N 104 
GLN HG3   H  N N 105 
GLN HE21  H  N N 106 
GLN HE22  H  N N 107 
GLN HXT   H  N N 108 
GLU N     N  N N 109 
GLU CA    C  N S 110 
GLU C     C  N N 111 
GLU O     O  N N 112 
GLU CB    C  N N 113 
GLU CG    C  N N 114 
GLU CD    C  N N 115 
GLU OE1   O  N N 116 
GLU OE2   O  N N 117 
GLU OXT   O  N N 118 
GLU H     H  N N 119 
GLU H2    H  N N 120 
GLU HA    H  N N 121 
GLU HB2   H  N N 122 
GLU HB3   H  N N 123 
GLU HG2   H  N N 124 
GLU HG3   H  N N 125 
GLU HE2   H  N N 126 
GLU HXT   H  N N 127 
GLY N     N  N N 128 
GLY CA    C  N N 129 
GLY C     C  N N 130 
GLY O     O  N N 131 
GLY OXT   O  N N 132 
GLY H     H  N N 133 
GLY H2    H  N N 134 
GLY HA2   H  N N 135 
GLY HA3   H  N N 136 
GLY HXT   H  N N 137 
HBA "C1'" C  N N 138 
HBA "O1'" O  N N 139 
HBA C1    C  Y N 140 
HBA C2    C  Y N 141 
HBA C3    C  Y N 142 
HBA C4    C  Y N 143 
HBA C5    C  Y N 144 
HBA C6    C  Y N 145 
HBA O4    O  N N 146 
HBA "H1'" H  N N 147 
HBA H2    H  N N 148 
HBA H3    H  N N 149 
HBA H5    H  N N 150 
HBA H6    H  N N 151 
HBA HO4   H  N N 152 
HIS N     N  N N 153 
HIS CA    C  N S 154 
HIS C     C  N N 155 
HIS O     O  N N 156 
HIS CB    C  N N 157 
HIS CG    C  Y N 158 
HIS ND1   N  Y N 159 
HIS CD2   C  Y N 160 
HIS CE1   C  Y N 161 
HIS NE2   N  Y N 162 
HIS OXT   O  N N 163 
HIS H     H  N N 164 
HIS H2    H  N N 165 
HIS HA    H  N N 166 
HIS HB2   H  N N 167 
HIS HB3   H  N N 168 
HIS HD1   H  N N 169 
HIS HD2   H  N N 170 
HIS HE1   H  N N 171 
HIS HE2   H  N N 172 
HIS HXT   H  N N 173 
HOH O     O  N N 174 
HOH H1    H  N N 175 
HOH H2    H  N N 176 
ILE N     N  N N 177 
ILE CA    C  N S 178 
ILE C     C  N N 179 
ILE O     O  N N 180 
ILE CB    C  N S 181 
ILE CG1   C  N N 182 
ILE CG2   C  N N 183 
ILE CD1   C  N N 184 
ILE OXT   O  N N 185 
ILE H     H  N N 186 
ILE H2    H  N N 187 
ILE HA    H  N N 188 
ILE HB    H  N N 189 
ILE HG12  H  N N 190 
ILE HG13  H  N N 191 
ILE HG21  H  N N 192 
ILE HG22  H  N N 193 
ILE HG23  H  N N 194 
ILE HD11  H  N N 195 
ILE HD12  H  N N 196 
ILE HD13  H  N N 197 
ILE HXT   H  N N 198 
LEU N     N  N N 199 
LEU CA    C  N S 200 
LEU C     C  N N 201 
LEU O     O  N N 202 
LEU CB    C  N N 203 
LEU CG    C  N N 204 
LEU CD1   C  N N 205 
LEU CD2   C  N N 206 
LEU OXT   O  N N 207 
LEU H     H  N N 208 
LEU H2    H  N N 209 
LEU HA    H  N N 210 
LEU HB2   H  N N 211 
LEU HB3   H  N N 212 
LEU HG    H  N N 213 
LEU HD11  H  N N 214 
LEU HD12  H  N N 215 
LEU HD13  H  N N 216 
LEU HD21  H  N N 217 
LEU HD22  H  N N 218 
LEU HD23  H  N N 219 
LEU HXT   H  N N 220 
LYS N     N  N N 221 
LYS CA    C  N S 222 
LYS C     C  N N 223 
LYS O     O  N N 224 
LYS CB    C  N N 225 
LYS CG    C  N N 226 
LYS CD    C  N N 227 
LYS CE    C  N N 228 
LYS NZ    N  N N 229 
LYS OXT   O  N N 230 
LYS H     H  N N 231 
LYS H2    H  N N 232 
LYS HA    H  N N 233 
LYS HB2   H  N N 234 
LYS HB3   H  N N 235 
LYS HG2   H  N N 236 
LYS HG3   H  N N 237 
LYS HD2   H  N N 238 
LYS HD3   H  N N 239 
LYS HE2   H  N N 240 
LYS HE3   H  N N 241 
LYS HZ1   H  N N 242 
LYS HZ2   H  N N 243 
LYS HZ3   H  N N 244 
LYS HXT   H  N N 245 
MET N     N  N N 246 
MET CA    C  N S 247 
MET C     C  N N 248 
MET O     O  N N 249 
MET CB    C  N N 250 
MET CG    C  N N 251 
MET SD    S  N N 252 
MET CE    C  N N 253 
MET OXT   O  N N 254 
MET H     H  N N 255 
MET H2    H  N N 256 
MET HA    H  N N 257 
MET HB2   H  N N 258 
MET HB3   H  N N 259 
MET HG2   H  N N 260 
MET HG3   H  N N 261 
MET HE1   H  N N 262 
MET HE2   H  N N 263 
MET HE3   H  N N 264 
MET HXT   H  N N 265 
PHE N     N  N N 266 
PHE CA    C  N S 267 
PHE C     C  N N 268 
PHE O     O  N N 269 
PHE CB    C  N N 270 
PHE CG    C  Y N 271 
PHE CD1   C  Y N 272 
PHE CD2   C  Y N 273 
PHE CE1   C  Y N 274 
PHE CE2   C  Y N 275 
PHE CZ    C  Y N 276 
PHE OXT   O  N N 277 
PHE H     H  N N 278 
PHE H2    H  N N 279 
PHE HA    H  N N 280 
PHE HB2   H  N N 281 
PHE HB3   H  N N 282 
PHE HD1   H  N N 283 
PHE HD2   H  N N 284 
PHE HE1   H  N N 285 
PHE HE2   H  N N 286 
PHE HZ    H  N N 287 
PHE HXT   H  N N 288 
PRO N     N  N N 289 
PRO CA    C  N S 290 
PRO C     C  N N 291 
PRO O     O  N N 292 
PRO CB    C  N N 293 
PRO CG    C  N N 294 
PRO CD    C  N N 295 
PRO OXT   O  N N 296 
PRO H     H  N N 297 
PRO HA    H  N N 298 
PRO HB2   H  N N 299 
PRO HB3   H  N N 300 
PRO HG2   H  N N 301 
PRO HG3   H  N N 302 
PRO HD2   H  N N 303 
PRO HD3   H  N N 304 
PRO HXT   H  N N 305 
SER N     N  N N 306 
SER CA    C  N S 307 
SER C     C  N N 308 
SER O     O  N N 309 
SER CB    C  N N 310 
SER OG    O  N N 311 
SER OXT   O  N N 312 
SER H     H  N N 313 
SER H2    H  N N 314 
SER HA    H  N N 315 
SER HB2   H  N N 316 
SER HB3   H  N N 317 
SER HG    H  N N 318 
SER HXT   H  N N 319 
THR N     N  N N 320 
THR CA    C  N S 321 
THR C     C  N N 322 
THR O     O  N N 323 
THR CB    C  N R 324 
THR OG1   O  N N 325 
THR CG2   C  N N 326 
THR OXT   O  N N 327 
THR H     H  N N 328 
THR H2    H  N N 329 
THR HA    H  N N 330 
THR HB    H  N N 331 
THR HG1   H  N N 332 
THR HG21  H  N N 333 
THR HG22  H  N N 334 
THR HG23  H  N N 335 
THR HXT   H  N N 336 
TRP N     N  N N 337 
TRP CA    C  N S 338 
TRP C     C  N N 339 
TRP O     O  N N 340 
TRP CB    C  N N 341 
TRP CG    C  Y N 342 
TRP CD1   C  Y N 343 
TRP CD2   C  Y N 344 
TRP NE1   N  Y N 345 
TRP CE2   C  Y N 346 
TRP CE3   C  Y N 347 
TRP CZ2   C  Y N 348 
TRP CZ3   C  Y N 349 
TRP CH2   C  Y N 350 
TRP OXT   O  N N 351 
TRP H     H  N N 352 
TRP H2    H  N N 353 
TRP HA    H  N N 354 
TRP HB2   H  N N 355 
TRP HB3   H  N N 356 
TRP HD1   H  N N 357 
TRP HE1   H  N N 358 
TRP HE3   H  N N 359 
TRP HZ2   H  N N 360 
TRP HZ3   H  N N 361 
TRP HH2   H  N N 362 
TRP HXT   H  N N 363 
TYR N     N  N N 364 
TYR CA    C  N S 365 
TYR C     C  N N 366 
TYR O     O  N N 367 
TYR CB    C  N N 368 
TYR CG    C  Y N 369 
TYR CD1   C  Y N 370 
TYR CD2   C  Y N 371 
TYR CE1   C  Y N 372 
TYR CE2   C  Y N 373 
TYR CZ    C  Y N 374 
TYR OH    O  N N 375 
TYR OXT   O  N N 376 
TYR H     H  N N 377 
TYR H2    H  N N 378 
TYR HA    H  N N 379 
TYR HB2   H  N N 380 
TYR HB3   H  N N 381 
TYR HD1   H  N N 382 
TYR HD2   H  N N 383 
TYR HE1   H  N N 384 
TYR HE2   H  N N 385 
TYR HH    H  N N 386 
TYR HXT   H  N N 387 
VAL N     N  N N 388 
VAL CA    C  N S 389 
VAL C     C  N N 390 
VAL O     O  N N 391 
VAL CB    C  N N 392 
VAL CG1   C  N N 393 
VAL CG2   C  N N 394 
VAL OXT   O  N N 395 
VAL H     H  N N 396 
VAL H2    H  N N 397 
VAL HA    H  N N 398 
VAL HB    H  N N 399 
VAL HG11  H  N N 400 
VAL HG12  H  N N 401 
VAL HG13  H  N N 402 
VAL HG21  H  N N 403 
VAL HG22  H  N N 404 
VAL HG23  H  N N 405 
VAL HXT   H  N N 406 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA    sing N N 1   
ALA N     H     sing N N 2   
ALA N     H2    sing N N 3   
ALA CA    C     sing N N 4   
ALA CA    CB    sing N N 5   
ALA CA    HA    sing N N 6   
ALA C     O     doub N N 7   
ALA C     OXT   sing N N 8   
ALA CB    HB1   sing N N 9   
ALA CB    HB2   sing N N 10  
ALA CB    HB3   sing N N 11  
ALA OXT   HXT   sing N N 12  
ARG N     CA    sing N N 13  
ARG N     H     sing N N 14  
ARG N     H2    sing N N 15  
ARG CA    C     sing N N 16  
ARG CA    CB    sing N N 17  
ARG CA    HA    sing N N 18  
ARG C     O     doub N N 19  
ARG C     OXT   sing N N 20  
ARG CB    CG    sing N N 21  
ARG CB    HB2   sing N N 22  
ARG CB    HB3   sing N N 23  
ARG CG    CD    sing N N 24  
ARG CG    HG2   sing N N 25  
ARG CG    HG3   sing N N 26  
ARG CD    NE    sing N N 27  
ARG CD    HD2   sing N N 28  
ARG CD    HD3   sing N N 29  
ARG NE    CZ    sing N N 30  
ARG NE    HE    sing N N 31  
ARG CZ    NH1   sing N N 32  
ARG CZ    NH2   doub N N 33  
ARG NH1   HH11  sing N N 34  
ARG NH1   HH12  sing N N 35  
ARG NH2   HH21  sing N N 36  
ARG NH2   HH22  sing N N 37  
ARG OXT   HXT   sing N N 38  
ASN N     CA    sing N N 39  
ASN N     H     sing N N 40  
ASN N     H2    sing N N 41  
ASN CA    C     sing N N 42  
ASN CA    CB    sing N N 43  
ASN CA    HA    sing N N 44  
ASN C     O     doub N N 45  
ASN C     OXT   sing N N 46  
ASN CB    CG    sing N N 47  
ASN CB    HB2   sing N N 48  
ASN CB    HB3   sing N N 49  
ASN CG    OD1   doub N N 50  
ASN CG    ND2   sing N N 51  
ASN ND2   HD21  sing N N 52  
ASN ND2   HD22  sing N N 53  
ASN OXT   HXT   sing N N 54  
ASP N     CA    sing N N 55  
ASP N     H     sing N N 56  
ASP N     H2    sing N N 57  
ASP CA    C     sing N N 58  
ASP CA    CB    sing N N 59  
ASP CA    HA    sing N N 60  
ASP C     O     doub N N 61  
ASP C     OXT   sing N N 62  
ASP CB    CG    sing N N 63  
ASP CB    HB2   sing N N 64  
ASP CB    HB3   sing N N 65  
ASP CG    OD1   doub N N 66  
ASP CG    OD2   sing N N 67  
ASP OD2   HD2   sing N N 68  
ASP OXT   HXT   sing N N 69  
CYS N     CA    sing N N 70  
CYS N     H     sing N N 71  
CYS N     H2    sing N N 72  
CYS CA    C     sing N N 73  
CYS CA    CB    sing N N 74  
CYS CA    HA    sing N N 75  
CYS C     O     doub N N 76  
CYS C     OXT   sing N N 77  
CYS CB    SG    sing N N 78  
CYS CB    HB2   sing N N 79  
CYS CB    HB3   sing N N 80  
CYS SG    HG    sing N N 81  
CYS OXT   HXT   sing N N 82  
GLN N     CA    sing N N 83  
GLN N     H     sing N N 84  
GLN N     H2    sing N N 85  
GLN CA    C     sing N N 86  
GLN CA    CB    sing N N 87  
GLN CA    HA    sing N N 88  
GLN C     O     doub N N 89  
GLN C     OXT   sing N N 90  
GLN CB    CG    sing N N 91  
GLN CB    HB2   sing N N 92  
GLN CB    HB3   sing N N 93  
GLN CG    CD    sing N N 94  
GLN CG    HG2   sing N N 95  
GLN CG    HG3   sing N N 96  
GLN CD    OE1   doub N N 97  
GLN CD    NE2   sing N N 98  
GLN NE2   HE21  sing N N 99  
GLN NE2   HE22  sing N N 100 
GLN OXT   HXT   sing N N 101 
GLU N     CA    sing N N 102 
GLU N     H     sing N N 103 
GLU N     H2    sing N N 104 
GLU CA    C     sing N N 105 
GLU CA    CB    sing N N 106 
GLU CA    HA    sing N N 107 
GLU C     O     doub N N 108 
GLU C     OXT   sing N N 109 
GLU CB    CG    sing N N 110 
GLU CB    HB2   sing N N 111 
GLU CB    HB3   sing N N 112 
GLU CG    CD    sing N N 113 
GLU CG    HG2   sing N N 114 
GLU CG    HG3   sing N N 115 
GLU CD    OE1   doub N N 116 
GLU CD    OE2   sing N N 117 
GLU OE2   HE2   sing N N 118 
GLU OXT   HXT   sing N N 119 
GLY N     CA    sing N N 120 
GLY N     H     sing N N 121 
GLY N     H2    sing N N 122 
GLY CA    C     sing N N 123 
GLY CA    HA2   sing N N 124 
GLY CA    HA3   sing N N 125 
GLY C     O     doub N N 126 
GLY C     OXT   sing N N 127 
GLY OXT   HXT   sing N N 128 
HBA "C1'" "O1'" doub N N 129 
HBA "C1'" C1    sing N N 130 
HBA "C1'" "H1'" sing N N 131 
HBA C1    C2    sing Y N 132 
HBA C1    C6    doub Y N 133 
HBA C2    C3    doub Y N 134 
HBA C2    H2    sing N N 135 
HBA C3    C4    sing Y N 136 
HBA C3    H3    sing N N 137 
HBA C4    C5    doub Y N 138 
HBA C4    O4    sing N N 139 
HBA C5    C6    sing Y N 140 
HBA C5    H5    sing N N 141 
HBA C6    H6    sing N N 142 
HBA O4    HO4   sing N N 143 
HIS N     CA    sing N N 144 
HIS N     H     sing N N 145 
HIS N     H2    sing N N 146 
HIS CA    C     sing N N 147 
HIS CA    CB    sing N N 148 
HIS CA    HA    sing N N 149 
HIS C     O     doub N N 150 
HIS C     OXT   sing N N 151 
HIS CB    CG    sing N N 152 
HIS CB    HB2   sing N N 153 
HIS CB    HB3   sing N N 154 
HIS CG    ND1   sing Y N 155 
HIS CG    CD2   doub Y N 156 
HIS ND1   CE1   doub Y N 157 
HIS ND1   HD1   sing N N 158 
HIS CD2   NE2   sing Y N 159 
HIS CD2   HD2   sing N N 160 
HIS CE1   NE2   sing Y N 161 
HIS CE1   HE1   sing N N 162 
HIS NE2   HE2   sing N N 163 
HIS OXT   HXT   sing N N 164 
HOH O     H1    sing N N 165 
HOH O     H2    sing N N 166 
ILE N     CA    sing N N 167 
ILE N     H     sing N N 168 
ILE N     H2    sing N N 169 
ILE CA    C     sing N N 170 
ILE CA    CB    sing N N 171 
ILE CA    HA    sing N N 172 
ILE C     O     doub N N 173 
ILE C     OXT   sing N N 174 
ILE CB    CG1   sing N N 175 
ILE CB    CG2   sing N N 176 
ILE CB    HB    sing N N 177 
ILE CG1   CD1   sing N N 178 
ILE CG1   HG12  sing N N 179 
ILE CG1   HG13  sing N N 180 
ILE CG2   HG21  sing N N 181 
ILE CG2   HG22  sing N N 182 
ILE CG2   HG23  sing N N 183 
ILE CD1   HD11  sing N N 184 
ILE CD1   HD12  sing N N 185 
ILE CD1   HD13  sing N N 186 
ILE OXT   HXT   sing N N 187 
LEU N     CA    sing N N 188 
LEU N     H     sing N N 189 
LEU N     H2    sing N N 190 
LEU CA    C     sing N N 191 
LEU CA    CB    sing N N 192 
LEU CA    HA    sing N N 193 
LEU C     O     doub N N 194 
LEU C     OXT   sing N N 195 
LEU CB    CG    sing N N 196 
LEU CB    HB2   sing N N 197 
LEU CB    HB3   sing N N 198 
LEU CG    CD1   sing N N 199 
LEU CG    CD2   sing N N 200 
LEU CG    HG    sing N N 201 
LEU CD1   HD11  sing N N 202 
LEU CD1   HD12  sing N N 203 
LEU CD1   HD13  sing N N 204 
LEU CD2   HD21  sing N N 205 
LEU CD2   HD22  sing N N 206 
LEU CD2   HD23  sing N N 207 
LEU OXT   HXT   sing N N 208 
LYS N     CA    sing N N 209 
LYS N     H     sing N N 210 
LYS N     H2    sing N N 211 
LYS CA    C     sing N N 212 
LYS CA    CB    sing N N 213 
LYS CA    HA    sing N N 214 
LYS C     O     doub N N 215 
LYS C     OXT   sing N N 216 
LYS CB    CG    sing N N 217 
LYS CB    HB2   sing N N 218 
LYS CB    HB3   sing N N 219 
LYS CG    CD    sing N N 220 
LYS CG    HG2   sing N N 221 
LYS CG    HG3   sing N N 222 
LYS CD    CE    sing N N 223 
LYS CD    HD2   sing N N 224 
LYS CD    HD3   sing N N 225 
LYS CE    NZ    sing N N 226 
LYS CE    HE2   sing N N 227 
LYS CE    HE3   sing N N 228 
LYS NZ    HZ1   sing N N 229 
LYS NZ    HZ2   sing N N 230 
LYS NZ    HZ3   sing N N 231 
LYS OXT   HXT   sing N N 232 
MET N     CA    sing N N 233 
MET N     H     sing N N 234 
MET N     H2    sing N N 235 
MET CA    C     sing N N 236 
MET CA    CB    sing N N 237 
MET CA    HA    sing N N 238 
MET C     O     doub N N 239 
MET C     OXT   sing N N 240 
MET CB    CG    sing N N 241 
MET CB    HB2   sing N N 242 
MET CB    HB3   sing N N 243 
MET CG    SD    sing N N 244 
MET CG    HG2   sing N N 245 
MET CG    HG3   sing N N 246 
MET SD    CE    sing N N 247 
MET CE    HE1   sing N N 248 
MET CE    HE2   sing N N 249 
MET CE    HE3   sing N N 250 
MET OXT   HXT   sing N N 251 
PHE N     CA    sing N N 252 
PHE N     H     sing N N 253 
PHE N     H2    sing N N 254 
PHE CA    C     sing N N 255 
PHE CA    CB    sing N N 256 
PHE CA    HA    sing N N 257 
PHE C     O     doub N N 258 
PHE C     OXT   sing N N 259 
PHE CB    CG    sing N N 260 
PHE CB    HB2   sing N N 261 
PHE CB    HB3   sing N N 262 
PHE CG    CD1   doub Y N 263 
PHE CG    CD2   sing Y N 264 
PHE CD1   CE1   sing Y N 265 
PHE CD1   HD1   sing N N 266 
PHE CD2   CE2   doub Y N 267 
PHE CD2   HD2   sing N N 268 
PHE CE1   CZ    doub Y N 269 
PHE CE1   HE1   sing N N 270 
PHE CE2   CZ    sing Y N 271 
PHE CE2   HE2   sing N N 272 
PHE CZ    HZ    sing N N 273 
PHE OXT   HXT   sing N N 274 
PRO N     CA    sing N N 275 
PRO N     CD    sing N N 276 
PRO N     H     sing N N 277 
PRO CA    C     sing N N 278 
PRO CA    CB    sing N N 279 
PRO CA    HA    sing N N 280 
PRO C     O     doub N N 281 
PRO C     OXT   sing N N 282 
PRO CB    CG    sing N N 283 
PRO CB    HB2   sing N N 284 
PRO CB    HB3   sing N N 285 
PRO CG    CD    sing N N 286 
PRO CG    HG2   sing N N 287 
PRO CG    HG3   sing N N 288 
PRO CD    HD2   sing N N 289 
PRO CD    HD3   sing N N 290 
PRO OXT   HXT   sing N N 291 
SER N     CA    sing N N 292 
SER N     H     sing N N 293 
SER N     H2    sing N N 294 
SER CA    C     sing N N 295 
SER CA    CB    sing N N 296 
SER CA    HA    sing N N 297 
SER C     O     doub N N 298 
SER C     OXT   sing N N 299 
SER CB    OG    sing N N 300 
SER CB    HB2   sing N N 301 
SER CB    HB3   sing N N 302 
SER OG    HG    sing N N 303 
SER OXT   HXT   sing N N 304 
THR N     CA    sing N N 305 
THR N     H     sing N N 306 
THR N     H2    sing N N 307 
THR CA    C     sing N N 308 
THR CA    CB    sing N N 309 
THR CA    HA    sing N N 310 
THR C     O     doub N N 311 
THR C     OXT   sing N N 312 
THR CB    OG1   sing N N 313 
THR CB    CG2   sing N N 314 
THR CB    HB    sing N N 315 
THR OG1   HG1   sing N N 316 
THR CG2   HG21  sing N N 317 
THR CG2   HG22  sing N N 318 
THR CG2   HG23  sing N N 319 
THR OXT   HXT   sing N N 320 
TRP N     CA    sing N N 321 
TRP N     H     sing N N 322 
TRP N     H2    sing N N 323 
TRP CA    C     sing N N 324 
TRP CA    CB    sing N N 325 
TRP CA    HA    sing N N 326 
TRP C     O     doub N N 327 
TRP C     OXT   sing N N 328 
TRP CB    CG    sing N N 329 
TRP CB    HB2   sing N N 330 
TRP CB    HB3   sing N N 331 
TRP CG    CD1   doub Y N 332 
TRP CG    CD2   sing Y N 333 
TRP CD1   NE1   sing Y N 334 
TRP CD1   HD1   sing N N 335 
TRP CD2   CE2   doub Y N 336 
TRP CD2   CE3   sing Y N 337 
TRP NE1   CE2   sing Y N 338 
TRP NE1   HE1   sing N N 339 
TRP CE2   CZ2   sing Y N 340 
TRP CE3   CZ3   doub Y N 341 
TRP CE3   HE3   sing N N 342 
TRP CZ2   CH2   doub Y N 343 
TRP CZ2   HZ2   sing N N 344 
TRP CZ3   CH2   sing Y N 345 
TRP CZ3   HZ3   sing N N 346 
TRP CH2   HH2   sing N N 347 
TRP OXT   HXT   sing N N 348 
TYR N     CA    sing N N 349 
TYR N     H     sing N N 350 
TYR N     H2    sing N N 351 
TYR CA    C     sing N N 352 
TYR CA    CB    sing N N 353 
TYR CA    HA    sing N N 354 
TYR C     O     doub N N 355 
TYR C     OXT   sing N N 356 
TYR CB    CG    sing N N 357 
TYR CB    HB2   sing N N 358 
TYR CB    HB3   sing N N 359 
TYR CG    CD1   doub Y N 360 
TYR CG    CD2   sing Y N 361 
TYR CD1   CE1   sing Y N 362 
TYR CD1   HD1   sing N N 363 
TYR CD2   CE2   doub Y N 364 
TYR CD2   HD2   sing N N 365 
TYR CE1   CZ    doub Y N 366 
TYR CE1   HE1   sing N N 367 
TYR CE2   CZ    sing Y N 368 
TYR CE2   HE2   sing N N 369 
TYR CZ    OH    sing N N 370 
TYR OH    HH    sing N N 371 
TYR OXT   HXT   sing N N 372 
VAL N     CA    sing N N 373 
VAL N     H     sing N N 374 
VAL N     H2    sing N N 375 
VAL CA    C     sing N N 376 
VAL CA    CB    sing N N 377 
VAL CA    HA    sing N N 378 
VAL C     O     doub N N 379 
VAL C     OXT   sing N N 380 
VAL CB    CG1   sing N N 381 
VAL CB    CG2   sing N N 382 
VAL CB    HB    sing N N 383 
VAL CG1   HG11  sing N N 384 
VAL CG1   HG12  sing N N 385 
VAL CG1   HG13  sing N N 386 
VAL CG2   HG21  sing N N 387 
VAL CG2   HG22  sing N N 388 
VAL CG2   HG23  sing N N 389 
VAL OXT   HXT   sing N N 390 
# 
_pdbx_audit_support.funding_organization   'Austrian Science Fund' 
_pdbx_audit_support.country                Austria 
_pdbx_audit_support.grant_number           P33687 
_pdbx_audit_support.ordinal                1 
# 
_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                    9G8A 
_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]   0.013921 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003600 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011932 
_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]   0.010527 
_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 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512 0.2156   
FE 26 26 11.7738 4.7611  7.3600 0.3072  3.5235 15.3535 2.3054 76.8805 1.3245   
N  7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826  -11.5379 
O  8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089 0.2508   
S  16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720 1.0182   
# 
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     . TYR A 1 32  ? 3.059   -18.971 18.147  1 52.275  ? 24   TYR A N     1 
ATOM   2    C  CA    . TYR A 1 32  ? 2.464   -17.853 17.364  1 52.252  ? 24   TYR A CA    1 
ATOM   3    C  C     . TYR A 1 32  ? 3.123   -16.534 17.768  1 53.664  ? 24   TYR A C     1 
ATOM   4    O  O     . TYR A 1 32  ? 3.202   -16.204 18.954  1 54.372  ? 24   TYR A O     1 
ATOM   5    C  CB    . TYR A 1 32  ? 0.931   -17.747 17.44   1 52.387  ? 24   TYR A CB    1 
ATOM   6    C  CG    . TYR A 1 32  ? 0.312   -16.669 16.548  1 54.731  ? 24   TYR A CG    1 
ATOM   7    C  CD1   . TYR A 1 32  ? 0.152   -16.891 15.165  1 52.907  ? 24   TYR A CD1   1 
ATOM   8    C  CD2   . TYR A 1 32  ? -0.11   -15.426 17.073  1 48.398  ? 24   TYR A CD2   1 
ATOM   9    C  CE1   . TYR A 1 32  ? -0.397  -15.912 14.334  1 51.85   ? 24   TYR A CE1   1 
ATOM   10   C  CE2   . TYR A 1 32  ? -0.653  -14.439 16.247  1 45.254  ? 24   TYR A CE2   1 
ATOM   11   C  CZ    . TYR A 1 32  ? -0.806  -14.692 14.88   1 48.193  ? 24   TYR A CZ    1 
ATOM   12   O  OH    . TYR A 1 32  ? -1.36   -13.757 14.052  1 42.383  ? 24   TYR A OH    1 
ATOM   13   N  N     . VAL A 1 33  ? 3.563   -15.798 16.735  1 48.481  ? 25   VAL A N     1 
ATOM   14   C  CA    . VAL A 1 33  ? 4.038   -14.417 16.779  1 45.13   ? 25   VAL A CA    1 
ATOM   15   C  C     . VAL A 1 33  ? 3.21    -13.636 15.748  1 45.609  ? 25   VAL A C     1 
ATOM   16   O  O     . VAL A 1 33  ? 3.125   -14.056 14.579  1 47.312  ? 25   VAL A O     1 
ATOM   17   C  CB    . VAL A 1 33  ? 5.567   -14.245 16.551  1 43.659  ? 25   VAL A CB    1 
ATOM   18   C  CG1   . VAL A 1 33  ? 6.043   -12.808 16.768  1 41.842  ? 25   VAL A CG1   1 
ATOM   19   C  CG2   . VAL A 1 33  ? 6.436   -15.188 17.393  1 41.586  ? 25   VAL A CG2   1 
ATOM   20   N  N     . HIS A 1 34  ? 2.612   -12.503 16.183  1 35.734  ? 26   HIS A N     1 
ATOM   21   C  CA    . HIS A 1 34  ? 1.918   -11.566 15.303  1 32.494  ? 26   HIS A CA    1 
ATOM   22   C  C     . HIS A 1 34  ? 2.908   -10.908 14.333  1 29.323  ? 26   HIS A C     1 
ATOM   23   O  O     . HIS A 1 34  ? 3.891   -10.336 14.803  1 26.997  ? 26   HIS A O     1 
ATOM   24   C  CB    . HIS A 1 34  ? 1.046   -10.541 16.041  1 31.93   ? 26   HIS A CB    1 
ATOM   25   C  CG    . HIS A 1 34  ? 0.011   -9.903  15.156  1 33.03   ? 26   HIS A CG    1 
ATOM   26   N  ND1   . HIS A 1 34  ? 0.28    -9.038  14.108  1 31.717  ? 26   HIS A ND1   1 
ATOM   27   C  CD2   . HIS A 1 34  ? -1.32   -10.071 15.158  1 32.557  ? 26   HIS A CD2   1 
ATOM   28   C  CE1   . HIS A 1 34  ? -0.857  -8.692  13.519  1 31.996  ? 26   HIS A CE1   1 
ATOM   29   N  NE2   . HIS A 1 34  ? -1.846  -9.278  14.161  1 31.215  ? 26   HIS A NE2   1 
ATOM   30   N  N     . PRO A 1 35  ? 2.699   -10.992 12.98   1 28.732  ? 27   PRO A N     1 
ATOM   31   C  CA    . PRO A 1 35  ? 3.619   -10.427 11.987  1 28.467  ? 27   PRO A CA    1 
ATOM   32   C  C     . PRO A 1 35  ? 3.979   -8.955  12.185  1 26.999  ? 27   PRO A C     1 
ATOM   33   O  O     . PRO A 1 35  ? 5.123   -8.602  11.921  1 26.12   ? 27   PRO A O     1 
ATOM   34   C  CB    . PRO A 1 35  ? 2.981   -10.776 10.636  1 27.688  ? 27   PRO A CB    1 
ATOM   35   C  CG    . PRO A 1 35  ? 2.28    -12.075 10.991  1 28.587  ? 27   PRO A CG    1 
ATOM   36   C  CD    . PRO A 1 35  ? 1.617   -11.726 12.294  1 28.307  ? 27   PRO A CD    1 
ATOM   37   N  N     . THR A 1 36  ? 3.03    -8.143  12.7    1 27.425  ? 28   THR A N     1 
ATOM   38   C  CA    . THR A 1 36  ? 3.224   -6.708  12.936  1 27.642  ? 28   THR A CA    1 
ATOM   39   C  C     . THR A 1 36  ? 4.099   -6.446  14.173  1 26.933  ? 28   THR A C     1 
ATOM   40   O  O     . THR A 1 36  ? 4.669   -5.364  14.291  1 25.762  ? 28   THR A O     1 
ATOM   41   C  CB    . THR A 1 36  ? 1.925   -5.894  12.975  1 28.947  ? 28   THR A CB    1 
ATOM   42   O  OG1   . THR A 1 36  ? 1.173   -6.324  14.096  1 30.56   ? 28   THR A OG1   1 
ATOM   43   C  CG2   . THR A 1 36  ? 1.03    -6.037  11.757  1 30.095  ? 28   THR A CG2   1 
ATOM   44   N  N     . ASP A 1 37  ? 4.192   -7.431  15.087  1 27.305  ? 29   ASP A N     1 
ATOM   45   C  CA    . ASP A 1 37  ? 4.939   -7.346  16.335  1 28.619  ? 29   ASP A CA    1 
ATOM   46   C  C     . ASP A 1 37  ? 6.455   -7.418  16.145  1 32.747  ? 29   ASP A C     1 
ATOM   47   O  O     . ASP A 1 37  ? 7.173   -6.955  17.033  1 36.068  ? 29   ASP A O     1 
ATOM   48   C  CB    . ASP A 1 37  ? 4.35    -8.247  17.406  1 27.198  ? 29   ASP A CB    1 
ATOM   49   C  CG    . ASP A 1 37  ? 3.007   -7.814  17.982  1 26.814  ? 29   ASP A CG    1 
ATOM   50   O  OD1   . ASP A 1 37  ? 2.532   -6.691  17.661  1 28.153  ? 29   ASP A OD1   1 
ATOM   51   O  OD2   . ASP A 1 37  ? 2.447   -8.598  18.769  1 25.467  ? 29   ASP A OD2   1 
ATOM   52   N  N     . ILE A 1 38  ? 6.917   -7.954  15.001  1 34.135  ? 30   ILE A N     1 
ATOM   53   C  CA    . ILE A 1 38  ? 8.335   -8.006  14.639  1 35.156  ? 30   ILE A CA    1 
ATOM   54   C  C     . ILE A 1 38  ? 8.772   -6.771  13.826  1 32.941  ? 30   ILE A C     1 
ATOM   55   O  O     . ILE A 1 38  ? 9.94    -6.691  13.435  1 34.033  ? 30   ILE A O     1 
ATOM   56   C  CB    . ILE A 1 38  ? 8.771   -9.365  14.028  1 36.982  ? 30   ILE A CB    1 
ATOM   57   C  CG1   . ILE A 1 38  ? 8.209   -9.616  12.609  1 38.09   ? 30   ILE A CG1   1 
ATOM   58   C  CG2   . ILE A 1 38  ? 8.53    -10.539 14.986  1 35.239  ? 30   ILE A CG2   1 
ATOM   59   C  CD1   . ILE A 1 38  ? 9.237   -10.098 11.601  1 41.61   ? 30   ILE A CD1   1 
ATOM   60   N  N     . LEU A 1 39  ? 7.845   -5.825  13.558  1 28.519  ? 31   LEU A N     1 
ATOM   61   C  CA    . LEU A 1 39  ? 8.169   -4.539  12.952  1 27.175  ? 31   LEU A CA    1 
ATOM   62   C  C     . LEU A 1 39  ? 8.919   -3.675  13.973  1 26.641  ? 31   LEU A C     1 
ATOM   63   O  O     . LEU A 1 39  ? 8.473   -3.621  15.121  1 29.24   ? 31   LEU A O     1 
ATOM   64   C  CB    . LEU A 1 39  ? 6.978   -3.813  12.317  1 26.455  ? 31   LEU A CB    1 
ATOM   65   C  CG    . LEU A 1 39  ? 6.29    -4.475  11.111  1 26.43   ? 31   LEU A CG    1 
ATOM   66   C  CD1   . LEU A 1 39  ? 4.942   -3.797  10.894  1 25.974  ? 31   LEU A CD1   1 
ATOM   67   C  CD2   . LEU A 1 39  ? 7.088   -4.415  9.806   1 27.909  ? 31   LEU A CD2   1 
ATOM   68   N  N     . PRO A 1 40  ? 10.082  -3.034  13.633  1 28.641  ? 32   PRO A N     1 
ATOM   69   C  CA    . PRO A 1 40  ? 10.907  -2.318  14.619  1 28.22   ? 32   PRO A CA    1 
ATOM   70   C  C     . PRO A 1 40  ? 10.297  -1.049  15.215  1 27.625  ? 32   PRO A C     1 
ATOM   71   O  O     . PRO A 1 40  ? 9.658   -0.265  14.52   1 25.998  ? 32   PRO A O     1 
ATOM   72   C  CB    . PRO A 1 40  ? 12.216  -2.036  13.895  1 27.346  ? 32   PRO A CB    1 
ATOM   73   C  CG    . PRO A 1 40  ? 11.786  -1.983  12.432  1 29.694  ? 32   PRO A CG    1 
ATOM   74   C  CD    . PRO A 1 40  ? 10.728  -3.03   12.302  1 30.089  ? 32   PRO A CD    1 
ATOM   75   N  N     . SER A 1 41  ? 10.52   -0.901  16.523  1 29.169  ? 33   SER A N     1 
ATOM   76   C  CA    . SER A 1 41  ? 10.27   0.277   17.336  1 28.951  ? 33   SER A CA    1 
ATOM   77   C  C     . SER A 1 41  ? 11.578  1.039   17.533  1 29.834  ? 33   SER A C     1 
ATOM   78   O  O     . SER A 1 41  ? 12.638  0.422   17.666  1 35.462  ? 33   SER A O     1 
ATOM   79   C  CB    . SER A 1 41  ? 9.698   -0.157  18.67   1 31.107  ? 33   SER A CB    1 
ATOM   80   O  OG    . SER A 1 41  ? 9.541   0.932   19.575  1 27.663  ? 33   SER A OG    1 
ATOM   81   N  N     . GLY A 1 42  ? 11.464  2.377   17.602  1 29.798  ? 34   GLY A N     1 
ATOM   82   C  CA    . GLY A 1 42  ? 12.526  3.309   17.97   1 28.692  ? 34   GLY A CA    1 
ATOM   83   C  C     . GLY A 1 42  ? 12.605  3.613   19.474  1 28.943  ? 34   GLY A C     1 
ATOM   84   O  O     . GLY A 1 42  ? 13.499  4.368   19.882  1 31.397  ? 34   GLY A O     1 
ATOM   85   N  N     . TRP A 1 43  ? 11.669  3.063   20.272  1 22.517  ? 35   TRP A N     1 
ATOM   86   C  CA    . TRP A 1 43  ? 11.565  3.359   21.688  1 20.963  ? 35   TRP A CA    1 
ATOM   87   C  C     . TRP A 1 43  ? 12.613  2.568   22.459  1 23.686  ? 35   TRP A C     1 
ATOM   88   O  O     . TRP A 1 43  ? 12.723  1.356   22.222  1 22.12   ? 35   TRP A O     1 
ATOM   89   C  CB    . TRP A 1 43  ? 10.143  3.138   22.235  1 20.842  ? 35   TRP A CB    1 
ATOM   90   C  CG    . TRP A 1 43  ? 9.344   4.414   22.268  1 18.28   ? 35   TRP A CG    1 
ATOM   91   C  CD1   . TRP A 1 43  ? 8.714   5.014   21.22   1 19.018  ? 35   TRP A CD1   1 
ATOM   92   C  CD2   . TRP A 1 43  ? 9.143   5.28    23.407  1 18.147  ? 35   TRP A CD2   1 
ATOM   93   N  NE1   . TRP A 1 43  ? 8.121   6.184   21.619  1 18.18   ? 35   TRP A NE1   1 
ATOM   94   C  CE2   . TRP A 1 43  ? 8.363   6.379   22.953  1 18.204  ? 35   TRP A CE2   1 
ATOM   95   C  CE3   . TRP A 1 43  ? 9.533   5.238   24.758  1 17.563  ? 35   TRP A CE3   1 
ATOM   96   C  CZ2   . TRP A 1 43  ? 7.968   7.418   23.806  1 18.1    ? 35   TRP A CZ2   1 
ATOM   97   C  CZ3   . TRP A 1 43  ? 9.145   6.263   25.607  1 18.338  ? 35   TRP A CZ3   1 
ATOM   98   C  CH2   . TRP A 1 43  ? 8.394   7.352   25.127  1 18.15   ? 35   TRP A CH2   1 
ATOM   99   N  N     . PRO A 1 44  ? 13.388  3.207   23.388  1 24.469  ? 36   PRO A N     1 
ATOM   100  C  CA    . PRO A 1 44  ? 14.096  2.46    24.429  1 26.834  ? 36   PRO A CA    1 
ATOM   101  C  C     . PRO A 1 44  ? 13.14   1.92    25.491  1 26.423  ? 36   PRO A C     1 
ATOM   102  O  O     . PRO A 1 44  ? 11.952  2.295   25.498  1 25.392  ? 36   PRO A O     1 
ATOM   103  C  CB    . PRO A 1 44  ? 15.128  3.455   24.964  1 27.56   ? 36   PRO A CB    1 
ATOM   104  C  CG    . PRO A 1 44  ? 14.48   4.805   24.748  1 28.722  ? 36   PRO A CG    1 
ATOM   105  C  CD    . PRO A 1 44  ? 13.633  4.665   23.502  1 26.979  ? 36   PRO A CD    1 
ATOM   106  N  N     . THR A 1 45  ? 13.677  1.05    26.363  1 22.787  ? 37   THR A N     1 
ATOM   107  C  CA    . THR A 1 45  ? 12.949  0.554   27.523  1 23.868  ? 37   THR A CA    1 
ATOM   108  C  C     . THR A 1 45  ? 12.908  1.676   28.569  1 24.35   ? 37   THR A C     1 
ATOM   109  O  O     . THR A 1 45  ? 13.923  1.973   29.208  1 24.387  ? 37   THR A O     1 
ATOM   110  C  CB    . THR A 1 45  ? 13.514  -0.786  28.015  1 24.517  ? 37   THR A CB    1 
ATOM   111  O  OG1   . THR A 1 45  ? 13.43   -1.635  26.874  1 25.582  ? 37   THR A OG1   1 
ATOM   112  C  CG2   . THR A 1 45  ? 12.639  -1.464  29.057  1 23.498  ? 37   THR A CG2   1 
ATOM   113  N  N     . ALA A 1 46  ? 11.719  2.301   28.701  1 21.835  ? 38   ALA A N     1 
ATOM   114  C  CA    . ALA A 1 46  ? 11.442  3.366   29.665  1 20.327  ? 38   ALA A CA    1 
ATOM   115  C  C     . ALA A 1 46  ? 10.532  2.833   30.782  1 19.971  ? 38   ALA A C     1 
ATOM   116  O  O     . ALA A 1 46  ? 9.294   2.828   30.668  1 20.523  ? 38   ALA A O     1 
ATOM   117  C  CB    . ALA A 1 46  ? 10.915  4.608   28.941  1 19.963  ? 38   ALA A CB    1 
ATOM   118  N  N     . THR A 1 47  ? 11.173  2.279   31.826  1 18.994  ? 39   THR A N     1 
ATOM   119  C  CA    . THR A 1 47  ? 10.485  1.713   32.988  1 19.013  ? 39   THR A CA    1 
ATOM   120  C  C     . THR A 1 47  ? 9.947   2.85    33.876  1 18.449  ? 39   THR A C     1 
ATOM   121  O  O     . THR A 1 47  ? 10.496  3.96    33.887  1 17.185  ? 39   THR A O     1 
ATOM   122  C  CB    . THR A 1 47  ? 11.284  0.672   33.799  1 17.901  ? 39   THR A CB    1 
ATOM   123  O  OG1   . THR A 1 47  ? 12.226  1.395   34.581  1 18.686  ? 39   THR A OG1   1 
ATOM   124  C  CG2   . THR A 1 47  ? 11.932  -0.459  33.011  1 17.875  ? 39   THR A CG2   1 
ATOM   125  N  N     . ASP A 1 48  ? 8.874   2.533   34.616  1 17.622  ? 40   ASP A N     1 
ATOM   126  C  CA    . ASP A 1 48  ? 8.486   3.197   35.856  1 19.759  ? 40   ASP A CA    1 
ATOM   127  C  C     . ASP A 1 48  ? 8.948   2.339   37.05   1 19.303  ? 40   ASP A C     1 
ATOM   128  O  O     . ASP A 1 48  ? 9.518   1.25    36.856  1 19.751  ? 40   ASP A O     1 
ATOM   129  C  CB    . ASP A 1 48  ? 6.998   3.53    35.814  1 20.044  ? 40   ASP A CB    1 
ATOM   130  C  CG    . ASP A 1 48  ? 6.073   2.326   35.682  1 23.433  ? 40   ASP A CG    1 
ATOM   131  O  OD1   . ASP A 1 48  ? 6.181   1.383   36.514  1 22.484  ? 40   ASP A OD1   1 
ATOM   132  O  OD2   . ASP A 1 48  ? 5.251   2.329   34.737  1 22.25   ? 40   ASP A OD2   1 
ATOM   133  N  N     . LEU A 1 49  ? 8.673   2.811   38.287  1 18.562  ? 41   LEU A N     1 
ATOM   134  C  CA    . LEU A 1 49  ? 9.112   2.163   39.525  1 18.229  ? 41   LEU A CA    1 
ATOM   135  C  C     . LEU A 1 49  ? 8.654   0.703   39.665  1 18.17   ? 41   LEU A C     1 
ATOM   136  O  O     . LEU A 1 49  ? 9.393   -0.098  40.246  1 18.711  ? 41   LEU A O     1 
ATOM   137  C  CB    . LEU A 1 49  ? 8.91    2.989   40.803  1 17.862  ? 41   LEU A CB    1 
ATOM   138  C  CG    . LEU A 1 49  ? 9.925   4.104   41.106  1 18.257  ? 41   LEU A CG    1 
ATOM   139  C  CD1   . LEU A 1 49  ? 9.405   4.838   42.318  1 18.436  ? 41   LEU A CD1   1 
ATOM   140  C  CD2   . LEU A 1 49  ? 11.348  3.616   41.416  1 18.555  ? 41   LEU A CD2   1 
ATOM   141  N  N     . SER A 1 50  ? 7.495   0.34    39.076  1 17.605  ? 42   SER A N     1 
ATOM   142  C  CA    . SER A 1 50  ? 6.981   -1.031  39.1    1 19.232  ? 42   SER A CA    1 
ATOM   143  C  C     . SER A 1 50  ? 7.813   -2.009  38.259  1 18.503  ? 42   SER A C     1 
ATOM   144  O  O     . SER A 1 50  ? 7.671   -3.23   38.429  1 18.033  ? 42   SER A O     1 
ATOM   145  C  CB    . SER A 1 50  ? 5.517   -1.099  38.733  1 19.386  ? 42   SER A CB    1 
ATOM   146  O  OG    . SER A 1 50  ? 5.365   -0.868  37.342  1 18.254  ? 42   SER A OG    1 
ATOM   147  N  N     . GLY A 1 51  ? 8.633   -1.466  37.338  1 17.951  ? 43   GLY A N     1 
ATOM   148  C  CA    . GLY A 1 51  ? 9.319   -2.239  36.318  1 18.948  ? 43   GLY A CA    1 
ATOM   149  C  C     . GLY A 1 51  ? 8.513   -2.342  35.021  1 19.689  ? 43   GLY A C     1 
ATOM   150  O  O     . GLY A 1 51  ? 9.044   -2.842  34.035  1 20.216  ? 43   GLY A O     1 
ATOM   151  N  N     . GLY A 1 52  ? 7.232   -1.91   35.022  1 22.859  ? 44   GLY A N     1 
ATOM   152  C  CA    . GLY A 1 52  ? 6.381   -1.769  33.834  1 21.499  ? 44   GLY A CA    1 
ATOM   153  C  C     . GLY A 1 52  ? 7.022   -0.816  32.823  1 21.595  ? 44   GLY A C     1 
ATOM   154  O  O     . GLY A 1 52  ? 7.6     0.191   33.228  1 20.433  ? 44   GLY A O     1 
ATOM   155  N  N     . ALA A 1 53  ? 6.976   -1.179  31.53   1 21.243  ? 45   ALA A N     1 
ATOM   156  C  CA    . ALA A 1 53  ? 7.734   -0.478  30.494  1 22.339  ? 45   ALA A CA    1 
ATOM   157  C  C     . ALA A 1 53  ? 6.881   0.013   29.313  1 22.675  ? 45   ALA A C     1 
ATOM   158  O  O     . ALA A 1 53  ? 7.438   0.377   28.274  1 24.329  ? 45   ALA A O     1 
ATOM   159  C  CB    . ALA A 1 53  ? 8.948   -1.291  30.09   1 20.766  ? 45   ALA A CB    1 
ATOM   160  N  N     . GLN A 1 54  ? 5.549   0.089   29.49   1 20.187  ? 46   GLN A N     1 
ATOM   161  C  CA    . GLN A 1 54  ? 4.629   0.49    28.43   1 20.894  ? 46   GLN A CA    1 
ATOM   162  C  C     . GLN A 1 54  ? 4.388   2.014   28.48   1 19.197  ? 46   GLN A C     1 
ATOM   163  O  O     . GLN A 1 54  ? 3.702   2.473   29.405  1 17.932  ? 46   GLN A O     1 
ATOM   164  C  CB    . GLN A 1 54  ? 3.442   -0.477  28.392  1 23.12   ? 46   GLN A CB    1 
ATOM   165  C  CG    . GLN A 1 54  ? 2.33    -0.118  27.405  1 30.567  ? 46   GLN A CG    1 
ATOM   166  C  CD    . GLN A 1 54  ? 2.755   -0.011  25.956  1 34.033  ? 46   GLN A CD    1 
ATOM   167  O  OE1   . GLN A 1 54  ? 3.325   -0.936  25.362  1 33.126  ? 46   GLN A OE1   1 
ATOM   168  N  NE2   . GLN A 1 54  ? 2.477   1.148   25.383  1 31.715  ? 46   GLN A NE2   1 
ATOM   169  N  N     . PRO A 1 55  ? 4.89    2.825   27.498  1 17.518  ? 47   PRO A N     1 
ATOM   170  C  CA    . PRO A 1 55  ? 4.535   4.248   27.387  1 18.239  ? 47   PRO A CA    1 
ATOM   171  C  C     . PRO A 1 55  ? 3.025   4.458   27.219  1 17.467  ? 47   PRO A C     1 
ATOM   172  O  O     . PRO A 1 55  ? 2.387   3.668   26.512  1 18.285  ? 47   PRO A O     1 
ATOM   173  C  CB    . PRO A 1 55  ? 5.301   4.742   26.145  1 17.137  ? 47   PRO A CB    1 
ATOM   174  C  CG    . PRO A 1 55  ? 6.422   3.727   26.02   1 19.248  ? 47   PRO A CG    1 
ATOM   175  C  CD    . PRO A 1 55  ? 5.762   2.421   26.37   1 17.828  ? 47   PRO A CD    1 
ATOM   176  N  N     . ARG A 1 56  ? 2.475   5.47    27.914  1 16.704  ? 48   ARG A N     1 
ATOM   177  C  CA    . ARG A 1 56  ? 1.035   5.762   27.921  1 17.135  ? 48   ARG A CA    1 
ATOM   178  C  C     . ARG A 1 56  ? 0.785   7.09    27.208  1 17.137  ? 48   ARG A C     1 
ATOM   179  O  O     . ARG A 1 56  ? 0.456   7.086   26.017  1 18.098  ? 48   ARG A O     1 
ATOM   180  C  CB    . ARG A 1 56  ? 0.381   5.551   29.298  1 16.801  ? 48   ARG A CB    1 
ATOM   181  C  CG    . ARG A 1 56  ? 0.555   4.181   29.947  1 16.782  ? 48   ARG A CG    1 
ATOM   182  C  CD    . ARG A 1 56  ? -0.224  3.097   29.219  1 15.571  ? 48   ARG A CD    1 
ATOM   183  N  NE    . ARG A 1 56  ? 0.077   1.825   29.886  1 17.129  ? 48   ARG A NE    1 
ATOM   184  C  CZ    . ARG A 1 56  ? -0.387  0.62    29.577  1 18.686  ? 48   ARG A CZ    1 
ATOM   185  N  NH1   . ARG A 1 56  ? -1.223  0.433   28.553  1 19.611  ? 48   ARG A NH1   1 
ATOM   186  N  NH2   . ARG A 1 56  ? -0.011  -0.39   30.326  1 17.743  ? 48   ARG A NH2   1 
ATOM   187  N  N     . ARG A 1 57  ? 1.014   8.206   27.935  1 17.679  ? 49   ARG A N     1 
ATOM   188  C  CA    . ARG A 1 57  ? 1.326   9.545   27.422  1 17.857  ? 49   ARG A CA    1 
ATOM   189  C  C     . ARG A 1 57  ? 0.071   10.275  26.935  1 18.926  ? 49   ARG A C     1 
ATOM   190  O  O     . ARG A 1 57  ? 0.176   11.333  26.313  1 21.132  ? 49   ARG A O     1 
ATOM   191  C  CB    . ARG A 1 57  ? 2.499   9.604   26.417  1 16.881  ? 49   ARG A CB    1 
ATOM   192  C  CG    . ARG A 1 57  ? 3.743   8.762   26.686  1 16.761  ? 49   ARG A CG    1 
ATOM   193  C  CD    . ARG A 1 57  ? 4.649   8.588   25.496  1 16.936  ? 49   ARG A CD    1 
ATOM   194  N  NE    . ARG A 1 57  ? 4.068   8.045   24.264  1 16.967  ? 49   ARG A NE    1 
ATOM   195  C  CZ    . ARG A 1 57  ? 4.191   8.509   23.02   1 18.603  ? 49   ARG A CZ    1 
ATOM   196  N  NH1   . ARG A 1 57  ? 4.89    9.61    22.725  1 18.004  ? 49   ARG A NH1   1 
ATOM   197  N  NH2   . ARG A 1 57  ? 3.611   7.813   22.053  1 19.438  ? 49   ARG A NH2   1 
ATOM   198  N  N     . PHE A 1 58  ? -1.115  9.741   27.249  1 20.081  ? 50   PHE A N     1 
ATOM   199  C  CA    . PHE A 1 58  ? -2.377  10.359  26.852  1 20.718  ? 50   PHE A CA    1 
ATOM   200  C  C     . PHE A 1 58  ? -2.664  11.537  27.767  1 17.304  ? 50   PHE A C     1 
ATOM   201  O  O     . PHE A 1 58  ? -2.392  11.485  28.968  1 16.733  ? 50   PHE A O     1 
ATOM   202  C  CB    . PHE A 1 58  ? -3.579  9.419   26.709  1 23.828  ? 50   PHE A CB    1 
ATOM   203  C  CG    . PHE A 1 58  ? -3.646  8.313   27.751  1 24.519  ? 50   PHE A CG    1 
ATOM   204  C  CD1   . PHE A 1 58  ? -4.182  8.558   29.027  1 23.783  ? 50   PHE A CD1   1 
ATOM   205  C  CD2   . PHE A 1 58  ? -3.144  7.022   27.459  1 26.338  ? 50   PHE A CD2   1 
ATOM   206  C  CE1   . PHE A 1 58  ? -4.224  7.519   29.975  1 26.633  ? 50   PHE A CE1   1 
ATOM   207  C  CE2   . PHE A 1 58  ? -3.238  5.972   28.392  1 24.408  ? 50   PHE A CE2   1 
ATOM   208  C  CZ    . PHE A 1 58  ? -3.777  6.226   29.651  1 25.063  ? 50   PHE A CZ    1 
ATOM   209  N  N     . GLU A 1 59  ? -3.225  12.576  27.147  1 16.664  ? 51   GLU A N     1 
ATOM   210  C  CA    . GLU A 1 59  ? -3.721  13.757  27.829  1 16.089  ? 51   GLU A CA    1 
ATOM   211  C  C     . GLU A 1 59  ? -5.2    13.921  27.515  1 16.675  ? 51   GLU A C     1 
ATOM   212  O  O     . GLU A 1 59  ? -5.559  14.09   26.343  1 16.475  ? 51   GLU A O     1 
ATOM   213  C  CB    . GLU A 1 59  ? -2.932  15.021  27.481  1 16.118  ? 51   GLU A CB    1 
ATOM   214  C  CG    . GLU A 1 59  ? -1.453  14.922  27.853  1 16.747  ? 51   GLU A CG    1 
ATOM   215  C  CD    . GLU A 1 59  ? -0.747  16.225  27.544  1 16.312  ? 51   GLU A CD    1 
ATOM   216  O  OE1   . GLU A 1 59  ? -0.541  16.546  26.345  1 17.122  ? 51   GLU A OE1   1 
ATOM   217  O  OE2   . GLU A 1 59  ? -0.456  16.928  28.524  1 15.062  ? 51   GLU A OE2   1 
ATOM   218  N  N     . GLY A 1 60  ? -6.027  13.875  28.57   1 15.852  ? 52   GLY A N     1 
ATOM   219  C  CA    . GLY A 1 60  ? -7.453  14.158  28.428  1 14.944  ? 52   GLY A CA    1 
ATOM   220  C  C     . GLY A 1 60  ? -8.301  13.576  29.554  1 16.451  ? 52   GLY A C     1 
ATOM   221  O  O     . GLY A 1 60  ? -7.807  13.368  30.667  1 16.694  ? 52   GLY A O     1 
ATOM   222  N  N     . THR A 1 61  ? -9.591  13.344  29.241  1 16.565  ? 53   THR A N     1 
ATOM   223  C  CA    . THR A 1 61  ? -10.662 13.227  30.234  1 15.224  ? 53   THR A CA    1 
ATOM   224  C  C     . THR A 1 61  ? -11.528 12.002  29.965  1 15.726  ? 53   THR A C     1 
ATOM   225  O  O     . THR A 1 61  ? -11.652 11.577  28.807  1 15.945  ? 53   THR A O     1 
ATOM   226  C  CB    . THR A 1 61  ? -11.523 14.492  30.378  1 13.753  ? 53   THR A CB    1 
ATOM   227  O  OG1   . THR A 1 61  ? -12.139 14.766  29.126  1 14.128  ? 53   THR A OG1   1 
ATOM   228  C  CG2   . THR A 1 61  ? -10.775 15.699  30.908  1 13.475  ? 53   THR A CG2   1 
ATOM   229  N  N     . ILE A 1 62  ? -12.105 11.456  31.06   1 16.868  ? 54   ILE A N     1 
ATOM   230  C  CA    . ILE A 1 62  ? -13.349 10.68   31.037  1 17.026  ? 54   ILE A CA    1 
ATOM   231  C  C     . ILE A 1 62  ? -14.328 11.31   32.028  1 17.137  ? 54   ILE A C     1 
ATOM   232  O  O     . ILE A 1 62  ? -14.024 11.427  33.216  1 16.148  ? 54   ILE A O     1 
ATOM   233  C  CB    . ILE A 1 62  ? -13.135 9.165   31.288  1 17.088  ? 54   ILE A CB    1 
ATOM   234  C  CG1   . ILE A 1 62  ? -12.157 8.54    30.279  1 17.222  ? 54   ILE A CG1   1 
ATOM   235  C  CG2   . ILE A 1 62  ? -14.472 8.394   31.318  1 15.705  ? 54   ILE A CG2   1 
ATOM   236  C  CD1   . ILE A 1 62  ? -11.375 7.379   30.856  1 18.455  ? 54   ILE A CD1   1 
ATOM   237  N  N     . PHE A 1 63  ? -15.497 11.7    31.506  1 16.856  ? 55   PHE A N     1 
ATOM   238  C  CA    . PHE A 1 63  ? -16.621 12.165  32.305  1 17.342  ? 55   PHE A CA    1 
ATOM   239  C  C     . PHE A 1 63  ? -17.433 10.945  32.73   1 17.164  ? 55   PHE A C     1 
ATOM   240  O  O     . PHE A 1 63  ? -17.832 10.132  31.891  1 17.704  ? 55   PHE A O     1 
ATOM   241  C  CB    . PHE A 1 63  ? -17.447 13.176  31.508  1 18.44   ? 55   PHE A CB    1 
ATOM   242  C  CG    . PHE A 1 63  ? -18.576 13.849  32.275  1 19.22   ? 55   PHE A CG    1 
ATOM   243  C  CD1   . PHE A 1 63  ? -18.333 15.026  33.02   1 18.761  ? 55   PHE A CD1   1 
ATOM   244  C  CD2   . PHE A 1 63  ? -19.889 13.349  32.204  1 18.365  ? 55   PHE A CD2   1 
ATOM   245  C  CE1   . PHE A 1 63  ? -19.375 15.676  33.703  1 19.518  ? 55   PHE A CE1   1 
ATOM   246  C  CE2   . PHE A 1 63  ? -20.944 13.992  32.884  1 19.846  ? 55   PHE A CE2   1 
ATOM   247  C  CZ    . PHE A 1 63  ? -20.681 15.15   33.645  1 19.18   ? 55   PHE A CZ    1 
ATOM   248  N  N     . ASP A 1 64  ? -17.667 10.845  34.048  1 18.216  ? 56   ASP A N     1 
ATOM   249  C  CA    . ASP A 1 64  ? -18.552 9.855   34.666  1 18.305  ? 56   ASP A CA    1 
ATOM   250  C  C     . ASP A 1 64  ? -17.958 8.459   34.456  1 16.534  ? 56   ASP A C     1 
ATOM   251  O  O     . ASP A 1 64  ? -18.53  7.64    33.73   1 15.722  ? 56   ASP A O     1 
ATOM   252  C  CB    . ASP A 1 64  ? -20.021 10.121  34.326  1 19.03   ? 56   ASP A CB    1 
ATOM   253  C  CG    . ASP A 1 64  ? -21.052 9.547   35.285  1 22.193  ? 56   ASP A CG    1 
ATOM   254  O  OD1   . ASP A 1 64  ? -20.817 9.621   36.511  1 22.342  ? 56   ASP A OD1   1 
ATOM   255  O  OD2   . ASP A 1 64  ? -22.109 9.084   34.8    1 22.818  ? 56   ASP A OD2   1 
ATOM   256  N  N     . VAL A 1 65  ? -16.75  8.265   35.019  1 15.613  ? 57   VAL A N     1 
ATOM   257  C  CA    . VAL A 1 65  ? -15.977 7.018   35.037  1 14.177  ? 57   VAL A CA    1 
ATOM   258  C  C     . VAL A 1 65  ? -16.884 5.898   35.554  1 13.329  ? 57   VAL A C     1 
ATOM   259  O  O     . VAL A 1 65  ? -17.577 6.087   36.562  1 13.354  ? 57   VAL A O     1 
ATOM   260  C  CB    . VAL A 1 65  ? -14.629 7.06    35.805  1 12.775  ? 57   VAL A CB    1 
ATOM   261  C  CG1   . VAL A 1 65  ? -13.708 5.901   35.433  1 12.513  ? 57   VAL A CG1   1 
ATOM   262  C  CG2   . VAL A 1 65  ? -13.837 8.348   35.556  1 11.917  ? 57   VAL A CG2   1 
ATOM   263  N  N     . MET A 1 66  ? -16.874 4.763   34.83   1 13.524  ? 58   MET A N     1 
ATOM   264  C  CA    . MET A 1 66  ? -17.576 3.548   35.24   1 17.095  ? 58   MET A CA    1 
ATOM   265  C  C     . MET A 1 66  ? -17.076 3.09    36.611  1 17.503  ? 58   MET A C     1 
ATOM   266  O  O     . MET A 1 66  ? -15.87  3.109   36.889  1 19.46   ? 58   MET A O     1 
ATOM   267  C  CB    . MET A 1 66  ? -17.41  2.378   34.266  1 18.516  ? 58   MET A CB    1 
ATOM   268  C  CG    . MET A 1 66  ? -17.901 2.651   32.846  1 20.36   ? 58   MET A CG    1 
ATOM   269  S  SD    . MET A 1 66  ? -17.544 1.201   31.841  1 24.563  ? 58   MET A SD    1 
ATOM   270  C  CE    . MET A 1 66  ? -15.745 1.301   31.833  1 38.57   ? 58   MET A CE    1 
ATOM   271  N  N     . THR A 1 67  ? -18.052 2.784   37.473  1 16.36   ? 59   THR A N     1 
ATOM   272  C  CA    . THR A 1 67  ? -17.834 2.332   38.84   1 15.831  ? 59   THR A CA    1 
ATOM   273  C  C     . THR A 1 67  ? -18.509 0.979   39.074  1 16.398  ? 59   THR A C     1 
ATOM   274  O  O     . THR A 1 67  ? -19.503 0.658   38.417  1 15.08   ? 59   THR A O     1 
ATOM   275  C  CB    . THR A 1 67  ? -18.231 3.405   39.854  1 16.121  ? 59   THR A CB    1 
ATOM   276  O  OG1   . THR A 1 67  ? -19.637 3.577   39.669  1 16.972  ? 59   THR A OG1   1 
ATOM   277  C  CG2   . THR A 1 67  ? -17.413 4.685   39.729  1 14.646  ? 59   THR A CG2   1 
ATOM   278  N  N     . ARG A 1 68  ? -17.923 0.195   39.992  1 16.564  ? 60   ARG A N     1 
ATOM   279  C  CA    . ARG A 1 68  ? -18.493 -1.037  40.535  1 18.483  ? 60   ARG A CA    1 
ATOM   280  C  C     . ARG A 1 68  ? -18.712 -0.859  42.036  1 21.022  ? 60   ARG A C     1 
ATOM   281  O  O     . ARG A 1 68  ? -17.87  -0.246  42.689  1 21.534  ? 60   ARG A O     1 
ATOM   282  C  CB    . ARG A 1 68  ? -17.617 -2.263  40.248  1 17.326  ? 60   ARG A CB    1 
ATOM   283  C  CG    . ARG A 1 68  ? -17.343 -2.591  38.784  1 18.299  ? 60   ARG A CG    1 
ATOM   284  C  CD    . ARG A 1 68  ? -16.763 -3.965  38.526  1 19.219  ? 60   ARG A CD    1 
ATOM   285  N  NE    . ARG A 1 68  ? -15.438 -4.237  39.113  1 20.181  ? 60   ARG A NE    1 
ATOM   286  C  CZ    . ARG A 1 68  ? -14.204 -3.81   38.785  1 23.274  ? 60   ARG A CZ    1 
ATOM   287  N  NH1   . ARG A 1 68  ? -13.97  -3.002  37.752  1 21.515  ? 60   ARG A NH1   1 
ATOM   288  N  NH2   . ARG A 1 68  ? -13.178 -4.203  39.532  1 23.242  ? 60   ARG A NH2   1 
ATOM   289  N  N     . GLY A 1 69  ? -19.818 -1.423  42.569  1 21.698  ? 61   GLY A N     1 
ATOM   290  C  CA    . GLY A 1 69  ? -20.213 -1.302  43.976  1 22.513  ? 61   GLY A CA    1 
ATOM   291  C  C     . GLY A 1 69  ? -20.754 0.095   44.299  1 23.256  ? 61   GLY A C     1 
ATOM   292  O  O     . GLY A 1 69  ? -21.274 0.759   43.404  1 24.606  ? 61   GLY A O     1 
ATOM   293  N  N     . THR A 1 70  ? -20.629 0.539   45.561  1 22.498  ? 62   THR A N     1 
ATOM   294  C  CA    . THR A 1 70  ? -21.147 1.844   45.976  1 24.13   ? 62   THR A CA    1 
ATOM   295  C  C     . THR A 1 70  ? -19.983 2.779   46.305  1 21.135  ? 62   THR A C     1 
ATOM   296  O  O     . THR A 1 70  ? -19.243 2.505   47.253  1 20.472  ? 62   THR A O     1 
ATOM   297  C  CB    . THR A 1 70  ? -22.185 1.738   47.102  1 26.277  ? 62   THR A CB    1 
ATOM   298  O  OG1   . THR A 1 70  ? -23.237 0.955   46.547  1 30.504  ? 62   THR A OG1   1 
ATOM   299  C  CG2   . THR A 1 70  ? -22.81  3.079   47.471  1 28.167  ? 62   THR A CG2   1 
ATOM   300  N  N     . ILE A 1 71  ? -19.872 3.879   45.533  1 19.585  ? 63   ILE A N     1 
ATOM   301  C  CA    . ILE A 1 71  ? -18.941 4.968   45.826  1 19.264  ? 63   ILE A CA    1 
ATOM   302  C  C     . ILE A 1 71  ? -19.434 5.651   47.111  1 18.652  ? 63   ILE A C     1 
ATOM   303  O  O     . ILE A 1 71  ? -20.553 6.162   47.094  1 18.057  ? 63   ILE A O     1 
ATOM   304  C  CB    . ILE A 1 71  ? -18.687 5.935   44.641  1 19.251  ? 63   ILE A CB    1 
ATOM   305  C  CG1   . ILE A 1 71  ? -18.148 5.254   43.34   1 18.594  ? 63   ILE A CG1   1 
ATOM   306  C  CG2   . ILE A 1 71  ? -17.877 7.181   45.043  1 18.078  ? 63   ILE A CG2   1 
ATOM   307  C  CD1   . ILE A 1 71  ? -16.72  4.716   43.346  1 19.973  ? 63   ILE A CD1   1 
ATOM   308  N  N     . PRO A 1 72  ? -18.656 5.64    48.24   1 18.818  ? 64   PRO A N     1 
ATOM   309  C  CA    . PRO A 1 72  ? -19.057 6.337   49.463  1 18.587  ? 64   PRO A CA    1 
ATOM   310  C  C     . PRO A 1 72  ? -19.401 7.803   49.21   1 19.862  ? 64   PRO A C     1 
ATOM   311  O  O     . PRO A 1 72  ? -18.658 8.515   48.523  1 18.034  ? 64   PRO A O     1 
ATOM   312  C  CB    . PRO A 1 72  ? -17.881 6.119   50.406  1 17.737  ? 64   PRO A CB    1 
ATOM   313  C  CG    . PRO A 1 72  ? -17.2   4.869   49.86   1 16.465  ? 64   PRO A CG    1 
ATOM   314  C  CD    . PRO A 1 72  ? -17.325 5.006   48.394  1 16.59   ? 64   PRO A CD    1 
ATOM   315  N  N     . LYS A 1 73  ? -20.587 8.189   49.708  1 21.086  ? 65   LYS A N     1 
ATOM   316  C  CA    . LYS A 1 73  ? -21.109 9.556   49.675  1 23.943  ? 65   LYS A CA    1 
ATOM   317  C  C     . LYS A 1 73  ? -20.24  10.532  50.477  1 20.331  ? 65   LYS A C     1 
ATOM   318  O  O     . LYS A 1 73  ? -20.23  11.729  50.162  1 18.761  ? 65   LYS A O     1 
ATOM   319  C  CB    . LYS A 1 73  ? -22.615 9.626   49.996  1 28.269  ? 65   LYS A CB    1 
ATOM   320  C  CG    . LYS A 1 73  ? -23.591 9.139   48.896  1 36.582  ? 65   LYS A CG    1 
ATOM   321  C  CD    . LYS A 1 73  ? -23.674 9.931   47.582  1 44.112  ? 65   LYS A CD    1 
ATOM   322  C  CE    . LYS A 1 73  ? -24.291 9.192   46.42   1 50.755  ? 65   LYS A CE    1 
ATOM   323  N  NZ    . LYS A 1 73  ? -25.754 9.153   46.443  1 57.124  ? 65   LYS A NZ    1 
ATOM   324  N  N     . GLU A 1 74  ? -19.501 10.001  51.473  1 19.788  ? 66   GLU A N     1 
ATOM   325  C  CA    . GLU A 1 74  ? -18.563 10.719  52.333  1 19.938  ? 66   GLU A CA    1 
ATOM   326  C  C     . GLU A 1 74  ? -17.346 11.225  51.541  1 21.097  ? 66   GLU A C     1 
ATOM   327  O  O     . GLU A 1 74  ? -16.669 12.134  52.039  1 23.619  ? 66   GLU A O     1 
ATOM   328  C  CB    . GLU A 1 74  ? -18.058 9.9     53.531  1 23.425  ? 66   GLU A CB    1 
ATOM   329  C  CG    . GLU A 1 74  ? -19.132 9.319   54.45   1 24.844  ? 66   GLU A CG    1 
ATOM   330  C  CD    . GLU A 1 74  ? -19.835 8.02    54.102  1 28.717  ? 66   GLU A CD    1 
ATOM   331  O  OE1   . GLU A 1 74  ? -19.676 7.47    52.979  1 27.281  ? 66   GLU A OE1   1 
ATOM   332  O  OE2   . GLU A 1 74  ? -20.563 7.552   55.013  1 26.531  ? 66   GLU A OE2   1 
ATOM   333  N  N     . LEU A 1 75  ? -17.064 10.658  50.339  1 18.621  ? 67   LEU A N     1 
ATOM   334  C  CA    . LEU A 1 75  ? -15.963 11.106  49.484  1 18.029  ? 67   LEU A CA    1 
ATOM   335  C  C     . LEU A 1 75  ? -16.342 12.414  48.791  1 16.74   ? 67   LEU A C     1 
ATOM   336  O  O     . LEU A 1 75  ? -17.322 12.454  48.039  1 17.147  ? 67   LEU A O     1 
ATOM   337  C  CB    . LEU A 1 75  ? -15.426 10.042  48.513  1 16.545  ? 67   LEU A CB    1 
ATOM   338  C  CG    . LEU A 1 75  ? -14.727 8.824   49.136  1 16.709  ? 67   LEU A CG    1 
ATOM   339  C  CD1   . LEU A 1 75  ? -14.39  7.731   48.113  1 16.21   ? 67   LEU A CD1   1 
ATOM   340  C  CD2   . LEU A 1 75  ? -13.5   9.122   49.982  1 15.489  ? 67   LEU A CD2   1 
ATOM   341  N  N     . HIS A 1 76  ? -15.551 13.464  49.072  1 16.429  ? 68   HIS A N     1 
ATOM   342  C  CA    . HIS A 1 76  ? -15.785 14.824  48.594  1 18.354  ? 68   HIS A CA    1 
ATOM   343  C  C     . HIS A 1 76  ? -14.442 15.509  48.348  1 17.316  ? 68   HIS A C     1 
ATOM   344  O  O     . HIS A 1 76  ? -13.948 16.24   49.207  1 17.894  ? 68   HIS A O     1 
ATOM   345  C  CB    . HIS A 1 76  ? -16.796 15.569  49.489  1 17.485  ? 68   HIS A CB    1 
ATOM   346  C  CG    . HIS A 1 76  ? -17.271 16.875  48.931  1 18.063  ? 68   HIS A CG    1 
ATOM   347  N  ND1   . HIS A 1 76  ? -18.289 16.902  48      1 18.386  ? 68   HIS A ND1   1 
ATOM   348  C  CD2   . HIS A 1 76  ? -16.929 18.153  49.157  1 17.659  ? 68   HIS A CD2   1 
ATOM   349  C  CE1   . HIS A 1 76  ? -18.535 18.157  47.652  1 19.714  ? 68   HIS A CE1   1 
ATOM   350  N  NE2   . HIS A 1 76  ? -17.733 18.937  48.351  1 19.011  ? 68   HIS A NE2   1 
ATOM   351  N  N     . GLY A 1 77  ? -13.877 15.27   47.159  1 17.244  ? 69   GLY A N     1 
ATOM   352  C  CA    . GLY A 1 77  ? -12.505 15.669  46.869  1 15.583  ? 69   GLY A CA    1 
ATOM   353  C  C     . GLY A 1 77  ? -11.929 14.958  45.657  1 15.226  ? 69   GLY A C     1 
ATOM   354  O  O     . GLY A 1 77  ? -12.676 14.407  44.85   1 16.034  ? 69   GLY A O     1 
ATOM   355  N  N     . THR A 1 78  ? -10.593 15.007  45.546  1 14.81   ? 70   THR A N     1 
ATOM   356  C  CA    . THR A 1 78  ? -9.863  14.521  44.385  1 15.071  ? 70   THR A CA    1 
ATOM   357  C  C     . THR A 1 78  ? -8.677  13.677  44.855  1 15.588  ? 70   THR A C     1 
ATOM   358  O  O     . THR A 1 78  ? -7.919  14.087  45.743  1 15.506  ? 70   THR A O     1 
ATOM   359  C  CB    . THR A 1 78  ? -9.433  15.671  43.464  1 15.353  ? 70   THR A CB    1 
ATOM   360  O  OG1   . THR A 1 78  ? -10.461 16.644  43.287  1 15.116  ? 70   THR A OG1   1 
ATOM   361  C  CG2   . THR A 1 78  ? -9.03   15.208  42.075  1 14.851  ? 70   THR A CG2   1 
ATOM   362  N  N     . PHE A 1 79  ? -8.566  12.489  44.252  1 15.555  ? 71   PHE A N     1 
ATOM   363  C  CA    . PHE A 1 79  ? -7.369  11.673  44.321  1 15.356  ? 71   PHE A CA    1 
ATOM   364  C  C     . PHE A 1 79  ? -6.47   12.073  43.155  1 14.512  ? 71   PHE A C     1 
ATOM   365  O  O     . PHE A 1 79  ? -6.781  11.763  42.008  1 14.461  ? 71   PHE A O     1 
ATOM   366  C  CB    . PHE A 1 79  ? -7.747  10.193  44.471  1 16.086  ? 71   PHE A CB    1 
ATOM   367  C  CG    . PHE A 1 79  ? -6.624  9.157   44.548  1 16.824  ? 71   PHE A CG    1 
ATOM   368  C  CD1   . PHE A 1 79  ? -5.313  9.481   44.971  1 17.001  ? 71   PHE A CD1   1 
ATOM   369  C  CD2   . PHE A 1 79  ? -6.903  7.82    44.21   1 17.494  ? 71   PHE A CD2   1 
ATOM   370  C  CE1   . PHE A 1 79  ? -4.311  8.497   45.028  1 17.667  ? 71   PHE A CE1   1 
ATOM   371  C  CE2   . PHE A 1 79  ? -5.915  6.831   44.298  1 18.133  ? 71   PHE A CE2   1 
ATOM   372  C  CZ    . PHE A 1 79  ? -4.62   7.165   44.718  1 17.194  ? 71   PHE A CZ    1 
ATOM   373  N  N     . TYR A 1 80  ? -5.393  12.811  43.476  1 15.137  ? 72   TYR A N     1 
ATOM   374  C  CA    . TYR A 1 80  ? -4.373  13.245  42.526  1 16      ? 72   TYR A CA    1 
ATOM   375  C  C     . TYR A 1 80  ? -3.159  12.332  42.635  1 17.495  ? 72   TYR A C     1 
ATOM   376  O  O     . TYR A 1 80  ? -2.599  12.197  43.718  1 16.385  ? 72   TYR A O     1 
ATOM   377  C  CB    . TYR A 1 80  ? -3.852  14.677  42.622  1 15.596  ? 72   TYR A CB    1 
ATOM   378  C  CG    . TYR A 1 80  ? -4.869  15.773  42.398  1 16.474  ? 72   TYR A CG    1 
ATOM   379  C  CD1   . TYR A 1 80  ? -5.131  16.269  41.111  1 16.927  ? 72   TYR A CD1   1 
ATOM   380  C  CD2   . TYR A 1 80  ? -5.53   16.346  43.49   1 16.517  ? 72   TYR A CD2   1 
ATOM   381  C  CE1   . TYR A 1 80  ? -6.019  17.33   40.93   1 17.371  ? 72   TYR A CE1   1 
ATOM   382  C  CE2   . TYR A 1 80  ? -6.399  17.422  43.321  1 17.441  ? 72   TYR A CE2   1 
ATOM   383  C  CZ    . TYR A 1 80  ? -6.663  17.884  42.033  1 17.422  ? 72   TYR A CZ    1 
ATOM   384  O  OH    . TYR A 1 80  ? -7.562  18.881  41.848  1 16.923  ? 72   TYR A OH    1 
ATOM   385  N  N     . ARG A 1 81  ? -2.789  11.736  41.492  1 17.803  ? 73   ARG A N     1 
ATOM   386  C  CA    . ARG A 1 81  ? -1.697  10.786  41.374  1 19.107  ? 73   ARG A CA    1 
ATOM   387  C  C     . ARG A 1 81  ? -0.722  11.29   40.313  1 19.982  ? 73   ARG A C     1 
ATOM   388  O  O     . ARG A 1 81  ? -1.152  11.837  39.303  1 22.423  ? 73   ARG A O     1 
ATOM   389  C  CB    . ARG A 1 81  ? -2.39   9.479   40.993  1 21.108  ? 73   ARG A CB    1 
ATOM   390  C  CG    . ARG A 1 81  ? -1.534  8.255   41.222  1 23.76   ? 73   ARG A CG    1 
ATOM   391  C  CD    . ARG A 1 81  ? -1.601  7.572   42.563  1 21.366  ? 73   ARG A CD    1 
ATOM   392  N  NE    . ARG A 1 81  ? -0.613  6.51    42.337  1 21.118  ? 73   ARG A NE    1 
ATOM   393  C  CZ    . ARG A 1 81  ? 0.542   6.271   42.968  1 19.27   ? 73   ARG A CZ    1 
ATOM   394  N  NH1   . ARG A 1 81  ? 0.827   6.797   44.146  1 17.377  ? 73   ARG A NH1   1 
ATOM   395  N  NH2   . ARG A 1 81  ? 1.407   5.438   42.427  1 18.618  ? 73   ARG A NH2   1 
ATOM   396  N  N     . ILE A 1 82  ? 0.582   11.107  40.539  1 16.691  ? 74   ILE A N     1 
ATOM   397  C  CA    . ILE A 1 82  ? 1.617   11.589  39.627  1 15.436  ? 74   ILE A CA    1 
ATOM   398  C  C     . ILE A 1 82  ? 2.547   10.437  39.255  1 15.523  ? 74   ILE A C     1 
ATOM   399  O  O     . ILE A 1 82  ? 2.88    9.589   40.089  1 16.736  ? 74   ILE A O     1 
ATOM   400  C  CB    . ILE A 1 82  ? 2.296   12.872  40.16   1 14.788  ? 74   ILE A CB    1 
ATOM   401  C  CG1   . ILE A 1 82  ? 2.999   13.73   39.061  1 14.551  ? 74   ILE A CG1   1 
ATOM   402  C  CG2   . ILE A 1 82  ? 3.186   12.59   41.375  1 14.645  ? 74   ILE A CG2   1 
ATOM   403  C  CD1   . ILE A 1 82  ? 3.385   15.148  39.494  1 14.159  ? 74   ILE A CD1   1 
ATOM   404  N  N     . MET A 1 83  ? 2.945   10.42   37.981  1 16.083  ? 75   MET A N     1 
ATOM   405  C  CA    . MET A 1 83  ? 3.615   9.281   37.358  1 15.507  ? 75   MET A CA    1 
ATOM   406  C  C     . MET A 1 83  ? 4.743   9.759   36.436  1 14.545  ? 75   MET A C     1 
ATOM   407  O  O     . MET A 1 83  ? 4.605   10.843  35.859  1 14.949  ? 75   MET A O     1 
ATOM   408  C  CB    . MET A 1 83  ? 2.658   8.5     36.447  1 15.732  ? 75   MET A CB    1 
ATOM   409  C  CG    . MET A 1 83  ? 1.501   7.825   37.129  1 19.883  ? 75   MET A CG    1 
ATOM   410  S  SD    . MET A 1 83  ? -0.002  7.803   36.144  1 22.164  ? 75   MET A SD    1 
ATOM   411  C  CE    . MET A 1 83  ? -0.541  9.38    36.813  1 20.735  ? 75   MET A CE    1 
ATOM   412  N  N     . PRO A 1 84  ? 5.86    8.979   36.275  1 14.81   ? 76   PRO A N     1 
ATOM   413  C  CA    . PRO A 1 84  ? 6.829   9.197   35.197  1 15.301  ? 76   PRO A CA    1 
ATOM   414  C  C     . PRO A 1 84  ? 6.355   8.567   33.892  1 16.428  ? 76   PRO A C     1 
ATOM   415  O  O     . PRO A 1 84  ? 5.999   7.382   33.873  1 18.067  ? 76   PRO A O     1 
ATOM   416  C  CB    . PRO A 1 84  ? 8.121   8.62    35.769  1 14.492  ? 76   PRO A CB    1 
ATOM   417  C  CG    . PRO A 1 84  ? 7.636   7.493   36.667  1 14.715  ? 76   PRO A CG    1 
ATOM   418  C  CD    . PRO A 1 84  ? 6.265   7.829   37.13   1 14.36   ? 76   PRO A CD    1 
ATOM   419  N  N     . ASP A 1 85  ? 6.279   9.385   32.826  1 16.671  ? 77   ASP A N     1 
ATOM   420  C  CA    . ASP A 1 85  ? 5.786   8.924   31.531  1 17.294  ? 77   ASP A CA    1 
ATOM   421  C  C     . ASP A 1 85  ? 6.455   9.749   30.443  1 18.273  ? 77   ASP A C     1 
ATOM   422  O  O     . ASP A 1 85  ? 5.85    10.682  29.925  1 19.806  ? 77   ASP A O     1 
ATOM   423  C  CB    . ASP A 1 85  ? 4.258   8.972   31.456  1 17.361  ? 77   ASP A CB    1 
ATOM   424  C  CG    . ASP A 1 85  ? 3.506   8.057   30.489  1 18.107  ? 77   ASP A CG    1 
ATOM   425  O  OD1   . ASP A 1 85  ? 4.124   7.108   29.911  1 16.543  ? 77   ASP A OD1   1 
ATOM   426  O  OD2   . ASP A 1 85  ? 2.252   8.237   30.41   1 20.416  ? 77   ASP A OD2   1 
ATOM   427  N  N     . TYR A 1 86  ? 7.711   9.413   30.118  1 18.577  ? 78   TYR A N     1 
ATOM   428  C  CA    . TYR A 1 86  ? 8.487   10.067  29.072  1 17.326  ? 78   TYR A CA    1 
ATOM   429  C  C     . TYR A 1 86  ? 7.608   10.334  27.849  1 18.422  ? 78   TYR A C     1 
ATOM   430  O  O     . TYR A 1 86  ? 7.038   9.404   27.28   1 17.011  ? 78   TYR A O     1 
ATOM   431  C  CB    . TYR A 1 86  ? 9.679   9.151   28.78   1 18.442  ? 78   TYR A CB    1 
ATOM   432  C  CG    . TYR A 1 86  ? 11.017  9.459   29.444  1 17.342  ? 78   TYR A CG    1 
ATOM   433  C  CD1   . TYR A 1 86  ? 11.629  10.728  29.324  1 18.368  ? 78   TYR A CD1   1 
ATOM   434  C  CD2   . TYR A 1 86  ? 11.697  8.452   30.145  1 16.684  ? 78   TYR A CD2   1 
ATOM   435  C  CE1   . TYR A 1 86  ? 12.881  10.975  29.889  1 17.481  ? 78   TYR A CE1   1 
ATOM   436  C  CE2   . TYR A 1 86  ? 12.957  8.685   30.698  1 18.682  ? 78   TYR A CE2   1 
ATOM   437  C  CZ    . TYR A 1 86  ? 13.545  9.948   30.566  1 18.604  ? 78   TYR A CZ    1 
ATOM   438  O  OH    . TYR A 1 86  ? 14.795  10.161  31.091  1 19.577  ? 78   TYR A OH    1 
ATOM   439  N  N     . ALA A 1 87  ? 7.406   11.628  27.571  1 16.579  ? 79   ALA A N     1 
ATOM   440  C  CA    . ALA A 1 87  ? 6.544   12.113  26.505  1 17.717  ? 79   ALA A CA    1 
ATOM   441  C  C     . ALA A 1 87  ? 7.159   11.839  25.122  1 18.529  ? 79   ALA A C     1 
ATOM   442  O  O     . ALA A 1 87  ? 6.441   11.454  24.193  1 19.655  ? 79   ALA A O     1 
ATOM   443  C  CB    . ALA A 1 87  ? 6.194   13.565  26.751  1 15.694  ? 79   ALA A CB    1 
ATOM   444  N  N     . GLN A 1 88  ? 8.487   12.019  25.012  1 18.437  ? 80   GLN A N     1 
ATOM   445  C  CA    . GLN A 1 88  ? 9.3     11.69   23.841  1 18.578  ? 80   GLN A CA    1 
ATOM   446  C  C     . GLN A 1 88  ? 10.203  10.489  24.139  1 18.313  ? 80   GLN A C     1 
ATOM   447  O  O     . GLN A 1 88  ? 10.651  10.391  25.289  1 18.18   ? 80   GLN A O     1 
ATOM   448  C  CB    . GLN A 1 88  ? 10.128  12.894  23.389  1 19.036  ? 80   GLN A CB    1 
ATOM   449  C  CG    . GLN A 1 88  ? 9.311   14.071  22.839  1 18.069  ? 80   GLN A CG    1 
ATOM   450  C  CD    . GLN A 1 88  ? 8.355   13.739  21.715  1 18.206  ? 80   GLN A CD    1 
ATOM   451  O  OE1   . GLN A 1 88  ? 7.149   13.997  21.824  1 19.459  ? 80   GLN A OE1   1 
ATOM   452  N  NE2   . GLN A 1 88  ? 8.88    13.194  20.617  1 17.332  ? 80   GLN A NE2   1 
ATOM   453  N  N     . PRO A 1 89  ? 10.525  9.583   23.156  1 17.564  ? 81   PRO A N     1 
ATOM   454  C  CA    . PRO A 1 89  ? 11.505  8.516   23.381  1 17.23   ? 81   PRO A CA    1 
ATOM   455  C  C     . PRO A 1 89  ? 12.847  9.076   23.87   1 18.26   ? 81   PRO A C     1 
ATOM   456  O  O     . PRO A 1 89  ? 13.388  9.961   23.187  1 17.646  ? 81   PRO A O     1 
ATOM   457  C  CB    . PRO A 1 89  ? 11.565  7.733   22.065  1 17.688  ? 81   PRO A CB    1 
ATOM   458  C  CG    . PRO A 1 89  ? 11.051  8.746   21.044  1 16.671  ? 81   PRO A CG    1 
ATOM   459  C  CD    . PRO A 1 89  ? 10.018  9.557   21.76   1 16.202  ? 81   PRO A CD    1 
ATOM   460  N  N     . PRO A 1 90  ? 13.328  8.733   25.107  1 17.771  ? 82   PRO A N     1 
ATOM   461  C  CA    . PRO A 1 90  ? 14.441  9.458   25.742  1 19.432  ? 82   PRO A CA    1 
ATOM   462  C  C     . PRO A 1 90  ? 15.844  9.152   25.196  1 20.579  ? 82   PRO A C     1 
ATOM   463  O  O     . PRO A 1 90  ? 16.753  8.845   25.976  1 20.528  ? 82   PRO A O     1 
ATOM   464  C  CB    . PRO A 1 90  ? 14.241  9.145   27.224  1 18.052  ? 82   PRO A CB    1 
ATOM   465  C  CG    . PRO A 1 90  ? 13.714  7.724   27.19   1 18.643  ? 82   PRO A CG    1 
ATOM   466  C  CD    . PRO A 1 90  ? 12.738  7.749   26.038  1 18.059  ? 82   PRO A CD    1 
ATOM   467  N  N     . THR A 1 91  ? 16.026  9.317   23.874  1 21.193  ? 83   THR A N     1 
ATOM   468  C  CA    . THR A 1 91  ? 17.152  8.75    23.133  1 21.722  ? 83   THR A CA    1 
ATOM   469  C  C     . THR A 1 91  ? 18.404  9.64    23.147  1 22.585  ? 83   THR A C     1 
ATOM   470  O  O     . THR A 1 91  ? 19.41   9.23    22.559  1 24.035  ? 83   THR A O     1 
ATOM   471  C  CB    . THR A 1 91  ? 16.746  8.377   21.702  1 23.421  ? 83   THR A CB    1 
ATOM   472  O  OG1   . THR A 1 91  ? 16.263  9.59    21.13   1 26.565  ? 83   THR A OG1   1 
ATOM   473  C  CG2   . THR A 1 91  ? 15.758  7.226   21.606  1 24.428  ? 83   THR A CG2   1 
ATOM   474  N  N     . TYR A 1 92  ? 18.369  10.831  23.787  1 23.09   ? 84   TYR A N     1 
ATOM   475  C  CA    . TYR A 1 92  ? 19.442  11.827  23.724  1 23.666  ? 84   TYR A CA    1 
ATOM   476  C  C     . TYR A 1 92  ? 20.809  11.241  24.113  1 23.097  ? 84   TYR A C     1 
ATOM   477  O  O     . TYR A 1 92  ? 21.752  11.349  23.322  1 22.766  ? 84   TYR A O     1 
ATOM   478  C  CB    . TYR A 1 92  ? 19.231  13.228  24.322  1 23.03   ? 84   TYR A CB    1 
ATOM   479  C  CG    . TYR A 1 92  ? 20.42   14.139  24.013  1 22.404  ? 84   TYR A CG    1 
ATOM   480  C  CD1   . TYR A 1 92  ? 20.539  14.724  22.745  1 22.645  ? 84   TYR A CD1   1 
ATOM   481  C  CD2   . TYR A 1 92  ? 21.455  14.349  24.945  1 22.812  ? 84   TYR A CD2   1 
ATOM   482  C  CE1   . TYR A 1 92  ? 21.63   15.521  22.413  1 24.613  ? 84   TYR A CE1   1 
ATOM   483  C  CE2   . TYR A 1 92  ? 22.55   15.15   24.621  1 24.269  ? 84   TYR A CE2   1 
ATOM   484  C  CZ    . TYR A 1 92  ? 22.631  15.734  23.354  1 25.453  ? 84   TYR A CZ    1 
ATOM   485  O  OH    . TYR A 1 92  ? 23.662  16.525  22.943  1 28.035  ? 84   TYR A OH    1 
ATOM   486  N  N     . TYR A 1 93  ? 20.894  10.664  25.321  1 23.22   ? 85   TYR A N     1 
ATOM   487  C  CA    . TYR A 1 93  ? 22.155  10.178  25.875  1 24.765  ? 85   TYR A CA    1 
ATOM   488  C  C     . TYR A 1 93  ? 22.18   8.657   25.886  1 22.935  ? 85   TYR A C     1 
ATOM   489  O  O     . TYR A 1 93  ? 21.305  8.039   26.487  1 22.097  ? 85   TYR A O     1 
ATOM   490  C  CB    . TYR A 1 93  ? 22.476  10.807  27.233  1 26.355  ? 85   TYR A CB    1 
ATOM   491  C  CG    . TYR A 1 93  ? 23.856  10.51   27.805  1 26.528  ? 85   TYR A CG    1 
ATOM   492  C  CD1   . TYR A 1 93  ? 25.004  11.145  27.306  1 27.724  ? 85   TYR A CD1   1 
ATOM   493  C  CD2   . TYR A 1 93  ? 24.009  9.617   28.875  1 25.23   ? 85   TYR A CD2   1 
ATOM   494  C  CE1   . TYR A 1 93  ? 26.269  10.893  27.849  1 28.318  ? 85   TYR A CE1   1 
ATOM   495  C  CE2   . TYR A 1 93  ? 25.267  9.368   29.433  1 25.384  ? 85   TYR A CE2   1 
ATOM   496  C  CZ    . TYR A 1 93  ? 26.393  9.991   28.906  1 27.124  ? 85   TYR A CZ    1 
ATOM   497  O  OH    . TYR A 1 93  ? 27.622  9.748   29.444  1 29.116  ? 85   TYR A OH    1 
ATOM   498  N  N     . LYS A 1 94  ? 23.183  8.095   25.183  1 21.975  ? 86   LYS A N     1 
ATOM   499  C  CA    . LYS A 1 94  ? 23.461  6.663   25.05   1 23.924  ? 86   LYS A CA    1 
ATOM   500  C  C     . LYS A 1 94  ? 22.217  5.885   24.589  1 24.442  ? 86   LYS A C     1 
ATOM   501  O  O     . LYS A 1 94  ? 21.962  4.793   25.099  1 27.029  ? 86   LYS A O     1 
ATOM   502  C  CB    . LYS A 1 94  ? 24.116  6.109   26.333  1 26.421  ? 86   LYS A CB    1 
ATOM   503  C  CG    . LYS A 1 94  ? 25.517  6.613   26.635  1 28.463  ? 86   LYS A CG    1 
ATOM   504  C  CD    . LYS A 1 94  ? 26.137  6.138   27.943  1 29.162  ? 86   LYS A CD    1 
ATOM   505  C  CE    . LYS A 1 94  ? 27.53   6.664   27.993  1 30.481  ? 86   LYS A CE    1 
ATOM   506  N  NZ    . LYS A 1 94  ? 28.154  6.354   29.276  1 32.774  ? 86   LYS A NZ    1 
ATOM   507  N  N     . GLY A 1 95  ? 21.417  6.482   23.68   1 23.02   ? 87   GLY A N     1 
ATOM   508  C  CA    . GLY A 1 95  ? 20.158  5.949   23.159  1 23.354  ? 87   GLY A CA    1 
ATOM   509  C  C     . GLY A 1 95  ? 19.077  5.712   24.228  1 24.935  ? 87   GLY A C     1 
ATOM   510  O  O     . GLY A 1 95  ? 18.183  4.889   24.009  1 24.53   ? 87   GLY A O     1 
ATOM   511  N  N     . GLY A 1 96  ? 19.186  6.42    25.37   1 24.501  ? 88   GLY A N     1 
ATOM   512  C  CA    . GLY A 1 96  ? 18.369  6.267   26.568  1 29.051  ? 88   GLY A CA    1 
ATOM   513  C  C     . GLY A 1 96  ? 18.562  4.966   27.352  1 30.019  ? 88   GLY A C     1 
ATOM   514  O  O     . GLY A 1 96  ? 17.698  4.63    28.171  1 27.234  ? 88   GLY A O     1 
ATOM   515  N  N     . GLU A 1 97  ? 19.707  4.282   27.167  1 27.647  ? 89   GLU A N     1 
ATOM   516  C  CA    . GLU A 1 97  ? 19.972  2.99    27.799  1 29.511  ? 89   GLU A CA    1 
ATOM   517  C  C     . GLU A 1 97  ? 20.122  3.083   29.318  1 24.936  ? 89   GLU A C     1 
ATOM   518  O  O     . GLU A 1 97  ? 19.874  2.08    29.988  1 23.05   ? 89   GLU A O     1 
ATOM   519  C  CB    . GLU A 1 97  ? 21.023  2.154   27.071  1 39.888  ? 89   GLU A CB    1 
ATOM   520  C  CG    . GLU A 1 97  ? 20.41   1.473   25.846  1 56.847  ? 89   GLU A CG    1 
ATOM   521  C  CD    . GLU A 1 97  ? 21.352  0.959   24.772  1 69.291  ? 89   GLU A CD    1 
ATOM   522  O  OE1   . GLU A 1 97  ? 22.085  -0.006  25.076  1 78.437  ? 89   GLU A OE1   1 
ATOM   523  O  OE2   . GLU A 1 97  ? 21.361  1.525   23.652  1 70.492  ? 89   GLU A OE2   1 
ATOM   524  N  N     . LEU A 1 98  ? 20.495  4.266   29.838  1 22.65   ? 90   LEU A N     1 
ATOM   525  C  CA    . LEU A 1 98  ? 20.705  4.471   31.271  1 22.459  ? 90   LEU A CA    1 
ATOM   526  C  C     . LEU A 1 98  ? 19.622  5.35    31.908  1 22.105  ? 90   LEU A C     1 
ATOM   527  O  O     . LEU A 1 98  ? 19.84   5.91    32.983  1 23.708  ? 90   LEU A O     1 
ATOM   528  C  CB    . LEU A 1 98  ? 22.147  4.861   31.625  1 22.459  ? 90   LEU A CB    1 
ATOM   529  C  CG    . LEU A 1 98  ? 23.294  3.928   31.211  1 22.89   ? 90   LEU A CG    1 
ATOM   530  C  CD1   . LEU A 1 98  ? 24.582  4.675   31.542  1 24.525  ? 90   LEU A CD1   1 
ATOM   531  C  CD2   . LEU A 1 98  ? 23.318  2.575   31.925  1 24.542  ? 90   LEU A CD2   1 
ATOM   532  N  N     . ASN A 1 99  ? 18.43   5.414   31.275  1 22.218  ? 91   ASN A N     1 
ATOM   533  C  CA    . ASN A 1 99  ? 17.256  6.1     31.816  1 21.755  ? 91   ASN A CA    1 
ATOM   534  C  C     . ASN A 1 99  ? 16.816  5.357   33.081  1 21.19   ? 91   ASN A C     1 
ATOM   535  O  O     . ASN A 1 99  ? 16.818  4.123   33.101  1 21.071  ? 91   ASN A O     1 
ATOM   536  C  CB    . ASN A 1 99  ? 16.19   6.395   30.755  1 21.762  ? 91   ASN A CB    1 
ATOM   537  C  CG    . ASN A 1 99  ? 15.194  5.267   30.559  1 22.093  ? 91   ASN A CG    1 
ATOM   538  O  OD1   . ASN A 1 99  ? 14.273  5.09    31.369  1 20.85   ? 91   ASN A OD1   1 
ATOM   539  N  ND2   . ASN A 1 99  ? 15.336  4.51    29.481  1 21.235  ? 91   ASN A ND2   1 
ATOM   540  N  N     . ALA A 1 100 ? 16.502  6.134   34.124  1 18.92   ? 92   ALA A N     1 
ATOM   541  C  CA    . ALA A 1 100 ? 16.099  5.617   35.421  1 20.038  ? 92   ALA A CA    1 
ATOM   542  C  C     . ALA A 1 100 ? 14.564  5.612   35.513  1 19.093  ? 92   ALA A C     1 
ATOM   543  O  O     . ALA A 1 100 ? 13.926  6.452   34.867  1 20.371  ? 92   ALA A O     1 
ATOM   544  C  CB    . ALA A 1 100 ? 16.77   6.415   36.524  1 19.174  ? 92   ALA A CB    1 
ATOM   545  N  N     . PRO A 1 101 ? 13.9    4.686   36.27   1 18.626  ? 93   PRO A N     1 
ATOM   546  C  CA    . PRO A 1 101 ? 12.441  4.725   36.443  1 17.865  ? 93   PRO A CA    1 
ATOM   547  C  C     . PRO A 1 101 ? 11.861  6.015   37.044  1 17.828  ? 93   PRO A C     1 
ATOM   548  O  O     . PRO A 1 101 ? 10.674  6.294   36.84   1 15.98   ? 93   PRO A O     1 
ATOM   549  C  CB    . PRO A 1 101 ? 12.15   3.509   37.307  1 17.87   ? 93   PRO A CB    1 
ATOM   550  C  CG    . PRO A 1 101 ? 13.465  3.274   38.021  1 17.932  ? 93   PRO A CG    1 
ATOM   551  C  CD    . PRO A 1 101 ? 14.477  3.521   36.978  1 18.043  ? 93   PRO A CD    1 
ATOM   552  N  N     . ILE A 1 102 ? 12.72   6.796   37.73   1 15.676  ? 94   ILE A N     1 
ATOM   553  C  CA    . ILE A 1 102 ? 12.372  8.046   38.398  1 15.814  ? 94   ILE A CA    1 
ATOM   554  C  C     . ILE A 1 102 ? 12.516  9.261   37.459  1 15.847  ? 94   ILE A C     1 
ATOM   555  O  O     . ILE A 1 102 ? 12.264  10.392  37.891  1 16.095  ? 94   ILE A O     1 
ATOM   556  C  CB    . ILE A 1 102 ? 13.106  8.194   39.753  1 15.292  ? 94   ILE A CB    1 
ATOM   557  C  CG1   . ILE A 1 102 ? 14.672  8.218   39.624  1 15.609  ? 94   ILE A CG1   1 
ATOM   558  C  CG2   . ILE A 1 102 ? 12.599  7.17    40.775  1 13.973  ? 94   ILE A CG2   1 
ATOM   559  C  CD1   . ILE A 1 102 ? 15.433  8.651   40.88   1 14.777  ? 94   ILE A CD1   1 
ATOM   560  N  N     . ASP A 1 103 ? 12.895  9.027   36.188  1 15.365  ? 95   ASP A N     1 
ATOM   561  C  CA    . ASP A 1 103 ? 13.264  10.067  35.235  1 16.618  ? 95   ASP A CA    1 
ATOM   562  C  C     . ASP A 1 103 ? 12.082  10.762  34.558  1 16.98   ? 95   ASP A C     1 
ATOM   563  O  O     . ASP A 1 103 ? 12.114  11.994  34.448  1 17.989  ? 95   ASP A O     1 
ATOM   564  C  CB    . ASP A 1 103 ? 14.242  9.592   34.169  1 18.08   ? 95   ASP A CB    1 
ATOM   565  C  CG    . ASP A 1 103 ? 15.726  9.835   34.416  1 20.209  ? 95   ASP A CG    1 
ATOM   566  O  OD1   . ASP A 1 103 ? 16.114  11.021  34.669  1 20.652  ? 95   ASP A OD1   1 
ATOM   567  O  OD2   . ASP A 1 103 ? 16.499  8.86    34.266  1 19.841  ? 95   ASP A OD2   1 
ATOM   568  N  N     . GLY A 1 104 ? 11.106  9.986   34.043  1 16.391  ? 96   GLY A N     1 
ATOM   569  C  CA    . GLY A 1 104 ? 10.208  10.411  32.966  1 14.581  ? 96   GLY A CA    1 
ATOM   570  C  C     . GLY A 1 104 ? 9.311   11.593  33.339  1 15.605  ? 96   GLY A C     1 
ATOM   571  O  O     . GLY A 1 104 ? 9.012   11.787  34.522  1 15.335  ? 96   GLY A O     1 
ATOM   572  N  N     . ASP A 1 105 ? 8.917   12.366  32.301  1 14.671  ? 97   ASP A N     1 
ATOM   573  C  CA    . ASP A 1 105 ? 8.034   13.539  32.348  1 15.395  ? 97   ASP A CA    1 
ATOM   574  C  C     . ASP A 1 105 ? 6.808   13.275  33.225  1 13.575  ? 97   ASP A C     1 
ATOM   575  O  O     . ASP A 1 105 ? 6.151   12.244  33.075  1 12.195  ? 97   ASP A O     1 
ATOM   576  C  CB    . ASP A 1 105 ? 7.603   13.991  30.953  1 15.185  ? 97   ASP A CB    1 
ATOM   577  C  CG    . ASP A 1 105 ? 8.762   14.263  30.012  1 15.613  ? 97   ASP A CG    1 
ATOM   578  O  OD1   . ASP A 1 105 ? 9.49    15.257  30.257  1 16.659  ? 97   ASP A OD1   1 
ATOM   579  O  OD2   . ASP A 1 105 ? 8.962   13.447  29.086  1 15.1    ? 97   ASP A OD2   1 
ATOM   580  N  N     . GLY A 1 106 ? 6.608   14.184  34.199  1 13.447  ? 98   GLY A N     1 
ATOM   581  C  CA    . GLY A 1 106 ? 5.479   14.149  35.13   1 14.708  ? 98   GLY A CA    1 
ATOM   582  C  C     . GLY A 1 106 ? 4.152   14.369  34.413  1 14.497  ? 98   GLY A C     1 
ATOM   583  O  O     . GLY A 1 106 ? 3.988   15.354  33.681  1 13.662  ? 98   GLY A O     1 
ATOM   584  N  N     . THR A 1 107 ? 3.261   13.399  34.653  1 15.052  ? 99   THR A N     1 
ATOM   585  C  CA    . THR A 1 107 ? 1.853   13.397  34.273  1 15.922  ? 99   THR A CA    1 
ATOM   586  C  C     . THR A 1 107 ? 0.98    13.169  35.512  1 16.737  ? 99   THR A C     1 
ATOM   587  O  O     . THR A 1 107 ? 1.247   12.263  36.31   1 18.775  ? 99   THR A O     1 
ATOM   588  C  CB    . THR A 1 107 ? 1.586   12.424  33.116  1 15.317  ? 99   THR A CB    1 
ATOM   589  O  OG1   . THR A 1 107 ? 0.224   12.651  32.765  1 14.354  ? 99   THR A OG1   1 
ATOM   590  C  CG2   . THR A 1 107 ? 1.905   10.964  33.4    1 14.043  ? 99   THR A CG2   1 
ATOM   591  N  N     . VAL A 1 108 ? -0.043  14.026  35.66   1 16.008  ? 100  VAL A N     1 
ATOM   592  C  CA    . VAL A 1 108 ? -0.954  13.995  36.8    1 14.577  ? 100  VAL A CA    1 
ATOM   593  C  C     . VAL A 1 108 ? -2.246  13.325  36.346  1 16.884  ? 100  VAL A C     1 
ATOM   594  O  O     . VAL A 1 108 ? -2.811  13.745  35.329  1 14.915  ? 100  VAL A O     1 
ATOM   595  C  CB    . VAL A 1 108 ? -1.172  15.379  37.453  1 15.674  ? 100  VAL A CB    1 
ATOM   596  C  CG1   . VAL A 1 108 ? -2.214  15.402  38.579  1 15.198  ? 100  VAL A CG1   1 
ATOM   597  C  CG2   . VAL A 1 108 ? 0.132   16.01   37.934  1 14.472  ? 100  VAL A CG2   1 
ATOM   598  N  N     . ALA A 1 109 ? -2.686  12.287  37.09   1 15.848  ? 101  ALA A N     1 
ATOM   599  C  CA    . ALA A 1 109 ? -4.052  11.779  37.006  1 18.058  ? 101  ALA A CA    1 
ATOM   600  C  C     . ALA A 1 109 ? -4.879  12.279  38.196  1 18.706  ? 101  ALA A C     1 
ATOM   601  O  O     . ALA A 1 109 ? -4.437  12.167  39.345  1 21.235  ? 101  ALA A O     1 
ATOM   602  C  CB    . ALA A 1 109 ? -4.08   10.261  36.883  1 17.039  ? 101  ALA A CB    1 
ATOM   603  N  N     . ALA A 1 110 ? -6.08   12.802  37.892  1 16.749  ? 102  ALA A N     1 
ATOM   604  C  CA    . ALA A 1 110 ? -7.043  13.309  38.859  1 16.192  ? 102  ALA A CA    1 
ATOM   605  C  C     . ALA A 1 110 ? -8.318  12.467  38.784  1 16.987  ? 102  ALA A C     1 
ATOM   606  O  O     . ALA A 1 110 ? -8.872  12.312  37.699  1 15.515  ? 102  ALA A O     1 
ATOM   607  C  CB    . ALA A 1 110 ? -7.308  14.791  38.629  1 14.521  ? 102  ALA A CB    1 
ATOM   608  N  N     . PHE A 1 111 ? -8.743  11.944  39.948  1 15.469  ? 103  PHE A N     1 
ATOM   609  C  CA    . PHE A 1 111 ? -10.003 11.233  40.14   1 15.7    ? 103  PHE A CA    1 
ATOM   610  C  C     . PHE A 1 111 ? -10.854 12.048  41.122  1 15.3    ? 103  PHE A C     1 
ATOM   611  O  O     . PHE A 1 111 ? -10.592 12.002  42.317  1 15.338  ? 103  PHE A O     1 
ATOM   612  C  CB    . PHE A 1 111 ? -9.738  9.787   40.588  1 14.259  ? 103  PHE A CB    1 
ATOM   613  C  CG    . PHE A 1 111 ? -8.867  8.938   39.679  1 14.155  ? 103  PHE A CG    1 
ATOM   614  C  CD1   . PHE A 1 111 ? -7.47   8.927   39.826  1 14.996  ? 103  PHE A CD1   1 
ATOM   615  C  CD2   . PHE A 1 111 ? -9.46   8.135   38.691  1 13.905  ? 103  PHE A CD2   1 
ATOM   616  C  CE1   . PHE A 1 111 ? -6.663  8.14    38.985  1 15.883  ? 103  PHE A CE1   1 
ATOM   617  C  CE2   . PHE A 1 111 ? -8.669  7.334   37.858  1 13.912  ? 103  PHE A CE2   1 
ATOM   618  C  CZ    . PHE A 1 111 ? -7.272  7.319   38.012  1 15.826  ? 103  PHE A CZ    1 
ATOM   619  N  N     . ARG A 1 112 ? -11.838 12.808  40.607  1 15.756  ? 104  ARG A N     1 
ATOM   620  C  CA    . ARG A 1 112 ? -12.701 13.663  41.419  1 15.928  ? 104  ARG A CA    1 
ATOM   621  C  C     . ARG A 1 112 ? -13.984 12.929  41.808  1 16.286  ? 104  ARG A C     1 
ATOM   622  O  O     . ARG A 1 112 ? -14.732 12.508  40.93   1 15.931  ? 104  ARG A O     1 
ATOM   623  C  CB    . ARG A 1 112 ? -12.96  15.014  40.751  1 14.715  ? 104  ARG A CB    1 
ATOM   624  C  CG    . ARG A 1 112 ? -13.747 15.965  41.637  1 14.657  ? 104  ARG A CG    1 
ATOM   625  C  CD    . ARG A 1 112 ? -13.534 17.342  41.102  1 14.707  ? 104  ARG A CD    1 
ATOM   626  N  NE    . ARG A 1 112 ? -12.239 17.932  41.46   1 14.202  ? 104  ARG A NE    1 
ATOM   627  C  CZ    . ARG A 1 112 ? -11.786 19.113  41.055  1 14.02   ? 104  ARG A CZ    1 
ATOM   628  N  NH1   . ARG A 1 112 ? -12.567 19.929  40.348  1 13.687  ? 104  ARG A NH1   1 
ATOM   629  N  NH2   . ARG A 1 112 ? -10.54  19.463  41.346  1 12.782  ? 104  ARG A NH2   1 
ATOM   630  N  N     . PHE A 1 113 ? -14.225 12.872  43.13   1 16.765  ? 105  PHE A N     1 
ATOM   631  C  CA    . PHE A 1 113 ? -15.354 12.237  43.793  1 17.283  ? 105  PHE A CA    1 
ATOM   632  C  C     . PHE A 1 113 ? -16.278 13.344  44.311  1 19.162  ? 105  PHE A C     1 
ATOM   633  O  O     . PHE A 1 113 ? -15.89  14.171  45.15   1 18.148  ? 105  PHE A O     1 
ATOM   634  C  CB    . PHE A 1 113 ? -14.861 11.279  44.884  1 17.816  ? 105  PHE A CB    1 
ATOM   635  C  CG    . PHE A 1 113 ? -14.026 10.075  44.454  1 17.579  ? 105  PHE A CG    1 
ATOM   636  C  CD1   . PHE A 1 113 ? -12.685 10.216  44.042  1 17.587  ? 105  PHE A CD1   1 
ATOM   637  C  CD2   . PHE A 1 113 ? -14.568 8.781   44.52   1 18.075  ? 105  PHE A CD2   1 
ATOM   638  C  CE1   . PHE A 1 113 ? -11.91  9.095   43.677  1 17.888  ? 105  PHE A CE1   1 
ATOM   639  C  CE2   . PHE A 1 113 ? -13.798 7.656   44.168  1 18.307  ? 105  PHE A CE2   1 
ATOM   640  C  CZ    . PHE A 1 113 ? -12.475 7.817   43.723  1 17.755  ? 105  PHE A CZ    1 
ATOM   641  N  N     . LYS A 1 114 ? -17.496 13.374  43.758  1 19.506  ? 106  LYS A N     1 
ATOM   642  C  CA    . LYS A 1 114 ? -18.545 14.3    44.175  1 22.819  ? 106  LYS A CA    1 
ATOM   643  C  C     . LYS A 1 114 ? -19.886 13.581  44.053  1 22.482  ? 106  LYS A C     1 
ATOM   644  O  O     . LYS A 1 114 ? -20.227 13.124  42.965  1 22.234  ? 106  LYS A O     1 
ATOM   645  C  CB    . LYS A 1 114 ? -18.426 15.613  43.383  1 21.913  ? 106  LYS A CB    1 
ATOM   646  C  CG    . LYS A 1 114 ? -19.136 16.804  43.992  1 24.521  ? 106  LYS A CG    1 
ATOM   647  C  CD    . LYS A 1 114 ? -18.983 18.093  43.187  1 24.403  ? 106  LYS A CD    1 
ATOM   648  C  CE    . LYS A 1 114 ? -19.689 19.172  43.957  1 27.434  ? 106  LYS A CE    1 
ATOM   649  N  NZ    . LYS A 1 114 ? -20.253 20.227  43.104  1 31.009  ? 106  LYS A NZ    1 
ATOM   650  N  N     . ASP A 1 115 ? -20.587 13.417  45.193  1 25.226  ? 107  ASP A N     1 
ATOM   651  C  CA    . ASP A 1 115 ? -21.959 12.903  45.284  1 26.493  ? 107  ASP A CA    1 
ATOM   652  C  C     . ASP A 1 115 ? -22.092 11.497  44.67   1 24.741  ? 107  ASP A C     1 
ATOM   653  O  O     . ASP A 1 115 ? -23.074 11.216  43.976  1 25.889  ? 107  ASP A O     1 
ATOM   654  C  CB    . ASP A 1 115 ? -22.973 13.944  44.798  1 29.77   ? 107  ASP A CB    1 
ATOM   655  C  CG    . ASP A 1 115 ? -22.784 15.392  45.237  1 37.6    ? 107  ASP A CG    1 
ATOM   656  O  OD1   . ASP A 1 115 ? -22.623 15.639  46.454  1 43.673  ? 107  ASP A OD1   1 
ATOM   657  O  OD2   . ASP A 1 115 ? -22.824 16.278  44.354  1 41.599  ? 107  ASP A OD2   1 
ATOM   658  N  N     . GLY A 1 116 ? -21.087 10.629  44.9    1 22.602  ? 108  GLY A N     1 
ATOM   659  C  CA    . GLY A 1 116 ? -21.038 9.254   44.392  1 20.287  ? 108  GLY A CA    1 
ATOM   660  C  C     . GLY A 1 116 ? -20.552 9.103   42.939  1 18.85   ? 108  GLY A C     1 
ATOM   661  O  O     . GLY A 1 116 ? -20.467 7.975   42.469  1 19.911  ? 108  GLY A O     1 
ATOM   662  N  N     . LYS A 1 117 ? -20.227 10.203  42.244  1 17.35   ? 109  LYS A N     1 
ATOM   663  C  CA    . LYS A 1 117 ? -19.822 10.208  40.832  1 18.233  ? 109  LYS A CA    1 
ATOM   664  C  C     . LYS A 1 117 ? -18.333 10.544  40.696  1 17.838  ? 109  LYS A C     1 
ATOM   665  O  O     . LYS A 1 117 ? -17.821 11.355  41.476  1 17.158  ? 109  LYS A O     1 
ATOM   666  C  CB    . LYS A 1 117 ? -20.747 11.111  39.993  1 17.759  ? 109  LYS A CB    1 
ATOM   667  C  CG    . LYS A 1 117 ? -22.274 10.857  40.101  1 19.246  ? 109  LYS A CG    1 
ATOM   668  C  CD    . LYS A 1 117 ? -22.787 9.594   39.405  1 20.752  ? 109  LYS A CD    1 
ATOM   669  C  CE    . LYS A 1 117 ? -24.261 9.395   39.59   1 22.218  ? 109  LYS A CE    1 
ATOM   670  N  NZ    . LYS A 1 117 ? -24.61  8.136   38.911  1 25.2    ? 109  LYS A NZ    1 
ATOM   671  N  N     . VAL A 1 118 ? -17.658 9.93    39.696  1 17.782  ? 110  VAL A N     1 
ATOM   672  C  CA    . VAL A 1 118 ? -16.206 10.029  39.507  1 17.948  ? 110  VAL A CA    1 
ATOM   673  C  C     . VAL A 1 118 ? -15.918 10.588  38.109  1 18.059  ? 110  VAL A C     1 
ATOM   674  O  O     . VAL A 1 118 ? -16.411 10.042  37.128  1 16.552  ? 110  VAL A O     1 
ATOM   675  C  CB    . VAL A 1 118 ? -15.371 8.759   39.807  1 17.291  ? 110  VAL A CB    1 
ATOM   676  C  CG1   . VAL A 1 118 ? -13.867 9.012   39.862  1 18.148  ? 110  VAL A CG1   1 
ATOM   677  C  CG2   . VAL A 1 118 ? -15.781 8.035   41.091  1 18.816  ? 110  VAL A CG2   1 
ATOM   678  N  N     . ASP A 1 119 ? -15.074 11.635  38.044  1 16.557  ? 111  ASP A N     1 
ATOM   679  C  CA    . ASP A 1 119 ? -14.48  12.169  36.814  1 16.831  ? 111  ASP A CA    1 
ATOM   680  C  C     . ASP A 1 119 ? -12.973 11.928  36.81   1 16.147  ? 111  ASP A C     1 
ATOM   681  O  O     . ASP A 1 119 ? -12.363 11.825  37.873  1 14.713  ? 111  ASP A O     1 
ATOM   682  C  CB    . ASP A 1 119 ? -14.88  13.623  36.557  1 16.642  ? 111  ASP A CB    1 
ATOM   683  C  CG    . ASP A 1 119 ? -16.379 13.886  36.452  1 17.456  ? 111  ASP A CG    1 
ATOM   684  O  OD1   . ASP A 1 119 ? -17.096 13.011  35.925  1 18.009  ? 111  ASP A OD1   1 
ATOM   685  O  OD2   . ASP A 1 119 ? -16.818 14.99   36.821  1 16.594  ? 111  ASP A OD2   1 
ATOM   686  N  N     . TYR A 1 120 ? -12.406 11.846  35.597  1 16.805  ? 112  TYR A N     1 
ATOM   687  C  CA    . TYR A 1 120 ? -10.978 11.614  35.371  1 15.894  ? 112  TYR A CA    1 
ATOM   688  C  C     . TYR A 1 120 ? -10.411 12.666  34.427  1 15.772  ? 112  TYR A C     1 
ATOM   689  O  O     . TYR A 1 120 ? -11.041 12.954  33.418  1 16.036  ? 112  TYR A O     1 
ATOM   690  C  CB    . TYR A 1 120 ? -10.709 10.165  34.941  1 15.464  ? 112  TYR A CB    1 
ATOM   691  C  CG    . TYR A 1 120 ? -9.381  9.845   34.284  1 15.875  ? 112  TYR A CG    1 
ATOM   692  C  CD1   . TYR A 1 120 ? -8.265  9.504   35.052  1 15.28   ? 112  TYR A CD1   1 
ATOM   693  C  CD2   . TYR A 1 120 ? -9.253  9.883   32.885  1 17.234  ? 112  TYR A CD2   1 
ATOM   694  C  CE1   . TYR A 1 120 ? -7.041  9.201   34.455  1 16.916  ? 112  TYR A CE1   1 
ATOM   695  C  CE2   . TYR A 1 120 ? -8.036  9.572   32.276  1 17.583  ? 112  TYR A CE2   1 
ATOM   696  C  CZ    . TYR A 1 120 ? -6.948  9.22    33.066  1 18.297  ? 112  TYR A CZ    1 
ATOM   697  O  OH    . TYR A 1 120 ? -5.777  8.871   32.487  1 20.337  ? 112  TYR A OH    1 
ATOM   698  N  N     . ARG A 1 121 ? -9.214  13.186  34.772  1 16.133  ? 113  ARG A N     1 
ATOM   699  C  CA    . ARG A 1 121 ? -8.346  13.942  33.871  1 16.899  ? 113  ARG A CA    1 
ATOM   700  C  C     . ARG A 1 121 ? -6.895  13.506  34.063  1 18.385  ? 113  ARG A C     1 
ATOM   701  O  O     . ARG A 1 121 ? -6.448  13.322  35.204  1 19.166  ? 113  ARG A O     1 
ATOM   702  C  CB    . ARG A 1 121 ? -8.443  15.467  34.011  1 14.489  ? 113  ARG A CB    1 
ATOM   703  C  CG    . ARG A 1 121 ? -7.614  16.301  33.033  1 12.641  ? 113  ARG A CG    1 
ATOM   704  C  CD    . ARG A 1 121 ? -7.746  17.753  33.375  1 12.289  ? 113  ARG A CD    1 
ATOM   705  N  NE    . ARG A 1 121 ? -8.982  18.364  32.843  1 12.394  ? 113  ARG A NE    1 
ATOM   706  C  CZ    . ARG A 1 121 ? -9.233  18.763  31.592  1 12.204  ? 113  ARG A CZ    1 
ATOM   707  N  NH1   . ARG A 1 121 ? -8.387  18.558  30.596  1 13.158  ? 113  ARG A NH1   1 
ATOM   708  N  NH2   . ARG A 1 121 ? -10.364 19.375  31.335  1 12.081  ? 113  ARG A NH2   1 
ATOM   709  N  N     . GLN A 1 122 ? -6.189  13.397  32.929  1 18.041  ? 114  GLN A N     1 
ATOM   710  C  CA    . GLN A 1 122 ? -4.746  13.239  32.88   1 18.028  ? 114  GLN A CA    1 
ATOM   711  C  C     . GLN A 1 122 ? -4.111  14.319  32.007  1 17.908  ? 114  GLN A C     1 
ATOM   712  O  O     . GLN A 1 122 ? -4.601  14.61   30.91   1 18.167  ? 114  GLN A O     1 
ATOM   713  C  CB    . GLN A 1 122 ? -4.433  11.804  32.459  1 19.156  ? 114  GLN A CB    1 
ATOM   714  C  CG    . GLN A 1 122 ? -2.945  11.467  32.429  1 23.619  ? 114  GLN A CG    1 
ATOM   715  C  CD    . GLN A 1 122 ? -2.575  10.12   32.993  1 26.193  ? 114  GLN A CD    1 
ATOM   716  O  OE1   . GLN A 1 122 ? -3.406  9.343   33.472  1 25.271  ? 114  GLN A OE1   1 
ATOM   717  N  NE2   . GLN A 1 122 ? -1.285  9.849   32.941  1 30.867  ? 114  GLN A NE2   1 
ATOM   718  N  N     . ARG A 1 123 ? -2.982  14.859  32.5    1 16.614  ? 115  ARG A N     1 
ATOM   719  C  CA    . ARG A 1 123 ? -2.217  15.872  31.784  1 17.14   ? 115  ARG A CA    1 
ATOM   720  C  C     . ARG A 1 123 ? -0.767  15.876  32.256  1 16.9    ? 115  ARG A C     1 
ATOM   721  O  O     . ARG A 1 123 ? -0.496  15.718  33.451  1 16.091  ? 115  ARG A O     1 
ATOM   722  C  CB    . ARG A 1 123 ? -2.884  17.236  31.985  1 14.74   ? 115  ARG A CB    1 
ATOM   723  C  CG    . ARG A 1 123 ? -2.558  18.214  30.88   1 16.568  ? 115  ARG A CG    1 
ATOM   724  C  CD    . ARG A 1 123 ? -3.393  19.417  31.149  1 16.605  ? 115  ARG A CD    1 
ATOM   725  N  NE    . ARG A 1 123 ? -3.18   20.369  30.058  1 18.599  ? 115  ARG A NE    1 
ATOM   726  C  CZ    . ARG A 1 123 ? -3.948  21.43   29.762  1 22.68   ? 115  ARG A CZ    1 
ATOM   727  N  NH1   . ARG A 1 123 ? -5.04   21.742  30.456  1 22.517  ? 115  ARG A NH1   1 
ATOM   728  N  NH2   . ARG A 1 123 ? -3.595  22.216  28.762  1 23.215  ? 115  ARG A NH2   1 
ATOM   729  N  N     . PHE A 1 124 ? 0.123   16.114  31.285  1 16.076  ? 116  PHE A N     1 
ATOM   730  C  CA    . PHE A 1 124 ? 1.52    16.407  31.528  1 15.262  ? 116  PHE A CA    1 
ATOM   731  C  C     . PHE A 1 124 ? 1.677   17.768  32.194  1 13.81   ? 116  PHE A C     1 
ATOM   732  O  O     . PHE A 1 124 ? 1.04    18.738  31.792  1 15.072  ? 116  PHE A O     1 
ATOM   733  C  CB    . PHE A 1 124 ? 2.355   16.39   30.241  1 16.056  ? 116  PHE A CB    1 
ATOM   734  C  CG    . PHE A 1 124 ? 2.683   14.993  29.745  1 17.618  ? 116  PHE A CG    1 
ATOM   735  C  CD1   . PHE A 1 124 ? 3.521   14.15   30.498  1 18.243  ? 116  PHE A CD1   1 
ATOM   736  C  CD2   . PHE A 1 124 ? 2.177   14.537  28.514  1 17.888  ? 116  PHE A CD2   1 
ATOM   737  C  CE1   . PHE A 1 124 ? 3.816   12.868  30.039  1 19.916  ? 116  PHE A CE1   1 
ATOM   738  C  CE2   . PHE A 1 124 ? 2.477   13.257  28.045  1 19.24   ? 116  PHE A CE2   1 
ATOM   739  C  CZ    . PHE A 1 124 ? 3.313   12.419  28.806  1 19.259  ? 116  PHE A CZ    1 
ATOM   740  N  N     . VAL A 1 125 ? 2.598   17.814  33.159  1 13.89   ? 117  VAL A N     1 
ATOM   741  C  CA    . VAL A 1 125 ? 3.208   19.047  33.654  1 14.051  ? 117  VAL A CA    1 
ATOM   742  C  C     . VAL A 1 125 ? 4.012   19.668  32.501  1 14.498  ? 117  VAL A C     1 
ATOM   743  O  O     . VAL A 1 125 ? 4.88    19.003  31.912  1 15.09   ? 117  VAL A O     1 
ATOM   744  C  CB    . VAL A 1 125 ? 4.066   18.869  34.923  1 13.757  ? 117  VAL A CB    1 
ATOM   745  C  CG1   . VAL A 1 125 ? 4.37    20.225  35.549  1 14.433  ? 117  VAL A CG1   1 
ATOM   746  C  CG2   . VAL A 1 125 ? 3.412   17.989  35.979  1 13.829  ? 117  VAL A CG2   1 
ATOM   747  N  N     . GLU A 1 126 ? 3.719   20.945  32.198  1 14.495  ? 118  GLU A N     1 
ATOM   748  C  CA    . GLU A 1 126 ? 4.374   21.693  31.129  1 16.187  ? 118  GLU A CA    1 
ATOM   749  C  C     . GLU A 1 126 ? 5.675   22.295  31.677  1 17.264  ? 118  GLU A C     1 
ATOM   750  O  O     . GLU A 1 126 ? 5.868   23.517  31.681  1 16.254  ? 118  GLU A O     1 
ATOM   751  C  CB    . GLU A 1 126 ? 3.455   22.633  30.335  1 19.336  ? 118  GLU A CB    1 
ATOM   752  C  CG    . GLU A 1 126 ? 2.315   21.922  29.599  1 26.091  ? 118  GLU A CG    1 
ATOM   753  C  CD    . GLU A 1 126 ? 1.605   22.567  28.4    1 34.702  ? 118  GLU A CD    1 
ATOM   754  O  OE1   . GLU A 1 126 ? 1.504   23.832  28.407  1 28.352  ? 118  GLU A OE1   1 
ATOM   755  O  OE2   . GLU A 1 126 ? 1.1     21.787  27.493  1 36.436  ? 118  GLU A OE2   1 
ATOM   756  N  N     . THR A 1 127 ? 6.581   21.404  32.13   1 16.902  ? 119  THR A N     1 
ATOM   757  C  CA    . THR A 1 127 ? 7.923   21.761  32.592  1 17.385  ? 119  THR A CA    1 
ATOM   758  C  C     . THR A 1 127 ? 8.69    22.386  31.421  1 16.102  ? 119  THR A C     1 
ATOM   759  O  O     . THR A 1 127 ? 8.425   22.033  30.274  1 16.439  ? 119  THR A O     1 
ATOM   760  C  CB    . THR A 1 127 ? 8.699   20.586  33.205  1 17.311  ? 119  THR A CB    1 
ATOM   761  O  OG1   . THR A 1 127 ? 9.079   19.692  32.161  1 16.925  ? 119  THR A OG1   1 
ATOM   762  C  CG2   . THR A 1 127 ? 7.962   19.85   34.309  1 17.958  ? 119  THR A CG2   1 
ATOM   763  N  N     . ASP A 1 128 ? 9.631   23.295  31.722  1 15.906  ? 120  ASP A N     1 
ATOM   764  C  CA    . ASP A 1 128 ? 10.591  23.816  30.749  1 16.928  ? 120  ASP A CA    1 
ATOM   765  C  C     . ASP A 1 128 ? 11.21   22.721  29.879  1 15.431  ? 120  ASP A C     1 
ATOM   766  O  O     . ASP A 1 128 ? 11.26   22.897  28.669  1 14.621  ? 120  ASP A O     1 
ATOM   767  C  CB    . ASP A 1 128 ? 11.563  24.796  31.385  1 17.785  ? 120  ASP A CB    1 
ATOM   768  C  CG    . ASP A 1 128 ? 10.95   26.111  31.853  1 19.08   ? 120  ASP A CG    1 
ATOM   769  O  OD1   . ASP A 1 128 ? 9.764   26.398  31.514  1 18.57   ? 120  ASP A OD1   1 
ATOM   770  O  OD2   . ASP A 1 128 ? 11.66   26.841  32.577  1 20.065  ? 120  ASP A OD2   1 
ATOM   771  N  N     . ARG A 1 129 ? 11.588  21.589  30.503  1 15.806  ? 121  ARG A N     1 
ATOM   772  C  CA    . ARG A 1 129 ? 12.1    20.384  29.857  1 14.964  ? 121  ARG A CA    1 
ATOM   773  C  C     . ARG A 1 129 ? 11.07   19.79   28.89   1 15.968  ? 121  ARG A C     1 
ATOM   774  O  O     . ARG A 1 129 ? 11.413  19.509  27.737  1 16.195  ? 121  ARG A O     1 
ATOM   775  C  CB    . ARG A 1 129 ? 12.612  19.445  30.956  1 14.54   ? 121  ARG A CB    1 
ATOM   776  C  CG    . ARG A 1 129 ? 12.793  17.999  30.52   1 13.994  ? 121  ARG A CG    1 
ATOM   777  C  CD    . ARG A 1 129 ? 13.721  17.435  31.519  1 14.889  ? 121  ARG A CD    1 
ATOM   778  N  NE    . ARG A 1 129 ? 14.003  16.037  31.179  1 14.647  ? 121  ARG A NE    1 
ATOM   779  C  CZ    . ARG A 1 129 ? 14.753  15.198  31.872  1 14.452  ? 121  ARG A CZ    1 
ATOM   780  N  NH1   . ARG A 1 129 ? 15.457  15.598  32.928  1 15.64   ? 121  ARG A NH1   1 
ATOM   781  N  NH2   . ARG A 1 129 ? 14.801  13.939  31.487  1 13.977  ? 121  ARG A NH2   1 
ATOM   782  N  N     . PHE A 1 130 ? 9.838   19.543  29.377  1 17.295  ? 122  PHE A N     1 
ATOM   783  C  CA    . PHE A 1 130 ? 8.725   19.009  28.584  1 16.025  ? 122  PHE A CA    1 
ATOM   784  C  C     . PHE A 1 130 ? 8.488   19.845  27.322  1 15.49   ? 122  PHE A C     1 
ATOM   785  O  O     . PHE A 1 130 ? 8.371   19.286  26.222  1 16.988  ? 122  PHE A O     1 
ATOM   786  C  CB    . PHE A 1 130 ? 7.447   18.864  29.413  1 15.756  ? 122  PHE A CB    1 
ATOM   787  C  CG    . PHE A 1 130 ? 6.202   18.506  28.614  1 16.121  ? 122  PHE A CG    1 
ATOM   788  C  CD1   . PHE A 1 130 ? 5.895   17.167  28.313  1 15.851  ? 122  PHE A CD1   1 
ATOM   789  C  CD2   . PHE A 1 130 ? 5.339   19.523  28.151  1 16.936  ? 122  PHE A CD2   1 
ATOM   790  C  CE1   . PHE A 1 130 ? 4.744   16.854  27.568  1 15.82   ? 122  PHE A CE1   1 
ATOM   791  C  CE2   . PHE A 1 130 ? 4.182   19.21   27.422  1 16.444  ? 122  PHE A CE2   1 
ATOM   792  C  CZ    . PHE A 1 130 ? 3.888   17.875  27.147  1 16.948  ? 122  PHE A CZ    1 
ATOM   793  N  N     . LYS A 1 131 ? 8.417   21.167  27.514  1 14.908  ? 123  LYS A N     1 
ATOM   794  C  CA    . LYS A 1 131 ? 8.116   22.116  26.449  1 15.785  ? 123  LYS A CA    1 
ATOM   795  C  C     . LYS A 1 131 ? 9.204   22.132  25.371  1 17.103  ? 123  LYS A C     1 
ATOM   796  O  O     . LYS A 1 131 ? 8.863   22.087  24.193  1 18.431  ? 123  LYS A O     1 
ATOM   797  C  CB    . LYS A 1 131 ? 7.855   23.514  26.98   1 15.913  ? 123  LYS A CB    1 
ATOM   798  C  CG    . LYS A 1 131 ? 6.745   23.705  28.009  1 16.027  ? 123  LYS A CG    1 
ATOM   799  C  CD    . LYS A 1 131 ? 6.341   25.16   28.227  1 17.416  ? 123  LYS A CD    1 
ATOM   800  C  CE    . LYS A 1 131 ? 7.335   26.148  28.781  1 16.734  ? 123  LYS A CE    1 
ATOM   801  N  NZ    . LYS A 1 131 ? 8.289   26.555  27.742  1 16.473  ? 123  LYS A NZ    1 
ATOM   802  N  N     . VAL A 1 132 ? 10.481  22.1    25.78   1 16.665  ? 124  VAL A N     1 
ATOM   803  C  CA    . VAL A 1 132 ? 11.652  21.958  24.913  1 16.392  ? 124  VAL A CA    1 
ATOM   804  C  C     . VAL A 1 132 ? 11.521  20.701  24.045  1 16.73   ? 124  VAL A C     1 
ATOM   805  O  O     . VAL A 1 132 ? 11.598  20.805  22.818  1 17.155  ? 124  VAL A O     1 
ATOM   806  C  CB    . VAL A 1 132 ? 12.957  22.032  25.747  1 16.173  ? 124  VAL A CB    1 
ATOM   807  C  CG1   . VAL A 1 132 ? 14.158  21.356  25.076  1 17.691  ? 124  VAL A CG1   1 
ATOM   808  C  CG2   . VAL A 1 132 ? 13.311  23.468  26.141  1 15.506  ? 124  VAL A CG2   1 
ATOM   809  N  N     . GLU A 1 133 ? 11.271  19.552  24.691  1 16.785  ? 125  GLU A N     1 
ATOM   810  C  CA    . GLU A 1 133 ? 11.253  18.251  24.033  1 18.743  ? 125  GLU A CA    1 
ATOM   811  C  C     . GLU A 1 133 ? 10.076  18.107  23.061  1 19.241  ? 125  GLU A C     1 
ATOM   812  O  O     . GLU A 1 133 ? 10.272  17.508  22.003  1 18.623  ? 125  GLU A O     1 
ATOM   813  C  CB    . GLU A 1 133 ? 11.378  17.076  24.999  1 19.172  ? 125  GLU A CB    1 
ATOM   814  C  CG    . GLU A 1 133 ? 12.767  16.981  25.629  1 20.69   ? 125  GLU A CG    1 
ATOM   815  C  CD    . GLU A 1 133 ? 13.125  15.748  26.431  1 22.002  ? 125  GLU A CD    1 
ATOM   816  O  OE1   . GLU A 1 133 ? 12.237  14.905  26.757  1 21.422  ? 125  GLU A OE1   1 
ATOM   817  O  OE2   . GLU A 1 133 ? 14.356  15.602  26.667  1 20.702  ? 125  GLU A OE2   1 
ATOM   818  N  N     . ARG A 1 134 ? 8.893   18.641  23.435  1 18.383  ? 126  ARG A N     1 
ATOM   819  C  CA    . ARG A 1 134 ? 7.675   18.621  22.62   1 18.638  ? 126  ARG A CA    1 
ATOM   820  C  C     . ARG A 1 134 ? 7.86    19.453  21.347  1 18.07   ? 126  ARG A C     1 
ATOM   821  O  O     . ARG A 1 134 ? 7.62    18.929  20.262  1 18.993  ? 126  ARG A O     1 
ATOM   822  C  CB    . ARG A 1 134 ? 6.367   18.948  23.366  1 17.502  ? 126  ARG A CB    1 
ATOM   823  C  CG    . ARG A 1 134 ? 5.119   18.819  22.498  1 18.813  ? 126  ARG A CG    1 
ATOM   824  C  CD    . ARG A 1 134 ? 3.816   18.573  23.249  1 18.636  ? 126  ARG A CD    1 
ATOM   825  N  NE    . ARG A 1 134 ? 3.653   17.191  23.714  1 18.659  ? 126  ARG A NE    1 
ATOM   826  C  CZ    . ARG A 1 134 ? 2.589   16.638  24.316  1 19.59   ? 126  ARG A CZ    1 
ATOM   827  N  NH1   . ARG A 1 134 ? 1.457   17.302  24.52   1 21.13   ? 126  ARG A NH1   1 
ATOM   828  N  NH2   . ARG A 1 134 ? 2.677   15.399  24.765  1 19.267  ? 126  ARG A NH2   1 
ATOM   829  N  N     . ARG A 1 135 ? 8.27    20.723  21.508  1 18.5    ? 127  ARG A N     1 
ATOM   830  C  CA    . ARG A 1 135 ? 8.54    21.681  20.436  1 19.496  ? 127  ARG A CA    1 
ATOM   831  C  C     . ARG A 1 135 ? 9.566   21.167  19.418  1 20.123  ? 127  ARG A C     1 
ATOM   832  O  O     . ARG A 1 135 ? 9.412   21.438  18.23   1 20.232  ? 127  ARG A O     1 
ATOM   833  C  CB    . ARG A 1 135 ? 8.973   23.037  21.002  1 19.605  ? 127  ARG A CB    1 
ATOM   834  C  CG    . ARG A 1 135 ? 7.78    23.748  21.628  1 20.814  ? 127  ARG A CG    1 
ATOM   835  C  CD    . ARG A 1 135 ? 8.136   25.064  22.288  1 23.499  ? 127  ARG A CD    1 
ATOM   836  N  NE    . ARG A 1 135 ? 8.469   26.073  21.271  1 25.52   ? 127  ARG A NE    1 
ATOM   837  C  CZ    . ARG A 1 135 ? 7.673   26.688  20.375  1 28.648  ? 127  ARG A CZ    1 
ATOM   838  N  NH1   . ARG A 1 135 ? 6.356   26.674  20.482  1 26.72   ? 127  ARG A NH1   1 
ATOM   839  N  NH2   . ARG A 1 135 ? 8.216   27.361  19.376  1 28.591  ? 127  ARG A NH2   1 
ATOM   840  N  N     . ALA A 1 136 ? 10.588  20.428  19.89   1 19.449  ? 128  ALA A N     1 
ATOM   841  C  CA    . ALA A 1 136 ? 11.653  19.857  19.069  1 20.151  ? 128  ALA A CA    1 
ATOM   842  C  C     . ALA A 1 136 ? 11.299  18.482  18.487  1 21.237  ? 128  ALA A C     1 
ATOM   843  O  O     . ALA A 1 136 ? 12.008  18.029  17.587  1 23.903  ? 128  ALA A O     1 
ATOM   844  C  CB    . ALA A 1 136 ? 12.936  19.821  19.874  1 18.148  ? 128  ALA A CB    1 
ATOM   845  N  N     . ARG A 1 137 ? 10.237  17.818  19.002  1 22.542  ? 129  ARG A N     1 
ATOM   846  C  CA    . ARG A 1 137 ? 9.894   16.403  18.815  1 22.822  ? 129  ARG A CA    1 
ATOM   847  C  C     . ARG A 1 137 ? 11.117  15.489  19.065  1 19.964  ? 129  ARG A C     1 
ATOM   848  O  O     . ARG A 1 137 ? 11.397  14.576  18.282  1 18.931  ? 129  ARG A O     1 
ATOM   849  C  CB    . ARG A 1 137 ? 9.108   16.218  17.501  1 23.516  ? 129  ARG A CB    1 
ATOM   850  C  CG    . ARG A 1 137 ? 8.447   14.858  17.283  1 29.825  ? 129  ARG A CG    1 
ATOM   851  C  CD    . ARG A 1 137 ? 7.688   14.61   15.987  1 39.29   ? 129  ARG A CD    1 
ATOM   852  N  NE    . ARG A 1 137 ? 6.451   15.412  15.867  1 50.333  ? 129  ARG A NE    1 
ATOM   853  C  CZ    . ARG A 1 137 ? 5.141   15.065  15.918  1 44.877  ? 129  ARG A CZ    1 
ATOM   854  N  NH1   . ARG A 1 137 ? 4.762   13.835  16.212  1 46.145  ? 129  ARG A NH1   1 
ATOM   855  N  NH2   . ARG A 1 137 ? 4.191   15.945  15.607  1 36.616  ? 129  ARG A NH2   1 
ATOM   856  N  N     . LYS A 1 138 ? 11.886  15.779  20.128  1 19.755  ? 130  LYS A N     1 
ATOM   857  C  CA    . LYS A 1 138 ? 13.225  15.231  20.32   1 19.073  ? 130  LYS A CA    1 
ATOM   858  C  C     . LYS A 1 138 ? 13.629  15.347  21.781  1 18.682  ? 130  LYS A C     1 
ATOM   859  O  O     . LYS A 1 138 ? 13.502  16.422  22.369  1 17.237  ? 130  LYS A O     1 
ATOM   860  C  CB    . LYS A 1 138 ? 14.271  15.895  19.417  1 22.116  ? 130  LYS A CB    1 
ATOM   861  C  CG    . LYS A 1 138 ? 15.556  15.1    19.223  1 25.214  ? 130  LYS A CG    1 
ATOM   862  C  CD    . LYS A 1 138 ? 16.579  15.837  18.375  1 27.229  ? 130  LYS A CD    1 
ATOM   863  C  CE    . LYS A 1 138 ? 17.895  15.104  18.423  1 29.646  ? 130  LYS A CE    1 
ATOM   864  N  NZ    . LYS A 1 138 ? 18.933  15.73   17.604  1 29.459  ? 130  LYS A NZ    1 
ATOM   865  N  N     . SER A 1 139 ? 14.13   14.211  22.312  1 19.929  ? 131  SER A N     1 
ATOM   866  C  CA    . SER A 1 139 ? 14.865  14.099  23.566  1 18.319  ? 131  SER A CA    1 
ATOM   867  C  C     . SER A 1 139 ? 16.123  14.967  23.51   1 18.97   ? 131  SER A C     1 
ATOM   868  O  O     . SER A 1 139 ? 16.895  14.87   22.544  1 18.851  ? 131  SER A O     1 
ATOM   869  C  CB    . SER A 1 139 ? 15.232  12.655  23.833  1 17.628  ? 131  SER A CB    1 
ATOM   870  O  OG    . SER A 1 139 ? 16.007  12.531  25.022  1 16.49   ? 131  SER A OG    1 
ATOM   871  N  N     . MET A 1 140 ? 16.299  15.796  24.555  1 19.57   ? 132  MET A N     1 
ATOM   872  C  CA    . MET A 1 140 ? 17.406  16.748  24.674  1 20.14   ? 132  MET A CA    1 
ATOM   873  C  C     . MET A 1 140 ? 18.065  16.71   26.055  1 18.883  ? 132  MET A C     1 
ATOM   874  O  O     . MET A 1 140 ? 18.929  17.537  26.34   1 18.809  ? 132  MET A O     1 
ATOM   875  C  CB    . MET A 1 140 ? 17.023  18.133  24.135  1 24.306  ? 132  MET A CB    1 
ATOM   876  C  CG    . MET A 1 140 ? 17.27   18.179  22.617  1 30.592  ? 132  MET A CG    1 
ATOM   877  S  SD    . MET A 1 140 ? 16.619  19.635  21.818  1 46.325  ? 132  MET A SD    1 
ATOM   878  C  CE    . MET A 1 140 ? 17.882  20.881  22.109  1 36.422  ? 132  MET A CE    1 
ATOM   879  N  N     . TYR A 1 141 ? 17.689  15.712  26.868  1 16.544  ? 133  TYR A N     1 
ATOM   880  C  CA    . TYR A 1 141 ? 18.138  15.538  28.241  1 16.803  ? 133  TYR A CA    1 
ATOM   881  C  C     . TYR A 1 141 ? 18.67   14.121  28.403  1 17.837  ? 133  TYR A C     1 
ATOM   882  O  O     . TYR A 1 141 ? 18.113  13.161  27.828  1 16.933  ? 133  TYR A O     1 
ATOM   883  C  CB    . TYR A 1 141 ? 17.03   15.907  29.231  1 15.194  ? 133  TYR A CB    1 
ATOM   884  C  CG    . TYR A 1 141 ? 16.664  17.385  29.281  1 14.437  ? 133  TYR A CG    1 
ATOM   885  C  CD1   . TYR A 1 141 ? 15.799  17.957  28.334  1 14.892  ? 133  TYR A CD1   1 
ATOM   886  C  CD2   . TYR A 1 141 ? 17.14   18.209  30.311  1 14.942  ? 133  TYR A CD2   1 
ATOM   887  C  CE1   . TYR A 1 141 ? 15.468  19.311  28.367  1 14.996  ? 133  TYR A CE1   1 
ATOM   888  C  CE2   . TYR A 1 141 ? 16.797  19.565  30.376  1 14.821  ? 133  TYR A CE2   1 
ATOM   889  C  CZ    . TYR A 1 141 ? 15.95   20.104  29.405  1 15.149  ? 133  TYR A CZ    1 
ATOM   890  O  OH    . TYR A 1 141 ? 15.57   21.423  29.392  1 16.519  ? 133  TYR A OH    1 
ATOM   891  N  N     . GLY A 1 142 ? 19.759  14.04   29.188  1 17.738  ? 134  GLY A N     1 
ATOM   892  C  CA    . GLY A 1 142 ? 20.512  12.827  29.446  1 16.178  ? 134  GLY A CA    1 
ATOM   893  C  C     . GLY A 1 142 ? 20.11   12.16   30.753  1 16.84   ? 134  GLY A C     1 
ATOM   894  O  O     . GLY A 1 142 ? 18.917  11.943  31.015  1 16.12   ? 134  GLY A O     1 
ATOM   895  N  N     . LEU A 1 143 ? 21.149  11.832  31.532  1 15.269  ? 135  LEU A N     1 
ATOM   896  C  CA    . LEU A 1 143 ? 21.041  11.188  32.838  1 16.689  ? 135  LEU A CA    1 
ATOM   897  C  C     . LEU A 1 143 ? 20.324  12.063  33.862  1 16.735  ? 135  LEU A C     1 
ATOM   898  O  O     . LEU A 1 143 ? 20.395  13.302  33.799  1 17.573  ? 135  LEU A O     1 
ATOM   899  C  CB    . LEU A 1 143 ? 22.41   10.73   33.358  1 16.902  ? 135  LEU A CB    1 
ATOM   900  C  CG    . LEU A 1 143 ? 23.225  9.789   32.467  1 17.056  ? 135  LEU A CG    1 
ATOM   901  C  CD1   . LEU A 1 143 ? 24.531  9.483   33.199  1 18.075  ? 135  LEU A CD1   1 
ATOM   902  C  CD2   . LEU A 1 143 ? 22.497  8.496   32.017  1 16.919  ? 135  LEU A CD2   1 
ATOM   903  N  N     . TYR A 1 144 ? 19.639  11.366  34.789  1 18.203  ? 136  TYR A N     1 
ATOM   904  C  CA    . TYR A 1 144 ? 19.013  11.902  35.991  1 17.971  ? 136  TYR A CA    1 
ATOM   905  C  C     . TYR A 1 144 ? 19.987  12.861  36.669  1 18.884  ? 136  TYR A C     1 
ATOM   906  O  O     . TYR A 1 144 ? 21.11   12.465  37.003  1 18.796  ? 136  TYR A O     1 
ATOM   907  C  CB    . TYR A 1 144 ? 18.568  10.775  36.926  1 17.573  ? 136  TYR A CB    1 
ATOM   908  C  CG    . TYR A 1 144 ? 17.921  11.213  38.238  1 18.604  ? 136  TYR A CG    1 
ATOM   909  C  CD1   . TYR A 1 144 ? 16.576  11.616  38.282  1 19.264  ? 136  TYR A CD1   1 
ATOM   910  C  CD2   . TYR A 1 144 ? 18.651  11.191  39.444  1 18.639  ? 136  TYR A CD2   1 
ATOM   911  C  CE1   . TYR A 1 144 ? 15.99   12.009  39.482  1 19.31   ? 136  TYR A CE1   1 
ATOM   912  C  CE2   . TYR A 1 144 ? 18.056  11.539  40.656  1 19.232  ? 136  TYR A CE2   1 
ATOM   913  C  CZ    . TYR A 1 144 ? 16.733  11.985  40.66   1 20.028  ? 136  TYR A CZ    1 
ATOM   914  O  OH    . TYR A 1 144 ? 16.133  12.361  41.822  1 20.377  ? 136  TYR A OH    1 
ATOM   915  N  N     . ARG A 1 145 ? 19.568  14.142  36.74   1 17.907  ? 137  ARG A N     1 
ATOM   916  C  CA    . ARG A 1 145 ? 20.268  15.21   37.45   1 16.124  ? 137  ARG A CA    1 
ATOM   917  C  C     . ARG A 1 145 ? 21.697  15.451  36.928  1 16.211  ? 137  ARG A C     1 
ATOM   918  O  O     . ARG A 1 145 ? 22.565  15.902  37.69   1 16.318  ? 137  ARG A O     1 
ATOM   919  C  CB    . ARG A 1 145 ? 20.137  14.971  38.96   1 15.14   ? 137  ARG A CB    1 
ATOM   920  C  CG    . ARG A 1 145 ? 18.739  14.958  39.562  1 15.788  ? 137  ARG A CG    1 
ATOM   921  C  CD    . ARG A 1 145 ? 18.859  14.999  41.046  1 15.086  ? 137  ARG A CD    1 
ATOM   922  N  NE    . ARG A 1 145 ? 19.261  16.316  41.581  1 14.091  ? 137  ARG A NE    1 
ATOM   923  C  CZ    . ARG A 1 145 ? 19.027  16.761  42.812  1 14.026  ? 137  ARG A CZ    1 
ATOM   924  N  NH1   . ARG A 1 145 ? 18.443  16      43.739  1 14.15   ? 137  ARG A NH1   1 
ATOM   925  N  NH2   . ARG A 1 145 ? 19.349  18.008  43.095  1 14.784  ? 137  ARG A NH2   1 
ATOM   926  N  N     . ASN A 1 146 ? 21.946  15.171  35.633  1 15.859  ? 138  ASN A N     1 
ATOM   927  C  CA    . ASN A 1 146 ? 23.266  15.397  35.034  1 15.808  ? 138  ASN A CA    1 
ATOM   928  C  C     . ASN A 1 146 ? 23.182  16.336  33.825  1 15.538  ? 138  ASN A C     1 
ATOM   929  O  O     . ASN A 1 146 ? 23.182  15.845  32.69   1 14.786  ? 138  ASN A O     1 
ATOM   930  C  CB    . ASN A 1 146 ? 24.11   14.135  34.842  1 15.18   ? 138  ASN A CB    1 
ATOM   931  C  CG    . ASN A 1 146 ? 25.566  14.438  34.535  1 15.749  ? 138  ASN A CG    1 
ATOM   932  O  OD1   . ASN A 1 146 ? 25.972  15.604  34.441  1 15.664  ? 138  ASN A OD1   1 
ATOM   933  N  ND2   . ASN A 1 146 ? 26.388  13.399  34.414  1 14.334  ? 138  ASN A ND2   1 
ATOM   934  N  N     . PRO A 1 147 ? 23.202  17.688  34.034  1 16.351  ? 139  PRO A N     1 
ATOM   935  C  CA    . PRO A 1 147 ? 23.339  18.683  32.963  1 16.508  ? 139  PRO A CA    1 
ATOM   936  C  C     . PRO A 1 147 ? 24.506  18.527  31.989  1 17.029  ? 139  PRO A C     1 
ATOM   937  O  O     . PRO A 1 147 ? 24.345  18.936  30.846  1 17.026  ? 139  PRO A O     1 
ATOM   938  C  CB    . PRO A 1 147 ? 23.38   20.029  33.683  1 16.064  ? 139  PRO A CB    1 
ATOM   939  C  CG    . PRO A 1 147 ? 22.602  19.738  34.93   1 16.417  ? 139  PRO A CG    1 
ATOM   940  C  CD    . PRO A 1 147 ? 23.003  18.363  35.332  1 15.661  ? 139  PRO A CD    1 
ATOM   941  N  N     . TYR A 1 148 ? 25.618  17.887  32.421  1 16.608  ? 140  TYR A N     1 
ATOM   942  C  CA    . TYR A 1 148 ? 26.758  17.58   31.561  1 17.442  ? 140  TYR A CA    1 
ATOM   943  C  C     . TYR A 1 148 ? 26.394  16.588  30.45   1 17.38   ? 140  TYR A C     1 
ATOM   944  O  O     . TYR A 1 148 ? 27.103  16.582  29.435  1 17.618  ? 140  TYR A O     1 
ATOM   945  C  CB    . TYR A 1 148 ? 28.034  17.241  32.357  1 17.225  ? 140  TYR A CB    1 
ATOM   946  C  CG    . TYR A 1 148 ? 28.421  18.343  33.332  1 17.007  ? 140  TYR A CG    1 
ATOM   947  C  CD1   . TYR A 1 148 ? 29.107  19.479  32.884  1 17.477  ? 140  TYR A CD1   1 
ATOM   948  C  CD2   . TYR A 1 148 ? 28.039  18.283  34.683  1 18.997  ? 140  TYR A CD2   1 
ATOM   949  C  CE1   . TYR A 1 148 ? 29.421  20.511  33.761  1 17.903  ? 140  TYR A CE1   1 
ATOM   950  C  CE2   . TYR A 1 148 ? 28.366  19.304  35.577  1 18.703  ? 140  TYR A CE2   1 
ATOM   951  C  CZ    . TYR A 1 148 ? 29.044  20.42   35.097  1 17.492  ? 140  TYR A CZ    1 
ATOM   952  O  OH    . TYR A 1 148 ? 29.364  21.426  35.943  1 18.256  ? 140  TYR A OH    1 
ATOM   953  N  N     . THR A 1 149 ? 25.293  15.82   30.628  1 17.971  ? 141  THR A N     1 
ATOM   954  C  CA    . THR A 1 149 ? 24.763  14.852  29.649  1 17.824  ? 141  THR A CA    1 
ATOM   955  C  C     . THR A 1 149 ? 23.501  15.36   28.923  1 17.636  ? 141  THR A C     1 
ATOM   956  O  O     . THR A 1 149 ? 22.939  14.616  28.112  1 19.352  ? 141  THR A O     1 
ATOM   957  C  CB    . THR A 1 149 ? 24.55   13.464  30.272  1 17.512  ? 141  THR A CB    1 
ATOM   958  O  OG1   . THR A 1 149 ? 23.476  13.54   31.212  1 17.919  ? 141  THR A OG1   1 
ATOM   959  C  CG2   . THR A 1 149 ? 25.798  12.89   30.924  1 17.073  ? 141  THR A CG2   1 
ATOM   960  N  N     . HIS A 1 150 ? 23.07   16.613  29.181  1 16.893  ? 142  HIS A N     1 
ATOM   961  C  CA    . HIS A 1 150 ? 22.018  17.274  28.404  1 18.892  ? 142  HIS A CA    1 
ATOM   962  C  C     . HIS A 1 150 ? 22.644  17.91   27.156  1 18.999  ? 142  HIS A C     1 
ATOM   963  O  O     . HIS A 1 150 ? 23.847  18.178  27.15   1 19.545  ? 142  HIS A O     1 
ATOM   964  C  CB    . HIS A 1 150 ? 21.185  18.243  29.268  1 18.876  ? 142  HIS A CB    1 
ATOM   965  C  CG    . HIS A 1 150 ? 20.615  17.731  30.562  1 18.419  ? 142  HIS A CG    1 
ATOM   966  N  ND1   . HIS A 1 150 ? 20.408  16.4    30.877  1 18.605  ? 142  HIS A ND1   1 
ATOM   967  C  CD2   . HIS A 1 150 ? 20.22   18.417  31.645  1 17.657  ? 142  HIS A CD2   1 
ATOM   968  C  CE1   . HIS A 1 150 ? 19.92   16.291  32.1    1 17.9    ? 142  HIS A CE1   1 
ATOM   969  N  NE2   . HIS A 1 150 ? 19.79   17.5    32.587  1 18.534  ? 142  HIS A NE2   1 
ATOM   970  N  N     . HIS A 1 151 ? 21.827  18.129  26.104  1 18.445  ? 143  HIS A N     1 
ATOM   971  C  CA    . HIS A 1 151 ? 22.158  18.931  24.93   1 18.601  ? 143  HIS A CA    1 
ATOM   972  C  C     . HIS A 1 151 ? 22.699  20.308  25.355  1 17.955  ? 143  HIS A C     1 
ATOM   973  O  O     . HIS A 1 151 ? 22.117  20.904  26.271  1 18.264  ? 143  HIS A O     1 
ATOM   974  C  CB    . HIS A 1 151 ? 20.959  19.009  23.973  1 19.035  ? 143  HIS A CB    1 
ATOM   975  C  CG    . HIS A 1 151 ? 21.235  19.675  22.653  1 20.492  ? 143  HIS A CG    1 
ATOM   976  N  ND1   . HIS A 1 151 ? 21.466  21.029  22.51   1 20.885  ? 143  HIS A ND1   1 
ATOM   977  C  CD2   . HIS A 1 151 ? 21.282  19.179  21.409  1 20.457  ? 143  HIS A CD2   1 
ATOM   978  C  CE1   . HIS A 1 151 ? 21.677  21.319  21.238  1 21.023  ? 143  HIS A CE1   1 
ATOM   979  N  NE2   . HIS A 1 151 ? 21.564  20.211  20.552  1 20.861  ? 143  HIS A NE2   1 
ATOM   980  N  N     . PRO A 1 152 ? 23.828  20.827  24.768  1 19.589  ? 144  PRO A N     1 
ATOM   981  C  CA    . PRO A 1 152 ? 24.421  22.118  25.175  1 20.595  ? 144  PRO A CA    1 
ATOM   982  C  C     . PRO A 1 152 ? 23.466  23.306  25.309  1 20.33   ? 144  PRO A C     1 
ATOM   983  O  O     . PRO A 1 152 ? 23.616  24.087  26.236  1 20.54   ? 144  PRO A O     1 
ATOM   984  C  CB    . PRO A 1 152 ? 25.558  22.382  24.182  1 20.59   ? 144  PRO A CB    1 
ATOM   985  C  CG    . PRO A 1 152 ? 25.91   20.984  23.696  1 20.887  ? 144  PRO A CG    1 
ATOM   986  C  CD    . PRO A 1 152 ? 24.658  20.154  23.742  1 19.306  ? 144  PRO A CD    1 
ATOM   987  N  N     . CYS A 1 153 ? 22.45   23.365  24.436  1 20.967  ? 145  CYS A N     1 
ATOM   988  C  CA    . CYS A 1 153 ? 21.429  24.404  24.377  1 23.996  ? 145  CYS A CA    1 
ATOM   989  C  C     . CYS A 1 153 ? 20.517  24.438  25.61   1 22.907  ? 145  CYS A C     1 
ATOM   990  O  O     . CYS A 1 153 ? 19.886  25.464  25.838  1 23.538  ? 145  CYS A O     1 
ATOM   991  C  CB    . CYS A 1 153 ? 20.634  24.293  23.081  1 26.289  ? 145  CYS A CB    1 
ATOM   992  S  SG    . CYS A 1 153 ? 21.514  24.96   21.647  1 30.762  ? 145  CYS A SG    1 
ATOM   993  N  N     . VAL A 1 154 ? 20.441  23.343  26.392  1 22.012  ? 146  VAL A N     1 
ATOM   994  C  CA    . VAL A 1 154 ? 19.462  23.202  27.474  1 21.422  ? 146  VAL A CA    1 
ATOM   995  C  C     . VAL A 1 154 ? 20.129  23.059  28.847  1 21.592  ? 146  VAL A C     1 
ATOM   996  O  O     . VAL A 1 154 ? 19.432  22.859  29.849  1 22.7    ? 146  VAL A O     1 
ATOM   997  C  CB    . VAL A 1 154 ? 18.349  22.149  27.243  1 21.097  ? 146  VAL A CB    1 
ATOM   998  C  CG1   . VAL A 1 154 ? 17.608  22.38   25.933  1 23.917  ? 146  VAL A CG1   1 
ATOM   999  C  CG2   . VAL A 1 154 ? 18.841  20.712  27.306  1 19.687  ? 146  VAL A CG2   1 
ATOM   1000 N  N     . ARG A 1 155 ? 21.466  23.17   28.902  1 22.29   ? 147  ARG A N     1 
ATOM   1001 C  CA    . ARG A 1 155 ? 22.239  22.861  30.11   1 21.604  ? 147  ARG A CA    1 
ATOM   1002 C  C     . ARG A 1 155 ? 21.887  23.792  31.268  1 21.846  ? 147  ARG A C     1 
ATOM   1003 O  O     . ARG A 1 155 ? 21.915  23.346  32.41   1 21.933  ? 147  ARG A O     1 
ATOM   1004 C  CB    . ARG A 1 155 ? 23.753  22.818  29.904  1 20.418  ? 147  ARG A CB    1 
ATOM   1005 C  CG    . ARG A 1 155 ? 24.1    21.564  29.127  1 22.602  ? 147  ARG A CG    1 
ATOM   1006 C  CD    . ARG A 1 155 ? 25.583  21.449  28.994  1 26.167  ? 147  ARG A CD    1 
ATOM   1007 N  NE    . ARG A 1 155 ? 25.81   20.189  28.279  1 27.905  ? 147  ARG A NE    1 
ATOM   1008 C  CZ    . ARG A 1 155 ? 26.847  19.862  27.521  1 28.156  ? 147  ARG A CZ    1 
ATOM   1009 N  NH1   . ARG A 1 155 ? 27.951  20.59   27.544  1 26.136  ? 147  ARG A NH1   1 
ATOM   1010 N  NH2   . ARG A 1 155 ? 26.778  18.771  26.768  1 27.613  ? 147  ARG A NH2   1 
ATOM   1011 N  N     . GLN A 1 156 ? 21.526  25.046  30.941  1 22.807  ? 148  GLN A N     1 
ATOM   1012 C  CA    . GLN A 1 156 ? 21.189  26.074  31.915  1 24.336  ? 148  GLN A CA    1 
ATOM   1013 C  C     . GLN A 1 156 ? 19.672  26.262  32.109  1 22.852  ? 148  GLN A C     1 
ATOM   1014 O  O     . GLN A 1 156 ? 19.245  27.312  32.609  1 19.451  ? 148  GLN A O     1 
ATOM   1015 C  CB    . GLN A 1 156 ? 22.019  27.296  31.547  1 26.827  ? 148  GLN A CB    1 
ATOM   1016 C  CG    . GLN A 1 156 ? 22.675  27.934  32.763  1 30.934  ? 148  GLN A CG    1 
ATOM   1017 C  CD    . GLN A 1 156 ? 23.578  29.101  32.428  1 30.006  ? 148  GLN A CD    1 
ATOM   1018 O  OE1   . GLN A 1 156 ? 24.078  29.242  31.305  1 29.937  ? 148  GLN A OE1   1 
ATOM   1019 N  NE2   . GLN A 1 156 ? 23.806  29.936  33.431  1 29.87   ? 148  GLN A NE2   1 
ATOM   1020 N  N     . THR A 1 157 ? 18.885  25.212  31.786  1 21.468  ? 149  THR A N     1 
ATOM   1021 C  CA    . THR A 1 157 ? 17.447  25.15   32.043  1 19.67   ? 149  THR A CA    1 
ATOM   1022 C  C     . THR A 1 157 ? 17.201  24.525  33.417  1 18.73   ? 149  THR A C     1 
ATOM   1023 O  O     . THR A 1 157 ? 18.07   23.822  33.955  1 18.131  ? 149  THR A O     1 
ATOM   1024 C  CB    . THR A 1 157 ? 16.643  24.432  30.944  1 19.137  ? 149  THR A CB    1 
ATOM   1025 O  OG1   . THR A 1 157 ? 17.047  23.068  30.901  1 17.791  ? 149  THR A OG1   1 
ATOM   1026 C  CG2   . THR A 1 157 ? 16.714  25.092  29.576  1 19.6    ? 149  THR A CG2   1 
ATOM   1027 N  N     . VAL A 1 158 ? 15.984  24.767  33.955  1 16.171  ? 150  VAL A N     1 
ATOM   1028 C  CA    . VAL A 1 158 ? 15.395  23.896  34.967  1 16.174  ? 150  VAL A CA    1 
ATOM   1029 C  C     . VAL A 1 158 ? 15.11   22.534  34.311  1 15.884  ? 150  VAL A C     1 
ATOM   1030 O  O     . VAL A 1 158 ? 14.387  22.462  33.32   1 16.302  ? 150  VAL A O     1 
ATOM   1031 C  CB    . VAL A 1 158 ? 14.235  24.547  35.76   1 15.742  ? 150  VAL A CB    1 
ATOM   1032 C  CG1   . VAL A 1 158 ? 13.424  23.563  36.608  1 16.39   ? 150  VAL A CG1   1 
ATOM   1033 C  CG2   . VAL A 1 158 ? 14.78   25.626  36.68   1 14.814  ? 150  VAL A CG2   1 
ATOM   1034 N  N     . GLU A 1 159 ? 15.748  21.485  34.856  1 16.398  ? 151  GLU A N     1 
ATOM   1035 C  CA    . GLU A 1 159 ? 15.803  20.129  34.289  1 17.994  ? 151  GLU A CA    1 
ATOM   1036 C  C     . GLU A 1 159 ? 14.829  19.147  34.966  1 17.773  ? 151  GLU A C     1 
ATOM   1037 O  O     . GLU A 1 159 ? 14.797  17.956  34.602  1 20.094  ? 151  GLU A O     1 
ATOM   1038 C  CB    . GLU A 1 159 ? 17.238  19.588  34.263  1 18.916  ? 151  GLU A CB    1 
ATOM   1039 C  CG    . GLU A 1 159 ? 17.908  19.552  35.642  1 20.106  ? 151  GLU A CG    1 
ATOM   1040 C  CD    . GLU A 1 159 ? 18.629  18.289  36.059  1 21.808  ? 151  GLU A CD    1 
ATOM   1041 O  OE1   . GLU A 1 159 ? 19.027  17.432  35.227  1 20.787  ? 151  GLU A OE1   1 
ATOM   1042 O  OE2   . GLU A 1 159 ? 18.762  18.185  37.29   1 22.494  ? 151  GLU A OE2   1 
ATOM   1043 N  N     . SER A 1 160 ? 14.073  19.636  35.966  1 16.221  ? 152  SER A N     1 
ATOM   1044 C  CA    . SER A 1 160 ? 13.009  18.921  36.667  1 16.187  ? 152  SER A CA    1 
ATOM   1045 C  C     . SER A 1 160 ? 11.929  18.428  35.704  1 14.829  ? 152  SER A C     1 
ATOM   1046 O  O     . SER A 1 160 ? 11.462  19.201  34.856  1 15.897  ? 152  SER A O     1 
ATOM   1047 C  CB    . SER A 1 160 ? 12.393  19.786  37.711  1 16.354  ? 152  SER A CB    1 
ATOM   1048 O  OG    . SER A 1 160 ? 11.231  19.132  38.191  1 17.663  ? 152  SER A OG    1 
ATOM   1049 N  N     . THR A 1 161 ? 11.557  17.148  35.88   1 13.442  ? 153  THR A N     1 
ATOM   1050 C  CA    . THR A 1 161 ? 10.402  16.529  35.236  1 13.649  ? 153  THR A CA    1 
ATOM   1051 C  C     . THR A 1 161 ? 9.142   16.583  36.105  1 13.466  ? 153  THR A C     1 
ATOM   1052 O  O     . THR A 1 161 ? 8.099   16.113  35.649  1 14.592  ? 153  THR A O     1 
ATOM   1053 C  CB    . THR A 1 161 ? 10.665  15.121  34.714  1 13.074  ? 153  THR A CB    1 
ATOM   1054 O  OG1   . THR A 1 161 ? 11.229  14.379  35.798  1 12.808  ? 153  THR A OG1   1 
ATOM   1055 C  CG2   . THR A 1 161 ? 11.523  15.13   33.465  1 13.533  ? 153  THR A CG2   1 
ATOM   1056 N  N     . ALA A 1 162 ? 9.213   17.17   37.317  1 13.286  ? 154  ALA A N     1 
ATOM   1057 C  CA    . ALA A 1 162 ? 8.074   17.444  38.212  1 13.995  ? 154  ALA A CA    1 
ATOM   1058 C  C     . ALA A 1 162 ? 7.139   16.23   38.316  1 14.078  ? 154  ALA A C     1 
ATOM   1059 O  O     . ALA A 1 162 ? 5.975   16.326  37.932  1 14.579  ? 154  ALA A O     1 
ATOM   1060 C  CB    . ALA A 1 162 ? 7.34    18.724  37.765  1 13.305  ? 154  ALA A CB    1 
ATOM   1061 N  N     . ASN A 1 163 ? 7.676   15.077  38.777  1 15.254  ? 155  ASN A N     1 
ATOM   1062 C  CA    . ASN A 1 163 ? 7.042   13.769  38.566  1 15.797  ? 155  ASN A CA    1 
ATOM   1063 C  C     . ASN A 1 163 ? 6.8     12.971  39.855  1 16.253  ? 155  ASN A C     1 
ATOM   1064 O  O     . ASN A 1 163 ? 6.377   11.814  39.758  1 18.336  ? 155  ASN A O     1 
ATOM   1065 C  CB    . ASN A 1 163 ? 7.816   12.951  37.526  1 16.193  ? 155  ASN A CB    1 
ATOM   1066 C  CG    . ASN A 1 163 ? 9.171   12.434  37.968  1 18.222  ? 155  ASN A CG    1 
ATOM   1067 O  OD1   . ASN A 1 163 ? 9.676   12.745  39.064  1 15.919  ? 155  ASN A OD1   1 
ATOM   1068 N  ND2   . ASN A 1 163 ? 9.78    11.626  37.11   1 19.27   ? 155  ASN A ND2   1 
ATOM   1069 N  N     . THR A 1 164 ? 7.088   13.558  41.035  1 15.813  ? 156  THR A N     1 
ATOM   1070 C  CA    . THR A 1 164 ? 7.287   12.797  42.264  1 16.055  ? 156  THR A CA    1 
ATOM   1071 C  C     . THR A 1 164 ? 6.052   12.818  43.17   1 15.816  ? 156  THR A C     1 
ATOM   1072 O  O     . THR A 1 164 ? 5.624   11.741  43.612  1 15.214  ? 156  THR A O     1 
ATOM   1073 C  CB    . THR A 1 164 ? 8.574   13.199  42.991  1 17.051  ? 156  THR A CB    1 
ATOM   1074 O  OG1   . THR A 1 164 ? 9.648   13.106  42.06   1 16.874  ? 156  THR A OG1   1 
ATOM   1075 C  CG2   . THR A 1 164 ? 8.886   12.323  44.193  1 18.113  ? 156  THR A CG2   1 
ATOM   1076 N  N     . ASN A 1 165 ? 5.538   14.022  43.487  1 15.807  ? 157  ASN A N     1 
ATOM   1077 C  CA    . ASN A 1 165 ? 4.488   14.231  44.481  1 16.614  ? 157  ASN A CA    1 
ATOM   1078 C  C     . ASN A 1 165 ? 3.716   15.516  44.169  1 16.511  ? 157  ASN A C     1 
ATOM   1079 O  O     . ASN A 1 165 ? 4.186   16.35   43.399  1 15.172  ? 157  ASN A O     1 
ATOM   1080 C  CB    . ASN A 1 165 ? 5.016   14.091  45.917  1 17.633  ? 157  ASN A CB    1 
ATOM   1081 C  CG    . ASN A 1 165 ? 3.949   13.925  46.987  1 18.185  ? 157  ASN A CG    1 
ATOM   1082 O  OD1   . ASN A 1 165 ? 2.782   13.593  46.719  1 17.82   ? 157  ASN A OD1   1 
ATOM   1083 N  ND2   . ASN A 1 165 ? 4.348   14.118  48.234  1 19.513  ? 157  ASN A ND2   1 
ATOM   1084 N  N     . VAL A 1 166 ? 2.516   15.636  44.77   1 16.337  ? 158  VAL A N     1 
ATOM   1085 C  CA    . VAL A 1 166 ? 1.608   16.77   44.637  1 16.852  ? 158  VAL A CA    1 
ATOM   1086 C  C     . VAL A 1 166 ? 1.243   17.292  46.031  1 17.654  ? 158  VAL A C     1 
ATOM   1087 O  O     . VAL A 1 166 ? 1.318   16.547  47.025  1 18.887  ? 158  VAL A O     1 
ATOM   1088 C  CB    . VAL A 1 166 ? 0.366   16.552  43.731  1 17.291  ? 158  VAL A CB    1 
ATOM   1089 C  CG1   . VAL A 1 166 ? 0.749   16.17   42.299  1 17.339  ? 158  VAL A CG1   1 
ATOM   1090 C  CG2   . VAL A 1 166 ? -0.618  15.525  44.294  1 15.681  ? 158  VAL A CG2   1 
ATOM   1091 N  N     . VAL A 1 167 ? 0.852   18.576  46.083  1 16.562  ? 159  VAL A N     1 
ATOM   1092 C  CA    . VAL A 1 167 ? 0.36    19.232  47.289  1 15.333  ? 159  VAL A CA    1 
ATOM   1093 C  C     . VAL A 1 167 ? -0.563  20.384  46.89   1 14.887  ? 159  VAL A C     1 
ATOM   1094 O  O     . VAL A 1 167 ? -0.341  21.04   45.856  1 15.5    ? 159  VAL A O     1 
ATOM   1095 C  CB    . VAL A 1 167 ? 1.487   19.629  48.281  1 16.428  ? 159  VAL A CB    1 
ATOM   1096 C  CG1   . VAL A 1 167 ? 2.368   20.805  47.836  1 15.307  ? 159  VAL A CG1   1 
ATOM   1097 C  CG2   . VAL A 1 167 ? 0.984   19.794  49.721  1 16.89   ? 159  VAL A CG2   1 
ATOM   1098 N  N     . MET A 1 168 ? -1.621  20.532  47.696  1 13.756  ? 160  MET A N     1 
ATOM   1099 C  CA    . MET A 1 168 ? -2.465  21.715  47.744  1 15.255  ? 160  MET A CA    1 
ATOM   1100 C  C     . MET A 1 168 ? -2.179  22.478  49.044  1 14.581  ? 160  MET A C     1 
ATOM   1101 O  O     . MET A 1 168 ? -2.496  22.012  50.15   1 14.47   ? 160  MET A O     1 
ATOM   1102 C  CB    . MET A 1 168 ? -3.947  21.325  47.616  1 15.789  ? 160  MET A CB    1 
ATOM   1103 C  CG    . MET A 1 168 ? -4.937  22.494  47.634  1 15.984  ? 160  MET A CG    1 
ATOM   1104 S  SD    . MET A 1 168 ? -4.918  23.472  46.12   1 18.332  ? 160  MET A SD    1 
ATOM   1105 C  CE    . MET A 1 168 ? -5.833  22.314  45.09   1 17.771  ? 160  MET A CE    1 
ATOM   1106 N  N     . HIS A 1 169 ? -1.624  23.68   48.87   1 14.443  ? 161  HIS A N     1 
ATOM   1107 C  CA    . HIS A 1 169 ? -1.233  24.552  49.969  1 15.721  ? 161  HIS A CA    1 
ATOM   1108 C  C     . HIS A 1 169 ? -1.565  25.99   49.607  1 16.028  ? 161  HIS A C     1 
ATOM   1109 O  O     . HIS A 1 169 ? -1.174  26.451  48.525  1 18.683  ? 161  HIS A O     1 
ATOM   1110 C  CB    . HIS A 1 169 ? 0.255   24.392  50.331  1 16.319  ? 161  HIS A CB    1 
ATOM   1111 C  CG    . HIS A 1 169 ? 0.588   25.171  51.566  1 18.601  ? 161  HIS A CG    1 
ATOM   1112 N  ND1   . HIS A 1 169 ? 0.197   24.752  52.825  1 19.331  ? 161  HIS A ND1   1 
ATOM   1113 C  CD2   . HIS A 1 169 ? 1.168   26.377  51.727  1 18.064  ? 161  HIS A CD2   1 
ATOM   1114 C  CE1   . HIS A 1 169 ? 0.559   25.667  53.717  1 19.592  ? 161  HIS A CE1   1 
ATOM   1115 N  NE2   . HIS A 1 169 ? 1.156   26.655  53.073  1 19.232  ? 161  HIS A NE2   1 
ATOM   1116 N  N     . ALA A 1 170 ? -2.249  26.682  50.549  1 15.744  ? 162  ALA A N     1 
ATOM   1117 C  CA    . ALA A 1 170 ? -2.671  28.082  50.439  1 16.144  ? 162  ALA A CA    1 
ATOM   1118 C  C     . ALA A 1 170 ? -3.364  28.352  49.092  1 15.577  ? 162  ALA A C     1 
ATOM   1119 O  O     . ALA A 1 170 ? -3.063  29.33   48.396  1 16.053  ? 162  ALA A O     1 
ATOM   1120 C  CB    . ALA A 1 170 ? -1.485  29.012  50.738  1 16.723  ? 162  ALA A CB    1 
ATOM   1121 N  N     . GLY A 1 171 ? -4.292  27.443  48.732  1 16.005  ? 163  GLY A N     1 
ATOM   1122 C  CA    . GLY A 1 171 ? -5.096  27.47   47.512  1 16.69   ? 163  GLY A CA    1 
ATOM   1123 C  C     . GLY A 1 171 ? -4.285  27.283  46.223  1 18.893  ? 163  GLY A C     1 
ATOM   1124 O  O     . GLY A 1 171 ? -4.76   27.674  45.159  1 19.386  ? 163  GLY A O     1 
ATOM   1125 N  N     . ARG A 1 172 ? -3.071  26.711  46.319  1 18.379  ? 164  ARG A N     1 
ATOM   1126 C  CA    . ARG A 1 172 ? -2.162  26.518  45.189  1 19.397  ? 164  ARG A CA    1 
ATOM   1127 C  C     . ARG A 1 172 ? -1.812  25.035  45.073  1 18.83   ? 164  ARG A C     1 
ATOM   1128 O  O     . ARG A 1 172 ? -1.451  24.417  46.078  1 18.626  ? 164  ARG A O     1 
ATOM   1129 C  CB    . ARG A 1 172 ? -0.929  27.424  45.266  1 20.406  ? 164  ARG A CB    1 
ATOM   1130 C  CG    . ARG A 1 172 ? -1.24   28.919  45.244  1 25.702  ? 164  ARG A CG    1 
ATOM   1131 C  CD    . ARG A 1 172 ? 0.022   29.407  44.687  1 31.115  ? 164  ARG A CD    1 
ATOM   1132 N  NE    . ARG A 1 172 ? 0.189   30.847  44.812  1 32.527  ? 164  ARG A NE    1 
ATOM   1133 C  CZ    . ARG A 1 172 ? 0.688   31.644  43.894  1 32.172  ? 164  ARG A CZ    1 
ATOM   1134 N  NH1   . ARG A 1 172 ? 0.736   31.325  42.604  1 27.196  ? 164  ARG A NH1   1 
ATOM   1135 N  NH2   . ARG A 1 172 ? 1.107   32.822  44.306  1 35.518  ? 164  ARG A NH2   1 
ATOM   1136 N  N     . PHE A 1 173 ? -1.935  24.516  43.84   1 18.187  ? 165  PHE A N     1 
ATOM   1137 C  CA    . PHE A 1 173 ? -1.68   23.122  43.5    1 17.718  ? 165  PHE A CA    1 
ATOM   1138 C  C     . PHE A 1 173 ? -0.338  23      42.785  1 17.88   ? 165  PHE A C     1 
ATOM   1139 O  O     . PHE A 1 173 ? -0.16   23.593  41.723  1 20.448  ? 165  PHE A O     1 
ATOM   1140 C  CB    . PHE A 1 173 ? -2.86   22.476  42.76   1 17.086  ? 165  PHE A CB    1 
ATOM   1141 C  CG    . PHE A 1 173 ? -2.685  20.995  42.448  1 15.553  ? 165  PHE A CG    1 
ATOM   1142 C  CD1   . PHE A 1 173 ? -2.801  20.025  43.453  1 14.799  ? 165  PHE A CD1   1 
ATOM   1143 C  CD2   . PHE A 1 173 ? -2.451  20.578  41.136  1 15.509  ? 165  PHE A CD2   1 
ATOM   1144 C  CE1   . PHE A 1 173 ? -2.673  18.662  43.154  1 14.435  ? 165  PHE A CE1   1 
ATOM   1145 C  CE2   . PHE A 1 173 ? -2.32   19.22   40.833  1 15.438  ? 165  PHE A CE2   1 
ATOM   1146 C  CZ    . PHE A 1 173 ? -2.413  18.271  41.848  1 14.779  ? 165  PHE A CZ    1 
ATOM   1147 N  N     . LEU A 1 174 ? 0.555   22.191  43.383  1 17.048  ? 166  LEU A N     1 
ATOM   1148 C  CA    . LEU A 1 174 ? 1.966   22.047  43.048  1 16.895  ? 166  LEU A CA    1 
ATOM   1149 C  C     . LEU A 1 174 ? 2.264   20.616  42.616  1 16.396  ? 166  LEU A C     1 
ATOM   1150 O  O     . LEU A 1 174 ? 1.828   19.666  43.271  1 16.87   ? 166  LEU A O     1 
ATOM   1151 C  CB    . LEU A 1 174 ? 2.824   22.417  44.267  1 16.688  ? 166  LEU A CB    1 
ATOM   1152 C  CG    . LEU A 1 174 ? 3.107   23.902  44.562  1 16.465  ? 166  LEU A CG    1 
ATOM   1153 C  CD1   . LEU A 1 174 ? 1.919   24.819  44.877  1 17.715  ? 166  LEU A CD1   1 
ATOM   1154 C  CD2   . LEU A 1 174 ? 4.05    23.949  45.772  1 14.793  ? 166  LEU A CD2   1 
ATOM   1155 N  N     . ALA A 1 175 ? 3.03    20.504  41.518  1 16.375  ? 167  ALA A N     1 
ATOM   1156 C  CA    . ALA A 1 175 ? 3.731   19.3    41.104  1 17.321  ? 167  ALA A CA    1 
ATOM   1157 C  C     . ALA A 1 175 ? 5.206   19.485  41.437  1 17.051  ? 167  ALA A C     1 
ATOM   1158 O  O     . ALA A 1 175 ? 5.777   20.506  41.076  1 15.724  ? 167  ALA A O     1 
ATOM   1159 C  CB    . ALA A 1 175 ? 3.51    19.043  39.627  1 16.671  ? 167  ALA A CB    1 
ATOM   1160 N  N     . MET A 1 176 ? 5.801   18.462  42.07   1 16.537  ? 168  MET A N     1 
ATOM   1161 C  CA    . MET A 1 176 ? 7.082   18.565  42.765  1 16.477  ? 168  MET A CA    1 
ATOM   1162 C  C     . MET A 1 176 ? 8.047   17.473  42.311  1 16.015  ? 168  MET A C     1 
ATOM   1163 O  O     . MET A 1 176 ? 7.645   16.36   41.971  1 15.641  ? 168  MET A O     1 
ATOM   1164 C  CB    . MET A 1 176 ? 6.896   18.461  44.283  1 17.849  ? 168  MET A CB    1 
ATOM   1165 C  CG    . MET A 1 176 ? 5.959   19.5    44.914  1 18.22   ? 168  MET A CG    1 
ATOM   1166 S  SD    . MET A 1 176 ? 5.774   19.227  46.687  1 19.519  ? 168  MET A SD    1 
ATOM   1167 C  CE    . MET A 1 176 ? 4.683   17.807  46.807  1 19.138  ? 168  MET A CE    1 
ATOM   1168 N  N     . LYS A 1 177 ? 9.336   17.844  42.319  1 16.004  ? 169  LYS A N     1 
ATOM   1169 C  CA    . LYS A 1 177 ? 10.502  16.979  42.164  1 14.519  ? 169  LYS A CA    1 
ATOM   1170 C  C     . LYS A 1 177 ? 11.69   17.705  42.781  1 13.438  ? 169  LYS A C     1 
ATOM   1171 O  O     . LYS A 1 177 ? 11.855  18.911  42.55   1 13.102  ? 169  LYS A O     1 
ATOM   1172 C  CB    . LYS A 1 177 ? 10.77   16.582  40.704  1 14.288  ? 169  LYS A CB    1 
ATOM   1173 C  CG    . LYS A 1 177 ? 11.784  15.457  40.497  1 13.793  ? 169  LYS A CG    1 
ATOM   1174 C  CD    . LYS A 1 177 ? 12.03   15.15   39.017  1 16.063  ? 169  LYS A CD    1 
ATOM   1175 C  CE    . LYS A 1 177 ? 12.98   13.99   38.828  1 17.319  ? 169  LYS A CE    1 
ATOM   1176 N  NZ    . LYS A 1 177 ? 12.446  12.723  39.368  1 15.885  ? 169  LYS A NZ    1 
ATOM   1177 N  N     . GLU A 1 178 ? 12.509  16.941  43.521  1 14.365  ? 170  GLU A N     1 
ATOM   1178 C  CA    . GLU A 1 178 ? 13.532  17.436  44.449  1 15.403  ? 170  GLU A CA    1 
ATOM   1179 C  C     . GLU A 1 178 ? 14.66   18.25   43.802  1 14.579  ? 170  GLU A C     1 
ATOM   1180 O  O     . GLU A 1 178 ? 15.36   18.948  44.548  1 15.453  ? 170  GLU A O     1 
ATOM   1181 C  CB    . GLU A 1 178 ? 14.073  16.381  45.426  1 15.857  ? 170  GLU A CB    1 
ATOM   1182 C  CG    . GLU A 1 178 ? 14.893  15.26   44.791  1 15.829  ? 170  GLU A CG    1 
ATOM   1183 C  CD    . GLU A 1 178 ? 14.71   14.048  45.666  1 17.305  ? 170  GLU A CD    1 
ATOM   1184 O  OE1   . GLU A 1 178 ? 13.624  13.404  45.64   1 20.631  ? 170  GLU A OE1   1 
ATOM   1185 O  OE2   . GLU A 1 178 ? 15.65   13.783  46.42   1 17.537  ? 170  GLU A OE2   1 
ATOM   1186 N  N     . ASN A 1 179 ? 14.846  18.156  42.467  1 15.135  ? 171  ASN A N     1 
ATOM   1187 C  CA    . ASN A 1 179 ? 15.913  18.848  41.732  1 15.442  ? 171  ASN A CA    1 
ATOM   1188 C  C     . ASN A 1 179 ? 15.48   20.239  41.23   1 15.835  ? 171  ASN A C     1 
ATOM   1189 O  O     . ASN A 1 179 ? 16.223  20.877  40.474  1 17.172  ? 171  ASN A O     1 
ATOM   1190 C  CB    . ASN A 1 179 ? 16.511  17.961  40.636  1 14.627  ? 171  ASN A CB    1 
ATOM   1191 C  CG    . ASN A 1 179 ? 15.532  17.536  39.567  1 15.244  ? 171  ASN A CG    1 
ATOM   1192 O  OD1   . ASN A 1 179 ? 14.324  17.502  39.809  1 15.416  ? 171  ASN A OD1   1 
ATOM   1193 N  ND2   . ASN A 1 179 ? 16.023  17.193  38.385  1 14.944  ? 171  ASN A ND2   1 
ATOM   1194 N  N     . GLY A 1 180 ? 14.326  20.739  41.694  1 16.03   ? 172  GLY A N     1 
ATOM   1195 C  CA    . GLY A 1 180 ? 13.843  22.08   41.373  1 16.188  ? 172  GLY A CA    1 
ATOM   1196 C  C     . GLY A 1 180 ? 12.713  22.531  42.296  1 15.546  ? 172  GLY A C     1 
ATOM   1197 O  O     . GLY A 1 180 ? 12.195  21.762  43.108  1 16.817  ? 172  GLY A O     1 
ATOM   1198 N  N     . ASN A 1 181 ? 12.33   23.799  42.142  1 15.371  ? 173  ASN A N     1 
ATOM   1199 C  CA    . ASN A 1 181 ? 11.069  24.304  42.672  1 15.119  ? 173  ASN A CA    1 
ATOM   1200 C  C     . ASN A 1 181 ? 9.901   23.633  41.953  1 15.117  ? 173  ASN A C     1 
ATOM   1201 O  O     . ASN A 1 181 ? 10.067  23.043  40.875  1 15.521  ? 173  ASN A O     1 
ATOM   1202 C  CB    . ASN A 1 181 ? 11.08   25.822  42.829  1 14.633  ? 173  ASN A CB    1 
ATOM   1203 C  CG    . ASN A 1 181 ? 11.876  26.238  44.044  1 13.892  ? 173  ASN A CG    1 
ATOM   1204 O  OD1   . ASN A 1 181 ? 11.419  26.048  45.181  1 13.794  ? 173  ASN A OD1   1 
ATOM   1205 N  ND2   . ASN A 1 181 ? 13.042  26.839  43.82   1 13.008  ? 173  ASN A ND2   1 
ATOM   1206 N  N     . ALA A 1 182 ? 8.746   23.655  42.622  1 15.149  ? 174  ALA A N     1 
ATOM   1207 C  CA    . ALA A 1 182 ? 7.496   23.121  42.092  1 16.534  ? 174  ALA A CA    1 
ATOM   1208 C  C     . ALA A 1 182 ? 6.997   23.914  40.887  1 16.375  ? 174  ALA A C     1 
ATOM   1209 O  O     . ALA A 1 182 ? 7.289   25.103  40.745  1 18.201  ? 174  ALA A O     1 
ATOM   1210 C  CB    . ALA A 1 182 ? 6.477   23.086  43.184  1 16.433  ? 174  ALA A CB    1 
ATOM   1211 N  N     . TYR A 1 183 ? 6.27    23.211  40.007  1 16.37   ? 175  TYR A N     1 
ATOM   1212 C  CA    . TYR A 1 183 ? 5.4     23.819  39.017  1 16.984  ? 175  TYR A CA    1 
ATOM   1213 C  C     . TYR A 1 183 ? 3.962   23.824  39.529  1 17.305  ? 175  TYR A C     1 
ATOM   1214 O  O     . TYR A 1 183 ? 3.479   22.819  40.056  1 18.015  ? 175  TYR A O     1 
ATOM   1215 C  CB    . TYR A 1 183 ? 5.524   23.082  37.685  1 16.327  ? 175  TYR A CB    1 
ATOM   1216 C  CG    . TYR A 1 183 ? 6.825   23.287  36.919  1 15.566  ? 175  TYR A CG    1 
ATOM   1217 C  CD1   . TYR A 1 183 ? 7.942   22.472  37.156  1 15.25   ? 175  TYR A CD1   1 
ATOM   1218 C  CD2   . TYR A 1 183 ? 6.903   24.244  35.898  1 15.513  ? 175  TYR A CD2   1 
ATOM   1219 C  CE1   . TYR A 1 183 ? 9.121   22.632  36.42   1 14.985  ? 175  TYR A CE1   1 
ATOM   1220 C  CE2   . TYR A 1 183 ? 8.076   24.408  35.155  1 15.759  ? 175  TYR A CE2   1 
ATOM   1221 C  CZ    . TYR A 1 183 ? 9.181   23.598  35.422  1 14.307  ? 175  TYR A CZ    1 
ATOM   1222 O  OH    . TYR A 1 183 ? 10.324  23.746  34.691  1 15.523  ? 175  TYR A OH    1 
ATOM   1223 N  N     . GLU A 1 184 ? 3.304   24.977  39.339  1 17.991  ? 176  GLU A N     1 
ATOM   1224 C  CA    . GLU A 1 184 ? 1.906   25.204  39.682  1 17.606  ? 176  GLU A CA    1 
ATOM   1225 C  C     . GLU A 1 184 ? 1.02    24.814  38.504  1 16.975  ? 176  GLU A C     1 
ATOM   1226 O  O     . GLU A 1 184 ? 1.305   25.151  37.353  1 16.583  ? 176  GLU A O     1 
ATOM   1227 C  CB    . GLU A 1 184 ? 1.616   26.645  40.101  1 19.43   ? 176  GLU A CB    1 
ATOM   1228 C  CG    . GLU A 1 184 ? 0.268   26.822  40.801  1 21.164  ? 176  GLU A CG    1 
ATOM   1229 C  CD    . GLU A 1 184 ? -0.253  28.215  41.128  1 22.364  ? 176  GLU A CD    1 
ATOM   1230 O  OE1   . GLU A 1 184 ? 0.378   29.227  40.781  1 23.923  ? 176  GLU A OE1   1 
ATOM   1231 O  OE2   . GLU A 1 184 ? -1.314  28.289  41.778  1 23.552  ? 176  GLU A OE2   1 
ATOM   1232 N  N     . MET A 1 185 ? -0.079  24.136  38.859  1 17.491  ? 177  MET A N     1 
ATOM   1233 C  CA    . MET A 1 185 ? -1.104  23.667  37.939  1 17.222  ? 177  MET A CA    1 
ATOM   1234 C  C     . MET A 1 185 ? -2.477  24.106  38.449  1 17.929  ? 177  MET A C     1 
ATOM   1235 O  O     . MET A 1 185 ? -2.709  24.165  39.669  1 16.179  ? 177  MET A O     1 
ATOM   1236 C  CB    . MET A 1 185 ? -1.065  22.144  37.754  1 16.77   ? 177  MET A CB    1 
ATOM   1237 C  CG    . MET A 1 185 ? 0.249   21.595  37.208  1 17.314  ? 177  MET A CG    1 
ATOM   1238 S  SD    . MET A 1 185 ? 0.353   19.804  37.427  1 19.824  ? 177  MET A SD    1 
ATOM   1239 C  CE    . MET A 1 185 ? -0.312  19.244  35.863  1 17.787  ? 177  MET A CE    1 
ATOM   1240 N  N     . ASP A 1 186 ? -3.362  24.433  37.485  1 16.948  ? 178  ASP A N     1 
ATOM   1241 C  CA    . ASP A 1 186 ? -4.792  24.579  37.726  1 16.679  ? 178  ASP A CA    1 
ATOM   1242 C  C     . ASP A 1 186 ? -5.352  23.264  38.272  1 15.613  ? 178  ASP A C     1 
ATOM   1243 O  O     . ASP A 1 186 ? -5.107  22.239  37.654  1 14.577  ? 178  ASP A O     1 
ATOM   1244 C  CB    . ASP A 1 186 ? -5.553  25.059  36.5    1 16.478  ? 178  ASP A CB    1 
ATOM   1245 C  CG    . ASP A 1 186 ? -7.023  25.351  36.776  1 18.765  ? 178  ASP A CG    1 
ATOM   1246 O  OD1   . ASP A 1 186 ? -7.848  24.392  36.748  1 16.787  ? 178  ASP A OD1   1 
ATOM   1247 O  OD2   . ASP A 1 186 ? -7.321  26.528  37.09   1 21.722  ? 178  ASP A OD2   1 
ATOM   1248 N  N     . PRO A 1 187 ? -6.114  23.245  39.405  1 16.954  ? 179  PRO A N     1 
ATOM   1249 C  CA    . PRO A 1 187 ? -6.602  21.99   39.988  1 16.645  ? 179  PRO A CA    1 
ATOM   1250 C  C     . PRO A 1 187 ? -7.704  21.251  39.222  1 15.983  ? 179  PRO A C     1 
ATOM   1251 O  O     . PRO A 1 187 ? -8.034  20.124  39.601  1 14.526  ? 179  PRO A O     1 
ATOM   1252 C  CB    . PRO A 1 187 ? -6.938  22.371  41.425  1 16.5    ? 179  PRO A CB    1 
ATOM   1253 C  CG    . PRO A 1 187 ? -7.38   23.817  41.275  1 17.577  ? 179  PRO A CG    1 
ATOM   1254 C  CD    . PRO A 1 187 ? -6.482  24.409  40.244  1 16.567  ? 179  PRO A CD    1 
ATOM   1255 N  N     . HIS A 1 188 ? -8.246  21.874  38.159  1 16.34   ? 180  HIS A N     1 
ATOM   1256 C  CA    . HIS A 1 188 ? -9.413  21.386  37.421  1 17.216  ? 180  HIS A CA    1 
ATOM   1257 C  C     . HIS A 1 188 ? -9.042  21.011  35.985  1 17.102  ? 180  HIS A C     1 
ATOM   1258 O  O     . HIS A 1 188 ? -9.394  19.915  35.537  1 17.566  ? 180  HIS A O     1 
ATOM   1259 C  CB    . HIS A 1 188 ? -10.583 22.379  37.454  1 17.144  ? 180  HIS A CB    1 
ATOM   1260 C  CG    . HIS A 1 188 ? -10.726 23.136  38.733  1 16.591  ? 180  HIS A CG    1 
ATOM   1261 N  ND1   . HIS A 1 188 ? -11.289 22.547  39.838  1 16.237  ? 180  HIS A ND1   1 
ATOM   1262 C  CD2   . HIS A 1 188 ? -10.376 24.377  39.099  1 16.945  ? 180  HIS A CD2   1 
ATOM   1263 C  CE1   . HIS A 1 188 ? -11.295 23.409  40.838  1 16.579  ? 180  HIS A CE1   1 
ATOM   1264 N  NE2   . HIS A 1 188 ? -10.759 24.541  40.408  1 17.364  ? 180  HIS A NE2   1 
ATOM   1265 N  N     . THR A 1 189 ? -8.359  21.928  35.279  1 16.698  ? 181  THR A N     1 
ATOM   1266 C  CA    . THR A 1 189 ? -7.901  21.715  33.905  1 15.816  ? 181  THR A CA    1 
ATOM   1267 C  C     . THR A 1 189 ? -6.528  21.034  33.87   1 15.988  ? 181  THR A C     1 
ATOM   1268 O  O     . THR A 1 189 ? -6.158  20.543  32.805  1 15.262  ? 181  THR A O     1 
ATOM   1269 C  CB    . THR A 1 189 ? -7.889  22.992  33.06   1 16.371  ? 181  THR A CB    1 
ATOM   1270 O  OG1   . THR A 1 189 ? -6.871  23.839  33.599  1 16.425  ? 181  THR A OG1   1 
ATOM   1271 C  CG2   . THR A 1 189 ? -9.255  23.641  32.908  1 17.072  ? 181  THR A CG2   1 
ATOM   1272 N  N     . LEU A 1 190 ? -5.753  21.102  34.974  1 16.748  ? 182  LEU A N     1 
ATOM   1273 C  CA    . LEU A 1 190 ? -4.352  20.657  35.074  1 18.256  ? 182  LEU A CA    1 
ATOM   1274 C  C     . LEU A 1 190 ? -3.387  21.434  34.162  1 19.233  ? 182  LEU A C     1 
ATOM   1275 O  O     . LEU A 1 190 ? -2.248  20.99   33.95   1 20.741  ? 182  LEU A O     1 
ATOM   1276 C  CB    . LEU A 1 190 ? -4.166  19.13   35.036  1 18.738  ? 182  LEU A CB    1 
ATOM   1277 C  CG    . LEU A 1 190 ? -4.791  18.301  36.168  1 17.548  ? 182  LEU A CG    1 
ATOM   1278 C  CD1   . LEU A 1 190 ? -4.619  16.832  35.77   1 16.784  ? 182  LEU A CD1   1 
ATOM   1279 C  CD2   . LEU A 1 190 ? -4.172  18.583  37.55   1 16.324  ? 182  LEU A CD2   1 
ATOM   1280 N  N     . LYS A 1 191 ? -3.83   22.597  33.631  1 18.389  ? 183  LYS A N     1 
ATOM   1281 C  CA    . LYS A 1 191 ? -3.004  23.554  32.896  1 19.083  ? 183  LYS A CA    1 
ATOM   1282 C  C     . LYS A 1 191 ? -1.897  24.076  33.825  1 19.053  ? 183  LYS A C     1 
ATOM   1283 O  O     . LYS A 1 191 ? -2.186  24.438  34.966  1 18.507  ? 183  LYS A O     1 
ATOM   1284 C  CB    . LYS A 1 191 ? -3.86   24.672  32.285  1 21.966  ? 183  LYS A CB    1 
ATOM   1285 C  CG    . LYS A 1 191 ? -3.113  25.683  31.422  1 28.311  ? 183  LYS A CG    1 
ATOM   1286 C  CD    . LYS A 1 191 ? -3.968  26.691  30.657  1 35.676  ? 183  LYS A CD    1 
ATOM   1287 C  CE    . LYS A 1 191 ? -3.19   27.647  29.783  1 41.217  ? 183  LYS A CE    1 
ATOM   1288 N  NZ    . LYS A 1 191 ? -2.334  27.01   28.772  1 46.443  ? 183  LYS A NZ    1 
ATOM   1289 N  N     . THR A 1 192 ? -0.65   24.079  33.314  1 17.836  ? 184  THR A N     1 
ATOM   1290 C  CA    . THR A 1 192 ? 0.522   24.638  33.983  1 17.446  ? 184  THR A CA    1 
ATOM   1291 C  C     . THR A 1 192 ? 0.422   26.169  33.966  1 16.696  ? 184  THR A C     1 
ATOM   1292 O  O     . THR A 1 192 ? 0.192   26.78   32.919  1 17.306  ? 184  THR A O     1 
ATOM   1293 C  CB    . THR A 1 192 ? 1.809   24.112  33.342  1 18.111  ? 184  THR A CB    1 
ATOM   1294 O  OG1   . THR A 1 192 ? 1.754   22.692  33.386  1 18.712  ? 184  THR A OG1   1 
ATOM   1295 C  CG2   . THR A 1 192 ? 3.078   24.541  34.071  1 18.45   ? 184  THR A CG2   1 
ATOM   1296 N  N     . LEU A 1 193 ? 0.632   26.749  35.147  1 15.972  ? 185  LEU A N     1 
ATOM   1297 C  CA    . LEU A 1 193 ? 0.41    28.164  35.437  1 17.238  ? 185  LEU A CA    1 
ATOM   1298 C  C     . LEU A 1 193 ? 1.722   28.927  35.656  1 16.58   ? 185  LEU A C     1 
ATOM   1299 O  O     . LEU A 1 193 ? 1.776   30.138  35.387  1 16.532  ? 185  LEU A O     1 
ATOM   1300 C  CB    . LEU A 1 193 ? -0.574  28.346  36.602  1 17.444  ? 185  LEU A CB    1 
ATOM   1301 C  CG    . LEU A 1 193 ? -1.974  27.726  36.464  1 18.61   ? 185  LEU A CG    1 
ATOM   1302 C  CD1   . LEU A 1 193 ? -2.781  27.94   37.737  1 17.466  ? 185  LEU A CD1   1 
ATOM   1303 C  CD2   . LEU A 1 193 ? -2.753  28.229  35.24   1 18.85   ? 185  LEU A CD2   1 
ATOM   1304 N  N     . GLY A 1 194 ? 2.754   28.22   36.154  1 15.772  ? 186  GLY A N     1 
ATOM   1305 C  CA    . GLY A 1 194 ? 4.06    28.805  36.403  1 16.965  ? 186  GLY A CA    1 
ATOM   1306 C  C     . GLY A 1 194 ? 4.996   27.911  37.198  1 17.98   ? 186  GLY A C     1 
ATOM   1307 O  O     . GLY A 1 194 ? 4.685   26.745  37.461  1 19.065  ? 186  GLY A O     1 
ATOM   1308 N  N     . TYR A 1 195 ? 6.135   28.515  37.563  1 17.616  ? 187  TYR A N     1 
ATOM   1309 C  CA    . TYR A 1 195 ? 7.221   27.898  38.309  1 17.087  ? 187  TYR A CA    1 
ATOM   1310 C  C     . TYR A 1 195 ? 7.46    28.716  39.568  1 16.573  ? 187  TYR A C     1 
ATOM   1311 O  O     . TYR A 1 195 ? 7.464   29.945  39.519  1 15.32   ? 187  TYR A O     1 
ATOM   1312 C  CB    . TYR A 1 195 ? 8.481   27.788  37.438  1 16.921  ? 187  TYR A CB    1 
ATOM   1313 C  CG    . TYR A 1 195 ? 9.724   27.225  38.111  1 17.161  ? 187  TYR A CG    1 
ATOM   1314 C  CD1   . TYR A 1 195 ? 9.908   25.833  38.235  1 17.428  ? 187  TYR A CD1   1 
ATOM   1315 C  CD2   . TYR A 1 195 ? 10.722  28.081  38.616  1 16.599  ? 187  TYR A CD2   1 
ATOM   1316 C  CE1   . TYR A 1 195 ? 11.048  25.313  38.858  1 16.658  ? 187  TYR A CE1   1 
ATOM   1317 C  CE2   . TYR A 1 195 ? 11.865  27.562  39.233  1 16.582  ? 187  TYR A CE2   1 
ATOM   1318 C  CZ    . TYR A 1 195 ? 12.028  26.174  39.351  1 17.613  ? 187  TYR A CZ    1 
ATOM   1319 O  OH    . TYR A 1 195 ? 13.124  25.624  39.975  1 17.45   ? 187  TYR A OH    1 
ATOM   1320 N  N     . ASN A 1 196 ? 7.733   27.982  40.664  1 17.779  ? 188  ASN A N     1 
ATOM   1321 C  CA    . ASN A 1 196 ? 8.147   28.489  41.974  1 17.624  ? 188  ASN A CA    1 
ATOM   1322 C  C     . ASN A 1 196 ? 7.06    29.418  42.541  1 17.805  ? 188  ASN A C     1 
ATOM   1323 O  O     . ASN A 1 196 ? 7.405   30.57   42.86   1 16.937  ? 188  ASN A O     1 
ATOM   1324 C  CB    . ASN A 1 196 ? 9.565   29.082  41.915  1 15.41   ? 188  ASN A CB    1 
ATOM   1325 C  CG    . ASN A 1 196 ? 10.215  29.328  43.261  1 18.048  ? 188  ASN A CG    1 
ATOM   1326 O  OD1   . ASN A 1 196 ? 9.695   28.937  44.321  1 19.382  ? 188  ASN A OD1   1 
ATOM   1327 N  ND2   . ASN A 1 196 ? 11.386  29.955  43.236  1 16.396  ? 188  ASN A ND2   1 
ATOM   1328 N  N     . PRO A 1 197 ? 5.758   28.986  42.699  1 17.433  ? 189  PRO A N     1 
ATOM   1329 C  CA    . PRO A 1 197 ? 4.679   29.87   43.151  1 17.021  ? 189  PRO A CA    1 
ATOM   1330 C  C     . PRO A 1 197 ? 4.904   30.58   44.487  1 17.021  ? 189  PRO A C     1 
ATOM   1331 O  O     . PRO A 1 197 ? 4.508   31.734  44.603  1 17.021  ? 189  PRO A O     1 
ATOM   1332 C  CB    . PRO A 1 197 ? 3.426   28.995  43.156  1 16.087  ? 189  PRO A CB    1 
ATOM   1333 C  CG    . PRO A 1 197 ? 3.984   27.6    43.351  1 16.938  ? 189  PRO A CG    1 
ATOM   1334 C  CD    . PRO A 1 197 ? 5.219   27.62   42.504  1 17.896  ? 189  PRO A CD    1 
ATOM   1335 N  N     . PHE A 1 198 ? 5.576   29.915  45.443  1 18.074  ? 190  PHE A N     1 
ATOM   1336 C  CA    . PHE A 1 198 ? 5.907   30.485  46.759  1 19.627  ? 190  PHE A CA    1 
ATOM   1337 C  C     . PHE A 1 198 ? 7.162   31.373  46.755  1 18.869  ? 190  PHE A C     1 
ATOM   1338 O  O     . PHE A 1 198 ? 7.456   31.998  47.784  1 19.161  ? 190  PHE A O     1 
ATOM   1339 C  CB    . PHE A 1 198 ? 5.837   29.496  47.939  1 18.434  ? 190  PHE A CB    1 
ATOM   1340 C  CG    . PHE A 1 198 ? 4.478   28.836  48.074  1 18.061  ? 190  PHE A CG    1 
ATOM   1341 C  CD1   . PHE A 1 198 ? 3.326   29.599  48.386  1 18.124  ? 190  PHE A CD1   1 
ATOM   1342 C  CD2   . PHE A 1 198 ? 4.347   27.447  47.859  1 18.879  ? 190  PHE A CD2   1 
ATOM   1343 C  CE1   . PHE A 1 198 ? 2.058   28.982  48.454  1 16.814  ? 190  PHE A CE1   1 
ATOM   1344 C  CE2   . PHE A 1 198 ? 3.085   26.834  47.948  1 18.351  ? 190  PHE A CE2   1 
ATOM   1345 C  CZ    . PHE A 1 198 ? 1.953   27.604  48.25   1 16.782  ? 190  PHE A CZ    1 
ATOM   1346 N  N     . ASN A 1 199 ? 7.875   31.424  45.612  1 17.848  ? 191  ASN A N     1 
ATOM   1347 C  CA    . ASN A 1 199 ? 9.055   32.247  45.374  1 18.257  ? 191  ASN A CA    1 
ATOM   1348 C  C     . ASN A 1 199 ? 10.171  31.931  46.385  1 18.324  ? 191  ASN A C     1 
ATOM   1349 O  O     . ASN A 1 199 ? 10.749  32.819  47.022  1 16.872  ? 191  ASN A O     1 
ATOM   1350 C  CB    . ASN A 1 199 ? 8.639   33.673  45.04   1 19.937  ? 191  ASN A CB    1 
ATOM   1351 C  CG    . ASN A 1 199 ? 9.825   34.558  44.768  1 22.925  ? 191  ASN A CG    1 
ATOM   1352 O  OD1   . ASN A 1 199 ? 10.012  35.542  45.482  1 26.512  ? 191  ASN A OD1   1 
ATOM   1353 N  ND2   . ASN A 1 199 ? 10.669  34.208  43.809  1 24.804  ? 191  ASN A ND2   1 
ATOM   1354 N  N     . LEU A 1 200 ? 10.444  30.624  46.531  1 18.164  ? 192  LEU A N     1 
ATOM   1355 C  CA    . LEU A 1 200 ? 11.483  30.098  47.416  1 17.038  ? 192  LEU A CA    1 
ATOM   1356 C  C     . LEU A 1 200 ? 12.869  30.514  46.91   1 16.079  ? 192  LEU A C     1 
ATOM   1357 O  O     . LEU A 1 200 ? 13.067  30.493  45.685  1 14.236  ? 192  LEU A O     1 
ATOM   1358 C  CB    . LEU A 1 200 ? 11.362  28.592  47.675  1 17.863  ? 192  LEU A CB    1 
ATOM   1359 C  CG    . LEU A 1 200 ? 10.042  28.089  48.281  1 18.445  ? 192  LEU A CG    1 
ATOM   1360 C  CD1   . LEU A 1 200 ? 10.173  26.594  48.425  1 19.505  ? 192  LEU A CD1   1 
ATOM   1361 C  CD2   . LEU A 1 200 ? 9.638   28.664  49.636  1 17.421  ? 192  LEU A CD2   1 
ATOM   1362 N  N     . PRO A 1 201 ? 13.816  30.975  47.794  1 15.994  ? 193  PRO A N     1 
ATOM   1363 C  CA    . PRO A 1 201 ? 15.135  31.453  47.352  1 16.547  ? 193  PRO A CA    1 
ATOM   1364 C  C     . PRO A 1 201 ? 16.137  30.377  46.918  1 16.964  ? 193  PRO A C     1 
ATOM   1365 O  O     . PRO A 1 201 ? 17.121  30.701  46.242  1 16.745  ? 193  PRO A O     1 
ATOM   1366 C  CB    . PRO A 1 201 ? 15.632  32.295  48.523  1 16.827  ? 193  PRO A CB    1 
ATOM   1367 C  CG    . PRO A 1 201 ? 15.06   31.518  49.702  1 15.888  ? 193  PRO A CG    1 
ATOM   1368 C  CD    . PRO A 1 201 ? 13.662  31.148  49.253  1 15.642  ? 193  PRO A CD    1 
ATOM   1369 N  N     . SER A 1 202 ? 15.899  29.12   47.339  1 16.571  ? 194  SER A N     1 
ATOM   1370 C  CA    . SER A 1 202 ? 16.69   27.954  46.948  1 17.367  ? 194  SER A CA    1 
ATOM   1371 C  C     . SER A 1 202 ? 16.425  27.597  45.481  1 17.704  ? 194  SER A C     1 
ATOM   1372 O  O     . SER A 1 202 ? 15.396  27.979  44.901  1 18.249  ? 194  SER A O     1 
ATOM   1373 C  CB    . SER A 1 202 ? 16.404  26.785  47.868  1 18.135  ? 194  SER A CB    1 
ATOM   1374 O  OG    . SER A 1 202 ? 15.002  26.553  47.927  1 18.196  ? 194  SER A OG    1 
ATOM   1375 N  N     . LYS A 1 203 ? 17.376  26.855  44.892  1 17.871  ? 195  LYS A N     1 
ATOM   1376 C  CA    . LYS A 1 203 ? 17.241  26.281  43.554  1 19.019  ? 195  LYS A CA    1 
ATOM   1377 C  C     . LYS A 1 203 ? 16.288  25.078  43.532  1 17.751  ? 195  LYS A C     1 
ATOM   1378 O  O     . LYS A 1 203 ? 15.844  24.671  42.453  1 17.915  ? 195  LYS A O     1 
ATOM   1379 C  CB    . LYS A 1 203 ? 18.6    25.945  42.933  1 20.329  ? 195  LYS A CB    1 
ATOM   1380 C  CG    . LYS A 1 203 ? 19.434  27.153  42.575  1 21.189  ? 195  LYS A CG    1 
ATOM   1381 C  CD    . LYS A 1 203 ? 20.705  26.679  41.901  1 24.999  ? 195  LYS A CD    1 
ATOM   1382 C  CE    . LYS A 1 203 ? 21.769  27.739  41.779  1 24.425  ? 195  LYS A CE    1 
ATOM   1383 N  NZ    . LYS A 1 203 ? 21.497  28.588  40.618  1 26.064  ? 195  LYS A NZ    1 
ATOM   1384 N  N     . THR A 1 204 ? 16.011  24.507  44.715  1 15.99   ? 196  THR A N     1 
ATOM   1385 C  CA    . THR A 1 204 ? 15.321  23.234  44.874  1 15.382  ? 196  THR A CA    1 
ATOM   1386 C  C     . THR A 1 204 ? 14.242  23.364  45.958  1 15.923  ? 196  THR A C     1 
ATOM   1387 O  O     . THR A 1 204 ? 14.307  24.24   46.832  1 17.493  ? 196  THR A O     1 
ATOM   1388 C  CB    . THR A 1 204 ? 16.313  22.115  45.221  1 14.034  ? 196  THR A CB    1 
ATOM   1389 O  OG1   . THR A 1 204 ? 16.907  22.466  46.474  1 13.75   ? 196  THR A OG1   1 
ATOM   1390 C  CG2   . THR A 1 204 ? 17.308  21.764  44.119  1 14.105  ? 196  THR A CG2   1 
ATOM   1391 N  N     . MET A 1 205 ? 13.278  22.437  45.898  1 16.096  ? 197  MET A N     1 
ATOM   1392 C  CA    . MET A 1 205 ? 12.336  22.12   46.967  1 15.693  ? 197  MET A CA    1 
ATOM   1393 C  C     . MET A 1 205 ? 12.1    20.612  46.949  1 15.49   ? 197  MET A C     1 
ATOM   1394 O  O     . MET A 1 205 ? 11.895  20.053  45.871  1 15.598  ? 197  MET A O     1 
ATOM   1395 C  CB    . MET A 1 205 ? 11.023  22.897  46.806  1 15.812  ? 197  MET A CB    1 
ATOM   1396 C  CG    . MET A 1 205 ? 10.106  22.787  48.042  1 14.924  ? 197  MET A CG    1 
ATOM   1397 S  SD    . MET A 1 205 ? 8.413   23.362  47.872  1 15.847  ? 197  MET A SD    1 
ATOM   1398 C  CE    . MET A 1 205 ? 7.765   22.101  46.766  1 13.948  ? 197  MET A CE    1 
ATOM   1399 N  N     . THR A 1 206 ? 12.114  20.001  48.152  1 15.188  ? 198  THR A N     1 
ATOM   1400 C  CA    . THR A 1 206 ? 11.671  18.63   48.415  1 15.649  ? 198  THR A CA    1 
ATOM   1401 C  C     . THR A 1 206 ? 10.32   18.35   47.74   1 15.414  ? 198  THR A C     1 
ATOM   1402 O  O     . THR A 1 206 ? 9.476   19.249  47.622  1 13.648  ? 198  THR A O     1 
ATOM   1403 C  CB    . THR A 1 206 ? 11.658  18.309  49.916  1 15.431  ? 198  THR A CB    1 
ATOM   1404 O  OG1   . THR A 1 206 ? 11.46   16.899  50.068  1 16.297  ? 198  THR A OG1   1 
ATOM   1405 C  CG2   . THR A 1 206 ? 10.592  19.023  50.739  1 14.579  ? 198  THR A CG2   1 
ATOM   1406 N  N     . ALA A 1 207 ? 10.144  17.093  47.319  1 15.561  ? 199  ALA A N     1 
ATOM   1407 C  CA    . ALA A 1 207 ? 8.83    16.574  46.957  1 14.96   ? 199  ALA A CA    1 
ATOM   1408 C  C     . ALA A 1 207 ? 8.097   15.979  48.167  1 16.089  ? 199  ALA A C     1 
ATOM   1409 O  O     . ALA A 1 207 ? 6.94    15.561  48.066  1 16.439  ? 199  ALA A O     1 
ATOM   1410 C  CB    . ALA A 1 207 ? 8.94    15.631  45.8    1 14.935  ? 199  ALA A CB    1 
ATOM   1411 N  N     . HIS A 1 208 ? 8.738   16.042  49.34   1 16.229  ? 200  HIS A N     1 
ATOM   1412 C  CA    . HIS A 1 208 ? 8.166   15.586  50.592  1 16.05   ? 200  HIS A CA    1 
ATOM   1413 C  C     . HIS A 1 208 ? 8.023   16.712  51.621  1 15.954  ? 200  HIS A C     1 
ATOM   1414 O  O     . HIS A 1 208 ? 8.499   16.515  52.745  1 15.5    ? 200  HIS A O     1 
ATOM   1415 C  CB    . HIS A 1 208 ? 8.939   14.356  51.068  1 16.141  ? 200  HIS A CB    1 
ATOM   1416 C  CG    . HIS A 1 208 ? 8.575   13.152  50.295  1 17.166  ? 200  HIS A CG    1 
ATOM   1417 N  ND1   . HIS A 1 208 ? 7.317   12.6    50.352  1 16.469  ? 200  HIS A ND1   1 
ATOM   1418 C  CD2   . HIS A 1 208 ? 9.293   12.415  49.443  1 16.856  ? 200  HIS A CD2   1 
ATOM   1419 C  CE1   . HIS A 1 208 ? 7.29    11.56   49.551  1 16.654  ? 200  HIS A CE1   1 
ATOM   1420 N  NE2   . HIS A 1 208 ? 8.47    11.435  48.985  1 18.461  ? 200  HIS A NE2   1 
ATOM   1421 N  N     . PRO A 1 209 ? 7.325   17.868  51.356  1 16.813  ? 201  PRO A N     1 
ATOM   1422 C  CA    . PRO A 1 209 ? 6.934   18.745  52.451  1 16.621  ? 201  PRO A CA    1 
ATOM   1423 C  C     . PRO A 1 209 ? 5.796   18.132  53.268  1 16.922  ? 201  PRO A C     1 
ATOM   1424 O  O     . PRO A 1 209 ? 5.106   17.234  52.794  1 16.773  ? 201  PRO A O     1 
ATOM   1425 C  CB    . PRO A 1 209 ? 6.648   20.078  51.764  1 16.337  ? 201  PRO A CB    1 
ATOM   1426 C  CG    . PRO A 1 209 ? 6.031   19.632  50.445  1 16.282  ? 201  PRO A CG    1 
ATOM   1427 C  CD    . PRO A 1 209 ? 6.778   18.383  50.074  1 16.57   ? 201  PRO A CD    1 
ATOM   1428 N  N     . LYS A 1 210 ? 5.656   18.601  54.508  1 17.626  ? 202  LYS A N     1 
ATOM   1429 C  CA    . LYS A 1 210 ? 4.656   18.091  55.436  1 17.612  ? 202  LYS A CA    1 
ATOM   1430 C  C     . LYS A 1 210 ? 3.772   19.245  55.869  1 17.185  ? 202  LYS A C     1 
ATOM   1431 O  O     . LYS A 1 210 ? 4.288   20.286  56.284  1 16.894  ? 202  LYS A O     1 
ATOM   1432 C  CB    . LYS A 1 210 ? 5.286   17.319  56.607  1 16.423  ? 202  LYS A CB    1 
ATOM   1433 C  CG    . LYS A 1 210 ? 6.333   16.25   56.275  1 17.824  ? 202  LYS A CG    1 
ATOM   1434 C  CD    . LYS A 1 210 ? 5.924   15.04   55.429  1 16.961  ? 202  LYS A CD    1 
ATOM   1435 C  CE    . LYS A 1 210 ? 7.139   14.208  55.095  1 15.808  ? 202  LYS A CE    1 
ATOM   1436 N  NZ    . LYS A 1 210 ? 6.774   13.037  54.296  1 14.32   ? 202  LYS A NZ    1 
ATOM   1437 N  N     . GLN A 1 211 ? 2.451   19.013  55.768  1 16.569  ? 203  GLN A N     1 
ATOM   1438 C  CA    . GLN A 1 211 ? 1.444   19.977  56.199  1 16.735  ? 203  GLN A CA    1 
ATOM   1439 C  C     . GLN A 1 211 ? 1.107   19.714  57.662  1 16.573  ? 203  GLN A C     1 
ATOM   1440 O  O     . GLN A 1 211 ? 0.394   18.765  57.967  1 16.193  ? 203  GLN A O     1 
ATOM   1441 C  CB    . GLN A 1 211 ? 0.257   20.038  55.239  1 17.335  ? 203  GLN A CB    1 
ATOM   1442 C  CG    . GLN A 1 211 ? 0.638   20.619  53.882  1 18.344  ? 203  GLN A CG    1 
ATOM   1443 C  CD    . GLN A 1 211 ? -0.537  20.748  52.946  1 20.431  ? 203  GLN A CD    1 
ATOM   1444 O  OE1   . GLN A 1 211 ? -0.951  21.865  52.615  1 22.157  ? 203  GLN A OE1   1 
ATOM   1445 N  NE2   . GLN A 1 211 ? -1.087  19.618  52.518  1 17.939  ? 203  GLN A NE2   1 
ATOM   1446 N  N     . CYS A 1 212 ? 1.668   20.563  58.541  1 19.48   ? 204  CYS A N     1 
ATOM   1447 C  CA    . CYS A 1 212 ? 1.501   20.594  59.997  1 18.232  ? 204  CYS A CA    1 
ATOM   1448 C  C     . CYS A 1 212 ? 0.021   20.732  60.362  1 17.753  ? 204  CYS A C     1 
ATOM   1449 O  O     . CYS A 1 212 ? -0.613  21.689  59.953  1 17.305  ? 204  CYS A O     1 
ATOM   1450 C  CB    . CYS A 1 212 ? 2.317   21.758  60.553  1 18.428  ? 204  CYS A CB    1 
ATOM   1451 S  SG    . CYS A 1 212 ? 2.286   21.915  62.361  1 18.715  ? 204  CYS A SG    1 
ATOM   1452 N  N     . SER A 1 213 ? -0.496  19.786  61.152  1 18.155  ? 205  SER A N     1 
ATOM   1453 C  CA    . SER A 1 213 ? -1.882  19.779  61.628  1 20.579  ? 205  SER A CA    1 
ATOM   1454 C  C     . SER A 1 213 ? -2.14   20.83   62.71   1 21.911  ? 205  SER A C     1 
ATOM   1455 O  O     . SER A 1 213 ? -3.312  21.116  62.968  1 26.102  ? 205  SER A O     1 
ATOM   1456 C  CB    . SER A 1 213 ? -2.349  18.391  62.066  1 19.115  ? 205  SER A CB    1 
ATOM   1457 O  OG    . SER A 1 213 ? -1.601  17.979  63.196  1 18.549  ? 205  SER A OG    1 
ATOM   1458 N  N     . VAL A 1 214 ? -1.063  21.368  63.324  1 20.196  ? 206  VAL A N     1 
ATOM   1459 C  CA    . VAL A 1 214 ? -1.107  22.38   64.374  1 19.288  ? 206  VAL A CA    1 
ATOM   1460 C  C     . VAL A 1 214 ? -1.185  23.766  63.729  1 19.101  ? 206  VAL A C     1 
ATOM   1461 O  O     . VAL A 1 214 ? -2.133  24.496  63.992  1 17.906  ? 206  VAL A O     1 
ATOM   1462 C  CB    . VAL A 1 214 ? -0.029  22.26   65.486  1 18.677  ? 206  VAL A CB    1 
ATOM   1463 C  CG1   . VAL A 1 214 ? -0.119  23.349  66.554  1 19.348  ? 206  VAL A CG1   1 
ATOM   1464 C  CG2   . VAL A 1 214 ? -0.118  20.926  66.218  1 18.071  ? 206  VAL A CG2   1 
ATOM   1465 N  N     . THR A 1 215 ? -0.185  24.112  62.903  1 18.985  ? 207  THR A N     1 
ATOM   1466 C  CA    . THR A 1 215 ? -0.004  25.461  62.37   1 18.029  ? 207  THR A CA    1 
ATOM   1467 C  C     . THR A 1 215 ? -0.659  25.64   60.994  1 17.914  ? 207  THR A C     1 
ATOM   1468 O  O     . THR A 1 215 ? -0.86   26.78   60.557  1 16.801  ? 207  THR A O     1 
ATOM   1469 C  CB    . THR A 1 215 ? 1.485   25.836  62.348  1 19.133  ? 207  THR A CB    1 
ATOM   1470 O  OG1   . THR A 1 215 ? 2.109   24.923  61.453  1 16.058  ? 207  THR A OG1   1 
ATOM   1471 C  CG2   . THR A 1 215 ? 2.145   25.9    63.724  1 18.088  ? 207  THR A CG2   1 
ATOM   1472 N  N     . GLY A 1 216 ? -0.925  24.527  60.285  1 17.149  ? 208  GLY A N     1 
ATOM   1473 C  CA    . GLY A 1 216 ? -1.267  24.547  58.867  1 18.053  ? 208  GLY A CA    1 
ATOM   1474 C  C     . GLY A 1 216 ? -0.09   24.894  57.94   1 18.821  ? 208  GLY A C     1 
ATOM   1475 O  O     . GLY A 1 216 ? -0.338  25.084  56.755  1 23.119  ? 208  GLY A O     1 
ATOM   1476 N  N     . ASN A 1 217 ? 1.156   24.998  58.463  1 18.732  ? 209  ASN A N     1 
ATOM   1477 C  CA    . ASN A 1 217 ? 2.345   25.343  57.697  1 17.011  ? 209  ASN A CA    1 
ATOM   1478 C  C     . ASN A 1 217 ? 2.751   24.178  56.803  1 16.594  ? 209  ASN A C     1 
ATOM   1479 O  O     . ASN A 1 217 ? 2.616   23.012  57.196  1 16.504  ? 209  ASN A O     1 
ATOM   1480 C  CB    . ASN A 1 217 ? 3.549   25.754  58.551  1 17.585  ? 209  ASN A CB    1 
ATOM   1481 C  CG    . ASN A 1 217 ? 3.414   27.04   59.341  1 18.882  ? 209  ASN A CG    1 
ATOM   1482 O  OD1   . ASN A 1 217 ? 2.464   27.814  59.176  1 18.969  ? 209  ASN A OD1   1 
ATOM   1483 N  ND2   . ASN A 1 217 ? 4.364   27.29   60.235  1 18.901  ? 209  ASN A ND2   1 
ATOM   1484 N  N     . LEU A 1 218 ? 3.204   24.541  55.593  1 16.692  ? 210  LEU A N     1 
ATOM   1485 C  CA    . LEU A 1 218 ? 3.971   23.697  54.681  1 19.066  ? 210  LEU A CA    1 
ATOM   1486 C  C     . LEU A 1 218 ? 5.435   23.73   55.129  1 18.632  ? 210  LEU A C     1 
ATOM   1487 O  O     . LEU A 1 218 ? 6.135   24.745  54.964  1 18.315  ? 210  LEU A O     1 
ATOM   1488 C  CB    . LEU A 1 218 ? 3.783   24.117  53.214  1 19.43   ? 210  LEU A CB    1 
ATOM   1489 C  CG    . LEU A 1 218 ? 4.352   23.219  52.11   1 19.419  ? 210  LEU A CG    1 
ATOM   1490 C  CD1   . LEU A 1 218 ? 3.47    21.991  51.873  1 19.839  ? 210  LEU A CD1   1 
ATOM   1491 C  CD2   . LEU A 1 218 ? 4.475   24.039  50.823  1 18.61   ? 210  LEU A CD2   1 
ATOM   1492 N  N     . VAL A 1 219 ? 5.854   22.606  55.729  1 16.724  ? 211  VAL A N     1 
ATOM   1493 C  CA    . VAL A 1 219 ? 7.167   22.475  56.345  1 15.811  ? 211  VAL A CA    1 
ATOM   1494 C  C     . VAL A 1 219 ? 7.992   21.59   55.423  1 16.549  ? 211  VAL A C     1 
ATOM   1495 O  O     . VAL A 1 219 ? 7.616   20.432  55.158  1 15.894  ? 211  VAL A O     1 
ATOM   1496 C  CB    . VAL A 1 219 ? 7.174   21.924  57.791  1 16.131  ? 211  VAL A CB    1 
ATOM   1497 C  CG1   . VAL A 1 219 ? 8.569   21.986  58.424  1 17.484  ? 211  VAL A CG1   1 
ATOM   1498 C  CG2   . VAL A 1 219 ? 6.111   22.545  58.694  1 13.642  ? 211  VAL A CG2   1 
ATOM   1499 N  N     . GLY A 1 220 ? 9.132   22.147  54.994  1 16.043  ? 212  GLY A N     1 
ATOM   1500 C  CA    . GLY A 1 220 ? 10.052  21.404  54.159  1 15.18   ? 212  GLY A CA    1 
ATOM   1501 C  C     . GLY A 1 220 ? 11.415  22.059  54.046  1 14.778  ? 212  GLY A C     1 
ATOM   1502 O  O     . GLY A 1 220 ? 11.836  22.881  54.874  1 14.757  ? 212  GLY A O     1 
ATOM   1503 N  N     . PHE A 1 221 ? 12.088  21.624  52.979  1 15.229  ? 213  PHE A N     1 
ATOM   1504 C  CA    . PHE A 1 221 ? 13.488  21.899  52.724  1 15.422  ? 213  PHE A CA    1 
ATOM   1505 C  C     . PHE A 1 221 ? 13.755  21.816  51.223  1 16.568  ? 213  PHE A C     1 
ATOM   1506 O  O     . PHE A 1 221 ? 12.921  21.323  50.459  1 15.444  ? 213  PHE A O     1 
ATOM   1507 C  CB    . PHE A 1 221 ? 14.336  20.961  53.6    1 16.194  ? 213  PHE A CB    1 
ATOM   1508 C  CG    . PHE A 1 221 ? 14.265  19.505  53.165  1 16.199  ? 213  PHE A CG    1 
ATOM   1509 C  CD1   . PHE A 1 221 ? 13.152  18.693  53.493  1 15.416  ? 213  PHE A CD1   1 
ATOM   1510 C  CD2   . PHE A 1 221 ? 15.309  18.958  52.399  1 16.033  ? 213  PHE A CD2   1 
ATOM   1511 C  CE1   . PHE A 1 221 ? 13.103  17.354  53.075  1 15.992  ? 213  PHE A CE1   1 
ATOM   1512 C  CE2   . PHE A 1 221 ? 15.247  17.626  51.963  1 15.184  ? 213  PHE A CE2   1 
ATOM   1513 C  CZ    . PHE A 1 221 ? 14.15   16.826  52.316  1 15.881  ? 213  PHE A CZ    1 
ATOM   1514 N  N     . GLY A 1 222 ? 14.954  22.277  50.837  1 16.146  ? 214  GLY A N     1 
ATOM   1515 C  CA    . GLY A 1 222 ? 15.59   21.966  49.571  1 15.382  ? 214  GLY A CA    1 
ATOM   1516 C  C     . GLY A 1 222 ? 17.066  21.707  49.831  1 16.961  ? 214  GLY A C     1 
ATOM   1517 O  O     . GLY A 1 222 ? 17.719  22.54   50.468  1 17.81   ? 214  GLY A O     1 
ATOM   1518 N  N     . TYR A 1 223 ? 17.555  20.539  49.387  1 15.775  ? 215  TYR A N     1 
ATOM   1519 C  CA    . TYR A 1 223 ? 18.986  20.236  49.391  1 16.354  ? 215  TYR A CA    1 
ATOM   1520 C  C     . TYR A 1 223 ? 19.545  20.52   47.991  1 17.189  ? 215  TYR A C     1 
ATOM   1521 O  O     . TYR A 1 223 ? 18.78   20.707  47.04   1 17.287  ? 215  TYR A O     1 
ATOM   1522 C  CB    . TYR A 1 223 ? 19.199  18.824  49.965  1 16.249  ? 215  TYR A CB    1 
ATOM   1523 C  CG    . TYR A 1 223 ? 18.935  17.684  48.982  1 15.515  ? 215  TYR A CG    1 
ATOM   1524 C  CD1   . TYR A 1 223 ? 17.637  17.183  48.805  1 16.028  ? 215  TYR A CD1   1 
ATOM   1525 C  CD2   . TYR A 1 223 ? 19.971  17.129  48.207  1 15.915  ? 215  TYR A CD2   1 
ATOM   1526 C  CE1   . TYR A 1 223 ? 17.388  16.143  47.912  1 17.943  ? 215  TYR A CE1   1 
ATOM   1527 C  CE2   . TYR A 1 223 ? 19.722  16.085  47.311  1 17.12   ? 215  TYR A CE2   1 
ATOM   1528 C  CZ    . TYR A 1 223 ? 18.428  15.593  47.167  1 17.891  ? 215  TYR A CZ    1 
ATOM   1529 O  OH    . TYR A 1 223 ? 18.151  14.564  46.306  1 18.517  ? 215  TYR A OH    1 
ATOM   1530 N  N     . GLU A 1 224 ? 20.889  20.502  47.865  1 16.805  ? 216  GLU A N     1 
ATOM   1531 C  CA    . GLU A 1 224 ? 21.627  21.049  46.728  1 16.309  ? 216  GLU A CA    1 
ATOM   1532 C  C     . GLU A 1 224 ? 21.111  22.458  46.393  1 16.363  ? 216  GLU A C     1 
ATOM   1533 O  O     . GLU A 1 224 ? 20.883  22.799  45.218  1 16.505  ? 216  GLU A O     1 
ATOM   1534 C  CB    . GLU A 1 224 ? 21.659  20.148  45.492  1 16.084  ? 216  GLU A CB    1 
ATOM   1535 C  CG    . GLU A 1 224 ? 22.184  18.74   45.738  1 15.393  ? 216  GLU A CG    1 
ATOM   1536 C  CD    . GLU A 1 224 ? 22.602  17.911  44.537  1 15.17   ? 216  GLU A CD    1 
ATOM   1537 O  OE1   . GLU A 1 224 ? 22.839  18.422  43.416  1 14.782  ? 216  GLU A OE1   1 
ATOM   1538 O  OE2   . GLU A 1 224 ? 22.72   16.7    44.764  1 15.244  ? 216  GLU A OE2   1 
ATOM   1539 N  N     . ALA A 1 225 ? 20.935  23.273  47.447  1 16.623  ? 217  ALA A N     1 
ATOM   1540 C  CA    . ALA A 1 225 ? 20.106  24.475  47.414  1 18.143  ? 217  ALA A CA    1 
ATOM   1541 C  C     . ALA A 1 225 ? 20.756  25.593  46.592  1 18.93   ? 217  ALA A C     1 
ATOM   1542 O  O     . ALA A 1 225 ? 20.038  26.504  46.15   1 18.2    ? 217  ALA A O     1 
ATOM   1543 C  CB    . ALA A 1 225 ? 19.757  24.896  48.829  1 17.89   ? 217  ALA A CB    1 
ATOM   1544 N  N     . LYS A 1 226 ? 22.087  25.456  46.346  1 19.061  ? 218  LYS A N     1 
ATOM   1545 C  CA    . LYS A 1 226 ? 22.957  26.397  45.643  1 20.273  ? 218  LYS A CA    1 
ATOM   1546 C  C     . LYS A 1 226 ? 23.502  25.839  44.323  1 19.494  ? 218  LYS A C     1 
ATOM   1547 O  O     . LYS A 1 226 ? 24.365  26.46   43.702  1 20.858  ? 218  LYS A O     1 
ATOM   1548 C  CB    . LYS A 1 226 ? 24.048  26.923  46.59   1 19.562  ? 218  LYS A CB    1 
ATOM   1549 C  CG    . LYS A 1 226 ? 23.528  27.922  47.638  1 22.367  ? 218  LYS A CG    1 
ATOM   1550 C  CD    . LYS A 1 226 ? 24.66   28.492  48.491  1 23.631  ? 218  LYS A CD    1 
ATOM   1551 C  CE    . LYS A 1 226 ? 24.168  29.036  49.802  1 26.156  ? 218  LYS A CE    1 
ATOM   1552 N  NZ    . LYS A 1 226 ? 25.339  29.248  50.655  1 28.675  ? 218  LYS A NZ    1 
ATOM   1553 N  N     . GLY A 1 227 ? 22.985  24.696  43.865  1 17.555  ? 219  GLY A N     1 
ATOM   1554 C  CA    . GLY A 1 227 ? 23.398  24.14   42.586  1 18.726  ? 219  GLY A CA    1 
ATOM   1555 C  C     . GLY A 1 227 ? 23.894  22.71   42.739  1 20.344  ? 219  GLY A C     1 
ATOM   1556 O  O     . GLY A 1 227 ? 23.902  22.157  43.85   1 19.723  ? 219  GLY A O     1 
ATOM   1557 N  N     . LEU A 1 228 ? 24.301  22.152  41.592  1 19.897  ? 220  LEU A N     1 
ATOM   1558 C  CA    . LEU A 1 228 ? 24.761  20.778  41.427  1 19.915  ? 220  LEU A CA    1 
ATOM   1559 C  C     . LEU A 1 228 ? 25.901  20.474  42.406  1 20.988  ? 220  LEU A C     1 
ATOM   1560 O  O     . LEU A 1 228 ? 26.873  21.232  42.48   1 20.164  ? 220  LEU A O     1 
ATOM   1561 C  CB    . LEU A 1 228 ? 25.192  20.724  39.964  1 20.647  ? 220  LEU A CB    1 
ATOM   1562 C  CG    . LEU A 1 228 ? 24.9    19.461  39.148  1 25.432  ? 220  LEU A CG    1 
ATOM   1563 C  CD1   . LEU A 1 228 ? 23.452  18.976  38.966  1 21.332  ? 220  LEU A CD1   1 
ATOM   1564 C  CD2   . LEU A 1 228 ? 25.479  19.812  37.774  1 25.759  ? 220  LEU A CD2   1 
ATOM   1565 N  N     . ALA A 1 229 ? 25.68   19.426  43.228  1 19.955  ? 221  ALA A N     1 
ATOM   1566 C  CA    . ALA A 1 229 ? 26.578  18.83   44.218  1 20.097  ? 221  ALA A CA    1 
ATOM   1567 C  C     . ALA A 1 229 ? 26.848  19.711  45.455  1 19.909  ? 221  ALA A C     1 
ATOM   1568 O  O     . ALA A 1 229 ? 27.676  19.348  46.292  1 19.39   ? 221  ALA A O     1 
ATOM   1569 C  CB    . ALA A 1 229 ? 27.848  18.246  43.57   1 19.104  ? 221  ALA A CB    1 
ATOM   1570 N  N     . THR A 1 230 ? 26.12   20.829  45.629  1 21.502  ? 222  THR A N     1 
ATOM   1571 C  CA    . THR A 1 230 ? 26.249  21.73   46.783  1 20.161  ? 222  THR A CA    1 
ATOM   1572 C  C     . THR A 1 230 ? 25.688  21.043  48.027  1 19.593  ? 222  THR A C     1 
ATOM   1573 O  O     . THR A 1 230 ? 24.722  20.273  47.93   1 18.921  ? 222  THR A O     1 
ATOM   1574 C  CB    . THR A 1 230 ? 25.702  23.151  46.587  1 19.195  ? 222  THR A CB    1 
ATOM   1575 O  OG1   . THR A 1 230 ? 24.287  23.114  46.381  1 18.117  ? 222  THR A OG1   1 
ATOM   1576 C  CG2   . THR A 1 230 ? 26.376  23.897  45.449  1 18.615  ? 222  THR A CG2   1 
ATOM   1577 N  N     . LYS A 1 231 ? 26.349  21.295  49.172  1 17.318  ? 223  LYS A N     1 
ATOM   1578 C  CA    . LYS A 1 231 ? 26.01   20.675  50.447  1 18.159  ? 223  LYS A CA    1 
ATOM   1579 C  C     . LYS A 1 231 ? 24.915  21.452  51.185  1 17.381  ? 223  LYS A C     1 
ATOM   1580 O  O     . LYS A 1 231 ? 24.376  20.969  52.186  1 17.948  ? 223  LYS A O     1 
ATOM   1581 C  CB    . LYS A 1 231 ? 27.264  20.453  51.297  1 21.56   ? 223  LYS A CB    1 
ATOM   1582 C  CG    . LYS A 1 231 ? 28.163  19.304  50.812  1 25.645  ? 223  LYS A CG    1 
ATOM   1583 C  CD    . LYS A 1 231 ? 29.281  18.949  51.786  1 29.931  ? 223  LYS A CD    1 
ATOM   1584 C  CE    . LYS A 1 231 ? 30.466  19.876  51.755  1 35.438  ? 223  LYS A CE    1 
ATOM   1585 N  NZ    . LYS A 1 231 ? 30.732  20.191  53.161  1 38.406  ? 223  LYS A NZ    1 
ATOM   1586 N  N     . ASP A 1 232 ? 24.571  22.639  50.67   1 16.548  ? 224  ASP A N     1 
ATOM   1587 C  CA    . ASP A 1 232 ? 23.61   23.57   51.243  1 17.07   ? 224  ASP A CA    1 
ATOM   1588 C  C     . ASP A 1 232 ? 22.212  22.958  51.266  1 16.798  ? 224  ASP A C     1 
ATOM   1589 O  O     . ASP A 1 232 ? 21.801  22.249  50.334  1 15.706  ? 224  ASP A O     1 
ATOM   1590 C  CB    . ASP A 1 232 ? 23.648  24.912  50.531  1 18.417  ? 224  ASP A CB    1 
ATOM   1591 C  CG    . ASP A 1 232 ? 25.047  25.49   50.421  1 18.798  ? 224  ASP A CG    1 
ATOM   1592 O  OD1   . ASP A 1 232 ? 25.739  25.089  49.462  1 18.719  ? 224  ASP A OD1   1 
ATOM   1593 O  OD2   . ASP A 1 232 ? 25.422  26.282  51.319  1 16.888  ? 224  ASP A OD2   1 
ATOM   1594 N  N     . VAL A 1 233 ? 21.549  23.195  52.405  1 17.522  ? 225  VAL A N     1 
ATOM   1595 C  CA    . VAL A 1 233 ? 20.16   22.836  52.675  1 17.335  ? 225  VAL A CA    1 
ATOM   1596 C  C     . VAL A 1 233 ? 19.467  24.112  53.168  1 17.932  ? 225  VAL A C     1 
ATOM   1597 O  O     . VAL A 1 233 ? 19.961  24.775  54.084  1 16.794  ? 225  VAL A O     1 
ATOM   1598 C  CB    . VAL A 1 233 ? 20.016  21.647  53.666  1 18.327  ? 225  VAL A CB    1 
ATOM   1599 C  CG1   . VAL A 1 233 ? 18.566  21.327  54.037  1 16.236  ? 225  VAL A CG1   1 
ATOM   1600 C  CG2   . VAL A 1 233 ? 20.707  20.357  53.185  1 18.038  ? 225  VAL A CG2   1 
ATOM   1601 N  N     . TYR A 1 234 ? 18.32   24.429  52.543  1 18.27   ? 226  TYR A N     1 
ATOM   1602 C  CA    . TYR A 1 234 ? 17.405  25.48   52.969  1 18.404  ? 226  TYR A CA    1 
ATOM   1603 C  C     . TYR A 1 234 ? 16.176  24.833  53.604  1 18.523  ? 226  TYR A C     1 
ATOM   1604 O  O     . TYR A 1 234 ? 15.49   24.08   52.929  1 21.475  ? 226  TYR A O     1 
ATOM   1605 C  CB    . TYR A 1 234 ? 17.054  26.347  51.751  1 18.452  ? 226  TYR A CB    1 
ATOM   1606 C  CG    . TYR A 1 234 ? 15.999  27.421  52.006  1 18.578  ? 226  TYR A CG    1 
ATOM   1607 C  CD1   . TYR A 1 234 ? 16.294  28.53   52.819  1 16.414  ? 226  TYR A CD1   1 
ATOM   1608 C  CD2   . TYR A 1 234 ? 14.716  27.342  51.432  1 16.778  ? 226  TYR A CD2   1 
ATOM   1609 C  CE1   . TYR A 1 234 ? 15.356  29.531  53.028  1 16.615  ? 226  TYR A CE1   1 
ATOM   1610 C  CE2   . TYR A 1 234 ? 13.775  28.352  51.636  1 15.927  ? 226  TYR A CE2   1 
ATOM   1611 C  CZ    . TYR A 1 234 ? 14.092  29.43   52.455  1 16.356  ? 226  TYR A CZ    1 
ATOM   1612 O  OH    . TYR A 1 234 ? 13.198  30.42   52.718  1 16.671  ? 226  TYR A OH    1 
ATOM   1613 N  N     . TYR A 1 235 ? 15.933  25.127  54.885  1 16.164  ? 227  TYR A N     1 
ATOM   1614 C  CA    . TYR A 1 235 ? 14.703  24.806  55.598  1 15.964  ? 227  TYR A CA    1 
ATOM   1615 C  C     . TYR A 1 235 ? 13.709  25.967  55.465  1 16.759  ? 227  TYR A C     1 
ATOM   1616 O  O     . TYR A 1 235 ? 14.136  27.121  55.487  1 17.816  ? 227  TYR A O     1 
ATOM   1617 C  CB    . TYR A 1 235 ? 15.084  24.411  57.032  1 14.522  ? 227  TYR A CB    1 
ATOM   1618 C  CG    . TYR A 1 235 ? 14.026  24.722  58.086  1 14.537  ? 227  TYR A CG    1 
ATOM   1619 C  CD1   . TYR A 1 235 ? 12.886  23.906  58.245  1 13.314  ? 227  TYR A CD1   1 
ATOM   1620 C  CD2   . TYR A 1 235 ? 14.154  25.874  58.895  1 13.999  ? 227  TYR A CD2   1 
ATOM   1621 C  CE1   . TYR A 1 235 ? 11.913  24.223  59.2    1 13.502  ? 227  TYR A CE1   1 
ATOM   1622 C  CE2   . TYR A 1 235 ? 13.198  26.181  59.863  1 13.421  ? 227  TYR A CE2   1 
ATOM   1623 C  CZ    . TYR A 1 235 ? 12.069  25.363  60.002  1 13.054  ? 227  TYR A CZ    1 
ATOM   1624 O  OH    . TYR A 1 235 ? 11.14   25.675  60.962  1 12.108  ? 227  TYR A OH    1 
ATOM   1625 N  N     . PHE A 1 236 ? 12.399  25.66   55.373  1 15.994  ? 228  PHE A N     1 
ATOM   1626 C  CA    . PHE A 1 236 ? 11.345  26.678  55.298  1 15.935  ? 228  PHE A CA    1 
ATOM   1627 C  C     . PHE A 1 236 ? 10.069  26.194  55.982  1 16.451  ? 228  PHE A C     1 
ATOM   1628 O  O     . PHE A 1 236 ? 9.82    24.986  56.078  1 17.768  ? 228  PHE A O     1 
ATOM   1629 C  CB    . PHE A 1 236 ? 11.067  27.14   53.862  1 15.963  ? 228  PHE A CB    1 
ATOM   1630 C  CG    . PHE A 1 236 ? 10.531  26.028  52.962  1 16.732  ? 228  PHE A CG    1 
ATOM   1631 C  CD1   . PHE A 1 236 ? 9.151   25.69   52.96   1 16.912  ? 228  PHE A CD1   1 
ATOM   1632 C  CD2   . PHE A 1 236 ? 11.413  25.283  52.157  1 15.322  ? 228  PHE A CD2   1 
ATOM   1633 C  CE1   . PHE A 1 236 ? 8.677   24.631  52.176  1 18.478  ? 228  PHE A CE1   1 
ATOM   1634 C  CE2   . PHE A 1 236 ? 10.929  24.256  51.341  1 16.568  ? 228  PHE A CE2   1 
ATOM   1635 C  CZ    . PHE A 1 236 ? 9.574   23.922  51.36   1 16.697  ? 228  PHE A CZ    1 
ATOM   1636 N  N     . GLU A 1 237 ? 9.232   27.162  56.374  1 17.463  ? 229  GLU A N     1 
ATOM   1637 C  CA    . GLU A 1 237 ? 7.842   26.934  56.747  1 16.854  ? 229  GLU A CA    1 
ATOM   1638 C  C     . GLU A 1 237 ? 6.996   28.009  56.069  1 18.352  ? 229  GLU A C     1 
ATOM   1639 O  O     . GLU A 1 237 ? 7.206   29.199  56.329  1 18.478  ? 229  GLU A O     1 
ATOM   1640 C  CB    . GLU A 1 237 ? 7.562   26.866  58.249  1 16.335  ? 229  GLU A CB    1 
ATOM   1641 C  CG    . GLU A 1 237 ? 8.308   25.767  59      1 16.171  ? 229  GLU A CG    1 
ATOM   1642 C  CD    . GLU A 1 237 ? 7.799   25.306  60.354  1 15.723  ? 229  GLU A CD    1 
ATOM   1643 O  OE1   . GLU A 1 237 ? 6.627   25.56   60.701  1 15.56   ? 229  GLU A OE1   1 
ATOM   1644 O  OE2   . GLU A 1 237 ? 8.606   24.677  61.07   1 16.107  ? 229  GLU A OE2   1 
ATOM   1645 N  N     . VAL A 1 238 ? 6.092   27.553  55.177  1 17.93   ? 230  VAL A N     1 
ATOM   1646 C  CA    . VAL A 1 238 ? 5.158   28.405  54.46   1 17.256  ? 230  VAL A CA    1 
ATOM   1647 C  C     . VAL A 1 238 ? 3.815   28.33   55.195  1 16.908  ? 230  VAL A C     1 
ATOM   1648 O  O     . VAL A 1 238 ? 3.227   27.261  55.265  1 16.874  ? 230  VAL A O     1 
ATOM   1649 C  CB    . VAL A 1 238 ? 5.021   28.06   52.961  1 19.016  ? 230  VAL A CB    1 
ATOM   1650 C  CG1   . VAL A 1 238 ? 3.998   28.95   52.262  1 17.625  ? 230  VAL A CG1   1 
ATOM   1651 C  CG2   . VAL A 1 238 ? 6.336   28.097  52.188  1 17.553  ? 230  VAL A CG2   1 
ATOM   1652 N  N     . ASP A 1 239 ? 3.298   29.487  55.652  1 16.931  ? 231  ASP A N     1 
ATOM   1653 C  CA    . ASP A 1 239 ? 2.072   29.601  56.447  1 16.726  ? 231  ASP A CA    1 
ATOM   1654 C  C     . ASP A 1 239 ? 0.817   29.301  55.602  1 14.956  ? 231  ASP A C     1 
ATOM   1655 O  O     . ASP A 1 239 ? 0.968   29.216  54.382  1 14.409  ? 231  ASP A O     1 
ATOM   1656 C  CB    . ASP A 1 239 ? 2.092   30.885  57.271  1 18.605  ? 231  ASP A CB    1 
ATOM   1657 C  CG    . ASP A 1 239 ? 1.569   32.18   56.658  1 20.732  ? 231  ASP A CG    1 
ATOM   1658 O  OD1   . ASP A 1 239 ? 1.337   32.256  55.426  1 22.094  ? 231  ASP A OD1   1 
ATOM   1659 O  OD2   . ASP A 1 239 ? 1.361   33.122  57.439  1 21.844  ? 231  ASP A OD2   1 
ATOM   1660 N  N     . PRO A 1 240 ? -0.425  29.149  56.167  1 14.53   ? 232  PRO A N     1 
ATOM   1661 C  CA    . PRO A 1 240 ? -1.653  29.006  55.369  1 15.657  ? 232  PRO A CA    1 
ATOM   1662 C  C     . PRO A 1 240 ? -2.012  30.113  54.37   1 16.426  ? 232  PRO A C     1 
ATOM   1663 O  O     . PRO A 1 240 ? -2.893  29.893  53.531  1 18.463  ? 232  PRO A O     1 
ATOM   1664 C  CB    . PRO A 1 240 ? -2.78   28.774  56.384  1 14.652  ? 232  PRO A CB    1 
ATOM   1665 C  CG    . PRO A 1 240 ? -2.027  28.181  57.575  1 15.428  ? 232  PRO A CG    1 
ATOM   1666 C  CD    . PRO A 1 240 ? -0.732  28.929  57.598  1 14.96   ? 232  PRO A CD    1 
ATOM   1667 N  N     . SER A 1 241 ? -1.365  31.286  54.484  1 16.718  ? 233  SER A N     1 
ATOM   1668 C  CA    . SER A 1 241 ? -1.588  32.438  53.621  1 17.48   ? 233  SER A CA    1 
ATOM   1669 C  C     . SER A 1 241 ? -0.518  32.548  52.525  1 18.879  ? 233  SER A C     1 
ATOM   1670 O  O     . SER A 1 241 ? -0.55   33.505  51.739  1 20.711  ? 233  SER A O     1 
ATOM   1671 C  CB    . SER A 1 241 ? -1.77   33.712  54.436  1 17.904  ? 233  SER A CB    1 
ATOM   1672 O  OG    . SER A 1 241 ? -0.56   34.162  55.044  1 20.08   ? 233  SER A OG    1 
ATOM   1673 N  N     . GLY A 1 242 ? 0.427   31.585  52.492  1 19.356  ? 234  GLY A N     1 
ATOM   1674 C  CA    . GLY A 1 242 ? 1.439   31.462  51.44   1 20.661  ? 234  GLY A CA    1 
ATOM   1675 C  C     . GLY A 1 242 ? 2.724   32.27   51.674  1 21.312  ? 234  GLY A C     1 
ATOM   1676 O  O     . GLY A 1 242 ? 3.505   32.46   50.732  1 22.169  ? 234  GLY A O     1 
ATOM   1677 N  N     . LYS A 1 243 ? 2.949   32.707  52.924  1 20.911  ? 235  LYS A N     1 
ATOM   1678 C  CA    . LYS A 1 243 ? 4.112   33.475  53.358  1 24.478  ? 235  LYS A CA    1 
ATOM   1679 C  C     . LYS A 1 243 ? 5.128   32.551  54.049  1 22.829  ? 235  LYS A C     1 
ATOM   1680 O  O     . LYS A 1 243 ? 4.734   31.713  54.871  1 20.018  ? 235  LYS A O     1 
ATOM   1681 C  CB    . LYS A 1 243 ? 3.537   34.573  54.27   1 27.05   ? 235  LYS A CB    1 
ATOM   1682 C  CG    . LYS A 1 243 ? 4.434   35.73   54.677  1 39.138  ? 235  LYS A CG    1 
ATOM   1683 C  CD    . LYS A 1 243 ? 4.79    36.731  53.572  1 47.737  ? 235  LYS A CD    1 
ATOM   1684 C  CE    . LYS A 1 243 ? 5.214   38.073  54.061  1 48.041  ? 235  LYS A CE    1 
ATOM   1685 N  NZ    . LYS A 1 243 ? 6.01    38.774  53.046  1 49.718  ? 235  LYS A NZ    1 
ATOM   1686 N  N     . VAL A 1 244 ? 6.43    32.73   53.726  1 21.901  ? 236  VAL A N     1 
ATOM   1687 C  CA    . VAL A 1 244 ? 7.538   32.07   54.418  1 21.221  ? 236  VAL A CA    1 
ATOM   1688 C  C     . VAL A 1 244 ? 7.688   32.767  55.777  1 21.679  ? 236  VAL A C     1 
ATOM   1689 O  O     . VAL A 1 244 ? 8.035   33.949  55.817  1 23.296  ? 236  VAL A O     1 
ATOM   1690 C  CB    . VAL A 1 244 ? 8.869   32.005  53.617  1 21.993  ? 236  VAL A CB    1 
ATOM   1691 C  CG1   . VAL A 1 244 ? 10.041  31.403  54.404  1 19.41   ? 236  VAL A CG1   1 
ATOM   1692 C  CG2   . VAL A 1 244 ? 8.727   31.273  52.286  1 22.704  ? 236  VAL A CG2   1 
ATOM   1693 N  N     . VAL A 1 245 ? 7.431   32.018  56.865  1 20.872  ? 237  VAL A N     1 
ATOM   1694 C  CA    . VAL A 1 245 ? 7.366   32.543  58.228  1 20.42   ? 237  VAL A CA    1 
ATOM   1695 C  C     . VAL A 1 245 ? 8.578   32.1    59.057  1 22.313  ? 237  VAL A C     1 
ATOM   1696 O  O     . VAL A 1 245 ? 8.906   32.737  60.064  1 20.906  ? 237  VAL A O     1 
ATOM   1697 C  CB    . VAL A 1 245 ? 6.035   32.376  59.004  1 20.513  ? 237  VAL A CB    1 
ATOM   1698 C  CG1   . VAL A 1 245 ? 4.91    33.192  58.359  1 21.657  ? 237  VAL A CG1   1 
ATOM   1699 C  CG2   . VAL A 1 245 ? 5.617   30.907  59.237  1 19.123  ? 237  VAL A CG2   1 
ATOM   1700 N  N     . ARG A 1 246 ? 9.175   30.96   58.677  1 21.224  ? 238  ARG A N     1 
ATOM   1701 C  CA    . ARG A 1 246 ? 10.359  30.391  59.301  1 20.033  ? 238  ARG A CA    1 
ATOM   1702 C  C     . ARG A 1 246 ? 11.253  29.852  58.197  1 20.857  ? 238  ARG A C     1 
ATOM   1703 O  O     . ARG A 1 246 ? 10.753  29.274  57.231  1 19.671  ? 238  ARG A O     1 
ATOM   1704 C  CB    . ARG A 1 246 ? 10.007  29.26   60.274  1 21.094  ? 238  ARG A CB    1 
ATOM   1705 C  CG    . ARG A 1 246 ? 9.27    29.645  61.549  1 20.782  ? 238  ARG A CG    1 
ATOM   1706 C  CD    . ARG A 1 246 ? 8.607   28.407  62.093  1 23.334  ? 238  ARG A CD    1 
ATOM   1707 N  NE    . ARG A 1 246 ? 8.005   28.57   63.422  1 24.366  ? 238  ARG A NE    1 
ATOM   1708 C  CZ    . ARG A 1 246 ? 7.319   27.672  64.154  1 27.76   ? 238  ARG A CZ    1 
ATOM   1709 N  NH1   . ARG A 1 246 ? 7.028   26.448  63.719  1 27.635  ? 238  ARG A NH1   1 
ATOM   1710 N  NH2   . ARG A 1 246 ? 6.909   28.015  65.356  1 27.048  ? 238  ARG A NH2   1 
ATOM   1711 N  N     . ASP A 1 247 ? 12.565  30.107  58.34   1 19.972  ? 239  ASP A N     1 
ATOM   1712 C  CA    . ASP A 1 247 ? 13.58   29.539  57.465  1 19.901  ? 239  ASP A CA    1 
ATOM   1713 C  C     . ASP A 1 247 ? 14.944  29.467  58.153  1 18.93   ? 239  ASP A C     1 
ATOM   1714 O  O     . ASP A 1 247 ? 15.155  30.09   59.194  1 18.3    ? 239  ASP A O     1 
ATOM   1715 C  CB    . ASP A 1 247 ? 13.555  30.206  56.088  1 22.065  ? 239  ASP A CB    1 
ATOM   1716 C  CG    . ASP A 1 247 ? 14.074  31.63   55.956  1 23.964  ? 239  ASP A CG    1 
ATOM   1717 O  OD1   . ASP A 1 247 ? 14.522  32.226  56.966  1 21.543  ? 239  ASP A OD1   1 
ATOM   1718 O  OD2   . ASP A 1 247 ? 13.992  32.137  54.804  1 25.178  ? 239  ASP A OD2   1 
ATOM   1719 N  N     . LEU A 1 248 ? 15.88   28.749  57.509  1 18.898  ? 240  LEU A N     1 
ATOM   1720 C  CA    . LEU A 1 248 ? 17.277  28.578  57.909  1 18.408  ? 240  LEU A CA    1 
ATOM   1721 C  C     . LEU A 1 248 ? 18.083  28.03   56.738  1 18.507  ? 240  LEU A C     1 
ATOM   1722 O  O     . LEU A 1 248 ? 17.637  27.108  56.055  1 19.433  ? 240  LEU A O     1 
ATOM   1723 C  CB    . LEU A 1 248 ? 17.403  27.658  59.13   1 18.182  ? 240  LEU A CB    1 
ATOM   1724 C  CG    . LEU A 1 248 ? 18.743  27.629  59.882  1 18.378  ? 240  LEU A CG    1 
ATOM   1725 C  CD1   . LEU A 1 248 ? 19.048  28.914  60.677  1 17.89   ? 240  LEU A CD1   1 
ATOM   1726 C  CD2   . LEU A 1 248 ? 18.736  26.425  60.816  1 16.931  ? 240  LEU A CD2   1 
ATOM   1727 N  N     . TRP A 1 249 ? 19.274  28.615  56.543  1 18.047  ? 241  TRP A N     1 
ATOM   1728 C  CA    . TRP A 1 249 ? 20.356  28.064  55.733  1 18.869  ? 241  TRP A CA    1 
ATOM   1729 C  C     . TRP A 1 249 ? 21.296  27.233  56.602  1 18.561  ? 241  TRP A C     1 
ATOM   1730 O  O     . TRP A 1 249 ? 21.727  27.687  57.67   1 18.384  ? 241  TRP A O     1 
ATOM   1731 C  CB    . TRP A 1 249 ? 21.059  29.178  54.945  1 19.254  ? 241  TRP A CB    1 
ATOM   1732 C  CG    . TRP A 1 249 ? 20.167  29.701  53.841  1 18.984  ? 241  TRP A CG    1 
ATOM   1733 C  CD1   . TRP A 1 249 ? 19.24   30.697  53.956  1 18.043  ? 241  TRP A CD1   1 
ATOM   1734 C  CD2   . TRP A 1 249 ? 20.081  29.232  52.473  1 19.163  ? 241  TRP A CD2   1 
ATOM   1735 N  NE1   . TRP A 1 249 ? 18.61   30.909  52.765  1 18.58   ? 241  TRP A NE1   1 
ATOM   1736 C  CE2   . TRP A 1 249 ? 19.097  30.035  51.828  1 18.712  ? 241  TRP A CE2   1 
ATOM   1737 C  CE3   . TRP A 1 249 ? 20.75   28.249  51.715  1 18.387  ? 241  TRP A CE3   1 
ATOM   1738 C  CZ2   . TRP A 1 249 ? 18.733  29.857  50.483  1 18.462  ? 241  TRP A CZ2   1 
ATOM   1739 C  CZ3   . TRP A 1 249 ? 20.411  28.095  50.379  1 19.514  ? 241  TRP A CZ3   1 
ATOM   1740 C  CH2   . TRP A 1 249 ? 19.412  28.886  49.768  1 17.696  ? 241  TRP A CH2   1 
ATOM   1741 N  N     . LEU A 1 250 ? 21.514  25.982  56.159  1 18.848  ? 242  LEU A N     1 
ATOM   1742 C  CA    . LEU A 1 250 ? 22.324  24.965  56.838  1 17.461  ? 242  LEU A CA    1 
ATOM   1743 C  C     . LEU A 1 250 ? 23.112  24.151  55.801  1 17.526  ? 242  LEU A C     1 
ATOM   1744 O  O     . LEU A 1 250 ? 23.075  24.475  54.61   1 17.734  ? 242  LEU A O     1 
ATOM   1745 C  CB    . LEU A 1 250 ? 21.516  24.103  57.823  1 16.902  ? 242  LEU A CB    1 
ATOM   1746 C  CG    . LEU A 1 250 ? 20.397  23.223  57.247  1 19.524  ? 242  LEU A CG    1 
ATOM   1747 C  CD1   . LEU A 1 250 ? 20.483  21.843  57.864  1 17.286  ? 242  LEU A CD1   1 
ATOM   1748 C  CD2   . LEU A 1 250 ? 19.032  23.859  57.531  1 18.835  ? 242  LEU A CD2   1 
ATOM   1749 N  N     . GLU A 1 251 ? 23.834  23.111  56.258  1 17.59   ? 243  GLU A N     1 
ATOM   1750 C  CA    . GLU A 1 251 ? 24.519  22.162  55.38   1 18.457  ? 243  GLU A CA    1 
ATOM   1751 C  C     . GLU A 1 251 ? 24.317  20.725  55.85   1 17.889  ? 243  GLU A C     1 
ATOM   1752 O  O     . GLU A 1 251 ? 24.123  20.483  57.04   1 17.806  ? 243  GLU A O     1 
ATOM   1753 C  CB    . GLU A 1 251 ? 26.033  22.347  55.304  1 18.522  ? 243  GLU A CB    1 
ATOM   1754 C  CG    . GLU A 1 251 ? 26.502  23.622  54.623  1 22.497  ? 243  GLU A CG    1 
ATOM   1755 C  CD    . GLU A 1 251 ? 28.002  23.868  54.77   1 26.716  ? 243  GLU A CD    1 
ATOM   1756 O  OE1   . GLU A 1 251 ? 28.763  23.154  55.48   1 31.128  ? 243  GLU A OE1   1 
ATOM   1757 O  OE2   . GLU A 1 251 ? 28.43   24.837  54.131  1 27.418  ? 243  GLU A OE2   1 
ATOM   1758 N  N     . ALA A 1 252 ? 24.36   19.804  54.875  1 17.474  ? 244  ALA A N     1 
ATOM   1759 C  CA    . ALA A 1 252 ? 24.465  18.375  55.112  1 16.918  ? 244  ALA A CA    1 
ATOM   1760 C  C     . ALA A 1 252 ? 25.936  18.011  55.347  1 18.396  ? 244  ALA A C     1 
ATOM   1761 O  O     . ALA A 1 252 ? 26.802  18.753  54.849  1 18.97   ? 244  ALA A O     1 
ATOM   1762 C  CB    . ALA A 1 252 ? 23.823  17.646  53.956  1 14.281  ? 244  ALA A CB    1 
ATOM   1763 N  N     . PRO A 1 253 ? 26.278  16.925  56.118  1 18.215  ? 245  PRO A N     1 
ATOM   1764 C  CA    . PRO A 1 253 ? 27.674  16.489  56.297  1 18.277  ? 245  PRO A CA    1 
ATOM   1765 C  C     . PRO A 1 253 ? 28.425  16.116  55.013  1 19.604  ? 245  PRO A C     1 
ATOM   1766 O  O     . PRO A 1 253 ? 29.635  16.325  54.925  1 21.055  ? 245  PRO A O     1 
ATOM   1767 C  CB    . PRO A 1 253 ? 27.605  15.399  57.38   1 18.432  ? 245  PRO A CB    1 
ATOM   1768 C  CG    . PRO A 1 253 ? 26.197  14.85   57.177  1 18.737  ? 245  PRO A CG    1 
ATOM   1769 C  CD    . PRO A 1 253 ? 25.371  16.084  56.927  1 17.939  ? 245  PRO A CD    1 
ATOM   1770 N  N     . TRP A 1 254 ? 27.699  15.543  54.045  1 19.36   ? 246  TRP A N     1 
ATOM   1771 C  CA    . TRP A 1 254 ? 28.109  15.398  52.651  1 18.349  ? 246  TRP A CA    1 
ATOM   1772 C  C     . TRP A 1 254 ? 26.911  15.722  51.738  1 19.448  ? 246  TRP A C     1 
ATOM   1773 O  O     . TRP A 1 254 ? 25.778  15.826  52.215  1 18.737  ? 246  TRP A O     1 
ATOM   1774 C  CB    . TRP A 1 254 ? 28.707  13.998  52.421  1 17.75   ? 246  TRP A CB    1 
ATOM   1775 C  CG    . TRP A 1 254 ? 27.691  12.895  52.254  1 18.081  ? 246  TRP A CG    1 
ATOM   1776 C  CD1   . TRP A 1 254 ? 27.212  12.421  51.066  1 18.458  ? 246  TRP A CD1   1 
ATOM   1777 C  CD2   . TRP A 1 254 ? 27.024  12.14   53.288  1 16.666  ? 246  TRP A CD2   1 
ATOM   1778 N  NE1   . TRP A 1 254 ? 26.294  11.429  51.276  1 17.341  ? 246  TRP A NE1   1 
ATOM   1779 C  CE2   . TRP A 1 254 ? 26.154  11.227  52.621  1 17.723  ? 246  TRP A CE2   1 
ATOM   1780 C  CE3   . TRP A 1 254 ? 27.085  12.124  54.696  1 15.623  ? 246  TRP A CE3   1 
ATOM   1781 C  CZ2   . TRP A 1 254 ? 25.334  10.318  53.312  1 16.176  ? 246  TRP A CZ2   1 
ATOM   1782 C  CZ3   . TRP A 1 254 ? 26.282  11.225  55.381  1 16.563  ? 246  TRP A CZ3   1 
ATOM   1783 C  CH2   . TRP A 1 254 ? 25.409  10.342  54.698  1 16.369  ? 246  TRP A CH2   1 
ATOM   1784 N  N     . CYS A 1 255 ? 27.151  15.864  50.423  1 17.737  ? 247  CYS A N     1 
ATOM   1785 C  CA    . CYS A 1 255 ? 26.067  16.028  49.468  1 17.82   ? 247  CYS A CA    1 
ATOM   1786 C  C     . CYS A 1 255 ? 25.357  14.679  49.301  1 15.616  ? 247  CYS A C     1 
ATOM   1787 O  O     . CYS A 1 255 ? 25.765  13.854  48.485  1 14.441  ? 247  CYS A O     1 
ATOM   1788 C  CB    . CYS A 1 255 ? 26.51   16.713  48.185  1 18.354  ? 247  CYS A CB    1 
ATOM   1789 S  SG    . CYS A 1 255 ? 25.089  16.981  47.089  1 20.096  ? 247  CYS A SG    1 
ATOM   1790 N  N     . ALA A 1 256 ? 24.304  14.512  50.109  1 13.683  ? 248  ALA A N     1 
ATOM   1791 C  CA    . ALA A 1 256 ? 23.52   13.301  50.291  1 13.899  ? 248  ALA A CA    1 
ATOM   1792 C  C     . ALA A 1 256 ? 22.162  13.425  49.61   1 14.633  ? 248  ALA A C     1 
ATOM   1793 O  O     . ALA A 1 256 ? 21.698  14.538  49.361  1 15.319  ? 248  ALA A O     1 
ATOM   1794 C  CB    . ALA A 1 256 ? 23.327  13.091  51.763  1 13.582  ? 248  ALA A CB    1 
ATOM   1795 N  N     . PHE A 1 257 ? 21.549  12.264  49.335  1 14.423  ? 249  PHE A N     1 
ATOM   1796 C  CA    . PHE A 1 257 ? 20.223  12.135  48.749  1 15.67   ? 249  PHE A CA    1 
ATOM   1797 C  C     . PHE A 1 257 ? 19.195  12.215  49.875  1 15.091  ? 249  PHE A C     1 
ATOM   1798 O  O     . PHE A 1 257 ? 18.923  11.209  50.529  1 14.077  ? 249  PHE A O     1 
ATOM   1799 C  CB    . PHE A 1 257 ? 20.26   10.836  47.92   1 15.781  ? 249  PHE A CB    1 
ATOM   1800 C  CG    . PHE A 1 257 ? 19.212  10.577  46.844  1 15.798  ? 249  PHE A CG    1 
ATOM   1801 C  CD1   . PHE A 1 257 ? 17.909  11.121  46.901  1 15.56   ? 249  PHE A CD1   1 
ATOM   1802 C  CD2   . PHE A 1 257 ? 19.531  9.714   45.772  1 16.391  ? 249  PHE A CD2   1 
ATOM   1803 C  CE1   . PHE A 1 257 ? 16.971  10.848  45.895  1 16.058  ? 249  PHE A CE1   1 
ATOM   1804 C  CE2   . PHE A 1 257 ? 18.585  9.429   44.763  1 15.545  ? 249  PHE A CE2   1 
ATOM   1805 C  CZ    . PHE A 1 257 ? 17.311  10.003  44.821  1 16.16   ? 249  PHE A CZ    1 
ATOM   1806 N  N     . ILE A 1 258 ? 18.655  13.429  50.087  1 14.902  ? 250  ILE A N     1 
ATOM   1807 C  CA    . ILE A 1 258 ? 17.712  13.719  51.166  1 15.104  ? 250  ILE A CA    1 
ATOM   1808 C  C     . ILE A 1 258 ? 16.314  13.775  50.54   1 16.246  ? 250  ILE A C     1 
ATOM   1809 O  O     . ILE A 1 258 ? 15.76   14.857  50.286  1 15.371  ? 250  ILE A O     1 
ATOM   1810 C  CB    . ILE A 1 258 ? 18.061  14.97   52.021  1 15.191  ? 250  ILE A CB    1 
ATOM   1811 C  CG1   . ILE A 1 258 ? 19.58   15.181  52.254  1 15.184  ? 250  ILE A CG1   1 
ATOM   1812 C  CG2   . ILE A 1 258 ? 17.252  14.954  53.331  1 13.406  ? 250  ILE A CG2   1 
ATOM   1813 C  CD1   . ILE A 1 258 ? 19.967  16.488  52.941  1 15.324  ? 250  ILE A CD1   1 
ATOM   1814 N  N     . HIS A 1 259 ? 15.768  12.577  50.281  1 15.981  ? 251  HIS A N     1 
ATOM   1815 C  CA    . HIS A 1 259 ? 14.498  12.411  49.588  1 14.821  ? 251  HIS A CA    1 
ATOM   1816 C  C     . HIS A 1 259 ? 13.299  12.814  50.458  1 14.586  ? 251  HIS A C     1 
ATOM   1817 O  O     . HIS A 1 259 ? 12.405  13.532  49.983  1 12.968  ? 251  HIS A O     1 
ATOM   1818 C  CB    . HIS A 1 259 ? 14.426  11.005  49.005  1 14.871  ? 251  HIS A CB    1 
ATOM   1819 C  CG    . HIS A 1 259 ? 13.126  10.751  48.328  1 16.367  ? 251  HIS A CG    1 
ATOM   1820 N  ND1   . HIS A 1 259 ? 12.783  11.428  47.18   1 15.652  ? 251  HIS A ND1   1 
ATOM   1821 C  CD2   . HIS A 1 259 ? 12.063  9.999   48.664  1 16.113  ? 251  HIS A CD2   1 
ATOM   1822 C  CE1   . HIS A 1 259 ? 11.564  11.082  46.825  1 14.88   ? 251  HIS A CE1   1 
ATOM   1823 N  NE2   . HIS A 1 259 ? 11.126  10.194  47.686  1 15.775  ? 251  HIS A NE2   1 
ATOM   1824 N  N     . ASP A 1 260 ? 13.285  12.309  51.701  1 13.959  ? 252  ASP A N     1 
ATOM   1825 C  CA    . ASP A 1 260 ? 12.167  12.378  52.628  1 14.594  ? 252  ASP A CA    1 
ATOM   1826 C  C     . ASP A 1 260 ? 12.646  12.889  53.994  1 15.448  ? 252  ASP A C     1 
ATOM   1827 O  O     . ASP A 1 260 ? 13.846  13.097  54.215  1 14.874  ? 252  ASP A O     1 
ATOM   1828 C  CB    . ASP A 1 260 ? 11.359  11.082  52.568  1 13.455  ? 252  ASP A CB    1 
ATOM   1829 C  CG    . ASP A 1 260 ? 9.916   11.117  53.047  1 13.743  ? 252  ASP A CG    1 
ATOM   1830 O  OD1   . ASP A 1 260 ? 9.394   12.196  53.442  1 13.523  ? 252  ASP A OD1   1 
ATOM   1831 O  OD2   . ASP A 1 260 ? 9.325   10.036  53.072  1 14.752  ? 252  ASP A OD2   1 
ATOM   1832 N  N     . CYS A 1 261 ? 11.665  13.11   54.887  1 15.619  ? 253  CYS A N     1 
ATOM   1833 C  CA    . CYS A 1 261 ? 11.797  13.795  56.163  1 16.122  ? 253  CYS A CA    1 
ATOM   1834 C  C     . CYS A 1 261 ? 10.649  13.395  57.097  1 16.811  ? 253  CYS A C     1 
ATOM   1835 O  O     . CYS A 1 261 ? 9.72    12.69   56.682  1 18.795  ? 253  CYS A O     1 
ATOM   1836 C  CB    . CYS A 1 261 ? 11.916  15.304  55.931  1 16.778  ? 253  CYS A CB    1 
ATOM   1837 S  SG    . CYS A 1 261 ? 10.385  16.086  55.358  1 15.879  ? 253  CYS A SG    1 
ATOM   1838 N  N     . ALA A 1 262 ? 10.729  13.835  58.361  1 16.136  ? 254  ALA A N     1 
ATOM   1839 C  CA    . ALA A 1 262 ? 9.666   13.644  59.341  1 16.56   ? 254  ALA A CA    1 
ATOM   1840 C  C     . ALA A 1 262 ? 9.433   14.934  60.128  1 16.521  ? 254  ALA A C     1 
ATOM   1841 O  O     . ALA A 1 262 ? 10.376  15.657  60.478  1 15.487  ? 254  ALA A O     1 
ATOM   1842 C  CB    . ALA A 1 262 ? 9.922   12.44   60.239  1 15.019  ? 254  ALA A CB    1 
ATOM   1843 N  N     . LEU A 1 263 ? 8.141   15.214  60.327  1 16.439  ? 255  LEU A N     1 
ATOM   1844 C  CA    . LEU A 1 263 ? 7.657   16.372  61.06   1 16.115  ? 255  LEU A CA    1 
ATOM   1845 C  C     . LEU A 1 263 ? 7.126   15.924  62.418  1 16.141  ? 255  LEU A C     1 
ATOM   1846 O  O     . LEU A 1 263 ? 6.312   15.001  62.487  1 16.706  ? 255  LEU A O     1 
ATOM   1847 C  CB    . LEU A 1 263 ? 6.605   17.149  60.254  1 16.196  ? 255  LEU A CB    1 
ATOM   1848 C  CG    . LEU A 1 263 ? 6.117   18.462  60.884  1 14.756  ? 255  LEU A CG    1 
ATOM   1849 C  CD1   . LEU A 1 263 ? 7.133   19.602  60.846  1 13.456  ? 255  LEU A CD1   1 
ATOM   1850 C  CD2   . LEU A 1 263 ? 4.818   18.851  60.217  1 14.764  ? 255  LEU A CD2   1 
ATOM   1851 N  N     . THR A 1 264 ? 7.613   16.607  63.469  1 16.095  ? 256  THR A N     1 
ATOM   1852 C  CA    . THR A 1 264 ? 7.224   16.435  64.863  1 16.542  ? 256  THR A CA    1 
ATOM   1853 C  C     . THR A 1 264 ? 6.808   17.818  65.4    1 17.439  ? 256  THR A C     1 
ATOM   1854 O  O     . THR A 1 264 ? 7.009   18.793  64.66   1 17.694  ? 256  THR A O     1 
ATOM   1855 C  CB    . THR A 1 264 ? 8.338   15.744  65.673  1 16.819  ? 256  THR A CB    1 
ATOM   1856 O  OG1   . THR A 1 264 ? 9.297   16.744  65.99   1 16.129  ? 256  THR A OG1   1 
ATOM   1857 C  CG2   . THR A 1 264 ? 8.985   14.533  65.016  1 15.619  ? 256  THR A CG2   1 
ATOM   1858 N  N     . PRO A 1 265 ? 6.246   18.011  66.644  1 17.491  ? 257  PRO A N     1 
ATOM   1859 C  CA    . PRO A 1 265 ? 5.963   19.36   67.159  1 18.449  ? 257  PRO A CA    1 
ATOM   1860 C  C     . PRO A 1 265 ? 7.118   20.367  67.103  1 18.775  ? 257  PRO A C     1 
ATOM   1861 O  O     . PRO A 1 265 ? 6.882   21.512  66.701  1 18.49   ? 257  PRO A O     1 
ATOM   1862 C  CB    . PRO A 1 265 ? 5.343   19.152  68.548  1 17.704  ? 257  PRO A CB    1 
ATOM   1863 C  CG    . PRO A 1 265 ? 4.732   17.775  68.402  1 18.617  ? 257  PRO A CG    1 
ATOM   1864 C  CD    . PRO A 1 265 ? 5.75    16.998  67.604  1 18.99   ? 257  PRO A CD    1 
ATOM   1865 N  N     . ASN A 1 266 ? 8.354   19.904  67.395  1 18.922  ? 258  ASN A N     1 
ATOM   1866 C  CA    . ASN A 1 266 ? 9.487   20.79   67.653  1 18.929  ? 258  ASN A CA    1 
ATOM   1867 C  C     . ASN A 1 266 ? 10.593  20.703  66.592  1 18.994  ? 258  ASN A C     1 
ATOM   1868 O  O     . ASN A 1 266 ? 11.511  21.528  66.632  1 19.573  ? 258  ASN A O     1 
ATOM   1869 C  CB    . ASN A 1 266 ? 9.962   20.649  69.096  1 17.906  ? 258  ASN A CB    1 
ATOM   1870 C  CG    . ASN A 1 266 ? 8.871   20.972  70.081  1 18.713  ? 258  ASN A CG    1 
ATOM   1871 O  OD1   . ASN A 1 266 ? 8.338   22.087  70.086  1 19.738  ? 258  ASN A OD1   1 
ATOM   1872 N  ND2   . ASN A 1 266 ? 8.491   19.987  70.875  1 17.351  ? 258  ASN A ND2   1 
ATOM   1873 N  N     . TYR A 1 267 ? 10.486  19.748  65.647  1 19.358  ? 259  TYR A N     1 
ATOM   1874 C  CA    . TYR A 1 267 ? 11.559  19.399  64.714  1 19.12   ? 259  TYR A CA    1 
ATOM   1875 C  C     . TYR A 1 267 ? 11.043  19.115  63.305  1 18.639  ? 259  TYR A C     1 
ATOM   1876 O  O     . TYR A 1 267 ? 9.953   18.552  63.133  1 18.488  ? 259  TYR A O     1 
ATOM   1877 C  CB    . TYR A 1 267 ? 12.333  18.167  65.192  1 19.55   ? 259  TYR A CB    1 
ATOM   1878 C  CG    . TYR A 1 267 ? 13.13   18.389  66.463  1 20.475  ? 259  TYR A CG    1 
ATOM   1879 C  CD1   . TYR A 1 267 ? 14.437  18.918  66.404  1 21.656  ? 259  TYR A CD1   1 
ATOM   1880 C  CD2   . TYR A 1 267 ? 12.588  18.053  67.71   1 21.94   ? 259  TYR A CD2   1 
ATOM   1881 C  CE1   . TYR A 1 267 ? 15.178  19.122  67.56   1 24.434  ? 259  TYR A CE1   1 
ATOM   1882 C  CE2   . TYR A 1 267 ? 13.326  18.248  68.876  1 24.301  ? 259  TYR A CE2   1 
ATOM   1883 C  CZ    . TYR A 1 267 ? 14.614  18.792  68.789  1 25.276  ? 259  TYR A CZ    1 
ATOM   1884 O  OH    . TYR A 1 267 ? 15.388  19.012  69.88   1 28.3    ? 259  TYR A OH    1 
ATOM   1885 N  N     . LEU A 1 268 ? 11.876  19.516  62.328  1 17.503  ? 260  LEU A N     1 
ATOM   1886 C  CA    . LEU A 1 268 ? 11.969  18.884  61.017  1 18.08   ? 260  LEU A CA    1 
ATOM   1887 C  C     . LEU A 1 268 ? 13.195  17.978  61.029  1 16.961  ? 260  LEU A C     1 
ATOM   1888 O  O     . LEU A 1 268 ? 14.309  18.441  61.321  1 18.903  ? 260  LEU A O     1 
ATOM   1889 C  CB    . LEU A 1 268 ? 11.938  19.857  59.829  1 17.068  ? 260  LEU A CB    1 
ATOM   1890 C  CG    . LEU A 1 268 ? 11.874  19.248  58.418  1 18.544  ? 260  LEU A CG    1 
ATOM   1891 C  CD1   . LEU A 1 268 ? 10.521  18.566  58.148  1 19.653  ? 260  LEU A CD1   1 
ATOM   1892 C  CD2   . LEU A 1 268 ? 12.191  20.257  57.311  1 15.517  ? 260  LEU A CD2   1 
ATOM   1893 N  N     . VAL A 1 269 ? 12.955  16.686  60.719  1 16.587  ? 261  VAL A N     1 
ATOM   1894 C  CA    . VAL A 1 269 ? 13.996  15.661  60.759  1 14.852  ? 261  VAL A CA    1 
ATOM   1895 C  C     . VAL A 1 269 ? 14.236  15.206  59.318  1 16.223  ? 261  VAL A C     1 
ATOM   1896 O  O     . VAL A 1 269 ? 13.385  14.518  58.757  1 17.073  ? 261  VAL A O     1 
ATOM   1897 C  CB    . VAL A 1 269 ? 13.785  14.467  61.726  1 13.348  ? 261  VAL A CB    1 
ATOM   1898 C  CG1   . VAL A 1 269 ? 15.055  13.621  61.867  1 12.379  ? 261  VAL A CG1   1 
ATOM   1899 C  CG2   . VAL A 1 269 ? 13.291  14.895  63.109  1 12.886  ? 261  VAL A CG2   1 
ATOM   1900 N  N     . LEU A 1 270 ? 15.428  15.53   58.78   1 16.438  ? 262  LEU A N     1 
ATOM   1901 C  CA    . LEU A 1 270 ? 15.874  15.141  57.442  1 15.262  ? 262  LEU A CA    1 
ATOM   1902 C  C     . LEU A 1 270 ? 16.499  13.751  57.484  1 15.53   ? 262  LEU A C     1 
ATOM   1903 O  O     . LEU A 1 270 ? 17.263  13.466  58.408  1 15.813  ? 262  LEU A O     1 
ATOM   1904 C  CB    . LEU A 1 270 ? 16.853  16.172  56.871  1 14.681  ? 262  LEU A CB    1 
ATOM   1905 C  CG    . LEU A 1 270 ? 16.427  17.644  56.825  1 15.43   ? 262  LEU A CG    1 
ATOM   1906 C  CD1   . LEU A 1 270 ? 17.462  18.408  56.031  1 15.077  ? 262  LEU A CD1   1 
ATOM   1907 C  CD2   . LEU A 1 270 ? 15.043  17.89   56.277  1 14.705  ? 262  LEU A CD2   1 
ATOM   1908 N  N     . MET A 1 271 ? 16.21   12.954  56.444  1 15.812  ? 263  MET A N     1 
ATOM   1909 C  CA    . MET A 1 271 ? 16.615  11.556  56.325  1 17.418  ? 263  MET A CA    1 
ATOM   1910 C  C     . MET A 1 271 ? 17.565  11.407  55.13   1 18.317  ? 263  MET A C     1 
ATOM   1911 O  O     . MET A 1 271 ? 17.149  11.52   53.978  1 19.224  ? 263  MET A O     1 
ATOM   1912 C  CB    . MET A 1 271 ? 15.357  10.673  56.246  1 17.349  ? 263  MET A CB    1 
ATOM   1913 C  CG    . MET A 1 271 ? 15.608  9.16    56.201  1 17.041  ? 263  MET A CG    1 
ATOM   1914 S  SD    . MET A 1 271 ? 14.115  8.157   56.306  1 17.982  ? 263  MET A SD    1 
ATOM   1915 C  CE    . MET A 1 271 ? 13.232  8.594   54.791  1 17.224  ? 263  MET A CE    1 
ATOM   1916 N  N     . LEU A 1 272 ? 18.847  11.146  55.432  1 18.096  ? 264  LEU A N     1 
ATOM   1917 C  CA    . LEU A 1 272 ? 19.927  11.055  54.449  1 17.409  ? 264  LEU A CA    1 
ATOM   1918 C  C     . LEU A 1 272 ? 20.129  9.603   54.008  1 16.51   ? 264  LEU A C     1 
ATOM   1919 O  O     . LEU A 1 272 ? 20.488  8.743   54.825  1 16.828  ? 264  LEU A O     1 
ATOM   1920 C  CB    . LEU A 1 272 ? 21.219  11.697  54.968  1 16.162  ? 264  LEU A CB    1 
ATOM   1921 C  CG    . LEU A 1 272 ? 21.311  13.226  55.008  1 15.888  ? 264  LEU A CG    1 
ATOM   1922 C  CD1   . LEU A 1 272 ? 20.321  13.984  55.892  1 15.515  ? 264  LEU A CD1   1 
ATOM   1923 C  CD2   . LEU A 1 272 ? 22.726  13.554  55.448  1 14.731  ? 264  LEU A CD2   1 
ATOM   1924 N  N     . TRP A 1 273 ? 19.869  9.354   52.717  1 15.904  ? 265  TRP A N     1 
ATOM   1925 C  CA    . TRP A 1 273 ? 20.23   8.102   52.063  1 17.61   ? 265  TRP A CA    1 
ATOM   1926 C  C     . TRP A 1 273 ? 21.747  8.022   51.835  1 17.223  ? 265  TRP A C     1 
ATOM   1927 O  O     . TRP A 1 273 ? 22.35   9.058   51.542  1 16.59   ? 265  TRP A O     1 
ATOM   1928 C  CB    . TRP A 1 273 ? 19.481  7.905   50.736  1 16.168  ? 265  TRP A CB    1 
ATOM   1929 C  CG    . TRP A 1 273 ? 17.977  7.789   50.795  1 17.481  ? 265  TRP A CG    1 
ATOM   1930 C  CD1   . TRP A 1 273 ? 17.162  7.653   51.887  1 16.162  ? 265  TRP A CD1   1 
ATOM   1931 C  CD2   . TRP A 1 273 ? 17.11   7.745   49.637  1 16.413  ? 265  TRP A CD2   1 
ATOM   1932 N  NE1   . TRP A 1 273 ? 15.854  7.582   51.496  1 14.972  ? 265  TRP A NE1   1 
ATOM   1933 C  CE2   . TRP A 1 273 ? 15.783  7.616   50.126  1 17.159  ? 265  TRP A CE2   1 
ATOM   1934 C  CE3   . TRP A 1 273 ? 17.314  7.793   48.237  1 17.675  ? 265  TRP A CE3   1 
ATOM   1935 C  CZ2   . TRP A 1 273 ? 14.673  7.532   49.26   1 15.576  ? 265  TRP A CZ2   1 
ATOM   1936 C  CZ3   . TRP A 1 273 ? 16.219  7.702   47.383  1 16.312  ? 265  TRP A CZ3   1 
ATOM   1937 C  CH2   . TRP A 1 273 ? 14.916  7.582   47.897  1 16.14   ? 265  TRP A CH2   1 
ATOM   1938 N  N     . PRO A 1 274 ? 22.401  6.818   51.894  1 17.31   ? 266  PRO A N     1 
ATOM   1939 C  CA    . PRO A 1 274 ? 23.842  6.68    51.649  1 18.668  ? 266  PRO A CA    1 
ATOM   1940 C  C     . PRO A 1 274 ? 24.227  6.692   50.165  1 19.911  ? 266  PRO A C     1 
ATOM   1941 O  O     . PRO A 1 274 ? 24.767  5.706   49.631  1 24.125  ? 266  PRO A O     1 
ATOM   1942 C  CB    . PRO A 1 274 ? 24.181  5.435   52.461  1 19.009  ? 266  PRO A CB    1 
ATOM   1943 C  CG    . PRO A 1 274 ? 22.974  4.556   52.142  1 18.887  ? 266  PRO A CG    1 
ATOM   1944 C  CD    . PRO A 1 274 ? 21.809  5.512   52.215  1 17.797  ? 266  PRO A CD    1 
ATOM   1945 N  N     . PHE A 1 275 ? 23.906  7.817   49.499  1 18.361  ? 267  PHE A N     1 
ATOM   1946 C  CA    . PHE A 1 275 ? 24.382  8.176   48.166  1 17.315  ? 267  PHE A CA    1 
ATOM   1947 C  C     . PHE A 1 275 ? 25.089  9.519   48.29   1 17.086  ? 267  PHE A C     1 
ATOM   1948 O  O     . PHE A 1 275 ? 24.673  10.36   49.1    1 15.984  ? 267  PHE A O     1 
ATOM   1949 C  CB    . PHE A 1 275 ? 23.306  8.289   47.074  1 17.707  ? 267  PHE A CB    1 
ATOM   1950 C  CG    . PHE A 1 275 ? 22.39   7.097   46.834  1 17.489  ? 267  PHE A CG    1 
ATOM   1951 C  CD1   . PHE A 1 275 ? 21.318  6.818   47.705  1 16.517  ? 267  PHE A CD1   1 
ATOM   1952 C  CD2   . PHE A 1 275 ? 22.565  6.291   45.699  1 16.314  ? 267  PHE A CD2   1 
ATOM   1953 C  CE1   . PHE A 1 275 ? 20.451  5.748   47.462  1 16.787  ? 267  PHE A CE1   1 
ATOM   1954 C  CE2   . PHE A 1 275 ? 21.726  5.192   45.467  1 14.975  ? 267  PHE A CE2   1 
ATOM   1955 C  CZ    . PHE A 1 275 ? 20.656  4.938   46.332  1 16.613  ? 267  PHE A CZ    1 
ATOM   1956 N  N     . GLU A 1 276 ? 26.156  9.668   47.494  1 18.407  ? 268  GLU A N     1 
ATOM   1957 C  CA    . GLU A 1 276 ? 26.963  10.881  47.407  1 20.448  ? 268  GLU A CA    1 
ATOM   1958 C  C     . GLU A 1 276 ? 26.961  11.392  45.97   1 18.674  ? 268  GLU A C     1 
ATOM   1959 O  O     . GLU A 1 276 ? 27.065  10.586  45.039  1 17.088  ? 268  GLU A O     1 
ATOM   1960 C  CB    . GLU A 1 276 ? 28.362  10.602  47.968  1 23.802  ? 268  GLU A CB    1 
ATOM   1961 C  CG    . GLU A 1 276 ? 29.254  11.846  48.091  1 31.817  ? 268  GLU A CG    1 
ATOM   1962 C  CD    . GLU A 1 276 ? 30.463  11.899  49.021  1 35.494  ? 268  GLU A CD    1 
ATOM   1963 O  OE1   . GLU A 1 276 ? 31.046  10.853  49.376  1 38.112  ? 268  GLU A OE1   1 
ATOM   1964 O  OE2   . GLU A 1 276 ? 30.799  13.034  49.437  1 41.326  ? 268  GLU A OE2   1 
ATOM   1965 N  N     . ALA A 1 277 ? 26.805  12.723  45.827  1 17.868  ? 269  ALA A N     1 
ATOM   1966 C  CA    . ALA A 1 277 ? 26.963  13.412  44.545  1 19.292  ? 269  ALA A CA    1 
ATOM   1967 C  C     . ALA A 1 277 ? 28.405  13.884  44.397  1 21.304  ? 269  ALA A C     1 
ATOM   1968 O  O     . ALA A 1 277 ? 29.024  14.312  45.381  1 22.054  ? 269  ALA A O     1 
ATOM   1969 C  CB    . ALA A 1 277 ? 25.971  14.54   44.36   1 16.723  ? 269  ALA A CB    1 
ATOM   1970 N  N     . ASN A 1 278 ? 28.902  13.791  43.153  1 20.786  ? 270  ASN A N     1 
ATOM   1971 C  CA    . ASN A 1 278 ? 30.273  14.095  42.785  1 20.063  ? 270  ASN A CA    1 
ATOM   1972 C  C     . ASN A 1 278 ? 30.267  14.823  41.443  1 18.683  ? 270  ASN A C     1 
ATOM   1973 O  O     . ASN A 1 278 ? 29.893  14.226  40.425  1 17.592  ? 270  ASN A O     1 
ATOM   1974 C  CB    . ASN A 1 278 ? 31.122  12.823  42.824  1 21.803  ? 270  ASN A CB    1 
ATOM   1975 C  CG    . ASN A 1 278 ? 32.576  13.124  42.571  1 23.825  ? 270  ASN A CG    1 
ATOM   1976 O  OD1   . ASN A 1 278 ? 33.011  13.221  41.413  1 24.515  ? 270  ASN A OD1   1 
ATOM   1977 N  ND2   . ASN A 1 278 ? 33.324  13.316  43.648  1 27.248  ? 270  ASN A ND2   1 
ATOM   1978 N  N     . LEU A 1 279 ? 30.717  16.094  41.465  1 18.45   ? 271  LEU A N     1 
ATOM   1979 C  CA    . LEU A 1 279 ? 30.734  16.982  40.302  1 18.93   ? 271  LEU A CA    1 
ATOM   1980 C  C     . LEU A 1 279 ? 31.657  16.453  39.195  1 19.68   ? 271  LEU A C     1 
ATOM   1981 O  O     . LEU A 1 279 ? 31.299  16.523  38.02   1 19.302  ? 271  LEU A O     1 
ATOM   1982 C  CB    . LEU A 1 279 ? 31.044  18.432  40.693  1 19.719  ? 271  LEU A CB    1 
ATOM   1983 C  CG    . LEU A 1 279 ? 30.759  19.514  39.642  1 21.163  ? 271  LEU A CG    1 
ATOM   1984 C  CD1   . LEU A 1 279 ? 29.274  19.804  39.385  1 19.984  ? 271  LEU A CD1   1 
ATOM   1985 C  CD2   . LEU A 1 279 ? 31.539  20.791  39.927  1 22.067  ? 271  LEU A CD2   1 
ATOM   1986 N  N     . GLU A 1 280 ? 32.819  15.907  39.587  1 22.114  ? 272  GLU A N     1 
ATOM   1987 C  CA    . GLU A 1 280 ? 33.812  15.328  38.69   1 24.016  ? 272  GLU A CA    1 
ATOM   1988 C  C     . GLU A 1 280 ? 33.254  14.141  37.91   1 21.933  ? 272  GLU A C     1 
ATOM   1989 O  O     . GLU A 1 280 ? 33.451  14.103  36.686  1 21.239  ? 272  GLU A O     1 
ATOM   1990 C  CB    . GLU A 1 280 ? 35.129  15.059  39.409  1 32.324  ? 272  GLU A CB    1 
ATOM   1991 C  CG    . GLU A 1 280 ? 36.05   16.281  39.367  1 47.472  ? 272  GLU A CG    1 
ATOM   1992 C  CD    . GLU A 1 280 ? 36.842  16.468  38.073  1 60.502  ? 272  GLU A CD    1 
ATOM   1993 O  OE1   . GLU A 1 280 ? 37.784  15.659  37.869  1 74.617  ? 272  GLU A OE1   1 
ATOM   1994 O  OE2   . GLU A 1 280 ? 36.529  17.383  37.263  1 56.422  ? 272  GLU A OE2   1 
ATOM   1995 N  N     . ARG A 1 281 ? 32.547  13.226  38.615  1 19.421  ? 273  ARG A N     1 
ATOM   1996 C  CA    . ARG A 1 281 ? 31.88   12.07   38.008  1 19.61   ? 273  ARG A CA    1 
ATOM   1997 C  C     . ARG A 1 281 ? 30.821  12.52   37      1 19.469  ? 273  ARG A C     1 
ATOM   1998 O  O     . ARG A 1 281 ? 30.721  11.926  35.916  1 20.089  ? 273  ARG A O     1 
ATOM   1999 C  CB    . ARG A 1 281 ? 31.325  11.088  39.039  1 18.595  ? 273  ARG A CB    1 
ATOM   2000 C  CG    . ARG A 1 281 ? 30.634  9.822   38.535  1 18.297  ? 273  ARG A CG    1 
ATOM   2001 C  CD    . ARG A 1 281 ? 30.014  8.901   39.582  1 18.152  ? 273  ARG A CD    1 
ATOM   2002 N  NE    . ARG A 1 281 ? 29.019  9.577   40.438  1 18.974  ? 273  ARG A NE    1 
ATOM   2003 C  CZ    . ARG A 1 281 ? 29.146  9.856   41.755  1 21.633  ? 273  ARG A CZ    1 
ATOM   2004 N  NH1   . ARG A 1 281 ? 30.153  9.399   42.489  1 19.54   ? 273  ARG A NH1   1 
ATOM   2005 N  NH2   . ARG A 1 281 ? 28.217  10.569  42.369  1 19.422  ? 273  ARG A NH2   1 
ATOM   2006 N  N     . MET A 1 282 ? 30.072  13.575  37.371  1 19.335  ? 274  MET A N     1 
ATOM   2007 C  CA    . MET A 1 282 ? 29.037  14.178  36.532  1 19.343  ? 274  MET A CA    1 
ATOM   2008 C  C     . MET A 1 282 ? 29.632  14.686  35.218  1 19.364  ? 274  MET A C     1 
ATOM   2009 O  O     . MET A 1 282 ? 29.123  14.315  34.151  1 21.349  ? 274  MET A O     1 
ATOM   2010 C  CB    . MET A 1 282 ? 28.203  15.236  37.27   1 18.031  ? 274  MET A CB    1 
ATOM   2011 C  CG    . MET A 1 282 ? 27.178  14.636  38.22   1 18.956  ? 274  MET A CG    1 
ATOM   2012 S  SD    . MET A 1 282 ? 26.193  15.916  39.025  1 21.281  ? 274  MET A SD    1 
ATOM   2013 C  CE    . MET A 1 282 ? 26.701  15.95   40.744  1 21.078  ? 274  MET A CE    1 
ATOM   2014 N  N     . LYS A 1 283 ? 30.733  15.455  35.319  1 17.821  ? 275  LYS A N     1 
ATOM   2015 C  CA    . LYS A 1 283 ? 31.497  15.992  34.194  1 18.399  ? 275  LYS A CA    1 
ATOM   2016 C  C     . LYS A 1 283 ? 31.965  14.882  33.244  1 17.582  ? 275  LYS A C     1 
ATOM   2017 O  O     . LYS A 1 283 ? 31.88   15.059  32.041  1 18.154  ? 275  LYS A O     1 
ATOM   2018 C  CB    . LYS A 1 283 ? 32.613  16.925  34.672  1 20.253  ? 275  LYS A CB    1 
ATOM   2019 C  CG    . LYS A 1 283 ? 32.132  18.284  35.172  1 20.799  ? 275  LYS A CG    1 
ATOM   2020 C  CD    . LYS A 1 283 ? 33.293  19.157  35.622  1 22.201  ? 275  LYS A CD    1 
ATOM   2021 C  CE    . LYS A 1 283 ? 32.858  20.536  35.976  1 22.78   ? 275  LYS A CE    1 
ATOM   2022 N  NZ    . LYS A 1 283 ? 33.929  21.256  36.678  1 25.841  ? 275  LYS A NZ    1 
ATOM   2023 N  N     . ALA A 1 284 ? 32.345  13.719  33.793  1 18.282  ? 276  ALA A N     1 
ATOM   2024 C  CA    . ALA A 1 284 ? 32.783  12.513  33.103  1 18.138  ? 276  ALA A CA    1 
ATOM   2025 C  C     . ALA A 1 284 ? 31.632  11.704  32.483  1 19.794  ? 276  ALA A C     1 
ATOM   2026 O  O     . ALA A 1 284 ? 31.89   10.677  31.843  1 20.794  ? 276  ALA A O     1 
ATOM   2027 C  CB    . ALA A 1 284 ? 33.636  11.686  34.05   1 17.047  ? 276  ALA A CB    1 
ATOM   2028 N  N     . GLY A 1 285 ? 30.378  12.157  32.671  1 18.373  ? 277  GLY A N     1 
ATOM   2029 C  CA    . GLY A 1 285 ? 29.18   11.566  32.092  1 18.13   ? 277  GLY A CA    1 
ATOM   2030 C  C     . GLY A 1 285 ? 28.66   10.372  32.888  1 18.023  ? 277  GLY A C     1 
ATOM   2031 O  O     . GLY A 1 285 ? 27.91   9.584   32.329  1 19.181  ? 277  GLY A O     1 
ATOM   2032 N  N     . GLY A 1 286 ? 29.072  10.264  34.168  1 18.276  ? 278  GLY A N     1 
ATOM   2033 C  CA    . GLY A 1 286 ? 28.558  9.307   35.138  1 17.645  ? 278  GLY A CA    1 
ATOM   2034 C  C     . GLY A 1 286 ? 27.253  9.807   35.757  1 17.681  ? 278  GLY A C     1 
ATOM   2035 O  O     . GLY A 1 286 ? 26.86   10.96   35.544  1 20.138  ? 278  GLY A O     1 
ATOM   2036 N  N     . HIS A 1 287 ? 26.618  8.933   36.55   1 17.454  ? 279  HIS A N     1 
ATOM   2037 C  CA    . HIS A 1 287 ? 25.411  9.231   37.318  1 17.792  ? 279  HIS A CA    1 
ATOM   2038 C  C     . HIS A 1 287 ? 25.675  10.289  38.393  1 18.358  ? 279  HIS A C     1 
ATOM   2039 O  O     . HIS A 1 287 ? 26.774  10.33   38.952  1 18.675  ? 279  HIS A O     1 
ATOM   2040 C  CB    . HIS A 1 287 ? 24.82   7.952   37.909  1 18.201  ? 279  HIS A CB    1 
ATOM   2041 C  CG    . HIS A 1 287 ? 23.976  7.167   36.957  1 19.231  ? 279  HIS A CG    1 
ATOM   2042 N  ND1   . HIS A 1 287 ? 22.845  7.656   36.326  1 20.115  ? 279  HIS A ND1   1 
ATOM   2043 C  CD2   . HIS A 1 287 ? 24.096  5.89    36.558  1 20.443  ? 279  HIS A CD2   1 
ATOM   2044 C  CE1   . HIS A 1 287 ? 22.303  6.703   35.571  1 19.793  ? 279  HIS A CE1   1 
ATOM   2045 N  NE2   . HIS A 1 287 ? 23.047  5.626   35.695  1 19.578  ? 279  HIS A NE2   1 
ATOM   2046 N  N     . HIS A 1 288 ? 24.66   11.152  38.633  1 17.43   ? 280  HIS A N     1 
ATOM   2047 C  CA    . HIS A 1 288 ? 24.618  12.153  39.693  1 16.644  ? 280  HIS A CA    1 
ATOM   2048 C  C     . HIS A 1 288 ? 24.983  11.519  41.038  1 16.869  ? 280  HIS A C     1 
ATOM   2049 O  O     . HIS A 1 288 ? 25.923  12.009  41.678  1 17.743  ? 280  HIS A O     1 
ATOM   2050 C  CB    . HIS A 1 288 ? 23.263  12.881  39.734  1 16.427  ? 280  HIS A CB    1 
ATOM   2051 C  CG    . HIS A 1 288 ? 23.22   14.032  40.698  1 15.776  ? 280  HIS A CG    1 
ATOM   2052 N  ND1   . HIS A 1 288 ? 23.184  15.343  40.279  1 16.142  ? 280  HIS A ND1   1 
ATOM   2053 C  CD2   . HIS A 1 288 ? 23.201  14.083  42.024  1 15.877  ? 280  HIS A CD2   1 
ATOM   2054 C  CE1   . HIS A 1 288 ? 23.109  16.138  41.322  1 16.043  ? 280  HIS A CE1   1 
ATOM   2055 N  NE2   . HIS A 1 288 ? 23.127  15.391  42.4    1 16.639  ? 280  HIS A NE2   1 
ATOM   2056 N  N     . TRP A 1 289 ? 24.299  10.409  41.382  1 15.902  ? 281  TRP A N     1 
ATOM   2057 C  CA    . TRP A 1 289 ? 24.442  9.677   42.632  1 17.027  ? 281  TRP A CA    1 
ATOM   2058 C  C     . TRP A 1 289 ? 25.254  8.403   42.43   1 17.033  ? 281  TRP A C     1 
ATOM   2059 O  O     . TRP A 1 289 ? 25.094  7.708   41.426  1 16.932  ? 281  TRP A O     1 
ATOM   2060 C  CB    . TRP A 1 289 ? 23.066  9.327   43.213  1 16.852  ? 281  TRP A CB    1 
ATOM   2061 C  CG    . TRP A 1 289 ? 22.206  10.522  43.52   1 17.938  ? 281  TRP A CG    1 
ATOM   2062 C  CD1   . TRP A 1 289 ? 21.073  10.902  42.859  1 17.728  ? 281  TRP A CD1   1 
ATOM   2063 C  CD2   . TRP A 1 289 ? 22.447  11.526  44.533  1 18.478  ? 281  TRP A CD2   1 
ATOM   2064 N  NE1   . TRP A 1 289 ? 20.557  12.039  43.419  1 17.823  ? 281  TRP A NE1   1 
ATOM   2065 C  CE2   . TRP A 1 289 ? 21.38   12.458  44.43   1 18.381  ? 281  TRP A CE2   1 
ATOM   2066 C  CE3   . TRP A 1 289 ? 23.442  11.729  45.517  1 19.604  ? 281  TRP A CE3   1 
ATOM   2067 C  CZ2   . TRP A 1 289 ? 21.296  13.577  45.261  1 18.44   ? 281  TRP A CZ2   1 
ATOM   2068 C  CZ3   . TRP A 1 289 ? 23.358  12.842  46.342  1 20.13   ? 281  TRP A CZ3   1 
ATOM   2069 C  CH2   . TRP A 1 289 ? 22.304  13.762  46.194  1 19.714  ? 281  TRP A CH2   1 
ATOM   2070 N  N     . ALA A 1 290 ? 26.065  8.087   43.447  1 17.454  ? 282  ALA A N     1 
ATOM   2071 C  CA    . ALA A 1 290 ? 26.586  6.737   43.652  1 16.663  ? 282  ALA A CA    1 
ATOM   2072 C  C     . ALA A 1 290 ? 26.295  6.301   45.078  1 16.865  ? 282  ALA A C     1 
ATOM   2073 O  O     . ALA A 1 290 ? 26.571  7.066   46.012  1 18.588  ? 282  ALA A O     1 
ATOM   2074 C  CB    . ALA A 1 290 ? 28.071  6.683   43.322  1 14.561  ? 282  ALA A CB    1 
ATOM   2075 N  N     . TYR A 1 291 ? 25.738  5.079   45.211  1 17.224  ? 283  TYR A N     1 
ATOM   2076 C  CA    . TYR A 1 291 ? 25.536  4.397   46.492  1 16.519  ? 283  TYR A CA    1 
ATOM   2077 C  C     . TYR A 1 291 ? 26.894  4.168   47.139  1 16.55   ? 283  TYR A C     1 
ATOM   2078 O  O     . TYR A 1 291 ? 27.86   3.835   46.448  1 15.075  ? 283  TYR A O     1 
ATOM   2079 C  CB    . TYR A 1 291 ? 24.833  3.044   46.36   1 16.002  ? 283  TYR A CB    1 
ATOM   2080 C  CG    . TYR A 1 291 ? 24.34   2.441   47.669  1 15.308  ? 283  TYR A CG    1 
ATOM   2081 C  CD1   . TYR A 1 291 ? 23.066  2.763   48.147  1 14.931  ? 283  TYR A CD1   1 
ATOM   2082 C  CD2   . TYR A 1 291 ? 25.128  1.559   48.433  1 16.38   ? 283  TYR A CD2   1 
ATOM   2083 C  CE1   . TYR A 1 291 ? 22.579  2.208   49.33   1 14.7    ? 283  TYR A CE1   1 
ATOM   2084 C  CE2   . TYR A 1 291 ? 24.662  1.045   49.644  1 15.986  ? 283  TYR A CE2   1 
ATOM   2085 C  CZ    . TYR A 1 291 ? 23.379  1.36    50.08   1 14.916  ? 283  TYR A CZ    1 
ATOM   2086 O  OH    . TYR A 1 291 ? 22.86   0.849   51.233  1 16.333  ? 283  TYR A OH    1 
ATOM   2087 N  N     . ASP A 1 292 ? 26.938  4.406   48.455  1 17.186  ? 284  ASP A N     1 
ATOM   2088 C  CA    . ASP A 1 292 ? 28.168  4.285   49.22   1 17.293  ? 284  ASP A CA    1 
ATOM   2089 C  C     . ASP A 1 292 ? 27.906  3.482   50.488  1 18.177  ? 284  ASP A C     1 
ATOM   2090 O  O     . ASP A 1 292 ? 27.317  4.006   51.443  1 19.749  ? 284  ASP A O     1 
ATOM   2091 C  CB    . ASP A 1 292 ? 28.866  5.631   49.393  1 17.98   ? 284  ASP A CB    1 
ATOM   2092 C  CG    . ASP A 1 292 ? 30.181  5.622   50.173  1 20.806  ? 284  ASP A CG    1 
ATOM   2093 O  OD1   . ASP A 1 292 ? 30.714  4.535   50.533  1 19.482  ? 284  ASP A OD1   1 
ATOM   2094 O  OD2   . ASP A 1 292 ? 30.669  6.724   50.439  1 25.014  ? 284  ASP A OD2   1 
ATOM   2095 N  N     . TYR A 1 293 ? 28.421  2.235   50.479  1 18.964  ? 285  TYR A N     1 
ATOM   2096 C  CA    . TYR A 1 293 ? 28.414  1.29    51.596  1 19.442  ? 285  TYR A CA    1 
ATOM   2097 C  C     . TYR A 1 293 ? 29.057  1.833   52.878  1 19.109  ? 285  TYR A C     1 
ATOM   2098 O  O     . TYR A 1 293 ? 28.661  1.382   53.951  1 20.646  ? 285  TYR A O     1 
ATOM   2099 C  CB    . TYR A 1 293 ? 28.937  -0.113  51.266  1 19.567  ? 285  TYR A CB    1 
ATOM   2100 C  CG    . TYR A 1 293 ? 27.953  -0.902  50.42   1 20.453  ? 285  TYR A CG    1 
ATOM   2101 C  CD1   . TYR A 1 293 ? 26.854  -1.528  51.026  1 20.835  ? 285  TYR A CD1   1 
ATOM   2102 C  CD2   . TYR A 1 293 ? 28.077  -0.963  49.023  1 23.282  ? 285  TYR A CD2   1 
ATOM   2103 C  CE1   . TYR A 1 293 ? 25.914  -2.213  50.27   1 23.325  ? 285  TYR A CE1   1 
ATOM   2104 C  CE2   . TYR A 1 293 ? 27.156  -1.678  48.253  1 24.79   ? 285  TYR A CE2   1 
ATOM   2105 C  CZ    . TYR A 1 293 ? 26.077  -2.293  48.894  1 25.811  ? 285  TYR A CZ    1 
ATOM   2106 O  OH    . TYR A 1 293 ? 25.1    -2.988  48.251  1 31.61   ? 285  TYR A OH    1 
ATOM   2107 N  N     . THR A 1 294 ? 29.996  2.785   52.765  1 20.585  ? 286  THR A N     1 
ATOM   2108 C  CA    . THR A 1 294 ? 30.712  3.364   53.905  1 22.884  ? 286  THR A CA    1 
ATOM   2109 C  C     . THR A 1 294 ? 29.882  4.437   54.626  1 23.607  ? 286  THR A C     1 
ATOM   2110 O  O     . THR A 1 294 ? 30.16   4.711   55.795  1 26.359  ? 286  THR A O     1 
ATOM   2111 C  CB    . THR A 1 294 ? 32.145  3.815   53.579  1 24.932  ? 286  THR A CB    1 
ATOM   2112 O  OG1   . THR A 1 294 ? 32.074  5.001   52.785  1 25.632  ? 286  THR A OG1   1 
ATOM   2113 C  CG2   . THR A 1 294 ? 33.02   2.749   52.932  1 23.389  ? 286  THR A CG2   1 
ATOM   2114 N  N     . LYS A 1 295 ? 28.859  5.008   53.952  1 22.716  ? 287  LYS A N     1 
ATOM   2115 C  CA    . LYS A 1 295 ? 27.983  6.019   54.536  1 20.944  ? 287  LYS A CA    1 
ATOM   2116 C  C     . LYS A 1 295 ? 26.942  5.347   55.44   1 21.118  ? 287  LYS A C     1 
ATOM   2117 O  O     . LYS A 1 295 ? 26.242  4.427   54.981  1 20.105  ? 287  LYS A O     1 
ATOM   2118 C  CB    . LYS A 1 295 ? 27.337  7.001   53.545  1 20.571  ? 287  LYS A CB    1 
ATOM   2119 C  CG    . LYS A 1 295 ? 28.238  7.804   52.621  1 21.166  ? 287  LYS A CG    1 
ATOM   2120 C  CD    . LYS A 1 295 ? 28.911  9.011   53.239  1 22.79   ? 287  LYS A CD    1 
ATOM   2121 C  CE    . LYS A 1 295 ? 29.897  9.471   52.23   1 23.644  ? 287  LYS A CE    1 
ATOM   2122 N  NZ    . LYS A 1 295 ? 30.516  10.664  52.789  1 29.537  ? 287  LYS A NZ    1 
ATOM   2123 N  N     . PRO A 1 296 ? 26.808  5.755   56.739  1 20.347  ? 288  PRO A N     1 
ATOM   2124 C  CA    . PRO A 1 296 ? 25.64   5.371   57.536  1 19.105  ? 288  PRO A CA    1 
ATOM   2125 C  C     . PRO A 1 296 ? 24.396  6.178   57.151  1 17.776  ? 288  PRO A C     1 
ATOM   2126 O  O     . PRO A 1 296 ? 24.535  7.319   56.687  1 16.836  ? 288  PRO A O     1 
ATOM   2127 C  CB    . PRO A 1 296 ? 26.101  5.627   58.967  1 18.981  ? 288  PRO A CB    1 
ATOM   2128 C  CG    . PRO A 1 296 ? 27.058  6.807   58.819  1 18.475  ? 288  PRO A CG    1 
ATOM   2129 C  CD    . PRO A 1 296 ? 27.755  6.603   57.511  1 19.556  ? 288  PRO A CD    1 
ATOM   2130 N  N     . ILE A 1 297 ? 23.203  5.601   57.404  1 17.347  ? 289  ILE A N     1 
ATOM   2131 C  CA    . ILE A 1 297 ? 21.944  6.351   57.496  1 15.748  ? 289  ILE A CA    1 
ATOM   2132 C  C     . ILE A 1 297 ? 22.184  7.502   58.472  1 16.194  ? 289  ILE A C     1 
ATOM   2133 O  O     . ILE A 1 297 ? 22.617  7.251   59.599  1 15.779  ? 289  ILE A O     1 
ATOM   2134 C  CB    . ILE A 1 297 ? 20.733  5.475   57.909  1 16.285  ? 289  ILE A CB    1 
ATOM   2135 C  CG1   . ILE A 1 297 ? 20.421  4.421   56.834  1 16.912  ? 289  ILE A CG1   1 
ATOM   2136 C  CG2   . ILE A 1 297 ? 19.49   6.326   58.269  1 14.578  ? 289  ILE A CG2   1 
ATOM   2137 C  CD1   . ILE A 1 297 ? 19.646  3.206   57.321  1 17.438  ? 289  ILE A CD1   1 
ATOM   2138 N  N     . THR A 1 298 ? 21.954  8.729   57.987  1 14.89   ? 290  THR A N     1 
ATOM   2139 C  CA    . THR A 1 298 ? 22.204  9.95    58.741  1 15.893  ? 290  THR A CA    1 
ATOM   2140 C  C     . THR A 1 298 ? 20.9    10.75   58.82   1 18.08   ? 290  THR A C     1 
ATOM   2141 O  O     . THR A 1 298 ? 20.086  10.696  57.888  1 17.533  ? 290  THR A O     1 
ATOM   2142 C  CB    . THR A 1 298 ? 23.417  10.683  58.144  1 16.633  ? 290  THR A CB    1 
ATOM   2143 O  OG1   . THR A 1 298 ? 24.519  9.781   58.256  1 16.798  ? 290  THR A OG1   1 
ATOM   2144 C  CG2   . THR A 1 298 ? 23.822  11.975  58.846  1 15.658  ? 290  THR A CG2   1 
ATOM   2145 N  N     . TRP A 1 299 ? 20.687  11.396  59.984  1 17.82   ? 291  TRP A N     1 
ATOM   2146 C  CA    . TRP A 1 299 ? 19.542  12.251  60.263  1 19.48   ? 291  TRP A CA    1 
ATOM   2147 C  C     . TRP A 1 299 ? 20.034  13.64   60.649  1 19.939  ? 291  TRP A C     1 
ATOM   2148 O  O     . TRP A 1 299 ? 20.992  13.729  61.423  1 18.081  ? 291  TRP A O     1 
ATOM   2149 C  CB    . TRP A 1 299 ? 18.652  11.684  61.379  1 18.793  ? 291  TRP A CB    1 
ATOM   2150 C  CG    . TRP A 1 299 ? 18.196  10.261  61.196  1 21.958  ? 291  TRP A CG    1 
ATOM   2151 C  CD1   . TRP A 1 299 ? 18.893  9.131   61.541  1 21.767  ? 291  TRP A CD1   1 
ATOM   2152 C  CD2   . TRP A 1 299 ? 16.932  9.811   60.656  1 21.749  ? 291  TRP A CD2   1 
ATOM   2153 N  NE1   . TRP A 1 299 ? 18.156  8.008   61.26   1 22.85   ? 291  TRP A NE1   1 
ATOM   2154 C  CE2   . TRP A 1 299 ? 16.949  8.386   60.727  1 21.546  ? 291  TRP A CE2   1 
ATOM   2155 C  CE3   . TRP A 1 299 ? 15.794  10.464  60.128  1 20.239  ? 291  TRP A CE3   1 
ATOM   2156 C  CZ2   . TRP A 1 299 ? 15.876  7.604   60.279  1 21.992  ? 291  TRP A CZ2   1 
ATOM   2157 C  CZ3   . TRP A 1 299 ? 14.731  9.692   59.694  1 20.61   ? 291  TRP A CZ3   1 
ATOM   2158 C  CH2   . TRP A 1 299 ? 14.777  8.279   59.768  1 22.326  ? 291  TRP A CH2   1 
ATOM   2159 N  N     . ILE A 1 300 ? 19.373  14.683  60.095  1 17.745  ? 292  ILE A N     1 
ATOM   2160 C  CA    . ILE A 1 300 ? 19.567  16.084  60.467  1 16.691  ? 292  ILE A CA    1 
ATOM   2161 C  C     . ILE A 1 300 ? 18.32   16.534  61.24   1 17.766  ? 292  ILE A C     1 
ATOM   2162 O  O     . ILE A 1 300 ? 17.242  16.602  60.655  1 17.847  ? 292  ILE A O     1 
ATOM   2163 C  CB    . ILE A 1 300 ? 19.904  17.013  59.275  1 15.906  ? 292  ILE A CB    1 
ATOM   2164 C  CG1   . ILE A 1 300 ? 21.149  16.552  58.458  1 16.82   ? 292  ILE A CG1   1 
ATOM   2165 C  CG2   . ILE A 1 300 ? 20.067  18.462  59.747  1 15.194  ? 292  ILE A CG2   1 
ATOM   2166 C  CD1   . ILE A 1 300 ? 21.385  17.266  57.129  1 17.015  ? 292  ILE A CD1   1 
ATOM   2167 N  N     . THR A 1 301 ? 18.487  16.837  62.541  1 17.779  ? 293  THR A N     1 
ATOM   2168 C  CA    . THR A 1 301 ? 17.432  17.425  63.377  1 18.481  ? 293  THR A CA    1 
ATOM   2169 C  C     . THR A 1 301 ? 17.54   18.945  63.275  1 19.132  ? 293  THR A C     1 
ATOM   2170 O  O     . THR A 1 301 ? 18.615  19.504  63.515  1 21.12   ? 293  THR A O     1 
ATOM   2171 C  CB    . THR A 1 301 ? 17.405  16.91   64.827  1 17.083  ? 293  THR A CB    1 
ATOM   2172 O  OG1   . THR A 1 301 ? 18.686  17.141  65.406  1 15.711  ? 293  THR A OG1   1 
ATOM   2173 C  CG2   . THR A 1 301 ? 17.006  15.448  64.934  1 16.357  ? 293  THR A CG2   1 
ATOM   2174 N  N     . ILE A 1 302 ? 16.455  19.573  62.798  1 18.648  ? 294  ILE A N     1 
ATOM   2175 C  CA    . ILE A 1 302 ? 16.327  21.022  62.683  1 17.679  ? 294  ILE A CA    1 
ATOM   2176 C  C     . ILE A 1 302 ? 15.235  21.46   63.677  1 18.832  ? 294  ILE A C     1 
ATOM   2177 O  O     . ILE A 1 302 ? 14.055  21.181  63.404  1 18.054  ? 294  ILE A O     1 
ATOM   2178 C  CB    . ILE A 1 302 ? 16.067  21.493  61.227  1 16.129  ? 294  ILE A CB    1 
ATOM   2179 C  CG1   . ILE A 1 302 ? 17.118  20.94   60.215  1 15.191  ? 294  ILE A CG1   1 
ATOM   2180 C  CG2   . ILE A 1 302 ? 15.947  23.03   61.165  1 15.479  ? 294  ILE A CG2   1 
ATOM   2181 C  CD1   . ILE A 1 302 ? 16.738  21.034  58.74   1 14.15   ? 294  ILE A CD1   1 
ATOM   2182 N  N     . PRO A 1 303 ? 15.569  22.142  64.819  1 18.499  ? 295  PRO A N     1 
ATOM   2183 C  CA    . PRO A 1 303 ? 14.558  22.794  65.662  1 18.202  ? 295  PRO A CA    1 
ATOM   2184 C  C     . PRO A 1 303 ? 13.73   23.781  64.852  1 19.193  ? 295  PRO A C     1 
ATOM   2185 O  O     . PRO A 1 303 ? 14.295  24.576  64.105  1 19.006  ? 295  PRO A O     1 
ATOM   2186 C  CB    . PRO A 1 303 ? 15.327  23.469  66.801  1 18.444  ? 295  PRO A CB    1 
ATOM   2187 C  CG    . PRO A 1 303 ? 16.635  22.697  66.823  1 18.181  ? 295  PRO A CG    1 
ATOM   2188 C  CD    . PRO A 1 303 ? 16.922  22.308  65.391  1 17.556  ? 295  PRO A CD    1 
ATOM   2189 N  N     . ARG A 1 304 ? 12.403  23.605  64.902  1 18.41   ? 296  ARG A N     1 
ATOM   2190 C  CA    . ARG A 1 304 ? 11.455  24.414  64.142  1 18.393  ? 296  ARG A CA    1 
ATOM   2191 C  C     . ARG A 1 304 ? 11.55   25.854  64.635  1 18.746  ? 296  ARG A C     1 
ATOM   2192 O  O     . ARG A 1 304 ? 11.575  26.09   65.84   1 18.239  ? 296  ARG A O     1 
ATOM   2193 C  CB    . ARG A 1 304 ? 10.024  23.864  64.206  1 17.946  ? 296  ARG A CB    1 
ATOM   2194 C  CG    . ARG A 1 304 ? 9.887   22.564  63.423  1 17.818  ? 296  ARG A CG    1 
ATOM   2195 C  CD    . ARG A 1 304 ? 8.505   21.948  63.578  1 17.223  ? 296  ARG A CD    1 
ATOM   2196 N  NE    . ARG A 1 304 ? 7.479   22.705  62.841  1 17.041  ? 296  ARG A NE    1 
ATOM   2197 C  CZ    . ARG A 1 304 ? 6.167   22.526  62.904  1 17.102  ? 296  ARG A CZ    1 
ATOM   2198 N  NH1   . ARG A 1 304 ? 5.645   21.556  63.649  1 17.302  ? 296  ARG A NH1   1 
ATOM   2199 N  NH2   . ARG A 1 304 ? 5.376   23.33   62.214  1 16.827  ? 296  ARG A NH2   1 
ATOM   2200 N  N     . GLY A 1 305 ? 11.714  26.766  63.667  1 18.473  ? 297  GLY A N     1 
ATOM   2201 C  CA    . GLY A 1 305 ? 11.986  28.169  63.919  1 19.945  ? 297  GLY A CA    1 
ATOM   2202 C  C     . GLY A 1 305 ? 13.367  28.421  64.528  1 20.237  ? 297  GLY A C     1 
ATOM   2203 O  O     . GLY A 1 305 ? 13.517  29.464  65.158  1 23.694  ? 297  GLY A O     1 
ATOM   2204 N  N     . ALA A 1 306 ? 14.359  27.526  64.314  1 19.381  ? 298  ALA A N     1 
ATOM   2205 C  CA    . ALA A 1 306 ? 15.75   27.707  64.764  1 20.21   ? 298  ALA A CA    1 
ATOM   2206 C  C     . ALA A 1 306 ? 16.299  29.056  64.285  1 21.413  ? 298  ALA A C     1 
ATOM   2207 O  O     . ALA A 1 306 ? 16.012  29.484  63.162  1 18.162  ? 298  ALA A O     1 
ATOM   2208 C  CB    . ALA A 1 306 ? 16.65   26.577  64.321  1 17.341  ? 298  ALA A CB    1 
ATOM   2209 N  N     . LYS A 1 307 ? 17.022  29.733  65.191  1 22.666  ? 299  LYS A N     1 
ATOM   2210 C  CA    . LYS A 1 307 ? 17.589  31.049  64.913  1 25.848  ? 299  LYS A CA    1 
ATOM   2211 C  C     . LYS A 1 307 ? 18.976  30.938  64.278  1 23.677  ? 299  LYS A C     1 
ATOM   2212 O  O     . LYS A 1 307 ? 19.416  31.889  63.631  1 22.79   ? 299  LYS A O     1 
ATOM   2213 C  CB    . LYS A 1 307 ? 17.468  32.011  66.106  1 30.814  ? 299  LYS A CB    1 
ATOM   2214 C  CG    . LYS A 1 307 ? 16.042  32.556  66.363  1 36.371  ? 299  LYS A CG    1 
ATOM   2215 C  CD    . LYS A 1 307 ? 15.589  33.663  65.407  1 43.013  ? 299  LYS A CD    1 
ATOM   2216 C  CE    . LYS A 1 307 ? 14.37   34.407  65.843  1 46.295  ? 299  LYS A CE    1 
ATOM   2217 N  NZ    . LYS A 1 307 ? 13.124  33.707  65.541  1 41.799  ? 299  LYS A NZ    1 
ATOM   2218 N  N     . SER A 1 308 ? 19.616  29.763  64.422  1 22.357  ? 300  SER A N     1 
ATOM   2219 C  CA    . SER A 1 308 ? 20.995  29.519  64.019  1 20.713  ? 300  SER A CA    1 
ATOM   2220 C  C     . SER A 1 308 ? 21.179  28.083  63.538  1 20.842  ? 300  SER A C     1 
ATOM   2221 O  O     . SER A 1 308 ? 20.592  27.156  64.098  1 18.449  ? 300  SER A O     1 
ATOM   2222 C  CB    . SER A 1 308 ? 21.941  29.88   65.149  1 18.971  ? 300  SER A CB    1 
ATOM   2223 O  OG    . SER A 1 308 ? 23.265  29.462  64.881  1 19.428  ? 300  SER A OG    1 
ATOM   2224 N  N     . LYS A 1 309 ? 22.098  27.924  62.569  1 21.077  ? 301  LYS A N     1 
ATOM   2225 C  CA    . LYS A 1 309 ? 22.577  26.63   62.105  1 24.311  ? 301  LYS A CA    1 
ATOM   2226 C  C     . LYS A 1 309 ? 23.29   25.836  63.213  1 25.378  ? 301  LYS A C     1 
ATOM   2227 O  O     . LYS A 1 309 ? 23.429  24.622  63.058  1 24.992  ? 301  LYS A O     1 
ATOM   2228 C  CB    . LYS A 1 309 ? 23.334  26.746  60.775  1 25.162  ? 301  LYS A CB    1 
ATOM   2229 C  CG    . LYS A 1 309 ? 24.738  27.322  60.865  1 24.638  ? 301  LYS A CG    1 
ATOM   2230 C  CD    . LYS A 1 309 ? 25.359  27.515  59.495  1 27.463  ? 301  LYS A CD    1 
ATOM   2231 C  CE    . LYS A 1 309 ? 26.797  27.813  59.767  1 26.477  ? 301  LYS A CE    1 
ATOM   2232 N  NZ    . LYS A 1 309 ? 27.456  27.917  58.466  1 32.317  ? 301  LYS A NZ    1 
ATOM   2233 N  N     . ASP A 1 310 ? 23.72   26.508  64.303  1 25.39   ? 302  ASP A N     1 
ATOM   2234 C  CA    . ASP A 1 310 ? 24.324  25.908  65.495  1 28.91   ? 302  ASP A CA    1 
ATOM   2235 C  C     . ASP A 1 310 ? 23.385  24.962  66.239  1 26.775  ? 302  ASP A C     1 
ATOM   2236 O  O     . ASP A 1 310 ? 23.87   24.052  66.908  1 27.62   ? 302  ASP A O     1 
ATOM   2237 C  CB    . ASP A 1 310 ? 24.899  26.95   66.447  1 32.405  ? 302  ASP A CB    1 
ATOM   2238 C  CG    . ASP A 1 310 ? 25.987  27.861  65.9    1 37.331  ? 302  ASP A CG    1 
ATOM   2239 O  OD1   . ASP A 1 310 ? 26.608  27.528  64.854  1 37.223  ? 302  ASP A OD1   1 
ATOM   2240 O  OD2   . ASP A 1 310 ? 26.197  28.925  66.523  1 46.628  ? 302  ASP A OD2   1 
ATOM   2241 N  N     . GLU A 1 311 ? 22.07   25.186  66.111  1 26.574  ? 303  GLU A N     1 
ATOM   2242 C  CA    . GLU A 1 311 ? 21.01   24.375  66.704  1 26.412  ? 303  GLU A CA    1 
ATOM   2243 C  C     . GLU A 1 311 ? 20.843  22.998  66.042  1 24.477  ? 303  GLU A C     1 
ATOM   2244 O  O     . GLU A 1 311 ? 20.226  22.111  66.648  1 24.446  ? 303  GLU A O     1 
ATOM   2245 C  CB    . GLU A 1 311 ? 19.691  25.148  66.656  1 25.649  ? 303  GLU A CB    1 
ATOM   2246 C  CG    . GLU A 1 311 ? 19.659  26.355  67.594  1 26.422  ? 303  GLU A CG    1 
ATOM   2247 C  CD    . GLU A 1 311 ? 18.365  27.143  67.505  1 26.27   ? 303  GLU A CD    1 
ATOM   2248 O  OE1   . GLU A 1 311 ? 17.279  26.613  67.836  1 24.618  ? 303  GLU A OE1   1 
ATOM   2249 O  OE2   . GLU A 1 311 ? 18.482  28.3    67.058  1 29.08   ? 303  GLU A OE2   1 
ATOM   2250 N  N     . VAL A 1 312 ? 21.321  22.849  64.796  1 22.217  ? 304  VAL A N     1 
ATOM   2251 C  CA    . VAL A 1 312 ? 21.155  21.656  63.967  1 23.307  ? 304  VAL A CA    1 
ATOM   2252 C  C     . VAL A 1 312 ? 22.107  20.57   64.477  1 23.993  ? 304  VAL A C     1 
ATOM   2253 O  O     . VAL A 1 312 ? 23.262  20.887  64.792  1 25.204  ? 304  VAL A O     1 
ATOM   2254 C  CB    . VAL A 1 312 ? 21.396  22.1    62.5    1 24.032  ? 304  VAL A CB    1 
ATOM   2255 C  CG1   . VAL A 1 312 ? 21.741  20.998  61.507  1 24.275  ? 304  VAL A CG1   1 
ATOM   2256 C  CG2   . VAL A 1 312 ? 20.272  22.978  61.947  1 22.531  ? 304  VAL A CG2   1 
ATOM   2257 N  N     . LYS A 1 313 ? 21.62   19.309  64.533  1 23.182  ? 305  LYS A N     1 
ATOM   2258 C  CA    . LYS A 1 313 ? 22.436  18.153  64.91   1 24.778  ? 305  LYS A CA    1 
ATOM   2259 C  C     . LYS A 1 313 ? 22.342  17.025  63.883  1 24.407  ? 305  LYS A C     1 
ATOM   2260 O  O     . LYS A 1 313 ? 21.271  16.761  63.327  1 20.689  ? 305  LYS A O     1 
ATOM   2261 C  CB    . LYS A 1 313 ? 22.123  17.633  66.318  1 27.058  ? 305  LYS A CB    1 
ATOM   2262 C  CG    . LYS A 1 313 ? 22.464  18.535  67.504  1 30.788  ? 305  LYS A CG    1 
ATOM   2263 C  CD    . LYS A 1 313 ? 22.078  17.783  68.778  1 36.362  ? 305  LYS A CD    1 
ATOM   2264 C  CE    . LYS A 1 313 ? 21.5    18.531  69.941  1 41.072  ? 305  LYS A CE    1 
ATOM   2265 N  NZ    . LYS A 1 313 ? 22.511  18.962  70.908  1 43.095  ? 305  LYS A NZ    1 
ATOM   2266 N  N     . TYR A 1 314 ? 23.496  16.375  63.673  1 22.26   ? 306  TYR A N     1 
ATOM   2267 C  CA    . TYR A 1 314 ? 23.659  15.204  62.822  1 22.61   ? 306  TYR A CA    1 
ATOM   2268 C  C     . TYR A 1 314 ? 23.711  13.941  63.686  1 20.89   ? 306  TYR A C     1 
ATOM   2269 O  O     . TYR A 1 314 ? 24.497  13.865  64.619  1 22.523  ? 306  TYR A O     1 
ATOM   2270 C  CB    . TYR A 1 314 ? 24.934  15.308  61.972  1 22.762  ? 306  TYR A CB    1 
ATOM   2271 C  CG    . TYR A 1 314 ? 25.193  16.532  61.104  1 24.676  ? 306  TYR A CG    1 
ATOM   2272 C  CD1   . TYR A 1 314 ? 24.146  17.291  60.531  1 24.449  ? 306  TYR A CD1   1 
ATOM   2273 C  CD2   . TYR A 1 314 ? 26.523  16.883  60.794  1 25.563  ? 306  TYR A CD2   1 
ATOM   2274 C  CE1   . TYR A 1 314 ? 24.417  18.386  59.716  1 22.898  ? 306  TYR A CE1   1 
ATOM   2275 C  CE2   . TYR A 1 314 ? 26.804  17.979  59.976  1 26.542  ? 306  TYR A CE2   1 
ATOM   2276 C  CZ    . TYR A 1 314 ? 25.743  18.723  59.442  1 24.309  ? 306  TYR A CZ    1 
ATOM   2277 O  OH    . TYR A 1 314 ? 25.998  19.793  58.643  1 22.04   ? 306  TYR A OH    1 
ATOM   2278 N  N     . TRP A 1 315 ? 22.928  12.936  63.295  1 18.38   ? 307  TRP A N     1 
ATOM   2279 C  CA    . TRP A 1 315 ? 22.773  11.66   63.987  1 18.164  ? 307  TRP A CA    1 
ATOM   2280 C  C     . TRP A 1 315 ? 23.053  10.545  62.987  1 19.336  ? 307  TRP A C     1 
ATOM   2281 O  O     . TRP A 1 315 ? 22.675  10.705  61.832  1 20.342  ? 307  TRP A O     1 
ATOM   2282 C  CB    . TRP A 1 315 ? 21.344  11.541  64.547  1 17.091  ? 307  TRP A CB    1 
ATOM   2283 C  CG    . TRP A 1 315 ? 20.919  12.711  65.402  1 17.697  ? 307  TRP A CG    1 
ATOM   2284 C  CD1   . TRP A 1 315 ? 20.466  13.931  64.971  1 16.928  ? 307  TRP A CD1   1 
ATOM   2285 C  CD2   . TRP A 1 315 ? 20.943  12.771  66.845  1 16.974  ? 307  TRP A CD2   1 
ATOM   2286 N  NE1   . TRP A 1 315 ? 20.195  14.746  66.036  1 17.497  ? 307  TRP A NE1   1 
ATOM   2287 C  CE2   . TRP A 1 315 ? 20.485  14.068  67.197  1 18.2    ? 307  TRP A CE2   1 
ATOM   2288 C  CE3   . TRP A 1 315 ? 21.297  11.863  67.867  1 18.269  ? 307  TRP A CE3   1 
ATOM   2289 C  CZ2   . TRP A 1 315 ? 20.38   14.48   68.533  1 19.077  ? 307  TRP A CZ2   1 
ATOM   2290 C  CZ3   . TRP A 1 315 ? 21.194  12.266  69.191  1 18.868  ? 307  TRP A CZ3   1 
ATOM   2291 C  CH2   . TRP A 1 315 ? 20.751  13.565  69.511  1 20.468  ? 307  TRP A CH2   1 
ATOM   2292 N  N     . HIS A 1 316 ? 23.652  9.415   63.41   1 19.174  ? 308  HIS A N     1 
ATOM   2293 C  CA    . HIS A 1 316 ? 23.943  8.338   62.463  1 19.799  ? 308  HIS A CA    1 
ATOM   2294 C  C     . HIS A 1 316 ? 23.621  6.954   63.03   1 20.076  ? 308  HIS A C     1 
ATOM   2295 O  O     . HIS A 1 316 ? 23.7    6.743   64.244  1 21.34   ? 308  HIS A O     1 
ATOM   2296 C  CB    . HIS A 1 316 ? 25.367  8.471   61.9    1 19.98   ? 308  HIS A CB    1 
ATOM   2297 C  CG    . HIS A 1 316 ? 26.407  8.123   62.901  1 21.604  ? 308  HIS A CG    1 
ATOM   2298 N  ND1   . HIS A 1 316 ? 26.852  9.015   63.855  1 20.475  ? 308  HIS A ND1   1 
ATOM   2299 C  CD2   . HIS A 1 316 ? 27.017  6.947   63.143  1 21.202  ? 308  HIS A CD2   1 
ATOM   2300 C  CE1   . HIS A 1 316 ? 27.744  8.402   64.616  1 21.465  ? 308  HIS A CE1   1 
ATOM   2301 N  NE2   . HIS A 1 316 ? 27.847  7.144   64.21   1 21.495  ? 308  HIS A NE2   1 
ATOM   2302 N  N     . TRP A 1 317 ? 23.343  6.016   62.113  1 18.169  ? 309  TRP A N     1 
ATOM   2303 C  CA    . TRP A 1 317 ? 23.16   4.602   62.432  1 20.099  ? 309  TRP A CA    1 
ATOM   2304 C  C     . TRP A 1 317 ? 24.206  3.771   61.673  1 20.748  ? 309  TRP A C     1 
ATOM   2305 O  O     . TRP A 1 317 ? 25.378  3.896   61.992  1 21.56   ? 309  TRP A O     1 
ATOM   2306 C  CB    . TRP A 1 317 ? 21.68   4.144   62.347  1 19.61   ? 309  TRP A CB    1 
ATOM   2307 C  CG    . TRP A 1 317 ? 21.482  2.682   62.674  1 21.142  ? 309  TRP A CG    1 
ATOM   2308 C  CD1   . TRP A 1 317 ? 21.721  2.061   63.867  1 21.884  ? 309  TRP A CD1   1 
ATOM   2309 C  CD2   . TRP A 1 317 ? 21.099  1.632   61.756  1 21.175  ? 309  TRP A CD2   1 
ATOM   2310 N  NE1   . TRP A 1 317 ? 21.493  0.712   63.762  1 21.964  ? 309  TRP A NE1   1 
ATOM   2311 C  CE2   . TRP A 1 317 ? 21.114  0.413   62.485  1 21.407  ? 309  TRP A CE2   1 
ATOM   2312 C  CE3   . TRP A 1 317 ? 20.744  1.592   60.392  1 22.442  ? 309  TRP A CE3   1 
ATOM   2313 C  CZ2   . TRP A 1 317 ? 20.782  -0.821  61.902  1 21.457  ? 309  TRP A CZ2   1 
ATOM   2314 C  CZ3   . TRP A 1 317 ? 20.406  0.374   59.815  1 22.637  ? 309  TRP A CZ3   1 
ATOM   2315 C  CH2   . TRP A 1 317 ? 20.431  -0.821  60.561  1 21.798  ? 309  TRP A CH2   1 
ATOM   2316 N  N     . LYS A 1 318 ? 23.792  3.009   60.647  1 19.675  ? 310  LYS A N     1 
ATOM   2317 C  CA    . LYS A 1 318 ? 24.555  2.061   59.844  1 19.764  ? 310  LYS A CA    1 
ATOM   2318 C  C     . LYS A 1 318 ? 24.061  2.212   58.407  1 19.509  ? 310  LYS A C     1 
ATOM   2319 O  O     . LYS A 1 318 ? 23.032  2.849   58.171  1 19.3    ? 310  LYS A O     1 
ATOM   2320 C  CB    . LYS A 1 318 ? 24.333  0.617   60.33   1 20.557  ? 310  LYS A CB    1 
ATOM   2321 C  CG    . LYS A 1 318 ? 24.798  0.256   61.753  1 23.882  ? 310  LYS A CG    1 
ATOM   2322 C  CD    . LYS A 1 318 ? 24.488  -1.164  62.219  1 24.584  ? 310  LYS A CD    1 
ATOM   2323 C  CE    . LYS A 1 318 ? 25.117  -1.392  63.566  1 27.367  ? 310  LYS A CE    1 
ATOM   2324 N  NZ    . LYS A 1 318 ? 24.355  -2.311  64.423  1 27.56   ? 310  LYS A NZ    1 
ATOM   2325 N  N     . ASN A 1 319 ? 24.813  1.646   57.456  1 18.608  ? 311  ASN A N     1 
ATOM   2326 C  CA    . ASN A 1 319 ? 24.434  1.587   56.051  1 18.627  ? 311  ASN A CA    1 
ATOM   2327 C  C     . ASN A 1 319 ? 23.113  0.829   55.869  1 17.713  ? 311  ASN A C     1 
ATOM   2328 O  O     . ASN A 1 319 ? 22.882  -0.21   56.479  1 18.166  ? 311  ASN A O     1 
ATOM   2329 C  CB    . ASN A 1 319 ? 25.552  1.008   55.191  1 17.896  ? 311  ASN A CB    1 
ATOM   2330 C  CG    . ASN A 1 319 ? 25.278  1.18    53.715  1 19.125  ? 311  ASN A CG    1 
ATOM   2331 O  OD1   . ASN A 1 319 ? 24.892  0.219   53.041  1 19.492  ? 311  ASN A OD1   1 
ATOM   2332 N  ND2   . ASN A 1 319 ? 25.456  2.387   53.196  1 18.071  ? 311  ASN A ND2   1 
ATOM   2333 N  N     . GLY A 1 320 ? 22.263  1.422   55.039  1 17.816  ? 312  GLY A N     1 
ATOM   2334 C  CA    . GLY A 1 320 ? 20.963  0.922   54.609  1 17.398  ? 312  GLY A CA    1 
ATOM   2335 C  C     . GLY A 1 320 ? 20.211  2.04    53.891  1 17.549  ? 312  GLY A C     1 
ATOM   2336 O  O     . GLY A 1 320 ? 20.696  3.169   53.84   1 17.376  ? 312  GLY A O     1 
ATOM   2337 N  N     . MET A 1 321 ? 19.016  1.73    53.374  1 16.574  ? 313  MET A N     1 
ATOM   2338 C  CA    . MET A 1 321 ? 18.205  2.67    52.617  1 17.349  ? 313  MET A CA    1 
ATOM   2339 C  C     . MET A 1 321 ? 16.799  2.721   53.239  1 17.326  ? 313  MET A C     1 
ATOM   2340 O  O     . MET A 1 321 ? 15.979  1.839   52.961  1 15.836  ? 313  MET A O     1 
ATOM   2341 C  CB    . MET A 1 321 ? 18.284  2.405   51.106  1 16.49   ? 313  MET A CB    1 
ATOM   2342 C  CG    . MET A 1 321 ? 17.738  3.5     50.222  1 17.594  ? 313  MET A CG    1 
ATOM   2343 S  SD    . MET A 1 321 ? 18.09   3.073   48.505  1 20.3    ? 313  MET A SD    1 
ATOM   2344 C  CE    . MET A 1 321 ? 16.933  4.089   47.552  1 17.779  ? 313  MET A CE    1 
ATOM   2345 N  N     . PRO A 1 322 ? 16.507  3.741   54.104  1 16.142  ? 314  PRO A N     1 
ATOM   2346 C  CA    . PRO A 1 322 ? 15.154  4.02    54.55   1 16.229  ? 314  PRO A CA    1 
ATOM   2347 C  C     . PRO A 1 322 ? 14.454  4.955   53.562  1 16.684  ? 314  PRO A C     1 
ATOM   2348 O  O     . PRO A 1 322 ? 14.798  6.135   53.499  1 16.965  ? 314  PRO A O     1 
ATOM   2349 C  CB    . PRO A 1 322 ? 15.378  4.528   55.97   1 15.826  ? 314  PRO A CB    1 
ATOM   2350 C  CG    . PRO A 1 322 ? 16.743  5.207   55.905  1 17.25   ? 314  PRO A CG    1 
ATOM   2351 C  CD    . PRO A 1 322 ? 17.447  4.741   54.661  1 16.243  ? 314  PRO A CD    1 
ATOM   2352 N  N     . ILE A 1 323 ? 13.523  4.41    52.762  1 16.666  ? 315  ILE A N     1 
ATOM   2353 C  CA    . ILE A 1 323 ? 13.084  5.089   51.545  1 16.063  ? 315  ILE A CA    1 
ATOM   2354 C  C     . ILE A 1 323 ? 12.117  6.213   51.911  1 16.702  ? 315  ILE A C     1 
ATOM   2355 O  O     . ILE A 1 323 ? 12.37   7.359   51.535  1 18.056  ? 315  ILE A O     1 
ATOM   2356 C  CB    . ILE A 1 323 ? 12.571  4.147   50.43   1 15.638  ? 315  ILE A CB    1 
ATOM   2357 C  CG1   . ILE A 1 323 ? 13.595  3.047   50.102  1 15.271  ? 315  ILE A CG1   1 
ATOM   2358 C  CG2   . ILE A 1 323 ? 12.137  4.934   49.179  1 12.98   ? 315  ILE A CG2   1 
ATOM   2359 C  CD1   . ILE A 1 323 ? 12.988  1.809   49.466  1 15.358  ? 315  ILE A CD1   1 
ATOM   2360 N  N     . HIS A 1 324 ? 11.041  5.859   52.636  1 16.859  ? 316  HIS A N     1 
ATOM   2361 C  CA    . HIS A 1 324 ? 9.978   6.771   53.025  1 16.802  ? 316  HIS A CA    1 
ATOM   2362 C  C     . HIS A 1 324 ? 9.623   6.607   54.497  1 17.171  ? 316  HIS A C     1 
ATOM   2363 O  O     . HIS A 1 324 ? 9.529   5.476   54.981  1 18.47   ? 316  HIS A O     1 
ATOM   2364 C  CB    . HIS A 1 324 ? 8.74    6.55    52.146  1 17.782  ? 316  HIS A CB    1 
ATOM   2365 C  CG    . HIS A 1 324 ? 8.901   7.011   50.746  1 17.395  ? 316  HIS A CG    1 
ATOM   2366 N  ND1   . HIS A 1 324 ? 8.859   6.144   49.681  1 17.09   ? 316  HIS A ND1   1 
ATOM   2367 C  CD2   . HIS A 1 324 ? 9.035   8.245   50.239  1 16.347  ? 316  HIS A CD2   1 
ATOM   2368 C  CE1   . HIS A 1 324 ? 9       6.825   48.568  1 16.445  ? 316  HIS A CE1   1 
ATOM   2369 N  NE2   . HIS A 1 324 ? 9.13    8.096   48.895  1 16.76   ? 316  HIS A NE2   1 
ATOM   2370 N  N     . THR A 1 325 ? 9.369   7.756   55.146  1 17.056  ? 317  THR A N     1 
ATOM   2371 C  CA    . THR A 1 325 ? 8.767   7.856   56.474  1 17.804  ? 317  THR A CA    1 
ATOM   2372 C  C     . THR A 1 325 ? 7.249   7.665   56.372  1 17.541  ? 317  THR A C     1 
ATOM   2373 O  O     . THR A 1 325 ? 6.627   8.121   55.402  1 18.003  ? 317  THR A O     1 
ATOM   2374 C  CB    . THR A 1 325 ? 9.114   9.179   57.176  1 18.173  ? 317  THR A CB    1 
ATOM   2375 O  OG1   . THR A 1 325 ? 8.615   10.256  56.382  1 18.481  ? 317  THR A OG1   1 
ATOM   2376 C  CG2   . THR A 1 325 ? 10.6    9.399   57.406  1 16.878  ? 317  THR A CG2   1 
ATOM   2377 N  N     . ALA A 1 326 ? 6.665   7.019   57.4    1 16.709  ? 318  ALA A N     1 
ATOM   2378 C  CA    . ALA A 1 326 ? 5.233   7.097   57.673  1 16.48   ? 318  ALA A CA    1 
ATOM   2379 C  C     . ALA A 1 326 ? 4.948   8.516   58.173  1 16.031  ? 318  ALA A C     1 
ATOM   2380 O  O     . ALA A 1 326 ? 4.499   9.374   57.405  1 17.069  ? 318  ALA A O     1 
ATOM   2381 C  CB    . ALA A 1 326 ? 4.824   5.994   58.637  1 15.814  ? 318  ALA A CB    1 
ATOM   2382 N  N     . SER A 1 327 ? 5.323   8.772   59.429  1 16.003  ? 319  SER A N     1 
ATOM   2383 C  CA    . SER A 1 327 ? 5.477   10.099  60.007  1 16.235  ? 319  SER A CA    1 
ATOM   2384 C  C     . SER A 1 327 ? 6.381   10.011  61.237  1 16.451  ? 319  SER A C     1 
ATOM   2385 O  O     . SER A 1 327 ? 6.988   8.962   61.489  1 15.174  ? 319  SER A O     1 
ATOM   2386 C  CB    . SER A 1 327 ? 4.121   10.753  60.303  1 16.346  ? 319  SER A CB    1 
ATOM   2387 O  OG    . SER A 1 327 ? 4.258   12.169  60.35   1 15.79   ? 319  SER A OG    1 
ATOM   2388 N  N     . GLY A 1 328 ? 6.459   11.134  61.97   1 16.799  ? 320  GLY A N     1 
ATOM   2389 C  CA    . GLY A 1 328 ? 7.202   11.291  63.202  1 17.449  ? 320  GLY A CA    1 
ATOM   2390 C  C     . GLY A 1 328 ? 6.343   11.885  64.315  1 19.368  ? 320  GLY A C     1 
ATOM   2391 O  O     . GLY A 1 328 ? 5.268   12.462  64.055  1 18.962  ? 320  GLY A O     1 
ATOM   2392 N  N     . PHE A 1 329 ? 6.85    11.729  65.554  1 19.661  ? 321  PHE A N     1 
ATOM   2393 C  CA    . PHE A 1 329 ? 6.301   12.385  66.744  1 19.756  ? 321  PHE A CA    1 
ATOM   2394 C  C     . PHE A 1 329 ? 7.357   12.505  67.846  1 19.812  ? 321  PHE A C     1 
ATOM   2395 O  O     . PHE A 1 329 ? 8.453   11.948  67.731  1 20.135  ? 321  PHE A O     1 
ATOM   2396 C  CB    . PHE A 1 329 ? 4.978   11.751  67.197  1 18.482  ? 321  PHE A CB    1 
ATOM   2397 C  CG    . PHE A 1 329 ? 5.022   10.364  67.816  1 17.857  ? 321  PHE A CG    1 
ATOM   2398 C  CD1   . PHE A 1 329 ? 4.975   9.213   67.012  1 18.513  ? 321  PHE A CD1   1 
ATOM   2399 C  CD2   . PHE A 1 329 ? 5.039   10.211  69.211  1 17.117  ? 321  PHE A CD2   1 
ATOM   2400 C  CE1   . PHE A 1 329 ? 5.003   7.936   67.599  1 16.528  ? 321  PHE A CE1   1 
ATOM   2401 C  CE2   . PHE A 1 329 ? 5.076   8.935   69.794  1 17.179  ? 321  PHE A CE2   1 
ATOM   2402 C  CZ    . PHE A 1 329 ? 5.064   7.805   68.982  1 16.332  ? 321  PHE A CZ    1 
ATOM   2403 N  N     . GLU A 1 330 ? 6.987   13.244  68.904  1 17.276  ? 322  GLU A N     1 
ATOM   2404 C  CA    . GLU A 1 330 ? 7.71    13.261  70.171  1 17.789  ? 322  GLU A CA    1 
ATOM   2405 C  C     . GLU A 1 330 ? 6.886   12.509  71.219  1 18.157  ? 322  GLU A C     1 
ATOM   2406 O  O     . GLU A 1 330 ? 5.728   12.859  71.478  1 18.121  ? 322  GLU A O     1 
ATOM   2407 C  CB    . GLU A 1 330 ? 8.19    14.658  70.565  1 17.903  ? 322  GLU A CB    1 
ATOM   2408 C  CG    . GLU A 1 330 ? 9.255   15.249  69.627  1 17.45   ? 322  GLU A CG    1 
ATOM   2409 C  CD    . GLU A 1 330 ? 9.284   16.774  69.603  1 17.927  ? 322  GLU A CD    1 
ATOM   2410 O  OE1   . GLU A 1 330 ? 9.554   17.356  70.666  1 20.858  ? 322  GLU A OE1   1 
ATOM   2411 O  OE2   . GLU A 1 330 ? 9.028   17.414  68.558  1 17.87   ? 322  GLU A OE2   1 
ATOM   2412 N  N     . ASP A 1 331 ? 7.515   11.489  71.829  1 17.167  ? 323  ASP A N     1 
ATOM   2413 C  CA    . ASP A 1 331 ? 6.929   10.701  72.912  1 18.715  ? 323  ASP A CA    1 
ATOM   2414 C  C     . ASP A 1 331 ? 6.896   11.525  74.215  1 21.08   ? 323  ASP A C     1 
ATOM   2415 O  O     . ASP A 1 331 ? 7.434   12.636  74.284  1 20.564  ? 323  ASP A O     1 
ATOM   2416 C  CB    . ASP A 1 331 ? 7.587   9.32    72.965  1 19.841  ? 323  ASP A CB    1 
ATOM   2417 C  CG    . ASP A 1 331 ? 9.02    9.194   73.504  1 21.163  ? 323  ASP A CG    1 
ATOM   2418 O  OD1   . ASP A 1 331 ? 9.566   10.13   74.126  1 19.654  ? 323  ASP A OD1   1 
ATOM   2419 O  OD2   . ASP A 1 331 ? 9.636   8.153   73.258  1 25.77   ? 323  ASP A OD2   1 
ATOM   2420 N  N     . GLU A 1 332 ? 6.311   10.938  75.266  1 23.17   ? 324  GLU A N     1 
ATOM   2421 C  CA    . GLU A 1 332 ? 6.261   11.411  76.649  1 30.991  ? 324  GLU A CA    1 
ATOM   2422 C  C     . GLU A 1 332 ? 7.646   11.74   77.233  1 31.285  ? 324  GLU A C     1 
ATOM   2423 O  O     . GLU A 1 332 ? 7.721   12.647  78.056  1 32.896  ? 324  GLU A O     1 
ATOM   2424 C  CB    . GLU A 1 332 ? 5.362   10.532  77.533  1 40.738  ? 324  GLU A CB    1 
ATOM   2425 C  CG    . GLU A 1 332 ? 5.805   9.076   77.754  1 53.436  ? 324  GLU A CG    1 
ATOM   2426 C  CD    . GLU A 1 332 ? 6.042   8.108   76.585  1 63.767  ? 324  GLU A CD    1 
ATOM   2427 O  OE1   . GLU A 1 332 ? 5.199   8.08    75.654  1 64.451  ? 324  GLU A OE1   1 
ATOM   2428 O  OE2   . GLU A 1 332 ? 7.08    7.396   76.576  1 65.522  ? 324  GLU A OE2   1 
ATOM   2429 N  N     . GLN A 1 333 ? 8.722   11.056  76.784  1 31.368  ? 325  GLN A N     1 
ATOM   2430 C  CA    . GLN A 1 333 ? 10.108  11.265  77.216  1 35.036  ? 325  GLN A CA    1 
ATOM   2431 C  C     . GLN A 1 333 ? 10.84   12.341  76.389  1 36.612  ? 325  GLN A C     1 
ATOM   2432 O  O     . GLN A 1 333 ? 12.026  12.602  76.635  1 38.563  ? 325  GLN A O     1 
ATOM   2433 C  CB    . GLN A 1 333 ? 10.765  9.882   77.228  1 38.185  ? 325  GLN A CB    1 
ATOM   2434 C  CG    . GLN A 1 333 ? 11.921  9.756   78.211  1 48.36   ? 325  GLN A CG    1 
ATOM   2435 C  CD    . GLN A 1 333 ? 12.866  8.595   77.989  1 46.05   ? 325  GLN A CD    1 
ATOM   2436 O  OE1   . GLN A 1 333 ? 13.998  8.791   77.527  1 42.381  ? 325  GLN A OE1   1 
ATOM   2437 N  NE2   . GLN A 1 333 ? 12.433  7.393   78.363  1 49.735  ? 325  GLN A NE2   1 
ATOM   2438 N  N     . GLY A 1 334 ? 10.129  12.959  75.42   1 35.794  ? 326  GLY A N     1 
ATOM   2439 C  CA    . GLY A 1 334 ? 10.596  13.995  74.501  1 30.795  ? 326  GLY A CA    1 
ATOM   2440 C  C     . GLY A 1 334 ? 11.463  13.477  73.347  1 29.193  ? 326  GLY A C     1 
ATOM   2441 O  O     . GLY A 1 334 ? 12.09   14.281  72.652  1 29.826  ? 326  GLY A O     1 
ATOM   2442 N  N     . ARG A 1 335 ? 11.472  12.153  73.136  1 25.716  ? 327  ARG A N     1 
ATOM   2443 C  CA    . ARG A 1 335 ? 12.271  11.477  72.119  1 23.222  ? 327  ARG A CA    1 
ATOM   2444 C  C     . ARG A 1 335 ? 11.515  11.512  70.792  1 23.622  ? 327  ARG A C     1 
ATOM   2445 O  O     . ARG A 1 335 ? 10.286  11.394  70.789  1 22.391  ? 327  ARG A O     1 
ATOM   2446 C  CB    . ARG A 1 335 ? 12.524  10.018  72.509  1 23.574  ? 327  ARG A CB    1 
ATOM   2447 C  CG    . ARG A 1 335 ? 13.234  9.795   73.84   1 23.794  ? 327  ARG A CG    1 
ATOM   2448 C  CD    . ARG A 1 335 ? 13.501  8.333   74.132  1 25.399  ? 327  ARG A CD    1 
ATOM   2449 N  NE    . ARG A 1 335 ? 12.294  7.56    74.456  1 29.151  ? 327  ARG A NE    1 
ATOM   2450 C  CZ    . ARG A 1 335 ? 12.157  6.315   74.921  1 35.004  ? 327  ARG A CZ    1 
ATOM   2451 N  NH1   . ARG A 1 335 ? 13.182  5.538   75.259  1 33.057  ? 327  ARG A NH1   1 
ATOM   2452 N  NH2   . ARG A 1 335 ? 10.932  5.86    75.075  1 31.903  ? 327  ARG A NH2   1 
ATOM   2453 N  N     . ILE A 1 336 ? 12.269  11.674  69.683  1 22.286  ? 328  ILE A N     1 
ATOM   2454 C  CA    . ILE A 1 336 ? 11.783  11.639  68.3    1 18.536  ? 328  ILE A CA    1 
ATOM   2455 C  C     . ILE A 1 336 ? 11.602  10.164  67.898  1 20.492  ? 328  ILE A C     1 
ATOM   2456 O  O     . ILE A 1 336 ? 12.545  9.366   67.97   1 20.066  ? 328  ILE A O     1 
ATOM   2457 C  CB    . ILE A 1 336 ? 12.664  12.471  67.33   1 16.784  ? 328  ILE A CB    1 
ATOM   2458 C  CG1   . ILE A 1 336 ? 12.783  13.962  67.751  1 15.851  ? 328  ILE A CG1   1 
ATOM   2459 C  CG2   . ILE A 1 336 ? 12.196  12.35   65.869  1 17.671  ? 328  ILE A CG2   1 
ATOM   2460 C  CD1   . ILE A 1 336 ? 14.027  14.676  67.245  1 15.069  ? 328  ILE A CD1   1 
ATOM   2461 N  N     . ILE A 1 337 ? 10.359  9.834   67.49   1 19.595  ? 329  ILE A N     1 
ATOM   2462 C  CA    . ILE A 1 337 ? 9.931   8.519   67.027  1 17.625  ? 329  ILE A CA    1 
ATOM   2463 C  C     . ILE A 1 337 ? 9.511   8.672   65.563  1 18.231  ? 329  ILE A C     1 
ATOM   2464 O  O     . ILE A 1 337 ? 8.629   9.467   65.272  1 18.978  ? 329  ILE A O     1 
ATOM   2465 C  CB    . ILE A 1 337 ? 8.821   7.908   67.923  1 17.57   ? 329  ILE A CB    1 
ATOM   2466 C  CG1   . ILE A 1 337 ? 9.08    7.964   69.479  1 16.879  ? 329  ILE A CG1   1 
ATOM   2467 C  CG2   . ILE A 1 337 ? 8.401   6.507   67.44   1 15.594  ? 329  ILE A CG2   1 
ATOM   2468 C  CD1   . ILE A 1 337 ? 10.328  7.241   69.997  1 16.467  ? 329  ILE A CD1   1 
ATOM   2469 N  N     . ILE A 1 338 ? 10.181  7.922   64.666  1 18.451  ? 330  ILE A N     1 
ATOM   2470 C  CA    . ILE A 1 338 ? 9.979   7.912   63.219  1 17.411  ? 330  ILE A CA    1 
ATOM   2471 C  C     . ILE A 1 338 ? 9.865   6.448   62.785  1 18.178  ? 330  ILE A C     1 
ATOM   2472 O  O     . ILE A 1 338 ? 10.778  5.656   63.041  1 18.17   ? 330  ILE A O     1 
ATOM   2473 C  CB    . ILE A 1 338 ? 11.103  8.673   62.463  1 16.208  ? 330  ILE A CB    1 
ATOM   2474 C  CG1   . ILE A 1 338 ? 11.273  10.15   62.898  1 15.292  ? 330  ILE A CG1   1 
ATOM   2475 C  CG2   . ILE A 1 338 ? 10.936  8.553   60.938  1 15.853  ? 330  ILE A CG2   1 
ATOM   2476 C  CD1   . ILE A 1 338 ? 12.63   10.771  62.594  1 14.821  ? 330  ILE A CD1   1 
ATOM   2477 N  N     . ASP A 1 339 ? 8.764   6.12    62.084  1 17.76   ? 331  ASP A N     1 
ATOM   2478 C  CA    . ASP A 1 339 ? 8.645   4.881   61.324  1 17.544  ? 331  ASP A CA    1 
ATOM   2479 C  C     . ASP A 1 339 ? 8.96    5.103   59.859  1 18.323  ? 331  ASP A C     1 
ATOM   2480 O  O     . ASP A 1 339 ? 8.564   6.121   59.291  1 20.274  ? 331  ASP A O     1 
ATOM   2481 C  CB    . ASP A 1 339 ? 7.304   4.188   61.478  1 19.731  ? 331  ASP A CB    1 
ATOM   2482 C  CG    . ASP A 1 339 ? 6.949   3.645   62.856  1 21.43   ? 331  ASP A CG    1 
ATOM   2483 O  OD1   . ASP A 1 339 ? 7.634   3.994   63.841  1 19.58   ? 331  ASP A OD1   1 
ATOM   2484 O  OD2   . ASP A 1 339 ? 5.945   2.906   62.935  1 22.471  ? 331  ASP A OD2   1 
ATOM   2485 N  N     . SER A 1 340 ? 9.676   4.131   59.279  1 17.686  ? 332  SER A N     1 
ATOM   2486 C  CA    . SER A 1 340 ? 10.074  4.148   57.879  1 17.531  ? 332  SER A CA    1 
ATOM   2487 C  C     . SER A 1 340 ? 10.136  2.733   57.309  1 17.863  ? 332  SER A C     1 
ATOM   2488 O  O     . SER A 1 340 ? 10.233  1.756   58.071  1 19.905  ? 332  SER A O     1 
ATOM   2489 C  CB    . SER A 1 340 ? 11.357  4.941   57.659  1 17.657  ? 332  SER A CB    1 
ATOM   2490 O  OG    . SER A 1 340 ? 12.525  4.199   57.991  1 19.46   ? 332  SER A OG    1 
ATOM   2491 N  N     . SER A 1 341 ? 10.103  2.63    55.964  1 17.396  ? 333  SER A N     1 
ATOM   2492 C  CA    . SER A 1 341 ? 10.65   1.455   55.275  1 19.198  ? 333  SER A CA    1 
ATOM   2493 C  C     . SER A 1 341 ? 12.155  1.371   55.538  1 19.442  ? 333  SER A C     1 
ATOM   2494 O  O     . SER A 1 341 ? 12.783  2.397   55.83   1 18.69   ? 333  SER A O     1 
ATOM   2495 C  CB    . SER A 1 341 ? 10.334  1.427   53.797  1 18.874  ? 333  SER A CB    1 
ATOM   2496 O  OG    . SER A 1 341 ? 10.88   2.547   53.11   1 20.395  ? 333  SER A OG    1 
ATOM   2497 N  N     . LEU A 1 342 ? 12.693  0.138   55.515  1 18.716  ? 334  LEU A N     1 
ATOM   2498 C  CA    . LEU A 1 342 ? 14.125  -0.107  55.578  1 17.926  ? 334  LEU A CA    1 
ATOM   2499 C  C     . LEU A 1 342 ? 14.498  -1.259  54.656  1 18.68   ? 334  LEU A C     1 
ATOM   2500 O  O     . LEU A 1 342 ? 14.095  -2.405  54.895  1 19.034  ? 334  LEU A O     1 
ATOM   2501 C  CB    . LEU A 1 342 ? 14.653  -0.308  57.003  1 16.639  ? 334  LEU A CB    1 
ATOM   2502 C  CG    . LEU A 1 342 ? 16.166  -0.515  57.174  1 16.376  ? 334  LEU A CG    1 
ATOM   2503 C  CD1   . LEU A 1 342 ? 17.039  0.622   56.68   1 16.852  ? 334  LEU A CD1   1 
ATOM   2504 C  CD2   . LEU A 1 342 ? 16.458  -0.806  58.622  1 16.534  ? 334  LEU A CD2   1 
ATOM   2505 N  N     . VAL A 1 343 ? 15.291  -0.899  53.641  1 18.825  ? 335  VAL A N     1 
ATOM   2506 C  CA    . VAL A 1 343 ? 15.964  -1.827  52.744  1 19.488  ? 335  VAL A CA    1 
ATOM   2507 C  C     . VAL A 1 343 ? 17.427  -1.89   53.2    1 18.727  ? 335  VAL A C     1 
ATOM   2508 O  O     . VAL A 1 343 ? 18.072  -0.85   53.308  1 16.226  ? 335  VAL A O     1 
ATOM   2509 C  CB    . VAL A 1 343 ? 15.778  -1.506  51.242  1 20.469  ? 335  VAL A CB    1 
ATOM   2510 C  CG1   . VAL A 1 343 ? 16.414  -2.55   50.323  1 23.292  ? 335  VAL A CG1   1 
ATOM   2511 C  CG2   . VAL A 1 343 ? 14.313  -1.388  50.849  1 19.962  ? 335  VAL A CG2   1 
ATOM   2512 N  N     . HIS A 1 344 ? 17.931  -3.12   53.43   1 18.417  ? 336  HIS A N     1 
ATOM   2513 C  CA    . HIS A 1 344 ? 19.283  -3.398  53.934  1 18.467  ? 336  HIS A CA    1 
ATOM   2514 C  C     . HIS A 1 344 ? 20.294  -3.422  52.782  1 19.318  ? 336  HIS A C     1 
ATOM   2515 O  O     . HIS A 1 344 ? 21.039  -4.391  52.625  1 20.358  ? 336  HIS A O     1 
ATOM   2516 C  CB    . HIS A 1 344 ? 19.278  -4.651  54.831  1 18.933  ? 336  HIS A CB    1 
ATOM   2517 C  CG    . HIS A 1 344 ? 18.419  -4.525  56.046  1 19.811  ? 336  HIS A CG    1 
ATOM   2518 N  ND1   . HIS A 1 344 ? 18.95   -4.384  57.304  1 21.236  ? 336  HIS A ND1   1 
ATOM   2519 C  CD2   . HIS A 1 344 ? 17.083  -4.523  56.2    1 20.633  ? 336  HIS A CD2   1 
ATOM   2520 C  CE1   . HIS A 1 344 ? 17.965  -4.271  58.186  1 23.222  ? 336  HIS A CE1   1 
ATOM   2521 N  NE2   . HIS A 1 344 ? 16.814  -4.361  57.535  1 23.779  ? 336  HIS A NE2   1 
ATOM   2522 N  N     . GLY A 1 345 ? 20.32   -2.346  51.98   1 18.459  ? 337  GLY A N     1 
ATOM   2523 C  CA    . GLY A 1 345 ? 21.132  -2.189  50.783  1 17.875  ? 337  GLY A CA    1 
ATOM   2524 C  C     . GLY A 1 345 ? 20.435  -1.248  49.798  1 19.296  ? 337  GLY A C     1 
ATOM   2525 O  O     . GLY A 1 345 ? 19.524  -0.524  50.185  1 21.577  ? 337  GLY A O     1 
ATOM   2526 N  N     . ASN A 1 346 ? 20.865  -1.293  48.529  1 18.105  ? 338  ASN A N     1 
ATOM   2527 C  CA    . ASN A 1 346 ? 20.49   -0.324  47.513  1 17.963  ? 338  ASN A CA    1 
ATOM   2528 C  C     . ASN A 1 346 ? 19.174  -0.735  46.85   1 18.537  ? 338  ASN A C     1 
ATOM   2529 O  O     . ASN A 1 346 ? 19.152  -1.683  46.071  1 19.992  ? 338  ASN A O     1 
ATOM   2530 C  CB    . ASN A 1 346 ? 21.641  -0.101  46.536  1 17.827  ? 338  ASN A CB    1 
ATOM   2531 C  CG    . ASN A 1 346 ? 21.424  1.065   45.591  1 17.811  ? 338  ASN A CG    1 
ATOM   2532 O  OD1   . ASN A 1 346 ? 20.446  1.808   45.695  1 18.42   ? 338  ASN A OD1   1 
ATOM   2533 N  ND2   . ASN A 1 346 ? 22.357  1.287   44.69   1 15.354  ? 338  ASN A ND2   1 
ATOM   2534 N  N     . ALA A 1 347 ? 18.098  0.025   47.136  1 18.409  ? 339  ALA A N     1 
ATOM   2535 C  CA    . ALA A 1 347 ? 16.799  -0.111  46.483  1 19.229  ? 339  ALA A CA    1 
ATOM   2536 C  C     . ALA A 1 347 ? 16.737  0.561   45.103  1 18.514  ? 339  ALA A C     1 
ATOM   2537 O  O     . ALA A 1 347 ? 15.79   0.292   44.349  1 18.996  ? 339  ALA A O     1 
ATOM   2538 C  CB    . ALA A 1 347 ? 15.705  0.353   47.412  1 18.423  ? 339  ALA A CB    1 
ATOM   2539 N  N     . PHE A 1 348 ? 17.763  1.373   44.758  1 17.387  ? 340  PHE A N     1 
ATOM   2540 C  CA    . PHE A 1 348 ? 17.988  1.962   43.438  1 17.433  ? 340  PHE A CA    1 
ATOM   2541 C  C     . PHE A 1 348 ? 19.27   1.382   42.806  1 19.092  ? 340  PHE A C     1 
ATOM   2542 O  O     . PHE A 1 348 ? 20.216  2.161   42.624  1 18.669  ? 340  PHE A O     1 
ATOM   2543 C  CB    . PHE A 1 348 ? 18.015  3.486   43.654  1 17.861  ? 340  PHE A CB    1 
ATOM   2544 C  CG    . PHE A 1 348 ? 16.753  4.328   43.788  1 16.769  ? 340  PHE A CG    1 
ATOM   2545 C  CD1   . PHE A 1 348 ? 15.469  3.76    43.906  1 16.909  ? 340  PHE A CD1   1 
ATOM   2546 C  CD2   . PHE A 1 348 ? 16.877  5.727   43.834  1 17.254  ? 340  PHE A CD2   1 
ATOM   2547 C  CE1   . PHE A 1 348 ? 14.327  4.579   44.003  1 18.988  ? 340  PHE A CE1   1 
ATOM   2548 C  CE2   . PHE A 1 348 ? 15.748  6.548   43.967  1 16.774  ? 340  PHE A CE2   1 
ATOM   2549 C  CZ    . PHE A 1 348 ? 14.472  5.974   44.048  1 18.184  ? 340  PHE A CZ    1 
ATOM   2550 N  N     . PRO A 1 349 ? 19.375  0.06    42.418  1 20.141  ? 341  PRO A N     1 
ATOM   2551 C  CA    . PRO A 1 349 ? 20.617  -0.502  41.854  1 19.396  ? 341  PRO A CA    1 
ATOM   2552 C  C     . PRO A 1 349 ? 21.128  0.14    40.548  1 19.613  ? 341  PRO A C     1 
ATOM   2553 O  O     . PRO A 1 349 ? 22.326  0.062   40.255  1 21.915  ? 341  PRO A O     1 
ATOM   2554 C  CB    . PRO A 1 349 ? 20.346  -2.018  41.816  1 19.708  ? 341  PRO A CB    1 
ATOM   2555 C  CG    . PRO A 1 349 ? 18.856  -2.082  41.553  1 19.253  ? 341  PRO A CG    1 
ATOM   2556 C  CD    . PRO A 1 349 ? 18.31   -0.977  42.426  1 19.423  ? 341  PRO A CD    1 
ATOM   2557 N  N     . PHE A 1 350 ? 20.241  0.852   39.826  1 18.923  ? 342  PHE A N     1 
ATOM   2558 C  CA    . PHE A 1 350 ? 20.523  1.686   38.656  1 18.338  ? 342  PHE A CA    1 
ATOM   2559 C  C     . PHE A 1 350 ? 21.419  2.898   38.98   1 18.66   ? 342  PHE A C     1 
ATOM   2560 O  O     . PHE A 1 350 ? 21.943  3.503   38.042  1 18.686  ? 342  PHE A O     1 
ATOM   2561 C  CB    . PHE A 1 350 ? 19.225  2.027   37.891  1 16.986  ? 342  PHE A CB    1 
ATOM   2562 C  CG    . PHE A 1 350 ? 18.124  2.616   38.763  1 17.523  ? 342  PHE A CG    1 
ATOM   2563 C  CD1   . PHE A 1 350 ? 18.126  3.987   39.104  1 16.709  ? 342  PHE A CD1   1 
ATOM   2564 C  CD2   . PHE A 1 350 ? 17.115  1.789   39.289  1 17.45   ? 342  PHE A CD2   1 
ATOM   2565 C  CE1   . PHE A 1 350 ? 17.15   4.513   39.952  1 17      ? 342  PHE A CE1   1 
ATOM   2566 C  CE2   . PHE A 1 350 ? 16.136  2.318   40.14   1 16.988  ? 342  PHE A CE2   1 
ATOM   2567 C  CZ    . PHE A 1 350 ? 16.144  3.683   40.445  1 16.569  ? 342  PHE A CZ    1 
ATOM   2568 N  N     . PHE A 1 351 ? 21.596  3.262   40.275  1 18.692  ? 343  PHE A N     1 
ATOM   2569 C  CA    . PHE A 1 351 ? 22.641  4.183   40.728  1 17.831  ? 343  PHE A CA    1 
ATOM   2570 C  C     . PHE A 1 351 ? 23.7    3.408   41.518  1 18.939  ? 343  PHE A C     1 
ATOM   2571 O  O     . PHE A 1 351 ? 23.74   3.573   42.747  1 17.348  ? 343  PHE A O     1 
ATOM   2572 C  CB    . PHE A 1 351 ? 22.088  5.45    41.391  1 16.905  ? 343  PHE A CB    1 
ATOM   2573 C  CG    . PHE A 1 351 ? 21.03   6.252   40.642  1 17.303  ? 343  PHE A CG    1 
ATOM   2574 C  CD1   . PHE A 1 351 ? 21.08   6.437   39.245  1 15.897  ? 343  PHE A CD1   1 
ATOM   2575 C  CD2   . PHE A 1 351 ? 19.986  6.849   41.37   1 17.25   ? 343  PHE A CD2   1 
ATOM   2576 C  CE1   . PHE A 1 351 ? 20.107  7.196   38.586  1 16.859  ? 343  PHE A CE1   1 
ATOM   2577 C  CE2   . PHE A 1 351 ? 19.002  7.598   40.709  1 16.223  ? 343  PHE A CE2   1 
ATOM   2578 C  CZ    . PHE A 1 351 ? 19.058  7.749   39.324  1 16.696  ? 343  PHE A CZ    1 
ATOM   2579 N  N     . PRO A 1 352 ? 24.602  2.597   40.864  1 20.433  ? 344  PRO A N     1 
ATOM   2580 C  CA    . PRO A 1 352 ? 25.555  1.745   41.579  1 18.836  ? 344  PRO A CA    1 
ATOM   2581 C  C     . PRO A 1 352 ? 26.642  2.521   42.331  1 19.07   ? 344  PRO A C     1 
ATOM   2582 O  O     . PRO A 1 352 ? 26.748  3.747   42.134  1 17.466  ? 344  PRO A O     1 
ATOM   2583 C  CB    . PRO A 1 352 ? 26.072  0.793   40.486  1 18.889  ? 344  PRO A CB    1 
ATOM   2584 C  CG    . PRO A 1 352 ? 26.082  1.676   39.273  1 18.26   ? 344  PRO A CG    1 
ATOM   2585 C  CD    . PRO A 1 352 ? 24.822  2.469   39.402  1 19.458  ? 344  PRO A CD    1 
ATOM   2586 N  N     . PRO A 1 353 ? 27.486  1.853   43.176  1 18.504  ? 345  PRO A N     1 
ATOM   2587 C  CA    . PRO A 1 353 ? 28.713  2.47    43.673  1 19.432  ? 345  PRO A CA    1 
ATOM   2588 C  C     . PRO A 1 353 ? 29.719  2.872   42.597  1 21.106  ? 345  PRO A C     1 
ATOM   2589 O  O     . PRO A 1 353 ? 29.697  2.309   41.489  1 22.326  ? 345  PRO A O     1 
ATOM   2590 C  CB    . PRO A 1 353 ? 29.266  1.435   44.648  1 18.537  ? 345  PRO A CB    1 
ATOM   2591 C  CG    . PRO A 1 353 ? 28.079  0.592   45.051  1 19.172  ? 345  PRO A CG    1 
ATOM   2592 C  CD    . PRO A 1 353 ? 27.301  0.503   43.771  1 18.818  ? 345  PRO A CD    1 
ATOM   2593 N  N     . ASP A 1 354 ? 30.569  3.853   42.958  1 22.178  ? 346  ASP A N     1 
ATOM   2594 C  CA    . ASP A 1 354 ? 31.743  4.285   42.208  1 25.947  ? 346  ASP A CA    1 
ATOM   2595 C  C     . ASP A 1 354 ? 32.762  3.158   42.05   1 24.96   ? 346  ASP A C     1 
ATOM   2596 O  O     . ASP A 1 354 ? 33.123  2.87    40.912  1 27.955  ? 346  ASP A O     1 
ATOM   2597 C  CB    . ASP A 1 354 ? 32.465  5.468   42.834  1 30.087  ? 346  ASP A CB    1 
ATOM   2598 C  CG    . ASP A 1 354 ? 32.292  6.836   42.2    1 35.98   ? 346  ASP A CG    1 
ATOM   2599 O  OD1   . ASP A 1 354 ? 32.495  6.99    40.977  1 35.875  ? 346  ASP A OD1   1 
ATOM   2600 O  OD2   . ASP A 1 354 ? 32.038  7.761   42.969  1 43.461  ? 346  ASP A OD2   1 
ATOM   2601 N  N     . SER A 1 355 ? 33.23   2.563   43.169  1 26.138  ? 347  SER A N     1 
ATOM   2602 C  CA    . SER A 1 355 ? 34.369  1.645   43.158  1 24.978  ? 347  SER A CA    1 
ATOM   2603 C  C     . SER A 1 355 ? 33.939  0.252   42.692  1 26.145  ? 347  SER A C     1 
ATOM   2604 O  O     . SER A 1 355 ? 32.777  -0.142  42.874  1 24.381  ? 347  SER A O     1 
ATOM   2605 C  CB    . SER A 1 355 ? 35.115  1.629   44.465  1 24.32   ? 347  SER A CB    1 
ATOM   2606 O  OG    . SER A 1 355 ? 34.406  0.974   45.507  1 24.904  ? 347  SER A OG    1 
ATOM   2607 N  N     . ASP A 1 356 ? 34.911  -0.47   42.109  1 25.752  ? 348  ASP A N     1 
ATOM   2608 C  CA    . ASP A 1 356 ? 34.769  -1.835  41.611  1 29.494  ? 348  ASP A CA    1 
ATOM   2609 C  C     . ASP A 1 356 ? 34.42   -2.796  42.741  1 27.455  ? 348  ASP A C     1 
ATOM   2610 O  O     . ASP A 1 356 ? 33.536  -3.645  42.548  1 26.722  ? 348  ASP A O     1 
ATOM   2611 C  CB    . ASP A 1 356 ? 35.987  -2.262  40.807  1 34.829  ? 348  ASP A CB    1 
ATOM   2612 C  CG    . ASP A 1 356 ? 36.246  -1.501  39.513  1 36.408  ? 348  ASP A CG    1 
ATOM   2613 O  OD1   . ASP A 1 356 ? 35.292  -0.954  38.921  1 37.643  ? 348  ASP A OD1   1 
ATOM   2614 O  OD2   . ASP A 1 356 ? 37.418  -1.451  39.101  1 46.603  ? 348  ASP A OD2   1 
ATOM   2615 N  N     . GLU A 1 357 ? 35.074  -2.583  43.903  1 24.57   ? 349  GLU A N     1 
ATOM   2616 C  CA    . GLU A 1 357 ? 34.892  -3.329  45.14   1 25.54   ? 349  GLU A CA    1 
ATOM   2617 C  C     . GLU A 1 357 ? 33.443  -3.221  45.64   1 21.225  ? 349  GLU A C     1 
ATOM   2618 O  O     . GLU A 1 357 ? 32.813  -4.246  45.924  1 19.122  ? 349  GLU A O     1 
ATOM   2619 C  CB    . GLU A 1 357 ? 35.937  -2.83   46.138  1 30.856  ? 349  GLU A CB    1 
ATOM   2620 C  CG    . GLU A 1 357 ? 36.174  -3.825  47.269  1 46.423  ? 349  GLU A CG    1 
ATOM   2621 C  CD    . GLU A 1 357 ? 36.107  -3.345  48.716  1 57.675  ? 349  GLU A CD    1 
ATOM   2622 O  OE1   . GLU A 1 357 ? 36.763  -2.331  49.059  1 59.068  ? 349  GLU A OE1   1 
ATOM   2623 O  OE2   . GLU A 1 357 ? 35.386  -4.01   49.508  1 60.53   ? 349  GLU A OE2   1 
ATOM   2624 N  N     . GLN A 1 358 ? 32.935  -1.973  45.71   1 19.661  ? 350  GLN A N     1 
ATOM   2625 C  CA    . GLN A 1 358 ? 31.602  -1.653  46.205  1 20.273  ? 350  GLN A CA    1 
ATOM   2626 C  C     . GLN A 1 358 ? 30.509  -2.133  45.242  1 20.491  ? 350  GLN A C     1 
ATOM   2627 O  O     . GLN A 1 358 ? 29.432  -2.532  45.705  1 20.765  ? 350  GLN A O     1 
ATOM   2628 C  CB    . GLN A 1 358 ? 31.556  -0.188  46.598  1 19.215  ? 350  GLN A CB    1 
ATOM   2629 C  CG    . GLN A 1 358 ? 31.99   0.111   48.027  1 19.399  ? 350  GLN A CG    1 
ATOM   2630 C  CD    . GLN A 1 358 ? 31.316  1.366   48.53   1 21.668  ? 350  GLN A CD    1 
ATOM   2631 O  OE1   . GLN A 1 358 ? 30.107  1.549   48.331  1 20.746  ? 350  GLN A OE1   1 
ATOM   2632 N  NE2   . GLN A 1 358 ? 32.091  2.262   49.13   1 20.367  ? 350  GLN A NE2   1 
ATOM   2633 N  N     . LYS A 1 359 ? 30.811  -2.109  43.925  1 20.044  ? 351  LYS A N     1 
ATOM   2634 C  CA    . LYS A 1 359 ? 29.962  -2.64   42.856  1 21.041  ? 351  LYS A CA    1 
ATOM   2635 C  C     . LYS A 1 359 ? 29.671  -4.13   43.067  1 21.299  ? 351  LYS A C     1 
ATOM   2636 O  O     . LYS A 1 359 ? 28.51   -4.555  42.961  1 19.077  ? 351  LYS A O     1 
ATOM   2637 C  CB    . LYS A 1 359 ? 30.504  -2.373  41.449  1 21.851  ? 351  LYS A CB    1 
ATOM   2638 C  CG    . LYS A 1 359 ? 30.16   -1.008  40.848  1 25.14   ? 351  LYS A CG    1 
ATOM   2639 C  CD    . LYS A 1 359 ? 30.725  -0.881  39.437  1 27.191  ? 351  LYS A CD    1 
ATOM   2640 C  CE    . LYS A 1 359 ? 30.406  0.389   38.711  1 29.345  ? 351  LYS A CE    1 
ATOM   2641 N  NZ    . LYS A 1 359 ? 31.267  1.508   39.094  1 30.381  ? 351  LYS A NZ    1 
ATOM   2642 N  N     . LYS A 1 360 ? 30.728  -4.888  43.433  1 19.9    ? 352  LYS A N     1 
ATOM   2643 C  CA    . LYS A 1 360 ? 30.671  -6.317  43.737  1 18.401  ? 352  LYS A CA    1 
ATOM   2644 C  C     . LYS A 1 360 ? 29.806  -6.591  44.974  1 18.936  ? 352  LYS A C     1 
ATOM   2645 O  O     . LYS A 1 360 ? 29.102  -7.596  44.991  1 17.996  ? 352  LYS A O     1 
ATOM   2646 C  CB    . LYS A 1 360 ? 32.071  -6.928  43.861  1 18.304  ? 352  LYS A CB    1 
ATOM   2647 C  CG    . LYS A 1 360 ? 32.921  -6.901  42.602  1 20.221  ? 352  LYS A CG    1 
ATOM   2648 C  CD    . LYS A 1 360 ? 34.256  -7.64   42.626  1 18.069  ? 352  LYS A CD    1 
ATOM   2649 C  CE    . LYS A 1 360 ? 35.166  -7.255  41.499  1 20.108  ? 352  LYS A CE    1 
ATOM   2650 N  NZ    . LYS A 1 360 ? 34.553  -7.219  40.165  1 21.21   ? 352  LYS A NZ    1 
ATOM   2651 N  N     . LYS A 1 361 ? 29.859  -5.698  45.979  1 19.495  ? 353  LYS A N     1 
ATOM   2652 C  CA    . LYS A 1 361 ? 29.013  -5.754  47.172  1 22.419  ? 353  LYS A CA    1 
ATOM   2653 C  C     . LYS A 1 361 ? 27.52   -5.671  46.809  1 21.063  ? 353  LYS A C     1 
ATOM   2654 O  O     . LYS A 1 361 ? 26.738  -6.447  47.37   1 20.52   ? 353  LYS A O     1 
ATOM   2655 C  CB    . LYS A 1 361 ? 29.49   -4.921  48.369  1 22.176  ? 353  LYS A CB    1 
ATOM   2656 C  CG    . LYS A 1 361 ? 28.834  -5.325  49.704  1 26.793  ? 353  LYS A CG    1 
ATOM   2657 C  CD    . LYS A 1 361 ? 29.13   -4.491  50.945  1 30.188  ? 353  LYS A CD    1 
ATOM   2658 C  CE    . LYS A 1 361 ? 28.194  -4.775  52.096  1 33.925  ? 353  LYS A CE    1 
ATOM   2659 N  NZ    . LYS A 1 361 ? 28.361  -6.051  52.8    1 33.883  ? 353  LYS A NZ    1 
ATOM   2660 N  N     . GLN A 1 362 ? 27.152  -4.767  45.876  1 19.739  ? 354  GLN A N     1 
ATOM   2661 C  CA    . GLN A 1 362 ? 25.774  -4.576  45.414  1 19.679  ? 354  GLN A CA    1 
ATOM   2662 C  C     . GLN A 1 362 ? 25.243  -5.852  44.75   1 20.526  ? 354  GLN A C     1 
ATOM   2663 O  O     . GLN A 1 362 ? 24.145  -6.305  45.091  1 20.325  ? 354  GLN A O     1 
ATOM   2664 C  CB    . GLN A 1 362 ? 25.604  -3.312  44.569  1 18.173  ? 354  GLN A CB    1 
ATOM   2665 C  CG    . GLN A 1 362 ? 24.16   -3.035  44.166  1 18.59   ? 354  GLN A CG    1 
ATOM   2666 C  CD    . GLN A 1 362 ? 24.013  -1.77   43.369  1 18.536  ? 354  GLN A CD    1 
ATOM   2667 O  OE1   . GLN A 1 362 ? 24.121  -0.664  43.904  1 20.402  ? 354  GLN A OE1   1 
ATOM   2668 N  NE2   . GLN A 1 362 ? 23.773  -1.936  42.08   1 17.07   ? 354  GLN A NE2   1 
ATOM   2669 N  N     . GLU A 1 363 ? 26.061  -6.426  43.857  1 20.637  ? 355  GLU A N     1 
ATOM   2670 C  CA    . GLU A 1 363 ? 25.816  -7.706  43.198  1 23.298  ? 355  GLU A CA    1 
ATOM   2671 C  C     . GLU A 1 363 ? 25.59   -8.828  44.211  1 24.378  ? 355  GLU A C     1 
ATOM   2672 O  O     . GLU A 1 363 ? 24.628  -9.575  44.044  1 25.487  ? 355  GLU A O     1 
ATOM   2673 C  CB    . GLU A 1 363 ? 26.925  -8.055  42.209  1 25.378  ? 355  GLU A CB    1 
ATOM   2674 C  CG    . GLU A 1 363 ? 27.013  -7.113  41.012  1 29.359  ? 355  GLU A CG    1 
ATOM   2675 C  CD    . GLU A 1 363 ? 27.779  -7.793  39.906  1 35.438  ? 355  GLU A CD    1 
ATOM   2676 O  OE1   . GLU A 1 363 ? 27.197  -8.694  39.244  1 41.46   ? 355  GLU A OE1   1 
ATOM   2677 O  OE2   . GLU A 1 363 ? 28.966  -7.425  39.747  1 35.79   ? 355  GLU A OE2   1 
ATOM   2678 N  N     . ALA A 1 364 ? 26.437  -8.886  45.26   1 21.72   ? 356  ALA A N     1 
ATOM   2679 C  CA    . ALA A 1 364 ? 26.393  -9.865  46.345  1 23.846  ? 356  ALA A CA    1 
ATOM   2680 C  C     . ALA A 1 364 ? 25.129  -9.757  47.197  1 25.242  ? 356  ALA A C     1 
ATOM   2681 O  O     . ALA A 1 364 ? 24.609  -10.794 47.623  1 22.498  ? 356  ALA A O     1 
ATOM   2682 C  CB    . ALA A 1 364 ? 27.622  -9.758  47.215  1 22.926  ? 356  ALA A CB    1 
ATOM   2683 N  N     . ASP A 1 365 ? 24.665  -8.504  47.405  1 26.355  ? 357  ASP A N     1 
ATOM   2684 C  CA    . ASP A 1 365 ? 23.496  -8.193  48.223  1 26.773  ? 357  ASP A CA    1 
ATOM   2685 C  C     . ASP A 1 365 ? 22.22   -8.707  47.576  1 26.49   ? 357  ASP A C     1 
ATOM   2686 O  O     . ASP A 1 365 ? 21.332  -9.1    48.319  1 31.618  ? 357  ASP A O     1 
ATOM   2687 C  CB    . ASP A 1 365 ? 23.466  -6.748  48.715  1 26.515  ? 357  ASP A CB    1 
ATOM   2688 C  CG    . ASP A 1 365 ? 24.413  -6.386  49.863  1 27.68   ? 357  ASP A CG    1 
ATOM   2689 O  OD1   . ASP A 1 365 ? 25.026  -7.295  50.471  1 25.498  ? 357  ASP A OD1   1 
ATOM   2690 O  OD2   . ASP A 1 365 ? 24.534  -5.182  50.162  1 31.499  ? 357  ASP A OD2   1 
ATOM   2691 N  N     . GLY A 1 366 ? 22.179  -8.736  46.227  1 27.738  ? 358  GLY A N     1 
ATOM   2692 C  CA    . GLY A 1 366 ? 21.038  -9.132  45.402  1 30.296  ? 358  GLY A CA    1 
ATOM   2693 C  C     . GLY A 1 366 ? 19.833  -8.241  45.694  1 29.424  ? 358  GLY A C     1 
ATOM   2694 O  O     . GLY A 1 366 ? 19.967  -7.023  45.748  1 32.956  ? 358  GLY A O     1 
ATOM   2695 N  N     . THR A 1 367 ? 18.689  -8.887  45.942  1 29.361  ? 359  THR A N     1 
ATOM   2696 C  CA    . THR A 1 367 ? 17.498  -8.274  46.514  1 25.509  ? 359  THR A CA    1 
ATOM   2697 C  C     . THR A 1 367 ? 17.734  -8.199  48.024  1 21.506  ? 359  THR A C     1 
ATOM   2698 O  O     . THR A 1 367 ? 17.69   -9.262  48.652  1 20.975  ? 359  THR A O     1 
ATOM   2699 C  CB    . THR A 1 367 ? 16.248  -9.099  46.182  1 26.184  ? 359  THR A CB    1 
ATOM   2700 O  OG1   . THR A 1 367 ? 16.234  -9.332  44.779  1 30.637  ? 359  THR A OG1   1 
ATOM   2701 C  CG2   . THR A 1 367 ? 14.968  -8.463  46.705  1 24.748  ? 359  THR A CG2   1 
ATOM   2702 N  N     . PRO A 1 368 ? 17.956  -7.002  48.657  1 20.863  ? 360  PRO A N     1 
ATOM   2703 C  CA    . PRO A 1 368 ? 18.215  -6.935  50.099  1 21.797  ? 360  PRO A CA    1 
ATOM   2704 C  C     . PRO A 1 368 ? 16.95   -7.212  50.906  1 21.732  ? 360  PRO A C     1 
ATOM   2705 O  O     . PRO A 1 368 ? 15.844  -7.139  50.354  1 20.712  ? 360  PRO A O     1 
ATOM   2706 C  CB    . PRO A 1 368 ? 18.789  -5.525  50.33   1 22.568  ? 360  PRO A CB    1 
ATOM   2707 C  CG    . PRO A 1 368 ? 18.988  -4.967  48.924  1 22.714  ? 360  PRO A CG    1 
ATOM   2708 C  CD    . PRO A 1 368 ? 17.936  -5.643  48.079  1 21.885  ? 360  PRO A CD    1 
ATOM   2709 N  N     . LYS A 1 369 ? 17.133  -7.558  52.193  1 22.374  ? 361  LYS A N     1 
ATOM   2710 C  CA    . LYS A 1 369 ? 16.08   -7.615  53.2    1 22.704  ? 361  LYS A CA    1 
ATOM   2711 C  C     . LYS A 1 369 ? 15.367  -6.26   53.277  1 21.555  ? 361  LYS A C     1 
ATOM   2712 O  O     . LYS A 1 369 ? 16.019  -5.205  53.203  1 19.658  ? 361  LYS A O     1 
ATOM   2713 C  CB    . LYS A 1 369 ? 16.753  -7.936  54.53   1 25.287  ? 361  LYS A CB    1 
ATOM   2714 C  CG    . LYS A 1 369 ? 15.875  -8.325  55.71   1 28.655  ? 361  LYS A CG    1 
ATOM   2715 C  CD    . LYS A 1 369 ? 16.848  -8.011  56.835  1 33.09   ? 361  LYS A CD    1 
ATOM   2716 C  CE    . LYS A 1 369 ? 16.929  -8.992  57.907  1 39.299  ? 361  LYS A CE    1 
ATOM   2717 N  NZ    . LYS A 1 369 ? 17.705  -10.173 57.526  1 38.083  ? 361  LYS A NZ    1 
ATOM   2718 N  N     . ALA A 1 370 ? 14.029  -6.329  53.353  1 20.529  ? 362  ALA A N     1 
ATOM   2719 C  CA    . ALA A 1 370 ? 13.147  -5.17   53.337  1 20.469  ? 362  ALA A CA    1 
ATOM   2720 C  C     . ALA A 1 370 ? 12.068  -5.313  54.409  1 20.141  ? 362  ALA A C     1 
ATOM   2721 O  O     . ALA A 1 370 ? 11.328  -6.306  54.432  1 19.665  ? 362  ALA A O     1 
ATOM   2722 C  CB    . ALA A 1 370 ? 12.603  -4.908  51.934  1 19      ? 362  ALA A CB    1 
ATOM   2723 N  N     . GLN A 1 371 ? 12.017  -4.297  55.297  1 18.667  ? 363  GLN A N     1 
ATOM   2724 C  CA    . GLN A 1 371 ? 11.191  -4.246  56.499  1 17.965  ? 363  GLN A CA    1 
ATOM   2725 C  C     . GLN A 1 371 ? 10.577  -2.854  56.666  1 18.447  ? 363  GLN A C     1 
ATOM   2726 O  O     . GLN A 1 371 ? 10.906  -1.934  55.916  1 18.052  ? 363  GLN A O     1 
ATOM   2727 C  CB    . GLN A 1 371 ? 12.023  -4.6    57.736  1 19.104  ? 363  GLN A CB    1 
ATOM   2728 C  CG    . GLN A 1 371 ? 12.594  -6.018  57.743  1 21.113  ? 363  GLN A CG    1 
ATOM   2729 C  CD    . GLN A 1 371 ? 13.694  -6.223  58.758  1 21.192  ? 363  GLN A CD    1 
ATOM   2730 O  OE1   . GLN A 1 371 ? 14.531  -5.346  59.011  1 23.197  ? 363  GLN A OE1   1 
ATOM   2731 N  NE2   . GLN A 1 371 ? 13.686  -7.408  59.343  1 21      ? 363  GLN A NE2   1 
ATOM   2732 N  N     . PHE A 1 372 ? 9.635   -2.759  57.628  1 19.517  ? 364  PHE A N     1 
ATOM   2733 C  CA    . PHE A 1 372 ? 9.101   -1.528  58.189  1 19.881  ? 364  PHE A CA    1 
ATOM   2734 C  C     . PHE A 1 372 ? 9.58    -1.439  59.633  1 19.928  ? 364  PHE A C     1 
ATOM   2735 O  O     . PHE A 1 372 ? 9.439   -2.415  60.378  1 21.027  ? 364  PHE A O     1 
ATOM   2736 C  CB    . PHE A 1 372 ? 7.578   -1.537  58.025  1 20.353  ? 364  PHE A CB    1 
ATOM   2737 C  CG    . PHE A 1 372 ? 6.897   -0.21   58.331  1 20.005  ? 364  PHE A CG    1 
ATOM   2738 C  CD1   . PHE A 1 372 ? 6.956   0.869   57.43   1 20.239  ? 364  PHE A CD1   1 
ATOM   2739 C  CD2   . PHE A 1 372 ? 6.158   -0.054  59.513  1 19.118  ? 364  PHE A CD2   1 
ATOM   2740 C  CE1   . PHE A 1 372 ? 6.307   2.084   57.717  1 19.626  ? 364  PHE A CE1   1 
ATOM   2741 C  CE2   . PHE A 1 372 ? 5.5     1.157   59.795  1 18.856  ? 364  PHE A CE2   1 
ATOM   2742 C  CZ    . PHE A 1 372 ? 5.573   2.219   58.902  1 18.82   ? 364  PHE A CZ    1 
ATOM   2743 N  N     . VAL A 1 373 ? 10.171  -0.278  59.99   1 19.081  ? 365  VAL A N     1 
ATOM   2744 C  CA    . VAL A 1 373 ? 11.026  -0.113  61.165  1 17.667  ? 365  VAL A CA    1 
ATOM   2745 C  C     . VAL A 1 373 ? 10.69   1.172   61.929  1 17.581  ? 365  VAL A C     1 
ATOM   2746 O  O     . VAL A 1 373 ? 10.16   2.108   61.329  1 18.375  ? 365  VAL A O     1 
ATOM   2747 C  CB    . VAL A 1 373 ? 12.55   -0.287  60.929  1 17.59   ? 365  VAL A CB    1 
ATOM   2748 C  CG1   . VAL A 1 373 ? 12.933  -1.637  60.307  1 16.146  ? 365  VAL A CG1   1 
ATOM   2749 C  CG2   . VAL A 1 373 ? 13.187  0.885   60.196  1 17.381  ? 365  VAL A CG2   1 
ATOM   2750 N  N     . ARG A 1 374 ? 11.054  1.206   63.227  1 17.474  ? 366  ARG A N     1 
ATOM   2751 C  CA    . ARG A 1 374 ? 10.866  2.329   64.144  1 19.402  ? 366  ARG A CA    1 
ATOM   2752 C  C     . ARG A 1 374 ? 12.215  2.801   64.692  1 19.984  ? 366  ARG A C     1 
ATOM   2753 O  O     . ARG A 1 374 ? 12.912  2.031   65.368  1 19.209  ? 366  ARG A O     1 
ATOM   2754 C  CB    . ARG A 1 374 ? 9.902   1.968   65.285  1 19.755  ? 366  ARG A CB    1 
ATOM   2755 C  CG    . ARG A 1 374 ? 9.69    3.076   66.317  1 19.421  ? 366  ARG A CG    1 
ATOM   2756 C  CD    . ARG A 1 374 ? 8.475   2.843   67.185  1 20.242  ? 366  ARG A CD    1 
ATOM   2757 N  NE    . ARG A 1 374 ? 7.24    2.75    66.394  1 20.255  ? 366  ARG A NE    1 
ATOM   2758 C  CZ    . ARG A 1 374 ? 6.241   1.871   66.514  1 20.094  ? 366  ARG A CZ    1 
ATOM   2759 N  NH1   . ARG A 1 374 ? 6.101   1.128   67.597  1 19.171  ? 366  ARG A NH1   1 
ATOM   2760 N  NH2   . ARG A 1 374 ? 5.319   1.8     65.567  1 18.758  ? 366  ARG A NH2   1 
ATOM   2761 N  N     . TRP A 1 375 ? 12.482  4.096   64.457  1 18.689  ? 367  TRP A N     1 
ATOM   2762 C  CA    . TRP A 1 375 ? 13.66   4.837   64.892  1 20.191  ? 367  TRP A CA    1 
ATOM   2763 C  C     . TRP A 1 375 ? 13.341  5.618   66.169  1 20.527  ? 367  TRP A C     1 
ATOM   2764 O  O     . TRP A 1 375 ? 12.224  6.135   66.314  1 20.513  ? 367  TRP A O     1 
ATOM   2765 C  CB    . TRP A 1 375 ? 14.146  5.786   63.78   1 20.145  ? 367  TRP A CB    1 
ATOM   2766 C  CG    . TRP A 1 375 ? 14.369  5.135   62.431  1 20.827  ? 367  TRP A CG    1 
ATOM   2767 C  CD1   . TRP A 1 375 ? 13.474  5.075   61.397  1 19.701  ? 367  TRP A CD1   1 
ATOM   2768 C  CD2   . TRP A 1 375 ? 15.566  4.47    61.96   1 21.248  ? 367  TRP A CD2   1 
ATOM   2769 N  NE1   . TRP A 1 375 ? 14.007  4.408   60.328  1 18.539  ? 367  TRP A NE1   1 
ATOM   2770 C  CE2   . TRP A 1 375 ? 15.293  4.037   60.631  1 20.735  ? 367  TRP A CE2   1 
ATOM   2771 C  CE3   . TRP A 1 375 ? 16.839  4.216   62.517  1 22.971  ? 367  TRP A CE3   1 
ATOM   2772 C  CZ2   . TRP A 1 375 ? 16.24   3.346   59.86   1 20.605  ? 367  TRP A CZ2   1 
ATOM   2773 C  CZ3   . TRP A 1 375 ? 17.779  3.549   61.748  1 23.098  ? 367  TRP A CZ3   1 
ATOM   2774 C  CH2   . TRP A 1 375 ? 17.476  3.116   60.44   1 22.446  ? 367  TRP A CH2   1 
ATOM   2775 N  N     . THR A 1 376 ? 14.335  5.678   67.072  1 19.291  ? 368  THR A N     1 
ATOM   2776 C  CA    . THR A 1 376 ? 14.335  6.516   68.269  1 20.431  ? 368  THR A CA    1 
ATOM   2777 C  C     . THR A 1 376 ? 15.554  7.435   68.217  1 18.887  ? 368  THR A C     1 
ATOM   2778 O  O     . THR A 1 376 ? 16.688  6.953   68.248  1 17.742  ? 368  THR A O     1 
ATOM   2779 C  CB    . THR A 1 376 ? 14.256  5.687   69.562  1 21.397  ? 368  THR A CB    1 
ATOM   2780 O  OG1   . THR A 1 376 ? 13.169  4.77    69.489  1 20.192  ? 368  THR A OG1   1 
ATOM   2781 C  CG2   . THR A 1 376 ? 14.082  6.534   70.818  1 22.323  ? 368  THR A CG2   1 
ATOM   2782 N  N     . ILE A 1 377 ? 15.273  8.746   68.135  1 19.466  ? 369  ILE A N     1 
ATOM   2783 C  CA    . ILE A 1 377 ? 16.272  9.808   68.215  1 21.483  ? 369  ILE A CA    1 
ATOM   2784 C  C     . ILE A 1 377 ? 15.954  10.641  69.458  1 22.953  ? 369  ILE A C     1 
ATOM   2785 O  O     . ILE A 1 377 ? 15.018  11.449  69.435  1 21.034  ? 369  ILE A O     1 
ATOM   2786 C  CB    . ILE A 1 377 ? 16.385  10.631  66.906  1 22.104  ? 369  ILE A CB    1 
ATOM   2787 C  CG1   . ILE A 1 377 ? 16.686  9.736   65.676  1 21.873  ? 369  ILE A CG1   1 
ATOM   2788 C  CG2   . ILE A 1 377 ? 17.432  11.755  67.048  1 25.783  ? 369  ILE A CG2   1 
ATOM   2789 C  CD1   . ILE A 1 377 ? 16.32   10.337  64.331  1 23.821  ? 369  ILE A CD1   1 
ATOM   2790 N  N     . ASP A 1 378 ? 16.743  10.429  70.533  1 20.534  ? 370  ASP A N     1 
ATOM   2791 C  CA    . ASP A 1 378 ? 16.64   11.255  71.732  1 21.824  ? 370  ASP A CA    1 
ATOM   2792 C  C     . ASP A 1 378 ? 17.484  12.518  71.555  1 23.447  ? 370  ASP A C     1 
ATOM   2793 O  O     . ASP A 1 378 ? 18.714  12.402  71.68   1 24.152  ? 370  ASP A O     1 
ATOM   2794 C  CB    . ASP A 1 378 ? 16.866  10.481  73.028  1 23.569  ? 370  ASP A CB    1 
ATOM   2795 C  CG    . ASP A 1 378 ? 16.695  11.219  74.36   1 24.287  ? 370  ASP A CG    1 
ATOM   2796 O  OD1   . ASP A 1 378 ? 16.722  12.474  74.421  1 21.953  ? 370  ASP A OD1   1 
ATOM   2797 O  OD2   . ASP A 1 378 ? 16.557  10.51   75.369  1 26.569  ? 370  ASP A OD2   1 
ATOM   2798 N  N     . PRO A 1 379 ? 16.874  13.74   71.386  1 23.111  ? 371  PRO A N     1 
ATOM   2799 C  CA    . PRO A 1 379 ? 17.631  14.964  71.095  1 26.128  ? 371  PRO A CA    1 
ATOM   2800 C  C     . PRO A 1 379 ? 18.584  15.461  72.191  1 27.384  ? 371  PRO A C     1 
ATOM   2801 O  O     . PRO A 1 379 ? 19.422  16.32   71.908  1 31.035  ? 371  PRO A O     1 
ATOM   2802 C  CB    . PRO A 1 379 ? 16.558  15.948  70.646  1 25.702  ? 371  PRO A CB    1 
ATOM   2803 C  CG    . PRO A 1 379 ? 15.342  15.511  71.451  1 25.036  ? 371  PRO A CG    1 
ATOM   2804 C  CD    . PRO A 1 379 ? 15.43   14.026  71.523  1 21.331  ? 371  PRO A CD    1 
ATOM   2805 N  N     . ARG A 1 380 ? 18.481  14.866  73.397  1 28.048  ? 372  ARG A N     1 
ATOM   2806 C  CA    . ARG A 1 380 ? 19.276  15.159  74.583  1 28.279  ? 372  ARG A CA    1 
ATOM   2807 C  C     . ARG A 1 380 ? 20.55   14.317  74.661  1 26.603  ? 372  ARG A C     1 
ATOM   2808 O  O     . ARG A 1 380 ? 21.467  14.689  75.404  1 26.353  ? 372  ARG A O     1 
ATOM   2809 C  CB    . ARG A 1 380 ? 18.424  15.019  75.849  1 32.912  ? 372  ARG A CB    1 
ATOM   2810 C  CG    . ARG A 1 380 ? 17.348  16.091  75.974  1 37.172  ? 372  ARG A CG    1 
ATOM   2811 C  CD    . ARG A 1 380 ? 16.764  16.145  77.37   1 39.811  ? 372  ARG A CD    1 
ATOM   2812 N  NE    . ARG A 1 380 ? 15.922  14.968  77.61   1 42.665  ? 372  ARG A NE    1 
ATOM   2813 C  CZ    . ARG A 1 380 ? 14.7    14.886  78.131  1 40.262  ? 372  ARG A CZ    1 
ATOM   2814 N  NH1   . ARG A 1 380 ? 14.079  15.936  78.649  1 37.95   ? 372  ARG A NH1   1 
ATOM   2815 N  NH2   . ARG A 1 380 ? 14.12   13.701  78.13   1 38.753  ? 372  ARG A NH2   1 
ATOM   2816 N  N     . LYS A 1 381 ? 20.605  13.205  73.9    1 25.428  ? 373  LYS A N     1 
ATOM   2817 C  CA    . LYS A 1 381 ? 21.759  12.306  73.837  1 27.863  ? 373  LYS A CA    1 
ATOM   2818 C  C     . LYS A 1 381 ? 22.883  12.986  73.054  1 26.856  ? 373  LYS A C     1 
ATOM   2819 O  O     . LYS A 1 381 ? 22.646  13.98   72.362  1 27.377  ? 373  LYS A O     1 
ATOM   2820 C  CB    . LYS A 1 381 ? 21.415  10.872  73.394  1 28.416  ? 373  LYS A CB    1 
ATOM   2821 C  CG    . LYS A 1 381 ? 20.592  10.059  74.394  1 32.036  ? 373  LYS A CG    1 
ATOM   2822 C  CD    . LYS A 1 381 ? 19.934  8.731   74.034  1 35.99   ? 373  LYS A CD    1 
ATOM   2823 C  CE    . LYS A 1 381 ? 20.562  7.402   74.308  1 41.794  ? 373  LYS A CE    1 
ATOM   2824 N  NZ    . LYS A 1 381 ? 19.678  6.3     73.884  1 38.238  ? 373  LYS A NZ    1 
ATOM   2825 N  N     . ASP A 1 382 ? 24.106  12.452  73.203  1 26.539  ? 374  ASP A N     1 
ATOM   2826 C  CA    . ASP A 1 382 ? 25.255  12.765  72.37   1 27.63   ? 374  ASP A CA    1 
ATOM   2827 C  C     . ASP A 1 382 ? 25.011  12.241  70.949  1 28.392  ? 374  ASP A C     1 
ATOM   2828 O  O     . ASP A 1 382 ? 24.879  11.032  70.743  1 27.782  ? 374  ASP A O     1 
ATOM   2829 C  CB    . ASP A 1 382 ? 26.555  12.299  73.015  1 30.063  ? 374  ASP A CB    1 
ATOM   2830 C  CG    . ASP A 1 382 ? 27.858  12.886  72.476  1 34.589  ? 374  ASP A CG    1 
ATOM   2831 O  OD1   . ASP A 1 382 ? 27.877  13.501  71.379  1 35.779  ? 374  ASP A OD1   1 
ATOM   2832 O  OD2   . ASP A 1 382 ? 28.875  12.748  73.187  1 35.16   ? 374  ASP A OD2   1 
ATOM   2833 N  N     . ASN A 1 383 ? 24.986  13.184  69.989  1 27.369  ? 375  ASN A N     1 
ATOM   2834 C  CA    . ASN A 1 383 ? 24.733  12.944  68.571  1 28.285  ? 375  ASN A CA    1 
ATOM   2835 C  C     . ASN A 1 383 ? 25.944  12.316  67.865  1 29.806  ? 375  ASN A C     1 
ATOM   2836 O  O     . ASN A 1 383 ? 25.769  11.753  66.778  1 29.928  ? 375  ASN A O     1 
ATOM   2837 C  CB    . ASN A 1 383 ? 24.136  14.181  67.901  1 25.908  ? 375  ASN A CB    1 
ATOM   2838 C  CG    . ASN A 1 383 ? 25.118  15.324  67.779  1 25.825  ? 375  ASN A CG    1 
ATOM   2839 O  OD1   . ASN A 1 383 ? 25.483  15.93   68.783  1 26.583  ? 375  ASN A OD1   1 
ATOM   2840 N  ND2   . ASN A 1 383 ? 25.556  15.64   66.57   1 24.551  ? 375  ASN A ND2   1 
ATOM   2841 N  N     . ASN A 1 384 ? 27.149  12.41   68.469  1 30.969  ? 376  ASN A N     1 
ATOM   2842 C  CA    . ASN A 1 384 ? 28.349  11.725  67.981  1 33.06   ? 376  ASN A CA    1 
ATOM   2843 C  C     . ASN A 1 384 ? 28.279  10.205  68.175  1 32.509  ? 376  ASN A C     1 
ATOM   2844 O  O     . ASN A 1 384 ? 28.956  9.484   67.433  1 32.42   ? 376  ASN A O     1 
ATOM   2845 C  CB    . ASN A 1 384 ? 29.659  12.341  68.469  1 33.783  ? 376  ASN A CB    1 
ATOM   2846 C  CG    . ASN A 1 384 ? 29.832  13.798  68.107  1 39.547  ? 376  ASN A CG    1 
ATOM   2847 O  OD1   . ASN A 1 384 ? 30.202  14.581  68.984  1 41.95   ? 376  ASN A OD1   1 
ATOM   2848 N  ND2   . ASN A 1 384 ? 29.625  14.192  66.854  1 41.466  ? 376  ASN A ND2   1 
ATOM   2849 N  N     . GLU A 1 385 ? 27.482  9.752   69.165  1 33.188  ? 377  GLU A N     1 
ATOM   2850 C  CA    . GLU A 1 385 ? 27.298  8.34    69.472  1 34.305  ? 377  GLU A CA    1 
ATOM   2851 C  C     . GLU A 1 385 ? 26.254  7.758   68.519  1 29.447  ? 377  GLU A C     1 
ATOM   2852 O  O     . GLU A 1 385 ? 25.213  8.379   68.308  1 25.573  ? 377  GLU A O     1 
ATOM   2853 C  CB    . GLU A 1 385 ? 27.041  8.041   70.952  1 40.443  ? 377  GLU A CB    1 
ATOM   2854 C  CG    . GLU A 1 385 ? 28.008  6.972   71.469  1 55.998  ? 377  GLU A CG    1 
ATOM   2855 C  CD    . GLU A 1 385 ? 27.655  5.848   72.449  1 71.784  ? 377  GLU A CD    1 
ATOM   2856 O  OE1   . GLU A 1 385 ? 28.624  5.224   72.946  1 74.278  ? 377  GLU A OE1   1 
ATOM   2857 O  OE2   . GLU A 1 385 ? 26.459  5.546   72.701  1 72.998  ? 377  GLU A OE2   1 
ATOM   2858 N  N     . GLN A 1 386 ? 26.576  6.575   67.957  1 27.503  ? 378  GLN A N     1 
ATOM   2859 C  CA    . GLN A 1 386 ? 25.721  5.745   67.108  1 27.016  ? 378  GLN A CA    1 
ATOM   2860 C  C     . GLN A 1 386 ? 24.348  5.53    67.756  1 25.151  ? 378  GLN A C     1 
ATOM   2861 O  O     . GLN A 1 386 ? 24.269  5.191   68.938  1 24.853  ? 378  GLN A O     1 
ATOM   2862 C  CB    . GLN A 1 386 ? 26.381  4.41    66.758  1 27.511  ? 378  GLN A CB    1 
ATOM   2863 C  CG    . GLN A 1 386 ? 25.682  3.663   65.627  1 28.437  ? 378  GLN A CG    1 
ATOM   2864 C  CD    . GLN A 1 386 ? 26.404  2.42    65.165  1 33.434  ? 378  GLN A CD    1 
ATOM   2865 O  OE1   . GLN A 1 386 ? 26.032  1.294   65.512  1 36.091  ? 378  GLN A OE1   1 
ATOM   2866 N  NE2   . GLN A 1 386 ? 27.428  2.615   64.351  1 32.452  ? 378  GLN A NE2   1 
ATOM   2867 N  N     . LEU A 1 387 ? 23.286  5.769   66.962  1 21.965  ? 379  LEU A N     1 
ATOM   2868 C  CA    . LEU A 1 387 ? 21.889  5.556   67.324  1 21.114  ? 379  LEU A CA    1 
ATOM   2869 C  C     . LEU A 1 387 ? 21.626  4.074   67.618  1 22.115  ? 379  LEU A C     1 
ATOM   2870 O  O     . LEU A 1 387 ? 22.29   3.231   66.999  1 20.903  ? 379  LEU A O     1 
ATOM   2871 C  CB    . LEU A 1 387 ? 20.966  6.037   66.196  1 22.213  ? 379  LEU A CB    1 
ATOM   2872 C  CG    . LEU A 1 387 ? 20.805  7.551   65.976  1 20.576  ? 379  LEU A CG    1 
ATOM   2873 C  CD1   . LEU A 1 387 ? 20.06   7.73    64.664  1 18.048  ? 379  LEU A CD1   1 
ATOM   2874 C  CD2   . LEU A 1 387 ? 20.051  8.259   67.111  1 19.06   ? 379  LEU A CD2   1 
ATOM   2875 N  N     . PRO A 1 388 ? 20.663  3.703   68.525  1 23.93   ? 380  PRO A N     1 
ATOM   2876 C  CA    . PRO A 1 388 ? 20.252  2.3     68.68   1 23.784  ? 380  PRO A CA    1 
ATOM   2877 C  C     . PRO A 1 388 ? 19.648  1.715   67.407  1 22.53   ? 380  PRO A C     1 
ATOM   2878 O  O     . PRO A 1 388 ? 19.056  2.466   66.621  1 21.342  ? 380  PRO A O     1 
ATOM   2879 C  CB    . PRO A 1 388 ? 19.273  2.306   69.852  1 24.717  ? 380  PRO A CB    1 
ATOM   2880 C  CG    . PRO A 1 388 ? 18.747  3.73    69.847  1 28.189  ? 380  PRO A CG    1 
ATOM   2881 C  CD    . PRO A 1 388 ? 19.897  4.586   69.433  1 23.702  ? 380  PRO A CD    1 
ATOM   2882 N  N     . ASP A 1 389 ? 19.843  0.394   67.217  1 21.202  ? 381  ASP A N     1 
ATOM   2883 C  CA    . ASP A 1 389 ? 19.265  -0.393  66.126  1 21.008  ? 381  ASP A CA    1 
ATOM   2884 C  C     . ASP A 1 389 ? 17.755  -0.187  66.075  1 23.543  ? 381  ASP A C     1 
ATOM   2885 O  O     . ASP A 1 389 ? 17.152  -0.195  67.148  1 23.182  ? 381  ASP A O     1 
ATOM   2886 C  CB    . ASP A 1 389 ? 19.563  -1.887  66.209  1 23.554  ? 381  ASP A CB    1 
ATOM   2887 C  CG    . ASP A 1 389 ? 21.008  -2.324  66.025  1 24.699  ? 381  ASP A CG    1 
ATOM   2888 O  OD1   . ASP A 1 389 ? 21.872  -1.488  65.655  1 25.553  ? 381  ASP A OD1   1 
ATOM   2889 O  OD2   . ASP A 1 389 ? 21.256  -3.512  66.269  1 26.885  ? 381  ASP A OD2   1 
ATOM   2890 N  N     . PRO A 1 390 ? 17.112  0.042   64.885  1 24.065  ? 382  PRO A N     1 
ATOM   2891 C  CA    . PRO A 1 390 ? 15.67   0.256   64.832  1 23.974  ? 382  PRO A CA    1 
ATOM   2892 C  C     . PRO A 1 390 ? 14.882  -1.006  65.198  1 24.193  ? 382  PRO A C     1 
ATOM   2893 O  O     . PRO A 1 390 ? 15.408  -2.115  65.085  1 24.591  ? 382  PRO A O     1 
ATOM   2894 C  CB    . PRO A 1 390 ? 15.442  0.837   63.433  1 23.983  ? 382  PRO A CB    1 
ATOM   2895 C  CG    . PRO A 1 390 ? 16.527  0.147   62.618  1 23.156  ? 382  PRO A CG    1 
ATOM   2896 C  CD    . PRO A 1 390 ? 17.703  0.036   63.53   1 23.264  ? 382  PRO A CD    1 
ATOM   2897 N  N     . GLU A 1 391 ? 13.65   -0.806  65.678  1 22.91   ? 383  GLU A N     1 
ATOM   2898 C  CA    . GLU A 1 391 ? 12.717  -1.887  65.958  1 21.919  ? 383  GLU A CA    1 
ATOM   2899 C  C     . GLU A 1 391 ? 12.031  -2.313  64.663  1 20.275  ? 383  GLU A C     1 
ATOM   2900 O  O     . GLU A 1 391 ? 11.469  -1.459  63.97   1 21.055  ? 383  GLU A O     1 
ATOM   2901 C  CB    . GLU A 1 391 ? 11.729  -1.431  67.031  1 22.17   ? 383  GLU A CB    1 
ATOM   2902 C  CG    . GLU A 1 391 ? 10.831  -2.552  67.558  1 23.104  ? 383  GLU A CG    1 
ATOM   2903 C  CD    . GLU A 1 391 ? 9.662   -2.183  68.452  1 24.532  ? 383  GLU A CD    1 
ATOM   2904 O  OE1   . GLU A 1 391 ? 9.601   -1.077  69.04   1 27.277  ? 383  GLU A OE1   1 
ATOM   2905 O  OE2   . GLU A 1 391 ? 8.765   -3.04   68.51   1 25.923  ? 383  GLU A OE2   1 
ATOM   2906 N  N     . VAL A 1 392 ? 12.031  -3.631  64.42   1 19.115  ? 384  VAL A N     1 
ATOM   2907 C  CA    . VAL A 1 392 ? 11.298  -4.27   63.334  1 20.676  ? 384  VAL A CA    1 
ATOM   2908 C  C     . VAL A 1 392 ? 9.806   -4.253  63.713  1 21.269  ? 384  VAL A C     1 
ATOM   2909 O  O     . VAL A 1 392 ? 9.402   -4.931  64.657  1 21.45   ? 384  VAL A O     1 
ATOM   2910 C  CB    . VAL A 1 392 ? 11.832  -5.662  62.906  1 18.043  ? 384  VAL A CB    1 
ATOM   2911 C  CG1   . VAL A 1 392 ? 10.947  -6.339  61.863  1 18.048  ? 384  VAL A CG1   1 
ATOM   2912 C  CG2   . VAL A 1 392 ? 13.258  -5.608  62.367  1 17.991  ? 384  VAL A CG2   1 
ATOM   2913 N  N     . ILE A 1 393 ? 9.016   -3.479  62.948  1 21.232  ? 385  ILE A N     1 
ATOM   2914 C  CA    . ILE A 1 393 ? 7.569   -3.335  63.1    1 20.735  ? 385  ILE A CA    1 
ATOM   2915 C  C     . ILE A 1 393 ? 6.843   -4.369  62.233  1 20.572  ? 385  ILE A C     1 
ATOM   2916 O  O     . ILE A 1 393 ? 5.992   -5.086  62.758  1 19.867  ? 385  ILE A O     1 
ATOM   2917 C  CB    . ILE A 1 393 ? 7.1     -1.862  62.94   1 19.926  ? 385  ILE A CB    1 
ATOM   2918 C  CG1   . ILE A 1 393 ? 7.696   -0.876  63.996  1 19.08   ? 385  ILE A CG1   1 
ATOM   2919 C  CG2   . ILE A 1 393 ? 5.58    -1.71   62.804  1 20.785  ? 385  ILE A CG2   1 
ATOM   2920 C  CD1   . ILE A 1 393 ? 7.528   -1.237  65.477  1 18.925  ? 385  ILE A CD1   1 
ATOM   2921 N  N     . LEU A 1 394 ? 7.194   -4.431  60.931  1 22.132  ? 386  LEU A N     1 
ATOM   2922 C  CA    . LEU A 1 394 ? 6.732   -5.446  59.989  1 21.571  ? 386  LEU A CA    1 
ATOM   2923 C  C     . LEU A 1 394 ? 7.948   -6.069  59.334  1 23.816  ? 386  LEU A C     1 
ATOM   2924 O  O     . LEU A 1 394 ? 8.735   -5.353  58.704  1 23.098  ? 386  LEU A O     1 
ATOM   2925 C  CB    . LEU A 1 394 ? 5.732   -4.982  58.925  1 21.347  ? 386  LEU A CB    1 
ATOM   2926 C  CG    . LEU A 1 394 ? 4.469   -4.233  59.383  1 22.577  ? 386  LEU A CG    1 
ATOM   2927 C  CD1   . LEU A 1 394 ? 3.913   -3.527  58.152  1 21.757  ? 386  LEU A CD1   1 
ATOM   2928 C  CD2   . LEU A 1 394 ? 3.405   -5.087  60.092  1 22.004  ? 386  LEU A CD2   1 
ATOM   2929 N  N     . ASP A 1 395 ? 8.041   -7.405  59.47   1 25.681  ? 387  ASP A N     1 
ATOM   2930 C  CA    . ASP A 1 395 ? 9.042   -8.208  58.775  1 26.164  ? 387  ASP A CA    1 
ATOM   2931 C  C     . ASP A 1 395 ? 8.52    -8.625  57.398  1 23.298  ? 387  ASP A C     1 
ATOM   2932 O  O     . ASP A 1 395 ? 8.468   -9.812  57.066  1 22.861  ? 387  ASP A O     1 
ATOM   2933 C  CB    . ASP A 1 395 ? 9.706   -9.234  59.691  1 28.56   ? 387  ASP A CB    1 
ATOM   2934 C  CG    . ASP A 1 395 ? 10.831  -10.054 59.061  1 31.479  ? 387  ASP A CG    1 
ATOM   2935 O  OD1   . ASP A 1 395 ? 11.653  -9.482  58.312  1 32.401  ? 387  ASP A OD1   1 
ATOM   2936 O  OD2   . ASP A 1 395 ? 10.892  -11.27  59.321  1 33.973  ? 387  ASP A OD2   1 
ATOM   2937 N  N     . THR A 1 396 ? 8.114   -7.623  56.605  1 22.167  ? 388  THR A N     1 
ATOM   2938 C  CA    . THR A 1 396 ? 7.619   -7.792  55.246  1 22.658  ? 388  THR A CA    1 
ATOM   2939 C  C     . THR A 1 396 ? 8.099   -6.615  54.393  1 20.424  ? 388  THR A C     1 
ATOM   2940 O  O     . THR A 1 396 ? 8.164   -5.508  54.94   1 20.95   ? 388  THR A O     1 
ATOM   2941 C  CB    . THR A 1 396 ? 6.106   -8.083  55.209  1 25.902  ? 388  THR A CB    1 
ATOM   2942 O  OG1   . THR A 1 396 ? 5.802   -8.582  53.906  1 27.305  ? 388  THR A OG1   1 
ATOM   2943 C  CG2   . THR A 1 396 ? 5.179   -6.909  55.469  1 27.475  ? 388  THR A CG2   1 
ATOM   2944 N  N     . PRO A 1 397 ? 8.481   -6.793  53.088  1 19.217  ? 389  PRO A N     1 
ATOM   2945 C  CA    . PRO A 1 397 ? 8.751   -5.651  52.211  1 19.1    ? 389  PRO A CA    1 
ATOM   2946 C  C     . PRO A 1 397 ? 7.594   -4.656  52.182  1 19.66   ? 389  PRO A C     1 
ATOM   2947 O  O     . PRO A 1 397 ? 6.444   -5.048  52.018  1 18.629  ? 389  PRO A O     1 
ATOM   2948 C  CB    . PRO A 1 397 ? 9.19    -6.262  50.874  1 18.648  ? 389  PRO A CB    1 
ATOM   2949 C  CG    . PRO A 1 397 ? 9.466   -7.725  51.167  1 16.746  ? 389  PRO A CG    1 
ATOM   2950 C  CD    . PRO A 1 397 ? 8.664   -8.077  52.372  1 17.683  ? 389  PRO A CD    1 
ATOM   2951 N  N     . SER A 1 398 ? 7.945   -3.406  52.505  1 19.736  ? 390  SER A N     1 
ATOM   2952 C  CA    . SER A 1 398 ? 7.04    -2.313  52.836  1 18.825  ? 390  SER A CA    1 
ATOM   2953 C  C     . SER A 1 398 ? 7.539   -1.049  52.151  1 19.674  ? 390  SER A C     1 
ATOM   2954 O  O     . SER A 1 398 ? 8.744   -0.792  52.145  1 19.728  ? 390  SER A O     1 
ATOM   2955 C  CB    . SER A 1 398 ? 6.994   -2.125  54.331  1 17.755  ? 390  SER A CB    1 
ATOM   2956 O  OG    . SER A 1 398 ? 6.462   -3.283  54.959  1 17.764  ? 390  SER A OG    1 
ATOM   2957 N  N     . GLU A 1 399 ? 6.609   -0.311  51.542  1 19.795  ? 391  GLU A N     1 
ATOM   2958 C  CA    . GLU A 1 399 ? 6.897   0.945   50.858  1 19.051  ? 391  GLU A CA    1 
ATOM   2959 C  C     . GLU A 1 399 ? 5.679   1.864   50.854  1 18.568  ? 391  GLU A C     1 
ATOM   2960 O  O     . GLU A 1 399 ? 4.623   1.495   51.362  1 19.331  ? 391  GLU A O     1 
ATOM   2961 C  CB    . GLU A 1 399 ? 7.617   0.789   49.508  1 19.932  ? 391  GLU A CB    1 
ATOM   2962 C  CG    . GLU A 1 399 ? 9.047   1.33    49.541  1 22.814  ? 391  GLU A CG    1 
ATOM   2963 C  CD    . GLU A 1 399 ? 9.1     2.803   49.923  1 23.743  ? 391  GLU A CD    1 
ATOM   2964 O  OE1   . GLU A 1 399 ? 8.636   3.596   49.099  1 26.677  ? 391  GLU A OE1   1 
ATOM   2965 O  OE2   . GLU A 1 399 ? 9.47    3.155   51.051  1 21.805  ? 391  GLU A OE2   1 
ATOM   2966 N  N     . PHE A 1 400 ? 5.891   3.103   50.37   1 18.389  ? 392  PHE A N     1 
ATOM   2967 C  CA    . PHE A 1 400 ? 4.883   4.138   50.168  1 18.6    ? 392  PHE A CA    1 
ATOM   2968 C  C     . PHE A 1 400 ? 3.906   4.229   51.365  1 17.346  ? 392  PHE A C     1 
ATOM   2969 O  O     . PHE A 1 400 ? 2.693   4.093   51.147  1 16.929  ? 392  PHE A O     1 
ATOM   2970 C  CB    . PHE A 1 400 ? 4.289   3.886   48.768  1 17.693  ? 392  PHE A CB    1 
ATOM   2971 C  CG    . PHE A 1 400 ? 5.176   4.155   47.559  1 18.145  ? 392  PHE A CG    1 
ATOM   2972 C  CD1   . PHE A 1 400 ? 5.533   5.472   47.203  1 16.866  ? 392  PHE A CD1   1 
ATOM   2973 C  CD2   . PHE A 1 400 ? 5.569   3.101   46.714  1 17.829  ? 392  PHE A CD2   1 
ATOM   2974 C  CE1   . PHE A 1 400 ? 6.316   5.743   46.07   1 17.25   ? 392  PHE A CE1   1 
ATOM   2975 C  CE2   . PHE A 1 400 ? 6.332   3.367   45.567  1 18.003  ? 392  PHE A CE2   1 
ATOM   2976 C  CZ    . PHE A 1 400 ? 6.722   4.685   45.256  1 17.916  ? 392  PHE A CZ    1 
ATOM   2977 N  N     . PRO A 1 401 ? 4.353   4.42    52.652  1 16.671  ? 393  PRO A N     1 
ATOM   2978 C  CA    . PRO A 1 401 ? 3.415   4.655   53.737  1 16.078  ? 393  PRO A CA    1 
ATOM   2979 C  C     . PRO A 1 401 ? 2.785   6.046   53.686  1 16.511  ? 393  PRO A C     1 
ATOM   2980 O  O     . PRO A 1 401 ? 3.422   7.012   53.257  1 16.036  ? 393  PRO A O     1 
ATOM   2981 C  CB    . PRO A 1 401 ? 4.218   4.328   55.003  1 16.353  ? 393  PRO A CB    1 
ATOM   2982 C  CG    . PRO A 1 401 ? 5.604   4.823   54.619  1 16.267  ? 393  PRO A CG    1 
ATOM   2983 C  CD    . PRO A 1 401 ? 5.746   4.525   53.154  1 15.905  ? 393  PRO A CD    1 
ATOM   2984 N  N     . GLN A 1 402 ? 1.507   6.098   54.094  1 17.469  ? 394  GLN A N     1 
ATOM   2985 C  CA    . GLN A 1 402 ? 0.792   7.333   54.402  1 18.213  ? 394  GLN A CA    1 
ATOM   2986 C  C     . GLN A 1 402 ? 0.12    7.177   55.767  1 17.72   ? 394  GLN A C     1 
ATOM   2987 O  O     . GLN A 1 402 ? 0.015   6.061   56.303  1 18.111  ? 394  GLN A O     1 
ATOM   2988 C  CB    . GLN A 1 402 ? -0.137  7.752   53.256  1 17.499  ? 394  GLN A CB    1 
ATOM   2989 C  CG    . GLN A 1 402 ? 0.561   8.405   52.054  1 19.555  ? 394  GLN A CG    1 
ATOM   2990 C  CD    . GLN A 1 402 ? -0.3    9.319   51.186  1 19.577  ? 394  GLN A CD    1 
ATOM   2991 O  OE1   . GLN A 1 402 ? -1.419  9.732   51.534  1 19.335  ? 394  GLN A OE1   1 
ATOM   2992 N  NE2   . GLN A 1 402 ? 0.243   9.704   50.037  1 16.872  ? 394  GLN A NE2   1 
ATOM   2993 N  N     . ILE A 1 403 ? -0.299  8.318   56.327  1 15.882  ? 395  ILE A N     1 
ATOM   2994 C  CA    . ILE A 1 403 ? -0.95   8.405   57.633  1 15.519  ? 395  ILE A CA    1 
ATOM   2995 C  C     . ILE A 1 403 ? -2.33   9.075   57.497  1 15.188  ? 395  ILE A C     1 
ATOM   2996 O  O     . ILE A 1 403 ? -2.758  9.42    56.39   1 15.513  ? 395  ILE A O     1 
ATOM   2997 C  CB    . ILE A 1 403 ? -0.018  9.015   58.717  1 15.793  ? 395  ILE A CB    1 
ATOM   2998 C  CG1   . ILE A 1 403 ? 0.263   10.538  58.544  1 16.557  ? 395  ILE A CG1   1 
ATOM   2999 C  CG2   . ILE A 1 403 ? 1.277   8.2     58.905  1 15.896  ? 395  ILE A CG2   1 
ATOM   3000 C  CD1   . ILE A 1 403 ? 0.437   11.304  59.864  1 18.824  ? 395  ILE A CD1   1 
ATOM   3001 N  N     . ASP A 1 404 ? -3.033  9.205   58.633  1 15.515  ? 396  ASP A N     1 
ATOM   3002 C  CA    . ASP A 1 404 ? -4.119  10.158  58.825  1 16.708  ? 396  ASP A CA    1 
ATOM   3003 C  C     . ASP A 1 404 ? -3.525  11.545  59.079  1 16.389  ? 396  ASP A C     1 
ATOM   3004 O  O     . ASP A 1 404 ? -3.071  11.842  60.193  1 17.802  ? 396  ASP A O     1 
ATOM   3005 C  CB    . ASP A 1 404 ? -5.078  9.641   59.892  1 17.595  ? 396  ASP A CB    1 
ATOM   3006 C  CG    . ASP A 1 404 ? -6.327  10.455  60.2    1 18.262  ? 396  ASP A CG    1 
ATOM   3007 O  OD1   . ASP A 1 404 ? -6.437  11.62   59.745  1 17.772  ? 396  ASP A OD1   1 
ATOM   3008 O  OD2   . ASP A 1 404 ? -7.225  9.878   60.87   1 19.344  ? 396  ASP A OD2   1 
ATOM   3009 N  N     . ASN A 1 405 ? -3.61   12.407  58.059  1 16.184  ? 397  ASN A N     1 
ATOM   3010 C  CA    . ASN A 1 405 ? -2.949  13.712  58.022  1 17.146  ? 397  ASN A CA    1 
ATOM   3011 C  C     . ASN A 1 405 ? -3.503  14.732  59.029  1 18.17   ? 397  ASN A C     1 
ATOM   3012 O  O     . ASN A 1 405 ? -2.854  15.741  59.301  1 17.768  ? 397  ASN A O     1 
ATOM   3013 C  CB    . ASN A 1 405 ? -2.867  14.254  56.598  1 17.462  ? 397  ASN A CB    1 
ATOM   3014 C  CG    . ASN A 1 405 ? -1.789  13.605  55.761  1 17.239  ? 397  ASN A CG    1 
ATOM   3015 O  OD1   . ASN A 1 405 ? -0.847  12.985  56.273  1 17.415  ? 397  ASN A OD1   1 
ATOM   3016 N  ND2   . ASN A 1 405 ? -1.905  13.761  54.451  1 16.073  ? 397  ASN A ND2   1 
ATOM   3017 N  N     . ARG A 1 406 ? -4.663  14.439  59.636  1 18.402  ? 398  ARG A N     1 
ATOM   3018 C  CA    . ARG A 1 406 ? -5.166  15.144  60.811  1 18.117  ? 398  ARG A CA    1 
ATOM   3019 C  C     . ARG A 1 406 ? -4.227  15.005  62.021  1 18.557  ? 398  ARG A C     1 
ATOM   3020 O  O     . ARG A 1 406 ? -4.362  15.78   62.971  1 16.863  ? 398  ARG A O     1 
ATOM   3021 C  CB    . ARG A 1 406 ? -6.606  14.711  61.119  1 18.078  ? 398  ARG A CB    1 
ATOM   3022 C  CG    . ARG A 1 406 ? -7.622  15.037  60.028  1 18.695  ? 398  ARG A CG    1 
ATOM   3023 C  CD    . ARG A 1 406 ? -8.979  14.455  60.351  1 20      ? 398  ARG A CD    1 
ATOM   3024 N  NE    . ARG A 1 406 ? -8.947  13.009  60.626  1 19.647  ? 398  ARG A NE    1 
ATOM   3025 C  CZ    . ARG A 1 406 ? -9.836  12.265  61.277  1 19.703  ? 398  ARG A CZ    1 
ATOM   3026 N  NH1   . ARG A 1 406 ? -10.959 12.789  61.728  1 18.081  ? 398  ARG A NH1   1 
ATOM   3027 N  NH2   . ARG A 1 406 ? -9.606  10.975  61.451  1 18.108  ? 398  ARG A NH2   1 
ATOM   3028 N  N     . PHE A 1 407 ? -3.257  14.063  61.936  1 19.341  ? 399  PHE A N     1 
ATOM   3029 C  CA    . PHE A 1 407 ? -2.254  13.77   62.949  1 18.765  ? 399  PHE A CA    1 
ATOM   3030 C  C     . PHE A 1 407 ? -0.838  14.102  62.454  1 19.657  ? 399  PHE A C     1 
ATOM   3031 O  O     . PHE A 1 407 ? 0.133   13.66   63.079  1 18.438  ? 399  PHE A O     1 
ATOM   3032 C  CB    . PHE A 1 407 ? -2.511  12.351  63.48   1 19.017  ? 399  PHE A CB    1 
ATOM   3033 C  CG    . PHE A 1 407 ? -3.83   12.216  64.239  1 19.71   ? 399  PHE A CG    1 
ATOM   3034 C  CD1   . PHE A 1 407 ? -5.027  11.92   63.56   1 19.255  ? 399  PHE A CD1   1 
ATOM   3035 C  CD2   . PHE A 1 407 ? -3.867  12.391  65.64   1 19.992  ? 399  PHE A CD2   1 
ATOM   3036 C  CE1   . PHE A 1 407 ? -6.241  11.834  64.26   1 20.717  ? 399  PHE A CE1   1 
ATOM   3037 C  CE2   . PHE A 1 407 ? -5.082  12.285  66.349  1 20.854  ? 399  PHE A CE2   1 
ATOM   3038 C  CZ    . PHE A 1 407 ? -6.269  12.008  65.649  1 21.098  ? 399  PHE A CZ    1 
ATOM   3039 N  N     . MET A 1 408 ? -0.72   14.884  61.363  1 18.794  ? 400  MET A N     1 
ATOM   3040 C  CA    . MET A 1 408 ? 0.579   15.226  60.794  1 19.317  ? 400  MET A CA    1 
ATOM   3041 C  C     . MET A 1 408 ? 1.304   16.228  61.693  1 20.027  ? 400  MET A C     1 
ATOM   3042 O  O     . MET A 1 408 ? 0.774   17.296  61.992  1 19.802  ? 400  MET A O     1 
ATOM   3043 C  CB    . MET A 1 408 ? 0.494   15.675  59.328  1 18.861  ? 400  MET A CB    1 
ATOM   3044 C  CG    . MET A 1 408 ? 1.855   16.013  58.684  1 19.643  ? 400  MET A CG    1 
ATOM   3045 S  SD    . MET A 1 408 ? 3.15    14.756  58.716  1 18.472  ? 400  MET A SD    1 
ATOM   3046 C  CE    . MET A 1 408 ? 2.602   13.651  57.41   1 19.093  ? 400  MET A CE    1 
ATOM   3047 N  N     . GLY A 1 409 ? 2.522   15.839  62.101  1 19.893  ? 401  GLY A N     1 
ATOM   3048 C  CA    . GLY A 1 409 ? 3.4     16.621  62.957  1 18.812  ? 401  GLY A CA    1 
ATOM   3049 C  C     . GLY A 1 409 ? 3.035   16.549  64.438  1 18.714  ? 401  GLY A C     1 
ATOM   3050 O  O     . GLY A 1 409 ? 3.557   17.35   65.207  1 18.142  ? 401  GLY A O     1 
ATOM   3051 N  N     . VAL A 1 410 ? 2.124   15.626  64.803  1 18.253  ? 402  VAL A N     1 
ATOM   3052 C  CA    . VAL A 1 410 ? 1.746   15.258  66.166  1 18.587  ? 402  VAL A CA    1 
ATOM   3053 C  C     . VAL A 1 410 ? 1.794   13.733  66.276  1 19.507  ? 402  VAL A C     1 
ATOM   3054 O  O     . VAL A 1 410 ? 2.027   13.064  65.256  1 23.538  ? 402  VAL A O     1 
ATOM   3055 C  CB    . VAL A 1 410 ? 0.44    15.896  66.715  1 19.2    ? 402  VAL A CB    1 
ATOM   3056 C  CG1   . VAL A 1 410 ? 0.533   17.42   66.821  1 19.499  ? 402  VAL A CG1   1 
ATOM   3057 C  CG2   . VAL A 1 410 ? -0.833  15.507  65.965  1 19.512  ? 402  VAL A CG2   1 
ATOM   3058 N  N     . GLU A 1 411 ? 1.604   13.198  67.503  1 19.604  ? 403  GLU A N     1 
ATOM   3059 C  CA    . GLU A 1 411 ? 1.439   11.772  67.779  1 20.072  ? 403  GLU A CA    1 
ATOM   3060 C  C     . GLU A 1 411 ? 0.371   11.159  66.862  1 17.968  ? 403  GLU A C     1 
ATOM   3061 O  O     . GLU A 1 411 ? -0.739  11.666  66.814  1 17.446  ? 403  GLU A O     1 
ATOM   3062 C  CB    . GLU A 1 411 ? 1.184   11.48   69.256  1 19.616  ? 403  GLU A CB    1 
ATOM   3063 C  CG    . GLU A 1 411 ? 1.223   9.982   69.568  1 22.862  ? 403  GLU A CG    1 
ATOM   3064 C  CD    . GLU A 1 411 ? 1.142   9.506   71.009  1 25.037  ? 403  GLU A CD    1 
ATOM   3065 O  OE1   . GLU A 1 411 ? 1.221   10.326  71.944  1 25.025  ? 403  GLU A OE1   1 
ATOM   3066 O  OE2   . GLU A 1 411 ? 0.979   8.282   71.192  1 29.299  ? 403  GLU A OE2   1 
ATOM   3067 N  N     . TYR A 1 412 ? 0.772   10.098  66.143  1 17.513  ? 404  TYR A N     1 
ATOM   3068 C  CA    . TYR A 1 412 ? -0.063  9.332   65.231  1 18.573  ? 404  TYR A CA    1 
ATOM   3069 C  C     . TYR A 1 412 ? 0.055   7.85    65.592  1 18.41   ? 404  TYR A C     1 
ATOM   3070 O  O     . TYR A 1 412 ? 1.033   7.441   66.214  1 17.902  ? 404  TYR A O     1 
ATOM   3071 C  CB    . TYR A 1 412 ? 0.351   9.721   63.801  1 17.501  ? 404  TYR A CB    1 
ATOM   3072 C  CG    . TYR A 1 412 ? 1.55    8.935   63.295  1 19.078  ? 404  TYR A CG    1 
ATOM   3073 C  CD1   . TYR A 1 412 ? 2.866   9.321   63.629  1 19.355  ? 404  TYR A CD1   1 
ATOM   3074 C  CD2   . TYR A 1 412 ? 1.369   7.78    62.512  1 17.613  ? 404  TYR A CD2   1 
ATOM   3075 C  CE1   . TYR A 1 412 ? 3.955   8.568   63.196  1 18.924  ? 404  TYR A CE1   1 
ATOM   3076 C  CE2   . TYR A 1 412 ? 2.461   7.024   62.082  1 17.315  ? 404  TYR A CE2   1 
ATOM   3077 C  CZ    . TYR A 1 412 ? 3.747   7.429   62.414  1 18.261  ? 404  TYR A CZ    1 
ATOM   3078 O  OH    . TYR A 1 412 ? 4.806   6.674   62.004  1 18.628  ? 404  TYR A OH    1 
ATOM   3079 N  N     . SER A 1 413 ? -0.891  7.052   65.071  1 19.61   ? 405  SER A N     1 
ATOM   3080 C  CA    . SER A 1 413 ? -1.051  5.63    65.346  1 19.113  ? 405  SER A CA    1 
ATOM   3081 C  C     . SER A 1 413 ? -1.235  4.827   64.055  1 18.815  ? 405  SER A C     1 
ATOM   3082 O  O     . SER A 1 413 ? -0.582  3.786   63.916  1 21.783  ? 405  SER A O     1 
ATOM   3083 C  CB    . SER A 1 413 ? -2.16   5.361   66.357  1 18.346  ? 405  SER A CB    1 
ATOM   3084 O  OG    . SER A 1 413 ? -2.29   3.955   66.595  1 18.745  ? 405  SER A OG    1 
ATOM   3085 N  N     . SER A 1 414 ? -2.157  5.274   63.173  1 17.883  ? 406  SER A N     1 
ATOM   3086 C  CA    . SER A 1 414 ? -2.481  4.639   61.892  1 15.626  ? 406  SER A CA    1 
ATOM   3087 C  C     . SER A 1 414 ? -1.372  4.878   60.865  1 16.579  ? 406  SER A C     1 
ATOM   3088 O  O     . SER A 1 414 ? -0.919  6.021   60.675  1 17.926  ? 406  SER A O     1 
ATOM   3089 C  CB    . SER A 1 414 ? -3.806  5.106   61.376  1 15.236  ? 406  SER A CB    1 
ATOM   3090 O  OG    . SER A 1 414 ? -4.85   4.249   61.793  1 16.36   ? 406  SER A OG    1 
ATOM   3091 N  N     . ALA A 1 415 ? -0.925  3.783   60.227  1 16.775  ? 407  ALA A N     1 
ATOM   3092 C  CA    . ALA A 1 415 ? -0.158  3.839   58.985  1 16.725  ? 407  ALA A CA    1 
ATOM   3093 C  C     . ALA A 1 415 ? -0.776  2.929   57.921  1 17.477  ? 407  ALA A C     1 
ATOM   3094 O  O     . ALA A 1 415 ? -1.153  1.79    58.22   1 19.821  ? 407  ALA A O     1 
ATOM   3095 C  CB    . ALA A 1 415 ? 1.318   3.556   59.223  1 16.387  ? 407  ALA A CB    1 
ATOM   3096 N  N     . PHE A 1 416 ? -0.891  3.478   56.7    1 15.691  ? 408  PHE A N     1 
ATOM   3097 C  CA    . PHE A 1 416 ? -1.355  2.779   55.508  1 16.052  ? 408  PHE A CA    1 
ATOM   3098 C  C     . PHE A 1 416 ? -0.144  2.527   54.609  1 16.989  ? 408  PHE A C     1 
ATOM   3099 O  O     . PHE A 1 416 ? 0.481   3.47    54.133  1 17.233  ? 408  PHE A O     1 
ATOM   3100 C  CB    . PHE A 1 416 ? -2.522  3.516   54.844  1 15.439  ? 408  PHE A CB    1 
ATOM   3101 C  CG    . PHE A 1 416 ? -3.622  3.953   55.797  1 16.273  ? 408  PHE A CG    1 
ATOM   3102 C  CD1   . PHE A 1 416 ? -4.596  3.043   56.241  1 16.564  ? 408  PHE A CD1   1 
ATOM   3103 C  CD2   . PHE A 1 416 ? -3.666  5.283   56.267  1 17.847  ? 408  PHE A CD2   1 
ATOM   3104 C  CE1   . PHE A 1 416 ? -5.615  3.467   57.104  1 17.103  ? 408  PHE A CE1   1 
ATOM   3105 C  CE2   . PHE A 1 416 ? -4.67   5.694   57.167  1 18.059  ? 408  PHE A CE2   1 
ATOM   3106 C  CZ    . PHE A 1 416 ? -5.64   4.779   57.581  1 16.537  ? 408  PHE A CZ    1 
ATOM   3107 N  N     . ILE A 1 417 ? 0.21    1.246   54.447  1 16.821  ? 409  ILE A N     1 
ATOM   3108 C  CA    . ILE A 1 417 ? 1.515   0.836   53.934  1 16.427  ? 409  ILE A CA    1 
ATOM   3109 C  C     . ILE A 1 417 ? 1.271   -0.043  52.705  1 17.075  ? 409  ILE A C     1 
ATOM   3110 O  O     . ILE A 1 417 ? 0.466   -0.973  52.768  1 15.649  ? 409  ILE A O     1 
ATOM   3111 C  CB    . ILE A 1 417 ? 2.369   0.15    55.035  1 17.046  ? 409  ILE A CB    1 
ATOM   3112 C  CG1   . ILE A 1 417 ? 2.401   0.937   56.386  1 17.871  ? 409  ILE A CG1   1 
ATOM   3113 C  CG2   . ILE A 1 417 ? 3.788   -0.154  54.528  1 17.471  ? 409  ILE A CG2   1 
ATOM   3114 C  CD1   . ILE A 1 417 ? 2.616   0.105   57.65   1 19.524  ? 409  ILE A CD1   1 
ATOM   3115 N  N     . ASN A 1 418 ? 1.988   0.268   51.607  1 17.483  ? 410  ASN A N     1 
ATOM   3116 C  CA    . ASN A 1 418 ? 2.082   -0.545  50.394  1 17.297  ? 410  ASN A CA    1 
ATOM   3117 C  C     . ASN A 1 418 ? 3.023   -1.713  50.699  1 17.463  ? 410  ASN A C     1 
ATOM   3118 O  O     . ASN A 1 418 ? 4.15    -1.479  51.155  1 18.754  ? 410  ASN A O     1 
ATOM   3119 C  CB    . ASN A 1 418 ? 2.46    0.374   49.226  1 17.014  ? 410  ASN A CB    1 
ATOM   3120 C  CG    . ASN A 1 418 ? 2.16    -0.092  47.823  1 17.443  ? 410  ASN A CG    1 
ATOM   3121 O  OD1   . ASN A 1 418 ? 1.432   -1.068  47.591  1 20.563  ? 410  ASN A OD1   1 
ATOM   3122 N  ND2   . ASN A 1 418 ? 2.725   0.608   46.85   1 15.596  ? 410  ASN A ND2   1 
ATOM   3123 N  N     . VAL A 1 419 ? 2.544   -2.959  50.503  1 16.641  ? 411  VAL A N     1 
ATOM   3124 C  CA    . VAL A 1 419 ? 3.221   -4.154  51.029  1 16.583  ? 411  VAL A CA    1 
ATOM   3125 C  C     . VAL A 1 419 ? 3.365   -5.25   49.966  1 18.056  ? 411  VAL A C     1 
ATOM   3126 O  O     . VAL A 1 419 ? 2.542   -5.357  49.04   1 17.159  ? 411  VAL A O     1 
ATOM   3127 C  CB    . VAL A 1 419 ? 2.69    -4.748  52.361  1 16.29   ? 411  VAL A CB    1 
ATOM   3128 C  CG1   . VAL A 1 419 ? 3.028   -3.886  53.569  1 15.254  ? 411  VAL A CG1   1 
ATOM   3129 C  CG2   . VAL A 1 419 ? 1.212   -5.146  52.334  1 15.386  ? 411  VAL A CG2   1 
ATOM   3130 N  N     . PHE A 1 420 ? 4.417   -6.076  50.143  1 17.978  ? 412  PHE A N     1 
ATOM   3131 C  CA    . PHE A 1 420 ? 4.441   -7.455  49.666  1 19.264  ? 412  PHE A CA    1 
ATOM   3132 C  C     . PHE A 1 420 ? 3.658   -8.29   50.681  1 19.867  ? 412  PHE A C     1 
ATOM   3133 O  O     . PHE A 1 420 ? 4.028   -8.319  51.864  1 20.061  ? 412  PHE A O     1 
ATOM   3134 C  CB    . PHE A 1 420 ? 5.847   -8.048  49.489  1 20.335  ? 412  PHE A CB    1 
ATOM   3135 C  CG    . PHE A 1 420 ? 6.864   -7.563  48.459  1 22.208  ? 412  PHE A CG    1 
ATOM   3136 C  CD1   . PHE A 1 420 ? 6.978   -6.204  48.067  1 22.195  ? 412  PHE A CD1   1 
ATOM   3137 C  CD2   . PHE A 1 420 ? 7.792   -8.486  47.934  1 23.695  ? 412  PHE A CD2   1 
ATOM   3138 C  CE1   . PHE A 1 420 ? 7.974   -5.789  47.168  1 21.424  ? 412  PHE A CE1   1 
ATOM   3139 C  CE2   . PHE A 1 420 ? 8.783   -8.071  47.025  1 24.181  ? 412  PHE A CE2   1 
ATOM   3140 C  CZ    . PHE A 1 420 ? 8.879   -6.718  46.651  1 23.765  ? 412  PHE A CZ    1 
ATOM   3141 N  N     . VAL A 1 421 ? 2.564   -8.926  50.214  1 19.404  ? 413  VAL A N     1 
ATOM   3142 C  CA    . VAL A 1 421 ? 1.626   -9.656  51.074  1 19.059  ? 413  VAL A CA    1 
ATOM   3143 C  C     . VAL A 1 421 ? 2.342   -10.926 51.569  1 19.475  ? 413  VAL A C     1 
ATOM   3144 O  O     . VAL A 1 421 ? 2.775   -11.709 50.708  1 18.193  ? 413  VAL A O     1 
ATOM   3145 C  CB    . VAL A 1 421 ? 0.213   -9.956  50.507  1 17.949  ? 413  VAL A CB    1 
ATOM   3146 C  CG1   . VAL A 1 421 ? -0.695  -10.685 51.492  1 19.347  ? 413  VAL A CG1   1 
ATOM   3147 C  CG2   . VAL A 1 421 ? -0.502  -8.704  50.047  1 16.759  ? 413  VAL A CG2   1 
ATOM   3148 N  N     . PRO A 1 422 ? 2.493   -11.154 52.92   1 21.727  ? 414  PRO A N     1 
ATOM   3149 C  CA    . PRO A 1 422 ? 3.08    -12.396 53.456  1 23.592  ? 414  PRO A CA    1 
ATOM   3150 C  C     . PRO A 1 422 ? 2.392   -13.646 52.908  1 24.774  ? 414  PRO A C     1 
ATOM   3151 O  O     . PRO A 1 422 ? 1.16    -13.673 52.83   1 25.108  ? 414  PRO A O     1 
ATOM   3152 C  CB    . PRO A 1 422 ? 2.956   -12.272 54.986  1 22.52   ? 414  PRO A CB    1 
ATOM   3153 C  CG    . PRO A 1 422 ? 2.842   -10.781 55.224  1 21.422  ? 414  PRO A CG    1 
ATOM   3154 C  CD    . PRO A 1 422 ? 2.088   -10.253 54.022  1 20.491  ? 414  PRO A CD    1 
ATOM   3155 N  N     . ASP A 1 423 ? 3.219   -14.588 52.41   1 28.88   ? 415  ASP A N     1 
ATOM   3156 C  CA    . ASP A 1 423 ? 2.883   -15.91  51.865  1 31.073  ? 415  ASP A CA    1 
ATOM   3157 C  C     . ASP A 1 423 ? 2.157   -15.836 50.506  1 30.023  ? 415  ASP A C     1 
ATOM   3158 O  O     . ASP A 1 423 ? 1.764   -16.875 49.974  1 29.539  ? 415  ASP A O     1 
ATOM   3159 C  CB    . ASP A 1 423 ? 2.271   -16.846 52.916  1 36.553  ? 415  ASP A CB    1 
ATOM   3160 C  CG    . ASP A 1 423 ? 2.983   -16.981 54.263  1 41.788  ? 415  ASP A CG    1 
ATOM   3161 O  OD1   . ASP A 1 423 ? 4.19    -17.332 54.289  1 48.817  ? 415  ASP A OD1   1 
ATOM   3162 O  OD2   . ASP A 1 423 ? 2.324   -16.748 55.302  1 46.996  ? 415  ASP A OD2   1 
ATOM   3163 N  N     . ARG A 1 424 ? 2.043   -14.631 49.91   1 30.095  ? 416  ARG A N     1 
ATOM   3164 C  CA    . ARG A 1 424 ? 1.218   -14.348 48.738  1 30.398  ? 416  ARG A CA    1 
ATOM   3165 C  C     . ARG A 1 424 ? 1.968   -13.539 47.677  1 31.777  ? 416  ARG A C     1 
ATOM   3166 O  O     . ARG A 1 424 ? 1.357   -13.154 46.67   1 36.821  ? 416  ARG A O     1 
ATOM   3167 C  CB    . ARG A 1 424 ? -0.068  -13.62  49.166  1 31.691  ? 416  ARG A CB    1 
ATOM   3168 C  CG    . ARG A 1 424 ? -1.08   -14.249 50.115  1 36.541  ? 416  ARG A CG    1 
ATOM   3169 C  CD    . ARG A 1 424 ? -1.997  -15.261 49.451  1 40.026  ? 416  ARG A CD    1 
ATOM   3170 N  NE    . ARG A 1 424 ? -3.133  -14.81  48.632  1 38.139  ? 416  ARG A NE    1 
ATOM   3171 C  CZ    . ARG A 1 424 ? -4.287  -14.244 48.998  1 38.705  ? 416  ARG A CZ    1 
ATOM   3172 N  NH1   . ARG A 1 424 ? -4.401  -13.396 50.012  1 39.071  ? 416  ARG A NH1   1 
ATOM   3173 N  NH2   . ARG A 1 424 ? -5.342  -14.446 48.23   1 37.518  ? 416  ARG A NH2   1 
ATOM   3174 N  N     . SER A 1 425 ? 3.278   -13.314 47.895  1 30      ? 417  SER A N     1 
ATOM   3175 C  CA    . SER A 1 425 ? 4.117   -12.427 47.1    1 29.31   ? 417  SER A CA    1 
ATOM   3176 C  C     . SER A 1 425 ? 5.463   -13.074 46.766  1 31.921  ? 417  SER A C     1 
ATOM   3177 O  O     . SER A 1 425 ? 5.779   -14.147 47.298  1 32.968  ? 417  SER A O     1 
ATOM   3178 C  CB    . SER A 1 425 ? 4.255   -11.076 47.763  1 29.3    ? 417  SER A CB    1 
ATOM   3179 O  OG    . SER A 1 425 ? 4.875   -11.173 49.029  1 27.437  ? 417  SER A OG    1 
ATOM   3180 N  N     . ASP A 1 426 ? 6.238   -12.403 45.888  1 31.778  ? 418  ASP A N     1 
ATOM   3181 C  CA    . ASP A 1 426 ? 7.503   -12.908 45.367  1 35.765  ? 418  ASP A CA    1 
ATOM   3182 C  C     . ASP A 1 426 ? 8.6     -12.821 46.438  1 41.08   ? 418  ASP A C     1 
ATOM   3183 O  O     . ASP A 1 426 ? 8.911   -13.842 47.068  1 52.908  ? 418  ASP A O     1 
ATOM   3184 C  CB    . ASP A 1 426 ? 7.716   -12.468 43.927  1 33.416  ? 418  ASP A CB    1 
ATOM   3185 C  CG    . ASP A 1 426 ? 8.817   -13.136 43.109  1 32.518  ? 418  ASP A CG    1 
ATOM   3186 O  OD1   . ASP A 1 426 ? 9.829   -13.62  43.678  1 30.555  ? 418  ASP A OD1   1 
ATOM   3187 O  OD2   . ASP A 1 426 ? 8.652   -13.159 41.881  1 34.571  ? 418  ASP A OD2   1 
ATOM   3188 N  N     . GLY A 1 427 ? 9.172   -11.628 46.642  1 39.017  ? 419  GLY A N     1 
ATOM   3189 C  CA    . GLY A 1 427 ? 10.228  -11.44  47.64   1 38.986  ? 419  GLY A CA    1 
ATOM   3190 C  C     . GLY A 1 427 ? 11.643  -11.441 47.05   1 37.848  ? 419  GLY A C     1 
ATOM   3191 O  O     . GLY A 1 427 ? 12.532  -10.842 47.662  1 40.595  ? 419  GLY A O     1 
ATOM   3192 N  N     . ASN A 1 428 ? 11.829  -12.119 45.891  1 35.986  ? 420  ASN A N     1 
ATOM   3193 C  CA    . ASN A 1 428 ? 12.967  -11.941 44.989  1 37.614  ? 420  ASN A CA    1 
ATOM   3194 C  C     . ASN A 1 428 ? 12.916  -10.612 44.221  1 33.816  ? 420  ASN A C     1 
ATOM   3195 O  O     . ASN A 1 428 ? 13.942  -10.201 43.675  1 35.422  ? 420  ASN A O     1 
ATOM   3196 C  CB    . ASN A 1 428 ? 13.196  -13.132 44.057  1 43.007  ? 420  ASN A CB    1 
ATOM   3197 C  CG    . ASN A 1 428 ? 13.576  -14.423 44.751  1 50.712  ? 420  ASN A CG    1 
ATOM   3198 O  OD1   . ASN A 1 428 ? 13.054  -15.479 44.381  1 54.096  ? 420  ASN A OD1   1 
ATOM   3199 N  ND2   . ASN A 1 428 ? 14.504  -14.402 45.701  1 51.354  ? 420  ASN A ND2   1 
ATOM   3200 N  N     . LYS A 1 429 ? 11.731  -9.969  44.15   1 28.184  ? 421  LYS A N     1 
ATOM   3201 C  CA    . LYS A 1 429 ? 11.512  -8.676  43.51   1 28.844  ? 421  LYS A CA    1 
ATOM   3202 C  C     . LYS A 1 429 ? 12.157  -7.573  44.356  1 26.07   ? 421  LYS A C     1 
ATOM   3203 O  O     . LYS A 1 429 ? 12.038  -7.59   45.59   1 24.52   ? 421  LYS A O     1 
ATOM   3204 C  CB    . LYS A 1 429 ? 10.032  -8.272  43.402  1 32.607  ? 421  LYS A CB    1 
ATOM   3205 C  CG    . LYS A 1 429 ? 8.941   -9.195  42.849  1 37.891  ? 421  LYS A CG    1 
ATOM   3206 C  CD    . LYS A 1 429 ? 8.955   -9.779  41.439  1 46.084  ? 421  LYS A CD    1 
ATOM   3207 C  CE    . LYS A 1 429 ? 8.759   -8.836  40.3    1 50.058  ? 421  LYS A CE    1 
ATOM   3208 N  NZ    . LYS A 1 429 ? 9.113   -9.539  39.067  1 55.981  ? 421  LYS A NZ    1 
ATOM   3209 N  N     . ASN A 1 430 ? 12.809  -6.613  43.662  1 23.285  ? 422  ASN A N     1 
ATOM   3210 C  CA    . ASN A 1 430 ? 13.067  -5.25   44.13   1 22.781  ? 422  ASN A CA    1 
ATOM   3211 C  C     . ASN A 1 430 ? 11.798  -4.703  44.814  1 20.557  ? 422  ASN A C     1 
ATOM   3212 O  O     . ASN A 1 430 ? 10.672  -4.962  44.344  1 20.22   ? 422  ASN A O     1 
ATOM   3213 C  CB    . ASN A 1 430 ? 13.648  -4.402  42.989  1 21.991  ? 422  ASN A CB    1 
ATOM   3214 C  CG    . ASN A 1 430 ? 13.709  -2.915  43.286  1 21.501  ? 422  ASN A CG    1 
ATOM   3215 O  OD1   . ASN A 1 430 ? 12.691  -2.211  43.174  1 19.26   ? 422  ASN A OD1   1 
ATOM   3216 N  ND2   . ASN A 1 430 ? 14.875  -2.422  43.685  1 18.109  ? 422  ASN A ND2   1 
ATOM   3217 N  N     . VAL A 1 431 ? 12.006  -3.927  45.89   1 16.411  ? 423  VAL A N     1 
ATOM   3218 C  CA    . VAL A 1 431 ? 10.992  -3.414  46.81   1 17.743  ? 423  VAL A CA    1 
ATOM   3219 C  C     . VAL A 1 431 ? 9.849   -2.682  46.079  1 17.915  ? 423  VAL A C     1 
ATOM   3220 O  O     . VAL A 1 431 ? 8.706   -2.773  46.532  1 16.334  ? 423  VAL A O     1 
ATOM   3221 C  CB    . VAL A 1 431 ? 11.604  -2.642  48.006  1 19.587  ? 423  VAL A CB    1 
ATOM   3222 C  CG1   . VAL A 1 431 ? 12.275  -1.322  47.608  1 20.675  ? 423  VAL A CG1   1 
ATOM   3223 C  CG2   . VAL A 1 431 ? 10.652  -2.432  49.183  1 19.267  ? 423  VAL A CG2   1 
ATOM   3224 N  N     . PHE A 1 432 ? 10.15   -2.018  44.944  1 16.878  ? 424  PHE A N     1 
ATOM   3225 C  CA    . PHE A 1 432 ? 9.175   -1.233  44.184  1 17.641  ? 424  PHE A CA    1 
ATOM   3226 C  C     . PHE A 1 432 ? 8.329   -2.07   43.219  1 17.1    ? 424  PHE A C     1 
ATOM   3227 O  O     . PHE A 1 432 ? 7.362   -1.549  42.662  1 16.457  ? 424  PHE A O     1 
ATOM   3228 C  CB    . PHE A 1 432 ? 9.863   -0.065  43.469  1 16.669  ? 424  PHE A CB    1 
ATOM   3229 C  CG    . PHE A 1 432 ? 10.474  0.989   44.378  1 18.966  ? 424  PHE A CG    1 
ATOM   3230 C  CD1   . PHE A 1 432 ? 9.668   1.947   45.022  1 18.825  ? 424  PHE A CD1   1 
ATOM   3231 C  CD2   . PHE A 1 432 ? 11.866  1.031   44.569  1 18.718  ? 424  PHE A CD2   1 
ATOM   3232 C  CE1   . PHE A 1 432 ? 10.243  2.925   45.843  1 20.243  ? 424  PHE A CE1   1 
ATOM   3233 C  CE2   . PHE A 1 432 ? 12.435  2.001   45.405  1 20.397  ? 424  PHE A CE2   1 
ATOM   3234 C  CZ    . PHE A 1 432 ? 11.626  2.952   46.033  1 20.298  ? 424  PHE A CZ    1 
ATOM   3235 N  N     . GLN A 1 433 ? 8.673   -3.358  43.047  1 17.984  ? 425  GLN A N     1 
ATOM   3236 C  CA    . GLN A 1 433 ? 8.237   -4.174  41.913  1 18.809  ? 425  GLN A CA    1 
ATOM   3237 C  C     . GLN A 1 433 ? 7.32    -5.333  42.318  1 19.596  ? 425  GLN A C     1 
ATOM   3238 O  O     . GLN A 1 433 ? 6.745   -5.969  41.423  1 19.545  ? 425  GLN A O     1 
ATOM   3239 C  CB    . GLN A 1 433 ? 9.42    -4.652  41.068  1 18.714  ? 425  GLN A CB    1 
ATOM   3240 C  CG    . GLN A 1 433 ? 10.28   -3.516  40.519  1 19.368  ? 425  GLN A CG    1 
ATOM   3241 C  CD    . GLN A 1 433 ? 11.302  -3.919  39.485  1 20.4    ? 425  GLN A CD    1 
ATOM   3242 O  OE1   . GLN A 1 433 ? 11.363  -5.064  39.027  1 21.555  ? 425  GLN A OE1   1 
ATOM   3243 N  NE2   . GLN A 1 433 ? 12.128  -2.956  39.102  1 19.189  ? 425  GLN A NE2   1 
ATOM   3244 N  N     . GLY A 1 434 ? 7.182   -5.612  43.631  1 19.991  ? 426  GLY A N     1 
ATOM   3245 C  CA    . GLY A 1 434 ? 6.336   -6.712  44.092  1 20.422  ? 426  GLY A CA    1 
ATOM   3246 C  C     . GLY A 1 434 ? 5.188   -6.297  45.008  1 20.667  ? 426  GLY A C     1 
ATOM   3247 O  O     . GLY A 1 434 ? 4.7     -7.144  45.762  1 22.041  ? 426  GLY A O     1 
ATOM   3248 N  N     . LEU A 1 435 ? 4.763   -5.022  44.924  1 17.562  ? 427  LEU A N     1 
ATOM   3249 C  CA    . LEU A 1 435 ? 3.824   -4.441  45.875  1 17.348  ? 427  LEU A CA    1 
ATOM   3250 C  C     . LEU A 1 435 ? 2.393   -4.826  45.473  1 17.475  ? 427  LEU A C     1 
ATOM   3251 O  O     . LEU A 1 435 ? 1.809   -4.253  44.546  1 18.026  ? 427  LEU A O     1 
ATOM   3252 C  CB    . LEU A 1 435 ? 4.065   -2.942  46.092  1 16.032  ? 427  LEU A CB    1 
ATOM   3253 C  CG    . LEU A 1 435 ? 5.427   -2.519  46.661  1 14.499  ? 427  LEU A CG    1 
ATOM   3254 C  CD1   . LEU A 1 435 ? 5.724   -1.047  46.265  1 12.756  ? 427  LEU A CD1   1 
ATOM   3255 C  CD2   . LEU A 1 435 ? 5.615   -2.762  48.19   1 12.067  ? 427  LEU A CD2   1 
ATOM   3256 N  N     . ASN A 1 436 ? 1.871   -5.865  46.145  1 17.461  ? 428  ASN A N     1 
ATOM   3257 C  CA    . ASN A 1 436 ? 0.639   -6.55   45.746  1 17.606  ? 428  ASN A CA    1 
ATOM   3258 C  C     . ASN A 1 436 ? -0.429  -6.461  46.834  1 18.089  ? 428  ASN A C     1 
ATOM   3259 O  O     . ASN A 1 436 ? -1.431  -7.191  46.777  1 19.334  ? 428  ASN A O     1 
ATOM   3260 C  CB    . ASN A 1 436 ? 0.926   -7.949  45.204  1 17.509  ? 428  ASN A CB    1 
ATOM   3261 C  CG    . ASN A 1 436 ? 1.357   -8.971  46.238  1 18.267  ? 428  ASN A CG    1 
ATOM   3262 O  OD1   . ASN A 1 436 ? 1.743   -8.661  47.374  1 18.673  ? 428  ASN A OD1   1 
ATOM   3263 N  ND2   . ASN A 1 436 ? 1.292   -10.229 45.844  1 18.579  ? 428  ASN A ND2   1 
ATOM   3264 N  N     . GLY A 1 437 ? -0.187  -5.598  47.826  1 17.494  ? 429  GLY A N     1 
ATOM   3265 C  CA    . GLY A 1 437 ? -1.141  -5.38   48.895  1 18.283  ? 429  GLY A CA    1 
ATOM   3266 C  C     . GLY A 1 437 ? -0.954  -4.09   49.679  1 17.405  ? 429  GLY A C     1 
ATOM   3267 O  O     . GLY A 1 437 ? -0.056  -3.285  49.407  1 16.099  ? 429  GLY A O     1 
ATOM   3268 N  N     . LEU A 1 438 ? -1.858  -3.966  50.66   1 17.333  ? 430  LEU A N     1 
ATOM   3269 C  CA    . LEU A 1 438 ? -1.936  -2.869  51.609  1 17.252  ? 430  LEU A CA    1 
ATOM   3270 C  C     . LEU A 1 438 ? -2.004  -3.454  53.019  1 19.765  ? 430  LEU A C     1 
ATOM   3271 O  O     . LEU A 1 438 ? -2.608  -4.517  53.232  1 21.675  ? 430  LEU A O     1 
ATOM   3272 C  CB    . LEU A 1 438 ? -3.081  -1.887  51.325  1 15.283  ? 430  LEU A CB    1 
ATOM   3273 C  CG    . LEU A 1 438 ? -3.192  -1.24   49.933  1 14.502  ? 430  LEU A CG    1 
ATOM   3274 C  CD1   . LEU A 1 438 ? -4.443  -0.422  49.917  1 13.632  ? 430  LEU A CD1   1 
ATOM   3275 C  CD2   . LEU A 1 438 ? -2.053  -0.301  49.528  1 14.004  ? 430  LEU A CD2   1 
ATOM   3276 N  N     . ALA A 1 439 ? -1.358  -2.732  53.95   1 17.273  ? 431  ALA A N     1 
ATOM   3277 C  CA    . ALA A 1 439 ? -1.427  -2.947  55.382  1 17.865  ? 431  ALA A CA    1 
ATOM   3278 C  C     . ALA A 1 439 ? -1.959  -1.697  56.083  1 17.974  ? 431  ALA A C     1 
ATOM   3279 O  O     . ALA A 1 439 ? -1.562  -0.568  55.761  1 18.165  ? 431  ALA A O     1 
ATOM   3280 C  CB    . ALA A 1 439 ? -0.074  -3.378  55.913  1 17.006  ? 431  ALA A CB    1 
ATOM   3281 N  N     . HIS A 1 440 ? -2.915  -1.934  56.995  1 18.445  ? 432  HIS A N     1 
ATOM   3282 C  CA    . HIS A 1 440 ? -3.317  -0.954  57.987  1 17.312  ? 432  HIS A CA    1 
ATOM   3283 C  C     . HIS A 1 440 ? -2.75   -1.391  59.326  1 17.307  ? 432  HIS A C     1 
ATOM   3284 O  O     . HIS A 1 440 ? -3.286  -2.311  59.958  1 17.236  ? 432  HIS A O     1 
ATOM   3285 C  CB    . HIS A 1 440 ? -4.823  -0.672  57.983  1 16.258  ? 432  HIS A CB    1 
ATOM   3286 C  CG    . HIS A 1 440 ? -5.268  0.427   58.892  1 16.357  ? 432  HIS A CG    1 
ATOM   3287 N  ND1   . HIS A 1 440 ? -6.617  0.635   59.112  1 15.755  ? 432  HIS A ND1   1 
ATOM   3288 C  CD2   . HIS A 1 440 ? -4.625  1.392   59.582  1 16.114  ? 432  HIS A CD2   1 
ATOM   3289 C  CE1   . HIS A 1 440 ? -6.771  1.694   59.89   1 16.504  ? 432  HIS A CE1   1 
ATOM   3290 N  NE2   . HIS A 1 440 ? -5.57   2.167   60.194  1 16.766  ? 432  HIS A NE2   1 
ATOM   3291 N  N     . TYR A 1 441 ? -1.671  -0.685  59.706  1 17.973  ? 433  TYR A N     1 
ATOM   3292 C  CA    . TYR A 1 441 ? -1.007  -0.809  60.998  1 17.834  ? 433  TYR A CA    1 
ATOM   3293 C  C     . TYR A 1 441 ? -1.567  0.254   61.937  1 19.028  ? 433  TYR A C     1 
ATOM   3294 O  O     . TYR A 1 441 ? -1.712  1.412   61.54   1 20.051  ? 433  TYR A O     1 
ATOM   3295 C  CB    . TYR A 1 441 ? 0.519   -0.747  60.827  1 17.534  ? 433  TYR A CB    1 
ATOM   3296 C  CG    . TYR A 1 441 ? 1.297   -0.694  62.138  1 16.688  ? 433  TYR A CG    1 
ATOM   3297 C  CD1   . TYR A 1 441 ? 1.474   -1.843  62.931  1 15.72   ? 433  TYR A CD1   1 
ATOM   3298 C  CD2   . TYR A 1 441 ? 1.852   0.519   62.581  1 17.397  ? 433  TYR A CD2   1 
ATOM   3299 C  CE1   . TYR A 1 441 ? 2.183   -1.788  64.132  1 16.374  ? 433  TYR A CE1   1 
ATOM   3300 C  CE2   . TYR A 1 441 ? 2.569   0.583   63.777  1 17.266  ? 433  TYR A CE2   1 
ATOM   3301 C  CZ    . TYR A 1 441 ? 2.722   -0.573  64.552  1 16.417  ? 433  TYR A CZ    1 
ATOM   3302 O  OH    . TYR A 1 441 ? 3.422   -0.486  65.719  1 17.465  ? 433  TYR A OH    1 
ATOM   3303 N  N     . LYS A 1 442 ? -1.834  -0.167  63.186  1 19.943  ? 434  LYS A N     1 
ATOM   3304 C  CA    . LYS A 1 442 ? -2.207  0.707   64.293  1 19.956  ? 434  LYS A CA    1 
ATOM   3305 C  C     . LYS A 1 442 ? -1.225  0.469   65.437  1 21.398  ? 434  LYS A C     1 
ATOM   3306 O  O     . LYS A 1 442 ? -1.219  -0.622  66.009  1 20.423  ? 434  LYS A O     1 
ATOM   3307 C  CB    . LYS A 1 442 ? -3.659  0.473   64.733  1 20.428  ? 434  LYS A CB    1 
ATOM   3308 C  CG    . LYS A 1 442 ? -4.755  0.867   63.748  1 21.487  ? 434  LYS A CG    1 
ATOM   3309 C  CD    . LYS A 1 442 ? -6.133  0.494   64.274  1 20.829  ? 434  LYS A CD    1 
ATOM   3310 C  CE    . LYS A 1 442 ? -7.147  0.864   63.259  1 20.98   ? 434  LYS A CE    1 
ATOM   3311 N  NZ    . LYS A 1 442 ? -8.489  0.761   63.826  1 22.479  ? 434  LYS A NZ    1 
ATOM   3312 N  N     . ARG A 1 443 ? -0.412  1.494   65.744  1 22.258  ? 435  ARG A N     1 
ATOM   3313 C  CA    . ARG A 1 443 ? 0.591   1.463   66.806  1 22.733  ? 435  ARG A CA    1 
ATOM   3314 C  C     . ARG A 1 443 ? -0.052  1.191   68.177  1 24.621  ? 435  ARG A C     1 
ATOM   3315 O  O     . ARG A 1 443 ? 0.399   0.266   68.869  1 25.238  ? 435  ARG A O     1 
ATOM   3316 C  CB    . ARG A 1 443 ? 1.559   2.654   66.741  1 20.55   ? 435  ARG A CB    1 
ATOM   3317 C  CG    . ARG A 1 443 ? 2.682   2.612   67.78   1 20.188  ? 435  ARG A CG    1 
ATOM   3318 C  CD    . ARG A 1 443 ? 3.57    3.844   67.813  1 18.836  ? 435  ARG A CD    1 
ATOM   3319 N  NE    . ARG A 1 443 ? 2.826   5.092   68.021  1 18.6    ? 435  ARG A NE    1 
ATOM   3320 C  CZ    . ARG A 1 443 ? 2.229   5.561   69.12   1 20.196  ? 435  ARG A CZ    1 
ATOM   3321 N  NH1   . ARG A 1 443 ? 2.399   5.01    70.316  1 19.864  ? 435  ARG A NH1   1 
ATOM   3322 N  NH2   . ARG A 1 443 ? 1.464   6.635   69.016  1 20.41   ? 435  ARG A NH2   1 
ATOM   3323 N  N     . LYS A 1 444 ? -1.101  1.965   68.525  1 24.233  ? 436  LYS A N     1 
ATOM   3324 C  CA    . LYS A 1 444 ? -1.773  1.936   69.826  1 26.607  ? 436  LYS A CA    1 
ATOM   3325 C  C     . LYS A 1 444 ? -2.345  0.544   70.112  1 29.165  ? 436  LYS A C     1 
ATOM   3326 O  O     . LYS A 1 444 ? -2.036  -0.015  71.163  1 30.395  ? 436  LYS A O     1 
ATOM   3327 C  CB    . LYS A 1 444 ? -2.743  3.108   70.022  1 28.496  ? 436  LYS A CB    1 
ATOM   3328 C  CG    . LYS A 1 444 ? -1.998  4.417   70.322  1 32.511  ? 436  LYS A CG    1 
ATOM   3329 C  CD    . LYS A 1 444 ? -2.849  5.673   70.223  1 34.701  ? 436  LYS A CD    1 
ATOM   3330 C  CE    . LYS A 1 444 ? -2.113  6.864   70.732  1 37.127  ? 436  LYS A CE    1 
ATOM   3331 N  NZ    . LYS A 1 444 ? -3      8.026   70.65   1 34.978  ? 436  LYS A NZ    1 
ATOM   3332 N  N     . GLU A 1 445 ? -3.078  -0.02   69.137  1 26.372  ? 437  GLU A N     1 
ATOM   3333 C  CA    . GLU A 1 445 ? -3.665  -1.357  69.2    1 27.973  ? 437  GLU A CA    1 
ATOM   3334 C  C     . GLU A 1 445 ? -2.612  -2.455  69.021  1 27.656  ? 437  GLU A C     1 
ATOM   3335 O  O     . GLU A 1 445 ? -2.812  -3.552  69.531  1 28.336  ? 437  GLU A O     1 
ATOM   3336 C  CB    . GLU A 1 445 ? -4.875  -1.56   68.281  1 28.804  ? 437  GLU A CB    1 
ATOM   3337 C  CG    . GLU A 1 445 ? -6.104  -0.718  68.636  1 27.205  ? 437  GLU A CG    1 
ATOM   3338 C  CD    . GLU A 1 445 ? -6.139  0.764   68.259  1 29.73   ? 437  GLU A CD    1 
ATOM   3339 O  OE1   . GLU A 1 445 ? -5.15   1.357   67.757  1 31.613  ? 437  GLU A OE1   1 
ATOM   3340 O  OE2   . GLU A 1 445 ? -7.212  1.355   68.47   1 30.759  ? 437  GLU A OE2   1 
ATOM   3341 N  N     . GLY A 1 446 ? -1.506  -2.164  68.307  1 27.559  ? 438  GLY A N     1 
ATOM   3342 C  CA    . GLY A 1 446 ? -0.505  -3.142  67.89   1 26.123  ? 438  GLY A CA    1 
ATOM   3343 C  C     . GLY A 1 446 ? -1.042  -4.172  66.889  1 27.393  ? 438  GLY A C     1 
ATOM   3344 O  O     . GLY A 1 446 ? -0.551  -5.3    66.865  1 29.913  ? 438  GLY A O     1 
ATOM   3345 N  N     . THR A 1 447 ? -2.024  -3.775  66.058  1 26.072  ? 439  THR A N     1 
ATOM   3346 C  CA    . THR A 1 447 ? -2.709  -4.641  65.097  1 26.352  ? 439  THR A CA    1 
ATOM   3347 C  C     . THR A 1 447 ? -2.275  -4.273  63.675  1 25.22   ? 439  THR A C     1 
ATOM   3348 O  O     . THR A 1 447 ? -1.995  -3.096  63.401  1 24.794  ? 439  THR A O     1 
ATOM   3349 C  CB    . THR A 1 447 ? -4.239  -4.616  65.251  1 26.48   ? 439  THR A CB    1 
ATOM   3350 O  OG1   . THR A 1 447 ? -4.72   -3.297  65.005  1 27.86   ? 439  THR A OG1   1 
ATOM   3351 C  CG2   . THR A 1 447 ? -4.759  -5.129  66.586  1 25.946  ? 439  THR A CG2   1 
ATOM   3352 N  N     . THR A 1 448 ? -2.227  -5.298  62.799  1 23.138  ? 440  THR A N     1 
ATOM   3353 C  CA    . THR A 1 448 ? -2.08   -5.131  61.356  1 24.246  ? 440  THR A CA    1 
ATOM   3354 C  C     . THR A 1 448 ? -3.19   -5.899  60.63   1 24.488  ? 440  THR A C     1 
ATOM   3355 O  O     . THR A 1 448 ? -3.372  -7.096  60.875  1 23.006  ? 440  THR A O     1 
ATOM   3356 C  CB    . THR A 1 448 ? -0.672  -5.489  60.852  1 23.342  ? 440  THR A CB    1 
ATOM   3357 O  OG1   . THR A 1 448 ? 0.295   -4.798  61.632  1 23.095  ? 440  THR A OG1   1 
ATOM   3358 C  CG2   . THR A 1 448 ? -0.409  -5.003  59.435  1 23.046  ? 440  THR A CG2   1 
ATOM   3359 N  N     . GLU A 1 449 ? -3.863  -5.185  59.705  1 22.904  ? 441  GLU A N     1 
ATOM   3360 C  CA    . GLU A 1 449 ? -4.866  -5.711  58.776  1 22.603  ? 441  GLU A CA    1 
ATOM   3361 C  C     . GLU A 1 449 ? -4.345  -5.633  57.34   1 21.249  ? 441  GLU A C     1 
ATOM   3362 O  O     . GLU A 1 449 ? -3.621  -4.689  56.994  1 21.457  ? 441  GLU A O     1 
ATOM   3363 C  CB    . GLU A 1 449 ? -6.175  -4.94   58.942  1 23.892  ? 441  GLU A CB    1 
ATOM   3364 C  CG    . GLU A 1 449 ? -6.911  -5.212  60.254  1 27.094  ? 441  GLU A CG    1 
ATOM   3365 C  CD    . GLU A 1 449 ? -7.922  -4.131  60.581  1 31.078  ? 441  GLU A CD    1 
ATOM   3366 O  OE1   . GLU A 1 449 ? -9.108  -4.388  60.291  1 32.761  ? 441  GLU A OE1   1 
ATOM   3367 O  OE2   . GLU A 1 449 ? -7.536  -3.043  61.094  1 33.297  ? 441  GLU A OE2   1 
ATOM   3368 N  N     . TRP A 1 450 ? -4.782  -6.594  56.508  1 20.427  ? 442  TRP A N     1 
ATOM   3369 C  CA    . TRP A 1 450 ? -4.197  -6.855  55.195  1 20.897  ? 442  TRP A CA    1 
ATOM   3370 C  C     . TRP A 1 450 ? -5.255  -6.817  54.094  1 20.968  ? 442  TRP A C     1 
ATOM   3371 O  O     . TRP A 1 450 ? -6.316  -7.407  54.267  1 20.137  ? 442  TRP A O     1 
ATOM   3372 C  CB    . TRP A 1 450 ? -3.388  -8.163  55.162  1 20.635  ? 442  TRP A CB    1 
ATOM   3373 C  CG    . TRP A 1 450 ? -2.358  -8.271  56.262  1 20.826  ? 442  TRP A CG    1 
ATOM   3374 C  CD1   . TRP A 1 450 ? -2.572  -8.748  57.521  1 20.709  ? 442  TRP A CD1   1 
ATOM   3375 C  CD2   . TRP A 1 450 ? -0.967  -7.876  56.207  1 21.083  ? 442  TRP A CD2   1 
ATOM   3376 N  NE1   . TRP A 1 450 ? -1.421  -8.677  58.256  1 21.589  ? 442  TRP A NE1   1 
ATOM   3377 C  CE2   . TRP A 1 450 ? -0.414  -8.161  57.485  1 21.22   ? 442  TRP A CE2   1 
ATOM   3378 C  CE3   . TRP A 1 450 ? -0.132  -7.32   55.212  1 20.698  ? 442  TRP A CE3   1 
ATOM   3379 C  CZ2   . TRP A 1 450 ? 0.935   -7.915  57.799  1 21.265  ? 442  TRP A CZ2   1 
ATOM   3380 C  CZ3   . TRP A 1 450 ? 1.198   -7.061  55.526  1 23.185  ? 442  TRP A CZ3   1 
ATOM   3381 C  CH2   . TRP A 1 450 ? 1.723   -7.355  56.805  1 22.237  ? 442  TRP A CH2   1 
ATOM   3382 N  N     . TYR A 1 451 ? -4.942  -6.071  53.01   1 19.897  ? 443  TYR A N     1 
ATOM   3383 C  CA    . TYR A 1 451 ? -5.676  -6.055  51.75   1 19.164  ? 443  TYR A CA    1 
ATOM   3384 C  C     . TYR A 1 451 ? -4.792  -6.668  50.665  1 19.163  ? 443  TYR A C     1 
ATOM   3385 O  O     . TYR A 1 451 ? -3.684  -6.188  50.441  1 19.319  ? 443  TYR A O     1 
ATOM   3386 C  CB    . TYR A 1 451 ? -6.235  -4.683  51.341  1 18.132  ? 443  TYR A CB    1 
ATOM   3387 C  CG    . TYR A 1 451 ? -6.999  -4.72   50.013  1 18.557  ? 443  TYR A CG    1 
ATOM   3388 C  CD1   . TYR A 1 451 ? -8.342  -5.133  49.965  1 17.255  ? 443  TYR A CD1   1 
ATOM   3389 C  CD2   . TYR A 1 451 ? -6.375  -4.361  48.799  1 17.052  ? 443  TYR A CD2   1 
ATOM   3390 C  CE1   . TYR A 1 451 ? -9.048  -5.195  48.758  1 16.446  ? 443  TYR A CE1   1 
ATOM   3391 C  CE2   . TYR A 1 451 ? -7.072  -4.429  47.588  1 17.492  ? 443  TYR A CE2   1 
ATOM   3392 C  CZ    . TYR A 1 451 ? -8.404  -4.856  47.571  1 17.211  ? 443  TYR A CZ    1 
ATOM   3393 O  OH    . TYR A 1 451 ? -9.09   -4.915  46.383  1 18.452  ? 443  TYR A OH    1 
ATOM   3394 N  N     . TYR A 1 452 ? -5.33   -7.677  49.96   1 20.248  ? 444  TYR A N     1 
ATOM   3395 C  CA    . TYR A 1 452 ? -4.66   -8.295  48.822  1 19.705  ? 444  TYR A CA    1 
ATOM   3396 C  C     . TYR A 1 452 ? -5.204  -7.712  47.517  1 20.988  ? 444  TYR A C     1 
ATOM   3397 O  O     . TYR A 1 452 ? -6.416  -7.727  47.335  1 23.497  ? 444  TYR A O     1 
ATOM   3398 C  CB    . TYR A 1 452 ? -4.747  -9.821  48.946  1 17.075  ? 444  TYR A CB    1 
ATOM   3399 C  CG    . TYR A 1 452 ? -4.18   -10.604 47.766  1 14.954  ? 444  TYR A CG    1 
ATOM   3400 C  CD1   . TYR A 1 452 ? -2.802  -10.588 47.473  1 15.75   ? 444  TYR A CD1   1 
ATOM   3401 C  CD2   . TYR A 1 452 ? -5.022  -11.391 46.963  1 14.525  ? 444  TYR A CD2   1 
ATOM   3402 C  CE1   . TYR A 1 452 ? -2.276  -11.321 46.408  1 16.14   ? 444  TYR A CE1   1 
ATOM   3403 C  CE2   . TYR A 1 452 ? -4.502  -12.162 45.923  1 15.115  ? 444  TYR A CE2   1 
ATOM   3404 C  CZ    . TYR A 1 452 ? -3.133  -12.111 45.639  1 16.658  ? 444  TYR A CZ    1 
ATOM   3405 O  OH    . TYR A 1 452 ? -2.611  -12.843 44.618  1 17.692  ? 444  TYR A OH    1 
ATOM   3406 N  N     . ALA A 1 453 ? -4.307  -7.232  46.622  1 20.653  ? 445  ALA A N     1 
ATOM   3407 C  CA    . ALA A 1 453 ? -4.685  -6.578  45.364  1 20.759  ? 445  ALA A CA    1 
ATOM   3408 C  C     . ALA A 1 453 ? -5.367  -7.528  44.379  1 20.937  ? 445  ALA A C     1 
ATOM   3409 O  O     . ALA A 1 453 ? -6.193  -7.047  43.608  1 20.944  ? 445  ALA A O     1 
ATOM   3410 C  CB    . ALA A 1 453 ? -3.531  -5.879  44.687  1 18.807  ? 445  ALA A CB    1 
ATOM   3411 N  N     . GLY A 1 454 ? -5.04   -8.837  44.433  1 20.254  ? 446  GLY A N     1 
ATOM   3412 C  CA    . GLY A 1 454 ? -5.537  -9.855  43.512  1 20.292  ? 446  GLY A CA    1 
ATOM   3413 C  C     . GLY A 1 454 ? -4.395  -10.58  42.801  1 22.887  ? 446  GLY A C     1 
ATOM   3414 O  O     . GLY A 1 454 ? -3.27   -10.068 42.776  1 19.872  ? 446  GLY A O     1 
ATOM   3415 N  N     . ASP A 1 455 ? -4.677  -11.791 42.273  1 25.011  ? 447  ASP A N     1 
ATOM   3416 C  CA    . ASP A 1 455 ? -3.749  -12.533 41.417  1 25.472  ? 447  ASP A CA    1 
ATOM   3417 C  C     . ASP A 1 455 ? -3.509  -11.745 40.13   1 25.687  ? 447  ASP A C     1 
ATOM   3418 O  O     . ASP A 1 455 ? -4.458  -11.17  39.599  1 28.323  ? 447  ASP A O     1 
ATOM   3419 C  CB    . ASP A 1 455 ? -4.243  -13.937 41.082  1 24.359  ? 447  ASP A CB    1 
ATOM   3420 C  CG    . ASP A 1 455 ? -4.332  -14.993 42.183  1 23.925  ? 447  ASP A CG    1 
ATOM   3421 O  OD1   . ASP A 1 455 ? -4.163  -14.693 43.404  1 22.792  ? 447  ASP A OD1   1 
ATOM   3422 O  OD2   . ASP A 1 455 ? -4.592  -16.14  41.804  1 22.718  ? 447  ASP A OD2   1 
ATOM   3423 N  N     . ASN A 1 456 ? -2.231  -11.685 39.697  1 26.207  ? 448  ASN A N     1 
ATOM   3424 C  CA    . ASN A 1 456 ? -1.729  -10.941 38.534  1 29.144  ? 448  ASN A CA    1 
ATOM   3425 C  C     . ASN A 1 456 ? -2.051  -9.439  38.654  1 25.041  ? 448  ASN A C     1 
ATOM   3426 O  O     . ASN A 1 456 ? -2.407  -8.782  37.66   1 22.676  ? 448  ASN A O     1 
ATOM   3427 C  CB    . ASN A 1 456 ? -2.184  -11.541 37.191  1 34.534  ? 448  ASN A CB    1 
ATOM   3428 C  CG    . ASN A 1 456 ? -2.063  -13.043 37.082  1 39.883  ? 448  ASN A CG    1 
ATOM   3429 O  OD1   . ASN A 1 456 ? -3.07   -13.757 37.191  1 42.413  ? 448  ASN A OD1   1 
ATOM   3430 N  ND2   . ASN A 1 456 ? -0.852  -13.535 36.864  1 40.253  ? 448  ASN A ND2   1 
ATOM   3431 N  N     . CYS A 1 457 ? -1.986  -8.924  39.899  1 22.829  ? 449  CYS A N     1 
ATOM   3432 C  CA    . CYS A 1 457 ? -2.274  -7.535  40.232  1 21.594  ? 449  CYS A CA    1 
ATOM   3433 C  C     . CYS A 1 457 ? -1.15   -6.958  41.078  1 19.392  ? 449  CYS A C     1 
ATOM   3434 O  O     . CYS A 1 457 ? -0.588  -7.648  41.922  1 18.289  ? 449  CYS A O     1 
ATOM   3435 C  CB    . CYS A 1 457 ? -3.604  -7.332  40.956  1 19.048  ? 449  CYS A CB    1 
ATOM   3436 S  SG    . CYS A 1 457 ? -5.085  -7.863  40.051  1 22.077  ? 449  CYS A SG    1 
ATOM   3437 N  N     . LEU A 1 458 ? -0.883  -5.675  40.833  1 19.888  ? 450  LEU A N     1 
ATOM   3438 C  CA    . LEU A 1 458 ? -0.102  -4.814  41.706  1 18.161  ? 450  LEU A CA    1 
ATOM   3439 C  C     . LEU A 1 458 ? -1.007  -3.699  42.202  1 18.899  ? 450  LEU A C     1 
ATOM   3440 O  O     . LEU A 1 458 ? -2.002  -3.379  41.543  1 20.592  ? 450  LEU A O     1 
ATOM   3441 C  CB    . LEU A 1 458 ? 1.163   -4.269  41.024  1 17.956  ? 450  LEU A CB    1 
ATOM   3442 C  CG    . LEU A 1 458 ? 2.197   -5.269  40.479  1 17.408  ? 450  LEU A CG    1 
ATOM   3443 C  CD1   . LEU A 1 458 ? 3.143   -4.508  39.552  1 16.627  ? 450  LEU A CD1   1 
ATOM   3444 C  CD2   . LEU A 1 458 ? 2.985   -6.031  41.561  1 18.188  ? 450  LEU A CD2   1 
ATOM   3445 N  N     . ILE A 1 459 ? -0.647  -3.148  43.375  1 18.587  ? 451  ILE A N     1 
ATOM   3446 C  CA    . ILE A 1 459 ? -1.295  -1.983  43.976  1 18.29   ? 451  ILE A CA    1 
ATOM   3447 C  C     . ILE A 1 459 ? -0.243  -0.926  44.338  1 17.818  ? 451  ILE A C     1 
ATOM   3448 O  O     . ILE A 1 459 ? 0.872   -1.257  44.734  1 17.536  ? 451  ILE A O     1 
ATOM   3449 C  CB    . ILE A 1 459 ? -2.246  -2.389  45.127  1 16.74   ? 451  ILE A CB    1 
ATOM   3450 C  CG1   . ILE A 1 459 ? -3.291  -1.313  45.481  1 15.584  ? 451  ILE A CG1   1 
ATOM   3451 C  CG2   . ILE A 1 459 ? -1.473  -2.871  46.354  1 17.574  ? 451  ILE A CG2   1 
ATOM   3452 C  CD1   . ILE A 1 459 ? -4.454  -1.792  46.355  1 16.483  ? 451  ILE A CD1   1 
ATOM   3453 N  N     . GLN A 1 460 ? -0.641  0.339   44.187  1 16.274  ? 452  GLN A N     1 
ATOM   3454 C  CA    . GLN A 1 460 ? 0.203   1.501   44.401  1 16.209  ? 452  GLN A CA    1 
ATOM   3455 C  C     . GLN A 1 460 ? -0.136  2.124   45.756  1 17.648  ? 452  GLN A C     1 
ATOM   3456 O  O     . GLN A 1 460 ? -0.979  1.575   46.494  1 20.114  ? 452  GLN A O     1 
ATOM   3457 C  CB    . GLN A 1 460 ? 0.015   2.363   43.152  1 14.622  ? 452  GLN A CB    1 
ATOM   3458 C  CG    . GLN A 1 460 ? 0.626   1.778   41.878  1 13.574  ? 452  GLN A CG    1 
ATOM   3459 C  CD    . GLN A 1 460 ? 0.124   2.447   40.622  1 13.156  ? 452  GLN A CD    1 
ATOM   3460 O  OE1   . GLN A 1 460 ? 0.2     3.674   40.469  1 13.318  ? 452  GLN A OE1   1 
ATOM   3461 N  NE2   . GLN A 1 460 ? -0.383  1.635   39.697  1 12.76   ? 452  GLN A NE2   1 
ATOM   3462 N  N     . GLU A 1 461 ? 0.516   3.267   46.057  1 16.549  ? 453  GLU A N     1 
ATOM   3463 C  CA    . GLU A 1 461 ? 0.468   3.979   47.332  1 16.523  ? 453  GLU A CA    1 
ATOM   3464 C  C     . GLU A 1 461 ? -0.974  4.261   47.793  1 15.417  ? 453  GLU A C     1 
ATOM   3465 O  O     . GLU A 1 461 ? -1.745  4.883   47.042  1 16.331  ? 453  GLU A O     1 
ATOM   3466 C  CB    . GLU A 1 461 ? 1.281   5.267   47.25   1 14.849  ? 453  GLU A CB    1 
ATOM   3467 C  CG    . GLU A 1 461 ? 1.229   6.097   48.535  1 15.983  ? 453  GLU A CG    1 
ATOM   3468 C  CD    . GLU A 1 461 ? 1.755   7.496   48.316  1 16.446  ? 453  GLU A CD    1 
ATOM   3469 O  OE1   . GLU A 1 461 ? 1.259   8.167   47.399  1 16.98   ? 453  GLU A OE1   1 
ATOM   3470 O  OE2   . GLU A 1 461 ? 2.623   7.934   49.091  1 17.371  ? 453  GLU A OE2   1 
ATOM   3471 N  N     . PRO A 1 462 ? -1.358  3.877   49.045  1 14.788  ? 454  PRO A N     1 
ATOM   3472 C  CA    . PRO A 1 462 ? -2.662  4.248   49.588  1 14.606  ? 454  PRO A CA    1 
ATOM   3473 C  C     . PRO A 1 462 ? -2.732  5.722   50.002  1 14.574  ? 454  PRO A C     1 
ATOM   3474 O  O     . PRO A 1 462 ? -1.722  6.325   50.376  1 14.063  ? 454  PRO A O     1 
ATOM   3475 C  CB    . PRO A 1 462 ? -2.879  3.237   50.706  1 13.405  ? 454  PRO A CB    1 
ATOM   3476 C  CG    . PRO A 1 462 ? -1.447  3.048   51.228  1 12.937  ? 454  PRO A CG    1 
ATOM   3477 C  CD    . PRO A 1 462 ? -0.558  3.119   50.032  1 13.891  ? 454  PRO A CD    1 
ATOM   3478 N  N     . VAL A 1 463 ? -3.946  6.271   49.91   1 14.339  ? 455  VAL A N     1 
ATOM   3479 C  CA    . VAL A 1 463 ? -4.327  7.562   50.479  1 15.381  ? 455  VAL A CA    1 
ATOM   3480 C  C     . VAL A 1 463 ? -5.578  7.349   51.348  1 16.512  ? 455  VAL A C     1 
ATOM   3481 O  O     . VAL A 1 463 ? -6.403  6.475   51.041  1 16.394  ? 455  VAL A O     1 
ATOM   3482 C  CB    . VAL A 1 463 ? -4.491  8.713   49.449  1 14.344  ? 455  VAL A CB    1 
ATOM   3483 C  CG1   . VAL A 1 463 ? -3.213  8.967   48.645  1 13.08   ? 455  VAL A CG1   1 
ATOM   3484 C  CG2   . VAL A 1 463 ? -5.657  8.52    48.482  1 14.833  ? 455  VAL A CG2   1 
ATOM   3485 N  N     . PHE A 1 464 ? -5.705  8.17    52.403  1 16.404  ? 456  PHE A N     1 
ATOM   3486 C  CA    . PHE A 1 464 ? -6.804  8.107   53.354  1 17.184  ? 456  PHE A CA    1 
ATOM   3487 C  C     . PHE A 1 464 ? -7.657  9.379   53.308  1 18.216  ? 456  PHE A C     1 
ATOM   3488 O  O     . PHE A 1 464 ? -7.143  10.508  53.256  1 17.359  ? 456  PHE A O     1 
ATOM   3489 C  CB    . PHE A 1 464 ? -6.237  7.715   54.723  1 15.773  ? 456  PHE A CB    1 
ATOM   3490 C  CG    . PHE A 1 464 ? -7.251  7.784   55.86   1 15.113  ? 456  PHE A CG    1 
ATOM   3491 C  CD1   . PHE A 1 464 ? -8.127  6.714   56.107  1 15.043  ? 456  PHE A CD1   1 
ATOM   3492 C  CD2   . PHE A 1 464 ? -7.333  8.932   56.667  1 13.696  ? 456  PHE A CD2   1 
ATOM   3493 C  CE1   . PHE A 1 464 ? -9.07   6.787   57.137  1 14.451  ? 456  PHE A CE1   1 
ATOM   3494 C  CE2   . PHE A 1 464 ? -8.277  9.014   57.684  1 13.468  ? 456  PHE A CE2   1 
ATOM   3495 C  CZ    . PHE A 1 464 ? -9.138  7.933   57.922  1 15.124  ? 456  PHE A CZ    1 
ATOM   3496 N  N     . SER A 1 465 ? -8.978  9.145   53.371  1 20.507  ? 457  SER A N     1 
ATOM   3497 C  CA    . SER A 1 465 ? -10.003 10.157  53.592  1 18.991  ? 457  SER A CA    1 
ATOM   3498 C  C     . SER A 1 465 ? -10.809 9.783   54.839  1 19.416  ? 457  SER A C     1 
ATOM   3499 O  O     . SER A 1 465 ? -11.343 8.662   54.876  1 20.203  ? 457  SER A O     1 
ATOM   3500 C  CB    . SER A 1 465 ? -10.884 10.347  52.369  1 19.406  ? 457  SER A CB    1 
ATOM   3501 O  OG    . SER A 1 465 ? -11.89  11.328  52.598  1 18.586  ? 457  SER A OG    1 
ATOM   3502 N  N     . PRO A 1 466 ? -10.92  10.672  55.877  1 18.313  ? 458  PRO A N     1 
ATOM   3503 C  CA    . PRO A 1 466 ? -11.71  10.357  57.071  1 17.608  ? 458  PRO A CA    1 
ATOM   3504 C  C     . PRO A 1 466 ? -13.203 10.299  56.774  1 18.102  ? 458  PRO A C     1 
ATOM   3505 O  O     . PRO A 1 466 ? -13.658 11.034  55.896  1 18.102  ? 458  PRO A O     1 
ATOM   3506 C  CB    . PRO A 1 466 ? -11.295 11.417  58.095  1 17.251  ? 458  PRO A CB    1 
ATOM   3507 C  CG    . PRO A 1 466 ? -10.897 12.602  57.232  1 18.283  ? 458  PRO A CG    1 
ATOM   3508 C  CD    . PRO A 1 466 ? -10.344 12.04   55.945  1 18.331  ? 458  PRO A CD    1 
ATOM   3509 N  N     . ARG A 1 467 ? -13.923 9.408   57.487  1 18.565  ? 459  ARG A N     1 
ATOM   3510 C  CA    . ARG A 1 467 ? -15.374 9.193   57.375  1 19.691  ? 459  ARG A CA    1 
ATOM   3511 C  C     . ARG A 1 467 ? -16.148 10.51   57.486  1 20.449  ? 459  ARG A C     1 
ATOM   3512 O  O     . ARG A 1 467 ? -17.069 10.74   56.704  1 20.937  ? 459  ARG A O     1 
ATOM   3513 C  CB    . ARG A 1 467 ? -15.921 8.177   58.384  1 18.697  ? 459  ARG A CB    1 
ATOM   3514 C  CG    . ARG A 1 467 ? -17.286 7.591   58.01   1 18.484  ? 459  ARG A CG    1 
ATOM   3515 C  CD    . ARG A 1 467 ? -17.753 6.511   58.98   1 18.793  ? 459  ARG A CD    1 
ATOM   3516 N  NE    . ARG A 1 467 ? -16.799 5.39    59.018  1 19.57   ? 459  ARG A NE    1 
ATOM   3517 C  CZ    . ARG A 1 467 ? -16.53  4.444   58.109  1 19.397  ? 459  ARG A CZ    1 
ATOM   3518 N  NH1   . ARG A 1 467 ? -17.372 4.193   57.109  1 17.459  ? 459  ARG A NH1   1 
ATOM   3519 N  NH2   . ARG A 1 467 ? -15.41  3.732   58.247  1 18.547  ? 459  ARG A NH2   1 
ATOM   3520 N  N     . SER A 1 468 ? -15.753 11.334  58.471  1 21.544  ? 460  SER A N     1 
ATOM   3521 C  CA    . SER A 1 468 ? -16.139 12.727  58.672  1 21.381  ? 460  SER A CA    1 
ATOM   3522 C  C     . SER A 1 468 ? -14.981 13.424  59.392  1 21.251  ? 460  SER A C     1 
ATOM   3523 O  O     . SER A 1 468 ? -14.048 12.755  59.844  1 20.893  ? 460  SER A O     1 
ATOM   3524 C  CB    . SER A 1 468 ? -17.437 12.809  59.451  1 22.032  ? 460  SER A CB    1 
ATOM   3525 O  OG    . SER A 1 468 ? -17.259 12.197  60.723  1 22.719  ? 460  SER A OG    1 
ATOM   3526 N  N     . LYS A 1 469 ? -15.06  14.757  59.504  1 22.783  ? 461  LYS A N     1 
ATOM   3527 C  CA    . LYS A 1 469 ? -14.041 15.644  60.068  1 27.09   ? 461  LYS A CA    1 
ATOM   3528 C  C     . LYS A 1 469 ? -13.622 15.221  61.481  1 25.487  ? 461  LYS A C     1 
ATOM   3529 O  O     . LYS A 1 469 ? -12.422 15.264  61.773  1 25.169  ? 461  LYS A O     1 
ATOM   3530 C  CB    . LYS A 1 469 ? -14.42  17.128  59.945  1 32.175  ? 461  LYS A CB    1 
ATOM   3531 C  CG    . LYS A 1 469 ? -14.624 17.645  58.497  1 47.064  ? 461  LYS A CG    1 
ATOM   3532 C  CD    . LYS A 1 469 ? -13.496 17.782  57.453  1 51.644  ? 461  LYS A CD    1 
ATOM   3533 C  CE    . LYS A 1 469 ? -13.89  18.166  56.043  1 45.382  ? 461  LYS A CE    1 
ATOM   3534 N  NZ    . LYS A 1 469 ? -14.581 19.458  55.905  1 38.672  ? 461  LYS A NZ    1 
ATOM   3535 N  N     . ASP A 1 470 ? -14.586 14.738  62.29   1 23.505  ? 462  ASP A N     1 
ATOM   3536 C  CA    . ASP A 1 470 ? -14.395 14.393  63.696  1 26.453  ? 462  ASP A CA    1 
ATOM   3537 C  C     . ASP A 1 470 ? -14.392 12.878  63.94   1 25.002  ? 462  ASP A C     1 
ATOM   3538 O  O     . ASP A 1 470 ? -14.414 12.463  65.094  1 24.099  ? 462  ASP A O     1 
ATOM   3539 C  CB    . ASP A 1 470 ? -15.292 15.229  64.614  1 32.306  ? 462  ASP A CB    1 
ATOM   3540 C  CG    . ASP A 1 470 ? -15.117 16.745  64.571  1 39.538  ? 462  ASP A CG    1 
ATOM   3541 O  OD1   . ASP A 1 470 ? -13.965 17.231  64.633  1 42.27   ? 462  ASP A OD1   1 
ATOM   3542 O  OD2   . ASP A 1 470 ? -16.149 17.448  64.516  1 47.378  ? 462  ASP A OD2   1 
ATOM   3543 N  N     . ALA A 1 471 ? -14.33  12.054  62.874  1 23.344  ? 463  ALA A N     1 
ATOM   3544 C  CA    . ALA A 1 471 ? -14.206 10.598  62.953  1 20.475  ? 463  ALA A CA    1 
ATOM   3545 C  C     . ALA A 1 471 ? -12.906 10.206  63.68   1 20.009  ? 463  ALA A C     1 
ATOM   3546 O  O     . ALA A 1 471 ? -11.927 10.949  63.523  1 19.132  ? 463  ALA A O     1 
ATOM   3547 C  CB    . ALA A 1 471 ? -14.281 9.983   61.574  1 18.99   ? 463  ALA A CB    1 
ATOM   3548 N  N     . PRO A 1 472 ? -12.83  9.068   64.454  1 19.089  ? 464  PRO A N     1 
ATOM   3549 C  CA    . PRO A 1 472 ? -11.574 8.601   65.058  1 19.391  ? 464  PRO A CA    1 
ATOM   3550 C  C     . PRO A 1 472 ? -10.428 8.437   64.054  1 18.96   ? 464  PRO A C     1 
ATOM   3551 O  O     . PRO A 1 472 ? -10.668 8.316   62.849  1 17.849  ? 464  PRO A O     1 
ATOM   3552 C  CB    . PRO A 1 472 ? -11.905 7.265   65.731  1 19.785  ? 464  PRO A CB    1 
ATOM   3553 C  CG    . PRO A 1 472 ? -13.41  7.284   65.882  1 20.862  ? 464  PRO A CG    1 
ATOM   3554 C  CD    . PRO A 1 472 ? -13.946 8.149   64.776  1 20.928  ? 464  PRO A CD    1 
ATOM   3555 N  N     . GLU A 1 473 ? -9.189  8.503   64.563  1 18.669  ? 465  GLU A N     1 
ATOM   3556 C  CA    . GLU A 1 473 ? -7.988  8.319   63.763  1 18.564  ? 465  GLU A CA    1 
ATOM   3557 C  C     . GLU A 1 473 ? -8.083  7.028   62.951  1 17.959  ? 465  GLU A C     1 
ATOM   3558 O  O     . GLU A 1 473 ? -8.36   5.962   63.514  1 16.288  ? 465  GLU A O     1 
ATOM   3559 C  CB    . GLU A 1 473 ? -6.751  8.287   64.654  1 18.741  ? 465  GLU A CB    1 
ATOM   3560 C  CG    . GLU A 1 473 ? -5.457  8.246   63.838  1 20.072  ? 465  GLU A CG    1 
ATOM   3561 C  CD    . GLU A 1 473 ? -4.137  8.236   64.573  1 20.626  ? 465  GLU A CD    1 
ATOM   3562 O  OE1   . GLU A 1 473 ? -4.144  8.449   65.812  1 19.551  ? 465  GLU A OE1   1 
ATOM   3563 O  OE2   . GLU A 1 473 ? -3.108  8.003   63.869  1 21.037  ? 465  GLU A OE2   1 
ATOM   3564 N  N     . GLY A 1 474 ? -7.876  7.179   61.63   1 18.513  ? 466  GLY A N     1 
ATOM   3565 C  CA    . GLY A 1 474 ? -7.806  6.063   60.692  1 20.131  ? 466  GLY A CA    1 
ATOM   3566 C  C     . GLY A 1 474 ? -9.16   5.405   60.423  1 21.495  ? 466  GLY A C     1 
ATOM   3567 O  O     . GLY A 1 474 ? -9.183  4.289   59.896  1 23.444  ? 466  GLY A O     1 
ATOM   3568 N  N     . ASP A 1 475 ? -10.257 6.116   60.744  1 20.384  ? 467  ASP A N     1 
ATOM   3569 C  CA    . ASP A 1 475 ? -11.616 5.707   60.419  1 20.037  ? 467  ASP A CA    1 
ATOM   3570 C  C     . ASP A 1 475 ? -12.099 6.451   59.172  1 17.784  ? 467  ASP A C     1 
ATOM   3571 O  O     . ASP A 1 475 ? -12.303 7.669   59.199  1 18.485  ? 467  ASP A O     1 
ATOM   3572 C  CB    . ASP A 1 475 ? -12.56  5.763   61.615  1 19.703  ? 467  ASP A CB    1 
ATOM   3573 C  CG    . ASP A 1 475 ? -13.98  5.319   61.273  1 21.403  ? 467  ASP A CG    1 
ATOM   3574 O  OD1   . ASP A 1 475 ? -14.167 4.122   60.945  1 21.686  ? 467  ASP A OD1   1 
ATOM   3575 O  OD2   . ASP A 1 475 ? -14.86  6.188   61.236  1 21.5    ? 467  ASP A OD2   1 
ATOM   3576 N  N     . GLY A 1 476 ? -12.276 5.681   58.094  1 16.376  ? 468  GLY A N     1 
ATOM   3577 C  CA    . GLY A 1 476 ? -12.769 6.194   56.832  1 16.044  ? 468  GLY A CA    1 
ATOM   3578 C  C     . GLY A 1 476 ? -12.45  5.244   55.693  1 16.066  ? 468  GLY A C     1 
ATOM   3579 O  O     . GLY A 1 476 ? -12.674 4.022   55.804  1 15.153  ? 468  GLY A O     1 
ATOM   3580 N  N     . PHE A 1 477 ? -11.904 5.862   54.632  1 15.86   ? 469  PHE A N     1 
ATOM   3581 C  CA    . PHE A 1 477 ? -11.772 5.267   53.308  1 16.158  ? 469  PHE A CA    1 
ATOM   3582 C  C     . PHE A 1 477 ? -10.328 5.358   52.835  1 16.243  ? 469  PHE A C     1 
ATOM   3583 O  O     . PHE A 1 477 ? -9.686  6.403   52.991  1 16.891  ? 469  PHE A O     1 
ATOM   3584 C  CB    . PHE A 1 477 ? -12.781 5.799   52.283  1 17.402  ? 469  PHE A CB    1 
ATOM   3585 C  CG    . PHE A 1 477 ? -14.218 5.699   52.79   1 18.044  ? 469  PHE A CG    1 
ATOM   3586 C  CD1   . PHE A 1 477 ? -14.926 4.477   52.749  1 19.448  ? 469  PHE A CD1   1 
ATOM   3587 C  CD2   . PHE A 1 477 ? -14.825 6.818   53.396  1 18.533  ? 469  PHE A CD2   1 
ATOM   3588 C  CE1   . PHE A 1 477 ? -16.23  4.391   53.277  1 19.198  ? 469  PHE A CE1   1 
ATOM   3589 C  CE2   . PHE A 1 477 ? -16.118 6.739   53.94   1 18.242  ? 469  PHE A CE2   1 
ATOM   3590 C  CZ    . PHE A 1 477 ? -16.823 5.53    53.869  1 19.673  ? 469  PHE A CZ    1 
ATOM   3591 N  N     . VAL A 1 478 ? -9.874  4.245   52.252  1 15.671  ? 470  VAL A N     1 
ATOM   3592 C  CA    . VAL A 1 478 ? -8.554  4.092   51.653  1 16.298  ? 470  VAL A CA    1 
ATOM   3593 C  C     . VAL A 1 478 ? -8.74   3.87    50.154  1 16.945  ? 470  VAL A C     1 
ATOM   3594 O  O     . VAL A 1 478 ? -9.51   2.998   49.75   1 17.938  ? 470  VAL A O     1 
ATOM   3595 C  CB    . VAL A 1 478 ? -7.707  3.014   52.376  1 18.07   ? 470  VAL A CB    1 
ATOM   3596 C  CG1   . VAL A 1 478 ? -6.441  2.599   51.625  1 18.259  ? 470  VAL A CG1   1 
ATOM   3597 C  CG2   . VAL A 1 478 ? -7.319  3.452   53.795  1 17.031  ? 470  VAL A CG2   1 
ATOM   3598 N  N     . LEU A 1 479 ? -8.002  4.662   49.368  1 15.965  ? 471  LEU A N     1 
ATOM   3599 C  CA    . LEU A 1 479 ? -7.982  4.629   47.913  1 16.145  ? 471  LEU A CA    1 
ATOM   3600 C  C     . LEU A 1 479 ? -6.563  4.323   47.434  1 15.931  ? 471  LEU A C     1 
ATOM   3601 O  O     . LEU A 1 479 ? -5.594  4.812   48.033  1 14.803  ? 471  LEU A O     1 
ATOM   3602 C  CB    . LEU A 1 479 ? -8.495  5.945   47.323  1 17.614  ? 471  LEU A CB    1 
ATOM   3603 C  CG    . LEU A 1 479 ? -9.96   6.351   47.572  1 19.743  ? 471  LEU A CG    1 
ATOM   3604 C  CD1   . LEU A 1 479 ? -10.317 6.947   48.929  1 21.414  ? 471  LEU A CD1   1 
ATOM   3605 C  CD2   . LEU A 1 479 ? -10.258 7.417   46.541  1 19.909  ? 471  LEU A CD2   1 
ATOM   3606 N  N     . ALA A 1 480 ? -6.465  3.505   46.368  1 14.875  ? 472  ALA A N     1 
ATOM   3607 C  CA    . ALA A 1 480 ? -5.206  3.109   45.728  1 15.679  ? 472  ALA A CA    1 
ATOM   3608 C  C     . ALA A 1 480 ? -5.449  2.666   44.287  1 16.224  ? 472  ALA A C     1 
ATOM   3609 O  O     . ALA A 1 480 ? -6.518  2.145   43.978  1 17.437  ? 472  ALA A O     1 
ATOM   3610 C  CB    . ALA A 1 480 ? -4.528  2.005   46.531  1 14.926  ? 472  ALA A CB    1 
ATOM   3611 N  N     . ILE A 1 481 ? -4.431  2.86    43.424  1 16.834  ? 473  ILE A N     1 
ATOM   3612 C  CA    . ILE A 1 481 ? -4.437  2.422   42.029  1 15.499  ? 473  ILE A CA    1 
ATOM   3613 C  C     . ILE A 1 481 ? -4.034  0.948   42.011  1 16.173  ? 473  ILE A C     1 
ATOM   3614 O  O     . ILE A 1 481 ? -3.022  0.586   42.598  1 15.736  ? 473  ILE A O     1 
ATOM   3615 C  CB    . ILE A 1 481 ? -3.589  3.325   41.095  1 15.504  ? 473  ILE A CB    1 
ATOM   3616 C  CG1   . ILE A 1 481 ? -3.855  4.867   41.257  1 14.798  ? 473  ILE A CG1   1 
ATOM   3617 C  CG2   . ILE A 1 481 ? -3.594  2.88    39.617  1 13.984  ? 473  ILE A CG2   1 
ATOM   3618 C  CD1   . ILE A 1 481 ? -5.255  5.36    40.952  1 15.935  ? 473  ILE A CD1   1 
ATOM   3619 N  N     . VAL A 1 482 ? -4.868  0.132   41.351  1 15.333  ? 474  VAL A N     1 
ATOM   3620 C  CA    . VAL A 1 482 ? -4.617  -1.279  41.1    1 16.995  ? 474  VAL A CA    1 
ATOM   3621 C  C     . VAL A 1 482 ? -4.268  -1.434  39.618  1 17.495  ? 474  VAL A C     1 
ATOM   3622 O  O     . VAL A 1 482 ? -5.026  -0.943  38.779  1 17.573  ? 474  VAL A O     1 
ATOM   3623 C  CB    . VAL A 1 482 ? -5.777  -2.213  41.527  1 17.392  ? 474  VAL A CB    1 
ATOM   3624 C  CG1   . VAL A 1 482 ? -5.445  -3.686  41.306  1 18.993  ? 474  VAL A CG1   1 
ATOM   3625 C  CG2   . VAL A 1 482 ? -6.192  -2.042  42.989  1 18.287  ? 474  VAL A CG2   1 
ATOM   3626 N  N     . ASP A 1 483 ? -3.151  -2.125  39.325  1 17.211  ? 475  ASP A N     1 
ATOM   3627 C  CA    . ASP A 1 483 ? -2.814  -2.571  37.982  1 19.16   ? 475  ASP A CA    1 
ATOM   3628 C  C     . ASP A 1 483 ? -3.416  -3.959  37.781  1 19.386  ? 475  ASP A C     1 
ATOM   3629 O  O     . ASP A 1 483 ? -3.008  -4.909  38.461  1 18.608  ? 475  ASP A O     1 
ATOM   3630 C  CB    . ASP A 1 483 ? -1.32   -2.572  37.693  1 21.473  ? 475  ASP A CB    1 
ATOM   3631 C  CG    . ASP A 1 483 ? -0.586  -1.278  37.969  1 26.546  ? 475  ASP A CG    1 
ATOM   3632 O  OD1   . ASP A 1 483 ? -0.195  -1.07   39.141  1 32.863  ? 475  ASP A OD1   1 
ATOM   3633 O  OD2   . ASP A 1 483 ? -0.445  -0.493  37.027  1 26.904  ? 475  ASP A OD2   1 
ATOM   3634 N  N     . ARG A 1 484 ? -4.384  -4.047  36.851  1 18.705  ? 476  ARG A N     1 
ATOM   3635 C  CA    . ARG A 1 484 ? -5.004  -5.31   36.468  1 19.366  ? 476  ARG A CA    1 
ATOM   3636 C  C     . ARG A 1 484 ? -4.192  -5.856  35.299  1 20.122  ? 476  ARG A C     1 
ATOM   3637 O  O     . ARG A 1 484 ? -4.538  -5.594  34.145  1 21.522  ? 476  ARG A O     1 
ATOM   3638 C  CB    . ARG A 1 484 ? -6.514  -5.137  36.223  1 19.354  ? 476  ARG A CB    1 
ATOM   3639 C  CG    . ARG A 1 484 ? -7.484  -4.648  37.294  1 18.817  ? 476  ARG A CG    1 
ATOM   3640 C  CD    . ARG A 1 484 ? -7.609  -5.568  38.502  1 20.05   ? 476  ARG A CD    1 
ATOM   3641 N  NE    . ARG A 1 484 ? -8.224  -6.853  38.144  1 20.687  ? 476  ARG A NE    1 
ATOM   3642 C  CZ    . ARG A 1 484 ? -9.534  -7.128  38.025  1 20.895  ? 476  ARG A CZ    1 
ATOM   3643 N  NH1   . ARG A 1 484 ? -10.472 -6.236  38.309  1 19.745  ? 476  ARG A NH1   1 
ATOM   3644 N  NH2   . ARG A 1 484 ? -9.899  -8.325  37.627  1 19.889  ? 476  ARG A NH2   1 
ATOM   3645 N  N     . LEU A 1 485 ? -3.091  -6.558  35.62   1 21.248  ? 477  LEU A N     1 
ATOM   3646 C  CA    . LEU A 1 485 ? -2.001  -6.856  34.692  1 23.885  ? 477  LEU A CA    1 
ATOM   3647 C  C     . LEU A 1 485 ? -2.442  -7.705  33.504  1 26.643  ? 477  LEU A C     1 
ATOM   3648 O  O     . LEU A 1 485 ? -2.066  -7.398  32.372  1 29.627  ? 477  LEU A O     1 
ATOM   3649 C  CB    . LEU A 1 485 ? -0.708  -7.396  35.316  1 24      ? 477  LEU A CB    1 
ATOM   3650 C  CG    . LEU A 1 485 ? 0.035   -6.467  36.294  1 23.442  ? 477  LEU A CG    1 
ATOM   3651 C  CD1   . LEU A 1 485 ? 1.14    -7.327  36.887  1 24.054  ? 477  LEU A CD1   1 
ATOM   3652 C  CD2   . LEU A 1 485 ? 0.6     -5.162  35.67   1 22.628  ? 477  LEU A CD2   1 
ATOM   3653 N  N     . ASP A 1 486 ? -3.288  -8.711  33.758  1 31.508  ? 478  ASP A N     1 
ATOM   3654 C  CA    . ASP A 1 486 ? -3.789  -9.553  32.673  1 33.943  ? 478  ASP A CA    1 
ATOM   3655 C  C     . ASP A 1 486 ? -4.948  -8.903  31.902  1 32.191  ? 478  ASP A C     1 
ATOM   3656 O  O     . ASP A 1 486 ? -5.3    -9.411  30.841  1 30.822  ? 478  ASP A O     1 
ATOM   3657 C  CB    . ASP A 1 486 ? -3.841  -11.016 33.074  1 38.511  ? 478  ASP A CB    1 
ATOM   3658 C  CG    . ASP A 1 486 ? -4.721  -11.399 34.248  1 43.766  ? 478  ASP A CG    1 
ATOM   3659 O  OD1   . ASP A 1 486 ? -5.589  -10.588 34.678  1 48.418  ? 478  ASP A OD1   1 
ATOM   3660 O  OD2   . ASP A 1 486 ? -4.523  -12.534 34.721  1 47.018  ? 478  ASP A OD2   1 
ATOM   3661 N  N     . LEU A 1 487 ? -5.477  -7.757  32.379  1 29.025  ? 479  LEU A N     1 
ATOM   3662 C  CA    . LEU A 1 487 ? -6.54   -7.011  31.713  1 25.566  ? 479  LEU A CA    1 
ATOM   3663 C  C     . LEU A 1 487 ? -6.056  -5.786  30.925  1 23.272  ? 479  LEU A C     1 
ATOM   3664 O  O     . LEU A 1 487 ? -6.852  -5.251  30.165  1 23.444  ? 479  LEU A O     1 
ATOM   3665 C  CB    . LEU A 1 487 ? -7.727  -6.709  32.634  1 26.367  ? 479  LEU A CB    1 
ATOM   3666 C  CG    . LEU A 1 487 ? -8.453  -7.894  33.29   1 30.046  ? 479  LEU A CG    1 
ATOM   3667 C  CD1   . LEU A 1 487 ? -9.458  -7.304  34.265  1 28.85   ? 479  LEU A CD1   1 
ATOM   3668 C  CD2   . LEU A 1 487 ? -9.19   -8.859  32.357  1 32.463  ? 479  LEU A CD2   1 
ATOM   3669 N  N     . ASN A 1 488 ? -4.79   -5.336  31.091  1 23.808  ? 480  ASN A N     1 
ATOM   3670 C  CA    . ASN A 1 488 ? -4.236  -4.082  30.551  1 24.029  ? 480  ASN A CA    1 
ATOM   3671 C  C     . ASN A 1 488 ? -5.131  -2.891  30.939  1 23.591  ? 480  ASN A C     1 
ATOM   3672 O  O     . ASN A 1 488 ? -5.534  -2.097  30.08   1 24.224  ? 480  ASN A O     1 
ATOM   3673 C  CB    . ASN A 1 488 ? -3.783  -4.216  29.084  1 26.657  ? 480  ASN A CB    1 
ATOM   3674 C  CG    . ASN A 1 488 ? -3.079  -3      28.482  1 29.403  ? 480  ASN A CG    1 
ATOM   3675 O  OD1   . ASN A 1 488 ? -2.104  -2.483  29.042  1 28.686  ? 480  ASN A OD1   1 
ATOM   3676 N  ND2   . ASN A 1 488 ? -3.542  -2.514  27.332  1 27.444  ? 480  ASN A ND2   1 
ATOM   3677 N  N     . ARG A 1 489 ? -5.511  -2.835  32.234  1 22.696  ? 481  ARG A N     1 
ATOM   3678 C  CA    . ARG A 1 489 ? -6.285  -1.742  32.808  1 22.288  ? 481  ARG A CA    1 
ATOM   3679 C  C     . ARG A 1 489 ? -5.798  -1.358  34.202  1 19.64   ? 481  ARG A C     1 
ATOM   3680 O  O     . ARG A 1 489 ? -5.212  -2.182  34.912  1 18.98   ? 481  ARG A O     1 
ATOM   3681 C  CB    . ARG A 1 489 ? -7.803  -1.902  32.631  1 24.768  ? 481  ARG A CB    1 
ATOM   3682 C  CG    . ARG A 1 489 ? -8.58   -2.761  33.609  1 28.195  ? 481  ARG A CG    1 
ATOM   3683 C  CD    . ARG A 1 489 ? -10.036 -2.453  33.339  1 29.211  ? 481  ARG A CD    1 
ATOM   3684 N  NE    . ARG A 1 489 ? -10.878 -3.124  34.335  1 34.601  ? 481  ARG A NE    1 
ATOM   3685 C  CZ    . ARG A 1 489 ? -11.666 -4.188  34.167  1 33.508  ? 481  ARG A CZ    1 
ATOM   3686 N  NH1   . ARG A 1 489 ? -11.811 -4.756  32.984  1 34.355  ? 481  ARG A NH1   1 
ATOM   3687 N  NH2   . ARG A 1 489 ? -12.292 -4.702  35.213  1 32.954  ? 481  ARG A NH2   1 
ATOM   3688 N  N     . SER A 1 490 ? -6.065  -0.09   34.549  1 19.283  ? 482  SER A N     1 
ATOM   3689 C  CA    . SER A 1 490 ? -5.911  0.467   35.889  1 18.369  ? 482  SER A CA    1 
ATOM   3690 C  C     . SER A 1 490 ? -7.288  0.724   36.506  1 17.586  ? 482  SER A C     1 
ATOM   3691 O  O     . SER A 1 490 ? -8.214  1.116   35.803  1 15.554  ? 482  SER A O     1 
ATOM   3692 C  CB    . SER A 1 490 ? -5.075  1.719   35.876  1 18.345  ? 482  SER A CB    1 
ATOM   3693 O  OG    . SER A 1 490 ? -3.779  1.454   35.368  1 17.13   ? 482  SER A OG    1 
ATOM   3694 N  N     . GLU A 1 491 ? -7.376  0.548   37.835  1 17.12   ? 483  GLU A N     1 
ATOM   3695 C  CA    . GLU A 1 491 ? -8.57   0.789   38.644  1 18.113  ? 483  GLU A CA    1 
ATOM   3696 C  C     . GLU A 1 491 ? -8.224  1.564   39.909  1 16.944  ? 483  GLU A C     1 
ATOM   3697 O  O     . GLU A 1 491 ? -7.101  1.459   40.38   1 19.609  ? 483  GLU A O     1 
ATOM   3698 C  CB    . GLU A 1 491 ? -9.183  -0.54   39.09   1 19.422  ? 483  GLU A CB    1 
ATOM   3699 C  CG    . GLU A 1 491 ? -9.991  -1.199  37.981  1 21.758  ? 483  GLU A CG    1 
ATOM   3700 C  CD    . GLU A 1 491 ? -10.518 -2.602  38.15   1 24.175  ? 483  GLU A CD    1 
ATOM   3701 O  OE1   . GLU A 1 491 ? -10.304 -3.278  39.196  1 24.033  ? 483  GLU A OE1   1 
ATOM   3702 O  OE2   . GLU A 1 491 ? -11.166 -3      37.136  1 27.857  ? 483  GLU A OE2   1 
ATOM   3703 N  N     . VAL A 1 492 ? -9.201  2.303   40.447  1 16.544  ? 484  VAL A N     1 
ATOM   3704 C  CA    . VAL A 1 492 ? -9.161  2.862   41.796  1 18.475  ? 484  VAL A CA    1 
ATOM   3705 C  C     . VAL A 1 492 ? -9.998  1.934   42.689  1 18.229  ? 484  VAL A C     1 
ATOM   3706 O  O     . VAL A 1 492 ? -11.209 1.852   42.528  1 17.63   ? 484  VAL A O     1 
ATOM   3707 C  CB    . VAL A 1 492 ? -9.531  4.359   42.004  1 18.518  ? 484  VAL A CB    1 
ATOM   3708 C  CG1   . VAL A 1 492 ? -9.103  4.906   43.364  1 17.316  ? 484  VAL A CG1   1 
ATOM   3709 C  CG2   . VAL A 1 492 ? -9.026  5.288   40.907  1 18.468  ? 484  VAL A CG2   1 
ATOM   3710 N  N     . VAL A 1 493 ? -9.332  1.258   43.637  1 18.674  ? 485  VAL A N     1 
ATOM   3711 C  CA    . VAL A 1 493 ? -9.995  0.518   44.703  1 17.071  ? 485  VAL A CA    1 
ATOM   3712 C  C     . VAL A 1 493 ? -10.392 1.494   45.818  1 18.312  ? 485  VAL A C     1 
ATOM   3713 O  O     . VAL A 1 493 ? -9.672  2.47    46.077  1 17.232  ? 485  VAL A O     1 
ATOM   3714 C  CB    . VAL A 1 493 ? -9.151  -0.704  45.129  1 19.23   ? 485  VAL A CB    1 
ATOM   3715 C  CG1   . VAL A 1 493 ? -7.958  -0.401  46.039  1 18.925  ? 485  VAL A CG1   1 
ATOM   3716 C  CG2   . VAL A 1 493 ? -9.999  -1.769  45.771  1 20.465  ? 485  VAL A CG2   1 
ATOM   3717 N  N     . VAL A 1 494 ? -11.579 1.251   46.425  1 17.013  ? 486  VAL A N     1 
ATOM   3718 C  CA    . VAL A 1 494 ? -12.093 1.97    47.591  1 17.201  ? 486  VAL A CA    1 
ATOM   3719 C  C     . VAL A 1 494 ? -12.368 0.927   48.677  1 18.057  ? 486  VAL A C     1 
ATOM   3720 O  O     . VAL A 1 494 ? -13.152 0.004   48.441  1 17.682  ? 486  VAL A O     1 
ATOM   3721 C  CB    . VAL A 1 494 ? -13.283 2.933   47.343  1 16.988  ? 486  VAL A CB    1 
ATOM   3722 C  CG1   . VAL A 1 494 ? -13.576 3.836   48.533  1 16.176  ? 486  VAL A CG1   1 
ATOM   3723 C  CG2   . VAL A 1 494 ? -13.063 3.838   46.13   1 15.47   ? 486  VAL A CG2   1 
ATOM   3724 N  N     . ILE A 1 495 ? -11.687 1.091   49.83   1 16.535  ? 487  ILE A N     1 
ATOM   3725 C  CA    . ILE A 1 495 ? -11.736 0.22    51.009  1 17.175  ? 487  ILE A CA    1 
ATOM   3726 C  C     . ILE A 1 495 ? -12.258 1.051   52.188  1 18.723  ? 487  ILE A C     1 
ATOM   3727 O  O     . ILE A 1 495 ? -11.71  2.12    52.464  1 17.888  ? 487  ILE A O     1 
ATOM   3728 C  CB    . ILE A 1 495 ? -10.349 -0.401  51.331  1 16.254  ? 487  ILE A CB    1 
ATOM   3729 C  CG1   . ILE A 1 495 ? -9.746  -1.185  50.134  1 15.845  ? 487  ILE A CG1   1 
ATOM   3730 C  CG2   . ILE A 1 495 ? -10.412 -1.271  52.604  1 16.593  ? 487  ILE A CG2   1 
ATOM   3731 C  CD1   . ILE A 1 495 ? -8.228  -1.244  50.106  1 14.633  ? 487  ILE A CD1   1 
ATOM   3732 N  N     . ASP A 1 496 ? -13.31  0.542   52.863  1 18.294  ? 488  ASP A N     1 
ATOM   3733 C  CA    . ASP A 1 496 ? -13.764 1.039   54.154  1 19.314  ? 488  ASP A CA    1 
ATOM   3734 C  C     . ASP A 1 496 ? -12.905 0.373   55.226  1 19.497  ? 488  ASP A C     1 
ATOM   3735 O  O     . ASP A 1 496 ? -12.798 -0.854  55.252  1 18.053  ? 488  ASP A O     1 
ATOM   3736 C  CB    . ASP A 1 496 ? -15.259 0.815   54.352  1 19.907  ? 488  ASP A CB    1 
ATOM   3737 C  CG    . ASP A 1 496 ? -15.912 1.477   55.561  1 22.091  ? 488  ASP A CG    1 
ATOM   3738 O  OD1   . ASP A 1 496 ? -15.339 1.447   56.677  1 20.661  ? 488  ASP A OD1   1 
ATOM   3739 O  OD2   . ASP A 1 496 ? -17.03  1.987   55.388  1 21.901  ? 488  ASP A OD2   1 
ATOM   3740 N  N     . THR A 1 497 ? -12.351 1.203   56.126  1 19.679  ? 489  THR A N     1 
ATOM   3741 C  CA    . THR A 1 497 ? -11.439 0.781   57.192  1 21.457  ? 489  THR A CA    1 
ATOM   3742 C  C     . THR A 1 497 ? -12.113 -0.142  58.218  1 20.663  ? 489  THR A C     1 
ATOM   3743 O  O     . THR A 1 497 ? -11.395 -0.871  58.892  1 18.048  ? 489  THR A O     1 
ATOM   3744 C  CB    . THR A 1 497 ? -10.675 1.935   57.856  1 20.936  ? 489  THR A CB    1 
ATOM   3745 O  OG1   . THR A 1 497 ? -11.678 2.798   58.388  1 20.547  ? 489  THR A OG1   1 
ATOM   3746 C  CG2   . THR A 1 497 ? -9.701  2.623   56.916  1 19.566  ? 489  THR A CG2   1 
ATOM   3747 N  N     . ARG A 1 498 ? -13.467 -0.136  58.304  1 22.435  ? 490  ARG A N     1 
ATOM   3748 C  CA    . ARG A 1 498 ? -14.263 -1.061  59.118  1 25.277  ? 490  ARG A CA    1 
ATOM   3749 C  C     . ARG A 1 498 ? -14.039 -2.524  58.715  1 25.799  ? 490  ARG A C     1 
ATOM   3750 O  O     . ARG A 1 498 ? -14.15  -3.409  59.573  1 26.041  ? 490  ARG A O     1 
ATOM   3751 C  CB    . ARG A 1 498 ? -15.771 -0.759  59.131  1 27.508  ? 490  ARG A CB    1 
ATOM   3752 C  CG    . ARG A 1 498 ? -16.165 0.517   59.859  1 28.106  ? 490  ARG A CG    1 
ATOM   3753 C  CD    . ARG A 1 498 ? -17.531 0.931   59.357  1 33.135  ? 490  ARG A CD    1 
ATOM   3754 N  NE    . ARG A 1 498 ? -18.007 2.108   60.097  1 40.872  ? 490  ARG A NE    1 
ATOM   3755 C  CZ    . ARG A 1 498 ? -19.118 2.855   59.965  1 44.745  ? 490  ARG A CZ    1 
ATOM   3756 N  NH1   . ARG A 1 498 ? -19.996 2.63    58.997  1 46.369  ? 490  ARG A NH1   1 
ATOM   3757 N  NH2   . ARG A 1 498 ? -19.338 3.85    60.815  1 43.667  ? 490  ARG A NH2   1 
ATOM   3758 N  N     . ASP A 1 499 ? -13.783 -2.77   57.415  1 24.464  ? 491  ASP A N     1 
ATOM   3759 C  CA    . ASP A 1 499 ? -13.29  -4.049  56.92   1 22.984  ? 491  ASP A CA    1 
ATOM   3760 C  C     . ASP A 1 499 ? -12.243 -3.807  55.842  1 22.984  ? 491  ASP A C     1 
ATOM   3761 O  O     . ASP A 1 499 ? -12.575 -3.761  54.654  1 24.828  ? 491  ASP A O     1 
ATOM   3762 C  CB    . ASP A 1 499 ? -14.39  -5.02   56.504  1 22.08   ? 491  ASP A CB    1 
ATOM   3763 C  CG    . ASP A 1 499 ? -13.929 -6.405  56.04   1 23.175  ? 491  ASP A CG    1 
ATOM   3764 O  OD1   . ASP A 1 499 ? -12.733 -6.783  56.193  1 22.893  ? 491  ASP A OD1   1 
ATOM   3765 O  OD2   . ASP A 1 499 ? -14.785 -7.129  55.533  1 27.59   ? 491  ASP A OD2   1 
ATOM   3766 N  N     . PHE A 1 500 ? -10.985 -3.765  56.301  1 21.991  ? 492  PHE A N     1 
ATOM   3767 C  CA    . PHE A 1 500 ? -9.791  -3.486  55.52   1 22.795  ? 492  PHE A CA    1 
ATOM   3768 C  C     . PHE A 1 500 ? -9.513  -4.56   54.46   1 22.437  ? 492  PHE A C     1 
ATOM   3769 O  O     . PHE A 1 500 ? -8.864  -4.245  53.454  1 24.225  ? 492  PHE A O     1 
ATOM   3770 C  CB    . PHE A 1 500 ? -8.593  -3.099  56.405  1 20.92   ? 492  PHE A CB    1 
ATOM   3771 C  CG    . PHE A 1 500 ? -7.488  -2.387  55.637  1 20.72   ? 492  PHE A CG    1 
ATOM   3772 C  CD1   . PHE A 1 500 ? -7.617  -1.015  55.311  1 21.027  ? 492  PHE A CD1   1 
ATOM   3773 C  CD2   . PHE A 1 500 ? -6.33   -3.084  55.22   1 19.687  ? 492  PHE A CD2   1 
ATOM   3774 C  CE1   . PHE A 1 500 ? -6.621  -0.358  54.566  1 20.019  ? 492  PHE A CE1   1 
ATOM   3775 C  CE2   . PHE A 1 500 ? -5.325  -2.414  54.497  1 19.466  ? 492  PHE A CE2   1 
ATOM   3776 C  CZ    . PHE A 1 500 ? -5.476  -1.062  54.163  1 19.131  ? 492  PHE A CZ    1 
ATOM   3777 N  N     . THR A 1 501 ? -10.028 -5.788  54.658  1 20.325  ? 493  THR A N     1 
ATOM   3778 C  CA    . THR A 1 501 ? -9.777  -6.928  53.77   1 21.182  ? 493  THR A CA    1 
ATOM   3779 C  C     . THR A 1 501 ? -10.583 -6.84   52.463  1 21.177  ? 493  THR A C     1 
ATOM   3780 O  O     . THR A 1 501 ? -10.23  -7.559  51.514  1 21.55   ? 493  THR A O     1 
ATOM   3781 C  CB    . THR A 1 501 ? -9.931  -8.296  54.457  1 19.492  ? 493  THR A CB    1 
ATOM   3782 O  OG1   . THR A 1 501 ? -11.323 -8.538  54.619  1 19.073  ? 493  THR A OG1   1 
ATOM   3783 C  CG2   . THR A 1 501 ? -9.147  -8.455  55.752  1 19.765  ? 493  THR A CG2   1 
ATOM   3784 N  N     . LYS A 1 502 ? -11.619 -5.963  52.405  1 19.672  ? 494  LYS A N     1 
ATOM   3785 C  CA    . LYS A 1 502 ? -12.628 -5.957  51.345  1 20.977  ? 494  LYS A CA    1 
ATOM   3786 C  C     . LYS A 1 502 ? -12.773 -4.571  50.723  1 20.034  ? 494  LYS A C     1 
ATOM   3787 O  O     . LYS A 1 502 ? -12.826 -3.562  51.424  1 21.555  ? 494  LYS A O     1 
ATOM   3788 C  CB    . LYS A 1 502 ? -14.012 -6.404  51.842  1 23.888  ? 494  LYS A CB    1 
ATOM   3789 C  CG    . LYS A 1 502 ? -15.008 -6.993  50.854  1 28.887  ? 494  LYS A CG    1 
ATOM   3790 C  CD    . LYS A 1 502 ? -15.973 -7.819  51.694  1 32.112  ? 494  LYS A CD    1 
ATOM   3791 C  CE    . LYS A 1 502 ? -16.785 -8.772  50.888  1 38.088  ? 494  LYS A CE    1 
ATOM   3792 N  NZ    . LYS A 1 502 ? -18.058 -8.163  50.505  1 40.635  ? 494  LYS A NZ    1 
ATOM   3793 N  N     . ALA A 1 503 ? -12.854 -4.567  49.391  1 18.486  ? 495  ALA A N     1 
ATOM   3794 C  CA    . ALA A 1 503 ? -13.222 -3.389  48.622  1 20.53   ? 495  ALA A CA    1 
ATOM   3795 C  C     . ALA A 1 503 ? -14.736 -3.193  48.65   1 20.129  ? 495  ALA A C     1 
ATOM   3796 O  O     . ALA A 1 503 ? -15.479 -4.161  48.506  1 18.962  ? 495  ALA A O     1 
ATOM   3797 C  CB    . ALA A 1 503 ? -12.711 -3.5    47.211  1 20.925  ? 495  ALA A CB    1 
ATOM   3798 N  N     . VAL A 1 504 ? -15.141 -1.929  48.858  1 19.435  ? 496  VAL A N     1 
ATOM   3799 C  CA    . VAL A 1 504 ? -16.522 -1.458  48.757  1 18.884  ? 496  VAL A CA    1 
ATOM   3800 C  C     . VAL A 1 504 ? -16.836 -1.019  47.326  1 19.7    ? 496  VAL A C     1 
ATOM   3801 O  O     . VAL A 1 504 ? -18     -1.077  46.923  1 19.687  ? 496  VAL A O     1 
ATOM   3802 C  CB    . VAL A 1 504 ? -16.995 -0.406  49.787  1 19.306  ? 496  VAL A CB    1 
ATOM   3803 C  CG1   . VAL A 1 504 ? -17.129 -1      51.185  1 19.637  ? 496  VAL A CG1   1 
ATOM   3804 C  CG2   . VAL A 1 504 ? -16.211 0.918   49.783  1 18.769  ? 496  VAL A CG2   1 
ATOM   3805 N  N     . ALA A 1 505 ? -15.821 -0.502  46.605  1 17.203  ? 497  ALA A N     1 
ATOM   3806 C  CA    . ALA A 1 505 ? -16     0.101   45.286  1 17.309  ? 497  ALA A CA    1 
ATOM   3807 C  C     . ALA A 1 505 ? -14.735 -0.012  44.438  1 17.845  ? 497  ALA A C     1 
ATOM   3808 O  O     . ALA A 1 505 ? -13.642 -0.177  44.982  1 17.315  ? 497  ALA A O     1 
ATOM   3809 C  CB    . ALA A 1 505 ? -16.499 1.534   45.389  1 16.71   ? 497  ALA A CB    1 
ATOM   3810 N  N     . ALA A 1 506 ? -14.922 0.032   43.108  1 18.809  ? 498  ALA A N     1 
ATOM   3811 C  CA    . ALA A 1 506 ? -13.874 0.136   42.101  1 19.696  ? 498  ALA A CA    1 
ATOM   3812 C  C     . ALA A 1 506 ? -14.261 1.206   41.078  1 21.305  ? 498  ALA A C     1 
ATOM   3813 O  O     . ALA A 1 506 ? -15.4   1.234   40.611  1 22.891  ? 498  ALA A O     1 
ATOM   3814 C  CB    . ALA A 1 506 ? -13.594 -1.213  41.457  1 20.006  ? 498  ALA A CB    1 
ATOM   3815 N  N     . VAL A 1 507 ? -13.307 2.091   40.782  1 18.169  ? 499  VAL A N     1 
ATOM   3816 C  CA    . VAL A 1 507 ? -13.356 3.058   39.698  1 18.072  ? 499  VAL A CA    1 
ATOM   3817 C  C     . VAL A 1 507 ? -12.6   2.416   38.531  1 18.915  ? 499  VAL A C     1 
ATOM   3818 O  O     . VAL A 1 507 ? -11.383 2.257   38.599  1 18.849  ? 499  VAL A O     1 
ATOM   3819 C  CB    . VAL A 1 507 ? -12.796 4.443   40.097  1 18.072  ? 499  VAL A CB    1 
ATOM   3820 C  CG1   . VAL A 1 507 ? -12.918 5.469   38.982  1 16.015  ? 499  VAL A CG1   1 
ATOM   3821 C  CG2   . VAL A 1 507 ? -13.434 4.997   41.366  1 18.474  ? 499  VAL A CG2   1 
ATOM   3822 N  N     . GLN A 1 508 ? -13.34  2.072   37.466  1 19.569  ? 500  GLN A N     1 
ATOM   3823 C  CA    . GLN A 1 508 ? -12.873 1.246   36.358  1 19.045  ? 500  GLN A CA    1 
ATOM   3824 C  C     . GLN A 1 508 ? -12.577 2.131   35.15   1 18.115  ? 500  GLN A C     1 
ATOM   3825 O  O     . GLN A 1 508 ? -13.51  2.535   34.435  1 16.468  ? 500  GLN A O     1 
ATOM   3826 C  CB    . GLN A 1 508 ? -13.929 0.159   36.152  1 21.083  ? 500  GLN A CB    1 
ATOM   3827 C  CG    . GLN A 1 508 ? -13.566 -0.883  35.102  1 23.326  ? 500  GLN A CG    1 
ATOM   3828 C  CD    . GLN A 1 508 ? -14.717 -1.801  34.738  1 28.148  ? 500  GLN A CD    1 
ATOM   3829 O  OE1   . GLN A 1 508 ? -15.486 -2.261  35.597  1 28.296  ? 500  GLN A OE1   1 
ATOM   3830 N  NE2   . GLN A 1 508 ? -14.847 -2.076  33.447  1 25.596  ? 500  GLN A NE2   1 
ATOM   3831 N  N     . LEU A 1 509 ? -11.261 2.402   34.938  1 16.31   ? 501  LEU A N     1 
ATOM   3832 C  CA    . LEU A 1 509 ? -10.728 2.987   33.706  1 14.442  ? 501  LEU A CA    1 
ATOM   3833 C  C     . LEU A 1 509 ? -10.897 2.008   32.54   1 14.529  ? 501  LEU A C     1 
ATOM   3834 O  O     . LEU A 1 509 ? -10.86  0.796   32.769  1 15.574  ? 501  LEU A O     1 
ATOM   3835 C  CB    . LEU A 1 509 ? -9.304  3.561   33.799  1 14.72   ? 501  LEU A CB    1 
ATOM   3836 C  CG    . LEU A 1 509 ? -9.143  4.819   34.678  1 14.713  ? 501  LEU A CG    1 
ATOM   3837 C  CD1   . LEU A 1 509 ? -7.661  5.051   34.953  1 13.968  ? 501  LEU A CD1   1 
ATOM   3838 C  CD2   . LEU A 1 509 ? -9.799  6.113   34.103  1 13.719  ? 501  LEU A CD2   1 
ATOM   3839 N  N     . PRO A 1 510 ? -11.102 2.473   31.277  1 14.186  ? 502  PRO A N     1 
ATOM   3840 C  CA    . PRO A 1 510 ? -11.113 1.59    30.099  1 15.844  ? 502  PRO A CA    1 
ATOM   3841 C  C     . PRO A 1 510 ? -9.724  1.166   29.59   1 17.335  ? 502  PRO A C     1 
ATOM   3842 O  O     . PRO A 1 510 ? -9.599  0.459   28.584  1 20.142  ? 502  PRO A O     1 
ATOM   3843 C  CB    . PRO A 1 510 ? -11.948 2.388   29.079  1 14.091  ? 502  PRO A CB    1 
ATOM   3844 C  CG    . PRO A 1 510 ? -11.554 3.809   29.41   1 13.458  ? 502  PRO A CG    1 
ATOM   3845 C  CD    . PRO A 1 510 ? -11.419 3.863   30.892  1 13.241  ? 502  PRO A CD    1 
ATOM   3846 N  N     . PHE A 1 511 ? -8.682  1.628   30.294  1 16.241  ? 503  PHE A N     1 
ATOM   3847 C  CA    . PHE A 1 511 ? -7.27   1.512   29.934  1 15.392  ? 503  PHE A CA    1 
ATOM   3848 C  C     . PHE A 1 511 ? -6.401  1.438   31.193  1 14.747  ? 503  PHE A C     1 
ATOM   3849 O  O     . PHE A 1 511 ? -6.897  1.625   32.312  1 14.018  ? 503  PHE A O     1 
ATOM   3850 C  CB    . PHE A 1 511 ? -6.931  2.679   28.993  1 14.799  ? 503  PHE A CB    1 
ATOM   3851 C  CG    . PHE A 1 511 ? -7.269  4.119   29.367  1 17.646  ? 503  PHE A CG    1 
ATOM   3852 C  CD1   . PHE A 1 511 ? -6.967  4.663   30.633  1 17.401  ? 503  PHE A CD1   1 
ATOM   3853 C  CD2   . PHE A 1 511 ? -7.9    4.949   28.42   1 19.492  ? 503  PHE A CD2   1 
ATOM   3854 C  CE1   . PHE A 1 511 ? -7.249  5.996   30.934  1 18.192  ? 503  PHE A CE1   1 
ATOM   3855 C  CE2   . PHE A 1 511 ? -8.165  6.299   28.712  1 19.725  ? 503  PHE A CE2   1 
ATOM   3856 C  CZ    . PHE A 1 511 ? -7.849  6.811   29.973  1 19.205  ? 503  PHE A CZ    1 
ATOM   3857 N  N     . ALA A 1 512 ? -5.104  1.173   30.972  1 14.467  ? 504  ALA A N     1 
ATOM   3858 C  CA    . ALA A 1 512 ? -4.061  1.267   31.983  1 15.123  ? 504  ALA A CA    1 
ATOM   3859 C  C     . ALA A 1 512 ? -3.371  2.625   31.911  1 15.039  ? 504  ALA A C     1 
ATOM   3860 O  O     . ALA A 1 512 ? -3.215  3.203   30.831  1 15.706  ? 504  ALA A O     1 
ATOM   3861 C  CB    . ALA A 1 512 ? -3.091  0.093   31.888  1 13.637  ? 504  ALA A CB    1 
ATOM   3862 N  N     . ILE A 1 513 ? -3.014  3.131   33.097  1 15.41   ? 505  ILE A N     1 
ATOM   3863 C  CA    . ILE A 1 513 ? -2.125  4.275   33.272  1 16.246  ? 505  ILE A CA    1 
ATOM   3864 C  C     . ILE A 1 513 ? -0.776  3.758   33.787  1 16.352  ? 505  ILE A C     1 
ATOM   3865 O  O     . ILE A 1 513 ? -0.66   2.598   34.202  1 16.869  ? 505  ILE A O     1 
ATOM   3866 C  CB    . ILE A 1 513 ? -2.759  5.42    34.104  1 15.287  ? 505  ILE A CB    1 
ATOM   3867 C  CG1   . ILE A 1 513 ? -3.045  5.019   35.579  1 14.795  ? 505  ILE A CG1   1 
ATOM   3868 C  CG2   . ILE A 1 513 ? -3.987  5.975   33.375  1 14.218  ? 505  ILE A CG2   1 
ATOM   3869 C  CD1   . ILE A 1 513 ? -3.404  6.15    36.544  1 16.413  ? 505  ILE A CD1   1 
ATOM   3870 N  N     . ARG A 1 514 ? 0.239   4.627   33.761  1 16.454  ? 506  ARG A N     1 
ATOM   3871 C  CA    . ARG A 1 514 ? 1.547   4.343   34.341  1 17.43   ? 506  ARG A CA    1 
ATOM   3872 C  C     . ARG A 1 514 ? 1.419   4.031   35.823  1 16.612  ? 506  ARG A C     1 
ATOM   3873 O  O     . ARG A 1 514 ? 0.577   4.596   36.512  1 18.08   ? 506  ARG A O     1 
ATOM   3874 C  CB    . ARG A 1 514 ? 2.523   5.512   34.156  1 17.122  ? 506  ARG A CB    1 
ATOM   3875 C  CG    . ARG A 1 514 ? 3.17    5.575   32.782  1 17.612  ? 506  ARG A CG    1 
ATOM   3876 C  CD    . ARG A 1 514 ? 4.349   4.636   32.652  1 18.831  ? 506  ARG A CD    1 
ATOM   3877 N  NE    . ARG A 1 514 ? 5.243   4.832   31.505  1 19.655  ? 506  ARG A NE    1 
ATOM   3878 C  CZ    . ARG A 1 514 ? 6.315   4.099   31.198  1 20.029  ? 506  ARG A CZ    1 
ATOM   3879 N  NH1   . ARG A 1 514 ? 6.713   3.077   31.964  1 19.396  ? 506  ARG A NH1   1 
ATOM   3880 N  NH2   . ARG A 1 514 ? 7.018   4.434   30.122  1 20.479  ? 506  ARG A NH2   1 
ATOM   3881 N  N     . SER A 1 515 ? 2.257   3.099   36.287  1 17.924  ? 507  SER A N     1 
ATOM   3882 C  CA    . SER A 1 515 ? 2.502   2.94    37.709  1 17.898  ? 507  SER A CA    1 
ATOM   3883 C  C     . SER A 1 515 ? 3.291   4.156   38.199  1 17.595  ? 507  SER A C     1 
ATOM   3884 O  O     . SER A 1 515 ? 4.34    4.491   37.661  1 18.51   ? 507  SER A O     1 
ATOM   3885 C  CB    . SER A 1 515 ? 3.147   1.61    38.007  1 17.348  ? 507  SER A CB    1 
ATOM   3886 O  OG    . SER A 1 515 ? 3.197   1.38    39.409  1 16.44   ? 507  SER A OG    1 
ATOM   3887 N  N     . GLY A 1 516 ? 2.71    4.87    39.167  1 18.456  ? 508  GLY A N     1 
ATOM   3888 C  CA    . GLY A 1 516 ? 3.215   6.173   39.591  1 17.096  ? 508  GLY A CA    1 
ATOM   3889 C  C     . GLY A 1 516 ? 4.142   6.116   40.803  1 16.258  ? 508  GLY A C     1 
ATOM   3890 O  O     . GLY A 1 516 ? 4.626   5.051   41.196  1 16.613  ? 508  GLY A O     1 
ATOM   3891 N  N     . ILE A 1 517 ? 4.334   7.305   41.382  1 14.595  ? 509  ILE A N     1 
ATOM   3892 C  CA    . ILE A 1 517 ? 5.2     7.502   42.529  1 13.896  ? 509  ILE A CA    1 
ATOM   3893 C  C     . ILE A 1 517 ? 4.267   7.806   43.708  1 14.1    ? 509  ILE A C     1 
ATOM   3894 O  O     . ILE A 1 517 ? 3.747   6.856   44.323  1 13.16   ? 509  ILE A O     1 
ATOM   3895 C  CB    . ILE A 1 517 ? 6.375   8.474   42.215  1 14.019  ? 509  ILE A CB    1 
ATOM   3896 C  CG1   . ILE A 1 517 ? 7.138   8.084   40.898  1 13.403  ? 509  ILE A CG1   1 
ATOM   3897 C  CG2   . ILE A 1 517 ? 7.331   8.534   43.415  1 12.761  ? 509  ILE A CG2   1 
ATOM   3898 C  CD1   . ILE A 1 517 ? 8.294   8.978   40.447  1 13.839  ? 509  ILE A CD1   1 
ATOM   3899 N  N     . HIS A 1 518 ? 3.991   9.097   43.964  1 13.569  ? 510  HIS A N     1 
ATOM   3900 C  CA    . HIS A 1 518 ? 3.074   9.506   45.017  1 14.447  ? 510  HIS A CA    1 
ATOM   3901 C  C     . HIS A 1 518 ? 1.738   9.964   44.446  1 15.889  ? 510  HIS A C     1 
ATOM   3902 O  O     . HIS A 1 518 ? 1.651   10.359  43.279  1 17.894  ? 510  HIS A O     1 
ATOM   3903 C  CB    . HIS A 1 518 ? 3.685   10.549  45.967  1 14.692  ? 510  HIS A CB    1 
ATOM   3904 C  CG    . HIS A 1 518 ? 4.833   9.987   46.707  1 15.881  ? 510  HIS A CG    1 
ATOM   3905 N  ND1   . HIS A 1 518 ? 4.727   9.153   47.804  1 15.535  ? 510  HIS A ND1   1 
ATOM   3906 C  CD2   . HIS A 1 518 ? 6.12    10.106  46.435  1 15.22   ? 510  HIS A CD2   1 
ATOM   3907 C  CE1   . HIS A 1 518 ? 5.943   8.792   48.192  1 16.003  ? 510  HIS A CE1   1 
ATOM   3908 N  NE2   . HIS A 1 518 ? 6.797   9.336   47.357  1 15.647  ? 510  HIS A NE2   1 
ATOM   3909 N  N     . GLY A 1 519 ? 0.726   9.886   45.314  1 15.417  ? 511  GLY A N     1 
ATOM   3910 C  CA    . GLY A 1 519 ? -0.543  10.573  45.178  1 16.335  ? 511  GLY A CA    1 
ATOM   3911 C  C     . GLY A 1 519 ? -1.035  11.111  46.518  1 17.127  ? 511  GLY A C     1 
ATOM   3912 O  O     . GLY A 1 519 ? -0.446  10.819  47.564  1 17.019  ? 511  GLY A O     1 
ATOM   3913 N  N     . GLN A 1 520 ? -2.101  11.924  46.451  1 16.961  ? 512  GLN A N     1 
ATOM   3914 C  CA    . GLN A 1 520 ? -2.685  12.586  47.616  1 16.605  ? 512  GLN A CA    1 
ATOM   3915 C  C     . GLN A 1 520 ? -4.206  12.627  47.48   1 16.612  ? 512  GLN A C     1 
ATOM   3916 O  O     . GLN A 1 520 ? -4.737  12.894  46.389  1 14.426  ? 512  GLN A O     1 
ATOM   3917 C  CB    . GLN A 1 520 ? -2.139  13.999  47.874  1 16.017  ? 512  GLN A CB    1 
ATOM   3918 C  CG    . GLN A 1 520 ? -0.626  14.136  48.058  1 16.953  ? 512  GLN A CG    1 
ATOM   3919 C  CD    . GLN A 1 520 ? -0.024  13.407  49.249  1 16.492  ? 512  GLN A CD    1 
ATOM   3920 O  OE1   . GLN A 1 520 ? -0.66   13.191  50.28   1 17.598  ? 512  GLN A OE1   1 
ATOM   3921 N  NE2   . GLN A 1 520 ? 1.23    13.013  49.12   1 15.81   ? 512  GLN A NE2   1 
ATOM   3922 N  N     . TRP A 1 521 ? -4.878  12.382  48.617  1 17.023  ? 513  TRP A N     1 
ATOM   3923 C  CA    . TRP A 1 521 ? -6.265  12.794  48.795  1 16.478  ? 513  TRP A CA    1 
ATOM   3924 C  C     . TRP A 1 521 ? -6.31   14.289  49.123  1 15.857  ? 513  TRP A C     1 
ATOM   3925 O  O     . TRP A 1 521 ? -5.741  14.713  50.119  1 16.511  ? 513  TRP A O     1 
ATOM   3926 C  CB    . TRP A 1 521 ? -7.013  11.963  49.843  1 15.978  ? 513  TRP A CB    1 
ATOM   3927 C  CG    . TRP A 1 521 ? -8.457  12.392  49.918  1 16.558  ? 513  TRP A CG    1 
ATOM   3928 C  CD1   . TRP A 1 521 ? -9.041  13.194  50.862  1 16.457  ? 513  TRP A CD1   1 
ATOM   3929 C  CD2   . TRP A 1 521 ? -9.468  12.123  48.92   1 16.625  ? 513  TRP A CD2   1 
ATOM   3930 N  NE1   . TRP A 1 521 ? -10.37  13.391  50.558  1 17.594  ? 513  TRP A NE1   1 
ATOM   3931 C  CE2   . TRP A 1 521 ? -10.663 12.752  49.377  1 17.742  ? 513  TRP A CE2   1 
ATOM   3932 C  CE3   . TRP A 1 521 ? -9.491  11.389  47.71   1 16.096  ? 513  TRP A CE3   1 
ATOM   3933 C  CZ2   . TRP A 1 521 ? -11.868 12.654  48.665  1 16.476  ? 513  TRP A CZ2   1 
ATOM   3934 C  CZ3   . TRP A 1 521 ? -10.675 11.317  46.999  1 16.639  ? 513  TRP A CZ3   1 
ATOM   3935 C  CH2   . TRP A 1 521 ? -11.845 11.938  47.478  1 17.055  ? 513  TRP A CH2   1 
ATOM   3936 N  N     . ILE A 1 522 ? -6.978  15.059  48.256  1 15.779  ? 514  ILE A N     1 
ATOM   3937 C  CA    . ILE A 1 522 ? -7.139  16.496  48.439  1 16.748  ? 514  ILE A CA    1 
ATOM   3938 C  C     . ILE A 1 522 ? -8.642  16.73   48.632  1 17.02   ? 514  ILE A C     1 
ATOM   3939 O  O     . ILE A 1 522 ? -9.393  16.586  47.65   1 16.491  ? 514  ILE A O     1 
ATOM   3940 C  CB    . ILE A 1 522 ? -6.51   17.326  47.288  1 16.572  ? 514  ILE A CB    1 
ATOM   3941 C  CG1   . ILE A 1 522 ? -5.037  16.919  46.903  1 17.861  ? 514  ILE A CG1   1 
ATOM   3942 C  CG2   . ILE A 1 522 ? -6.691  18.833  47.501  1 14.682  ? 514  ILE A CG2   1 
ATOM   3943 C  CD1   . ILE A 1 522 ? -3.899  17.325  47.829  1 20.989  ? 514  ILE A CD1   1 
ATOM   3944 N  N     . PRO A 1 523 ? -9.137  17.065  49.864  1 18.047  ? 515  PRO A N     1 
ATOM   3945 C  CA    . PRO A 1 523 ? -10.558 17.365  50.054  1 17.32   ? 515  PRO A CA    1 
ATOM   3946 C  C     . PRO A 1 523 ? -11.034 18.585  49.268  1 17.934  ? 515  PRO A C     1 
ATOM   3947 O  O     . PRO A 1 523 ? -10.242 19.501  49      1 17.068  ? 515  PRO A O     1 
ATOM   3948 C  CB    . PRO A 1 523 ? -10.734 17.566  51.56   1 18.839  ? 515  PRO A CB    1 
ATOM   3949 C  CG    . PRO A 1 523 ? -9.349  17.698  52.112  1 18.727  ? 515  PRO A CG    1 
ATOM   3950 C  CD    . PRO A 1 523 ? -8.375  17.131  51.135  1 18.692  ? 515  PRO A CD    1 
ATOM   3951 N  N     . GLY A 1 524 ? -12.33  18.553  48.903  1 16.896  ? 516  GLY A N     1 
ATOM   3952 C  CA    . GLY A 1 524 ? -13.04  19.624  48.215  1 18.015  ? 516  GLY A CA    1 
ATOM   3953 C  C     . GLY A 1 524 ? -12.87  21      48.863  1 18.66   ? 516  GLY A C     1 
ATOM   3954 O  O     . GLY A 1 524 ? -12.617 21.968  48.163  1 16.898  ? 516  GLY A O     1 
ATOM   3955 N  N     . GLU A 1 525 ? -12.94  21.033  50.204  1 19.874  ? 517  GLU A N     1 
ATOM   3956 C  CA    . GLU A 1 525 ? -12.965 22.22   51.047  1 21.911  ? 517  GLU A CA    1 
ATOM   3957 C  C     . GLU A 1 525 ? -11.668 23.024  50.955  1 21.317  ? 517  GLU A C     1 
ATOM   3958 O  O     . GLU A 1 525 ? -11.701 24.221  51.232  1 20.344  ? 517  GLU A O     1 
ATOM   3959 C  CB    . GLU A 1 525 ? -13.279 21.866  52.499  1 24.645  ? 517  GLU A CB    1 
ATOM   3960 C  CG    . GLU A 1 525 ? -14.699 21.335  52.709  1 27.75   ? 517  GLU A CG    1 
ATOM   3961 C  CD    . GLU A 1 525 ? -15.059 19.887  52.35   1 33.771  ? 517  GLU A CD    1 
ATOM   3962 O  OE1   . GLU A 1 525 ? -14.181 19.013  52.068  1 35.773  ? 517  GLU A OE1   1 
ATOM   3963 O  OE2   . GLU A 1 525 ? -16.284 19.625  52.331  1 32.73   ? 517  GLU A OE2   1 
ATOM   3964 N  N     . VAL A 1 526 ? -10.55  22.379  50.57   1 18.816  ? 518  VAL A N     1 
ATOM   3965 C  CA    . VAL A 1 526 ? -9.242  23.018  50.441  1 17.639  ? 518  VAL A CA    1 
ATOM   3966 C  C     . VAL A 1 526 ? -8.95   23.389  48.981  1 18.714  ? 518  VAL A C     1 
ATOM   3967 O  O     . VAL A 1 526 ? -7.957  24.068  48.722  1 20.92   ? 518  VAL A O     1 
ATOM   3968 C  CB    . VAL A 1 526 ? -8.07   22.288  51.155  1 17.346  ? 518  VAL A CB    1 
ATOM   3969 C  CG1   . VAL A 1 526 ? -8.349  22.031  52.639  1 15.389  ? 518  VAL A CG1   1 
ATOM   3970 C  CG2   . VAL A 1 526 ? -7.627  20.99   50.477  1 15.959  ? 518  VAL A CG2   1 
ATOM   3971 N  N     . THR A 1 527 ? -9.803  22.938  48.038  1 17.057  ? 519  THR A N     1 
ATOM   3972 C  CA    . THR A 1 527 ? -9.66   23.109  46.595  1 17.169  ? 519  THR A CA    1 
ATOM   3973 C  C     . THR A 1 527 ? -10.451 24.361  46.199  1 17.026  ? 519  THR A C     1 
ATOM   3974 O  O     . THR A 1 527 ? -11.681 24.327  46.356  1 18.74   ? 519  THR A O     1 
ATOM   3975 C  CB    . THR A 1 527 ? -10.122 21.849  45.838  1 16.953  ? 519  THR A CB    1 
ATOM   3976 O  OG1   . THR A 1 527 ? -9.485  20.708  46.403  1 18.739  ? 519  THR A OG1   1 
ATOM   3977 C  CG2   . THR A 1 527 ? -9.824  21.896  44.349  1 15.183  ? 519  THR A CG2   1 
ATOM   3978 N  N     . PRO A 1 528 ? -9.816  25.476  45.714  1 17.915  ? 520  PRO A N     1 
ATOM   3979 C  CA    . PRO A 1 528 ? -10.558 26.609  45.146  1 17.552  ? 520  PRO A CA    1 
ATOM   3980 C  C     . PRO A 1 528 ? -11.547 26.193  44.053  1 18.137  ? 520  PRO A C     1 
ATOM   3981 O  O     . PRO A 1 528 ? -11.183 25.402  43.167  1 17.281  ? 520  PRO A O     1 
ATOM   3982 C  CB    . PRO A 1 528 ? -9.499  27.584  44.618  1 17.935  ? 520  PRO A CB    1 
ATOM   3983 C  CG    . PRO A 1 528 ? -8.247  27.183  45.371  1 18.488  ? 520  PRO A CG    1 
ATOM   3984 C  CD    . PRO A 1 528 ? -8.355  25.713  45.67   1 17.314  ? 520  PRO A CD    1 
ATOM   3985 N  N     . ASP A 1 529 ? -12.811 26.638  44.212  1 18.527  ? 521  ASP A N     1 
ATOM   3986 C  CA    . ASP A 1 529 ? -13.894 26.542  43.223  1 18.55   ? 521  ASP A CA    1 
ATOM   3987 C  C     . ASP A 1 529 ? -14.327 25.097  42.931  1 17.366  ? 521  ASP A C     1 
ATOM   3988 O  O     . ASP A 1 529 ? -14.9   24.82   41.861  1 17.024  ? 521  ASP A O     1 
ATOM   3989 C  CB    . ASP A 1 529 ? -13.587 27.298  41.932  1 19.567  ? 521  ASP A CB    1 
ATOM   3990 C  CG    . ASP A 1 529 ? -12.993 28.679  42.094  1 20.103  ? 521  ASP A CG    1 
ATOM   3991 O  OD1   . ASP A 1 529 ? -13.674 29.538  42.675  1 20.402  ? 521  ASP A OD1   1 
ATOM   3992 O  OD2   . ASP A 1 529 ? -11.85  28.847  41.643  1 20.083  ? 521  ASP A OD2   1 
ATOM   3993 N  N     . PHE A 1 530 ? -14.09  24.192  43.902  1 16.756  ? 522  PHE A N     1 
ATOM   3994 C  CA    . PHE A 1 530 ? -14.52  22.801  43.852  1 17.157  ? 522  PHE A CA    1 
ATOM   3995 C  C     . PHE A 1 530 ? -16.042 22.69   43.647  1 19.052  ? 522  PHE A C     1 
ATOM   3996 O  O     . PHE A 1 530 ? -16.477 21.78   42.94   1 16.318  ? 522  PHE A O     1 
ATOM   3997 C  CB    . PHE A 1 530 ? -14.087 22.04   45.109  1 15.396  ? 522  PHE A CB    1 
ATOM   3998 C  CG    . PHE A 1 530 ? -14.331 20.536  45.048  1 16.334  ? 522  PHE A CG    1 
ATOM   3999 C  CD1   . PHE A 1 530 ? -13.328 19.683  44.562  1 15.97   ? 522  PHE A CD1   1 
ATOM   4000 C  CD2   . PHE A 1 530 ? -15.536 19.966  45.517  1 15.513  ? 522  PHE A CD2   1 
ATOM   4001 C  CE1   . PHE A 1 530 ? -13.523 18.298  44.556  1 16.257  ? 522  PHE A CE1   1 
ATOM   4002 C  CE2   . PHE A 1 530 ? -15.746 18.583  45.473  1 16.095  ? 522  PHE A CE2   1 
ATOM   4003 C  CZ    . PHE A 1 530 ? -14.737 17.753  44.987  1 16.965  ? 522  PHE A CZ    1 
ATOM   4004 N  N     . GLU A 1 531 ? -16.817 23.593  44.288  1 19.996  ? 523  GLU A N     1 
ATOM   4005 C  CA    . GLU A 1 531 ? -18.275 23.624  44.232  1 21.071  ? 523  GLU A CA    1 
ATOM   4006 C  C     . GLU A 1 531 ? -18.806 24.027  42.848  1 21.284  ? 523  GLU A C     1 
ATOM   4007 O  O     . GLU A 1 531 ? -19.947 23.67   42.549  1 23.113  ? 523  GLU A O     1 
ATOM   4008 C  CB    . GLU A 1 531 ? -18.905 24.371  45.415  1 21.733  ? 523  GLU A CB    1 
ATOM   4009 C  CG    . GLU A 1 531 ? -18.648 23.758  46.797  1 23.112  ? 523  GLU A CG    1 
ATOM   4010 C  CD    . GLU A 1 531 ? -18.846 22.253  47.006  1 27.059  ? 523  GLU A CD    1 
ATOM   4011 O  OE1   . GLU A 1 531 ? -19.88  21.725  46.561  1 27.172  ? 523  GLU A OE1   1 
ATOM   4012 O  OE2   . GLU A 1 531 ? -17.98  21.582  47.598  1 27.395  ? 523  GLU A OE2   1 
ATOM   4013 N  N     . THR A 1 532 ? -18.001 24.724  42.019  1 20.794  ? 524  THR A N     1 
ATOM   4014 C  CA    . THR A 1 532 ? -18.451 25.32   40.753  1 24.479  ? 524  THR A CA    1 
ATOM   4015 C  C     . THR A 1 532 ? -17.716 24.781  39.513  1 26.149  ? 524  THR A C     1 
ATOM   4016 O  O     . THR A 1 532 ? -18.188 25.024  38.398  1 26.013  ? 524  THR A O     1 
ATOM   4017 C  CB    . THR A 1 532 ? -18.49  26.856  40.774  1 25.849  ? 524  THR A CB    1 
ATOM   4018 O  OG1   . THR A 1 532 ? -17.146 27.271  40.976  1 28.223  ? 524  THR A OG1   1 
ATOM   4019 C  CG2   . THR A 1 532 ? -19.477 27.459  41.767  1 24.78   ? 524  THR A CG2   1 
ATOM   4020 N  N     . LYS A 1 533 ? -16.571 24.089  39.69   1 25.685  ? 525  LYS A N     1 
ATOM   4021 C  CA    . LYS A 1 533 ? -15.754 23.583  38.587  1 26.881  ? 525  LYS A CA    1 
ATOM   4022 C  C     . LYS A 1 533 ? -15.558 22.074  38.712  1 27.529  ? 525  LYS A C     1 
ATOM   4023 O  O     . LYS A 1 533 ? -15.204 21.577  39.784  1 27.955  ? 525  LYS A O     1 
ATOM   4024 C  CB    . LYS A 1 533 ? -14.401 24.298  38.466  1 25.673  ? 525  LYS A CB    1 
ATOM   4025 C  CG    . LYS A 1 533 ? -14.477 25.7    37.908  1 27.89   ? 525  LYS A CG    1 
ATOM   4026 C  CD    . LYS A 1 533 ? -13.155 26.454  37.97   1 30.328  ? 525  LYS A CD    1 
ATOM   4027 C  CE    . LYS A 1 533 ? -13.286 27.794  37.334  1 33.551  ? 525  LYS A CE    1 
ATOM   4028 N  NZ    . LYS A 1 533 ? -11.973 28.438  37.279  1 35.182  ? 525  LYS A NZ    1 
ATOM   4029 N  N     . GLY A 1 534 ? -15.814 21.363  37.602  1 24.971  ? 526  GLY A N     1 
ATOM   4030 C  CA    . GLY A 1 534 ? -15.452 19.958  37.434  1 20.934  ? 526  GLY A CA    1 
ATOM   4031 C  C     . GLY A 1 534 ? -14.094 19.813  36.737  1 19.81   ? 526  GLY A C     1 
ATOM   4032 O  O     . GLY A 1 534 ? -13.519 20.8    36.257  1 18.58   ? 526  GLY A O     1 
ATOM   4033 N  N     . LEU A 1 535 ? -13.637 18.551  36.625  1 18.259  ? 527  LEU A N     1 
ATOM   4034 C  CA    . LEU A 1 535 ? -12.476 18.169  35.826  1 17.415  ? 527  LEU A CA    1 
ATOM   4035 C  C     . LEU A 1 535 ? -12.726 18.37   34.328  1 19.1    ? 527  LEU A C     1 
ATOM   4036 O  O     . LEU A 1 535 ? -11.772 18.581  33.583  1 21.119  ? 527  LEU A O     1 
ATOM   4037 C  CB    . LEU A 1 535 ? -11.952 16.772  36.159  1 15.062  ? 527  LEU A CB    1 
ATOM   4038 C  CG    . LEU A 1 535 ? -11.429 16.508  37.579  1 15.04   ? 527  LEU A CG    1 
ATOM   4039 C  CD1   . LEU A 1 535 ? -10.938 15.064  37.558  1 14.183  ? 527  LEU A CD1   1 
ATOM   4040 C  CD2   . LEU A 1 535 ? -10.34  17.41   38.188  1 15.037  ? 527  LEU A CD2   1 
ATOM   4041 N  N     . VAL A 1 536 ? -14.005 18.332  33.91   1 19.512  ? 528  VAL A N     1 
ATOM   4042 C  CA    . VAL A 1 536 ? -14.457 18.417  32.526  1 21.614  ? 528  VAL A CA    1 
ATOM   4043 C  C     . VAL A 1 536 ? -15.292 19.693  32.409  1 23.452  ? 528  VAL A C     1 
ATOM   4044 O  O     . VAL A 1 536 ? -16.247 19.876  33.172  1 25.203  ? 528  VAL A O     1 
ATOM   4045 C  CB    . VAL A 1 536 ? -15.22  17.159  32.036  1 21.496  ? 528  VAL A CB    1 
ATOM   4046 C  CG1   . VAL A 1 536 ? -15.47  17.168  30.525  1 20.37   ? 528  VAL A CG1   1 
ATOM   4047 C  CG2   . VAL A 1 536 ? -14.52  15.848  32.414  1 22.011  ? 528  VAL A CG2   1 
ATOM   4048 N  N     . ASP A 1 537 ? -14.929 20.544  31.434  1 27.253  ? 529  ASP A N     1 
ATOM   4049 C  CA    . ASP A 1 537 ? -15.73  21.716  31.083  1 33.871  ? 529  ASP A CA    1 
ATOM   4050 C  C     . ASP A 1 537 ? -17.036 21.281  30.428  1 30.379  ? 529  ASP A C     1 
ATOM   4051 O  O     . ASP A 1 537 ? -17.007 20.494  29.484  1 30.982  ? 529  ASP A O     1 
ATOM   4052 C  CB    . ASP A 1 537 ? -15.012 22.735  30.212  1 41.678  ? 529  ASP A CB    1 
ATOM   4053 C  CG    . ASP A 1 537 ? -13.856 23.487  30.854  1 52.528  ? 529  ASP A CG    1 
ATOM   4054 O  OD1   . ASP A 1 537 ? -14.027 23.994  31.996  1 55.044  ? 529  ASP A OD1   1 
ATOM   4055 O  OD2   . ASP A 1 537 ? -12.8   23.583  30.187  1 58.307  ? 529  ASP A OD2   1 
ATOM   4056 N  N     . LEU A 1 538 ? -18.147 21.758  31.009  1 29.282  ? 530  LEU A N     1 
ATOM   4057 C  CA    . LEU A 1 538 ? -19.491 21.463  30.539  1 28.208  ? 530  LEU A CA    1 
ATOM   4058 C  C     . LEU A 1 538 ? -19.711 22.081  29.161  1 26.353  ? 530  LEU A C     1 
ATOM   4059 O  O     . LEU A 1 538 ? -19.283 23.218  28.96   1 24.149  ? 530  LEU A O     1 
ATOM   4060 C  CB    . LEU A 1 538 ? -20.6   21.845  31.517  1 31.529  ? 530  LEU A CB    1 
ATOM   4061 C  CG    . LEU A 1 538 ? -20.76  20.98   32.775  1 33.365  ? 530  LEU A CG    1 
ATOM   4062 C  CD1   . LEU A 1 538 ? -21.981 21.567  33.473  1 30.074  ? 530  LEU A CD1   1 
ATOM   4063 C  CD2   . LEU A 1 538 ? -20.869 19.439  32.624  1 32.869  ? 530  LEU A CD2   1 
ATOM   4064 N  N     . PRO A 1 539 ? -20.351 21.369  28.186  1 25.097  ? 531  PRO A N     1 
ATOM   4065 C  CA    . PRO A 1 539 ? -20.836 22.017  26.972  1 24.689  ? 531  PRO A CA    1 
ATOM   4066 C  C     . PRO A 1 539 ? -21.924 23.047  27.26   1 24.596  ? 531  PRO A C     1 
ATOM   4067 O  O     . PRO A 1 539 ? -22.543 22.993  28.337  1 25.373  ? 531  PRO A O     1 
ATOM   4068 C  CB    . PRO A 1 539 ? -21.286 20.847  26.103  1 24.96   ? 531  PRO A CB    1 
ATOM   4069 C  CG    . PRO A 1 539 ? -21.701 19.796  27.11   1 24.347  ? 531  PRO A CG    1 
ATOM   4070 C  CD    . PRO A 1 539 ? -20.679 19.926  28.198  1 24.482  ? 531  PRO A CD    1 
ATOM   4071 N  N     . LYS A 1 540 ? -22.124 23.969  26.3    1 23.972  ? 532  LYS A N     1 
ATOM   4072 C  CA    . LYS A 1 540 ? -23.105 25.053  26.396  1 24.156  ? 532  LYS A CA    1 
ATOM   4073 C  C     . LYS A 1 540 ? -24.524 24.471  26.501  1 23.507  ? 532  LYS A C     1 
ATOM   4074 O  O     . LYS A 1 540 ? -24.804 23.388  25.965  1 23.383  ? 532  LYS A O     1 
ATOM   4075 C  CB    . LYS A 1 540 ? -22.928 26.092  25.275  1 22.427  ? 532  LYS A CB    1 
ATOM   4076 C  CG    . LYS A 1 540 ? -23.363 25.661  23.871  1 22.094  ? 532  LYS A CG    1 
ATOM   4077 C  CD    . LYS A 1 540 ? -23.379 26.779  22.838  1 22.347  ? 532  LYS A CD    1 
ATOM   4078 C  CE    . LYS A 1 540 ? -24.019 26.307  21.562  1 20.765  ? 532  LYS A CE    1 
ATOM   4079 N  NZ    . LYS A 1 540 ? -24.003 27.406  20.596  1 21.161  ? 532  LYS A NZ    1 
ATOM   4080 N  N     . GLU A 1 541 ? -25.392 25.212  27.203  1 21.825  ? 533  GLU A N     1 
ATOM   4081 C  CA    . GLU A 1 541 ? -26.797 24.885  27.376  1 22.92   ? 533  GLU A CA    1 
ATOM   4082 C  C     . GLU A 1 541 ? -27.568 24.977  26.057  1 23.163  ? 533  GLU A C     1 
ATOM   4083 O  O     . GLU A 1 541 ? -28.278 24.023  25.726  1 22.906  ? 533  GLU A O     1 
ATOM   4084 C  CB    . GLU A 1 541 ? -27.363 25.752  28.491  1 25.706  ? 533  GLU A CB    1 
ATOM   4085 C  CG    . GLU A 1 541 ? -28.767 25.34   28.933  1 30.53   ? 533  GLU A CG    1 
ATOM   4086 C  CD    . GLU A 1 541 ? -29.461 26.284  29.895  1 33.216  ? 533  GLU A CD    1 
ATOM   4087 O  OE1   . GLU A 1 541 ? -28.994 27.408  30.172  1 36.82   ? 533  GLU A OE1   1 
ATOM   4088 O  OE2   . GLU A 1 541 ? -30.509 25.849  30.386  1 40.596  ? 533  GLU A OE2   1 
ATOM   4089 N  N     . GLU A 1 542 ? -27.431 26.118  25.345  1 25.289  ? 534  GLU A N     1 
ATOM   4090 C  CA    . GLU A 1 542 ? -28.202 26.461  24.154  1 28.508  ? 534  GLU A CA    1 
ATOM   4091 C  C     . GLU A 1 542 ? -28.021 25.369  23.097  1 26.698  ? 534  GLU A C     1 
ATOM   4092 O  O     . GLU A 1 542 ? -26.886 24.929  22.89   1 25.122  ? 534  GLU A O     1 
ATOM   4093 C  CB    . GLU A 1 542 ? -27.703 27.833  23.693  1 33.259  ? 534  GLU A CB    1 
ATOM   4094 C  CG    . GLU A 1 542 ? -28.299 28.346  22.385  1 41.759  ? 534  GLU A CG    1 
ATOM   4095 C  CD    . GLU A 1 542 ? -27.636 29.618  21.908  1 48.043  ? 534  GLU A CD    1 
ATOM   4096 O  OE1   . GLU A 1 542 ? -26.392 29.671  21.683  1 53.263  ? 534  GLU A OE1   1 
ATOM   4097 O  OE2   . GLU A 1 542 ? -28.428 30.572  21.762  1 51.129  ? 534  GLU A OE2   1 
ATOM   4098 N  N     . HIS A 1 543 ? -29.144 24.946  22.482  1 23.295  ? 535  HIS A N     1 
ATOM   4099 C  CA    . HIS A 1 543 ? -29.159 24.015  21.356  1 24.15   ? 535  HIS A CA    1 
ATOM   4100 C  C     . HIS A 1 543 ? -28.51  24.651  20.127  1 24.412  ? 535  HIS A C     1 
ATOM   4101 O  O     . HIS A 1 543 ? -28.709 25.841  19.885  1 24.111  ? 535  HIS A O     1 
ATOM   4102 C  CB    . HIS A 1 543 ? -30.579 23.509  21.071  1 24.648  ? 535  HIS A CB    1 
ATOM   4103 C  CG    . HIS A 1 543 ? -31.21  22.719  22.18   1 26.221  ? 535  HIS A CG    1 
ATOM   4104 N  ND1   . HIS A 1 543 ? -32.554 22.859  22.46   1 27.323  ? 535  HIS A ND1   1 
ATOM   4105 C  CD2   . HIS A 1 543 ? -30.754 21.797  23.049  1 24.835  ? 535  HIS A CD2   1 
ATOM   4106 C  CE1   . HIS A 1 543 ? -32.877 22.088  23.49   1 24.878  ? 535  HIS A CE1   1 
ATOM   4107 N  NE2   . HIS A 1 543 ? -31.802 21.432  23.862  1 25.835  ? 535  HIS A NE2   1 
ATOM   4108 N  N     . TRP A 1 544 ? -27.697 23.854  19.409  1 22.924  ? 536  TRP A N     1 
ATOM   4109 C  CA    . TRP A 1 544 ? -27.207 24.149  18.067  1 22.963  ? 536  TRP A CA    1 
ATOM   4110 C  C     . TRP A 1 544 ? -28.364 24.216  17.063  1 24.043  ? 536  TRP A C     1 
ATOM   4111 O  O     . TRP A 1 544 ? -28.4   25.136  16.25   1 25.949  ? 536  TRP A O     1 
ATOM   4112 C  CB    . TRP A 1 544 ? -26.166 23.133  17.572  1 21.402  ? 536  TRP A CB    1 
ATOM   4113 C  CG    . TRP A 1 544 ? -24.872 23.022  18.341  1 21.297  ? 536  TRP A CG    1 
ATOM   4114 C  CD1   . TRP A 1 544 ? -24.486 21.948  19.088  1 21.062  ? 536  TRP A CD1   1 
ATOM   4115 C  CD2   . TRP A 1 544 ? -23.78  23.966  18.399  1 20.572  ? 536  TRP A CD2   1 
ATOM   4116 N  NE1   . TRP A 1 544 ? -23.237 22.144  19.614  1 20.726  ? 536  TRP A NE1   1 
ATOM   4117 C  CE2   . TRP A 1 544 ? -22.777 23.373  19.215  1 21.495  ? 536  TRP A CE2   1 
ATOM   4118 C  CE3   . TRP A 1 544 ? -23.548 25.251  17.866  1 20.677  ? 536  TRP A CE3   1 
ATOM   4119 C  CZ2   . TRP A 1 544 ? -21.562 24.025  19.492  1 23.1    ? 536  TRP A CZ2   1 
ATOM   4120 C  CZ3   . TRP A 1 544 ? -22.346 25.893  18.135  1 20.605  ? 536  TRP A CZ3   1 
ATOM   4121 C  CH2   . TRP A 1 544 ? -21.363 25.285  18.941  1 21.589  ? 536  TRP A CH2   1 
ATOM   4122 N  N     . ALA A 1 545 ? -29.264 23.219  17.089  1 23.55   ? 537  ALA A N     1 
ATOM   4123 C  CA    . ALA A 1 545 ? -30.288 23.053  16.065  1 23.484  ? 537  ALA A CA    1 
ATOM   4124 C  C     . ALA A 1 545 ? -31.508 23.929  16.361  1 24.674  ? 537  ALA A C     1 
ATOM   4125 O  O     . ALA A 1 545 ? -31.895 24.022  17.538  1 21.863  ? 537  ALA A O     1 
ATOM   4126 C  CB    . ALA A 1 545 ? -30.69  21.616  15.938  1 23.477  ? 537  ALA A CB    1 
ATOM   4127 N  N     . PRO A 1 546 ? -32.156 24.559  15.33   1 24.287  ? 538  PRO A N     1 
ATOM   4128 C  CA    . PRO A 1 546 ? -33.464 25.202  15.524  1 27.007  ? 538  PRO A CA    1 
ATOM   4129 C  C     . PRO A 1 546 ? -34.585 24.207  15.827  1 25.19   ? 538  PRO A C     1 
ATOM   4130 O  O     . PRO A 1 546 ? -34.483 23.034  15.448  1 22.519  ? 538  PRO A O     1 
ATOM   4131 C  CB    . PRO A 1 546 ? -33.699 25.966  14.221  1 28.669  ? 538  PRO A CB    1 
ATOM   4132 C  CG    . PRO A 1 546 ? -32.899 25.174  13.2    1 27.726  ? 538  PRO A CG    1 
ATOM   4133 C  CD    . PRO A 1 546 ? -31.689 24.681  13.935  1 23.663  ? 538  PRO A CD    1 
ATOM   4134 N  N     . LEU A 1 547 ? -35.649 24.706  16.483  1 29.172  ? 539  LEU A N     1 
ATOM   4135 C  CA    . LEU A 1 547 ? -36.836 23.95   16.888  1 30.822  ? 539  LEU A CA    1 
ATOM   4136 C  C     . LEU A 1 547 ? -37.475 23.194  15.716  1 31.575  ? 539  LEU A C     1 
ATOM   4137 O  O     . LEU A 1 547 ? -37.83  22.015  15.885  1 33.611  ? 539  LEU A O     1 
ATOM   4138 C  CB    . LEU A 1 547 ? -37.826 24.849  17.642  1 36.701  ? 539  LEU A CB    1 
ATOM   4139 C  CG    . LEU A 1 547 ? -39.061 24.193  18.287  1 40.676  ? 539  LEU A CG    1 
ATOM   4140 C  CD1   . LEU A 1 547 ? -38.796 23.292  19.51   1 41.929  ? 539  LEU A CD1   1 
ATOM   4141 C  CD2   . LEU A 1 547 ? -40.122 25.248  18.586  1 37.933  ? 539  LEU A CD2   1 
ATOM   4142 N  N     . SER A 1 548 ? -37.526 23.854  14.537  1 30.055  ? 540  SER A N     1 
ATOM   4143 C  CA    . SER A 1 548 ? -38.061 23.354  13.271  1 31.574  ? 540  SER A CA    1 
ATOM   4144 C  C     . SER A 1 548 ? -37.387 22.063  12.789  1 32.822  ? 540  SER A C     1 
ATOM   4145 O  O     . SER A 1 548 ? -37.999 21.326  12.01   1 32.106  ? 540  SER A O     1 
ATOM   4146 C  CB    . SER A 1 548 ? -38.048 24.421  12.187  1 32.554  ? 540  SER A CB    1 
ATOM   4147 O  OG    . SER A 1 548 ? -36.726 24.759  11.776  1 34.127  ? 540  SER A OG    1 
ATOM   4148 N  N     . GLN A 1 549 ? -36.146 21.794  13.245  1 26.625  ? 541  GLN A N     1 
ATOM   4149 C  CA    . GLN A 1 549 ? -35.343 20.677  12.77   1 25.259  ? 541  GLN A CA    1 
ATOM   4150 C  C     . GLN A 1 549 ? -35.691 19.352  13.456  1 23.985  ? 541  GLN A C     1 
ATOM   4151 O  O     . GLN A 1 549 ? -35.194 18.317  13.009  1 26.795  ? 541  GLN A O     1 
ATOM   4152 C  CB    . GLN A 1 549 ? -33.85  21.013  12.768  1 25.695  ? 541  GLN A CB    1 
ATOM   4153 C  CG    . GLN A 1 549 ? -33.368 21.782  11.543  1 26.845  ? 541  GLN A CG    1 
ATOM   4154 C  CD    . GLN A 1 549 ? -33.169 20.944  10.297  1 26.424  ? 541  GLN A CD    1 
ATOM   4155 O  OE1   . GLN A 1 549 ? -32.438 19.947  10.285  1 23.5    ? 541  GLN A OE1   1 
ATOM   4156 N  NE2   . GLN A 1 549 ? -33.818 21.378  9.226   1 24.352  ? 541  GLN A NE2   1 
ATOM   4157 N  N     . SER A 1 550 ? -36.519 19.382  14.516  1 24.676  ? 542  SER A N     1 
ATOM   4158 C  CA    . SER A 1 550 ? -36.975 18.197  15.242  1 25.696  ? 542  SER A CA    1 
ATOM   4159 C  C     . SER A 1 550 ? -37.736 17.236  14.321  1 23.785  ? 542  SER A C     1 
ATOM   4160 O  O     . SER A 1 550 ? -38.614 17.703  13.595  1 26.933  ? 542  SER A O     1 
ATOM   4161 C  CB    . SER A 1 550 ? -37.833 18.538  16.429  1 30.245  ? 542  SER A CB    1 
ATOM   4162 O  OG    . SER A 1 550 ? -38.128 17.327  17.125  1 31.215  ? 542  SER A OG    1 
ATOM   4163 N  N     . PRO A 1 551 ? -37.469 15.898  14.345  1 22.129  ? 543  PRO A N     1 
ATOM   4164 C  CA    . PRO A 1 551 ? -38.331 14.919  13.678  1 21.353  ? 543  PRO A CA    1 
ATOM   4165 C  C     . PRO A 1 551 ? -39.749 14.848  14.259  1 23.232  ? 543  PRO A C     1 
ATOM   4166 O  O     . PRO A 1 551 ? -40.679 14.491  13.538  1 22.1    ? 543  PRO A O     1 
ATOM   4167 C  CB    . PRO A 1 551 ? -37.568 13.598  13.837  1 21.752  ? 543  PRO A CB    1 
ATOM   4168 C  CG    . PRO A 1 551 ? -36.747 13.802  15.108  1 20.847  ? 543  PRO A CG    1 
ATOM   4169 C  CD    . PRO A 1 551 ? -36.325 15.239  15.017  1 21.84   ? 543  PRO A CD    1 
ATOM   4170 N  N     . TYR A 1 552 ? -39.877 15.199  15.554  1 23.107  ? 544  TYR A N     1 
ATOM   4171 C  CA    . TYR A 1 552 ? -41.096 15.165  16.34   1 25.288  ? 544  TYR A CA    1 
ATOM   4172 C  C     . TYR A 1 552 ? -41.88  16.458  16.148  1 26.801  ? 544  TYR A C     1 
ATOM   4173 O  O     . TYR A 1 552 ? -41.335 17.556  16.309  1 27.434  ? 544  TYR A O     1 
ATOM   4174 C  CB    . TYR A 1 552 ? -40.76  14.86   17.804  1 23.591  ? 544  TYR A CB    1 
ATOM   4175 C  CG    . TYR A 1 552 ? -41.868 15.077  18.829  1 26.042  ? 544  TYR A CG    1 
ATOM   4176 C  CD1   . TYR A 1 552 ? -42.84  14.092  19.069  1 24.956  ? 544  TYR A CD1   1 
ATOM   4177 C  CD2   . TYR A 1 552 ? -41.933 16.276  19.572  1 26.405  ? 544  TYR A CD2   1 
ATOM   4178 C  CE1   . TYR A 1 552 ? -43.84  14.303  20.02   1 26.734  ? 544  TYR A CE1   1 
ATOM   4179 C  CE2   . TYR A 1 552 ? -42.962 16.51   20.482  1 26.723  ? 544  TYR A CE2   1 
ATOM   4180 C  CZ    . TYR A 1 552 ? -43.905 15.512  20.715  1 27.104  ? 544  TYR A CZ    1 
ATOM   4181 O  OH    . TYR A 1 552 ? -44.883 15.717  21.65   1 29.118  ? 544  TYR A OH    1 
ATOM   4182 N  N     . ASP A 1 553 ? -43.182 16.256  15.881  1 26.267  ? 545  ASP A N     1 
ATOM   4183 C  CA    . ASP A 1 553 ? -44.229 17.26   15.852  1 27.117  ? 545  ASP A CA    1 
ATOM   4184 C  C     . ASP A 1 553 ? -45.27  16.904  16.923  1 25.481  ? 545  ASP A C     1 
ATOM   4185 O  O     . ASP A 1 553 ? -45.896 15.84   16.806  1 26.365  ? 545  ASP A O     1 
ATOM   4186 C  CB    . ASP A 1 553 ? -44.76  17.423  14.432  1 28.914  ? 545  ASP A CB    1 
ATOM   4187 C  CG    . ASP A 1 553 ? -45.94  18.366  14.183  1 32.186  ? 545  ASP A CG    1 
ATOM   4188 O  OD1   . ASP A 1 553 ? -46.381 19.11   15.119  1 28.262  ? 545  ASP A OD1   1 
ATOM   4189 O  OD2   . ASP A 1 553 ? -46.432 18.339  13.026  1 32.241  ? 545  ASP A OD2   1 
ATOM   4190 N  N     . PRO A 1 554 ? -45.534 17.769  17.95   1 24.711  ? 546  PRO A N     1 
ATOM   4191 C  CA    . PRO A 1 554 ? -46.569 17.51   18.962  1 26.792  ? 546  PRO A CA    1 
ATOM   4192 C  C     . PRO A 1 554 ? -48.01  17.383  18.445  1 22.895  ? 546  PRO A C     1 
ATOM   4193 O  O     . PRO A 1 554 ? -48.846 16.857  19.178  1 23.769  ? 546  PRO A O     1 
ATOM   4194 C  CB    . PRO A 1 554 ? -46.359 18.585  20.048  1 27.032  ? 546  PRO A CB    1 
ATOM   4195 C  CG    . PRO A 1 554 ? -45.731 19.706  19.253  1 28.652  ? 546  PRO A CG    1 
ATOM   4196 C  CD    . PRO A 1 554 ? -44.861 19.061  18.209  1 26.625  ? 546  PRO A CD    1 
ATOM   4197 N  N     . ASP A 1 555 ? -48.276 17.82   17.196  1 23.279  ? 547  ASP A N     1 
ATOM   4198 C  CA    . ASP A 1 555 ? -49.577 17.71   16.537  1 23.757  ? 547  ASP A CA    1 
ATOM   4199 C  C     . ASP A 1 555 ? -49.762 16.425  15.72   1 25.331  ? 547  ASP A C     1 
ATOM   4200 O  O     . ASP A 1 555 ? -50.906 16.065  15.442  1 24.922  ? 547  ASP A O     1 
ATOM   4201 C  CB    . ASP A 1 555 ? -49.962 18.993  15.823  1 24.806  ? 547  ASP A CB    1 
ATOM   4202 C  CG    . ASP A 1 555 ? -50.039 20.214  16.723  1 27.624  ? 547  ASP A CG    1 
ATOM   4203 O  OD1   . ASP A 1 555 ? -50.714 20.142  17.783  1 31.33   ? 547  ASP A OD1   1 
ATOM   4204 O  OD2   . ASP A 1 555 ? -49.427 21.225  16.354  1 28.125  ? 547  ASP A OD2   1 
ATOM   4205 N  N     . ALA A 1 556 ? -48.652 15.751  15.36   1 26.66   ? 548  ALA A N     1 
ATOM   4206 C  CA    . ALA A 1 556 ? -48.624 14.571  14.497  1 27.35   ? 548  ALA A CA    1 
ATOM   4207 C  C     . ALA A 1 556 ? -49.183 13.336  15.217  1 28.871  ? 548  ALA A C     1 
ATOM   4208 O  O     . ALA A 1 556 ? -49.583 12.396  14.49   1 29.748  ? 548  ALA A O     1 
ATOM   4209 C  CB    . ALA A 1 556 ? -47.206 14.342  14.01   1 28.324  ? 548  ALA A CB    1 
ATOM   4210 O  OXT   . ALA A 1 556 ? -49.201 13.323  16.471  1 30.916  ? 548  ALA A OXT   1 
ATOM   4211 N  N     . TYR B 1 32  ? -9.824  -18.488 38.441  1 28.216  ? 24   TYR B N     1 
ATOM   4212 C  CA    . TYR B 1 32  ? -9.656  -17.277 39.3    1 28.56   ? 24   TYR B CA    1 
ATOM   4213 C  C     . TYR B 1 32  ? -10.78  -16.28  39.031  1 27.892  ? 24   TYR B C     1 
ATOM   4214 O  O     . TYR B 1 32  ? -11.025 -15.941 37.874  1 27.941  ? 24   TYR B O     1 
ATOM   4215 C  CB    . TYR B 1 32  ? -8.272  -16.607 39.216  1 27.214  ? 24   TYR B CB    1 
ATOM   4216 C  CG    . TYR B 1 32  ? -8.065  -15.423 40.163  1 26.032  ? 24   TYR B CG    1 
ATOM   4217 C  CD1   . TYR B 1 32  ? -7.85   -15.62  41.547  1 25.423  ? 24   TYR B CD1   1 
ATOM   4218 C  CD2   . TYR B 1 32  ? -8.112  -14.103 39.68   1 25.319  ? 24   TYR B CD2   1 
ATOM   4219 C  CE1   . TYR B 1 32  ? -7.706  -14.537 42.418  1 26.761  ? 24   TYR B CE1   1 
ATOM   4220 C  CE2   . TYR B 1 32  ? -7.951  -13.012 40.544  1 27.178  ? 24   TYR B CE2   1 
ATOM   4221 C  CZ    . TYR B 1 32  ? -7.734  -13.239 41.908  1 27.279  ? 24   TYR B CZ    1 
ATOM   4222 O  OH    . TYR B 1 32  ? -7.572  -12.213 42.774  1 27.628  ? 24   TYR B OH    1 
ATOM   4223 N  N     . VAL B 1 33  ? -11.41  -15.816 40.128  1 29.008  ? 25   VAL B N     1 
ATOM   4224 C  CA    . VAL B 1 33  ? -12.386 -14.727 40.16   1 28.174  ? 25   VAL B CA    1 
ATOM   4225 C  C     . VAL B 1 33  ? -11.84  -13.613 41.065  1 26.713  ? 25   VAL B C     1 
ATOM   4226 O  O     . VAL B 1 33  ? -11.578 -13.845 42.251  1 25.751  ? 25   VAL B O     1 
ATOM   4227 C  CB    . VAL B 1 33  ? -13.825 -15.17  40.533  1 30.572  ? 25   VAL B CB    1 
ATOM   4228 C  CG1   . VAL B 1 33  ? -14.844 -14.018 40.531  1 31.873  ? 25   VAL B CG1   1 
ATOM   4229 C  CG2   . VAL B 1 33  ? -14.345 -16.287 39.621  1 30.937  ? 25   VAL B CG2   1 
ATOM   4230 N  N     . HIS B 1 34  ? -11.695 -12.414 40.475  1 24.811  ? 26   HIS B N     1 
ATOM   4231 C  CA    . HIS B 1 34  ? -11.305 -11.214 41.202  1 22.495  ? 26   HIS B CA    1 
ATOM   4232 C  C     . HIS B 1 34  ? -12.464 -10.76  42.094  1 20.095  ? 26   HIS B C     1 
ATOM   4233 O  O     . HIS B 1 34  ? -13.556 -10.529 41.556  1 20.299  ? 26   HIS B O     1 
ATOM   4234 C  CB    . HIS B 1 34  ? -10.742 -10.102 40.307  1 21.668  ? 26   HIS B CB    1 
ATOM   4235 C  CG    . HIS B 1 34  ? -9.924  -9.123  41.101  1 20.757  ? 26   HIS B CG    1 
ATOM   4236 N  ND1   . HIS B 1 34  ? -10.43  -8.225  42.026  1 20.128  ? 26   HIS B ND1   1 
ATOM   4237 C  CD2   . HIS B 1 34  ? -8.585  -8.978  41.15   1 20.675  ? 26   HIS B CD2   1 
ATOM   4238 C  CE1   . HIS B 1 34  ? -9.437  -7.537  42.58   1 20.5    ? 26   HIS B CE1   1 
ATOM   4239 N  NE2   . HIS B 1 34  ? -8.309  -7.974  42.052  1 21.721  ? 26   HIS B NE2   1 
ATOM   4240 N  N     . PRO B 1 35  ? -12.267 -10.6   43.444  1 21.045  ? 27   PRO B N     1 
ATOM   4241 C  CA    . PRO B 1 35  ? -13.322 -10.139 44.359  1 21.202  ? 27   PRO B CA    1 
ATOM   4242 C  C     . PRO B 1 35  ? -14.055 -8.863  43.94   1 21.455  ? 27   PRO B C     1 
ATOM   4243 O  O     . PRO B 1 35  ? -15.27  -8.789  44.128  1 21.997  ? 27   PRO B O     1 
ATOM   4244 C  CB    . PRO B 1 35  ? -12.64  -10.058 45.735  1 20.6    ? 27   PRO B CB    1 
ATOM   4245 C  CG    . PRO B 1 35  ? -11.514 -11.086 45.594  1 19.814  ? 27   PRO B CG    1 
ATOM   4246 C  CD    . PRO B 1 35  ? -11.025 -10.888 44.199  1 18.841  ? 27   PRO B CD    1 
ATOM   4247 N  N     . THR B 1 36  ? -13.328 -7.906  43.322  1 21.37   ? 28   THR B N     1 
ATOM   4248 C  CA    . THR B 1 36  ? -13.87  -6.602  42.913  1 20.332  ? 28   THR B CA    1 
ATOM   4249 C  C     . THR B 1 36  ? -14.717 -6.725  41.641  1 19.049  ? 28   THR B C     1 
ATOM   4250 O  O     . THR B 1 36  ? -15.534 -5.835  41.397  1 21.063  ? 28   THR B O     1 
ATOM   4251 C  CB    . THR B 1 36  ? -12.809 -5.498  42.785  1 20.168  ? 28   THR B CB    1 
ATOM   4252 O  OG1   . THR B 1 36  ? -11.962 -5.836  41.686  1 20.476  ? 28   THR B OG1   1 
ATOM   4253 C  CG2   . THR B 1 36  ? -11.986 -5.267  44.039  1 19.949  ? 28   THR B CG2   1 
ATOM   4254 N  N     . ASP B 1 37  ? -14.533 -7.813  40.865  1 19.412  ? 29   ASP B N     1 
ATOM   4255 C  CA    . ASP B 1 37  ? -15.279 -8.101  39.64   1 21.011  ? 29   ASP B CA    1 
ATOM   4256 C  C     . ASP B 1 37  ? -16.747 -8.453  39.876  1 19.918  ? 29   ASP B C     1 
ATOM   4257 O  O     . ASP B 1 37  ? -17.542 -8.262  38.961  1 19.355  ? 29   ASP B O     1 
ATOM   4258 C  CB    . ASP B 1 37  ? -14.516 -9.023  38.701  1 20.907  ? 29   ASP B CB    1 
ATOM   4259 C  CG    . ASP B 1 37  ? -13.327 -8.402  37.991  1 21.624  ? 29   ASP B CG    1 
ATOM   4260 O  OD1   . ASP B 1 37  ? -13.091 -7.169  38.162  1 21.78   ? 29   ASP B OD1   1 
ATOM   4261 O  OD2   . ASP B 1 37  ? -12.649 -9.162  37.265  1 21.789  ? 29   ASP B OD2   1 
ATOM   4262 N  N     . ILE B 1 38  ? -17.083 -8.938  41.085  1 19.72   ? 30   ILE B N     1 
ATOM   4263 C  CA    . ILE B 1 38  ? -18.451 -9.287  41.483  1 20.449  ? 30   ILE B CA    1 
ATOM   4264 C  C     . ILE B 1 38  ? -19.168 -8.106  42.171  1 21.216  ? 30   ILE B C     1 
ATOM   4265 O  O     . ILE B 1 38  ? -20.296 -8.257  42.642  1 22.669  ? 30   ILE B O     1 
ATOM   4266 C  CB    . ILE B 1 38  ? -18.52  -10.646 42.228  1 21.025  ? 30   ILE B CB    1 
ATOM   4267 C  CG1   . ILE B 1 38  ? -18.001 -10.596 43.662  1 22.287  ? 30   ILE B CG1   1 
ATOM   4268 C  CG2   . ILE B 1 38  ? -17.853 -11.782 41.428  1 20.791  ? 30   ILE B CG2   1 
ATOM   4269 C  CD1   . ILE B 1 38  ? -18.911 -11.277 44.674  1 21.428  ? 30   ILE B CD1   1 
ATOM   4270 N  N     . LEU B 1 39  ? -18.512 -6.931  42.284  1 19.937  ? 31   LEU B N     1 
ATOM   4271 C  CA    . LEU B 1 39  ? -19.155 -5.693  42.722  1 18.949  ? 31   LEU B CA    1 
ATOM   4272 C  C     . LEU B 1 39  ? -20.113 -5.198  41.625  1 17.711  ? 31   LEU B C     1 
ATOM   4273 O  O     . LEU B 1 39  ? -19.685 -5.186  40.471  1 16.566  ? 31   LEU B O     1 
ATOM   4274 C  CB    . LEU B 1 39  ? -18.188 -4.6    43.195  1 19.694  ? 31   LEU B CB    1 
ATOM   4275 C  CG    . LEU B 1 39  ? -17.352 -4.89   44.452  1 19.804  ? 31   LEU B CG    1 
ATOM   4276 C  CD1   . LEU B 1 39  ? -16.259 -3.854  44.53   1 21.082  ? 31   LEU B CD1   1 
ATOM   4277 C  CD2   . LEU B 1 39  ? -18.127 -4.945  45.796  1 21.197  ? 31   LEU B CD2   1 
ATOM   4278 N  N     . PRO B 1 40  ? -21.399 -4.821  41.923  1 17.781  ? 32   PRO B N     1 
ATOM   4279 C  CA    . PRO B 1 40  ? -22.381 -4.459  40.888  1 17.395  ? 32   PRO B CA    1 
ATOM   4280 C  C     . PRO B 1 40  ? -22.086 -3.202  40.076  1 16.482  ? 32   PRO B C     1 
ATOM   4281 O  O     . PRO B 1 40  ? -21.686 -2.183  40.639  1 15.823  ? 32   PRO B O     1 
ATOM   4282 C  CB    . PRO B 1 40  ? -23.714 -4.349  41.638  1 16.882  ? 32   PRO B CB    1 
ATOM   4283 C  CG    . PRO B 1 40  ? -23.29  -4.016  43.056  1 17.248  ? 32   PRO B CG    1 
ATOM   4284 C  CD    . PRO B 1 40  ? -22.017 -4.776  43.271  1 16.434  ? 32   PRO B CD    1 
ATOM   4285 N  N     . SER B 1 41  ? -22.341 -3.306  38.762  1 17.563  ? 33   SER B N     1 
ATOM   4286 C  CA    . SER B 1 41  ? -22.37  -2.198  37.815  1 19.118  ? 33   SER B CA    1 
ATOM   4287 C  C     . SER B 1 41  ? -23.809 -1.753  37.555  1 19.373  ? 33   SER B C     1 
ATOM   4288 O  O     . SER B 1 41  ? -24.698 -2.596  37.467  1 20.109  ? 33   SER B O     1 
ATOM   4289 C  CB    . SER B 1 41  ? -21.681 -2.577  36.523  1 19.208  ? 33   SER B CB    1 
ATOM   4290 O  OG    . SER B 1 41  ? -21.759 -1.524  35.569  1 18.515  ? 33   SER B OG    1 
ATOM   4291 N  N     . GLY B 1 42  ? -23.985 -0.429  37.386  1 19.585  ? 34   GLY B N     1 
ATOM   4292 C  CA    . GLY B 1 42  ? -25.206 0.22    36.923  1 19.719  ? 34   GLY B CA    1 
ATOM   4293 C  C     . GLY B 1 42  ? -25.274 0.437   35.404  1 21.305  ? 34   GLY B C     1 
ATOM   4294 O  O     . GLY B 1 42  ? -26.238 1.04    34.931  1 23.101  ? 34   GLY B O     1 
ATOM   4295 N  N     . TRP B 1 43  ? -24.259 -0.01   34.638  1 20.867  ? 35   TRP B N     1 
ATOM   4296 C  CA    . TRP B 1 43  ? -24.263 0.094   33.18   1 19.664  ? 35   TRP B CA    1 
ATOM   4297 C  C     . TRP B 1 43  ? -25.18  -0.977  32.589  1 19.905  ? 35   TRP B C     1 
ATOM   4298 O  O     . TRP B 1 43  ? -25.093 -2.128  33.03   1 22.036  ? 35   TRP B O     1 
ATOM   4299 C  CB    . TRP B 1 43  ? -22.85  0.054   32.567  1 19.319  ? 35   TRP B CB    1 
ATOM   4300 C  CG    . TRP B 1 43  ? -22.286 1.431   32.304  1 19.161  ? 35   TRP B CG    1 
ATOM   4301 C  CD1   . TRP B 1 43  ? -21.746 2.27    33.24   1 18.06   ? 35   TRP B CD1   1 
ATOM   4302 C  CD2   . TRP B 1 43  ? -22.244 2.152   31.048  1 17.407  ? 35   TRP B CD2   1 
ATOM   4303 N  NE1   . TRP B 1 43  ? -21.38  3.456   32.663  1 18.148  ? 35   TRP B NE1   1 
ATOM   4304 C  CE2   . TRP B 1 43  ? -21.664 3.423   31.324  1 17.21   ? 35   TRP B CE2   1 
ATOM   4305 C  CE3   . TRP B 1 43  ? -22.644 1.87    29.724  1 16.675  ? 35   TRP B CE3   1 
ATOM   4306 C  CZ2   . TRP B 1 43  ? -21.47  4.403   30.333  1 16.765  ? 35   TRP B CZ2   1 
ATOM   4307 C  CZ3   . TRP B 1 43  ? -22.469 2.842   28.745  1 16.547  ? 35   TRP B CZ3   1 
ATOM   4308 C  CH2   . TRP B 1 43  ? -21.891 4.097   29.048  1 17.06   ? 35   TRP B CH2   1 
ATOM   4309 N  N     . PRO B 1 44  ? -26.083 -0.66   31.609  1 19.76   ? 36   PRO B N     1 
ATOM   4310 C  CA    . PRO B 1 44  ? -26.615 -1.687  30.699  1 19.261  ? 36   PRO B CA    1 
ATOM   4311 C  C     . PRO B 1 44  ? -25.558 -2.167  29.712  1 18.459  ? 36   PRO B C     1 
ATOM   4312 O  O     . PRO B 1 44  ? -24.494 -1.548  29.607  1 20.685  ? 36   PRO B O     1 
ATOM   4313 C  CB    . PRO B 1 44  ? -27.797 -1.026  29.991  1 20.195  ? 36   PRO B CB    1 
ATOM   4314 C  CG    . PRO B 1 44  ? -27.507 0.446   30.11   1 19.381  ? 36   PRO B CG    1 
ATOM   4315 C  CD    . PRO B 1 44  ? -26.61  0.683   31.302  1 18.713  ? 36   PRO B CD    1 
ATOM   4316 N  N     . THR B 1 45  ? -25.846 -3.268  29.008  1 18.884  ? 37   THR B N     1 
ATOM   4317 C  CA    . THR B 1 45  ? -24.982 -3.764  27.948  1 21.621  ? 37   THR B CA    1 
ATOM   4318 C  C     . THR B 1 45  ? -25.117 -2.823  26.743  1 22.753  ? 37   THR B C     1 
ATOM   4319 O  O     . THR B 1 45  ? -26.161 -2.809  26.084  1 23.632  ? 37   THR B O     1 
ATOM   4320 C  CB    . THR B 1 45  ? -25.221 -5.249  27.653  1 24.339  ? 37   THR B CB    1 
ATOM   4321 O  OG1   . THR B 1 45  ? -25.139 -5.892  28.925  1 26.813  ? 37   THR B OG1   1 
ATOM   4322 C  CG2   . THR B 1 45  ? -24.178 -5.857  26.716  1 23.707  ? 37   THR B CG2   1 
ATOM   4323 N  N     . ALA B 1 46  ? -24.049 -2.035  26.502  1 21.681  ? 38   ALA B N     1 
ATOM   4324 C  CA    . ALA B 1 46  ? -23.968 -1.081  25.394  1 22.421  ? 38   ALA B CA    1 
ATOM   4325 C  C     . ALA B 1 46  ? -22.974 -1.581  24.34   1 21.849  ? 38   ALA B C     1 
ATOM   4326 O  O     . ALA B 1 46  ? -21.768 -1.297  24.423  1 22.399  ? 38   ALA B O     1 
ATOM   4327 C  CB    . ALA B 1 46  ? -23.691 0.334   25.922  1 21.274  ? 38   ALA B CB    1 
ATOM   4328 N  N     . THR B 1 47  ? -23.496 -2.401  23.4    1 20.795  ? 39   THR B N     1 
ATOM   4329 C  CA    . THR B 1 47  ? -22.715 -3      22.314  1 20.096  ? 39   THR B CA    1 
ATOM   4330 C  C     . THR B 1 47  ? -22.412 -1.933  21.258  1 20.684  ? 39   THR B C     1 
ATOM   4331 O  O     . THR B 1 47  ? -23.171 -0.967  21.123  1 22.087  ? 39   THR B O     1 
ATOM   4332 C  CB    . THR B 1 47  ? -23.306 -4.27   21.661  1 19.351  ? 39   THR B CB    1 
ATOM   4333 O  OG1   . THR B 1 47  ? -24.442 -3.837  20.914  1 18.891  ? 39   THR B OG1   1 
ATOM   4334 C  CG2   . THR B 1 47  ? -23.677 -5.393  22.613  1 17.262  ? 39   THR B CG2   1 
ATOM   4335 N  N     . ASP B 1 48  ? -21.289 -2.128  20.533  1 20.159  ? 40   ASP B N     1 
ATOM   4336 C  CA    . ASP B 1 48  ? -21.047 -1.577  19.204  1 19.295  ? 40   ASP B CA    1 
ATOM   4337 C  C     . ASP B 1 48  ? -21.301 -2.683  18.166  1 18.401  ? 40   ASP B C     1 
ATOM   4338 O  O     . ASP B 1 48  ? -21.596 -3.828  18.54   1 17.007  ? 40   ASP B O     1 
ATOM   4339 C  CB    . ASP B 1 48  ? -19.675 -0.91   19.155  1 21.491  ? 40   ASP B CB    1 
ATOM   4340 C  CG    . ASP B 1 48  ? -18.488 -1.836  19.408  1 22.148  ? 40   ASP B CG    1 
ATOM   4341 O  OD1   . ASP B 1 48  ? -18.374 -2.872  18.713  1 22.706  ? 40   ASP B OD1   1 
ATOM   4342 O  OD2   . ASP B 1 48  ? -17.699 -1.535  20.314  1 20.547  ? 40   ASP B OD2   1 
ATOM   4343 N  N     . LEU B 1 49  ? -21.136 -2.357  16.868  1 17.739  ? 41   LEU B N     1 
ATOM   4344 C  CA    . LEU B 1 49  ? -21.432 -3.261  15.755  1 18.751  ? 41   LEU B CA    1 
ATOM   4345 C  C     . LEU B 1 49  ? -20.632 -4.572  15.8    1 20.805  ? 41   LEU B C     1 
ATOM   4346 O  O     . LEU B 1 49  ? -21.157 -5.61   15.369  1 22.827  ? 41   LEU B O     1 
ATOM   4347 C  CB    . LEU B 1 49  ? -21.432 -2.628  14.358  1 17.941  ? 41   LEU B CB    1 
ATOM   4348 C  CG    . LEU B 1 49  ? -22.639 -1.779  13.954  1 17.386  ? 41   LEU B CG    1 
ATOM   4349 C  CD1   . LEU B 1 49  ? -22.288 -1.099  12.637  1 17.887  ? 41   LEU B CD1   1 
ATOM   4350 C  CD2   . LEU B 1 49  ? -23.925 -2.569  13.76   1 16.891  ? 41   LEU B CD2   1 
ATOM   4351 N  N     . SER B 1 50  ? -19.408 -4.554  16.378  1 20.132  ? 42   SER B N     1 
ATOM   4352 C  CA    . SER B 1 50  ? -18.567 -5.747  16.534  1 18.452  ? 42   SER B CA    1 
ATOM   4353 C  C     . SER B 1 50  ? -19.141 -6.758  17.539  1 18.076  ? 42   SER B C     1 
ATOM   4354 O  O     . SER B 1 50  ? -18.708 -7.91   17.553  1 19.74   ? 42   SER B O     1 
ATOM   4355 C  CB    . SER B 1 50  ? -17.129 -5.388  16.838  1 17.387  ? 42   SER B CB    1 
ATOM   4356 O  OG    . SER B 1 50  ? -17.03  -4.976  18.192  1 17.282  ? 42   SER B OG    1 
ATOM   4357 N  N     . GLY B 1 51  ? -20.098 -6.315  18.369  1 17.207  ? 43   GLY B N     1 
ATOM   4358 C  CA    . GLY B 1 51  ? -20.596 -7.069  19.508  1 18.822  ? 43   GLY B CA    1 
ATOM   4359 C  C     . GLY B 1 51  ? -19.821 -6.771  20.796  1 19.974  ? 43   GLY B C     1 
ATOM   4360 O  O     . GLY B 1 51  ? -20.272 -7.207  21.852  1 20.592  ? 43   GLY B O     1 
ATOM   4361 N  N     . GLY B 1 52  ? -18.686 -6.037  20.705  1 20.857  ? 44   GLY B N     1 
ATOM   4362 C  CA    . GLY B 1 52  ? -17.918 -5.55   21.856  1 20.949  ? 44   GLY B CA    1 
ATOM   4363 C  C     . GLY B 1 52  ? -18.777 -4.654  22.755  1 21.748  ? 44   GLY B C     1 
ATOM   4364 O  O     . GLY B 1 52  ? -19.573 -3.874  22.23   1 20.464  ? 44   GLY B O     1 
ATOM   4365 N  N     . ALA B 1 53  ? -18.615 -4.784  24.087  1 20.701  ? 45   ALA B N     1 
ATOM   4366 C  CA    . ALA B 1 53  ? -19.502 -4.126  25.05   1 21.078  ? 45   ALA B CA    1 
ATOM   4367 C  C     . ALA B 1 53  ? -18.782 -3.234  26.079  1 21.763  ? 45   ALA B C     1 
ATOM   4368 O  O     . ALA B 1 53  ? -19.391 -2.847  27.079  1 22.545  ? 45   ALA B O     1 
ATOM   4369 C  CB    . ALA B 1 53  ? -20.482 -5.134  25.671  1 20.261  ? 45   ALA B CB    1 
ATOM   4370 N  N     . GLN B 1 54  ? -17.523 -2.855  25.809  1 19.687  ? 46   GLN B N     1 
ATOM   4371 C  CA    . GLN B 1 54  ? -16.725 -2.072  26.74   1 19.447  ? 46   GLN B CA    1 
ATOM   4372 C  C     . GLN B 1 54  ? -16.842 -0.574  26.429  1 17.719  ? 46   GLN B C     1 
ATOM   4373 O  O     . GLN B 1 54  ? -16.27  -0.151  25.423  1 19.536  ? 46   GLN B O     1 
ATOM   4374 C  CB    . GLN B 1 54  ? -15.32  -2.683  26.848  1 21.169  ? 46   GLN B CB    1 
ATOM   4375 C  CG    . GLN B 1 54  ? -14.367 -1.955  27.797  1 23.618  ? 46   GLN B CG    1 
ATOM   4376 C  CD    . GLN B 1 54  ? -14.87  -1.778  29.218  1 25.37   ? 46   GLN B CD    1 
ATOM   4377 O  OE1   . GLN B 1 54  ? -15.218 -2.74   29.92   1 27.353  ? 46   GLN B OE1   1 
ATOM   4378 N  NE2   . GLN B 1 54  ? -14.908 -0.525  29.645  1 22.104  ? 46   GLN B NE2   1 
ATOM   4379 N  N     . PRO B 1 55  ? -17.506 0.274   27.275  1 16.017  ? 47   PRO B N     1 
ATOM   4380 C  CA    . PRO B 1 55  ? -17.45  1.728   27.14   1 15.25   ? 47   PRO B CA    1 
ATOM   4381 C  C     . PRO B 1 55  ? -16.026 2.264   27.258  1 15.277  ? 47   PRO B C     1 
ATOM   4382 O  O     . PRO B 1 55  ? -15.263 1.76    28.09   1 15.039  ? 47   PRO B O     1 
ATOM   4383 C  CB    . PRO B 1 55  ? -18.344 2.255   28.271  1 14.971  ? 47   PRO B CB    1 
ATOM   4384 C  CG    . PRO B 1 55  ? -19.257 1.077   28.51   1 15.294  ? 47   PRO B CG    1 
ATOM   4385 C  CD    . PRO B 1 55  ? -18.324 -0.084  28.447  1 15.151  ? 47   PRO B CD    1 
ATOM   4386 N  N     . ARG B 1 56  ? -15.684 3.218   26.369  1 14.815  ? 48   ARG B N     1 
ATOM   4387 C  CA    . ARG B 1 56  ? -14.347 3.8     26.261  1 15.282  ? 48   ARG B CA    1 
ATOM   4388 C  C     . ARG B 1 56  ? -14.401 5.252   26.736  1 16.483  ? 48   ARG B C     1 
ATOM   4389 O  O     . ARG B 1 56  ? -14.052 5.519   27.892  1 16.571  ? 48   ARG B O     1 
ATOM   4390 C  CB    . ARG B 1 56  ? -13.651 3.488   24.925  1 14.154  ? 48   ARG B CB    1 
ATOM   4391 C  CG    . ARG B 1 56  ? -13.513 2.011   24.591  1 15.677  ? 48   ARG B CG    1 
ATOM   4392 C  CD    . ARG B 1 56  ? -12.538 1.255   25.489  1 15.786  ? 48   ARG B CD    1 
ATOM   4393 N  NE    . ARG B 1 56  ? -12.508 -0.127  25.005  1 16.569  ? 48   ARG B NE    1 
ATOM   4394 C  CZ    . ARG B 1 56  ? -11.774 -1.135  25.499  1 16.625  ? 48   ARG B CZ    1 
ATOM   4395 N  NH1   . ARG B 1 56  ? -10.972 -0.984  26.561  1 14.67   ? 48   ARG B NH1   1 
ATOM   4396 N  NH2   . ARG B 1 56  ? -11.877 -2.309  24.895  1 15.227  ? 48   ARG B NH2   1 
ATOM   4397 N  N     . ARG B 1 57  ? -14.893 6.148   25.848  1 15.279  ? 49   ARG B N     1 
ATOM   4398 C  CA    . ARG B 1 57  ? -15.444 7.475   26.15   1 15.426  ? 49   ARG B CA    1 
ATOM   4399 C  C     . ARG B 1 57  ? -14.328 8.495   26.419  1 15.969  ? 49   ARG B C     1 
ATOM   4400 O  O     . ARG B 1 57  ? -14.576 9.548   27.014  1 14.593  ? 49   ARG B O     1 
ATOM   4401 C  CB    . ARG B 1 57  ? -16.577 7.452   27.202  1 14.227  ? 49   ARG B CB    1 
ATOM   4402 C  CG    . ARG B 1 57  ? -17.627 6.347   27.108  1 15.595  ? 49   ARG B CG    1 
ATOM   4403 C  CD    . ARG B 1 57  ? -18.526 6.191   28.317  1 15.88   ? 49   ARG B CD    1 
ATOM   4404 N  NE    . ARG B 1 57  ? -17.836 5.95    29.584  1 18.175  ? 49   ARG B NE    1 
ATOM   4405 C  CZ    . ARG B 1 57  ? -18.056 6.526   30.762  1 17.58   ? 49   ARG B CZ    1 
ATOM   4406 N  NH1   . ARG B 1 57  ? -19.008 7.443   30.941  1 16.961  ? 49   ARG B NH1   1 
ATOM   4407 N  NH2   . ARG B 1 57  ? -17.291 6.123   31.764  1 16.187  ? 49   ARG B NH2   1 
ATOM   4408 N  N     . PHE B 1 58  ? -13.097 8.186   25.971  1 17.879  ? 50   PHE B N     1 
ATOM   4409 C  CA    . PHE B 1 58  ? -11.922 9.024   26.186  1 18.9    ? 50   PHE B CA    1 
ATOM   4410 C  C     . PHE B 1 58  ? -11.993 10.22   25.241  1 17.12   ? 50   PHE B C     1 
ATOM   4411 O  O     . PHE B 1 58  ? -12.292 10.054  24.051  1 16.83   ? 50   PHE B O     1 
ATOM   4412 C  CB    . PHE B 1 58  ? -10.57  8.287   26.151  1 21.027  ? 50   PHE B CB    1 
ATOM   4413 C  CG    . PHE B 1 58  ? -9.329  9.176   26.251  1 23.749  ? 50   PHE B CG    1 
ATOM   4414 C  CD1   . PHE B 1 58  ? -8.895  9.694   27.49   1 25.27   ? 50   PHE B CD1   1 
ATOM   4415 C  CD2   . PHE B 1 58  ? -8.579  9.498   25.096  1 25.021  ? 50   PHE B CD2   1 
ATOM   4416 C  CE1   . PHE B 1 58  ? -7.736  10.501  27.583  1 23.748  ? 50   PHE B CE1   1 
ATOM   4417 C  CE2   . PHE B 1 58  ? -7.426  10.315  25.182  1 23.49   ? 50   PHE B CE2   1 
ATOM   4418 C  CZ    . PHE B 1 58  ? -7.012  10.818  26.425  1 23.641  ? 50   PHE B CZ    1 
ATOM   4419 N  N     . GLU B 1 59  ? -11.68  11.399  25.805  1 15.989  ? 51   GLU B N     1 
ATOM   4420 C  CA    . GLU B 1 59  ? -11.514 12.628  25.043  1 17.131  ? 51   GLU B CA    1 
ATOM   4421 C  C     . GLU B 1 59  ? -10.132 13.206  25.325  1 16.963  ? 51   GLU B C     1 
ATOM   4422 O  O     . GLU B 1 59  ? -9.849  13.562  26.466  1 16.64   ? 51   GLU B O     1 
ATOM   4423 C  CB    . GLU B 1 59  ? -12.602 13.677  25.279  1 17.531  ? 51   GLU B CB    1 
ATOM   4424 C  CG    . GLU B 1 59  ? -14.012 13.181  24.976  1 18.014  ? 51   GLU B CG    1 
ATOM   4425 C  CD    . GLU B 1 59  ? -14.988 14.329  25.145  1 20.522  ? 51   GLU B CD    1 
ATOM   4426 O  OE1   . GLU B 1 59  ? -15.25  14.726  26.311  1 20.011  ? 51   GLU B OE1   1 
ATOM   4427 O  OE2   . GLU B 1 59  ? -15.443 14.845  24.099  1 18.524  ? 51   GLU B OE2   1 
ATOM   4428 N  N     . GLY B 1 60  ? -9.299  13.266  24.279  1 15.842  ? 52   GLY B N     1 
ATOM   4429 C  CA    . GLY B 1 60  ? -7.99   13.896  24.35   1 17.11   ? 52   GLY B CA    1 
ATOM   4430 C  C     . GLY B 1 60  ? -7.024  13.39   23.277  1 18.535  ? 52   GLY B C     1 
ATOM   4431 O  O     . GLY B 1 60  ? -7.447  12.919  22.216  1 17.366  ? 52   GLY B O     1 
ATOM   4432 N  N     . THR B 1 61  ? -5.72   13.515  23.579  1 17.295  ? 53   THR B N     1 
ATOM   4433 C  CA    . THR B 1 61  ? -4.638  13.501  22.593  1 17.025  ? 53   THR B CA    1 
ATOM   4434 C  C     . THR B 1 61  ? -3.512  12.564  23.034  1 17.297  ? 53   THR B C     1 
ATOM   4435 O  O     . THR B 1 61  ? -3.334  12.329  24.232  1 18.922  ? 53   THR B O     1 
ATOM   4436 C  CB    . THR B 1 61  ? -4.094  14.899  22.265  1 15.322  ? 53   THR B CB    1 
ATOM   4437 O  OG1   . THR B 1 61  ? -3.586  15.483  23.457  1 16.752  ? 53   THR B OG1   1 
ATOM   4438 C  CG2   . THR B 1 61  ? -5.087  15.842  21.603  1 13.495  ? 53   THR B CG2   1 
ATOM   4439 N  N     . ILE B 1 62  ? -2.8    12.012  22.034  1 17.233  ? 54   ILE B N     1 
ATOM   4440 C  CA    . ILE B 1 62  ? -1.432  11.511  22.141  1 17.19   ? 54   ILE B CA    1 
ATOM   4441 C  C     . ILE B 1 62  ? -0.615  12.205  21.046  1 17.306  ? 54   ILE B C     1 
ATOM   4442 O  O     . ILE B 1 62  ? -0.926  12.08   19.862  1 17.501  ? 54   ILE B O     1 
ATOM   4443 C  CB    . ILE B 1 62  ? -1.336  9.965   22.099  1 16.264  ? 54   ILE B CB    1 
ATOM   4444 C  CG1   . ILE B 1 62  ? -2.102  9.312   23.248  1 16.711  ? 54   ILE B CG1   1 
ATOM   4445 C  CG2   . ILE B 1 62  ? 0.129   9.499   22.109  1 14.112  ? 54   ILE B CG2   1 
ATOM   4446 C  CD1   . ILE B 1 62  ? -2.7    7.948   22.985  1 16.899  ? 54   ILE B CD1   1 
ATOM   4447 N  N     . PHE B 1 63  ? 0.438   12.906  21.48   1 16.255  ? 55   PHE B N     1 
ATOM   4448 C  CA    . PHE B 1 63  ? 1.438   13.486  20.6    1 17.07   ? 55   PHE B CA    1 
ATOM   4449 C  C     . PHE B 1 63  ? 2.499   12.424  20.339  1 18.027  ? 55   PHE B C     1 
ATOM   4450 O  O     . PHE B 1 63  ? 3.037   11.834  21.29   1 18.023  ? 55   PHE B O     1 
ATOM   4451 C  CB    . PHE B 1 63  ? 2.014   14.754  21.238  1 17.656  ? 55   PHE B CB    1 
ATOM   4452 C  CG    . PHE B 1 63  ? 3.007   15.524  20.381  1 18.823  ? 55   PHE B CG    1 
ATOM   4453 C  CD1   . PHE B 1 63  ? 2.553   16.491  19.461  1 19.36   ? 55   PHE B CD1   1 
ATOM   4454 C  CD2   . PHE B 1 63  ? 4.399   15.32   20.535  1 19.882  ? 55   PHE B CD2   1 
ATOM   4455 C  CE1   . PHE B 1 63  ? 3.47    17.197  18.659  1 21.682  ? 55   PHE B CE1   1 
ATOM   4456 C  CE2   . PHE B 1 63  ? 5.319   16.051  19.758  1 20.83   ? 55   PHE B CE2   1 
ATOM   4457 C  CZ    . PHE B 1 63  ? 4.852   16.991  18.822  1 19.383  ? 55   PHE B CZ    1 
ATOM   4458 N  N     . ASP B 1 64  ? 2.788   12.208  19.045  1 17.497  ? 56   ASP B N     1 
ATOM   4459 C  CA    . ASP B 1 64  ? 3.857   11.328  18.582  1 19.16   ? 56   ASP B CA    1 
ATOM   4460 C  C     . ASP B 1 64  ? 3.563   9.886   19.026  1 18.369  ? 56   ASP B C     1 
ATOM   4461 O  O     . ASP B 1 64  ? 4.282   9.326   19.868  1 17.104  ? 56   ASP B O     1 
ATOM   4462 C  CB    . ASP B 1 64  ? 5.24    11.918  18.904  1 19.299  ? 56   ASP B CB    1 
ATOM   4463 C  CG    . ASP B 1 64  ? 6.418   11.432  18.071  1 20.554  ? 56   ASP B CG    1 
ATOM   4464 O  OD1   . ASP B 1 64  ? 6.212   10.664  17.1    1 20.852  ? 56   ASP B OD1   1 
ATOM   4465 O  OD2   . ASP B 1 64  ? 7.541   11.838  18.413  1 21.211  ? 56   ASP B OD2   1 
ATOM   4466 N  N     . VAL B 1 65  ? 2.438   9.34    18.514  1 17.289  ? 57   VAL B N     1 
ATOM   4467 C  CA    . VAL B 1 65  ? 1.965   7.969   18.735  1 17.721  ? 57   VAL B CA    1 
ATOM   4468 C  C     . VAL B 1 65  ? 3.096   7.005   18.348  1 17.488  ? 57   VAL B C     1 
ATOM   4469 O  O     . VAL B 1 65  ? 3.731   7.203   17.302  1 17.632  ? 57   VAL B O     1 
ATOM   4470 C  CB    . VAL B 1 65  ? 0.643   7.588   18.004  1 18.043  ? 57   VAL B CB    1 
ATOM   4471 C  CG1   . VAL B 1 65  ? 0.008   6.302   18.529  1 17.807  ? 57   VAL B CG1   1 
ATOM   4472 C  CG2   . VAL B 1 65  ? -0.405  8.687   18.042  1 16.573  ? 57   VAL B CG2   1 
ATOM   4473 N  N     . MET B 1 66  ? 3.34    6.005   19.219  1 16.978  ? 58   MET B N     1 
ATOM   4474 C  CA    . MET B 1 66  ? 4.313   4.947   18.98   1 20.068  ? 58   MET B CA    1 
ATOM   4475 C  C     . MET B 1 66  ? 3.936   4.19    17.708  1 20.334  ? 58   MET B C     1 
ATOM   4476 O  O     . MET B 1 66  ? 2.758   3.86    17.494  1 20.04   ? 58   MET B O     1 
ATOM   4477 C  CB    . MET B 1 66  ? 4.405   3.923   20.115  1 21.725  ? 58   MET B CB    1 
ATOM   4478 C  CG    . MET B 1 66  ? 4.897   4.421   21.454  1 28.486  ? 58   MET B CG    1 
ATOM   4479 S  SD    . MET B 1 66  ? 4.794   3.091   22.68   1 37.231  ? 58   MET B SD    1 
ATOM   4480 C  CE    . MET B 1 66  ? 3.006   2.855   22.777  1 40.408  ? 58   MET B CE    1 
ATOM   4481 N  N     . THR B 1 67  ? 4.949   4.019   16.846  1 19.198  ? 59   THR B N     1 
ATOM   4482 C  CA    . THR B 1 67  ? 4.822   3.326   15.57   1 21.962  ? 59   THR B CA    1 
ATOM   4483 C  C     . THR B 1 67  ? 5.829   2.173   15.49   1 23.514  ? 59   THR B C     1 
ATOM   4484 O  O     . THR B 1 67  ? 6.901   2.233   16.114  1 24.293  ? 59   THR B O     1 
ATOM   4485 C  CB    . THR B 1 67  ? 4.903   4.28    14.374  1 23.454  ? 59   THR B CB    1 
ATOM   4486 O  OG1   . THR B 1 67  ? 6.206   4.848   14.447  1 24.226  ? 59   THR B OG1   1 
ATOM   4487 C  CG2   . THR B 1 67  ? 3.85    5.379   14.389  1 19.889  ? 59   THR B CG2   1 
ATOM   4488 N  N     . ARG B 1 68  ? 5.442   1.122   14.755  1 21.418  ? 60   ARG B N     1 
ATOM   4489 C  CA    . ARG B 1 68  ? 6.296   -0.019  14.424  1 23.506  ? 60   ARG B CA    1 
ATOM   4490 C  C     . ARG B 1 68  ? 6.481   -0.063  12.907  1 22.916  ? 60   ARG B C     1 
ATOM   4491 O  O     . ARG B 1 68  ? 5.512   0.153   12.188  1 20.109  ? 60   ARG B O     1 
ATOM   4492 C  CB    . ARG B 1 68  ? 5.794   -1.368  14.943  1 23.12   ? 60   ARG B CB    1 
ATOM   4493 C  CG    . ARG B 1 68  ? 5.516   -1.493  16.434  1 26.241  ? 60   ARG B CG    1 
ATOM   4494 C  CD    . ARG B 1 68  ? 5.263   -2.923  16.917  1 27.549  ? 60   ARG B CD    1 
ATOM   4495 N  NE    . ARG B 1 68  ? 4.048   -3.562  16.377  1 30.358  ? 60   ARG B NE    1 
ATOM   4496 C  CZ    . ARG B 1 68  ? 2.733   -3.374  16.63   1 29.862  ? 60   ARG B CZ    1 
ATOM   4497 N  NH1   . ARG B 1 68  ? 2.293   -2.496  17.517  1 26.39   ? 60   ARG B NH1   1 
ATOM   4498 N  NH2   . ARG B 1 68  ? 1.835   -4.104  15.981  1 29.539  ? 60   ARG B NH2   1 
ATOM   4499 N  N     . GLY B 1 69  ? 7.728   -0.31   12.46   1 21.905  ? 61   GLY B N     1 
ATOM   4500 C  CA    . GLY B 1 69  ? 8.119   -0.224  11.055  1 26.567  ? 61   GLY B CA    1 
ATOM   4501 C  C     . GLY B 1 69  ? 8.261   1.227   10.593  1 27.024  ? 61   GLY B C     1 
ATOM   4502 O  O     . GLY B 1 69  ? 8.445   2.124   11.415  1 31.297  ? 61   GLY B O     1 
ATOM   4503 N  N     . THR B 1 70  ? 8.156   1.449   9.276   1 28.387  ? 62   THR B N     1 
ATOM   4504 C  CA    . THR B 1 70  ? 8.303   2.778   8.687   1 27.524  ? 62   THR B CA    1 
ATOM   4505 C  C     . THR B 1 70  ? 6.953   3.271   8.148   1 26.26   ? 62   THR B C     1 
ATOM   4506 O  O     . THR B 1 70  ? 6.35    2.647   7.271   1 23.493  ? 62   THR B O     1 
ATOM   4507 C  CB    . THR B 1 70  ? 9.467   2.833   7.686   1 29.027  ? 62   THR B CB    1 
ATOM   4508 O  OG1   . THR B 1 70  ? 10.62   2.514   8.468   1 32.384  ? 62   THR B OG1   1 
ATOM   4509 C  CG2   . THR B 1 70  ? 9.736   4.222   7.125   1 27.221  ? 62   THR B CG2   1 
ATOM   4510 N  N     . ILE B 1 71  ? 6.528   4.422   8.695   1 25.928  ? 63   ILE B N     1 
ATOM   4511 C  CA    . ILE B 1 71  ? 5.372   5.189   8.247   1 24.27   ? 63   ILE B CA    1 
ATOM   4512 C  C     . ILE B 1 71  ? 5.688   5.728   6.848   1 24.171  ? 63   ILE B C     1 
ATOM   4513 O  O     . ILE B 1 71  ? 6.636   6.501   6.739   1 23.996  ? 63   ILE B O     1 
ATOM   4514 C  CB    . ILE B 1 71  ? 4.921   6.261   9.278   1 24.56   ? 63   ILE B CB    1 
ATOM   4515 C  CG1   . ILE B 1 71  ? 4.524   5.664   10.698  1 23.28   ? 63   ILE B CG1   1 
ATOM   4516 C  CG2   . ILE B 1 71  ? 3.86    7.226   8.718   1 23.299  ? 63   ILE B CG2   1 
ATOM   4517 C  CD1   . ILE B 1 71  ? 3.25    4.811   10.776  1 23.762  ? 63   ILE B CD1   1 
ATOM   4518 N  N     . PRO B 1 72  ? 4.941   5.33    5.772   1 23.915  ? 64   PRO B N     1 
ATOM   4519 C  CA    . PRO B 1 72  ? 5.155   5.866   4.426   1 23.825  ? 64   PRO B CA    1 
ATOM   4520 C  C     . PRO B 1 72  ? 5.148   7.387   4.39    1 22.846  ? 64   PRO B C     1 
ATOM   4521 O  O     . PRO B 1 72  ? 4.263   8.015   4.987   1 22.404  ? 64   PRO B O     1 
ATOM   4522 C  CB    . PRO B 1 72  ? 4.071   5.222   3.559   1 23.315  ? 64   PRO B CB    1 
ATOM   4523 C  CG    . PRO B 1 72  ? 3.724   3.962   4.342   1 24.542  ? 64   PRO B CG    1 
ATOM   4524 C  CD    . PRO B 1 72  ? 3.84    4.343   5.78    1 24.079  ? 64   PRO B CD    1 
ATOM   4525 N  N     . LYS B 1 73  ? 6.203   7.935   3.761   1 24.781  ? 65   LYS B N     1 
ATOM   4526 C  CA    . LYS B 1 73  ? 6.384   9.376   3.571   1 30.66   ? 65   LYS B CA    1 
ATOM   4527 C  C     . LYS B 1 73  ? 5.306   9.983   2.661   1 27.053  ? 65   LYS B C     1 
ATOM   4528 O  O     . LYS B 1 73  ? 5.028   11.177  2.769   1 26.721  ? 65   LYS B O     1 
ATOM   4529 C  CB    . LYS B 1 73  ? 7.836   9.788   3.272   1 35.639  ? 65   LYS B CB    1 
ATOM   4530 C  CG    . LYS B 1 73  ? 8.841   9.775   4.454   1 46.23   ? 65   LYS B CG    1 
ATOM   4531 C  CD    . LYS B 1 73  ? 8.605   10.717  5.643   1 52.531  ? 65   LYS B CD    1 
ATOM   4532 C  CE    . LYS B 1 73  ? 9.738   11.098  6.543   1 57.786  ? 65   LYS B CE    1 
ATOM   4533 N  NZ    . LYS B 1 73  ? 10.614  12.109  5.939   1 62.189  ? 65   LYS B NZ    1 
ATOM   4534 N  N     . GLU B 1 74  ? 4.685   9.143   1.814   1 28.203  ? 66   GLU B N     1 
ATOM   4535 C  CA    . GLU B 1 74  ? 3.598   9.482   0.892   1 28.807  ? 66   GLU B CA    1 
ATOM   4536 C  C     . GLU B 1 74  ? 2.293   9.818   1.635   1 27.843  ? 66   GLU B C     1 
ATOM   4537 O  O     . GLU B 1 74  ? 1.425   10.476  1.056   1 29.234  ? 66   GLU B O     1 
ATOM   4538 C  CB    . GLU B 1 74  ? 3.331   8.423   -0.18   1 29.953  ? 66   GLU B CB    1 
ATOM   4539 C  CG    . GLU B 1 74  ? 4.533   7.988   -1.017  1 32.825  ? 66   GLU B CG    1 
ATOM   4540 C  CD    . GLU B 1 74  ? 5.508   6.947   -0.474  1 35.639  ? 66   GLU B CD    1 
ATOM   4541 O  OE1   . GLU B 1 74  ? 5.481   6.529   0.712   1 38.472  ? 66   GLU B OE1   1 
ATOM   4542 O  OE2   . GLU B 1 74  ? 6.328   6.516   -1.301  1 39.375  ? 66   GLU B OE2   1 
ATOM   4543 N  N     . LEU B 1 75  ? 2.148   9.38    2.903   1 25.948  ? 67   LEU B N     1 
ATOM   4544 C  CA    . LEU B 1 75  ? 0.988   9.704   3.738   1 22.891  ? 67   LEU B CA    1 
ATOM   4545 C  C     . LEU B 1 75  ? 1.091   11.141  4.258   1 22.865  ? 67   LEU B C     1 
ATOM   4546 O  O     . LEU B 1 75  ? 2.055   11.495  4.95    1 23.439  ? 67   LEU B O     1 
ATOM   4547 C  CB    . LEU B 1 75  ? 0.73    8.681   4.849   1 20.881  ? 67   LEU B CB    1 
ATOM   4548 C  CG    . LEU B 1 75  ? 0.372   7.251   4.425   1 20.097  ? 67   LEU B CG    1 
ATOM   4549 C  CD1   . LEU B 1 75  ? 0.359   6.351   5.658   1 19.565  ? 67   LEU B CD1   1 
ATOM   4550 C  CD2   . LEU B 1 75  ? -0.944  7.14    3.645   1 21.099  ? 67   LEU B CD2   1 
ATOM   4551 N  N     . HIS B 1 76  ? 0.107   11.963  3.862   1 22.282  ? 68   HIS B N     1 
ATOM   4552 C  CA    . HIS B 1 76  ? 0.046   13.398  4.145   1 22.252  ? 68   HIS B CA    1 
ATOM   4553 C  C     . HIS B 1 76  ? -1.421  13.808  4.32    1 21.178  ? 68   HIS B C     1 
ATOM   4554 O  O     . HIS B 1 76  ? -2.059  14.292  3.386   1 22.097  ? 68   HIS B O     1 
ATOM   4555 C  CB    . HIS B 1 76  ? 0.865   14.185  3.109   1 21.673  ? 68   HIS B CB    1 
ATOM   4556 C  CG    . HIS B 1 76  ? 1.079   15.616  3.458   1 21.964  ? 68   HIS B CG    1 
ATOM   4557 N  ND1   . HIS B 1 76  ? 2.036   16.028  4.354   1 21.822  ? 68   HIS B ND1   1 
ATOM   4558 C  CD2   . HIS B 1 76  ? 0.476   16.738  3.027   1 21.94   ? 68   HIS B CD2   1 
ATOM   4559 C  CE1   . HIS B 1 76  ? 1.987   17.354  4.47    1 20.642  ? 68   HIS B CE1   1 
ATOM   4560 N  NE2   . HIS B 1 76  ? 1.052   17.799  3.675   1 20.798  ? 68   HIS B NE2   1 
ATOM   4561 N  N     . GLY B 1 77  ? -1.942  13.603  5.533   1 20.046  ? 69   GLY B N     1 
ATOM   4562 C  CA    . GLY B 1 77  ? -3.378  13.72   5.792   1 21.993  ? 69   GLY B CA    1 
ATOM   4563 C  C     . GLY B 1 77  ? -3.79   13.094  7.115   1 22.225  ? 69   GLY B C     1 
ATOM   4564 O  O     . GLY B 1 77  ? -2.936  12.864  7.98    1 25.723  ? 69   GLY B O     1 
ATOM   4565 N  N     . THR B 1 78  ? -5.103  12.841  7.246   1 19.619  ? 70   THR B N     1 
ATOM   4566 C  CA    . THR B 1 78  ? -5.713  12.368  8.479   1 19.11   ? 70   THR B CA    1 
ATOM   4567 C  C     . THR B 1 78  ? -6.657  11.205  8.175   1 18.998  ? 70   THR B C     1 
ATOM   4568 O  O     . THR B 1 78  ? -7.485  11.289  7.253   1 17.997  ? 70   THR B O     1 
ATOM   4569 C  CB    . THR B 1 78  ? -6.399  13.511  9.237   1 19.099  ? 70   THR B CB    1 
ATOM   4570 O  OG1   . THR B 1 78  ? -5.63   14.709  9.225   1 19.029  ? 70   THR B OG1   1 
ATOM   4571 C  CG2   . THR B 1 78  ? -6.684  13.181  10.692  1 18.817  ? 70   THR B CG2   1 
ATOM   4572 N  N     . PHE B 1 79  ? -6.493  10.132  8.968   1 17.02   ? 71   PHE B N     1 
ATOM   4573 C  CA    . PHE B 1 79  ? -7.468  9.064   9.05    1 16.63   ? 71   PHE B CA    1 
ATOM   4574 C  C     . PHE B 1 79  ? -8.429  9.421   10.179  1 17.072  ? 71   PHE B C     1 
ATOM   4575 O  O     . PHE B 1 79  ? -8.051  9.346   11.346  1 18.506  ? 71   PHE B O     1 
ATOM   4576 C  CB    . PHE B 1 79  ? -6.768  7.703   9.144   1 16.122  ? 71   PHE B CB    1 
ATOM   4577 C  CG    . PHE B 1 79  ? -7.617  6.441   9.249   1 17.047  ? 71   PHE B CG    1 
ATOM   4578 C  CD1   . PHE B 1 79  ? -8.975  6.39    8.841   1 18.39   ? 71   PHE B CD1   1 
ATOM   4579 C  CD2   . PHE B 1 79  ? -7.034  5.271   9.754   1 16.249  ? 71   PHE B CD2   1 
ATOM   4580 C  CE1   . PHE B 1 79  ? -9.726  5.212   8.954   1 18.182  ? 71   PHE B CE1   1 
ATOM   4581 C  CE2   . PHE B 1 79  ? -7.775  4.086   9.876   1 16.957  ? 71   PHE B CE2   1 
ATOM   4582 C  CZ    . PHE B 1 79  ? -9.112  4.05    9.456   1 18.374  ? 71   PHE B CZ    1 
ATOM   4583 N  N     . TYR B 1 80  ? -9.649  9.835   9.792   1 17.571  ? 72   TYR B N     1 
ATOM   4584 C  CA    . TYR B 1 80  ? -10.743 10.149  10.712  1 17.99   ? 72   TYR B CA    1 
ATOM   4585 C  C     . TYR B 1 80  ? -11.7   8.968   10.764  1 18.988  ? 72   TYR B C     1 
ATOM   4586 O  O     . TYR B 1 80  ? -12.229 8.566   9.734   1 20.963  ? 72   TYR B O     1 
ATOM   4587 C  CB    . TYR B 1 80  ? -11.593 11.386  10.422  1 16.75   ? 72   TYR B CB    1 
ATOM   4588 C  CG    . TYR B 1 80  ? -10.869 12.719  10.446  1 18.228  ? 72   TYR B CG    1 
ATOM   4589 C  CD1   . TYR B 1 80  ? -10.721 13.447  11.633  1 16.648  ? 72   TYR B CD1   1 
ATOM   4590 C  CD2   . TYR B 1 80  ? -10.357 13.262  9.259   1 17.571  ? 72   TYR B CD2   1 
ATOM   4591 C  CE1   . TYR B 1 80  ? -10.11  14.7    11.626  1 17.868  ? 72   TYR B CE1   1 
ATOM   4592 C  CE2   . TYR B 1 80  ? -9.761  14.518  9.242   1 18.322  ? 72   TYR B CE2   1 
ATOM   4593 C  CZ    . TYR B 1 80  ? -9.605  15.217  10.437  1 19.335  ? 72   TYR B CZ    1 
ATOM   4594 O  OH    . TYR B 1 80  ? -8.968  16.426  10.421  1 21.816  ? 72   TYR B OH    1 
ATOM   4595 N  N     . ARG B 1 81  ? -11.904 8.465   11.983  1 18.473  ? 73   ARG B N     1 
ATOM   4596 C  CA    . ARG B 1 81  ? -12.776 7.342   12.272  1 17.64   ? 73   ARG B CA    1 
ATOM   4597 C  C     . ARG B 1 81  ? -13.829 7.789   13.278  1 16.569  ? 73   ARG B C     1 
ATOM   4598 O  O     . ARG B 1 81  ? -13.526 8.527   14.206  1 17.299  ? 73   ARG B O     1 
ATOM   4599 C  CB    . ARG B 1 81  ? -11.799 6.292   12.803  1 17.655  ? 73   ARG B CB    1 
ATOM   4600 C  CG    . ARG B 1 81  ? -12.39  4.902   12.834  1 18.703  ? 73   ARG B CG    1 
ATOM   4601 C  CD    . ARG B 1 81  ? -12.152 4.06    11.599  1 17.573  ? 73   ARG B CD    1 
ATOM   4602 N  NE    . ARG B 1 81  ? -12.86  2.851   12.03   1 18.194  ? 73   ARG B NE    1 
ATOM   4603 C  CZ    . ARG B 1 81  ? -13.929 2.269   11.492  1 17.518  ? 73   ARG B CZ    1 
ATOM   4604 N  NH1   . ARG B 1 81  ? -14.335 2.512   10.251  1 16.269  ? 73   ARG B NH1   1 
ATOM   4605 N  NH2   . ARG B 1 81  ? -14.541 1.361   12.215  1 18.859  ? 73   ARG B NH2   1 
ATOM   4606 N  N     . ILE B 1 82  ? -15.058 7.303   13.094  1 16.776  ? 74   ILE B N     1 
ATOM   4607 C  CA    . ILE B 1 82  ? -16.172 7.633   13.979  1 15.939  ? 74   ILE B CA    1 
ATOM   4608 C  C     . ILE B 1 82  ? -16.777 6.355   14.554  1 15.76   ? 74   ILE B C     1 
ATOM   4609 O  O     . ILE B 1 82  ? -16.891 5.342   13.861  1 15.292  ? 74   ILE B O     1 
ATOM   4610 C  CB    . ILE B 1 82  ? -17.149 8.608   13.282  1 14.832  ? 74   ILE B CB    1 
ATOM   4611 C  CG1   . ILE B 1 82  ? -18.032 9.421   14.255  1 15.962  ? 74   ILE B CG1   1 
ATOM   4612 C  CG2   . ILE B 1 82  ? -17.957 7.937   12.163  1 15.072  ? 74   ILE B CG2   1 
ATOM   4613 C  CD1   . ILE B 1 82  ? -18.763 10.616  13.627  1 13.12   ? 74   ILE B CD1   1 
ATOM   4614 N  N     . MET B 1 83  ? -17.157 6.446   15.842  1 15.57   ? 75   MET B N     1 
ATOM   4615 C  CA    . MET B 1 83  ? -17.575 5.294   16.633  1 15.689  ? 75   MET B CA    1 
ATOM   4616 C  C     . MET B 1 83  ? -18.818 5.626   17.461  1 16.3    ? 75   MET B C     1 
ATOM   4617 O  O     . MET B 1 83  ? -18.948 6.789   17.868  1 15.635  ? 75   MET B O     1 
ATOM   4618 C  CB    . MET B 1 83  ? -16.486 4.866   17.625  1 14.98   ? 75   MET B CB    1 
ATOM   4619 C  CG    . MET B 1 83  ? -15.191 4.394   17.015  1 16.474  ? 75   MET B CG    1 
ATOM   4620 S  SD    . MET B 1 83  ? -13.725 4.884   17.949  1 19.405  ? 75   MET B SD    1 
ATOM   4621 C  CE    . MET B 1 83  ? -13.576 6.473   17.122  1 19.024  ? 75   MET B CE    1 
ATOM   4622 N  N     . PRO B 1 84  ? -19.736 4.638   17.741  1 16.215  ? 76   PRO B N     1 
ATOM   4623 C  CA    . PRO B 1 84  ? -20.74  4.777   18.796  1 15.218  ? 76   PRO B CA    1 
ATOM   4624 C  C     . PRO B 1 84  ? -20.149 4.449   20.171  1 17.301  ? 76   PRO B C     1 
ATOM   4625 O  O     . PRO B 1 84  ? -19.548 3.374   20.358  1 17.572  ? 76   PRO B O     1 
ATOM   4626 C  CB    . PRO B 1 84  ? -21.855 3.846   18.344  1 15.267  ? 76   PRO B CB    1 
ATOM   4627 C  CG    . PRO B 1 84  ? -21.106 2.719   17.64   1 16.052  ? 76   PRO B CG    1 
ATOM   4628 C  CD    . PRO B 1 84  ? -19.835 3.314   17.083  1 16.292  ? 76   PRO B CD    1 
ATOM   4629 N  N     . ASP B 1 85  ? -20.255 5.41    21.102  1 16.107  ? 77   ASP B N     1 
ATOM   4630 C  CA    . ASP B 1 85  ? -19.669 5.267   22.43   1 16.088  ? 77   ASP B CA    1 
ATOM   4631 C  C     . ASP B 1 85  ? -20.516 6.05    23.413  1 14.759  ? 77   ASP B C     1 
ATOM   4632 O  O     . ASP B 1 85  ? -20.149 7.165   23.75   1 14.451  ? 77   ASP B O     1 
ATOM   4633 C  CB    . ASP B 1 85  ? -18.197 5.684   22.437  1 17.032  ? 77   ASP B CB    1 
ATOM   4634 C  CG    . ASP B 1 85  ? -17.253 5.071   23.47   1 19.221  ? 77   ASP B CG    1 
ATOM   4635 O  OD1   . ASP B 1 85  ? -17.667 4.121   24.232  1 18.72   ? 77   ASP B OD1   1 
ATOM   4636 O  OD2   . ASP B 1 85  ? -16.059 5.495   23.451  1 18.744  ? 77   ASP B OD2   1 
ATOM   4637 N  N     . TYR B 1 86  ? -21.663 5.469   23.826  1 15.553  ? 78   TYR B N     1 
ATOM   4638 C  CA    . TYR B 1 86  ? -22.591 6.093   24.766  1 16.01   ? 78   TYR B CA    1 
ATOM   4639 C  C     . TYR B 1 86  ? -21.832 6.784   25.896  1 16.346  ? 78   TYR B C     1 
ATOM   4640 O  O     . TYR B 1 86  ? -21.068 6.119   26.603  1 17.07   ? 78   TYR B O     1 
ATOM   4641 C  CB    . TYR B 1 86  ? -23.51  4.988   25.283  1 16.246  ? 78   TYR B CB    1 
ATOM   4642 C  CG    . TYR B 1 86  ? -24.901 4.905   24.673  1 17.176  ? 78   TYR B CG    1 
ATOM   4643 C  CD1   . TYR B 1 86  ? -25.761 6.022   24.628  1 18.192  ? 78   TYR B CD1   1 
ATOM   4644 C  CD2   . TYR B 1 86  ? -25.369 3.68    24.18   1 19.371  ? 78   TYR B CD2   1 
ATOM   4645 C  CE1   . TYR B 1 86  ? -27.043 5.917   24.087  1 19.004  ? 78   TYR B CE1   1 
ATOM   4646 C  CE2   . TYR B 1 86  ? -26.657 3.568   23.646  1 18.928  ? 78   TYR B CE2   1 
ATOM   4647 C  CZ    . TYR B 1 86  ? -27.487 4.686   23.611  1 17.634  ? 78   TYR B CZ    1 
ATOM   4648 O  OH    . TYR B 1 86  ? -28.755 4.56    23.137  1 19.56   ? 78   TYR B OH    1 
ATOM   4649 N  N     . ALA B 1 87  ? -21.944 8.119   25.938  1 15.625  ? 79   ALA B N     1 
ATOM   4650 C  CA    . ALA B 1 87  ? -21.224 8.963   26.894  1 16.747  ? 79   ALA B CA    1 
ATOM   4651 C  C     . ALA B 1 87  ? -21.733 8.763   28.333  1 18.473  ? 79   ALA B C     1 
ATOM   4652 O  O     . ALA B 1 87  ? -20.922 8.721   29.269  1 18.432  ? 79   ALA B O     1 
ATOM   4653 C  CB    . ALA B 1 87  ? -21.221 10.406  26.427  1 15.213  ? 79   ALA B CB    1 
ATOM   4654 N  N     . GLN B 1 88  ? -23.066 8.621   28.491  1 18.887  ? 80   GLN B N     1 
ATOM   4655 C  CA    . GLN B 1 88  ? -23.748 8.293   29.743  1 18.561  ? 80   GLN B CA    1 
ATOM   4656 C  C     . GLN B 1 88  ? -24.337 6.883   29.691  1 17.61   ? 80   GLN B C     1 
ATOM   4657 O  O     . GLN B 1 88  ? -24.764 6.491   28.604  1 18.087  ? 80   GLN B O     1 
ATOM   4658 C  CB    . GLN B 1 88  ? -24.849 9.309   30.069  1 18.033  ? 80   GLN B CB    1 
ATOM   4659 C  CG    . GLN B 1 88  ? -24.363 10.727  30.366  1 19.335  ? 80   GLN B CG    1 
ATOM   4660 C  CD    . GLN B 1 88  ? -23.295 10.851  31.439  1 22.462  ? 80   GLN B CD    1 
ATOM   4661 O  OE1   . GLN B 1 88  ? -22.234 11.427  31.179  1 22.7    ? 80   GLN B OE1   1 
ATOM   4662 N  NE2   . GLN B 1 88  ? -23.537 10.312  32.635  1 23.561  ? 80   GLN B NE2   1 
ATOM   4663 N  N     . PRO B 1 89  ? -24.433 6.102   30.817  1 18.886  ? 81   PRO B N     1 
ATOM   4664 C  CA    . PRO B 1 89  ? -25.175 4.833   30.811  1 19.388  ? 81   PRO B CA    1 
ATOM   4665 C  C     . PRO B 1 89  ? -26.625 5.024   30.333  1 19.913  ? 81   PRO B C     1 
ATOM   4666 O  O     . PRO B 1 89  ? -27.324 5.86    30.92   1 20.442  ? 81   PRO B O     1 
ATOM   4667 C  CB    . PRO B 1 89  ? -25.036 4.275   32.227  1 19.757  ? 81   PRO B CB    1 
ATOM   4668 C  CG    . PRO B 1 89  ? -24.694 5.52    33.054  1 19.441  ? 81   PRO B CG    1 
ATOM   4669 C  CD    . PRO B 1 89  ? -23.881 6.389   32.16   1 17.879  ? 81   PRO B CD    1 
ATOM   4670 N  N     . PRO B 1 90  ? -27.062 4.387   29.198  1 19.522  ? 82   PRO B N     1 
ATOM   4671 C  CA    . PRO B 1 90  ? -28.305 4.747   28.521  1 19.148  ? 82   PRO B CA    1 
ATOM   4672 C  C     . PRO B 1 90  ? -29.604 4.249   29.178  1 19.196  ? 82   PRO B C     1 
ATOM   4673 O  O     . PRO B 1 90  ? -30.455 3.701   28.494  1 19.497  ? 82   PRO B O     1 
ATOM   4674 C  CB    . PRO B 1 90  ? -27.997 4.355   27.077  1 18.561  ? 82   PRO B CB    1 
ATOM   4675 C  CG    . PRO B 1 90  ? -27.246 3.06    27.275  1 18.192  ? 82   PRO B CG    1 
ATOM   4676 C  CD    . PRO B 1 90  ? -26.31  3.399   28.388  1 19.033  ? 82   PRO B CD    1 
ATOM   4677 N  N     . THR B 1 91  ? -29.808 4.584   30.46   1 19.462  ? 83   THR B N     1 
ATOM   4678 C  CA    . THR B 1 91  ? -30.797 3.944   31.325  1 19.396  ? 83   THR B CA    1 
ATOM   4679 C  C     . THR B 1 91  ? -32.209 4.553   31.246  1 19.379  ? 83   THR B C     1 
ATOM   4680 O  O     . THR B 1 91  ? -33.103 4.025   31.918  1 18.678  ? 83   THR B O     1 
ATOM   4681 C  CB    . THR B 1 91  ? -30.301 3.874   32.777  1 18.768  ? 83   THR B CB    1 
ATOM   4682 O  OG1   . THR B 1 91  ? -30.06  5.223   33.148  1 19.064  ? 83   THR B OG1   1 
ATOM   4683 C  CG2   . THR B 1 91  ? -29.101 2.978   32.993  1 19.868  ? 83   THR B CG2   1 
ATOM   4684 N  N     . TYR B 1 92  ? -32.432 5.629   30.452  1 19.996  ? 84   TYR B N     1 
ATOM   4685 C  CA    . TYR B 1 92  ? -33.689 6.393   30.427  1 19.956  ? 84   TYR B CA    1 
ATOM   4686 C  C     . TYR B 1 92  ? -34.901 5.473   30.163  1 20.674  ? 84   TYR B C     1 
ATOM   4687 O  O     . TYR B 1 92  ? -35.876 5.536   30.928  1 17.178  ? 84   TYR B O     1 
ATOM   4688 C  CB    . TYR B 1 92  ? -33.756 7.708   29.61   1 20.959  ? 84   TYR B CB    1 
ATOM   4689 C  CG    . TYR B 1 92  ? -35.145 8.345   29.622  1 19.918  ? 84   TYR B CG    1 
ATOM   4690 C  CD1   . TYR B 1 92  ? -35.602 9.107   30.715  1 18.851  ? 84   TYR B CD1   1 
ATOM   4691 C  CD2   . TYR B 1 92  ? -36.049 8.083   28.577  1 20.747  ? 84   TYR B CD2   1 
ATOM   4692 C  CE1   . TYR B 1 92  ? -36.914 9.583   30.774  1 19.02   ? 84   TYR B CE1   1 
ATOM   4693 C  CE2   . TYR B 1 92  ? -37.356 8.567   28.628  1 20.78   ? 84   TYR B CE2   1 
ATOM   4694 C  CZ    . TYR B 1 92  ? -37.783 9.31    29.723  1 19.781  ? 84   TYR B CZ    1 
ATOM   4695 O  OH    . TYR B 1 92  ? -39.065 9.741   29.648  1 18.016  ? 84   TYR B OH    1 
ATOM   4696 N  N     . TYR B 1 93  ? -34.861 4.697   29.058  1 21.489  ? 85   TYR B N     1 
ATOM   4697 C  CA    . TYR B 1 93  ? -36.004 3.896   28.628  1 20.466  ? 85   TYR B CA    1 
ATOM   4698 C  C     . TYR B 1 93  ? -35.74  2.417   28.883  1 20.12   ? 85   TYR B C     1 
ATOM   4699 O  O     . TYR B 1 93  ? -34.794 1.866   28.319  1 22.366  ? 85   TYR B O     1 
ATOM   4700 C  CB    . TYR B 1 93  ? -36.426 4.204   27.191  1 21.248  ? 85   TYR B CB    1 
ATOM   4701 C  CG    . TYR B 1 93  ? -37.725 3.548   26.737  1 23.466  ? 85   TYR B CG    1 
ATOM   4702 C  CD1   . TYR B 1 93  ? -38.975 4.026   27.194  1 24.14   ? 85   TYR B CD1   1 
ATOM   4703 C  CD2   . TYR B 1 93  ? -37.709 2.473   25.836  1 20.952  ? 85   TYR B CD2   1 
ATOM   4704 C  CE1   . TYR B 1 93  ? -40.167 3.439   26.777  1 24.82   ? 85   TYR B CE1   1 
ATOM   4705 C  CE2   . TYR B 1 93  ? -38.894 1.895   25.395  1 23.057  ? 85   TYR B CE2   1 
ATOM   4706 C  CZ    . TYR B 1 93  ? -40.116 2.374   25.884  1 25.512  ? 85   TYR B CZ    1 
ATOM   4707 O  OH    . TYR B 1 93  ? -41.302 1.836   25.495  1 30.239  ? 85   TYR B OH    1 
ATOM   4708 N  N     . LYS B 1 94  ? -36.601 1.808   29.723  1 19.322  ? 86   LYS B N     1 
ATOM   4709 C  CA    . LYS B 1 94  ? -36.594 0.397   30.126  1 21.185  ? 86   LYS B CA    1 
ATOM   4710 C  C     . LYS B 1 94  ? -35.195 -0.074  30.562  1 19.025  ? 86   LYS B C     1 
ATOM   4711 O  O     . LYS B 1 94  ? -34.724 -1.155  30.171  1 18.426  ? 86   LYS B O     1 
ATOM   4712 C  CB    . LYS B 1 94  ? -37.218 -0.467  29.016  1 21.97   ? 86   LYS B CB    1 
ATOM   4713 C  CG    . LYS B 1 94  ? -38.693 -0.247  28.703  1 24.853  ? 86   LYS B CG    1 
ATOM   4714 C  CD    . LYS B 1 94  ? -39.135 -1.095  27.515  1 26.216  ? 86   LYS B CD    1 
ATOM   4715 C  CE    . LYS B 1 94  ? -40.607 -0.938  27.311  1 28.284  ? 86   LYS B CE    1 
ATOM   4716 N  NZ    . LYS B 1 94  ? -40.949 -1.589  26.045  1 33.462  ? 86   LYS B NZ    1 
ATOM   4717 N  N     . GLY B 1 95  ? -34.514 0.797   31.325  1 19.67   ? 87   GLY B N     1 
ATOM   4718 C  CA    . GLY B 1 95  ? -33.157 0.627   31.847  1 18.694  ? 87   GLY B CA    1 
ATOM   4719 C  C     . GLY B 1 95  ? -32.078 0.452   30.773  1 19.278  ? 87   GLY B C     1 
ATOM   4720 O  O     . GLY B 1 95  ? -31.041 -0.125  31.074  1 20.233  ? 87   GLY B O     1 
ATOM   4721 N  N     . GLY B 1 96  ? -32.341 0.944   29.543  1 20.594  ? 88   GLY B N     1 
ATOM   4722 C  CA    . GLY B 1 96  ? -31.527 0.797   28.345  1 21.559  ? 88   GLY B CA    1 
ATOM   4723 C  C     . GLY B 1 96  ? -31.413 -0.621  27.784  1 22.294  ? 88   GLY B C     1 
ATOM   4724 O  O     . GLY B 1 96  ? -30.485 -0.873  27.002  1 21.23   ? 88   GLY B O     1 
ATOM   4725 N  N     . GLU B 1 97  ? -32.376 -1.502  28.109  1 22.714  ? 89   GLU B N     1 
ATOM   4726 C  CA    . GLU B 1 97  ? -32.357 -2.91   27.703  1 24.945  ? 89   GLU B CA    1 
ATOM   4727 C  C     . GLU B 1 97  ? -32.453 -3.094  26.182  1 21.612  ? 89   GLU B C     1 
ATOM   4728 O  O     . GLU B 1 97  ? -31.988 -4.107  25.667  1 21.493  ? 89   GLU B O     1 
ATOM   4729 C  CB    . GLU B 1 97  ? -33.432 -3.752  28.391  1 31.477  ? 89   GLU B CB    1 
ATOM   4730 C  CG    . GLU B 1 97  ? -33.095 -4.075  29.844  1 49.352  ? 89   GLU B CG    1 
ATOM   4731 C  CD    . GLU B 1 97  ? -34.073 -4.994  30.553  1 61.41   ? 89   GLU B CD    1 
ATOM   4732 O  OE1   . GLU B 1 97  ? -35.306 -4.72   30.596  1 66.287  ? 89   GLU B OE1   1 
ATOM   4733 O  OE2   . GLU B 1 97  ? -33.561 -6.011  31.078  1 61.83   ? 89   GLU B OE2   1 
ATOM   4734 N  N     . LEU B 1 98  ? -33.039 -2.117  25.474  1 20.295  ? 90   LEU B N     1 
ATOM   4735 C  CA    . LEU B 1 98  ? -33.304 -2.195  24.047  1 20.503  ? 90   LEU B CA    1 
ATOM   4736 C  C     . LEU B 1 98  ? -32.443 -1.206  23.251  1 19.852  ? 90   LEU B C     1 
ATOM   4737 O  O     . LEU B 1 98  ? -32.764 -0.919  22.089  1 19.585  ? 90   LEU B O     1 
ATOM   4738 C  CB    . LEU B 1 98  ? -34.809 -2.115  23.741  1 21.707  ? 90   LEU B CB    1 
ATOM   4739 C  CG    . LEU B 1 98  ? -35.747 -3.154  24.378  1 23.011  ? 90   LEU B CG    1 
ATOM   4740 C  CD1   . LEU B 1 98  ? -37.168 -2.65   24.174  1 24.156  ? 90   LEU B CD1   1 
ATOM   4741 C  CD2   . LEU B 1 98  ? -35.563 -4.61   23.874  1 22.153  ? 90   LEU B CD2   1 
ATOM   4742 N  N     . ASN B 1 99  ? -31.319 -0.752  23.843  1 18.053  ? 91   ASN B N     1 
ATOM   4743 C  CA    . ASN B 1 99  ? -30.299 0.045   23.152  1 19.517  ? 91   ASN B CA    1 
ATOM   4744 C  C     . ASN B 1 99  ? -29.698 -0.791  22.016  1 19.155  ? 91   ASN B C     1 
ATOM   4745 O  O     . ASN B 1 99  ? -29.457 -1.983  22.201  1 18.392  ? 91   ASN B O     1 
ATOM   4746 C  CB    . ASN B 1 99  ? -29.323 0.722   24.119  1 18.418  ? 91   ASN B CB    1 
ATOM   4747 C  CG    . ASN B 1 99  ? -28.13  -0.139  24.482  1 19.64   ? 91   ASN B CG    1 
ATOM   4748 O  OD1   . ASN B 1 99  ? -27.179 -0.294  23.69   1 18.053  ? 91   ASN B OD1   1 
ATOM   4749 N  ND2   . ASN B 1 99  ? -28.15  -0.697  25.686  1 20.533  ? 91   ASN B ND2   1 
ATOM   4750 N  N     . ALA B 1 100 ? -29.498 -0.146  20.861  1 20.004  ? 92   ALA B N     1 
ATOM   4751 C  CA    . ALA B 1 100 ? -28.995 -0.765  19.641  1 19.534  ? 92   ALA B CA    1 
ATOM   4752 C  C     . ALA B 1 100 ? -27.507 -0.434  19.464  1 19.521  ? 92   ALA B C     1 
ATOM   4753 O  O     . ALA B 1 100 ? -27.069 0.608   19.959  1 19.407  ? 92   ALA B O     1 
ATOM   4754 C  CB    . ALA B 1 100 ? -29.84  -0.323  18.46   1 20.595  ? 92   ALA B CB    1 
ATOM   4755 N  N     . PRO B 1 101 ? -26.666 -1.277  18.788  1 19.141  ? 93   PRO B N     1 
ATOM   4756 C  CA    . PRO B 1 101 ? -25.251 -0.958  18.559  1 18.383  ? 93   PRO B CA    1 
ATOM   4757 C  C     . PRO B 1 101 ? -24.966 0.34    17.806  1 19.69   ? 93   PRO B C     1 
ATOM   4758 O  O     . PRO B 1 101 ? -23.872 0.903   17.945  1 19.136  ? 93   PRO B O     1 
ATOM   4759 C  CB    . PRO B 1 101 ? -24.682 -2.201  17.862  1 18.041  ? 93   PRO B CB    1 
ATOM   4760 C  CG    . PRO B 1 101 ? -25.906 -2.824  17.255  1 17.178  ? 93   PRO B CG    1 
ATOM   4761 C  CD    . PRO B 1 101 ? -26.958 -2.643  18.306  1 17.685  ? 93   PRO B CD    1 
ATOM   4762 N  N     . ILE B 1 102 ? -25.971 0.789   17.034  1 19.067  ? 94   ILE B N     1 
ATOM   4763 C  CA    . ILE B 1 102 ? -25.932 1.959   16.164  1 19.07   ? 94   ILE B CA    1 
ATOM   4764 C  C     . ILE B 1 102 ? -26.346 3.235   16.905  1 18.796  ? 94   ILE B C     1 
ATOM   4765 O  O     . ILE B 1 102 ? -26.346 4.309   16.29   1 18.036  ? 94   ILE B O     1 
ATOM   4766 C  CB    . ILE B 1 102 ? -26.714 1.72    14.852  1 19.324  ? 94   ILE B CB    1 
ATOM   4767 C  CG1   . ILE B 1 102 ? -28.245 1.411   15.078  1 19.277  ? 94   ILE B CG1   1 
ATOM   4768 C  CG2   . ILE B 1 102 ? -25.982 0.677   13.992  1 22.685  ? 94   ILE B CG2   1 
ATOM   4769 C  CD1   . ILE B 1 102 ? -29.123 1.422   13.837  1 18.222  ? 94   ILE B CD1   1 
ATOM   4770 N  N     . ASP B 1 103 ? -26.674 3.118   18.21   1 19.097  ? 95   ASP B N     1 
ATOM   4771 C  CA    . ASP B 1 103 ? -27.266 4.196   18.998  1 20.236  ? 95   ASP B CA    1 
ATOM   4772 C  C     . ASP B 1 103 ? -26.255 5.222   19.519  1 19.792  ? 95   ASP B C     1 
ATOM   4773 O  O     . ASP B 1 103 ? -26.544 6.42    19.436  1 19.387  ? 95   ASP B O     1 
ATOM   4774 C  CB    . ASP B 1 103 ? -28.102 3.685   20.162  1 21.001  ? 95   ASP B CB    1 
ATOM   4775 C  CG    . ASP B 1 103 ? -29.596 3.533   19.94   1 24.384  ? 95   ASP B CG    1 
ATOM   4776 O  OD1   . ASP B 1 103 ? -30.229 4.52    19.508  1 25.289  ? 95   ASP B OD1   1 
ATOM   4777 O  OD2   . ASP B 1 103 ? -30.124 2.458   20.283  1 24.846  ? 95   ASP B OD2   1 
ATOM   4778 N  N     . GLY B 1 104 ? -25.126 4.751   20.089  1 18.881  ? 96   GLY B N     1 
ATOM   4779 C  CA    . GLY B 1 104 ? -24.308 5.505   21.036  1 17.092  ? 96   GLY B CA    1 
ATOM   4780 C  C     . GLY B 1 104 ? -23.7   6.773   20.435  1 17.84   ? 96   GLY B C     1 
ATOM   4781 O  O     . GLY B 1 104 ? -23.448 6.823   19.231  1 17.525  ? 96   GLY B O     1 
ATOM   4782 N  N     . ASP B 1 105 ? -23.485 7.778   21.306  1 17.769  ? 97   ASP B N     1 
ATOM   4783 C  CA    . ASP B 1 105 ? -22.895 9.088   21.032  1 18.229  ? 97   ASP B CA    1 
ATOM   4784 C  C     . ASP B 1 105 ? -21.646 8.978   20.157  1 17.483  ? 97   ASP B C     1 
ATOM   4785 O  O     . ASP B 1 105 ? -20.759 8.168   20.44   1 16.044  ? 97   ASP B O     1 
ATOM   4786 C  CB    . ASP B 1 105 ? -22.613 9.845   22.32   1 18.814  ? 97   ASP B CB    1 
ATOM   4787 C  CG    . ASP B 1 105 ? -23.822 10.01   23.222  1 19.993  ? 97   ASP B CG    1 
ATOM   4788 O  OD1   . ASP B 1 105 ? -24.704 10.817  22.863  1 21.251  ? 97   ASP B OD1   1 
ATOM   4789 O  OD2   . ASP B 1 105 ? -23.886 9.28    24.24   1 21.097  ? 97   ASP B OD2   1 
ATOM   4790 N  N     . GLY B 1 106 ? -21.65  9.772   19.074  1 16.821  ? 98   GLY B N     1 
ATOM   4791 C  CA    . GLY B 1 106 ? -20.542 9.874   18.132  1 16.234  ? 98   GLY B CA    1 
ATOM   4792 C  C     . GLY B 1 106 ? -19.315 10.502  18.77   1 15.674  ? 98   GLY B C     1 
ATOM   4793 O  O     . GLY B 1 106 ? -19.397 11.592  19.336  1 14.9    ? 98   GLY B O     1 
ATOM   4794 N  N     . THR B 1 107 ? -18.218 9.744   18.653  1 16.171  ? 99   THR B N     1 
ATOM   4795 C  CA    . THR B 1 107 ? -16.858 10.131  18.982  1 15.831  ? 99   THR B CA    1 
ATOM   4796 C  C     . THR B 1 107 ? -15.956 9.931   17.763  1 14.758  ? 99   THR B C     1 
ATOM   4797 O  O     . THR B 1 107 ? -15.985 8.876   17.138  1 15.684  ? 99   THR B O     1 
ATOM   4798 C  CB    . THR B 1 107 ? -16.372 9.429   20.264  1 15.482  ? 99   THR B CB    1 
ATOM   4799 O  OG1   . THR B 1 107 ? -15.089 10.007  20.515  1 14.722  ? 99   THR B OG1   1 
ATOM   4800 C  CG2   . THR B 1 107 ? -16.339 7.907   20.212  1 13.146  ? 99   THR B CG2   1 
ATOM   4801 N  N     . VAL B 1 108 ? -15.167 10.961  17.451  1 14.95   ? 100  VAL B N     1 
ATOM   4802 C  CA    . VAL B 1 108 ? -14.269 10.969  16.303  1 14.603  ? 100  VAL B CA    1 
ATOM   4803 C  C     . VAL B 1 108 ? -12.852 10.715  16.834  1 16.018  ? 100  VAL B C     1 
ATOM   4804 O  O     . VAL B 1 108 ? -12.41  11.438  17.721  1 14.832  ? 100  VAL B O     1 
ATOM   4805 C  CB    . VAL B 1 108 ? -14.378 12.245  15.426  1 14.359  ? 100  VAL B CB    1 
ATOM   4806 C  CG1   . VAL B 1 108 ? -13.339 12.33   14.289  1 13.744  ? 100  VAL B CG1   1 
ATOM   4807 C  CG2   . VAL B 1 108 ? -15.782 12.452  14.866  1 13.438  ? 100  VAL B CG2   1 
ATOM   4808 N  N     . ALA B 1 109 ? -12.165 9.704   16.276  1 17.707  ? 101  ALA B N     1 
ATOM   4809 C  CA    . ALA B 1 109 ? -10.716 9.551   16.398  1 19.367  ? 101  ALA B CA    1 
ATOM   4810 C  C     . ALA B 1 109 ? -10.017 9.98    15.105  1 20.804  ? 101  ALA B C     1 
ATOM   4811 O  O     . ALA B 1 109 ? -10.399 9.548   14.02   1 22.292  ? 101  ALA B O     1 
ATOM   4812 C  CB    . ALA B 1 109 ? -10.336 8.144   16.813  1 18.321  ? 101  ALA B CB    1 
ATOM   4813 N  N     . ALA B 1 110 ? -8.997  10.842  15.257  1 21.371  ? 102  ALA B N     1 
ATOM   4814 C  CA    . ALA B 1 110 ? -8.159  11.378  14.19   1 20.005  ? 102  ALA B CA    1 
ATOM   4815 C  C     . ALA B 1 110 ? -6.724  10.894  14.383  1 19.629  ? 102  ALA B C     1 
ATOM   4816 O  O     . ALA B 1 110 ? -6.152  11.056  15.46   1 18.639  ? 102  ALA B O     1 
ATOM   4817 C  CB    . ALA B 1 110 ? -8.231  12.89   14.184  1 18.127  ? 102  ALA B CB    1 
ATOM   4818 N  N     . PHE B 1 111 ? -6.176  10.311  13.305  1 20.227  ? 103  PHE B N     1 
ATOM   4819 C  CA    . PHE B 1 111 ? -4.788  9.885   13.183  1 19.495  ? 103  PHE B CA    1 
ATOM   4820 C  C     . PHE B 1 111 ? -4.165  10.716  12.06   1 20.133  ? 103  PHE B C     1 
ATOM   4821 O  O     . PHE B 1 111 ? -4.417  10.431  10.884  1 19.788  ? 103  PHE B O     1 
ATOM   4822 C  CB    . PHE B 1 111 ? -4.712  8.366   12.986  1 18.085  ? 103  PHE B CB    1 
ATOM   4823 C  CG    . PHE B 1 111 ? -5.378  7.499   14.043  1 18.63   ? 103  PHE B CG    1 
ATOM   4824 C  CD1   . PHE B 1 111 ? -6.74   7.151   13.936  1 19.282  ? 103  PHE B CD1   1 
ATOM   4825 C  CD2   . PHE B 1 111 ? -4.646  7.022   15.14   1 18.257  ? 103  PHE B CD2   1 
ATOM   4826 C  CE1   . PHE B 1 111 ? -7.358  6.364   14.916  1 19.926  ? 103  PHE B CE1   1 
ATOM   4827 C  CE2   . PHE B 1 111 ? -5.252  6.208   16.107  1 19.281  ? 103  PHE B CE2   1 
ATOM   4828 C  CZ    . PHE B 1 111 ? -6.606  5.888   16.002  1 20.025  ? 103  PHE B CZ    1 
ATOM   4829 N  N     . ARG B 1 112 ? -3.381  11.751  12.436  1 20.288  ? 104  ARG B N     1 
ATOM   4830 C  CA    . ARG B 1 112 ? -2.756  12.661  11.48   1 20.284  ? 104  ARG B CA    1 
ATOM   4831 C  C     . ARG B 1 112 ? -1.333  12.197  11.166  1 20.867  ? 104  ARG B C     1 
ATOM   4832 O  O     . ARG B 1 112 ? -0.504  12.11   12.073  1 19.025  ? 104  ARG B O     1 
ATOM   4833 C  CB    . ARG B 1 112 ? -2.83   14.13   11.905  1 19.368  ? 104  ARG B CB    1 
ATOM   4834 C  CG    . ARG B 1 112 ? -2.272  15.086  10.851  1 18.829  ? 104  ARG B CG    1 
ATOM   4835 C  CD    . ARG B 1 112 ? -2.774  16.464  11.133  1 18.593  ? 104  ARG B CD    1 
ATOM   4836 N  NE    . ARG B 1 112 ? -4.195  16.641  10.778  1 17.731  ? 104  ARG B NE    1 
ATOM   4837 C  CZ    . ARG B 1 112 ? -4.916  17.718  11.039  1 17.513  ? 104  ARG B CZ    1 
ATOM   4838 N  NH1   . ARG B 1 112 ? -4.363  18.794  11.583  1 16.941  ? 104  ARG B NH1   1 
ATOM   4839 N  NH2   . ARG B 1 112 ? -6.208  17.709  10.759  1 17.529  ? 104  ARG B NH2   1 
ATOM   4840 N  N     . PHE B 1 113 ? -1.084  11.982  9.862   1 22.236  ? 105  PHE B N     1 
ATOM   4841 C  CA    . PHE B 1 113 ? 0.176   11.537  9.27    1 22.501  ? 105  PHE B CA    1 
ATOM   4842 C  C     . PHE B 1 113 ? 0.815   12.727  8.559   1 24.205  ? 105  PHE B C     1 
ATOM   4843 O  O     . PHE B 1 113 ? 0.247   13.258  7.609   1 22.629  ? 105  PHE B O     1 
ATOM   4844 C  CB    . PHE B 1 113 ? -0.049  10.334  8.343   1 22.459  ? 105  PHE B CB    1 
ATOM   4845 C  CG    . PHE B 1 113 ? -0.575  9.054   8.979   1 22.206  ? 105  PHE B CG    1 
ATOM   4846 C  CD1   . PHE B 1 113 ? -1.912  8.936   9.416   1 22.492  ? 105  PHE B CD1   1 
ATOM   4847 C  CD2   . PHE B 1 113 ? 0.257   7.931   9.059   1 21.681  ? 105  PHE B CD2   1 
ATOM   4848 C  CE1   . PHE B 1 113 ? -2.382  7.74    9.988   1 23.645  ? 105  PHE B CE1   1 
ATOM   4849 C  CE2   . PHE B 1 113 ? -0.21   6.726   9.614   1 22.752  ? 105  PHE B CE2   1 
ATOM   4850 C  CZ    . PHE B 1 113 ? -1.523  6.635   10.091  1 22.603  ? 105  PHE B CZ    1 
ATOM   4851 N  N     . LYS B 1 114 ? 1.969   13.175  9.083   1 23.981  ? 106  LYS B N     1 
ATOM   4852 C  CA    . LYS B 1 114 ? 2.733   14.277  8.513   1 26.526  ? 106  LYS B CA    1 
ATOM   4853 C  C     . LYS B 1 114 ? 4.213   13.95   8.697   1 28.128  ? 106  LYS B C     1 
ATOM   4854 O  O     . LYS B 1 114 ? 4.65    13.8    9.829   1 27.438  ? 106  LYS B O     1 
ATOM   4855 C  CB    . LYS B 1 114 ? 2.252   15.615  9.094   1 27.558  ? 106  LYS B CB    1 
ATOM   4856 C  CG    . LYS B 1 114 ? 2.711   16.824  8.299   1 32.403  ? 106  LYS B CG    1 
ATOM   4857 C  CD    . LYS B 1 114 ? 2.33    18.211  8.788   1 35.451  ? 106  LYS B CD    1 
ATOM   4858 C  CE    . LYS B 1 114 ? 3.076   19.132  7.859   1 41.493  ? 106  LYS B CE    1 
ATOM   4859 N  NZ    . LYS B 1 114 ? 3.127   20.482  8.413   1 46.53   ? 106  LYS B NZ    1 
ATOM   4860 N  N     . ASP B 1 115 ? 4.936   13.745  7.58    1 27.601  ? 107  ASP B N     1 
ATOM   4861 C  CA    . ASP B 1 115 ? 6.393   13.578  7.533   1 32.379  ? 107  ASP B CA    1 
ATOM   4862 C  C     . ASP B 1 115 ? 6.86    12.383  8.389   1 33.912  ? 107  ASP B C     1 
ATOM   4863 O  O     . ASP B 1 115 ? 7.89    12.47   9.067   1 34.028  ? 107  ASP B O     1 
ATOM   4864 C  CB    . ASP B 1 115 ? 7.124   14.907  7.747   1 36.397  ? 107  ASP B CB    1 
ATOM   4865 C  CG    . ASP B 1 115 ? 6.568   16.154  7.056   1 46.319  ? 107  ASP B CG    1 
ATOM   4866 O  OD1   . ASP B 1 115 ? 6.329   16.126  5.822   1 46.171  ? 107  ASP B OD1   1 
ATOM   4867 O  OD2   . ASP B 1 115 ? 6.383   17.172  7.759   1 54.755  ? 107  ASP B OD2   1 
ATOM   4868 N  N     . GLY B 1 116 ? 6.079   11.278  8.388   1 31.768  ? 108  GLY B N     1 
ATOM   4869 C  CA    . GLY B 1 116 ? 6.375   10.055  9.13    1 28.757  ? 108  GLY B CA    1 
ATOM   4870 C  C     . GLY B 1 116 ? 5.948   10.059  10.609  1 28.045  ? 108  GLY B C     1 
ATOM   4871 O  O     . GLY B 1 116 ? 6.015   9       11.247  1 27.371  ? 108  GLY B O     1 
ATOM   4872 N  N     . LYS B 1 117 ? 5.511   11.221  11.146  1 25.025  ? 109  LYS B N     1 
ATOM   4873 C  CA    . LYS B 1 117 ? 5.002   11.369  12.51   1 27.032  ? 109  LYS B CA    1 
ATOM   4874 C  C     . LYS B 1 117 ? 3.469   11.216  12.539  1 24.685  ? 109  LYS B C     1 
ATOM   4875 O  O     . LYS B 1 117 ? 2.778   11.691  11.627  1 24.196  ? 109  LYS B O     1 
ATOM   4876 C  CB    . LYS B 1 117 ? 5.582   12.651  13.125  1 31.234  ? 109  LYS B CB    1 
ATOM   4877 C  CG    . LYS B 1 117 ? 4.917   14.001  12.772  1 44.732  ? 109  LYS B CG    1 
ATOM   4878 C  CD    . LYS B 1 117 ? 5.682   15.303  12.495  1 55.062  ? 109  LYS B CD    1 
ATOM   4879 C  CE    . LYS B 1 117 ? 4.924   16.428  11.819  1 50.835  ? 109  LYS B CE    1 
ATOM   4880 N  NZ    . LYS B 1 117 ? 3.778   17.015  12.53   1 53.398  ? 109  LYS B NZ    1 
ATOM   4881 N  N     . VAL B 1 118 ? 2.964   10.564  13.603  1 21.927  ? 110  VAL B N     1 
ATOM   4882 C  CA    . VAL B 1 118 ? 1.536   10.308  13.806  1 21.13   ? 110  VAL B CA    1 
ATOM   4883 C  C     . VAL B 1 118 ? 1.112   10.955  15.128  1 20.355  ? 110  VAL B C     1 
ATOM   4884 O  O     . VAL B 1 118 ? 1.732   10.678  16.164  1 19.514  ? 110  VAL B O     1 
ATOM   4885 C  CB    . VAL B 1 118 ? 1.055   8.84    13.692  1 22.135  ? 110  VAL B CB    1 
ATOM   4886 C  CG1   . VAL B 1 118 ? -0.469  8.701   13.65   1 24.246  ? 110  VAL B CG1   1 
ATOM   4887 C  CG2   . VAL B 1 118 ? 1.636   8.088   12.496  1 22.783  ? 110  VAL B CG2   1 
ATOM   4888 N  N     . ASP B 1 119 ? 0.056   11.792  15.056  1 17.132  ? 111  ASP B N     1 
ATOM   4889 C  CA    . ASP B 1 119 ? -0.666  12.312  16.21   1 17.128  ? 111  ASP B CA    1 
ATOM   4890 C  C     . ASP B 1 119 ? -2.068  11.705  16.287  1 17.409  ? 111  ASP B C     1 
ATOM   4891 O  O     . ASP B 1 119 ? -2.623  11.28   15.276  1 16.517  ? 111  ASP B O     1 
ATOM   4892 C  CB    . ASP B 1 119 ? -0.626  13.831  16.298  1 18.386  ? 111  ASP B CB    1 
ATOM   4893 C  CG    . ASP B 1 119 ? 0.76    14.473  16.343  1 19.546  ? 111  ASP B CG    1 
ATOM   4894 O  OD1   . ASP B 1 119 ? 1.697   13.879  16.903  1 18.897  ? 111  ASP B OD1   1 
ATOM   4895 O  OD2   . ASP B 1 119 ? 0.884   15.609  15.858  1 22.101  ? 111  ASP B OD2   1 
ATOM   4896 N  N     . TYR B 1 120 ? -2.609  11.677  17.52   1 17.082  ? 112  TYR B N     1 
ATOM   4897 C  CA    . TYR B 1 120 ? -3.947  11.181  17.83   1 17.82   ? 112  TYR B CA    1 
ATOM   4898 C  C     . TYR B 1 120 ? -4.735  12.236  18.607  1 17.218  ? 112  TYR B C     1 
ATOM   4899 O  O     . TYR B 1 120 ? -4.187  12.846  19.523  1 16.78   ? 112  TYR B O     1 
ATOM   4900 C  CB    . TYR B 1 120 ? -3.89   9.784   18.465  1 17.47   ? 112  TYR B CB    1 
ATOM   4901 C  CG    . TYR B 1 120 ? -5.107  9.327   19.257  1 18.491  ? 112  TYR B CG    1 
ATOM   4902 C  CD1   . TYR B 1 120 ? -6.165  8.643   18.644  1 18.304  ? 112  TYR B CD1   1 
ATOM   4903 C  CD2   . TYR B 1 120 ? -5.183  9.585   20.63   1 21.358  ? 112  TYR B CD2   1 
ATOM   4904 C  CE1   . TYR B 1 120 ? -7.273  8.231   19.384  1 19.617  ? 112  TYR B CE1   1 
ATOM   4905 C  CE2   . TYR B 1 120 ? -6.281  9.176   21.383  1 23.389  ? 112  TYR B CE2   1 
ATOM   4906 C  CZ    . TYR B 1 120 ? -7.333  8.529   20.748  1 21.423  ? 112  TYR B CZ    1 
ATOM   4907 O  OH    . TYR B 1 120 ? -8.32   8.148   21.604  1 21.16   ? 112  TYR B OH    1 
ATOM   4908 N  N     . ARG B 1 121 ? -6.009  12.414  18.212  1 16.869  ? 113  ARG B N     1 
ATOM   4909 C  CA    . ARG B 1 121 ? -7.036  13.125  18.968  1 17.933  ? 113  ARG B CA    1 
ATOM   4910 C  C     . ARG B 1 121 ? -8.352  12.366  18.877  1 19.07   ? 113  ARG B C     1 
ATOM   4911 O  O     . ARG B 1 121 ? -8.732  11.893  17.804  1 21.202  ? 113  ARG B O     1 
ATOM   4912 C  CB    . ARG B 1 121 ? -7.248  14.599  18.598  1 16.405  ? 113  ARG B CB    1 
ATOM   4913 C  CG    . ARG B 1 121 ? -8.242  15.368  19.452  1 14.662  ? 113  ARG B CG    1 
ATOM   4914 C  CD    . ARG B 1 121 ? -8.442  16.738  18.859  1 14.832  ? 113  ARG B CD    1 
ATOM   4915 N  NE    . ARG B 1 121 ? -7.425  17.706  19.293  1 14.976  ? 113  ARG B NE    1 
ATOM   4916 C  CZ    . ARG B 1 121 ? -7.292  18.311  20.489  1 15.966  ? 113  ARG B CZ    1 
ATOM   4917 N  NH1   . ARG B 1 121 ? -8.101  18.064  21.515  1 15.402  ? 113  ARG B NH1   1 
ATOM   4918 N  NH2   . ARG B 1 121 ? -6.269  19.123  20.69   1 15.701  ? 113  ARG B NH2   1 
ATOM   4919 N  N     . GLN B 1 122 ? -9.021  12.277  20.03   1 18.941  ? 114  GLN B N     1 
ATOM   4920 C  CA    . GLN B 1 122 ? -10.387 11.796  20.14   1 18.169  ? 114  GLN B CA    1 
ATOM   4921 C  C     . GLN B 1 122 ? -11.258 12.819  20.86   1 17.726  ? 114  GLN B C     1 
ATOM   4922 O  O     . GLN B 1 122 ? -10.833 13.397  21.867  1 17.026  ? 114  GLN B O     1 
ATOM   4923 C  CB    . GLN B 1 122 ? -10.435 10.423  20.788  1 17.81   ? 114  GLN B CB    1 
ATOM   4924 C  CG    . GLN B 1 122 ? -11.736 9.693   20.49   1 19.382  ? 114  GLN B CG    1 
ATOM   4925 C  CD    . GLN B 1 122 ? -11.785 8.242   20.901  1 21.295  ? 114  GLN B CD    1 
ATOM   4926 O  OE1   . GLN B 1 122 ? -10.789 7.609   21.261  1 21.413  ? 114  GLN B OE1   1 
ATOM   4927 N  NE2   . GLN B 1 122 ? -12.976 7.678   20.807  1 21.533  ? 114  GLN B NE2   1 
ATOM   4928 N  N     . ARG B 1 123 ? -12.502 12.969  20.354  1 16.564  ? 115  ARG B N     1 
ATOM   4929 C  CA    . ARG B 1 123 ? -13.499 13.842  20.954  1 16.126  ? 115  ARG B CA    1 
ATOM   4930 C  C     . ARG B 1 123 ? -14.901 13.42   20.529  1 15.657  ? 115  ARG B C     1 
ATOM   4931 O  O     . ARG B 1 123 ? -15.125 13.023  19.383  1 15.269  ? 115  ARG B O     1 
ATOM   4932 C  CB    . ARG B 1 123 ? -13.219 15.291  20.551  1 16.543  ? 115  ARG B CB    1 
ATOM   4933 C  CG    . ARG B 1 123 ? -13.74  16.31   21.547  1 19.197  ? 115  ARG B CG    1 
ATOM   4934 C  CD    . ARG B 1 123 ? -13.199 17.619  21.03   1 21.545  ? 115  ARG B CD    1 
ATOM   4935 N  NE    . ARG B 1 123 ? -13.585 18.67   21.97   1 24.968  ? 115  ARG B NE    1 
ATOM   4936 C  CZ    . ARG B 1 123 ? -13.082 19.903  22.081  1 25.961  ? 115  ARG B CZ    1 
ATOM   4937 N  NH1   . ARG B 1 123 ? -12.121 20.352  21.294  1 26.782  ? 115  ARG B NH1   1 
ATOM   4938 N  NH2   . ARG B 1 123 ? -13.577 20.706  23      1 25.574  ? 115  ARG B NH2   1 
ATOM   4939 N  N     . PHE B 1 124 ? -15.826 13.568  21.481  1 14.582  ? 116  PHE B N     1 
ATOM   4940 C  CA    . PHE B 1 124 ? -17.246 13.474  21.226  1 15.125  ? 116  PHE B CA    1 
ATOM   4941 C  C     . PHE B 1 124 ? -17.719 14.669  20.418  1 15.054  ? 116  PHE B C     1 
ATOM   4942 O  O     . PHE B 1 124 ? -17.323 15.802  20.698  1 14.736  ? 116  PHE B O     1 
ATOM   4943 C  CB    . PHE B 1 124 ? -18.061 13.44   22.521  1 14.746  ? 116  PHE B CB    1 
ATOM   4944 C  CG    . PHE B 1 124 ? -18.082 12.096  23.223  1 14.587  ? 116  PHE B CG    1 
ATOM   4945 C  CD1   . PHE B 1 124 ? -18.728 11.003  22.63   1 13.951  ? 116  PHE B CD1   1 
ATOM   4946 C  CD2   . PHE B 1 124 ? -17.496 11.944  24.492  1 15.025  ? 116  PHE B CD2   1 
ATOM   4947 C  CE1   . PHE B 1 124 ? -18.715 9.762   23.259  1 13.85   ? 116  PHE B CE1   1 
ATOM   4948 C  CE2   . PHE B 1 124 ? -17.508 10.698  25.145  1 15.27   ? 116  PHE B CE2   1 
ATOM   4949 C  CZ    . PHE B 1 124 ? -18.109 9.606   24.51   1 14.954  ? 116  PHE B CZ    1 
ATOM   4950 N  N     . VAL B 1 125 ? -18.607 14.369  19.458  1 15.159  ? 117  VAL B N     1 
ATOM   4951 C  CA    . VAL B 1 125 ? -19.44  15.351  18.77   1 16.118  ? 117  VAL B CA    1 
ATOM   4952 C  C     . VAL B 1 125 ? -20.379 15.956  19.816  1 17.062  ? 117  VAL B C     1 
ATOM   4953 O  O     . VAL B 1 125 ? -21.085 15.216  20.522  1 18.061  ? 117  VAL B O     1 
ATOM   4954 C  CB    . VAL B 1 125 ? -20.223 14.777  17.565  1 15.596  ? 117  VAL B CB    1 
ATOM   4955 C  CG1   . VAL B 1 125 ? -20.871 15.879  16.733  1 15.485  ? 117  VAL B CG1   1 
ATOM   4956 C  CG2   . VAL B 1 125 ? -19.364 13.907  16.653  1 16.753  ? 117  VAL B CG2   1 
ATOM   4957 N  N     . GLU B 1 126 ? -20.371 17.299  19.901  1 18.028  ? 118  GLU B N     1 
ATOM   4958 C  CA    . GLU B 1 126 ? -21.169 18.049  20.862  1 19.18   ? 118  GLU B CA    1 
ATOM   4959 C  C     . GLU B 1 126 ? -22.583 18.245  20.3    1 19.498  ? 118  GLU B C     1 
ATOM   4960 O  O     . GLU B 1 126 ? -23.049 19.382  20.146  1 19.577  ? 118  GLU B O     1 
ATOM   4961 C  CB    . GLU B 1 126 ? -20.478 19.278  21.466  1 21.342  ? 118  GLU B CB    1 
ATOM   4962 C  CG    . GLU B 1 126 ? -19.213 18.969  22.265  1 25.355  ? 118  GLU B CG    1 
ATOM   4963 C  CD    . GLU B 1 126 ? -18.688 19.924  23.345  1 33.416  ? 118  GLU B CD    1 
ATOM   4964 O  OE1   . GLU B 1 126 ? -18.889 21.16   23.171  1 29.921  ? 118  GLU B OE1   1 
ATOM   4965 O  OE2   . GLU B 1 126 ? -18.023 19.435  24.336  1 34.042  ? 118  GLU B OE2   1 
ATOM   4966 N  N     . THR B 1 127 ? -23.268 17.111  20.024  1 17.322  ? 119  THR B N     1 
ATOM   4967 C  CA    . THR B 1 127 ? -24.659 17.079  19.579  1 19.035  ? 119  THR B CA    1 
ATOM   4968 C  C     . THR B 1 127 ? -25.525 17.682  20.689  1 17.197  ? 119  THR B C     1 
ATOM   4969 O  O     . THR B 1 127 ? -25.171 17.56   21.867  1 17.342  ? 119  THR B O     1 
ATOM   4970 C  CB    . THR B 1 127 ? -25.149 15.677  19.181  1 18.778  ? 119  THR B CB    1 
ATOM   4971 O  OG1   . THR B 1 127 ? -25.313 14.903  20.366  1 20.11   ? 119  THR B OG1   1 
ATOM   4972 C  CG2   . THR B 1 127 ? -24.287 14.957  18.154  1 18.527  ? 119  THR B CG2   1 
ATOM   4973 N  N     . ASP B 1 128 ? -26.65  18.301  20.296  1 16.489  ? 120  ASP B N     1 
ATOM   4974 C  CA    . ASP B 1 128 ? -27.691 18.731  21.219  1 17.15   ? 120  ASP B CA    1 
ATOM   4975 C  C     . ASP B 1 128 ? -28.021 17.66   22.264  1 18.357  ? 120  ASP B C     1 
ATOM   4976 O  O     . ASP B 1 128 ? -28.116 18.002  23.445  1 19.725  ? 120  ASP B O     1 
ATOM   4977 C  CB    . ASP B 1 128 ? -28.869 19.355  20.487  1 16.874  ? 120  ASP B CB    1 
ATOM   4978 C  CG    . ASP B 1 128 ? -28.579 20.674  19.775  1 18.248  ? 120  ASP B CG    1 
ATOM   4979 O  OD1   . ASP B 1 128 ? -27.518 21.293  20.042  1 20.292  ? 120  ASP B OD1   1 
ATOM   4980 O  OD2   . ASP B 1 128 ? -29.425 21.097  18.957  1 18.525  ? 120  ASP B OD2   1 
ATOM   4981 N  N     . ARG B 1 129 ? -28.148 16.389  21.824  1 16.335  ? 121  ARG B N     1 
ATOM   4982 C  CA    . ARG B 1 129 ? -28.372 15.211  22.662  1 15.456  ? 121  ARG B CA    1 
ATOM   4983 C  C     . ARG B 1 129 ? -27.245 15.018  23.691  1 17.101  ? 121  ARG B C     1 
ATOM   4984 O  O     . ARG B 1 129 ? -27.53  14.858  24.891  1 17.574  ? 121  ARG B O     1 
ATOM   4985 C  CB    . ARG B 1 129 ? -28.633 14.016  21.742  1 15.082  ? 121  ARG B CB    1 
ATOM   4986 C  CG    . ARG B 1 129 ? -28.453 12.64   22.358  1 14.565  ? 121  ARG B CG    1 
ATOM   4987 C  CD    . ARG B 1 129 ? -29.252 11.742  21.499  1 13.914  ? 121  ARG B CD    1 
ATOM   4988 N  NE    . ARG B 1 129 ? -29.211 10.379  22.042  1 14.258  ? 121  ARG B NE    1 
ATOM   4989 C  CZ    . ARG B 1 129 ? -29.776 9.297   21.522  1 13.517  ? 121  ARG B CZ    1 
ATOM   4990 N  NH1   . ARG B 1 129 ? -30.581 9.376   20.47   1 13.94   ? 121  ARG B NH1   1 
ATOM   4991 N  NH2   . ARG B 1 129 ? -29.532 8.132   22.084  1 13.093  ? 121  ARG B NH2   1 
ATOM   4992 N  N     . PHE B 1 130 ? -25.991 15.002  23.198  1 16.2    ? 122  PHE B N     1 
ATOM   4993 C  CA    . PHE B 1 130 ? -24.793 14.847  24.012  1 17.484  ? 122  PHE B CA    1 
ATOM   4994 C  C     . PHE B 1 130 ? -24.741 15.916  25.113  1 16.716  ? 122  PHE B C     1 
ATOM   4995 O  O     . PHE B 1 130 ? -24.487 15.573  26.267  1 17.106  ? 122  PHE B O     1 
ATOM   4996 C  CB    . PHE B 1 130 ? -23.541 14.845  23.126  1 16.227  ? 122  PHE B CB    1 
ATOM   4997 C  CG    . PHE B 1 130 ? -22.238 14.928  23.905  1 17.408  ? 122  PHE B CG    1 
ATOM   4998 C  CD1   . PHE B 1 130 ? -21.646 13.752  24.4    1 16.499  ? 122  PHE B CD1   1 
ATOM   4999 C  CD2   . PHE B 1 130 ? -21.623 16.178  24.153  1 17.222  ? 122  PHE B CD2   1 
ATOM   5000 C  CE1   . PHE B 1 130 ? -20.464 13.822  25.137  1 16.677  ? 122  PHE B CE1   1 
ATOM   5001 C  CE2   . PHE B 1 130 ? -20.416 16.242  24.871  1 16.803  ? 122  PHE B CE2   1 
ATOM   5002 C  CZ    . PHE B 1 130 ? -19.846 15.059  25.346  1 15.551  ? 122  PHE B CZ    1 
ATOM   5003 N  N     . LYS B 1 131 ? -24.958 17.182  24.725  1 16.396  ? 123  LYS B N     1 
ATOM   5004 C  CA    . LYS B 1 131 ? -24.877 18.346  25.606  1 16.864  ? 123  LYS B CA    1 
ATOM   5005 C  C     . LYS B 1 131 ? -25.907 18.275  26.729  1 16.946  ? 123  LYS B C     1 
ATOM   5006 O  O     . LYS B 1 131 ? -25.546 18.509  27.873  1 16.726  ? 123  LYS B O     1 
ATOM   5007 C  CB    . LYS B 1 131 ? -24.984 19.669  24.85   1 16.235  ? 123  LYS B CB    1 
ATOM   5008 C  CG    . LYS B 1 131 ? -23.904 19.958  23.781  1 16.484  ? 123  LYS B CG    1 
ATOM   5009 C  CD    . LYS B 1 131 ? -23.818 21.418  23.336  1 17.85   ? 123  LYS B CD    1 
ATOM   5010 C  CE    . LYS B 1 131 ? -25.008 22.088  22.673  1 17.502  ? 123  LYS B CE    1 
ATOM   5011 N  NZ    . LYS B 1 131 ? -26.075 22.393  23.64   1 18.508  ? 123  LYS B NZ    1 
ATOM   5012 N  N     . VAL B 1 132 ? -27.156 17.893  26.392  1 17.127  ? 124  VAL B N     1 
ATOM   5013 C  CA    . VAL B 1 132 ? -28.247 17.678  27.335  1 18.659  ? 124  VAL B CA    1 
ATOM   5014 C  C     . VAL B 1 132 ? -27.858 16.6    28.361  1 18.001  ? 124  VAL B C     1 
ATOM   5015 O  O     . VAL B 1 132 ? -27.983 16.838  29.561  1 16.977  ? 124  VAL B O     1 
ATOM   5016 C  CB    . VAL B 1 132 ? -29.522 17.38   26.508  1 21.385  ? 124  VAL B CB    1 
ATOM   5017 C  CG1   . VAL B 1 132 ? -30.51  16.444  27.168  1 26.452  ? 124  VAL B CG1   1 
ATOM   5018 C  CG2   . VAL B 1 132 ? -30.224 18.662  26.086  1 24.567  ? 124  VAL B CG2   1 
ATOM   5019 N  N     . GLU B 1 133 ? -27.372 15.446  27.878  1 17.872  ? 125  GLU B N     1 
ATOM   5020 C  CA    . GLU B 1 133 ? -27.078 14.281  28.702  1 17.757  ? 125  GLU B CA    1 
ATOM   5021 C  C     . GLU B 1 133 ? -25.864 14.513  29.595  1 17.694  ? 125  GLU B C     1 
ATOM   5022 O  O     . GLU B 1 133 ? -25.895 14.04   30.725  1 18.433  ? 125  GLU B O     1 
ATOM   5023 C  CB    . GLU B 1 133 ? -26.935 12.986  27.914  1 17.174  ? 125  GLU B CB    1 
ATOM   5024 C  CG    . GLU B 1 133 ? -28.28  12.451  27.426  1 18.471  ? 125  GLU B CG    1 
ATOM   5025 C  CD    . GLU B 1 133 ? -28.308 11.061  26.829  1 18.811  ? 125  GLU B CD    1 
ATOM   5026 O  OE1   . GLU B 1 133 ? -27.238 10.483  26.539  1 20.425  ? 125  GLU B OE1   1 
ATOM   5027 O  OE2   . GLU B 1 133 ? -29.428 10.547  26.655  1 17.691  ? 125  GLU B OE2   1 
ATOM   5028 N  N     . ARG B 1 134 ? -24.852 15.251  29.095  1 19.445  ? 126  ARG B N     1 
ATOM   5029 C  CA    . ARG B 1 134 ? -23.649 15.623  29.846  1 20.126  ? 126  ARG B CA    1 
ATOM   5030 C  C     . ARG B 1 134 ? -23.999 16.557  30.998  1 18.381  ? 126  ARG B C     1 
ATOM   5031 O  O     . ARG B 1 134 ? -23.609 16.278  32.119  1 19.267  ? 126  ARG B O     1 
ATOM   5032 C  CB    . ARG B 1 134 ? -22.451 16.096  29.005  1 20.918  ? 126  ARG B CB    1 
ATOM   5033 C  CG    . ARG B 1 134 ? -21.205 16.427  29.826  1 20.186  ? 126  ARG B CG    1 
ATOM   5034 C  CD    . ARG B 1 134 ? -19.886 16.35   29.109  1 19.995  ? 126  ARG B CD    1 
ATOM   5035 N  NE    . ARG B 1 134 ? -19.46  14.97   28.829  1 18.844  ? 126  ARG B NE    1 
ATOM   5036 C  CZ    . ARG B 1 134 ? -18.318 14.554  28.263  1 19.127  ? 126  ARG B CZ    1 
ATOM   5037 N  NH1   . ARG B 1 134 ? -17.363 15.419  27.931  1 17.31   ? 126  ARG B NH1   1 
ATOM   5038 N  NH2   . ARG B 1 134 ? -18.171 13.259  28.018  1 17.68   ? 126  ARG B NH2   1 
ATOM   5039 N  N     . ARG B 1 135 ? -24.699 17.655  30.697  1 21.188  ? 127  ARG B N     1 
ATOM   5040 C  CA    . ARG B 1 135 ? -25.141 18.678  31.644  1 21.026  ? 127  ARG B CA    1 
ATOM   5041 C  C     . ARG B 1 135 ? -26.007 18.101  32.771  1 21.015  ? 127  ARG B C     1 
ATOM   5042 O  O     . ARG B 1 135 ? -25.864 18.558  33.904  1 21.12   ? 127  ARG B O     1 
ATOM   5043 C  CB    . ARG B 1 135 ? -25.845 19.83   30.934  1 20.659  ? 127  ARG B CB    1 
ATOM   5044 C  CG    . ARG B 1 135 ? -24.85  20.671  30.154  1 21.794  ? 127  ARG B CG    1 
ATOM   5045 C  CD    . ARG B 1 135 ? -25.573 21.713  29.293  1 23.597  ? 127  ARG B CD    1 
ATOM   5046 N  NE    . ARG B 1 135 ? -26.115 22.788  30.134  1 23.193  ? 127  ARG B NE    1 
ATOM   5047 C  CZ    . ARG B 1 135 ? -25.463 23.746  30.81   1 24.204  ? 127  ARG B CZ    1 
ATOM   5048 N  NH1   . ARG B 1 135 ? -24.166 23.978  30.648  1 23.974  ? 127  ARG B NH1   1 
ATOM   5049 N  NH2   . ARG B 1 135 ? -26.157 24.53   31.609  1 24.442  ? 127  ARG B NH2   1 
ATOM   5050 N  N     . ALA B 1 136 ? -26.841 17.086  32.462  1 19.534  ? 128  ALA B N     1 
ATOM   5051 C  CA    . ALA B 1 136 ? -27.698 16.389  33.424  1 18.834  ? 128  ALA B CA    1 
ATOM   5052 C  C     . ALA B 1 136 ? -26.989 15.237  34.16   1 19.665  ? 128  ALA B C     1 
ATOM   5053 O  O     . ALA B 1 136 ? -27.51  14.763  35.166  1 20.517  ? 128  ALA B O     1 
ATOM   5054 C  CB    . ALA B 1 136 ? -28.964 15.93   32.733  1 16.702  ? 128  ALA B CB    1 
ATOM   5055 N  N     . ARG B 1 137 ? -25.831 14.769  33.646  1 19.3    ? 129  ARG B N     1 
ATOM   5056 C  CA    . ARG B 1 137 ? -25.141 13.518  33.976  1 20.337  ? 129  ARG B CA    1 
ATOM   5057 C  C     . ARG B 1 137 ? -26.114 12.327  33.936  1 20.5    ? 129  ARG B C     1 
ATOM   5058 O  O     . ARG B 1 137 ? -26.106 11.472  34.822  1 21.095  ? 129  ARG B O     1 
ATOM   5059 C  CB    . ARG B 1 137 ? -24.285 13.704  35.24   1 19.947  ? 129  ARG B CB    1 
ATOM   5060 C  CG    . ARG B 1 137 ? -23.371 12.55   35.656  1 19.716  ? 129  ARG B CG    1 
ATOM   5061 C  CD    . ARG B 1 137 ? -22.677 12.733  36.998  1 21.012  ? 129  ARG B CD    1 
ATOM   5062 N  NE    . ARG B 1 137 ? -21.723 13.857  37.056  1 21.117  ? 129  ARG B NE    1 
ATOM   5063 C  CZ    . ARG B 1 137 ? -20.388 13.889  36.979  1 20.615  ? 129  ARG B CZ    1 
ATOM   5064 N  NH1   . ARG B 1 137 ? -19.667 12.802  36.761  1 19.171  ? 129  ARG B NH1   1 
ATOM   5065 N  NH2   . ARG B 1 137 ? -19.771 15.057  37.069  1 19.32   ? 129  ARG B NH2   1 
ATOM   5066 N  N     . LYS B 1 138 ? -26.991 12.288  32.916  1 21.147  ? 130  LYS B N     1 
ATOM   5067 C  CA    . LYS B 1 138 ? -28.136 11.382  32.901  1 21.342  ? 130  LYS B CA    1 
ATOM   5068 C  C     . LYS B 1 138 ? -28.603 11.168  31.463  1 18.893  ? 130  LYS B C     1 
ATOM   5069 O  O     . LYS B 1 138 ? -28.727 12.142  30.712  1 17.808  ? 130  LYS B O     1 
ATOM   5070 C  CB    . LYS B 1 138 ? -29.263 11.908  33.81   1 26.119  ? 130  LYS B CB    1 
ATOM   5071 C  CG    . LYS B 1 138 ? -30.321 10.877  34.18   1 32.044  ? 130  LYS B CG    1 
ATOM   5072 C  CD    . LYS B 1 138 ? -30.981 11.17   35.525  1 38.081  ? 130  LYS B CD    1 
ATOM   5073 C  CE    . LYS B 1 138 ? -31.812 10.023  36.011  1 42.161  ? 130  LYS B CE    1 
ATOM   5074 N  NZ    . LYS B 1 138 ? -31.005 8.897   36.495  1 44.924  ? 130  LYS B NZ    1 
ATOM   5075 N  N     . SER B 1 139 ? -28.91  9.896   31.156  1 16.549  ? 131  SER B N     1 
ATOM   5076 C  CA    . SER B 1 139 ? -29.633 9.454   29.966  1 17.379  ? 131  SER B CA    1 
ATOM   5077 C  C     . SER B 1 139 ? -31.03  10.075  29.927  1 17.714  ? 131  SER B C     1 
ATOM   5078 O  O     . SER B 1 139 ? -31.752 10.073  30.923  1 20.765  ? 131  SER B O     1 
ATOM   5079 C  CB    . SER B 1 139 ? -29.708 7.966   29.958  1 17.817  ? 131  SER B CB    1 
ATOM   5080 O  OG    . SER B 1 139 ? -30.467 7.487   28.859  1 18.443  ? 131  SER B OG    1 
ATOM   5081 N  N     . MET B 1 140 ? -31.383 10.636  28.764  1 18.235  ? 132  MET B N     1 
ATOM   5082 C  CA    . MET B 1 140 ? -32.621 11.381  28.535  1 19.317  ? 132  MET B CA    1 
ATOM   5083 C  C     . MET B 1 140 ? -33.261 10.991  27.2    1 18.451  ? 132  MET B C     1 
ATOM   5084 O  O     . MET B 1 140 ? -34.264 11.57   26.797  1 20.023  ? 132  MET B O     1 
ATOM   5085 C  CB    . MET B 1 140 ? -32.371 12.89   28.694  1 19.741  ? 132  MET B CB    1 
ATOM   5086 C  CG    . MET B 1 140 ? -32.239 13.348  30.142  1 21.223  ? 132  MET B CG    1 
ATOM   5087 S  SD    . MET B 1 140 ? -31.862 15.104  30.189  1 26.663  ? 132  MET B SD    1 
ATOM   5088 C  CE    . MET B 1 140 ? -33.526 15.772  30.337  1 23.097  ? 132  MET B CE    1 
ATOM   5089 N  N     . TYR B 1 141 ? -32.697 9.971   26.537  1 17.495  ? 133  TYR B N     1 
ATOM   5090 C  CA    . TYR B 1 141 ? -33.124 9.47    25.238  1 17.457  ? 133  TYR B CA    1 
ATOM   5091 C  C     . TYR B 1 141 ? -33.397 7.979   25.364  1 16.758  ? 133  TYR B C     1 
ATOM   5092 O  O     . TYR B 1 141 ? -32.705 7.28    26.112  1 18.922  ? 133  TYR B O     1 
ATOM   5093 C  CB    . TYR B 1 141 ? -32.107 9.845   24.152  1 17.188  ? 133  TYR B CB    1 
ATOM   5094 C  CG    . TYR B 1 141 ? -32.081 11.335  23.831  1 17.923  ? 133  TYR B CG    1 
ATOM   5095 C  CD1   . TYR B 1 141 ? -31.349 12.236  24.626  1 18.21   ? 133  TYR B CD1   1 
ATOM   5096 C  CD2   . TYR B 1 141 ? -32.767 11.853  22.728  1 17.037  ? 133  TYR B CD2   1 
ATOM   5097 C  CE1   . TYR B 1 141 ? -31.367 13.604  24.373  1 18.245  ? 133  TYR B CE1   1 
ATOM   5098 C  CE2   . TYR B 1 141 ? -32.754 13.22   22.445  1 19.095  ? 133  TYR B CE2   1 
ATOM   5099 C  CZ    . TYR B 1 141 ? -32.033 14.088  23.259  1 17.524  ? 133  TYR B CZ    1 
ATOM   5100 O  OH    . TYR B 1 141 ? -31.962 15.42   23.021  1 19.089  ? 133  TYR B OH    1 
ATOM   5101 N  N     . GLY B 1 142 ? -34.424 7.546   24.626  1 15.496  ? 134  GLY B N     1 
ATOM   5102 C  CA    . GLY B 1 142 ? -34.888 6.176   24.576  1 15.454  ? 134  GLY B CA    1 
ATOM   5103 C  C     . GLY B 1 142 ? -34.365 5.43    23.364  1 17.028  ? 134  GLY B C     1 
ATOM   5104 O  O     . GLY B 1 142 ? -33.157 5.428   23.104  1 16.588  ? 134  GLY B O     1 
ATOM   5105 N  N     . LEU B 1 143 ? -35.317 4.78    22.678  1 17.551  ? 135  LEU B N     1 
ATOM   5106 C  CA    . LEU B 1 143 ? -35.079 3.931   21.512  1 17.726  ? 135  LEU B CA    1 
ATOM   5107 C  C     . LEU B 1 143 ? -34.574 4.755   20.329  1 18.317  ? 135  LEU B C     1 
ATOM   5108 O  O     . LEU B 1 143 ? -34.923 5.946   20.193  1 19.896  ? 135  LEU B O     1 
ATOM   5109 C  CB    . LEU B 1 143 ? -36.324 3.114   21.141  1 17.324  ? 135  LEU B CB    1 
ATOM   5110 C  CG    . LEU B 1 143 ? -36.942 2.211   22.224  1 16.013  ? 135  LEU B CG    1 
ATOM   5111 C  CD1   . LEU B 1 143 ? -38.185 1.512   21.662  1 15.59   ? 135  LEU B CD1   1 
ATOM   5112 C  CD2   . LEU B 1 143 ? -36.025 1.173   22.822  1 15.332  ? 135  LEU B CD2   1 
ATOM   5113 N  N     . TYR B 1 144 ? -33.758 4.082   19.494  1 17.475  ? 136  TYR B N     1 
ATOM   5114 C  CA    . TYR B 1 144 ? -33.272 4.56    18.208  1 18.606  ? 136  TYR B CA    1 
ATOM   5115 C  C     . TYR B 1 144 ? -34.439 5.158   17.427  1 20.378  ? 136  TYR B C     1 
ATOM   5116 O  O     . TYR B 1 144 ? -35.439 4.473   17.184  1 22.017  ? 136  TYR B O     1 
ATOM   5117 C  CB    . TYR B 1 144 ? -32.596 3.41    17.448  1 18.724  ? 136  TYR B CB    1 
ATOM   5118 C  CG    . TYR B 1 144 ? -32.067 3.754   16.058  1 18.011  ? 136  TYR B CG    1 
ATOM   5119 C  CD1   . TYR B 1 144 ? -30.856 4.459   15.897  1 16.926  ? 136  TYR B CD1   1 
ATOM   5120 C  CD2   . TYR B 1 144 ? -32.781 3.38    14.908  1 17.775  ? 136  TYR B CD2   1 
ATOM   5121 C  CE1   . TYR B 1 144 ? -30.379 4.776   14.63   1 18.348  ? 136  TYR B CE1   1 
ATOM   5122 C  CE2   . TYR B 1 144 ? -32.291 3.657   13.637  1 17.66   ? 136  TYR B CE2   1 
ATOM   5123 C  CZ    . TYR B 1 144 ? -31.098 4.372   13.507  1 17.867  ? 136  TYR B CZ    1 
ATOM   5124 O  OH    . TYR B 1 144 ? -30.616 4.649   12.268  1 19.592  ? 136  TYR B OH    1 
ATOM   5125 N  N     . ARG B 1 145 ? -34.325 6.47    17.149  1 19.915  ? 137  ARG B N     1 
ATOM   5126 C  CA    . ARG B 1 145 ? -35.232 7.239   16.303  1 19.092  ? 137  ARG B CA    1 
ATOM   5127 C  C     . ARG B 1 145 ? -36.679 7.258   16.846  1 19.135  ? 137  ARG B C     1 
ATOM   5128 O  O     . ARG B 1 145 ? -37.627 7.376   16.059  1 18.013  ? 137  ARG B O     1 
ATOM   5129 C  CB    . ARG B 1 145 ? -35.063 6.78    14.841  1 18.781  ? 137  ARG B CB    1 
ATOM   5130 C  CG    . ARG B 1 145 ? -33.703 6.994   14.195  1 19.783  ? 137  ARG B CG    1 
ATOM   5131 C  CD    . ARG B 1 145 ? -33.784 6.777   12.696  1 19.944  ? 137  ARG B CD    1 
ATOM   5132 N  NE    . ARG B 1 145 ? -34.543 7.818   11.984  1 22.016  ? 137  ARG B NE    1 
ATOM   5133 C  CZ    . ARG B 1 145 ? -34.416 8.214   10.715  1 22.751  ? 137  ARG B CZ    1 
ATOM   5134 N  NH1   . ARG B 1 145 ? -33.61  7.583   9.855   1 21.819  ? 137  ARG B NH1   1 
ATOM   5135 N  NH2   . ARG B 1 145 ? -35.049 9.318   10.337  1 21.99   ? 137  ARG B NH2   1 
ATOM   5136 N  N     . ASN B 1 146 ? -36.854 7.155   18.179  1 18.765  ? 138  ASN B N     1 
ATOM   5137 C  CA    . ASN B 1 146 ? -38.182 7.195   18.795  1 18.215  ? 138  ASN B CA    1 
ATOM   5138 C  C     . ASN B 1 146 ? -38.306 8.322   19.827  1 15.665  ? 138  ASN B C     1 
ATOM   5139 O  O     . ASN B 1 146 ? -38.17  8.032   21.02   1 16.188  ? 138  ASN B O     1 
ATOM   5140 C  CB    . ASN B 1 146 ? -38.742 5.827   19.208  1 19      ? 138  ASN B CB    1 
ATOM   5141 C  CG    . ASN B 1 146 ? -40.222 5.879   19.563  1 20.211  ? 138  ASN B CG    1 
ATOM   5142 O  OD1   . ASN B 1 146 ? -40.88  6.931   19.459  1 18.129  ? 138  ASN B OD1   1 
ATOM   5143 N  ND2   . ASN B 1 146 ? -40.78  4.739   19.972  1 20.332  ? 138  ASN B ND2   1 
ATOM   5144 N  N     . PRO B 1 147 ? -38.642 9.58    19.414  1 15.19   ? 139  PRO B N     1 
ATOM   5145 C  CA    . PRO B 1 147 ? -38.99  10.681  20.32   1 15.934  ? 139  PRO B CA    1 
ATOM   5146 C  C     . PRO B 1 147 ? -40.06  10.448  21.393  1 17.602  ? 139  PRO B C     1 
ATOM   5147 O  O     . PRO B 1 147 ? -39.985 11.068  22.467  1 17.127  ? 139  PRO B O     1 
ATOM   5148 C  CB    . PRO B 1 147 ? -39.338 11.848  19.409  1 16.971  ? 139  PRO B CB    1 
ATOM   5149 C  CG    . PRO B 1 147 ? -38.526 11.534  18.15   1 16.601  ? 139  PRO B CG    1 
ATOM   5150 C  CD    . PRO B 1 147 ? -38.597 10.059  18.018  1 15.296  ? 139  PRO B CD    1 
ATOM   5151 N  N     . TYR B 1 148 ? -41.001 9.523   21.135  1 16.857  ? 140  TYR B N     1 
ATOM   5152 C  CA    . TYR B 1 148 ? -42.032 9.107   22.081  1 17.978  ? 140  TYR B CA    1 
ATOM   5153 C  C     . TYR B 1 148 ? -41.446 8.307   23.252  1 19.083  ? 140  TYR B C     1 
ATOM   5154 O  O     . TYR B 1 148 ? -42.171 8.036   24.217  1 20.953  ? 140  TYR B O     1 
ATOM   5155 C  CB    . TYR B 1 148 ? -43.211 8.407   21.376  1 19.3    ? 140  TYR B CB    1 
ATOM   5156 C  CG    . TYR B 1 148 ? -43.84  9.264   20.291  1 19.204  ? 140  TYR B CG    1 
ATOM   5157 C  CD1   . TYR B 1 148 ? -44.735 10.303  20.618  1 19.934  ? 140  TYR B CD1   1 
ATOM   5158 C  CD2   . TYR B 1 148 ? -43.512 9.051   18.949  1 18.721  ? 140  TYR B CD2   1 
ATOM   5159 C  CE1   . TYR B 1 148 ? -45.287 11.11   19.629  1 18.366  ? 140  TYR B CE1   1 
ATOM   5160 C  CE2   . TYR B 1 148 ? -44.06  9.867   17.955  1 18.658  ? 140  TYR B CE2   1 
ATOM   5161 C  CZ    . TYR B 1 148 ? -44.943 10.892  18.299  1 17.846  ? 140  TYR B CZ    1 
ATOM   5162 O  OH    . TYR B 1 148 ? -45.479 11.705  17.339  1 16.039  ? 140  TYR B OH    1 
ATOM   5163 N  N     . THR B 1 149 ? -40.166 7.884   23.158  1 18.214  ? 141  THR B N     1 
ATOM   5164 C  CA    . THR B 1 149 ? -39.437 7.211   24.241  1 17.033  ? 141  THR B CA    1 
ATOM   5165 C  C     . THR B 1 149 ? -38.342 8.109   24.836  1 18.379  ? 141  THR B C     1 
ATOM   5166 O  O     . THR B 1 149 ? -37.6   7.649   25.697  1 17.6    ? 141  THR B O     1 
ATOM   5167 C  CB    . THR B 1 149 ? -38.952 5.812   23.843  1 15.862  ? 141  THR B CB    1 
ATOM   5168 O  OG1   . THR B 1 149 ? -37.949 5.973   22.844  1 15.658  ? 141  THR B OG1   1 
ATOM   5169 C  CG2   . THR B 1 149 ? -40.071 4.903   23.371  1 14.32   ? 141  THR B CG2   1 
ATOM   5170 N  N     . HIS B 1 150 ? -38.227 9.375   24.378  1 18.347  ? 142  HIS B N     1 
ATOM   5171 C  CA    . HIS B 1 150 ? -37.316 10.361  24.969  1 18.19   ? 142  HIS B CA    1 
ATOM   5172 C  C     . HIS B 1 150 ? -38.001 11.073  26.137  1 17.871  ? 142  HIS B C     1 
ATOM   5173 O  O     . HIS B 1 150 ? -39.232 11.094  26.214  1 19.017  ? 142  HIS B O     1 
ATOM   5174 C  CB    . HIS B 1 150 ? -36.715 11.319  23.916  1 17.504  ? 142  HIS B CB    1 
ATOM   5175 C  CG    . HIS B 1 150 ? -36.067 10.688  22.711  1 16.569  ? 142  HIS B CG    1 
ATOM   5176 N  ND1   . HIS B 1 150 ? -35.573 9.401   22.616  1 15.131  ? 142  HIS B ND1   1 
ATOM   5177 C  CD2   . HIS B 1 150 ? -35.86  11.254  21.503  1 16.37   ? 142  HIS B CD2   1 
ATOM   5178 C  CE1   . HIS B 1 150 ? -35.085 9.196   21.398  1 16.353  ? 142  HIS B CE1   1 
ATOM   5179 N  NE2   . HIS B 1 150 ? -35.245 10.319  20.71   1 17.818  ? 142  HIS B NE2   1 
ATOM   5180 N  N     . HIS B 1 151 ? -37.183 11.623  27.05   1 16.835  ? 143  HIS B N     1 
ATOM   5181 C  CA    . HIS B 1 151 ? -37.591 12.498  28.147  1 19.067  ? 143  HIS B CA    1 
ATOM   5182 C  C     . HIS B 1 151 ? -38.415 13.676  27.615  1 18.409  ? 143  HIS B C     1 
ATOM   5183 O  O     . HIS B 1 151 ? -38.028 14.24   26.589  1 18.615  ? 143  HIS B O     1 
ATOM   5184 C  CB    . HIS B 1 151 ? -36.352 12.895  28.952  1 18.368  ? 143  HIS B CB    1 
ATOM   5185 C  CG    . HIS B 1 151 ? -36.541 13.725  30.168  1 20.717  ? 143  HIS B CG    1 
ATOM   5186 N  ND1   . HIS B 1 151 ? -37.075 14.998  30.217  1 22.324  ? 143  HIS B ND1   1 
ATOM   5187 C  CD2   . HIS B 1 151 ? -36.124 13.438  31.422  1 20.641  ? 143  HIS B CD2   1 
ATOM   5188 C  CE1   . HIS B 1 151 ? -36.983 15.449  31.462  1 21.507  ? 143  HIS B CE1   1 
ATOM   5189 N  NE2   . HIS B 1 151 ? -36.42  14.52   32.215  1 20.16   ? 143  HIS B NE2   1 
ATOM   5190 N  N     . PRO B 1 152 ? -39.582 14.045  28.229  1 19.785  ? 144  PRO B N     1 
ATOM   5191 C  CA    . PRO B 1 152 ? -40.428 15.164  27.773  1 20.812  ? 144  PRO B CA    1 
ATOM   5192 C  C     . PRO B 1 152 ? -39.732 16.479  27.422  1 21.851  ? 144  PRO B C     1 
ATOM   5193 O  O     . PRO B 1 152 ? -40.091 17.065  26.401  1 21.232  ? 144  PRO B O     1 
ATOM   5194 C  CB    . PRO B 1 152 ? -41.516 15.332  28.839  1 19.382  ? 144  PRO B CB    1 
ATOM   5195 C  CG    . PRO B 1 152 ? -41.66  13.913  29.325  1 19.234  ? 144  PRO B CG    1 
ATOM   5196 C  CD    . PRO B 1 152 ? -40.256 13.331  29.328  1 18.964  ? 144  PRO B CD    1 
ATOM   5197 N  N     . CYS B 1 153 ? -38.695 16.843  28.195  1 22.728  ? 145  CYS B N     1 
ATOM   5198 C  CA    . CYS B 1 153 ? -37.9   18.056  28.028  1 27.586  ? 145  CYS B CA    1 
ATOM   5199 C  C     . CYS B 1 153 ? -37.119 18.094  26.707  1 24.73   ? 145  CYS B C     1 
ATOM   5200 O  O     . CYS B 1 153 ? -36.774 19.192  26.252  1 23.105  ? 145  CYS B O     1 
ATOM   5201 C  CB    . CYS B 1 153 ? -36.938 18.266  29.199  1 36.104  ? 145  CYS B CB    1 
ATOM   5202 S  SG    . CYS B 1 153 ? -37.69  18.949  30.706  1 48.629  ? 145  CYS B SG    1 
ATOM   5203 N  N     . VAL B 1 154 ? -36.874 16.925  26.08   1 22.485  ? 146  VAL B N     1 
ATOM   5204 C  CA    . VAL B 1 154 ? -35.971 16.822  24.928  1 24.151  ? 146  VAL B CA    1 
ATOM   5205 C  C     . VAL B 1 154 ? -36.68  16.281  23.676  1 24.278  ? 146  VAL B C     1 
ATOM   5206 O  O     . VAL B 1 154 ? -36.016 16.001  22.668  1 24.661  ? 146  VAL B O     1 
ATOM   5207 C  CB    . VAL B 1 154 ? -34.644 16.079  25.233  1 22.459  ? 146  VAL B CB    1 
ATOM   5208 C  CG1   . VAL B 1 154 ? -33.869 16.748  26.358  1 22.988  ? 146  VAL B CG1   1 
ATOM   5209 C  CG2   . VAL B 1 154 ? -34.816 14.579  25.498  1 21.226  ? 146  VAL B CG2   1 
ATOM   5210 N  N     . ARG B 1 155 ? -38.015 16.125  23.725  1 25.232  ? 147  ARG B N     1 
ATOM   5211 C  CA    . ARG B 1 155 ? -38.77  15.449  22.664  1 26.834  ? 147  ARG B CA    1 
ATOM   5212 C  C     . ARG B 1 155 ? -38.682 16.192  21.333  1 26.055  ? 147  ARG B C     1 
ATOM   5213 O  O     . ARG B 1 155 ? -38.658 15.539  20.292  1 24.082  ? 147  ARG B O     1 
ATOM   5214 C  CB    . ARG B 1 155 ? -40.245 15.165  22.951  1 29.42   ? 147  ARG B CB    1 
ATOM   5215 C  CG    . ARG B 1 155 ? -40.335 14.019  23.933  1 31.427  ? 147  ARG B CG    1 
ATOM   5216 C  CD    . ARG B 1 155 ? -41.756 13.527  24.031  1 36.588  ? 147  ARG B CD    1 
ATOM   5217 N  NE    . ARG B 1 155 ? -41.653 12.492  25.069  1 35.468  ? 147  ARG B NE    1 
ATOM   5218 C  CZ    . ARG B 1 155 ? -42.566 11.62   25.448  1 39.395  ? 147  ARG B CZ    1 
ATOM   5219 N  NH1   . ARG B 1 155 ? -43.788 11.645  24.923  1 39.873  ? 147  ARG B NH1   1 
ATOM   5220 N  NH2   . ARG B 1 155 ? -42.243 10.72   26.368  1 41.972  ? 147  ARG B NH2   1 
ATOM   5221 N  N     . GLN B 1 156 ? -38.581 17.533  21.409  1 24.859  ? 148  GLN B N     1 
ATOM   5222 C  CA    . GLN B 1 156 ? -38.501 18.408  20.255  1 26.774  ? 148  GLN B CA    1 
ATOM   5223 C  C     . GLN B 1 156 ? -37.062 18.858  19.944  1 24.057  ? 148  GLN B C     1 
ATOM   5224 O  O     . GLN B 1 156 ? -36.868 19.914  19.317  1 23.823  ? 148  GLN B O     1 
ATOM   5225 C  CB    . GLN B 1 156 ? -39.597 19.457  20.434  1 30.013  ? 148  GLN B CB    1 
ATOM   5226 C  CG    . GLN B 1 156 ? -40.343 19.672  19.123  1 35.93   ? 148  GLN B CG    1 
ATOM   5227 C  CD    . GLN B 1 156 ? -41.441 20.709  19.159  1 38.201  ? 148  GLN B CD    1 
ATOM   5228 O  OE1   . GLN B 1 156 ? -41.847 21.23   20.21   1 34.635  ? 148  GLN B OE1   1 
ATOM   5229 N  NE2   . GLN B 1 156 ? -41.929 20.998  17.959  1 38.063  ? 148  GLN B NE2   1 
ATOM   5230 N  N     . THR B 1 157 ? -36.066 18.045  20.359  1 20.273  ? 149  THR B N     1 
ATOM   5231 C  CA    . THR B 1 157 ? -34.662 18.242  19.998  1 18.622  ? 149  THR B CA    1 
ATOM   5232 C  C     . THR B 1 157 ? -34.353 17.487  18.705  1 17.282  ? 149  THR B C     1 
ATOM   5233 O  O     . THR B 1 157 ? -35.046 16.531  18.361  1 18.312  ? 149  THR B O     1 
ATOM   5234 C  CB    . THR B 1 157 ? -33.68  17.875  21.125  1 18.167  ? 149  THR B CB    1 
ATOM   5235 O  OG1   . THR B 1 157 ? -33.776 16.471  21.367  1 15.625  ? 149  THR B OG1   1 
ATOM   5236 C  CG2   . THR B 1 157 ? -33.778 18.756  22.364  1 16.588  ? 149  THR B CG2   1 
ATOM   5237 N  N     . VAL B 1 158 ? -33.264 17.897  18.034  1 18.271  ? 150  VAL B N     1 
ATOM   5238 C  CA    . VAL B 1 158 ? -32.472 17.047  17.148  1 18.652  ? 150  VAL B CA    1 
ATOM   5239 C  C     . VAL B 1 158 ? -31.846 15.934  18.003  1 20.262  ? 150  VAL B C     1 
ATOM   5240 O  O     . VAL B 1 158 ? -31.11  16.213  18.957  1 18.668  ? 150  VAL B O     1 
ATOM   5241 C  CB    . VAL B 1 158 ? -31.489 17.81   16.226  1 18.545  ? 150  VAL B CB    1 
ATOM   5242 C  CG1   . VAL B 1 158 ? -30.474 16.911  15.51   1 18.501  ? 150  VAL B CG1   1 
ATOM   5243 C  CG2   . VAL B 1 158 ? -32.264 18.619  15.201  1 17.887  ? 150  VAL B CG2   1 
ATOM   5244 N  N     . GLU B 1 159 ? -32.247 14.688  17.681  1 19.623  ? 151  GLU B N     1 
ATOM   5245 C  CA    . GLU B 1 159 ? -31.989 13.483  18.471  1 19.695  ? 151  GLU B CA    1 
ATOM   5246 C  C     . GLU B 1 159 ? -30.816 12.649  17.928  1 18.049  ? 151  GLU B C     1 
ATOM   5247 O  O     . GLU B 1 159 ? -30.527 11.579  18.475  1 18.65   ? 151  GLU B O     1 
ATOM   5248 C  CB    . GLU B 1 159 ? -33.272 12.667  18.644  1 20.553  ? 151  GLU B CB    1 
ATOM   5249 C  CG    . GLU B 1 159 ? -33.934 12.245  17.329  1 21.691  ? 151  GLU B CG    1 
ATOM   5250 C  CD    . GLU B 1 159 ? -34.325 10.803  17.122  1 21.637  ? 151  GLU B CD    1 
ATOM   5251 O  OE1   . GLU B 1 159 ? -34.483 10.017  18.078  1 22.752  ? 151  GLU B OE1   1 
ATOM   5252 O  OE2   . GLU B 1 159 ? -34.444 10.469  15.938  1 24.084  ? 151  GLU B OE2   1 
ATOM   5253 N  N     . SER B 1 160 ? -30.177 13.125  16.845  1 17.473  ? 152  SER B N     1 
ATOM   5254 C  CA    . SER B 1 160 ? -28.993 12.545  16.213  1 17.184  ? 152  SER B CA    1 
ATOM   5255 C  C     . SER B 1 160 ? -27.828 12.461  17.194  1 17.885  ? 152  SER B C     1 
ATOM   5256 O  O     . SER B 1 160 ? -27.54  13.458  17.887  1 16.784  ? 152  SER B O     1 
ATOM   5257 C  CB    . SER B 1 160 ? -28.592 13.348  15.014  1 16.734  ? 152  SER B CB    1 
ATOM   5258 O  OG    . SER B 1 160 ? -27.31  12.919  14.581  1 18.769  ? 152  SER B OG    1 
ATOM   5259 N  N     . THR B 1 161 ? -27.169 11.284  17.189  1 16.975  ? 153  THR B N     1 
ATOM   5260 C  CA    . THR B 1 161 ? -25.891 11.057  17.875  1 15.46   ? 153  THR B CA    1 
ATOM   5261 C  C     . THR B 1 161 ? -24.673 11.271  16.967  1 15.242  ? 153  THR B C     1 
ATOM   5262 O  O     . THR B 1 161 ? -23.544 11.134  17.449  1 15.279  ? 153  THR B O     1 
ATOM   5263 C  CB    . THR B 1 161 ? -25.807 9.707   18.588  1 14.706  ? 153  THR B CB    1 
ATOM   5264 O  OG1   . THR B 1 161 ? -26.204 8.691   17.673  1 14.085  ? 153  THR B OG1   1 
ATOM   5265 C  CG2   . THR B 1 161 ? -26.634 9.684   19.849  1 14.718  ? 153  THR B CG2   1 
ATOM   5266 N  N     . ALA B 1 162 ? -24.885 11.614  15.682  1 13.942  ? 154  ALA B N     1 
ATOM   5267 C  CA    . ALA B 1 162 ? -23.847 11.974  14.71   1 14.454  ? 154  ALA B CA    1 
ATOM   5268 C  C     . ALA B 1 162 ? -22.655 11.001  14.756  1 14.823  ? 154  ALA B C     1 
ATOM   5269 O  O     . ALA B 1 162 ? -21.539 11.423  15.062  1 14.89   ? 154  ALA B O     1 
ATOM   5270 C  CB    . ALA B 1 162 ? -23.442 13.446  14.876  1 13.683  ? 154  ALA B CB    1 
ATOM   5271 N  N     . ASN B 1 163 ? -22.916 9.695   14.522  1 15.297  ? 155  ASN B N     1 
ATOM   5272 C  CA    . ASN B 1 163 ? -22.003 8.614   14.899  1 14.431  ? 155  ASN B CA    1 
ATOM   5273 C  C     . ASN B 1 163 ? -21.57  7.7     13.743  1 14.794  ? 155  ASN B C     1 
ATOM   5274 O  O     . ASN B 1 163 ? -20.879 6.705   14.009  1 15.181  ? 155  ASN B O     1 
ATOM   5275 C  CB    . ASN B 1 163 ? -22.577 7.822   16.079  1 15.061  ? 155  ASN B CB    1 
ATOM   5276 C  CG    . ASN B 1 163 ? -23.766 6.93    15.775  1 14.246  ? 155  ASN B CG    1 
ATOM   5277 O  OD1   . ASN B 1 163 ? -24.315 6.917   14.67   1 14.573  ? 155  ASN B OD1   1 
ATOM   5278 N  ND2   . ASN B 1 163 ? -24.188 6.155   16.758  1 13.355  ? 155  ASN B ND2   1 
ATOM   5279 N  N     . THR B 1 164 ? -21.977 8.022   12.496  1 15.404  ? 156  THR B N     1 
ATOM   5280 C  CA    . THR B 1 164 ? -22.008 7.051   11.404  1 15.83   ? 156  THR B CA    1 
ATOM   5281 C  C     . THR B 1 164 ? -20.814 7.22    10.461  1 15.883  ? 156  THR B C     1 
ATOM   5282 O  O     . THR B 1 164 ? -20.14  6.234   10.183  1 15.467  ? 156  THR B O     1 
ATOM   5283 C  CB    . THR B 1 164 ? -23.361 7.016   10.675  1 17.045  ? 156  THR B CB    1 
ATOM   5284 O  OG1   . THR B 1 164 ? -24.368 6.834   11.669  1 18.258  ? 156  THR B OG1   1 
ATOM   5285 C  CG2   . THR B 1 164 ? -23.45  5.935   9.606   1 15.682  ? 156  THR B CG2   1 
ATOM   5286 N  N     . ASN B 1 165 ? -20.611 8.436   9.917   1 17.02   ? 157  ASN B N     1 
ATOM   5287 C  CA    . ASN B 1 165 ? -19.631 8.723   8.869   1 16.353  ? 157  ASN B CA    1 
ATOM   5288 C  C     . ASN B 1 165 ? -19.186 10.185  8.952   1 17.118  ? 157  ASN B C     1 
ATOM   5289 O  O     . ASN B 1 165 ? -19.826 10.995  9.637   1 18.603  ? 157  ASN B O     1 
ATOM   5290 C  CB    . ASN B 1 165 ? -20.106 8.261   7.49    1 16.21   ? 157  ASN B CB    1 
ATOM   5291 C  CG    . ASN B 1 165 ? -19.027 8.175   6.416   1 16.172  ? 157  ASN B CG    1 
ATOM   5292 O  OD1   . ASN B 1 165 ? -17.816 8.181   6.686   1 15.922  ? 157  ASN B OD1   1 
ATOM   5293 N  ND2   . ASN B 1 165 ? -19.443 8.071   5.16    1 17.082  ? 157  ASN B ND2   1 
ATOM   5294 N  N     . VAL B 1 166 ? -18.045 10.486  8.301   1 14.991  ? 158  VAL B N     1 
ATOM   5295 C  CA    . VAL B 1 166 ? -17.434 11.811  8.248   1 15.89   ? 158  VAL B CA    1 
ATOM   5296 C  C     . VAL B 1 166 ? -17.176 12.19   6.785   1 15.703  ? 158  VAL B C     1 
ATOM   5297 O  O     . VAL B 1 166 ? -17.055 11.308  5.93    1 16.811  ? 158  VAL B O     1 
ATOM   5298 C  CB    . VAL B 1 166 ? -16.19  12.038  9.149   1 15.05   ? 158  VAL B CB    1 
ATOM   5299 C  CG1   . VAL B 1 166 ? -16.497 11.828  10.624  1 15.253  ? 158  VAL B CG1   1 
ATOM   5300 C  CG2   . VAL B 1 166 ? -14.971 11.203  8.744   1 14.669  ? 158  VAL B CG2   1 
ATOM   5301 N  N     . VAL B 1 167 ? -17.081 13.504  6.526   1 15.892  ? 159  VAL B N     1 
ATOM   5302 C  CA    . VAL B 1 167 ? -16.738 14.07   5.224   1 15.585  ? 159  VAL B CA    1 
ATOM   5303 C  C     . VAL B 1 167 ? -16.087 15.443  5.434   1 16.587  ? 159  VAL B C     1 
ATOM   5304 O  O     . VAL B 1 167 ? -16.467 16.184  6.358   1 17.595  ? 159  VAL B O     1 
ATOM   5305 C  CB    . VAL B 1 167 ? -17.93  14.057  4.229   1 14.399  ? 159  VAL B CB    1 
ATOM   5306 C  CG1   . VAL B 1 167 ? -19.044 15.058  4.564   1 13.001  ? 159  VAL B CG1   1 
ATOM   5307 C  CG2   . VAL B 1 167 ? -17.505 14.142  2.758   1 14.009  ? 159  VAL B CG2   1 
ATOM   5308 N  N     . MET B 1 168 ? -15.104 15.739  4.561   1 16.632  ? 160  MET B N     1 
ATOM   5309 C  CA    . MET B 1 168 ? -14.589 17.077  4.318   1 17.933  ? 160  MET B CA    1 
ATOM   5310 C  C     . MET B 1 168 ? -15.099 17.575  2.958   1 18.76   ? 160  MET B C     1 
ATOM   5311 O  O     . MET B 1 168 ? -14.68  17.074  1.901   1 20.483  ? 160  MET B O     1 
ATOM   5312 C  CB    . MET B 1 168 ? -13.059 17.1    4.429   1 18.984  ? 160  MET B CB    1 
ATOM   5313 C  CG    . MET B 1 168 ? -12.408 18.464  4.199   1 20.917  ? 160  MET B CG    1 
ATOM   5314 S  SD    . MET B 1 168 ? -12.59  19.638  5.557   1 23.844  ? 160  MET B SD    1 
ATOM   5315 C  CE    . MET B 1 168 ? -11.444 18.847  6.708   1 22.634  ? 160  MET B CE    1 
ATOM   5316 N  N     . HIS B 1 169 ? -15.978 18.584  3.013   1 18.281  ? 161  HIS B N     1 
ATOM   5317 C  CA    . HIS B 1 169 ? -16.552 19.193  1.816   1 18.756  ? 161  HIS B CA    1 
ATOM   5318 C  C     . HIS B 1 169 ? -16.577 20.71   1.958   1 19.715  ? 161  HIS B C     1 
ATOM   5319 O  O     . HIS B 1 169 ? -17.041 21.226  2.982   1 19.466  ? 161  HIS B O     1 
ATOM   5320 C  CB    . HIS B 1 169 ? -17.943 18.627  1.499   1 19.497  ? 161  HIS B CB    1 
ATOM   5321 C  CG    . HIS B 1 169 ? -18.449 19.109  0.178   1 18.518  ? 161  HIS B CG    1 
ATOM   5322 N  ND1   . HIS B 1 169 ? -17.972 18.624  -1.024  1 17.689  ? 161  HIS B ND1   1 
ATOM   5323 C  CD2   . HIS B 1 169 ? -19.305 20.091  -0.124  1 18.061  ? 161  HIS B CD2   1 
ATOM   5324 C  CE1   . HIS B 1 169 ? -18.557 19.277  -2.016  1 17.417  ? 161  HIS B CE1   1 
ATOM   5325 N  NE2   . HIS B 1 169 ? -19.37  20.174  -1.496  1 18.811  ? 161  HIS B NE2   1 
ATOM   5326 N  N     . ALA B 1 170 ? -16.092 21.394  0.9     1 19.14   ? 162  ALA B N     1 
ATOM   5327 C  CA    . ALA B 1 170 ? -16.02  22.85   0.796   1 20.246  ? 162  ALA B CA    1 
ATOM   5328 C  C     . ALA B 1 170 ? -15.325 23.476  2.02    1 19.069  ? 162  ALA B C     1 
ATOM   5329 O  O     . ALA B 1 170 ? -15.811 24.453  2.59    1 19.766  ? 162  ALA B O     1 
ATOM   5330 C  CB    . ALA B 1 170 ? -17.417 23.416  0.49    1 19.762  ? 162  ALA B CB    1 
ATOM   5331 N  N     . GLY B 1 171 ? -14.211 22.852  2.453   1 19.967  ? 163  GLY B N     1 
ATOM   5332 C  CA    . GLY B 1 171 ? -13.412 23.216  3.622   1 19.604  ? 163  GLY B CA    1 
ATOM   5333 C  C     . GLY B 1 171 ? -14.142 23.091  4.96    1 21.576  ? 163  GLY B C     1 
ATOM   5334 O  O     . GLY B 1 171 ? -13.75  23.762  5.92    1 22.441  ? 163  GLY B O     1 
ATOM   5335 N  N     . ARG B 1 172 ? -15.179 22.238  5.013   1 20.383  ? 164  ARG B N     1 
ATOM   5336 C  CA    . ARG B 1 172 ? -15.99  21.994  6.204   1 22.17   ? 164  ARG B CA    1 
ATOM   5337 C  C     . ARG B 1 172 ? -15.976 20.503  6.541   1 20.09   ? 164  ARG B C     1 
ATOM   5338 O  O     . ARG B 1 172 ? -16.212 19.679  5.654   1 20.472  ? 164  ARG B O     1 
ATOM   5339 C  CB    . ARG B 1 172 ? -17.403 22.578  6.069   1 25.223  ? 164  ARG B CB    1 
ATOM   5340 C  CG    . ARG B 1 172 ? -17.471 24.084  5.868   1 28.491  ? 164  ARG B CG    1 
ATOM   5341 C  CD    . ARG B 1 172 ? -18.899 24.344  6.229   1 35.224  ? 164  ARG B CD    1 
ATOM   5342 N  NE    . ARG B 1 172 ? -19.274 25.728  5.93    1 35.089  ? 164  ARG B NE    1 
ATOM   5343 C  CZ    . ARG B 1 172 ? -19.726 26.656  6.754   1 34.184  ? 164  ARG B CZ    1 
ATOM   5344 N  NH1   . ARG B 1 172 ? -19.826 26.457  8.06    1 27.618  ? 164  ARG B NH1   1 
ATOM   5345 N  NH2   . ARG B 1 172 ? -20.077 27.813  6.231   1 38.15   ? 164  ARG B NH2   1 
ATOM   5346 N  N     . PHE B 1 173 ? -15.689 20.193  7.818   1 18.675  ? 165  PHE B N     1 
ATOM   5347 C  CA    . PHE B 1 173 ? -15.598 18.836  8.349   1 18.663  ? 165  PHE B CA    1 
ATOM   5348 C  C     . PHE B 1 173 ? -16.875 18.502  9.128   1 18.255  ? 165  PHE B C     1 
ATOM   5349 O  O     . PHE B 1 173 ? -17.191 19.195  10.097  1 17.667  ? 165  PHE B O     1 
ATOM   5350 C  CB    . PHE B 1 173 ? -14.301 18.638  9.144   1 18.24   ? 165  PHE B CB    1 
ATOM   5351 C  CG    . PHE B 1 173 ? -14.111 17.227  9.689   1 18.566  ? 165  PHE B CG    1 
ATOM   5352 C  CD1   . PHE B 1 173 ? -13.801 16.144  8.842   1 18.989  ? 165  PHE B CD1   1 
ATOM   5353 C  CD2   . PHE B 1 173 ? -14.235 16.991  11.068  1 19.064  ? 165  PHE B CD2   1 
ATOM   5354 C  CE1   . PHE B 1 173 ? -13.687 14.841  9.358   1 18.974  ? 165  PHE B CE1   1 
ATOM   5355 C  CE2   . PHE B 1 173 ? -14.096 15.697  11.589  1 19.629  ? 165  PHE B CE2   1 
ATOM   5356 C  CZ    . PHE B 1 173 ? -13.846 14.615  10.728  1 18.876  ? 165  PHE B CZ    1 
ATOM   5357 N  N     . LEU B 1 174 ? -17.561 17.432  8.684   1 16.889  ? 166  LEU B N     1 
ATOM   5358 C  CA    . LEU B 1 174 ? -18.926 17.072  9.065   1 17.411  ? 166  LEU B CA    1 
ATOM   5359 C  C     . LEU B 1 174 ? -18.943 15.671  9.67    1 17.577  ? 166  LEU B C     1 
ATOM   5360 O  O     . LEU B 1 174 ? -18.343 14.75   9.121   1 18.464  ? 166  LEU B O     1 
ATOM   5361 C  CB    . LEU B 1 174 ? -19.835 17.113  7.83    1 18.421  ? 166  LEU B CB    1 
ATOM   5362 C  CG    . LEU B 1 174 ? -20.47  18.439  7.378   1 18.617  ? 166  LEU B CG    1 
ATOM   5363 C  CD1   . LEU B 1 174 ? -19.575 19.583  6.985   1 19.293  ? 166  LEU B CD1   1 
ATOM   5364 C  CD2   . LEU B 1 174 ? -21.331 18.07   6.166   1 17.418  ? 166  LEU B CD2   1 
ATOM   5365 N  N     . ALA B 1 175 ? -19.645 15.545  10.798  1 17.18   ? 167  ALA B N     1 
ATOM   5366 C  CA    . ALA B 1 175 ? -20.041 14.281  11.401  1 17.476  ? 167  ALA B CA    1 
ATOM   5367 C  C     . ALA B 1 175 ? -21.533 14.09   11.122  1 17.518  ? 167  ALA B C     1 
ATOM   5368 O  O     . ALA B 1 175 ? -22.325 15.023  11.314  1 17.829  ? 167  ALA B O     1 
ATOM   5369 C  CB    . ALA B 1 175 ? -19.75  14.298  12.89   1 18.424  ? 167  ALA B CB    1 
ATOM   5370 N  N     . MET B 1 176 ? -21.879 12.87   10.683  1 16.963  ? 168  MET B N     1 
ATOM   5371 C  CA    . MET B 1 176 ? -23.157 12.574  10.044  1 17.303  ? 168  MET B CA    1 
ATOM   5372 C  C     . MET B 1 176 ? -23.837 11.373  10.695  1 17.966  ? 168  MET B C     1 
ATOM   5373 O  O     . MET B 1 176 ? -23.172 10.436  11.163  1 17.976  ? 168  MET B O     1 
ATOM   5374 C  CB    . MET B 1 176 ? -22.957 12.276  8.555   1 17.25   ? 168  MET B CB    1 
ATOM   5375 C  CG    . MET B 1 176 ? -22.338 13.409  7.735   1 16.351  ? 168  MET B CG    1 
ATOM   5376 S  SD    . MET B 1 176 ? -22.04  12.96   6.017   1 17.525  ? 168  MET B SD    1 
ATOM   5377 C  CE    . MET B 1 176 ? -20.651 11.797  6.044   1 15.016  ? 168  MET B CE    1 
ATOM   5378 N  N     . LYS B 1 177 ? -25.181 11.443  10.705  1 16.996  ? 169  LYS B N     1 
ATOM   5379 C  CA    . LYS B 1 177 ? -26.112 10.362  11.009  1 17.597  ? 169  LYS B CA    1 
ATOM   5380 C  C     . LYS B 1 177 ? -27.451 10.7    10.347  1 17.213  ? 169  LYS B C     1 
ATOM   5381 O  O     . LYS B 1 177 ? -27.884 11.858  10.387  1 16.522  ? 169  LYS B O     1 
ATOM   5382 C  CB    . LYS B 1 177 ? -26.262 10.126  12.519  1 16.034  ? 169  LYS B CB    1 
ATOM   5383 C  CG    . LYS B 1 177 ? -26.949 8.84    12.923  1 15.336  ? 169  LYS B CG    1 
ATOM   5384 C  CD    . LYS B 1 177 ? -27.182 8.733   14.426  1 16.188  ? 169  LYS B CD    1 
ATOM   5385 C  CE    . LYS B 1 177 ? -27.828 7.434   14.845  1 16.086  ? 169  LYS B CE    1 
ATOM   5386 N  NZ    . LYS B 1 177 ? -27.039 6.254   14.475  1 17.102  ? 169  LYS B NZ    1 
ATOM   5387 N  N     . GLU B 1 178 ? -28.086 9.668   9.766   1 17.642  ? 170  GLU B N     1 
ATOM   5388 C  CA    . GLU B 1 178 ? -29.195 9.775   8.815   1 16.816  ? 170  GLU B CA    1 
ATOM   5389 C  C     . GLU B 1 178 ? -30.481 10.41   9.373   1 17.949  ? 170  GLU B C     1 
ATOM   5390 O  O     . GLU B 1 178 ? -31.322 10.817  8.566   1 20.167  ? 170  GLU B O     1 
ATOM   5391 C  CB    . GLU B 1 178 ? -29.452 8.49    8.022   1 17.356  ? 170  GLU B CB    1 
ATOM   5392 C  CG    . GLU B 1 178 ? -29.996 7.323   8.849   1 17.741  ? 170  GLU B CG    1 
ATOM   5393 C  CD    . GLU B 1 178 ? -29.583 6.036   8.191   1 19.364  ? 170  GLU B CD    1 
ATOM   5394 O  OE1   . GLU B 1 178 ? -28.401 5.675   8.243   1 19.171  ? 170  GLU B OE1   1 
ATOM   5395 O  OE2   . GLU B 1 178 ? -30.457 5.413   7.583   1 21.75   ? 170  GLU B OE2   1 
ATOM   5396 N  N     . ASN B 1 179 ? -30.65  10.481  10.711  1 17.084  ? 171  ASN B N     1 
ATOM   5397 C  CA    . ASN B 1 179 ? -31.838 11.041  11.369  1 17.876  ? 171  ASN B CA    1 
ATOM   5398 C  C     . ASN B 1 179 ? -31.725 12.557  11.629  1 19.108  ? 171  ASN B C     1 
ATOM   5399 O  O     . ASN B 1 179 ? -32.578 13.123  12.333  1 17.701  ? 171  ASN B O     1 
ATOM   5400 C  CB    . ASN B 1 179 ? -32.232 10.256  12.626  1 15.943  ? 171  ASN B CB    1 
ATOM   5401 C  CG    . ASN B 1 179 ? -31.153 10.199  13.683  1 16.097  ? 171  ASN B CG    1 
ATOM   5402 O  OD1   . ASN B 1 179 ? -29.956 10.365  13.392  1 15.291  ? 171  ASN B OD1   1 
ATOM   5403 N  ND2   . ASN B 1 179 ? -31.56  9.954   14.919  1 14.865  ? 171  ASN B ND2   1 
ATOM   5404 N  N     . GLY B 1 180 ? -30.708 13.219  11.035  1 18.062  ? 172  GLY B N     1 
ATOM   5405 C  CA    . GLY B 1 180 ? -30.515 14.662  11.15   1 16.759  ? 172  GLY B CA    1 
ATOM   5406 C  C     . GLY B 1 180 ? -29.537 15.21   10.117  1 17.382  ? 172  GLY B C     1 
ATOM   5407 O  O     . GLY B 1 180 ? -28.84  14.452  9.439   1 16.589  ? 172  GLY B O     1 
ATOM   5408 N  N     . ASN B 1 181 ? -29.472 16.552  10.053  1 17.117  ? 173  ASN B N     1 
ATOM   5409 C  CA    . ASN B 1 181 ? -28.374 17.246  9.397   1 17.489  ? 173  ASN B CA    1 
ATOM   5410 C  C     . ASN B 1 181 ? -27.067 16.987  10.147  1 17.236  ? 173  ASN B C     1 
ATOM   5411 O  O     . ASN B 1 181 ? -27.07  16.566  11.316  1 18.235  ? 173  ASN B O     1 
ATOM   5412 C  CB    . ASN B 1 181 ? -28.735 18.682  9.01    1 19.269  ? 173  ASN B CB    1 
ATOM   5413 C  CG    . ASN B 1 181 ? -29.624 18.713  7.785   1 20.998  ? 173  ASN B CG    1 
ATOM   5414 O  OD1   . ASN B 1 181 ? -29.163 18.444  6.663   1 18.722  ? 173  ASN B OD1   1 
ATOM   5415 N  ND2   . ASN B 1 181 ? -30.897 19.042  7.981   1 20.464  ? 173  ASN B ND2   1 
ATOM   5416 N  N     . ALA B 1 182 ? -25.96  17.19   9.422   1 17.219  ? 174  ALA B N     1 
ATOM   5417 C  CA    . ALA B 1 182 ? -24.607 17.04   9.941   1 17.618  ? 174  ALA B CA    1 
ATOM   5418 C  C     . ALA B 1 182 ? -24.288 18.11   10.984  1 17.601  ? 174  ALA B C     1 
ATOM   5419 O  O     . ALA B 1 182 ? -24.87  19.213  10.975  1 17.727  ? 174  ALA B O     1 
ATOM   5420 C  CB    . ALA B 1 182 ? -23.626 17.082  8.822   1 16.685  ? 174  ALA B CB    1 
ATOM   5421 N  N     . TYR B 1 183 ? -23.413 17.708  11.918  1 16.837  ? 175  TYR B N     1 
ATOM   5422 C  CA    . TYR B 1 183 ? -22.715 18.62   12.807  1 17.446  ? 175  TYR B CA    1 
ATOM   5423 C  C     . TYR B 1 183 ? -21.312 18.844  12.264  1 17.713  ? 175  TYR B C     1 
ATOM   5424 O  O     . TYR B 1 183 ? -20.623 17.889  11.9    1 19.922  ? 175  TYR B O     1 
ATOM   5425 C  CB    . TYR B 1 183 ? -22.678 18.102  14.24   1 17.018  ? 175  TYR B CB    1 
ATOM   5426 C  CG    . TYR B 1 183 ? -23.989 18.119  15.006  1 17.906  ? 175  TYR B CG    1 
ATOM   5427 C  CD1   . TYR B 1 183 ? -24.888 17.037  14.922  1 18.055  ? 175  TYR B CD1   1 
ATOM   5428 C  CD2   . TYR B 1 183 ? -24.295 19.19   15.868  1 17.131  ? 175  TYR B CD2   1 
ATOM   5429 C  CE1   . TYR B 1 183 ? -26.066 17.027  15.675  1 18.41   ? 175  TYR B CE1   1 
ATOM   5430 C  CE2   . TYR B 1 183 ? -25.469 19.184  16.622  1 18.055  ? 175  TYR B CE2   1 
ATOM   5431 C  CZ    . TYR B 1 183 ? -26.35  18.099  16.528  1 17.875  ? 175  TYR B CZ    1 
ATOM   5432 O  OH    . TYR B 1 183 ? -27.501 18.069  17.268  1 17.553  ? 175  TYR B OH    1 
ATOM   5433 N  N     . GLU B 1 184 ? -20.924 20.126  12.25   1 18.144  ? 176  GLU B N     1 
ATOM   5434 C  CA    . GLU B 1 184 ? -19.607 20.592  11.856  1 17.736  ? 176  GLU B CA    1 
ATOM   5435 C  C     . GLU B 1 184 ? -18.686 20.602  13.069  1 18.074  ? 176  GLU B C     1 
ATOM   5436 O  O     . GLU B 1 184 ? -19.066 21.036  14.161  1 17.732  ? 176  GLU B O     1 
ATOM   5437 C  CB    . GLU B 1 184 ? -19.661 21.976  11.212  1 17.103  ? 176  GLU B CB    1 
ATOM   5438 C  CG    . GLU B 1 184 ? -18.364 22.368  10.504  1 18.623  ? 176  GLU B CG    1 
ATOM   5439 C  CD    . GLU B 1 184 ? -18.262 23.747  9.896   1 21.104  ? 176  GLU B CD    1 
ATOM   5440 O  OE1   . GLU B 1 184 ? -19.249 24.514  9.967   1 21.296  ? 176  GLU B OE1   1 
ATOM   5441 O  OE2   . GLU B 1 184 ? -17.177 24.022  9.351   1 19.929  ? 176  GLU B OE2   1 
ATOM   5442 N  N     . MET B 1 185 ? -17.442 20.174  12.8    1 19.098  ? 177  MET B N     1 
ATOM   5443 C  CA    . MET B 1 185 ? -16.347 20.123  13.759  1 19.267  ? 177  MET B CA    1 
ATOM   5444 C  C     . MET B 1 185 ? -15.122 20.799  13.159  1 19.235  ? 177  MET B C     1 
ATOM   5445 O  O     . MET B 1 185 ? -14.912 20.735  11.939  1 18.969  ? 177  MET B O     1 
ATOM   5446 C  CB    . MET B 1 185 ? -16.022 18.677  14.16   1 18.279  ? 177  MET B CB    1 
ATOM   5447 C  CG    . MET B 1 185 ? -17.174 17.908  14.816  1 18.393  ? 177  MET B CG    1 
ATOM   5448 S  SD    . MET B 1 185 ? -16.871 16.131  14.838  1 19.473  ? 177  MET B SD    1 
ATOM   5449 C  CE    . MET B 1 185 ? -16.027 15.973  16.417  1 20.307  ? 177  MET B CE    1 
ATOM   5450 N  N     . ASP B 1 186 ? -14.326 21.439  14.041  1 18.54   ? 178  ASP B N     1 
ATOM   5451 C  CA    . ASP B 1 186 ? -12.984 21.896  13.707  1 18.927  ? 178  ASP B CA    1 
ATOM   5452 C  C     . ASP B 1 186 ? -12.136 20.677  13.326  1 17.896  ? 178  ASP B C     1 
ATOM   5453 O  O     . ASP B 1 186 ? -12.128 19.716  14.095  1 17.256  ? 178  ASP B O     1 
ATOM   5454 C  CB    . ASP B 1 186 ? -12.352 22.729  14.811  1 18.046  ? 178  ASP B CB    1 
ATOM   5455 C  CG    . ASP B 1 186 ? -11     23.318  14.434  1 18.381  ? 178  ASP B CG    1 
ATOM   5456 O  OD1   . ASP B 1 186 ? -9.968  22.606  14.533  1 19.576  ? 178  ASP B OD1   1 
ATOM   5457 O  OD2   . ASP B 1 186 ? -10.99  24.479  14.012  1 19.371  ? 178  ASP B OD2   1 
ATOM   5458 N  N     . PRO B 1 187 ? -11.406 20.658  12.173  1 18.728  ? 179  PRO B N     1 
ATOM   5459 C  CA    . PRO B 1 187 ? -10.639 19.476  11.771  1 19.634  ? 179  PRO B CA    1 
ATOM   5460 C  C     . PRO B 1 187 ? -9.393  19.147  12.607  1 21.482  ? 179  PRO B C     1 
ATOM   5461 O  O     . PRO B 1 187 ? -8.834  18.062  12.429  1 20.591  ? 179  PRO B O     1 
ATOM   5462 C  CB    . PRO B 1 187 ? -10.374 19.702  10.291  1 20.444  ? 179  PRO B CB    1 
ATOM   5463 C  CG    . PRO B 1 187 ? -10.305 21.219  10.208  1 19.136  ? 179  PRO B CG    1 
ATOM   5464 C  CD    . PRO B 1 187 ? -11.319 21.735  11.164  1 18.742  ? 179  PRO B CD    1 
ATOM   5465 N  N     . HIS B 1 188 ? -9.001  20.05   13.529  1 19.653  ? 180  HIS B N     1 
ATOM   5466 C  CA    . HIS B 1 188 ? -7.761  19.956  14.296  1 20.244  ? 180  HIS B CA    1 
ATOM   5467 C  C     . HIS B 1 188 ? -8.047  19.74   15.787  1 19.954  ? 180  HIS B C     1 
ATOM   5468 O  O     . HIS B 1 188 ? -7.403  18.885  16.401  1 22.111  ? 180  HIS B O     1 
ATOM   5469 C  CB    . HIS B 1 188 ? -6.861  21.18   14.069  1 19.747  ? 180  HIS B CB    1 
ATOM   5470 C  CG    . HIS B 1 188 ? -6.878  21.728  12.685  1 19.541  ? 180  HIS B CG    1 
ATOM   5471 N  ND1   . HIS B 1 188 ? -6.207  21.103  11.658  1 19.619  ? 180  HIS B ND1   1 
ATOM   5472 C  CD2   . HIS B 1 188 ? -7.491  22.788  12.14   1 19.903  ? 180  HIS B CD2   1 
ATOM   5473 C  CE1   . HIS B 1 188 ? -6.383  21.788  10.54   1 20.044  ? 180  HIS B CE1   1 
ATOM   5474 N  NE2   . HIS B 1 188 ? -7.161  22.812  10.804  1 19.122  ? 180  HIS B NE2   1 
ATOM   5475 N  N     . THR B 1 189 ? -8.945  20.552  16.36   1 17.461  ? 181  THR B N     1 
ATOM   5476 C  CA    . THR B 1 189 ? -9.322  20.476  17.774  1 17.634  ? 181  THR B CA    1 
ATOM   5477 C  C     . THR B 1 189 ? -10.486 19.507  17.973  1 17.341  ? 181  THR B C     1 
ATOM   5478 O  O     . THR B 1 189 ? -10.726 19.104  19.11   1 18.076  ? 181  THR B O     1 
ATOM   5479 C  CB    . THR B 1 189 ? -9.641  21.838  18.417  1 16.634  ? 181  THR B CB    1 
ATOM   5480 O  OG1   . THR B 1 189 ? -10.844 22.296  17.801  1 15.335  ? 181  THR B OG1   1 
ATOM   5481 C  CG2   . THR B 1 189 ? -8.487  22.832  18.374  1 15.657  ? 181  THR B CG2   1 
ATOM   5482 N  N     . LEU B 1 190 ? -11.266 19.233  16.903  1 18.117  ? 182  LEU B N     1 
ATOM   5483 C  CA    . LEU B 1 190 ? -12.507 18.444  16.923  1 18.316  ? 182  LEU B CA    1 
ATOM   5484 C  C     . LEU B 1 190 ? -13.637 19.096  17.741  1 19.766  ? 182  LEU B C     1 
ATOM   5485 O  O     . LEU B 1 190 ? -14.643 18.434  18.047  1 18.735  ? 182  LEU B O     1 
ATOM   5486 C  CB    . LEU B 1 190 ? -12.298 16.946  17.228  1 17.652  ? 182  LEU B CB    1 
ATOM   5487 C  CG    . LEU B 1 190 ? -11.48  16.124  16.219  1 16.448  ? 182  LEU B CG    1 
ATOM   5488 C  CD1   . LEU B 1 190 ? -11.329 14.734  16.828  1 16.056  ? 182  LEU B CD1   1 
ATOM   5489 C  CD2   . LEU B 1 190 ? -12.161 16.012  14.855  1 14.598  ? 182  LEU B CD2   1 
ATOM   5490 N  N     . LYS B 1 191 ? -13.482 20.403  18.078  1 21.178  ? 183  LYS B N     1 
ATOM   5491 C  CA    . LYS B 1 191 ? -14.504 21.252  18.686  1 21.07   ? 183  LYS B CA    1 
ATOM   5492 C  C     . LYS B 1 191 ? -15.685 21.366  17.718  1 18.661  ? 183  LYS B C     1 
ATOM   5493 O  O     . LYS B 1 191 ? -15.467 21.617  16.542  1 17.432  ? 183  LYS B O     1 
ATOM   5494 C  CB    . LYS B 1 191 ? -13.926 22.612  19.113  1 25.051  ? 183  LYS B CB    1 
ATOM   5495 C  CG    . LYS B 1 191 ? -14.889 23.632  19.728  1 28.523  ? 183  LYS B CG    1 
ATOM   5496 C  CD    . LYS B 1 191 ? -14.213 24.827  20.395  1 36.671  ? 183  LYS B CD    1 
ATOM   5497 C  CE    . LYS B 1 191 ? -15.106 25.9    20.953  1 37.757  ? 183  LYS B CE    1 
ATOM   5498 N  NZ    . LYS B 1 191 ? -16.113 25.409  21.899  1 37.585  ? 183  LYS B NZ    1 
ATOM   5499 N  N     . THR B 1 192 ? -16.907 21.169  18.245  1 17.36   ? 184  THR B N     1 
ATOM   5500 C  CA    . THR B 1 192 ? -18.16  21.326  17.516  1 18.147  ? 184  THR B CA    1 
ATOM   5501 C  C     . THR B 1 192 ? -18.428 22.82   17.276  1 18.409  ? 184  THR B C     1 
ATOM   5502 O  O     . THR B 1 192 ? -18.38  23.641  18.204  1 19.267  ? 184  THR B O     1 
ATOM   5503 C  CB    . THR B 1 192 ? -19.291 20.602  18.251  1 18.863  ? 184  THR B CB    1 
ATOM   5504 O  OG1   . THR B 1 192 ? -18.896 19.232  18.344  1 18.978  ? 184  THR B OG1   1 
ATOM   5505 C  CG2   . THR B 1 192 ? -20.632 20.637  17.531  1 18.186  ? 184  THR B CG2   1 
ATOM   5506 N  N     . LEU B 1 193 ? -18.748 23.116  16.012  1 19.146  ? 185  LEU B N     1 
ATOM   5507 C  CA    . LEU B 1 193 ? -18.851 24.466  15.472  1 19.817  ? 185  LEU B CA    1 
ATOM   5508 C  C     . LEU B 1 193 ? -20.298 24.862  15.175  1 18.641  ? 185  LEU B C     1 
ATOM   5509 O  O     . LEU B 1 193 ? -20.61  26.048  15.271  1 17.562  ? 185  LEU B O     1 
ATOM   5510 C  CB    . LEU B 1 193 ? -17.926 24.652  14.266  1 17.901  ? 185  LEU B CB    1 
ATOM   5511 C  CG    . LEU B 1 193 ? -16.415 24.478  14.507  1 19.633  ? 185  LEU B CG    1 
ATOM   5512 C  CD1   . LEU B 1 193 ? -15.674 24.734  13.194  1 18.511  ? 185  LEU B CD1   1 
ATOM   5513 C  CD2   . LEU B 1 193 ? -15.785 25.321  15.651  1 19.751  ? 185  LEU B CD2   1 
ATOM   5514 N  N     . GLY B 1 194 ? -21.145 23.889  14.794  1 16.925  ? 186  GLY B N     1 
ATOM   5515 C  CA    . GLY B 1 194 ? -22.528 24.171  14.44   1 17.503  ? 186  GLY B CA    1 
ATOM   5516 C  C     . GLY B 1 194 ? -23.269 22.977  13.846  1 19.527  ? 186  GLY B C     1 
ATOM   5517 O  O     . GLY B 1 194 ? -22.734 21.864  13.751  1 18.16   ? 186  GLY B O     1 
ATOM   5518 N  N     . TYR B 1 195 ? -24.547 23.251  13.534  1 20.899  ? 187  TYR B N     1 
ATOM   5519 C  CA    . TYR B 1 195 ? -25.501 22.307  12.973  1 19.949  ? 187  TYR B CA    1 
ATOM   5520 C  C     . TYR B 1 195 ? -25.961 22.848  11.623  1 21.897  ? 187  TYR B C     1 
ATOM   5521 O  O     . TYR B 1 195 ? -26.249 24.048  11.496  1 20.197  ? 187  TYR B O     1 
ATOM   5522 C  CB    . TYR B 1 195 ? -26.66  22.038  13.943  1 19.252  ? 187  TYR B CB    1 
ATOM   5523 C  CG    . TYR B 1 195 ? -27.741 21.097  13.411  1 20.053  ? 187  TYR B CG    1 
ATOM   5524 C  CD1   . TYR B 1 195 ? -27.581 19.704  13.48   1 18.382  ? 187  TYR B CD1   1 
ATOM   5525 C  CD2   . TYR B 1 195 ? -28.926 21.598  12.83   1 20.433  ? 187  TYR B CD2   1 
ATOM   5526 C  CE1   . TYR B 1 195 ? -28.558 18.844  12.98   1 20.408  ? 187  TYR B CE1   1 
ATOM   5527 C  CE2   . TYR B 1 195 ? -29.902 20.736  12.322  1 19.735  ? 187  TYR B CE2   1 
ATOM   5528 C  CZ    . TYR B 1 195 ? -29.723 19.357  12.41   1 20.601  ? 187  TYR B CZ    1 
ATOM   5529 O  OH    . TYR B 1 195 ? -30.663 18.468  11.938  1 21.569  ? 187  TYR B OH    1 
ATOM   5530 N  N     . ASN B 1 196 ? -26.072 21.911  10.663  1 21.402  ? 188  ASN B N     1 
ATOM   5531 C  CA    . ASN B 1 196 ? -26.619 22.098  9.325   1 22.213  ? 188  ASN B CA    1 
ATOM   5532 C  C     . ASN B 1 196 ? -25.815 23.167  8.567   1 23.725  ? 188  ASN B C     1 
ATOM   5533 O  O     . ASN B 1 196 ? -26.447 24.139  8.109   1 24.486  ? 188  ASN B O     1 
ATOM   5534 C  CB    . ASN B 1 196 ? -28.136 22.339  9.368   1 19.638  ? 188  ASN B CB    1 
ATOM   5535 C  CG    . ASN B 1 196 ? -28.855 22.212  8.041   1 19.187  ? 188  ASN B CG    1 
ATOM   5536 O  OD1   . ASN B 1 196 ? -28.267 21.815  7.026   1 18.019  ? 188  ASN B OD1   1 
ATOM   5537 N  ND2   . ASN B 1 196 ? -30.145 22.538  8.039   1 20.654  ? 188  ASN B ND2   1 
ATOM   5538 N  N     . PRO B 1 197 ? -24.444 23.066  8.42    1 25.409  ? 189  PRO B N     1 
ATOM   5539 C  CA    . PRO B 1 197 ? -23.648 24.15   7.824   1 25.066  ? 189  PRO B CA    1 
ATOM   5540 C  C     . PRO B 1 197 ? -24.048 24.551  6.4     1 24.282  ? 189  PRO B C     1 
ATOM   5541 O  O     . PRO B 1 197 ? -23.969 25.73   6.078   1 24.581  ? 189  PRO B O     1 
ATOM   5542 C  CB    . PRO B 1 197 ? -22.198 23.713  7.96    1 24.028  ? 189  PRO B CB    1 
ATOM   5543 C  CG    . PRO B 1 197 ? -22.314 22.195  8.017   1 25.741  ? 189  PRO B CG    1 
ATOM   5544 C  CD    . PRO B 1 197 ? -23.567 21.918  8.775   1 26.056  ? 189  PRO B CD    1 
ATOM   5545 N  N     . PHE B 1 198 ? -24.529 23.576  5.601   1 22.753  ? 190  PHE B N     1 
ATOM   5546 C  CA    . PHE B 1 198 ? -25.002 23.788  4.231   1 21.919  ? 190  PHE B CA    1 
ATOM   5547 C  C     . PHE B 1 198 ? -26.44  24.31   4.145   1 21.356  ? 190  PHE B C     1 
ATOM   5548 O  O     . PHE B 1 198 ? -26.884 24.623  3.042   1 21.852  ? 190  PHE B O     1 
ATOM   5549 C  CB    . PHE B 1 198 ? -24.648 22.631  3.294   1 21.917  ? 190  PHE B CB    1 
ATOM   5550 C  CG    . PHE B 1 198 ? -23.17  22.256  3.225   1 22.711  ? 190  PHE B CG    1 
ATOM   5551 C  CD1   . PHE B 1 198 ? -22.179 23.205  2.898   1 21.223  ? 190  PHE B CD1   1 
ATOM   5552 C  CD2   . PHE B 1 198 ? -22.776 20.935  3.508   1 22.041  ? 190  PHE B CD2   1 
ATOM   5553 C  CE1   . PHE B 1 198 ? -20.824 22.843  2.854   1 23.377  ? 190  PHE B CE1   1 
ATOM   5554 C  CE2   . PHE B 1 198 ? -21.425 20.566  3.438   1 23.622  ? 190  PHE B CE2   1 
ATOM   5555 C  CZ    . PHE B 1 198 ? -20.444 21.527  3.133   1 23.893  ? 190  PHE B CZ    1 
ATOM   5556 N  N     . ASN B 1 199 ? -27.145 24.425  5.288   1 23.736  ? 191  ASN B N     1 
ATOM   5557 C  CA    . ASN B 1 199 ? -28.496 24.982  5.446   1 25.658  ? 191  ASN B CA    1 
ATOM   5558 C  C     . ASN B 1 199 ? -29.491 24.232  4.555   1 23.74   ? 191  ASN B C     1 
ATOM   5559 O  O     . ASN B 1 199 ? -30.24  24.846  3.775   1 21.842  ? 191  ASN B O     1 
ATOM   5560 C  CB    . ASN B 1 199 ? -28.568 26.504  5.249   1 29.297  ? 191  ASN B CB    1 
ATOM   5561 C  CG    . ASN B 1 199 ? -27.688 27.279  6.195   1 37.241  ? 191  ASN B CG    1 
ATOM   5562 O  OD1   . ASN B 1 199 ? -26.716 27.908  5.759   1 40.546  ? 191  ASN B OD1   1 
ATOM   5563 N  ND2   . ASN B 1 199 ? -28.005 27.254  7.483   1 42.088  ? 191  ASN B ND2   1 
ATOM   5564 N  N     . LEU B 1 200 ? -29.452 22.893  4.657   1 21.27   ? 192  LEU B N     1 
ATOM   5565 C  CA    . LEU B 1 200 ? -30.317 21.997  3.896   1 22.096  ? 192  LEU B CA    1 
ATOM   5566 C  C     . LEU B 1 200 ? -31.767 22.151  4.381   1 21.52   ? 192  LEU B C     1 
ATOM   5567 O  O     . LEU B 1 200 ? -31.951 22.282  5.595   1 24.236  ? 192  LEU B O     1 
ATOM   5568 C  CB    . LEU B 1 200 ? -29.812 20.546  3.875   1 21.458  ? 192  LEU B CB    1 
ATOM   5569 C  CG    . LEU B 1 200 ? -28.405 20.28   3.299   1 21.654  ? 192  LEU B CG    1 
ATOM   5570 C  CD1   . LEU B 1 200 ? -28.139 18.793  3.38    1 21.154  ? 192  LEU B CD1   1 
ATOM   5571 C  CD2   . LEU B 1 200 ? -28.091 20.807  1.88    1 20.372  ? 192  LEU B CD2   1 
ATOM   5572 N  N     . PRO B 1 201 ? -32.807 22.22   3.49    1 21.948  ? 193  PRO B N     1 
ATOM   5573 C  CA    . PRO B 1 201 ? -34.203 22.414  3.916   1 21.685  ? 193  PRO B CA    1 
ATOM   5574 C  C     . PRO B 1 201 ? -34.887 21.18   4.511   1 22.932  ? 193  PRO B C     1 
ATOM   5575 O  O     . PRO B 1 201 ? -35.931 21.319  5.157   1 24.523  ? 193  PRO B O     1 
ATOM   5576 C  CB    . PRO B 1 201 ? -34.919 22.942  2.667   1 21.363  ? 193  PRO B CB    1 
ATOM   5577 C  CG    . PRO B 1 201 ? -34.153 22.223  1.563   1 23.251  ? 193  PRO B CG    1 
ATOM   5578 C  CD    . PRO B 1 201 ? -32.707 22.206  2.014   1 20.466  ? 193  PRO B CD    1 
ATOM   5579 N  N     . SER B 1 202 ? -34.32  19.99   4.258   1 21.704  ? 194  SER B N     1 
ATOM   5580 C  CA    . SER B 1 202 ? -34.729 18.743  4.896   1 21.596  ? 194  SER B CA    1 
ATOM   5581 C  C     . SER B 1 202 ? -34.344 18.736  6.376   1 20.117  ? 194  SER B C     1 
ATOM   5582 O  O     . SER B 1 202 ? -33.412 19.422  6.793   1 18.754  ? 194  SER B O     1 
ATOM   5583 C  CB    . SER B 1 202 ? -34.182 17.54   4.159   1 24.158  ? 194  SER B CB    1 
ATOM   5584 O  OG    . SER B 1 202 ? -32.772 17.633  4.048   1 29.097  ? 194  SER B OG    1 
ATOM   5585 N  N     . LYS B 1 203 ? -35.071 17.934  7.156   1 19.633  ? 195  LYS B N     1 
ATOM   5586 C  CA    . LYS B 1 203 ? -34.781 17.665  8.563   1 20.905  ? 195  LYS B CA    1 
ATOM   5587 C  C     . LYS B 1 203 ? -33.608 16.686  8.709   1 21.381  ? 195  LYS B C     1 
ATOM   5588 O  O     . LYS B 1 203 ? -33.067 16.547  9.807   1 23.623  ? 195  LYS B O     1 
ATOM   5589 C  CB    . LYS B 1 203 ? -36.038 17.188  9.308   1 20.867  ? 195  LYS B CB    1 
ATOM   5590 C  CG    . LYS B 1 203 ? -37.187 18.201  9.429   1 21.944  ? 195  LYS B CG    1 
ATOM   5591 C  CD    . LYS B 1 203 ? -38.272 17.561  10.287  1 24.184  ? 195  LYS B CD    1 
ATOM   5592 C  CE    . LYS B 1 203 ? -39.576 18.272  10.344  1 26.481  ? 195  LYS B CE    1 
ATOM   5593 N  NZ    . LYS B 1 203 ? -39.629 19.615  10.902  1 27.456  ? 195  LYS B NZ    1 
ATOM   5594 N  N     . THR B 1 204 ? -33.221 16.01   7.612   1 18.656  ? 196  THR B N     1 
ATOM   5595 C  CA    . THR B 1 204 ? -32.277 14.897  7.605   1 18.659  ? 196  THR B CA    1 
ATOM   5596 C  C     . THR B 1 204 ? -31.276 15.075  6.46    1 18.176  ? 196  THR B C     1 
ATOM   5597 O  O     . THR B 1 204 ? -31.553 15.77   5.474   1 17.496  ? 196  THR B O     1 
ATOM   5598 C  CB    . THR B 1 204 ? -32.997 13.545  7.483   1 20.505  ? 196  THR B CB    1 
ATOM   5599 O  OG1   . THR B 1 204 ? -33.698 13.584  6.239   1 20.024  ? 196  THR B OG1   1 
ATOM   5600 C  CG2   . THR B 1 204 ? -33.895 13.172  8.656   1 19.828  ? 196  THR B CG2   1 
ATOM   5601 N  N     . MET B 1 205 ? -30.124 14.41   6.612   1 17.253  ? 197  MET B N     1 
ATOM   5602 C  CA    . MET B 1 205 ? -29.127 14.18   5.573   1 17.507  ? 197  MET B CA    1 
ATOM   5603 C  C     . MET B 1 205 ? -28.537 12.796  5.815   1 17.441  ? 197  MET B C     1 
ATOM   5604 O  O     . MET B 1 205 ? -28.215 12.476  6.964   1 17.311  ? 197  MET B O     1 
ATOM   5605 C  CB    . MET B 1 205 ? -28.038 15.267  5.58    1 17.835  ? 197  MET B CB    1 
ATOM   5606 C  CG    . MET B 1 205 ? -27.122 15.206  4.362   1 18.008  ? 197  MET B CG    1 
ATOM   5607 S  SD    . MET B 1 205 ? -25.616 16.201  4.377   1 19.923  ? 197  MET B SD    1 
ATOM   5608 C  CE    . MET B 1 205 ? -24.673 15.234  5.562   1 18.117  ? 197  MET B CE    1 
ATOM   5609 N  N     . THR B 1 206 ? -28.394 12.021  4.719   1 17.813  ? 198  THR B N     1 
ATOM   5610 C  CA    . THR B 1 206 ? -27.669 10.753  4.663   1 19.591  ? 198  THR B CA    1 
ATOM   5611 C  C     . THR B 1 206 ? -26.284 10.899  5.304   1 20.067  ? 198  THR B C     1 
ATOM   5612 O  O     . THR B 1 206 ? -25.67  11.968  5.236   1 18.796  ? 198  THR B O     1 
ATOM   5613 C  CB    . THR B 1 206 ? -27.608 10.18   3.239   1 20.684  ? 198  THR B CB    1 
ATOM   5614 O  OG1   . THR B 1 206 ? -27.094 8.845   3.3     1 19.816  ? 198  THR B OG1   1 
ATOM   5615 C  CG2   . THR B 1 206 ? -26.779 10.984  2.247   1 20.083  ? 198  THR B CG2   1 
ATOM   5616 N  N     . ALA B 1 207 ? -25.827 9.804   5.927   1 21.188  ? 199  ALA B N     1 
ATOM   5617 C  CA    . ALA B 1 207 ? -24.429 9.642   6.301   1 19.385  ? 199  ALA B CA    1 
ATOM   5618 C  C     . ALA B 1 207 ? -23.593 9.035   5.17    1 19.165  ? 199  ALA B C     1 
ATOM   5619 O  O     . ALA B 1 207 ? -22.367 8.914   5.286   1 20.373  ? 199  ALA B O     1 
ATOM   5620 C  CB    . ALA B 1 207 ? -24.349 8.855   7.573   1 19.276  ? 199  ALA B CB    1 
ATOM   5621 N  N     . HIS B 1 208 ? -24.246 8.758   4.028   1 18.954  ? 200  HIS B N     1 
ATOM   5622 C  CA    . HIS B 1 208 ? -23.591 8.257   2.837   1 17.449  ? 200  HIS B CA    1 
ATOM   5623 C  C     . HIS B 1 208 ? -23.731 9.221   1.65    1 18.286  ? 200  HIS B C     1 
ATOM   5624 O  O     . HIS B 1 208 ? -24.166 8.755   0.577   1 17.569  ? 200  HIS B O     1 
ATOM   5625 C  CB    . HIS B 1 208 ? -24.072 6.823   2.592   1 17.275  ? 200  HIS B CB    1 
ATOM   5626 C  CG    . HIS B 1 208 ? -23.439 5.87    3.529   1 17.109  ? 200  HIS B CG    1 
ATOM   5627 N  ND1   . HIS B 1 208 ? -22.081 5.633   3.513   1 17.355  ? 200  HIS B ND1   1 
ATOM   5628 C  CD2   . HIS B 1 208 ? -23.957 5.126   4.515   1 17.202  ? 200  HIS B CD2   1 
ATOM   5629 C  CE1   . HIS B 1 208 ? -21.804 4.766   4.465   1 17.492  ? 200  HIS B CE1   1 
ATOM   5630 N  NE2   . HIS B 1 208 ? -22.926 4.442   5.085   1 15.855  ? 200  HIS B NE2   1 
ATOM   5631 N  N     . PRO B 1 209 ? -23.325 10.532  1.714   1 17.299  ? 201  PRO B N     1 
ATOM   5632 C  CA    . PRO B 1 209 ? -23.164 11.302  0.491   1 17.749  ? 201  PRO B CA    1 
ATOM   5633 C  C     . PRO B 1 209 ? -21.917 10.852  -0.266  1 18.988  ? 201  PRO B C     1 
ATOM   5634 O  O     . PRO B 1 209 ? -21.034 10.203  0.316   1 19.451  ? 201  PRO B O     1 
ATOM   5635 C  CB    . PRO B 1 209 ? -23.183 12.752  0.962   1 16.973  ? 201  PRO B CB    1 
ATOM   5636 C  CG    . PRO B 1 209 ? -22.502 12.684  2.303   1 16.716  ? 201  PRO B CG    1 
ATOM   5637 C  CD    . PRO B 1 209 ? -22.868 11.34   2.873   1 17.288  ? 201  PRO B CD    1 
ATOM   5638 N  N     . LYS B 1 210 ? -21.891 11.177  -1.561  1 18.199  ? 202  LYS B N     1 
ATOM   5639 C  CA    . LYS B 1 210 ? -20.795 10.788  -2.436  1 18.272  ? 202  LYS B CA    1 
ATOM   5640 C  C     . LYS B 1 210 ? -20.215 12.05   -3.059  1 18.268  ? 202  LYS B C     1 
ATOM   5641 O  O     . LYS B 1 210 ? -20.958 12.864  -3.622  1 18.376  ? 202  LYS B O     1 
ATOM   5642 C  CB    . LYS B 1 210 ? -21.241 9.708   -3.437  1 18.33   ? 202  LYS B CB    1 
ATOM   5643 C  CG    . LYS B 1 210 ? -22.098 8.521   -2.931  1 17.817  ? 202  LYS B CG    1 
ATOM   5644 C  CD    . LYS B 1 210 ? -21.418 7.529   -1.992  1 18.367  ? 202  LYS B CD    1 
ATOM   5645 C  CE    . LYS B 1 210 ? -22.338 6.468   -1.486  1 16.755  ? 202  LYS B CE    1 
ATOM   5646 N  NZ    . LYS B 1 210 ? -21.687 5.589   -0.511  1 16.374  ? 202  LYS B NZ    1 
ATOM   5647 N  N     . GLN B 1 211 ? -18.886 12.168  -2.962  1 18.695  ? 203  GLN B N     1 
ATOM   5648 C  CA    . GLN B 1 211 ? -18.126 13.248  -3.579  1 20.055  ? 203  GLN B CA    1 
ATOM   5649 C  C     . GLN B 1 211 ? -17.731 12.83   -4.994  1 20.479  ? 203  GLN B C     1 
ATOM   5650 O  O     . GLN B 1 211 ? -16.793 12.052  -5.183  1 20.751  ? 203  GLN B O     1 
ATOM   5651 C  CB    . GLN B 1 211 ? -16.963 13.73   -2.71   1 21.966  ? 203  GLN B CB    1 
ATOM   5652 C  CG    . GLN B 1 211 ? -17.401 14.37   -1.401  1 21.835  ? 203  GLN B CG    1 
ATOM   5653 C  CD    . GLN B 1 211 ? -16.25  14.937  -0.604  1 22.948  ? 203  GLN B CD    1 
ATOM   5654 O  OE1   . GLN B 1 211 ? -16.136 16.158  -0.444  1 29.181  ? 203  GLN B OE1   1 
ATOM   5655 N  NE2   . GLN B 1 211 ? -15.399 14.063  -0.082  1 18.569  ? 203  GLN B NE2   1 
ATOM   5656 N  N     . CYS B 1 212 ? -18.477 13.376  -5.969  1 20.227  ? 204  CYS B N     1 
ATOM   5657 C  CA    . CYS B 1 212 ? -18.319 13.222  -7.407  1 20.945  ? 204  CYS B CA    1 
ATOM   5658 C  C     . CYS B 1 212 ? -16.913 13.639  -7.842  1 20.176  ? 204  CYS B C     1 
ATOM   5659 O  O     . CYS B 1 212 ? -16.522 14.775  -7.596  1 18.732  ? 204  CYS B O     1 
ATOM   5660 C  CB    . CYS B 1 212 ? -19.404 14.056  -8.082  1 21.361  ? 204  CYS B CB    1 
ATOM   5661 S  SG    . CYS B 1 212 ? -19.419 13.94   -9.887  1 24.484  ? 204  CYS B SG    1 
ATOM   5662 N  N     . SER B 1 213 ? -16.191 12.712  -8.502  1 20.842  ? 205  SER B N     1 
ATOM   5663 C  CA    . SER B 1 213 ? -14.851 12.942  -9.036  1 22.379  ? 205  SER B CA    1 
ATOM   5664 C  C     . SER B 1 213 ? -14.863 13.826  -10.293 1 24.68   ? 205  SER B C     1 
ATOM   5665 O  O     . SER B 1 213 ? -13.796 14.281  -10.702 1 25.623  ? 205  SER B O     1 
ATOM   5666 C  CB    . SER B 1 213 ? -14.103 11.643  -9.294  1 22.256  ? 205  SER B CB    1 
ATOM   5667 O  OG    . SER B 1 213 ? -14.725 10.901  -10.338 1 21.99   ? 205  SER B OG    1 
ATOM   5668 N  N     . VAL B 1 214 ? -16.042 14.027  -10.912 1 24.223  ? 206  VAL B N     1 
ATOM   5669 C  CA    . VAL B 1 214 ? -16.218 14.831  -12.117 1 24.238  ? 206  VAL B CA    1 
ATOM   5670 C  C     . VAL B 1 214 ? -16.47  16.275  -11.695 1 25.752  ? 206  VAL B C     1 
ATOM   5671 O  O     . VAL B 1 214 ? -15.719 17.151  -12.12  1 29.998  ? 206  VAL B O     1 
ATOM   5672 C  CB    . VAL B 1 214 ? -17.251 14.329  -13.16  1 26.976  ? 206  VAL B CB    1 
ATOM   5673 C  CG1   . VAL B 1 214 ? -17.34  15.209  -14.414 1 24.036  ? 206  VAL B CG1   1 
ATOM   5674 C  CG2   . VAL B 1 214 ? -16.986 12.89   -13.586 1 25.214  ? 206  VAL B CG2   1 
ATOM   5675 N  N     . THR B 1 215 ? -17.524 16.504  -10.892 1 24.034  ? 207  THR B N     1 
ATOM   5676 C  CA    . THR B 1 215 ? -18.019 17.847  -10.59  1 24.469  ? 207  THR B CA    1 
ATOM   5677 C  C     . THR B 1 215 ? -17.413 18.408  -9.294  1 24.876  ? 207  THR B C     1 
ATOM   5678 O  O     . THR B 1 215 ? -17.461 19.621  -9.065  1 26.155  ? 207  THR B O     1 
ATOM   5679 C  CB    . THR B 1 215 ? -19.553 17.876  -10.57  1 24.245  ? 207  THR B CB    1 
ATOM   5680 O  OG1   . THR B 1 215 ? -19.952 16.996  -9.524  1 22.497  ? 207  THR B OG1   1 
ATOM   5681 C  CG2   . THR B 1 215 ? -20.207 17.542  -11.903 1 23.093  ? 207  THR B CG2   1 
ATOM   5682 N  N     . GLY B 1 216 ? -16.924 17.515  -8.41   1 23.717  ? 208  GLY B N     1 
ATOM   5683 C  CA    . GLY B 1 216 ? -16.593 17.859  -7.038  1 21.6    ? 208  GLY B CA    1 
ATOM   5684 C  C     . GLY B 1 216 ? -17.813 18.068  -6.139  1 22.078  ? 208  GLY B C     1 
ATOM   5685 O  O     . GLY B 1 216 ? -17.624 18.477  -4.996  1 22.919  ? 208  GLY B O     1 
ATOM   5686 N  N     . ASN B 1 217 ? -19.04  17.789  -6.632  1 21.849  ? 209  ASN B N     1 
ATOM   5687 C  CA    . ASN B 1 217 ? -20.277 17.948  -5.871  1 21.669  ? 209  ASN B CA    1 
ATOM   5688 C  C     . ASN B 1 217 ? -20.396 16.882  -4.786  1 20.98   ? 209  ASN B C     1 
ATOM   5689 O  O     . ASN B 1 217 ? -19.991 15.729  -5      1 22.511  ? 209  ASN B O     1 
ATOM   5690 C  CB    . ASN B 1 217 ? -21.532 17.936  -6.737  1 21.22   ? 209  ASN B CB    1 
ATOM   5691 C  CG    . ASN B 1 217 ? -21.679 19.084  -7.709  1 21.821  ? 209  ASN B CG    1 
ATOM   5692 O  OD1   . ASN B 1 217 ? -20.949 20.086  -7.689  1 21.268  ? 209  ASN B OD1   1 
ATOM   5693 N  ND2   . ASN B 1 217 ? -22.666 18.944  -8.575  1 22.438  ? 209  ASN B ND2   1 
ATOM   5694 N  N     . LEU B 1 218 ? -20.911 17.317  -3.625  1 19.69   ? 210  LEU B N     1 
ATOM   5695 C  CA    . LEU B 1 218 ? -21.449 16.465  -2.569  1 21.234  ? 210  LEU B CA    1 
ATOM   5696 C  C     . LEU B 1 218 ? -22.882 16.079  -2.947  1 21.47   ? 210  LEU B C     1 
ATOM   5697 O  O     . LEU B 1 218 ? -23.802 16.904  -2.869  1 22.646  ? 210  LEU B O     1 
ATOM   5698 C  CB    . LEU B 1 218 ? -21.34  17.108  -1.178  1 21.145  ? 210  LEU B CB    1 
ATOM   5699 C  CG    . LEU B 1 218 ? -21.632 16.223  0.045   1 20.822  ? 210  LEU B CG    1 
ATOM   5700 C  CD1   . LEU B 1 218 ? -20.511 15.256  0.395   1 20.404  ? 210  LEU B CD1   1 
ATOM   5701 C  CD2   . LEU B 1 218 ? -21.91  17.146  1.244   1 19.768  ? 210  LEU B CD2   1 
ATOM   5702 N  N     . VAL B 1 219 ? -23.024 14.817  -3.387  1 19.543  ? 211  VAL B N     1 
ATOM   5703 C  CA    . VAL B 1 219 ? -24.271 14.275  -3.905  1 17.531  ? 211  VAL B CA    1 
ATOM   5704 C  C     . VAL B 1 219 ? -24.861 13.385  -2.817  1 16.607  ? 211  VAL B C     1 
ATOM   5705 O  O     . VAL B 1 219 ? -24.22  12.417  -2.395  1 14.782  ? 211  VAL B O     1 
ATOM   5706 C  CB    . VAL B 1 219 ? -24.153 13.526  -5.253  1 19.567  ? 211  VAL B CB    1 
ATOM   5707 C  CG1   . VAL B 1 219 ? -25.534 13.188  -5.835  1 16.38   ? 211  VAL B CG1   1 
ATOM   5708 C  CG2   . VAL B 1 219 ? -23.297 14.272  -6.284  1 18.466  ? 211  VAL B CG2   1 
ATOM   5709 N  N     . GLY B 1 220 ? -26.101 13.713  -2.424  1 16.281  ? 212  GLY B N     1 
ATOM   5710 C  CA    . GLY B 1 220 ? -26.834 12.904  -1.475  1 15.255  ? 212  GLY B CA    1 
ATOM   5711 C  C     . GLY B 1 220 ? -28.319 13.23   -1.412  1 17.622  ? 212  GLY B C     1 
ATOM   5712 O  O     . GLY B 1 220 ? -28.917 13.815  -2.327  1 20.551  ? 212  GLY B O     1 
ATOM   5713 N  N     . PHE B 1 221 ? -28.873 12.817  -0.276  1 15.913  ? 213  PHE B N     1 
ATOM   5714 C  CA    . PHE B 1 221 ? -30.296 12.791  -0.002  1 16.933  ? 213  PHE B CA    1 
ATOM   5715 C  C     . PHE B 1 221 ? -30.513 12.866  1.506   1 17.643  ? 213  PHE B C     1 
ATOM   5716 O  O     . PHE B 1 221 ? -29.573 12.708  2.294   1 19.782  ? 213  PHE B O     1 
ATOM   5717 C  CB    . PHE B 1 221 ? -30.906 11.556  -0.685  1 15.791  ? 213  PHE B CB    1 
ATOM   5718 C  CG    . PHE B 1 221 ? -30.494 10.239  -0.033  1 16.481  ? 213  PHE B CG    1 
ATOM   5719 C  CD1   . PHE B 1 221 ? -29.233 9.65    -0.281  1 16.279  ? 213  PHE B CD1   1 
ATOM   5720 C  CD2   . PHE B 1 221 ? -31.379 9.594   0.848   1 17.614  ? 213  PHE B CD2   1 
ATOM   5721 C  CE1   . PHE B 1 221 ? -28.878 8.434   0.323   1 16.041  ? 213  PHE B CE1   1 
ATOM   5722 C  CE2   . PHE B 1 221 ? -31.011 8.387   1.478   1 17.793  ? 213  PHE B CE2   1 
ATOM   5723 C  CZ    . PHE B 1 221 ? -29.755 7.814   1.215   1 16.781  ? 213  PHE B CZ    1 
ATOM   5724 N  N     . GLY B 1 222 ? -31.774 13.105  1.874   1 16.796  ? 214  GLY B N     1 
ATOM   5725 C  CA    . GLY B 1 222 ? -32.309 12.874  3.203   1 17.306  ? 214  GLY B CA    1 
ATOM   5726 C  C     . GLY B 1 222 ? -33.698 12.267  3.075   1 17.454  ? 214  GLY B C     1 
ATOM   5727 O  O     . GLY B 1 222 ? -34.509 12.806  2.32    1 20.4    ? 214  GLY B O     1 
ATOM   5728 N  N     . TYR B 1 223 ? -33.897 11.106  3.713   1 16.245  ? 215  TYR B N     1 
ATOM   5729 C  CA    . TYR B 1 223 ? -35.206 10.467  3.818   1 16.542  ? 215  TYR B CA    1 
ATOM   5730 C  C     . TYR B 1 223 ? -35.813 10.828  5.173   1 15.922  ? 215  TYR B C     1 
ATOM   5731 O  O     . TYR B 1 223 ? -35.101 11.316  6.054   1 15.99   ? 215  TYR B O     1 
ATOM   5732 C  CB    . TYR B 1 223 ? -35.08  8.977   3.472   1 17.253  ? 215  TYR B CB    1 
ATOM   5733 C  CG    . TYR B 1 223 ? -34.54  8.092   4.591   1 16.191  ? 215  TYR B CG    1 
ATOM   5734 C  CD1   . TYR B 1 223 ? -33.162 7.929   4.781   1 15.954  ? 215  TYR B CD1   1 
ATOM   5735 C  CD2   . TYR B 1 223 ? -35.417 7.434   5.47    1 16.469  ? 215  TYR B CD2   1 
ATOM   5736 C  CE1   . TYR B 1 223 ? -32.675 7.119   5.805   1 16.58   ? 215  TYR B CE1   1 
ATOM   5737 C  CE2   . TYR B 1 223 ? -34.946 6.611   6.489   1 16.865  ? 215  TYR B CE2   1 
ATOM   5738 C  CZ    . TYR B 1 223 ? -33.563 6.445   6.647   1 17.985  ? 215  TYR B CZ    1 
ATOM   5739 O  OH    . TYR B 1 223 ? -33.053 5.648   7.636   1 16.272  ? 215  TYR B OH    1 
ATOM   5740 N  N     . GLU B 1 224 ? -37.12  10.551  5.34    1 15.811  ? 216  GLU B N     1 
ATOM   5741 C  CA    . GLU B 1 224 ? -37.976 11.109  6.398   1 16.85   ? 216  GLU B CA    1 
ATOM   5742 C  C     . GLU B 1 224 ? -37.751 12.622  6.534   1 16.85   ? 216  GLU B C     1 
ATOM   5743 O  O     . GLU B 1 224 ? -37.612 13.162  7.644   1 16.522  ? 216  GLU B O     1 
ATOM   5744 C  CB    . GLU B 1 224 ? -37.839 10.414  7.754   1 18.83   ? 216  GLU B CB    1 
ATOM   5745 C  CG    . GLU B 1 224 ? -37.985 8.894   7.733   1 20.406  ? 216  GLU B CG    1 
ATOM   5746 C  CD    . GLU B 1 224 ? -38.224 8.225   9.069   1 20.862  ? 216  GLU B CD    1 
ATOM   5747 O  OE1   . GLU B 1 224 ? -38.559 8.857   10.115  1 22.225  ? 216  GLU B OE1   1 
ATOM   5748 O  OE2   . GLU B 1 224 ? -38.046 6.994   9.009   1 21.241  ? 216  GLU B OE2   1 
ATOM   5749 N  N     . ALA B 1 225 ? -37.716 13.295  5.371   1 16.817  ? 217  ALA B N     1 
ATOM   5750 C  CA    . ALA B 1 225 ? -37.174 14.636  5.207   1 18.12   ? 217  ALA B CA    1 
ATOM   5751 C  C     . ALA B 1 225 ? -38.065 15.699  5.863   1 19.551  ? 217  ALA B C     1 
ATOM   5752 O  O     . ALA B 1 225 ? -37.582 16.789  6.13    1 21.204  ? 217  ALA B O     1 
ATOM   5753 C  CB    . ALA B 1 225 ? -36.93  14.883  3.733   1 16.978  ? 217  ALA B CB    1 
ATOM   5754 N  N     . LYS B 1 226 ? -39.331 15.342  6.162   1 22.257  ? 218  LYS B N     1 
ATOM   5755 C  CA    . LYS B 1 226 ? -40.394 16.176  6.716   1 22.502  ? 218  LYS B CA    1 
ATOM   5756 C  C     . LYS B 1 226 ? -40.818 15.731  8.12    1 24.278  ? 218  LYS B C     1 
ATOM   5757 O  O     . LYS B 1 226 ? -41.805 16.251  8.647   1 27.377  ? 218  LYS B O     1 
ATOM   5758 C  CB    . LYS B 1 226 ? -41.569 16.3    5.731   1 22.461  ? 218  LYS B CB    1 
ATOM   5759 C  CG    . LYS B 1 226 ? -41.262 17.275  4.618   1 25.497  ? 218  LYS B CG    1 
ATOM   5760 C  CD    . LYS B 1 226 ? -42.323 17.515  3.559   1 28.843  ? 218  LYS B CD    1 
ATOM   5761 C  CE    . LYS B 1 226 ? -41.846 18.51   2.562   1 29.277  ? 218  LYS B CE    1 
ATOM   5762 N  NZ    . LYS B 1 226 ? -42.93  18.878  1.647   1 31.824  ? 218  LYS B NZ    1 
ATOM   5763 N  N     . GLY B 1 227 ? -40.059 14.823  8.748   1 22.61   ? 219  GLY B N     1 
ATOM   5764 C  CA    . GLY B 1 227 ? -40.349 14.401  10.11   1 20.725  ? 219  GLY B CA    1 
ATOM   5765 C  C     . GLY B 1 227 ? -40.529 12.897  10.193  1 21.952  ? 219  GLY B C     1 
ATOM   5766 O  O     . GLY B 1 227 ? -40.413 12.189  9.184   1 21.857  ? 219  GLY B O     1 
ATOM   5767 N  N     . LEU B 1 228 ? -40.819 12.447  11.424  1 24.438  ? 220  LEU B N     1 
ATOM   5768 C  CA    . LEU B 1 228 ? -40.92  11.043  11.796  1 25.413  ? 220  LEU B CA    1 
ATOM   5769 C  C     . LEU B 1 228 ? -41.981 10.347  10.937  1 24.044  ? 220  LEU B C     1 
ATOM   5770 O  O     . LEU B 1 228 ? -43.095 10.854  10.787  1 25.082  ? 220  LEU B O     1 
ATOM   5771 C  CB    . LEU B 1 228 ? -41.267 11.123  13.282  1 27.885  ? 220  LEU B CB    1 
ATOM   5772 C  CG    . LEU B 1 228 ? -40.811 10.018  14.241  1 29.717  ? 220  LEU B CG    1 
ATOM   5773 C  CD1   . LEU B 1 228 ? -39.313 9.825   14.404  1 25.757  ? 220  LEU B CD1   1 
ATOM   5774 C  CD2   . LEU B 1 228 ? -41.398 10.526  15.541  1 31.459  ? 220  LEU B CD2   1 
ATOM   5775 N  N     . ALA B 1 229 ? -41.547 9.259   10.279  1 23.939  ? 221  ALA B N     1 
ATOM   5776 C  CA    . ALA B 1 229 ? -42.31  8.325   9.444   1 23.899  ? 221  ALA B CA    1 
ATOM   5777 C  C     . ALA B 1 229 ? -42.767 8.917   8.091   1 24.094  ? 221  ALA B C     1 
ATOM   5778 O  O     . ALA B 1 229 ? -43.508 8.236   7.355   1 23.09   ? 221  ALA B O     1 
ATOM   5779 C  CB    . ALA B 1 229 ? -43.432 7.623   10.236  1 23.051  ? 221  ALA B CB    1 
ATOM   5780 N  N     . THR B 1 230 ? -42.295 10.135  7.727   1 21.919  ? 222  THR B N     1 
ATOM   5781 C  CA    . THR B 1 230 ? -42.625 10.782  6.449   1 23.167  ? 222  THR B CA    1 
ATOM   5782 C  C     . THR B 1 230 ? -41.931 10.032  5.306   1 23.505  ? 222  THR B C     1 
ATOM   5783 O  O     . THR B 1 230 ? -40.834 9.505   5.493   1 25.094  ? 222  THR B O     1 
ATOM   5784 C  CB    . THR B 1 230 ? -42.386 12.298  6.395   1 21.385  ? 222  THR B CB    1 
ATOM   5785 O  OG1   . THR B 1 230 ? -41.003 12.618  6.553   1 20.086  ? 222  THR B OG1   1 
ATOM   5786 C  CG2   . THR B 1 230 ? -43.21  13.069  7.409   1 22.435  ? 222  THR B CG2   1 
ATOM   5787 N  N     . LYS B 1 231 ? -42.623 9.943   4.158   1 23.738  ? 223  LYS B N     1 
ATOM   5788 C  CA    . LYS B 1 231 ? -42.16  9.238   2.964   1 25.22   ? 223  LYS B CA    1 
ATOM   5789 C  C     . LYS B 1 231 ? -41.255 10.111  2.091   1 23.584  ? 223  LYS B C     1 
ATOM   5790 O  O     . LYS B 1 231 ? -40.603 9.584   1.175   1 22.141  ? 223  LYS B O     1 
ATOM   5791 C  CB    . LYS B 1 231 ? -43.318 8.61    2.174   1 28.066  ? 223  LYS B CB    1 
ATOM   5792 C  CG    . LYS B 1 231 ? -43.893 7.347   2.826   1 29.04   ? 223  LYS B CG    1 
ATOM   5793 C  CD    . LYS B 1 231 ? -44.933 6.607   1.991   1 35.967  ? 223  LYS B CD    1 
ATOM   5794 C  CE    . LYS B 1 231 ? -46.308 7.203   2.086   1 39.429  ? 223  LYS B CE    1 
ATOM   5795 N  NZ    . LYS B 1 231 ? -46.788 7.311   0.711   1 42.945  ? 223  LYS B NZ    1 
ATOM   5796 N  N     . ASP B 1 232 ? -41.186 11.413  2.425   1 20.785  ? 224  ASP B N     1 
ATOM   5797 C  CA    . ASP B 1 232 ? -40.446 12.44   1.704   1 21.367  ? 224  ASP B CA    1 
ATOM   5798 C  C     . ASP B 1 232 ? -38.952 12.133  1.683   1 19.644  ? 224  ASP B C     1 
ATOM   5799 O  O     . ASP B 1 232 ? -38.381 11.693  2.687   1 18.649  ? 224  ASP B O     1 
ATOM   5800 C  CB    . ASP B 1 232 ? -40.739 13.838  2.227   1 20.433  ? 224  ASP B CB    1 
ATOM   5801 C  CG    . ASP B 1 232 ? -42.225 14.139  2.31    1 20.88   ? 224  ASP B CG    1 
ATOM   5802 O  OD1   . ASP B 1 232 ? -42.863 13.716  3.287   1 18.198  ? 224  ASP B OD1   1 
ATOM   5803 O  OD2   . ASP B 1 232 ? -42.733 14.726  1.361   1 21.726  ? 224  ASP B OD2   1 
ATOM   5804 N  N     . VAL B 1 233 ? -38.39  12.333  0.485   1 19.177  ? 225  VAL B N     1 
ATOM   5805 C  CA    . VAL B 1 233 ? -36.968 12.254  0.19    1 19.144  ? 225  VAL B CA    1 
ATOM   5806 C  C     . VAL B 1 233 ? -36.592 13.576  -0.492  1 21.158  ? 225  VAL B C     1 
ATOM   5807 O  O     . VAL B 1 233 ? -37.258 13.979  -1.459  1 22.08   ? 225  VAL B O     1 
ATOM   5808 C  CB    . VAL B 1 233 ? -36.542 10.993  -0.608  1 16.951  ? 225  VAL B CB    1 
ATOM   5809 C  CG1   . VAL B 1 233 ? -35.067 10.994  -1.005  1 17.008  ? 225  VAL B CG1   1 
ATOM   5810 C  CG2   . VAL B 1 233 ? -36.862 9.679   0.114   1 15.946  ? 225  VAL B CG2   1 
ATOM   5811 N  N     . TYR B 1 234 ? -35.522 14.217  0.026   1 19.041  ? 226  TYR B N     1 
ATOM   5812 C  CA    . TYR B 1 234 ? -34.907 15.376  -0.598  1 20.036  ? 226  TYR B CA    1 
ATOM   5813 C  C     . TYR B 1 234 ? -33.558 14.958  -1.167  1 20.762  ? 226  TYR B C     1 
ATOM   5814 O  O     . TYR B 1 234 ? -32.699 14.534  -0.395  1 23.954  ? 226  TYR B O     1 
ATOM   5815 C  CB    . TYR B 1 234 ? -34.775 16.509  0.433   1 19.147  ? 226  TYR B CB    1 
ATOM   5816 C  CG    . TYR B 1 234 ? -34.052 17.755  -0.055  1 19.027  ? 226  TYR B CG    1 
ATOM   5817 C  CD1   . TYR B 1 234 ? -34.637 18.607  -1.012  1 18.815  ? 226  TYR B CD1   1 
ATOM   5818 C  CD2   . TYR B 1 234 ? -32.785 18.087  0.449   1 19.473  ? 226  TYR B CD2   1 
ATOM   5819 C  CE1   . TYR B 1 234 ? -33.983 19.76   -1.443  1 19.253  ? 226  TYR B CE1   1 
ATOM   5820 C  CE2   . TYR B 1 234 ? -32.106 19.22   0.001   1 19.768  ? 226  TYR B CE2   1 
ATOM   5821 C  CZ    . TYR B 1 234 ? -32.717 20.06   -0.935  1 20.339  ? 226  TYR B CZ    1 
ATOM   5822 O  OH    . TYR B 1 234 ? -32.068 21.175  -1.382  1 21.399  ? 226  TYR B OH    1 
ATOM   5823 N  N     . TYR B 1 235 ? -33.404 15.084  -2.49   1 19.336  ? 227  TYR B N     1 
ATOM   5824 C  CA    . TYR B 1 235 ? -32.14  14.933  -3.21   1 19.239  ? 227  TYR B CA    1 
ATOM   5825 C  C     . TYR B 1 235 ? -31.444 16.294  -3.317  1 21.52   ? 227  TYR B C     1 
ATOM   5826 O  O     . TYR B 1 235 ? -32.119 17.311  -3.49   1 19.41   ? 227  TYR B O     1 
ATOM   5827 C  CB    . TYR B 1 235 ? -32.427 14.25   -4.557  1 19.365  ? 227  TYR B CB    1 
ATOM   5828 C  CG    . TYR B 1 235 ? -31.492 14.62   -5.706  1 19.068  ? 227  TYR B CG    1 
ATOM   5829 C  CD1   . TYR B 1 235 ? -30.191 14.073  -5.796  1 18.308  ? 227  TYR B CD1   1 
ATOM   5830 C  CD2   . TYR B 1 235 ? -31.892 15.564  -6.672  1 17.964  ? 227  TYR B CD2   1 
ATOM   5831 C  CE1   . TYR B 1 235 ? -29.327 14.437  -6.832  1 17.463  ? 227  TYR B CE1   1 
ATOM   5832 C  CE2   . TYR B 1 235 ? -31.034 15.941  -7.709  1 18.598  ? 227  TYR B CE2   1 
ATOM   5833 C  CZ    . TYR B 1 235 ? -29.757 15.365  -7.789  1 19.819  ? 227  TYR B CZ    1 
ATOM   5834 O  OH    . TYR B 1 235 ? -28.936 15.714  -8.831  1 20.237  ? 227  TYR B OH    1 
ATOM   5835 N  N     . PHE B 1 236 ? -30.092 16.296  -3.251  1 23.105  ? 228  PHE B N     1 
ATOM   5836 C  CA    . PHE B 1 236 ? -29.29  17.511  -3.353  1 21.329  ? 228  PHE B CA    1 
ATOM   5837 C  C     . PHE B 1 236 ? -27.943 17.213  -4.008  1 21.511  ? 228  PHE B C     1 
ATOM   5838 O  O     . PHE B 1 236 ? -27.425 16.092  -3.937  1 20.24   ? 228  PHE B O     1 
ATOM   5839 C  CB    . PHE B 1 236 ? -29.134 18.247  -2.01   1 22.132  ? 228  PHE B CB    1 
ATOM   5840 C  CG    . PHE B 1 236 ? -28.374 17.417  -0.977  1 22.79   ? 228  PHE B CG    1 
ATOM   5841 C  CD1   . PHE B 1 236 ? -26.963 17.408  -0.957  1 21.975  ? 228  PHE B CD1   1 
ATOM   5842 C  CD2   . PHE B 1 236 ? -29.076 16.635  -0.037  1 23.615  ? 228  PHE B CD2   1 
ATOM   5843 C  CE1   . PHE B 1 236 ? -26.26  16.615  -0.048  1 23.012  ? 228  PHE B CE1   1 
ATOM   5844 C  CE2   . PHE B 1 236 ? -28.369 15.869  0.91    1 24.028  ? 228  PHE B CE2   1 
ATOM   5845 C  CZ    . PHE B 1 236 ? -26.966 15.856  0.889   1 23.489  ? 228  PHE B CZ    1 
ATOM   5846 N  N     . GLU B 1 237 ? -27.363 18.274  -4.582  1 20.531  ? 229  GLU B N     1 
ATOM   5847 C  CA    . GLU B 1 237 ? -25.961 18.338  -4.978  1 21.413  ? 229  GLU B CA    1 
ATOM   5848 C  C     . GLU B 1 237 ? -25.403 19.662  -4.462  1 20.496  ? 229  GLU B C     1 
ATOM   5849 O  O     . GLU B 1 237 ? -25.9   20.727  -4.845  1 21.552  ? 229  GLU B O     1 
ATOM   5850 C  CB    . GLU B 1 237 ? -25.704 18.125  -6.469  1 21.094  ? 229  GLU B CB    1 
ATOM   5851 C  CG    . GLU B 1 237 ? -26.191 16.785  -7.032  1 20.803  ? 229  GLU B CG    1 
ATOM   5852 C  CD    . GLU B 1 237 ? -25.595 16.25   -8.324  1 23.705  ? 229  GLU B CD    1 
ATOM   5853 O  OE1   . GLU B 1 237 ? -24.493 16.7    -8.727  1 21.839  ? 229  GLU B OE1   1 
ATOM   5854 O  OE2   . GLU B 1 237 ? -26.239 15.346  -8.918  1 24.282  ? 229  GLU B OE2   1 
ATOM   5855 N  N     . VAL B 1 238 ? -24.432 19.564  -3.542  1 18.278  ? 230  VAL B N     1 
ATOM   5856 C  CA    . VAL B 1 238 ? -23.724 20.709  -2.976  1 19.5    ? 230  VAL B CA    1 
ATOM   5857 C  C     . VAL B 1 238 ? -22.395 20.861  -3.721  1 20.151  ? 230  VAL B C     1 
ATOM   5858 O  O     . VAL B 1 238 ? -21.575 19.953  -3.687  1 22.62   ? 230  VAL B O     1 
ATOM   5859 C  CB    . VAL B 1 238 ? -23.549 20.628  -1.446  1 19.2    ? 230  VAL B CB    1 
ATOM   5860 C  CG1   . VAL B 1 238 ? -22.725 21.783  -0.881  1 17.425  ? 230  VAL B CG1   1 
ATOM   5861 C  CG2   . VAL B 1 238 ? -24.889 20.535  -0.72   1 19.575  ? 230  VAL B CG2   1 
ATOM   5862 N  N     . ASP B 1 239 ? -22.175 22.036  -4.334  1 20.783  ? 231  ASP B N     1 
ATOM   5863 C  CA    . ASP B 1 239 ? -21.018 22.312  -5.19   1 23.354  ? 231  ASP B CA    1 
ATOM   5864 C  C     . ASP B 1 239 ? -19.732 22.441  -4.35   1 23.395  ? 231  ASP B C     1 
ATOM   5865 O  O     . ASP B 1 239 ? -19.867 22.503  -3.121  1 24.272  ? 231  ASP B O     1 
ATOM   5866 C  CB    . ASP B 1 239 ? -21.319 23.435  -6.173  1 22.737  ? 231  ASP B CB    1 
ATOM   5867 C  CG    . ASP B 1 239 ? -21.17  24.892  -5.734  1 24.876  ? 231  ASP B CG    1 
ATOM   5868 O  OD1   . ASP B 1 239 ? -20.942 25.195  -4.528  1 23.019  ? 231  ASP B OD1   1 
ATOM   5869 O  OD2   . ASP B 1 239 ? -21.336 25.743  -6.631  1 29.175  ? 231  ASP B OD2   1 
ATOM   5870 N  N     . PRO B 1 240 ? -18.483 22.494  -4.927  1 22.623  ? 232  PRO B N     1 
ATOM   5871 C  CA    . PRO B 1 240 ? -17.261 22.738  -4.147  1 24.679  ? 232  PRO B CA    1 
ATOM   5872 C  C     . PRO B 1 240 ? -17.172 24.022  -3.309  1 25.696  ? 232  PRO B C     1 
ATOM   5873 O  O     . PRO B 1 240 ? -16.277 24.104  -2.466  1 24.754  ? 232  PRO B O     1 
ATOM   5874 C  CB    . PRO B 1 240 ? -16.134 22.639  -5.176  1 25.348  ? 232  PRO B CB    1 
ATOM   5875 C  CG    . PRO B 1 240 ? -16.711 21.708  -6.217  1 23.01   ? 232  PRO B CG    1 
ATOM   5876 C  CD    . PRO B 1 240 ? -18.122 22.17   -6.322  1 22.533  ? 232  PRO B CD    1 
ATOM   5877 N  N     . SER B 1 241 ? -18.071 24.999  -3.551  1 24.864  ? 233  SER B N     1 
ATOM   5878 C  CA    . SER B 1 241 ? -18.112 26.269  -2.834  1 27.543  ? 233  SER B CA    1 
ATOM   5879 C  C     . SER B 1 241 ? -19.171 26.271  -1.722  1 27.971  ? 233  SER B C     1 
ATOM   5880 O  O     . SER B 1 241 ? -19.298 27.266  -1.002  1 28.209  ? 233  SER B O     1 
ATOM   5881 C  CB    . SER B 1 241 ? -18.215 27.449  -3.784  1 27.414  ? 233  SER B CB    1 
ATOM   5882 O  OG    . SER B 1 241 ? -19.501 27.478  -4.389  1 38.857  ? 233  SER B OG    1 
ATOM   5883 N  N     . GLY B 1 242 ? -19.897 25.146  -1.57   1 24.112  ? 234  GLY B N     1 
ATOM   5884 C  CA    . GLY B 1 242 ? -20.829 24.928  -0.47   1 24.256  ? 234  GLY B CA    1 
ATOM   5885 C  C     . GLY B 1 242 ? -22.263 25.378  -0.75   1 24.301  ? 234  GLY B C     1 
ATOM   5886 O  O     . GLY B 1 242 ? -23.032 25.507  0.205   1 25.486  ? 234  GLY B O     1 
ATOM   5887 N  N     . LYS B 1 243 ? -22.606 25.562  -2.038  1 24.7    ? 235  LYS B N     1 
ATOM   5888 C  CA    . LYS B 1 243 ? -23.914 25.992  -2.533  1 28.176  ? 235  LYS B CA    1 
ATOM   5889 C  C     . LYS B 1 243 ? -24.677 24.795  -3.117  1 27.613  ? 235  LYS B C     1 
ATOM   5890 O  O     . LYS B 1 243 ? -24.086 23.96   -3.814  1 25.408  ? 235  LYS B O     1 
ATOM   5891 C  CB    . LYS B 1 243 ? -23.567 27.102  -3.535  1 35.349  ? 235  LYS B CB    1 
ATOM   5892 C  CG    . LYS B 1 243 ? -24.665 27.942  -4.179  1 53.396  ? 235  LYS B CG    1 
ATOM   5893 C  CD    . LYS B 1 243 ? -24.193 29.288  -4.731  1 58.395  ? 235  LYS B CD    1 
ATOM   5894 C  CE    . LYS B 1 243 ? -25.043 29.766  -5.883  1 64.115  ? 235  LYS B CE    1 
ATOM   5895 N  NZ    . LYS B 1 243 ? -24.561 30.993  -6.525  1 58.108  ? 235  LYS B NZ    1 
ATOM   5896 N  N     . VAL B 1 244 ? -25.999 24.735  -2.85   1 25.416  ? 236  VAL B N     1 
ATOM   5897 C  CA    . VAL B 1 244 ? -26.907 23.73   -3.412  1 25.721  ? 236  VAL B CA    1 
ATOM   5898 C  C     . VAL B 1 244 ? -27.167 24.131  -4.868  1 27.54   ? 236  VAL B C     1 
ATOM   5899 O  O     . VAL B 1 244 ? -27.768 25.178  -5.11   1 32.026  ? 236  VAL B O     1 
ATOM   5900 C  CB    . VAL B 1 244 ? -28.211 23.502  -2.602  1 25.914  ? 236  VAL B CB    1 
ATOM   5901 C  CG1   . VAL B 1 244 ? -29.188 22.52   -3.256  1 24.633  ? 236  VAL B CG1   1 
ATOM   5902 C  CG2   . VAL B 1 244 ? -27.936 23.059  -1.165  1 26.22   ? 236  VAL B CG2   1 
ATOM   5903 N  N     . VAL B 1 245 ? -26.716 23.288  -5.812  1 27.367  ? 237  VAL B N     1 
ATOM   5904 C  CA    . VAL B 1 245 ? -26.751 23.577  -7.252  1 27.621  ? 237  VAL B CA    1 
ATOM   5905 C  C     . VAL B 1 245 ? -27.834 22.771  -7.968  1 27.166  ? 237  VAL B C     1 
ATOM   5906 O  O     . VAL B 1 245 ? -28.277 23.183  -9.04   1 30.579  ? 237  VAL B O     1 
ATOM   5907 C  CB    . VAL B 1 245 ? -25.42  23.572  -8.038  1 26.349  ? 237  VAL B CB    1 
ATOM   5908 C  CG1   . VAL B 1 245 ? -24.503 24.689  -7.549  1 28.68   ? 237  VAL B CG1   1 
ATOM   5909 C  CG2   . VAL B 1 245 ? -24.702 22.218  -8.027  1 23.023  ? 237  VAL B CG2   1 
ATOM   5910 N  N     . ARG B 1 246 ? -28.182 21.606  -7.404  1 25.765  ? 238  ARG B N     1 
ATOM   5911 C  CA    . ARG B 1 246 ? -29.231 20.727  -7.901  1 24.451  ? 238  ARG B CA    1 
ATOM   5912 C  C     . ARG B 1 246 ? -29.959 20.147  -6.699  1 24.42   ? 238  ARG B C     1 
ATOM   5913 O  O     . ARG B 1 246 ? -29.339 19.836  -5.674  1 22.399  ? 238  ARG B O     1 
ATOM   5914 C  CB    . ARG B 1 246 ? -28.649 19.57   -8.728  1 26.112  ? 238  ARG B CB    1 
ATOM   5915 C  CG    . ARG B 1 246 ? -28.086 19.905  -10.1   1 24.639  ? 238  ARG B CG    1 
ATOM   5916 C  CD    . ARG B 1 246 ? -27.191 18.754  -10.483 1 27.288  ? 238  ARG B CD    1 
ATOM   5917 N  NE    . ARG B 1 246 ? -26.691 18.805  -11.865 1 30.304  ? 238  ARG B NE    1 
ATOM   5918 C  CZ    . ARG B 1 246 ? -25.805 17.977  -12.453 1 32.696  ? 238  ARG B CZ    1 
ATOM   5919 N  NH1   . ARG B 1 246 ? -25.325 16.88   -11.869 1 29.673  ? 238  ARG B NH1   1 
ATOM   5920 N  NH2   . ARG B 1 246 ? -25.391 18.266  -13.672 1 32.03   ? 238  ARG B NH2   1 
ATOM   5921 N  N     . ASP B 1 247 ? -31.279 20.035  -6.844  1 22.733  ? 239  ASP B N     1 
ATOM   5922 C  CA    . ASP B 1 247 ? -32.153 19.443  -5.835  1 24.141  ? 239  ASP B CA    1 
ATOM   5923 C  C     . ASP B 1 247 ? -33.468 18.954  -6.447  1 22.166  ? 239  ASP B C     1 
ATOM   5924 O  O     . ASP B 1 247 ? -33.781 19.302  -7.591  1 19.588  ? 239  ASP B O     1 
ATOM   5925 C  CB    . ASP B 1 247 ? -32.313 20.355  -4.62   1 23.238  ? 239  ASP B CB    1 
ATOM   5926 C  CG    . ASP B 1 247 ? -33.156 21.617  -4.754  1 23.541  ? 239  ASP B CG    1 
ATOM   5927 O  OD1   . ASP B 1 247 ? -33.681 21.909  -5.867  1 22.328  ? 239  ASP B OD1   1 
ATOM   5928 O  OD2   . ASP B 1 247 ? -33.273 22.301  -3.72   1 23.47   ? 239  ASP B OD2   1 
ATOM   5929 N  N     . LEU B 1 248 ? -34.207 18.161  -5.649  1 21.834  ? 240  LEU B N     1 
ATOM   5930 C  CA    . LEU B 1 248 ? -35.542 17.65   -5.945  1 21.851  ? 240  LEU B CA    1 
ATOM   5931 C  C     . LEU B 1 248 ? -36.201 17.134  -4.663  1 21.606  ? 240  LEU B C     1 
ATOM   5932 O  O     . LEU B 1 248 ? -35.548 16.41   -3.898  1 20.676  ? 240  LEU B O     1 
ATOM   5933 C  CB    . LEU B 1 248 ? -35.484 16.55   -7.017  1 21.975  ? 240  LEU B CB    1 
ATOM   5934 C  CG    . LEU B 1 248 ? -36.802 16.126  -7.678  1 23.494  ? 240  LEU B CG    1 
ATOM   5935 C  CD1   . LEU B 1 248 ? -37.393 17.132  -8.662  1 24.492  ? 240  LEU B CD1   1 
ATOM   5936 C  CD2   . LEU B 1 248 ? -36.568 14.776  -8.336  1 26.753  ? 240  LEU B CD2   1 
ATOM   5937 N  N     . TRP B 1 249 ? -37.505 17.46   -4.509  1 20.307  ? 241  TRP B N     1 
ATOM   5938 C  CA    . TRP B 1 249 ? -38.412 16.777  -3.59   1 19.842  ? 241  TRP B CA    1 
ATOM   5939 C  C     . TRP B 1 249 ? -39.131 15.614  -4.277  1 19.896  ? 241  TRP B C     1 
ATOM   5940 O  O     . TRP B 1 249 ? -39.708 15.794  -5.349  1 19.824  ? 241  TRP B O     1 
ATOM   5941 C  CB    . TRP B 1 249 ? -39.365 17.772  -2.926  1 21.513  ? 241  TRP B CB    1 
ATOM   5942 C  CG    . TRP B 1 249 ? -38.652 18.67   -1.943  1 22.788  ? 241  TRP B CG    1 
ATOM   5943 C  CD1   . TRP B 1 249 ? -38.057 19.86   -2.228  1 22.161  ? 241  TRP B CD1   1 
ATOM   5944 C  CD2   . TRP B 1 249 ? -38.436 18.44   -0.531  1 23.13   ? 241  TRP B CD2   1 
ATOM   5945 N  NE1   . TRP B 1 249 ? -37.514 20.408  -1.095  1 23.904  ? 241  TRP B NE1   1 
ATOM   5946 C  CE2   . TRP B 1 249 ? -37.721 19.566  -0.038  1 24.107  ? 241  TRP B CE2   1 
ATOM   5947 C  CE3   . TRP B 1 249 ? -38.777 17.404  0.369   1 25.03   ? 241  TRP B CE3   1 
ATOM   5948 C  CZ2   . TRP B 1 249 ? -37.32  19.682  1.305   1 24.345  ? 241  TRP B CZ2   1 
ATOM   5949 C  CZ3   . TRP B 1 249 ? -38.379 17.516  1.695   1 25.045  ? 241  TRP B CZ3   1 
ATOM   5950 C  CH2   . TRP B 1 249 ? -37.67  18.649  2.159   1 24.391  ? 241  TRP B CH2   1 
ATOM   5951 N  N     . LEU B 1 250 ? -39.044 14.426  -3.651  1 19.33   ? 242  LEU B N     1 
ATOM   5952 C  CA    . LEU B 1 250 ? -39.608 13.159  -4.115  1 20.452  ? 242  LEU B CA    1 
ATOM   5953 C  C     . LEU B 1 250 ? -40.178 12.367  -2.928  1 21.365  ? 242  LEU B C     1 
ATOM   5954 O  O     . LEU B 1 250 ? -40.223 12.883  -1.804  1 21.531  ? 242  LEU B O     1 
ATOM   5955 C  CB    . LEU B 1 250 ? -38.614 12.365  -4.979  1 20.586  ? 242  LEU B CB    1 
ATOM   5956 C  CG    . LEU B 1 250 ? -37.327 11.863  -4.299  1 20.253  ? 242  LEU B CG    1 
ATOM   5957 C  CD1   . LEU B 1 250 ? -37.063 10.389  -4.567  1 20.014  ? 242  LEU B CD1   1 
ATOM   5958 C  CD2   . LEU B 1 250 ? -36.157 12.704  -4.748  1 18.91   ? 242  LEU B CD2   1 
ATOM   5959 N  N     . GLU B 1 251 ? -40.631 11.12   -3.189  1 22.962  ? 243  GLU B N     1 
ATOM   5960 C  CA    . GLU B 1 251 ? -41.069 10.183  -2.155  1 24.037  ? 243  GLU B CA    1 
ATOM   5961 C  C     . GLU B 1 251 ? -40.531 8.78    -2.429  1 24.143  ? 243  GLU B C     1 
ATOM   5962 O  O     . GLU B 1 251 ? -40.323 8.403   -3.591  1 25.746  ? 243  GLU B O     1 
ATOM   5963 C  CB    . GLU B 1 251 ? -42.583 10.033  -2.011  1 24.259  ? 243  GLU B CB    1 
ATOM   5964 C  CG    . GLU B 1 251 ? -43.299 11.288  -1.521  1 29.121  ? 243  GLU B CG    1 
ATOM   5965 C  CD    . GLU B 1 251 ? -44.81  11.253  -1.613  1 32.418  ? 243  GLU B CD    1 
ATOM   5966 O  OE1   . GLU B 1 251 ? -45.38  10.748  -2.6    1 36.7    ? 243  GLU B OE1   1 
ATOM   5967 O  OE2   . GLU B 1 251 ? -45.416 11.784  -0.673  1 36.93   ? 243  GLU B OE2   1 
ATOM   5968 N  N     . ALA B 1 252 ? -40.323 8.035   -1.329  1 20.141  ? 244  ALA B N     1 
ATOM   5969 C  CA    . ALA B 1 252 ? -40.117 6.597   -1.344  1 19.029  ? 244  ALA B CA    1 
ATOM   5970 C  C     . ALA B 1 252 ? -41.466 5.874   -1.474  1 18.31   ? 244  ALA B C     1 
ATOM   5971 O  O     . ALA B 1 252 ? -42.479 6.46    -1.067  1 17.301  ? 244  ALA B O     1 
ATOM   5972 C  CB    . ALA B 1 252 ? -39.341 6.213   -0.105  1 18.526  ? 244  ALA B CB    1 
ATOM   5973 N  N     . PRO B 1 253 ? -41.548 4.636   -2.065  1 19.611  ? 245  PRO B N     1 
ATOM   5974 C  CA    . PRO B 1 253 ? -42.805 3.876   -2.141  1 20.616  ? 245  PRO B CA    1 
ATOM   5975 C  C     . PRO B 1 253 ? -43.455 3.533   -0.793  1 22.838  ? 245  PRO B C     1 
ATOM   5976 O  O     . PRO B 1 253 ? -44.684 3.504   -0.686  1 23.02   ? 245  PRO B O     1 
ATOM   5977 C  CB    . PRO B 1 253 ? -42.455 2.672   -3.022  1 20.775  ? 245  PRO B CB    1 
ATOM   5978 C  CG    . PRO B 1 253 ? -40.954 2.49    -2.793  1 19.567  ? 245  PRO B CG    1 
ATOM   5979 C  CD    . PRO B 1 253 ? -40.463 3.903   -2.765  1 18.583  ? 245  PRO B CD    1 
ATOM   5980 N  N     . TRP B 1 254 ? -42.619 3.27    0.225   1 21.488  ? 246  TRP B N     1 
ATOM   5981 C  CA    . TRP B 1 254 ? -43.013 3.235   1.633   1 21.434  ? 246  TRP B CA    1 
ATOM   5982 C  C     . TRP B 1 254 ? -41.943 3.958   2.464   1 20.794  ? 246  TRP B C     1 
ATOM   5983 O  O     . TRP B 1 254 ? -40.849 4.225   1.933   1 20.684  ? 246  TRP B O     1 
ATOM   5984 C  CB    . TRP B 1 254 ? -43.275 1.781   2.077   1 20.767  ? 246  TRP B CB    1 
ATOM   5985 C  CG    . TRP B 1 254 ? -42.042 0.978   2.399   1 22.211  ? 246  TRP B CG    1 
ATOM   5986 C  CD1   . TRP B 1 254 ? -41.468 0.826   3.631   1 23.528  ? 246  TRP B CD1   1 
ATOM   5987 C  CD2   . TRP B 1 254 ? -41.218 0.236   1.476   1 22.614  ? 246  TRP B CD2   1 
ATOM   5988 N  NE1   . TRP B 1 254 ? -40.352 0.041   3.549   1 22.762  ? 246  TRP B NE1   1 
ATOM   5989 C  CE2   . TRP B 1 254 ? -40.168 -0.338  2.244   1 23.969  ? 246  TRP B CE2   1 
ATOM   5990 C  CE3   . TRP B 1 254 ? -41.262 -0.01   0.087   1 25.074  ? 246  TRP B CE3   1 
ATOM   5991 C  CZ2   . TRP B 1 254 ? -39.169 -1.134  1.661   1 25.798  ? 246  TRP B CZ2   1 
ATOM   5992 C  CZ3   . TRP B 1 254 ? -40.281 -0.805  -0.489  1 26.102  ? 246  TRP B CZ3   1 
ATOM   5993 C  CH2   . TRP B 1 254 ? -39.249 -1.364  0.29    1 27.056  ? 246  TRP B CH2   1 
ATOM   5994 N  N     . CYS B 1 255 ? -42.235 4.24    3.752   1 18.54   ? 247  CYS B N     1 
ATOM   5995 C  CA    . CYS B 1 255 ? -41.228 4.807   4.645   1 17.674  ? 247  CYS B CA    1 
ATOM   5996 C  C     . CYS B 1 255 ? -40.208 3.722   4.984   1 17.181  ? 247  CYS B C     1 
ATOM   5997 O  O     . CYS B 1 255 ? -40.413 2.967   5.935   1 18.27   ? 247  CYS B O     1 
ATOM   5998 C  CB    . CYS B 1 255 ? -41.835 5.586   5.806   1 19.018  ? 247  CYS B CB    1 
ATOM   5999 S  SG    . CYS B 1 255 ? -40.542 6.358   6.81    1 23.215  ? 247  CYS B SG    1 
ATOM   6000 N  N     . ALA B 1 256 ? -39.144 3.671   4.164   1 16.601  ? 248  ALA B N     1 
ATOM   6001 C  CA    . ALA B 1 256 ? -38.096 2.651   4.146   1 17.62   ? 248  ALA B CA    1 
ATOM   6002 C  C     . ALA B 1 256 ? -36.798 3.189   4.752   1 18.583  ? 248  ALA B C     1 
ATOM   6003 O  O     . ALA B 1 256 ? -36.588 4.411   4.79    1 18.856  ? 248  ALA B O     1 
ATOM   6004 C  CB    . ALA B 1 256 ? -37.847 2.239   2.717   1 16.681  ? 248  ALA B CB    1 
ATOM   6005 N  N     . PHE B 1 257 ? -35.934 2.249   5.18    1 19.177  ? 249  PHE B N     1 
ATOM   6006 C  CA    . PHE B 1 257 ? -34.603 2.5     5.721   1 19.475  ? 249  PHE B CA    1 
ATOM   6007 C  C     . PHE B 1 257 ? -33.627 2.619   4.553   1 20.36   ? 249  PHE B C     1 
ATOM   6008 O  O     . PHE B 1 257 ? -33.132 1.602   4.055   1 22.036  ? 249  PHE B O     1 
ATOM   6009 C  CB    . PHE B 1 257 ? -34.348 1.37    6.738   1 18.019  ? 249  PHE B CB    1 
ATOM   6010 C  CG    . PHE B 1 257 ? -33.246 1.493   7.788   1 16.316  ? 249  PHE B CG    1 
ATOM   6011 C  CD1   . PHE B 1 257 ? -32.097 2.296   7.596   1 16.075  ? 249  PHE B CD1   1 
ATOM   6012 C  CD2   . PHE B 1 257 ? -33.359 0.777   8.986   1 16.143  ? 249  PHE B CD2   1 
ATOM   6013 C  CE1   . PHE B 1 257 ? -31.102 2.388   8.579   1 16.264  ? 249  PHE B CE1   1 
ATOM   6014 C  CE2   . PHE B 1 257 ? -32.37  0.861   9.977   1 15.439  ? 249  PHE B CE2   1 
ATOM   6015 C  CZ    . PHE B 1 257 ? -31.247 1.668   9.768   1 15.681  ? 249  PHE B CZ    1 
ATOM   6016 N  N     . ILE B 1 258 ? -33.363 3.874   4.134   1 20.101  ? 250  ILE B N     1 
ATOM   6017 C  CA    . ILE B 1 258 ? -32.496 4.191   3.003   1 20.383  ? 250  ILE B CA    1 
ATOM   6018 C  C     . ILE B 1 258 ? -31.144 4.648   3.56    1 21.077  ? 250  ILE B C     1 
ATOM   6019 O  O     . ILE B 1 258 ? -30.83  5.848   3.601   1 20.817  ? 250  ILE B O     1 
ATOM   6020 C  CB    . ILE B 1 258 ? -33.119 5.174   1.977   1 19.955  ? 250  ILE B CB    1 
ATOM   6021 C  CG1   . ILE B 1 258 ? -34.648 4.976   1.765   1 19.474  ? 250  ILE B CG1   1 
ATOM   6022 C  CG2   . ILE B 1 258 ? -32.324 5.132   0.658   1 19.658  ? 250  ILE B CG2   1 
ATOM   6023 C  CD1   . ILE B 1 258 ? -35.339 6.052   0.932   1 22.181  ? 250  ILE B CD1   1 
ATOM   6024 N  N     . HIS B 1 259 ? -30.345 3.652   3.967   1 19.585  ? 251  HIS B N     1 
ATOM   6025 C  CA    . HIS B 1 259 ? -29.046 3.871   4.591   1 20.315  ? 251  HIS B CA    1 
ATOM   6026 C  C     . HIS B 1 259 ? -27.979 4.403   3.62    1 17.854  ? 251  HIS B C     1 
ATOM   6027 O  O     . HIS B 1 259 ? -27.287 5.379   3.933   1 17.537  ? 251  HIS B O     1 
ATOM   6028 C  CB    . HIS B 1 259 ? -28.652 2.635   5.396   1 20.051  ? 251  HIS B CB    1 
ATOM   6029 C  CG    . HIS B 1 259 ? -27.315 2.781   6.024   1 22.132  ? 251  HIS B CG    1 
ATOM   6030 N  ND1   . HIS B 1 259 ? -27.123 3.699   7.03    1 21.674  ? 251  HIS B ND1   1 
ATOM   6031 C  CD2   . HIS B 1 259 ? -26.113 2.258   5.755   1 22.165  ? 251  HIS B CD2   1 
ATOM   6032 C  CE1   . HIS B 1 259 ? -25.857 3.708   7.381   1 22.677  ? 251  HIS B CE1   1 
ATOM   6033 N  NE2   . HIS B 1 259 ? -25.233 2.826   6.641   1 22.24   ? 251  HIS B NE2   1 
ATOM   6034 N  N     . ASP B 1 260 ? -27.851 3.733   2.471   1 18.314  ? 252  ASP B N     1 
ATOM   6035 C  CA    . ASP B 1 260 ? -26.781 3.939   1.495   1 18.293  ? 252  ASP B CA    1 
ATOM   6036 C  C     . ASP B 1 260 ? -27.365 4.112   0.087   1 18.696  ? 252  ASP B C     1 
ATOM   6037 O  O     . ASP B 1 260 ? -28.578 4.02    -0.116  1 16.835  ? 252  ASP B O     1 
ATOM   6038 C  CB    . ASP B 1 260 ? -25.676 2.906   1.698   1 18.435  ? 252  ASP B CB    1 
ATOM   6039 C  CG    . ASP B 1 260 ? -24.28  3.208   1.167   1 17.793  ? 252  ASP B CG    1 
ATOM   6040 O  OD1   . ASP B 1 260 ? -24.054 4.289   0.594   1 17.46   ? 252  ASP B OD1   1 
ATOM   6041 O  OD2   . ASP B 1 260 ? -23.407 2.336   1.315   1 20.393  ? 252  ASP B OD2   1 
ATOM   6042 N  N     . CYS B 1 261 ? -26.469 4.434   -0.862  1 18.775  ? 253  CYS B N     1 
ATOM   6043 C  CA    . CYS B 1 261 ? -26.769 4.856   -2.22   1 18.323  ? 253  CYS B CA    1 
ATOM   6044 C  C     . CYS B 1 261 ? -25.577 4.568   -3.132  1 19.452  ? 253  CYS B C     1 
ATOM   6045 O  O     . CYS B 1 261 ? -24.507 4.171   -2.651  1 18.88   ? 253  CYS B O     1 
ATOM   6046 C  CB    . CYS B 1 261 ? -27.228 6.309   -2.245  1 18.896  ? 253  CYS B CB    1 
ATOM   6047 S  SG    . CYS B 1 261 ? -25.936 7.51    -1.836  1 18.809  ? 253  CYS B SG    1 
ATOM   6048 N  N     . ALA B 1 262 ? -25.774 4.786   -4.445  1 19.226  ? 254  ALA B N     1 
ATOM   6049 C  CA    . ALA B 1 262 ? -24.686 4.762   -5.412  1 20.329  ? 254  ALA B CA    1 
ATOM   6050 C  C     . ALA B 1 262 ? -24.786 5.957   -6.349  1 20.103  ? 254  ALA B C     1 
ATOM   6051 O  O     . ALA B 1 262 ? -25.886 6.325   -6.789  1 19.519  ? 254  ALA B O     1 
ATOM   6052 C  CB    . ALA B 1 262 ? -24.614 3.435   -6.15   1 20.114  ? 254  ALA B CB    1 
ATOM   6053 N  N     . LEU B 1 263 ? -23.606 6.526   -6.618  1 18.105  ? 255  LEU B N     1 
ATOM   6054 C  CA    . LEU B 1 263 ? -23.414 7.604   -7.57   1 18.983  ? 255  LEU B CA    1 
ATOM   6055 C  C     . LEU B 1 263 ? -22.782 7.048   -8.849  1 20.781  ? 255  LEU B C     1 
ATOM   6056 O  O     . LEU B 1 263 ? -21.767 6.347   -8.81   1 20.406  ? 255  LEU B O     1 
ATOM   6057 C  CB    . LEU B 1 263 ? -22.604 8.738   -6.935  1 17.904  ? 255  LEU B CB    1 
ATOM   6058 C  CG    . LEU B 1 263 ? -22.338 9.977   -7.798  1 19.783  ? 255  LEU B CG    1 
ATOM   6059 C  CD1   . LEU B 1 263 ? -23.568 10.871  -7.934  1 19.321  ? 255  LEU B CD1   1 
ATOM   6060 C  CD2   . LEU B 1 263 ? -21.142 10.734  -7.229  1 19.793  ? 255  LEU B CD2   1 
ATOM   6061 N  N     . THR B 1 264 ? -23.419 7.41    -9.978  1 20.734  ? 256  THR B N     1 
ATOM   6062 C  CA    . THR B 1 264 ? -22.992 7.098   -11.337 1 20.741  ? 256  THR B CA    1 
ATOM   6063 C  C     . THR B 1 264 ? -22.897 8.428   -12.104 1 21.25   ? 256  THR B C     1 
ATOM   6064 O  O     . THR B 1 264 ? -23.329 9.437   -11.528 1 21.726  ? 256  THR B O     1 
ATOM   6065 C  CB    . THR B 1 264 ? -23.915 6.048   -11.988 1 20.998  ? 256  THR B CB    1 
ATOM   6066 O  OG1   . THR B 1 264 ? -25.083 6.74    -12.416 1 21.409  ? 256  THR B OG1   1 
ATOM   6067 C  CG2   . THR B 1 264 ? -24.26  4.838   -11.128 1 21.138  ? 256  THR B CG2   1 
ATOM   6068 N  N     . PRO B 1 265 ? -22.383 8.528   -13.379 1 20.708  ? 257  PRO B N     1 
ATOM   6069 C  CA    . PRO B 1 265 ? -22.417 9.794   -14.12  1 22.199  ? 257  PRO B CA    1 
ATOM   6070 C  C     . PRO B 1 265 ? -23.768 10.517  -14.172 1 22.319  ? 257  PRO B C     1 
ATOM   6071 O  O     . PRO B 1 265 ? -23.785 11.734  -13.985 1 23.179  ? 257  PRO B O     1 
ATOM   6072 C  CB    . PRO B 1 265 ? -21.764 9.495   -15.477 1 22.123  ? 257  PRO B CB    1 
ATOM   6073 C  CG    . PRO B 1 265 ? -20.843 8.345   -15.115 1 21.232  ? 257  PRO B CG    1 
ATOM   6074 C  CD    . PRO B 1 265 ? -21.673 7.508   -14.179 1 20.129  ? 257  PRO B CD    1 
ATOM   6075 N  N     . ASN B 1 266 ? -24.869 9.757   -14.331 1 21.591  ? 258  ASN B N     1 
ATOM   6076 C  CA    . ASN B 1 266 ? -26.185 10.3    -14.678 1 21.463  ? 258  ASN B CA    1 
ATOM   6077 C  C     . ASN B 1 266 ? -27.252 10.129  -13.593 1 21.177  ? 258  ASN B C     1 
ATOM   6078 O  O     . ASN B 1 266 ? -28.344 10.687  -13.74  1 22.612  ? 258  ASN B O     1 
ATOM   6079 C  CB    . ASN B 1 266 ? -26.613 9.873   -16.081 1 20.688  ? 258  ASN B CB    1 
ATOM   6080 C  CG    . ASN B 1 266 ? -25.583 10.266  -17.114 1 20.749  ? 258  ASN B CG    1 
ATOM   6081 O  OD1   . ASN B 1 266 ? -25.267 11.452  -17.3   1 19.502  ? 258  ASN B OD1   1 
ATOM   6082 N  ND2   . ASN B 1 266 ? -25.006 9.26    -17.747 1 20.762  ? 258  ASN B ND2   1 
ATOM   6083 N  N     . TYR B 1 267 ? -26.933 9.392   -12.509 1 21.193  ? 259  TYR B N     1 
ATOM   6084 C  CA    . TYR B 1 267 ? -27.9   8.982   -11.49  1 21.223  ? 259  TYR B CA    1 
ATOM   6085 C  C     . TYR B 1 267 ? -27.33  9.061   -10.072 1 21.141  ? 259  TYR B C     1 
ATOM   6086 O  O     . TYR B 1 267 ? -26.144 8.799   -9.862  1 21.106  ? 259  TYR B O     1 
ATOM   6087 C  CB    . TYR B 1 267 ? -28.368 7.545   -11.729 1 22.111  ? 259  TYR B CB    1 
ATOM   6088 C  CG    . TYR B 1 267 ? -29.208 7.346   -12.977 1 24.017  ? 259  TYR B CG    1 
ATOM   6089 C  CD1   . TYR B 1 267 ? -30.601 7.529   -12.923 1 24.886  ? 259  TYR B CD1   1 
ATOM   6090 C  CD2   . TYR B 1 267 ? -28.618 6.964   -14.195 1 22.185  ? 259  TYR B CD2   1 
ATOM   6091 C  CE1   . TYR B 1 267 ? -31.393 7.326   -14.052 1 25.641  ? 259  TYR B CE1   1 
ATOM   6092 C  CE2   . TYR B 1 267 ? -29.405 6.773   -15.329 1 24.151  ? 259  TYR B CE2   1 
ATOM   6093 C  CZ    . TYR B 1 267 ? -30.787 6.955   -15.25  1 26.28   ? 259  TYR B CZ    1 
ATOM   6094 O  OH    . TYR B 1 267 ? -31.593 6.775   -16.329 1 29.657  ? 259  TYR B OH    1 
ATOM   6095 N  N     . LEU B 1 268 ? -28.219 9.403   -9.124  1 21.629  ? 260  LEU B N     1 
ATOM   6096 C  CA    . LEU B 1 268 ? -28.157 8.961   -7.735  1 21.806  ? 260  LEU B CA    1 
ATOM   6097 C  C     . LEU B 1 268 ? -29.147 7.812   -7.544  1 22.556  ? 260  LEU B C     1 
ATOM   6098 O  O     . LEU B 1 268 ? -30.34  7.967   -7.834  1 22.836  ? 260  LEU B O     1 
ATOM   6099 C  CB    . LEU B 1 268 ? -28.352 10.1    -6.725  1 21.279  ? 260  LEU B CB    1 
ATOM   6100 C  CG    . LEU B 1 268 ? -28.106 9.764   -5.25   1 20.955  ? 260  LEU B CG    1 
ATOM   6101 C  CD1   . LEU B 1 268 ? -26.633 9.489   -4.947  1 22.866  ? 260  LEU B CD1   1 
ATOM   6102 C  CD2   . LEU B 1 268 ? -28.643 10.855  -4.36   1 20.86   ? 260  LEU B CD2   1 
ATOM   6103 N  N     . VAL B 1 269 ? -28.633 6.67    -7.062  1 21.119  ? 261  VAL B N     1 
ATOM   6104 C  CA    . VAL B 1 269 ? -29.413 5.438   -6.924  1 21.536  ? 261  VAL B CA    1 
ATOM   6105 C  C     . VAL B 1 269 ? -29.52  5.113   -5.429  1 22.898  ? 261  VAL B C     1 
ATOM   6106 O  O     . VAL B 1 269 ? -28.528 4.692   -4.836  1 23.068  ? 261  VAL B O     1 
ATOM   6107 C  CB    . VAL B 1 269 ? -28.964 4.201   -7.742  1 19.706  ? 261  VAL B CB    1 
ATOM   6108 C  CG1   . VAL B 1 269 ? -29.978 3.06    -7.708  1 20.762  ? 261  VAL B CG1   1 
ATOM   6109 C  CG2   . VAL B 1 269 ? -28.562 4.531   -9.173  1 19.686  ? 261  VAL B CG2   1 
ATOM   6110 N  N     . LEU B 1 270 ? -30.741 5.256   -4.878  1 21.773  ? 262  LEU B N     1 
ATOM   6111 C  CA    . LEU B 1 270 ? -31.071 4.988   -3.476  1 22.242  ? 262  LEU B CA    1 
ATOM   6112 C  C     . LEU B 1 270 ? -31.365 3.5     -3.263  1 21.963  ? 262  LEU B C     1 
ATOM   6113 O  O     . LEU B 1 270 ? -32.037 2.892   -4.1    1 21.024  ? 262  LEU B O     1 
ATOM   6114 C  CB    . LEU B 1 270 ? -32.242 5.856   -3.009  1 21.695  ? 262  LEU B CB    1 
ATOM   6115 C  CG    . LEU B 1 270 ? -32.179 7.38    -3.212  1 23.158  ? 262  LEU B CG    1 
ATOM   6116 C  CD1   . LEU B 1 270 ? -33.338 8.033   -2.482  1 22.007  ? 262  LEU B CD1   1 
ATOM   6117 C  CD2   . LEU B 1 270 ? -30.859 8.059   -2.868  1 20.604  ? 262  LEU B CD2   1 
ATOM   6118 N  N     . MET B 1 271 ? -30.872 2.953   -2.133  1 19.642  ? 263  MET B N     1 
ATOM   6119 C  CA    . MET B 1 271 ? -30.94  1.541   -1.779  1 19.581  ? 263  MET B CA    1 
ATOM   6120 C  C     . MET B 1 271 ? -31.827 1.353   -0.542  1 20.877  ? 263  MET B C     1 
ATOM   6121 O  O     . MET B 1 271 ? -31.443 1.733   0.565   1 23.15   ? 263  MET B O     1 
ATOM   6122 C  CB    . MET B 1 271 ? -29.516 0.995   -1.612  1 20.641  ? 263  MET B CB    1 
ATOM   6123 C  CG    . MET B 1 271 ? -29.402 -0.509  -1.383  1 19.759  ? 263  MET B CG    1 
ATOM   6124 S  SD    . MET B 1 271 ? -27.707 -1.138  -1.416  1 21.245  ? 263  MET B SD    1 
ATOM   6125 C  CE    . MET B 1 271 ? -26.9   -0.272  -0.055  1 18.103  ? 263  MET B CE    1 
ATOM   6126 N  N     . LEU B 1 272 ? -33.005 0.747   -0.754  1 19.561  ? 264  LEU B N     1 
ATOM   6127 C  CA    . LEU B 1 272 ? -34.046 0.579   0.258   1 19.554  ? 264  LEU B CA    1 
ATOM   6128 C  C     . LEU B 1 272 ? -33.928 -0.792  0.93    1 20.06   ? 264  LEU B C     1 
ATOM   6129 O  O     . LEU B 1 272 ? -34.058 -1.843  0.276   1 21.398  ? 264  LEU B O     1 
ATOM   6130 C  CB    . LEU B 1 272 ? -35.449 0.835   -0.303  1 18.053  ? 264  LEU B CB    1 
ATOM   6131 C  CG    . LEU B 1 272 ? -35.878 2.278   -0.568  1 19.013  ? 264  LEU B CG    1 
ATOM   6132 C  CD1   . LEU B 1 272 ? -35.091 3.087   -1.581  1 17.531  ? 264  LEU B CD1   1 
ATOM   6133 C  CD2   . LEU B 1 272 ? -37.323 2.199   -1.04   1 21.056  ? 264  LEU B CD2   1 
ATOM   6134 N  N     . TRP B 1 273 ? -33.664 -0.752  2.246   1 18.828  ? 265  TRP B N     1 
ATOM   6135 C  CA    . TRP B 1 273 ? -33.702 -1.931  3.099   1 19.436  ? 265  TRP B CA    1 
ATOM   6136 C  C     . TRP B 1 273 ? -35.156 -2.322  3.384   1 20.27   ? 265  TRP B C     1 
ATOM   6137 O  O     . TRP B 1 273 ? -35.988 -1.413  3.533   1 19.165  ? 265  TRP B O     1 
ATOM   6138 C  CB    . TRP B 1 273 ? -32.911 -1.738  4.398   1 17.744  ? 265  TRP B CB    1 
ATOM   6139 C  CG    . TRP B 1 273 ? -31.418 -1.525  4.279   1 19.29   ? 265  TRP B CG    1 
ATOM   6140 C  CD1   . TRP B 1 273 ? -30.596 -1.619  3.187   1 19.879  ? 265  TRP B CD1   1 
ATOM   6141 C  CD2   . TRP B 1 273 ? -30.547 -1.199  5.39    1 18.769  ? 265  TRP B CD2   1 
ATOM   6142 N  NE1   . TRP B 1 273 ? -29.298 -1.322  3.522   1 19.503  ? 265  TRP B NE1   1 
ATOM   6143 C  CE2   . TRP B 1 273 ? -29.228 -1.086  4.871   1 19.541  ? 265  TRP B CE2   1 
ATOM   6144 C  CE3   . TRP B 1 273 ? -30.75  -0.982  6.771   1 19.002  ? 265  TRP B CE3   1 
ATOM   6145 C  CZ2   . TRP B 1 273 ? -28.123 -0.784  5.685   1 17.382  ? 265  TRP B CZ2   1 
ATOM   6146 C  CZ3   . TRP B 1 273 ? -29.654 -0.692  7.578   1 18.354  ? 265  TRP B CZ3   1 
ATOM   6147 C  CH2   . TRP B 1 273 ? -28.354 -0.596  7.037   1 17.507  ? 265  TRP B CH2   1 
ATOM   6148 N  N     . PRO B 1 274 ? -35.494 -3.64   3.548   1 21.177  ? 266  PRO B N     1 
ATOM   6149 C  CA    . PRO B 1 274 ? -36.85  -4.074  3.874   1 21.061  ? 266  PRO B CA    1 
ATOM   6150 C  C     . PRO B 1 274 ? -37.242 -3.887  5.35    1 22.11   ? 266  PRO B C     1 
ATOM   6151 O  O     . PRO B 1 274 ? -37.554 -4.865  6.043   1 24.565  ? 266  PRO B O     1 
ATOM   6152 C  CB    . PRO B 1 274 ? -36.857 -5.488  3.289   1 21.584  ? 266  PRO B CB    1 
ATOM   6153 C  CG    . PRO B 1 274 ? -35.495 -5.985  3.728   1 20.705  ? 266  PRO B CG    1 
ATOM   6154 C  CD    . PRO B 1 274 ? -34.591 -4.812  3.49    1 21.239  ? 266  PRO B CD    1 
ATOM   6155 N  N     . PHE B 1 275 ? -37.192 -2.626  5.81    1 20.134  ? 267  PHE B N     1 
ATOM   6156 C  CA    . PHE B 1 275 ? -37.739 -2.148  7.072   1 19.485  ? 267  PHE B CA    1 
ATOM   6157 C  C     . PHE B 1 275 ? -38.752 -1.046  6.758   1 21.617  ? 267  PHE B C     1 
ATOM   6158 O  O     . PHE B 1 275 ? -38.547 -0.257  5.826   1 22.144  ? 267  PHE B O     1 
ATOM   6159 C  CB    . PHE B 1 275 ? -36.713 -1.627  8.091   1 18.515  ? 267  PHE B CB    1 
ATOM   6160 C  CG    . PHE B 1 275 ? -35.551 -2.538  8.483   1 18.125  ? 267  PHE B CG    1 
ATOM   6161 C  CD1   . PHE B 1 275 ? -34.439 -2.689  7.633   1 17.133  ? 267  PHE B CD1   1 
ATOM   6162 C  CD2   . PHE B 1 275 ? -35.555 -3.233  9.706   1 16.612  ? 267  PHE B CD2   1 
ATOM   6163 C  CE1   . PHE B 1 275 ? -33.375 -3.534  7.966   1 17.062  ? 267  PHE B CE1   1 
ATOM   6164 C  CE2   . PHE B 1 275 ? -34.492 -4.099  10.039  1 15.825  ? 267  PHE B CE2   1 
ATOM   6165 C  CZ    . PHE B 1 275 ? -33.403 -4.231  9.179   1 17.24   ? 267  PHE B CZ    1 
ATOM   6166 N  N     . GLU B 1 276 ? -39.823 -1.009  7.567   1 22.326  ? 268  GLU B N     1 
ATOM   6167 C  CA    . GLU B 1 276 ? -40.882 -0.009  7.501   1 23.707  ? 268  GLU B CA    1 
ATOM   6168 C  C     . GLU B 1 276 ? -41.005 0.685   8.857   1 22.11   ? 268  GLU B C     1 
ATOM   6169 O  O     . GLU B 1 276 ? -40.948 0.016   9.896   1 21.487  ? 268  GLU B O     1 
ATOM   6170 C  CB    . GLU B 1 276 ? -42.181 -0.678  7.034   1 25.624  ? 268  GLU B CB    1 
ATOM   6171 C  CG    . GLU B 1 276 ? -43.327 0.294   6.72    1 30.909  ? 268  GLU B CG    1 
ATOM   6172 C  CD    . GLU B 1 276 ? -44.501 -0.087  5.814   1 32.808  ? 268  GLU B CD    1 
ATOM   6173 O  OE1   . GLU B 1 276 ? -44.815 -1.282  5.634   1 35.267  ? 268  GLU B OE1   1 
ATOM   6174 O  OE2   . GLU B 1 276 ? -45.106 0.846   5.237   1 32.943  ? 268  GLU B OE2   1 
ATOM   6175 N  N     . ALA B 1 277 ? -41.186 2.017   8.806   1 20.707  ? 269  ALA B N     1 
ATOM   6176 C  CA    . ALA B 1 277 ? -41.5   2.835   9.97    1 22.596  ? 269  ALA B CA    1 
ATOM   6177 C  C     . ALA B 1 277 ? -43.015 2.942   10.161  1 24.108  ? 269  ALA B C     1 
ATOM   6178 O  O     . ALA B 1 277 ? -43.745 2.986   9.177   1 24.631  ? 269  ALA B O     1 
ATOM   6179 C  CB    . ALA B 1 277 ? -40.82  4.195   9.906   1 20.372  ? 269  ALA B CB    1 
ATOM   6180 N  N     . ASN B 1 278 ? -43.451 2.972   11.434  1 22.842  ? 270  ASN B N     1 
ATOM   6181 C  CA    . ASN B 1 278 ? -44.856 3.011   11.83   1 22.876  ? 270  ASN B CA    1 
ATOM   6182 C  C     . ASN B 1 278 ? -45.003 3.951   13.022  1 21.015  ? 270  ASN B C     1 
ATOM   6183 O  O     . ASN B 1 278 ? -44.507 3.643   14.1    1 21.258  ? 270  ASN B O     1 
ATOM   6184 C  CB    . ASN B 1 278 ? -45.399 1.602   12.07   1 26.52   ? 270  ASN B CB    1 
ATOM   6185 C  CG    . ASN B 1 278 ? -46.892 1.609   12.319  1 29.656  ? 270  ASN B CG    1 
ATOM   6186 O  OD1   . ASN B 1 278 ? -47.361 1.824   13.447  1 26.778  ? 270  ASN B OD1   1 
ATOM   6187 N  ND2   . ASN B 1 278 ? -47.654 1.381   11.261  1 31.67   ? 270  ASN B ND2   1 
ATOM   6188 N  N     . LEU B 1 279 ? -45.699 5.08    12.81   1 22.013  ? 271  LEU B N     1 
ATOM   6189 C  CA    . LEU B 1 279 ? -45.92  6.131   13.801  1 23.686  ? 271  LEU B CA    1 
ATOM   6190 C  C     . LEU B 1 279 ? -46.684 5.608   15.027  1 24.502  ? 271  LEU B C     1 
ATOM   6191 O  O     . LEU B 1 279 ? -46.314 5.957   16.157  1 22.762  ? 271  LEU B O     1 
ATOM   6192 C  CB    . LEU B 1 279 ? -46.537 7.401   13.206  1 22.629  ? 271  LEU B CB    1 
ATOM   6193 C  CG    . LEU B 1 279 ? -46.495 8.682   14.058  1 23.101  ? 271  LEU B CG    1 
ATOM   6194 C  CD1   . LEU B 1 279 ? -45.122 9.347   14.313  1 22.051  ? 271  LEU B CD1   1 
ATOM   6195 C  CD2   . LEU B 1 279 ? -47.437 9.717   13.439  1 22.688  ? 271  LEU B CD2   1 
ATOM   6196 N  N     . GLU B 1 280 ? -47.705 4.765   14.79   1 24.487  ? 272  GLU B N     1 
ATOM   6197 C  CA    . GLU B 1 280 ? -48.544 4.151   15.814  1 26.303  ? 272  GLU B CA    1 
ATOM   6198 C  C     . GLU B 1 280 ? -47.721 3.278   16.763  1 23.814  ? 272  GLU B C     1 
ATOM   6199 O  O     . GLU B 1 280 ? -47.863 3.44    17.978  1 23.083  ? 272  GLU B O     1 
ATOM   6200 C  CB    . GLU B 1 280 ? -49.783 3.44    15.26   1 32.014  ? 272  GLU B CB    1 
ATOM   6201 C  CG    . GLU B 1 280 ? -50.913 4.38    14.842  1 43.973  ? 272  GLU B CG    1 
ATOM   6202 C  CD    . GLU B 1 280 ? -51.703 5.094   15.937  1 55.516  ? 272  GLU B CD    1 
ATOM   6203 O  OE1   . GLU B 1 280 ? -52.468 4.41    16.657  1 61.755  ? 272  GLU B OE1   1 
ATOM   6204 O  OE2   . GLU B 1 280 ? -51.542 6.332   16.088  1 59.899  ? 272  GLU B OE2   1 
ATOM   6205 N  N     . ARG B 1 281 ? -46.855 2.409   16.201  1 22.017  ? 273  ARG B N     1 
ATOM   6206 C  CA    . ARG B 1 281 ? -45.91  1.564   16.937  1 23.303  ? 273  ARG B CA    1 
ATOM   6207 C  C     . ARG B 1 281 ? -44.985 2.415   17.814  1 21.435  ? 273  ARG B C     1 
ATOM   6208 O  O     . ARG B 1 281 ? -44.766 2.069   18.98   1 22.872  ? 273  ARG B O     1 
ATOM   6209 C  CB    . ARG B 1 281 ? -45.115 0.604   16.029  1 24.477  ? 273  ARG B CB    1 
ATOM   6210 C  CG    . ARG B 1 281 ? -44.138 -0.369  16.691  1 23.44   ? 273  ARG B CG    1 
ATOM   6211 C  CD    . ARG B 1 281 ? -43.356 -1.296  15.781  1 22.417  ? 273  ARG B CD    1 
ATOM   6212 N  NE    . ARG B 1 281 ? -42.582 -0.615  14.728  1 23.668  ? 273  ARG B NE    1 
ATOM   6213 C  CZ    . ARG B 1 281 ? -42.744 -0.664  13.404  1 23.376  ? 273  ARG B CZ    1 
ATOM   6214 N  NH1   . ARG B 1 281 ? -43.614 -1.485  12.857  1 23.999  ? 273  ARG B NH1   1 
ATOM   6215 N  NH2   . ARG B 1 281 ? -42.026 0.11    12.609  1 23.162  ? 273  ARG B NH2   1 
ATOM   6216 N  N     . MET B 1 282 ? -44.48  3.517   17.238  1 21.947  ? 274  MET B N     1 
ATOM   6217 C  CA    . MET B 1 282 ? -43.584 4.461   17.904  1 22.124  ? 274  MET B CA    1 
ATOM   6218 C  C     . MET B 1 282 ? -44.256 5.087   19.125  1 21.681  ? 274  MET B C     1 
ATOM   6219 O  O     . MET B 1 282 ? -43.662 5.066   20.197  1 23.85   ? 274  MET B O     1 
ATOM   6220 C  CB    . MET B 1 282 ? -43.003 5.492   16.93   1 21.8    ? 274  MET B CB    1 
ATOM   6221 C  CG    . MET B 1 282 ? -41.868 4.907   16.092  1 23.621  ? 274  MET B CG    1 
ATOM   6222 S  SD    . MET B 1 282 ? -41.043 6.102   15.031  1 25.422  ? 274  MET B SD    1 
ATOM   6223 C  CE    . MET B 1 282 ? -41.731 5.932   13.376  1 22.609  ? 274  MET B CE    1 
ATOM   6224 N  N     . LYS B 1 283 ? -45.498 5.575   18.949  1 21.074  ? 275  LYS B N     1 
ATOM   6225 C  CA    . LYS B 1 283 ? -46.354 6.156   19.98   1 21.658  ? 275  LYS B CA    1 
ATOM   6226 C  C     . LYS B 1 283 ? -46.613 5.166   21.119  1 21.78   ? 275  LYS B C     1 
ATOM   6227 O  O     . LYS B 1 283 ? -46.612 5.598   22.266  1 23.882  ? 275  LYS B O     1 
ATOM   6228 C  CB    . LYS B 1 283 ? -47.647 6.749   19.407  1 21.154  ? 275  LYS B CB    1 
ATOM   6229 C  CG    . LYS B 1 283 ? -47.465 8.074   18.691  1 22.315  ? 275  LYS B CG    1 
ATOM   6230 C  CD    . LYS B 1 283 ? -48.785 8.538   18.09   1 23.756  ? 275  LYS B CD    1 
ATOM   6231 C  CE    . LYS B 1 283 ? -48.581 9.869   17.442  1 24.724  ? 275  LYS B CE    1 
ATOM   6232 N  NZ    . LYS B 1 283 ? -49.751 10.31   16.67   1 24.977  ? 275  LYS B NZ    1 
ATOM   6233 N  N     . ALA B 1 284 ? -46.731 3.861   20.8    1 21.48   ? 276  ALA B N     1 
ATOM   6234 C  CA    . ALA B 1 284 ? -46.893 2.762   21.75   1 23.733  ? 276  ALA B CA    1 
ATOM   6235 C  C     . ALA B 1 284 ? -45.582 2.379   22.454  1 26.734  ? 276  ALA B C     1 
ATOM   6236 O  O     . ALA B 1 284 ? -45.603 1.535   23.352  1 31.139  ? 276  ALA B O     1 
ATOM   6237 C  CB    . ALA B 1 284 ? -47.55  1.577   21.054  1 23.312  ? 276  ALA B CB    1 
ATOM   6238 N  N     . GLY B 1 285 ? -44.456 3.019   22.087  1 26.622  ? 277  GLY B N     1 
ATOM   6239 C  CA    . GLY B 1 285 ? -43.155 2.803   22.702  1 23.607  ? 277  GLY B CA    1 
ATOM   6240 C  C     . GLY B 1 285 ? -42.382 1.636   22.094  1 24.189  ? 277  GLY B C     1 
ATOM   6241 O  O     . GLY B 1 285 ? -41.485 1.118   22.754  1 25.544  ? 277  GLY B O     1 
ATOM   6242 N  N     . GLY B 1 286 ? -42.75  1.231   20.872  1 21.422  ? 278  GLY B N     1 
ATOM   6243 C  CA    . GLY B 1 286 ? -42.032 0.248   20.076  1 23.187  ? 278  GLY B CA    1 
ATOM   6244 C  C     . GLY B 1 286 ? -40.92  0.888   19.244  1 23.365  ? 278  GLY B C     1 
ATOM   6245 O  O     . GLY B 1 286 ? -40.771 2.112   19.252  1 24.237  ? 278  GLY B O     1 
ATOM   6246 N  N     . HIS B 1 287 ? -40.156 0.035   18.533  1 23.682  ? 279  HIS B N     1 
ATOM   6247 C  CA    . HIS B 1 287 ? -39.038 0.431   17.681  1 21.319  ? 279  HIS B CA    1 
ATOM   6248 C  C     . HIS B 1 287 ? -39.521 1.221   16.466  1 21.837  ? 279  HIS B C     1 
ATOM   6249 O  O     . HIS B 1 287 ? -40.632 0.969   15.976  1 22.161  ? 279  HIS B O     1 
ATOM   6250 C  CB    . HIS B 1 287 ? -38.214 -0.782  17.258  1 20.828  ? 279  HIS B CB    1 
ATOM   6251 C  CG    . HIS B 1 287 ? -37.17  -1.193  18.245  1 22.365  ? 279  HIS B CG    1 
ATOM   6252 N  ND1   . HIS B 1 287 ? -36.172 -0.373  18.746  1 22.089  ? 279  HIS B ND1   1 
ATOM   6253 C  CD2   . HIS B 1 287 ? -36.983 -2.392  18.797  1 21.733  ? 279  HIS B CD2   1 
ATOM   6254 C  CE1   . HIS B 1 287 ? -35.427 -1.063  19.591  1 22.144  ? 279  HIS B CE1   1 
ATOM   6255 N  NE2   . HIS B 1 287 ? -35.896 -2.294  19.632  1 22.829  ? 279  HIS B NE2   1 
ATOM   6256 N  N     . HIS B 1 288 ? -38.672 2.168   16.015  1 20.179  ? 280  HIS B N     1 
ATOM   6257 C  CA    . HIS B 1 288 ? -38.857 2.95    14.795  1 19.443  ? 280  HIS B CA    1 
ATOM   6258 C  C     . HIS B 1 288 ? -39.104 2.026   13.599  1 19.843  ? 280  HIS B C     1 
ATOM   6259 O  O     . HIS B 1 288 ? -40.131 2.177   12.935  1 20.679  ? 280  HIS B O     1 
ATOM   6260 C  CB    . HIS B 1 288 ? -37.707 3.944   14.576  1 17.775  ? 280  HIS B CB    1 
ATOM   6261 C  CG    . HIS B 1 288 ? -37.936 4.892   13.439  1 17.393  ? 280  HIS B CG    1 
ATOM   6262 N  ND1   . HIS B 1 288 ? -38.134 6.235   13.655  1 16.335  ? 280  HIS B ND1   1 
ATOM   6263 C  CD2   . HIS B 1 288 ? -37.978 4.728   12.099  1 17.272  ? 280  HIS B CD2   1 
ATOM   6264 C  CE1   . HIS B 1 288 ? -38.27  6.862   12.493  1 17.454  ? 280  HIS B CE1   1 
ATOM   6265 N  NE2   . HIS B 1 288 ? -38.171 5.97    11.53   1 16.794  ? 280  HIS B NE2   1 
ATOM   6266 N  N     . TRP B 1 289 ? -38.189 1.066   13.389  1 18.657  ? 281  TRP B N     1 
ATOM   6267 C  CA    . TRP B 1 289 ? -38.153 0.136   12.267  1 17.741  ? 281  TRP B CA    1 
ATOM   6268 C  C     . TRP B 1 289 ? -38.623 -1.25   12.699  1 19.392  ? 281  TRP B C     1 
ATOM   6269 O  O     . TRP B 1 289 ? -38.323 -1.699  13.817  1 19.019  ? 281  TRP B O     1 
ATOM   6270 C  CB    . TRP B 1 289 ? -36.727 0.024   11.705  1 16.076  ? 281  TRP B CB    1 
ATOM   6271 C  CG    . TRP B 1 289 ? -36.162 1.313   11.183  1 17.985  ? 281  TRP B CG    1 
ATOM   6272 C  CD1   . TRP B 1 289 ? -35.135 2.029   11.738  1 17.854  ? 281  TRP B CD1   1 
ATOM   6273 C  CD2   . TRP B 1 289 ? -36.621 2.073   10.04   1 18.043  ? 281  TRP B CD2   1 
ATOM   6274 N  NE1   . TRP B 1 289 ? -34.883 3.152   10.993  1 18.157  ? 281  TRP B NE1   1 
ATOM   6275 C  CE2   . TRP B 1 289 ? -35.785 3.223   9.96    1 17.545  ? 281  TRP B CE2   1 
ATOM   6276 C  CE3   . TRP B 1 289 ? -37.655 1.907   9.084   1 19.577  ? 281  TRP B CE3   1 
ATOM   6277 C  CZ2   . TRP B 1 289 ? -35.951 4.202   8.968   1 17.883  ? 281  TRP B CZ2   1 
ATOM   6278 C  CZ3   . TRP B 1 289 ? -37.831 2.881   8.108   1 18.304  ? 281  TRP B CZ3   1 
ATOM   6279 C  CH2   . TRP B 1 289 ? -36.996 4.025   8.071   1 18.68   ? 281  TRP B CH2   1 
ATOM   6280 N  N     . ALA B 1 290 ? -39.328 -1.916  11.771  1 18.698  ? 282  ALA B N     1 
ATOM   6281 C  CA    . ALA B 1 290 ? -39.537 -3.356  11.8    1 19.157  ? 282  ALA B CA    1 
ATOM   6282 C  C     . ALA B 1 290 ? -39.189 -3.943  10.435  1 18.646  ? 282  ALA B C     1 
ATOM   6283 O  O     . ALA B 1 290 ? -39.618 -3.411  9.417   1 19.383  ? 282  ALA B O     1 
ATOM   6284 C  CB    . ALA B 1 290 ? -40.945 -3.693  12.237  1 16.584  ? 282  ALA B CB    1 
ATOM   6285 N  N     . TYR B 1 291 ? -38.368 -5.009  10.458  1 20.478  ? 283  TYR B N     1 
ATOM   6286 C  CA    . TYR B 1 291 ? -38.011 -5.861  9.325   1 22.015  ? 283  TYR B CA    1 
ATOM   6287 C  C     . TYR B 1 291 ? -39.289 -6.465  8.754   1 22.177  ? 283  TYR B C     1 
ATOM   6288 O  O     . TYR B 1 291 ? -40.182 -6.854  9.507   1 23.145  ? 283  TYR B O     1 
ATOM   6289 C  CB    . TYR B 1 291 ? -37.008 -6.982  9.641   1 21.412  ? 283  TYR B CB    1 
ATOM   6290 C  CG    . TYR B 1 291 ? -36.387 -7.677  8.429   1 20.553  ? 283  TYR B CG    1 
ATOM   6291 C  CD1   . TYR B 1 291 ? -35.223 -7.162  7.837   1 19.881  ? 283  TYR B CD1   1 
ATOM   6292 C  CD2   . TYR B 1 291 ? -36.958 -8.842  7.863   1 20.102  ? 283  TYR B CD2   1 
ATOM   6293 C  CE1   . TYR B 1 291 ? -34.63  -7.802  6.75    1 20.326  ? 283  TYR B CE1   1 
ATOM   6294 C  CE2   . TYR B 1 291 ? -36.392 -9.474  6.748   1 18.893  ? 283  TYR B CE2   1 
ATOM   6295 C  CZ    . TYR B 1 291 ? -35.227 -8.937  6.187   1 20.331  ? 283  TYR B CZ    1 
ATOM   6296 O  OH    . TYR B 1 291 ? -34.602 -9.492  5.104   1 19.046  ? 283  TYR B OH    1 
ATOM   6297 N  N     . ASP B 1 292 ? -39.363 -6.475  7.425   1 22.321  ? 284  ASP B N     1 
ATOM   6298 C  CA    . ASP B 1 292 ? -40.515 -7.008  6.719   1 24.118  ? 284  ASP B CA    1 
ATOM   6299 C  C     . ASP B 1 292 ? -40.042 -7.933  5.605   1 23.969  ? 284  ASP B C     1 
ATOM   6300 O  O     . ASP B 1 292 ? -39.567 -7.446  4.571   1 24.233  ? 284  ASP B O     1 
ATOM   6301 C  CB    . ASP B 1 292 ? -41.515 -5.916  6.35    1 24.299  ? 284  ASP B CB    1 
ATOM   6302 C  CG    . ASP B 1 292 ? -42.78  -6.366  5.617   1 27.746  ? 284  ASP B CG    1 
ATOM   6303 O  OD1   . ASP B 1 292 ? -43.037 -7.59   5.483   1 27.682  ? 284  ASP B OD1   1 
ATOM   6304 O  OD2   . ASP B 1 292 ? -43.515 -5.484  5.159   1 28.676  ? 284  ASP B OD2   1 
ATOM   6305 N  N     . TYR B 1 293 ? -40.267 -9.247  5.825   1 24.064  ? 285  TYR B N     1 
ATOM   6306 C  CA    . TYR B 1 293 ? -40.037 -10.333 4.87    1 26.773  ? 285  TYR B CA    1 
ATOM   6307 C  C     . TYR B 1 293 ? -40.766 -10.147 3.532   1 26.076  ? 285  TYR B C     1 
ATOM   6308 O  O     . TYR B 1 293 ? -40.266 -10.641 2.523   1 24.297  ? 285  TYR B O     1 
ATOM   6309 C  CB    . TYR B 1 293 ? -40.282 -11.735 5.443   1 25.86   ? 285  TYR B CB    1 
ATOM   6310 C  CG    . TYR B 1 293 ? -39.135 -12.249 6.298   1 26.587  ? 285  TYR B CG    1 
ATOM   6311 C  CD1   . TYR B 1 293 ? -39.072 -11.97  7.673   1 25.699  ? 285  TYR B CD1   1 
ATOM   6312 C  CD2   . TYR B 1 293 ? -38.093 -12.996 5.719   1 27.413  ? 285  TYR B CD2   1 
ATOM   6313 C  CE1   . TYR B 1 293 ? -38.008 -12.432 8.446   1 25.946  ? 285  TYR B CE1   1 
ATOM   6314 C  CE2   . TYR B 1 293 ? -37.03  -13.468 6.488   1 25.453  ? 285  TYR B CE2   1 
ATOM   6315 C  CZ    . TYR B 1 293 ? -36.997 -13.186 7.849   1 26.431  ? 285  TYR B CZ    1 
ATOM   6316 O  OH    . TYR B 1 293 ? -35.937 -13.634 8.575   1 28.808  ? 285  TYR B OH    1 
ATOM   6317 N  N     . THR B 1 294 ? -41.9   -9.422  3.525   1 27.246  ? 286  THR B N     1 
ATOM   6318 C  CA    . THR B 1 294 ? -42.704 -9.208  2.32    1 27.594  ? 286  THR B CA    1 
ATOM   6319 C  C     . THR B 1 294 ? -42.153 -8.07   1.447   1 29.653  ? 286  THR B C     1 
ATOM   6320 O  O     . THR B 1 294 ? -42.494 -8.02   0.263   1 31.587  ? 286  THR B O     1 
ATOM   6321 C  CB    . THR B 1 294 ? -44.21  -9.102  2.572   1 26.176  ? 286  THR B CB    1 
ATOM   6322 O  OG1   . THR B 1 294 ? -44.461 -7.876  3.242   1 28.756  ? 286  THR B OG1   1 
ATOM   6323 C  CG2   . THR B 1 294 ? -44.79  -10.27  3.348   1 27.773  ? 286  THR B CG2   1 
ATOM   6324 N  N     . LYS B 1 295 ? -41.289 -7.194  2.001   1 27.117  ? 287  LYS B N     1 
ATOM   6325 C  CA    . LYS B 1 295 ? -40.661 -6.112  1.242   1 25.967  ? 287  LYS B CA    1 
ATOM   6326 C  C     . LYS B 1 295 ? -39.501 -6.655  0.396   1 24.859  ? 287  LYS B C     1 
ATOM   6327 O  O     . LYS B 1 295 ? -38.61  -7.294  0.966   1 24.57   ? 287  LYS B O     1 
ATOM   6328 C  CB    . LYS B 1 295 ? -40.273 -4.867  2.049   1 24.438  ? 287  LYS B CB    1 
ATOM   6329 C  CG    . LYS B 1 295 ? -41.354 -4.161  2.837   1 26.709  ? 287  LYS B CG    1 
ATOM   6330 C  CD    . LYS B 1 295 ? -42.287 -3.242  2.062   1 28.575  ? 287  LYS B CD    1 
ATOM   6331 C  CE    . LYS B 1 295 ? -43.34  -2.829  3.017   1 31.924  ? 287  LYS B CE    1 
ATOM   6332 N  NZ    . LYS B 1 295 ? -44.23  -1.924  2.303   1 36.859  ? 287  LYS B NZ    1 
ATOM   6333 N  N     . PRO B 1 296 ? -39.483 -6.459  -0.963  1 25.215  ? 288  PRO B N     1 
ATOM   6334 C  CA    . PRO B 1 296 ? -38.27  -6.648  -1.752  1 25.123  ? 288  PRO B CA    1 
ATOM   6335 C  C     . PRO B 1 296 ? -37.25  -5.53   -1.54   1 23.096  ? 288  PRO B C     1 
ATOM   6336 O  O     . PRO B 1 296 ? -37.649 -4.396  -1.244  1 21.599  ? 288  PRO B O     1 
ATOM   6337 C  CB    . PRO B 1 296 ? -38.765 -6.714  -3.2    1 24.193  ? 288  PRO B CB    1 
ATOM   6338 C  CG    . PRO B 1 296 ? -39.985 -5.801  -3.181  1 25.366  ? 288  PRO B CG    1 
ATOM   6339 C  CD    . PRO B 1 296 ? -40.61  -6.015  -1.822  1 25.982  ? 288  PRO B CD    1 
ATOM   6340 N  N     . ILE B 1 297 ? -35.957 -5.861  -1.754  1 23.821  ? 289  ILE B N     1 
ATOM   6341 C  CA    . ILE B 1 297 ? -34.903 -4.875  -2.025  1 22.918  ? 289  ILE B CA    1 
ATOM   6342 C  C     . ILE B 1 297 ? -35.42  -3.979  -3.152  1 22.947  ? 289  ILE B C     1 
ATOM   6343 O  O     . ILE B 1 297 ? -35.791 -4.488  -4.216  1 20.336  ? 289  ILE B O     1 
ATOM   6344 C  CB    . ILE B 1 297 ? -33.538 -5.53   -2.356  1 22.63   ? 289  ILE B CB    1 
ATOM   6345 C  CG1   . ILE B 1 297 ? -32.97  -6.254  -1.125  1 22.49   ? 289  ILE B CG1   1 
ATOM   6346 C  CG2   . ILE B 1 297 ? -32.535 -4.516  -2.93   1 20.785  ? 289  ILE B CG2   1 
ATOM   6347 C  CD1   . ILE B 1 297 ? -31.944 -7.329  -1.422  1 24.112  ? 289  ILE B CD1   1 
ATOM   6348 N  N     . THR B 1 298 ? -35.485 -2.677  -2.844  1 22.193  ? 290  THR B N     1 
ATOM   6349 C  CA    . THR B 1 298 ? -36.013 -1.661  -3.745  1 21.899  ? 290  THR B CA    1 
ATOM   6350 C  C     . THR B 1 298 ? -34.926 -0.605  -3.977  1 22.589  ? 290  THR B C     1 
ATOM   6351 O  O     . THR B 1 298 ? -34.132 -0.325  -3.071  1 21.477  ? 290  THR B O     1 
ATOM   6352 C  CB    . THR B 1 298 ? -37.364 -1.146  -3.224  1 21.566  ? 290  THR B CB    1 
ATOM   6353 O  OG1   . THR B 1 298 ? -38.217 -2.291  -3.192  1 20.395  ? 290  THR B OG1   1 
ATOM   6354 C  CG2   . THR B 1 298 ? -38.061 -0.122  -4.111  1 22.763  ? 290  THR B CG2   1 
ATOM   6355 N  N     . TRP B 1 299 ? -34.856 -0.125  -5.231  1 20.933  ? 291  TRP B N     1 
ATOM   6356 C  CA    . TRP B 1 299 ? -33.95  0.923   -5.675  1 21.278  ? 291  TRP B CA    1 
ATOM   6357 C  C     . TRP B 1 299 ? -34.773 2.076   -6.238  1 22.172  ? 291  TRP B C     1 
ATOM   6358 O  O     . TRP B 1 299 ? -35.724 1.822   -6.992  1 23.326  ? 291  TRP B O     1 
ATOM   6359 C  CB    . TRP B 1 299 ? -32.952 0.417   -6.73   1 20.966  ? 291  TRP B CB    1 
ATOM   6360 C  CG    . TRP B 1 299 ? -32.171 -0.81   -6.344  1 22.693  ? 291  TRP B CG    1 
ATOM   6361 C  CD1   . TRP B 1 299 ? -32.576 -2.107  -6.472  1 22.571  ? 291  TRP B CD1   1 
ATOM   6362 C  CD2   . TRP B 1 299 ? -30.827 -0.857  -5.813  1 23.091  ? 291  TRP B CD2   1 
ATOM   6363 N  NE1   . TRP B 1 299 ? -31.602 -2.962  -6.038  1 23.756  ? 291  TRP B NE1   1 
ATOM   6364 C  CE2   . TRP B 1 299 ? -30.514 -2.234  -5.633  1 24.942  ? 291  TRP B CE2   1 
ATOM   6365 C  CE3   . TRP B 1 299 ? -29.869 0.118   -5.463  1 24.562  ? 291  TRP B CE3   1 
ATOM   6366 C  CZ2   . TRP B 1 299 ? -29.28  -2.662  -5.116  1 25.93   ? 291  TRP B CZ2   1 
ATOM   6367 C  CZ3   . TRP B 1 299 ? -28.643 -0.301  -4.973  1 27.27   ? 291  TRP B CZ3   1 
ATOM   6368 C  CH2   . TRP B 1 299 ? -28.356 -1.676  -4.807  1 27.617  ? 291  TRP B CH2   1 
ATOM   6369 N  N     . ILE B 1 300 ? -34.382 3.31    -5.866  1 20.257  ? 292  ILE B N     1 
ATOM   6370 C  CA    . ILE B 1 300 ? -34.898 4.552   -6.44   1 19.636  ? 292  ILE B CA    1 
ATOM   6371 C  C     . ILE B 1 300 ? -33.792 5.138   -7.326  1 20.504  ? 292  ILE B C     1 
ATOM   6372 O  O     . ILE B 1 300 ? -32.757 5.543   -6.8    1 21.437  ? 292  ILE B O     1 
ATOM   6373 C  CB    . ILE B 1 300 ? -35.431 5.563   -5.385  1 19.933  ? 292  ILE B CB    1 
ATOM   6374 C  CG1   . ILE B 1 300 ? -36.5   4.981   -4.452  1 19.502  ? 292  ILE B CG1   1 
ATOM   6375 C  CG2   . ILE B 1 300 ? -35.933 6.846   -6.066  1 19.719  ? 292  ILE B CG2   1 
ATOM   6376 C  CD1   . ILE B 1 300 ? -36.85  5.827   -3.231  1 19.135  ? 292  ILE B CD1   1 
ATOM   6377 N  N     . THR B 1 301 ? -34.042 5.212   -8.646  1 19.799  ? 293  THR B N     1 
ATOM   6378 C  CA    . THR B 1 301 ? -33.176 5.917   -9.581  1 20.866  ? 293  THR B CA    1 
ATOM   6379 C  C     . THR B 1 301 ? -33.629 7.378   -9.661  1 22.41   ? 293  THR B C     1 
ATOM   6380 O  O     . THR B 1 301 ? -34.801 7.644   -9.938  1 21.538  ? 293  THR B O     1 
ATOM   6381 C  CB    . THR B 1 301 ? -33.071 5.23    -10.951 1 22.962  ? 293  THR B CB    1 
ATOM   6382 O  OG1   . THR B 1 301 ? -34.368 5.103   -11.531 1 25.929  ? 293  THR B OG1   1 
ATOM   6383 C  CG2   . THR B 1 301 ? -32.325 3.905   -10.906 1 23.541  ? 293  THR B CG2   1 
ATOM   6384 N  N     . ILE B 1 302 ? -32.7   8.299   -9.346  1 21.966  ? 294  ILE B N     1 
ATOM   6385 C  CA    . ILE B 1 302 ? -32.888 9.742   -9.468  1 22.764  ? 294  ILE B CA    1 
ATOM   6386 C  C     . ILE B 1 302 ? -31.939 10.239  -10.569 1 23.778  ? 294  ILE B C     1 
ATOM   6387 O  O     . ILE B 1 302 ? -30.725 10.301  -10.316 1 23.15   ? 294  ILE B O     1 
ATOM   6388 C  CB    . ILE B 1 302 ? -32.754 10.514  -8.13   1 22.326  ? 294  ILE B CB    1 
ATOM   6389 C  CG1   . ILE B 1 302 ? -33.623 9.896   -6.987  1 23.478  ? 294  ILE B CG1   1 
ATOM   6390 C  CG2   . ILE B 1 302 ? -33.031 12.014  -8.335  1 20.125  ? 294  ILE B CG2   1 
ATOM   6391 C  CD1   . ILE B 1 302 ? -33.251 10.318  -5.571  1 22.578  ? 294  ILE B CD1   1 
ATOM   6392 N  N     . PRO B 1 303 ? -32.431 10.613  -11.794 1 23.976  ? 295  PRO B N     1 
ATOM   6393 C  CA    . PRO B 1 303 ? -31.598 11.315  -12.776 1 23.392  ? 295  PRO B CA    1 
ATOM   6394 C  C     . PRO B 1 303 ? -31.04  12.609  -12.19  1 23.018  ? 295  PRO B C     1 
ATOM   6395 O  O     . PRO B 1 303 ? -31.781 13.374  -11.566 1 24.214  ? 295  PRO B O     1 
ATOM   6396 C  CB    . PRO B 1 303 ? -32.5   11.526  -13.998 1 24.101  ? 295  PRO B CB    1 
ATOM   6397 C  CG    . PRO B 1 303 ? -33.622 10.529  -13.771 1 22.666  ? 295  PRO B CG    1 
ATOM   6398 C  CD    . PRO B 1 303 ? -33.804 10.402  -12.303 1 23.415  ? 295  PRO B CD    1 
ATOM   6399 N  N     . ARG B 1 304 ? -29.716 12.748  -12.28  1 20.883  ? 296  ARG B N     1 
ATOM   6400 C  CA    . ARG B 1 304 ? -28.988 13.9    -11.753 1 21.499  ? 296  ARG B CA    1 
ATOM   6401 C  C     . ARG B 1 304 ? -29.461 15.172  -12.457 1 21.857  ? 296  ARG B C     1 
ATOM   6402 O  O     . ARG B 1 304 ? -29.556 15.194  -13.677 1 21.785  ? 296  ARG B O     1 
ATOM   6403 C  CB    . ARG B 1 304 ? -27.474 13.682  -11.805 1 19.73   ? 296  ARG B CB    1 
ATOM   6404 C  CG    . ARG B 1 304 ? -27.007 12.609  -10.829 1 20.518  ? 296  ARG B CG    1 
ATOM   6405 C  CD    . ARG B 1 304 ? -25.521 12.326  -10.927 1 22.618  ? 296  ARG B CD    1 
ATOM   6406 N  NE    . ARG B 1 304 ? -24.691 13.424  -10.389 1 21.288  ? 296  ARG B NE    1 
ATOM   6407 C  CZ    . ARG B 1 304 ? -23.358 13.543  -10.477 1 20.386  ? 296  ARG B CZ    1 
ATOM   6408 N  NH1   . ARG B 1 304 ? -22.626 12.598  -11.057 1 21.929  ? 296  ARG B NH1   1 
ATOM   6409 N  NH2   . ARG B 1 304 ? -22.749 14.589  -9.928  1 19.121  ? 296  ARG B NH2   1 
ATOM   6410 N  N     . GLY B 1 305 ? -29.859 16.159  -11.647 1 21.86   ? 297  GLY B N     1 
ATOM   6411 C  CA    . GLY B 1 305 ? -30.483 17.396  -12.092 1 22.581  ? 297  GLY B CA    1 
ATOM   6412 C  C     . GLY B 1 305 ? -31.876 17.191  -12.704 1 23.13   ? 297  GLY B C     1 
ATOM   6413 O  O     . GLY B 1 305 ? -32.276 18.013  -13.525 1 22.331  ? 297  GLY B O     1 
ATOM   6414 N  N     . ALA B 1 306 ? -32.61  16.135  -12.282 1 23.358  ? 298  ALA B N     1 
ATOM   6415 C  CA    . ALA B 1 306 ? -34.007 15.876  -12.645 1 25.711  ? 298  ALA B CA    1 
ATOM   6416 C  C     . ALA B 1 306 ? -34.883 17.116  -12.444 1 25.242  ? 298  ALA B C     1 
ATOM   6417 O  O     . ALA B 1 306 ? -34.708 17.85   -11.475 1 21.682  ? 298  ALA B O     1 
ATOM   6418 C  CB    . ALA B 1 306 ? -34.576 14.701  -11.88  1 25.314  ? 298  ALA B CB    1 
ATOM   6419 N  N     . LYS B 1 307 ? -35.781 17.346  -13.407 1 26.58   ? 299  LYS B N     1 
ATOM   6420 C  CA    . LYS B 1 307 ? -36.636 18.529  -13.437 1 27.572  ? 299  LYS B CA    1 
ATOM   6421 C  C     . LYS B 1 307 ? -37.927 18.318  -12.643 1 26.753  ? 299  LYS B C     1 
ATOM   6422 O  O     . LYS B 1 307 ? -38.581 19.296  -12.276 1 29.032  ? 299  LYS B O     1 
ATOM   6423 C  CB    . LYS B 1 307 ? -36.854 19.063  -14.859 1 30.903  ? 299  LYS B CB    1 
ATOM   6424 C  CG    . LYS B 1 307 ? -35.639 19.543  -15.647 1 33.632  ? 299  LYS B CG    1 
ATOM   6425 C  CD    . LYS B 1 307 ? -36.055 19.932  -17.063 1 36.659  ? 299  LYS B CD    1 
ATOM   6426 C  CE    . LYS B 1 307 ? -34.918 20.303  -17.97  1 42.238  ? 299  LYS B CE    1 
ATOM   6427 N  NZ    . LYS B 1 307 ? -34.386 21.65   -17.727 1 56.65   ? 299  LYS B NZ    1 
ATOM   6428 N  N     . SER B 1 308 ? -38.28  17.046  -12.402 1 22.42   ? 300  SER B N     1 
ATOM   6429 C  CA    . SER B 1 308 ? -39.557 16.589  -11.881 1 22.985  ? 300  SER B CA    1 
ATOM   6430 C  C     . SER B 1 308 ? -39.365 15.268  -11.132 1 24.348  ? 300  SER B C     1 
ATOM   6431 O  O     . SER B 1 308 ? -38.553 14.421  -11.538 1 23.221  ? 300  SER B O     1 
ATOM   6432 C  CB    . SER B 1 308 ? -40.53  16.412  -13.039 1 22.412  ? 300  SER B CB    1 
ATOM   6433 O  OG    . SER B 1 308 ? -41.741 15.841  -12.586 1 23.569  ? 300  SER B OG    1 
ATOM   6434 N  N     . LYS B 1 309 ? -40.215 15.061  -10.111 1 22.178  ? 301  LYS B N     1 
ATOM   6435 C  CA    . LYS B 1 309 ? -40.368 13.786  -9.419  1 25.559  ? 301  LYS B CA    1 
ATOM   6436 C  C     . LYS B 1 309 ? -40.853 12.661  -10.354 1 27.623  ? 301  LYS B C     1 
ATOM   6437 O  O     . LYS B 1 309 ? -40.699 11.494  -10.006 1 29.726  ? 301  LYS B O     1 
ATOM   6438 C  CB    . LYS B 1 309 ? -41.169 13.959  -8.12   1 27.96   ? 301  LYS B CB    1 
ATOM   6439 C  CG    . LYS B 1 309 ? -42.669 14.183  -8.262  1 31.155  ? 301  LYS B CG    1 
ATOM   6440 C  CD    . LYS B 1 309 ? -43.293 14.173  -6.878  1 35.7    ? 301  LYS B CD    1 
ATOM   6441 C  CE    . LYS B 1 309 ? -44.769 14.212  -7.013  1 39.687  ? 301  LYS B CE    1 
ATOM   6442 N  NZ    . LYS B 1 309 ? -45.279 14.498  -5.673  1 50.133  ? 301  LYS B NZ    1 
ATOM   6443 N  N     . ASP B 1 310 ? -41.426 13.01   -11.525 1 25.459  ? 302  ASP B N     1 
ATOM   6444 C  CA    . ASP B 1 310 ? -41.859 12.09   -12.578 1 25.92   ? 302  ASP B CA    1 
ATOM   6445 C  C     . ASP B 1 310 ? -40.714 11.283  -13.188 1 22.689  ? 302  ASP B C     1 
ATOM   6446 O  O     . ASP B 1 310 ? -40.962 10.194  -13.699 1 23.219  ? 302  ASP B O     1 
ATOM   6447 C  CB    . ASP B 1 310 ? -42.67  12.803  -13.654 1 28.242  ? 302  ASP B CB    1 
ATOM   6448 C  CG    . ASP B 1 310 ? -43.967 13.479  -13.212 1 34.634  ? 302  ASP B CG    1 
ATOM   6449 O  OD1   . ASP B 1 310 ? -44.488 13.156  -12.115 1 37.029  ? 302  ASP B OD1   1 
ATOM   6450 O  OD2   . ASP B 1 310 ? -44.447 14.353  -13.965 1 37.471  ? 302  ASP B OD2   1 
ATOM   6451 N  N     . GLU B 1 311 ? -39.491 11.828  -13.139 1 21.148  ? 303  GLU B N     1 
ATOM   6452 C  CA    . GLU B 1 311 ? -38.268 11.236  -13.672 1 21.104  ? 303  GLU B CA    1 
ATOM   6453 C  C     . GLU B 1 311 ? -37.767 10.06   -12.82  1 23.752  ? 303  GLU B C     1 
ATOM   6454 O  O     . GLU B 1 311 ? -36.979 9.24    -13.296 1 24.603  ? 303  GLU B O     1 
ATOM   6455 C  CB    . GLU B 1 311 ? -37.153 12.277  -13.757 1 22.285  ? 303  GLU B CB    1 
ATOM   6456 C  CG    . GLU B 1 311 ? -37.467 13.524  -14.591 1 22.622  ? 303  GLU B CG    1 
ATOM   6457 C  CD    . GLU B 1 311 ? -36.27  14.287  -15.114 1 24.19   ? 303  GLU B CD    1 
ATOM   6458 O  OE1   . GLU B 1 311 ? -35.185 13.694  -15.215 1 22.288  ? 303  GLU B OE1   1 
ATOM   6459 O  OE2   . GLU B 1 311 ? -36.395 15.495  -15.374 1 24.011  ? 303  GLU B OE2   1 
ATOM   6460 N  N     . VAL B 1 312 ? -38.195 10.001  -11.548 1 24.154  ? 304  VAL B N     1 
ATOM   6461 C  CA    . VAL B 1 312 ? -37.764 9.038   -10.543 1 23.041  ? 304  VAL B CA    1 
ATOM   6462 C  C     . VAL B 1 312 ? -38.464 7.703   -10.831 1 23.183  ? 304  VAL B C     1 
ATOM   6463 O  O     . VAL B 1 312 ? -39.658 7.703   -11.13  1 23.53   ? 304  VAL B O     1 
ATOM   6464 C  CB    . VAL B 1 312 ? -38.088 9.69    -9.176  1 24.475  ? 304  VAL B CB    1 
ATOM   6465 C  CG1   . VAL B 1 312 ? -38.118 8.742   -7.999  1 28.216  ? 304  VAL B CG1   1 
ATOM   6466 C  CG2   . VAL B 1 312 ? -37.195 10.878  -8.833  1 23.558  ? 304  VAL B CG2   1 
ATOM   6467 N  N     . LYS B 1 313 ? -37.723 6.581   -10.732 1 22.834  ? 305  LYS B N     1 
ATOM   6468 C  CA    . LYS B 1 313 ? -38.232 5.225   -10.972 1 24.552  ? 305  LYS B CA    1 
ATOM   6469 C  C     . LYS B 1 313 ? -37.866 4.286   -9.824  1 25.497  ? 305  LYS B C     1 
ATOM   6470 O  O     . LYS B 1 313 ? -36.757 4.365   -9.274  1 24.741  ? 305  LYS B O     1 
ATOM   6471 C  CB    . LYS B 1 313 ? -37.851 4.594   -12.318 1 27.825  ? 305  LYS B CB    1 
ATOM   6472 C  CG    . LYS B 1 313 ? -38.411 5.297   -13.554 1 36.666  ? 305  LYS B CG    1 
ATOM   6473 C  CD    . LYS B 1 313 ? -38.215 4.53    -14.856 1 46.602  ? 305  LYS B CD    1 
ATOM   6474 C  CE    . LYS B 1 313 ? -38.799 5.201   -16.071 1 51.68   ? 305  LYS B CE    1 
ATOM   6475 N  NZ    . LYS B 1 313 ? -40.256 5.42    -16.042 1 58.814  ? 305  LYS B NZ    1 
ATOM   6476 N  N     . TYR B 1 314 ? -38.824 3.398   -9.505  1 21.814  ? 306  TYR B N     1 
ATOM   6477 C  CA    . TYR B 1 314 ? -38.715 2.373   -8.479  1 23.709  ? 306  TYR B CA    1 
ATOM   6478 C  C     . TYR B 1 314 ? -38.46  1.023   -9.141  1 24.169  ? 306  TYR B C     1 
ATOM   6479 O  O     . TYR B 1 314 ? -39.207 0.613   -10.041 1 23.613  ? 306  TYR B O     1 
ATOM   6480 C  CB    . TYR B 1 314 ? -39.972 2.332   -7.591  1 22.929  ? 306  TYR B CB    1 
ATOM   6481 C  CG    . TYR B 1 314 ? -40.484 3.604   -6.923  1 23.896  ? 306  TYR B CG    1 
ATOM   6482 C  CD1   . TYR B 1 314 ? -39.622 4.655   -6.53   1 24.739  ? 306  TYR B CD1   1 
ATOM   6483 C  CD2   . TYR B 1 314 ? -41.859 3.747   -6.654  1 24.223  ? 306  TYR B CD2   1 
ATOM   6484 C  CE1   . TYR B 1 314 ? -40.113 5.81    -5.915  1 25.494  ? 306  TYR B CE1   1 
ATOM   6485 C  CE2   . TYR B 1 314 ? -42.35  4.895   -6.027  1 25.146  ? 306  TYR B CE2   1 
ATOM   6486 C  CZ    . TYR B 1 314 ? -41.477 5.916   -5.649  1 24.355  ? 306  TYR B CZ    1 
ATOM   6487 O  OH    . TYR B 1 314 ? -41.948 7.029   -5.021  1 25.607  ? 306  TYR B OH    1 
ATOM   6488 N  N     . TRP B 1 315 ? -37.423 0.33    -8.65   1 21.668  ? 307  TRP B N     1 
ATOM   6489 C  CA    . TRP B 1 315 ? -36.962 -0.946  -9.188  1 21.743  ? 307  TRP B CA    1 
ATOM   6490 C  C     . TRP B 1 315 ? -36.932 -1.945  -8.038  1 22.869  ? 307  TRP B C     1 
ATOM   6491 O  O     . TRP B 1 315 ? -36.578 -1.54   -6.929  1 24.856  ? 307  TRP B O     1 
ATOM   6492 C  CB    . TRP B 1 315 ? -35.559 -0.784  -9.804  1 20.871  ? 307  TRP B CB    1 
ATOM   6493 C  CG    . TRP B 1 315 ? -35.457 0.312   -10.834 1 21.566  ? 307  TRP B CG    1 
ATOM   6494 C  CD1   . TRP B 1 315 ? -35.325 1.652   -10.604 1 22.437  ? 307  TRP B CD1   1 
ATOM   6495 C  CD2   . TRP B 1 315 ? -35.484 0.152   -12.272 1 20.7    ? 307  TRP B CD2   1 
ATOM   6496 N  NE1   . TRP B 1 315 ? -35.262 2.342   -11.786 1 21.705  ? 307  TRP B NE1   1 
ATOM   6497 C  CE2   . TRP B 1 315 ? -35.355 1.451   -12.828 1 21.495  ? 307  TRP B CE2   1 
ATOM   6498 C  CE3   . TRP B 1 315 ? -35.593 -0.96   -13.137 1 20.213  ? 307  TRP B CE3   1 
ATOM   6499 C  CZ2   . TRP B 1 315 ? -35.351 1.665   -14.216 1 21.448  ? 307  TRP B CZ2   1 
ATOM   6500 C  CZ3   . TRP B 1 315 ? -35.595 -0.748  -14.504 1 21.304  ? 307  TRP B CZ3   1 
ATOM   6501 C  CH2   . TRP B 1 315 ? -35.49  0.552   -15.033 1 22.889  ? 307  TRP B CH2   1 
ATOM   6502 N  N     . HIS B 1 316 ? -37.265 -3.227  -8.296  1 21.48   ? 308  HIS B N     1 
ATOM   6503 C  CA    . HIS B 1 316 ? -37.296 -4.197  -7.202  1 22.687  ? 308  HIS B CA    1 
ATOM   6504 C  C     . HIS B 1 316 ? -36.628 -5.512  -7.573  1 21.763  ? 308  HIS B C     1 
ATOM   6505 O  O     . HIS B 1 316 ? -36.648 -5.909  -8.731  1 23.224  ? 308  HIS B O     1 
ATOM   6506 C  CB    . HIS B 1 316 ? -38.707 -4.335  -6.601  1 24.595  ? 308  HIS B CB    1 
ATOM   6507 C  CG    . HIS B 1 316 ? -39.626 -5.066  -7.519  1 24.793  ? 308  HIS B CG    1 
ATOM   6508 N  ND1   . HIS B 1 316 ? -40.287 -4.453  -8.559  1 26.802  ? 308  HIS B ND1   1 
ATOM   6509 C  CD2   . HIS B 1 316 ? -39.921 -6.375  -7.61   1 25.603  ? 308  HIS B CD2   1 
ATOM   6510 C  CE1   . HIS B 1 316 ? -40.98  -5.365  -9.236  1 25.576  ? 308  HIS B CE1   1 
ATOM   6511 N  NE2   . HIS B 1 316 ? -40.772 -6.536  -8.672  1 24.481  ? 308  HIS B NE2   1 
ATOM   6512 N  N     . TRP B 1 317 ? -36.113 -6.194  -6.543  1 23.008  ? 309  TRP B N     1 
ATOM   6513 C  CA    . TRP B 1 317 ? -35.645 -7.57   -6.624  1 24.343  ? 309  TRP B CA    1 
ATOM   6514 C  C     . TRP B 1 317 ? -36.488 -8.457  -5.696  1 25.512  ? 309  TRP B C     1 
ATOM   6515 O  O     . TRP B 1 317 ? -37.655 -8.666  -6.009  1 25.143  ? 309  TRP B O     1 
ATOM   6516 C  CB    . TRP B 1 317 ? -34.11  -7.676  -6.513  1 27.293  ? 309  TRP B CB    1 
ATOM   6517 C  CG    . TRP B 1 317 ? -33.586 -9.089  -6.604  1 29.335  ? 309  TRP B CG    1 
ATOM   6518 C  CD1   . TRP B 1 317 ? -33.654 -9.912  -7.693  1 29.592  ? 309  TRP B CD1   1 
ATOM   6519 C  CD2   . TRP B 1 317 ? -32.978 -9.869  -5.545  1 29.096  ? 309  TRP B CD2   1 
ATOM   6520 N  NE1   . TRP B 1 317 ? -33.13  -11.144 -7.393  1 29.944  ? 309  TRP B NE1   1 
ATOM   6521 C  CE2   . TRP B 1 317 ? -32.714 -11.159 -6.087  1 30.253  ? 309  TRP B CE2   1 
ATOM   6522 C  CE3   . TRP B 1 317 ? -32.637 -9.62   -4.202  1 26.642  ? 309  TRP B CE3   1 
ATOM   6523 C  CZ2   . TRP B 1 317 ? -32.115 -12.185 -5.335  1 31.195  ? 309  TRP B CZ2   1 
ATOM   6524 C  CZ3   . TRP B 1 317 ? -32.05  -10.634 -3.456  1 30.179  ? 309  TRP B CZ3   1 
ATOM   6525 C  CH2   . TRP B 1 317 ? -31.795 -11.908 -4.015  1 29.916  ? 309  TRP B CH2   1 
ATOM   6526 N  N     . LYS B 1 318 ? -35.918 -8.953  -4.583  1 27.128  ? 310  LYS B N     1 
ATOM   6527 C  CA    . LYS B 1 318 ? -36.457 -9.919  -3.624  1 26.876  ? 310  LYS B CA    1 
ATOM   6528 C  C     . LYS B 1 318 ? -36.025 -9.461  -2.227  1 26.235  ? 310  LYS B C     1 
ATOM   6529 O  O     . LYS B 1 318 ? -35.175 -8.57   -2.112  1 23.808  ? 310  LYS B O     1 
ATOM   6530 C  CB    . LYS B 1 318 ? -35.928 -11.332 -3.92   1 26.578  ? 310  LYS B CB    1 
ATOM   6531 C  CG    . LYS B 1 318 ? -36.278 -11.994 -5.257  1 29.588  ? 310  LYS B CG    1 
ATOM   6532 C  CD    . LYS B 1 318 ? -35.657 -13.366 -5.5    1 32.024  ? 310  LYS B CD    1 
ATOM   6533 C  CE    . LYS B 1 318 ? -36.139 -13.933 -6.803  1 37.219  ? 310  LYS B CE    1 
ATOM   6534 N  NZ    . LYS B 1 318 ? -35.155 -14.775 -7.5    1 38.744  ? 310  LYS B NZ    1 
ATOM   6535 N  N     . ASN B 1 319 ? -36.618 -10.052 -1.173  1 24.955  ? 311  ASN B N     1 
ATOM   6536 C  CA    . ASN B 1 319 ? -36.248 -9.802  0.219   1 24.636  ? 311  ASN B CA    1 
ATOM   6537 C  C     . ASN B 1 319 ? -34.79  -10.178 0.464   1 25.078  ? 311  ASN B C     1 
ATOM   6538 O  O     . ASN B 1 319 ? -34.323 -11.216 0.001   1 23.172  ? 311  ASN B O     1 
ATOM   6539 C  CB    . ASN B 1 319 ? -37.186 -10.482 1.208   1 26.563  ? 311  ASN B CB    1 
ATOM   6540 C  CG    . ASN B 1 319 ? -36.967 -10.046 2.643   1 28.033  ? 311  ASN B CG    1 
ATOM   6541 O  OD1   . ASN B 1 319 ? -36.386 -10.798 3.436   1 27.592  ? 311  ASN B OD1   1 
ATOM   6542 N  ND2   . ASN B 1 319 ? -37.409 -8.846  3.003   1 25.377  ? 311  ASN B ND2   1 
ATOM   6543 N  N     . GLY B 1 320 ? -34.104 -9.27   1.167   1 23.76   ? 312  GLY B N     1 
ATOM   6544 C  CA    . GLY B 1 320 ? -32.736 -9.389  1.652   1 22.147  ? 312  GLY B CA    1 
ATOM   6545 C  C     . GLY B 1 320 ? -32.249 -8.031  2.152   1 20.546  ? 312  GLY B C     1 
ATOM   6546 O  O     . GLY B 1 320 ? -32.991 -7.062  2.054   1 19.82   ? 312  GLY B O     1 
ATOM   6547 N  N     . MET B 1 321 ? -30.99  -7.971  2.608   1 20.83   ? 313  MET B N     1 
ATOM   6548 C  CA    . MET B 1 321 ? -30.413 -6.775  3.209   1 20.792  ? 313  MET B CA    1 
ATOM   6549 C  C     . MET B 1 321 ? -29.063 -6.474  2.545   1 20.906  ? 313  MET B C     1 
ATOM   6550 O  O     . MET B 1 321 ? -28.05  -7.081  2.915   1 21.671  ? 313  MET B O     1 
ATOM   6551 C  CB    . MET B 1 321 ? -30.4   -6.829  4.741   1 20.83   ? 313  MET B CB    1 
ATOM   6552 C  CG    . MET B 1 321 ? -30.092 -5.492  5.438   1 20.304  ? 313  MET B CG    1 
ATOM   6553 S  SD    . MET B 1 321 ? -30.433 -5.718  7.187   1 19.227  ? 313  MET B SD    1 
ATOM   6554 C  CE    . MET B 1 321 ? -29.57  -4.327  7.939   1 20.228  ? 313  MET B CE    1 
ATOM   6555 N  N     . PRO B 1 322 ? -29.024 -5.546  1.547   1 19.685  ? 314  PRO B N     1 
ATOM   6556 C  CA    . PRO B 1 322 ? -27.769 -5.026  1.019   1 19.695  ? 314  PRO B CA    1 
ATOM   6557 C  C     . PRO B 1 322 ? -27.306 -3.813  1.828   1 19.63   ? 314  PRO B C     1 
ATOM   6558 O  O     . PRO B 1 322 ? -27.919 -2.748  1.712   1 19.781  ? 314  PRO B O     1 
ATOM   6559 C  CB    . PRO B 1 322 ? -28.106 -4.817  -0.469  1 19.291  ? 314  PRO B CB    1 
ATOM   6560 C  CG    . PRO B 1 322 ? -29.611 -4.482  -0.447  1 19.098  ? 314  PRO B CG    1 
ATOM   6561 C  CD    . PRO B 1 322 ? -30.182 -4.898  0.888   1 18.828  ? 314  PRO B CD    1 
ATOM   6562 N  N     . ILE B 1 323 ? -26.27  -3.99   2.664   1 18.345  ? 315  ILE B N     1 
ATOM   6563 C  CA    . ILE B 1 323 ? -25.965 -3.026  3.728   1 16.964  ? 315  ILE B CA    1 
ATOM   6564 C  C     . ILE B 1 323 ? -25.28  -1.792  3.14    1 16.903  ? 315  ILE B C     1 
ATOM   6565 O  O     . ILE B 1 323 ? -25.787 -0.688  3.332   1 16.564  ? 315  ILE B O     1 
ATOM   6566 C  CB    . ILE B 1 323 ? -25.231 -3.634  4.948   1 17.213  ? 315  ILE B CB    1 
ATOM   6567 C  CG1   . ILE B 1 323 ? -25.974 -4.852  5.512   1 17.226  ? 315  ILE B CG1   1 
ATOM   6568 C  CG2   . ILE B 1 323 ? -24.973 -2.578  6.037   1 16.253  ? 315  ILE B CG2   1 
ATOM   6569 C  CD1   . ILE B 1 323 ? -25.072 -5.826  6.234   1 18.413  ? 315  ILE B CD1   1 
ATOM   6570 N  N     . HIS B 1 324 ? -24.147 -2.006  2.446   1 17.441  ? 316  HIS B N     1 
ATOM   6571 C  CA    . HIS B 1 324 ? -23.329 -0.947  1.879   1 18.964  ? 316  HIS B CA    1 
ATOM   6572 C  C     . HIS B 1 324 ? -22.932 -1.261  0.436   1 20.749  ? 316  HIS B C     1 
ATOM   6573 O  O     . HIS B 1 324 ? -22.573 -2.398  0.13    1 21.517  ? 316  HIS B O     1 
ATOM   6574 C  CB    . HIS B 1 324 ? -22.063 -0.729  2.72    1 18.798  ? 316  HIS B CB    1 
ATOM   6575 C  CG    . HIS B 1 324 ? -22.3   -0.116  4.047   1 18.762  ? 316  HIS B CG    1 
ATOM   6576 N  ND1   . HIS B 1 324 ? -22.028 -0.778  5.227   1 18.296  ? 316  HIS B ND1   1 
ATOM   6577 C  CD2   . HIS B 1 324 ? -22.738 1.092   4.381   1 17.809  ? 316  HIS B CD2   1 
ATOM   6578 C  CE1   . HIS B 1 324 ? -22.312 0       6.25    1 17.118  ? 316  HIS B CE1   1 
ATOM   6579 N  NE2   . HIS B 1 324 ? -22.771 1.131   5.753   1 18.094  ? 316  HIS B NE2   1 
ATOM   6580 N  N     . THR B 1 325 ? -22.942 -0.202  -0.395  1 20.17   ? 317  THR B N     1 
ATOM   6581 C  CA    . THR B 1 325 ? -22.387 -0.178  -1.748  1 19.574  ? 317  THR B CA    1 
ATOM   6582 C  C     . THR B 1 325 ? -20.872 0.023   -1.686  1 19.746  ? 317  THR B C     1 
ATOM   6583 O  O     . THR B 1 325 ? -20.383 0.753   -0.812  1 18.394  ? 317  THR B O     1 
ATOM   6584 C  CB    . THR B 1 325 ? -23.052 0.881   -2.637  1 20.878  ? 317  THR B CB    1 
ATOM   6585 O  OG1   . THR B 1 325 ? -22.837 2.161   -2.045  1 20.727  ? 317  THR B OG1   1 
ATOM   6586 C  CG2   . THR B 1 325 ? -24.551 0.679   -2.815  1 20.583  ? 317  THR B CG2   1 
ATOM   6587 N  N     . ALA B 1 326 ? -20.147 -0.619  -2.628  1 18.363  ? 318  ALA B N     1 
ATOM   6588 C  CA    . ALA B 1 326 ? -18.778 -0.25   -2.965  1 16.079  ? 318  ALA B CA    1 
ATOM   6589 C  C     . ALA B 1 326 ? -18.831 1.106   -3.682  1 18.053  ? 318  ALA B C     1 
ATOM   6590 O  O     . ALA B 1 326 ? -18.569 2.162   -3.071  1 18.407  ? 318  ALA B O     1 
ATOM   6591 C  CB    . ALA B 1 326 ? -18.135 -1.357  -3.766  1 15.565  ? 318  ALA B CB    1 
ATOM   6592 N  N     . SER B 1 327 ? -19.253 1.071   -4.956  1 17.27   ? 319  SER B N     1 
ATOM   6593 C  CA    . SER B 1 327 ? -19.713 2.222   -5.721  1 17.942  ? 319  SER B CA    1 
ATOM   6594 C  C     . SER B 1 327 ? -20.597 1.736   -6.879  1 18.194  ? 319  SER B C     1 
ATOM   6595 O  O     . SER B 1 327 ? -20.949 0.547   -6.94   1 18.432  ? 319  SER B O     1 
ATOM   6596 C  CB    . SER B 1 327 ? -18.556 3.097   -6.172  1 17.601  ? 319  SER B CB    1 
ATOM   6597 O  OG    . SER B 1 327 ? -18.997 4.412   -6.479  1 18.874  ? 319  SER B OG    1 
ATOM   6598 N  N     . GLY B 1 328 ? -20.952 2.676   -7.767  1 17.334  ? 320  GLY B N     1 
ATOM   6599 C  CA    . GLY B 1 328 ? -21.718 2.427   -8.974  1 20.247  ? 320  GLY B CA    1 
ATOM   6600 C  C     . GLY B 1 328 ? -21.075 3.053   -10.203 1 20.576  ? 320  GLY B C     1 
ATOM   6601 O  O     . GLY B 1 328 ? -20.205 3.928   -10.074 1 19.342  ? 320  GLY B O     1 
ATOM   6602 N  N     . PHE B 1 329 ? -21.538 2.58    -11.378 1 20.991  ? 321  PHE B N     1 
ATOM   6603 C  CA    . PHE B 1 329 ? -21.187 3.137   -12.688 1 21.244  ? 321  PHE B CA    1 
ATOM   6604 C  C     . PHE B 1 329 ? -22.259 2.816   -13.731 1 20.756  ? 321  PHE B C     1 
ATOM   6605 O  O     . PHE B 1 329 ? -23.183 2.05    -13.461 1 22.299  ? 321  PHE B O     1 
ATOM   6606 C  CB    . PHE B 1 329 ? -19.74  2.809   -13.098 1 20.089  ? 321  PHE B CB    1 
ATOM   6607 C  CG    . PHE B 1 329 ? -19.46  1.368   -13.513 1 19.372  ? 321  PHE B CG    1 
ATOM   6608 C  CD1   . PHE B 1 329 ? -19.139 0.394   -12.552 1 18.186  ? 321  PHE B CD1   1 
ATOM   6609 C  CD2   . PHE B 1 329 ? -19.471 1.008   -14.882 1 18.947  ? 321  PHE B CD2   1 
ATOM   6610 C  CE1   . PHE B 1 329 ? -18.911 -0.934  -12.95  1 18.593  ? 321  PHE B CE1   1 
ATOM   6611 C  CE2   . PHE B 1 329 ? -19.219 -0.313  -15.289 1 19.663  ? 321  PHE B CE2   1 
ATOM   6612 C  CZ    . PHE B 1 329 ? -18.944 -1.289  -14.315 1 19.668  ? 321  PHE B CZ    1 
ATOM   6613 N  N     . GLU B 1 330 ? -22.11  3.437   -14.911 1 21.467  ? 322  GLU B N     1 
ATOM   6614 C  CA    . GLU B 1 330 ? -22.826 3.082   -16.128 1 21.768  ? 322  GLU B CA    1 
ATOM   6615 C  C     . GLU B 1 330 ? -21.868 2.413   -17.123 1 22.672  ? 322  GLU B C     1 
ATOM   6616 O  O     . GLU B 1 330 ? -20.833 2.982   -17.487 1 21.573  ? 322  GLU B O     1 
ATOM   6617 C  CB    . GLU B 1 330 ? -23.584 4.297   -16.667 1 21.715  ? 322  GLU B CB    1 
ATOM   6618 C  CG    . GLU B 1 330 ? -24.738 4.763   -15.778 1 21.775  ? 322  GLU B CG    1 
ATOM   6619 C  CD    . GLU B 1 330 ? -25.107 6.217   -15.989 1 23.402  ? 322  GLU B CD    1 
ATOM   6620 O  OE1   . GLU B 1 330 ? -25.538 6.552   -17.11  1 25.642  ? 322  GLU B OE1   1 
ATOM   6621 O  OE2   . GLU B 1 330 ? -24.986 7.042   -15.062 1 23.399  ? 322  GLU B OE2   1 
ATOM   6622 N  N     . ASP B 1 331 ? -22.249 1.206   -17.578 1 24.522  ? 323  ASP B N     1 
ATOM   6623 C  CA    . ASP B 1 331 ? -21.548 0.428   -18.603 1 28.223  ? 323  ASP B CA    1 
ATOM   6624 C  C     . ASP B 1 331 ? -21.737 1.061   -20     1 29.087  ? 323  ASP B C     1 
ATOM   6625 O  O     . ASP B 1 331 ? -22.5   2.029   -20.161 1 25.715  ? 323  ASP B O     1 
ATOM   6626 C  CB    . ASP B 1 331 ? -21.9   -1.054  -18.456 1 28.771  ? 323  ASP B CB    1 
ATOM   6627 C  CG    . ASP B 1 331 ? -23.256 -1.558  -18.958 1 27.317  ? 323  ASP B CG    1 
ATOM   6628 O  OD1   . ASP B 1 331 ? -24.02  -0.832  -19.639 1 28.595  ? 323  ASP B OD1   1 
ATOM   6629 O  OD2   . ASP B 1 331 ? -23.567 -2.719  -18.68  1 27      ? 323  ASP B OD2   1 
ATOM   6630 N  N     . GLU B 1 332 ? -21.094 0.447   -21.016 1 29.301  ? 324  GLU B N     1 
ATOM   6631 C  CA    . GLU B 1 332 ? -21.176 0.75    -22.446 1 37.474  ? 324  GLU B CA    1 
ATOM   6632 C  C     . GLU B 1 332 ? -22.622 0.811   -22.98  1 34.118  ? 324  GLU B C     1 
ATOM   6633 O  O     . GLU B 1 332 ? -22.876 1.617   -23.876 1 34.124  ? 324  GLU B O     1 
ATOM   6634 C  CB    . GLU B 1 332 ? -20.294 -0.221  -23.239 1 46.48   ? 324  GLU B CB    1 
ATOM   6635 C  CG    . GLU B 1 332 ? -19.848 0.288   -24.613 1 68.209  ? 324  GLU B CG    1 
ATOM   6636 C  CD    . GLU B 1 332 ? -19.048 -0.584  -25.582 1 81.378  ? 324  GLU B CD    1 
ATOM   6637 O  OE1   . GLU B 1 332 ? -18.439 -1.621  -25.207 1 86.252  ? 324  GLU B OE1   1 
ATOM   6638 O  OE2   . GLU B 1 332 ? -19.054 -0.2    -26.775 1 79.471  ? 324  GLU B OE2   1 
ATOM   6639 N  N     . GLN B 1 333 ? -23.539 -0.006  -22.424 1 31.377  ? 325  GLN B N     1 
ATOM   6640 C  CA    . GLN B 1 333 ? -24.944 -0.1    -22.824 1 29.926  ? 325  GLN B CA    1 
ATOM   6641 C  C     . GLN B 1 333 ? -25.855 0.84    -22.016 1 31.555  ? 325  GLN B C     1 
ATOM   6642 O  O     . GLN B 1 333 ? -27.086 0.798   -22.191 1 29.435  ? 325  GLN B O     1 
ATOM   6643 C  CB    . GLN B 1 333 ? -25.387 -1.568  -22.869 1 28.844  ? 325  GLN B CB    1 
ATOM   6644 C  CG    . GLN B 1 333 ? -24.845 -2.382  -24.048 1 29.436  ? 325  GLN B CG    1 
ATOM   6645 C  CD    . GLN B 1 333 ? -25.066 -1.759  -25.416 1 28.916  ? 325  GLN B CD    1 
ATOM   6646 O  OE1   . GLN B 1 333 ? -26.191 -1.475  -25.832 1 27.837  ? 325  GLN B OE1   1 
ATOM   6647 N  NE2   . GLN B 1 333 ? -23.972 -1.486  -26.109 1 29.715  ? 325  GLN B NE2   1 
ATOM   6648 N  N     . GLY B 1 334 ? -25.244 1.681   -21.153 1 27.987  ? 326  GLY B N     1 
ATOM   6649 C  CA    . GLY B 1 334 ? -25.894 2.654   -20.278 1 27.361  ? 326  GLY B CA    1 
ATOM   6650 C  C     . GLY B 1 334 ? -26.567 2.049   -19.039 1 27.36   ? 326  GLY B C     1 
ATOM   6651 O  O     . GLY B 1 334 ? -27.319 2.765   -18.372 1 28.493  ? 326  GLY B O     1 
ATOM   6652 N  N     . ARG B 1 335 ? -26.272 0.769   -18.722 1 25.693  ? 327  ARG B N     1 
ATOM   6653 C  CA    . ARG B 1 335 ? -26.812 0.019   -17.581 1 25.337  ? 327  ARG B CA    1 
ATOM   6654 C  C     . ARG B 1 335 ? -26.082 0.427   -16.3   1 23.591  ? 327  ARG B C     1 
ATOM   6655 O  O     . ARG B 1 335 ? -24.869 0.613   -16.344 1 23.645  ? 327  ARG B O     1 
ATOM   6656 C  CB    . ARG B 1 335 ? -26.702 -1.505  -17.728 1 25.694  ? 327  ARG B CB    1 
ATOM   6657 C  CG    . ARG B 1 335 ? -27.425 -2.1    -18.933 1 30.854  ? 327  ARG B CG    1 
ATOM   6658 C  CD    . ARG B 1 335 ? -27.341 -3.603  -19.057 1 33.653  ? 327  ARG B CD    1 
ATOM   6659 N  NE    . ARG B 1 335 ? -26.035 -4.045  -19.557 1 42.754  ? 327  ARG B NE    1 
ATOM   6660 C  CZ    . ARG B 1 335 ? -25.709 -4.702  -20.678 1 47.683  ? 327  ARG B CZ    1 
ATOM   6661 N  NH1   . ARG B 1 335 ? -26.599 -5.085  -21.593 1 43.376  ? 327  ARG B NH1   1 
ATOM   6662 N  NH2   . ARG B 1 335 ? -24.435 -4.964  -20.885 1 50.057  ? 327  ARG B NH2   1 
ATOM   6663 N  N     . ILE B 1 336 ? -26.844 0.577   -15.197 1 22.836  ? 328  ILE B N     1 
ATOM   6664 C  CA    . ILE B 1 336 ? -26.355 0.899   -13.849 1 22.274  ? 328  ILE B CA    1 
ATOM   6665 C  C     . ILE B 1 336 ? -25.83  -0.402  -13.221 1 20.905  ? 328  ILE B C     1 
ATOM   6666 O  O     . ILE B 1 336 ? -26.553 -1.399  -13.141 1 21.879  ? 328  ILE B O     1 
ATOM   6667 C  CB    . ILE B 1 336 ? -27.409 1.648   -12.987 1 20.95   ? 328  ILE B CB    1 
ATOM   6668 C  CG1   . ILE B 1 336 ? -27.885 2.981   -13.622 1 20.217  ? 328  ILE B CG1   1 
ATOM   6669 C  CG2   . ILE B 1 336 ? -26.921 1.888   -11.555 1 21.069  ? 328  ILE B CG2   1 
ATOM   6670 C  CD1   . ILE B 1 336 ? -29.306 3.41    -13.246 1 19.804  ? 328  ILE B CD1   1 
ATOM   6671 N  N     . ILE B 1 337 ? -24.553 -0.366  -12.817 1 21.047  ? 329  ILE B N     1 
ATOM   6672 C  CA    . ILE B 1 337 ? -23.808 -1.468  -12.21  1 20.973  ? 329  ILE B CA    1 
ATOM   6673 C  C     . ILE B 1 337 ? -23.397 -1.002  -10.81  1 21.326  ? 329  ILE B C     1 
ATOM   6674 O  O     . ILE B 1 337 ? -22.684 -0.006  -10.693 1 24.27   ? 329  ILE B O     1 
ATOM   6675 C  CB    . ILE B 1 337 ? -22.591 -1.923  -13.068 1 18.749  ? 329  ILE B CB    1 
ATOM   6676 C  CG1   . ILE B 1 337 ? -22.842 -2.119  -14.618 1 17.214  ? 329  ILE B CG1   1 
ATOM   6677 C  CG2   . ILE B 1 337 ? -21.856 -3.11   -12.423 1 18.582  ? 329  ILE B CG2   1 
ATOM   6678 C  CD1   . ILE B 1 337 ? -23.898 -3.128  -15.04  1 17.548  ? 329  ILE B CD1   1 
ATOM   6679 N  N     . ILE B 1 338 ? -23.877 -1.725  -9.785  1 21.849  ? 330  ILE B N     1 
ATOM   6680 C  CA    . ILE B 1 338 ? -23.664 -1.45   -8.364  1 21.3    ? 330  ILE B CA    1 
ATOM   6681 C  C     . ILE B 1 338 ? -23.202 -2.75   -7.688  1 21.453  ? 330  ILE B C     1 
ATOM   6682 O  O     . ILE B 1 338 ? -23.893 -3.77   -7.774  1 21.497  ? 330  ILE B O     1 
ATOM   6683 C  CB    . ILE B 1 338 ? -24.914 -0.831  -7.686  1 20.377  ? 330  ILE B CB    1 
ATOM   6684 C  CG1   . ILE B 1 338 ? -25.401 0.502   -8.35   1 20.639  ? 330  ILE B CG1   1 
ATOM   6685 C  CG2   . ILE B 1 338 ? -24.703 -0.655  -6.174  1 20.277  ? 330  ILE B CG2   1 
ATOM   6686 C  CD1   . ILE B 1 338 ? -26.86  0.864   -8.051  1 20.628  ? 330  ILE B CD1   1 
ATOM   6687 N  N     . ASP B 1 339 ? -22.039 -2.68   -7.011  1 22.834  ? 331  ASP B N     1 
ATOM   6688 C  CA    . ASP B 1 339 ? -21.615 -3.721  -6.082  1 23.936  ? 331  ASP B CA    1 
ATOM   6689 C  C     . ASP B 1 339 ? -21.977 -3.359  -4.648  1 23.906  ? 331  ASP B C     1 
ATOM   6690 O  O     . ASP B 1 339 ? -21.783 -2.221  -4.236  1 22.419  ? 331  ASP B O     1 
ATOM   6691 C  CB    . ASP B 1 339 ? -20.15  -4.097  -6.205  1 23.872  ? 331  ASP B CB    1 
ATOM   6692 C  CG    . ASP B 1 339 ? -19.689 -4.734  -7.51   1 27.291  ? 331  ASP B CG    1 
ATOM   6693 O  OD1   . ASP B 1 339 ? -20.463 -4.751  -8.505  1 26.965  ? 331  ASP B OD1   1 
ATOM   6694 O  OD2   . ASP B 1 339 ? -18.521 -5.168  -7.544  1 27.007  ? 331  ASP B OD2   1 
ATOM   6695 N  N     . SER B 1 340 ? -22.479 -4.361  -3.919  1 22.609  ? 332  SER B N     1 
ATOM   6696 C  CA    . SER B 1 340 ? -22.847 -4.231  -2.518  1 22.376  ? 332  SER B CA    1 
ATOM   6697 C  C     . SER B 1 340 ? -22.555 -5.52   -1.746  1 20.224  ? 332  SER B C     1 
ATOM   6698 O  O     . SER B 1 340 ? -22.428 -6.584  -2.353  1 20.687  ? 332  SER B O     1 
ATOM   6699 C  CB    . SER B 1 340 ? -24.288 -3.73   -2.357  1 21.352  ? 332  SER B CB    1 
ATOM   6700 O  OG    . SER B 1 340 ? -25.247 -4.766  -2.539  1 22.11   ? 332  SER B OG    1 
ATOM   6701 N  N     . SER B 1 341 ? -22.499 -5.405  -0.406  1 19.496  ? 333  SER B N     1 
ATOM   6702 C  CA    . SER B 1 341 ? -22.777 -6.535  0.482   1 20.144  ? 333  SER B CA    1 
ATOM   6703 C  C     . SER B 1 341 ? -24.22  -7.002  0.299   1 21.957  ? 333  SER B C     1 
ATOM   6704 O  O     . SER B 1 341 ? -25.071 -6.215  -0.116  1 21.684  ? 333  SER B O     1 
ATOM   6705 C  CB    . SER B 1 341 ? -22.451 -6.244  1.928   1 19.964  ? 333  SER B CB    1 
ATOM   6706 O  OG    . SER B 1 341 ? -23.284 -5.238  2.484   1 20.298  ? 333  SER B OG    1 
ATOM   6707 N  N     . LEU B 1 342 ? -24.455 -8.301  0.543   1 23.336  ? 334  LEU B N     1 
ATOM   6708 C  CA    . LEU B 1 342 ? -25.786 -8.887  0.534   1 22.66   ? 334  LEU B CA    1 
ATOM   6709 C  C     . LEU B 1 342 ? -25.878 -9.956  1.617   1 23.646  ? 334  LEU B C     1 
ATOM   6710 O  O     . LEU B 1 342 ? -25.197 -10.992 1.539   1 24.161  ? 334  LEU B O     1 
ATOM   6711 C  CB    . LEU B 1 342 ? -26.267 -9.391  -0.835  1 23.042  ? 334  LEU B CB    1 
ATOM   6712 C  CG    . LEU B 1 342 ? -27.663 -10.025 -0.914  1 22.806  ? 334  LEU B CG    1 
ATOM   6713 C  CD1   . LEU B 1 342 ? -28.788 -9.062  -0.553  1 22.458  ? 334  LEU B CD1   1 
ATOM   6714 C  CD2   . LEU B 1 342 ? -27.863 -10.611 -2.303  1 24.618  ? 334  LEU B CD2   1 
ATOM   6715 N  N     . VAL B 1 343 ? -26.753 -9.649  2.592   1 21.233  ? 335  VAL B N     1 
ATOM   6716 C  CA    . VAL B 1 343 ? -27.159 -10.571 3.65    1 20.994  ? 335  VAL B CA    1 
ATOM   6717 C  C     . VAL B 1 343 ? -28.556 -11.057 3.273   1 19.937  ? 335  VAL B C     1 
ATOM   6718 O  O     . VAL B 1 343 ? -29.444 -10.241 3.034   1 19.787  ? 335  VAL B O     1 
ATOM   6719 C  CB    . VAL B 1 343 ? -27.061 -9.96   5.07    1 19.695  ? 335  VAL B CB    1 
ATOM   6720 C  CG1   . VAL B 1 343 ? -27.418 -10.938 6.176   1 21.709  ? 335  VAL B CG1   1 
ATOM   6721 C  CG2   . VAL B 1 343 ? -25.662 -9.426  5.363   1 19.875  ? 335  VAL B CG2   1 
ATOM   6722 N  N     . HIS B 1 344 ? -28.724 -12.388 3.249   1 21.023  ? 336  HIS B N     1 
ATOM   6723 C  CA    . HIS B 1 344 ? -29.954 -13.083 2.863   1 21.506  ? 336  HIS B CA    1 
ATOM   6724 C  C     . HIS B 1 344 ? -30.919 -13.174 4.051   1 21.334  ? 336  HIS B C     1 
ATOM   6725 O  O     . HIS B 1 344 ? -31.38  -14.261 4.395   1 23.633  ? 336  HIS B O     1 
ATOM   6726 C  CB    . HIS B 1 344 ? -29.643 -14.414 2.159   1 21.741  ? 336  HIS B CB    1 
ATOM   6727 C  CG    . HIS B 1 344 ? -28.855 -14.27  0.906   1 24.077  ? 336  HIS B CG    1 
ATOM   6728 N  ND1   . HIS B 1 344 ? -29.414 -14.425 -0.341  1 27.237  ? 336  HIS B ND1   1 
ATOM   6729 C  CD2   . HIS B 1 344 ? -27.552 -13.977 0.694   1 26.791  ? 336  HIS B CD2   1 
ATOM   6730 C  CE1   . HIS B 1 344 ? -28.474 -14.23  -1.268  1 29.836  ? 336  HIS B CE1   1 
ATOM   6731 N  NE2   . HIS B 1 344 ? -27.333 -13.949 -0.662  1 27.81   ? 336  HIS B NE2   1 
ATOM   6732 N  N     . GLY B 1 345 ? -31.245 -12.017 4.652   1 21.363  ? 337  GLY B N     1 
ATOM   6733 C  CA    . GLY B 1 345 ? -32.054 -11.89  5.865   1 21.403  ? 337  GLY B CA    1 
ATOM   6734 C  C     . GLY B 1 345 ? -31.656 -10.641 6.645   1 20.372  ? 337  GLY B C     1 
ATOM   6735 O  O     . GLY B 1 345 ? -30.967 -9.785  6.1     1 24.175  ? 337  GLY B O     1 
ATOM   6736 N  N     . ASN B 1 346 ? -32.064 -10.58  7.916   1 21.039  ? 338  ASN B N     1 
ATOM   6737 C  CA    . ASN B 1 346 ? -31.923 -9.415  8.775   1 21.765  ? 338  ASN B CA    1 
ATOM   6738 C  C     . ASN B 1 346 ? -30.531 -9.387  9.427   1 22.095  ? 338  ASN B C     1 
ATOM   6739 O  O     . ASN B 1 346 ? -30.274 -10.166 10.341  1 22.258  ? 338  ASN B O     1 
ATOM   6740 C  CB    . ASN B 1 346 ? -33.083 -9.324  9.766   1 20.45   ? 338  ASN B CB    1 
ATOM   6741 C  CG    . ASN B 1 346 ? -33.166 -8.006  10.508  1 20.353  ? 338  ASN B CG    1 
ATOM   6742 O  OD1   . ASN B 1 346 ? -32.387 -7.077  10.245  1 19.994  ? 338  ASN B OD1   1 
ATOM   6743 N  ND2   . ASN B 1 346 ? -34.145 -7.879  11.401  1 18.357  ? 338  ASN B ND2   1 
ATOM   6744 N  N     . ALA B 1 347 ? -29.675 -8.444  8.979   1 21.957  ? 339  ALA B N     1 
ATOM   6745 C  CA    . ALA B 1 347 ? -28.378 -8.145  9.585   1 22.142  ? 339  ALA B CA    1 
ATOM   6746 C  C     . ALA B 1 347 ? -28.479 -7.27   10.843  1 21.732  ? 339  ALA B C     1 
ATOM   6747 O  O     . ALA B 1 347 ? -27.489 -7.179  11.589  1 23.545  ? 339  ALA B O     1 
ATOM   6748 C  CB    . ALA B 1 347 ? -27.429 -7.572  8.552   1 22.349  ? 339  ALA B CB    1 
ATOM   6749 N  N     . PHE B 1 348 ? -29.672 -6.691  11.107  1 20.492  ? 340  PHE B N     1 
ATOM   6750 C  CA    . PHE B 1 348 ? -30.031 -5.969  12.331  1 19.684  ? 340  PHE B CA    1 
ATOM   6751 C  C     . PHE B 1 348 ? -31.139 -6.717  13.099  1 20.155  ? 340  PHE B C     1 
ATOM   6752 O  O     . PHE B 1 348 ? -32.255 -6.164  13.192  1 20.221  ? 340  PHE B O     1 
ATOM   6753 C  CB    . PHE B 1 348 ? -30.416 -4.547  11.891  1 18.814  ? 340  PHE B CB    1 
ATOM   6754 C  CG    . PHE B 1 348 ? -29.388 -3.465  11.604  1 18.117  ? 340  PHE B CG    1 
ATOM   6755 C  CD1   . PHE B 1 348 ? -28.001 -3.727  11.521  1 18.129  ? 340  PHE B CD1   1 
ATOM   6756 C  CD2   . PHE B 1 348 ? -29.835 -2.153  11.374  1 18.572  ? 340  PHE B CD2   1 
ATOM   6757 C  CE1   . PHE B 1 348 ? -27.091 -2.693  11.26   1 18.259  ? 340  PHE B CE1   1 
ATOM   6758 C  CE2   . PHE B 1 348 ? -28.925 -1.117  11.113  1 17.972  ? 340  PHE B CE2   1 
ATOM   6759 C  CZ    . PHE B 1 348 ? -27.552 -1.391  11.05   1 17.844  ? 340  PHE B CZ    1 
ATOM   6760 N  N     . PRO B 1 349 ? -30.914 -7.947  13.694  1 20.398  ? 341  PRO B N     1 
ATOM   6761 C  CA    . PRO B 1 349 ? -31.976 -8.694  14.382  1 20.288  ? 341  PRO B CA    1 
ATOM   6762 C  C     . PRO B 1 349 ? -32.66  -7.997  15.569  1 20.156  ? 341  PRO B C     1 
ATOM   6763 O  O     . PRO B 1 349 ? -33.798 -8.332  15.904  1 21.041  ? 341  PRO B O     1 
ATOM   6764 C  CB    . PRO B 1 349 ? -31.34  -10.056 14.715  1 21.65   ? 341  PRO B CB    1 
ATOM   6765 C  CG    . PRO B 1 349 ? -29.873 -9.702  14.875  1 20.772  ? 341  PRO B CG    1 
ATOM   6766 C  CD    . PRO B 1 349 ? -29.642 -8.708  13.768  1 18.989  ? 341  PRO B CD    1 
ATOM   6767 N  N     . PHE B 1 350 ? -31.994 -6.973  16.13   1 21.195  ? 342  PHE B N     1 
ATOM   6768 C  CA    . PHE B 1 350 ? -32.463 -6.086  17.197  1 21.037  ? 342  PHE B CA    1 
ATOM   6769 C  C     . PHE B 1 350 ? -33.634 -5.193  16.749  1 21.867  ? 342  PHE B C     1 
ATOM   6770 O  O     . PHE B 1 350 ? -34.299 -4.613  17.612  1 22.313  ? 342  PHE B O     1 
ATOM   6771 C  CB    . PHE B 1 350 ? -31.279 -5.362  17.861  1 19.658  ? 342  PHE B CB    1 
ATOM   6772 C  CG    . PHE B 1 350 ? -30.346 -4.651  16.884  1 18.87   ? 342  PHE B CG    1 
ATOM   6773 C  CD1   . PHE B 1 350 ? -30.678 -3.391  16.347  1 18.121  ? 342  PHE B CD1   1 
ATOM   6774 C  CD2   . PHE B 1 350 ? -29.165 -5.28   16.454  1 19.089  ? 342  PHE B CD2   1 
ATOM   6775 C  CE1   . PHE B 1 350 ? -29.858 -2.781  15.388  1 17.849  ? 342  PHE B CE1   1 
ATOM   6776 C  CE2   . PHE B 1 350 ? -28.342 -4.675  15.49   1 18.982  ? 342  PHE B CE2   1 
ATOM   6777 C  CZ    . PHE B 1 350 ? -28.676 -3.416  14.983  1 17.703  ? 342  PHE B CZ    1 
ATOM   6778 N  N     . PHE B 1 351 ? -33.893 -5.073  15.428  1 24.123  ? 343  PHE B N     1 
ATOM   6779 C  CA    . PHE B 1 351 ? -35.127 -4.507  14.882  1 21.858  ? 343  PHE B CA    1 
ATOM   6780 C  C     . PHE B 1 351 ? -35.958 -5.625  14.245  1 22.303  ? 343  PHE B C     1 
ATOM   6781 O  O     . PHE B 1 351 ? -36.043 -5.653  13.013  1 22.432  ? 343  PHE B O     1 
ATOM   6782 C  CB    . PHE B 1 351 ? -34.898 -3.244  14.033  1 21.201  ? 343  PHE B CB    1 
ATOM   6783 C  CG    . PHE B 1 351 ? -34.043 -2.123  14.624  1 22.497  ? 343  PHE B CG    1 
ATOM   6784 C  CD1   . PHE B 1 351 ? -34.134 -1.749  15.987  1 21.841  ? 343  PHE B CD1   1 
ATOM   6785 C  CD2   . PHE B 1 351 ? -33.155 -1.416  13.795  1 20.122  ? 343  PHE B CD2   1 
ATOM   6786 C  CE1   . PHE B 1 351 ? -33.341 -0.71   16.501  1 21.68   ? 343  PHE B CE1   1 
ATOM   6787 C  CE2   . PHE B 1 351 ? -32.38  -0.366  14.31   1 21.098  ? 343  PHE B CE2   1 
ATOM   6788 C  CZ    . PHE B 1 351 ? -32.462 -0.025  15.66   1 19.973  ? 343  PHE B CZ    1 
ATOM   6789 N  N     . PRO B 1 352 ? -36.625 -6.546  15.02   1 23.096  ? 344  PRO B N     1 
ATOM   6790 C  CA    . PRO B 1 352 ? -37.324 -7.694  14.437  1 22.543  ? 344  PRO B CA    1 
ATOM   6791 C  C     . PRO B 1 352 ? -38.587 -7.307  13.637  1 23.365  ? 344  PRO B C     1 
ATOM   6792 O  O     . PRO B 1 352 ? -38.986 -6.129  13.668  1 22.07   ? 344  PRO B O     1 
ATOM   6793 C  CB    . PRO B 1 352 ? -37.607 -8.567  15.676  1 21.451  ? 344  PRO B CB    1 
ATOM   6794 C  CG    . PRO B 1 352 ? -37.898 -7.534  16.753  1 19.414  ? 344  PRO B CG    1 
ATOM   6795 C  CD    . PRO B 1 352 ? -36.824 -6.523  16.495  1 21.756  ? 344  PRO B CD    1 
ATOM   6796 N  N     . PRO B 1 353 ? -39.28  -8.26   12.938  1 26.846  ? 345  PRO B N     1 
ATOM   6797 C  CA    . PRO B 1 353 ? -40.662 -8.031  12.5    1 27.814  ? 345  PRO B CA    1 
ATOM   6798 C  C     . PRO B 1 353 ? -41.669 -7.776  13.622  1 32.128  ? 345  PRO B C     1 
ATOM   6799 O  O     . PRO B 1 353 ? -41.42  -8.174  14.763  1 35.778  ? 345  PRO B O     1 
ATOM   6800 C  CB    . PRO B 1 353 ? -40.976 -9.244  11.659  1 26.213  ? 345  PRO B CB    1 
ATOM   6801 C  CG    . PRO B 1 353 ? -39.648 -9.88   11.307  1 25.541  ? 345  PRO B CG    1 
ATOM   6802 C  CD    . PRO B 1 353 ? -38.775 -9.571  12.463  1 24.295  ? 345  PRO B CD    1 
ATOM   6803 N  N     . ASP B 1 354 ? -42.774 -7.09   13.267  1 34.025  ? 346  ASP B N     1 
ATOM   6804 C  CA    . ASP B 1 354 ? -43.9   -6.75   14.135  1 37.438  ? 346  ASP B CA    1 
ATOM   6805 C  C     . ASP B 1 354 ? -44.583 -7.983  14.732  1 37.123  ? 346  ASP B C     1 
ATOM   6806 O  O     . ASP B 1 354 ? -44.658 -8.082  15.956  1 41.643  ? 346  ASP B O     1 
ATOM   6807 C  CB    . ASP B 1 354 ? -44.957 -5.892  13.452  1 42.397  ? 346  ASP B CB    1 
ATOM   6808 C  CG    . ASP B 1 354 ? -44.997 -4.412  13.804  1 45.695  ? 346  ASP B CG    1 
ATOM   6809 O  OD1   . ASP B 1 354 ? -45.111 -4.072  15.005  1 43.245  ? 346  ASP B OD1   1 
ATOM   6810 O  OD2   . ASP B 1 354 ? -45.009 -3.618  12.853  1 51.923  ? 346  ASP B OD2   1 
ATOM   6811 N  N     . SER B 1 355 ? -45.07  -8.888  13.866  1 36.345  ? 347  SER B N     1 
ATOM   6812 C  CA    . SER B 1 355 ? -45.884 -10.036 14.245  1 36.126  ? 347  SER B CA    1 
ATOM   6813 C  C     . SER B 1 355 ? -45.017 -11.14  14.849  1 39.551  ? 347  SER B C     1 
ATOM   6814 O  O     . SER B 1 355 ? -43.83  -11.266 14.511  1 35.151  ? 347  SER B O     1 
ATOM   6815 C  CB    . SER B 1 355 ? -46.717 -10.529 13.093  1 33.073  ? 347  SER B CB    1 
ATOM   6816 O  OG    . SER B 1 355 ? -45.917 -11.099 12.067  1 30.673  ? 347  SER B OG    1 
ATOM   6817 N  N     . ASP B 1 356 ? -45.66  -11.938 15.728  1 44.404  ? 348  ASP B N     1 
ATOM   6818 C  CA    . ASP B 1 356 ? -45.104 -13.117 16.386  1 46.881  ? 348  ASP B CA    1 
ATOM   6819 C  C     . ASP B 1 356 ? -44.644 -14.155 15.368  1 41.247  ? 348  ASP B C     1 
ATOM   6820 O  O     . ASP B 1 356 ? -43.57  -14.72  15.535  1 41.46   ? 348  ASP B O     1 
ATOM   6821 C  CB    . ASP B 1 356 ? -46.057 -13.68  17.429  1 55.697  ? 348  ASP B CB    1 
ATOM   6822 C  CG    . ASP B 1 356 ? -46.327 -12.809 18.649  1 71.018  ? 348  ASP B CG    1 
ATOM   6823 O  OD1   . ASP B 1 356 ? -45.479 -11.95  19.001  1 79.715  ? 348  ASP B OD1   1 
ATOM   6824 O  OD2   . ASP B 1 356 ? -47.404 -12.988 19.244  1 80.852  ? 348  ASP B OD2   1 
ATOM   6825 N  N     . GLU B 1 357 ? -45.46  -14.336 14.32   1 38.72   ? 349  GLU B N     1 
ATOM   6826 C  CA    . GLU B 1 357 ? -45.249 -15.195 13.166  1 38.993  ? 349  GLU B CA    1 
ATOM   6827 C  C     . GLU B 1 357 ? -43.958 -14.836 12.424  1 30.797  ? 349  GLU B C     1 
ATOM   6828 O  O     . GLU B 1 357 ? -43.151 -15.726 12.196  1 28.637  ? 349  GLU B O     1 
ATOM   6829 C  CB    . GLU B 1 357 ? -46.566 -15.03  12.415  1 50.663  ? 349  GLU B CB    1 
ATOM   6830 C  CG    . GLU B 1 357 ? -46.673 -15.769 11.087  1 69.077  ? 349  GLU B CG    1 
ATOM   6831 C  CD    . GLU B 1 357 ? -47.965 -15.305 10.451  1 76.571  ? 349  GLU B CD    1 
ATOM   6832 O  OE1   . GLU B 1 357 ? -49.028 -15.861 10.815  1 80.603  ? 349  GLU B OE1   1 
ATOM   6833 O  OE2   . GLU B 1 357 ? -47.894 -14.385 9.596   1 75.309  ? 349  GLU B OE2   1 
ATOM   6834 N  N     . GLN B 1 358 ? -43.795 -13.555 12.051  1 30.195  ? 350  GLN B N     1 
ATOM   6835 C  CA    . GLN B 1 358 ? -42.666 -13.037 11.276  1 30.276  ? 350  GLN B CA    1 
ATOM   6836 C  C     . GLN B 1 358 ? -41.381 -13.037 12.12   1 28.612  ? 350  GLN B C     1 
ATOM   6837 O  O     . GLN B 1 358 ? -40.301 -13.302 11.577  1 28.318  ? 350  GLN B O     1 
ATOM   6838 C  CB    . GLN B 1 358 ? -43.03  -11.705 10.614  1 32.737  ? 350  GLN B CB    1 
ATOM   6839 C  CG    . GLN B 1 358 ? -43.295 -11.704 9.107   1 40.112  ? 350  GLN B CG    1 
ATOM   6840 C  CD    . GLN B 1 358 ? -42.977 -10.383 8.411   1 46.114  ? 350  GLN B CD    1 
ATOM   6841 O  OE1   . GLN B 1 358 ? -41.828 -10.061 8.067   1 44.8    ? 350  GLN B OE1   1 
ATOM   6842 N  NE2   . GLN B 1 358 ? -44.01  -9.596  8.141   1 46.55   ? 350  GLN B NE2   1 
ATOM   6843 N  N     . LYS B 1 359 ? -41.514 -12.76  13.435  1 29.816  ? 351  LYS B N     1 
ATOM   6844 C  CA    . LYS B 1 359 ? -40.462 -12.911 14.446  1 31.057  ? 351  LYS B CA    1 
ATOM   6845 C  C     . LYS B 1 359 ? -39.902 -14.332 14.461  1 29.041  ? 351  LYS B C     1 
ATOM   6846 O  O     . LYS B 1 359 ? -38.687 -14.474 14.468  1 31.409  ? 351  LYS B O     1 
ATOM   6847 C  CB    . LYS B 1 359 ? -40.863 -12.499 15.867  1 34.062  ? 351  LYS B CB    1 
ATOM   6848 C  CG    . LYS B 1 359 ? -40.543 -11.072 16.253  1 44.972  ? 351  LYS B CG    1 
ATOM   6849 C  CD    . LYS B 1 359 ? -40.878 -10.74  17.707  1 50.546  ? 351  LYS B CD    1 
ATOM   6850 C  CE    . LYS B 1 359 ? -41.025 -9.27   18.041  1 54.301  ? 351  LYS B CE    1 
ATOM   6851 N  NZ    . LYS B 1 359 ? -42.273 -8.653  17.576  1 55.914  ? 351  LYS B NZ    1 
ATOM   6852 N  N     . LYS B 1 360 ? -40.787 -15.347 14.429  1 27.448  ? 352  LYS B N     1 
ATOM   6853 C  CA    . LYS B 1 360 ? -40.425 -16.762 14.438  1 31.236  ? 352  LYS B CA    1 
ATOM   6854 C  C     . LYS B 1 360 ? -39.689 -17.161 13.161  1 28.914  ? 352  LYS B C     1 
ATOM   6855 O  O     . LYS B 1 360 ? -38.799 -18.002 13.24   1 28.858  ? 352  LYS B O     1 
ATOM   6856 C  CB    . LYS B 1 360 ? -41.581 -17.707 14.777  1 35.869  ? 352  LYS B CB    1 
ATOM   6857 C  CG    . LYS B 1 360 ? -42.046 -17.641 16.238  1 38.008  ? 352  LYS B CG    1 
ATOM   6858 C  CD    . LYS B 1 360 ? -42.914 -18.753 16.827  1 44.579  ? 352  LYS B CD    1 
ATOM   6859 C  CE    . LYS B 1 360 ? -44.238 -19.134 16.205  1 54.444  ? 352  LYS B CE    1 
ATOM   6860 N  NZ    . LYS B 1 360 ? -45.247 -18.067 16.172  1 66.444  ? 352  LYS B NZ    1 
ATOM   6861 N  N     . LYS B 1 361 ? -40.048 -16.532 12.022  1 27.421  ? 353  LYS B N     1 
ATOM   6862 C  CA    . LYS B 1 361 ? -39.358 -16.657 10.742  1 29.855  ? 353  LYS B CA    1 
ATOM   6863 C  C     . LYS B 1 361 ? -37.886 -16.212 10.843  1 29.652  ? 353  LYS B C     1 
ATOM   6864 O  O     . LYS B 1 361 ? -37.009 -16.95  10.373  1 30.42   ? 353  LYS B O     1 
ATOM   6865 C  CB    . LYS B 1 361 ? -40.273 -16.085 9.649   1 32.383  ? 353  LYS B CB    1 
ATOM   6866 C  CG    . LYS B 1 361 ? -39.907 -16.164 8.16    1 36.09   ? 353  LYS B CG    1 
ATOM   6867 C  CD    . LYS B 1 361 ? -41.156 -16.011 7.279   1 39.204  ? 353  LYS B CD    1 
ATOM   6868 C  CE    . LYS B 1 361 ? -41.016 -15.479 5.867   1 44.153  ? 353  LYS B CE    1 
ATOM   6869 N  NZ    . LYS B 1 361 ? -40.266 -16.337 4.942   1 47.368  ? 353  LYS B NZ    1 
ATOM   6870 N  N     . GLN B 1 362 ? -37.628 -15.055 11.493  1 27.912  ? 354  GLN B N     1 
ATOM   6871 C  CA    . GLN B 1 362 ? -36.294 -14.5   11.75   1 27.615  ? 354  GLN B CA    1 
ATOM   6872 C  C     . GLN B 1 362 ? -35.451 -15.471 12.583  1 27.473  ? 354  GLN B C     1 
ATOM   6873 O  O     . GLN B 1 362 ? -34.308 -15.744 12.203  1 26.034  ? 354  GLN B O     1 
ATOM   6874 C  CB    . GLN B 1 362 ? -36.32  -13.06  12.282  1 25.328  ? 354  GLN B CB    1 
ATOM   6875 C  CG    . GLN B 1 362 ? -34.953 -12.414 12.512  1 24.589  ? 354  GLN B CG    1 
ATOM   6876 C  CD    . GLN B 1 362 ? -35.048 -11.017 13.09   1 23.812  ? 354  GLN B CD    1 
ATOM   6877 O  OE1   . GLN B 1 362 ? -35.446 -10.072 12.407  1 26.157  ? 354  GLN B OE1   1 
ATOM   6878 N  NE2   . GLN B 1 362 ? -34.706 -10.861 14.358  1 24.404  ? 354  GLN B NE2   1 
ATOM   6879 N  N     . GLU B 1 363 ? -36.041 -15.974 13.685  1 28.379  ? 355  GLU B N     1 
ATOM   6880 C  CA    . GLU B 1 363 ? -35.458 -16.979 14.576  1 32.482  ? 355  GLU B CA    1 
ATOM   6881 C  C     . GLU B 1 363 ? -35.027 -18.225 13.794  1 30.002  ? 355  GLU B C     1 
ATOM   6882 O  O     . GLU B 1 363 ? -33.885 -18.66  13.954  1 32.688  ? 355  GLU B O     1 
ATOM   6883 C  CB    . GLU B 1 363 ? -36.359 -17.364 15.757  1 38.322  ? 355  GLU B CB    1 
ATOM   6884 C  CG    . GLU B 1 363 ? -36.692 -16.246 16.744  1 51.509  ? 355  GLU B CG    1 
ATOM   6885 C  CD    . GLU B 1 363 ? -35.596 -15.523 17.516  1 57.721  ? 355  GLU B CD    1 
ATOM   6886 O  OE1   . GLU B 1 363 ? -35.134 -16.027 18.563  1 60.105  ? 355  GLU B OE1   1 
ATOM   6887 O  OE2   . GLU B 1 363 ? -35.186 -14.445 17.034  1 60.194  ? 355  GLU B OE2   1 
ATOM   6888 N  N     . ALA B 1 364 ? -35.912 -18.714 12.899  1 26.645  ? 356  ALA B N     1 
ATOM   6889 C  CA    . ALA B 1 364 ? -35.725 -19.922 12.102  1 27.346  ? 356  ALA B CA    1 
ATOM   6890 C  C     . ALA B 1 364 ? -34.699 -19.757 10.968  1 28.55   ? 356  ALA B C     1 
ATOM   6891 O  O     . ALA B 1 364 ? -34.345 -20.752 10.323  1 31.49   ? 356  ALA B O     1 
ATOM   6892 C  CB    . ALA B 1 364 ? -37.079 -20.506 11.656  1 25.637  ? 356  ALA B CB    1 
ATOM   6893 N  N     . ASP B 1 365 ? -34.227 -18.522 10.716  1 28.669  ? 357  ASP B N     1 
ATOM   6894 C  CA    . ASP B 1 365 ? -33.251 -18.189 9.68    1 32.633  ? 357  ASP B CA    1 
ATOM   6895 C  C     . ASP B 1 365 ? -31.804 -18.225 10.184  1 34.325  ? 357  ASP B C     1 
ATOM   6896 O  O     . ASP B 1 365 ? -30.899 -18.375 9.347   1 37.369  ? 357  ASP B O     1 
ATOM   6897 C  CB    . ASP B 1 365 ? -33.673 -16.968 8.873   1 31.407  ? 357  ASP B CB    1 
ATOM   6898 C  CG    . ASP B 1 365 ? -34.763 -17.157 7.818   1 32.841  ? 357  ASP B CG    1 
ATOM   6899 O  OD1   . ASP B 1 365 ? -35.208 -18.319 7.567   1 32.449  ? 357  ASP B OD1   1 
ATOM   6900 O  OD2   . ASP B 1 365 ? -35.155 -16.117 7.226   1 31.62   ? 357  ASP B OD2   1 
ATOM   6901 N  N     . GLY B 1 366 ? -31.613 -18.106 11.518  1 33.403  ? 358  GLY B N     1 
ATOM   6902 C  CA    . GLY B 1 366 ? -30.328 -18.101 12.212  1 31.82   ? 358  GLY B CA    1 
ATOM   6903 C  C     . GLY B 1 366 ? -29.414 -16.987 11.694  1 34.735  ? 358  GLY B C     1 
ATOM   6904 O  O     . GLY B 1 366 ? -29.862 -15.843 11.52   1 38.086  ? 358  GLY B O     1 
ATOM   6905 N  N     . THR B 1 367 ? -28.159 -17.362 11.419  1 32.353  ? 359  THR B N     1 
ATOM   6906 C  CA    . THR B 1 367 ? -27.187 -16.496 10.769  1 31.41   ? 359  THR B CA    1 
ATOM   6907 C  C     . THR B 1 367 ? -27.43  -16.593 9.259   1 29.608  ? 359  THR B C     1 
ATOM   6908 O  O     . THR B 1 367 ? -27.111 -17.651 8.714   1 26.632  ? 359  THR B O     1 
ATOM   6909 C  CB    . THR B 1 367 ? -25.74  -16.805 11.178  1 33.46   ? 359  THR B CB    1 
ATOM   6910 O  OG1   . THR B 1 367 ? -25.659 -16.652 12.596  1 33.596  ? 359  THR B OG1   1 
ATOM   6911 C  CG2   . THR B 1 367 ? -24.724 -15.859 10.549  1 32.56   ? 359  THR B CG2   1 
ATOM   6912 N  N     . PRO B 1 368 ? -27.926 -15.528 8.549   1 26.562  ? 360  PRO B N     1 
ATOM   6913 C  CA    . PRO B 1 368 ? -28.125 -15.58  7.102   1 26.059  ? 360  PRO B CA    1 
ATOM   6914 C  C     . PRO B 1 368 ? -26.816 -15.647 6.322   1 26.781  ? 360  PRO B C     1 
ATOM   6915 O  O     . PRO B 1 368 ? -25.77  -15.266 6.846   1 29.485  ? 360  PRO B O     1 
ATOM   6916 C  CB    . PRO B 1 368 ? -28.92  -14.316 6.774   1 26.268  ? 360  PRO B CB    1 
ATOM   6917 C  CG    . PRO B 1 368 ? -29.276 -13.666 8.097   1 25.122  ? 360  PRO B CG    1 
ATOM   6918 C  CD    . PRO B 1 368 ? -28.228 -14.176 9.055   1 27.664  ? 360  PRO B CD    1 
ATOM   6919 N  N     . LYS B 1 369 ? -26.891 -16.194 5.096   1 26.169  ? 361  LYS B N     1 
ATOM   6920 C  CA    . LYS B 1 369 ? -25.833 -16.187 4.096   1 27.962  ? 361  LYS B CA    1 
ATOM   6921 C  C     . LYS B 1 369 ? -25.462 -14.736 3.793   1 25.926  ? 361  LYS B C     1 
ATOM   6922 O  O     . LYS B 1 369 ? -26.344 -13.879 3.717   1 26.473  ? 361  LYS B O     1 
ATOM   6923 C  CB    . LYS B 1 369 ? -26.404 -16.895 2.867   1 29.548  ? 361  LYS B CB    1 
ATOM   6924 C  CG    . LYS B 1 369 ? -25.478 -17.238 1.72    1 37.693  ? 361  LYS B CG    1 
ATOM   6925 C  CD    . LYS B 1 369 ? -26.47  -17.368 0.567   1 44.228  ? 361  LYS B CD    1 
ATOM   6926 C  CE    . LYS B 1 369 ? -26.127 -18.271 -0.568  1 47.945  ? 361  LYS B CE    1 
ATOM   6927 N  NZ    . LYS B 1 369 ? -27.321 -18.379 -1.44   1 51.582  ? 361  LYS B NZ    1 
ATOM   6928 N  N     . ALA B 1 370 ? -24.152 -14.49  3.664   1 24.98   ? 362  ALA B N     1 
ATOM   6929 C  CA    . ALA B 1 370 ? -23.583 -13.161 3.475   1 24.278  ? 362  ALA B CA    1 
ATOM   6930 C  C     . ALA B 1 370 ? -22.496 -13.202 2.408   1 24.482  ? 362  ALA B C     1 
ATOM   6931 O  O     . ALA B 1 370 ? -21.554 -13.989 2.506   1 26.752  ? 362  ALA B O     1 
ATOM   6932 C  CB    . ALA B 1 370 ? -23.101 -12.582 4.787   1 25.292  ? 362  ALA B CB    1 
ATOM   6933 N  N     . GLN B 1 371 ? -22.675 -12.335 1.396   1 22.818  ? 363  GLN B N     1 
ATOM   6934 C  CA    . GLN B 1 371 ? -21.894 -12.287 0.162   1 23.758  ? 363  GLN B CA    1 
ATOM   6935 C  C     . GLN B 1 371 ? -21.623 -10.832 -0.228  1 23.819  ? 363  GLN B C     1 
ATOM   6936 O  O     . GLN B 1 371 ? -22.193 -9.917  0.368   1 24.011  ? 363  GLN B O     1 
ATOM   6937 C  CB    . GLN B 1 371 ? -22.614 -13.003 -0.988  1 23.654  ? 363  GLN B CB    1 
ATOM   6938 C  CG    . GLN B 1 371 ? -22.875 -14.493 -0.773  1 27.824  ? 363  GLN B CG    1 
ATOM   6939 C  CD    . GLN B 1 371 ? -23.888 -15.093 -1.726  1 30.784  ? 363  GLN B CD    1 
ATOM   6940 O  OE1   . GLN B 1 371 ? -24.889 -14.467 -2.111  1 31.717  ? 363  GLN B OE1   1 
ATOM   6941 N  NE2   . GLN B 1 371 ? -23.612 -16.325 -2.125  1 30.131  ? 363  GLN B NE2   1 
ATOM   6942 N  N     . PHE B 1 372 ? -20.722 -10.664 -1.215  1 22.707  ? 364  PHE B N     1 
ATOM   6943 C  CA    . PHE B 1 372 ? -20.507 -9.465  -2.008  1 22.641  ? 364  PHE B CA    1 
ATOM   6944 C  C     . PHE B 1 372 ? -20.992 -9.723  -3.435  1 21.608  ? 364  PHE B C     1 
ATOM   6945 O  O     . PHE B 1 372 ? -20.622 -10.741 -4.028  1 23.576  ? 364  PHE B O     1 
ATOM   6946 C  CB    . PHE B 1 372 ? -19.022 -9.103  -1.904  1 20.462  ? 364  PHE B CB    1 
ATOM   6947 C  CG    . PHE B 1 372 ? -18.657 -7.734  -2.462  1 21.315  ? 364  PHE B CG    1 
ATOM   6948 C  CD1   . PHE B 1 372 ? -18.987 -6.564  -1.755  1 21.909  ? 364  PHE B CD1   1 
ATOM   6949 C  CD2   . PHE B 1 372 ? -18.005 -7.617  -3.7    1 20.809  ? 364  PHE B CD2   1 
ATOM   6950 C  CE1   . PHE B 1 372 ? -18.664 -5.308  -2.269  1 22.354  ? 364  PHE B CE1   1 
ATOM   6951 C  CE2   . PHE B 1 372 ? -17.661 -6.366  -4.212  1 20.958  ? 364  PHE B CE2   1 
ATOM   6952 C  CZ    . PHE B 1 372 ? -17.981 -5.217  -3.486  1 24.094  ? 364  PHE B CZ    1 
ATOM   6953 N  N     . VAL B 1 373 ? -21.84  -8.809  -3.953  1 21.825  ? 365  VAL B N     1 
ATOM   6954 C  CA    . VAL B 1 373 ? -22.706 -9.052  -5.109  1 20.737  ? 365  VAL B CA    1 
ATOM   6955 C  C     . VAL B 1 373 ? -22.683 -7.854  -6.064  1 23.892  ? 365  VAL B C     1 
ATOM   6956 O  O     . VAL B 1 373 ? -22.405 -6.742  -5.622  1 22.696  ? 365  VAL B O     1 
ATOM   6957 C  CB    . VAL B 1 373 ? -24.151 -9.536  -4.809  1 20.112  ? 365  VAL B CB    1 
ATOM   6958 C  CG1   . VAL B 1 373 ? -24.202 -10.825 -3.982  1 19.597  ? 365  VAL B CG1   1 
ATOM   6959 C  CG2   . VAL B 1 373 ? -25.061 -8.455  -4.208  1 18.437  ? 365  VAL B CG2   1 
ATOM   6960 N  N     . ARG B 1 374 ? -23.056 -8.105  -7.339  1 23.715  ? 366  ARG B N     1 
ATOM   6961 C  CA    . ARG B 1 374 ? -23.167 -7.133  -8.423  1 25.174  ? 366  ARG B CA    1 
ATOM   6962 C  C     . ARG B 1 374 ? -24.6   -7.086  -8.961  1 25.536  ? 366  ARG B C     1 
ATOM   6963 O  O     . ARG B 1 374 ? -25.092 -8.089  -9.478  1 25.191  ? 366  ARG B O     1 
ATOM   6964 C  CB    . ARG B 1 374 ? -22.148 -7.452  -9.529  1 23.506  ? 366  ARG B CB    1 
ATOM   6965 C  CG    . ARG B 1 374 ? -22.202 -6.518  -10.732 1 22.622  ? 366  ARG B CG    1 
ATOM   6966 C  CD    . ARG B 1 374 ? -20.974 -6.6    -11.596 1 21.935  ? 366  ARG B CD    1 
ATOM   6967 N  NE    . ARG B 1 374 ? -19.757 -6.218  -10.855 1 24.991  ? 366  ARG B NE    1 
ATOM   6968 C  CZ    . ARG B 1 374 ? -18.564 -6.821  -10.885 1 25.687  ? 366  ARG B CZ    1 
ATOM   6969 N  NH1   . ARG B 1 374 ? -18.248 -7.681  -11.841 1 23.419  ? 366  ARG B NH1   1 
ATOM   6970 N  NH2   . ARG B 1 374 ? -17.648 -6.506  -9.986  1 24.63   ? 366  ARG B NH2   1 
ATOM   6971 N  N     . TRP B 1 375 ? -25.182 -5.876  -8.909  1 25.795  ? 367  TRP B N     1 
ATOM   6972 C  CA    . TRP B 1 375 ? -26.517 -5.513  -9.39   1 27.147  ? 367  TRP B CA    1 
ATOM   6973 C  C     . TRP B 1 375 ? -26.419 -4.893  -10.786 1 28.642  ? 367  TRP B C     1 
ATOM   6974 O  O     . TRP B 1 375 ? -25.449 -4.176  -11.061 1 26.487  ? 367  TRP B O     1 
ATOM   6975 C  CB    . TRP B 1 375 ? -27.207 -4.533  -8.422  1 26.276  ? 367  TRP B CB    1 
ATOM   6976 C  CG    . TRP B 1 375 ? -27.285 -5.006  -6.993  1 28.406  ? 367  TRP B CG    1 
ATOM   6977 C  CD1   . TRP B 1 375 ? -26.386 -4.715  -6.005  1 28.763  ? 367  TRP B CD1   1 
ATOM   6978 C  CD2   . TRP B 1 375 ? -28.289 -5.854  -6.383  1 28.465  ? 367  TRP B CD2   1 
ATOM   6979 N  NE1   . TRP B 1 375 ? -26.745 -5.32   -4.829  1 28.303  ? 367  TRP B NE1   1 
ATOM   6980 C  CE2   . TRP B 1 375 ? -27.908 -6.021  -5.018  1 28.126  ? 367  TRP B CE2   1 
ATOM   6981 C  CE3   . TRP B 1 375 ? -29.464 -6.49   -6.837  1 28.837  ? 367  TRP B CE3   1 
ATOM   6982 C  CZ2   . TRP B 1 375 ? -28.659 -6.787  -4.113  1 25.803  ? 367  TRP B CZ2   1 
ATOM   6983 C  CZ3   . TRP B 1 375 ? -30.205 -7.247  -5.936  1 27.541  ? 367  TRP B CZ3   1 
ATOM   6984 C  CH2   . TRP B 1 375 ? -29.806 -7.397  -4.595  1 26.949  ? 367  TRP B CH2   1 
ATOM   6985 N  N     . THR B 1 376 ? -27.423 -5.197  -11.642 1 26.773  ? 368  THR B N     1 
ATOM   6986 C  CA    . THR B 1 376 ? -27.606 -4.605  -12.966 1 25.985  ? 368  THR B CA    1 
ATOM   6987 C  C     . THR B 1 376 ? -29.012 -4.003  -13.035 1 26.448  ? 368  THR B C     1 
ATOM   6988 O  O     . THR B 1 376 ? -30.008 -4.737  -12.983 1 25.249  ? 368  THR B O     1 
ATOM   6989 C  CB    . THR B 1 376 ? -27.316 -5.591  -14.111 1 27.648  ? 368  THR B CB    1 
ATOM   6990 O  OG1   . THR B 1 376 ? -26.01  -6.134  -13.946 1 26.903  ? 368  THR B OG1   1 
ATOM   6991 C  CG2   . THR B 1 376 ? -27.348 -4.966  -15.501 1 25.935  ? 368  THR B CG2   1 
ATOM   6992 N  N     . ILE B 1 377 ? -29.052 -2.665  -13.171 1 24.975  ? 369  ILE B N     1 
ATOM   6993 C  CA    . ILE B 1 377 ? -30.271 -1.885  -13.363 1 25.445  ? 369  ILE B CA    1 
ATOM   6994 C  C     . ILE B 1 377 ? -30.179 -1.214  -14.736 1 25.409  ? 369  ILE B C     1 
ATOM   6995 O  O     . ILE B 1 377 ? -29.488 -0.206  -14.884 1 26.739  ? 369  ILE B O     1 
ATOM   6996 C  CB    . ILE B 1 377 ? -30.569 -0.92   -12.182 1 25.665  ? 369  ILE B CB    1 
ATOM   6997 C  CG1   . ILE B 1 377 ? -30.613 -1.659  -10.807 1 25.333  ? 369  ILE B CG1   1 
ATOM   6998 C  CG2   . ILE B 1 377 ? -31.846 -0.09   -12.43  1 26.712  ? 369  ILE B CG2   1 
ATOM   6999 C  CD1   . ILE B 1 377 ? -30.437 -0.775  -9.575  1 24.836  ? 369  ILE B CD1   1 
ATOM   7000 N  N     . ASP B 1 378 ? -30.878 -1.804  -15.719 1 28.313  ? 370  ASP B N     1 
ATOM   7001 C  CA    . ASP B 1 378 ? -31.006 -1.258  -17.065 1 28.439  ? 370  ASP B CA    1 
ATOM   7002 C  C     . ASP B 1 378 ? -32.149 -0.236  -17.1   1 28.05   ? 370  ASP B C     1 
ATOM   7003 O  O     . ASP B 1 378 ? -33.31  -0.67   -17.166 1 27.662  ? 370  ASP B O     1 
ATOM   7004 C  CB    . ASP B 1 378 ? -31.111 -2.337  -18.143 1 29.921  ? 370  ASP B CB    1 
ATOM   7005 C  CG    . ASP B 1 378 ? -31.089 -1.891  -19.605 1 29.716  ? 370  ASP B CG    1 
ATOM   7006 O  OD1   . ASP B 1 378 ? -31.273 -0.682  -19.904 1 28.636  ? 370  ASP B OD1   1 
ATOM   7007 O  OD2   . ASP B 1 378 ? -30.84  -2.76   -20.456 1 30.33   ? 370  ASP B OD2   1 
ATOM   7008 N  N     . PRO B 1 379 ? -31.874 1.106   -17.192 1 29.153  ? 371  PRO B N     1 
ATOM   7009 C  CA    . PRO B 1 379 ? -32.927 2.132   -17.15  1 30.456  ? 371  PRO B CA    1 
ATOM   7010 C  C     . PRO B 1 379 ? -33.93  2.129   -18.32  1 31.582  ? 371  PRO B C     1 
ATOM   7011 O  O     . PRO B 1 379 ? -34.976 2.772   -18.217 1 35.685  ? 371  PRO B O     1 
ATOM   7012 C  CB    . PRO B 1 379 ? -32.192 3.447   -16.889 1 30.982  ? 371  PRO B CB    1 
ATOM   7013 C  CG    . PRO B 1 379 ? -30.859 3.191   -17.547 1 31.245  ? 371  PRO B CG    1 
ATOM   7014 C  CD    . PRO B 1 379 ? -30.548 1.727   -17.405 1 29.325  ? 371  PRO B CD    1 
ATOM   7015 N  N     . ARG B 1 380 ? -33.613 1.364   -19.378 1 31.917  ? 372  ARG B N     1 
ATOM   7016 C  CA    . ARG B 1 380 ? -34.381 1.186   -20.607 1 33.427  ? 372  ARG B CA    1 
ATOM   7017 C  C     . ARG B 1 380 ? -35.411 0.055   -20.501 1 33.83   ? 372  ARG B C     1 
ATOM   7018 O  O     . ARG B 1 380 ? -36.371 0.048   -21.275 1 31.645  ? 372  ARG B O     1 
ATOM   7019 C  CB    . ARG B 1 380 ? -33.466 0.988   -21.814 1 34.057  ? 372  ARG B CB    1 
ATOM   7020 C  CG    . ARG B 1 380 ? -32.492 2.133   -22.075 1 36.702  ? 372  ARG B CG    1 
ATOM   7021 C  CD    . ARG B 1 380 ? -31.84  2.11    -23.422 1 37.264  ? 372  ARG B CD    1 
ATOM   7022 N  NE    . ARG B 1 380 ? -31.081 0.885   -23.696 1 40.181  ? 372  ARG B NE    1 
ATOM   7023 C  CZ    . ARG B 1 380 ? -31.1   0.145   -24.803 1 48.42   ? 372  ARG B CZ    1 
ATOM   7024 N  NH1   . ARG B 1 380 ? -31.93  0.389   -25.817 1 50.095  ? 372  ARG B NH1   1 
ATOM   7025 N  NH2   . ARG B 1 380 ? -30.245 -0.859  -24.905 1 46.424  ? 372  ARG B NH2   1 
ATOM   7026 N  N     . LYS B 1 381 ? -35.229 -0.874  -19.54  1 31.278  ? 373  LYS B N     1 
ATOM   7027 C  CA    . LYS B 1 381 ? -36.214 -1.898  -19.198 1 31.369  ? 373  LYS B CA    1 
ATOM   7028 C  C     . LYS B 1 381 ? -37.403 -1.248  -18.477 1 32.204  ? 373  LYS B C     1 
ATOM   7029 O  O     . LYS B 1 381 ? -37.296 -0.122  -17.962 1 32.207  ? 373  LYS B O     1 
ATOM   7030 C  CB    . LYS B 1 381 ? -35.576 -3.064  -18.427 1 31.106  ? 373  LYS B CB    1 
ATOM   7031 C  CG    . LYS B 1 381 ? -34.621 -3.961  -19.219 1 32.167  ? 373  LYS B CG    1 
ATOM   7032 C  CD    . LYS B 1 381 ? -33.894 -5.087  -18.494 1 35.754  ? 373  LYS B CD    1 
ATOM   7033 C  CE    . LYS B 1 381 ? -34.684 -6.276  -18.028 1 40.108  ? 373  LYS B CE    1 
ATOM   7034 N  NZ    . LYS B 1 381 ? -35.134 -7.101  -19.149 1 45.966  ? 373  LYS B NZ    1 
ATOM   7035 N  N     . ASP B 1 382 ? -38.54  -1.969  -18.479 1 30.809  ? 374  ASP B N     1 
ATOM   7036 C  CA    . ASP B 1 382 ? -39.706 -1.709  -17.644 1 31.208  ? 374  ASP B CA    1 
ATOM   7037 C  C     . ASP B 1 382 ? -39.325 -1.974  -16.18  1 31.44   ? 374  ASP B C     1 
ATOM   7038 O  O     . ASP B 1 382 ? -38.908 -3.088  -15.833 1 31.519  ? 374  ASP B O     1 
ATOM   7039 C  CB    . ASP B 1 382 ? -40.891 -2.512  -18.168 1 33.309  ? 374  ASP B CB    1 
ATOM   7040 C  CG    . ASP B 1 382 ? -42.274 -2.318  -17.547 1 37.353  ? 374  ASP B CG    1 
ATOM   7041 O  OD1   . ASP B 1 382 ? -42.44  -1.529  -16.586 1 36.116  ? 374  ASP B OD1   1 
ATOM   7042 O  OD2   . ASP B 1 382 ? -43.194 -3.001  -18.019 1 40.4    ? 374  ASP B OD2   1 
ATOM   7043 N  N     . ASN B 1 383 ? -39.489 -0.927  -15.349 1 29.351  ? 375  ASN B N     1 
ATOM   7044 C  CA    . ASN B 1 383 ? -39.175 -0.903  -13.915 1 30.115  ? 375  ASN B CA    1 
ATOM   7045 C  C     . ASN B 1 383 ? -40.147 -1.746  -13.078 1 31.128  ? 375  ASN B C     1 
ATOM   7046 O  O     . ASN B 1 383 ? -39.817 -2.089  -11.944 1 28.153  ? 375  ASN B O     1 
ATOM   7047 C  CB    . ASN B 1 383 ? -38.941 0.524   -13.412 1 27.525  ? 375  ASN B CB    1 
ATOM   7048 C  CG    . ASN B 1 383 ? -40.209 1.352   -13.375 1 27.665  ? 375  ASN B CG    1 
ATOM   7049 O  OD1   . ASN B 1 383 ? -40.802 1.662   -14.418 1 25.211  ? 375  ASN B OD1   1 
ATOM   7050 N  ND2   . ASN B 1 383 ? -40.659 1.701   -12.177 1 25.908  ? 375  ASN B ND2   1 
ATOM   7051 N  N     . ASN B 1 384 ? -41.344 -2.049  -13.63  1 32.306  ? 376  ASN B N     1 
ATOM   7052 C  CA    . ASN B 1 384 ? -42.337 -2.912  -13.003 1 33.321  ? 376  ASN B CA    1 
ATOM   7053 C  C     . ASN B 1 384 ? -41.913 -4.377  -13.018 1 31.485  ? 376  ASN B C     1 
ATOM   7054 O  O     . ASN B 1 384 ? -42.387 -5.131  -12.168 1 31.233  ? 376  ASN B O     1 
ATOM   7055 C  CB    . ASN B 1 384 ? -43.766 -2.631  -13.467 1 36.885  ? 376  ASN B CB    1 
ATOM   7056 C  CG    . ASN B 1 384 ? -44.233 -1.217  -13.189 1 42.036  ? 376  ASN B CG    1 
ATOM   7057 O  OD1   . ASN B 1 384 ? -44.757 -0.555  -14.092 1 46.275  ? 376  ASN B OD1   1 
ATOM   7058 N  ND2   . ASN B 1 384 ? -44.099 -0.735  -11.959 1 44.257  ? 376  ASN B ND2   1 
ATOM   7059 N  N     . GLU B 1 385 ? -41.057 -4.768  -13.981 1 33.183  ? 377  GLU B N     1 
ATOM   7060 C  CA    . GLU B 1 385 ? -40.494 -6.109  -14.097 1 35.473  ? 377  GLU B CA    1 
ATOM   7061 C  C     . GLU B 1 385 ? -39.349 -6.256  -13.09  1 32.693  ? 377  GLU B C     1 
ATOM   7062 O  O     . GLU B 1 385 ? -38.479 -5.371  -13.023 1 28.497  ? 377  GLU B O     1 
ATOM   7063 C  CB    . GLU B 1 385 ? -40.083 -6.323  -15.553 1 40.87   ? 377  GLU B CB    1 
ATOM   7064 C  CG    . GLU B 1 385 ? -40.045 -7.792  -15.964 1 55.707  ? 377  GLU B CG    1 
ATOM   7065 C  CD    . GLU B 1 385 ? -39.363 -8.166  -17.272 1 64.637  ? 377  GLU B CD    1 
ATOM   7066 O  OE1   . GLU B 1 385 ? -39.987 -8.984  -17.985 1 70.544  ? 377  GLU B OE1   1 
ATOM   7067 O  OE2   . GLU B 1 385 ? -38.24  -7.689  -17.594 1 63.304  ? 377  GLU B OE2   1 
ATOM   7068 N  N     . GLN B 1 386 ? -39.383 -7.373  -12.327 1 28.523  ? 378  GLN B N     1 
ATOM   7069 C  CA    . GLN B 1 386 ? -38.365 -7.799  -11.368 1 28.238  ? 378  GLN B CA    1 
ATOM   7070 C  C     . GLN B 1 386 ? -36.973 -7.779  -12.009 1 26.71   ? 378  GLN B C     1 
ATOM   7071 O  O     . GLN B 1 386 ? -36.799 -8.267  -13.123 1 27.187  ? 378  GLN B O     1 
ATOM   7072 C  CB    . GLN B 1 386 ? -38.681 -9.177  -10.778 1 31.072  ? 378  GLN B CB    1 
ATOM   7073 C  CG    . GLN B 1 386 ? -37.815 -9.56   -9.577  1 32.308  ? 378  GLN B CG    1 
ATOM   7074 C  CD    . GLN B 1 386 ? -38.217 -10.861 -8.925  1 36.612  ? 378  GLN B CD    1 
ATOM   7075 O  OE1   . GLN B 1 386 ? -37.595 -11.906 -9.148  1 39.613  ? 378  GLN B OE1   1 
ATOM   7076 N  NE2   . GLN B 1 386 ? -39.272 -10.81  -8.122  1 36.195  ? 378  GLN B NE2   1 
ATOM   7077 N  N     . LEU B 1 387 ? -36.012 -7.174  -11.284 1 26.449  ? 379  LEU B N     1 
ATOM   7078 C  CA    . LEU B 1 387 ? -34.599 -7.089  -11.632 1 25.439  ? 379  LEU B CA    1 
ATOM   7079 C  C     . LEU B 1 387 ? -33.987 -8.487  -11.735 1 25.786  ? 379  LEU B C     1 
ATOM   7080 O  O     . LEU B 1 387 ? -34.419 -9.369  -10.978 1 24.082  ? 379  LEU B O     1 
ATOM   7081 C  CB    . LEU B 1 387 ? -33.815 -6.242  -10.627 1 23.868  ? 379  LEU B CB    1 
ATOM   7082 C  CG    . LEU B 1 387 ? -34.03  -4.726  -10.641 1 25.39   ? 379  LEU B CG    1 
ATOM   7083 C  CD1   . LEU B 1 387 ? -33.363 -4.149  -9.361  1 23.278  ? 379  LEU B CD1   1 
ATOM   7084 C  CD2   . LEU B 1 387 ? -33.547 -4.016  -11.923 1 22.886  ? 379  LEU B CD2   1 
ATOM   7085 N  N     . PRO B 1 388 ? -32.977 -8.737  -12.629 1 25.888  ? 380  PRO B N     1 
ATOM   7086 C  CA    . PRO B 1 388 ? -32.24  -10.002 -12.612 1 26.316  ? 380  PRO B CA    1 
ATOM   7087 C  C     . PRO B 1 388 ? -31.508 -10.219 -11.292 1 26.85   ? 380  PRO B C     1 
ATOM   7088 O  O     . PRO B 1 388 ? -31.106 -9.234  -10.656 1 26.555  ? 380  PRO B O     1 
ATOM   7089 C  CB    . PRO B 1 388 ? -31.32  -9.932  -13.83  1 25.262  ? 380  PRO B CB    1 
ATOM   7090 C  CG    . PRO B 1 388 ? -31.133 -8.429  -14.023 1 26.715  ? 380  PRO B CG    1 
ATOM   7091 C  CD    . PRO B 1 388 ? -32.477 -7.835  -13.694 1 27.362  ? 380  PRO B CD    1 
ATOM   7092 N  N     . ASP B 1 389 ? -31.404 -11.503 -10.893 1 28.834  ? 381  ASP B N     1 
ATOM   7093 C  CA    . ASP B 1 389 ? -30.679 -11.973 -9.716  1 28.284  ? 381  ASP B CA    1 
ATOM   7094 C  C     . ASP B 1 389 ? -29.258 -11.409 -9.732  1 26.98   ? 381  ASP B C     1 
ATOM   7095 O  O     . ASP B 1 389 ? -28.647 -11.435 -10.805 1 26.637  ? 381  ASP B O     1 
ATOM   7096 C  CB    . ASP B 1 389 ? -30.641 -13.496 -9.613  1 28.907  ? 381  ASP B CB    1 
ATOM   7097 C  CG    . ASP B 1 389 ? -31.944 -14.226 -9.308  1 31.215  ? 381  ASP B CG    1 
ATOM   7098 O  OD1   . ASP B 1 389 ? -32.948 -13.581 -8.965  1 31.57   ? 381  ASP B OD1   1 
ATOM   7099 O  OD2   . ASP B 1 389 ? -31.947 -15.463 -9.406  1 34.855  ? 381  ASP B OD2   1 
ATOM   7100 N  N     . PRO B 1 390 ? -28.704 -10.875 -8.599  1 25.674  ? 382  PRO B N     1 
ATOM   7101 C  CA    . PRO B 1 390 ? -27.346 -10.342 -8.598  1 24.451  ? 382  PRO B CA    1 
ATOM   7102 C  C     . PRO B 1 390 ? -26.287 -11.426 -8.813  1 25      ? 382  PRO B C     1 
ATOM   7103 O  O     . PRO B 1 390 ? -26.535 -12.591 -8.497  1 24.504  ? 382  PRO B O     1 
ATOM   7104 C  CB    . PRO B 1 390 ? -27.274 -9.536  -7.295  1 24.278  ? 382  PRO B CB    1 
ATOM   7105 C  CG    . PRO B 1 390 ? -28.18  -10.339 -6.377  1 26.151  ? 382  PRO B CG    1 
ATOM   7106 C  CD    . PRO B 1 390 ? -29.308 -10.808 -7.251  1 25.051  ? 382  PRO B CD    1 
ATOM   7107 N  N     . GLU B 1 391 ? -25.141 -11.025 -9.383  1 24.566  ? 383  GLU B N     1 
ATOM   7108 C  CA    . GLU B 1 391 ? -23.981 -11.896 -9.544  1 25.747  ? 383  GLU B CA    1 
ATOM   7109 C  C     . GLU B 1 391 ? -23.185 -11.91  -8.237  1 26.018  ? 383  GLU B C     1 
ATOM   7110 O  O     . GLU B 1 391 ? -22.846 -10.848 -7.713  1 24.985  ? 383  GLU B O     1 
ATOM   7111 C  CB    . GLU B 1 391 ? -23.172 -11.411 -10.747 1 27.54   ? 383  GLU B CB    1 
ATOM   7112 C  CG    . GLU B 1 391 ? -21.981 -12.291 -11.124 1 32.47   ? 383  GLU B CG    1 
ATOM   7113 C  CD    . GLU B 1 391 ? -20.991 -11.782 -12.167 1 36.979  ? 383  GLU B CD    1 
ATOM   7114 O  OE1   . GLU B 1 391 ? -21.152 -10.69  -12.766 1 39.949  ? 383  GLU B OE1   1 
ATOM   7115 O  OE2   . GLU B 1 391 ? -20.021 -12.532 -12.403 1 39.206  ? 383  GLU B OE2   1 
ATOM   7116 N  N     . VAL B 1 392 ? -22.862 -13.126 -7.765  1 26.061  ? 384  VAL B N     1 
ATOM   7117 C  CA    . VAL B 1 392 ? -21.997 -13.377 -6.615  1 24.926  ? 384  VAL B CA    1 
ATOM   7118 C  C     . VAL B 1 392 ? -20.555 -13.076 -7.053  1 27.547  ? 384  VAL B C     1 
ATOM   7119 O  O     . VAL B 1 392 ? -20.014 -13.76  -7.929  1 27.091  ? 384  VAL B O     1 
ATOM   7120 C  CB    . VAL B 1 392 ? -22.165 -14.777 -5.972  1 24.941  ? 384  VAL B CB    1 
ATOM   7121 C  CG1   . VAL B 1 392 ? -21.176 -15.008 -4.835  1 26.557  ? 384  VAL B CG1   1 
ATOM   7122 C  CG2   . VAL B 1 392 ? -23.569 -15.024 -5.423  1 27.442  ? 384  VAL B CG2   1 
ATOM   7123 N  N     . ILE B 1 393 ? -19.96  -12.036 -6.438  1 26.205  ? 385  ILE B N     1 
ATOM   7124 C  CA    . ILE B 1 393 ? -18.582 -11.604 -6.667  1 24.923  ? 385  ILE B CA    1 
ATOM   7125 C  C     . ILE B 1 393 ? -17.634 -12.29  -5.673  1 26.303  ? 385  ILE B C     1 
ATOM   7126 O  O     . ILE B 1 393 ? -16.626 -12.839 -6.107  1 24.258  ? 385  ILE B O     1 
ATOM   7127 C  CB    . ILE B 1 393 ? -18.461 -10.059 -6.767  1 23.552  ? 385  ILE B CB    1 
ATOM   7128 C  CG1   . ILE B 1 393 ? -19.28  -9.428  -7.948  1 22.197  ? 385  ILE B CG1   1 
ATOM   7129 C  CG2   . ILE B 1 393 ? -17.011 -9.557  -6.747  1 22.419  ? 385  ILE B CG2   1 
ATOM   7130 C  CD1   . ILE B 1 393 ? -19.027 -9.969  -9.364  1 23.494  ? 385  ILE B CD1   1 
ATOM   7131 N  N     . LEU B 1 394 ? -17.955 -12.223 -4.369  1 28.109  ? 386  LEU B N     1 
ATOM   7132 C  CA    . LEU B 1 394 ? -17.262 -12.924 -3.289  1 26.14   ? 386  LEU B CA    1 
ATOM   7133 C  C     . LEU B 1 394 ? -18.291 -13.703 -2.486  1 26.51   ? 386  LEU B C     1 
ATOM   7134 O  O     . LEU B 1 394 ? -19.243 -13.121 -1.955  1 28.643  ? 386  LEU B O     1 
ATOM   7135 C  CB    . LEU B 1 394 ? -16.394 -12.069 -2.355  1 24.134  ? 386  LEU B CB    1 
ATOM   7136 C  CG    . LEU B 1 394 ? -15.354 -11.114 -2.955  1 24.513  ? 386  LEU B CG    1 
ATOM   7137 C  CD1   . LEU B 1 394 ? -14.887 -10.234 -1.803  1 22.767  ? 386  LEU B CD1   1 
ATOM   7138 C  CD2   . LEU B 1 394 ? -14.126 -11.744 -3.61   1 25.959  ? 386  LEU B CD2   1 
ATOM   7139 N  N     . ASP B 1 395 ? -18.062 -15.02  -2.403  1 29.083  ? 387  ASP B N     1 
ATOM   7140 C  CA    . ASP B 1 395 ? -18.879 -15.925 -1.607  1 32.624  ? 387  ASP B CA    1 
ATOM   7141 C  C     . ASP B 1 395 ? -18.293 -16.037 -0.2    1 33.641  ? 387  ASP B C     1 
ATOM   7142 O  O     . ASP B 1 395 ? -17.93  -17.127 0.252   1 31.99   ? 387  ASP B O     1 
ATOM   7143 C  CB    . ASP B 1 395 ? -19.273 -17.188 -2.37   1 34.155  ? 387  ASP B CB    1 
ATOM   7144 C  CG    . ASP B 1 395 ? -20.176 -18.152 -1.616  1 37.756  ? 387  ASP B CG    1 
ATOM   7145 O  OD1   . ASP B 1 395 ? -21.122 -17.682 -0.916  1 39.233  ? 387  ASP B OD1   1 
ATOM   7146 O  OD2   . ASP B 1 395 ? -19.916 -19.372 -1.735  1 45.194  ? 387  ASP B OD2   1 
ATOM   7147 N  N     . THR B 1 396 ? -18.167 -14.875 0.457   1 33.639  ? 388  THR B N     1 
ATOM   7148 C  CA    . THR B 1 396 ? -17.606 -14.725 1.793   1 34.095  ? 388  THR B CA    1 
ATOM   7149 C  C     . THR B 1 396 ? -18.325 -13.562 2.478   1 30.091  ? 388  THR B C     1 
ATOM   7150 O  O     . THR B 1 396 ? -18.642 -12.591 1.776   1 29.813  ? 388  THR B O     1 
ATOM   7151 C  CB    . THR B 1 396 ? -16.063 -14.666 1.815   1 43.423  ? 388  THR B CB    1 
ATOM   7152 O  OG1   . THR B 1 396 ? -15.633 -14.879 3.16    1 44.98   ? 388  THR B OG1   1 
ATOM   7153 C  CG2   . THR B 1 396 ? -15.413 -13.386 1.308   1 41.484  ? 388  THR B CG2   1 
ATOM   7154 N  N     . PRO B 1 397 ? -18.633 -13.616 3.814   1 27.461  ? 389  PRO B N     1 
ATOM   7155 C  CA    . PRO B 1 397 ? -19.159 -12.445 4.516   1 26.719  ? 389  PRO B CA    1 
ATOM   7156 C  C     . PRO B 1 397 ? -18.256 -11.222 4.349   1 26.036  ? 389  PRO B C     1 
ATOM   7157 O  O     . PRO B 1 397 ? -17.035 -11.326 4.507   1 24.216  ? 389  PRO B O     1 
ATOM   7158 C  CB    . PRO B 1 397 ? -19.457 -12.939 5.925   1 27.267  ? 389  PRO B CB    1 
ATOM   7159 C  CG    . PRO B 1 397 ? -19.407 -14.445 5.856   1 27.686  ? 389  PRO B CG    1 
ATOM   7160 C  CD    . PRO B 1 397 ? -18.517 -14.785 4.716   1 26.127  ? 389  PRO B CD    1 
ATOM   7161 N  N     . SER B 1 398 ? -18.89  -10.15  3.86    1 25.192  ? 390  SER B N     1 
ATOM   7162 C  CA    . SER B 1 398 ? -18.281 -8.954  3.296   1 24.59   ? 390  SER B CA    1 
ATOM   7163 C  C     . SER B 1 398 ? -19.071 -7.738  3.761   1 24.26   ? 390  SER B C     1 
ATOM   7164 O  O     . SER B 1 398 ? -20.302 -7.743  3.74    1 25.88   ? 390  SER B O     1 
ATOM   7165 C  CB    . SER B 1 398 ? -18.262 -9.013  1.79    1 23.686  ? 390  SER B CB    1 
ATOM   7166 O  OG    . SER B 1 398 ? -17.484 -10.108 1.344   1 26.144  ? 390  SER B OG    1 
ATOM   7167 N  N     . GLU B 1 399 ? -18.339 -6.717  4.217   1 23.047  ? 391  GLU B N     1 
ATOM   7168 C  CA    . GLU B 1 399 ? -18.908 -5.483  4.737   1 21.581  ? 391  GLU B CA    1 
ATOM   7169 C  C     . GLU B 1 399 ? -17.929 -4.332  4.554   1 21.197  ? 391  GLU B C     1 
ATOM   7170 O  O     . GLU B 1 399 ? -16.825 -4.526  4.041   1 21.029  ? 391  GLU B O     1 
ATOM   7171 C  CB    . GLU B 1 399 ? -19.587 -5.611  6.114   1 20.526  ? 391  GLU B CB    1 
ATOM   7172 C  CG    . GLU B 1 399 ? -21.105 -5.432  6.047   1 20.524  ? 391  GLU B CG    1 
ATOM   7173 C  CD    . GLU B 1 399 ? -21.495 -4.07   5.485   1 22.079  ? 391  GLU B CD    1 
ATOM   7174 O  OE1   . GLU B 1 399 ? -21.201 -3.072  6.152   1 22.215  ? 391  GLU B OE1   1 
ATOM   7175 O  OE2   . GLU B 1 399 ? -21.952 -3.981  4.344   1 22.398  ? 391  GLU B OE2   1 
ATOM   7176 N  N     . PHE B 1 400 ? -18.409 -3.122  4.893   1 21.164  ? 392  PHE B N     1 
ATOM   7177 C  CA    . PHE B 1 400 ? -17.671 -1.86   4.896   1 21.645  ? 392  PHE B CA    1 
ATOM   7178 C  C     . PHE B 1 400 ? -16.777 -1.705  3.645   1 21.958  ? 392  PHE B C     1 
ATOM   7179 O  O     . PHE B 1 400 ? -15.558 -1.526  3.814   1 19.897  ? 392  PHE B O     1 
ATOM   7180 C  CB    . PHE B 1 400 ? -17.011 -1.783  6.286   1 20.476  ? 392  PHE B CB    1 
ATOM   7181 C  CG    . PHE B 1 400 ? -17.918 -1.553  7.486   1 22.918  ? 392  PHE B CG    1 
ATOM   7182 C  CD1   . PHE B 1 400 ? -18.605 -0.322  7.651   1 22.067  ? 392  PHE B CD1   1 
ATOM   7183 C  CD2   . PHE B 1 400 ? -18.046 -2.545  8.482   1 23.353  ? 392  PHE B CD2   1 
ATOM   7184 C  CE1   . PHE B 1 400 ? -19.435 -0.1    8.76    1 21.803  ? 392  PHE B CE1   1 
ATOM   7185 C  CE2   . PHE B 1 400 ? -18.878 -2.323  9.598   1 23.139  ? 392  PHE B CE2   1 
ATOM   7186 C  CZ    . PHE B 1 400 ? -19.563 -1.103  9.733   1 23.689  ? 392  PHE B CZ    1 
ATOM   7187 N  N     . PRO B 1 401 ? -17.286 -1.82   2.371   1 21.62   ? 393  PRO B N     1 
ATOM   7188 C  CA    . PRO B 1 401 ? -16.445 -1.56   1.201   1 21.52   ? 393  PRO B CA    1 
ATOM   7189 C  C     . PRO B 1 401 ? -16.16  -0.071  0.996   1 20.381  ? 393  PRO B C     1 
ATOM   7190 O  O     . PRO B 1 401 ? -17.002 0.782   1.301   1 20.3    ? 393  PRO B O     1 
ATOM   7191 C  CB    . PRO B 1 401 ? -17.159 -2.272  0.046   1 20.467  ? 393  PRO B CB    1 
ATOM   7192 C  CG    . PRO B 1 401 ? -18.608 -2.039  0.428   1 20.547  ? 393  PRO B CG    1 
ATOM   7193 C  CD    . PRO B 1 401 ? -18.67  -2.129  1.934   1 20.556  ? 393  PRO B CD    1 
ATOM   7194 N  N     . GLN B 1 402 ? -14.949 0.198   0.516   1 18.93   ? 394  GLN B N     1 
ATOM   7195 C  CA    . GLN B 1 402 ? -14.522 1.493   0.007   1 18.788  ? 394  GLN B CA    1 
ATOM   7196 C  C     . GLN B 1 402 ? -13.838 1.286   -1.344  1 17.767  ? 394  GLN B C     1 
ATOM   7197 O  O     . GLN B 1 402 ? -13.508 0.159   -1.716  1 17.333  ? 394  GLN B O     1 
ATOM   7198 C  CB    . GLN B 1 402 ? -13.676 2.243   1.051   1 20.157  ? 394  GLN B CB    1 
ATOM   7199 C  CG    . GLN B 1 402 ? -14.483 2.93    2.16    1 21.819  ? 394  GLN B CG    1 
ATOM   7200 C  CD    . GLN B 1 402 ? -13.819 4.106   2.865   1 22.985  ? 394  GLN B CD    1 
ATOM   7201 O  OE1   . GLN B 1 402 ? -12.831 4.698   2.404   1 24.039  ? 394  GLN B OE1   1 
ATOM   7202 N  NE2   . GLN B 1 402 ? -14.426 4.526   3.969   1 23.284  ? 394  GLN B NE2   1 
ATOM   7203 N  N     . ILE B 1 403 ? -13.687 2.394   -2.082  1 19.087  ? 395  ILE B N     1 
ATOM   7204 C  CA    . ILE B 1 403 ? -13.083 2.426   -3.41   1 20.97   ? 395  ILE B CA    1 
ATOM   7205 C  C     . ILE B 1 403 ? -11.897 3.404   -3.424  1 22.358  ? 395  ILE B C     1 
ATOM   7206 O  O     . ILE B 1 403 ? -11.564 4.014   -2.393  1 22.668  ? 395  ILE B O     1 
ATOM   7207 C  CB    . ILE B 1 403 ? -14.13  2.629   -4.547  1 21.018  ? 395  ILE B CB    1 
ATOM   7208 C  CG1   . ILE B 1 403 ? -14.754 4.035   -4.602  1 21.287  ? 395  ILE B CG1   1 
ATOM   7209 C  CG2   . ILE B 1 403 ? -15.202 1.532   -4.555  1 20.362  ? 395  ILE B CG2   1 
ATOM   7210 C  CD1   . ILE B 1 403 ? -15.086 4.521   -6.007  1 20.903  ? 395  ILE B CD1   1 
ATOM   7211 N  N     . ASP B 1 404 ? -11.243 3.503   -4.598  1 21.845  ? 396  ASP B N     1 
ATOM   7212 C  CA    . ASP B 1 404 ? -10.404 4.631   -4.974  1 22.307  ? 396  ASP B CA    1 
ATOM   7213 C  C     . ASP B 1 404 ? -11.309 5.794   -5.4    1 22.217  ? 396  ASP B C     1 
ATOM   7214 O  O     . ASP B 1 404 ? -11.819 5.804   -6.522  1 21.214  ? 396  ASP B O     1 
ATOM   7215 C  CB    . ASP B 1 404 ? -9.341  4.202   -5.982  1 22.126  ? 396  ASP B CB    1 
ATOM   7216 C  CG    . ASP B 1 404 ? -8.321  5.245   -6.438  1 25.723  ? 396  ASP B CG    1 
ATOM   7217 O  OD1   . ASP B 1 404 ? -8.479  6.461   -6.142  1 26.219  ? 396  ASP B OD1   1 
ATOM   7218 O  OD2   . ASP B 1 404 ? -7.324  4.823   -7.067  1 28.154  ? 396  ASP B OD2   1 
ATOM   7219 N  N     . ASN B 1 405 ? -11.418 6.805   -4.522  1 19.342  ? 397  ASN B N     1 
ATOM   7220 C  CA    . ASN B 1 405 ? -12.376 7.908   -4.644  1 19.828  ? 397  ASN B CA    1 
ATOM   7221 C  C     . ASN B 1 405 ? -12.091 8.863   -5.801  1 18.645  ? 397  ASN B C     1 
ATOM   7222 O  O     . ASN B 1 405 ? -12.969 9.639   -6.173  1 18.927  ? 397  ASN B O     1 
ATOM   7223 C  CB    . ASN B 1 405 ? -12.611 8.631   -3.323  1 19.207  ? 397  ASN B CB    1 
ATOM   7224 C  CG    . ASN B 1 405 ? -13.429 7.816   -2.346  1 19.366  ? 397  ASN B CG    1 
ATOM   7225 O  OD1   . ASN B 1 405 ? -14.245 6.971   -2.738  1 19.181  ? 397  ASN B OD1   1 
ATOM   7226 N  ND2   . ASN B 1 405 ? -13.24  8.084   -1.065  1 18.499  ? 397  ASN B ND2   1 
ATOM   7227 N  N     . ARG B 1 406 ? -10.902 8.755   -6.407  1 18.783  ? 398  ARG B N     1 
ATOM   7228 C  CA    . ARG B 1 406 ? -10.574 9.381   -7.684  1 20.767  ? 398  ARG B CA    1 
ATOM   7229 C  C     . ARG B 1 406 ? -11.475 8.864   -8.817  1 21.993  ? 398  ARG B C     1 
ATOM   7230 O  O     . ARG B 1 406 ? -11.54  9.503   -9.871  1 24.462  ? 398  ARG B O     1 
ATOM   7231 C  CB    . ARG B 1 406 ? -9.076  9.247   -7.978  1 19.709  ? 398  ARG B CB    1 
ATOM   7232 C  CG    . ARG B 1 406 ? -8.175  9.97    -6.976  1 18.041  ? 398  ARG B CG    1 
ATOM   7233 C  CD    . ARG B 1 406 ? -6.702  9.703   -7.211  1 17.641  ? 398  ARG B CD    1 
ATOM   7234 N  NE    . ARG B 1 406 ? -6.376  8.269   -7.261  1 19.505  ? 398  ARG B NE    1 
ATOM   7235 C  CZ    . ARG B 1 406 ? -5.318  7.686   -7.841  1 20.519  ? 398  ARG B CZ    1 
ATOM   7236 N  NH1   . ARG B 1 406 ? -4.34   8.41    -8.397  1 21.136  ? 398  ARG B NH1   1 
ATOM   7237 N  NH2   . ARG B 1 406 ? -5.225  6.363   -7.829  1 19.504  ? 398  ARG B NH2   1 
ATOM   7238 N  N     . PHE B 1 407 ? -12.19  7.748   -8.569  1 22.166  ? 399  PHE B N     1 
ATOM   7239 C  CA    . PHE B 1 407 ? -13.101 7.069   -9.487  1 22.776  ? 399  PHE B CA    1 
ATOM   7240 C  C     . PHE B 1 407 ? -14.552 7.127   -8.98   1 22.452  ? 399  PHE B C     1 
ATOM   7241 O  O     . PHE B 1 407 ? -15.392 6.387   -9.494  1 21.74   ? 399  PHE B O     1 
ATOM   7242 C  CB    . PHE B 1 407 ? -12.499 5.693   -9.812  1 21.674  ? 399  PHE B CB    1 
ATOM   7243 C  CG    . PHE B 1 407 ? -11.194 5.763   -10.597 1 23.879  ? 399  PHE B CG    1 
ATOM   7244 C  CD1   . PHE B 1 407 ? -9.954  5.88    -9.935  1 23.264  ? 399  PHE B CD1   1 
ATOM   7245 C  CD2   . PHE B 1 407 ? -11.206 5.718   -12.007 1 24.824  ? 399  PHE B CD2   1 
ATOM   7246 C  CE1   . PHE B 1 407 ? -8.756  5.966   -10.668 1 25.446  ? 399  PHE B CE1   1 
ATOM   7247 C  CE2   . PHE B 1 407 ? -10.008 5.803   -12.743 1 26.166  ? 399  PHE B CE2   1 
ATOM   7248 C  CZ    . PHE B 1 407 ? -8.78   5.931   -12.071 1 25.082  ? 399  PHE B CZ    1 
ATOM   7249 N  N     . MET B 1 408 ? -14.847 8.004   -7.995  1 21.412  ? 400  MET B N     1 
ATOM   7250 C  CA    . MET B 1 408 ? -16.187 8.136   -7.436  1 19.882  ? 400  MET B CA    1 
ATOM   7251 C  C     . MET B 1 408 ? -17.126 8.798   -8.451  1 21.695  ? 400  MET B C     1 
ATOM   7252 O  O     . MET B 1 408 ? -16.855 9.895   -8.944  1 22.043  ? 400  MET B O     1 
ATOM   7253 C  CB    . MET B 1 408 ? -16.208 8.816   -6.065  1 18.948  ? 400  MET B CB    1 
ATOM   7254 C  CG    . MET B 1 408 ? -17.609 8.981   -5.44   1 20.182  ? 400  MET B CG    1 
ATOM   7255 S  SD    . MET B 1 408 ? -18.516 7.443   -5.225  1 20.235  ? 400  MET B SD    1 
ATOM   7256 C  CE    . MET B 1 408 ? -17.783 6.61    -3.813  1 21.054  ? 400  MET B CE    1 
ATOM   7257 N  N     . GLY B 1 409 ? -18.238 8.086   -8.724  1 22.363  ? 401  GLY B N     1 
ATOM   7258 C  CA    . GLY B 1 409 ? -19.287 8.508   -9.646  1 21.038  ? 401  GLY B CA    1 
ATOM   7259 C  C     . GLY B 1 409 ? -18.932 8.293   -11.115 1 20.841  ? 401  GLY B C     1 
ATOM   7260 O  O     . GLY B 1 409 ? -19.627 8.845   -11.97  1 22.59   ? 401  GLY B O     1 
ATOM   7261 N  N     . VAL B 1 410 ? -17.84  7.548   -11.378 1 18.829  ? 402  VAL B N     1 
ATOM   7262 C  CA    . VAL B 1 410 ? -17.393 7.084   -12.688 1 18.349  ? 402  VAL B CA    1 
ATOM   7263 C  C     . VAL B 1 410 ? -17.081 5.591   -12.567 1 20.303  ? 402  VAL B C     1 
ATOM   7264 O  O     . VAL B 1 410 ? -17.151 5.037   -11.462 1 22.641  ? 402  VAL B O     1 
ATOM   7265 C  CB    . VAL B 1 410 ? -16.292 7.906   -13.404 1 17.364  ? 402  VAL B CB    1 
ATOM   7266 C  CG1   . VAL B 1 410 ? -16.775 9.299   -13.773 1 16.591  ? 402  VAL B CG1   1 
ATOM   7267 C  CG2   . VAL B 1 410 ? -14.964 7.981   -12.658 1 16.27   ? 402  VAL B CG2   1 
ATOM   7268 N  N     . GLU B 1 411 ? -16.768 4.939   -13.704 1 20.29   ? 403  GLU B N     1 
ATOM   7269 C  CA    . GLU B 1 411 ? -16.297 3.56    -13.758 1 21.505  ? 403  GLU B CA    1 
ATOM   7270 C  C     . GLU B 1 411 ? -15.067 3.381   -12.861 1 21.017  ? 403  GLU B C     1 
ATOM   7271 O  O     . GLU B 1 411 ? -14.109 4.136   -12.961 1 21.464  ? 403  GLU B O     1 
ATOM   7272 C  CB    . GLU B 1 411 ? -16.037 3.148   -15.202 1 24.341  ? 403  GLU B CB    1 
ATOM   7273 C  CG    . GLU B 1 411 ? -15.747 1.656   -15.339 1 26.158  ? 403  GLU B CG    1 
ATOM   7274 C  CD    . GLU B 1 411 ? -15.598 1.056   -16.722 1 30.032  ? 403  GLU B CD    1 
ATOM   7275 O  OE1   . GLU B 1 411 ? -15.74  1.778   -17.741 1 29.18   ? 403  GLU B OE1   1 
ATOM   7276 O  OE2   . GLU B 1 411 ? -15.326 -0.173  -16.752 1 31.356  ? 403  GLU B OE2   1 
ATOM   7277 N  N     . TYR B 1 412 ? -15.173 2.396   -11.967 1 20.711  ? 404  TYR B N     1 
ATOM   7278 C  CA    . TYR B 1 412 ? -14.157 1.999   -11.002 1 20.118  ? 404  TYR B CA    1 
ATOM   7279 C  C     . TYR B 1 412 ? -13.933 0.496   -11.149 1 20.102  ? 404  TYR B C     1 
ATOM   7280 O  O     . TYR B 1 412 ? -14.807 -0.222  -11.643 1 23.191  ? 404  TYR B O     1 
ATOM   7281 C  CB    . TYR B 1 412 ? -14.661 2.472   -9.629  1 18.505  ? 404  TYR B CB    1 
ATOM   7282 C  CG    . TYR B 1 412 ? -15.642 1.516   -8.962  1 18.529  ? 404  TYR B CG    1 
ATOM   7283 C  CD1   . TYR B 1 412 ? -17.008 1.533   -9.285  1 18.967  ? 404  TYR B CD1   1 
ATOM   7284 C  CD2   . TYR B 1 412 ? -15.188 0.558   -8.037  1 19.501  ? 404  TYR B CD2   1 
ATOM   7285 C  CE1   . TYR B 1 412 ? -17.897 0.626   -8.713  1 19.464  ? 404  TYR B CE1   1 
ATOM   7286 C  CE2   . TYR B 1 412 ? -16.074 -0.351  -7.456  1 20.327  ? 404  TYR B CE2   1 
ATOM   7287 C  CZ    . TYR B 1 412 ? -17.429 -0.306  -7.788  1 20.058  ? 404  TYR B CZ    1 
ATOM   7288 O  OH    . TYR B 1 412 ? -18.306 -1.194  -7.224  1 20.903  ? 404  TYR B OH    1 
ATOM   7289 N  N     . SER B 1 413 ? -12.812 0.035   -10.579 1 20.993  ? 405  SER B N     1 
ATOM   7290 C  CA    . SER B 1 413 ? -12.344 -1.343  -10.615 1 22.056  ? 405  SER B CA    1 
ATOM   7291 C  C     . SER B 1 413 ? -12.002 -1.887  -9.222  1 22.546  ? 405  SER B C     1 
ATOM   7292 O  O     . SER B 1 413 ? -12.404 -3.016  -8.909  1 23.46   ? 405  SER B O     1 
ATOM   7293 C  CB    . SER B 1 413 ? -11.194 -1.496  -11.591 1 21.274  ? 405  SER B CB    1 
ATOM   7294 O  OG    . SER B 1 413 ? -10.772 -2.853  -11.637 1 22.904  ? 405  SER B OG    1 
ATOM   7295 N  N     . SER B 1 414 ? -11.227 -1.104  -8.448  1 20.927  ? 406  SER B N     1 
ATOM   7296 C  CA    . SER B 1 414 ? -10.722 -1.436  -7.116  1 20.62   ? 406  SER B CA    1 
ATOM   7297 C  C     . SER B 1 414 ? -11.827 -1.312  -6.064  1 21.172  ? 406  SER B C     1 
ATOM   7298 O  O     . SER B 1 414 ? -12.513 -0.287  -6.01   1 21.97   ? 406  SER B O     1 
ATOM   7299 C  CB    . SER B 1 414 ? -9.512  -0.588  -6.758  1 19.531  ? 406  SER B CB    1 
ATOM   7300 O  OG    . SER B 1 414 ? -8.3    -1.186  -7.196  1 19.69   ? 406  SER B OG    1 
ATOM   7301 N  N     . ALA B 1 415 ? -12.005 -2.378  -5.263  1 19.152  ? 407  ALA B N     1 
ATOM   7302 C  CA    . ALA B 1 415 ? -12.793 -2.326  -4.031  1 20.474  ? 407  ALA B CA    1 
ATOM   7303 C  C     . ALA B 1 415 ? -11.983 -2.898  -2.869  1 21.248  ? 407  ALA B C     1 
ATOM   7304 O  O     . ALA B 1 415 ? -11.353 -3.949  -3.003  1 21.829  ? 407  ALA B O     1 
ATOM   7305 C  CB    . ALA B 1 415 ? -14.16  -2.99   -4.182  1 18.418  ? 407  ALA B CB    1 
ATOM   7306 N  N     . PHE B 1 416 ? -12.008 -2.16   -1.749  1 20.981  ? 408  PHE B N     1 
ATOM   7307 C  CA    . PHE B 1 416 ? -11.368 -2.537  -0.491  1 20.066  ? 408  PHE B CA    1 
ATOM   7308 C  C     . PHE B 1 416 ? -12.47  -2.928  0.485   1 19.779  ? 408  PHE B C     1 
ATOM   7309 O  O     . PHE B 1 416 ? -13.298 -2.092  0.847   1 20.55   ? 408  PHE B O     1 
ATOM   7310 C  CB    . PHE B 1 416 ? -10.415 -1.439  -0.01   1 19.051  ? 408  PHE B CB    1 
ATOM   7311 C  CG    . PHE B 1 416 ? -9.455  -0.91   -1.062  1 18.771  ? 408  PHE B CG    1 
ATOM   7312 C  CD1   . PHE B 1 416 ? -8.28   -1.612  -1.373  1 19.43   ? 408  PHE B CD1   1 
ATOM   7313 C  CD2   . PHE B 1 416 ? -9.718  0.307   -1.72   1 19.617  ? 408  PHE B CD2   1 
ATOM   7314 C  CE1   . PHE B 1 416 ? -7.382  -1.106  -2.322  1 19.505  ? 408  PHE B CE1   1 
ATOM   7315 C  CE2   . PHE B 1 416 ? -8.823  0.8     -2.693  1 19.924  ? 408  PHE B CE2   1 
ATOM   7316 C  CZ    . PHE B 1 416 ? -7.664  0.086   -2.993  1 19.335  ? 408  PHE B CZ    1 
ATOM   7317 N  N     . ILE B 1 417 ? -12.492 -4.222  0.841   1 18.926  ? 409  ILE B N     1 
ATOM   7318 C  CA    . ILE B 1 417 ? -13.655 -4.839  1.473   1 21.002  ? 409  ILE B CA    1 
ATOM   7319 C  C     . ILE B 1 417 ? -13.207 -5.436  2.813   1 20.723  ? 409  ILE B C     1 
ATOM   7320 O  O     . ILE B 1 417 ? -12.193 -6.14   2.863   1 22.569  ? 409  ILE B O     1 
ATOM   7321 C  CB    . ILE B 1 417 ? -14.338 -5.864  0.524   1 21.561  ? 409  ILE B CB    1 
ATOM   7322 C  CG1   . ILE B 1 417 ? -14.605 -5.305  -0.926  1 23.634  ? 409  ILE B CG1   1 
ATOM   7323 C  CG2   . ILE B 1 417 ? -15.615 -6.439  1.14    1 21.704  ? 409  ILE B CG2   1 
ATOM   7324 C  CD1   . ILE B 1 417 ? -14.617 -6.342  -2.043  1 24.84   ? 409  ILE B CD1   1 
ATOM   7325 N  N     . ASN B 1 418 ? -13.982 -5.147  3.875   1 19.805  ? 410  ASN B N     1 
ATOM   7326 C  CA    . ASN B 1 418 ? -13.865 -5.777  5.191   1 20.624  ? 410  ASN B CA    1 
ATOM   7327 C  C     . ASN B 1 418 ? -14.497 -7.172  5.098   1 20.318  ? 410  ASN B C     1 
ATOM   7328 O  O     . ASN B 1 418 ? -15.654 -7.275  4.676   1 20.594  ? 410  ASN B O     1 
ATOM   7329 C  CB    . ASN B 1 418 ? -14.427 -4.813  6.244   1 20.266  ? 410  ASN B CB    1 
ATOM   7330 C  CG    . ASN B 1 418 ? -13.996 -5.005  7.686   1 20.058  ? 410  ASN B CG    1 
ATOM   7331 O  OD1   . ASN B 1 418 ? -13.056 -5.746  8.019   1 20.604  ? 410  ASN B OD1   1 
ATOM   7332 N  ND2   . ASN B 1 418 ? -14.706 -4.327  8.573   1 17.641  ? 410  ASN B ND2   1 
ATOM   7333 N  N     . VAL B 1 419 ? -13.734 -8.225  5.454   1 20.083  ? 411  VAL B N     1 
ATOM   7334 C  CA    . VAL B 1 419 ? -14.086 -9.616  5.153   1 21.727  ? 411  VAL B CA    1 
ATOM   7335 C  C     . VAL B 1 419 ? -13.943 -10.537 6.367   1 25.46   ? 411  VAL B C     1 
ATOM   7336 O  O     . VAL B 1 419 ? -13.103 -10.301 7.247   1 24.659  ? 411  VAL B O     1 
ATOM   7337 C  CB    . VAL B 1 419 ? -13.434 -10.254 3.899   1 23.634  ? 411  VAL B CB    1 
ATOM   7338 C  CG1   . VAL B 1 419 ? -13.974 -9.68   2.585   1 20.014  ? 411  VAL B CG1   1 
ATOM   7339 C  CG2   . VAL B 1 419 ? -11.898 -10.277 3.909   1 21.338  ? 411  VAL B CG2   1 
ATOM   7340 N  N     . PHE B 1 420 ? -14.779 -11.595 6.381   1 29.535  ? 412  PHE B N     1 
ATOM   7341 C  CA    . PHE B 1 420 ? -14.491 -12.848 7.077   1 35.434  ? 412  PHE B CA    1 
ATOM   7342 C  C     . PHE B 1 420 ? -13.546 -13.638 6.17    1 36.414  ? 412  PHE B C     1 
ATOM   7343 O  O     . PHE B 1 420 ? -13.902 -13.919 5.015   1 37.204  ? 412  PHE B O     1 
ATOM   7344 C  CB    . PHE B 1 420 ? -15.726 -13.709 7.392   1 39.617  ? 412  PHE B CB    1 
ATOM   7345 C  CG    . PHE B 1 420 ? -16.841 -13.339 8.366   1 45.625  ? 412  PHE B CG    1 
ATOM   7346 C  CD1   . PHE B 1 420 ? -17.258 -12.006 8.569   1 48.246  ? 412  PHE B CD1   1 
ATOM   7347 C  CD2   . PHE B 1 420 ? -17.536 -14.363 9.042   1 48.194  ? 412  PHE B CD2   1 
ATOM   7348 C  CE1   . PHE B 1 420 ? -18.334 -11.701 9.422   1 43.39   ? 412  PHE B CE1   1 
ATOM   7349 C  CE2   . PHE B 1 420 ? -18.618 -14.066 9.893   1 50.241  ? 412  PHE B CE2   1 
ATOM   7350 C  CZ    . PHE B 1 420 ? -19.02  -12.732 10.078  1 44.175  ? 412  PHE B CZ    1 
ATOM   7351 N  N     . VAL B 1 421 ? -12.344 -13.955 6.688   1 33.827  ? 413  VAL B N     1 
ATOM   7352 C  CA    . VAL B 1 421 ? -11.282 -14.614 5.927   1 35.565  ? 413  VAL B CA    1 
ATOM   7353 C  C     . VAL B 1 421 ? -11.719 -16.066 5.667   1 36.973  ? 413  VAL B C     1 
ATOM   7354 O  O     . VAL B 1 421 ? -11.962 -16.765 6.657   1 34.406  ? 413  VAL B O     1 
ATOM   7355 C  CB    . VAL B 1 421 ? -9.822  -14.5   6.448   1 36.493  ? 413  VAL B CB    1 
ATOM   7356 C  CG1   . VAL B 1 421 ? -8.795  -15.2   5.546   1 35.725  ? 413  VAL B CG1   1 
ATOM   7357 C  CG2   . VAL B 1 421 ? -9.389  -13.047 6.646   1 31.962  ? 413  VAL B CG2   1 
ATOM   7358 N  N     . PRO B 1 422 ? -11.854 -16.542 4.375   1 43.088  ? 414  PRO B N     1 
ATOM   7359 C  CA    . PRO B 1 422 ? -12.2   -17.944 4.089   1 43.585  ? 414  PRO B CA    1 
ATOM   7360 C  C     . PRO B 1 422 ? -11.236 -18.935 4.749   1 52.451  ? 414  PRO B C     1 
ATOM   7361 O  O     . PRO B 1 422 ? -10.023 -18.688 4.761   1 50.442  ? 414  PRO B O     1 
ATOM   7362 C  CB    . PRO B 1 422 ? -12.291 -18.038 2.568   1 39.976  ? 414  PRO B CB    1 
ATOM   7363 C  CG    . PRO B 1 422 ? -12.321 -16.604 2.068   1 39.577  ? 414  PRO B CG    1 
ATOM   7364 C  CD    . PRO B 1 422 ? -11.654 -15.772 3.119   1 40.225  ? 414  PRO B CD    1 
ATOM   7365 N  N     . ASP B 1 423 ? -11.824 -19.944 5.424   1 60.151  ? 415  ASP B N     1 
ATOM   7366 C  CA    . ASP B 1 423 ? -11.191 -21.044 6.162   1 74.614  ? 415  ASP B CA    1 
ATOM   7367 C  C     . ASP B 1 423 ? -10.501 -20.595 7.466   1 75.37   ? 415  ASP B C     1 
ATOM   7368 O  O     . ASP B 1 423 ? -9.903  -21.432 8.149   1 82.146  ? 415  ASP B O     1 
ATOM   7369 C  CB    . ASP B 1 423 ? -10.365 -21.981 5.269   1 79.415  ? 415  ASP B CB    1 
ATOM   7370 C  CG    . ASP B 1 423 ? -10.99  -22.508 3.98    1 79.647  ? 415  ASP B CG    1 
ATOM   7371 O  OD1   . ASP B 1 423 ? -12.07  -23.143 4.044   1 76.195  ? 415  ASP B OD1   1 
ATOM   7372 O  OD2   . ASP B 1 423 ? -10.363 -22.315 2.916   1 76.914  ? 415  ASP B OD2   1 
ATOM   7373 N  N     . ARG B 1 424 ? -10.621 -19.307 7.847   1 80.714  ? 416  ARG B N     1 
ATOM   7374 C  CA    . ARG B 1 424 ? -9.843  -18.662 8.909   1 83.882  ? 416  ARG B CA    1 
ATOM   7375 C  C     . ARG B 1 424 ? -10.731 -17.866 9.876   1 85.619  ? 416  ARG B C     1 
ATOM   7376 O  O     . ARG B 1 424 ? -10.221 -17.224 10.799  1 89.63   ? 416  ARG B O     1 
ATOM   7377 C  CB    . ARG B 1 424 ? -8.733  -17.783 8.311   1 80.655  ? 416  ARG B CB    1 
ATOM   7378 C  CG    . ARG B 1 424 ? -7.658  -18.354 7.395   1 82.108  ? 416  ARG B CG    1 
ATOM   7379 C  CD    . ARG B 1 424 ? -6.499  -19.063 8.073   1 82.381  ? 416  ARG B CD    1 
ATOM   7380 N  NE    . ARG B 1 424 ? -5.438  -18.289 8.738   1 78.101  ? 416  ARG B NE    1 
ATOM   7381 C  CZ    . ARG B 1 424 ? -4.53   -17.408 8.279   1 81.577  ? 416  ARG B CZ    1 
ATOM   7382 N  NH1   . ARG B 1 424 ? -4.683  -16.699 7.166   1 79.861  ? 416  ARG B NH1   1 
ATOM   7383 N  NH2   . ARG B 1 424 ? -3.436  -17.227 8.992   1 80.028  ? 416  ARG B NH2   1 
ATOM   7384 N  N     . SER B 1 425 ? -12.055 -17.948 9.675   1 83.993  ? 417  SER B N     1 
ATOM   7385 C  CA    . SER B 1 425 ? -13.092 -17.203 10.38   1 81.944  ? 417  SER B CA    1 
ATOM   7386 C  C     . SER B 1 425 ? -14.244 -18.137 10.782  1 85.456  ? 417  SER B C     1 
ATOM   7387 O  O     . SER B 1 425 ? -14.278 -19.306 10.376  1 80.229  ? 417  SER B O     1 
ATOM   7388 C  CB    . SER B 1 425 ? -13.536 -15.998 9.552   1 73.928  ? 417  SER B CB    1 
ATOM   7389 O  OG    . SER B 1 425 ? -14.095 -16.414 8.316   1 66.076  ? 417  SER B OG    1 
ATOM   7390 N  N     . ASP B 1 426 ? -15.177 -17.599 11.591  1 96.032  ? 418  ASP B N     1 
ATOM   7391 C  CA    . ASP B 1 426 ? -16.299 -18.316 12.188  1 97.22   ? 418  ASP B CA    1 
ATOM   7392 C  C     . ASP B 1 426 ? -17.363 -18.608 11.121  1 101.675 ? 418  ASP B C     1 
ATOM   7393 O  O     . ASP B 1 426 ? -17.434 -19.751 10.66   1 112.117 ? 418  ASP B O     1 
ATOM   7394 C  CB    . ASP B 1 426 ? -16.655 -17.716 13.544  1 93.82   ? 418  ASP B CB    1 
ATOM   7395 C  CG    . ASP B 1 426 ? -17.633 -18.45  14.459  1 95.105  ? 418  ASP B CG    1 
ATOM   7396 O  OD1   . ASP B 1 426 ? -18.504 -19.219 13.972  1 99.385  ? 418  ASP B OD1   1 
ATOM   7397 O  OD2   . ASP B 1 426 ? -17.518 -18.242 15.685  1 88.585  ? 418  ASP B OD2   1 
ATOM   7398 N  N     . GLY B 1 427 ? -18.161 -17.591 10.734  1 93.283  ? 419  GLY B N     1 
ATOM   7399 C  CA    . GLY B 1 427 ? -19.204 -17.74  9.723   1 82.871  ? 419  GLY B CA    1 
ATOM   7400 C  C     . GLY B 1 427 ? -20.608 -17.92  10.304  1 75.61   ? 419  GLY B C     1 
ATOM   7401 O  O     . GLY B 1 427 ? -21.585 -17.588 9.624   1 73.417  ? 419  GLY B O     1 
ATOM   7402 N  N     . ASN B 1 428 ? -20.692 -18.47  11.535  1 65.316  ? 420  ASN B N     1 
ATOM   7403 C  CA    . ASN B 1 428 ? -21.875 -18.415 12.389  1 62.045  ? 420  ASN B CA    1 
ATOM   7404 C  C     . ASN B 1 428 ? -22.074 -17.051 13.065  1 55.35   ? 420  ASN B C     1 
ATOM   7405 O  O     . ASN B 1 428 ? -23.14  -16.829 13.643  1 53.706  ? 420  ASN B O     1 
ATOM   7406 C  CB    . ASN B 1 428 ? -22.039 -19.665 13.257  1 69.527  ? 420  ASN B CB    1 
ATOM   7407 C  CG    . ASN B 1 428 ? -22.712 -20.813 12.527  1 76.093  ? 420  ASN B CG    1 
ATOM   7408 O  OD1   . ASN B 1 428 ? -22.18  -21.93  12.511  1 79.872  ? 420  ASN B OD1   1 
ATOM   7409 N  ND2   . ASN B 1 428 ? -23.895 -20.593 11.96   1 70.591  ? 420  ASN B ND2   1 
ATOM   7410 N  N     . LYS B 1 429 ? -21.071 -16.153 12.993  1 50.363  ? 421  LYS B N     1 
ATOM   7411 C  CA    . LYS B 1 429 ? -21.16  -14.764 13.442  1 45.735  ? 421  LYS B CA    1 
ATOM   7412 C  C     . LYS B 1 429 ? -22.073 -13.983 12.494  1 40.227  ? 421  LYS B C     1 
ATOM   7413 O  O     . LYS B 1 429 ? -21.989 -14.163 11.269  1 36.662  ? 421  LYS B O     1 
ATOM   7414 C  CB    . LYS B 1 429 ? -19.823 -14.004 13.483  1 47.204  ? 421  LYS B CB    1 
ATOM   7415 C  CG    . LYS B 1 429 ? -18.537 -14.602 14.08   1 50.134  ? 421  LYS B CG    1 
ATOM   7416 C  CD    . LYS B 1 429 ? -18.401 -14.935 15.565  1 52.881  ? 421  LYS B CD    1 
ATOM   7417 C  CE    . LYS B 1 429 ? -18.319 -13.786 16.525  1 54.891  ? 421  LYS B CE    1 
ATOM   7418 N  NZ    . LYS B 1 429 ? -17.574 -14.164 17.728  1 56.019  ? 421  LYS B NZ    1 
ATOM   7419 N  N     . ASN B 1 430 ? -22.905 -13.092 13.083  1 36.35   ? 422  ASN B N     1 
ATOM   7420 C  CA    . ASN B 1 430 ? -23.48  -11.9   12.446  1 30.786  ? 422  ASN B CA    1 
ATOM   7421 C  C     . ASN B 1 430 ? -22.383 -11.188 11.636  1 28.521  ? 422  ASN B C     1 
ATOM   7422 O  O     . ASN B 1 430 ? -21.225 -11.118 12.082  1 26.559  ? 422  ASN B O     1 
ATOM   7423 C  CB    . ASN B 1 430 ? -24.245 -11.042 13.461  1 29.496  ? 422  ASN B CB    1 
ATOM   7424 C  CG    . ASN B 1 430 ? -24.656 -9.672  12.955  1 29.447  ? 422  ASN B CG    1 
ATOM   7425 O  OD1   . ASN B 1 430 ? -23.835 -8.747  12.896  1 28.974  ? 422  ASN B OD1   1 
ATOM   7426 N  ND2   . ASN B 1 430 ? -25.924 -9.501  12.609  1 30.214  ? 422  ASN B ND2   1 
ATOM   7427 N  N     . VAL B 1 431 ? -22.776 -10.663 10.459  1 24.795  ? 423  VAL B N     1 
ATOM   7428 C  CA    . VAL B 1 431 ? -21.908 -10.09  9.428   1 24.076  ? 423  VAL B CA    1 
ATOM   7429 C  C     . VAL B 1 431 ? -20.955 -9.017  9.99    1 24.394  ? 423  VAL B C     1 
ATOM   7430 O  O     . VAL B 1 431 ? -19.831 -8.916  9.491   1 23.479  ? 423  VAL B O     1 
ATOM   7431 C  CB    . VAL B 1 431 ? -22.713 -9.609  8.191   1 24.941  ? 423  VAL B CB    1 
ATOM   7432 C  CG1   . VAL B 1 431 ? -23.675 -8.431  8.477   1 21.842  ? 423  VAL B CG1   1 
ATOM   7433 C  CG2   . VAL B 1 431 ? -21.842 -9.375  6.939   1 21.6    ? 423  VAL B CG2   1 
ATOM   7434 N  N     . PHE B 1 432 ? -21.395 -8.253  11.02   1 22.681  ? 424  PHE B N     1 
ATOM   7435 C  CA    . PHE B 1 432 ? -20.598 -7.175  11.599  1 24.221  ? 424  PHE B CA    1 
ATOM   7436 C  C     . PHE B 1 432 ? -19.569 -7.646  12.641  1 24.147  ? 424  PHE B C     1 
ATOM   7437 O  O     . PHE B 1 432 ? -18.742 -6.832  13.073  1 21.855  ? 424  PHE B O     1 
ATOM   7438 C  CB    . PHE B 1 432 ? -21.551 -6.125  12.165  1 22.952  ? 424  PHE B CB    1 
ATOM   7439 C  CG    . PHE B 1 432 ? -22.405 -5.361  11.167  1 21.997  ? 424  PHE B CG    1 
ATOM   7440 C  CD1   . PHE B 1 432 ? -21.858 -4.338  10.379  1 21.829  ? 424  PHE B CD1   1 
ATOM   7441 C  CD2   . PHE B 1 432 ? -23.775 -5.634  11.076  1 21.797  ? 424  PHE B CD2   1 
ATOM   7442 C  CE1   . PHE B 1 432 ? -22.66  -3.62   9.486   1 23.864  ? 424  PHE B CE1   1 
ATOM   7443 C  CE2   . PHE B 1 432 ? -24.59  -4.913  10.19   1 22.896  ? 424  PHE B CE2   1 
ATOM   7444 C  CZ    . PHE B 1 432 ? -24.038 -3.893  9.41    1 23.117  ? 424  PHE B CZ    1 
ATOM   7445 N  N     . GLN B 1 433 ? -19.591 -8.943  13.003  1 26.303  ? 425  GLN B N     1 
ATOM   7446 C  CA    . GLN B 1 433 ? -18.986 -9.45   14.235  1 30.783  ? 425  GLN B CA    1 
ATOM   7447 C  C     . GLN B 1 433 ? -17.81  -10.405 14.017  1 34.172  ? 425  GLN B C     1 
ATOM   7448 O  O     . GLN B 1 433 ? -17.091 -10.695 14.982  1 40.276  ? 425  GLN B O     1 
ATOM   7449 C  CB    . GLN B 1 433 ? -20.01  -10.081 15.171  1 28.488  ? 425  GLN B CB    1 
ATOM   7450 C  CG    . GLN B 1 433 ? -21.132 -9.142  15.585  1 27.702  ? 425  GLN B CG    1 
ATOM   7451 C  CD    . GLN B 1 433 ? -21.989 -9.679  16.703  1 29.974  ? 425  GLN B CD    1 
ATOM   7452 O  OE1   . GLN B 1 433 ? -21.735 -10.726 17.319  1 32.381  ? 425  GLN B OE1   1 
ATOM   7453 N  NE2   . GLN B 1 433 ? -23.024 -8.914  16.987  1 29.494  ? 425  GLN B NE2   1 
ATOM   7454 N  N     . GLY B 1 434 ? -17.585 -10.862 12.778  1 34.017  ? 426  GLY B N     1 
ATOM   7455 C  CA    . GLY B 1 434 ? -16.48  -11.782 12.511  1 39.098  ? 426  GLY B CA    1 
ATOM   7456 C  C     . GLY B 1 434 ? -15.444 -11.253 11.515  1 36.673  ? 426  GLY B C     1 
ATOM   7457 O  O     . GLY B 1 434 ? -14.759 -12.07  10.893  1 42.528  ? 426  GLY B O     1 
ATOM   7458 N  N     . LEU B 1 435 ? -15.317 -9.915  11.4    1 29.589  ? 427  LEU B N     1 
ATOM   7459 C  CA    . LEU B 1 435 ? -14.55  -9.277  10.337  1 25.242  ? 427  LEU B CA    1 
ATOM   7460 C  C     . LEU B 1 435 ? -13.064 -9.258  10.726  1 25.022  ? 427  LEU B C     1 
ATOM   7461 O  O     . LEU B 1 435 ? -12.632 -8.433  11.545  1 25.543  ? 427  LEU B O     1 
ATOM   7462 C  CB    . LEU B 1 435 ? -15.141 -7.937  9.881   1 21.811  ? 427  LEU B CB    1 
ATOM   7463 C  CG    . LEU B 1 435 ? -16.571 -7.944  9.31    1 20.464  ? 427  LEU B CG    1 
ATOM   7464 C  CD1   . LEU B 1 435 ? -17.233 -6.577  9.433   1 18.848  ? 427  LEU B CD1   1 
ATOM   7465 C  CD2   . LEU B 1 435 ? -16.722 -8.429  7.867   1 21.287  ? 427  LEU B CD2   1 
ATOM   7466 N  N     . ASN B 1 436 ? -12.314 -10.236 10.183  1 23.538  ? 428  ASN B N     1 
ATOM   7467 C  CA    . ASN B 1 436 ? -10.947 -10.538 10.609  1 21.881  ? 428  ASN B CA    1 
ATOM   7468 C  C     . ASN B 1 436 ? -9.946  -10.369 9.465   1 20.496  ? 428  ASN B C     1 
ATOM   7469 O  O     . ASN B 1 436 ? -8.801  -10.826 9.569   1 20.103  ? 428  ASN B O     1 
ATOM   7470 C  CB    . ASN B 1 436 ? -10.874 -11.859 11.38   1 22.731  ? 428  ASN B CB    1 
ATOM   7471 C  CG    . ASN B 1 436 ? -11.096 -13.105 10.545  1 24.088  ? 428  ASN B CG    1 
ATOM   7472 O  OD1   . ASN B 1 436 ? -11.547 -13.068 9.393   1 24.55   ? 428  ASN B OD1   1 
ATOM   7473 N  ND2   . ASN B 1 436 ? -10.822 -14.25  11.141  1 25.386  ? 428  ASN B ND2   1 
ATOM   7474 N  N     . GLY B 1 437 ? -10.398 -9.752  8.368   1 18.713  ? 429  GLY B N     1 
ATOM   7475 C  CA    . GLY B 1 437 ? -9.529  -9.464  7.24    1 18.985  ? 429  GLY B CA    1 
ATOM   7476 C  C     . GLY B 1 437 ? -10.026 -8.379  6.287   1 19.392  ? 429  GLY B C     1 
ATOM   7477 O  O     . GLY B 1 437 ? -11.097 -7.781  6.468   1 18.896  ? 429  GLY B O     1 
ATOM   7478 N  N     . LEU B 1 438 ? -9.183  -8.171  5.269   1 20.201  ? 430  LEU B N     1 
ATOM   7479 C  CA    . LEU B 1 438 ? -9.374  -7.227  4.177   1 20.155  ? 430  LEU B CA    1 
ATOM   7480 C  C     . LEU B 1 438 ? -9.176  -7.963  2.856   1 22.685  ? 430  LEU B C     1 
ATOM   7481 O  O     . LEU B 1 438 ? -8.338  -8.867  2.766   1 27.318  ? 430  LEU B O     1 
ATOM   7482 C  CB    . LEU B 1 438 ? -8.533  -5.945  4.254   1 17.426  ? 430  LEU B CB    1 
ATOM   7483 C  CG    . LEU B 1 438 ? -8.538  -5.125  5.554   1 16.516  ? 430  LEU B CG    1 
ATOM   7484 C  CD1   . LEU B 1 438 ? -7.457  -4.07   5.424   1 17.578  ? 430  LEU B CD1   1 
ATOM   7485 C  CD2   . LEU B 1 438 ? -9.864  -4.441  5.857   1 16.852  ? 430  LEU B CD2   1 
ATOM   7486 N  N     . ALA B 1 439 ? -9.989  -7.571  1.863   1 24.398  ? 431  ALA B N     1 
ATOM   7487 C  CA    . ALA B 1 439 ? -9.869  -7.981  0.47    1 22.877  ? 431  ALA B CA    1 
ATOM   7488 C  C     . ALA B 1 439 ? -9.666  -6.762  -0.429  1 22.062  ? 431  ALA B C     1 
ATOM   7489 O  O     . ALA B 1 439 ? -10.347 -5.744  -0.267  1 22.541  ? 431  ALA B O     1 
ATOM   7490 C  CB    . ALA B 1 439 ? -11.053 -8.846  0.068   1 23.39   ? 431  ALA B CB    1 
ATOM   7491 N  N     . HIS B 1 440 ? -8.674  -6.875  -1.331  1 22.065  ? 432  HIS B N     1 
ATOM   7492 C  CA    . HIS B 1 440 ? -8.532  -5.995  -2.478  1 21.872  ? 432  HIS B CA    1 
ATOM   7493 C  C     . HIS B 1 440 ? -9.01   -6.74   -3.717  1 22.315  ? 432  HIS B C     1 
ATOM   7494 O  O     . HIS B 1 440 ? -8.303  -7.601  -4.234  1 24.951  ? 432  HIS B O     1 
ATOM   7495 C  CB    . HIS B 1 440 ? -7.124  -5.386  -2.575  1 22.654  ? 432  HIS B CB    1 
ATOM   7496 C  CG    . HIS B 1 440 ? -6.983  -4.35   -3.654  1 22.237  ? 432  HIS B CG    1 
ATOM   7497 N  ND1   . HIS B 1 440 ? -5.736  -3.85   -3.965  1 21.884  ? 432  HIS B ND1   1 
ATOM   7498 C  CD2   . HIS B 1 440 ? -7.863  -3.675  -4.462  1 21.82   ? 432  HIS B CD2   1 
ATOM   7499 C  CE1   . HIS B 1 440 ? -5.856  -2.924  -4.919  1 22.863  ? 432  HIS B CE1   1 
ATOM   7500 N  NE2   . HIS B 1 440 ? -7.142  -2.808  -5.238  1 22.728  ? 432  HIS B NE2   1 
ATOM   7501 N  N     . TYR B 1 441 ? -10.224 -6.383  -4.15   1 21.638  ? 433  TYR B N     1 
ATOM   7502 C  CA    . TYR B 1 441 ? -10.87  -6.858  -5.362  1 21.833  ? 433  TYR B CA    1 
ATOM   7503 C  C     . TYR B 1 441 ? -10.586 -5.865  -6.485  1 22.527  ? 433  TYR B C     1 
ATOM   7504 O  O     . TYR B 1 441 ? -10.693 -4.659  -6.276  1 20.86   ? 433  TYR B O     1 
ATOM   7505 C  CB    . TYR B 1 441 ? -12.366 -7.141  -5.125  1 22.175  ? 433  TYR B CB    1 
ATOM   7506 C  CG    . TYR B 1 441 ? -13.158 -7.467  -6.391  1 23.902  ? 433  TYR B CG    1 
ATOM   7507 C  CD1   . TYR B 1 441 ? -13.056 -8.732  -7.006  1 23.404  ? 433  TYR B CD1   1 
ATOM   7508 C  CD2   . TYR B 1 441 ? -13.967 -6.491  -7.006  1 23.27   ? 433  TYR B CD2   1 
ATOM   7509 C  CE1   . TYR B 1 441 ? -13.72  -9.01   -8.2    1 25.005  ? 433  TYR B CE1   1 
ATOM   7510 C  CE2   . TYR B 1 441 ? -14.653 -6.772  -8.186  1 25.802  ? 433  TYR B CE2   1 
ATOM   7511 C  CZ    . TYR B 1 441 ? -14.533 -8.032  -8.779  1 26.655  ? 433  TYR B CZ    1 
ATOM   7512 O  OH    . TYR B 1 441 ? -15.231 -8.292  -9.928  1 25.181  ? 433  TYR B OH    1 
ATOM   7513 N  N     . LYS B 1 442 ? -10.258 -6.405  -7.672  1 23.112  ? 434  LYS B N     1 
ATOM   7514 C  CA    . LYS B 1 442 ? -10.073 -5.641  -8.898  1 23.95   ? 434  LYS B CA    1 
ATOM   7515 C  C     . LYS B 1 442 ? -10.961 -6.273  -9.973  1 27.307  ? 434  LYS B C     1 
ATOM   7516 O  O     . LYS B 1 442 ? -10.7   -7.412  -10.391 1 25.008  ? 434  LYS B O     1 
ATOM   7517 C  CB    . LYS B 1 442 ? -8.605  -5.577  -9.352  1 23.761  ? 434  LYS B CB    1 
ATOM   7518 C  CG    . LYS B 1 442 ? -7.583  -4.915  -8.456  1 24.229  ? 434  LYS B CG    1 
ATOM   7519 C  CD    . LYS B 1 442 ? -6.198  -4.853  -9.09   1 21.305  ? 434  LYS B CD    1 
ATOM   7520 C  CE    . LYS B 1 442 ? -5.249  -4.409  -8.038  1 22.185  ? 434  LYS B CE    1 
ATOM   7521 N  NZ    . LYS B 1 442 ? -3.944  -3.996  -8.561  1 22.364  ? 434  LYS B NZ    1 
ATOM   7522 N  N     . ARG B 1 443 ? -12.001 -5.52   -10.392 1 26.367  ? 435  ARG B N     1 
ATOM   7523 C  CA    . ARG B 1 443 ? -12.967 -5.946  -11.407 1 26.364  ? 435  ARG B CA    1 
ATOM   7524 C  C     . ARG B 1 443 ? -12.278 -6.262  -12.743 1 27.501  ? 435  ARG B C     1 
ATOM   7525 O  O     . ARG B 1 443 ? -12.491 -7.357  -13.268 1 28.499  ? 435  ARG B O     1 
ATOM   7526 C  CB    . ARG B 1 443 ? -14.19  -5.023  -11.487 1 23.329  ? 435  ARG B CB    1 
ATOM   7527 C  CG    . ARG B 1 443 ? -15.279 -5.492  -12.448 1 23.595  ? 435  ARG B CG    1 
ATOM   7528 C  CD    . ARG B 1 443 ? -16.456 -4.52   -12.605 1 23.515  ? 435  ARG B CD    1 
ATOM   7529 N  NE    . ARG B 1 443 ? -16.081 -3.153  -13.002 1 21.843  ? 435  ARG B NE    1 
ATOM   7530 C  CZ    . ARG B 1 443 ? -15.628 -2.73   -14.186 1 22.624  ? 435  ARG B CZ    1 
ATOM   7531 N  NH1   . ARG B 1 443 ? -15.671 -3.484  -15.278 1 23.436  ? 435  ARG B NH1   1 
ATOM   7532 N  NH2   . ARG B 1 443 ? -15.167 -1.5    -14.286 1 23.928  ? 435  ARG B NH2   1 
ATOM   7533 N  N     . LYS B 1 444 ? -11.445 -5.323  -13.229 1 28.131  ? 436  LYS B N     1 
ATOM   7534 C  CA    . LYS B 1 444 ? -10.788 -5.368  -14.54  1 30.568  ? 436  LYS B CA    1 
ATOM   7535 C  C     . LYS B 1 444 ? -9.91   -6.614  -14.681 1 29.401  ? 436  LYS B C     1 
ATOM   7536 O  O     . LYS B 1 444 ? -10.094 -7.375  -15.627 1 25.721  ? 436  LYS B O     1 
ATOM   7537 C  CB    . LYS B 1 444 ? -10.127 -4.043  -14.932 1 29.297  ? 436  LYS B CB    1 
ATOM   7538 C  CG    . LYS B 1 444 ? -11.159 -3.014  -15.382 1 33.628  ? 436  LYS B CG    1 
ATOM   7539 C  CD    . LYS B 1 444 ? -10.617 -1.596  -15.481 1 36.065  ? 436  LYS B CD    1 
ATOM   7540 C  CE    . LYS B 1 444 ? -11.617 -0.537  -15.749 1 35.953  ? 436  LYS B CE    1 
ATOM   7541 N  NZ    . LYS B 1 444 ? -10.812 0.679   -15.859 1 39.447  ? 436  LYS B NZ    1 
ATOM   7542 N  N     . GLU B 1 445 ? -9.063  -6.853  -13.668 1 32.568  ? 437  GLU B N     1 
ATOM   7543 C  CA    . GLU B 1 445 ? -8.181  -8.01   -13.568 1 32.13   ? 437  GLU B CA    1 
ATOM   7544 C  C     . GLU B 1 445 ? -8.948  -9.286  -13.202 1 30.791  ? 437  GLU B C     1 
ATOM   7545 O  O     . GLU B 1 445 ? -8.483  -10.367 -13.549 1 35.252  ? 437  GLU B O     1 
ATOM   7546 C  CB    . GLU B 1 445 ? -6.946  -7.778  -12.693 1 32.624  ? 437  GLU B CB    1 
ATOM   7547 C  CG    . GLU B 1 445 ? -5.984  -6.721  -13.234 1 36.462  ? 437  GLU B CG    1 
ATOM   7548 C  CD    . GLU B 1 445 ? -6.303  -5.235  -13.068 1 40.263  ? 437  GLU B CD    1 
ATOM   7549 O  OE1   . GLU B 1 445 ? -7.381  -4.851  -12.549 1 41.759  ? 437  GLU B OE1   1 
ATOM   7550 O  OE2   . GLU B 1 445 ? -5.438  -4.434  -13.473 1 40.668  ? 437  GLU B OE2   1 
ATOM   7551 N  N     . GLY B 1 446 ? -10.095 -9.169  -12.507 1 30.058  ? 438  GLY B N     1 
ATOM   7552 C  CA    . GLY B 1 446 ? -10.822 -10.289 -11.915 1 30.364  ? 438  GLY B CA    1 
ATOM   7553 C  C     . GLY B 1 446 ? -10.051 -10.989 -10.782 1 30.85   ? 438  GLY B C     1 
ATOM   7554 O  O     . GLY B 1 446 ? -10.26  -12.187 -10.578 1 33.029  ? 438  GLY B O     1 
ATOM   7555 N  N     . THR B 1 447 ? -9.206  -10.238 -10.045 1 27.961  ? 439  THR B N     1 
ATOM   7556 C  CA    . THR B 1 447 ? -8.336  -10.745 -8.981  1 28.197  ? 439  THR B CA    1 
ATOM   7557 C  C     . THR B 1 447 ? -8.859  -10.301 -7.61   1 27.615  ? 439  THR B C     1 
ATOM   7558 O  O     . THR B 1 447 ? -9.417  -9.208  -7.49   1 26.287  ? 439  THR B O     1 
ATOM   7559 C  CB    . THR B 1 447 ? -6.866  -10.341 -9.182  1 27.083  ? 439  THR B CB    1 
ATOM   7560 O  OG1   . THR B 1 447 ? -6.755  -8.92   -9.144  1 25.786  ? 439  THR B OG1   1 
ATOM   7561 C  CG2   . THR B 1 447 ? -6.209  -10.906 -10.436 1 26.628  ? 439  THR B CG2   1 
ATOM   7562 N  N     . THR B 1 448 ? -8.642  -11.155 -6.588  1 27.847  ? 440  THR B N     1 
ATOM   7563 C  CA    . THR B 1 448 ? -8.804  -10.819 -5.173  1 26.86   ? 440  THR B CA    1 
ATOM   7564 C  C     . THR B 1 448 ? -7.523  -11.172 -4.406  1 27.104  ? 440  THR B C     1 
ATOM   7565 O  O     . THR B 1 448 ? -7.046  -12.306 -4.487  1 27.653  ? 440  THR B O     1 
ATOM   7566 C  CB    . THR B 1 448 ? -10.067 -11.428 -4.546  1 26.103  ? 440  THR B CB    1 
ATOM   7567 O  OG1   . THR B 1 448 ? -11.185 -11.131 -5.372  1 27.052  ? 440  THR B OG1   1 
ATOM   7568 C  CG2   . THR B 1 448 ? -10.412 -10.828 -3.19   1 26.143  ? 440  THR B CG2   1 
ATOM   7569 N  N     . GLU B 1 449 ? -7.03   -10.18  -3.64   1 25.033  ? 441  GLU B N     1 
ATOM   7570 C  CA    . GLU B 1 449 ? -5.905  -10.268 -2.708  1 24.496  ? 441  GLU B CA    1 
ATOM   7571 C  C     . GLU B 1 449 ? -6.4    -10.102 -1.269  1 24.562  ? 441  GLU B C     1 
ATOM   7572 O  O     . GLU B 1 449 ? -7.322  -9.331  -1.032  1 24.057  ? 441  GLU B O     1 
ATOM   7573 C  CB    . GLU B 1 449 ? -4.861  -9.212  -3.083  1 26.631  ? 441  GLU B CB    1 
ATOM   7574 C  CG    . GLU B 1 449 ? -4.143  -9.48   -4.405  1 29.507  ? 441  GLU B CG    1 
ATOM   7575 C  CD    . GLU B 1 449 ? -3.391  -8.272  -4.912  1 35.655  ? 441  GLU B CD    1 
ATOM   7576 O  OE1   . GLU B 1 449 ? -2.161  -8.333  -4.764  1 42.653  ? 441  GLU B OE1   1 
ATOM   7577 O  OE2   . GLU B 1 449 ? -3.988  -7.301  -5.441  1 36.257  ? 441  GLU B OE2   1 
ATOM   7578 N  N     . TRP B 1 450 ? -5.749  -10.784 -0.309  1 24.597  ? 442  TRP B N     1 
ATOM   7579 C  CA    . TRP B 1 450 ? -6.239  -10.987 1.054   1 23.139  ? 442  TRP B CA    1 
ATOM   7580 C  C     . TRP B 1 450 ? -5.213  -10.537 2.096   1 22.996  ? 442  TRP B C     1 
ATOM   7581 O  O     . TRP B 1 450 ? -4.024  -10.84  1.951   1 22.354  ? 442  TRP B O     1 
ATOM   7582 C  CB    . TRP B 1 450 ? -6.64   -12.452 1.275   1 24.724  ? 442  TRP B CB    1 
ATOM   7583 C  CG    . TRP B 1 450 ? -7.651  -12.967 0.279   1 28.59   ? 442  TRP B CG    1 
ATOM   7584 C  CD1   . TRP B 1 450 ? -7.358  -13.549 -0.922  1 29.585  ? 442  TRP B CD1   1 
ATOM   7585 C  CD2   . TRP B 1 450 ? -9.094  -12.971 0.393   1 28.208  ? 442  TRP B CD2   1 
ATOM   7586 N  NE1   . TRP B 1 450 ? -8.509  -13.913 -1.57   1 31.853  ? 442  TRP B NE1   1 
ATOM   7587 C  CE2   . TRP B 1 450 ? -9.59   -13.586 -0.791  1 29.716  ? 442  TRP B CE2   1 
ATOM   7588 C  CE3   . TRP B 1 450 ? -10.018 -12.535 1.37    1 29.035  ? 442  TRP B CE3   1 
ATOM   7589 C  CZ2   . TRP B 1 450 ? -10.961 -13.767 -1.025  1 30.305  ? 442  TRP B CZ2   1 
ATOM   7590 C  CZ3   . TRP B 1 450 ? -11.377 -12.709 1.135   1 30.182  ? 442  TRP B CZ3   1 
ATOM   7591 C  CH2   . TRP B 1 450 ? -11.841 -13.322 -0.049  1 32.04   ? 442  TRP B CH2   1 
ATOM   7592 N  N     . TYR B 1 451 ? -5.701  -9.779  3.101   1 22.061  ? 443  TYR B N     1 
ATOM   7593 C  CA    . TYR B 1 451 ? -4.988  -9.422  4.327   1 21.721  ? 443  TYR B CA    1 
ATOM   7594 C  C     . TYR B 1 451 ? -5.687  -10.084 5.509   1 21.842  ? 443  TYR B C     1 
ATOM   7595 O  O     . TYR B 1 451 ? -6.877  -9.858  5.708   1 23.77   ? 443  TYR B O     1 
ATOM   7596 C  CB    . TYR B 1 451 ? -4.764  -7.918  4.553   1 21.595  ? 443  TYR B CB    1 
ATOM   7597 C  CG    . TYR B 1 451 ? -4.008  -7.59   5.835   1 25.212  ? 443  TYR B CG    1 
ATOM   7598 C  CD1   . TYR B 1 451 ? -2.602  -7.693  5.902   1 25.71   ? 443  TYR B CD1   1 
ATOM   7599 C  CD2   . TYR B 1 451 ? -4.698  -7.211  6.999   1 23.702  ? 443  TYR B CD2   1 
ATOM   7600 C  CE1   . TYR B 1 451 ? -1.908  -7.405  7.081   1 26.118  ? 443  TYR B CE1   1 
ATOM   7601 C  CE2   . TYR B 1 451 ? -4.011  -6.945  8.184   1 26.752  ? 443  TYR B CE2   1 
ATOM   7602 C  CZ    . TYR B 1 451 ? -2.617  -7.043  8.225   1 26.234  ? 443  TYR B CZ    1 
ATOM   7603 O  OH    . TYR B 1 451 ? -1.947  -6.772  9.384   1 25.552  ? 443  TYR B OH    1 
ATOM   7604 N  N     . TYR B 1 452 ? -4.922  -10.848 6.303   1 21.331  ? 444  TYR B N     1 
ATOM   7605 C  CA    . TYR B 1 452 ? -5.407  -11.441 7.549   1 24.32   ? 444  TYR B CA    1 
ATOM   7606 C  C     . TYR B 1 452 ? -5.001  -10.558 8.737   1 24.645  ? 444  TYR B C     1 
ATOM   7607 O  O     . TYR B 1 452 ? -3.823  -10.271 8.869   1 24.327  ? 444  TYR B O     1 
ATOM   7608 C  CB    . TYR B 1 452 ? -4.959  -12.907 7.632   1 23.433  ? 444  TYR B CB    1 
ATOM   7609 C  CG    . TYR B 1 452 ? -5.295  -13.623 8.934   1 23.976  ? 444  TYR B CG    1 
ATOM   7610 C  CD1   . TYR B 1 452 ? -6.637  -13.85  9.314   1 25.87   ? 444  TYR B CD1   1 
ATOM   7611 C  CD2   . TYR B 1 452 ? -4.274  -14.082 9.784   1 24.732  ? 444  TYR B CD2   1 
ATOM   7612 C  CE1   . TYR B 1 452 ? -6.962  -14.496 10.506  1 25.173  ? 444  TYR B CE1   1 
ATOM   7613 C  CE2   . TYR B 1 452 ? -4.588  -14.761 10.965  1 26.13   ? 444  TYR B CE2   1 
ATOM   7614 C  CZ    . TYR B 1 452 ? -5.928  -14.954 11.321  1 25.816  ? 444  TYR B CZ    1 
ATOM   7615 O  OH    . TYR B 1 452 ? -6.261  -15.61  12.464  1 26.141  ? 444  TYR B OH    1 
ATOM   7616 N  N     . ALA B 1 453 ? -5.971  -10.165 9.598   1 25.824  ? 445  ALA B N     1 
ATOM   7617 C  CA    . ALA B 1 453 ? -5.747  -9.265  10.735  1 24.291  ? 445  ALA B CA    1 
ATOM   7618 C  C     . ALA B 1 453 ? -4.804  -9.844  11.793  1 25.93   ? 445  ALA B C     1 
ATOM   7619 O  O     . ALA B 1 453 ? -4.095  -9.061  12.426  1 24.186  ? 445  ALA B O     1 
ATOM   7620 C  CB    . ALA B 1 453 ? -7.026  -8.766  11.366  1 21.595  ? 445  ALA B CB    1 
ATOM   7621 N  N     . GLY B 1 454 ? -4.798  -11.186 11.944  1 26.926  ? 446  GLY B N     1 
ATOM   7622 C  CA    . GLY B 1 454 ? -4.059  -11.914 12.968  1 26.284  ? 446  GLY B CA    1 
ATOM   7623 C  C     . GLY B 1 454 ? -4.994  -12.767 13.825  1 28.143  ? 446  GLY B C     1 
ATOM   7624 O  O     . GLY B 1 454 ? -6.203  -12.53  13.851  1 29.141  ? 446  GLY B O     1 
ATOM   7625 N  N     . ASP B 1 455 ? -4.425  -13.787 14.503  1 30.574  ? 447  ASP B N     1 
ATOM   7626 C  CA    . ASP B 1 455 ? -5.141  -14.577 15.51   1 33.665  ? 447  ASP B CA    1 
ATOM   7627 C  C     . ASP B 1 455 ? -5.508  -13.667 16.681  1 30.861  ? 447  ASP B C     1 
ATOM   7628 O  O     . ASP B 1 455 ? -4.693  -12.811 17.06   1 28.935  ? 447  ASP B O     1 
ATOM   7629 C  CB    . ASP B 1 455 ? -4.347  -15.782 16.008  1 38.763  ? 447  ASP B CB    1 
ATOM   7630 C  CG    . ASP B 1 455 ? -3.894  -16.861 15.022  1 41.125  ? 447  ASP B CG    1 
ATOM   7631 O  OD1   . ASP B 1 455 ? -4.278  -16.846 13.831  1 45.358  ? 447  ASP B OD1   1 
ATOM   7632 O  OD2   . ASP B 1 455 ? -3.116  -17.724 15.453  1 45.271  ? 447  ASP B OD2   1 
ATOM   7633 N  N     . ASN B 1 456 ? -6.749  -13.831 17.189  1 28.873  ? 448  ASN B N     1 
ATOM   7634 C  CA    . ASN B 1 456 ? -7.352  -13.056 18.282  1 30.876  ? 448  ASN B CA    1 
ATOM   7635 C  C     . ASN B 1 456 ? -7.41   -11.561 17.92   1 31.629  ? 448  ASN B C     1 
ATOM   7636 O  O     . ASN B 1 456 ? -7.169  -10.691 18.769  1 34.22   ? 448  ASN B O     1 
ATOM   7637 C  CB    . ASN B 1 456 ? -6.719  -13.337 19.653  1 31.948  ? 448  ASN B CB    1 
ATOM   7638 C  CG    . ASN B 1 456 ? -6.473  -14.798 19.961  1 35.516  ? 448  ASN B CG    1 
ATOM   7639 O  OD1   . ASN B 1 456 ? -5.329  -15.251 19.885  1 40.009  ? 448  ASN B OD1   1 
ATOM   7640 N  ND2   . ASN B 1 456 ? -7.504  -15.557 20.304  1 40.213  ? 448  ASN B ND2   1 
ATOM   7641 N  N     . CYS B 1 457 ? -7.666  -11.28  16.63   1 28.603  ? 449  CYS B N     1 
ATOM   7642 C  CA    . CYS B 1 457 ? -7.76   -9.935  16.078  1 28.033  ? 449  CYS B CA    1 
ATOM   7643 C  C     . CYS B 1 457 ? -9.022  -9.801  15.238  1 24.957  ? 449  CYS B C     1 
ATOM   7644 O  O     . CYS B 1 457 ? -9.423  -10.741 14.552  1 26.004  ? 449  CYS B O     1 
ATOM   7645 C  CB    . CYS B 1 457 ? -6.554  -9.54   15.222  1 29.447  ? 449  CYS B CB    1 
ATOM   7646 S  SG    . CYS B 1 457 ? -4.957  -9.571  16.079  1 31.598  ? 449  CYS B SG    1 
ATOM   7647 N  N     . LEU B 1 458 ? -9.614  -8.606  15.32   1 23.615  ? 450  LEU B N     1 
ATOM   7648 C  CA    . LEU B 1 458 ? -10.59  -8.103  14.359  1 25.406  ? 450  LEU B CA    1 
ATOM   7649 C  C     . LEU B 1 458 ? -9.986  -6.898  13.642  1 23.766  ? 450  LEU B C     1 
ATOM   7650 O  O     . LEU B 1 458 ? -9.036  -6.297  14.159  1 25.099  ? 450  LEU B O     1 
ATOM   7651 C  CB    . LEU B 1 458 ? -11.948 -7.798  15.01   1 25.118  ? 450  LEU B CB    1 
ATOM   7652 C  CG    . LEU B 1 458 ? -12.709 -8.953  15.678  1 26.717  ? 450  LEU B CG    1 
ATOM   7653 C  CD1   . LEU B 1 458 ? -13.844 -8.388  16.522  1 27.577  ? 450  LEU B CD1   1 
ATOM   7654 C  CD2   . LEU B 1 458 ? -13.266 -10.034 14.753  1 27.19   ? 450  LEU B CD2   1 
ATOM   7655 N  N     . ILE B 1 459 ? -10.54  -6.584  12.458  1 22.843  ? 451  ILE B N     1 
ATOM   7656 C  CA    . ILE B 1 459 ? -10.168 -5.424  11.646  1 20.265  ? 451  ILE B CA    1 
ATOM   7657 C  C     . ILE B 1 459 ? -11.438 -4.717  11.165  1 19.585  ? 451  ILE B C     1 
ATOM   7658 O  O     . ILE B 1 459 ? -12.45  -5.362  10.859  1 19.531  ? 451  ILE B O     1 
ATOM   7659 C  CB    . ILE B 1 459 ? -9.149  -5.776  10.532  1 20.175  ? 451  ILE B CB    1 
ATOM   7660 C  CG1   . ILE B 1 459 ? -8.387  -4.534  9.991   1 19.639  ? 451  ILE B CG1   1 
ATOM   7661 C  CG2   . ILE B 1 459 ? -9.787  -6.611  9.412   1 19.122  ? 451  ILE B CG2   1 
ATOM   7662 C  CD1   . ILE B 1 459 ? -7.154  -4.829  9.14    1 19.532  ? 451  ILE B CD1   1 
ATOM   7663 N  N     . GLN B 1 460 ? -11.352 -3.382  11.113  1 18.528  ? 452  GLN B N     1 
ATOM   7664 C  CA    . GLN B 1 460 ? -12.465 -2.507  10.746  1 17.85   ? 452  GLN B CA    1 
ATOM   7665 C  C     . GLN B 1 460 ? -12.278 -2.029  9.302   1 18.448  ? 452  GLN B C     1 
ATOM   7666 O  O     . GLN B 1 460 ? -11.327 -2.456  8.632   1 18.053  ? 452  GLN B O     1 
ATOM   7667 C  CB    . GLN B 1 460 ? -12.556 -1.445  11.841  1 16.792  ? 452  GLN B CB    1 
ATOM   7668 C  CG    . GLN B 1 460 ? -12.981 -1.972  13.213  1 16.868  ? 452  GLN B CG    1 
ATOM   7669 C  CD    . GLN B 1 460 ? -12.677 -1.011  14.339  1 17.072  ? 452  GLN B CD    1 
ATOM   7670 O  OE1   . GLN B 1 460 ? -13.05  0.169   14.299  1 17.325  ? 452  GLN B OE1   1 
ATOM   7671 N  NE2   . GLN B 1 460 ? -11.985 -1.513  15.354  1 16.154  ? 452  GLN B NE2   1 
ATOM   7672 N  N     . GLU B 1 461 ? -13.181 -1.128  8.852   1 17.585  ? 453  GLU B N     1 
ATOM   7673 C  CA    . GLU B 1 461 ? -13.297 -0.62   7.492   1 19.008  ? 453  GLU B CA    1 
ATOM   7674 C  C     . GLU B 1 461 ? -11.962 -0.081  6.941   1 20.88   ? 453  GLU B C     1 
ATOM   7675 O  O     . GLU B 1 461 ? -11.358 0.809   7.574   1 19.747  ? 453  GLU B O     1 
ATOM   7676 C  CB    . GLU B 1 461 ? -14.392 0.446   7.422   1 18.86   ? 453  GLU B CB    1 
ATOM   7677 C  CG    . GLU B 1 461 ? -14.548 1.069   6.037   1 18.978  ? 453  GLU B CG    1 
ATOM   7678 C  CD    . GLU B 1 461 ? -15.386 2.315   6.056   1 20.011  ? 453  GLU B CD    1 
ATOM   7679 O  OE1   . GLU B 1 461 ? -15.042 3.23    6.839   1 19.788  ? 453  GLU B OE1   1 
ATOM   7680 O  OE2   . GLU B 1 461 ? -16.347 2.365   5.254   1 19.881  ? 453  GLU B OE2   1 
ATOM   7681 N  N     . PRO B 1 462 ? -11.513 -0.539  5.73    1 20.998  ? 454  PRO B N     1 
ATOM   7682 C  CA    . PRO B 1 462 ? -10.338 0.042   5.084   1 20.049  ? 454  PRO B CA    1 
ATOM   7683 C  C     . PRO B 1 462 ? -10.62  1.412   4.469   1 21.143  ? 454  PRO B C     1 
ATOM   7684 O  O     . PRO B 1 462 ? -11.751 1.698   4.037   1 20.326  ? 454  PRO B O     1 
ATOM   7685 C  CB    . PRO B 1 462 ? -9.92   -1.028  4.096   1 19.669  ? 454  PRO B CB    1 
ATOM   7686 C  CG    . PRO B 1 462 ? -11.253 -1.646  3.695   1 19.235  ? 454  PRO B CG    1 
ATOM   7687 C  CD    . PRO B 1 462 ? -12.128 -1.597  4.894   1 19.587  ? 454  PRO B CD    1 
ATOM   7688 N  N     . VAL B 1 463 ? -9.566  2.241   4.462   1 20.95   ? 455  VAL B N     1 
ATOM   7689 C  CA    . VAL B 1 463 ? -9.494  3.496   3.712   1 20.145  ? 455  VAL B CA    1 
ATOM   7690 C  C     . VAL B 1 463 ? -8.241  3.448   2.829   1 19.837  ? 455  VAL B C     1 
ATOM   7691 O  O     . VAL B 1 463 ? -7.237  2.854   3.223   1 18.441  ? 455  VAL B O     1 
ATOM   7692 C  CB    . VAL B 1 463 ? -9.612  4.789   4.559   1 19.022  ? 455  VAL B CB    1 
ATOM   7693 C  CG1   . VAL B 1 463 ? -10.913 4.843   5.358   1 17.991  ? 455  VAL B CG1   1 
ATOM   7694 C  CG2   . VAL B 1 463 ? -8.432  5.014   5.499   1 17.539  ? 455  VAL B CG2   1 
ATOM   7695 N  N     . PHE B 1 464 ? -8.306  4.123   1.67    1 21.441  ? 456  PHE B N     1 
ATOM   7696 C  CA    . PHE B 1 464 ? -7.242  4.157   0.677   1 22.005  ? 456  PHE B CA    1 
ATOM   7697 C  C     . PHE B 1 464 ? -6.707  5.578   0.517   1 23.326  ? 456  PHE B C     1 
ATOM   7698 O  O     . PHE B 1 464 ? -7.47   6.543   0.47    1 24.367  ? 456  PHE B O     1 
ATOM   7699 C  CB    . PHE B 1 464 ? -7.702  3.447   -0.606  1 24.259  ? 456  PHE B CB    1 
ATOM   7700 C  CG    . PHE B 1 464 ? -6.744  3.57    -1.786  1 23.373  ? 456  PHE B CG    1 
ATOM   7701 C  CD1   . PHE B 1 464 ? -5.633  2.712   -1.907  1 22.234  ? 456  PHE B CD1   1 
ATOM   7702 C  CD2   . PHE B 1 464 ? -6.937  4.573   -2.753  1 23.244  ? 456  PHE B CD2   1 
ATOM   7703 C  CE1   . PHE B 1 464 ? -4.744  2.837   -2.978  1 23.143  ? 456  PHE B CE1   1 
ATOM   7704 C  CE2   . PHE B 1 464 ? -6.046  4.715   -3.823  1 22.875  ? 456  PHE B CE2   1 
ATOM   7705 C  CZ    . PHE B 1 464 ? -4.951  3.853   -3.933  1 24.874  ? 456  PHE B CZ    1 
ATOM   7706 N  N     . SER B 1 465 ? -5.371  5.657   0.418   1 23.603  ? 457  SER B N     1 
ATOM   7707 C  CA    . SER B 1 465 ? -4.625  6.836   0.003   1 24.168  ? 457  SER B CA    1 
ATOM   7708 C  C     . SER B 1 465 ? -3.759  6.476   -1.207  1 23.561  ? 457  SER B C     1 
ATOM   7709 O  O     . SER B 1 465 ? -2.978  5.521   -1.097  1 22.012  ? 457  SER B O     1 
ATOM   7710 C  CB    . SER B 1 465 ? -3.78   7.407   1.14    1 24.691  ? 457  SER B CB    1 
ATOM   7711 O  OG    . SER B 1 465 ? -3.09   8.572   0.708   1 26.531  ? 457  SER B OG    1 
ATOM   7712 N  N     . PRO B 1 466 ? -3.853  7.201   -2.367  1 23.859  ? 458  PRO B N     1 
ATOM   7713 C  CA    . PRO B 1 466 ? -2.993  6.919   -3.515  1 24.488  ? 458  PRO B CA    1 
ATOM   7714 C  C     . PRO B 1 466 ? -1.527  7.261   -3.24   1 24.958  ? 458  PRO B C     1 
ATOM   7715 O  O     . PRO B 1 466 ? -1.266  8.222   -2.509  1 21.313  ? 458  PRO B O     1 
ATOM   7716 C  CB    . PRO B 1 466 ? -3.623  7.713   -4.655  1 24.179  ? 458  PRO B CB    1 
ATOM   7717 C  CG    . PRO B 1 466 ? -4.288  8.884   -3.959  1 25.652  ? 458  PRO B CG    1 
ATOM   7718 C  CD    . PRO B 1 466 ? -4.768  8.337   -2.639  1 25.349  ? 458  PRO B CD    1 
ATOM   7719 N  N     . ARG B 1 467 ? -0.618  6.471   -3.843  1 25.817  ? 459  ARG B N     1 
ATOM   7720 C  CA    . ARG B 1 467 ? 0.838   6.625   -3.763  1 27.06   ? 459  ARG B CA    1 
ATOM   7721 C  C     . ARG B 1 467 ? 1.289   8.053   -4.094  1 27.541  ? 459  ARG B C     1 
ATOM   7722 O  O     . ARG B 1 467 ? 2.147   8.595   -3.402  1 28.325  ? 459  ARG B O     1 
ATOM   7723 C  CB    . ARG B 1 467 ? 1.594   5.619   -4.637  1 26.421  ? 459  ARG B CB    1 
ATOM   7724 C  CG    . ARG B 1 467 ? 3.057   5.417   -4.232  1 24.345  ? 459  ARG B CG    1 
ATOM   7725 C  CD    . ARG B 1 467 ? 3.71    4.322   -5.055  1 24.182  ? 459  ARG B CD    1 
ATOM   7726 N  NE    . ARG B 1 467 ? 3.044   3.021   -4.899  1 24.268  ? 459  ARG B NE    1 
ATOM   7727 C  CZ    . ARG B 1 467 ? 3       2.191   -3.863  1 25.26   ? 459  ARG B CZ    1 
ATOM   7728 N  NH1   . ARG B 1 467 ? 3.84    2.304   -2.852  1 25.434  ? 459  ARG B NH1   1 
ATOM   7729 N  NH2   . ARG B 1 467 ? 2.107   1.212   -3.865  1 26.097  ? 459  ARG B NH2   1 
ATOM   7730 N  N     . SER B 1 468 ? 0.721   8.61    -5.169  1 27.712  ? 460  SER B N     1 
ATOM   7731 C  CA    . SER B 1 468 ? 0.788   10.003  -5.599  1 31.747  ? 460  SER B CA    1 
ATOM   7732 C  C     . SER B 1 468 ? -0.5    10.324  -6.362  1 32.265  ? 460  SER B C     1 
ATOM   7733 O  O     . SER B 1 468 ? -1.263  9.4     -6.665  1 26.889  ? 460  SER B O     1 
ATOM   7734 C  CB    . SER B 1 468 ? 2.037   10.249  -6.426  1 30.852  ? 460  SER B CB    1 
ATOM   7735 O  OG    . SER B 1 468 ? 1.986   9.419   -7.575  1 33.346  ? 460  SER B OG    1 
ATOM   7736 N  N     . LYS B 1 469 ? -0.725  11.62   -6.67   1 36.907  ? 461  LYS B N     1 
ATOM   7737 C  CA    . LYS B 1 469 ? -1.944  12.159  -7.288  1 40.509  ? 461  LYS B CA    1 
ATOM   7738 C  C     . LYS B 1 469 ? -2.318  11.429  -8.589  1 39.764  ? 461  LYS B C     1 
ATOM   7739 O  O     . LYS B 1 469 ? -3.497  11.137  -8.813  1 35.056  ? 461  LYS B O     1 
ATOM   7740 C  CB    . LYS B 1 469 ? -1.9    13.685  -7.469  1 43.626  ? 461  LYS B CB    1 
ATOM   7741 C  CG    . LYS B 1 469 ? -2.173  14.579  -6.244  1 55.359  ? 461  LYS B CG    1 
ATOM   7742 C  CD    . LYS B 1 469 ? -1.15   14.7    -5.105  1 63.904  ? 461  LYS B CD    1 
ATOM   7743 C  CE    . LYS B 1 469 ? 0.159   15.414  -5.358  1 67.615  ? 461  LYS B CE    1 
ATOM   7744 N  NZ    . LYS B 1 469 ? 0.004   16.832  -5.708  1 69.605  ? 461  LYS B NZ    1 
ATOM   7745 N  N     . ASP B 1 470 ? -1.285  11.073  -9.372  1 40.545  ? 462  ASP B N     1 
ATOM   7746 C  CA    . ASP B 1 470 ? -1.361  10.515  -10.714 1 42.603  ? 462  ASP B CA    1 
ATOM   7747 C  C     . ASP B 1 470 ? -1.056  9.004   -10.743 1 37.822  ? 462  ASP B C     1 
ATOM   7748 O  O     . ASP B 1 470 ? -0.987  8.449   -11.843 1 37.958  ? 462  ASP B O     1 
ATOM   7749 C  CB    . ASP B 1 470 ? -0.505  11.373  -11.645 1 50.537  ? 462  ASP B CB    1 
ATOM   7750 C  CG    . ASP B 1 470 ? 0.996   11.498  -11.347 1 59.799  ? 462  ASP B CG    1 
ATOM   7751 O  OD1   . ASP B 1 470 ? 1.527   10.86   -10.383 1 52.821  ? 462  ASP B OD1   1 
ATOM   7752 O  OD2   . ASP B 1 470 ? 1.655   12.263  -12.085 1 63.934  ? 462  ASP B OD2   1 
ATOM   7753 N  N     . ALA B 1 471 ? -0.884  8.346   -9.567  1 30.456  ? 463  ALA B N     1 
ATOM   7754 C  CA    . ALA B 1 471 ? -0.656  6.902   -9.442  1 28.332  ? 463  ALA B CA    1 
ATOM   7755 C  C     . ALA B 1 471 ? -1.837  6.109   -10.026 1 27.64   ? 463  ALA B C     1 
ATOM   7756 O  O     . ALA B 1 471 ? -2.96   6.622   -9.946  1 27.168  ? 463  ALA B O     1 
ATOM   7757 C  CB    . ALA B 1 471 ? -0.397  6.509   -7.995  1 28.939  ? 463  ALA B CB    1 
ATOM   7758 N  N     . PRO B 1 472 ? -1.659  4.882   -10.626 1 24.914  ? 464  PRO B N     1 
ATOM   7759 C  CA    . PRO B 1 472 ? -2.784  4.076   -11.129 1 25.296  ? 464  PRO B CA    1 
ATOM   7760 C  C     . PRO B 1 472 ? -3.848  3.754   -10.079 1 24.018  ? 464  PRO B C     1 
ATOM   7761 O  O     . PRO B 1 472 ? -3.578  3.854   -8.887  1 26.29   ? 464  PRO B O     1 
ATOM   7762 C  CB    . PRO B 1 472 ? -2.142  2.818   -11.727 1 23.614  ? 464  PRO B CB    1 
ATOM   7763 C  CG    . PRO B 1 472 ? -0.73   3.273   -12.027 1 23.628  ? 464  PRO B CG    1 
ATOM   7764 C  CD    . PRO B 1 472 ? -0.378  4.183   -10.881 1 24.101  ? 464  PRO B CD    1 
ATOM   7765 N  N     . GLU B 1 473 ? -5.055  3.421   -10.538 1 24.608  ? 465  GLU B N     1 
ATOM   7766 C  CA    . GLU B 1 473 ? -6.197  3.072   -9.695  1 24.177  ? 465  GLU B CA    1 
ATOM   7767 C  C     . GLU B 1 473 ? -5.812  1.966   -8.71   1 23.549  ? 465  GLU B C     1 
ATOM   7768 O  O     . GLU B 1 473 ? -5.278  0.934   -9.126  1 23.922  ? 465  GLU B O     1 
ATOM   7769 C  CB    . GLU B 1 473 ? -7.383  2.605   -10.537 1 23.886  ? 465  GLU B CB    1 
ATOM   7770 C  CG    . GLU B 1 473 ? -8.645  2.417   -9.696  1 24.739  ? 465  GLU B CG    1 
ATOM   7771 C  CD    . GLU B 1 473 ? -9.927  1.987   -10.358 1 24.815  ? 465  GLU B CD    1 
ATOM   7772 O  OE1   . GLU B 1 473 ? -9.969  2.003   -11.598 1 22.209  ? 465  GLU B OE1   1 
ATOM   7773 O  OE2   . GLU B 1 473 ? -10.867 1.627   -9.609  1 25.927  ? 465  GLU B OE2   1 
ATOM   7774 N  N     . GLY B 1 474 ? -6.062  2.241   -7.415  1 23.757  ? 466  GLY B N     1 
ATOM   7775 C  CA    . GLY B 1 474 ? -5.813  1.308   -6.317  1 22.993  ? 466  GLY B CA    1 
ATOM   7776 C  C     . GLY B 1 474 ? -4.326  1.054   -6.03   1 22.116  ? 466  GLY B C     1 
ATOM   7777 O  O     . GLY B 1 474 ? -4.002  0.064   -5.376  1 22.896  ? 466  GLY B O     1 
ATOM   7778 N  N     . ASP B 1 475 ? -3.445  1.961   -6.48   1 22.901  ? 467  ASP B N     1 
ATOM   7779 C  CA    . ASP B 1 475 ? -2.025  1.938   -6.151  1 23.643  ? 467  ASP B CA    1 
ATOM   7780 C  C     . ASP B 1 475 ? -1.715  2.948   -5.04   1 22.393  ? 467  ASP B C     1 
ATOM   7781 O  O     . ASP B 1 475 ? -1.8    4.161   -5.238  1 25.379  ? 467  ASP B O     1 
ATOM   7782 C  CB    . ASP B 1 475 ? -1.129  2.01    -7.382  1 24.953  ? 467  ASP B CB    1 
ATOM   7783 C  CG    . ASP B 1 475 ? 0.353   1.961   -7.044  1 24.882  ? 467  ASP B CG    1 
ATOM   7784 O  OD1   . ASP B 1 475 ? 0.812   0.901   -6.574  1 25.866  ? 467  ASP B OD1   1 
ATOM   7785 O  OD2   . ASP B 1 475 ? 1       3.016   -7.152  1 25.318  ? 467  ASP B OD2   1 
ATOM   7786 N  N     . GLY B 1 476 ? -1.352  2.411   -3.873  1 20.791  ? 468  GLY B N     1 
ATOM   7787 C  CA    . GLY B 1 476 ? -0.962  3.208   -2.719  1 21.061  ? 468  GLY B CA    1 
ATOM   7788 C  C     . GLY B 1 476 ? -1.069  2.401   -1.435  1 21.563  ? 468  GLY B C     1 
ATOM   7789 O  O     . GLY B 1 476 ? -0.58   1.265   -1.386  1 19.73   ? 468  GLY B O     1 
ATOM   7790 N  N     . PHE B 1 477 ? -1.763  3.011   -0.454  1 21.622  ? 469  PHE B N     1 
ATOM   7791 C  CA    . PHE B 1 477 ? -1.747  2.592   0.946   1 22.798  ? 469  PHE B CA    1 
ATOM   7792 C  C     . PHE B 1 477 ? -3.17   2.433   1.46    1 21.979  ? 469  PHE B C     1 
ATOM   7793 O  O     . PHE B 1 477 ? -4.025  3.272   1.188   1 21.143  ? 469  PHE B O     1 
ATOM   7794 C  CB    . PHE B 1 477 ? -0.889  3.479   1.857   1 22.514  ? 469  PHE B CB    1 
ATOM   7795 C  CG    . PHE B 1 477 ? 0.528   3.66    1.322   1 22.519  ? 469  PHE B CG    1 
ATOM   7796 C  CD1   . PHE B 1 477 ? 1.507   2.673   1.539   1 25.067  ? 469  PHE B CD1   1 
ATOM   7797 C  CD2   . PHE B 1 477 ? 0.861   4.781   0.548   1 23.029  ? 469  PHE B CD2   1 
ATOM   7798 C  CE1   . PHE B 1 477 ? 2.806   2.81    1.008   1 25.097  ? 469  PHE B CE1   1 
ATOM   7799 C  CE2   . PHE B 1 477 ? 2.159   4.929   0.03    1 25.555  ? 469  PHE B CE2   1 
ATOM   7800 C  CZ    . PHE B 1 477 ? 3.129   3.942   0.265   1 24.67   ? 469  PHE B CZ    1 
ATOM   7801 N  N     . VAL B 1 478 ? -3.362  1.337   2.199   1 22.769  ? 470  VAL B N     1 
ATOM   7802 C  CA    . VAL B 1 478 ? -4.612  0.982   2.862   1 23.515  ? 470  VAL B CA    1 
ATOM   7803 C  C     . VAL B 1 478 ? -4.374  1.02    4.378   1 22.722  ? 470  VAL B C     1 
ATOM   7804 O  O     . VAL B 1 478 ? -3.409  0.42    4.874   1 24.493  ? 470  VAL B O     1 
ATOM   7805 C  CB    . VAL B 1 478 ? -5.19   -0.349  2.319   1 23.072  ? 470  VAL B CB    1 
ATOM   7806 C  CG1   . VAL B 1 478 ? -6.311  -0.948  3.167   1 23.957  ? 470  VAL B CG1   1 
ATOM   7807 C  CG2   . VAL B 1 478 ? -5.667  -0.221  0.87    1 21.747  ? 470  VAL B CG2   1 
ATOM   7808 N  N     . LEU B 1 479 ? -5.28   1.723   5.072   1 19.321  ? 471  LEU B N     1 
ATOM   7809 C  CA    . LEU B 1 479 ? -5.27   1.922   6.518   1 20.071  ? 471  LEU B CA    1 
ATOM   7810 C  C     . LEU B 1 479 ? -6.569  1.375   7.102   1 20.16   ? 471  LEU B C     1 
ATOM   7811 O  O     . LEU B 1 479 ? -7.635  1.541   6.489   1 21.087  ? 471  LEU B O     1 
ATOM   7812 C  CB    . LEU B 1 479 ? -5.052  3.385   6.914   1 18.579  ? 471  LEU B CB    1 
ATOM   7813 C  CG    . LEU B 1 479 ? -3.719  4.052   6.538   1 20.571  ? 471  LEU B CG    1 
ATOM   7814 C  CD1   . LEU B 1 479 ? -3.542  4.521   5.095   1 21.232  ? 471  LEU B CD1   1 
ATOM   7815 C  CD2   . LEU B 1 479 ? -3.515  5.253   7.431   1 21.328  ? 471  LEU B CD2   1 
ATOM   7816 N  N     . ALA B 1 480 ? -6.456  0.728   8.277   1 18.834  ? 472  ALA B N     1 
ATOM   7817 C  CA    . ALA B 1 480 ? -7.574  0.125   9.006   1 18.499  ? 472  ALA B CA    1 
ATOM   7818 C  C     . ALA B 1 480 ? -7.249  -0.015  10.493  1 17.579  ? 472  ALA B C     1 
ATOM   7819 O  O     . ALA B 1 480 ? -6.091  -0.252  10.835  1 18.203  ? 472  ALA B O     1 
ATOM   7820 C  CB    . ALA B 1 480 ? -7.953  -1.214  8.4     1 16.359  ? 472  ALA B CB    1 
ATOM   7821 N  N     . ILE B 1 481 ? -8.293  0.094   11.347  1 19.189  ? 473  ILE B N     1 
ATOM   7822 C  CA    . ILE B 1 481 ? -8.216  -0.122  12.797  1 17.517  ? 473  ILE B CA    1 
ATOM   7823 C  C     . ILE B 1 481 ? -8.247  -1.628  13.048  1 17.755  ? 473  ILE B C     1 
ATOM   7824 O  O     . ILE B 1 481 ? -9.14   -2.304  12.543  1 17.517  ? 473  ILE B O     1 
ATOM   7825 C  CB    . ILE B 1 481 ? -9.267  0.685   13.618  1 17.45   ? 473  ILE B CB    1 
ATOM   7826 C  CG1   . ILE B 1 481 ? -9.33   2.213   13.258  1 17.658  ? 473  ILE B CG1   1 
ATOM   7827 C  CG2   . ILE B 1 481 ? -9.172  0.464   15.138  1 16.921  ? 473  ILE B CG2   1 
ATOM   7828 C  CD1   . ILE B 1 481 ? -8.063  3.041   13.458  1 18.58   ? 473  ILE B CD1   1 
ATOM   7829 N  N     . VAL B 1 482 ? -7.252  -2.115  13.814  1 17.703  ? 474  VAL B N     1 
ATOM   7830 C  CA    . VAL B 1 482 ? -7.135  -3.504  14.251  1 17.651  ? 474  VAL B CA    1 
ATOM   7831 C  C     . VAL B 1 482 ? -7.427  -3.529  15.75   1 18.259  ? 474  VAL B C     1 
ATOM   7832 O  O     . VAL B 1 482 ? -6.84   -2.752  16.505  1 18.757  ? 474  VAL B O     1 
ATOM   7833 C  CB    . VAL B 1 482 ? -5.763  -4.153  13.918  1 18.697  ? 474  VAL B CB    1 
ATOM   7834 C  CG1   . VAL B 1 482 ? -5.634  -5.605  14.403  1 19.265  ? 474  VAL B CG1   1 
ATOM   7835 C  CG2   . VAL B 1 482 ? -5.427  -4.123  12.431  1 17.658  ? 474  VAL B CG2   1 
ATOM   7836 N  N     . ASP B 1 483 ? -8.304  -4.456  16.163  1 19.367  ? 475  ASP B N     1 
ATOM   7837 C  CA    . ASP B 1 483 ? -8.566  -4.767  17.562  1 20.039  ? 475  ASP B CA    1 
ATOM   7838 C  C     . ASP B 1 483 ? -7.628  -5.893  17.976  1 20.016  ? 475  ASP B C     1 
ATOM   7839 O  O     . ASP B 1 483 ? -7.722  -6.998  17.435  1 19.148  ? 475  ASP B O     1 
ATOM   7840 C  CB    . ASP B 1 483 ? -10.024 -5.098  17.833  1 19.792  ? 475  ASP B CB    1 
ATOM   7841 C  CG    . ASP B 1 483 ? -11.021 -4.043  17.392  1 24.037  ? 475  ASP B CG    1 
ATOM   7842 O  OD1   . ASP B 1 483 ? -11.43  -4.089  16.209  1 27.952  ? 475  ASP B OD1   1 
ATOM   7843 O  OD2   . ASP B 1 483 ? -11.342 -3.168  18.21   1 22.882  ? 475  ASP B OD2   1 
ATOM   7844 N  N     . ARG B 1 484 ? -6.71   -5.574  18.903  1 19.63   ? 476  ARG B N     1 
ATOM   7845 C  CA    . ARG B 1 484 ? -5.786  -6.56   19.454  1 22.799  ? 476  ARG B CA    1 
ATOM   7846 C  C     . ARG B 1 484 ? -6.448  -7.127  20.699  1 22.563  ? 476  ARG B C     1 
ATOM   7847 O  O     . ARG B 1 484 ? -6.202  -6.622  21.801  1 27.112  ? 476  ARG B O     1 
ATOM   7848 C  CB    . ARG B 1 484 ? -4.351  -6.03   19.635  1 22.107  ? 476  ARG B CB    1 
ATOM   7849 C  CG    . ARG B 1 484 ? -3.546  -5.542  18.439  1 21.813  ? 476  ARG B CG    1 
ATOM   7850 C  CD    . ARG B 1 484 ? -3.216  -6.594  17.409  1 22.196  ? 476  ARG B CD    1 
ATOM   7851 N  NE    . ARG B 1 484 ? -2.3    -7.622  17.919  1 21.27   ? 476  ARG B NE    1 
ATOM   7852 C  CZ    . ARG B 1 484 ? -0.966  -7.559  18.001  1 24.694  ? 476  ARG B CZ    1 
ATOM   7853 N  NH1   . ARG B 1 484 ? -0.289  -6.511  17.528  1 22.156  ? 476  ARG B NH1   1 
ATOM   7854 N  NH2   . ARG B 1 484 ? -0.312  -8.586  18.544  1 21.323  ? 476  ARG B NH2   1 
ATOM   7855 N  N     . LEU B 1 485 ? -7.3    -8.142  20.48   1 23.23   ? 477  LEU B N     1 
ATOM   7856 C  CA    . LEU B 1 485 ? -8.329  -8.572  21.433  1 25.667  ? 477  LEU B CA    1 
ATOM   7857 C  C     . LEU B 1 485 ? -7.723  -9.079  22.746  1 29.009  ? 477  LEU B C     1 
ATOM   7858 O  O     . LEU B 1 485 ? -8.21   -8.729  23.815  1 32.739  ? 477  LEU B O     1 
ATOM   7859 C  CB    . LEU B 1 485 ? -9.385  -9.533  20.886  1 25.626  ? 477  LEU B CB    1 
ATOM   7860 C  CG    . LEU B 1 485 ? -10.254 -9.05   19.714  1 27.533  ? 477  LEU B CG    1 
ATOM   7861 C  CD1   . LEU B 1 485 ? -11.016 -10.251 19.137  1 28.15   ? 477  LEU B CD1   1 
ATOM   7862 C  CD2   . LEU B 1 485 ? -11.214 -7.907  20.06   1 26.818  ? 477  LEU B CD2   1 
ATOM   7863 N  N     . ASP B 1 486 ? -6.642  -9.856  22.629  1 30.035  ? 478  ASP B N     1 
ATOM   7864 C  CA    . ASP B 1 486 ? -5.856  -10.44  23.709  1 33.3    ? 478  ASP B CA    1 
ATOM   7865 C  C     . ASP B 1 486 ? -5.058  -9.385  24.486  1 31.254  ? 478  ASP B C     1 
ATOM   7866 O  O     . ASP B 1 486 ? -4.658  -9.642  25.618  1 30.354  ? 478  ASP B O     1 
ATOM   7867 C  CB    . ASP B 1 486 ? -4.978  -11.546 23.134  1 37.446  ? 478  ASP B CB    1 
ATOM   7868 C  CG    . ASP B 1 486 ? -4.013  -11.15  22.012  1 41.043  ? 478  ASP B CG    1 
ATOM   7869 O  OD1   . ASP B 1 486 ? -4.427  -10.448 21.044  1 44.13   ? 478  ASP B OD1   1 
ATOM   7870 O  OD2   . ASP B 1 486 ? -2.849  -11.562 22.095  1 43.48   ? 478  ASP B OD2   1 
ATOM   7871 N  N     . LEU B 1 487 ? -4.803  -8.217  23.87   1 30.672  ? 479  LEU B N     1 
ATOM   7872 C  CA    . LEU B 1 487 ? -3.925  -7.179  24.398  1 28.068  ? 479  LEU B CA    1 
ATOM   7873 C  C     . LEU B 1 487 ? -4.67   -5.962  24.961  1 27.277  ? 479  LEU B C     1 
ATOM   7874 O  O     . LEU B 1 487 ? -4.008  -5.115  25.566  1 27.323  ? 479  LEU B O     1 
ATOM   7875 C  CB    . LEU B 1 487 ? -2.836  -6.796  23.382  1 28.614  ? 479  LEU B CB    1 
ATOM   7876 C  CG    . LEU B 1 487 ? -1.852  -7.882  22.926  1 26.304  ? 479  LEU B CG    1 
ATOM   7877 C  CD1   . LEU B 1 487 ? -1.061  -7.314  21.773  1 26.131  ? 479  LEU B CD1   1 
ATOM   7878 C  CD2   . LEU B 1 487 ? -0.908  -8.406  24.01   1 29.07   ? 479  LEU B CD2   1 
ATOM   7879 N  N     . ASN B 1 488 ? -6.009  -5.858  24.774  1 26.677  ? 480  ASN B N     1 
ATOM   7880 C  CA    . ASN B 1 488 ? -6.834  -4.699  25.158  1 26.506  ? 480  ASN B CA    1 
ATOM   7881 C  C     . ASN B 1 488 ? -6.272  -3.39   24.564  1 24.152  ? 480  ASN B C     1 
ATOM   7882 O  O     . ASN B 1 488 ? -6.094  -2.395  25.281  1 22.323  ? 480  ASN B O     1 
ATOM   7883 C  CB    . ASN B 1 488 ? -7.191  -4.715  26.659  1 28.181  ? 480  ASN B CB    1 
ATOM   7884 C  CG    . ASN B 1 488 ? -8.226  -3.684  27.093  1 33.132  ? 480  ASN B CG    1 
ATOM   7885 O  OD1   . ASN B 1 488 ? -9.3    -3.533  26.488  1 29.218  ? 480  ASN B OD1   1 
ATOM   7886 N  ND2   . ASN B 1 488 ? -7.914  -2.939  28.145  1 33.266  ? 480  ASN B ND2   1 
ATOM   7887 N  N     . ARG B 1 489 ? -5.917  -3.438  23.261  1 22.802  ? 481  ARG B N     1 
ATOM   7888 C  CA    . ARG B 1 489 ? -5.429  -2.285  22.511  1 22.981  ? 481  ARG B CA    1 
ATOM   7889 C  C     . ARG B 1 489 ? -5.981  -2.257  21.082  1 19.651  ? 481  ARG B C     1 
ATOM   7890 O  O     . ARG B 1 489 ? -6.313  -3.307  20.516  1 18.312  ? 481  ARG B O     1 
ATOM   7891 C  CB    . ARG B 1 489 ? -3.921  -2.02   22.666  1 25.793  ? 481  ARG B CB    1 
ATOM   7892 C  CG    . ARG B 1 489 ? -2.954  -2.823  21.818  1 27.573  ? 481  ARG B CG    1 
ATOM   7893 C  CD    . ARG B 1 489 ? -1.574  -2.273  22.013  1 30.414  ? 481  ARG B CD    1 
ATOM   7894 N  NE    . ARG B 1 489 ? -0.694  -2.941  21.042  1 35.551  ? 481  ARG B NE    1 
ATOM   7895 C  CZ    . ARG B 1 489 ? 0.321   -3.768  21.298  1 35.985  ? 481  ARG B CZ    1 
ATOM   7896 N  NH1   . ARG B 1 489 ? 0.624   -4.138  22.532  1 36.067  ? 481  ARG B NH1   1 
ATOM   7897 N  NH2   . ARG B 1 489 ? 1.039   -4.24   20.297  1 39.372  ? 481  ARG B NH2   1 
ATOM   7898 N  N     . SER B 1 490 ? -6.043  -1.028  20.535  1 17.721  ? 482  SER B N     1 
ATOM   7899 C  CA    . SER B 1 490 ? -6.317  -0.748  19.129  1 16.16   ? 482  SER B CA    1 
ATOM   7900 C  C     . SER B 1 490 ? -5.044  -0.257  18.442  1 17.341  ? 482  SER B C     1 
ATOM   7901 O  O     . SER B 1 490 ? -4.247  0.458   19.054  1 17.109  ? 482  SER B O     1 
ATOM   7902 C  CB    . SER B 1 490 ? -7.442  0.235   18.973  1 15.417  ? 482  SER B CB    1 
ATOM   7903 O  OG    . SER B 1 490 ? -8.64   -0.274  19.551  1 16.482  ? 482  SER B OG    1 
ATOM   7904 N  N     . GLU B 1 491 ? -4.915  -0.602  17.146  1 17.501  ? 483  GLU B N     1 
ATOM   7905 C  CA    . GLU B 1 491 ? -3.812  -0.227  16.27   1 18.403  ? 483  GLU B CA    1 
ATOM   7906 C  C     . GLU B 1 491 ? -4.33   0.263   14.921  1 17.63   ? 483  GLU B C     1 
ATOM   7907 O  O     . GLU B 1 491 ? -5.415  -0.138  14.518  1 19.545  ? 483  GLU B O     1 
ATOM   7908 C  CB    . GLU B 1 491 ? -2.925  -1.441  15.994  1 19.767  ? 483  GLU B CB    1 
ATOM   7909 C  CG    . GLU B 1 491 ? -1.988  -1.732  17.154  1 24.527  ? 483  GLU B CG    1 
ATOM   7910 C  CD    . GLU B 1 491 ? -1.142  -2.984  17.175  1 26.045  ? 483  GLU B CD    1 
ATOM   7911 O  OE1   . GLU B 1 491 ? -1.212  -3.843  16.252  1 24.457  ? 483  GLU B OE1   1 
ATOM   7912 O  OE2   . GLU B 1 491 ? -0.436  -3.077  18.224  1 27.77   ? 483  GLU B OE2   1 
ATOM   7913 N  N     . VAL B 1 492 ? -3.53   1.096   14.238  1 17.378  ? 484  VAL B N     1 
ATOM   7914 C  CA    . VAL B 1 492 ? -3.687  1.425   12.82   1 18.049  ? 484  VAL B CA    1 
ATOM   7915 C  C     . VAL B 1 492 ? -2.662  0.583   12.048  1 20.416  ? 484  VAL B C     1 
ATOM   7916 O  O     . VAL B 1 492 ? -1.457  0.816   12.168  1 19.76   ? 484  VAL B O     1 
ATOM   7917 C  CB    . VAL B 1 492 ? -3.653  2.915   12.388  1 17.284  ? 484  VAL B CB    1 
ATOM   7918 C  CG1   . VAL B 1 492 ? -4.212  3.128   10.978  1 16.653  ? 484  VAL B CG1   1 
ATOM   7919 C  CG2   . VAL B 1 492 ? -4.378  3.862   13.359  1 17.398  ? 484  VAL B CG2   1 
ATOM   7920 N  N     . VAL B 1 493 ? -3.152  -0.379  11.244  1 19.389  ? 485  VAL B N     1 
ATOM   7921 C  CA    . VAL B 1 493 ? -2.323  -1.07   10.26   1 19.548  ? 485  VAL B CA    1 
ATOM   7922 C  C     . VAL B 1 493 ? -2.166  -0.187  9.005   1 20.213  ? 485  VAL B C     1 
ATOM   7923 O  O     . VAL B 1 493 ? -3.108  0.525   8.629   1 19.883  ? 485  VAL B O     1 
ATOM   7924 C  CB    . VAL B 1 493 ? -2.836  -2.509  10.018  1 20.547  ? 485  VAL B CB    1 
ATOM   7925 C  CG1   . VAL B 1 493 ? -4.065  -2.632  9.128   1 18.164  ? 485  VAL B CG1   1 
ATOM   7926 C  CG2   . VAL B 1 493 ? -1.749  -3.404  9.481   1 22.064  ? 485  VAL B CG2   1 
ATOM   7927 N  N     . VAL B 1 494 ? -0.959  -0.208  8.401   1 18.069  ? 486  VAL B N     1 
ATOM   7928 C  CA    . VAL B 1 494 ? -0.655  0.421   7.11    1 18.308  ? 486  VAL B CA    1 
ATOM   7929 C  C     . VAL B 1 494 ? -0.128  -0.685  6.184   1 20.56   ? 486  VAL B C     1 
ATOM   7930 O  O     . VAL B 1 494 ? 0.849   -1.356  6.533   1 20.576  ? 486  VAL B O     1 
ATOM   7931 C  CB    . VAL B 1 494 ? 0.279   1.659   7.172   1 17.57   ? 486  VAL B CB    1 
ATOM   7932 C  CG1   . VAL B 1 494 ? 0.382   2.401   5.849   1 16.78   ? 486  VAL B CG1   1 
ATOM   7933 C  CG2   . VAL B 1 494 ? -0.134  2.683   8.228   1 17.696  ? 486  VAL B CG2   1 
ATOM   7934 N  N     . ILE B 1 495 ? -0.823  -0.876  5.042   1 22.448  ? 487  ILE B N     1 
ATOM   7935 C  CA    . ILE B 1 495 ? -0.551  -1.88   4.004   1 22.565  ? 487  ILE B CA    1 
ATOM   7936 C  C     . ILE B 1 495 ? -0.259  -1.134  2.698   1 23.837  ? 487  ILE B C     1 
ATOM   7937 O  O     . ILE B 1 495 ? -1.066  -0.302  2.277   1 23.537  ? 487  ILE B O     1 
ATOM   7938 C  CB    . ILE B 1 495 ? -1.72   -2.886  3.839   1 20.844  ? 487  ILE B CB    1 
ATOM   7939 C  CG1   . ILE B 1 495 ? -2.087  -3.623  5.14    1 20.93   ? 487  ILE B CG1   1 
ATOM   7940 C  CG2   . ILE B 1 495 ? -1.487  -3.875  2.684   1 19.71   ? 487  ILE B CG2   1 
ATOM   7941 C  CD1   . ILE B 1 495 ? -3.564  -3.994  5.269   1 20.235  ? 487  ILE B CD1   1 
ATOM   7942 N  N     . ASP B 1 496 ? 0.881   -1.466  2.062   1 24.064  ? 488  ASP B N     1 
ATOM   7943 C  CA    . ASP B 1 496 ? 1.184   -1.094  0.683   1 23.759  ? 488  ASP B CA    1 
ATOM   7944 C  C     . ASP B 1 496 ? 0.489   -2.091  -0.242  1 24.041  ? 488  ASP B C     1 
ATOM   7945 O  O     . ASP B 1 496 ? 0.648   -3.296  -0.066  1 22.108  ? 488  ASP B O     1 
ATOM   7946 C  CB    . ASP B 1 496 ? 2.688   -1.009  0.452   1 27.204  ? 488  ASP B CB    1 
ATOM   7947 C  CG    . ASP B 1 496 ? 3.158   -0.409  -0.873  1 29.022  ? 488  ASP B CG    1 
ATOM   7948 O  OD1   . ASP B 1 496 ? 2.613   -0.767  -1.955  1 29.338  ? 488  ASP B OD1   1 
ATOM   7949 O  OD2   . ASP B 1 496 ? 4.107   0.389   -0.829  1 26.349  ? 488  ASP B OD2   1 
ATOM   7950 N  N     . THR B 1 497 ? -0.243  -1.562  -1.241  1 24.166  ? 489  THR B N     1 
ATOM   7951 C  CA    . THR B 1 497 ? -1.034  -2.339  -2.196  1 25.385  ? 489  THR B CA    1 
ATOM   7952 C  C     . THR B 1 497 ? -0.174  -3.244  -3.084  1 27.88   ? 489  THR B C     1 
ATOM   7953 O  O     . THR B 1 497 ? -0.715  -4.223  -3.595  1 31.112  ? 489  THR B O     1 
ATOM   7954 C  CB    . THR B 1 497 ? -2.035  -1.515  -3.014  1 24.318  ? 489  THR B CB    1 
ATOM   7955 O  OG1   . THR B 1 497 ? -1.272  -0.536  -3.712  1 24.599  ? 489  THR B OG1   1 
ATOM   7956 C  CG2   . THR B 1 497 ? -3.143  -0.928  -2.16   1 23.704  ? 489  THR B CG2   1 
ATOM   7957 N  N     . ARG B 1 498 ? 1.139   -2.943  -3.238  1 28.473  ? 490  ARG B N     1 
ATOM   7958 C  CA    . ARG B 1 498 ? 2.103   -3.773  -3.963  1 29.508  ? 490  ARG B CA    1 
ATOM   7959 C  C     . ARG B 1 498 ? 2.254   -5.157  -3.322  1 29.361  ? 490  ARG B C     1 
ATOM   7960 O  O     . ARG B 1 498 ? 2.544   -6.129  -4.024  1 29.18   ? 490  ARG B O     1 
ATOM   7961 C  CB    . ARG B 1 498 ? 3.483   -3.144  -4.161  1 32.723  ? 490  ARG B CB    1 
ATOM   7962 C  CG    . ARG B 1 498 ? 3.55    -1.914  -5.052  1 37.881  ? 490  ARG B CG    1 
ATOM   7963 C  CD    . ARG B 1 498 ? 4.793   -1.11   -4.688  1 43.854  ? 490  ARG B CD    1 
ATOM   7964 N  NE    . ARG B 1 498 ? 4.957   0.006   -5.635  1 50.216  ? 490  ARG B NE    1 
ATOM   7965 C  CZ    . ARG B 1 498 ? 5.847   1.01    -5.688  1 54.062  ? 490  ARG B CZ    1 
ATOM   7966 N  NH1   . ARG B 1 498 ? 6.77    1.198   -4.747  1 52.066  ? 490  ARG B NH1   1 
ATOM   7967 N  NH2   . ARG B 1 498 ? 5.78    1.856   -6.71   1 48.639  ? 490  ARG B NH2   1 
ATOM   7968 N  N     . ASP B 1 499 ? 2.098   -5.231  -1.987  1 29.794  ? 491  ASP B N     1 
ATOM   7969 C  CA    . ASP B 1 499 ? 1.945   -6.485  -1.268  1 30.201  ? 491  ASP B CA    1 
ATOM   7970 C  C     . ASP B 1 499 ? 0.872   -6.347  -0.199  1 29.901  ? 491  ASP B C     1 
ATOM   7971 O  O     . ASP B 1 499 ? 1.183   -6.044  0.962   1 26.898  ? 491  ASP B O     1 
ATOM   7972 C  CB    . ASP B 1 499 ? 3.263   -7.07   -0.78   1 30.844  ? 491  ASP B CB    1 
ATOM   7973 C  CG    . ASP B 1 499 ? 3.191   -8.426  -0.09   1 32.858  ? 491  ASP B CG    1 
ATOM   7974 O  OD1   . ASP B 1 499 ? 2.127   -9.124  -0.147  1 31.375  ? 491  ASP B OD1   1 
ATOM   7975 O  OD2   . ASP B 1 499 ? 4.21    -8.768  0.532   1 33.471  ? 491  ASP B OD2   1 
ATOM   7976 N  N     . PHE B 1 500 ? -0.352  -6.7    -0.624  1 28.519  ? 492  PHE B N     1 
ATOM   7977 C  CA    . PHE B 1 500 ? -1.591  -6.596  0.136   1 27.003  ? 492  PHE B CA    1 
ATOM   7978 C  C     . PHE B 1 500 ? -1.596  -7.52   1.36    1 25.396  ? 492  PHE B C     1 
ATOM   7979 O  O     . PHE B 1 500 ? -2.309  -7.215  2.32    1 26.515  ? 492  PHE B O     1 
ATOM   7980 C  CB    . PHE B 1 500 ? -2.858  -6.666  -0.728  1 24.796  ? 492  PHE B CB    1 
ATOM   7981 C  CG    . PHE B 1 500 ? -4.089  -6.072  -0.059  1 23.781  ? 492  PHE B CG    1 
ATOM   7982 C  CD1   . PHE B 1 500 ? -4.276  -4.678  0.038   1 25.018  ? 492  PHE B CD1   1 
ATOM   7983 C  CD2   . PHE B 1 500 ? -5.07   -6.917  0.479   1 25.38   ? 492  PHE B CD2   1 
ATOM   7984 C  CE1   . PHE B 1 500 ? -5.412  -4.148  0.676   1 25.823  ? 492  PHE B CE1   1 
ATOM   7985 C  CE2   . PHE B 1 500 ? -6.211  -6.396  1.125   1 23.444  ? 492  PHE B CE2   1 
ATOM   7986 C  CZ    . PHE B 1 500 ? -6.372  -5.011  1.227   1 25.044  ? 492  PHE B CZ    1 
ATOM   7987 N  N     . THR B 1 501 ? -0.789  -8.597  1.33    1 22.09   ? 493  THR B N     1 
ATOM   7988 C  CA    . THR B 1 501 ? -0.735  -9.598  2.392   1 23.138  ? 493  THR B CA    1 
ATOM   7989 C  C     . THR B 1 501 ? 0.021   -9.093  3.634   1 24.102  ? 493  THR B C     1 
ATOM   7990 O  O     . THR B 1 501 ? -0.12   -9.734  4.682   1 25.712  ? 493  THR B O     1 
ATOM   7991 C  CB    . THR B 1 501 ? -0.217  -10.964 1.912   1 24.158  ? 493  THR B CB    1 
ATOM   7992 O  OG1   . THR B 1 501 ? 1.178   -10.78  1.689   1 22.807  ? 493  THR B OG1   1 
ATOM   7993 C  CG2   . THR B 1 501 ? -0.927  -11.555 0.696   1 20.666  ? 493  THR B CG2   1 
ATOM   7994 N  N     . LYS B 1 502 ? 0.818   -8.004  3.521   1 24.882  ? 494  LYS B N     1 
ATOM   7995 C  CA    . LYS B 1 502 ? 1.796   -7.581  4.53    1 28.919  ? 494  LYS B CA    1 
ATOM   7996 C  C     . LYS B 1 502 ? 1.587   -6.133  4.969   1 26.062  ? 494  LYS B C     1 
ATOM   7997 O  O     . LYS B 1 502 ? 1.435   -5.244  4.138   1 23.66   ? 494  LYS B O     1 
ATOM   7998 C  CB    . LYS B 1 502 ? 3.282   -7.705  4.136   1 35.05   ? 494  LYS B CB    1 
ATOM   7999 C  CG    . LYS B 1 502 ? 3.885   -9.08   3.826   1 43.205  ? 494  LYS B CG    1 
ATOM   8000 C  CD    . LYS B 1 502 ? 3.9     -10.207 4.858   1 46.55   ? 494  LYS B CD    1 
ATOM   8001 C  CE    . LYS B 1 502 ? 3.265   -11.457 4.296   1 47.51   ? 494  LYS B CE    1 
ATOM   8002 N  NZ    . LYS B 1 502 ? 4.066   -12.228 3.336   1 55.467  ? 494  LYS B NZ    1 
ATOM   8003 N  N     . ALA B 1 503 ? 1.625   -5.932  6.294   1 24.739  ? 495  ALA B N     1 
ATOM   8004 C  CA    . ALA B 1 503 ? 1.69    -4.62   6.915   1 24.633  ? 495  ALA B CA    1 
ATOM   8005 C  C     . ALA B 1 503 ? 3.11    -4.079  6.842   1 24.133  ? 495  ALA B C     1 
ATOM   8006 O  O     . ALA B 1 503 ? 4.047   -4.805  7.173   1 27.047  ? 495  ALA B O     1 
ATOM   8007 C  CB    . ALA B 1 503 ? 1.263   -4.733  8.344   1 24.127  ? 495  ALA B CB    1 
ATOM   8008 N  N     . VAL B 1 504 ? 3.219   -2.808  6.416   1 25.466  ? 496  VAL B N     1 
ATOM   8009 C  CA    . VAL B 1 504 ? 4.466   -2.04   6.361   1 26.751  ? 496  VAL B CA    1 
ATOM   8010 C  C     . VAL B 1 504 ? 4.715   -1.325  7.693   1 25.643  ? 496  VAL B C     1 
ATOM   8011 O  O     . VAL B 1 504 ? 5.868   -1.068  8.035   1 24.488  ? 496  VAL B O     1 
ATOM   8012 C  CB    . VAL B 1 504 ? 4.697   -1.096  5.157   1 25.87   ? 496  VAL B CB    1 
ATOM   8013 C  CG1   . VAL B 1 504 ? 4.864   -1.872  3.846   1 28.945  ? 496  VAL B CG1   1 
ATOM   8014 C  CG2   . VAL B 1 504 ? 3.651   0.018   5.025   1 26.306  ? 496  VAL B CG2   1 
ATOM   8015 N  N     . ALA B 1 505 ? 3.623   -0.951  8.392   1 24.084  ? 497  ALA B N     1 
ATOM   8016 C  CA    . ALA B 1 505 ? 3.647   -0.114  9.587   1 22.891  ? 497  ALA B CA    1 
ATOM   8017 C  C     . ALA B 1 505 ? 2.421   -0.381  10.456  1 21.068  ? 497  ALA B C     1 
ATOM   8018 O  O     . ALA B 1 505 ? 1.398   -0.84   9.949   1 20.773  ? 497  ALA B O     1 
ATOM   8019 C  CB    . ALA B 1 505 ? 3.78    1.36    9.214   1 23.644  ? 497  ALA B CB    1 
ATOM   8020 N  N     . ALA B 1 506 ? 2.583   -0.144  11.771  1 21.555  ? 498  ALA B N     1 
ATOM   8021 C  CA    . ALA B 1 506 ? 1.533   -0.216  12.786  1 20.958  ? 498  ALA B CA    1 
ATOM   8022 C  C     . ALA B 1 506 ? 1.642   0.997   13.7    1 23.936  ? 498  ALA B C     1 
ATOM   8023 O  O     . ALA B 1 506 ? 2.739   1.298   14.182  1 23.905  ? 498  ALA B O     1 
ATOM   8024 C  CB    . ALA B 1 506 ? 1.562   -1.533  13.548  1 20.051  ? 498  ALA B CB    1 
ATOM   8025 N  N     . VAL B 1 507 ? 0.506   1.695   13.86   1 22.776  ? 499  VAL B N     1 
ATOM   8026 C  CA    . VAL B 1 507 ? 0.329   2.829   14.759  1 22.624  ? 499  VAL B CA    1 
ATOM   8027 C  C     . VAL B 1 507 ? -0.259  2.239   16.043  1 22.931  ? 499  VAL B C     1 
ATOM   8028 O  O     . VAL B 1 507 ? -1.393  1.774   16.013  1 24.205  ? 499  VAL B O     1 
ATOM   8029 C  CB    . VAL B 1 507 ? -0.522  3.981   14.162  1 21.204  ? 499  VAL B CB    1 
ATOM   8030 C  CG1   . VAL B 1 507 ? -0.699  5.164   15.115  1 21.112  ? 499  VAL B CG1   1 
ATOM   8031 C  CG2   . VAL B 1 507 ? 0.032   4.496   12.841  1 21.074  ? 499  VAL B CG2   1 
ATOM   8032 N  N     . GLN B 1 508 ? 0.529   2.261   17.136  1 18.842  ? 500  GLN B N     1 
ATOM   8033 C  CA    . GLN B 1 508 ? 0.249   1.508   18.352  1 20.24   ? 500  GLN B CA    1 
ATOM   8034 C  C     . GLN B 1 508 ? -0.233  2.469   19.434  1 19.376  ? 500  GLN B C     1 
ATOM   8035 O  O     . GLN B 1 508 ? 0.591   3.159   20.061  1 20.042  ? 500  GLN B O     1 
ATOM   8036 C  CB    . GLN B 1 508 ? 1.499   0.695   18.697  1 22.806  ? 500  GLN B CB    1 
ATOM   8037 C  CG    . GLN B 1 508 ? 1.365   -0.23   19.904  1 25.213  ? 500  GLN B CG    1 
ATOM   8038 C  CD    . GLN B 1 508 ? 2.69    -0.804  20.368  1 29.728  ? 500  GLN B CD    1 
ATOM   8039 O  OE1   . GLN B 1 508 ? 3.57    -1.182  19.577  1 27.81   ? 500  GLN B OE1   1 
ATOM   8040 N  NE2   . GLN B 1 508 ? 2.856   -0.855  21.682  1 29.334  ? 500  GLN B NE2   1 
ATOM   8041 N  N     . LEU B 1 509 ? -1.57   2.496   19.628  1 17.781  ? 501  LEU B N     1 
ATOM   8042 C  CA    . LEU B 1 509 ? -2.223  3.119   20.777  1 17.75   ? 501  LEU B CA    1 
ATOM   8043 C  C     . LEU B 1 509 ? -1.854  2.375   22.069  1 17.98   ? 501  LEU B C     1 
ATOM   8044 O  O     . LEU B 1 509 ? -1.641  1.159   22.018  1 18.384  ? 501  LEU B O     1 
ATOM   8045 C  CB    . LEU B 1 509 ? -3.732  3.365   20.655  1 16.346  ? 501  LEU B CB    1 
ATOM   8046 C  CG    . LEU B 1 509 ? -4.169  4.409   19.623  1 17.218  ? 501  LEU B CG    1 
ATOM   8047 C  CD1   . LEU B 1 509 ? -5.686  4.249   19.389  1 16.994  ? 501  LEU B CD1   1 
ATOM   8048 C  CD2   . LEU B 1 509 ? -3.814  5.878   19.959  1 17.059  ? 501  LEU B CD2   1 
ATOM   8049 N  N     . PRO B 1 510 ? -1.735  3.062   23.246  1 18.871  ? 502  PRO B N     1 
ATOM   8050 C  CA    . PRO B 1 510 ? -1.566  2.388   24.537  1 19.973  ? 502  PRO B CA    1 
ATOM   8051 C  C     . PRO B 1 510 ? -2.839  1.733   25.099  1 21.267  ? 502  PRO B C     1 
ATOM   8052 O  O     . PRO B 1 510 ? -2.777  1.091   26.155  1 23.293  ? 502  PRO B O     1 
ATOM   8053 C  CB    . PRO B 1 510 ? -1.001  3.503   25.42   1 19.985  ? 502  PRO B CB    1 
ATOM   8054 C  CG    . PRO B 1 510 ? -1.716  4.735   24.882  1 19.404  ? 502  PRO B CG    1 
ATOM   8055 C  CD    . PRO B 1 510 ? -1.688  4.53    23.41   1 19.364  ? 502  PRO B CD    1 
ATOM   8056 N  N     . PHE B 1 511 ? -3.971  1.908   24.382  1 18.638  ? 503  PHE B N     1 
ATOM   8057 C  CA    . PHE B 1 511 ? -5.305  1.503   24.803  1 18.062  ? 503  PHE B CA    1 
ATOM   8058 C  C     . PHE B 1 511 ? -6.14   1.046   23.603  1 18.839  ? 503  PHE B C     1 
ATOM   8059 O  O     . PHE B 1 511 ? -5.708  1.197   22.441  1 18.634  ? 503  PHE B O     1 
ATOM   8060 C  CB    . PHE B 1 511 ? -5.925  2.653   25.608  1 16.521  ? 503  PHE B CB    1 
ATOM   8061 C  CG    . PHE B 1 511 ? -6.003  4.063   25.036  1 16.677  ? 503  PHE B CG    1 
ATOM   8062 C  CD1   . PHE B 1 511 ? -6.458  4.34    23.725  1 16.668  ? 503  PHE B CD1   1 
ATOM   8063 C  CD2   . PHE B 1 511 ? -5.619  5.151   25.836  1 18.651  ? 503  PHE B CD2   1 
ATOM   8064 C  CE1   . PHE B 1 511 ? -6.532  5.664   23.242  1 16.817  ? 503  PHE B CE1   1 
ATOM   8065 C  CE2   . PHE B 1 511 ? -5.692  6.485   25.356  1 18.603  ? 503  PHE B CE2   1 
ATOM   8066 C  CZ    . PHE B 1 511 ? -6.148  6.742   24.058  1 17.684  ? 503  PHE B CZ    1 
ATOM   8067 N  N     . ALA B 1 512 ? -7.331  0.49    23.92   1 18.341  ? 504  ALA B N     1 
ATOM   8068 C  CA    . ALA B 1 512 ? -8.358  0.165   22.94   1 18.579  ? 504  ALA B CA    1 
ATOM   8069 C  C     . ALA B 1 512 ? -9.361  1.314   22.809  1 18.556  ? 504  ALA B C     1 
ATOM   8070 O  O     . ALA B 1 512 ? -9.704  1.973   23.792  1 18.81   ? 504  ALA B O     1 
ATOM   8071 C  CB    . ALA B 1 512 ? -8.992  -1.165  23.266  1 18.259  ? 504  ALA B CB    1 
ATOM   8072 N  N     . ILE B 1 513 ? -9.779  1.568   21.559  1 19.277  ? 505  ILE B N     1 
ATOM   8073 C  CA    . ILE B 1 513 ? -10.916 2.436   21.243  1 18.583  ? 505  ILE B CA    1 
ATOM   8074 C  C     . ILE B 1 513 ? -12.095 1.553   20.824  1 20.532  ? 505  ILE B C     1 
ATOM   8075 O  O     . ILE B 1 513 ? -11.917 0.35    20.568  1 22.56   ? 505  ILE B O     1 
ATOM   8076 C  CB    . ILE B 1 513 ? -10.568 3.567   20.249  1 16.718  ? 505  ILE B CB    1 
ATOM   8077 C  CG1   . ILE B 1 513 ? -10.187 3.008   18.84   1 16.406  ? 505  ILE B CG1   1 
ATOM   8078 C  CG2   . ILE B 1 513 ? -9.497  4.488   20.864  1 15.871  ? 505  ILE B CG2   1 
ATOM   8079 C  CD1   . ILE B 1 513 ? -10.039 4.023   17.711  1 18.25   ? 505  ILE B CD1   1 
ATOM   8080 N  N     . ARG B 1 514 ? -13.297 2.159   20.781  1 20.044  ? 506  ARG B N     1 
ATOM   8081 C  CA    . ARG B 1 514 ? -14.497 1.48    20.307  1 18.26   ? 506  ARG B CA    1 
ATOM   8082 C  C     . ARG B 1 514 ? -14.315 0.977   18.882  1 17.434  ? 506  ARG B C     1 
ATOM   8083 O  O     . ARG B 1 514 ? -13.611 1.615   18.083  1 16.64   ? 506  ARG B O     1 
ATOM   8084 C  CB    . ARG B 1 514 ? -15.7   2.425   20.336  1 19.716  ? 506  ARG B CB    1 
ATOM   8085 C  CG    . ARG B 1 514 ? -16.41  2.394   21.676  1 18.368  ? 506  ARG B CG    1 
ATOM   8086 C  CD    . ARG B 1 514 ? -17.37  1.249   21.901  1 17.911  ? 506  ARG B CD    1 
ATOM   8087 N  NE    . ARG B 1 514 ? -18.296 1.431   23.025  1 17.541  ? 506  ARG B NE    1 
ATOM   8088 C  CZ    . ARG B 1 514 ? -19.188 0.54    23.473  1 18.874  ? 506  ARG B CZ    1 
ATOM   8089 N  NH1   . ARG B 1 514 ? -19.318 -0.68   22.949  1 17.455  ? 506  ARG B NH1   1 
ATOM   8090 N  NH2   . ARG B 1 514 ? -19.943 0.867   24.51   1 19.771  ? 506  ARG B NH2   1 
ATOM   8091 N  N     . SER B 1 515 ? -14.918 -0.197  18.611  1 16.438  ? 507  SER B N     1 
ATOM   8092 C  CA    . SER B 1 515 ? -15.12  -0.63   17.237  1 16.704  ? 507  SER B CA    1 
ATOM   8093 C  C     . SER B 1 515 ? -16.17  0.291   16.606  1 17.05   ? 507  SER B C     1 
ATOM   8094 O  O     . SER B 1 515 ? -17.288 0.423   17.133  1 18.352  ? 507  SER B O     1 
ATOM   8095 C  CB    . SER B 1 515 ? -15.446 -2.095  17.139  1 17.025  ? 507  SER B CB    1 
ATOM   8096 O  OG    . SER B 1 515 ? -15.468 -2.492  15.776  1 17.603  ? 507  SER B OG    1 
ATOM   8097 N  N     . GLY B 1 516 ? -15.758 0.969   15.526  1 16.409  ? 508  GLY B N     1 
ATOM   8098 C  CA    . GLY B 1 516 ? -16.55  2.039   14.928  1 17.528  ? 508  GLY B CA    1 
ATOM   8099 C  C     . GLY B 1 516 ? -17.407 1.596   13.75   1 17.723  ? 508  GLY B C     1 
ATOM   8100 O  O     . GLY B 1 516 ? -17.639 0.403   13.518  1 16.747  ? 508  GLY B O     1 
ATOM   8101 N  N     . ILE B 1 517 ? -17.846 2.619   13.009  1 17.831  ? 509  ILE B N     1 
ATOM   8102 C  CA    . ILE B 1 517 ? -18.741 2.46    11.882  1 17.993  ? 509  ILE B CA    1 
ATOM   8103 C  C     . ILE B 1 517 ? -17.893 2.778   10.641  1 20.482  ? 509  ILE B C     1 
ATOM   8104 O  O     . ILE B 1 517 ? -17.158 1.888   10.174  1 21.644  ? 509  ILE B O     1 
ATOM   8105 C  CB    . ILE B 1 517 ? -20.108 3.175   12.097  1 15.939  ? 509  ILE B CB    1 
ATOM   8106 C  CG1   . ILE B 1 517 ? -20.78  2.78    13.451  1 15.321  ? 509  ILE B CG1   1 
ATOM   8107 C  CG2   . ILE B 1 517 ? -21.039 2.831   10.938  1 17.06   ? 509  ILE B CG2   1 
ATOM   8108 C  CD1   . ILE B 1 517 ? -22.143 3.407   13.793  1 16.088  ? 509  ILE B CD1   1 
ATOM   8109 N  N     . HIS B 1 518 ? -17.936 4.041   10.168  1 18.956  ? 510  HIS B N     1 
ATOM   8110 C  CA    . HIS B 1 518 ? -17.14  4.483   9.034   1 18.337  ? 510  HIS B CA    1 
ATOM   8111 C  C     . HIS B 1 518 ? -15.946 5.311   9.483   1 18.88   ? 510  HIS B C     1 
ATOM   8112 O  O     . HIS B 1 518 ? -15.906 5.838   10.592  1 20.777  ? 510  HIS B O     1 
ATOM   8113 C  CB    . HIS B 1 518 ? -17.982 5.18    7.967   1 17.677  ? 510  HIS B CB    1 
ATOM   8114 C  CG    . HIS B 1 518 ? -18.959 4.248   7.358   1 18.735  ? 510  HIS B CG    1 
ATOM   8115 N  ND1   . HIS B 1 518 ? -18.676 3.306   6.386   1 19.123  ? 510  HIS B ND1   1 
ATOM   8116 C  CD2   . HIS B 1 518 ? -20.241 4.103   7.666   1 18.456  ? 510  HIS B CD2   1 
ATOM   8117 C  CE1   . HIS B 1 518 ? -19.781 2.611   6.12    1 18.62   ? 510  HIS B CE1   1 
ATOM   8118 N  NE2   . HIS B 1 518 ? -20.729 3.068   6.907   1 18.911  ? 510  HIS B NE2   1 
ATOM   8119 N  N     . GLY B 1 519 ? -14.955 5.35    8.594   1 20.015  ? 511  GLY B N     1 
ATOM   8120 C  CA    . GLY B 1 519 ? -13.878 6.321   8.59    1 21.548  ? 511  GLY B CA    1 
ATOM   8121 C  C     . GLY B 1 519 ? -13.527 6.752   7.17    1 21.16   ? 511  GLY B C     1 
ATOM   8122 O  O     . GLY B 1 519 ? -14.029 6.173   6.189   1 20.543  ? 511  GLY B O     1 
ATOM   8123 N  N     . GLN B 1 520 ? -12.667 7.784   7.094   1 18.506  ? 512  GLN B N     1 
ATOM   8124 C  CA    . GLN B 1 520 ? -12.248 8.393   5.838   1 17.768  ? 512  GLN B CA    1 
ATOM   8125 C  C     . GLN B 1 520 ? -10.774 8.781   5.89    1 17.656  ? 512  GLN B C     1 
ATOM   8126 O  O     . GLN B 1 520 ? -10.302 9.282   6.915   1 16.456  ? 512  GLN B O     1 
ATOM   8127 C  CB    . GLN B 1 520 ? -13.123 9.593   5.443   1 17.424  ? 512  GLN B CB    1 
ATOM   8128 C  CG    . GLN B 1 520 ? -14.617 9.322   5.218   1 17.243  ? 512  GLN B CG    1 
ATOM   8129 C  CD    . GLN B 1 520 ? -14.982 8.298   4.152   1 17.801  ? 512  GLN B CD    1 
ATOM   8130 O  OE1   . GLN B 1 520 ? -14.253 8.087   3.175   1 17.781  ? 512  GLN B OE1   1 
ATOM   8131 N  NE2   . GLN B 1 520 ? -16.126 7.645   4.322   1 16.419  ? 512  GLN B NE2   1 
ATOM   8132 N  N     . TRP B 1 521 ? -10.081 8.556   4.764   1 17.986  ? 513  TRP B N     1 
ATOM   8133 C  CA    . TRP B 1 521 ? -8.821  9.238   4.5     1 18.478  ? 513  TRP B CA    1 
ATOM   8134 C  C     . TRP B 1 521 ? -9.106  10.634  3.952   1 17.559  ? 513  TRP B C     1 
ATOM   8135 O  O     . TRP B 1 521 ? -9.74   10.769  2.91    1 17.828  ? 513  TRP B O     1 
ATOM   8136 C  CB    . TRP B 1 521 ? -7.881  8.43    3.597   1 18.541  ? 513  TRP B CB    1 
ATOM   8137 C  CG    . TRP B 1 521 ? -6.563  9.141   3.426   1 20.485  ? 513  TRP B CG    1 
ATOM   8138 C  CD1   . TRP B 1 521 ? -6.17   9.915   2.364   1 21.417  ? 513  TRP B CD1   1 
ATOM   8139 C  CD2   . TRP B 1 521 ? -5.509  9.24    4.41    1 20.211  ? 513  TRP B CD2   1 
ATOM   8140 N  NE1   . TRP B 1 521 ? -4.927  10.449  2.589   1 20.368  ? 513  TRP B NE1   1 
ATOM   8141 C  CE2   . TRP B 1 521 ? -4.495  10.063  3.836   1 20.469  ? 513  TRP B CE2   1 
ATOM   8142 C  CE3   . TRP B 1 521 ? -5.321  8.721   5.711   1 19.457  ? 513  TRP B CE3   1 
ATOM   8143 C  CZ2   . TRP B 1 521 ? -3.309  10.373  4.521   1 20.663  ? 513  TRP B CZ2   1 
ATOM   8144 C  CZ3   . TRP B 1 521 ? -4.156  9.048   6.397   1 20.894  ? 513  TRP B CZ3   1 
ATOM   8145 C  CH2   . TRP B 1 521 ? -3.161  9.863   5.805   1 20.736  ? 513  TRP B CH2   1 
ATOM   8146 N  N     . ILE B 1 522 ? -8.624  11.654  4.663   1 17.903  ? 514  ILE B N     1 
ATOM   8147 C  CA    . ILE B 1 522 ? -8.795  13.047  4.266   1 19.761  ? 514  ILE B CA    1 
ATOM   8148 C  C     . ILE B 1 522 ? -7.386  13.585  3.997   1 21.926  ? 514  ILE B C     1 
ATOM   8149 O  O     . ILE B 1 522 ? -6.641  13.779  4.972   1 24.202  ? 514  ILE B O     1 
ATOM   8150 C  CB    . ILE B 1 522 ? -9.596  13.88   5.304   1 21.844  ? 514  ILE B CB    1 
ATOM   8151 C  CG1   . ILE B 1 522 ? -10.937 13.219  5.8     1 23.272  ? 514  ILE B CG1   1 
ATOM   8152 C  CG2   . ILE B 1 522 ? -9.779  15.34   4.86    1 21.955  ? 514  ILE B CG2   1 
ATOM   8153 C  CD1   . ILE B 1 522 ? -12.141 13.223  4.875   1 24.777  ? 514  ILE B CD1   1 
ATOM   8154 N  N     . PRO B 1 523 ? -6.956  13.81   2.716   1 20.722  ? 515  PRO B N     1 
ATOM   8155 C  CA    . PRO B 1 523 ? -5.64   14.396  2.446   1 19.769  ? 515  PRO B CA    1 
ATOM   8156 C  C     . PRO B 1 523 ? -5.466  15.8    3.021   1 19.206  ? 515  PRO B C     1 
ATOM   8157 O  O     . PRO B 1 523 ? -6.445  16.549  3.166   1 16.728  ? 515  PRO B O     1 
ATOM   8158 C  CB    . PRO B 1 523 ? -5.464  14.36   0.927   1 20.257  ? 515  PRO B CB    1 
ATOM   8159 C  CG    . PRO B 1 523 ? -6.875  14.182  0.39    1 21.92   ? 515  PRO B CG    1 
ATOM   8160 C  CD    . PRO B 1 523 ? -7.695  13.516  1.471   1 20.773  ? 515  PRO B CD    1 
ATOM   8161 N  N     . GLY B 1 524 ? -4.2    16.12   3.34    1 18.64   ? 516  GLY B N     1 
ATOM   8162 C  CA    . GLY B 1 524 ? -3.744  17.433  3.759   1 19.213  ? 516  GLY B CA    1 
ATOM   8163 C  C     . GLY B 1 524 ? -4.253  18.578  2.877   1 21.973  ? 516  GLY B C     1 
ATOM   8164 O  O     . GLY B 1 524 ? -4.756  19.565  3.431   1 20.297  ? 516  GLY B O     1 
ATOM   8165 N  N     . GLU B 1 525 ? -4.193  18.371  1.539   1 23.583  ? 517  GLU B N     1 
ATOM   8166 C  CA    . GLU B 1 525 ? -4.508  19.336  0.475   1 28.184  ? 517  GLU B CA    1 
ATOM   8167 C  C     . GLU B 1 525 ? -5.943  19.881  0.585   1 26.035  ? 517  GLU B C     1 
ATOM   8168 O  O     . GLU B 1 525 ? -6.178  21.025  0.185   1 27.658  ? 517  GLU B O     1 
ATOM   8169 C  CB    . GLU B 1 525 ? -4.431  18.897  -0.998  1 36.395  ? 517  GLU B CB    1 
ATOM   8170 C  CG    . GLU B 1 525 ? -3.476  17.778  -1.415  1 49.452  ? 517  GLU B CG    1 
ATOM   8171 C  CD    . GLU B 1 525 ? -4.03   16.869  -2.521  1 59.147  ? 517  GLU B CD    1 
ATOM   8172 O  OE1   . GLU B 1 525 ? -5.095  16.218  -2.34   1 56.678  ? 517  GLU B OE1   1 
ATOM   8173 O  OE2   . GLU B 1 525 ? -3.379  16.79   -3.59   1 65.839  ? 517  GLU B OE2   1 
ATOM   8174 N  N     . VAL B 1 526 ? -6.877  19.07   1.124   1 22.843  ? 518  VAL B N     1 
ATOM   8175 C  CA    . VAL B 1 526 ? -8.296  19.423  1.222   1 22.262  ? 518  VAL B CA    1 
ATOM   8176 C  C     . VAL B 1 526 ? -8.662  19.97   2.615   1 21.462  ? 518  VAL B C     1 
ATOM   8177 O  O     . VAL B 1 526 ? -9.781  20.469  2.79    1 19.838  ? 518  VAL B O     1 
ATOM   8178 C  CB    . VAL B 1 526 ? -9.284  18.354  0.689   1 22.215  ? 518  VAL B CB    1 
ATOM   8179 C  CG1   . VAL B 1 526 ? -9.003  17.954  -0.768  1 22.293  ? 518  VAL B CG1   1 
ATOM   8180 C  CG2   . VAL B 1 526 ? -9.386  17.117  1.58    1 19.593  ? 518  VAL B CG2   1 
ATOM   8181 N  N     . THR B 1 527 ? -7.716  19.874  3.58    1 21.818  ? 519  THR B N     1 
ATOM   8182 C  CA    . THR B 1 527 ? -7.886  20.248  4.978   1 20.41   ? 519  THR B CA    1 
ATOM   8183 C  C     . THR B 1 527 ? -7.407  21.693  5.136   1 22.618  ? 519  THR B C     1 
ATOM   8184 O  O     . THR B 1 527 ? -6.204  21.915  4.932   1 23.76   ? 519  THR B O     1 
ATOM   8185 C  CB    . THR B 1 527 ? -7.154  19.269  5.906   1 19.211  ? 519  THR B CB    1 
ATOM   8186 O  OG1   . THR B 1 527 ? -7.522  17.931  5.569   1 20.044  ? 519  THR B OG1   1 
ATOM   8187 C  CG2   . THR B 1 527 ? -7.489  19.473  7.374   1 17.87   ? 519  THR B CG2   1 
ATOM   8188 N  N     . PRO B 1 528 ? -8.283  22.697  5.469   1 23.365  ? 520  PRO B N     1 
ATOM   8189 C  CA    . PRO B 1 528 ? -7.821  24.05   5.803   1 24.087  ? 520  PRO B CA    1 
ATOM   8190 C  C     . PRO B 1 528 ? -6.776  24.056  6.921   1 26.165  ? 520  PRO B C     1 
ATOM   8191 O  O     . PRO B 1 528 ? -6.963  23.373  7.94    1 25.822  ? 520  PRO B O     1 
ATOM   8192 C  CB    . PRO B 1 528 ? -9.082  24.825  6.184   1 23.872  ? 520  PRO B CB    1 
ATOM   8193 C  CG    . PRO B 1 528 ? -10.201 24.044  5.521   1 22.876  ? 520  PRO B CG    1 
ATOM   8194 C  CD    . PRO B 1 528 ? -9.759  22.607  5.55    1 23.04   ? 520  PRO B CD    1 
ATOM   8195 N  N     . ASP B 1 529 ? -5.635  24.732  6.647   1 23.297  ? 521  ASP B N     1 
ATOM   8196 C  CA    . ASP B 1 529 ? -4.564  25.03   7.6     1 22.115  ? 521  ASP B CA    1 
ATOM   8197 C  C     . ASP B 1 529 ? -3.812  23.79   8.07    1 21.591  ? 521  ASP B C     1 
ATOM   8198 O  O     . ASP B 1 529 ? -3.164  23.83   9.127   1 22.735  ? 521  ASP B O     1 
ATOM   8199 C  CB    . ASP B 1 529 ? -5.042  25.908  8.753   1 22.653  ? 521  ASP B CB    1 
ATOM   8200 C  CG    . ASP B 1 529 ? -5.825  27.133  8.317   1 24.375  ? 521  ASP B CG    1 
ATOM   8201 O  OD1   . ASP B 1 529 ? -5.218  27.976  7.637   1 25.332  ? 521  ASP B OD1   1 
ATOM   8202 O  OD2   . ASP B 1 529 ? -7.029  27.201  8.625   1 26.779  ? 521  ASP B OD2   1 
ATOM   8203 N  N     . PHE B 1 530 ? -3.829  22.732  7.246   1 20.004  ? 522  PHE B N     1 
ATOM   8204 C  CA    . PHE B 1 530 ? -3.065  21.509  7.46    1 22.289  ? 522  PHE B CA    1 
ATOM   8205 C  C     . PHE B 1 530 ? -1.566  21.785  7.636   1 23.463  ? 522  PHE B C     1 
ATOM   8206 O  O     . PHE B 1 530 ? -0.938  21.129  8.466   1 22.7    ? 522  PHE B O     1 
ATOM   8207 C  CB    . PHE B 1 530 ? -3.312  20.466  6.369   1 20.115  ? 522  PHE B CB    1 
ATOM   8208 C  CG    . PHE B 1 530 ? -2.753  19.087  6.691   1 20.326  ? 522  PHE B CG    1 
ATOM   8209 C  CD1   . PHE B 1 530 ? -3.535  18.137  7.382   1 18.443  ? 522  PHE B CD1   1 
ATOM   8210 C  CD2   . PHE B 1 530 ? -1.445  18.728  6.288   1 21.195  ? 522  PHE B CD2   1 
ATOM   8211 C  CE1   . PHE B 1 530 ? -3.023  16.855  7.626   1 17.62   ? 522  PHE B CE1   1 
ATOM   8212 C  CE2   . PHE B 1 530 ? -0.926  17.461  6.568   1 20.231  ? 522  PHE B CE2   1 
ATOM   8213 C  CZ    . PHE B 1 530 ? -1.71   16.531  7.251   1 18.5    ? 522  PHE B CZ    1 
ATOM   8214 N  N     . GLU B 1 531 ? -1.022  22.722  6.838   1 25.225  ? 523  GLU B N     1 
ATOM   8215 C  CA    . GLU B 1 531 ? 0.393   23.088  6.831   1 25.205  ? 523  GLU B CA    1 
ATOM   8216 C  C     . GLU B 1 531 ? 0.836   23.783  8.124   1 25.451  ? 523  GLU B C     1 
ATOM   8217 O  O     . GLU B 1 531 ? 2.028   23.721  8.43    1 26.192  ? 523  GLU B O     1 
ATOM   8218 C  CB    . GLU B 1 531 ? 0.87    23.776  5.542   1 27.065  ? 523  GLU B CB    1 
ATOM   8219 C  CG    . GLU B 1 531 ? 0.798   22.91   4.279   1 29.204  ? 523  GLU B CG    1 
ATOM   8220 C  CD    . GLU B 1 531 ? 1.309   21.472  4.312   1 29.723  ? 523  GLU B CD    1 
ATOM   8221 O  OE1   . GLU B 1 531 ? 2.437   21.274  4.814   1 34.363  ? 523  GLU B OE1   1 
ATOM   8222 O  OE2   . GLU B 1 531 ? 0.599   20.54   3.864   1 31.273  ? 523  GLU B OE2   1 
ATOM   8223 N  N     . THR B 1 532 ? -0.101  24.406  8.868   1 26.294  ? 524  THR B N     1 
ATOM   8224 C  CA    . THR B 1 532 ? 0.207   25.255  10.018  1 30.526  ? 524  THR B CA    1 
ATOM   8225 C  C     . THR B 1 532 ? -0.405  24.753  11.339  1 32.916  ? 524  THR B C     1 
ATOM   8226 O  O     . THR B 1 532 ? -0.001  25.255  12.391  1 38.267  ? 524  THR B O     1 
ATOM   8227 C  CB    . THR B 1 532 ? -0.115  26.734  9.753   1 31.433  ? 524  THR B CB    1 
ATOM   8228 O  OG1   . THR B 1 532 ? -1.52   26.806  9.536   1 36.138  ? 524  THR B OG1   1 
ATOM   8229 C  CG2   . THR B 1 532 ? 0.686   27.385  8.634   1 31.417  ? 524  THR B CG2   1 
ATOM   8230 N  N     . LYS B 1 533 ? -1.367  23.807  11.305  1 29.986  ? 525  LYS B N     1 
ATOM   8231 C  CA    . LYS B 1 533 ? -2.061  23.314  12.501  1 30.241  ? 525  LYS B CA    1 
ATOM   8232 C  C     . LYS B 1 533 ? -1.915  21.799  12.638  1 30.4    ? 525  LYS B C     1 
ATOM   8233 O  O     . LYS B 1 533 ? -2.145  21.065  11.676  1 31.579  ? 525  LYS B O     1 
ATOM   8234 C  CB    . LYS B 1 533 ? -3.544  23.71   12.567  1 31.194  ? 525  LYS B CB    1 
ATOM   8235 C  CG    . LYS B 1 533 ? -3.798  25.191  12.803  1 35.54   ? 525  LYS B CG    1 
ATOM   8236 C  CD    . LYS B 1 533 ? -5.26   25.614  12.799  1 37.564  ? 525  LYS B CD    1 
ATOM   8237 C  CE    . LYS B 1 533 ? -5.309  27.104  12.658  1 41.883  ? 525  LYS B CE    1 
ATOM   8238 N  NZ    . LYS B 1 533 ? -6.508  27.71   13.243  1 52.125  ? 525  LYS B NZ    1 
ATOM   8239 N  N     . GLY B 1 534 ? -1.516  21.362  13.843  1 26.714  ? 526  GLY B N     1 
ATOM   8240 C  CA    . GLY B 1 534 ? -1.519  19.969  14.27   1 25.283  ? 526  GLY B CA    1 
ATOM   8241 C  C     . GLY B 1 534 ? -2.789  19.623  15.051  1 25.425  ? 526  GLY B C     1 
ATOM   8242 O  O     . GLY B 1 534 ? -3.588  20.509  15.366  1 23.412  ? 526  GLY B O     1 
ATOM   8243 N  N     . LEU B 1 535 ? -2.937  18.325  15.395  1 24.792  ? 527  LEU B N     1 
ATOM   8244 C  CA    . LEU B 1 535 ? -3.988  17.841  16.298  1 22.558  ? 527  LEU B CA    1 
ATOM   8245 C  C     . LEU B 1 535 ? -3.76   18.346  17.732  1 21.033  ? 527  LEU B C     1 
ATOM   8246 O  O     . LEU B 1 535 ? -4.728  18.516  18.474  1 20.326  ? 527  LEU B O     1 
ATOM   8247 C  CB    . LEU B 1 535 ? -4.224  16.327  16.242  1 20.09   ? 527  LEU B CB    1 
ATOM   8248 C  CG    . LEU B 1 535 ? -4.644  15.687  14.909  1 20.595  ? 527  LEU B CG    1 
ATOM   8249 C  CD1   . LEU B 1 535 ? -4.743  14.184  15.151  1 18.404  ? 527  LEU B CD1   1 
ATOM   8250 C  CD2   . LEU B 1 535 ? -5.915  16.21   14.206  1 19.883  ? 527  LEU B CD2   1 
ATOM   8251 N  N     . VAL B 1 536 ? -2.482  18.597  18.087  1 19.731  ? 528  VAL B N     1 
ATOM   8252 C  CA    . VAL B 1 536 ? -2.005  18.93   19.425  1 20.353  ? 528  VAL B CA    1 
ATOM   8253 C  C     . VAL B 1 536 ? -1.342  20.306  19.321  1 24.023  ? 528  VAL B C     1 
ATOM   8254 O  O     . VAL B 1 536 ? -0.412  20.49   18.525  1 27.348  ? 528  VAL B O     1 
ATOM   8255 C  CB    . VAL B 1 536 ? -1.045  17.892  20.065  1 20.622  ? 528  VAL B CB    1 
ATOM   8256 C  CG1   . VAL B 1 536 ? -0.796  18.15   21.556  1 18.674  ? 528  VAL B CG1   1 
ATOM   8257 C  CG2   . VAL B 1 536 ? -1.475  16.436  19.854  1 21.244  ? 528  VAL B CG2   1 
ATOM   8258 N  N     . ASP B 1 537 ? -1.809  21.26   20.142  1 27.608  ? 529  ASP B N     1 
ATOM   8259 C  CA    . ASP B 1 537 ? -1.148  22.557  20.229  1 30.573  ? 529  ASP B CA    1 
ATOM   8260 C  C     . ASP B 1 537 ? 0.147   22.416  21.017  1 29.799  ? 529  ASP B C     1 
ATOM   8261 O  O     . ASP B 1 537 ? 0.183   21.785  22.08   1 30.646  ? 529  ASP B O     1 
ATOM   8262 C  CB    . ASP B 1 537 ? -2.036  23.699  20.692  1 35.308  ? 529  ASP B CB    1 
ATOM   8263 C  CG    . ASP B 1 537 ? -3.108  24.148  19.71   1 41.451  ? 529  ASP B CG    1 
ATOM   8264 O  OD1   . ASP B 1 537 ? -2.797  24.32   18.501  1 42.425  ? 529  ASP B OD1   1 
ATOM   8265 O  OD2   . ASP B 1 537 ? -4.24   24.359  20.188  1 43.576  ? 529  ASP B OD2   1 
ATOM   8266 N  N     . LEU B 1 538 ? 1.197   22.996  20.431  1 27.692  ? 530  LEU B N     1 
ATOM   8267 C  CA    . LEU B 1 538 ? 2.51    23.108  21.047  1 27.678  ? 530  LEU B CA    1 
ATOM   8268 C  C     . LEU B 1 538 ? 2.433   23.974  22.31   1 24.32   ? 530  LEU B C     1 
ATOM   8269 O  O     . LEU B 1 538 ? 1.731   24.988  22.298  1 24.419  ? 530  LEU B O     1 
ATOM   8270 C  CB    . LEU B 1 538 ? 3.609   23.55   20.081  1 27.491  ? 530  LEU B CB    1 
ATOM   8271 C  CG    . LEU B 1 538 ? 4.028   22.534  19.004  1 28.229  ? 530  LEU B CG    1 
ATOM   8272 C  CD1   . LEU B 1 538 ? 5.075   23.204  18.14   1 26.305  ? 530  LEU B CD1   1 
ATOM   8273 C  CD2   . LEU B 1 538 ? 4.522   21.144  19.452  1 26.106  ? 530  LEU B CD2   1 
ATOM   8274 N  N     . PRO B 1 539 ? 3.122   23.618  23.432  1 23.878  ? 531  PRO B N     1 
ATOM   8275 C  CA    . PRO B 1 539 ? 3.315   24.561  24.541  1 22.433  ? 531  PRO B CA    1 
ATOM   8276 C  C     . PRO B 1 539 ? 4.169   25.756  24.126  1 21.363  ? 531  PRO B C     1 
ATOM   8277 O  O     . PRO B 1 539 ? 4.851   25.676  23.103  1 21.658  ? 531  PRO B O     1 
ATOM   8278 C  CB    . PRO B 1 539 ? 3.936   23.704  25.641  1 22.713  ? 531  PRO B CB    1 
ATOM   8279 C  CG    . PRO B 1 539 ? 4.667   22.617  24.873  1 23.136  ? 531  PRO B CG    1 
ATOM   8280 C  CD    . PRO B 1 539 ? 3.785   22.322  23.696  1 23.424  ? 531  PRO B CD    1 
ATOM   8281 N  N     . LYS B 1 540 ? 4.116   26.842  24.917  1 22.808  ? 532  LYS B N     1 
ATOM   8282 C  CA    . LYS B 1 540 ? 4.857   28.083  24.677  1 23.157  ? 532  LYS B CA    1 
ATOM   8283 C  C     . LYS B 1 540 ? 6.373   27.824  24.674  1 22.628  ? 532  LYS B C     1 
ATOM   8284 O  O     . LYS B 1 540 ? 6.855   26.911  25.365  1 22.474  ? 532  LYS B O     1 
ATOM   8285 C  CB    . LYS B 1 540 ? 4.402   29.221  25.598  1 20.426  ? 532  LYS B CB    1 
ATOM   8286 C  CG    . LYS B 1 540 ? 4.857   29.121  27.054  1 21.267  ? 532  LYS B CG    1 
ATOM   8287 C  CD    . LYS B 1 540 ? 4.455   30.294  27.945  1 21.142  ? 532  LYS B CD    1 
ATOM   8288 C  CE    . LYS B 1 540 ? 5.26    30.222  29.211  1 21.505  ? 532  LYS B CE    1 
ATOM   8289 N  NZ    . LYS B 1 540 ? 5.103   31.426  30.027  1 20.77   ? 532  LYS B NZ    1 
ATOM   8290 N  N     . GLU B 1 541 ? 7.09    28.623  23.867  1 21.29   ? 533  GLU B N     1 
ATOM   8291 C  CA    . GLU B 1 541 ? 8.54    28.574  23.754  1 21.98   ? 533  GLU B CA    1 
ATOM   8292 C  C     . GLU B 1 541 ? 9.211   29.063  25.042  1 22.354  ? 533  GLU B C     1 
ATOM   8293 O  O     . GLU B 1 541 ? 10.109  28.377  25.536  1 22.042  ? 533  GLU B O     1 
ATOM   8294 C  CB    . GLU B 1 541 ? 8.989   29.31   22.498  1 24.818  ? 533  GLU B CB    1 
ATOM   8295 C  CG    . GLU B 1 541 ? 10.467  29.106  22.175  1 28.003  ? 533  GLU B CG    1 
ATOM   8296 C  CD    . GLU B 1 541 ? 11.022  29.835  20.966  1 31.279  ? 533  GLU B CD    1 
ATOM   8297 O  OE1   . GLU B 1 541 ? 10.3    30.485  20.179  1 31.884  ? 533  GLU B OE1   1 
ATOM   8298 O  OE2   . GLU B 1 541 ? 12.244  29.734  20.829  1 33.203  ? 533  GLU B OE2   1 
ATOM   8299 N  N     . GLU B 1 542 ? 8.779   30.229  25.555  1 21.353  ? 534  GLU B N     1 
ATOM   8300 C  CA    . GLU B 1 542 ? 9.382   30.898  26.699  1 23.611  ? 534  GLU B CA    1 
ATOM   8301 C  C     . GLU B 1 542 ? 9.384   29.953  27.908  1 24.029  ? 534  GLU B C     1 
ATOM   8302 O  O     . GLU B 1 542 ? 8.39    29.274  28.172  1 23.007  ? 534  GLU B O     1 
ATOM   8303 C  CB    . GLU B 1 542 ? 8.829   32.323  26.804  1 26.706  ? 534  GLU B CB    1 
ATOM   8304 C  CG    . GLU B 1 542 ? 8.816   32.964  28.189  1 32.936  ? 534  GLU B CG    1 
ATOM   8305 C  CD    . GLU B 1 542 ? 7.806   34.099  28.298  1 38.571  ? 534  GLU B CD    1 
ATOM   8306 O  OE1   . GLU B 1 542 ? 6.575   33.916  28.082  1 39.841  ? 534  GLU B OE1   1 
ATOM   8307 O  OE2   . GLU B 1 542 ? 8.285   35.2    28.631  1 43.147  ? 534  GLU B OE2   1 
ATOM   8308 N  N     . HIS B 1 543 ? 10.55   29.895  28.574  1 22.995  ? 535  HIS B N     1 
ATOM   8309 C  CA    . HIS B 1 543 ? 10.764  29.174  29.823  1 22.313  ? 535  HIS B CA    1 
ATOM   8310 C  C     . HIS B 1 543 ? 9.942   29.816  30.938  1 19.826  ? 535  HIS B C     1 
ATOM   8311 O  O     . HIS B 1 543 ? 9.831   31.039  30.985  1 21.704  ? 535  HIS B O     1 
ATOM   8312 C  CB    . HIS B 1 543 ? 12.261  29.09   30.146  1 20.619  ? 535  HIS B CB    1 
ATOM   8313 C  CG    . HIS B 1 543 ? 13.089  28.318  29.167  1 20.274  ? 535  HIS B CG    1 
ATOM   8314 N  ND1   . HIS B 1 543 ? 14.359  28.732  28.826  1 20.924  ? 535  HIS B ND1   1 
ATOM   8315 C  CD2   . HIS B 1 543 ? 12.888  27.186  28.5    1 19.565  ? 535  HIS B CD2   1 
ATOM   8316 C  CE1   . HIS B 1 543 ? 14.883  27.874  27.953  1 21.285  ? 535  HIS B CE1   1 
ATOM   8317 N  NE2   . HIS B 1 543 ? 14.003  26.919  27.744  1 22.632  ? 535  HIS B NE2   1 
ATOM   8318 N  N     . TRP B 1 544 ? 9.318   28.967  31.773  1 19.67   ? 536  TRP B N     1 
ATOM   8319 C  CA    . TRP B 1 544 ? 8.711   29.359  33.042  1 19.539  ? 536  TRP B CA    1 
ATOM   8320 C  C     . TRP B 1 544 ? 9.793   29.822  34.016  1 20.781  ? 536  TRP B C     1 
ATOM   8321 O  O     . TRP B 1 544 ? 9.601   30.837  34.686  1 23.513  ? 536  TRP B O     1 
ATOM   8322 C  CB    . TRP B 1 544 ? 7.886   28.238  33.695  1 19.769  ? 536  TRP B CB    1 
ATOM   8323 C  CG    . TRP B 1 544 ? 6.699   27.699  32.932  1 18.633  ? 536  TRP B CG    1 
ATOM   8324 C  CD1   . TRP B 1 544 ? 6.616   26.458  32.372  1 17.558  ? 536  TRP B CD1   1 
ATOM   8325 C  CD2   . TRP B 1 544 ? 5.427   28.343  32.685  1 19.455  ? 536  TRP B CD2   1 
ATOM   8326 N  NE1   . TRP B 1 544 ? 5.391   26.272  31.796  1 18.298  ? 536  TRP B NE1   1 
ATOM   8327 C  CE2   . TRP B 1 544 ? 4.638   27.408  31.961  1 18.956  ? 536  TRP B CE2   1 
ATOM   8328 C  CE3   . TRP B 1 544 ? 4.878   29.606  32.998  1 18.457  ? 536  TRP B CE3   1 
ATOM   8329 C  CZ2   . TRP B 1 544 ? 3.333   27.701  31.541  1 19.851  ? 536  TRP B CZ2   1 
ATOM   8330 C  CZ3   . TRP B 1 544 ? 3.583   29.891  32.597  1 19.567  ? 536  TRP B CZ3   1 
ATOM   8331 C  CH2   . TRP B 1 544 ? 2.824   28.952  31.868  1 20.202  ? 536  TRP B CH2   1 
ATOM   8332 N  N     . ALA B 1 545 ? 10.895  29.058  34.118  1 19.389  ? 537  ALA B N     1 
ATOM   8333 C  CA    . ALA B 1 545 ? 11.89   29.27   35.158  1 20.033  ? 537  ALA B CA    1 
ATOM   8334 C  C     . ALA B 1 545 ? 12.89   30.352  34.744  1 20.913  ? 537  ALA B C     1 
ATOM   8335 O  O     . ALA B 1 545 ? 13.281  30.366  33.568  1 21.512  ? 537  ALA B O     1 
ATOM   8336 C  CB    . ALA B 1 545 ? 12.597  27.996  35.501  1 18.91   ? 537  ALA B CB    1 
ATOM   8337 N  N     . PRO B 1 546 ? 13.347  31.241  35.678  1 20.593  ? 538  PRO B N     1 
ATOM   8338 C  CA    . PRO B 1 546 ? 14.462  32.146  35.383  1 21.685  ? 538  PRO B CA    1 
ATOM   8339 C  C     . PRO B 1 546 ? 15.797  31.412  35.239  1 23.392  ? 538  PRO B C     1 
ATOM   8340 O  O     . PRO B 1 546 ? 15.967  30.324  35.818  1 23      ? 538  PRO B O     1 
ATOM   8341 C  CB    . PRO B 1 546 ? 14.432  33.137  36.548  1 20.706  ? 538  PRO B CB    1 
ATOM   8342 C  CG    . PRO B 1 546 ? 13.848  32.327  37.694  1 21.537  ? 538  PRO B CG    1 
ATOM   8343 C  CD    . PRO B 1 546 ? 12.825  31.428  37.058  1 18.299  ? 538  PRO B CD    1 
ATOM   8344 N  N     . LEU B 1 547 ? 16.736  32.051  34.51   1 23.372  ? 539  LEU B N     1 
ATOM   8345 C  CA    . LEU B 1 547 ? 18.095  31.561  34.272  1 26.213  ? 539  LEU B CA    1 
ATOM   8346 C  C     . LEU B 1 547 ? 18.824  31.213  35.585  1 26.467  ? 539  LEU B C     1 
ATOM   8347 O  O     . LEU B 1 547 ? 19.488  30.175  35.626  1 25.973  ? 539  LEU B O     1 
ATOM   8348 C  CB    . LEU B 1 547 ? 18.873  32.547  33.394  1 28.719  ? 539  LEU B CB    1 
ATOM   8349 C  CG    . LEU B 1 547 ? 20.293  32.172  32.928  1 33.768  ? 539  LEU B CG    1 
ATOM   8350 C  CD1   . LEU B 1 547 ? 20.418  30.993  31.923  1 30.824  ? 539  LEU B CD1   1 
ATOM   8351 C  CD2   . LEU B 1 547 ? 20.95   33.457  32.376  1 31.303  ? 539  LEU B CD2   1 
ATOM   8352 N  N     . SER B 1 548 ? 18.622  32.036  36.645  1 23.408  ? 540  SER B N     1 
ATOM   8353 C  CA    . SER B 1 548 ? 19.192  31.89   37.983  1 22.476  ? 540  SER B CA    1 
ATOM   8354 C  C     . SER B 1 548 ? 18.869  30.541  38.647  1 22.829  ? 540  SER B C     1 
ATOM   8355 O  O     . SER B 1 548 ? 19.623  30.104  39.52   1 23.18   ? 540  SER B O     1 
ATOM   8356 C  CB    . SER B 1 548 ? 18.848  33.062  38.88   1 21.43   ? 540  SER B CB    1 
ATOM   8357 O  OG    . SER B 1 548 ? 17.465  33.087  39.206  1 21.374  ? 540  SER B OG    1 
ATOM   8358 N  N     . GLN B 1 549 ? 17.779  29.879  38.215  1 20.96   ? 541  GLN B N     1 
ATOM   8359 C  CA    . GLN B 1 549 ? 17.269  28.662  38.842  1 21.073  ? 541  GLN B CA    1 
ATOM   8360 C  C     . GLN B 1 549 ? 17.975  27.395  38.335  1 21.899  ? 541  GLN B C     1 
ATOM   8361 O  O     . GLN B 1 549 ? 17.693  26.318  38.874  1 22.311  ? 541  GLN B O     1 
ATOM   8362 C  CB    . GLN B 1 549 ? 15.737  28.611  38.775  1 19.771  ? 541  GLN B CB    1 
ATOM   8363 C  CG    . GLN B 1 549 ? 15.03   29.414  39.862  1 18.113  ? 541  GLN B CG    1 
ATOM   8364 C  CD    . GLN B 1 549 ? 14.937  28.709  41.196  1 18.348  ? 541  GLN B CD    1 
ATOM   8365 O  OE1   . GLN B 1 549 ? 14.388  27.602  41.323  1 16.527  ? 541  GLN B OE1   1 
ATOM   8366 N  NE2   . GLN B 1 549 ? 15.462  29.373  42.22   1 18.571  ? 541  GLN B NE2   1 
ATOM   8367 N  N     . SER B 1 550 ? 18.867  27.521  37.324  1 21.357  ? 542  SER B N     1 
ATOM   8368 C  CA    . SER B 1 550 ? 19.648  26.42   36.761  1 23.403  ? 542  SER B CA    1 
ATOM   8369 C  C     . SER B 1 550 ? 20.503  25.726  37.825  1 20.683  ? 542  SER B C     1 
ATOM   8370 O  O     . SER B 1 550 ? 21.206  26.443  38.542  1 21.788  ? 542  SER B O     1 
ATOM   8371 C  CB    . SER B 1 550 ? 20.54   26.84   35.632  1 25.956  ? 542  SER B CB    1 
ATOM   8372 O  OG    . SER B 1 550 ? 21.151  25.669  35.095  1 31.382  ? 542  SER B OG    1 
ATOM   8373 N  N     . PRO B 1 551 ? 20.483  24.359  37.934  1 18.723  ? 543  PRO B N     1 
ATOM   8374 C  CA    . PRO B 1 551 ? 21.438  23.647  38.777  1 19.203  ? 543  PRO B CA    1 
ATOM   8375 C  C     . PRO B 1 551 ? 22.885  23.765  38.288  1 20.562  ? 543  PRO B C     1 
ATOM   8376 O  O     . PRO B 1 551 ? 23.82   23.713  39.089  1 20.841  ? 543  PRO B O     1 
ATOM   8377 C  CB    . PRO B 1 551 ? 20.894  22.223  38.824  1 20.233  ? 543  PRO B CB    1 
ATOM   8378 C  CG    . PRO B 1 551 ? 20.12   22.08   37.514  1 20.249  ? 543  PRO B CG    1 
ATOM   8379 C  CD    . PRO B 1 551 ? 19.549  23.429  37.249  1 19.825  ? 543  PRO B CD    1 
ATOM   8380 N  N     . TYR B 1 552 ? 23.034  23.936  36.963  1 22.016  ? 544  TYR B N     1 
ATOM   8381 C  CA    . TYR B 1 552 ? 24.31   23.987  36.265  1 23.803  ? 544  TYR B CA    1 
ATOM   8382 C  C     . TYR B 1 552 ? 24.85   25.412  36.254  1 24.814  ? 544  TYR B C     1 
ATOM   8383 O  O     . TYR B 1 552 ? 24.129  26.365  35.918  1 25.942  ? 544  TYR B O     1 
ATOM   8384 C  CB    . TYR B 1 552 ? 24.103  23.405  34.867  1 23.453  ? 544  TYR B CB    1 
ATOM   8385 C  CG    . TYR B 1 552 ? 25.172  23.664  33.813  1 24.276  ? 544  TYR B CG    1 
ATOM   8386 C  CD1   . TYR B 1 552 ? 26.327  22.863  33.735  1 22.145  ? 544  TYR B CD1   1 
ATOM   8387 C  CD2   . TYR B 1 552 ? 25.025  24.732  32.902  1 22.571  ? 544  TYR B CD2   1 
ATOM   8388 C  CE1   . TYR B 1 552 ? 27.298  23.116  32.766  1 22.26   ? 544  TYR B CE1   1 
ATOM   8389 C  CE2   . TYR B 1 552 ? 25.99   24.979  31.929  1 22.242  ? 544  TYR B CE2   1 
ATOM   8390 C  CZ    . TYR B 1 552 ? 27.114  24.158  31.854  1 22.77   ? 544  TYR B CZ    1 
ATOM   8391 O  OH    . TYR B 1 552 ? 28.046  24.42   30.891  1 25.382  ? 544  TYR B OH    1 
ATOM   8392 N  N     . ASP B 1 553 ? 26.148  25.481  36.575  1 25.86   ? 545  ASP B N     1 
ATOM   8393 C  CA    . ASP B 1 553 ? 26.998  26.651  36.441  1 25.004  ? 545  ASP B CA    1 
ATOM   8394 C  C     . ASP B 1 553 ? 28.111  26.33   35.434  1 24.023  ? 545  ASP B C     1 
ATOM   8395 O  O     . ASP B 1 553 ? 28.934  25.45   35.736  1 23.003  ? 545  ASP B O     1 
ATOM   8396 C  CB    . ASP B 1 553 ? 27.465  27.157  37.801  1 27.841  ? 545  ASP B CB    1 
ATOM   8397 C  CG    . ASP B 1 553 ? 28.395  28.371  37.86   1 29.623  ? 545  ASP B CG    1 
ATOM   8398 O  OD1   . ASP B 1 553 ? 28.73   28.99   36.813  1 26.714  ? 545  ASP B OD1   1 
ATOM   8399 O  OD2   . ASP B 1 553 ? 28.787  28.71   38.998  1 35.545  ? 545  ASP B OD2   1 
ATOM   8400 N  N     . PRO B 1 554 ? 28.202  27.053  34.269  1 22.673  ? 546  PRO B N     1 
ATOM   8401 C  CA    . PRO B 1 554 ? 29.273  26.839  33.286  1 24.363  ? 546  PRO B CA    1 
ATOM   8402 C  C     . PRO B 1 554 ? 30.706  27.029  33.794  1 25.025  ? 546  PRO B C     1 
ATOM   8403 O  O     . PRO B 1 554 ? 31.62   26.494  33.182  1 28.982  ? 546  PRO B O     1 
ATOM   8404 C  CB    . PRO B 1 554 ? 28.89   27.711  32.076  1 23.933  ? 546  PRO B CB    1 
ATOM   8405 C  CG    . PRO B 1 554 ? 28.049  28.797  32.719  1 24.022  ? 546  PRO B CG    1 
ATOM   8406 C  CD    . PRO B 1 554 ? 27.289  28.134  33.827  1 22.571  ? 546  PRO B CD    1 
ATOM   8407 N  N     . ASP B 1 555 ? 30.872  27.733  34.928  1 25.793  ? 547  ASP B N     1 
ATOM   8408 C  CA    . ASP B 1 555 ? 32.142  28.09   35.546  1 27.902  ? 547  ASP B CA    1 
ATOM   8409 C  C     . ASP B 1 555 ? 32.56   27.13   36.662  1 29.15   ? 547  ASP B C     1 
ATOM   8410 O  O     . ASP B 1 555 ? 33.735  27.149  37.054  1 31.246  ? 547  ASP B O     1 
ATOM   8411 C  CB    . ASP B 1 555 ? 32.156  29.574  35.897  1 28.045  ? 547  ASP B CB    1 
ATOM   8412 C  CG    . ASP B 1 555 ? 32.035  30.494  34.689  1 28.75   ? 547  ASP B CG    1 
ATOM   8413 O  OD1   . ASP B 1 555 ? 32.817  30.312  33.735  1 31.157  ? 547  ASP B OD1   1 
ATOM   8414 O  OD2   . ASP B 1 555 ? 31.121  31.33   34.668  1 31.053  ? 547  ASP B OD2   1 
ATOM   8415 N  N     . ALA B 1 556 ? 31.624  26.301  37.162  1 27.948  ? 548  ALA B N     1 
ATOM   8416 C  CA    . ALA B 1 556 ? 31.85   25.33   38.23   1 25.578  ? 548  ALA B CA    1 
ATOM   8417 C  C     . ALA B 1 556 ? 32.749  24.173  37.76   1 25.446  ? 548  ALA B C     1 
ATOM   8418 O  O     . ALA B 1 556 ? 33.341  23.516  38.638  1 27.109  ? 548  ALA B O     1 
ATOM   8419 C  CB    . ALA B 1 556 ? 30.52   24.849  38.759  1 25.7    ? 548  ALA B CB    1 
ATOM   8420 O  OXT   . ALA B 1 556 ? 32.841  23.936  36.544  1 25.863  ? 548  ALA B OXT   1 
HETATM 8421 C  "C1'" . HBA C 2 .   ? 11.766  7.897   45.168  1 22.109  ? 601  HBA A "C1'" 1 
HETATM 8422 O  "O1'" . HBA C 2 .   ? 10.643  7.438   45.293  1 22.831  ? 601  HBA A "O1'" 1 
HETATM 8423 C  C1    . HBA C 2 .   ? 12.185  8.985   44.25   1 20.191  ? 601  HBA A C1    1 
HETATM 8424 C  C2    . HBA C 2 .   ? 11.295  9.531   43.306  1 18.605  ? 601  HBA A C2    1 
HETATM 8425 C  C3    . HBA C 2 .   ? 11.694  10.559  42.46   1 18.134  ? 601  HBA A C3    1 
HETATM 8426 C  C4    . HBA C 2 .   ? 12.985  11.084  42.586  1 19.322  ? 601  HBA A C4    1 
HETATM 8427 C  C5    . HBA C 2 .   ? 13.865  10.594  43.558  1 20.043  ? 601  HBA A C5    1 
HETATM 8428 C  C6    . HBA C 2 .   ? 13.471  9.542   44.379  1 20.49   ? 601  HBA A C6    1 
HETATM 8429 O  O4    . HBA C 2 .   ? 13.39   12.132  41.795  1 20.764  ? 601  HBA A O4    1 
HETATM 8430 FE FE    . FE2 D 3 .   ? 8.928   9.747   47.572  1 28.744  ? 602  FE2 A FE    1 
HETATM 8431 C  "C1'" . HBA E 2 .   ? -24.988 1.032   9.828   1 28.74   ? 601  HBA B "C1'" 1 
HETATM 8432 O  "O1'" . HBA E 2 .   ? -25.247 0.338   8.879   1 34.905  ? 601  HBA B "O1'" 1 
HETATM 8433 C  C1    . HBA E 2 .   ? -25.831 2.099   10.406  1 25.534  ? 601  HBA B C1    1 
HETATM 8434 C  C2    . HBA E 2 .   ? -25.24  3.025   11.279  1 22.639  ? 601  HBA B C2    1 
HETATM 8435 C  C3    . HBA E 2 .   ? -25.989 4.034   11.867  1 21.93   ? 601  HBA B C3    1 
HETATM 8436 C  C4    . HBA E 2 .   ? -27.362 4.113   11.613  1 22.299  ? 601  HBA B C4    1 
HETATM 8437 C  C5    . HBA E 2 .   ? -27.983 3.184   10.759  1 22.819  ? 601  HBA B C5    1 
HETATM 8438 C  C6    . HBA E 2 .   ? -27.223 2.165   10.182  1 25.007  ? 601  HBA B C6    1 
HETATM 8439 O  O4    . HBA E 2 .   ? -28.047 5.118   12.236  1 21.383  ? 601  HBA B O4    1 
HETATM 8440 FE FE    . FE2 F 3 .   ? -22.966 2.958   6.71    1 31.361  ? 602  FE2 B FE    1 
HETATM 8441 O  O     . HOH G 4 .   ? -23.792 7.859   36.152  1 29.473  ? 701  HOH A O     1 
HETATM 8442 O  O     . HOH G 4 .   ? 22.651  -3.421  47.999  1 17.552  ? 702  HOH A O     1 
HETATM 8443 O  O     . HOH G 4 .   ? 1       12.86   24.507  1 19.619  ? 703  HOH A O     1 
HETATM 8444 O  O     . HOH G 4 .   ? -16.565 28.683  42.993  1 38.493  ? 704  HOH A O     1 
HETATM 8445 O  O     . HOH G 4 .   ? -13.940 21.071  57.756  1 26.031  ? 705  HOH A O     1 
HETATM 8446 O  O     . HOH G 4 .   ? -2.483  9.097   67.618  1 19.657  ? 706  HOH A O     1 
HETATM 8447 O  O     . HOH G 4 .   ? -0.667  29.12   61.534  1 31.913  ? 707  HOH A O     1 
HETATM 8448 O  O     . HOH G 4 .   ? -15.838 19.742  41.442  1 32.386  ? 708  HOH A O     1 
HETATM 8449 O  O     . HOH G 4 .   ? -7.035  26.26   32.804  1 25.298  ? 709  HOH A O     1 
HETATM 8450 O  O     . HOH G 4 .   ? 12.104  34.107  48.772  1 26.291  ? 710  HOH A O     1 
HETATM 8451 O  O     . HOH G 4 .   ? 12.052  14.738  47.746  1 12.107  ? 711  HOH A O     1 
HETATM 8452 O  O     . HOH G 4 .   ? 17.595  2.423   31.338  1 35.838  ? 712  HOH A O     1 
HETATM 8453 O  O     . HOH G 4 .   ? 9.508   3.595   16.459  1 33.489  ? 713  HOH A O     1 
HETATM 8454 O  O     . HOH G 4 .   ? 6.148   14.533  78.822  1 31.144  ? 714  HOH A O     1 
HETATM 8455 O  O     . HOH G 4 .   ? 0.08    12.654  52.685  1 20.103  ? 715  HOH A O     1 
HETATM 8456 O  O     . HOH G 4 .   ? -19.982 -2.218  48.104  1 21.9    ? 716  HOH A O     1 
HETATM 8457 O  O     . HOH G 4 .   ? 8.645   5.867   72.607  1 37.986  ? 717  HOH A O     1 
HETATM 8458 O  O     . HOH G 4 .   ? 2.327   -1.391  69.3    1 30.067  ? 718  HOH A O     1 
HETATM 8459 O  O     . HOH G 4 .   ? 14.029  29.874  67.653  1 34.865  ? 719  HOH A O     1 
HETATM 8460 O  O     . HOH G 4 .   ? 16.228  11.756  29.652  1 20.871  ? 720  HOH A O     1 
HETATM 8461 O  O     . HOH G 4 .   ? -21.425 22.214  44.548  1 61.092  ? 721  HOH A O     1 
HETATM 8462 O  O     . HOH G 4 .   ? -15.893 22.523  48.811  1 25.091  ? 722  HOH A O     1 
HETATM 8463 O  O     . HOH G 4 .   ? 21.958  12.017  20.825  1 36.593  ? 723  HOH A O     1 
HETATM 8464 O  O     . HOH G 4 .   ? 14.032  2.84    32.644  1 19.846  ? 724  HOH A O     1 
HETATM 8465 O  O     . HOH G 4 .   ? 39.041  -3.338  39.846  1 49.818  ? 725  HOH A O     1 
HETATM 8466 O  O     . HOH G 4 .   ? 17.18   12.759  33.055  1 17.525  ? 726  HOH A O     1 
HETATM 8467 O  O     . HOH G 4 .   ? -2.531  24.375  55.548  1 21.866  ? 727  HOH A O     1 
HETATM 8468 O  O     . HOH G 4 .   ? -33.417 16.451  12.634  1 27.518  ? 728  HOH A O     1 
HETATM 8469 O  O     . HOH G 4 .   ? 25.812  5.506   40.224  1 18.625  ? 729  HOH A O     1 
HETATM 8470 O  O     . HOH G 4 .   ? -21.38  2.24    41.258  1 27.587  ? 730  HOH A O     1 
HETATM 8471 O  O     . HOH G 4 .   ? 6.104   16.731  32.299  1 15.981  ? 731  HOH A O     1 
HETATM 8472 O  O     . HOH G 4 .   ? -4.938  3.64    66.51   1 29.781  ? 732  HOH A O     1 
HETATM 8473 O  O     . HOH G 4 .   ? 9.089   9.476   45.789  1 31.277  ? 733  HOH A O     1 
HETATM 8474 O  O     . HOH G 4 .   ? 13.973  18.596  72.038  1 33.289  ? 734  HOH A O     1 
HETATM 8475 O  O     . HOH G 4 .   ? 3.209   19.918  64.818  1 14.118  ? 735  HOH A O     1 
HETATM 8476 O  O     . HOH G 4 .   ? 12.603  22.914  21.627  1 24.658  ? 736  HOH A O     1 
HETATM 8477 O  O     . HOH G 4 .   ? 11.915  21.578  33.84   1 16.445  ? 737  HOH A O     1 
HETATM 8478 O  O     . HOH G 4 .   ? 19.95   18.273  39.632  1 17.493  ? 738  HOH A O     1 
HETATM 8479 O  O     . HOH G 4 .   ? 4.653   7.341   50.959  1 14.133  ? 739  HOH A O     1 
HETATM 8480 O  O     . HOH G 4 .   ? -47.069 13.804  17.983  1 27.345  ? 740  HOH A O     1 
HETATM 8481 O  O     . HOH G 4 .   ? 22.26   2.993   35.483  1 23.415  ? 741  HOH A O     1 
HETATM 8482 O  O     . HOH G 4 .   ? 11.97   -0.228  39.74   1 33.464  ? 742  HOH A O     1 
HETATM 8483 O  O     . HOH G 4 .   ? -20.365 4.96    52.599  1 28.083  ? 743  HOH A O     1 
HETATM 8484 O  O     . HOH G 4 .   ? 2.216   -0.876  40.342  1 16.52   ? 744  HOH A O     1 
HETATM 8485 O  O     . HOH G 4 .   ? 22.261  10.114  37.323  1 11.812  ? 745  HOH A O     1 
HETATM 8486 O  O     . HOH G 4 .   ? -2.243  4.605   44.467  1 14.453  ? 746  HOH A O     1 
HETATM 8487 O  O     . HOH G 4 .   ? -12.311 17.315  28.47   1 33.296  ? 747  HOH A O     1 
HETATM 8488 O  O     . HOH G 4 .   ? 13.24   -10.413 56.422  1 36.851  ? 748  HOH A O     1 
HETATM 8489 O  O     . HOH G 4 .   ? -15.295 16.556  38.3    1 19.839  ? 749  HOH A O     1 
HETATM 8490 O  O     . HOH G 4 .   ? -6.468  28.634  35.744  1 26.366  ? 750  HOH A O     1 
HETATM 8491 O  O     . HOH G 4 .   ? 20.956  6.926   28.857  1 32.033  ? 751  HOH A O     1 
HETATM 8492 O  O     . HOH G 4 .   ? 0.64    35.195  50.094  1 29.193  ? 752  HOH A O     1 
HETATM 8493 O  O     . HOH G 4 .   ? 25.325  -12.086 49.814  1 30.917  ? 753  HOH A O     1 
HETATM 8494 O  O     . HOH G 4 .   ? -17.637 13.794  62.795  1 42.368  ? 754  HOH A O     1 
HETATM 8495 O  O     . HOH G 4 .   ? 18.885  19.453  66.675  1 16.95   ? 755  HOH A O     1 
HETATM 8496 O  O     . HOH G 4 .   ? 19.297  22.599  69.077  1 40.285  ? 756  HOH A O     1 
HETATM 8497 O  O     . HOH G 4 .   ? 15.394  10.327  52.394  1 15.42   ? 757  HOH A O     1 
HETATM 8498 O  O     . HOH G 4 .   ? 14.185  16.393  48.811  1 16.692  ? 758  HOH A O     1 
HETATM 8499 O  O     . HOH G 4 .   ? -0.038  11.919  30.104  1 17.087  ? 759  HOH A O     1 
HETATM 8500 O  O     . HOH G 4 .   ? -6      17.853  62.75   1 17.56   ? 760  HOH A O     1 
HETATM 8501 O  O     . HOH G 4 .   ? 8.72    17.079  32.437  1 12.008  ? 761  HOH A O     1 
HETATM 8502 O  O     . HOH G 4 .   ? -10.081 18.169  45.634  1 15.143  ? 762  HOH A O     1 
HETATM 8503 O  O     . HOH G 4 .   ? -20.561 5.907   38.792  1 26.162  ? 763  HOH A O     1 
HETATM 8504 O  O     . HOH G 4 .   ? -5.061  12.114  52.883  1 25.671  ? 764  HOH A O     1 
HETATM 8505 O  O     . HOH G 4 .   ? 2.86    -1.262  42.972  1 15.797  ? 765  HOH A O     1 
HETATM 8506 O  O     . HOH G 4 .   ? 23.609  26.814  53.469  1 24.283  ? 766  HOH A O     1 
HETATM 8507 O  O     . HOH G 4 .   ? 26.777  -3.583  41.197  1 24.253  ? 767  HOH A O     1 
HETATM 8508 O  O     . HOH G 4 .   ? -5.835  8.941   67.802  1 27.956  ? 768  HOH A O     1 
HETATM 8509 O  O     . HOH G 4 .   ? 13.461  2.512   68.118  1 27.532  ? 769  HOH A O     1 
HETATM 8510 O  O     . HOH G 4 .   ? -13.882 16.374  51.96   1 30.056  ? 770  HOH A O     1 
HETATM 8511 O  O     . HOH G 4 .   ? -14.648 -9.643  54.677  1 39.097  ? 771  HOH A O     1 
HETATM 8512 O  O     . HOH G 4 .   ? -8.07   -8.843  50.639  1 15.134  ? 772  HOH A O     1 
HETATM 8513 O  O     . HOH G 4 .   ? 7.088   1.672   18.854  1 31.161  ? 773  HOH A O     1 
HETATM 8514 O  O     . HOH G 4 .   ? -0.12   21.071  32.337  1 12.086  ? 774  HOH A O     1 
HETATM 8515 O  O     . HOH G 4 .   ? -14.515 13.638  28.707  1 15.88   ? 775  HOH A O     1 
HETATM 8516 O  O     . HOH G 4 .   ? 10.721  25.321  27.704  1 16.453  ? 776  HOH A O     1 
HETATM 8517 O  O     . HOH G 4 .   ? 10.203  23.978  69.876  1 55.766  ? 777  HOH A O     1 
HETATM 8518 O  O     . HOH G 4 .   ? 0.786   0.419   33.686  1 35.089  ? 778  HOH A O     1 
HETATM 8519 O  O     . HOH G 4 .   ? -14.242 -2.14   53.179  1 17.297  ? 779  HOH A O     1 
HETATM 8520 O  O     . HOH G 4 .   ? 19.138  8.494   34.381  1 25.311  ? 780  HOH A O     1 
HETATM 8521 O  O     . HOH G 4 .   ? 30.745  8.251   48.254  1 45.799  ? 781  HOH A O     1 
HETATM 8522 O  O     . HOH G 4 .   ? -9.47   27.733  38.114  1 25.869  ? 782  HOH A O     1 
HETATM 8523 O  O     . HOH G 4 .   ? 13.002  22.081  68.775  1 27.129  ? 783  HOH A O     1 
HETATM 8524 O  O     . HOH G 4 .   ? 6.859   15.239  74.153  1 30.237  ? 784  HOH A O     1 
HETATM 8525 O  O     . HOH G 4 .   ? -18.129 -2.378  35.235  1 22.856  ? 785  HOH A O     1 
HETATM 8526 O  O     . HOH G 4 .   ? 28.932  20.217  55.52   1 22.695  ? 786  HOH A O     1 
HETATM 8527 O  O     . HOH G 4 .   ? -19.904 1.871   49.762  1 25.763  ? 787  HOH A O     1 
HETATM 8528 O  O     . HOH G 4 .   ? 13.958  29.195  61.477  1 30.882  ? 788  HOH A O     1 
HETATM 8529 O  O     . HOH G 4 .   ? 21.294  19.877  41.789  1 19.458  ? 789  HOH A O     1 
HETATM 8530 O  O     . HOH G 4 .   ? 1.887   5.804   24.153  1 24.338  ? 790  HOH A O     1 
HETATM 8531 O  O     . HOH G 4 .   ? -17.425 21.398  35.034  1 35.352  ? 791  HOH A O     1 
HETATM 8532 O  O     . HOH G 4 .   ? -7.818  -4.903  44.026  1 18.852  ? 792  HOH A O     1 
HETATM 8533 O  O     . HOH G 4 .   ? 18.605  10.392  27.139  1 18.598  ? 793  HOH A O     1 
HETATM 8534 O  O     . HOH G 4 .   ? -0.096  19.562  28.859  1 21.837  ? 794  HOH A O     1 
HETATM 8535 O  O     . HOH G 4 .   ? -2.3    8.297   61.327  1 15.97   ? 795  HOH A O     1 
HETATM 8536 O  O     . HOH G 4 .   ? 25.509  16.674  24.885  1 28.455  ? 796  HOH A O     1 
HETATM 8537 O  O     . HOH G 4 .   ? 29.669  17.783  47.181  1 37.614  ? 797  HOH A O     1 
HETATM 8538 O  O     . HOH G 4 .   ? 2.395   29.928  39.151  1 43.134  ? 798  HOH A O     1 
HETATM 8539 O  O     . HOH G 4 .   ? -0.834  17      56.355  1 19.092  ? 799  HOH A O     1 
HETATM 8540 O  O     . HOH G 4 .   ? -13.923 25.533  51.984  1 27.433  ? 800  HOH A O     1 
HETATM 8541 O  O     . HOH G 4 .   ? 0.259   10.86   55.053  1 17.547  ? 801  HOH A O     1 
HETATM 8542 O  O     . HOH G 4 .   ? 35.417  14.776  34.977  1 20.636  ? 802  HOH A O     1 
HETATM 8543 O  O     . HOH G 4 .   ? -17.932 9.632   61.18   1 25.198  ? 803  HOH A O     1 
HETATM 8544 O  O     . HOH G 4 .   ? 12.047  24.439  67.917  1 34.922  ? 804  HOH A O     1 
HETATM 8545 O  O     . HOH G 4 .   ? 5.111   -9.698  45.006  1 20.308  ? 805  HOH A O     1 
HETATM 8546 O  O     . HOH G 4 .   ? 14.336  26.545  32.443  1 16.281  ? 806  HOH A O     1 
HETATM 8547 O  O     . HOH G 4 .   ? 5.253   2.355   40.855  1 18.733  ? 807  HOH A O     1 
HETATM 8548 O  O     . HOH G 4 .   ? 8.849   25.235  45.121  1 15.612  ? 808  HOH A O     1 
HETATM 8549 O  O     . HOH G 4 .   ? 1.845   29.812  60.882  1 25.882  ? 809  HOH A O     1 
HETATM 8550 O  O     . HOH G 4 .   ? 0.253   31.914  47.291  1 28.916  ? 810  HOH A O     1 
HETATM 8551 O  O     . HOH G 4 .   ? 34.753  11.262  40.766  1 26.242  ? 811  HOH A O     1 
HETATM 8552 O  O     . HOH G 4 .   ? 23.955  9.477   66.184  1 19.239  ? 812  HOH A O     1 
HETATM 8553 O  O     . HOH G 4 .   ? 12.192  14.747  29.454  1 18.329  ? 813  HOH A O     1 
HETATM 8554 O  O     . HOH G 4 .   ? 11.757  5.704   32.14   1 20.896  ? 814  HOH A O     1 
HETATM 8555 O  O     . HOH G 4 .   ? -3.266  9.492   53.493  1 20.386  ? 815  HOH A O     1 
HETATM 8556 O  O     . HOH G 4 .   ? 21.967  8.604   21.943  1 31.008  ? 816  HOH A O     1 
HETATM 8557 O  O     . HOH G 4 .   ? 5.1     -3.03   42.59   1 16.443  ? 817  HOH A O     1 
HETATM 8558 O  O     . HOH G 4 .   ? -12.587 1.943   61.219  1 25.865  ? 818  HOH A O     1 
HETATM 8559 O  O     . HOH G 4 .   ? -0.293  25.162  26.883  1 34.798  ? 819  HOH A O     1 
HETATM 8560 O  O     . HOH G 4 .   ? -5.951  4.698   64.225  1 21.404  ? 820  HOH A O     1 
HETATM 8561 O  O     . HOH G 4 .   ? 17.582  15.157  34.972  1 14.878  ? 821  HOH A O     1 
HETATM 8562 O  O     . HOH G 4 .   ? 10.699  20.433  40.505  1 14.706  ? 822  HOH A O     1 
HETATM 8563 O  O     . HOH G 4 .   ? -46.278 21.767  15.633  1 40.095  ? 823  HOH A O     1 
HETATM 8564 O  O     . HOH G 4 .   ? 9.539   14.484  26.651  1 15.503  ? 824  HOH A O     1 
HETATM 8565 O  O     . HOH G 4 .   ? 13.85   6.644   18.455  1 38.242  ? 825  HOH A O     1 
HETATM 8566 O  O     . HOH G 4 .   ? -9.936  27.177  40.695  1 18.011  ? 826  HOH A O     1 
HETATM 8567 O  O     . HOH G 4 .   ? -4.172  24.716  27.884  1 33.348  ? 827  HOH A O     1 
HETATM 8568 O  O     . HOH G 4 .   ? 6.462   6.952   28.291  1 16.283  ? 828  HOH A O     1 
HETATM 8569 O  O     . HOH G 4 .   ? -50.559 14.505  18.503  1 24.689  ? 829  HOH A O     1 
HETATM 8570 O  O     . HOH G 4 .   ? -19.996 5.303   56.424  1 20.363  ? 830  HOH A O     1 
HETATM 8571 O  O     . HOH G 4 .   ? 3.915   4.074   61.561  1 19.733  ? 831  HOH A O     1 
HETATM 8572 O  O     . HOH G 4 .   ? -6.005  27.716  39.147  1 33.617  ? 832  HOH A O     1 
HETATM 8573 O  O     . HOH G 4 .   ? 17.553  12.805  20.907  1 26.645  ? 833  HOH A O     1 
HETATM 8574 O  O     . HOH G 4 .   ? 6.313   6.407   64.248  1 29.63   ? 834  HOH A O     1 
HETATM 8575 O  O     . HOH G 4 .   ? 17.943  13.25   43.642  1 23.167  ? 835  HOH A O     1 
HETATM 8576 O  O     . HOH G 4 .   ? 10.697  -2.402  53.248  1 17.217  ? 836  HOH A O     1 
HETATM 8577 O  O     . HOH G 4 .   ? 4.612   14.609  69.724  1 24.855  ? 837  HOH A O     1 
HETATM 8578 O  O     . HOH G 4 .   ? -5.636  26.083  43.136  1 17.229  ? 838  HOH A O     1 
HETATM 8579 O  O     . HOH G 4 .   ? -14.973 -6.506  47.226  1 24.819  ? 839  HOH A O     1 
HETATM 8580 O  O     . HOH G 4 .   ? -17.817 -4.632  49.812  1 33.632  ? 840  HOH A O     1 
HETATM 8581 O  O     . HOH G 4 .   ? 25.379  21.132  66.482  1 39.048  ? 841  HOH A O     1 
HETATM 8582 O  O     . HOH G 4 .   ? -0.821  5.859   39.208  1 20.636  ? 842  HOH A O     1 
HETATM 8583 O  O     . HOH G 4 .   ? 8.913   16.743  73.239  1 48.618  ? 843  HOH A O     1 
HETATM 8584 O  O     . HOH G 4 .   ? -6.328  16.606  25.644  1 28.24   ? 844  HOH A O     1 
HETATM 8585 O  O     . HOH G 4 .   ? 30.797  26.051  53.552  1 39.515  ? 845  HOH A O     1 
HETATM 8586 O  O     . HOH G 4 .   ? -11.84  25.611  32.115  1 31.035  ? 846  HOH A O     1 
HETATM 8587 O  O     . HOH G 4 .   ? -1.913  31.739  48.932  1 23.651  ? 847  HOH A O     1 
HETATM 8588 O  O     . HOH G 4 .   ? 12.011  16.709  77.055  1 43.877  ? 848  HOH A O     1 
HETATM 8589 O  O     . HOH G 4 .   ? 12.568  -0.078  36.847  1 27.118  ? 849  HOH A O     1 
HETATM 8590 O  O     . HOH G 4 .   ? 0.505   17.419  52.285  1 27.116  ? 850  HOH A O     1 
HETATM 8591 O  O     . HOH G 4 .   ? -5.921  16.858  30.116  1 16.769  ? 851  HOH A O     1 
HETATM 8592 O  O     . HOH G 4 .   ? 13.495  11.639  21.042  1 19.507  ? 852  HOH A O     1 
HETATM 8593 O  O     . HOH G 4 .   ? 17.489  2.101   34.801  1 31.645  ? 853  HOH A O     1 
HETATM 8594 O  O     . HOH G 4 .   ? -17.432 14.657  52.738  1 38.693  ? 854  HOH A O     1 
HETATM 8595 O  O     . HOH G 4 .   ? -6.125  -18.188 42.753  1 43.506  ? 855  HOH A O     1 
HETATM 8596 O  O     . HOH G 4 .   ? 20.487  2.434   21.232  1 25.989  ? 856  HOH A O     1 
HETATM 8597 O  O     . HOH G 4 .   ? 11.825  14.188  43.743  1 17.427  ? 857  HOH A O     1 
HETATM 8598 O  O     . HOH G 4 .   ? -2.936  26.053  41.627  1 22.232  ? 858  HOH A O     1 
HETATM 8599 O  O     . HOH G 4 .   ? -19.799 -6.784  48.917  1 30.146  ? 859  HOH A O     1 
HETATM 8600 O  O     . HOH G 4 .   ? -4.554  27.726  53.438  1 20.292  ? 860  HOH A O     1 
HETATM 8601 O  O     . HOH G 4 .   ? -15.971 28.92   39.141  1 51.507  ? 861  HOH A O     1 
HETATM 8602 O  O     . HOH G 4 .   ? 17.366  24.484  69.548  1 28.71   ? 862  HOH A O     1 
HETATM 8603 O  O     . HOH G 4 .   ? 20.5    22.39   42.542  1 13.377  ? 863  HOH A O     1 
HETATM 8604 O  O     . HOH G 4 .   ? -28.263 21.422  26.569  1 20.669  ? 864  HOH A O     1 
HETATM 8605 O  O     . HOH G 4 .   ? -14.428 10.452  53.118  1 22.579  ? 865  HOH A O     1 
HETATM 8606 O  O     . HOH G 4 .   ? 2.899   13.013  62.569  1 14.267  ? 866  HOH A O     1 
HETATM 8607 O  O     . HOH G 4 .   ? 12.503  12.238  26.205  1 15.256  ? 867  HOH A O     1 
HETATM 8608 O  O     . HOH G 4 .   ? -16.537 3.358   62.08   1 27.601  ? 868  HOH A O     1 
HETATM 8609 O  O     . HOH G 4 .   ? 2.384   33.365  48.405  1 28.139  ? 869  HOH A O     1 
HETATM 8610 O  O     . HOH G 4 .   ? 27.502  -10.732 37.442  1 16.316  ? 870  HOH A O     1 
HETATM 8611 O  O     . HOH G 4 .   ? 18.015  18.532  45.564  1 13.143  ? 871  HOH A O     1 
HETATM 8612 O  O     . HOH G 4 .   ? -49.223 23.109  18.33   1 33.988  ? 872  HOH A O     1 
HETATM 8613 O  O     . HOH G 4 .   ? -3.164  11.793  51.082  1 17.994  ? 873  HOH A O     1 
HETATM 8614 O  O     . HOH G 4 .   ? 30.307  4.876   45.794  1 21.728  ? 874  HOH A O     1 
HETATM 8615 O  O     . HOH G 4 .   ? -11.306 -11.185 55.322  1 33.51   ? 875  HOH A O     1 
HETATM 8616 O  O     . HOH G 4 .   ? 28.827  22.442  48.954  1 26.956  ? 876  HOH A O     1 
HETATM 8617 O  O     . HOH G 4 .   ? 1.687   16.282  49.727  1 13.162  ? 877  HOH A O     1 
HETATM 8618 O  O     . HOH G 4 .   ? 6.232   11.551  56.795  1 14.159  ? 878  HOH A O     1 
HETATM 8619 O  O     . HOH G 4 .   ? -6.76   12.395  57.133  1 19.984  ? 879  HOH A O     1 
HETATM 8620 O  O     . HOH G 4 .   ? -19.385 14.216  47.599  1 16.788  ? 880  HOH A O     1 
HETATM 8621 O  O     . HOH G 4 .   ? -4.568  15.945  65.707  1 22.475  ? 881  HOH A O     1 
HETATM 8622 O  O     . HOH G 4 .   ? 18.226  22.709  40.923  1 21.994  ? 882  HOH A O     1 
HETATM 8623 O  O     . HOH G 4 .   ? 29.603  15.587  49.204  1 19.152  ? 883  HOH A O     1 
HETATM 8624 O  O     . HOH G 4 .   ? 23.376  0.716   66.713  1 27.015  ? 884  HOH A O     1 
HETATM 8625 O  O     . HOH G 4 .   ? 17.347  33.337  45.475  1 20.394  ? 885  HOH A O     1 
HETATM 8626 O  O     . HOH G 4 .   ? 2.152   3.878   63.589  1 18.648  ? 886  HOH A O     1 
HETATM 8627 O  O     . HOH G 4 .   ? 1.489   13.035  72.377  1 25.025  ? 887  HOH A O     1 
HETATM 8628 O  O     . HOH G 4 .   ? 5.909   15.452  23.81   1 18.982  ? 888  HOH A O     1 
HETATM 8629 O  O     . HOH G 4 .   ? -1.237  7.456   46.192  1 16.062  ? 889  HOH A O     1 
HETATM 8630 O  O     . HOH G 4 .   ? -16.707 7.825   62.468  1 26.594  ? 890  HOH A O     1 
HETATM 8631 O  O     . HOH G 4 .   ? 4.443   29.258  62.168  1 15.344  ? 891  HOH A O     1 
HETATM 8632 O  O     . HOH G 4 .   ? 2.394   1.772   31.732  1 21.474  ? 892  HOH A O     1 
HETATM 8633 O  O     . HOH G 4 .   ? 3.65    1.018   44.28   1 20.572  ? 893  HOH A O     1 
HETATM 8634 O  O     . HOH G 4 .   ? 24.195  15.063  75.633  1 34.952  ? 894  HOH A O     1 
HETATM 8635 O  O     . HOH G 4 .   ? 8.929   36.083  54.306  1 40.556  ? 895  HOH A O     1 
HETATM 8636 O  O     . HOH G 4 .   ? -0.97   29.188  32.213  1 31.467  ? 896  HOH A O     1 
HETATM 8637 O  O     . HOH G 4 .   ? -17.524 18.365  27.796  1 17.782  ? 897  HOH A O     1 
HETATM 8638 O  O     . HOH G 4 .   ? 26.218  11.704  63.984  1 24.031  ? 898  HOH A O     1 
HETATM 8639 O  O     . HOH G 4 .   ? 3.849   9.34    54.715  1 18.779  ? 899  HOH A O     1 
HETATM 8640 O  O     . HOH G 4 .   ? 27.255  0.588   58.219  1 24.871  ? 900  HOH A O     1 
HETATM 8641 O  O     . HOH G 4 .   ? -20.618 5.894   34.237  1 17.408  ? 901  HOH A O     1 
HETATM 8642 O  O     . HOH G 4 .   ? 14.472  13.264  35.15   1 17.392  ? 902  HOH A O     1 
HETATM 8643 O  O     . HOH G 4 .   ? 3.276   33.631  42.786  1 31.069  ? 903  HOH A O     1 
HETATM 8644 O  O     . HOH G 4 .   ? -18.929 10.545  46.653  1 18.527  ? 904  HOH A O     1 
HETATM 8645 O  O     . HOH G 4 .   ? -20.528 6.347   61.054  1 49.952  ? 905  HOH A O     1 
HETATM 8646 O  O     . HOH G 4 .   ? 0.154   26.389  30.17   1 23.805  ? 906  HOH A O     1 
HETATM 8647 O  O     . HOH G 4 .   ? -2.328  10.573  71.536  1 38.63   ? 907  HOH A O     1 
HETATM 8648 O  O     . HOH G 4 .   ? -16.526 17.381  35.433  1 20.648  ? 908  HOH A O     1 
HETATM 8649 O  O     . HOH G 4 .   ? -40.302 20.813  15.458  1 44.309  ? 909  HOH A O     1 
HETATM 8650 O  O     . HOH G 4 .   ? 7.11    19.436  17.574  1 26.916  ? 910  HOH A O     1 
HETATM 8651 O  O     . HOH G 4 .   ? 29.415  4.862   64.509  1 43.542  ? 911  HOH A O     1 
HETATM 8652 O  O     . HOH G 4 .   ? -22.143 1.524   38.216  1 25.739  ? 912  HOH A O     1 
HETATM 8653 O  O     . HOH G 4 .   ? -36.185 22.96   9.717   1 42.864  ? 913  HOH A O     1 
HETATM 8654 O  O     . HOH G 4 .   ? 18.745  18.481  18.017  1 38.039  ? 914  HOH A O     1 
HETATM 8655 O  O     . HOH G 4 .   ? 4.357   27.731  18.85   1 35.771  ? 915  HOH A O     1 
HETATM 8656 O  O     . HOH G 4 .   ? -14.65  4.321   32.618  1 14.843  ? 916  HOH A O     1 
HETATM 8657 O  O     . HOH G 4 .   ? -2.315  18.939  50.104  1 16.003  ? 917  HOH A O     1 
HETATM 8658 O  O     . HOH G 4 .   ? -1.389  35.807  57.143  1 28.533  ? 918  HOH A O     1 
HETATM 8659 O  O     . HOH G 4 .   ? 5.915   20.033  71.955  1 44.574  ? 919  HOH A O     1 
HETATM 8660 O  O     . HOH G 4 .   ? 6.746   5.023   38.978  1 16.903  ? 920  HOH A O     1 
HETATM 8661 O  O     . HOH G 4 .   ? 16.493  32.662  53.269  1 26.895  ? 921  HOH A O     1 
HETATM 8662 O  O     . HOH G 4 .   ? 17.147  28.022  34.314  1 30.625  ? 922  HOH A O     1 
HETATM 8663 O  O     . HOH G 4 .   ? -4.607  31      46.771  1 21.795  ? 923  HOH A O     1 
HETATM 8664 O  O     . HOH G 4 .   ? -19.08  -7.289  52.956  1 41.976  ? 924  HOH A O     1 
HETATM 8665 O  O     . HOH G 4 .   ? 10.867  26.527  19.692  1 38.591  ? 925  HOH A O     1 
HETATM 8666 O  O     . HOH G 4 .   ? -10.066 2.463   61.822  1 32.368  ? 926  HOH A O     1 
HETATM 8667 O  O     . HOH G 4 .   ? 11.35   12.089  19.563  1 21.844  ? 927  HOH A O     1 
HETATM 8668 O  O     . HOH G 4 .   ? 9.528   1.731   26.996  1 23.669  ? 928  HOH A O     1 
HETATM 8669 O  O     . HOH G 4 .   ? 6.544   10.126  53.386  1 17.081  ? 929  HOH A O     1 
HETATM 8670 O  O     . HOH G 4 .   ? 13.735  -0.026  41.763  1 31.17   ? 930  HOH A O     1 
HETATM 8671 O  O     . HOH G 4 .   ? 13.149  32.966  44.217  1 22.471  ? 931  HOH A O     1 
HETATM 8672 O  O     . HOH G 4 .   ? 14.714  12.921  27.482  1 18.734  ? 932  HOH A O     1 
HETATM 8673 O  O     . HOH G 4 .   ? -4.676  11.432  55.653  1 20.72   ? 933  HOH A O     1 
HETATM 8674 O  O     . HOH G 4 .   ? -12.692 -1.092  31.789  1 30.782  ? 934  HOH A O     1 
HETATM 8675 O  O     . HOH G 4 .   ? 6.302   13.44   58.904  1 14.845  ? 935  HOH A O     1 
HETATM 8676 O  O     . HOH G 4 .   ? 5.133   13.521  52.068  1 15.129  ? 936  HOH A O     1 
HETATM 8677 O  O     . HOH G 4 .   ? 22.759  30.28   61.188  1 24.084  ? 937  HOH A O     1 
HETATM 8678 O  O     . HOH G 4 .   ? -19.109 7.979   38.026  1 15.305  ? 938  HOH A O     1 
HETATM 8679 O  O     . HOH G 4 .   ? -5.02   -2.405  62.183  1 20.761  ? 939  HOH A O     1 
HETATM 8680 O  O     . HOH G 4 .   ? 14.264  19.15   16.328  1 35.484  ? 940  HOH A O     1 
HETATM 8681 O  O     . HOH G 4 .   ? -3.934  18.284  58.754  1 34.002  ? 941  HOH A O     1 
HETATM 8682 O  O     . HOH G 4 .   ? 34.772  19.424  38.645  1 34.451  ? 942  HOH A O     1 
HETATM 8683 O  O     . HOH G 4 .   ? -8.756  9.178   67.265  1 33.566  ? 943  HOH A O     1 
HETATM 8684 O  O     . HOH G 4 .   ? 17.927  9.41    31.763  1 33.696  ? 944  HOH A O     1 
HETATM 8685 O  O     . HOH G 4 .   ? 19.166  29.999  44.43   1 31.269  ? 945  HOH A O     1 
HETATM 8686 O  O     . HOH G 4 .   ? 16.417  21.842  37.825  1 21.613  ? 946  HOH A O     1 
HETATM 8687 O  O     . HOH G 4 .   ? 11.492  4.521   71.751  1 24.164  ? 947  HOH A O     1 
HETATM 8688 O  O     . HOH G 4 .   ? 3.389   32.367  36.049  1 28.569  ? 948  HOH A O     1 
HETATM 8689 O  O     . HOH G 4 .   ? 10.654  7.192   34.064  1 12.917  ? 949  HOH A O     1 
HETATM 8690 O  O     . HOH G 4 .   ? 32.383  3.207   45.797  1 21.665  ? 950  HOH A O     1 
HETATM 8691 O  O     . HOH G 4 .   ? -5.536  24.918  49.933  1 15.383  ? 951  HOH A O     1 
HETATM 8692 O  O     . HOH G 4 .   ? 22.004  9.539   39.956  1 15.275  ? 952  HOH A O     1 
HETATM 8693 O  O     . HOH G 4 .   ? -4.453  21.232  52.055  1 21.203  ? 953  HOH A O     1 
HETATM 8694 O  O     . HOH G 4 .   ? -21.144 20.262  48.645  1 29.957  ? 954  HOH A O     1 
HETATM 8695 O  O     . HOH G 4 .   ? -44.195 17.666  23.602  1 30.601  ? 955  HOH A O     1 
HETATM 8696 O  O     . HOH G 4 .   ? 29.493  18.649  28.937  1 39.354  ? 956  HOH A O     1 
HETATM 8697 O  O     . HOH G 4 .   ? -21.18  9.388   57.095  1 32.575  ? 957  HOH A O     1 
HETATM 8698 O  O     . HOH G 4 .   ? -4.237  -16.19  45.824  1 36.212  ? 958  HOH A O     1 
HETATM 8699 O  O     . HOH G 4 .   ? -0.566  23.233  30.595  1 23.629  ? 959  HOH A O     1 
HETATM 8700 O  O     . HOH G 4 .   ? 1.804   32.608  60.206  1 25.156  ? 960  HOH A O     1 
HETATM 8701 O  O     . HOH G 4 .   ? 18.228  7.965   70.422  1 27.353  ? 961  HOH A O     1 
HETATM 8702 O  O     . HOH G 4 .   ? 6.225   1.039   43.031  1 18.686  ? 962  HOH A O     1 
HETATM 8703 O  O     . HOH G 4 .   ? -20.535 23.515  23.977  1 26.834  ? 963  HOH A O     1 
HETATM 8704 O  O     . HOH G 4 .   ? 6.934   34.747  51.774  1 26.438  ? 964  HOH A O     1 
HETATM 8705 O  O     . HOH G 4 .   ? 11.684  0.823   69.487  1 28.768  ? 965  HOH A O     1 
HETATM 8706 O  O     . HOH G 4 .   ? 35.725  21.593  34.483  1 46.748  ? 966  HOH A O     1 
HETATM 8707 O  O     . HOH G 4 .   ? 7.298   27.641  45.238  1 16.643  ? 967  HOH A O     1 
HETATM 8708 O  O     . HOH G 4 .   ? 7.142   24.287  66.056  1 36.104  ? 968  HOH A O     1 
HETATM 8709 O  O     . HOH G 4 .   ? 9.755   20.436  44.008  1 17.282  ? 969  HOH A O     1 
HETATM 8710 O  O     . HOH G 4 .   ? 29.295  21.857  43.878  1 16.662  ? 970  HOH A O     1 
HETATM 8711 O  O     . HOH G 4 .   ? -6.554  24.005  29.552  1 28.87   ? 971  HOH A O     1 
HETATM 8712 O  O     . HOH G 4 .   ? 27.081  10.765  59.102  1 23.9    ? 972  HOH A O     1 
HETATM 8713 O  O     . HOH G 4 .   ? 31.442  15.678  46.121  1 39.733  ? 973  HOH A O     1 
HETATM 8714 O  O     . HOH G 4 .   ? -24.375 27.55   28.531  1 23.562  ? 974  HOH A O     1 
HETATM 8715 O  O     . HOH G 4 .   ? 30.184  10.185  45.262  1 27.161  ? 975  HOH A O     1 
HETATM 8716 O  O     . HOH G 4 .   ? 38.064  13.797  40.053  1 39.028  ? 976  HOH A O     1 
HETATM 8717 O  O     . HOH G 4 .   ? 1.414   16.521  54.753  1 11.446  ? 977  HOH A O     1 
HETATM 8718 O  O     . HOH G 4 .   ? -10     26.112  35.891  1 23.258  ? 978  HOH A O     1 
HETATM 8719 O  O     . HOH G 4 .   ? 22.757  19.488  49.904  1 20.246  ? 979  HOH A O     1 
HETATM 8720 O  O     . HOH G 4 .   ? -7.784  -13.381 49.361  1 26.851  ? 980  HOH A O     1 
HETATM 8721 O  O     . HOH G 4 .   ? 6.473   31.034  36.175  1 29.681  ? 981  HOH A O     1 
HETATM 8722 O  O     . HOH G 4 .   ? 19.879  21.562  33.439  1 23.278  ? 982  HOH A O     1 
HETATM 8723 O  O     . HOH G 4 .   ? -2.466  18.697  26.591  1 25.539  ? 983  HOH A O     1 
HETATM 8724 O  O     . HOH G 4 .   ? 27.423  15.027  27.011  1 33.512  ? 984  HOH A O     1 
HETATM 8725 O  O     . HOH G 4 .   ? 25.981  17.805  64.098  1 29.696  ? 985  HOH A O     1 
HETATM 8726 O  O     . HOH G 4 .   ? -21.798 3.895   43.366  1 38.641  ? 986  HOH A O     1 
HETATM 8727 O  O     . HOH G 4 .   ? 15.939  33.077  59.348  1 37.192  ? 987  HOH A O     1 
HETATM 8728 O  O     . HOH G 4 .   ? 3.038   3.842   44.217  1 18.534  ? 988  HOH A O     1 
HETATM 8729 O  O     . HOH G 4 .   ? 14.455  15.679  36.371  1 17.276  ? 989  HOH A O     1 
HETATM 8730 O  O     . HOH G 4 .   ? -12.452 -7.064  47.962  1 17.055  ? 990  HOH A O     1 
HETATM 8731 O  O     . HOH G 4 .   ? -34.938 20.903  17.371  1 29.977  ? 991  HOH A O     1 
HETATM 8732 O  O     . HOH G 4 .   ? 35.556  1.189   48.17   1 40.562  ? 992  HOH A O     1 
HETATM 8733 O  O     . HOH G 4 .   ? 3.218   5.844   65.147  1 22.149  ? 993  HOH A O     1 
HETATM 8734 O  O     . HOH G 4 .   ? -13.081 28.549  46.39   1 20.243  ? 994  HOH A O     1 
HETATM 8735 O  O     . HOH G 4 .   ? 25.187  22.812  61.607  1 43.248  ? 995  HOH A O     1 
HETATM 8736 O  O     . HOH G 4 .   ? -33.616 22.366  19.209  1 36.038  ? 996  HOH A O     1 
HETATM 8737 O  O     . HOH G 4 .   ? 22.536  16.927  50.809  1 16.914  ? 997  HOH A O     1 
HETATM 8738 O  O     . HOH G 4 .   ? -0.002  7.304   32.322  1 21.035  ? 998  HOH A O     1 
HETATM 8739 O  O     . HOH G 4 .   ? 24.864  23.357  58.978  1 25.63   ? 999  HOH A O     1 
HETATM 8740 O  O     . HOH G 4 .   ? 8.047   16.468  25.51   1 18.861  ? 1000 HOH A O     1 
HETATM 8741 O  O     . HOH G 4 .   ? 27.81   23.225  40.551  1 17.642  ? 1001 HOH A O     1 
HETATM 8742 O  O     . HOH G 4 .   ? -3.246  18.328  65.597  1 22.926  ? 1002 HOH A O     1 
HETATM 8743 O  O     . HOH G 4 .   ? -13.711 13.322  51.451  1 18.312  ? 1003 HOH A O     1 
HETATM 8744 O  O     . HOH G 4 .   ? -17.216 13.956  40.245  1 22.109  ? 1004 HOH A O     1 
HETATM 8745 O  O     . HOH G 4 .   ? -3.067  25.321  53.027  1 15.845  ? 1005 HOH A O     1 
HETATM 8746 O  O     . HOH G 4 .   ? 25.264  9.494   23.641  1 34.34   ? 1006 HOH A O     1 
HETATM 8747 O  O     . HOH G 4 .   ? 31.702  17.232  43.996  1 21.865  ? 1007 HOH A O     1 
HETATM 8748 O  O     . HOH G 4 .   ? 33.947  16.61   42.218  1 23.51   ? 1008 HOH A O     1 
HETATM 8749 O  O     . HOH G 4 .   ? -37.243 26.787  14.673  1 40.324  ? 1009 HOH A O     1 
HETATM 8750 O  O     . HOH G 4 .   ? -15.89  25.85   45.948  1 17.732  ? 1010 HOH A O     1 
HETATM 8751 O  O     . HOH G 4 .   ? 12.168  31.045  40.602  1 17.345  ? 1011 HOH A O     1 
HETATM 8752 O  O     . HOH G 4 .   ? -2.581  18.071  54.547  1 23.315  ? 1012 HOH A O     1 
HETATM 8753 O  O     . HOH G 4 .   ? -4.709  0.131   28.221  1 11.874  ? 1013 HOH A O     1 
HETATM 8754 O  O     . HOH G 4 .   ? 34.19   7.393   44.98   1 39.907  ? 1014 HOH A O     1 
HETATM 8755 O  O     . HOH G 4 .   ? 2.465   26.464  27.423  1 29.55   ? 1015 HOH A O     1 
HETATM 8756 O  O     . HOH G 4 .   ? 15.854  5.959   74.026  1 37.374  ? 1016 HOH A O     1 
HETATM 8757 O  O     . HOH G 4 .   ? 19.359  -11.498 47.258  1 42.378  ? 1017 HOH A O     1 
HETATM 8758 O  O     . HOH G 4 .   ? -25.668 28.414  26.16   1 24.55   ? 1018 HOH A O     1 
HETATM 8759 O  O     . HOH G 4 .   ? 32.29   7.934   33.01   1 29.368  ? 1019 HOH A O     1 
HETATM 8760 O  O     . HOH G 4 .   ? 15.187  19.046  47.564  1 15.57   ? 1020 HOH A O     1 
HETATM 8761 O  O     . HOH G 4 .   ? -1.736  21.212  26.526  1 20.452  ? 1021 HOH A O     1 
HETATM 8762 O  O     . HOH G 4 .   ? 7.358   32.842  40.473  1 43.2    ? 1022 HOH A O     1 
HETATM 8763 O  O     . HOH G 4 .   ? -25.031 16.758  42.296  1 54.514  ? 1023 HOH A O     1 
HETATM 8764 O  O     . HOH G 4 .   ? 18.322  19.625  69.286  1 29.159  ? 1024 HOH A O     1 
HETATM 8765 O  O     . HOH G 4 .   ? 20.292  26.675  28.614  1 32.941  ? 1025 HOH A O     1 
HETATM 8766 O  O     . HOH G 4 .   ? 1.999   15.087  69.874  1 24.324  ? 1026 HOH A O     1 
HETATM 8767 O  O     . HOH G 4 .   ? 37.66   0.866   41.968  1 36.362  ? 1027 HOH A O     1 
HETATM 8768 O  O     . HOH G 4 .   ? 24.515  12.629  23.634  1 29.968  ? 1028 HOH A O     1 
HETATM 8769 O  O     . HOH G 4 .   ? -12.73  19.811  29.425  1 24.244  ? 1029 HOH A O     1 
HETATM 8770 O  O     . HOH G 4 .   ? 35.891  14.907  43.099  1 27.035  ? 1030 HOH A O     1 
HETATM 8771 O  O     . HOH G 4 .   ? 21.32   16.219  78.066  1 29.58   ? 1031 HOH A O     1 
HETATM 8772 O  O     . HOH G 4 .   ? 8.932   30.971  65.116  1 31.155  ? 1032 HOH A O     1 
HETATM 8773 O  O     . HOH G 4 .   ? 4.87    25.625  65.767  1 37.921  ? 1033 HOH A O     1 
HETATM 8774 O  O     . HOH G 4 .   ? -28.48  29.453  27.903  1 44.433  ? 1034 HOH A O     1 
HETATM 8775 O  O     . HOH G 4 .   ? -2.764  21.644  55.117  1 31.468  ? 1035 HOH A O     1 
HETATM 8776 O  O     . HOH G 4 .   ? -17.193 24.192  32.696  1 43.903  ? 1036 HOH A O     1 
HETATM 8777 O  O     . HOH G 4 .   ? -11.355 31.777  42.572  1 36.344  ? 1037 HOH A O     1 
HETATM 8778 O  O     . HOH G 4 .   ? 4.386   2.789   71.22   1 23.856  ? 1038 HOH A O     1 
HETATM 8779 O  O     . HOH G 4 .   ? -1.389  32.354  40.544  1 45.464  ? 1039 HOH A O     1 
HETATM 8780 O  O     . HOH G 4 .   ? -20.78  3.867   36.32   1 22.946  ? 1040 HOH A O     1 
HETATM 8781 O  O     . HOH G 4 .   ? -19.767 14.818  40.337  1 42.842  ? 1041 HOH A O     1 
HETATM 8782 O  O     . HOH G 4 .   ? 8.778   6.801   31.593  1 19.214  ? 1042 HOH A O     1 
HETATM 8783 O  O     . HOH G 4 .   ? 1.564   36.243  58.055  1 37.501  ? 1043 HOH A O     1 
HETATM 8784 O  O     . HOH G 4 .   ? 36.405  17.335  34.067  1 31.092  ? 1044 HOH A O     1 
HETATM 8785 O  O     . HOH G 4 .   ? -47.52  14.076  20.88   1 29.511  ? 1045 HOH A O     1 
HETATM 8786 O  O     . HOH G 4 .   ? 16.792  26.28   25.59   1 35.568  ? 1046 HOH A O     1 
HETATM 8787 O  O     . HOH G 4 .   ? -1.569  -15.774 46      1 50.911  ? 1047 HOH A O     1 
HETATM 8788 O  O     . HOH G 4 .   ? -22.681 5.843   50.575  1 25.625  ? 1048 HOH A O     1 
HETATM 8789 O  O     . HOH G 4 .   ? 35.191  5.817   52.191  1 46.835  ? 1049 HOH A O     1 
HETATM 8790 O  O     . HOH G 4 .   ? 6.996   -0.413  70.918  1 47.237  ? 1050 HOH A O     1 
HETATM 8791 O  O     . HOH G 4 .   ? 7.974   17.397  13.731  1 44.8    ? 1051 HOH A O     1 
HETATM 8792 O  O     . HOH G 4 .   ? 32.927  10.952  45.911  1 35.161  ? 1052 HOH A O     1 
HETATM 8793 O  O     . HOH G 4 .   ? 25.519  19.961  62.536  1 37.789  ? 1053 HOH A O     1 
HETATM 8794 O  O     . HOH G 4 .   ? -13.303 21.62   27.513  1 54.461  ? 1054 HOH A O     1 
HETATM 8795 O  O     . HOH G 4 .   ? 37.233  -4.987  42.974  1 32.525  ? 1055 HOH A O     1 
HETATM 8796 O  O     . HOH G 4 .   ? -20.878 -10.072 50.800  1 29.969  ? 1056 HOH A O     1 
HETATM 8797 O  O     . HOH G 4 .   ? -0.790  -19.075 49.403  1 45.305  ? 1057 HOH A O     1 
HETATM 8798 O  O     . HOH G 4 .   ? 15.842  22.377  70.384  1 35.899  ? 1058 HOH A O     1 
HETATM 8799 O  O     . HOH G 4 .   ? 26.816  18.831  66.853  1 32.649  ? 1059 HOH A O     1 
HETATM 8800 O  O     . HOH G 4 .   ? -25.491 12.595  46.47   1 57.94   ? 1060 HOH A O     1 
HETATM 8801 O  O     . HOH G 4 .   ? 24.065  -9.932  40.059  1 31.997  ? 1061 HOH A O     1 
HETATM 8802 O  O     . HOH G 4 .   ? -20.597 27.795  21.148  1 33.253  ? 1062 HOH A O     1 
HETATM 8803 O  O     . HOH G 4 .   ? 3.416   21.846  67.049  1 37.453  ? 1063 HOH A O     1 
HETATM 8804 O  O     . HOH G 4 .   ? -32.528 21.293  27.292  1 46.566  ? 1064 HOH A O     1 
HETATM 8805 O  O     . HOH G 4 .   ? 5.075   10.021  51.198  1 15.056  ? 1065 HOH A O     1 
HETATM 8806 O  O     . HOH G 4 .   ? 8.862   25.153  67.909  1 44.028  ? 1066 HOH A O     1 
HETATM 8807 O  O     . HOH G 4 .   ? 14.102  16.949  75.253  1 43.758  ? 1067 HOH A O     1 
HETATM 8808 O  O     . HOH G 4 .   ? -33.175 24.886  9.553   1 47.398  ? 1068 HOH A O     1 
HETATM 8809 O  O     . HOH G 4 .   ? -4.989  18.121  27.936  1 20.843  ? 1069 HOH A O     1 
HETATM 8810 O  O     . HOH G 4 .   ? -14.547 14.972  55.963  1 34.324  ? 1070 HOH A O     1 
HETATM 8811 O  O     . HOH G 4 .   ? 11.698  25.288  22.623  1 30.561  ? 1071 HOH A O     1 
HETATM 8812 O  O     . HOH G 4 .   ? -12.786 -9.329  49.717  1 33.995  ? 1072 HOH A O     1 
HETATM 8813 O  O     . HOH G 4 .   ? 18.818  8.74    29.333  1 20.246  ? 1073 HOH A O     1 
HETATM 8814 O  O     . HOH G 4 .   ? 23.438  0.28    28.437  1 52.709  ? 1074 HOH A O     1 
HETATM 8815 O  O     . HOH G 4 .   ? -5.038  23.694  52.139  1 24.572  ? 1075 HOH A O     1 
HETATM 8816 O  O     . HOH G 4 .   ? -19.107 -8.563  47.028  1 25.477  ? 1076 HOH A O     1 
HETATM 8817 O  O     . HOH G 4 .   ? -18.496 19.057  36.047  1 47.32   ? 1077 HOH A O     1 
HETATM 8818 O  O     . HOH G 4 .   ? 29.051  9.224   60.833  1 31.295  ? 1078 HOH A O     1 
HETATM 8819 O  O     . HOH G 4 .   ? -5.854  16.621  56.816  1 26.196  ? 1079 HOH A O     1 
HETATM 8820 O  O     . HOH G 4 .   ? 3.23    11.752  54.238  1 35.323  ? 1080 HOH A O     1 
HETATM 8821 O  O     . HOH G 4 .   ? 24.98   28.047  55.599  1 31.75   ? 1081 HOH A O     1 
HETATM 8822 O  O     . HOH G 4 .   ? 21.106  7.557   70.59   1 30.57   ? 1082 HOH A O     1 
HETATM 8823 O  O     . HOH G 4 .   ? 35.725  5.419   43.598  1 46.09   ? 1083 HOH A O     1 
HETATM 8824 O  O     . HOH G 4 .   ? 12.483  31.379  61.988  1 34.383  ? 1084 HOH A O     1 
HETATM 8825 O  O     . HOH G 4 .   ? 24.373  30.324  56.75   1 33.151  ? 1085 HOH A O     1 
HETATM 8826 O  O     . HOH G 4 .   ? 29.747  18.163  67.645  1 44.447  ? 1086 HOH A O     1 
HETATM 8827 O  O     . HOH G 4 .   ? 38.477  -0.711  35.433  1 41.814  ? 1087 HOH A O     1 
HETATM 8828 O  O     . HOH G 4 .   ? 5.401   16.754  71.952  1 32.483  ? 1088 HOH A O     1 
HETATM 8829 O  O     . HOH G 4 .   ? -21.8   -3.168  46.287  1 30.434  ? 1089 HOH A O     1 
HETATM 8830 O  O     . HOH G 4 .   ? 10.179  35.3    50.056  1 40.028  ? 1090 HOH A O     1 
HETATM 8831 O  O     . HOH G 4 .   ? 33.327  8.305   47.352  1 47.65   ? 1091 HOH A O     1 
HETATM 8832 O  O     . HOH G 4 .   ? -1.869  35.742  48.699  1 19.805  ? 1092 HOH A O     1 
HETATM 8833 O  O     . HOH G 4 .   ? 29.984  22.626  46.361  1 28.915  ? 1093 HOH A O     1 
HETATM 8834 O  O     . HOH G 4 .   ? 29.952  23.796  42.045  1 31.574  ? 1094 HOH A O     1 
HETATM 8835 O  O     . HOH G 4 .   ? 24.4    2.514   27.436  1 45.181  ? 1095 HOH A O     1 
HETATM 8836 O  O     . HOH G 4 .   ? 3.012   29.088  64.539  1 39.708  ? 1096 HOH A O     1 
HETATM 8837 O  O     . HOH G 4 .   ? -17.695 -10.028 54.199  1 33.142  ? 1097 HOH A O     1 
HETATM 8838 O  O     . HOH G 4 .   ? 6.243   5.96    71.617  1 36.533  ? 1098 HOH A O     1 
HETATM 8839 O  O     . HOH G 4 .   ? -16.649 -2.972  53.986  1 34.653  ? 1099 HOH A O     1 
HETATM 8840 O  O     . HOH G 4 .   ? 2.248   14.191  53.683  1 19.994  ? 1100 HOH A O     1 
HETATM 8841 O  O     . HOH G 4 .   ? -5.21   24.007  25.302  1 49.185  ? 1101 HOH A O     1 
HETATM 8842 O  O     . HOH G 4 .   ? -16.779 17.638  40.174  1 32.748  ? 1102 HOH A O     1 
HETATM 8843 O  O     . HOH G 4 .   ? -7.247  15.793  66.123  1 29.996  ? 1103 HOH A O     1 
HETATM 8844 O  O     . HOH G 4 .   ? -9.637  27.032  32.902  1 49.988  ? 1104 HOH A O     1 
HETATM 8845 O  O     . HOH G 4 .   ? -5.231  18.717  51.871  1 21.477  ? 1105 HOH A O     1 
HETATM 8846 O  O     . HOH G 4 .   ? -4.618  25.073  57.13   1 25.811  ? 1106 HOH A O     1 
HETATM 8847 O  O     . HOH G 4 .   ? -18.76  -5.047  35.859  1 24.586  ? 1107 HOH A O     1 
HETATM 8848 O  O     . HOH G 4 .   ? 7.127   37.077  58.639  1 39.839  ? 1108 HOH A O     1 
HETATM 8849 O  O     . HOH G 4 .   ? -20.309 9.232   59.946  1 42.798  ? 1109 HOH A O     1 
HETATM 8850 O  O     . HOH G 4 .   ? 15.114  34.463  45.192  1 22.565  ? 1110 HOH A O     1 
HETATM 8851 O  O     . HOH G 4 .   ? -16.061 24.427  50.731  1 41.043  ? 1111 HOH A O     1 
HETATM 8852 O  O     . HOH G 4 .   ? -46.794 23.188  13.424  1 44.382  ? 1112 HOH A O     1 
HETATM 8853 O  O     . HOH G 4 .   ? -22.091 22.033  50.384  1 42.437  ? 1113 HOH A O     1 
HETATM 8854 O  O     . HOH G 4 .   ? -20.988 -0.574  50.189  1 24.126  ? 1114 HOH A O     1 
HETATM 8855 O  O     . HOH G 4 .   ? 11.125  17.968  74.978  1 40.656  ? 1115 HOH A O     1 
HETATM 8856 O  O     . HOH G 4 .   ? 25.97   31.041  61.362  1 40.755  ? 1116 HOH A O     1 
HETATM 8857 O  O     . HOH G 4 .   ? 37.672  3.532   43.405  1 39.395  ? 1117 HOH A O     1 
HETATM 8858 O  O     . HOH G 4 .   ? 30.894  6.811   36.665  1 38.55   ? 1118 HOH A O     1 
HETATM 8859 O  O     . HOH G 4 .   ? -21.808 3.359   50.98   1 40.093  ? 1119 HOH A O     1 
HETATM 8860 O  O     . HOH G 4 .   ? 16.179  19.576  18.784  1 42.125  ? 1120 HOH A O     1 
HETATM 8861 O  O     . HOH G 4 .   ? -5.564  28.254  33.19   1 40.489  ? 1121 HOH A O     1 
HETATM 8862 O  O     . HOH G 4 .   ? 26.899  12.821  60.804  1 30.562  ? 1122 HOH A O     1 
HETATM 8863 O  O     . HOH G 4 .   ? -7.731  14.788  56.182  1 29.087  ? 1123 HOH A O     1 
HETATM 8864 O  O     . HOH G 4 .   ? -5.018  30.201  39.665  1 29.97   ? 1124 HOH A O     1 
HETATM 8865 O  O     . HOH G 4 .   ? 1.982   37.366  50.821  1 27.595  ? 1125 HOH A O     1 
HETATM 8866 O  O     . HOH G 4 .   ? -25.089 5.496   49.351  1 43.512  ? 1126 HOH A O     1 
HETATM 8867 O  O     . HOH G 4 .   ? -5.595  30.93   37.166  1 41.298  ? 1127 HOH A O     1 
HETATM 8868 O  O     . HOH G 4 .   ? -3.83   29.931  32.206  1 44.592  ? 1128 HOH A O     1 
HETATM 8869 O  O     . HOH G 4 .   ? 6.422   26.454  70.558  1 50.466  ? 1129 HOH A O     1 
HETATM 8870 O  O     . HOH G 4 .   ? -3.771  15.156  68.163  1 31.231  ? 1130 HOH A O     1 
HETATM 8871 O  O     . HOH G 4 .   ? 3.881   33.696  61.611  1 33.333  ? 1131 HOH A O     1 
HETATM 8872 O  O     . HOH G 4 .   ? 22.027  0.34    34.212  1 50.553  ? 1132 HOH A O     1 
HETATM 8873 O  O     . HOH G 4 .   ? 17.226  -0.342  35.942  1 45.09   ? 1133 HOH A O     1 
HETATM 8874 O  O     . HOH G 4 .   ? -2.767  18.551  68.205  1 38.428  ? 1134 HOH A O     1 
HETATM 8875 O  O     . HOH G 4 .   ? 1.335   17.668  70.254  1 37.43   ? 1135 HOH A O     1 
HETATM 8876 O  O     . HOH G 4 .   ? -20.564 -1.438  52.811  1 51.063  ? 1136 HOH A O     1 
HETATM 8877 O  O     . HOH G 4 .   ? -49.711 8.465   10.147  1 35.061  ? 1137 HOH A O     1 
HETATM 8878 O  O     . HOH H 4 .   ? -0.913  19.363  10.386  1 30.015  ? 701  HOH B O     1 
HETATM 8879 O  O     . HOH H 4 .   ? -15.391 18.838  -3.904  1 24.214  ? 702  HOH B O     1 
HETATM 8880 O  O     . HOH H 4 .   ? -22.056 -4.456  -17.641 1 23.912  ? 703  HOH B O     1 
HETATM 8881 O  O     . HOH H 4 .   ? 9.686   10.586  17.952  1 22.329  ? 704  HOH B O     1 
HETATM 8882 O  O     . HOH H 4 .   ? -24.705 10.347  26.543  1 24.277  ? 705  HOH B O     1 
HETATM 8883 O  O     . HOH H 4 .   ? -27.712 5.277   -18.216 1 26.903  ? 706  HOH B O     1 
HETATM 8884 O  O     . HOH H 4 .   ? -11.853 1.987   -6.956  1 17.428  ? 707  HOH B O     1 
HETATM 8885 O  O     . HOH H 4 .   ? -36.177 2.032   17.307  1 12.864  ? 708  HOH B O     1 
HETATM 8886 O  O     . HOH H 4 .   ? -15.712 -3.068  20.891  1 28.961  ? 709  HOH B O     1 
HETATM 8887 O  O     . HOH H 4 .   ? -23.604 -6.333  15.739  1 33.459  ? 710  HOH B O     1 
HETATM 8888 O  O     . HOH H 4 .   ? -19.171 27.806  16.495  1 23.336  ? 711  HOH B O     1 
HETATM 8889 O  O     . HOH H 4 .   ? -22.462 -8.571  21.987  1 29.982  ? 712  HOH B O     1 
HETATM 8890 O  O     . HOH H 4 .   ? -21.145 25.176  11.594  1 21.496  ? 713  HOH B O     1 
HETATM 8891 O  O     . HOH H 4 .   ? -16.738 16.948  23.332  1 19.083  ? 714  HOH B O     1 
HETATM 8892 O  O     . HOH H 4 .   ? -43.966 -3.483  6.741   1 27.392  ? 715  HOH B O     1 
HETATM 8893 O  O     . HOH H 4 .   ? -8.387  -7.611  26.148  1 52.704  ? 716  HOH B O     1 
HETATM 8894 O  O     . HOH H 4 .   ? -3.02   -6.736  11.747  1 18.973  ? 717  HOH B O     1 
HETATM 8895 O  O     . HOH H 4 .   ? -40.08  -0.942  23.488  1 31.404  ? 718  HOH B O     1 
HETATM 8896 O  O     . HOH H 4 .   ? -16.868 -9.8    17.413  1 51.275  ? 719  HOH B O     1 
HETATM 8897 O  O     . HOH H 4 .   ? -15.915 11.149  28.568  1 13.597  ? 720  HOH B O     1 
HETATM 8898 O  O     . HOH H 4 .   ? -21.118 -8.017  45.100  1 22.166  ? 721  HOH B O     1 
HETATM 8899 O  O     . HOH H 4 .   ? -16.506 -8.747  46.42   1 19.99   ? 722  HOH B O     1 
HETATM 8900 O  O     . HOH H 4 .   ? -32.835 14.101  14.741  1 18.969  ? 723  HOH B O     1 
HETATM 8901 O  O     . HOH H 4 .   ? -10.569 11.923  -10.032 1 29.151  ? 724  HOH B O     1 
HETATM 8902 O  O     . HOH H 4 .   ? -19.817 3.657   25.642  1 14.672  ? 725  HOH B O     1 
HETATM 8903 O  O     . HOH H 4 .   ? -29.572 7.9     4.618   1 15.682  ? 726  HOH B O     1 
HETATM 8904 O  O     . HOH H 4 .   ? -18.163 5.281   -8.798  1 22.406  ? 727  HOH B O     1 
HETATM 8905 O  O     . HOH H 4 .   ? -15.446 -2.287  -18.284 1 47.665  ? 728  HOH B O     1 
HETATM 8906 O  O     . HOH H 4 .   ? 8.269   4.225   12.968  1 35.947  ? 729  HOH B O     1 
HETATM 8907 O  O     . HOH H 4 .   ? -2.06   -11.308 5.456   1 23.467  ? 730  HOH B O     1 
HETATM 8908 O  O     . HOH H 4 .   ? -34.603 -4.587  20.21   1 29.438  ? 731  HOH B O     1 
HETATM 8909 O  O     . HOH H 4 .   ? -28.185 20.572  23.965  1 19.258  ? 732  HOH B O     1 
HETATM 8910 O  O     . HOH H 4 .   ? -29.206 18.934  30.558  1 22.991  ? 733  HOH B O     1 
HETATM 8911 O  O     . HOH H 4 .   ? -29.468 7.905   26.469  1 19.485  ? 734  HOH B O     1 
HETATM 8912 O  O     . HOH H 4 .   ? -9.807  7.738   0.433   1 19.623  ? 735  HOH B O     1 
HETATM 8913 O  O     . HOH H 4 .   ? -30.434 6.084   24.461  1 14.77   ? 736  HOH B O     1 
HETATM 8914 O  O     . HOH H 4 .   ? -34.83  -13.499 -1.196  1 32.393  ? 737  HOH B O     1 
HETATM 8915 O  O     . HOH H 4 .   ? -29.509 -1.772  -22.553 1 33.413  ? 738  HOH B O     1 
HETATM 8916 O  O     . HOH H 4 .   ? -10.781 -0.594  18.054  1 22.869  ? 739  HOH B O     1 
HETATM 8917 O  O     . HOH H 4 .   ? -34.697 -11.959 -10.598 1 33.643  ? 740  HOH B O     1 
HETATM 8918 O  O     . HOH H 4 .   ? -14.88  9.844   23.136  1 17.651  ? 741  HOH B O     1 
HETATM 8919 O  O     . HOH H 4 .   ? -18.341 -4.294  12.485  1 17.893  ? 742  HOH B O     1 
HETATM 8920 O  O     . HOH H 4 .   ? -25.47  -8.081  -12.088 1 22.849  ? 743  HOH B O     1 
HETATM 8921 O  O     . HOH H 4 .   ? -23.22  -9.123  -13.239 1 33.762  ? 744  HOH B O     1 
HETATM 8922 O  O     . HOH H 4 .   ? -27.855 7.486   32.928  1 16.889  ? 745  HOH B O     1 
HETATM 8923 O  O     . HOH H 4 .   ? -6.044  25.425  18.584  1 35.021  ? 746  HOH B O     1 
HETATM 8924 O  O     . HOH H 4 .   ? -26.69  7.045   9.714   1 17.872  ? 747  HOH B O     1 
HETATM 8925 O  O     . HOH H 4 .   ? -22.5   -12.718 15.764  1 51.344  ? 748  HOH B O     1 
HETATM 8926 O  O     . HOH H 4 .   ? -50.726 -17.102 9.218   1 45.348  ? 749  HOH B O     1 
HETATM 8927 O  O     . HOH H 4 .   ? -13.368 -3.285  19.903  1 46.083  ? 750  HOH B O     1 
HETATM 8928 O  O     . HOH H 4 .   ? -8.082  -2.408  -11.816 1 28.818  ? 751  HOH B O     1 
HETATM 8929 O  O     . HOH H 4 .   ? -20.965 3.217   0.802   1 20.196  ? 752  HOH B O     1 
HETATM 8930 O  O     . HOH H 4 .   ? -37.803 -3.55   -11.042 1 22.657  ? 753  HOH B O     1 
HETATM 8931 O  O     . HOH H 4 .   ? -13.198 26.346  5.769   1 22.322  ? 754  HOH B O     1 
HETATM 8932 O  O     . HOH H 4 .   ? 8.314   -0.449  7.23    1 38.194  ? 755  HOH B O     1 
HETATM 8933 O  O     . HOH H 4 .   ? -1.021  14.964  23.864  1 24.001  ? 756  HOH B O     1 
HETATM 8934 O  O     . HOH H 4 .   ? -16.826 18.229  19.66   1 14.268  ? 757  HOH B O     1 
HETATM 8935 O  O     . HOH H 4 .   ? -21.663 -1.932  28.092  1 22.113  ? 758  HOH B O     1 
HETATM 8936 O  O     . HOH H 4 .   ? -27.227 9.492   24.08   1 17.237  ? 759  HOH B O     1 
HETATM 8937 O  O     . HOH H 4 .   ? -37.638 -18.928 8.435   1 20.369  ? 760  HOH B O     1 
HETATM 8938 O  O     . HOH H 4 .   ? -16.948 -3.351  -6.418  1 22.031  ? 761  HOH B O     1 
HETATM 8939 O  O     . HOH H 4 .   ? -44.186 12.632  12.428  1 20.178  ? 762  HOH B O     1 
HETATM 8940 O  O     . HOH H 4 .   ? -19.506 -0.14   35.808  1 17.023  ? 763  HOH B O     1 
HETATM 8941 O  O     . HOH H 4 .   ? 0.317   18.095  16.602  1 19.26   ? 764  HOH B O     1 
HETATM 8942 O  O     . HOH H 4 .   ? -13.924 -9.594  -13.203 1 41.868  ? 765  HOH B O     1 
HETATM 8943 O  O     . HOH H 4 .   ? -30.312 6.433   -18.635 1 41.144  ? 766  HOH B O     1 
HETATM 8944 O  O     . HOH H 4 .   ? -22.184 4.67    -20.068 1 24.666  ? 767  HOH B O     1 
HETATM 8945 O  O     . HOH H 4 .   ? -11.444 9.122   -12.504 1 40.266  ? 768  HOH B O     1 
HETATM 8946 O  O     . HOH H 4 .   ? -26.985 13.903  12.127  1 12.916  ? 769  HOH B O     1 
HETATM 8947 O  O     . HOH H 4 .   ? -31.538 -4.508  -15.154 1 17.782  ? 770  HOH B O     1 
HETATM 8948 O  O     . HOH H 4 .   ? 1.108   20.225  24.034  1 16.695  ? 771  HOH B O     1 
HETATM 8949 O  O     . HOH H 4 .   ? -41.112 17.901  -6.185  1 31.6    ? 772  HOH B O     1 
HETATM 8950 O  O     . HOH H 4 .   ? -30.55  -0.786  33.611  1 21.888  ? 773  HOH B O     1 
HETATM 8951 O  O     . HOH H 4 .   ? -14.169 13.945  2.282   1 21.16   ? 774  HOH B O     1 
HETATM 8952 O  O     . HOH H 4 .   ? -22.059 -13.762 8.632   1 26.619  ? 775  HOH B O     1 
HETATM 8953 O  O     . HOH H 4 .   ? -23.485 27.626  7.892   1 37.527  ? 776  HOH B O     1 
HETATM 8954 O  O     . HOH H 4 .   ? 10.692  25.811  25.093  1 25.44   ? 777  HOH B O     1 
HETATM 8955 O  O     . HOH H 4 .   ? -41.36  15.171  -0.885  1 21.789  ? 778  HOH B O     1 
HETATM 8956 O  O     . HOH H 4 .   ? -30.221 -5.247  -19.707 1 38.151  ? 779  HOH B O     1 
HETATM 8957 O  O     . HOH H 4 .   ? -8.298  25.254  9.941   1 18.758  ? 780  HOH B O     1 
HETATM 8958 O  O     . HOH H 4 .   ? -22.786 27.526  14.808  1 31.308  ? 781  HOH B O     1 
HETATM 8959 O  O     . HOH H 4 .   ? -20.087 11.47   -11.78  1 17.629  ? 782  HOH B O     1 
HETATM 8960 O  O     . HOH H 4 .   ? -27.077 7       6.047   1 18.717  ? 783  HOH B O     1 
HETATM 8961 O  O     . HOH H 4 .   ? -16.101 11.537  0.436   1 20.005  ? 784  HOH B O     1 
HETATM 8962 O  O     . HOH H 4 .   ? -14.526 -5.444  12.54   1 16.573  ? 785  HOH B O     1 
HETATM 8963 O  O     . HOH H 4 .   ? 16.789  31.963  41.535  1 19.632  ? 786  HOH B O     1 
HETATM 8964 O  O     . HOH H 4 .   ? -21.949 -9.776  3.193   1 21.17   ? 787  HOH B O     1 
HETATM 8965 O  O     . HOH H 4 .   ? -32.529 4.727   10.402  1 14.714  ? 788  HOH B O     1 
HETATM 8966 O  O     . HOH H 4 .   ? -28.432 15.886  18.564  1 18.222  ? 789  HOH B O     1 
HETATM 8967 O  O     . HOH H 4 .   ? 30.66   23.571  34.931  1 24.804  ? 790  HOH B O     1 
HETATM 8968 O  O     . HOH H 4 .   ? -11.924 -19.911 39.293  1 54.076  ? 791  HOH B O     1 
HETATM 8969 O  O     . HOH H 4 .   ? -34.573 20.39   25.313  1 43.027  ? 792  HOH B O     1 
HETATM 8970 O  O     . HOH H 4 .   ? 15.508  29.232  32.609  1 33.144  ? 793  HOH B O     1 
HETATM 8971 O  O     . HOH H 4 .   ? -6.319  15.917  6.859   1 23.226  ? 794  HOH B O     1 
HETATM 8972 O  O     . HOH H 4 .   ? -37.234 13.351  10.288  1 15.109  ? 795  HOH B O     1 
HETATM 8973 O  O     . HOH H 4 .   ? -17.482 10.577  3.388   1 15.191  ? 796  HOH B O     1 
HETATM 8974 O  O     . HOH H 4 .   ? -35.064 -9.239  18.087  1 33.969  ? 797  HOH B O     1 
HETATM 8975 O  O     . HOH H 4 .   ? -22.553 28.033  -7.317  1 56.668  ? 798  HOH B O     1 
HETATM 8976 O  O     . HOH H 4 .   ? -13.473 23.358  23.395  1 38.265  ? 799  HOH B O     1 
HETATM 8977 O  O     . HOH H 4 .   ? 2.488   4.767   -8.539  1 31.236  ? 800  HOH B O     1 
HETATM 8978 O  O     . HOH H 4 .   ? -8.328  2.424   -13.681 1 41.389  ? 801  HOH B O     1 
HETATM 8979 O  O     . HOH H 4 .   ? -24.865 0.587   22.516  1 16.256  ? 802  HOH B O     1 
HETATM 8980 O  O     . HOH H 4 .   ? -13.846 -4.772  15.247  1 16.693  ? 803  HOH B O     1 
HETATM 8981 O  O     . HOH H 4 .   ? -44.473 9.072   25.304  1 37.771  ? 804  HOH B O     1 
HETATM 8982 O  O     . HOH H 4 .   ? -32.542 8.251   18.672  1 19.129  ? 805  HOH B O     1 
HETATM 8983 O  O     . HOH H 4 .   ? 6.837   4.277   1.289   1 25.848  ? 806  HOH B O     1 
HETATM 8984 O  O     . HOH H 4 .   ? -14.918 4.973   -1.065  1 21.882  ? 807  HOH B O     1 
HETATM 8985 O  O     . HOH H 4 .   ? -21.263 12.637  28.979  1 18.327  ? 808  HOH B O     1 
HETATM 8986 O  O     . HOH H 4 .   ? -29.978 -4.048  23.876  1 25.929  ? 809  HOH B O     1 
HETATM 8987 O  O     . HOH H 4 .   ? -31.943 20.185  19.24   1 17.664  ? 810  HOH B O     1 
HETATM 8988 O  O     . HOH H 4 .   ? -30.747 -12.298 11.92   1 26.931  ? 811  HOH B O     1 
HETATM 8989 O  O     . HOH H 4 .   ? -27.524 26.171  9.904   1 36.94   ? 812  HOH B O     1 
HETATM 8990 O  O     . HOH H 4 .   ? -42.702 16.987  25.734  1 26.451  ? 813  HOH B O     1 
HETATM 8991 O  O     . HOH H 4 .   ? -2.336  27.609  7.092   1 39.693  ? 814  HOH B O     1 
HETATM 8992 O  O     . HOH H 4 .   ? -31.703 6.306   20.896  1 18.712  ? 815  HOH B O     1 
HETATM 8993 O  O     . HOH H 4 .   ? -2.562  28.5    11.363  1 41.019  ? 816  HOH B O     1 
HETATM 8994 O  O     . HOH H 4 .   ? -33.963 -14.855 5.157   1 33.319  ? 817  HOH B O     1 
HETATM 8995 O  O     . HOH H 4 .   ? 27.449  26.146  28.901  1 46.626  ? 818  HOH B O     1 
HETATM 8996 O  O     . HOH H 4 .   ? 16.299  24.101  39.536  1 28.483  ? 819  HOH B O     1 
HETATM 8997 O  O     . HOH H 4 .   ? -18.267 1.184   3.654   1 22.523  ? 820  HOH B O     1 
HETATM 8998 O  O     . HOH H 4 .   ? 25.775  25.101  40.334  1 30.793  ? 821  HOH B O     1 
HETATM 8999 O  O     . HOH H 4 .   ? -50.009 3.988   19.527  1 28.637  ? 822  HOH B O     1 
HETATM 9000 O  O     . HOH H 4 .   ? -15.187 10.703  -3.478  1 32.105  ? 823  HOH B O     1 
HETATM 9001 O  O     . HOH H 4 .   ? -13.237 5.546   -15.096 1 24.894  ? 824  HOH B O     1 
HETATM 9002 O  O     . HOH H 4 .   ? -12.626 -11.777 37.95   1 29.439  ? 825  HOH B O     1 
HETATM 9003 O  O     . HOH H 4 .   ? -36.714 -3.991  -14.536 1 25.896  ? 826  HOH B O     1 
HETATM 9004 O  O     . HOH H 4 .   ? -26.253 -2.8    22.633  1 23.881  ? 827  HOH B O     1 
HETATM 9005 O  O     . HOH H 4 .   ? -24.847 -12.983 7.963   1 24.944  ? 828  HOH B O     1 
HETATM 9006 O  O     . HOH H 4 .   ? -1.665  20.509  2.385   1 28.934  ? 829  HOH B O     1 
HETATM 9007 O  O     . HOH H 4 .   ? -38.439 -3.81   15.504  1 21.432  ? 830  HOH B O     1 
HETATM 9008 O  O     . HOH H 4 .   ? 3.84    12.819  23.678  1 20.488  ? 831  HOH B O     1 
HETATM 9009 O  O     . HOH H 4 .   ? -8.32   7.631   -3.708  1 23.092  ? 832  HOH B O     1 
HETATM 9010 O  O     . HOH H 4 .   ? -12.523 16.349  0.438   1 20.566  ? 833  HOH B O     1 
HETATM 9011 O  O     . HOH H 4 .   ? -17.796 -2.211  14.197  1 15.698  ? 834  HOH B O     1 
HETATM 9012 O  O     . HOH H 4 .   ? -46.252 -0.215  3.025   1 47.292  ? 835  HOH B O     1 
HETATM 9013 O  O     . HOH H 4 .   ? -16.899 22.731  24.127  1 33.929  ? 836  HOH B O     1 
HETATM 9014 O  O     . HOH H 4 .   ? -35.168 -18.737 18.641  1 52.857  ? 837  HOH B O     1 
HETATM 9015 O  O     . HOH H 4 .   ? -32.905 -13.026 1.439   1 32.604  ? 838  HOH B O     1 
HETATM 9016 O  O     . HOH H 4 .   ? -11.611 7.113   2.591   1 17.815  ? 839  HOH B O     1 
HETATM 9017 O  O     . HOH H 4 .   ? -25.865 21.002  6.064   1 24.082  ? 840  HOH B O     1 
HETATM 9018 O  O     . HOH H 4 .   ? -23.136 -15.878 7.085   1 48.987  ? 841  HOH B O     1 
HETATM 9019 O  O     . HOH H 4 .   ? -16.284 26.583  9.48    1 25.25   ? 842  HOH B O     1 
HETATM 9020 O  O     . HOH H 4 .   ? -29.367 1.329   2.269   1 17.449  ? 843  HOH B O     1 
HETATM 9021 O  O     . HOH H 4 .   ? 6.356   13.103  4.149   1 36.703  ? 844  HOH B O     1 
HETATM 9022 O  O     . HOH H 4 .   ? 12.568  31.501  27.722  1 26.656  ? 845  HOH B O     1 
HETATM 9023 O  O     . HOH H 4 .   ? -1.521  10.808  -3.302  1 35.222  ? 846  HOH B O     1 
HETATM 9024 O  O     . HOH H 4 .   ? -15.7   -3.571  10.986  1 17.483  ? 847  HOH B O     1 
HETATM 9025 O  O     . HOH H 4 .   ? -31.26  20.487  -14.014 1 20.451  ? 848  HOH B O     1 
HETATM 9026 O  O     . HOH H 4 .   ? -7.167  -1.098  -9.666  1 23.325  ? 849  HOH B O     1 
HETATM 9027 O  O     . HOH H 4 .   ? -15.464 -10.929 -10.548 1 25.932  ? 850  HOH B O     1 
HETATM 9028 O  O     . HOH H 4 .   ? -20.97  22.052  -9.567  1 37.878  ? 851  HOH B O     1 
HETATM 9029 O  O     . HOH H 4 .   ? -35.065 -13.174 3.333   1 25.742  ? 852  HOH B O     1 
HETATM 9030 O  O     . HOH H 4 .   ? -18.48  21.694  -10.504 1 38.841  ? 853  HOH B O     1 
HETATM 9031 O  O     . HOH H 4 .   ? -6.448  -7.65   -6.552  1 20.457  ? 854  HOH B O     1 
HETATM 9032 O  O     . HOH H 4 .   ? -0.959  16.601  14.117  1 22.957  ? 855  HOH B O     1 
HETATM 9033 O  O     . HOH H 4 .   ? -26.311 13.712  -16.198 1 26.986  ? 856  HOH B O     1 
HETATM 9034 O  O     . HOH H 4 .   ? -20.718 3.82    -2.852  1 26.567  ? 857  HOH B O     1 
HETATM 9035 O  O     . HOH H 4 .   ? -15.083 6.658   1.01    1 25.209  ? 858  HOH B O     1 
HETATM 9036 O  O     . HOH H 4 .   ? -12.476 2.669   15.217  1 15.021  ? 859  HOH B O     1 
HETATM 9037 O  O     . HOH H 4 .   ? -0.409  8.163   0.078   1 21.548  ? 860  HOH B O     1 
HETATM 9038 O  O     . HOH H 4 .   ? -0.188  -1.612  -6.226  1 22.382  ? 861  HOH B O     1 
HETATM 9039 O  O     . HOH H 4 .   ? 3.837   10.283  6.621   1 17.727  ? 862  HOH B O     1 
HETATM 9040 O  O     . HOH H 4 .   ? -46.855 -2.766  16.647  1 43.98   ? 863  HOH B O     1 
HETATM 9041 O  O     . HOH H 4 .   ? 3.627   13.938  5.101   1 21.829  ? 864  HOH B O     1 
HETATM 9042 O  O     . HOH H 4 .   ? -18.033 23.654  20.914  1 19.814  ? 865  HOH B O     1 
HETATM 9043 O  O     . HOH H 4 .   ? -32.637 1.385   20.36   1 16.414  ? 866  HOH B O     1 
HETATM 9044 O  O     . HOH H 4 .   ? -25.888 8.841   34.109  1 20.562  ? 867  HOH B O     1 
HETATM 9045 O  O     . HOH H 4 .   ? -2.354  24.348  5.088   1 27.557  ? 868  HOH B O     1 
HETATM 9046 O  O     . HOH H 4 .   ? -34.124 0.359   26.136  1 20.972  ? 869  HOH B O     1 
HETATM 9047 O  O     . HOH H 4 .   ? -44.576 3.727   5.074   1 21.086  ? 870  HOH B O     1 
HETATM 9048 O  O     . HOH H 4 .   ? -24.351 12.311  20.597  1 13.903  ? 871  HOH B O     1 
HETATM 9049 O  O     . HOH H 4 .   ? -32.214 -14.56  10.889  1 26.77   ? 872  HOH B O     1 
HETATM 9050 O  O     . HOH H 4 .   ? -38.467 19.576  -5.962  1 29.208  ? 873  HOH B O     1 
HETATM 9051 O  O     . HOH H 4 .   ? -3.906  22.535  3.569   1 30.356  ? 874  HOH B O     1 
HETATM 9052 O  O     . HOH H 4 .   ? -37.297 10.886  11.463  1 15.591  ? 875  HOH B O     1 
HETATM 9053 O  O     . HOH H 4 .   ? -17.348 -6.79   25.466  1 33.62   ? 876  HOH B O     1 
HETATM 9054 O  O     . HOH H 4 .   ? -40.832 -2.374  -4.021  1 24.11   ? 877  HOH B O     1 
HETATM 9055 O  O     . HOH H 4 .   ? -21.698 12.514  20.514  1 15.381  ? 878  HOH B O     1 
HETATM 9056 O  O     . HOH H 4 .   ? -15.08  -3.453  -8.461  1 26.678  ? 879  HOH B O     1 
HETATM 9057 O  O     . HOH H 4 .   ? -35.166 7.172   -13.222 1 18.628  ? 880  HOH B O     1 
HETATM 9058 O  O     . HOH H 4 .   ? -34.991 14.279  11.686  1 17.426  ? 881  HOH B O     1 
HETATM 9059 O  O     . HOH H 4 .   ? -52.425 1.668   16.41   1 36.092  ? 882  HOH B O     1 
HETATM 9060 O  O     . HOH H 4 .   ? -26.281 13.656  8.804   1 21.811  ? 883  HOH B O     1 
HETATM 9061 O  O     . HOH H 4 .   ? 4.576   9.084   15.466  1 15.439  ? 884  HOH B O     1 
HETATM 9062 O  O     . HOH H 4 .   ? -16.63  27.155  23.977  1 34.321  ? 885  HOH B O     1 
HETATM 9063 O  O     . HOH H 4 .   ? -20.378 6.845   1.705   1 21.328  ? 886  HOH B O     1 
HETATM 9064 O  O     . HOH H 4 .   ? -29.023 -7.415  -10.709 1 32.735  ? 887  HOH B O     1 
HETATM 9065 O  O     . HOH H 4 .   ? -3.313  -5.165  -3.715  1 25.738  ? 888  HOH B O     1 
HETATM 9066 O  O     . HOH H 4 .   ? -12.587 3.253   8.116   1 18.351  ? 889  HOH B O     1 
HETATM 9067 O  O     . HOH H 4 .   ? 6.685   7.96    19.682  1 25.462  ? 890  HOH B O     1 
HETATM 9068 O  O     . HOH H 4 .   ? -15.856 -0.582  10.739  1 20.096  ? 891  HOH B O     1 
HETATM 9069 O  O     . HOH H 4 .   ? -11.844 12.123  1.715   1 28.779  ? 892  HOH B O     1 
HETATM 9070 O  O     . HOH H 4 .   ? -12.649 22.617  8.194   1 20.822  ? 893  HOH B O     1 
HETATM 9071 O  O     . HOH H 4 .   ? -10.715 0.982   10.267  1 14.482  ? 894  HOH B O     1 
HETATM 9072 O  O     . HOH H 4 .   ? -33.794 9.487   7.843   1 21.167  ? 895  HOH B O     1 
HETATM 9073 O  O     . HOH H 4 .   ? 4.915   33.338  25.933  1 30.927  ? 896  HOH B O     1 
HETATM 9074 O  O     . HOH H 4 .   ? -16.14  -7.78   13.272  1 20.218  ? 897  HOH B O     1 
HETATM 9075 O  O     . HOH H 4 .   ? -41.687 -9.157  -8.61   1 38.746  ? 898  HOH B O     1 
HETATM 9076 O  O     . HOH H 4 .   ? -23.023 2.758   8.443   1 47.809  ? 899  HOH B O     1 
HETATM 9077 O  O     . HOH H 4 .   ? -32.701 4.721   27.212  1 13.535  ? 900  HOH B O     1 
HETATM 9078 O  O     . HOH H 4 .   ? -19.525 -2.277  -9.476  1 29.774  ? 901  HOH B O     1 
HETATM 9079 O  O     . HOH H 4 .   ? -21.110 3.565   -24.781 1 26.621  ? 902  HOH B O     1 
HETATM 9080 O  O     . HOH H 4 .   ? 1.278   5.465   21.459  1 21.886  ? 903  HOH B O     1 
HETATM 9081 O  O     . HOH H 4 .   ? 3.326   0.234   -7.881  1 38.392  ? 904  HOH B O     1 
HETATM 9082 O  O     . HOH H 4 .   ? 7.063   32.389  31.758  1 36.276  ? 905  HOH B O     1 
HETATM 9083 O  O     . HOH H 4 .   ? -9.517  -2.917  20.301  1 37.619  ? 906  HOH B O     1 
HETATM 9084 O  O     . HOH H 4 .   ? -44.684 7.454   -4.691  1 31.344  ? 907  HOH B O     1 
HETATM 9085 O  O     . HOH H 4 .   ? -10.961 4.348   0.365   1 16.78   ? 908  HOH B O     1 
HETATM 9086 O  O     . HOH H 4 .   ? -42.167 20.554  11.577  1 41.095  ? 909  HOH B O     1 
HETATM 9087 O  O     . HOH H 4 .   ? -30.476 -18.562 6.595   1 35.242  ? 910  HOH B O     1 
HETATM 9088 O  O     . HOH H 4 .   ? -35.951 9.859   13.669  1 18.861  ? 911  HOH B O     1 
HETATM 9089 O  O     . HOH H 4 .   ? -3.377  -12.936 3.678   1 32.04   ? 912  HOH B O     1 
HETATM 9090 O  O     . HOH H 4 .   ? -10.05  16.044  22.289  1 16.313  ? 913  HOH B O     1 
HETATM 9091 O  O     . HOH H 4 .   ? 32.849  23.583  41.386  1 33.461  ? 914  HOH B O     1 
HETATM 9092 O  O     . HOH H 4 .   ? -18.643 10.334  29.189  1 21.435  ? 915  HOH B O     1 
HETATM 9093 O  O     . HOH H 4 .   ? -14.797 20.384  -1.361  1 22.383  ? 916  HOH B O     1 
HETATM 9094 O  O     . HOH H 4 .   ? -45.544 10.463  9.492   1 21.328  ? 917  HOH B O     1 
HETATM 9095 O  O     . HOH H 4 .   ? -4.082  -2.689  -11.032 1 31.021  ? 918  HOH B O     1 
HETATM 9096 O  O     . HOH H 4 .   ? -23.363 15.986  37.843  1 37.86   ? 919  HOH B O     1 
HETATM 9097 O  O     . HOH H 4 .   ? -14.897 22.379  9.671   1 19.283  ? 920  HOH B O     1 
HETATM 9098 O  O     . HOH H 4 .   ? -38.888 3.122   30.667  1 32.376  ? 921  HOH B O     1 
HETATM 9099 O  O     . HOH H 4 .   ? -26.379 18.108  6.665   1 17.153  ? 922  HOH B O     1 
HETATM 9100 O  O     . HOH H 4 .   ? -42.768 -6.45   10.518  1 28.443  ? 923  HOH B O     1 
HETATM 9101 O  O     . HOH H 4 .   ? 0.573   -0.027  23.275  1 29.345  ? 924  HOH B O     1 
HETATM 9102 O  O     . HOH H 4 .   ? -44.797 -8.4    10.56   1 32.621  ? 925  HOH B O     1 
HETATM 9103 O  O     . HOH H 4 .   ? -19.992 5.093   -15.832 1 24.779  ? 926  HOH B O     1 
HETATM 9104 O  O     . HOH H 4 .   ? -13.811 22.772  -2.245  1 25.567  ? 927  HOH B O     1 
HETATM 9105 O  O     . HOH H 4 .   ? -16.837 20.9    21.045  1 31.507  ? 928  HOH B O     1 
HETATM 9106 O  O     . HOH H 4 .   ? -12.474 20.776  1.684   1 20.03   ? 929  HOH B O     1 
HETATM 9107 O  O     . HOH H 4 .   ? -36.278 14.168  19.267  1 20.544  ? 930  HOH B O     1 
HETATM 9108 O  O     . HOH H 4 .   ? -9.642  -4.244  41.776  1 17.355  ? 931  HOH B O     1 
HETATM 9109 O  O     . HOH H 4 .   ? -27.022 7.788   27.529  1 16.414  ? 932  HOH B O     1 
HETATM 9110 O  O     . HOH H 4 .   ? 0.691   24.598  18.169  1 35.554  ? 933  HOH B O     1 
HETATM 9111 O  O     . HOH H 4 .   ? -32.898 24.63   6.84    1 25.76   ? 934  HOH B O     1 
HETATM 9112 O  O     . HOH H 4 .   ? -40.555 -1.701  -9.151  1 24.377  ? 935  HOH B O     1 
HETATM 9113 O  O     . HOH H 4 .   ? -12.357 -2.027  22.025  1 36.129  ? 936  HOH B O     1 
HETATM 9114 O  O     . HOH H 4 .   ? -11.378 25.048  18.136  1 25.522  ? 937  HOH B O     1 
HETATM 9115 O  O     . HOH H 4 .   ? -38.552 -4.612  -19.473 1 38.745  ? 938  HOH B O     1 
HETATM 9116 O  O     . HOH H 4 .   ? -11.874 6.341   23.541  1 17.118  ? 939  HOH B O     1 
HETATM 9117 O  O     . HOH H 4 .   ? -27.156 -4.893  24.455  1 31.652  ? 940  HOH B O     1 
HETATM 9118 O  O     . HOH H 4 .   ? -14.829 -0.861  23.095  1 21.205  ? 941  HOH B O     1 
HETATM 9119 O  O     . HOH H 4 .   ? -44.28  5.79    23.863  1 39.544  ? 942  HOH B O     1 
HETATM 9120 O  O     . HOH H 4 .   ? -19.769 -0.034  15.839  1 16.427  ? 943  HOH B O     1 
HETATM 9121 O  O     . HOH H 4 .   ? -1.769  11.388  1.813   1 21.644  ? 944  HOH B O     1 
HETATM 9122 O  O     . HOH H 4 .   ? -31.703 3.001   22.892  1 20.782  ? 945  HOH B O     1 
HETATM 9123 O  O     . HOH H 4 .   ? -24.299 -6.796  -16.116 1 35.235  ? 946  HOH B O     1 
HETATM 9124 O  O     . HOH H 4 .   ? -38.727 -11.913 -1.579  1 25.996  ? 947  HOH B O     1 
HETATM 9125 O  O     . HOH H 4 .   ? -13.605 4.851   21.643  1 23.453  ? 948  HOH B O     1 
HETATM 9126 O  O     . HOH H 4 .   ? -1.593  -5.421  13.917  1 32.093  ? 949  HOH B O     1 
HETATM 9127 O  O     . HOH H 4 .   ? -41.858 10.752  -5.728  1 24.183  ? 950  HOH B O     1 
HETATM 9128 O  O     . HOH H 4 .   ? -24.642 3.839   -24.063 1 29.285  ? 951  HOH B O     1 
HETATM 9129 O  O     . HOH H 4 .   ? -41.404 17.439  -9.097  1 31.203  ? 952  HOH B O     1 
HETATM 9130 O  O     . HOH H 4 .   ? -23.083 17.664  34.548  1 28.137  ? 953  HOH B O     1 
HETATM 9131 O  O     . HOH H 4 .   ? -29.132 7.074   18.447  1 18.415  ? 954  HOH B O     1 
HETATM 9132 O  O     . HOH H 4 .   ? 17.593  34.661  36.231  1 27.148  ? 955  HOH B O     1 
HETATM 9133 O  O     . HOH H 4 .   ? -45.448 10.322  4.173   1 25.213  ? 956  HOH B O     1 
HETATM 9134 O  O     . HOH H 4 .   ? -33.131 -13.185 8.842   1 31.917  ? 957  HOH B O     1 
HETATM 9135 O  O     . HOH H 4 .   ? -12.586 26.717  14.782  1 31.819  ? 958  HOH B O     1 
HETATM 9136 O  O     . HOH H 4 .   ? -24.054 2.158   20.64   1 14.184  ? 959  HOH B O     1 
HETATM 9137 O  O     . HOH H 4 .   ? -4.343  11.085  -0.141  1 25.928  ? 960  HOH B O     1 
HETATM 9138 O  O     . HOH H 4 .   ? -17.892 3.019   -0.424  1 25.121  ? 961  HOH B O     1 
HETATM 9139 O  O     . HOH H 4 .   ? -15.459 4.194   30.01   1 14.222  ? 962  HOH B O     1 
HETATM 9140 O  O     . HOH H 4 .   ? -7.325  -0.256  26.747  1 17.329  ? 963  HOH B O     1 
HETATM 9141 O  O     . HOH H 4 .   ? -40.637 -11.78  -17.902 1 60.76   ? 964  HOH B O     1 
HETATM 9142 O  O     . HOH H 4 .   ? -44.09  22.901  17.793  1 38.294  ? 965  HOH B O     1 
HETATM 9143 O  O     . HOH H 4 .   ? 6.594   31.795  24.509  1 25.105  ? 966  HOH B O     1 
HETATM 9144 O  O     . HOH H 4 .   ? 8.699   6.538   3.37    1 33.458  ? 967  HOH B O     1 
HETATM 9145 O  O     . HOH H 4 .   ? -32.137 -13.434 -12.912 1 41.273  ? 968  HOH B O     1 
HETATM 9146 O  O     . HOH H 4 .   ? -48.484 -0.591  14.567  1 36.506  ? 969  HOH B O     1 
HETATM 9147 O  O     . HOH H 4 .   ? -37.955 6.205   2.982   1 21.273  ? 970  HOH B O     1 
HETATM 9148 O  O     . HOH H 4 .   ? -27.466 -11.676 11.492  1 30.423  ? 971  HOH B O     1 
HETATM 9149 O  O     . HOH H 4 .   ? -43.933 -5.607  17.264  1 34.768  ? 972  HOH B O     1 
HETATM 9150 O  O     . HOH H 4 .   ? -5.514  27.662  15.965  1 40.545  ? 973  HOH B O     1 
HETATM 9151 O  O     . HOH H 4 .   ? -10.173 6.501   -1.854  1 21.789  ? 974  HOH B O     1 
HETATM 9152 O  O     . HOH H 4 .   ? 29.666  22.107  30.23   1 42.398  ? 975  HOH B O     1 
HETATM 9153 O  O     . HOH H 4 .   ? -43.953 13.185  15.364  1 22.858  ? 976  HOH B O     1 
HETATM 9154 O  O     . HOH H 4 .   ? -13.39  -4.841  29.091  1 49.633  ? 977  HOH B O     1 
HETATM 9155 O  O     . HOH H 4 .   ? -40.926 -2.701  19.145  1 19.937  ? 978  HOH B O     1 
HETATM 9156 O  O     . HOH H 4 .   ? -35.632 1.212   14.77   1 21.738  ? 979  HOH B O     1 
HETATM 9157 O  O     . HOH H 4 .   ? -42.238 9.028   -9.862  1 47.366  ? 980  HOH B O     1 
HETATM 9158 O  O     . HOH H 4 .   ? -5.488  26.131  4.089   1 25.445  ? 981  HOH B O     1 
HETATM 9159 O  O     . HOH H 4 .   ? -43.009 -5.228  -19.9   1 42.015  ? 982  HOH B O     1 
HETATM 9160 O  O     . HOH H 4 .   ? -43.835 -1.373  9.946   1 24.228  ? 983  HOH B O     1 
HETATM 9161 O  O     . HOH H 4 .   ? -17.612 5.757   2.658   1 21.563  ? 984  HOH B O     1 
HETATM 9162 O  O     . HOH H 4 .   ? -15.752 -3.379  23.538  1 25.014  ? 985  HOH B O     1 
HETATM 9163 O  O     . HOH H 4 .   ? -29.708 9.148   17.038  1 14.964  ? 986  HOH B O     1 
HETATM 9164 O  O     . HOH H 4 .   ? -23.986 25.811  10.911  1 37.693  ? 987  HOH B O     1 
HETATM 9165 O  O     . HOH H 4 .   ? -16.913 -6.96   36.413  1 35.825  ? 988  HOH B O     1 
HETATM 9166 O  O     . HOH H 4 .   ? -23.468 13.008  27.25   1 13.569  ? 989  HOH B O     1 
HETATM 9167 O  O     . HOH H 4 .   ? -46.682 5.659   10.109  1 25.614  ? 990  HOH B O     1 
HETATM 9168 O  O     . HOH H 4 .   ? -21.388 5.337   -5.056  1 14.967  ? 991  HOH B O     1 
HETATM 9169 O  O     . HOH H 4 .   ? 5.396   0.824   20.693  1 68.822  ? 992  HOH B O     1 
HETATM 9170 O  O     . HOH H 4 .   ? -38.719 8.83    3.566   1 14.716  ? 993  HOH B O     1 
HETATM 9171 O  O     . HOH H 4 .   ? -16.663 -2.079  -10.315 1 23.674  ? 994  HOH B O     1 
HETATM 9172 O  O     . HOH H 4 .   ? -17.287 10.147  -1.532  1 19.124  ? 995  HOH B O     1 
HETATM 9173 O  O     . HOH H 4 .   ? -2.254  15.876  0.906   1 31.515  ? 996  HOH B O     1 
HETATM 9174 O  O     . HOH H 4 .   ? -7.362  -13.741 -7.215  1 31.043  ? 997  HOH B O     1 
HETATM 9175 O  O     . HOH H 4 .   ? 7.432   5.423   17.627  1 24.488  ? 998  HOH B O     1 
HETATM 9176 O  O     . HOH H 4 .   ? -28.31  20.348  -13.804 1 41.156  ? 999  HOH B O     1 
HETATM 9177 O  O     . HOH H 4 .   ? -30.91  23.847  10.585  1 18.426  ? 1000 HOH B O     1 
HETATM 9178 O  O     . HOH H 4 .   ? -8.183  25.038  14.8    1 24.185  ? 1001 HOH B O     1 
HETATM 9179 O  O     . HOH H 4 .   ? 5.51    30.343  22.034  1 20.731  ? 1002 HOH B O     1 
HETATM 9180 O  O     . HOH H 4 .   ? -15.806 -16.522 -3.619  1 35.618  ? 1003 HOH B O     1 
HETATM 9181 O  O     . HOH H 4 .   ? -22.808 -5.285  30.666  1 47.929  ? 1004 HOH B O     1 
HETATM 9182 O  O     . HOH H 4 .   ? -26.753 -4.108  38.999  1 38.019  ? 1005 HOH B O     1 
HETATM 9183 O  O     . HOH H 4 .   ? -25.247 26.113  13.978  1 30.241  ? 1006 HOH B O     1 
HETATM 9184 O  O     . HOH H 4 .   ? -3.741  -12.583 -1.598  1 27.564  ? 1007 HOH B O     1 
HETATM 9185 O  O     . HOH H 4 .   ? -9.008  26.251  12.5    1 31.147  ? 1008 HOH B O     1 
HETATM 9186 O  O     . HOH H 4 .   ? -35.725 -6.126  27.987  1 37.657  ? 1009 HOH B O     1 
HETATM 9187 O  O     . HOH H 4 .   ? -17.998 26.565  18.769  1 29.953  ? 1010 HOH B O     1 
HETATM 9188 O  O     . HOH H 4 .   ? -40.817 -9.479  -1.771  1 38.399  ? 1011 HOH B O     1 
HETATM 9189 O  O     . HOH H 4 .   ? -5.744  3.29    -13.471 1 33.077  ? 1012 HOH B O     1 
HETATM 9190 O  O     . HOH H 4 .   ? 8.752   14.203  4.82    1 50.095  ? 1013 HOH B O     1 
HETATM 9191 O  O     . HOH H 4 .   ? -23.716 -15.533 -9.375  1 25.138  ? 1014 HOH B O     1 
HETATM 9192 O  O     . HOH H 4 .   ? -29.717 -17.063 4.437   1 28.607  ? 1015 HOH B O     1 
HETATM 9193 O  O     . HOH H 4 .   ? -2.726  -5.74   -13.816 1 41.461  ? 1016 HOH B O     1 
HETATM 9194 O  O     . HOH H 4 .   ? 8.044   6.063   10.743  1 33.06   ? 1017 HOH B O     1 
HETATM 9195 O  O     . HOH H 4 .   ? -20.952 12.831  -13.938 1 34.588  ? 1018 HOH B O     1 
HETATM 9196 O  O     . HOH H 4 .   ? 27.446  22.986  37.726  1 15.291  ? 1019 HOH B O     1 
HETATM 9197 O  O     . HOH H 4 .   ? -18.406 8.3     2.31    1 42.63   ? 1020 HOH B O     1 
HETATM 9198 O  O     . HOH H 4 .   ? -22.967 20.56   -11.146 1 29.706  ? 1021 HOH B O     1 
HETATM 9199 O  O     . HOH H 4 .   ? -31.182 10.531  5.531   1 12.575  ? 1022 HOH B O     1 
HETATM 9200 O  O     . HOH H 4 .   ? -22.187 2.821   22.392  1 17.713  ? 1023 HOH B O     1 
HETATM 9201 O  O     . HOH H 4 .   ? -38.077 19.797  23.409  1 36.682  ? 1024 HOH B O     1 
HETATM 9202 O  O     . HOH H 4 .   ? -45.403 -0.813  19.799  1 43.39   ? 1025 HOH B O     1 
HETATM 9203 O  O     . HOH H 4 .   ? 1.563   14.307  12.701  1 24.715  ? 1026 HOH B O     1 
HETATM 9204 O  O     . HOH H 4 .   ? -45.043 5.566   7.189   1 34.96   ? 1027 HOH B O     1 
HETATM 9205 O  O     . HOH H 4 .   ? -48.11  -18.763 11.334  1 36.256  ? 1028 HOH B O     1 
HETATM 9206 O  O     . HOH H 4 .   ? -14.171 16.124  -2.837  1 28.964  ? 1029 HOH B O     1 
HETATM 9207 O  O     . HOH H 4 .   ? -25.859 -1.826  40.243  1 25.227  ? 1030 HOH B O     1 
HETATM 9208 O  O     . HOH H 4 .   ? -48.654 4.957   11.81   1 28.192  ? 1031 HOH B O     1 
HETATM 9209 O  O     . HOH H 4 .   ? 15.785  34.699  33.127  1 31.111  ? 1032 HOH B O     1 
HETATM 9210 O  O     . HOH H 4 .   ? -38.345 -4.15   30.064  1 44.731  ? 1033 HOH B O     1 
HETATM 9211 O  O     . HOH H 4 .   ? -26.238 11.763  37.95   1 45.673  ? 1034 HOH B O     1 
HETATM 9212 O  O     . HOH H 4 .   ? -24.633 26.492  33.539  1 39.197  ? 1035 HOH B O     1 
HETATM 9213 O  O     . HOH H 4 .   ? -13.703 17.389  25.638  1 27.827  ? 1036 HOH B O     1 
HETATM 9214 O  O     . HOH H 4 .   ? -6.215  19.337  23.837  1 31.348  ? 1037 HOH B O     1 
HETATM 9215 O  O     . HOH H 4 .   ? -8.865  19.828  24.021  1 43.081  ? 1038 HOH B O     1 
HETATM 9216 O  O     . HOH H 4 .   ? -33.02  21.358  -20.564 1 48.175  ? 1039 HOH B O     1 
HETATM 9217 O  O     . HOH H 4 .   ? -28.084 28.325  -5.223  1 49.451  ? 1040 HOH B O     1 
HETATM 9218 O  O     . HOH H 4 .   ? -15.097 -12.996 15.861  1 44.185  ? 1041 HOH B O     1 
HETATM 9219 O  O     . HOH H 4 .   ? -11.73  10.901  -1.137  1 27.314  ? 1042 HOH B O     1 
HETATM 9220 O  O     . HOH H 4 .   ? -3.765  20.081  22.439  1 30.526  ? 1043 HOH B O     1 
HETATM 9221 O  O     . HOH H 4 .   ? -43.467 14.813  -3.05   1 37.201  ? 1044 HOH B O     1 
HETATM 9222 O  O     . HOH H 4 .   ? -27.916 -8.961  -12.712 1 32.996  ? 1045 HOH B O     1 
HETATM 9223 O  O     . HOH H 4 .   ? -25.862 -6.475  14.268  1 45.752  ? 1046 HOH B O     1 
HETATM 9224 O  O     . HOH H 4 .   ? -19.031 26.21   2.761   1 37.631  ? 1047 HOH B O     1 
HETATM 9225 O  O     . HOH H 4 .   ? -46.16  -0.41   9.036   1 38.127  ? 1048 HOH B O     1 
HETATM 9226 O  O     . HOH H 4 .   ? -38.694 -1.874  -22.463 1 48.922  ? 1049 HOH B O     1 
HETATM 9227 O  O     . HOH H 4 .   ? -10.525 -13.032 36.518  1 27.622  ? 1050 HOH B O     1 
HETATM 9228 O  O     . HOH H 4 .   ? -18.158 -2.609  -22.124 1 50.522  ? 1051 HOH B O     1 
HETATM 9229 O  O     . HOH H 4 .   ? -17.382 6.466   -16.51  1 29.311  ? 1052 HOH B O     1 
HETATM 9230 O  O     . HOH H 4 .   ? -43.551 20.888  4.132   1 48.585  ? 1053 HOH B O     1 
HETATM 9231 O  O     . HOH H 4 .   ? -31.257 26.806  7.152   1 45.072  ? 1054 HOH B O     1 
HETATM 9232 O  O     . HOH H 4 .   ? -9.747  5.071   24.932  1 23.496  ? 1055 HOH B O     1 
HETATM 9233 O  O     . HOH H 4 .   ? -54.745 4.983   19.026  1 46.236  ? 1056 HOH B O     1 
HETATM 9234 O  O     . HOH H 4 .   ? -13.699 13.338  -5.634  1 43.941  ? 1057 HOH B O     1 
HETATM 9235 O  O     . HOH H 4 .   ? -48.038 0.08    6.768   1 47.31   ? 1058 HOH B O     1 
HETATM 9236 O  O     . HOH H 4 .   ? -28.957 21.155  29.245  1 17.274  ? 1059 HOH B O     1 
HETATM 9237 O  O     . HOH H 4 .   ? -37.278 21.38   28.841  1 44.851  ? 1060 HOH B O     1 
HETATM 9238 O  O     . HOH H 4 .   ? 31.057  23.233  32.209  1 35.346  ? 1061 HOH B O     1 
HETATM 9239 O  O     . HOH H 4 .   ? -10.982 -2.518  29.672  1 15.692  ? 1062 HOH B O     1 
HETATM 9240 O  O     . HOH H 4 .   ? -19.194 3.567   2.968   1 20.679  ? 1063 HOH B O     1 
HETATM 9241 O  O     . HOH H 4 .   ? -17.188 28.716  21.918  1 40.759  ? 1064 HOH B O     1 
HETATM 9242 O  O     . HOH H 4 .   ? -4.006  22.689  23.234  1 70.146  ? 1065 HOH B O     1 
HETATM 9243 O  O     . HOH H 4 .   ? -13.387 12.521  -2.476  1 36.6    ? 1066 HOH B O     1 
HETATM 9244 O  O     . HOH H 4 .   ? 0.367   17.448  11.903  1 33.766  ? 1067 HOH B O     1 
HETATM 9245 O  O     . HOH H 4 .   ? -30.718 -4.322  -24.953 1 43.391  ? 1068 HOH B O     1 
HETATM 9246 O  O     . HOH H 4 .   ? -44.908 -14.247 7.765   1 39.905  ? 1069 HOH B O     1 
HETATM 9247 O  O     . HOH H 4 .   ? -44.892 22.967  20.581  1 41.577  ? 1070 HOH B O     1 
HETATM 9248 O  O     . HOH H 4 .   ? -24.49  -8.582  20.217  1 28.227  ? 1071 HOH B O     1 
HETATM 9249 O  O     . HOH H 4 .   ? 0.513   0.841   -10.141 1 56.854  ? 1072 HOH B O     1 
HETATM 9250 O  O     . HOH H 4 .   ? -38.449 -13.823 18.385  1 63.249  ? 1073 HOH B O     1 
HETATM 9251 O  O     . HOH H 4 .   ? 11.781  28.903  17.285  1 43.73   ? 1074 HOH B O     1 
HETATM 9252 O  O     . HOH H 4 .   ? -1.577  -11.274 -2.728  1 28.458  ? 1075 HOH B O     1 
HETATM 9253 O  O     . HOH H 4 .   ? -12.537 18.944  -0.351  1 28.787  ? 1076 HOH B O     1 
HETATM 9254 O  O     . HOH H 4 .   ? -30.253 -13.648 14.404  1 39.783  ? 1077 HOH B O     1 
HETATM 9255 O  O     . HOH H 4 .   ? -33.327 26.464  4.903   1 50.426  ? 1078 HOH B O     1 
HETATM 9256 O  O     . HOH H 4 .   ? -47.502 -2.573  7.793   1 39.992  ? 1079 HOH B O     1 
HETATM 9257 O  O     . HOH H 4 .   ? -32.313 2.508   25.291  1 30.2    ? 1080 HOH B O     1 
HETATM 9258 O  O     . HOH H 4 .   ? -1.882  -0.414  -9.786  1 36.373  ? 1081 HOH B O     1 
HETATM 9259 O  O     . HOH H 4 .   ? -11.264 17.155  24.453  1 30.337  ? 1082 HOH B O     1 
HETATM 9260 O  O     . HOH H 4 .   ? -12.998 -14.07  14.196  1 34.231  ? 1083 HOH B O     1 
HETATM 9261 O  O     . HOH H 4 .   ? -21.622 -15.562 16.842  1 52.484  ? 1084 HOH B O     1 
HETATM 9262 O  O     . HOH H 4 .   ? 14.345  28.447  23.7    1 49.088  ? 1085 HOH B O     1 
HETATM 9263 O  O     . HOH H 4 .   ? -9.398  26.451  16.822  1 33.362  ? 1086 HOH B O     1 
HETATM 9264 O  O     . HOH H 4 .   ? 0.784   28.27   26.141  1 43.002  ? 1087 HOH B O     1 
HETATM 9265 O  O     . HOH H 4 .   ? 35.713  25.873  34.033  1 40.035  ? 1088 HOH B O     1 
HETATM 9266 O  O     . HOH H 4 .   ? -14.27  -5.311  25.095  1 45.324  ? 1089 HOH B O     1 
HETATM 9267 O  O     . HOH H 4 .   ? -46.583 12.525  10.957  1 27.63   ? 1090 HOH B O     1 
HETATM 9268 O  O     . HOH H 4 .   ? -7.76   -1.018  -14.126 1 49.306  ? 1091 HOH B O     1 
HETATM 9269 O  O     . HOH H 4 .   ? -0.317  17.523  -0.024  1 44.647  ? 1092 HOH B O     1 
HETATM 9270 O  O     . HOH H 4 .   ? 13.923  32.949  41.379  1 21.918  ? 1093 HOH B O     1 
HETATM 9271 O  O     . HOH H 4 .   ? -31.544 19.080  -18.953 1 48.928  ? 1094 HOH B O     1 
HETATM 9272 O  O     . HOH H 4 .   ? -50.454 7.046   12.275  1 26.527  ? 1095 HOH B O     1 
HETATM 9273 O  O     . HOH H 4 .   ? -46.483 10.895  6.732   1 27.651  ? 1096 HOH B O     1 
HETATM 9274 O  O     . HOH H 4 .   ? -17.654 28.733  14.587  1 35.306  ? 1097 HOH B O     1 
HETATM 9275 O  O     . HOH H 4 .   ? 7.856   2.782   -0.838  1 25.22   ? 1098 HOH B O     1 
HETATM 9276 O  O     . HOH H 4 .   ? -23.823 2.542   40.166  1 38.469  ? 1099 HOH B O     1 
HETATM 9277 O  O     . HOH H 4 .   ? 32.5    23.985  30.065  1 46.104  ? 1100 HOH B O     1 
HETATM 9278 O  O     . HOH H 4 .   ? 17.692  29.881  26.722  1 44.446  ? 1101 HOH B O     1 
HETATM 9279 O  O     . HOH H 4 .   ? 11.896  34.115  26.937  1 32.329  ? 1102 HOH B O     1 
HETATM 9280 O  O     . HOH H 4 .   ? -17.685 7.786   -0.205  1 22.019  ? 1103 HOH B O     1 
HETATM 9281 O  O     . HOH H 4 .   ? -10.183 11.613  -3.464  1 36.444  ? 1104 HOH B O     1 
HETATM 9282 O  O     . HOH H 4 .   ? -47.091 8.17    9.504   1 22.6    ? 1105 HOH B O     1 
HETATM 9283 O  O     . HOH H 4 .   ? -28.091 -9.531  -15.37  1 27.775  ? 1106 HOH B O     1 
HETATM 9284 O  O     . HOH H 4 .   ? -23.413 -5.824  35.02   1 35.507  ? 1107 HOH B O     1 
HETATM 9285 O  O     . HOH H 4 .   ? -3.172  18.191  -8.207  1 51.785  ? 1108 HOH B O     1 
HETATM 9286 O  O     . HOH H 4 .   ? 10.187  1.316   -7.301  1 52.028  ? 1109 HOH B O     1 
HETATM 9287 O  O     . HOH H 4 .   ? -10.984 24.574  9.119   1 21.966  ? 1110 HOH B O     1 
HETATM 9288 O  O     . HOH H 4 .   ? -11.425 26.803  7.928   1 27.553  ? 1111 HOH B O     1 
HETATM 9289 O  O     . HOH H 4 .   ? -31.306 1.144   35.265  1 34.157  ? 1112 HOH B O     1 
HETATM 9290 O  O     . HOH H 4 .   ? -35.426 -6.935  21.171  1 35.859  ? 1113 HOH B O     1 
HETATM 9291 O  O     . HOH H 4 .   ? -29.074 -2.158  37.342  1 25.919  ? 1114 HOH B O     1 
HETATM 9292 O  O     . HOH H 4 .   ? -10.856 14.231  0.434   1 29.792  ? 1115 HOH B O     1 
HETATM 9293 O  O     . HOH H 4 .   ? -7.546  11.178  -0.975  1 29.312  ? 1116 HOH B O     1 
HETATM 9294 O  O     . HOH H 4 .   ? -13.279 19.509  -5.474  1 34.485  ? 1117 HOH B O     1 
HETATM 9295 O  O     . HOH H 4 .   ? -1.18   26.722  4.776   1 40.396  ? 1118 HOH B O     1 
HETATM 9296 O  O     . HOH H 4 .   ? -7.686  10.366  -3.494  1 25.319  ? 1119 HOH B O     1 
HETATM 9297 O  O     . HOH H 4 .   ? -20.377 -6.045  -19.215 1 49.884  ? 1120 HOH B O     1 
HETATM 9298 O  O     . HOH H 4 .   ? -23.757 -17.641 -7.558  1 41.091  ? 1121 HOH B O     1 
HETATM 9299 O  O     . HOH H 4 .   ? 33.451  21.365  42.726  1 27.139  ? 1122 HOH B O     1 
HETATM 9300 O  O     . HOH H 4 .   ? -48.156 8.113   -5.219  1 53.08   ? 1123 HOH B O     1 
HETATM 9301 O  O     . HOH H 4 .   ? -31.886 18.595  31.373  1 25.109  ? 1124 HOH B O     1 
HETATM 9302 O  O     . HOH H 4 .   ? -30.654 -6.305  -17.382 1 23.811  ? 1125 HOH B O     1 
HETATM 9303 O  O     . HOH H 4 .   ? -11.887 7.859   -14.787 1 37.261  ? 1126 HOH B O     1 
HETATM 9304 O  O     . HOH H 4 .   ? -12.303 17.558  -7.354  1 37.375  ? 1127 HOH B O     1 
HETATM 9305 O  O     . HOH H 4 .   ? -23.906 -8.827  24.576  1 34.242  ? 1128 HOH B O     1 
HETATM 9306 O  O     . HOH H 4 .   ? 3.022   25.512  16.594  1 42.505  ? 1129 HOH B O     1 
HETATM 9307 O  O     . HOH H 4 .   ? -47.056 9.654   -7.122  1 44.902  ? 1130 HOH B O     1 
HETATM 9308 O  O     . HOH H 4 .   ? -48.188 7.815   5.523   1 39.699  ? 1131 HOH B O     1 
HETATM 9309 O  O     . HOH H 4 .   ? -26.405 -7.468  24.143  1 27.888  ? 1132 HOH B O     1 
HETATM 9310 O  O     . HOH H 4 .   ? -13.814 7.6     -17.022 1 48.197  ? 1133 HOH B O     1 
HETATM 9311 O  O     . HOH H 4 .   ? 1.923   32.176  25.789  1 40.26   ? 1134 HOH B O     1 
HETATM 9312 O  O     . HOH H 4 .   ? -16.37  -7.986  28.558  1 56.751  ? 1135 HOH B O     1 
HETATM 9313 O  O     . HOH H 4 .   ? -17.038 31.267  20.962  1 45.97   ? 1136 HOH B O     1 
HETATM 9314 O  O     . HOH H 4 .   ? -9.445  6.887   -16.116 1 46.506  ? 1137 HOH B O     1 
# 
