data_9AYI
# 
_entry.id   9AYI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9AYI         pdb_00009ayi 10.2210/pdb9ayi/pdb 
WWPDB D_1000282281 ?            ?                   
# 
_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       2025-03-12 
_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                        9AYI 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Same protein but with inhibitor NPD-389' 
_pdbx_database_related.db_id          8W24 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              k.loomes@auckland.ac.nz 
_pdbx_contact_author.name_first         Kerry 
_pdbx_contact_author.name_last          Loomes 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7562-3216 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Krinkel, B.A.' 1 ? 
'Squire, C.J.'  2 ? 
'Loomes, K.M.'  3 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Human malic enzyme 2 complex with inhibitor NPD-389' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_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 'Krinkel, B.A.' 1 ? 
primary 'Squire, C.J.'  2 ? 
primary 'Loomes, K.M.'  3 ? 
# 
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 'NAD-dependent malic enzyme, mitochondrial' 64706.309 4    1.1.1.38 ? ? ? 
2 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE           663.425   8    ?        ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                              62.068    5    ?        ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                              35.453    4    ?        ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                             24.305    2    ?        ? ? ? 
6 non-polymer syn 'L(+)-TARTARIC ACID'                        150.087   4    ?        ? ? ? 
7 water       nat water                                       18.015    1960 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'NAD-ME,Malic enzyme 2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFY
RILQDDIESLMPIVYTPTVGLA(CSX)SQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLG
VYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQ
FEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLS
EQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINER
PVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLE
AAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWP
ESASSPPVITELEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFY
RILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGM
GIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDF
GNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEA
QKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIF
ALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKA
LTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESAS
SPPVITELEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD 
3 1,2-ETHANEDIOL                    EDO 
4 'CHLORIDE ION'                    CL  
5 'MAGNESIUM ION'                   MG  
6 'L(+)-TARTARIC ACID'              TLA 
7 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   LEU n 
1 3   HIS n 
1 4   ILE n 
1 5   LYS n 
1 6   GLU n 
1 7   LYS n 
1 8   GLY n 
1 9   LYS n 
1 10  PRO n 
1 11  LEU n 
1 12  MET n 
1 13  LEU n 
1 14  ASN n 
1 15  PRO n 
1 16  ARG n 
1 17  THR n 
1 18  ASN n 
1 19  LYS n 
1 20  GLY n 
1 21  MET n 
1 22  ALA n 
1 23  PHE n 
1 24  THR n 
1 25  LEU n 
1 26  GLN n 
1 27  GLU n 
1 28  ARG n 
1 29  GLN n 
1 30  MET n 
1 31  LEU n 
1 32  GLY n 
1 33  LEU n 
1 34  GLN n 
1 35  GLY n 
1 36  LEU n 
1 37  LEU n 
1 38  PRO n 
1 39  PRO n 
1 40  LYS n 
1 41  ILE n 
1 42  GLU n 
1 43  THR n 
1 44  GLN n 
1 45  ASP n 
1 46  ILE n 
1 47  GLN n 
1 48  ALA n 
1 49  LEU n 
1 50  ARG n 
1 51  PHE n 
1 52  HIS n 
1 53  ARG n 
1 54  ASN n 
1 55  LEU n 
1 56  LYS n 
1 57  LYS n 
1 58  MET n 
1 59  THR n 
1 60  SER n 
1 61  PRO n 
1 62  LEU n 
1 63  GLU n 
1 64  LYS n 
1 65  TYR n 
1 66  ILE n 
1 67  TYR n 
1 68  ILE n 
1 69  MET n 
1 70  GLY n 
1 71  ILE n 
1 72  GLN n 
1 73  GLU n 
1 74  ARG n 
1 75  ASN n 
1 76  GLU n 
1 77  LYS n 
1 78  LEU n 
1 79  PHE n 
1 80  TYR n 
1 81  ARG n 
1 82  ILE n 
1 83  LEU n 
1 84  GLN n 
1 85  ASP n 
1 86  ASP n 
1 87  ILE n 
1 88  GLU n 
1 89  SER n 
1 90  LEU n 
1 91  MET n 
1 92  PRO n 
1 93  ILE n 
1 94  VAL n 
1 95  TYR n 
1 96  THR n 
1 97  PRO n 
1 98  THR n 
1 99  VAL n 
1 100 GLY n 
1 101 LEU n 
1 102 ALA n 
1 103 CSX n 
1 104 SER n 
1 105 GLN n 
1 106 TYR n 
1 107 GLY n 
1 108 HIS n 
1 109 ILE n 
1 110 PHE n 
1 111 ARG n 
1 112 ARG n 
1 113 PRO n 
1 114 LYS n 
1 115 GLY n 
1 116 LEU n 
1 117 PHE n 
1 118 ILE n 
1 119 SER n 
1 120 ILE n 
1 121 SER n 
1 122 ASP n 
1 123 ARG n 
1 124 GLY n 
1 125 HIS n 
1 126 VAL n 
1 127 ARG n 
1 128 SER n 
1 129 ILE n 
1 130 VAL n 
1 131 ASP n 
1 132 ASN n 
1 133 TRP n 
1 134 PRO n 
1 135 GLU n 
1 136 ASN n 
1 137 HIS n 
1 138 VAL n 
1 139 LYS n 
1 140 ALA n 
1 141 VAL n 
1 142 VAL n 
1 143 VAL n 
1 144 THR n 
1 145 ASP n 
1 146 GLY n 
1 147 GLU n 
1 148 ARG n 
1 149 ILE n 
1 150 LEU n 
1 151 GLY n 
1 152 LEU n 
1 153 GLY n 
1 154 ASP n 
1 155 LEU n 
1 156 GLY n 
1 157 VAL n 
1 158 TYR n 
1 159 GLY n 
1 160 MET n 
1 161 GLY n 
1 162 ILE n 
1 163 PRO n 
1 164 VAL n 
1 165 GLY n 
1 166 LYS n 
1 167 LEU n 
1 168 CYS n 
1 169 LEU n 
1 170 TYR n 
1 171 THR n 
1 172 ALA n 
1 173 CYS n 
1 174 ALA n 
1 175 GLY n 
1 176 ILE n 
1 177 ARG n 
1 178 PRO n 
1 179 ASP n 
1 180 ARG n 
1 181 CYS n 
1 182 LEU n 
1 183 PRO n 
1 184 VAL n 
1 185 CYS n 
1 186 ILE n 
1 187 ASP n 
1 188 VAL n 
1 189 GLY n 
1 190 THR n 
1 191 ASP n 
1 192 ASN n 
1 193 ILE n 
1 194 ALA n 
1 195 LEU n 
1 196 LEU n 
1 197 LYS n 
1 198 ASP n 
1 199 PRO n 
1 200 PHE n 
1 201 TYR n 
1 202 MET n 
1 203 GLY n 
1 204 LEU n 
1 205 TYR n 
1 206 GLN n 
1 207 LYS n 
1 208 ARG n 
1 209 ASP n 
1 210 ARG n 
1 211 THR n 
1 212 GLN n 
1 213 GLN n 
1 214 TYR n 
1 215 ASP n 
1 216 ASP n 
1 217 LEU n 
1 218 ILE n 
1 219 ASP n 
1 220 GLU n 
1 221 PHE n 
1 222 MET n 
1 223 LYS n 
1 224 ALA n 
1 225 ILE n 
1 226 THR n 
1 227 ASP n 
1 228 ARG n 
1 229 TYR n 
1 230 GLY n 
1 231 ARG n 
1 232 ASN n 
1 233 THR n 
1 234 LEU n 
1 235 ILE n 
1 236 GLN n 
1 237 PHE n 
1 238 GLU n 
1 239 ASP n 
1 240 PHE n 
1 241 GLY n 
1 242 ASN n 
1 243 HIS n 
1 244 ASN n 
1 245 ALA n 
1 246 PHE n 
1 247 ARG n 
1 248 PHE n 
1 249 LEU n 
1 250 ARG n 
1 251 LYS n 
1 252 TYR n 
1 253 ARG n 
1 254 GLU n 
1 255 LYS n 
1 256 TYR n 
1 257 CYS n 
1 258 THR n 
1 259 PHE n 
1 260 ASN n 
1 261 ASP n 
1 262 ASP n 
1 263 ILE n 
1 264 GLN n 
1 265 GLY n 
1 266 THR n 
1 267 ALA n 
1 268 ALA n 
1 269 VAL n 
1 270 ALA n 
1 271 LEU n 
1 272 ALA n 
1 273 GLY n 
1 274 LEU n 
1 275 LEU n 
1 276 ALA n 
1 277 ALA n 
1 278 GLN n 
1 279 LYS n 
1 280 VAL n 
1 281 ILE n 
1 282 SER n 
1 283 LYS n 
1 284 PRO n 
1 285 ILE n 
1 286 SER n 
1 287 GLU n 
1 288 HIS n 
1 289 LYS n 
1 290 ILE n 
1 291 LEU n 
1 292 PHE n 
1 293 LEU n 
1 294 GLY n 
1 295 ALA n 
1 296 GLY n 
1 297 GLU n 
1 298 ALA n 
1 299 ALA n 
1 300 LEU n 
1 301 GLY n 
1 302 ILE n 
1 303 ALA n 
1 304 ASN n 
1 305 LEU n 
1 306 ILE n 
1 307 VAL n 
1 308 MET n 
1 309 SER n 
1 310 MET n 
1 311 VAL n 
1 312 GLU n 
1 313 ASN n 
1 314 GLY n 
1 315 LEU n 
1 316 SER n 
1 317 GLU n 
1 318 GLN n 
1 319 GLU n 
1 320 ALA n 
1 321 GLN n 
1 322 LYS n 
1 323 LYS n 
1 324 ILE n 
1 325 TRP n 
1 326 MET n 
1 327 PHE n 
1 328 ASP n 
1 329 LYS n 
1 330 TYR n 
1 331 GLY n 
1 332 LEU n 
1 333 LEU n 
1 334 VAL n 
1 335 LYS n 
1 336 GLY n 
1 337 ARG n 
1 338 LYS n 
1 339 ALA n 
1 340 LYS n 
1 341 ILE n 
1 342 ASP n 
1 343 SER n 
1 344 TYR n 
1 345 GLN n 
1 346 GLU n 
1 347 PRO n 
1 348 PHE n 
1 349 THR n 
1 350 HIS n 
1 351 SER n 
1 352 ALA n 
1 353 PRO n 
1 354 GLU n 
1 355 SER n 
1 356 ILE n 
1 357 PRO n 
1 358 ASP n 
1 359 THR n 
1 360 PHE n 
1 361 GLU n 
1 362 ASP n 
1 363 ALA n 
1 364 VAL n 
1 365 ASN n 
1 366 ILE n 
1 367 LEU n 
1 368 LYS n 
1 369 PRO n 
1 370 SER n 
1 371 THR n 
1 372 ILE n 
1 373 ILE n 
1 374 GLY n 
1 375 VAL n 
1 376 ALA n 
1 377 GLY n 
1 378 ALA n 
1 379 GLY n 
1 380 ARG n 
1 381 LEU n 
1 382 PHE n 
1 383 THR n 
1 384 PRO n 
1 385 ASP n 
1 386 VAL n 
1 387 ILE n 
1 388 ARG n 
1 389 ALA n 
1 390 MET n 
1 391 ALA n 
1 392 SER n 
1 393 ILE n 
1 394 ASN n 
1 395 GLU n 
1 396 ARG n 
1 397 PRO n 
1 398 VAL n 
1 399 ILE n 
1 400 PHE n 
1 401 ALA n 
1 402 LEU n 
1 403 SER n 
1 404 ASN n 
1 405 PRO n 
1 406 THR n 
1 407 ALA n 
1 408 GLN n 
1 409 ALA n 
1 410 GLU n 
1 411 CYS n 
1 412 THR n 
1 413 ALA n 
1 414 GLU n 
1 415 GLU n 
1 416 ALA n 
1 417 TYR n 
1 418 THR n 
1 419 LEU n 
1 420 THR n 
1 421 GLU n 
1 422 GLY n 
1 423 ARG n 
1 424 CYS n 
1 425 LEU n 
1 426 PHE n 
1 427 ALA n 
1 428 SER n 
1 429 GLY n 
1 430 SER n 
1 431 PRO n 
1 432 PHE n 
1 433 GLY n 
1 434 PRO n 
1 435 VAL n 
1 436 LYS n 
1 437 LEU n 
1 438 THR n 
1 439 ASP n 
1 440 GLY n 
1 441 ARG n 
1 442 VAL n 
1 443 PHE n 
1 444 THR n 
1 445 PRO n 
1 446 GLY n 
1 447 GLN n 
1 448 GLY n 
1 449 ASN n 
1 450 ASN n 
1 451 VAL n 
1 452 TYR n 
1 453 ILE n 
1 454 PHE n 
1 455 PRO n 
1 456 GLY n 
1 457 VAL n 
1 458 ALA n 
1 459 LEU n 
1 460 ALA n 
1 461 VAL n 
1 462 ILE n 
1 463 LEU n 
1 464 CYS n 
1 465 ASN n 
1 466 THR n 
1 467 ARG n 
1 468 HIS n 
1 469 ILE n 
1 470 SER n 
1 471 ASP n 
1 472 SER n 
1 473 VAL n 
1 474 PHE n 
1 475 LEU n 
1 476 GLU n 
1 477 ALA n 
1 478 ALA n 
1 479 LYS n 
1 480 ALA n 
1 481 LEU n 
1 482 THR n 
1 483 SER n 
1 484 GLN n 
1 485 LEU n 
1 486 THR n 
1 487 ASP n 
1 488 GLU n 
1 489 GLU n 
1 490 LEU n 
1 491 ALA n 
1 492 GLN n 
1 493 GLY n 
1 494 ARG n 
1 495 LEU n 
1 496 TYR n 
1 497 PRO n 
1 498 PRO n 
1 499 LEU n 
1 500 ALA n 
1 501 ASN n 
1 502 ILE n 
1 503 GLN n 
1 504 GLU n 
1 505 VAL n 
1 506 SER n 
1 507 ILE n 
1 508 ASN n 
1 509 ILE n 
1 510 ALA n 
1 511 ILE n 
1 512 LYS n 
1 513 VAL n 
1 514 THR n 
1 515 GLU n 
1 516 TYR n 
1 517 LEU n 
1 518 TYR n 
1 519 ALA n 
1 520 ASN n 
1 521 LYS n 
1 522 MET n 
1 523 ALA n 
1 524 PHE n 
1 525 ARG n 
1 526 TYR n 
1 527 PRO n 
1 528 GLU n 
1 529 PRO n 
1 530 GLU n 
1 531 ASP n 
1 532 LYS n 
1 533 ALA n 
1 534 LYS n 
1 535 TYR n 
1 536 VAL n 
1 537 LYS n 
1 538 GLU n 
1 539 ARG n 
1 540 THR n 
1 541 TRP n 
1 542 ARG n 
1 543 SER n 
1 544 GLU n 
1 545 TYR n 
1 546 ASP n 
1 547 SER n 
1 548 LEU n 
1 549 LEU n 
1 550 PRO n 
1 551 ASP n 
1 552 VAL n 
1 553 TYR n 
1 554 GLU n 
1 555 TRP n 
1 556 PRO n 
1 557 GLU n 
1 558 SER n 
1 559 ALA n 
1 560 SER n 
1 561 SER n 
1 562 PRO n 
1 563 PRO n 
1 564 VAL n 
1 565 ILE n 
1 566 THR n 
1 567 GLU n 
1 568 LEU n 
1 569 GLU n 
1 570 HIS n 
1 571 HIS n 
1 572 HIS n 
1 573 HIS n 
1 574 HIS n 
1 575 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   575 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ME2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_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 
CL  non-polymer         . 'CHLORIDE ION'                    ?                 'Cl -1'             35.453  
CSX 'L-peptide linking' n 'S-OXY CYSTEINE'                  ?                 'C3 H7 N O3 S'      137.158 
CYS 'L-peptide linking' y CYSTEINE                          ?                 'C3 H7 N O2 S'      121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                    'ETHYLENE GLYCOL' 'C2 H6 O2'          62.068  
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  
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 
MG  non-polymer         . 'MAGNESIUM ION'                   ?                 'Mg 2'              24.305  
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ?                 'C21 H27 N7 O14 P2' 663.425 
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 
TLA non-polymer         . 'L(+)-TARTARIC ACID'              ?                 'C4 H6 O6'          150.087 
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   18  ?   ?   ?   A . n 
A 1 2   LEU 2   19  ?   ?   ?   A . n 
A 1 3   HIS 3   20  ?   ?   ?   A . n 
A 1 4   ILE 4   21  ?   ?   ?   A . n 
A 1 5   LYS 5   22  22  LYS LYS A . n 
A 1 6   GLU 6   23  23  GLU GLU A . n 
A 1 7   LYS 7   24  24  LYS LYS A . n 
A 1 8   GLY 8   25  25  GLY GLY A . n 
A 1 9   LYS 9   26  26  LYS LYS A . n 
A 1 10  PRO 10  27  27  PRO PRO A . n 
A 1 11  LEU 11  28  28  LEU LEU A . n 
A 1 12  MET 12  29  29  MET MET A . n 
A 1 13  LEU 13  30  30  LEU LEU A . n 
A 1 14  ASN 14  31  31  ASN ASN A . n 
A 1 15  PRO 15  32  32  PRO PRO A . n 
A 1 16  ARG 16  33  33  ARG ARG A . n 
A 1 17  THR 17  34  34  THR THR A . n 
A 1 18  ASN 18  35  35  ASN ASN A . n 
A 1 19  LYS 19  36  36  LYS LYS A . n 
A 1 20  GLY 20  37  37  GLY GLY A . n 
A 1 21  MET 21  38  38  MET MET A . n 
A 1 22  ALA 22  39  39  ALA ALA A . n 
A 1 23  PHE 23  40  40  PHE PHE A . n 
A 1 24  THR 24  41  41  THR THR A . n 
A 1 25  LEU 25  42  42  LEU LEU A . n 
A 1 26  GLN 26  43  43  GLN GLN A . n 
A 1 27  GLU 27  44  44  GLU GLU A . n 
A 1 28  ARG 28  45  45  ARG ARG A . n 
A 1 29  GLN 29  46  46  GLN GLN A . n 
A 1 30  MET 30  47  47  MET MET A . n 
A 1 31  LEU 31  48  48  LEU LEU A . n 
A 1 32  GLY 32  49  49  GLY GLY A . n 
A 1 33  LEU 33  50  50  LEU LEU A . n 
A 1 34  GLN 34  51  51  GLN GLN A . n 
A 1 35  GLY 35  52  52  GLY GLY A . n 
A 1 36  LEU 36  53  53  LEU LEU A . n 
A 1 37  LEU 37  54  54  LEU LEU A . n 
A 1 38  PRO 38  55  55  PRO PRO A . n 
A 1 39  PRO 39  56  56  PRO PRO A . n 
A 1 40  LYS 40  57  57  LYS LYS A . n 
A 1 41  ILE 41  58  58  ILE ILE A . n 
A 1 42  GLU 42  59  59  GLU GLU A . n 
A 1 43  THR 43  60  60  THR THR A . n 
A 1 44  GLN 44  61  61  GLN GLN A . n 
A 1 45  ASP 45  62  62  ASP ASP A . n 
A 1 46  ILE 46  63  63  ILE ILE A . n 
A 1 47  GLN 47  64  64  GLN GLN A . n 
A 1 48  ALA 48  65  65  ALA ALA A . n 
A 1 49  LEU 49  66  66  LEU LEU A . n 
A 1 50  ARG 50  67  67  ARG ARG A . n 
A 1 51  PHE 51  68  68  PHE PHE A . n 
A 1 52  HIS 52  69  69  HIS HIS A . n 
A 1 53  ARG 53  70  70  ARG ARG A . n 
A 1 54  ASN 54  71  71  ASN ASN A . n 
A 1 55  LEU 55  72  72  LEU LEU A . n 
A 1 56  LYS 56  73  73  LYS LYS A . n 
A 1 57  LYS 57  74  74  LYS LYS A . n 
A 1 58  MET 58  75  75  MET MET A . n 
A 1 59  THR 59  76  76  THR THR A . n 
A 1 60  SER 60  77  77  SER SER A . n 
A 1 61  PRO 61  78  78  PRO PRO A . n 
A 1 62  LEU 62  79  79  LEU LEU A . n 
A 1 63  GLU 63  80  80  GLU GLU A . n 
A 1 64  LYS 64  81  81  LYS LYS A . n 
A 1 65  TYR 65  82  82  TYR TYR A . n 
A 1 66  ILE 66  83  83  ILE ILE A . n 
A 1 67  TYR 67  84  84  TYR TYR A . n 
A 1 68  ILE 68  85  85  ILE ILE A . n 
A 1 69  MET 69  86  86  MET MET A . n 
A 1 70  GLY 70  87  87  GLY GLY A . n 
A 1 71  ILE 71  88  88  ILE ILE A . n 
A 1 72  GLN 72  89  89  GLN GLN A . n 
A 1 73  GLU 73  90  90  GLU GLU A . n 
A 1 74  ARG 74  91  91  ARG ARG A . n 
A 1 75  ASN 75  92  92  ASN ASN A . n 
A 1 76  GLU 76  93  93  GLU GLU A . n 
A 1 77  LYS 77  94  94  LYS LYS A . n 
A 1 78  LEU 78  95  95  LEU LEU A . n 
A 1 79  PHE 79  96  96  PHE PHE A . n 
A 1 80  TYR 80  97  97  TYR TYR A . n 
A 1 81  ARG 81  98  98  ARG ARG A . n 
A 1 82  ILE 82  99  99  ILE ILE A . n 
A 1 83  LEU 83  100 100 LEU LEU A . n 
A 1 84  GLN 84  101 101 GLN GLN A . n 
A 1 85  ASP 85  102 102 ASP ASP A . n 
A 1 86  ASP 86  103 103 ASP ASP A . n 
A 1 87  ILE 87  104 104 ILE ILE A . n 
A 1 88  GLU 88  105 105 GLU GLU A . n 
A 1 89  SER 89  106 106 SER SER A . n 
A 1 90  LEU 90  107 107 LEU LEU A . n 
A 1 91  MET 91  108 108 MET MET A . n 
A 1 92  PRO 92  109 109 PRO PRO A . n 
A 1 93  ILE 93  110 110 ILE ILE A . n 
A 1 94  VAL 94  111 111 VAL VAL A . n 
A 1 95  TYR 95  112 112 TYR TYR A . n 
A 1 96  THR 96  113 113 THR THR A . n 
A 1 97  PRO 97  114 114 PRO PRO A . n 
A 1 98  THR 98  115 115 THR THR A . n 
A 1 99  VAL 99  116 116 VAL VAL A . n 
A 1 100 GLY 100 117 117 GLY GLY A . n 
A 1 101 LEU 101 118 118 LEU LEU A . n 
A 1 102 ALA 102 119 119 ALA ALA A . n 
A 1 103 CSX 103 120 120 CSX CSX A . n 
A 1 104 SER 104 121 121 SER SER A . n 
A 1 105 GLN 105 122 122 GLN GLN A . n 
A 1 106 TYR 106 123 123 TYR TYR A . n 
A 1 107 GLY 107 124 124 GLY GLY A . n 
A 1 108 HIS 108 125 125 HIS HIS A . n 
A 1 109 ILE 109 126 126 ILE ILE A . n 
A 1 110 PHE 110 127 127 PHE PHE A . n 
A 1 111 ARG 111 128 128 ARG ARG A . n 
A 1 112 ARG 112 129 129 ARG ARG A . n 
A 1 113 PRO 113 130 130 PRO PRO A . n 
A 1 114 LYS 114 131 131 LYS LYS A . n 
A 1 115 GLY 115 132 132 GLY GLY A . n 
A 1 116 LEU 116 133 133 LEU LEU A . n 
A 1 117 PHE 117 134 134 PHE PHE A . n 
A 1 118 ILE 118 135 135 ILE ILE A . n 
A 1 119 SER 119 136 136 SER SER A . n 
A 1 120 ILE 120 137 137 ILE ILE A . n 
A 1 121 SER 121 138 138 SER SER A . n 
A 1 122 ASP 122 139 139 ASP ASP A . n 
A 1 123 ARG 123 140 140 ARG ARG A . n 
A 1 124 GLY 124 141 141 GLY GLY A . n 
A 1 125 HIS 125 142 142 HIS HIS A . n 
A 1 126 VAL 126 143 143 VAL VAL A . n 
A 1 127 ARG 127 144 144 ARG ARG A . n 
A 1 128 SER 128 145 145 SER SER A . n 
A 1 129 ILE 129 146 146 ILE ILE A . n 
A 1 130 VAL 130 147 147 VAL VAL A . n 
A 1 131 ASP 131 148 148 ASP ASP A . n 
A 1 132 ASN 132 149 149 ASN ASN A . n 
A 1 133 TRP 133 150 150 TRP TRP A . n 
A 1 134 PRO 134 151 151 PRO PRO A . n 
A 1 135 GLU 135 152 152 GLU GLU A . n 
A 1 136 ASN 136 153 153 ASN ASN A . n 
A 1 137 HIS 137 154 154 HIS HIS A . n 
A 1 138 VAL 138 155 155 VAL VAL A . n 
A 1 139 LYS 139 156 156 LYS LYS A . n 
A 1 140 ALA 140 157 157 ALA ALA A . n 
A 1 141 VAL 141 158 158 VAL VAL A . n 
A 1 142 VAL 142 159 159 VAL VAL A . n 
A 1 143 VAL 143 160 160 VAL VAL A . n 
A 1 144 THR 144 161 161 THR THR A . n 
A 1 145 ASP 145 162 162 ASP ASP A . n 
A 1 146 GLY 146 163 163 GLY GLY A . n 
A 1 147 GLU 147 164 164 GLU GLU A . n 
A 1 148 ARG 148 165 165 ARG ARG A . n 
A 1 149 ILE 149 166 166 ILE ILE A . n 
A 1 150 LEU 150 167 167 LEU LEU A . n 
A 1 151 GLY 151 168 168 GLY GLY A . n 
A 1 152 LEU 152 169 169 LEU LEU A . n 
A 1 153 GLY 153 170 170 GLY GLY A . n 
A 1 154 ASP 154 171 171 ASP ASP A . n 
A 1 155 LEU 155 172 172 LEU LEU A . n 
A 1 156 GLY 156 173 173 GLY GLY A . n 
A 1 157 VAL 157 174 174 VAL VAL A . n 
A 1 158 TYR 158 175 175 TYR TYR A . n 
A 1 159 GLY 159 176 176 GLY GLY A . n 
A 1 160 MET 160 177 177 MET MET A . n 
A 1 161 GLY 161 178 178 GLY GLY A . n 
A 1 162 ILE 162 179 179 ILE ILE A . n 
A 1 163 PRO 163 180 180 PRO PRO A . n 
A 1 164 VAL 164 181 181 VAL VAL A . n 
A 1 165 GLY 165 182 182 GLY GLY A . n 
A 1 166 LYS 166 183 183 LYS LYS A . n 
A 1 167 LEU 167 184 184 LEU LEU A . n 
A 1 168 CYS 168 185 185 CYS CYS A . n 
A 1 169 LEU 169 186 186 LEU LEU A . n 
A 1 170 TYR 170 187 187 TYR TYR A . n 
A 1 171 THR 171 188 188 THR THR A . n 
A 1 172 ALA 172 189 189 ALA ALA A . n 
A 1 173 CYS 173 190 190 CYS CYS A . n 
A 1 174 ALA 174 191 191 ALA ALA A . n 
A 1 175 GLY 175 192 192 GLY GLY A . n 
A 1 176 ILE 176 193 193 ILE ILE A . n 
A 1 177 ARG 177 194 194 ARG ARG A . n 
A 1 178 PRO 178 195 195 PRO PRO A . n 
A 1 179 ASP 179 196 196 ASP ASP A . n 
A 1 180 ARG 180 197 197 ARG ARG A . n 
A 1 181 CYS 181 198 198 CYS CYS A . n 
A 1 182 LEU 182 199 199 LEU LEU A . n 
A 1 183 PRO 183 200 200 PRO PRO A . n 
A 1 184 VAL 184 201 201 VAL VAL A . n 
A 1 185 CYS 185 202 202 CYS CYS A . n 
A 1 186 ILE 186 203 203 ILE ILE A . n 
A 1 187 ASP 187 204 204 ASP ASP A . n 
A 1 188 VAL 188 205 205 VAL VAL A . n 
A 1 189 GLY 189 206 206 GLY GLY A . n 
A 1 190 THR 190 207 207 THR THR A . n 
A 1 191 ASP 191 208 208 ASP ASP A . n 
A 1 192 ASN 192 209 209 ASN ASN A . n 
A 1 193 ILE 193 210 210 ILE ILE A . n 
A 1 194 ALA 194 211 211 ALA ALA A . n 
A 1 195 LEU 195 212 212 LEU LEU A . n 
A 1 196 LEU 196 213 213 LEU LEU A . n 
A 1 197 LYS 197 214 214 LYS LYS A . n 
A 1 198 ASP 198 215 215 ASP ASP A . n 
A 1 199 PRO 199 216 216 PRO PRO A . n 
A 1 200 PHE 200 217 217 PHE PHE A . n 
A 1 201 TYR 201 218 218 TYR TYR A . n 
A 1 202 MET 202 219 219 MET MET A . n 
A 1 203 GLY 203 220 220 GLY GLY A . n 
A 1 204 LEU 204 221 221 LEU LEU A . n 
A 1 205 TYR 205 222 222 TYR TYR A . n 
A 1 206 GLN 206 223 223 GLN GLN A . n 
A 1 207 LYS 207 224 224 LYS LYS A . n 
A 1 208 ARG 208 225 225 ARG ARG A . n 
A 1 209 ASP 209 226 226 ASP ASP A . n 
A 1 210 ARG 210 227 227 ARG ARG A . n 
A 1 211 THR 211 228 228 THR THR A . n 
A 1 212 GLN 212 229 229 GLN GLN A . n 
A 1 213 GLN 213 230 230 GLN GLN A . n 
A 1 214 TYR 214 231 231 TYR TYR A . n 
A 1 215 ASP 215 232 232 ASP ASP A . n 
A 1 216 ASP 216 233 233 ASP ASP A . n 
A 1 217 LEU 217 234 234 LEU LEU A . n 
A 1 218 ILE 218 235 235 ILE ILE A . n 
A 1 219 ASP 219 236 236 ASP ASP A . n 
A 1 220 GLU 220 237 237 GLU GLU A . n 
A 1 221 PHE 221 238 238 PHE PHE A . n 
A 1 222 MET 222 239 239 MET MET A . n 
A 1 223 LYS 223 240 240 LYS LYS A . n 
A 1 224 ALA 224 241 241 ALA ALA A . n 
A 1 225 ILE 225 242 242 ILE ILE A . n 
A 1 226 THR 226 243 243 THR THR A . n 
A 1 227 ASP 227 244 244 ASP ASP A . n 
A 1 228 ARG 228 245 245 ARG ARG A . n 
A 1 229 TYR 229 246 246 TYR TYR A . n 
A 1 230 GLY 230 247 247 GLY GLY A . n 
A 1 231 ARG 231 248 248 ARG ARG A . n 
A 1 232 ASN 232 249 249 ASN ASN A . n 
A 1 233 THR 233 250 250 THR THR A . n 
A 1 234 LEU 234 251 251 LEU LEU A . n 
A 1 235 ILE 235 252 252 ILE ILE A . n 
A 1 236 GLN 236 253 253 GLN GLN A . n 
A 1 237 PHE 237 254 254 PHE PHE A . n 
A 1 238 GLU 238 255 255 GLU GLU A . n 
A 1 239 ASP 239 256 256 ASP ASP A . n 
A 1 240 PHE 240 257 257 PHE PHE A . n 
A 1 241 GLY 241 258 258 GLY GLY A . n 
A 1 242 ASN 242 259 259 ASN ASN A . n 
A 1 243 HIS 243 260 260 HIS HIS A . n 
A 1 244 ASN 244 261 261 ASN ASN A . n 
A 1 245 ALA 245 262 262 ALA ALA A . n 
A 1 246 PHE 246 263 263 PHE PHE A . n 
A 1 247 ARG 247 264 264 ARG ARG A . n 
A 1 248 PHE 248 265 265 PHE PHE A . n 
A 1 249 LEU 249 266 266 LEU LEU A . n 
A 1 250 ARG 250 267 267 ARG ARG A . n 
A 1 251 LYS 251 268 268 LYS LYS A . n 
A 1 252 TYR 252 269 269 TYR TYR A . n 
A 1 253 ARG 253 270 270 ARG ARG A . n 
A 1 254 GLU 254 271 271 GLU GLU A . n 
A 1 255 LYS 255 272 272 LYS LYS A . n 
A 1 256 TYR 256 273 273 TYR TYR A . n 
A 1 257 CYS 257 274 274 CYS CYS A . n 
A 1 258 THR 258 275 275 THR THR A . n 
A 1 259 PHE 259 276 276 PHE PHE A . n 
A 1 260 ASN 260 277 277 ASN ASN A . n 
A 1 261 ASP 261 278 278 ASP ASP A . n 
A 1 262 ASP 262 279 279 ASP ASP A . n 
A 1 263 ILE 263 280 280 ILE ILE A . n 
A 1 264 GLN 264 281 281 GLN GLN A . n 
A 1 265 GLY 265 282 282 GLY GLY A . n 
A 1 266 THR 266 283 283 THR THR A . n 
A 1 267 ALA 267 284 284 ALA ALA A . n 
A 1 268 ALA 268 285 285 ALA ALA A . n 
A 1 269 VAL 269 286 286 VAL VAL A . n 
A 1 270 ALA 270 287 287 ALA ALA A . n 
A 1 271 LEU 271 288 288 LEU LEU A . n 
A 1 272 ALA 272 289 289 ALA ALA A . n 
A 1 273 GLY 273 290 290 GLY GLY A . n 
A 1 274 LEU 274 291 291 LEU LEU A . n 
A 1 275 LEU 275 292 292 LEU LEU A . n 
A 1 276 ALA 276 293 293 ALA ALA A . n 
A 1 277 ALA 277 294 294 ALA ALA A . n 
A 1 278 GLN 278 295 295 GLN GLN A . n 
A 1 279 LYS 279 296 296 LYS LYS A . n 
A 1 280 VAL 280 297 297 VAL VAL A . n 
A 1 281 ILE 281 298 298 ILE ILE A . n 
A 1 282 SER 282 299 299 SER SER A . n 
A 1 283 LYS 283 300 300 LYS LYS A . n 
A 1 284 PRO 284 301 301 PRO PRO A . n 
A 1 285 ILE 285 302 302 ILE ILE A . n 
A 1 286 SER 286 303 303 SER SER A . n 
A 1 287 GLU 287 304 304 GLU GLU A . n 
A 1 288 HIS 288 305 305 HIS HIS A . n 
A 1 289 LYS 289 306 306 LYS LYS A . n 
A 1 290 ILE 290 307 307 ILE ILE A . n 
A 1 291 LEU 291 308 308 LEU LEU A . n 
A 1 292 PHE 292 309 309 PHE PHE A . n 
A 1 293 LEU 293 310 310 LEU LEU A . n 
A 1 294 GLY 294 311 311 GLY GLY A . n 
A 1 295 ALA 295 312 312 ALA ALA A . n 
A 1 296 GLY 296 313 313 GLY GLY A . n 
A 1 297 GLU 297 314 314 GLU GLU A . n 
A 1 298 ALA 298 315 315 ALA ALA A . n 
A 1 299 ALA 299 316 316 ALA ALA A . n 
A 1 300 LEU 300 317 317 LEU LEU A . n 
A 1 301 GLY 301 318 318 GLY GLY A . n 
A 1 302 ILE 302 319 319 ILE ILE A . n 
A 1 303 ALA 303 320 320 ALA ALA A . n 
A 1 304 ASN 304 321 321 ASN ASN A . n 
A 1 305 LEU 305 322 322 LEU LEU A . n 
A 1 306 ILE 306 323 323 ILE ILE A . n 
A 1 307 VAL 307 324 324 VAL VAL A . n 
A 1 308 MET 308 325 325 MET MET A . n 
A 1 309 SER 309 326 326 SER SER A . n 
A 1 310 MET 310 327 327 MET MET A . n 
A 1 311 VAL 311 328 328 VAL VAL A . n 
A 1 312 GLU 312 329 329 GLU GLU A . n 
A 1 313 ASN 313 330 330 ASN ASN A . n 
A 1 314 GLY 314 331 331 GLY GLY A . n 
A 1 315 LEU 315 332 332 LEU LEU A . n 
A 1 316 SER 316 333 333 SER SER A . n 
A 1 317 GLU 317 334 334 GLU GLU A . n 
A 1 318 GLN 318 335 335 GLN GLN A . n 
A 1 319 GLU 319 336 336 GLU GLU A . n 
A 1 320 ALA 320 337 337 ALA ALA A . n 
A 1 321 GLN 321 338 338 GLN GLN A . n 
A 1 322 LYS 322 339 339 LYS LYS A . n 
A 1 323 LYS 323 340 340 LYS LYS A . n 
A 1 324 ILE 324 341 341 ILE ILE A . n 
A 1 325 TRP 325 342 342 TRP TRP A . n 
A 1 326 MET 326 343 343 MET MET A . n 
A 1 327 PHE 327 344 344 PHE PHE A . n 
A 1 328 ASP 328 345 345 ASP ASP A . n 
A 1 329 LYS 329 346 346 LYS LYS A . n 
A 1 330 TYR 330 347 347 TYR TYR A . n 
A 1 331 GLY 331 348 348 GLY GLY A . n 
A 1 332 LEU 332 349 349 LEU LEU A . n 
A 1 333 LEU 333 350 350 LEU LEU A . n 
A 1 334 VAL 334 351 351 VAL VAL A . n 
A 1 335 LYS 335 352 352 LYS LYS A . n 
A 1 336 GLY 336 353 353 GLY GLY A . n 
A 1 337 ARG 337 354 354 ARG ARG A . n 
A 1 338 LYS 338 355 355 LYS LYS A . n 
A 1 339 ALA 339 356 356 ALA ALA A . n 
A 1 340 LYS 340 357 357 LYS LYS A . n 
A 1 341 ILE 341 358 358 ILE ILE A . n 
A 1 342 ASP 342 359 359 ASP ASP A . n 
A 1 343 SER 343 360 360 SER SER A . n 
A 1 344 TYR 344 361 361 TYR TYR A . n 
A 1 345 GLN 345 362 362 GLN GLN A . n 
A 1 346 GLU 346 363 363 GLU GLU A . n 
A 1 347 PRO 347 364 364 PRO PRO A . n 
A 1 348 PHE 348 365 365 PHE PHE A . n 
A 1 349 THR 349 366 366 THR THR A . n 
A 1 350 HIS 350 367 367 HIS HIS A . n 
A 1 351 SER 351 368 368 SER SER A . n 
A 1 352 ALA 352 369 369 ALA ALA A . n 
A 1 353 PRO 353 370 370 PRO PRO A . n 
A 1 354 GLU 354 371 371 GLU GLU A . n 
A 1 355 SER 355 372 372 SER SER A . n 
A 1 356 ILE 356 373 373 ILE ILE A . n 
A 1 357 PRO 357 374 374 PRO PRO A . n 
A 1 358 ASP 358 375 375 ASP ASP A . n 
A 1 359 THR 359 376 376 THR THR A . n 
A 1 360 PHE 360 377 377 PHE PHE A . n 
A 1 361 GLU 361 378 378 GLU GLU A . n 
A 1 362 ASP 362 379 379 ASP ASP A . n 
A 1 363 ALA 363 380 380 ALA ALA A . n 
A 1 364 VAL 364 381 381 VAL VAL A . n 
A 1 365 ASN 365 382 382 ASN ASN A . n 
A 1 366 ILE 366 383 383 ILE ILE A . n 
A 1 367 LEU 367 384 384 LEU LEU A . n 
A 1 368 LYS 368 385 385 LYS LYS A . n 
A 1 369 PRO 369 386 386 PRO PRO A . n 
A 1 370 SER 370 387 387 SER SER A . n 
A 1 371 THR 371 388 388 THR THR A . n 
A 1 372 ILE 372 389 389 ILE ILE A . n 
A 1 373 ILE 373 390 390 ILE ILE A . n 
A 1 374 GLY 374 391 391 GLY GLY A . n 
A 1 375 VAL 375 392 392 VAL VAL A . n 
A 1 376 ALA 376 393 393 ALA ALA A . n 
A 1 377 GLY 377 394 394 GLY GLY A . n 
A 1 378 ALA 378 395 395 ALA ALA A . n 
A 1 379 GLY 379 396 396 GLY GLY A . n 
A 1 380 ARG 380 397 397 ARG ARG A . n 
A 1 381 LEU 381 398 398 LEU LEU A . n 
A 1 382 PHE 382 399 399 PHE PHE A . n 
A 1 383 THR 383 400 400 THR THR A . n 
A 1 384 PRO 384 401 401 PRO PRO A . n 
A 1 385 ASP 385 402 402 ASP ASP A . n 
A 1 386 VAL 386 403 403 VAL VAL A . n 
A 1 387 ILE 387 404 404 ILE ILE A . n 
A 1 388 ARG 388 405 405 ARG ARG A . n 
A 1 389 ALA 389 406 406 ALA ALA A . n 
A 1 390 MET 390 407 407 MET MET A . n 
A 1 391 ALA 391 408 408 ALA ALA A . n 
A 1 392 SER 392 409 409 SER SER A . n 
A 1 393 ILE 393 410 410 ILE ILE A . n 
A 1 394 ASN 394 411 411 ASN ASN A . n 
A 1 395 GLU 395 412 412 GLU GLU A . n 
A 1 396 ARG 396 413 413 ARG ARG A . n 
A 1 397 PRO 397 414 414 PRO PRO A . n 
A 1 398 VAL 398 415 415 VAL VAL A . n 
A 1 399 ILE 399 416 416 ILE ILE A . n 
A 1 400 PHE 400 417 417 PHE PHE A . n 
A 1 401 ALA 401 418 418 ALA ALA A . n 
A 1 402 LEU 402 419 419 LEU LEU A . n 
A 1 403 SER 403 420 420 SER SER A . n 
A 1 404 ASN 404 421 421 ASN ASN A . n 
A 1 405 PRO 405 422 422 PRO PRO A . n 
A 1 406 THR 406 423 423 THR THR A . n 
A 1 407 ALA 407 424 424 ALA ALA A . n 
A 1 408 GLN 408 425 425 GLN GLN A . n 
A 1 409 ALA 409 426 426 ALA ALA A . n 
A 1 410 GLU 410 427 427 GLU GLU A . n 
A 1 411 CYS 411 428 428 CYS CYS A . n 
A 1 412 THR 412 429 429 THR THR A . n 
A 1 413 ALA 413 430 430 ALA ALA A . n 
A 1 414 GLU 414 431 431 GLU GLU A . n 
A 1 415 GLU 415 432 432 GLU GLU A . n 
A 1 416 ALA 416 433 433 ALA ALA A . n 
A 1 417 TYR 417 434 434 TYR TYR A . n 
A 1 418 THR 418 435 435 THR THR A . n 
A 1 419 LEU 419 436 436 LEU LEU A . n 
A 1 420 THR 420 437 437 THR THR A . n 
A 1 421 GLU 421 438 438 GLU GLU A . n 
A 1 422 GLY 422 439 439 GLY GLY A . n 
A 1 423 ARG 423 440 440 ARG ARG A . n 
A 1 424 CYS 424 441 441 CYS CYS A . n 
A 1 425 LEU 425 442 442 LEU LEU A . n 
A 1 426 PHE 426 443 443 PHE PHE A . n 
A 1 427 ALA 427 444 444 ALA ALA A . n 
A 1 428 SER 428 445 445 SER SER A . n 
A 1 429 GLY 429 446 446 GLY GLY A . n 
A 1 430 SER 430 447 447 SER SER A . n 
A 1 431 PRO 431 448 448 PRO PRO A . n 
A 1 432 PHE 432 449 449 PHE PHE A . n 
A 1 433 GLY 433 450 450 GLY GLY A . n 
A 1 434 PRO 434 451 451 PRO PRO A . n 
A 1 435 VAL 435 452 452 VAL VAL A . n 
A 1 436 LYS 436 453 453 LYS LYS A . n 
A 1 437 LEU 437 454 454 LEU LEU A . n 
A 1 438 THR 438 455 455 THR THR A . n 
A 1 439 ASP 439 456 456 ASP ASP A . n 
A 1 440 GLY 440 457 457 GLY GLY A . n 
A 1 441 ARG 441 458 458 ARG ARG A . n 
A 1 442 VAL 442 459 459 VAL VAL A . n 
A 1 443 PHE 443 460 460 PHE PHE A . n 
A 1 444 THR 444 461 461 THR THR A . n 
A 1 445 PRO 445 462 462 PRO PRO A . n 
A 1 446 GLY 446 463 463 GLY GLY A . n 
A 1 447 GLN 447 464 464 GLN GLN A . n 
A 1 448 GLY 448 465 465 GLY GLY A . n 
A 1 449 ASN 449 466 466 ASN ASN A . n 
A 1 450 ASN 450 467 467 ASN ASN A . n 
A 1 451 VAL 451 468 468 VAL VAL A . n 
A 1 452 TYR 452 469 469 TYR TYR A . n 
A 1 453 ILE 453 470 470 ILE ILE A . n 
A 1 454 PHE 454 471 471 PHE PHE A . n 
A 1 455 PRO 455 472 472 PRO PRO A . n 
A 1 456 GLY 456 473 473 GLY GLY A . n 
A 1 457 VAL 457 474 474 VAL VAL A . n 
A 1 458 ALA 458 475 475 ALA ALA A . n 
A 1 459 LEU 459 476 476 LEU LEU A . n 
A 1 460 ALA 460 477 477 ALA ALA A . n 
A 1 461 VAL 461 478 478 VAL VAL A . n 
A 1 462 ILE 462 479 479 ILE ILE A . n 
A 1 463 LEU 463 480 480 LEU LEU A . n 
A 1 464 CYS 464 481 481 CYS CYS A . n 
A 1 465 ASN 465 482 482 ASN ASN A . n 
A 1 466 THR 466 483 483 THR THR A . n 
A 1 467 ARG 467 484 484 ARG ARG A . n 
A 1 468 HIS 468 485 485 HIS HIS A . n 
A 1 469 ILE 469 486 486 ILE ILE A . n 
A 1 470 SER 470 487 487 SER SER A . n 
A 1 471 ASP 471 488 488 ASP ASP A . n 
A 1 472 SER 472 489 489 SER SER A . n 
A 1 473 VAL 473 490 490 VAL VAL A . n 
A 1 474 PHE 474 491 491 PHE PHE A . n 
A 1 475 LEU 475 492 492 LEU LEU A . n 
A 1 476 GLU 476 493 493 GLU GLU A . n 
A 1 477 ALA 477 494 494 ALA ALA A . n 
A 1 478 ALA 478 495 495 ALA ALA A . n 
A 1 479 LYS 479 496 496 LYS LYS A . n 
A 1 480 ALA 480 497 497 ALA ALA A . n 
A 1 481 LEU 481 498 498 LEU LEU A . n 
A 1 482 THR 482 499 499 THR THR A . n 
A 1 483 SER 483 500 500 SER SER A . n 
A 1 484 GLN 484 501 501 GLN GLN A . n 
A 1 485 LEU 485 502 502 LEU LEU A . n 
A 1 486 THR 486 503 503 THR THR A . n 
A 1 487 ASP 487 504 504 ASP ASP A . n 
A 1 488 GLU 488 505 505 GLU GLU A . n 
A 1 489 GLU 489 506 506 GLU GLU A . n 
A 1 490 LEU 490 507 507 LEU LEU A . n 
A 1 491 ALA 491 508 508 ALA ALA A . n 
A 1 492 GLN 492 509 509 GLN GLN A . n 
A 1 493 GLY 493 510 510 GLY GLY A . n 
A 1 494 ARG 494 511 511 ARG ARG A . n 
A 1 495 LEU 495 512 512 LEU LEU A . n 
A 1 496 TYR 496 513 513 TYR TYR A . n 
A 1 497 PRO 497 514 514 PRO PRO A . n 
A 1 498 PRO 498 515 515 PRO PRO A . n 
A 1 499 LEU 499 516 516 LEU LEU A . n 
A 1 500 ALA 500 517 517 ALA ALA A . n 
A 1 501 ASN 501 518 518 ASN ASN A . n 
A 1 502 ILE 502 519 519 ILE ILE A . n 
A 1 503 GLN 503 520 520 GLN GLN A . n 
A 1 504 GLU 504 521 521 GLU GLU A . n 
A 1 505 VAL 505 522 522 VAL VAL A . n 
A 1 506 SER 506 523 523 SER SER A . n 
A 1 507 ILE 507 524 524 ILE ILE A . n 
A 1 508 ASN 508 525 525 ASN ASN A . n 
A 1 509 ILE 509 526 526 ILE ILE A . n 
A 1 510 ALA 510 527 527 ALA ALA A . n 
A 1 511 ILE 511 528 528 ILE ILE A . n 
A 1 512 LYS 512 529 529 LYS LYS A . n 
A 1 513 VAL 513 530 530 VAL VAL A . n 
A 1 514 THR 514 531 531 THR THR A . n 
A 1 515 GLU 515 532 532 GLU GLU A . n 
A 1 516 TYR 516 533 533 TYR TYR A . n 
A 1 517 LEU 517 534 534 LEU LEU A . n 
A 1 518 TYR 518 535 535 TYR TYR A . n 
A 1 519 ALA 519 536 536 ALA ALA A . n 
A 1 520 ASN 520 537 537 ASN ASN A . n 
A 1 521 LYS 521 538 538 LYS LYS A . n 
A 1 522 MET 522 539 539 MET MET A . n 
A 1 523 ALA 523 540 540 ALA ALA A . n 
A 1 524 PHE 524 541 541 PHE PHE A . n 
A 1 525 ARG 525 542 542 ARG ARG A . n 
A 1 526 TYR 526 543 543 TYR TYR A . n 
A 1 527 PRO 527 544 544 PRO PRO A . n 
A 1 528 GLU 528 545 545 GLU GLU A . n 
A 1 529 PRO 529 546 546 PRO PRO A . n 
A 1 530 GLU 530 547 547 GLU GLU A . n 
A 1 531 ASP 531 548 548 ASP ASP A . n 
A 1 532 LYS 532 549 549 LYS LYS A . n 
A 1 533 ALA 533 550 550 ALA ALA A . n 
A 1 534 LYS 534 551 551 LYS LYS A . n 
A 1 535 TYR 535 552 552 TYR TYR A . n 
A 1 536 VAL 536 553 553 VAL VAL A . n 
A 1 537 LYS 537 554 554 LYS LYS A . n 
A 1 538 GLU 538 555 555 GLU GLU A . n 
A 1 539 ARG 539 556 556 ARG ARG A . n 
A 1 540 THR 540 557 557 THR THR A . n 
A 1 541 TRP 541 558 558 TRP TRP A . n 
A 1 542 ARG 542 559 559 ARG ARG A . n 
A 1 543 SER 543 560 560 SER SER A . n 
A 1 544 GLU 544 561 561 GLU GLU A . n 
A 1 545 TYR 545 562 562 TYR TYR A . n 
A 1 546 ASP 546 563 563 ASP ASP A . n 
A 1 547 SER 547 564 564 SER SER A . n 
A 1 548 LEU 548 565 565 LEU LEU A . n 
A 1 549 LEU 549 566 566 LEU LEU A . n 
A 1 550 PRO 550 567 567 PRO PRO A . n 
A 1 551 ASP 551 568 568 ASP ASP A . n 
A 1 552 VAL 552 569 569 VAL VAL A . n 
A 1 553 TYR 553 570 570 TYR TYR A . n 
A 1 554 GLU 554 571 571 GLU GLU A . n 
A 1 555 TRP 555 572 572 TRP TRP A . n 
A 1 556 PRO 556 573 573 PRO PRO A . n 
A 1 557 GLU 557 574 574 GLU GLU A . n 
A 1 558 SER 558 575 ?   ?   ?   A . n 
A 1 559 ALA 559 576 ?   ?   ?   A . n 
A 1 560 SER 560 577 ?   ?   ?   A . n 
A 1 561 SER 561 578 578 SER SER A . n 
A 1 562 PRO 562 579 579 PRO PRO A . n 
A 1 563 PRO 563 580 580 PRO PRO A . n 
A 1 564 VAL 564 581 ?   ?   ?   A . n 
A 1 565 ILE 565 582 ?   ?   ?   A . n 
A 1 566 THR 566 583 ?   ?   ?   A . n 
A 1 567 GLU 567 584 ?   ?   ?   A . n 
A 1 568 LEU 568 585 ?   ?   ?   A . n 
A 1 569 GLU 569 586 ?   ?   ?   A . n 
A 1 570 HIS 570 587 ?   ?   ?   A . n 
A 1 571 HIS 571 588 ?   ?   ?   A . n 
A 1 572 HIS 572 589 ?   ?   ?   A . n 
A 1 573 HIS 573 590 ?   ?   ?   A . n 
A 1 574 HIS 574 591 ?   ?   ?   A . n 
A 1 575 HIS 575 592 ?   ?   ?   A . n 
B 1 1   MET 1   18  ?   ?   ?   B . n 
B 1 2   LEU 2   19  ?   ?   ?   B . n 
B 1 3   HIS 3   20  ?   ?   ?   B . n 
B 1 4   ILE 4   21  ?   ?   ?   B . n 
B 1 5   LYS 5   22  ?   ?   ?   B . n 
B 1 6   GLU 6   23  23  GLU GLU B . n 
B 1 7   LYS 7   24  24  LYS LYS B . n 
B 1 8   GLY 8   25  25  GLY GLY B . n 
B 1 9   LYS 9   26  26  LYS LYS B . n 
B 1 10  PRO 10  27  27  PRO PRO B . n 
B 1 11  LEU 11  28  28  LEU LEU B . n 
B 1 12  MET 12  29  29  MET MET B . n 
B 1 13  LEU 13  30  30  LEU LEU B . n 
B 1 14  ASN 14  31  31  ASN ASN B . n 
B 1 15  PRO 15  32  32  PRO PRO B . n 
B 1 16  ARG 16  33  33  ARG ARG B . n 
B 1 17  THR 17  34  34  THR THR B . n 
B 1 18  ASN 18  35  35  ASN ASN B . n 
B 1 19  LYS 19  36  36  LYS LYS B . n 
B 1 20  GLY 20  37  37  GLY GLY B . n 
B 1 21  MET 21  38  38  MET MET B . n 
B 1 22  ALA 22  39  39  ALA ALA B . n 
B 1 23  PHE 23  40  40  PHE PHE B . n 
B 1 24  THR 24  41  41  THR THR B . n 
B 1 25  LEU 25  42  42  LEU LEU B . n 
B 1 26  GLN 26  43  43  GLN GLN B . n 
B 1 27  GLU 27  44  44  GLU GLU B . n 
B 1 28  ARG 28  45  45  ARG ARG B . n 
B 1 29  GLN 29  46  46  GLN GLN B . n 
B 1 30  MET 30  47  47  MET MET B . n 
B 1 31  LEU 31  48  48  LEU LEU B . n 
B 1 32  GLY 32  49  49  GLY GLY B . n 
B 1 33  LEU 33  50  50  LEU LEU B . n 
B 1 34  GLN 34  51  51  GLN GLN B . n 
B 1 35  GLY 35  52  52  GLY GLY B . n 
B 1 36  LEU 36  53  53  LEU LEU B . n 
B 1 37  LEU 37  54  54  LEU LEU B . n 
B 1 38  PRO 38  55  55  PRO PRO B . n 
B 1 39  PRO 39  56  56  PRO PRO B . n 
B 1 40  LYS 40  57  57  LYS LYS B . n 
B 1 41  ILE 41  58  58  ILE ILE B . n 
B 1 42  GLU 42  59  59  GLU GLU B . n 
B 1 43  THR 43  60  60  THR THR B . n 
B 1 44  GLN 44  61  61  GLN GLN B . n 
B 1 45  ASP 45  62  62  ASP ASP B . n 
B 1 46  ILE 46  63  63  ILE ILE B . n 
B 1 47  GLN 47  64  64  GLN GLN B . n 
B 1 48  ALA 48  65  65  ALA ALA B . n 
B 1 49  LEU 49  66  66  LEU LEU B . n 
B 1 50  ARG 50  67  67  ARG ARG B . n 
B 1 51  PHE 51  68  68  PHE PHE B . n 
B 1 52  HIS 52  69  69  HIS HIS B . n 
B 1 53  ARG 53  70  70  ARG ARG B . n 
B 1 54  ASN 54  71  71  ASN ASN B . n 
B 1 55  LEU 55  72  72  LEU LEU B . n 
B 1 56  LYS 56  73  73  LYS LYS B . n 
B 1 57  LYS 57  74  74  LYS LYS B . n 
B 1 58  MET 58  75  75  MET MET B . n 
B 1 59  THR 59  76  76  THR THR B . n 
B 1 60  SER 60  77  77  SER SER B . n 
B 1 61  PRO 61  78  78  PRO PRO B . n 
B 1 62  LEU 62  79  79  LEU LEU B . n 
B 1 63  GLU 63  80  80  GLU GLU B . n 
B 1 64  LYS 64  81  81  LYS LYS B . n 
B 1 65  TYR 65  82  82  TYR TYR B . n 
B 1 66  ILE 66  83  83  ILE ILE B . n 
B 1 67  TYR 67  84  84  TYR TYR B . n 
B 1 68  ILE 68  85  85  ILE ILE B . n 
B 1 69  MET 69  86  86  MET MET B . n 
B 1 70  GLY 70  87  87  GLY GLY B . n 
B 1 71  ILE 71  88  88  ILE ILE B . n 
B 1 72  GLN 72  89  89  GLN GLN B . n 
B 1 73  GLU 73  90  90  GLU GLU B . n 
B 1 74  ARG 74  91  91  ARG ARG B . n 
B 1 75  ASN 75  92  92  ASN ASN B . n 
B 1 76  GLU 76  93  93  GLU GLU B . n 
B 1 77  LYS 77  94  94  LYS LYS B . n 
B 1 78  LEU 78  95  95  LEU LEU B . n 
B 1 79  PHE 79  96  96  PHE PHE B . n 
B 1 80  TYR 80  97  97  TYR TYR B . n 
B 1 81  ARG 81  98  98  ARG ARG B . n 
B 1 82  ILE 82  99  99  ILE ILE B . n 
B 1 83  LEU 83  100 100 LEU LEU B . n 
B 1 84  GLN 84  101 101 GLN GLN B . n 
B 1 85  ASP 85  102 102 ASP ASP B . n 
B 1 86  ASP 86  103 103 ASP ASP B . n 
B 1 87  ILE 87  104 104 ILE ILE B . n 
B 1 88  GLU 88  105 105 GLU GLU B . n 
B 1 89  SER 89  106 106 SER SER B . n 
B 1 90  LEU 90  107 107 LEU LEU B . n 
B 1 91  MET 91  108 108 MET MET B . n 
B 1 92  PRO 92  109 109 PRO PRO B . n 
B 1 93  ILE 93  110 110 ILE ILE B . n 
B 1 94  VAL 94  111 111 VAL VAL B . n 
B 1 95  TYR 95  112 112 TYR TYR B . n 
B 1 96  THR 96  113 113 THR THR B . n 
B 1 97  PRO 97  114 114 PRO PRO B . n 
B 1 98  THR 98  115 115 THR THR B . n 
B 1 99  VAL 99  116 116 VAL VAL B . n 
B 1 100 GLY 100 117 117 GLY GLY B . n 
B 1 101 LEU 101 118 118 LEU LEU B . n 
B 1 102 ALA 102 119 119 ALA ALA B . n 
B 1 103 CSX 103 120 120 CSX CSX B . n 
B 1 104 SER 104 121 121 SER SER B . n 
B 1 105 GLN 105 122 122 GLN GLN B . n 
B 1 106 TYR 106 123 123 TYR TYR B . n 
B 1 107 GLY 107 124 124 GLY GLY B . n 
B 1 108 HIS 108 125 125 HIS HIS B . n 
B 1 109 ILE 109 126 126 ILE ILE B . n 
B 1 110 PHE 110 127 127 PHE PHE B . n 
B 1 111 ARG 111 128 128 ARG ARG B . n 
B 1 112 ARG 112 129 129 ARG ARG B . n 
B 1 113 PRO 113 130 130 PRO PRO B . n 
B 1 114 LYS 114 131 131 LYS LYS B . n 
B 1 115 GLY 115 132 132 GLY GLY B . n 
B 1 116 LEU 116 133 133 LEU LEU B . n 
B 1 117 PHE 117 134 134 PHE PHE B . n 
B 1 118 ILE 118 135 135 ILE ILE B . n 
B 1 119 SER 119 136 136 SER SER B . n 
B 1 120 ILE 120 137 137 ILE ILE B . n 
B 1 121 SER 121 138 138 SER SER B . n 
B 1 122 ASP 122 139 139 ASP ASP B . n 
B 1 123 ARG 123 140 140 ARG ARG B . n 
B 1 124 GLY 124 141 141 GLY GLY B . n 
B 1 125 HIS 125 142 142 HIS HIS B . n 
B 1 126 VAL 126 143 143 VAL VAL B . n 
B 1 127 ARG 127 144 144 ARG ARG B . n 
B 1 128 SER 128 145 145 SER SER B . n 
B 1 129 ILE 129 146 146 ILE ILE B . n 
B 1 130 VAL 130 147 147 VAL VAL B . n 
B 1 131 ASP 131 148 148 ASP ASP B . n 
B 1 132 ASN 132 149 149 ASN ASN B . n 
B 1 133 TRP 133 150 150 TRP TRP B . n 
B 1 134 PRO 134 151 151 PRO PRO B . n 
B 1 135 GLU 135 152 152 GLU GLU B . n 
B 1 136 ASN 136 153 153 ASN ASN B . n 
B 1 137 HIS 137 154 154 HIS HIS B . n 
B 1 138 VAL 138 155 155 VAL VAL B . n 
B 1 139 LYS 139 156 156 LYS LYS B . n 
B 1 140 ALA 140 157 157 ALA ALA B . n 
B 1 141 VAL 141 158 158 VAL VAL B . n 
B 1 142 VAL 142 159 159 VAL VAL B . n 
B 1 143 VAL 143 160 160 VAL VAL B . n 
B 1 144 THR 144 161 161 THR THR B . n 
B 1 145 ASP 145 162 162 ASP ASP B . n 
B 1 146 GLY 146 163 163 GLY GLY B . n 
B 1 147 GLU 147 164 164 GLU GLU B . n 
B 1 148 ARG 148 165 165 ARG ARG B . n 
B 1 149 ILE 149 166 166 ILE ILE B . n 
B 1 150 LEU 150 167 167 LEU LEU B . n 
B 1 151 GLY 151 168 168 GLY GLY B . n 
B 1 152 LEU 152 169 169 LEU LEU B . n 
B 1 153 GLY 153 170 170 GLY GLY B . n 
B 1 154 ASP 154 171 171 ASP ASP B . n 
B 1 155 LEU 155 172 172 LEU LEU B . n 
B 1 156 GLY 156 173 173 GLY GLY B . n 
B 1 157 VAL 157 174 174 VAL VAL B . n 
B 1 158 TYR 158 175 175 TYR TYR B . n 
B 1 159 GLY 159 176 176 GLY GLY B . n 
B 1 160 MET 160 177 177 MET MET B . n 
B 1 161 GLY 161 178 178 GLY GLY B . n 
B 1 162 ILE 162 179 179 ILE ILE B . n 
B 1 163 PRO 163 180 180 PRO PRO B . n 
B 1 164 VAL 164 181 181 VAL VAL B . n 
B 1 165 GLY 165 182 182 GLY GLY B . n 
B 1 166 LYS 166 183 183 LYS LYS B . n 
B 1 167 LEU 167 184 184 LEU LEU B . n 
B 1 168 CYS 168 185 185 CYS CYS B . n 
B 1 169 LEU 169 186 186 LEU LEU B . n 
B 1 170 TYR 170 187 187 TYR TYR B . n 
B 1 171 THR 171 188 188 THR THR B . n 
B 1 172 ALA 172 189 189 ALA ALA B . n 
B 1 173 CYS 173 190 190 CYS CYS B . n 
B 1 174 ALA 174 191 191 ALA ALA B . n 
B 1 175 GLY 175 192 192 GLY GLY B . n 
B 1 176 ILE 176 193 193 ILE ILE B . n 
B 1 177 ARG 177 194 194 ARG ARG B . n 
B 1 178 PRO 178 195 195 PRO PRO B . n 
B 1 179 ASP 179 196 196 ASP ASP B . n 
B 1 180 ARG 180 197 197 ARG ARG B . n 
B 1 181 CYS 181 198 198 CYS CYS B . n 
B 1 182 LEU 182 199 199 LEU LEU B . n 
B 1 183 PRO 183 200 200 PRO PRO B . n 
B 1 184 VAL 184 201 201 VAL VAL B . n 
B 1 185 CYS 185 202 202 CYS CYS B . n 
B 1 186 ILE 186 203 203 ILE ILE B . n 
B 1 187 ASP 187 204 204 ASP ASP B . n 
B 1 188 VAL 188 205 205 VAL VAL B . n 
B 1 189 GLY 189 206 206 GLY GLY B . n 
B 1 190 THR 190 207 207 THR THR B . n 
B 1 191 ASP 191 208 208 ASP ASP B . n 
B 1 192 ASN 192 209 209 ASN ASN B . n 
B 1 193 ILE 193 210 210 ILE ILE B . n 
B 1 194 ALA 194 211 211 ALA ALA B . n 
B 1 195 LEU 195 212 212 LEU LEU B . n 
B 1 196 LEU 196 213 213 LEU LEU B . n 
B 1 197 LYS 197 214 214 LYS LYS B . n 
B 1 198 ASP 198 215 215 ASP ASP B . n 
B 1 199 PRO 199 216 216 PRO PRO B . n 
B 1 200 PHE 200 217 217 PHE PHE B . n 
B 1 201 TYR 201 218 218 TYR TYR B . n 
B 1 202 MET 202 219 219 MET MET B . n 
B 1 203 GLY 203 220 220 GLY GLY B . n 
B 1 204 LEU 204 221 221 LEU LEU B . n 
B 1 205 TYR 205 222 222 TYR TYR B . n 
B 1 206 GLN 206 223 223 GLN GLN B . n 
B 1 207 LYS 207 224 224 LYS LYS B . n 
B 1 208 ARG 208 225 225 ARG ARG B . n 
B 1 209 ASP 209 226 226 ASP ASP B . n 
B 1 210 ARG 210 227 227 ARG ARG B . n 
B 1 211 THR 211 228 228 THR THR B . n 
B 1 212 GLN 212 229 229 GLN GLN B . n 
B 1 213 GLN 213 230 230 GLN GLN B . n 
B 1 214 TYR 214 231 231 TYR TYR B . n 
B 1 215 ASP 215 232 232 ASP ASP B . n 
B 1 216 ASP 216 233 233 ASP ASP B . n 
B 1 217 LEU 217 234 234 LEU LEU B . n 
B 1 218 ILE 218 235 235 ILE ILE B . n 
B 1 219 ASP 219 236 236 ASP ASP B . n 
B 1 220 GLU 220 237 237 GLU GLU B . n 
B 1 221 PHE 221 238 238 PHE PHE B . n 
B 1 222 MET 222 239 239 MET MET B . n 
B 1 223 LYS 223 240 240 LYS LYS B . n 
B 1 224 ALA 224 241 241 ALA ALA B . n 
B 1 225 ILE 225 242 242 ILE ILE B . n 
B 1 226 THR 226 243 243 THR THR B . n 
B 1 227 ASP 227 244 244 ASP ASP B . n 
B 1 228 ARG 228 245 245 ARG ARG B . n 
B 1 229 TYR 229 246 246 TYR TYR B . n 
B 1 230 GLY 230 247 247 GLY GLY B . n 
B 1 231 ARG 231 248 248 ARG ARG B . n 
B 1 232 ASN 232 249 249 ASN ASN B . n 
B 1 233 THR 233 250 250 THR THR B . n 
B 1 234 LEU 234 251 251 LEU LEU B . n 
B 1 235 ILE 235 252 252 ILE ILE B . n 
B 1 236 GLN 236 253 253 GLN GLN B . n 
B 1 237 PHE 237 254 254 PHE PHE B . n 
B 1 238 GLU 238 255 255 GLU GLU B . n 
B 1 239 ASP 239 256 256 ASP ASP B . n 
B 1 240 PHE 240 257 257 PHE PHE B . n 
B 1 241 GLY 241 258 258 GLY GLY B . n 
B 1 242 ASN 242 259 259 ASN ASN B . n 
B 1 243 HIS 243 260 260 HIS HIS B . n 
B 1 244 ASN 244 261 261 ASN ASN B . n 
B 1 245 ALA 245 262 262 ALA ALA B . n 
B 1 246 PHE 246 263 263 PHE PHE B . n 
B 1 247 ARG 247 264 264 ARG ARG B . n 
B 1 248 PHE 248 265 265 PHE PHE B . n 
B 1 249 LEU 249 266 266 LEU LEU B . n 
B 1 250 ARG 250 267 267 ARG ARG B . n 
B 1 251 LYS 251 268 268 LYS LYS B . n 
B 1 252 TYR 252 269 269 TYR TYR B . n 
B 1 253 ARG 253 270 270 ARG ARG B . n 
B 1 254 GLU 254 271 271 GLU GLU B . n 
B 1 255 LYS 255 272 272 LYS LYS B . n 
B 1 256 TYR 256 273 273 TYR TYR B . n 
B 1 257 CYS 257 274 274 CYS CYS B . n 
B 1 258 THR 258 275 275 THR THR B . n 
B 1 259 PHE 259 276 276 PHE PHE B . n 
B 1 260 ASN 260 277 277 ASN ASN B . n 
B 1 261 ASP 261 278 278 ASP ASP B . n 
B 1 262 ASP 262 279 279 ASP ASP B . n 
B 1 263 ILE 263 280 280 ILE ILE B . n 
B 1 264 GLN 264 281 281 GLN GLN B . n 
B 1 265 GLY 265 282 282 GLY GLY B . n 
B 1 266 THR 266 283 283 THR THR B . n 
B 1 267 ALA 267 284 284 ALA ALA B . n 
B 1 268 ALA 268 285 285 ALA ALA B . n 
B 1 269 VAL 269 286 286 VAL VAL B . n 
B 1 270 ALA 270 287 287 ALA ALA B . n 
B 1 271 LEU 271 288 288 LEU LEU B . n 
B 1 272 ALA 272 289 289 ALA ALA B . n 
B 1 273 GLY 273 290 290 GLY GLY B . n 
B 1 274 LEU 274 291 291 LEU LEU B . n 
B 1 275 LEU 275 292 292 LEU LEU B . n 
B 1 276 ALA 276 293 293 ALA ALA B . n 
B 1 277 ALA 277 294 294 ALA ALA B . n 
B 1 278 GLN 278 295 295 GLN GLN B . n 
B 1 279 LYS 279 296 296 LYS LYS B . n 
B 1 280 VAL 280 297 297 VAL VAL B . n 
B 1 281 ILE 281 298 298 ILE ILE B . n 
B 1 282 SER 282 299 299 SER SER B . n 
B 1 283 LYS 283 300 300 LYS LYS B . n 
B 1 284 PRO 284 301 301 PRO PRO B . n 
B 1 285 ILE 285 302 302 ILE ILE B . n 
B 1 286 SER 286 303 303 SER SER B . n 
B 1 287 GLU 287 304 304 GLU GLU B . n 
B 1 288 HIS 288 305 305 HIS HIS B . n 
B 1 289 LYS 289 306 306 LYS LYS B . n 
B 1 290 ILE 290 307 307 ILE ILE B . n 
B 1 291 LEU 291 308 308 LEU LEU B . n 
B 1 292 PHE 292 309 309 PHE PHE B . n 
B 1 293 LEU 293 310 310 LEU LEU B . n 
B 1 294 GLY 294 311 311 GLY GLY B . n 
B 1 295 ALA 295 312 312 ALA ALA B . n 
B 1 296 GLY 296 313 313 GLY GLY B . n 
B 1 297 GLU 297 314 314 GLU GLU B . n 
B 1 298 ALA 298 315 315 ALA ALA B . n 
B 1 299 ALA 299 316 316 ALA ALA B . n 
B 1 300 LEU 300 317 317 LEU LEU B . n 
B 1 301 GLY 301 318 318 GLY GLY B . n 
B 1 302 ILE 302 319 319 ILE ILE B . n 
B 1 303 ALA 303 320 320 ALA ALA B . n 
B 1 304 ASN 304 321 321 ASN ASN B . n 
B 1 305 LEU 305 322 322 LEU LEU B . n 
B 1 306 ILE 306 323 323 ILE ILE B . n 
B 1 307 VAL 307 324 324 VAL VAL B . n 
B 1 308 MET 308 325 325 MET MET B . n 
B 1 309 SER 309 326 326 SER SER B . n 
B 1 310 MET 310 327 327 MET MET B . n 
B 1 311 VAL 311 328 328 VAL VAL B . n 
B 1 312 GLU 312 329 329 GLU GLU B . n 
B 1 313 ASN 313 330 330 ASN ASN B . n 
B 1 314 GLY 314 331 331 GLY GLY B . n 
B 1 315 LEU 315 332 332 LEU LEU B . n 
B 1 316 SER 316 333 333 SER SER B . n 
B 1 317 GLU 317 334 334 GLU GLU B . n 
B 1 318 GLN 318 335 335 GLN GLN B . n 
B 1 319 GLU 319 336 336 GLU GLU B . n 
B 1 320 ALA 320 337 337 ALA ALA B . n 
B 1 321 GLN 321 338 338 GLN GLN B . n 
B 1 322 LYS 322 339 339 LYS LYS B . n 
B 1 323 LYS 323 340 340 LYS LYS B . n 
B 1 324 ILE 324 341 341 ILE ILE B . n 
B 1 325 TRP 325 342 342 TRP TRP B . n 
B 1 326 MET 326 343 343 MET MET B . n 
B 1 327 PHE 327 344 344 PHE PHE B . n 
B 1 328 ASP 328 345 345 ASP ASP B . n 
B 1 329 LYS 329 346 346 LYS LYS B . n 
B 1 330 TYR 330 347 347 TYR TYR B . n 
B 1 331 GLY 331 348 348 GLY GLY B . n 
B 1 332 LEU 332 349 349 LEU LEU B . n 
B 1 333 LEU 333 350 350 LEU LEU B . n 
B 1 334 VAL 334 351 351 VAL VAL B . n 
B 1 335 LYS 335 352 352 LYS LYS B . n 
B 1 336 GLY 336 353 353 GLY GLY B . n 
B 1 337 ARG 337 354 354 ARG ARG B . n 
B 1 338 LYS 338 355 355 LYS LYS B . n 
B 1 339 ALA 339 356 356 ALA ALA B . n 
B 1 340 LYS 340 357 357 LYS LYS B . n 
B 1 341 ILE 341 358 358 ILE ILE B . n 
B 1 342 ASP 342 359 359 ASP ASP B . n 
B 1 343 SER 343 360 360 SER SER B . n 
B 1 344 TYR 344 361 361 TYR TYR B . n 
B 1 345 GLN 345 362 362 GLN GLN B . n 
B 1 346 GLU 346 363 363 GLU GLU B . n 
B 1 347 PRO 347 364 364 PRO PRO B . n 
B 1 348 PHE 348 365 365 PHE PHE B . n 
B 1 349 THR 349 366 366 THR THR B . n 
B 1 350 HIS 350 367 367 HIS HIS B . n 
B 1 351 SER 351 368 368 SER SER B . n 
B 1 352 ALA 352 369 369 ALA ALA B . n 
B 1 353 PRO 353 370 370 PRO PRO B . n 
B 1 354 GLU 354 371 371 GLU GLU B . n 
B 1 355 SER 355 372 372 SER SER B . n 
B 1 356 ILE 356 373 373 ILE ILE B . n 
B 1 357 PRO 357 374 374 PRO PRO B . n 
B 1 358 ASP 358 375 375 ASP ASP B . n 
B 1 359 THR 359 376 376 THR THR B . n 
B 1 360 PHE 360 377 377 PHE PHE B . n 
B 1 361 GLU 361 378 378 GLU GLU B . n 
B 1 362 ASP 362 379 379 ASP ASP B . n 
B 1 363 ALA 363 380 380 ALA ALA B . n 
B 1 364 VAL 364 381 381 VAL VAL B . n 
B 1 365 ASN 365 382 382 ASN ASN B . n 
B 1 366 ILE 366 383 383 ILE ILE B . n 
B 1 367 LEU 367 384 384 LEU LEU B . n 
B 1 368 LYS 368 385 385 LYS LYS B . n 
B 1 369 PRO 369 386 386 PRO PRO B . n 
B 1 370 SER 370 387 387 SER SER B . n 
B 1 371 THR 371 388 388 THR THR B . n 
B 1 372 ILE 372 389 389 ILE ILE B . n 
B 1 373 ILE 373 390 390 ILE ILE B . n 
B 1 374 GLY 374 391 391 GLY GLY B . n 
B 1 375 VAL 375 392 392 VAL VAL B . n 
B 1 376 ALA 376 393 393 ALA ALA B . n 
B 1 377 GLY 377 394 394 GLY GLY B . n 
B 1 378 ALA 378 395 395 ALA ALA B . n 
B 1 379 GLY 379 396 396 GLY GLY B . n 
B 1 380 ARG 380 397 397 ARG ARG B . n 
B 1 381 LEU 381 398 398 LEU LEU B . n 
B 1 382 PHE 382 399 399 PHE PHE B . n 
B 1 383 THR 383 400 400 THR THR B . n 
B 1 384 PRO 384 401 401 PRO PRO B . n 
B 1 385 ASP 385 402 402 ASP ASP B . n 
B 1 386 VAL 386 403 403 VAL VAL B . n 
B 1 387 ILE 387 404 404 ILE ILE B . n 
B 1 388 ARG 388 405 405 ARG ARG B . n 
B 1 389 ALA 389 406 406 ALA ALA B . n 
B 1 390 MET 390 407 407 MET MET B . n 
B 1 391 ALA 391 408 408 ALA ALA B . n 
B 1 392 SER 392 409 409 SER SER B . n 
B 1 393 ILE 393 410 410 ILE ILE B . n 
B 1 394 ASN 394 411 411 ASN ASN B . n 
B 1 395 GLU 395 412 412 GLU GLU B . n 
B 1 396 ARG 396 413 413 ARG ARG B . n 
B 1 397 PRO 397 414 414 PRO PRO B . n 
B 1 398 VAL 398 415 415 VAL VAL B . n 
B 1 399 ILE 399 416 416 ILE ILE B . n 
B 1 400 PHE 400 417 417 PHE PHE B . n 
B 1 401 ALA 401 418 418 ALA ALA B . n 
B 1 402 LEU 402 419 419 LEU LEU B . n 
B 1 403 SER 403 420 420 SER SER B . n 
B 1 404 ASN 404 421 421 ASN ASN B . n 
B 1 405 PRO 405 422 422 PRO PRO B . n 
B 1 406 THR 406 423 423 THR THR B . n 
B 1 407 ALA 407 424 424 ALA ALA B . n 
B 1 408 GLN 408 425 425 GLN GLN B . n 
B 1 409 ALA 409 426 426 ALA ALA B . n 
B 1 410 GLU 410 427 427 GLU GLU B . n 
B 1 411 CYS 411 428 428 CYS CYS B . n 
B 1 412 THR 412 429 429 THR THR B . n 
B 1 413 ALA 413 430 430 ALA ALA B . n 
B 1 414 GLU 414 431 431 GLU GLU B . n 
B 1 415 GLU 415 432 432 GLU GLU B . n 
B 1 416 ALA 416 433 433 ALA ALA B . n 
B 1 417 TYR 417 434 434 TYR TYR B . n 
B 1 418 THR 418 435 435 THR THR B . n 
B 1 419 LEU 419 436 436 LEU LEU B . n 
B 1 420 THR 420 437 437 THR THR B . n 
B 1 421 GLU 421 438 438 GLU GLU B . n 
B 1 422 GLY 422 439 439 GLY GLY B . n 
B 1 423 ARG 423 440 440 ARG ARG B . n 
B 1 424 CYS 424 441 441 CYS CYS B . n 
B 1 425 LEU 425 442 442 LEU LEU B . n 
B 1 426 PHE 426 443 443 PHE PHE B . n 
B 1 427 ALA 427 444 444 ALA ALA B . n 
B 1 428 SER 428 445 445 SER SER B . n 
B 1 429 GLY 429 446 446 GLY GLY B . n 
B 1 430 SER 430 447 447 SER SER B . n 
B 1 431 PRO 431 448 448 PRO PRO B . n 
B 1 432 PHE 432 449 449 PHE PHE B . n 
B 1 433 GLY 433 450 450 GLY GLY B . n 
B 1 434 PRO 434 451 451 PRO PRO B . n 
B 1 435 VAL 435 452 452 VAL VAL B . n 
B 1 436 LYS 436 453 453 LYS LYS B . n 
B 1 437 LEU 437 454 454 LEU LEU B . n 
B 1 438 THR 438 455 455 THR THR B . n 
B 1 439 ASP 439 456 456 ASP ASP B . n 
B 1 440 GLY 440 457 457 GLY GLY B . n 
B 1 441 ARG 441 458 458 ARG ARG B . n 
B 1 442 VAL 442 459 459 VAL VAL B . n 
B 1 443 PHE 443 460 460 PHE PHE B . n 
B 1 444 THR 444 461 461 THR THR B . n 
B 1 445 PRO 445 462 462 PRO PRO B . n 
B 1 446 GLY 446 463 463 GLY GLY B . n 
B 1 447 GLN 447 464 464 GLN GLN B . n 
B 1 448 GLY 448 465 465 GLY GLY B . n 
B 1 449 ASN 449 466 466 ASN ASN B . n 
B 1 450 ASN 450 467 467 ASN ASN B . n 
B 1 451 VAL 451 468 468 VAL VAL B . n 
B 1 452 TYR 452 469 469 TYR TYR B . n 
B 1 453 ILE 453 470 470 ILE ILE B . n 
B 1 454 PHE 454 471 471 PHE PHE B . n 
B 1 455 PRO 455 472 472 PRO PRO B . n 
B 1 456 GLY 456 473 473 GLY GLY B . n 
B 1 457 VAL 457 474 474 VAL VAL B . n 
B 1 458 ALA 458 475 475 ALA ALA B . n 
B 1 459 LEU 459 476 476 LEU LEU B . n 
B 1 460 ALA 460 477 477 ALA ALA B . n 
B 1 461 VAL 461 478 478 VAL VAL B . n 
B 1 462 ILE 462 479 479 ILE ILE B . n 
B 1 463 LEU 463 480 480 LEU LEU B . n 
B 1 464 CYS 464 481 481 CYS CYS B . n 
B 1 465 ASN 465 482 482 ASN ASN B . n 
B 1 466 THR 466 483 483 THR THR B . n 
B 1 467 ARG 467 484 484 ARG ARG B . n 
B 1 468 HIS 468 485 485 HIS HIS B . n 
B 1 469 ILE 469 486 486 ILE ILE B . n 
B 1 470 SER 470 487 487 SER SER B . n 
B 1 471 ASP 471 488 488 ASP ASP B . n 
B 1 472 SER 472 489 489 SER SER B . n 
B 1 473 VAL 473 490 490 VAL VAL B . n 
B 1 474 PHE 474 491 491 PHE PHE B . n 
B 1 475 LEU 475 492 492 LEU LEU B . n 
B 1 476 GLU 476 493 493 GLU GLU B . n 
B 1 477 ALA 477 494 494 ALA ALA B . n 
B 1 478 ALA 478 495 495 ALA ALA B . n 
B 1 479 LYS 479 496 496 LYS LYS B . n 
B 1 480 ALA 480 497 497 ALA ALA B . n 
B 1 481 LEU 481 498 498 LEU LEU B . n 
B 1 482 THR 482 499 499 THR THR B . n 
B 1 483 SER 483 500 500 SER SER B . n 
B 1 484 GLN 484 501 501 GLN GLN B . n 
B 1 485 LEU 485 502 502 LEU LEU B . n 
B 1 486 THR 486 503 503 THR THR B . n 
B 1 487 ASP 487 504 504 ASP ASP B . n 
B 1 488 GLU 488 505 505 GLU GLU B . n 
B 1 489 GLU 489 506 506 GLU GLU B . n 
B 1 490 LEU 490 507 507 LEU LEU B . n 
B 1 491 ALA 491 508 508 ALA ALA B . n 
B 1 492 GLN 492 509 509 GLN GLN B . n 
B 1 493 GLY 493 510 510 GLY GLY B . n 
B 1 494 ARG 494 511 511 ARG ARG B . n 
B 1 495 LEU 495 512 512 LEU LEU B . n 
B 1 496 TYR 496 513 513 TYR TYR B . n 
B 1 497 PRO 497 514 514 PRO PRO B . n 
B 1 498 PRO 498 515 515 PRO PRO B . n 
B 1 499 LEU 499 516 516 LEU LEU B . n 
B 1 500 ALA 500 517 517 ALA ALA B . n 
B 1 501 ASN 501 518 518 ASN ASN B . n 
B 1 502 ILE 502 519 519 ILE ILE B . n 
B 1 503 GLN 503 520 520 GLN GLN B . n 
B 1 504 GLU 504 521 521 GLU GLU B . n 
B 1 505 VAL 505 522 522 VAL VAL B . n 
B 1 506 SER 506 523 523 SER SER B . n 
B 1 507 ILE 507 524 524 ILE ILE B . n 
B 1 508 ASN 508 525 525 ASN ASN B . n 
B 1 509 ILE 509 526 526 ILE ILE B . n 
B 1 510 ALA 510 527 527 ALA ALA B . n 
B 1 511 ILE 511 528 528 ILE ILE B . n 
B 1 512 LYS 512 529 529 LYS LYS B . n 
B 1 513 VAL 513 530 530 VAL VAL B . n 
B 1 514 THR 514 531 531 THR THR B . n 
B 1 515 GLU 515 532 532 GLU GLU B . n 
B 1 516 TYR 516 533 533 TYR TYR B . n 
B 1 517 LEU 517 534 534 LEU LEU B . n 
B 1 518 TYR 518 535 535 TYR TYR B . n 
B 1 519 ALA 519 536 536 ALA ALA B . n 
B 1 520 ASN 520 537 537 ASN ASN B . n 
B 1 521 LYS 521 538 538 LYS LYS B . n 
B 1 522 MET 522 539 539 MET MET B . n 
B 1 523 ALA 523 540 540 ALA ALA B . n 
B 1 524 PHE 524 541 541 PHE PHE B . n 
B 1 525 ARG 525 542 542 ARG ARG B . n 
B 1 526 TYR 526 543 543 TYR TYR B . n 
B 1 527 PRO 527 544 544 PRO PRO B . n 
B 1 528 GLU 528 545 545 GLU GLU B . n 
B 1 529 PRO 529 546 546 PRO PRO B . n 
B 1 530 GLU 530 547 547 GLU GLU B . n 
B 1 531 ASP 531 548 548 ASP ASP B . n 
B 1 532 LYS 532 549 549 LYS LYS B . n 
B 1 533 ALA 533 550 550 ALA ALA B . n 
B 1 534 LYS 534 551 551 LYS LYS B . n 
B 1 535 TYR 535 552 552 TYR TYR B . n 
B 1 536 VAL 536 553 553 VAL VAL B . n 
B 1 537 LYS 537 554 554 LYS LYS B . n 
B 1 538 GLU 538 555 555 GLU GLU B . n 
B 1 539 ARG 539 556 556 ARG ARG B . n 
B 1 540 THR 540 557 557 THR THR B . n 
B 1 541 TRP 541 558 558 TRP TRP B . n 
B 1 542 ARG 542 559 559 ARG ARG B . n 
B 1 543 SER 543 560 560 SER SER B . n 
B 1 544 GLU 544 561 561 GLU GLU B . n 
B 1 545 TYR 545 562 562 TYR TYR B . n 
B 1 546 ASP 546 563 563 ASP ASP B . n 
B 1 547 SER 547 564 564 SER SER B . n 
B 1 548 LEU 548 565 565 LEU LEU B . n 
B 1 549 LEU 549 566 566 LEU LEU B . n 
B 1 550 PRO 550 567 567 PRO PRO B . n 
B 1 551 ASP 551 568 568 ASP ASP B . n 
B 1 552 VAL 552 569 569 VAL VAL B . n 
B 1 553 TYR 553 570 570 TYR TYR B . n 
B 1 554 GLU 554 571 571 GLU GLU B . n 
B 1 555 TRP 555 572 572 TRP TRP B . n 
B 1 556 PRO 556 573 573 PRO PRO B . n 
B 1 557 GLU 557 574 574 GLU GLU B . n 
B 1 558 SER 558 575 ?   ?   ?   B . n 
B 1 559 ALA 559 576 ?   ?   ?   B . n 
B 1 560 SER 560 577 ?   ?   ?   B . n 
B 1 561 SER 561 578 ?   ?   ?   B . n 
B 1 562 PRO 562 579 ?   ?   ?   B . n 
B 1 563 PRO 563 580 ?   ?   ?   B . n 
B 1 564 VAL 564 581 ?   ?   ?   B . n 
B 1 565 ILE 565 582 ?   ?   ?   B . n 
B 1 566 THR 566 583 ?   ?   ?   B . n 
B 1 567 GLU 567 584 ?   ?   ?   B . n 
B 1 568 LEU 568 585 ?   ?   ?   B . n 
B 1 569 GLU 569 586 ?   ?   ?   B . n 
B 1 570 HIS 570 587 ?   ?   ?   B . n 
B 1 571 HIS 571 588 ?   ?   ?   B . n 
B 1 572 HIS 572 589 ?   ?   ?   B . n 
B 1 573 HIS 573 590 ?   ?   ?   B . n 
B 1 574 HIS 574 591 ?   ?   ?   B . n 
B 1 575 HIS 575 592 ?   ?   ?   B . n 
C 1 1   MET 1   18  ?   ?   ?   C . n 
C 1 2   LEU 2   19  ?   ?   ?   C . n 
C 1 3   HIS 3   20  ?   ?   ?   C . n 
C 1 4   ILE 4   21  ?   ?   ?   C . n 
C 1 5   LYS 5   22  22  LYS LYS C . n 
C 1 6   GLU 6   23  23  GLU GLU C . n 
C 1 7   LYS 7   24  24  LYS LYS C . n 
C 1 8   GLY 8   25  25  GLY GLY C . n 
C 1 9   LYS 9   26  26  LYS LYS C . n 
C 1 10  PRO 10  27  27  PRO PRO C . n 
C 1 11  LEU 11  28  28  LEU LEU C . n 
C 1 12  MET 12  29  29  MET MET C . n 
C 1 13  LEU 13  30  30  LEU LEU C . n 
C 1 14  ASN 14  31  31  ASN ASN C . n 
C 1 15  PRO 15  32  32  PRO PRO C . n 
C 1 16  ARG 16  33  33  ARG ARG C . n 
C 1 17  THR 17  34  34  THR THR C . n 
C 1 18  ASN 18  35  35  ASN ASN C . n 
C 1 19  LYS 19  36  36  LYS LYS C . n 
C 1 20  GLY 20  37  37  GLY GLY C . n 
C 1 21  MET 21  38  38  MET MET C . n 
C 1 22  ALA 22  39  39  ALA ALA C . n 
C 1 23  PHE 23  40  40  PHE PHE C . n 
C 1 24  THR 24  41  41  THR THR C . n 
C 1 25  LEU 25  42  42  LEU LEU C . n 
C 1 26  GLN 26  43  43  GLN GLN C . n 
C 1 27  GLU 27  44  44  GLU GLU C . n 
C 1 28  ARG 28  45  45  ARG ARG C . n 
C 1 29  GLN 29  46  46  GLN GLN C . n 
C 1 30  MET 30  47  47  MET MET C . n 
C 1 31  LEU 31  48  48  LEU LEU C . n 
C 1 32  GLY 32  49  49  GLY GLY C . n 
C 1 33  LEU 33  50  50  LEU LEU C . n 
C 1 34  GLN 34  51  51  GLN GLN C . n 
C 1 35  GLY 35  52  52  GLY GLY C . n 
C 1 36  LEU 36  53  53  LEU LEU C . n 
C 1 37  LEU 37  54  54  LEU LEU C . n 
C 1 38  PRO 38  55  55  PRO PRO C . n 
C 1 39  PRO 39  56  56  PRO PRO C . n 
C 1 40  LYS 40  57  57  LYS LYS C . n 
C 1 41  ILE 41  58  58  ILE ILE C . n 
C 1 42  GLU 42  59  59  GLU GLU C . n 
C 1 43  THR 43  60  60  THR THR C . n 
C 1 44  GLN 44  61  61  GLN GLN C . n 
C 1 45  ASP 45  62  62  ASP ASP C . n 
C 1 46  ILE 46  63  63  ILE ILE C . n 
C 1 47  GLN 47  64  64  GLN GLN C . n 
C 1 48  ALA 48  65  65  ALA ALA C . n 
C 1 49  LEU 49  66  66  LEU LEU C . n 
C 1 50  ARG 50  67  67  ARG ARG C . n 
C 1 51  PHE 51  68  68  PHE PHE C . n 
C 1 52  HIS 52  69  69  HIS HIS C . n 
C 1 53  ARG 53  70  70  ARG ARG C . n 
C 1 54  ASN 54  71  71  ASN ASN C . n 
C 1 55  LEU 55  72  72  LEU LEU C . n 
C 1 56  LYS 56  73  73  LYS LYS C . n 
C 1 57  LYS 57  74  74  LYS LYS C . n 
C 1 58  MET 58  75  75  MET MET C . n 
C 1 59  THR 59  76  76  THR THR C . n 
C 1 60  SER 60  77  77  SER SER C . n 
C 1 61  PRO 61  78  78  PRO PRO C . n 
C 1 62  LEU 62  79  79  LEU LEU C . n 
C 1 63  GLU 63  80  80  GLU GLU C . n 
C 1 64  LYS 64  81  81  LYS LYS C . n 
C 1 65  TYR 65  82  82  TYR TYR C . n 
C 1 66  ILE 66  83  83  ILE ILE C . n 
C 1 67  TYR 67  84  84  TYR TYR C . n 
C 1 68  ILE 68  85  85  ILE ILE C . n 
C 1 69  MET 69  86  86  MET MET C . n 
C 1 70  GLY 70  87  87  GLY GLY C . n 
C 1 71  ILE 71  88  88  ILE ILE C . n 
C 1 72  GLN 72  89  89  GLN GLN C . n 
C 1 73  GLU 73  90  90  GLU GLU C . n 
C 1 74  ARG 74  91  91  ARG ARG C . n 
C 1 75  ASN 75  92  92  ASN ASN C . n 
C 1 76  GLU 76  93  93  GLU GLU C . n 
C 1 77  LYS 77  94  94  LYS LYS C . n 
C 1 78  LEU 78  95  95  LEU LEU C . n 
C 1 79  PHE 79  96  96  PHE PHE C . n 
C 1 80  TYR 80  97  97  TYR TYR C . n 
C 1 81  ARG 81  98  98  ARG ARG C . n 
C 1 82  ILE 82  99  99  ILE ILE C . n 
C 1 83  LEU 83  100 100 LEU LEU C . n 
C 1 84  GLN 84  101 101 GLN GLN C . n 
C 1 85  ASP 85  102 102 ASP ASP C . n 
C 1 86  ASP 86  103 103 ASP ASP C . n 
C 1 87  ILE 87  104 104 ILE ILE C . n 
C 1 88  GLU 88  105 105 GLU GLU C . n 
C 1 89  SER 89  106 106 SER SER C . n 
C 1 90  LEU 90  107 107 LEU LEU C . n 
C 1 91  MET 91  108 108 MET MET C . n 
C 1 92  PRO 92  109 109 PRO PRO C . n 
C 1 93  ILE 93  110 110 ILE ILE C . n 
C 1 94  VAL 94  111 111 VAL VAL C . n 
C 1 95  TYR 95  112 112 TYR TYR C . n 
C 1 96  THR 96  113 113 THR THR C . n 
C 1 97  PRO 97  114 114 PRO PRO C . n 
C 1 98  THR 98  115 115 THR THR C . n 
C 1 99  VAL 99  116 116 VAL VAL C . n 
C 1 100 GLY 100 117 117 GLY GLY C . n 
C 1 101 LEU 101 118 118 LEU LEU C . n 
C 1 102 ALA 102 119 119 ALA ALA C . n 
C 1 103 CSX 103 120 120 CSX CSX C . n 
C 1 104 SER 104 121 121 SER SER C . n 
C 1 105 GLN 105 122 122 GLN GLN C . n 
C 1 106 TYR 106 123 123 TYR TYR C . n 
C 1 107 GLY 107 124 124 GLY GLY C . n 
C 1 108 HIS 108 125 125 HIS HIS C . n 
C 1 109 ILE 109 126 126 ILE ILE C . n 
C 1 110 PHE 110 127 127 PHE PHE C . n 
C 1 111 ARG 111 128 128 ARG ARG C . n 
C 1 112 ARG 112 129 129 ARG ARG C . n 
C 1 113 PRO 113 130 130 PRO PRO C . n 
C 1 114 LYS 114 131 131 LYS LYS C . n 
C 1 115 GLY 115 132 132 GLY GLY C . n 
C 1 116 LEU 116 133 133 LEU LEU C . n 
C 1 117 PHE 117 134 134 PHE PHE C . n 
C 1 118 ILE 118 135 135 ILE ILE C . n 
C 1 119 SER 119 136 136 SER SER C . n 
C 1 120 ILE 120 137 137 ILE ILE C . n 
C 1 121 SER 121 138 138 SER SER C . n 
C 1 122 ASP 122 139 139 ASP ASP C . n 
C 1 123 ARG 123 140 140 ARG ARG C . n 
C 1 124 GLY 124 141 141 GLY GLY C . n 
C 1 125 HIS 125 142 142 HIS HIS C . n 
C 1 126 VAL 126 143 143 VAL VAL C . n 
C 1 127 ARG 127 144 144 ARG ARG C . n 
C 1 128 SER 128 145 145 SER SER C . n 
C 1 129 ILE 129 146 146 ILE ILE C . n 
C 1 130 VAL 130 147 147 VAL VAL C . n 
C 1 131 ASP 131 148 148 ASP ASP C . n 
C 1 132 ASN 132 149 149 ASN ASN C . n 
C 1 133 TRP 133 150 150 TRP TRP C . n 
C 1 134 PRO 134 151 151 PRO PRO C . n 
C 1 135 GLU 135 152 152 GLU GLU C . n 
C 1 136 ASN 136 153 153 ASN ASN C . n 
C 1 137 HIS 137 154 154 HIS HIS C . n 
C 1 138 VAL 138 155 155 VAL VAL C . n 
C 1 139 LYS 139 156 156 LYS LYS C . n 
C 1 140 ALA 140 157 157 ALA ALA C . n 
C 1 141 VAL 141 158 158 VAL VAL C . n 
C 1 142 VAL 142 159 159 VAL VAL C . n 
C 1 143 VAL 143 160 160 VAL VAL C . n 
C 1 144 THR 144 161 161 THR THR C . n 
C 1 145 ASP 145 162 162 ASP ASP C . n 
C 1 146 GLY 146 163 163 GLY GLY C . n 
C 1 147 GLU 147 164 164 GLU GLU C . n 
C 1 148 ARG 148 165 165 ARG ARG C . n 
C 1 149 ILE 149 166 166 ILE ILE C . n 
C 1 150 LEU 150 167 167 LEU LEU C . n 
C 1 151 GLY 151 168 168 GLY GLY C . n 
C 1 152 LEU 152 169 169 LEU LEU C . n 
C 1 153 GLY 153 170 170 GLY GLY C . n 
C 1 154 ASP 154 171 171 ASP ASP C . n 
C 1 155 LEU 155 172 172 LEU LEU C . n 
C 1 156 GLY 156 173 173 GLY GLY C . n 
C 1 157 VAL 157 174 174 VAL VAL C . n 
C 1 158 TYR 158 175 175 TYR TYR C . n 
C 1 159 GLY 159 176 176 GLY GLY C . n 
C 1 160 MET 160 177 177 MET MET C . n 
C 1 161 GLY 161 178 178 GLY GLY C . n 
C 1 162 ILE 162 179 179 ILE ILE C . n 
C 1 163 PRO 163 180 180 PRO PRO C . n 
C 1 164 VAL 164 181 181 VAL VAL C . n 
C 1 165 GLY 165 182 182 GLY GLY C . n 
C 1 166 LYS 166 183 183 LYS LYS C . n 
C 1 167 LEU 167 184 184 LEU LEU C . n 
C 1 168 CYS 168 185 185 CYS CYS C . n 
C 1 169 LEU 169 186 186 LEU LEU C . n 
C 1 170 TYR 170 187 187 TYR TYR C . n 
C 1 171 THR 171 188 188 THR THR C . n 
C 1 172 ALA 172 189 189 ALA ALA C . n 
C 1 173 CYS 173 190 190 CYS CYS C . n 
C 1 174 ALA 174 191 191 ALA ALA C . n 
C 1 175 GLY 175 192 192 GLY GLY C . n 
C 1 176 ILE 176 193 193 ILE ILE C . n 
C 1 177 ARG 177 194 194 ARG ARG C . n 
C 1 178 PRO 178 195 195 PRO PRO C . n 
C 1 179 ASP 179 196 196 ASP ASP C . n 
C 1 180 ARG 180 197 197 ARG ARG C . n 
C 1 181 CYS 181 198 198 CYS CYS C . n 
C 1 182 LEU 182 199 199 LEU LEU C . n 
C 1 183 PRO 183 200 200 PRO PRO C . n 
C 1 184 VAL 184 201 201 VAL VAL C . n 
C 1 185 CYS 185 202 202 CYS CYS C . n 
C 1 186 ILE 186 203 203 ILE ILE C . n 
C 1 187 ASP 187 204 204 ASP ASP C . n 
C 1 188 VAL 188 205 205 VAL VAL C . n 
C 1 189 GLY 189 206 206 GLY GLY C . n 
C 1 190 THR 190 207 207 THR THR C . n 
C 1 191 ASP 191 208 208 ASP ASP C . n 
C 1 192 ASN 192 209 209 ASN ASN C . n 
C 1 193 ILE 193 210 210 ILE ILE C . n 
C 1 194 ALA 194 211 211 ALA ALA C . n 
C 1 195 LEU 195 212 212 LEU LEU C . n 
C 1 196 LEU 196 213 213 LEU LEU C . n 
C 1 197 LYS 197 214 214 LYS LYS C . n 
C 1 198 ASP 198 215 215 ASP ASP C . n 
C 1 199 PRO 199 216 216 PRO PRO C . n 
C 1 200 PHE 200 217 217 PHE PHE C . n 
C 1 201 TYR 201 218 218 TYR TYR C . n 
C 1 202 MET 202 219 219 MET MET C . n 
C 1 203 GLY 203 220 220 GLY GLY C . n 
C 1 204 LEU 204 221 221 LEU LEU C . n 
C 1 205 TYR 205 222 222 TYR TYR C . n 
C 1 206 GLN 206 223 223 GLN GLN C . n 
C 1 207 LYS 207 224 224 LYS LYS C . n 
C 1 208 ARG 208 225 225 ARG ARG C . n 
C 1 209 ASP 209 226 226 ASP ASP C . n 
C 1 210 ARG 210 227 227 ARG ARG C . n 
C 1 211 THR 211 228 228 THR THR C . n 
C 1 212 GLN 212 229 229 GLN GLN C . n 
C 1 213 GLN 213 230 230 GLN GLN C . n 
C 1 214 TYR 214 231 231 TYR TYR C . n 
C 1 215 ASP 215 232 232 ASP ASP C . n 
C 1 216 ASP 216 233 233 ASP ASP C . n 
C 1 217 LEU 217 234 234 LEU LEU C . n 
C 1 218 ILE 218 235 235 ILE ILE C . n 
C 1 219 ASP 219 236 236 ASP ASP C . n 
C 1 220 GLU 220 237 237 GLU GLU C . n 
C 1 221 PHE 221 238 238 PHE PHE C . n 
C 1 222 MET 222 239 239 MET MET C . n 
C 1 223 LYS 223 240 240 LYS LYS C . n 
C 1 224 ALA 224 241 241 ALA ALA C . n 
C 1 225 ILE 225 242 242 ILE ILE C . n 
C 1 226 THR 226 243 243 THR THR C . n 
C 1 227 ASP 227 244 244 ASP ASP C . n 
C 1 228 ARG 228 245 245 ARG ARG C . n 
C 1 229 TYR 229 246 246 TYR TYR C . n 
C 1 230 GLY 230 247 247 GLY GLY C . n 
C 1 231 ARG 231 248 248 ARG ARG C . n 
C 1 232 ASN 232 249 249 ASN ASN C . n 
C 1 233 THR 233 250 250 THR THR C . n 
C 1 234 LEU 234 251 251 LEU LEU C . n 
C 1 235 ILE 235 252 252 ILE ILE C . n 
C 1 236 GLN 236 253 253 GLN GLN C . n 
C 1 237 PHE 237 254 254 PHE PHE C . n 
C 1 238 GLU 238 255 255 GLU GLU C . n 
C 1 239 ASP 239 256 256 ASP ASP C . n 
C 1 240 PHE 240 257 257 PHE PHE C . n 
C 1 241 GLY 241 258 258 GLY GLY C . n 
C 1 242 ASN 242 259 259 ASN ASN C . n 
C 1 243 HIS 243 260 260 HIS HIS C . n 
C 1 244 ASN 244 261 261 ASN ASN C . n 
C 1 245 ALA 245 262 262 ALA ALA C . n 
C 1 246 PHE 246 263 263 PHE PHE C . n 
C 1 247 ARG 247 264 264 ARG ARG C . n 
C 1 248 PHE 248 265 265 PHE PHE C . n 
C 1 249 LEU 249 266 266 LEU LEU C . n 
C 1 250 ARG 250 267 267 ARG ARG C . n 
C 1 251 LYS 251 268 268 LYS LYS C . n 
C 1 252 TYR 252 269 269 TYR TYR C . n 
C 1 253 ARG 253 270 270 ARG ARG C . n 
C 1 254 GLU 254 271 271 GLU GLU C . n 
C 1 255 LYS 255 272 272 LYS LYS C . n 
C 1 256 TYR 256 273 273 TYR TYR C . n 
C 1 257 CYS 257 274 274 CYS CYS C . n 
C 1 258 THR 258 275 275 THR THR C . n 
C 1 259 PHE 259 276 276 PHE PHE C . n 
C 1 260 ASN 260 277 277 ASN ASN C . n 
C 1 261 ASP 261 278 278 ASP ASP C . n 
C 1 262 ASP 262 279 279 ASP ASP C . n 
C 1 263 ILE 263 280 280 ILE ILE C . n 
C 1 264 GLN 264 281 281 GLN GLN C . n 
C 1 265 GLY 265 282 282 GLY GLY C . n 
C 1 266 THR 266 283 283 THR THR C . n 
C 1 267 ALA 267 284 284 ALA ALA C . n 
C 1 268 ALA 268 285 285 ALA ALA C . n 
C 1 269 VAL 269 286 286 VAL VAL C . n 
C 1 270 ALA 270 287 287 ALA ALA C . n 
C 1 271 LEU 271 288 288 LEU LEU C . n 
C 1 272 ALA 272 289 289 ALA ALA C . n 
C 1 273 GLY 273 290 290 GLY GLY C . n 
C 1 274 LEU 274 291 291 LEU LEU C . n 
C 1 275 LEU 275 292 292 LEU LEU C . n 
C 1 276 ALA 276 293 293 ALA ALA C . n 
C 1 277 ALA 277 294 294 ALA ALA C . n 
C 1 278 GLN 278 295 295 GLN GLN C . n 
C 1 279 LYS 279 296 296 LYS LYS C . n 
C 1 280 VAL 280 297 297 VAL VAL C . n 
C 1 281 ILE 281 298 298 ILE ILE C . n 
C 1 282 SER 282 299 299 SER SER C . n 
C 1 283 LYS 283 300 300 LYS LYS C . n 
C 1 284 PRO 284 301 301 PRO PRO C . n 
C 1 285 ILE 285 302 302 ILE ILE C . n 
C 1 286 SER 286 303 303 SER SER C . n 
C 1 287 GLU 287 304 304 GLU GLU C . n 
C 1 288 HIS 288 305 305 HIS HIS C . n 
C 1 289 LYS 289 306 306 LYS LYS C . n 
C 1 290 ILE 290 307 307 ILE ILE C . n 
C 1 291 LEU 291 308 308 LEU LEU C . n 
C 1 292 PHE 292 309 309 PHE PHE C . n 
C 1 293 LEU 293 310 310 LEU LEU C . n 
C 1 294 GLY 294 311 311 GLY GLY C . n 
C 1 295 ALA 295 312 312 ALA ALA C . n 
C 1 296 GLY 296 313 313 GLY GLY C . n 
C 1 297 GLU 297 314 314 GLU GLU C . n 
C 1 298 ALA 298 315 315 ALA ALA C . n 
C 1 299 ALA 299 316 316 ALA ALA C . n 
C 1 300 LEU 300 317 317 LEU LEU C . n 
C 1 301 GLY 301 318 318 GLY GLY C . n 
C 1 302 ILE 302 319 319 ILE ILE C . n 
C 1 303 ALA 303 320 320 ALA ALA C . n 
C 1 304 ASN 304 321 321 ASN ASN C . n 
C 1 305 LEU 305 322 322 LEU LEU C . n 
C 1 306 ILE 306 323 323 ILE ILE C . n 
C 1 307 VAL 307 324 324 VAL VAL C . n 
C 1 308 MET 308 325 325 MET MET C . n 
C 1 309 SER 309 326 326 SER SER C . n 
C 1 310 MET 310 327 327 MET MET C . n 
C 1 311 VAL 311 328 328 VAL VAL C . n 
C 1 312 GLU 312 329 329 GLU GLU C . n 
C 1 313 ASN 313 330 330 ASN ASN C . n 
C 1 314 GLY 314 331 331 GLY GLY C . n 
C 1 315 LEU 315 332 332 LEU LEU C . n 
C 1 316 SER 316 333 333 SER SER C . n 
C 1 317 GLU 317 334 334 GLU GLU C . n 
C 1 318 GLN 318 335 335 GLN GLN C . n 
C 1 319 GLU 319 336 336 GLU GLU C . n 
C 1 320 ALA 320 337 337 ALA ALA C . n 
C 1 321 GLN 321 338 338 GLN GLN C . n 
C 1 322 LYS 322 339 339 LYS LYS C . n 
C 1 323 LYS 323 340 340 LYS LYS C . n 
C 1 324 ILE 324 341 341 ILE ILE C . n 
C 1 325 TRP 325 342 342 TRP TRP C . n 
C 1 326 MET 326 343 343 MET MET C . n 
C 1 327 PHE 327 344 344 PHE PHE C . n 
C 1 328 ASP 328 345 345 ASP ASP C . n 
C 1 329 LYS 329 346 346 LYS LYS C . n 
C 1 330 TYR 330 347 347 TYR TYR C . n 
C 1 331 GLY 331 348 348 GLY GLY C . n 
C 1 332 LEU 332 349 349 LEU LEU C . n 
C 1 333 LEU 333 350 350 LEU LEU C . n 
C 1 334 VAL 334 351 351 VAL VAL C . n 
C 1 335 LYS 335 352 352 LYS LYS C . n 
C 1 336 GLY 336 353 353 GLY GLY C . n 
C 1 337 ARG 337 354 354 ARG ARG C . n 
C 1 338 LYS 338 355 355 LYS LYS C . n 
C 1 339 ALA 339 356 356 ALA ALA C . n 
C 1 340 LYS 340 357 357 LYS LYS C . n 
C 1 341 ILE 341 358 358 ILE ILE C . n 
C 1 342 ASP 342 359 359 ASP ASP C . n 
C 1 343 SER 343 360 360 SER SER C . n 
C 1 344 TYR 344 361 361 TYR TYR C . n 
C 1 345 GLN 345 362 362 GLN GLN C . n 
C 1 346 GLU 346 363 363 GLU GLU C . n 
C 1 347 PRO 347 364 364 PRO PRO C . n 
C 1 348 PHE 348 365 365 PHE PHE C . n 
C 1 349 THR 349 366 366 THR THR C . n 
C 1 350 HIS 350 367 367 HIS HIS C . n 
C 1 351 SER 351 368 368 SER SER C . n 
C 1 352 ALA 352 369 369 ALA ALA C . n 
C 1 353 PRO 353 370 370 PRO PRO C . n 
C 1 354 GLU 354 371 371 GLU GLU C . n 
C 1 355 SER 355 372 372 SER SER C . n 
C 1 356 ILE 356 373 373 ILE ILE C . n 
C 1 357 PRO 357 374 374 PRO PRO C . n 
C 1 358 ASP 358 375 375 ASP ASP C . n 
C 1 359 THR 359 376 376 THR THR C . n 
C 1 360 PHE 360 377 377 PHE PHE C . n 
C 1 361 GLU 361 378 378 GLU GLU C . n 
C 1 362 ASP 362 379 379 ASP ASP C . n 
C 1 363 ALA 363 380 380 ALA ALA C . n 
C 1 364 VAL 364 381 381 VAL VAL C . n 
C 1 365 ASN 365 382 382 ASN ASN C . n 
C 1 366 ILE 366 383 383 ILE ILE C . n 
C 1 367 LEU 367 384 384 LEU LEU C . n 
C 1 368 LYS 368 385 385 LYS LYS C . n 
C 1 369 PRO 369 386 386 PRO PRO C . n 
C 1 370 SER 370 387 387 SER SER C . n 
C 1 371 THR 371 388 388 THR THR C . n 
C 1 372 ILE 372 389 389 ILE ILE C . n 
C 1 373 ILE 373 390 390 ILE ILE C . n 
C 1 374 GLY 374 391 391 GLY GLY C . n 
C 1 375 VAL 375 392 392 VAL VAL C . n 
C 1 376 ALA 376 393 393 ALA ALA C . n 
C 1 377 GLY 377 394 394 GLY GLY C . n 
C 1 378 ALA 378 395 395 ALA ALA C . n 
C 1 379 GLY 379 396 396 GLY GLY C . n 
C 1 380 ARG 380 397 397 ARG ARG C . n 
C 1 381 LEU 381 398 398 LEU LEU C . n 
C 1 382 PHE 382 399 399 PHE PHE C . n 
C 1 383 THR 383 400 400 THR THR C . n 
C 1 384 PRO 384 401 401 PRO PRO C . n 
C 1 385 ASP 385 402 402 ASP ASP C . n 
C 1 386 VAL 386 403 403 VAL VAL C . n 
C 1 387 ILE 387 404 404 ILE ILE C . n 
C 1 388 ARG 388 405 405 ARG ARG C . n 
C 1 389 ALA 389 406 406 ALA ALA C . n 
C 1 390 MET 390 407 407 MET MET C . n 
C 1 391 ALA 391 408 408 ALA ALA C . n 
C 1 392 SER 392 409 409 SER SER C . n 
C 1 393 ILE 393 410 410 ILE ILE C . n 
C 1 394 ASN 394 411 411 ASN ASN C . n 
C 1 395 GLU 395 412 412 GLU GLU C . n 
C 1 396 ARG 396 413 413 ARG ARG C . n 
C 1 397 PRO 397 414 414 PRO PRO C . n 
C 1 398 VAL 398 415 415 VAL VAL C . n 
C 1 399 ILE 399 416 416 ILE ILE C . n 
C 1 400 PHE 400 417 417 PHE PHE C . n 
C 1 401 ALA 401 418 418 ALA ALA C . n 
C 1 402 LEU 402 419 419 LEU LEU C . n 
C 1 403 SER 403 420 420 SER SER C . n 
C 1 404 ASN 404 421 421 ASN ASN C . n 
C 1 405 PRO 405 422 422 PRO PRO C . n 
C 1 406 THR 406 423 423 THR THR C . n 
C 1 407 ALA 407 424 424 ALA ALA C . n 
C 1 408 GLN 408 425 425 GLN GLN C . n 
C 1 409 ALA 409 426 426 ALA ALA C . n 
C 1 410 GLU 410 427 427 GLU GLU C . n 
C 1 411 CYS 411 428 428 CYS CYS C . n 
C 1 412 THR 412 429 429 THR THR C . n 
C 1 413 ALA 413 430 430 ALA ALA C . n 
C 1 414 GLU 414 431 431 GLU GLU C . n 
C 1 415 GLU 415 432 432 GLU GLU C . n 
C 1 416 ALA 416 433 433 ALA ALA C . n 
C 1 417 TYR 417 434 434 TYR TYR C . n 
C 1 418 THR 418 435 435 THR THR C . n 
C 1 419 LEU 419 436 436 LEU LEU C . n 
C 1 420 THR 420 437 437 THR THR C . n 
C 1 421 GLU 421 438 438 GLU GLU C . n 
C 1 422 GLY 422 439 439 GLY GLY C . n 
C 1 423 ARG 423 440 440 ARG ARG C . n 
C 1 424 CYS 424 441 441 CYS CYS C . n 
C 1 425 LEU 425 442 442 LEU LEU C . n 
C 1 426 PHE 426 443 443 PHE PHE C . n 
C 1 427 ALA 427 444 444 ALA ALA C . n 
C 1 428 SER 428 445 445 SER SER C . n 
C 1 429 GLY 429 446 446 GLY GLY C . n 
C 1 430 SER 430 447 447 SER SER C . n 
C 1 431 PRO 431 448 448 PRO PRO C . n 
C 1 432 PHE 432 449 449 PHE PHE C . n 
C 1 433 GLY 433 450 450 GLY GLY C . n 
C 1 434 PRO 434 451 451 PRO PRO C . n 
C 1 435 VAL 435 452 452 VAL VAL C . n 
C 1 436 LYS 436 453 453 LYS LYS C . n 
C 1 437 LEU 437 454 454 LEU LEU C . n 
C 1 438 THR 438 455 455 THR THR C . n 
C 1 439 ASP 439 456 456 ASP ASP C . n 
C 1 440 GLY 440 457 457 GLY GLY C . n 
C 1 441 ARG 441 458 458 ARG ARG C . n 
C 1 442 VAL 442 459 459 VAL VAL C . n 
C 1 443 PHE 443 460 460 PHE PHE C . n 
C 1 444 THR 444 461 461 THR THR C . n 
C 1 445 PRO 445 462 462 PRO PRO C . n 
C 1 446 GLY 446 463 463 GLY GLY C . n 
C 1 447 GLN 447 464 464 GLN GLN C . n 
C 1 448 GLY 448 465 465 GLY GLY C . n 
C 1 449 ASN 449 466 466 ASN ASN C . n 
C 1 450 ASN 450 467 467 ASN ASN C . n 
C 1 451 VAL 451 468 468 VAL VAL C . n 
C 1 452 TYR 452 469 469 TYR TYR C . n 
C 1 453 ILE 453 470 470 ILE ILE C . n 
C 1 454 PHE 454 471 471 PHE PHE C . n 
C 1 455 PRO 455 472 472 PRO PRO C . n 
C 1 456 GLY 456 473 473 GLY GLY C . n 
C 1 457 VAL 457 474 474 VAL VAL C . n 
C 1 458 ALA 458 475 475 ALA ALA C . n 
C 1 459 LEU 459 476 476 LEU LEU C . n 
C 1 460 ALA 460 477 477 ALA ALA C . n 
C 1 461 VAL 461 478 478 VAL VAL C . n 
C 1 462 ILE 462 479 479 ILE ILE C . n 
C 1 463 LEU 463 480 480 LEU LEU C . n 
C 1 464 CYS 464 481 481 CYS CYS C . n 
C 1 465 ASN 465 482 482 ASN ASN C . n 
C 1 466 THR 466 483 483 THR THR C . n 
C 1 467 ARG 467 484 484 ARG ARG C . n 
C 1 468 HIS 468 485 485 HIS HIS C . n 
C 1 469 ILE 469 486 486 ILE ILE C . n 
C 1 470 SER 470 487 487 SER SER C . n 
C 1 471 ASP 471 488 488 ASP ASP C . n 
C 1 472 SER 472 489 489 SER SER C . n 
C 1 473 VAL 473 490 490 VAL VAL C . n 
C 1 474 PHE 474 491 491 PHE PHE C . n 
C 1 475 LEU 475 492 492 LEU LEU C . n 
C 1 476 GLU 476 493 493 GLU GLU C . n 
C 1 477 ALA 477 494 494 ALA ALA C . n 
C 1 478 ALA 478 495 495 ALA ALA C . n 
C 1 479 LYS 479 496 496 LYS LYS C . n 
C 1 480 ALA 480 497 497 ALA ALA C . n 
C 1 481 LEU 481 498 498 LEU LEU C . n 
C 1 482 THR 482 499 499 THR THR C . n 
C 1 483 SER 483 500 500 SER SER C . n 
C 1 484 GLN 484 501 501 GLN GLN C . n 
C 1 485 LEU 485 502 502 LEU LEU C . n 
C 1 486 THR 486 503 503 THR THR C . n 
C 1 487 ASP 487 504 504 ASP ASP C . n 
C 1 488 GLU 488 505 505 GLU GLU C . n 
C 1 489 GLU 489 506 506 GLU GLU C . n 
C 1 490 LEU 490 507 507 LEU LEU C . n 
C 1 491 ALA 491 508 508 ALA ALA C . n 
C 1 492 GLN 492 509 509 GLN GLN C . n 
C 1 493 GLY 493 510 510 GLY GLY C . n 
C 1 494 ARG 494 511 511 ARG ARG C . n 
C 1 495 LEU 495 512 512 LEU LEU C . n 
C 1 496 TYR 496 513 513 TYR TYR C . n 
C 1 497 PRO 497 514 514 PRO PRO C . n 
C 1 498 PRO 498 515 515 PRO PRO C . n 
C 1 499 LEU 499 516 516 LEU LEU C . n 
C 1 500 ALA 500 517 517 ALA ALA C . n 
C 1 501 ASN 501 518 518 ASN ASN C . n 
C 1 502 ILE 502 519 519 ILE ILE C . n 
C 1 503 GLN 503 520 520 GLN GLN C . n 
C 1 504 GLU 504 521 521 GLU GLU C . n 
C 1 505 VAL 505 522 522 VAL VAL C . n 
C 1 506 SER 506 523 523 SER SER C . n 
C 1 507 ILE 507 524 524 ILE ILE C . n 
C 1 508 ASN 508 525 525 ASN ASN C . n 
C 1 509 ILE 509 526 526 ILE ILE C . n 
C 1 510 ALA 510 527 527 ALA ALA C . n 
C 1 511 ILE 511 528 528 ILE ILE C . n 
C 1 512 LYS 512 529 529 LYS LYS C . n 
C 1 513 VAL 513 530 530 VAL VAL C . n 
C 1 514 THR 514 531 531 THR THR C . n 
C 1 515 GLU 515 532 532 GLU GLU C . n 
C 1 516 TYR 516 533 533 TYR TYR C . n 
C 1 517 LEU 517 534 534 LEU LEU C . n 
C 1 518 TYR 518 535 535 TYR TYR C . n 
C 1 519 ALA 519 536 536 ALA ALA C . n 
C 1 520 ASN 520 537 537 ASN ASN C . n 
C 1 521 LYS 521 538 538 LYS LYS C . n 
C 1 522 MET 522 539 539 MET MET C . n 
C 1 523 ALA 523 540 540 ALA ALA C . n 
C 1 524 PHE 524 541 541 PHE PHE C . n 
C 1 525 ARG 525 542 542 ARG ARG C . n 
C 1 526 TYR 526 543 543 TYR TYR C . n 
C 1 527 PRO 527 544 544 PRO PRO C . n 
C 1 528 GLU 528 545 545 GLU GLU C . n 
C 1 529 PRO 529 546 546 PRO PRO C . n 
C 1 530 GLU 530 547 547 GLU GLU C . n 
C 1 531 ASP 531 548 548 ASP ASP C . n 
C 1 532 LYS 532 549 549 LYS LYS C . n 
C 1 533 ALA 533 550 550 ALA ALA C . n 
C 1 534 LYS 534 551 551 LYS LYS C . n 
C 1 535 TYR 535 552 552 TYR TYR C . n 
C 1 536 VAL 536 553 553 VAL VAL C . n 
C 1 537 LYS 537 554 554 LYS LYS C . n 
C 1 538 GLU 538 555 555 GLU GLU C . n 
C 1 539 ARG 539 556 556 ARG ARG C . n 
C 1 540 THR 540 557 557 THR THR C . n 
C 1 541 TRP 541 558 558 TRP TRP C . n 
C 1 542 ARG 542 559 559 ARG ARG C . n 
C 1 543 SER 543 560 560 SER SER C . n 
C 1 544 GLU 544 561 561 GLU GLU C . n 
C 1 545 TYR 545 562 562 TYR TYR C . n 
C 1 546 ASP 546 563 563 ASP ASP C . n 
C 1 547 SER 547 564 564 SER SER C . n 
C 1 548 LEU 548 565 565 LEU LEU C . n 
C 1 549 LEU 549 566 566 LEU LEU C . n 
C 1 550 PRO 550 567 567 PRO PRO C . n 
C 1 551 ASP 551 568 568 ASP ASP C . n 
C 1 552 VAL 552 569 569 VAL VAL C . n 
C 1 553 TYR 553 570 570 TYR TYR C . n 
C 1 554 GLU 554 571 571 GLU GLU C . n 
C 1 555 TRP 555 572 572 TRP TRP C . n 
C 1 556 PRO 556 573 573 PRO PRO C . n 
C 1 557 GLU 557 574 574 GLU GLU C . n 
C 1 558 SER 558 575 575 SER SER C . n 
C 1 559 ALA 559 576 ?   ?   ?   C . n 
C 1 560 SER 560 577 577 SER SER C . n 
C 1 561 SER 561 578 578 SER SER C . n 
C 1 562 PRO 562 579 579 PRO PRO C . n 
C 1 563 PRO 563 580 580 PRO PRO C . n 
C 1 564 VAL 564 581 ?   ?   ?   C . n 
C 1 565 ILE 565 582 ?   ?   ?   C . n 
C 1 566 THR 566 583 ?   ?   ?   C . n 
C 1 567 GLU 567 584 ?   ?   ?   C . n 
C 1 568 LEU 568 585 ?   ?   ?   C . n 
C 1 569 GLU 569 586 ?   ?   ?   C . n 
C 1 570 HIS 570 587 ?   ?   ?   C . n 
C 1 571 HIS 571 588 ?   ?   ?   C . n 
C 1 572 HIS 572 589 ?   ?   ?   C . n 
C 1 573 HIS 573 590 ?   ?   ?   C . n 
C 1 574 HIS 574 591 ?   ?   ?   C . n 
C 1 575 HIS 575 592 ?   ?   ?   C . n 
D 1 1   MET 1   18  ?   ?   ?   D . n 
D 1 2   LEU 2   19  ?   ?   ?   D . n 
D 1 3   HIS 3   20  ?   ?   ?   D . n 
D 1 4   ILE 4   21  ?   ?   ?   D . n 
D 1 5   LYS 5   22  ?   ?   ?   D . n 
D 1 6   GLU 6   23  23  GLU GLU D . n 
D 1 7   LYS 7   24  24  LYS LYS D . n 
D 1 8   GLY 8   25  25  GLY GLY D . n 
D 1 9   LYS 9   26  26  LYS LYS D . n 
D 1 10  PRO 10  27  27  PRO PRO D . n 
D 1 11  LEU 11  28  28  LEU LEU D . n 
D 1 12  MET 12  29  29  MET MET D . n 
D 1 13  LEU 13  30  30  LEU LEU D . n 
D 1 14  ASN 14  31  31  ASN ASN D . n 
D 1 15  PRO 15  32  32  PRO PRO D . n 
D 1 16  ARG 16  33  33  ARG ARG D . n 
D 1 17  THR 17  34  34  THR THR D . n 
D 1 18  ASN 18  35  35  ASN ASN D . n 
D 1 19  LYS 19  36  36  LYS LYS D . n 
D 1 20  GLY 20  37  37  GLY GLY D . n 
D 1 21  MET 21  38  38  MET MET D . n 
D 1 22  ALA 22  39  39  ALA ALA D . n 
D 1 23  PHE 23  40  40  PHE PHE D . n 
D 1 24  THR 24  41  41  THR THR D . n 
D 1 25  LEU 25  42  42  LEU LEU D . n 
D 1 26  GLN 26  43  43  GLN GLN D . n 
D 1 27  GLU 27  44  44  GLU GLU D . n 
D 1 28  ARG 28  45  45  ARG ARG D . n 
D 1 29  GLN 29  46  46  GLN GLN D . n 
D 1 30  MET 30  47  47  MET MET D . n 
D 1 31  LEU 31  48  48  LEU LEU D . n 
D 1 32  GLY 32  49  49  GLY GLY D . n 
D 1 33  LEU 33  50  50  LEU LEU D . n 
D 1 34  GLN 34  51  51  GLN GLN D . n 
D 1 35  GLY 35  52  52  GLY GLY D . n 
D 1 36  LEU 36  53  53  LEU LEU D . n 
D 1 37  LEU 37  54  54  LEU LEU D . n 
D 1 38  PRO 38  55  55  PRO PRO D . n 
D 1 39  PRO 39  56  56  PRO PRO D . n 
D 1 40  LYS 40  57  57  LYS LYS D . n 
D 1 41  ILE 41  58  58  ILE ILE D . n 
D 1 42  GLU 42  59  59  GLU GLU D . n 
D 1 43  THR 43  60  60  THR THR D . n 
D 1 44  GLN 44  61  61  GLN GLN D . n 
D 1 45  ASP 45  62  62  ASP ASP D . n 
D 1 46  ILE 46  63  63  ILE ILE D . n 
D 1 47  GLN 47  64  64  GLN GLN D . n 
D 1 48  ALA 48  65  65  ALA ALA D . n 
D 1 49  LEU 49  66  66  LEU LEU D . n 
D 1 50  ARG 50  67  67  ARG ARG D . n 
D 1 51  PHE 51  68  68  PHE PHE D . n 
D 1 52  HIS 52  69  69  HIS HIS D . n 
D 1 53  ARG 53  70  70  ARG ARG D . n 
D 1 54  ASN 54  71  71  ASN ASN D . n 
D 1 55  LEU 55  72  72  LEU LEU D . n 
D 1 56  LYS 56  73  73  LYS LYS D . n 
D 1 57  LYS 57  74  74  LYS LYS D . n 
D 1 58  MET 58  75  75  MET MET D . n 
D 1 59  THR 59  76  76  THR THR D . n 
D 1 60  SER 60  77  77  SER SER D . n 
D 1 61  PRO 61  78  78  PRO PRO D . n 
D 1 62  LEU 62  79  79  LEU LEU D . n 
D 1 63  GLU 63  80  80  GLU GLU D . n 
D 1 64  LYS 64  81  81  LYS LYS D . n 
D 1 65  TYR 65  82  82  TYR TYR D . n 
D 1 66  ILE 66  83  83  ILE ILE D . n 
D 1 67  TYR 67  84  84  TYR TYR D . n 
D 1 68  ILE 68  85  85  ILE ILE D . n 
D 1 69  MET 69  86  86  MET MET D . n 
D 1 70  GLY 70  87  87  GLY GLY D . n 
D 1 71  ILE 71  88  88  ILE ILE D . n 
D 1 72  GLN 72  89  89  GLN GLN D . n 
D 1 73  GLU 73  90  90  GLU GLU D . n 
D 1 74  ARG 74  91  91  ARG ARG D . n 
D 1 75  ASN 75  92  92  ASN ASN D . n 
D 1 76  GLU 76  93  93  GLU GLU D . n 
D 1 77  LYS 77  94  94  LYS LYS D . n 
D 1 78  LEU 78  95  95  LEU LEU D . n 
D 1 79  PHE 79  96  96  PHE PHE D . n 
D 1 80  TYR 80  97  97  TYR TYR D . n 
D 1 81  ARG 81  98  98  ARG ARG D . n 
D 1 82  ILE 82  99  99  ILE ILE D . n 
D 1 83  LEU 83  100 100 LEU LEU D . n 
D 1 84  GLN 84  101 101 GLN GLN D . n 
D 1 85  ASP 85  102 102 ASP ASP D . n 
D 1 86  ASP 86  103 103 ASP ASP D . n 
D 1 87  ILE 87  104 104 ILE ILE D . n 
D 1 88  GLU 88  105 105 GLU GLU D . n 
D 1 89  SER 89  106 106 SER SER D . n 
D 1 90  LEU 90  107 107 LEU LEU D . n 
D 1 91  MET 91  108 108 MET MET D . n 
D 1 92  PRO 92  109 109 PRO PRO D . n 
D 1 93  ILE 93  110 110 ILE ILE D . n 
D 1 94  VAL 94  111 111 VAL VAL D . n 
D 1 95  TYR 95  112 112 TYR TYR D . n 
D 1 96  THR 96  113 113 THR THR D . n 
D 1 97  PRO 97  114 114 PRO PRO D . n 
D 1 98  THR 98  115 115 THR THR D . n 
D 1 99  VAL 99  116 116 VAL VAL D . n 
D 1 100 GLY 100 117 117 GLY GLY D . n 
D 1 101 LEU 101 118 118 LEU LEU D . n 
D 1 102 ALA 102 119 119 ALA ALA D . n 
D 1 103 CSX 103 120 120 CSX CSX D . n 
D 1 104 SER 104 121 121 SER SER D . n 
D 1 105 GLN 105 122 122 GLN GLN D . n 
D 1 106 TYR 106 123 123 TYR TYR D . n 
D 1 107 GLY 107 124 124 GLY GLY D . n 
D 1 108 HIS 108 125 125 HIS HIS D . n 
D 1 109 ILE 109 126 126 ILE ILE D . n 
D 1 110 PHE 110 127 127 PHE PHE D . n 
D 1 111 ARG 111 128 128 ARG ARG D . n 
D 1 112 ARG 112 129 129 ARG ARG D . n 
D 1 113 PRO 113 130 130 PRO PRO D . n 
D 1 114 LYS 114 131 131 LYS LYS D . n 
D 1 115 GLY 115 132 132 GLY GLY D . n 
D 1 116 LEU 116 133 133 LEU LEU D . n 
D 1 117 PHE 117 134 134 PHE PHE D . n 
D 1 118 ILE 118 135 135 ILE ILE D . n 
D 1 119 SER 119 136 136 SER SER D . n 
D 1 120 ILE 120 137 137 ILE ILE D . n 
D 1 121 SER 121 138 138 SER SER D . n 
D 1 122 ASP 122 139 139 ASP ASP D . n 
D 1 123 ARG 123 140 140 ARG ARG D . n 
D 1 124 GLY 124 141 141 GLY GLY D . n 
D 1 125 HIS 125 142 142 HIS HIS D . n 
D 1 126 VAL 126 143 143 VAL VAL D . n 
D 1 127 ARG 127 144 144 ARG ARG D . n 
D 1 128 SER 128 145 145 SER SER D . n 
D 1 129 ILE 129 146 146 ILE ILE D . n 
D 1 130 VAL 130 147 147 VAL VAL D . n 
D 1 131 ASP 131 148 148 ASP ASP D . n 
D 1 132 ASN 132 149 149 ASN ASN D . n 
D 1 133 TRP 133 150 150 TRP TRP D . n 
D 1 134 PRO 134 151 151 PRO PRO D . n 
D 1 135 GLU 135 152 152 GLU GLU D . n 
D 1 136 ASN 136 153 153 ASN ASN D . n 
D 1 137 HIS 137 154 154 HIS HIS D . n 
D 1 138 VAL 138 155 155 VAL VAL D . n 
D 1 139 LYS 139 156 156 LYS LYS D . n 
D 1 140 ALA 140 157 157 ALA ALA D . n 
D 1 141 VAL 141 158 158 VAL VAL D . n 
D 1 142 VAL 142 159 159 VAL VAL D . n 
D 1 143 VAL 143 160 160 VAL VAL D . n 
D 1 144 THR 144 161 161 THR THR D . n 
D 1 145 ASP 145 162 162 ASP ASP D . n 
D 1 146 GLY 146 163 163 GLY GLY D . n 
D 1 147 GLU 147 164 164 GLU GLU D . n 
D 1 148 ARG 148 165 165 ARG ARG D . n 
D 1 149 ILE 149 166 166 ILE ILE D . n 
D 1 150 LEU 150 167 167 LEU LEU D . n 
D 1 151 GLY 151 168 168 GLY GLY D . n 
D 1 152 LEU 152 169 169 LEU LEU D . n 
D 1 153 GLY 153 170 170 GLY GLY D . n 
D 1 154 ASP 154 171 171 ASP ASP D . n 
D 1 155 LEU 155 172 172 LEU LEU D . n 
D 1 156 GLY 156 173 173 GLY GLY D . n 
D 1 157 VAL 157 174 174 VAL VAL D . n 
D 1 158 TYR 158 175 175 TYR TYR D . n 
D 1 159 GLY 159 176 176 GLY GLY D . n 
D 1 160 MET 160 177 177 MET MET D . n 
D 1 161 GLY 161 178 178 GLY GLY D . n 
D 1 162 ILE 162 179 179 ILE ILE D . n 
D 1 163 PRO 163 180 180 PRO PRO D . n 
D 1 164 VAL 164 181 181 VAL VAL D . n 
D 1 165 GLY 165 182 182 GLY GLY D . n 
D 1 166 LYS 166 183 183 LYS LYS D . n 
D 1 167 LEU 167 184 184 LEU LEU D . n 
D 1 168 CYS 168 185 185 CYS CYS D . n 
D 1 169 LEU 169 186 186 LEU LEU D . n 
D 1 170 TYR 170 187 187 TYR TYR D . n 
D 1 171 THR 171 188 188 THR THR D . n 
D 1 172 ALA 172 189 189 ALA ALA D . n 
D 1 173 CYS 173 190 190 CYS CYS D . n 
D 1 174 ALA 174 191 191 ALA ALA D . n 
D 1 175 GLY 175 192 192 GLY GLY D . n 
D 1 176 ILE 176 193 193 ILE ILE D . n 
D 1 177 ARG 177 194 194 ARG ARG D . n 
D 1 178 PRO 178 195 195 PRO PRO D . n 
D 1 179 ASP 179 196 196 ASP ASP D . n 
D 1 180 ARG 180 197 197 ARG ARG D . n 
D 1 181 CYS 181 198 198 CYS CYS D . n 
D 1 182 LEU 182 199 199 LEU LEU D . n 
D 1 183 PRO 183 200 200 PRO PRO D . n 
D 1 184 VAL 184 201 201 VAL VAL D . n 
D 1 185 CYS 185 202 202 CYS CYS D . n 
D 1 186 ILE 186 203 203 ILE ILE D . n 
D 1 187 ASP 187 204 204 ASP ASP D . n 
D 1 188 VAL 188 205 205 VAL VAL D . n 
D 1 189 GLY 189 206 206 GLY GLY D . n 
D 1 190 THR 190 207 207 THR THR D . n 
D 1 191 ASP 191 208 208 ASP ASP D . n 
D 1 192 ASN 192 209 209 ASN ASN D . n 
D 1 193 ILE 193 210 210 ILE ILE D . n 
D 1 194 ALA 194 211 211 ALA ALA D . n 
D 1 195 LEU 195 212 212 LEU LEU D . n 
D 1 196 LEU 196 213 213 LEU LEU D . n 
D 1 197 LYS 197 214 214 LYS LYS D . n 
D 1 198 ASP 198 215 215 ASP ASP D . n 
D 1 199 PRO 199 216 216 PRO PRO D . n 
D 1 200 PHE 200 217 217 PHE PHE D . n 
D 1 201 TYR 201 218 218 TYR TYR D . n 
D 1 202 MET 202 219 219 MET MET D . n 
D 1 203 GLY 203 220 220 GLY GLY D . n 
D 1 204 LEU 204 221 221 LEU LEU D . n 
D 1 205 TYR 205 222 222 TYR TYR D . n 
D 1 206 GLN 206 223 223 GLN GLN D . n 
D 1 207 LYS 207 224 224 LYS LYS D . n 
D 1 208 ARG 208 225 225 ARG ARG D . n 
D 1 209 ASP 209 226 226 ASP ASP D . n 
D 1 210 ARG 210 227 227 ARG ARG D . n 
D 1 211 THR 211 228 228 THR THR D . n 
D 1 212 GLN 212 229 229 GLN GLN D . n 
D 1 213 GLN 213 230 230 GLN GLN D . n 
D 1 214 TYR 214 231 231 TYR TYR D . n 
D 1 215 ASP 215 232 232 ASP ASP D . n 
D 1 216 ASP 216 233 233 ASP ASP D . n 
D 1 217 LEU 217 234 234 LEU LEU D . n 
D 1 218 ILE 218 235 235 ILE ILE D . n 
D 1 219 ASP 219 236 236 ASP ASP D . n 
D 1 220 GLU 220 237 237 GLU GLU D . n 
D 1 221 PHE 221 238 238 PHE PHE D . n 
D 1 222 MET 222 239 239 MET MET D . n 
D 1 223 LYS 223 240 240 LYS LYS D . n 
D 1 224 ALA 224 241 241 ALA ALA D . n 
D 1 225 ILE 225 242 242 ILE ILE D . n 
D 1 226 THR 226 243 243 THR THR D . n 
D 1 227 ASP 227 244 244 ASP ASP D . n 
D 1 228 ARG 228 245 245 ARG ARG D . n 
D 1 229 TYR 229 246 246 TYR TYR D . n 
D 1 230 GLY 230 247 247 GLY GLY D . n 
D 1 231 ARG 231 248 248 ARG ARG D . n 
D 1 232 ASN 232 249 249 ASN ASN D . n 
D 1 233 THR 233 250 250 THR THR D . n 
D 1 234 LEU 234 251 251 LEU LEU D . n 
D 1 235 ILE 235 252 252 ILE ILE D . n 
D 1 236 GLN 236 253 253 GLN GLN D . n 
D 1 237 PHE 237 254 254 PHE PHE D . n 
D 1 238 GLU 238 255 255 GLU GLU D . n 
D 1 239 ASP 239 256 256 ASP ASP D . n 
D 1 240 PHE 240 257 257 PHE PHE D . n 
D 1 241 GLY 241 258 258 GLY GLY D . n 
D 1 242 ASN 242 259 259 ASN ASN D . n 
D 1 243 HIS 243 260 260 HIS HIS D . n 
D 1 244 ASN 244 261 261 ASN ASN D . n 
D 1 245 ALA 245 262 262 ALA ALA D . n 
D 1 246 PHE 246 263 263 PHE PHE D . n 
D 1 247 ARG 247 264 264 ARG ARG D . n 
D 1 248 PHE 248 265 265 PHE PHE D . n 
D 1 249 LEU 249 266 266 LEU LEU D . n 
D 1 250 ARG 250 267 267 ARG ARG D . n 
D 1 251 LYS 251 268 268 LYS LYS D . n 
D 1 252 TYR 252 269 269 TYR TYR D . n 
D 1 253 ARG 253 270 270 ARG ARG D . n 
D 1 254 GLU 254 271 271 GLU GLU D . n 
D 1 255 LYS 255 272 272 LYS LYS D . n 
D 1 256 TYR 256 273 273 TYR TYR D . n 
D 1 257 CYS 257 274 274 CYS CYS D . n 
D 1 258 THR 258 275 275 THR THR D . n 
D 1 259 PHE 259 276 276 PHE PHE D . n 
D 1 260 ASN 260 277 277 ASN ASN D . n 
D 1 261 ASP 261 278 278 ASP ASP D . n 
D 1 262 ASP 262 279 279 ASP ASP D . n 
D 1 263 ILE 263 280 280 ILE ILE D . n 
D 1 264 GLN 264 281 281 GLN GLN D . n 
D 1 265 GLY 265 282 282 GLY GLY D . n 
D 1 266 THR 266 283 283 THR THR D . n 
D 1 267 ALA 267 284 284 ALA ALA D . n 
D 1 268 ALA 268 285 285 ALA ALA D . n 
D 1 269 VAL 269 286 286 VAL VAL D . n 
D 1 270 ALA 270 287 287 ALA ALA D . n 
D 1 271 LEU 271 288 288 LEU LEU D . n 
D 1 272 ALA 272 289 289 ALA ALA D . n 
D 1 273 GLY 273 290 290 GLY GLY D . n 
D 1 274 LEU 274 291 291 LEU LEU D . n 
D 1 275 LEU 275 292 292 LEU LEU D . n 
D 1 276 ALA 276 293 293 ALA ALA D . n 
D 1 277 ALA 277 294 294 ALA ALA D . n 
D 1 278 GLN 278 295 295 GLN GLN D . n 
D 1 279 LYS 279 296 296 LYS LYS D . n 
D 1 280 VAL 280 297 297 VAL VAL D . n 
D 1 281 ILE 281 298 298 ILE ILE D . n 
D 1 282 SER 282 299 299 SER SER D . n 
D 1 283 LYS 283 300 300 LYS LYS D . n 
D 1 284 PRO 284 301 301 PRO PRO D . n 
D 1 285 ILE 285 302 302 ILE ILE D . n 
D 1 286 SER 286 303 303 SER SER D . n 
D 1 287 GLU 287 304 304 GLU GLU D . n 
D 1 288 HIS 288 305 305 HIS HIS D . n 
D 1 289 LYS 289 306 306 LYS LYS D . n 
D 1 290 ILE 290 307 307 ILE ILE D . n 
D 1 291 LEU 291 308 308 LEU LEU D . n 
D 1 292 PHE 292 309 309 PHE PHE D . n 
D 1 293 LEU 293 310 310 LEU LEU D . n 
D 1 294 GLY 294 311 311 GLY GLY D . n 
D 1 295 ALA 295 312 312 ALA ALA D . n 
D 1 296 GLY 296 313 313 GLY GLY D . n 
D 1 297 GLU 297 314 314 GLU GLU D . n 
D 1 298 ALA 298 315 315 ALA ALA D . n 
D 1 299 ALA 299 316 316 ALA ALA D . n 
D 1 300 LEU 300 317 317 LEU LEU D . n 
D 1 301 GLY 301 318 318 GLY GLY D . n 
D 1 302 ILE 302 319 319 ILE ILE D . n 
D 1 303 ALA 303 320 320 ALA ALA D . n 
D 1 304 ASN 304 321 321 ASN ASN D . n 
D 1 305 LEU 305 322 322 LEU LEU D . n 
D 1 306 ILE 306 323 323 ILE ILE D . n 
D 1 307 VAL 307 324 324 VAL VAL D . n 
D 1 308 MET 308 325 325 MET MET D . n 
D 1 309 SER 309 326 326 SER SER D . n 
D 1 310 MET 310 327 327 MET MET D . n 
D 1 311 VAL 311 328 328 VAL VAL D . n 
D 1 312 GLU 312 329 329 GLU GLU D . n 
D 1 313 ASN 313 330 330 ASN ASN D . n 
D 1 314 GLY 314 331 331 GLY GLY D . n 
D 1 315 LEU 315 332 332 LEU LEU D . n 
D 1 316 SER 316 333 333 SER SER D . n 
D 1 317 GLU 317 334 334 GLU GLU D . n 
D 1 318 GLN 318 335 335 GLN GLN D . n 
D 1 319 GLU 319 336 336 GLU GLU D . n 
D 1 320 ALA 320 337 337 ALA ALA D . n 
D 1 321 GLN 321 338 338 GLN GLN D . n 
D 1 322 LYS 322 339 339 LYS LYS D . n 
D 1 323 LYS 323 340 340 LYS LYS D . n 
D 1 324 ILE 324 341 341 ILE ILE D . n 
D 1 325 TRP 325 342 342 TRP TRP D . n 
D 1 326 MET 326 343 343 MET MET D . n 
D 1 327 PHE 327 344 344 PHE PHE D . n 
D 1 328 ASP 328 345 345 ASP ASP D . n 
D 1 329 LYS 329 346 346 LYS LYS D . n 
D 1 330 TYR 330 347 347 TYR TYR D . n 
D 1 331 GLY 331 348 348 GLY GLY D . n 
D 1 332 LEU 332 349 349 LEU LEU D . n 
D 1 333 LEU 333 350 350 LEU LEU D . n 
D 1 334 VAL 334 351 351 VAL VAL D . n 
D 1 335 LYS 335 352 352 LYS LYS D . n 
D 1 336 GLY 336 353 353 GLY GLY D . n 
D 1 337 ARG 337 354 354 ARG ARG D . n 
D 1 338 LYS 338 355 355 LYS LYS D . n 
D 1 339 ALA 339 356 356 ALA ALA D . n 
D 1 340 LYS 340 357 357 LYS LYS D . n 
D 1 341 ILE 341 358 358 ILE ILE D . n 
D 1 342 ASP 342 359 359 ASP ASP D . n 
D 1 343 SER 343 360 360 SER SER D . n 
D 1 344 TYR 344 361 361 TYR TYR D . n 
D 1 345 GLN 345 362 362 GLN GLN D . n 
D 1 346 GLU 346 363 363 GLU GLU D . n 
D 1 347 PRO 347 364 364 PRO PRO D . n 
D 1 348 PHE 348 365 365 PHE PHE D . n 
D 1 349 THR 349 366 366 THR THR D . n 
D 1 350 HIS 350 367 367 HIS HIS D . n 
D 1 351 SER 351 368 ?   ?   ?   D . n 
D 1 352 ALA 352 369 ?   ?   ?   D . n 
D 1 353 PRO 353 370 ?   ?   ?   D . n 
D 1 354 GLU 354 371 ?   ?   ?   D . n 
D 1 355 SER 355 372 ?   ?   ?   D . n 
D 1 356 ILE 356 373 ?   ?   ?   D . n 
D 1 357 PRO 357 374 374 PRO PRO D . n 
D 1 358 ASP 358 375 375 ASP ASP D . n 
D 1 359 THR 359 376 376 THR THR D . n 
D 1 360 PHE 360 377 377 PHE PHE D . n 
D 1 361 GLU 361 378 378 GLU GLU D . n 
D 1 362 ASP 362 379 379 ASP ASP D . n 
D 1 363 ALA 363 380 380 ALA ALA D . n 
D 1 364 VAL 364 381 381 VAL VAL D . n 
D 1 365 ASN 365 382 382 ASN ASN D . n 
D 1 366 ILE 366 383 383 ILE ILE D . n 
D 1 367 LEU 367 384 384 LEU LEU D . n 
D 1 368 LYS 368 385 385 LYS LYS D . n 
D 1 369 PRO 369 386 386 PRO PRO D . n 
D 1 370 SER 370 387 387 SER SER D . n 
D 1 371 THR 371 388 388 THR THR D . n 
D 1 372 ILE 372 389 389 ILE ILE D . n 
D 1 373 ILE 373 390 390 ILE ILE D . n 
D 1 374 GLY 374 391 391 GLY GLY D . n 
D 1 375 VAL 375 392 392 VAL VAL D . n 
D 1 376 ALA 376 393 393 ALA ALA D . n 
D 1 377 GLY 377 394 394 GLY GLY D . n 
D 1 378 ALA 378 395 395 ALA ALA D . n 
D 1 379 GLY 379 396 396 GLY GLY D . n 
D 1 380 ARG 380 397 397 ARG ARG D . n 
D 1 381 LEU 381 398 398 LEU LEU D . n 
D 1 382 PHE 382 399 399 PHE PHE D . n 
D 1 383 THR 383 400 400 THR THR D . n 
D 1 384 PRO 384 401 401 PRO PRO D . n 
D 1 385 ASP 385 402 402 ASP ASP D . n 
D 1 386 VAL 386 403 403 VAL VAL D . n 
D 1 387 ILE 387 404 404 ILE ILE D . n 
D 1 388 ARG 388 405 405 ARG ARG D . n 
D 1 389 ALA 389 406 406 ALA ALA D . n 
D 1 390 MET 390 407 407 MET MET D . n 
D 1 391 ALA 391 408 408 ALA ALA D . n 
D 1 392 SER 392 409 409 SER SER D . n 
D 1 393 ILE 393 410 410 ILE ILE D . n 
D 1 394 ASN 394 411 411 ASN ASN D . n 
D 1 395 GLU 395 412 412 GLU GLU D . n 
D 1 396 ARG 396 413 413 ARG ARG D . n 
D 1 397 PRO 397 414 414 PRO PRO D . n 
D 1 398 VAL 398 415 415 VAL VAL D . n 
D 1 399 ILE 399 416 416 ILE ILE D . n 
D 1 400 PHE 400 417 417 PHE PHE D . n 
D 1 401 ALA 401 418 418 ALA ALA D . n 
D 1 402 LEU 402 419 419 LEU LEU D . n 
D 1 403 SER 403 420 420 SER SER D . n 
D 1 404 ASN 404 421 421 ASN ASN D . n 
D 1 405 PRO 405 422 422 PRO PRO D . n 
D 1 406 THR 406 423 423 THR THR D . n 
D 1 407 ALA 407 424 424 ALA ALA D . n 
D 1 408 GLN 408 425 425 GLN GLN D . n 
D 1 409 ALA 409 426 426 ALA ALA D . n 
D 1 410 GLU 410 427 427 GLU GLU D . n 
D 1 411 CYS 411 428 428 CYS CYS D . n 
D 1 412 THR 412 429 429 THR THR D . n 
D 1 413 ALA 413 430 430 ALA ALA D . n 
D 1 414 GLU 414 431 431 GLU GLU D . n 
D 1 415 GLU 415 432 432 GLU GLU D . n 
D 1 416 ALA 416 433 433 ALA ALA D . n 
D 1 417 TYR 417 434 434 TYR TYR D . n 
D 1 418 THR 418 435 435 THR THR D . n 
D 1 419 LEU 419 436 436 LEU LEU D . n 
D 1 420 THR 420 437 437 THR THR D . n 
D 1 421 GLU 421 438 438 GLU GLU D . n 
D 1 422 GLY 422 439 439 GLY GLY D . n 
D 1 423 ARG 423 440 440 ARG ARG D . n 
D 1 424 CYS 424 441 441 CYS CYS D . n 
D 1 425 LEU 425 442 442 LEU LEU D . n 
D 1 426 PHE 426 443 443 PHE PHE D . n 
D 1 427 ALA 427 444 444 ALA ALA D . n 
D 1 428 SER 428 445 445 SER SER D . n 
D 1 429 GLY 429 446 446 GLY GLY D . n 
D 1 430 SER 430 447 447 SER SER D . n 
D 1 431 PRO 431 448 448 PRO PRO D . n 
D 1 432 PHE 432 449 449 PHE PHE D . n 
D 1 433 GLY 433 450 450 GLY GLY D . n 
D 1 434 PRO 434 451 451 PRO PRO D . n 
D 1 435 VAL 435 452 452 VAL VAL D . n 
D 1 436 LYS 436 453 ?   ?   ?   D . n 
D 1 437 LEU 437 454 ?   ?   ?   D . n 
D 1 438 THR 438 455 ?   ?   ?   D . n 
D 1 439 ASP 439 456 ?   ?   ?   D . n 
D 1 440 GLY 440 457 ?   ?   ?   D . n 
D 1 441 ARG 441 458 458 ARG ARG D . n 
D 1 442 VAL 442 459 459 VAL VAL D . n 
D 1 443 PHE 443 460 460 PHE PHE D . n 
D 1 444 THR 444 461 461 THR THR D . n 
D 1 445 PRO 445 462 462 PRO PRO D . n 
D 1 446 GLY 446 463 463 GLY GLY D . n 
D 1 447 GLN 447 464 464 GLN GLN D . n 
D 1 448 GLY 448 465 465 GLY GLY D . n 
D 1 449 ASN 449 466 466 ASN ASN D . n 
D 1 450 ASN 450 467 467 ASN ASN D . n 
D 1 451 VAL 451 468 468 VAL VAL D . n 
D 1 452 TYR 452 469 469 TYR TYR D . n 
D 1 453 ILE 453 470 470 ILE ILE D . n 
D 1 454 PHE 454 471 471 PHE PHE D . n 
D 1 455 PRO 455 472 472 PRO PRO D . n 
D 1 456 GLY 456 473 473 GLY GLY D . n 
D 1 457 VAL 457 474 474 VAL VAL D . n 
D 1 458 ALA 458 475 475 ALA ALA D . n 
D 1 459 LEU 459 476 476 LEU LEU D . n 
D 1 460 ALA 460 477 477 ALA ALA D . n 
D 1 461 VAL 461 478 478 VAL VAL D . n 
D 1 462 ILE 462 479 479 ILE ILE D . n 
D 1 463 LEU 463 480 480 LEU LEU D . n 
D 1 464 CYS 464 481 481 CYS CYS D . n 
D 1 465 ASN 465 482 482 ASN ASN D . n 
D 1 466 THR 466 483 483 THR THR D . n 
D 1 467 ARG 467 484 484 ARG ARG D . n 
D 1 468 HIS 468 485 485 HIS HIS D . n 
D 1 469 ILE 469 486 486 ILE ILE D . n 
D 1 470 SER 470 487 487 SER SER D . n 
D 1 471 ASP 471 488 488 ASP ASP D . n 
D 1 472 SER 472 489 489 SER SER D . n 
D 1 473 VAL 473 490 490 VAL VAL D . n 
D 1 474 PHE 474 491 491 PHE PHE D . n 
D 1 475 LEU 475 492 492 LEU LEU D . n 
D 1 476 GLU 476 493 493 GLU GLU D . n 
D 1 477 ALA 477 494 494 ALA ALA D . n 
D 1 478 ALA 478 495 495 ALA ALA D . n 
D 1 479 LYS 479 496 496 LYS LYS D . n 
D 1 480 ALA 480 497 497 ALA ALA D . n 
D 1 481 LEU 481 498 498 LEU LEU D . n 
D 1 482 THR 482 499 499 THR THR D . n 
D 1 483 SER 483 500 500 SER SER D . n 
D 1 484 GLN 484 501 501 GLN GLN D . n 
D 1 485 LEU 485 502 502 LEU LEU D . n 
D 1 486 THR 486 503 503 THR THR D . n 
D 1 487 ASP 487 504 504 ASP ASP D . n 
D 1 488 GLU 488 505 505 GLU GLU D . n 
D 1 489 GLU 489 506 506 GLU GLU D . n 
D 1 490 LEU 490 507 507 LEU LEU D . n 
D 1 491 ALA 491 508 508 ALA ALA D . n 
D 1 492 GLN 492 509 509 GLN GLN D . n 
D 1 493 GLY 493 510 510 GLY GLY D . n 
D 1 494 ARG 494 511 511 ARG ARG D . n 
D 1 495 LEU 495 512 512 LEU LEU D . n 
D 1 496 TYR 496 513 513 TYR TYR D . n 
D 1 497 PRO 497 514 514 PRO PRO D . n 
D 1 498 PRO 498 515 515 PRO PRO D . n 
D 1 499 LEU 499 516 516 LEU LEU D . n 
D 1 500 ALA 500 517 517 ALA ALA D . n 
D 1 501 ASN 501 518 518 ASN ASN D . n 
D 1 502 ILE 502 519 519 ILE ILE D . n 
D 1 503 GLN 503 520 520 GLN GLN D . n 
D 1 504 GLU 504 521 521 GLU GLU D . n 
D 1 505 VAL 505 522 522 VAL VAL D . n 
D 1 506 SER 506 523 523 SER SER D . n 
D 1 507 ILE 507 524 524 ILE ILE D . n 
D 1 508 ASN 508 525 525 ASN ASN D . n 
D 1 509 ILE 509 526 526 ILE ILE D . n 
D 1 510 ALA 510 527 527 ALA ALA D . n 
D 1 511 ILE 511 528 528 ILE ILE D . n 
D 1 512 LYS 512 529 529 LYS LYS D . n 
D 1 513 VAL 513 530 530 VAL VAL D . n 
D 1 514 THR 514 531 531 THR THR D . n 
D 1 515 GLU 515 532 532 GLU GLU D . n 
D 1 516 TYR 516 533 533 TYR TYR D . n 
D 1 517 LEU 517 534 534 LEU LEU D . n 
D 1 518 TYR 518 535 535 TYR TYR D . n 
D 1 519 ALA 519 536 536 ALA ALA D . n 
D 1 520 ASN 520 537 537 ASN ASN D . n 
D 1 521 LYS 521 538 538 LYS LYS D . n 
D 1 522 MET 522 539 539 MET MET D . n 
D 1 523 ALA 523 540 540 ALA ALA D . n 
D 1 524 PHE 524 541 541 PHE PHE D . n 
D 1 525 ARG 525 542 542 ARG ARG D . n 
D 1 526 TYR 526 543 543 TYR TYR D . n 
D 1 527 PRO 527 544 544 PRO PRO D . n 
D 1 528 GLU 528 545 545 GLU GLU D . n 
D 1 529 PRO 529 546 546 PRO PRO D . n 
D 1 530 GLU 530 547 547 GLU GLU D . n 
D 1 531 ASP 531 548 548 ASP ASP D . n 
D 1 532 LYS 532 549 549 LYS LYS D . n 
D 1 533 ALA 533 550 550 ALA ALA D . n 
D 1 534 LYS 534 551 551 LYS LYS D . n 
D 1 535 TYR 535 552 552 TYR TYR D . n 
D 1 536 VAL 536 553 553 VAL VAL D . n 
D 1 537 LYS 537 554 554 LYS LYS D . n 
D 1 538 GLU 538 555 555 GLU GLU D . n 
D 1 539 ARG 539 556 556 ARG ARG D . n 
D 1 540 THR 540 557 557 THR THR D . n 
D 1 541 TRP 541 558 558 TRP TRP D . n 
D 1 542 ARG 542 559 559 ARG ARG D . n 
D 1 543 SER 543 560 560 SER SER D . n 
D 1 544 GLU 544 561 561 GLU GLU D . n 
D 1 545 TYR 545 562 562 TYR TYR D . n 
D 1 546 ASP 546 563 563 ASP ASP D . n 
D 1 547 SER 547 564 564 SER SER D . n 
D 1 548 LEU 548 565 565 LEU LEU D . n 
D 1 549 LEU 549 566 566 LEU LEU D . n 
D 1 550 PRO 550 567 567 PRO PRO D . n 
D 1 551 ASP 551 568 568 ASP ASP D . n 
D 1 552 VAL 552 569 569 VAL VAL D . n 
D 1 553 TYR 553 570 570 TYR TYR D . n 
D 1 554 GLU 554 571 571 GLU GLU D . n 
D 1 555 TRP 555 572 572 TRP TRP D . n 
D 1 556 PRO 556 573 573 PRO PRO D . n 
D 1 557 GLU 557 574 574 GLU GLU D . n 
D 1 558 SER 558 575 ?   ?   ?   D . n 
D 1 559 ALA 559 576 ?   ?   ?   D . n 
D 1 560 SER 560 577 ?   ?   ?   D . n 
D 1 561 SER 561 578 ?   ?   ?   D . n 
D 1 562 PRO 562 579 579 PRO PRO D . n 
D 1 563 PRO 563 580 580 PRO PRO D . n 
D 1 564 VAL 564 581 ?   ?   ?   D . n 
D 1 565 ILE 565 582 ?   ?   ?   D . n 
D 1 566 THR 566 583 ?   ?   ?   D . n 
D 1 567 GLU 567 584 ?   ?   ?   D . n 
D 1 568 LEU 568 585 ?   ?   ?   D . n 
D 1 569 GLU 569 586 ?   ?   ?   D . n 
D 1 570 HIS 570 587 ?   ?   ?   D . n 
D 1 571 HIS 571 588 ?   ?   ?   D . n 
D 1 572 HIS 572 589 ?   ?   ?   D . n 
D 1 573 HIS 573 590 ?   ?   ?   D . n 
D 1 574 HIS 574 591 ?   ?   ?   D . n 
D 1 575 HIS 575 592 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 NAD 1   601  600  NAD NAD A . 
F  3 EDO 1   602  601  EDO EDO A . 
G  3 EDO 1   603  603  EDO EDO A . 
H  4 CL  1   604  605  CL  CL  A . 
I  2 NAD 1   605  606  NAD NAD A . 
J  5 MG  1   606  600  MG  MG  A . 
K  6 TLA 1   607  603  TLA TLA A . 
L  4 CL  1   601  604  CL  CL  B . 
M  2 NAD 1   602  600  NAD NAD B . 
N  6 TLA 1   603  601  TLA TLA B . 
O  3 EDO 1   604  602  EDO EDO B . 
P  2 NAD 1   605  603  NAD NAD B . 
Q  5 MG  1   606  600  MG  MG  B . 
R  6 TLA 1   601  601  TLA TLA C . 
S  3 EDO 1   602  602  EDO EDO C . 
T  4 CL  1   603  603  CL  CL  C . 
U  2 NAD 1   604  605  NAD NAD C . 
V  2 NAD 1   605  606  NAD NAD C . 
W  6 TLA 1   601  602  TLA TLA D . 
X  4 CL  1   602  604  CL  CL  D . 
Y  2 NAD 1   603  601  NAD NAD D . 
Z  3 EDO 1   604  602  EDO EDO D . 
AA 2 NAD 1   605  604  NAD NAD D . 
BA 7 HOH 1   701  1213 HOH HOH A . 
BA 7 HOH 2   702  1953 HOH HOH A . 
BA 7 HOH 3   703  2106 HOH HOH A . 
BA 7 HOH 4   704  1225 HOH HOH A . 
BA 7 HOH 5   705  1287 HOH HOH A . 
BA 7 HOH 6   706  995  HOH HOH A . 
BA 7 HOH 7   707  1269 HOH HOH A . 
BA 7 HOH 8   708  1283 HOH HOH A . 
BA 7 HOH 9   709  226  HOH HOH A . 
BA 7 HOH 10  710  879  HOH HOH A . 
BA 7 HOH 11  711  1940 HOH HOH A . 
BA 7 HOH 12  712  510  HOH HOH A . 
BA 7 HOH 13  713  1033 HOH HOH A . 
BA 7 HOH 14  714  1996 HOH HOH A . 
BA 7 HOH 15  715  1518 HOH HOH A . 
BA 7 HOH 16  716  1206 HOH HOH A . 
BA 7 HOH 17  717  1984 HOH HOH A . 
BA 7 HOH 18  718  123  HOH HOH A . 
BA 7 HOH 19  719  2068 HOH HOH A . 
BA 7 HOH 20  720  1351 HOH HOH A . 
BA 7 HOH 21  721  1612 HOH HOH A . 
BA 7 HOH 22  722  1036 HOH HOH A . 
BA 7 HOH 23  723  1597 HOH HOH A . 
BA 7 HOH 24  724  936  HOH HOH A . 
BA 7 HOH 25  725  1553 HOH HOH A . 
BA 7 HOH 26  726  730  HOH HOH A . 
BA 7 HOH 27  727  549  HOH HOH A . 
BA 7 HOH 28  728  1385 HOH HOH A . 
BA 7 HOH 29  729  41   HOH HOH A . 
BA 7 HOH 30  730  1859 HOH HOH A . 
BA 7 HOH 31  731  860  HOH HOH A . 
BA 7 HOH 32  732  1348 HOH HOH A . 
BA 7 HOH 33  733  722  HOH HOH A . 
BA 7 HOH 34  734  2094 HOH HOH A . 
BA 7 HOH 35  735  1455 HOH HOH A . 
BA 7 HOH 36  736  1884 HOH HOH A . 
BA 7 HOH 37  737  563  HOH HOH A . 
BA 7 HOH 38  738  396  HOH HOH A . 
BA 7 HOH 39  739  411  HOH HOH A . 
BA 7 HOH 40  740  1119 HOH HOH A . 
BA 7 HOH 41  741  232  HOH HOH A . 
BA 7 HOH 42  742  1032 HOH HOH A . 
BA 7 HOH 43  743  428  HOH HOH A . 
BA 7 HOH 44  744  820  HOH HOH A . 
BA 7 HOH 45  745  1504 HOH HOH A . 
BA 7 HOH 46  746  529  HOH HOH A . 
BA 7 HOH 47  747  141  HOH HOH A . 
BA 7 HOH 48  748  1815 HOH HOH A . 
BA 7 HOH 49  749  537  HOH HOH A . 
BA 7 HOH 50  750  380  HOH HOH A . 
BA 7 HOH 51  751  164  HOH HOH A . 
BA 7 HOH 52  752  222  HOH HOH A . 
BA 7 HOH 53  753  939  HOH HOH A . 
BA 7 HOH 54  754  269  HOH HOH A . 
BA 7 HOH 55  755  720  HOH HOH A . 
BA 7 HOH 56  756  746  HOH HOH A . 
BA 7 HOH 57  757  1101 HOH HOH A . 
BA 7 HOH 58  758  513  HOH HOH A . 
BA 7 HOH 59  759  873  HOH HOH A . 
BA 7 HOH 60  760  1628 HOH HOH A . 
BA 7 HOH 61  761  632  HOH HOH A . 
BA 7 HOH 62  762  18   HOH HOH A . 
BA 7 HOH 63  763  1889 HOH HOH A . 
BA 7 HOH 64  764  1531 HOH HOH A . 
BA 7 HOH 65  765  1020 HOH HOH A . 
BA 7 HOH 66  766  619  HOH HOH A . 
BA 7 HOH 67  767  137  HOH HOH A . 
BA 7 HOH 68  768  1968 HOH HOH A . 
BA 7 HOH 69  769  2124 HOH HOH A . 
BA 7 HOH 70  770  519  HOH HOH A . 
BA 7 HOH 71  771  1347 HOH HOH A . 
BA 7 HOH 72  772  817  HOH HOH A . 
BA 7 HOH 73  773  1978 HOH HOH A . 
BA 7 HOH 74  774  605  HOH HOH A . 
BA 7 HOH 75  775  167  HOH HOH A . 
BA 7 HOH 76  776  392  HOH HOH A . 
BA 7 HOH 77  777  849  HOH HOH A . 
BA 7 HOH 78  778  618  HOH HOH A . 
BA 7 HOH 79  779  1410 HOH HOH A . 
BA 7 HOH 80  780  243  HOH HOH A . 
BA 7 HOH 81  781  1064 HOH HOH A . 
BA 7 HOH 82  782  1536 HOH HOH A . 
BA 7 HOH 83  783  316  HOH HOH A . 
BA 7 HOH 84  784  831  HOH HOH A . 
BA 7 HOH 85  785  373  HOH HOH A . 
BA 7 HOH 86  786  960  HOH HOH A . 
BA 7 HOH 87  787  1016 HOH HOH A . 
BA 7 HOH 88  788  1667 HOH HOH A . 
BA 7 HOH 89  789  1724 HOH HOH A . 
BA 7 HOH 90  790  1468 HOH HOH A . 
BA 7 HOH 91  791  2186 HOH HOH A . 
BA 7 HOH 92  792  436  HOH HOH A . 
BA 7 HOH 93  793  959  HOH HOH A . 
BA 7 HOH 94  794  346  HOH HOH A . 
BA 7 HOH 95  795  32   HOH HOH A . 
BA 7 HOH 96  796  1026 HOH HOH A . 
BA 7 HOH 97  797  1277 HOH HOH A . 
BA 7 HOH 98  798  1185 HOH HOH A . 
BA 7 HOH 99  799  1662 HOH HOH A . 
BA 7 HOH 100 800  1350 HOH HOH A . 
BA 7 HOH 101 801  1563 HOH HOH A . 
BA 7 HOH 102 802  2178 HOH HOH A . 
BA 7 HOH 103 803  171  HOH HOH A . 
BA 7 HOH 104 804  463  HOH HOH A . 
BA 7 HOH 105 805  1015 HOH HOH A . 
BA 7 HOH 106 806  1851 HOH HOH A . 
BA 7 HOH 107 807  461  HOH HOH A . 
BA 7 HOH 108 808  1    HOH HOH A . 
BA 7 HOH 109 809  474  HOH HOH A . 
BA 7 HOH 110 810  2125 HOH HOH A . 
BA 7 HOH 111 811  67   HOH HOH A . 
BA 7 HOH 112 812  300  HOH HOH A . 
BA 7 HOH 113 813  1869 HOH HOH A . 
BA 7 HOH 114 814  254  HOH HOH A . 
BA 7 HOH 115 815  210  HOH HOH A . 
BA 7 HOH 116 816  1446 HOH HOH A . 
BA 7 HOH 117 817  122  HOH HOH A . 
BA 7 HOH 118 818  160  HOH HOH A . 
BA 7 HOH 119 819  265  HOH HOH A . 
BA 7 HOH 120 820  1007 HOH HOH A . 
BA 7 HOH 121 821  2011 HOH HOH A . 
BA 7 HOH 122 822  941  HOH HOH A . 
BA 7 HOH 123 823  1262 HOH HOH A . 
BA 7 HOH 124 824  1441 HOH HOH A . 
BA 7 HOH 125 825  1587 HOH HOH A . 
BA 7 HOH 126 826  1660 HOH HOH A . 
BA 7 HOH 127 827  1576 HOH HOH A . 
BA 7 HOH 128 828  805  HOH HOH A . 
BA 7 HOH 129 829  1634 HOH HOH A . 
BA 7 HOH 130 830  87   HOH HOH A . 
BA 7 HOH 131 831  1971 HOH HOH A . 
BA 7 HOH 132 832  1594 HOH HOH A . 
BA 7 HOH 133 833  1267 HOH HOH A . 
BA 7 HOH 134 834  759  HOH HOH A . 
BA 7 HOH 135 835  962  HOH HOH A . 
BA 7 HOH 136 836  938  HOH HOH A . 
BA 7 HOH 137 837  487  HOH HOH A . 
BA 7 HOH 138 838  225  HOH HOH A . 
BA 7 HOH 139 839  166  HOH HOH A . 
BA 7 HOH 140 840  562  HOH HOH A . 
BA 7 HOH 141 841  1297 HOH HOH A . 
BA 7 HOH 142 842  1516 HOH HOH A . 
BA 7 HOH 143 843  1425 HOH HOH A . 
BA 7 HOH 144 844  71   HOH HOH A . 
BA 7 HOH 145 845  238  HOH HOH A . 
BA 7 HOH 146 846  571  HOH HOH A . 
BA 7 HOH 147 847  1567 HOH HOH A . 
BA 7 HOH 148 848  1450 HOH HOH A . 
BA 7 HOH 149 849  283  HOH HOH A . 
BA 7 HOH 150 850  554  HOH HOH A . 
BA 7 HOH 151 851  701  HOH HOH A . 
BA 7 HOH 152 852  192  HOH HOH A . 
BA 7 HOH 153 853  1681 HOH HOH A . 
BA 7 HOH 154 854  1752 HOH HOH A . 
BA 7 HOH 155 855  2114 HOH HOH A . 
BA 7 HOH 156 856  734  HOH HOH A . 
BA 7 HOH 157 857  1502 HOH HOH A . 
BA 7 HOH 158 858  1488 HOH HOH A . 
BA 7 HOH 159 859  421  HOH HOH A . 
BA 7 HOH 160 860  511  HOH HOH A . 
BA 7 HOH 161 861  284  HOH HOH A . 
BA 7 HOH 162 862  569  HOH HOH A . 
BA 7 HOH 163 863  2017 HOH HOH A . 
BA 7 HOH 164 864  2134 HOH HOH A . 
BA 7 HOH 165 865  868  HOH HOH A . 
BA 7 HOH 166 866  1745 HOH HOH A . 
BA 7 HOH 167 867  359  HOH HOH A . 
BA 7 HOH 168 868  1409 HOH HOH A . 
BA 7 HOH 169 869  395  HOH HOH A . 
BA 7 HOH 170 870  79   HOH HOH A . 
BA 7 HOH 171 871  369  HOH HOH A . 
BA 7 HOH 172 872  278  HOH HOH A . 
BA 7 HOH 173 873  858  HOH HOH A . 
BA 7 HOH 174 874  2122 HOH HOH A . 
BA 7 HOH 175 875  1359 HOH HOH A . 
BA 7 HOH 176 876  768  HOH HOH A . 
BA 7 HOH 177 877  20   HOH HOH A . 
BA 7 HOH 178 878  489  HOH HOH A . 
BA 7 HOH 179 879  448  HOH HOH A . 
BA 7 HOH 180 880  961  HOH HOH A . 
BA 7 HOH 181 881  1655 HOH HOH A . 
BA 7 HOH 182 882  1245 HOH HOH A . 
BA 7 HOH 183 883  1839 HOH HOH A . 
BA 7 HOH 184 884  142  HOH HOH A . 
BA 7 HOH 185 885  55   HOH HOH A . 
BA 7 HOH 186 886  1604 HOH HOH A . 
BA 7 HOH 187 887  2140 HOH HOH A . 
BA 7 HOH 188 888  70   HOH HOH A . 
BA 7 HOH 189 889  1608 HOH HOH A . 
BA 7 HOH 190 890  2026 HOH HOH A . 
BA 7 HOH 191 891  2126 HOH HOH A . 
BA 7 HOH 192 892  800  HOH HOH A . 
BA 7 HOH 193 893  196  HOH HOH A . 
BA 7 HOH 194 894  2069 HOH HOH A . 
BA 7 HOH 195 895  1029 HOH HOH A . 
BA 7 HOH 196 896  126  HOH HOH A . 
BA 7 HOH 197 897  1115 HOH HOH A . 
BA 7 HOH 198 898  846  HOH HOH A . 
BA 7 HOH 199 899  1730 HOH HOH A . 
BA 7 HOH 200 900  95   HOH HOH A . 
BA 7 HOH 201 901  38   HOH HOH A . 
BA 7 HOH 202 902  66   HOH HOH A . 
BA 7 HOH 203 903  279  HOH HOH A . 
BA 7 HOH 204 904  90   HOH HOH A . 
BA 7 HOH 205 905  1527 HOH HOH A . 
BA 7 HOH 206 906  1444 HOH HOH A . 
BA 7 HOH 207 907  1523 HOH HOH A . 
BA 7 HOH 208 908  943  HOH HOH A . 
BA 7 HOH 209 909  830  HOH HOH A . 
BA 7 HOH 210 910  106  HOH HOH A . 
BA 7 HOH 211 911  1301 HOH HOH A . 
BA 7 HOH 212 912  2187 HOH HOH A . 
BA 7 HOH 213 913  2184 HOH HOH A . 
BA 7 HOH 214 914  1040 HOH HOH A . 
BA 7 HOH 215 915  1637 HOH HOH A . 
BA 7 HOH 216 916  454  HOH HOH A . 
BA 7 HOH 217 917  249  HOH HOH A . 
BA 7 HOH 218 918  5    HOH HOH A . 
BA 7 HOH 219 919  937  HOH HOH A . 
BA 7 HOH 220 920  285  HOH HOH A . 
BA 7 HOH 221 921  1182 HOH HOH A . 
BA 7 HOH 222 922  1288 HOH HOH A . 
BA 7 HOH 223 923  419  HOH HOH A . 
BA 7 HOH 224 924  1431 HOH HOH A . 
BA 7 HOH 225 925  1979 HOH HOH A . 
BA 7 HOH 226 926  1242 HOH HOH A . 
BA 7 HOH 227 927  825  HOH HOH A . 
BA 7 HOH 228 928  679  HOH HOH A . 
BA 7 HOH 229 929  735  HOH HOH A . 
BA 7 HOH 230 930  1544 HOH HOH A . 
BA 7 HOH 231 931  645  HOH HOH A . 
BA 7 HOH 232 932  1477 HOH HOH A . 
BA 7 HOH 233 933  684  HOH HOH A . 
BA 7 HOH 234 934  478  HOH HOH A . 
BA 7 HOH 235 935  992  HOH HOH A . 
BA 7 HOH 236 936  156  HOH HOH A . 
BA 7 HOH 237 937  248  HOH HOH A . 
BA 7 HOH 238 938  2048 HOH HOH A . 
BA 7 HOH 239 939  410  HOH HOH A . 
BA 7 HOH 240 940  1021 HOH HOH A . 
BA 7 HOH 241 941  157  HOH HOH A . 
BA 7 HOH 242 942  262  HOH HOH A . 
BA 7 HOH 243 943  1220 HOH HOH A . 
BA 7 HOH 244 944  737  HOH HOH A . 
BA 7 HOH 245 945  89   HOH HOH A . 
BA 7 HOH 246 946  726  HOH HOH A . 
BA 7 HOH 247 947  281  HOH HOH A . 
BA 7 HOH 248 948  542  HOH HOH A . 
BA 7 HOH 249 949  653  HOH HOH A . 
BA 7 HOH 250 950  567  HOH HOH A . 
BA 7 HOH 251 951  277  HOH HOH A . 
BA 7 HOH 252 952  12   HOH HOH A . 
BA 7 HOH 253 953  793  HOH HOH A . 
BA 7 HOH 254 954  2181 HOH HOH A . 
BA 7 HOH 255 955  1668 HOH HOH A . 
BA 7 HOH 256 956  1192 HOH HOH A . 
BA 7 HOH 257 957  209  HOH HOH A . 
BA 7 HOH 258 958  488  HOH HOH A . 
BA 7 HOH 259 959  613  HOH HOH A . 
BA 7 HOH 260 960  577  HOH HOH A . 
BA 7 HOH 261 961  703  HOH HOH A . 
BA 7 HOH 262 962  147  HOH HOH A . 
BA 7 HOH 263 963  731  HOH HOH A . 
BA 7 HOH 264 964  606  HOH HOH A . 
BA 7 HOH 265 965  1092 HOH HOH A . 
BA 7 HOH 266 966  674  HOH HOH A . 
BA 7 HOH 267 967  1344 HOH HOH A . 
BA 7 HOH 268 968  2141 HOH HOH A . 
BA 7 HOH 269 969  381  HOH HOH A . 
BA 7 HOH 270 970  1684 HOH HOH A . 
BA 7 HOH 271 971  1591 HOH HOH A . 
BA 7 HOH 272 972  102  HOH HOH A . 
BA 7 HOH 273 973  432  HOH HOH A . 
BA 7 HOH 274 974  1956 HOH HOH A . 
BA 7 HOH 275 975  7    HOH HOH A . 
BA 7 HOH 276 976  933  HOH HOH A . 
BA 7 HOH 277 977  714  HOH HOH A . 
BA 7 HOH 278 978  1550 HOH HOH A . 
BA 7 HOH 279 979  342  HOH HOH A . 
BA 7 HOH 280 980  1722 HOH HOH A . 
BA 7 HOH 281 981  1969 HOH HOH A . 
BA 7 HOH 282 982  1682 HOH HOH A . 
BA 7 HOH 283 983  530  HOH HOH A . 
BA 7 HOH 284 984  438  HOH HOH A . 
BA 7 HOH 285 985  1933 HOH HOH A . 
BA 7 HOH 286 986  1855 HOH HOH A . 
BA 7 HOH 287 987  1955 HOH HOH A . 
BA 7 HOH 288 988  2097 HOH HOH A . 
BA 7 HOH 289 989  789  HOH HOH A . 
BA 7 HOH 290 990  1257 HOH HOH A . 
BA 7 HOH 291 991  1416 HOH HOH A . 
BA 7 HOH 292 992  728  HOH HOH A . 
BA 7 HOH 293 993  514  HOH HOH A . 
BA 7 HOH 294 994  1209 HOH HOH A . 
BA 7 HOH 295 995  1447 HOH HOH A . 
BA 7 HOH 296 996  1473 HOH HOH A . 
BA 7 HOH 297 997  98   HOH HOH A . 
BA 7 HOH 298 998  1551 HOH HOH A . 
BA 7 HOH 299 999  108  HOH HOH A . 
BA 7 HOH 300 1000 400  HOH HOH A . 
BA 7 HOH 301 1001 1421 HOH HOH A . 
BA 7 HOH 302 1002 506  HOH HOH A . 
BA 7 HOH 303 1003 940  HOH HOH A . 
BA 7 HOH 304 1004 1214 HOH HOH A . 
BA 7 HOH 305 1005 485  HOH HOH A . 
BA 7 HOH 306 1006 1688 HOH HOH A . 
BA 7 HOH 307 1007 2163 HOH HOH A . 
BA 7 HOH 308 1008 356  HOH HOH A . 
BA 7 HOH 309 1009 388  HOH HOH A . 
BA 7 HOH 310 1010 309  HOH HOH A . 
BA 7 HOH 311 1011 1605 HOH HOH A . 
BA 7 HOH 312 1012 1352 HOH HOH A . 
BA 7 HOH 313 1013 2148 HOH HOH A . 
BA 7 HOH 314 1014 76   HOH HOH A . 
BA 7 HOH 315 1015 1509 HOH HOH A . 
BA 7 HOH 316 1016 351  HOH HOH A . 
BA 7 HOH 317 1017 1560 HOH HOH A . 
BA 7 HOH 318 1018 1008 HOH HOH A . 
BA 7 HOH 319 1019 56   HOH HOH A . 
BA 7 HOH 320 1020 2188 HOH HOH A . 
BA 7 HOH 321 1021 2153 HOH HOH A . 
BA 7 HOH 322 1022 46   HOH HOH A . 
BA 7 HOH 323 1023 2189 HOH HOH A . 
BA 7 HOH 324 1024 1964 HOH HOH A . 
BA 7 HOH 325 1025 483  HOH HOH A . 
BA 7 HOH 326 1026 2129 HOH HOH A . 
BA 7 HOH 327 1027 117  HOH HOH A . 
BA 7 HOH 328 1028 1313 HOH HOH A . 
BA 7 HOH 329 1029 1144 HOH HOH A . 
BA 7 HOH 330 1030 326  HOH HOH A . 
BA 7 HOH 331 1031 608  HOH HOH A . 
BA 7 HOH 332 1032 125  HOH HOH A . 
BA 7 HOH 333 1033 2157 HOH HOH A . 
BA 7 HOH 334 1034 318  HOH HOH A . 
BA 7 HOH 335 1035 1640 HOH HOH A . 
BA 7 HOH 336 1036 1238 HOH HOH A . 
BA 7 HOH 337 1037 1547 HOH HOH A . 
BA 7 HOH 338 1038 2182 HOH HOH A . 
BA 7 HOH 339 1039 585  HOH HOH A . 
BA 7 HOH 340 1040 1899 HOH HOH A . 
BA 7 HOH 341 1041 1836 HOH HOH A . 
BA 7 HOH 342 1042 1812 HOH HOH A . 
BA 7 HOH 343 1043 1140 HOH HOH A . 
BA 7 HOH 344 1044 1513 HOH HOH A . 
BA 7 HOH 345 1045 219  HOH HOH A . 
BA 7 HOH 346 1046 138  HOH HOH A . 
BA 7 HOH 347 1047 74   HOH HOH A . 
BA 7 HOH 348 1048 148  HOH HOH A . 
BA 7 HOH 349 1049 1841 HOH HOH A . 
BA 7 HOH 350 1050 1212 HOH HOH A . 
BA 7 HOH 351 1051 688  HOH HOH A . 
BA 7 HOH 352 1052 1994 HOH HOH A . 
BA 7 HOH 353 1053 385  HOH HOH A . 
BA 7 HOH 354 1054 194  HOH HOH A . 
BA 7 HOH 355 1055 836  HOH HOH A . 
BA 7 HOH 356 1056 1479 HOH HOH A . 
BA 7 HOH 357 1057 676  HOH HOH A . 
BA 7 HOH 358 1058 1809 HOH HOH A . 
BA 7 HOH 359 1059 1181 HOH HOH A . 
BA 7 HOH 360 1060 159  HOH HOH A . 
BA 7 HOH 361 1061 1095 HOH HOH A . 
BA 7 HOH 362 1062 772  HOH HOH A . 
BA 7 HOH 363 1063 1625 HOH HOH A . 
BA 7 HOH 364 1064 197  HOH HOH A . 
BA 7 HOH 365 1065 1481 HOH HOH A . 
BA 7 HOH 366 1066 1223 HOH HOH A . 
BA 7 HOH 367 1067 1586 HOH HOH A . 
BA 7 HOH 368 1068 172  HOH HOH A . 
BA 7 HOH 369 1069 479  HOH HOH A . 
BA 7 HOH 370 1070 1442 HOH HOH A . 
BA 7 HOH 371 1071 1842 HOH HOH A . 
BA 7 HOH 372 1072 1275 HOH HOH A . 
BA 7 HOH 373 1073 1817 HOH HOH A . 
BA 7 HOH 374 1074 727  HOH HOH A . 
BA 7 HOH 375 1075 500  HOH HOH A . 
BA 7 HOH 376 1076 1590 HOH HOH A . 
BA 7 HOH 377 1077 139  HOH HOH A . 
BA 7 HOH 378 1078 942  HOH HOH A . 
BA 7 HOH 379 1079 1366 HOH HOH A . 
BA 7 HOH 380 1080 501  HOH HOH A . 
BA 7 HOH 381 1081 1987 HOH HOH A . 
BA 7 HOH 382 1082 465  HOH HOH A . 
BA 7 HOH 383 1083 105  HOH HOH A . 
BA 7 HOH 384 1084 696  HOH HOH A . 
BA 7 HOH 385 1085 671  HOH HOH A . 
BA 7 HOH 386 1086 765  HOH HOH A . 
BA 7 HOH 387 1087 1919 HOH HOH A . 
BA 7 HOH 388 1088 33   HOH HOH A . 
BA 7 HOH 389 1089 391  HOH HOH A . 
BA 7 HOH 390 1090 1760 HOH HOH A . 
BA 7 HOH 391 1091 430  HOH HOH A . 
BA 7 HOH 392 1092 751  HOH HOH A . 
BA 7 HOH 393 1093 1795 HOH HOH A . 
BA 7 HOH 394 1094 1799 HOH HOH A . 
BA 7 HOH 395 1095 1480 HOH HOH A . 
BA 7 HOH 396 1096 495  HOH HOH A . 
BA 7 HOH 397 1097 1514 HOH HOH A . 
BA 7 HOH 398 1098 2133 HOH HOH A . 
BA 7 HOH 399 1099 1512 HOH HOH A . 
BA 7 HOH 400 1100 2192 HOH HOH A . 
BA 7 HOH 401 1101 1139 HOH HOH A . 
BA 7 HOH 402 1102 1445 HOH HOH A . 
BA 7 HOH 403 1103 183  HOH HOH A . 
BA 7 HOH 404 1104 169  HOH HOH A . 
BA 7 HOH 405 1105 704  HOH HOH A . 
BA 7 HOH 406 1106 1304 HOH HOH A . 
BA 7 HOH 407 1107 1986 HOH HOH A . 
BA 7 HOH 408 1108 1626 HOH HOH A . 
BA 7 HOH 409 1109 2006 HOH HOH A . 
BA 7 HOH 410 1110 131  HOH HOH A . 
BA 7 HOH 411 1111 887  HOH HOH A . 
BA 7 HOH 412 1112 223  HOH HOH A . 
BA 7 HOH 413 1113 1017 HOH HOH A . 
BA 7 HOH 414 1114 2049 HOH HOH A . 
BA 7 HOH 415 1115 303  HOH HOH A . 
BA 7 HOH 416 1116 840  HOH HOH A . 
BA 7 HOH 417 1117 1907 HOH HOH A . 
BA 7 HOH 418 1118 499  HOH HOH A . 
BA 7 HOH 419 1119 1076 HOH HOH A . 
BA 7 HOH 420 1120 1787 HOH HOH A . 
BA 7 HOH 421 1121 1674 HOH HOH A . 
BA 7 HOH 422 1122 576  HOH HOH A . 
BA 7 HOH 423 1123 878  HOH HOH A . 
BA 7 HOH 424 1124 1233 HOH HOH A . 
BA 7 HOH 425 1125 229  HOH HOH A . 
BA 7 HOH 426 1126 2128 HOH HOH A . 
BA 7 HOH 427 1127 2037 HOH HOH A . 
BA 7 HOH 428 1128 1216 HOH HOH A . 
BA 7 HOH 429 1129 745  HOH HOH A . 
BA 7 HOH 430 1130 2169 HOH HOH A . 
BA 7 HOH 431 1131 536  HOH HOH A . 
BA 7 HOH 432 1132 670  HOH HOH A . 
BA 7 HOH 433 1133 1967 HOH HOH A . 
BA 7 HOH 434 1134 2120 HOH HOH A . 
BA 7 HOH 435 1135 1251 HOH HOH A . 
BA 7 HOH 436 1136 545  HOH HOH A . 
BA 7 HOH 437 1137 1846 HOH HOH A . 
BA 7 HOH 438 1138 1861 HOH HOH A . 
BA 7 HOH 439 1139 1765 HOH HOH A . 
BA 7 HOH 440 1140 987  HOH HOH A . 
BA 7 HOH 441 1141 1031 HOH HOH A . 
BA 7 HOH 442 1142 1202 HOH HOH A . 
BA 7 HOH 443 1143 1739 HOH HOH A . 
BA 7 HOH 444 1144 1602 HOH HOH A . 
BA 7 HOH 445 1145 1872 HOH HOH A . 
BA 7 HOH 446 1146 1227 HOH HOH A . 
BA 7 HOH 447 1147 1466 HOH HOH A . 
BA 7 HOH 448 1148 783  HOH HOH A . 
BA 7 HOH 449 1149 583  HOH HOH A . 
BA 7 HOH 450 1150 327  HOH HOH A . 
BA 7 HOH 451 1151 1654 HOH HOH A . 
BA 7 HOH 452 1152 1252 HOH HOH A . 
BA 7 HOH 453 1153 341  HOH HOH A . 
BA 7 HOH 454 1154 818  HOH HOH A . 
BA 7 HOH 455 1155 985  HOH HOH A . 
BA 7 HOH 456 1156 1247 HOH HOH A . 
BA 7 HOH 457 1157 1205 HOH HOH A . 
BA 7 HOH 458 1158 531  HOH HOH A . 
BA 7 HOH 459 1159 1025 HOH HOH A . 
BA 7 HOH 460 1160 1285 HOH HOH A . 
BA 7 HOH 461 1161 1114 HOH HOH A . 
BA 7 HOH 462 1162 913  HOH HOH A . 
BA 7 HOH 463 1163 1309 HOH HOH A . 
BA 7 HOH 464 1164 246  HOH HOH A . 
BA 7 HOH 465 1165 1329 HOH HOH A . 
BA 7 HOH 466 1166 1422 HOH HOH A . 
BA 7 HOH 467 1167 1169 HOH HOH A . 
BA 7 HOH 468 1168 1972 HOH HOH A . 
BA 7 HOH 469 1169 544  HOH HOH A . 
BA 7 HOH 470 1170 893  HOH HOH A . 
BA 7 HOH 471 1171 1165 HOH HOH A . 
BA 7 HOH 472 1172 1673 HOH HOH A . 
BA 7 HOH 473 1173 1891 HOH HOH A . 
BA 7 HOH 474 1174 338  HOH HOH A . 
BA 7 HOH 475 1175 1174 HOH HOH A . 
BA 7 HOH 476 1176 1763 HOH HOH A . 
BA 7 HOH 477 1177 241  HOH HOH A . 
BA 7 HOH 478 1178 888  HOH HOH A . 
BA 7 HOH 479 1179 658  HOH HOH A . 
BA 7 HOH 480 1180 1383 HOH HOH A . 
BA 7 HOH 481 1181 865  HOH HOH A . 
BA 7 HOH 482 1182 1657 HOH HOH A . 
BA 7 HOH 483 1183 907  HOH HOH A . 
BA 7 HOH 484 1184 1923 HOH HOH A . 
BA 7 HOH 485 1185 1156 HOH HOH A . 
BA 7 HOH 486 1186 812  HOH HOH A . 
BA 7 HOH 487 1187 1134 HOH HOH A . 
BA 7 HOH 488 1188 687  HOH HOH A . 
BA 7 HOH 489 1189 677  HOH HOH A . 
BA 7 HOH 490 1190 764  HOH HOH A . 
BA 7 HOH 491 1191 1107 HOH HOH A . 
BA 7 HOH 492 1192 1327 HOH HOH A . 
BA 7 HOH 493 1193 1717 HOH HOH A . 
BA 7 HOH 494 1194 547  HOH HOH A . 
BA 7 HOH 495 1195 884  HOH HOH A . 
BA 7 HOH 496 1196 1767 HOH HOH A . 
BA 7 HOH 497 1197 650  HOH HOH A . 
BA 7 HOH 498 1198 894  HOH HOH A . 
BA 7 HOH 499 1199 1838 HOH HOH A . 
BA 7 HOH 500 1200 2147 HOH HOH A . 
BA 7 HOH 501 1201 890  HOH HOH A . 
BA 7 HOH 502 1202 1234 HOH HOH A . 
BA 7 HOH 503 1203 1349 HOH HOH A . 
BA 7 HOH 504 1204 659  HOH HOH A . 
BA 7 HOH 505 1205 694  HOH HOH A . 
BA 7 HOH 506 1206 733  HOH HOH A . 
BA 7 HOH 507 1207 345  HOH HOH A . 
BA 7 HOH 508 1208 1335 HOH HOH A . 
BA 7 HOH 509 1209 1930 HOH HOH A . 
BA 7 HOH 510 1210 427  HOH HOH A . 
BA 7 HOH 511 1211 2093 HOH HOH A . 
BA 7 HOH 512 1212 797  HOH HOH A . 
BA 7 HOH 513 1213 442  HOH HOH A . 
BA 7 HOH 514 1214 2038 HOH HOH A . 
BA 7 HOH 515 1215 874  HOH HOH A . 
BA 7 HOH 516 1216 1149 HOH HOH A . 
BA 7 HOH 517 1217 899  HOH HOH A . 
BA 7 HOH 518 1218 1761 HOH HOH A . 
BA 7 HOH 519 1219 257  HOH HOH A . 
BA 7 HOH 520 1220 288  HOH HOH A . 
BA 7 HOH 521 1221 851  HOH HOH A . 
BA 7 HOH 522 1222 1175 HOH HOH A . 
BA 7 HOH 523 1223 611  HOH HOH A . 
BA 7 HOH 524 1224 794  HOH HOH A . 
BA 7 HOH 525 1225 502  HOH HOH A . 
BA 7 HOH 526 1226 450  HOH HOH A . 
BA 7 HOH 527 1227 1258 HOH HOH A . 
BA 7 HOH 528 1228 1100 HOH HOH A . 
BA 7 HOH 529 1229 415  HOH HOH A . 
BA 7 HOH 530 1230 1924 HOH HOH A . 
BA 7 HOH 531 1231 1326 HOH HOH A . 
BA 7 HOH 532 1232 781  HOH HOH A . 
BA 7 HOH 533 1233 1164 HOH HOH A . 
BA 7 HOH 534 1234 2165 HOH HOH A . 
BA 7 HOH 535 1235 1334 HOH HOH A . 
BA 7 HOH 536 1236 355  HOH HOH A . 
BA 7 HOH 537 1237 898  HOH HOH A . 
BA 7 HOH 538 1238 769  HOH HOH A . 
BA 7 HOH 539 1239 1002 HOH HOH A . 
BA 7 HOH 540 1240 315  HOH HOH A . 
BA 7 HOH 541 1241 838  HOH HOH A . 
BA 7 HOH 542 1242 903  HOH HOH A . 
BA 7 HOH 543 1243 690  HOH HOH A . 
BA 7 HOH 544 1244 842  HOH HOH A . 
CA 7 HOH 1   701  1824 HOH HOH B . 
CA 7 HOH 2   702  2025 HOH HOH B . 
CA 7 HOH 3   703  1073 HOH HOH B . 
CA 7 HOH 4   704  296  HOH HOH B . 
CA 7 HOH 5   705  1796 HOH HOH B . 
CA 7 HOH 6   706  1013 HOH HOH B . 
CA 7 HOH 7   707  1340 HOH HOH B . 
CA 7 HOH 8   708  1186 HOH HOH B . 
CA 7 HOH 9   709  1503 HOH HOH B . 
CA 7 HOH 10  710  387  HOH HOH B . 
CA 7 HOH 11  711  1505 HOH HOH B . 
CA 7 HOH 12  712  260  HOH HOH B . 
CA 7 HOH 13  713  1286 HOH HOH B . 
CA 7 HOH 14  714  2113 HOH HOH B . 
CA 7 HOH 15  715  799  HOH HOH B . 
CA 7 HOH 16  716  1180 HOH HOH B . 
CA 7 HOH 17  717  1129 HOH HOH B . 
CA 7 HOH 18  718  349  HOH HOH B . 
CA 7 HOH 19  719  1679 HOH HOH B . 
CA 7 HOH 20  720  1546 HOH HOH B . 
CA 7 HOH 21  721  1098 HOH HOH B . 
CA 7 HOH 22  722  1511 HOH HOH B . 
CA 7 HOH 23  723  1999 HOH HOH B . 
CA 7 HOH 24  724  344  HOH HOH B . 
CA 7 HOH 25  725  612  HOH HOH B . 
CA 7 HOH 26  726  538  HOH HOH B . 
CA 7 HOH 27  727  146  HOH HOH B . 
CA 7 HOH 28  728  368  HOH HOH B . 
CA 7 HOH 29  729  1880 HOH HOH B . 
CA 7 HOH 30  730  516  HOH HOH B . 
CA 7 HOH 31  731  1123 HOH HOH B . 
CA 7 HOH 32  732  237  HOH HOH B . 
CA 7 HOH 33  733  2050 HOH HOH B . 
CA 7 HOH 34  734  1000 HOH HOH B . 
CA 7 HOH 35  735  292  HOH HOH B . 
CA 7 HOH 36  736  94   HOH HOH B . 
CA 7 HOH 37  737  1943 HOH HOH B . 
CA 7 HOH 38  738  1337 HOH HOH B . 
CA 7 HOH 39  739  617  HOH HOH B . 
CA 7 HOH 40  740  480  HOH HOH B . 
CA 7 HOH 41  741  91   HOH HOH B . 
CA 7 HOH 42  742  1260 HOH HOH B . 
CA 7 HOH 43  743  595  HOH HOH B . 
CA 7 HOH 44  744  1997 HOH HOH B . 
CA 7 HOH 45  745  1353 HOH HOH B . 
CA 7 HOH 46  746  1208 HOH HOH B . 
CA 7 HOH 47  747  1810 HOH HOH B . 
CA 7 HOH 48  748  1834 HOH HOH B . 
CA 7 HOH 49  749  447  HOH HOH B . 
CA 7 HOH 50  750  758  HOH HOH B . 
CA 7 HOH 51  751  669  HOH HOH B . 
CA 7 HOH 52  752  1947 HOH HOH B . 
CA 7 HOH 53  753  553  HOH HOH B . 
CA 7 HOH 54  754  350  HOH HOH B . 
CA 7 HOH 55  755  2103 HOH HOH B . 
CA 7 HOH 56  756  515  HOH HOH B . 
CA 7 HOH 57  757  673  HOH HOH B . 
CA 7 HOH 58  758  1677 HOH HOH B . 
CA 7 HOH 59  759  1240 HOH HOH B . 
CA 7 HOH 60  760  2177 HOH HOH B . 
CA 7 HOH 61  761  1614 HOH HOH B . 
CA 7 HOH 62  762  466  HOH HOH B . 
CA 7 HOH 63  763  3    HOH HOH B . 
CA 7 HOH 64  764  2062 HOH HOH B . 
CA 7 HOH 65  765  1011 HOH HOH B . 
CA 7 HOH 66  766  64   HOH HOH B . 
CA 7 HOH 67  767  6    HOH HOH B . 
CA 7 HOH 68  768  118  HOH HOH B . 
CA 7 HOH 69  769  1050 HOH HOH B . 
CA 7 HOH 70  770  1946 HOH HOH B . 
CA 7 HOH 71  771  1826 HOH HOH B . 
CA 7 HOH 72  772  945  HOH HOH B . 
CA 7 HOH 73  773  1215 HOH HOH B . 
CA 7 HOH 74  774  165  HOH HOH B . 
CA 7 HOH 75  775  556  HOH HOH B . 
CA 7 HOH 76  776  175  HOH HOH B . 
CA 7 HOH 77  777  235  HOH HOH B . 
CA 7 HOH 78  778  236  HOH HOH B . 
CA 7 HOH 79  779  113  HOH HOH B . 
CA 7 HOH 80  780  168  HOH HOH B . 
CA 7 HOH 81  781  272  HOH HOH B . 
CA 7 HOH 82  782  1079 HOH HOH B . 
CA 7 HOH 83  783  1478 HOH HOH B . 
CA 7 HOH 84  784  1065 HOH HOH B . 
CA 7 HOH 85  785  1088 HOH HOH B . 
CA 7 HOH 86  786  951  HOH HOH B . 
CA 7 HOH 87  787  1265 HOH HOH B . 
CA 7 HOH 88  788  517  HOH HOH B . 
CA 7 HOH 89  789  1377 HOH HOH B . 
CA 7 HOH 90  790  998  HOH HOH B . 
CA 7 HOH 91  791  1047 HOH HOH B . 
CA 7 HOH 92  792  1816 HOH HOH B . 
CA 7 HOH 93  793  37   HOH HOH B . 
CA 7 HOH 94  794  1217 HOH HOH B . 
CA 7 HOH 95  795  2119 HOH HOH B . 
CA 7 HOH 96  796  295  HOH HOH B . 
CA 7 HOH 97  797  2053 HOH HOH B . 
CA 7 HOH 98  798  1535 HOH HOH B . 
CA 7 HOH 99  799  1960 HOH HOH B . 
CA 7 HOH 100 800  389  HOH HOH B . 
CA 7 HOH 101 801  14   HOH HOH B . 
CA 7 HOH 102 802  1528 HOH HOH B . 
CA 7 HOH 103 803  2015 HOH HOH B . 
CA 7 HOH 104 804  1538 HOH HOH B . 
CA 7 HOH 105 805  112  HOH HOH B . 
CA 7 HOH 106 806  1543 HOH HOH B . 
CA 7 HOH 107 807  199  HOH HOH B . 
CA 7 HOH 108 808  361  HOH HOH B . 
CA 7 HOH 109 809  1823 HOH HOH B . 
CA 7 HOH 110 810  1942 HOH HOH B . 
CA 7 HOH 111 811  468  HOH HOH B . 
CA 7 HOH 112 812  867  HOH HOH B . 
CA 7 HOH 113 813  261  HOH HOH B . 
CA 7 HOH 114 814  1428 HOH HOH B . 
CA 7 HOH 115 815  1583 HOH HOH B . 
CA 7 HOH 116 816  2035 HOH HOH B . 
CA 7 HOH 117 817  610  HOH HOH B . 
CA 7 HOH 118 818  1293 HOH HOH B . 
CA 7 HOH 119 819  2032 HOH HOH B . 
CA 7 HOH 120 820  1438 HOH HOH B . 
CA 7 HOH 121 821  1585 HOH HOH B . 
CA 7 HOH 122 822  330  HOH HOH B . 
CA 7 HOH 123 823  1003 HOH HOH B . 
CA 7 HOH 124 824  956  HOH HOH B . 
CA 7 HOH 125 825  220  HOH HOH B . 
CA 7 HOH 126 826  754  HOH HOH B . 
CA 7 HOH 127 827  1463 HOH HOH B . 
CA 7 HOH 128 828  50   HOH HOH B . 
CA 7 HOH 129 829  121  HOH HOH B . 
CA 7 HOH 130 830  1426 HOH HOH B . 
CA 7 HOH 131 831  8    HOH HOH B . 
CA 7 HOH 132 832  682  HOH HOH B . 
CA 7 HOH 133 833  1821 HOH HOH B . 
CA 7 HOH 134 834  124  HOH HOH B . 
CA 7 HOH 135 835  1642 HOH HOH B . 
CA 7 HOH 136 836  332  HOH HOH B . 
CA 7 HOH 137 837  2046 HOH HOH B . 
CA 7 HOH 138 838  299  HOH HOH B . 
CA 7 HOH 139 839  206  HOH HOH B . 
CA 7 HOH 140 840  1519 HOH HOH B . 
CA 7 HOH 141 841  247  HOH HOH B . 
CA 7 HOH 142 842  1474 HOH HOH B . 
CA 7 HOH 143 843  379  HOH HOH B . 
CA 7 HOH 144 844  1452 HOH HOH B . 
CA 7 HOH 145 845  28   HOH HOH B . 
CA 7 HOH 146 846  1379 HOH HOH B . 
CA 7 HOH 147 847  512  HOH HOH B . 
CA 7 HOH 148 848  1549 HOH HOH B . 
CA 7 HOH 149 849  1471 HOH HOH B . 
CA 7 HOH 150 850  1520 HOH HOH B . 
CA 7 HOH 151 851  944  HOH HOH B . 
CA 7 HOH 152 852  1733 HOH HOH B . 
CA 7 HOH 153 853  135  HOH HOH B . 
CA 7 HOH 154 854  1818 HOH HOH B . 
CA 7 HOH 155 855  1773 HOH HOH B . 
CA 7 HOH 156 856  1453 HOH HOH B . 
CA 7 HOH 157 857  459  HOH HOH B . 
CA 7 HOH 158 858  1993 HOH HOH B . 
CA 7 HOH 159 859  2039 HOH HOH B . 
CA 7 HOH 160 860  1412 HOH HOH B . 
CA 7 HOH 161 861  1589 HOH HOH B . 
CA 7 HOH 162 862  1620 HOH HOH B . 
CA 7 HOH 163 863  570  HOH HOH B . 
CA 7 HOH 164 864  978  HOH HOH B . 
CA 7 HOH 165 865  1593 HOH HOH B . 
CA 7 HOH 166 866  457  HOH HOH B . 
CA 7 HOH 167 867  521  HOH HOH B . 
CA 7 HOH 168 868  1067 HOH HOH B . 
CA 7 HOH 169 869  1656 HOH HOH B . 
CA 7 HOH 170 870  2173 HOH HOH B . 
CA 7 HOH 171 871  646  HOH HOH B . 
CA 7 HOH 172 872  19   HOH HOH B . 
CA 7 HOH 173 873  622  HOH HOH B . 
CA 7 HOH 174 874  1522 HOH HOH B . 
CA 7 HOH 175 875  1584 HOH HOH B . 
CA 7 HOH 176 876  1253 HOH HOH B . 
CA 7 HOH 177 877  1470 HOH HOH B . 
CA 7 HOH 178 878  1559 HOH HOH B . 
CA 7 HOH 179 879  496  HOH HOH B . 
CA 7 HOH 180 880  276  HOH HOH B . 
CA 7 HOH 181 881  36   HOH HOH B . 
CA 7 HOH 182 882  208  HOH HOH B . 
CA 7 HOH 183 883  1588 HOH HOH B . 
CA 7 HOH 184 884  416  HOH HOH B . 
CA 7 HOH 185 885  130  HOH HOH B . 
CA 7 HOH 186 886  1832 HOH HOH B . 
CA 7 HOH 187 887  52   HOH HOH B . 
CA 7 HOH 188 888  1791 HOH HOH B . 
CA 7 HOH 189 889  186  HOH HOH B . 
CA 7 HOH 190 890  770  HOH HOH B . 
CA 7 HOH 191 891  34   HOH HOH B . 
CA 7 HOH 192 892  443  HOH HOH B . 
CA 7 HOH 193 893  4    HOH HOH B . 
CA 7 HOH 194 894  475  HOH HOH B . 
CA 7 HOH 195 895  1537 HOH HOH B . 
CA 7 HOH 196 896  1339 HOH HOH B . 
CA 7 HOH 197 897  872  HOH HOH B . 
CA 7 HOH 198 898  100  HOH HOH B . 
CA 7 HOH 199 899  1005 HOH HOH B . 
CA 7 HOH 200 900  250  HOH HOH B . 
CA 7 HOH 201 901  320  HOH HOH B . 
CA 7 HOH 202 902  692  HOH HOH B . 
CA 7 HOH 203 903  72   HOH HOH B . 
CA 7 HOH 204 904  1432 HOH HOH B . 
CA 7 HOH 205 905  1454 HOH HOH B . 
CA 7 HOH 206 906  325  HOH HOH B . 
CA 7 HOH 207 907  534  HOH HOH B . 
CA 7 HOH 208 908  837  HOH HOH B . 
CA 7 HOH 209 909  1178 HOH HOH B . 
CA 7 HOH 210 910  258  HOH HOH B . 
CA 7 HOH 211 911  2018 HOH HOH B . 
CA 7 HOH 212 912  407  HOH HOH B . 
CA 7 HOH 213 913  470  HOH HOH B . 
CA 7 HOH 214 914  723  HOH HOH B . 
CA 7 HOH 215 915  469  HOH HOH B . 
CA 7 HOH 216 916  1056 HOH HOH B . 
CA 7 HOH 217 917  693  HOH HOH B . 
CA 7 HOH 218 918  578  HOH HOH B . 
CA 7 HOH 219 919  440  HOH HOH B . 
CA 7 HOH 220 920  96   HOH HOH B . 
CA 7 HOH 221 921  2183 HOH HOH B . 
CA 7 HOH 222 922  1272 HOH HOH B . 
CA 7 HOH 223 923  2118 HOH HOH B . 
CA 7 HOH 224 924  708  HOH HOH B . 
CA 7 HOH 225 925  273  HOH HOH B . 
CA 7 HOH 226 926  2190 HOH HOH B . 
CA 7 HOH 227 927  2164 HOH HOH B . 
CA 7 HOH 228 928  1342 HOH HOH B . 
CA 7 HOH 229 929  1059 HOH HOH B . 
CA 7 HOH 230 930  1874 HOH HOH B . 
CA 7 HOH 231 931  58   HOH HOH B . 
CA 7 HOH 232 932  293  HOH HOH B . 
CA 7 HOH 233 933  2131 HOH HOH B . 
CA 7 HOH 234 934  1195 HOH HOH B . 
CA 7 HOH 235 935  1680 HOH HOH B . 
CA 7 HOH 236 936  1396 HOH HOH B . 
CA 7 HOH 237 937  643  HOH HOH B . 
CA 7 HOH 238 938  11   HOH HOH B . 
CA 7 HOH 239 939  1462 HOH HOH B . 
CA 7 HOH 240 940  2162 HOH HOH B . 
CA 7 HOH 241 941  766  HOH HOH B . 
CA 7 HOH 242 942  1762 HOH HOH B . 
CA 7 HOH 243 943  604  HOH HOH B . 
CA 7 HOH 244 944  1083 HOH HOH B . 
CA 7 HOH 245 945  2052 HOH HOH B . 
CA 7 HOH 246 946  418  HOH HOH B . 
CA 7 HOH 247 947  1044 HOH HOH B . 
CA 7 HOH 248 948  624  HOH HOH B . 
CA 7 HOH 249 949  152  HOH HOH B . 
CA 7 HOH 250 950  784  HOH HOH B . 
CA 7 HOH 251 951  957  HOH HOH B . 
CA 7 HOH 252 952  1458 HOH HOH B . 
CA 7 HOH 253 953  1094 HOH HOH B . 
CA 7 HOH 254 954  881  HOH HOH B . 
CA 7 HOH 255 955  433  HOH HOH B . 
CA 7 HOH 256 956  190  HOH HOH B . 
CA 7 HOH 257 957  446  HOH HOH B . 
CA 7 HOH 258 958  476  HOH HOH B . 
CA 7 HOH 259 959  221  HOH HOH B . 
CA 7 HOH 260 960  1075 HOH HOH B . 
CA 7 HOH 261 961  408  HOH HOH B . 
CA 7 HOH 262 962  625  HOH HOH B . 
CA 7 HOH 263 963  1932 HOH HOH B . 
CA 7 HOH 264 964  958  HOH HOH B . 
CA 7 HOH 265 965  1099 HOH HOH B . 
CA 7 HOH 266 966  153  HOH HOH B . 
CA 7 HOH 267 967  256  HOH HOH B . 
CA 7 HOH 268 968  634  HOH HOH B . 
CA 7 HOH 269 969  1415 HOH HOH B . 
CA 7 HOH 270 970  1958 HOH HOH B . 
CA 7 HOH 271 971  2012 HOH HOH B . 
CA 7 HOH 272 972  1055 HOH HOH B . 
CA 7 HOH 273 973  57   HOH HOH B . 
CA 7 HOH 274 974  1028 HOH HOH B . 
CA 7 HOH 275 975  2170 HOH HOH B . 
CA 7 HOH 276 976  1464 HOH HOH B . 
CA 7 HOH 277 977  773  HOH HOH B . 
CA 7 HOH 278 978  1705 HOH HOH B . 
CA 7 HOH 279 979  77   HOH HOH B . 
CA 7 HOH 280 980  1786 HOH HOH B . 
CA 7 HOH 281 981  1060 HOH HOH B . 
CA 7 HOH 282 982  69   HOH HOH B . 
CA 7 HOH 283 983  1483 HOH HOH B . 
CA 7 HOH 284 984  1622 HOH HOH B . 
CA 7 HOH 285 985  1561 HOH HOH B . 
CA 7 HOH 286 986  24   HOH HOH B . 
CA 7 HOH 287 987  1177 HOH HOH B . 
CA 7 HOH 288 988  1429 HOH HOH B . 
CA 7 HOH 289 989  1570 HOH HOH B . 
CA 7 HOH 290 990  1782 HOH HOH B . 
CA 7 HOH 291 991  990  HOH HOH B . 
CA 7 HOH 292 992  598  HOH HOH B . 
CA 7 HOH 293 993  1090 HOH HOH B . 
CA 7 HOH 294 994  179  HOH HOH B . 
CA 7 HOH 295 995  1621 HOH HOH B . 
CA 7 HOH 296 996  1974 HOH HOH B . 
CA 7 HOH 297 997  1755 HOH HOH B . 
CA 7 HOH 298 998  636  HOH HOH B . 
CA 7 HOH 299 999  1124 HOH HOH B . 
CA 7 HOH 300 1000 786  HOH HOH B . 
CA 7 HOH 301 1001 1141 HOH HOH B . 
CA 7 HOH 302 1002 397  HOH HOH B . 
CA 7 HOH 303 1003 1647 HOH HOH B . 
CA 7 HOH 304 1004 548  HOH HOH B . 
CA 7 HOH 305 1005 104  HOH HOH B . 
CA 7 HOH 306 1006 2116 HOH HOH B . 
CA 7 HOH 307 1007 1820 HOH HOH B . 
CA 7 HOH 308 1008 205  HOH HOH B . 
CA 7 HOH 309 1009 1501 HOH HOH B . 
CA 7 HOH 310 1010 597  HOH HOH B . 
CA 7 HOH 311 1011 1279 HOH HOH B . 
CA 7 HOH 312 1012 78   HOH HOH B . 
CA 7 HOH 313 1013 1695 HOH HOH B . 
CA 7 HOH 314 1014 1084 HOH HOH B . 
CA 7 HOH 315 1015 1713 HOH HOH B . 
CA 7 HOH 316 1016 29   HOH HOH B . 
CA 7 HOH 317 1017 1937 HOH HOH B . 
CA 7 HOH 318 1018 1037 HOH HOH B . 
CA 7 HOH 319 1019 1097 HOH HOH B . 
CA 7 HOH 320 1020 1122 HOH HOH B . 
CA 7 HOH 321 1021 84   HOH HOH B . 
CA 7 HOH 322 1022 640  HOH HOH B . 
CA 7 HOH 323 1023 1552 HOH HOH B . 
CA 7 HOH 324 1024 1448 HOH HOH B . 
CA 7 HOH 325 1025 189  HOH HOH B . 
CA 7 HOH 326 1026 1465 HOH HOH B . 
CA 7 HOH 327 1027 231  HOH HOH B . 
CA 7 HOH 328 1028 352  HOH HOH B . 
CA 7 HOH 329 1029 540  HOH HOH B . 
CA 7 HOH 330 1030 557  HOH HOH B . 
CA 7 HOH 331 1031 1418 HOH HOH B . 
CA 7 HOH 332 1032 1982 HOH HOH B . 
CA 7 HOH 333 1033 808  HOH HOH B . 
CA 7 HOH 334 1034 1866 HOH HOH B . 
CA 7 HOH 335 1035 63   HOH HOH B . 
CA 7 HOH 336 1036 522  HOH HOH B . 
CA 7 HOH 337 1037 1931 HOH HOH B . 
CA 7 HOH 338 1038 1391 HOH HOH B . 
CA 7 HOH 339 1039 504  HOH HOH B . 
CA 7 HOH 340 1040 242  HOH HOH B . 
CA 7 HOH 341 1041 862  HOH HOH B . 
CA 7 HOH 342 1042 239  HOH HOH B . 
CA 7 HOH 343 1043 1790 HOH HOH B . 
CA 7 HOH 344 1044 1046 HOH HOH B . 
CA 7 HOH 345 1045 590  HOH HOH B . 
CA 7 HOH 346 1046 1789 HOH HOH B . 
CA 7 HOH 347 1047 477  HOH HOH B . 
CA 7 HOH 348 1048 2179 HOH HOH B . 
CA 7 HOH 349 1049 594  HOH HOH B . 
CA 7 HOH 350 1050 1368 HOH HOH B . 
CA 7 HOH 351 1051 1066 HOH HOH B . 
CA 7 HOH 352 1052 301  HOH HOH B . 
CA 7 HOH 353 1053 1496 HOH HOH B . 
CA 7 HOH 354 1054 1224 HOH HOH B . 
CA 7 HOH 355 1055 185  HOH HOH B . 
CA 7 HOH 356 1056 103  HOH HOH B . 
CA 7 HOH 357 1057 1300 HOH HOH B . 
CA 7 HOH 358 1058 979  HOH HOH B . 
CA 7 HOH 359 1059 1863 HOH HOH B . 
CA 7 HOH 360 1060 191  HOH HOH B . 
CA 7 HOH 361 1061 329  HOH HOH B . 
CA 7 HOH 362 1062 1676 HOH HOH B . 
CA 7 HOH 363 1063 1108 HOH HOH B . 
CA 7 HOH 364 1064 413  HOH HOH B . 
CA 7 HOH 365 1065 111  HOH HOH B . 
CA 7 HOH 366 1066 2175 HOH HOH B . 
CA 7 HOH 367 1067 399  HOH HOH B . 
CA 7 HOH 368 1068 630  HOH HOH B . 
CA 7 HOH 369 1069 366  HOH HOH B . 
CA 7 HOH 370 1070 984  HOH HOH B . 
CA 7 HOH 371 1071 382  HOH HOH B . 
CA 7 HOH 372 1072 1748 HOH HOH B . 
CA 7 HOH 373 1073 1456 HOH HOH B . 
CA 7 HOH 374 1074 697  HOH HOH B . 
CA 7 HOH 375 1075 409  HOH HOH B . 
CA 7 HOH 376 1076 1806 HOH HOH B . 
CA 7 HOH 377 1077 1962 HOH HOH B . 
CA 7 HOH 378 1078 1256 HOH HOH B . 
CA 7 HOH 379 1079 526  HOH HOH B . 
CA 7 HOH 380 1080 2071 HOH HOH B . 
CA 7 HOH 381 1081 1831 HOH HOH B . 
CA 7 HOH 382 1082 749  HOH HOH B . 
CA 7 HOH 383 1083 35   HOH HOH B . 
CA 7 HOH 384 1084 170  HOH HOH B . 
CA 7 HOH 385 1085 180  HOH HOH B . 
CA 7 HOH 386 1086 607  HOH HOH B . 
CA 7 HOH 387 1087 1912 HOH HOH B . 
CA 7 HOH 388 1088 1054 HOH HOH B . 
CA 7 HOH 389 1089 321  HOH HOH B . 
CA 7 HOH 390 1090 445  HOH HOH B . 
CA 7 HOH 391 1091 462  HOH HOH B . 
CA 7 HOH 392 1092 806  HOH HOH B . 
CA 7 HOH 393 1093 633  HOH HOH B . 
CA 7 HOH 394 1094 1378 HOH HOH B . 
CA 7 HOH 395 1095 1811 HOH HOH B . 
CA 7 HOH 396 1096 2105 HOH HOH B . 
CA 7 HOH 397 1097 729  HOH HOH B . 
CA 7 HOH 398 1098 661  HOH HOH B . 
CA 7 HOH 399 1099 1772 HOH HOH B . 
CA 7 HOH 400 1100 1434 HOH HOH B . 
CA 7 HOH 401 1101 2102 HOH HOH B . 
CA 7 HOH 402 1102 566  HOH HOH B . 
CA 7 HOH 403 1103 1936 HOH HOH B . 
CA 7 HOH 404 1104 182  HOH HOH B . 
CA 7 HOH 405 1105 1316 HOH HOH B . 
CA 7 HOH 406 1106 1137 HOH HOH B . 
CA 7 HOH 407 1107 602  HOH HOH B . 
CA 7 HOH 408 1108 467  HOH HOH B . 
CA 7 HOH 409 1109 1196 HOH HOH B . 
CA 7 HOH 410 1110 2014 HOH HOH B . 
CA 7 HOH 411 1111 1072 HOH HOH B . 
CA 7 HOH 412 1112 919  HOH HOH B . 
CA 7 HOH 413 1113 823  HOH HOH B . 
CA 7 HOH 414 1114 335  HOH HOH B . 
CA 7 HOH 415 1115 1004 HOH HOH B . 
CA 7 HOH 416 1116 1112 HOH HOH B . 
CA 7 HOH 417 1117 1371 HOH HOH B . 
CA 7 HOH 418 1118 2098 HOH HOH B . 
CA 7 HOH 419 1119 1437 HOH HOH B . 
CA 7 HOH 420 1120 290  HOH HOH B . 
CA 7 HOH 421 1121 667  HOH HOH B . 
CA 7 HOH 422 1122 1985 HOH HOH B . 
CA 7 HOH 423 1123 1893 HOH HOH B . 
CA 7 HOH 424 1124 1482 HOH HOH B . 
CA 7 HOH 425 1125 983  HOH HOH B . 
CA 7 HOH 426 1126 1057 HOH HOH B . 
CA 7 HOH 427 1127 1868 HOH HOH B . 
CA 7 HOH 428 1128 1541 HOH HOH B . 
CA 7 HOH 429 1129 895  HOH HOH B . 
CA 7 HOH 430 1130 1804 HOH HOH B . 
CA 7 HOH 431 1131 1367 HOH HOH B . 
CA 7 HOH 432 1132 1890 HOH HOH B . 
CA 7 HOH 433 1133 150  HOH HOH B . 
CA 7 HOH 434 1134 2160 HOH HOH B . 
CA 7 HOH 435 1135 1609 HOH HOH B . 
CA 7 HOH 436 1136 870  HOH HOH B . 
CA 7 HOH 437 1137 1888 HOH HOH B . 
CA 7 HOH 438 1138 2167 HOH HOH B . 
CA 7 HOH 439 1139 1896 HOH HOH B . 
CA 7 HOH 440 1140 1653 HOH HOH B . 
CA 7 HOH 441 1141 435  HOH HOH B . 
CA 7 HOH 442 1142 1910 HOH HOH B . 
CA 7 HOH 443 1143 1633 HOH HOH B . 
CA 7 HOH 444 1144 1965 HOH HOH B . 
CA 7 HOH 445 1145 656  HOH HOH B . 
CA 7 HOH 446 1146 852  HOH HOH B . 
CA 7 HOH 447 1147 1148 HOH HOH B . 
CA 7 HOH 448 1148 815  HOH HOH B . 
CA 7 HOH 449 1149 742  HOH HOH B . 
CA 7 HOH 450 1150 1902 HOH HOH B . 
CA 7 HOH 451 1151 1400 HOH HOH B . 
CA 7 HOH 452 1152 2136 HOH HOH B . 
CA 7 HOH 453 1153 1375 HOH HOH B . 
CA 7 HOH 454 1154 1318 HOH HOH B . 
CA 7 HOH 455 1155 405  HOH HOH B . 
CA 7 HOH 456 1156 437  HOH HOH B . 
CA 7 HOH 457 1157 367  HOH HOH B . 
CA 7 HOH 458 1158 1756 HOH HOH B . 
CA 7 HOH 459 1159 917  HOH HOH B . 
CA 7 HOH 460 1160 1289 HOH HOH B . 
CA 7 HOH 461 1161 791  HOH HOH B . 
CA 7 HOH 462 1162 652  HOH HOH B . 
CA 7 HOH 463 1163 2158 HOH HOH B . 
CA 7 HOH 464 1164 744  HOH HOH B . 
CA 7 HOH 465 1165 705  HOH HOH B . 
CA 7 HOH 466 1166 740  HOH HOH B . 
CA 7 HOH 467 1167 1317 HOH HOH B . 
CA 7 HOH 468 1168 287  HOH HOH B . 
CA 7 HOH 469 1169 828  HOH HOH B . 
CA 7 HOH 470 1170 813  HOH HOH B . 
CA 7 HOH 471 1171 426  HOH HOH B . 
CA 7 HOH 472 1172 1759 HOH HOH B . 
CA 7 HOH 473 1173 691  HOH HOH B . 
CA 7 HOH 474 1174 929  HOH HOH B . 
CA 7 HOH 475 1175 1911 HOH HOH B . 
CA 7 HOH 476 1176 1693 HOH HOH B . 
CA 7 HOH 477 1177 809  HOH HOH B . 
CA 7 HOH 478 1178 1741 HOH HOH B . 
CA 7 HOH 479 1179 908  HOH HOH B . 
CA 7 HOH 480 1180 2088 HOH HOH B . 
CA 7 HOH 481 1181 1226 HOH HOH B . 
CA 7 HOH 482 1182 1678 HOH HOH B . 
CA 7 HOH 483 1183 1126 HOH HOH B . 
CA 7 HOH 484 1184 853  HOH HOH B . 
CA 7 HOH 485 1185 552  HOH HOH B . 
CA 7 HOH 486 1186 1665 HOH HOH B . 
CA 7 HOH 487 1187 1807 HOH HOH B . 
CA 7 HOH 488 1188 912  HOH HOH B . 
CA 7 HOH 489 1189 1600 HOH HOH B . 
CA 7 HOH 490 1190 1321 HOH HOH B . 
CA 7 HOH 491 1191 1322 HOH HOH B . 
CA 7 HOH 492 1192 1672 HOH HOH B . 
CA 7 HOH 493 1193 2085 HOH HOH B . 
CA 7 HOH 494 1194 771  HOH HOH B . 
CA 7 HOH 495 1195 1068 HOH HOH B . 
CA 7 HOH 496 1196 1170 HOH HOH B . 
CA 7 HOH 497 1197 1171 HOH HOH B . 
CA 7 HOH 498 1198 1883 HOH HOH B . 
CA 7 HOH 499 1199 922  HOH HOH B . 
CA 7 HOH 500 1200 1159 HOH HOH B . 
CA 7 HOH 501 1201 889  HOH HOH B . 
CA 7 HOH 502 1202 1392 HOH HOH B . 
CA 7 HOH 503 1203 525  HOH HOH B . 
CA 7 HOH 504 1204 686  HOH HOH B . 
CA 7 HOH 505 1205 924  HOH HOH B . 
CA 7 HOH 506 1206 709  HOH HOH B . 
CA 7 HOH 507 1207 822  HOH HOH B . 
CA 7 HOH 508 1208 906  HOH HOH B . 
CA 7 HOH 509 1209 934  HOH HOH B . 
CA 7 HOH 510 1210 1671 HOH HOH B . 
CA 7 HOH 511 1211 1922 HOH HOH B . 
CA 7 HOH 512 1212 915  HOH HOH B . 
CA 7 HOH 513 1213 1160 HOH HOH B . 
CA 7 HOH 514 1214 900  HOH HOH B . 
CA 7 HOH 515 1215 1401 HOH HOH B . 
DA 7 HOH 1   701  558  HOH HOH C . 
DA 7 HOH 2   702  1802 HOH HOH C . 
DA 7 HOH 3   703  1298 HOH HOH C . 
DA 7 HOH 4   704  1529 HOH HOH C . 
DA 7 HOH 5   705  280  HOH HOH C . 
DA 7 HOH 6   706  1435 HOH HOH C . 
DA 7 HOH 7   707  1388 HOH HOH C . 
DA 7 HOH 8   708  484  HOH HOH C . 
DA 7 HOH 9   709  1690 HOH HOH C . 
DA 7 HOH 10  710  1222 HOH HOH C . 
DA 7 HOH 11  711  264  HOH HOH C . 
DA 7 HOH 12  712  972  HOH HOH C . 
DA 7 HOH 13  713  1290 HOH HOH C . 
DA 7 HOH 14  714  2149 HOH HOH C . 
DA 7 HOH 15  715  2099 HOH HOH C . 
DA 7 HOH 16  716  140  HOH HOH C . 
DA 7 HOH 17  717  950  HOH HOH C . 
DA 7 HOH 18  718  629  HOH HOH C . 
DA 7 HOH 19  719  244  HOH HOH C . 
DA 7 HOH 20  720  996  HOH HOH C . 
DA 7 HOH 21  721  204  HOH HOH C . 
DA 7 HOH 22  722  109  HOH HOH C . 
DA 7 HOH 23  723  706  HOH HOH C . 
DA 7 HOH 24  724  1565 HOH HOH C . 
DA 7 HOH 25  725  541  HOH HOH C . 
DA 7 HOH 26  726  1451 HOH HOH C . 
DA 7 HOH 27  727  1093 HOH HOH C . 
DA 7 HOH 28  728  2001 HOH HOH C . 
DA 7 HOH 29  729  523  HOH HOH C . 
DA 7 HOH 30  730  2056 HOH HOH C . 
DA 7 HOH 31  731  532  HOH HOH C . 
DA 7 HOH 32  732  1508 HOH HOH C . 
DA 7 HOH 33  733  1142 HOH HOH C . 
DA 7 HOH 34  734  994  HOH HOH C . 
DA 7 HOH 35  735  406  HOH HOH C . 
DA 7 HOH 36  736  660  HOH HOH C . 
DA 7 HOH 37  737  626  HOH HOH C . 
DA 7 HOH 38  738  1264 HOH HOH C . 
DA 7 HOH 39  739  1734 HOH HOH C . 
DA 7 HOH 40  740  591  HOH HOH C . 
DA 7 HOH 41  741  22   HOH HOH C . 
DA 7 HOH 42  742  2070 HOH HOH C . 
DA 7 HOH 43  743  2023 HOH HOH C . 
DA 7 HOH 44  744  1489 HOH HOH C . 
DA 7 HOH 45  745  439  HOH HOH C . 
DA 7 HOH 46  746  698  HOH HOH C . 
DA 7 HOH 47  747  449  HOH HOH C . 
DA 7 HOH 48  748  1539 HOH HOH C . 
DA 7 HOH 49  749  1849 HOH HOH C . 
DA 7 HOH 50  750  203  HOH HOH C . 
DA 7 HOH 51  751  2135 HOH HOH C . 
DA 7 HOH 52  752  1664 HOH HOH C . 
DA 7 HOH 53  753  1517 HOH HOH C . 
DA 7 HOH 54  754  1574 HOH HOH C . 
DA 7 HOH 55  755  340  HOH HOH C . 
DA 7 HOH 56  756  49   HOH HOH C . 
DA 7 HOH 57  757  1027 HOH HOH C . 
DA 7 HOH 58  758  655  HOH HOH C . 
DA 7 HOH 59  759  23   HOH HOH C . 
DA 7 HOH 60  760  1607 HOH HOH C . 
DA 7 HOH 61  761  1276 HOH HOH C . 
DA 7 HOH 62  762  555  HOH HOH C . 
DA 7 HOH 63  763  39   HOH HOH C . 
DA 7 HOH 64  764  1581 HOH HOH C . 
DA 7 HOH 65  765  2064 HOH HOH C . 
DA 7 HOH 66  766  662  HOH HOH C . 
DA 7 HOH 67  767  755  HOH HOH C . 
DA 7 HOH 68  768  1639 HOH HOH C . 
DA 7 HOH 69  769  1176 HOH HOH C . 
DA 7 HOH 70  770  954  HOH HOH C . 
DA 7 HOH 71  771  1125 HOH HOH C . 
DA 7 HOH 72  772  816  HOH HOH C . 
DA 7 HOH 73  773  565  HOH HOH C . 
DA 7 HOH 74  774  1750 HOH HOH C . 
DA 7 HOH 75  775  2075 HOH HOH C . 
DA 7 HOH 76  776  763  HOH HOH C . 
DA 7 HOH 77  777  631  HOH HOH C . 
DA 7 HOH 78  778  2123 HOH HOH C . 
DA 7 HOH 79  779  1991 HOH HOH C . 
DA 7 HOH 80  780  1737 HOH HOH C . 
DA 7 HOH 81  781  2008 HOH HOH C . 
DA 7 HOH 82  782  1476 HOH HOH C . 
DA 7 HOH 83  783  353  HOH HOH C . 
DA 7 HOH 84  784  114  HOH HOH C . 
DA 7 HOH 85  785  1707 HOH HOH C . 
DA 7 HOH 86  786  596  HOH HOH C . 
DA 7 HOH 87  787  582  HOH HOH C . 
DA 7 HOH 88  788  2059 HOH HOH C . 
DA 7 HOH 89  789  775  HOH HOH C . 
DA 7 HOH 90  790  1109 HOH HOH C . 
DA 7 HOH 91  791  1417 HOH HOH C . 
DA 7 HOH 92  792  980  HOH HOH C . 
DA 7 HOH 93  793  294  HOH HOH C . 
DA 7 HOH 94  794  85   HOH HOH C . 
DA 7 HOH 95  795  162  HOH HOH C . 
DA 7 HOH 96  796  748  HOH HOH C . 
DA 7 HOH 97  797  291  HOH HOH C . 
DA 7 HOH 98  798  1631 HOH HOH C . 
DA 7 HOH 99  799  2040 HOH HOH C . 
DA 7 HOH 100 800  1370 HOH HOH C . 
DA 7 HOH 101 801  1781 HOH HOH C . 
DA 7 HOH 102 802  1573 HOH HOH C . 
DA 7 HOH 103 803  324  HOH HOH C . 
DA 7 HOH 104 804  2    HOH HOH C . 
DA 7 HOH 105 805  2058 HOH HOH C . 
DA 7 HOH 106 806  414  HOH HOH C . 
DA 7 HOH 107 807  1525 HOH HOH C . 
DA 7 HOH 108 808  508  HOH HOH C . 
DA 7 HOH 109 809  1882 HOH HOH C . 
DA 7 HOH 110 810  1670 HOH HOH C . 
DA 7 HOH 111 811  305  HOH HOH C . 
DA 7 HOH 112 812  40   HOH HOH C . 
DA 7 HOH 113 813  716  HOH HOH C . 
DA 7 HOH 114 814  601  HOH HOH C . 
DA 7 HOH 115 815  2079 HOH HOH C . 
DA 7 HOH 116 816  1636 HOH HOH C . 
DA 7 HOH 117 817  1623 HOH HOH C . 
DA 7 HOH 118 818  1697 HOH HOH C . 
DA 7 HOH 119 819  314  HOH HOH C . 
DA 7 HOH 120 820  154  HOH HOH C . 
DA 7 HOH 121 821  1557 HOH HOH C . 
DA 7 HOH 122 822  230  HOH HOH C . 
DA 7 HOH 123 823  1894 HOH HOH C . 
DA 7 HOH 124 824  1443 HOH HOH C . 
DA 7 HOH 125 825  721  HOH HOH C . 
DA 7 HOH 126 826  1469 HOH HOH C . 
DA 7 HOH 127 827  267  HOH HOH C . 
DA 7 HOH 128 828  390  HOH HOH C . 
DA 7 HOH 129 829  2104 HOH HOH C . 
DA 7 HOH 130 830  2022 HOH HOH C . 
DA 7 HOH 131 831  88   HOH HOH C . 
DA 7 HOH 132 832  213  HOH HOH C . 
DA 7 HOH 133 833  1571 HOH HOH C . 
DA 7 HOH 134 834  259  HOH HOH C . 
DA 7 HOH 135 835  61   HOH HOH C . 
DA 7 HOH 136 836  648  HOH HOH C . 
DA 7 HOH 137 837  1498 HOH HOH C . 
DA 7 HOH 138 838  1708 HOH HOH C . 
DA 7 HOH 139 839  1439 HOH HOH C . 
DA 7 HOH 140 840  1294 HOH HOH C . 
DA 7 HOH 141 841  1361 HOH HOH C . 
DA 7 HOH 142 842  1039 HOH HOH C . 
DA 7 HOH 143 843  42   HOH HOH C . 
DA 7 HOH 144 844  310  HOH HOH C . 
DA 7 HOH 145 845  334  HOH HOH C . 
DA 7 HOH 146 846  1299 HOH HOH C . 
DA 7 HOH 147 847  1467 HOH HOH C . 
DA 7 HOH 148 848  1687 HOH HOH C . 
DA 7 HOH 149 849  1951 HOH HOH C . 
DA 7 HOH 150 850  1346 HOH HOH C . 
DA 7 HOH 151 851  1132 HOH HOH C . 
DA 7 HOH 152 852  234  HOH HOH C . 
DA 7 HOH 153 853  700  HOH HOH C . 
DA 7 HOH 154 854  1086 HOH HOH C . 
DA 7 HOH 155 855  343  HOH HOH C . 
DA 7 HOH 156 856  1440 HOH HOH C . 
DA 7 HOH 157 857  871  HOH HOH C . 
DA 7 HOH 158 858  101  HOH HOH C . 
DA 7 HOH 159 859  26   HOH HOH C . 
DA 7 HOH 160 860  955  HOH HOH C . 
DA 7 HOH 161 861  1719 HOH HOH C . 
DA 7 HOH 162 862  760  HOH HOH C . 
DA 7 HOH 163 863  362  HOH HOH C . 
DA 7 HOH 164 864  1506 HOH HOH C . 
DA 7 HOH 165 865  1199 HOH HOH C . 
DA 7 HOH 166 866  2029 HOH HOH C . 
DA 7 HOH 167 867  412  HOH HOH C . 
DA 7 HOH 168 868  657  HOH HOH C . 
DA 7 HOH 169 869  666  HOH HOH C . 
DA 7 HOH 170 870  174  HOH HOH C . 
DA 7 HOH 171 871  1062 HOH HOH C . 
DA 7 HOH 172 872  322  HOH HOH C . 
DA 7 HOH 173 873  1492 HOH HOH C . 
DA 7 HOH 174 874  1651 HOH HOH C . 
DA 7 HOH 175 875  1788 HOH HOH C . 
DA 7 HOH 176 876  358  HOH HOH C . 
DA 7 HOH 177 877  422  HOH HOH C . 
DA 7 HOH 178 878  184  HOH HOH C . 
DA 7 HOH 179 879  81   HOH HOH C . 
DA 7 HOH 180 880  378  HOH HOH C . 
DA 7 HOH 181 881  217  HOH HOH C . 
DA 7 HOH 182 882  31   HOH HOH C . 
DA 7 HOH 183 883  216  HOH HOH C . 
DA 7 HOH 184 884  795  HOH HOH C . 
DA 7 HOH 185 885  1716 HOH HOH C . 
DA 7 HOH 186 886  119  HOH HOH C . 
DA 7 HOH 187 887  2150 HOH HOH C . 
DA 7 HOH 188 888  268  HOH HOH C . 
DA 7 HOH 189 889  711  HOH HOH C . 
DA 7 HOH 190 890  383  HOH HOH C . 
DA 7 HOH 191 891  883  HOH HOH C . 
DA 7 HOH 192 892  564  HOH HOH C . 
DA 7 HOH 193 893  568  HOH HOH C . 
DA 7 HOH 194 894  1497 HOH HOH C . 
DA 7 HOH 195 895  798  HOH HOH C . 
DA 7 HOH 196 896  417  HOH HOH C . 
DA 7 HOH 197 897  2073 HOH HOH C . 
DA 7 HOH 198 898  304  HOH HOH C . 
DA 7 HOH 199 899  1430 HOH HOH C . 
DA 7 HOH 200 900  1244 HOH HOH C . 
DA 7 HOH 201 901  1906 HOH HOH C . 
DA 7 HOH 202 902  214  HOH HOH C . 
DA 7 HOH 203 903  1303 HOH HOH C . 
DA 7 HOH 204 904  875  HOH HOH C . 
DA 7 HOH 205 905  472  HOH HOH C . 
DA 7 HOH 206 906  271  HOH HOH C . 
DA 7 HOH 207 907  1356 HOH HOH C . 
DA 7 HOH 208 908  107  HOH HOH C . 
DA 7 HOH 209 909  1268 HOH HOH C . 
DA 7 HOH 210 910  9    HOH HOH C . 
DA 7 HOH 211 911  252  HOH HOH C . 
DA 7 HOH 212 912  2083 HOH HOH C . 
DA 7 HOH 213 913  1187 HOH HOH C . 
DA 7 HOH 214 914  997  HOH HOH C . 
DA 7 HOH 215 915  1459 HOH HOH C . 
DA 7 HOH 216 916  649  HOH HOH C . 
DA 7 HOH 217 917  402  HOH HOH C . 
DA 7 HOH 218 918  642  HOH HOH C . 
DA 7 HOH 219 919  592  HOH HOH C . 
DA 7 HOH 220 920  2020 HOH HOH C . 
DA 7 HOH 221 921  1805 HOH HOH C . 
DA 7 HOH 222 922  1295 HOH HOH C . 
DA 7 HOH 223 923  2034 HOH HOH C . 
DA 7 HOH 224 924  811  HOH HOH C . 
DA 7 HOH 225 925  1390 HOH HOH C . 
DA 7 HOH 226 926  424  HOH HOH C . 
DA 7 HOH 227 927  1230 HOH HOH C . 
DA 7 HOH 228 928  963  HOH HOH C . 
DA 7 HOH 229 929  974  HOH HOH C . 
DA 7 HOH 230 930  1532 HOH HOH C . 
DA 7 HOH 231 931  1727 HOH HOH C . 
DA 7 HOH 232 932  1423 HOH HOH C . 
DA 7 HOH 233 933  298  HOH HOH C . 
DA 7 HOH 234 934  1749 HOH HOH C . 
DA 7 HOH 235 935  2007 HOH HOH C . 
DA 7 HOH 236 936  17   HOH HOH C . 
DA 7 HOH 237 937  524  HOH HOH C . 
DA 7 HOH 238 938  1393 HOH HOH C . 
DA 7 HOH 239 939  491  HOH HOH C . 
DA 7 HOH 240 940  312  HOH HOH C . 
DA 7 HOH 241 941  1058 HOH HOH C . 
DA 7 HOH 242 942  136  HOH HOH C . 
DA 7 HOH 243 943  725  HOH HOH C . 
DA 7 HOH 244 944  187  HOH HOH C . 
DA 7 HOH 245 945  1903 HOH HOH C . 
DA 7 HOH 246 946  964  HOH HOH C . 
DA 7 HOH 247 947  444  HOH HOH C . 
DA 7 HOH 248 948  1615 HOH HOH C . 
DA 7 HOH 249 949  15   HOH HOH C . 
DA 7 HOH 250 950  1325 HOH HOH C . 
DA 7 HOH 251 951  2144 HOH HOH C . 
DA 7 HOH 252 952  145  HOH HOH C . 
DA 7 HOH 253 953  777  HOH HOH C . 
DA 7 HOH 254 954  616  HOH HOH C . 
DA 7 HOH 255 955  1578 HOH HOH C . 
DA 7 HOH 256 956  1652 HOH HOH C . 
DA 7 HOH 257 957  313  HOH HOH C . 
DA 7 HOH 258 958  1085 HOH HOH C . 
DA 7 HOH 259 959  1332 HOH HOH C . 
DA 7 HOH 260 960  1579 HOH HOH C . 
DA 7 HOH 261 961  2146 HOH HOH C . 
DA 7 HOH 262 962  550  HOH HOH C . 
DA 7 HOH 263 963  699  HOH HOH C . 
DA 7 HOH 264 964  1413 HOH HOH C . 
DA 7 HOH 265 965  2151 HOH HOH C . 
DA 7 HOH 266 966  587  HOH HOH C . 
DA 7 HOH 267 967  801  HOH HOH C . 
DA 7 HOH 268 968  1867 HOH HOH C . 
DA 7 HOH 269 969  374  HOH HOH C . 
DA 7 HOH 270 970  844  HOH HOH C . 
DA 7 HOH 271 971  2019 HOH HOH C . 
DA 7 HOH 272 972  1800 HOH HOH C . 
DA 7 HOH 273 973  2117 HOH HOH C . 
DA 7 HOH 274 974  1577 HOH HOH C . 
DA 7 HOH 275 975  1663 HOH HOH C . 
DA 7 HOH 276 976  1915 HOH HOH C . 
DA 7 HOH 277 977  386  HOH HOH C . 
DA 7 HOH 278 978  1049 HOH HOH C . 
DA 7 HOH 279 979  1117 HOH HOH C . 
DA 7 HOH 280 980  1566 HOH HOH C . 
DA 7 HOH 281 981  712  HOH HOH C . 
DA 7 HOH 282 982  533  HOH HOH C . 
DA 7 HOH 283 983  73   HOH HOH C . 
DA 7 HOH 284 984  429  HOH HOH C . 
DA 7 HOH 285 985  490  HOH HOH C . 
DA 7 HOH 286 986  678  HOH HOH C . 
DA 7 HOH 287 987  365  HOH HOH C . 
DA 7 HOH 288 988  263  HOH HOH C . 
DA 7 HOH 289 989  2155 HOH HOH C . 
DA 7 HOH 290 990  80   HOH HOH C . 
DA 7 HOH 291 991  1280 HOH HOH C . 
DA 7 HOH 292 992  16   HOH HOH C . 
DA 7 HOH 293 993  493  HOH HOH C . 
DA 7 HOH 294 994  1643 HOH HOH C . 
DA 7 HOH 295 995  1533 HOH HOH C . 
DA 7 HOH 296 996  1051 HOH HOH C . 
DA 7 HOH 297 997  1548 HOH HOH C . 
DA 7 HOH 298 998  543  HOH HOH C . 
DA 7 HOH 299 999  2066 HOH HOH C . 
DA 7 HOH 300 1000 2028 HOH HOH C . 
DA 7 HOH 301 1001 1408 HOH HOH C . 
DA 7 HOH 302 1002 86   HOH HOH C . 
DA 7 HOH 303 1003 458  HOH HOH C . 
DA 7 HOH 304 1004 973  HOH HOH C . 
DA 7 HOH 305 1005 1540 HOH HOH C . 
DA 7 HOH 306 1006 193  HOH HOH C . 
DA 7 HOH 307 1007 1345 HOH HOH C . 
DA 7 HOH 308 1008 1315 HOH HOH C . 
DA 7 HOH 309 1009 654  HOH HOH C . 
DA 7 HOH 310 1010 245  HOH HOH C . 
DA 7 HOH 311 1011 638  HOH HOH C . 
DA 7 HOH 312 1012 1580 HOH HOH C . 
DA 7 HOH 313 1013 43   HOH HOH C . 
DA 7 HOH 314 1014 520  HOH HOH C . 
DA 7 HOH 315 1015 282  HOH HOH C . 
DA 7 HOH 316 1016 357  HOH HOH C . 
DA 7 HOH 317 1017 1018 HOH HOH C . 
DA 7 HOH 318 1018 176  HOH HOH C . 
DA 7 HOH 319 1019 1001 HOH HOH C . 
DA 7 HOH 320 1020 302  HOH HOH C . 
DA 7 HOH 321 1021 702  HOH HOH C . 
DA 7 HOH 322 1022 1905 HOH HOH C . 
DA 7 HOH 323 1023 2152 HOH HOH C . 
DA 7 HOH 324 1024 802  HOH HOH C . 
DA 7 HOH 325 1025 2130 HOH HOH C . 
DA 7 HOH 326 1026 2021 HOH HOH C . 
DA 7 HOH 327 1027 1121 HOH HOH C . 
DA 7 HOH 328 1028 460  HOH HOH C . 
DA 7 HOH 329 1029 827  HOH HOH C . 
DA 7 HOH 330 1030 120  HOH HOH C . 
DA 7 HOH 331 1031 1728 HOH HOH C . 
DA 7 HOH 332 1032 2166 HOH HOH C . 
DA 7 HOH 333 1033 1255 HOH HOH C . 
DA 7 HOH 334 1034 1524 HOH HOH C . 
DA 7 HOH 335 1035 1145 HOH HOH C . 
DA 7 HOH 336 1036 528  HOH HOH C . 
DA 7 HOH 337 1037 2005 HOH HOH C . 
DA 7 HOH 338 1038 518  HOH HOH C . 
DA 7 HOH 339 1039 1263 HOH HOH C . 
DA 7 HOH 340 1040 2045 HOH HOH C . 
DA 7 HOH 341 1041 83   HOH HOH C . 
DA 7 HOH 342 1042 240  HOH HOH C . 
DA 7 HOH 343 1043 228  HOH HOH C . 
DA 7 HOH 344 1044 743  HOH HOH C . 
DA 7 HOH 345 1045 1813 HOH HOH C . 
DA 7 HOH 346 1046 1306 HOH HOH C . 
DA 7 HOH 347 1047 675  HOH HOH C . 
DA 7 HOH 348 1048 328  HOH HOH C . 
DA 7 HOH 349 1049 1198 HOH HOH C . 
DA 7 HOH 350 1050 620  HOH HOH C . 
DA 7 HOH 351 1051 1395 HOH HOH C . 
DA 7 HOH 352 1052 935  HOH HOH C . 
DA 7 HOH 353 1053 739  HOH HOH C . 
DA 7 HOH 354 1054 275  HOH HOH C . 
DA 7 HOH 355 1055 2110 HOH HOH C . 
DA 7 HOH 356 1056 1794 HOH HOH C . 
DA 7 HOH 357 1057 1374 HOH HOH C . 
DA 7 HOH 358 1058 1487 HOH HOH C . 
DA 7 HOH 359 1059 464  HOH HOH C . 
DA 7 HOH 360 1060 1219 HOH HOH C . 
DA 7 HOH 361 1061 1449 HOH HOH C . 
DA 7 HOH 362 1062 1845 HOH HOH C . 
DA 7 HOH 363 1063 1703 HOH HOH C . 
DA 7 HOH 364 1064 866  HOH HOH C . 
DA 7 HOH 365 1065 423  HOH HOH C . 
DA 7 HOH 366 1066 2156 HOH HOH C . 
DA 7 HOH 367 1067 1241 HOH HOH C . 
DA 7 HOH 368 1068 2000 HOH HOH C . 
DA 7 HOH 369 1069 1024 HOH HOH C . 
DA 7 HOH 370 1070 1827 HOH HOH C . 
DA 7 HOH 371 1071 1837 HOH HOH C . 
DA 7 HOH 372 1072 599  HOH HOH C . 
DA 7 HOH 373 1073 59   HOH HOH C . 
DA 7 HOH 374 1074 233  HOH HOH C . 
DA 7 HOH 375 1075 173  HOH HOH C . 
DA 7 HOH 376 1076 65   HOH HOH C . 
DA 7 HOH 377 1077 2168 HOH HOH C . 
DA 7 HOH 378 1078 2185 HOH HOH C . 
DA 7 HOH 379 1079 286  HOH HOH C . 
DA 7 HOH 380 1080 297  HOH HOH C . 
DA 7 HOH 381 1081 993  HOH HOH C . 
DA 7 HOH 382 1082 1069 HOH HOH C . 
DA 7 HOH 383 1083 1193 HOH HOH C . 
DA 7 HOH 384 1084 2065 HOH HOH C . 
DA 7 HOH 385 1085 1981 HOH HOH C . 
DA 7 HOH 386 1086 2031 HOH HOH C . 
DA 7 HOH 387 1087 635  HOH HOH C . 
DA 7 HOH 388 1088 1828 HOH HOH C . 
DA 7 HOH 389 1089 1945 HOH HOH C . 
DA 7 HOH 390 1090 575  HOH HOH C . 
DA 7 HOH 391 1091 2138 HOH HOH C . 
DA 7 HOH 392 1092 1854 HOH HOH C . 
DA 7 HOH 393 1093 53   HOH HOH C . 
DA 7 HOH 394 1094 1154 HOH HOH C . 
DA 7 HOH 395 1095 1131 HOH HOH C . 
DA 7 HOH 396 1096 1424 HOH HOH C . 
DA 7 HOH 397 1097 188  HOH HOH C . 
DA 7 HOH 398 1098 1534 HOH HOH C . 
DA 7 HOH 399 1099 1783 HOH HOH C . 
DA 7 HOH 400 1100 1712 HOH HOH C . 
DA 7 HOH 401 1101 1491 HOH HOH C . 
DA 7 HOH 402 1102 1341 HOH HOH C . 
DA 7 HOH 403 1103 2115 HOH HOH C . 
DA 7 HOH 404 1104 1829 HOH HOH C . 
DA 7 HOH 405 1105 2127 HOH HOH C . 
DA 7 HOH 406 1106 1278 HOH HOH C . 
DA 7 HOH 407 1107 1877 HOH HOH C . 
DA 7 HOH 408 1108 1302 HOH HOH C . 
DA 7 HOH 409 1109 2121 HOH HOH C . 
DA 7 HOH 410 1110 1914 HOH HOH C . 
DA 7 HOH 411 1111 1266 HOH HOH C . 
DA 7 HOH 412 1112 2095 HOH HOH C . 
DA 7 HOH 413 1113 1848 HOH HOH C . 
DA 7 HOH 414 1114 1754 HOH HOH C . 
DA 7 HOH 415 1115 741  HOH HOH C . 
DA 7 HOH 416 1116 1218 HOH HOH C . 
DA 7 HOH 417 1117 923  HOH HOH C . 
DA 7 HOH 418 1118 600  HOH HOH C . 
DA 7 HOH 419 1119 683  HOH HOH C . 
DA 7 HOH 420 1120 375  HOH HOH C . 
DA 7 HOH 421 1121 1938 HOH HOH C . 
DA 7 HOH 422 1122 925  HOH HOH C . 
DA 7 HOH 423 1123 2091 HOH HOH C . 
DA 7 HOH 424 1124 270  HOH HOH C . 
DA 7 HOH 425 1125 1221 HOH HOH C . 
DA 7 HOH 426 1126 580  HOH HOH C . 
DA 7 HOH 427 1127 1692 HOH HOH C . 
DA 7 HOH 428 1128 2089 HOH HOH C . 
DA 7 HOH 429 1129 2086 HOH HOH C . 
DA 7 HOH 430 1130 1211 HOH HOH C . 
DA 7 HOH 431 1131 780  HOH HOH C . 
DA 7 HOH 432 1132 1043 HOH HOH C . 
DA 7 HOH 433 1133 1954 HOH HOH C . 
DA 7 HOH 434 1134 1852 HOH HOH C . 
DA 7 HOH 435 1135 1404 HOH HOH C . 
DA 7 HOH 436 1136 1210 HOH HOH C . 
DA 7 HOH 437 1137 1296 HOH HOH C . 
DA 7 HOH 438 1138 1554 HOH HOH C . 
DA 7 HOH 439 1139 1364 HOH HOH C . 
DA 7 HOH 440 1140 921  HOH HOH C . 
DA 7 HOH 441 1141 1150 HOH HOH C . 
DA 7 HOH 442 1142 1111 HOH HOH C . 
DA 7 HOH 443 1143 841  HOH HOH C . 
DA 7 HOH 444 1144 885  HOH HOH C . 
DA 7 HOH 445 1145 1403 HOH HOH C . 
DA 7 HOH 446 1146 1373 HOH HOH C . 
DA 7 HOH 447 1147 891  HOH HOH C . 
DA 7 HOH 448 1148 1330 HOH HOH C . 
DA 7 HOH 449 1149 1526 HOH HOH C . 
DA 7 HOH 450 1150 1172 HOH HOH C . 
DA 7 HOH 451 1151 497  HOH HOH C . 
DA 7 HOH 452 1152 2084 HOH HOH C . 
DA 7 HOH 453 1153 834  HOH HOH C . 
DA 7 HOH 454 1154 431  HOH HOH C . 
DA 7 HOH 455 1155 1921 HOH HOH C . 
DA 7 HOH 456 1156 1405 HOH HOH C . 
DA 7 HOH 457 1157 1764 HOH HOH C . 
DA 7 HOH 458 1158 965  HOH HOH C . 
DA 7 HOH 459 1159 1284 HOH HOH C . 
DA 7 HOH 460 1160 1973 HOH HOH C . 
DA 7 HOH 461 1161 641  HOH HOH C . 
DA 7 HOH 462 1162 897  HOH HOH C . 
DA 7 HOH 463 1163 1157 HOH HOH C . 
DA 7 HOH 464 1164 914  HOH HOH C . 
DA 7 HOH 465 1165 1320 HOH HOH C . 
DA 7 HOH 466 1166 1397 HOH HOH C . 
DA 7 HOH 467 1167 681  HOH HOH C . 
DA 7 HOH 468 1168 2174 HOH HOH C . 
DA 7 HOH 469 1169 2043 HOH HOH C . 
DA 7 HOH 470 1170 1312 HOH HOH C . 
DA 7 HOH 471 1171 1232 HOH HOH C . 
DA 7 HOH 472 1172 762  HOH HOH C . 
DA 7 HOH 473 1173 904  HOH HOH C . 
DA 7 HOH 474 1174 1926 HOH HOH C . 
DA 7 HOH 475 1175 364  HOH HOH C . 
DA 7 HOH 476 1176 861  HOH HOH C . 
DA 7 HOH 477 1177 1162 HOH HOH C . 
DA 7 HOH 478 1178 1354 HOH HOH C . 
DA 7 HOH 479 1179 1333 HOH HOH C . 
DA 7 HOH 480 1180 1758 HOH HOH C . 
DA 7 HOH 481 1181 1957 HOH HOH C . 
DA 7 HOH 482 1182 348  HOH HOH C . 
DA 7 HOH 483 1183 1336 HOH HOH C . 
DA 7 HOH 484 1184 1166 HOH HOH C . 
DA 7 HOH 485 1185 718  HOH HOH C . 
DA 7 HOH 486 1186 1363 HOH HOH C . 
DA 7 HOH 487 1187 876  HOH HOH C . 
DA 7 HOH 488 1188 509  HOH HOH C . 
DA 7 HOH 489 1189 2092 HOH HOH C . 
DA 7 HOH 490 1190 1961 HOH HOH C . 
DA 7 HOH 491 1191 819  HOH HOH C . 
DA 7 HOH 492 1192 1753 HOH HOH C . 
DA 7 HOH 493 1193 559  HOH HOH C . 
DA 7 HOH 494 1194 928  HOH HOH C . 
DA 7 HOH 495 1195 911  HOH HOH C . 
DA 7 HOH 496 1196 473  HOH HOH C . 
EA 7 HOH 1   701  452  HOH HOH D . 
EA 7 HOH 2   702  1358 HOH HOH D . 
EA 7 HOH 3   703  1738 HOH HOH D . 
EA 7 HOH 4   704  1194 HOH HOH D . 
EA 7 HOH 5   705  1833 HOH HOH D . 
EA 7 HOH 6   706  1704 HOH HOH D . 
EA 7 HOH 7   707  1725 HOH HOH D . 
EA 7 HOH 8   708  1963 HOH HOH D . 
EA 7 HOH 9   709  1860 HOH HOH D . 
EA 7 HOH 10  710  2054 HOH HOH D . 
EA 7 HOH 11  711  804  HOH HOH D . 
EA 7 HOH 12  712  255  HOH HOH D . 
EA 7 HOH 13  713  307  HOH HOH D . 
EA 7 HOH 14  714  1035 HOH HOH D . 
EA 7 HOH 15  715  843  HOH HOH D . 
EA 7 HOH 16  716  593  HOH HOH D . 
EA 7 HOH 17  717  1644 HOH HOH D . 
EA 7 HOH 18  718  1204 HOH HOH D . 
EA 7 HOH 19  719  1273 HOH HOH D . 
EA 7 HOH 20  720  1746 HOH HOH D . 
EA 7 HOH 21  721  752  HOH HOH D . 
EA 7 HOH 22  722  1494 HOH HOH D . 
EA 7 HOH 23  723  1879 HOH HOH D . 
EA 7 HOH 24  724  1966 HOH HOH D . 
EA 7 HOH 25  725  253  HOH HOH D . 
EA 7 HOH 26  726  2042 HOH HOH D . 
EA 7 HOH 27  727  2154 HOH HOH D . 
EA 7 HOH 28  728  2191 HOH HOH D . 
EA 7 HOH 29  729  1355 HOH HOH D . 
EA 7 HOH 30  730  1376 HOH HOH D . 
EA 7 HOH 31  731  1632 HOH HOH D . 
EA 7 HOH 32  732  1701 HOH HOH D . 
EA 7 HOH 33  733  1495 HOH HOH D . 
EA 7 HOH 34  734  1556 HOH HOH D . 
EA 7 HOH 35  735  574  HOH HOH D . 
EA 7 HOH 36  736  2002 HOH HOH D . 
EA 7 HOH 37  737  707  HOH HOH D . 
EA 7 HOH 38  738  715  HOH HOH D . 
EA 7 HOH 39  739  644  HOH HOH D . 
EA 7 HOH 40  740  589  HOH HOH D . 
EA 7 HOH 41  741  404  HOH HOH D . 
EA 7 HOH 42  742  1983 HOH HOH D . 
EA 7 HOH 43  743  2030 HOH HOH D . 
EA 7 HOH 44  744  551  HOH HOH D . 
EA 7 HOH 45  745  757  HOH HOH D . 
EA 7 HOH 46  746  372  HOH HOH D . 
EA 7 HOH 47  747  2159 HOH HOH D . 
EA 7 HOH 48  748  48   HOH HOH D . 
EA 7 HOH 49  749  621  HOH HOH D . 
EA 7 HOH 50  750  1699 HOH HOH D . 
EA 7 HOH 51  751  1338 HOH HOH D . 
EA 7 HOH 52  752  10   HOH HOH D . 
EA 7 HOH 53  753  45   HOH HOH D . 
EA 7 HOH 54  754  134  HOH HOH D . 
EA 7 HOH 55  755  1700 HOH HOH D . 
EA 7 HOH 56  756  133  HOH HOH D . 
EA 7 HOH 57  757  2060 HOH HOH D . 
EA 7 HOH 58  758  2003 HOH HOH D . 
EA 7 HOH 59  759  695  HOH HOH D . 
EA 7 HOH 60  760  319  HOH HOH D . 
EA 7 HOH 61  761  110  HOH HOH D . 
EA 7 HOH 62  762  999  HOH HOH D . 
EA 7 HOH 63  763  609  HOH HOH D . 
EA 7 HOH 64  764  403  HOH HOH D . 
EA 7 HOH 65  765  1461 HOH HOH D . 
EA 7 HOH 66  766  1197 HOH HOH D . 
EA 7 HOH 67  767  1030 HOH HOH D . 
EA 7 HOH 68  768  1012 HOH HOH D . 
EA 7 HOH 69  769  1635 HOH HOH D . 
EA 7 HOH 70  770  1569 HOH HOH D . 
EA 7 HOH 71  771  1611 HOH HOH D . 
EA 7 HOH 72  772  1128 HOH HOH D . 
EA 7 HOH 73  773  370  HOH HOH D . 
EA 7 HOH 74  774  54   HOH HOH D . 
EA 7 HOH 75  775  1010 HOH HOH D . 
EA 7 HOH 76  776  1778 HOH HOH D . 
EA 7 HOH 77  777  21   HOH HOH D . 
EA 7 HOH 78  778  1485 HOH HOH D . 
EA 7 HOH 79  779  1998 HOH HOH D . 
EA 7 HOH 80  780  274  HOH HOH D . 
EA 7 HOH 81  781  814  HOH HOH D . 
EA 7 HOH 82  782  1711 HOH HOH D . 
EA 7 HOH 83  783  377  HOH HOH D . 
EA 7 HOH 84  784  732  HOH HOH D . 
EA 7 HOH 85  785  572  HOH HOH D . 
EA 7 HOH 86  786  1844 HOH HOH D . 
EA 7 HOH 87  787  1189 HOH HOH D . 
EA 7 HOH 88  788  1179 HOH HOH D . 
EA 7 HOH 89  789  1061 HOH HOH D . 
EA 7 HOH 90  790  948  HOH HOH D . 
EA 7 HOH 91  791  218  HOH HOH D . 
EA 7 HOH 92  792  1757 HOH HOH D . 
EA 7 HOH 93  793  724  HOH HOH D . 
EA 7 HOH 94  794  628  HOH HOH D . 
EA 7 HOH 95  795  62   HOH HOH D . 
EA 7 HOH 96  796  371  HOH HOH D . 
EA 7 HOH 97  797  1419 HOH HOH D . 
EA 7 HOH 98  798  200  HOH HOH D . 
EA 7 HOH 99  799  1507 HOH HOH D . 
EA 7 HOH 100 800  1870 HOH HOH D . 
EA 7 HOH 101 801  976  HOH HOH D . 
EA 7 HOH 102 802  13   HOH HOH D . 
EA 7 HOH 103 803  1661 HOH HOH D . 
EA 7 HOH 104 804  451  HOH HOH D . 
EA 7 HOH 105 805  202  HOH HOH D . 
EA 7 HOH 106 806  331  HOH HOH D . 
EA 7 HOH 107 807  75   HOH HOH D . 
EA 7 HOH 108 808  1901 HOH HOH D . 
EA 7 HOH 109 809  212  HOH HOH D . 
EA 7 HOH 110 810  539  HOH HOH D . 
EA 7 HOH 111 811  1089 HOH HOH D . 
EA 7 HOH 112 812  968  HOH HOH D . 
EA 7 HOH 113 813  584  HOH HOH D . 
EA 7 HOH 114 814  991  HOH HOH D . 
EA 7 HOH 115 815  1989 HOH HOH D . 
EA 7 HOH 116 816  1041 HOH HOH D . 
EA 7 HOH 117 817  158  HOH HOH D . 
EA 7 HOH 118 818  1720 HOH HOH D . 
EA 7 HOH 119 819  363  HOH HOH D . 
EA 7 HOH 120 820  2137 HOH HOH D . 
EA 7 HOH 121 821  144  HOH HOH D . 
EA 7 HOH 122 822  1045 HOH HOH D . 
EA 7 HOH 123 823  311  HOH HOH D . 
EA 7 HOH 124 824  1715 HOH HOH D . 
EA 7 HOH 125 825  1970 HOH HOH D . 
EA 7 HOH 126 826  713  HOH HOH D . 
EA 7 HOH 127 827  266  HOH HOH D . 
EA 7 HOH 128 828  323  HOH HOH D . 
EA 7 HOH 129 829  2161 HOH HOH D . 
EA 7 HOH 130 830  2132 HOH HOH D . 
EA 7 HOH 131 831  441  HOH HOH D . 
EA 7 HOH 132 832  1305 HOH HOH D . 
EA 7 HOH 133 833  1228 HOH HOH D . 
EA 7 HOH 134 834  2142 HOH HOH D . 
EA 7 HOH 135 835  1689 HOH HOH D . 
EA 7 HOH 136 836  988  HOH HOH D . 
EA 7 HOH 137 837  953  HOH HOH D . 
EA 7 HOH 138 838  129  HOH HOH D . 
EA 7 HOH 139 839  92   HOH HOH D . 
EA 7 HOH 140 840  1515 HOH HOH D . 
EA 7 HOH 141 841  966  HOH HOH D . 
EA 7 HOH 142 842  1814 HOH HOH D . 
EA 7 HOH 143 843  1729 HOH HOH D . 
EA 7 HOH 144 844  1389 HOH HOH D . 
EA 7 HOH 145 845  2172 HOH HOH D . 
EA 7 HOH 146 846  546  HOH HOH D . 
EA 7 HOH 147 847  207  HOH HOH D . 
EA 7 HOH 148 848  93   HOH HOH D . 
EA 7 HOH 149 849  738  HOH HOH D . 
EA 7 HOH 150 850  224  HOH HOH D . 
EA 7 HOH 151 851  44   HOH HOH D . 
EA 7 HOH 152 852  1188 HOH HOH D . 
EA 7 HOH 153 853  977  HOH HOH D . 
EA 7 HOH 154 854  1048 HOH HOH D . 
EA 7 HOH 155 855  503  HOH HOH D . 
EA 7 HOH 156 856  494  HOH HOH D . 
EA 7 HOH 157 857  128  HOH HOH D . 
EA 7 HOH 158 858  1599 HOH HOH D . 
EA 7 HOH 159 859  1686 HOH HOH D . 
EA 7 HOH 160 860  1314 HOH HOH D . 
EA 7 HOH 161 861  1917 HOH HOH D . 
EA 7 HOH 162 862  952  HOH HOH D . 
EA 7 HOH 163 863  1365 HOH HOH D . 
EA 7 HOH 164 864  1793 HOH HOH D . 
EA 7 HOH 165 865  1562 HOH HOH D . 
EA 7 HOH 166 866  1104 HOH HOH D . 
EA 7 HOH 167 867  116  HOH HOH D . 
EA 7 HOH 168 868  507  HOH HOH D . 
EA 7 HOH 169 869  393  HOH HOH D . 
EA 7 HOH 170 870  97   HOH HOH D . 
EA 7 HOH 171 871  1714 HOH HOH D . 
EA 7 HOH 172 872  47   HOH HOH D . 
EA 7 HOH 173 873  1610 HOH HOH D . 
EA 7 HOH 174 874  1203 HOH HOH D . 
EA 7 HOH 175 875  1865 HOH HOH D . 
EA 7 HOH 176 876  785  HOH HOH D . 
EA 7 HOH 177 877  1490 HOH HOH D . 
EA 7 HOH 178 878  561  HOH HOH D . 
EA 7 HOH 179 879  776  HOH HOH D . 
EA 7 HOH 180 880  27   HOH HOH D . 
EA 7 HOH 181 881  1649 HOH HOH D . 
EA 7 HOH 182 882  1184 HOH HOH D . 
EA 7 HOH 183 883  1433 HOH HOH D . 
EA 7 HOH 184 884  1082 HOH HOH D . 
EA 7 HOH 185 885  481  HOH HOH D . 
EA 7 HOH 186 886  2033 HOH HOH D . 
EA 7 HOH 187 887  1053 HOH HOH D . 
EA 7 HOH 188 888  581  HOH HOH D . 
EA 7 HOH 189 889  1006 HOH HOH D . 
EA 7 HOH 190 890  774  HOH HOH D . 
EA 7 HOH 191 891  1486 HOH HOH D . 
EA 7 HOH 192 892  1136 HOH HOH D . 
EA 7 HOH 193 893  719  HOH HOH D . 
EA 7 HOH 194 894  2143 HOH HOH D . 
EA 7 HOH 195 895  1042 HOH HOH D . 
EA 7 HOH 196 896  1568 HOH HOH D . 
EA 7 HOH 197 897  1207 HOH HOH D . 
EA 7 HOH 198 898  60   HOH HOH D . 
EA 7 HOH 199 899  680  HOH HOH D . 
EA 7 HOH 200 900  1311 HOH HOH D . 
EA 7 HOH 201 901  455  HOH HOH D . 
EA 7 HOH 202 902  1875 HOH HOH D . 
EA 7 HOH 203 903  25   HOH HOH D . 
EA 7 HOH 204 904  1510 HOH HOH D . 
EA 7 HOH 205 905  177  HOH HOH D . 
EA 7 HOH 206 906  810  HOH HOH D . 
EA 7 HOH 207 907  1819 HOH HOH D . 
EA 7 HOH 208 908  1801 HOH HOH D . 
EA 7 HOH 209 909  1063 HOH HOH D . 
EA 7 HOH 210 910  949  HOH HOH D . 
EA 7 HOH 211 911  1291 HOH HOH D . 
EA 7 HOH 212 912  163  HOH HOH D . 
EA 7 HOH 213 913  471  HOH HOH D . 
EA 7 HOH 214 914  211  HOH HOH D . 
EA 7 HOH 215 915  1650 HOH HOH D . 
EA 7 HOH 216 916  155  HOH HOH D . 
EA 7 HOH 217 917  251  HOH HOH D . 
EA 7 HOH 218 918  2193 HOH HOH D . 
EA 7 HOH 219 919  1460 HOH HOH D . 
EA 7 HOH 220 920  1555 HOH HOH D . 
EA 7 HOH 221 921  736  HOH HOH D . 
EA 7 HOH 222 922  1742 HOH HOH D . 
EA 7 HOH 223 923  717  HOH HOH D . 
EA 7 HOH 224 924  425  HOH HOH D . 
EA 7 HOH 225 925  1840 HOH HOH D . 
EA 7 HOH 226 926  2013 HOH HOH D . 
EA 7 HOH 227 927  151  HOH HOH D . 
EA 7 HOH 228 928  747  HOH HOH D . 
EA 7 HOH 229 929  947  HOH HOH D . 
EA 7 HOH 230 930  505  HOH HOH D . 
EA 7 HOH 231 931  2180 HOH HOH D . 
EA 7 HOH 232 932  975  HOH HOH D . 
EA 7 HOH 233 933  1034 HOH HOH D . 
EA 7 HOH 234 934  1146 HOH HOH D . 
EA 7 HOH 235 935  1825 HOH HOH D . 
EA 7 HOH 236 936  1427 HOH HOH D . 
EA 7 HOH 237 937  1743 HOH HOH D . 
EA 7 HOH 238 938  989  HOH HOH D . 
EA 7 HOH 239 939  492  HOH HOH D . 
EA 7 HOH 240 940  1977 HOH HOH D . 
EA 7 HOH 241 941  1167 HOH HOH D . 
EA 7 HOH 242 942  1475 HOH HOH D . 
EA 7 HOH 243 943  1457 HOH HOH D . 
EA 7 HOH 244 944  306  HOH HOH D . 
EA 7 HOH 245 945  1052 HOH HOH D . 
EA 7 HOH 246 946  201  HOH HOH D . 
EA 7 HOH 247 947  1499 HOH HOH D . 
EA 7 HOH 248 948  1019 HOH HOH D . 
EA 7 HOH 249 949  880  HOH HOH D . 
EA 7 HOH 250 950  2027 HOH HOH D . 
EA 7 HOH 251 951  1558 HOH HOH D . 
EA 7 HOH 252 952  1988 HOH HOH D . 
EA 7 HOH 253 953  651  HOH HOH D . 
EA 7 HOH 254 954  337  HOH HOH D . 
EA 7 HOH 255 955  376  HOH HOH D . 
EA 7 HOH 256 956  1980 HOH HOH D . 
EA 7 HOH 257 957  339  HOH HOH D . 
EA 7 HOH 258 958  1542 HOH HOH D . 
EA 7 HOH 259 959  1472 HOH HOH D . 
EA 7 HOH 260 960  161  HOH HOH D . 
EA 7 HOH 261 961  317  HOH HOH D . 
EA 7 HOH 262 962  869  HOH HOH D . 
EA 7 HOH 263 963  1105 HOH HOH D . 
EA 7 HOH 264 964  1638 HOH HOH D . 
EA 7 HOH 265 965  1658 HOH HOH D . 
EA 7 HOH 266 966  1038 HOH HOH D . 
EA 7 HOH 267 967  877  HOH HOH D . 
EA 7 HOH 268 968  227  HOH HOH D . 
EA 7 HOH 269 969  198  HOH HOH D . 
EA 7 HOH 270 970  1575 HOH HOH D . 
EA 7 HOH 271 971  839  HOH HOH D . 
EA 7 HOH 272 972  360  HOH HOH D . 
EA 7 HOH 273 973  1803 HOH HOH D . 
EA 7 HOH 274 974  1014 HOH HOH D . 
EA 7 HOH 275 975  2074 HOH HOH D . 
EA 7 HOH 276 976  308  HOH HOH D . 
EA 7 HOH 277 977  2112 HOH HOH D . 
EA 7 HOH 278 978  920  HOH HOH D . 
EA 7 HOH 279 979  833  HOH HOH D . 
EA 7 HOH 280 980  1078 HOH HOH D . 
EA 7 HOH 281 981  1420 HOH HOH D . 
EA 7 HOH 282 982  1254 HOH HOH D . 
EA 7 HOH 283 983  181  HOH HOH D . 
EA 7 HOH 284 984  2111 HOH HOH D . 
EA 7 HOH 285 985  535  HOH HOH D . 
EA 7 HOH 286 986  401  HOH HOH D . 
EA 7 HOH 287 987  767  HOH HOH D . 
EA 7 HOH 288 988  1484 HOH HOH D . 
EA 7 HOH 289 989  1592 HOH HOH D . 
EA 7 HOH 290 990  2109 HOH HOH D . 
EA 7 HOH 291 991  99   HOH HOH D . 
EA 7 HOH 292 992  788  HOH HOH D . 
EA 7 HOH 293 993  1601 HOH HOH D . 
EA 7 HOH 294 994  333  HOH HOH D . 
EA 7 HOH 295 995  1414 HOH HOH D . 
EA 7 HOH 296 996  1201 HOH HOH D . 
EA 7 HOH 297 997  398  HOH HOH D . 
EA 7 HOH 298 998  1362 HOH HOH D . 
EA 7 HOH 299 999  1731 HOH HOH D . 
EA 7 HOH 300 1000 710  HOH HOH D . 
EA 7 HOH 301 1001 2176 HOH HOH D . 
EA 7 HOH 302 1002 2036 HOH HOH D . 
EA 7 HOH 303 1003 981  HOH HOH D . 
EA 7 HOH 304 1004 1792 HOH HOH D . 
EA 7 HOH 305 1005 579  HOH HOH D . 
EA 7 HOH 306 1006 354  HOH HOH D . 
EA 7 HOH 307 1007 761  HOH HOH D . 
EA 7 HOH 308 1008 115  HOH HOH D . 
EA 7 HOH 309 1009 347  HOH HOH D . 
EA 7 HOH 310 1010 946  HOH HOH D . 
EA 7 HOH 311 1011 1669 HOH HOH D . 
EA 7 HOH 312 1012 1830 HOH HOH D . 
EA 7 HOH 313 1013 1779 HOH HOH D . 
EA 7 HOH 314 1014 1292 HOH HOH D . 
EA 7 HOH 315 1015 2107 HOH HOH D . 
EA 7 HOH 316 1016 143  HOH HOH D . 
EA 7 HOH 317 1017 289  HOH HOH D . 
EA 7 HOH 318 1018 685  HOH HOH D . 
EA 7 HOH 319 1019 1070 HOH HOH D . 
EA 7 HOH 320 1020 127  HOH HOH D . 
EA 7 HOH 321 1021 1776 HOH HOH D . 
EA 7 HOH 322 1022 1606 HOH HOH D . 
EA 7 HOH 323 1023 2101 HOH HOH D . 
EA 7 HOH 324 1024 68   HOH HOH D . 
EA 7 HOH 325 1025 2004 HOH HOH D . 
EA 7 HOH 326 1026 434  HOH HOH D . 
EA 7 HOH 327 1027 2010 HOH HOH D . 
EA 7 HOH 328 1028 1808 HOH HOH D . 
EA 7 HOH 329 1029 1022 HOH HOH D . 
EA 7 HOH 330 1030 665  HOH HOH D . 
EA 7 HOH 331 1031 336  HOH HOH D . 
EA 7 HOH 332 1032 1231 HOH HOH D . 
EA 7 HOH 333 1033 2067 HOH HOH D . 
EA 7 HOH 334 1034 1239 HOH HOH D . 
EA 7 HOH 335 1035 2108 HOH HOH D . 
EA 7 HOH 336 1036 1087 HOH HOH D . 
EA 7 HOH 337 1037 2044 HOH HOH D . 
EA 7 HOH 338 1038 1858 HOH HOH D . 
EA 7 HOH 339 1039 1071 HOH HOH D . 
EA 7 HOH 340 1040 2139 HOH HOH D . 
EA 7 HOH 341 1041 1200 HOH HOH D . 
EA 7 HOH 342 1042 1822 HOH HOH D . 
EA 7 HOH 343 1043 1887 HOH HOH D . 
EA 7 HOH 344 1044 560  HOH HOH D . 
EA 7 HOH 345 1045 1190 HOH HOH D . 
EA 7 HOH 346 1046 826  HOH HOH D . 
EA 7 HOH 347 1047 750  HOH HOH D . 
EA 7 HOH 348 1048 1138 HOH HOH D . 
EA 7 HOH 349 1049 967  HOH HOH D . 
EA 7 HOH 350 1050 527  HOH HOH D . 
EA 7 HOH 351 1051 1617 HOH HOH D . 
EA 7 HOH 352 1052 1975 HOH HOH D . 
EA 7 HOH 353 1053 1402 HOH HOH D . 
EA 7 HOH 354 1054 1133 HOH HOH D . 
EA 7 HOH 355 1055 1382 HOH HOH D . 
EA 7 HOH 356 1056 664  HOH HOH D . 
EA 7 HOH 357 1057 902  HOH HOH D . 
EA 7 HOH 358 1058 982  HOH HOH D . 
EA 7 HOH 359 1059 1274 HOH HOH D . 
EA 7 HOH 360 1060 855  HOH HOH D . 
EA 7 HOH 361 1061 2171 HOH HOH D . 
EA 7 HOH 362 1062 847  HOH HOH D . 
EA 7 HOH 363 1063 586  HOH HOH D . 
EA 7 HOH 364 1064 1081 HOH HOH D . 
EA 7 HOH 365 1065 918  HOH HOH D . 
EA 7 HOH 366 1066 663  HOH HOH D . 
EA 7 HOH 367 1067 1161 HOH HOH D . 
EA 7 HOH 368 1068 756  HOH HOH D . 
EA 7 HOH 369 1069 1768 HOH HOH D . 
EA 7 HOH 370 1070 1530 HOH HOH D . 
EA 7 HOH 371 1071 1675 HOH HOH D . 
EA 7 HOH 372 1072 778  HOH HOH D . 
EA 7 HOH 373 1073 453  HOH HOH D . 
EA 7 HOH 374 1074 1770 HOH HOH D . 
EA 7 HOH 375 1075 1248 HOH HOH D . 
EA 7 HOH 376 1076 498  HOH HOH D . 
EA 7 HOH 377 1077 668  HOH HOH D . 
EA 7 HOH 378 1078 639  HOH HOH D . 
EA 7 HOH 379 1079 1843 HOH HOH D . 
EA 7 HOH 380 1080 1698 HOH HOH D . 
EA 7 HOH 381 1081 790  HOH HOH D . 
EA 7 HOH 382 1082 896  HOH HOH D . 
EA 7 HOH 383 1083 1572 HOH HOH D . 
EA 7 HOH 384 1084 215  HOH HOH D . 
EA 7 HOH 385 1085 864  HOH HOH D . 
EA 7 HOH 386 1086 1777 HOH HOH D . 
EA 7 HOH 387 1087 1920 HOH HOH D . 
EA 7 HOH 388 1088 1694 HOH HOH D . 
EA 7 HOH 389 1089 863  HOH HOH D . 
EA 7 HOH 390 1090 614  HOH HOH D . 
EA 7 HOH 391 1091 2009 HOH HOH D . 
EA 7 HOH 392 1092 796  HOH HOH D . 
EA 7 HOH 393 1093 1151 HOH HOH D . 
EA 7 HOH 394 1094 2194 HOH HOH D . 
EA 7 HOH 395 1095 384  HOH HOH D . 
EA 7 HOH 396 1096 845  HOH HOH D . 
EA 7 HOH 397 1097 1158 HOH HOH D . 
EA 7 HOH 398 1098 1500 HOH HOH D . 
EA 7 HOH 399 1099 1398 HOH HOH D . 
EA 7 HOH 400 1100 627  HOH HOH D . 
EA 7 HOH 401 1101 782  HOH HOH D . 
EA 7 HOH 402 1102 672  HOH HOH D . 
EA 7 HOH 403 1103 1648 HOH HOH D . 
EA 7 HOH 404 1104 1493 HOH HOH D . 
EA 7 HOH 405 1105 1928 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 22  ? CG  ? A LYS 5   CG  
2   1 Y 1 A LYS 22  ? CD  ? A LYS 5   CD  
3   1 Y 1 A LYS 22  ? CE  ? A LYS 5   CE  
4   1 Y 1 A LYS 22  ? NZ  ? A LYS 5   NZ  
5   1 Y 1 A LYS 26  ? CG  ? A LYS 9   CG  
6   1 Y 1 A LYS 26  ? CD  ? A LYS 9   CD  
7   1 Y 1 A LYS 26  ? CE  ? A LYS 9   CE  
8   1 Y 1 A LYS 26  ? NZ  ? A LYS 9   NZ  
9   1 Y 1 A GLU 80  ? CG  ? A GLU 63  CG  
10  1 Y 1 A GLU 80  ? CD  ? A GLU 63  CD  
11  1 Y 1 A GLU 80  ? OE1 ? A GLU 63  OE1 
12  1 Y 1 A GLU 80  ? OE2 ? A GLU 63  OE2 
13  1 Y 1 A LYS 131 ? CG  ? A LYS 114 CG  
14  1 Y 1 A LYS 131 ? CD  ? A LYS 114 CD  
15  1 Y 1 A LYS 131 ? CE  ? A LYS 114 CE  
16  1 Y 1 A LYS 131 ? NZ  ? A LYS 114 NZ  
17  1 Y 1 A GLN 335 ? CG  ? A GLN 318 CG  
18  1 Y 1 A GLN 335 ? CD  ? A GLN 318 CD  
19  1 Y 1 A GLN 335 ? OE1 ? A GLN 318 OE1 
20  1 Y 1 A GLN 335 ? NE2 ? A GLN 318 NE2 
21  1 Y 1 A GLU 547 ? CG  ? A GLU 530 CG  
22  1 Y 1 A GLU 547 ? CD  ? A GLU 530 CD  
23  1 Y 1 A GLU 547 ? OE1 ? A GLU 530 OE1 
24  1 Y 1 A GLU 547 ? OE2 ? A GLU 530 OE2 
25  1 Y 1 A GLU 574 ? CG  ? A GLU 557 CG  
26  1 Y 1 A GLU 574 ? CD  ? A GLU 557 CD  
27  1 Y 1 A GLU 574 ? OE1 ? A GLU 557 OE1 
28  1 Y 1 A GLU 574 ? OE2 ? A GLU 557 OE2 
29  1 Y 1 B LYS 74  ? CG  ? B LYS 57  CG  
30  1 Y 1 B LYS 74  ? CD  ? B LYS 57  CD  
31  1 Y 1 B LYS 74  ? CE  ? B LYS 57  CE  
32  1 Y 1 B LYS 74  ? NZ  ? B LYS 57  NZ  
33  1 Y 1 B GLN 122 ? CG  ? B GLN 105 CG  
34  1 Y 1 B GLN 122 ? CD  ? B GLN 105 CD  
35  1 Y 1 B GLN 122 ? OE1 ? B GLN 105 OE1 
36  1 Y 1 B GLN 122 ? NE2 ? B GLN 105 NE2 
37  1 Y 1 B HIS 260 ? CG  ? B HIS 243 CG  
38  1 Y 1 B HIS 260 ? ND1 ? B HIS 243 ND1 
39  1 Y 1 B HIS 260 ? CD2 ? B HIS 243 CD2 
40  1 Y 1 B HIS 260 ? CE1 ? B HIS 243 CE1 
41  1 Y 1 B HIS 260 ? NE2 ? B HIS 243 NE2 
42  1 Y 1 B GLU 574 ? CG  ? B GLU 557 CG  
43  1 Y 1 B GLU 574 ? CD  ? B GLU 557 CD  
44  1 Y 1 B GLU 574 ? OE1 ? B GLU 557 OE1 
45  1 Y 1 B GLU 574 ? OE2 ? B GLU 557 OE2 
46  1 Y 1 C LYS 26  ? CG  ? C LYS 9   CG  
47  1 Y 1 C LYS 26  ? CD  ? C LYS 9   CD  
48  1 Y 1 C LYS 26  ? CE  ? C LYS 9   CE  
49  1 Y 1 C LYS 26  ? NZ  ? C LYS 9   NZ  
50  1 Y 1 C LYS 346 ? CG  ? C LYS 329 CG  
51  1 Y 1 C LYS 346 ? CD  ? C LYS 329 CD  
52  1 Y 1 C LYS 346 ? CE  ? C LYS 329 CE  
53  1 Y 1 C LYS 346 ? NZ  ? C LYS 329 NZ  
54  1 Y 1 C LYS 357 ? CG  ? C LYS 340 CG  
55  1 Y 1 C LYS 357 ? CD  ? C LYS 340 CD  
56  1 Y 1 C LYS 357 ? CE  ? C LYS 340 CE  
57  1 Y 1 C LYS 357 ? NZ  ? C LYS 340 NZ  
58  1 Y 1 C GLU 505 ? CG  ? C GLU 488 CG  
59  1 Y 1 C GLU 505 ? CD  ? C GLU 488 CD  
60  1 Y 1 C GLU 505 ? OE1 ? C GLU 488 OE1 
61  1 Y 1 C GLU 505 ? OE2 ? C GLU 488 OE2 
62  1 Y 1 D LYS 73  ? CG  ? D LYS 56  CG  
63  1 Y 1 D LYS 73  ? CD  ? D LYS 56  CD  
64  1 Y 1 D LYS 73  ? CE  ? D LYS 56  CE  
65  1 Y 1 D LYS 73  ? NZ  ? D LYS 56  NZ  
66  1 Y 1 D LYS 74  ? CG  ? D LYS 57  CG  
67  1 Y 1 D LYS 74  ? CD  ? D LYS 57  CD  
68  1 Y 1 D LYS 74  ? CE  ? D LYS 57  CE  
69  1 Y 1 D LYS 74  ? NZ  ? D LYS 57  NZ  
70  1 Y 1 D MET 75  ? CG  ? D MET 58  CG  
71  1 Y 1 D MET 75  ? SD  ? D MET 58  SD  
72  1 Y 1 D MET 75  ? CE  ? D MET 58  CE  
73  1 Y 1 D GLU 80  ? CG  ? D GLU 63  CG  
74  1 Y 1 D GLU 80  ? CD  ? D GLU 63  CD  
75  1 Y 1 D GLU 80  ? OE1 ? D GLU 63  OE1 
76  1 Y 1 D GLU 80  ? OE2 ? D GLU 63  OE2 
77  1 Y 1 D LYS 339 ? CG  ? D LYS 322 CG  
78  1 Y 1 D LYS 339 ? CD  ? D LYS 322 CD  
79  1 Y 1 D LYS 339 ? CE  ? D LYS 322 CE  
80  1 Y 1 D LYS 339 ? NZ  ? D LYS 322 NZ  
81  1 Y 1 D LYS 346 ? CG  ? D LYS 329 CG  
82  1 Y 1 D LYS 346 ? CD  ? D LYS 329 CD  
83  1 Y 1 D LYS 346 ? CE  ? D LYS 329 CE  
84  1 Y 1 D LYS 346 ? NZ  ? D LYS 329 NZ  
85  1 Y 1 D VAL 351 ? CG1 ? D VAL 334 CG1 
86  1 Y 1 D VAL 351 ? CG2 ? D VAL 334 CG2 
87  1 Y 1 D LYS 355 ? CG  ? D LYS 338 CG  
88  1 Y 1 D LYS 355 ? CD  ? D LYS 338 CD  
89  1 Y 1 D LYS 355 ? CE  ? D LYS 338 CE  
90  1 Y 1 D LYS 355 ? NZ  ? D LYS 338 NZ  
91  1 Y 1 D LYS 357 ? CG  ? D LYS 340 CG  
92  1 Y 1 D LYS 357 ? CD  ? D LYS 340 CD  
93  1 Y 1 D LYS 357 ? CE  ? D LYS 340 CE  
94  1 Y 1 D LYS 357 ? NZ  ? D LYS 340 NZ  
95  1 Y 1 D TYR 361 ? CG  ? D TYR 344 CG  
96  1 Y 1 D TYR 361 ? CD1 ? D TYR 344 CD1 
97  1 Y 1 D TYR 361 ? CD2 ? D TYR 344 CD2 
98  1 Y 1 D TYR 361 ? CE1 ? D TYR 344 CE1 
99  1 Y 1 D TYR 361 ? CE2 ? D TYR 344 CE2 
100 1 Y 1 D TYR 361 ? CZ  ? D TYR 344 CZ  
101 1 Y 1 D TYR 361 ? OH  ? D TYR 344 OH  
102 1 Y 1 D GLU 363 ? CG  ? D GLU 346 CG  
103 1 Y 1 D GLU 363 ? CD  ? D GLU 346 CD  
104 1 Y 1 D GLU 363 ? OE1 ? D GLU 346 OE1 
105 1 Y 1 D GLU 363 ? OE2 ? D GLU 346 OE2 
106 1 Y 1 D GLU 505 ? CG  ? D GLU 488 CG  
107 1 Y 1 D GLU 505 ? CD  ? D GLU 488 CD  
108 1 Y 1 D GLU 505 ? OE1 ? D GLU 488 OE1 
109 1 Y 1 D GLU 505 ? OE2 ? D GLU 488 OE2 
110 1 Y 1 D GLU 574 ? CG  ? D GLU 557 CG  
111 1 Y 1 D GLU 574 ? CD  ? D GLU 557 CD  
112 1 Y 1 D GLU 574 ? OE1 ? D GLU 557 OE1 
113 1 Y 1 D GLU 574 ? OE2 ? D GLU 557 OE2 
# 
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  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  65.32 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   70.75 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  74.89 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9AYI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.325 
_cell.length_a_esd                 ? 
_cell.length_b                     98.166 
_cell.length_b_esd                 ? 
_cell.length_c                     107.739 
_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                         9AYI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   9AYI 
_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             2.67 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.87 
_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              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Bis-Tris, 0.1 M Ammonium Tartrate, 0.02 M Potassium Citrate, 20% PEG-3350.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-07 
_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   0.9537 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9537 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9AYI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.89 
_reflns.d_resolution_low                               47.42 
_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                                     200119 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.990 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.89 
_reflns_shell.d_res_low                                     1.93 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8176 
_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                               3.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.483 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          79.9 
_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               ? 
# 
_refine.aniso_B[1][1]                            0.76 
_refine.aniso_B[1][2]                            1.56 
_refine.aniso_B[1][3]                            -1.51 
_refine.aniso_B[2][2]                            -0.49 
_refine.aniso_B[2][3]                            -0.36 
_refine.aniso_B[3][3]                            -0.27 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.068 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9AYI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.89 
_refine.ls_d_res_low                             47.42 
_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                     189840 
_refine.ls_number_reflns_R_free                  10256 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.12 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17836 
_refine.ls_R_factor_R_free                       0.20096 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17712 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.148 
_refine.pdbx_overall_ESU_R_Free                  0.127 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.540 
_refine.overall_SU_ML                            0.100 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.89 
_refine_hist.d_res_low                        47.42 
_refine_hist.number_atoms_solvent             1960 
_refine_hist.number_atoms_total               19712 
_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        17334 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         418 
_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' ? 0.003  0.012  18553 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  17534 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.094  1.832  25229 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.404  1.754  40423 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.792  5.000  2270  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 4.562  5.000  137   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.727 10.000 3104  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.056  0.200  2816  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  21632 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  4221  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.391  3.050  8993  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.391  3.050  8993  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.294  5.478  11265 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.294  5.479  11266 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.791  3.311  9560  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.791  3.311  9561  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.036  6.004  13956 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.170  30.98  21340 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.982  29.58  20841 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.893 
_refine_ls_shell.d_res_low                        1.942 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             713 
_refine_ls_shell.number_reflns_R_work             12285 
_refine_ls_shell.percent_reflns_obs               85.34 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.286 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.279 
# 
_struct.entry_id                     9AYI 
_struct.title                        'Human malic enzyme 2 cofactor complex at 1.89 Angstrom.' 
_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        9AYI 
_struct_keywords.text            
'Malic enzyme 2, NAD+, co-factor complex, ME2, mitochondrial localisation, m-NAD-ME, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 4 ? 
I  N N 2 ? 
J  N N 5 ? 
K  N N 6 ? 
L  N N 4 ? 
M  N N 2 ? 
N  N N 6 ? 
O  N N 3 ? 
P  N N 2 ? 
Q  N N 5 ? 
R  N N 6 ? 
S  N N 3 ? 
T  N N 4 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 6 ? 
X  N N 4 ? 
Y  N N 2 ? 
Z  N N 3 ? 
AA N N 2 ? 
BA N N 7 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MAOM_HUMAN 
_struct_ref.pdbx_db_accession          P23368 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYR
ILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMG
IPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFG
NHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQ
KKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFA
LSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKAL
TSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASS
PPVITE
;
_struct_ref.pdbx_align_begin           19 
# 
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 9AYI A 2 ? 567 ? P23368 19 ? 584 ? 19 584 
2 1 9AYI B 2 ? 567 ? P23368 19 ? 584 ? 19 584 
3 1 9AYI C 2 ? 567 ? P23368 19 ? 584 ? 19 584 
4 1 9AYI D 2 ? 567 ? P23368 19 ? 584 ? 19 584 
# 
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 9AYI MET A 1   ? UNP P23368 ? ? 'initiating methionine' 18  1  
1 9AYI LEU A 568 ? UNP P23368 ? ? 'expression tag'        585 2  
1 9AYI GLU A 569 ? UNP P23368 ? ? 'expression tag'        586 3  
1 9AYI HIS A 570 ? UNP P23368 ? ? 'expression tag'        587 4  
1 9AYI HIS A 571 ? UNP P23368 ? ? 'expression tag'        588 5  
1 9AYI HIS A 572 ? UNP P23368 ? ? 'expression tag'        589 6  
1 9AYI HIS A 573 ? UNP P23368 ? ? 'expression tag'        590 7  
1 9AYI HIS A 574 ? UNP P23368 ? ? 'expression tag'        591 8  
1 9AYI HIS A 575 ? UNP P23368 ? ? 'expression tag'        592 9  
2 9AYI MET B 1   ? UNP P23368 ? ? 'initiating methionine' 18  10 
2 9AYI LEU B 568 ? UNP P23368 ? ? 'expression tag'        585 11 
2 9AYI GLU B 569 ? UNP P23368 ? ? 'expression tag'        586 12 
2 9AYI HIS B 570 ? UNP P23368 ? ? 'expression tag'        587 13 
2 9AYI HIS B 571 ? UNP P23368 ? ? 'expression tag'        588 14 
2 9AYI HIS B 572 ? UNP P23368 ? ? 'expression tag'        589 15 
2 9AYI HIS B 573 ? UNP P23368 ? ? 'expression tag'        590 16 
2 9AYI HIS B 574 ? UNP P23368 ? ? 'expression tag'        591 17 
2 9AYI HIS B 575 ? UNP P23368 ? ? 'expression tag'        592 18 
3 9AYI MET C 1   ? UNP P23368 ? ? 'initiating methionine' 18  19 
3 9AYI LEU C 568 ? UNP P23368 ? ? 'expression tag'        585 20 
3 9AYI GLU C 569 ? UNP P23368 ? ? 'expression tag'        586 21 
3 9AYI HIS C 570 ? UNP P23368 ? ? 'expression tag'        587 22 
3 9AYI HIS C 571 ? UNP P23368 ? ? 'expression tag'        588 23 
3 9AYI HIS C 572 ? UNP P23368 ? ? 'expression tag'        589 24 
3 9AYI HIS C 573 ? UNP P23368 ? ? 'expression tag'        590 25 
3 9AYI HIS C 574 ? UNP P23368 ? ? 'expression tag'        591 26 
3 9AYI HIS C 575 ? UNP P23368 ? ? 'expression tag'        592 27 
4 9AYI MET D 1   ? UNP P23368 ? ? 'initiating methionine' 18  28 
4 9AYI LEU D 568 ? UNP P23368 ? ? 'expression tag'        585 29 
4 9AYI GLU D 569 ? UNP P23368 ? ? 'expression tag'        586 30 
4 9AYI HIS D 570 ? UNP P23368 ? ? 'expression tag'        587 31 
4 9AYI HIS D 571 ? UNP P23368 ? ? 'expression tag'        588 32 
4 9AYI HIS D 572 ? UNP P23368 ? ? 'expression tag'        589 33 
4 9AYI HIS D 573 ? UNP P23368 ? ? 'expression tag'        590 34 
4 9AYI HIS D 574 ? UNP P23368 ? ? 'expression tag'        591 35 
4 9AYI HIS D 575 ? UNP P23368 ? ? 'expression tag'        592 36 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 29340 ? 
1 MORE         -160  ? 
1 'SSA (A^2)'  78460 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA 
# 
_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 LYS A 9   ? ASN A 14  ? LYS A 26  ASN A 31  1 ? 6  
HELX_P HELX_P2   AA2 LYS A 19  ? PHE A 23  ? LYS A 36  PHE A 40  5 ? 5  
HELX_P HELX_P3   AA3 THR A 24  ? LEU A 31  ? THR A 41  LEU A 48  1 ? 8  
HELX_P HELX_P4   AA4 THR A 43  ? LYS A 56  ? THR A 60  LYS A 73  1 ? 14 
HELX_P HELX_P5   AA5 SER A 60  ? GLU A 73  ? SER A 77  GLU A 90  1 ? 14 
HELX_P HELX_P6   AA6 ASN A 75  ? ASP A 86  ? ASN A 92  ASP A 103 1 ? 12 
HELX_P HELX_P7   AA7 ASP A 86  ? TYR A 95  ? ASP A 103 TYR A 112 1 ? 10 
HELX_P HELX_P8   AA8 GLY A 100 ? GLY A 107 ? GLY A 117 GLY A 124 1 ? 8  
HELX_P HELX_P9   AA9 SER A 121 ? ARG A 123 ? SER A 138 ARG A 140 5 ? 3  
HELX_P HELX_P10  AB1 HIS A 125 ? ASN A 132 ? HIS A 142 ASN A 149 1 ? 8  
HELX_P HELX_P11  AB2 LEU A 155 ? GLY A 159 ? LEU A 172 GLY A 176 5 ? 5  
HELX_P HELX_P12  AB3 MET A 160 ? GLY A 175 ? MET A 177 GLY A 192 1 ? 16 
HELX_P HELX_P13  AB4 ARG A 177 ? ASP A 179 ? ARG A 194 ASP A 196 5 ? 3  
HELX_P HELX_P14  AB5 ASN A 192 ? LYS A 197 ? ASN A 209 LYS A 214 1 ? 6  
HELX_P HELX_P15  AB6 THR A 211 ? GLY A 230 ? THR A 228 GLY A 247 1 ? 20 
HELX_P HELX_P16  AB7 GLY A 241 ? ARG A 253 ? GLY A 258 ARG A 270 1 ? 13 
HELX_P HELX_P17  AB8 ASP A 261 ? ILE A 281 ? ASP A 278 ILE A 298 1 ? 21 
HELX_P HELX_P18  AB9 PRO A 284 ? HIS A 288 ? PRO A 301 HIS A 305 5 ? 5  
HELX_P HELX_P19  AC1 GLY A 296 ? ASN A 313 ? GLY A 313 ASN A 330 1 ? 18 
HELX_P HELX_P20  AC2 SER A 316 ? LYS A 322 ? SER A 333 LYS A 339 1 ? 7  
HELX_P HELX_P21  AC3 GLN A 345 ? THR A 349 ? GLN A 362 THR A 366 5 ? 5  
HELX_P HELX_P22  AC4 THR A 359 ? LYS A 368 ? THR A 376 LYS A 385 1 ? 10 
HELX_P HELX_P23  AC5 THR A 383 ? ASN A 394 ? THR A 400 ASN A 411 1 ? 12 
HELX_P HELX_P24  AC6 PRO A 405 ? ALA A 409 ? PRO A 422 ALA A 426 5 ? 5  
HELX_P HELX_P25  AC7 THR A 412 ? THR A 420 ? THR A 429 THR A 437 1 ? 9  
HELX_P HELX_P26  AC8 ASN A 449 ? TYR A 452 ? ASN A 466 TYR A 469 5 ? 4  
HELX_P HELX_P27  AC9 ILE A 453 ? CYS A 464 ? ILE A 470 CYS A 481 1 ? 12 
HELX_P HELX_P28  AD1 SER A 470 ? SER A 483 ? SER A 487 SER A 500 1 ? 14 
HELX_P HELX_P29  AD2 THR A 486 ? GLN A 492 ? THR A 503 GLN A 509 1 ? 7  
HELX_P HELX_P30  AD3 PRO A 498 ? ALA A 500 ? PRO A 515 ALA A 517 5 ? 3  
HELX_P HELX_P31  AD4 ASN A 501 ? ASN A 520 ? ASN A 518 ASN A 537 1 ? 20 
HELX_P HELX_P32  AD5 ASP A 531 ? GLU A 538 ? ASP A 548 GLU A 555 1 ? 8  
HELX_P HELX_P33  AD6 LYS B 9   ? ASN B 14  ? LYS B 26  ASN B 31  1 ? 6  
HELX_P HELX_P34  AD7 LYS B 19  ? PHE B 23  ? LYS B 36  PHE B 40  5 ? 5  
HELX_P HELX_P35  AD8 THR B 24  ? LEU B 31  ? THR B 41  LEU B 48  1 ? 8  
HELX_P HELX_P36  AD9 THR B 43  ? MET B 58  ? THR B 60  MET B 75  1 ? 16 
HELX_P HELX_P37  AE1 SER B 60  ? GLU B 73  ? SER B 77  GLU B 90  1 ? 14 
HELX_P HELX_P38  AE2 ASN B 75  ? ASP B 86  ? ASN B 92  ASP B 103 1 ? 12 
HELX_P HELX_P39  AE3 ASP B 86  ? TYR B 95  ? ASP B 103 TYR B 112 1 ? 10 
HELX_P HELX_P40  AE4 GLY B 100 ? GLY B 107 ? GLY B 117 GLY B 124 1 ? 8  
HELX_P HELX_P41  AE5 SER B 121 ? ARG B 123 ? SER B 138 ARG B 140 5 ? 3  
HELX_P HELX_P42  AE6 HIS B 125 ? ASP B 131 ? HIS B 142 ASP B 148 1 ? 7  
HELX_P HELX_P43  AE7 LEU B 155 ? GLY B 159 ? LEU B 172 GLY B 176 5 ? 5  
HELX_P HELX_P44  AE8 MET B 160 ? GLY B 175 ? MET B 177 GLY B 192 1 ? 16 
HELX_P HELX_P45  AE9 ARG B 177 ? ASP B 179 ? ARG B 194 ASP B 196 5 ? 3  
HELX_P HELX_P46  AF1 ASN B 192 ? LYS B 197 ? ASN B 209 LYS B 214 1 ? 6  
HELX_P HELX_P47  AF2 THR B 211 ? GLY B 230 ? THR B 228 GLY B 247 1 ? 20 
HELX_P HELX_P48  AF3 GLY B 241 ? ARG B 253 ? GLY B 258 ARG B 270 1 ? 13 
HELX_P HELX_P49  AF4 ASP B 261 ? SER B 282 ? ASP B 278 SER B 299 1 ? 22 
HELX_P HELX_P50  AF5 PRO B 284 ? HIS B 288 ? PRO B 301 HIS B 305 5 ? 5  
HELX_P HELX_P51  AF6 GLY B 296 ? ASN B 313 ? GLY B 313 ASN B 330 1 ? 18 
HELX_P HELX_P52  AF7 SER B 316 ? LYS B 322 ? SER B 333 LYS B 339 1 ? 7  
HELX_P HELX_P53  AF8 GLN B 345 ? THR B 349 ? GLN B 362 THR B 366 5 ? 5  
HELX_P HELX_P54  AF9 THR B 359 ? LYS B 368 ? THR B 376 LYS B 385 1 ? 10 
HELX_P HELX_P55  AG1 THR B 383 ? ASN B 394 ? THR B 400 ASN B 411 1 ? 12 
HELX_P HELX_P56  AG2 PRO B 405 ? ALA B 409 ? PRO B 422 ALA B 426 5 ? 5  
HELX_P HELX_P57  AG3 THR B 412 ? THR B 420 ? THR B 429 THR B 437 1 ? 9  
HELX_P HELX_P58  AG4 ASN B 449 ? TYR B 452 ? ASN B 466 TYR B 469 5 ? 4  
HELX_P HELX_P59  AG5 ILE B 453 ? CYS B 464 ? ILE B 470 CYS B 481 1 ? 12 
HELX_P HELX_P60  AG6 SER B 470 ? SER B 483 ? SER B 487 SER B 500 1 ? 14 
HELX_P HELX_P61  AG7 THR B 486 ? GLN B 492 ? THR B 503 GLN B 509 1 ? 7  
HELX_P HELX_P62  AG8 PRO B 498 ? ALA B 500 ? PRO B 515 ALA B 517 5 ? 3  
HELX_P HELX_P63  AG9 ASN B 501 ? ASN B 520 ? ASN B 518 ASN B 537 1 ? 20 
HELX_P HELX_P64  AH1 ASP B 531 ? GLU B 538 ? ASP B 548 GLU B 555 1 ? 8  
HELX_P HELX_P65  AH2 LYS C 9   ? ASN C 14  ? LYS C 26  ASN C 31  1 ? 6  
HELX_P HELX_P66  AH3 LYS C 19  ? PHE C 23  ? LYS C 36  PHE C 40  5 ? 5  
HELX_P HELX_P67  AH4 THR C 24  ? LEU C 31  ? THR C 41  LEU C 48  1 ? 8  
HELX_P HELX_P68  AH5 THR C 43  ? LYS C 56  ? THR C 60  LYS C 73  1 ? 14 
HELX_P HELX_P69  AH6 SER C 60  ? GLU C 73  ? SER C 77  GLU C 90  1 ? 14 
HELX_P HELX_P70  AH7 ASN C 75  ? ASP C 86  ? ASN C 92  ASP C 103 1 ? 12 
HELX_P HELX_P71  AH8 ASP C 86  ? TYR C 95  ? ASP C 103 TYR C 112 1 ? 10 
HELX_P HELX_P72  AH9 THR C 98  ? GLY C 107 ? THR C 115 GLY C 124 1 ? 10 
HELX_P HELX_P73  AI1 SER C 121 ? ARG C 123 ? SER C 138 ARG C 140 5 ? 3  
HELX_P HELX_P74  AI2 HIS C 125 ? ASP C 131 ? HIS C 142 ASP C 148 1 ? 7  
HELX_P HELX_P75  AI3 LEU C 155 ? GLY C 159 ? LEU C 172 GLY C 176 5 ? 5  
HELX_P HELX_P76  AI4 MET C 160 ? GLY C 175 ? MET C 177 GLY C 192 1 ? 16 
HELX_P HELX_P77  AI5 ARG C 177 ? ASP C 179 ? ARG C 194 ASP C 196 5 ? 3  
HELX_P HELX_P78  AI6 ASN C 192 ? LYS C 197 ? ASN C 209 LYS C 214 1 ? 6  
HELX_P HELX_P79  AI7 THR C 211 ? GLY C 230 ? THR C 228 GLY C 247 1 ? 20 
HELX_P HELX_P80  AI8 GLY C 241 ? ARG C 253 ? GLY C 258 ARG C 270 1 ? 13 
HELX_P HELX_P81  AI9 ILE C 263 ? LYS C 279 ? ILE C 280 LYS C 296 1 ? 17 
HELX_P HELX_P82  AJ1 PRO C 284 ? HIS C 288 ? PRO C 301 HIS C 305 5 ? 5  
HELX_P HELX_P83  AJ2 GLY C 296 ? ASN C 313 ? GLY C 313 ASN C 330 1 ? 18 
HELX_P HELX_P84  AJ3 SER C 316 ? LYS C 322 ? SER C 333 LYS C 339 1 ? 7  
HELX_P HELX_P85  AJ4 GLN C 345 ? THR C 349 ? GLN C 362 THR C 366 5 ? 5  
HELX_P HELX_P86  AJ5 THR C 359 ? LYS C 368 ? THR C 376 LYS C 385 1 ? 10 
HELX_P HELX_P87  AJ6 THR C 383 ? ASN C 394 ? THR C 400 ASN C 411 1 ? 12 
HELX_P HELX_P88  AJ7 PRO C 405 ? ALA C 409 ? PRO C 422 ALA C 426 5 ? 5  
HELX_P HELX_P89  AJ8 THR C 412 ? THR C 420 ? THR C 429 THR C 437 1 ? 9  
HELX_P HELX_P90  AJ9 ASN C 449 ? TYR C 452 ? ASN C 466 TYR C 469 5 ? 4  
HELX_P HELX_P91  AK1 ILE C 453 ? CYS C 464 ? ILE C 470 CYS C 481 1 ? 12 
HELX_P HELX_P92  AK2 SER C 470 ? SER C 483 ? SER C 487 SER C 500 1 ? 14 
HELX_P HELX_P93  AK3 THR C 486 ? GLY C 493 ? THR C 503 GLY C 510 1 ? 8  
HELX_P HELX_P94  AK4 PRO C 498 ? ALA C 500 ? PRO C 515 ALA C 517 5 ? 3  
HELX_P HELX_P95  AK5 ASN C 501 ? ASN C 520 ? ASN C 518 ASN C 537 1 ? 20 
HELX_P HELX_P96  AK6 ASP C 531 ? THR C 540 ? ASP C 548 THR C 557 1 ? 10 
HELX_P HELX_P97  AK7 LYS D 9   ? ASN D 14  ? LYS D 26  ASN D 31  1 ? 6  
HELX_P HELX_P98  AK8 LYS D 19  ? PHE D 23  ? LYS D 36  PHE D 40  5 ? 5  
HELX_P HELX_P99  AK9 THR D 24  ? LEU D 31  ? THR D 41  LEU D 48  1 ? 8  
HELX_P HELX_P100 AL1 THR D 43  ? LYS D 57  ? THR D 60  LYS D 74  1 ? 15 
HELX_P HELX_P101 AL2 SER D 60  ? GLU D 73  ? SER D 77  GLU D 90  1 ? 14 
HELX_P HELX_P102 AL3 ASN D 75  ? ASP D 86  ? ASN D 92  ASP D 103 1 ? 12 
HELX_P HELX_P103 AL4 ASP D 86  ? TYR D 95  ? ASP D 103 TYR D 112 1 ? 10 
HELX_P HELX_P104 AL5 THR D 98  ? GLY D 107 ? THR D 115 GLY D 124 1 ? 10 
HELX_P HELX_P105 AL6 SER D 121 ? ARG D 123 ? SER D 138 ARG D 140 5 ? 3  
HELX_P HELX_P106 AL7 HIS D 125 ? ASP D 131 ? HIS D 142 ASP D 148 1 ? 7  
HELX_P HELX_P107 AL8 LEU D 155 ? GLY D 159 ? LEU D 172 GLY D 176 5 ? 5  
HELX_P HELX_P108 AL9 MET D 160 ? GLY D 175 ? MET D 177 GLY D 192 1 ? 16 
HELX_P HELX_P109 AM1 ARG D 177 ? ASP D 179 ? ARG D 194 ASP D 196 5 ? 3  
HELX_P HELX_P110 AM2 ASN D 192 ? LYS D 197 ? ASN D 209 LYS D 214 1 ? 6  
HELX_P HELX_P111 AM3 THR D 211 ? GLY D 230 ? THR D 228 GLY D 247 1 ? 20 
HELX_P HELX_P112 AM4 GLY D 241 ? ARG D 253 ? GLY D 258 ARG D 270 1 ? 13 
HELX_P HELX_P113 AM5 ASP D 261 ? SER D 282 ? ASP D 278 SER D 299 1 ? 22 
HELX_P HELX_P114 AM6 PRO D 284 ? HIS D 288 ? PRO D 301 HIS D 305 5 ? 5  
HELX_P HELX_P115 AM7 GLY D 296 ? ASN D 313 ? GLY D 313 ASN D 330 1 ? 18 
HELX_P HELX_P116 AM8 SER D 316 ? LYS D 322 ? SER D 333 LYS D 339 1 ? 7  
HELX_P HELX_P117 AM9 GLN D 345 ? THR D 349 ? GLN D 362 THR D 366 5 ? 5  
HELX_P HELX_P118 AN1 THR D 359 ? LYS D 368 ? THR D 376 LYS D 385 1 ? 10 
HELX_P HELX_P119 AN2 THR D 383 ? ASN D 394 ? THR D 400 ASN D 411 1 ? 12 
HELX_P HELX_P120 AN3 PRO D 405 ? ALA D 409 ? PRO D 422 ALA D 426 5 ? 5  
HELX_P HELX_P121 AN4 THR D 412 ? THR D 420 ? THR D 429 THR D 437 1 ? 9  
HELX_P HELX_P122 AN5 ASN D 449 ? TYR D 452 ? ASN D 466 TYR D 469 5 ? 4  
HELX_P HELX_P123 AN6 ILE D 453 ? CYS D 464 ? ILE D 470 CYS D 481 1 ? 12 
HELX_P HELX_P124 AN7 SER D 470 ? SER D 483 ? SER D 487 SER D 500 1 ? 14 
HELX_P HELX_P125 AN8 THR D 486 ? GLN D 492 ? THR D 503 GLN D 509 1 ? 7  
HELX_P HELX_P126 AN9 PRO D 498 ? ALA D 500 ? PRO D 515 ALA D 517 5 ? 3  
HELX_P HELX_P127 AO1 ASN D 501 ? ASN D 520 ? ASN D 518 ASN D 537 1 ? 20 
HELX_P HELX_P128 AO2 ASP D 531 ? GLU D 538 ? ASP D 548 GLU D 555 1 ? 8  
# 
_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 
covale1  covale both ? A ALA 102 C  ? ? ? 1_555 A  CSX 103 N ? ? A ALA 119 A CSX 120  1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale2  covale both ? A CSX 103 C  ? ? ? 1_555 A  SER 104 N A ? A CSX 120 A SER 121  1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale3  covale both ? A CSX 103 C  ? ? ? 1_555 A  SER 104 N B ? A CSX 120 A SER 121  1_555 ? ? ? ? ? ? ? 1.337 ? ? 
covale4  covale both ? B ALA 102 C  ? ? ? 1_555 B  CSX 103 N ? ? B ALA 119 B CSX 120  1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale5  covale both ? B CSX 103 C  ? ? ? 1_555 B  SER 104 N ? ? B CSX 120 B SER 121  1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale6  covale both ? C ALA 102 C  ? ? ? 1_555 C  CSX 103 N ? ? C ALA 119 C CSX 120  1_555 ? ? ? ? ? ? ? 1.342 ? ? 
covale7  covale both ? C CSX 103 C  ? ? ? 1_555 C  SER 104 N A ? C CSX 120 C SER 121  1_555 ? ? ? ? ? ? ? 1.338 ? ? 
covale8  covale both ? C CSX 103 C  ? ? ? 1_555 C  SER 104 N B ? C CSX 120 C SER 121  1_555 ? ? ? ? ? ? ? 1.339 ? ? 
covale9  covale both ? D ALA 102 C  ? ? ? 1_555 D  CSX 103 N ? ? D ALA 119 D CSX 120  1_555 ? ? ? ? ? ? ? 1.341 ? ? 
covale10 covale both ? D CSX 103 C  ? ? ? 1_555 D  SER 104 N ? ? D CSX 120 D SER 121  1_555 ? ? ? ? ? ? ? 1.339 ? ? 
metalc1  metalc ?    ? J MG  .   MG ? ? ? 1_555 BA HOH .   O ? ? A MG  606 A HOH 1071 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc2  metalc ?    ? J MG  .   MG ? ? ? 1_555 BA HOH .   O ? ? A MG  606 A HOH 1087 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc3  metalc ?    ? J MG  .   MG ? ? ? 1_555 EA HOH .   O ? ? A MG  606 D HOH 918  1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc4  metalc ?    ? J MG  .   MG ? ? ? 1_555 EA HOH .   O ? ? A MG  606 D HOH 1012 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc5  metalc ?    ? Q MG  .   MG ? ? ? 1_555 CA HOH .   O ? ? B MG  606 B HOH 1017 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc6  metalc ?    ? Q MG  .   MG ? ? ? 1_555 CA HOH .   O ? ? B MG  606 B HOH 1103 1_555 ? ? ? ? ? ? ? 1.983 ? ? 
metalc7  metalc ?    ? Q MG  .   MG ? ? ? 1_555 CA HOH .   O ? ? B MG  606 B HOH 1144 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc8  metalc ?    ? Q MG  .   MG ? ? ? 1_555 DA HOH .   O ? ? B MG  606 C HOH 1121 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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  O ? BA HOH . ? A HOH 1071 ? 1_555 MG ? J MG . ? A MG 606 ? 1_555 O ? BA HOH . ? A HOH 1087 ? 1_555 66.8  ? 
2  O ? BA HOH . ? A HOH 1071 ? 1_555 MG ? J MG . ? A MG 606 ? 1_555 O ? EA HOH . ? D HOH 918  ? 1_555 72.8  ? 
3  O ? BA HOH . ? A HOH 1087 ? 1_555 MG ? J MG . ? A MG 606 ? 1_555 O ? EA HOH . ? D HOH 918  ? 1_555 66.1  ? 
4  O ? BA HOH . ? A HOH 1071 ? 1_555 MG ? J MG . ? A MG 606 ? 1_555 O ? EA HOH . ? D HOH 1012 ? 1_555 147.3 ? 
5  O ? BA HOH . ? A HOH 1087 ? 1_555 MG ? J MG . ? A MG 606 ? 1_555 O ? EA HOH . ? D HOH 1012 ? 1_555 87.6  ? 
6  O ? EA HOH . ? D HOH 918  ? 1_555 MG ? J MG . ? A MG 606 ? 1_555 O ? EA HOH . ? D HOH 1012 ? 1_555 78.5  ? 
7  O ? CA HOH . ? B HOH 1017 ? 1_555 MG ? Q MG . ? B MG 606 ? 1_555 O ? CA HOH . ? B HOH 1103 ? 1_555 153.5 ? 
8  O ? CA HOH . ? B HOH 1017 ? 1_555 MG ? Q MG . ? B MG 606 ? 1_555 O ? CA HOH . ? B HOH 1144 ? 1_555 92.1  ? 
9  O ? CA HOH . ? B HOH 1103 ? 1_555 MG ? Q MG . ? B MG 606 ? 1_555 O ? CA HOH . ? B HOH 1144 ? 1_555 63.2  ? 
10 O ? CA HOH . ? B HOH 1017 ? 1_555 MG ? Q MG . ? B MG 606 ? 1_555 O ? DA HOH . ? C HOH 1121 ? 1_555 74.5  ? 
11 O ? CA HOH . ? B HOH 1103 ? 1_555 MG ? Q MG . ? B MG 606 ? 1_555 O ? DA HOH . ? C HOH 1121 ? 1_555 85.5  ? 
12 O ? CA HOH . ? B HOH 1144 ? 1_555 MG ? Q MG . ? B MG 606 ? 1_555 O ? DA HOH . ? C HOH 1121 ? 1_555 64.0  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CSX A 103 ? . . . . CSX A 120 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
2 CSX B 103 ? . . . . CSX B 120 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
3 CSX C 103 ? . . . . CSX C 120 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
4 CSX D 103 ? . . . . CSX D 120 ? 1_555 . . . . . . . CYS 1 CSX Oxidation 'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  THR 96  A . ? THR 113 A PRO 97  A ? PRO 114 A 1 1.19   
2  THR 96  A . ? THR 113 A PRO 97  A ? PRO 114 A 1 2.46   
3  ASN 404 A . ? ASN 421 A PRO 405 A ? PRO 422 A 1 -10.26 
4  TYR 526 A . ? TYR 543 A PRO 527 A ? PRO 544 A 1 3.17   
5  THR 96  B . ? THR 113 B PRO 97  B ? PRO 114 B 1 -2.83  
6  THR 96  B . ? THR 113 B PRO 97  B ? PRO 114 B 1 1.26   
7  ASN 404 B . ? ASN 421 B PRO 405 B ? PRO 422 B 1 -5.99  
8  TYR 526 B . ? TYR 543 B PRO 527 B ? PRO 544 B 1 2.55   
9  THR 96  C . ? THR 113 C PRO 97  C ? PRO 114 C 1 1.96   
10 ASN 404 C . ? ASN 421 C PRO 405 C ? PRO 422 C 1 -4.28  
11 TYR 526 C . ? TYR 543 C PRO 527 C ? PRO 544 C 1 3.17   
12 THR 96  D . ? THR 113 D PRO 97  D ? PRO 114 D 1 1.45   
13 ASN 404 D . ? ASN 421 D PRO 405 D ? PRO 422 D 1 -5.22  
14 TYR 526 D . ? TYR 543 D PRO 527 D ? PRO 544 D 1 2.27   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 7 ? 
AA6 ? 2 ? 
AA7 ? 5 ? 
AA8 ? 7 ? 
AA9 ? 2 ? 
AB1 ? 5 ? 
AB2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? parallel      
AA8 6 7 ? parallel      
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB2 1 2 ? anti-parallel 
AB2 2 3 ? parallel      
AB2 3 4 ? parallel      
AB2 4 5 ? parallel      
AB2 5 6 ? parallel      
AB2 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 116 ? SER A 119 ? LEU A 133 SER A 136 
AA1 2 CYS A 181 ? ASP A 187 ? CYS A 198 ASP A 204 
AA1 3 ALA A 140 ? THR A 144 ? ALA A 157 THR A 161 
AA1 4 LEU A 234 ? PHE A 237 ? LEU A 251 PHE A 254 
AA1 5 CYS A 257 ? ASN A 260 ? CYS A 274 ASN A 277 
AA2 1 GLY A 331 ? LEU A 332 ? GLY A 348 LEU A 349 
AA2 2 ILE A 324 ? ASP A 328 ? ILE A 341 ASP A 345 
AA2 3 ILE A 290 ? LEU A 293 ? ILE A 307 LEU A 310 
AA2 4 THR A 371 ? GLY A 374 ? THR A 388 GLY A 391 
AA2 5 VAL A 398 ? ALA A 401 ? VAL A 415 ALA A 418 
AA2 6 LEU A 425 ? SER A 428 ? LEU A 442 SER A 445 
AA2 7 GLY A 446 ? GLN A 447 ? GLY A 463 GLN A 464 
AA3 1 VAL A 435 ? LYS A 436 ? VAL A 452 LYS A 453 
AA3 2 VAL A 442 ? PHE A 443 ? VAL A 459 PHE A 460 
AA4 1 LEU B 116 ? SER B 119 ? LEU B 133 SER B 136 
AA4 2 CYS B 181 ? ASP B 187 ? CYS B 198 ASP B 204 
AA4 3 ALA B 140 ? THR B 144 ? ALA B 157 THR B 161 
AA4 4 LEU B 234 ? PHE B 237 ? LEU B 251 PHE B 254 
AA4 5 CYS B 257 ? ASN B 260 ? CYS B 274 ASN B 277 
AA5 1 GLY B 331 ? LEU B 332 ? GLY B 348 LEU B 349 
AA5 2 ILE B 324 ? ASP B 328 ? ILE B 341 ASP B 345 
AA5 3 ILE B 290 ? LEU B 293 ? ILE B 307 LEU B 310 
AA5 4 THR B 371 ? GLY B 374 ? THR B 388 GLY B 391 
AA5 5 VAL B 398 ? ALA B 401 ? VAL B 415 ALA B 418 
AA5 6 LEU B 425 ? SER B 428 ? LEU B 442 SER B 445 
AA5 7 GLY B 446 ? GLN B 447 ? GLY B 463 GLN B 464 
AA6 1 VAL B 435 ? LYS B 436 ? VAL B 452 LYS B 453 
AA6 2 VAL B 442 ? PHE B 443 ? VAL B 459 PHE B 460 
AA7 1 LEU C 116 ? SER C 119 ? LEU C 133 SER C 136 
AA7 2 CYS C 181 ? ASP C 187 ? CYS C 198 ASP C 204 
AA7 3 ALA C 140 ? THR C 144 ? ALA C 157 THR C 161 
AA7 4 LEU C 234 ? PHE C 237 ? LEU C 251 PHE C 254 
AA7 5 CYS C 257 ? ASN C 260 ? CYS C 274 ASN C 277 
AA8 1 GLY C 331 ? LEU C 332 ? GLY C 348 LEU C 349 
AA8 2 ILE C 324 ? ASP C 328 ? ILE C 341 ASP C 345 
AA8 3 ILE C 290 ? LEU C 293 ? ILE C 307 LEU C 310 
AA8 4 THR C 371 ? GLY C 374 ? THR C 388 GLY C 391 
AA8 5 VAL C 398 ? ALA C 401 ? VAL C 415 ALA C 418 
AA8 6 LEU C 425 ? SER C 428 ? LEU C 442 SER C 445 
AA8 7 GLY C 446 ? GLN C 447 ? GLY C 463 GLN C 464 
AA9 1 VAL C 435 ? LYS C 436 ? VAL C 452 LYS C 453 
AA9 2 VAL C 442 ? PHE C 443 ? VAL C 459 PHE C 460 
AB1 1 LEU D 116 ? SER D 119 ? LEU D 133 SER D 136 
AB1 2 CYS D 181 ? ASP D 187 ? CYS D 198 ASP D 204 
AB1 3 ALA D 140 ? THR D 144 ? ALA D 157 THR D 161 
AB1 4 LEU D 234 ? PHE D 237 ? LEU D 251 PHE D 254 
AB1 5 CYS D 257 ? ASN D 260 ? CYS D 274 ASN D 277 
AB2 1 GLY D 331 ? LEU D 332 ? GLY D 348 LEU D 349 
AB2 2 ILE D 324 ? ASP D 328 ? ILE D 341 ASP D 345 
AB2 3 ILE D 290 ? LEU D 293 ? ILE D 307 LEU D 310 
AB2 4 THR D 371 ? GLY D 374 ? THR D 388 GLY D 391 
AB2 5 VAL D 398 ? ALA D 401 ? VAL D 415 ALA D 418 
AB2 6 LEU D 425 ? SER D 428 ? LEU D 442 SER D 445 
AB2 7 GLY D 446 ? GLN D 447 ? GLY D 463 GLN D 464 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 116 ? N LEU A 133 O CYS A 185 ? O CYS A 202 
AA1 2 3 O ILE A 186 ? O ILE A 203 N THR A 144 ? N THR A 161 
AA1 3 4 N VAL A 141 ? N VAL A 158 O GLN A 236 ? O GLN A 253 
AA1 4 5 N ILE A 235 ? N ILE A 252 O CYS A 257 ? O CYS A 274 
AA2 1 2 O GLY A 331 ? O GLY A 348 N ASP A 328 ? N ASP A 345 
AA2 2 3 O TRP A 325 ? O TRP A 342 N ILE A 290 ? N ILE A 307 
AA2 3 4 N LEU A 293 ? N LEU A 310 O ILE A 373 ? O ILE A 390 
AA2 4 5 N GLY A 374 ? N GLY A 391 O PHE A 400 ? O PHE A 417 
AA2 5 6 N ALA A 401 ? N ALA A 418 O ALA A 427 ? O ALA A 444 
AA2 6 7 N SER A 428 ? N SER A 445 O GLY A 446 ? O GLY A 463 
AA3 1 2 N VAL A 435 ? N VAL A 452 O PHE A 443 ? O PHE A 460 
AA4 1 2 N LEU B 116 ? N LEU B 133 O CYS B 185 ? O CYS B 202 
AA4 2 3 O LEU B 182 ? O LEU B 199 N ALA B 140 ? N ALA B 157 
AA4 3 4 N VAL B 141 ? N VAL B 158 O GLN B 236 ? O GLN B 253 
AA4 4 5 N ILE B 235 ? N ILE B 252 O CYS B 257 ? O CYS B 274 
AA5 1 2 O GLY B 331 ? O GLY B 348 N ASP B 328 ? N ASP B 345 
AA5 2 3 O TRP B 325 ? O TRP B 342 N ILE B 290 ? N ILE B 307 
AA5 3 4 N LEU B 293 ? N LEU B 310 O ILE B 373 ? O ILE B 390 
AA5 4 5 N GLY B 374 ? N GLY B 391 O PHE B 400 ? O PHE B 417 
AA5 5 6 N ILE B 399 ? N ILE B 416 O LEU B 425 ? O LEU B 442 
AA5 6 7 N PHE B 426 ? N PHE B 443 O GLY B 446 ? O GLY B 463 
AA6 1 2 N VAL B 435 ? N VAL B 452 O PHE B 443 ? O PHE B 460 
AA7 1 2 N LEU C 116 ? N LEU C 133 O CYS C 185 ? O CYS C 202 
AA7 2 3 O ILE C 186 ? O ILE C 203 N THR C 144 ? N THR C 161 
AA7 3 4 N VAL C 141 ? N VAL C 158 O GLN C 236 ? O GLN C 253 
AA7 4 5 N ILE C 235 ? N ILE C 252 O CYS C 257 ? O CYS C 274 
AA8 1 2 O GLY C 331 ? O GLY C 348 N ASP C 328 ? N ASP C 345 
AA8 2 3 O TRP C 325 ? O TRP C 342 N ILE C 290 ? N ILE C 307 
AA8 3 4 N LEU C 293 ? N LEU C 310 O ILE C 373 ? O ILE C 390 
AA8 4 5 N GLY C 374 ? N GLY C 391 O PHE C 400 ? O PHE C 417 
AA8 5 6 N ILE C 399 ? N ILE C 416 O LEU C 425 ? O LEU C 442 
AA8 6 7 N SER C 428 ? N SER C 445 O GLY C 446 ? O GLY C 463 
AA9 1 2 N VAL C 435 ? N VAL C 452 O PHE C 443 ? O PHE C 460 
AB1 1 2 N LEU D 116 ? N LEU D 133 O CYS D 185 ? O CYS D 202 
AB1 2 3 O ILE D 186 ? O ILE D 203 N THR D 144 ? N THR D 161 
AB1 3 4 N VAL D 141 ? N VAL D 158 O GLN D 236 ? O GLN D 253 
AB1 4 5 N ILE D 235 ? N ILE D 252 O CYS D 257 ? O CYS D 274 
AB2 1 2 O GLY D 331 ? O GLY D 348 N ASP D 328 ? N ASP D 345 
AB2 2 3 O TRP D 325 ? O TRP D 342 N ILE D 290 ? N ILE D 307 
AB2 3 4 N LEU D 293 ? N LEU D 310 O ILE D 373 ? O ILE D 390 
AB2 4 5 N GLY D 374 ? N GLY D 391 O PHE D 400 ? O PHE D 417 
AB2 5 6 N ALA D 401 ? N ALA D 418 O ALA D 427 ? O ALA D 444 
AB2 6 7 N SER D 428 ? N SER D 445 O GLY D 446 ? O GLY D 463 
# 
_pdbx_entry_details.entry_id                   9AYI 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 THR A 76  ? ? -96.89  -69.09  
2  1 TYR A 112 ? ? -123.22 -151.88 
3  1 TYR A 112 ? ? -123.22 -151.25 
4  1 ARG A 128 ? ? -128.62 -78.79  
5  1 ARG A 128 ? ? -128.62 -77.80  
6  1 TYR A 175 ? ? -69.86  4.13    
7  1 TYR A 175 ? ? -69.86  5.17    
8  1 TYR A 175 ? ? -69.86  4.18    
9  1 TYR A 175 ? ? -69.86  6.58    
10 1 LYS A 300 ? ? -37.79  129.71  
11 1 ALA A 312 ? ? -143.85 35.27   
12 1 ASP A 345 ? ? -103.98 -166.43 
13 1 VAL A 392 ? ? -143.62 49.49   
14 1 THR B 76  ? ? -131.78 -36.67  
15 1 TYR B 112 ? ? -123.50 -151.71 
16 1 TYR B 112 ? ? -123.50 -151.49 
17 1 ARG B 128 ? ? -125.33 -82.18  
18 1 TYR B 175 ? ? -67.81  2.02    
19 1 TYR B 175 ? ? -67.81  7.19    
20 1 ASP B 345 ? ? -106.93 -168.59 
21 1 VAL B 392 ? ? -144.39 51.63   
22 1 PRO B 422 ? ? -77.66  -168.08 
23 1 GLU C 23  ? ? -57.33  108.65  
24 1 THR C 76  ? ? -92.86  -71.99  
25 1 TYR C 112 ? ? -122.02 -151.01 
26 1 ARG C 128 ? ? -127.45 -79.54  
27 1 ALA C 312 ? ? -142.38 39.00   
28 1 ASP C 345 ? ? -102.76 -166.52 
29 1 VAL C 392 ? ? -141.45 52.31   
30 1 LYS D 74  ? ? -92.18  36.29   
31 1 TYR D 112 ? ? -122.86 -154.32 
32 1 ARG D 128 ? ? -131.22 -80.83  
33 1 LEU D 167 ? ? -50.55  105.22  
34 1 TYR D 175 ? ? -69.40  5.70    
35 1 TYR D 175 ? ? -69.40  0.36    
36 1 ALA D 312 ? ? -147.11 33.89   
37 1 ASP D 345 ? ? -95.32  -159.25 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSX 103 A CSX 120 ? CYS 'modified residue' 
2 B CSX 103 B CSX 120 ? CYS 'modified residue' 
3 C CSX 103 C CSX 120 ? CYS 'modified residue' 
4 D CSX 103 D CSX 120 ? CYS 'modified residue' 
# 
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 1244 ? .    6.00 
2 1 O ? B HOH 1215 ? 6.74 .    
# 
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 18  ? A MET 1   
2  1 Y 1 A LEU 19  ? A LEU 2   
3  1 Y 1 A HIS 20  ? A HIS 3   
4  1 Y 1 A ILE 21  ? A ILE 4   
5  1 Y 1 A SER 575 ? A SER 558 
6  1 Y 1 A ALA 576 ? A ALA 559 
7  1 Y 1 A SER 577 ? A SER 560 
8  1 Y 1 A VAL 581 ? A VAL 564 
9  1 Y 1 A ILE 582 ? A ILE 565 
10 1 Y 1 A THR 583 ? A THR 566 
11 1 Y 1 A GLU 584 ? A GLU 567 
12 1 Y 1 A LEU 585 ? A LEU 568 
13 1 Y 1 A GLU 586 ? A GLU 569 
14 1 Y 1 A HIS 587 ? A HIS 570 
15 1 Y 1 A HIS 588 ? A HIS 571 
16 1 Y 1 A HIS 589 ? A HIS 572 
17 1 Y 1 A HIS 590 ? A HIS 573 
18 1 Y 1 A HIS 591 ? A HIS 574 
19 1 Y 1 A HIS 592 ? A HIS 575 
20 1 Y 1 B MET 18  ? B MET 1   
21 1 Y 1 B LEU 19  ? B LEU 2   
22 1 Y 1 B HIS 20  ? B HIS 3   
23 1 Y 1 B ILE 21  ? B ILE 4   
24 1 Y 1 B LYS 22  ? B LYS 5   
25 1 Y 1 B SER 575 ? B SER 558 
26 1 Y 1 B ALA 576 ? B ALA 559 
27 1 Y 1 B SER 577 ? B SER 560 
28 1 Y 1 B SER 578 ? B SER 561 
29 1 Y 1 B PRO 579 ? B PRO 562 
30 1 Y 1 B PRO 580 ? B PRO 563 
31 1 Y 1 B VAL 581 ? B VAL 564 
32 1 Y 1 B ILE 582 ? B ILE 565 
33 1 Y 1 B THR 583 ? B THR 566 
34 1 Y 1 B GLU 584 ? B GLU 567 
35 1 Y 1 B LEU 585 ? B LEU 568 
36 1 Y 1 B GLU 586 ? B GLU 569 
37 1 Y 1 B HIS 587 ? B HIS 570 
38 1 Y 1 B HIS 588 ? B HIS 571 
39 1 Y 1 B HIS 589 ? B HIS 572 
40 1 Y 1 B HIS 590 ? B HIS 573 
41 1 Y 1 B HIS 591 ? B HIS 574 
42 1 Y 1 B HIS 592 ? B HIS 575 
43 1 Y 1 C MET 18  ? C MET 1   
44 1 Y 1 C LEU 19  ? C LEU 2   
45 1 Y 1 C HIS 20  ? C HIS 3   
46 1 Y 1 C ILE 21  ? C ILE 4   
47 1 Y 1 C ALA 576 ? C ALA 559 
48 1 Y 1 C VAL 581 ? C VAL 564 
49 1 Y 1 C ILE 582 ? C ILE 565 
50 1 Y 1 C THR 583 ? C THR 566 
51 1 Y 1 C GLU 584 ? C GLU 567 
52 1 Y 1 C LEU 585 ? C LEU 568 
53 1 Y 1 C GLU 586 ? C GLU 569 
54 1 Y 1 C HIS 587 ? C HIS 570 
55 1 Y 1 C HIS 588 ? C HIS 571 
56 1 Y 1 C HIS 589 ? C HIS 572 
57 1 Y 1 C HIS 590 ? C HIS 573 
58 1 Y 1 C HIS 591 ? C HIS 574 
59 1 Y 1 C HIS 592 ? C HIS 575 
60 1 Y 1 D MET 18  ? D MET 1   
61 1 Y 1 D LEU 19  ? D LEU 2   
62 1 Y 1 D HIS 20  ? D HIS 3   
63 1 Y 1 D ILE 21  ? D ILE 4   
64 1 Y 1 D LYS 22  ? D LYS 5   
65 1 Y 1 D SER 368 ? D SER 351 
66 1 Y 1 D ALA 369 ? D ALA 352 
67 1 Y 1 D PRO 370 ? D PRO 353 
68 1 Y 1 D GLU 371 ? D GLU 354 
69 1 Y 1 D SER 372 ? D SER 355 
70 1 Y 1 D ILE 373 ? D ILE 356 
71 1 Y 1 D LYS 453 ? D LYS 436 
72 1 Y 1 D LEU 454 ? D LEU 437 
73 1 Y 1 D THR 455 ? D THR 438 
74 1 Y 1 D ASP 456 ? D ASP 439 
75 1 Y 1 D GLY 457 ? D GLY 440 
76 1 Y 1 D SER 575 ? D SER 558 
77 1 Y 1 D ALA 576 ? D ALA 559 
78 1 Y 1 D SER 577 ? D SER 560 
79 1 Y 1 D SER 578 ? D SER 561 
80 1 Y 1 D VAL 581 ? D VAL 564 
81 1 Y 1 D ILE 582 ? D ILE 565 
82 1 Y 1 D THR 583 ? D THR 566 
83 1 Y 1 D GLU 584 ? D GLU 567 
84 1 Y 1 D LEU 585 ? D LEU 568 
85 1 Y 1 D GLU 586 ? D GLU 569 
86 1 Y 1 D HIS 587 ? D HIS 570 
87 1 Y 1 D HIS 588 ? D HIS 571 
88 1 Y 1 D HIS 589 ? D HIS 572 
89 1 Y 1 D HIS 590 ? D HIS 573 
90 1 Y 1 D HIS 591 ? D HIS 574 
91 1 Y 1 D HIS 592 ? D HIS 575 
# 
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  
CL  CL   CL N N 74  
CSX N    N  N N 75  
CSX CA   C  N R 76  
CSX CB   C  N N 77  
CSX SG   S  N S 78  
CSX C    C  N N 79  
CSX O    O  N N 80  
CSX OXT  O  N N 81  
CSX OD   O  N N 82  
CSX H    H  N N 83  
CSX H2   H  N N 84  
CSX HA   H  N N 85  
CSX HB2  H  N N 86  
CSX HB3  H  N N 87  
CSX HG   H  N N 88  
CSX HXT  H  N N 89  
CYS N    N  N N 90  
CYS CA   C  N R 91  
CYS C    C  N N 92  
CYS O    O  N N 93  
CYS CB   C  N N 94  
CYS SG   S  N N 95  
CYS OXT  O  N N 96  
CYS H    H  N N 97  
CYS H2   H  N N 98  
CYS HA   H  N N 99  
CYS HB2  H  N N 100 
CYS HB3  H  N N 101 
CYS HG   H  N N 102 
CYS HXT  H  N N 103 
EDO C1   C  N N 104 
EDO O1   O  N N 105 
EDO C2   C  N N 106 
EDO O2   O  N N 107 
EDO H11  H  N N 108 
EDO H12  H  N N 109 
EDO HO1  H  N N 110 
EDO H21  H  N N 111 
EDO H22  H  N N 112 
EDO HO2  H  N N 113 
GLN N    N  N N 114 
GLN CA   C  N S 115 
GLN C    C  N N 116 
GLN O    O  N N 117 
GLN CB   C  N N 118 
GLN CG   C  N N 119 
GLN CD   C  N N 120 
GLN OE1  O  N N 121 
GLN NE2  N  N N 122 
GLN OXT  O  N N 123 
GLN H    H  N N 124 
GLN H2   H  N N 125 
GLN HA   H  N N 126 
GLN HB2  H  N N 127 
GLN HB3  H  N N 128 
GLN HG2  H  N N 129 
GLN HG3  H  N N 130 
GLN HE21 H  N N 131 
GLN HE22 H  N N 132 
GLN HXT  H  N N 133 
GLU N    N  N N 134 
GLU CA   C  N S 135 
GLU C    C  N N 136 
GLU O    O  N N 137 
GLU CB   C  N N 138 
GLU CG   C  N N 139 
GLU CD   C  N N 140 
GLU OE1  O  N N 141 
GLU OE2  O  N N 142 
GLU OXT  O  N N 143 
GLU H    H  N N 144 
GLU H2   H  N N 145 
GLU HA   H  N N 146 
GLU HB2  H  N N 147 
GLU HB3  H  N N 148 
GLU HG2  H  N N 149 
GLU HG3  H  N N 150 
GLU HE2  H  N N 151 
GLU HXT  H  N N 152 
GLY N    N  N N 153 
GLY CA   C  N N 154 
GLY C    C  N N 155 
GLY O    O  N N 156 
GLY OXT  O  N N 157 
GLY H    H  N N 158 
GLY H2   H  N N 159 
GLY HA2  H  N N 160 
GLY HA3  H  N N 161 
GLY HXT  H  N N 162 
HIS N    N  N N 163 
HIS CA   C  N S 164 
HIS C    C  N N 165 
HIS O    O  N N 166 
HIS CB   C  N N 167 
HIS CG   C  Y N 168 
HIS ND1  N  Y N 169 
HIS CD2  C  Y N 170 
HIS CE1  C  Y N 171 
HIS NE2  N  Y N 172 
HIS OXT  O  N N 173 
HIS H    H  N N 174 
HIS H2   H  N N 175 
HIS HA   H  N N 176 
HIS HB2  H  N N 177 
HIS HB3  H  N N 178 
HIS HD1  H  N N 179 
HIS HD2  H  N N 180 
HIS HE1  H  N N 181 
HIS HE2  H  N N 182 
HIS HXT  H  N N 183 
HOH O    O  N N 184 
HOH H1   H  N N 185 
HOH H2   H  N N 186 
ILE N    N  N N 187 
ILE CA   C  N S 188 
ILE C    C  N N 189 
ILE O    O  N N 190 
ILE CB   C  N S 191 
ILE CG1  C  N N 192 
ILE CG2  C  N N 193 
ILE CD1  C  N N 194 
ILE OXT  O  N N 195 
ILE H    H  N N 196 
ILE H2   H  N N 197 
ILE HA   H  N N 198 
ILE HB   H  N N 199 
ILE HG12 H  N N 200 
ILE HG13 H  N N 201 
ILE HG21 H  N N 202 
ILE HG22 H  N N 203 
ILE HG23 H  N N 204 
ILE HD11 H  N N 205 
ILE HD12 H  N N 206 
ILE HD13 H  N N 207 
ILE HXT  H  N N 208 
LEU N    N  N N 209 
LEU CA   C  N S 210 
LEU C    C  N N 211 
LEU O    O  N N 212 
LEU CB   C  N N 213 
LEU CG   C  N N 214 
LEU CD1  C  N N 215 
LEU CD2  C  N N 216 
LEU OXT  O  N N 217 
LEU H    H  N N 218 
LEU H2   H  N N 219 
LEU HA   H  N N 220 
LEU HB2  H  N N 221 
LEU HB3  H  N N 222 
LEU HG   H  N N 223 
LEU HD11 H  N N 224 
LEU HD12 H  N N 225 
LEU HD13 H  N N 226 
LEU HD21 H  N N 227 
LEU HD22 H  N N 228 
LEU HD23 H  N N 229 
LEU HXT  H  N N 230 
LYS N    N  N N 231 
LYS CA   C  N S 232 
LYS C    C  N N 233 
LYS O    O  N N 234 
LYS CB   C  N N 235 
LYS CG   C  N N 236 
LYS CD   C  N N 237 
LYS CE   C  N N 238 
LYS NZ   N  N N 239 
LYS OXT  O  N N 240 
LYS H    H  N N 241 
LYS H2   H  N N 242 
LYS HA   H  N N 243 
LYS HB2  H  N N 244 
LYS HB3  H  N N 245 
LYS HG2  H  N N 246 
LYS HG3  H  N N 247 
LYS HD2  H  N N 248 
LYS HD3  H  N N 249 
LYS HE2  H  N N 250 
LYS HE3  H  N N 251 
LYS HZ1  H  N N 252 
LYS HZ2  H  N N 253 
LYS HZ3  H  N N 254 
LYS HXT  H  N N 255 
MET N    N  N N 256 
MET CA   C  N S 257 
MET C    C  N N 258 
MET O    O  N N 259 
MET CB   C  N N 260 
MET CG   C  N N 261 
MET SD   S  N N 262 
MET CE   C  N N 263 
MET OXT  O  N N 264 
MET H    H  N N 265 
MET H2   H  N N 266 
MET HA   H  N N 267 
MET HB2  H  N N 268 
MET HB3  H  N N 269 
MET HG2  H  N N 270 
MET HG3  H  N N 271 
MET HE1  H  N N 272 
MET HE2  H  N N 273 
MET HE3  H  N N 274 
MET HXT  H  N N 275 
MG  MG   MG N N 276 
NAD PA   P  N S 277 
NAD O1A  O  N N 278 
NAD O2A  O  N N 279 
NAD O5B  O  N N 280 
NAD C5B  C  N N 281 
NAD C4B  C  N R 282 
NAD O4B  O  N N 283 
NAD C3B  C  N S 284 
NAD O3B  O  N N 285 
NAD C2B  C  N R 286 
NAD O2B  O  N N 287 
NAD C1B  C  N R 288 
NAD N9A  N  Y N 289 
NAD C8A  C  Y N 290 
NAD N7A  N  Y N 291 
NAD C5A  C  Y N 292 
NAD C6A  C  Y N 293 
NAD N6A  N  N N 294 
NAD N1A  N  Y N 295 
NAD C2A  C  Y N 296 
NAD N3A  N  Y N 297 
NAD C4A  C  Y N 298 
NAD O3   O  N N 299 
NAD PN   P  N N 300 
NAD O1N  O  N N 301 
NAD O2N  O  N N 302 
NAD O5D  O  N N 303 
NAD C5D  C  N N 304 
NAD C4D  C  N R 305 
NAD O4D  O  N N 306 
NAD C3D  C  N S 307 
NAD O3D  O  N N 308 
NAD C2D  C  N R 309 
NAD O2D  O  N N 310 
NAD C1D  C  N R 311 
NAD N1N  N  Y N 312 
NAD C2N  C  Y N 313 
NAD C3N  C  Y N 314 
NAD C7N  C  N N 315 
NAD O7N  O  N N 316 
NAD N7N  N  N N 317 
NAD C4N  C  Y N 318 
NAD C5N  C  Y N 319 
NAD C6N  C  Y N 320 
NAD HOA2 H  N N 321 
NAD H51A H  N N 322 
NAD H52A H  N N 323 
NAD H4B  H  N N 324 
NAD H3B  H  N N 325 
NAD HO3A H  N N 326 
NAD H2B  H  N N 327 
NAD HO2A H  N N 328 
NAD H1B  H  N N 329 
NAD H8A  H  N N 330 
NAD H61A H  N N 331 
NAD H62A H  N N 332 
NAD H2A  H  N N 333 
NAD H51N H  N N 334 
NAD H52N H  N N 335 
NAD H4D  H  N N 336 
NAD H3D  H  N N 337 
NAD HO3N H  N N 338 
NAD H2D  H  N N 339 
NAD HO2N H  N N 340 
NAD H1D  H  N N 341 
NAD H2N  H  N N 342 
NAD H71N H  N N 343 
NAD H72N H  N N 344 
NAD H4N  H  N N 345 
NAD H5N  H  N N 346 
NAD H6N  H  N N 347 
PHE N    N  N N 348 
PHE CA   C  N S 349 
PHE C    C  N N 350 
PHE O    O  N N 351 
PHE CB   C  N N 352 
PHE CG   C  Y N 353 
PHE CD1  C  Y N 354 
PHE CD2  C  Y N 355 
PHE CE1  C  Y N 356 
PHE CE2  C  Y N 357 
PHE CZ   C  Y N 358 
PHE OXT  O  N N 359 
PHE H    H  N N 360 
PHE H2   H  N N 361 
PHE HA   H  N N 362 
PHE HB2  H  N N 363 
PHE HB3  H  N N 364 
PHE HD1  H  N N 365 
PHE HD2  H  N N 366 
PHE HE1  H  N N 367 
PHE HE2  H  N N 368 
PHE HZ   H  N N 369 
PHE HXT  H  N N 370 
PRO N    N  N N 371 
PRO CA   C  N S 372 
PRO C    C  N N 373 
PRO O    O  N N 374 
PRO CB   C  N N 375 
PRO CG   C  N N 376 
PRO CD   C  N N 377 
PRO OXT  O  N N 378 
PRO H    H  N N 379 
PRO HA   H  N N 380 
PRO HB2  H  N N 381 
PRO HB3  H  N N 382 
PRO HG2  H  N N 383 
PRO HG3  H  N N 384 
PRO HD2  H  N N 385 
PRO HD3  H  N N 386 
PRO HXT  H  N N 387 
SER N    N  N N 388 
SER CA   C  N S 389 
SER C    C  N N 390 
SER O    O  N N 391 
SER CB   C  N N 392 
SER OG   O  N N 393 
SER OXT  O  N N 394 
SER H    H  N N 395 
SER H2   H  N N 396 
SER HA   H  N N 397 
SER HB2  H  N N 398 
SER HB3  H  N N 399 
SER HG   H  N N 400 
SER HXT  H  N N 401 
THR N    N  N N 402 
THR CA   C  N S 403 
THR C    C  N N 404 
THR O    O  N N 405 
THR CB   C  N R 406 
THR OG1  O  N N 407 
THR CG2  C  N N 408 
THR OXT  O  N N 409 
THR H    H  N N 410 
THR H2   H  N N 411 
THR HA   H  N N 412 
THR HB   H  N N 413 
THR HG1  H  N N 414 
THR HG21 H  N N 415 
THR HG22 H  N N 416 
THR HG23 H  N N 417 
THR HXT  H  N N 418 
TLA O1   O  N N 419 
TLA O11  O  N N 420 
TLA C1   C  N N 421 
TLA C2   C  N R 422 
TLA O2   O  N N 423 
TLA C3   C  N R 424 
TLA O3   O  N N 425 
TLA C4   C  N N 426 
TLA O4   O  N N 427 
TLA O41  O  N N 428 
TLA H11  H  N N 429 
TLA H2   H  N N 430 
TLA HA   H  N N 431 
TLA H3   H  N N 432 
TLA HB   H  N N 433 
TLA H41  H  N N 434 
TRP N    N  N N 435 
TRP CA   C  N S 436 
TRP C    C  N N 437 
TRP O    O  N N 438 
TRP CB   C  N N 439 
TRP CG   C  Y N 440 
TRP CD1  C  Y N 441 
TRP CD2  C  Y N 442 
TRP NE1  N  Y N 443 
TRP CE2  C  Y N 444 
TRP CE3  C  Y N 445 
TRP CZ2  C  Y N 446 
TRP CZ3  C  Y N 447 
TRP CH2  C  Y N 448 
TRP OXT  O  N N 449 
TRP H    H  N N 450 
TRP H2   H  N N 451 
TRP HA   H  N N 452 
TRP HB2  H  N N 453 
TRP HB3  H  N N 454 
TRP HD1  H  N N 455 
TRP HE1  H  N N 456 
TRP HE3  H  N N 457 
TRP HZ2  H  N N 458 
TRP HZ3  H  N N 459 
TRP HH2  H  N N 460 
TRP HXT  H  N N 461 
TYR N    N  N N 462 
TYR CA   C  N S 463 
TYR C    C  N N 464 
TYR O    O  N N 465 
TYR CB   C  N N 466 
TYR CG   C  Y N 467 
TYR CD1  C  Y N 468 
TYR CD2  C  Y N 469 
TYR CE1  C  Y N 470 
TYR CE2  C  Y N 471 
TYR CZ   C  Y N 472 
TYR OH   O  N N 473 
TYR OXT  O  N N 474 
TYR H    H  N N 475 
TYR H2   H  N N 476 
TYR HA   H  N N 477 
TYR HB2  H  N N 478 
TYR HB3  H  N N 479 
TYR HD1  H  N N 480 
TYR HD2  H  N N 481 
TYR HE1  H  N N 482 
TYR HE2  H  N N 483 
TYR HH   H  N N 484 
TYR HXT  H  N N 485 
VAL N    N  N N 486 
VAL CA   C  N S 487 
VAL C    C  N N 488 
VAL O    O  N N 489 
VAL CB   C  N N 490 
VAL CG1  C  N N 491 
VAL CG2  C  N N 492 
VAL OXT  O  N N 493 
VAL H    H  N N 494 
VAL H2   H  N N 495 
VAL HA   H  N N 496 
VAL HB   H  N N 497 
VAL HG11 H  N N 498 
VAL HG12 H  N N 499 
VAL HG13 H  N N 500 
VAL HG21 H  N N 501 
VAL HG22 H  N N 502 
VAL HG23 H  N N 503 
VAL HXT  H  N N 504 
# 
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  
CSX N   CA   sing N N 70  
CSX N   H    sing N N 71  
CSX N   H2   sing N N 72  
CSX CA  CB   sing N N 73  
CSX CA  C    sing N N 74  
CSX CA  HA   sing N N 75  
CSX CB  SG   sing N N 76  
CSX CB  HB2  sing N N 77  
CSX CB  HB3  sing N N 78  
CSX SG  OD   doub N N 79  
CSX SG  HG   sing N N 80  
CSX C   O    doub N N 81  
CSX C   OXT  sing N N 82  
CSX OXT HXT  sing N N 83  
CYS N   CA   sing N N 84  
CYS N   H    sing N N 85  
CYS N   H2   sing N N 86  
CYS CA  C    sing N N 87  
CYS CA  CB   sing N N 88  
CYS CA  HA   sing N N 89  
CYS C   O    doub N N 90  
CYS C   OXT  sing N N 91  
CYS CB  SG   sing N N 92  
CYS CB  HB2  sing N N 93  
CYS CB  HB3  sing N N 94  
CYS SG  HG   sing N N 95  
CYS OXT HXT  sing N N 96  
EDO C1  O1   sing N N 97  
EDO C1  C2   sing N N 98  
EDO C1  H11  sing N N 99  
EDO C1  H12  sing N N 100 
EDO O1  HO1  sing N N 101 
EDO C2  O2   sing N N 102 
EDO C2  H21  sing N N 103 
EDO C2  H22  sing N N 104 
EDO O2  HO2  sing N N 105 
GLN N   CA   sing N N 106 
GLN N   H    sing N N 107 
GLN N   H2   sing N N 108 
GLN CA  C    sing N N 109 
GLN CA  CB   sing N N 110 
GLN CA  HA   sing N N 111 
GLN C   O    doub N N 112 
GLN C   OXT  sing N N 113 
GLN CB  CG   sing N N 114 
GLN CB  HB2  sing N N 115 
GLN CB  HB3  sing N N 116 
GLN CG  CD   sing N N 117 
GLN CG  HG2  sing N N 118 
GLN CG  HG3  sing N N 119 
GLN CD  OE1  doub N N 120 
GLN CD  NE2  sing N N 121 
GLN NE2 HE21 sing N N 122 
GLN NE2 HE22 sing N N 123 
GLN OXT HXT  sing N N 124 
GLU N   CA   sing N N 125 
GLU N   H    sing N N 126 
GLU N   H2   sing N N 127 
GLU CA  C    sing N N 128 
GLU CA  CB   sing N N 129 
GLU CA  HA   sing N N 130 
GLU C   O    doub N N 131 
GLU C   OXT  sing N N 132 
GLU CB  CG   sing N N 133 
GLU CB  HB2  sing N N 134 
GLU CB  HB3  sing N N 135 
GLU CG  CD   sing N N 136 
GLU CG  HG2  sing N N 137 
GLU CG  HG3  sing N N 138 
GLU CD  OE1  doub N N 139 
GLU CD  OE2  sing N N 140 
GLU OE2 HE2  sing N N 141 
GLU OXT HXT  sing N N 142 
GLY N   CA   sing N N 143 
GLY N   H    sing N N 144 
GLY N   H2   sing N N 145 
GLY CA  C    sing N N 146 
GLY CA  HA2  sing N N 147 
GLY CA  HA3  sing N N 148 
GLY C   O    doub N N 149 
GLY C   OXT  sing N N 150 
GLY OXT HXT  sing N N 151 
HIS N   CA   sing N N 152 
HIS N   H    sing N N 153 
HIS N   H2   sing N N 154 
HIS CA  C    sing N N 155 
HIS CA  CB   sing N N 156 
HIS CA  HA   sing N N 157 
HIS C   O    doub N N 158 
HIS C   OXT  sing N N 159 
HIS CB  CG   sing N N 160 
HIS CB  HB2  sing N N 161 
HIS CB  HB3  sing N N 162 
HIS CG  ND1  sing Y N 163 
HIS CG  CD2  doub Y N 164 
HIS ND1 CE1  doub Y N 165 
HIS ND1 HD1  sing N N 166 
HIS CD2 NE2  sing Y N 167 
HIS CD2 HD2  sing N N 168 
HIS CE1 NE2  sing Y N 169 
HIS CE1 HE1  sing N N 170 
HIS NE2 HE2  sing N N 171 
HIS OXT HXT  sing N N 172 
HOH O   H1   sing N N 173 
HOH O   H2   sing N N 174 
ILE N   CA   sing N N 175 
ILE N   H    sing N N 176 
ILE N   H2   sing N N 177 
ILE CA  C    sing N N 178 
ILE CA  CB   sing N N 179 
ILE CA  HA   sing N N 180 
ILE C   O    doub N N 181 
ILE C   OXT  sing N N 182 
ILE CB  CG1  sing N N 183 
ILE CB  CG2  sing N N 184 
ILE CB  HB   sing N N 185 
ILE CG1 CD1  sing N N 186 
ILE CG1 HG12 sing N N 187 
ILE CG1 HG13 sing N N 188 
ILE CG2 HG21 sing N N 189 
ILE CG2 HG22 sing N N 190 
ILE CG2 HG23 sing N N 191 
ILE CD1 HD11 sing N N 192 
ILE CD1 HD12 sing N N 193 
ILE CD1 HD13 sing N N 194 
ILE OXT HXT  sing N N 195 
LEU N   CA   sing N N 196 
LEU N   H    sing N N 197 
LEU N   H2   sing N N 198 
LEU CA  C    sing N N 199 
LEU CA  CB   sing N N 200 
LEU CA  HA   sing N N 201 
LEU C   O    doub N N 202 
LEU C   OXT  sing N N 203 
LEU CB  CG   sing N N 204 
LEU CB  HB2  sing N N 205 
LEU CB  HB3  sing N N 206 
LEU CG  CD1  sing N N 207 
LEU CG  CD2  sing N N 208 
LEU CG  HG   sing N N 209 
LEU CD1 HD11 sing N N 210 
LEU CD1 HD12 sing N N 211 
LEU CD1 HD13 sing N N 212 
LEU CD2 HD21 sing N N 213 
LEU CD2 HD22 sing N N 214 
LEU CD2 HD23 sing N N 215 
LEU OXT HXT  sing N N 216 
LYS N   CA   sing N N 217 
LYS N   H    sing N N 218 
LYS N   H2   sing N N 219 
LYS CA  C    sing N N 220 
LYS CA  CB   sing N N 221 
LYS CA  HA   sing N N 222 
LYS C   O    doub N N 223 
LYS C   OXT  sing N N 224 
LYS CB  CG   sing N N 225 
LYS CB  HB2  sing N N 226 
LYS CB  HB3  sing N N 227 
LYS CG  CD   sing N N 228 
LYS CG  HG2  sing N N 229 
LYS CG  HG3  sing N N 230 
LYS CD  CE   sing N N 231 
LYS CD  HD2  sing N N 232 
LYS CD  HD3  sing N N 233 
LYS CE  NZ   sing N N 234 
LYS CE  HE2  sing N N 235 
LYS CE  HE3  sing N N 236 
LYS NZ  HZ1  sing N N 237 
LYS NZ  HZ2  sing N N 238 
LYS NZ  HZ3  sing N N 239 
LYS OXT HXT  sing N N 240 
MET N   CA   sing N N 241 
MET N   H    sing N N 242 
MET N   H2   sing N N 243 
MET CA  C    sing N N 244 
MET CA  CB   sing N N 245 
MET CA  HA   sing N N 246 
MET C   O    doub N N 247 
MET C   OXT  sing N N 248 
MET CB  CG   sing N N 249 
MET CB  HB2  sing N N 250 
MET CB  HB3  sing N N 251 
MET CG  SD   sing N N 252 
MET CG  HG2  sing N N 253 
MET CG  HG3  sing N N 254 
MET SD  CE   sing N N 255 
MET CE  HE1  sing N N 256 
MET CE  HE2  sing N N 257 
MET CE  HE3  sing N N 258 
MET OXT HXT  sing N N 259 
NAD PA  O1A  doub N N 260 
NAD PA  O2A  sing N N 261 
NAD PA  O5B  sing N N 262 
NAD PA  O3   sing N N 263 
NAD O2A HOA2 sing N N 264 
NAD O5B C5B  sing N N 265 
NAD C5B C4B  sing N N 266 
NAD C5B H51A sing N N 267 
NAD C5B H52A sing N N 268 
NAD C4B O4B  sing N N 269 
NAD C4B C3B  sing N N 270 
NAD C4B H4B  sing N N 271 
NAD O4B C1B  sing N N 272 
NAD C3B O3B  sing N N 273 
NAD C3B C2B  sing N N 274 
NAD C3B H3B  sing N N 275 
NAD O3B HO3A sing N N 276 
NAD C2B O2B  sing N N 277 
NAD C2B C1B  sing N N 278 
NAD C2B H2B  sing N N 279 
NAD O2B HO2A sing N N 280 
NAD C1B N9A  sing N N 281 
NAD C1B H1B  sing N N 282 
NAD N9A C8A  sing Y N 283 
NAD N9A C4A  sing Y N 284 
NAD C8A N7A  doub Y N 285 
NAD C8A H8A  sing N N 286 
NAD N7A C5A  sing Y N 287 
NAD C5A C6A  sing Y N 288 
NAD C5A C4A  doub Y N 289 
NAD C6A N6A  sing N N 290 
NAD C6A N1A  doub Y N 291 
NAD N6A H61A sing N N 292 
NAD N6A H62A sing N N 293 
NAD N1A C2A  sing Y N 294 
NAD C2A N3A  doub Y N 295 
NAD C2A H2A  sing N N 296 
NAD N3A C4A  sing Y N 297 
NAD O3  PN   sing N N 298 
NAD PN  O1N  doub N N 299 
NAD PN  O2N  sing N N 300 
NAD PN  O5D  sing N N 301 
NAD O5D C5D  sing N N 302 
NAD C5D C4D  sing N N 303 
NAD C5D H51N sing N N 304 
NAD C5D H52N sing N N 305 
NAD C4D O4D  sing N N 306 
NAD C4D C3D  sing N N 307 
NAD C4D H4D  sing N N 308 
NAD O4D C1D  sing N N 309 
NAD C3D O3D  sing N N 310 
NAD C3D C2D  sing N N 311 
NAD C3D H3D  sing N N 312 
NAD O3D HO3N sing N N 313 
NAD C2D O2D  sing N N 314 
NAD C2D C1D  sing N N 315 
NAD C2D H2D  sing N N 316 
NAD O2D HO2N sing N N 317 
NAD C1D N1N  sing N N 318 
NAD C1D H1D  sing N N 319 
NAD N1N C2N  sing Y N 320 
NAD N1N C6N  doub Y N 321 
NAD C2N C3N  doub Y N 322 
NAD C2N H2N  sing N N 323 
NAD C3N C7N  sing N N 324 
NAD C3N C4N  sing Y N 325 
NAD C7N O7N  doub N N 326 
NAD C7N N7N  sing N N 327 
NAD N7N H71N sing N N 328 
NAD N7N H72N sing N N 329 
NAD C4N C5N  doub Y N 330 
NAD C4N H4N  sing N N 331 
NAD C5N C6N  sing Y N 332 
NAD C5N H5N  sing N N 333 
NAD C6N H6N  sing N N 334 
PHE N   CA   sing N N 335 
PHE N   H    sing N N 336 
PHE N   H2   sing N N 337 
PHE CA  C    sing N N 338 
PHE CA  CB   sing N N 339 
PHE CA  HA   sing N N 340 
PHE C   O    doub N N 341 
PHE C   OXT  sing N N 342 
PHE CB  CG   sing N N 343 
PHE CB  HB2  sing N N 344 
PHE CB  HB3  sing N N 345 
PHE CG  CD1  doub Y N 346 
PHE CG  CD2  sing Y N 347 
PHE CD1 CE1  sing Y N 348 
PHE CD1 HD1  sing N N 349 
PHE CD2 CE2  doub Y N 350 
PHE CD2 HD2  sing N N 351 
PHE CE1 CZ   doub Y N 352 
PHE CE1 HE1  sing N N 353 
PHE CE2 CZ   sing Y N 354 
PHE CE2 HE2  sing N N 355 
PHE CZ  HZ   sing N N 356 
PHE OXT HXT  sing N N 357 
PRO N   CA   sing N N 358 
PRO N   CD   sing N N 359 
PRO N   H    sing N N 360 
PRO CA  C    sing N N 361 
PRO CA  CB   sing N N 362 
PRO CA  HA   sing N N 363 
PRO C   O    doub N N 364 
PRO C   OXT  sing N N 365 
PRO CB  CG   sing N N 366 
PRO CB  HB2  sing N N 367 
PRO CB  HB3  sing N N 368 
PRO CG  CD   sing N N 369 
PRO CG  HG2  sing N N 370 
PRO CG  HG3  sing N N 371 
PRO CD  HD2  sing N N 372 
PRO CD  HD3  sing N N 373 
PRO OXT HXT  sing N N 374 
SER N   CA   sing N N 375 
SER N   H    sing N N 376 
SER N   H2   sing N N 377 
SER CA  C    sing N N 378 
SER CA  CB   sing N N 379 
SER CA  HA   sing N N 380 
SER C   O    doub N N 381 
SER C   OXT  sing N N 382 
SER CB  OG   sing N N 383 
SER CB  HB2  sing N N 384 
SER CB  HB3  sing N N 385 
SER OG  HG   sing N N 386 
SER OXT HXT  sing N N 387 
THR N   CA   sing N N 388 
THR N   H    sing N N 389 
THR N   H2   sing N N 390 
THR CA  C    sing N N 391 
THR CA  CB   sing N N 392 
THR CA  HA   sing N N 393 
THR C   O    doub N N 394 
THR C   OXT  sing N N 395 
THR CB  OG1  sing N N 396 
THR CB  CG2  sing N N 397 
THR CB  HB   sing N N 398 
THR OG1 HG1  sing N N 399 
THR CG2 HG21 sing N N 400 
THR CG2 HG22 sing N N 401 
THR CG2 HG23 sing N N 402 
THR OXT HXT  sing N N 403 
TLA O1  C1   doub N N 404 
TLA O11 C1   sing N N 405 
TLA O11 H11  sing N N 406 
TLA C1  C2   sing N N 407 
TLA C2  O2   sing N N 408 
TLA C2  C3   sing N N 409 
TLA C2  H2   sing N N 410 
TLA O2  HA   sing N N 411 
TLA C3  O3   sing N N 412 
TLA C3  C4   sing N N 413 
TLA C3  H3   sing N N 414 
TLA O3  HB   sing N N 415 
TLA C4  O4   doub N N 416 
TLA C4  O41  sing N N 417 
TLA O41 H41  sing N N 418 
TRP N   CA   sing N N 419 
TRP N   H    sing N N 420 
TRP N   H2   sing N N 421 
TRP CA  C    sing N N 422 
TRP CA  CB   sing N N 423 
TRP CA  HA   sing N N 424 
TRP C   O    doub N N 425 
TRP C   OXT  sing N N 426 
TRP CB  CG   sing N N 427 
TRP CB  HB2  sing N N 428 
TRP CB  HB3  sing N N 429 
TRP CG  CD1  doub Y N 430 
TRP CG  CD2  sing Y N 431 
TRP CD1 NE1  sing Y N 432 
TRP CD1 HD1  sing N N 433 
TRP CD2 CE2  doub Y N 434 
TRP CD2 CE3  sing Y N 435 
TRP NE1 CE2  sing Y N 436 
TRP NE1 HE1  sing N N 437 
TRP CE2 CZ2  sing Y N 438 
TRP CE3 CZ3  doub Y N 439 
TRP CE3 HE3  sing N N 440 
TRP CZ2 CH2  doub Y N 441 
TRP CZ2 HZ2  sing N N 442 
TRP CZ3 CH2  sing Y N 443 
TRP CZ3 HZ3  sing N N 444 
TRP CH2 HH2  sing N N 445 
TRP OXT HXT  sing N N 446 
TYR N   CA   sing N N 447 
TYR N   H    sing N N 448 
TYR N   H2   sing N N 449 
TYR CA  C    sing N N 450 
TYR CA  CB   sing N N 451 
TYR CA  HA   sing N N 452 
TYR C   O    doub N N 453 
TYR C   OXT  sing N N 454 
TYR CB  CG   sing N N 455 
TYR CB  HB2  sing N N 456 
TYR CB  HB3  sing N N 457 
TYR CG  CD1  doub Y N 458 
TYR CG  CD2  sing Y N 459 
TYR CD1 CE1  sing Y N 460 
TYR CD1 HD1  sing N N 461 
TYR CD2 CE2  doub Y N 462 
TYR CD2 HD2  sing N N 463 
TYR CE1 CZ   doub Y N 464 
TYR CE1 HE1  sing N N 465 
TYR CE2 CZ   sing Y N 466 
TYR CE2 HE2  sing N N 467 
TYR CZ  OH   sing N N 468 
TYR OH  HH   sing N N 469 
TYR OXT HXT  sing N N 470 
VAL N   CA   sing N N 471 
VAL N   H    sing N N 472 
VAL N   H2   sing N N 473 
VAL CA  C    sing N N 474 
VAL CA  CB   sing N N 475 
VAL CA  HA   sing N N 476 
VAL C   O    doub N N 477 
VAL C   OXT  sing N N 478 
VAL CB  CG1  sing N N 479 
VAL CB  CG2  sing N N 480 
VAL CB  HB   sing N N 481 
VAL CG1 HG11 sing N N 482 
VAL CG1 HG12 sing N N 483 
VAL CG1 HG13 sing N N 484 
VAL CG2 HG21 sing N N 485 
VAL CG2 HG22 sing N N 486 
VAL CG2 HG23 sing N N 487 
VAL OXT HXT  sing N N 488 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8W24 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9AYI 
_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]   0.013454 
_atom_sites.fract_transf_matrix[1][2]   -0.003632 
_atom_sites.fract_transf_matrix[1][3]   -0.003627 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010551 
_atom_sites.fract_transf_matrix[2][3]   -0.004121 
_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]   0.010555 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . LYS A  1 5   ? 14.167  -4.080  19.580  1.00 59.92 ? 22   LYS A N   1 
ATOM   2     C  CA  . LYS A  1 5   ? 15.307  -3.964  18.628  1.00 59.69 ? 22   LYS A CA  1 
ATOM   3     C  C   . LYS A  1 5   ? 16.338  -2.986  19.192  1.00 58.22 ? 22   LYS A C   1 
ATOM   4     O  O   . LYS A  1 5   ? 16.108  -1.777  19.179  1.00 56.90 ? 22   LYS A O   1 
ATOM   5     C  CB  . LYS A  1 5   ? 14.808  -3.539  17.240  1.00 60.09 ? 22   LYS A CB  1 
ATOM   6     N  N   . GLU A  1 6   ? 17.465  -3.524  19.690  1.00 57.85 ? 23   GLU A N   1 
ATOM   7     C  CA  . GLU A  1 6   ? 18.523  -2.709  20.273  1.00 55.85 ? 23   GLU A CA  1 
ATOM   8     C  C   . GLU A  1 6   ? 19.128  -1.838  19.173  1.00 57.03 ? 23   GLU A C   1 
ATOM   9     O  O   . GLU A  1 6   ? 19.767  -2.350  18.256  1.00 56.84 ? 23   GLU A O   1 
ATOM   10    C  CB  . GLU A  1 6   ? 19.611  -3.535  20.969  1.00 52.88 ? 23   GLU A CB  1 
ATOM   11    C  CG  . GLU A  1 6   ? 20.560  -2.689  21.819  1.00 50.36 ? 23   GLU A CG  1 
ATOM   12    C  CD  . GLU A  1 6   ? 21.621  -3.432  22.623  1.00 49.59 ? 23   GLU A CD  1 
ATOM   13    O  OE1 . GLU A  1 6   ? 21.818  -4.649  22.425  1.00 53.49 ? 23   GLU A OE1 1 
ATOM   14    O  OE2 . GLU A  1 6   ? 22.258  -2.781  23.475  1.00 46.85 ? 23   GLU A OE2 1 
ATOM   15    N  N   . LYS A  1 7   ? 18.910  -0.521  19.280  1.00 58.03 ? 24   LYS A N   1 
ATOM   16    C  CA  . LYS A  1 7   ? 19.315  0.416   18.244  1.00 57.65 ? 24   LYS A CA  1 
ATOM   17    C  C   . LYS A  1 7   ? 20.829  0.596   18.304  1.00 54.01 ? 24   LYS A C   1 
ATOM   18    O  O   . LYS A  1 7   ? 21.392  0.756   19.387  1.00 52.58 ? 24   LYS A O   1 
ATOM   19    C  CB  . LYS A  1 7   ? 18.614  1.769   18.408  1.00 58.85 ? 24   LYS A CB  1 
ATOM   20    C  CG  . LYS A  1 7   ? 17.093  1.717   18.463  1.00 60.97 ? 24   LYS A CG  1 
ATOM   21    C  CD  . LYS A  1 7   ? 16.467  3.046   18.863  1.00 62.55 ? 24   LYS A CD  1 
ATOM   22    C  CE  . LYS A  1 7   ? 16.384  4.014   17.731  1.00 63.74 ? 24   LYS A CE  1 
ATOM   23    N  NZ  . LYS A  1 7   ? 15.201  3.759   16.907  1.00 66.03 ? 24   LYS A NZ  1 
ATOM   24    N  N   . GLY A  1 8   ? 21.467  0.576   17.127  1.00 49.87 ? 25   GLY A N   1 
ATOM   25    C  CA  . GLY A  1 8   ? 22.911  0.695   17.017  1.00 49.18 ? 25   GLY A CA  1 
ATOM   26    C  C   . GLY A  1 8   ? 23.465  -0.253  15.958  1.00 48.44 ? 25   GLY A C   1 
ATOM   27    O  O   . GLY A  1 8   ? 22.705  -0.866  15.210  1.00 49.66 ? 25   GLY A O   1 
ATOM   28    N  N   . LYS A  1 9   ? 24.798  -0.364  15.913  1.00 45.58 ? 26   LYS A N   1 
ATOM   29    C  CA  . LYS A  1 9   ? 25.479  -1.194  14.935  1.00 44.16 ? 26   LYS A CA  1 
ATOM   30    C  C   . LYS A  1 9   ? 25.667  -2.591  15.525  1.00 43.70 ? 26   LYS A C   1 
ATOM   31    O  O   . LYS A  1 9   ? 26.351  -2.744  16.536  1.00 40.89 ? 26   LYS A O   1 
ATOM   32    C  CB  . LYS A  1 9   ? 26.805  -0.537  14.537  1.00 42.39 ? 26   LYS A CB  1 
ATOM   33    N  N   . PRO A  1 10  ? 25.047  -3.644  14.935  1.00 44.32 ? 27   PRO A N   1 
ATOM   34    C  CA  . PRO A  1 10  ? 25.132  -5.006  15.477  1.00 44.19 ? 27   PRO A CA  1 
ATOM   35    C  C   . PRO A  1 10  ? 26.530  -5.539  15.790  1.00 41.17 ? 27   PRO A C   1 
ATOM   36    O  O   . PRO A  1 10  ? 26.700  -6.271  16.760  1.00 41.71 ? 27   PRO A O   1 
ATOM   37    C  CB  . PRO A  1 10  ? 24.447  -5.843  14.377  1.00 44.94 ? 27   PRO A CB  1 
ATOM   38    C  CG  . PRO A  1 10  ? 23.444  -4.891  13.778  1.00 46.04 ? 27   PRO A CG  1 
ATOM   39    C  CD  . PRO A  1 10  ? 24.191  -3.569  13.738  1.00 44.66 ? 27   PRO A CD  1 
ATOM   40    N  N   . LEU A  1 11  ? 27.522  -5.171  14.969  1.00 39.39 ? 28   LEU A N   1 
ATOM   41    C  CA  . LEU A  1 11  ? 28.883  -5.663  15.139  1.00 37.78 ? 28   LEU A CA  1 
ATOM   42    C  C   . LEU A  1 11  ? 29.462  -5.184  16.472  1.00 35.41 ? 28   LEU A C   1 
ATOM   43    O  O   . LEU A  1 11  ? 30.278  -5.875  17.078  1.00 34.67 ? 28   LEU A O   1 
ATOM   44    C  CB  . LEU A  1 11  ? 29.749  -5.244  13.950  1.00 38.27 ? 28   LEU A CB  1 
ATOM   45    C  CG  . LEU A  1 11  ? 29.399  -5.892  12.606  1.00 40.97 ? 28   LEU A CG  1 
ATOM   46    C  CD1 . LEU A  1 11  ? 30.169  -5.247  11.468  1.00 42.84 ? 28   LEU A CD1 1 
ATOM   47    C  CD2 . LEU A  1 11  ? 29.658  -7.393  12.625  1.00 41.99 ? 28   LEU A CD2 1 
ATOM   48    N  N   . MET A  1 12  ? 29.018  -4.007  16.926  1.00 31.55 ? 29   MET A N   1 
ATOM   49    C  CA  . MET A  1 12  ? 29.480  -3.409  18.168  1.00 30.52 ? 29   MET A CA  1 
ATOM   50    C  C   . MET A  1 12  ? 28.708  -3.986  19.357  1.00 28.76 ? 29   MET A C   1 
ATOM   51    O  O   . MET A  1 12  ? 29.265  -4.203  20.433  1.00 27.82 ? 29   MET A O   1 
ATOM   52    C  CB  . MET A  1 12  ? 29.252  -1.897  18.085  1.00 32.92 ? 29   MET A CB  1 
ATOM   53    C  CG  . MET A  1 12  ? 30.097  -1.072  19.004  1.00 34.84 ? 29   MET A CG  1 
ATOM   54    S  SD  . MET A  1 12  ? 29.699  0.683   18.838  1.00 35.03 ? 29   MET A SD  1 
ATOM   55    C  CE  . MET A  1 12  ? 30.716  1.165   20.238  1.00 34.09 ? 29   MET A CE  1 
ATOM   56    N  N   . LEU A  1 13  ? 27.404  -4.217  19.160  1.00 27.95 ? 30   LEU A N   1 
ATOM   57    C  CA  . LEU A  1 13  ? 26.506  -4.612  20.235  1.00 27.36 ? 30   LEU A CA  1 
ATOM   58    C  C   . LEU A  1 13  ? 26.622  -6.108  20.529  1.00 26.49 ? 30   LEU A C   1 
ATOM   59    O  O   . LEU A  1 13  ? 26.345  -6.543  21.641  1.00 26.98 ? 30   LEU A O   1 
ATOM   60    C  CB  . LEU A  1 13  ? 25.083  -4.241  19.823  1.00 27.94 ? 30   LEU A CB  1 
ATOM   61    C  CG  . LEU A  1 13  ? 24.797  -2.746  19.649  1.00 29.50 ? 30   LEU A CG  1 
ATOM   62    C  CD1 . LEU A  1 13  ? 23.353  -2.542  19.227  1.00 30.64 ? 30   LEU A CD1 1 
ATOM   63    C  CD2 . LEU A  1 13  ? 25.099  -1.963  20.917  1.00 30.14 ? 30   LEU A CD2 1 
ATOM   64    N  N   . ASN A  1 14  ? 26.999  -6.891  19.516  1.00 26.27 ? 31   ASN A N   1 
ATOM   65    C  CA  . ASN A  1 14  ? 27.098  -8.336  19.646  1.00 26.14 ? 31   ASN A CA  1 
ATOM   66    C  C   . ASN A  1 14  ? 28.456  -8.693  20.244  1.00 24.76 ? 31   ASN A C   1 
ATOM   67    O  O   . ASN A  1 14  ? 29.482  -8.482  19.600  1.00 23.37 ? 31   ASN A O   1 
ATOM   68    C  CB  . ASN A  1 14  ? 26.892  -9.000  18.291  1.00 27.03 ? 31   ASN A CB  1 
ATOM   69    C  CG  . ASN A  1 14  ? 27.026  -10.503 18.334  1.00 27.55 ? 31   ASN A CG  1 
ATOM   70    O  OD1 . ASN A  1 14  ? 27.269  -11.091 19.394  1.00 27.45 ? 31   ASN A OD1 1 
ATOM   71    N  ND2 . ASN A  1 14  ? 26.884  -11.136 17.180  1.00 29.53 ? 31   ASN A ND2 1 
ATOM   72    N  N   . PRO A  1 15  ? 28.519  -9.263  21.468  1.00 24.84 ? 32   PRO A N   1 
ATOM   73    C  CA  . PRO A  1 15  ? 29.807  -9.588  22.087  1.00 24.95 ? 32   PRO A CA  1 
ATOM   74    C  C   . PRO A  1 15  ? 30.664  -10.567 21.286  1.00 24.29 ? 32   PRO A C   1 
ATOM   75    O  O   . PRO A  1 15  ? 31.876  -10.621 21.470  1.00 23.37 ? 32   PRO A O   1 
ATOM   76    C  CB  . PRO A  1 15  ? 29.445  -10.133 23.482  1.00 25.80 ? 32   PRO A CB  1 
ATOM   77    C  CG  . PRO A  1 15  ? 27.976  -10.486 23.397  1.00 27.20 ? 32   PRO A CG  1 
ATOM   78    C  CD  . PRO A  1 15  ? 27.372  -9.605  22.322  1.00 26.56 ? 32   PRO A CD  1 
ATOM   79    N  N   . ARG A  1 16  ? 30.034  -11.320 20.380  1.00 25.14 ? 33   ARG A N   1 
ATOM   80    C  CA  . ARG A  1 16  ? 30.739  -12.295 19.567  1.00 26.27 ? 33   ARG A CA  1 
ATOM   81    C  C   . ARG A  1 16  ? 31.626  -11.600 18.533  1.00 24.64 ? 33   ARG A C   1 
ATOM   82    O  O   . ARG A  1 16  ? 32.692  -12.116 18.203  1.00 24.89 ? 33   ARG A O   1 
ATOM   83    C  CB  . ARG A  1 16  ? 29.704  -13.235 18.943  1.00 28.92 ? 33   ARG A CB  1 
ATOM   84    C  CG  . ARG A  1 16  ? 30.277  -14.468 18.263  1.00 32.68 ? 33   ARG A CG  1 
ATOM   85    C  CD  . ARG A  1 16  ? 29.373  -15.683 18.479  1.00 35.23 ? 33   ARG A CD  1 
ATOM   86    N  NE  . ARG A  1 16  ? 29.536  -16.252 19.824  1.00 37.22 ? 33   ARG A NE  1 
ATOM   87    C  CZ  . ARG A  1 16  ? 28.581  -16.686 20.652  1.00 37.86 ? 33   ARG A CZ  1 
ATOM   88    N  NH1 . ARG A  1 16  ? 27.310  -16.679 20.292  1.00 39.86 ? 33   ARG A NH1 1 
ATOM   89    N  NH2 . ARG A  1 16  ? 28.912  -17.160 21.841  1.00 35.60 ? 33   ARG A NH2 1 
ATOM   90    N  N   . THR A  1 17  ? 31.189  -10.440 18.024  1.00 23.87 ? 34   THR A N   1 
ATOM   91    C  CA  . THR A  1 17  ? 31.913  -9.739  16.971  1.00 24.15 ? 34   THR A CA  1 
ATOM   92    C  C   . THR A  1 17  ? 32.600  -8.478  17.506  1.00 23.13 ? 34   THR A C   1 
ATOM   93    O  O   . THR A  1 17  ? 33.564  -8.021  16.899  1.00 22.71 ? 34   THR A O   1 
ATOM   94    C  CB  . THR A  1 17  ? 30.975  -9.408  15.808  1.00 24.55 ? 34   THR A CB  1 
ATOM   95    O  OG1 . THR A  1 17  ? 29.901  -8.640  16.341  1.00 24.35 ? 34   THR A OG1 1 
ATOM   96    C  CG2 . THR A  1 17  ? 30.436  -10.650 15.121  1.00 25.90 ? 34   THR A CG2 1 
ATOM   97    N  N   . ASN A  1 18  ? 32.130  -7.942  18.644  1.00 21.66 ? 35   ASN A N   1 
ATOM   98    C  CA  . ASN A  1 18  ? 32.599  -6.668  19.178  1.00 20.80 ? 35   ASN A CA  1 
ATOM   99    C  C   . ASN A  1 18  ? 34.088  -6.711  19.521  1.00 20.64 ? 35   ASN A C   1 
ATOM   100   O  O   . ASN A  1 18  ? 34.558  -7.631  20.186  1.00 21.04 ? 35   ASN A O   1 
ATOM   101   C  CB  . ASN A  1 18  ? 31.792  -6.257  20.402  1.00 21.03 ? 35   ASN A CB  1 
ATOM   102   C  CG  . ASN A  1 18  ? 32.277  -4.973  21.034  1.00 20.81 ? 35   ASN A CG  1 
ATOM   103   O  OD1 . ASN A  1 18  ? 32.588  -4.002  20.334  1.00 21.38 ? 35   ASN A OD1 1 
ATOM   104   N  ND2 . ASN A  1 18  ? 32.343  -4.946  22.354  1.00 20.28 ? 35   ASN A ND2 1 
ATOM   105   N  N   . LYS A  1 19  ? 34.813  -5.678  19.075  1.00 20.70 ? 36   LYS A N   1 
ATOM   106   C  CA  . LYS A  1 19  ? 36.240  -5.534  19.327  1.00 21.51 ? 36   LYS A CA  1 
ATOM   107   C  C   . LYS A  1 19  ? 36.510  -4.329  20.230  1.00 20.67 ? 36   LYS A C   1 
ATOM   108   O  O   . LYS A  1 19  ? 37.651  -4.108  20.630  1.00 20.70 ? 36   LYS A O   1 
ATOM   109   C  CB  . LYS A  1 19  ? 36.991  -5.382  17.997  1.00 22.53 ? 36   LYS A CB  1 
ATOM   110   C  CG  . LYS A  1 19  ? 36.933  -6.602  17.082  1.00 23.88 ? 36   LYS A CG  1 
ATOM   111   C  CD  . LYS A  1 19  ? 37.340  -6.373  15.629  1.00 26.12 ? 36   LYS A CD  1 
ATOM   112   C  CE  . LYS A  1 19  ? 38.727  -5.870  15.461  1.00 28.12 ? 36   LYS A CE  1 
ATOM   113   N  NZ  . LYS A  1 19  ? 39.141  -5.933  14.057  1.00 28.95 ? 36   LYS A NZ  1 
ATOM   114   N  N   . GLY A  1 20  ? 35.471  -3.542  20.534  1.00 20.22 ? 37   GLY A N   1 
ATOM   115   C  CA  . GLY A  1 20  ? 35.628  -2.362  21.372  1.00 20.01 ? 37   GLY A CA  1 
ATOM   116   C  C   . GLY A  1 20  ? 36.665  -1.410  20.775  1.00 19.95 ? 37   GLY A C   1 
ATOM   117   O  O   . GLY A  1 20  ? 36.625  -1.122  19.584  1.00 19.75 ? 37   GLY A O   1 
ATOM   118   N  N   . MET A  1 21  ? 37.627  -0.973  21.591  1.00 20.77 ? 38   MET A N   1 
ATOM   119   C  CA  . MET A  1 21  ? 38.615  -0.004  21.135  1.00 23.24 ? 38   MET A CA  1 
ATOM   120   C  C   . MET A  1 21  ? 39.629  -0.612  20.160  1.00 22.24 ? 38   MET A C   1 
ATOM   121   O  O   . MET A  1 21  ? 40.465  0.119   19.637  1.00 22.04 ? 38   MET A O   1 
ATOM   122   C  CB  . MET A  1 21  ? 39.321  0.643   22.327  1.00 26.29 ? 38   MET A CB  1 
ATOM   123   C  CG  . MET A  1 21  ? 38.478  1.743   22.949  1.00 29.44 ? 38   MET A CG  1 
ATOM   124   S  SD  . MET A  1 21  ? 39.324  2.651   24.250  1.00 36.18 ? 38   MET A SD  1 
ATOM   125   C  CE  . MET A  1 21  ? 39.556  1.364   25.483  1.00 37.22 ? 38   MET A CE  1 
ATOM   126   N  N   . ALA A  1 22  ? 39.541  -1.924  19.883  1.00 20.89 ? 39   ALA A N   1 
ATOM   127   C  CA  . ALA A  1 22  ? 40.408  -2.553  18.896  1.00 20.22 ? 39   ALA A CA  1 
ATOM   128   C  C   . ALA A  1 22  ? 39.836  -2.462  17.480  1.00 19.40 ? 39   ALA A C   1 
ATOM   129   O  O   . ALA A  1 22  ? 40.522  -2.815  16.529  1.00 19.53 ? 39   ALA A O   1 
ATOM   130   C  CB  . ALA A  1 22  ? 40.697  -3.987  19.280  1.00 20.53 ? 39   ALA A CB  1 
ATOM   131   N  N   . PHE A  1 23  ? 38.597  -1.986  17.316  1.00 18.43 ? 40   PHE A N   1 
ATOM   132   C  CA  . PHE A  1 23  ? 38.132  -1.607  15.993  1.00 18.69 ? 40   PHE A CA  1 
ATOM   133   C  C   . PHE A  1 23  ? 39.110  -0.581  15.423  1.00 18.59 ? 40   PHE A C   1 
ATOM   134   O  O   . PHE A  1 23  ? 39.424  0.400   16.089  1.00 18.51 ? 40   PHE A O   1 
ATOM   135   C  CB  . PHE A  1 23  ? 36.706  -1.041  15.998  1.00 19.01 ? 40   PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 23  ? 35.576  -2.062  16.056  1.00 19.07 ? 40   PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 23  ? 35.349  -2.934  14.996  1.00 20.23 ? 40   PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 23  ? 34.712  -2.111  17.143  1.00 19.90 ? 40   PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 23  ? 34.314  -3.855  15.045  1.00 20.32 ? 40   PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 23  ? 33.665  -3.020  17.182  1.00 20.43 ? 40   PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 23  ? 33.469  -3.886  16.134  1.00 20.50 ? 40   PHE A CZ  1 
ATOM   142   N  N   . THR A  1 24  ? 39.592  -0.809  14.192  1.00 18.44 ? 41   THR A N   1 
ATOM   143   C  CA  . THR A  1 24  ? 40.561  0.085   13.576  1.00 19.14 ? 41   THR A CA  1 
ATOM   144   C  C   . THR A  1 24  ? 39.827  1.347   13.130  1.00 19.72 ? 41   THR A C   1 
ATOM   145   O  O   . THR A  1 24  ? 38.602  1.356   13.056  1.00 19.37 ? 41   THR A O   1 
ATOM   146   C  CB  . THR A  1 24  ? 41.287  -0.574  12.398  1.00 19.84 ? 41   THR A CB  1 
ATOM   147   O  OG1 . THR A  1 24  ? 40.339  -0.714  11.348  1.00 19.39 ? 41   THR A OG1 1 
ATOM   148   C  CG2 . THR A  1 24  ? 41.895  -1.926  12.736  1.00 20.32 ? 41   THR A CG2 1 
ATOM   149   N  N   . LEU A  1 25  ? 40.585  2.406   12.827  1.00 20.42 ? 42   LEU A N   1 
ATOM   150   C  CA  . LEU A  1 25  ? 40.000  3.650   12.354  1.00 21.74 ? 42   LEU A CA  1 
ATOM   151   C  C   . LEU A  1 25  ? 39.141  3.387   11.117  1.00 21.84 ? 42   LEU A C   1 
ATOM   152   O  O   . LEU A  1 25  ? 38.012  3.877   11.035  1.00 19.21 ? 42   LEU A O   1 
ATOM   153   C  CB  . LEU A  1 25  ? 41.082  4.694   12.068  1.00 22.41 ? 42   LEU A CB  1 
ATOM   154   C  CG  . LEU A  1 25  ? 40.577  6.061   11.587  1.00 22.42 ? 42   LEU A CG  1 
ATOM   155   C  CD1 . LEU A  1 25  ? 39.629  6.701   12.590  1.00 22.48 ? 42   LEU A CD1 1 
ATOM   156   C  CD2 . LEU A  1 25  ? 41.747  6.996   11.316  1.00 22.48 ? 42   LEU A CD2 1 
ATOM   157   N  N   . GLN A  1 26  ? 39.681  2.620   10.155  1.00 22.53 ? 43   GLN A N   1 
ATOM   158   C  CA  . GLN A  1 26  ? 38.961  2.347   8.919   1.00 24.37 ? 43   GLN A CA  1 
ATOM   159   C  C   . GLN A  1 26  ? 37.716  1.502   9.191   1.00 22.17 ? 43   GLN A C   1 
ATOM   160   O  O   . GLN A  1 26  ? 36.676  1.736   8.576   1.00 22.10 ? 43   GLN A O   1 
ATOM   161   C  CB  . GLN A  1 26  ? 39.795  1.663   7.832   1.00 28.90 ? 43   GLN A CB  1 
ATOM   162   C  CG  . GLN A  1 26  ? 40.750  2.590   7.089   1.00 33.23 ? 43   GLN A CG  1 
ATOM   163   C  CD  . GLN A  1 26  ? 40.778  2.345   5.593   1.00 38.36 ? 43   GLN A CD  1 
ATOM   164   O  OE1 . GLN A  1 26  ? 40.979  1.220   5.120   1.00 38.09 ? 43   GLN A OE1 1 
ATOM   165   N  NE2 . GLN A  1 26  ? 40.555  3.403   4.824   1.00 43.25 ? 43   GLN A NE2 1 
ATOM   166   N  N   . GLU A  1 27  ? 37.824  0.518   10.092  1.00 20.71 ? 44   GLU A N   1 
ATOM   167   C  CA  . GLU A  1 27  ? 36.676  -0.305  10.450  1.00 20.08 ? 44   GLU A CA  1 
ATOM   168   C  C   . GLU A  1 27  ? 35.572  0.576   11.028  1.00 19.82 ? 44   GLU A C   1 
ATOM   169   O  O   . GLU A  1 27  ? 34.408  0.440   10.652  1.00 20.99 ? 44   GLU A O   1 
ATOM   170   C  CB  . GLU A  1 27  ? 37.038  -1.403  11.450  1.00 20.62 ? 44   GLU A CB  1 
ATOM   171   C  CG  . GLU A  1 27  ? 37.747  -2.596  10.813  1.00 21.38 ? 44   GLU A CG  1 
ATOM   172   C  CD  . GLU A  1 27  ? 38.297  -3.613  11.803  1.00 21.57 ? 44   GLU A CD  1 
ATOM   173   O  OE1 . GLU A  1 27  ? 38.423  -3.295  13.003  1.00 20.76 ? 44   GLU A OE1 1 
ATOM   174   O  OE2 . GLU A  1 27  ? 38.590  -4.748  11.371  1.00 22.54 ? 44   GLU A OE2 1 
ATOM   175   N  N   . ARG A  1 28  ? 35.947  1.470   11.951  1.00 19.48 ? 45   ARG A N   1 
ATOM   176   C  CA  . ARG A  1 28  ? 34.989  2.350   12.598  1.00 19.15 ? 45   ARG A CA  1 
ATOM   177   C  C   . ARG A  1 28  ? 34.271  3.218   11.570  1.00 19.24 ? 45   ARG A C   1 
ATOM   178   O  O   . ARG A  1 28  ? 33.052  3.372   11.636  1.00 18.55 ? 45   ARG A O   1 
ATOM   179   C  CB  . ARG A  1 28  ? 35.646  3.232   13.664  1.00 18.72 ? 45   ARG A CB  1 
ATOM   180   C  CG  . ARG A  1 28  ? 36.202  2.481   14.863  1.00 18.51 ? 45   ARG A CG  1 
ATOM   181   C  CD  . ARG A  1 28  ? 36.899  3.428   15.809  1.00 18.78 ? 45   ARG A CD  1 
ATOM   182   N  NE  . ARG A  1 28  ? 37.710  2.733   16.813  1.00 19.84 ? 45   ARG A NE  1 
ATOM   183   C  CZ  . ARG A  1 28  ? 38.180  3.283   17.929  1.00 20.23 ? 45   ARG A CZ  1 
ATOM   184   N  NH1 . ARG A  1 28  ? 37.903  4.540   18.226  1.00 20.04 ? 45   ARG A NH1 1 
ATOM   185   N  NH2 . ARG A  1 28  ? 38.914  2.564   18.761  1.00 21.45 ? 45   ARG A NH2 1 
ATOM   186   N  N   . GLN A  1 29  ? 35.022  3.791   10.625  1.00 19.65 ? 46   GLN A N   1 
ATOM   187   C  CA  . GLN A  1 29  ? 34.430  4.710   9.664   1.00 20.92 ? 46   GLN A CA  1 
ATOM   188   C  C   . GLN A  1 29  ? 33.491  3.957   8.719   1.00 22.00 ? 46   GLN A C   1 
ATOM   189   O  O   . GLN A  1 29  ? 32.366  4.393   8.474   1.00 21.19 ? 46   GLN A O   1 
ATOM   190   C  CB  . GLN A  1 29  ? 35.541  5.475   8.943   1.00 20.61 ? 46   GLN A CB  1 
ATOM   191   C  CG  . GLN A  1 29  ? 36.234  6.505   9.829   1.00 21.00 ? 46   GLN A CG  1 
ATOM   192   C  CD  . GLN A  1 29  ? 37.420  7.167   9.166   1.00 22.30 ? 46   GLN A CD  1 
ATOM   193   O  OE1 . GLN A  1 29  ? 37.913  6.723   8.121   1.00 22.39 ? 46   GLN A OE1 1 
ATOM   194   N  NE2 . GLN A  1 29  ? 37.907  8.232   9.784   1.00 22.22 ? 46   GLN A NE2 1 
ATOM   195   N  N   . MET A  1 30  ? 33.945  2.812   8.206   1.00 22.53 ? 47   MET A N   1 
ATOM   196   C  CA  . MET A  1 30  ? 33.201  2.107   7.173   1.00 23.38 ? 47   MET A CA  1 
ATOM   197   C  C   . MET A  1 30  ? 31.953  1.443   7.757   1.00 23.40 ? 47   MET A C   1 
ATOM   198   O  O   . MET A  1 30  ? 30.954  1.307   7.049   1.00 23.62 ? 47   MET A O   1 
ATOM   199   C  CB  . MET A  1 30  ? 34.078  1.067   6.469   1.00 24.70 ? 47   MET A CB  1 
ATOM   200   C  CG  . MET A  1 30  ? 35.100  1.673   5.525   1.00 27.65 ? 47   MET A CG  1 
ATOM   201   S  SD  . MET A  1 30  ? 35.864  0.451   4.436   1.00 31.04 ? 47   MET A SD  1 
ATOM   202   C  CE  . MET A  1 30  ? 37.209  1.410   3.722   1.00 31.54 ? 47   MET A CE  1 
ATOM   203   N  N   . LEU A  1 31  ? 32.006  1.056   9.040   1.00 22.40 ? 48   LEU A N   1 
ATOM   204   C  CA  . LEU A  1 31  ? 30.917  0.329   9.677   1.00 23.80 ? 48   LEU A CA  1 
ATOM   205   C  C   . LEU A  1 31  ? 30.001  1.259   10.474  1.00 23.72 ? 48   LEU A C   1 
ATOM   206   O  O   . LEU A  1 31  ? 29.068  0.782   11.116  1.00 24.37 ? 48   LEU A O   1 
ATOM   207   C  CB  . LEU A  1 31  ? 31.493  -0.774  10.566  1.00 23.98 ? 48   LEU A CB  1 
ATOM   208   C  CG  . LEU A  1 31  ? 32.370  -1.809  9.854   1.00 25.01 ? 48   LEU A CG  1 
ATOM   209   C  CD1 . LEU A  1 31  ? 33.041  -2.739  10.851  1.00 25.70 ? 48   LEU A CD1 1 
ATOM   210   C  CD2 . LEU A  1 31  ? 31.557  -2.590  8.834   1.00 26.14 ? 48   LEU A CD2 1 
ATOM   211   N  N   . GLY A  1 32  ? 30.263  2.572   10.443  1.00 22.84 ? 49   GLY A N   1 
ATOM   212   C  CA  . GLY A  1 32  ? 29.403  3.551   11.090  1.00 22.94 ? 49   GLY A CA  1 
ATOM   213   C  C   . GLY A  1 32  ? 29.560  3.581   12.612  1.00 22.73 ? 49   GLY A C   1 
ATOM   214   O  O   . GLY A  1 32  ? 28.595  3.863   13.324  1.00 23.21 ? 49   GLY A O   1 
ATOM   215   N  N   . LEU A  1 33  ? 30.781  3.317   13.105  1.00 20.87 ? 50   LEU A N   1 
ATOM   216   C  CA  . LEU A  1 33  ? 31.069  3.315   14.531  1.00 20.77 ? 50   LEU A CA  1 
ATOM   217   C  C   . LEU A  1 33  ? 31.836  4.571   14.942  1.00 20.35 ? 50   LEU A C   1 
ATOM   218   O  O   . LEU A  1 33  ? 32.079  4.773   16.129  1.00 19.50 ? 50   LEU A O   1 
ATOM   219   C  CB  . LEU A  1 33  ? 31.879  2.078   14.907  1.00 21.72 ? 50   LEU A CB  1 
ATOM   220   C  CG  . LEU A  1 33  ? 31.347  0.731   14.412  1.00 22.66 ? 50   LEU A CG  1 
ATOM   221   C  CD1 . LEU A  1 33  ? 32.274  -0.368  14.889  1.00 23.03 ? 50   LEU A CD1 1 
ATOM   222   C  CD2 . LEU A  1 33  ? 29.934  0.475   14.889  1.00 23.61 ? 50   LEU A CD2 1 
ATOM   223   N  N   . GLN A  1 34  ? 32.257  5.389   13.970  1.00 20.86 ? 51   GLN A N   1 
ATOM   224   C  CA  . GLN A  1 34  ? 33.104  6.533   14.264  1.00 21.01 ? 51   GLN A CA  1 
ATOM   225   C  C   . GLN A  1 34  ? 32.362  7.467   15.214  1.00 21.04 ? 51   GLN A C   1 
ATOM   226   O  O   . GLN A  1 34  ? 31.230  7.861   14.945  1.00 20.24 ? 51   GLN A O   1 
ATOM   227   C  CB  . GLN A  1 34  ? 33.507  7.231   12.965  1.00 22.28 ? 51   GLN A CB  1 
ATOM   228   C  CG  . GLN A  1 34  ? 34.499  8.377   13.143  1.00 23.47 ? 51   GLN A CG  1 
ATOM   229   C  CD  . GLN A  1 34  ? 35.897  7.938   13.521  1.00 23.95 ? 51   GLN A CD  1 
ATOM   230   O  OE1 . GLN A  1 34  ? 36.170  6.760   13.769  1.00 23.88 ? 51   GLN A OE1 1 
ATOM   231   N  NE2 . GLN A  1 34  ? 36.810  8.898   13.580  1.00 26.10 ? 51   GLN A NE2 1 
ATOM   232   N  N   . GLY A  1 35  ? 33.003  7.781   16.342  1.00 22.06 ? 52   GLY A N   1 
ATOM   233   C  CA  . GLY A  1 35  ? 32.421  8.658   17.343  1.00 22.65 ? 52   GLY A CA  1 
ATOM   234   C  C   . GLY A  1 35  ? 31.710  7.898   18.464  1.00 22.15 ? 52   GLY A C   1 
ATOM   235   O  O   . GLY A  1 35  ? 31.378  8.494   19.483  1.00 22.84 ? 52   GLY A O   1 
ATOM   236   N  N   . LEU A  1 36  ? 31.475  6.591   18.277  1.00 21.63 ? 53   LEU A N   1 
ATOM   237   C  CA  . LEU A  1 36  ? 30.804  5.781   19.282  1.00 21.65 ? 53   LEU A CA  1 
ATOM   238   C  C   . LEU A  1 36  ? 31.831  5.151   20.215  1.00 21.94 ? 53   LEU A C   1 
ATOM   239   O  O   . LEU A  1 36  ? 31.455  4.517   21.201  1.00 23.33 ? 53   LEU A O   1 
ATOM   240   C  CB  . LEU A  1 36  ? 29.926  4.729   18.604  1.00 22.93 ? 53   LEU A CB  1 
ATOM   241   C  CG  . LEU A  1 36  ? 28.859  5.262   17.640  1.00 23.40 ? 53   LEU A CG  1 
ATOM   242   C  CD1 . LEU A  1 36  ? 27.929  4.151   17.171  1.00 23.99 ? 53   LEU A CD1 1 
ATOM   243   C  CD2 . LEU A  1 36  ? 28.054  6.380   18.271  1.00 23.81 ? 53   LEU A CD2 1 
ATOM   244   N  N   . LEU A  1 37  ? 33.122  5.340   19.892  1.00 21.11 ? 54   LEU A N   1 
ATOM   245   C  CA  . LEU A  1 37  ? 34.231  4.854   20.696  1.00 21.43 ? 54   LEU A CA  1 
ATOM   246   C  C   . LEU A  1 37  ? 35.194  6.010   20.950  1.00 21.41 ? 54   LEU A C   1 
ATOM   247   O  O   . LEU A  1 37  ? 35.261  6.938   20.147  1.00 20.72 ? 54   LEU A O   1 
ATOM   248   C  CB  . LEU A  1 37  ? 34.941  3.716   19.966  1.00 21.86 ? 54   LEU A CB  1 
ATOM   249   C  CG  . LEU A  1 37  ? 34.148  2.413   19.834  1.00 22.75 ? 54   LEU A CG  1 
ATOM   250   C  CD1 . LEU A  1 37  ? 34.669  1.607   18.652  1.00 23.58 ? 54   LEU A CD1 1 
ATOM   251   C  CD2 . LEU A  1 37  ? 34.213  1.613   21.127  1.00 22.87 ? 54   LEU A CD2 1 
ATOM   252   N  N   . PRO A  1 38  ? 35.962  5.987   22.060  1.00 22.17 ? 55   PRO A N   1 
ATOM   253   C  CA  . PRO A  1 38  ? 36.967  7.020   22.325  1.00 23.87 ? 55   PRO A CA  1 
ATOM   254   C  C   . PRO A  1 38  ? 37.988  7.086   21.190  1.00 24.28 ? 55   PRO A C   1 
ATOM   255   O  O   . PRO A  1 38  ? 38.233  6.084   20.522  1.00 23.36 ? 55   PRO A O   1 
ATOM   256   C  CB  . PRO A  1 38  ? 37.623  6.607   23.651  1.00 23.76 ? 55   PRO A CB  1 
ATOM   257   C  CG  . PRO A  1 38  ? 36.707  5.567   24.245  1.00 24.23 ? 55   PRO A CG  1 
ATOM   258   C  CD  . PRO A  1 38  ? 35.927  4.949   23.099  1.00 22.96 ? 55   PRO A CD  1 
ATOM   259   N  N   . PRO A  1 39  ? 38.629  8.253   20.955  1.00 26.43 ? 56   PRO A N   1 
ATOM   260   C  CA  . PRO A  1 39  ? 39.518  8.424   19.807  1.00 27.93 ? 56   PRO A CA  1 
ATOM   261   C  C   . PRO A  1 39  ? 40.915  7.841   19.999  1.00 29.56 ? 56   PRO A C   1 
ATOM   262   O  O   . PRO A  1 39  ? 41.915  8.530   19.822  1.00 34.33 ? 56   PRO A O   1 
ATOM   263   C  CB  . PRO A  1 39  ? 39.518  9.948   19.654  1.00 29.13 ? 56   PRO A CB  1 
ATOM   264   C  CG  . PRO A  1 39  ? 39.414  10.454  21.068  1.00 28.99 ? 56   PRO A CG  1 
ATOM   265   C  CD  . PRO A  1 39  ? 38.503  9.473   21.770  1.00 28.03 ? 56   PRO A CD  1 
ATOM   266   N  N   . LYS A  1 40  ? 40.955  6.559   20.361  1.00 28.77 ? 57   LYS A N   1 
ATOM   267   C  CA  . LYS A  1 40  ? 42.192  5.814   20.497  1.00 29.52 ? 57   LYS A CA  1 
ATOM   268   C  C   . LYS A  1 40  ? 41.952  4.393   19.995  1.00 27.93 ? 57   LYS A C   1 
ATOM   269   O  O   . LYS A  1 40  ? 40.941  3.777   20.332  1.00 24.57 ? 57   LYS A O   1 
ATOM   270   C  CB  . LYS A  1 40  ? 42.666  5.764   21.948  1.00 30.46 ? 57   LYS A CB  1 
ATOM   271   C  CG  . LYS A  1 40  ? 44.098  5.268   22.104  1.00 32.06 ? 57   LYS A CG  1 
ATOM   272   C  CD  . LYS A  1 40  ? 44.272  4.497   23.397  1.00 31.15 ? 57   LYS A CD  1 
ATOM   273   C  CE  . LYS A  1 40  ? 45.668  4.045   23.654  1.00 29.31 ? 57   LYS A CE  1 
ATOM   274   N  NZ  . LYS A  1 40  ? 45.712  3.465   24.995  1.00 29.26 ? 57   LYS A NZ  1 
ATOM   275   N  N   . ILE A  1 41  ? 42.888  3.913   19.166  1.00 27.20 ? 58   ILE A N   1 
ATOM   276   C  CA  . ILE A  1 41  ? 42.837  2.582   18.589  1.00 26.50 ? 58   ILE A CA  1 
ATOM   277   C  C   . ILE A  1 41  ? 43.808  1.718   19.384  1.00 27.03 ? 58   ILE A C   1 
ATOM   278   O  O   . ILE A  1 41  ? 44.987  2.050   19.451  1.00 27.24 ? 58   ILE A O   1 
ATOM   279   C  CB  . ILE A  1 41  ? 43.222  2.601   17.095  1.00 26.70 ? 58   ILE A CB  1 
ATOM   280   C  CG1 . ILE A  1 41  ? 42.585  3.760   16.314  1.00 27.92 ? 58   ILE A CG1 1 
ATOM   281   C  CG2 . ILE A  1 41  ? 42.929  1.250   16.441  1.00 26.71 ? 58   ILE A CG2 1 
ATOM   282   C  CD1 . ILE A  1 41  ? 41.073  3.798   16.352  1.00 28.63 ? 58   ILE A CD1 1 
ATOM   283   N  N   . GLU A  1 42  ? 43.310  0.629   19.982  1.00 25.92 ? 59   GLU A N   1 
ATOM   284   C  CA  . GLU A  1 42  ? 44.147  -0.259  20.770  1.00 27.01 ? 59   GLU A CA  1 
ATOM   285   C  C   . GLU A  1 42  ? 44.232  -1.622  20.091  1.00 26.10 ? 59   GLU A C   1 
ATOM   286   O  O   . GLU A  1 42  ? 43.424  -1.945  19.231  1.00 26.13 ? 59   GLU A O   1 
ATOM   287   C  CB  . GLU A  1 42  ? 43.602  -0.397  22.191  1.00 28.35 ? 59   GLU A CB  1 
ATOM   288   C  CG  . GLU A  1 42  ? 43.714  0.896   22.991  1.00 29.99 ? 59   GLU A CG  1 
ATOM   289   C  CD  . GLU A  1 42  ? 43.265  0.813   24.436  1.00 30.12 ? 59   GLU A CD  1 
ATOM   290   O  OE1 . GLU A  1 42  ? 42.566  -0.154  24.808  1.00 32.32 ? 59   GLU A OE1 1 
ATOM   291   O  OE2 . GLU A  1 42  ? 43.638  1.729   25.196  1.00 30.54 ? 59   GLU A OE2 1 
ATOM   292   N  N   . THR A  1 43  ? 45.249  -2.400  20.467  1.00 25.84 ? 60   THR A N   1 
ATOM   293   C  CA  . THR A  1 43  ? 45.328  -3.803  20.096  1.00 25.47 ? 60   THR A CA  1 
ATOM   294   C  C   . THR A  1 43  ? 44.709  -4.622  21.223  1.00 23.99 ? 60   THR A C   1 
ATOM   295   O  O   . THR A  1 43  ? 44.529  -4.124  22.327  1.00 24.63 ? 60   THR A O   1 
ATOM   296   C  CB  . THR A  1 43  ? 46.784  -4.200  19.865  1.00 25.71 ? 60   THR A CB  1 
ATOM   297   O  OG1 . THR A  1 43  ? 47.435  -3.928  21.102  1.00 26.68 ? 60   THR A OG1 1 
ATOM   298   C  CG2 . THR A  1 43  ? 47.437  -3.428  18.735  1.00 27.52 ? 60   THR A CG2 1 
ATOM   299   N  N   . GLN A  1 44  ? 44.433  -5.897  20.949  1.00 24.25 ? 61   GLN A N   1 
ATOM   300   C  CA  . GLN A  1 44  ? 43.968  -6.813  21.978  1.00 24.63 ? 61   GLN A CA  1 
ATOM   301   C  C   . GLN A  1 44  ? 44.988  -6.901  23.116  1.00 25.64 ? 61   GLN A C   1 
ATOM   302   O  O   . GLN A  1 44  ? 44.604  -7.093  24.264  1.00 25.21 ? 61   GLN A O   1 
ATOM   303   C  CB  . GLN A  1 44  ? 43.710  -8.196  21.383  1.00 24.05 ? 61   GLN A CB  1 
ATOM   304   C  CG  . GLN A  1 44  ? 42.817  -9.078  22.247  1.00 23.59 ? 61   GLN A CG  1 
ATOM   305   C  CD  . GLN A  1 44  ? 42.644  -10.466 21.674  1.00 23.94 ? 61   GLN A CD  1 
ATOM   306   O  OE1 . GLN A  1 44  ? 43.544  -11.309 21.748  1.00 24.64 ? 61   GLN A OE1 1 
ATOM   307   N  NE2 . GLN A  1 44  ? 41.484  -10.717 21.089  1.00 23.29 ? 61   GLN A NE2 1 
ATOM   308   N  N   . ASP A  1 45  ? 46.282  -6.792  22.783  1.00 27.84 ? 62   ASP A N   1 
ATOM   309   C  CA  . ASP A  1 45  ? 47.351  -6.771  23.774  1.00 30.57 ? 62   ASP A CA  1 
ATOM   310   C  C   . ASP A  1 45  ? 47.104  -5.692  24.833  1.00 29.35 ? 62   ASP A C   1 
ATOM   311   O  O   . ASP A  1 45  ? 47.208  -5.969  26.022  1.00 29.83 ? 62   ASP A O   1 
ATOM   312   C  CB  . ASP A  1 45  ? 48.716  -6.605  23.119  1.00 31.74 ? 62   ASP A CB  1 
ATOM   313   C  CG  . ASP A  1 45  ? 49.283  -7.844  22.437  1.00 34.99 ? 62   ASP A CG  1 
ATOM   314   O  OD1 . ASP A  1 45  ? 48.635  -8.908  22.510  1.00 36.28 ? 62   ASP A OD1 1 
ATOM   315   O  OD2 . ASP A  1 45  ? 50.380  -7.739  21.847  1.00 39.24 ? 62   ASP A OD2 1 
ATOM   316   N  N   . ILE A  1 46  ? 46.768  -4.468  24.408  1.00 28.49 ? 63   ILE A N   1 
ATOM   317   C  CA  . ILE A  1 46  ? 46.598  -3.360  25.340  1.00 27.19 ? 63   ILE A CA  1 
ATOM   318   C  C   . ILE A  1 46  ? 45.344  -3.570  26.192  1.00 26.29 ? 63   ILE A C   1 
ATOM   319   O  O   . ILE A  1 46  ? 45.347  -3.292  27.389  1.00 25.88 ? 63   ILE A O   1 
ATOM   320   C  CB  . ILE A  1 46  ? 46.544  -2.013  24.596  1.00 27.68 ? 63   ILE A CB  1 
ATOM   321   C  CG1 . ILE A  1 46  ? 47.796  -1.770  23.741  1.00 29.55 ? 63   ILE A CG1 1 
ATOM   322   C  CG2 . ILE A  1 46  ? 46.292  -0.859  25.568  1.00 27.00 ? 63   ILE A CG2 1 
ATOM   323   C  CD1 . ILE A  1 46  ? 49.099  -1.729  24.514  1.00 30.55 ? 63   ILE A CD1 1 
ATOM   324   N  N   . GLN A  1 47  ? 44.254  -4.026  25.563  1.00 24.83 ? 64   GLN A N   1 
ATOM   325   C  CA  . GLN A  1 47  ? 43.008  -4.274  26.278  1.00 23.96 ? 64   GLN A CA  1 
ATOM   326   C  C   . GLN A  1 47  ? 43.207  -5.300  27.390  1.00 23.96 ? 64   GLN A C   1 
ATOM   327   O  O   . GLN A  1 47  ? 42.607  -5.180  28.459  1.00 24.75 ? 64   GLN A O   1 
ATOM   328   C  CB  . GLN A  1 47  ? 41.930  -4.795  25.327  1.00 23.60 ? 64   GLN A CB  1 
ATOM   329   C  CG  . GLN A  1 47  ? 41.370  -3.728  24.396  1.00 23.25 ? 64   GLN A CG  1 
ATOM   330   C  CD  . GLN A  1 47  ? 40.477  -4.305  23.322  1.00 21.93 ? 64   GLN A CD  1 
ATOM   331   O  OE1 . GLN A  1 47  ? 40.855  -5.253  22.628  1.00 20.99 ? 64   GLN A OE1 1 
ATOM   332   N  NE2 . GLN A  1 47  ? 39.290  -3.734  23.171  1.00 21.50 ? 64   GLN A NE2 1 
ATOM   333   N  N   . ALA A  1 48  ? 44.013  -6.332  27.108  1.00 24.08 ? 65   ALA A N   1 
ATOM   334   C  CA  . ALA A  1 48  ? 44.243  -7.407  28.060  1.00 25.38 ? 65   ALA A CA  1 
ATOM   335   C  C   . ALA A  1 48  ? 45.046  -6.896  29.255  1.00 25.36 ? 65   ALA A C   1 
ATOM   336   O  O   . ALA A  1 48  ? 44.745  -7.243  30.392  1.00 25.36 ? 65   ALA A O   1 
ATOM   337   C  CB  . ALA A  1 48  ? 44.936  -8.567  27.382  1.00 24.74 ? 65   ALA A CB  1 
ATOM   338   N  N   . LEU A  1 49  ? 46.070  -6.078  28.986  1.00 28.07 ? 66   LEU A N   1 
ATOM   339   C  CA  . LEU A  1 49  ? 46.918  -5.523  30.031  1.00 28.32 ? 66   LEU A CA  1 
ATOM   340   C  C   . LEU A  1 49  ? 46.120  -4.604  30.956  1.00 29.04 ? 66   LEU A C   1 
ATOM   341   O  O   . LEU A  1 49  ? 46.372  -4.581  32.159  1.00 29.33 ? 66   LEU A O   1 
ATOM   342   C  CB  . LEU A  1 49  ? 48.103  -4.793  29.404  1.00 29.67 ? 66   LEU A CB  1 
ATOM   343   C  CG  . LEU A  1 49  ? 49.171  -5.685  28.771  1.00 31.08 ? 66   LEU A CG  1 
ATOM   344   C  CD1 . LEU A  1 49  ? 50.145  -4.862  27.952  1.00 31.95 ? 66   LEU A CD1 1 
ATOM   345   C  CD2 . LEU A  1 49  ? 49.904  -6.482  29.834  1.00 32.61 ? 66   LEU A CD2 1 
ATOM   346   N  N   . ARG A  1 50  ? 45.172  -3.839  30.400  1.00 27.16 ? 67   ARG A N   1 
ATOM   347   C  CA  . ARG A  1 50  ? 44.309  -2.996  31.215  1.00 27.36 ? 67   ARG A CA  1 
ATOM   348   C  C   . ARG A  1 50  ? 43.484  -3.874  32.155  1.00 28.68 ? 67   ARG A C   1 
ATOM   349   O  O   . ARG A  1 50  ? 43.334  -3.556  33.338  1.00 28.73 ? 67   ARG A O   1 
ATOM   350   C  CB  . ARG A  1 50  ? 43.384  -2.116  30.365  1.00 26.97 ? 67   ARG A CB  1 
ATOM   351   C  CG  . ARG A  1 50  ? 42.328  -1.373  31.171  1.00 27.50 ? 67   ARG A CG  1 
ATOM   352   C  CD  . ARG A  1 50  ? 41.312  -0.653  30.308  1.00 27.91 ? 67   ARG A CD  1 
ATOM   353   N  NE  . ARG A  1 50  ? 41.920  0.470   29.585  1.00 28.52 ? 67   ARG A NE  1 
ATOM   354   C  CZ  . ARG A  1 50  ? 42.215  0.495   28.288  1.00 28.61 ? 67   ARG A CZ  1 
ATOM   355   N  NH1 . ARG A  1 50  ? 41.948  -0.535  27.500  1.00 28.33 ? 67   ARG A NH1 1 
ATOM   356   N  NH2 . ARG A  1 50  ? 42.786  1.566   27.777  1.00 28.72 ? 67   ARG A NH2 1 
ATOM   357   N  N   . PHE A  1 51  ? 42.940  -4.975  31.619  1.00 28.51 ? 68   PHE A N   1 
ATOM   358   C  CA  . PHE A  1 51  ? 42.134  -5.886  32.414  1.00 29.60 ? 68   PHE A CA  1 
ATOM   359   C  C   . PHE A  1 51  ? 42.962  -6.457  33.564  1.00 29.79 ? 68   PHE A C   1 
ATOM   360   O  O   . PHE A  1 51  ? 42.498  -6.469  34.703  1.00 30.39 ? 68   PHE A O   1 
ATOM   361   C  CB  . PHE A  1 51  ? 41.559  -7.048  31.599  1.00 31.50 ? 68   PHE A CB  1 
ATOM   362   C  CG  . PHE A  1 51  ? 41.199  -8.236  32.478  1.00 31.86 ? 68   PHE A CG  1 
ATOM   363   C  CD1 . PHE A  1 51  ? 39.949  -8.328  33.075  1.00 32.89 ? 68   PHE A CD1 1 
ATOM   364   C  CD2 . PHE A  1 51  ? 42.131  -9.235  32.734  1.00 34.33 ? 68   PHE A CD2 1 
ATOM   365   C  CE1 . PHE A  1 51  ? 39.634  -9.404  33.890  1.00 33.21 ? 68   PHE A CE1 1 
ATOM   366   C  CE2 . PHE A  1 51  ? 41.816  -10.301 33.562  1.00 35.10 ? 68   PHE A CE2 1 
ATOM   367   C  CZ  . PHE A  1 51  ? 40.567  -10.389 34.126  1.00 34.39 ? 68   PHE A CZ  1 
ATOM   368   N  N   . HIS A  1 52  ? 44.166  -6.953  33.247  1.00 31.31 ? 69   HIS A N   1 
ATOM   369   C  CA  . HIS A  1 52  ? 45.016  -7.622  34.219  1.00 33.87 ? 69   HIS A CA  1 
ATOM   370   C  C   . HIS A  1 52  ? 45.350  -6.653  35.352  1.00 36.55 ? 69   HIS A C   1 
ATOM   371   O  O   . HIS A  1 52  ? 45.319  -7.032  36.522  1.00 38.64 ? 69   HIS A O   1 
ATOM   372   C  CB  . HIS A  1 52  ? 46.270  -8.198  33.546  1.00 34.32 ? 69   HIS A CB  1 
ATOM   373   C  CG  . HIS A  1 52  ? 46.012  -9.389  32.672  1.00 35.98 ? 69   HIS A CG  1 
ATOM   374   N  ND1 . HIS A  1 52  ? 45.164  -10.421 33.020  1.00 36.67 ? 69   HIS A ND1 1 
ATOM   375   C  CD2 . HIS A  1 52  ? 46.508  -9.715  31.469  1.00 36.73 ? 69   HIS A CD2 1 
ATOM   376   C  CE1 . HIS A  1 52  ? 45.152  -11.327 32.050  1.00 36.85 ? 69   HIS A CE1 1 
ATOM   377   N  NE2 . HIS A  1 52  ? 45.961  -10.917 31.097  1.00 36.55 ? 69   HIS A NE2 1 
ATOM   378   N  N   . ARG A  1 53  ? 45.642  -5.398  34.989  1.00 35.49 ? 70   ARG A N   1 
ATOM   379   C  CA  . ARG A  1 53  ? 45.932  -4.362  35.967  1.00 36.95 ? 70   ARG A CA  1 
ATOM   380   C  C   . ARG A  1 53  ? 44.740  -4.155  36.902  1.00 36.41 ? 70   ARG A C   1 
ATOM   381   O  O   . ARG A  1 53  ? 44.918  -4.078  38.116  1.00 39.71 ? 70   ARG A O   1 
ATOM   382   C  CB  . ARG A  1 53  ? 46.295  -3.038  35.285  1.00 38.75 ? 70   ARG A CB  1 
ATOM   383   C  CG  . ARG A  1 53  ? 46.668  -1.955  36.288  1.00 41.09 ? 70   ARG A CG  1 
ATOM   384   C  CD  . ARG A  1 53  ? 46.410  -0.571  35.757  1.00 44.04 ? 70   ARG A CD  1 
ATOM   385   N  NE  . ARG A  1 53  ? 44.994  -0.314  35.466  1.00 45.11 ? 70   ARG A NE  1 
ATOM   386   C  CZ  . ARG A  1 53  ? 44.567  0.789   34.864  1.00 44.99 ? 70   ARG A CZ  1 
ATOM   387   N  NH1 . ARG A  1 53  ? 45.429  1.745   34.563  1.00 45.23 ? 70   ARG A NH1 1 
ATOM   388   N  NH2 . ARG A  1 53  ? 43.287  0.941   34.572  1.00 44.31 ? 70   ARG A NH2 1 
ATOM   389   N  N   . ASN A  1 54  ? 43.537  -4.047  36.330  1.00 35.63 ? 71   ASN A N   1 
ATOM   390   C  CA  . ASN A  1 54  ? 42.322  -3.823  37.098  1.00 37.53 ? 71   ASN A CA  1 
ATOM   391   C  C   . ASN A  1 54  ? 42.036  -4.998  38.034  1.00 43.09 ? 71   ASN A C   1 
ATOM   392   O  O   . ASN A  1 54  ? 41.489  -4.802  39.120  1.00 45.20 ? 71   ASN A O   1 
ATOM   393   C  CB  . ASN A  1 54  ? 41.114  -3.599  36.192  1.00 37.62 ? 71   ASN A CB  1 
ATOM   394   C  CG  . ASN A  1 54  ? 41.144  -2.271  35.474  1.00 36.50 ? 71   ASN A CG  1 
ATOM   395   O  OD1 . ASN A  1 54  ? 41.908  -1.371  35.841  1.00 36.70 ? 71   ASN A OD1 1 
ATOM   396   N  ND2 . ASN A  1 54  ? 40.293  -2.118  34.470  1.00 35.87 ? 71   ASN A ND2 1 
ATOM   397   N  N   . LEU A  1 55  ? 42.385  -6.217  37.601  1.00 46.20 ? 72   LEU A N   1 
ATOM   398   C  CA  . LEU A  1 55  ? 42.033  -7.419  38.341  1.00 50.20 ? 72   LEU A CA  1 
ATOM   399   C  C   . LEU A  1 55  ? 42.772  -7.450  39.679  1.00 53.48 ? 72   LEU A C   1 
ATOM   400   O  O   . LEU A  1 55  ? 42.190  -7.830  40.694  1.00 54.27 ? 72   LEU A O   1 
ATOM   401   C  CB  . LEU A  1 55  ? 42.329  -8.673  37.520  1.00 48.82 ? 72   LEU A CB  1 
ATOM   402   C  CG  . LEU A  1 55  ? 41.697  -9.968  38.042  1.00 49.59 ? 72   LEU A CG  1 
ATOM   403   C  CD1 . LEU A  1 55  ? 40.185  -9.960  37.860  1.00 50.21 ? 72   LEU A CD1 1 
ATOM   404   C  CD2 . LEU A  1 55  ? 42.312  -11.176 37.366  1.00 50.54 ? 72   LEU A CD2 1 
ATOM   405   N  N   . LYS A  1 56  ? 44.045  -7.035  39.670  1.00 59.34 ? 73   LYS A N   1 
ATOM   406   C  CA  . LYS A  1 56  ? 44.883  -7.035  40.862  1.00 62.92 ? 73   LYS A CA  1 
ATOM   407   C  C   . LYS A  1 56  ? 44.305  -6.143  41.963  1.00 64.96 ? 73   LYS A C   1 
ATOM   408   O  O   . LYS A  1 56  ? 44.639  -6.326  43.132  1.00 66.82 ? 73   LYS A O   1 
ATOM   409   C  CB  . LYS A  1 56  ? 46.303  -6.572  40.524  1.00 64.72 ? 73   LYS A CB  1 
ATOM   410   C  CG  . LYS A  1 56  ? 47.120  -7.545  39.689  1.00 66.95 ? 73   LYS A CG  1 
ATOM   411   C  CD  . LYS A  1 56  ? 48.459  -6.989  39.220  1.00 70.52 ? 73   LYS A CD  1 
ATOM   412   C  CE  . LYS A  1 56  ? 49.334  -6.526  40.344  1.00 71.93 ? 73   LYS A CE  1 
ATOM   413   N  NZ  . LYS A  1 56  ? 50.626  -6.043  39.853  1.00 74.76 ? 73   LYS A NZ  1 
ATOM   414   N  N   . LYS A  1 57  ? 43.453  -5.180  41.592  1.00 67.29 ? 74   LYS A N   1 
ATOM   415   C  CA  . LYS A  1 57  ? 42.865  -4.252  42.547  1.00 70.31 ? 74   LYS A CA  1 
ATOM   416   C  C   . LYS A  1 57  ? 41.514  -4.762  43.049  1.00 71.01 ? 74   LYS A C   1 
ATOM   417   O  O   . LYS A  1 57  ? 40.877  -4.111  43.876  1.00 71.63 ? 74   LYS A O   1 
ATOM   418   C  CB  . LYS A  1 57  ? 42.685  -2.875  41.901  1.00 72.45 ? 74   LYS A CB  1 
ATOM   419   C  CG  . LYS A  1 57  ? 43.928  -2.292  41.231  1.00 73.26 ? 74   LYS A CG  1 
ATOM   420   C  CD  . LYS A  1 57  ? 43.690  -0.984  40.484  1.00 74.10 ? 74   LYS A CD  1 
ATOM   421   C  CE  . LYS A  1 57  ? 42.333  -0.913  39.850  1.00 74.38 ? 74   LYS A CE  1 
ATOM   422   N  NZ  . LYS A  1 57  ? 42.281  0.052   38.753  1.00 75.64 ? 74   LYS A NZ  1 
ATOM   423   N  N   . MET A  1 58  ? 41.064  -5.910  42.528  1.00 70.68 ? 75   MET A N   1 
ATOM   424   C  CA  . MET A  1 58  ? 39.916  -6.611  43.081  1.00 69.81 ? 75   MET A CA  1 
ATOM   425   C  C   . MET A  1 58  ? 40.421  -7.445  44.258  1.00 67.16 ? 75   MET A C   1 
ATOM   426   O  O   . MET A  1 58  ? 41.542  -7.949  44.213  1.00 68.70 ? 75   MET A O   1 
ATOM   427   C  CB  . MET A  1 58  ? 39.259  -7.521  42.034  1.00 71.43 ? 75   MET A CB  1 
ATOM   428   C  CG  . MET A  1 58  ? 39.002  -6.872  40.680  1.00 71.02 ? 75   MET A CG  1 
ATOM   429   S  SD  . MET A  1 58  ? 37.553  -5.798  40.643  1.00 72.48 ? 75   MET A SD  1 
ATOM   430   C  CE  . MET A  1 58  ? 37.869  -4.926  39.102  1.00 71.09 ? 75   MET A CE  1 
ATOM   431   N  N   . THR A  1 59  ? 39.612  -7.580  45.317  1.00 59.75 ? 76   THR A N   1 
ATOM   432   C  CA  . THR A  1 59  ? 40.080  -8.258  46.517  1.00 55.95 ? 76   THR A CA  1 
ATOM   433   C  C   . THR A  1 59  ? 39.622  -9.717  46.501  1.00 48.64 ? 76   THR A C   1 
ATOM   434   O  O   . THR A  1 59  ? 40.445  -10.617 46.352  1.00 45.03 ? 76   THR A O   1 
ATOM   435   C  CB  . THR A  1 59  ? 39.617  -7.526  47.778  1.00 55.87 ? 76   THR A CB  1 
ATOM   436   O  OG1 . THR A  1 59  ? 39.865  -6.137  47.592  1.00 57.19 ? 76   THR A OG1 1 
ATOM   437   C  CG2 . THR A  1 59  ? 40.369  -8.000  49.009  1.00 56.50 ? 76   THR A CG2 1 
ATOM   438   N  N   . SER A  1 60  ? 38.311  -9.936  46.649  1.00 45.41 ? 77   SER A N   1 
ATOM   439   C  CA  . SER A  1 60  ? 37.756  -11.268 46.835  1.00 46.39 ? 77   SER A CA  1 
ATOM   440   C  C   . SER A  1 60  ? 37.706  -12.028 45.510  1.00 45.21 ? 77   SER A C   1 
ATOM   441   O  O   . SER A  1 60  ? 37.610  -11.422 44.441  1.00 42.22 ? 77   SER A O   1 
ATOM   442   C  CB  . SER A  1 60  ? 36.383  -11.197 47.456  1.00 47.87 ? 77   SER A CB  1 
ATOM   443   O  OG  . SER A  1 60  ? 35.493  -10.456 46.632  1.00 49.70 ? 77   SER A OG  1 
ATOM   444   N  N   . PRO A  1 61  ? 37.749  -13.382 45.536  1.00 44.01 ? 78   PRO A N   1 
ATOM   445   C  CA  . PRO A  1 61  ? 37.510  -14.179 44.330  1.00 41.51 ? 78   PRO A CA  1 
ATOM   446   C  C   . PRO A  1 61  ? 36.142  -13.896 43.710  1.00 40.59 ? 78   PRO A C   1 
ATOM   447   O  O   . PRO A  1 61  ? 36.000  -13.939 42.491  1.00 41.06 ? 78   PRO A O   1 
ATOM   448   C  CB  . PRO A  1 61  ? 37.645  -15.630 44.830  1.00 42.23 ? 78   PRO A CB  1 
ATOM   449   C  CG  . PRO A  1 61  ? 38.500  -15.516 46.078  1.00 43.95 ? 78   PRO A CG  1 
ATOM   450   C  CD  . PRO A  1 61  ? 38.049  -14.215 46.715  1.00 43.58 ? 78   PRO A CD  1 
ATOM   451   N  N   . LEU A  1 62  ? 35.148  -13.596 44.560  1.00 39.18 ? 79   LEU A N   1 
ATOM   452   C  CA  . LEU A  1 62  ? 33.800  -13.279 44.112  1.00 42.01 ? 79   LEU A CA  1 
ATOM   453   C  C   . LEU A  1 62  ? 33.800  -12.000 43.277  1.00 41.46 ? 79   LEU A C   1 
ATOM   454   O  O   . LEU A  1 62  ? 33.090  -11.922 42.276  1.00 39.15 ? 79   LEU A O   1 
ATOM   455   C  CB  . LEU A  1 62  ? 32.826  -13.165 45.286  1.00 43.83 ? 79   LEU A CB  1 
ATOM   456   C  CG  . LEU A  1 62  ? 32.051  -14.437 45.646  1.00 46.59 ? 79   LEU A CG  1 
ATOM   457   C  CD1 . LEU A  1 62  ? 32.970  -15.556 46.111  1.00 47.61 ? 79   LEU A CD1 1 
ATOM   458   C  CD2 . LEU A  1 62  ? 31.000  -14.140 46.703  1.00 46.94 ? 79   LEU A CD2 1 
ATOM   459   N  N   . GLU A  1 63  ? 34.577  -10.997 43.706  1.00 39.78 ? 80   GLU A N   1 
ATOM   460   C  CA  . GLU A  1 63  ? 34.638  -9.719  43.010  1.00 39.55 ? 80   GLU A CA  1 
ATOM   461   C  C   . GLU A  1 63  ? 35.309  -9.890  41.646  1.00 37.02 ? 80   GLU A C   1 
ATOM   462   O  O   . GLU A  1 63  ? 34.883  -9.279  40.669  1.00 35.19 ? 80   GLU A O   1 
ATOM   463   C  CB  . GLU A  1 63  ? 35.365  -8.680  43.866  1.00 41.08 ? 80   GLU A CB  1 
ATOM   464   N  N   . LYS A  1 64  ? 36.357  -10.725 41.590  1.00 35.72 ? 81   LYS A N   1 
ATOM   465   C  CA  . LYS A  1 64  ? 37.065  -11.012 40.353  1.00 36.21 ? 81   LYS A CA  1 
ATOM   466   C  C   . LYS A  1 64  ? 36.141  -11.738 39.372  1.00 36.26 ? 81   LYS A C   1 
ATOM   467   O  O   . LYS A  1 64  ? 36.179  -11.465 38.172  1.00 35.05 ? 81   LYS A O   1 
ATOM   468   C  CB  . LYS A  1 64  ? 38.324  -11.846 40.628  1.00 37.25 ? 81   LYS A CB  1 
ATOM   469   C  CG  . LYS A  1 64  ? 39.434  -11.155 41.413  1.00 38.60 ? 81   LYS A CG  1 
ATOM   470   C  CD  . LYS A  1 64  ? 40.656  -12.041 41.635  1.00 40.59 ? 81   LYS A CD  1 
ATOM   471   C  CE  . LYS A  1 64  ? 41.615  -11.522 42.668  1.00 42.60 ? 81   LYS A CE  1 
ATOM   472   N  NZ  . LYS A  1 64  ? 42.284  -10.281 42.268  1.00 44.34 ? 81   LYS A NZ  1 
ATOM   473   N  N   . TYR A  1 65  ? 35.314  -12.657 39.896  1.00 34.59 ? 82   TYR A N   1 
ATOM   474   C  CA  . TYR A  1 65  ? 34.403  -13.457 39.090  1.00 34.42 ? 82   TYR A CA  1 
ATOM   475   C  C   . TYR A  1 65  ? 33.399  -12.549 38.386  1.00 34.84 ? 82   TYR A C   1 
ATOM   476   O  O   . TYR A  1 65  ? 33.204  -12.666 37.180  1.00 33.15 ? 82   TYR A O   1 
ATOM   477   C  CB  . TYR A  1 65  ? 33.682  -14.501 39.950  1.00 33.59 ? 82   TYR A CB  1 
ATOM   478   C  CG  . TYR A  1 65  ? 32.528  -15.220 39.261  1.00 31.94 ? 82   TYR A CG  1 
ATOM   479   C  CD1 . TYR A  1 65  ? 31.235  -14.715 39.313  1.00 31.43 ? 82   TYR A CD1 1 
ATOM   480   C  CD2 . TYR A  1 65  ? 32.731  -16.406 38.563  1.00 31.94 ? 82   TYR A CD2 1 
ATOM   481   C  CE1 . TYR A  1 65  ? 30.182  -15.362 38.687  1.00 31.03 ? 82   TYR A CE1 1 
ATOM   482   C  CE2 . TYR A  1 65  ? 31.685  -17.067 37.936  1.00 31.07 ? 82   TYR A CE2 1 
ATOM   483   C  CZ  . TYR A  1 65  ? 30.407  -16.543 38.002  1.00 30.89 ? 82   TYR A CZ  1 
ATOM   484   O  OH  . TYR A  1 65  ? 29.371  -17.173 37.385  1.00 28.85 ? 82   TYR A OH  1 
ATOM   485   N  N   . ILE A  1 66  ? 32.765  -11.658 39.158  1.00 35.42 ? 83   ILE A N   1 
ATOM   486   C  CA  . ILE A  1 66  ? 31.756  -10.744 38.645  1.00 35.88 ? 83   ILE A CA  1 
ATOM   487   C  C   . ILE A  1 66  ? 32.350  -9.890  37.525  1.00 34.97 ? 83   ILE A C   1 
ATOM   488   O  O   . ILE A  1 66  ? 31.677  -9.626  36.528  1.00 33.61 ? 83   ILE A O   1 
ATOM   489   C  CB  . ILE A  1 66  ? 31.183  -9.879  39.784  1.00 37.96 ? 83   ILE A CB  1 
ATOM   490   C  CG1 . ILE A  1 66  ? 30.359  -10.718 40.771  1.00 40.00 ? 83   ILE A CG1 1 
ATOM   491   C  CG2 . ILE A  1 66  ? 30.371  -8.701  39.242  1.00 38.54 ? 83   ILE A CG2 1 
ATOM   492   C  CD1 . ILE A  1 66  ? 29.067  -11.280 40.202  1.00 40.41 ? 83   ILE A CD1 1 
ATOM   493   N  N   . TYR A  1 67  ? 33.612  -9.480  37.697  1.00 33.13 ? 84   TYR A N   1 
ATOM   494   C  CA  . TYR A  1 67  ? 34.275  -8.583  36.766  1.00 34.47 ? 84   TYR A CA  1 
ATOM   495   C  C   . TYR A  1 67  ? 34.633  -9.303  35.461  1.00 31.86 ? 84   TYR A C   1 
ATOM   496   O  O   . TYR A  1 67  ? 34.356  -8.789  34.379  1.00 29.61 ? 84   TYR A O   1 
ATOM   497   C  CB  . TYR A  1 67  ? 35.518  -7.989  37.437  1.00 37.08 ? 84   TYR A CB  1 
ATOM   498   C  CG  . TYR A  1 67  ? 36.294  -7.025  36.548  1.00 40.99 ? 84   TYR A CG  1 
ATOM   499   C  CD1 . TYR A  1 67  ? 35.667  -5.938  35.947  1.00 44.69 ? 84   TYR A CD1 1 
ATOM   500   C  CD2 . TYR A  1 67  ? 37.641  -7.232  36.273  1.00 42.50 ? 84   TYR A CD2 1 
ATOM   501   C  CE1 . TYR A  1 67  ? 36.365  -5.066  35.126  1.00 46.66 ? 84   TYR A CE1 1 
ATOM   502   C  CE2 . TYR A  1 67  ? 38.347  -6.372  35.450  1.00 44.92 ? 84   TYR A CE2 1 
ATOM   503   C  CZ  . TYR A  1 67  ? 37.706  -5.290  34.872  1.00 46.56 ? 84   TYR A CZ  1 
ATOM   504   O  OH  . TYR A  1 67  ? 38.411  -4.446  34.065  1.00 53.18 ? 84   TYR A OH  1 
ATOM   505   N  N   A ILE A  1 68  ? 35.249  -10.487 35.561  0.50 29.82 ? 85   ILE A N   1 
ATOM   506   N  N   B ILE A  1 68  ? 35.273  -10.472 35.588  0.50 30.50 ? 85   ILE A N   1 
ATOM   507   C  CA  A ILE A  1 68  ? 35.709  -11.196 34.376  0.50 28.79 ? 85   ILE A CA  1 
ATOM   508   C  CA  B ILE A  1 68  ? 35.709  -11.268 34.452  0.50 29.94 ? 85   ILE A CA  1 
ATOM   509   C  C   A ILE A  1 68  ? 34.509  -11.716 33.583  0.50 27.99 ? 85   ILE A C   1 
ATOM   510   C  C   B ILE A  1 68  ? 34.504  -11.683 33.608  0.50 28.57 ? 85   ILE A C   1 
ATOM   511   O  O   A ILE A  1 68  ? 34.528  -11.669 32.356  0.50 27.18 ? 85   ILE A O   1 
ATOM   512   O  O   B ILE A  1 68  ? 34.518  -11.534 32.390  0.50 27.62 ? 85   ILE A O   1 
ATOM   513   C  CB  A ILE A  1 68  ? 36.702  -12.319 34.732  0.50 28.55 ? 85   ILE A CB  1 
ATOM   514   C  CB  B ILE A  1 68  ? 36.504  -12.491 34.943  0.50 30.72 ? 85   ILE A CB  1 
ATOM   515   C  CG1 A ILE A  1 68  ? 37.583  -12.680 33.534  0.50 28.80 ? 85   ILE A CG1 1 
ATOM   516   C  CG1 B ILE A  1 68  ? 37.850  -12.076 35.517  0.50 31.04 ? 85   ILE A CG1 1 
ATOM   517   C  CG2 A ILE A  1 68  ? 35.986  -13.545 35.298  0.50 27.99 ? 85   ILE A CG2 1 
ATOM   518   C  CG2 B ILE A  1 68  ? 36.667  -13.526 33.832  0.50 31.21 ? 85   ILE A CG2 1 
ATOM   519   C  CD1 A ILE A  1 68  ? 38.586  -13.784 33.817  0.50 28.84 ? 85   ILE A CD1 1 
ATOM   520   C  CD1 B ILE A  1 68  ? 38.588  -13.189 36.235  0.50 31.07 ? 85   ILE A CD1 1 
ATOM   521   N  N   . MET A  1 69  ? 33.461  -12.195 34.271  1.00 27.56 ? 86   MET A N   1 
ATOM   522   C  CA  . MET A  1 69  ? 32.293  -12.730 33.584  1.00 28.27 ? 86   MET A CA  1 
ATOM   523   C  C   . MET A  1 69  ? 31.527  -11.617 32.864  1.00 28.03 ? 86   MET A C   1 
ATOM   524   O  O   . MET A  1 69  ? 30.901  -11.872 31.837  1.00 27.60 ? 86   MET A O   1 
ATOM   525   C  CB  . MET A  1 69  ? 31.359  -13.483 34.541  1.00 28.62 ? 86   MET A CB  1 
ATOM   526   C  CG  . MET A  1 69  ? 31.945  -14.775 35.112  1.00 29.76 ? 86   MET A CG  1 
ATOM   527   S  SD  . MET A  1 69  ? 32.734  -15.876 33.915  1.00 29.38 ? 86   MET A SD  1 
ATOM   528   C  CE  . MET A  1 69  ? 31.303  -16.252 32.893  1.00 32.10 ? 86   MET A CE  1 
ATOM   529   N  N   . GLY A  1 70  ? 31.591  -10.386 33.390  1.00 27.05 ? 87   GLY A N   1 
ATOM   530   C  CA  . GLY A  1 70  ? 31.009  -9.232  32.721  1.00 28.46 ? 87   GLY A CA  1 
ATOM   531   C  C   . GLY A  1 70  ? 31.572  -9.046  31.310  1.00 29.81 ? 87   GLY A C   1 
ATOM   532   O  O   . GLY A  1 70  ? 30.851  -8.642  30.399  1.00 29.65 ? 87   GLY A O   1 
ATOM   533   N  N   . ILE A  1 71  ? 32.861  -9.363  31.135  1.00 29.19 ? 88   ILE A N   1 
ATOM   534   C  CA  . ILE A  1 71  ? 33.529  -9.211  29.853  1.00 29.70 ? 88   ILE A CA  1 
ATOM   535   C  C   . ILE A  1 71  ? 32.958  -10.212 28.849  1.00 29.85 ? 88   ILE A C   1 
ATOM   536   O  O   . ILE A  1 71  ? 32.851  -9.893  27.668  1.00 25.76 ? 88   ILE A O   1 
ATOM   537   C  CB  . ILE A  1 71  ? 35.058  -9.337  29.995  1.00 30.64 ? 88   ILE A CB  1 
ATOM   538   C  CG1 . ILE A  1 71  ? 35.598  -8.373  31.056  1.00 32.08 ? 88   ILE A CG1 1 
ATOM   539   C  CG2 . ILE A  1 71  ? 35.748  -9.134  28.644  1.00 31.48 ? 88   ILE A CG2 1 
ATOM   540   C  CD1 . ILE A  1 71  ? 37.109  -8.371  31.205  1.00 32.56 ? 88   ILE A CD1 1 
ATOM   541   N  N   . GLN A  1 72  ? 32.567  -11.407 29.314  1.00 30.26 ? 89   GLN A N   1 
ATOM   542   C  CA  . GLN A  1 72  ? 31.984  -12.401 28.425  1.00 30.79 ? 89   GLN A CA  1 
ATOM   543   C  C   . GLN A  1 72  ? 30.765  -11.815 27.712  1.00 30.21 ? 89   GLN A C   1 
ATOM   544   O  O   . GLN A  1 72  ? 30.533  -12.120 26.544  1.00 31.36 ? 89   GLN A O   1 
ATOM   545   C  CB  . GLN A  1 72  ? 31.586  -13.691 29.146  1.00 32.09 ? 89   GLN A CB  1 
ATOM   546   C  CG  . GLN A  1 72  ? 31.066  -14.781 28.211  1.00 33.33 ? 89   GLN A CG  1 
ATOM   547   C  CD  . GLN A  1 72  ? 30.557  -16.007 28.935  1.00 36.00 ? 89   GLN A CD  1 
ATOM   548   O  OE1 . GLN A  1 72  ? 30.909  -17.147 28.605  1.00 39.94 ? 89   GLN A OE1 1 
ATOM   549   N  NE2 . GLN A  1 72  ? 29.701  -15.784 29.920  1.00 35.57 ? 89   GLN A NE2 1 
ATOM   550   N  N   . GLU A  1 73  ? 29.995  -10.977 28.419  1.00 30.38 ? 90   GLU A N   1 
ATOM   551   C  CA  . GLU A  1 73  ? 28.780  -10.391 27.872  1.00 32.06 ? 90   GLU A CA  1 
ATOM   552   C  C   . GLU A  1 73  ? 29.066  -9.126  27.058  1.00 28.99 ? 90   GLU A C   1 
ATOM   553   O  O   . GLU A  1 73  ? 28.125  -8.512  26.562  1.00 29.17 ? 90   GLU A O   1 
ATOM   554   C  CB  . GLU A  1 73  ? 27.773  -10.044 28.975  1.00 36.07 ? 90   GLU A CB  1 
ATOM   555   C  CG  . GLU A  1 73  ? 26.916  -11.224 29.429  1.00 40.51 ? 90   GLU A CG  1 
ATOM   556   C  CD  . GLU A  1 73  ? 25.627  -10.871 30.164  1.00 44.23 ? 90   GLU A CD  1 
ATOM   557   O  OE1 . GLU A  1 73  ? 24.749  -10.137 29.626  1.00 40.62 ? 90   GLU A OE1 1 
ATOM   558   O  OE2 . GLU A  1 73  ? 25.505  -11.365 31.308  1.00 47.85 ? 90   GLU A OE2 1 
ATOM   559   N  N   . ARG A  1 74  ? 30.340  -8.727  26.920  1.00 25.73 ? 91   ARG A N   1 
ATOM   560   C  CA  . ARG A  1 74  ? 30.687  -7.510  26.198  1.00 25.37 ? 91   ARG A CA  1 
ATOM   561   C  C   . ARG A  1 74  ? 31.577  -7.786  24.986  1.00 23.02 ? 91   ARG A C   1 
ATOM   562   O  O   . ARG A  1 74  ? 31.332  -7.242  23.912  1.00 22.28 ? 91   ARG A O   1 
ATOM   563   C  CB  . ARG A  1 74  ? 31.419  -6.531  27.122  1.00 26.99 ? 91   ARG A CB  1 
ATOM   564   C  CG  . ARG A  1 74  ? 30.541  -5.988  28.238  1.00 29.41 ? 91   ARG A CG  1 
ATOM   565   C  CD  . ARG A  1 74  ? 31.270  -4.952  29.079  1.00 32.24 ? 91   ARG A CD  1 
ATOM   566   N  NE  . ARG A  1 74  ? 30.369  -4.450  30.123  1.00 35.31 ? 91   ARG A NE  1 
ATOM   567   C  CZ  . ARG A  1 74  ? 29.883  -3.219  30.232  1.00 38.21 ? 91   ARG A CZ  1 
ATOM   568   N  NH1 . ARG A  1 74  ? 30.291  -2.246  29.432  1.00 37.46 ? 91   ARG A NH1 1 
ATOM   569   N  NH2 . ARG A  1 74  ? 28.991  -2.963  31.175  1.00 41.59 ? 91   ARG A NH2 1 
ATOM   570   N  N   . ASN A  1 75  ? 32.637  -8.578  25.190  1.00 21.73 ? 92   ASN A N   1 
ATOM   571   C  CA  . ASN A  1 75  ? 33.656  -8.828  24.180  1.00 21.72 ? 92   ASN A CA  1 
ATOM   572   C  C   . ASN A  1 75  ? 34.191  -10.246 24.373  1.00 22.30 ? 92   ASN A C   1 
ATOM   573   O  O   . ASN A  1 75  ? 35.062  -10.483 25.204  1.00 22.10 ? 92   ASN A O   1 
ATOM   574   C  CB  . ASN A  1 75  ? 34.754  -7.772  24.256  1.00 21.55 ? 92   ASN A CB  1 
ATOM   575   C  CG  . ASN A  1 75  ? 35.796  -7.899  23.169  1.00 20.94 ? 92   ASN A CG  1 
ATOM   576   O  OD1 . ASN A  1 75  ? 36.001  -8.982  22.608  1.00 20.84 ? 92   ASN A OD1 1 
ATOM   577   N  ND2 . ASN A  1 75  ? 36.487  -6.803  22.880  1.00 20.89 ? 92   ASN A ND2 1 
ATOM   578   N  N   . GLU A  1 76  ? 33.677  -11.178 23.568  1.00 22.67 ? 93   GLU A N   1 
ATOM   579   C  CA  . GLU A  1 76  ? 33.925  -12.597 23.768  1.00 24.13 ? 93   GLU A CA  1 
ATOM   580   C  C   . GLU A  1 76  ? 35.400  -12.927 23.550  1.00 22.52 ? 93   GLU A C   1 
ATOM   581   O  O   . GLU A  1 76  ? 35.993  -13.673 24.323  1.00 22.51 ? 93   GLU A O   1 
ATOM   582   C  CB  . GLU A  1 76  ? 33.019  -13.368 22.811  1.00 25.69 ? 93   GLU A CB  1 
ATOM   583   C  CG  . GLU A  1 76  ? 33.224  -14.876 22.854  1.00 28.22 ? 93   GLU A CG  1 
ATOM   584   C  CD  . GLU A  1 76  ? 32.170  -15.578 22.027  1.00 30.64 ? 93   GLU A CD  1 
ATOM   585   O  OE1 . GLU A  1 76  ? 31.209  -16.057 22.655  1.00 33.39 ? 93   GLU A OE1 1 
ATOM   586   O  OE2 . GLU A  1 76  ? 32.305  -15.639 20.786  1.00 32.20 ? 93   GLU A OE2 1 
ATOM   587   N  N   . LYS A  1 77  ? 36.000  -12.377 22.493  1.00 21.59 ? 94   LYS A N   1 
ATOM   588   C  CA  . LYS A  1 77  ? 37.383  -12.708 22.176  1.00 22.06 ? 94   LYS A CA  1 
ATOM   589   C  C   . LYS A  1 77  ? 38.331  -12.164 23.246  1.00 21.47 ? 94   LYS A C   1 
ATOM   590   O  O   . LYS A  1 77  ? 39.274  -12.851 23.641  1.00 21.59 ? 94   LYS A O   1 
ATOM   591   C  CB  . LYS A  1 77  ? 37.721  -12.260 20.753  1.00 22.94 ? 94   LYS A CB  1 
ATOM   592   C  CG  . LYS A  1 77  ? 37.214  -13.235 19.714  1.00 24.53 ? 94   LYS A CG  1 
ATOM   593   C  CD  . LYS A  1 77  ? 37.616  -12.906 18.287  1.00 27.14 ? 94   LYS A CD  1 
ATOM   594   C  CE  . LYS A  1 77  ? 37.325  -14.039 17.348  1.00 28.38 ? 94   LYS A CE  1 
ATOM   595   N  NZ  . LYS A  1 77  ? 37.623  -13.647 15.966  1.00 30.36 ? 94   LYS A NZ  1 
ATOM   596   N  N   . LEU A  1 78  ? 38.077  -10.944 23.728  1.00 20.37 ? 95   LEU A N   1 
ATOM   597   C  CA  . LEU A  1 78  ? 38.859  -10.384 24.824  1.00 21.23 ? 95   LEU A CA  1 
ATOM   598   C  C   . LEU A  1 78  ? 38.740  -11.268 26.069  1.00 21.60 ? 95   LEU A C   1 
ATOM   599   O  O   . LEU A  1 78  ? 39.733  -11.529 26.741  1.00 22.40 ? 95   LEU A O   1 
ATOM   600   C  CB  . LEU A  1 78  ? 38.419  -8.951  25.124  1.00 21.18 ? 95   LEU A CB  1 
ATOM   601   C  CG  . LEU A  1 78  ? 39.169  -8.239  26.256  1.00 21.81 ? 95   LEU A CG  1 
ATOM   602   C  CD1 . LEU A  1 78  ? 40.677  -8.247  26.037  1.00 21.34 ? 95   LEU A CD1 1 
ATOM   603   C  CD2 . LEU A  1 78  ? 38.645  -6.817  26.402  1.00 21.79 ? 95   LEU A CD2 1 
ATOM   604   N  N   . PHE A  1 79  ? 37.516  -11.711 26.377  1.00 21.91 ? 96   PHE A N   1 
ATOM   605   C  CA  . PHE A  1 79  ? 37.266  -12.565 27.529  1.00 21.89 ? 96   PHE A CA  1 
ATOM   606   C  C   . PHE A  1 79  ? 38.145  -13.812 27.460  1.00 21.26 ? 96   PHE A C   1 
ATOM   607   O  O   . PHE A  1 79  ? 38.793  -14.158 28.447  1.00 21.01 ? 96   PHE A O   1 
ATOM   608   C  CB  . PHE A  1 79  ? 35.769  -12.884 27.617  1.00 22.75 ? 96   PHE A CB  1 
ATOM   609   C  CG  . PHE A  1 79  ? 35.393  -13.983 28.603  1.00 24.79 ? 96   PHE A CG  1 
ATOM   610   C  CD1 . PHE A  1 79  ? 35.370  -13.740 29.972  1.00 26.05 ? 96   PHE A CD1 1 
ATOM   611   C  CD2 . PHE A  1 79  ? 35.051  -15.256 28.157  1.00 25.96 ? 96   PHE A CD2 1 
ATOM   612   C  CE1 . PHE A  1 79  ? 35.024  -14.746 30.867  1.00 27.46 ? 96   PHE A CE1 1 
ATOM   613   C  CE2 . PHE A  1 79  ? 34.710  -16.260 29.053  1.00 26.86 ? 96   PHE A CE2 1 
ATOM   614   C  CZ  . PHE A  1 79  ? 34.693  -16.002 30.406  1.00 27.37 ? 96   PHE A CZ  1 
ATOM   615   N  N   . TYR A  1 80  ? 38.165  -14.490 26.304  1.00 21.33 ? 97   TYR A N   1 
ATOM   616   C  CA  . TYR A  1 80  ? 38.906  -15.736 26.170  1.00 22.08 ? 97   TYR A CA  1 
ATOM   617   C  C   . TYR A  1 80  ? 40.412  -15.469 26.153  1.00 22.30 ? 97   TYR A C   1 
ATOM   618   O  O   . TYR A  1 80  ? 41.171  -16.270 26.696  1.00 22.31 ? 97   TYR A O   1 
ATOM   619   C  CB  . TYR A  1 80  ? 38.388  -16.572 24.991  1.00 22.19 ? 97   TYR A CB  1 
ATOM   620   C  CG  . TYR A  1 80  ? 37.070  -17.248 25.347  1.00 22.99 ? 97   TYR A CG  1 
ATOM   621   C  CD1 . TYR A  1 80  ? 37.034  -18.266 26.295  1.00 23.50 ? 97   TYR A CD1 1 
ATOM   622   C  CD2 . TYR A  1 80  ? 35.864  -16.851 24.780  1.00 23.28 ? 97   TYR A CD2 1 
ATOM   623   C  CE1 . TYR A  1 80  ? 35.843  -18.868 26.666  1.00 23.54 ? 97   TYR A CE1 1 
ATOM   624   C  CE2 . TYR A  1 80  ? 34.665  -17.451 25.140  1.00 23.94 ? 97   TYR A CE2 1 
ATOM   625   C  CZ  . TYR A  1 80  ? 34.657  -18.458 26.090  1.00 24.39 ? 97   TYR A CZ  1 
ATOM   626   O  OH  . TYR A  1 80  ? 33.493  -19.068 26.455  1.00 27.76 ? 97   TYR A OH  1 
ATOM   627   N  N   . ARG A  1 81  ? 40.843  -14.343 25.568  1.00 22.67 ? 98   ARG A N   1 
ATOM   628   C  CA  . ARG A  1 81  ? 42.249  -13.956 25.581  1.00 23.76 ? 98   ARG A CA  1 
ATOM   629   C  C   . ARG A  1 81  ? 42.755  -13.829 27.018  1.00 25.20 ? 98   ARG A C   1 
ATOM   630   O  O   . ARG A  1 81  ? 43.846  -14.294 27.346  1.00 24.52 ? 98   ARG A O   1 
ATOM   631   C  CB  . ARG A  1 81  ? 42.465  -12.618 24.863  1.00 24.95 ? 98   ARG A CB  1 
ATOM   632   C  CG  . ARG A  1 81  ? 43.840  -11.987 25.051  1.00 25.18 ? 98   ARG A CG  1 
ATOM   633   C  CD  . ARG A  1 81  ? 44.973  -12.879 24.572  1.00 25.84 ? 98   ARG A CD  1 
ATOM   634   N  NE  . ARG A  1 81  ? 46.287  -12.276 24.821  1.00 26.90 ? 98   ARG A NE  1 
ATOM   635   C  CZ  . ARG A  1 81  ? 46.823  -11.244 24.173  1.00 29.03 ? 98   ARG A CZ  1 
ATOM   636   N  NH1 . ARG A  1 81  ? 46.272  -10.766 23.072  1.00 29.17 ? 98   ARG A NH1 1 
ATOM   637   N  NH2 . ARG A  1 81  ? 47.949  -10.710 24.617  1.00 30.86 ? 98   ARG A NH2 1 
ATOM   638   N  N   . ILE A  1 82  ? 41.944  -13.171 27.853  1.00 26.39 ? 99   ILE A N   1 
ATOM   639   C  CA  . ILE A  1 82  ? 42.263  -12.890 29.243  1.00 28.87 ? 99   ILE A CA  1 
ATOM   640   C  C   . ILE A  1 82  ? 42.378  -14.193 30.033  1.00 29.70 ? 99   ILE A C   1 
ATOM   641   O  O   . ILE A  1 82  ? 43.316  -14.383 30.811  1.00 27.97 ? 99   ILE A O   1 
ATOM   642   C  CB  . ILE A  1 82  ? 41.186  -11.945 29.806  1.00 31.54 ? 99   ILE A CB  1 
ATOM   643   C  CG1 . ILE A  1 82  ? 41.518  -10.486 29.484  1.00 33.05 ? 99   ILE A CG1 1 
ATOM   644   C  CG2 . ILE A  1 82  ? 40.958  -12.173 31.297  1.00 34.60 ? 99   ILE A CG2 1 
ATOM   645   C  CD1 . ILE A  1 82  ? 40.322  -9.553  29.568  1.00 35.29 ? 99   ILE A CD1 1 
ATOM   646   N  N   . LEU A  1 83  ? 41.397  -15.077 29.834  1.00 29.06 ? 100  LEU A N   1 
ATOM   647   C  CA  . LEU A  1 83  ? 41.371  -16.363 30.507  1.00 29.52 ? 100  LEU A CA  1 
ATOM   648   C  C   . LEU A  1 83  ? 42.605  -17.169 30.107  1.00 28.44 ? 100  LEU A C   1 
ATOM   649   O  O   . LEU A  1 83  ? 43.264  -17.750 30.960  1.00 28.31 ? 100  LEU A O   1 
ATOM   650   C  CB  . LEU A  1 83  ? 40.048  -17.031 30.133  1.00 30.80 ? 100  LEU A CB  1 
ATOM   651   C  CG  . LEU A  1 83  ? 39.650  -18.303 30.883  1.00 32.53 ? 100  LEU A CG  1 
ATOM   652   C  CD1 . LEU A  1 83  ? 39.902  -18.266 32.387  1.00 33.08 ? 100  LEU A CD1 1 
ATOM   653   C  CD2 . LEU A  1 83  ? 38.167  -18.524 30.599  1.00 33.23 ? 100  LEU A CD2 1 
ATOM   654   N  N   . GLN A  1 84  ? 42.948  -17.155 28.814  1.00 29.14 ? 101  GLN A N   1 
ATOM   655   C  CA  . GLN A  1 84  ? 44.095  -17.898 28.307  1.00 28.59 ? 101  GLN A CA  1 
ATOM   656   C  C   . GLN A  1 84  ? 45.413  -17.315 28.827  1.00 30.45 ? 101  GLN A C   1 
ATOM   657   O  O   . GLN A  1 84  ? 46.351  -18.064 29.095  1.00 31.73 ? 101  GLN A O   1 
ATOM   658   C  CB  . GLN A  1 84  ? 44.051  -17.933 26.778  1.00 29.18 ? 101  GLN A CB  1 
ATOM   659   C  CG  . GLN A  1 84  ? 42.945  -18.828 26.226  1.00 29.67 ? 101  GLN A CG  1 
ATOM   660   C  CD  . GLN A  1 84  ? 42.647  -18.626 24.754  1.00 30.12 ? 101  GLN A CD  1 
ATOM   661   O  OE1 . GLN A  1 84  ? 42.964  -17.596 24.140  1.00 27.20 ? 101  GLN A OE1 1 
ATOM   662   N  NE2 . GLN A  1 84  ? 41.993  -19.623 24.179  1.00 29.59 ? 101  GLN A NE2 1 
ATOM   663   N  N   . ASP A  1 85  ? 45.491  -15.984 28.956  1.00 30.33 ? 102  ASP A N   1 
ATOM   664   C  CA  . ASP A  1 85  ? 46.694  -15.317 29.441  1.00 31.62 ? 102  ASP A CA  1 
ATOM   665   C  C   . ASP A  1 85  ? 47.083  -15.818 30.832  1.00 32.43 ? 102  ASP A C   1 
ATOM   666   O  O   . ASP A  1 85  ? 48.263  -16.028 31.099  1.00 31.89 ? 102  ASP A O   1 
ATOM   667   C  CB  . ASP A  1 85  ? 46.528  -13.806 29.528  1.00 32.32 ? 102  ASP A CB  1 
ATOM   668   C  CG  . ASP A  1 85  ? 46.687  -13.015 28.236  1.00 32.99 ? 102  ASP A CG  1 
ATOM   669   O  OD1 . ASP A  1 85  ? 47.133  -13.606 27.233  1.00 32.04 ? 102  ASP A OD1 1 
ATOM   670   O  OD2 . ASP A  1 85  ? 46.352  -11.805 28.245  1.00 33.06 ? 102  ASP A OD2 1 
ATOM   671   N  N   . ASP A  1 86  ? 46.087  -15.982 31.712  1.00 32.62 ? 103  ASP A N   1 
ATOM   672   C  CA  . ASP A  1 86  ? 46.328  -16.190 33.133  1.00 33.74 ? 103  ASP A CA  1 
ATOM   673   C  C   . ASP A  1 86  ? 45.542  -17.416 33.593  1.00 31.92 ? 103  ASP A C   1 
ATOM   674   O  O   . ASP A  1 86  ? 44.858  -17.387 34.616  1.00 33.96 ? 103  ASP A O   1 
ATOM   675   C  CB  . ASP A  1 86  ? 45.990  -14.915 33.892  1.00 35.29 ? 103  ASP A CB  1 
ATOM   676   C  CG  . ASP A  1 86  ? 46.455  -14.840 35.338  1.00 37.36 ? 103  ASP A CG  1 
ATOM   677   O  OD1 . ASP A  1 86  ? 47.567  -15.335 35.621  1.00 38.18 ? 103  ASP A OD1 1 
ATOM   678   O  OD2 . ASP A  1 86  ? 45.717  -14.245 36.157  1.00 38.66 ? 103  ASP A OD2 1 
ATOM   679   N  N   . ILE A  1 87  ? 45.681  -18.506 32.834  1.00 31.02 ? 104  ILE A N   1 
ATOM   680   C  CA  . ILE A  1 87  ? 44.740  -19.613 32.893  1.00 30.72 ? 104  ILE A CA  1 
ATOM   681   C  C   . ILE A  1 87  ? 44.826  -20.315 34.250  1.00 29.46 ? 104  ILE A C   1 
ATOM   682   O  O   . ILE A  1 87  ? 43.799  -20.618 34.848  1.00 27.61 ? 104  ILE A O   1 
ATOM   683   C  CB  . ILE A  1 87  ? 44.939  -20.575 31.700  1.00 31.52 ? 104  ILE A CB  1 
ATOM   684   C  CG1 . ILE A  1 87  ? 43.826  -21.621 31.625  1.00 31.95 ? 104  ILE A CG1 1 
ATOM   685   C  CG2 . ILE A  1 87  ? 46.321  -21.234 31.700  1.00 31.37 ? 104  ILE A CG2 1 
ATOM   686   C  CD1 . ILE A  1 87  ? 42.457  -21.053 31.306  1.00 32.81 ? 104  ILE A CD1 1 
ATOM   687   N  N   . GLU A  1 88  ? 46.040  -20.544 34.756  1.00 30.13 ? 105  GLU A N   1 
ATOM   688   C  CA  . GLU A  1 88  ? 46.197  -21.305 35.987  1.00 31.45 ? 105  GLU A CA  1 
ATOM   689   C  C   . GLU A  1 88  ? 45.514  -20.577 37.145  1.00 29.75 ? 105  GLU A C   1 
ATOM   690   O  O   . GLU A  1 88  ? 44.869  -21.211 37.977  1.00 28.09 ? 105  GLU A O   1 
ATOM   691   C  CB  . GLU A  1 88  ? 47.663  -21.610 36.294  1.00 32.41 ? 105  GLU A CB  1 
ATOM   692   C  CG  . GLU A  1 88  ? 47.837  -22.391 37.596  1.00 34.38 ? 105  GLU A CG  1 
ATOM   693   C  CD  . GLU A  1 88  ? 49.220  -22.964 37.842  1.00 35.51 ? 105  GLU A CD  1 
ATOM   694   O  OE1 . GLU A  1 88  ? 50.116  -22.768 36.995  1.00 36.96 ? 105  GLU A OE1 1 
ATOM   695   O  OE2 . GLU A  1 88  ? 49.392  -23.622 38.886  1.00 37.03 ? 105  GLU A OE2 1 
ATOM   696   N  N   . SER A  1 89  ? 45.645  -19.245 37.183  1.00 30.61 ? 106  SER A N   1 
ATOM   697   C  CA  . SER A  1 89  ? 45.111  -18.447 38.275  1.00 31.60 ? 106  SER A CA  1 
ATOM   698   C  C   . SER A  1 89  ? 43.612  -18.213 38.121  1.00 31.37 ? 106  SER A C   1 
ATOM   699   O  O   . SER A  1 89  ? 42.940  -17.956 39.114  1.00 31.17 ? 106  SER A O   1 
ATOM   700   C  CB  . SER A  1 89  ? 45.830  -17.125 38.387  1.00 33.73 ? 106  SER A CB  1 
ATOM   701   O  OG  . SER A  1 89  ? 47.217  -17.328 38.619  1.00 36.86 ? 106  SER A OG  1 
ATOM   702   N  N   . LEU A  1 90  ? 43.094  -18.259 36.885  1.00 31.33 ? 107  LEU A N   1 
ATOM   703   C  CA  . LEU A  1 90  ? 41.729  -17.816 36.633  1.00 31.80 ? 107  LEU A CA  1 
ATOM   704   C  C   . LEU A  1 90  ? 40.748  -18.987 36.547  1.00 31.73 ? 107  LEU A C   1 
ATOM   705   O  O   . LEU A  1 90  ? 39.551  -18.775 36.714  1.00 31.19 ? 107  LEU A O   1 
ATOM   706   C  CB  . LEU A  1 90  ? 41.691  -16.942 35.381  1.00 32.51 ? 107  LEU A CB  1 
ATOM   707   C  CG  . LEU A  1 90  ? 42.349  -15.563 35.513  1.00 32.27 ? 107  LEU A CG  1 
ATOM   708   C  CD1 . LEU A  1 90  ? 42.264  -14.787 34.211  1.00 32.36 ? 107  LEU A CD1 1 
ATOM   709   C  CD2 . LEU A  1 90  ? 41.721  -14.766 36.640  1.00 32.67 ? 107  LEU A CD2 1 
ATOM   710   N  N   . MET A  1 91  ? 41.237  -20.216 36.327  1.00 34.10 ? 108  MET A N   1 
ATOM   711   C  CA  . MET A  1 91  ? 40.360  -21.380 36.271  1.00 35.16 ? 108  MET A CA  1 
ATOM   712   C  C   . MET A  1 91  ? 39.616  -21.545 37.597  1.00 35.58 ? 108  MET A C   1 
ATOM   713   O  O   . MET A  1 91  ? 38.424  -21.832 37.584  1.00 35.92 ? 108  MET A O   1 
ATOM   714   C  CB  . MET A  1 91  ? 41.119  -22.659 35.882  1.00 38.43 ? 108  MET A CB  1 
ATOM   715   C  CG  . MET A  1 91  ? 41.542  -22.681 34.414  1.00 41.54 ? 108  MET A CG  1 
ATOM   716   S  SD  . MET A  1 91  ? 42.168  -24.245 33.757  1.00 46.22 ? 108  MET A SD  1 
ATOM   717   C  CE  . MET A  1 91  ? 43.762  -24.434 34.568  1.00 45.52 ? 108  MET A CE  1 
ATOM   718   N  N   . PRO A  1 92  ? 40.264  -21.355 38.775  1.00 35.66 ? 109  PRO A N   1 
ATOM   719   C  CA  . PRO A  1 92  ? 39.562  -21.391 40.063  1.00 35.17 ? 109  PRO A CA  1 
ATOM   720   C  C   . PRO A  1 92  ? 38.590  -20.245 40.334  1.00 34.59 ? 109  PRO A C   1 
ATOM   721   O  O   . PRO A  1 92  ? 37.846  -20.298 41.311  1.00 33.52 ? 109  PRO A O   1 
ATOM   722   C  CB  . PRO A  1 92  ? 40.697  -21.401 41.112  1.00 36.54 ? 109  PRO A CB  1 
ATOM   723   C  CG  . PRO A  1 92  ? 41.949  -21.723 40.332  1.00 36.99 ? 109  PRO A CG  1 
ATOM   724   C  CD  . PRO A  1 92  ? 41.711  -21.163 38.942  1.00 36.79 ? 109  PRO A CD  1 
ATOM   725   N  N   . ILE A  1 93  ? 38.629  -19.204 39.491  1.00 35.22 ? 110  ILE A N   1 
ATOM   726   C  CA  . ILE A  1 93  ? 37.741  -18.059 39.613  1.00 34.18 ? 110  ILE A CA  1 
ATOM   727   C  C   . ILE A  1 93  ? 36.487  -18.302 38.775  1.00 32.41 ? 110  ILE A C   1 
ATOM   728   O  O   . ILE A  1 93  ? 35.374  -18.141 39.271  1.00 31.84 ? 110  ILE A O   1 
ATOM   729   C  CB  . ILE A  1 93  ? 38.461  -16.760 39.191  1.00 34.74 ? 110  ILE A CB  1 
ATOM   730   C  CG1 . ILE A  1 93  ? 39.699  -16.487 40.058  1.00 36.95 ? 110  ILE A CG1 1 
ATOM   731   C  CG2 . ILE A  1 93  ? 37.500  -15.570 39.190  1.00 33.77 ? 110  ILE A CG2 1 
ATOM   732   C  CD1 . ILE A  1 93  ? 39.395  -16.215 41.522  1.00 36.51 ? 110  ILE A CD1 1 
ATOM   733   N  N   . VAL A  1 94  ? 36.682  -18.675 37.505  1.00 30.72 ? 111  VAL A N   1 
ATOM   734   C  CA  . VAL A  1 94  ? 35.575  -18.855 36.576  1.00 31.32 ? 111  VAL A CA  1 
ATOM   735   C  C   . VAL A  1 94  ? 34.865  -20.176 36.865  1.00 30.28 ? 111  VAL A C   1 
ATOM   736   O  O   . VAL A  1 94  ? 33.693  -20.320 36.525  1.00 28.08 ? 111  VAL A O   1 
ATOM   737   C  CB  . VAL A  1 94  ? 35.987  -18.781 35.091  1.00 31.70 ? 111  VAL A CB  1 
ATOM   738   C  CG1 . VAL A  1 94  ? 36.467  -17.386 34.710  1.00 33.06 ? 111  VAL A CG1 1 
ATOM   739   C  CG2 . VAL A  1 94  ? 37.019  -19.837 34.715  1.00 31.40 ? 111  VAL A CG2 1 
ATOM   740   N  N   . TYR A  1 95  ? 35.578  -21.139 37.466  1.00 30.95 ? 112  TYR A N   1 
ATOM   741   C  CA  . TYR A  1 95  ? 34.980  -22.428 37.780  1.00 32.39 ? 112  TYR A CA  1 
ATOM   742   C  C   . TYR A  1 95  ? 35.115  -22.702 39.283  1.00 34.25 ? 112  TYR A C   1 
ATOM   743   O  O   . TYR A  1 95  ? 35.138  -21.770 40.084  1.00 34.93 ? 112  TYR A O   1 
ATOM   744   C  CB  . TYR A  1 95  ? 35.584  -23.451 36.807  1.00 31.79 ? 112  TYR A CB  1 
ATOM   745   C  CG  . TYR A  1 95  ? 34.793  -24.750 36.774  1.00 32.14 ? 112  TYR A CG  1 
ATOM   746   C  CD1 . TYR A  1 95  ? 33.410  -24.731 36.649  1.00 32.40 ? 112  TYR A CD1 1 
ATOM   747   C  CD2 . TYR A  1 95  ? 35.415  -25.980 36.958  1.00 33.24 ? 112  TYR A CD2 1 
ATOM   748   C  CE1 . TYR A  1 95  ? 32.668  -25.898 36.669  1.00 35.16 ? 112  TYR A CE1 1 
ATOM   749   C  CE2 . TYR A  1 95  ? 34.682  -27.157 36.982  1.00 34.67 ? 112  TYR A CE2 1 
ATOM   750   C  CZ  . TYR A  1 95  ? 33.307  -27.112 36.838  1.00 36.10 ? 112  TYR A CZ  1 
ATOM   751   O  OH  . TYR A  1 95  ? 32.558  -28.247 36.851  1.00 45.43 ? 112  TYR A OH  1 
ATOM   752   N  N   A THR A  1 96  ? 35.171  -23.988 39.655  0.50 35.15 ? 113  THR A N   1 
ATOM   753   N  N   B THR A  1 96  ? 35.184  -23.987 39.651  0.50 35.22 ? 113  THR A N   1 
ATOM   754   C  CA  A THR A  1 96  ? 35.233  -24.414 41.046  0.50 34.60 ? 113  THR A CA  1 
ATOM   755   C  CA  B THR A  1 96  ? 35.231  -24.412 41.042  0.50 34.76 ? 113  THR A CA  1 
ATOM   756   C  C   A THR A  1 96  ? 36.556  -23.953 41.653  0.50 34.79 ? 113  THR A C   1 
ATOM   757   C  C   B THR A  1 96  ? 36.556  -23.964 41.657  0.50 34.86 ? 113  THR A C   1 
ATOM   758   O  O   A THR A  1 96  ? 37.589  -24.074 40.998  0.50 34.72 ? 113  THR A O   1 
ATOM   759   O  O   B THR A  1 96  ? 37.592  -24.103 41.009  0.50 34.80 ? 113  THR A O   1 
ATOM   760   C  CB  A THR A  1 96  ? 35.104  -25.937 41.115  0.50 34.76 ? 113  THR A CB  1 
ATOM   761   C  CB  B THR A  1 96  ? 35.077  -25.933 41.090  0.50 34.96 ? 113  THR A CB  1 
ATOM   762   O  OG1 A THR A  1 96  ? 33.851  -26.261 40.525  0.50 34.02 ? 113  THR A OG1 1 
ATOM   763   O  OG1 B THR A  1 96  ? 34.806  -26.275 42.445  0.50 35.32 ? 113  THR A OG1 1 
ATOM   764   C  CG2 A THR A  1 96  ? 35.166  -26.473 42.535  0.50 35.03 ? 113  THR A CG2 1 
ATOM   765   C  CG2 B THR A  1 96  ? 36.322  -26.657 40.608  0.50 34.66 ? 113  THR A CG2 1 
ATOM   766   N  N   . PRO A  1 97  ? 36.594  -23.443 42.910  1.00 35.09 ? 114  PRO A N   1 
ATOM   767   C  CA  . PRO A  1 97  ? 35.411  -23.318 43.777  1.00 36.31 ? 114  PRO A CA  1 
ATOM   768   C  C   . PRO A  1 97  ? 34.632  -22.005 43.886  1.00 35.86 ? 114  PRO A C   1 
ATOM   769   O  O   . PRO A  1 97  ? 33.682  -21.925 44.663  1.00 36.58 ? 114  PRO A O   1 
ATOM   770   C  CB  . PRO A  1 97  ? 36.112  -23.631 45.111  1.00 36.48 ? 114  PRO A CB  1 
ATOM   771   C  CG  . PRO A  1 97  ? 37.397  -22.840 45.035  1.00 37.12 ? 114  PRO A CG  1 
ATOM   772   C  CD  . PRO A  1 97  ? 37.823  -22.984 43.581  1.00 36.99 ? 114  PRO A CD  1 
ATOM   773   N  N   . THR A  1 98  ? 35.013  -20.978 43.119  1.00 34.25 ? 115  THR A N   1 
ATOM   774   C  CA  . THR A  1 98  ? 34.388  -19.671 43.260  1.00 33.39 ? 115  THR A CA  1 
ATOM   775   C  C   . THR A  1 98  ? 32.963  -19.675 42.704  1.00 33.82 ? 115  THR A C   1 
ATOM   776   O  O   . THR A  1 98  ? 32.073  -19.050 43.280  1.00 33.31 ? 115  THR A O   1 
ATOM   777   C  CB  . THR A  1 98  ? 35.230  -18.602 42.565  1.00 33.84 ? 115  THR A CB  1 
ATOM   778   O  OG1 . THR A  1 98  ? 36.525  -18.639 43.155  1.00 32.78 ? 115  THR A OG1 1 
ATOM   779   C  CG2 . THR A  1 98  ? 34.641  -17.211 42.723  1.00 32.99 ? 115  THR A CG2 1 
ATOM   780   N  N   . VAL A  1 99  ? 32.756  -20.357 41.570  1.00 33.18 ? 116  VAL A N   1 
ATOM   781   C  CA  . VAL A  1 99  ? 31.591  -20.113 40.733  1.00 32.73 ? 116  VAL A CA  1 
ATOM   782   C  C   . VAL A  1 99  ? 30.300  -20.370 41.514  1.00 32.66 ? 116  VAL A C   1 
ATOM   783   O  O   . VAL A  1 99  ? 29.329  -19.636 41.355  1.00 33.08 ? 116  VAL A O   1 
ATOM   784   C  CB  . VAL A  1 99  ? 31.631  -20.924 39.421  1.00 33.66 ? 116  VAL A CB  1 
ATOM   785   C  CG1 . VAL A  1 99  ? 31.710  -22.429 39.659  1.00 34.06 ? 116  VAL A CG1 1 
ATOM   786   C  CG2 . VAL A  1 99  ? 30.448  -20.589 38.522  1.00 34.13 ? 116  VAL A CG2 1 
ATOM   787   N  N   . GLY A  1 100 ? 30.290  -21.402 42.362  1.00 33.04 ? 117  GLY A N   1 
ATOM   788   C  CA  . GLY A  1 100 ? 29.083  -21.790 43.076  1.00 34.31 ? 117  GLY A CA  1 
ATOM   789   C  C   . GLY A  1 100 ? 28.631  -20.758 44.110  1.00 35.74 ? 117  GLY A C   1 
ATOM   790   O  O   . GLY A  1 100 ? 27.460  -20.731 44.479  1.00 39.05 ? 117  GLY A O   1 
ATOM   791   N  N   . LEU A  1 101 ? 29.557  -19.910 44.575  1.00 36.09 ? 118  LEU A N   1 
ATOM   792   C  CA  . LEU A  1 101 ? 29.257  -18.913 45.594  1.00 37.60 ? 118  LEU A CA  1 
ATOM   793   C  C   . LEU A  1 101 ? 28.511  -17.710 45.009  1.00 38.45 ? 118  LEU A C   1 
ATOM   794   O  O   . LEU A  1 101 ? 27.804  -17.020 45.740  1.00 35.92 ? 118  LEU A O   1 
ATOM   795   C  CB  . LEU A  1 101 ? 30.567  -18.479 46.250  1.00 38.32 ? 118  LEU A CB  1 
ATOM   796   C  CG  . LEU A  1 101 ? 31.340  -19.572 46.993  1.00 40.23 ? 118  LEU A CG  1 
ATOM   797   C  CD1 . LEU A  1 101 ? 32.755  -19.118 47.302  1.00 41.40 ? 118  LEU A CD1 1 
ATOM   798   C  CD2 . LEU A  1 101 ? 30.616  -19.977 48.269  1.00 41.94 ? 118  LEU A CD2 1 
ATOM   799   N  N   . ALA A  1 102 ? 28.649  -17.478 43.695  1.00 39.80 ? 119  ALA A N   1 
ATOM   800   C  CA  . ALA A  1 102 ? 28.281  -16.214 43.071  1.00 40.42 ? 119  ALA A CA  1 
ATOM   801   C  C   . ALA A  1 102 ? 26.775  -15.943 43.119  1.00 40.48 ? 119  ALA A C   1 
ATOM   802   O  O   . ALA A  1 102 ? 26.369  -14.857 43.525  1.00 37.72 ? 119  ALA A O   1 
ATOM   803   C  CB  . ALA A  1 102 ? 28.789  -16.185 41.648  1.00 42.45 ? 119  ALA A CB  1 
HETATM 804   N  N   . CSX A  1 103 ? 25.948  -16.905 42.686  1.00 41.79 ? 120  CSX A N   1 
HETATM 805   C  CA  . CSX A  1 103 ? 24.504  -16.707 42.652  1.00 43.61 ? 120  CSX A CA  1 
HETATM 806   C  CB  . CSX A  1 103 ? 23.769  -17.874 41.988  1.00 47.48 ? 120  CSX A CB  1 
HETATM 807   S  SG  . CSX A  1 103 ? 24.099  -17.967 40.211  1.00 50.76 ? 120  CSX A SG  1 
HETATM 808   C  C   . CSX A  1 103 ? 23.954  -16.493 44.062  1.00 45.62 ? 120  CSX A C   1 
HETATM 809   O  O   . CSX A  1 103 ? 23.152  -15.583 44.288  1.00 46.94 ? 120  CSX A O   1 
HETATM 810   O  OD  . CSX A  1 103 ? 23.702  -16.630 39.630  1.00 48.35 ? 120  CSX A OD  1 
ATOM   811   N  N   A SER A  1 104 ? 24.390  -17.343 45.000  0.50 44.58 ? 121  SER A N   1 
ATOM   812   N  N   B SER A  1 104 ? 24.389  -17.336 45.004  0.50 44.79 ? 121  SER A N   1 
ATOM   813   C  CA  A SER A  1 104 ? 23.947  -17.274 46.382  0.50 44.91 ? 121  SER A CA  1 
ATOM   814   C  CA  B SER A  1 104 ? 23.922  -17.265 46.379  0.50 45.28 ? 121  SER A CA  1 
ATOM   815   C  C   A SER A  1 104 ? 24.192  -15.878 46.950  0.50 45.15 ? 121  SER A C   1 
ATOM   816   C  C   B SER A  1 104 ? 24.199  -15.884 46.970  0.50 45.33 ? 121  SER A C   1 
ATOM   817   O  O   A SER A  1 104 ? 23.337  -15.325 47.637  0.50 46.16 ? 121  SER A O   1 
ATOM   818   O  O   B SER A  1 104 ? 23.370  -15.343 47.698  0.50 46.21 ? 121  SER A O   1 
ATOM   819   C  CB  A SER A  1 104 ? 24.630  -18.328 47.222  0.50 45.15 ? 121  SER A CB  1 
ATOM   820   C  CB  B SER A  1 104 ? 24.542  -18.358 47.215  0.50 45.85 ? 121  SER A CB  1 
ATOM   821   O  OG  A SER A  1 104 ? 24.388  -19.631 46.710  0.50 43.65 ? 121  SER A OG  1 
ATOM   822   O  OG  B SER A  1 104 ? 25.957  -18.358 47.082  0.50 44.91 ? 121  SER A OG  1 
ATOM   823   N  N   . GLN A  1 105 ? 25.368  -15.317 46.647  1.00 45.24 ? 122  GLN A N   1 
ATOM   824   C  CA  . GLN A  1 105 ? 25.760  -14.018 47.169  1.00 46.78 ? 122  GLN A CA  1 
ATOM   825   C  C   . GLN A  1 105 ? 25.049  -12.882 46.425  1.00 45.51 ? 122  GLN A C   1 
ATOM   826   O  O   . GLN A  1 105 ? 24.551  -11.959 47.069  1.00 44.81 ? 122  GLN A O   1 
ATOM   827   C  CB  . GLN A  1 105 ? 27.286  -13.904 47.184  1.00 48.65 ? 122  GLN A CB  1 
ATOM   828   C  CG  . GLN A  1 105 ? 27.921  -14.286 48.521  1.00 53.71 ? 122  GLN A CG  1 
ATOM   829   C  CD  . GLN A  1 105 ? 27.463  -15.624 49.067  1.00 55.27 ? 122  GLN A CD  1 
ATOM   830   O  OE1 . GLN A  1 105 ? 26.696  -15.691 50.035  1.00 55.87 ? 122  GLN A OE1 1 
ATOM   831   N  NE2 . GLN A  1 105 ? 27.921  -16.705 48.451  1.00 55.93 ? 122  GLN A NE2 1 
ATOM   832   N  N   . TYR A  1 106 ? 24.994  -12.947 45.085  1.00 42.00 ? 123  TYR A N   1 
ATOM   833   C  CA  . TYR A  1 106 ? 24.643  -11.778 44.283  1.00 42.47 ? 123  TYR A CA  1 
ATOM   834   C  C   . TYR A  1 106 ? 23.336  -11.956 43.509  1.00 39.19 ? 123  TYR A C   1 
ATOM   835   O  O   . TYR A  1 106 ? 22.639  -10.974 43.261  1.00 37.44 ? 123  TYR A O   1 
ATOM   836   C  CB  . TYR A  1 106 ? 25.748  -11.432 43.280  1.00 44.22 ? 123  TYR A CB  1 
ATOM   837   C  CG  . TYR A  1 106 ? 27.033  -10.917 43.913  1.00 47.46 ? 123  TYR A CG  1 
ATOM   838   C  CD1 . TYR A  1 106 ? 27.071  -9.683  44.552  1.00 49.37 ? 123  TYR A CD1 1 
ATOM   839   C  CD2 . TYR A  1 106 ? 28.212  -11.650 43.848  1.00 50.67 ? 123  TYR A CD2 1 
ATOM   840   C  CE1 . TYR A  1 106 ? 28.236  -9.203  45.129  1.00 51.31 ? 123  TYR A CE1 1 
ATOM   841   C  CE2 . TYR A  1 106 ? 29.386  -11.178 44.415  1.00 53.81 ? 123  TYR A CE2 1 
ATOM   842   C  CZ  . TYR A  1 106 ? 29.397  -9.952  45.058  1.00 54.83 ? 123  TYR A CZ  1 
ATOM   843   O  OH  . TYR A  1 106 ? 30.548  -9.478  45.617  1.00 59.65 ? 123  TYR A OH  1 
ATOM   844   N  N   . GLY A  1 107 ? 23.020  -13.186 43.095  1.00 37.54 ? 124  GLY A N   1 
ATOM   845   C  CA  . GLY A  1 107 ? 22.022  -13.400 42.060  1.00 37.38 ? 124  GLY A CA  1 
ATOM   846   C  C   . GLY A  1 107 ? 22.561  -12.954 40.701  1.00 37.03 ? 124  GLY A C   1 
ATOM   847   O  O   . GLY A  1 107 ? 23.763  -13.022 40.459  1.00 37.09 ? 124  GLY A O   1 
ATOM   848   N  N   . HIS A  1 108 ? 21.668  -12.492 39.820  1.00 35.37 ? 125  HIS A N   1 
ATOM   849   C  CA  . HIS A  1 108 ? 22.060  -12.016 38.502  1.00 33.94 ? 125  HIS A CA  1 
ATOM   850   C  C   . HIS A  1 108 ? 21.017  -11.019 37.997  1.00 32.14 ? 125  HIS A C   1 
ATOM   851   O  O   . HIS A  1 108 ? 19.836  -11.126 38.335  1.00 32.02 ? 125  HIS A O   1 
ATOM   852   C  CB  . HIS A  1 108 ? 22.252  -13.201 37.546  1.00 33.71 ? 125  HIS A CB  1 
ATOM   853   C  CG  . HIS A  1 108 ? 22.781  -12.845 36.193  1.00 34.71 ? 125  HIS A CG  1 
ATOM   854   N  ND1 . HIS A  1 108 ? 24.079  -12.436 35.977  1.00 34.73 ? 125  HIS A ND1 1 
ATOM   855   C  CD2 . HIS A  1 108 ? 22.185  -12.826 34.990  1.00 33.57 ? 125  HIS A CD2 1 
ATOM   856   C  CE1 . HIS A  1 108 ? 24.253  -12.194 34.685  1.00 33.92 ? 125  HIS A CE1 1 
ATOM   857   N  NE2 . HIS A  1 108 ? 23.114  -12.421 34.068  1.00 33.37 ? 125  HIS A NE2 1 
ATOM   858   N  N   . ILE A  1 109 ? 21.483  -10.029 37.225  1.00 29.38 ? 126  ILE A N   1 
ATOM   859   C  CA  . ILE A  1 109 ? 20.609  -9.164  36.448  1.00 28.10 ? 126  ILE A CA  1 
ATOM   860   C  C   . ILE A  1 109 ? 20.768  -9.551  34.981  1.00 27.00 ? 126  ILE A C   1 
ATOM   861   O  O   . ILE A  1 109 ? 21.859  -9.437  34.421  1.00 27.42 ? 126  ILE A O   1 
ATOM   862   C  CB  . ILE A  1 109 ? 20.921  -7.674  36.685  1.00 29.25 ? 126  ILE A CB  1 
ATOM   863   C  CG1 . ILE A  1 109 ? 20.833  -7.311  38.167  1.00 31.19 ? 126  ILE A CG1 1 
ATOM   864   C  CG2 . ILE A  1 109 ? 20.017  -6.783  35.831  1.00 29.14 ? 126  ILE A CG2 1 
ATOM   865   C  CD1 . ILE A  1 109 ? 21.179  -5.865  38.474  1.00 33.29 ? 126  ILE A CD1 1 
ATOM   866   N  N   . PHE A  1 110 ? 19.660  -9.981  34.371  1.00 25.34 ? 127  PHE A N   1 
ATOM   867   C  CA  . PHE A  1 110 ? 19.670  -10.585 33.050  1.00 26.06 ? 127  PHE A CA  1 
ATOM   868   C  C   . PHE A  1 110 ? 19.574  -9.526  31.958  1.00 27.89 ? 127  PHE A C   1 
ATOM   869   O  O   . PHE A  1 110 ? 18.810  -8.565  32.077  1.00 26.91 ? 127  PHE A O   1 
ATOM   870   C  CB  . PHE A  1 110 ? 18.511  -11.579 32.943  1.00 26.23 ? 127  PHE A CB  1 
ATOM   871   C  CG  . PHE A  1 110 ? 18.837  -12.923 33.575  1.00 26.86 ? 127  PHE A CG  1 
ATOM   872   C  CD1 . PHE A  1 110 ? 19.480  -13.917 32.838  1.00 27.95 ? 127  PHE A CD1 1 
ATOM   873   C  CD2 . PHE A  1 110 ? 18.519  -13.182 34.901  1.00 26.87 ? 127  PHE A CD2 1 
ATOM   874   C  CE1 . PHE A  1 110 ? 19.791  -15.138 33.417  1.00 28.50 ? 127  PHE A CE1 1 
ATOM   875   C  CE2 . PHE A  1 110 ? 18.842  -14.402 35.478  1.00 27.98 ? 127  PHE A CE2 1 
ATOM   876   C  CZ  . PHE A  1 110 ? 19.477  -15.374 34.739  1.00 27.79 ? 127  PHE A CZ  1 
ATOM   877   N  N   . ARG A  1 111 ? 20.392  -9.720  30.913  1.00 28.50 ? 128  ARG A N   1 
ATOM   878   C  CA  . ARG A  1 111 ? 20.139  -9.163  29.595  1.00 28.67 ? 128  ARG A CA  1 
ATOM   879   C  C   . ARG A  1 111 ? 20.244  -10.319 28.601  1.00 28.91 ? 128  ARG A C   1 
ATOM   880   O  O   . ARG A  1 111 ? 19.221  -10.851 28.173  1.00 27.10 ? 128  ARG A O   1 
ATOM   881   C  CB  . ARG A  1 111 ? 21.054  -7.965  29.297  1.00 30.44 ? 128  ARG A CB  1 
ATOM   882   C  CG  . ARG A  1 111 ? 20.802  -7.308  27.946  1.00 30.76 ? 128  ARG A CG  1 
ATOM   883   C  CD  . ARG A  1 111 ? 21.898  -6.315  27.565  1.00 31.93 ? 128  ARG A CD  1 
ATOM   884   N  NE  . ARG A  1 111 ? 23.097  -6.952  27.003  1.00 31.23 ? 128  ARG A NE  1 
ATOM   885   C  CZ  . ARG A  1 111 ? 23.248  -7.380  25.749  1.00 31.43 ? 128  ARG A CZ  1 
ATOM   886   N  NH1 . ARG A  1 111 ? 22.286  -7.220  24.856  1.00 30.50 ? 128  ARG A NH1 1 
ATOM   887   N  NH2 . ARG A  1 111 ? 24.383  -7.954  25.382  1.00 32.53 ? 128  ARG A NH2 1 
ATOM   888   N  N   A ARG A  1 112 ? 21.482  -10.704 28.256  0.50 28.85 ? 129  ARG A N   1 
ATOM   889   N  N   B ARG A  1 112 ? 21.477  -10.722 28.268  0.50 29.14 ? 129  ARG A N   1 
ATOM   890   C  CA  A ARG A  1 112 ? 21.723  -11.844 27.387  0.50 30.49 ? 129  ARG A CA  1 
ATOM   891   C  CA  B ARG A  1 112 ? 21.704  -11.824 27.347  0.50 31.00 ? 129  ARG A CA  1 
ATOM   892   C  C   A ARG A  1 112 ? 21.366  -13.124 28.133  0.50 30.68 ? 129  ARG A C   1 
ATOM   893   C  C   B ARG A  1 112 ? 21.460  -13.141 28.084  0.50 30.97 ? 129  ARG A C   1 
ATOM   894   O  O   A ARG A  1 112 ? 21.556  -13.208 29.346  0.50 29.95 ? 129  ARG A O   1 
ATOM   895   O  O   B ARG A  1 112 ? 21.829  -13.269 29.251  0.50 30.47 ? 129  ARG A O   1 
ATOM   896   C  CB  A ARG A  1 112 ? 23.192  -11.990 26.972  0.50 32.00 ? 129  ARG A CB  1 
ATOM   897   C  CB  B ARG A  1 112 ? 23.133  -11.738 26.795  0.50 32.93 ? 129  ARG A CB  1 
ATOM   898   C  CG  A ARG A  1 112 ? 23.686  -10.976 25.954  0.50 32.51 ? 129  ARG A CG  1 
ATOM   899   C  CG  B ARG A  1 112 ? 23.479  -12.749 25.711  0.50 34.24 ? 129  ARG A CG  1 
ATOM   900   C  CD  A ARG A  1 112 ? 25.171  -11.152 25.653  0.50 33.75 ? 129  ARG A CD  1 
ATOM   901   C  CD  B ARG A  1 112 ? 24.971  -12.760 25.404  0.50 34.79 ? 129  ARG A CD  1 
ATOM   902   N  NE  A ARG A  1 112 ? 25.481  -12.220 24.694  0.50 34.62 ? 129  ARG A NE  1 
ATOM   903   N  NE  B ARG A  1 112 ? 25.326  -13.610 24.262  0.50 36.16 ? 129  ARG A NE  1 
ATOM   904   C  CZ  A ARG A  1 112 ? 26.322  -13.230 24.909  0.50 35.58 ? 129  ARG A CZ  1 
ATOM   905   C  CZ  B ARG A  1 112 ? 24.996  -13.370 22.998  0.50 36.72 ? 129  ARG A CZ  1 
ATOM   906   N  NH1 A ARG A  1 112 ? 26.794  -13.459 26.121  0.50 36.12 ? 129  ARG A NH1 1 
ATOM   907   N  NH1 B ARG A  1 112 ? 24.249  -12.328 22.691  0.50 36.11 ? 129  ARG A NH1 1 
ATOM   908   N  NH2 A ARG A  1 112 ? 26.670  -14.024 23.912  0.50 35.60 ? 129  ARG A NH2 1 
ATOM   909   N  NH2 B ARG A  1 112 ? 25.413  -14.176 22.039  0.50 38.64 ? 129  ARG A NH2 1 
ATOM   910   N  N   . PRO A  1 113 ? 20.828  -14.154 27.441  1.00 31.36 ? 130  PRO A N   1 
ATOM   911   C  CA  . PRO A  1 113 ? 20.668  -15.471 28.058  1.00 32.30 ? 130  PRO A CA  1 
ATOM   912   C  C   . PRO A  1 113 ? 22.039  -16.051 28.411  1.00 34.03 ? 130  PRO A C   1 
ATOM   913   O  O   . PRO A  1 113 ? 22.978  -15.928 27.631  1.00 33.22 ? 130  PRO A O   1 
ATOM   914   C  CB  . PRO A  1 113 ? 19.939  -16.330 27.006  1.00 33.30 ? 130  PRO A CB  1 
ATOM   915   C  CG  . PRO A  1 113 ? 19.469  -15.358 25.938  1.00 32.93 ? 130  PRO A CG  1 
ATOM   916   C  CD  . PRO A  1 113 ? 20.291  -14.088 26.072  1.00 32.40 ? 130  PRO A CD  1 
ATOM   917   N  N   . LYS A  1 114 ? 22.135  -16.663 29.595  1.00 37.23 ? 131  LYS A N   1 
ATOM   918   C  CA  . LYS A  1 114 ? 23.345  -17.336 30.047  1.00 39.34 ? 131  LYS A CA  1 
ATOM   919   C  C   . LYS A  1 114 ? 23.357  -18.775 29.530  1.00 38.43 ? 131  LYS A C   1 
ATOM   920   O  O   . LYS A  1 114 ? 24.413  -19.371 29.315  1.00 40.62 ? 131  LYS A O   1 
ATOM   921   C  CB  . LYS A  1 114 ? 23.375  -17.288 31.579  1.00 40.32 ? 131  LYS A CB  1 
ATOM   922   N  N   . GLY A  1 115 ? 22.153  -19.318 29.340  1.00 33.83 ? 132  GLY A N   1 
ATOM   923   C  CA  . GLY A  1 115 ? 21.941  -20.679 28.886  1.00 30.59 ? 132  GLY A CA  1 
ATOM   924   C  C   . GLY A  1 115 ? 20.450  -20.988 28.963  1.00 28.42 ? 132  GLY A C   1 
ATOM   925   O  O   . GLY A  1 115 ? 19.650  -20.064 29.111  1.00 26.79 ? 132  GLY A O   1 
ATOM   926   N  N   . LEU A  1 116 ? 20.094  -22.274 28.867  1.00 24.83 ? 133  LEU A N   1 
ATOM   927   C  CA  . LEU A  1 116 ? 18.703  -22.691 28.923  1.00 23.31 ? 133  LEU A CA  1 
ATOM   928   C  C   . LEU A  1 116 ? 18.355  -23.111 30.343  1.00 22.45 ? 133  LEU A C   1 
ATOM   929   O  O   . LEU A  1 116 ? 19.117  -23.839 30.978  1.00 22.26 ? 133  LEU A O   1 
ATOM   930   C  CB  . LEU A  1 116 ? 18.419  -23.839 27.957  1.00 23.15 ? 133  LEU A CB  1 
ATOM   931   C  CG  . LEU A  1 116 ? 18.315  -23.481 26.474  1.00 23.60 ? 133  LEU A CG  1 
ATOM   932   C  CD1 . LEU A  1 116 ? 18.064  -24.756 25.701  1.00 24.08 ? 133  LEU A CD1 1 
ATOM   933   C  CD2 . LEU A  1 116 ? 17.229  -22.455 26.183  1.00 23.65 ? 133  LEU A CD2 1 
ATOM   934   N  N   . PHE A  1 117 ? 17.177  -22.673 30.797  1.00 20.89 ? 134  PHE A N   1 
ATOM   935   C  CA  . PHE A  1 117 ? 16.553  -23.172 32.009  1.00 21.77 ? 134  PHE A CA  1 
ATOM   936   C  C   . PHE A  1 117 ? 15.341  -24.010 31.615  1.00 22.05 ? 134  PHE A C   1 
ATOM   937   O  O   . PHE A  1 117 ? 14.438  -23.517 30.943  1.00 21.94 ? 134  PHE A O   1 
ATOM   938   C  CB  . PHE A  1 117 ? 16.113  -22.037 32.936  1.00 22.13 ? 134  PHE A CB  1 
ATOM   939   C  CG  . PHE A  1 117 ? 17.256  -21.208 33.491  1.00 22.71 ? 134  PHE A CG  1 
ATOM   940   C  CD1 . PHE A  1 117 ? 17.885  -21.565 34.679  1.00 23.26 ? 134  PHE A CD1 1 
ATOM   941   C  CD2 . PHE A  1 117 ? 17.712  -20.084 32.815  1.00 24.40 ? 134  PHE A CD2 1 
ATOM   942   C  CE1 . PHE A  1 117 ? 18.928  -20.804 35.178  1.00 24.56 ? 134  PHE A CE1 1 
ATOM   943   C  CE2 . PHE A  1 117 ? 18.756  -19.326 33.323  1.00 24.65 ? 134  PHE A CE2 1 
ATOM   944   C  CZ  . PHE A  1 117 ? 19.359  -19.686 34.499  1.00 24.49 ? 134  PHE A CZ  1 
ATOM   945   N  N   . ILE A  1 118 ? 15.349  -25.284 32.018  1.00 21.72 ? 135  ILE A N   1 
ATOM   946   C  CA  . ILE A  1 118 ? 14.244  -26.192 31.764  1.00 22.98 ? 135  ILE A CA  1 
ATOM   947   C  C   . ILE A  1 118 ? 13.699  -26.623 33.119  1.00 22.78 ? 135  ILE A C   1 
ATOM   948   O  O   . ILE A  1 118 ? 14.417  -27.269 33.879  1.00 22.86 ? 135  ILE A O   1 
ATOM   949   C  CB  . ILE A  1 118 ? 14.703  -27.400 30.922  1.00 23.79 ? 135  ILE A CB  1 
ATOM   950   C  CG1 . ILE A  1 118 ? 15.253  -26.977 29.556  1.00 23.44 ? 135  ILE A CG1 1 
ATOM   951   C  CG2 . ILE A  1 118 ? 13.588  -28.435 30.782  1.00 23.99 ? 135  ILE A CG2 1 
ATOM   952   C  CD1 . ILE A  1 118 ? 16.046  -28.060 28.849  1.00 23.58 ? 135  ILE A CD1 1 
ATOM   953   N  N   . SER A  1 119 ? 12.445  -26.258 33.416  1.00 22.29 ? 136  SER A N   1 
ATOM   954   C  CA  . SER A  1 119 ? 11.862  -26.569 34.711  1.00 22.27 ? 136  SER A CA  1 
ATOM   955   C  C   . SER A  1 119 ? 10.887  -27.738 34.592  1.00 22.50 ? 136  SER A C   1 
ATOM   956   O  O   . SER A  1 119 ? 10.409  -28.056 33.504  1.00 22.83 ? 136  SER A O   1 
ATOM   957   C  CB  . SER A  1 119 ? 11.205  -25.366 35.333  1.00 23.28 ? 136  SER A CB  1 
ATOM   958   O  OG  . SER A  1 119 ? 9.895   -25.148 34.830  1.00 24.27 ? 136  SER A OG  1 
ATOM   959   N  N   . ILE A  1 120 ? 10.595  -28.364 35.738  1.00 23.16 ? 137  ILE A N   1 
ATOM   960   C  CA  . ILE A  1 120 ? 9.635   -29.454 35.805  1.00 24.89 ? 137  ILE A CA  1 
ATOM   961   C  C   . ILE A  1 120 ? 8.253   -28.939 35.390  1.00 24.50 ? 137  ILE A C   1 
ATOM   962   O  O   . ILE A  1 120 ? 7.442   -29.703 34.871  1.00 24.57 ? 137  ILE A O   1 
ATOM   963   C  CB  . ILE A  1 120 ? 9.643   -30.114 37.202  1.00 25.51 ? 137  ILE A CB  1 
ATOM   964   C  CG1 . ILE A  1 120 ? 8.819   -31.403 37.246  1.00 26.32 ? 137  ILE A CG1 1 
ATOM   965   C  CG2 . ILE A  1 120 ? 9.199   -29.141 38.298  1.00 25.98 ? 137  ILE A CG2 1 
ATOM   966   C  CD1 . ILE A  1 120 ? 9.401   -32.557 36.454  1.00 27.06 ? 137  ILE A CD1 1 
ATOM   967   N  N   . SER A  1 121 ? 8.009   -27.632 35.560  1.00 24.19 ? 138  SER A N   1 
ATOM   968   C  CA  . SER A  1 121 ? 6.749   -27.027 35.143  1.00 24.76 ? 138  SER A CA  1 
ATOM   969   C  C   . SER A  1 121 ? 6.634   -26.948 33.619  1.00 24.73 ? 138  SER A C   1 
ATOM   970   O  O   . SER A  1 121 ? 5.551   -26.664 33.103  1.00 23.84 ? 138  SER A O   1 
ATOM   971   C  CB  . SER A  1 121 ? 6.576   -25.666 35.764  1.00 25.53 ? 138  SER A CB  1 
ATOM   972   O  OG  . SER A  1 121 ? 6.515   -25.761 37.181  1.00 25.94 ? 138  SER A OG  1 
ATOM   973   N  N   . ASP A  1 122 ? 7.746   -27.191 32.906  1.00 22.58 ? 139  ASP A N   1 
ATOM   974   C  CA  . ASP A  1 122 ? 7.778   -27.112 31.453  1.00 22.89 ? 139  ASP A CA  1 
ATOM   975   C  C   . ASP A  1 122 ? 7.672   -28.497 30.810  1.00 23.04 ? 139  ASP A C   1 
ATOM   976   O  O   . ASP A  1 122 ? 7.837   -28.630 29.594  1.00 22.79 ? 139  ASP A O   1 
ATOM   977   C  CB  . ASP A  1 122 ? 9.038   -26.401 30.978  1.00 23.87 ? 139  ASP A CB  1 
ATOM   978   C  CG  . ASP A  1 122 ? 9.220   -24.976 31.482  1.00 24.67 ? 139  ASP A CG  1 
ATOM   979   O  OD1 . ASP A  1 122 ? 8.328   -24.144 31.221  1.00 25.10 ? 139  ASP A OD1 1 
ATOM   980   O  OD2 . ASP A  1 122 ? 10.262  -24.706 32.114  1.00 25.36 ? 139  ASP A OD2 1 
ATOM   981   N  N   . ARG A  1 123 ? 7.391   -29.532 31.611  1.00 24.34 ? 140  ARG A N   1 
ATOM   982   C  CA  . ARG A  1 123 ? 7.246   -30.885 31.091  1.00 25.83 ? 140  ARG A CA  1 
ATOM   983   C  C   . ARG A  1 123 ? 6.230   -30.899 29.947  1.00 26.10 ? 140  ARG A C   1 
ATOM   984   O  O   . ARG A  1 123 ? 5.183   -30.266 30.040  1.00 26.16 ? 140  ARG A O   1 
ATOM   985   C  CB  . ARG A  1 123 ? 6.846   -31.853 32.210  1.00 28.22 ? 140  ARG A CB  1 
ATOM   986   C  CG  . ARG A  1 123 ? 5.489   -31.627 32.862  1.00 31.25 ? 140  ARG A CG  1 
ATOM   987   C  CD  . ARG A  1 123 ? 5.347   -32.462 34.128  1.00 34.98 ? 140  ARG A CD  1 
ATOM   988   N  NE  . ARG A  1 123 ? 5.549   -33.896 33.887  1.00 37.70 ? 140  ARG A NE  1 
ATOM   989   C  CZ  . ARG A  1 123 ? 4.646   -34.755 33.414  1.00 41.87 ? 140  ARG A CZ  1 
ATOM   990   N  NH1 . ARG A  1 123 ? 3.404   -34.364 33.175  1.00 42.47 ? 140  ARG A NH1 1 
ATOM   991   N  NH2 . ARG A  1 123 ? 4.988   -36.018 33.207  1.00 42.55 ? 140  ARG A NH2 1 
ATOM   992   N  N   . GLY A  1 124 ? 6.569   -31.605 28.863  1.00 25.60 ? 141  GLY A N   1 
ATOM   993   C  CA  . GLY A  1 124 ? 5.746   -31.660 27.663  1.00 26.49 ? 141  GLY A CA  1 
ATOM   994   C  C   . GLY A  1 124 ? 6.042   -30.532 26.669  1.00 25.33 ? 141  GLY A C   1 
ATOM   995   O  O   . GLY A  1 124 ? 5.587   -30.585 25.528  1.00 26.19 ? 141  GLY A O   1 
ATOM   996   N  N   . HIS A  1 125 ? 6.818   -29.524 27.086  1.00 23.58 ? 142  HIS A N   1 
ATOM   997   C  CA  . HIS A  1 125 ? 7.085   -28.361 26.255  1.00 23.44 ? 142  HIS A CA  1 
ATOM   998   C  C   . HIS A  1 125 ? 8.583   -28.066 26.191  1.00 22.17 ? 142  HIS A C   1 
ATOM   999   O  O   . HIS A  1 125 ? 8.969   -26.928 25.968  1.00 22.88 ? 142  HIS A O   1 
ATOM   1000  C  CB  . HIS A  1 125 ? 6.316   -27.146 26.787  1.00 23.57 ? 142  HIS A CB  1 
ATOM   1001  C  CG  . HIS A  1 125 ? 4.838   -27.348 26.840  1.00 24.39 ? 142  HIS A CG  1 
ATOM   1002  N  ND1 . HIS A  1 125 ? 4.027   -27.168 25.740  1.00 25.49 ? 142  HIS A ND1 1 
ATOM   1003  C  CD2 . HIS A  1 125 ? 4.032   -27.743 27.839  1.00 24.55 ? 142  HIS A CD2 1 
ATOM   1004  C  CE1 . HIS A  1 125 ? 2.770   -27.435 26.080  1.00 25.36 ? 142  HIS A CE1 1 
ATOM   1005  N  NE2 . HIS A  1 125 ? 2.751   -27.783 27.351  1.00 24.78 ? 142  HIS A NE2 1 
ATOM   1006  N  N   . VAL A  1 126 ? 9.428   -29.088 26.363  1.00 22.34 ? 143  VAL A N   1 
ATOM   1007  C  CA  . VAL A  1 126 ? 10.868  -28.874 26.416  1.00 21.52 ? 143  VAL A CA  1 
ATOM   1008  C  C   . VAL A  1 126 ? 11.402  -28.479 25.039  1.00 21.77 ? 143  VAL A C   1 
ATOM   1009  O  O   . VAL A  1 126 ? 12.280  -27.623 24.947  1.00 22.84 ? 143  VAL A O   1 
ATOM   1010  C  CB  . VAL A  1 126 ? 11.601  -30.102 26.988  1.00 21.47 ? 143  VAL A CB  1 
ATOM   1011  C  CG1 . VAL A  1 126 ? 13.115  -30.002 26.821  1.00 21.45 ? 143  VAL A CG1 1 
ATOM   1012  C  CG2 . VAL A  1 126 ? 11.235  -30.326 28.451  1.00 21.22 ? 143  VAL A CG2 1 
ATOM   1013  N  N   . ARG A  1 127 ? 10.880  -29.086 23.969  1.00 22.46 ? 144  ARG A N   1 
ATOM   1014  C  CA  . ARG A  1 127 ? 11.364  -28.792 22.628  1.00 24.51 ? 144  ARG A CA  1 
ATOM   1015  C  C   . ARG A  1 127 ? 11.204  -27.304 22.301  1.00 23.75 ? 144  ARG A C   1 
ATOM   1016  O  O   . ARG A  1 127 ? 12.078  -26.726 21.662  1.00 22.05 ? 144  ARG A O   1 
ATOM   1017  C  CB  . ARG A  1 127 ? 10.684  -29.629 21.536  1.00 26.20 ? 144  ARG A CB  1 
ATOM   1018  C  CG  . ARG A  1 127 ? 11.165  -29.352 20.115  1.00 29.00 ? 144  ARG A CG  1 
ATOM   1019  C  CD  . ARG A  1 127 ? 12.670  -29.523 19.907  1.00 31.12 ? 144  ARG A CD  1 
ATOM   1020  N  NE  . ARG A  1 127 ? 13.114  -29.212 18.543  1.00 33.54 ? 144  ARG A NE  1 
ATOM   1021  C  CZ  . ARG A  1 127 ? 12.961  -29.980 17.461  1.00 36.21 ? 144  ARG A CZ  1 
ATOM   1022  N  NH1 . ARG A  1 127 ? 12.367  -31.161 17.539  1.00 37.58 ? 144  ARG A NH1 1 
ATOM   1023  N  NH2 . ARG A  1 127 ? 13.416  -29.562 16.294  1.00 36.77 ? 144  ARG A NH2 1 
ATOM   1024  N  N   . SER A  1 128 ? 10.089  -26.686 22.712  1.00 24.03 ? 145  SER A N   1 
ATOM   1025  C  CA  . SER A  1 128 ? 9.870   -25.279 22.403  1.00 25.94 ? 145  SER A CA  1 
ATOM   1026  C  C   . SER A  1 128 ? 10.894  -24.402 23.129  1.00 25.44 ? 145  SER A C   1 
ATOM   1027  O  O   . SER A  1 128 ? 11.283  -23.357 22.609  1.00 24.38 ? 145  SER A O   1 
ATOM   1028  C  CB  . SER A  1 128 ? 8.435   -24.847 22.682  1.00 28.12 ? 145  SER A CB  1 
ATOM   1029  O  OG  . SER A  1 128 ? 8.081   -25.030 24.043  1.00 30.69 ? 145  SER A OG  1 
ATOM   1030  N  N   . ILE A  1 129 ? 11.358  -24.839 24.313  1.00 24.45 ? 146  ILE A N   1 
ATOM   1031  C  CA  . ILE A  1 129 ? 12.423  -24.146 25.027  1.00 23.74 ? 146  ILE A CA  1 
ATOM   1032  C  C   . ILE A  1 129 ? 13.741  -24.302 24.267  1.00 22.90 ? 146  ILE A C   1 
ATOM   1033  O  O   . ILE A  1 129 ? 14.444  -23.319 24.047  1.00 23.06 ? 146  ILE A O   1 
ATOM   1034  C  CB  . ILE A  1 129 ? 12.528  -24.612 26.494  1.00 24.28 ? 146  ILE A CB  1 
ATOM   1035  C  CG1 . ILE A  1 129 ? 11.404  -24.023 27.335  1.00 24.97 ? 146  ILE A CG1 1 
ATOM   1036  C  CG2 . ILE A  1 129 ? 13.900  -24.285 27.081  1.00 25.17 ? 146  ILE A CG2 1 
ATOM   1037  C  CD1 . ILE A  1 129 ? 11.261  -24.625 28.722  1.00 25.42 ? 146  ILE A CD1 1 
ATOM   1038  N  N   . VAL A  1 130 ? 14.065  -25.529 23.843  1.00 22.81 ? 147  VAL A N   1 
ATOM   1039  C  CA  . VAL A  1 130 ? 15.288  -25.768 23.093  1.00 22.55 ? 147  VAL A CA  1 
ATOM   1040  C  C   . VAL A  1 130 ? 15.261  -24.947 21.803  1.00 22.53 ? 147  VAL A C   1 
ATOM   1041  O  O   . VAL A  1 130 ? 16.300  -24.462 21.361  1.00 21.75 ? 147  VAL A O   1 
ATOM   1042  C  CB  . VAL A  1 130 ? 15.487  -27.273 22.826  1.00 22.55 ? 147  VAL A CB  1 
ATOM   1043  C  CG1 . VAL A  1 130 ? 16.549  -27.549 21.770  1.00 23.16 ? 147  VAL A CG1 1 
ATOM   1044  C  CG2 . VAL A  1 130 ? 15.810  -28.028 24.111  1.00 22.61 ? 147  VAL A CG2 1 
ATOM   1045  N  N   . ASP A  1 131 ? 14.067  -24.757 21.223  1.00 23.16 ? 148  ASP A N   1 
ATOM   1046  C  CA  . ASP A  1 131 ? 13.937  -24.018 19.972  1.00 24.51 ? 148  ASP A CA  1 
ATOM   1047  C  C   . ASP A  1 131 ? 14.151  -22.517 20.179  1.00 23.72 ? 148  ASP A C   1 
ATOM   1048  O  O   . ASP A  1 131 ? 14.404  -21.803 19.211  1.00 24.21 ? 148  ASP A O   1 
ATOM   1049  C  CB  . ASP A  1 131 ? 12.627  -24.333 19.264  1.00 26.22 ? 148  ASP A CB  1 
ATOM   1050  C  CG  . ASP A  1 131 ? 12.572  -25.675 18.545  1.00 28.68 ? 148  ASP A CG  1 
ATOM   1051  O  OD1 . ASP A  1 131 ? 13.642  -26.290 18.342  1.00 29.06 ? 148  ASP A OD1 1 
ATOM   1052  O  OD2 . ASP A  1 131 ? 11.453  -26.108 18.208  1.00 30.68 ? 148  ASP A OD2 1 
ATOM   1053  N  N   . ASN A  1 132 ? 14.064  -22.037 21.425  1.00 22.90 ? 149  ASN A N   1 
ATOM   1054  C  CA  . ASN A  1 132 ? 14.281  -20.630 21.724  1.00 23.12 ? 149  ASN A CA  1 
ATOM   1055  C  C   . ASN A  1 132 ? 15.768  -20.298 21.851  1.00 22.87 ? 149  ASN A C   1 
ATOM   1056  O  O   . ASN A  1 132 ? 16.115  -19.123 21.910  1.00 23.50 ? 149  ASN A O   1 
ATOM   1057  C  CB  . ASN A  1 132 ? 13.555  -20.192 22.993  1.00 23.22 ? 149  ASN A CB  1 
ATOM   1058  C  CG  . ASN A  1 132 ? 12.068  -20.044 22.786  1.00 23.18 ? 149  ASN A CG  1 
ATOM   1059  O  OD1 . ASN A  1 132 ? 11.615  -19.875 21.651  1.00 22.85 ? 149  ASN A OD1 1 
ATOM   1060  N  ND2 . ASN A  1 132 ? 11.298  -20.083 23.863  1.00 23.87 ? 149  ASN A ND2 1 
ATOM   1061  N  N   . TRP A  1 133 ? 16.651  -21.297 21.940  1.00 22.38 ? 150  TRP A N   1 
ATOM   1062  C  CA  . TRP A  1 133 ? 18.075  -20.994 21.952  1.00 22.55 ? 150  TRP A CA  1 
ATOM   1063  C  C   . TRP A  1 133 ? 18.472  -20.427 20.593  1.00 23.03 ? 150  TRP A C   1 
ATOM   1064  O  O   . TRP A  1 133 ? 18.184  -21.044 19.576  1.00 22.74 ? 150  TRP A O   1 
ATOM   1065  C  CB  . TRP A  1 133 ? 18.929  -22.223 22.295  1.00 22.21 ? 150  TRP A CB  1 
ATOM   1066  C  CG  . TRP A  1 133 ? 20.374  -21.878 22.531  1.00 22.04 ? 150  TRP A CG  1 
ATOM   1067  C  CD1 . TRP A  1 133 ? 21.452  -22.233 21.775  1.00 22.77 ? 150  TRP A CD1 1 
ATOM   1068  C  CD2 . TRP A  1 133 ? 20.890  -21.061 23.605  1.00 22.50 ? 150  TRP A CD2 1 
ATOM   1069  N  NE1 . TRP A  1 133 ? 22.601  -21.715 22.310  1.00 22.79 ? 150  TRP A NE1 1 
ATOM   1070  C  CE2 . TRP A  1 133 ? 22.288  -20.985 23.428  1.00 23.07 ? 150  TRP A CE2 1 
ATOM   1071  C  CE3 . TRP A  1 133 ? 20.309  -20.385 24.682  1.00 22.70 ? 150  TRP A CE3 1 
ATOM   1072  C  CZ2 . TRP A  1 133 ? 23.108  -20.270 24.298  1.00 23.38 ? 150  TRP A CZ2 1 
ATOM   1073  C  CZ3 . TRP A  1 133 ? 21.122  -19.677 25.540  1.00 23.93 ? 150  TRP A CZ3 1 
ATOM   1074  C  CH2 . TRP A  1 133 ? 22.503  -19.626 25.353  1.00 24.16 ? 150  TRP A CH2 1 
ATOM   1075  N  N   . PRO A  1 134 ? 19.127  -19.244 20.522  1.00 25.10 ? 151  PRO A N   1 
ATOM   1076  C  CA  . PRO A  1 134 ? 19.382  -18.597 19.233  1.00 27.94 ? 151  PRO A CA  1 
ATOM   1077  C  C   . PRO A  1 134 ? 20.469  -19.183 18.327  1.00 29.96 ? 151  PRO A C   1 
ATOM   1078  O  O   . PRO A  1 134 ? 20.534  -18.815 17.161  1.00 32.99 ? 151  PRO A O   1 
ATOM   1079  C  CB  . PRO A  1 134 ? 19.690  -17.137 19.624  1.00 27.42 ? 151  PRO A CB  1 
ATOM   1080  C  CG  . PRO A  1 134 ? 20.150  -17.183 21.059  1.00 27.16 ? 151  PRO A CG  1 
ATOM   1081  C  CD  . PRO A  1 134 ? 19.595  -18.455 21.670  1.00 25.38 ? 151  PRO A CD  1 
ATOM   1082  N  N   . GLU A  1 135 ? 21.307  -20.092 18.843  1.00 29.96 ? 152  GLU A N   1 
ATOM   1083  C  CA  . GLU A  1 135 ? 22.382  -20.688 18.055  1.00 29.91 ? 152  GLU A CA  1 
ATOM   1084  C  C   . GLU A  1 135 ? 21.902  -22.002 17.437  1.00 29.25 ? 152  GLU A C   1 
ATOM   1085  O  O   . GLU A  1 135 ? 21.242  -22.795 18.109  1.00 26.62 ? 152  GLU A O   1 
ATOM   1086  C  CB  . GLU A  1 135 ? 23.616  -20.926 18.926  1.00 31.17 ? 152  GLU A CB  1 
ATOM   1087  C  CG  . GLU A  1 135 ? 24.078  -19.685 19.685  1.00 34.07 ? 152  GLU A CG  1 
ATOM   1088  C  CD  . GLU A  1 135 ? 24.560  -18.530 18.824  1.00 37.68 ? 152  GLU A CD  1 
ATOM   1089  O  OE1 . GLU A  1 135 ? 24.911  -18.738 17.642  1.00 38.31 ? 152  GLU A OE1 1 
ATOM   1090  O  OE2 . GLU A  1 135 ? 24.552  -17.398 19.351  1.00 43.89 ? 152  GLU A OE2 1 
ATOM   1091  N  N   . ASN A  1 136 ? 22.276  -22.245 16.168  1.00 28.47 ? 153  ASN A N   1 
ATOM   1092  C  CA  . ASN A  1 136 ? 21.720  -23.352 15.400  1.00 29.46 ? 153  ASN A CA  1 
ATOM   1093  C  C   . ASN A  1 136 ? 22.659  -24.554 15.290  1.00 27.47 ? 153  ASN A C   1 
ATOM   1094  O  O   . ASN A  1 136 ? 22.224  -25.596 14.793  1.00 26.50 ? 153  ASN A O   1 
ATOM   1095  C  CB  . ASN A  1 136 ? 21.366  -22.948 13.973  1.00 32.15 ? 153  ASN A CB  1 
ATOM   1096  C  CG  . ASN A  1 136 ? 20.391  -21.800 13.922  1.00 35.56 ? 153  ASN A CG  1 
ATOM   1097  O  OD1 . ASN A  1 136 ? 19.307  -21.887 14.506  1.00 40.22 ? 153  ASN A OD1 1 
ATOM   1098  N  ND2 . ASN A  1 136 ? 20.752  -20.728 13.234  1.00 40.22 ? 153  ASN A ND2 1 
ATOM   1099  N  N   . HIS A  1 137 ? 23.923  -24.428 15.724  1.00 26.46 ? 154  HIS A N   1 
ATOM   1100  C  CA  . HIS A  1 137 ? 24.915  -25.472 15.483  1.00 27.33 ? 154  HIS A CA  1 
ATOM   1101  C  C   . HIS A  1 137 ? 25.634  -25.902 16.760  1.00 25.54 ? 154  HIS A C   1 
ATOM   1102  O  O   . HIS A  1 137 ? 26.853  -26.071 16.757  1.00 26.17 ? 154  HIS A O   1 
ATOM   1103  C  CB  . HIS A  1 137 ? 25.981  -25.002 14.489  1.00 29.76 ? 154  HIS A CB  1 
ATOM   1104  C  CG  . HIS A  1 137 ? 25.410  -24.518 13.211  1.00 33.45 ? 154  HIS A CG  1 
ATOM   1105  N  ND1 . HIS A  1 137 ? 24.848  -25.371 12.286  1.00 34.88 ? 154  HIS A ND1 1 
ATOM   1106  C  CD2 . HIS A  1 137 ? 25.278  -23.282 12.718  1.00 34.59 ? 154  HIS A CD2 1 
ATOM   1107  C  CE1 . HIS A  1 137 ? 24.404  -24.663 11.261  1.00 34.50 ? 154  HIS A CE1 1 
ATOM   1108  N  NE2 . HIS A  1 137 ? 24.667  -23.397 11.502  1.00 36.22 ? 154  HIS A NE2 1 
ATOM   1109  N  N   . VAL A  1 138 ? 24.866  -26.152 17.820  1.00 23.39 ? 155  VAL A N   1 
ATOM   1110  C  CA  . VAL A  1 138 ? 25.410  -26.573 19.101  1.00 21.18 ? 155  VAL A CA  1 
ATOM   1111  C  C   . VAL A  1 138 ? 26.104  -27.926 18.956  1.00 20.88 ? 155  VAL A C   1 
ATOM   1112  O  O   . VAL A  1 138 ? 25.530  -28.860 18.395  1.00 20.87 ? 155  VAL A O   1 
ATOM   1113  C  CB  . VAL A  1 138 ? 24.280  -26.629 20.144  1.00 21.15 ? 155  VAL A CB  1 
ATOM   1114  C  CG1 . VAL A  1 138 ? 24.719  -27.308 21.437  1.00 20.62 ? 155  VAL A CG1 1 
ATOM   1115  C  CG2 . VAL A  1 138 ? 23.713  -25.246 20.425  1.00 21.41 ? 155  VAL A CG2 1 
ATOM   1116  N  N   . LYS A  1 139 ? 27.336  -28.013 19.486  1.00 20.66 ? 156  LYS A N   1 
ATOM   1117  C  CA  . LYS A  1 139 ? 28.123  -29.238 19.482  1.00 20.76 ? 156  LYS A CA  1 
ATOM   1118  C  C   . LYS A  1 139 ? 28.374  -29.767 20.896  1.00 20.78 ? 156  LYS A C   1 
ATOM   1119  O  O   . LYS A  1 139 ? 28.675  -30.951 21.043  1.00 21.19 ? 156  LYS A O   1 
ATOM   1120  C  CB  . LYS A  1 139 ? 29.480  -29.004 18.805  1.00 21.48 ? 156  LYS A CB  1 
ATOM   1121  C  CG  . LYS A  1 139 ? 29.417  -28.670 17.316  1.00 22.90 ? 156  LYS A CG  1 
ATOM   1122  C  CD  . LYS A  1 139 ? 28.653  -29.651 16.434  1.00 24.08 ? 156  LYS A CD  1 
ATOM   1123  C  CE  . LYS A  1 139 ? 29.182  -31.049 16.509  1.00 26.05 ? 156  LYS A CE  1 
ATOM   1124  N  NZ  . LYS A  1 139 ? 28.397  -31.979 15.694  1.00 26.91 ? 156  LYS A NZ  1 
ATOM   1125  N  N   . ALA A  1 140 ? 28.279  -28.898 21.920  1.00 20.55 ? 157  ALA A N   1 
ATOM   1126  C  CA  . ALA A  1 140 ? 28.652  -29.244 23.286  1.00 20.25 ? 157  ALA A CA  1 
ATOM   1127  C  C   . ALA A  1 140 ? 27.648  -28.669 24.283  1.00 19.78 ? 157  ALA A C   1 
ATOM   1128  O  O   . ALA A  1 140 ? 27.498  -27.453 24.399  1.00 19.54 ? 157  ALA A O   1 
ATOM   1129  C  CB  . ALA A  1 140 ? 30.047  -28.754 23.593  1.00 20.23 ? 157  ALA A CB  1 
ATOM   1130  N  N   . VAL A  1 141 ? 26.980  -29.573 25.006  1.00 19.10 ? 158  VAL A N   1 
ATOM   1131  C  CA  . VAL A  1 141 ? 26.029  -29.228 26.049  1.00 19.11 ? 158  VAL A CA  1 
ATOM   1132  C  C   . VAL A  1 141 ? 26.584  -29.694 27.390  1.00 18.79 ? 158  VAL A C   1 
ATOM   1133  O  O   . VAL A  1 141 ? 27.012  -30.842 27.507  1.00 18.98 ? 158  VAL A O   1 
ATOM   1134  C  CB  . VAL A  1 141 ? 24.683  -29.913 25.756  1.00 19.64 ? 158  VAL A CB  1 
ATOM   1135  C  CG1 . VAL A  1 141 ? 23.645  -29.625 26.836  1.00 20.05 ? 158  VAL A CG1 1 
ATOM   1136  C  CG2 . VAL A  1 141 ? 24.144  -29.550 24.379  1.00 20.14 ? 158  VAL A CG2 1 
ATOM   1137  N  N   . VAL A  1 142 ? 26.571  -28.807 28.391  1.00 18.48 ? 159  VAL A N   1 
ATOM   1138  C  CA  . VAL A  1 142 ? 26.817  -29.201 29.776  1.00 18.14 ? 159  VAL A CA  1 
ATOM   1139  C  C   . VAL A  1 142 ? 25.551  -28.907 30.579  1.00 18.25 ? 159  VAL A C   1 
ATOM   1140  O  O   . VAL A  1 142 ? 25.038  -27.788 30.528  1.00 18.06 ? 159  VAL A O   1 
ATOM   1141  C  CB  . VAL A  1 142 ? 28.052  -28.512 30.387  1.00 18.03 ? 159  VAL A CB  1 
ATOM   1142  C  CG1 . VAL A  1 142 ? 28.234  -28.843 31.867  1.00 18.18 ? 159  VAL A CG1 1 
ATOM   1143  C  CG2 . VAL A  1 142 ? 29.320  -28.850 29.613  1.00 18.01 ? 159  VAL A CG2 1 
ATOM   1144  N  N   . VAL A  1 143 ? 25.053  -29.924 31.301  1.00 17.57 ? 160  VAL A N   1 
ATOM   1145  C  CA  . VAL A  1 143 ? 23.785  -29.840 32.012  1.00 18.64 ? 160  VAL A CA  1 
ATOM   1146  C  C   . VAL A  1 143 ? 23.975  -30.222 33.481  1.00 19.77 ? 160  VAL A C   1 
ATOM   1147  O  O   . VAL A  1 143 ? 24.728  -31.146 33.795  1.00 20.13 ? 160  VAL A O   1 
ATOM   1148  C  CB  . VAL A  1 143 ? 22.714  -30.713 31.325  1.00 18.83 ? 160  VAL A CB  1 
ATOM   1149  C  CG1 . VAL A  1 143 ? 23.109  -32.182 31.258  1.00 18.91 ? 160  VAL A CG1 1 
ATOM   1150  C  CG2 . VAL A  1 143 ? 21.334  -30.569 31.966  1.00 19.78 ? 160  VAL A CG2 1 
ATOM   1151  N  N   . THR A  1 144 ? 23.278  -29.487 34.368  1.00 20.09 ? 161  THR A N   1 
ATOM   1152  C  CA  . THR A  1 144 ? 23.197  -29.796 35.789  1.00 20.95 ? 161  THR A CA  1 
ATOM   1153  C  C   . THR A  1 144 ? 21.747  -29.640 36.254  1.00 21.07 ? 161  THR A C   1 
ATOM   1154  O  O   . THR A  1 144 ? 20.956  -28.933 35.624  1.00 20.53 ? 161  THR A O   1 
ATOM   1155  C  CB  . THR A  1 144 ? 24.141  -28.886 36.580  1.00 21.09 ? 161  THR A CB  1 
ATOM   1156  O  OG1 . THR A  1 144 ? 24.201  -29.387 37.911  1.00 21.20 ? 161  THR A OG1 1 
ATOM   1157  C  CG2 . THR A  1 144 ? 23.690  -27.437 36.647  1.00 21.20 ? 161  THR A CG2 1 
ATOM   1158  N  N   . ASP A  1 145 ? 21.422  -30.287 37.379  1.00 20.86 ? 162  ASP A N   1 
ATOM   1159  C  CA  . ASP A  1 145 ? 20.186  -30.023 38.106  1.00 20.81 ? 162  ASP A CA  1 
ATOM   1160  C  C   . ASP A  1 145 ? 20.482  -29.325 39.435  1.00 20.67 ? 162  ASP A C   1 
ATOM   1161  O  O   . ASP A  1 145 ? 19.569  -29.072 40.215  1.00 20.87 ? 162  ASP A O   1 
ATOM   1162  C  CB  . ASP A  1 145 ? 19.372  -31.286 38.322  1.00 20.54 ? 162  ASP A CB  1 
ATOM   1163  C  CG  . ASP A  1 145 ? 19.990  -32.335 39.237  1.00 20.39 ? 162  ASP A CG  1 
ATOM   1164  O  OD1 . ASP A  1 145 ? 21.152  -32.149 39.648  1.00 19.96 ? 162  ASP A OD1 1 
ATOM   1165  O  OD2 . ASP A  1 145 ? 19.302  -33.339 39.520  1.00 21.22 ? 162  ASP A OD2 1 
ATOM   1166  N  N   . GLY A  1 146 ? 21.760  -29.036 39.702  1.00 20.90 ? 163  GLY A N   1 
ATOM   1167  C  CA  . GLY A  1 146 ? 22.151  -28.214 40.837  1.00 21.25 ? 163  GLY A CA  1 
ATOM   1168  C  C   . GLY A  1 146 ? 22.095  -28.953 42.176  1.00 22.12 ? 163  GLY A C   1 
ATOM   1169  O  O   . GLY A  1 146 ? 22.267  -28.327 43.219  1.00 21.32 ? 163  GLY A O   1 
ATOM   1170  N  N   . GLU A  1 147 ? 21.902  -30.281 42.157  1.00 22.70 ? 164  GLU A N   1 
ATOM   1171  C  CA  . GLU A  1 147 ? 21.673  -31.017 43.393  1.00 23.77 ? 164  GLU A CA  1 
ATOM   1172  C  C   . GLU A  1 147 ? 22.974  -31.215 44.175  1.00 23.20 ? 164  GLU A C   1 
ATOM   1173  O  O   . GLU A  1 147 ? 22.947  -31.233 45.402  1.00 22.20 ? 164  GLU A O   1 
ATOM   1174  C  CB  . GLU A  1 147 ? 20.978  -32.362 43.167  1.00 24.74 ? 164  GLU A CB  1 
ATOM   1175  C  CG  . GLU A  1 147 ? 20.694  -33.088 44.481  1.00 26.54 ? 164  GLU A CG  1 
ATOM   1176  C  CD  . GLU A  1 147 ? 19.648  -34.187 44.467  1.00 29.48 ? 164  GLU A CD  1 
ATOM   1177  O  OE1 . GLU A  1 147 ? 19.274  -34.679 43.383  1.00 30.21 ? 164  GLU A OE1 1 
ATOM   1178  O  OE2 . GLU A  1 147 ? 19.183  -34.531 45.576  1.00 31.66 ? 164  GLU A OE2 1 
ATOM   1179  N  N   . ARG A  1 148 ? 24.102  -31.393 43.481  1.00 23.47 ? 165  ARG A N   1 
ATOM   1180  C  CA  . ARG A  1 148 ? 25.357  -31.705 44.146  1.00 24.41 ? 165  ARG A CA  1 
ATOM   1181  C  C   . ARG A  1 148 ? 26.489  -30.880 43.538  1.00 24.48 ? 165  ARG A C   1 
ATOM   1182  O  O   . ARG A  1 148 ? 27.377  -31.409 42.872  1.00 22.33 ? 165  ARG A O   1 
ATOM   1183  C  CB  . ARG A  1 148 ? 25.648  -33.210 44.069  1.00 25.42 ? 165  ARG A CB  1 
ATOM   1184  C  CG  . ARG A  1 148 ? 26.732  -33.654 45.041  1.00 27.48 ? 165  ARG A CG  1 
ATOM   1185  C  CD  . ARG A  1 148 ? 27.709  -34.646 44.432  1.00 29.80 ? 165  ARG A CD  1 
ATOM   1186  N  NE  . ARG A  1 148 ? 28.490  -34.000 43.370  1.00 31.78 ? 165  ARG A NE  1 
ATOM   1187  C  CZ  . ARG A  1 148 ? 29.581  -34.487 42.787  1.00 33.87 ? 165  ARG A CZ  1 
ATOM   1188  N  NH1 . ARG A  1 148 ? 30.078  -35.656 43.158  1.00 34.77 ? 165  ARG A NH1 1 
ATOM   1189  N  NH2 . ARG A  1 148 ? 30.185  -33.783 41.844  1.00 33.77 ? 165  ARG A NH2 1 
ATOM   1190  N  N   . ILE A  1 149 ? 26.450  -29.568 43.790  1.00 26.32 ? 166  ILE A N   1 
ATOM   1191  C  CA  . ILE A  1 149 ? 27.516  -28.677 43.367  1.00 27.15 ? 166  ILE A CA  1 
ATOM   1192  C  C   . ILE A  1 149 ? 28.762  -29.033 44.172  1.00 29.25 ? 166  ILE A C   1 
ATOM   1193  O  O   . ILE A  1 149 ? 28.737  -29.012 45.401  1.00 28.56 ? 166  ILE A O   1 
ATOM   1194  C  CB  . ILE A  1 149 ? 27.113  -27.199 43.536  1.00 27.34 ? 166  ILE A CB  1 
ATOM   1195  C  CG1 . ILE A  1 149 ? 25.849  -26.847 42.735  1.00 26.63 ? 166  ILE A CG1 1 
ATOM   1196  C  CG2 . ILE A  1 149 ? 28.281  -26.270 43.199  1.00 27.44 ? 166  ILE A CG2 1 
ATOM   1197  C  CD1 . ILE A  1 149 ? 25.927  -27.166 41.255  1.00 27.23 ? 166  ILE A CD1 1 
ATOM   1198  N  N   . LEU A  1 150 ? 29.849  -29.363 43.466  1.00 30.58 ? 167  LEU A N   1 
ATOM   1199  C  CA  . LEU A  1 150 ? 31.030  -29.895 44.120  1.00 33.88 ? 167  LEU A CA  1 
ATOM   1200  C  C   . LEU A  1 150 ? 31.416  -28.949 45.256  1.00 34.61 ? 167  LEU A C   1 
ATOM   1201  O  O   . LEU A  1 150 ? 31.674  -27.770 45.027  1.00 33.94 ? 167  LEU A O   1 
ATOM   1202  C  CB  . LEU A  1 150 ? 32.171  -30.097 43.120  1.00 36.22 ? 167  LEU A CB  1 
ATOM   1203  C  CG  . LEU A  1 150 ? 33.407  -30.841 43.647  1.00 37.75 ? 167  LEU A CG  1 
ATOM   1204  C  CD1 . LEU A  1 150 ? 33.083  -32.272 44.037  1.00 38.25 ? 167  LEU A CD1 1 
ATOM   1205  C  CD2 . LEU A  1 150 ? 34.534  -30.824 42.629  1.00 39.70 ? 167  LEU A CD2 1 
ATOM   1206  N  N   . GLY A  1 151 ? 31.358  -29.467 46.489  1.00 35.85 ? 168  GLY A N   1 
ATOM   1207  C  CA  . GLY A  1 151 ? 31.843  -28.758 47.660  1.00 35.70 ? 168  GLY A CA  1 
ATOM   1208  C  C   . GLY A  1 151 ? 30.781  -27.885 48.327  1.00 35.13 ? 168  GLY A C   1 
ATOM   1209  O  O   . GLY A  1 151 ? 31.054  -27.304 49.375  1.00 35.85 ? 168  GLY A O   1 
ATOM   1210  N  N   . LEU A  1 152 ? 29.577  -27.786 47.743  1.00 34.07 ? 169  LEU A N   1 
ATOM   1211  C  CA  . LEU A  1 152 ? 28.591  -26.828 48.227  1.00 34.16 ? 169  LEU A CA  1 
ATOM   1212  C  C   . LEU A  1 152 ? 27.217  -27.459 48.470  1.00 33.31 ? 169  LEU A C   1 
ATOM   1213  O  O   . LEU A  1 152 ? 26.435  -26.914 49.243  1.00 34.89 ? 169  LEU A O   1 
ATOM   1214  C  CB  . LEU A  1 152 ? 28.506  -25.652 47.252  1.00 36.14 ? 169  LEU A CB  1 
ATOM   1215  C  CG  . LEU A  1 152 ? 29.675  -24.661 47.287  1.00 37.83 ? 169  LEU A CG  1 
ATOM   1216  C  CD1 . LEU A  1 152 ? 29.626  -23.711 46.102  1.00 38.68 ? 169  LEU A CD1 1 
ATOM   1217  C  CD2 . LEU A  1 152 ? 29.704  -23.867 48.586  1.00 37.26 ? 169  LEU A CD2 1 
ATOM   1218  N  N   . GLY A  1 153 ? 26.895  -28.573 47.801  1.00 31.78 ? 170  GLY A N   1 
ATOM   1219  C  CA  . GLY A  1 153 ? 25.612  -29.233 48.000  1.00 30.19 ? 170  GLY A CA  1 
ATOM   1220  C  C   . GLY A  1 153 ? 24.534  -28.693 47.059  1.00 28.33 ? 170  GLY A C   1 
ATOM   1221  O  O   . GLY A  1 153 ? 24.825  -28.278 45.940  1.00 26.87 ? 170  GLY A O   1 
ATOM   1222  N  N   . ASP A  1 154 ? 23.282  -28.708 47.533  1.00 27.50 ? 171  ASP A N   1 
ATOM   1223  C  CA  . ASP A  1 154 ? 22.117  -28.429 46.706  1.00 26.91 ? 171  ASP A CA  1 
ATOM   1224  C  C   . ASP A  1 154 ? 21.897  -26.920 46.641  1.00 27.10 ? 171  ASP A C   1 
ATOM   1225  O  O   . ASP A  1 154 ? 21.502  -26.316 47.634  1.00 28.08 ? 171  ASP A O   1 
ATOM   1226  C  CB  . ASP A  1 154 ? 20.909  -29.183 47.249  1.00 27.02 ? 171  ASP A CB  1 
ATOM   1227  C  CG  . ASP A  1 154 ? 19.596  -29.048 46.492  1.00 27.18 ? 171  ASP A CG  1 
ATOM   1228  O  OD1 . ASP A  1 154 ? 19.506  -28.176 45.598  1.00 27.56 ? 171  ASP A OD1 1 
ATOM   1229  O  OD2 . ASP A  1 154 ? 18.669  -29.836 46.792  1.00 26.47 ? 171  ASP A OD2 1 
ATOM   1230  N  N   . LEU A  1 155 ? 22.150  -26.324 45.468  1.00 26.03 ? 172  LEU A N   1 
ATOM   1231  C  CA  . LEU A  1 155 ? 21.998  -24.888 45.282  1.00 26.02 ? 172  LEU A CA  1 
ATOM   1232  C  C   . LEU A  1 155 ? 20.850  -24.579 44.324  1.00 25.80 ? 172  LEU A C   1 
ATOM   1233  O  O   . LEU A  1 155 ? 20.643  -23.419 43.988  1.00 26.63 ? 172  LEU A O   1 
ATOM   1234  C  CB  . LEU A  1 155 ? 23.297  -24.277 44.761  1.00 26.89 ? 172  LEU A CB  1 
ATOM   1235  C  CG  . LEU A  1 155 ? 24.520  -24.362 45.680  1.00 28.20 ? 172  LEU A CG  1 
ATOM   1236  C  CD1 . LEU A  1 155 ? 25.648  -23.584 45.028  1.00 29.68 ? 172  LEU A CD1 1 
ATOM   1237  C  CD2 . LEU A  1 155 ? 24.263  -23.848 47.085  1.00 28.92 ? 172  LEU A CD2 1 
ATOM   1238  N  N   . GLY A  1 156 ? 20.124  -25.604 43.869  1.00 25.63 ? 173  GLY A N   1 
ATOM   1239  C  CA  . GLY A  1 156 ? 19.025  -25.402 42.939  1.00 26.01 ? 173  GLY A CA  1 
ATOM   1240  C  C   . GLY A  1 156 ? 19.487  -24.657 41.686  1.00 25.07 ? 173  GLY A C   1 
ATOM   1241  O  O   . GLY A  1 156 ? 20.531  -24.973 41.122  1.00 22.57 ? 173  GLY A O   1 
ATOM   1242  N  N   . VAL A  1 157 ? 18.719  -23.638 41.284  1.00 25.43 ? 174  VAL A N   1 
ATOM   1243  C  CA  . VAL A  1 157 ? 19.016  -22.883 40.074  1.00 27.38 ? 174  VAL A CA  1 
ATOM   1244  C  C   . VAL A  1 157 ? 20.213  -21.962 40.303  1.00 27.53 ? 174  VAL A C   1 
ATOM   1245  O  O   . VAL A  1 157 ? 20.783  -21.462 39.341  1.00 28.66 ? 174  VAL A O   1 
ATOM   1246  C  CB  . VAL A  1 157 ? 17.822  -22.066 39.545  1.00 29.35 ? 174  VAL A CB  1 
ATOM   1247  C  CG1 . VAL A  1 157 ? 16.620  -22.953 39.254  1.00 30.58 ? 174  VAL A CG1 1 
ATOM   1248  C  CG2 . VAL A  1 157 ? 17.449  -20.926 40.479  1.00 31.41 ? 174  VAL A CG2 1 
ATOM   1249  N  N   . TYR A  1 158 ? 20.640  -21.782 41.559  1.00 29.69 ? 175  TYR A N   1 
ATOM   1250  C  CA  . TYR A  1 158 ? 21.860  -21.040 41.845  1.00 31.95 ? 175  TYR A CA  1 
ATOM   1251  C  C   . TYR A  1 158 ? 23.128  -21.790 41.406  1.00 33.29 ? 175  TYR A C   1 
ATOM   1252  O  O   . TYR A  1 158 ? 24.230  -21.313 41.684  1.00 36.52 ? 175  TYR A O   1 
ATOM   1253  C  CB  . TYR A  1 158 ? 21.992  -20.678 43.331  1.00 33.16 ? 175  TYR A CB  1 
ATOM   1254  C  CG  . TYR A  1 158 ? 21.117  -19.574 43.920  1.00 33.31 ? 175  TYR A CG  1 
ATOM   1255  C  CD1 . TYR A  1 158 ? 20.443  -18.639 43.135  1.00 35.51 ? 175  TYR A CD1 1 
ATOM   1256  C  CD2 . TYR A  1 158 ? 21.032  -19.424 45.298  1.00 34.70 ? 175  TYR A CD2 1 
ATOM   1257  C  CE1 . TYR A  1 158 ? 19.676  -17.631 43.707  1.00 34.01 ? 175  TYR A CE1 1 
ATOM   1258  C  CE2 . TYR A  1 158 ? 20.278  -18.419 45.880  1.00 35.65 ? 175  TYR A CE2 1 
ATOM   1259  C  CZ  . TYR A  1 158 ? 19.594  -17.518 45.083  1.00 36.34 ? 175  TYR A CZ  1 
ATOM   1260  O  OH  . TYR A  1 158 ? 18.855  -16.531 45.686  1.00 38.66 ? 175  TYR A OH  1 
ATOM   1261  N  N   A GLY A  1 159 ? 22.961  -22.954 40.757  0.25 32.77 ? 176  GLY A N   1 
ATOM   1262  N  N   B GLY A  1 159 ? 22.962  -22.942 40.739  0.11 33.07 ? 176  GLY A N   1 
ATOM   1263  N  N   C GLY A  1 159 ? 22.959  -22.952 40.757  0.23 32.39 ? 176  GLY A N   1 
ATOM   1264  N  N   D GLY A  1 159 ? 22.965  -22.928 40.713  0.41 31.96 ? 176  GLY A N   1 
ATOM   1265  C  CA  A GLY A  1 159 ? 24.063  -23.686 40.153  0.25 32.50 ? 176  GLY A CA  1 
ATOM   1266  C  CA  B GLY A  1 159 ? 24.072  -23.691 40.172  0.11 32.86 ? 176  GLY A CA  1 
ATOM   1267  C  CA  C GLY A  1 159 ? 24.056  -23.669 40.127  0.23 31.84 ? 176  GLY A CA  1 
ATOM   1268  C  CA  D GLY A  1 159 ? 24.085  -23.709 40.213  0.41 31.27 ? 176  GLY A CA  1 
ATOM   1269  C  C   A GLY A  1 159 ? 24.125  -23.464 38.643  0.25 31.98 ? 176  GLY A C   1 
ATOM   1270  C  C   B GLY A  1 159 ? 24.096  -23.604 38.647  0.11 32.52 ? 176  GLY A C   1 
ATOM   1271  C  C   C GLY A  1 159 ? 24.077  -23.448 38.616  0.23 31.05 ? 176  GLY A C   1 
ATOM   1272  C  C   D GLY A  1 159 ? 24.246  -23.598 38.697  0.41 30.04 ? 176  GLY A C   1 
ATOM   1273  O  O   A GLY A  1 159 ? 24.914  -24.104 37.951  0.25 30.92 ? 176  GLY A O   1 
ATOM   1274  O  O   B GLY A  1 159 ? 24.777  -24.391 37.994  0.11 32.03 ? 176  GLY A O   1 
ATOM   1275  O  O   C GLY A  1 159 ? 24.795  -24.141 37.899  0.23 30.16 ? 176  GLY A O   1 
ATOM   1276  O  O   D GLY A  1 159 ? 25.122  -24.241 38.124  0.41 28.66 ? 176  GLY A O   1 
ATOM   1277  N  N   A MET A  1 160 ? 23.287  -22.544 38.145  0.25 31.44 ? 177  MET A N   1 
ATOM   1278  N  N   B MET A  1 160 ? 23.353  -22.641 38.085  0.25 32.40 ? 177  MET A N   1 
ATOM   1279  N  N   C MET A  1 160 ? 23.289  -22.471 38.145  0.25 30.04 ? 177  MET A N   1 
ATOM   1280  N  N   D MET A  1 160 ? 23.416  -22.773 38.045  0.25 29.13 ? 177  MET A N   1 
ATOM   1281  C  CA  A MET A  1 160 ? 23.294  -22.149 36.744  0.25 30.49 ? 177  MET A CA  1 
ATOM   1282  C  CA  B MET A  1 160 ? 23.397  -22.385 36.653  0.25 31.42 ? 177  MET A CA  1 
ATOM   1283  C  CA  C MET A  1 160 ? 23.275  -22.096 36.738  0.25 28.81 ? 177  MET A CA  1 
ATOM   1284  C  CA  D MET A  1 160 ? 23.517  -22.604 36.602  0.25 27.48 ? 177  MET A CA  1 
ATOM   1285  C  C   A MET A  1 160 ? 24.723  -21.866 36.280  0.25 29.11 ? 177  MET A C   1 
ATOM   1286  C  C   B MET A  1 160 ? 24.794  -21.917 36.250  0.25 29.60 ? 177  MET A C   1 
ATOM   1287  C  C   C MET A  1 160 ? 24.703  -21.818 36.267  0.25 28.26 ? 177  MET A C   1 
ATOM   1288  C  C   D MET A  1 160 ? 24.841  -21.941 36.229  0.25 27.55 ? 177  MET A C   1 
ATOM   1289  O  O   A MET A  1 160 ? 25.086  -22.172 35.146  0.25 29.23 ? 177  MET A O   1 
ATOM   1290  O  O   B MET A  1 160 ? 25.205  -22.133 35.112  0.25 29.59 ? 177  MET A O   1 
ATOM   1291  O  O   C MET A  1 160 ? 25.049  -22.089 35.119  0.25 28.58 ? 177  MET A O   1 
ATOM   1292  O  O   D MET A  1 160 ? 25.252  -22.041 35.075  0.25 27.73 ? 177  MET A O   1 
ATOM   1293  C  CB  A MET A  1 160 ? 22.418  -20.906 36.528  0.25 30.76 ? 177  MET A CB  1 
ATOM   1294  C  CB  B MET A  1 160 ? 22.381  -21.319 36.225  0.25 32.38 ? 177  MET A CB  1 
ATOM   1295  C  CB  C MET A  1 160 ? 22.377  -20.870 36.499  0.25 28.02 ? 177  MET A CB  1 
ATOM   1296  C  CB  D MET A  1 160 ? 22.372  -21.772 36.015  0.25 26.33 ? 177  MET A CB  1 
ATOM   1297  C  CG  A MET A  1 160 ? 22.659  -19.778 37.524  0.25 30.69 ? 177  MET A CG  1 
ATOM   1298  C  CG  B MET A  1 160 ? 22.655  -20.708 34.852  0.25 32.75 ? 177  MET A CG  1 
ATOM   1299  C  CG  C MET A  1 160 ? 22.859  -19.572 37.141  0.25 27.16 ? 177  MET A CG  1 
ATOM   1300  C  CG  D MET A  1 160 ? 22.607  -21.294 34.581  0.25 25.05 ? 177  MET A CG  1 
ATOM   1301  S  SD  A MET A  1 160 ? 21.517  -18.389 37.357  0.25 31.58 ? 177  MET A SD  1 
ATOM   1302  S  SD  B MET A  1 160 ? 22.160  -21.700 33.425  0.25 33.74 ? 177  MET A SD  1 
ATOM   1303  S  SD  C MET A  1 160 ? 21.819  -18.137 36.784  0.25 25.93 ? 177  MET A SD  1 
ATOM   1304  S  SD  D MET A  1 160 ? 22.927  -22.574 33.346  0.25 22.70 ? 177  MET A SD  1 
ATOM   1305  C  CE  A MET A  1 160 ? 22.395  -17.376 36.160  0.25 31.15 ? 177  MET A CE  1 
ATOM   1306  C  CE  B MET A  1 160 ? 23.383  -23.016 33.420  0.25 32.71 ? 177  MET A CE  1 
ATOM   1307  C  CE  C MET A  1 160 ? 20.409  -18.446 37.858  0.25 25.40 ? 177  MET A CE  1 
ATOM   1308  C  CE  D MET A  1 160 ? 21.873  -21.965 32.024  0.25 22.82 ? 177  MET A CE  1 
ATOM   1309  N  N   . GLY A  1 161 ? 25.519  -21.276 37.178  1.00 27.59 ? 178  GLY A N   1 
ATOM   1310  C  CA  . GLY A  1 161 ? 26.879  -20.833 36.902  1.00 26.61 ? 178  GLY A CA  1 
ATOM   1311  C  C   . GLY A  1 161 ? 27.850  -21.968 36.566  1.00 24.55 ? 178  GLY A C   1 
ATOM   1312  O  O   . GLY A  1 161 ? 28.836  -21.729 35.872  1.00 24.19 ? 178  GLY A O   1 
ATOM   1313  N  N   . ILE A  1 162 ? 27.577  -23.194 37.042  1.00 23.50 ? 179  ILE A N   1 
ATOM   1314  C  CA  . ILE A  1 162 ? 28.514  -24.299 36.883  1.00 23.64 ? 179  ILE A CA  1 
ATOM   1315  C  C   . ILE A  1 162 ? 28.639  -24.703 35.408  1.00 23.04 ? 179  ILE A C   1 
ATOM   1316  O  O   . ILE A  1 162 ? 29.758  -24.794 34.909  1.00 21.67 ? 179  ILE A O   1 
ATOM   1317  C  CB  . ILE A  1 162 ? 28.166  -25.482 37.814  1.00 23.93 ? 179  ILE A CB  1 
ATOM   1318  C  CG1 . ILE A  1 162 ? 28.749  -25.288 39.216  1.00 24.10 ? 179  ILE A CG1 1 
ATOM   1319  C  CG2 . ILE A  1 162 ? 28.632  -26.814 37.224  1.00 24.67 ? 179  ILE A CG2 1 
ATOM   1320  C  CD1 . ILE A  1 162 ? 28.185  -24.113 39.993  1.00 24.22 ? 179  ILE A CD1 1 
ATOM   1321  N  N   . PRO A  1 163 ? 27.549  -25.024 34.669  1.00 23.88 ? 180  PRO A N   1 
ATOM   1322  C  CA  . PRO A  1 163 ? 27.663  -25.295 33.229  1.00 23.86 ? 180  PRO A CA  1 
ATOM   1323  C  C   . PRO A  1 163 ? 28.304  -24.173 32.407  1.00 22.37 ? 180  PRO A C   1 
ATOM   1324  O  O   . PRO A  1 163 ? 29.051  -24.449 31.473  1.00 21.11 ? 180  PRO A O   1 
ATOM   1325  C  CB  . PRO A  1 163 ? 26.214  -25.564 32.788  1.00 24.19 ? 180  PRO A CB  1 
ATOM   1326  C  CG  . PRO A  1 163 ? 25.523  -26.049 34.043  1.00 25.12 ? 180  PRO A CG  1 
ATOM   1327  C  CD  . PRO A  1 163 ? 26.197  -25.298 35.185  1.00 24.88 ? 180  PRO A CD  1 
ATOM   1328  N  N   . VAL A  1 164 ? 27.990  -22.919 32.757  1.00 22.27 ? 181  VAL A N   1 
ATOM   1329  C  CA  . VAL A  1 164 ? 28.575  -21.747 32.122  1.00 21.74 ? 181  VAL A CA  1 
ATOM   1330  C  C   . VAL A  1 164 ? 30.095  -21.796 32.278  1.00 20.60 ? 181  VAL A C   1 
ATOM   1331  O  O   . VAL A  1 164 ? 30.822  -21.688 31.295  1.00 20.60 ? 181  VAL A O   1 
ATOM   1332  C  CB  . VAL A  1 164 ? 27.975  -20.449 32.702  1.00 22.92 ? 181  VAL A CB  1 
ATOM   1333  C  CG1 . VAL A  1 164 ? 28.708  -19.202 32.218  1.00 23.68 ? 181  VAL A CG1 1 
ATOM   1334  C  CG2 . VAL A  1 164 ? 26.484  -20.324 32.393  1.00 23.35 ? 181  VAL A CG2 1 
ATOM   1335  N  N   . GLY A  1 165 ? 30.565  -21.961 33.520  1.00 20.42 ? 182  GLY A N   1 
ATOM   1336  C  CA  . GLY A  1 165 ? 31.987  -21.980 33.826  1.00 20.33 ? 182  GLY A CA  1 
ATOM   1337  C  C   . GLY A  1 165 ? 32.712  -23.156 33.172  1.00 20.82 ? 182  GLY A C   1 
ATOM   1338  O  O   . GLY A  1 165 ? 33.828  -22.997 32.681  1.00 22.08 ? 182  GLY A O   1 
ATOM   1339  N  N   . LYS A  1 166 ? 32.078  -24.333 33.168  1.00 20.32 ? 183  LYS A N   1 
ATOM   1340  C  CA  . LYS A  1 166 ? 32.670  -25.514 32.561  1.00 21.12 ? 183  LYS A CA  1 
ATOM   1341  C  C   . LYS A  1 166 ? 32.900  -25.275 31.067  1.00 20.44 ? 183  LYS A C   1 
ATOM   1342  O  O   . LYS A  1 166 ? 33.970  -25.569 30.534  1.00 19.31 ? 183  LYS A O   1 
ATOM   1343  C  CB  . LYS A  1 166 ? 31.748  -26.712 32.802  1.00 22.71 ? 183  LYS A CB  1 
ATOM   1344  C  CG  . LYS A  1 166 ? 32.339  -28.085 32.518  1.00 25.11 ? 183  LYS A CG  1 
ATOM   1345  C  CD  . LYS A  1 166 ? 33.114  -28.658 33.695  1.00 26.90 ? 183  LYS A CD  1 
ATOM   1346  C  CE  . LYS A  1 166 ? 33.478  -30.092 33.503  1.00 26.79 ? 183  LYS A CE  1 
ATOM   1347  N  NZ  . LYS A  1 166 ? 34.056  -30.595 34.747  1.00 28.13 ? 183  LYS A NZ  1 
ATOM   1348  N  N   . LEU A  1 167 ? 31.895  -24.719 30.386  1.00 20.07 ? 184  LEU A N   1 
ATOM   1349  C  CA  . LEU A  1 167 ? 31.996  -24.516 28.950  1.00 20.44 ? 184  LEU A CA  1 
ATOM   1350  C  C   . LEU A  1 167 ? 33.024  -23.430 28.628  1.00 20.60 ? 184  LEU A C   1 
ATOM   1351  O  O   . LEU A  1 167 ? 33.678  -23.516 27.591  1.00 21.45 ? 184  LEU A O   1 
ATOM   1352  C  CB  . LEU A  1 167 ? 30.619  -24.252 28.344  1.00 20.26 ? 184  LEU A CB  1 
ATOM   1353  C  CG  . LEU A  1 167 ? 29.738  -25.502 28.222  1.00 20.47 ? 184  LEU A CG  1 
ATOM   1354  C  CD1 . LEU A  1 167 ? 28.273  -25.148 28.037  1.00 20.11 ? 184  LEU A CD1 1 
ATOM   1355  C  CD2 . LEU A  1 167 ? 30.228  -26.399 27.098  1.00 20.46 ? 184  LEU A CD2 1 
ATOM   1356  N  N   . CYS A  1 168 ? 33.207  -22.447 29.522  1.00 21.04 ? 185  CYS A N   1 
ATOM   1357  C  CA  . CYS A  1 168 ? 34.291  -21.482 29.380  1.00 21.93 ? 185  CYS A CA  1 
ATOM   1358  C  C   . CYS A  1 168 ? 35.634  -22.207 29.267  1.00 21.77 ? 185  CYS A C   1 
ATOM   1359  O  O   . CYS A  1 168 ? 36.506  -21.790 28.513  1.00 21.27 ? 185  CYS A O   1 
ATOM   1360  C  CB  . CYS A  1 168 ? 34.314  -20.479 30.532  1.00 23.47 ? 185  CYS A CB  1 
ATOM   1361  S  SG  . CYS A  1 168 ? 32.952  -19.284 30.477  1.00 27.46 ? 185  CYS A SG  1 
ATOM   1362  N  N   . LEU A  1 169 ? 35.795  -23.308 30.008  1.00 22.35 ? 186  LEU A N   1 
ATOM   1363  C  CA  . LEU A  1 169 ? 37.033  -24.073 29.993  1.00 22.54 ? 186  LEU A CA  1 
ATOM   1364  C  C   . LEU A  1 169 ? 37.124  -24.970 28.758  1.00 21.86 ? 186  LEU A C   1 
ATOM   1365  O  O   . LEU A  1 169 ? 38.226  -25.235 28.283  1.00 21.40 ? 186  LEU A O   1 
ATOM   1366  C  CB  . LEU A  1 169 ? 37.144  -24.873 31.292  1.00 24.30 ? 186  LEU A CB  1 
ATOM   1367  C  CG  . LEU A  1 169 ? 37.209  -24.042 32.578  1.00 26.21 ? 186  LEU A CG  1 
ATOM   1368  C  CD1 . LEU A  1 169 ? 37.404  -24.932 33.796  1.00 27.36 ? 186  LEU A CD1 1 
ATOM   1369  C  CD2 . LEU A  1 169 ? 38.301  -22.988 32.508  1.00 27.24 ? 186  LEU A CD2 1 
ATOM   1370  N  N   . TYR A  1 170 ? 35.983  -25.452 28.246  1.00 20.85 ? 187  TYR A N   1 
ATOM   1371  C  CA  . TYR A  1 170 ? 35.962  -26.131 26.955  1.00 20.75 ? 187  TYR A CA  1 
ATOM   1372  C  C   . TYR A  1 170 ? 36.610  -25.231 25.899  1.00 20.29 ? 187  TYR A C   1 
ATOM   1373  O  O   . TYR A  1 170 ? 37.467  -25.679 25.135  1.00 20.20 ? 187  TYR A O   1 
ATOM   1374  C  CB  . TYR A  1 170 ? 34.564  -26.498 26.441  1.00 20.66 ? 187  TYR A CB  1 
ATOM   1375  C  CG  . TYR A  1 170 ? 33.905  -27.778 26.948  1.00 20.45 ? 187  TYR A CG  1 
ATOM   1376  C  CD1 . TYR A  1 170 ? 33.889  -28.125 28.294  1.00 20.39 ? 187  TYR A CD1 1 
ATOM   1377  C  CD2 . TYR A  1 170 ? 33.249  -28.623 26.058  1.00 20.52 ? 187  TYR A CD2 1 
ATOM   1378  C  CE1 . TYR A  1 170 ? 33.260  -29.282 28.734  1.00 20.78 ? 187  TYR A CE1 1 
ATOM   1379  C  CE2 . TYR A  1 170 ? 32.617  -29.777 26.485  1.00 20.70 ? 187  TYR A CE2 1 
ATOM   1380  C  CZ  . TYR A  1 170 ? 32.638  -30.120 27.824  1.00 21.26 ? 187  TYR A CZ  1 
ATOM   1381  O  OH  . TYR A  1 170 ? 32.004  -31.266 28.216  1.00 23.21 ? 187  TYR A OH  1 
ATOM   1382  N  N   . THR A  1 171 ? 36.195  -23.958 25.861  1.00 19.84 ? 188  THR A N   1 
ATOM   1383  C  CA  . THR A  1 171 ? 36.679  -23.027 24.853  1.00 20.84 ? 188  THR A CA  1 
ATOM   1384  C  C   . THR A  1 171 ? 38.132  -22.647 25.128  1.00 20.72 ? 188  THR A C   1 
ATOM   1385  O  O   . THR A  1 171 ? 38.969  -22.732 24.235  1.00 20.65 ? 188  THR A O   1 
ATOM   1386  C  CB  . THR A  1 171 ? 35.801  -21.778 24.794  1.00 21.36 ? 188  THR A CB  1 
ATOM   1387  O  OG1 . THR A  1 171 ? 34.490  -22.210 24.448  1.00 22.69 ? 188  THR A OG1 1 
ATOM   1388  C  CG2 . THR A  1 171 ? 36.278  -20.796 23.741  1.00 21.11 ? 188  THR A CG2 1 
ATOM   1389  N  N   . ALA A  1 172 ? 38.420  -22.193 26.353  1.00 21.00 ? 189  ALA A N   1 
ATOM   1390  C  CA  . ALA A  1 172 ? 39.721  -21.615 26.660  1.00 21.65 ? 189  ALA A CA  1 
ATOM   1391  C  C   . ALA A  1 172 ? 40.828  -22.659 26.525  1.00 22.17 ? 189  ALA A C   1 
ATOM   1392  O  O   . ALA A  1 172 ? 41.912  -22.336 26.042  1.00 22.87 ? 189  ALA A O   1 
ATOM   1393  C  CB  . ALA A  1 172 ? 39.704  -20.994 28.035  1.00 21.48 ? 189  ALA A CB  1 
ATOM   1394  N  N   . CYS A  1 173 ? 40.547  -23.908 26.923  1.00 21.58 ? 190  CYS A N   1 
ATOM   1395  C  CA  . CYS A  1 173 ? 41.569  -24.944 26.998  1.00 22.48 ? 190  CYS A CA  1 
ATOM   1396  C  C   . CYS A  1 173 ? 41.702  -25.722 25.687  1.00 22.81 ? 190  CYS A C   1 
ATOM   1397  O  O   . CYS A  1 173 ? 42.809  -26.118 25.340  1.00 23.52 ? 190  CYS A O   1 
ATOM   1398  C  CB  . CYS A  1 173 ? 41.321  -25.911 28.154  1.00 23.82 ? 190  CYS A CB  1 
ATOM   1399  S  SG  . CYS A  1 173 ? 41.254  -25.111 29.783  1.00 26.83 ? 190  CYS A SG  1 
ATOM   1400  N  N   . ALA A  1 174 ? 40.594  -25.981 24.973  1.00 22.24 ? 191  ALA A N   1 
ATOM   1401  C  CA  . ALA A  1 174 ? 40.635  -26.884 23.826  1.00 21.72 ? 191  ALA A CA  1 
ATOM   1402  C  C   . ALA A  1 174 ? 40.195  -26.220 22.521  1.00 22.25 ? 191  ALA A C   1 
ATOM   1403  O  O   . ALA A  1 174 ? 40.226  -26.858 21.474  1.00 22.50 ? 191  ALA A O   1 
ATOM   1404  C  CB  . ALA A  1 174 ? 39.789  -28.100 24.104  1.00 22.70 ? 191  ALA A CB  1 
ATOM   1405  N  N   . GLY A  1 175 ? 39.766  -24.956 22.570  1.00 22.67 ? 192  GLY A N   1 
ATOM   1406  C  CA  . GLY A  1 175 ? 39.396  -24.237 21.360  1.00 22.46 ? 192  GLY A CA  1 
ATOM   1407  C  C   . GLY A  1 175 ? 38.087  -24.745 20.757  1.00 22.66 ? 192  GLY A C   1 
ATOM   1408  O  O   . GLY A  1 175 ? 37.892  -24.673 19.545  1.00 22.18 ? 192  GLY A O   1 
ATOM   1409  N  N   . ILE A  1 176 ? 37.175  -25.235 21.607  1.00 21.84 ? 193  ILE A N   1 
ATOM   1410  C  CA  . ILE A  1 176 ? 35.823  -25.525 21.169  1.00 21.65 ? 193  ILE A CA  1 
ATOM   1411  C  C   . ILE A  1 176 ? 35.107  -24.191 20.989  1.00 21.27 ? 193  ILE A C   1 
ATOM   1412  O  O   . ILE A  1 176 ? 35.150  -23.339 21.875  1.00 20.89 ? 193  ILE A O   1 
ATOM   1413  C  CB  . ILE A  1 176 ? 35.108  -26.470 22.151  1.00 22.50 ? 193  ILE A CB  1 
ATOM   1414  C  CG1 . ILE A  1 176 ? 35.789  -27.843 22.166  1.00 23.16 ? 193  ILE A CG1 1 
ATOM   1415  C  CG2 . ILE A  1 176 ? 33.620  -26.592 21.823  1.00 22.49 ? 193  ILE A CG2 1 
ATOM   1416  C  CD1 . ILE A  1 176 ? 35.434  -28.708 23.359  1.00 23.52 ? 193  ILE A CD1 1 
ATOM   1417  N  N   . ARG A  1 177 ? 34.491  -24.009 19.816  1.00 21.37 ? 194  ARG A N   1 
ATOM   1418  C  CA  . ARG A  1 177 ? 33.886  -22.739 19.451  1.00 22.16 ? 194  ARG A CA  1 
ATOM   1419  C  C   . ARG A  1 177 ? 32.797  -22.374 20.453  1.00 22.04 ? 194  ARG A C   1 
ATOM   1420  O  O   . ARG A  1 177 ? 31.885  -23.167 20.682  1.00 20.15 ? 194  ARG A O   1 
ATOM   1421  C  CB  . ARG A  1 177 ? 33.262  -22.787 18.053  1.00 24.12 ? 194  ARG A CB  1 
ATOM   1422  C  CG  . ARG A  1 177 ? 34.276  -22.707 16.923  1.00 28.24 ? 194  ARG A CG  1 
ATOM   1423  C  CD  . ARG A  1 177 ? 33.677  -23.085 15.576  1.00 31.15 ? 194  ARG A CD  1 
ATOM   1424  N  NE  . ARG A  1 177 ? 32.521  -22.241 15.257  1.00 35.92 ? 194  ARG A NE  1 
ATOM   1425  C  CZ  . ARG A  1 177 ? 32.549  -20.965 14.887  1.00 43.08 ? 194  ARG A CZ  1 
ATOM   1426  N  NH1 . ARG A  1 177 ? 33.692  -20.297 14.838  1.00 46.37 ? 194  ARG A NH1 1 
ATOM   1427  N  NH2 . ARG A  1 177 ? 31.420  -20.353 14.566  1.00 45.23 ? 194  ARG A NH2 1 
ATOM   1428  N  N   . PRO A  1 178 ? 32.849  -21.156 21.052  1.00 22.96 ? 195  PRO A N   1 
ATOM   1429  C  CA  . PRO A  1 178 ? 31.857  -20.739 22.044  1.00 22.70 ? 195  PRO A CA  1 
ATOM   1430  C  C   . PRO A  1 178 ? 30.417  -20.679 21.540  1.00 22.63 ? 195  PRO A C   1 
ATOM   1431  O  O   . PRO A  1 178 ? 29.502  -20.954 22.308  1.00 22.17 ? 195  PRO A O   1 
ATOM   1432  C  CB  . PRO A  1 178 ? 32.344  -19.372 22.557  1.00 23.59 ? 195  PRO A CB  1 
ATOM   1433  C  CG  . PRO A  1 178 ? 33.378  -18.913 21.550  1.00 24.23 ? 195  PRO A CG  1 
ATOM   1434  C  CD  . PRO A  1 178 ? 33.903  -20.150 20.846  1.00 23.16 ? 195  PRO A CD  1 
ATOM   1435  N  N   . ASP A  1 179 ? 30.208  -20.355 20.255  1.00 22.94 ? 196  ASP A N   1 
ATOM   1436  C  CA  . ASP A  1 179 ? 28.851  -20.287 19.725  1.00 24.53 ? 196  ASP A CA  1 
ATOM   1437  C  C   . ASP A  1 179 ? 28.237  -21.681 19.580  1.00 23.59 ? 196  ASP A C   1 
ATOM   1438  O  O   . ASP A  1 179 ? 27.042  -21.789 19.310  1.00 23.56 ? 196  ASP A O   1 
ATOM   1439  C  CB  . ASP A  1 179 ? 28.755  -19.497 18.427  1.00 26.32 ? 196  ASP A CB  1 
ATOM   1440  C  CG  . ASP A  1 179 ? 29.611  -19.977 17.265  1.00 29.15 ? 196  ASP A CG  1 
ATOM   1441  O  OD1 . ASP A  1 179 ? 30.456  -20.875 17.470  1.00 30.35 ? 196  ASP A OD1 1 
ATOM   1442  O  OD2 . ASP A  1 179 ? 29.436  -19.431 16.158  1.00 33.11 ? 196  ASP A OD2 1 
ATOM   1443  N  N   . ARG A  1 180 ? 29.044  -22.738 19.755  1.00 22.68 ? 197  ARG A N   1 
ATOM   1444  C  CA  . ARG A  1 180 ? 28.548  -24.106 19.669  1.00 23.56 ? 197  ARG A CA  1 
ATOM   1445  C  C   . ARG A  1 180 ? 28.437  -24.751 21.054  1.00 21.80 ? 197  ARG A C   1 
ATOM   1446  O  O   . ARG A  1 180 ? 28.230  -25.960 21.152  1.00 20.08 ? 197  ARG A O   1 
ATOM   1447  C  CB  . ARG A  1 180 ? 29.453  -24.887 18.714  1.00 24.93 ? 197  ARG A CB  1 
ATOM   1448  C  CG  . ARG A  1 180 ? 29.461  -24.221 17.346  1.00 27.94 ? 197  ARG A CG  1 
ATOM   1449  C  CD  . ARG A  1 180 ? 30.031  -25.085 16.255  1.00 31.01 ? 197  ARG A CD  1 
ATOM   1450  N  NE  . ARG A  1 180 ? 30.036  -24.369 14.974  1.00 33.67 ? 197  ARG A NE  1 
ATOM   1451  C  CZ  . ARG A  1 180 ? 30.744  -24.740 13.911  1.00 36.98 ? 197  ARG A CZ  1 
ATOM   1452  N  NH1 . ARG A  1 180 ? 31.474  -25.847 13.941  1.00 35.88 ? 197  ARG A NH1 1 
ATOM   1453  N  NH2 . ARG A  1 180 ? 30.717  -23.996 12.816  1.00 38.97 ? 197  ARG A NH2 1 
ATOM   1454  N  N   . CYS A  1 181 ? 28.528  -23.933 22.112  1.00 21.43 ? 198  CYS A N   1 
ATOM   1455  C  CA  . CYS A  1 181 ? 28.424  -24.401 23.486  1.00 20.99 ? 198  CYS A CA  1 
ATOM   1456  C  C   . CYS A  1 181 ? 27.078  -23.982 24.074  1.00 20.33 ? 198  CYS A C   1 
ATOM   1457  O  O   . CYS A  1 181 ? 26.669  -22.841 23.890  1.00 20.17 ? 198  CYS A O   1 
ATOM   1458  C  CB  . CYS A  1 181 ? 29.566  -23.849 24.330  1.00 21.80 ? 198  CYS A CB  1 
ATOM   1459  S  SG  . CYS A  1 181 ? 31.187  -24.512 23.863  1.00 22.92 ? 198  CYS A SG  1 
ATOM   1460  N  N   . LEU A  1 182 ? 26.422  -24.898 24.806  1.00 18.66 ? 199  LEU A N   1 
ATOM   1461  C  CA  . LEU A  1 182 ? 25.095  -24.648 25.357  1.00 18.96 ? 199  LEU A CA  1 
ATOM   1462  C  C   . LEU A  1 182 ? 25.025  -25.096 26.819  1.00 18.66 ? 199  LEU A C   1 
ATOM   1463  O  O   . LEU A  1 182 ? 24.907  -26.285 27.110  1.00 18.28 ? 199  LEU A O   1 
ATOM   1464  C  CB  . LEU A  1 182 ? 24.024  -25.334 24.512  1.00 18.91 ? 199  LEU A CB  1 
ATOM   1465  C  CG  . LEU A  1 182 ? 22.607  -25.325 25.097  1.00 19.68 ? 199  LEU A CG  1 
ATOM   1466  C  CD1 . LEU A  1 182 ? 22.143  -23.911 25.401  1.00 19.98 ? 199  LEU A CD1 1 
ATOM   1467  C  CD2 . LEU A  1 182 ? 21.638  -26.019 24.168  1.00 20.60 ? 199  LEU A CD2 1 
ATOM   1468  N  N   . PRO A  1 183 ? 25.074  -24.158 27.793  1.00 18.13 ? 200  PRO A N   1 
ATOM   1469  C  CA  . PRO A  1 183 ? 24.869  -24.493 29.203  1.00 18.45 ? 200  PRO A CA  1 
ATOM   1470  C  C   . PRO A  1 183 ? 23.383  -24.667 29.508  1.00 18.74 ? 200  PRO A C   1 
ATOM   1471  O  O   . PRO A  1 183 ? 22.552  -23.912 29.006  1.00 19.01 ? 200  PRO A O   1 
ATOM   1472  C  CB  . PRO A  1 183 ? 25.475  -23.310 29.983  1.00 18.79 ? 200  PRO A CB  1 
ATOM   1473  C  CG  . PRO A  1 183 ? 25.981  -22.337 28.923  1.00 18.81 ? 200  PRO A CG  1 
ATOM   1474  C  CD  . PRO A  1 183 ? 25.354  -22.729 27.595  1.00 18.47 ? 200  PRO A CD  1 
ATOM   1475  N  N   . VAL A  1 184 ? 23.058  -25.673 30.328  1.00 18.64 ? 201  VAL A N   1 
ATOM   1476  C  CA  . VAL A  1 184 ? 21.673  -26.002 30.628  1.00 18.88 ? 201  VAL A CA  1 
ATOM   1477  C  C   . VAL A  1 184 ? 21.530  -26.266 32.122  1.00 19.46 ? 201  VAL A C   1 
ATOM   1478  O  O   . VAL A  1 184 ? 22.319  -27.011 32.707  1.00 18.54 ? 201  VAL A O   1 
ATOM   1479  C  CB  . VAL A  1 184 ? 21.172  -27.212 29.820  1.00 19.05 ? 201  VAL A CB  1 
ATOM   1480  C  CG1 . VAL A  1 184 ? 19.735  -27.572 30.179  1.00 19.48 ? 201  VAL A CG1 1 
ATOM   1481  C  CG2 . VAL A  1 184 ? 21.296  -26.983 28.318  1.00 19.49 ? 201  VAL A CG2 1 
ATOM   1482  N  N   . CYS A  1 185 ? 20.495  -25.662 32.717  1.00 20.68 ? 202  CYS A N   1 
ATOM   1483  C  CA  . CYS A  1 185 ? 20.130  -25.907 34.101  1.00 22.86 ? 202  CYS A CA  1 
ATOM   1484  C  C   . CYS A  1 185 ? 18.720  -26.497 34.157  1.00 23.72 ? 202  CYS A C   1 
ATOM   1485  O  O   . CYS A  1 185 ? 17.774  -25.895 33.648  1.00 23.97 ? 202  CYS A O   1 
ATOM   1486  C  CB  . CYS A  1 185 ? 20.259  -24.624 34.909  1.00 25.77 ? 202  CYS A CB  1 
ATOM   1487  S  SG  . CYS A  1 185 ? 19.743  -24.800 36.635  1.00 31.71 ? 202  CYS A SG  1 
ATOM   1488  N  N   . ILE A  1 186 ? 18.605  -27.684 34.766  1.00 23.49 ? 203  ILE A N   1 
ATOM   1489  C  CA  . ILE A  1 186 ? 17.335  -28.363 34.988  1.00 25.30 ? 203  ILE A CA  1 
ATOM   1490  C  C   . ILE A  1 186 ? 16.825  -27.981 36.375  1.00 25.10 ? 203  ILE A C   1 
ATOM   1491  O  O   . ILE A  1 186 ? 17.498  -28.272 37.356  1.00 25.08 ? 203  ILE A O   1 
ATOM   1492  C  CB  . ILE A  1 186 ? 17.507  -29.892 34.889  1.00 27.51 ? 203  ILE A CB  1 
ATOM   1493  C  CG1 . ILE A  1 186 ? 18.148  -30.333 33.577  1.00 28.95 ? 203  ILE A CG1 1 
ATOM   1494  C  CG2 . ILE A  1 186 ? 16.183  -30.619 35.137  1.00 28.25 ? 203  ILE A CG2 1 
ATOM   1495  C  CD1 . ILE A  1 186 ? 17.339  -30.019 32.336  1.00 29.46 ? 203  ILE A CD1 1 
ATOM   1496  N  N   . ASP A  1 187 ? 15.643  -27.354 36.459  1.00 24.88 ? 204  ASP A N   1 
ATOM   1497  C  CA  . ASP A  1 187 ? 15.076  -26.950 37.737  1.00 25.67 ? 204  ASP A CA  1 
ATOM   1498  C  C   . ASP A  1 187 ? 13.860  -27.808 38.077  1.00 25.02 ? 204  ASP A C   1 
ATOM   1499  O  O   . ASP A  1 187 ? 12.774  -27.596 37.543  1.00 24.53 ? 204  ASP A O   1 
ATOM   1500  C  CB  . ASP A  1 187 ? 14.642  -25.493 37.753  1.00 26.08 ? 204  ASP A CB  1 
ATOM   1501  C  CG  . ASP A  1 187 ? 14.074  -25.009 39.083  1.00 27.26 ? 204  ASP A CG  1 
ATOM   1502  O  OD1 . ASP A  1 187 ? 14.252  -25.718 40.104  1.00 27.64 ? 204  ASP A OD1 1 
ATOM   1503  O  OD2 . ASP A  1 187 ? 13.465  -23.920 39.098  1.00 25.68 ? 204  ASP A OD2 1 
ATOM   1504  N  N   . VAL A  1 188 ? 14.034  -28.732 39.026  1.00 25.54 ? 205  VAL A N   1 
ATOM   1505  C  CA  . VAL A  1 188 ? 12.936  -29.573 39.473  1.00 25.93 ? 205  VAL A CA  1 
ATOM   1506  C  C   . VAL A  1 188 ? 12.622  -29.292 40.942  1.00 25.76 ? 205  VAL A C   1 
ATOM   1507  O  O   . VAL A  1 188 ? 11.913  -30.068 41.581  1.00 27.38 ? 205  VAL A O   1 
ATOM   1508  C  CB  . VAL A  1 188 ? 13.289  -31.050 39.223  1.00 26.30 ? 205  VAL A CB  1 
ATOM   1509  C  CG1 . VAL A  1 188 ? 13.582  -31.297 37.747  1.00 26.00 ? 205  VAL A CG1 1 
ATOM   1510  C  CG2 . VAL A  1 188 ? 14.448  -31.516 40.099  1.00 26.48 ? 205  VAL A CG2 1 
ATOM   1511  N  N   . GLY A  1 189 ? 13.129  -28.164 41.455  1.00 25.62 ? 206  GLY A N   1 
ATOM   1512  C  CA  . GLY A  1 189 ? 13.008  -27.808 42.859  1.00 25.44 ? 206  GLY A CA  1 
ATOM   1513  C  C   . GLY A  1 189 ? 14.357  -27.881 43.569  1.00 26.02 ? 206  GLY A C   1 
ATOM   1514  O  O   . GLY A  1 189 ? 15.378  -28.162 42.943  1.00 26.22 ? 206  GLY A O   1 
ATOM   1515  N  N   . THR A  1 190 ? 14.339  -27.634 44.884  1.00 26.31 ? 207  THR A N   1 
ATOM   1516  C  CA  . THR A  1 190 ? 15.528  -27.715 45.715  1.00 26.95 ? 207  THR A CA  1 
ATOM   1517  C  C   . THR A  1 190 ? 15.134  -28.171 47.120  1.00 27.89 ? 207  THR A C   1 
ATOM   1518  O  O   . THR A  1 190 ? 14.079  -27.791 47.625  1.00 27.23 ? 207  THR A O   1 
ATOM   1519  C  CB  . THR A  1 190 ? 16.236  -26.363 45.747  1.00 26.16 ? 207  THR A CB  1 
ATOM   1520  O  OG1 . THR A  1 190 ? 17.386  -26.569 46.563  1.00 25.29 ? 207  THR A OG1 1 
ATOM   1521  C  CG2 . THR A  1 190 ? 15.373  -25.253 46.318  1.00 26.54 ? 207  THR A CG2 1 
ATOM   1522  N  N   . ASP A  1 191 ? 16.002  -28.974 47.745  1.00 27.97 ? 208  ASP A N   1 
ATOM   1523  C  CA  . ASP A  1 191 ? 15.785  -29.421 49.114  1.00 30.33 ? 208  ASP A CA  1 
ATOM   1524  C  C   . ASP A  1 191 ? 16.469  -28.471 50.098  1.00 29.84 ? 208  ASP A C   1 
ATOM   1525  O  O   . ASP A  1 191 ? 16.371  -28.662 51.306  1.00 29.55 ? 208  ASP A O   1 
ATOM   1526  C  CB  . ASP A  1 191 ? 16.211  -30.870 49.297  1.00 31.42 ? 208  ASP A CB  1 
ATOM   1527  C  CG  . ASP A  1 191 ? 15.266  -31.909 48.704  1.00 32.62 ? 208  ASP A CG  1 
ATOM   1528  O  OD1 . ASP A  1 191 ? 14.219  -31.512 48.143  1.00 33.09 ? 208  ASP A OD1 1 
ATOM   1529  O  OD2 . ASP A  1 191 ? 15.580  -33.113 48.814  1.00 33.74 ? 208  ASP A OD2 1 
ATOM   1530  N  N   . ASN A  1 192 ? 17.157  -27.450 49.576  1.00 29.67 ? 209  ASN A N   1 
ATOM   1531  C  CA  . ASN A  1 192 ? 17.821  -26.452 50.396  1.00 30.50 ? 209  ASN A CA  1 
ATOM   1532  C  C   . ASN A  1 192 ? 16.757  -25.567 51.047  1.00 32.01 ? 209  ASN A C   1 
ATOM   1533  O  O   . ASN A  1 192 ? 16.100  -24.782 50.366  1.00 31.61 ? 209  ASN A O   1 
ATOM   1534  C  CB  . ASN A  1 192 ? 18.814  -25.655 49.557  1.00 30.28 ? 209  ASN A CB  1 
ATOM   1535  C  CG  . ASN A  1 192 ? 19.727  -24.783 50.382  1.00 30.30 ? 209  ASN A CG  1 
ATOM   1536  O  OD1 . ASN A  1 192 ? 19.303  -24.206 51.390  1.00 30.99 ? 209  ASN A OD1 1 
ATOM   1537  N  ND2 . ASN A  1 192 ? 20.983  -24.672 49.976  1.00 30.08 ? 209  ASN A ND2 1 
ATOM   1538  N  N   . ILE A  1 193 ? 16.605  -25.704 52.370  1.00 33.50 ? 210  ILE A N   1 
ATOM   1539  C  CA  . ILE A  1 193 ? 15.564  -25.026 53.133  1.00 35.36 ? 210  ILE A CA  1 
ATOM   1540  C  C   . ILE A  1 193 ? 15.802  -23.516 53.115  1.00 33.01 ? 210  ILE A C   1 
ATOM   1541  O  O   . ILE A  1 193 ? 14.847  -22.742 53.078  1.00 33.35 ? 210  ILE A O   1 
ATOM   1542  C  CB  . ILE A  1 193 ? 15.509  -25.560 54.578  1.00 38.57 ? 210  ILE A CB  1 
ATOM   1543  C  CG1 . ILE A  1 193 ? 15.199  -27.060 54.628  1.00 42.18 ? 210  ILE A CG1 1 
ATOM   1544  C  CG2 . ILE A  1 193 ? 14.519  -24.759 55.425  1.00 39.80 ? 210  ILE A CG2 1 
ATOM   1545  C  CD1 . ILE A  1 193 ? 13.817  -27.434 54.129  1.00 43.35 ? 210  ILE A CD1 1 
ATOM   1546  N  N   . ALA A  1 194 ? 17.074  -23.110 53.161  1.00 31.06 ? 211  ALA A N   1 
ATOM   1547  C  CA  . ALA A  1 194 ? 17.435  -21.702 53.114  1.00 31.52 ? 211  ALA A CA  1 
ATOM   1548  C  C   . ALA A  1 194 ? 16.919  -21.053 51.827  1.00 30.56 ? 211  ALA A C   1 
ATOM   1549  O  O   . ALA A  1 194 ? 16.406  -19.938 51.868  1.00 30.21 ? 211  ALA A O   1 
ATOM   1550  C  CB  . ALA A  1 194 ? 18.933  -21.543 53.259  1.00 31.24 ? 211  ALA A CB  1 
ATOM   1551  N  N   . LEU A  1 195 ? 17.021  -21.763 50.693  1.00 29.20 ? 212  LEU A N   1 
ATOM   1552  C  CA  . LEU A  1 195 ? 16.621  -21.214 49.406  1.00 28.81 ? 212  LEU A CA  1 
ATOM   1553  C  C   . LEU A  1 195 ? 15.099  -21.132 49.323  1.00 29.46 ? 212  LEU A C   1 
ATOM   1554  O  O   . LEU A  1 195 ? 14.554  -20.189 48.752  1.00 28.42 ? 212  LEU A O   1 
ATOM   1555  C  CB  . LEU A  1 195 ? 17.209  -22.049 48.267  1.00 28.87 ? 212  LEU A CB  1 
ATOM   1556  C  CG  . LEU A  1 195 ? 18.740  -22.128 48.228  1.00 29.36 ? 212  LEU A CG  1 
ATOM   1557  C  CD1 . LEU A  1 195 ? 19.243  -22.900 47.016  1.00 29.79 ? 212  LEU A CD1 1 
ATOM   1558  C  CD2 . LEU A  1 195 ? 19.362  -20.750 48.261  1.00 30.19 ? 212  LEU A CD2 1 
ATOM   1559  N  N   . LEU A  1 196 ? 14.414  -22.114 49.916  1.00 29.21 ? 213  LEU A N   1 
ATOM   1560  C  CA  . LEU A  1 196 ? 12.963  -22.164 49.858  1.00 30.54 ? 213  LEU A CA  1 
ATOM   1561  C  C   . LEU A  1 196 ? 12.338  -20.982 50.602  1.00 31.50 ? 213  LEU A C   1 
ATOM   1562  O  O   . LEU A  1 196 ? 11.206  -20.612 50.299  1.00 32.25 ? 213  LEU A O   1 
ATOM   1563  C  CB  . LEU A  1 196 ? 12.469  -23.506 50.401  1.00 30.88 ? 213  LEU A CB  1 
ATOM   1564  C  CG  . LEU A  1 196 ? 12.748  -24.728 49.518  1.00 31.24 ? 213  LEU A CG  1 
ATOM   1565  C  CD1 . LEU A  1 196 ? 12.232  -25.992 50.181  1.00 32.08 ? 213  LEU A CD1 1 
ATOM   1566  C  CD2 . LEU A  1 196 ? 12.135  -24.575 48.133  1.00 30.93 ? 213  LEU A CD2 1 
ATOM   1567  N  N   . LYS A  1 197 ? 13.080  -20.395 51.552  1.00 32.55 ? 214  LYS A N   1 
ATOM   1568  C  CA  . LYS A  1 197 ? 12.601  -19.277 52.350  1.00 35.42 ? 214  LYS A CA  1 
ATOM   1569  C  C   . LYS A  1 197 ? 13.175  -17.949 51.853  1.00 34.08 ? 214  LYS A C   1 
ATOM   1570  O  O   . LYS A  1 197 ? 12.948  -16.914 52.481  1.00 33.95 ? 214  LYS A O   1 
ATOM   1571  C  CB  . LYS A  1 197 ? 13.014  -19.453 53.818  1.00 38.57 ? 214  LYS A CB  1 
ATOM   1572  C  CG  . LYS A  1 197 ? 12.461  -20.693 54.507  1.00 42.81 ? 214  LYS A CG  1 
ATOM   1573  C  CD  . LYS A  1 197 ? 12.903  -20.829 55.960  1.00 46.38 ? 214  LYS A CD  1 
ATOM   1574  C  CE  . LYS A  1 197 ? 12.368  -22.056 56.633  1.00 48.46 ? 214  LYS A CE  1 
ATOM   1575  N  NZ  . LYS A  1 197 ? 10.907  -22.038 56.740  1.00 50.57 ? 214  LYS A NZ  1 
ATOM   1576  N  N   . ASP A  1 198 ? 13.926  -17.982 50.741  1.00 31.01 ? 215  ASP A N   1 
ATOM   1577  C  CA  . ASP A  1 198 ? 14.641  -16.815 50.248  1.00 30.23 ? 215  ASP A CA  1 
ATOM   1578  C  C   . ASP A  1 198 ? 13.772  -16.092 49.220  1.00 29.25 ? 215  ASP A C   1 
ATOM   1579  O  O   . ASP A  1 198 ? 13.514  -16.624 48.144  1.00 27.83 ? 215  ASP A O   1 
ATOM   1580  C  CB  . ASP A  1 198 ? 15.995  -17.210 49.674  1.00 30.36 ? 215  ASP A CB  1 
ATOM   1581  C  CG  . ASP A  1 198 ? 16.912  -16.072 49.236  1.00 31.72 ? 215  ASP A CG  1 
ATOM   1582  O  OD1 . ASP A  1 198 ? 16.454  -14.910 49.216  1.00 32.95 ? 215  ASP A OD1 1 
ATOM   1583  O  OD2 . ASP A  1 198 ? 18.089  -16.355 48.920  1.00 33.24 ? 215  ASP A OD2 1 
ATOM   1584  N  N   . PRO A  1 199 ? 13.338  -14.838 49.480  1.00 29.59 ? 216  PRO A N   1 
ATOM   1585  C  CA  . PRO A  1 199 ? 12.524  -14.104 48.511  1.00 29.61 ? 216  PRO A CA  1 
ATOM   1586  C  C   . PRO A  1 199 ? 13.276  -13.767 47.221  1.00 28.98 ? 216  PRO A C   1 
ATOM   1587  O  O   . PRO A  1 199 ? 12.656  -13.413 46.217  1.00 28.92 ? 216  PRO A O   1 
ATOM   1588  C  CB  . PRO A  1 199 ? 12.077  -12.853 49.293  1.00 30.54 ? 216  PRO A CB  1 
ATOM   1589  C  CG  . PRO A  1 199 ? 13.145  -12.662 50.344  1.00 31.11 ? 216  PRO A CG  1 
ATOM   1590  C  CD  . PRO A  1 199 ? 13.626  -14.059 50.696  1.00 30.42 ? 216  PRO A CD  1 
ATOM   1591  N  N   . PHE A  1 200 ? 14.607  -13.915 47.246  1.00 28.72 ? 217  PHE A N   1 
ATOM   1592  C  CA  . PHE A  1 200 ? 15.444  -13.595 46.100  1.00 28.85 ? 217  PHE A CA  1 
ATOM   1593  C  C   . PHE A  1 200 ? 15.885  -14.853 45.353  1.00 28.46 ? 217  PHE A C   1 
ATOM   1594  O  O   . PHE A  1 200 ? 16.616  -14.739 44.371  1.00 28.74 ? 217  PHE A O   1 
ATOM   1595  C  CB  . PHE A  1 200 ? 16.642  -12.787 46.602  1.00 29.55 ? 217  PHE A CB  1 
ATOM   1596  C  CG  . PHE A  1 200 ? 16.249  -11.470 47.253  1.00 31.10 ? 217  PHE A CG  1 
ATOM   1597  C  CD1 . PHE A  1 200 ? 15.420  -10.568 46.592  1.00 31.37 ? 217  PHE A CD1 1 
ATOM   1598  C  CD2 . PHE A  1 200 ? 16.672  -11.157 48.542  1.00 32.95 ? 217  PHE A CD2 1 
ATOM   1599  C  CE1 . PHE A  1 200 ? 15.057  -9.373  47.192  1.00 32.54 ? 217  PHE A CE1 1 
ATOM   1600  C  CE2 . PHE A  1 200 ? 16.296  -9.963  49.141  1.00 33.44 ? 217  PHE A CE2 1 
ATOM   1601  C  CZ  . PHE A  1 200 ? 15.488  -9.077  48.467  1.00 32.84 ? 217  PHE A CZ  1 
ATOM   1602  N  N   . TYR A  1 201 ? 15.447  -16.040 45.803  1.00 28.22 ? 218  TYR A N   1 
ATOM   1603  C  CA  . TYR A  1 201 ? 15.762  -17.274 45.097  1.00 27.83 ? 218  TYR A CA  1 
ATOM   1604  C  C   . TYR A  1 201 ? 15.115  -17.208 43.713  1.00 27.42 ? 218  TYR A C   1 
ATOM   1605  O  O   . TYR A  1 201 ? 13.984  -16.748 43.576  1.00 29.32 ? 218  TYR A O   1 
ATOM   1606  C  CB  . TYR A  1 201 ? 15.340  -18.516 45.896  1.00 27.06 ? 218  TYR A CB  1 
ATOM   1607  C  CG  . TYR A  1 201 ? 15.610  -19.835 45.182  1.00 25.52 ? 218  TYR A CG  1 
ATOM   1608  C  CD1 . TYR A  1 201 ? 16.883  -20.171 44.732  1.00 25.78 ? 218  TYR A CD1 1 
ATOM   1609  C  CD2 . TYR A  1 201 ? 14.578  -20.720 44.901  1.00 25.72 ? 218  TYR A CD2 1 
ATOM   1610  C  CE1 . TYR A  1 201 ? 17.124  -21.359 44.058  1.00 25.34 ? 218  TYR A CE1 1 
ATOM   1611  C  CE2 . TYR A  1 201 ? 14.803  -21.904 44.219  1.00 25.90 ? 218  TYR A CE2 1 
ATOM   1612  C  CZ  . TYR A  1 201 ? 16.080  -22.229 43.796  1.00 26.14 ? 218  TYR A CZ  1 
ATOM   1613  O  OH  . TYR A  1 201 ? 16.283  -23.400 43.114  1.00 25.55 ? 218  TYR A OH  1 
ATOM   1614  N  N   . MET A  1 202 ? 15.841  -17.677 42.693  1.00 28.24 ? 219  MET A N   1 
ATOM   1615  C  CA  . MET A  1 202 ? 15.472  -17.459 41.302  1.00 27.91 ? 219  MET A CA  1 
ATOM   1616  C  C   . MET A  1 202 ? 14.903  -18.726 40.657  1.00 27.65 ? 219  MET A C   1 
ATOM   1617  O  O   . MET A  1 202 ? 14.760  -18.779 39.434  1.00 26.27 ? 219  MET A O   1 
ATOM   1618  C  CB  . MET A  1 202 ? 16.695  -16.974 40.514  1.00 30.16 ? 219  MET A CB  1 
ATOM   1619  C  CG  . MET A  1 202 ? 17.231  -15.639 40.991  1.00 32.51 ? 219  MET A CG  1 
ATOM   1620  S  SD  . MET A  1 202 ? 18.617  -15.023 40.013  1.00 37.24 ? 219  MET A SD  1 
ATOM   1621  C  CE  . MET A  1 202 ? 19.944  -16.129 40.515  1.00 37.70 ? 219  MET A CE  1 
ATOM   1622  N  N   . GLY A  1 203 ? 14.563  -19.739 41.469  1.00 25.20 ? 220  GLY A N   1 
ATOM   1623  C  CA  . GLY A  1 203 ? 14.050  -21.002 40.961  1.00 24.76 ? 220  GLY A CA  1 
ATOM   1624  C  C   . GLY A  1 203 ? 12.643  -21.295 41.479  1.00 25.68 ? 220  GLY A C   1 
ATOM   1625  O  O   . GLY A  1 203 ? 12.023  -20.439 42.102  1.00 26.11 ? 220  GLY A O   1 
ATOM   1626  N  N   . LEU A  1 204 ? 12.147  -22.511 41.202  1.00 26.57 ? 221  LEU A N   1 
ATOM   1627  C  CA  . LEU A  1 204 ? 10.835  -22.942 41.656  1.00 27.50 ? 221  LEU A CA  1 
ATOM   1628  C  C   . LEU A  1 204 ? 10.880  -23.149 43.168  1.00 27.68 ? 221  LEU A C   1 
ATOM   1629  O  O   . LEU A  1 204 ? 11.833  -23.729 43.691  1.00 25.88 ? 221  LEU A O   1 
ATOM   1630  C  CB  . LEU A  1 204 ? 10.393  -24.225 40.950  1.00 28.36 ? 221  LEU A CB  1 
ATOM   1631  C  CG  . LEU A  1 204 ? 10.186  -24.158 39.433  1.00 29.46 ? 221  LEU A CG  1 
ATOM   1632  C  CD1 . LEU A  1 204 ? 9.920   -25.574 38.940  1.00 30.26 ? 221  LEU A CD1 1 
ATOM   1633  C  CD2 . LEU A  1 204 ? 9.065   -23.222 38.996  1.00 30.67 ? 221  LEU A CD2 1 
ATOM   1634  N  N   . TYR A  1 205 ? 9.836   -22.669 43.859  1.00 27.23 ? 222  TYR A N   1 
ATOM   1635  C  CA  . TYR A  1 205 ? 9.714   -22.841 45.297  1.00 27.84 ? 222  TYR A CA  1 
ATOM   1636  C  C   . TYR A  1 205 ? 8.998   -24.159 45.574  1.00 28.79 ? 222  TYR A C   1 
ATOM   1637  O  O   . TYR A  1 205 ? 7.802   -24.182 45.854  1.00 28.69 ? 222  TYR A O   1 
ATOM   1638  C  CB  . TYR A  1 205 ? 8.977   -21.665 45.948  1.00 28.39 ? 222  TYR A CB  1 
ATOM   1639  C  CG  . TYR A  1 205 ? 9.752   -20.355 45.983  1.00 27.44 ? 222  TYR A CG  1 
ATOM   1640  C  CD1 . TYR A  1 205 ? 10.820  -20.170 46.856  1.00 27.15 ? 222  TYR A CD1 1 
ATOM   1641  C  CD2 . TYR A  1 205 ? 9.395   -19.292 45.162  1.00 28.35 ? 222  TYR A CD2 1 
ATOM   1642  C  CE1 . TYR A  1 205 ? 11.517  -18.972 46.901  1.00 26.68 ? 222  TYR A CE1 1 
ATOM   1643  C  CE2 . TYR A  1 205 ? 10.085  -18.090 45.196  1.00 28.28 ? 222  TYR A CE2 1 
ATOM   1644  C  CZ  . TYR A  1 205 ? 11.151  -17.931 46.065  1.00 28.04 ? 222  TYR A CZ  1 
ATOM   1645  O  OH  . TYR A  1 205 ? 11.816  -16.739 46.101  1.00 29.20 ? 222  TYR A OH  1 
ATOM   1646  N  N   . GLN A  1 206 ? 9.744   -25.259 45.455  1.00 28.87 ? 223  GLN A N   1 
ATOM   1647  C  CA  . GLN A  1 206 ? 9.253   -26.576 45.815  1.00 28.80 ? 223  GLN A CA  1 
ATOM   1648  C  C   . GLN A  1 206 ? 10.454  -27.455 46.141  1.00 28.51 ? 223  GLN A C   1 
ATOM   1649  O  O   . GLN A  1 206 ? 11.560  -27.190 45.673  1.00 25.53 ? 223  GLN A O   1 
ATOM   1650  C  CB  . GLN A  1 206 ? 8.416   -27.187 44.688  1.00 30.85 ? 223  GLN A CB  1 
ATOM   1651  C  CG  . GLN A  1 206 ? 9.195   -27.487 43.409  1.00 31.43 ? 223  GLN A CG  1 
ATOM   1652  C  CD  . GLN A  1 206 ? 8.364   -28.173 42.345  1.00 31.73 ? 223  GLN A CD  1 
ATOM   1653  O  OE1 . GLN A  1 206 ? 7.381   -27.621 41.844  1.00 33.20 ? 223  GLN A OE1 1 
ATOM   1654  N  NE2 . GLN A  1 206 ? 8.753   -29.383 41.965  1.00 31.88 ? 223  GLN A NE2 1 
ATOM   1655  N  N   . LYS A  1 207 ? 10.211  -28.504 46.934  1.00 28.90 ? 224  LYS A N   1 
ATOM   1656  C  CA  . LYS A  1 207 ? 11.175  -29.573 47.126  1.00 30.74 ? 224  LYS A CA  1 
ATOM   1657  C  C   . LYS A  1 207 ? 11.433  -30.250 45.783  1.00 27.98 ? 224  LYS A C   1 
ATOM   1658  O  O   . LYS A  1 207 ? 10.603  -30.175 44.882  1.00 28.06 ? 224  LYS A O   1 
ATOM   1659  C  CB  . LYS A  1 207 ? 10.639  -30.648 48.078  1.00 34.91 ? 224  LYS A CB  1 
ATOM   1660  C  CG  . LYS A  1 207 ? 10.259  -30.208 49.486  1.00 39.38 ? 224  LYS A CG  1 
ATOM   1661  C  CD  . LYS A  1 207 ? 11.423  -30.003 50.444  1.00 43.28 ? 224  LYS A CD  1 
ATOM   1662  C  CE  . LYS A  1 207 ? 10.949  -30.090 51.862  1.00 47.11 ? 224  LYS A CE  1 
ATOM   1663  N  NZ  . LYS A  1 207 ? 11.871  -29.437 52.792  1.00 48.73 ? 224  LYS A NZ  1 
ATOM   1664  N  N   . ARG A  1 208 ? 12.568  -30.945 45.677  1.00 27.40 ? 225  ARG A N   1 
ATOM   1665  C  CA  . ARG A  1 208 ? 12.931  -31.640 44.454  1.00 27.43 ? 225  ARG A CA  1 
ATOM   1666  C  C   . ARG A  1 208 ? 11.887  -32.698 44.116  1.00 28.56 ? 225  ARG A C   1 
ATOM   1667  O  O   . ARG A  1 208 ? 11.453  -33.452 44.985  1.00 29.91 ? 225  ARG A O   1 
ATOM   1668  C  CB  . ARG A  1 208 ? 14.312  -32.294 44.572  1.00 27.07 ? 225  ARG A CB  1 
ATOM   1669  C  CG  . ARG A  1 208 ? 15.434  -31.273 44.507  1.00 25.87 ? 225  ARG A CG  1 
ATOM   1670  C  CD  . ARG A  1 208 ? 16.813  -31.907 44.452  1.00 24.83 ? 225  ARG A CD  1 
ATOM   1671  N  NE  . ARG A  1 208 ? 17.802  -30.861 44.169  1.00 24.49 ? 225  ARG A NE  1 
ATOM   1672  C  CZ  . ARG A  1 208 ? 18.037  -30.267 42.995  1.00 22.92 ? 225  ARG A CZ  1 
ATOM   1673  N  NH1 . ARG A  1 208 ? 17.584  -30.788 41.874  1.00 21.76 ? 225  ARG A NH1 1 
ATOM   1674  N  NH2 . ARG A  1 208 ? 18.781  -29.170 42.948  1.00 22.87 ? 225  ARG A NH2 1 
ATOM   1675  N  N   . ASP A  1 209 ? 11.501  -32.738 42.840  1.00 28.46 ? 226  ASP A N   1 
ATOM   1676  C  CA  . ASP A  1 209 ? 10.647  -33.792 42.325  1.00 30.38 ? 226  ASP A CA  1 
ATOM   1677  C  C   . ASP A  1 209 ? 11.481  -35.063 42.175  1.00 30.61 ? 226  ASP A C   1 
ATOM   1678  O  O   . ASP A  1 209 ? 12.474  -35.075 41.448  1.00 28.38 ? 226  ASP A O   1 
ATOM   1679  C  CB  . ASP A  1 209 ? 10.004  -33.375 41.015  1.00 31.06 ? 226  ASP A CB  1 
ATOM   1680  C  CG  . ASP A  1 209 ? 8.879   -34.272 40.521  1.00 32.17 ? 226  ASP A CG  1 
ATOM   1681  O  OD1 . ASP A  1 209 ? 9.055   -35.512 40.539  1.00 32.60 ? 226  ASP A OD1 1 
ATOM   1682  O  OD2 . ASP A  1 209 ? 7.851   -33.718 40.085  1.00 33.16 ? 226  ASP A OD2 1 
ATOM   1683  N  N   . ARG A  1 210 ? 11.068  -36.123 42.883  1.00 31.13 ? 227  ARG A N   1 
ATOM   1684  C  CA  . ARG A  1 210 ? 11.750  -37.406 42.833  1.00 32.22 ? 227  ARG A CA  1 
ATOM   1685  C  C   . ARG A  1 210 ? 10.778  -38.489 42.371  1.00 32.44 ? 227  ARG A C   1 
ATOM   1686  O  O   . ARG A  1 210 ? 10.887  -39.641 42.780  1.00 35.26 ? 227  ARG A O   1 
ATOM   1687  C  CB  . ARG A  1 210 ? 12.364  -37.693 44.207  1.00 35.12 ? 227  ARG A CB  1 
ATOM   1688  C  CG  . ARG A  1 210 ? 13.429  -36.675 44.590  1.00 36.45 ? 227  ARG A CG  1 
ATOM   1689  C  CD  . ARG A  1 210 ? 13.949  -36.931 45.984  1.00 38.73 ? 227  ARG A CD  1 
ATOM   1690  N  NE  . ARG A  1 210 ? 14.878  -35.914 46.491  1.00 39.16 ? 227  ARG A NE  1 
ATOM   1691  C  CZ  . ARG A  1 210 ? 16.104  -35.648 46.046  1.00 39.48 ? 227  ARG A CZ  1 
ATOM   1692  N  NH1 . ARG A  1 210 ? 16.574  -36.198 44.940  1.00 41.51 ? 227  ARG A NH1 1 
ATOM   1693  N  NH2 . ARG A  1 210 ? 16.862  -34.799 46.713  1.00 38.01 ? 227  ARG A NH2 1 
ATOM   1694  N  N   . THR A  1 211 ? 9.830   -38.101 41.509  1.00 30.96 ? 228  THR A N   1 
ATOM   1695  C  CA  . THR A  1 211 ? 8.873   -39.027 40.928  1.00 29.74 ? 228  THR A CA  1 
ATOM   1696  C  C   . THR A  1 211 ? 9.333   -39.374 39.517  1.00 28.30 ? 228  THR A C   1 
ATOM   1697  O  O   . THR A  1 211 ? 10.406  -38.948 39.082  1.00 26.89 ? 228  THR A O   1 
ATOM   1698  C  CB  . THR A  1 211 ? 7.475   -38.404 40.936  1.00 30.49 ? 228  THR A CB  1 
ATOM   1699  O  OG1 . THR A  1 211 ? 7.463   -37.343 39.983  1.00 30.38 ? 228  THR A OG1 1 
ATOM   1700  C  CG2 . THR A  1 211 ? 7.078   -37.882 42.304  1.00 30.28 ? 228  THR A CG2 1 
ATOM   1701  N  N   . GLN A  1 212 ? 8.481   -40.126 38.810  1.00 27.81 ? 229  GLN A N   1 
ATOM   1702  C  CA  . GLN A  1 212 ? 8.682   -40.470 37.412  1.00 28.75 ? 229  GLN A CA  1 
ATOM   1703  C  C   . GLN A  1 212 ? 8.762   -39.208 36.548  1.00 29.34 ? 229  GLN A C   1 
ATOM   1704  O  O   . GLN A  1 212 ? 9.372   -39.237 35.479  1.00 27.57 ? 229  GLN A O   1 
ATOM   1705  C  CB  . GLN A  1 212 ? 7.541   -41.382 36.958  1.00 29.27 ? 229  GLN A CB  1 
ATOM   1706  C  CG  . GLN A  1 212 ? 7.707   -41.980 35.565  1.00 30.12 ? 229  GLN A CG  1 
ATOM   1707  C  CD  . GLN A  1 212 ? 8.951   -42.833 35.439  1.00 32.53 ? 229  GLN A CD  1 
ATOM   1708  O  OE1 . GLN A  1 212 ? 9.238   -43.679 36.293  1.00 32.89 ? 229  GLN A OE1 1 
ATOM   1709  N  NE2 . GLN A  1 212 ? 9.720   -42.601 34.383  1.00 34.76 ? 229  GLN A NE2 1 
ATOM   1710  N  N   . GLN A  1 213 ? 8.144   -38.108 37.003  1.00 27.81 ? 230  GLN A N   1 
ATOM   1711  C  CA  . GLN A  1 213 ? 8.181   -36.855 36.260  1.00 28.67 ? 230  GLN A CA  1 
ATOM   1712  C  C   . GLN A  1 213 ? 9.625   -36.384 36.074  1.00 26.19 ? 230  GLN A C   1 
ATOM   1713  O  O   . GLN A  1 213 ? 9.961   -35.859 35.017  1.00 26.16 ? 230  GLN A O   1 
ATOM   1714  C  CB  . GLN A  1 213 ? 7.321   -35.787 36.937  1.00 29.60 ? 230  GLN A CB  1 
ATOM   1715  C  CG  . GLN A  1 213 ? 5.839   -36.143 36.962  1.00 31.29 ? 230  GLN A CG  1 
ATOM   1716  C  CD  . GLN A  1 213 ? 4.950   -35.000 37.396  1.00 34.11 ? 230  GLN A CD  1 
ATOM   1717  O  OE1 . GLN A  1 213 ? 5.396   -34.013 37.993  1.00 36.29 ? 230  GLN A OE1 1 
ATOM   1718  N  NE2 . GLN A  1 213 ? 3.666   -35.132 37.101  1.00 35.37 ? 230  GLN A NE2 1 
ATOM   1719  N  N   . TYR A  1 214 ? 10.464  -36.579 37.098  1.00 25.31 ? 231  TYR A N   1 
ATOM   1720  C  CA  . TYR A  1 214 ? 11.866  -36.194 37.043  1.00 25.20 ? 231  TYR A CA  1 
ATOM   1721  C  C   . TYR A  1 214 ? 12.570  -36.955 35.919  1.00 25.39 ? 231  TYR A C   1 
ATOM   1722  O  O   . TYR A  1 214 ? 13.198  -36.343 35.065  1.00 25.30 ? 231  TYR A O   1 
ATOM   1723  C  CB  . TYR A  1 214 ? 12.554  -36.409 38.396  1.00 25.08 ? 231  TYR A CB  1 
ATOM   1724  C  CG  . TYR A  1 214 ? 14.057  -36.159 38.362  1.00 25.04 ? 231  TYR A CG  1 
ATOM   1725  C  CD1 . TYR A  1 214 ? 14.569  -34.868 38.348  1.00 25.39 ? 231  TYR A CD1 1 
ATOM   1726  C  CD2 . TYR A  1 214 ? 14.961  -37.214 38.335  1.00 25.24 ? 231  TYR A CD2 1 
ATOM   1727  C  CE1 . TYR A  1 214 ? 15.934  -34.630 38.301  1.00 25.35 ? 231  TYR A CE1 1 
ATOM   1728  C  CE2 . TYR A  1 214 ? 16.328  -36.992 38.283  1.00 25.37 ? 231  TYR A CE2 1 
ATOM   1729  C  CZ  . TYR A  1 214 ? 16.815  -35.696 38.266  1.00 25.34 ? 231  TYR A CZ  1 
ATOM   1730  O  OH  . TYR A  1 214 ? 18.159  -35.469 38.227  1.00 25.51 ? 231  TYR A OH  1 
ATOM   1731  N  N   . ASP A  1 215 ? 12.459  -38.287 35.930  1.00 24.93 ? 232  ASP A N   1 
ATOM   1732  C  CA  . ASP A  1 215 ? 13.068  -39.133 34.913  1.00 25.93 ? 232  ASP A CA  1 
ATOM   1733  C  C   . ASP A  1 215 ? 12.549  -38.787 33.521  1.00 25.17 ? 232  ASP A C   1 
ATOM   1734  O  O   . ASP A  1 215 ? 13.315  -38.771 32.559  1.00 24.31 ? 232  ASP A O   1 
ATOM   1735  C  CB  . ASP A  1 215 ? 12.817  -40.603 35.205  1.00 27.04 ? 232  ASP A CB  1 
ATOM   1736  C  CG  . ASP A  1 215 ? 13.578  -41.171 36.393  1.00 28.77 ? 232  ASP A CG  1 
ATOM   1737  O  OD1 . ASP A  1 215 ? 13.725  -40.446 37.398  1.00 28.22 ? 232  ASP A OD1 1 
ATOM   1738  O  OD2 . ASP A  1 215 ? 13.999  -42.344 36.308  1.00 32.06 ? 232  ASP A OD2 1 
ATOM   1739  N  N   . ASP A  1 216 ? 11.239  -38.529 33.419  1.00 24.05 ? 233  ASP A N   1 
ATOM   1740  C  CA  . ASP A  1 216 ? 10.608  -38.224 32.143  1.00 24.92 ? 233  ASP A CA  1 
ATOM   1741  C  C   . ASP A  1 216 ? 11.127  -36.893 31.593  1.00 22.76 ? 233  ASP A C   1 
ATOM   1742  O  O   . ASP A  1 216 ? 11.277  -36.736 30.386  1.00 22.97 ? 233  ASP A O   1 
ATOM   1743  C  CB  . ASP A  1 216 ? 9.090   -38.231 32.270  1.00 26.65 ? 233  ASP A CB  1 
ATOM   1744  C  CG  . ASP A  1 216 ? 8.446   -39.596 32.474  1.00 28.87 ? 233  ASP A CG  1 
ATOM   1745  O  OD1 . ASP A  1 216 ? 9.175   -40.617 32.434  1.00 30.30 ? 233  ASP A OD1 1 
ATOM   1746  O  OD2 . ASP A  1 216 ? 7.217   -39.629 32.681  1.00 30.63 ? 233  ASP A OD2 1 
ATOM   1747  N  N   . LEU A  1 217 ? 11.390  -35.932 32.481  1.00 23.19 ? 234  LEU A N   1 
ATOM   1748  C  CA  . LEU A  1 217 ? 11.896  -34.630 32.068  1.00 23.25 ? 234  LEU A CA  1 
ATOM   1749  C  C   . LEU A  1 217 ? 13.301  -34.773 31.487  1.00 22.17 ? 234  LEU A C   1 
ATOM   1750  O  O   . LEU A  1 217 ? 13.604  -34.175 30.460  1.00 21.91 ? 234  LEU A O   1 
ATOM   1751  C  CB  . LEU A  1 217 ? 11.892  -33.648 33.235  1.00 22.65 ? 234  LEU A CB  1 
ATOM   1752  C  CG  . LEU A  1 217 ? 12.205  -32.191 32.876  1.00 22.88 ? 234  LEU A CG  1 
ATOM   1753  C  CD1 . LEU A  1 217 ? 11.070  -31.579 32.070  1.00 23.32 ? 234  LEU A CD1 1 
ATOM   1754  C  CD2 . LEU A  1 217 ? 12.486  -31.380 34.118  1.00 22.89 ? 234  LEU A CD2 1 
ATOM   1755  N  N   . ILE A  1 218 ? 14.155  -35.568 32.142  1.00 22.20 ? 235  ILE A N   1 
ATOM   1756  C  CA  . ILE A  1 218 ? 15.519  -35.755 31.662  1.00 22.20 ? 235  ILE A CA  1 
ATOM   1757  C  C   . ILE A  1 218 ? 15.474  -36.413 30.281  1.00 21.95 ? 235  ILE A C   1 
ATOM   1758  O  O   . ILE A  1 218 ? 16.218  -36.015 29.388  1.00 22.07 ? 235  ILE A O   1 
ATOM   1759  C  CB  . ILE A  1 218 ? 16.380  -36.553 32.659  1.00 21.84 ? 235  ILE A CB  1 
ATOM   1760  C  CG1 . ILE A  1 218 ? 16.369  -35.947 34.068  1.00 23.20 ? 235  ILE A CG1 1 
ATOM   1761  C  CG2 . ILE A  1 218 ? 17.810  -36.713 32.136  1.00 21.91 ? 235  ILE A CG2 1 
ATOM   1762  C  CD1 . ILE A  1 218 ? 16.907  -34.529 34.147  1.00 24.06 ? 235  ILE A CD1 1 
ATOM   1763  N  N   . ASP A  1 219 ? 14.604  -37.418 30.102  1.00 22.15 ? 236  ASP A N   1 
ATOM   1764  C  CA  . ASP A  1 219 ? 14.439  -38.078 28.812  1.00 23.38 ? 236  ASP A CA  1 
ATOM   1765  C  C   . ASP A  1 219 ? 13.998  -37.078 27.745  1.00 22.65 ? 236  ASP A C   1 
ATOM   1766  O  O   . ASP A  1 219 ? 14.472  -37.128 26.617  1.00 22.23 ? 236  ASP A O   1 
ATOM   1767  C  CB  . ASP A  1 219 ? 13.411  -39.204 28.849  1.00 26.16 ? 236  ASP A CB  1 
ATOM   1768  C  CG  . ASP A  1 219 ? 13.863  -40.531 29.445  1.00 29.53 ? 236  ASP A CG  1 
ATOM   1769  O  OD1 . ASP A  1 219 ? 15.091  -40.720 29.626  1.00 32.06 ? 236  ASP A OD1 1 
ATOM   1770  O  OD2 . ASP A  1 219 ? 12.974  -41.365 29.741  1.00 31.64 ? 236  ASP A OD2 1 
ATOM   1771  N  N   . GLU A  1 220 ? 13.050  -36.205 28.098  1.00 22.55 ? 237  GLU A N   1 
ATOM   1772  C  CA  . GLU A  1 220 ? 12.500  -35.241 27.159  1.00 22.26 ? 237  GLU A CA  1 
ATOM   1773  C  C   . GLU A  1 220 ? 13.594  -34.273 26.708  1.00 21.35 ? 237  GLU A C   1 
ATOM   1774  O  O   . GLU A  1 220 ? 13.654  -33.902 25.541  1.00 20.12 ? 237  GLU A O   1 
ATOM   1775  C  CB  . GLU A  1 220 ? 11.335  -34.513 27.826  1.00 22.87 ? 237  GLU A CB  1 
ATOM   1776  C  CG  . GLU A  1 220 ? 10.541  -33.648 26.856  1.00 23.98 ? 237  GLU A CG  1 
ATOM   1777  C  CD  . GLU A  1 220 ? 9.383   -32.879 27.468  1.00 24.76 ? 237  GLU A CD  1 
ATOM   1778  O  OE1 . GLU A  1 220 ? 9.077   -33.048 28.671  1.00 25.10 ? 237  GLU A OE1 1 
ATOM   1779  O  OE2 . GLU A  1 220 ? 8.785   -32.086 26.710  1.00 25.93 ? 237  GLU A OE2 1 
ATOM   1780  N  N   . PHE A  1 221 ? 14.451  -33.874 27.653  1.00 21.86 ? 238  PHE A N   1 
ATOM   1781  C  CA  . PHE A  1 221 ? 15.587  -33.009 27.376  1.00 21.86 ? 238  PHE A CA  1 
ATOM   1782  C  C   . PHE A  1 221 ? 16.550  -33.665 26.382  1.00 21.92 ? 238  PHE A C   1 
ATOM   1783  O  O   . PHE A  1 221 ? 16.946  -33.040 25.398  1.00 21.88 ? 238  PHE A O   1 
ATOM   1784  C  CB  . PHE A  1 221 ? 16.262  -32.659 28.706  1.00 22.31 ? 238  PHE A CB  1 
ATOM   1785  C  CG  . PHE A  1 221 ? 17.708  -32.209 28.568  1.00 22.89 ? 238  PHE A CG  1 
ATOM   1786  C  CD1 . PHE A  1 221 ? 18.016  -30.946 28.073  1.00 23.63 ? 238  PHE A CD1 1 
ATOM   1787  C  CD2 . PHE A  1 221 ? 18.752  -33.049 28.934  1.00 23.64 ? 238  PHE A CD2 1 
ATOM   1788  C  CE1 . PHE A  1 221 ? 19.336  -30.548 27.936  1.00 22.97 ? 238  PHE A CE1 1 
ATOM   1789  C  CE2 . PHE A  1 221 ? 20.070  -32.640 28.795  1.00 23.89 ? 238  PHE A CE2 1 
ATOM   1790  C  CZ  . PHE A  1 221 ? 20.354  -31.391 28.299  1.00 23.23 ? 238  PHE A CZ  1 
ATOM   1791  N  N   . MET A  1 222 ? 16.952  -34.914 26.645  1.00 21.62 ? 239  MET A N   1 
ATOM   1792  C  CA  . MET A  1 222 ? 17.912  -35.591 25.788  1.00 21.85 ? 239  MET A CA  1 
ATOM   1793  C  C   . MET A  1 222 ? 17.366  -35.660 24.360  1.00 22.39 ? 239  MET A C   1 
ATOM   1794  O  O   . MET A  1 222 ? 18.075  -35.362 23.398  1.00 22.99 ? 239  MET A O   1 
ATOM   1795  C  CB  . MET A  1 222 ? 18.233  -37.002 26.304  1.00 21.95 ? 239  MET A CB  1 
ATOM   1796  C  CG  . MET A  1 222 ? 18.878  -37.033 27.683  1.00 21.93 ? 239  MET A CG  1 
ATOM   1797  S  SD  . MET A  1 222 ? 20.505  -36.257 27.774  1.00 22.05 ? 239  MET A SD  1 
ATOM   1798  C  CE  . MET A  1 222 ? 21.558  -37.571 27.136  1.00 21.57 ? 239  MET A CE  1 
ATOM   1799  N  N   . LYS A  1 223 ? 16.083  -36.010 24.232  1.00 22.76 ? 240  LYS A N   1 
ATOM   1800  C  CA  . LYS A  1 223 ? 15.451  -36.150 22.930  1.00 24.22 ? 240  LYS A CA  1 
ATOM   1801  C  C   . LYS A  1 223 ? 15.364  -34.795 22.226  1.00 22.26 ? 240  LYS A C   1 
ATOM   1802  O  O   . LYS A  1 223 ? 15.637  -34.717 21.035  1.00 21.41 ? 240  LYS A O   1 
ATOM   1803  C  CB  . LYS A  1 223 ? 14.081  -36.827 23.077  1.00 26.81 ? 240  LYS A CB  1 
ATOM   1804  C  CG  . LYS A  1 223 ? 13.231  -36.836 21.815  1.00 29.72 ? 240  LYS A CG  1 
ATOM   1805  C  CD  . LYS A  1 223 ? 11.992  -37.723 21.884  1.00 32.69 ? 240  LYS A CD  1 
ATOM   1806  C  CE  . LYS A  1 223 ? 10.910  -37.258 20.955  1.00 34.53 ? 240  LYS A CE  1 
ATOM   1807  N  NZ  . LYS A  1 223 ? 11.365  -37.179 19.566  1.00 35.46 ? 240  LYS A NZ  1 
ATOM   1808  N  N   . ALA A  1 224 ? 15.020  -33.734 22.971  1.00 22.46 ? 241  ALA A N   1 
ATOM   1809  C  CA  . ALA A  1 224 ? 14.815  -32.414 22.392  1.00 22.04 ? 241  ALA A CA  1 
ATOM   1810  C  C   . ALA A  1 224 ? 16.129  -31.856 21.844  1.00 22.47 ? 241  ALA A C   1 
ATOM   1811  O  O   . ALA A  1 224 ? 16.159  -31.347 20.728  1.00 22.07 ? 241  ALA A O   1 
ATOM   1812  C  CB  . ALA A  1 224 ? 14.213  -31.485 23.416  1.00 21.94 ? 241  ALA A CB  1 
ATOM   1813  N  N   . ILE A  1 225 ? 17.210  -31.983 22.628  1.00 21.96 ? 242  ILE A N   1 
ATOM   1814  C  CA  . ILE A  1 225 ? 18.530  -31.525 22.218  1.00 22.04 ? 242  ILE A CA  1 
ATOM   1815  C  C   . ILE A  1 225 ? 18.956  -32.220 20.927  1.00 21.94 ? 242  ILE A C   1 
ATOM   1816  O  O   . ILE A  1 225 ? 19.417  -31.562 19.992  1.00 21.01 ? 242  ILE A O   1 
ATOM   1817  C  CB  . ILE A  1 225 ? 19.569  -31.745 23.338  1.00 22.12 ? 242  ILE A CB  1 
ATOM   1818  C  CG1 . ILE A  1 225 ? 19.327  -30.817 24.531  1.00 22.91 ? 242  ILE A CG1 1 
ATOM   1819  C  CG2 . ILE A  1 225 ? 20.997  -31.609 22.805  1.00 21.62 ? 242  ILE A CG2 1 
ATOM   1820  C  CD1 . ILE A  1 225 ? 19.627  -29.354 24.263  1.00 23.84 ? 242  ILE A CD1 1 
ATOM   1821  N  N   . THR A  1 226 ? 18.849  -33.554 20.893  1.00 21.96 ? 243  THR A N   1 
ATOM   1822  C  CA  . THR A  1 226 ? 19.365  -34.321 19.768  1.00 22.26 ? 243  THR A CA  1 
ATOM   1823  C  C   . THR A  1 226 ? 18.430  -34.179 18.564  1.00 22.73 ? 243  THR A C   1 
ATOM   1824  O  O   . THR A  1 226 ? 18.883  -34.265 17.430  1.00 22.91 ? 243  THR A O   1 
ATOM   1825  C  CB  . THR A  1 226 ? 19.588  -35.786 20.154  1.00 23.27 ? 243  THR A CB  1 
ATOM   1826  O  OG1 . THR A  1 226 ? 18.389  -36.302 20.731  1.00 24.07 ? 243  THR A OG1 1 
ATOM   1827  C  CG2 . THR A  1 226 ? 20.731  -35.951 21.137  1.00 23.36 ? 243  THR A CG2 1 
ATOM   1828  N  N   . ASP A  1 227 ? 17.133  -33.964 18.806  1.00 23.57 ? 244  ASP A N   1 
ATOM   1829  C  CA  . ASP A  1 227 ? 16.189  -33.694 17.731  1.00 24.63 ? 244  ASP A CA  1 
ATOM   1830  C  C   . ASP A  1 227 ? 16.566  -32.407 16.994  1.00 23.92 ? 244  ASP A C   1 
ATOM   1831  O  O   . ASP A  1 227 ? 16.497  -32.358 15.769  1.00 23.17 ? 244  ASP A O   1 
ATOM   1832  C  CB  . ASP A  1 227 ? 14.752  -33.637 18.234  1.00 26.11 ? 244  ASP A CB  1 
ATOM   1833  C  CG  . ASP A  1 227 ? 14.061  -34.982 18.429  1.00 27.12 ? 244  ASP A CG  1 
ATOM   1834  O  OD1 . ASP A  1 227 ? 14.653  -36.022 18.052  1.00 26.83 ? 244  ASP A OD1 1 
ATOM   1835  O  OD2 . ASP A  1 227 ? 12.932  -34.982 18.962  1.00 28.01 ? 244  ASP A OD2 1 
ATOM   1836  N  N   . ARG A  1 228 ? 16.964  -31.368 17.738  1.00 22.35 ? 245  ARG A N   1 
ATOM   1837  C  CA  . ARG A  1 228 ? 17.320  -30.100 17.128  1.00 22.29 ? 245  ARG A CA  1 
ATOM   1838  C  C   . ARG A  1 228 ? 18.715  -30.157 16.500  1.00 21.87 ? 245  ARG A C   1 
ATOM   1839  O  O   . ARG A  1 228 ? 18.894  -29.697 15.376  1.00 22.32 ? 245  ARG A O   1 
ATOM   1840  C  CB  . ARG A  1 228 ? 17.222  -28.919 18.100  1.00 22.22 ? 245  ARG A CB  1 
ATOM   1841  C  CG  . ARG A  1 228 ? 17.548  -27.623 17.373  1.00 23.37 ? 245  ARG A CG  1 
ATOM   1842  C  CD  . ARG A  1 228 ? 17.300  -26.347 18.160  1.00 23.94 ? 245  ARG A CD  1 
ATOM   1843  N  NE  . ARG A  1 228 ? 17.694  -25.208 17.324  1.00 23.77 ? 245  ARG A NE  1 
ATOM   1844  C  CZ  . ARG A  1 228 ? 17.707  -23.934 17.680  1.00 24.48 ? 245  ARG A CZ  1 
ATOM   1845  N  NH1 . ARG A  1 228 ? 17.381  -23.575 18.908  1.00 25.15 ? 245  ARG A NH1 1 
ATOM   1846  N  NH2 . ARG A  1 228 ? 18.055  -23.013 16.795  1.00 25.37 ? 245  ARG A NH2 1 
ATOM   1847  N  N   . TYR A  1 229 ? 19.700  -30.705 17.220  1.00 20.81 ? 246  TYR A N   1 
ATOM   1848  C  CA  . TYR A  1 229 ? 21.102  -30.474 16.897  1.00 21.22 ? 246  TYR A CA  1 
ATOM   1849  C  C   . TYR A  1 229 ? 21.788  -31.718 16.333  1.00 22.13 ? 246  TYR A C   1 
ATOM   1850  O  O   . TYR A  1 229 ? 22.881  -31.615 15.773  1.00 22.63 ? 246  TYR A O   1 
ATOM   1851  C  CB  . TYR A  1 229 ? 21.777  -29.965 18.175  1.00 21.59 ? 246  TYR A CB  1 
ATOM   1852  C  CG  . TYR A  1 229 ? 21.374  -28.551 18.580  1.00 20.67 ? 246  TYR A CG  1 
ATOM   1853  C  CD1 . TYR A  1 229 ? 21.457  -27.487 17.686  1.00 21.01 ? 246  TYR A CD1 1 
ATOM   1854  C  CD2 . TYR A  1 229 ? 20.908  -28.280 19.860  1.00 21.39 ? 246  TYR A CD2 1 
ATOM   1855  C  CE1 . TYR A  1 229 ? 21.095  -26.202 18.061  1.00 21.21 ? 246  TYR A CE1 1 
ATOM   1856  C  CE2 . TYR A  1 229 ? 20.532  -27.002 20.243  1.00 21.72 ? 246  TYR A CE2 1 
ATOM   1857  C  CZ  . TYR A  1 229 ? 20.625  -25.958 19.341  1.00 21.92 ? 246  TYR A CZ  1 
ATOM   1858  O  OH  . TYR A  1 229 ? 20.268  -24.697 19.740  1.00 22.60 ? 246  TYR A OH  1 
ATOM   1859  N  N   . GLY A  1 230 ? 21.162  -32.889 16.488  1.00 21.78 ? 247  GLY A N   1 
ATOM   1860  C  CA  . GLY A  1 230 ? 21.710  -34.124 15.950  1.00 23.14 ? 247  GLY A CA  1 
ATOM   1861  C  C   . GLY A  1 230 ? 22.075  -35.109 17.059  1.00 23.60 ? 247  GLY A C   1 
ATOM   1862  O  O   . GLY A  1 230 ? 22.393  -34.713 18.177  1.00 22.04 ? 247  GLY A O   1 
ATOM   1863  N  N   . ARG A  1 231 ? 22.049  -36.399 16.713  1.00 25.27 ? 248  ARG A N   1 
ATOM   1864  C  CA  . ARG A  1 231 ? 22.296  -37.469 17.668  1.00 28.52 ? 248  ARG A CA  1 
ATOM   1865  C  C   . ARG A  1 231 ? 23.747  -37.488 18.145  1.00 25.76 ? 248  ARG A C   1 
ATOM   1866  O  O   . ARG A  1 231 ? 24.032  -38.095 19.171  1.00 27.44 ? 248  ARG A O   1 
ATOM   1867  C  CB  . ARG A  1 231 ? 21.949  -38.835 17.062  1.00 34.06 ? 248  ARG A CB  1 
ATOM   1868  C  CG  . ARG A  1 231 ? 20.453  -39.095 16.957  1.00 39.35 ? 248  ARG A CG  1 
ATOM   1869  C  CD  . ARG A  1 231 ? 20.138  -40.557 16.663  1.00 45.07 ? 248  ARG A CD  1 
ATOM   1870  N  NE  . ARG A  1 231 ? 20.158  -41.406 17.863  1.00 50.04 ? 248  ARG A NE  1 
ATOM   1871  C  CZ  . ARG A  1 231 ? 19.261  -41.397 18.853  1.00 51.44 ? 248  ARG A CZ  1 
ATOM   1872  N  NH1 . ARG A  1 231 ? 19.356  -42.277 19.838  1.00 51.56 ? 248  ARG A NH1 1 
ATOM   1873  N  NH2 . ARG A  1 231 ? 18.256  -40.534 18.847  1.00 51.49 ? 248  ARG A NH2 1 
ATOM   1874  N  N   . ASN A  1 232 ? 24.670  -36.849 17.418  1.00 24.10 ? 249  ASN A N   1 
ATOM   1875  C  CA  . ASN A  1 232 ? 26.068  -36.883 17.820  1.00 25.05 ? 249  ASN A CA  1 
ATOM   1876  C  C   . ASN A  1 232 ? 26.413  -35.719 18.756  1.00 23.43 ? 249  ASN A C   1 
ATOM   1877  O  O   . ASN A  1 232 ? 27.571  -35.595 19.150  1.00 21.75 ? 249  ASN A O   1 
ATOM   1878  C  CB  . ASN A  1 232 ? 27.006  -36.992 16.620  1.00 25.88 ? 249  ASN A CB  1 
ATOM   1879  C  CG  . ASN A  1 232 ? 27.104  -35.734 15.791  1.00 27.92 ? 249  ASN A CG  1 
ATOM   1880  O  OD1 . ASN A  1 232 ? 26.761  -34.640 16.250  1.00 29.89 ? 249  ASN A OD1 1 
ATOM   1881  N  ND2 . ASN A  1 232 ? 27.600  -35.867 14.569  1.00 29.41 ? 249  ASN A ND2 1 
ATOM   1882  N  N   . THR A  1 233 ? 25.416  -34.894 19.126  1.00 22.15 ? 250  THR A N   1 
ATOM   1883  C  CA  . THR A  1 233 ? 25.637  -33.744 19.994  1.00 21.23 ? 250  THR A CA  1 
ATOM   1884  C  C   . THR A  1 233 ? 26.156  -34.230 21.349  1.00 20.27 ? 250  THR A C   1 
ATOM   1885  O  O   . THR A  1 233 ? 25.519  -35.048 22.009  1.00 19.78 ? 250  THR A O   1 
ATOM   1886  C  CB  . THR A  1 233 ? 24.342  -32.944 20.158  1.00 21.47 ? 250  THR A CB  1 
ATOM   1887  O  OG1 . THR A  1 233 ? 23.836  -32.603 18.865  1.00 21.20 ? 250  THR A OG1 1 
ATOM   1888  C  CG2 . THR A  1 233 ? 24.552  -31.682 20.974  1.00 20.69 ? 250  THR A CG2 1 
ATOM   1889  N  N   . LEU A  1 234 ? 27.308  -33.699 21.766  1.00 19.77 ? 251  LEU A N   1 
ATOM   1890  C  CA  . LEU A  1 234 ? 27.941  -34.092 23.015  1.00 20.55 ? 251  LEU A CA  1 
ATOM   1891  C  C   . LEU A  1 234 ? 27.163  -33.485 24.180  1.00 19.97 ? 251  LEU A C   1 
ATOM   1892  O  O   . LEU A  1 234 ? 26.982  -32.269 24.225  1.00 19.43 ? 251  LEU A O   1 
ATOM   1893  C  CB  . LEU A  1 234 ? 29.402  -33.642 23.005  1.00 20.88 ? 251  LEU A CB  1 
ATOM   1894  C  CG  . LEU A  1 234 ? 30.204  -33.875 24.291  1.00 21.65 ? 251  LEU A CG  1 
ATOM   1895  C  CD1 . LEU A  1 234 ? 30.184  -35.329 24.723  1.00 21.89 ? 251  LEU A CD1 1 
ATOM   1896  C  CD2 . LEU A  1 234 ? 31.639  -33.421 24.098  1.00 22.14 ? 251  LEU A CD2 1 
ATOM   1897  N  N   . ILE A  1 235 ? 26.696  -34.348 25.096  1.00 19.05 ? 252  ILE A N   1 
ATOM   1898  C  CA  . ILE A  1 235 ? 25.948  -33.924 26.272  1.00 19.09 ? 252  ILE A CA  1 
ATOM   1899  C  C   . ILE A  1 235 ? 26.664  -34.430 27.522  1.00 18.84 ? 252  ILE A C   1 
ATOM   1900  O  O   . ILE A  1 235 ? 26.705  -35.634 27.775  1.00 18.06 ? 252  ILE A O   1 
ATOM   1901  C  CB  . ILE A  1 235 ? 24.489  -34.420 26.231  1.00 19.35 ? 252  ILE A CB  1 
ATOM   1902  C  CG1 . ILE A  1 235 ? 23.757  -33.972 24.959  1.00 19.65 ? 252  ILE A CG1 1 
ATOM   1903  C  CG2 . ILE A  1 235 ? 23.746  -33.975 27.490  1.00 19.90 ? 252  ILE A CG2 1 
ATOM   1904  C  CD1 . ILE A  1 235 ? 22.480  -34.739 24.675  1.00 19.88 ? 252  ILE A CD1 1 
ATOM   1905  N  N   . GLN A  1 236 ? 27.205  -33.492 28.307  1.00 19.22 ? 253  GLN A N   1 
ATOM   1906  C  CA  . GLN A  1 236 ? 27.972  -33.828 29.495  1.00 20.11 ? 253  GLN A CA  1 
ATOM   1907  C  C   . GLN A  1 236 ? 27.191  -33.443 30.746  1.00 20.42 ? 253  GLN A C   1 
ATOM   1908  O  O   . GLN A  1 236 ? 26.793  -32.288 30.899  1.00 19.37 ? 253  GLN A O   1 
ATOM   1909  C  CB  . GLN A  1 236 ? 29.316  -33.112 29.513  1.00 20.67 ? 253  GLN A CB  1 
ATOM   1910  C  CG  . GLN A  1 236 ? 30.217  -33.576 30.651  1.00 21.99 ? 253  GLN A CG  1 
ATOM   1911  C  CD  . GLN A  1 236 ? 30.811  -32.433 31.439  1.00 22.42 ? 253  GLN A CD  1 
ATOM   1912  O  OE1 . GLN A  1 236 ? 31.575  -31.618 30.916  1.00 22.74 ? 253  GLN A OE1 1 
ATOM   1913  N  NE2 . GLN A  1 236 ? 30.462  -32.367 32.715  1.00 23.79 ? 253  GLN A NE2 1 
ATOM   1914  N  N   . PHE A  1 237 ? 27.002  -34.425 31.640  1.00 20.13 ? 254  PHE A N   1 
ATOM   1915  C  CA  . PHE A  1 237 ? 26.294  -34.232 32.894  1.00 20.61 ? 254  PHE A CA  1 
ATOM   1916  C  C   . PHE A  1 237 ? 27.292  -33.797 33.965  1.00 20.67 ? 254  PHE A C   1 
ATOM   1917  O  O   . PHE A  1 237 ? 28.391  -34.339 34.047  1.00 20.95 ? 254  PHE A O   1 
ATOM   1918  C  CB  . PHE A  1 237 ? 25.568  -35.496 33.374  1.00 21.29 ? 254  PHE A CB  1 
ATOM   1919  C  CG  . PHE A  1 237 ? 24.282  -35.860 32.645  1.00 21.62 ? 254  PHE A CG  1 
ATOM   1920  C  CD1 . PHE A  1 237 ? 24.231  -35.922 31.256  1.00 22.61 ? 254  PHE A CD1 1 
ATOM   1921  C  CD2 . PHE A  1 237 ? 23.119  -36.135 33.357  1.00 21.90 ? 254  PHE A CD2 1 
ATOM   1922  C  CE1 . PHE A  1 237 ? 23.054  -36.255 30.603  1.00 22.58 ? 254  PHE A CE1 1 
ATOM   1923  C  CE2 . PHE A  1 237 ? 21.946  -36.473 32.700  1.00 21.93 ? 254  PHE A CE2 1 
ATOM   1924  C  CZ  . PHE A  1 237 ? 21.915  -36.530 31.324  1.00 22.08 ? 254  PHE A CZ  1 
ATOM   1925  N  N   . GLU A  1 238 ? 26.842  -32.826 34.761  1.00 21.91 ? 255  GLU A N   1 
ATOM   1926  C  CA  . GLU A  1 238 ? 27.726  -32.240 35.789  1.00 23.27 ? 255  GLU A CA  1 
ATOM   1927  C  C   . GLU A  1 238 ? 26.976  -31.914 37.081  1.00 22.72 ? 255  GLU A C   1 
ATOM   1928  O  O   . GLU A  1 238 ? 25.898  -31.315 37.004  1.00 21.18 ? 255  GLU A O   1 
ATOM   1929  C  CB  . GLU A  1 238 ? 28.311  -30.925 35.278  1.00 26.33 ? 255  GLU A CB  1 
ATOM   1930  C  CG  . GLU A  1 238 ? 29.293  -30.276 36.248  1.00 28.24 ? 255  GLU A CG  1 
ATOM   1931  C  CD  . GLU A  1 238 ? 30.726  -30.739 36.072  1.00 30.49 ? 255  GLU A CD  1 
ATOM   1932  O  OE1 . GLU A  1 238 ? 31.012  -31.426 35.075  1.00 32.28 ? 255  GLU A OE1 1 
ATOM   1933  O  OE2 . GLU A  1 238 ? 31.557  -30.412 36.938  1.00 33.88 ? 255  GLU A OE2 1 
ATOM   1934  N  N   . ASP A  1 239 ? 27.500  -32.366 38.207  1.00 22.18 ? 256  ASP A N   1 
ATOM   1935  C  CA  . ASP A  1 239 ? 27.022  -31.994 39.537  1.00 22.67 ? 256  ASP A CA  1 
ATOM   1936  C  C   . ASP A  1 239 ? 25.590  -32.471 39.798  1.00 21.54 ? 256  ASP A C   1 
ATOM   1937  O  O   . ASP A  1 239 ? 24.859  -31.858 40.574  1.00 22.38 ? 256  ASP A O   1 
ATOM   1938  C  CB  . ASP A  1 239 ? 27.237  -30.515 39.823  1.00 24.21 ? 256  ASP A CB  1 
ATOM   1939  C  CG  . ASP A  1 239 ? 28.645  -30.114 40.246  1.00 25.95 ? 256  ASP A CG  1 
ATOM   1940  O  OD1 . ASP A  1 239 ? 29.473  -31.015 40.531  1.00 27.93 ? 256  ASP A OD1 1 
ATOM   1941  O  OD2 . ASP A  1 239 ? 28.910  -28.898 40.298  1.00 28.06 ? 256  ASP A OD2 1 
ATOM   1942  N  N   . PHE A  1 240 ? 25.211  -33.599 39.193  1.00 21.30 ? 257  PHE A N   1 
ATOM   1943  C  CA  . PHE A  1 240 ? 24.038  -34.347 39.622  1.00 20.97 ? 257  PHE A CA  1 
ATOM   1944  C  C   . PHE A  1 240 ? 24.363  -35.030 40.949  1.00 21.43 ? 257  PHE A C   1 
ATOM   1945  O  O   . PHE A  1 240 ? 25.529  -35.172 41.315  1.00 20.42 ? 257  PHE A O   1 
ATOM   1946  C  CB  . PHE A  1 240 ? 23.630  -35.351 38.536  1.00 21.07 ? 257  PHE A CB  1 
ATOM   1947  C  CG  . PHE A  1 240 ? 22.801  -34.754 37.406  1.00 21.10 ? 257  PHE A CG  1 
ATOM   1948  C  CD1 . PHE A  1 240 ? 23.387  -33.954 36.429  1.00 21.58 ? 257  PHE A CD1 1 
ATOM   1949  C  CD2 . PHE A  1 240 ? 21.436  -34.997 37.318  1.00 21.16 ? 257  PHE A CD2 1 
ATOM   1950  C  CE1 . PHE A  1 240 ? 22.627  -33.415 35.403  1.00 21.21 ? 257  PHE A CE1 1 
ATOM   1951  C  CE2 . PHE A  1 240 ? 20.682  -34.452 36.289  1.00 22.00 ? 257  PHE A CE2 1 
ATOM   1952  C  CZ  . PHE A  1 240 ? 21.277  -33.658 35.337  1.00 21.40 ? 257  PHE A CZ  1 
ATOM   1953  N  N   . GLY A  1 241 ? 23.324  -35.443 41.681  1.00 20.56 ? 258  GLY A N   1 
ATOM   1954  C  CA  . GLY A  1 241 ? 23.515  -36.357 42.792  1.00 21.01 ? 258  GLY A CA  1 
ATOM   1955  C  C   . GLY A  1 241 ? 24.185  -37.642 42.315  1.00 20.71 ? 258  GLY A C   1 
ATOM   1956  O  O   . GLY A  1 241 ? 23.992  -38.051 41.173  1.00 20.29 ? 258  GLY A O   1 
ATOM   1957  N  N   . ASN A  1 242 ? 24.959  -38.270 43.208  1.00 22.29 ? 259  ASN A N   1 
ATOM   1958  C  CA  . ASN A  1 242 ? 25.829  -39.384 42.849  1.00 23.75 ? 259  ASN A CA  1 
ATOM   1959  C  C   . ASN A  1 242 ? 25.066  -40.495 42.133  1.00 23.59 ? 259  ASN A C   1 
ATOM   1960  O  O   . ASN A  1 242 ? 25.513  -40.992 41.102  1.00 22.30 ? 259  ASN A O   1 
ATOM   1961  C  CB  . ASN A  1 242 ? 26.538  -39.966 44.069  1.00 24.75 ? 259  ASN A CB  1 
ATOM   1962  C  CG  . ASN A  1 242 ? 27.829  -39.247 44.372  1.00 26.65 ? 259  ASN A CG  1 
ATOM   1963  O  OD1 . ASN A  1 242 ? 28.149  -38.242 43.726  1.00 28.41 ? 259  ASN A OD1 1 
ATOM   1964  N  ND2 . ASN A  1 242 ? 28.581  -39.746 45.342  1.00 25.62 ? 259  ASN A ND2 1 
ATOM   1965  N  N   . HIS A  1 243 ? 23.932  -40.907 42.702  1.00 23.96 ? 260  HIS A N   1 
ATOM   1966  C  CA  . HIS A  1 243 ? 23.213  -42.055 42.177  1.00 24.51 ? 260  HIS A CA  1 
ATOM   1967  C  C   . HIS A  1 243 ? 22.530  -41.700 40.860  1.00 22.58 ? 260  HIS A C   1 
ATOM   1968  O  O   . HIS A  1 243 ? 22.521  -42.510 39.940  1.00 21.97 ? 260  HIS A O   1 
ATOM   1969  C  CB  . HIS A  1 243 ? 22.297  -42.638 43.257  1.00 26.68 ? 260  HIS A CB  1 
ATOM   1970  C  CG  . HIS A  1 243 ? 23.061  -43.277 44.372  1.00 28.75 ? 260  HIS A CG  1 
ATOM   1971  N  ND1 . HIS A  1 243 ? 22.480  -43.652 45.563  1.00 31.08 ? 260  HIS A ND1 1 
ATOM   1972  C  CD2 . HIS A  1 243 ? 24.354  -43.636 44.458  1.00 29.47 ? 260  HIS A CD2 1 
ATOM   1973  C  CE1 . HIS A  1 243 ? 23.403  -44.202 46.342  1.00 30.91 ? 260  HIS A CE1 1 
ATOM   1974  N  NE2 . HIS A  1 243 ? 24.548  -44.206 45.688  1.00 31.54 ? 260  HIS A NE2 1 
ATOM   1975  N  N   . ASN A  1 244 ? 21.970  -40.490 40.768  1.00 22.70 ? 261  ASN A N   1 
ATOM   1976  C  CA  . ASN A  1 244 ? 21.385  -40.012 39.526  1.00 22.07 ? 261  ASN A CA  1 
ATOM   1977  C  C   . ASN A  1 244 ? 22.457  -39.978 38.434  1.00 20.87 ? 261  ASN A C   1 
ATOM   1978  O  O   . ASN A  1 244 ? 22.220  -40.423 37.312  1.00 21.27 ? 261  ASN A O   1 
ATOM   1979  C  CB  . ASN A  1 244 ? 20.723  -38.647 39.701  1.00 22.63 ? 261  ASN A CB  1 
ATOM   1980  C  CG  . ASN A  1 244 ? 19.348  -38.705 40.333  1.00 23.82 ? 261  ASN A CG  1 
ATOM   1981  O  OD1 . ASN A  1 244 ? 18.732  -39.770 40.424  1.00 24.94 ? 261  ASN A OD1 1 
ATOM   1982  N  ND2 . ASN A  1 244 ? 18.831  -37.559 40.751  1.00 24.58 ? 261  ASN A ND2 1 
ATOM   1983  N  N   . ALA A  1 245 ? 23.633  -39.432 38.760  1.00 20.14 ? 262  ALA A N   1 
ATOM   1984  C  CA  . ALA A  1 245 ? 24.731  -39.348 37.803  1.00 20.12 ? 262  ALA A CA  1 
ATOM   1985  C  C   . ALA A  1 245 ? 25.060  -40.733 37.242  1.00 19.95 ? 262  ALA A C   1 
ATOM   1986  O  O   . ALA A  1 245 ? 25.162  -40.909 36.026  1.00 18.91 ? 262  ALA A O   1 
ATOM   1987  C  CB  . ALA A  1 245 ? 25.940  -38.710 38.452  1.00 20.32 ? 262  ALA A CB  1 
ATOM   1988  N  N   . PHE A  1 246 ? 25.206  -41.716 38.138  1.00 19.88 ? 263  PHE A N   1 
ATOM   1989  C  CA  . PHE A  1 246 ? 25.600  -43.059 37.738  1.00 20.26 ? 263  PHE A CA  1 
ATOM   1990  C  C   . PHE A  1 246 ? 24.531  -43.688 36.847  1.00 19.55 ? 263  PHE A C   1 
ATOM   1991  O  O   . PHE A  1 246 ? 24.852  -44.241 35.798  1.00 19.22 ? 263  PHE A O   1 
ATOM   1992  C  CB  . PHE A  1 246 ? 25.871  -43.940 38.960  1.00 21.07 ? 263  PHE A CB  1 
ATOM   1993  C  CG  . PHE A  1 246 ? 26.387  -45.330 38.611  1.00 21.84 ? 263  PHE A CG  1 
ATOM   1994  C  CD1 . PHE A  1 246 ? 27.756  -45.571 38.487  1.00 22.49 ? 263  PHE A CD1 1 
ATOM   1995  C  CD2 . PHE A  1 246 ? 25.511  -46.393 38.423  1.00 22.72 ? 263  PHE A CD2 1 
ATOM   1996  C  CE1 . PHE A  1 246 ? 28.228  -46.839 38.175  1.00 22.90 ? 263  PHE A CE1 1 
ATOM   1997  C  CE2 . PHE A  1 246 ? 25.993  -47.660 38.109  1.00 23.45 ? 263  PHE A CE2 1 
ATOM   1998  C  CZ  . PHE A  1 246 ? 27.347  -47.878 37.985  1.00 22.91 ? 263  PHE A CZ  1 
ATOM   1999  N  N   . ARG A  1 247 ? 23.260  -43.605 37.260  1.00 19.99 ? 264  ARG A N   1 
ATOM   2000  C  CA  . ARG A  1 247 ? 22.205  -44.319 36.556  1.00 20.81 ? 264  ARG A CA  1 
ATOM   2001  C  C   . ARG A  1 247 ? 21.927  -43.673 35.197  1.00 20.47 ? 264  ARG A C   1 
ATOM   2002  O  O   . ARG A  1 247 ? 21.597  -44.376 34.248  1.00 19.67 ? 264  ARG A O   1 
ATOM   2003  C  CB  . ARG A  1 247 ? 20.935  -44.451 37.405  1.00 21.78 ? 264  ARG A CB  1 
ATOM   2004  C  CG  . ARG A  1 247 ? 20.127  -43.182 37.606  1.00 23.78 ? 264  ARG A CG  1 
ATOM   2005  C  CD  . ARG A  1 247 ? 19.025  -43.391 38.639  1.00 25.37 ? 264  ARG A CD  1 
ATOM   2006  N  NE  . ARG A  1 247 ? 18.214  -42.179 38.805  1.00 26.63 ? 264  ARG A NE  1 
ATOM   2007  C  CZ  . ARG A  1 247 ? 16.996  -41.983 38.304  1.00 27.19 ? 264  ARG A CZ  1 
ATOM   2008  N  NH1 . ARG A  1 247 ? 16.452  -42.864 37.478  1.00 29.19 ? 264  ARG A NH1 1 
ATOM   2009  N  NH2 . ARG A  1 247 ? 16.335  -40.885 38.617  1.00 26.58 ? 264  ARG A NH2 1 
ATOM   2010  N  N   . PHE A  1 248 ? 22.060  -42.343 35.098  1.00 19.94 ? 265  PHE A N   1 
ATOM   2011  C  CA  . PHE A  1 248 ? 21.837  -41.667 33.826  1.00 19.93 ? 265  PHE A CA  1 
ATOM   2012  C  C   . PHE A  1 248 ? 22.963  -41.986 32.841  1.00 19.48 ? 265  PHE A C   1 
ATOM   2013  O  O   . PHE A  1 248 ? 22.710  -42.157 31.647  1.00 19.48 ? 265  PHE A O   1 
ATOM   2014  C  CB  . PHE A  1 248 ? 21.643  -40.162 34.039  1.00 20.06 ? 265  PHE A CB  1 
ATOM   2015  C  CG  . PHE A  1 248 ? 20.299  -39.784 34.651  1.00 20.72 ? 265  PHE A CG  1 
ATOM   2016  C  CD1 . PHE A  1 248 ? 19.151  -40.527 34.386  1.00 22.03 ? 265  PHE A CD1 1 
ATOM   2017  C  CD2 . PHE A  1 248 ? 20.189  -38.686 35.497  1.00 21.25 ? 265  PHE A CD2 1 
ATOM   2018  C  CE1 . PHE A  1 248 ? 17.929  -40.179 34.950  1.00 21.67 ? 265  PHE A CE1 1 
ATOM   2019  C  CE2 . PHE A  1 248 ? 18.965  -38.336 36.053  1.00 21.77 ? 265  PHE A CE2 1 
ATOM   2020  C  CZ  . PHE A  1 248 ? 17.840  -39.086 35.781  1.00 22.02 ? 265  PHE A CZ  1 
ATOM   2021  N  N   . LEU A  1 249 ? 24.202  -42.075 33.334  1.00 19.46 ? 266  LEU A N   1 
ATOM   2022  C  CA  . LEU A  1 249 ? 25.316  -42.454 32.475  1.00 19.64 ? 266  LEU A CA  1 
ATOM   2023  C  C   . LEU A  1 249 ? 25.042  -43.838 31.886  1.00 19.38 ? 266  LEU A C   1 
ATOM   2024  O  O   . LEU A  1 249 ? 25.189  -44.050 30.685  1.00 19.03 ? 266  LEU A O   1 
ATOM   2025  C  CB  . LEU A  1 249 ? 26.637  -42.403 33.238  1.00 19.44 ? 266  LEU A CB  1 
ATOM   2026  C  CG  . LEU A  1 249 ? 27.883  -42.863 32.471  1.00 20.36 ? 266  LEU A CG  1 
ATOM   2027  C  CD1 . LEU A  1 249 ? 28.159  -41.975 31.266  1.00 20.39 ? 266  LEU A CD1 1 
ATOM   2028  C  CD2 . LEU A  1 249 ? 29.087  -42.907 33.391  1.00 20.21 ? 266  LEU A CD2 1 
ATOM   2029  N  N   . ARG A  1 250 ? 24.596  -44.769 32.736  1.00 20.06 ? 267  ARG A N   1 
ATOM   2030  C  CA  . ARG A  1 250 ? 24.280  -46.121 32.301  1.00 20.90 ? 267  ARG A CA  1 
ATOM   2031  C  C   . ARG A  1 250 ? 23.145  -46.094 31.278  1.00 20.76 ? 267  ARG A C   1 
ATOM   2032  O  O   . ARG A  1 250 ? 23.195  -46.786 30.266  1.00 20.85 ? 267  ARG A O   1 
ATOM   2033  C  CB  . ARG A  1 250 ? 23.923  -47.011 33.498  1.00 20.99 ? 267  ARG A CB  1 
ATOM   2034  C  CG  . ARG A  1 250 ? 23.681  -48.469 33.130  1.00 22.17 ? 267  ARG A CG  1 
ATOM   2035  C  CD  . ARG A  1 250 ? 23.338  -49.332 34.337  1.00 22.33 ? 267  ARG A CD  1 
ATOM   2036  N  NE  . ARG A  1 250 ? 22.155  -48.806 35.029  1.00 21.80 ? 267  ARG A NE  1 
ATOM   2037  C  CZ  . ARG A  1 250 ? 22.014  -48.680 36.344  1.00 22.79 ? 267  ARG A CZ  1 
ATOM   2038  N  NH1 . ARG A  1 250 ? 22.910  -49.196 37.167  1.00 22.94 ? 267  ARG A NH1 1 
ATOM   2039  N  NH2 . ARG A  1 250 ? 20.953  -48.062 36.838  1.00 23.54 ? 267  ARG A NH2 1 
ATOM   2040  N  N   . LYS A  1 251 ? 22.112  -45.294 31.551  1.00 21.60 ? 268  LYS A N   1 
ATOM   2041  C  CA  . LYS A  1 251 ? 20.919  -45.282 30.721  1.00 22.73 ? 268  LYS A CA  1 
ATOM   2042  C  C   . LYS A  1 251 ? 21.216  -44.718 29.327  1.00 21.92 ? 268  LYS A C   1 
ATOM   2043  O  O   . LYS A  1 251 ? 20.716  -45.260 28.343  1.00 21.51 ? 268  LYS A O   1 
ATOM   2044  C  CB  . LYS A  1 251 ? 19.799  -44.515 31.436  1.00 24.80 ? 268  LYS A CB  1 
ATOM   2045  C  CG  . LYS A  1 251 ? 18.464  -44.474 30.704  1.00 26.91 ? 268  LYS A CG  1 
ATOM   2046  C  CD  . LYS A  1 251 ? 17.359  -43.785 31.497  1.00 28.55 ? 268  LYS A CD  1 
ATOM   2047  C  CE  . LYS A  1 251 ? 16.044  -43.835 30.796  1.00 30.53 ? 268  LYS A CE  1 
ATOM   2048  N  NZ  . LYS A  1 251 ? 14.984  -43.210 31.593  1.00 32.66 ? 268  LYS A NZ  1 
ATOM   2049  N  N   . TYR A  1 252 ? 22.040  -43.661 29.233  1.00 21.19 ? 269  TYR A N   1 
ATOM   2050  C  CA  . TYR A  1 252 ? 22.137  -42.883 28.005  1.00 21.24 ? 269  TYR A CA  1 
ATOM   2051  C  C   . TYR A  1 252 ? 23.420  -43.121 27.200  1.00 22.36 ? 269  TYR A C   1 
ATOM   2052  O  O   . TYR A  1 252 ? 23.479  -42.720 26.038  1.00 22.14 ? 269  TYR A O   1 
ATOM   2053  C  CB  . TYR A  1 252 ? 22.032  -41.397 28.349  1.00 21.96 ? 269  TYR A CB  1 
ATOM   2054  C  CG  . TYR A  1 252 ? 20.690  -40.949 28.913  1.00 22.91 ? 269  TYR A CG  1 
ATOM   2055  C  CD1 . TYR A  1 252 ? 19.488  -41.296 28.310  1.00 24.13 ? 269  TYR A CD1 1 
ATOM   2056  C  CD2 . TYR A  1 252 ? 20.636  -40.177 30.067  1.00 24.55 ? 269  TYR A CD2 1 
ATOM   2057  C  CE1 . TYR A  1 252 ? 18.271  -40.886 28.836  1.00 25.19 ? 269  TYR A CE1 1 
ATOM   2058  C  CE2 . TYR A  1 252 ? 19.428  -39.762 30.602  1.00 25.11 ? 269  TYR A CE2 1 
ATOM   2059  C  CZ  . TYR A  1 252 ? 18.244  -40.117 29.987  1.00 25.41 ? 269  TYR A CZ  1 
ATOM   2060  O  OH  . TYR A  1 252 ? 17.076  -39.681 30.540  1.00 29.74 ? 269  TYR A OH  1 
ATOM   2061  N  N   . ARG A  1 253 ? 24.452  -43.759 27.767  1.00 22.28 ? 270  ARG A N   1 
ATOM   2062  C  CA  . ARG A  1 253 ? 25.758  -43.756 27.113  1.00 22.85 ? 270  ARG A CA  1 
ATOM   2063  C  C   . ARG A  1 253 ? 25.773  -44.513 25.780  1.00 23.41 ? 270  ARG A C   1 
ATOM   2064  O  O   . ARG A  1 253 ? 26.614  -44.216 24.936  1.00 22.81 ? 270  ARG A O   1 
ATOM   2065  C  CB  . ARG A  1 253 ? 26.881  -44.288 28.004  1.00 24.24 ? 270  ARG A CB  1 
ATOM   2066  C  CG  . ARG A  1 253 ? 26.747  -45.740 28.433  1.00 24.76 ? 270  ARG A CG  1 
ATOM   2067  C  CD  . ARG A  1 253 ? 27.836  -46.062 29.432  1.00 25.64 ? 270  ARG A CD  1 
ATOM   2068  N  NE  . ARG A  1 253 ? 29.173  -45.865 28.856  1.00 25.90 ? 270  ARG A NE  1 
ATOM   2069  C  CZ  . ARG A  1 253 ? 30.299  -45.779 29.549  1.00 25.79 ? 270  ARG A CZ  1 
ATOM   2070  N  NH1 . ARG A  1 253 ? 30.282  -45.905 30.865  1.00 26.25 ? 270  ARG A NH1 1 
ATOM   2071  N  NH2 . ARG A  1 253 ? 31.445  -45.577 28.917  1.00 25.90 ? 270  ARG A NH2 1 
ATOM   2072  N  N   . GLU A  1 254 ? 24.876  -45.494 25.585  1.00 24.23 ? 271  GLU A N   1 
ATOM   2073  C  CA  . GLU A  1 254 ? 24.842  -46.248 24.339  1.00 26.12 ? 271  GLU A CA  1 
ATOM   2074  C  C   . GLU A  1 254 ? 23.755  -45.715 23.406  1.00 25.04 ? 271  GLU A C   1 
ATOM   2075  O  O   . GLU A  1 254 ? 23.647  -46.171 22.271  1.00 24.28 ? 271  GLU A O   1 
ATOM   2076  C  CB  . GLU A  1 254 ? 24.643  -47.741 24.602  1.00 30.78 ? 271  GLU A CB  1 
ATOM   2077  C  CG  . GLU A  1 254 ? 25.883  -48.423 25.173  1.00 34.97 ? 271  GLU A CG  1 
ATOM   2078  C  CD  . GLU A  1 254 ? 25.742  -49.929 25.340  1.00 42.33 ? 271  GLU A CD  1 
ATOM   2079  O  OE1 . GLU A  1 254 ? 24.617  -50.456 25.185  1.00 44.40 ? 271  GLU A OE1 1 
ATOM   2080  O  OE2 . GLU A  1 254 ? 26.773  -50.583 25.619  1.00 48.70 ? 271  GLU A OE2 1 
ATOM   2081  N  N   . LYS A  1 255 ? 22.956  -44.753 23.884  1.00 24.69 ? 272  LYS A N   1 
ATOM   2082  C  CA  . LYS A  1 255 ? 21.879  -44.183 23.091  1.00 26.19 ? 272  LYS A CA  1 
ATOM   2083  C  C   . LYS A  1 255 ? 22.264  -42.791 22.589  1.00 24.00 ? 272  LYS A C   1 
ATOM   2084  O  O   . LYS A  1 255 ? 21.838  -42.385 21.516  1.00 23.46 ? 272  LYS A O   1 
ATOM   2085  C  CB  . LYS A  1 255 ? 20.593  -44.136 23.922  1.00 30.38 ? 272  LYS A CB  1 
ATOM   2086  C  CG  . LYS A  1 255 ? 19.395  -43.550 23.182  1.00 36.41 ? 272  LYS A CG  1 
ATOM   2087  C  CD  . LYS A  1 255 ? 18.079  -43.600 23.951  1.00 40.56 ? 272  LYS A CD  1 
ATOM   2088  C  CE  . LYS A  1 255 ? 16.933  -43.189 23.082  1.00 42.52 ? 272  LYS A CE  1 
ATOM   2089  N  NZ  . LYS A  1 255 ? 15.676  -43.215 23.832  1.00 45.35 ? 272  LYS A NZ  1 
ATOM   2090  N  N   . TYR A  1 256 ? 23.032  -42.044 23.389  1.00 21.43 ? 273  TYR A N   1 
ATOM   2091  C  CA  . TYR A  1 256 ? 23.428  -40.695 23.030  1.00 20.90 ? 273  TYR A CA  1 
ATOM   2092  C  C   . TYR A  1 256 ? 24.940  -40.558 23.164  1.00 19.54 ? 273  TYR A C   1 
ATOM   2093  O  O   . TYR A  1 256 ? 25.610  -41.482 23.615  1.00 20.75 ? 273  TYR A O   1 
ATOM   2094  C  CB  . TYR A  1 256 ? 22.702  -39.706 23.942  1.00 21.51 ? 273  TYR A CB  1 
ATOM   2095  C  CG  . TYR A  1 256 ? 21.187  -39.716 23.818  1.00 22.16 ? 273  TYR A CG  1 
ATOM   2096  C  CD1 . TYR A  1 256 ? 20.559  -39.139 22.724  1.00 23.53 ? 273  TYR A CD1 1 
ATOM   2097  C  CD2 . TYR A  1 256 ? 20.384  -40.280 24.801  1.00 23.13 ? 273  TYR A CD2 1 
ATOM   2098  C  CE1 . TYR A  1 256 ? 19.177  -39.130 22.602  1.00 24.30 ? 273  TYR A CE1 1 
ATOM   2099  C  CE2 . TYR A  1 256 ? 19.001  -40.274 24.695  1.00 23.93 ? 273  TYR A CE2 1 
ATOM   2100  C  CZ  . TYR A  1 256 ? 18.395  -39.698 23.592  1.00 24.89 ? 273  TYR A CZ  1 
ATOM   2101  O  OH  . TYR A  1 256 ? 17.031  -39.693 23.477  1.00 26.30 ? 273  TYR A OH  1 
ATOM   2102  N  N   . CYS A  1 257 ? 25.458  -39.390 22.771  1.00 18.89 ? 274  CYS A N   1 
ATOM   2103  C  CA  . CYS A  1 257 ? 26.868  -39.072 22.925  1.00 19.31 ? 274  CYS A CA  1 
ATOM   2104  C  C   . CYS A  1 257 ? 27.053  -38.342 24.252  1.00 18.76 ? 274  CYS A C   1 
ATOM   2105  O  O   . CYS A  1 257 ? 26.910  -37.125 24.311  1.00 19.10 ? 274  CYS A O   1 
ATOM   2106  C  CB  . CYS A  1 257 ? 27.364  -38.251 21.739  1.00 19.94 ? 274  CYS A CB  1 
ATOM   2107  S  SG  . CYS A  1 257 ? 29.143  -37.918 21.790  1.00 21.55 ? 274  CYS A SG  1 
ATOM   2108  N  N   . THR A  1 258 ? 27.339  -39.094 25.322  1.00 18.37 ? 275  THR A N   1 
ATOM   2109  C  CA  . THR A  1 258 ? 27.279  -38.537 26.660  1.00 18.47 ? 275  THR A CA  1 
ATOM   2110  C  C   . THR A  1 258 ? 28.380  -39.117 27.540  1.00 19.13 ? 275  THR A C   1 
ATOM   2111  O  O   . THR A  1 258 ? 28.809  -40.260 27.381  1.00 18.07 ? 275  THR A O   1 
ATOM   2112  C  CB  . THR A  1 258 ? 25.887  -38.769 27.251  1.00 19.71 ? 275  THR A CB  1 
ATOM   2113  O  OG1 . THR A  1 258 ? 25.859  -38.070 28.496  1.00 20.05 ? 275  THR A OG1 1 
ATOM   2114  C  CG2 . THR A  1 258 ? 25.576  -40.239 27.454  1.00 20.13 ? 275  THR A CG2 1 
ATOM   2115  N  N   . PHE A  1 259 ? 28.834  -38.283 28.475  1.00 19.24 ? 276  PHE A N   1 
ATOM   2116  C  CA  . PHE A  1 259 ? 29.758  -38.709 29.506  1.00 19.92 ? 276  PHE A CA  1 
ATOM   2117  C  C   . PHE A  1 259 ? 29.444  -37.889 30.746  1.00 19.85 ? 276  PHE A C   1 
ATOM   2118  O  O   . PHE A  1 259 ? 28.703  -36.906 30.676  1.00 19.27 ? 276  PHE A O   1 
ATOM   2119  C  CB  . PHE A  1 259 ? 31.218  -38.605 29.046  1.00 20.75 ? 276  PHE A CB  1 
ATOM   2120  C  CG  . PHE A  1 259 ? 31.872  -37.229 29.052  1.00 22.48 ? 276  PHE A CG  1 
ATOM   2121  C  CD1 . PHE A  1 259 ? 31.696  -36.349 27.989  1.00 24.05 ? 276  PHE A CD1 1 
ATOM   2122  C  CD2 . PHE A  1 259 ? 32.718  -36.842 30.088  1.00 22.89 ? 276  PHE A CD2 1 
ATOM   2123  C  CE1 . PHE A  1 259 ? 32.316  -35.107 27.980  1.00 24.21 ? 276  PHE A CE1 1 
ATOM   2124  C  CE2 . PHE A  1 259 ? 33.337  -35.598 30.077  1.00 23.54 ? 276  PHE A CE2 1 
ATOM   2125  C  CZ  . PHE A  1 259 ? 33.134  -34.733 29.025  1.00 23.81 ? 276  PHE A CZ  1 
ATOM   2126  N  N   . ASN A  1 260 ? 29.989  -38.339 31.873  1.00 19.69 ? 277  ASN A N   1 
ATOM   2127  C  CA  . ASN A  1 260 ? 29.871  -37.626 33.129  1.00 20.92 ? 277  ASN A CA  1 
ATOM   2128  C  C   . ASN A  1 260 ? 31.282  -37.352 33.638  1.00 21.53 ? 277  ASN A C   1 
ATOM   2129  O  O   . ASN A  1 260 ? 32.024  -38.285 33.935  1.00 21.13 ? 277  ASN A O   1 
ATOM   2130  C  CB  . ASN A  1 260 ? 29.032  -38.419 34.121  1.00 21.10 ? 277  ASN A CB  1 
ATOM   2131  C  CG  . ASN A  1 260 ? 28.819  -37.651 35.403  1.00 22.00 ? 277  ASN A CG  1 
ATOM   2132  O  OD1 . ASN A  1 260 ? 29.788  -37.360 36.109  1.00 22.49 ? 277  ASN A OD1 1 
ATOM   2133  N  ND2 . ASN A  1 260 ? 27.577  -37.308 35.715  1.00 22.48 ? 277  ASN A ND2 1 
ATOM   2134  N  N   . ASP A  1 261 ? 31.639  -36.067 33.737  1.00 21.88 ? 278  ASP A N   1 
ATOM   2135  C  CA  . ASP A  1 261 ? 32.999  -35.693 34.089  1.00 23.08 ? 278  ASP A CA  1 
ATOM   2136  C  C   . ASP A  1 261 ? 33.319  -36.075 35.536  1.00 21.68 ? 278  ASP A C   1 
ATOM   2137  O  O   . ASP A  1 261 ? 34.440  -36.481 35.832  1.00 21.52 ? 278  ASP A O   1 
ATOM   2138  C  CB  . ASP A  1 261 ? 33.274  -34.225 33.821  1.00 23.69 ? 278  ASP A CB  1 
ATOM   2139  C  CG  . ASP A  1 261 ? 34.731  -33.857 34.029  1.00 25.69 ? 278  ASP A CG  1 
ATOM   2140  O  OD1 . ASP A  1 261 ? 35.579  -34.469 33.354  1.00 26.98 ? 278  ASP A OD1 1 
ATOM   2141  O  OD2 . ASP A  1 261 ? 35.002  -33.019 34.910  1.00 26.98 ? 278  ASP A OD2 1 
ATOM   2142  N  N   . ASP A  1 262 ? 32.327  -35.963 36.423  1.00 21.44 ? 279  ASP A N   1 
ATOM   2143  C  CA  . ASP A  1 262 ? 32.500  -36.274 37.837  1.00 22.22 ? 279  ASP A CA  1 
ATOM   2144  C  C   . ASP A  1 262 ? 32.879  -37.744 38.032  1.00 22.00 ? 279  ASP A C   1 
ATOM   2145  O  O   . ASP A  1 262 ? 33.640  -38.068 38.947  1.00 23.79 ? 279  ASP A O   1 
ATOM   2146  C  CB  . ASP A  1 262 ? 31.265  -35.901 38.644  1.00 22.83 ? 279  ASP A CB  1 
ATOM   2147  C  CG  . ASP A  1 262 ? 30.891  -34.427 38.592  1.00 24.48 ? 279  ASP A CG  1 
ATOM   2148  O  OD1 . ASP A  1 262 ? 31.761  -33.590 38.930  1.00 28.53 ? 279  ASP A OD1 1 
ATOM   2149  O  OD2 . ASP A  1 262 ? 29.741  -34.121 38.222  1.00 24.16 ? 279  ASP A OD2 1 
ATOM   2150  N  N   . ILE A  1 263 ? 32.344  -38.631 37.184  1.00 21.86 ? 280  ILE A N   1 
ATOM   2151  C  CA  . ILE A  1 263 ? 32.655  -40.050 37.261  1.00 22.21 ? 280  ILE A CA  1 
ATOM   2152  C  C   . ILE A  1 263 ? 33.908  -40.333 36.428  1.00 21.52 ? 280  ILE A C   1 
ATOM   2153  O  O   . ILE A  1 263 ? 34.909  -40.822 36.951  1.00 20.77 ? 280  ILE A O   1 
ATOM   2154  C  CB  . ILE A  1 263 ? 31.448  -40.904 36.821  1.00 22.61 ? 280  ILE A CB  1 
ATOM   2155  C  CG1 . ILE A  1 263 ? 30.223  -40.651 37.712  1.00 22.93 ? 280  ILE A CG1 1 
ATOM   2156  C  CG2 . ILE A  1 263 ? 31.808  -42.391 36.773  1.00 23.82 ? 280  ILE A CG2 1 
ATOM   2157  C  CD1 . ILE A  1 263 ? 28.954  -41.351 37.257  1.00 22.80 ? 280  ILE A CD1 1 
ATOM   2158  N  N   . GLN A  1 264 ? 33.855  -40.002 35.134  1.00 20.75 ? 281  GLN A N   1 
ATOM   2159  C  CA  . GLN A  1 264 ? 34.812  -40.532 34.171  1.00 20.95 ? 281  GLN A CA  1 
ATOM   2160  C  C   . GLN A  1 264 ? 36.069  -39.672 34.080  1.00 20.24 ? 281  GLN A C   1 
ATOM   2161  O  O   . GLN A  1 264 ? 37.174  -40.202 33.948  1.00 20.36 ? 281  GLN A O   1 
ATOM   2162  C  CB  . GLN A  1 264 ? 34.137  -40.679 32.811  1.00 20.83 ? 281  GLN A CB  1 
ATOM   2163  C  CG  . GLN A  1 264 ? 33.023  -41.718 32.815  1.00 20.92 ? 281  GLN A CG  1 
ATOM   2164  C  CD  . GLN A  1 264 ? 32.122  -41.622 31.605  1.00 20.65 ? 281  GLN A CD  1 
ATOM   2165  O  OE1 . GLN A  1 264 ? 31.418  -40.625 31.410  1.00 20.84 ? 281  GLN A OE1 1 
ATOM   2166  N  NE2 . GLN A  1 264 ? 32.125  -42.664 30.790  1.00 20.31 ? 281  GLN A NE2 1 
ATOM   2167  N  N   . GLY A  1 265 ? 35.893  -38.348 34.101  1.00 20.32 ? 282  GLY A N   1 
ATOM   2168  C  CA  . GLY A  1 265 ? 37.022  -37.433 34.122  1.00 20.37 ? 282  GLY A CA  1 
ATOM   2169  C  C   . GLY A  1 265 ? 37.899  -37.679 35.348  1.00 20.13 ? 282  GLY A C   1 
ATOM   2170  O  O   . GLY A  1 265 ? 39.122  -37.746 35.237  1.00 18.79 ? 282  GLY A O   1 
ATOM   2171  N  N   . THR A  1 266 ? 37.239  -37.813 36.506  1.00 20.15 ? 283  THR A N   1 
ATOM   2172  C  CA  . THR A  1 266 ? 37.894  -38.066 37.783  1.00 20.81 ? 283  THR A CA  1 
ATOM   2173  C  C   . THR A  1 266 ? 38.748  -39.328 37.682  1.00 20.86 ? 283  THR A C   1 
ATOM   2174  O  O   . THR A  1 266 ? 39.916  -39.319 38.070  1.00 21.24 ? 283  THR A O   1 
ATOM   2175  C  CB  . THR A  1 266 ? 36.831  -38.195 38.876  1.00 21.54 ? 283  THR A CB  1 
ATOM   2176  O  OG1 . THR A  1 266 ? 36.214  -36.912 38.949  1.00 21.23 ? 283  THR A OG1 1 
ATOM   2177  C  CG2 . THR A  1 266 ? 37.407  -38.581 40.230  1.00 21.55 ? 283  THR A CG2 1 
ATOM   2178  N  N   . ALA A  1 267 ? 38.155  -40.410 37.165  1.00 20.00 ? 284  ALA A N   1 
ATOM   2179  C  CA  . ALA A  1 267 ? 38.860  -41.680 37.075  1.00 21.12 ? 284  ALA A CA  1 
ATOM   2180  C  C   . ALA A  1 267 ? 40.092  -41.546 36.180  1.00 20.86 ? 284  ALA A C   1 
ATOM   2181  O  O   . ALA A  1 267 ? 41.155  -42.080 36.491  1.00 19.93 ? 284  ALA A O   1 
ATOM   2182  C  CB  . ALA A  1 267 ? 37.934  -42.766 36.580  1.00 20.82 ? 284  ALA A CB  1 
ATOM   2183  N  N   . ALA A  1 268 ? 39.945  -40.823 35.068  1.00 20.80 ? 285  ALA A N   1 
ATOM   2184  C  CA  . ALA A  1 268 ? 41.024  -40.692 34.104  1.00 20.97 ? 285  ALA A CA  1 
ATOM   2185  C  C   . ALA A  1 268 ? 42.191  -39.890 34.687  1.00 20.43 ? 285  ALA A C   1 
ATOM   2186  O  O   . ALA A  1 268 ? 43.345  -40.263 34.487  1.00 20.47 ? 285  ALA A O   1 
ATOM   2187  C  CB  . ALA A  1 268 ? 40.500  -40.081 32.824  1.00 20.63 ? 285  ALA A CB  1 
ATOM   2188  N  N   . VAL A  1 269 ? 41.902  -38.793 35.399  1.00 19.74 ? 286  VAL A N   1 
ATOM   2189  C  CA  . VAL A  1 269 ? 42.960  -37.930 35.908  1.00 20.58 ? 286  VAL A CA  1 
ATOM   2190  C  C   . VAL A  1 269 ? 43.691  -38.643 37.051  1.00 20.75 ? 286  VAL A C   1 
ATOM   2191  O  O   . VAL A  1 269 ? 44.913  -38.548 37.152  1.00 19.39 ? 286  VAL A O   1 
ATOM   2192  C  CB  . VAL A  1 269 ? 42.483  -36.518 36.310  1.00 22.79 ? 286  VAL A CB  1 
ATOM   2193  C  CG1 . VAL A  1 269 ? 41.533  -36.526 37.501  1.00 24.01 ? 286  VAL A CG1 1 
ATOM   2194  C  CG2 . VAL A  1 269 ? 43.658  -35.584 36.585  1.00 23.67 ? 286  VAL A CG2 1 
ATOM   2195  N  N   . ALA A  1 270 ? 42.950  -39.379 37.890  1.00 21.35 ? 287  ALA A N   1 
ATOM   2196  C  CA  . ALA A  1 270 ? 43.556  -40.154 38.961  1.00 21.17 ? 287  ALA A CA  1 
ATOM   2197  C  C   . ALA A  1 270 ? 44.492  -41.209 38.374  1.00 20.99 ? 287  ALA A C   1 
ATOM   2198  O  O   . ALA A  1 270 ? 45.629  -41.348 38.823  1.00 21.52 ? 287  ALA A O   1 
ATOM   2199  C  CB  . ALA A  1 270 ? 42.485  -40.776 39.831  1.00 21.25 ? 287  ALA A CB  1 
ATOM   2200  N  N   . LEU A  1 271 ? 44.017  -41.929 37.350  1.00 20.60 ? 288  LEU A N   1 
ATOM   2201  C  CA  . LEU A  1 271 ? 44.787  -42.993 36.729  1.00 20.53 ? 288  LEU A CA  1 
ATOM   2202  C  C   . LEU A  1 271 ? 46.062  -42.416 36.120  1.00 20.77 ? 288  LEU A C   1 
ATOM   2203  O  O   . LEU A  1 271 ? 47.127  -43.014 36.253  1.00 21.25 ? 288  LEU A O   1 
ATOM   2204  C  CB  . LEU A  1 271 ? 43.976  -43.761 35.683  1.00 21.12 ? 288  LEU A CB  1 
ATOM   2205  C  CG  . LEU A  1 271 ? 44.757  -44.801 34.873  1.00 21.58 ? 288  LEU A CG  1 
ATOM   2206  C  CD1 . LEU A  1 271 ? 45.363  -45.877 35.768  1.00 21.91 ? 288  LEU A CD1 1 
ATOM   2207  C  CD2 . LEU A  1 271 ? 43.900  -45.446 33.807  1.00 21.98 ? 288  LEU A CD2 1 
ATOM   2208  N  N   . ALA A  1 272 ? 45.949  -41.256 35.456  1.00 20.85 ? 289  ALA A N   1 
ATOM   2209  C  CA  . ALA A  1 272 ? 47.099  -40.628 34.828  1.00 20.58 ? 289  ALA A CA  1 
ATOM   2210  C  C   . ALA A  1 272 ? 48.204  -40.418 35.861  1.00 20.85 ? 289  ALA A C   1 
ATOM   2211  O  O   . ALA A  1 272 ? 49.366  -40.705 35.593  1.00 21.16 ? 289  ALA A O   1 
ATOM   2212  C  CB  . ALA A  1 272 ? 46.706  -39.327 34.167  1.00 19.71 ? 289  ALA A CB  1 
ATOM   2213  N  N   . GLY A  1 273 ? 47.824  -39.919 37.042  1.00 21.68 ? 290  GLY A N   1 
ATOM   2214  C  CA  . GLY A  1 273 ? 48.770  -39.671 38.121  1.00 21.54 ? 290  GLY A CA  1 
ATOM   2215  C  C   . GLY A  1 273 ? 49.470  -40.948 38.578  1.00 21.09 ? 290  GLY A C   1 
ATOM   2216  O  O   . GLY A  1 273 ? 50.672  -40.939 38.841  1.00 20.74 ? 290  GLY A O   1 
ATOM   2217  N  N   . LEU A  1 274 ? 48.699  -42.035 38.678  1.00 21.62 ? 291  LEU A N   1 
ATOM   2218  C  CA  . LEU A  1 274 ? 49.218  -43.335 39.073  1.00 22.28 ? 291  LEU A CA  1 
ATOM   2219  C  C   . LEU A  1 274 ? 50.150  -43.896 37.999  1.00 22.97 ? 291  LEU A C   1 
ATOM   2220  O  O   . LEU A  1 274 ? 51.149  -44.532 38.325  1.00 22.07 ? 291  LEU A O   1 
ATOM   2221  C  CB  . LEU A  1 274 ? 48.053  -44.287 39.337  1.00 22.54 ? 291  LEU A CB  1 
ATOM   2222  C  CG  . LEU A  1 274 ? 47.118  -43.899 40.488  1.00 23.26 ? 291  LEU A CG  1 
ATOM   2223  C  CD1 . LEU A  1 274 ? 45.979  -44.904 40.596  1.00 23.68 ? 291  LEU A CD1 1 
ATOM   2224  C  CD2 . LEU A  1 274 ? 47.853  -43.772 41.809  1.00 23.32 ? 291  LEU A CD2 1 
ATOM   2225  N  N   . LEU A  1 275 ? 49.813  -43.679 36.721  1.00 23.34 ? 292  LEU A N   1 
ATOM   2226  C  CA  . LEU A  1 275 ? 50.667  -44.128 35.631  1.00 24.55 ? 292  LEU A CA  1 
ATOM   2227  C  C   . LEU A  1 275 ? 51.992  -43.368 35.680  1.00 24.13 ? 292  LEU A C   1 
ATOM   2228  O  O   . LEU A  1 275 ? 53.041  -43.940 35.406  1.00 25.48 ? 292  LEU A O   1 
ATOM   2229  C  CB  . LEU A  1 275 ? 49.982  -43.969 34.273  1.00 25.01 ? 292  LEU A CB  1 
ATOM   2230  C  CG  . LEU A  1 275 ? 48.795  -44.896 33.991  1.00 25.81 ? 292  LEU A CG  1 
ATOM   2231  C  CD1 . LEU A  1 275 ? 48.100  -44.449 32.715  1.00 25.70 ? 292  LEU A CD1 1 
ATOM   2232  C  CD2 . LEU A  1 275 ? 49.193  -46.364 33.888  1.00 25.91 ? 292  LEU A CD2 1 
ATOM   2233  N  N   . ALA A  1 276 ? 51.944  -42.080 36.034  1.00 23.56 ? 293  ALA A N   1 
ATOM   2234  C  CA  . ALA A  1 276 ? 53.158  -41.293 36.171  1.00 23.67 ? 293  ALA A CA  1 
ATOM   2235  C  C   . ALA A  1 276 ? 54.009  -41.838 37.316  1.00 25.44 ? 293  ALA A C   1 
ATOM   2236  O  O   . ALA A  1 276 ? 55.229  -41.941 37.190  1.00 25.90 ? 293  ALA A O   1 
ATOM   2237  C  CB  . ALA A  1 276 ? 52.823  -39.839 36.372  1.00 23.17 ? 293  ALA A CB  1 
ATOM   2238  N  N   . ALA A  1 277 ? 53.356  -42.201 38.426  1.00 26.62 ? 294  ALA A N   1 
ATOM   2239  C  CA  . ALA A  1 277 ? 54.050  -42.729 39.593  1.00 28.65 ? 294  ALA A CA  1 
ATOM   2240  C  C   . ALA A  1 277 ? 54.759  -44.037 39.249  1.00 31.31 ? 294  ALA A C   1 
ATOM   2241  O  O   . ALA A  1 277 ? 55.864  -44.284 39.735  1.00 31.35 ? 294  ALA A O   1 
ATOM   2242  C  CB  . ALA A  1 277 ? 53.084  -42.912 40.744  1.00 28.23 ? 294  ALA A CB  1 
ATOM   2243  N  N   A GLN A  1 278 ? 54.113  -44.853 38.409  0.50 32.69 ? 295  GLN A N   1 
ATOM   2244  N  N   B GLN A  1 278 ? 54.114  -44.858 38.409  0.50 32.88 ? 295  GLN A N   1 
ATOM   2245  C  CA  A GLN A  1 278 ? 54.640  -46.143 37.997  0.50 35.39 ? 295  GLN A CA  1 
ATOM   2246  C  CA  B GLN A  1 278 ? 54.643  -46.150 37.995  0.50 35.74 ? 295  GLN A CA  1 
ATOM   2247  C  C   A GLN A  1 278 ? 55.893  -45.986 37.136  0.50 36.89 ? 295  GLN A C   1 
ATOM   2248  C  C   B GLN A  1 278 ? 55.896  -45.987 37.134  0.50 37.08 ? 295  GLN A C   1 
ATOM   2249  O  O   A GLN A  1 278 ? 56.738  -46.879 37.114  0.50 36.63 ? 295  GLN A O   1 
ATOM   2250  O  O   B GLN A  1 278 ? 56.742  -46.879 37.109  0.50 36.80 ? 295  GLN A O   1 
ATOM   2251  C  CB  A GLN A  1 278 ? 53.545  -46.897 37.243  0.50 36.85 ? 295  GLN A CB  1 
ATOM   2252  C  CB  B GLN A  1 278 ? 53.570  -46.938 37.241  0.50 37.46 ? 295  GLN A CB  1 
ATOM   2253  C  CG  A GLN A  1 278 ? 54.063  -48.023 36.357  0.50 38.64 ? 295  GLN A CG  1 
ATOM   2254  C  CG  B GLN A  1 278 ? 54.113  -48.045 36.342  0.50 39.48 ? 295  GLN A CG  1 
ATOM   2255  C  CD  A GLN A  1 278 ? 52.998  -48.565 35.431  0.50 40.51 ? 295  GLN A CD  1 
ATOM   2256  C  CD  B GLN A  1 278 ? 54.850  -49.136 37.090  0.50 41.75 ? 295  GLN A CD  1 
ATOM   2257  O  OE1 A GLN A  1 278 ? 53.283  -49.299 34.479  0.50 43.11 ? 295  GLN A OE1 1 
ATOM   2258  O  OE1 B GLN A  1 278 ? 55.292  -50.131 36.505  0.50 42.79 ? 295  GLN A OE1 1 
ATOM   2259  N  NE2 A GLN A  1 278 ? 51.756  -48.188 35.695  0.50 40.43 ? 295  GLN A NE2 1 
ATOM   2260  N  NE2 B GLN A  1 278 ? 54.991  -48.959 38.395  0.50 43.26 ? 295  GLN A NE2 1 
ATOM   2261  N  N   . LYS A  1 279 ? 56.006  -44.864 36.413  1.00 38.12 ? 296  LYS A N   1 
ATOM   2262  C  CA  . LYS A  1 279 ? 57.196  -44.586 35.619  1.00 43.67 ? 296  LYS A CA  1 
ATOM   2263  C  C   . LYS A  1 279 ? 58.385  -44.336 36.546  1.00 47.12 ? 296  LYS A C   1 
ATOM   2264  O  O   . LYS A  1 279 ? 59.515  -44.681 36.209  1.00 47.95 ? 296  LYS A O   1 
ATOM   2265  C  CB  . LYS A  1 279 ? 57.000  -43.431 34.628  1.00 47.26 ? 296  LYS A CB  1 
ATOM   2266  C  CG  . LYS A  1 279 ? 56.049  -43.756 33.483  1.00 50.61 ? 296  LYS A CG  1 
ATOM   2267  C  CD  . LYS A  1 279 ? 55.966  -42.704 32.383  1.00 53.27 ? 296  LYS A CD  1 
ATOM   2268  C  CE  . LYS A  1 279 ? 57.167  -42.689 31.490  1.00 54.29 ? 296  LYS A CE  1 
ATOM   2269  N  NZ  . LYS A  1 279 ? 56.981  -41.767 30.365  1.00 54.44 ? 296  LYS A NZ  1 
ATOM   2270  N  N   . VAL A  1 280 ? 58.118  -43.765 37.725  1.00 48.93 ? 297  VAL A N   1 
ATOM   2271  C  CA  . VAL A  1 280 ? 59.156  -43.526 38.715  1.00 50.18 ? 297  VAL A CA  1 
ATOM   2272  C  C   . VAL A  1 280 ? 59.435  -44.827 39.468  1.00 49.72 ? 297  VAL A C   1 
ATOM   2273  O  O   . VAL A  1 280 ? 60.594  -45.173 39.676  1.00 53.38 ? 297  VAL A O   1 
ATOM   2274  C  CB  . VAL A  1 280 ? 58.780  -42.375 39.671  1.00 52.10 ? 297  VAL A CB  1 
ATOM   2275  C  CG1 . VAL A  1 280 ? 59.929  -42.019 40.608  1.00 54.52 ? 297  VAL A CG1 1 
ATOM   2276  C  CG2 . VAL A  1 280 ? 58.322  -41.129 38.919  1.00 50.61 ? 297  VAL A CG2 1 
ATOM   2277  N  N   . ILE A  1 281 ? 58.374  -45.546 39.862  1.00 53.01 ? 298  ILE A N   1 
ATOM   2278  C  CA  . ILE A  1 281 ? 58.496  -46.808 40.582  1.00 54.25 ? 298  ILE A CA  1 
ATOM   2279  C  C   . ILE A  1 281 ? 58.299  -47.975 39.612  1.00 55.67 ? 298  ILE A C   1 
ATOM   2280  O  O   . ILE A  1 281 ? 57.199  -48.514 39.491  1.00 55.72 ? 298  ILE A O   1 
ATOM   2281  C  CB  . ILE A  1 281 ? 57.489  -46.893 41.744  1.00 55.57 ? 298  ILE A CB  1 
ATOM   2282  C  CG1 . ILE A  1 281 ? 57.494  -45.637 42.608  1.00 55.90 ? 298  ILE A CG1 1 
ATOM   2283  C  CG2 . ILE A  1 281 ? 57.734  -48.150 42.580  1.00 57.09 ? 298  ILE A CG2 1 
ATOM   2284  C  CD1 . ILE A  1 281 ? 56.318  -45.557 43.563  1.00 56.59 ? 298  ILE A CD1 1 
ATOM   2285  N  N   . SER A  1 282 ? 59.404  -48.414 39.005  1.00 54.89 ? 299  SER A N   1 
ATOM   2286  C  CA  . SER A  1 282 ? 59.412  -49.369 37.908  1.00 52.97 ? 299  SER A CA  1 
ATOM   2287  C  C   . SER A  1 282 ? 58.740  -50.701 38.257  1.00 53.50 ? 299  SER A C   1 
ATOM   2288  O  O   . SER A  1 282 ? 58.522  -51.526 37.371  1.00 53.09 ? 299  SER A O   1 
ATOM   2289  C  CB  . SER A  1 282 ? 60.832  -49.600 37.467  1.00 52.32 ? 299  SER A CB  1 
ATOM   2290  O  OG  . SER A  1 282 ? 61.571  -48.387 37.490  1.00 49.86 ? 299  SER A OG  1 
ATOM   2291  N  N   . LYS A  1 283 ? 58.434  -50.919 39.543  1.00 53.33 ? 300  LYS A N   1 
ATOM   2292  C  CA  . LYS A  1 283 ? 57.793  -52.136 40.024  1.00 51.97 ? 300  LYS A CA  1 
ATOM   2293  C  C   . LYS A  1 283 ? 56.742  -52.645 39.033  1.00 48.66 ? 300  LYS A C   1 
ATOM   2294  O  O   . LYS A  1 283 ? 55.882  -51.879 38.602  1.00 46.96 ? 300  LYS A O   1 
ATOM   2295  C  CB  . LYS A  1 283 ? 57.121  -51.829 41.368  1.00 52.94 ? 300  LYS A CB  1 
ATOM   2296  C  CG  . LYS A  1 283 ? 56.661  -53.035 42.171  1.00 54.25 ? 300  LYS A CG  1 
ATOM   2297  C  CD  . LYS A  1 283 ? 55.453  -52.755 43.060  1.00 55.88 ? 300  LYS A CD  1 
ATOM   2298  C  CE  . LYS A  1 283 ? 55.690  -51.774 44.164  1.00 55.74 ? 300  LYS A CE  1 
ATOM   2299  N  NZ  . LYS A  1 283 ? 56.315  -52.414 45.323  1.00 55.56 ? 300  LYS A NZ  1 
ATOM   2300  N  N   . PRO A  1 284 ? 56.771  -53.945 38.648  1.00 45.69 ? 301  PRO A N   1 
ATOM   2301  C  CA  . PRO A  1 284 ? 55.702  -54.545 37.843  1.00 47.19 ? 301  PRO A CA  1 
ATOM   2302  C  C   . PRO A  1 284 ? 54.319  -54.469 38.490  1.00 45.64 ? 301  PRO A C   1 
ATOM   2303  O  O   . PRO A  1 284 ? 54.176  -54.654 39.697  1.00 42.92 ? 301  PRO A O   1 
ATOM   2304  C  CB  . PRO A  1 284 ? 56.149  -56.006 37.654  1.00 47.36 ? 301  PRO A CB  1 
ATOM   2305  C  CG  . PRO A  1 284 ? 57.645  -55.970 37.871  1.00 47.72 ? 301  PRO A CG  1 
ATOM   2306  C  CD  . PRO A  1 284 ? 57.862  -54.893 38.918  1.00 47.61 ? 301  PRO A CD  1 
ATOM   2307  N  N   . ILE A  1 285 ? 53.302  -54.254 37.651  1.00 43.32 ? 302  ILE A N   1 
ATOM   2308  C  CA  . ILE A  1 285 ? 51.941  -53.985 38.088  1.00 43.17 ? 302  ILE A CA  1 
ATOM   2309  C  C   . ILE A  1 285 ? 51.458  -55.063 39.056  1.00 41.79 ? 302  ILE A C   1 
ATOM   2310  O  O   . ILE A  1 285 ? 50.734  -54.759 40.000  1.00 40.78 ? 302  ILE A O   1 
ATOM   2311  C  CB  . ILE A  1 285 ? 51.017  -53.855 36.861  1.00 46.28 ? 302  ILE A CB  1 
ATOM   2312  C  CG1 . ILE A  1 285 ? 51.336  -52.601 36.050  1.00 47.38 ? 302  ILE A CG1 1 
ATOM   2313  C  CG2 . ILE A  1 285 ? 49.542  -53.902 37.254  1.00 47.89 ? 302  ILE A CG2 1 
ATOM   2314  C  CD1 . ILE A  1 285 ? 51.156  -51.300 36.810  1.00 49.52 ? 302  ILE A CD1 1 
ATOM   2315  N  N   . SER A  1 286 ? 51.872  -56.316 38.827  1.00 41.08 ? 303  SER A N   1 
ATOM   2316  C  CA  . SER A  1 286 ? 51.415  -57.445 39.623  1.00 41.51 ? 303  SER A CA  1 
ATOM   2317  C  C   . SER A  1 286 ? 51.855  -57.335 41.087  1.00 39.72 ? 303  SER A C   1 
ATOM   2318  O  O   . SER A  1 286 ? 51.319  -58.044 41.937  1.00 40.55 ? 303  SER A O   1 
ATOM   2319  C  CB  . SER A  1 286 ? 51.872  -58.752 39.012  1.00 44.32 ? 303  SER A CB  1 
ATOM   2320  O  OG  . SER A  1 286 ? 53.280  -58.768 38.821  1.00 44.79 ? 303  SER A OG  1 
ATOM   2321  N  N   . GLU A  1 287 ? 52.811  -56.447 41.383  1.00 36.86 ? 304  GLU A N   1 
ATOM   2322  C  CA  . GLU A  1 287 ? 53.321  -56.283 42.737  1.00 37.87 ? 304  GLU A CA  1 
ATOM   2323  C  C   . GLU A  1 287 ? 52.761  -55.032 43.423  1.00 36.45 ? 304  GLU A C   1 
ATOM   2324  O  O   . GLU A  1 287 ? 53.056  -54.787 44.592  1.00 34.83 ? 304  GLU A O   1 
ATOM   2325  C  CB  . GLU A  1 287 ? 54.848  -56.228 42.683  1.00 39.54 ? 304  GLU A CB  1 
ATOM   2326  C  CG  . GLU A  1 287 ? 55.492  -57.578 42.386  1.00 41.31 ? 304  GLU A CG  1 
ATOM   2327  C  CD  . GLU A  1 287 ? 56.997  -57.488 42.218  1.00 42.56 ? 304  GLU A CD  1 
ATOM   2328  O  OE1 . GLU A  1 287 ? 57.631  -56.818 43.054  1.00 44.02 ? 304  GLU A OE1 1 
ATOM   2329  O  OE2 . GLU A  1 287 ? 57.535  -58.083 41.261  1.00 44.89 ? 304  GLU A OE2 1 
ATOM   2330  N  N   . HIS A  1 288 ? 51.967  -54.230 42.705  1.00 34.63 ? 305  HIS A N   1 
ATOM   2331  C  CA  . HIS A  1 288 ? 51.322  -53.074 43.307  1.00 33.99 ? 305  HIS A CA  1 
ATOM   2332  C  C   . HIS A  1 288 ? 50.142  -53.533 44.161  1.00 29.34 ? 305  HIS A C   1 
ATOM   2333  O  O   . HIS A  1 288 ? 49.500  -54.535 43.857  1.00 27.99 ? 305  HIS A O   1 
ATOM   2334  C  CB  . HIS A  1 288 ? 50.931  -52.041 42.242  1.00 37.30 ? 305  HIS A CB  1 
ATOM   2335  C  CG  . HIS A  1 288 ? 52.090  -51.211 41.802  1.00 42.71 ? 305  HIS A CG  1 
ATOM   2336  N  ND1 . HIS A  1 288 ? 52.533  -50.132 42.540  1.00 45.07 ? 305  HIS A ND1 1 
ATOM   2337  C  CD2 . HIS A  1 288 ? 52.918  -51.312 40.752  1.00 43.12 ? 305  HIS A CD2 1 
ATOM   2338  C  CE1 . HIS A  1 288 ? 53.584  -49.594 41.934  1.00 47.32 ? 305  HIS A CE1 1 
ATOM   2339  N  NE2 . HIS A  1 288 ? 53.834  -50.296 40.847  1.00 46.30 ? 305  HIS A NE2 1 
ATOM   2340  N  N   . LYS A  1 289 ? 49.890  -52.797 45.248  1.00 27.59 ? 306  LYS A N   1 
ATOM   2341  C  CA  . LYS A  1 289 ? 48.709  -52.995 46.072  1.00 26.23 ? 306  LYS A CA  1 
ATOM   2342  C  C   . LYS A  1 289 ? 48.170  -51.622 46.461  1.00 24.39 ? 306  LYS A C   1 
ATOM   2343  O  O   . LYS A  1 289 ? 48.899  -50.801 47.019  1.00 24.47 ? 306  LYS A O   1 
ATOM   2344  C  CB  . LYS A  1 289 ? 49.001  -53.852 47.308  1.00 27.44 ? 306  LYS A CB  1 
ATOM   2345  C  CG  . LYS A  1 289 ? 47.748  -54.321 48.046  1.00 28.23 ? 306  LYS A CG  1 
ATOM   2346  C  CD  . LYS A  1 289 ? 47.988  -55.033 49.372  1.00 30.05 ? 306  LYS A CD  1 
ATOM   2347  C  CE  . LYS A  1 289 ? 48.696  -56.343 49.249  1.00 31.07 ? 306  LYS A CE  1 
ATOM   2348  N  NZ  . LYS A  1 289 ? 48.781  -56.995 50.561  1.00 31.66 ? 306  LYS A NZ  1 
ATOM   2349  N  N   . ILE A  1 290 ? 46.888  -51.394 46.151  1.00 22.67 ? 307  ILE A N   1 
ATOM   2350  C  CA  . ILE A  1 290 ? 46.258  -50.089 46.269  1.00 22.13 ? 307  ILE A CA  1 
ATOM   2351  C  C   . ILE A  1 290 ? 45.178  -50.164 47.349  1.00 21.43 ? 307  ILE A C   1 
ATOM   2352  O  O   . ILE A  1 290 ? 44.331  -51.051 47.310  1.00 22.94 ? 307  ILE A O   1 
ATOM   2353  C  CB  . ILE A  1 290 ? 45.674  -49.663 44.908  1.00 23.05 ? 307  ILE A CB  1 
ATOM   2354  C  CG1 . ILE A  1 290 ? 46.767  -49.569 43.842  1.00 24.95 ? 307  ILE A CG1 1 
ATOM   2355  C  CG2 . ILE A  1 290 ? 44.895  -48.352 45.020  1.00 22.81 ? 307  ILE A CG2 1 
ATOM   2356  C  CD1 . ILE A  1 290 ? 46.247  -49.635 42.422  1.00 26.47 ? 307  ILE A CD1 1 
ATOM   2357  N  N   . LEU A  1 291 ? 45.209  -49.224 48.303  1.00 20.24 ? 308  LEU A N   1 
ATOM   2358  C  CA  . LEU A  1 291 ? 44.225  -49.179 49.376  1.00 19.80 ? 308  LEU A CA  1 
ATOM   2359  C  C   . LEU A  1 291 ? 43.494  -47.840 49.326  1.00 19.05 ? 308  LEU A C   1 
ATOM   2360  O  O   . LEU A  1 291 ? 44.109  -46.778 49.429  1.00 18.76 ? 308  LEU A O   1 
ATOM   2361  C  CB  . LEU A  1 291 ? 44.903  -49.416 50.725  1.00 20.01 ? 308  LEU A CB  1 
ATOM   2362  C  CG  . LEU A  1 291 ? 44.056  -49.156 51.976  1.00 20.33 ? 308  LEU A CG  1 
ATOM   2363  C  CD1 . LEU A  1 291 ? 42.864  -50.099 52.046  1.00 20.42 ? 308  LEU A CD1 1 
ATOM   2364  C  CD2 . LEU A  1 291 ? 44.927  -49.263 53.222  1.00 20.66 ? 308  LEU A CD2 1 
ATOM   2365  N  N   . PHE A  1 292 ? 42.172  -47.907 49.160  1.00 18.95 ? 309  PHE A N   1 
ATOM   2366  C  CA  . PHE A  1 292 ? 41.334  -46.719 49.145  1.00 19.20 ? 309  PHE A CA  1 
ATOM   2367  C  C   . PHE A  1 292 ? 40.842  -46.426 50.560  1.00 20.05 ? 309  PHE A C   1 
ATOM   2368  O  O   . PHE A  1 292 ? 40.468  -47.344 51.295  1.00 19.63 ? 309  PHE A O   1 
ATOM   2369  C  CB  . PHE A  1 292 ? 40.129  -46.895 48.219  1.00 19.15 ? 309  PHE A CB  1 
ATOM   2370  C  CG  . PHE A  1 292 ? 40.440  -46.816 46.731  1.00 19.10 ? 309  PHE A CG  1 
ATOM   2371  C  CD1 . PHE A  1 292 ? 40.936  -47.918 46.043  1.00 19.07 ? 309  PHE A CD1 1 
ATOM   2372  C  CD2 . PHE A  1 292 ? 40.218  -45.638 46.020  1.00 18.83 ? 309  PHE A CD2 1 
ATOM   2373  C  CE1 . PHE A  1 292 ? 41.223  -47.839 44.684  1.00 19.54 ? 309  PHE A CE1 1 
ATOM   2374  C  CE2 . PHE A  1 292 ? 40.510  -45.566 44.665  1.00 18.76 ? 309  PHE A CE2 1 
ATOM   2375  C  CZ  . PHE A  1 292 ? 41.010  -46.663 44.000  1.00 19.25 ? 309  PHE A CZ  1 
ATOM   2376  N  N   . LEU A  1 293 ? 40.860  -45.137 50.921  1.00 19.76 ? 310  LEU A N   1 
ATOM   2377  C  CA  . LEU A  1 293 ? 40.068  -44.625 52.024  1.00 20.53 ? 310  LEU A CA  1 
ATOM   2378  C  C   . LEU A  1 293 ? 38.767  -44.094 51.431  1.00 20.83 ? 310  LEU A C   1 
ATOM   2379  O  O   . LEU A  1 293 ? 38.770  -43.080 50.736  1.00 20.81 ? 310  LEU A O   1 
ATOM   2380  C  CB  . LEU A  1 293 ? 40.820  -43.538 52.792  1.00 21.50 ? 310  LEU A CB  1 
ATOM   2381  C  CG  . LEU A  1 293 ? 40.053  -42.902 53.954  1.00 21.85 ? 310  LEU A CG  1 
ATOM   2382  C  CD1 . LEU A  1 293 ? 40.186  -43.745 55.205  1.00 23.45 ? 310  LEU A CD1 1 
ATOM   2383  C  CD2 . LEU A  1 293 ? 40.494  -41.467 54.201  1.00 23.31 ? 310  LEU A CD2 1 
ATOM   2384  N  N   . GLY A  1 294 ? 37.670  -44.812 51.699  1.00 21.17 ? 311  GLY A N   1 
ATOM   2385  C  CA  . GLY A  1 294 ? 36.407  -44.589 51.019  1.00 22.19 ? 311  GLY A CA  1 
ATOM   2386  C  C   . GLY A  1 294 ? 36.104  -45.728 50.048  1.00 21.71 ? 311  GLY A C   1 
ATOM   2387  O  O   . GLY A  1 294 ? 37.012  -46.367 49.524  1.00 21.51 ? 311  GLY A O   1 
ATOM   2388  N  N   . ALA A  1 295 ? 34.809  -45.974 49.828  1.00 22.06 ? 312  ALA A N   1 
ATOM   2389  C  CA  . ALA A  1 295 ? 34.361  -47.005 48.910  1.00 21.99 ? 312  ALA A CA  1 
ATOM   2390  C  C   . ALA A  1 295 ? 33.099  -46.539 48.189  1.00 22.34 ? 312  ALA A C   1 
ATOM   2391  O  O   . ALA A  1 295 ? 32.215  -47.338 47.889  1.00 22.67 ? 312  ALA A O   1 
ATOM   2392  C  CB  . ALA A  1 295 ? 34.140  -48.293 49.678  1.00 22.91 ? 312  ALA A CB  1 
ATOM   2393  N  N   . GLY A  1 296 ? 33.039  -45.235 47.905  1.00 22.08 ? 313  GLY A N   1 
ATOM   2394  C  CA  . GLY A  1 296 ? 31.891  -44.622 47.259  1.00 21.54 ? 313  GLY A CA  1 
ATOM   2395  C  C   . GLY A  1 296 ? 32.122  -44.441 45.760  1.00 21.08 ? 313  GLY A C   1 
ATOM   2396  O  O   . GLY A  1 296 ? 32.851  -45.206 45.135  1.00 19.36 ? 313  GLY A O   1 
ATOM   2397  N  N   . GLU A  1 297 ? 31.479  -43.421 45.184  1.00 21.98 ? 314  GLU A N   1 
ATOM   2398  C  CA  . GLU A  1 297 ? 31.454  -43.261 43.737  1.00 23.44 ? 314  GLU A CA  1 
ATOM   2399  C  C   . GLU A  1 297 ? 32.855  -42.998 43.188  1.00 21.91 ? 314  GLU A C   1 
ATOM   2400  O  O   . GLU A  1 297 ? 33.214  -43.564 42.160  1.00 21.54 ? 314  GLU A O   1 
ATOM   2401  C  CB  . GLU A  1 297 ? 30.480  -42.161 43.314  1.00 25.42 ? 314  GLU A CB  1 
ATOM   2402  C  CG  . GLU A  1 297 ? 29.027  -42.633 43.341  1.00 28.51 ? 314  GLU A CG  1 
ATOM   2403  C  CD  . GLU A  1 297 ? 28.791  -43.845 42.451  1.00 31.26 ? 314  GLU A CD  1 
ATOM   2404  O  OE1 . GLU A  1 297 ? 28.969  -43.728 41.212  1.00 34.85 ? 314  GLU A OE1 1 
ATOM   2405  O  OE2 . GLU A  1 297 ? 28.466  -44.914 43.003  1.00 31.68 ? 314  GLU A OE2 1 
ATOM   2406  N  N   . ALA A  1 298 ? 33.624  -42.124 43.849  1.00 21.19 ? 315  ALA A N   1 
ATOM   2407  C  CA  . ALA A  1 298 ? 34.965  -41.798 43.384  1.00 20.93 ? 315  ALA A CA  1 
ATOM   2408  C  C   . ALA A  1 298 ? 35.874  -43.022 43.491  1.00 20.84 ? 315  ALA A C   1 
ATOM   2409  O  O   . ALA A  1 298 ? 36.606  -43.323 42.552  1.00 22.52 ? 315  ALA A O   1 
ATOM   2410  C  CB  . ALA A  1 298 ? 35.528  -40.620 44.143  1.00 20.75 ? 315  ALA A CB  1 
ATOM   2411  N  N   . ALA A  1 299 ? 35.832  -43.727 44.630  1.00 19.99 ? 316  ALA A N   1 
ATOM   2412  C  CA  . ALA A  1 299 ? 36.657  -44.918 44.806  1.00 19.76 ? 316  ALA A CA  1 
ATOM   2413  C  C   . ALA A  1 299 ? 36.375  -45.933 43.700  1.00 19.46 ? 316  ALA A C   1 
ATOM   2414  O  O   . ALA A  1 299 ? 37.299  -46.485 43.105  1.00 19.02 ? 316  ALA A O   1 
ATOM   2415  C  CB  . ALA A  1 299 ? 36.432  -45.533 46.173  1.00 19.69 ? 316  ALA A CB  1 
ATOM   2416  N  N   . LEU A  1 300 ? 35.086  -46.179 43.429  1.00 19.43 ? 317  LEU A N   1 
ATOM   2417  C  CA  . LEU A  1 300 ? 34.686  -47.230 42.510  1.00 19.60 ? 317  LEU A CA  1 
ATOM   2418  C  C   . LEU A  1 300 ? 35.022  -46.844 41.069  1.00 19.57 ? 317  LEU A C   1 
ATOM   2419  O  O   . LEU A  1 300 ? 35.452  -47.688 40.291  1.00 21.03 ? 317  LEU A O   1 
ATOM   2420  C  CB  . LEU A  1 300 ? 33.198  -47.533 42.699  1.00 20.15 ? 317  LEU A CB  1 
ATOM   2421  C  CG  . LEU A  1 300 ? 32.814  -48.200 44.024  1.00 20.23 ? 317  LEU A CG  1 
ATOM   2422  C  CD1 . LEU A  1 300 ? 31.304  -48.243 44.211  1.00 20.03 ? 317  LEU A CD1 1 
ATOM   2423  C  CD2 . LEU A  1 300 ? 33.391  -49.602 44.121  1.00 21.28 ? 317  LEU A CD2 1 
ATOM   2424  N  N   . GLY A  1 301 ? 34.825  -45.571 40.711  1.00 20.40 ? 318  GLY A N   1 
ATOM   2425  C  CA  . GLY A  1 301 ? 35.166  -45.091 39.381  1.00 20.09 ? 318  GLY A CA  1 
ATOM   2426  C  C   . GLY A  1 301 ? 36.658  -45.254 39.082  1.00 19.24 ? 318  GLY A C   1 
ATOM   2427  O  O   . GLY A  1 301 ? 37.030  -45.794 38.044  1.00 19.59 ? 318  GLY A O   1 
ATOM   2428  N  N   . ILE A  1 302 ? 37.499  -44.779 40.006  1.00 18.96 ? 319  ILE A N   1 
ATOM   2429  C  CA  . ILE A  1 302 ? 38.945  -44.849 39.858  1.00 19.10 ? 319  ILE A CA  1 
ATOM   2430  C  C   . ILE A  1 302 ? 39.384  -46.313 39.808  1.00 19.33 ? 319  ILE A C   1 
ATOM   2431  O  O   . ILE A  1 302 ? 40.166  -46.691 38.939  1.00 19.73 ? 319  ILE A O   1 
ATOM   2432  C  CB  . ILE A  1 302 ? 39.659  -44.072 40.984  1.00 18.32 ? 319  ILE A CB  1 
ATOM   2433  C  CG1 . ILE A  1 302 ? 39.323  -42.581 40.934  1.00 17.96 ? 319  ILE A CG1 1 
ATOM   2434  C  CG2 . ILE A  1 302 ? 41.175  -44.301 40.944  1.00 17.74 ? 319  ILE A CG2 1 
ATOM   2435  C  CD1 . ILE A  1 302 ? 39.627  -41.820 42.215  1.00 18.02 ? 319  ILE A CD1 1 
ATOM   2436  N  N   . ALA A  1 303 ? 38.889  -47.128 40.747  1.00 19.62 ? 320  ALA A N   1 
ATOM   2437  C  CA  . ALA A  1 303 ? 39.285  -48.526 40.832  1.00 19.61 ? 320  ALA A CA  1 
ATOM   2438  C  C   . ALA A  1 303 ? 38.956  -49.255 39.529  1.00 20.71 ? 320  ALA A C   1 
ATOM   2439  O  O   . ALA A  1 303 ? 39.771  -50.029 39.030  1.00 20.01 ? 320  ALA A O   1 
ATOM   2440  C  CB  . ALA A  1 303 ? 38.630  -49.198 42.022  1.00 19.40 ? 320  ALA A CB  1 
ATOM   2441  N  N   . ASN A  1 304 ? 37.762  -49.005 38.971  1.00 21.38 ? 321  ASN A N   1 
ATOM   2442  C  CA  . ASN A  1 304 ? 37.339  -49.702 37.764  1.00 22.51 ? 321  ASN A CA  1 
ATOM   2443  C  C   . ASN A  1 304 ? 38.247  -49.325 36.594  1.00 21.97 ? 321  ASN A C   1 
ATOM   2444  O  O   . ASN A  1 304 ? 38.524  -50.173 35.743  1.00 21.81 ? 321  ASN A O   1 
ATOM   2445  C  CB  . ASN A  1 304 ? 35.848  -49.527 37.481  1.00 25.43 ? 321  ASN A CB  1 
ATOM   2446  C  CG  . ASN A  1 304 ? 34.996  -50.447 38.331  1.00 28.66 ? 321  ASN A CG  1 
ATOM   2447  O  OD1 . ASN A  1 304 ? 35.189  -51.672 38.325  1.00 29.23 ? 321  ASN A OD1 1 
ATOM   2448  N  ND2 . ASN A  1 304 ? 34.048  -49.889 39.071  1.00 29.89 ? 321  ASN A ND2 1 
ATOM   2449  N  N   . LEU A  1 305 ? 38.753  -48.085 36.564  1.00 21.18 ? 322  LEU A N   1 
ATOM   2450  C  CA  . LEU A  1 305 ? 39.625  -47.675 35.469  1.00 22.30 ? 322  LEU A CA  1 
ATOM   2451  C  C   . LEU A  1 305 ? 41.038  -48.225 35.681  1.00 21.68 ? 322  LEU A C   1 
ATOM   2452  O  O   . LEU A  1 305 ? 41.713  -48.579 34.718  1.00 22.20 ? 322  LEU A O   1 
ATOM   2453  C  CB  . LEU A  1 305 ? 39.624  -46.163 35.264  1.00 22.67 ? 322  LEU A CB  1 
ATOM   2454  C  CG  . LEU A  1 305 ? 40.072  -45.684 33.879  1.00 22.76 ? 322  LEU A CG  1 
ATOM   2455  C  CD1 . LEU A  1 305 ? 39.106  -46.092 32.772  1.00 23.03 ? 322  LEU A CD1 1 
ATOM   2456  C  CD2 . LEU A  1 305 ? 40.255  -44.183 33.880  1.00 22.58 ? 322  LEU A CD2 1 
ATOM   2457  N  N   . ILE A  1 306 ? 41.485  -48.316 36.936  1.00 21.37 ? 323  ILE A N   1 
ATOM   2458  C  CA  . ILE A  1 306 ? 42.764  -48.952 37.237  1.00 21.48 ? 323  ILE A CA  1 
ATOM   2459  C  C   . ILE A  1 306 ? 42.750  -50.383 36.697  1.00 20.95 ? 323  ILE A C   1 
ATOM   2460  O  O   . ILE A  1 306 ? 43.723  -50.830 36.095  1.00 21.83 ? 323  ILE A O   1 
ATOM   2461  C  CB  . ILE A  1 306 ? 43.078  -48.913 38.748  1.00 20.63 ? 323  ILE A CB  1 
ATOM   2462  C  CG1 . ILE A  1 306 ? 43.353  -47.480 39.224  1.00 20.48 ? 323  ILE A CG1 1 
ATOM   2463  C  CG2 . ILE A  1 306 ? 44.243  -49.848 39.093  1.00 19.84 ? 323  ILE A CG2 1 
ATOM   2464  C  CD1 . ILE A  1 306 ? 43.420  -47.325 40.732  1.00 20.75 ? 323  ILE A CD1 1 
ATOM   2465  N  N   . VAL A  1 307 ? 41.649  -51.099 36.937  1.00 20.92 ? 324  VAL A N   1 
ATOM   2466  C  CA  . VAL A  1 307 ? 41.520  -52.490 36.534  1.00 21.80 ? 324  VAL A CA  1 
ATOM   2467  C  C   . VAL A  1 307 ? 41.610  -52.606 35.013  1.00 22.49 ? 324  VAL A C   1 
ATOM   2468  O  O   . VAL A  1 307 ? 42.269  -53.510 34.506  1.00 22.19 ? 324  VAL A O   1 
ATOM   2469  C  CB  . VAL A  1 307 ? 40.223  -53.105 37.089  1.00 22.08 ? 324  VAL A CB  1 
ATOM   2470  C  CG1 . VAL A  1 307 ? 39.882  -54.446 36.450  1.00 22.26 ? 324  VAL A CG1 1 
ATOM   2471  C  CG2 . VAL A  1 307 ? 40.296  -53.252 38.601  1.00 22.65 ? 324  VAL A CG2 1 
ATOM   2472  N  N   . MET A  1 308 ? 40.965  -51.689 34.284  1.00 22.41 ? 325  MET A N   1 
ATOM   2473  C  CA  . MET A  1 308 ? 41.036  -51.718 32.832  1.00 24.14 ? 325  MET A CA  1 
ATOM   2474  C  C   . MET A  1 308 ? 42.482  -51.553 32.373  1.00 24.06 ? 325  MET A C   1 
ATOM   2475  O  O   . MET A  1 308 ? 42.910  -52.229 31.444  1.00 24.92 ? 325  MET A O   1 
ATOM   2476  C  CB  . MET A  1 308 ? 40.167  -50.630 32.195  1.00 24.96 ? 325  MET A CB  1 
ATOM   2477  C  CG  . MET A  1 308 ? 38.693  -50.930 32.256  1.00 26.82 ? 325  MET A CG  1 
ATOM   2478  S  SD  . MET A  1 308 ? 37.708  -49.626 31.492  1.00 31.52 ? 325  MET A SD  1 
ATOM   2479  C  CE  . MET A  1 308 ? 38.439  -49.565 29.850  1.00 31.18 ? 325  MET A CE  1 
ATOM   2480  N  N   . SER A  1 309 ? 43.228  -50.668 33.043  1.00 24.22 ? 326  SER A N   1 
ATOM   2481  C  CA  . SER A  1 309 ? 44.631  -50.446 32.731  1.00 24.36 ? 326  SER A CA  1 
ATOM   2482  C  C   . SER A  1 309 ? 45.451  -51.713 32.991  1.00 25.48 ? 326  SER A C   1 
ATOM   2483  O  O   . SER A  1 309 ? 46.336  -52.045 32.205  1.00 25.82 ? 326  SER A O   1 
ATOM   2484  C  CB  . SER A  1 309 ? 45.169  -49.271 33.516  1.00 24.69 ? 326  SER A CB  1 
ATOM   2485  O  OG  . SER A  1 309 ? 46.559  -49.069 33.283  1.00 24.66 ? 326  SER A OG  1 
ATOM   2486  N  N   . MET A  1 310 ? 45.167  -52.395 34.109  1.00 25.16 ? 327  MET A N   1 
ATOM   2487  C  CA  . MET A  1 310 ? 45.932  -53.560 34.534  1.00 26.39 ? 327  MET A CA  1 
ATOM   2488  C  C   . MET A  1 310 ? 45.682  -54.735 33.589  1.00 27.79 ? 327  MET A C   1 
ATOM   2489  O  O   . MET A  1 310 ? 46.590  -55.525 33.323  1.00 28.87 ? 327  MET A O   1 
ATOM   2490  C  CB  . MET A  1 310 ? 45.554  -53.979 35.958  1.00 26.25 ? 327  MET A CB  1 
ATOM   2491  C  CG  . MET A  1 310 ? 46.073  -53.050 37.038  1.00 27.62 ? 327  MET A CG  1 
ATOM   2492  S  SD  . MET A  1 310 ? 45.624  -53.617 38.690  1.00 29.54 ? 327  MET A SD  1 
ATOM   2493  C  CE  . MET A  1 310 ? 46.705  -52.601 39.707  1.00 31.00 ? 327  MET A CE  1 
ATOM   2494  N  N   . VAL A  1 311 ? 44.436  -54.857 33.117  1.00 26.86 ? 328  VAL A N   1 
ATOM   2495  C  CA  . VAL A  1 311 ? 44.040  -55.917 32.202  1.00 29.04 ? 328  VAL A CA  1 
ATOM   2496  C  C   . VAL A  1 311 ? 44.760  -55.735 30.867  1.00 30.61 ? 328  VAL A C   1 
ATOM   2497  O  O   . VAL A  1 311 ? 45.168  -56.710 30.241  1.00 32.54 ? 328  VAL A O   1 
ATOM   2498  C  CB  . VAL A  1 311 ? 42.508  -55.952 32.033  1.00 28.91 ? 328  VAL A CB  1 
ATOM   2499  C  CG1 . VAL A  1 311 ? 42.069  -56.733 30.799  1.00 30.22 ? 328  VAL A CG1 1 
ATOM   2500  C  CG2 . VAL A  1 311 ? 41.831  -56.501 33.282  1.00 29.05 ? 328  VAL A CG2 1 
ATOM   2501  N  N   . GLU A  1 312 ? 44.936  -54.478 30.457  1.00 31.47 ? 329  GLU A N   1 
ATOM   2502  C  CA  . GLU A  1 312 ? 45.639  -54.148 29.228  1.00 34.84 ? 329  GLU A CA  1 
ATOM   2503  C  C   . GLU A  1 312 ? 47.128  -54.495 29.329  1.00 35.29 ? 329  GLU A C   1 
ATOM   2504  O  O   . GLU A  1 312 ? 47.804  -54.598 28.307  1.00 32.99 ? 329  GLU A O   1 
ATOM   2505  C  CB  . GLU A  1 312 ? 45.411  -52.658 28.980  1.00 38.05 ? 329  GLU A CB  1 
ATOM   2506  C  CG  . GLU A  1 312 ? 45.774  -52.190 27.577  1.00 42.01 ? 329  GLU A CG  1 
ATOM   2507  C  CD  . GLU A  1 312 ? 45.334  -50.759 27.338  1.00 42.16 ? 329  GLU A CD  1 
ATOM   2508  O  OE1 . GLU A  1 312 ? 44.467  -50.548 26.465  1.00 46.36 ? 329  GLU A OE1 1 
ATOM   2509  O  OE2 . GLU A  1 312 ? 45.849  -49.861 28.035  1.00 43.48 ? 329  GLU A OE2 1 
ATOM   2510  N  N   . ASN A  1 313 ? 47.638  -54.652 30.560  1.00 35.67 ? 330  ASN A N   1 
ATOM   2511  C  CA  . ASN A  1 313 ? 49.052  -54.900 30.804  1.00 36.42 ? 330  ASN A CA  1 
ATOM   2512  C  C   . ASN A  1 313 ? 49.289  -56.316 31.329  1.00 37.06 ? 330  ASN A C   1 
ATOM   2513  O  O   . ASN A  1 313 ? 50.327  -56.581 31.934  1.00 39.28 ? 330  ASN A O   1 
ATOM   2514  C  CB  . ASN A  1 313 ? 49.621  -53.836 31.737  1.00 36.03 ? 330  ASN A CB  1 
ATOM   2515  C  CG  . ASN A  1 313 ? 49.756  -52.512 31.030  1.00 37.38 ? 330  ASN A CG  1 
ATOM   2516  O  OD1 . ASN A  1 313 ? 50.736  -52.296 30.310  1.00 39.31 ? 330  ASN A OD1 1 
ATOM   2517  N  ND2 . ASN A  1 313 ? 48.784  -51.627 31.197  1.00 37.45 ? 330  ASN A ND2 1 
ATOM   2518  N  N   . GLY A  1 314 ? 48.330  -57.225 31.107  1.00 37.73 ? 331  GLY A N   1 
ATOM   2519  C  CA  . GLY A  1 314 ? 48.601  -58.652 31.202  1.00 37.89 ? 331  GLY A CA  1 
ATOM   2520  C  C   . GLY A  1 314 ? 47.851  -59.356 32.330  1.00 37.93 ? 331  GLY A C   1 
ATOM   2521  O  O   . GLY A  1 314 ? 47.826  -60.584 32.365  1.00 38.73 ? 331  GLY A O   1 
ATOM   2522  N  N   . LEU A  1 315 ? 47.254  -58.603 33.260  1.00 35.98 ? 332  LEU A N   1 
ATOM   2523  C  CA  . LEU A  1 315 ? 46.536  -59.226 34.360  1.00 34.87 ? 332  LEU A CA  1 
ATOM   2524  C  C   . LEU A  1 315 ? 45.143  -59.627 33.886  1.00 34.77 ? 332  LEU A C   1 
ATOM   2525  O  O   . LEU A  1 315 ? 44.593  -59.002 32.985  1.00 37.25 ? 332  LEU A O   1 
ATOM   2526  C  CB  . LEU A  1 315 ? 46.475  -58.302 35.576  1.00 34.29 ? 332  LEU A CB  1 
ATOM   2527  C  CG  . LEU A  1 315 ? 47.802  -58.044 36.298  1.00 34.55 ? 332  LEU A CG  1 
ATOM   2528  C  CD1 . LEU A  1 315 ? 47.579  -57.157 37.509  1.00 35.06 ? 332  LEU A CD1 1 
ATOM   2529  C  CD2 . LEU A  1 315 ? 48.494  -59.329 36.729  1.00 35.16 ? 332  LEU A CD2 1 
ATOM   2530  N  N   . SER A  1 316 ? 44.598  -60.693 34.482  1.00 33.85 ? 333  SER A N   1 
ATOM   2531  C  CA  . SER A  1 316 ? 43.179  -60.988 34.371  1.00 34.09 ? 333  SER A CA  1 
ATOM   2532  C  C   . SER A  1 316 ? 42.398  -59.963 35.191  1.00 32.59 ? 333  SER A C   1 
ATOM   2533  O  O   . SER A  1 316 ? 42.950  -59.334 36.091  1.00 32.37 ? 333  SER A O   1 
ATOM   2534  C  CB  . SER A  1 316 ? 42.865  -62.398 34.815  1.00 33.92 ? 333  SER A CB  1 
ATOM   2535  O  OG  . SER A  1 316 ? 42.920  -62.523 36.230  1.00 35.49 ? 333  SER A OG  1 
ATOM   2536  N  N   . GLU A  1 317 ? 41.110  -59.805 34.877  1.00 32.35 ? 334  GLU A N   1 
ATOM   2537  C  CA  . GLU A  1 317 ? 40.258  -58.877 35.600  1.00 33.90 ? 334  GLU A CA  1 
ATOM   2538  C  C   . GLU A  1 317 ? 40.227  -59.252 37.084  1.00 32.19 ? 334  GLU A C   1 
ATOM   2539  O  O   . GLU A  1 317 ? 40.400  -58.390 37.944  1.00 28.02 ? 334  GLU A O   1 
ATOM   2540  C  CB  . GLU A  1 317 ? 38.871  -58.853 34.958  1.00 37.13 ? 334  GLU A CB  1 
ATOM   2541  C  CG  . GLU A  1 317 ? 37.887  -57.915 35.649  1.00 39.04 ? 334  GLU A CG  1 
ATOM   2542  C  CD  . GLU A  1 317 ? 36.613  -57.695 34.854  1.00 43.34 ? 334  GLU A CD  1 
ATOM   2543  O  OE1 . GLU A  1 317 ? 36.712  -57.145 33.735  1.00 44.92 ? 334  GLU A OE1 1 
ATOM   2544  O  OE2 . GLU A  1 317 ? 35.527  -58.070 35.349  1.00 46.30 ? 334  GLU A OE2 1 
ATOM   2545  N  N   . GLN A  1 318 ? 40.036  -60.547 37.371  1.00 31.32 ? 335  GLN A N   1 
ATOM   2546  C  CA  . GLN A  1 318 ? 39.928  -61.034 38.737  1.00 31.73 ? 335  GLN A CA  1 
ATOM   2547  C  C   . GLN A  1 318 ? 41.214  -60.750 39.513  1.00 32.08 ? 335  GLN A C   1 
ATOM   2548  O  O   . GLN A  1 318 ? 41.153  -60.382 40.687  1.00 29.84 ? 335  GLN A O   1 
ATOM   2549  C  CB  . GLN A  1 318 ? 39.605  -62.529 38.781  1.00 32.01 ? 335  GLN A CB  1 
ATOM   2550  N  N   . GLU A  1 319 ? 42.371  -60.919 38.859  1.00 32.16 ? 336  GLU A N   1 
ATOM   2551  C  CA  . GLU A  1 319 ? 43.647  -60.713 39.525  1.00 34.82 ? 336  GLU A CA  1 
ATOM   2552  C  C   . GLU A  1 319 ? 43.898  -59.221 39.737  1.00 31.75 ? 336  GLU A C   1 
ATOM   2553  O  O   . GLU A  1 319 ? 44.476  -58.842 40.753  1.00 30.34 ? 336  GLU A O   1 
ATOM   2554  C  CB  . GLU A  1 319 ? 44.813  -61.376 38.789  1.00 39.42 ? 336  GLU A CB  1 
ATOM   2555  C  CG  . GLU A  1 319 ? 44.839  -62.897 38.933  1.00 45.38 ? 336  GLU A CG  1 
ATOM   2556  C  CD  . GLU A  1 319 ? 44.754  -63.436 40.354  1.00 50.94 ? 336  GLU A CD  1 
ATOM   2557  O  OE1 . GLU A  1 319 ? 45.614  -63.079 41.192  1.00 54.17 ? 336  GLU A OE1 1 
ATOM   2558  O  OE2 . GLU A  1 319 ? 43.818  -64.224 40.620  1.00 56.56 ? 336  GLU A OE2 1 
ATOM   2559  N  N   . ALA A  1 320 ? 43.477  -58.386 38.776  1.00 28.19 ? 337  ALA A N   1 
ATOM   2560  C  CA  . ALA A  1 320 ? 43.583  -56.940 38.912  1.00 25.93 ? 337  ALA A CA  1 
ATOM   2561  C  C   . ALA A  1 320 ? 42.760  -56.458 40.108  1.00 23.60 ? 337  ALA A C   1 
ATOM   2562  O  O   . ALA A  1 320 ? 43.245  -55.678 40.923  1.00 22.62 ? 337  ALA A O   1 
ATOM   2563  C  CB  . ALA A  1 320 ? 43.145  -56.269 37.626  1.00 25.18 ? 337  ALA A CB  1 
ATOM   2564  N  N   . GLN A  1 321 ? 41.516  -56.939 40.207  1.00 24.71 ? 338  GLN A N   1 
ATOM   2565  C  CA  . GLN A  1 321 ? 40.619  -56.571 41.293  1.00 25.65 ? 338  GLN A CA  1 
ATOM   2566  C  C   . GLN A  1 321 ? 41.208  -56.960 42.650  1.00 26.01 ? 338  GLN A C   1 
ATOM   2567  O  O   . GLN A  1 321 ? 41.057  -56.214 43.615  1.00 24.26 ? 338  GLN A O   1 
ATOM   2568  C  CB  . GLN A  1 321 ? 39.235  -57.170 41.049  1.00 26.83 ? 338  GLN A CB  1 
ATOM   2569  C  CG  . GLN A  1 321 ? 38.507  -56.532 39.871  1.00 26.72 ? 338  GLN A CG  1 
ATOM   2570  C  CD  . GLN A  1 321 ? 37.209  -57.216 39.500  1.00 28.45 ? 338  GLN A CD  1 
ATOM   2571  O  OE1 . GLN A  1 321 ? 36.939  -58.360 39.883  1.00 28.04 ? 338  GLN A OE1 1 
ATOM   2572  N  NE2 . GLN A  1 321 ? 36.387  -56.509 38.737  1.00 28.31 ? 338  GLN A NE2 1 
ATOM   2573  N  N   . LYS A  1 322 ? 41.923  -58.093 42.708  1.00 27.99 ? 339  LYS A N   1 
ATOM   2574  C  CA  . LYS A  1 322 ? 42.536  -58.563 43.945  1.00 30.30 ? 339  LYS A CA  1 
ATOM   2575  C  C   . LYS A  1 322 ? 43.645  -57.633 44.442  1.00 28.28 ? 339  LYS A C   1 
ATOM   2576  O  O   . LYS A  1 322 ? 44.046  -57.743 45.596  1.00 27.53 ? 339  LYS A O   1 
ATOM   2577  C  CB  . LYS A  1 322 ? 43.140  -59.967 43.808  1.00 33.89 ? 339  LYS A CB  1 
ATOM   2578  C  CG  . LYS A  1 322 ? 42.143  -61.107 43.875  1.00 39.04 ? 339  LYS A CG  1 
ATOM   2579  C  CD  . LYS A  1 322 ? 42.785  -62.477 44.074  1.00 44.18 ? 339  LYS A CD  1 
ATOM   2580  C  CE  . LYS A  1 322 ? 41.763  -63.564 44.224  1.00 48.11 ? 339  LYS A CE  1 
ATOM   2581  N  NZ  . LYS A  1 322 ? 42.396  -64.873 44.412  1.00 50.73 ? 339  LYS A NZ  1 
ATOM   2582  N  N   . LYS A  1 323 ? 44.152  -56.734 43.589  1.00 26.96 ? 340  LYS A N   1 
ATOM   2583  C  CA  . LYS A  1 323 ? 45.212  -55.817 43.988  1.00 26.22 ? 340  LYS A CA  1 
ATOM   2584  C  C   . LYS A  1 323 ? 44.652  -54.583 44.699  1.00 24.18 ? 340  LYS A C   1 
ATOM   2585  O  O   . LYS A  1 323 ? 45.425  -53.751 45.167  1.00 23.65 ? 340  LYS A O   1 
ATOM   2586  C  CB  . LYS A  1 323 ? 46.018  -55.346 42.771  1.00 29.39 ? 340  LYS A CB  1 
ATOM   2587  C  CG  . LYS A  1 323 ? 46.624  -56.439 41.897  1.00 32.85 ? 340  LYS A CG  1 
ATOM   2588  C  CD  . LYS A  1 323 ? 47.657  -57.316 42.589  1.00 36.04 ? 340  LYS A CD  1 
ATOM   2589  C  CE  . LYS A  1 323 ? 48.069  -58.513 41.775  1.00 39.35 ? 340  LYS A CE  1 
ATOM   2590  N  NZ  . LYS A  1 323 ? 47.048  -59.568 41.795  1.00 41.21 ? 340  LYS A NZ  1 
ATOM   2591  N  N   . ILE A  1 324 ? 43.317  -54.458 44.771  1.00 22.93 ? 341  ILE A N   1 
ATOM   2592  C  CA  . ILE A  1 324 ? 42.666  -53.252 45.264  1.00 21.71 ? 341  ILE A CA  1 
ATOM   2593  C  C   . ILE A  1 324 ? 41.824  -53.577 46.498  1.00 20.43 ? 341  ILE A C   1 
ATOM   2594  O  O   . ILE A  1 324 ? 40.964  -54.451 46.452  1.00 20.35 ? 341  ILE A O   1 
ATOM   2595  C  CB  . ILE A  1 324 ? 41.818  -52.606 44.150  1.00 22.19 ? 341  ILE A CB  1 
ATOM   2596  C  CG1 . ILE A  1 324 ? 42.701  -52.110 43.005  1.00 22.39 ? 341  ILE A CG1 1 
ATOM   2597  C  CG2 . ILE A  1 324 ? 40.942  -51.483 44.710  1.00 21.71 ? 341  ILE A CG2 1 
ATOM   2598  C  CD1 . ILE A  1 324 ? 41.960  -51.775 41.725  1.00 23.02 ? 341  ILE A CD1 1 
ATOM   2599  N  N   . TRP A  1 325 ? 42.065  -52.825 47.580  1.00 20.68 ? 342  TRP A N   1 
ATOM   2600  C  CA  . TRP A  1 325 ? 41.314  -52.922 48.822  1.00 20.97 ? 342  TRP A CA  1 
ATOM   2601  C  C   . TRP A  1 325 ? 40.645  -51.585 49.129  1.00 21.47 ? 342  TRP A C   1 
ATOM   2602  O  O   . TRP A  1 325 ? 41.112  -50.538 48.681  1.00 21.38 ? 342  TRP A O   1 
ATOM   2603  C  CB  . TRP A  1 325 ? 42.240  -53.304 49.979  1.00 21.97 ? 342  TRP A CB  1 
ATOM   2604  C  CG  . TRP A  1 325 ? 42.883  -54.657 49.849  1.00 23.54 ? 342  TRP A CG  1 
ATOM   2605  C  CD1 . TRP A  1 325 ? 43.896  -55.015 49.008  1.00 24.61 ? 342  TRP A CD1 1 
ATOM   2606  C  CD2 . TRP A  1 325 ? 42.580  -55.825 50.640  1.00 24.37 ? 342  TRP A CD2 1 
ATOM   2607  N  NE1 . TRP A  1 325 ? 44.231  -56.329 49.209  1.00 25.28 ? 342  TRP A NE1 1 
ATOM   2608  C  CE2 . TRP A  1 325 ? 43.442  -56.852 50.200  1.00 25.34 ? 342  TRP A CE2 1 
ATOM   2609  C  CE3 . TRP A  1 325 ? 41.660  -56.104 51.657  1.00 24.65 ? 342  TRP A CE3 1 
ATOM   2610  C  CZ2 . TRP A  1 325 ? 43.412  -58.133 50.752  1.00 26.24 ? 342  TRP A CZ2 1 
ATOM   2611  C  CZ3 . TRP A  1 325 ? 41.630  -57.370 52.202  1.00 25.53 ? 342  TRP A CZ3 1 
ATOM   2612  C  CH2 . TRP A  1 325 ? 42.497  -58.367 51.756  1.00 25.64 ? 342  TRP A CH2 1 
ATOM   2613  N  N   . MET A  1 326 ? 39.574  -51.628 49.933  1.00 20.33 ? 343  MET A N   1 
ATOM   2614  C  CA  . MET A  1 326 ? 38.842  -50.422 50.280  1.00 20.64 ? 343  MET A CA  1 
ATOM   2615  C  C   . MET A  1 326 ? 38.460  -50.442 51.758  1.00 21.39 ? 343  MET A C   1 
ATOM   2616  O  O   . MET A  1 326 ? 38.119  -51.489 52.303  1.00 21.90 ? 343  MET A O   1 
ATOM   2617  C  CB  . MET A  1 326 ? 37.595  -50.284 49.403  1.00 20.94 ? 343  MET A CB  1 
ATOM   2618  C  CG  . MET A  1 326 ? 37.914  -50.179 47.931  1.00 21.67 ? 343  MET A CG  1 
ATOM   2619  S  SD  . MET A  1 326 ? 36.478  -49.744 46.935  1.00 22.78 ? 343  MET A SD  1 
ATOM   2620  C  CE  . MET A  1 326 ? 37.244  -49.591 45.316  1.00 22.71 ? 343  MET A CE  1 
ATOM   2621  N  N   . PHE A  1 327 ? 38.516  -49.257 52.377  1.00 21.99 ? 344  PHE A N   1 
ATOM   2622  C  CA  . PHE A  1 327 ? 38.222  -49.063 53.788  1.00 22.44 ? 344  PHE A CA  1 
ATOM   2623  C  C   . PHE A  1 327 ? 37.250  -47.892 53.918  1.00 22.70 ? 344  PHE A C   1 
ATOM   2624  O  O   . PHE A  1 327 ? 37.637  -46.755 53.668  1.00 22.33 ? 344  PHE A O   1 
ATOM   2625  C  CB  . PHE A  1 327 ? 39.550  -48.806 54.509  1.00 23.49 ? 344  PHE A CB  1 
ATOM   2626  C  CG  . PHE A  1 327 ? 39.489  -48.715 56.029  1.00 24.90 ? 344  PHE A CG  1 
ATOM   2627  C  CD1 . PHE A  1 327 ? 39.021  -47.567 56.661  1.00 25.89 ? 344  PHE A CD1 1 
ATOM   2628  C  CD2 . PHE A  1 327 ? 39.939  -49.764 56.827  1.00 26.35 ? 344  PHE A CD2 1 
ATOM   2629  C  CE1 . PHE A  1 327 ? 38.992  -47.476 58.045  1.00 26.52 ? 344  PHE A CE1 1 
ATOM   2630  C  CE2 . PHE A  1 327 ? 39.900  -49.669 58.212  1.00 26.53 ? 344  PHE A CE2 1 
ATOM   2631  C  CZ  . PHE A  1 327 ? 39.423  -48.528 58.817  1.00 26.21 ? 344  PHE A CZ  1 
ATOM   2632  N  N   . ASP A  1 328 ? 35.997  -48.179 54.305  1.00 22.03 ? 345  ASP A N   1 
ATOM   2633  C  CA  . ASP A  1 328 ? 34.950  -47.168 54.352  1.00 22.91 ? 345  ASP A CA  1 
ATOM   2634  C  C   . ASP A  1 328 ? 34.703  -46.765 55.807  1.00 24.32 ? 345  ASP A C   1 
ATOM   2635  O  O   . ASP A  1 328 ? 35.502  -47.087 56.681  1.00 22.53 ? 345  ASP A O   1 
ATOM   2636  C  CB  . ASP A  1 328 ? 33.717  -47.638 53.595  1.00 23.08 ? 345  ASP A CB  1 
ATOM   2637  C  CG  . ASP A  1 328 ? 32.862  -48.701 54.275  1.00 23.62 ? 345  ASP A CG  1 
ATOM   2638  O  OD1 . ASP A  1 328 ? 33.236  -49.155 55.373  1.00 23.18 ? 345  ASP A OD1 1 
ATOM   2639  O  OD2 . ASP A  1 328 ? 31.826  -49.071 53.690  1.00 25.13 ? 345  ASP A OD2 1 
ATOM   2640  N  N   . LYS A  1 329 ? 33.594  -46.058 56.074  1.00 25.87 ? 346  LYS A N   1 
ATOM   2641  C  CA  . LYS A  1 329 ? 33.365  -45.502 57.400  1.00 28.37 ? 346  LYS A CA  1 
ATOM   2642  C  C   . LYS A  1 329 ? 33.157  -46.607 58.440  1.00 27.18 ? 346  LYS A C   1 
ATOM   2643  O  O   . LYS A  1 329 ? 33.280  -46.338 59.628  1.00 27.49 ? 346  LYS A O   1 
ATOM   2644  C  CB  . LYS A  1 329 ? 32.216  -44.486 57.438  1.00 31.48 ? 346  LYS A CB  1 
ATOM   2645  C  CG  . LYS A  1 329 ? 30.812  -45.004 57.191  1.00 34.85 ? 346  LYS A CG  1 
ATOM   2646  C  CD  . LYS A  1 329 ? 29.783  -43.892 57.375  1.00 38.87 ? 346  LYS A CD  1 
ATOM   2647  C  CE  . LYS A  1 329 ? 28.427  -44.231 56.852  1.00 42.73 ? 346  LYS A CE  1 
ATOM   2648  N  NZ  . LYS A  1 329 ? 27.517  -43.085 56.941  1.00 45.10 ? 346  LYS A NZ  1 
ATOM   2649  N  N   . TYR A  1 330 ? 32.867  -47.840 57.999  1.00 28.53 ? 347  TYR A N   1 
ATOM   2650  C  CA  . TYR A  1 330 ? 32.673  -48.965 58.907  1.00 30.50 ? 347  TYR A CA  1 
ATOM   2651  C  C   . TYR A  1 330 ? 33.932  -49.822 59.036  1.00 29.32 ? 347  TYR A C   1 
ATOM   2652  O  O   . TYR A  1 330 ? 33.995  -50.676 59.915  1.00 30.63 ? 347  TYR A O   1 
ATOM   2653  C  CB  . TYR A  1 330 ? 31.485  -49.804 58.434  1.00 32.42 ? 347  TYR A CB  1 
ATOM   2654  C  CG  . TYR A  1 330 ? 30.188  -49.008 58.383  1.00 35.76 ? 347  TYR A CG  1 
ATOM   2655  C  CD1 . TYR A  1 330 ? 29.505  -48.673 59.548  1.00 38.91 ? 347  TYR A CD1 1 
ATOM   2656  C  CD2 . TYR A  1 330 ? 29.655  -48.585 57.172  1.00 38.72 ? 347  TYR A CD2 1 
ATOM   2657  C  CE1 . TYR A  1 330 ? 28.324  -47.948 59.509  1.00 39.84 ? 347  TYR A CE1 1 
ATOM   2658  C  CE2 . TYR A  1 330 ? 28.476  -47.859 57.118  1.00 40.54 ? 347  TYR A CE2 1 
ATOM   2659  C  CZ  . TYR A  1 330 ? 27.810  -47.539 58.289  1.00 42.95 ? 347  TYR A CZ  1 
ATOM   2660  O  OH  . TYR A  1 330 ? 26.649  -46.821 58.226  1.00 45.22 ? 347  TYR A OH  1 
ATOM   2661  N  N   . GLY A  1 331 ? 34.933  -49.594 58.178  1.00 27.22 ? 348  GLY A N   1 
ATOM   2662  C  CA  . GLY A  1 331 ? 36.174  -50.349 58.227  1.00 25.94 ? 348  GLY A CA  1 
ATOM   2663  C  C   . GLY A  1 331 ? 36.473  -51.030 56.894  1.00 25.60 ? 348  GLY A C   1 
ATOM   2664  O  O   . GLY A  1 331 ? 35.901  -50.678 55.865  1.00 25.54 ? 348  GLY A O   1 
ATOM   2665  N  N   . LEU A  1 332 ? 37.377  -52.016 56.934  1.00 25.71 ? 349  LEU A N   1 
ATOM   2666  C  CA  . LEU A  1 332 ? 37.865  -52.682 55.739  1.00 25.27 ? 349  LEU A CA  1 
ATOM   2667  C  C   . LEU A  1 332 ? 36.738  -53.493 55.103  1.00 25.76 ? 349  LEU A C   1 
ATOM   2668  O  O   . LEU A  1 332 ? 35.940  -54.108 55.809  1.00 26.85 ? 349  LEU A O   1 
ATOM   2669  C  CB  . LEU A  1 332 ? 39.054  -53.562 56.124  1.00 24.93 ? 349  LEU A CB  1 
ATOM   2670  C  CG  . LEU A  1 332 ? 39.845  -54.178 54.966  1.00 24.90 ? 349  LEU A CG  1 
ATOM   2671  C  CD1 . LEU A  1 332 ? 40.538  -53.104 54.143  1.00 25.10 ? 349  LEU A CD1 1 
ATOM   2672  C  CD2 . LEU A  1 332 ? 40.868  -55.167 55.493  1.00 25.33 ? 349  LEU A CD2 1 
ATOM   2673  N  N   . LEU A  1 333 ? 36.663  -53.459 53.765  1.00 24.78 ? 350  LEU A N   1 
ATOM   2674  C  CA  . LEU A  1 333 ? 35.670  -54.225 53.031  1.00 24.91 ? 350  LEU A CA  1 
ATOM   2675  C  C   . LEU A  1 333 ? 36.162  -55.666 52.901  1.00 26.35 ? 350  LEU A C   1 
ATOM   2676  O  O   . LEU A  1 333 ? 36.991  -55.968 52.044  1.00 26.19 ? 350  LEU A O   1 
ATOM   2677  C  CB  . LEU A  1 333 ? 35.352  -53.608 51.669  1.00 24.86 ? 350  LEU A CB  1 
ATOM   2678  C  CG  . LEU A  1 333 ? 34.285  -52.505 51.663  1.00 24.58 ? 350  LEU A CG  1 
ATOM   2679  C  CD1 . LEU A  1 333 ? 34.753  -51.244 52.366  1.00 24.85 ? 350  LEU A CD1 1 
ATOM   2680  C  CD2 . LEU A  1 333 ? 33.855  -52.182 50.238  1.00 24.16 ? 350  LEU A CD2 1 
ATOM   2681  N  N   . VAL A  1 334 ? 35.645  -56.535 53.781  1.00 26.89 ? 351  VAL A N   1 
ATOM   2682  C  CA  . VAL A  1 334 ? 35.999  -57.944 53.792  1.00 28.10 ? 351  VAL A CA  1 
ATOM   2683  C  C   . VAL A  1 334 ? 34.721  -58.777 53.729  1.00 28.61 ? 351  VAL A C   1 
ATOM   2684  O  O   . VAL A  1 334 ? 33.670  -58.368 54.219  1.00 27.47 ? 351  VAL A O   1 
ATOM   2685  C  CB  . VAL A  1 334 ? 36.849  -58.331 55.020  1.00 29.31 ? 351  VAL A CB  1 
ATOM   2686  C  CG1 . VAL A  1 334 ? 38.147  -57.536 55.083  1.00 29.57 ? 351  VAL A CG1 1 
ATOM   2687  C  CG2 . VAL A  1 334 ? 36.074  -58.208 56.327  1.00 28.99 ? 351  VAL A CG2 1 
ATOM   2688  N  N   . LYS A  1 335 ? 34.834  -59.960 53.124  1.00 30.97 ? 352  LYS A N   1 
ATOM   2689  C  CA  . LYS A  1 335 ? 33.714  -60.877 53.000  1.00 32.88 ? 352  LYS A CA  1 
ATOM   2690  C  C   . LYS A  1 335 ? 33.206  -61.260 54.387  1.00 32.22 ? 352  LYS A C   1 
ATOM   2691  O  O   . LYS A  1 335 ? 33.979  -61.709 55.226  1.00 30.62 ? 352  LYS A O   1 
ATOM   2692  C  CB  . LYS A  1 335 ? 34.144  -62.119 52.213  1.00 34.36 ? 352  LYS A CB  1 
ATOM   2693  C  CG  . LYS A  1 335 ? 34.484  -61.846 50.756  1.00 37.94 ? 352  LYS A CG  1 
ATOM   2694  C  CD  . LYS A  1 335 ? 34.867  -63.088 49.961  1.00 39.69 ? 352  LYS A CD  1 
ATOM   2695  C  CE  . LYS A  1 335 ? 35.015  -62.794 48.505  1.00 42.23 ? 352  LYS A CE  1 
ATOM   2696  N  NZ  . LYS A  1 335 ? 35.321  -64.010 47.752  1.00 44.37 ? 352  LYS A NZ  1 
ATOM   2697  N  N   . GLY A  1 336 ? 31.904  -61.059 54.616  1.00 33.58 ? 353  GLY A N   1 
ATOM   2698  C  CA  . GLY A  1 336 ? 31.248  -61.539 55.821  1.00 34.96 ? 353  GLY A CA  1 
ATOM   2699  C  C   . GLY A  1 336 ? 31.249  -60.509 56.949  1.00 36.32 ? 353  GLY A C   1 
ATOM   2700  O  O   . GLY A  1 336 ? 30.889  -60.841 58.076  1.00 38.32 ? 353  GLY A O   1 
ATOM   2701  N  N   . ARG A  1 337 ? 31.642  -59.263 56.653  1.00 35.22 ? 354  ARG A N   1 
ATOM   2702  C  CA  . ARG A  1 337 ? 31.602  -58.209 57.655  1.00 34.44 ? 354  ARG A CA  1 
ATOM   2703  C  C   . ARG A  1 337 ? 30.145  -57.827 57.917  1.00 35.42 ? 354  ARG A C   1 
ATOM   2704  O  O   . ARG A  1 337 ? 29.273  -58.089 57.092  1.00 36.47 ? 354  ARG A O   1 
ATOM   2705  C  CB  . ARG A  1 337 ? 32.434  -56.997 57.222  1.00 33.94 ? 354  ARG A CB  1 
ATOM   2706  C  CG  . ARG A  1 337 ? 31.787  -56.129 56.152  1.00 32.57 ? 354  ARG A CG  1 
ATOM   2707  C  CD  . ARG A  1 337 ? 32.457  -54.766 56.038  1.00 31.21 ? 354  ARG A CD  1 
ATOM   2708  N  NE  . ARG A  1 337 ? 31.608  -53.804 55.326  1.00 31.01 ? 354  ARG A NE  1 
ATOM   2709  C  CZ  . ARG A  1 337 ? 31.902  -52.529 55.101  1.00 29.66 ? 354  ARG A CZ  1 
ATOM   2710  N  NH1 . ARG A  1 337 ? 33.071  -52.036 55.475  1.00 30.23 ? 354  ARG A NH1 1 
ATOM   2711  N  NH2 . ARG A  1 337 ? 31.019  -51.751 54.499  1.00 29.98 ? 354  ARG A NH2 1 
ATOM   2712  N  N   . LYS A  1 338 ? 29.905  -57.185 59.063  1.00 37.06 ? 355  LYS A N   1 
ATOM   2713  C  CA  . LYS A  1 338 ? 28.566  -56.840 59.515  1.00 40.47 ? 355  LYS A CA  1 
ATOM   2714  C  C   . LYS A  1 338 ? 27.937  -55.780 58.610  1.00 39.06 ? 355  LYS A C   1 
ATOM   2715  O  O   . LYS A  1 338 ? 26.786  -55.918 58.202  1.00 39.20 ? 355  LYS A O   1 
ATOM   2716  C  CB  . LYS A  1 338 ? 28.634  -56.333 60.961  1.00 45.25 ? 355  LYS A CB  1 
ATOM   2717  C  CG  . LYS A  1 338 ? 27.347  -55.732 61.530  1.00 50.02 ? 355  LYS A CG  1 
ATOM   2718  C  CD  . LYS A  1 338 ? 27.514  -55.032 62.876  1.00 53.87 ? 355  LYS A CD  1 
ATOM   2719  C  CE  . LYS A  1 338 ? 28.016  -55.924 63.973  1.00 56.82 ? 355  LYS A CE  1 
ATOM   2720  N  NZ  . LYS A  1 338 ? 27.108  -57.042 64.253  1.00 59.00 ? 355  LYS A NZ  1 
ATOM   2721  N  N   . ALA A  1 339 ? 28.684  -54.704 58.333  1.00 37.91 ? 356  ALA A N   1 
ATOM   2722  C  CA  . ALA A  1 339 ? 28.157  -53.574 57.583  1.00 35.85 ? 356  ALA A CA  1 
ATOM   2723  C  C   . ALA A  1 339 ? 27.942  -53.967 56.125  1.00 34.22 ? 356  ALA A C   1 
ATOM   2724  O  O   . ALA A  1 339 ? 28.758  -54.671 55.539  1.00 34.15 ? 356  ALA A O   1 
ATOM   2725  C  CB  . ALA A  1 339 ? 29.093  -52.392 57.706  1.00 36.28 ? 356  ALA A CB  1 
ATOM   2726  N  N   . LYS A  1 340 ? 26.842  -53.481 55.544  1.00 34.51 ? 357  LYS A N   1 
ATOM   2727  C  CA  . LYS A  1 340 ? 26.457  -53.829 54.188  1.00 34.90 ? 357  LYS A CA  1 
ATOM   2728  C  C   . LYS A  1 340 ? 27.602  -53.554 53.211  1.00 32.50 ? 357  LYS A C   1 
ATOM   2729  O  O   . LYS A  1 340 ? 28.303  -52.552 53.326  1.00 30.80 ? 357  LYS A O   1 
ATOM   2730  C  CB  . LYS A  1 340 ? 25.220  -53.025 53.774  1.00 38.45 ? 357  LYS A CB  1 
ATOM   2731  C  CG  . LYS A  1 340 ? 24.669  -53.355 52.392  1.00 41.51 ? 357  LYS A CG  1 
ATOM   2732  C  CD  . LYS A  1 340 ? 23.452  -52.522 52.008  1.00 44.92 ? 357  LYS A CD  1 
ATOM   2733  C  CE  . LYS A  1 340 ? 22.767  -53.045 50.787  1.00 48.69 ? 357  LYS A CE  1 
ATOM   2734  N  NZ  . LYS A  1 340 ? 23.603  -52.965 49.588  1.00 50.26 ? 357  LYS A NZ  1 
ATOM   2735  N  N   . ILE A  1 341 ? 27.767  -54.474 52.257  1.00 30.30 ? 358  ILE A N   1 
ATOM   2736  C  CA  . ILE A  1 341 ? 28.575  -54.265 51.068  1.00 31.07 ? 358  ILE A CA  1 
ATOM   2737  C  C   . ILE A  1 341 ? 27.652  -54.443 49.865  1.00 30.35 ? 358  ILE A C   1 
ATOM   2738  O  O   . ILE A  1 341 ? 27.021  -55.486 49.720  1.00 28.68 ? 358  ILE A O   1 
ATOM   2739  C  CB  . ILE A  1 341 ? 29.774  -55.235 51.053  1.00 31.97 ? 358  ILE A CB  1 
ATOM   2740  C  CG1 . ILE A  1 341 ? 30.751  -54.903 52.189  1.00 32.37 ? 358  ILE A CG1 1 
ATOM   2741  C  CG2 . ILE A  1 341 ? 30.470  -55.256 49.690  1.00 31.90 ? 358  ILE A CG2 1 
ATOM   2742  C  CD1 . ILE A  1 341 ? 31.989  -55.778 52.239  1.00 32.70 ? 358  ILE A CD1 1 
ATOM   2743  N  N   . ASP A  1 342 ? 27.561  -53.415 49.015  1.00 30.30 ? 359  ASP A N   1 
ATOM   2744  C  CA  . ASP A  1 342 ? 26.641  -53.447 47.890  1.00 31.21 ? 359  ASP A CA  1 
ATOM   2745  C  C   . ASP A  1 342 ? 27.312  -54.151 46.716  1.00 31.39 ? 359  ASP A C   1 
ATOM   2746  O  O   . ASP A  1 342 ? 28.514  -54.425 46.750  1.00 32.17 ? 359  ASP A O   1 
ATOM   2747  C  CB  . ASP A  1 342 ? 26.083  -52.065 47.581  1.00 33.75 ? 359  ASP A CB  1 
ATOM   2748  C  CG  . ASP A  1 342 ? 26.866  -51.190 46.610  1.00 35.00 ? 359  ASP A CG  1 
ATOM   2749  O  OD1 . ASP A  1 342 ? 28.025  -51.523 46.296  1.00 37.23 ? 359  ASP A OD1 1 
ATOM   2750  O  OD2 . ASP A  1 342 ? 26.288  -50.192 46.145  1.00 38.53 ? 359  ASP A OD2 1 
ATOM   2751  N  N   . SER A  1 343 ? 26.517  -54.414 45.673  1.00 31.03 ? 360  SER A N   1 
ATOM   2752  C  CA  . SER A  1 343 ? 26.932  -55.258 44.564  1.00 30.77 ? 360  SER A CA  1 
ATOM   2753  C  C   . SER A  1 343 ? 28.094  -54.634 43.789  1.00 29.54 ? 360  SER A C   1 
ATOM   2754  O  O   . SER A  1 343 ? 28.879  -55.360 43.183  1.00 29.35 ? 360  SER A O   1 
ATOM   2755  C  CB  . SER A  1 343 ? 25.761  -55.572 43.655  1.00 32.00 ? 360  SER A CB  1 
ATOM   2756  O  OG  . SER A  1 343 ? 25.195  -54.396 43.087  1.00 33.69 ? 360  SER A OG  1 
ATOM   2757  N  N   . TYR A  1 344 ? 28.192  -53.295 43.800  1.00 26.65 ? 361  TYR A N   1 
ATOM   2758  C  CA  . TYR A  1 344 ? 29.250  -52.600 43.079  1.00 26.05 ? 361  TYR A CA  1 
ATOM   2759  C  C   . TYR A  1 344 ? 30.567  -52.660 43.847  1.00 23.95 ? 361  TYR A C   1 
ATOM   2760  O  O   . TYR A  1 344 ? 31.628  -52.550 43.240  1.00 23.95 ? 361  TYR A O   1 
ATOM   2761  C  CB  . TYR A  1 344 ? 28.817  -51.158 42.803  1.00 26.89 ? 361  TYR A CB  1 
ATOM   2762  C  CG  . TYR A  1 344 ? 27.617  -51.089 41.872  1.00 26.80 ? 361  TYR A CG  1 
ATOM   2763  C  CD1 . TYR A  1 344 ? 27.773  -51.217 40.497  1.00 27.12 ? 361  TYR A CD1 1 
ATOM   2764  C  CD2 . TYR A  1 344 ? 26.328  -50.931 42.369  1.00 28.32 ? 361  TYR A CD2 1 
ATOM   2765  C  CE1 . TYR A  1 344 ? 26.686  -51.172 39.640  1.00 27.48 ? 361  TYR A CE1 1 
ATOM   2766  C  CE2 . TYR A  1 344 ? 25.230  -50.889 41.523  1.00 27.59 ? 361  TYR A CE2 1 
ATOM   2767  C  CZ  . TYR A  1 344 ? 25.412  -51.010 40.157  1.00 28.09 ? 361  TYR A CZ  1 
ATOM   2768  O  OH  . TYR A  1 344 ? 24.345  -50.969 39.308  1.00 29.39 ? 361  TYR A OH  1 
ATOM   2769  N  N   . GLN A  1 345 ? 30.495  -52.834 45.173  1.00 23.35 ? 362  GLN A N   1 
ATOM   2770  C  CA  . GLN A  1 345 ? 31.680  -52.874 46.016  1.00 24.67 ? 362  GLN A CA  1 
ATOM   2771  C  C   . GLN A  1 345 ? 32.242  -54.295 46.093  1.00 25.89 ? 362  GLN A C   1 
ATOM   2772  O  O   . GLN A  1 345 ? 33.397  -54.474 46.476  1.00 25.46 ? 362  GLN A O   1 
ATOM   2773  C  CB  . GLN A  1 345 ? 31.354  -52.362 47.420  1.00 24.69 ? 362  GLN A CB  1 
ATOM   2774  C  CG  . GLN A  1 345 ? 30.947  -50.891 47.484  1.00 24.58 ? 362  GLN A CG  1 
ATOM   2775  C  CD  . GLN A  1 345 ? 30.388  -50.494 48.833  1.00 25.25 ? 362  GLN A CD  1 
ATOM   2776  O  OE1 . GLN A  1 345 ? 29.586  -51.219 49.438  1.00 25.94 ? 362  GLN A OE1 1 
ATOM   2777  N  NE2 . GLN A  1 345 ? 30.829  -49.354 49.346  1.00 25.69 ? 362  GLN A NE2 1 
ATOM   2778  N  N   . GLU A  1 346 ? 31.425  -55.290 45.721  1.00 26.36 ? 363  GLU A N   1 
ATOM   2779  C  CA  . GLU A  1 346 ? 31.748  -56.701 45.897  1.00 28.98 ? 363  GLU A CA  1 
ATOM   2780  C  C   . GLU A  1 346 ? 33.038  -57.098 45.175  1.00 26.89 ? 363  GLU A C   1 
ATOM   2781  O  O   . GLU A  1 346 ? 33.800  -57.906 45.703  1.00 27.35 ? 363  GLU A O   1 
ATOM   2782  C  CB  . GLU A  1 346 ? 30.586  -57.595 45.450  1.00 32.67 ? 363  GLU A CB  1 
ATOM   2783  C  CG  . GLU A  1 346 ? 29.448  -57.659 46.466  1.00 36.36 ? 363  GLU A CG  1 
ATOM   2784  C  CD  . GLU A  1 346 ? 28.231  -58.485 46.066  1.00 42.42 ? 363  GLU A CD  1 
ATOM   2785  O  OE1 . GLU A  1 346 ? 28.240  -59.122 44.984  1.00 44.18 ? 363  GLU A OE1 1 
ATOM   2786  O  OE2 . GLU A  1 346 ? 27.252  -58.472 46.854  1.00 44.83 ? 363  GLU A OE2 1 
ATOM   2787  N  N   . PRO A  1 347 ? 33.341  -56.582 43.961  1.00 25.19 ? 364  PRO A N   1 
ATOM   2788  C  CA  . PRO A  1 347 ? 34.591  -56.930 43.279  1.00 25.36 ? 364  PRO A CA  1 
ATOM   2789  C  C   . PRO A  1 347 ? 35.869  -56.561 44.030  1.00 25.78 ? 364  PRO A C   1 
ATOM   2790  O  O   . PRO A  1 347 ? 36.921  -57.128 43.749  1.00 25.73 ? 364  PRO A O   1 
ATOM   2791  C  CB  . PRO A  1 347 ? 34.482  -56.168 41.944  1.00 26.17 ? 364  PRO A CB  1 
ATOM   2792  C  CG  . PRO A  1 347 ? 32.998  -55.961 41.754  1.00 25.67 ? 364  PRO A CG  1 
ATOM   2793  C  CD  . PRO A  1 347 ? 32.498  -55.686 43.155  1.00 25.33 ? 364  PRO A CD  1 
ATOM   2794  N  N   . PHE A  1 348 ? 35.776  -55.597 44.960  1.00 25.01 ? 365  PHE A N   1 
ATOM   2795  C  CA  . PHE A  1 348 ? 36.936  -55.128 45.700  1.00 25.71 ? 365  PHE A CA  1 
ATOM   2796  C  C   . PHE A  1 348 ? 36.841  -55.547 47.164  1.00 27.03 ? 365  PHE A C   1 
ATOM   2797  O  O   . PHE A  1 348 ? 37.571  -55.007 47.993  1.00 27.95 ? 365  PHE A O   1 
ATOM   2798  C  CB  . PHE A  1 348 ? 37.048  -53.608 45.534  1.00 25.17 ? 365  PHE A CB  1 
ATOM   2799  C  CG  . PHE A  1 348 ? 37.048  -53.190 44.074  1.00 24.32 ? 365  PHE A CG  1 
ATOM   2800  C  CD1 . PHE A  1 348 ? 38.145  -53.461 43.263  1.00 23.39 ? 365  PHE A CD1 1 
ATOM   2801  C  CD2 . PHE A  1 348 ? 35.945  -52.559 43.508  1.00 23.58 ? 365  PHE A CD2 1 
ATOM   2802  C  CE1 . PHE A  1 348 ? 38.141  -53.101 41.928  1.00 22.84 ? 365  PHE A CE1 1 
ATOM   2803  C  CE2 . PHE A  1 348 ? 35.947  -52.204 42.167  1.00 22.88 ? 365  PHE A CE2 1 
ATOM   2804  C  CZ  . PHE A  1 348 ? 37.040  -52.479 41.381  1.00 23.32 ? 365  PHE A CZ  1 
ATOM   2805  N  N   . THR A  1 349 ? 35.946  -56.506 47.457  1.00 26.52 ? 366  THR A N   1 
ATOM   2806  C  CA  . THR A  1 349 ? 35.767  -57.062 48.789  1.00 27.26 ? 366  THR A CA  1 
ATOM   2807  C  C   . THR A  1 349 ? 36.451  -58.427 48.838  1.00 29.56 ? 366  THR A C   1 
ATOM   2808  O  O   . THR A  1 349 ? 36.147  -59.297 48.025  1.00 31.12 ? 366  THR A O   1 
ATOM   2809  C  CB  . THR A  1 349 ? 34.274  -57.195 49.086  1.00 27.46 ? 366  THR A CB  1 
ATOM   2810  O  OG1 . THR A  1 349 ? 33.716  -55.883 49.043  1.00 25.22 ? 366  THR A OG1 1 
ATOM   2811  C  CG2 . THR A  1 349 ? 34.004  -57.828 50.441  1.00 28.21 ? 366  THR A CG2 1 
ATOM   2812  N  N   . HIS A  1 350 ? 37.348  -58.625 49.810  1.00 29.61 ? 367  HIS A N   1 
ATOM   2813  C  CA  . HIS A  1 350 ? 38.220  -59.790 49.797  1.00 30.44 ? 367  HIS A CA  1 
ATOM   2814  C  C   . HIS A  1 350 ? 38.052  -60.591 51.084  1.00 30.94 ? 367  HIS A C   1 
ATOM   2815  O  O   . HIS A  1 350 ? 37.480  -60.115 52.063  1.00 29.75 ? 367  HIS A O   1 
ATOM   2816  C  CB  . HIS A  1 350 ? 39.668  -59.356 49.544  1.00 31.27 ? 367  HIS A CB  1 
ATOM   2817  C  CG  . HIS A  1 350 ? 39.803  -58.507 48.326  1.00 32.56 ? 367  HIS A CG  1 
ATOM   2818  N  ND1 . HIS A  1 350 ? 39.254  -58.869 47.112  1.00 32.47 ? 367  HIS A ND1 1 
ATOM   2819  C  CD2 . HIS A  1 350 ? 40.402  -57.324 48.129  1.00 32.47 ? 367  HIS A CD2 1 
ATOM   2820  C  CE1 . HIS A  1 350 ? 39.522  -57.926 46.214  1.00 33.70 ? 367  HIS A CE1 1 
ATOM   2821  N  NE2 . HIS A  1 350 ? 40.210  -56.975 46.814  1.00 33.25 ? 367  HIS A NE2 1 
ATOM   2822  N  N   . SER A  1 351 ? 38.552  -61.830 51.053  1.00 33.69 ? 368  SER A N   1 
ATOM   2823  C  CA  . SER A  1 351 ? 38.668  -62.629 52.258  1.00 35.29 ? 368  SER A CA  1 
ATOM   2824  C  C   . SER A  1 351 ? 39.514  -61.858 53.263  1.00 35.67 ? 368  SER A C   1 
ATOM   2825  O  O   . SER A  1 351 ? 40.541  -61.285 52.897  1.00 36.40 ? 368  SER A O   1 
ATOM   2826  C  CB  . SER A  1 351 ? 39.251  -63.988 51.967  1.00 35.55 ? 368  SER A CB  1 
ATOM   2827  O  OG  . SER A  1 351 ? 38.407  -64.706 51.078  1.00 36.89 ? 368  SER A OG  1 
ATOM   2828  N  N   . ALA A  1 352 ? 39.057  -61.840 54.521  1.00 35.82 ? 369  ALA A N   1 
ATOM   2829  C  CA  . ALA A  1 352 ? 39.725  -61.103 55.580  1.00 36.81 ? 369  ALA A CA  1 
ATOM   2830  C  C   . ALA A  1 352 ? 41.175  -61.564 55.694  1.00 36.73 ? 369  ALA A C   1 
ATOM   2831  O  O   . ALA A  1 352 ? 41.453  -62.750 55.547  1.00 36.45 ? 369  ALA A O   1 
ATOM   2832  C  CB  . ALA A  1 352 ? 38.983  -61.299 56.885  1.00 37.43 ? 369  ALA A CB  1 
ATOM   2833  N  N   . PRO A  1 353 ? 42.140  -60.646 55.936  1.00 38.08 ? 370  PRO A N   1 
ATOM   2834  C  CA  . PRO A  1 353 ? 43.519  -61.039 56.224  1.00 40.00 ? 370  PRO A CA  1 
ATOM   2835  C  C   . PRO A  1 353 ? 43.658  -61.581 57.647  1.00 42.62 ? 370  PRO A C   1 
ATOM   2836  O  O   . PRO A  1 353 ? 42.677  -61.647 58.384  1.00 40.25 ? 370  PRO A O   1 
ATOM   2837  C  CB  . PRO A  1 353 ? 44.329  -59.746 55.989  1.00 39.48 ? 370  PRO A CB  1 
ATOM   2838  C  CG  . PRO A  1 353 ? 43.337  -58.622 56.206  1.00 39.70 ? 370  PRO A CG  1 
ATOM   2839  C  CD  . PRO A  1 353 ? 41.957  -59.186 55.916  1.00 38.49 ? 370  PRO A CD  1 
ATOM   2840  N  N   . GLU A  1 354 ? 44.891  -61.961 58.009  1.00 47.51 ? 371  GLU A N   1 
ATOM   2841  C  CA  . GLU A  1 354 ? 45.209  -62.557 59.300  1.00 50.86 ? 371  GLU A CA  1 
ATOM   2842  C  C   . GLU A  1 354 ? 44.581  -61.749 60.433  1.00 50.74 ? 371  GLU A C   1 
ATOM   2843  O  O   . GLU A  1 354 ? 43.975  -62.318 61.339  1.00 50.02 ? 371  GLU A O   1 
ATOM   2844  C  CB  . GLU A  1 354 ? 46.725  -62.603 59.501  1.00 54.27 ? 371  GLU A CB  1 
ATOM   2845  C  CG  . GLU A  1 354 ? 47.166  -63.499 60.655  1.00 58.89 ? 371  GLU A CG  1 
ATOM   2846  C  CD  . GLU A  1 354 ? 47.113  -64.983 60.335  1.00 62.44 ? 371  GLU A CD  1 
ATOM   2847  O  OE1 . GLU A  1 354 ? 46.265  -65.688 60.923  1.00 64.49 ? 371  GLU A OE1 1 
ATOM   2848  O  OE2 . GLU A  1 354 ? 47.930  -65.437 59.503  1.00 63.01 ? 371  GLU A OE2 1 
ATOM   2849  N  N   . SER A  1 355 ? 44.758  -60.423 60.376  1.00 50.16 ? 372  SER A N   1 
ATOM   2850  C  CA  . SER A  1 355 ? 44.172  -59.504 61.337  1.00 50.46 ? 372  SER A CA  1 
ATOM   2851  C  C   . SER A  1 355 ? 43.282  -58.498 60.612  1.00 50.03 ? 372  SER A C   1 
ATOM   2852  O  O   . SER A  1 355 ? 43.661  -57.995 59.558  1.00 50.35 ? 372  SER A O   1 
ATOM   2853  C  CB  . SER A  1 355 ? 45.245  -58.806 62.124  1.00 51.70 ? 372  SER A CB  1 
ATOM   2854  O  OG  . SER A  1 355 ? 44.690  -57.745 62.888  1.00 55.15 ? 372  SER A OG  1 
ATOM   2855  N  N   . ILE A  1 356 ? 42.104  -58.213 61.187  1.00 47.78 ? 373  ILE A N   1 
ATOM   2856  C  CA  . ILE A  1 356 ? 41.197  -57.215 60.641  1.00 47.37 ? 373  ILE A CA  1 
ATOM   2857  C  C   . ILE A  1 356 ? 41.472  -55.884 61.338  1.00 45.57 ? 373  ILE A C   1 
ATOM   2858  O  O   . ILE A  1 356 ? 41.352  -55.791 62.558  1.00 45.36 ? 373  ILE A O   1 
ATOM   2859  C  CB  . ILE A  1 356 ? 39.725  -57.654 60.787  1.00 49.59 ? 373  ILE A CB  1 
ATOM   2860  C  CG1 . ILE A  1 356 ? 39.441  -58.940 59.995  1.00 51.13 ? 373  ILE A CG1 1 
ATOM   2861  C  CG2 . ILE A  1 356 ? 38.769  -56.525 60.388  1.00 48.96 ? 373  ILE A CG2 1 
ATOM   2862  C  CD1 . ILE A  1 356 ? 38.047  -59.513 60.197  1.00 52.50 ? 373  ILE A CD1 1 
ATOM   2863  N  N   . PRO A  1 357 ? 41.838  -54.814 60.590  1.00 43.29 ? 374  PRO A N   1 
ATOM   2864  C  CA  . PRO A  1 357 ? 42.149  -53.513 61.192  1.00 42.46 ? 374  PRO A CA  1 
ATOM   2865  C  C   . PRO A  1 357 ? 40.934  -52.724 61.678  1.00 42.69 ? 374  PRO A C   1 
ATOM   2866  O  O   . PRO A  1 357 ? 39.855  -52.821 61.097  1.00 46.18 ? 374  PRO A O   1 
ATOM   2867  C  CB  . PRO A  1 357 ? 42.870  -52.791 60.038  1.00 43.57 ? 374  PRO A CB  1 
ATOM   2868  C  CG  . PRO A  1 357 ? 42.220  -53.351 58.794  1.00 43.94 ? 374  PRO A CG  1 
ATOM   2869  C  CD  . PRO A  1 357 ? 41.981  -54.813 59.125  1.00 43.95 ? 374  PRO A CD  1 
ATOM   2870  N  N   . ASP A  1 358 ? 41.136  -51.932 62.740  1.00 41.99 ? 375  ASP A N   1 
ATOM   2871  C  CA  . ASP A  1 358 ? 40.111  -51.046 63.271  1.00 43.09 ? 375  ASP A CA  1 
ATOM   2872  C  C   . ASP A  1 358 ? 40.240  -49.644 62.677  1.00 39.25 ? 375  ASP A C   1 
ATOM   2873  O  O   . ASP A  1 358 ? 39.240  -48.940 62.549  1.00 40.28 ? 375  ASP A O   1 
ATOM   2874  C  CB  . ASP A  1 358 ? 40.175  -50.963 64.789  1.00 47.39 ? 375  ASP A CB  1 
ATOM   2875  C  CG  . ASP A  1 358 ? 39.743  -52.224 65.525  1.00 51.12 ? 375  ASP A CG  1 
ATOM   2876  O  OD1 . ASP A  1 358 ? 38.614  -52.694 65.265  1.00 50.76 ? 375  ASP A OD1 1 
ATOM   2877  O  OD2 . ASP A  1 358 ? 40.537  -52.723 66.350  1.00 53.36 ? 375  ASP A OD2 1 
ATOM   2878  N  N   . THR A  1 359 ? 41.478  -49.239 62.360  1.00 33.98 ? 376  THR A N   1 
ATOM   2879  C  CA  . THR A  1 359 ? 41.771  -47.905 61.856  1.00 31.06 ? 376  THR A CA  1 
ATOM   2880  C  C   . THR A  1 359 ? 42.481  -48.034 60.510  1.00 27.69 ? 376  THR A C   1 
ATOM   2881  O  O   . THR A  1 359 ? 42.976  -49.103 60.159  1.00 26.17 ? 376  THR A O   1 
ATOM   2882  C  CB  . THR A  1 359 ? 42.635  -47.137 62.858  1.00 30.99 ? 376  THR A CB  1 
ATOM   2883  O  OG1 . THR A  1 359 ? 43.900  -47.795 62.860  1.00 31.56 ? 376  THR A OG1 1 
ATOM   2884  C  CG2 . THR A  1 359 ? 42.059  -47.126 64.264  1.00 31.51 ? 376  THR A CG2 1 
ATOM   2885  N  N   . PHE A  1 360 ? 42.550  -46.925 59.770  1.00 26.42 ? 377  PHE A N   1 
ATOM   2886  C  CA  . PHE A  1 360 ? 43.192  -46.931 58.465  1.00 25.14 ? 377  PHE A CA  1 
ATOM   2887  C  C   . PHE A  1 360 ? 44.689  -47.208 58.634  1.00 25.53 ? 377  PHE A C   1 
ATOM   2888  O  O   . PHE A  1 360 ? 45.277  -47.930 57.833  1.00 24.26 ? 377  PHE A O   1 
ATOM   2889  C  CB  . PHE A  1 360 ? 42.889  -45.625 57.729  1.00 24.54 ? 377  PHE A CB  1 
ATOM   2890  C  CG  . PHE A  1 360 ? 43.327  -45.649 56.272  1.00 23.16 ? 377  PHE A CG  1 
ATOM   2891  C  CD1 . PHE A  1 360 ? 42.578  -46.326 55.317  1.00 22.71 ? 377  PHE A CD1 1 
ATOM   2892  C  CD2 . PHE A  1 360 ? 44.497  -45.013 55.868  1.00 22.68 ? 377  PHE A CD2 1 
ATOM   2893  C  CE1 . PHE A  1 360 ? 42.977  -46.351 53.989  1.00 21.70 ? 377  PHE A CE1 1 
ATOM   2894  C  CE2 . PHE A  1 360 ? 44.891  -45.044 54.539  1.00 22.32 ? 377  PHE A CE2 1 
ATOM   2895  C  CZ  . PHE A  1 360 ? 44.128  -45.706 53.604  1.00 21.81 ? 377  PHE A CZ  1 
ATOM   2896  N  N   . GLU A  1 361 ? 45.293  -46.651 59.695  1.00 27.25 ? 378  GLU A N   1 
ATOM   2897  C  CA  . GLU A  1 361 ? 46.695  -46.892 60.009  1.00 28.04 ? 378  GLU A CA  1 
ATOM   2898  C  C   . GLU A  1 361 ? 46.963  -48.390 60.145  1.00 27.82 ? 378  GLU A C   1 
ATOM   2899  O  O   . GLU A  1 361 ? 47.970  -48.882 59.642  1.00 27.09 ? 378  GLU A O   1 
ATOM   2900  C  CB  . GLU A  1 361 ? 47.107  -46.193 61.305  1.00 29.14 ? 378  GLU A CB  1 
ATOM   2901  C  CG  . GLU A  1 361 ? 48.567  -46.425 61.689  1.00 29.62 ? 378  GLU A CG  1 
ATOM   2902  C  CD  . GLU A  1 361 ? 48.937  -45.896 63.064  1.00 32.11 ? 378  GLU A CD  1 
ATOM   2903  O  OE1 . GLU A  1 361 ? 50.089  -46.115 63.484  1.00 32.81 ? 378  GLU A OE1 1 
ATOM   2904  O  OE2 . GLU A  1 361 ? 48.082  -45.251 63.708  1.00 34.49 ? 378  GLU A OE2 1 
ATOM   2905  N  N   . ASP A  1 362 ? 46.077  -49.097 60.858  1.00 28.33 ? 379  ASP A N   1 
ATOM   2906  C  CA  . ASP A  1 362 ? 46.204  -50.535 61.042  1.00 29.66 ? 379  ASP A CA  1 
ATOM   2907  C  C   . ASP A  1 362 ? 46.086  -51.247 59.695  1.00 27.75 ? 379  ASP A C   1 
ATOM   2908  O  O   . ASP A  1 362 ? 46.808  -52.205 59.432  1.00 27.81 ? 379  ASP A O   1 
ATOM   2909  C  CB  . ASP A  1 362 ? 45.165  -51.081 62.012  1.00 32.83 ? 379  ASP A CB  1 
ATOM   2910  C  CG  . ASP A  1 362 ? 45.264  -50.619 63.462  1.00 35.60 ? 379  ASP A CG  1 
ATOM   2911  O  OD1 . ASP A  1 362 ? 46.383  -50.302 63.915  1.00 36.69 ? 379  ASP A OD1 1 
ATOM   2912  O  OD2 . ASP A  1 362 ? 44.202  -50.562 64.124  1.00 37.41 ? 379  ASP A OD2 1 
ATOM   2913  N  N   . ALA A  1 363 ? 45.174  -50.768 58.838  1.00 25.50 ? 380  ALA A N   1 
ATOM   2914  C  CA  . ALA A  1 363 ? 44.986  -51.360 57.524  1.00 24.29 ? 380  ALA A CA  1 
ATOM   2915  C  C   . ALA A  1 363 ? 46.258  -51.212 56.689  1.00 23.88 ? 380  ALA A C   1 
ATOM   2916  O  O   . ALA A  1 363 ? 46.634  -52.150 55.995  1.00 23.99 ? 380  ALA A O   1 
ATOM   2917  C  CB  . ALA A  1 363 ? 43.788  -50.745 56.836  1.00 24.95 ? 380  ALA A CB  1 
ATOM   2918  N  N   . VAL A  1 364 ? 46.924  -50.052 56.782  1.00 24.37 ? 381  VAL A N   1 
ATOM   2919  C  CA  . VAL A  1 364 ? 48.180  -49.813 56.079  1.00 24.55 ? 381  VAL A CA  1 
ATOM   2920  C  C   . VAL A  1 364 ? 49.238  -50.805 56.564  1.00 26.05 ? 381  VAL A C   1 
ATOM   2921  O  O   . VAL A  1 364 ? 49.933  -51.413 55.756  1.00 26.50 ? 381  VAL A O   1 
ATOM   2922  C  CB  . VAL A  1 364 ? 48.656  -48.354 56.236  1.00 24.14 ? 381  VAL A CB  1 
ATOM   2923  C  CG1 . VAL A  1 364 ? 50.097  -48.147 55.776  1.00 24.57 ? 381  VAL A CG1 1 
ATOM   2924  C  CG2 . VAL A  1 364 ? 47.736  -47.385 55.504  1.00 24.13 ? 381  VAL A CG2 1 
ATOM   2925  N  N   . ASN A  1 365 ? 49.366  -50.967 57.888  1.00 28.25 ? 382  ASN A N   1 
ATOM   2926  C  CA  . ASN A  1 365 ? 50.409  -51.815 58.450  1.00 28.84 ? 382  ASN A CA  1 
ATOM   2927  C  C   . ASN A  1 365 ? 50.145  -53.286 58.134  1.00 28.83 ? 382  ASN A C   1 
ATOM   2928  O  O   . ASN A  1 365 ? 51.092  -54.043 57.935  1.00 30.99 ? 382  ASN A O   1 
ATOM   2929  C  CB  . ASN A  1 365 ? 50.591  -51.584 59.946  1.00 29.96 ? 382  ASN A CB  1 
ATOM   2930  C  CG  . ASN A  1 365 ? 51.295  -50.281 60.237  1.00 30.79 ? 382  ASN A CG  1 
ATOM   2931  O  OD1 . ASN A  1 365 ? 52.280  -49.949 59.568  1.00 31.27 ? 382  ASN A OD1 1 
ATOM   2932  N  ND2 . ASN A  1 365 ? 50.809  -49.526 61.213  1.00 30.18 ? 382  ASN A ND2 1 
ATOM   2933  N  N   . ILE A  1 366 ? 48.869  -53.687 58.081  1.00 28.02 ? 383  ILE A N   1 
ATOM   2934  C  CA  . ILE A  1 366 ? 48.510  -55.079 57.850  1.00 28.04 ? 383  ILE A CA  1 
ATOM   2935  C  C   . ILE A  1 366 ? 48.598  -55.425 56.360  1.00 26.77 ? 383  ILE A C   1 
ATOM   2936  O  O   . ILE A  1 366 ? 49.098  -56.489 56.009  1.00 26.07 ? 383  ILE A O   1 
ATOM   2937  C  CB  . ILE A  1 366 ? 47.123  -55.386 58.445  1.00 29.26 ? 383  ILE A CB  1 
ATOM   2938  C  CG1 . ILE A  1 366 ? 47.164  -55.364 59.979  1.00 31.52 ? 383  ILE A CG1 1 
ATOM   2939  C  CG2 . ILE A  1 366 ? 46.577  -56.716 57.925  1.00 30.55 ? 383  ILE A CG2 1 
ATOM   2940  C  CD1 . ILE A  1 366 ? 45.806  -55.198 60.641  1.00 31.45 ? 383  ILE A CD1 1 
ATOM   2941  N  N   . LEU A  1 367 ? 48.107  -54.542 55.481  1.00 25.27 ? 384  LEU A N   1 
ATOM   2942  C  CA  . LEU A  1 367 ? 48.032  -54.844 54.055  1.00 24.61 ? 384  LEU A CA  1 
ATOM   2943  C  C   . LEU A  1 367 ? 49.324  -54.451 53.338  1.00 24.60 ? 384  LEU A C   1 
ATOM   2944  O  O   . LEU A  1 367 ? 49.630  -55.003 52.283  1.00 25.14 ? 384  LEU A O   1 
ATOM   2945  C  CB  . LEU A  1 367 ? 46.843  -54.120 53.423  1.00 24.96 ? 384  LEU A CB  1 
ATOM   2946  C  CG  . LEU A  1 367 ? 45.446  -54.563 53.865  1.00 24.73 ? 384  LEU A CG  1 
ATOM   2947  C  CD1 . LEU A  1 367 ? 44.410  -53.645 53.242  1.00 25.43 ? 384  LEU A CD1 1 
ATOM   2948  C  CD2 . LEU A  1 367 ? 45.173  -56.009 53.490  1.00 24.90 ? 384  LEU A CD2 1 
ATOM   2949  N  N   . LYS A  1 368 ? 50.034  -53.456 53.881  1.00 26.38 ? 385  LYS A N   1 
ATOM   2950  C  CA  . LYS A  1 368 ? 51.268  -52.943 53.301  1.00 27.42 ? 385  LYS A CA  1 
ATOM   2951  C  C   . LYS A  1 368 ? 51.042  -52.546 51.844  1.00 25.57 ? 385  LYS A C   1 
ATOM   2952  O  O   . LYS A  1 368 ? 51.682  -53.086 50.944  1.00 24.99 ? 385  LYS A O   1 
ATOM   2953  C  CB  . LYS A  1 368 ? 52.412  -53.954 53.437  1.00 30.90 ? 385  LYS A CB  1 
ATOM   2954  C  CG  . LYS A  1 368 ? 52.753  -54.321 54.874  1.00 34.23 ? 385  LYS A CG  1 
ATOM   2955  C  CD  . LYS A  1 368 ? 53.916  -55.296 55.013  1.00 37.16 ? 385  LYS A CD  1 
ATOM   2956  C  CE  . LYS A  1 368 ? 54.003  -55.863 56.397  1.00 40.61 ? 385  LYS A CE  1 
ATOM   2957  N  NZ  . LYS A  1 368 ? 54.130  -54.826 57.425  1.00 43.45 ? 385  LYS A NZ  1 
ATOM   2958  N  N   . PRO A  1 369 ? 50.155  -51.564 51.564  1.00 22.14 ? 386  PRO A N   1 
ATOM   2959  C  CA  . PRO A  1 369 ? 49.940  -51.101 50.193  1.00 21.92 ? 386  PRO A CA  1 
ATOM   2960  C  C   . PRO A  1 369 ? 51.125  -50.271 49.713  1.00 21.12 ? 386  PRO A C   1 
ATOM   2961  O  O   . PRO A  1 369 ? 51.835  -49.674 50.518  1.00 21.53 ? 386  PRO A O   1 
ATOM   2962  C  CB  . PRO A  1 369 ? 48.665  -50.262 50.319  1.00 21.87 ? 386  PRO A CB  1 
ATOM   2963  C  CG  . PRO A  1 369 ? 48.776  -49.671 51.711  1.00 22.43 ? 386  PRO A CG  1 
ATOM   2964  C  CD  . PRO A  1 369 ? 49.373  -50.800 52.548  1.00 22.92 ? 386  PRO A CD  1 
ATOM   2965  N  N   . SER A  1 370 ? 51.312  -50.233 48.394  1.00 22.04 ? 387  SER A N   1 
ATOM   2966  C  CA  . SER A  1 370 ? 52.239  -49.310 47.763  1.00 21.93 ? 387  SER A CA  1 
ATOM   2967  C  C   . SER A  1 370 ? 51.594  -47.936 47.571  1.00 20.93 ? 387  SER A C   1 
ATOM   2968  O  O   . SER A  1 370 ? 52.297  -46.939 47.432  1.00 21.15 ? 387  SER A O   1 
ATOM   2969  C  CB  . SER A  1 370 ? 52.709  -49.873 46.451  1.00 23.68 ? 387  SER A CB  1 
ATOM   2970  O  OG  . SER A  1 370 ? 51.611  -50.154 45.596  1.00 24.81 ? 387  SER A OG  1 
ATOM   2971  N  N   . THR A  1 371 ? 50.254  -47.889 47.575  1.00 20.70 ? 388  THR A N   1 
ATOM   2972  C  CA  . THR A  1 371 ? 49.496  -46.706 47.184  1.00 20.59 ? 388  THR A CA  1 
ATOM   2973  C  C   . THR A  1 371 ? 48.277  -46.573 48.093  1.00 19.39 ? 388  THR A C   1 
ATOM   2974  O  O   . THR A  1 371 ? 47.569  -47.555 48.281  1.00 19.30 ? 388  THR A O   1 
ATOM   2975  C  CB  . THR A  1 371 ? 49.024  -46.845 45.734  1.00 21.37 ? 388  THR A CB  1 
ATOM   2976  O  OG1 . THR A  1 371 ? 50.152  -47.030 44.885  1.00 22.30 ? 388  THR A OG1 1 
ATOM   2977  C  CG2 . THR A  1 371 ? 48.258  -45.619 45.268  1.00 22.23 ? 388  THR A CG2 1 
ATOM   2978  N  N   . ILE A  1 372 ? 48.020  -45.360 48.608  1.00 18.59 ? 389  ILE A N   1 
ATOM   2979  C  CA  . ILE A  1 372 ? 46.760  -45.055 49.273  1.00 19.06 ? 389  ILE A CA  1 
ATOM   2980  C  C   . ILE A  1 372 ? 46.082  -43.890 48.556  1.00 18.78 ? 389  ILE A C   1 
ATOM   2981  O  O   . ILE A  1 372 ? 46.737  -42.932 48.157  1.00 19.78 ? 389  ILE A O   1 
ATOM   2982  C  CB  . ILE A  1 372 ? 46.942  -44.780 50.780  1.00 19.59 ? 389  ILE A CB  1 
ATOM   2983  C  CG1 . ILE A  1 372 ? 47.968  -43.671 51.062  1.00 20.00 ? 389  ILE A CG1 1 
ATOM   2984  C  CG2 . ILE A  1 372 ? 47.289  -46.079 51.508  1.00 19.45 ? 389  ILE A CG2 1 
ATOM   2985  C  CD1 . ILE A  1 372 ? 48.015  -43.221 52.515  1.00 20.62 ? 389  ILE A CD1 1 
ATOM   2986  N  N   . ILE A  1 373 ? 44.758  -43.995 48.406  1.00 18.41 ? 390  ILE A N   1 
ATOM   2987  C  CA  . ILE A  1 373 ? 43.964  -43.000 47.710  1.00 18.64 ? 390  ILE A CA  1 
ATOM   2988  C  C   . ILE A  1 373 ? 42.808  -42.590 48.619  1.00 19.73 ? 390  ILE A C   1 
ATOM   2989  O  O   . ILE A  1 373 ? 41.973  -43.424 48.980  1.00 19.19 ? 390  ILE A O   1 
ATOM   2990  C  CB  . ILE A  1 373 ? 43.469  -43.539 46.351  1.00 18.53 ? 390  ILE A CB  1 
ATOM   2991  C  CG1 . ILE A  1 373 ? 44.634  -44.003 45.462  1.00 18.54 ? 390  ILE A CG1 1 
ATOM   2992  C  CG2 . ILE A  1 373 ? 42.596  -42.500 45.644  1.00 18.36 ? 390  ILE A CG2 1 
ATOM   2993  C  CD1 . ILE A  1 373 ? 44.217  -44.621 44.133  1.00 18.75 ? 390  ILE A CD1 1 
ATOM   2994  N  N   . GLY A  1 374 ? 42.776  -41.295 48.965  1.00 19.53 ? 391  GLY A N   1 
ATOM   2995  C  CA  . GLY A  1 374 ? 41.781  -40.743 49.864  1.00 19.37 ? 391  GLY A CA  1 
ATOM   2996  C  C   . GLY A  1 374 ? 40.612  -40.117 49.104  1.00 19.55 ? 391  GLY A C   1 
ATOM   2997  O  O   . GLY A  1 374 ? 40.786  -39.101 48.430  1.00 19.31 ? 391  GLY A O   1 
ATOM   2998  N  N   . VAL A  1 375 ? 39.427  -40.724 49.263  1.00 19.80 ? 392  VAL A N   1 
ATOM   2999  C  CA  . VAL A  1 375 ? 38.196  -40.266 48.643  1.00 20.70 ? 392  VAL A CA  1 
ATOM   3000  C  C   . VAL A  1 375 ? 37.030  -40.493 49.608  1.00 21.59 ? 392  VAL A C   1 
ATOM   3001  O  O   . VAL A  1 375 ? 36.007  -41.060 49.235  1.00 21.61 ? 392  VAL A O   1 
ATOM   3002  C  CB  . VAL A  1 375 ? 37.975  -40.968 47.287  1.00 20.61 ? 392  VAL A CB  1 
ATOM   3003  C  CG1 . VAL A  1 375 ? 38.808  -40.331 46.179  1.00 21.00 ? 392  VAL A CG1 1 
ATOM   3004  C  CG2 . VAL A  1 375 ? 38.226  -42.472 47.357  1.00 20.79 ? 392  VAL A CG2 1 
ATOM   3005  N  N   . ALA A  1 376 ? 37.201  -40.051 50.860  1.00 22.79 ? 393  ALA A N   1 
ATOM   3006  C  CA  . ALA A  1 376 ? 36.214  -40.273 51.909  1.00 23.56 ? 393  ALA A CA  1 
ATOM   3007  C  C   . ALA A  1 376 ? 35.401  -39.009 52.185  1.00 25.52 ? 393  ALA A C   1 
ATOM   3008  O  O   . ALA A  1 376 ? 34.309  -39.101 52.741  1.00 25.85 ? 393  ALA A O   1 
ATOM   3009  C  CB  . ALA A  1 376 ? 36.894  -40.743 53.173  1.00 23.08 ? 393  ALA A CB  1 
ATOM   3010  N  N   . GLY A  1 377 ? 35.957  -37.840 51.837  1.00 26.84 ? 394  GLY A N   1 
ATOM   3011  C  CA  . GLY A  1 377 ? 35.308  -36.560 52.088  1.00 28.48 ? 394  GLY A CA  1 
ATOM   3012  C  C   . GLY A  1 377 ? 35.056  -36.313 53.576  1.00 30.47 ? 394  GLY A C   1 
ATOM   3013  O  O   . GLY A  1 377 ? 34.030  -35.740 53.939  1.00 32.87 ? 394  GLY A O   1 
ATOM   3014  N  N   . ALA A  1 378 ? 35.996  -36.736 54.429  1.00 30.91 ? 395  ALA A N   1 
ATOM   3015  C  CA  . ALA A  1 378 ? 35.764  -36.777 55.866  1.00 31.48 ? 395  ALA A CA  1 
ATOM   3016  C  C   . ALA A  1 378 ? 36.902  -36.132 56.655  1.00 30.27 ? 395  ALA A C   1 
ATOM   3017  O  O   . ALA A  1 378 ? 36.986  -36.341 57.862  1.00 30.81 ? 395  ALA A O   1 
ATOM   3018  C  CB  . ALA A  1 378 ? 35.561  -38.213 56.300  1.00 31.91 ? 395  ALA A CB  1 
ATOM   3019  N  N   . GLY A  1 379 ? 37.777  -35.363 55.990  1.00 28.51 ? 396  GLY A N   1 
ATOM   3020  C  CA  . GLY A  1 379 ? 38.824  -34.634 56.688  1.00 27.73 ? 396  GLY A CA  1 
ATOM   3021  C  C   . GLY A  1 379 ? 40.144  -35.400 56.732  1.00 27.65 ? 396  GLY A C   1 
ATOM   3022  O  O   . GLY A  1 379 ? 40.356  -36.323 55.948  1.00 26.63 ? 396  GLY A O   1 
ATOM   3023  N  N   . ARG A  1 380 ? 41.006  -35.008 57.680  1.00 27.39 ? 397  ARG A N   1 
ATOM   3024  C  CA  . ARG A  1 380 ? 42.435  -35.287 57.640  1.00 28.18 ? 397  ARG A CA  1 
ATOM   3025  C  C   . ARG A  1 380 ? 42.740  -36.679 58.193  1.00 27.34 ? 397  ARG A C   1 
ATOM   3026  O  O   . ARG A  1 380 ? 43.443  -36.812 59.190  1.00 27.77 ? 397  ARG A O   1 
ATOM   3027  C  CB  . ARG A  1 380 ? 43.196  -34.234 58.459  1.00 29.57 ? 397  ARG A CB  1 
ATOM   3028  C  CG  . ARG A  1 380 ? 43.172  -32.820 57.894  1.00 30.80 ? 397  ARG A CG  1 
ATOM   3029  C  CD  . ARG A  1 380 ? 44.272  -32.580 56.866  1.00 31.53 ? 397  ARG A CD  1 
ATOM   3030  N  NE  . ARG A  1 380 ? 44.364  -31.165 56.489  1.00 32.82 ? 397  ARG A NE  1 
ATOM   3031  C  CZ  . ARG A  1 380 ? 43.527  -30.499 55.700  1.00 32.58 ? 397  ARG A CZ  1 
ATOM   3032  N  NH1 . ARG A  1 380 ? 42.562  -31.125 55.046  1.00 32.71 ? 397  ARG A NH1 1 
ATOM   3033  N  NH2 . ARG A  1 380 ? 43.676  -29.193 55.542  1.00 33.24 ? 397  ARG A NH2 1 
ATOM   3034  N  N   . LEU A  1 381 ? 42.281  -37.714 57.486  1.00 26.30 ? 398  LEU A N   1 
ATOM   3035  C  CA  . LEU A  1 381 ? 42.368  -39.082 57.966  1.00 26.06 ? 398  LEU A CA  1 
ATOM   3036  C  C   . LEU A  1 381 ? 43.675  -39.752 57.537  1.00 24.73 ? 398  LEU A C   1 
ATOM   3037  O  O   . LEU A  1 381 ? 43.969  -40.851 57.995  1.00 25.62 ? 398  LEU A O   1 
ATOM   3038  C  CB  . LEU A  1 381 ? 41.140  -39.833 57.464  1.00 27.34 ? 398  LEU A CB  1 
ATOM   3039  C  CG  . LEU A  1 381 ? 39.792  -39.318 57.981  1.00 29.85 ? 398  LEU A CG  1 
ATOM   3040  C  CD1 . LEU A  1 381 ? 38.656  -40.053 57.304  1.00 31.13 ? 398  LEU A CD1 1 
ATOM   3041  C  CD2 . LEU A  1 381 ? 39.672  -39.449 59.492  1.00 31.25 ? 398  LEU A CD2 1 
ATOM   3042  N  N   . PHE A  1 382 ? 44.459  -39.114 56.661  1.00 24.27 ? 399  PHE A N   1 
ATOM   3043  C  CA  . PHE A  1 382 ? 45.837  -39.542 56.449  1.00 23.65 ? 399  PHE A CA  1 
ATOM   3044  C  C   . PHE A  1 382 ? 46.690  -38.844 57.508  1.00 23.98 ? 399  PHE A C   1 
ATOM   3045  O  O   . PHE A  1 382 ? 47.340  -37.836 57.237  1.00 23.42 ? 399  PHE A O   1 
ATOM   3046  C  CB  . PHE A  1 382 ? 46.357  -39.310 55.023  1.00 23.73 ? 399  PHE A CB  1 
ATOM   3047  C  CG  . PHE A  1 382 ? 45.725  -40.157 53.918  1.00 23.30 ? 399  PHE A CG  1 
ATOM   3048  C  CD1 . PHE A  1 382 ? 44.829  -41.186 54.202  1.00 22.77 ? 399  PHE A CD1 1 
ATOM   3049  C  CD2 . PHE A  1 382 ? 46.055  -39.932 52.584  1.00 22.50 ? 399  PHE A CD2 1 
ATOM   3050  C  CE1 . PHE A  1 382 ? 44.271  -41.948 53.184  1.00 22.94 ? 399  PHE A CE1 1 
ATOM   3051  C  CE2 . PHE A  1 382 ? 45.497  -40.695 51.571  1.00 22.37 ? 399  PHE A CE2 1 
ATOM   3052  C  CZ  . PHE A  1 382 ? 44.602  -41.700 51.870  1.00 23.02 ? 399  PHE A CZ  1 
ATOM   3053  N  N   . THR A  1 383 ? 46.647  -39.402 58.723  1.00 24.72 ? 400  THR A N   1 
ATOM   3054  C  CA  . THR A  1 383 ? 47.320  -38.845 59.886  1.00 26.32 ? 400  THR A CA  1 
ATOM   3055  C  C   . THR A  1 383 ? 48.829  -38.945 59.683  1.00 27.32 ? 400  THR A C   1 
ATOM   3056  O  O   . THR A  1 383 ? 49.289  -39.705 58.830  1.00 27.34 ? 400  THR A O   1 
ATOM   3057  C  CB  . THR A  1 383 ? 46.892  -39.586 61.155  1.00 25.07 ? 400  THR A CB  1 
ATOM   3058  O  OG1 . THR A  1 383 ? 47.406  -40.911 61.061  1.00 24.31 ? 400  THR A OG1 1 
ATOM   3059  C  CG2 . THR A  1 383 ? 45.387  -39.619 61.347  1.00 25.81 ? 400  THR A CG2 1 
ATOM   3060  N  N   . PRO A  1 384 ? 49.644  -38.191 60.459  1.00 29.50 ? 401  PRO A N   1 
ATOM   3061  C  CA  . PRO A  1 384 ? 51.097  -38.353 60.421  1.00 29.58 ? 401  PRO A CA  1 
ATOM   3062  C  C   . PRO A  1 384 ? 51.559  -39.793 60.636  1.00 29.26 ? 401  PRO A C   1 
ATOM   3063  O  O   . PRO A  1 384 ? 52.577  -40.194 60.071  1.00 29.63 ? 401  PRO A O   1 
ATOM   3064  C  CB  . PRO A  1 384 ? 51.587  -37.397 61.533  1.00 30.27 ? 401  PRO A CB  1 
ATOM   3065  C  CG  . PRO A  1 384 ? 50.508  -36.344 61.612  1.00 30.29 ? 401  PRO A CG  1 
ATOM   3066  C  CD  . PRO A  1 384 ? 49.220  -37.104 61.358  1.00 29.72 ? 401  PRO A CD  1 
ATOM   3067  N  N   . ASP A  1 385 ? 50.813  -40.561 61.450  1.00 28.00 ? 402  ASP A N   1 
ATOM   3068  C  CA  . ASP A  1 385 ? 51.120  -41.969 61.669  1.00 28.13 ? 402  ASP A CA  1 
ATOM   3069  C  C   . ASP A  1 385 ? 50.829  -42.788 60.405  1.00 26.61 ? 402  ASP A C   1 
ATOM   3070  O  O   . ASP A  1 385 ? 51.555  -43.732 60.099  1.00 25.57 ? 402  ASP A O   1 
ATOM   3071  C  CB  . ASP A  1 385 ? 50.423  -42.505 62.912  1.00 29.76 ? 402  ASP A CB  1 
ATOM   3072  C  CG  . ASP A  1 385 ? 50.971  -42.015 64.253  1.00 32.90 ? 402  ASP A CG  1 
ATOM   3073  O  OD1 . ASP A  1 385 ? 52.135  -41.553 64.301  1.00 34.16 ? 402  ASP A OD1 1 
ATOM   3074  O  OD2 . ASP A  1 385 ? 50.227  -42.086 65.249  1.00 32.90 ? 402  ASP A OD2 1 
ATOM   3075  N  N   . VAL A  1 386 ? 49.768  -42.439 59.669  1.00 25.27 ? 403  VAL A N   1 
ATOM   3076  C  CA  . VAL A  1 386 ? 49.476  -43.102 58.404  1.00 24.57 ? 403  VAL A CA  1 
ATOM   3077  C  C   . VAL A  1 386 ? 50.618  -42.832 57.422  1.00 23.90 ? 403  VAL A C   1 
ATOM   3078  O  O   . VAL A  1 386 ? 51.125  -43.757 56.798  1.00 24.85 ? 403  VAL A O   1 
ATOM   3079  C  CB  . VAL A  1 386 ? 48.114  -42.670 57.827  1.00 24.18 ? 403  VAL A CB  1 
ATOM   3080  C  CG1 . VAL A  1 386 ? 47.968  -43.029 56.352  1.00 23.84 ? 403  VAL A CG1 1 
ATOM   3081  C  CG2 . VAL A  1 386 ? 46.960  -43.242 58.642  1.00 24.84 ? 403  VAL A CG2 1 
ATOM   3082  N  N   . ILE A  1 387 ? 51.031  -41.565 57.319  1.00 24.76 ? 404  ILE A N   1 
ATOM   3083  C  CA  . ILE A  1 387 ? 52.043  -41.137 56.362  1.00 25.53 ? 404  ILE A CA  1 
ATOM   3084  C  C   . ILE A  1 387 ? 53.379  -41.818 56.672  1.00 26.20 ? 404  ILE A C   1 
ATOM   3085  O  O   . ILE A  1 387 ? 54.036  -42.333 55.770  1.00 24.35 ? 404  ILE A O   1 
ATOM   3086  C  CB  . ILE A  1 387 ? 52.147  -39.598 56.345  1.00 25.77 ? 404  ILE A CB  1 
ATOM   3087  C  CG1 . ILE A  1 387 ? 50.846  -38.964 55.819  1.00 26.73 ? 404  ILE A CG1 1 
ATOM   3088  C  CG2 . ILE A  1 387 ? 53.363  -39.133 55.543  1.00 25.75 ? 404  ILE A CG2 1 
ATOM   3089  C  CD1 . ILE A  1 387 ? 50.745  -37.462 56.000  1.00 26.79 ? 404  ILE A CD1 1 
ATOM   3090  N  N   . ARG A  1 388 ? 53.769  -41.834 57.953  1.00 27.01 ? 405  ARG A N   1 
ATOM   3091  C  CA  . ARG A  1 388 ? 55.040  -42.416 58.359  1.00 28.29 ? 405  ARG A CA  1 
ATOM   3092  C  C   . ARG A  1 388 ? 55.044  -43.920 58.100  1.00 26.77 ? 405  ARG A C   1 
ATOM   3093  O  O   . ARG A  1 388 ? 56.059  -44.472 57.689  1.00 28.87 ? 405  ARG A O   1 
ATOM   3094  C  CB  . ARG A  1 388 ? 55.352  -42.125 59.834  1.00 31.18 ? 405  ARG A CB  1 
ATOM   3095  C  CG  . ARG A  1 388 ? 55.824  -40.708 60.122  1.00 33.20 ? 405  ARG A CG  1 
ATOM   3096  C  CD  . ARG A  1 388 ? 56.026  -40.478 61.617  1.00 34.71 ? 405  ARG A CD  1 
ATOM   3097  N  NE  . ARG A  1 388 ? 56.938  -41.453 62.230  1.00 36.65 ? 405  ARG A NE  1 
ATOM   3098  C  CZ  . ARG A  1 388 ? 58.271  -41.456 62.180  1.00 37.92 ? 405  ARG A CZ  1 
ATOM   3099  N  NH1 . ARG A  1 388 ? 58.939  -40.516 61.532  1.00 38.38 ? 405  ARG A NH1 1 
ATOM   3100  N  NH2 . ARG A  1 388 ? 58.942  -42.405 62.807  1.00 40.29 ? 405  ARG A NH2 1 
ATOM   3101  N  N   . ALA A  1 389 ? 53.906  -44.581 58.333  1.00 26.43 ? 406  ALA A N   1 
ATOM   3102  C  CA  . ALA A  1 389 ? 53.787  -46.006 58.071  1.00 26.64 ? 406  ALA A CA  1 
ATOM   3103  C  C   . ALA A  1 389 ? 54.000  -46.285 56.584  1.00 26.03 ? 406  ALA A C   1 
ATOM   3104  O  O   . ALA A  1 389 ? 54.718  -47.217 56.226  1.00 25.94 ? 406  ALA A O   1 
ATOM   3105  C  CB  . ALA A  1 389 ? 52.444  -46.517 58.545  1.00 27.04 ? 406  ALA A CB  1 
ATOM   3106  N  N   . MET A  1 390 ? 53.387  -45.466 55.719  1.00 25.20 ? 407  MET A N   1 
ATOM   3107  C  CA  . MET A  1 390 ? 53.552  -45.628 54.281  1.00 24.53 ? 407  MET A CA  1 
ATOM   3108  C  C   . MET A  1 390 ? 55.028  -45.513 53.890  1.00 24.85 ? 407  MET A C   1 
ATOM   3109  O  O   . MET A  1 390 ? 55.494  -46.290 53.062  1.00 26.05 ? 407  MET A O   1 
ATOM   3110  C  CB  . MET A  1 390 ? 52.705  -44.620 53.493  1.00 24.06 ? 407  MET A CB  1 
ATOM   3111  C  CG  . MET A  1 390 ? 51.234  -45.003 53.393  1.00 23.36 ? 407  MET A CG  1 
ATOM   3112  S  SD  . MET A  1 390 ? 50.955  -46.539 52.493  1.00 24.34 ? 407  MET A SD  1 
ATOM   3113  C  CE  . MET A  1 390 ? 51.341  -46.082 50.796  1.00 24.03 ? 407  MET A CE  1 
ATOM   3114  N  N   . ALA A  1 391 ? 55.758  -44.570 54.499  1.00 26.14 ? 408  ALA A N   1 
ATOM   3115  C  CA  . ALA A  1 391 ? 57.151  -44.318 54.145  1.00 27.90 ? 408  ALA A CA  1 
ATOM   3116  C  C   . ALA A  1 391 ? 58.117  -45.328 54.773  1.00 30.96 ? 408  ALA A C   1 
ATOM   3117  O  O   . ALA A  1 391 ? 59.266  -45.416 54.340  1.00 31.96 ? 408  ALA A O   1 
ATOM   3118  C  CB  . ALA A  1 391 ? 57.527  -42.913 54.535  1.00 28.56 ? 408  ALA A CB  1 
ATOM   3119  N  N   . SER A  1 392 ? 57.679  -46.077 55.793  1.00 31.84 ? 409  SER A N   1 
ATOM   3120  C  CA  . SER A  1 392 ? 58.498  -47.147 56.348  1.00 33.86 ? 409  SER A CA  1 
ATOM   3121  C  C   . SER A  1 392 ? 58.275  -48.449 55.575  1.00 33.91 ? 409  SER A C   1 
ATOM   3122  O  O   . SER A  1 392 ? 59.183  -49.271 55.476  1.00 34.89 ? 409  SER A O   1 
ATOM   3123  C  CB  . SER A  1 392 ? 58.260  -47.324 57.835  1.00 35.58 ? 409  SER A CB  1 
ATOM   3124  O  OG  . SER A  1 392 ? 56.930  -47.741 58.111  1.00 40.89 ? 409  SER A OG  1 
ATOM   3125  N  N   . ILE A  1 393 ? 57.069  -48.626 55.015  1.00 31.03 ? 410  ILE A N   1 
ATOM   3126  C  CA  . ILE A  1 393 ? 56.743  -49.791 54.205  1.00 29.18 ? 410  ILE A CA  1 
ATOM   3127  C  C   . ILE A  1 393 ? 57.328  -49.639 52.798  1.00 28.53 ? 410  ILE A C   1 
ATOM   3128  O  O   . ILE A  1 393 ? 57.817  -50.609 52.227  1.00 28.96 ? 410  ILE A O   1 
ATOM   3129  C  CB  . ILE A  1 393 ? 55.217  -50.011 54.163  1.00 29.03 ? 410  ILE A CB  1 
ATOM   3130  C  CG1 . ILE A  1 393 ? 54.662  -50.395 55.538  1.00 29.15 ? 410  ILE A CG1 1 
ATOM   3131  C  CG2 . ILE A  1 393 ? 54.834  -51.045 53.102  1.00 29.12 ? 410  ILE A CG2 1 
ATOM   3132  C  CD1 . ILE A  1 393 ? 53.164  -50.191 55.682  1.00 28.87 ? 410  ILE A CD1 1 
ATOM   3133  N  N   . ASN A  1 394 ? 57.250  -48.430 52.230  1.00 28.06 ? 411  ASN A N   1 
ATOM   3134  C  CA  . ASN A  1 394 ? 57.650  -48.197 50.849  1.00 27.77 ? 411  ASN A CA  1 
ATOM   3135  C  C   . ASN A  1 394 ? 58.768  -47.161 50.794  1.00 28.26 ? 411  ASN A C   1 
ATOM   3136  O  O   . ASN A  1 394 ? 58.735  -46.162 51.509  1.00 29.07 ? 411  ASN A O   1 
ATOM   3137  C  CB  . ASN A  1 394 ? 56.481  -47.700 50.006  1.00 26.88 ? 411  ASN A CB  1 
ATOM   3138  C  CG  . ASN A  1 394 ? 55.289  -48.619 50.103  1.00 25.38 ? 411  ASN A CG  1 
ATOM   3139  O  OD1 . ASN A  1 394 ? 55.249  -49.655 49.433  1.00 24.83 ? 411  ASN A OD1 1 
ATOM   3140  N  ND2 . ASN A  1 394 ? 54.311  -48.264 50.925  1.00 25.92 ? 411  ASN A ND2 1 
ATOM   3141  N  N   . GLU A  1 395 ? 59.730  -47.391 49.899  1.00 30.36 ? 412  GLU A N   1 
ATOM   3142  C  CA  . GLU A  1 395 ? 60.780  -46.423 49.635  1.00 31.95 ? 412  GLU A CA  1 
ATOM   3143  C  C   . GLU A  1 395 ? 60.176  -45.160 49.023  1.00 29.83 ? 412  GLU A C   1 
ATOM   3144  O  O   . GLU A  1 395 ? 60.571  -44.058 49.390  1.00 29.33 ? 412  GLU A O   1 
ATOM   3145  C  CB  . GLU A  1 395 ? 61.847  -47.052 48.738  1.00 34.78 ? 412  GLU A CB  1 
ATOM   3146  C  CG  . GLU A  1 395 ? 63.017  -46.124 48.419  1.00 37.59 ? 412  GLU A CG  1 
ATOM   3147  C  CD  . GLU A  1 395 ? 63.786  -45.603 49.621  1.00 40.41 ? 412  GLU A CD  1 
ATOM   3148  O  OE1 . GLU A  1 395 ? 63.978  -46.367 50.593  1.00 44.30 ? 412  GLU A OE1 1 
ATOM   3149  O  OE2 . GLU A  1 395 ? 64.220  -44.434 49.566  1.00 43.40 ? 412  GLU A OE2 1 
ATOM   3150  N  N   . ARG A  1 396 ? 59.225  -45.326 48.093  1.00 28.93 ? 413  ARG A N   1 
ATOM   3151  C  CA  . ARG A  1 396 ? 58.575  -44.198 47.438  1.00 27.83 ? 413  ARG A CA  1 
ATOM   3152  C  C   . ARG A  1 396 ? 57.059  -44.371 47.531  1.00 27.26 ? 413  ARG A C   1 
ATOM   3153  O  O   . ARG A  1 396 ? 56.419  -44.811 46.579  1.00 26.10 ? 413  ARG A O   1 
ATOM   3154  C  CB  . ARG A  1 396 ? 58.994  -44.070 45.969  1.00 27.57 ? 413  ARG A CB  1 
ATOM   3155  C  CG  . ARG A  1 396 ? 60.494  -43.981 45.719  1.00 28.22 ? 413  ARG A CG  1 
ATOM   3156  C  CD  . ARG A  1 396 ? 61.122  -42.743 46.344  1.00 29.02 ? 413  ARG A CD  1 
ATOM   3157  N  NE  . ARG A  1 396 ? 60.631  -41.472 45.797  1.00 29.92 ? 413  ARG A NE  1 
ATOM   3158  C  CZ  . ARG A  1 396 ? 60.985  -40.918 44.635  1.00 32.85 ? 413  ARG A CZ  1 
ATOM   3159  N  NH1 . ARG A  1 396 ? 61.808  -41.540 43.806  1.00 35.45 ? 413  ARG A NH1 1 
ATOM   3160  N  NH2 . ARG A  1 396 ? 60.506  -39.735 44.300  1.00 34.05 ? 413  ARG A NH2 1 
ATOM   3161  N  N   . PRO A  1 397 ? 56.428  -44.031 48.677  1.00 26.74 ? 414  PRO A N   1 
ATOM   3162  C  CA  . PRO A  1 397 ? 54.997  -44.285 48.853  1.00 26.78 ? 414  PRO A CA  1 
ATOM   3163  C  C   . PRO A  1 397 ? 54.185  -43.333 47.980  1.00 24.36 ? 414  PRO A C   1 
ATOM   3164  O  O   . PRO A  1 397 ? 54.532  -42.160 47.837  1.00 24.46 ? 414  PRO A O   1 
ATOM   3165  C  CB  . PRO A  1 397 ? 54.784  -44.055 50.362  1.00 27.02 ? 414  PRO A CB  1 
ATOM   3166  C  CG  . PRO A  1 397 ? 55.831  -43.017 50.718  1.00 27.71 ? 414  PRO A CG  1 
ATOM   3167  C  CD  . PRO A  1 397 ? 57.034  -43.368 49.843  1.00 27.81 ? 414  PRO A CD  1 
ATOM   3168  N  N   . VAL A  1 398 ? 53.104  -43.855 47.397  1.00 23.22 ? 415  VAL A N   1 
ATOM   3169  C  CA  . VAL A  1 398 ? 52.203  -43.056 46.585  1.00 21.34 ? 415  VAL A CA  1 
ATOM   3170  C  C   . VAL A  1 398 ? 51.018  -42.664 47.463  1.00 20.37 ? 415  VAL A C   1 
ATOM   3171  O  O   . VAL A  1 398 ? 50.330  -43.525 47.999  1.00 20.14 ? 415  VAL A O   1 
ATOM   3172  C  CB  . VAL A  1 398 ? 51.755  -43.810 45.315  1.00 21.32 ? 415  VAL A CB  1 
ATOM   3173  C  CG1 . VAL A  1 398 ? 50.800  -42.986 44.457  1.00 20.89 ? 415  VAL A CG1 1 
ATOM   3174  C  CG2 . VAL A  1 398 ? 52.940  -44.260 44.472  1.00 22.28 ? 415  VAL A CG2 1 
ATOM   3175  N  N   . ILE A  1 399 ? 50.811  -41.358 47.627  1.00 20.09 ? 416  ILE A N   1 
ATOM   3176  C  CA  . ILE A  1 399 ? 49.786  -40.843 48.520  1.00 20.93 ? 416  ILE A CA  1 
ATOM   3177  C  C   . ILE A  1 399 ? 48.947  -39.829 47.748  1.00 20.65 ? 416  ILE A C   1 
ATOM   3178  O  O   . ILE A  1 399 ? 49.437  -38.754 47.415  1.00 20.81 ? 416  ILE A O   1 
ATOM   3179  C  CB  . ILE A  1 399 ? 50.421  -40.228 49.785  1.00 21.08 ? 416  ILE A CB  1 
ATOM   3180  C  CG1 . ILE A  1 399 ? 51.320  -41.238 50.521  1.00 22.34 ? 416  ILE A CG1 1 
ATOM   3181  C  CG2 . ILE A  1 399 ? 49.351  -39.639 50.704  1.00 22.04 ? 416  ILE A CG2 1 
ATOM   3182  C  CD1 . ILE A  1 399 ? 51.974  -40.697 51.780  1.00 23.23 ? 416  ILE A CD1 1 
ATOM   3183  N  N   . PHE A  1 400 ? 47.685  -40.187 47.476  1.00 20.59 ? 417  PHE A N   1 
ATOM   3184  C  CA  . PHE A  1 400 ? 46.748  -39.308 46.797  1.00 21.19 ? 417  PHE A CA  1 
ATOM   3185  C  C   . PHE A  1 400 ? 45.646  -38.889 47.771  1.00 21.50 ? 417  PHE A C   1 
ATOM   3186  O  O   . PHE A  1 400 ? 44.881  -39.729 48.241  1.00 21.24 ? 417  PHE A O   1 
ATOM   3187  C  CB  . PHE A  1 400 ? 46.147  -40.014 45.575  1.00 22.77 ? 417  PHE A CB  1 
ATOM   3188  C  CG  . PHE A  1 400 ? 46.997  -40.046 44.309  1.00 24.59 ? 417  PHE A CG  1 
ATOM   3189  C  CD1 . PHE A  1 400 ? 48.389  -40.103 44.364  1.00 25.96 ? 417  PHE A CD1 1 
ATOM   3190  C  CD2 . PHE A  1 400 ? 46.393  -40.034 43.054  1.00 25.79 ? 417  PHE A CD2 1 
ATOM   3191  C  CE1 . PHE A  1 400 ? 49.147  -40.140 43.202  1.00 26.54 ? 417  PHE A CE1 1 
ATOM   3192  C  CE2 . PHE A  1 400 ? 47.157  -40.066 41.897  1.00 26.31 ? 417  PHE A CE2 1 
ATOM   3193  C  CZ  . PHE A  1 400 ? 48.531  -40.119 41.971  1.00 26.20 ? 417  PHE A CZ  1 
ATOM   3194  N  N   . ALA A  1 401 ? 45.551  -37.579 48.034  1.00 21.97 ? 418  ALA A N   1 
ATOM   3195  C  CA  . ALA A  1 401 ? 44.542  -37.029 48.927  1.00 22.67 ? 418  ALA A CA  1 
ATOM   3196  C  C   . ALA A  1 401 ? 43.529  -36.226 48.112  1.00 23.07 ? 418  ALA A C   1 
ATOM   3197  O  O   . ALA A  1 401 ? 43.732  -35.039 47.876  1.00 23.75 ? 418  ALA A O   1 
ATOM   3198  C  CB  . ALA A  1 401 ? 45.217  -36.180 49.986  1.00 22.31 ? 418  ALA A CB  1 
ATOM   3199  N  N   . LEU A  1 402 ? 42.431  -36.877 47.695  1.00 23.68 ? 419  LEU A N   1 
ATOM   3200  C  CA  . LEU A  1 402 ? 41.610  -36.356 46.609  1.00 23.39 ? 419  LEU A CA  1 
ATOM   3201  C  C   . LEU A  1 402 ? 40.305  -35.739 47.115  1.00 24.87 ? 419  LEU A C   1 
ATOM   3202  O  O   . LEU A  1 402 ? 39.517  -35.242 46.313  1.00 26.43 ? 419  LEU A O   1 
ATOM   3203  C  CB  . LEU A  1 402 ? 41.322  -37.457 45.588  1.00 22.88 ? 419  LEU A CB  1 
ATOM   3204  C  CG  . LEU A  1 402 ? 42.529  -38.108 44.904  1.00 23.71 ? 419  LEU A CG  1 
ATOM   3205  C  CD1 . LEU A  1 402 ? 42.060  -39.061 43.816  1.00 23.50 ? 419  LEU A CD1 1 
ATOM   3206  C  CD2 . LEU A  1 402 ? 43.473  -37.082 44.306  1.00 24.98 ? 419  LEU A CD2 1 
ATOM   3207  N  N   . SER A  1 403 ? 40.062  -35.744 48.430  1.00 25.15 ? 420  SER A N   1 
ATOM   3208  C  CA  . SER A  1 403 ? 38.780  -35.280 48.931  1.00 24.96 ? 420  SER A CA  1 
ATOM   3209  C  C   . SER A  1 403 ? 38.671  -33.762 48.781  1.00 27.01 ? 420  SER A C   1 
ATOM   3210  O  O   . SER A  1 403 ? 39.681  -33.063 48.788  1.00 25.79 ? 420  SER A O   1 
ATOM   3211  C  CB  . SER A  1 403 ? 38.541  -35.736 50.342  1.00 24.32 ? 420  SER A CB  1 
ATOM   3212  O  OG  . SER A  1 403 ? 38.245  -37.128 50.366  1.00 23.17 ? 420  SER A OG  1 
ATOM   3213  N  N   . ASN A  1 404 ? 37.431  -33.285 48.606  1.00 29.80 ? 421  ASN A N   1 
ATOM   3214  C  CA  . ASN A  1 404 ? 37.112  -31.873 48.434  1.00 33.98 ? 421  ASN A CA  1 
ATOM   3215  C  C   . ASN A  1 404 ? 35.995  -31.483 49.397  1.00 35.06 ? 421  ASN A C   1 
ATOM   3216  O  O   . ASN A  1 404 ? 35.199  -32.336 49.785  1.00 32.24 ? 421  ASN A O   1 
ATOM   3217  C  CB  . ASN A  1 404 ? 36.619  -31.548 47.027  1.00 36.28 ? 421  ASN A CB  1 
ATOM   3218  C  CG  . ASN A  1 404 ? 37.565  -32.017 45.947  1.00 38.12 ? 421  ASN A CG  1 
ATOM   3219  O  OD1 . ASN A  1 404 ? 38.712  -31.560 45.878  1.00 38.33 ? 421  ASN A OD1 1 
ATOM   3220  N  ND2 . ASN A  1 404 ? 37.103  -32.923 45.096  1.00 39.91 ? 421  ASN A ND2 1 
ATOM   3221  N  N   . PRO A  1 405 ? 35.885  -30.200 49.824  1.00 38.82 ? 422  PRO A N   1 
ATOM   3222  C  CA  . PRO A  1 405 ? 36.914  -29.179 49.587  1.00 37.58 ? 422  PRO A CA  1 
ATOM   3223  C  C   . PRO A  1 405 ? 38.172  -29.380 50.436  1.00 37.99 ? 422  PRO A C   1 
ATOM   3224  O  O   . PRO A  1 405 ? 38.308  -30.401 51.105  1.00 36.88 ? 422  PRO A O   1 
ATOM   3225  C  CB  . PRO A  1 405 ? 36.157  -27.881 49.934  1.00 37.56 ? 422  PRO A CB  1 
ATOM   3226  C  CG  . PRO A  1 405 ? 35.180  -28.301 51.007  1.00 39.26 ? 422  PRO A CG  1 
ATOM   3227  C  CD  . PRO A  1 405 ? 34.716  -29.673 50.552  1.00 39.23 ? 422  PRO A CD  1 
ATOM   3228  N  N   . THR A  1 406 ? 39.081  -28.393 50.407  1.00 38.13 ? 423  THR A N   1 
ATOM   3229  C  CA  . THR A  1 406 ? 40.407  -28.506 51.004  1.00 40.14 ? 423  THR A CA  1 
ATOM   3230  C  C   . THR A  1 406 ? 40.336  -28.950 52.467  1.00 39.05 ? 423  THR A C   1 
ATOM   3231  O  O   . THR A  1 406 ? 41.186  -29.711 52.920  1.00 38.25 ? 423  THR A O   1 
ATOM   3232  C  CB  . THR A  1 406 ? 41.137  -27.170 50.874  1.00 41.98 ? 423  THR A CB  1 
ATOM   3233  O  OG1 . THR A  1 406 ? 40.957  -26.780 49.516  1.00 45.30 ? 423  THR A OG1 1 
ATOM   3234  C  CG2 . THR A  1 406 ? 42.615  -27.277 51.204  1.00 41.75 ? 423  THR A CG2 1 
ATOM   3235  N  N   . ALA A  1 407 ? 39.335  -28.464 53.207  1.00 39.20 ? 424  ALA A N   1 
ATOM   3236  C  CA  . ALA A  1 407 ? 39.181  -28.830 54.608  1.00 40.75 ? 424  ALA A CA  1 
ATOM   3237  C  C   . ALA A  1 407 ? 38.969  -30.337 54.761  1.00 38.74 ? 424  ALA A C   1 
ATOM   3238  O  O   . ALA A  1 407 ? 39.332  -30.903 55.792  1.00 38.80 ? 424  ALA A O   1 
ATOM   3239  C  CB  . ALA A  1 407 ? 38.041  -28.046 55.229  1.00 40.91 ? 424  ALA A CB  1 
ATOM   3240  N  N   . GLN A  1 408 ? 38.381  -30.979 53.739  1.00 36.05 ? 425  GLN A N   1 
ATOM   3241  C  CA  . GLN A  1 408 ? 38.038  -32.392 53.808  1.00 34.79 ? 425  GLN A CA  1 
ATOM   3242  C  C   . GLN A  1 408 ? 39.171  -33.281 53.287  1.00 30.71 ? 425  GLN A C   1 
ATOM   3243  O  O   . GLN A  1 408 ? 39.046  -34.500 53.340  1.00 29.70 ? 425  GLN A O   1 
ATOM   3244  C  CB  . GLN A  1 408 ? 36.761  -32.698 53.022  1.00 37.61 ? 425  GLN A CB  1 
ATOM   3245  C  CG  . GLN A  1 408 ? 35.531  -31.920 53.481  1.00 39.82 ? 425  GLN A CG  1 
ATOM   3246  C  CD  . GLN A  1 408 ? 35.350  -31.918 54.982  1.00 43.48 ? 425  GLN A CD  1 
ATOM   3247  O  OE1 . GLN A  1 408 ? 35.264  -30.859 55.613  1.00 45.27 ? 425  GLN A OE1 1 
ATOM   3248  N  NE2 . GLN A  1 408 ? 35.303  -33.106 55.570  1.00 43.65 ? 425  GLN A NE2 1 
ATOM   3249  N  N   . ALA A  1 409 ? 40.261  -32.684 52.786  1.00 28.23 ? 426  ALA A N   1 
ATOM   3250  C  CA  . ALA A  1 409 ? 41.376  -33.438 52.232  1.00 27.18 ? 426  ALA A CA  1 
ATOM   3251  C  C   . ALA A  1 409 ? 42.049  -34.282 53.315  1.00 26.41 ? 426  ALA A C   1 
ATOM   3252  O  O   . ALA A  1 409 ? 42.125  -33.871 54.471  1.00 28.22 ? 426  ALA A O   1 
ATOM   3253  C  CB  . ALA A  1 409 ? 42.365  -32.501 51.577  1.00 26.71 ? 426  ALA A CB  1 
ATOM   3254  N  N   . GLU A  1 410 ? 42.568  -35.449 52.909  1.00 24.85 ? 427  GLU A N   1 
ATOM   3255  C  CA  . GLU A  1 410 ? 43.072  -36.455 53.833  1.00 24.45 ? 427  GLU A CA  1 
ATOM   3256  C  C   . GLU A  1 410 ? 44.388  -36.015 54.476  1.00 25.19 ? 427  GLU A C   1 
ATOM   3257  O  O   . GLU A  1 410 ? 44.680  -36.439 55.590  1.00 24.25 ? 427  GLU A O   1 
ATOM   3258  C  CB  . GLU A  1 410 ? 43.222  -37.814 53.148  1.00 23.97 ? 427  GLU A CB  1 
ATOM   3259  C  CG  . GLU A  1 410 ? 41.896  -38.520 52.882  1.00 23.78 ? 427  GLU A CG  1 
ATOM   3260  C  CD  . GLU A  1 410 ? 41.041  -37.998 51.737  1.00 24.05 ? 427  GLU A CD  1 
ATOM   3261  O  OE1 . GLU A  1 410 ? 41.510  -37.158 50.930  1.00 24.11 ? 427  GLU A OE1 1 
ATOM   3262  O  OE2 . GLU A  1 410 ? 39.874  -38.448 51.660  1.00 23.47 ? 427  GLU A OE2 1 
ATOM   3263  N  N   . CYS A  1 411 ? 45.183  -35.202 53.763  1.00 26.41 ? 428  CYS A N   1 
ATOM   3264  C  CA  . CYS A  1 411 ? 46.367  -34.560 54.315  1.00 27.81 ? 428  CYS A CA  1 
ATOM   3265  C  C   . CYS A  1 411 ? 46.792  -33.419 53.394  1.00 29.12 ? 428  CYS A C   1 
ATOM   3266  O  O   . CYS A  1 411 ? 46.235  -33.273 52.306  1.00 29.14 ? 428  CYS A O   1 
ATOM   3267  C  CB  . CYS A  1 411 ? 47.522  -35.538 54.518  1.00 29.04 ? 428  CYS A CB  1 
ATOM   3268  S  SG  . CYS A  1 411 ? 48.198  -36.243 52.988  1.00 29.80 ? 428  CYS A SG  1 
ATOM   3269  N  N   . THR A  1 412 ? 47.771  -32.619 53.845  1.00 27.91 ? 429  THR A N   1 
ATOM   3270  C  CA  . THR A  1 412 ? 48.336  -31.545 53.040  1.00 28.82 ? 429  THR A CA  1 
ATOM   3271  C  C   . THR A  1 412 ? 49.607  -32.034 52.355  1.00 27.88 ? 429  THR A C   1 
ATOM   3272  O  O   . THR A  1 412 ? 50.180  -33.048 52.749  1.00 29.00 ? 429  THR A O   1 
ATOM   3273  C  CB  . THR A  1 412 ? 48.641  -30.316 53.901  1.00 30.17 ? 429  THR A CB  1 
ATOM   3274  O  OG1 . THR A  1 412 ? 49.721  -30.684 54.752  1.00 29.90 ? 429  THR A OG1 1 
ATOM   3275  C  CG2 . THR A  1 412 ? 47.445  -29.848 54.709  1.00 30.80 ? 429  THR A CG2 1 
ATOM   3276  N  N   . ALA A  1 413 ? 50.057  -31.272 51.351  1.00 28.13 ? 430  ALA A N   1 
ATOM   3277  C  CA  . ALA A  1 413 ? 51.329  -31.526 50.692  1.00 29.45 ? 430  ALA A CA  1 
ATOM   3278  C  C   . ALA A  1 413 ? 52.478  -31.374 51.686  1.00 30.00 ? 430  ALA A C   1 
ATOM   3279  O  O   . ALA A  1 413 ? 53.401  -32.184 51.694  1.00 28.62 ? 430  ALA A O   1 
ATOM   3280  C  CB  . ALA A  1 413 ? 51.500  -30.597 49.510  1.00 29.80 ? 430  ALA A CB  1 
ATOM   3281  N  N   . GLU A  1 414 ? 52.415  -30.333 52.523  1.00 33.63 ? 431  GLU A N   1 
ATOM   3282  C  CA  A GLU A  1 414 ? 53.433  -30.090 53.536  0.55 34.60 ? 431  GLU A CA  1 
ATOM   3283  C  CA  B GLU A  1 414 ? 53.454  -30.101 53.514  0.45 33.97 ? 431  GLU A CA  1 
ATOM   3284  C  C   . GLU A  1 414 ? 53.606  -31.349 54.384  1.00 33.26 ? 431  GLU A C   1 
ATOM   3285  O  O   . GLU A  1 414 ? 54.720  -31.826 54.583  1.00 31.73 ? 431  GLU A O   1 
ATOM   3286  C  CB  A GLU A  1 414 ? 53.045  -28.917 54.440  0.55 36.97 ? 431  GLU A CB  1 
ATOM   3287  C  CB  B GLU A  1 414 ? 53.165  -28.859 54.359  0.45 35.41 ? 431  GLU A CB  1 
ATOM   3288  C  CG  A GLU A  1 414 ? 52.963  -27.562 53.739  0.55 38.37 ? 431  GLU A CG  1 
ATOM   3289  C  CG  B GLU A  1 414 ? 54.358  -28.413 55.200  0.45 36.25 ? 431  GLU A CG  1 
ATOM   3290  C  CD  A GLU A  1 414 ? 54.260  -26.791 53.570  0.55 40.29 ? 431  GLU A CD  1 
ATOM   3291  C  CD  B GLU A  1 414 ? 54.017  -27.380 56.258  0.45 36.88 ? 431  GLU A CD  1 
ATOM   3292  O  OE1 A GLU A  1 414 ? 55.339  -27.299 53.948  0.55 42.24 ? 431  GLU A OE1 1 
ATOM   3293  O  OE1 B GLU A  1 414 ? 54.317  -27.641 57.440  0.45 38.69 ? 431  GLU A OE1 1 
ATOM   3294  O  OE2 A GLU A  1 414 ? 54.174  -25.660 53.042  0.55 40.41 ? 431  GLU A OE2 1 
ATOM   3295  O  OE2 B GLU A  1 414 ? 53.444  -26.328 55.907  0.45 36.85 ? 431  GLU A OE2 1 
ATOM   3296  N  N   . GLU A  1 415 ? 52.480  -31.885 54.879  1.00 32.60 ? 432  GLU A N   1 
ATOM   3297  C  CA  . GLU A  1 415 ? 52.496  -33.072 55.723  1.00 32.37 ? 432  GLU A CA  1 
ATOM   3298  C  C   . GLU A  1 415 ? 53.133  -34.248 54.985  1.00 30.02 ? 432  GLU A C   1 
ATOM   3299  O  O   . GLU A  1 415 ? 53.936  -34.971 55.564  1.00 30.68 ? 432  GLU A O   1 
ATOM   3300  C  CB  . GLU A  1 415 ? 51.090  -33.434 56.206  1.00 33.91 ? 432  GLU A CB  1 
ATOM   3301  C  CG  . GLU A  1 415 ? 50.548  -32.475 57.264  1.00 35.75 ? 432  GLU A CG  1 
ATOM   3302  C  CD  . GLU A  1 415 ? 49.048  -32.551 57.517  1.00 38.97 ? 432  GLU A CD  1 
ATOM   3303  O  OE1 . GLU A  1 415 ? 48.568  -31.845 58.436  1.00 40.55 ? 432  GLU A OE1 1 
ATOM   3304  O  OE2 . GLU A  1 415 ? 48.347  -33.295 56.797  1.00 37.88 ? 432  GLU A OE2 1 
ATOM   3305  N  N   . ALA A  1 416 ? 52.780  -34.429 53.706  1.00 29.86 ? 433  ALA A N   1 
ATOM   3306  C  CA  . ALA A  1 416 ? 53.190  -35.604 52.951  1.00 28.75 ? 433  ALA A CA  1 
ATOM   3307  C  C   . ALA A  1 416 ? 54.693  -35.599 52.684  1.00 28.58 ? 433  ALA A C   1 
ATOM   3308  O  O   . ALA A  1 416 ? 55.349  -36.621 52.859  1.00 28.75 ? 433  ALA A O   1 
ATOM   3309  C  CB  . ALA A  1 416 ? 52.411  -35.687 51.659  1.00 29.54 ? 433  ALA A CB  1 
ATOM   3310  N  N   . TYR A  1 417 ? 55.237  -34.458 52.244  1.00 29.46 ? 434  TYR A N   1 
ATOM   3311  C  CA  . TYR A  1 417 ? 56.644  -34.406 51.873  1.00 31.48 ? 434  TYR A CA  1 
ATOM   3312  C  C   . TYR A  1 417 ? 57.539  -34.406 53.116  1.00 32.00 ? 434  TYR A C   1 
ATOM   3313  O  O   . TYR A  1 417 ? 58.564  -35.088 53.122  1.00 31.34 ? 434  TYR A O   1 
ATOM   3314  C  CB  . TYR A  1 417 ? 56.928  -33.224 50.942  1.00 32.85 ? 434  TYR A CB  1 
ATOM   3315  C  CG  . TYR A  1 417 ? 56.368  -33.402 49.537  1.00 32.29 ? 434  TYR A CG  1 
ATOM   3316  C  CD1 . TYR A  1 417 ? 56.873  -34.373 48.677  1.00 33.48 ? 434  TYR A CD1 1 
ATOM   3317  C  CD2 . TYR A  1 417 ? 55.351  -32.587 49.065  1.00 33.41 ? 434  TYR A CD2 1 
ATOM   3318  C  CE1 . TYR A  1 417 ? 56.370  -34.537 47.395  1.00 32.88 ? 434  TYR A CE1 1 
ATOM   3319  C  CE2 . TYR A  1 417 ? 54.839  -32.740 47.787  1.00 34.98 ? 434  TYR A CE2 1 
ATOM   3320  C  CZ  . TYR A  1 417 ? 55.350  -33.715 46.948  1.00 33.14 ? 434  TYR A CZ  1 
ATOM   3321  O  OH  . TYR A  1 417 ? 54.838  -33.851 45.689  1.00 33.55 ? 434  TYR A OH  1 
ATOM   3322  N  N   . THR A  1 418 ? 57.159  -33.661 54.163  1.00 32.30 ? 435  THR A N   1 
ATOM   3323  C  CA  . THR A  1 418 ? 58.014  -33.533 55.339  1.00 34.89 ? 435  THR A CA  1 
ATOM   3324  C  C   . THR A  1 418 ? 58.107  -34.869 56.078  1.00 33.46 ? 435  THR A C   1 
ATOM   3325  O  O   . THR A  1 418 ? 59.202  -35.286 56.443  1.00 32.12 ? 435  THR A O   1 
ATOM   3326  C  CB  . THR A  1 418 ? 57.537  -32.408 56.259  1.00 37.74 ? 435  THR A CB  1 
ATOM   3327  O  OG1 . THR A  1 418 ? 56.185  -32.683 56.608  1.00 43.33 ? 435  THR A OG1 1 
ATOM   3328  C  CG2 . THR A  1 418 ? 57.622  -31.040 55.608  1.00 38.18 ? 435  THR A CG2 1 
ATOM   3329  N  N   . LEU A  1 419 ? 56.972  -35.558 56.261  1.00 32.43 ? 436  LEU A N   1 
ATOM   3330  C  CA  . LEU A  1 419 ? 56.931  -36.760 57.084  1.00 32.38 ? 436  LEU A CA  1 
ATOM   3331  C  C   . LEU A  1 419 ? 57.442  -37.986 56.333  1.00 33.14 ? 436  LEU A C   1 
ATOM   3332  O  O   . LEU A  1 419 ? 57.664  -39.019 56.961  1.00 33.84 ? 436  LEU A O   1 
ATOM   3333  C  CB  . LEU A  1 419 ? 55.516  -36.999 57.606  1.00 33.45 ? 436  LEU A CB  1 
ATOM   3334  C  CG  . LEU A  1 419 ? 54.942  -35.908 58.511  1.00 33.97 ? 436  LEU A CG  1 
ATOM   3335  C  CD1 . LEU A  1 419 ? 53.480  -36.182 58.792  1.00 34.52 ? 436  LEU A CD1 1 
ATOM   3336  C  CD2 . LEU A  1 419 ? 55.719  -35.794 59.816  1.00 36.99 ? 436  LEU A CD2 1 
ATOM   3337  N  N   . THR A  1 420 ? 57.609  -37.894 55.003  1.00 31.88 ? 437  THR A N   1 
ATOM   3338  C  CA  . THR A  1 420 ? 58.234  -38.972 54.247  1.00 32.69 ? 437  THR A CA  1 
ATOM   3339  C  C   . THR A  1 420 ? 59.663  -38.594 53.848  1.00 34.55 ? 437  THR A C   1 
ATOM   3340  O  O   . THR A  1 420 ? 60.293  -39.321 53.086  1.00 34.72 ? 437  THR A O   1 
ATOM   3341  C  CB  . THR A  1 420 ? 57.384  -39.331 53.026  1.00 31.10 ? 437  THR A CB  1 
ATOM   3342  O  OG1 . THR A  1 420 ? 57.327  -38.168 52.203  1.00 29.67 ? 437  THR A OG1 1 
ATOM   3343  C  CG2 . THR A  1 420 ? 55.986  -39.781 53.418  1.00 31.20 ? 437  THR A CG2 1 
ATOM   3344  N  N   . GLU A  1 421 ? 60.174  -37.469 54.367  1.00 38.55 ? 438  GLU A N   1 
ATOM   3345  C  CA  . GLU A  1 421 ? 61.524  -37.004 54.070  1.00 40.90 ? 438  GLU A CA  1 
ATOM   3346  C  C   . GLU A  1 421 ? 61.715  -36.866 52.558  1.00 39.84 ? 438  GLU A C   1 
ATOM   3347  O  O   . GLU A  1 421 ? 62.780  -37.184 52.029  1.00 38.27 ? 438  GLU A O   1 
ATOM   3348  C  CB  . GLU A  1 421 ? 62.568  -37.927 54.706  1.00 44.81 ? 438  GLU A CB  1 
ATOM   3349  C  CG  . GLU A  1 421 ? 62.480  -37.987 56.229  1.00 49.15 ? 438  GLU A CG  1 
ATOM   3350  C  CD  . GLU A  1 421 ? 63.564  -38.824 56.889  1.00 53.85 ? 438  GLU A CD  1 
ATOM   3351  O  OE1 . GLU A  1 421 ? 63.581  -40.055 56.671  1.00 56.68 ? 438  GLU A OE1 1 
ATOM   3352  O  OE2 . GLU A  1 421 ? 64.402  -38.243 57.610  1.00 56.34 ? 438  GLU A OE2 1 
ATOM   3353  N  N   . GLY A  1 422 ? 60.662  -36.394 51.877  1.00 39.14 ? 439  GLY A N   1 
ATOM   3354  C  CA  . GLY A  1 422 ? 60.712  -36.070 50.461  1.00 37.78 ? 439  GLY A CA  1 
ATOM   3355  C  C   . GLY A  1 422 ? 60.598  -37.292 49.551  1.00 35.94 ? 439  GLY A C   1 
ATOM   3356  O  O   . GLY A  1 422 ? 60.851  -37.178 48.357  1.00 36.96 ? 439  GLY A O   1 
ATOM   3357  N  N   . ARG A  1 423 ? 60.192  -38.445 50.095  1.00 33.77 ? 440  ARG A N   1 
ATOM   3358  C  CA  . ARG A  1 423 ? 60.202  -39.685 49.334  1.00 32.53 ? 440  ARG A CA  1 
ATOM   3359  C  C   . ARG A  1 423 ? 58.835  -39.985 48.709  1.00 31.19 ? 440  ARG A C   1 
ATOM   3360  O  O   . ARG A  1 423 ? 58.749  -40.816 47.809  1.00 29.67 ? 440  ARG A O   1 
ATOM   3361  C  CB  . ARG A  1 423 ? 60.688  -40.844 50.211  1.00 33.64 ? 440  ARG A CB  1 
ATOM   3362  C  CG  . ARG A  1 423 ? 62.184  -40.800 50.496  1.00 33.86 ? 440  ARG A CG  1 
ATOM   3363  C  CD  . ARG A  1 423 ? 62.680  -42.051 51.208  1.00 35.27 ? 440  ARG A CD  1 
ATOM   3364  N  NE  . ARG A  1 423 ? 62.202  -42.144 52.593  1.00 36.15 ? 440  ARG A NE  1 
ATOM   3365  C  CZ  . ARG A  1 423 ? 61.395  -43.071 53.108  1.00 37.86 ? 440  ARG A CZ  1 
ATOM   3366  N  NH1 . ARG A  1 423 ? 60.822  -43.988 52.344  1.00 36.07 ? 440  ARG A NH1 1 
ATOM   3367  N  NH2 . ARG A  1 423 ? 61.141  -43.059 54.408  1.00 38.29 ? 440  ARG A NH2 1 
ATOM   3368  N  N   . CYS A  1 424 ? 57.767  -39.322 49.165  1.00 30.46 ? 441  CYS A N   1 
ATOM   3369  C  CA  . CYS A  1 424 ? 56.432  -39.657 48.692  1.00 30.52 ? 441  CYS A CA  1 
ATOM   3370  C  C   . CYS A  1 424 ? 56.204  -39.100 47.285  1.00 29.82 ? 441  CYS A C   1 
ATOM   3371  O  O   . CYS A  1 424 ? 56.751  -38.064 46.919  1.00 29.90 ? 441  CYS A O   1 
ATOM   3372  C  CB  . CYS A  1 424 ? 55.352  -39.148 49.637  1.00 31.08 ? 441  CYS A CB  1 
ATOM   3373  S  SG  . CYS A  1 424 ? 55.272  -37.343 49.753  1.00 34.81 ? 441  CYS A SG  1 
ATOM   3374  N  N   . LEU A  1 425 ? 55.407  -39.828 46.497  1.00 28.35 ? 442  LEU A N   1 
ATOM   3375  C  CA  . LEU A  1 425 ? 54.833  -39.308 45.269  1.00 28.30 ? 442  LEU A CA  1 
ATOM   3376  C  C   . LEU A  1 425 ? 53.395  -38.913 45.584  1.00 26.20 ? 442  LEU A C   1 
ATOM   3377  O  O   . LEU A  1 425 ? 52.574  -39.781 45.868  1.00 26.60 ? 442  LEU A O   1 
ATOM   3378  C  CB  . LEU A  1 425 ? 54.923  -40.372 44.177  1.00 30.16 ? 442  LEU A CB  1 
ATOM   3379  C  CG  . LEU A  1 425 ? 56.342  -40.802 43.783  1.00 32.34 ? 442  LEU A CG  1 
ATOM   3380  C  CD1 . LEU A  1 425 ? 56.299  -41.969 42.823  1.00 33.92 ? 442  LEU A CD1 1 
ATOM   3381  C  CD2 . LEU A  1 425 ? 57.127  -39.654 43.176  1.00 32.82 ? 442  LEU A CD2 1 
ATOM   3382  N  N   . PHE A  1 426 ? 53.123  -37.604 45.574  1.00 24.89 ? 443  PHE A N   1 
ATOM   3383  C  CA  . PHE A  1 426 ? 51.913  -37.062 46.171  1.00 24.87 ? 443  PHE A CA  1 
ATOM   3384  C  C   . PHE A  1 426 ? 51.083  -36.332 45.121  1.00 25.90 ? 443  PHE A C   1 
ATOM   3385  O  O   . PHE A  1 426 ? 51.625  -35.681 44.227  1.00 25.92 ? 443  PHE A O   1 
ATOM   3386  C  CB  . PHE A  1 426 ? 52.257  -36.121 47.331  1.00 24.86 ? 443  PHE A CB  1 
ATOM   3387  C  CG  . PHE A  1 426 ? 51.054  -35.409 47.934  1.00 24.31 ? 443  PHE A CG  1 
ATOM   3388  C  CD1 . PHE A  1 426 ? 50.275  -36.027 48.905  1.00 25.42 ? 443  PHE A CD1 1 
ATOM   3389  C  CD2 . PHE A  1 426 ? 50.687  -34.137 47.506  1.00 25.37 ? 443  PHE A CD2 1 
ATOM   3390  C  CE1 . PHE A  1 426 ? 49.170  -35.382 49.443  1.00 26.02 ? 443  PHE A CE1 1 
ATOM   3391  C  CE2 . PHE A  1 426 ? 49.582  -33.495 48.045  1.00 25.61 ? 443  PHE A CE2 1 
ATOM   3392  C  CZ  . PHE A  1 426 ? 48.830  -34.115 49.018  1.00 25.57 ? 443  PHE A CZ  1 
ATOM   3393  N  N   . ALA A  1 427 ? 49.755  -36.433 45.272  1.00 24.69 ? 444  ALA A N   1 
ATOM   3394  C  CA  . ALA A  1 427 ? 48.821  -35.625 44.507  1.00 23.94 ? 444  ALA A CA  1 
ATOM   3395  C  C   . ALA A  1 427 ? 47.582  -35.349 45.357  1.00 24.72 ? 444  ALA A C   1 
ATOM   3396  O  O   . ALA A  1 427 ? 47.232  -36.133 46.241  1.00 24.37 ? 444  ALA A O   1 
ATOM   3397  C  CB  . ALA A  1 427 ? 48.462  -36.323 43.208  1.00 24.09 ? 444  ALA A CB  1 
ATOM   3398  N  N   . SER A  1 428 ? 46.920  -34.225 45.078  1.00 24.48 ? 445  SER A N   1 
ATOM   3399  C  CA  . SER A  1 428 ? 45.672  -33.895 45.741  1.00 26.07 ? 445  SER A CA  1 
ATOM   3400  C  C   . SER A  1 428 ? 44.703  -33.290 44.733  1.00 27.34 ? 445  SER A C   1 
ATOM   3401  O  O   . SER A  1 428 ? 45.077  -33.005 43.597  1.00 27.76 ? 445  SER A O   1 
ATOM   3402  C  CB  . SER A  1 428 ? 45.906  -32.962 46.907  1.00 27.70 ? 445  SER A CB  1 
ATOM   3403  O  OG  . SER A  1 428 ? 46.051  -31.617 46.474  1.00 29.42 ? 445  SER A OG  1 
ATOM   3404  N  N   . GLY A  1 429 ? 43.450  -33.112 45.165  1.00 27.82 ? 446  GLY A N   1 
ATOM   3405  C  CA  . GLY A  1 429 ? 42.459  -32.384 44.392  1.00 29.23 ? 446  GLY A CA  1 
ATOM   3406  C  C   . GLY A  1 429 ? 42.366  -30.923 44.828  1.00 31.51 ? 446  GLY A C   1 
ATOM   3407  O  O   . GLY A  1 429 ? 41.509  -30.195 44.339  1.00 34.50 ? 446  GLY A O   1 
ATOM   3408  N  N   . SER A  1 430 ? 43.248  -30.521 45.756  1.00 33.30 ? 447  SER A N   1 
ATOM   3409  C  CA  . SER A  1 430 ? 43.261  -29.191 46.343  1.00 36.34 ? 447  SER A CA  1 
ATOM   3410  C  C   . SER A  1 430 ? 44.473  -28.411 45.837  1.00 39.46 ? 447  SER A C   1 
ATOM   3411  O  O   . SER A  1 430 ? 45.499  -29.002 45.511  1.00 41.13 ? 447  SER A O   1 
ATOM   3412  C  CB  . SER A  1 430 ? 43.292  -29.266 47.854  1.00 36.45 ? 447  SER A CB  1 
ATOM   3413  O  OG  . SER A  1 430 ? 42.122  -29.878 48.375  1.00 38.64 ? 447  SER A OG  1 
ATOM   3414  N  N   . PRO A  1 431 ? 44.413  -27.060 45.799  1.00 43.69 ? 448  PRO A N   1 
ATOM   3415  C  CA  . PRO A  1 431 ? 45.551  -26.253 45.351  1.00 45.65 ? 448  PRO A CA  1 
ATOM   3416  C  C   . PRO A  1 431 ? 46.562  -25.956 46.460  1.00 46.60 ? 448  PRO A C   1 
ATOM   3417  O  O   . PRO A  1 431 ? 46.490  -24.914 47.109  1.00 50.25 ? 448  PRO A O   1 
ATOM   3418  C  CB  . PRO A  1 431 ? 44.818  -24.992 44.851  1.00 44.86 ? 448  PRO A CB  1 
ATOM   3419  C  CG  . PRO A  1 431 ? 43.684  -24.815 45.842  1.00 44.58 ? 448  PRO A CG  1 
ATOM   3420  C  CD  . PRO A  1 431 ? 43.253  -26.237 46.186  1.00 44.91 ? 448  PRO A CD  1 
ATOM   3421  N  N   . PHE A  1 432 ? 47.499  -26.889 46.673  1.00 44.96 ? 449  PHE A N   1 
ATOM   3422  C  CA  . PHE A  1 432 ? 48.613  -26.680 47.585  1.00 42.06 ? 449  PHE A CA  1 
ATOM   3423  C  C   . PHE A  1 432 ? 49.807  -26.173 46.783  1.00 41.51 ? 449  PHE A C   1 
ATOM   3424  O  O   . PHE A  1 432 ? 50.073  -26.667 45.689  1.00 43.14 ? 449  PHE A O   1 
ATOM   3425  C  CB  . PHE A  1 432 ? 49.041  -27.945 48.336  1.00 39.44 ? 449  PHE A CB  1 
ATOM   3426  C  CG  . PHE A  1 432 ? 47.950  -28.594 49.174  1.00 37.88 ? 449  PHE A CG  1 
ATOM   3427  C  CD1 . PHE A  1 432 ? 47.442  -27.953 50.301  1.00 37.07 ? 449  PHE A CD1 1 
ATOM   3428  C  CD2 . PHE A  1 432 ? 47.455  -29.855 48.851  1.00 37.47 ? 449  PHE A CD2 1 
ATOM   3429  C  CE1 . PHE A  1 432 ? 46.447  -28.545 51.064  1.00 36.88 ? 449  PHE A CE1 1 
ATOM   3430  C  CE2 . PHE A  1 432 ? 46.468  -30.448 49.624  1.00 36.47 ? 449  PHE A CE2 1 
ATOM   3431  C  CZ  . PHE A  1 432 ? 45.965  -29.792 50.727  1.00 37.96 ? 449  PHE A CZ  1 
ATOM   3432  N  N   . GLY A  1 433 ? 50.518  -25.190 47.348  1.00 41.62 ? 450  GLY A N   1 
ATOM   3433  C  CA  . GLY A  1 433 ? 51.677  -24.597 46.702  1.00 41.23 ? 450  GLY A CA  1 
ATOM   3434  C  C   . GLY A  1 433 ? 52.937  -25.424 46.940  1.00 40.71 ? 450  GLY A C   1 
ATOM   3435  O  O   . GLY A  1 433 ? 52.899  -26.428 47.649  1.00 41.32 ? 450  GLY A O   1 
ATOM   3436  N  N   . PRO A  1 434 ? 54.091  -25.019 46.359  1.00 40.78 ? 451  PRO A N   1 
ATOM   3437  C  CA  . PRO A  1 434 ? 55.348  -25.750 46.532  1.00 40.95 ? 451  PRO A CA  1 
ATOM   3438  C  C   . PRO A  1 434 ? 55.729  -25.926 48.001  1.00 39.06 ? 451  PRO A C   1 
ATOM   3439  O  O   . PRO A  1 434 ? 55.403  -25.090 48.838  1.00 37.94 ? 451  PRO A O   1 
ATOM   3440  C  CB  . PRO A  1 434 ? 56.385  -24.895 45.770  1.00 41.89 ? 451  PRO A CB  1 
ATOM   3441  C  CG  . PRO A  1 434 ? 55.566  -24.070 44.803  1.00 40.88 ? 451  PRO A CG  1 
ATOM   3442  C  CD  . PRO A  1 434 ? 54.242  -23.829 45.505  1.00 41.35 ? 451  PRO A CD  1 
ATOM   3443  N  N   . VAL A  1 435 ? 56.427  -27.027 48.294  1.00 39.28 ? 452  VAL A N   1 
ATOM   3444  C  CA  . VAL A  1 435 ? 56.872  -27.336 49.642  1.00 39.99 ? 452  VAL A CA  1 
ATOM   3445  C  C   . VAL A  1 435 ? 58.398  -27.386 49.643  1.00 41.20 ? 452  VAL A C   1 
ATOM   3446  O  O   . VAL A  1 435 ? 58.991  -28.203 48.940  1.00 40.27 ? 452  VAL A O   1 
ATOM   3447  C  CB  . VAL A  1 435 ? 56.258  -28.664 50.133  1.00 38.56 ? 452  VAL A CB  1 
ATOM   3448  C  CG1 . VAL A  1 435 ? 56.883  -29.150 51.438  1.00 37.76 ? 452  VAL A CG1 1 
ATOM   3449  C  CG2 . VAL A  1 435 ? 54.743  -28.565 50.270  1.00 37.87 ? 452  VAL A CG2 1 
ATOM   3450  N  N   . LYS A  1 436 ? 59.017  -26.509 50.444  1.00 44.95 ? 453  LYS A N   1 
ATOM   3451  C  CA  . LYS A  1 436 ? 60.463  -26.485 50.608  1.00 47.66 ? 453  LYS A CA  1 
ATOM   3452  C  C   . LYS A  1 436 ? 60.841  -27.218 51.895  1.00 44.85 ? 453  LYS A C   1 
ATOM   3453  O  O   . LYS A  1 436 ? 60.270  -26.946 52.946  1.00 45.24 ? 453  LYS A O   1 
ATOM   3454  C  CB  . LYS A  1 436 ? 60.925  -25.023 50.636  1.00 51.68 ? 453  LYS A CB  1 
ATOM   3455  C  CG  . LYS A  1 436 ? 62.430  -24.797 50.607  1.00 55.10 ? 453  LYS A CG  1 
ATOM   3456  C  CD  . LYS A  1 436 ? 62.808  -23.324 50.490  1.00 58.41 ? 453  LYS A CD  1 
ATOM   3457  C  CE  . LYS A  1 436 ? 64.253  -23.108 50.165  1.00 61.57 ? 453  LYS A CE  1 
ATOM   3458  N  NZ  . LYS A  1 436 ? 65.143  -23.567 51.235  1.00 64.24 ? 453  LYS A NZ  1 
ATOM   3459  N  N   . LEU A  1 437 ? 61.804  -28.145 51.804  1.00 44.45 ? 454  LEU A N   1 
ATOM   3460  C  CA  . LEU A  1 437 ? 62.310  -28.854 52.971  1.00 46.87 ? 454  LEU A CA  1 
ATOM   3461  C  C   . LEU A  1 437 ? 63.575  -28.159 53.474  1.00 50.82 ? 454  LEU A C   1 
ATOM   3462  O  O   . LEU A  1 437 ? 64.136  -27.307 52.786  1.00 50.20 ? 454  LEU A O   1 
ATOM   3463  C  CB  . LEU A  1 437 ? 62.565  -30.323 52.636  1.00 45.02 ? 454  LEU A CB  1 
ATOM   3464  C  CG  . LEU A  1 437 ? 61.349  -31.137 52.177  1.00 44.54 ? 454  LEU A CG  1 
ATOM   3465  C  CD1 . LEU A  1 437 ? 61.739  -32.586 51.956  1.00 44.03 ? 454  LEU A CD1 1 
ATOM   3466  C  CD2 . LEU A  1 437 ? 60.190  -31.058 53.155  1.00 44.64 ? 454  LEU A CD2 1 
ATOM   3467  N  N   . THR A  1 438 ? 64.018  -28.540 54.681  1.00 54.00 ? 455  THR A N   1 
ATOM   3468  C  CA  . THR A  1 438 ? 65.094  -27.845 55.375  1.00 56.08 ? 455  THR A CA  1 
ATOM   3469  C  C   . THR A  1 438 ? 66.409  -28.001 54.609  1.00 54.75 ? 455  THR A C   1 
ATOM   3470  O  O   . THR A  1 438 ? 67.252  -27.110 54.654  1.00 55.18 ? 455  THR A O   1 
ATOM   3471  C  CB  . THR A  1 438 ? 65.205  -28.364 56.811  1.00 60.72 ? 455  THR A CB  1 
ATOM   3472  O  OG1 . THR A  1 438 ? 63.934  -28.172 57.427  1.00 63.96 ? 455  THR A OG1 1 
ATOM   3473  C  CG2 . THR A  1 438 ? 66.237  -27.613 57.634  1.00 62.74 ? 455  THR A CG2 1 
ATOM   3474  N  N   . ASP A  1 439 ? 66.573  -29.125 53.900  1.00 52.59 ? 456  ASP A N   1 
ATOM   3475  C  CA  . ASP A  1 439 ? 67.774  -29.385 53.117  1.00 53.48 ? 456  ASP A CA  1 
ATOM   3476  C  C   . ASP A  1 439 ? 67.761  -28.621 51.788  1.00 52.48 ? 456  ASP A C   1 
ATOM   3477  O  O   . ASP A  1 439 ? 68.701  -28.739 51.004  1.00 49.77 ? 456  ASP A O   1 
ATOM   3478  C  CB  . ASP A  1 439 ? 67.965  -30.875 52.877  1.00 55.33 ? 456  ASP A CB  1 
ATOM   3479  C  CG  . ASP A  1 439 ? 66.917  -31.544 51.995  1.00 56.27 ? 456  ASP A CG  1 
ATOM   3480  O  OD1 . ASP A  1 439 ? 65.975  -30.844 51.558  1.00 53.86 ? 456  ASP A OD1 1 
ATOM   3481  O  OD2 . ASP A  1 439 ? 67.055  -32.760 51.748  1.00 57.57 ? 456  ASP A OD2 1 
ATOM   3482  N  N   . GLY A  1 440 ? 66.681  -27.877 51.512  1.00 52.79 ? 457  GLY A N   1 
ATOM   3483  C  CA  . GLY A  1 440 ? 66.645  -26.968 50.378  1.00 53.96 ? 457  GLY A CA  1 
ATOM   3484  C  C   . GLY A  1 440 ? 65.754  -27.468 49.241  1.00 52.72 ? 457  GLY A C   1 
ATOM   3485  O  O   . GLY A  1 440 ? 65.291  -26.662 48.437  1.00 54.11 ? 457  GLY A O   1 
ATOM   3486  N  N   . ARG A  1 441 ? 65.529  -28.789 49.177  1.00 51.24 ? 458  ARG A N   1 
ATOM   3487  C  CA  . ARG A  1 441 ? 64.766  -29.402 48.098  1.00 49.38 ? 458  ARG A CA  1 
ATOM   3488  C  C   . ARG A  1 441 ? 63.336  -28.864 48.094  1.00 47.49 ? 458  ARG A C   1 
ATOM   3489  O  O   . ARG A  1 441 ? 62.674  -28.851 49.129  1.00 47.22 ? 458  ARG A O   1 
ATOM   3490  C  CB  . ARG A  1 441 ? 64.724  -30.929 48.242  1.00 48.80 ? 458  ARG A CB  1 
ATOM   3491  C  CG  . ARG A  1 441 ? 66.045  -31.659 48.043  1.00 48.71 ? 458  ARG A CG  1 
ATOM   3492  C  CD  . ARG A  1 441 ? 65.886  -33.162 48.239  1.00 48.53 ? 458  ARG A CD  1 
ATOM   3493  N  NE  . ARG A  1 441 ? 65.481  -33.473 49.615  1.00 50.11 ? 458  ARG A NE  1 
ATOM   3494  C  CZ  . ARG A  1 441 ? 65.020  -34.637 50.071  1.00 49.32 ? 458  ARG A CZ  1 
ATOM   3495  N  NH1 . ARG A  1 441 ? 64.825  -35.658 49.255  1.00 48.81 ? 458  ARG A NH1 1 
ATOM   3496  N  NH2 . ARG A  1 441 ? 64.735  -34.766 51.355  1.00 50.40 ? 458  ARG A NH2 1 
ATOM   3497  N  N   . VAL A  1 442 ? 62.878  -28.421 46.915  1.00 46.27 ? 459  VAL A N   1 
ATOM   3498  C  CA  . VAL A  1 442 ? 61.522  -27.927 46.727  1.00 46.03 ? 459  VAL A CA  1 
ATOM   3499  C  C   . VAL A  1 442 ? 60.726  -28.980 45.955  1.00 44.83 ? 459  VAL A C   1 
ATOM   3500  O  O   . VAL A  1 442 ? 61.229  -29.548 44.988  1.00 45.71 ? 459  VAL A O   1 
ATOM   3501  C  CB  . VAL A  1 442 ? 61.519  -26.568 45.996  1.00 44.72 ? 459  VAL A CB  1 
ATOM   3502  C  CG1 . VAL A  1 442 ? 60.115  -26.127 45.595  1.00 44.00 ? 459  VAL A CG1 1 
ATOM   3503  C  CG2 . VAL A  1 442 ? 62.201  -25.482 46.821  1.00 45.94 ? 459  VAL A CG2 1 
ATOM   3504  N  N   . PHE A  1 443 ? 59.482  -29.221 46.392  1.00 42.96 ? 460  PHE A N   1 
ATOM   3505  C  CA  . PHE A  1 443 ? 58.608  -30.212 45.780  1.00 40.39 ? 460  PHE A CA  1 
ATOM   3506  C  C   . PHE A  1 443 ? 57.324  -29.533 45.314  1.00 38.69 ? 460  PHE A C   1 
ATOM   3507  O  O   . PHE A  1 443 ? 56.667  -28.847 46.094  1.00 39.29 ? 460  PHE A O   1 
ATOM   3508  C  CB  . PHE A  1 443 ? 58.271  -31.341 46.759  1.00 39.37 ? 460  PHE A CB  1 
ATOM   3509  C  CG  . PHE A  1 443 ? 59.419  -32.295 47.053  1.00 38.36 ? 460  PHE A CG  1 
ATOM   3510  C  CD1 . PHE A  1 443 ? 59.658  -33.392 46.233  1.00 38.77 ? 460  PHE A CD1 1 
ATOM   3511  C  CD2 . PHE A  1 443 ? 60.254  -32.094 48.147  1.00 38.04 ? 460  PHE A CD2 1 
ATOM   3512  C  CE1 . PHE A  1 443 ? 60.703  -34.261 46.498  1.00 39.00 ? 460  PHE A CE1 1 
ATOM   3513  C  CE2 . PHE A  1 443 ? 61.298  -32.964 48.405  1.00 36.98 ? 460  PHE A CE2 1 
ATOM   3514  C  CZ  . PHE A  1 443 ? 61.520  -34.046 47.584  1.00 39.05 ? 460  PHE A CZ  1 
ATOM   3515  N  N   . THR A  1 444 ? 56.968  -29.748 44.042  1.00 36.83 ? 461  THR A N   1 
ATOM   3516  C  CA  . THR A  1 444 ? 55.739  -29.207 43.484  1.00 37.17 ? 461  THR A CA  1 
ATOM   3517  C  C   . THR A  1 444 ? 54.692  -30.319 43.441  1.00 33.74 ? 461  THR A C   1 
ATOM   3518  O  O   . THR A  1 444 ? 54.814  -31.251 42.652  1.00 32.50 ? 461  THR A O   1 
ATOM   3519  C  CB  . THR A  1 444 ? 56.024  -28.632 42.098  1.00 38.39 ? 461  THR A CB  1 
ATOM   3520  O  OG1 . THR A  1 444 ? 57.189  -27.825 42.245  1.00 40.37 ? 461  THR A OG1 1 
ATOM   3521  C  CG2 . THR A  1 444 ? 54.874  -27.794 41.574  1.00 39.38 ? 461  THR A CG2 1 
ATOM   3522  N  N   . PRO A  1 445 ? 53.638  -30.270 44.286  1.00 33.18 ? 462  PRO A N   1 
ATOM   3523  C  CA  . PRO A  1 445 ? 52.651  -31.352 44.346  1.00 32.58 ? 462  PRO A CA  1 
ATOM   3524  C  C   . PRO A  1 445 ? 51.726  -31.350 43.133  1.00 32.26 ? 462  PRO A C   1 
ATOM   3525  O  O   . PRO A  1 445 ? 51.338  -30.289 42.654  1.00 31.95 ? 462  PRO A O   1 
ATOM   3526  C  CB  . PRO A  1 445 ? 51.897  -31.046 45.644  1.00 32.87 ? 462  PRO A CB  1 
ATOM   3527  C  CG  . PRO A  1 445 ? 51.950  -29.538 45.741  1.00 33.27 ? 462  PRO A CG  1 
ATOM   3528  C  CD  . PRO A  1 445 ? 53.325  -29.169 45.210  1.00 33.17 ? 462  PRO A CD  1 
ATOM   3529  N  N   . GLY A  1 446 ? 51.379  -32.547 42.649  1.00 31.37 ? 463  GLY A N   1 
ATOM   3530  C  CA  . GLY A  1 446 ? 50.451  -32.683 41.542  1.00 30.74 ? 463  GLY A CA  1 
ATOM   3531  C  C   . GLY A  1 446 ? 49.029  -32.348 41.982  1.00 28.00 ? 463  GLY A C   1 
ATOM   3532  O  O   . GLY A  1 446 ? 48.640  -32.642 43.107  1.00 27.23 ? 463  GLY A O   1 
ATOM   3533  N  N   . GLN A  1 447 ? 48.270  -31.707 41.090  1.00 28.36 ? 464  GLN A N   1 
ATOM   3534  C  CA  . GLN A  1 447 ? 46.844  -31.531 41.301  1.00 29.15 ? 464  GLN A CA  1 
ATOM   3535  C  C   . GLN A  1 447 ? 46.094  -32.379 40.279  1.00 27.52 ? 464  GLN A C   1 
ATOM   3536  O  O   . GLN A  1 447 ? 46.236  -32.169 39.077  1.00 26.19 ? 464  GLN A O   1 
ATOM   3537  C  CB  . GLN A  1 447 ? 46.434  -30.063 41.209  1.00 32.07 ? 464  GLN A CB  1 
ATOM   3538  C  CG  . GLN A  1 447 ? 45.022  -29.802 41.723  1.00 35.07 ? 464  GLN A CG  1 
ATOM   3539  C  CD  . GLN A  1 447 ? 44.489  -28.431 41.369  1.00 37.81 ? 464  GLN A CD  1 
ATOM   3540  O  OE1 . GLN A  1 447 ? 45.190  -27.581 40.810  1.00 39.01 ? 464  GLN A OE1 1 
ATOM   3541  N  NE2 . GLN A  1 447 ? 43.226  -28.207 41.699  1.00 39.92 ? 464  GLN A NE2 1 
ATOM   3542  N  N   . GLY A  1 448 ? 45.313  -33.352 40.766  1.00 25.64 ? 465  GLY A N   1 
ATOM   3543  C  CA  . GLY A  1 448 ? 44.462  -34.156 39.904  1.00 25.16 ? 465  GLY A CA  1 
ATOM   3544  C  C   . GLY A  1 448 ? 43.209  -33.380 39.506  1.00 25.20 ? 465  GLY A C   1 
ATOM   3545  O  O   . GLY A  1 448 ? 42.120  -33.670 39.991  1.00 27.26 ? 465  GLY A O   1 
ATOM   3546  N  N   . ASN A  1 449 ? 43.381  -32.396 38.617  1.00 23.57 ? 466  ASN A N   1 
ATOM   3547  C  CA  . ASN A  1 449 ? 42.311  -31.509 38.191  1.00 23.66 ? 466  ASN A CA  1 
ATOM   3548  C  C   . ASN A  1 449 ? 41.671  -32.078 36.923  1.00 23.25 ? 466  ASN A C   1 
ATOM   3549  O  O   . ASN A  1 449 ? 42.369  -32.384 35.959  1.00 21.50 ? 466  ASN A O   1 
ATOM   3550  C  CB  . ASN A  1 449 ? 42.865  -30.105 37.977  1.00 25.55 ? 466  ASN A CB  1 
ATOM   3551  C  CG  . ASN A  1 449 ? 41.785  -29.066 37.793  1.00 27.59 ? 466  ASN A CG  1 
ATOM   3552  O  OD1 . ASN A  1 449 ? 40.824  -29.286 37.049  1.00 26.17 ? 466  ASN A OD1 1 
ATOM   3553  N  ND2 . ASN A  1 449 ? 41.918  -27.933 38.466  1.00 30.63 ? 466  ASN A ND2 1 
ATOM   3554  N  N   . ASN A  1 450 ? 40.336  -32.192 36.911  1.00 22.88 ? 467  ASN A N   1 
ATOM   3555  C  CA  . ASN A  1 450 ? 39.628  -32.800 35.793  1.00 23.45 ? 467  ASN A CA  1 
ATOM   3556  C  C   . ASN A  1 450 ? 39.838  -32.018 34.494  1.00 21.64 ? 467  ASN A C   1 
ATOM   3557  O  O   . ASN A  1 450 ? 39.631  -32.570 33.420  1.00 20.75 ? 467  ASN A O   1 
ATOM   3558  C  CB  . ASN A  1 450 ? 38.140  -32.972 36.082  1.00 24.96 ? 467  ASN A CB  1 
ATOM   3559  C  CG  . ASN A  1 450 ? 37.870  -34.145 36.994  1.00 26.90 ? 467  ASN A CG  1 
ATOM   3560  O  OD1 . ASN A  1 450 ? 38.803  -34.749 37.539  1.00 29.44 ? 467  ASN A OD1 1 
ATOM   3561  N  ND2 . ASN A  1 450 ? 36.604  -34.484 37.176  1.00 26.89 ? 467  ASN A ND2 1 
ATOM   3562  N  N   . VAL A  1 451 ? 40.270  -30.753 34.580  1.00 22.07 ? 468  VAL A N   1 
ATOM   3563  C  CA  . VAL A  1 451 ? 40.483  -29.935 33.392  1.00 23.19 ? 468  VAL A CA  1 
ATOM   3564  C  C   . VAL A  1 451 ? 41.591  -30.524 32.511  1.00 22.59 ? 468  VAL A C   1 
ATOM   3565  O  O   . VAL A  1 451 ? 41.692  -30.174 31.338  1.00 22.65 ? 468  VAL A O   1 
ATOM   3566  C  CB  . VAL A  1 451 ? 40.784  -28.463 33.748  1.00 23.44 ? 468  VAL A CB  1 
ATOM   3567  C  CG1 . VAL A  1 451 ? 42.199  -28.272 34.284  1.00 23.06 ? 468  VAL A CG1 1 
ATOM   3568  C  CG2 . VAL A  1 451 ? 40.543  -27.541 32.556  1.00 23.56 ? 468  VAL A CG2 1 
ATOM   3569  N  N   . TYR A  1 452 ? 42.422  -31.422 33.059  1.00 21.98 ? 469  TYR A N   1 
ATOM   3570  C  CA  . TYR A  1 452 ? 43.441  -32.098 32.266  1.00 22.08 ? 469  TYR A CA  1 
ATOM   3571  C  C   . TYR A  1 452 ? 42.809  -33.002 31.205  1.00 20.87 ? 469  TYR A C   1 
ATOM   3572  O  O   . TYR A  1 452 ? 43.434  -33.257 30.186  1.00 22.75 ? 469  TYR A O   1 
ATOM   3573  C  CB  . TYR A  1 452 ? 44.375  -32.946 33.137  1.00 22.90 ? 469  TYR A CB  1 
ATOM   3574  C  CG  . TYR A  1 452 ? 45.479  -32.190 33.868  1.00 23.62 ? 469  TYR A CG  1 
ATOM   3575  C  CD1 . TYR A  1 452 ? 46.419  -31.425 33.179  1.00 23.81 ? 469  TYR A CD1 1 
ATOM   3576  C  CD2 . TYR A  1 452 ? 45.586  -32.251 35.253  1.00 23.26 ? 469  TYR A CD2 1 
ATOM   3577  C  CE1 . TYR A  1 452 ? 47.428  -30.747 33.848  1.00 23.57 ? 469  TYR A CE1 1 
ATOM   3578  C  CE2 . TYR A  1 452 ? 46.579  -31.564 35.933  1.00 23.77 ? 469  TYR A CE2 1 
ATOM   3579  C  CZ  . TYR A  1 452 ? 47.508  -30.818 35.229  1.00 23.95 ? 469  TYR A CZ  1 
ATOM   3580  O  OH  . TYR A  1 452 ? 48.480  -30.155 35.920  1.00 24.16 ? 469  TYR A OH  1 
ATOM   3581  N  N   . ILE A  1 453 ? 41.581  -33.488 31.439  1.00 20.21 ? 470  ILE A N   1 
ATOM   3582  C  CA  . ILE A  1 453 ? 40.999  -34.548 30.630  1.00 20.14 ? 470  ILE A CA  1 
ATOM   3583  C  C   . ILE A  1 453 ? 39.838  -34.034 29.772  1.00 20.82 ? 470  ILE A C   1 
ATOM   3584  O  O   . ILE A  1 453 ? 39.820  -34.299 28.573  1.00 21.60 ? 470  ILE A O   1 
ATOM   3585  C  CB  . ILE A  1 453 ? 40.574  -35.727 31.523  1.00 20.11 ? 470  ILE A CB  1 
ATOM   3586  C  CG1 . ILE A  1 453 ? 41.795  -36.406 32.176  1.00 21.08 ? 470  ILE A CG1 1 
ATOM   3587  C  CG2 . ILE A  1 453 ? 39.708  -36.732 30.761  1.00 20.29 ? 470  ILE A CG2 1 
ATOM   3588  C  CD1 . ILE A  1 453 ? 42.809  -36.975 31.197  1.00 20.77 ? 470  ILE A CD1 1 
ATOM   3589  N  N   . PHE A  1 454 ? 38.847  -33.357 30.371  1.00 20.29 ? 471  PHE A N   1 
ATOM   3590  C  CA  . PHE A  1 454 ? 37.566  -33.170 29.698  1.00 20.15 ? 471  PHE A CA  1 
ATOM   3591  C  C   . PHE A  1 454 ? 37.707  -32.319 28.430  1.00 19.87 ? 471  PHE A C   1 
ATOM   3592  O  O   . PHE A  1 454 ? 37.095  -32.657 27.422  1.00 19.57 ? 471  PHE A O   1 
ATOM   3593  C  CB  . PHE A  1 454 ? 36.431  -32.656 30.596  1.00 20.17 ? 471  PHE A CB  1 
ATOM   3594  C  CG  . PHE A  1 454 ? 36.561  -31.283 31.244  1.00 20.89 ? 471  PHE A CG  1 
ATOM   3595  C  CD1 . PHE A  1 454 ? 36.286  -30.118 30.528  1.00 21.35 ? 471  PHE A CD1 1 
ATOM   3596  C  CD2 . PHE A  1 454 ? 36.886  -31.164 32.591  1.00 20.78 ? 471  PHE A CD2 1 
ATOM   3597  C  CE1 . PHE A  1 454 ? 36.391  -28.874 31.134  1.00 21.41 ? 471  PHE A CE1 1 
ATOM   3598  C  CE2 . PHE A  1 454 ? 36.978  -29.915 33.195  1.00 21.47 ? 471  PHE A CE2 1 
ATOM   3599  C  CZ  . PHE A  1 454 ? 36.731  -28.775 32.466  1.00 21.72 ? 471  PHE A CZ  1 
ATOM   3600  N  N   . PRO A  1 455 ? 38.485  -31.210 28.387  1.00 19.93 ? 472  PRO A N   1 
ATOM   3601  C  CA  . PRO A  1 455 ? 38.570  -30.399 27.167  1.00 20.31 ? 472  PRO A CA  1 
ATOM   3602  C  C   . PRO A  1 455 ? 39.052  -31.181 25.943  1.00 20.53 ? 472  PRO A C   1 
ATOM   3603  O  O   . PRO A  1 455 ? 38.434  -31.132 24.878  1.00 20.36 ? 472  PRO A O   1 
ATOM   3604  C  CB  . PRO A  1 455 ? 39.540  -29.266 27.562  1.00 20.30 ? 472  PRO A CB  1 
ATOM   3605  C  CG  . PRO A  1 455 ? 39.445  -29.206 29.070  1.00 20.34 ? 472  PRO A CG  1 
ATOM   3606  C  CD  . PRO A  1 455 ? 39.313  -30.665 29.476  1.00 20.35 ? 472  PRO A CD  1 
ATOM   3607  N  N   . GLY A  1 456 ? 40.147  -31.928 26.118  1.00 20.45 ? 473  GLY A N   1 
ATOM   3608  C  CA  . GLY A  1 456 ? 40.754  -32.683 25.034  1.00 20.06 ? 473  GLY A CA  1 
ATOM   3609  C  C   . GLY A  1 456 ? 39.873  -33.837 24.568  1.00 19.60 ? 473  GLY A C   1 
ATOM   3610  O  O   . GLY A  1 456 ? 39.809  -34.109 23.372  1.00 20.81 ? 473  GLY A O   1 
ATOM   3611  N  N   . VAL A  1 457 ? 39.212  -34.528 25.506  1.00 18.49 ? 474  VAL A N   1 
ATOM   3612  C  CA  . VAL A  1 457 ? 38.298  -35.600 25.140  1.00 18.58 ? 474  VAL A CA  1 
ATOM   3613  C  C   . VAL A  1 457 ? 37.116  -35.010 24.370  1.00 18.00 ? 474  VAL A C   1 
ATOM   3614  O  O   . VAL A  1 457 ? 36.734  -35.537 23.331  1.00 17.90 ? 474  VAL A O   1 
ATOM   3615  C  CB  . VAL A  1 457 ? 37.842  -36.436 26.350  1.00 18.85 ? 474  VAL A CB  1 
ATOM   3616  C  CG1 . VAL A  1 457 ? 36.696  -37.385 26.011  1.00 19.28 ? 474  VAL A CG1 1 
ATOM   3617  C  CG2 . VAL A  1 457 ? 39.006  -37.227 26.927  1.00 19.42 ? 474  VAL A CG2 1 
ATOM   3618  N  N   . ALA A  1 458 ? 36.555  -33.905 24.869  1.00 18.00 ? 475  ALA A N   1 
ATOM   3619  C  CA  . ALA A  1 458 ? 35.421  -33.269 24.218  1.00 17.81 ? 475  ALA A CA  1 
ATOM   3620  C  C   . ALA A  1 458 ? 35.758  -32.887 22.775  1.00 18.53 ? 475  ALA A C   1 
ATOM   3621  O  O   . ALA A  1 458 ? 34.967  -33.153 21.866  1.00 19.38 ? 475  ALA A O   1 
ATOM   3622  C  CB  . ALA A  1 458 ? 34.978  -32.070 25.016  1.00 17.53 ? 475  ALA A CB  1 
ATOM   3623  N  N   . LEU A  1 459 ? 36.934  -32.280 22.560  1.00 19.34 ? 476  LEU A N   1 
ATOM   3624  C  CA  . LEU A  1 459 ? 37.294  -31.779 21.240  1.00 19.87 ? 476  LEU A CA  1 
ATOM   3625  C  C   . LEU A  1 459 ? 37.381  -32.944 20.256  1.00 19.58 ? 476  LEU A C   1 
ATOM   3626  O  O   . LEU A  1 459 ? 36.832  -32.873 19.161  1.00 20.05 ? 476  LEU A O   1 
ATOM   3627  C  CB  . LEU A  1 459 ? 38.597  -30.975 21.282  1.00 20.25 ? 476  LEU A CB  1 
ATOM   3628  C  CG  . LEU A  1 459 ? 39.105  -30.444 19.937  1.00 20.37 ? 476  LEU A CG  1 
ATOM   3629  C  CD1 . LEU A  1 459 ? 38.164  -29.401 19.354  1.00 20.76 ? 476  LEU A CD1 1 
ATOM   3630  C  CD2 . LEU A  1 459 ? 40.508  -29.878 20.072  1.00 20.77 ? 476  LEU A CD2 1 
ATOM   3631  N  N   . ALA A  1 460 ? 38.075  -34.018 20.652  1.00 19.30 ? 477  ALA A N   1 
ATOM   3632  C  CA  . ALA A  1 460 ? 38.286  -35.164 19.783  1.00 19.37 ? 477  ALA A CA  1 
ATOM   3633  C  C   . ALA A  1 460 ? 36.951  -35.789 19.379  1.00 19.28 ? 477  ALA A C   1 
ATOM   3634  O  O   . ALA A  1 460 ? 36.733  -36.113 18.213  1.00 19.38 ? 477  ALA A O   1 
ATOM   3635  C  CB  . ALA A  1 460 ? 39.178  -36.172 20.476  1.00 19.99 ? 477  ALA A CB  1 
ATOM   3636  N  N   . VAL A  1 461 ? 36.065  -35.976 20.359  1.00 19.01 ? 478  VAL A N   1 
ATOM   3637  C  CA  . VAL A  1 461 ? 34.763  -36.571 20.113  1.00 19.23 ? 478  VAL A CA  1 
ATOM   3638  C  C   . VAL A  1 461 ? 33.991  -35.743 19.080  1.00 19.18 ? 478  VAL A C   1 
ATOM   3639  O  O   . VAL A  1 461 ? 33.447  -36.302 18.125  1.00 17.97 ? 478  VAL A O   1 
ATOM   3640  C  CB  . VAL A  1 461 ? 33.995  -36.728 21.439  1.00 19.41 ? 478  VAL A CB  1 
ATOM   3641  C  CG1 . VAL A  1 461 ? 32.505  -36.984 21.241  1.00 19.91 ? 478  VAL A CG1 1 
ATOM   3642  C  CG2 . VAL A  1 461 ? 34.614  -37.825 22.290  1.00 19.38 ? 478  VAL A CG2 1 
ATOM   3643  N  N   . ILE A  1 462 ? 33.964  -34.420 19.271  1.00 18.63 ? 479  ILE A N   1 
ATOM   3644  C  CA  . ILE A  1 462 ? 33.241  -33.514 18.389  1.00 19.54 ? 479  ILE A CA  1 
ATOM   3645  C  C   . ILE A  1 462 ? 33.837  -33.548 16.980  1.00 19.58 ? 479  ILE A C   1 
ATOM   3646  O  O   . ILE A  1 462 ? 33.100  -33.714 16.008  1.00 19.77 ? 479  ILE A O   1 
ATOM   3647  C  CB  . ILE A  1 462 ? 33.216  -32.088 18.976  1.00 20.32 ? 479  ILE A CB  1 
ATOM   3648  C  CG1 . ILE A  1 462 ? 32.320  -32.002 20.224  1.00 20.58 ? 479  ILE A CG1 1 
ATOM   3649  C  CG2 . ILE A  1 462 ? 32.786  -31.059 17.926  1.00 20.46 ? 479  ILE A CG2 1 
ATOM   3650  C  CD1 . ILE A  1 462 ? 32.591  -30.779 21.088  1.00 21.16 ? 479  ILE A CD1 1 
ATOM   3651  N  N   . LEU A  1 463 ? 35.169  -33.409 16.874  1.00 20.84 ? 480  LEU A N   1 
ATOM   3652  C  CA  . LEU A  1 463 ? 35.847  -33.320 15.589  1.00 20.10 ? 480  LEU A CA  1 
ATOM   3653  C  C   . LEU A  1 463 ? 35.716  -34.623 14.802  1.00 20.29 ? 480  LEU A C   1 
ATOM   3654  O  O   . LEU A  1 463 ? 35.760  -34.598 13.573  1.00 21.13 ? 480  LEU A O   1 
ATOM   3655  C  CB  . LEU A  1 463 ? 37.316  -32.934 15.759  1.00 20.26 ? 480  LEU A CB  1 
ATOM   3656  C  CG  . LEU A  1 463 ? 37.604  -31.534 16.312  1.00 20.92 ? 480  LEU A CG  1 
ATOM   3657  C  CD1 . LEU A  1 463 ? 39.097  -31.251 16.225  1.00 21.04 ? 480  LEU A CD1 1 
ATOM   3658  C  CD2 . LEU A  1 463 ? 36.815  -30.433 15.629  1.00 20.99 ? 480  LEU A CD2 1 
ATOM   3659  N  N   . CYS A  1 464 ? 35.560  -35.756 15.500  1.00 19.45 ? 481  CYS A N   1 
ATOM   3660  C  CA  . CYS A  1 464 ? 35.468  -37.059 14.863  1.00 19.71 ? 481  CYS A CA  1 
ATOM   3661  C  C   . CYS A  1 464 ? 34.023  -37.447 14.553  1.00 20.44 ? 481  CYS A C   1 
ATOM   3662  O  O   . CYS A  1 464 ? 33.783  -38.513 13.976  1.00 20.53 ? 481  CYS A O   1 
ATOM   3663  C  CB  . CYS A  1 464 ? 36.106  -38.133 15.737  1.00 19.66 ? 481  CYS A CB  1 
ATOM   3664  S  SG  . CYS A  1 464 ? 37.910  -38.018 15.776  1.00 20.88 ? 481  CYS A SG  1 
ATOM   3665  N  N   . ASN A  1 465 ? 33.067  -36.589 14.927  1.00 20.52 ? 482  ASN A N   1 
ATOM   3666  C  CA  . ASN A  1 465 ? 31.653  -36.921 14.832  1.00 21.46 ? 482  ASN A CA  1 
ATOM   3667  C  C   . ASN A  1 465 ? 31.388  -38.264 15.515  1.00 20.89 ? 482  ASN A C   1 
ATOM   3668  O  O   . ASN A  1 465 ? 30.635  -39.086 14.995  1.00 20.68 ? 482  ASN A O   1 
ATOM   3669  C  CB  . ASN A  1 465 ? 31.141  -36.945 13.392  1.00 23.35 ? 482  ASN A CB  1 
ATOM   3670  C  CG  . ASN A  1 465 ? 31.186  -35.596 12.707  1.00 24.98 ? 482  ASN A CG  1 
ATOM   3671  O  OD1 . ASN A  1 465 ? 30.926  -34.562 13.331  1.00 26.65 ? 482  ASN A OD1 1 
ATOM   3672  N  ND2 . ASN A  1 465 ? 31.505  -35.583 11.422  1.00 26.32 ? 482  ASN A ND2 1 
ATOM   3673  N  N   . THR A  1 466 ? 32.016  -38.473 16.679  1.00 20.93 ? 483  THR A N   1 
ATOM   3674  C  CA  . THR A  1 466 ? 31.822  -39.671 17.483  1.00 20.73 ? 483  THR A CA  1 
ATOM   3675  C  C   . THR A  1 466 ? 30.417  -39.624 18.084  1.00 21.18 ? 483  THR A C   1 
ATOM   3676  O  O   . THR A  1 466 ? 29.899  -38.545 18.376  1.00 21.25 ? 483  THR A O   1 
ATOM   3677  C  CB  . THR A  1 466 ? 32.931  -39.739 18.535  1.00 20.76 ? 483  THR A CB  1 
ATOM   3678  O  OG1 . THR A  1 466 ? 34.107  -40.107 17.820  1.00 20.83 ? 483  THR A OG1 1 
ATOM   3679  C  CG2 . THR A  1 466 ? 32.698  -40.777 19.619  1.00 21.00 ? 483  THR A CG2 1 
ATOM   3680  N  N   . ARG A  1 467 ? 29.813  -40.806 18.251  1.00 21.15 ? 484  ARG A N   1 
ATOM   3681  C  CA  . ARG A  1 467 ? 28.413  -40.931 18.620  1.00 21.41 ? 484  ARG A CA  1 
ATOM   3682  C  C   . ARG A  1 467 ? 28.245  -41.500 20.030  1.00 21.13 ? 484  ARG A C   1 
ATOM   3683  O  O   . ARG A  1 467 ? 27.216  -41.256 20.653  1.00 19.93 ? 484  ARG A O   1 
ATOM   3684  C  CB  . ARG A  1 467 ? 27.699  -41.806 17.586  1.00 23.07 ? 484  ARG A CB  1 
ATOM   3685  C  CG  . ARG A  1 467 ? 27.724  -41.196 16.192  1.00 24.76 ? 484  ARG A CG  1 
ATOM   3686  C  CD  . ARG A  1 467 ? 27.149  -42.133 15.147  1.00 27.16 ? 484  ARG A CD  1 
ATOM   3687  N  NE  . ARG A  1 467 ? 25.685  -42.096 15.123  1.00 28.07 ? 484  ARG A NE  1 
ATOM   3688  C  CZ  . ARG A  1 467 ? 24.931  -41.147 14.575  1.00 30.04 ? 484  ARG A CZ  1 
ATOM   3689  N  NH1 . ARG A  1 467 ? 25.465  -40.099 13.980  1.00 29.48 ? 484  ARG A NH1 1 
ATOM   3690  N  NH2 . ARG A  1 467 ? 23.619  -41.255 14.628  1.00 31.97 ? 484  ARG A NH2 1 
ATOM   3691  N  N   . HIS A  1 468 ? 29.227  -42.280 20.508  1.00 21.09 ? 485  HIS A N   1 
ATOM   3692  C  CA  . HIS A  1 468 ? 29.207  -42.838 21.854  1.00 21.32 ? 485  HIS A CA  1 
ATOM   3693  C  C   . HIS A  1 468 ? 30.633  -42.908 22.396  1.00 20.74 ? 485  HIS A C   1 
ATOM   3694  O  O   . HIS A  1 468 ? 31.578  -43.096 21.633  1.00 20.50 ? 485  HIS A O   1 
ATOM   3695  C  CB  . HIS A  1 468 ? 28.549  -44.226 21.881  1.00 22.67 ? 485  HIS A CB  1 
ATOM   3696  C  CG  . HIS A  1 468 ? 27.243  -44.289 21.167  1.00 23.62 ? 485  HIS A CG  1 
ATOM   3697  N  ND1 . HIS A  1 468 ? 26.090  -43.713 21.661  1.00 23.86 ? 485  HIS A ND1 1 
ATOM   3698  C  CD2 . HIS A  1 468 ? 26.922  -44.814 19.972  1.00 24.75 ? 485  HIS A CD2 1 
ATOM   3699  C  CE1 . HIS A  1 468 ? 25.102  -43.904 20.786  1.00 25.44 ? 485  HIS A CE1 1 
ATOM   3700  N  NE2 . HIS A  1 468 ? 25.585  -44.574 19.755  1.00 24.83 ? 485  HIS A NE2 1 
ATOM   3701  N  N   . ILE A  1 469 ? 30.773  -42.769 23.721  1.00 21.11 ? 486  ILE A N   1 
ATOM   3702  C  CA  . ILE A  1 469 ? 32.077  -42.649 24.360  1.00 20.80 ? 486  ILE A CA  1 
ATOM   3703  C  C   . ILE A  1 469 ? 32.277  -43.825 25.312  1.00 20.88 ? 486  ILE A C   1 
ATOM   3704  O  O   . ILE A  1 469 ? 31.636  -43.902 26.356  1.00 21.59 ? 486  ILE A O   1 
ATOM   3705  C  CB  . ILE A  1 469 ? 32.196  -41.299 25.088  1.00 20.92 ? 486  ILE A CB  1 
ATOM   3706  C  CG1 . ILE A  1 469 ? 31.815  -40.133 24.175  1.00 20.92 ? 486  ILE A CG1 1 
ATOM   3707  C  CG2 . ILE A  1 469 ? 33.592  -41.120 25.685  1.00 21.14 ? 486  ILE A CG2 1 
ATOM   3708  C  CD1 . ILE A  1 469 ? 31.630  -38.817 24.905  1.00 21.41 ? 486  ILE A CD1 1 
ATOM   3709  N  N   . SER A  1 470 ? 33.180  -44.734 24.940  1.00 22.03 ? 487  SER A N   1 
ATOM   3710  C  CA  . SER A  1 470 ? 33.489  -45.899 25.750  1.00 22.26 ? 487  SER A CA  1 
ATOM   3711  C  C   . SER A  1 470 ? 34.413  -45.497 26.898  1.00 22.14 ? 487  SER A C   1 
ATOM   3712  O  O   . SER A  1 470 ? 35.102  -44.479 26.824  1.00 20.95 ? 487  SER A O   1 
ATOM   3713  C  CB  . SER A  1 470 ? 34.115  -46.972 24.902  1.00 23.48 ? 487  SER A CB  1 
ATOM   3714  O  OG  . SER A  1 470 ? 35.356  -46.514 24.382  1.00 24.55 ? 487  SER A OG  1 
ATOM   3715  N  N   . ASP A  1 471 ? 34.463  -46.326 27.945  1.00 22.63 ? 488  ASP A N   1 
ATOM   3716  C  CA  . ASP A  1 471 ? 35.402  -46.097 29.034  1.00 23.18 ? 488  ASP A CA  1 
ATOM   3717  C  C   . ASP A  1 471 ? 36.840  -46.170 28.516  1.00 22.38 ? 488  ASP A C   1 
ATOM   3718  O  O   . ASP A  1 471 ? 37.726  -45.527 29.081  1.00 22.41 ? 488  ASP A O   1 
ATOM   3719  C  CB  . ASP A  1 471 ? 35.135  -47.017 30.215  1.00 25.96 ? 488  ASP A CB  1 
ATOM   3720  C  CG  . ASP A  1 471 ? 34.034  -46.570 31.170  1.00 28.56 ? 488  ASP A CG  1 
ATOM   3721  O  OD1 . ASP A  1 471 ? 33.458  -45.475 30.958  1.00 28.88 ? 488  ASP A OD1 1 
ATOM   3722  O  OD2 . ASP A  1 471 ? 33.772  -47.310 32.142  1.00 31.74 ? 488  ASP A OD2 1 
ATOM   3723  N  N   . SER A  1 472 ? 37.064  -46.924 27.431  1.00 21.55 ? 489  SER A N   1 
ATOM   3724  C  CA  . SER A  1 472 ? 38.387  -47.060 26.835  1.00 22.10 ? 489  SER A CA  1 
ATOM   3725  C  C   . SER A  1 472 ? 38.913  -45.724 26.302  1.00 21.41 ? 489  SER A C   1 
ATOM   3726  O  O   . SER A  1 472 ? 40.126  -45.541 26.184  1.00 20.79 ? 489  SER A O   1 
ATOM   3727  C  CB  . SER A  1 472 ? 38.411  -48.144 25.769  1.00 23.65 ? 489  SER A CB  1 
ATOM   3728  O  OG  . SER A  1 472 ? 37.622  -47.817 24.629  1.00 24.82 ? 489  SER A OG  1 
ATOM   3729  N  N   . VAL A  1 473 ? 38.014  -44.780 25.992  1.00 19.97 ? 490  VAL A N   1 
ATOM   3730  C  CA  . VAL A  1 473 ? 38.425  -43.451 25.570  1.00 19.19 ? 490  VAL A CA  1 
ATOM   3731  C  C   . VAL A  1 473 ? 39.115  -42.739 26.738  1.00 19.46 ? 490  VAL A C   1 
ATOM   3732  O  O   . VAL A  1 473 ? 40.102  -42.039 26.533  1.00 19.60 ? 490  VAL A O   1 
ATOM   3733  C  CB  . VAL A  1 473 ? 37.232  -42.640 25.019  1.00 19.49 ? 490  VAL A CB  1 
ATOM   3734  C  CG1 . VAL A  1 473 ? 37.593  -41.192 24.718  1.00 19.48 ? 490  VAL A CG1 1 
ATOM   3735  C  CG2 . VAL A  1 473 ? 36.640  -43.292 23.777  1.00 19.73 ? 490  VAL A CG2 1 
ATOM   3736  N  N   . PHE A  1 474 ? 38.588  -42.912 27.958  1.00 18.75 ? 491  PHE A N   1 
ATOM   3737  C  CA  . PHE A  1 474 ? 39.152  -42.278 29.142  1.00 19.44 ? 491  PHE A CA  1 
ATOM   3738  C  C   . PHE A  1 474 ? 40.479  -42.939 29.515  1.00 19.34 ? 491  PHE A C   1 
ATOM   3739  O  O   . PHE A  1 474 ? 41.367  -42.276 30.029  1.00 19.31 ? 491  PHE A O   1 
ATOM   3740  C  CB  . PHE A  1 474 ? 38.123  -42.268 30.277  1.00 19.34 ? 491  PHE A CB  1 
ATOM   3741  C  CG  . PHE A  1 474 ? 36.994  -41.290 29.984  1.00 19.22 ? 491  PHE A CG  1 
ATOM   3742  C  CD1 . PHE A  1 474 ? 37.151  -39.934 30.243  1.00 19.71 ? 491  PHE A CD1 1 
ATOM   3743  C  CD2 . PHE A  1 474 ? 35.811  -41.719 29.395  1.00 19.57 ? 491  PHE A CD2 1 
ATOM   3744  C  CE1 . PHE A  1 474 ? 36.145  -39.031 29.930  1.00 20.34 ? 491  PHE A CE1 1 
ATOM   3745  C  CE2 . PHE A  1 474 ? 34.805  -40.814 29.093  1.00 20.18 ? 491  PHE A CE2 1 
ATOM   3746  C  CZ  . PHE A  1 474 ? 34.972  -39.473 29.367  1.00 20.13 ? 491  PHE A CZ  1 
ATOM   3747  N  N   . LEU A  1 475 ? 40.627  -44.235 29.237  1.00 20.87 ? 492  LEU A N   1 
ATOM   3748  C  CA  . LEU A  1 475 ? 41.901  -44.902 29.465  1.00 22.12 ? 492  LEU A CA  1 
ATOM   3749  C  C   . LEU A  1 475 ? 42.959  -44.308 28.533  1.00 21.72 ? 492  LEU A C   1 
ATOM   3750  O  O   . LEU A  1 475 ? 44.063  -43.996 28.969  1.00 22.48 ? 492  LEU A O   1 
ATOM   3751  C  CB  . LEU A  1 475 ? 41.750  -46.410 29.289  1.00 23.33 ? 492  LEU A CB  1 
ATOM   3752  C  CG  . LEU A  1 475 ? 43.043  -47.231 29.346  1.00 24.40 ? 492  LEU A CG  1 
ATOM   3753  C  CD1 . LEU A  1 475 ? 43.789  -47.012 30.642  1.00 25.34 ? 492  LEU A CD1 1 
ATOM   3754  C  CD2 . LEU A  1 475 ? 42.732  -48.706 29.152  1.00 25.38 ? 492  LEU A CD2 1 
ATOM   3755  N  N   . GLU A  1 476 ? 42.611  -44.148 27.252  1.00 22.19 ? 493  GLU A N   1 
ATOM   3756  C  CA  . GLU A  1 476 ? 43.503  -43.548 26.271  1.00 22.86 ? 493  GLU A CA  1 
ATOM   3757  C  C   . GLU A  1 476 ? 43.870  -42.124 26.684  1.00 21.11 ? 493  GLU A C   1 
ATOM   3758  O  O   . GLU A  1 476 ? 45.034  -41.750 26.599  1.00 21.11 ? 493  GLU A O   1 
ATOM   3759  C  CB  . GLU A  1 476 ? 42.892  -43.555 24.868  1.00 25.44 ? 493  GLU A CB  1 
ATOM   3760  C  CG  . GLU A  1 476 ? 43.770  -42.876 23.819  1.00 27.89 ? 493  GLU A CG  1 
ATOM   3761  C  CD  . GLU A  1 476 ? 45.128  -43.521 23.569  1.00 31.26 ? 493  GLU A CD  1 
ATOM   3762  O  OE1 . GLU A  1 476 ? 45.328  -44.710 23.902  1.00 30.81 ? 493  GLU A OE1 1 
ATOM   3763  O  OE2 . GLU A  1 476 ? 46.005  -42.800 23.041  1.00 36.05 ? 493  GLU A OE2 1 
ATOM   3764  N  N   . ALA A  1 477 ? 42.882  -41.333 27.125  1.00 19.61 ? 494  ALA A N   1 
ATOM   3765  C  CA  . ALA A  1 477 ? 43.130  -39.972 27.584  1.00 19.64 ? 494  ALA A CA  1 
ATOM   3766  C  C   . ALA A  1 477 ? 44.142  -39.952 28.734  1.00 19.60 ? 494  ALA A C   1 
ATOM   3767  O  O   . ALA A  1 477 ? 45.030  -39.098 28.768  1.00 19.63 ? 494  ALA A O   1 
ATOM   3768  C  CB  . ALA A  1 477 ? 41.829  -39.310 27.996  1.00 19.27 ? 494  ALA A CB  1 
ATOM   3769  N  N   . ALA A  1 478 ? 43.990  -40.875 29.688  1.00 19.97 ? 495  ALA A N   1 
ATOM   3770  C  CA  . ALA A  1 478 ? 44.884  -40.940 30.836  1.00 20.67 ? 495  ALA A CA  1 
ATOM   3771  C  C   . ALA A  1 478 ? 46.324  -41.205 30.382  1.00 21.06 ? 495  ALA A C   1 
ATOM   3772  O  O   . ALA A  1 478 ? 47.249  -40.541 30.844  1.00 21.38 ? 495  ALA A O   1 
ATOM   3773  C  CB  . ALA A  1 478 ? 44.401  -41.987 31.812  1.00 20.49 ? 495  ALA A CB  1 
ATOM   3774  N  N   . LYS A  1 479 ? 46.507  -42.157 29.462  1.00 22.45 ? 496  LYS A N   1 
ATOM   3775  C  CA  . LYS A  1 479 ? 47.833  -42.482 28.947  1.00 23.85 ? 496  LYS A CA  1 
ATOM   3776  C  C   . LYS A  1 479 ? 48.413  -41.302 28.164  1.00 23.67 ? 496  LYS A C   1 
ATOM   3777  O  O   . LYS A  1 479 ? 49.615  -41.046 28.230  1.00 23.63 ? 496  LYS A O   1 
ATOM   3778  C  CB  . LYS A  1 479 ? 47.798  -43.732 28.062  1.00 25.17 ? 496  LYS A CB  1 
ATOM   3779  C  CG  . LYS A  1 479 ? 47.473  -45.028 28.789  1.00 27.53 ? 496  LYS A CG  1 
ATOM   3780  C  CD  . LYS A  1 479 ? 47.546  -46.273 27.915  1.00 30.15 ? 496  LYS A CD  1 
ATOM   3781  C  CE  . LYS A  1 479 ? 46.549  -46.254 26.807  1.00 32.75 ? 496  LYS A CE  1 
ATOM   3782  N  NZ  . LYS A  1 479 ? 46.433  -47.562 26.155  1.00 35.02 ? 496  LYS A NZ  1 
ATOM   3783  N  N   . ALA A  1 480 ? 47.549  -40.588 27.427  1.00 22.74 ? 497  ALA A N   1 
ATOM   3784  C  CA  . ALA A  1 480 ? 47.972  -39.463 26.602  1.00 22.94 ? 497  ALA A CA  1 
ATOM   3785  C  C   . ALA A  1 480 ? 48.441  -38.306 27.480  1.00 23.02 ? 497  ALA A C   1 
ATOM   3786  O  O   . ALA A  1 480 ? 49.365  -37.588 27.104  1.00 23.04 ? 497  ALA A O   1 
ATOM   3787  C  CB  . ALA A  1 480 ? 46.851  -39.035 25.681  1.00 23.07 ? 497  ALA A CB  1 
ATOM   3788  N  N   . LEU A  1 481 ? 47.800  -38.132 28.645  1.00 21.75 ? 498  LEU A N   1 
ATOM   3789  C  CA  . LEU A  1 481 ? 48.198  -37.104 29.596  1.00 22.44 ? 498  LEU A CA  1 
ATOM   3790  C  C   . LEU A  1 481 ? 49.594  -37.415 30.143  1.00 23.15 ? 498  LEU A C   1 
ATOM   3791  O  O   . LEU A  1 481 ? 50.486  -36.569 30.083  1.00 23.94 ? 498  LEU A O   1 
ATOM   3792  C  CB  . LEU A  1 481 ? 47.160  -36.986 30.715  1.00 21.99 ? 498  LEU A CB  1 
ATOM   3793  C  CG  . LEU A  1 481 ? 47.452  -35.961 31.819  1.00 21.78 ? 498  LEU A CG  1 
ATOM   3794  C  CD1 . LEU A  1 481 ? 47.607  -34.546 31.289  1.00 21.43 ? 498  LEU A CD1 1 
ATOM   3795  C  CD2 . LEU A  1 481 ? 46.373  -35.985 32.883  1.00 22.18 ? 498  LEU A CD2 1 
ATOM   3796  N  N   . THR A  1 482 ? 49.769  -38.633 30.673  1.00 24.18 ? 499  THR A N   1 
ATOM   3797  C  CA  . THR A  1 482 ? 51.010  -39.045 31.311  1.00 24.98 ? 499  THR A CA  1 
ATOM   3798  C  C   . THR A  1 482 ? 52.162  -39.028 30.303  1.00 25.97 ? 499  THR A C   1 
ATOM   3799  O  O   . THR A  1 482 ? 53.297  -38.749 30.685  1.00 24.42 ? 499  THR A O   1 
ATOM   3800  C  CB  . THR A  1 482 ? 50.832  -40.420 31.953  1.00 26.81 ? 499  THR A CB  1 
ATOM   3801  O  OG1 . THR A  1 482 ? 49.914  -40.201 33.022  1.00 30.14 ? 499  THR A OG1 1 
ATOM   3802  C  CG2 . THR A  1 482 ? 52.117  -40.986 32.529  1.00 27.85 ? 499  THR A CG2 1 
ATOM   3803  N  N   . SER A  1 483 ? 51.860  -39.296 29.022  1.00 27.21 ? 500  SER A N   1 
ATOM   3804  C  CA  . SER A  1 483 ? 52.874  -39.363 27.980  1.00 27.89 ? 500  SER A CA  1 
ATOM   3805  C  C   . SER A  1 483 ? 53.528  -38.002 27.742  1.00 28.04 ? 500  SER A C   1 
ATOM   3806  O  O   . SER A  1 483 ? 54.564  -37.934 27.085  1.00 29.15 ? 500  SER A O   1 
ATOM   3807  C  CB  . SER A  1 483 ? 52.304  -39.904 26.690  1.00 28.72 ? 500  SER A CB  1 
ATOM   3808  O  OG  . SER A  1 483 ? 51.566  -38.898 26.007  1.00 30.47 ? 500  SER A OG  1 
ATOM   3809  N  N   . GLN A  1 484 ? 52.930  -36.923 28.256  1.00 27.44 ? 501  GLN A N   1 
ATOM   3810  C  CA  . GLN A  1 484 ? 53.452  -35.584 28.027  1.00 29.42 ? 501  GLN A CA  1 
ATOM   3811  C  C   . GLN A  1 484 ? 54.442  -35.145 29.106  1.00 31.23 ? 501  GLN A C   1 
ATOM   3812  O  O   . GLN A  1 484 ? 55.032  -34.072 28.986  1.00 32.73 ? 501  GLN A O   1 
ATOM   3813  C  CB  . GLN A  1 484 ? 52.284  -34.608 27.929  1.00 30.11 ? 501  GLN A CB  1 
ATOM   3814  C  CG  . GLN A  1 484 ? 51.377  -34.917 26.744  1.00 30.92 ? 501  GLN A CG  1 
ATOM   3815  C  CD  . GLN A  1 484 ? 50.393  -33.811 26.465  1.00 33.03 ? 501  GLN A CD  1 
ATOM   3816  O  OE1 . GLN A  1 484 ? 50.783  -32.684 26.140  1.00 34.74 ? 501  GLN A OE1 1 
ATOM   3817  N  NE2 . GLN A  1 484 ? 49.109  -34.123 26.588  1.00 33.68 ? 501  GLN A NE2 1 
ATOM   3818  N  N   . LEU A  1 485 ? 54.617  -35.958 30.155  1.00 31.82 ? 502  LEU A N   1 
ATOM   3819  C  CA  . LEU A  1 485 ? 55.590  -35.666 31.200  1.00 34.33 ? 502  LEU A CA  1 
ATOM   3820  C  C   . LEU A  1 485 ? 56.992  -35.899 30.648  1.00 36.44 ? 502  LEU A C   1 
ATOM   3821  O  O   . LEU A  1 485 ? 57.276  -36.987 30.153  1.00 36.60 ? 502  LEU A O   1 
ATOM   3822  C  CB  . LEU A  1 485 ? 55.355  -36.550 32.423  1.00 34.89 ? 502  LEU A CB  1 
ATOM   3823  C  CG  . LEU A  1 485 ? 54.284  -36.088 33.411  1.00 35.34 ? 502  LEU A CG  1 
ATOM   3824  C  CD1 . LEU A  1 485 ? 54.058  -37.192 34.428  1.00 36.52 ? 502  LEU A CD1 1 
ATOM   3825  C  CD2 . LEU A  1 485 ? 54.680  -34.798 34.107  1.00 35.50 ? 502  LEU A CD2 1 
ATOM   3826  N  N   . THR A  1 486 ? 57.851  -34.875 30.746  1.00 40.03 ? 503  THR A N   1 
ATOM   3827  C  CA  . THR A  1 486 ? 59.227  -34.964 30.279  1.00 43.76 ? 503  THR A CA  1 
ATOM   3828  C  C   . THR A  1 486 ? 60.066  -35.740 31.294  1.00 46.86 ? 503  THR A C   1 
ATOM   3829  O  O   . THR A  1 486 ? 59.704  -35.830 32.468  1.00 46.16 ? 503  THR A O   1 
ATOM   3830  C  CB  . THR A  1 486 ? 59.788  -33.559 30.054  1.00 43.84 ? 503  THR A CB  1 
ATOM   3831  O  OG1 . THR A  1 486 ? 59.668  -32.890 31.306  1.00 44.21 ? 503  THR A OG1 1 
ATOM   3832  C  CG2 . THR A  1 486 ? 59.035  -32.787 28.984  1.00 43.28 ? 503  THR A CG2 1 
ATOM   3833  N  N   . ASP A  1 487 ? 61.204  -36.276 30.830  1.00 51.99 ? 504  ASP A N   1 
ATOM   3834  C  CA  . ASP A  1 487 ? 62.134  -37.007 31.682  1.00 54.72 ? 504  ASP A CA  1 
ATOM   3835  C  C   . ASP A  1 487 ? 62.558  -36.146 32.872  1.00 54.19 ? 504  ASP A C   1 
ATOM   3836  O  O   . ASP A  1 487 ? 62.673  -36.652 33.984  1.00 55.88 ? 504  ASP A O   1 
ATOM   3837  C  CB  . ASP A  1 487 ? 63.348  -37.493 30.905  1.00 57.49 ? 504  ASP A CB  1 
ATOM   3838  C  CG  . ASP A  1 487 ? 63.066  -38.522 29.818  1.00 60.78 ? 504  ASP A CG  1 
ATOM   3839  O  OD1 . ASP A  1 487 ? 61.889  -38.921 29.676  1.00 63.47 ? 504  ASP A OD1 1 
ATOM   3840  O  OD2 . ASP A  1 487 ? 64.027  -38.917 29.122  1.00 59.85 ? 504  ASP A OD2 1 
ATOM   3841  N  N   A GLU A  1 488 ? 62.775  -34.849 32.620  0.50 55.19 ? 505  GLU A N   1 
ATOM   3842  N  N   B GLU A  1 488 ? 62.801  -34.852 32.617  0.50 55.83 ? 505  GLU A N   1 
ATOM   3843  C  CA  A GLU A  1 488 ? 63.169  -33.907 33.655  0.50 56.27 ? 505  GLU A CA  1 
ATOM   3844  C  CA  B GLU A  1 488 ? 63.164  -33.899 33.656  0.50 57.44 ? 505  GLU A CA  1 
ATOM   3845  C  C   A GLU A  1 488 ? 62.071  -33.799 34.713  0.50 56.12 ? 505  GLU A C   1 
ATOM   3846  C  C   B GLU A  1 488 ? 62.066  -33.837 34.715  0.50 56.77 ? 505  GLU A C   1 
ATOM   3847  O  O   A GLU A  1 488 ? 62.362  -33.821 35.908  0.50 56.74 ? 505  GLU A O   1 
ATOM   3848  O  O   B GLU A  1 488 ? 62.350  -33.925 35.908  0.50 57.43 ? 505  GLU A O   1 
ATOM   3849  C  CB  A GLU A  1 488 ? 63.487  -32.547 33.029  0.50 55.99 ? 505  GLU A CB  1 
ATOM   3850  C  CB  B GLU A  1 488 ? 63.389  -32.505 33.066  0.50 58.10 ? 505  GLU A CB  1 
ATOM   3851  C  CG  A GLU A  1 488 ? 64.364  -32.643 31.783  0.50 55.30 ? 505  GLU A CG  1 
ATOM   3852  C  CG  B GLU A  1 488 ? 63.735  -31.447 34.111  0.50 58.29 ? 505  GLU A CG  1 
ATOM   3853  C  CD  A GLU A  1 488 ? 63.604  -32.930 30.499  0.50 54.74 ? 505  GLU A CD  1 
ATOM   3854  C  CD  B GLU A  1 488 ? 65.165  -31.499 34.619  0.50 58.58 ? 505  GLU A CD  1 
ATOM   3855  O  OE1 A GLU A  1 488 ? 63.672  -34.073 30.000  0.50 53.77 ? 505  GLU A OE1 1 
ATOM   3856  O  OE1 B GLU A  1 488 ? 66.076  -31.164 33.836  0.50 59.83 ? 505  GLU A OE1 1 
ATOM   3857  O  OE2 A GLU A  1 488 ? 62.954  -31.994 29.986  0.50 54.32 ? 505  GLU A OE2 1 
ATOM   3858  O  OE2 B GLU A  1 488 ? 65.372  -31.880 35.790  0.50 57.89 ? 505  GLU A OE2 1 
ATOM   3859  N  N   . GLU A  1 489 ? 60.815  -33.681 34.262  1.00 56.12 ? 506  GLU A N   1 
ATOM   3860  C  CA  . GLU A  1 489 ? 59.663  -33.596 35.152  1.00 54.13 ? 506  GLU A CA  1 
ATOM   3861  C  C   . GLU A  1 489 ? 59.479  -34.901 35.929  1.00 52.40 ? 506  GLU A C   1 
ATOM   3862  O  O   . GLU A  1 489 ? 59.127  -34.873 37.105  1.00 51.82 ? 506  GLU A O   1 
ATOM   3863  C  CB  . GLU A  1 489 ? 58.402  -33.246 34.358  1.00 54.80 ? 506  GLU A CB  1 
ATOM   3864  C  CG  . GLU A  1 489 ? 58.328  -31.780 33.934  1.00 54.57 ? 506  GLU A CG  1 
ATOM   3865  C  CD  . GLU A  1 489 ? 57.247  -31.445 32.915  1.00 53.23 ? 506  GLU A CD  1 
ATOM   3866  O  OE1 . GLU A  1 489 ? 56.687  -32.380 32.308  1.00 50.87 ? 506  GLU A OE1 1 
ATOM   3867  O  OE2 . GLU A  1 489 ? 56.959  -30.242 32.726  1.00 53.76 ? 506  GLU A OE2 1 
ATOM   3868  N  N   . LEU A  1 490 ? 59.718  -36.043 35.269  1.00 55.84 ? 507  LEU A N   1 
ATOM   3869  C  CA  . LEU A  1 490 ? 59.556  -37.352 35.888  1.00 57.17 ? 507  LEU A CA  1 
ATOM   3870  C  C   . LEU A  1 490 ? 60.591  -37.557 36.995  1.00 61.51 ? 507  LEU A C   1 
ATOM   3871  O  O   . LEU A  1 490 ? 60.297  -38.205 37.997  1.00 62.46 ? 507  LEU A O   1 
ATOM   3872  C  CB  . LEU A  1 490 ? 59.663  -38.453 34.833  1.00 58.32 ? 507  LEU A CB  1 
ATOM   3873  C  CG  . LEU A  1 490 ? 58.469  -38.617 33.886  1.00 57.32 ? 507  LEU A CG  1 
ATOM   3874  C  CD1 . LEU A  1 490 ? 58.831  -39.536 32.731  1.00 55.27 ? 507  LEU A CD1 1 
ATOM   3875  C  CD2 . LEU A  1 490 ? 57.241  -39.145 34.615  1.00 57.58 ? 507  LEU A CD2 1 
ATOM   3876  N  N   . ALA A  1 491 ? 61.802  -37.019 36.792  1.00 65.53 ? 508  ALA A N   1 
ATOM   3877  C  CA  . ALA A  1 491 ? 62.876  -37.105 37.772  1.00 68.11 ? 508  ALA A CA  1 
ATOM   3878  C  C   . ALA A  1 491 ? 62.543  -36.276 39.014  1.00 68.06 ? 508  ALA A C   1 
ATOM   3879  O  O   . ALA A  1 491 ? 62.883  -36.675 40.127  1.00 70.94 ? 508  ALA A O   1 
ATOM   3880  C  CB  . ALA A  1 491 ? 64.181  -36.658 37.147  1.00 67.38 ? 508  ALA A CB  1 
ATOM   3881  N  N   . GLN A  1 492 ? 61.867  -35.135 38.811  1.00 66.27 ? 509  GLN A N   1 
ATOM   3882  C  CA  . GLN A  1 492 ? 61.505  -34.224 39.889  1.00 63.94 ? 509  GLN A CA  1 
ATOM   3883  C  C   . GLN A  1 492 ? 60.221  -34.662 40.594  1.00 62.47 ? 509  GLN A C   1 
ATOM   3884  O  O   . GLN A  1 492 ? 59.763  -33.982 41.511  1.00 61.63 ? 509  GLN A O   1 
ATOM   3885  C  CB  . GLN A  1 492 ? 61.303  -32.813 39.336  1.00 64.78 ? 509  GLN A CB  1 
ATOM   3886  C  CG  . GLN A  1 492 ? 62.575  -32.176 38.787  1.00 67.47 ? 509  GLN A CG  1 
ATOM   3887  C  CD  . GLN A  1 492 ? 62.313  -30.955 37.933  1.00 69.42 ? 509  GLN A CD  1 
ATOM   3888  O  OE1 . GLN A  1 492 ? 61.164  -30.568 37.685  1.00 70.42 ? 509  GLN A OE1 1 
ATOM   3889  N  NE2 . GLN A  1 492 ? 63.388  -30.341 37.461  1.00 69.96 ? 509  GLN A NE2 1 
ATOM   3890  N  N   . GLY A  1 493 ? 59.623  -35.775 40.149  1.00 58.11 ? 510  GLY A N   1 
ATOM   3891  C  CA  . GLY A  1 493 ? 58.470  -36.348 40.828  1.00 58.86 ? 510  GLY A CA  1 
ATOM   3892  C  C   . GLY A  1 493 ? 57.190  -35.545 40.592  1.00 54.20 ? 510  GLY A C   1 
ATOM   3893  O  O   . GLY A  1 493 ? 56.288  -35.550 41.430  1.00 54.73 ? 510  GLY A O   1 
ATOM   3894  N  N   . ARG A  1 494 ? 57.129  -34.842 39.456  1.00 48.96 ? 511  ARG A N   1 
ATOM   3895  C  CA  . ARG A  1 494 ? 55.886  -34.280 38.958  1.00 44.23 ? 511  ARG A CA  1 
ATOM   3896  C  C   . ARG A  1 494 ? 55.050  -35.424 38.395  1.00 36.23 ? 511  ARG A C   1 
ATOM   3897  O  O   . ARG A  1 494 ? 55.568  -36.242 37.635  1.00 35.14 ? 511  ARG A O   1 
ATOM   3898  C  CB  . ARG A  1 494 ? 56.169  -33.247 37.862  1.00 47.31 ? 511  ARG A CB  1 
ATOM   3899  C  CG  . ARG A  1 494 ? 56.497  -31.833 38.320  1.00 51.94 ? 511  ARG A CG  1 
ATOM   3900  C  CD  . ARG A  1 494 ? 55.278  -30.909 38.266  1.00 54.98 ? 511  ARG A CD  1 
ATOM   3901  N  NE  . ARG A  1 494 ? 55.638  -29.510 37.997  1.00 56.48 ? 511  ARG A NE  1 
ATOM   3902  C  CZ  . ARG A  1 494 ? 54.786  -28.536 37.680  1.00 57.79 ? 511  ARG A CZ  1 
ATOM   3903  N  NH1 . ARG A  1 494 ? 55.224  -27.297 37.510  1.00 59.18 ? 511  ARG A NH1 1 
ATOM   3904  N  NH2 . ARG A  1 494 ? 53.496  -28.789 37.541  1.00 56.75 ? 511  ARG A NH2 1 
ATOM   3905  N  N   . LEU A  1 495 ? 53.768  -35.489 38.783  1.00 31.96 ? 512  LEU A N   1 
ATOM   3906  C  CA  . LEU A  1 495 ? 52.890  -36.562 38.334  1.00 28.02 ? 512  LEU A CA  1 
ATOM   3907  C  C   . LEU A  1 495 ? 51.920  -36.069 37.261  1.00 25.58 ? 512  LEU A C   1 
ATOM   3908  O  O   . LEU A  1 495 ? 51.203  -36.880 36.679  1.00 23.72 ? 512  LEU A O   1 
ATOM   3909  C  CB  . LEU A  1 495 ? 52.142  -37.163 39.522  1.00 28.06 ? 512  LEU A CB  1 
ATOM   3910  C  CG  . LEU A  1 495 ? 53.007  -37.822 40.601  1.00 27.86 ? 512  LEU A CG  1 
ATOM   3911  C  CD1 . LEU A  1 495 ? 52.143  -38.375 41.724  1.00 28.23 ? 512  LEU A CD1 1 
ATOM   3912  C  CD2 . LEU A  1 495 ? 53.876  -38.914 40.023  1.00 27.34 ? 512  LEU A CD2 1 
ATOM   3913  N  N   . TYR A  1 496 ? 51.897  -34.752 37.023  1.00 23.93 ? 513  TYR A N   1 
ATOM   3914  C  CA  . TYR A  1 496 ? 51.073  -34.157 35.984  1.00 24.72 ? 513  TYR A CA  1 
ATOM   3915  C  C   . TYR A  1 496 ? 51.848  -33.044 35.284  1.00 25.10 ? 513  TYR A C   1 
ATOM   3916  O  O   . TYR A  1 496 ? 52.623  -32.340 35.919  1.00 23.93 ? 513  TYR A O   1 
ATOM   3917  C  CB  . TYR A  1 496 ? 49.793  -33.538 36.549  1.00 22.92 ? 513  TYR A CB  1 
ATOM   3918  C  CG  . TYR A  1 496 ? 48.873  -34.543 37.218  1.00 22.16 ? 513  TYR A CG  1 
ATOM   3919  C  CD1 . TYR A  1 496 ? 48.047  -35.363 36.460  1.00 21.74 ? 513  TYR A CD1 1 
ATOM   3920  C  CD2 . TYR A  1 496 ? 48.836  -34.675 38.600  1.00 21.38 ? 513  TYR A CD2 1 
ATOM   3921  C  CE1 . TYR A  1 496 ? 47.215  -36.291 37.060  1.00 22.09 ? 513  TYR A CE1 1 
ATOM   3922  C  CE2 . TYR A  1 496 ? 48.004  -35.598 39.212  1.00 21.60 ? 513  TYR A CE2 1 
ATOM   3923  C  CZ  . TYR A  1 496 ? 47.186  -36.402 38.438  1.00 20.86 ? 513  TYR A CZ  1 
ATOM   3924  O  OH  . TYR A  1 496 ? 46.358  -37.308 39.034  1.00 20.73 ? 513  TYR A OH  1 
ATOM   3925  N  N   . PRO A  1 497 ? 51.609  -32.802 33.976  1.00 26.50 ? 514  PRO A N   1 
ATOM   3926  C  CA  . PRO A  1 497 ? 52.180  -31.633 33.304  1.00 26.74 ? 514  PRO A CA  1 
ATOM   3927  C  C   . PRO A  1 497 ? 51.717  -30.345 33.983  1.00 28.24 ? 514  PRO A C   1 
ATOM   3928  O  O   . PRO A  1 497 ? 50.683  -30.330 34.650  1.00 29.96 ? 514  PRO A O   1 
ATOM   3929  C  CB  . PRO A  1 497 ? 51.701  -31.723 31.843  1.00 26.38 ? 514  PRO A CB  1 
ATOM   3930  C  CG  . PRO A  1 497 ? 51.114  -33.111 31.697  1.00 26.47 ? 514  PRO A CG  1 
ATOM   3931  C  CD  . PRO A  1 497 ? 50.767  -33.620 33.088  1.00 26.44 ? 514  PRO A CD  1 
ATOM   3932  N  N   . PRO A  1 498 ? 52.469  -29.229 33.856  1.00 28.81 ? 515  PRO A N   1 
ATOM   3933  C  CA  . PRO A  1 498 ? 52.057  -27.952 34.445  1.00 29.51 ? 515  PRO A CA  1 
ATOM   3934  C  C   . PRO A  1 498 ? 50.693  -27.472 33.953  1.00 28.87 ? 515  PRO A C   1 
ATOM   3935  O  O   . PRO A  1 498 ? 50.403  -27.563 32.764  1.00 25.93 ? 515  PRO A O   1 
ATOM   3936  C  CB  . PRO A  1 498 ? 53.183  -26.983 34.027  1.00 30.78 ? 515  PRO A CB  1 
ATOM   3937  C  CG  . PRO A  1 498 ? 54.366  -27.876 33.731  1.00 31.09 ? 515  PRO A CG  1 
ATOM   3938  C  CD  . PRO A  1 498 ? 53.770  -29.153 33.171  1.00 30.81 ? 515  PRO A CD  1 
ATOM   3939  N  N   . LEU A  1 499 ? 49.875  -26.955 34.882  1.00 29.58 ? 516  LEU A N   1 
ATOM   3940  C  CA  . LEU A  1 499 ? 48.561  -26.410 34.563  1.00 29.97 ? 516  LEU A CA  1 
ATOM   3941  C  C   . LEU A  1 499 ? 48.696  -25.195 33.651  1.00 28.71 ? 516  LEU A C   1 
ATOM   3942  O  O   . LEU A  1 499 ? 47.799  -24.916 32.865  1.00 30.06 ? 516  LEU A O   1 
ATOM   3943  C  CB  . LEU A  1 499 ? 47.786  -26.026 35.823  1.00 30.96 ? 516  LEU A CB  1 
ATOM   3944  C  CG  . LEU A  1 499 ? 47.007  -27.137 36.531  1.00 33.91 ? 516  LEU A CG  1 
ATOM   3945  C  CD1 . LEU A  1 499 ? 46.399  -26.560 37.799  1.00 35.18 ? 516  LEU A CD1 1 
ATOM   3946  C  CD2 . LEU A  1 499 ? 45.923  -27.754 35.656  1.00 34.98 ? 516  LEU A CD2 1 
ATOM   3947  N  N   . ALA A  1 500 ? 49.804  -24.456 33.782  1.00 29.24 ? 517  ALA A N   1 
ATOM   3948  C  CA  . ALA A  1 500 ? 50.069  -23.318 32.915  1.00 28.91 ? 517  ALA A CA  1 
ATOM   3949  C  C   . ALA A  1 500 ? 50.043  -23.732 31.442  1.00 28.39 ? 517  ALA A C   1 
ATOM   3950  O  O   . ALA A  1 500 ? 49.756  -22.902 30.587  1.00 29.46 ? 517  ALA A O   1 
ATOM   3951  C  CB  . ALA A  1 500 ? 51.395  -22.687 33.282  1.00 29.63 ? 517  ALA A CB  1 
ATOM   3952  N  N   . ASN A  1 501 ? 50.336  -25.009 31.154  1.00 27.89 ? 518  ASN A N   1 
ATOM   3953  C  CA  . ASN A  1 501 ? 50.445  -25.505 29.791  1.00 28.60 ? 518  ASN A CA  1 
ATOM   3954  C  C   . ASN A  1 501 ? 49.168  -26.216 29.331  1.00 26.50 ? 518  ASN A C   1 
ATOM   3955  O  O   . ASN A  1 501 ? 49.220  -27.022 28.402  1.00 25.79 ? 518  ASN A O   1 
ATOM   3956  C  CB  . ASN A  1 501 ? 51.630  -26.460 29.667  1.00 31.79 ? 518  ASN A CB  1 
ATOM   3957  C  CG  . ASN A  1 501 ? 52.953  -25.801 29.985  1.00 35.77 ? 518  ASN A CG  1 
ATOM   3958  O  OD1 . ASN A  1 501 ? 53.033  -24.572 30.095  1.00 38.73 ? 518  ASN A OD1 1 
ATOM   3959  N  ND2 . ASN A  1 501 ? 54.004  -26.598 30.106  1.00 37.81 ? 518  ASN A ND2 1 
ATOM   3960  N  N   . ILE A  1 502 ? 48.014  -25.884 29.929  1.00 25.77 ? 519  ILE A N   1 
ATOM   3961  C  CA  . ILE A  1 502 ? 46.806  -26.682 29.761  1.00 24.24 ? 519  ILE A CA  1 
ATOM   3962  C  C   . ILE A  1 502 ? 46.323  -26.651 28.307  1.00 23.65 ? 519  ILE A C   1 
ATOM   3963  O  O   . ILE A  1 502 ? 45.754  -27.635 27.837  1.00 22.90 ? 519  ILE A O   1 
ATOM   3964  C  CB  . ILE A  1 502 ? 45.698  -26.268 30.756  1.00 23.82 ? 519  ILE A CB  1 
ATOM   3965  C  CG1 . ILE A  1 502 ? 44.502  -27.223 30.710  1.00 23.16 ? 519  ILE A CG1 1 
ATOM   3966  C  CG2 . ILE A  1 502 ? 45.250  -24.820 30.558  1.00 25.08 ? 519  ILE A CG2 1 
ATOM   3967  C  CD1 . ILE A  1 502 ? 44.842  -28.669 31.013  1.00 23.40 ? 519  ILE A CD1 1 
ATOM   3968  N  N   . GLN A  1 503 ? 46.533  -25.536 27.596  1.00 25.15 ? 520  GLN A N   1 
ATOM   3969  C  CA  . GLN A  1 503 ? 46.110  -25.448 26.207  1.00 26.82 ? 520  GLN A CA  1 
ATOM   3970  C  C   . GLN A  1 503 ? 46.829  -26.507 25.372  1.00 26.58 ? 520  GLN A C   1 
ATOM   3971  O  O   . GLN A  1 503 ? 46.186  -27.304 24.691  1.00 26.18 ? 520  GLN A O   1 
ATOM   3972  C  CB  . GLN A  1 503 ? 46.342  -24.065 25.601  1.00 29.21 ? 520  GLN A CB  1 
ATOM   3973  C  CG  . GLN A  1 503 ? 45.342  -23.009 26.055  1.00 31.87 ? 520  GLN A CG  1 
ATOM   3974  C  CD  . GLN A  1 503 ? 45.387  -21.764 25.195  1.00 34.97 ? 520  GLN A CD  1 
ATOM   3975  O  OE1 . GLN A  1 503 ? 44.990  -21.778 24.024  1.00 41.02 ? 520  GLN A OE1 1 
ATOM   3976  N  NE2 . GLN A  1 503 ? 45.884  -20.675 25.759  1.00 36.83 ? 520  GLN A NE2 1 
ATOM   3977  N  N   . GLU A  1 504 ? 48.167  -26.497 25.425  1.00 26.90 ? 521  GLU A N   1 
ATOM   3978  C  CA  . GLU A  1 504 ? 48.990  -27.431 24.672  1.00 27.80 ? 521  GLU A CA  1 
ATOM   3979  C  C   . GLU A  1 504 ? 48.670  -28.867 25.086  1.00 25.73 ? 521  GLU A C   1 
ATOM   3980  O  O   . GLU A  1 504 ? 48.588  -29.750 24.237  1.00 23.97 ? 521  GLU A O   1 
ATOM   3981  C  CB  . GLU A  1 504 ? 50.466  -27.093 24.897  1.00 31.65 ? 521  GLU A CB  1 
ATOM   3982  C  CG  . GLU A  1 504 ? 51.450  -28.132 24.363  1.00 36.26 ? 521  GLU A CG  1 
ATOM   3983  C  CD  . GLU A  1 504 ? 52.901  -27.846 24.731  1.00 41.24 ? 521  GLU A CD  1 
ATOM   3984  O  OE1 . GLU A  1 504 ? 53.157  -26.868 25.471  1.00 44.14 ? 521  GLU A OE1 1 
ATOM   3985  O  OE2 . GLU A  1 504 ? 53.784  -28.601 24.273  1.00 46.38 ? 521  GLU A OE2 1 
ATOM   3986  N  N   . VAL A  1 505 ? 48.516  -29.089 26.398  1.00 25.01 ? 522  VAL A N   1 
ATOM   3987  C  CA  . VAL A  1 505 ? 48.225  -30.410 26.936  1.00 23.79 ? 522  VAL A CA  1 
ATOM   3988  C  C   . VAL A  1 505 ? 46.893  -30.910 26.373  1.00 22.74 ? 522  VAL A C   1 
ATOM   3989  O  O   . VAL A  1 505 ? 46.812  -32.052 25.929  1.00 21.66 ? 522  VAL A O   1 
ATOM   3990  C  CB  . VAL A  1 505 ? 48.243  -30.404 28.479  1.00 24.05 ? 522  VAL A CB  1 
ATOM   3991  C  CG1 . VAL A  1 505 ? 47.636  -31.668 29.076  1.00 24.75 ? 522  VAL A CG1 1 
ATOM   3992  C  CG2 . VAL A  1 505 ? 49.651  -30.193 29.020  1.00 23.91 ? 522  VAL A CG2 1 
ATOM   3993  N  N   . SER A  1 506 ? 45.870  -30.042 26.355  1.00 21.95 ? 523  SER A N   1 
ATOM   3994  C  CA  . SER A  1 506 ? 44.544  -30.440 25.900  1.00 21.83 ? 523  SER A CA  1 
ATOM   3995  C  C   . SER A  1 506 ? 44.560  -30.822 24.420  1.00 22.58 ? 523  SER A C   1 
ATOM   3996  O  O   . SER A  1 506 ? 43.919  -31.795 24.031  1.00 21.63 ? 523  SER A O   1 
ATOM   3997  C  CB  . SER A  1 506 ? 43.507  -29.371 26.170  1.00 21.49 ? 523  SER A CB  1 
ATOM   3998  O  OG  . SER A  1 506 ? 43.370  -29.135 27.569  1.00 21.61 ? 523  SER A OG  1 
ATOM   3999  N  N   . ILE A  1 507 ? 45.268  -30.042 23.593  1.00 23.02 ? 524  ILE A N   1 
ATOM   4000  C  CA  . ILE A  1 507 ? 45.301  -30.298 22.162  1.00 24.00 ? 524  ILE A CA  1 
ATOM   4001  C  C   . ILE A  1 507 ? 46.005  -31.627 21.909  1.00 23.11 ? 524  ILE A C   1 
ATOM   4002  O  O   . ILE A  1 507 ? 45.553  -32.413 21.082  1.00 22.31 ? 524  ILE A O   1 
ATOM   4003  C  CB  . ILE A  1 507 ? 45.939  -29.124 21.395  1.00 25.26 ? 524  ILE A CB  1 
ATOM   4004  C  CG1 . ILE A  1 507 ? 45.096  -27.853 21.514  1.00 27.47 ? 524  ILE A CG1 1 
ATOM   4005  C  CG2 . ILE A  1 507 ? 46.199  -29.476 19.932  1.00 26.03 ? 524  ILE A CG2 1 
ATOM   4006  C  CD1 . ILE A  1 507 ? 43.612  -28.056 21.266  1.00 29.24 ? 524  ILE A CD1 1 
ATOM   4007  N  N   . ASN A  1 508 ? 47.096  -31.884 22.640  1.00 24.15 ? 525  ASN A N   1 
ATOM   4008  C  CA  . ASN A  1 508 ? 47.853  -33.116 22.480  1.00 24.09 ? 525  ASN A CA  1 
ATOM   4009  C  C   . ASN A  1 508 ? 47.007  -34.328 22.867  1.00 22.57 ? 525  ASN A C   1 
ATOM   4010  O  O   . ASN A  1 508 ? 47.122  -35.383 22.245  1.00 21.66 ? 525  ASN A O   1 
ATOM   4011  C  CB  . ASN A  1 508 ? 49.155  -33.074 23.271  1.00 26.48 ? 525  ASN A CB  1 
ATOM   4012  C  CG  . ASN A  1 508 ? 50.217  -32.237 22.596  1.00 29.54 ? 525  ASN A CG  1 
ATOM   4013  O  OD1 . ASN A  1 508 ? 50.072  -31.853 21.428  1.00 31.93 ? 525  ASN A OD1 1 
ATOM   4014  N  ND2 . ASN A  1 508 ? 51.302  -31.960 23.306  1.00 30.50 ? 525  ASN A ND2 1 
ATOM   4015  N  N   . ILE A  1 509 ? 46.170  -34.181 23.901  1.00 21.98 ? 526  ILE A N   1 
ATOM   4016  C  CA  . ILE A  1 509 ? 45.241  -35.239 24.272  1.00 22.64 ? 526  ILE A CA  1 
ATOM   4017  C  C   . ILE A  1 509 ? 44.233  -35.446 23.143  1.00 21.40 ? 526  ILE A C   1 
ATOM   4018  O  O   . ILE A  1 509 ? 43.970  -36.583 22.771  1.00 21.06 ? 526  ILE A O   1 
ATOM   4019  C  CB  . ILE A  1 509 ? 44.559  -34.949 25.621  1.00 23.55 ? 526  ILE A CB  1 
ATOM   4020  C  CG1 . ILE A  1 509 ? 45.560  -35.085 26.774  1.00 24.90 ? 526  ILE A CG1 1 
ATOM   4021  C  CG2 . ILE A  1 509 ? 43.343  -35.855 25.832  1.00 23.65 ? 526  ILE A CG2 1 
ATOM   4022  C  CD1 . ILE A  1 509 ? 45.063  -34.510 28.083  1.00 25.43 ? 526  ILE A CD1 1 
ATOM   4023  N  N   . ALA A  1 510 ? 43.693  -34.350 22.591  1.00 21.42 ? 527  ALA A N   1 
ATOM   4024  C  CA  . ALA A  1 510 ? 42.695  -34.434 21.533  1.00 21.71 ? 527  ALA A CA  1 
ATOM   4025  C  C   . ALA A  1 510 ? 43.255  -35.154 20.306  1.00 21.42 ? 527  ALA A C   1 
ATOM   4026  O  O   . ALA A  1 510 ? 42.552  -35.940 19.675  1.00 21.51 ? 527  ALA A O   1 
ATOM   4027  C  CB  . ALA A  1 510 ? 42.194  -33.054 21.177  1.00 22.16 ? 527  ALA A CB  1 
ATOM   4028  N  N   . ILE A  1 511 ? 44.532  -34.909 19.986  1.00 21.75 ? 528  ILE A N   1 
ATOM   4029  C  CA  . ILE A  1 511 ? 45.162  -35.552 18.841  1.00 21.83 ? 528  ILE A CA  1 
ATOM   4030  C  C   . ILE A  1 511 ? 45.275  -37.055 19.082  1.00 22.99 ? 528  ILE A C   1 
ATOM   4031  O  O   . ILE A  1 511 ? 44.994  -37.849 18.185  1.00 23.66 ? 528  ILE A O   1 
ATOM   4032  C  CB  . ILE A  1 511 ? 46.527  -34.909 18.529  1.00 21.89 ? 528  ILE A CB  1 
ATOM   4033  C  CG1 . ILE A  1 511 ? 46.355  -33.465 18.071  1.00 21.28 ? 528  ILE A CG1 1 
ATOM   4034  C  CG2 . ILE A  1 511 ? 47.300  -35.734 17.500  1.00 22.68 ? 528  ILE A CG2 1 
ATOM   4035  C  CD1 . ILE A  1 511 ? 47.640  -32.661 18.007  1.00 21.24 ? 528  ILE A CD1 1 
ATOM   4036  N  N   . LYS A  1 512 ? 45.690  -37.449 20.292  1.00 23.82 ? 529  LYS A N   1 
ATOM   4037  C  CA  . LYS A  1 512 ? 45.842  -38.856 20.625  1.00 24.19 ? 529  LYS A CA  1 
ATOM   4038  C  C   . LYS A  1 512 ? 44.489  -39.560 20.637  1.00 22.64 ? 529  LYS A C   1 
ATOM   4039  O  O   . LYS A  1 512 ? 44.377  -40.694 20.172  1.00 23.11 ? 529  LYS A O   1 
ATOM   4040  C  CB  . LYS A  1 512 ? 46.508  -39.051 21.993  1.00 26.58 ? 529  LYS A CB  1 
ATOM   4041  C  CG  . LYS A  1 512 ? 47.998  -38.770 22.037  1.00 30.18 ? 529  LYS A CG  1 
ATOM   4042  C  CD  . LYS A  1 512 ? 48.813  -39.633 21.084  1.00 34.01 ? 529  LYS A CD  1 
ATOM   4043  C  CE  . LYS A  1 512 ? 50.214  -39.868 21.568  1.00 38.50 ? 529  LYS A CE  1 
ATOM   4044  N  NZ  . LYS A  1 512 ? 50.908  -38.623 21.915  1.00 41.40 ? 529  LYS A NZ  1 
ATOM   4045  N  N   . VAL A  1 513 ? 43.469  -38.896 21.191  1.00 21.28 ? 530  VAL A N   1 
ATOM   4046  C  CA  . VAL A  1 513 ? 42.144  -39.488 21.284  1.00 20.69 ? 530  VAL A CA  1 
ATOM   4047  C  C   . VAL A  1 513 ? 41.540  -39.603 19.883  1.00 20.81 ? 530  VAL A C   1 
ATOM   4048  O  O   . VAL A  1 513 ? 40.890  -40.599 19.583  1.00 21.09 ? 530  VAL A O   1 
ATOM   4049  C  CB  . VAL A  1 513 ? 41.235  -38.717 22.260  1.00 21.18 ? 530  VAL A CB  1 
ATOM   4050  C  CG1 . VAL A  1 513 ? 39.793  -39.208 22.230  1.00 20.78 ? 530  VAL A CG1 1 
ATOM   4051  C  CG2 . VAL A  1 513 ? 41.763  -38.785 23.691  1.00 21.88 ? 530  VAL A CG2 1 
ATOM   4052  N  N   . THR A  1 514 ? 41.776  -38.599 19.026  1.00 20.88 ? 531  THR A N   1 
ATOM   4053  C  CA  . THR A  1 514 ? 41.313  -38.629 17.643  1.00 20.95 ? 531  THR A CA  1 
ATOM   4054  C  C   . THR A  1 514 ? 41.907  -39.841 16.921  1.00 21.12 ? 531  THR A C   1 
ATOM   4055  O  O   . THR A  1 514 ? 41.187  -40.579 16.251  1.00 20.27 ? 531  THR A O   1 
ATOM   4056  C  CB  . THR A  1 514 ? 41.676  -37.327 16.930  1.00 20.89 ? 531  THR A CB  1 
ATOM   4057  O  OG1 . THR A  1 514 ? 40.936  -36.268 17.531  1.00 20.51 ? 531  THR A OG1 1 
ATOM   4058  C  CG2 . THR A  1 514 ? 41.340  -37.370 15.449  1.00 21.40 ? 531  THR A CG2 1 
ATOM   4059  N  N   . GLU A  1 515 ? 43.222  -40.049 17.073  1.00 21.99 ? 532  GLU A N   1 
ATOM   4060  C  CA  . GLU A  1 515 ? 43.889  -41.220 16.522  1.00 23.76 ? 532  GLU A CA  1 
ATOM   4061  C  C   . GLU A  1 515 ? 43.206  -42.497 17.010  1.00 23.13 ? 532  GLU A C   1 
ATOM   4062  O  O   . GLU A  1 515 ? 42.944  -43.406 16.219  1.00 22.27 ? 532  GLU A O   1 
ATOM   4063  C  CB  . GLU A  1 515 ? 45.389  -41.220 16.828  1.00 25.99 ? 532  GLU A CB  1 
ATOM   4064  C  CG  . GLU A  1 515 ? 46.146  -40.175 16.013  1.00 30.10 ? 532  GLU A CG  1 
ATOM   4065  C  CD  . GLU A  1 515 ? 47.603  -39.919 16.364  1.00 35.69 ? 532  GLU A CD  1 
ATOM   4066  O  OE1 . GLU A  1 515 ? 48.292  -39.283 15.534  1.00 39.01 ? 532  GLU A OE1 1 
ATOM   4067  O  OE2 . GLU A  1 515 ? 48.056  -40.313 17.460  1.00 41.76 ? 532  GLU A OE2 1 
ATOM   4068  N  N   . TYR A  1 516 ? 42.915  -42.557 18.313  1.00 22.12 ? 533  TYR A N   1 
ATOM   4069  C  CA  . TYR A  1 516 ? 42.288  -43.732 18.898  1.00 21.59 ? 533  TYR A CA  1 
ATOM   4070  C  C   . TYR A  1 516 ? 40.904  -43.962 18.289  1.00 20.49 ? 533  TYR A C   1 
ATOM   4071  O  O   . TYR A  1 516 ? 40.566  -45.089 17.936  1.00 20.60 ? 533  TYR A O   1 
ATOM   4072  C  CB  . TYR A  1 516 ? 42.238  -43.586 20.424  1.00 21.44 ? 533  TYR A CB  1 
ATOM   4073  C  CG  . TYR A  1 516 ? 41.502  -44.722 21.117  1.00 21.88 ? 533  TYR A CG  1 
ATOM   4074  C  CD1 . TYR A  1 516 ? 42.163  -45.896 21.466  1.00 23.56 ? 533  TYR A CD1 1 
ATOM   4075  C  CD2 . TYR A  1 516 ? 40.149  -44.626 21.407  1.00 22.72 ? 533  TYR A CD2 1 
ATOM   4076  C  CE1 . TYR A  1 516 ? 41.495  -46.948 22.073  1.00 23.67 ? 533  TYR A CE1 1 
ATOM   4077  C  CE2 . TYR A  1 516 ? 39.471  -45.664 22.025  1.00 23.89 ? 533  TYR A CE2 1 
ATOM   4078  C  CZ  . TYR A  1 516 ? 40.147  -46.826 22.359  1.00 24.52 ? 533  TYR A CZ  1 
ATOM   4079  O  OH  . TYR A  1 516 ? 39.486  -47.855 22.967  1.00 26.17 ? 533  TYR A OH  1 
ATOM   4080  N  N   . LEU A  1 517 ? 40.100  -42.897 18.183  1.00 21.06 ? 534  LEU A N   1 
ATOM   4081  C  CA  . LEU A  1 517 ? 38.726  -43.015 17.713  1.00 21.30 ? 534  LEU A CA  1 
ATOM   4082  C  C   . LEU A  1 517 ? 38.706  -43.528 16.270  1.00 21.24 ? 534  LEU A C   1 
ATOM   4083  O  O   . LEU A  1 517 ? 37.888  -44.374 15.923  1.00 20.73 ? 534  LEU A O   1 
ATOM   4084  C  CB  . LEU A  1 517 ? 37.993  -41.677 17.856  1.00 20.88 ? 534  LEU A CB  1 
ATOM   4085  C  CG  . LEU A  1 517 ? 37.728  -41.172 19.281  1.00 20.39 ? 534  LEU A CG  1 
ATOM   4086  C  CD1 . LEU A  1 517 ? 37.257  -39.722 19.236  1.00 19.83 ? 534  LEU A CD1 1 
ATOM   4087  C  CD2 . LEU A  1 517 ? 36.714  -42.020 20.042  1.00 20.82 ? 534  LEU A CD2 1 
ATOM   4088  N  N   . TYR A  1 518 ? 39.632  -43.046 15.432  1.00 22.43 ? 535  TYR A N   1 
ATOM   4089  C  CA  . TYR A  1 518 ? 39.698  -43.486 14.044  1.00 22.73 ? 535  TYR A CA  1 
ATOM   4090  C  C   . TYR A  1 518 ? 40.143  -44.948 13.971  1.00 24.24 ? 535  TYR A C   1 
ATOM   4091  O  O   . TYR A  1 518 ? 39.613  -45.713 13.167  1.00 25.17 ? 535  TYR A O   1 
ATOM   4092  C  CB  . TYR A  1 518 ? 40.595  -42.591 13.181  1.00 22.40 ? 535  TYR A CB  1 
ATOM   4093  C  CG  . TYR A  1 518 ? 39.866  -41.392 12.584  1.00 21.37 ? 535  TYR A CG  1 
ATOM   4094  C  CD1 . TYR A  1 518 ? 38.923  -41.555 11.574  1.00 21.45 ? 535  TYR A CD1 1 
ATOM   4095  C  CD2 . TYR A  1 518 ? 40.113  -40.101 13.031  1.00 21.88 ? 535  TYR A CD2 1 
ATOM   4096  C  CE1 . TYR A  1 518 ? 38.241  -40.474 11.038  1.00 21.07 ? 535  TYR A CE1 1 
ATOM   4097  C  CE2 . TYR A  1 518 ? 39.450  -39.010 12.491  1.00 21.78 ? 535  TYR A CE2 1 
ATOM   4098  C  CZ  . TYR A  1 518 ? 38.510  -39.196 11.494  1.00 21.25 ? 535  TYR A CZ  1 
ATOM   4099  O  OH  . TYR A  1 518 ? 37.865  -38.109 10.980  1.00 22.69 ? 535  TYR A OH  1 
ATOM   4100  N  N   . ALA A  1 519 ? 41.105  -45.336 14.818  1.00 25.58 ? 536  ALA A N   1 
ATOM   4101  C  CA  . ALA A  1 519 ? 41.683  -46.671 14.762  1.00 25.57 ? 536  ALA A CA  1 
ATOM   4102  C  C   . ALA A  1 519 ? 40.703  -47.728 15.279  1.00 26.83 ? 536  ALA A C   1 
ATOM   4103  O  O   . ALA A  1 519 ? 40.848  -48.899 14.946  1.00 26.67 ? 536  ALA A O   1 
ATOM   4104  C  CB  . ALA A  1 519 ? 42.992  -46.707 15.527  1.00 25.40 ? 536  ALA A CB  1 
ATOM   4105  N  N   . ASN A  1 520 ? 39.704  -47.324 16.074  1.00 26.36 ? 537  ASN A N   1 
ATOM   4106  C  CA  . ASN A  1 520 ? 38.795  -48.274 16.699  1.00 27.65 ? 537  ASN A CA  1 
ATOM   4107  C  C   . ASN A  1 520 ? 37.373  -48.134 16.148  1.00 28.90 ? 537  ASN A C   1 
ATOM   4108  O  O   . ASN A  1 520 ? 36.424  -48.633 16.750  1.00 29.45 ? 537  ASN A O   1 
ATOM   4109  C  CB  . ASN A  1 520 ? 38.870  -48.161 18.218  1.00 28.35 ? 537  ASN A CB  1 
ATOM   4110  C  CG  . ASN A  1 520 ? 40.209  -48.621 18.741  1.00 28.62 ? 537  ASN A CG  1 
ATOM   4111  O  OD1 . ASN A  1 520 ? 40.361  -49.797 19.082  1.00 30.23 ? 537  ASN A OD1 1 
ATOM   4112  N  ND2 . ASN A  1 520 ? 41.199  -47.740 18.768  1.00 29.23 ? 537  ASN A ND2 1 
ATOM   4113  N  N   . LYS A  1 521 ? 37.243  -47.485 14.986  1.00 29.94 ? 538  LYS A N   1 
ATOM   4114  C  CA  . LYS A  1 521 ? 36.000  -47.407 14.233  1.00 32.27 ? 538  LYS A CA  1 
ATOM   4115  C  C   . LYS A  1 521 ? 34.937  -46.666 15.042  1.00 28.64 ? 538  LYS A C   1 
ATOM   4116  O  O   . LYS A  1 521 ? 33.767  -47.021 14.981  1.00 28.93 ? 538  LYS A O   1 
ATOM   4117  C  CB  . LYS A  1 521 ? 35.443  -48.777 13.817  1.00 37.69 ? 538  LYS A CB  1 
ATOM   4118  C  CG  . LYS A  1 521 ? 36.449  -49.855 13.431  1.00 42.76 ? 538  LYS A CG  1 
ATOM   4119  C  CD  . LYS A  1 521 ? 37.534  -49.457 12.436  1.00 45.87 ? 538  LYS A CD  1 
ATOM   4120  C  CE  . LYS A  1 521 ? 38.488  -50.597 12.202  1.00 48.76 ? 538  LYS A CE  1 
ATOM   4121  N  NZ  . LYS A  1 521 ? 39.735  -50.170 11.561  1.00 49.62 ? 538  LYS A NZ  1 
ATOM   4122  N  N   . MET A  1 522 ? 35.345  -45.632 15.786  1.00 26.29 ? 539  MET A N   1 
ATOM   4123  C  CA  . MET A  1 522 ? 34.422  -44.869 16.612  1.00 25.00 ? 539  MET A CA  1 
ATOM   4124  C  C   . MET A  1 522 ? 34.182  -43.480 16.020  1.00 23.84 ? 539  MET A C   1 
ATOM   4125  O  O   . MET A  1 522 ? 33.353  -42.733 16.539  1.00 23.43 ? 539  MET A O   1 
ATOM   4126  C  CB  . MET A  1 522 ? 34.965  -44.736 18.039  1.00 24.90 ? 539  MET A CB  1 
ATOM   4127  C  CG  . MET A  1 522 ? 35.126  -46.065 18.762  1.00 25.33 ? 539  MET A CG  1 
ATOM   4128  S  SD  . MET A  1 522 ? 36.053  -45.888 20.302  1.00 26.42 ? 539  MET A SD  1 
ATOM   4129  C  CE  . MET A  1 522 ? 36.057  -47.572 20.933  1.00 26.96 ? 539  MET A CE  1 
ATOM   4130  N  N   . ALA A  1 523 ? 34.910  -43.138 14.949  1.00 22.32 ? 540  ALA A N   1 
ATOM   4131  C  CA  . ALA A  1 523 ? 34.756  -41.862 14.266  1.00 21.62 ? 540  ALA A CA  1 
ATOM   4132  C  C   . ALA A  1 523 ? 33.851  -42.030 13.047  1.00 22.30 ? 540  ALA A C   1 
ATOM   4133  O  O   . ALA A  1 523 ? 33.830  -43.103 12.444  1.00 21.31 ? 540  ALA A O   1 
ATOM   4134  C  CB  . ALA A  1 523 ? 36.116  -41.337 13.859  1.00 21.25 ? 540  ALA A CB  1 
ATOM   4135  N  N   . PHE A  1 524 ? 33.115  -40.961 12.695  1.00 22.89 ? 541  PHE A N   1 
ATOM   4136  C  CA  . PHE A  1 524 ? 32.221  -40.968 11.545  1.00 23.25 ? 541  PHE A CA  1 
ATOM   4137  C  C   . PHE A  1 524 ? 32.515  -39.814 10.586  1.00 24.20 ? 541  PHE A C   1 
ATOM   4138  O  O   . PHE A  1 524 ? 31.839  -39.693 9.568   1.00 25.93 ? 541  PHE A O   1 
ATOM   4139  C  CB  . PHE A  1 524 ? 30.760  -40.948 12.010  1.00 24.04 ? 541  PHE A CB  1 
ATOM   4140  C  CG  . PHE A  1 524 ? 30.356  -42.281 12.625  1.00 24.95 ? 541  PHE A CG  1 
ATOM   4141  C  CD1 . PHE A  1 524 ? 29.978  -43.348 11.818  1.00 25.45 ? 541  PHE A CD1 1 
ATOM   4142  C  CD2 . PHE A  1 524 ? 30.413  -42.481 14.000  1.00 25.69 ? 541  PHE A CD2 1 
ATOM   4143  C  CE1 . PHE A  1 524 ? 29.641  -44.575 12.375  1.00 26.47 ? 541  PHE A CE1 1 
ATOM   4144  C  CE2 . PHE A  1 524 ? 30.075  -43.709 14.552  1.00 26.47 ? 541  PHE A CE2 1 
ATOM   4145  C  CZ  . PHE A  1 524 ? 29.690  -44.752 13.740  1.00 26.63 ? 541  PHE A CZ  1 
ATOM   4146  N  N   . ARG A  1 525 ? 33.535  -38.997 10.883  1.00 24.14 ? 542  ARG A N   1 
ATOM   4147  C  CA  . ARG A  1 525 ? 33.944  -37.921 9.993   1.00 23.97 ? 542  ARG A CA  1 
ATOM   4148  C  C   . ARG A  1 525 ? 34.897  -38.480 8.943   1.00 23.31 ? 542  ARG A C   1 
ATOM   4149  O  O   . ARG A  1 525 ? 36.020  -38.873 9.259   1.00 22.83 ? 542  ARG A O   1 
ATOM   4150  C  CB  . ARG A  1 525 ? 34.586  -36.787 10.797  1.00 24.28 ? 542  ARG A CB  1 
ATOM   4151  C  CG  . ARG A  1 525 ? 34.722  -35.466 10.056  1.00 24.59 ? 542  ARG A CG  1 
ATOM   4152  C  CD  . ARG A  1 525 ? 35.800  -35.483 8.983   1.00 25.60 ? 542  ARG A CD  1 
ATOM   4153  N  NE  . ARG A  1 525 ? 35.986  -34.131 8.446   1.00 26.57 ? 542  ARG A NE  1 
ATOM   4154  C  CZ  . ARG A  1 525 ? 36.647  -33.801 7.345   1.00 27.61 ? 542  ARG A CZ  1 
ATOM   4155  N  NH1 . ARG A  1 525 ? 37.183  -34.725 6.568   1.00 28.18 ? 542  ARG A NH1 1 
ATOM   4156  N  NH2 . ARG A  1 525 ? 36.754  -32.528 7.025   1.00 27.43 ? 542  ARG A NH2 1 
ATOM   4157  N  N   . TYR A  1 526 ? 34.426  -38.513 7.689   1.00 24.04 ? 543  TYR A N   1 
ATOM   4158  C  CA  . TYR A  1 526 ? 35.212  -38.969 6.552   1.00 25.24 ? 543  TYR A CA  1 
ATOM   4159  C  C   . TYR A  1 526 ? 35.109  -37.922 5.443   1.00 25.27 ? 543  TYR A C   1 
ATOM   4160  O  O   . TYR A  1 526 ? 34.080  -37.269 5.319   1.00 23.63 ? 543  TYR A O   1 
ATOM   4161  C  CB  . TYR A  1 526 ? 34.741  -40.359 6.109   1.00 27.00 ? 543  TYR A CB  1 
ATOM   4162  C  CG  . TYR A  1 526 ? 35.102  -41.440 7.115   1.00 28.72 ? 543  TYR A CG  1 
ATOM   4163  C  CD1 . TYR A  1 526 ? 36.403  -41.919 7.206   1.00 30.36 ? 543  TYR A CD1 1 
ATOM   4164  C  CD2 . TYR A  1 526 ? 34.156  -41.951 7.997   1.00 30.55 ? 543  TYR A CD2 1 
ATOM   4165  C  CE1 . TYR A  1 526 ? 36.753  -42.882 8.139   1.00 31.71 ? 543  TYR A CE1 1 
ATOM   4166  C  CE2 . TYR A  1 526 ? 34.494  -42.916 8.933   1.00 31.88 ? 543  TYR A CE2 1 
ATOM   4167  C  CZ  . TYR A  1 526 ? 35.795  -43.385 9.000   1.00 32.16 ? 543  TYR A CZ  1 
ATOM   4168  O  OH  . TYR A  1 526 ? 36.151  -44.334 9.912   1.00 34.61 ? 543  TYR A OH  1 
ATOM   4169  N  N   . PRO A  1 527 ? 36.146  -37.706 4.601   1.00 26.40 ? 544  PRO A N   1 
ATOM   4170  C  CA  . PRO A  1 527 ? 37.394  -38.477 4.630   1.00 26.58 ? 544  PRO A CA  1 
ATOM   4171  C  C   . PRO A  1 527 ? 38.198  -38.380 5.926   1.00 26.72 ? 544  PRO A C   1 
ATOM   4172  O  O   . PRO A  1 527 ? 38.213  -37.339 6.579   1.00 26.36 ? 544  PRO A O   1 
ATOM   4173  C  CB  . PRO A  1 527 ? 38.215  -37.908 3.444   1.00 26.64 ? 544  PRO A CB  1 
ATOM   4174  C  CG  . PRO A  1 527 ? 37.223  -37.139 2.598   1.00 26.87 ? 544  PRO A CG  1 
ATOM   4175  C  CD  . PRO A  1 527 ? 36.132  -36.689 3.538   1.00 27.09 ? 544  PRO A CD  1 
ATOM   4176  N  N   . GLU A  1 528 ? 38.875  -39.484 6.267   1.00 26.31 ? 545  GLU A N   1 
ATOM   4177  C  CA  . GLU A  1 528 ? 39.753  -39.553 7.424   1.00 26.88 ? 545  GLU A CA  1 
ATOM   4178  C  C   . GLU A  1 528 ? 41.046  -38.802 7.125   1.00 27.19 ? 545  GLU A C   1 
ATOM   4179  O  O   . GLU A  1 528 ? 41.699  -39.086 6.127   1.00 28.01 ? 545  GLU A O   1 
ATOM   4180  C  CB  . GLU A  1 528 ? 40.087  -41.011 7.741   1.00 26.73 ? 545  GLU A CB  1 
ATOM   4181  C  CG  . GLU A  1 528 ? 41.150  -41.179 8.825   1.00 27.96 ? 545  GLU A CG  1 
ATOM   4182  C  CD  . GLU A  1 528 ? 41.394  -42.614 9.257   1.00 27.83 ? 545  GLU A CD  1 
ATOM   4183  O  OE1 . GLU A  1 528 ? 40.613  -43.510 8.869   1.00 30.15 ? 545  GLU A OE1 1 
ATOM   4184  O  OE2 . GLU A  1 528 ? 42.378  -42.827 9.994   1.00 29.19 ? 545  GLU A OE2 1 
ATOM   4185  N  N   . PRO A  1 529 ? 41.479  -37.860 7.994   1.00 27.01 ? 546  PRO A N   1 
ATOM   4186  C  CA  . PRO A  1 529 ? 42.722  -37.126 7.766   1.00 27.80 ? 546  PRO A CA  1 
ATOM   4187  C  C   . PRO A  1 529 ? 43.924  -38.051 7.916   1.00 29.09 ? 546  PRO A C   1 
ATOM   4188  O  O   . PRO A  1 529 ? 43.954  -38.892 8.813   1.00 29.04 ? 546  PRO A O   1 
ATOM   4189  C  CB  . PRO A  1 529 ? 42.684  -36.038 8.844   1.00 27.75 ? 546  PRO A CB  1 
ATOM   4190  C  CG  . PRO A  1 529 ? 41.876  -36.670 9.960   1.00 27.81 ? 546  PRO A CG  1 
ATOM   4191  C  CD  . PRO A  1 529 ? 40.813  -37.476 9.250   1.00 27.08 ? 546  PRO A CD  1 
ATOM   4192  N  N   . GLU A  1 530 ? 44.905  -37.889 7.024   1.00 30.21 ? 547  GLU A N   1 
ATOM   4193  C  CA  . GLU A  1 530 ? 46.156  -38.618 7.124   1.00 31.17 ? 547  GLU A CA  1 
ATOM   4194  C  C   . GLU A  1 530 ? 46.936  -38.129 8.342   1.00 31.70 ? 547  GLU A C   1 
ATOM   4195  O  O   . GLU A  1 530 ? 47.579  -38.931 9.011   1.00 32.79 ? 547  GLU A O   1 
ATOM   4196  C  CB  . GLU A  1 530 ? 46.989  -38.451 5.852   1.00 32.75 ? 547  GLU A CB  1 
ATOM   4197  N  N   . ASP A  1 531 ? 46.881  -36.815 8.612   1.00 31.34 ? 548  ASP A N   1 
ATOM   4198  C  CA  . ASP A  1 531 ? 47.657  -36.196 9.676   1.00 31.88 ? 548  ASP A CA  1 
ATOM   4199  C  C   . ASP A  1 531 ? 46.706  -35.631 10.733  1.00 30.28 ? 548  ASP A C   1 
ATOM   4200  O  O   . ASP A  1 531 ? 46.115  -34.569 10.542  1.00 28.26 ? 548  ASP A O   1 
ATOM   4201  C  CB  . ASP A  1 531 ? 48.610  -35.149 9.117   1.00 33.35 ? 548  ASP A CB  1 
ATOM   4202  C  CG  . ASP A  1 531 ? 49.512  -34.449 10.126  1.00 35.72 ? 548  ASP A CG  1 
ATOM   4203  O  OD1 . ASP A  1 531 ? 49.307  -34.637 11.345  1.00 36.36 ? 548  ASP A OD1 1 
ATOM   4204  O  OD2 . ASP A  1 531 ? 50.424  -33.724 9.685   1.00 38.18 ? 548  ASP A OD2 1 
ATOM   4205  N  N   . LYS A  1 532 ? 46.589  -36.344 11.862  1.00 28.88 ? 549  LYS A N   1 
ATOM   4206  C  CA  . LYS A  1 532 ? 45.598  -36.026 12.881  1.00 28.51 ? 549  LYS A CA  1 
ATOM   4207  C  C   . LYS A  1 532 ? 45.992  -34.764 13.646  1.00 26.80 ? 549  LYS A C   1 
ATOM   4208  O  O   . LYS A  1 532 ? 45.124  -34.020 14.098  1.00 26.83 ? 549  LYS A O   1 
ATOM   4209  C  CB  . LYS A  1 532 ? 45.383  -37.202 13.844  1.00 28.45 ? 549  LYS A CB  1 
ATOM   4210  C  CG  . LYS A  1 532 ? 44.398  -38.263 13.380  1.00 28.25 ? 549  LYS A CG  1 
ATOM   4211  C  CD  . LYS A  1 532 ? 44.809  -38.999 12.112  1.00 28.67 ? 549  LYS A CD  1 
ATOM   4212  C  CE  . LYS A  1 532 ? 43.978  -40.216 11.865  1.00 29.12 ? 549  LYS A CE  1 
ATOM   4213  N  NZ  . LYS A  1 532 ? 44.356  -40.900 10.627  1.00 29.14 ? 549  LYS A NZ  1 
ATOM   4214  N  N   . ALA A  1 533 ? 47.297  -34.530 13.808  1.00 26.69 ? 550  ALA A N   1 
ATOM   4215  C  CA  . ALA A  1 533 ? 47.772  -33.347 14.506  1.00 27.12 ? 550  ALA A CA  1 
ATOM   4216  C  C   . ALA A  1 533 ? 47.351  -32.093 13.743  1.00 26.98 ? 550  ALA A C   1 
ATOM   4217  O  O   . ALA A  1 533 ? 46.839  -31.145 14.332  1.00 25.68 ? 550  ALA A O   1 
ATOM   4218  C  CB  . ALA A  1 533 ? 49.274  -33.413 14.696  1.00 28.20 ? 550  ALA A CB  1 
ATOM   4219  N  N   . LYS A  1 534 ? 47.563  -32.109 12.424  1.00 28.51 ? 551  LYS A N   1 
ATOM   4220  C  CA  . LYS A  1 534 ? 47.191  -31.004 11.555  1.00 29.11 ? 551  LYS A CA  1 
ATOM   4221  C  C   . LYS A  1 534 ? 45.676  -30.828 11.555  1.00 27.09 ? 551  LYS A C   1 
ATOM   4222  O  O   . LYS A  1 534 ? 45.183  -29.706 11.623  1.00 28.42 ? 551  LYS A O   1 
ATOM   4223  C  CB  . LYS A  1 534 ? 47.705  -31.289 10.139  1.00 32.74 ? 551  LYS A CB  1 
ATOM   4224  C  CG  . LYS A  1 534 ? 47.381  -30.244 9.081   1.00 36.84 ? 551  LYS A CG  1 
ATOM   4225  C  CD  . LYS A  1 534 ? 47.991  -30.590 7.727   1.00 41.42 ? 551  LYS A CD  1 
ATOM   4226  C  CE  . LYS A  1 534 ? 47.666  -29.602 6.650   1.00 44.99 ? 551  LYS A CE  1 
ATOM   4227  N  NZ  . LYS A  1 534 ? 46.251  -29.637 6.272   1.00 47.56 ? 551  LYS A NZ  1 
ATOM   4228  N  N   . TYR A  1 535 ? 44.955  -31.950 11.462  1.00 25.34 ? 552  TYR A N   1 
ATOM   4229  C  CA  . TYR A  1 535 ? 43.501  -31.960 11.461  1.00 24.77 ? 552  TYR A CA  1 
ATOM   4230  C  C   . TYR A  1 535 ? 42.956  -31.204 12.672  1.00 24.09 ? 552  TYR A C   1 
ATOM   4231  O  O   . TYR A  1 535 ? 42.093  -30.347 12.522  1.00 23.64 ? 552  TYR A O   1 
ATOM   4232  C  CB  . TYR A  1 535 ? 42.992  -33.405 11.437  1.00 23.25 ? 552  TYR A CB  1 
ATOM   4233  C  CG  . TYR A  1 535 ? 41.476  -33.535 11.445  1.00 22.65 ? 552  TYR A CG  1 
ATOM   4234  C  CD1 . TYR A  1 535 ? 40.730  -33.259 10.306  1.00 22.53 ? 552  TYR A CD1 1 
ATOM   4235  C  CD2 . TYR A  1 535 ? 40.792  -33.956 12.580  1.00 22.59 ? 552  TYR A CD2 1 
ATOM   4236  C  CE1 . TYR A  1 535 ? 39.349  -33.367 10.300  1.00 22.51 ? 552  TYR A CE1 1 
ATOM   4237  C  CE2 . TYR A  1 535 ? 39.411  -34.085 12.583  1.00 22.43 ? 552  TYR A CE2 1 
ATOM   4238  C  CZ  . TYR A  1 535 ? 38.686  -33.782 11.442  1.00 22.65 ? 552  TYR A CZ  1 
ATOM   4239  O  OH  . TYR A  1 535 ? 37.325  -33.892 11.428  1.00 23.57 ? 552  TYR A OH  1 
ATOM   4240  N  N   . VAL A  1 536 ? 43.451  -31.542 13.869  1.00 23.90 ? 553  VAL A N   1 
ATOM   4241  C  CA  . VAL A  1 536 ? 42.941  -30.968 15.105  1.00 23.54 ? 553  VAL A CA  1 
ATOM   4242  C  C   . VAL A  1 536 ? 43.369  -29.503 15.214  1.00 24.26 ? 553  VAL A C   1 
ATOM   4243  O  O   . VAL A  1 536 ? 42.542  -28.639 15.494  1.00 22.99 ? 553  VAL A O   1 
ATOM   4244  C  CB  . VAL A  1 536 ? 43.381  -31.791 16.334  1.00 23.34 ? 553  VAL A CB  1 
ATOM   4245  C  CG1 . VAL A  1 536 ? 43.021  -31.104 17.645  1.00 23.47 ? 553  VAL A CG1 1 
ATOM   4246  C  CG2 . VAL A  1 536 ? 42.807  -33.203 16.307  1.00 23.58 ? 553  VAL A CG2 1 
ATOM   4247  N  N   . LYS A  1 537 ? 44.651  -29.213 14.961  1.00 25.37 ? 554  LYS A N   1 
ATOM   4248  C  CA  . LYS A  1 537 ? 45.187  -27.874 15.175  1.00 27.67 ? 554  LYS A CA  1 
ATOM   4249  C  C   . LYS A  1 537 ? 44.560  -26.845 14.232  1.00 28.19 ? 554  LYS A C   1 
ATOM   4250  O  O   . LYS A  1 537 ? 44.473  -25.672 14.588  1.00 29.23 ? 554  LYS A O   1 
ATOM   4251  C  CB  . LYS A  1 537 ? 46.716  -27.871 15.070  1.00 29.54 ? 554  LYS A CB  1 
ATOM   4252  C  CG  . LYS A  1 537 ? 47.427  -28.545 16.242  1.00 30.66 ? 554  LYS A CG  1 
ATOM   4253  C  CD  . LYS A  1 537 ? 48.943  -28.639 16.104  1.00 32.36 ? 554  LYS A CD  1 
ATOM   4254  C  CE  . LYS A  1 537 ? 49.574  -29.295 17.294  1.00 35.15 ? 554  LYS A CE  1 
ATOM   4255  N  NZ  . LYS A  1 537 ? 51.039  -29.249 17.240  1.00 36.34 ? 554  LYS A NZ  1 
ATOM   4256  N  N   . GLU A  1 538 ? 44.120  -27.272 13.041  1.00 28.99 ? 555  GLU A N   1 
ATOM   4257  C  CA  . GLU A  1 538 ? 43.511  -26.365 12.076  1.00 29.68 ? 555  GLU A CA  1 
ATOM   4258  C  C   . GLU A  1 538 ? 42.060  -26.053 12.441  1.00 28.03 ? 555  GLU A C   1 
ATOM   4259  O  O   . GLU A  1 538 ? 41.470  -25.138 11.872  1.00 27.03 ? 555  GLU A O   1 
ATOM   4260  C  CB  . GLU A  1 538 ? 43.577  -26.926 10.654  1.00 32.06 ? 555  GLU A CB  1 
ATOM   4261  C  CG  . GLU A  1 538 ? 44.972  -26.824 10.046  1.00 35.66 ? 555  GLU A CG  1 
ATOM   4262  C  CD  . GLU A  1 538 ? 45.120  -27.331 8.621   1.00 39.90 ? 555  GLU A CD  1 
ATOM   4263  O  OE1 . GLU A  1 538 ? 44.154  -27.887 8.050   1.00 40.84 ? 555  GLU A OE1 1 
ATOM   4264  O  OE2 . GLU A  1 538 ? 46.234  -27.152 8.083   1.00 45.64 ? 555  GLU A OE2 1 
ATOM   4265  N  N   . ARG A  1 539 ? 41.483  -26.788 13.398  1.00 25.92 ? 556  ARG A N   1 
ATOM   4266  C  CA  . ARG A  1 539 ? 40.068  -26.641 13.705  1.00 25.34 ? 556  ARG A CA  1 
ATOM   4267  C  C   . ARG A  1 539 ? 39.828  -25.983 15.066  1.00 25.84 ? 556  ARG A C   1 
ATOM   4268  O  O   . ARG A  1 539 ? 38.680  -25.680 15.389  1.00 26.76 ? 556  ARG A O   1 
ATOM   4269  C  CB  . ARG A  1 539 ? 39.390  -28.010 13.576  1.00 24.92 ? 556  ARG A CB  1 
ATOM   4270  C  CG  . ARG A  1 539 ? 39.190  -28.388 12.114  1.00 25.81 ? 556  ARG A CG  1 
ATOM   4271  C  CD  . ARG A  1 539 ? 38.788  -29.838 11.886  1.00 26.78 ? 556  ARG A CD  1 
ATOM   4272  N  NE  . ARG A  1 539 ? 38.650  -30.128 10.451  1.00 27.13 ? 556  ARG A NE  1 
ATOM   4273  C  CZ  . ARG A  1 539 ? 39.635  -30.136 9.552   1.00 27.89 ? 556  ARG A CZ  1 
ATOM   4274  N  NH1 . ARG A  1 539 ? 40.890  -29.971 9.926   1.00 28.28 ? 556  ARG A NH1 1 
ATOM   4275  N  NH2 . ARG A  1 539 ? 39.368  -30.337 8.273   1.00 28.25 ? 556  ARG A NH2 1 
ATOM   4276  N  N   . THR A  1 540 ? 40.882  -25.737 15.857  1.00 25.55 ? 557  THR A N   1 
ATOM   4277  C  CA  . THR A  1 540 ? 40.703  -25.114 17.162  1.00 25.52 ? 557  THR A CA  1 
ATOM   4278  C  C   . THR A  1 540 ? 40.348  -23.643 16.968  1.00 25.15 ? 557  THR A C   1 
ATOM   4279  O  O   . THR A  1 540 ? 40.939  -22.963 16.135  1.00 24.32 ? 557  THR A O   1 
ATOM   4280  C  CB  . THR A  1 540 ? 41.939  -25.256 18.050  1.00 27.04 ? 557  THR A CB  1 
ATOM   4281  O  OG1 . THR A  1 540 ? 43.029  -24.674 17.344  1.00 27.05 ? 557  THR A OG1 1 
ATOM   4282  C  CG2 . THR A  1 540 ? 42.259  -26.696 18.400  1.00 28.43 ? 557  THR A CG2 1 
ATOM   4283  N  N   . TRP A  1 541 ? 39.382  -23.168 17.759  1.00 24.51 ? 558  TRP A N   1 
ATOM   4284  C  CA  . TRP A  1 541 ? 38.943  -21.782 17.722  1.00 25.66 ? 558  TRP A CA  1 
ATOM   4285  C  C   . TRP A  1 541 ? 40.014  -20.876 18.324  1.00 26.72 ? 558  TRP A C   1 
ATOM   4286  O  O   . TRP A  1 541 ? 40.621  -21.222 19.330  1.00 27.45 ? 558  TRP A O   1 
ATOM   4287  C  CB  . TRP A  1 541 ? 37.614  -21.650 18.478  1.00 24.57 ? 558  TRP A CB  1 
ATOM   4288  C  CG  . TRP A  1 541 ? 37.057  -20.256 18.539  1.00 23.16 ? 558  TRP A CG  1 
ATOM   4289  C  CD1 . TRP A  1 541 ? 36.261  -19.646 17.613  1.00 23.54 ? 558  TRP A CD1 1 
ATOM   4290  C  CD2 . TRP A  1 541 ? 37.230  -19.303 19.608  1.00 22.87 ? 558  TRP A CD2 1 
ATOM   4291  N  NE1 . TRP A  1 541 ? 35.937  -18.381 18.023  1.00 22.93 ? 558  TRP A NE1 1 
ATOM   4292  C  CE2 . TRP A  1 541 ? 36.511  -18.142 19.242  1.00 22.60 ? 558  TRP A CE2 1 
ATOM   4293  C  CE3 . TRP A  1 541 ? 37.916  -19.314 20.826  1.00 22.96 ? 558  TRP A CE3 1 
ATOM   4294  C  CZ2 . TRP A  1 541 ? 36.466  -17.009 20.051  1.00 22.61 ? 558  TRP A CZ2 1 
ATOM   4295  C  CZ3 . TRP A  1 541 ? 37.867  -18.193 21.626  1.00 23.38 ? 558  TRP A CZ3 1 
ATOM   4296  C  CH2 . TRP A  1 541 ? 37.146  -17.060 21.245  1.00 22.80 ? 558  TRP A CH2 1 
ATOM   4297  N  N   . ARG A  1 542 ? 40.208  -19.709 17.703  1.00 27.73 ? 559  ARG A N   1 
ATOM   4298  C  CA  . ARG A  1 542 ? 41.272  -18.783 18.055  1.00 30.51 ? 559  ARG A CA  1 
ATOM   4299  C  C   . ARG A  1 542 ? 40.667  -17.488 18.593  1.00 28.61 ? 559  ARG A C   1 
ATOM   4300  O  O   . ARG A  1 542 ? 39.657  -17.010 18.085  1.00 27.44 ? 559  ARG A O   1 
ATOM   4301  C  CB  . ARG A  1 542 ? 42.117  -18.518 16.804  1.00 33.97 ? 559  ARG A CB  1 
ATOM   4302  C  CG  . ARG A  1 542 ? 42.749  -19.750 16.169  1.00 38.37 ? 559  ARG A CG  1 
ATOM   4303  C  CD  . ARG A  1 542 ? 43.404  -19.428 14.829  1.00 42.66 ? 559  ARG A CD  1 
ATOM   4304  N  NE  . ARG A  1 542 ? 44.591  -18.573 14.972  1.00 48.41 ? 559  ARG A NE  1 
ATOM   4305  C  CZ  . ARG A  1 542 ? 44.689  -17.276 14.658  1.00 53.00 ? 559  ARG A CZ  1 
ATOM   4306  N  NH1 . ARG A  1 542 ? 43.631  -16.582 14.265  1.00 52.59 ? 559  ARG A NH1 1 
ATOM   4307  N  NH2 . ARG A  1 542 ? 45.858  -16.665 14.764  1.00 55.19 ? 559  ARG A NH2 1 
ATOM   4308  N  N   . SER A  1 543 ? 41.319  -16.905 19.602  1.00 28.54 ? 560  SER A N   1 
ATOM   4309  C  CA  . SER A  1 543 ? 40.807  -15.721 20.277  1.00 28.42 ? 560  SER A CA  1 
ATOM   4310  C  C   . SER A  1 543 ? 41.326  -14.437 19.626  1.00 27.06 ? 560  SER A C   1 
ATOM   4311  O  O   . SER A  1 543 ? 40.903  -13.349 20.013  1.00 26.17 ? 560  SER A O   1 
ATOM   4312  C  CB  . SER A  1 543 ? 41.147  -15.762 21.743  1.00 28.92 ? 560  SER A CB  1 
ATOM   4313  O  OG  . SER A  1 543 ? 42.554  -15.828 21.920  1.00 29.61 ? 560  SER A OG  1 
ATOM   4314  N  N   . GLU A  1 544 ? 42.242  -14.553 18.653  1.00 26.00 ? 561  GLU A N   1 
ATOM   4315  C  CA  . GLU A  1 544 ? 42.695  -13.392 17.901  1.00 26.93 ? 561  GLU A CA  1 
ATOM   4316  C  C   . GLU A  1 544 ? 41.510  -12.756 17.173  1.00 25.52 ? 561  GLU A C   1 
ATOM   4317  O  O   . GLU A  1 544 ? 40.702  -13.458 16.568  1.00 23.98 ? 561  GLU A O   1 
ATOM   4318  C  CB  . GLU A  1 544 ? 43.751  -13.711 16.843  1.00 29.32 ? 561  GLU A CB  1 
ATOM   4319  C  CG  . GLU A  1 544 ? 45.140  -14.000 17.408  1.00 33.03 ? 561  GLU A CG  1 
ATOM   4320  C  CD  . GLU A  1 544 ? 45.371  -15.405 17.936  1.00 36.43 ? 561  GLU A CD  1 
ATOM   4321  O  OE1 . GLU A  1 544 ? 46.487  -15.656 18.438  1.00 39.57 ? 561  GLU A OE1 1 
ATOM   4322  O  OE2 . GLU A  1 544 ? 44.453  -16.250 17.855  1.00 38.44 ? 561  GLU A OE2 1 
ATOM   4323  N  N   . TYR A  1 545 ? 41.435  -11.420 17.222  1.00 23.90 ? 562  TYR A N   1 
ATOM   4324  C  CA  . TYR A  1 545 ? 40.460  -10.672 16.447  1.00 24.23 ? 562  TYR A CA  1 
ATOM   4325  C  C   . TYR A  1 545 ? 40.682  -10.912 14.953  1.00 26.31 ? 562  TYR A C   1 
ATOM   4326  O  O   . TYR A  1 545 ? 41.819  -11.041 14.501  1.00 27.36 ? 562  TYR A O   1 
ATOM   4327  C  CB  . TYR A  1 545 ? 40.564  -9.164  16.701  1.00 22.95 ? 562  TYR A CB  1 
ATOM   4328  C  CG  . TYR A  1 545 ? 40.191  -8.656  18.090  1.00 22.12 ? 562  TYR A CG  1 
ATOM   4329  C  CD1 . TYR A  1 545 ? 39.027  -9.063  18.741  1.00 21.54 ? 562  TYR A CD1 1 
ATOM   4330  C  CD2 . TYR A  1 545 ? 40.993  -7.721  18.735  1.00 21.67 ? 562  TYR A CD2 1 
ATOM   4331  C  CE1 . TYR A  1 545 ? 38.691  -8.575  19.997  1.00 20.77 ? 562  TYR A CE1 1 
ATOM   4332  C  CE2 . TYR A  1 545 ? 40.671  -7.228  19.992  1.00 21.59 ? 562  TYR A CE2 1 
ATOM   4333  C  CZ  . TYR A  1 545 ? 39.513  -7.649  20.623  1.00 21.05 ? 562  TYR A CZ  1 
ATOM   4334  O  OH  . TYR A  1 545 ? 39.213  -7.145  21.860  1.00 20.07 ? 562  TYR A OH  1 
ATOM   4335  N  N   . ASP A  1 546 ? 39.580  -10.948 14.196  1.00 27.27 ? 563  ASP A N   1 
ATOM   4336  C  CA  . ASP A  1 546 ? 39.628  -10.951 12.742  1.00 30.09 ? 563  ASP A CA  1 
ATOM   4337  C  C   . ASP A  1 546 ? 39.442  -9.533  12.216  1.00 28.58 ? 563  ASP A C   1 
ATOM   4338  O  O   . ASP A  1 546 ? 38.979  -8.647  12.934  1.00 26.72 ? 563  ASP A O   1 
ATOM   4339  C  CB  . ASP A  1 546 ? 38.565  -11.852 12.139  1.00 33.36 ? 563  ASP A CB  1 
ATOM   4340  C  CG  . ASP A  1 546 ? 38.651  -13.314 12.553  1.00 37.04 ? 563  ASP A CG  1 
ATOM   4341  O  OD1 . ASP A  1 546 ? 39.765  -13.878 12.478  1.00 40.20 ? 563  ASP A OD1 1 
ATOM   4342  O  OD2 . ASP A  1 546 ? 37.603  -13.872 12.943  1.00 41.55 ? 563  ASP A OD2 1 
ATOM   4343  N  N   . SER A  1 547 ? 39.812  -9.335  10.949  1.00 27.07 ? 564  SER A N   1 
ATOM   4344  C  CA  . SER A  1 547 ? 39.521  -8.090  10.262  1.00 28.10 ? 564  SER A CA  1 
ATOM   4345  C  C   . SER A  1 547 ? 38.035  -8.052  9.916   1.00 28.31 ? 564  SER A C   1 
ATOM   4346  O  O   . SER A  1 547 ? 37.488  -9.046  9.445   1.00 28.36 ? 564  SER A O   1 
ATOM   4347  C  CB  . SER A  1 547 ? 40.367  -7.927  9.026   1.00 29.02 ? 564  SER A CB  1 
ATOM   4348  O  OG  . SER A  1 547 ? 39.947  -6.790  8.284   1.00 29.90 ? 564  SER A OG  1 
ATOM   4349  N  N   . LEU A  1 548 ? 37.395  -6.903  10.157  1.00 27.48 ? 565  LEU A N   1 
ATOM   4350  C  CA  . LEU A  1 548 ? 36.009  -6.698  9.766   1.00 28.85 ? 565  LEU A CA  1 
ATOM   4351  C  C   . LEU A  1 548 ? 35.938  -5.593  8.715   1.00 28.87 ? 565  LEU A C   1 
ATOM   4352  O  O   . LEU A  1 548 ? 34.881  -5.003  8.501   1.00 29.98 ? 565  LEU A O   1 
ATOM   4353  C  CB  . LEU A  1 548 ? 35.171  -6.379  11.004  1.00 30.28 ? 565  LEU A CB  1 
ATOM   4354  C  CG  . LEU A  1 548 ? 35.030  -7.520  12.016  1.00 32.02 ? 565  LEU A CG  1 
ATOM   4355  C  CD1 . LEU A  1 548 ? 34.414  -7.049  13.324  1.00 34.43 ? 565  LEU A CD1 1 
ATOM   4356  C  CD2 . LEU A  1 548 ? 34.206  -8.647  11.431  1.00 33.17 ? 565  LEU A CD2 1 
ATOM   4357  N  N   . LEU A  1 549 ? 37.069  -5.350  8.039   1.00 28.26 ? 566  LEU A N   1 
ATOM   4358  C  CA  . LEU A  1 549 ? 37.179  -4.283  7.063   1.00 27.46 ? 566  LEU A CA  1 
ATOM   4359  C  C   . LEU A  1 549 ? 36.575  -4.740  5.740   1.00 27.27 ? 566  LEU A C   1 
ATOM   4360  O  O   . LEU A  1 549 ? 37.011  -5.741  5.181   1.00 26.50 ? 566  LEU A O   1 
ATOM   4361  C  CB  . LEU A  1 549 ? 38.650  -3.917  6.890   1.00 27.03 ? 566  LEU A CB  1 
ATOM   4362  C  CG  . LEU A  1 549 ? 38.936  -2.722  5.976   1.00 29.27 ? 566  LEU A CG  1 
ATOM   4363  C  CD1 . LEU A  1 549 ? 38.438  -1.428  6.603   1.00 30.20 ? 566  LEU A CD1 1 
ATOM   4364  C  CD2 . LEU A  1 549 ? 40.417  -2.637  5.659   1.00 30.02 ? 566  LEU A CD2 1 
ATOM   4365  N  N   . PRO A  1 550 ? 35.582  -4.011  5.180   1.00 27.25 ? 567  PRO A N   1 
ATOM   4366  C  CA  . PRO A  1 550 ? 35.117  -4.275  3.817   1.00 28.24 ? 567  PRO A CA  1 
ATOM   4367  C  C   . PRO A  1 550 ? 36.267  -4.225  2.813   1.00 28.60 ? 567  PRO A C   1 
ATOM   4368  O  O   . PRO A  1 550 ? 37.231  -3.490  3.014   1.00 27.62 ? 567  PRO A O   1 
ATOM   4369  C  CB  . PRO A  1 550 ? 34.080  -3.166  3.563   1.00 28.50 ? 567  PRO A CB  1 
ATOM   4370  C  CG  . PRO A  1 550 ? 33.621  -2.754  4.948   1.00 29.69 ? 567  PRO A CG  1 
ATOM   4371  C  CD  . PRO A  1 550 ? 34.841  -2.921  5.834   1.00 28.83 ? 567  PRO A CD  1 
ATOM   4372  N  N   . ASP A  1 551 ? 36.130  -4.985  1.719   1.00 28.18 ? 568  ASP A N   1 
ATOM   4373  C  CA  . ASP A  1 551 ? 37.153  -5.068  0.690   1.00 27.84 ? 568  ASP A CA  1 
ATOM   4374  C  C   . ASP A  1 551 ? 36.900  -4.012  -0.387  1.00 27.78 ? 568  ASP A C   1 
ATOM   4375  O  O   . ASP A  1 551 ? 36.029  -4.186  -1.242  1.00 27.11 ? 568  ASP A O   1 
ATOM   4376  C  CB  . ASP A  1 551 ? 37.225  -6.469  0.102   1.00 28.19 ? 568  ASP A CB  1 
ATOM   4377  C  CG  . ASP A  1 551 ? 38.456  -6.733  -0.753  1.00 29.02 ? 568  ASP A CG  1 
ATOM   4378  O  OD1 . ASP A  1 551 ? 39.257  -5.796  -0.907  1.00 28.17 ? 568  ASP A OD1 1 
ATOM   4379  O  OD2 . ASP A  1 551 ? 38.610  -7.870  -1.250  1.00 28.41 ? 568  ASP A OD2 1 
ATOM   4380  N  N   . VAL A  1 552 ? 37.708  -2.942  -0.360  1.00 27.49 ? 569  VAL A N   1 
ATOM   4381  C  CA  . VAL A  1 552 ? 37.553  -1.814  -1.265  1.00 27.17 ? 569  VAL A CA  1 
ATOM   4382  C  C   . VAL A  1 552 ? 38.736  -1.785  -2.233  1.00 27.75 ? 569  VAL A C   1 
ATOM   4383  O  O   . VAL A  1 552 ? 39.886  -1.858  -1.811  1.00 28.29 ? 569  VAL A O   1 
ATOM   4384  C  CB  . VAL A  1 552 ? 37.419  -0.499  -0.473  1.00 27.44 ? 569  VAL A CB  1 
ATOM   4385  C  CG1 . VAL A  1 552 ? 37.289  0.717   -1.385  1.00 27.33 ? 569  VAL A CG1 1 
ATOM   4386  C  CG2 . VAL A  1 552 ? 36.248  -0.546  0.502   1.00 27.57 ? 569  VAL A CG2 1 
ATOM   4387  N  N   . TYR A  1 553 ? 38.442  -1.657  -3.535  1.00 27.86 ? 570  TYR A N   1 
ATOM   4388  C  CA  . TYR A  1 553 ? 39.458  -1.734  -4.575  1.00 27.98 ? 570  TYR A CA  1 
ATOM   4389  C  C   . TYR A  1 553 ? 38.925  -1.115  -5.865  1.00 29.38 ? 570  TYR A C   1 
ATOM   4390  O  O   . TYR A  1 553 ? 37.718  -1.039  -6.079  1.00 28.68 ? 570  TYR A O   1 
ATOM   4391  C  CB  . TYR A  1 553 ? 39.889  -3.192  -4.781  1.00 27.53 ? 570  TYR A CB  1 
ATOM   4392  C  CG  . TYR A  1 553 ? 38.758  -4.147  -5.137  1.00 26.43 ? 570  TYR A CG  1 
ATOM   4393  C  CD1 . TYR A  1 553 ? 38.020  -4.776  -4.143  1.00 26.24 ? 570  TYR A CD1 1 
ATOM   4394  C  CD2 . TYR A  1 553 ? 38.424  -4.417  -6.461  1.00 26.68 ? 570  TYR A CD2 1 
ATOM   4395  C  CE1 . TYR A  1 553 ? 36.988  -5.646  -4.453  1.00 26.21 ? 570  TYR A CE1 1 
ATOM   4396  C  CE2 . TYR A  1 553 ? 37.392  -5.285  -6.786  1.00 26.43 ? 570  TYR A CE2 1 
ATOM   4397  C  CZ  . TYR A  1 553 ? 36.667  -5.896  -5.776  1.00 26.17 ? 570  TYR A CZ  1 
ATOM   4398  O  OH  . TYR A  1 553 ? 35.648  -6.754  -6.061  1.00 25.71 ? 570  TYR A OH  1 
ATOM   4399  N  N   . GLU A  1 554 ? 39.845  -0.680  -6.733  1.00 32.73 ? 571  GLU A N   1 
ATOM   4400  C  CA  . GLU A  1 554 ? 39.478  -0.007  -7.968  1.00 35.38 ? 571  GLU A CA  1 
ATOM   4401  C  C   . GLU A  1 554 ? 39.220  -1.035  -9.068  1.00 34.08 ? 571  GLU A C   1 
ATOM   4402  O  O   . GLU A  1 554 ? 39.853  -2.086  -9.099  1.00 33.83 ? 571  GLU A O   1 
ATOM   4403  C  CB  . GLU A  1 554 ? 40.580  0.967   -8.384  1.00 40.50 ? 571  GLU A CB  1 
ATOM   4404  C  CG  . GLU A  1 554 ? 40.721  2.150   -7.431  1.00 44.85 ? 571  GLU A CG  1 
ATOM   4405  C  CD  . GLU A  1 554 ? 41.573  3.279   -7.980  1.00 50.61 ? 571  GLU A CD  1 
ATOM   4406  O  OE1 . GLU A  1 554 ? 42.766  3.040   -8.262  1.00 55.13 ? 571  GLU A OE1 1 
ATOM   4407  O  OE2 . GLU A  1 554 ? 41.036  4.395   -8.133  1.00 54.78 ? 571  GLU A OE2 1 
ATOM   4408  N  N   . TRP A  1 555 ? 38.273  -0.717  -9.957  1.00 33.62 ? 572  TRP A N   1 
ATOM   4409  C  CA  . TRP A  1 555 ? 38.037  -1.490  -11.166 1.00 35.19 ? 572  TRP A CA  1 
ATOM   4410  C  C   . TRP A  1 555 ? 38.896  -0.937  -12.301 1.00 38.80 ? 572  TRP A C   1 
ATOM   4411  O  O   . TRP A  1 555 ? 39.178  0.258   -12.335 1.00 38.38 ? 572  TRP A O   1 
ATOM   4412  C  CB  . TRP A  1 555 ? 36.552  -1.456  -11.561 1.00 32.60 ? 572  TRP A CB  1 
ATOM   4413  C  CG  . TRP A  1 555 ? 35.693  -2.541  -10.967 1.00 30.99 ? 572  TRP A CG  1 
ATOM   4414  C  CD1 . TRP A  1 555 ? 36.071  -3.602  -10.193 1.00 30.85 ? 572  TRP A CD1 1 
ATOM   4415  C  CD2 . TRP A  1 555 ? 34.273  -2.686  -11.172 1.00 31.22 ? 572  TRP A CD2 1 
ATOM   4416  N  NE1 . TRP A  1 555 ? 34.987  -4.381  -9.887  1.00 30.42 ? 572  TRP A NE1 1 
ATOM   4417  C  CE2 . TRP A  1 555 ? 33.871  -3.846  -10.475 1.00 31.00 ? 572  TRP A CE2 1 
ATOM   4418  C  CE3 . TRP A  1 555 ? 33.309  -1.942  -11.863 1.00 31.46 ? 572  TRP A CE3 1 
ATOM   4419  C  CZ2 . TRP A  1 555 ? 32.547  -4.276  -10.458 1.00 31.40 ? 572  TRP A CZ2 1 
ATOM   4420  C  CZ3 . TRP A  1 555 ? 31.999  -2.367  -11.839 1.00 32.23 ? 572  TRP A CZ3 1 
ATOM   4421  C  CH2 . TRP A  1 555 ? 31.626  -3.518  -11.146 1.00 32.42 ? 572  TRP A CH2 1 
ATOM   4422  N  N   . PRO A  1 556 ? 39.331  -1.771  -13.274 1.00 43.01 ? 573  PRO A N   1 
ATOM   4423  C  CA  . PRO A  1 556 ? 39.987  -1.260  -14.479 1.00 45.83 ? 573  PRO A CA  1 
ATOM   4424  C  C   . PRO A  1 556 ? 39.042  -0.367  -15.283 1.00 49.75 ? 573  PRO A C   1 
ATOM   4425  O  O   . PRO A  1 556 ? 37.857  -0.669  -15.409 1.00 49.27 ? 573  PRO A O   1 
ATOM   4426  C  CB  . PRO A  1 556 ? 40.390  -2.528  -15.259 1.00 45.76 ? 573  PRO A CB  1 
ATOM   4427  C  CG  . PRO A  1 556 ? 40.322  -3.647  -14.239 1.00 45.43 ? 573  PRO A CG  1 
ATOM   4428  C  CD  . PRO A  1 556 ? 39.230  -3.239  -13.267 1.00 44.46 ? 573  PRO A CD  1 
ATOM   4429  N  N   . GLU A  1 557 ? 39.581  0.738   -15.815 1.00 54.86 ? 574  GLU A N   1 
ATOM   4430  C  CA  . GLU A  1 557 ? 38.829  1.649   -16.665 1.00 57.84 ? 574  GLU A CA  1 
ATOM   4431  C  C   . GLU A  1 557 ? 39.267  1.450   -18.126 1.00 60.49 ? 574  GLU A C   1 
ATOM   4432  O  O   . GLU A  1 557 ? 40.480  1.210   -18.327 1.00 62.89 ? 574  GLU A O   1 
ATOM   4433  C  CB  . GLU A  1 557 ? 39.041  3.101   -16.231 1.00 57.70 ? 574  GLU A CB  1 
ATOM   4434  N  N   . SER A  1 561 ? 31.184  3.401   -22.624 1.00 68.41 ? 578  SER A N   1 
ATOM   4435  C  CA  . SER A  1 561 ? 29.790  3.228   -22.133 1.00 66.91 ? 578  SER A CA  1 
ATOM   4436  C  C   . SER A  1 561 ? 28.805  3.856   -23.120 1.00 65.31 ? 578  SER A C   1 
ATOM   4437  O  O   . SER A  1 561 ? 28.788  5.073   -23.284 1.00 65.02 ? 578  SER A O   1 
ATOM   4438  C  CB  . SER A  1 561 ? 29.627  3.790   -20.740 1.00 67.01 ? 578  SER A CB  1 
ATOM   4439  O  OG  . SER A  1 561 ? 30.425  4.952   -20.558 1.00 69.21 ? 578  SER A OG  1 
ATOM   4440  N  N   . PRO A  1 562 ? 27.962  3.051   -23.812 1.00 63.08 ? 579  PRO A N   1 
ATOM   4441  C  CA  . PRO A  1 562 ? 27.018  3.583   -24.800 1.00 63.53 ? 579  PRO A CA  1 
ATOM   4442  C  C   . PRO A  1 562 ? 25.986  4.533   -24.195 1.00 65.28 ? 579  PRO A C   1 
ATOM   4443  O  O   . PRO A  1 562 ? 25.453  4.260   -23.122 1.00 65.15 ? 579  PRO A O   1 
ATOM   4444  C  CB  . PRO A  1 562 ? 26.362  2.315   -25.381 1.00 62.76 ? 579  PRO A CB  1 
ATOM   4445  C  CG  . PRO A  1 562 ? 26.511  1.285   -24.284 1.00 61.48 ? 579  PRO A CG  1 
ATOM   4446  C  CD  . PRO A  1 562 ? 27.869  1.587   -23.681 1.00 62.10 ? 579  PRO A CD  1 
ATOM   4447  N  N   . PRO A  1 563 ? 25.683  5.680   -24.851 1.00 67.94 ? 580  PRO A N   1 
ATOM   4448  C  CA  . PRO A  1 563 ? 24.638  6.592   -24.385 1.00 68.19 ? 580  PRO A CA  1 
ATOM   4449  C  C   . PRO A  1 563 ? 23.305  6.394   -25.101 1.00 64.56 ? 580  PRO A C   1 
ATOM   4450  O  O   . PRO A  1 563 ? 22.295  6.942   -24.613 1.00 63.65 ? 580  PRO A O   1 
ATOM   4451  C  CB  . PRO A  1 563 ? 25.300  7.941   -24.718 1.00 69.68 ? 580  PRO A CB  1 
ATOM   4452  C  CG  . PRO A  1 563 ? 26.032  7.684   -26.027 1.00 70.16 ? 580  PRO A CG  1 
ATOM   4453  C  CD  . PRO A  1 563 ? 26.358  6.193   -26.054 1.00 69.96 ? 580  PRO A CD  1 
ATOM   4454  N  N   . GLU B  1 6   ? 23.307  -9.184  16.929  1.00 51.23 ? 23   GLU B N   1 
ATOM   4455  C  CA  . GLU B  1 6   ? 23.337  -10.029 18.154  1.00 50.22 ? 23   GLU B CA  1 
ATOM   4456  C  C   . GLU B  1 6   ? 22.178  -11.024 18.109  1.00 53.60 ? 23   GLU B C   1 
ATOM   4457  O  O   . GLU B  1 6   ? 21.016  -10.624 18.122  1.00 54.35 ? 23   GLU B O   1 
ATOM   4458  C  CB  . GLU B  1 6   ? 23.268  -9.161  19.413  1.00 46.74 ? 23   GLU B CB  1 
ATOM   4459  C  CG  . GLU B  1 6   ? 23.531  -9.940  20.700  1.00 45.57 ? 23   GLU B CG  1 
ATOM   4460  C  CD  . GLU B  1 6   ? 23.589  -9.104  21.970  1.00 44.50 ? 23   GLU B CD  1 
ATOM   4461  O  OE1 . GLU B  1 6   ? 23.212  -7.914  21.932  1.00 45.72 ? 23   GLU B OE1 1 
ATOM   4462  O  OE2 . GLU B  1 6   ? 24.032  -9.645  23.004  1.00 42.31 ? 23   GLU B OE2 1 
ATOM   4463  N  N   . LYS B  1 7   ? 22.505  -12.321 18.065  1.00 55.80 ? 24   LYS B N   1 
ATOM   4464  C  CA  . LYS B  1 7   ? 21.495  -13.360 17.939  1.00 55.69 ? 24   LYS B CA  1 
ATOM   4465  C  C   . LYS B  1 7   ? 20.736  -13.489 19.258  1.00 54.25 ? 24   LYS B C   1 
ATOM   4466  O  O   . LYS B  1 7   ? 21.346  -13.545 20.326  1.00 51.05 ? 24   LYS B O   1 
ATOM   4467  C  CB  . LYS B  1 7   ? 22.116  -14.701 17.531  1.00 57.43 ? 24   LYS B CB  1 
ATOM   4468  C  CG  . LYS B  1 7   ? 22.851  -14.695 16.195  1.00 58.84 ? 24   LYS B CG  1 
ATOM   4469  C  CD  . LYS B  1 7   ? 23.320  -16.073 15.741  1.00 59.72 ? 24   LYS B CD  1 
ATOM   4470  C  CE  . LYS B  1 7   ? 22.217  -16.923 15.191  1.00 61.80 ? 24   LYS B CE  1 
ATOM   4471  N  NZ  . LYS B  1 7   ? 21.795  -16.494 13.855  1.00 63.25 ? 24   LYS B NZ  1 
ATOM   4472  N  N   . GLY B  1 8   ? 19.400  -13.540 19.156  1.00 50.91 ? 25   GLY B N   1 
ATOM   4473  C  CA  . GLY B  1 8   ? 18.517  -13.609 20.309  1.00 49.88 ? 25   GLY B CA  1 
ATOM   4474  C  C   . GLY B  1 8   ? 17.213  -12.858 20.045  1.00 50.58 ? 25   GLY B C   1 
ATOM   4475  O  O   . GLY B  1 8   ? 16.934  -12.487 18.906  1.00 52.06 ? 25   GLY B O   1 
ATOM   4476  N  N   . LYS B  1 9   ? 16.422  -12.641 21.106  1.00 48.13 ? 26   LYS B N   1 
ATOM   4477  C  CA  . LYS B  1 9   ? 15.177  -11.894 20.996  1.00 47.26 ? 26   LYS B CA  1 
ATOM   4478  C  C   . LYS B  1 9   ? 15.442  -10.429 21.326  1.00 44.31 ? 26   LYS B C   1 
ATOM   4479  O  O   . LYS B  1 9   ? 15.845  -10.108 22.441  1.00 41.00 ? 26   LYS B O   1 
ATOM   4480  C  CB  . LYS B  1 9   ? 14.066  -12.469 21.881  1.00 49.17 ? 26   LYS B CB  1 
ATOM   4481  C  CG  . LYS B  1 9   ? 13.287  -13.611 21.247  1.00 51.56 ? 26   LYS B CG  1 
ATOM   4482  C  CD  . LYS B  1 9   ? 14.114  -14.861 20.973  1.00 54.80 ? 26   LYS B CD  1 
ATOM   4483  C  CE  . LYS B  1 9   ? 13.323  -15.929 20.284  1.00 56.21 ? 26   LYS B CE  1 
ATOM   4484  N  NZ  . LYS B  1 9   ? 14.019  -17.215 20.337  1.00 57.40 ? 26   LYS B NZ  1 
ATOM   4485  N  N   . PRO B  1 10  ? 15.232  -9.502  20.361  1.00 43.53 ? 27   PRO B N   1 
ATOM   4486  C  CA  . PRO B  1 10  ? 15.501  -8.077  20.581  1.00 43.04 ? 27   PRO B CA  1 
ATOM   4487  C  C   . PRO B  1 10  ? 14.977  -7.475  21.886  1.00 40.02 ? 27   PRO B C   1 
ATOM   4488  O  O   . PRO B  1 10  ? 15.630  -6.621  22.474  1.00 38.48 ? 27   PRO B O   1 
ATOM   4489  C  CB  . PRO B  1 10  ? 14.829  -7.434  19.352  1.00 44.18 ? 27   PRO B CB  1 
ATOM   4490  C  CG  . PRO B  1 10  ? 14.946  -8.476  18.265  1.00 44.56 ? 27   PRO B CG  1 
ATOM   4491  C  CD  . PRO B  1 10  ? 14.769  -9.792  18.993  1.00 43.43 ? 27   PRO B CD  1 
ATOM   4492  N  N   . LEU B  1 11  ? 13.799  -7.925  22.338  1.00 40.14 ? 28   LEU B N   1 
ATOM   4493  C  CA  . LEU B  1 11  ? 13.139  -7.306  23.478  1.00 37.63 ? 28   LEU B CA  1 
ATOM   4494  C  C   . LEU B  1 11  ? 13.917  -7.552  24.772  1.00 34.52 ? 28   LEU B C   1 
ATOM   4495  O  O   . LEU B  1 11  ? 13.883  -6.689  25.644  1.00 34.40 ? 28   LEU B O   1 
ATOM   4496  C  CB  . LEU B  1 11  ? 11.676  -7.736  23.605  1.00 38.86 ? 28   LEU B CB  1 
ATOM   4497  C  CG  . LEU B  1 11  ? 10.718  -7.195  22.537  1.00 39.54 ? 28   LEU B CG  1 
ATOM   4498  C  CD1 . LEU B  1 11  ? 9.306   -7.697  22.788  1.00 40.04 ? 28   LEU B CD1 1 
ATOM   4499  C  CD2 . LEU B  1 11  ? 10.722  -5.676  22.459  1.00 40.12 ? 28   LEU B CD2 1 
ATOM   4500  N  N   . MET B  1 12  ? 14.627  -8.686  24.909  1.00 32.09 ? 29   MET B N   1 
ATOM   4501  C  CA  . MET B  1 12  ? 15.414  -8.910  26.119  1.00 30.88 ? 29   MET B CA  1 
ATOM   4502  C  C   . MET B  1 12  ? 16.844  -8.388  25.946  1.00 28.37 ? 29   MET B C   1 
ATOM   4503  O  O   . MET B  1 12  ? 17.495  -8.062  26.935  1.00 27.74 ? 29   MET B O   1 
ATOM   4504  C  CB  . MET B  1 12  ? 15.367  -10.371 26.606  1.00 31.96 ? 29   MET B CB  1 
ATOM   4505  C  CG  . MET B  1 12  ? 16.259  -11.374 25.892  1.00 33.14 ? 29   MET B CG  1 
ATOM   4506  S  SD  . MET B  1 12  ? 15.990  -13.071 26.465  1.00 33.66 ? 29   MET B SD  1 
ATOM   4507  C  CE  . MET B  1 12  ? 16.524  -13.010 28.177  1.00 29.27 ? 29   MET B CE  1 
ATOM   4508  N  N   . LEU B  1 13  ? 17.319  -8.259  24.699  1.00 29.11 ? 30   LEU B N   1 
ATOM   4509  C  CA  . LEU B  1 13  ? 18.681  -7.808  24.436  1.00 29.44 ? 30   LEU B CA  1 
ATOM   4510  C  C   . LEU B  1 13  ? 18.785  -6.287  24.562  1.00 28.83 ? 30   LEU B C   1 
ATOM   4511  O  O   . LEU B  1 13  ? 19.854  -5.756  24.860  1.00 28.83 ? 30   LEU B O   1 
ATOM   4512  C  CB  . LEU B  1 13  ? 19.101  -8.273  23.042  1.00 30.65 ? 30   LEU B CB  1 
ATOM   4513  C  CG  . LEU B  1 13  ? 19.189  -9.791  22.838  1.00 31.96 ? 30   LEU B CG  1 
ATOM   4514  C  CD1 . LEU B  1 13  ? 19.518  -10.093 21.389  1.00 33.42 ? 30   LEU B CD1 1 
ATOM   4515  C  CD2 . LEU B  1 13  ? 20.206  -10.436 23.760  1.00 31.88 ? 30   LEU B CD2 1 
ATOM   4516  N  N   . ASN B  1 14  ? 17.674  -5.594  24.301  1.00 27.56 ? 31   ASN B N   1 
ATOM   4517  C  CA  . ASN B  1 14  ? 17.644  -4.141  24.314  1.00 27.56 ? 31   ASN B CA  1 
ATOM   4518  C  C   . ASN B  1 14  ? 17.383  -3.670  25.742  1.00 25.99 ? 31   ASN B C   1 
ATOM   4519  O  O   . ASN B  1 14  ? 16.295  -3.881  26.273  1.00 24.26 ? 31   ASN B O   1 
ATOM   4520  C  CB  . ASN B  1 14  ? 16.603  -3.619  23.330  1.00 27.90 ? 31   ASN B CB  1 
ATOM   4521  C  CG  . ASN B  1 14  ? 16.550  -2.110  23.247  1.00 28.53 ? 31   ASN B CG  1 
ATOM   4522  O  OD1 . ASN B  1 14  ? 17.260  -1.407  23.973  1.00 28.28 ? 31   ASN B OD1 1 
ATOM   4523  N  ND2 . ASN B  1 14  ? 15.713  -1.595  22.360  1.00 30.26 ? 31   ASN B ND2 1 
ATOM   4524  N  N   . PRO B  1 15  ? 18.344  -2.983  26.400  1.00 25.92 ? 32   PRO B N   1 
ATOM   4525  C  CA  . PRO B  1 15  ? 18.139  -2.515  27.773  1.00 25.14 ? 32   PRO B CA  1 
ATOM   4526  C  C   . PRO B  1 15  ? 16.941  -1.580  27.938  1.00 26.11 ? 32   PRO B C   1 
ATOM   4527  O  O   . PRO B  1 15  ? 16.419  -1.426  29.044  1.00 24.88 ? 32   PRO B O   1 
ATOM   4528  C  CB  . PRO B  1 15  ? 19.460  -1.837  28.163  1.00 25.91 ? 32   PRO B CB  1 
ATOM   4529  C  CG  . PRO B  1 15  ? 20.200  -1.620  26.859  1.00 26.83 ? 32   PRO B CG  1 
ATOM   4530  C  CD  . PRO B  1 15  ? 19.672  -2.639  25.868  1.00 26.69 ? 32   PRO B CD  1 
ATOM   4531  N  N   . ARG B  1 16  ? 16.507  -0.969  26.829  1.00 26.80 ? 33   ARG B N   1 
ATOM   4532  C  CA  . ARG B  1 16  ? 15.388  -0.043  26.843  1.00 28.40 ? 33   ARG B CA  1 
ATOM   4533  C  C   . ARG B  1 16  ? 14.074  -0.781  27.091  1.00 26.95 ? 33   ARG B C   1 
ATOM   4534  O  O   . ARG B  1 16  ? 13.187  -0.233  27.739  1.00 27.89 ? 33   ARG B O   1 
ATOM   4535  C  CB  . ARG B  1 16  ? 15.387  0.721   25.516  1.00 32.16 ? 33   ARG B CB  1 
ATOM   4536  C  CG  . ARG B  1 16  ? 14.565  1.999   25.494  1.00 34.65 ? 33   ARG B CG  1 
ATOM   4537  C  CD  . ARG B  1 16  ? 15.360  3.093   24.782  1.00 37.24 ? 33   ARG B CD  1 
ATOM   4538  N  NE  . ARG B  1 16  ? 16.451  3.589   25.633  1.00 38.45 ? 33   ARG B NE  1 
ATOM   4539  C  CZ  . ARG B  1 16  ? 17.494  4.331   25.253  1.00 38.15 ? 33   ARG B CZ  1 
ATOM   4540  N  NH1 . ARG B  1 16  ? 17.749  4.538   23.973  1.00 40.38 ? 33   ARG B NH1 1 
ATOM   4541  N  NH2 . ARG B  1 16  ? 18.309  4.838   26.160  1.00 36.58 ? 33   ARG B NH2 1 
ATOM   4542  N  N   . THR B  1 17  ? 13.948  -2.008  26.563  1.00 25.55 ? 34   THR B N   1 
ATOM   4543  C  CA  . THR B  1 17  ? 12.722  -2.784  26.691  1.00 25.26 ? 34   THR B CA  1 
ATOM   4544  C  C   . THR B  1 17  ? 12.885  -3.917  27.708  1.00 24.38 ? 34   THR B C   1 
ATOM   4545  O  O   . THR B  1 17  ? 11.890  -4.384  28.257  1.00 23.83 ? 34   THR B O   1 
ATOM   4546  C  CB  . THR B  1 17  ? 12.269  -3.328  25.332  1.00 25.36 ? 34   THR B CB  1 
ATOM   4547  O  OG1 . THR B  1 17  ? 13.360  -3.990  24.704  1.00 24.85 ? 34   THR B OG1 1 
ATOM   4548  C  CG2 . THR B  1 17  ? 11.768  -2.243  24.398  1.00 26.71 ? 34   THR B CG2 1 
ATOM   4549  N  N   . ASN B  1 18  ? 14.123  -4.357  27.963  1.00 22.41 ? 35   ASN B N   1 
ATOM   4550  C  CA  . ASN B  1 18  ? 14.379  -5.540  28.772  1.00 22.65 ? 35   ASN B CA  1 
ATOM   4551  C  C   . ASN B  1 18  ? 13.801  -5.395  30.184  1.00 23.62 ? 35   ASN B C   1 
ATOM   4552  O  O   . ASN B  1 18  ? 14.075  -4.419  30.887  1.00 23.78 ? 35   ASN B O   1 
ATOM   4553  C  CB  . ASN B  1 18  ? 15.873  -5.838  28.833  1.00 22.87 ? 35   ASN B CB  1 
ATOM   4554  C  CG  . ASN B  1 18  ? 16.181  -7.069  29.652  1.00 22.83 ? 35   ASN B CG  1 
ATOM   4555  O  OD1 . ASN B  1 18  ? 15.439  -8.057  29.589  1.00 23.05 ? 35   ASN B OD1 1 
ATOM   4556  N  ND2 . ASN B  1 18  ? 17.251  -7.026  30.432  1.00 22.23 ? 35   ASN B ND2 1 
ATOM   4557  N  N   . LYS B  1 19  ? 13.024  -6.407  30.600  1.00 22.76 ? 36   LYS B N   1 
ATOM   4558  C  CA  . LYS B  1 19  ? 12.450  -6.483  31.937  1.00 22.14 ? 36   LYS B CA  1 
ATOM   4559  C  C   . LYS B  1 19  ? 13.118  -7.571  32.783  1.00 21.36 ? 36   LYS B C   1 
ATOM   4560  O  O   . LYS B  1 19  ? 12.843  -7.679  33.981  1.00 21.62 ? 36   LYS B O   1 
ATOM   4561  C  CB  . LYS B  1 19  ? 10.947  -6.751  31.794  1.00 22.75 ? 36   LYS B CB  1 
ATOM   4562  C  CG  . LYS B  1 19  ? 10.165  -5.618  31.153  1.00 23.44 ? 36   LYS B CG  1 
ATOM   4563  C  CD  . LYS B  1 19  ? 8.740   -5.964  30.734  1.00 25.31 ? 36   LYS B CD  1 
ATOM   4564  C  CE  . LYS B  1 19  ? 7.840   -6.340  31.852  1.00 26.15 ? 36   LYS B CE  1 
ATOM   4565  N  NZ  . LYS B  1 19  ? 6.441   -6.418  31.404  1.00 26.34 ? 36   LYS B NZ  1 
ATOM   4566  N  N   . GLY B  1 20  ? 13.991  -8.379  32.170  1.00 21.25 ? 37   GLY B N   1 
ATOM   4567  C  CA  . GLY B  1 20  ? 14.656  -9.468  32.873  1.00 20.88 ? 37   GLY B CA  1 
ATOM   4568  C  C   . GLY B  1 20  ? 13.646  -10.442 33.481  1.00 20.50 ? 37   GLY B C   1 
ATOM   4569  O  O   . GLY B  1 20  ? 12.697  -10.850 32.819  1.00 18.96 ? 37   GLY B O   1 
ATOM   4570  N  N   . MET B  1 21  ? 13.830  -10.774 34.764  1.00 21.98 ? 38   MET B N   1 
ATOM   4571  C  CA  . MET B  1 21  ? 12.975  -11.741 35.434  1.00 24.00 ? 38   MET B CA  1 
ATOM   4572  C  C   . MET B  1 21  ? 11.581  -11.176 35.721  1.00 24.04 ? 38   MET B C   1 
ATOM   4573  O  O   . MET B  1 21  ? 10.729  -11.905 36.217  1.00 23.86 ? 38   MET B O   1 
ATOM   4574  C  CB  . MET B  1 21  ? 13.617  -12.239 36.729  1.00 26.32 ? 38   MET B CB  1 
ATOM   4575  C  CG  . MET B  1 21  ? 14.688  -13.280 36.489  1.00 28.76 ? 38   MET B CG  1 
ATOM   4576  S  SD  . MET B  1 21  ? 15.258  -13.997 38.036  1.00 35.87 ? 38   MET B SD  1 
ATOM   4577  C  CE  . MET B  1 21  ? 16.080  -12.612 38.837  1.00 37.93 ? 38   MET B CE  1 
ATOM   4578  N  N   . ALA B  1 22  ? 11.335  -9.903  35.380  1.00 23.26 ? 39   ALA B N   1 
ATOM   4579  C  CA  . ALA B  1 22  ? 10.004  -9.324  35.493  1.00 22.46 ? 39   ALA B CA  1 
ATOM   4580  C  C   . ALA B  1 22  ? 9.149   -9.567  34.245  1.00 21.75 ? 39   ALA B C   1 
ATOM   4581  O  O   . ALA B  1 22  ? 7.963   -9.231  34.246  1.00 20.77 ? 39   ALA B O   1 
ATOM   4582  C  CB  . ALA B  1 22  ? 10.119  -7.851  35.805  1.00 23.00 ? 39   ALA B CB  1 
ATOM   4583  N  N   . PHE B  1 23  ? 9.721   -10.138 33.178  1.00 20.52 ? 40   PHE B N   1 
ATOM   4584  C  CA  . PHE B  1 23  ? 8.902   -10.652 32.086  1.00 21.15 ? 40   PHE B CA  1 
ATOM   4585  C  C   . PHE B  1 23  ? 7.943   -11.698 32.654  1.00 20.92 ? 40   PHE B C   1 
ATOM   4586  O  O   . PHE B  1 23  ? 8.375   -12.616 33.351  1.00 19.61 ? 40   PHE B O   1 
ATOM   4587  C  CB  . PHE B  1 23  ? 9.681   -11.295 30.931  1.00 21.18 ? 40   PHE B CB  1 
ATOM   4588  C  CG  . PHE B  1 23  ? 10.300  -10.325 29.936  1.00 21.77 ? 40   PHE B CG  1 
ATOM   4589  C  CD1 . PHE B  1 23  ? 9.495   -9.566  29.089  1.00 22.67 ? 40   PHE B CD1 1 
ATOM   4590  C  CD2 . PHE B  1 23  ? 11.684  -10.202 29.817  1.00 21.45 ? 40   PHE B CD2 1 
ATOM   4591  C  CE1 . PHE B  1 23  ? 10.061  -8.686  28.171  1.00 22.91 ? 40   PHE B CE1 1 
ATOM   4592  C  CE2 . PHE B  1 23  ? 12.243  -9.327  28.894  1.00 21.65 ? 40   PHE B CE2 1 
ATOM   4593  C  CZ  . PHE B  1 23  ? 11.431  -8.568  28.079  1.00 22.37 ? 40   PHE B CZ  1 
ATOM   4594  N  N   . THR B  1 24  ? 6.642   -11.543 32.373  1.00 20.67 ? 41   THR B N   1 
ATOM   4595  C  CA  . THR B  1 24  ? 5.638   -12.449 32.911  1.00 21.84 ? 41   THR B CA  1 
ATOM   4596  C  C   . THR B  1 24  ? 5.719   -13.774 32.162  1.00 21.50 ? 41   THR B C   1 
ATOM   4597  O  O   . THR B  1 24  ? 6.292   -13.849 31.073  1.00 20.29 ? 41   THR B O   1 
ATOM   4598  C  CB  . THR B  1 24  ? 4.226   -11.864 32.811  1.00 22.76 ? 41   THR B CB  1 
ATOM   4599  O  OG1 . THR B  1 24  ? 3.896   -11.813 31.427  1.00 22.67 ? 41   THR B OG1 1 
ATOM   4600  C  CG2 . THR B  1 24  ? 4.098   -10.494 33.448  1.00 23.69 ? 41   THR B CG2 1 
ATOM   4601  N  N   . LEU B  1 25  ? 5.104   -14.812 32.739  1.00 22.12 ? 42   LEU B N   1 
ATOM   4602  C  CA  . LEU B  1 25  ? 5.093   -16.123 32.108  1.00 22.90 ? 42   LEU B CA  1 
ATOM   4603  C  C   . LEU B  1 25  ? 4.556   -16.010 30.683  1.00 22.75 ? 42   LEU B C   1 
ATOM   4604  O  O   . LEU B  1 25  ? 5.164   -16.536 29.754  1.00 21.86 ? 42   LEU B O   1 
ATOM   4605  C  CB  . LEU B  1 25  ? 4.291   -17.141 32.917  1.00 23.58 ? 42   LEU B CB  1 
ATOM   4606  C  CG  . LEU B  1 25  ? 4.236   -18.557 32.331  1.00 24.01 ? 42   LEU B CG  1 
ATOM   4607  C  CD1 . LEU B  1 25  ? 5.612   -19.212 32.286  1.00 23.72 ? 42   LEU B CD1 1 
ATOM   4608  C  CD2 . LEU B  1 25  ? 3.261   -19.404 33.133  1.00 25.03 ? 42   LEU B CD2 1 
ATOM   4609  N  N   . GLN B  1 26  ? 3.409   -15.337 30.517  1.00 23.88 ? 43   GLN B N   1 
ATOM   4610  C  CA  . GLN B  1 26  ? 2.766   -15.250 29.214  1.00 24.58 ? 43   GLN B CA  1 
ATOM   4611  C  C   . GLN B  1 26  ? 3.628   -14.448 28.241  1.00 22.40 ? 43   GLN B C   1 
ATOM   4612  O  O   . GLN B  1 26  ? 3.705   -14.791 27.061  1.00 22.68 ? 43   GLN B O   1 
ATOM   4613  C  CB  . GLN B  1 26  ? 1.368   -14.632 29.267  1.00 28.38 ? 43   GLN B CB  1 
ATOM   4614  C  CG  . GLN B  1 26  ? 0.294   -15.563 29.816  1.00 32.22 ? 43   GLN B CG  1 
ATOM   4615  C  CD  . GLN B  1 26  ? -0.988  -15.519 29.010  1.00 36.65 ? 43   GLN B CD  1 
ATOM   4616  O  OE1 . GLN B  1 26  ? -1.491  -14.448 28.654  1.00 37.84 ? 43   GLN B OE1 1 
ATOM   4617  N  NE2 . GLN B  1 26  ? -1.513  -16.692 28.677  1.00 38.69 ? 43   GLN B NE2 1 
ATOM   4618  N  N   . GLU B  1 27  ? 4.255   -13.372 28.729  1.00 21.60 ? 44   GLU B N   1 
ATOM   4619  C  CA  . GLU B  1 27  ? 5.163   -12.586 27.908  1.00 22.27 ? 44   GLU B CA  1 
ATOM   4620  C  C   . GLU B  1 27  ? 6.288   -13.477 27.379  1.00 21.11 ? 44   GLU B C   1 
ATOM   4621  O  O   . GLU B  1 27  ? 6.586   -13.466 26.188  1.00 21.74 ? 44   GLU B O   1 
ATOM   4622  C  CB  . GLU B  1 27  ? 5.754   -11.411 28.689  1.00 22.99 ? 44   GLU B CB  1 
ATOM   4623  C  CG  . GLU B  1 27  ? 4.809   -10.217 28.803  1.00 23.34 ? 44   GLU B CG  1 
ATOM   4624  C  CD  . GLU B  1 27  ? 5.272   -9.101  29.727  1.00 23.15 ? 44   GLU B CD  1 
ATOM   4625  O  OE1 . GLU B  1 27  ? 6.228   -9.276  30.521  1.00 22.99 ? 44   GLU B OE1 1 
ATOM   4626  O  OE2 . GLU B  1 27  ? 4.662   -8.020  29.630  1.00 22.68 ? 44   GLU B OE2 1 
ATOM   4627  N  N   . ARG B  1 28  ? 6.902   -14.260 28.270  1.00 20.96 ? 45   ARG B N   1 
ATOM   4628  C  CA  . ARG B  1 28  ? 8.064   -15.053 27.902  1.00 20.90 ? 45   ARG B CA  1 
ATOM   4629  C  C   . ARG B  1 28  ? 7.697   -16.044 26.800  1.00 21.81 ? 45   ARG B C   1 
ATOM   4630  O  O   . ARG B  1 28  ? 8.452   -16.225 25.848  1.00 22.78 ? 45   ARG B O   1 
ATOM   4631  C  CB  . ARG B  1 28  ? 8.641   -15.784 29.116  1.00 20.28 ? 45   ARG B CB  1 
ATOM   4632  C  CG  . ARG B  1 28  ? 9.198   -14.892 30.209  1.00 20.35 ? 45   ARG B CG  1 
ATOM   4633  C  CD  . ARG B  1 28  ? 9.595   -15.751 31.396  1.00 20.58 ? 45   ARG B CD  1 
ATOM   4634  N  NE  . ARG B  1 28  ? 9.990   -14.914 32.528  1.00 20.87 ? 45   ARG B NE  1 
ATOM   4635  C  CZ  . ARG B  1 28  ? 10.681  -15.315 33.587  1.00 21.72 ? 45   ARG B CZ  1 
ATOM   4636  N  NH1 . ARG B  1 28  ? 11.116  -16.561 33.679  1.00 21.67 ? 45   ARG B NH1 1 
ATOM   4637  N  NH2 . ARG B  1 28  ? 10.940  -14.449 34.551  1.00 21.99 ? 45   ARG B NH2 1 
ATOM   4638  N  N   . GLN B  1 29  ? 6.524   -16.673 26.941  1.00 22.44 ? 46   GLN B N   1 
ATOM   4639  C  CA  . GLN B  1 29  ? 6.091   -17.727 26.039  1.00 23.07 ? 46   GLN B CA  1 
ATOM   4640  C  C   . GLN B  1 29  ? 5.784   -17.139 24.665  1.00 22.93 ? 46   GLN B C   1 
ATOM   4641  O  O   . GLN B  1 29  ? 6.262   -17.648 23.654  1.00 22.17 ? 46   GLN B O   1 
ATOM   4642  C  CB  . GLN B  1 29  ? 4.897   -18.470 26.644  1.00 23.51 ? 46   GLN B CB  1 
ATOM   4643  C  CG  . GLN B  1 29  ? 5.261   -19.319 27.858  1.00 24.36 ? 46   GLN B CG  1 
ATOM   4644  C  CD  . GLN B  1 29  ? 4.072   -19.987 28.516  1.00 26.40 ? 46   GLN B CD  1 
ATOM   4645  O  OE1 . GLN B  1 29  ? 2.909   -19.669 28.234  1.00 26.34 ? 46   GLN B OE1 1 
ATOM   4646  N  NE2 . GLN B  1 29  ? 4.354   -20.926 29.410  1.00 26.59 ? 46   GLN B NE2 1 
ATOM   4647  N  N   . MET B  1 30  ? 5.010   -16.046 24.633  1.00 24.07 ? 47   MET B N   1 
ATOM   4648  C  CA  . MET B  1 30  ? 4.570   -15.473 23.371  1.00 24.25 ? 47   MET B CA  1 
ATOM   4649  C  C   . MET B  1 30  ? 5.727   -14.803 22.633  1.00 24.16 ? 47   MET B C   1 
ATOM   4650  O  O   . MET B  1 30  ? 5.710   -14.752 21.408  1.00 26.54 ? 47   MET B O   1 
ATOM   4651  C  CB  . MET B  1 30  ? 3.444   -14.452 23.575  1.00 24.88 ? 47   MET B CB  1 
ATOM   4652  C  CG  . MET B  1 30  ? 2.130   -15.067 23.980  1.00 25.55 ? 47   MET B CG  1 
ATOM   4653  S  SD  . MET B  1 30  ? 0.789   -13.865 23.873  1.00 28.78 ? 47   MET B SD  1 
ATOM   4654  C  CE  . MET B  1 30  ? -0.519  -14.731 24.746  1.00 28.59 ? 47   MET B CE  1 
ATOM   4655  N  N   . LEU B  1 31  ? 6.719   -14.292 23.371  1.00 24.51 ? 48   LEU B N   1 
ATOM   4656  C  CA  . LEU B  1 31  ? 7.820   -13.543 22.782  1.00 25.04 ? 48   LEU B CA  1 
ATOM   4657  C  C   . LEU B  1 31  ? 9.022   -14.445 22.488  1.00 26.22 ? 48   LEU B C   1 
ATOM   4658  O  O   . LEU B  1 31  ? 10.017  -13.977 21.934  1.00 25.03 ? 48   LEU B O   1 
ATOM   4659  C  CB  . LEU B  1 31  ? 8.208   -12.414 23.736  1.00 25.86 ? 48   LEU B CB  1 
ATOM   4660  C  CG  . LEU B  1 31  ? 7.134   -11.357 24.016  1.00 27.53 ? 48   LEU B CG  1 
ATOM   4661  C  CD1 . LEU B  1 31  ? 7.615   -10.380 25.074  1.00 28.37 ? 48   LEU B CD1 1 
ATOM   4662  C  CD2 . LEU B  1 31  ? 6.735   -10.623 22.751  1.00 28.64 ? 48   LEU B CD2 1 
ATOM   4663  N  N   . GLY B  1 32  ? 8.948   -15.721 22.883  1.00 25.23 ? 49   GLY B N   1 
ATOM   4664  C  CA  . GLY B  1 32  ? 10.021  -16.668 22.618  1.00 25.33 ? 49   GLY B CA  1 
ATOM   4665  C  C   . GLY B  1 32  ? 11.196  -16.505 23.581  1.00 24.28 ? 49   GLY B C   1 
ATOM   4666  O  O   . GLY B  1 32  ? 12.346  -16.716 23.192  1.00 25.75 ? 49   GLY B O   1 
ATOM   4667  N  N   . LEU B  1 33  ? 10.898  -16.139 24.836  1.00 22.75 ? 50   LEU B N   1 
ATOM   4668  C  CA  . LEU B  1 33  ? 11.912  -15.995 25.872  1.00 23.37 ? 50   LEU B CA  1 
ATOM   4669  C  C   . LEU B  1 33  ? 11.872  -17.172 26.845  1.00 22.39 ? 50   LEU B C   1 
ATOM   4670  O  O   . LEU B  1 33  ? 12.728  -17.245 27.726  1.00 21.33 ? 50   LEU B O   1 
ATOM   4671  C  CB  . LEU B  1 33  ? 11.724  -14.691 26.645  1.00 23.40 ? 50   LEU B CB  1 
ATOM   4672  C  CG  . LEU B  1 33  ? 11.427  -13.437 25.814  1.00 23.82 ? 50   LEU B CG  1 
ATOM   4673  C  CD1 . LEU B  1 33  ? 11.284  -12.237 26.736  1.00 23.45 ? 50   LEU B CD1 1 
ATOM   4674  C  CD2 . LEU B  1 33  ? 12.498  -13.201 24.762  1.00 24.42 ? 50   LEU B CD2 1 
ATOM   4675  N  N   . GLN B  1 34  ? 10.856  -18.046 26.737  1.00 22.69 ? 51   GLN B N   1 
ATOM   4676  C  CA  . GLN B  1 34  ? 10.699  -19.144 27.682  1.00 22.97 ? 51   GLN B CA  1 
ATOM   4677  C  C   . GLN B  1 34  ? 11.948  -20.024 27.623  1.00 22.61 ? 51   GLN B C   1 
ATOM   4678  O  O   . GLN B  1 34  ? 12.340  -20.486 26.555  1.00 21.92 ? 51   GLN B O   1 
ATOM   4679  C  CB  . GLN B  1 34  ? 9.419   -19.932 27.394  1.00 24.72 ? 51   GLN B CB  1 
ATOM   4680  C  CG  . GLN B  1 34  ? 9.063   -20.984 28.442  1.00 24.96 ? 51   GLN B CG  1 
ATOM   4681  C  CD  . GLN B  1 34  ? 8.552   -20.415 29.747  1.00 27.05 ? 51   GLN B CD  1 
ATOM   4682  O  OE1 . GLN B  1 34  ? 8.596   -19.205 29.995  1.00 28.11 ? 51   GLN B OE1 1 
ATOM   4683  N  NE2 . GLN B  1 34  ? 8.068   -21.293 30.617  1.00 28.44 ? 51   GLN B NE2 1 
ATOM   4684  N  N   . GLY B  1 35  ? 12.595  -20.203 28.778  1.00 24.09 ? 52   GLY B N   1 
ATOM   4685  C  CA  . GLY B  1 35  ? 13.808  -21.000 28.876  1.00 24.46 ? 52   GLY B CA  1 
ATOM   4686  C  C   . GLY B  1 35  ? 15.087  -20.161 28.850  1.00 24.31 ? 52   GLY B C   1 
ATOM   4687  O  O   . GLY B  1 35  ? 16.155  -20.678 29.174  1.00 24.70 ? 52   GLY B O   1 
ATOM   4688  N  N   . LEU B  1 36  ? 14.984  -18.880 28.462  1.00 23.03 ? 53   LEU B N   1 
ATOM   4689  C  CA  . LEU B  1 36  ? 16.142  -17.997 28.386  1.00 22.89 ? 53   LEU B CA  1 
ATOM   4690  C  C   . LEU B  1 36  ? 16.303  -17.218 29.691  1.00 22.20 ? 53   LEU B C   1 
ATOM   4691  O  O   . LEU B  1 36  ? 17.249  -16.443 29.838  1.00 21.72 ? 53   LEU B O   1 
ATOM   4692  C  CB  . LEU B  1 36  ? 15.985  -17.048 27.198  1.00 23.61 ? 53   LEU B CB  1 
ATOM   4693  C  CG  . LEU B  1 36  ? 15.790  -17.696 25.824  1.00 23.96 ? 53   LEU B CG  1 
ATOM   4694  C  CD1 . LEU B  1 36  ? 15.743  -16.634 24.735  1.00 24.68 ? 53   LEU B CD1 1 
ATOM   4695  C  CD2 . LEU B  1 36  ? 16.880  -18.704 25.530  1.00 24.09 ? 53   LEU B CD2 1 
ATOM   4696  N  N   . LEU B  1 37  ? 15.343  -17.407 30.607  1.00 21.52 ? 54   LEU B N   1 
ATOM   4697  C  CA  . LEU B  1 37  ? 15.349  -16.801 31.927  1.00 22.59 ? 54   LEU B CA  1 
ATOM   4698  C  C   . LEU B  1 37  ? 15.077  -17.904 32.945  1.00 22.30 ? 54   LEU B C   1 
ATOM   4699  O  O   . LEU B  1 37  ? 14.473  -18.920 32.605  1.00 22.69 ? 54   LEU B O   1 
ATOM   4700  C  CB  . LEU B  1 37  ? 14.279  -15.711 32.028  1.00 22.52 ? 54   LEU B CB  1 
ATOM   4701  C  CG  . LEU B  1 37  ? 14.506  -14.455 31.183  1.00 22.60 ? 54   LEU B CG  1 
ATOM   4702  C  CD1 . LEU B  1 37  ? 13.194  -13.713 30.981  1.00 22.26 ? 54   LEU B CD1 1 
ATOM   4703  C  CD2 . LEU B  1 37  ? 15.540  -13.561 31.839  1.00 23.12 ? 54   LEU B CD2 1 
ATOM   4704  N  N   . PRO B  1 38  ? 15.510  -17.748 34.213  1.00 22.92 ? 55   PRO B N   1 
ATOM   4705  C  CA  . PRO B  1 38  ? 15.225  -18.747 35.241  1.00 23.68 ? 55   PRO B CA  1 
ATOM   4706  C  C   . PRO B  1 38  ? 13.734  -18.815 35.556  1.00 24.74 ? 55   PRO B C   1 
ATOM   4707  O  O   . PRO B  1 38  ? 13.008  -17.847 35.326  1.00 22.25 ? 55   PRO B O   1 
ATOM   4708  C  CB  . PRO B  1 38  ? 16.063  -18.313 36.443  1.00 24.15 ? 55   PRO B CB  1 
ATOM   4709  C  CG  . PRO B  1 38  ? 16.326  -16.847 36.212  1.00 25.07 ? 55   PRO B CG  1 
ATOM   4710  C  CD  . PRO B  1 38  ? 16.335  -16.638 34.708  1.00 24.56 ? 55   PRO B CD  1 
ATOM   4711  N  N   . PRO B  1 39  ? 13.244  -19.959 36.090  1.00 26.30 ? 56   PRO B N   1 
ATOM   4712  C  CA  . PRO B  1 39  ? 11.812  -20.237 36.181  1.00 29.09 ? 56   PRO B CA  1 
ATOM   4713  C  C   . PRO B  1 39  ? 11.141  -19.542 37.361  1.00 31.47 ? 56   PRO B C   1 
ATOM   4714  O  O   . PRO B  1 39  ? 10.471  -20.186 38.168  1.00 36.36 ? 56   PRO B O   1 
ATOM   4715  C  CB  . PRO B  1 39  ? 11.752  -21.777 36.316  1.00 29.44 ? 56   PRO B CB  1 
ATOM   4716  C  CG  . PRO B  1 39  ? 13.192  -22.248 36.236  1.00 28.95 ? 56   PRO B CG  1 
ATOM   4717  C  CD  . PRO B  1 39  ? 14.046  -21.065 36.631  1.00 28.50 ? 56   PRO B CD  1 
ATOM   4718  N  N   . LYS B  1 40  ? 11.350  -18.229 37.456  1.00 30.57 ? 57   LYS B N   1 
ATOM   4719  C  CA  . LYS B  1 40  ? 10.756  -17.421 38.502  1.00 30.16 ? 57   LYS B CA  1 
ATOM   4720  C  C   . LYS B  1 40  ? 10.353  -16.078 37.907  1.00 28.62 ? 57   LYS B C   1 
ATOM   4721  O  O   . LYS B  1 40  ? 11.154  -15.445 37.221  1.00 27.63 ? 57   LYS B O   1 
ATOM   4722  C  CB  . LYS B  1 40  ? 11.710  -17.142 39.661  1.00 30.64 ? 57   LYS B CB  1 
ATOM   4723  C  CG  . LYS B  1 40  ? 10.996  -16.507 40.845  1.00 31.98 ? 57   LYS B CG  1 
ATOM   4724  C  CD  . LYS B  1 40  ? 11.929  -15.733 41.751  1.00 31.28 ? 57   LYS B CD  1 
ATOM   4725  C  CE  . LYS B  1 40  ? 11.232  -15.158 42.934  1.00 29.73 ? 57   LYS B CE  1 
ATOM   4726  N  NZ  . LYS B  1 40  ? 12.207  -14.470 43.776  1.00 29.45 ? 57   LYS B NZ  1 
ATOM   4727  N  N   . ILE B  1 41  ? 9.112   -15.671 38.194  1.00 28.60 ? 58   ILE B N   1 
ATOM   4728  C  CA  . ILE B  1 41  ? 8.564   -14.405 37.741  1.00 27.64 ? 58   ILE B CA  1 
ATOM   4729  C  C   . ILE B  1 41  ? 8.655   -13.416 38.899  1.00 27.24 ? 58   ILE B C   1 
ATOM   4730  O  O   . ILE B  1 41  ? 8.053   -13.632 39.948  1.00 26.10 ? 58   ILE B O   1 
ATOM   4731  C  CB  . ILE B  1 41  ? 7.108   -14.575 37.265  1.00 28.44 ? 58   ILE B CB  1 
ATOM   4732  C  CG1 . ILE B  1 41  ? 6.926   -15.775 36.331  1.00 28.49 ? 58   ILE B CG1 1 
ATOM   4733  C  CG2 . ILE B  1 41  ? 6.584   -13.280 36.639  1.00 28.84 ? 58   ILE B CG2 1 
ATOM   4734  C  CD1 . ILE B  1 41  ? 7.798   -15.758 35.089  1.00 27.94 ? 58   ILE B CD1 1 
ATOM   4735  N  N   . GLU B  1 42  ? 9.411   -12.329 38.709  1.00 26.77 ? 59   GLU B N   1 
ATOM   4736  C  CA  . GLU B  1 42  ? 9.545   -11.315 39.743  1.00 26.75 ? 59   GLU B CA  1 
ATOM   4737  C  C   . GLU B  1 42  ? 8.819   -10.040 39.324  1.00 26.96 ? 59   GLU B C   1 
ATOM   4738  O  O   . GLU B  1 42  ? 8.282   -9.962  38.226  1.00 27.57 ? 59   GLU B O   1 
ATOM   4739  C  CB  . GLU B  1 42  ? 11.025  -11.077 40.035  1.00 27.98 ? 59   GLU B CB  1 
ATOM   4740  C  CG  . GLU B  1 42  ? 11.668  -12.252 40.764  1.00 28.97 ? 59   GLU B CG  1 
ATOM   4741  C  CD  . GLU B  1 42  ? 13.131  -12.066 41.097  1.00 29.84 ? 59   GLU B CD  1 
ATOM   4742  O  OE1 . GLU B  1 42  ? 13.721  -11.075 40.617  1.00 30.31 ? 59   GLU B OE1 1 
ATOM   4743  O  OE2 . GLU B  1 42  ? 13.670  -12.905 41.858  1.00 31.17 ? 59   GLU B OE2 1 
ATOM   4744  N  N   . THR B  1 43  ? 8.765   -9.076  40.246  1.00 25.93 ? 60   THR B N   1 
ATOM   4745  C  CA  . THR B  1 43  ? 8.309   -7.726  39.957  1.00 26.90 ? 60   THR B CA  1 
ATOM   4746  C  C   . THR B  1 43  ? 9.514   -6.796  40.027  1.00 25.23 ? 60   THR B C   1 
ATOM   4747  O  O   . THR B  1 43  ? 10.573  -7.187  40.505  1.00 23.95 ? 60   THR B O   1 
ATOM   4748  C  CB  . THR B  1 43  ? 7.237   -7.303  40.959  1.00 28.70 ? 60   THR B CB  1 
ATOM   4749  O  OG1 . THR B  1 43  ? 7.899   -7.322  42.222  1.00 29.32 ? 60   THR B OG1 1 
ATOM   4750  C  CG2 . THR B  1 43  ? 6.026   -8.220  40.953  1.00 29.37 ? 60   THR B CG2 1 
ATOM   4751  N  N   . GLN B  1 44  ? 9.337   -5.553  39.576  1.00 25.47 ? 61   GLN B N   1 
ATOM   4752  C  CA  . GLN B  1 44  ? 10.390  -4.550  39.673  1.00 25.09 ? 61   GLN B CA  1 
ATOM   4753  C  C   . GLN B  1 44  ? 10.762  -4.320  41.139  1.00 25.99 ? 61   GLN B C   1 
ATOM   4754  O  O   . GLN B  1 44  ? 11.930  -4.097  41.449  1.00 25.31 ? 61   GLN B O   1 
ATOM   4755  C  CB  . GLN B  1 44  ? 9.972   -3.240  39.005  1.00 24.49 ? 61   GLN B CB  1 
ATOM   4756  C  CG  . GLN B  1 44  ? 11.151  -2.348  38.634  1.00 24.16 ? 61   GLN B CG  1 
ATOM   4757  C  CD  . GLN B  1 44  ? 10.712  -1.003  38.099  1.00 24.32 ? 61   GLN B CD  1 
ATOM   4758  O  OE1 . GLN B  1 44  ? 10.303  -0.117  38.857  1.00 24.50 ? 61   GLN B OE1 1 
ATOM   4759  N  NE2 . GLN B  1 44  ? 10.807  -0.838  36.789  1.00 24.38 ? 61   GLN B NE2 1 
ATOM   4760  N  N   . ASP B  1 45  ? 9.763   -4.383  42.032  1.00 27.57 ? 62   ASP B N   1 
ATOM   4761  C  CA  . ASP B  1 45  ? 9.968   -4.237  43.465  1.00 28.68 ? 62   ASP B CA  1 
ATOM   4762  C  C   . ASP B  1 45  ? 11.035  -5.216  43.966  1.00 28.58 ? 62   ASP B C   1 
ATOM   4763  O  O   . ASP B  1 45  ? 11.925  -4.827  44.725  1.00 27.78 ? 62   ASP B O   1 
ATOM   4764  C  CB  . ASP B  1 45  ? 8.655   -4.384  44.221  1.00 31.59 ? 62   ASP B CB  1 
ATOM   4765  C  CG  . ASP B  1 45  ? 7.644   -3.255  44.051  1.00 34.80 ? 62   ASP B CG  1 
ATOM   4766  O  OD1 . ASP B  1 45  ? 8.000   -2.217  43.453  1.00 35.49 ? 62   ASP B OD1 1 
ATOM   4767  O  OD2 . ASP B  1 45  ? 6.498   -3.420  44.521  1.00 37.95 ? 62   ASP B OD2 1 
ATOM   4768  N  N   . ILE B  1 46  ? 10.962  -6.480  43.529  1.00 27.74 ? 63   ILE B N   1 
ATOM   4769  C  CA  . ILE B  1 46  ? 11.871  -7.512  44.011  1.00 28.52 ? 63   ILE B CA  1 
ATOM   4770  C  C   . ILE B  1 46  ? 13.268  -7.319  43.422  1.00 26.78 ? 63   ILE B C   1 
ATOM   4771  O  O   . ILE B  1 46  ? 14.262  -7.486  44.126  1.00 27.23 ? 63   ILE B O   1 
ATOM   4772  C  CB  . ILE B  1 46  ? 11.330  -8.922  43.705  1.00 30.57 ? 63   ILE B CB  1 
ATOM   4773  C  CG1 . ILE B  1 46  ? 9.994   -9.184  44.403  1.00 32.96 ? 63   ILE B CG1 1 
ATOM   4774  C  CG2 . ILE B  1 46  ? 12.364  -9.996  44.050  1.00 30.21 ? 63   ILE B CG2 1 
ATOM   4775  C  CD1 . ILE B  1 46  ? 10.059  -9.133  45.918  1.00 36.27 ? 63   ILE B CD1 1 
ATOM   4776  N  N   . GLN B  1 47  ? 13.349  -7.025  42.120  1.00 25.15 ? 64   GLN B N   1 
ATOM   4777  C  CA  . GLN B  1 47  ? 14.629  -6.784  41.471  1.00 24.17 ? 64   GLN B CA  1 
ATOM   4778  C  C   . GLN B  1 47  ? 15.363  -5.631  42.153  1.00 24.14 ? 64   GLN B C   1 
ATOM   4779  O  O   . GLN B  1 47  ? 16.585  -5.673  42.298  1.00 24.69 ? 64   GLN B O   1 
ATOM   4780  C  CB  . GLN B  1 47  ? 14.432  -6.434  39.999  1.00 23.91 ? 64   GLN B CB  1 
ATOM   4781  C  CG  . GLN B  1 47  ? 13.970  -7.603  39.139  1.00 23.62 ? 64   GLN B CG  1 
ATOM   4782  C  CD  . GLN B  1 47  ? 13.476  -7.157  37.782  1.00 23.42 ? 64   GLN B CD  1 
ATOM   4783  O  OE1 . GLN B  1 47  ? 12.603  -6.287  37.684  1.00 22.67 ? 64   GLN B OE1 1 
ATOM   4784  N  NE2 . GLN B  1 47  ? 14.047  -7.725  36.728  1.00 23.11 ? 64   GLN B NE2 1 
ATOM   4785  N  N   . ALA B  1 48  ? 14.610  -4.591  42.530  1.00 24.57 ? 65   ALA B N   1 
ATOM   4786  C  CA  . ALA B  1 48  ? 15.185  -3.419  43.174  1.00 26.82 ? 65   ALA B CA  1 
ATOM   4787  C  C   . ALA B  1 48  ? 15.756  -3.803  44.536  1.00 27.93 ? 65   ALA B C   1 
ATOM   4788  O  O   . ALA B  1 48  ? 16.870  -3.408  44.873  1.00 29.43 ? 65   ALA B O   1 
ATOM   4789  C  CB  . ALA B  1 48  ? 14.149  -2.327  43.304  1.00 26.69 ? 65   ALA B CB  1 
ATOM   4790  N  N   . LEU B  1 49  ? 14.983  -4.579  45.305  1.00 27.86 ? 66   LEU B N   1 
ATOM   4791  C  CA  . LEU B  1 49  ? 15.393  -4.995  46.637  1.00 28.81 ? 66   LEU B CA  1 
ATOM   4792  C  C   . LEU B  1 49  ? 16.660  -5.846  46.563  1.00 28.69 ? 66   LEU B C   1 
ATOM   4793  O  O   . LEU B  1 49  ? 17.547  -5.686  47.400  1.00 29.51 ? 66   LEU B O   1 
ATOM   4794  C  CB  . LEU B  1 49  ? 14.258  -5.727  47.349  1.00 29.63 ? 66   LEU B CB  1 
ATOM   4795  C  CG  . LEU B  1 49  ? 13.112  -4.852  47.865  1.00 31.52 ? 66   LEU B CG  1 
ATOM   4796  C  CD1 . LEU B  1 49  ? 11.930  -5.714  48.267  1.00 32.06 ? 66   LEU B CD1 1 
ATOM   4797  C  CD2 . LEU B  1 49  ? 13.547  -3.986  49.039  1.00 32.45 ? 66   LEU B CD2 1 
ATOM   4798  N  N   . ARG B  1 50  ? 16.752  -6.734  45.562  1.00 27.99 ? 67   ARG B N   1 
ATOM   4799  C  CA  . ARG B  1 50  ? 17.952  -7.540  45.372  1.00 27.83 ? 67   ARG B CA  1 
ATOM   4800  C  C   . ARG B  1 50  ? 19.163  -6.624  45.183  1.00 28.19 ? 67   ARG B C   1 
ATOM   4801  O  O   . ARG B  1 50  ? 20.222  -6.842  45.777  1.00 26.99 ? 67   ARG B O   1 
ATOM   4802  C  CB  . ARG B  1 50  ? 17.834  -8.505  44.184  1.00 27.31 ? 67   ARG B CB  1 
ATOM   4803  C  CG  . ARG B  1 50  ? 19.113  -9.292  43.921  1.00 26.55 ? 67   ARG B CG  1 
ATOM   4804  C  CD  . ARG B  1 50  ? 19.047  -10.183 42.695  1.00 27.22 ? 67   ARG B CD  1 
ATOM   4805  N  NE  . ARG B  1 50  ? 18.102  -11.289 42.882  1.00 27.96 ? 67   ARG B NE  1 
ATOM   4806  C  CZ  . ARG B  1 50  ? 16.872  -11.384 42.384  1.00 27.42 ? 67   ARG B CZ  1 
ATOM   4807  N  NH1 . ARG B  1 50  ? 16.353  -10.415 41.647  1.00 28.50 ? 67   ARG B NH1 1 
ATOM   4808  N  NH2 . ARG B  1 50  ? 16.145  -12.451 42.657  1.00 27.53 ? 67   ARG B NH2 1 
ATOM   4809  N  N   . PHE B  1 51  ? 18.995  -5.593  44.349  1.00 29.28 ? 68   PHE B N   1 
ATOM   4810  C  CA  . PHE B  1 51  ? 20.060  -4.642  44.081  1.00 30.92 ? 68   PHE B CA  1 
ATOM   4811  C  C   . PHE B  1 51  ? 20.486  -3.949  45.374  1.00 31.02 ? 68   PHE B C   1 
ATOM   4812  O  O   . PHE B  1 51  ? 21.677  -3.878  45.669  1.00 33.10 ? 68   PHE B O   1 
ATOM   4813  C  CB  . PHE B  1 51  ? 19.661  -3.583  43.050  1.00 33.15 ? 68   PHE B CB  1 
ATOM   4814  C  CG  . PHE B  1 51  ? 20.652  -2.430  43.024  1.00 35.78 ? 68   PHE B CG  1 
ATOM   4815  C  CD1 . PHE B  1 51  ? 21.812  -2.514  42.266  1.00 37.25 ? 68   PHE B CD1 1 
ATOM   4816  C  CD2 . PHE B  1 51  ? 20.445  -1.289  43.792  1.00 37.97 ? 68   PHE B CD2 1 
ATOM   4817  C  CE1 . PHE B  1 51  ? 22.731  -1.474  42.256  1.00 38.68 ? 68   PHE B CE1 1 
ATOM   4818  C  CE2 . PHE B  1 51  ? 21.373  -0.256  43.786  1.00 39.74 ? 68   PHE B CE2 1 
ATOM   4819  C  CZ  . PHE B  1 51  ? 22.508  -0.350  43.014  1.00 39.09 ? 68   PHE B CZ  1 
ATOM   4820  N  N   . HIS B  1 52  ? 19.514  -3.418  46.123  1.00 31.28 ? 69   HIS B N   1 
ATOM   4821  C  CA  . HIS B  1 52  ? 19.800  -2.647  47.323  1.00 33.70 ? 69   HIS B CA  1 
ATOM   4822  C  C   . HIS B  1 52  ? 20.563  -3.504  48.334  1.00 35.93 ? 69   HIS B C   1 
ATOM   4823  O  O   . HIS B  1 52  ? 21.436  -2.998  49.040  1.00 34.98 ? 69   HIS B O   1 
ATOM   4824  C  CB  . HIS B  1 52  ? 18.510  -2.057  47.904  1.00 35.44 ? 69   HIS B CB  1 
ATOM   4825  C  CG  . HIS B  1 52  ? 17.873  -1.016  47.039  1.00 36.63 ? 69   HIS B CG  1 
ATOM   4826  N  ND1 . HIS B  1 52  ? 18.582  0.008   46.445  1.00 36.80 ? 69   HIS B ND1 1 
ATOM   4827  C  CD2 . HIS B  1 52  ? 16.591  -0.832  46.682  1.00 37.10 ? 69   HIS B CD2 1 
ATOM   4828  C  CE1 . HIS B  1 52  ? 17.747  0.771   45.748  1.00 37.13 ? 69   HIS B CE1 1 
ATOM   4829  N  NE2 . HIS B  1 52  ? 16.533  0.275   45.872  1.00 35.54 ? 69   HIS B NE2 1 
ATOM   4830  N  N   . ARG B  1 53  ? 20.220  -4.798  48.397  1.00 37.24 ? 70   ARG B N   1 
ATOM   4831  C  CA  . ARG B  1 53  ? 20.884  -5.747  49.278  1.00 39.08 ? 70   ARG B CA  1 
ATOM   4832  C  C   . ARG B  1 53  ? 22.333  -5.950  48.840  1.00 38.14 ? 70   ARG B C   1 
ATOM   4833  O  O   . ARG B  1 53  ? 23.235  -5.996  49.672  1.00 38.82 ? 70   ARG B O   1 
ATOM   4834  C  CB  . ARG B  1 53  ? 20.154  -7.097  49.264  1.00 40.89 ? 70   ARG B CB  1 
ATOM   4835  C  CG  . ARG B  1 53  ? 20.749  -8.154  50.185  1.00 44.70 ? 70   ARG B CG  1 
ATOM   4836  C  CD  . ARG B  1 53  ? 20.472  -9.562  49.695  1.00 48.04 ? 70   ARG B CD  1 
ATOM   4837  N  NE  . ARG B  1 53  ? 21.169  -9.892  48.444  1.00 50.10 ? 70   ARG B NE  1 
ATOM   4838  C  CZ  . ARG B  1 53  ? 20.934  -10.975 47.710  1.00 51.16 ? 70   ARG B CZ  1 
ATOM   4839  N  NH1 . ARG B  1 53  ? 19.990  -11.829 48.069  1.00 53.71 ? 70   ARG B NH1 1 
ATOM   4840  N  NH2 . ARG B  1 53  ? 21.633  -11.201 46.611  1.00 50.46 ? 70   ARG B NH2 1 
ATOM   4841  N  N   . ASN B  1 54  ? 22.541  -6.100  47.530  1.00 37.87 ? 71   ASN B N   1 
ATOM   4842  C  CA  . ASN B  1 54  ? 23.869  -6.316  46.979  1.00 39.73 ? 71   ASN B CA  1 
ATOM   4843  C  C   . ASN B  1 54  ? 24.752  -5.087  47.182  1.00 44.65 ? 71   ASN B C   1 
ATOM   4844  O  O   . ASN B  1 54  ? 25.960  -5.226  47.381  1.00 45.77 ? 71   ASN B O   1 
ATOM   4845  C  CB  . ASN B  1 54  ? 23.807  -6.672  45.500  1.00 39.27 ? 71   ASN B CB  1 
ATOM   4846  C  CG  . ASN B  1 54  ? 23.291  -8.069  45.265  1.00 38.78 ? 71   ASN B CG  1 
ATOM   4847  O  OD1 . ASN B  1 54  ? 23.193  -8.866  46.207  1.00 37.18 ? 71   ASN B OD1 1 
ATOM   4848  N  ND2 . ASN B  1 54  ? 22.984  -8.388  44.016  1.00 37.89 ? 71   ASN B ND2 1 
ATOM   4849  N  N   . LEU B  1 55  ? 24.148  -3.893  47.112  1.00 45.35 ? 72   LEU B N   1 
ATOM   4850  C  CA  . LEU B  1 55  ? 24.895  -2.650  47.229  1.00 49.02 ? 72   LEU B CA  1 
ATOM   4851  C  C   . LEU B  1 55  ? 25.274  -2.403  48.690  1.00 53.00 ? 72   LEU B C   1 
ATOM   4852  O  O   . LEU B  1 55  ? 26.388  -1.964  48.971  1.00 55.19 ? 72   LEU B O   1 
ATOM   4853  C  CB  . LEU B  1 55  ? 24.100  -1.473  46.666  1.00 47.20 ? 72   LEU B CB  1 
ATOM   4854  C  CG  . LEU B  1 55  ? 24.921  -0.217  46.358  1.00 46.43 ? 72   LEU B CG  1 
ATOM   4855  C  CD1 . LEU B  1 55  ? 25.683  -0.402  45.061  1.00 45.65 ? 72   LEU B CD1 1 
ATOM   4856  C  CD2 . LEU B  1 55  ? 24.065  1.032   46.307  1.00 46.98 ? 72   LEU B CD2 1 
ATOM   4857  N  N   . LYS B  1 56  ? 24.344  -2.691  49.610  1.00 56.31 ? 73   LYS B N   1 
ATOM   4858  C  CA  . LYS B  1 56  ? 24.553  -2.450  51.030  1.00 60.88 ? 73   LYS B CA  1 
ATOM   4859  C  C   . LYS B  1 56  ? 25.727  -3.278  51.557  1.00 63.69 ? 73   LYS B C   1 
ATOM   4860  O  O   . LYS B  1 56  ? 26.336  -2.905  52.557  1.00 65.57 ? 73   LYS B O   1 
ATOM   4861  C  CB  . LYS B  1 56  ? 23.272  -2.733  51.824  1.00 63.68 ? 73   LYS B CB  1 
ATOM   4862  C  CG  . LYS B  1 56  ? 23.380  -2.470  53.320  1.00 67.59 ? 73   LYS B CG  1 
ATOM   4863  C  CD  . LYS B  1 56  ? 22.052  -2.406  54.062  1.00 71.31 ? 73   LYS B CD  1 
ATOM   4864  C  CE  . LYS B  1 56  ? 22.251  -2.066  55.508  1.00 73.56 ? 73   LYS B CE  1 
ATOM   4865  N  NZ  . LYS B  1 56  ? 20.983  -1.938  56.231  1.00 75.23 ? 73   LYS B NZ  1 
ATOM   4866  N  N   . LYS B  1 57  ? 26.032  -4.399  50.888  1.00 65.50 ? 74   LYS B N   1 
ATOM   4867  C  CA  . LYS B  1 57  ? 27.172  -5.232  51.241  1.00 68.60 ? 74   LYS B CA  1 
ATOM   4868  C  C   . LYS B  1 57  ? 28.480  -4.492  50.961  1.00 72.20 ? 74   LYS B C   1 
ATOM   4869  O  O   . LYS B  1 57  ? 29.433  -4.615  51.728  1.00 75.64 ? 74   LYS B O   1 
ATOM   4870  C  CB  . LYS B  1 57  ? 27.136  -6.554  50.464  1.00 67.31 ? 74   LYS B CB  1 
ATOM   4871  N  N   . MET B  1 58  ? 28.514  -3.729  49.860  1.00 73.37 ? 75   MET B N   1 
ATOM   4872  C  CA  . MET B  1 58  ? 29.719  -3.050  49.401  1.00 75.30 ? 75   MET B CA  1 
ATOM   4873  C  C   . MET B  1 58  ? 30.018  -1.823  50.266  1.00 70.96 ? 75   MET B C   1 
ATOM   4874  O  O   . MET B  1 58  ? 29.162  -1.363  51.023  1.00 67.80 ? 75   MET B O   1 
ATOM   4875  C  CB  . MET B  1 58  ? 29.563  -2.620  47.937  1.00 79.73 ? 75   MET B CB  1 
ATOM   4876  C  CG  . MET B  1 58  ? 29.487  -3.778  46.957  1.00 82.72 ? 75   MET B CG  1 
ATOM   4877  S  SD  . MET B  1 58  ? 29.073  -3.233  45.288  1.00 88.53 ? 75   MET B SD  1 
ATOM   4878  C  CE  . MET B  1 58  ? 29.300  -4.749  44.347  1.00 87.88 ? 75   MET B CE  1 
ATOM   4879  N  N   . THR B  1 59  ? 31.249  -1.304  50.136  1.00 66.57 ? 76   THR B N   1 
ATOM   4880  C  CA  . THR B  1 59  ? 31.708  -0.154  50.906  1.00 63.22 ? 76   THR B CA  1 
ATOM   4881  C  C   . THR B  1 59  ? 32.373  0.892   50.005  1.00 57.63 ? 76   THR B C   1 
ATOM   4882  O  O   . THR B  1 59  ? 32.229  2.087   50.261  1.00 55.97 ? 76   THR B O   1 
ATOM   4883  C  CB  . THR B  1 59  ? 32.652  -0.613  52.021  1.00 63.49 ? 76   THR B CB  1 
ATOM   4884  O  OG1 . THR B  1 59  ? 33.485  -1.633  51.476  1.00 65.81 ? 76   THR B OG1 1 
ATOM   4885  C  CG2 . THR B  1 59  ? 31.906  -1.166  53.221  1.00 62.47 ? 76   THR B CG2 1 
ATOM   4886  N  N   . SER B  1 60  ? 33.111  0.447   48.976  1.00 52.81 ? 77   SER B N   1 
ATOM   4887  C  CA  . SER B  1 60  ? 33.843  1.343   48.091  1.00 49.88 ? 77   SER B CA  1 
ATOM   4888  C  C   . SER B  1 60  ? 32.893  2.063   47.131  1.00 47.37 ? 77   SER B C   1 
ATOM   4889  O  O   . SER B  1 60  ? 32.186  1.412   46.367  1.00 41.13 ? 77   SER B O   1 
ATOM   4890  C  CB  . SER B  1 60  ? 34.893  0.588   47.321  1.00 50.43 ? 77   SER B CB  1 
ATOM   4891  O  OG  . SER B  1 60  ? 35.520  1.427   46.361  1.00 50.76 ? 77   SER B OG  1 
ATOM   4892  N  N   . PRO B  1 61  ? 32.857  3.419   47.120  1.00 46.11 ? 78   PRO B N   1 
ATOM   4893  C  CA  . PRO B  1 61  ? 32.081  4.165   46.123  1.00 45.58 ? 78   PRO B CA  1 
ATOM   4894  C  C   . PRO B  1 61  ? 32.347  3.761   44.674  1.00 44.38 ? 78   PRO B C   1 
ATOM   4895  O  O   . PRO B  1 61  ? 31.420  3.744   43.869  1.00 41.62 ? 78   PRO B O   1 
ATOM   4896  C  CB  . PRO B  1 61  ? 32.487  5.624   46.385  1.00 45.89 ? 78   PRO B CB  1 
ATOM   4897  C  CG  . PRO B  1 61  ? 32.844  5.647   47.852  1.00 46.54 ? 78   PRO B CG  1 
ATOM   4898  C  CD  . PRO B  1 61  ? 33.519  4.308   48.090  1.00 46.38 ? 78   PRO B CD  1 
ATOM   4899  N  N   . LEU B  1 62  ? 33.610  3.447   44.352  1.00 43.45 ? 79   LEU B N   1 
ATOM   4900  C  CA  . LEU B  1 62  ? 33.997  3.091   42.994  1.00 44.84 ? 79   LEU B CA  1 
ATOM   4901  C  C   . LEU B  1 62  ? 33.393  1.746   42.597  1.00 44.24 ? 79   LEU B C   1 
ATOM   4902  O  O   . LEU B  1 62  ? 32.929  1.597   41.471  1.00 41.35 ? 79   LEU B O   1 
ATOM   4903  C  CB  . LEU B  1 62  ? 35.515  3.082   42.822  1.00 46.46 ? 79   LEU B CB  1 
ATOM   4904  C  CG  . LEU B  1 62  ? 36.158  4.433   42.490  1.00 49.78 ? 79   LEU B CG  1 
ATOM   4905  C  CD1 . LEU B  1 62  ? 37.672  4.317   42.470  1.00 50.81 ? 79   LEU B CD1 1 
ATOM   4906  C  CD2 . LEU B  1 62  ? 35.649  4.973   41.161  1.00 51.29 ? 79   LEU B CD2 1 
ATOM   4907  N  N   . GLU B  1 63  ? 33.415  0.766   43.508  1.00 43.85 ? 80   GLU B N   1 
ATOM   4908  C  CA  . GLU B  1 63  ? 32.831  -0.538  43.229  1.00 45.08 ? 80   GLU B CA  1 
ATOM   4909  C  C   . GLU B  1 63  ? 31.314  -0.418  43.058  1.00 39.82 ? 80   GLU B C   1 
ATOM   4910  O  O   . GLU B  1 63  ? 30.736  -1.095  42.213  1.00 39.43 ? 80   GLU B O   1 
ATOM   4911  C  CB  . GLU B  1 63  ? 33.182  -1.547  44.322  1.00 49.81 ? 80   GLU B CB  1 
ATOM   4912  C  CG  . GLU B  1 63  ? 34.673  -1.868  44.381  1.00 54.67 ? 80   GLU B CG  1 
ATOM   4913  C  CD  . GLU B  1 63  ? 35.025  -3.035  45.289  1.00 58.55 ? 80   GLU B CD  1 
ATOM   4914  O  OE1 . GLU B  1 63  ? 36.218  -3.153  45.644  1.00 58.80 ? 80   GLU B OE1 1 
ATOM   4915  O  OE2 . GLU B  1 63  ? 34.120  -3.832  45.626  1.00 61.00 ? 80   GLU B OE2 1 
ATOM   4916  N  N   . LYS B  1 64  ? 30.684  0.447   43.860  1.00 36.94 ? 81   LYS B N   1 
ATOM   4917  C  CA  . LYS B  1 64  ? 29.259  0.722   43.749  1.00 36.77 ? 81   LYS B CA  1 
ATOM   4918  C  C   . LYS B  1 64  ? 28.955  1.388   42.408  1.00 35.07 ? 81   LYS B C   1 
ATOM   4919  O  O   . LYS B  1 64  ? 27.924  1.109   41.799  1.00 33.42 ? 81   LYS B O   1 
ATOM   4920  C  CB  . LYS B  1 64  ? 28.791  1.636   44.885  1.00 36.95 ? 81   LYS B CB  1 
ATOM   4921  C  CG  . LYS B  1 64  ? 28.960  1.066   46.288  1.00 38.65 ? 81   LYS B CG  1 
ATOM   4922  C  CD  . LYS B  1 64  ? 29.008  2.145   47.365  1.00 40.98 ? 81   LYS B CD  1 
ATOM   4923  C  CE  . LYS B  1 64  ? 27.785  2.250   48.212  1.00 42.88 ? 81   LYS B CE  1 
ATOM   4924  N  NZ  . LYS B  1 64  ? 27.893  1.334   49.352  1.00 43.80 ? 81   LYS B NZ  1 
ATOM   4925  N  N   . TYR B  1 65  ? 29.853  2.278   41.966  1.00 32.15 ? 82   TYR B N   1 
ATOM   4926  C  CA  . TYR B  1 65  ? 29.693  2.975   40.700  1.00 31.47 ? 82   TYR B CA  1 
ATOM   4927  C  C   . TYR B  1 65  ? 29.654  1.959   39.561  1.00 32.30 ? 82   TYR B C   1 
ATOM   4928  O  O   . TYR B  1 65  ? 28.744  1.993   38.736  1.00 31.30 ? 82   TYR B O   1 
ATOM   4929  C  CB  . TYR B  1 65  ? 30.813  4.002   40.491  1.00 29.98 ? 82   TYR B CB  1 
ATOM   4930  C  CG  . TYR B  1 65  ? 30.821  4.613   39.096  1.00 28.40 ? 82   TYR B CG  1 
ATOM   4931  C  CD1 . TYR B  1 65  ? 31.521  4.018   38.053  1.00 27.74 ? 82   TYR B CD1 1 
ATOM   4932  C  CD2 . TYR B  1 65  ? 30.106  5.770   38.819  1.00 27.55 ? 82   TYR B CD2 1 
ATOM   4933  C  CE1 . TYR B  1 65  ? 31.514  4.563   36.779  1.00 28.14 ? 82   TYR B CE1 1 
ATOM   4934  C  CE2 . TYR B  1 65  ? 30.096  6.327   37.553  1.00 26.94 ? 82   TYR B CE2 1 
ATOM   4935  C  CZ  . TYR B  1 65  ? 30.804  5.724   36.530  1.00 27.85 ? 82   TYR B CZ  1 
ATOM   4936  O  OH  . TYR B  1 65  ? 30.793  6.278   35.282  1.00 28.43 ? 82   TYR B OH  1 
ATOM   4937  N  N   . ILE B  1 66  ? 30.647  1.060   39.530  1.00 31.62 ? 83   ILE B N   1 
ATOM   4938  C  CA  . ILE B  1 66  ? 30.796  0.088   38.456  1.00 33.85 ? 83   ILE B CA  1 
ATOM   4939  C  C   . ILE B  1 66  ? 29.565  -0.817  38.411  1.00 32.66 ? 83   ILE B C   1 
ATOM   4940  O  O   . ILE B  1 66  ? 29.095  -1.174  37.331  1.00 32.05 ? 83   ILE B O   1 
ATOM   4941  C  CB  . ILE B  1 66  ? 32.097  -0.726  38.628  1.00 35.16 ? 83   ILE B CB  1 
ATOM   4942  C  CG1 . ILE B  1 66  ? 33.349  0.154   38.517  1.00 36.36 ? 83   ILE B CG1 1 
ATOM   4943  C  CG2 . ILE B  1 66  ? 32.156  -1.902  37.652  1.00 35.47 ? 83   ILE B CG2 1 
ATOM   4944  C  CD1 . ILE B  1 66  ? 33.547  0.809   37.161  1.00 37.61 ? 83   ILE B CD1 1 
ATOM   4945  N  N   . TYR B  1 67  ? 29.060  -1.181  39.594  1.00 32.08 ? 84   TYR B N   1 
ATOM   4946  C  CA  . TYR B  1 67  ? 27.926  -2.082  39.716  1.00 33.25 ? 84   TYR B CA  1 
ATOM   4947  C  C   . TYR B  1 67  ? 26.660  -1.411  39.180  1.00 31.94 ? 84   TYR B C   1 
ATOM   4948  O  O   . TYR B  1 67  ? 25.980  -1.980  38.329  1.00 32.43 ? 84   TYR B O   1 
ATOM   4949  C  CB  . TYR B  1 67  ? 27.793  -2.507  41.183  1.00 35.18 ? 84   TYR B CB  1 
ATOM   4950  C  CG  . TYR B  1 67  ? 26.599  -3.400  41.498  1.00 37.76 ? 84   TYR B CG  1 
ATOM   4951  C  CD1 . TYR B  1 67  ? 26.268  -4.484  40.691  1.00 40.52 ? 84   TYR B CD1 1 
ATOM   4952  C  CD2 . TYR B  1 67  ? 25.786  -3.140  42.596  1.00 39.71 ? 84   TYR B CD2 1 
ATOM   4953  C  CE1 . TYR B  1 67  ? 25.176  -5.291  40.977  1.00 41.27 ? 84   TYR B CE1 1 
ATOM   4954  C  CE2 . TYR B  1 67  ? 24.690  -3.935  42.891  1.00 40.80 ? 84   TYR B CE2 1 
ATOM   4955  C  CZ  . TYR B  1 67  ? 24.381  -5.012  42.077  1.00 41.41 ? 84   TYR B CZ  1 
ATOM   4956  O  OH  . TYR B  1 67  ? 23.302  -5.794  42.377  1.00 43.58 ? 84   TYR B OH  1 
ATOM   4957  N  N   . ILE B  1 68  ? 26.347  -0.207  39.677  1.00 30.51 ? 85   ILE B N   1 
ATOM   4958  C  CA  . ILE B  1 68  ? 25.095  0.450   39.326  1.00 30.34 ? 85   ILE B CA  1 
ATOM   4959  C  C   . ILE B  1 68  ? 25.094  0.811   37.841  1.00 28.11 ? 85   ILE B C   1 
ATOM   4960  O  O   . ILE B  1 68  ? 24.068  0.663   37.185  1.00 27.23 ? 85   ILE B O   1 
ATOM   4961  C  CB  . ILE B  1 68  ? 24.787  1.667   40.222  1.00 31.91 ? 85   ILE B CB  1 
ATOM   4962  C  CG1 . ILE B  1 68  ? 23.309  2.078   40.100  1.00 34.52 ? 85   ILE B CG1 1 
ATOM   4963  C  CG2 . ILE B  1 68  ? 25.721  2.840   39.930  1.00 33.01 ? 85   ILE B CG2 1 
ATOM   4964  C  CD1 . ILE B  1 68  ? 22.874  3.188   41.042  1.00 35.59 ? 85   ILE B CD1 1 
ATOM   4965  N  N   . MET B  1 69  ? 26.231  1.271   37.299  1.00 26.93 ? 86   MET B N   1 
ATOM   4966  C  CA  . MET B  1 69  ? 26.260  1.719   35.912  1.00 26.86 ? 86   MET B CA  1 
ATOM   4967  C  C   . MET B  1 69  ? 26.134  0.527   34.961  1.00 27.14 ? 86   MET B C   1 
ATOM   4968  O  O   . MET B  1 69  ? 25.645  0.678   33.845  1.00 27.34 ? 86   MET B O   1 
ATOM   4969  C  CB  . MET B  1 69  ? 27.523  2.531   35.596  1.00 26.66 ? 86   MET B CB  1 
ATOM   4970  C  CG  . MET B  1 69  ? 27.606  3.856   36.343  1.00 26.24 ? 86   MET B CG  1 
ATOM   4971  S  SD  . MET B  1 69  ? 26.148  4.904   36.156  1.00 26.68 ? 86   MET B SD  1 
ATOM   4972  C  CE  . MET B  1 69  ? 26.141  5.090   34.368  1.00 26.81 ? 86   MET B CE  1 
ATOM   4973  N  N   . GLY B  1 70  ? 26.563  -0.660  35.411  1.00 27.80 ? 87   GLY B N   1 
ATOM   4974  C  CA  . GLY B  1 70  ? 26.373  -1.889  34.658  1.00 28.77 ? 87   GLY B CA  1 
ATOM   4975  C  C   . GLY B  1 70  ? 24.896  -2.187  34.397  1.00 29.55 ? 87   GLY B C   1 
ATOM   4976  O  O   . GLY B  1 70  ? 24.549  -2.745  33.358  1.00 32.08 ? 87   GLY B O   1 
ATOM   4977  N  N   . ILE B  1 71  ? 24.030  -1.801  35.340  1.00 29.62 ? 88   ILE B N   1 
ATOM   4978  C  CA  . ILE B  1 71  ? 22.600  -2.045  35.223  1.00 28.70 ? 88   ILE B CA  1 
ATOM   4979  C  C   . ILE B  1 71  ? 22.022  -1.182  34.102  1.00 28.40 ? 88   ILE B C   1 
ATOM   4980  O  O   . ILE B  1 71  ? 21.118  -1.626  33.396  1.00 28.64 ? 88   ILE B O   1 
ATOM   4981  C  CB  . ILE B  1 71  ? 21.891  -1.818  36.573  1.00 29.00 ? 88   ILE B CB  1 
ATOM   4982  C  CG1 . ILE B  1 71  ? 22.532  -2.663  37.673  1.00 29.98 ? 88   ILE B CG1 1 
ATOM   4983  C  CG2 . ILE B  1 71  ? 20.389  -2.087  36.465  1.00 29.01 ? 88   ILE B CG2 1 
ATOM   4984  C  CD1 . ILE B  1 71  ? 21.953  -2.444  39.058  1.00 30.72 ? 88   ILE B CD1 1 
ATOM   4985  N  N   . GLN B  1 72  ? 22.563  0.029   33.905  1.00 28.63 ? 89   GLN B N   1 
ATOM   4986  C  CA  . GLN B  1 72  ? 22.089  0.906   32.840  1.00 28.90 ? 89   GLN B CA  1 
ATOM   4987  C  C   . GLN B  1 72  ? 22.219  0.209   31.484  1.00 29.14 ? 89   GLN B C   1 
ATOM   4988  O  O   . GLN B  1 72  ? 21.368  0.397   30.612  1.00 29.04 ? 89   GLN B O   1 
ATOM   4989  C  CB  . GLN B  1 72  ? 22.824  2.249   32.820  1.00 29.85 ? 89   GLN B CB  1 
ATOM   4990  C  CG  . GLN B  1 72  ? 22.313  3.220   31.761  1.00 31.29 ? 89   GLN B CG  1 
ATOM   4991  C  CD  . GLN B  1 72  ? 23.180  4.450   31.599  1.00 34.00 ? 89   GLN B CD  1 
ATOM   4992  O  OE1 . GLN B  1 72  ? 24.409  4.366   31.516  1.00 34.45 ? 89   GLN B OE1 1 
ATOM   4993  N  NE2 . GLN B  1 72  ? 22.546  5.613   31.552  1.00 35.52 ? 89   GLN B NE2 1 
ATOM   4994  N  N   . GLU B  1 73  ? 23.275  -0.599  31.313  1.00 28.83 ? 90   GLU B N   1 
ATOM   4995  C  CA  . GLU B  1 73  ? 23.529  -1.286  30.051  1.00 31.19 ? 90   GLU B CA  1 
ATOM   4996  C  C   . GLU B  1 73  ? 22.706  -2.572  29.919  1.00 29.47 ? 90   GLU B C   1 
ATOM   4997  O  O   . GLU B  1 73  ? 22.775  -3.229  28.880  1.00 30.17 ? 90   GLU B O   1 
ATOM   4998  C  CB  . GLU B  1 73  ? 25.013  -1.636  29.881  1.00 35.28 ? 90   GLU B CB  1 
ATOM   4999  C  CG  . GLU B  1 73  ? 25.863  -0.489  29.339  1.00 39.94 ? 90   GLU B CG  1 
ATOM   5000  C  CD  . GLU B  1 73  ? 27.250  -0.870  28.825  1.00 45.14 ? 90   GLU B CD  1 
ATOM   5001  O  OE1 . GLU B  1 73  ? 28.222  -0.411  29.476  1.00 49.32 ? 90   GLU B OE1 1 
ATOM   5002  O  OE2 . GLU B  1 73  ? 27.377  -1.595  27.796  1.00 40.90 ? 90   GLU B OE2 1 
ATOM   5003  N  N   . ARG B  1 74  ? 21.938  -2.940  30.956  1.00 27.17 ? 91   ARG B N   1 
ATOM   5004  C  CA  . ARG B  1 74  ? 21.203  -4.199  30.956  1.00 26.52 ? 91   ARG B CA  1 
ATOM   5005  C  C   . ARG B  1 74  ? 19.691  -3.982  31.009  1.00 23.76 ? 91   ARG B C   1 
ATOM   5006  O  O   . ARG B  1 74  ? 18.957  -4.635  30.271  1.00 24.07 ? 91   ARG B O   1 
ATOM   5007  C  CB  . ARG B  1 74  ? 21.640  -5.067  32.140  1.00 29.16 ? 91   ARG B CB  1 
ATOM   5008  C  CG  . ARG B  1 74  ? 23.096  -5.498  32.063  1.00 32.03 ? 91   ARG B CG  1 
ATOM   5009  C  CD  . ARG B  1 74  ? 23.481  -6.447  33.186  1.00 35.03 ? 91   ARG B CD  1 
ATOM   5010  N  NE  . ARG B  1 74  ? 24.838  -6.967  32.970  1.00 38.24 ? 91   ARG B NE  1 
ATOM   5011  C  CZ  . ARG B  1 74  ? 25.196  -8.244  32.837  1.00 42.33 ? 91   ARG B CZ  1 
ATOM   5012  N  NH1 . ARG B  1 74  ? 24.304  -9.218  32.927  1.00 41.99 ? 91   ARG B NH1 1 
ATOM   5013  N  NH2 . ARG B  1 74  ? 26.469  -8.545  32.616  1.00 45.15 ? 91   ARG B NH2 1 
ATOM   5014  N  N   . ASN B  1 75  ? 19.240  -3.101  31.908  1.00 22.69 ? 92   ASN B N   1 
ATOM   5015  C  CA  . ASN B  1 75  ? 17.823  -2.904  32.179  1.00 21.78 ? 92   ASN B CA  1 
ATOM   5016  C  C   . ASN B  1 75  ? 17.608  -1.456  32.615  1.00 21.26 ? 92   ASN B C   1 
ATOM   5017  O  O   . ASN B  1 75  ? 17.793  -1.116  33.780  1.00 20.69 ? 92   ASN B O   1 
ATOM   5018  C  CB  . ASN B  1 75  ? 17.335  -3.915  33.212  1.00 21.11 ? 92   ASN B CB  1 
ATOM   5019  C  CG  . ASN B  1 75  ? 15.853  -3.821  33.497  1.00 21.82 ? 92   ASN B CG  1 
ATOM   5020  O  OD1 . ASN B  1 75  ? 15.214  -2.783  33.256  1.00 21.02 ? 92   ASN B OD1 1 
ATOM   5021  N  ND2 . ASN B  1 75  ? 15.295  -4.896  34.036  1.00 21.89 ? 92   ASN B ND2 1 
ATOM   5022  N  N   . GLU B  1 76  ? 17.195  -0.619  31.657  1.00 23.35 ? 93   GLU B N   1 
ATOM   5023  C  CA  . GLU B  1 76  ? 17.138  0.823   31.839  1.00 24.71 ? 93   GLU B CA  1 
ATOM   5024  C  C   . GLU B  1 76  ? 16.137  1.204   32.925  1.00 22.94 ? 93   GLU B C   1 
ATOM   5025  O  O   . GLU B  1 76  ? 16.423  2.058   33.760  1.00 21.36 ? 93   GLU B O   1 
ATOM   5026  C  CB  . GLU B  1 76  ? 16.763  1.455   30.500  1.00 28.43 ? 93   GLU B CB  1 
ATOM   5027  C  CG  . GLU B  1 76  ? 16.744  2.978   30.516  1.00 31.31 ? 93   GLU B CG  1 
ATOM   5028  C  CD  . GLU B  1 76  ? 16.622  3.537   29.113  1.00 33.49 ? 93   GLU B CD  1 
ATOM   5029  O  OE1 . GLU B  1 76  ? 15.493  3.597   28.579  1.00 36.39 ? 93   GLU B OE1 1 
ATOM   5030  O  OE2 . GLU B  1 76  ? 17.681  3.867   28.544  1.00 34.88 ? 93   GLU B OE2 1 
ATOM   5031  N  N   . LYS B  1 77  ? 14.955  0.577   32.909  1.00 22.25 ? 94   LYS B N   1 
ATOM   5032  C  CA  . LYS B  1 77  ? 13.907  0.940   33.850  1.00 21.96 ? 94   LYS B CA  1 
ATOM   5033  C  C   . LYS B  1 77  ? 14.303  0.549   35.271  1.00 22.02 ? 94   LYS B C   1 
ATOM   5034  O  O   . LYS B  1 77  ? 14.065  1.315   36.202  1.00 21.73 ? 94   LYS B O   1 
ATOM   5035  C  CB  . LYS B  1 77  ? 12.553  0.380   33.407  1.00 22.84 ? 94   LYS B CB  1 
ATOM   5036  C  CG  . LYS B  1 77  ? 11.973  1.172   32.248  1.00 23.62 ? 94   LYS B CG  1 
ATOM   5037  C  CD  . LYS B  1 77  ? 10.510  0.905   31.951  1.00 25.40 ? 94   LYS B CD  1 
ATOM   5038  C  CE  . LYS B  1 77  ? 9.923   2.006   31.129  1.00 26.78 ? 94   LYS B CE  1 
ATOM   5039  N  NZ  . LYS B  1 77  ? 8.660   1.566   30.538  1.00 27.78 ? 94   LYS B NZ  1 
ATOM   5040  N  N   . LEU B  1 78  ? 14.932  -0.622  35.434  1.00 21.93 ? 95   LEU B N   1 
ATOM   5041  C  CA  . LEU B  1 78  ? 15.436  -1.029  36.737  1.00 22.08 ? 95   LEU B CA  1 
ATOM   5042  C  C   . LEU B  1 78  ? 16.473  -0.024  37.243  1.00 21.98 ? 95   LEU B C   1 
ATOM   5043  O  O   . LEU B  1 78  ? 16.446  0.351   38.412  1.00 22.22 ? 95   LEU B O   1 
ATOM   5044  C  CB  . LEU B  1 78  ? 16.014  -2.442  36.661  1.00 22.50 ? 95   LEU B CB  1 
ATOM   5045  C  CG  . LEU B  1 78  ? 16.544  -3.035  37.971  1.00 22.67 ? 95   LEU B CG  1 
ATOM   5046  C  CD1 . LEU B  1 78  ? 15.517  -3.018  39.097  1.00 23.40 ? 95   LEU B CD1 1 
ATOM   5047  C  CD2 . LEU B  1 78  ? 17.028  -4.458  37.718  1.00 22.94 ? 95   LEU B CD2 1 
ATOM   5048  N  N   . PHE B  1 79  ? 17.388  0.391   36.356  1.00 22.40 ? 96   PHE B N   1 
ATOM   5049  C  CA  . PHE B  1 79  ? 18.447  1.330   36.696  1.00 22.44 ? 96   PHE B CA  1 
ATOM   5050  C  C   . PHE B  1 79  ? 17.847  2.603   37.296  1.00 22.36 ? 96   PHE B C   1 
ATOM   5051  O  O   . PHE B  1 79  ? 18.262  3.029   38.370  1.00 22.56 ? 96   PHE B O   1 
ATOM   5052  C  CB  . PHE B  1 79  ? 19.317  1.590   35.459  1.00 22.76 ? 96   PHE B CB  1 
ATOM   5053  C  CG  . PHE B  1 79  ? 20.337  2.709   35.635  1.00 23.08 ? 96   PHE B CG  1 
ATOM   5054  C  CD1 . PHE B  1 79  ? 21.523  2.492   36.331  1.00 23.90 ? 96   PHE B CD1 1 
ATOM   5055  C  CD2 . PHE B  1 79  ? 20.108  3.975   35.106  1.00 24.66 ? 96   PHE B CD2 1 
ATOM   5056  C  CE1 . PHE B  1 79  ? 22.446  3.513   36.495  1.00 23.26 ? 96   PHE B CE1 1 
ATOM   5057  C  CE2 . PHE B  1 79  ? 21.038  4.994   35.268  1.00 24.19 ? 96   PHE B CE2 1 
ATOM   5058  C  CZ  . PHE B  1 79  ? 22.203  4.759   35.966  1.00 23.93 ? 96   PHE B CZ  1 
ATOM   5059  N  N   . TYR B  1 80  ? 16.845  3.187   36.626  1.00 22.72 ? 97   TYR B N   1 
ATOM   5060  C  CA  . TYR B  1 80  ? 16.257  4.443   37.078  1.00 22.32 ? 97   TYR B CA  1 
ATOM   5061  C  C   . TYR B  1 80  ? 15.414  4.220   38.334  1.00 23.10 ? 97   TYR B C   1 
ATOM   5062  O  O   . TYR B  1 80  ? 15.389  5.085   39.212  1.00 21.93 ? 97   TYR B O   1 
ATOM   5063  C  CB  . TYR B  1 80  ? 15.529  5.151   35.928  1.00 22.36 ? 97   TYR B CB  1 
ATOM   5064  C  CG  . TYR B  1 80  ? 16.540  5.745   34.958  1.00 22.94 ? 97   TYR B CG  1 
ATOM   5065  C  CD1 . TYR B  1 80  ? 17.360  6.795   35.356  1.00 23.81 ? 97   TYR B CD1 1 
ATOM   5066  C  CD2 . TYR B  1 80  ? 16.716  5.237   33.676  1.00 22.90 ? 97   TYR B CD2 1 
ATOM   5067  C  CE1 . TYR B  1 80  ? 18.319  7.324   34.509  1.00 23.76 ? 97   TYR B CE1 1 
ATOM   5068  C  CE2 . TYR B  1 80  ? 17.672  5.761   32.818  1.00 24.02 ? 97   TYR B CE2 1 
ATOM   5069  C  CZ  . TYR B  1 80  ? 18.474  6.808   33.238  1.00 24.31 ? 97   TYR B CZ  1 
ATOM   5070  O  OH  . TYR B  1 80  ? 19.430  7.341   32.422  1.00 27.46 ? 97   TYR B OH  1 
ATOM   5071  N  N   . ARG B  1 81  ? 14.758  3.056   38.440  1.00 23.18 ? 98   ARG B N   1 
ATOM   5072  C  CA  . ARG B  1 81  ? 14.021  2.704   39.648  1.00 24.15 ? 98   ARG B CA  1 
ATOM   5073  C  C   . ARG B  1 81  ? 14.947  2.734   40.865  1.00 24.61 ? 98   ARG B C   1 
ATOM   5074  O  O   . ARG B  1 81  ? 14.593  3.291   41.901  1.00 25.21 ? 98   ARG B O   1 
ATOM   5075  C  CB  . ARG B  1 81  ? 13.353  1.329   39.516  1.00 25.22 ? 98   ARG B CB  1 
ATOM   5076  C  CG  . ARG B  1 81  ? 12.761  0.751   40.798  1.00 26.25 ? 98   ARG B CG  1 
ATOM   5077  C  CD  . ARG B  1 81  ? 11.667  1.626   41.392  1.00 27.63 ? 98   ARG B CD  1 
ATOM   5078  N  NE  . ARG B  1 81  ? 11.155  1.117   42.670  1.00 29.74 ? 98   ARG B NE  1 
ATOM   5079  C  CZ  . ARG B  1 81  ? 10.295  0.112   42.848  1.00 30.02 ? 98   ARG B CZ  1 
ATOM   5080  N  NH1 . ARG B  1 81  ? 9.777   -0.532  41.817  1.00 28.93 ? 98   ARG B NH1 1 
ATOM   5081  N  NH2 . ARG B  1 81  ? 9.939   -0.237  44.074  1.00 31.72 ? 98   ARG B NH2 1 
ATOM   5082  N  N   . ILE B  1 82  ? 16.123  2.110   40.722  1.00 25.67 ? 99   ILE B N   1 
ATOM   5083  C  CA  . ILE B  1 82  ? 17.098  1.957   41.792  1.00 27.71 ? 99   ILE B CA  1 
ATOM   5084  C  C   . ILE B  1 82  ? 17.613  3.324   42.242  1.00 27.14 ? 99   ILE B C   1 
ATOM   5085  O  O   . ILE B  1 82  ? 17.770  3.582   43.436  1.00 26.35 ? 99   ILE B O   1 
ATOM   5086  C  CB  . ILE B  1 82  ? 18.230  1.033   41.303  1.00 30.59 ? 99   ILE B CB  1 
ATOM   5087  C  CG1 . ILE B  1 82  ? 17.861  -0.435  41.507  1.00 32.11 ? 99   ILE B CG1 1 
ATOM   5088  C  CG2 . ILE B  1 82  ? 19.569  1.383   41.945  1.00 32.49 ? 99   ILE B CG2 1 
ATOM   5089  C  CD1 . ILE B  1 82  ? 18.671  -1.392  40.650  1.00 34.05 ? 99   ILE B CD1 1 
ATOM   5090  N  N   . LEU B  1 83  ? 17.878  4.192   41.266  1.00 27.73 ? 100  LEU B N   1 
ATOM   5091  C  CA  . LEU B  1 83  ? 18.397  5.522   41.527  1.00 28.14 ? 100  LEU B CA  1 
ATOM   5092  C  C   . LEU B  1 83  ? 17.337  6.354   42.248  1.00 28.29 ? 100  LEU B C   1 
ATOM   5093  O  O   . LEU B  1 83  ? 17.629  6.998   43.252  1.00 26.11 ? 100  LEU B O   1 
ATOM   5094  C  CB  . LEU B  1 83  ? 18.816  6.092   40.174  1.00 29.44 ? 100  LEU B CB  1 
ATOM   5095  C  CG  . LEU B  1 83  ? 19.516  7.452   40.164  1.00 32.35 ? 100  LEU B CG  1 
ATOM   5096  C  CD1 . LEU B  1 83  ? 20.611  7.577   41.209  1.00 34.38 ? 100  LEU B CD1 1 
ATOM   5097  C  CD2 . LEU B  1 83  ? 20.081  7.661   38.765  1.00 32.79 ? 100  LEU B CD2 1 
ATOM   5098  N  N   . GLN B  1 84  ? 16.093  6.293   41.763  1.00 28.28 ? 101  GLN B N   1 
ATOM   5099  C  CA  . GLN B  1 84  ? 14.991  7.038   42.354  1.00 29.53 ? 101  GLN B CA  1 
ATOM   5100  C  C   . GLN B  1 84  ? 14.722  6.569   43.784  1.00 29.62 ? 101  GLN B C   1 
ATOM   5101  O  O   . GLN B  1 84  ? 14.447  7.392   44.654  1.00 29.08 ? 101  GLN B O   1 
ATOM   5102  C  CB  . GLN B  1 84  ? 13.756  6.925   41.460  1.00 30.66 ? 101  GLN B CB  1 
ATOM   5103  C  CG  . GLN B  1 84  ? 13.872  7.728   40.168  1.00 31.22 ? 101  GLN B CG  1 
ATOM   5104  C  CD  . GLN B  1 84  ? 12.828  7.385   39.126  1.00 32.25 ? 101  GLN B CD  1 
ATOM   5105  O  OE1 . GLN B  1 84  ? 12.135  6.363   39.204  1.00 31.11 ? 101  GLN B OE1 1 
ATOM   5106  N  NE2 . GLN B  1 84  ? 12.718  8.246   38.123  1.00 32.19 ? 101  GLN B NE2 1 
ATOM   5107  N  N   . ASP B  1 85  ? 14.810  5.252   44.021  1.00 30.31 ? 102  ASP B N   1 
ATOM   5108  C  CA  . ASP B  1 85  ? 14.553  4.677   45.333  1.00 31.36 ? 102  ASP B CA  1 
ATOM   5109  C  C   . ASP B  1 85  ? 15.465  5.302   46.387  1.00 32.42 ? 102  ASP B C   1 
ATOM   5110  O  O   . ASP B  1 85  ? 15.011  5.598   47.486  1.00 33.60 ? 102  ASP B O   1 
ATOM   5111  C  CB  . ASP B  1 85  ? 14.811  3.177   45.370  1.00 32.62 ? 102  ASP B CB  1 
ATOM   5112  C  CG  . ASP B  1 85  ? 13.742  2.262   44.788  1.00 33.49 ? 102  ASP B CG  1 
ATOM   5113  O  OD1 . ASP B  1 85  ? 12.613  2.738   44.547  1.00 31.84 ? 102  ASP B OD1 1 
ATOM   5114  O  OD2 . ASP B  1 85  ? 14.061  1.067   44.580  1.00 34.06 ? 102  ASP B OD2 1 
ATOM   5115  N  N   . ASP B  1 86  ? 16.752  5.461   46.045  1.00 32.11 ? 103  ASP B N   1 
ATOM   5116  C  CA  . ASP B  1 86  ? 17.788  5.797   47.007  1.00 33.04 ? 103  ASP B CA  1 
ATOM   5117  C  C   . ASP B  1 86  ? 18.572  7.001   46.490  1.00 32.32 ? 103  ASP B C   1 
ATOM   5118  O  O   . ASP B  1 86  ? 19.800  6.997   46.483  1.00 32.29 ? 103  ASP B O   1 
ATOM   5119  C  CB  . ASP B  1 86  ? 18.695  4.599   47.242  1.00 34.39 ? 103  ASP B CB  1 
ATOM   5120  C  CG  . ASP B  1 86  ? 19.537  4.636   48.509  1.00 35.44 ? 103  ASP B CG  1 
ATOM   5121  O  OD1 . ASP B  1 86  ? 19.150  5.365   49.446  1.00 35.20 ? 103  ASP B OD1 1 
ATOM   5122  O  OD2 . ASP B  1 86  ? 20.586  3.947   48.537  1.00 36.45 ? 103  ASP B OD2 1 
ATOM   5123  N  N   . ILE B  1 87  ? 17.839  8.042   46.085  1.00 32.30 ? 104  ILE B N   1 
ATOM   5124  C  CA  . ILE B  1 87  ? 18.389  9.103   45.256  1.00 32.13 ? 104  ILE B CA  1 
ATOM   5125  C  C   . ILE B  1 87  ? 19.424  9.923   46.032  1.00 30.48 ? 104  ILE B C   1 
ATOM   5126  O  O   . ILE B  1 87  ? 20.467  10.266  45.482  1.00 29.30 ? 104  ILE B O   1 
ATOM   5127  C  CB  . ILE B  1 87  ? 17.253  9.962   44.660  1.00 33.36 ? 104  ILE B CB  1 
ATOM   5128  C  CG1 . ILE B  1 87  ? 17.767  10.930  43.597  1.00 34.42 ? 104  ILE B CG1 1 
ATOM   5129  C  CG2 . ILE B  1 87  ? 16.447  10.691  45.740  1.00 34.34 ? 104  ILE B CG2 1 
ATOM   5130  C  CD1 . ILE B  1 87  ? 18.246  10.259  42.322  1.00 35.62 ? 104  ILE B CD1 1 
ATOM   5131  N  N   . GLU B  1 88  ? 19.157  10.221  47.308  1.00 30.98 ? 105  GLU B N   1 
ATOM   5132  C  CA  . GLU B  1 88  ? 20.058  11.066  48.077  1.00 32.29 ? 105  GLU B CA  1 
ATOM   5133  C  C   . GLU B  1 88  ? 21.420  10.388  48.219  1.00 30.30 ? 105  GLU B C   1 
ATOM   5134  O  O   . GLU B  1 88  ? 22.446  11.047  48.075  1.00 29.07 ? 105  GLU B O   1 
ATOM   5135  C  CB  . GLU B  1 88  ? 19.475  11.469  49.432  1.00 34.49 ? 105  GLU B CB  1 
ATOM   5136  C  CG  . GLU B  1 88  ? 20.372  12.462  50.167  1.00 36.72 ? 105  GLU B CG  1 
ATOM   5137  C  CD  . GLU B  1 88  ? 19.807  13.091  51.427  1.00 37.05 ? 105  GLU B CD  1 
ATOM   5138  O  OE1 . GLU B  1 88  ? 18.668  12.765  51.821  1.00 37.69 ? 105  GLU B OE1 1 
ATOM   5139  O  OE2 . GLU B  1 88  ? 20.534  13.925  52.009  1.00 37.17 ? 105  GLU B OE2 1 
ATOM   5140  N  N   . SER B  1 89  ? 21.424  9.071   48.456  1.00 30.50 ? 106  SER B N   1 
ATOM   5141  C  CA  . SER B  1 89  ? 22.654  8.319   48.664  1.00 30.80 ? 106  SER B CA  1 
ATOM   5142  C  C   . SER B  1 89  ? 23.370  7.982   47.359  1.00 29.85 ? 106  SER B C   1 
ATOM   5143  O  O   . SER B  1 89  ? 24.576  7.758   47.385  1.00 28.64 ? 106  SER B O   1 
ATOM   5144  C  CB  . SER B  1 89  ? 22.398  7.057   49.441  1.00 31.45 ? 106  SER B CB  1 
ATOM   5145  O  OG  . SER B  1 89  ? 22.060  7.367   50.785  1.00 34.68 ? 106  SER B OG  1 
ATOM   5146  N  N   . LEU B  1 90  ? 22.648  7.921   46.229  1.00 30.35 ? 107  LEU B N   1 
ATOM   5147  C  CA  . LEU B  1 90  ? 23.226  7.400   44.996  1.00 31.13 ? 107  LEU B CA  1 
ATOM   5148  C  C   . LEU B  1 90  ? 23.652  8.514   44.036  1.00 31.33 ? 107  LEU B C   1 
ATOM   5149  O  O   . LEU B  1 90  ? 24.477  8.265   43.156  1.00 29.87 ? 107  LEU B O   1 
ATOM   5150  C  CB  . LEU B  1 90  ? 22.255  6.428   44.328  1.00 32.55 ? 107  LEU B CB  1 
ATOM   5151  C  CG  . LEU B  1 90  ? 22.048  5.088   45.042  1.00 32.84 ? 107  LEU B CG  1 
ATOM   5152  C  CD1 . LEU B  1 90  ? 21.024  4.251   44.310  1.00 33.16 ? 107  LEU B CD1 1 
ATOM   5153  C  CD2 . LEU B  1 90  ? 23.341  4.308   45.182  1.00 34.20 ? 107  LEU B CD2 1 
ATOM   5154  N  N   . MET B  1 91  ? 23.115  9.732   44.204  1.00 33.45 ? 108  MET B N   1 
ATOM   5155  C  CA  . MET B  1 91  ? 23.511  10.865  43.374  1.00 34.17 ? 108  MET B CA  1 
ATOM   5156  C  C   . MET B  1 91  ? 25.027  11.067  43.460  1.00 34.16 ? 108  MET B C   1 
ATOM   5157  O  O   . MET B  1 91  ? 25.665  11.237  42.424  1.00 34.13 ? 108  MET B O   1 
ATOM   5158  C  CB  . MET B  1 91  ? 22.717  12.138  43.718  1.00 35.05 ? 108  MET B CB  1 
ATOM   5159  C  CG  . MET B  1 91  ? 21.311  12.154  43.108  1.00 36.43 ? 108  MET B CG  1 
ATOM   5160  S  SD  . MET B  1 91  ? 20.339  13.674  43.240  1.00 38.70 ? 108  MET B SD  1 
ATOM   5161  C  CE  . MET B  1 91  ? 20.225  13.907  45.020  1.00 37.07 ? 108  MET B CE  1 
ATOM   5162  N  N   . PRO B  1 92  ? 25.665  11.010  44.660  1.00 34.24 ? 109  PRO B N   1 
ATOM   5163  C  CA  . PRO B  1 92  ? 27.122  11.143  44.772  1.00 34.47 ? 109  PRO B CA  1 
ATOM   5164  C  C   . PRO B  1 92  ? 27.949  9.972   44.239  1.00 34.46 ? 109  PRO B C   1 
ATOM   5165  O  O   . PRO B  1 92  ? 29.172  10.075  44.158  1.00 33.23 ? 109  PRO B O   1 
ATOM   5166  C  CB  . PRO B  1 92  ? 27.389  11.354  46.281  1.00 34.69 ? 109  PRO B CB  1 
ATOM   5167  C  CG  . PRO B  1 92  ? 26.028  11.458  46.931  1.00 34.55 ? 109  PRO B CG  1 
ATOM   5168  C  CD  . PRO B  1 92  ? 25.029  10.838  45.973  1.00 34.55 ? 109  PRO B CD  1 
ATOM   5169  N  N   . ILE B  1 93  ? 27.283  8.856   43.911  1.00 33.93 ? 110  ILE B N   1 
ATOM   5170  C  CA  . ILE B  1 93  ? 27.938  7.700   43.317  1.00 33.15 ? 110  ILE B CA  1 
ATOM   5171  C  C   . ILE B  1 93  ? 27.918  7.828   41.794  1.00 30.71 ? 110  ILE B C   1 
ATOM   5172  O  O   . ILE B  1 93  ? 28.944  7.641   41.145  1.00 29.81 ? 110  ILE B O   1 
ATOM   5173  C  CB  . ILE B  1 93  ? 27.269  6.388   43.774  1.00 34.78 ? 110  ILE B CB  1 
ATOM   5174  C  CG1 . ILE B  1 93  ? 27.231  6.258   45.299  1.00 36.93 ? 110  ILE B CG1 1 
ATOM   5175  C  CG2 . ILE B  1 93  ? 27.946  5.181   43.124  1.00 35.10 ? 110  ILE B CG2 1 
ATOM   5176  C  CD1 . ILE B  1 93  ? 28.598  6.182   45.956  1.00 37.42 ? 110  ILE B CD1 1 
ATOM   5177  N  N   . VAL B  1 94  ? 26.743  8.115   41.222  1.00 29.10 ? 111  VAL B N   1 
ATOM   5178  C  CA  . VAL B  1 94  ? 26.606  8.145   39.772  1.00 29.53 ? 111  VAL B CA  1 
ATOM   5179  C  C   . VAL B  1 94  ? 27.163  9.463   39.234  1.00 28.63 ? 111  VAL B C   1 
ATOM   5180  O  O   . VAL B  1 94  ? 27.540  9.531   38.067  1.00 27.17 ? 111  VAL B O   1 
ATOM   5181  C  CB  . VAL B  1 94  ? 25.173  7.905   39.252  1.00 29.40 ? 111  VAL B CB  1 
ATOM   5182  C  CG1 . VAL B  1 94  ? 24.644  6.533   39.662  1.00 29.44 ? 111  VAL B CG1 1 
ATOM   5183  C  CG2 . VAL B  1 94  ? 24.208  9.006   39.668  1.00 30.10 ? 111  VAL B CG2 1 
ATOM   5184  N  N   . TYR B  1 95  ? 27.207  10.506  40.073  1.00 30.49 ? 112  TYR B N   1 
ATOM   5185  C  CA  . TYR B  1 95  ? 27.746  11.789  39.646  1.00 32.41 ? 112  TYR B CA  1 
ATOM   5186  C  C   . TYR B  1 95  ? 28.882  12.196  40.585  1.00 34.53 ? 112  TYR B C   1 
ATOM   5187  O  O   . TYR B  1 95  ? 29.564  11.335  41.144  1.00 34.10 ? 112  TYR B O   1 
ATOM   5188  C  CB  . TYR B  1 95  ? 26.584  12.783  39.519  1.00 32.04 ? 112  TYR B CB  1 
ATOM   5189  C  CG  . TYR B  1 95  ? 26.946  14.040  38.742  1.00 32.87 ? 112  TYR B CG  1 
ATOM   5190  C  CD1 . TYR B  1 95  ? 27.639  13.965  37.535  1.00 33.12 ? 112  TYR B CD1 1 
ATOM   5191  C  CD2 . TYR B  1 95  ? 26.654  15.302  39.247  1.00 34.57 ? 112  TYR B CD2 1 
ATOM   5192  C  CE1 . TYR B  1 95  ? 28.002  15.105  36.840  1.00 33.92 ? 112  TYR B CE1 1 
ATOM   5193  C  CE2 . TYR B  1 95  ? 27.009  16.449  38.558  1.00 35.67 ? 112  TYR B CE2 1 
ATOM   5194  C  CZ  . TYR B  1 95  ? 27.691  16.346  37.358  1.00 35.53 ? 112  TYR B CZ  1 
ATOM   5195  O  OH  . TYR B  1 95  ? 28.044  17.468  36.679  1.00 41.55 ? 112  TYR B OH  1 
ATOM   5196  N  N   A THR B  1 96  ? 29.086  13.514  40.726  0.50 34.18 ? 113  THR B N   1 
ATOM   5197  N  N   B THR B  1 96  ? 29.087  13.511  40.733  0.50 34.13 ? 113  THR B N   1 
ATOM   5198  C  CA  A THR B  1 96  ? 30.155  14.082  41.532  0.50 34.65 ? 113  THR B CA  1 
ATOM   5199  C  CA  B THR B  1 96  ? 30.191  14.044  41.514  0.50 34.60 ? 113  THR B CA  1 
ATOM   5200  C  C   A THR B  1 96  ? 29.899  13.756  43.002  0.50 34.92 ? 113  THR B C   1 
ATOM   5201  C  C   B THR B  1 96  ? 29.915  13.783  42.994  0.50 34.88 ? 113  THR B C   1 
ATOM   5202  O  O   A THR B  1 96  ? 28.756  13.829  43.445  0.50 35.72 ? 113  THR B O   1 
ATOM   5203  O  O   B THR B  1 96  ? 28.776  13.925  43.433  0.50 35.79 ? 113  THR B O   1 
ATOM   5204  C  CB  A THR B  1 96  ? 30.210  15.595  41.306  0.50 35.14 ? 113  THR B CB  1 
ATOM   5205  C  CB  B THR B  1 96  ? 30.346  15.535  41.207  0.50 34.92 ? 113  THR B CB  1 
ATOM   5206  O  OG1 A THR B  1 96  ? 30.568  15.794  39.942  0.50 34.31 ? 113  THR B OG1 1 
ATOM   5207  O  OG1 B THR B  1 96  ? 31.639  15.917  41.664  0.50 35.48 ? 113  THR B OG1 1 
ATOM   5208  C  CG2 A THR B  1 96  ? 31.222  16.285  42.202  0.50 35.68 ? 113  THR B CG2 1 
ATOM   5209  C  CG2 B THR B  1 96  ? 29.282  16.387  41.877  0.50 34.50 ? 113  THR B CG2 1 
ATOM   5210  N  N   . PRO B  1 97  ? 30.922  13.405  43.821  1.00 35.44 ? 114  PRO B N   1 
ATOM   5211  C  CA  . PRO B  1 97  ? 32.317  13.251  43.369  1.00 35.15 ? 114  PRO B CA  1 
ATOM   5212  C  C   . PRO B  1 97  ? 32.897  11.943  42.817  1.00 35.00 ? 114  PRO B C   1 
ATOM   5213  O  O   . PRO B  1 97  ? 34.070  11.922  42.448  1.00 36.51 ? 114  PRO B O   1 
ATOM   5214  C  CB  . PRO B  1 97  ? 33.020  13.601  44.698  1.00 35.70 ? 114  PRO B CB  1 
ATOM   5215  C  CG  . PRO B  1 97  ? 32.168  12.945  45.757  1.00 36.62 ? 114  PRO B CG  1 
ATOM   5216  C  CD  . PRO B  1 97  ? 30.759  13.189  45.268  1.00 36.21 ? 114  PRO B CD  1 
ATOM   5217  N  N   . THR B  1 98  ? 32.110  10.860  42.753  1.00 33.99 ? 115  THR B N   1 
ATOM   5218  C  CA  . THR B  1 98  ? 32.664  9.543   42.451  1.00 33.81 ? 115  THR B CA  1 
ATOM   5219  C  C   . THR B  1 98  ? 33.003  9.413   40.963  1.00 34.03 ? 115  THR B C   1 
ATOM   5220  O  O   . THR B  1 98  ? 34.054  8.875   40.609  1.00 33.97 ? 115  THR B O   1 
ATOM   5221  C  CB  . THR B  1 98  ? 31.684  8.453   42.887  1.00 34.81 ? 115  THR B CB  1 
ATOM   5222  O  OG1 . THR B  1 98  ? 31.443  8.658   44.276  1.00 34.40 ? 115  THR B OG1 1 
ATOM   5223  C  CG2 . THR B  1 98  ? 32.228  7.051   42.668  1.00 34.25 ? 115  THR B CG2 1 
ATOM   5224  N  N   . VAL B  1 99  ? 32.098  9.889   40.097  1.00 32.81 ? 116  VAL B N   1 
ATOM   5225  C  CA  . VAL B  1 99  ? 32.131  9.585   38.674  1.00 32.65 ? 116  VAL B CA  1 
ATOM   5226  C  C   . VAL B  1 99  ? 33.521  9.832   38.086  1.00 33.01 ? 116  VAL B C   1 
ATOM   5227  O  O   . VAL B  1 99  ? 33.997  9.023   37.293  1.00 33.30 ? 116  VAL B O   1 
ATOM   5228  C  CB  . VAL B  1 99  ? 31.052  10.372  37.901  1.00 33.24 ? 116  VAL B CB  1 
ATOM   5229  C  CG1 . VAL B  1 99  ? 31.215  11.883  38.041  1.00 32.69 ? 116  VAL B CG1 1 
ATOM   5230  C  CG2 . VAL B  1 99  ? 30.999  9.969   36.432  1.00 33.31 ? 116  VAL B CG2 1 
ATOM   5231  N  N   . GLY B  1 100 ? 34.161  10.947  38.463  1.00 33.62 ? 117  GLY B N   1 
ATOM   5232  C  CA  . GLY B  1 100 ? 35.423  11.358  37.861  1.00 35.64 ? 117  GLY B CA  1 
ATOM   5233  C  C   . GLY B  1 100 ? 36.579  10.407  38.179  1.00 36.60 ? 117  GLY B C   1 
ATOM   5234  O  O   . GLY B  1 100 ? 37.550  10.344  37.430  1.00 38.70 ? 117  GLY B O   1 
ATOM   5235  N  N   . LEU B  1 101 ? 36.470  9.666   39.288  1.00 37.76 ? 118  LEU B N   1 
ATOM   5236  C  CA  . LEU B  1 101 ? 37.513  8.746   39.718  1.00 37.70 ? 118  LEU B CA  1 
ATOM   5237  C  C   . LEU B  1 101 ? 37.505  7.458   38.886  1.00 38.80 ? 118  LEU B C   1 
ATOM   5238  O  O   . LEU B  1 101 ? 38.526  6.775   38.814  1.00 34.42 ? 118  LEU B O   1 
ATOM   5239  C  CB  . LEU B  1 101 ? 37.328  8.445   41.207  1.00 38.90 ? 118  LEU B CB  1 
ATOM   5240  C  CG  . LEU B  1 101 ? 37.272  9.652   42.150  1.00 40.74 ? 118  LEU B CG  1 
ATOM   5241  C  CD1 . LEU B  1 101 ? 37.069  9.204   43.591  1.00 41.71 ? 118  LEU B CD1 1 
ATOM   5242  C  CD2 . LEU B  1 101 ? 38.515  10.521  42.035  1.00 42.41 ? 118  LEU B CD2 1 
ATOM   5243  N  N   . ALA B  1 102 ? 36.368  7.140   38.245  1.00 40.56 ? 119  ALA B N   1 
ATOM   5244  C  CA  . ALA B  1 102 ? 36.140  5.833   37.636  1.00 43.25 ? 119  ALA B CA  1 
ATOM   5245  C  C   . ALA B  1 102 ? 37.087  5.551   36.468  1.00 43.71 ? 119  ALA B C   1 
ATOM   5246  O  O   . ALA B  1 102 ? 37.780  4.537   36.478  1.00 44.13 ? 119  ALA B O   1 
ATOM   5247  C  CB  . ALA B  1 102 ? 34.697  5.714   37.191  1.00 46.19 ? 119  ALA B CB  1 
HETATM 5248  N  N   . CSX B  1 103 ? 37.102  6.428   35.453  1.00 45.55 ? 120  CSX B N   1 
HETATM 5249  C  CA  . CSX B  1 103 ? 37.890  6.201   34.247  1.00 46.18 ? 120  CSX B CA  1 
HETATM 5250  C  CB  . CSX B  1 103 ? 37.694  7.309   33.209  1.00 50.86 ? 120  CSX B CB  1 
HETATM 5251  S  SG  . CSX B  1 103 ? 36.052  7.236   32.456  1.00 54.63 ? 120  CSX B SG  1 
HETATM 5252  C  C   . CSX B  1 103 ? 39.376  6.087   34.578  1.00 46.17 ? 120  CSX B C   1 
HETATM 5253  O  O   . CSX B  1 103 ? 40.070  5.229   34.034  1.00 45.83 ? 120  CSX B O   1 
HETATM 5254  O  OD  . CSX B  1 103 ? 35.882  5.827   31.947  1.00 53.02 ? 120  CSX B OD  1 
ATOM   5255  N  N   . SER B  1 104 ? 39.854  6.966   35.466  1.00 42.60 ? 121  SER B N   1 
ATOM   5256  C  CA  . SER B  1 104 ? 41.251  6.979   35.867  1.00 42.73 ? 121  SER B CA  1 
ATOM   5257  C  C   . SER B  1 104 ? 41.632  5.659   36.532  1.00 42.89 ? 121  SER B C   1 
ATOM   5258  O  O   . SER B  1 104 ? 42.739  5.160   36.331  1.00 43.76 ? 121  SER B O   1 
ATOM   5259  C  CB  . SER B  1 104 ? 41.539  8.146   36.784  1.00 44.19 ? 121  SER B CB  1 
ATOM   5260  O  OG  . SER B  1 104 ? 41.183  9.376   36.168  1.00 44.47 ? 121  SER B OG  1 
ATOM   5261  N  N   . GLN B  1 105 ? 40.714  5.108   37.334  1.00 40.44 ? 122  GLN B N   1 
ATOM   5262  C  CA  . GLN B  1 105 ? 40.998  3.913   38.113  1.00 41.19 ? 122  GLN B CA  1 
ATOM   5263  C  C   . GLN B  1 105 ? 40.877  2.668   37.232  1.00 40.98 ? 122  GLN B C   1 
ATOM   5264  O  O   . GLN B  1 105 ? 41.719  1.777   37.315  1.00 39.42 ? 122  GLN B O   1 
ATOM   5265  C  CB  . GLN B  1 105 ? 40.080  3.830   39.335  1.00 41.24 ? 122  GLN B CB  1 
ATOM   5266  N  N   . TYR B  1 106 ? 39.834  2.610   36.390  1.00 39.83 ? 123  TYR B N   1 
ATOM   5267  C  CA  . TYR B  1 106 ? 39.454  1.366   35.732  1.00 39.93 ? 123  TYR B CA  1 
ATOM   5268  C  C   . TYR B  1 106 ? 39.499  1.475   34.209  1.00 38.15 ? 123  TYR B C   1 
ATOM   5269  O  O   . TYR B  1 106 ? 39.786  0.490   33.536  1.00 37.03 ? 123  TYR B O   1 
ATOM   5270  C  CB  . TYR B  1 106 ? 38.050  0.947   36.178  1.00 42.55 ? 123  TYR B CB  1 
ATOM   5271  C  CG  . TYR B  1 106 ? 37.990  0.453   37.616  1.00 45.31 ? 123  TYR B CG  1 
ATOM   5272  C  CD1 . TYR B  1 106 ? 38.431  -0.822  37.952  1.00 47.59 ? 123  TYR B CD1 1 
ATOM   5273  C  CD2 . TYR B  1 106 ? 37.491  1.258   38.634  1.00 47.03 ? 123  TYR B CD2 1 
ATOM   5274  C  CE1 . TYR B  1 106 ? 38.386  -1.278  39.259  1.00 49.39 ? 123  TYR B CE1 1 
ATOM   5275  C  CE2 . TYR B  1 106 ? 37.436  0.810   39.944  1.00 48.87 ? 123  TYR B CE2 1 
ATOM   5276  C  CZ  . TYR B  1 106 ? 37.886  -0.460  40.257  1.00 49.59 ? 123  TYR B CZ  1 
ATOM   5277  O  OH  . TYR B  1 106 ? 37.836  -0.905  41.546  1.00 52.94 ? 123  TYR B OH  1 
ATOM   5278  N  N   . GLY B  1 107 ? 39.179  2.651   33.666  1.00 37.84 ? 124  GLY B N   1 
ATOM   5279  C  CA  . GLY B  1 107 ? 38.891  2.767   32.247  1.00 38.46 ? 124  GLY B CA  1 
ATOM   5280  C  C   . GLY B  1 107 ? 37.527  2.150   31.948  1.00 37.16 ? 124  GLY B C   1 
ATOM   5281  O  O   . GLY B  1 107 ? 36.643  2.170   32.800  1.00 36.48 ? 124  GLY B O   1 
ATOM   5282  N  N   . HIS B  1 108 ? 37.367  1.590   30.743  1.00 35.28 ? 125  HIS B N   1 
ATOM   5283  C  CA  . HIS B  1 108 ? 36.085  1.038   30.333  1.00 34.60 ? 125  HIS B CA  1 
ATOM   5284  C  C   . HIS B  1 108 ? 36.310  -0.063  29.298  1.00 33.64 ? 125  HIS B C   1 
ATOM   5285  O  O   . HIS B  1 108 ? 37.261  -0.002  28.519  1.00 33.86 ? 125  HIS B O   1 
ATOM   5286  C  CB  . HIS B  1 108 ? 35.169  2.164   29.833  1.00 33.92 ? 125  HIS B CB  1 
ATOM   5287  C  CG  . HIS B  1 108 ? 33.767  1.734   29.555  1.00 33.97 ? 125  HIS B CG  1 
ATOM   5288  N  ND1 . HIS B  1 108 ? 32.874  1.451   30.565  1.00 33.63 ? 125  HIS B ND1 1 
ATOM   5289  C  CD2 . HIS B  1 108 ? 33.111  1.513   28.407  1.00 33.13 ? 125  HIS B CD2 1 
ATOM   5290  C  CE1 . HIS B  1 108 ? 31.717  1.082   30.032  1.00 34.77 ? 125  HIS B CE1 1 
ATOM   5291  N  NE2 . HIS B  1 108 ? 31.837  1.116   28.721  1.00 33.05 ? 125  HIS B NE2 1 
ATOM   5292  N  N   . ILE B  1 109 ? 35.447  -1.089  29.341  1.00 31.26 ? 126  ILE B N   1 
ATOM   5293  C  CA  . ILE B  1 109 ? 35.354  -2.084  28.285  1.00 30.30 ? 126  ILE B CA  1 
ATOM   5294  C  C   . ILE B  1 109 ? 34.041  -1.835  27.549  1.00 29.86 ? 126  ILE B C   1 
ATOM   5295  O  O   . ILE B  1 109 ? 32.974  -1.939  28.153  1.00 29.51 ? 126  ILE B O   1 
ATOM   5296  C  CB  . ILE B  1 109 ? 35.429  -3.521  28.835  1.00 32.00 ? 126  ILE B CB  1 
ATOM   5297  C  CG1 . ILE B  1 109 ? 36.740  -3.774  29.583  1.00 33.95 ? 126  ILE B CG1 1 
ATOM   5298  C  CG2 . ILE B  1 109 ? 35.209  -4.543  27.716  1.00 30.17 ? 126  ILE B CG2 1 
ATOM   5299  C  CD1 . ILE B  1 109 ? 36.871  -5.174  30.157  1.00 35.52 ? 126  ILE B CD1 1 
ATOM   5300  N  N   . PHE B  1 110 ? 34.142  -1.519  26.253  1.00 28.05 ? 127  PHE B N   1 
ATOM   5301  C  CA  . PHE B  1 110 ? 33.009  -1.038  25.476  1.00 27.61 ? 127  PHE B CA  1 
ATOM   5302  C  C   . PHE B  1 110 ? 32.198  -2.199  24.904  1.00 27.95 ? 127  PHE B C   1 
ATOM   5303  O  O   . PHE B  1 110 ? 32.757  -3.173  24.393  1.00 26.15 ? 127  PHE B O   1 
ATOM   5304  C  CB  . PHE B  1 110 ? 33.495  -0.117  24.350  1.00 27.31 ? 127  PHE B CB  1 
ATOM   5305  C  CG  . PHE B  1 110 ? 33.813  1.283   24.853  1.00 27.29 ? 127  PHE B CG  1 
ATOM   5306  C  CD1 . PHE B  1 110 ? 35.069  1.588   25.362  1.00 26.87 ? 127  PHE B CD1 1 
ATOM   5307  C  CD2 . PHE B  1 110 ? 32.837  2.276   24.854  1.00 27.90 ? 127  PHE B CD2 1 
ATOM   5308  C  CE1 . PHE B  1 110 ? 35.345  2.858   25.850  1.00 28.21 ? 127  PHE B CE1 1 
ATOM   5309  C  CE2 . PHE B  1 110 ? 33.119  3.545   25.334  1.00 28.23 ? 127  PHE B CE2 1 
ATOM   5310  C  CZ  . PHE B  1 110 ? 34.370  3.832   25.837  1.00 27.96 ? 127  PHE B CZ  1 
ATOM   5311  N  N   . ARG B  1 111 ? 30.868  -2.065  25.013  1.00 27.98 ? 128  ARG B N   1 
ATOM   5312  C  CA  . ARG B  1 111 ? 29.930  -2.785  24.166  1.00 28.43 ? 128  ARG B CA  1 
ATOM   5313  C  C   . ARG B  1 111 ? 29.025  -1.740  23.520  1.00 28.88 ? 128  ARG B C   1 
ATOM   5314  O  O   . ARG B  1 111 ? 29.291  -1.319  22.399  1.00 29.97 ? 128  ARG B O   1 
ATOM   5315  C  CB  . ARG B  1 111 ? 29.155  -3.878  24.913  1.00 28.72 ? 128  ARG B CB  1 
ATOM   5316  C  CG  . ARG B  1 111 ? 28.201  -4.674  24.028  1.00 28.93 ? 128  ARG B CG  1 
ATOM   5317  C  CD  . ARG B  1 111 ? 27.288  -5.602  24.826  1.00 30.07 ? 128  ARG B CD  1 
ATOM   5318  N  NE  . ARG B  1 111 ? 26.146  -4.922  25.451  1.00 29.68 ? 128  ARG B NE  1 
ATOM   5319  C  CZ  . ARG B  1 111 ? 25.004  -4.584  24.849  1.00 29.40 ? 128  ARG B CZ  1 
ATOM   5320  N  NH1 . ARG B  1 111 ? 24.796  -4.884  23.577  1.00 28.37 ? 128  ARG B NH1 1 
ATOM   5321  N  NH2 . ARG B  1 111 ? 24.055  -3.959  25.537  1.00 29.42 ? 128  ARG B NH2 1 
ATOM   5322  N  N   . ARG B  1 112 ? 27.990  -1.291  24.245  1.00 29.54 ? 129  ARG B N   1 
ATOM   5323  C  CA  A ARG B  1 112 ? 27.085  -0.285  23.714  0.50 31.14 ? 129  ARG B CA  1 
ATOM   5324  C  CA  B ARG B  1 112 ? 27.073  -0.283  23.740  0.50 31.36 ? 129  ARG B CA  1 
ATOM   5325  C  C   . ARG B  1 112 ? 27.702  1.098   23.922  1.00 31.06 ? 129  ARG B C   1 
ATOM   5326  O  O   . ARG B  1 112 ? 28.408  1.328   24.903  1.00 31.84 ? 129  ARG B O   1 
ATOM   5327  C  CB  A ARG B  1 112 ? 25.681  -0.400  24.323  0.50 32.93 ? 129  ARG B CB  1 
ATOM   5328  C  CB  B ARG B  1 112 ? 25.732  -0.385  24.479  0.50 33.42 ? 129  ARG B CB  1 
ATOM   5329  C  CG  A ARG B  1 112 ? 25.442  0.286   25.661  0.50 33.97 ? 129  ARG B CG  1 
ATOM   5330  C  CG  B ARG B  1 112 ? 24.606  0.438   23.868  0.50 35.02 ? 129  ARG B CG  1 
ATOM   5331  C  CD  A ARG B  1 112 ? 23.992  0.096   26.096  0.50 35.48 ? 129  ARG B CD  1 
ATOM   5332  C  CD  B ARG B  1 112 ? 23.277  0.241   24.583  0.50 36.82 ? 129  ARG B CD  1 
ATOM   5333  N  NE  A ARG B  1 112 ? 23.055  0.597   25.084  0.50 36.27 ? 129  ARG B NE  1 
ATOM   5334  N  NE  B ARG B  1 112 ? 23.319  0.729   25.965  0.50 37.49 ? 129  ARG B NE  1 
ATOM   5335  C  CZ  A ARG B  1 112 ? 21.999  1.360   25.327  0.50 37.51 ? 129  ARG B CZ  1 
ATOM   5336  C  CZ  B ARG B  1 112 ? 22.535  1.680   26.454  0.50 39.92 ? 129  ARG B CZ  1 
ATOM   5337  N  NH1 A ARG B  1 112 ? 21.664  1.652   26.571  0.50 39.12 ? 129  ARG B NH1 1 
ATOM   5338  N  NH1 B ARG B  1 112 ? 21.635  2.258   25.676  0.50 40.46 ? 129  ARG B NH1 1 
ATOM   5339  N  NH2 A ARG B  1 112 ? 21.268  1.812   24.324  0.50 38.25 ? 129  ARG B NH2 1 
ATOM   5340  N  NH2 B ARG B  1 112 ? 22.655  2.047   27.718  0.50 39.53 ? 129  ARG B NH2 1 
ATOM   5341  N  N   . PRO B  1 113 ? 27.470  2.067   23.000  1.00 30.59 ? 130  PRO B N   1 
ATOM   5342  C  CA  . PRO B  1 113 ? 28.000  3.424   23.168  1.00 31.51 ? 130  PRO B CA  1 
ATOM   5343  C  C   . PRO B  1 113 ? 27.559  4.108   24.464  1.00 33.33 ? 130  PRO B C   1 
ATOM   5344  O  O   . PRO B  1 113 ? 26.400  4.013   24.851  1.00 33.57 ? 130  PRO B O   1 
ATOM   5345  C  CB  . PRO B  1 113 ? 27.469  4.180   21.934  1.00 31.15 ? 130  PRO B CB  1 
ATOM   5346  C  CG  . PRO B  1 113 ? 27.136  3.107   20.931  1.00 30.32 ? 130  PRO B CG  1 
ATOM   5347  C  CD  . PRO B  1 113 ? 26.712  1.912   21.750  1.00 30.25 ? 130  PRO B CD  1 
ATOM   5348  N  N   . LYS B  1 114 ? 28.500  4.803   25.113  1.00 37.78 ? 131  LYS B N   1 
ATOM   5349  C  CA  . LYS B  1 114 ? 28.223  5.644   26.271  1.00 41.24 ? 131  LYS B CA  1 
ATOM   5350  C  C   . LYS B  1 114 ? 27.677  6.999   25.814  1.00 38.19 ? 131  LYS B C   1 
ATOM   5351  O  O   . LYS B  1 114 ? 26.858  7.614   26.492  1.00 39.52 ? 131  LYS B O   1 
ATOM   5352  C  CB  . LYS B  1 114 ? 29.520  5.896   27.049  1.00 45.32 ? 131  LYS B CB  1 
ATOM   5353  C  CG  . LYS B  1 114 ? 30.254  4.671   27.589  1.00 49.72 ? 131  LYS B CG  1 
ATOM   5354  C  CD  . LYS B  1 114 ? 29.904  4.287   29.023  1.00 53.07 ? 131  LYS B CD  1 
ATOM   5355  C  CE  . LYS B  1 114 ? 28.468  3.918   29.214  1.00 55.89 ? 131  LYS B CE  1 
ATOM   5356  N  NZ  . LYS B  1 114 ? 28.209  3.553   30.608  1.00 57.43 ? 131  LYS B NZ  1 
ATOM   5357  N  N   . GLY B  1 115 ? 28.170  7.461   24.662  1.00 32.75 ? 132  GLY B N   1 
ATOM   5358  C  CA  . GLY B  1 115 ? 27.831  8.755   24.096  1.00 29.51 ? 132  GLY B CA  1 
ATOM   5359  C  C   . GLY B  1 115 ? 28.717  9.004   22.879  1.00 27.00 ? 132  GLY B C   1 
ATOM   5360  O  O   . GLY B  1 115 ? 29.336  8.064   22.390  1.00 26.73 ? 132  GLY B O   1 
ATOM   5361  N  N   . LEU B  1 116 ? 28.788  10.258  22.420  1.00 23.34 ? 133  LEU B N   1 
ATOM   5362  C  CA  . LEU B  1 116 ? 29.587  10.615  21.259  1.00 23.94 ? 133  LEU B CA  1 
ATOM   5363  C  C   . LEU B  1 116 ? 30.938  11.146  21.720  1.00 22.34 ? 133  LEU B C   1 
ATOM   5364  O  O   . LEU B  1 116 ? 31.003  11.946  22.651  1.00 22.06 ? 133  LEU B O   1 
ATOM   5365  C  CB  . LEU B  1 116 ? 28.910  11.657  20.370  1.00 24.04 ? 133  LEU B CB  1 
ATOM   5366  C  CG  . LEU B  1 116 ? 27.750  11.172  19.500  1.00 24.50 ? 133  LEU B CG  1 
ATOM   5367  C  CD1 . LEU B  1 116 ? 27.186  12.357  18.743  1.00 24.45 ? 133  LEU B CD1 1 
ATOM   5368  C  CD2 . LEU B  1 116 ? 28.150  10.065  18.544  1.00 24.26 ? 133  LEU B CD2 1 
ATOM   5369  N  N   . PHE B  1 117 ? 31.993  10.694  21.036  1.00 21.84 ? 134  PHE B N   1 
ATOM   5370  C  CA  . PHE B  1 117 ? 33.324  11.262  21.159  1.00 20.79 ? 134  PHE B CA  1 
ATOM   5371  C  C   . PHE B  1 117 ? 33.647  12.005  19.869  1.00 20.31 ? 134  PHE B C   1 
ATOM   5372  O  O   . PHE B  1 117 ? 33.531  11.439  18.781  1.00 20.18 ? 134  PHE B O   1 
ATOM   5373  C  CB  . PHE B  1 117 ? 34.378  10.182  21.415  1.00 20.78 ? 134  PHE B CB  1 
ATOM   5374  C  CG  . PHE B  1 117 ? 34.225  9.488   22.756  1.00 22.19 ? 134  PHE B CG  1 
ATOM   5375  C  CD1 . PHE B  1 117 ? 34.843  9.998   23.892  1.00 22.81 ? 134  PHE B CD1 1 
ATOM   5376  C  CD2 . PHE B  1 117 ? 33.444  8.346   22.882  1.00 22.67 ? 134  PHE B CD2 1 
ATOM   5377  C  CE1 . PHE B  1 117 ? 34.698  9.369   25.113  1.00 23.83 ? 134  PHE B CE1 1 
ATOM   5378  C  CE2 . PHE B  1 117 ? 33.307  7.722   24.106  1.00 23.54 ? 134  PHE B CE2 1 
ATOM   5379  C  CZ  . PHE B  1 117 ? 33.933  8.232   25.217  1.00 23.45 ? 134  PHE B CZ  1 
ATOM   5380  N  N   . ILE B  1 118 ? 34.024  13.281  20.003  1.00 20.39 ? 135  ILE B N   1 
ATOM   5381  C  CA  . ILE B  1 118 ? 34.354  14.128  18.866  1.00 21.29 ? 135  ILE B CA  1 
ATOM   5382  C  C   . ILE B  1 118 ? 35.759  14.668  19.107  1.00 22.64 ? 135  ILE B C   1 
ATOM   5383  O  O   . ILE B  1 118 ? 35.963  15.456  20.032  1.00 23.67 ? 135  ILE B O   1 
ATOM   5384  C  CB  . ILE B  1 118 ? 33.330  15.266  18.691  1.00 22.49 ? 135  ILE B CB  1 
ATOM   5385  C  CG1 . ILE B  1 118 ? 31.906  14.730  18.518  1.00 22.32 ? 135  ILE B CG1 1 
ATOM   5386  C  CG2 . ILE B  1 118 ? 33.726  16.197  17.540  1.00 23.04 ? 135  ILE B CG2 1 
ATOM   5387  C  CD1 . ILE B  1 118 ? 30.838  15.805  18.466  1.00 22.62 ? 135  ILE B CD1 1 
ATOM   5388  N  N   . SER B  1 119 ? 36.730  14.219  18.308  1.00 22.36 ? 136  SER B N   1 
ATOM   5389  C  CA  . SER B  1 119 ? 38.103  14.656  18.505  1.00 23.34 ? 136  SER B CA  1 
ATOM   5390  C  C   . SER B  1 119 ? 38.461  15.766  17.520  1.00 23.92 ? 136  SER B C   1 
ATOM   5391  O  O   . SER B  1 119 ? 37.816  15.934  16.490  1.00 25.21 ? 136  SER B O   1 
ATOM   5392  C  CB  . SER B  1 119 ? 39.072  13.516  18.400  1.00 24.42 ? 136  SER B CB  1 
ATOM   5393  O  OG  . SER B  1 119 ? 39.394  13.255  17.045  1.00 26.26 ? 136  SER B OG  1 
ATOM   5394  N  N   . ILE B  1 120 ? 39.524  16.508  17.841  1.00 24.64 ? 137  ILE B N   1 
ATOM   5395  C  CA  . ILE B  1 120 ? 40.052  17.527  16.945  1.00 25.03 ? 137  ILE B CA  1 
ATOM   5396  C  C   . ILE B  1 120 ? 40.471  16.895  15.613  1.00 23.75 ? 137  ILE B C   1 
ATOM   5397  O  O   . ILE B  1 120 ? 40.415  17.550  14.574  1.00 24.26 ? 137  ILE B O   1 
ATOM   5398  C  CB  . ILE B  1 120 ? 41.195  18.302  17.634  1.00 25.37 ? 137  ILE B CB  1 
ATOM   5399  C  CG1 . ILE B  1 120 ? 41.618  19.529  16.833  1.00 27.41 ? 137  ILE B CG1 1 
ATOM   5400  C  CG2 . ILE B  1 120 ? 42.393  17.403  17.948  1.00 25.07 ? 137  ILE B CG2 1 
ATOM   5401  C  CD1 . ILE B  1 120 ? 40.606  20.655  16.859  1.00 28.30 ? 137  ILE B CD1 1 
ATOM   5402  N  N   . SER B  1 121 ? 40.853  15.611  15.640  1.00 24.86 ? 138  SER B N   1 
ATOM   5403  C  CA  . SER B  1 121 ? 41.217  14.860  14.442  1.00 25.22 ? 138  SER B CA  1 
ATOM   5404  C  C   . SER B  1 121 ? 40.034  14.650  13.497  1.00 25.51 ? 138  SER B C   1 
ATOM   5405  O  O   . SER B  1 121 ? 40.234  14.299  12.332  1.00 25.02 ? 138  SER B O   1 
ATOM   5406  C  CB  . SER B  1 121 ? 41.821  13.530  14.811  1.00 26.15 ? 138  SER B CB  1 
ATOM   5407  O  OG  . SER B  1 121 ? 42.930  13.700  15.679  1.00 27.47 ? 138  SER B OG  1 
ATOM   5408  N  N   . ASP B  1 122 ? 38.806  14.847  13.999  1.00 25.22 ? 139  ASP B N   1 
ATOM   5409  C  CA  . ASP B  1 122 ? 37.597  14.673  13.210  1.00 24.84 ? 139  ASP B CA  1 
ATOM   5410  C  C   . ASP B  1 122 ? 37.082  15.997  12.648  1.00 24.79 ? 139  ASP B C   1 
ATOM   5411  O  O   . ASP B  1 122 ? 35.960  16.054  12.148  1.00 23.61 ? 139  ASP B O   1 
ATOM   5412  C  CB  . ASP B  1 122 ? 36.499  14.032  14.045  1.00 25.37 ? 139  ASP B CB  1 
ATOM   5413  C  CG  . ASP B  1 122 ? 36.840  12.669  14.620  1.00 26.10 ? 139  ASP B CG  1 
ATOM   5414  O  OD1 . ASP B  1 122 ? 37.085  11.749  13.815  1.00 27.37 ? 139  ASP B OD1 1 
ATOM   5415  O  OD2 . ASP B  1 122 ? 36.849  12.539  15.866  1.00 27.62 ? 139  ASP B OD2 1 
ATOM   5416  N  N   . ARG B  1 123 ? 37.885  17.065  12.716  1.00 25.13 ? 140  ARG B N   1 
ATOM   5417  C  CA  . ARG B  1 123 ? 37.443  18.364  12.231  1.00 26.25 ? 140  ARG B CA  1 
ATOM   5418  C  C   . ARG B  1 123 ? 37.058  18.256  10.755  1.00 25.56 ? 140  ARG B C   1 
ATOM   5419  O  O   . ARG B  1 123 ? 37.737  17.592  9.975   1.00 25.33 ? 140  ARG B O   1 
ATOM   5420  C  CB  . ARG B  1 123 ? 38.510  19.433  12.498  1.00 29.32 ? 140  ARG B CB  1 
ATOM   5421  C  CG  . ARG B  1 123 ? 39.834  19.256  11.769  1.00 32.98 ? 140  ARG B CG  1 
ATOM   5422  C  CD  . ARG B  1 123 ? 40.938  20.064  12.445  1.00 36.74 ? 140  ARG B CD  1 
ATOM   5423  N  NE  . ARG B  1 123 ? 42.239  19.912  11.781  1.00 39.96 ? 140  ARG B NE  1 
ATOM   5424  C  CZ  . ARG B  1 123 ? 43.237  19.117  12.169  1.00 40.51 ? 140  ARG B CZ  1 
ATOM   5425  N  NH1 . ARG B  1 123 ? 43.089  18.293  13.193  1.00 39.95 ? 140  ARG B NH1 1 
ATOM   5426  N  NH2 . ARG B  1 123 ? 44.381  19.126  11.503  1.00 41.35 ? 140  ARG B NH2 1 
ATOM   5427  N  N   . GLY B  1 124 ? 35.937  18.898  10.398  1.00 24.61 ? 141  GLY B N   1 
ATOM   5428  C  CA  . GLY B  1 124 ? 35.369  18.824  9.061   1.00 23.94 ? 141  GLY B CA  1 
ATOM   5429  C  C   . GLY B  1 124 ? 34.463  17.606  8.861   1.00 23.86 ? 141  GLY B C   1 
ATOM   5430  O  O   . GLY B  1 124 ? 33.820  17.499  7.822   1.00 24.33 ? 141  GLY B O   1 
ATOM   5431  N  N   . HIS B  1 125 ? 34.387  16.704  9.851   1.00 23.21 ? 142  HIS B N   1 
ATOM   5432  C  CA  . HIS B  1 125 ? 33.610  15.478  9.716   1.00 23.53 ? 142  HIS B CA  1 
ATOM   5433  C  C   . HIS B  1 125 ? 32.699  15.262  10.928  1.00 23.45 ? 142  HIS B C   1 
ATOM   5434  O  O   . HIS B  1 125 ? 32.286  14.132  11.206  1.00 23.10 ? 142  HIS B O   1 
ATOM   5435  C  CB  . HIS B  1 125 ? 34.548  14.285  9.486   1.00 23.98 ? 142  HIS B CB  1 
ATOM   5436  C  CG  . HIS B  1 125 ? 35.352  14.398  8.227   1.00 24.90 ? 142  HIS B CG  1 
ATOM   5437  N  ND1 . HIS B  1 125 ? 34.856  14.034  6.994   1.00 25.43 ? 142  HIS B ND1 1 
ATOM   5438  C  CD2 . HIS B  1 125 ? 36.592  14.858  8.003   1.00 25.97 ? 142  HIS B CD2 1 
ATOM   5439  C  CE1 . HIS B  1 125 ? 35.776  14.257  6.066   1.00 26.03 ? 142  HIS B CE1 1 
ATOM   5440  N  NE2 . HIS B  1 125 ? 36.842  14.752  6.658   1.00 25.85 ? 142  HIS B NE2 1 
ATOM   5441  N  N   . VAL B  1 126 ? 32.338  16.347  11.622  1.00 22.21 ? 143  VAL B N   1 
ATOM   5442  C  CA  . VAL B  1 126 ? 31.610  16.221  12.875  1.00 22.85 ? 143  VAL B CA  1 
ATOM   5443  C  C   . VAL B  1 126 ? 30.182  15.763  12.592  1.00 22.45 ? 143  VAL B C   1 
ATOM   5444  O  O   . VAL B  1 126 ? 29.619  14.995  13.369  1.00 21.95 ? 143  VAL B O   1 
ATOM   5445  C  CB  . VAL B  1 126 ? 31.641  17.503  13.723  1.00 22.77 ? 143  VAL B CB  1 
ATOM   5446  C  CG1 . VAL B  1 126 ? 30.735  17.404  14.947  1.00 22.88 ? 143  VAL B CG1 1 
ATOM   5447  C  CG2 . VAL B  1 126 ? 33.064  17.844  14.143  1.00 23.22 ? 143  VAL B CG2 1 
ATOM   5448  N  N   . ARG B  1 127 ? 29.611  16.203  11.466  1.00 23.24 ? 144  ARG B N   1 
ATOM   5449  C  CA  . ARG B  1 127 ? 28.247  15.829  11.125  1.00 24.42 ? 144  ARG B CA  1 
ATOM   5450  C  C   . ARG B  1 127 ? 28.125  14.310  10.969  1.00 23.95 ? 144  ARG B C   1 
ATOM   5451  O  O   . ARG B  1 127 ? 27.121  13.733  11.382  1.00 22.53 ? 144  ARG B O   1 
ATOM   5452  C  CB  . ARG B  1 127 ? 27.731  16.556  9.875   1.00 26.17 ? 144  ARG B CB  1 
ATOM   5453  C  CG  . ARG B  1 127 ? 26.288  16.220  9.516   1.00 28.51 ? 144  ARG B CG  1 
ATOM   5454  C  CD  . ARG B  1 127 ? 25.299  16.439  10.672  1.00 31.25 ? 144  ARG B CD  1 
ATOM   5455  N  NE  . ARG B  1 127 ? 23.943  15.942  10.406  1.00 32.81 ? 144  ARG B NE  1 
ATOM   5456  C  CZ  . ARG B  1 127 ? 23.015  16.511  9.636   1.00 36.32 ? 144  ARG B CZ  1 
ATOM   5457  N  NH1 . ARG B  1 127 ? 23.245  17.667  9.032   1.00 37.62 ? 144  ARG B NH1 1 
ATOM   5458  N  NH2 . ARG B  1 127 ? 21.842  15.919  9.477   1.00 37.32 ? 144  ARG B NH2 1 
ATOM   5459  N  N   A SER B  1 128 ? 29.146  13.689  10.363  0.51 23.46 ? 145  SER B N   1 
ATOM   5460  N  N   B SER B  1 128 ? 29.142  13.665  10.382  0.49 23.19 ? 145  SER B N   1 
ATOM   5461  C  CA  A SER B  1 128 ? 29.173  12.250  10.143  0.51 24.07 ? 145  SER B CA  1 
ATOM   5462  C  CA  B SER B  1 128 ? 29.090  12.228  10.151  0.49 23.53 ? 145  SER B CA  1 
ATOM   5463  C  C   A SER B  1 128 ? 29.153  11.501  11.474  0.51 23.09 ? 145  SER B C   1 
ATOM   5464  C  C   B SER B  1 128 ? 29.192  11.460  11.469  0.49 22.82 ? 145  SER B C   1 
ATOM   5465  O  O   A SER B  1 128 ? 28.534  10.442  11.575  0.51 23.21 ? 145  SER B O   1 
ATOM   5466  O  O   B SER B  1 128 ? 28.687  10.341  11.559  0.49 22.91 ? 145  SER B O   1 
ATOM   5467  C  CB  A SER B  1 128 ? 30.372  11.843  9.315   0.51 24.88 ? 145  SER B CB  1 
ATOM   5468  C  CB  B SER B  1 128 ? 30.139  11.771  9.158   0.49 23.99 ? 145  SER B CB  1 
ATOM   5469  O  OG  A SER B  1 128 ? 30.345  12.459  8.035   0.51 25.62 ? 145  SER B OG  1 
ATOM   5470  O  OG  B SER B  1 128 ? 31.457  11.985  9.640   0.49 24.21 ? 145  SER B OG  1 
ATOM   5471  N  N   . ILE B  1 129 ? 29.837  12.052  12.485  1.00 21.94 ? 146  ILE B N   1 
ATOM   5472  C  CA  . ILE B  1 129 ? 29.844  11.462  13.820  1.00 21.68 ? 146  ILE B CA  1 
ATOM   5473  C  C   . ILE B  1 129 ? 28.459  11.601  14.453  1.00 21.16 ? 146  ILE B C   1 
ATOM   5474  O  O   . ILE B  1 129 ? 27.926  10.636  14.996  1.00 20.53 ? 146  ILE B O   1 
ATOM   5475  C  CB  . ILE B  1 129 ? 30.958  12.053  14.701  1.00 22.27 ? 146  ILE B CB  1 
ATOM   5476  C  CG1 . ILE B  1 129 ? 32.326  11.512  14.266  1.00 23.06 ? 146  ILE B CG1 1 
ATOM   5477  C  CG2 . ILE B  1 129 ? 30.693  11.791  16.183  1.00 22.36 ? 146  ILE B CG2 1 
ATOM   5478  C  CD1 . ILE B  1 129 ? 33.510  12.148  14.963  1.00 24.12 ? 146  ILE B CD1 1 
ATOM   5479  N  N   . VAL B  1 130 ? 27.867  12.797  14.369  1.00 21.02 ? 147  VAL B N   1 
ATOM   5480  C  CA  . VAL B  1 130 ? 26.548  13.025  14.938  1.00 21.27 ? 147  VAL B CA  1 
ATOM   5481  C  C   . VAL B  1 130 ? 25.547  12.050  14.321  1.00 21.58 ? 147  VAL B C   1 
ATOM   5482  O  O   . VAL B  1 130 ? 24.690  11.521  15.033  1.00 21.66 ? 147  VAL B O   1 
ATOM   5483  C  CB  . VAL B  1 130 ? 26.108  14.492  14.765  1.00 21.62 ? 147  VAL B CB  1 
ATOM   5484  C  CG1 . VAL B  1 130 ? 24.634  14.699  15.098  1.00 22.61 ? 147  VAL B CG1 1 
ATOM   5485  C  CG2 . VAL B  1 130 ? 26.968  15.423  15.606  1.00 21.48 ? 147  VAL B CG2 1 
ATOM   5486  N  N   . ASP B  1 131 ? 25.688  11.788  13.011  1.00 22.24 ? 148  ASP B N   1 
ATOM   5487  C  CA  . ASP B  1 131 ? 24.768  10.932  12.273  1.00 22.72 ? 148  ASP B CA  1 
ATOM   5488  C  C   . ASP B  1 131 ? 24.911  9.457   12.651  1.00 22.53 ? 148  ASP B C   1 
ATOM   5489  O  O   . ASP B  1 131 ? 24.034  8.661   12.319  1.00 22.49 ? 148  ASP B O   1 
ATOM   5490  C  CB  . ASP B  1 131 ? 24.926  11.114  10.772  1.00 23.84 ? 148  ASP B CB  1 
ATOM   5491  C  CG  . ASP B  1 131 ? 24.374  12.416  10.212  1.00 26.39 ? 148  ASP B CG  1 
ATOM   5492  O  OD1 . ASP B  1 131 ? 23.631  13.116  10.946  1.00 26.02 ? 148  ASP B OD1 1 
ATOM   5493  O  OD2 . ASP B  1 131 ? 24.707  12.728  9.049   1.00 28.37 ? 148  ASP B OD2 1 
ATOM   5494  N  N   . ASN B  1 132 ? 26.001  9.087   13.334  1.00 22.06 ? 149  ASN B N   1 
ATOM   5495  C  CA  . ASN B  1 132 ? 26.175  7.721   13.806  1.00 21.65 ? 149  ASN B CA  1 
ATOM   5496  C  C   . ASN B  1 132 ? 25.453  7.473   15.131  1.00 21.30 ? 149  ASN B C   1 
ATOM   5497  O  O   . ASN B  1 132 ? 25.326  6.321   15.536  1.00 20.44 ? 149  ASN B O   1 
ATOM   5498  C  CB  . ASN B  1 132 ? 27.648  7.347   13.927  1.00 21.53 ? 149  ASN B CB  1 
ATOM   5499  C  CG  . ASN B  1 132 ? 28.290  7.053   12.590  1.00 21.40 ? 149  ASN B CG  1 
ATOM   5500  O  OD1 . ASN B  1 132 ? 27.603  6.746   11.610  1.00 20.64 ? 149  ASN B OD1 1 
ATOM   5501  N  ND2 . ASN B  1 132 ? 29.614  7.087   12.543  1.00 22.09 ? 149  ASN B ND2 1 
ATOM   5502  N  N   . TRP B  1 133 ? 25.014  8.524   15.840  1.00 21.68 ? 150  TRP B N   1 
ATOM   5503  C  CA  . TRP B  1 133 ? 24.254  8.300   17.061  1.00 21.60 ? 150  TRP B CA  1 
ATOM   5504  C  C   . TRP B  1 133 ? 22.951  7.594   16.701  1.00 21.94 ? 150  TRP B C   1 
ATOM   5505  O  O   . TRP B  1 133 ? 22.234  8.052   15.813  1.00 21.68 ? 150  TRP B O   1 
ATOM   5506  C  CB  . TRP B  1 133 ? 23.985  9.597   17.842  1.00 22.10 ? 150  TRP B CB  1 
ATOM   5507  C  CG  . TRP B  1 133 ? 23.415  9.351   19.215  1.00 21.17 ? 150  TRP B CG  1 
ATOM   5508  C  CD1 . TRP B  1 133 ? 22.181  9.710   19.665  1.00 21.01 ? 150  TRP B CD1 1 
ATOM   5509  C  CD2 . TRP B  1 133 ? 24.044  8.637   20.302  1.00 21.20 ? 150  TRP B CD2 1 
ATOM   5510  N  NE1 . TRP B  1 133 ? 22.005  9.297   20.957  1.00 20.99 ? 150  TRP B NE1 1 
ATOM   5511  C  CE2 . TRP B  1 133 ? 23.124  8.630   21.374  1.00 21.49 ? 150  TRP B CE2 1 
ATOM   5512  C  CE3 . TRP B  1 133 ? 25.285  8.018   20.482  1.00 21.32 ? 150  TRP B CE3 1 
ATOM   5513  C  CZ2 . TRP B  1 133 ? 23.409  8.031   22.599  1.00 22.08 ? 150  TRP B CZ2 1 
ATOM   5514  C  CZ3 . TRP B  1 133 ? 25.563  7.418   21.692  1.00 21.84 ? 150  TRP B CZ3 1 
ATOM   5515  C  CH2 . TRP B  1 133 ? 24.639  7.430   22.738  1.00 22.02 ? 150  TRP B CH2 1 
ATOM   5516  N  N   . PRO B  1 134 ? 22.619  6.448   17.342  1.00 23.85 ? 151  PRO B N   1 
ATOM   5517  C  CA  . PRO B  1 134 ? 21.431  5.675   16.963  1.00 25.29 ? 151  PRO B CA  1 
ATOM   5518  C  C   . PRO B  1 134 ? 20.053  6.314   17.171  1.00 26.50 ? 151  PRO B C   1 
ATOM   5519  O  O   . PRO B  1 134 ? 19.118  5.945   16.470  1.00 30.70 ? 151  PRO B O   1 
ATOM   5520  C  CB  . PRO B  1 134 ? 21.578  4.390   17.809  1.00 25.78 ? 151  PRO B CB  1 
ATOM   5521  C  CG  . PRO B  1 134 ? 23.037  4.351   18.203  1.00 25.63 ? 151  PRO B CG  1 
ATOM   5522  C  CD  . PRO B  1 134 ? 23.394  5.802   18.417  1.00 23.92 ? 151  PRO B CD  1 
ATOM   5523  N  N   . GLU B  1 135 ? 19.921  7.265   18.107  1.00 25.93 ? 152  GLU B N   1 
ATOM   5524  C  CA  . GLU B  1 135 ? 18.624  7.846   18.455  1.00 26.57 ? 152  GLU B CA  1 
ATOM   5525  C  C   . GLU B  1 135 ? 18.352  9.100   17.620  1.00 27.10 ? 152  GLU B C   1 
ATOM   5526  O  O   . GLU B  1 135 ? 19.240  9.932   17.436  1.00 26.61 ? 152  GLU B O   1 
ATOM   5527  C  CB  . GLU B  1 135 ? 18.569  8.225   19.935  1.00 27.28 ? 152  GLU B CB  1 
ATOM   5528  C  CG  . GLU B  1 135 ? 19.040  7.119   20.872  1.00 29.60 ? 152  GLU B CG  1 
ATOM   5529  C  CD  . GLU B  1 135 ? 18.181  5.875   20.876  1.00 33.00 ? 152  GLU B CD  1 
ATOM   5530  O  OE1 . GLU B  1 135 ? 18.702  4.831   21.332  1.00 38.09 ? 152  GLU B OE1 1 
ATOM   5531  O  OE2 . GLU B  1 135 ? 17.002  5.954   20.456  1.00 35.01 ? 152  GLU B OE2 1 
ATOM   5532  N  N   . ASN B  1 136 ? 17.107  9.263   17.150  1.00 27.05 ? 153  ASN B N   1 
ATOM   5533  C  CA  . ASN B  1 136 ? 16.806  10.297  16.168  1.00 29.40 ? 153  ASN B CA  1 
ATOM   5534  C  C   . ASN B  1 136 ? 16.075  11.501  16.771  1.00 27.40 ? 153  ASN B C   1 
ATOM   5535  O  O   . ASN B  1 136 ? 15.813  12.453  16.038  1.00 26.98 ? 153  ASN B O   1 
ATOM   5536  C  CB  . ASN B  1 136 ? 15.953  9.783   15.010  1.00 32.77 ? 153  ASN B CB  1 
ATOM   5537  C  CG  . ASN B  1 136 ? 16.476  8.512   14.383  1.00 36.39 ? 153  ASN B CG  1 
ATOM   5538  O  OD1 . ASN B  1 136 ? 17.614  8.473   13.906  1.00 40.12 ? 153  ASN B OD1 1 
ATOM   5539  N  ND2 . ASN B  1 136 ? 15.656  7.469   14.355  1.00 39.96 ? 153  ASN B ND2 1 
ATOM   5540  N  N   . HIS B  1 137 ? 15.731  11.469  18.069  1.00 26.16 ? 154  HIS B N   1 
ATOM   5541  C  CA  . HIS B  1 137 ? 14.931  12.531  18.675  1.00 27.24 ? 154  HIS B CA  1 
ATOM   5542  C  C   . HIS B  1 137 ? 15.584  13.070  19.951  1.00 25.06 ? 154  HIS B C   1 
ATOM   5543  O  O   . HIS B  1 137 ? 14.920  13.257  20.972  1.00 25.73 ? 154  HIS B O   1 
ATOM   5544  C  CB  . HIS B  1 137 ? 13.492  12.063  18.945  1.00 29.35 ? 154  HIS B CB  1 
ATOM   5545  C  CG  . HIS B  1 137 ? 12.841  11.458  17.748  1.00 34.17 ? 154  HIS B CG  1 
ATOM   5546  N  ND1 . HIS B  1 137 ? 12.437  12.208  16.663  1.00 36.23 ? 154  HIS B ND1 1 
ATOM   5547  C  CD2 . HIS B  1 137 ? 12.571  10.179  17.440  1.00 36.46 ? 154  HIS B CD2 1 
ATOM   5548  C  CE1 . HIS B  1 137 ? 11.927  11.403  15.741  1.00 36.05 ? 154  HIS B CE1 1 
ATOM   5549  N  NE2 . HIS B  1 137 ? 11.999  10.166  16.192  1.00 37.66 ? 154  HIS B NE2 1 
ATOM   5550  N  N   . VAL B  1 138 ? 16.867  13.429  19.858  1.00 21.22 ? 155  VAL B N   1 
ATOM   5551  C  CA  . VAL B  1 138 ? 17.582  13.989  20.991  1.00 19.27 ? 155  VAL B CA  1 
ATOM   5552  C  C   . VAL B  1 138 ? 17.040  15.376  21.340  1.00 19.38 ? 155  VAL B C   1 
ATOM   5553  O  O   . VAL B  1 138 ? 16.818  16.208  20.458  1.00 18.39 ? 155  VAL B O   1 
ATOM   5554  C  CB  . VAL B  1 138 ? 19.089  14.022  20.681  1.00 18.97 ? 155  VAL B CB  1 
ATOM   5555  C  CG1 . VAL B  1 138 ? 19.867  14.837  21.710  1.00 18.37 ? 155  VAL B CG1 1 
ATOM   5556  C  CG2 . VAL B  1 138 ? 19.648  12.609  20.571  1.00 18.69 ? 155  VAL B CG2 1 
ATOM   5557  N  N   . LYS B  1 139 ? 16.853  15.601  22.653  1.00 20.11 ? 156  LYS B N   1 
ATOM   5558  C  CA  . LYS B  1 139 ? 16.326  16.845  23.194  1.00 20.04 ? 156  LYS B CA  1 
ATOM   5559  C  C   . LYS B  1 139 ? 17.296  17.471  24.195  1.00 20.07 ? 156  LYS B C   1 
ATOM   5560  O  O   . LYS B  1 139 ? 17.226  18.679  24.418  1.00 21.24 ? 156  LYS B O   1 
ATOM   5561  C  CB  . LYS B  1 139 ? 14.994  16.629  23.926  1.00 21.27 ? 156  LYS B CB  1 
ATOM   5562  C  CG  . LYS B  1 139 ? 13.832  16.144  23.073  1.00 22.94 ? 156  LYS B CG  1 
ATOM   5563  C  CD  . LYS B  1 139 ? 13.476  17.031  21.886  1.00 24.81 ? 156  LYS B CD  1 
ATOM   5564  C  CE  . LYS B  1 139 ? 13.138  18.446  22.236  1.00 26.46 ? 156  LYS B CE  1 
ATOM   5565  N  NZ  . LYS B  1 139 ? 13.021  19.281  21.031  1.00 27.54 ? 156  LYS B NZ  1 
ATOM   5566  N  N   . ALA B  1 140 ? 18.171  16.663  24.815  1.00 18.07 ? 157  ALA B N   1 
ATOM   5567  C  CA  . ALA B  1 140 ? 19.073  17.145  25.849  1.00 17.70 ? 157  ALA B CA  1 
ATOM   5568  C  C   . ALA B  1 140 ? 20.485  16.619  25.601  1.00 17.72 ? 157  ALA B C   1 
ATOM   5569  O  O   . ALA B  1 140 ? 20.708  15.407  25.634  1.00 17.40 ? 157  ALA B O   1 
ATOM   5570  C  CB  . ALA B  1 140 ? 18.585  16.726  27.215  1.00 17.73 ? 157  ALA B CB  1 
ATOM   5571  N  N   . VAL B  1 141 ? 21.412  17.556  25.358  1.00 17.26 ? 158  VAL B N   1 
ATOM   5572  C  CA  . VAL B  1 141 ? 22.823  17.269  25.150  1.00 17.65 ? 158  VAL B CA  1 
ATOM   5573  C  C   . VAL B  1 141 ? 23.616  17.863  26.311  1.00 17.95 ? 158  VAL B C   1 
ATOM   5574  O  O   . VAL B  1 141 ? 23.432  19.029  26.659  1.00 18.66 ? 158  VAL B O   1 
ATOM   5575  C  CB  . VAL B  1 141 ? 23.328  17.851  23.817  1.00 18.14 ? 158  VAL B CB  1 
ATOM   5576  C  CG1 . VAL B  1 141 ? 24.835  17.664  23.650  1.00 18.62 ? 158  VAL B CG1 1 
ATOM   5577  C  CG2 . VAL B  1 141 ? 22.590  17.273  22.621  1.00 18.60 ? 158  VAL B CG2 1 
ATOM   5578  N  N   . VAL B  1 142 ? 24.521  17.066  26.890  1.00 18.02 ? 159  VAL B N   1 
ATOM   5579  C  CA  . VAL B  1 142 ? 25.484  17.572  27.851  1.00 18.01 ? 159  VAL B CA  1 
ATOM   5580  C  C   . VAL B  1 142 ? 26.873  17.270  27.293  1.00 18.83 ? 159  VAL B C   1 
ATOM   5581  O  O   . VAL B  1 142 ? 27.167  16.121  26.970  1.00 18.64 ? 159  VAL B O   1 
ATOM   5582  C  CB  . VAL B  1 142 ? 25.312  17.000  29.269  1.00 18.47 ? 159  VAL B CB  1 
ATOM   5583  C  CG1 . VAL B  1 142 ? 26.461  17.409  30.187  1.00 18.74 ? 159  VAL B CG1 1 
ATOM   5584  C  CG2 . VAL B  1 142 ? 23.973  17.397  29.887  1.00 19.15 ? 159  VAL B CG2 1 
ATOM   5585  N  N   . VAL B  1 143 ? 27.703  18.314  27.181  1.00 18.92 ? 160  VAL B N   1 
ATOM   5586  C  CA  . VAL B  1 143 ? 28.997  18.226  26.516  1.00 19.77 ? 160  VAL B CA  1 
ATOM   5587  C  C   . VAL B  1 143 ? 30.093  18.749  27.449  1.00 19.73 ? 160  VAL B C   1 
ATOM   5588  O  O   . VAL B  1 143 ? 29.903  19.759  28.124  1.00 20.24 ? 160  VAL B O   1 
ATOM   5589  C  CB  . VAL B  1 143 ? 28.971  18.997  25.177  1.00 19.78 ? 160  VAL B CB  1 
ATOM   5590  C  CG1 . VAL B  1 143 ? 28.589  20.466  25.353  1.00 20.51 ? 160  VAL B CG1 1 
ATOM   5591  C  CG2 . VAL B  1 143 ? 30.294  18.872  24.422  1.00 20.07 ? 160  VAL B CG2 1 
ATOM   5592  N  N   . THR B  1 144 ? 31.240  18.048  27.474  1.00 19.44 ? 161  THR B N   1 
ATOM   5593  C  CA  . THR B  1 144 ? 32.429  18.488  28.192  1.00 20.23 ? 161  THR B CA  1 
ATOM   5594  C  C   . THR B  1 144 ? 33.646  18.312  27.285  1.00 20.50 ? 161  THR B C   1 
ATOM   5595  O  O   . THR B  1 144 ? 33.620  17.493  26.367  1.00 20.61 ? 161  THR B O   1 
ATOM   5596  C  CB  . THR B  1 144 ? 32.581  17.697  29.495  1.00 20.88 ? 161  THR B CB  1 
ATOM   5597  O  OG1 . THR B  1 144 ? 33.648  18.294  30.229  1.00 22.00 ? 161  THR B OG1 1 
ATOM   5598  C  CG2 . THR B  1 144 ? 32.905  16.229  29.282  1.00 20.77 ? 161  THR B CG2 1 
ATOM   5599  N  N   . ASP B  1 145 ? 34.706  19.094  27.541  1.00 21.17 ? 162  ASP B N   1 
ATOM   5600  C  CA  . ASP B  1 145 ? 36.014  18.831  26.953  1.00 20.69 ? 162  ASP B CA  1 
ATOM   5601  C  C   . ASP B  1 145 ? 36.962  18.257  28.008  1.00 21.19 ? 162  ASP B C   1 
ATOM   5602  O  O   . ASP B  1 145 ? 38.128  17.978  27.712  1.00 20.05 ? 162  ASP B O   1 
ATOM   5603  C  CB  . ASP B  1 145 ? 36.583  20.053  26.249  1.00 21.43 ? 162  ASP B CB  1 
ATOM   5604  C  CG  . ASP B  1 145 ? 36.979  21.216  27.146  1.00 21.88 ? 162  ASP B CG  1 
ATOM   5605  O  OD1 . ASP B  1 145 ? 36.748  21.112  28.373  1.00 22.15 ? 162  ASP B OD1 1 
ATOM   5606  O  OD2 . ASP B  1 145 ? 37.511  22.214  26.604  1.00 22.46 ? 162  ASP B OD2 1 
ATOM   5607  N  N   . GLY B  1 146 ? 36.460  18.080  29.236  1.00 20.99 ? 163  GLY B N   1 
ATOM   5608  C  CA  . GLY B  1 146 ? 37.201  17.409  30.291  1.00 22.00 ? 163  GLY B CA  1 
ATOM   5609  C  C   . GLY B  1 146 ? 38.332  18.257  30.881  1.00 22.76 ? 163  GLY B C   1 
ATOM   5610  O  O   . GLY B  1 146 ? 39.180  17.725  31.596  1.00 23.55 ? 163  GLY B O   1 
ATOM   5611  N  N   . GLU B  1 147 ? 38.329  19.570  30.624  1.00 23.62 ? 164  GLU B N   1 
ATOM   5612  C  CA  . GLU B  1 147 ? 39.434  20.417  31.054  1.00 25.58 ? 164  GLU B CA  1 
ATOM   5613  C  C   . GLU B  1 147 ? 39.329  20.719  32.549  1.00 26.47 ? 164  GLU B C   1 
ATOM   5614  O  O   . GLU B  1 147 ? 40.346  20.755  33.241  1.00 24.68 ? 164  GLU B O   1 
ATOM   5615  C  CB  . GLU B  1 147 ? 39.566  21.707  30.244  1.00 26.46 ? 164  GLU B CB  1 
ATOM   5616  C  CG  . GLU B  1 147 ? 40.810  22.503  30.640  1.00 28.29 ? 164  GLU B CG  1 
ATOM   5617  C  CD  . GLU B  1 147 ? 41.309  23.560  29.672  1.00 29.51 ? 164  GLU B CD  1 
ATOM   5618  O  OE1 . GLU B  1 147 ? 40.631  23.897  28.675  1.00 28.23 ? 164  GLU B OE1 1 
ATOM   5619  O  OE2 . GLU B  1 147 ? 42.443  24.026  29.925  1.00 33.37 ? 164  GLU B OE2 1 
ATOM   5620  N  N   . ARG B  1 148 ? 38.107  20.931  33.056  1.00 27.21 ? 165  ARG B N   1 
ATOM   5621  C  CA  . ARG B  1 148 ? 37.939  21.287  34.456  1.00 28.38 ? 165  ARG B CA  1 
ATOM   5622  C  C   . ARG B  1 148 ? 36.856  20.423  35.094  1.00 28.55 ? 165  ARG B C   1 
ATOM   5623  O  O   . ARG B  1 148 ? 35.744  20.888  35.343  1.00 27.33 ? 165  ARG B O   1 
ATOM   5624  C  CB  . ARG B  1 148 ? 37.641  22.784  34.600  1.00 30.79 ? 165  ARG B CB  1 
ATOM   5625  C  CG  . ARG B  1 148 ? 37.610  23.240  36.052  1.00 34.49 ? 165  ARG B CG  1 
ATOM   5626  C  CD  . ARG B  1 148 ? 37.254  24.708  36.220  1.00 38.90 ? 165  ARG B CD  1 
ATOM   5627  N  NE  . ARG B  1 148 ? 36.028  25.153  35.544  1.00 43.43 ? 165  ARG B NE  1 
ATOM   5628  C  CZ  . ARG B  1 148 ? 34.775  24.796  35.821  1.00 48.08 ? 165  ARG B CZ  1 
ATOM   5629  N  NH1 . ARG B  1 148 ? 34.522  23.844  36.708  1.00 50.82 ? 165  ARG B NH1 1 
ATOM   5630  N  NH2 . ARG B  1 148 ? 33.770  25.389  35.186  1.00 46.85 ? 165  ARG B NH2 1 
ATOM   5631  N  N   . ILE B  1 149 ? 37.208  19.166  35.379  1.00 29.44 ? 166  ILE B N   1 
ATOM   5632  C  CA  . ILE B  1 149 ? 36.318  18.262  36.087  1.00 31.12 ? 166  ILE B CA  1 
ATOM   5633  C  C   . ILE B  1 149 ? 36.243  18.725  37.539  1.00 33.07 ? 166  ILE B C   1 
ATOM   5634  O  O   . ILE B  1 149 ? 37.268  18.851  38.206  1.00 33.58 ? 166  ILE B O   1 
ATOM   5635  C  CB  . ILE B  1 149 ? 36.780  16.795  35.969  1.00 31.16 ? 166  ILE B CB  1 
ATOM   5636  C  CG1 . ILE B  1 149 ? 36.870  16.335  34.509  1.00 31.56 ? 166  ILE B CG1 1 
ATOM   5637  C  CG2 . ILE B  1 149 ? 35.879  15.870  36.789  1.00 30.75 ? 166  ILE B CG2 1 
ATOM   5638  C  CD1 . ILE B  1 149 ? 35.550  16.366  33.757  1.00 32.81 ? 166  ILE B CD1 1 
ATOM   5639  N  N   . LEU B  1 150 ? 35.017  18.968  38.015  1.00 33.71 ? 167  LEU B N   1 
ATOM   5640  C  CA  . LEU B  1 150 ? 34.807  19.527  39.339  1.00 36.68 ? 167  LEU B CA  1 
ATOM   5641  C  C   . LEU B  1 150 ? 35.577  18.694  40.362  1.00 36.94 ? 167  LEU B C   1 
ATOM   5642  O  O   . LEU B  1 150 ? 35.286  17.514  40.556  1.00 35.66 ? 167  LEU B O   1 
ATOM   5643  C  CB  . LEU B  1 150 ? 33.313  19.588  39.654  1.00 38.20 ? 167  LEU B CB  1 
ATOM   5644  C  CG  . LEU B  1 150 ? 32.927  20.242  40.987  1.00 40.47 ? 167  LEU B CG  1 
ATOM   5645  C  CD1 . LEU B  1 150 ? 33.444  21.670  41.084  1.00 41.18 ? 167  LEU B CD1 1 
ATOM   5646  C  CD2 . LEU B  1 150 ? 31.417  20.219  41.184  1.00 41.72 ? 167  LEU B CD2 1 
ATOM   5647  N  N   . GLY B  1 151 ? 36.604  19.312  40.959  1.00 36.61 ? 168  GLY B N   1 
ATOM   5648  C  CA  . GLY B  1 151 ? 37.339  18.719  42.065  1.00 36.67 ? 168  GLY B CA  1 
ATOM   5649  C  C   . GLY B  1 151 ? 38.542  17.886  41.623  1.00 37.50 ? 168  GLY B C   1 
ATOM   5650  O  O   . GLY B  1 151 ? 39.269  17.386  42.478  1.00 38.78 ? 168  GLY B O   1 
ATOM   5651  N  N   . LEU B  1 152 ? 38.758  17.729  40.308  1.00 36.75 ? 169  LEU B N   1 
ATOM   5652  C  CA  . LEU B  1 152 ? 39.791  16.822  39.818  1.00 35.95 ? 169  LEU B CA  1 
ATOM   5653  C  C   . LEU B  1 152 ? 40.684  17.457  38.750  1.00 35.11 ? 169  LEU B C   1 
ATOM   5654  O  O   . LEU B  1 152 ? 41.800  16.983  38.545  1.00 36.39 ? 169  LEU B O   1 
ATOM   5655  C  CB  . LEU B  1 152 ? 39.125  15.545  39.305  1.00 36.39 ? 169  LEU B CB  1 
ATOM   5656  C  CG  . LEU B  1 152 ? 38.555  14.609  40.375  1.00 36.62 ? 169  LEU B CG  1 
ATOM   5657  C  CD1 . LEU B  1 152 ? 37.666  13.551  39.751  1.00 37.52 ? 169  LEU B CD1 1 
ATOM   5658  C  CD2 . LEU B  1 152 ? 39.664  13.951  41.181  1.00 36.55 ? 169  LEU B CD2 1 
ATOM   5659  N  N   . GLY B  1 153 ? 40.203  18.491  38.046  1.00 32.65 ? 170  GLY B N   1 
ATOM   5660  C  CA  . GLY B  1 153 ? 41.018  19.187  37.059  1.00 31.81 ? 170  GLY B CA  1 
ATOM   5661  C  C   . GLY B  1 153 ? 40.901  18.567  35.665  1.00 28.92 ? 170  GLY B C   1 
ATOM   5662  O  O   . GLY B  1 153 ? 39.817  18.154  35.258  1.00 26.05 ? 170  GLY B O   1 
ATOM   5663  N  N   . ASP B  1 154 ? 42.036  18.508  34.950  1.00 28.02 ? 171  ASP B N   1 
ATOM   5664  C  CA  . ASP B  1 154 ? 42.084  18.105  33.551  1.00 27.45 ? 171  ASP B CA  1 
ATOM   5665  C  C   . ASP B  1 154 ? 42.225  16.587  33.456  1.00 28.39 ? 171  ASP B C   1 
ATOM   5666  O  O   . ASP B  1 154 ? 43.293  16.044  33.725  1.00 29.89 ? 171  ASP B O   1 
ATOM   5667  C  CB  . ASP B  1 154 ? 43.212  18.830  32.828  1.00 26.59 ? 171  ASP B CB  1 
ATOM   5668  C  CG  . ASP B  1 154 ? 43.300  18.642  31.317  1.00 26.21 ? 171  ASP B CG  1 
ATOM   5669  O  OD1 . ASP B  1 154 ? 42.676  17.694  30.786  1.00 25.07 ? 171  ASP B OD1 1 
ATOM   5670  O  OD2 . ASP B  1 154 ? 43.981  19.466  30.668  1.00 25.39 ? 171  ASP B OD2 1 
ATOM   5671  N  N   . LEU B  1 155 ? 41.145  15.909  33.047  1.00 29.17 ? 172  LEU B N   1 
ATOM   5672  C  CA  . LEU B  1 155 ? 41.150  14.460  32.920  1.00 28.87 ? 172  LEU B CA  1 
ATOM   5673  C  C   . LEU B  1 155 ? 40.967  14.043  31.462  1.00 27.69 ? 172  LEU B C   1 
ATOM   5674  O  O   . LEU B  1 155 ? 40.870  12.856  31.174  1.00 27.33 ? 172  LEU B O   1 
ATOM   5675  C  CB  . LEU B  1 155 ? 40.057  13.857  33.802  1.00 30.49 ? 172  LEU B CB  1 
ATOM   5676  C  CG  . LEU B  1 155 ? 40.229  14.026  35.315  1.00 32.25 ? 172  LEU B CG  1 
ATOM   5677  C  CD1 . LEU B  1 155 ? 39.095  13.316  36.037  1.00 33.05 ? 172  LEU B CD1 1 
ATOM   5678  C  CD2 . LEU B  1 155 ? 41.567  13.511  35.812  1.00 32.59 ? 172  LEU B CD2 1 
ATOM   5679  N  N   . GLY B  1 156 ? 40.917  15.016  30.548  1.00 26.93 ? 173  GLY B N   1 
ATOM   5680  C  CA  . GLY B  1 156 ? 40.701  14.741  29.138  1.00 27.42 ? 173  GLY B CA  1 
ATOM   5681  C  C   . GLY B  1 156 ? 39.502  13.819  28.921  1.00 27.92 ? 173  GLY B C   1 
ATOM   5682  O  O   . GLY B  1 156 ? 38.437  14.030  29.502  1.00 26.01 ? 173  GLY B O   1 
ATOM   5683  N  N   . VAL B  1 157 ? 39.709  12.784  28.096  1.00 26.31 ? 174  VAL B N   1 
ATOM   5684  C  CA  . VAL B  1 157 ? 38.665  11.838  27.735  1.00 28.18 ? 174  VAL B CA  1 
ATOM   5685  C  C   . VAL B  1 157 ? 38.241  11.002  28.943  1.00 28.28 ? 174  VAL B C   1 
ATOM   5686  O  O   . VAL B  1 157 ? 37.139  10.460  28.947  1.00 28.82 ? 174  VAL B O   1 
ATOM   5687  C  CB  . VAL B  1 157 ? 39.153  10.961  26.568  1.00 29.01 ? 174  VAL B CB  1 
ATOM   5688  C  CG1 . VAL B  1 157 ? 38.273  9.747   26.329  1.00 30.45 ? 174  VAL B CG1 1 
ATOM   5689  C  CG2 . VAL B  1 157 ? 39.280  11.780  25.294  1.00 30.30 ? 174  VAL B CG2 1 
ATOM   5690  N  N   . TYR B  1 158 ? 39.078  10.938  29.988  1.00 29.12 ? 175  TYR B N   1 
ATOM   5691  C  CA  . TYR B  1 158 ? 38.694  10.261  31.217  1.00 31.79 ? 175  TYR B CA  1 
ATOM   5692  C  C   . TYR B  1 158 ? 37.570  11.020  31.932  1.00 32.18 ? 175  TYR B C   1 
ATOM   5693  O  O   . TYR B  1 158 ? 37.194  10.625  33.031  1.00 37.79 ? 175  TYR B O   1 
ATOM   5694  C  CB  . TYR B  1 158 ? 39.870  10.062  32.185  1.00 33.46 ? 175  TYR B CB  1 
ATOM   5695  C  CG  . TYR B  1 158 ? 40.864  8.934   31.928  1.00 34.33 ? 175  TYR B CG  1 
ATOM   5696  C  CD1 . TYR B  1 158 ? 40.643  7.930   30.987  1.00 36.13 ? 175  TYR B CD1 1 
ATOM   5697  C  CD2 . TYR B  1 158 ? 42.017  8.842   32.697  1.00 36.38 ? 175  TYR B CD2 1 
ATOM   5698  C  CE1 . TYR B  1 158 ? 41.557  6.903   30.796  1.00 35.32 ? 175  TYR B CE1 1 
ATOM   5699  C  CE2 . TYR B  1 158 ? 42.933  7.818   32.521  1.00 37.21 ? 175  TYR B CE2 1 
ATOM   5700  C  CZ  . TYR B  1 158 ? 42.703  6.843   31.568  1.00 37.16 ? 175  TYR B CZ  1 
ATOM   5701  O  OH  . TYR B  1 158 ? 43.622  5.843   31.411  1.00 38.50 ? 175  TYR B OH  1 
ATOM   5702  N  N   A GLY B  1 159 ? 37.088  12.123  31.338  0.50 30.90 ? 176  GLY B N   1 
ATOM   5703  N  N   B GLY B  1 159 ? 37.016  12.061  31.288  0.50 30.86 ? 176  GLY B N   1 
ATOM   5704  C  CA  A GLY B  1 159 ? 35.922  12.838  31.831  0.50 30.08 ? 176  GLY B CA  1 
ATOM   5705  C  CA  B GLY B  1 159 ? 35.945  12.862  31.857  0.50 29.84 ? 176  GLY B CA  1 
ATOM   5706  C  C   A GLY B  1 159 ? 34.654  12.436  31.078  0.50 29.80 ? 176  GLY B C   1 
ATOM   5707  C  C   B GLY B  1 159 ? 34.596  12.634  31.171  0.50 29.41 ? 176  GLY B C   1 
ATOM   5708  O  O   A GLY B  1 159 ? 33.620  13.091  31.200  0.50 27.90 ? 176  GLY B O   1 
ATOM   5709  O  O   B GLY B  1 159 ? 33.616  13.289  31.517  0.50 27.57 ? 176  GLY B O   1 
ATOM   5710  N  N   A MET B  1 160 ? 34.741  11.338  30.317  0.50 28.60 ? 177  MET B N   1 
ATOM   5711  N  N   B MET B  1 160 ? 34.522  11.700  30.213  0.50 28.27 ? 177  MET B N   1 
ATOM   5712  C  CA  A MET B  1 160 ? 33.624  10.862  29.514  0.50 28.26 ? 177  MET B CA  1 
ATOM   5713  C  CA  B MET B  1 160 ? 33.248  11.447  29.556  0.50 27.26 ? 177  MET B CA  1 
ATOM   5714  C  C   A MET B  1 160 ? 32.415  10.557  30.403  0.50 27.89 ? 177  MET B C   1 
ATOM   5715  C  C   B MET B  1 160 ? 32.238  10.878  30.550  0.50 27.35 ? 177  MET B C   1 
ATOM   5716  O  O   A MET B  1 160 ? 31.286  10.509  29.922  0.50 29.43 ? 177  MET B O   1 
ATOM   5717  O  O   B MET B  1 160 ? 31.040  10.961  30.291  0.50 28.55 ? 177  MET B O   1 
ATOM   5718  C  CB  A MET B  1 160 ? 34.031  9.616   28.712  0.50 27.39 ? 177  MET B CB  1 
ATOM   5719  C  CB  B MET B  1 160 ? 33.329  10.477  28.370  0.50 26.25 ? 177  MET B CB  1 
ATOM   5720  C  CG  A MET B  1 160 ? 34.526  8.444   29.549  0.50 27.54 ? 177  MET B CG  1 
ATOM   5721  C  CG  B MET B  1 160 ? 31.959  9.910   27.959  0.50 25.19 ? 177  MET B CG  1 
ATOM   5722  S  SD  A MET B  1 160 ? 34.711  6.918   28.598  0.50 28.36 ? 177  MET B SD  1 
ATOM   5723  S  SD  B MET B  1 160 ? 30.804  11.043  27.148  0.50 22.78 ? 177  MET B SD  1 
ATOM   5724  C  CE  A MET B  1 160 ? 36.276  7.239   27.774  0.50 27.32 ? 177  MET B CE  1 
ATOM   5725  C  CE  B MET B  1 160 ? 30.932  10.442  25.461  0.50 22.56 ? 177  MET B CE  1 
ATOM   5726  N  N   . GLY B  1 161 ? 32.684  10.334  31.694  1.00 26.59 ? 178  GLY B N   1 
ATOM   5727  C  CA  . GLY B  1 161 ? 31.714  9.863   32.672  1.00 26.49 ? 178  GLY B CA  1 
ATOM   5728  C  C   . GLY B  1 161 ? 30.789  10.973  33.177  1.00 25.36 ? 178  GLY B C   1 
ATOM   5729  O  O   . GLY B  1 161 ? 29.679  10.687  33.623  1.00 23.56 ? 178  GLY B O   1 
ATOM   5730  N  N   . ILE B  1 162 ? 31.242  12.234  33.091  1.00 25.14 ? 179  ILE B N   1 
ATOM   5731  C  CA  . ILE B  1 162 ? 30.547  13.351  33.714  1.00 25.10 ? 179  ILE B CA  1 
ATOM   5732  C  C   . ILE B  1 162 ? 29.240  13.639  32.970  1.00 24.40 ? 179  ILE B C   1 
ATOM   5733  O  O   . ILE B  1 162 ? 28.192  13.722  33.610  1.00 24.09 ? 179  ILE B O   1 
ATOM   5734  C  CB  . ILE B  1 162 ? 31.473  14.580  33.851  1.00 25.25 ? 179  ILE B CB  1 
ATOM   5735  C  CG1 . ILE B  1 162 ? 32.302  14.506  35.139  1.00 26.21 ? 179  ILE B CG1 1 
ATOM   5736  C  CG2 . ILE B  1 162 ? 30.698  15.898  33.788  1.00 25.76 ? 179  ILE B CG2 1 
ATOM   5737  C  CD1 . ILE B  1 162 ? 33.288  13.351  35.189  1.00 26.81 ? 179  ILE B CD1 1 
ATOM   5738  N  N   . PRO B  1 163 ? 29.235  13.817  31.627  1.00 23.77 ? 180  PRO B N   1 
ATOM   5739  C  CA  . PRO B  1 163 ? 27.980  13.959  30.878  1.00 23.51 ? 180  PRO B CA  1 
ATOM   5740  C  C   . PRO B  1 163 ? 26.996  12.802  31.067  1.00 22.03 ? 180  PRO B C   1 
ATOM   5741  O  O   . PRO B  1 163 ? 25.788  13.024  31.149  1.00 19.85 ? 180  PRO B O   1 
ATOM   5742  C  CB  . PRO B  1 163 ? 28.459  14.081  29.423  1.00 24.18 ? 180  PRO B CB  1 
ATOM   5743  C  CG  . PRO B  1 163 ? 29.838  14.667  29.540  1.00 24.99 ? 180  PRO B CG  1 
ATOM   5744  C  CD  . PRO B  1 163 ? 30.418  14.012  30.774  1.00 25.05 ? 180  PRO B CD  1 
ATOM   5745  N  N   . VAL B  1 164 ? 27.529  11.576  31.143  1.00 21.53 ? 181  VAL B N   1 
ATOM   5746  C  CA  . VAL B  1 164 ? 26.730  10.376  31.340  1.00 22.07 ? 181  VAL B CA  1 
ATOM   5747  C  C   . VAL B  1 164 ? 26.006  10.463  32.682  1.00 21.36 ? 181  VAL B C   1 
ATOM   5748  O  O   . VAL B  1 164 ? 24.798  10.234  32.751  1.00 20.52 ? 181  VAL B O   1 
ATOM   5749  C  CB  . VAL B  1 164 ? 27.603  9.105   31.247  1.00 23.54 ? 181  VAL B CB  1 
ATOM   5750  C  CG1 . VAL B  1 164 ? 26.830  7.836   31.594  1.00 23.64 ? 181  VAL B CG1 1 
ATOM   5751  C  CG2 . VAL B  1 164 ? 28.258  8.956   29.879  1.00 23.69 ? 181  VAL B CG2 1 
ATOM   5752  N  N   . GLY B  1 165 ? 26.755  10.786  33.745  1.00 21.22 ? 182  GLY B N   1 
ATOM   5753  C  CA  . GLY B  1 165 ? 26.199  10.877  35.086  1.00 21.25 ? 182  GLY B CA  1 
ATOM   5754  C  C   . GLY B  1 165 ? 25.179  12.008  35.207  1.00 22.43 ? 182  GLY B C   1 
ATOM   5755  O  O   . GLY B  1 165 ? 24.144  11.853  35.861  1.00 22.76 ? 182  GLY B O   1 
ATOM   5756  N  N   . LYS B  1 166 ? 25.502  13.143  34.583  1.00 21.56 ? 183  LYS B N   1 
ATOM   5757  C  CA  . LYS B  1 166 ? 24.665  14.331  34.612  1.00 22.47 ? 183  LYS B CA  1 
ATOM   5758  C  C   . LYS B  1 166 ? 23.297  14.022  34.011  1.00 21.42 ? 183  LYS B C   1 
ATOM   5759  O  O   . LYS B  1 166 ? 22.265  14.360  34.598  1.00 20.05 ? 183  LYS B O   1 
ATOM   5760  C  CB  . LYS B  1 166 ? 25.345  15.444  33.809  1.00 22.88 ? 183  LYS B CB  1 
ATOM   5761  C  CG  . LYS B  1 166 ? 24.686  16.806  33.895  1.00 24.57 ? 183  LYS B CG  1 
ATOM   5762  C  CD  . LYS B  1 166 ? 24.963  17.480  35.228  1.00 25.65 ? 183  LYS B CD  1 
ATOM   5763  C  CE  . LYS B  1 166 ? 24.744  18.957  35.208  1.00 26.27 ? 183  LYS B CE  1 
ATOM   5764  N  NZ  . LYS B  1 166 ? 25.365  19.544  36.394  1.00 26.52 ? 183  LYS B NZ  1 
ATOM   5765  N  N   . LEU B  1 167 ? 23.305  13.387  32.833  1.00 20.68 ? 184  LEU B N   1 
ATOM   5766  C  CA  . LEU B  1 167 ? 22.077  13.043  32.138  1.00 21.54 ? 184  LEU B CA  1 
ATOM   5767  C  C   . LEU B  1 167 ? 21.296  11.961  32.881  1.00 22.31 ? 184  LEU B C   1 
ATOM   5768  O  O   . LEU B  1 167 ? 20.074  11.948  32.781  1.00 22.30 ? 184  LEU B O   1 
ATOM   5769  C  CB  . LEU B  1 167 ? 22.372  12.658  30.690  1.00 21.32 ? 184  LEU B CB  1 
ATOM   5770  C  CG  . LEU B  1 167 ? 22.744  13.840  29.788  1.00 20.50 ? 184  LEU B CG  1 
ATOM   5771  C  CD1 . LEU B  1 167 ? 23.359  13.372  28.492  1.00 20.69 ? 184  LEU B CD1 1 
ATOM   5772  C  CD2 . LEU B  1 167 ? 21.519  14.721  29.519  1.00 20.51 ? 184  LEU B CD2 1 
ATOM   5773  N  N   . CYS B  1 168 ? 21.981  11.074  33.619  1.00 22.19 ? 185  CYS B N   1 
ATOM   5774  C  CA  . CYS B  1 168 ? 21.296  10.127  34.493  1.00 24.20 ? 185  CYS B CA  1 
ATOM   5775  C  C   . CYS B  1 168 ? 20.396  10.877  35.479  1.00 23.12 ? 185  CYS B C   1 
ATOM   5776  O  O   . CYS B  1 168 ? 19.291  10.424  35.775  1.00 24.50 ? 185  CYS B O   1 
ATOM   5777  C  CB  . CYS B  1 168 ? 22.268  9.214   35.238  1.00 25.67 ? 185  CYS B CB  1 
ATOM   5778  S  SG  . CYS B  1 168 ? 23.060  7.959   34.193  1.00 28.89 ? 185  CYS B SG  1 
ATOM   5779  N  N   . LEU B  1 169 ? 20.859  12.042  35.953  1.00 22.16 ? 186  LEU B N   1 
ATOM   5780  C  CA  . LEU B  1 169 ? 20.109  12.848  36.905  1.00 22.53 ? 186  LEU B CA  1 
ATOM   5781  C  C   . LEU B  1 169 ? 19.017  13.660  36.211  1.00 21.85 ? 186  LEU B C   1 
ATOM   5782  O  O   . LEU B  1 169 ? 17.982  13.914  36.818  1.00 22.07 ? 186  LEU B O   1 
ATOM   5783  C  CB  . LEU B  1 169 ? 21.054  13.744  37.706  1.00 24.15 ? 186  LEU B CB  1 
ATOM   5784  C  CG  . LEU B  1 169 ? 22.123  13.012  38.525  1.00 25.53 ? 186  LEU B CG  1 
ATOM   5785  C  CD1 . LEU B  1 169 ? 22.962  14.006  39.304  1.00 26.85 ? 186  LEU B CD1 1 
ATOM   5786  C  CD2 . LEU B  1 169 ? 21.519  11.987  39.456  1.00 26.59 ? 186  LEU B CD2 1 
ATOM   5787  N  N   . TYR B  1 170 ? 19.241  14.077  34.958  1.00 20.91 ? 187  TYR B N   1 
ATOM   5788  C  CA  . TYR B  1 170 ? 18.173  14.660  34.157  1.00 21.19 ? 187  TYR B CA  1 
ATOM   5789  C  C   . TYR B  1 170 ? 16.962  13.720  34.164  1.00 20.85 ? 187  TYR B C   1 
ATOM   5790  O  O   . TYR B  1 170 ? 15.824  14.157  34.345  1.00 19.83 ? 187  TYR B O   1 
ATOM   5791  C  CB  . TYR B  1 170 ? 18.563  14.891  32.694  1.00 21.27 ? 187  TYR B CB  1 
ATOM   5792  C  CG  . TYR B  1 170 ? 19.309  16.170  32.332  1.00 21.95 ? 187  TYR B CG  1 
ATOM   5793  C  CD1 . TYR B  1 170 ? 20.418  16.616  33.043  1.00 21.90 ? 187  TYR B CD1 1 
ATOM   5794  C  CD2 . TYR B  1 170 ? 18.906  16.917  31.231  1.00 22.47 ? 187  TYR B CD2 1 
ATOM   5795  C  CE1 . TYR B  1 170 ? 21.092  17.775  32.673  1.00 22.24 ? 187  TYR B CE1 1 
ATOM   5796  C  CE2 . TYR B  1 170 ? 19.562  18.078  30.857  1.00 22.46 ? 187  TYR B CE2 1 
ATOM   5797  C  CZ  . TYR B  1 170 ? 20.657  18.512  31.582  1.00 23.08 ? 187  TYR B CZ  1 
ATOM   5798  O  OH  . TYR B  1 170 ? 21.278  19.662  31.171  1.00 22.62 ? 187  TYR B OH  1 
ATOM   5799  N  N   . THR B  1 171 ? 17.214  12.423  33.948  1.00 20.65 ? 188  THR B N   1 
ATOM   5800  C  CA  . THR B  1 171 ? 16.143  11.436  33.876  1.00 21.32 ? 188  THR B CA  1 
ATOM   5801  C  C   . THR B  1 171 ? 15.603  11.138  35.274  1.00 21.78 ? 188  THR B C   1 
ATOM   5802  O  O   . THR B  1 171 ? 14.391  11.211  35.496  1.00 20.68 ? 188  THR B O   1 
ATOM   5803  C  CB  . THR B  1 171 ? 16.634  10.171  33.174  1.00 21.57 ? 188  THR B CB  1 
ATOM   5804  O  OG1 . THR B  1 171 ? 16.951  10.538  31.834  1.00 22.89 ? 188  THR B OG1 1 
ATOM   5805  C  CG2 . THR B  1 171 ? 15.586  9.077   33.123  1.00 21.42 ? 188  THR B CG2 1 
ATOM   5806  N  N   . ALA B  1 172 ? 16.497  10.782  36.206  1.00 21.81 ? 189  ALA B N   1 
ATOM   5807  C  CA  . ALA B  1 172 ? 16.079  10.324  37.524  1.00 22.94 ? 189  ALA B CA  1 
ATOM   5808  C  C   . ALA B  1 172 ? 15.270  11.397  38.254  1.00 23.35 ? 189  ALA B C   1 
ATOM   5809  O  O   . ALA B  1 172 ? 14.296  11.069  38.931  1.00 24.18 ? 189  ALA B O   1 
ATOM   5810  C  CB  . ALA B  1 172 ? 17.279  9.902   38.343  1.00 23.20 ? 189  ALA B CB  1 
ATOM   5811  N  N   . CYS B  1 173 ? 15.671  12.669  38.103  1.00 22.33 ? 190  CYS B N   1 
ATOM   5812  C  CA  . CYS B  1 173 ? 15.138  13.752  38.914  1.00 22.50 ? 190  CYS B CA  1 
ATOM   5813  C  C   . CYS B  1 173 ? 13.933  14.424  38.248  1.00 22.31 ? 190  CYS B C   1 
ATOM   5814  O  O   . CYS B  1 173 ? 13.004  14.827  38.948  1.00 22.27 ? 190  CYS B O   1 
ATOM   5815  C  CB  . CYS B  1 173 ? 16.211  14.783  39.261  1.00 23.16 ? 190  CYS B CB  1 
ATOM   5816  S  SG  . CYS B  1 173 ? 17.605  14.108  40.211  1.00 24.76 ? 190  CYS B SG  1 
ATOM   5817  N  N   . ALA B  1 174 ? 13.943  14.569  36.913  1.00 21.43 ? 191  ALA B N   1 
ATOM   5818  C  CA  . ALA B  1 174 ? 12.923  15.368  36.241  1.00 21.04 ? 191  ALA B CA  1 
ATOM   5819  C  C   . ALA B  1 174 ? 12.151  14.585  35.175  1.00 21.23 ? 191  ALA B C   1 
ATOM   5820  O  O   . ALA B  1 174 ? 11.271  15.147  34.525  1.00 21.84 ? 191  ALA B O   1 
ATOM   5821  C  CB  . ALA B  1 174 ? 13.563  16.600  35.638  1.00 20.31 ? 191  ALA B CB  1 
ATOM   5822  N  N   . GLY B  1 175 ? 12.463  13.302  34.977  1.00 20.66 ? 192  GLY B N   1 
ATOM   5823  C  CA  . GLY B  1 175 ? 11.717  12.483  34.031  1.00 20.68 ? 192  GLY B CA  1 
ATOM   5824  C  C   . GLY B  1 175 ? 11.940  12.885  32.572  1.00 20.81 ? 192  GLY B C   1 
ATOM   5825  O  O   . GLY B  1 175 ? 11.065  12.703  31.730  1.00 20.39 ? 192  GLY B O   1 
ATOM   5826  N  N   . ILE B  1 176 ? 13.121  13.424  32.262  1.00 21.14 ? 193  ILE B N   1 
ATOM   5827  C  CA  . ILE B  1 176 ? 13.516  13.593  30.877  1.00 20.75 ? 193  ILE B CA  1 
ATOM   5828  C  C   . ILE B  1 176 ? 13.800  12.201  30.323  1.00 21.02 ? 193  ILE B C   1 
ATOM   5829  O  O   . ILE B  1 176 ? 14.468  11.397  30.967  1.00 21.66 ? 193  ILE B O   1 
ATOM   5830  C  CB  . ILE B  1 176 ? 14.698  14.575  30.768  1.00 21.19 ? 193  ILE B CB  1 
ATOM   5831  C  CG1 . ILE B  1 176 ? 14.264  15.973  31.264  1.00 21.35 ? 193  ILE B CG1 1 
ATOM   5832  C  CG2 . ILE B  1 176 ? 15.266  14.624  29.348  1.00 20.20 ? 193  ILE B CG2 1 
ATOM   5833  C  CD1 . ILE B  1 176 ? 15.397  16.929  31.560  1.00 21.80 ? 193  ILE B CD1 1 
ATOM   5834  N  N   . ARG B  1 177 ? 13.236  11.907  29.148  1.00 21.90 ? 194  ARG B N   1 
ATOM   5835  C  CA  . ARG B  1 177 ? 13.318  10.578  28.571  1.00 22.99 ? 194  ARG B CA  1 
ATOM   5836  C  C   . ARG B  1 177 ? 14.772  10.223  28.271  1.00 22.10 ? 194  ARG B C   1 
ATOM   5837  O  O   . ARG B  1 177 ? 15.472  10.973  27.592  1.00 21.48 ? 194  ARG B O   1 
ATOM   5838  C  CB  . ARG B  1 177 ? 12.525  10.479  27.267  1.00 24.23 ? 194  ARG B CB  1 
ATOM   5839  C  CG  . ARG B  1 177 ? 11.014  10.559  27.424  1.00 26.65 ? 194  ARG B CG  1 
ATOM   5840  C  CD  . ARG B  1 177 ? 10.285  10.398  26.096  1.00 27.94 ? 194  ARG B CD  1 
ATOM   5841  N  NE  . ARG B  1 177 ? 10.697  9.168   25.408  1.00 30.36 ? 194  ARG B NE  1 
ATOM   5842  C  CZ  . ARG B  1 177 ? 10.071  8.601   24.381  1.00 36.07 ? 194  ARG B CZ  1 
ATOM   5843  N  NH1 . ARG B  1 177 ? 8.963   9.132   23.886  1.00 37.13 ? 194  ARG B NH1 1 
ATOM   5844  N  NH2 . ARG B  1 177 ? 10.544  7.479   23.867  1.00 37.57 ? 194  ARG B NH2 1 
ATOM   5845  N  N   . PRO B  1 178 ? 15.262  9.059   28.750  1.00 22.40 ? 195  PRO B N   1 
ATOM   5846  C  CA  . PRO B  1 178 ? 16.656  8.672   28.531  1.00 22.71 ? 195  PRO B CA  1 
ATOM   5847  C  C   . PRO B  1 178 ? 17.043  8.536   27.059  1.00 22.29 ? 195  PRO B C   1 
ATOM   5848  O  O   . PRO B  1 178 ? 18.150  8.919   26.698  1.00 22.54 ? 195  PRO B O   1 
ATOM   5849  C  CB  . PRO B  1 178 ? 16.861  7.355   29.304  1.00 22.59 ? 195  PRO B CB  1 
ATOM   5850  C  CG  . PRO B  1 178 ? 15.486  6.944   29.792  1.00 23.19 ? 195  PRO B CG  1 
ATOM   5851  C  CD  . PRO B  1 178 ? 14.522  8.103   29.582  1.00 22.52 ? 195  PRO B CD  1 
ATOM   5852  N  N   . ASP B  1 179 ? 16.135  8.026   26.211  1.00 22.77 ? 196  ASP B N   1 
ATOM   5853  C  CA  . ASP B  1 179 ? 16.432  7.863   24.793  1.00 24.03 ? 196  ASP B CA  1 
ATOM   5854  C  C   . ASP B  1 179 ? 16.615  9.218   24.104  1.00 23.15 ? 196  ASP B C   1 
ATOM   5855  O  O   . ASP B  1 179 ? 17.090  9.261   22.972  1.00 25.10 ? 196  ASP B O   1 
ATOM   5856  C  CB  . ASP B  1 179 ? 15.410  7.004   24.057  1.00 25.90 ? 196  ASP B CB  1 
ATOM   5857  C  CG  . ASP B  1 179 ? 13.980  7.528   23.986  1.00 28.85 ? 196  ASP B CG  1 
ATOM   5858  O  OD1 . ASP B  1 179 ? 13.665  8.499   24.698  1.00 31.24 ? 196  ASP B OD1 1 
ATOM   5859  O  OD2 . ASP B  1 179 ? 13.180  6.950   23.223  1.00 30.15 ? 196  ASP B OD2 1 
ATOM   5860  N  N   . ARG B  1 180 ? 16.240  10.315  24.777  1.00 22.01 ? 197  ARG B N   1 
ATOM   5861  C  CA  . ARG B  1 180 ? 16.373  11.653  24.212  1.00 21.98 ? 197  ARG B CA  1 
ATOM   5862  C  C   . ARG B  1 180 ? 17.562  12.416  24.802  1.00 20.13 ? 197  ARG B C   1 
ATOM   5863  O  O   . ARG B  1 180 ? 17.709  13.609  24.540  1.00 18.47 ? 197  ARG B O   1 
ATOM   5864  C  CB  . ARG B  1 180 ? 15.035  12.372  24.398  1.00 23.48 ? 197  ARG B CB  1 
ATOM   5865  C  CG  . ARG B  1 180 ? 13.965  11.645  23.600  1.00 26.31 ? 197  ARG B CG  1 
ATOM   5866  C  CD  . ARG B  1 180 ? 12.736  12.479  23.358  1.00 29.51 ? 197  ARG B CD  1 
ATOM   5867  N  NE  . ARG B  1 180 ? 11.717  11.714  22.634  1.00 30.55 ? 197  ARG B NE  1 
ATOM   5868  C  CZ  . ARG B  1 180 ? 10.442  12.081  22.539  1.00 34.51 ? 197  ARG B CZ  1 
ATOM   5869  N  NH1 . ARG B  1 180 ? 10.039  13.234  23.055  1.00 34.10 ? 197  ARG B NH1 1 
ATOM   5870  N  NH2 . ARG B  1 180 ? 9.574   11.292  21.925  1.00 35.06 ? 197  ARG B NH2 1 
ATOM   5871  N  N   . CYS B  1 181 ? 18.429  11.714  25.547  1.00 19.49 ? 198  CYS B N   1 
ATOM   5872  C  CA  . CYS B  1 181 ? 19.601  12.309  26.170  1.00 20.11 ? 198  CYS B CA  1 
ATOM   5873  C  C   . CYS B  1 181 ? 20.858  11.890  25.408  1.00 19.58 ? 198  CYS B C   1 
ATOM   5874  O  O   . CYS B  1 181 ? 20.990  10.724  25.032  1.00 19.05 ? 198  CYS B O   1 
ATOM   5875  C  CB  . CYS B  1 181 ? 19.703  11.884  27.630  1.00 21.20 ? 198  CYS B CB  1 
ATOM   5876  S  SG  . CYS B  1 181 ? 18.387  12.568  28.673  1.00 22.03 ? 198  CYS B SG  1 
ATOM   5877  N  N   . LEU B  1 182 ? 21.785  12.839  25.205  1.00 19.21 ? 199  LEU B N   1 
ATOM   5878  C  CA  . LEU B  1 182 ? 23.008  12.574  24.455  1.00 19.10 ? 199  LEU B CA  1 
ATOM   5879  C  C   . LEU B  1 182 ? 24.217  13.144  25.197  1.00 18.95 ? 199  LEU B C   1 
ATOM   5880  O  O   . LEU B  1 182 ? 24.440  14.350  25.192  1.00 18.22 ? 199  LEU B O   1 
ATOM   5881  C  CB  . LEU B  1 182 ? 22.889  13.148  23.043  1.00 19.83 ? 199  LEU B CB  1 
ATOM   5882  C  CG  . LEU B  1 182 ? 24.159  13.105  22.183  1.00 20.27 ? 199  LEU B CG  1 
ATOM   5883  C  CD1 . LEU B  1 182 ? 24.707  11.700  22.031  1.00 20.39 ? 199  LEU B CD1 1 
ATOM   5884  C  CD2 . LEU B  1 182 ? 23.889  13.702  20.825  1.00 21.31 ? 199  LEU B CD2 1 
ATOM   5885  N  N   . PRO B  1 183 ? 25.046  12.300  25.851  1.00 18.26 ? 200  PRO B N   1 
ATOM   5886  C  CA  . PRO B  1 183 ? 26.309  12.756  26.430  1.00 18.57 ? 200  PRO B CA  1 
ATOM   5887  C  C   . PRO B  1 183 ? 27.366  12.863  25.329  1.00 18.97 ? 200  PRO B C   1 
ATOM   5888  O  O   . PRO B  1 183 ? 27.400  12.038  24.402  1.00 17.06 ? 200  PRO B O   1 
ATOM   5889  C  CB  . PRO B  1 183 ? 26.664  11.692  27.488  1.00 19.18 ? 200  PRO B CB  1 
ATOM   5890  C  CG  . PRO B  1 183 ? 25.655  10.572  27.302  1.00 19.19 ? 200  PRO B CG  1 
ATOM   5891  C  CD  . PRO B  1 183 ? 24.810  10.870  26.084  1.00 18.74 ? 200  PRO B CD  1 
ATOM   5892  N  N   . VAL B  1 184 ? 28.220  13.891  25.443  1.00 19.16 ? 201  VAL B N   1 
ATOM   5893  C  CA  . VAL B  1 184 ? 29.207  14.194  24.416  1.00 19.38 ? 201  VAL B CA  1 
ATOM   5894  C  C   . VAL B  1 184 ? 30.525  14.565  25.087  1.00 19.92 ? 201  VAL B C   1 
ATOM   5895  O  O   . VAL B  1 184 ? 30.558  15.401  25.990  1.00 18.83 ? 201  VAL B O   1 
ATOM   5896  C  CB  . VAL B  1 184 ? 28.775  15.325  23.461  1.00 19.61 ? 201  VAL B CB  1 
ATOM   5897  C  CG1 . VAL B  1 184 ? 29.850  15.621  22.421  1.00 19.26 ? 201  VAL B CG1 1 
ATOM   5898  C  CG2 . VAL B  1 184 ? 27.443  15.039  22.784  1.00 19.73 ? 201  VAL B CG2 1 
ATOM   5899  N  N   . CYS B  1 185 ? 31.613  13.965  24.591  1.00 21.39 ? 202  CYS B N   1 
ATOM   5900  C  CA  . CYS B  1 185 ? 32.953  14.303  25.032  1.00 23.03 ? 202  CYS B CA  1 
ATOM   5901  C  C   . CYS B  1 185 ? 33.765  14.796  23.836  1.00 23.04 ? 202  CYS B C   1 
ATOM   5902  O  O   . CYS B  1 185 ? 33.880  14.107  22.824  1.00 22.50 ? 202  CYS B O   1 
ATOM   5903  C  CB  . CYS B  1 185 ? 33.602  13.113  25.721  1.00 26.16 ? 202  CYS B CB  1 
ATOM   5904  S  SG  . CYS B  1 185 ? 35.280  13.472  26.299  1.00 31.28 ? 202  CYS B SG  1 
ATOM   5905  N  N   . ILE B  1 186 ? 34.291  16.020  23.945  1.00 23.12 ? 203  ILE B N   1 
ATOM   5906  C  CA  . ILE B  1 186 ? 35.119  16.603  22.905  1.00 24.13 ? 203  ILE B CA  1 
ATOM   5907  C  C   . ILE B  1 186 ? 36.579  16.460  23.335  1.00 24.61 ? 203  ILE B C   1 
ATOM   5908  O  O   . ILE B  1 186 ? 36.945  16.888  24.426  1.00 25.46 ? 203  ILE B O   1 
ATOM   5909  C  CB  . ILE B  1 186 ? 34.682  18.056  22.632  1.00 26.32 ? 203  ILE B CB  1 
ATOM   5910  C  CG1 . ILE B  1 186 ? 33.266  18.075  22.025  1.00 27.24 ? 203  ILE B CG1 1 
ATOM   5911  C  CG2 . ILE B  1 186 ? 35.691  18.793  21.746  1.00 26.76 ? 203  ILE B CG2 1 
ATOM   5912  C  CD1 . ILE B  1 186 ? 32.679  19.453  21.803  1.00 28.87 ? 203  ILE B CD1 1 
ATOM   5913  N  N   . ASP B  1 187 ? 37.391  15.818  22.486  1.00 24.31 ? 204  ASP B N   1 
ATOM   5914  C  CA  . ASP B  1 187 ? 38.787  15.536  22.791  1.00 24.18 ? 204  ASP B CA  1 
ATOM   5915  C  C   . ASP B  1 187 ? 39.701  16.366  21.893  1.00 23.76 ? 204  ASP B C   1 
ATOM   5916  O  O   . ASP B  1 187 ? 39.838  16.081  20.702  1.00 23.19 ? 204  ASP B O   1 
ATOM   5917  C  CB  . ASP B  1 187 ? 39.132  14.067  22.608  1.00 25.33 ? 204  ASP B CB  1 
ATOM   5918  C  CG  . ASP B  1 187 ? 40.564  13.684  22.969  1.00 26.92 ? 204  ASP B CG  1 
ATOM   5919  O  OD1 . ASP B  1 187 ? 41.269  14.513  23.602  1.00 26.50 ? 204  ASP B OD1 1 
ATOM   5920  O  OD2 . ASP B  1 187 ? 40.968  12.554  22.620  1.00 27.11 ? 204  ASP B OD2 1 
ATOM   5921  N  N   . VAL B  1 188 ? 40.346  17.374  22.490  1.00 22.82 ? 205  VAL B N   1 
ATOM   5922  C  CA  . VAL B  1 188 ? 41.302  18.207  21.777  1.00 22.99 ? 205  VAL B CA  1 
ATOM   5923  C  C   . VAL B  1 188 ? 42.701  18.024  22.368  1.00 23.47 ? 205  VAL B C   1 
ATOM   5924  O  O   . VAL B  1 188 ? 43.605  18.811  22.079  1.00 24.81 ? 205  VAL B O   1 
ATOM   5925  C  CB  . VAL B  1 188 ? 40.850  19.675  21.826  1.00 23.42 ? 205  VAL B CB  1 
ATOM   5926  C  CG1 . VAL B  1 188 ? 39.496  19.855  21.143  1.00 23.61 ? 205  VAL B CG1 1 
ATOM   5927  C  CG2 . VAL B  1 188 ? 40.828  20.218  23.252  1.00 23.40 ? 205  VAL B CG2 1 
ATOM   5928  N  N   . GLY B  1 189 ? 42.872  16.983  23.191  1.00 22.66 ? 206  GLY B N   1 
ATOM   5929  C  CA  . GLY B  1 189 ? 44.108  16.766  23.924  1.00 23.47 ? 206  GLY B CA  1 
ATOM   5930  C  C   . GLY B  1 189 ? 43.908  16.959  25.425  1.00 24.20 ? 206  GLY B C   1 
ATOM   5931  O  O   . GLY B  1 189 ? 42.801  17.254  25.874  1.00 23.79 ? 206  GLY B O   1 
ATOM   5932  N  N   . THR B  1 190 ? 44.992  16.777  26.187  1.00 23.90 ? 207  THR B N   1 
ATOM   5933  C  CA  . THR B  1 190 ? 45.003  17.020  27.620  1.00 25.58 ? 207  THR B CA  1 
ATOM   5934  C  C   . THR B  1 190 ? 46.367  17.592  28.000  1.00 28.64 ? 207  THR B C   1 
ATOM   5935  O  O   . THR B  1 190 ? 47.380  17.218  27.410  1.00 28.49 ? 207  THR B O   1 
ATOM   5936  C  CB  . THR B  1 190 ? 44.704  15.733  28.389  1.00 25.07 ? 207  THR B CB  1 
ATOM   5937  O  OG1 . THR B  1 190 ? 44.712  16.072  29.778  1.00 25.45 ? 207  THR B OG1 1 
ATOM   5938  C  CG2 . THR B  1 190 ? 45.729  14.640  28.133  1.00 25.16 ? 207  THR B CG2 1 
ATOM   5939  N  N   . ASP B  1 191 ? 46.371  18.492  28.991  1.00 30.15 ? 208  ASP B N   1 
ATOM   5940  C  CA  . ASP B  1 191 ? 47.601  19.051  29.526  1.00 32.24 ? 208  ASP B CA  1 
ATOM   5941  C  C   . ASP B  1 191 ? 48.072  18.221  30.722  1.00 33.29 ? 208  ASP B C   1 
ATOM   5942  O  O   . ASP B  1 191 ? 49.133  18.498  31.277  1.00 35.05 ? 208  ASP B O   1 
ATOM   5943  C  CB  . ASP B  1 191 ? 47.434  20.530  29.842  1.00 32.79 ? 208  ASP B CB  1 
ATOM   5944  C  CG  . ASP B  1 191 ? 47.342  21.465  28.643  1.00 34.01 ? 208  ASP B CG  1 
ATOM   5945  O  OD1 . ASP B  1 191 ? 47.567  21.011  27.504  1.00 34.22 ? 208  ASP B OD1 1 
ATOM   5946  O  OD2 . ASP B  1 191 ? 47.043  22.653  28.855  1.00 38.05 ? 208  ASP B OD2 1 
ATOM   5947  N  N   . ASN B  1 192 ? 47.298  17.190  31.094  1.00 30.74 ? 209  ASN B N   1 
ATOM   5948  C  CA  . ASN B  1 192 ? 47.618  16.330  32.223  1.00 31.72 ? 209  ASN B CA  1 
ATOM   5949  C  C   . ASN B  1 192 ? 48.790  15.422  31.850  1.00 31.35 ? 209  ASN B C   1 
ATOM   5950  O  O   . ASN B  1 192 ? 48.627  14.474  31.091  1.00 30.13 ? 209  ASN B O   1 
ATOM   5951  C  CB  . ASN B  1 192 ? 46.398  15.523  32.660  1.00 30.63 ? 209  ASN B CB  1 
ATOM   5952  C  CG  . ASN B  1 192 ? 46.597  14.793  33.969  1.00 31.16 ? 209  ASN B CG  1 
ATOM   5953  O  OD1 . ASN B  1 192 ? 47.674  14.242  34.228  1.00 30.30 ? 209  ASN B OD1 1 
ATOM   5954  N  ND2 . ASN B  1 192 ? 45.561  14.746  34.794  1.00 29.99 ? 209  ASN B ND2 1 
ATOM   5955  N  N   . ILE B  1 193 ? 49.965  15.711  32.423  1.00 34.32 ? 210  ILE B N   1 
ATOM   5956  C  CA  . ILE B  1 193 ? 51.207  15.029  32.083  1.00 35.67 ? 210  ILE B CA  1 
ATOM   5957  C  C   . ILE B  1 193 ? 51.098  13.538  32.394  1.00 32.67 ? 210  ILE B C   1 
ATOM   5958  O  O   . ILE B  1 193 ? 51.616  12.718  31.640  1.00 33.12 ? 210  ILE B O   1 
ATOM   5959  C  CB  . ILE B  1 193 ? 52.395  15.684  32.818  1.00 40.10 ? 210  ILE B CB  1 
ATOM   5960  C  CG1 . ILE B  1 193 ? 52.638  17.120  32.335  1.00 41.56 ? 210  ILE B CG1 1 
ATOM   5961  C  CG2 . ILE B  1 193 ? 53.665  14.836  32.707  1.00 41.10 ? 210  ILE B CG2 1 
ATOM   5962  C  CD1 . ILE B  1 193 ? 53.033  17.237  30.872  1.00 42.72 ? 210  ILE B CD1 1 
ATOM   5963  N  N   . ALA B  1 194 ? 50.422  13.201  33.498  1.00 32.06 ? 211  ALA B N   1 
ATOM   5964  C  CA  . ALA B  1 194 ? 50.267  11.820  33.930  1.00 32.74 ? 211  ALA B CA  1 
ATOM   5965  C  C   . ALA B  1 194 ? 49.511  10.995  32.886  1.00 31.99 ? 211  ALA B C   1 
ATOM   5966  O  O   . ALA B  1 194 ? 49.838  9.831   32.674  1.00 33.08 ? 211  ALA B O   1 
ATOM   5967  C  CB  . ALA B  1 194 ? 49.572  11.770  35.275  1.00 32.66 ? 211  ALA B CB  1 
ATOM   5968  N  N   . LEU B  1 195 ? 48.506  11.594  32.236  1.00 30.39 ? 212  LEU B N   1 
ATOM   5969  C  CA  . LEU B  1 195 ? 47.713  10.883  31.244  1.00 29.88 ? 212  LEU B CA  1 
ATOM   5970  C  C   . LEU B  1 195 ? 48.516  10.698  29.958  1.00 28.38 ? 212  LEU B C   1 
ATOM   5971  O  O   . LEU B  1 195 ? 48.428  9.649   29.321  1.00 26.85 ? 212  LEU B O   1 
ATOM   5972  C  CB  . LEU B  1 195 ? 46.400  11.619  30.980  1.00 30.30 ? 212  LEU B CB  1 
ATOM   5973  C  CG  . LEU B  1 195 ? 45.482  11.788  32.193  1.00 30.89 ? 212  LEU B CG  1 
ATOM   5974  C  CD1 . LEU B  1 195 ? 44.197  12.500  31.801  1.00 31.95 ? 212  LEU B CD1 1 
ATOM   5975  C  CD2 . LEU B  1 195 ? 45.180  10.452  32.835  1.00 32.33 ? 212  LEU B CD2 1 
ATOM   5976  N  N   . LEU B  1 196 ? 49.300  11.714  29.586  1.00 28.24 ? 213  LEU B N   1 
ATOM   5977  C  CA  . LEU B  1 196 ? 50.113  11.654  28.383  1.00 30.33 ? 213  LEU B CA  1 
ATOM   5978  C  C   . LEU B  1 196 ? 51.175  10.556  28.485  1.00 30.92 ? 213  LEU B C   1 
ATOM   5979  O  O   . LEU B  1 196 ? 51.666  10.099  27.457  1.00 30.18 ? 213  LEU B O   1 
ATOM   5980  C  CB  . LEU B  1 196 ? 50.744  13.017  28.112  1.00 31.16 ? 213  LEU B CB  1 
ATOM   5981  C  CG  . LEU B  1 196 ? 49.772  14.136  27.726  1.00 32.61 ? 213  LEU B CG  1 
ATOM   5982  C  CD1 . LEU B  1 196 ? 50.535  15.437  27.586  1.00 33.29 ? 213  LEU B CD1 1 
ATOM   5983  C  CD2 . LEU B  1 196 ? 49.014  13.830  26.444  1.00 33.47 ? 213  LEU B CD2 1 
ATOM   5984  N  N   . LYS B  1 197 ? 51.514  10.134  29.711  1.00 33.50 ? 214  LYS B N   1 
ATOM   5985  C  CA  . LYS B  1 197 ? 52.473  9.058   29.924  1.00 37.21 ? 214  LYS B CA  1 
ATOM   5986  C  C   . LYS B  1 197 ? 51.778  7.754   30.326  1.00 35.72 ? 214  LYS B C   1 
ATOM   5987  O  O   . LYS B  1 197 ? 52.449  6.798   30.713  1.00 34.77 ? 214  LYS B O   1 
ATOM   5988  C  CB  . LYS B  1 197 ? 53.492  9.481   30.987  1.00 41.65 ? 214  LYS B CB  1 
ATOM   5989  C  CG  . LYS B  1 197 ? 54.321  10.697  30.587  1.00 46.53 ? 214  LYS B CG  1 
ATOM   5990  C  CD  . LYS B  1 197 ? 55.517  10.990  31.488  1.00 52.01 ? 214  LYS B CD  1 
ATOM   5991  C  CE  . LYS B  1 197 ? 55.140  11.333  32.897  1.00 54.09 ? 214  LYS B CE  1 
ATOM   5992  N  NZ  . LYS B  1 197 ? 56.271  11.911  33.629  1.00 54.44 ? 214  LYS B NZ  1 
ATOM   5993  N  N   . ASP B  1 198 ? 50.444  7.703   30.200  1.00 32.27 ? 215  ASP B N   1 
ATOM   5994  C  CA  . ASP B  1 198 ? 49.671  6.531   30.582  1.00 31.48 ? 215  ASP B CA  1 
ATOM   5995  C  C   . ASP B  1 198 ? 49.337  5.720   29.334  1.00 29.97 ? 215  ASP B C   1 
ATOM   5996  O  O   . ASP B  1 198 ? 48.589  6.194   28.480  1.00 28.38 ? 215  ASP B O   1 
ATOM   5997  C  CB  . ASP B  1 198 ? 48.404  6.931   31.324  1.00 31.97 ? 215  ASP B CB  1 
ATOM   5998  C  CG  . ASP B  1 198 ? 47.523  5.789   31.814  1.00 33.04 ? 215  ASP B CG  1 
ATOM   5999  O  OD1 . ASP B  1 198 ? 47.906  4.614   31.621  1.00 33.78 ? 215  ASP B OD1 1 
ATOM   6000  O  OD2 . ASP B  1 198 ? 46.455  6.086   32.385  1.00 36.21 ? 215  ASP B OD2 1 
ATOM   6001  N  N   . PRO B  1 199 ? 49.850  4.473   29.194  1.00 30.39 ? 216  PRO B N   1 
ATOM   6002  C  CA  . PRO B  1 199 ? 49.565  3.658   28.011  1.00 30.62 ? 216  PRO B CA  1 
ATOM   6003  C  C   . PRO B  1 199 ? 48.109  3.203   27.912  1.00 29.91 ? 216  PRO B C   1 
ATOM   6004  O  O   . PRO B  1 199 ? 47.704  2.698   26.865  1.00 29.15 ? 216  PRO B O   1 
ATOM   6005  C  CB  . PRO B  1 199 ? 50.540  2.476   28.147  1.00 31.19 ? 216  PRO B CB  1 
ATOM   6006  C  CG  . PRO B  1 199 ? 50.767  2.350   29.633  1.00 31.34 ? 216  PRO B CG  1 
ATOM   6007  C  CD  . PRO B  1 199 ? 50.725  3.778   30.156  1.00 31.11 ? 216  PRO B CD  1 
ATOM   6008  N  N   . PHE B  1 200 ? 47.331  3.407   28.989  1.00 28.16 ? 217  PHE B N   1 
ATOM   6009  C  CA  . PHE B  1 200 ? 45.928  3.018   29.014  1.00 28.60 ? 217  PHE B CA  1 
ATOM   6010  C  C   . PHE B  1 200 ? 45.009  4.228   28.849  1.00 27.68 ? 217  PHE B C   1 
ATOM   6011  O  O   . PHE B  1 200 ? 43.789  4.066   28.867  1.00 27.96 ? 217  PHE B O   1 
ATOM   6012  C  CB  . PHE B  1 200 ? 45.653  2.262   30.317  1.00 29.53 ? 217  PHE B CB  1 
ATOM   6013  C  CG  . PHE B  1 200 ? 46.463  0.980   30.451  1.00 31.41 ? 217  PHE B CG  1 
ATOM   6014  C  CD1 . PHE B  1 200 ? 46.420  0.001   29.465  1.00 32.51 ? 217  PHE B CD1 1 
ATOM   6015  C  CD2 . PHE B  1 200 ? 47.301  0.777   31.542  1.00 34.46 ? 217  PHE B CD2 1 
ATOM   6016  C  CE1 . PHE B  1 200 ? 47.177  -1.156  29.584  1.00 34.33 ? 217  PHE B CE1 1 
ATOM   6017  C  CE2 . PHE B  1 200 ? 48.059  -0.381  31.654  1.00 33.76 ? 217  PHE B CE2 1 
ATOM   6018  C  CZ  . PHE B  1 200 ? 47.993  -1.345  30.680  1.00 34.64 ? 217  PHE B CZ  1 
ATOM   6019  N  N   . TYR B  1 201 ? 45.577  5.428   28.660  1.00 25.76 ? 218  TYR B N   1 
ATOM   6020  C  CA  . TYR B  1 201 ? 44.774  6.614   28.395  1.00 25.86 ? 218  TYR B CA  1 
ATOM   6021  C  C   . TYR B  1 201 ? 44.005  6.411   27.088  1.00 26.93 ? 218  TYR B C   1 
ATOM   6022  O  O   . TYR B  1 201 ? 44.550  5.863   26.136  1.00 27.89 ? 218  TYR B O   1 
ATOM   6023  C  CB  . TYR B  1 201 ? 45.644  7.877   28.357  1.00 24.28 ? 218  TYR B CB  1 
ATOM   6024  C  CG  . TYR B  1 201 ? 44.848  9.142   28.071  1.00 22.63 ? 218  TYR B CG  1 
ATOM   6025  C  CD1 . TYR B  1 201 ? 43.768  9.506   28.869  1.00 22.95 ? 218  TYR B CD1 1 
ATOM   6026  C  CD2 . TYR B  1 201 ? 45.118  9.927   26.959  1.00 21.72 ? 218  TYR B CD2 1 
ATOM   6027  C  CE1 . TYR B  1 201 ? 43.017  10.638  28.596  1.00 21.92 ? 218  TYR B CE1 1 
ATOM   6028  C  CE2 . TYR B  1 201 ? 44.377  11.062  26.678  1.00 21.86 ? 218  TYR B CE2 1 
ATOM   6029  C  CZ  . TYR B  1 201 ? 43.318  11.417  27.496  1.00 21.51 ? 218  TYR B CZ  1 
ATOM   6030  O  OH  . TYR B  1 201 ? 42.579  12.532  27.209  1.00 21.87 ? 218  TYR B OH  1 
ATOM   6031  N  N   . MET B  1 202 ? 42.743  6.871   27.046  1.00 26.97 ? 219  MET B N   1 
ATOM   6032  C  CA  . MET B  1 202 ? 41.821  6.529   25.970  1.00 27.62 ? 219  MET B CA  1 
ATOM   6033  C  C   . MET B  1 202 ? 41.577  7.712   25.027  1.00 27.01 ? 219  MET B C   1 
ATOM   6034  O  O   . MET B  1 202 ? 40.700  7.644   24.163  1.00 26.28 ? 219  MET B O   1 
ATOM   6035  C  CB  . MET B  1 202 ? 40.493  6.037   26.562  1.00 29.60 ? 219  MET B CB  1 
ATOM   6036  C  CG  . MET B  1 202 ? 40.609  4.698   27.272  1.00 31.51 ? 219  MET B CG  1 
ATOM   6037  S  SD  . MET B  1 202 ? 39.039  4.060   27.895  1.00 36.17 ? 219  MET B SD  1 
ATOM   6038  C  CE  . MET B  1 202 ? 38.776  5.135   29.312  1.00 36.27 ? 219  MET B CE  1 
ATOM   6039  N  N   . GLY B  1 203 ? 42.371  8.783   25.167  1.00 25.02 ? 220  GLY B N   1 
ATOM   6040  C  CA  . GLY B  1 203 ? 42.235  9.965   24.333  1.00 24.77 ? 220  GLY B CA  1 
ATOM   6041  C  C   . GLY B  1 203 ? 43.452  10.173  23.438  1.00 25.75 ? 220  GLY B C   1 
ATOM   6042  O  O   . GLY B  1 203 ? 44.329  9.312   23.374  1.00 25.60 ? 220  GLY B O   1 
ATOM   6043  N  N   . LEU B  1 204 ? 43.463  11.320  22.744  1.00 27.13 ? 221  LEU B N   1 
ATOM   6044  C  CA  . LEU B  1 204 ? 44.581  11.777  21.932  1.00 28.65 ? 221  LEU B CA  1 
ATOM   6045  C  C   . LEU B  1 204 ? 45.769  12.101  22.833  1.00 28.13 ? 221  LEU B C   1 
ATOM   6046  O  O   . LEU B  1 204 ? 45.613  12.774  23.852  1.00 26.24 ? 221  LEU B O   1 
ATOM   6047  C  CB  . LEU B  1 204 ? 44.186  13.018  21.126  1.00 31.22 ? 221  LEU B CB  1 
ATOM   6048  C  CG  . LEU B  1 204 ? 43.683  12.804  19.695  1.00 33.92 ? 221  LEU B CG  1 
ATOM   6049  C  CD1 . LEU B  1 204 ? 42.749  11.618  19.540  1.00 35.66 ? 221  LEU B CD1 1 
ATOM   6050  C  CD2 . LEU B  1 204 ? 42.994  14.080  19.223  1.00 34.64 ? 221  LEU B CD2 1 
ATOM   6051  N  N   . TYR B  1 205 ? 46.959  11.653  22.420  1.00 28.05 ? 222  TYR B N   1 
ATOM   6052  C  CA  . TYR B  1 205 ? 48.181  11.945  23.150  1.00 28.97 ? 222  TYR B CA  1 
ATOM   6053  C  C   . TYR B  1 205 ? 48.794  13.233  22.610  1.00 30.78 ? 222  TYR B C   1 
ATOM   6054  O  O   . TYR B  1 205 ? 49.793  13.200  21.892  1.00 31.63 ? 222  TYR B O   1 
ATOM   6055  C  CB  . TYR B  1 205 ? 49.169  10.780  23.040  1.00 29.33 ? 222  TYR B CB  1 
ATOM   6056  C  CG  . TYR B  1 205 ? 48.801  9.537   23.833  1.00 28.28 ? 222  TYR B CG  1 
ATOM   6057  C  CD1 . TYR B  1 205 ? 49.081  9.437   25.191  1.00 27.77 ? 222  TYR B CD1 1 
ATOM   6058  C  CD2 . TYR B  1 205 ? 48.200  8.449   23.213  1.00 29.57 ? 222  TYR B CD2 1 
ATOM   6059  C  CE1 . TYR B  1 205 ? 48.761  8.297   25.912  1.00 27.60 ? 222  TYR B CE1 1 
ATOM   6060  C  CE2 . TYR B  1 205 ? 47.874  7.305   23.925  1.00 30.70 ? 222  TYR B CE2 1 
ATOM   6061  C  CZ  . TYR B  1 205 ? 48.154  7.227   25.277  1.00 29.56 ? 222  TYR B CZ  1 
ATOM   6062  O  OH  . TYR B  1 205 ? 47.833  6.083   25.954  1.00 31.69 ? 222  TYR B OH  1 
ATOM   6063  N  N   . GLN B  1 206 ? 48.173  14.365  22.956  1.00 29.63 ? 223  GLN B N   1 
ATOM   6064  C  CA  . GLN B  1 206 ? 48.713  15.675  22.642  1.00 29.40 ? 223  GLN B CA  1 
ATOM   6065  C  C   . GLN B  1 206 ? 48.227  16.669  23.691  1.00 29.69 ? 223  GLN B C   1 
ATOM   6066  O  O   . GLN B  1 206 ? 47.202  16.441  24.342  1.00 28.14 ? 223  GLN B O   1 
ATOM   6067  C  CB  . GLN B  1 206 ? 48.299  16.140  21.244  1.00 30.18 ? 223  GLN B CB  1 
ATOM   6068  C  CG  . GLN B  1 206 ? 46.797  16.332  21.059  1.00 30.65 ? 223  GLN B CG  1 
ATOM   6069  C  CD  . GLN B  1 206 ? 46.434  17.009  19.754  1.00 31.78 ? 223  GLN B CD  1 
ATOM   6070  O  OE1 . GLN B  1 206 ? 46.817  16.560  18.668  1.00 34.64 ? 223  GLN B OE1 1 
ATOM   6071  N  NE2 . GLN B  1 206 ? 45.692  18.103  19.837  1.00 32.01 ? 223  GLN B NE2 1 
ATOM   6072  N  N   . LYS B  1 207 ? 48.971  17.772  23.834  1.00 28.77 ? 224  LYS B N   1 
ATOM   6073  C  CA  A LYS B  1 207 ? 48.534  18.884  24.660  0.58 29.41 ? 224  LYS B CA  1 
ATOM   6074  C  CA  B LYS B  1 207 ? 48.541  18.891  24.654  0.42 29.06 ? 224  LYS B CA  1 
ATOM   6075  C  C   . LYS B  1 207 ? 47.262  19.459  24.042  1.00 27.69 ? 224  LYS B C   1 
ATOM   6076  O  O   . LYS B  1 207 ? 47.005  19.264  22.860  1.00 26.92 ? 224  LYS B O   1 
ATOM   6077  C  CB  A LYS B  1 207 ? 49.622  19.957  24.797  0.58 30.53 ? 224  LYS B CB  1 
ATOM   6078  C  CB  B LYS B  1 207 ? 49.620  19.980  24.744  0.42 29.79 ? 224  LYS B CB  1 
ATOM   6079  C  CG  A LYS B  1 207 ? 50.820  19.563  25.657  0.58 31.84 ? 224  LYS B CG  1 
ATOM   6080  C  CG  B LYS B  1 207 ? 51.042  19.501  25.034  0.42 30.79 ? 224  LYS B CG  1 
ATOM   6081  C  CD  A LYS B  1 207 ? 51.751  20.718  26.018  0.58 32.71 ? 224  LYS B CD  1 
ATOM   6082  C  CD  B LYS B  1 207 ? 51.161  18.474  26.153  0.42 31.02 ? 224  LYS B CD  1 
ATOM   6083  C  CE  A LYS B  1 207 ? 51.162  21.646  27.041  0.58 33.63 ? 224  LYS B CE  1 
ATOM   6084  C  CE  B LYS B  1 207 ? 51.156  19.071  27.522  0.42 31.19 ? 224  LYS B CE  1 
ATOM   6085  N  NZ  A LYS B  1 207 ? 52.100  22.689  27.462  0.58 33.96 ? 224  LYS B NZ  1 
ATOM   6086  N  NZ  B LYS B  1 207 ? 52.404  19.785  27.804  0.42 31.44 ? 224  LYS B NZ  1 
ATOM   6087  N  N   . ARG B  1 208 ? 46.467  20.161  24.853  1.00 27.29 ? 225  ARG B N   1 
ATOM   6088  C  CA  . ARG B  1 208 ? 45.220  20.734  24.369  1.00 27.32 ? 225  ARG B CA  1 
ATOM   6089  C  C   . ARG B  1 208 ? 45.497  21.726  23.242  1.00 27.93 ? 225  ARG B C   1 
ATOM   6090  O  O   . ARG B  1 208 ? 46.364  22.592  23.361  1.00 28.35 ? 225  ARG B O   1 
ATOM   6091  C  CB  . ARG B  1 208 ? 44.421  21.424  25.475  1.00 27.63 ? 225  ARG B CB  1 
ATOM   6092  C  CG  . ARG B  1 208 ? 43.750  20.436  26.417  1.00 27.25 ? 225  ARG B CG  1 
ATOM   6093  C  CD  . ARG B  1 208 ? 42.998  21.129  27.540  1.00 26.75 ? 225  ARG B CD  1 
ATOM   6094  N  NE  . ARG B  1 208 ? 42.302  20.119  28.345  1.00 26.14 ? 225  ARG B NE  1 
ATOM   6095  C  CZ  . ARG B  1 208 ? 41.237  19.414  27.967  1.00 24.22 ? 225  ARG B CZ  1 
ATOM   6096  N  NH1 . ARG B  1 208 ? 40.559  19.754  26.889  1.00 24.05 ? 225  ARG B NH1 1 
ATOM   6097  N  NH2 . ARG B  1 208 ? 40.840  18.382  28.689  1.00 23.14 ? 225  ARG B NH2 1 
ATOM   6098  N  N   . ASP B  1 209 ? 44.745  21.575  22.149  1.00 28.01 ? 226  ASP B N   1 
ATOM   6099  C  CA  . ASP B  1 209 ? 44.769  22.516  21.044  1.00 29.60 ? 226  ASP B CA  1 
ATOM   6100  C  C   . ASP B  1 209 ? 44.082  23.800  21.503  1.00 31.28 ? 226  ASP B C   1 
ATOM   6101  O  O   . ASP B  1 209 ? 42.917  23.770  21.898  1.00 29.85 ? 226  ASP B O   1 
ATOM   6102  C  CB  . ASP B  1 209 ? 44.114  21.912  19.813  1.00 29.39 ? 226  ASP B CB  1 
ATOM   6103  C  CG  . ASP B  1 209 ? 44.261  22.703  18.522  1.00 31.11 ? 226  ASP B CG  1 
ATOM   6104  O  OD1 . ASP B  1 209 ? 44.131  23.946  18.572  1.00 32.57 ? 226  ASP B OD1 1 
ATOM   6105  O  OD2 . ASP B  1 209 ? 44.456  22.063  17.469  1.00 31.84 ? 226  ASP B OD2 1 
ATOM   6106  N  N   . ARG B  1 210 ? 44.818  24.918  21.456  1.00 33.06 ? 227  ARG B N   1 
ATOM   6107  C  CA  . ARG B  1 210 ? 44.305  26.199  21.914  1.00 35.29 ? 227  ARG B CA  1 
ATOM   6108  C  C   . ARG B  1 210 ? 44.275  27.199  20.760  1.00 34.64 ? 227  ARG B C   1 
ATOM   6109  O  O   . ARG B  1 210 ? 44.084  28.392  20.984  1.00 37.46 ? 227  ARG B O   1 
ATOM   6110  C  CB  . ARG B  1 210 ? 45.128  26.663  23.123  1.00 37.05 ? 227  ARG B CB  1 
ATOM   6111  C  CG  . ARG B  1 210 ? 44.946  25.744  24.325  1.00 38.07 ? 227  ARG B CG  1 
ATOM   6112  C  CD  . ARG B  1 210 ? 45.677  26.249  25.555  1.00 39.93 ? 227  ARG B CD  1 
ATOM   6113  N  NE  . ARG B  1 210 ? 45.696  25.309  26.683  1.00 39.68 ? 227  ARG B NE  1 
ATOM   6114  C  CZ  . ARG B  1 210 ? 44.676  24.990  27.475  1.00 40.02 ? 227  ARG B CZ  1 
ATOM   6115  N  NH1 . ARG B  1 210 ? 43.463  25.460  27.243  1.00 43.42 ? 227  ARG B NH1 1 
ATOM   6116  N  NH2 . ARG B  1 210 ? 44.871  24.175  28.496  1.00 39.62 ? 227  ARG B NH2 1 
ATOM   6117  N  N   . THR B  1 211 ? 44.404  26.703  19.525  1.00 33.36 ? 228  THR B N   1 
ATOM   6118  C  CA  . THR B  1 211 ? 44.378  27.551  18.343  1.00 32.35 ? 228  THR B CA  1 
ATOM   6119  C  C   . THR B  1 211 ? 42.926  27.789  17.935  1.00 31.03 ? 228  THR B C   1 
ATOM   6120  O  O   . THR B  1 211 ? 41.994  27.309  18.585  1.00 28.71 ? 228  THR B O   1 
ATOM   6121  C  CB  . THR B  1 211 ? 45.173  26.913  17.200  1.00 33.46 ? 228  THR B CB  1 
ATOM   6122  O  OG1 . THR B  1 211 ? 44.432  25.777  16.766  1.00 34.75 ? 228  THR B OG1 1 
ATOM   6123  C  CG2 . THR B  1 211 ? 46.573  26.483  17.601  1.00 33.46 ? 228  THR B CG2 1 
ATOM   6124  N  N   . GLN B  1 212 ? 42.760  28.524  16.831  1.00 30.42 ? 229  GLN B N   1 
ATOM   6125  C  CA  . GLN B  1 212 ? 41.465  28.754  16.212  1.00 30.37 ? 229  GLN B CA  1 
ATOM   6126  C  C   . GLN B  1 212 ? 40.752  27.435  15.894  1.00 29.22 ? 229  GLN B C   1 
ATOM   6127  O  O   . GLN B  1 212 ? 39.526  27.404  15.822  1.00 28.11 ? 229  GLN B O   1 
ATOM   6128  C  CB  . GLN B  1 212 ? 41.685  29.578  14.942  1.00 32.09 ? 229  GLN B CB  1 
ATOM   6129  C  CG  . GLN B  1 212 ? 40.408  30.012  14.235  1.00 33.60 ? 229  GLN B CG  1 
ATOM   6130  C  CD  . GLN B  1 212 ? 39.469  30.797  15.124  1.00 36.60 ? 229  GLN B CD  1 
ATOM   6131  O  OE1 . GLN B  1 212 ? 39.894  31.638  15.924  1.00 38.48 ? 229  GLN B OE1 1 
ATOM   6132  N  NE2 . GLN B  1 212 ? 38.178  30.516  15.006  1.00 37.52 ? 229  GLN B NE2 1 
ATOM   6133  N  N   . GLN B  1 213 ? 41.510  26.351  15.691  1.00 28.41 ? 230  GLN B N   1 
ATOM   6134  C  CA  . GLN B  1 213 ? 40.919  25.057  15.373  1.00 30.04 ? 230  GLN B CA  1 
ATOM   6135  C  C   . GLN B  1 213 ? 40.000  24.573  16.498  1.00 27.36 ? 230  GLN B C   1 
ATOM   6136  O  O   . GLN B  1 213 ? 39.016  23.885  16.227  1.00 25.93 ? 230  GLN B O   1 
ATOM   6137  C  CB  . GLN B  1 213 ? 41.992  24.005  15.090  1.00 32.71 ? 230  GLN B CB  1 
ATOM   6138  C  CG  . GLN B  1 213 ? 42.861  24.328  13.880  1.00 35.51 ? 230  GLN B CG  1 
ATOM   6139  C  CD  . GLN B  1 213 ? 43.749  23.178  13.459  1.00 38.28 ? 230  GLN B CD  1 
ATOM   6140  O  OE1 . GLN B  1 213 ? 43.829  22.827  12.277  1.00 41.67 ? 230  GLN B OE1 1 
ATOM   6141  N  NE2 . GLN B  1 213 ? 44.433  22.580  14.424  1.00 40.95 ? 230  GLN B NE2 1 
ATOM   6142  N  N   . TYR B  1 214 ? 40.325  24.927  17.750  1.00 24.79 ? 231  TYR B N   1 
ATOM   6143  C  CA  . TYR B  1 214 ? 39.486  24.588  18.892  1.00 25.21 ? 231  TYR B CA  1 
ATOM   6144  C  C   . TYR B  1 214 ? 38.113  25.245  18.737  1.00 25.47 ? 231  TYR B C   1 
ATOM   6145  O  O   . TYR B  1 214 ? 37.093  24.560  18.748  1.00 24.71 ? 231  TYR B O   1 
ATOM   6146  C  CB  . TYR B  1 214 ? 40.172  24.983  20.204  1.00 25.55 ? 231  TYR B CB  1 
ATOM   6147  C  CG  . TYR B  1 214 ? 39.325  24.756  21.445  1.00 25.92 ? 231  TYR B CG  1 
ATOM   6148  C  CD1 . TYR B  1 214 ? 39.210  23.494  22.015  1.00 27.27 ? 231  TYR B CD1 1 
ATOM   6149  C  CD2 . TYR B  1 214 ? 38.632  25.802  22.042  1.00 26.93 ? 231  TYR B CD2 1 
ATOM   6150  C  CE1 . TYR B  1 214 ? 38.421  23.272  23.132  1.00 26.20 ? 231  TYR B CE1 1 
ATOM   6151  C  CE2 . TYR B  1 214 ? 37.849  25.596  23.166  1.00 27.04 ? 231  TYR B CE2 1 
ATOM   6152  C  CZ  . TYR B  1 214 ? 37.742  24.329  23.713  1.00 26.79 ? 231  TYR B CZ  1 
ATOM   6153  O  OH  . TYR B  1 214 ? 36.971  24.140  24.828  1.00 26.25 ? 231  TYR B OH  1 
ATOM   6154  N  N   . ASP B  1 215 ? 38.098  26.573  18.575  1.00 25.36 ? 232  ASP B N   1 
ATOM   6155  C  CA  . ASP B  1 215 ? 36.865  27.331  18.407  1.00 27.28 ? 232  ASP B CA  1 
ATOM   6156  C  C   . ASP B  1 215 ? 36.073  26.847  17.193  1.00 25.84 ? 232  ASP B C   1 
ATOM   6157  O  O   . ASP B  1 215 ? 34.846  26.789  17.238  1.00 24.82 ? 232  ASP B O   1 
ATOM   6158  C  CB  . ASP B  1 215 ? 37.150  28.820  18.296  1.00 29.83 ? 232  ASP B CB  1 
ATOM   6159  C  CG  . ASP B  1 215 ? 37.463  29.528  19.607  1.00 33.24 ? 232  ASP B CG  1 
ATOM   6160  O  OD1 . ASP B  1 215 ? 38.141  28.919  20.464  1.00 36.26 ? 232  ASP B OD1 1 
ATOM   6161  O  OD2 . ASP B  1 215 ? 37.050  30.697  19.747  1.00 35.40 ? 232  ASP B OD2 1 
ATOM   6162  N  N   . ASP B  1 216 ? 36.775  26.534  16.098  1.00 24.53 ? 233  ASP B N   1 
ATOM   6163  C  CA  . ASP B  1 216 ? 36.128  26.051  14.889  1.00 25.37 ? 233  ASP B CA  1 
ATOM   6164  C  C   . ASP B  1 216 ? 35.450  24.706  15.152  1.00 24.02 ? 233  ASP B C   1 
ATOM   6165  O  O   . ASP B  1 216 ? 34.382  24.438  14.600  1.00 24.00 ? 233  ASP B O   1 
ATOM   6166  C  CB  . ASP B  1 216 ? 37.107  25.944  13.729  1.00 27.15 ? 233  ASP B CB  1 
ATOM   6167  C  CG  . ASP B  1 216 ? 37.606  27.263  13.157  1.00 30.26 ? 233  ASP B CG  1 
ATOM   6168  O  OD1 . ASP B  1 216 ? 37.055  28.315  13.534  1.00 31.48 ? 233  ASP B OD1 1 
ATOM   6169  O  OD2 . ASP B  1 216 ? 38.558  27.226  12.349  1.00 35.16 ? 233  ASP B OD2 1 
ATOM   6170  N  N   . LEU B  1 217 ? 36.082  23.864  15.978  1.00 22.82 ? 234  LEU B N   1 
ATOM   6171  C  CA  . LEU B  1 217 ? 35.539  22.550  16.285  1.00 23.00 ? 234  LEU B CA  1 
ATOM   6172  C  C   . LEU B  1 217 ? 34.262  22.689  17.111  1.00 23.58 ? 234  LEU B C   1 
ATOM   6173  O  O   . LEU B  1 217 ? 33.299  21.968  16.868  1.00 22.74 ? 234  LEU B O   1 
ATOM   6174  C  CB  . LEU B  1 217 ? 36.554  21.675  17.013  1.00 21.91 ? 234  LEU B CB  1 
ATOM   6175  C  CG  . LEU B  1 217 ? 36.117  20.223  17.227  1.00 22.05 ? 234  LEU B CG  1 
ATOM   6176  C  CD1 . LEU B  1 217 ? 36.090  19.453  15.907  1.00 22.17 ? 234  LEU B CD1 1 
ATOM   6177  C  CD2 . LEU B  1 217 ? 36.993  19.540  18.253  1.00 22.73 ? 234  LEU B CD2 1 
ATOM   6178  N  N   . ILE B  1 218 ? 34.268  23.589  18.103  1.00 23.33 ? 235  ILE B N   1 
ATOM   6179  C  CA  . ILE B  1 218 ? 33.099  23.775  18.949  1.00 23.61 ? 235  ILE B CA  1 
ATOM   6180  C  C   . ILE B  1 218 ? 31.950  24.302  18.092  1.00 23.64 ? 235  ILE B C   1 
ATOM   6181  O  O   . ILE B  1 218 ? 30.828  23.825  18.232  1.00 23.40 ? 235  ILE B O   1 
ATOM   6182  C  CB  . ILE B  1 218 ? 33.394  24.675  20.166  1.00 24.00 ? 235  ILE B CB  1 
ATOM   6183  C  CG1 . ILE B  1 218 ? 34.535  24.129  21.028  1.00 24.39 ? 235  ILE B CG1 1 
ATOM   6184  C  CG2 . ILE B  1 218 ? 32.134  24.904  21.006  1.00 24.68 ? 235  ILE B CG2 1 
ATOM   6185  C  CD1 . ILE B  1 218 ? 34.305  22.734  21.580  1.00 25.54 ? 235  ILE B CD1 1 
ATOM   6186  N  N   . ASP B  1 219 ? 32.237  25.266  17.205  1.00 23.08 ? 236  ASP B N   1 
ATOM   6187  C  CA  . ASP B  1 219 ? 31.242  25.809  16.289  1.00 23.86 ? 236  ASP B CA  1 
ATOM   6188  C  C   . ASP B  1 219 ? 30.639  24.714  15.407  1.00 23.69 ? 236  ASP B C   1 
ATOM   6189  O  O   . ASP B  1 219 ? 29.436  24.716  15.162  1.00 21.71 ? 236  ASP B O   1 
ATOM   6190  C  CB  . ASP B  1 219 ? 31.822  26.866  15.362  1.00 26.29 ? 236  ASP B CB  1 
ATOM   6191  C  CG  . ASP B  1 219 ? 32.025  28.257  15.948  1.00 29.82 ? 236  ASP B CG  1 
ATOM   6192  O  OD1 . ASP B  1 219 ? 31.489  28.522  17.053  1.00 31.69 ? 236  ASP B OD1 1 
ATOM   6193  O  OD2 . ASP B  1 219 ? 32.715  29.067  15.283  1.00 31.93 ? 236  ASP B OD2 1 
ATOM   6194  N  N   . GLU B  1 220 ? 31.494  23.824  14.890  1.00 23.07 ? 237  GLU B N   1 
ATOM   6195  C  CA  . GLU B  1 220 ? 31.066  22.754  14.001  1.00 23.51 ? 237  GLU B CA  1 
ATOM   6196  C  C   . GLU B  1 220 ? 30.149  21.786  14.755  1.00 22.54 ? 237  GLU B C   1 
ATOM   6197  O  O   . GLU B  1 220 ? 29.186  21.273  14.191  1.00 21.10 ? 237  GLU B O   1 
ATOM   6198  C  CB  . GLU B  1 220 ? 32.309  22.066  13.433  1.00 24.22 ? 237  GLU B CB  1 
ATOM   6199  C  CG  . GLU B  1 220 ? 32.002  21.078  12.311  1.00 25.33 ? 237  GLU B CG  1 
ATOM   6200  C  CD  . GLU B  1 220 ? 33.177  20.244  11.818  1.00 25.14 ? 237  GLU B CD  1 
ATOM   6201  O  OE1 . GLU B  1 220 ? 34.336  20.455  12.249  1.00 24.42 ? 237  GLU B OE1 1 
ATOM   6202  O  OE2 . GLU B  1 220 ? 32.905  19.350  10.988  1.00 26.01 ? 237  GLU B OE2 1 
ATOM   6203  N  N   . PHE B  1 221 ? 30.457  21.556  16.038  1.00 22.48 ? 238  PHE B N   1 
ATOM   6204  C  CA  . PHE B  1 221 ? 29.657  20.704  16.906  1.00 22.66 ? 238  PHE B CA  1 
ATOM   6205  C  C   . PHE B  1 221 ? 28.260  21.298  17.111  1.00 22.65 ? 238  PHE B C   1 
ATOM   6206  O  O   . PHE B  1 221 ? 27.264  20.602  16.937  1.00 23.08 ? 238  PHE B O   1 
ATOM   6207  C  CB  . PHE B  1 221 ? 30.412  20.472  18.220  1.00 22.65 ? 238  PHE B CB  1 
ATOM   6208  C  CG  . PHE B  1 221 ? 29.526  20.028  19.373  1.00 22.89 ? 238  PHE B CG  1 
ATOM   6209  C  CD1 . PHE B  1 221 ? 29.022  18.733  19.424  1.00 24.00 ? 238  PHE B CD1 1 
ATOM   6210  C  CD2 . PHE B  1 221 ? 29.188  20.912  20.393  1.00 24.12 ? 238  PHE B CD2 1 
ATOM   6211  C  CE1 . PHE B  1 221 ? 28.205  18.335  20.469  1.00 23.82 ? 238  PHE B CE1 1 
ATOM   6212  C  CE2 . PHE B  1 221 ? 28.364  20.510  21.433  1.00 24.52 ? 238  PHE B CE2 1 
ATOM   6213  C  CZ  . PHE B  1 221 ? 27.880  19.221  21.470  1.00 23.97 ? 238  PHE B CZ  1 
ATOM   6214  N  N   . MET B  1 222 ? 28.176  22.581  17.475  1.00 22.17 ? 239  MET B N   1 
ATOM   6215  C  CA  . MET B  1 222 ? 26.882  23.206  17.726  1.00 21.65 ? 239  MET B CA  1 
ATOM   6216  C  C   . MET B  1 222 ? 26.018  23.143  16.468  1.00 21.74 ? 239  MET B C   1 
ATOM   6217  O  O   . MET B  1 222 ? 24.825  22.859  16.544  1.00 21.39 ? 239  MET B O   1 
ATOM   6218  C  CB  . MET B  1 222 ? 27.030  24.666  18.175  1.00 20.84 ? 239  MET B CB  1 
ATOM   6219  C  CG  . MET B  1 222 ? 27.841  24.859  19.457  1.00 21.69 ? 239  MET B CG  1 
ATOM   6220  S  SD  . MET B  1 222 ? 27.096  24.167  20.949  1.00 21.91 ? 239  MET B SD  1 
ATOM   6221  C  CE  . MET B  1 222 ? 25.759  25.324  21.270  1.00 22.19 ? 239  MET B CE  1 
ATOM   6222  N  N   . LYS B  1 223 ? 26.632  23.412  15.308  1.00 22.19 ? 240  LYS B N   1 
ATOM   6223  C  CA  . LYS B  1 223 ? 25.930  23.370  14.037  1.00 22.86 ? 240  LYS B CA  1 
ATOM   6224  C  C   . LYS B  1 223 ? 25.471  21.947  13.712  1.00 21.44 ? 240  LYS B C   1 
ATOM   6225  O  O   . LYS B  1 223 ? 24.336  21.751  13.281  1.00 21.34 ? 240  LYS B O   1 
ATOM   6226  C  CB  . LYS B  1 223 ? 26.818  23.950  12.931  1.00 24.65 ? 240  LYS B CB  1 
ATOM   6227  C  CG  . LYS B  1 223 ? 26.194  23.927  11.541  1.00 26.77 ? 240  LYS B CG  1 
ATOM   6228  C  CD  . LYS B  1 223 ? 27.061  24.576  10.467  1.00 30.08 ? 240  LYS B CD  1 
ATOM   6229  C  CE  . LYS B  1 223 ? 26.821  24.009  9.100   1.00 32.29 ? 240  LYS B CE  1 
ATOM   6230  N  NZ  . LYS B  1 223 ? 25.414  24.067  8.706   1.00 33.15 ? 240  LYS B NZ  1 
ATOM   6231  N  N   . ALA B  1 224 ? 26.342  20.954  13.917  1.00 21.23 ? 241  ALA B N   1 
ATOM   6232  C  CA  . ALA B  1 224 ? 26.018  19.573  13.577  1.00 20.76 ? 241  ALA B CA  1 
ATOM   6233  C  C   . ALA B  1 224 ? 24.844  19.060  14.417  1.00 20.86 ? 241  ALA B C   1 
ATOM   6234  O  O   . ALA B  1 224 ? 23.942  18.404  13.891  1.00 19.21 ? 241  ALA B O   1 
ATOM   6235  C  CB  . ALA B  1 224 ? 27.237  18.698  13.756  1.00 21.77 ? 241  ALA B CB  1 
ATOM   6236  N  N   . ILE B  1 225 ? 24.871  19.340  15.726  1.00 20.35 ? 242  ILE B N   1 
ATOM   6237  C  CA  . ILE B  1 225 ? 23.838  18.862  16.628  1.00 21.53 ? 242  ILE B CA  1 
ATOM   6238  C  C   . ILE B  1 225 ? 22.493  19.459  16.223  1.00 21.84 ? 242  ILE B C   1 
ATOM   6239  O  O   . ILE B  1 225 ? 21.492  18.743  16.178  1.00 21.27 ? 242  ILE B O   1 
ATOM   6240  C  CB  . ILE B  1 225 ? 24.180  19.187  18.096  1.00 23.10 ? 242  ILE B CB  1 
ATOM   6241  C  CG1 . ILE B  1 225 ? 25.318  18.312  18.623  1.00 24.24 ? 242  ILE B CG1 1 
ATOM   6242  C  CG2 . ILE B  1 225 ? 22.939  19.079  18.988  1.00 23.56 ? 242  ILE B CG2 1 
ATOM   6243  C  CD1 . ILE B  1 225 ? 24.943  16.856  18.847  1.00 24.51 ? 242  ILE B CD1 1 
ATOM   6244  N  N   . THR B  1 226 ? 22.465  20.771  15.957  1.00 21.16 ? 243  THR B N   1 
ATOM   6245  C  CA  . THR B  1 226 ? 21.203  21.443  15.688  1.00 22.43 ? 243  THR B CA  1 
ATOM   6246  C  C   . THR B  1 226 ? 20.740  21.170  14.255  1.00 22.35 ? 243  THR B C   1 
ATOM   6247  O  O   . THR B  1 226 ? 19.538  21.173  13.998  1.00 21.75 ? 243  THR B O   1 
ATOM   6248  C  CB  . THR B  1 226 ? 21.297  22.934  16.023  1.00 23.39 ? 243  THR B CB  1 
ATOM   6249  O  OG1 . THR B  1 226 ? 22.390  23.536  15.334  1.00 23.04 ? 243  THR B OG1 1 
ATOM   6250  C  CG2 . THR B  1 226 ? 21.487  23.146  17.514  1.00 23.78 ? 243  THR B CG2 1 
ATOM   6251  N  N   . ASP B  1 227 ? 21.672  20.898  13.333  1.00 22.34 ? 244  ASP B N   1 
ATOM   6252  C  CA  . ASP B  1 227 ? 21.303  20.500  11.979  1.00 23.37 ? 244  ASP B CA  1 
ATOM   6253  C  C   . ASP B  1 227 ? 20.530  19.185  12.011  1.00 22.63 ? 244  ASP B C   1 
ATOM   6254  O  O   . ASP B  1 227 ? 19.519  19.044  11.325  1.00 22.58 ? 244  ASP B O   1 
ATOM   6255  C  CB  . ASP B  1 227 ? 22.502  20.380  11.048  1.00 23.46 ? 244  ASP B CB  1 
ATOM   6256  C  CG  . ASP B  1 227 ? 23.041  21.679  10.466  1.00 24.89 ? 244  ASP B CG  1 
ATOM   6257  O  OD1 . ASP B  1 227 ? 22.366  22.724  10.602  1.00 25.26 ? 244  ASP B OD1 1 
ATOM   6258  O  OD2 . ASP B  1 227 ? 24.146  21.637  9.884   1.00 25.97 ? 244  ASP B OD2 1 
ATOM   6259  N  N   . ARG B  1 228 ? 21.002  18.227  12.815  1.00 21.21 ? 245  ARG B N   1 
ATOM   6260  C  CA  . ARG B  1 228 ? 20.350  16.931  12.886  1.00 21.12 ? 245  ARG B CA  1 
ATOM   6261  C  C   . ARG B  1 228 ? 19.065  17.007  13.715  1.00 20.19 ? 245  ARG B C   1 
ATOM   6262  O  O   . ARG B  1 228 ? 18.040  16.487  13.287  1.00 20.07 ? 245  ARG B O   1 
ATOM   6263  C  CB  . ARG B  1 228 ? 21.268  15.836  13.440  1.00 21.04 ? 245  ARG B CB  1 
ATOM   6264  C  CG  . ARG B  1 228 ? 20.539  14.500  13.429  1.00 21.60 ? 245  ARG B CG  1 
ATOM   6265  C  CD  . ARG B  1 228 ? 21.367  13.275  13.758  1.00 22.05 ? 245  ARG B CD  1 
ATOM   6266  N  NE  . ARG B  1 228 ? 20.481  12.106  13.726  1.00 21.88 ? 245  ARG B NE  1 
ATOM   6267  C  CZ  . ARG B  1 228 ? 20.808  10.861  14.047  1.00 22.69 ? 245  ARG B CZ  1 
ATOM   6268  N  NH1 . ARG B  1 228 ? 22.041  10.567  14.423  1.00 22.71 ? 245  ARG B NH1 1 
ATOM   6269  N  NH2 . ARG B  1 228 ? 19.887  9.909   13.997  1.00 22.48 ? 245  ARG B NH2 1 
ATOM   6270  N  N   . TYR B  1 229 ? 19.125  17.611  14.909  1.00 19.78 ? 246  TYR B N   1 
ATOM   6271  C  CA  . TYR B  1 229 ? 18.077  17.434  15.912  1.00 20.20 ? 246  TYR B CA  1 
ATOM   6272  C  C   . TYR B  1 229 ? 17.175  18.662  16.049  1.00 20.71 ? 246  TYR B C   1 
ATOM   6273  O  O   . TYR B  1 229 ? 16.114  18.567  16.674  1.00 20.85 ? 246  TYR B O   1 
ATOM   6274  C  CB  . TYR B  1 229 ? 18.729  17.069  17.247  1.00 19.60 ? 246  TYR B CB  1 
ATOM   6275  C  CG  . TYR B  1 229 ? 19.366  15.685  17.266  1.00 19.23 ? 246  TYR B CG  1 
ATOM   6276  C  CD1 . TYR B  1 229 ? 18.633  14.549  16.944  1.00 19.29 ? 246  TYR B CD1 1 
ATOM   6277  C  CD2 . TYR B  1 229 ? 20.712  15.519  17.574  1.00 19.06 ? 246  TYR B CD2 1 
ATOM   6278  C  CE1 . TYR B  1 229 ? 19.210  13.289  16.961  1.00 19.05 ? 246  TYR B CE1 1 
ATOM   6279  C  CE2 . TYR B  1 229 ? 21.302  14.265  17.590  1.00 18.82 ? 246  TYR B CE2 1 
ATOM   6280  C  CZ  . TYR B  1 229 ? 20.550  13.148  17.270  1.00 19.24 ? 246  TYR B CZ  1 
ATOM   6281  O  OH  . TYR B  1 229 ? 21.111  11.904  17.297  1.00 19.82 ? 246  TYR B OH  1 
ATOM   6282  N  N   . GLY B  1 230 ? 17.585  19.803  15.476  1.00 20.33 ? 247  GLY B N   1 
ATOM   6283  C  CA  . GLY B  1 230 ? 16.767  21.008  15.479  1.00 21.17 ? 247  GLY B CA  1 
ATOM   6284  C  C   . GLY B  1 230 ? 17.398  22.117  16.319  1.00 21.83 ? 247  GLY B C   1 
ATOM   6285  O  O   . GLY B  1 230 ? 18.171  21.846  17.234  1.00 20.10 ? 247  GLY B O   1 
ATOM   6286  N  N   . ARG B  1 231 ? 17.039  23.371  16.010  1.00 23.00 ? 248  ARG B N   1 
ATOM   6287  C  CA  . ARG B  1 231 ? 17.680  24.525  16.625  1.00 25.54 ? 248  ARG B CA  1 
ATOM   6288  C  C   . ARG B  1 231 ? 17.314  24.655  18.104  1.00 24.20 ? 248  ARG B C   1 
ATOM   6289  O  O   . ARG B  1 231 ? 18.041  25.317  18.839  1.00 25.37 ? 248  ARG B O   1 
ATOM   6290  C  CB  . ARG B  1 231 ? 17.358  25.837  15.898  1.00 29.74 ? 248  ARG B CB  1 
ATOM   6291  C  CG  . ARG B  1 231 ? 18.066  25.994  14.559  1.00 34.34 ? 248  ARG B CG  1 
ATOM   6292  C  CD  . ARG B  1 231 ? 18.195  27.447  14.114  1.00 37.22 ? 248  ARG B CD  1 
ATOM   6293  N  NE  . ARG B  1 231 ? 19.128  28.226  14.941  1.00 39.56 ? 248  ARG B NE  1 
ATOM   6294  C  CZ  . ARG B  1 231 ? 20.348  28.649  14.589  1.00 42.17 ? 248  ARG B CZ  1 
ATOM   6295  N  NH1 . ARG B  1 231 ? 20.919  28.232  13.471  1.00 43.12 ? 248  ARG B NH1 1 
ATOM   6296  N  NH2 . ARG B  1 231 ? 21.019  29.470  15.383  1.00 41.57 ? 248  ARG B NH2 1 
ATOM   6297  N  N   . ASN B  1 232 ? 16.203  24.043  18.546  1.00 23.27 ? 249  ASN B N   1 
ATOM   6298  C  CA  . ASN B  1 232 ? 15.772  24.183  19.931  1.00 23.66 ? 249  ASN B CA  1 
ATOM   6299  C  C   . ASN B  1 232 ? 16.367  23.098  20.830  1.00 22.01 ? 249  ASN B C   1 
ATOM   6300  O  O   . ASN B  1 232 ? 16.044  23.056  22.016  1.00 23.62 ? 249  ASN B O   1 
ATOM   6301  C  CB  . ASN B  1 232 ? 14.253  24.266  20.051  1.00 25.08 ? 249  ASN B CB  1 
ATOM   6302  C  CG  . ASN B  1 232 ? 13.529  22.965  19.796  1.00 27.25 ? 249  ASN B CG  1 
ATOM   6303  O  OD1 . ASN B  1 232 ? 14.131  21.884  19.761  1.00 28.56 ? 249  ASN B OD1 1 
ATOM   6304  N  ND2 . ASN B  1 232 ? 12.217  23.048  19.645  1.00 28.39 ? 249  ASN B ND2 1 
ATOM   6305  N  N   . THR B  1 233 ? 17.262  22.259  20.289  1.00 20.58 ? 250  THR B N   1 
ATOM   6306  C  CA  . THR B  1 233 ? 17.916  21.215  21.066  1.00 19.46 ? 250  THR B CA  1 
ATOM   6307  C  C   . THR B  1 233 ? 18.691  21.859  22.217  1.00 19.47 ? 250  THR B C   1 
ATOM   6308  O  O   . THR B  1 233 ? 19.537  22.719  21.990  1.00 20.55 ? 250  THR B O   1 
ATOM   6309  C  CB  . THR B  1 233 ? 18.850  20.396  20.171  1.00 18.94 ? 250  THR B CB  1 
ATOM   6310  O  OG1 . THR B  1 233 ? 18.113  19.831  19.086  1.00 18.69 ? 250  THR B OG1 1 
ATOM   6311  C  CG2 . THR B  1 233 ? 19.529  19.268  20.926  1.00 18.74 ? 250  THR B CG2 1 
ATOM   6312  N  N   . LEU B  1 234 ? 18.427  21.411  23.447  1.00 19.00 ? 251  LEU B N   1 
ATOM   6313  C  CA  . LEU B  1 234 ? 19.112  21.934  24.619  1.00 19.03 ? 251  LEU B CA  1 
ATOM   6314  C  C   . LEU B  1 234 ? 20.545  21.397  24.646  1.00 19.39 ? 251  LEU B C   1 
ATOM   6315  O  O   . LEU B  1 234 ? 20.750  20.185  24.594  1.00 19.15 ? 251  LEU B O   1 
ATOM   6316  C  CB  . LEU B  1 234 ? 18.336  21.530  25.872  1.00 19.76 ? 251  LEU B CB  1 
ATOM   6317  C  CG  . LEU B  1 234 ? 18.997  21.874  27.211  1.00 20.92 ? 251  LEU B CG  1 
ATOM   6318  C  CD1 . LEU B  1 234 ? 19.180  23.377  27.364  1.00 20.86 ? 251  LEU B CD1 1 
ATOM   6319  C  CD2 . LEU B  1 234 ? 18.213  21.309  28.380  1.00 21.67 ? 251  LEU B CD2 1 
ATOM   6320  N  N   . ILE B  1 235 ? 21.526  22.307  24.709  1.00 19.12 ? 252  ILE B N   1 
ATOM   6321  C  CA  . ILE B  1 235 ? 22.932  21.932  24.785  1.00 19.35 ? 252  ILE B CA  1 
ATOM   6322  C  C   . ILE B  1 235 ? 23.527  22.570  26.039  1.00 19.66 ? 252  ILE B C   1 
ATOM   6323  O  O   . ILE B  1 235 ? 23.645  23.793  26.129  1.00 19.94 ? 252  ILE B O   1 
ATOM   6324  C  CB  . ILE B  1 235 ? 23.688  22.333  23.503  1.00 19.62 ? 252  ILE B CB  1 
ATOM   6325  C  CG1 . ILE B  1 235 ? 23.014  21.779  22.250  1.00 20.52 ? 252  ILE B CG1 1 
ATOM   6326  C  CG2 . ILE B  1 235 ? 25.162  21.909  23.570  1.00 19.66 ? 252  ILE B CG2 1 
ATOM   6327  C  CD1 . ILE B  1 235 ? 23.531  22.378  20.955  1.00 21.50 ? 252  ILE B CD1 1 
ATOM   6328  N  N   . GLN B  1 236 ? 23.892  21.730  27.011  1.00 19.65 ? 253  GLN B N   1 
ATOM   6329  C  CA  . GLN B  1 236 ? 24.418  22.200  28.283  1.00 19.82 ? 253  GLN B CA  1 
ATOM   6330  C  C   . GLN B  1 236 ? 25.921  21.930  28.347  1.00 20.32 ? 253  GLN B C   1 
ATOM   6331  O  O   . GLN B  1 236 ? 26.342  20.788  28.202  1.00 19.77 ? 253  GLN B O   1 
ATOM   6332  C  CB  . GLN B  1 236 ? 23.725  21.490  29.444  1.00 20.61 ? 253  GLN B CB  1 
ATOM   6333  C  CG  . GLN B  1 236 ? 24.059  22.097  30.802  1.00 21.82 ? 253  GLN B CG  1 
ATOM   6334  C  CD  . GLN B  1 236 ? 24.482  21.066  31.820  1.00 23.17 ? 253  GLN B CD  1 
ATOM   6335  O  OE1 . GLN B  1 236 ? 23.683  20.245  32.282  1.00 23.30 ? 253  GLN B OE1 1 
ATOM   6336  N  NE2 . GLN B  1 236 ? 25.760  21.092  32.170  1.00 25.62 ? 253  GLN B NE2 1 
ATOM   6337  N  N   . PHE B  1 237 ? 26.713  22.987  28.573  1.00 20.44 ? 254  PHE B N   1 
ATOM   6338  C  CA  . PHE B  1 237 ? 28.157  22.883  28.723  1.00 20.96 ? 254  PHE B CA  1 
ATOM   6339  C  C   . PHE B  1 237 ? 28.480  22.550  30.177  1.00 20.63 ? 254  PHE B C   1 
ATOM   6340  O  O   . PHE B  1 237 ? 27.839  23.064  31.095  1.00 20.23 ? 254  PHE B O   1 
ATOM   6341  C  CB  . PHE B  1 237 ? 28.834  24.187  28.277  1.00 21.60 ? 254  PHE B CB  1 
ATOM   6342  C  CG  . PHE B  1 237 ? 28.953  24.403  26.772  1.00 23.01 ? 254  PHE B CG  1 
ATOM   6343  C  CD1 . PHE B  1 237 ? 27.822  24.507  25.967  1.00 24.16 ? 254  PHE B CD1 1 
ATOM   6344  C  CD2 . PHE B  1 237 ? 30.198  24.543  26.167  1.00 23.61 ? 254  PHE B CD2 1 
ATOM   6345  C  CE1 . PHE B  1 237 ? 27.934  24.700  24.595  1.00 24.91 ? 254  PHE B CE1 1 
ATOM   6346  C  CE2 . PHE B  1 237 ? 30.306  24.749  24.797  1.00 24.29 ? 254  PHE B CE2 1 
ATOM   6347  C  CZ  . PHE B  1 237 ? 29.176  24.824  24.012  1.00 24.75 ? 254  PHE B CZ  1 
ATOM   6348  N  N   . GLU B  1 238 ? 29.490  21.691  30.317  1.00 21.07 ? 255  GLU B N   1 
ATOM   6349  C  CA  . GLU B  1 238 ? 29.876  21.221  31.660  1.00 22.92 ? 255  GLU B CA  1 
ATOM   6350  C  C   . GLU B  1 238 ? 31.378  20.940  31.763  1.00 22.31 ? 255  GLU B C   1 
ATOM   6351  O  O   . GLU B  1 238 ? 31.914  20.292  30.860  1.00 21.08 ? 255  GLU B O   1 
ATOM   6352  C  CB  . GLU B  1 238 ? 29.162  19.912  31.981  1.00 25.48 ? 255  GLU B CB  1 
ATOM   6353  C  CG  . GLU B  1 238 ? 29.490  19.363  33.364  1.00 28.16 ? 255  GLU B CG  1 
ATOM   6354  C  CD  . GLU B  1 238 ? 28.472  19.726  34.426  1.00 29.81 ? 255  GLU B CD  1 
ATOM   6355  O  OE1 . GLU B  1 238 ? 28.723  19.389  35.594  1.00 33.10 ? 255  GLU B OE1 1 
ATOM   6356  O  OE2 . GLU B  1 238 ? 27.440  20.339  34.100  1.00 29.89 ? 255  GLU B OE2 1 
ATOM   6357  N  N   . ASP B  1 239 ? 32.029  21.496  32.772  1.00 22.00 ? 256  ASP B N   1 
ATOM   6358  C  CA  . ASP B  1 239 ? 33.408  21.193  33.134  1.00 22.37 ? 256  ASP B CA  1 
ATOM   6359  C  C   . ASP B  1 239 ? 34.393  21.652  32.056  1.00 22.54 ? 256  ASP B C   1 
ATOM   6360  O  O   . ASP B  1 239 ? 35.473  21.078  31.910  1.00 21.78 ? 256  ASP B O   1 
ATOM   6361  C  CB  . ASP B  1 239 ? 33.561  19.743  33.567  1.00 24.49 ? 256  ASP B CB  1 
ATOM   6362  C  CG  . ASP B  1 239 ? 33.022  19.413  34.955  1.00 26.42 ? 256  ASP B CG  1 
ATOM   6363  O  OD1 . ASP B  1 239 ? 32.579  20.345  35.666  1.00 28.28 ? 256  ASP B OD1 1 
ATOM   6364  O  OD2 . ASP B  1 239 ? 33.056  18.223  35.324  1.00 29.20 ? 256  ASP B OD2 1 
ATOM   6365  N  N   . PHE B  1 240 ? 34.025  22.719  31.338  1.00 23.19 ? 257  PHE B N   1 
ATOM   6366  C  CA  . PHE B  1 240 ? 34.955  23.470  30.514  1.00 23.83 ? 257  PHE B CA  1 
ATOM   6367  C  C   . PHE B  1 240 ? 35.831  24.320  31.429  1.00 25.67 ? 257  PHE B C   1 
ATOM   6368  O  O   . PHE B  1 240 ? 35.428  24.657  32.546  1.00 24.50 ? 257  PHE B O   1 
ATOM   6369  C  CB  . PHE B  1 240 ? 34.198  24.335  29.500  1.00 23.78 ? 257  PHE B CB  1 
ATOM   6370  C  CG  . PHE B  1 240 ? 33.756  23.602  28.240  1.00 23.81 ? 257  PHE B CG  1 
ATOM   6371  C  CD1 . PHE B  1 240 ? 32.697  22.700  28.267  1.00 23.31 ? 257  PHE B CD1 1 
ATOM   6372  C  CD2 . PHE B  1 240 ? 34.400  23.823  27.027  1.00 23.28 ? 257  PHE B CD2 1 
ATOM   6373  C  CE1 . PHE B  1 240 ? 32.305  22.033  27.114  1.00 23.93 ? 257  PHE B CE1 1 
ATOM   6374  C  CE2 . PHE B  1 240 ? 33.998  23.161  25.877  1.00 23.62 ? 257  PHE B CE2 1 
ATOM   6375  C  CZ  . PHE B  1 240 ? 32.952  22.266  25.922  1.00 23.81 ? 257  PHE B CZ  1 
ATOM   6376  N  N   . GLY B  1 241 ? 37.031  24.664  30.937  1.00 26.85 ? 258  GLY B N   1 
ATOM   6377  C  CA  . GLY B  1 241 ? 37.922  25.570  31.641  1.00 27.55 ? 258  GLY B CA  1 
ATOM   6378  C  C   . GLY B  1 241 ? 37.305  26.962  31.731  1.00 27.54 ? 258  GLY B C   1 
ATOM   6379  O  O   . GLY B  1 241 ? 36.441  27.311  30.934  1.00 26.73 ? 258  GLY B O   1 
ATOM   6380  N  N   . ASN B  1 242 ? 37.772  27.759  32.695  1.00 32.14 ? 259  ASN B N   1 
ATOM   6381  C  CA  . ASN B  1 242 ? 37.173  29.058  32.966  1.00 35.87 ? 259  ASN B CA  1 
ATOM   6382  C  C   . ASN B  1 242 ? 37.453  30.040  31.825  1.00 33.30 ? 259  ASN B C   1 
ATOM   6383  O  O   . ASN B  1 242 ? 36.671  30.956  31.604  1.00 34.13 ? 259  ASN B O   1 
ATOM   6384  C  CB  . ASN B  1 242 ? 37.584  29.559  34.347  1.00 40.43 ? 259  ASN B CB  1 
ATOM   6385  C  CG  . ASN B  1 242 ? 36.920  28.762  35.448  1.00 44.68 ? 259  ASN B CG  1 
ATOM   6386  O  OD1 . ASN B  1 242 ? 36.033  27.937  35.181  1.00 47.94 ? 259  ASN B OD1 1 
ATOM   6387  N  ND2 . ASN B  1 242 ? 37.321  28.997  36.690  1.00 44.93 ? 259  ASN B ND2 1 
ATOM   6388  N  N   . HIS B  1 243 ? 38.536  29.828  31.068  1.00 34.94 ? 260  HIS B N   1 
ATOM   6389  C  CA  . HIS B  1 243 ? 38.829  30.650  29.901  1.00 34.96 ? 260  HIS B CA  1 
ATOM   6390  C  C   . HIS B  1 243 ? 37.807  30.438  28.779  1.00 33.97 ? 260  HIS B C   1 
ATOM   6391  O  O   . HIS B  1 243 ? 37.734  31.261  27.867  1.00 36.27 ? 260  HIS B O   1 
ATOM   6392  C  CB  . HIS B  1 243 ? 40.237  30.351  29.373  1.00 37.32 ? 260  HIS B CB  1 
ATOM   6393  N  N   . ASN B  1 244 ? 37.043  29.333  28.835  1.00 28.65 ? 261  ASN B N   1 
ATOM   6394  C  CA  . ASN B  1 244 ? 36.136  28.943  27.763  1.00 26.91 ? 261  ASN B CA  1 
ATOM   6395  C  C   . ASN B  1 244 ? 34.673  28.926  28.220  1.00 25.58 ? 261  ASN B C   1 
ATOM   6396  O  O   . ASN B  1 244 ? 33.786  29.137  27.399  1.00 26.10 ? 261  ASN B O   1 
ATOM   6397  C  CB  . ASN B  1 244 ? 36.534  27.585  27.191  1.00 26.45 ? 261  ASN B CB  1 
ATOM   6398  C  CG  . ASN B  1 244 ? 37.839  27.642  26.430  1.00 26.92 ? 261  ASN B CG  1 
ATOM   6399  O  OD1 . ASN B  1 244 ? 38.168  28.676  25.843  1.00 26.25 ? 261  ASN B OD1 1 
ATOM   6400  N  ND2 . ASN B  1 244 ? 38.573  26.539  26.386  1.00 26.55 ? 261  ASN B ND2 1 
ATOM   6401  N  N   . ALA B  1 245 ? 34.413  28.683  29.511  1.00 25.41 ? 262  ALA B N   1 
ATOM   6402  C  CA  . ALA B  1 245 ? 33.050  28.480  29.991  1.00 25.35 ? 262  ALA B CA  1 
ATOM   6403  C  C   . ALA B  1 245 ? 32.192  29.732  29.785  1.00 25.56 ? 262  ALA B C   1 
ATOM   6404  O  O   . ALA B  1 245 ? 31.186  29.681  29.076  1.00 24.76 ? 262  ALA B O   1 
ATOM   6405  C  CB  . ALA B  1 245 ? 33.067  28.041  31.438  1.00 25.58 ? 262  ALA B CB  1 
ATOM   6406  N  N   A PHE B  1 246 ? 32.608  30.849  30.397  0.52 25.66 ? 263  PHE B N   1 
ATOM   6407  N  N   B PHE B  1 246 ? 32.589  30.853  30.404  0.48 24.50 ? 263  PHE B N   1 
ATOM   6408  C  CA  A PHE B  1 246 ? 31.886  32.106  30.269  0.52 26.28 ? 263  PHE B CA  1 
ATOM   6409  C  CA  B PHE B  1 246 ? 31.849  32.101  30.270  0.48 24.18 ? 263  PHE B CA  1 
ATOM   6410  C  C   A PHE B  1 246 ? 31.868  32.534  28.804  0.52 25.07 ? 263  PHE B C   1 
ATOM   6411  C  C   B PHE B  1 246 ? 31.874  32.566  28.813  0.48 24.00 ? 263  PHE B C   1 
ATOM   6412  O  O   A PHE B  1 246 ? 30.854  33.008  28.299  0.52 24.15 ? 263  PHE B O   1 
ATOM   6413  O  O   B PHE B  1 246 ? 30.882  33.089  28.312  0.48 23.23 ? 263  PHE B O   1 
ATOM   6414  C  CB  A PHE B  1 246 ? 32.518  33.203  31.134  0.52 28.43 ? 263  PHE B CB  1 
ATOM   6415  C  CB  B PHE B  1 246 ? 32.395  33.175  31.221  0.48 24.51 ? 263  PHE B CB  1 
ATOM   6416  C  CG  A PHE B  1 246 ? 31.892  34.579  30.946  0.52 29.86 ? 263  PHE B CG  1 
ATOM   6417  C  CG  B PHE B  1 246 ? 31.490  33.562  32.388  0.48 23.79 ? 263  PHE B CG  1 
ATOM   6418  C  CD1 A PHE B  1 246 ? 30.808  34.985  31.718  0.52 31.22 ? 263  PHE B CD1 1 
ATOM   6419  C  CD1 B PHE B  1 246 ? 30.171  33.949  32.171  0.48 23.67 ? 263  PHE B CD1 1 
ATOM   6420  C  CD2 A PHE B  1 246 ? 32.382  35.460  29.986  0.52 30.83 ? 263  PHE B CD2 1 
ATOM   6421  C  CD2 B PHE B  1 246 ? 31.958  33.547  33.698  0.48 23.90 ? 263  PHE B CD2 1 
ATOM   6422  C  CE1 A PHE B  1 246 ? 30.238  36.238  31.537  0.52 31.89 ? 263  PHE B CE1 1 
ATOM   6423  C  CE1 B PHE B  1 246 ? 29.352  34.310  33.230  0.48 24.04 ? 263  PHE B CE1 1 
ATOM   6424  C  CE2 A PHE B  1 246 ? 31.803  36.706  29.805  0.52 31.17 ? 263  PHE B CE2 1 
ATOM   6425  C  CE2 B PHE B  1 246 ? 31.133  33.904  34.756  0.48 23.39 ? 263  PHE B CE2 1 
ATOM   6426  C  CZ  A PHE B  1 246 ? 30.735  37.093  30.579  0.52 31.38 ? 263  PHE B CZ  1 
ATOM   6427  C  CZ  B PHE B  1 246 ? 29.833  34.284  34.521  0.48 23.99 ? 263  PHE B CZ  1 
ATOM   6428  N  N   . ARG B  1 247 ? 33.012  32.370  28.135  1.00 23.73 ? 264  ARG B N   1 
ATOM   6429  C  CA  . ARG B  1 247 ? 33.198  32.857  26.779  1.00 24.91 ? 264  ARG B CA  1 
ATOM   6430  C  C   . ARG B  1 247 ? 32.206  32.199  25.819  1.00 23.63 ? 264  ARG B C   1 
ATOM   6431  O  O   . ARG B  1 247 ? 31.620  32.868  24.971  1.00 23.73 ? 264  ARG B O   1 
ATOM   6432  C  CB  . ARG B  1 247 ? 34.664  32.581  26.428  1.00 26.60 ? 264  ARG B CB  1 
ATOM   6433  C  CG  . ARG B  1 247 ? 35.151  33.154  25.108  1.00 27.63 ? 264  ARG B CG  1 
ATOM   6434  C  CD  . ARG B  1 247 ? 36.659  32.959  24.982  1.00 27.93 ? 264  ARG B CD  1 
ATOM   6435  N  NE  . ARG B  1 247 ? 37.075  31.579  24.710  1.00 28.35 ? 264  ARG B NE  1 
ATOM   6436  C  CZ  . ARG B  1 247 ? 37.144  31.024  23.500  1.00 28.03 ? 264  ARG B CZ  1 
ATOM   6437  N  NH1 . ARG B  1 247 ? 36.738  31.682  22.432  1.00 28.53 ? 264  ARG B NH1 1 
ATOM   6438  N  NH2 . ARG B  1 247 ? 37.653  29.815  23.353  1.00 29.51 ? 264  ARG B NH2 1 
ATOM   6439  N  N   . PHE B  1 248 ? 32.017  30.882  25.960  1.00 23.88 ? 265  PHE B N   1 
ATOM   6440  C  CA  . PHE B  1 248 ? 31.125  30.143  25.081  1.00 23.89 ? 265  PHE B CA  1 
ATOM   6441  C  C   . PHE B  1 248 ? 29.672  30.419  25.460  1.00 23.61 ? 265  PHE B C   1 
ATOM   6442  O  O   . PHE B  1 248 ? 28.822  30.463  24.576  1.00 24.08 ? 265  PHE B O   1 
ATOM   6443  C  CB  . PHE B  1 248 ? 31.440  28.643  25.082  1.00 24.24 ? 265  PHE B CB  1 
ATOM   6444  C  CG  . PHE B  1 248 ? 32.671  28.231  24.281  1.00 24.31 ? 265  PHE B CG  1 
ATOM   6445  C  CD1 . PHE B  1 248 ? 33.057  28.924  23.137  1.00 26.22 ? 265  PHE B CD1 1 
ATOM   6446  C  CD2 . PHE B  1 248 ? 33.440  27.143  24.680  1.00 24.63 ? 265  PHE B CD2 1 
ATOM   6447  C  CE1 . PHE B  1 248 ? 34.182  28.541  22.419  1.00 26.28 ? 265  PHE B CE1 1 
ATOM   6448  C  CE2 . PHE B  1 248 ? 34.552  26.752  23.949  1.00 25.25 ? 265  PHE B CE2 1 
ATOM   6449  C  CZ  . PHE B  1 248 ? 34.925  27.457  22.827  1.00 26.13 ? 265  PHE B CZ  1 
ATOM   6450  N  N   . LEU B  1 249 ? 29.391  30.626  26.755  1.00 24.00 ? 266  LEU B N   1 
ATOM   6451  C  CA  . LEU B  1 249 ? 28.048  31.003  27.177  1.00 24.83 ? 266  LEU B CA  1 
ATOM   6452  C  C   . LEU B  1 249 ? 27.648  32.300  26.471  1.00 25.98 ? 266  LEU B C   1 
ATOM   6453  O  O   . LEU B  1 249 ? 26.568  32.396  25.891  1.00 23.59 ? 266  LEU B O   1 
ATOM   6454  C  CB  . LEU B  1 249 ? 27.947  31.129  28.698  1.00 24.68 ? 266  LEU B CB  1 
ATOM   6455  C  CG  . LEU B  1 249 ? 26.599  31.620  29.243  1.00 25.41 ? 266  LEU B CG  1 
ATOM   6456  C  CD1 . LEU B  1 249 ? 25.450  30.732  28.780  1.00 26.11 ? 266  LEU B CD1 1 
ATOM   6457  C  CD2 . LEU B  1 249 ? 26.615  31.705  30.755  1.00 25.18 ? 266  LEU B CD2 1 
ATOM   6458  N  N   . ARG B  1 250 ? 28.537  33.299  26.503  1.00 28.33 ? 267  ARG B N   1 
ATOM   6459  C  CA  . ARG B  1 250 ? 28.255  34.583  25.877  1.00 29.80 ? 267  ARG B CA  1 
ATOM   6460  C  C   . ARG B  1 250 ? 28.139  34.425  24.363  1.00 27.81 ? 267  ARG B C   1 
ATOM   6461  O  O   . ARG B  1 250 ? 27.297  35.067  23.745  1.00 26.51 ? 267  ARG B O   1 
ATOM   6462  C  CB  . ARG B  1 250 ? 29.320  35.628  26.226  1.00 34.26 ? 267  ARG B CB  1 
ATOM   6463  C  CG  . ARG B  1 250 ? 29.102  36.994  25.585  1.00 39.89 ? 267  ARG B CG  1 
ATOM   6464  C  CD  . ARG B  1 250 ? 30.068  38.042  26.128  1.00 45.29 ? 267  ARG B CD  1 
ATOM   6465  N  NE  . ARG B  1 250 ? 31.439  37.515  26.150  1.00 50.02 ? 267  ARG B NE  1 
ATOM   6466  C  CZ  . ARG B  1 250 ? 32.428  37.792  25.298  1.00 53.05 ? 267  ARG B CZ  1 
ATOM   6467  N  NH1 . ARG B  1 250 ? 32.279  38.703  24.348  1.00 54.92 ? 267  ARG B NH1 1 
ATOM   6468  N  NH2 . ARG B  1 250 ? 33.581  37.150  25.413  1.00 52.07 ? 267  ARG B NH2 1 
ATOM   6469  N  N   . LYS B  1 251 ? 28.983  33.573  23.770  1.00 27.18 ? 268  LYS B N   1 
ATOM   6470  C  CA  . LYS B  1 251 ? 29.010  33.404  22.323  1.00 27.75 ? 268  LYS B CA  1 
ATOM   6471  C  C   . LYS B  1 251 ? 27.706  32.787  21.807  1.00 26.65 ? 268  LYS B C   1 
ATOM   6472  O  O   . LYS B  1 251 ? 27.209  33.194  20.759  1.00 27.51 ? 268  LYS B O   1 
ATOM   6473  C  CB  . LYS B  1 251 ? 30.200  32.542  21.881  1.00 28.96 ? 268  LYS B CB  1 
ATOM   6474  C  CG  . LYS B  1 251 ? 30.448  32.505  20.374  1.00 30.26 ? 268  LYS B CG  1 
ATOM   6475  C  CD  . LYS B  1 251 ? 31.721  31.775  19.958  1.00 32.00 ? 268  LYS B CD  1 
ATOM   6476  C  CE  . LYS B  1 251 ? 31.900  31.713  18.468  1.00 33.67 ? 268  LYS B CE  1 
ATOM   6477  N  NZ  . LYS B  1 251 ? 33.137  31.015  18.103  1.00 34.95 ? 268  LYS B NZ  1 
ATOM   6478  N  N   . TYR B  1 252 ? 27.155  31.798  22.526  1.00 25.00 ? 269  TYR B N   1 
ATOM   6479  C  CA  . TYR B  1 252 ? 26.166  30.910  21.928  1.00 24.49 ? 269  TYR B CA  1 
ATOM   6480  C  C   . TYR B  1 252 ? 24.752  31.135  22.465  1.00 24.88 ? 269  TYR B C   1 
ATOM   6481  O  O   . TYR B  1 252 ? 23.800  30.650  21.862  1.00 24.80 ? 269  TYR B O   1 
ATOM   6482  C  CB  . TYR B  1 252 ? 26.582  29.455  22.164  1.00 24.33 ? 269  TYR B CB  1 
ATOM   6483  C  CG  . TYR B  1 252 ? 27.821  29.002  21.403  1.00 23.34 ? 269  TYR B CG  1 
ATOM   6484  C  CD1 . TYR B  1 252 ? 27.962  29.212  20.035  1.00 24.65 ? 269  TYR B CD1 1 
ATOM   6485  C  CD2 . TYR B  1 252 ? 28.860  28.369  22.067  1.00 23.33 ? 269  TYR B CD2 1 
ATOM   6486  C  CE1 . TYR B  1 252 ? 29.092  28.790  19.350  1.00 24.87 ? 269  TYR B CE1 1 
ATOM   6487  C  CE2 . TYR B  1 252 ? 29.994  27.943  21.399  1.00 24.39 ? 269  TYR B CE2 1 
ATOM   6488  C  CZ  . TYR B  1 252 ? 30.110  28.153  20.039  1.00 25.61 ? 269  TYR B CZ  1 
ATOM   6489  O  OH  . TYR B  1 252 ? 31.248  27.725  19.419  1.00 29.23 ? 269  TYR B OH  1 
ATOM   6490  N  N   . ARG B  1 253 ? 24.592  31.856  23.581  1.00 25.14 ? 270  ARG B N   1 
ATOM   6491  C  CA  . ARG B  1 253 ? 23.332  31.815  24.314  1.00 26.30 ? 270  ARG B CA  1 
ATOM   6492  C  C   . ARG B  1 253 ? 22.178  32.446  23.534  1.00 26.54 ? 270  ARG B C   1 
ATOM   6493  O  O   . ARG B  1 253 ? 21.021  32.111  23.793  1.00 24.35 ? 270  ARG B O   1 
ATOM   6494  C  CB  . ARG B  1 253 ? 23.433  32.458  25.700  1.00 27.75 ? 270  ARG B CB  1 
ATOM   6495  C  CG  . ARG B  1 253 ? 23.667  33.959  25.705  1.00 28.21 ? 270  ARG B CG  1 
ATOM   6496  C  CD  . ARG B  1 253 ? 23.852  34.453  27.127  1.00 28.98 ? 270  ARG B CD  1 
ATOM   6497  N  NE  . ARG B  1 253 ? 22.636  34.234  27.917  1.00 29.11 ? 270  ARG B NE  1 
ATOM   6498  C  CZ  . ARG B  1 253 ? 22.566  34.241  29.236  1.00 28.85 ? 270  ARG B CZ  1 
ATOM   6499  N  NH1 . ARG B  1 253 ? 23.616  34.605  29.955  1.00 30.14 ? 270  ARG B NH1 1 
ATOM   6500  N  NH2 . ARG B  1 253 ? 21.438  33.882  29.829  1.00 28.21 ? 270  ARG B NH2 1 
ATOM   6501  N  N   . GLU B  1 254 ? 22.476  33.365  22.605  1.00 26.46 ? 271  GLU B N   1 
ATOM   6502  C  CA  . GLU B  1 254 ? 21.434  33.993  21.806  1.00 30.59 ? 271  GLU B CA  1 
ATOM   6503  C  C   . GLU B  1 254 ? 21.322  33.335  20.431  1.00 29.05 ? 271  GLU B C   1 
ATOM   6504  O  O   . GLU B  1 254 ? 20.431  33.684  19.660  1.00 27.96 ? 271  GLU B O   1 
ATOM   6505  C  CB  . GLU B  1 254 ? 21.683  35.498  21.685  1.00 35.44 ? 271  GLU B CB  1 
ATOM   6506  C  CG  . GLU B  1 254 ? 21.454  36.248  22.995  1.00 40.08 ? 271  GLU B CG  1 
ATOM   6507  C  CD  . GLU B  1 254 ? 21.754  37.737  22.938  1.00 47.91 ? 271  GLU B CD  1 
ATOM   6508  O  OE1 . GLU B  1 254 ? 21.460  38.424  23.943  1.00 53.83 ? 271  GLU B OE1 1 
ATOM   6509  O  OE2 . GLU B  1 254 ? 22.283  38.212  21.905  1.00 51.19 ? 271  GLU B OE2 1 
ATOM   6510  N  N   . LYS B  1 255 ? 22.227  32.394  20.126  1.00 27.84 ? 272  LYS B N   1 
ATOM   6511  C  CA  . LYS B  1 255 ? 22.239  31.712  18.839  1.00 29.10 ? 272  LYS B CA  1 
ATOM   6512  C  C   . LYS B  1 255 ? 21.640  30.310  18.959  1.00 26.11 ? 272  LYS B C   1 
ATOM   6513  O  O   . LYS B  1 255 ? 21.094  29.792  17.990  1.00 25.00 ? 272  LYS B O   1 
ATOM   6514  C  CB  . LYS B  1 255 ? 23.669  31.596  18.297  1.00 33.66 ? 272  LYS B CB  1 
ATOM   6515  C  CG  . LYS B  1 255 ? 24.326  32.913  17.891  1.00 39.33 ? 272  LYS B CG  1 
ATOM   6516  C  CD  . LYS B  1 255 ? 25.736  32.782  17.315  1.00 43.75 ? 272  LYS B CD  1 
ATOM   6517  C  CE  . LYS B  1 255 ? 25.789  32.343  15.875  1.00 47.71 ? 272  LYS B CE  1 
ATOM   6518  N  NZ  . LYS B  1 255 ? 25.600  30.904  15.662  1.00 49.29 ? 272  LYS B NZ  1 
ATOM   6519  N  N   . TYR B  1 256 ? 21.779  29.697  20.140  1.00 24.48 ? 273  TYR B N   1 
ATOM   6520  C  CA  . TYR B  1 256 ? 21.366  28.324  20.371  1.00 23.49 ? 273  TYR B CA  1 
ATOM   6521  C  C   . TYR B  1 256 ? 20.650  28.226  21.713  1.00 22.42 ? 273  TYR B C   1 
ATOM   6522  O  O   . TYR B  1 256 ? 20.629  29.177  22.489  1.00 21.75 ? 273  TYR B O   1 
ATOM   6523  C  CB  . TYR B  1 256 ? 22.593  27.407  20.357  1.00 23.47 ? 273  TYR B CB  1 
ATOM   6524  C  CG  . TYR B  1 256 ? 23.323  27.314  19.025  1.00 23.64 ? 273  TYR B CG  1 
ATOM   6525  C  CD1 . TYR B  1 256 ? 22.777  26.598  17.970  1.00 24.21 ? 273  TYR B CD1 1 
ATOM   6526  C  CD2 . TYR B  1 256 ? 24.561  27.915  18.828  1.00 24.20 ? 273  TYR B CD2 1 
ATOM   6527  C  CE1 . TYR B  1 256 ? 23.422  26.499  16.752  1.00 24.69 ? 273  TYR B CE1 1 
ATOM   6528  C  CE2 . TYR B  1 256 ? 25.226  27.813  17.615  1.00 24.15 ? 273  TYR B CE2 1 
ATOM   6529  C  CZ  . TYR B  1 256 ? 24.655  27.100  16.576  1.00 24.47 ? 273  TYR B CZ  1 
ATOM   6530  O  OH  . TYR B  1 256 ? 25.266  26.983  15.364  1.00 24.60 ? 273  TYR B OH  1 
ATOM   6531  N  N   . CYS B  1 257 ? 20.058  27.058  21.976  1.00 21.20 ? 274  CYS B N   1 
ATOM   6532  C  CA  . CYS B  1 257 ? 19.420  26.799  23.253  1.00 21.10 ? 274  CYS B CA  1 
ATOM   6533  C  C   . CYS B  1 257 ? 20.450  26.197  24.202  1.00 20.93 ? 274  CYS B C   1 
ATOM   6534  O  O   . CYS B  1 257 ? 20.657  24.987  24.203  1.00 21.14 ? 274  CYS B O   1 
ATOM   6535  C  CB  . CYS B  1 257 ? 18.213  25.888  23.084  1.00 21.01 ? 274  CYS B CB  1 
ATOM   6536  S  SG  . CYS B  1 257 ? 17.278  25.688  24.618  1.00 22.04 ? 274  CYS B SG  1 
ATOM   6537  N  N   . THR B  1 258 ? 21.118  27.049  24.993  1.00 20.83 ? 275  THR B N   1 
ATOM   6538  C  CA  . THR B  1 258 ? 22.296  26.601  25.712  1.00 20.45 ? 275  THR B CA  1 
ATOM   6539  C  C   . THR B  1 258 ? 22.428  27.321  27.052  1.00 20.11 ? 275  THR B C   1 
ATOM   6540  O  O   . THR B  1 258 ? 22.048  28.486  27.188  1.00 20.37 ? 275  THR B O   1 
ATOM   6541  C  CB  . THR B  1 258 ? 23.531  26.775  24.824  1.00 21.29 ? 275  THR B CB  1 
ATOM   6542  O  OG1 . THR B  1 258 ? 24.612  26.219  25.572  1.00 23.17 ? 275  THR B OG1 1 
ATOM   6543  C  CG2 . THR B  1 258 ? 23.816  28.226  24.479  1.00 21.57 ? 275  THR B CG2 1 
ATOM   6544  N  N   . PHE B  1 259 ? 22.931  26.571  28.042  1.00 18.90 ? 276  PHE B N   1 
ATOM   6545  C  CA  . PHE B  1 259 ? 23.339  27.114  29.324  1.00 19.66 ? 276  PHE B CA  1 
ATOM   6546  C  C   . PHE B  1 259 ? 24.583  26.370  29.794  1.00 19.65 ? 276  PHE B C   1 
ATOM   6547  O  O   . PHE B  1 259 ? 24.954  25.343  29.226  1.00 19.11 ? 276  PHE B O   1 
ATOM   6548  C  CB  . PHE B  1 259 ? 22.227  27.078  30.380  1.00 19.93 ? 276  PHE B CB  1 
ATOM   6549  C  CG  . PHE B  1 259 ? 21.859  25.750  31.029  1.00 21.05 ? 276  PHE B CG  1 
ATOM   6550  C  CD1 . PHE B  1 259 ? 21.041  24.832  30.376  1.00 22.41 ? 276  PHE B CD1 1 
ATOM   6551  C  CD2 . PHE B  1 259 ? 22.254  25.462  32.332  1.00 21.49 ? 276  PHE B CD2 1 
ATOM   6552  C  CE1 . PHE B  1 259 ? 20.671  23.645  30.993  1.00 22.22 ? 276  PHE B CE1 1 
ATOM   6553  C  CE2 . PHE B  1 259 ? 21.871  24.279  32.950  1.00 21.86 ? 276  PHE B CE2 1 
ATOM   6554  C  CZ  . PHE B  1 259 ? 21.084  23.373  32.280  1.00 22.33 ? 276  PHE B CZ  1 
ATOM   6555  N  N   . ASN B  1 260 ? 25.217  26.943  30.821  1.00 19.63 ? 277  ASN B N   1 
ATOM   6556  C  CA  . ASN B  1 260 ? 26.356  26.356  31.497  1.00 21.43 ? 277  ASN B CA  1 
ATOM   6557  C  C   . ASN B  1 260 ? 25.969  26.174  32.960  1.00 21.19 ? 277  ASN B C   1 
ATOM   6558  O  O   . ASN B  1 260 ? 25.735  27.153  33.666  1.00 20.78 ? 277  ASN B O   1 
ATOM   6559  C  CB  . ASN B  1 260 ? 27.599  27.225  31.327  1.00 22.37 ? 277  ASN B CB  1 
ATOM   6560  C  CG  . ASN B  1 260 ? 28.818  26.587  31.950  1.00 23.04 ? 277  ASN B CG  1 
ATOM   6561  O  OD1 . ASN B  1 260 ? 28.823  26.310  33.154  1.00 23.06 ? 277  ASN B OD1 1 
ATOM   6562  N  ND2 . ASN B  1 260 ? 29.844  26.329  31.151  1.00 23.56 ? 277  ASN B ND2 1 
ATOM   6563  N  N   . ASP B  1 261 ? 25.899  24.919  33.408  1.00 21.97 ? 278  ASP B N   1 
ATOM   6564  C  CA  . ASP B  1 261 ? 25.398  24.640  34.742  1.00 23.28 ? 278  ASP B CA  1 
ATOM   6565  C  C   . ASP B  1 261 ? 26.370  25.129  35.811  1.00 23.49 ? 278  ASP B C   1 
ATOM   6566  O  O   . ASP B  1 261 ? 25.940  25.560  36.882  1.00 22.40 ? 278  ASP B O   1 
ATOM   6567  C  CB  . ASP B  1 261 ? 25.087  23.172  34.955  1.00 23.76 ? 278  ASP B CB  1 
ATOM   6568  C  CG  . ASP B  1 261 ? 24.399  22.906  36.283  1.00 24.99 ? 278  ASP B CG  1 
ATOM   6569  O  OD1 . ASP B  1 261 ? 23.336  23.522  36.504  1.00 24.66 ? 278  ASP B OD1 1 
ATOM   6570  O  OD2 . ASP B  1 261 ? 24.957  22.133  37.092  1.00 25.83 ? 278  ASP B OD2 1 
ATOM   6571  N  N   . ASP B  1 262 ? 27.673  25.065  35.507  1.00 24.45 ? 279  ASP B N   1 
ATOM   6572  C  CA  . ASP B  1 262 ? 28.707  25.434  36.461  1.00 25.37 ? 279  ASP B CA  1 
ATOM   6573  C  C   . ASP B  1 262 ? 28.550  26.904  36.852  1.00 23.48 ? 279  ASP B C   1 
ATOM   6574  O  O   . ASP B  1 262 ? 28.820  27.268  37.995  1.00 23.45 ? 279  ASP B O   1 
ATOM   6575  C  CB  . ASP B  1 262 ? 30.098  25.085  35.942  1.00 27.93 ? 279  ASP B CB  1 
ATOM   6576  C  CG  . ASP B  1 262 ? 30.331  23.614  35.608  1.00 31.75 ? 279  ASP B CG  1 
ATOM   6577  O  OD1 . ASP B  1 262 ? 29.897  22.751  36.402  1.00 36.52 ? 279  ASP B OD1 1 
ATOM   6578  O  OD2 . ASP B  1 262 ? 30.960  23.335  34.564  1.00 34.51 ? 279  ASP B OD2 1 
ATOM   6579  N  N   . ILE B  1 263 ? 28.093  27.733  35.908  1.00 22.47 ? 280  ILE B N   1 
ATOM   6580  C  CA  . ILE B  1 263 ? 27.943  29.164  36.121  1.00 22.18 ? 280  ILE B CA  1 
ATOM   6581  C  C   . ILE B  1 263 ? 26.521  29.470  36.598  1.00 22.19 ? 280  ILE B C   1 
ATOM   6582  O  O   . ILE B  1 263 ? 26.323  30.037  37.670  1.00 21.03 ? 280  ILE B O   1 
ATOM   6583  C  CB  . ILE B  1 263 ? 28.288  29.934  34.833  1.00 22.62 ? 280  ILE B CB  1 
ATOM   6584  C  CG1 . ILE B  1 263 ? 29.756  29.730  34.427  1.00 23.09 ? 280  ILE B CG1 1 
ATOM   6585  C  CG2 . ILE B  1 263 ? 27.953  31.422  34.970  1.00 23.09 ? 280  ILE B CG2 1 
ATOM   6586  C  CD1 . ILE B  1 263 ? 30.085  30.210  33.025  1.00 22.99 ? 280  ILE B CD1 1 
ATOM   6587  N  N   . GLN B  1 264 ? 25.533  29.101  35.777  1.00 21.89 ? 281  GLN B N   1 
ATOM   6588  C  CA  . GLN B  1 264 ? 24.165  29.570  35.952  1.00 21.62 ? 281  GLN B CA  1 
ATOM   6589  C  C   . GLN B  1 264 ? 23.426  28.728  36.988  1.00 21.73 ? 281  GLN B C   1 
ATOM   6590  O  O   . GLN B  1 264 ? 22.626  29.253  37.764  1.00 22.12 ? 281  GLN B O   1 
ATOM   6591  C  CB  . GLN B  1 264 ? 23.449  29.572  34.604  1.00 21.08 ? 281  GLN B CB  1 
ATOM   6592  C  CG  . GLN B  1 264 ? 23.958  30.645  33.650  1.00 21.83 ? 281  GLN B CG  1 
ATOM   6593  C  CD  . GLN B  1 264 ? 23.545  30.396  32.215  1.00 21.16 ? 281  GLN B CD  1 
ATOM   6594  O  OE1 . GLN B  1 264 ? 23.915  29.381  31.619  1.00 21.09 ? 281  GLN B OE1 1 
ATOM   6595  N  NE2 . GLN B  1 264 ? 22.787  31.317  31.639  1.00 20.32 ? 281  GLN B NE2 1 
ATOM   6596  N  N   . GLY B  1 265 ? 23.671  27.417  36.983  1.00 21.21 ? 282  GLY B N   1 
ATOM   6597  C  CA  . GLY B  1 265 ? 23.070  26.545  37.979  1.00 21.59 ? 282  GLY B CA  1 
ATOM   6598  C  C   . GLY B  1 265 ? 23.566  26.891  39.380  1.00 21.47 ? 282  GLY B C   1 
ATOM   6599  O  O   . GLY B  1 265 ? 22.786  26.956  40.328  1.00 20.67 ? 282  GLY B O   1 
ATOM   6600  N  N   . THR B  1 266 ? 24.882  27.099  39.490  1.00 20.56 ? 283  THR B N   1 
ATOM   6601  C  CA  . THR B  1 266 ? 25.501  27.476  40.747  1.00 21.48 ? 283  THR B CA  1 
ATOM   6602  C  C   . THR B  1 266 ? 24.907  28.793  41.244  1.00 20.26 ? 283  THR B C   1 
ATOM   6603  O  O   . THR B  1 266 ? 24.622  28.940  42.428  1.00 21.29 ? 283  THR B O   1 
ATOM   6604  C  CB  . THR B  1 266 ? 27.012  27.589  40.556  1.00 22.27 ? 283  THR B CB  1 
ATOM   6605  O  OG1 . THR B  1 266 ? 27.431  26.296  40.121  1.00 22.62 ? 283  THR B OG1 1 
ATOM   6606  C  CG2 . THR B  1 266 ? 27.716  27.985  41.842  1.00 23.69 ? 283  THR B CG2 1 
ATOM   6607  N  N   . ALA B  1 267 ? 24.740  29.756  40.337  1.00 19.82 ? 284  ALA B N   1 
ATOM   6608  C  CA  . ALA B  1 267 ? 24.232  31.061  40.723  1.00 19.69 ? 284  ALA B CA  1 
ATOM   6609  C  C   . ALA B  1 267 ? 22.824  30.923  41.304  1.00 20.02 ? 284  ALA B C   1 
ATOM   6610  O  O   . ALA B  1 267 ? 22.499  31.561  42.305  1.00 19.27 ? 284  ALA B O   1 
ATOM   6611  C  CB  . ALA B  1 267 ? 24.270  32.005  39.548  1.00 19.68 ? 284  ALA B CB  1 
ATOM   6612  N  N   . ALA B  1 268 ? 21.999  30.074  40.681  1.00 19.78 ? 285  ALA B N   1 
ATOM   6613  C  CA  . ALA B  1 268 ? 20.609  29.917  41.087  1.00 19.33 ? 285  ALA B CA  1 
ATOM   6614  C  C   . ALA B  1 268 ? 20.514  29.230  42.449  1.00 18.51 ? 285  ALA B C   1 
ATOM   6615  O  O   . ALA B  1 268 ? 19.693  29.609  43.276  1.00 18.70 ? 285  ALA B O   1 
ATOM   6616  C  CB  . ALA B  1 268 ? 19.849  29.154  40.022  1.00 19.60 ? 285  ALA B CB  1 
ATOM   6617  N  N   . VAL B  1 269 ? 21.360  28.223  42.691  1.00 18.75 ? 286  VAL B N   1 
ATOM   6618  C  CA  . VAL B  1 269 ? 21.283  27.472  43.932  1.00 20.15 ? 286  VAL B CA  1 
ATOM   6619  C  C   . VAL B  1 269 ? 21.810  28.334  45.081  1.00 19.89 ? 286  VAL B C   1 
ATOM   6620  O  O   . VAL B  1 269 ? 21.236  28.313  46.167  1.00 19.08 ? 286  VAL B O   1 
ATOM   6621  C  CB  . VAL B  1 269 ? 21.977  26.094  43.856  1.00 22.31 ? 286  VAL B CB  1 
ATOM   6622  C  CG1 . VAL B  1 269 ? 23.486  26.208  43.727  1.00 23.69 ? 286  VAL B CG1 1 
ATOM   6623  C  CG2 . VAL B  1 269 ? 21.621  25.211  45.047  1.00 23.59 ? 286  VAL B CG2 1 
ATOM   6624  N  N   . ALA B  1 270 ? 22.890  29.100  44.845  1.00 20.15 ? 287  ALA B N   1 
ATOM   6625  C  CA  . ALA B  1 270 ? 23.405  30.014  45.856  1.00 19.97 ? 287  ALA B CA  1 
ATOM   6626  C  C   . ALA B  1 270 ? 22.330  31.031  46.237  1.00 19.91 ? 287  ALA B C   1 
ATOM   6627  O  O   . ALA B  1 270 ? 22.079  31.251  47.420  1.00 19.42 ? 287  ALA B O   1 
ATOM   6628  C  CB  . ALA B  1 270 ? 24.664  30.709  45.376  1.00 19.87 ? 287  ALA B CB  1 
ATOM   6629  N  N   . LEU B  1 271 ? 21.706  31.647  45.226  1.00 19.84 ? 288  LEU B N   1 
ATOM   6630  C  CA  . LEU B  1 271 ? 20.698  32.669  45.453  1.00 19.45 ? 288  LEU B CA  1 
ATOM   6631  C  C   . LEU B  1 271 ? 19.539  32.082  46.263  1.00 20.15 ? 288  LEU B C   1 
ATOM   6632  O  O   . LEU B  1 271 ? 19.078  32.709  47.214  1.00 20.72 ? 288  LEU B O   1 
ATOM   6633  C  CB  . LEU B  1 271 ? 20.215  33.274  44.135  1.00 19.79 ? 288  LEU B CB  1 
ATOM   6634  C  CG  . LEU B  1 271 ? 19.093  34.311  44.252  1.00 20.03 ? 288  LEU B CG  1 
ATOM   6635  C  CD1 . LEU B  1 271 ? 19.535  35.517  45.065  1.00 20.76 ? 288  LEU B CD1 1 
ATOM   6636  C  CD2 . LEU B  1 271 ? 18.609  34.753  42.888  1.00 21.63 ? 288  LEU B CD2 1 
ATOM   6637  N  N   . ALA B  1 272 ? 19.062  30.887  45.888  1.00 20.64 ? 289  ALA B N   1 
ATOM   6638  C  CA  . ALA B  1 272 ? 17.930  30.273  46.575  1.00 20.58 ? 289  ALA B CA  1 
ATOM   6639  C  C   . ALA B  1 272 ? 18.212  30.157  48.075  1.00 21.53 ? 289  ALA B C   1 
ATOM   6640  O  O   . ALA B  1 272 ? 17.353  30.466  48.897  1.00 22.87 ? 289  ALA B O   1 
ATOM   6641  C  CB  . ALA B  1 272 ? 17.613  28.926  45.966  1.00 20.25 ? 289  ALA B CB  1 
ATOM   6642  N  N   . GLY B  1 273 ? 19.423  29.709  48.421  1.00 20.84 ? 290  GLY B N   1 
ATOM   6643  C  CA  . GLY B  1 273 ? 19.870  29.645  49.804  1.00 21.81 ? 290  GLY B CA  1 
ATOM   6644  C  C   . GLY B  1 273 ? 19.804  31.000  50.512  1.00 22.05 ? 290  GLY B C   1 
ATOM   6645  O  O   . GLY B  1 273 ? 19.394  31.069  51.670  1.00 23.18 ? 290  GLY B O   1 
ATOM   6646  N  N   . LEU B  1 274 ? 20.231  32.064  49.819  1.00 21.96 ? 291  LEU B N   1 
ATOM   6647  C  CA  . LEU B  1 274 ? 20.263  33.405  50.385  1.00 22.91 ? 291  LEU B CA  1 
ATOM   6648  C  C   . LEU B  1 274 ? 18.844  33.928  50.589  1.00 23.82 ? 291  LEU B C   1 
ATOM   6649  O  O   . LEU B  1 274 ? 18.579  34.615  51.574  1.00 25.16 ? 291  LEU B O   1 
ATOM   6650  C  CB  . LEU B  1 274 ? 21.066  34.361  49.505  1.00 22.76 ? 291  LEU B CB  1 
ATOM   6651  C  CG  . LEU B  1 274 ? 22.557  34.038  49.360  1.00 23.36 ? 291  LEU B CG  1 
ATOM   6652  C  CD1 . LEU B  1 274 ? 23.182  35.003  48.367  1.00 24.04 ? 291  LEU B CD1 1 
ATOM   6653  C  CD2 . LEU B  1 274 ? 23.281  34.084  50.695  1.00 23.76 ? 291  LEU B CD2 1 
ATOM   6654  N  N   . LEU B  1 275 ? 17.953  33.613  49.646  1.00 22.97 ? 292  LEU B N   1 
ATOM   6655  C  CA  . LEU B  1 275 ? 16.564  34.030  49.733  1.00 24.63 ? 292  LEU B CA  1 
ATOM   6656  C  C   . LEU B  1 275 ? 15.896  33.356  50.929  1.00 23.80 ? 292  LEU B C   1 
ATOM   6657  O  O   . LEU B  1 275 ? 15.068  33.971  51.595  1.00 24.74 ? 292  LEU B O   1 
ATOM   6658  C  CB  . LEU B  1 275 ? 15.831  33.731  48.423  1.00 24.83 ? 292  LEU B CB  1 
ATOM   6659  C  CG  . LEU B  1 275 ? 16.197  34.620  47.229  1.00 25.32 ? 292  LEU B CG  1 
ATOM   6660  C  CD1 . LEU B  1 275 ? 15.543  34.112  45.945  1.00 25.59 ? 292  LEU B CD1 1 
ATOM   6661  C  CD2 . LEU B  1 275 ? 15.812  36.070  47.466  1.00 25.63 ? 292  LEU B CD2 1 
ATOM   6662  N  N   . ALA B  1 276 ? 16.286  32.108  51.206  1.00 24.20 ? 293  ALA B N   1 
ATOM   6663  C  CA  . ALA B  1 276 ? 15.755  31.358  52.333  1.00 25.11 ? 293  ALA B CA  1 
ATOM   6664  C  C   . ALA B  1 276 ? 16.250  31.960  53.647  1.00 27.43 ? 293  ALA B C   1 
ATOM   6665  O  O   . ALA B  1 276 ? 15.484  32.078  54.602  1.00 27.78 ? 293  ALA B O   1 
ATOM   6666  C  CB  . ALA B  1 276 ? 16.129  29.901  52.213  1.00 24.97 ? 293  ALA B CB  1 
ATOM   6667  N  N   . ALA B  1 277 ? 17.529  32.359  53.683  1.00 27.89 ? 294  ALA B N   1 
ATOM   6668  C  CA  . ALA B  1 277 ? 18.105  32.965  54.874  1.00 27.56 ? 294  ALA B CA  1 
ATOM   6669  C  C   . ALA B  1 277 ? 17.390  34.273  55.194  1.00 28.45 ? 294  ALA B C   1 
ATOM   6670  O  O   . ALA B  1 277 ? 17.190  34.592  56.362  1.00 29.35 ? 294  ALA B O   1 
ATOM   6671  C  CB  . ALA B  1 277 ? 19.595  33.178  54.696  1.00 27.07 ? 294  ALA B CB  1 
ATOM   6672  N  N   . GLN B  1 278 ? 17.026  35.023  54.146  1.00 29.39 ? 295  GLN B N   1 
ATOM   6673  C  CA  . GLN B  1 278 ? 16.341  36.298  54.289  1.00 31.74 ? 295  GLN B CA  1 
ATOM   6674  C  C   . GLN B  1 278 ? 14.916  36.092  54.804  1.00 34.32 ? 295  GLN B C   1 
ATOM   6675  O  O   . GLN B  1 278 ? 14.383  36.968  55.483  1.00 34.48 ? 295  GLN B O   1 
ATOM   6676  C  CB  . GLN B  1 278 ? 16.373  37.055  52.960  1.00 32.81 ? 295  GLN B CB  1 
ATOM   6677  C  CG  . GLN B  1 278 ? 15.484  38.294  52.894  1.00 34.90 ? 295  GLN B CG  1 
ATOM   6678  C  CD  . GLN B  1 278 ? 15.881  39.397  53.854  1.00 37.06 ? 295  GLN B CD  1 
ATOM   6679  O  OE1 . GLN B  1 278 ? 16.863  39.301  54.598  1.00 37.36 ? 295  GLN B OE1 1 
ATOM   6680  N  NE2 . GLN B  1 278 ? 15.118  40.481  53.831  1.00 39.32 ? 295  GLN B NE2 1 
ATOM   6681  N  N   . LYS B  1 279 ? 14.293  34.955  54.470  1.00 35.70 ? 296  LYS B N   1 
ATOM   6682  C  CA  . LYS B  1 279 ? 12.967  34.646  54.986  1.00 39.95 ? 296  LYS B CA  1 
ATOM   6683  C  C   . LYS B  1 279 ? 13.025  34.453  56.501  1.00 42.18 ? 296  LYS B C   1 
ATOM   6684  O  O   . LYS B  1 279 ? 12.098  34.846  57.204  1.00 45.18 ? 296  LYS B O   1 
ATOM   6685  C  CB  . LYS B  1 279 ? 12.326  33.417  54.331  1.00 42.43 ? 296  LYS B CB  1 
ATOM   6686  C  CG  . LYS B  1 279 ? 11.590  33.681  53.024  1.00 45.30 ? 296  LYS B CG  1 
ATOM   6687  C  CD  . LYS B  1 279 ? 10.779  32.493  52.519  1.00 47.03 ? 296  LYS B CD  1 
ATOM   6688  C  CE  . LYS B  1 279 ? 9.543   32.207  53.321  1.00 49.93 ? 296  LYS B CE  1 
ATOM   6689  N  NZ  . LYS B  1 279 ? 8.487   33.199  53.105  1.00 51.69 ? 296  LYS B NZ  1 
ATOM   6690  N  N   . VAL B  1 280 ? 14.114  33.854  56.996  1.00 43.33 ? 297  VAL B N   1 
ATOM   6691  C  CA  . VAL B  1 280 ? 14.300  33.645  58.425  1.00 45.10 ? 297  VAL B CA  1 
ATOM   6692  C  C   . VAL B  1 280 ? 14.668  34.970  59.098  1.00 45.48 ? 297  VAL B C   1 
ATOM   6693  O  O   . VAL B  1 280 ? 14.165  35.275  60.177  1.00 47.81 ? 297  VAL B O   1 
ATOM   6694  C  CB  . VAL B  1 280 ? 15.364  32.564  58.706  1.00 46.62 ? 297  VAL B CB  1 
ATOM   6695  C  CG1 . VAL B  1 280 ? 15.556  32.331  60.201  1.00 47.77 ? 297  VAL B CG1 1 
ATOM   6696  C  CG2 . VAL B  1 280 ? 15.047  31.244  58.010  1.00 45.71 ? 297  VAL B CG2 1 
ATOM   6697  N  N   . ILE B  1 281 ? 15.537  35.760  58.454  1.00 44.79 ? 298  ILE B N   1 
ATOM   6698  C  CA  . ILE B  1 281 ? 16.199  36.884  59.102  1.00 46.75 ? 298  ILE B CA  1 
ATOM   6699  C  C   . ILE B  1 281 ? 15.364  38.159  58.965  1.00 45.56 ? 298  ILE B C   1 
ATOM   6700  O  O   . ILE B  1 281 ? 15.293  38.948  59.906  1.00 43.64 ? 298  ILE B O   1 
ATOM   6701  C  CB  . ILE B  1 281 ? 17.629  37.053  58.547  1.00 46.29 ? 298  ILE B CB  1 
ATOM   6702  C  CG1 . ILE B  1 281 ? 18.533  35.912  59.020  1.00 47.17 ? 298  ILE B CG1 1 
ATOM   6703  C  CG2 . ILE B  1 281 ? 18.217  38.419  58.910  1.00 47.54 ? 298  ILE B CG2 1 
ATOM   6704  C  CD1 . ILE B  1 281 ? 19.927  35.923  58.417  1.00 48.47 ? 298  ILE B CD1 1 
ATOM   6705  N  N   . SER B  1 282 ? 14.779  38.378  57.780  1.00 45.17 ? 299  SER B N   1 
ATOM   6706  C  CA  . SER B  1 282 ? 13.943  39.539  57.515  1.00 46.39 ? 299  SER B CA  1 
ATOM   6707  C  C   . SER B  1 282 ? 14.720  40.831  57.761  1.00 48.39 ? 299  SER B C   1 
ATOM   6708  O  O   . SER B  1 282 ? 14.233  41.728  58.447  1.00 49.66 ? 299  SER B O   1 
ATOM   6709  C  CB  . SER B  1 282 ? 12.671  39.507  58.334  1.00 47.03 ? 299  SER B CB  1 
ATOM   6710  O  OG  . SER B  1 282 ? 11.941  38.310  58.104  1.00 48.62 ? 299  SER B OG  1 
ATOM   6711  N  N   . LYS B  1 283 ? 15.926  40.917  57.189  1.00 47.89 ? 300  LYS B N   1 
ATOM   6712  C  CA  . LYS B  1 283 ? 16.729  42.127  57.269  1.00 50.96 ? 300  LYS B CA  1 
ATOM   6713  C  C   . LYS B  1 283 ? 16.373  43.027  56.088  1.00 52.78 ? 300  LYS B C   1 
ATOM   6714  O  O   . LYS B  1 283 ? 16.329  42.559  54.952  1.00 49.11 ? 300  LYS B O   1 
ATOM   6715  C  CB  . LYS B  1 283 ? 18.222  41.772  57.319  1.00 52.71 ? 300  LYS B CB  1 
ATOM   6716  C  CG  . LYS B  1 283 ? 19.185  42.900  56.958  1.00 54.19 ? 300  LYS B CG  1 
ATOM   6717  C  CD  . LYS B  1 283 ? 20.643  42.626  57.311  1.00 55.89 ? 300  LYS B CD  1 
ATOM   6718  C  CE  . LYS B  1 283 ? 21.009  43.142  58.670  1.00 57.64 ? 300  LYS B CE  1 
ATOM   6719  N  NZ  . LYS B  1 283 ? 22.223  42.508  59.186  1.00 58.88 ? 300  LYS B NZ  1 
ATOM   6720  N  N   . PRO B  1 284 ? 16.100  44.337  56.309  1.00 56.79 ? 301  PRO B N   1 
ATOM   6721  C  CA  . PRO B  1 284 ? 15.834  45.265  55.207  1.00 57.70 ? 301  PRO B CA  1 
ATOM   6722  C  C   . PRO B  1 284 ? 16.862  45.111  54.086  1.00 60.30 ? 301  PRO B C   1 
ATOM   6723  O  O   . PRO B  1 284 ? 18.064  45.152  54.339  1.00 59.65 ? 301  PRO B O   1 
ATOM   6724  C  CB  . PRO B  1 284 ? 15.902  46.650  55.882  1.00 57.68 ? 301  PRO B CB  1 
ATOM   6725  C  CG  . PRO B  1 284 ? 15.506  46.385  57.319  1.00 57.15 ? 301  PRO B CG  1 
ATOM   6726  C  CD  . PRO B  1 284 ? 16.025  44.988  57.628  1.00 57.12 ? 301  PRO B CD  1 
ATOM   6727  N  N   . ILE B  1 285 ? 16.372  44.966  52.848  1.00 60.92 ? 302  ILE B N   1 
ATOM   6728  C  CA  . ILE B  1 285 ? 17.202  44.612  51.706  1.00 63.36 ? 302  ILE B CA  1 
ATOM   6729  C  C   . ILE B  1 285 ? 18.311  45.651  51.524  1.00 61.69 ? 302  ILE B C   1 
ATOM   6730  O  O   . ILE B  1 285 ? 19.364  45.335  50.973  1.00 61.93 ? 302  ILE B O   1 
ATOM   6731  C  CB  . ILE B  1 285 ? 16.340  44.445  50.436  1.00 66.25 ? 302  ILE B CB  1 
ATOM   6732  C  CG1 . ILE B  1 285 ? 15.304  43.322  50.602  1.00 68.77 ? 302  ILE B CG1 1 
ATOM   6733  C  CG2 . ILE B  1 285 ? 17.208  44.214  49.196  1.00 66.73 ? 302  ILE B CG2 1 
ATOM   6734  C  CD1 . ILE B  1 285 ? 14.163  43.368  49.600  1.00 69.26 ? 302  ILE B CD1 1 
ATOM   6735  N  N   . SER B  1 286 ? 18.078  46.881  52.001  1.00 60.89 ? 303  SER B N   1 
ATOM   6736  C  CA  . SER B  1 286 ? 19.058  47.952  51.890  1.00 62.70 ? 303  SER B CA  1 
ATOM   6737  C  C   . SER B  1 286 ? 20.182  47.813  52.919  1.00 58.33 ? 303  SER B C   1 
ATOM   6738  O  O   . SER B  1 286 ? 21.211  48.467  52.774  1.00 59.75 ? 303  SER B O   1 
ATOM   6739  C  CB  . SER B  1 286 ? 18.405  49.314  51.983  1.00 65.32 ? 303  SER B CB  1 
ATOM   6740  O  OG  . SER B  1 286 ? 17.947  49.741  50.707  1.00 66.14 ? 303  SER B OG  1 
ATOM   6741  N  N   . GLU B  1 287 ? 19.988  46.979  53.951  1.00 57.26 ? 304  GLU B N   1 
ATOM   6742  C  CA  . GLU B  1 287 ? 21.003  46.774  54.977  1.00 56.47 ? 304  GLU B CA  1 
ATOM   6743  C  C   . GLU B  1 287 ? 21.932  45.607  54.631  1.00 50.02 ? 304  GLU B C   1 
ATOM   6744  O  O   . GLU B  1 287 ? 22.929  45.401  55.319  1.00 48.13 ? 304  GLU B O   1 
ATOM   6745  C  CB  . GLU B  1 287 ? 20.384  46.538  56.356  1.00 60.02 ? 304  GLU B CB  1 
ATOM   6746  C  CG  . GLU B  1 287 ? 19.971  47.822  57.070  1.00 64.95 ? 304  GLU B CG  1 
ATOM   6747  C  CD  . GLU B  1 287 ? 19.572  47.594  58.517  1.00 70.00 ? 304  GLU B CD  1 
ATOM   6748  O  OE1 . GLU B  1 287 ? 18.582  46.869  58.744  1.00 73.74 ? 304  GLU B OE1 1 
ATOM   6749  O  OE2 . GLU B  1 287 ? 20.256  48.129  59.416  1.00 74.25 ? 304  GLU B OE2 1 
ATOM   6750  N  N   . HIS B  1 288 ? 21.608  44.840  53.580  1.00 44.64 ? 305  HIS B N   1 
ATOM   6751  C  CA  . HIS B  1 288 ? 22.443  43.718  53.175  1.00 40.08 ? 305  HIS B CA  1 
ATOM   6752  C  C   . HIS B  1 288 ? 23.792  44.233  52.682  1.00 33.43 ? 305  HIS B C   1 
ATOM   6753  O  O   . HIS B  1 288 ? 23.856  45.220  51.957  1.00 30.16 ? 305  HIS B O   1 
ATOM   6754  C  CB  . HIS B  1 288 ? 21.785  42.887  52.067  1.00 42.45 ? 305  HIS B CB  1 
ATOM   6755  C  CG  . HIS B  1 288 ? 20.597  42.098  52.503  1.00 46.50 ? 305  HIS B CG  1 
ATOM   6756  N  ND1 . HIS B  1 288 ? 20.351  40.819  52.053  1.00 49.52 ? 305  HIS B ND1 1 
ATOM   6757  C  CD2 . HIS B  1 288 ? 19.595  42.395  53.339  1.00 47.57 ? 305  HIS B CD2 1 
ATOM   6758  C  CE1 . HIS B  1 288 ? 19.231  40.370  52.603  1.00 50.89 ? 305  HIS B CE1 1 
ATOM   6759  N  NE2 . HIS B  1 288 ? 18.754  41.313  53.387  1.00 49.04 ? 305  HIS B NE2 1 
ATOM   6760  N  N   . LYS B  1 289 ? 24.868  43.556  53.098  1.00 31.08 ? 306  LYS B N   1 
ATOM   6761  C  CA  . LYS B  1 289 ? 26.179  43.773  52.508  1.00 29.31 ? 306  LYS B CA  1 
ATOM   6762  C  C   . LYS B  1 289 ? 26.870  42.418  52.378  1.00 25.54 ? 306  LYS B C   1 
ATOM   6763  O  O   . LYS B  1 289 ? 27.039  41.708  53.364  1.00 24.11 ? 306  LYS B O   1 
ATOM   6764  C  CB  . LYS B  1 289 ? 27.013  44.787  53.299  1.00 30.46 ? 306  LYS B CB  1 
ATOM   6765  C  CG  . LYS B  1 289 ? 28.299  45.190  52.580  1.00 32.70 ? 306  LYS B CG  1 
ATOM   6766  C  CD  . LYS B  1 289 ? 29.233  46.105  53.358  1.00 35.04 ? 306  LYS B CD  1 
ATOM   6767  C  CE  . LYS B  1 289 ? 28.657  47.449  53.649  1.00 37.02 ? 306  LYS B CE  1 
ATOM   6768  N  NZ  . LYS B  1 289 ? 29.661  48.277  54.325  1.00 38.18 ? 306  LYS B NZ  1 
ATOM   6769  N  N   . ILE B  1 290 ? 27.231  42.062  51.141  1.00 23.82 ? 307  ILE B N   1 
ATOM   6770  C  CA  . ILE B  1 290 ? 27.728  40.733  50.825  1.00 22.95 ? 307  ILE B CA  1 
ATOM   6771  C  C   . ILE B  1 290 ? 29.206  40.844  50.454  1.00 21.54 ? 307  ILE B C   1 
ATOM   6772  O  O   . ILE B  1 290 ? 29.563  41.662  49.610  1.00 21.66 ? 307  ILE B O   1 
ATOM   6773  C  CB  . ILE B  1 290 ? 26.886  40.108  49.695  1.00 23.80 ? 307  ILE B CB  1 
ATOM   6774  C  CG1 . ILE B  1 290 ? 25.388  40.099  50.060  1.00 24.64 ? 307  ILE B CG1 1 
ATOM   6775  C  CG2 . ILE B  1 290 ? 27.391  38.710  49.344  1.00 23.71 ? 307  ILE B CG2 1 
ATOM   6776  C  CD1 . ILE B  1 290 ? 24.470  39.732  48.913  1.00 26.32 ? 307  ILE B CD1 1 
ATOM   6777  N  N   . LEU B  1 291 ? 30.038  39.988  51.062  1.00 20.35 ? 308  LEU B N   1 
ATOM   6778  C  CA  . LEU B  1 291 ? 31.472  39.972  50.813  1.00 20.25 ? 308  LEU B CA  1 
ATOM   6779  C  C   . LEU B  1 291 ? 31.875  38.581  50.330  1.00 19.43 ? 308  LEU B C   1 
ATOM   6780  O  O   . LEU B  1 291 ? 31.697  37.596  51.046  1.00 19.22 ? 308  LEU B O   1 
ATOM   6781  C  CB  . LEU B  1 291 ? 32.230  40.378  52.079  1.00 20.21 ? 308  LEU B CB  1 
ATOM   6782  C  CG  . LEU B  1 291 ? 33.758  40.221  52.049  1.00 20.68 ? 308  LEU B CG  1 
ATOM   6783  C  CD1 . LEU B  1 291 ? 34.395  41.054  50.950  1.00 20.91 ? 308  LEU B CD1 1 
ATOM   6784  C  CD2 . LEU B  1 291 ? 34.360  40.586  53.405  1.00 21.21 ? 308  LEU B CD2 1 
ATOM   6785  N  N   . PHE B  1 292 ? 32.407  38.523  49.104  1.00 19.53 ? 309  PHE B N   1 
ATOM   6786  C  CA  . PHE B  1 292 ? 32.892  37.289  48.508  1.00 19.60 ? 309  PHE B CA  1 
ATOM   6787  C  C   . PHE B  1 292 ? 34.372  37.104  48.830  1.00 19.75 ? 309  PHE B C   1 
ATOM   6788  O  O   . PHE B  1 292 ? 35.156  38.049  48.706  1.00 19.79 ? 309  PHE B O   1 
ATOM   6789  C  CB  . PHE B  1 292 ? 32.750  37.281  46.980  1.00 19.48 ? 309  PHE B CB  1 
ATOM   6790  C  CG  . PHE B  1 292 ? 31.336  37.062  46.460  1.00 19.40 ? 309  PHE B CG  1 
ATOM   6791  C  CD1 . PHE B  1 292 ? 30.454  38.129  46.299  1.00 20.23 ? 309  PHE B CD1 1 
ATOM   6792  C  CD2 . PHE B  1 292 ? 30.893  35.785  46.132  1.00 19.50 ? 309  PHE B CD2 1 
ATOM   6793  C  CE1 . PHE B  1 292 ? 29.162  37.915  45.830  1.00 20.23 ? 309  PHE B CE1 1 
ATOM   6794  C  CE2 . PHE B  1 292 ? 29.603  35.576  45.666  1.00 19.50 ? 309  PHE B CE2 1 
ATOM   6795  C  CZ  . PHE B  1 292 ? 28.739  36.639  45.520  1.00 19.59 ? 309  PHE B CZ  1 
ATOM   6796  N  N   . LEU B  1 293 ? 34.727  35.876  49.229  1.00 19.01 ? 310  LEU B N   1 
ATOM   6797  C  CA  . LEU B  1 293 ? 36.098  35.396  49.161  1.00 19.74 ? 310  LEU B CA  1 
ATOM   6798  C  C   . LEU B  1 293 ? 36.283  34.695  47.814  1.00 19.41 ? 310  LEU B C   1 
ATOM   6799  O  O   . LEU B  1 293 ? 35.790  33.591  47.613  1.00 19.82 ? 310  LEU B O   1 
ATOM   6800  C  CB  . LEU B  1 293 ? 36.419  34.454  50.316  1.00 19.75 ? 310  LEU B CB  1 
ATOM   6801  C  CG  . LEU B  1 293 ? 37.839  33.873  50.310  1.00 21.53 ? 310  LEU B CG  1 
ATOM   6802  C  CD1 . LEU B  1 293 ? 38.854  34.879  50.823  1.00 21.62 ? 310  LEU B CD1 1 
ATOM   6803  C  CD2 . LEU B  1 293 ? 37.910  32.590  51.113  1.00 22.43 ? 310  LEU B CD2 1 
ATOM   6804  N  N   . GLY B  1 294 ? 36.988  35.355  46.893  1.00 19.43 ? 311  GLY B N   1 
ATOM   6805  C  CA  . GLY B  1 294 ? 37.023  34.940  45.501  1.00 19.33 ? 311  GLY B CA  1 
ATOM   6806  C  C   . GLY B  1 294 ? 36.350  35.981  44.612  1.00 19.85 ? 311  GLY B C   1 
ATOM   6807  O  O   . GLY B  1 294 ? 35.393  36.630  45.039  1.00 20.03 ? 311  GLY B O   1 
ATOM   6808  N  N   . ALA B  1 295 ? 36.886  36.139  43.394  1.00 19.32 ? 312  ALA B N   1 
ATOM   6809  C  CA  . ALA B  1 295 ? 36.339  37.053  42.402  1.00 19.72 ? 312  ALA B CA  1 
ATOM   6810  C  C   . ALA B  1 295 ? 36.369  36.407  41.020  1.00 19.94 ? 312  ALA B C   1 
ATOM   6811  O  O   . ALA B  1 295 ? 36.501  37.096  40.008  1.00 20.74 ? 312  ALA B O   1 
ATOM   6812  C  CB  . ALA B  1 295 ? 37.103  38.360  42.417  1.00 19.57 ? 312  ALA B CB  1 
ATOM   6813  N  N   . GLY B  1 296 ? 36.199  35.083  40.988  1.00 20.03 ? 313  GLY B N   1 
ATOM   6814  C  CA  . GLY B  1 296 ? 36.320  34.319  39.760  1.00 20.72 ? 313  GLY B CA  1 
ATOM   6815  C  C   . GLY B  1 296 ? 34.958  34.026  39.147  1.00 21.37 ? 313  GLY B C   1 
ATOM   6816  O  O   . GLY B  1 296 ? 34.000  34.777  39.346  1.00 20.32 ? 313  GLY B O   1 
ATOM   6817  N  N   . GLU B  1 297 ? 34.897  32.906  38.421  1.00 22.72 ? 314  GLU B N   1 
ATOM   6818  C  CA  . GLU B  1 297 ? 33.715  32.505  37.678  1.00 24.35 ? 314  GLU B CA  1 
ATOM   6819  C  C   . GLU B  1 297 ? 32.504  32.383  38.604  1.00 22.69 ? 314  GLU B C   1 
ATOM   6820  O  O   . GLU B  1 297 ? 31.434  32.908  38.300  1.00 21.67 ? 314  GLU B O   1 
ATOM   6821  C  CB  . GLU B  1 297 ? 34.014  31.180  36.972  1.00 26.32 ? 314  GLU B CB  1 
ATOM   6822  C  CG  . GLU B  1 297 ? 32.796  30.560  36.294  1.00 28.78 ? 314  GLU B CG  1 
ATOM   6823  C  CD  . GLU B  1 297 ? 33.076  29.209  35.661  1.00 31.76 ? 314  GLU B CD  1 
ATOM   6824  O  OE1 . GLU B  1 297 ? 33.754  29.182  34.613  1.00 32.97 ? 314  GLU B OE1 1 
ATOM   6825  O  OE2 . GLU B  1 297 ? 32.626  28.190  36.231  1.00 33.59 ? 314  GLU B OE2 1 
ATOM   6826  N  N   . ALA B  1 298 ? 32.669  31.660  39.716  1.00 21.80 ? 315  ALA B N   1 
ATOM   6827  C  CA  . ALA B  1 298 ? 31.562  31.407  40.627  1.00 21.95 ? 315  ALA B CA  1 
ATOM   6828  C  C   . ALA B  1 298 ? 31.093  32.708  41.274  1.00 21.39 ? 315  ALA B C   1 
ATOM   6829  O  O   . ALA B  1 298 ? 29.892  32.966  41.340  1.00 22.02 ? 315  ALA B O   1 
ATOM   6830  C  CB  . ALA B  1 298 ? 31.959  30.391  41.668  1.00 22.02 ? 315  ALA B CB  1 
ATOM   6831  N  N   . ALA B  1 299 ? 32.043  33.523  41.749  1.00 20.88 ? 316  ALA B N   1 
ATOM   6832  C  CA  . ALA B  1 299 ? 31.709  34.785  42.391  1.00 20.55 ? 316  ALA B CA  1 
ATOM   6833  C  C   . ALA B  1 299 ? 30.890  35.672  41.457  1.00 20.59 ? 316  ALA B C   1 
ATOM   6834  O  O   . ALA B  1 299 ? 29.865  36.220  41.864  1.00 19.34 ? 316  ALA B O   1 
ATOM   6835  C  CB  . ALA B  1 299 ? 32.965  35.483  42.848  1.00 21.52 ? 316  ALA B CB  1 
ATOM   6836  N  N   . LEU B  1 300 ? 31.352  35.816  40.209  1.00 20.54 ? 317  LEU B N   1 
ATOM   6837  C  CA  . LEU B  1 300 ? 30.694  36.693  39.249  1.00 22.18 ? 317  LEU B CA  1 
ATOM   6838  C  C   . LEU B  1 300 ? 29.316  36.151  38.873  1.00 21.03 ? 317  LEU B C   1 
ATOM   6839  O  O   . LEU B  1 300 ? 28.368  36.920  38.706  1.00 21.00 ? 317  LEU B O   1 
ATOM   6840  C  CB  . LEU B  1 300 ? 31.578  36.881  38.019  1.00 23.27 ? 317  LEU B CB  1 
ATOM   6841  C  CG  . LEU B  1 300 ? 32.887  37.643  38.253  1.00 24.75 ? 317  LEU B CG  1 
ATOM   6842  C  CD1 . LEU B  1 300 ? 33.702  37.674  36.968  1.00 26.48 ? 317  LEU B CD1 1 
ATOM   6843  C  CD2 . LEU B  1 300 ? 32.654  39.048  38.775  1.00 25.35 ? 317  LEU B CD2 1 
ATOM   6844  N  N   . GLY B  1 301 ? 29.213  34.831  38.710  1.00 20.38 ? 318  GLY B N   1 
ATOM   6845  C  CA  . GLY B  1 301 ? 27.940  34.216  38.384  1.00 20.02 ? 318  GLY B CA  1 
ATOM   6846  C  C   . GLY B  1 301 ? 26.901  34.484  39.471  1.00 19.75 ? 318  GLY B C   1 
ATOM   6847  O  O   . GLY B  1 301 ? 25.800  34.939  39.175  1.00 19.48 ? 318  GLY B O   1 
ATOM   6848  N  N   . ILE B  1 302 ? 27.284  34.229  40.729  1.00 19.40 ? 319  ILE B N   1 
ATOM   6849  C  CA  . ILE B  1 302 ? 26.390  34.381  41.865  1.00 19.88 ? 319  ILE B CA  1 
ATOM   6850  C  C   . ILE B  1 302 ? 26.038  35.858  42.027  1.00 20.38 ? 319  ILE B C   1 
ATOM   6851  O  O   . ILE B  1 302 ? 24.867  36.204  42.179  1.00 19.81 ? 319  ILE B O   1 
ATOM   6852  C  CB  . ILE B  1 302 ? 27.016  33.778  43.137  1.00 19.49 ? 319  ILE B CB  1 
ATOM   6853  C  CG1 . ILE B  1 302 ? 27.242  32.269  42.980  1.00 19.77 ? 319  ILE B CG1 1 
ATOM   6854  C  CG2 . ILE B  1 302 ? 26.161  34.088  44.367  1.00 19.53 ? 319  ILE B CG2 1 
ATOM   6855  C  CD1 . ILE B  1 302 ? 28.141  31.637  44.027  1.00 20.12 ? 319  ILE B CD1 1 
ATOM   6856  N  N   . ALA B  1 303 ? 27.058  36.728  41.964  1.00 20.30 ? 320  ALA B N   1 
ATOM   6857  C  CA  . ALA B  1 303 ? 26.868  38.146  42.217  1.00 20.35 ? 320  ALA B CA  1 
ATOM   6858  C  C   . ALA B  1 303 ? 25.869  38.742  41.224  1.00 20.63 ? 320  ALA B C   1 
ATOM   6859  O  O   . ALA B  1 303 ? 24.996  39.521  41.608  1.00 20.11 ? 320  ALA B O   1 
ATOM   6860  C  CB  . ALA B  1 303 ? 28.202  38.865  42.172  1.00 20.13 ? 320  ALA B CB  1 
ATOM   6861  N  N   . ASN B  1 304 ? 25.990  38.365  39.949  1.00 21.24 ? 321  ASN B N   1 
ATOM   6862  C  CA  . ASN B  1 304 ? 25.135  38.919  38.907  1.00 23.08 ? 321  ASN B CA  1 
ATOM   6863  C  C   . ASN B  1 304 ? 23.669  38.542  39.139  1.00 21.69 ? 321  ASN B C   1 
ATOM   6864  O  O   . ASN B  1 304 ? 22.784  39.348  38.860  1.00 20.42 ? 321  ASN B O   1 
ATOM   6865  C  CB  . ASN B  1 304 ? 25.656  38.571  37.515  1.00 25.68 ? 321  ASN B CB  1 
ATOM   6866  C  CG  . ASN B  1 304 ? 26.796  39.481  37.105  1.00 29.02 ? 321  ASN B CG  1 
ATOM   6867  O  OD1 . ASN B  1 304 ? 26.651  40.711  37.112  1.00 31.55 ? 321  ASN B OD1 1 
ATOM   6868  N  ND2 . ASN B  1 304 ? 27.939  38.915  36.745  1.00 32.14 ? 321  ASN B ND2 1 
ATOM   6869  N  N   . LEU B  1 305 ? 23.405  37.350  39.682  1.00 21.80 ? 322  LEU B N   1 
ATOM   6870  C  CA  . LEU B  1 305 ? 22.031  36.924  39.929  1.00 23.62 ? 322  LEU B CA  1 
ATOM   6871  C  C   . LEU B  1 305 ? 21.463  37.592  41.188  1.00 23.37 ? 322  LEU B C   1 
ATOM   6872  O  O   . LEU B  1 305 ? 20.269  37.906  41.241  1.00 22.26 ? 322  LEU B O   1 
ATOM   6873  C  CB  . LEU B  1 305 ? 21.949  35.401  40.010  1.00 24.26 ? 322  LEU B CB  1 
ATOM   6874  C  CG  . LEU B  1 305 ? 20.594  34.790  39.642  1.00 24.84 ? 322  LEU B CG  1 
ATOM   6875  C  CD1 . LEU B  1 305 ? 20.199  35.082  38.197  1.00 25.05 ? 322  LEU B CD1 1 
ATOM   6876  C  CD2 . LEU B  1 305 ? 20.622  33.294  39.889  1.00 25.29 ? 322  LEU B CD2 1 
ATOM   6877  N  N   . ILE B  1 306 ? 22.316  37.823  42.195  1.00 21.66 ? 323  ILE B N   1 
ATOM   6878  C  CA  . ILE B  1 306 ? 21.914  38.569  43.381  1.00 22.09 ? 323  ILE B CA  1 
ATOM   6879  C  C   . ILE B  1 306 ? 21.442  39.956  42.953  1.00 22.27 ? 323  ILE B C   1 
ATOM   6880  O  O   . ILE B  1 306 ? 20.406  40.441  43.419  1.00 20.55 ? 323  ILE B O   1 
ATOM   6881  C  CB  . ILE B  1 306 ? 23.052  38.638  44.421  1.00 22.09 ? 323  ILE B CB  1 
ATOM   6882  C  CG1 . ILE B  1 306 ? 23.325  37.265  45.051  1.00 22.36 ? 323  ILE B CG1 1 
ATOM   6883  C  CG2 . ILE B  1 306 ? 22.761  39.698  45.487  1.00 22.19 ? 323  ILE B CG2 1 
ATOM   6884  C  CD1 . ILE B  1 306 ? 24.568  37.204  45.926  1.00 23.08 ? 323  ILE B CD1 1 
ATOM   6885  N  N   . VAL B  1 307 ? 22.209  40.588  42.059  1.00 21.64 ? 324  VAL B N   1 
ATOM   6886  C  CA  . VAL B  1 307 ? 21.891  41.927  41.590  1.00 22.38 ? 324  VAL B CA  1 
ATOM   6887  C  C   . VAL B  1 307 ? 20.537  41.927  40.880  1.00 22.72 ? 324  VAL B C   1 
ATOM   6888  O  O   . VAL B  1 307 ? 19.730  42.830  41.101  1.00 21.34 ? 324  VAL B O   1 
ATOM   6889  C  CB  . VAL B  1 307 ? 23.021  42.466  40.695  1.00 23.14 ? 324  VAL B CB  1 
ATOM   6890  C  CG1 . VAL B  1 307 ? 22.604  43.707  39.916  1.00 23.99 ? 324  VAL B CG1 1 
ATOM   6891  C  CG2 . VAL B  1 307 ? 24.279  42.748  41.509  1.00 23.55 ? 324  VAL B CG2 1 
ATOM   6892  N  N   . MET B  1 308 ? 20.289  40.918  40.032  1.00 22.76 ? 325  MET B N   1 
ATOM   6893  C  CA  . MET B  1 308 ? 19.010  40.797  39.345  1.00 23.57 ? 325  MET B CA  1 
ATOM   6894  C  C   . MET B  1 308 ? 17.868  40.682  40.355  1.00 23.13 ? 325  MET B C   1 
ATOM   6895  O  O   . MET B  1 308 ? 16.814  41.290  40.159  1.00 23.30 ? 325  MET B O   1 
ATOM   6896  C  CB  . MET B  1 308 ? 18.994  39.592  38.399  1.00 24.85 ? 325  MET B CB  1 
ATOM   6897  C  CG  . MET B  1 308 ? 19.899  39.762  37.196  1.00 26.42 ? 325  MET B CG  1 
ATOM   6898  S  SD  . MET B  1 308 ? 19.830  38.397  36.016  1.00 29.29 ? 325  MET B SD  1 
ATOM   6899  C  CE  . MET B  1 308 ? 18.112  38.439  35.481  1.00 29.53 ? 325  MET B CE  1 
ATOM   6900  N  N   . SER B  1 309 ? 18.087  39.908  41.425  1.00 22.72 ? 326  SER B N   1 
ATOM   6901  C  CA  . SER B  1 309 ? 17.110  39.755  42.495  1.00 24.96 ? 326  SER B CA  1 
ATOM   6902  C  C   . SER B  1 309 ? 16.812  41.108  43.145  1.00 25.98 ? 326  SER B C   1 
ATOM   6903  O  O   . SER B  1 309 ? 15.652  41.481  43.330  1.00 26.32 ? 326  SER B O   1 
ATOM   6904  C  CB  . SER B  1 309 ? 17.585  38.748  43.515  1.00 25.39 ? 326  SER B CB  1 
ATOM   6905  O  OG  . SER B  1 309 ? 16.637  38.560  44.560  1.00 26.26 ? 326  SER B OG  1 
ATOM   6906  N  N   . MET B  1 310 ? 17.875  41.855  43.454  1.00 25.23 ? 327  MET B N   1 
ATOM   6907  C  CA  . MET B  1 310 ? 17.758  43.136  44.132  1.00 26.11 ? 327  MET B CA  1 
ATOM   6908  C  C   . MET B  1 310 ? 17.057  44.153  43.230  1.00 26.95 ? 327  MET B C   1 
ATOM   6909  O  O   . MET B  1 310 ? 16.232  44.929  43.712  1.00 29.22 ? 327  MET B O   1 
ATOM   6910  C  CB  . MET B  1 310 ? 19.139  43.648  44.563  1.00 27.03 ? 327  MET B CB  1 
ATOM   6911  C  CG  . MET B  1 310 ? 19.738  42.903  45.745  1.00 28.40 ? 327  MET B CG  1 
ATOM   6912  S  SD  . MET B  1 310 ? 21.388  43.508  46.165  1.00 29.83 ? 327  MET B SD  1 
ATOM   6913  C  CE  . MET B  1 310 ? 21.816  42.592  47.649  1.00 28.83 ? 327  MET B CE  1 
ATOM   6914  N  N   . VAL B  1 311 ? 17.365  44.128  41.926  1.00 26.49 ? 328  VAL B N   1 
ATOM   6915  C  CA  . VAL B  1 311 ? 16.776  45.054  40.971  1.00 27.91 ? 328  VAL B CA  1 
ATOM   6916  C  C   . VAL B  1 311 ? 15.273  44.789  40.847  1.00 30.31 ? 328  VAL B C   1 
ATOM   6917  O  O   . VAL B  1 311 ? 14.497  45.728  40.682  1.00 30.99 ? 328  VAL B O   1 
ATOM   6918  C  CB  . VAL B  1 311 ? 17.480  45.003  39.601  1.00 28.45 ? 328  VAL B CB  1 
ATOM   6919  C  CG1 . VAL B  1 311 ? 16.676  45.697  38.504  1.00 29.12 ? 328  VAL B CG1 1 
ATOM   6920  C  CG2 . VAL B  1 311 ? 18.887  45.591  39.662  1.00 28.32 ? 328  VAL B CG2 1 
ATOM   6921  N  N   . GLU B  1 312 ? 14.860  43.519  40.943  1.00 31.28 ? 329  GLU B N   1 
ATOM   6922  C  CA  . GLU B  1 312 ? 13.447  43.166  40.890  1.00 34.69 ? 329  GLU B CA  1 
ATOM   6923  C  C   . GLU B  1 312 ? 12.693  43.734  42.092  1.00 36.11 ? 329  GLU B C   1 
ATOM   6924  O  O   . GLU B  1 312 ? 11.486  43.960  42.005  1.00 37.23 ? 329  GLU B O   1 
ATOM   6925  C  CB  . GLU B  1 312 ? 13.197  41.656  40.849  1.00 34.68 ? 329  GLU B CB  1 
ATOM   6926  C  CG  . GLU B  1 312 ? 13.140  41.086  39.437  1.00 36.67 ? 329  GLU B CG  1 
ATOM   6927  C  CD  . GLU B  1 312 ? 12.648  39.650  39.351  1.00 37.35 ? 329  GLU B CD  1 
ATOM   6928  O  OE1 . GLU B  1 312 ? 12.456  38.977  40.391  1.00 36.34 ? 329  GLU B OE1 1 
ATOM   6929  O  OE2 . GLU B  1 312 ? 12.452  39.210  38.200  1.00 42.54 ? 329  GLU B OE2 1 
ATOM   6930  N  N   . ASN B  1 313 ? 13.398  43.943  43.211  1.00 37.29 ? 330  ASN B N   1 
ATOM   6931  C  CA  . ASN B  1 313 ? 12.783  44.461  44.424  1.00 39.16 ? 330  ASN B CA  1 
ATOM   6932  C  C   . ASN B  1 313 ? 12.883  45.985  44.502  1.00 37.97 ? 330  ASN B C   1 
ATOM   6933  O  O   . ASN B  1 313 ? 12.541  46.562  45.528  1.00 42.64 ? 330  ASN B O   1 
ATOM   6934  C  CB  . ASN B  1 313 ? 13.348  43.769  45.657  1.00 40.35 ? 330  ASN B CB  1 
ATOM   6935  C  CG  . ASN B  1 313 ? 12.840  42.354  45.758  1.00 44.40 ? 330  ASN B CG  1 
ATOM   6936  O  OD1 . ASN B  1 313 ? 11.919  42.084  46.534  1.00 47.31 ? 330  ASN B OD1 1 
ATOM   6937  N  ND2 . ASN B  1 313 ? 13.379  41.456  44.945  1.00 45.99 ? 330  ASN B ND2 1 
ATOM   6938  N  N   . GLY B  1 314 ? 13.344  46.636  43.428  1.00 37.96 ? 331  GLY B N   1 
ATOM   6939  C  CA  . GLY B  1 314 ? 13.204  48.077  43.277  1.00 38.05 ? 331  GLY B CA  1 
ATOM   6940  C  C   . GLY B  1 314 ? 14.490  48.856  43.557  1.00 38.43 ? 331  GLY B C   1 
ATOM   6941  O  O   . GLY B  1 314 ? 14.453  50.084  43.632  1.00 37.57 ? 331  GLY B O   1 
ATOM   6942  N  N   . LEU B  1 315 ? 15.621  48.151  43.705  1.00 38.49 ? 332  LEU B N   1 
ATOM   6943  C  CA  . LEU B  1 315 ? 16.923  48.795  43.770  1.00 37.24 ? 332  LEU B CA  1 
ATOM   6944  C  C   . LEU B  1 315 ? 17.408  49.039  42.345  1.00 35.20 ? 332  LEU B C   1 
ATOM   6945  O  O   . LEU B  1 315 ? 17.190  48.213  41.463  1.00 34.61 ? 332  LEU B O   1 
ATOM   6946  C  CB  . LEU B  1 315 ? 17.945  47.958  44.538  1.00 38.65 ? 332  LEU B CB  1 
ATOM   6947  C  CG  . LEU B  1 315 ? 17.762  47.854  46.054  1.00 40.86 ? 332  LEU B CG  1 
ATOM   6948  C  CD1 . LEU B  1 315 ? 16.674  46.863  46.422  1.00 43.81 ? 332  LEU B CD1 1 
ATOM   6949  C  CD2 . LEU B  1 315 ? 19.073  47.461  46.707  1.00 42.07 ? 332  LEU B CD2 1 
ATOM   6950  N  N   . SER B  1 316 ? 18.079  50.175  42.130  1.00 32.21 ? 333  SER B N   1 
ATOM   6951  C  CA  . SER B  1 316 ? 18.782  50.407  40.883  1.00 33.09 ? 333  SER B CA  1 
ATOM   6952  C  C   . SER B  1 316 ? 19.883  49.360  40.729  1.00 31.68 ? 333  SER B C   1 
ATOM   6953  O  O   . SER B  1 316 ? 20.324  48.771  41.712  1.00 30.94 ? 333  SER B O   1 
ATOM   6954  C  CB  . SER B  1 316 ? 19.354  51.797  40.835  1.00 34.96 ? 333  SER B CB  1 
ATOM   6955  O  OG  . SER B  1 316 ? 20.394  51.937  41.793  1.00 34.78 ? 333  SER B OG  1 
ATOM   6956  N  N   . GLU B  1 317 ? 20.324  49.136  39.490  1.00 32.96 ? 334  GLU B N   1 
ATOM   6957  C  CA  . GLU B  1 317 ? 21.399  48.192  39.240  1.00 35.13 ? 334  GLU B CA  1 
ATOM   6958  C  C   . GLU B  1 317 ? 22.651  48.637  39.996  1.00 34.92 ? 334  GLU B C   1 
ATOM   6959  O  O   . GLU B  1 317 ? 23.372  47.806  40.547  1.00 31.50 ? 334  GLU B O   1 
ATOM   6960  C  CB  . GLU B  1 317 ? 21.656  48.075  37.740  1.00 37.21 ? 334  GLU B CB  1 
ATOM   6961  C  CG  . GLU B  1 317 ? 22.671  46.995  37.385  1.00 38.40 ? 334  GLU B CG  1 
ATOM   6962  C  CD  . GLU B  1 317 ? 22.739  46.716  35.899  1.00 40.61 ? 334  GLU B CD  1 
ATOM   6963  O  OE1 . GLU B  1 317 ? 23.288  47.559  35.159  1.00 44.78 ? 334  GLU B OE1 1 
ATOM   6964  O  OE2 . GLU B  1 317 ? 22.224  45.659  35.486  1.00 40.27 ? 334  GLU B OE2 1 
ATOM   6965  N  N   . GLN B  1 318 ? 22.885  49.956  40.026  1.00 34.92 ? 335  GLN B N   1 
ATOM   6966  C  CA  . GLN B  1 318 ? 24.087  50.515  40.625  1.00 36.68 ? 335  GLN B CA  1 
ATOM   6967  C  C   . GLN B  1 318 ? 24.027  50.368  42.146  1.00 34.60 ? 335  GLN B C   1 
ATOM   6968  O  O   . GLN B  1 318 ? 25.009  49.966  42.769  1.00 31.99 ? 335  GLN B O   1 
ATOM   6969  C  CB  . GLN B  1 318 ? 24.274  51.964  40.172  1.00 40.84 ? 335  GLN B CB  1 
ATOM   6970  C  CG  . GLN B  1 318 ? 25.707  52.463  40.307  1.00 46.77 ? 335  GLN B CG  1 
ATOM   6971  C  CD  . GLN B  1 318 ? 25.897  53.888  39.833  1.00 52.04 ? 335  GLN B CD  1 
ATOM   6972  O  OE1 . GLN B  1 318 ? 24.940  54.661  39.702  1.00 54.71 ? 335  GLN B OE1 1 
ATOM   6973  N  NE2 . GLN B  1 318 ? 27.147  54.253  39.589  1.00 54.74 ? 335  GLN B NE2 1 
ATOM   6974  N  N   . GLU B  1 319 ? 22.868  50.679  42.741  1.00 31.68 ? 336  GLU B N   1 
ATOM   6975  C  CA  . GLU B  1 319 ? 22.673  50.505  44.174  1.00 33.13 ? 336  GLU B CA  1 
ATOM   6976  C  C   . GLU B  1 319 ? 22.927  49.051  44.575  1.00 29.37 ? 336  GLU B C   1 
ATOM   6977  O  O   . GLU B  1 319 ? 23.528  48.792  45.619  1.00 27.94 ? 336  GLU B O   1 
ATOM   6978  C  CB  . GLU B  1 319 ? 21.251  50.851  44.622  1.00 37.96 ? 336  GLU B CB  1 
ATOM   6979  C  CG  . GLU B  1 319 ? 20.973  52.346  44.745  1.00 43.34 ? 336  GLU B CG  1 
ATOM   6980  C  CD  . GLU B  1 319 ? 19.532  52.630  45.135  1.00 48.82 ? 336  GLU B CD  1 
ATOM   6981  O  OE1 . GLU B  1 319 ? 18.619  52.190  44.400  1.00 50.59 ? 336  GLU B OE1 1 
ATOM   6982  O  OE2 . GLU B  1 319 ? 19.321  53.275  46.185  1.00 53.13 ? 336  GLU B OE2 1 
ATOM   6983  N  N   . ALA B  1 320 ? 22.435  48.113  43.753  1.00 26.13 ? 337  ALA B N   1 
ATOM   6984  C  CA  . ALA B  1 320 ? 22.567  46.691  44.035  1.00 24.76 ? 337  ALA B CA  1 
ATOM   6985  C  C   . ALA B  1 320 ? 24.038  46.269  44.021  1.00 23.87 ? 337  ALA B C   1 
ATOM   6986  O  O   . ALA B  1 320 ? 24.503  45.593  44.936  1.00 23.64 ? 337  ALA B O   1 
ATOM   6987  C  CB  . ALA B  1 320 ? 21.753  45.901  43.033  1.00 24.53 ? 337  ALA B CB  1 
ATOM   6988  N  N   . GLN B  1 321 ? 24.761  46.683  42.977  1.00 24.37 ? 338  GLN B N   1 
ATOM   6989  C  CA  . GLN B  1 321 ? 26.161  46.322  42.790  1.00 25.38 ? 338  GLN B CA  1 
ATOM   6990  C  C   . GLN B  1 321 ? 27.001  46.812  43.973  1.00 27.33 ? 338  GLN B C   1 
ATOM   6991  O  O   . GLN B  1 321 ? 27.915  46.116  44.417  1.00 26.34 ? 338  GLN B O   1 
ATOM   6992  C  CB  . GLN B  1 321 ? 26.633  46.847  41.433  1.00 24.93 ? 338  GLN B CB  1 
ATOM   6993  C  CG  . GLN B  1 321 ? 26.112  46.037  40.247  1.00 24.51 ? 338  GLN B CG  1 
ATOM   6994  C  CD  . GLN B  1 321 ? 26.313  46.699  38.901  1.00 24.70 ? 338  GLN B CD  1 
ATOM   6995  O  OE1 . GLN B  1 321 ? 26.682  47.875  38.794  1.00 27.62 ? 338  GLN B OE1 1 
ATOM   6996  N  NE2 . GLN B  1 321 ? 26.049  45.948  37.842  1.00 24.62 ? 338  GLN B NE2 1 
ATOM   6997  N  N   . LYS B  1 322 ? 26.649  47.988  44.514  1.00 27.43 ? 339  LYS B N   1 
ATOM   6998  C  CA  . LYS B  1 322 ? 27.393  48.602  45.602  1.00 30.07 ? 339  LYS B CA  1 
ATOM   6999  C  C   . LYS B  1 322 ? 27.220  47.841  46.919  1.00 29.00 ? 339  LYS B C   1 
ATOM   7000  O  O   . LYS B  1 322 ? 27.925  48.130  47.877  1.00 29.01 ? 339  LYS B O   1 
ATOM   7001  C  CB  . LYS B  1 322 ? 27.005  50.080  45.745  1.00 33.70 ? 339  LYS B CB  1 
ATOM   7002  C  CG  . LYS B  1 322 ? 27.691  51.001  44.738  1.00 38.68 ? 339  LYS B CG  1 
ATOM   7003  C  CD  . LYS B  1 322 ? 27.162  52.431  44.652  1.00 43.01 ? 339  LYS B CD  1 
ATOM   7004  C  CE  . LYS B  1 322 ? 27.092  53.159  45.964  1.00 47.51 ? 339  LYS B CE  1 
ATOM   7005  N  NZ  . LYS B  1 322 ? 28.411  53.363  46.572  1.00 51.08 ? 339  LYS B NZ  1 
ATOM   7006  N  N   . LYS B  1 323 ? 26.300  46.869  46.975  1.00 27.42 ? 340  LYS B N   1 
ATOM   7007  C  CA  . LYS B  1 323 ? 26.107  46.066  48.171  1.00 27.44 ? 340  LYS B CA  1 
ATOM   7008  C  C   . LYS B  1 323 ? 26.990  44.819  48.151  1.00 26.59 ? 340  LYS B C   1 
ATOM   7009  O  O   . LYS B  1 323 ? 26.979  44.056  49.119  1.00 25.12 ? 340  LYS B O   1 
ATOM   7010  C  CB  . LYS B  1 323 ? 24.630  45.698  48.335  1.00 30.04 ? 340  LYS B CB  1 
ATOM   7011  C  CG  . LYS B  1 323 ? 23.752  46.932  48.455  1.00 33.01 ? 340  LYS B CG  1 
ATOM   7012  C  CD  . LYS B  1 323 ? 22.368  46.718  49.046  1.00 36.63 ? 340  LYS B CD  1 
ATOM   7013  C  CE  . LYS B  1 323 ? 21.658  48.029  49.167  1.00 38.79 ? 340  LYS B CE  1 
ATOM   7014  N  NZ  . LYS B  1 323 ? 22.274  48.907  50.169  1.00 40.91 ? 340  LYS B NZ  1 
ATOM   7015  N  N   . ILE B  1 324 ? 27.754  44.623  47.064  1.00 25.23 ? 341  ILE B N   1 
ATOM   7016  C  CA  . ILE B  1 324 ? 28.529  43.405  46.885  1.00 24.39 ? 341  ILE B CA  1 
ATOM   7017  C  C   . ILE B  1 324 ? 30.006  43.757  46.744  1.00 22.81 ? 341  ILE B C   1 
ATOM   7018  O  O   . ILE B  1 324 ? 30.386  44.517  45.856  1.00 23.95 ? 341  ILE B O   1 
ATOM   7019  C  CB  . ILE B  1 324 ? 28.028  42.601  45.670  1.00 25.20 ? 341  ILE B CB  1 
ATOM   7020  C  CG1 . ILE B  1 324 ? 26.571  42.171  45.846  1.00 26.34 ? 341  ILE B CG1 1 
ATOM   7021  C  CG2 . ILE B  1 324 ? 28.947  41.406  45.407  1.00 25.42 ? 341  ILE B CG2 1 
ATOM   7022  C  CD1 . ILE B  1 324 ? 25.928  41.627  44.585  1.00 26.96 ? 341  ILE B CD1 1 
ATOM   7023  N  N   . TRP B  1 325 ? 30.823  43.172  47.625  1.00 21.75 ? 342  TRP B N   1 
ATOM   7024  C  CA  . TRP B  1 325 ? 32.263  43.365  47.629  1.00 21.53 ? 342  TRP B CA  1 
ATOM   7025  C  C   . TRP B  1 325 ? 32.929  42.023  47.360  1.00 20.69 ? 342  TRP B C   1 
ATOM   7026  O  O   . TRP B  1 325 ? 32.343  40.980  47.656  1.00 19.86 ? 342  TRP B O   1 
ATOM   7027  C  CB  . TRP B  1 325 ? 32.726  43.931  48.981  1.00 22.84 ? 342  TRP B CB  1 
ATOM   7028  C  CG  . TRP B  1 325 ? 32.277  45.341  49.252  1.00 24.85 ? 342  TRP B CG  1 
ATOM   7029  C  CD1 . TRP B  1 325 ? 31.032  45.759  49.617  1.00 26.45 ? 342  TRP B CD1 1 
ATOM   7030  C  CD2 . TRP B  1 325 ? 33.096  46.526  49.193  1.00 27.20 ? 342  TRP B CD2 1 
ATOM   7031  N  NE1 . TRP B  1 325 ? 31.012  47.120  49.771  1.00 27.92 ? 342  TRP B NE1 1 
ATOM   7032  C  CE2 . TRP B  1 325 ? 32.264  47.618  49.522  1.00 28.13 ? 342  TRP B CE2 1 
ATOM   7033  C  CE3 . TRP B  1 325 ? 34.442  46.766  48.896  1.00 28.71 ? 342  TRP B CE3 1 
ATOM   7034  C  CZ2 . TRP B  1 325 ? 32.740  48.927  49.567  1.00 29.26 ? 342  TRP B CZ2 1 
ATOM   7035  C  CZ3 . TRP B  1 325 ? 34.909  48.062  48.938  1.00 29.94 ? 342  TRP B CZ3 1 
ATOM   7036  C  CH2 . TRP B  1 325 ? 34.069  49.125  49.273  1.00 29.45 ? 342  TRP B CH2 1 
ATOM   7037  N  N   . MET B  1 326 ? 34.161  42.061  46.838  1.00 20.30 ? 343  MET B N   1 
ATOM   7038  C  CA  . MET B  1 326 ? 34.898  40.840  46.561  1.00 20.33 ? 343  MET B CA  1 
ATOM   7039  C  C   . MET B  1 326 ? 36.354  40.997  46.996  1.00 20.62 ? 343  MET B C   1 
ATOM   7040  O  O   . MET B  1 326 ? 36.915  42.090  46.942  1.00 20.36 ? 343  MET B O   1 
ATOM   7041  C  CB  . MET B  1 326 ? 34.837  40.493  45.071  1.00 21.12 ? 343  MET B CB  1 
ATOM   7042  C  CG  . MET B  1 326 ? 33.431  40.338  44.523  1.00 21.08 ? 343  MET B CG  1 
ATOM   7043  S  SD  . MET B  1 326 ? 33.413  39.727  42.828  1.00 23.09 ? 343  MET B SD  1 
ATOM   7044  C  CE  . MET B  1 326 ? 31.665  39.335  42.642  1.00 23.20 ? 343  MET B CE  1 
ATOM   7045  N  N   . PHE B  1 327 ? 36.949  39.873  47.408  1.00 20.66 ? 344  PHE B N   1 
ATOM   7046  C  CA  . PHE B  1 327 ? 38.311  39.817  47.911  1.00 21.79 ? 344  PHE B CA  1 
ATOM   7047  C  C   . PHE B  1 327 ? 38.986  38.605  47.276  1.00 22.20 ? 344  PHE B C   1 
ATOM   7048  O  O   . PHE B  1 327 ? 38.559  37.484  47.534  1.00 22.51 ? 344  PHE B O   1 
ATOM   7049  C  CB  . PHE B  1 327 ? 38.243  39.733  49.441  1.00 21.93 ? 344  PHE B CB  1 
ATOM   7050  C  CG  . PHE B  1 327 ? 39.568  39.780  50.192  1.00 22.92 ? 344  PHE B CG  1 
ATOM   7051  C  CD1 . PHE B  1 327 ? 40.403  38.668  50.241  1.00 23.20 ? 344  PHE B CD1 1 
ATOM   7052  C  CD2 . PHE B  1 327 ? 39.947  40.922  50.897  1.00 22.54 ? 344  PHE B CD2 1 
ATOM   7053  C  CE1 . PHE B  1 327 ? 41.603  38.716  50.938  1.00 24.39 ? 344  PHE B CE1 1 
ATOM   7054  C  CE2 . PHE B  1 327 ? 41.147  40.963  51.589  1.00 22.88 ? 344  PHE B CE2 1 
ATOM   7055  C  CZ  . PHE B  1 327 ? 41.971  39.860  51.612  1.00 22.49 ? 344  PHE B CZ  1 
ATOM   7056  N  N   . ASP B  1 328 ? 40.000  38.842  46.424  1.00 21.36 ? 345  ASP B N   1 
ATOM   7057  C  CA  . ASP B  1 328 ? 40.659  37.783  45.671  1.00 21.26 ? 345  ASP B CA  1 
ATOM   7058  C  C   . ASP B  1 328 ? 42.048  37.523  46.255  1.00 22.03 ? 345  ASP B C   1 
ATOM   7059  O  O   . ASP B  1 328 ? 42.371  38.004  47.336  1.00 21.52 ? 345  ASP B O   1 
ATOM   7060  C  CB  . ASP B  1 328 ? 40.660  38.097  44.180  1.00 20.90 ? 345  ASP B CB  1 
ATOM   7061  C  CG  . ASP B  1 328 ? 41.556  39.247  43.730  1.00 20.52 ? 345  ASP B CG  1 
ATOM   7062  O  OD1 . ASP B  1 328 ? 42.295  39.786  44.568  1.00 19.91 ? 345  ASP B OD1 1 
ATOM   7063  O  OD2 . ASP B  1 328 ? 41.496  39.604  42.540  1.00 19.84 ? 345  ASP B OD2 1 
ATOM   7064  N  N   . LYS B  1 329 ? 42.869  36.749  45.536  1.00 24.43 ? 346  LYS B N   1 
ATOM   7065  C  CA  . LYS B  1 329 ? 44.181  36.351  46.027  1.00 27.35 ? 346  LYS B CA  1 
ATOM   7066  C  C   . LYS B  1 329 ? 45.096  37.563  46.225  1.00 26.59 ? 346  LYS B C   1 
ATOM   7067  O  O   . LYS B  1 329 ? 46.110  37.447  46.914  1.00 26.30 ? 346  LYS B O   1 
ATOM   7068  C  CB  . LYS B  1 329 ? 44.831  35.331  45.085  1.00 30.42 ? 346  LYS B CB  1 
ATOM   7069  C  CG  . LYS B  1 329 ? 45.286  35.864  43.734  1.00 34.06 ? 346  LYS B CG  1 
ATOM   7070  C  CD  . LYS B  1 329 ? 46.251  34.935  43.005  1.00 39.87 ? 346  LYS B CD  1 
ATOM   7071  C  CE  . LYS B  1 329 ? 45.674  33.589  42.722  1.00 43.96 ? 346  LYS B CE  1 
ATOM   7072  N  NZ  . LYS B  1 329 ? 46.572  32.805  41.870  1.00 47.84 ? 346  LYS B NZ  1 
ATOM   7073  N  N   . TYR B  1 330 ? 44.742  38.713  45.627  1.00 25.87 ? 347  TYR B N   1 
ATOM   7074  C  CA  . TYR B  1 330 ? 45.528  39.935  45.751  1.00 25.75 ? 347  TYR B CA  1 
ATOM   7075  C  C   . TYR B  1 330 ? 44.962  40.878  46.815  1.00 25.60 ? 347  TYR B C   1 
ATOM   7076  O  O   . TYR B  1 330 ? 45.606  41.867  47.152  1.00 26.57 ? 347  TYR B O   1 
ATOM   7077  C  CB  . TYR B  1 330 ? 45.597  40.648  44.396  1.00 26.44 ? 347  TYR B CB  1 
ATOM   7078  C  CG  . TYR B  1 330 ? 46.078  39.752  43.265  1.00 27.97 ? 347  TYR B CG  1 
ATOM   7079  C  CD1 . TYR B  1 330 ? 47.389  39.294  43.229  1.00 29.21 ? 347  TYR B CD1 1 
ATOM   7080  C  CD2 . TYR B  1 330 ? 45.222  39.351  42.245  1.00 29.21 ? 347  TYR B CD2 1 
ATOM   7081  C  CE1 . TYR B  1 330 ? 47.837  38.472  42.211  1.00 31.04 ? 347  TYR B CE1 1 
ATOM   7082  C  CE2 . TYR B  1 330 ? 45.657  38.525  41.219  1.00 31.16 ? 347  TYR B CE2 1 
ATOM   7083  C  CZ  . TYR B  1 330 ? 46.970  38.084  41.204  1.00 32.30 ? 347  TYR B CZ  1 
ATOM   7084  O  OH  . TYR B  1 330 ? 47.428  37.270  40.211  1.00 33.73 ? 347  TYR B OH  1 
ATOM   7085  N  N   . GLY B  1 331 ? 43.756  40.600  47.330  1.00 24.14 ? 348  GLY B N   1 
ATOM   7086  C  CA  . GLY B  1 331 ? 43.136  41.445  48.338  1.00 22.92 ? 348  GLY B CA  1 
ATOM   7087  C  C   . GLY B  1 331 ? 41.788  41.990  47.870  1.00 22.56 ? 348  GLY B C   1 
ATOM   7088  O  O   . GLY B  1 331 ? 41.186  41.464  46.932  1.00 22.58 ? 348  GLY B O   1 
ATOM   7089  N  N   . LEU B  1 332 ? 41.331  43.061  48.529  1.00 22.47 ? 349  LEU B N   1 
ATOM   7090  C  CA  . LEU B  1 332 ? 40.017  43.623  48.270  1.00 21.83 ? 349  LEU B CA  1 
ATOM   7091  C  C   . LEU B  1 332 ? 40.014  44.275  46.888  1.00 22.38 ? 349  LEU B C   1 
ATOM   7092  O  O   . LEU B  1 332 ? 40.947  44.994  46.523  1.00 20.24 ? 349  LEU B O   1 
ATOM   7093  C  CB  . LEU B  1 332 ? 39.650  44.603  49.384  1.00 22.03 ? 349  LEU B CB  1 
ATOM   7094  C  CG  . LEU B  1 332 ? 38.206  45.117  49.396  1.00 22.57 ? 349  LEU B CG  1 
ATOM   7095  C  CD1 . LEU B  1 332 ? 37.237  43.995  49.742  1.00 22.68 ? 349  LEU B CD1 1 
ATOM   7096  C  CD2 . LEU B  1 332 ? 38.025  46.281  50.359  1.00 22.51 ? 349  LEU B CD2 1 
ATOM   7097  N  N   . LEU B  1 333 ? 38.959  43.988  46.111  1.00 21.82 ? 350  LEU B N   1 
ATOM   7098  C  CA  . LEU B  1 333 ? 38.761  44.623  44.821  1.00 22.00 ? 350  LEU B CA  1 
ATOM   7099  C  C   . LEU B  1 333 ? 38.266  46.047  45.060  1.00 23.06 ? 350  LEU B C   1 
ATOM   7100  O  O   . LEU B  1 333 ? 37.089  46.279  45.330  1.00 23.52 ? 350  LEU B O   1 
ATOM   7101  C  CB  . LEU B  1 333 ? 37.815  43.833  43.917  1.00 22.11 ? 350  LEU B CB  1 
ATOM   7102  C  CG  . LEU B  1 333 ? 38.445  42.681  43.126  1.00 22.32 ? 350  LEU B CG  1 
ATOM   7103  C  CD1 . LEU B  1 333 ? 38.807  41.496  44.017  1.00 22.58 ? 350  LEU B CD1 1 
ATOM   7104  C  CD2 . LEU B  1 333 ? 37.530  42.229  41.994  1.00 22.68 ? 350  LEU B CD2 1 
ATOM   7105  N  N   . VAL B  1 334 ? 39.202  46.995  44.973  1.00 23.46 ? 351  VAL B N   1 
ATOM   7106  C  CA  . VAL B  1 334 ? 38.902  48.404  45.122  1.00 24.16 ? 351  VAL B CA  1 
ATOM   7107  C  C   . VAL B  1 334 ? 39.387  49.126  43.868  1.00 24.23 ? 351  VAL B C   1 
ATOM   7108  O  O   . VAL B  1 334 ? 40.419  48.769  43.300  1.00 22.92 ? 351  VAL B O   1 
ATOM   7109  C  CB  . VAL B  1 334 ? 39.525  48.996  46.402  1.00 25.08 ? 351  VAL B CB  1 
ATOM   7110  C  CG1 . VAL B  1 334 ? 38.968  48.335  47.654  1.00 24.72 ? 351  VAL B CG1 1 
ATOM   7111  C  CG2 . VAL B  1 334 ? 41.048  48.928  46.402  1.00 25.46 ? 351  VAL B CG2 1 
ATOM   7112  N  N   . LYS B  1 335 ? 38.609  50.121  43.438  1.00 26.12 ? 352  LYS B N   1 
ATOM   7113  C  CA  . LYS B  1 335 ? 38.986  50.982  42.333  1.00 28.76 ? 352  LYS B CA  1 
ATOM   7114  C  C   . LYS B  1 335 ? 40.331  51.618  42.667  1.00 29.66 ? 352  LYS B C   1 
ATOM   7115  O  O   . LYS B  1 335 ? 40.482  52.247  43.718  1.00 31.62 ? 352  LYS B O   1 
ATOM   7116  C  CB  . LYS B  1 335 ? 38.002  52.136  42.108  1.00 31.43 ? 352  LYS B CB  1 
ATOM   7117  C  CG  . LYS B  1 335 ? 36.542  51.788  41.891  1.00 35.52 ? 352  LYS B CG  1 
ATOM   7118  C  CD  . LYS B  1 335 ? 36.143  51.404  40.472  1.00 39.56 ? 352  LYS B CD  1 
ATOM   7119  C  CE  . LYS B  1 335 ? 34.645  51.472  40.315  1.00 42.77 ? 352  LYS B CE  1 
ATOM   7120  N  NZ  . LYS B  1 335 ? 34.133  50.538  39.306  1.00 45.33 ? 352  LYS B NZ  1 
ATOM   7121  N  N   . GLY B  1 336 ? 41.315  51.399  41.794  1.00 29.21 ? 353  GLY B N   1 
ATOM   7122  C  CA  . GLY B  1 336 ? 42.589  52.077  41.913  1.00 29.59 ? 353  GLY B CA  1 
ATOM   7123  C  C   . GLY B  1 336 ? 43.651  51.226  42.600  1.00 29.89 ? 353  GLY B C   1 
ATOM   7124  O  O   . GLY B  1 336 ? 44.752  51.713  42.836  1.00 31.08 ? 353  GLY B O   1 
ATOM   7125  N  N   . ARG B  1 337 ? 43.343  49.959  42.904  1.00 28.61 ? 354  ARG B N   1 
ATOM   7126  C  CA  . ARG B  1 337 ? 44.366  49.070  43.435  1.00 26.48 ? 354  ARG B CA  1 
ATOM   7127  C  C   . ARG B  1 337 ? 45.360  48.762  42.318  1.00 25.66 ? 354  ARG B C   1 
ATOM   7128  O  O   . ARG B  1 337 ? 45.079  49.009  41.149  1.00 25.38 ? 354  ARG B O   1 
ATOM   7129  C  CB  . ARG B  1 337 ? 43.803  47.766  44.016  1.00 26.16 ? 354  ARG B CB  1 
ATOM   7130  C  CG  . ARG B  1 337 ? 43.438  46.709  42.985  1.00 24.96 ? 354  ARG B CG  1 
ATOM   7131  C  CD  . ARG B  1 337 ? 43.001  45.415  43.642  1.00 24.15 ? 354  ARG B CD  1 
ATOM   7132  N  NE  . ARG B  1 337 ? 42.891  44.331  42.662  1.00 23.82 ? 354  ARG B NE  1 
ATOM   7133  C  CZ  . ARG B  1 337 ? 42.577  43.071  42.950  1.00 22.81 ? 354  ARG B CZ  1 
ATOM   7134  N  NH1 . ARG B  1 337 ? 42.348  42.706  44.198  1.00 21.60 ? 354  ARG B NH1 1 
ATOM   7135  N  NH2 . ARG B  1 337 ? 42.515  42.180  41.982  1.00 21.42 ? 354  ARG B NH2 1 
ATOM   7136  N  N   . LYS B  1 338 ? 46.507  48.188  42.696  1.00 26.24 ? 355  LYS B N   1 
ATOM   7137  C  CA  . LYS B  1 338 ? 47.582  47.905  41.760  1.00 26.26 ? 355  LYS B CA  1 
ATOM   7138  C  C   . LYS B  1 338 ? 47.259  46.654  40.941  1.00 25.57 ? 355  LYS B C   1 
ATOM   7139  O  O   . LYS B  1 338 ? 47.420  46.657  39.727  1.00 25.08 ? 355  LYS B O   1 
ATOM   7140  C  CB  . LYS B  1 338 ? 48.895  47.793  42.546  1.00 26.28 ? 355  LYS B CB  1 
ATOM   7141  C  CG  . LYS B  1 338 ? 50.160  47.820  41.710  1.00 26.41 ? 355  LYS B CG  1 
ATOM   7142  C  CD  . LYS B  1 338 ? 51.440  47.663  42.522  1.00 26.10 ? 355  LYS B CD  1 
ATOM   7143  C  CE  . LYS B  1 338 ? 52.606  47.354  41.638  1.00 25.75 ? 355  LYS B CE  1 
ATOM   7144  N  NZ  . LYS B  1 338 ? 53.850  47.257  42.401  1.00 25.57 ? 355  LYS B NZ  1 
ATOM   7145  N  N   . ALA B  1 339 ? 46.795  45.584  41.598  1.00 25.45 ? 356  ALA B N   1 
ATOM   7146  C  CA  . ALA B  1 339 ? 46.542  44.326  40.908  1.00 25.88 ? 356  ALA B CA  1 
ATOM   7147  C  C   . ALA B  1 339 ? 45.387  44.474  39.919  1.00 26.01 ? 356  ALA B C   1 
ATOM   7148  O  O   . ALA B  1 339 ? 44.477  45.271  40.121  1.00 25.47 ? 356  ALA B O   1 
ATOM   7149  C  CB  . ALA B  1 339 ? 46.274  43.217  41.905  1.00 25.49 ? 356  ALA B CB  1 
ATOM   7150  N  N   . LYS B  1 340 ? 45.428  43.661  38.862  1.00 27.36 ? 357  LYS B N   1 
ATOM   7151  C  CA  . LYS B  1 340 ? 44.512  43.777  37.740  1.00 29.76 ? 357  LYS B CA  1 
ATOM   7152  C  C   . LYS B  1 340 ? 43.066  43.534  38.180  1.00 28.40 ? 357  LYS B C   1 
ATOM   7153  O  O   . LYS B  1 340 ? 42.804  42.663  39.009  1.00 24.89 ? 357  LYS B O   1 
ATOM   7154  C  CB  . LYS B  1 340 ? 44.940  42.758  36.678  1.00 33.63 ? 357  LYS B CB  1 
ATOM   7155  C  CG  . LYS B  1 340 ? 44.271  42.920  35.325  1.00 38.26 ? 357  LYS B CG  1 
ATOM   7156  C  CD  . LYS B  1 340 ? 44.657  41.887  34.269  1.00 41.39 ? 357  LYS B CD  1 
ATOM   7157  C  CE  . LYS B  1 340 ? 46.132  41.768  34.025  1.00 43.53 ? 357  LYS B CE  1 
ATOM   7158  N  NZ  . LYS B  1 340 ? 46.757  40.730  34.852  1.00 45.75 ? 357  LYS B NZ  1 
ATOM   7159  N  N   . ILE B  1 341 ? 42.157  44.348  37.620  1.00 27.35 ? 358  ILE B N   1 
ATOM   7160  C  CA  . ILE B  1 341 ? 40.718  44.138  37.655  1.00 27.40 ? 358  ILE B CA  1 
ATOM   7161  C  C   . ILE B  1 341 ? 40.241  44.013  36.209  1.00 28.65 ? 358  ILE B C   1 
ATOM   7162  O  O   . ILE B  1 341 ? 40.470  44.922  35.413  1.00 27.12 ? 358  ILE B O   1 
ATOM   7163  C  CB  . ILE B  1 341 ? 40.013  45.319  38.351  1.00 28.99 ? 358  ILE B CB  1 
ATOM   7164  C  CG1 . ILE B  1 341 ? 40.536  45.569  39.767  1.00 28.88 ? 358  ILE B CG1 1 
ATOM   7165  C  CG2 . ILE B  1 341 ? 38.492  45.139  38.348  1.00 29.32 ? 358  ILE B CG2 1 
ATOM   7166  C  CD1 . ILE B  1 341 ? 40.082  44.545  40.786  1.00 29.93 ? 358  ILE B CD1 1 
ATOM   7167  N  N   . ASP B  1 342 ? 39.559  42.914  35.865  1.00 28.71 ? 359  ASP B N   1 
ATOM   7168  C  CA  . ASP B  1 342 ? 39.071  42.751  34.503  1.00 30.76 ? 359  ASP B CA  1 
ATOM   7169  C  C   . ASP B  1 342 ? 37.695  43.405  34.389  1.00 29.31 ? 359  ASP B C   1 
ATOM   7170  O  O   . ASP B  1 342 ? 37.073  43.741  35.397  1.00 26.49 ? 359  ASP B O   1 
ATOM   7171  C  CB  . ASP B  1 342 ? 39.180  41.305  34.039  1.00 34.85 ? 359  ASP B CB  1 
ATOM   7172  C  CG  . ASP B  1 342 ? 38.029  40.369  34.376  1.00 38.80 ? 359  ASP B CG  1 
ATOM   7173  O  OD1 . ASP B  1 342 ? 36.988  40.855  34.864  1.00 41.78 ? 359  ASP B OD1 1 
ATOM   7174  O  OD2 . ASP B  1 342 ? 38.181  39.153  34.128  1.00 45.45 ? 359  ASP B OD2 1 
ATOM   7175  N  N   . SER B  1 343 ? 37.224  43.578  33.149  1.00 29.81 ? 360  SER B N   1 
ATOM   7176  C  CA  . SER B  1 343 ? 36.029  44.367  32.883  1.00 31.57 ? 360  SER B CA  1 
ATOM   7177  C  C   . SER B  1 343 ? 34.789  43.731  33.516  1.00 30.28 ? 360  SER B C   1 
ATOM   7178  O  O   . SER B  1 343 ? 33.846  44.440  33.857  1.00 31.50 ? 360  SER B O   1 
ATOM   7179  C  CB  . SER B  1 343 ? 35.839  44.585  31.401  1.00 34.06 ? 360  SER B CB  1 
ATOM   7180  O  OG  . SER B  1 343 ? 35.735  43.344  30.717  1.00 36.72 ? 360  SER B OG  1 
ATOM   7181  N  N   . TYR B  1 344 ? 34.787  42.401  33.676  1.00 28.12 ? 361  TYR B N   1 
ATOM   7182  C  CA  . TYR B  1 344 ? 33.650  41.710  34.267  1.00 28.73 ? 361  TYR B CA  1 
ATOM   7183  C  C   . TYR B  1 344 ? 33.627  41.877  35.788  1.00 25.89 ? 361  TYR B C   1 
ATOM   7184  O  O   . TYR B  1 344 ? 32.570  41.736  36.399  1.00 23.94 ? 361  TYR B O   1 
ATOM   7185  C  CB  . TYR B  1 344 ? 33.654  40.231  33.868  1.00 30.44 ? 361  TYR B CB  1 
ATOM   7186  C  CG  . TYR B  1 344 ? 33.511  40.035  32.366  1.00 33.01 ? 361  TYR B CG  1 
ATOM   7187  C  CD1 . TYR B  1 344 ? 32.314  40.319  31.718  1.00 34.63 ? 361  TYR B CD1 1 
ATOM   7188  C  CD2 . TYR B  1 344 ? 34.580  39.591  31.597  1.00 34.85 ? 361  TYR B CD2 1 
ATOM   7189  C  CE1 . TYR B  1 344 ? 32.184  40.162  30.347  1.00 37.38 ? 361  TYR B CE1 1 
ATOM   7190  C  CE2 . TYR B  1 344 ? 34.460  39.418  30.228  1.00 36.78 ? 361  TYR B CE2 1 
ATOM   7191  C  CZ  . TYR B  1 344 ? 33.261  39.710  29.603  1.00 38.29 ? 361  TYR B CZ  1 
ATOM   7192  O  OH  . TYR B  1 344 ? 33.145  39.536  28.256  1.00 43.29 ? 361  TYR B OH  1 
ATOM   7193  N  N   . GLN B  1 345 ? 34.783  42.171  36.399  1.00 23.87 ? 362  GLN B N   1 
ATOM   7194  C  CA  . GLN B  1 345 ? 34.854  42.376  37.839  1.00 23.25 ? 362  GLN B CA  1 
ATOM   7195  C  C   . GLN B  1 345 ? 34.555  43.829  38.215  1.00 23.91 ? 362  GLN B C   1 
ATOM   7196  O  O   . GLN B  1 345 ? 34.244  44.100  39.374  1.00 21.87 ? 362  GLN B O   1 
ATOM   7197  C  CB  . GLN B  1 345 ? 36.227  41.985  38.387  1.00 22.88 ? 362  GLN B CB  1 
ATOM   7198  C  CG  . GLN B  1 345 ? 36.577  40.513  38.210  1.00 22.13 ? 362  GLN B CG  1 
ATOM   7199  C  CD  . GLN B  1 345 ? 38.048  40.236  38.421  1.00 23.32 ? 362  GLN B CD  1 
ATOM   7200  O  OE1 . GLN B  1 345 ? 38.915  40.977  37.933  1.00 22.90 ? 362  GLN B OE1 1 
ATOM   7201  N  NE2 . GLN B  1 345 ? 38.347  39.196  39.188  1.00 22.76 ? 362  GLN B NE2 1 
ATOM   7202  N  N   . GLU B  1 346 ? 34.649  44.751  37.240  1.00 26.37 ? 363  GLU B N   1 
ATOM   7203  C  CA  . GLU B  1 346 ? 34.574  46.190  37.484  1.00 28.60 ? 363  GLU B CA  1 
ATOM   7204  C  C   . GLU B  1 346 ? 33.306  46.587  38.244  1.00 27.23 ? 363  GLU B C   1 
ATOM   7205  O  O   . GLU B  1 346 ? 33.369  47.431  39.138  1.00 25.70 ? 363  GLU B O   1 
ATOM   7206  C  CB  . GLU B  1 346 ? 34.642  47.011  36.191  1.00 32.96 ? 363  GLU B CB  1 
ATOM   7207  C  CG  . GLU B  1 346 ? 36.057  47.183  35.645  1.00 36.51 ? 363  GLU B CG  1 
ATOM   7208  C  CD  . GLU B  1 346 ? 36.179  47.986  34.354  1.00 41.53 ? 363  GLU B CD  1 
ATOM   7209  O  OE1 . GLU B  1 346 ? 35.196  48.625  33.915  1.00 43.86 ? 363  GLU B OE1 1 
ATOM   7210  O  OE2 . GLU B  1 346 ? 37.281  47.952  33.766  1.00 44.70 ? 363  GLU B OE2 1 
ATOM   7211  N  N   . PRO B  1 347 ? 32.113  46.047  37.908  1.00 25.79 ? 364  PRO B N   1 
ATOM   7212  C  CA  . PRO B  1 347 ? 30.892  46.396  38.640  1.00 26.52 ? 364  PRO B CA  1 
ATOM   7213  C  C   . PRO B  1 347 ? 30.925  46.172  40.152  1.00 25.99 ? 364  PRO B C   1 
ATOM   7214  O  O   . PRO B  1 347 ? 30.197  46.837  40.883  1.00 24.53 ? 364  PRO B O   1 
ATOM   7215  C  CB  . PRO B  1 347 ? 29.811  45.524  37.979  1.00 27.23 ? 364  PRO B CB  1 
ATOM   7216  C  CG  . PRO B  1 347 ? 30.364  45.171  36.623  1.00 26.89 ? 364  PRO B CG  1 
ATOM   7217  C  CD  . PRO B  1 347 ? 31.865  45.118  36.797  1.00 26.74 ? 364  PRO B CD  1 
ATOM   7218  N  N   . PHE B  1 348 ? 31.750  45.219  40.611  1.00 25.20 ? 365  PHE B N   1 
ATOM   7219  C  CA  . PHE B  1 348 ? 31.811  44.853  42.020  1.00 25.49 ? 365  PHE B CA  1 
ATOM   7220  C  C   . PHE B  1 348 ? 33.111  45.352  42.647  1.00 25.59 ? 365  PHE B C   1 
ATOM   7221  O  O   . PHE B  1 348 ? 33.465  44.940  43.751  1.00 26.72 ? 365  PHE B O   1 
ATOM   7222  C  CB  . PHE B  1 348 ? 31.656  43.335  42.139  1.00 24.67 ? 365  PHE B CB  1 
ATOM   7223  C  CG  . PHE B  1 348 ? 30.409  42.830  41.434  1.00 23.68 ? 365  PHE B CG  1 
ATOM   7224  C  CD1 . PHE B  1 348 ? 29.150  43.047  41.982  1.00 23.79 ? 365  PHE B CD1 1 
ATOM   7225  C  CD2 . PHE B  1 348 ? 30.496  42.172  40.214  1.00 23.43 ? 365  PHE B CD2 1 
ATOM   7226  C  CE1 . PHE B  1 348 ? 28.008  42.618  41.324  1.00 23.71 ? 365  PHE B CE1 1 
ATOM   7227  C  CE2 . PHE B  1 348 ? 29.352  41.734  39.565  1.00 23.48 ? 365  PHE B CE2 1 
ATOM   7228  C  CZ  . PHE B  1 348 ? 28.111  41.955  40.123  1.00 23.26 ? 365  PHE B CZ  1 
ATOM   7229  N  N   . THR B  1 349 ? 33.809  46.233  41.920  1.00 25.94 ? 366  THR B N   1 
ATOM   7230  C  CA  . THR B  1 349 ? 35.010  46.894  42.399  1.00 25.47 ? 366  THR B CA  1 
ATOM   7231  C  C   . THR B  1 349 ? 34.626  48.307  42.829  1.00 27.35 ? 366  THR B C   1 
ATOM   7232  O  O   . THR B  1 349 ? 34.158  49.082  42.001  1.00 29.34 ? 366  THR B O   1 
ATOM   7233  C  CB  . THR B  1 349 ? 36.033  46.904  41.264  1.00 24.82 ? 366  THR B CB  1 
ATOM   7234  O  OG1 . THR B  1 349 ? 36.275  45.538  40.945  1.00 24.10 ? 366  THR B OG1 1 
ATOM   7235  C  CG2 . THR B  1 349 ? 37.336  47.583  41.644  1.00 25.07 ? 366  THR B CG2 1 
ATOM   7236  N  N   . HIS B  1 350 ? 34.850  48.645  44.106  1.00 28.37 ? 367  HIS B N   1 
ATOM   7237  C  CA  . HIS B  1 350 ? 34.252  49.830  44.705  1.00 29.94 ? 367  HIS B CA  1 
ATOM   7238  C  C   . HIS B  1 350 ? 35.321  50.795  45.208  1.00 31.18 ? 367  HIS B C   1 
ATOM   7239  O  O   . HIS B  1 350 ? 36.481  50.418  45.370  1.00 30.06 ? 367  HIS B O   1 
ATOM   7240  C  CB  . HIS B  1 350 ? 33.306  49.411  45.834  1.00 30.10 ? 367  HIS B CB  1 
ATOM   7241  C  CG  . HIS B  1 350 ? 32.215  48.530  45.335  1.00 29.48 ? 367  HIS B CG  1 
ATOM   7242  N  ND1 . HIS B  1 350 ? 31.506  48.827  44.188  1.00 29.93 ? 367  HIS B ND1 1 
ATOM   7243  C  CD2 . HIS B  1 350 ? 31.726  47.375  45.788  1.00 29.58 ? 367  HIS B CD2 1 
ATOM   7244  C  CE1 . HIS B  1 350 ? 30.617  47.868  43.968  1.00 30.07 ? 367  HIS B CE1 1 
ATOM   7245  N  NE2 . HIS B  1 350 ? 30.736  46.974  44.928  1.00 29.07 ? 367  HIS B NE2 1 
ATOM   7246  N  N   . SER B  1 351 ? 34.897  52.046  45.443  1.00 31.93 ? 368  SER B N   1 
ATOM   7247  C  CA  . SER B  1 351 ? 35.748  53.067  46.038  1.00 32.11 ? 368  SER B CA  1 
ATOM   7248  C  C   . SER B  1 351 ? 36.315  52.540  47.348  1.00 32.51 ? 368  SER B C   1 
ATOM   7249  O  O   . SER B  1 351 ? 35.586  51.944  48.138  1.00 31.60 ? 368  SER B O   1 
ATOM   7250  C  CB  . SER B  1 351 ? 35.003  54.361  46.267  1.00 31.43 ? 368  SER B CB  1 
ATOM   7251  O  OG  . SER B  1 351 ? 34.436  54.840  45.058  1.00 31.56 ? 368  SER B OG  1 
ATOM   7252  N  N   . ALA B  1 352 ? 37.614  52.770  47.563  1.00 32.65 ? 369  ALA B N   1 
ATOM   7253  C  CA  . ALA B  1 352 ? 38.304  52.226  48.717  1.00 33.99 ? 369  ALA B CA  1 
ATOM   7254  C  C   . ALA B  1 352 ? 37.599  52.657  50.002  1.00 35.41 ? 369  ALA B C   1 
ATOM   7255  O  O   . ALA B  1 352 ? 37.173  53.805  50.121  1.00 33.23 ? 369  ALA B O   1 
ATOM   7256  C  CB  . ALA B  1 352 ? 39.749  52.670  48.709  1.00 34.90 ? 369  ALA B CB  1 
ATOM   7257  N  N   . PRO B  1 353 ? 37.440  51.751  50.995  1.00 35.66 ? 370  PRO B N   1 
ATOM   7258  C  CA  . PRO B  1 353 ? 36.983  52.148  52.326  1.00 39.55 ? 370  PRO B CA  1 
ATOM   7259  C  C   . PRO B  1 353 ? 38.121  52.882  53.033  1.00 42.58 ? 370  PRO B C   1 
ATOM   7260  O  O   . PRO B  1 353 ? 39.214  53.008  52.482  1.00 42.18 ? 370  PRO B O   1 
ATOM   7261  C  CB  . PRO B  1 353 ? 36.579  50.826  53.013  1.00 38.71 ? 370  PRO B CB  1 
ATOM   7262  C  CG  . PRO B  1 353 ? 37.333  49.745  52.260  1.00 37.08 ? 370  PRO B CG  1 
ATOM   7263  C  CD  . PRO B  1 353 ? 37.701  50.307  50.892  1.00 36.32 ? 370  PRO B CD  1 
ATOM   7264  N  N   . GLU B  1 354 ? 37.869  53.349  54.260  1.00 48.49 ? 371  GLU B N   1 
ATOM   7265  C  CA  . GLU B  1 354 ? 38.808  54.227  54.943  1.00 51.86 ? 371  GLU B CA  1 
ATOM   7266  C  C   . GLU B  1 354 ? 40.139  53.510  55.172  1.00 47.57 ? 371  GLU B C   1 
ATOM   7267  O  O   . GLU B  1 354 ? 41.188  54.144  55.107  1.00 47.74 ? 371  GLU B O   1 
ATOM   7268  C  CB  . GLU B  1 354 ? 38.226  54.775  56.248  1.00 59.60 ? 371  GLU B CB  1 
ATOM   7269  C  CG  . GLU B  1 354 ? 38.953  56.014  56.772  1.00 65.78 ? 371  GLU B CG  1 
ATOM   7270  C  CD  . GLU B  1 354 ? 38.725  57.307  55.997  1.00 69.22 ? 371  GLU B CD  1 
ATOM   7271  O  OE1 . GLU B  1 354 ? 39.109  57.388  54.809  1.00 70.51 ? 371  GLU B OE1 1 
ATOM   7272  O  OE2 . GLU B  1 354 ? 38.163  58.249  56.597  1.00 69.79 ? 371  GLU B OE2 1 
ATOM   7273  N  N   . SER B  1 355 ? 40.096  52.194  55.427  1.00 45.30 ? 372  SER B N   1 
ATOM   7274  C  CA  . SER B  1 355 ? 41.306  51.392  55.538  1.00 43.41 ? 372  SER B CA  1 
ATOM   7275  C  C   . SER B  1 355 ? 41.264  50.219  54.558  1.00 40.39 ? 372  SER B C   1 
ATOM   7276  O  O   . SER B  1 355 ? 40.195  49.683  54.274  1.00 39.31 ? 372  SER B O   1 
ATOM   7277  C  CB  . SER B  1 355 ? 41.515  50.924  56.955  1.00 46.23 ? 372  SER B CB  1 
ATOM   7278  O  OG  . SER B  1 355 ? 40.377  50.223  57.436  1.00 49.06 ? 372  SER B OG  1 
ATOM   7279  N  N   . ILE B  1 356 ? 42.444  49.832  54.051  1.00 37.84 ? 373  ILE B N   1 
ATOM   7280  C  CA  . ILE B  1 356 ? 42.575  48.742  53.093  1.00 36.63 ? 373  ILE B CA  1 
ATOM   7281  C  C   . ILE B  1 356 ? 42.960  47.475  53.851  1.00 34.84 ? 373  ILE B C   1 
ATOM   7282  O  O   . ILE B  1 356 ? 44.005  47.445  54.496  1.00 32.25 ? 373  ILE B O   1 
ATOM   7283  C  CB  . ILE B  1 356 ? 43.617  49.069  52.004  1.00 36.84 ? 373  ILE B CB  1 
ATOM   7284  C  CG1 . ILE B  1 356 ? 43.326  50.394  51.287  1.00 36.85 ? 373  ILE B CG1 1 
ATOM   7285  C  CG2 . ILE B  1 356 ? 43.753  47.914  51.009  1.00 37.16 ? 373  ILE B CG2 1 
ATOM   7286  C  CD1 . ILE B  1 356 ? 41.992  50.439  50.566  1.00 37.56 ? 373  ILE B CD1 1 
ATOM   7287  N  N   . PRO B  1 357 ? 42.146  46.391  53.796  1.00 33.97 ? 374  PRO B N   1 
ATOM   7288  C  CA  . PRO B  1 357 ? 42.465  45.155  54.514  1.00 33.48 ? 374  PRO B CA  1 
ATOM   7289  C  C   . PRO B  1 357 ? 43.592  44.360  53.863  1.00 33.48 ? 374  PRO B C   1 
ATOM   7290  O  O   . PRO B  1 357 ? 43.744  44.375  52.644  1.00 36.68 ? 374  PRO B O   1 
ATOM   7291  C  CB  . PRO B  1 357 ? 41.131  44.386  54.498  1.00 35.87 ? 374  PRO B CB  1 
ATOM   7292  C  CG  . PRO B  1 357 ? 40.442  44.860  53.235  1.00 35.32 ? 374  PRO B CG  1 
ATOM   7293  C  CD  . PRO B  1 357 ? 40.866  46.313  53.073  1.00 34.92 ? 374  PRO B CD  1 
ATOM   7294  N  N   . ASP B  1 358 ? 44.375  43.669  54.695  1.00 33.01 ? 375  ASP B N   1 
ATOM   7295  C  CA  . ASP B  1 358 ? 45.416  42.770  54.225  1.00 32.64 ? 375  ASP B CA  1 
ATOM   7296  C  C   . ASP B  1 358 ? 44.906  41.332  54.200  1.00 30.53 ? 375  ASP B C   1 
ATOM   7297  O  O   . ASP B  1 358 ? 45.374  40.537  53.391  1.00 29.88 ? 375  ASP B O   1 
ATOM   7298  C  CB  . ASP B  1 358 ? 46.666  42.874  55.084  1.00 34.38 ? 375  ASP B CB  1 
ATOM   7299  C  CG  . ASP B  1 358 ? 47.516  44.114  54.851  1.00 37.54 ? 375  ASP B CG  1 
ATOM   7300  O  OD1 . ASP B  1 358 ? 47.173  44.900  53.942  1.00 38.28 ? 375  ASP B OD1 1 
ATOM   7301  O  OD2 . ASP B  1 358 ? 48.515  44.281  55.584  1.00 43.87 ? 375  ASP B OD2 1 
ATOM   7302  N  N   . THR B  1 359 ? 43.978  41.005  55.110  1.00 29.27 ? 376  THR B N   1 
ATOM   7303  C  CA  . THR B  1 359 ? 43.435  39.661  55.231  1.00 27.86 ? 376  THR B CA  1 
ATOM   7304  C  C   . THR B  1 359 ? 41.913  39.731  55.121  1.00 25.83 ? 376  THR B C   1 
ATOM   7305  O  O   . THR B  1 359 ? 41.333  40.811  55.160  1.00 23.54 ? 376  THR B O   1 
ATOM   7306  C  CB  . THR B  1 359 ? 43.855  39.028  56.559  1.00 28.31 ? 376  THR B CB  1 
ATOM   7307  O  OG1 . THR B  1 359 ? 43.131  39.726  57.569  1.00 27.91 ? 376  THR B OG1 1 
ATOM   7308  C  CG2 . THR B  1 359 ? 45.355  39.087  56.796  1.00 28.93 ? 376  THR B CG2 1 
ATOM   7309  N  N   . PHE B  1 360 ? 41.282  38.558  55.000  1.00 25.06 ? 377  PHE B N   1 
ATOM   7310  C  CA  . PHE B  1 360 ? 39.836  38.476  54.886  1.00 24.33 ? 377  PHE B CA  1 
ATOM   7311  C  C   . PHE B  1 360 ? 39.190  38.883  56.211  1.00 23.74 ? 377  PHE B C   1 
ATOM   7312  O  O   . PHE B  1 360 ? 38.156  39.546  56.218  1.00 23.29 ? 377  PHE B O   1 
ATOM   7313  C  CB  . PHE B  1 360 ? 39.409  37.079  54.425  1.00 23.56 ? 377  PHE B CB  1 
ATOM   7314  C  CG  . PHE B  1 360 ? 37.949  37.042  54.001  1.00 23.73 ? 377  PHE B CG  1 
ATOM   7315  C  CD1 . PHE B  1 360 ? 37.545  37.618  52.802  1.00 23.10 ? 377  PHE B CD1 1 
ATOM   7316  C  CD2 . PHE B  1 360 ? 36.984  36.440  54.799  1.00 23.83 ? 377  PHE B CD2 1 
ATOM   7317  C  CE1 . PHE B  1 360 ? 36.215  37.594  52.418  1.00 22.34 ? 377  PHE B CE1 1 
ATOM   7318  C  CE2 . PHE B  1 360 ? 35.654  36.425  54.410  1.00 23.13 ? 377  PHE B CE2 1 
ATOM   7319  C  CZ  . PHE B  1 360 ? 35.275  37.000  53.223  1.00 22.02 ? 377  PHE B CZ  1 
ATOM   7320  N  N   . GLU B  1 361 ? 39.812  38.492  57.328  1.00 25.01 ? 378  GLU B N   1 
ATOM   7321  C  CA  . GLU B  1 361 ? 39.390  38.930  58.653  1.00 26.10 ? 378  GLU B CA  1 
ATOM   7322  C  C   . GLU B  1 361 ? 39.319  40.456  58.725  1.00 25.94 ? 378  GLU B C   1 
ATOM   7323  O  O   . GLU B  1 361 ? 38.334  41.009  59.217  1.00 24.54 ? 378  GLU B O   1 
ATOM   7324  C  CB  . GLU B  1 361 ? 40.361  38.399  59.706  1.00 27.70 ? 378  GLU B CB  1 
ATOM   7325  C  CG  . GLU B  1 361 ? 39.961  38.742  61.136  1.00 29.41 ? 378  GLU B CG  1 
ATOM   7326  C  CD  . GLU B  1 361 ? 41.032  38.444  62.169  1.00 31.43 ? 378  GLU B CD  1 
ATOM   7327  O  OE1 . GLU B  1 361 ? 40.770  38.693  63.362  1.00 30.61 ? 378  GLU B OE1 1 
ATOM   7328  O  OE2 . GLU B  1 361 ? 42.120  37.961  61.788  1.00 34.29 ? 378  GLU B OE2 1 
ATOM   7329  N  N   . ASP B  1 362 ? 40.375  41.131  58.247  1.00 25.92 ? 379  ASP B N   1 
ATOM   7330  C  CA  . ASP B  1 362 ? 40.407  42.587  58.218  1.00 26.92 ? 379  ASP B CA  1 
ATOM   7331  C  C   . ASP B  1 362 ? 39.233  43.116  57.399  1.00 25.50 ? 379  ASP B C   1 
ATOM   7332  O  O   . ASP B  1 362 ? 38.613  44.102  57.778  1.00 24.79 ? 379  ASP B O   1 
ATOM   7333  C  CB  . ASP B  1 362 ? 41.701  43.131  57.629  1.00 28.69 ? 379  ASP B CB  1 
ATOM   7334  C  CG  . ASP B  1 362 ? 42.980  42.846  58.404  1.00 32.82 ? 379  ASP B CG  1 
ATOM   7335  O  OD1 . ASP B  1 362 ? 42.885  42.522  59.606  1.00 34.08 ? 379  ASP B OD1 1 
ATOM   7336  O  OD2 . ASP B  1 362 ? 44.068  42.930  57.789  1.00 36.10 ? 379  ASP B OD2 1 
ATOM   7337  N  N   . ALA B  1 363 ? 38.964  42.474  56.255  1.00 25.13 ? 380  ALA B N   1 
ATOM   7338  C  CA  . ALA B  1 363 ? 37.914  42.915  55.350  1.00 23.82 ? 380  ALA B CA  1 
ATOM   7339  C  C   . ALA B  1 363 ? 36.548  42.819  56.030  1.00 23.72 ? 380  ALA B C   1 
ATOM   7340  O  O   . ALA B  1 363 ? 35.717  43.714  55.881  1.00 23.36 ? 380  ALA B O   1 
ATOM   7341  C  CB  . ALA B  1 363 ? 37.949  42.108  54.071  1.00 24.53 ? 380  ALA B CB  1 
ATOM   7342  N  N   . VAL B  1 364 ? 36.328  41.724  56.763  1.00 23.44 ? 381  VAL B N   1 
ATOM   7343  C  CA  . VAL B  1 364 ? 35.097  41.533  57.512  1.00 24.99 ? 381  VAL B CA  1 
ATOM   7344  C  C   . VAL B  1 364 ? 34.959  42.643  58.558  1.00 27.01 ? 381  VAL B C   1 
ATOM   7345  O  O   . VAL B  1 364 ? 33.903  43.267  58.662  1.00 26.63 ? 381  VAL B O   1 
ATOM   7346  C  CB  . VAL B  1 364 ? 35.050  40.128  58.144  1.00 24.86 ? 381  VAL B CB  1 
ATOM   7347  C  CG1 . VAL B  1 364 ? 33.928  39.989  59.168  1.00 25.26 ? 381  VAL B CG1 1 
ATOM   7348  C  CG2 . VAL B  1 364 ? 34.915  39.042  57.084  1.00 25.58 ? 381  VAL B CG2 1 
ATOM   7349  N  N   . ASN B  1 365 ? 36.034  42.904  59.318  1.00 27.78 ? 382  ASN B N   1 
ATOM   7350  C  CA  . ASN B  1 365 ? 35.990  43.916  60.365  1.00 29.05 ? 382  ASN B CA  1 
ATOM   7351  C  C   . ASN B  1 365 ? 35.778  45.316  59.788  1.00 29.50 ? 382  ASN B C   1 
ATOM   7352  O  O   . ASN B  1 365 ? 35.107  46.133  60.410  1.00 30.46 ? 382  ASN B O   1 
ATOM   7353  C  CB  . ASN B  1 365 ? 37.221  43.868  61.265  1.00 29.70 ? 382  ASN B CB  1 
ATOM   7354  C  CG  . ASN B  1 365 ? 37.142  42.732  62.254  1.00 30.83 ? 382  ASN B CG  1 
ATOM   7355  O  OD1 . ASN B  1 365 ? 36.092  42.535  62.874  1.00 31.39 ? 382  ASN B OD1 1 
ATOM   7356  N  ND2 . ASN B  1 365 ? 38.214  41.966  62.396  1.00 32.10 ? 382  ASN B ND2 1 
ATOM   7357  N  N   . ILE B  1 366 ? 36.331  45.595  58.602  1.00 29.32 ? 383  ILE B N   1 
ATOM   7358  C  CA  . ILE B  1 366 ? 36.226  46.925  58.019  1.00 29.77 ? 383  ILE B CA  1 
ATOM   7359  C  C   . ILE B  1 366 ? 34.853  47.132  57.378  1.00 29.66 ? 383  ILE B C   1 
ATOM   7360  O  O   . ILE B  1 366 ? 34.211  48.145  57.635  1.00 28.84 ? 383  ILE B O   1 
ATOM   7361  C  CB  . ILE B  1 366 ? 37.380  47.178  57.031  1.00 31.16 ? 383  ILE B CB  1 
ATOM   7362  C  CG1 . ILE B  1 366 ? 38.714  47.308  57.777  1.00 32.26 ? 383  ILE B CG1 1 
ATOM   7363  C  CG2 . ILE B  1 366 ? 37.097  48.402  56.161  1.00 31.43 ? 383  ILE B CG2 1 
ATOM   7364  C  CD1 . ILE B  1 366 ? 39.939  47.144  56.898  1.00 34.18 ? 383  ILE B CD1 1 
ATOM   7365  N  N   . LEU B  1 367 ? 34.414  46.183  56.536  1.00 28.37 ? 384  LEU B N   1 
ATOM   7366  C  CA  . LEU B  1 367 ? 33.218  46.357  55.725  1.00 28.38 ? 384  LEU B CA  1 
ATOM   7367  C  C   . LEU B  1 367 ? 31.956  45.989  56.508  1.00 29.43 ? 384  LEU B C   1 
ATOM   7368  O  O   . LEU B  1 367 ? 30.872  46.457  56.168  1.00 27.62 ? 384  LEU B O   1 
ATOM   7369  C  CB  . LEU B  1 367 ? 33.329  45.523  54.449  1.00 28.10 ? 384  LEU B CB  1 
ATOM   7370  C  CG  . LEU B  1 367 ? 34.427  45.925  53.458  1.00 28.48 ? 384  LEU B CG  1 
ATOM   7371  C  CD1 . LEU B  1 367 ? 34.629  44.836  52.421  1.00 28.86 ? 384  LEU B CD1 1 
ATOM   7372  C  CD2 . LEU B  1 367 ? 34.110  47.241  52.780  1.00 29.18 ? 384  LEU B CD2 1 
ATOM   7373  N  N   . LYS B  1 368 ? 32.094  45.126  57.523  1.00 29.80 ? 385  LYS B N   1 
ATOM   7374  C  CA  . LYS B  1 368 ? 30.965  44.667  58.323  1.00 32.07 ? 385  LYS B CA  1 
ATOM   7375  C  C   . LYS B  1 368 ? 29.870  44.092  57.420  1.00 30.61 ? 385  LYS B C   1 
ATOM   7376  O  O   . LYS B  1 368 ? 28.734  44.576  57.419  1.00 29.69 ? 385  LYS B O   1 
ATOM   7377  C  CB  . LYS B  1 368 ? 30.451  45.794  59.229  1.00 34.49 ? 385  LYS B CB  1 
ATOM   7378  C  CG  . LYS B  1 368 ? 31.414  46.184  60.341  1.00 37.77 ? 385  LYS B CG  1 
ATOM   7379  C  CD  . LYS B  1 368 ? 30.899  47.288  61.258  1.00 40.37 ? 385  LYS B CD  1 
ATOM   7380  C  CE  . LYS B  1 368 ? 31.624  47.331  62.569  1.00 43.30 ? 385  LYS B CE  1 
ATOM   7381  N  NZ  . LYS B  1 368 ? 33.068  47.521  62.399  1.00 45.29 ? 385  LYS B NZ  1 
ATOM   7382  N  N   . PRO B  1 369 ? 30.170  43.029  56.638  1.00 27.15 ? 386  PRO B N   1 
ATOM   7383  C  CA  . PRO B  1 369 ? 29.160  42.380  55.801  1.00 27.38 ? 386  PRO B CA  1 
ATOM   7384  C  C   . PRO B  1 369 ? 28.163  41.574  56.633  1.00 26.87 ? 386  PRO B C   1 
ATOM   7385  O  O   . PRO B  1 369 ? 28.487  41.102  57.722  1.00 26.26 ? 386  PRO B O   1 
ATOM   7386  C  CB  . PRO B  1 369 ? 30.015  41.487  54.895  1.00 26.66 ? 386  PRO B CB  1 
ATOM   7387  C  CG  . PRO B  1 369 ? 31.165  41.086  55.786  1.00 27.11 ? 386  PRO B CG  1 
ATOM   7388  C  CD  . PRO B  1 369 ? 31.481  42.365  56.551  1.00 27.45 ? 386  PRO B CD  1 
ATOM   7389  N  N   . SER B  1 370 ? 26.950  41.422  56.097  1.00 26.81 ? 387  SER B N   1 
ATOM   7390  C  CA  . SER B  1 370 ? 25.934  40.562  56.684  1.00 26.87 ? 387  SER B CA  1 
ATOM   7391  C  C   . SER B  1 370 ? 26.074  39.118  56.197  1.00 25.86 ? 387  SER B C   1 
ATOM   7392  O  O   . SER B  1 370 ? 25.614  38.192  56.870  1.00 26.18 ? 387  SER B O   1 
ATOM   7393  C  CB  . SER B  1 370 ? 24.560  41.107  56.386  1.00 27.53 ? 387  SER B CB  1 
ATOM   7394  O  OG  . SER B  1 370 ? 24.413  41.402  55.004  1.00 28.79 ? 387  SER B OG  1 
ATOM   7395  N  N   . THR B  1 371 ? 26.678  38.941  55.013  1.00 23.65 ? 388  THR B N   1 
ATOM   7396  C  CA  . THR B  1 371 ? 26.838  37.644  54.375  1.00 22.78 ? 388  THR B CA  1 
ATOM   7397  C  C   . THR B  1 371 ? 28.276  37.525  53.867  1.00 21.03 ? 388  THR B C   1 
ATOM   7398  O  O   . THR B  1 371 ? 28.773  38.464  53.258  1.00 21.50 ? 388  THR B O   1 
ATOM   7399  C  CB  . THR B  1 371 ? 25.839  37.541  53.218  1.00 24.19 ? 388  THR B CB  1 
ATOM   7400  O  OG1 . THR B  1 371 ? 24.508  37.621  53.727  1.00 24.44 ? 388  THR B OG1 1 
ATOM   7401  C  CG2 . THR B  1 371 ? 25.979  36.247  52.435  1.00 23.46 ? 388  THR B CG2 1 
ATOM   7402  N  N   . ILE B  1 372 ? 28.927  36.378  54.096  1.00 19.56 ? 389  ILE B N   1 
ATOM   7403  C  CA  . ILE B  1 372 ? 30.163  36.050  53.399  1.00 20.13 ? 389  ILE B CA  1 
ATOM   7404  C  C   . ILE B  1 372 ? 29.951  34.783  52.572  1.00 19.67 ? 389  ILE B C   1 
ATOM   7405  O  O   . ILE B  1 372 ? 29.298  33.842  53.019  1.00 19.75 ? 389  ILE B O   1 
ATOM   7406  C  CB  . ILE B  1 372 ? 31.370  35.922  54.351  1.00 20.30 ? 389  ILE B CB  1 
ATOM   7407  C  CG1 . ILE B  1 372 ? 31.143  34.885  55.456  1.00 20.89 ? 389  ILE B CG1 1 
ATOM   7408  C  CG2 . ILE B  1 372 ? 31.750  37.287  54.920  1.00 20.33 ? 389  ILE B CG2 1 
ATOM   7409  C  CD1 . ILE B  1 372 ? 32.350  34.660  56.349  1.00 20.66 ? 389  ILE B CD1 1 
ATOM   7410  N  N   . ILE B  1 373 ? 30.491  34.797  51.347  1.00 20.07 ? 390  ILE B N   1 
ATOM   7411  C  CA  . ILE B  1 373 ? 30.374  33.689  50.412  1.00 20.20 ? 390  ILE B CA  1 
ATOM   7412  C  C   . ILE B  1 373 ? 31.778  33.291  49.960  1.00 20.05 ? 390  ILE B C   1 
ATOM   7413  O  O   . ILE B  1 373 ? 32.491  34.096  49.355  1.00 19.41 ? 390  ILE B O   1 
ATOM   7414  C  CB  . ILE B  1 373 ? 29.474  34.055  49.215  1.00 20.88 ? 390  ILE B CB  1 
ATOM   7415  C  CG1 . ILE B  1 373 ? 28.068  34.510  49.657  1.00 21.33 ? 390  ILE B CG1 1 
ATOM   7416  C  CG2 . ILE B  1 373 ? 29.400  32.893  48.219  1.00 20.93 ? 390  ILE B CG2 1 
ATOM   7417  C  CD1 . ILE B  1 373 ? 27.219  35.094  48.538  1.00 21.58 ? 390  ILE B CD1 1 
ATOM   7418  N  N   . GLY B  1 374 ? 32.145  32.037  50.247  1.00 19.38 ? 391  GLY B N   1 
ATOM   7419  C  CA  . GLY B  1 374 ? 33.459  31.500  49.935  1.00 20.32 ? 391  GLY B CA  1 
ATOM   7420  C  C   . GLY B  1 374 ? 33.463  30.712  48.626  1.00 20.97 ? 391  GLY B C   1 
ATOM   7421  O  O   . GLY B  1 374 ? 32.813  29.673  48.512  1.00 21.67 ? 391  GLY B O   1 
ATOM   7422  N  N   . VAL B  1 375 ? 34.219  31.221  47.648  1.00 21.35 ? 392  VAL B N   1 
ATOM   7423  C  CA  . VAL B  1 375 ? 34.379  30.574  46.356  1.00 22.84 ? 392  VAL B CA  1 
ATOM   7424  C  C   . VAL B  1 375 ? 35.808  30.801  45.860  1.00 22.78 ? 392  VAL B C   1 
ATOM   7425  O  O   . VAL B  1 375 ? 36.012  31.245  44.734  1.00 23.29 ? 392  VAL B O   1 
ATOM   7426  C  CB  . VAL B  1 375 ? 33.335  31.104  45.353  1.00 22.91 ? 392  VAL B CB  1 
ATOM   7427  C  CG1 . VAL B  1 375 ? 31.949  30.521  45.605  1.00 23.60 ? 392  VAL B CG1 1 
ATOM   7428  C  CG2 . VAL B  1 375 ? 33.271  32.625  45.342  1.00 23.69 ? 392  VAL B CG2 1 
ATOM   7429  N  N   . ALA B  1 376 ? 36.795  30.489  46.710  1.00 23.64 ? 393  ALA B N   1 
ATOM   7430  C  CA  . ALA B  1 376 ? 38.196  30.748  46.396  1.00 23.99 ? 393  ALA B CA  1 
ATOM   7431  C  C   . ALA B  1 376 ? 38.949  29.478  46.000  1.00 25.41 ? 393  ALA B C   1 
ATOM   7432  O  O   . ALA B  1 376 ? 40.017  29.568  45.400  1.00 25.50 ? 393  ALA B O   1 
ATOM   7433  C  CB  . ALA B  1 376 ? 38.865  31.427  47.567  1.00 24.25 ? 393  ALA B CB  1 
ATOM   7434  N  N   . GLY B  1 377 ? 38.412  28.305  46.355  1.00 27.24 ? 394  GLY B N   1 
ATOM   7435  C  CA  . GLY B  1 377 ? 39.031  27.027  46.029  1.00 28.98 ? 394  GLY B CA  1 
ATOM   7436  C  C   . GLY B  1 377 ? 40.424  26.870  46.639  1.00 31.77 ? 394  GLY B C   1 
ATOM   7437  O  O   . GLY B  1 377 ? 41.290  26.214  46.052  1.00 31.78 ? 394  GLY B O   1 
ATOM   7438  N  N   . ALA B  1 378 ? 40.626  27.446  47.833  1.00 31.34 ? 395  ALA B N   1 
ATOM   7439  C  CA  . ALA B  1 378 ? 41.967  27.606  48.373  1.00 31.92 ? 395  ALA B CA  1 
ATOM   7440  C  C   . ALA B  1 378 ? 42.043  27.219  49.850  1.00 33.05 ? 395  ALA B C   1 
ATOM   7441  O  O   . ALA B  1 378 ? 42.984  27.616  50.534  1.00 35.44 ? 395  ALA B O   1 
ATOM   7442  C  CB  . ALA B  1 378 ? 42.412  29.034  48.152  1.00 31.46 ? 395  ALA B CB  1 
ATOM   7443  N  N   . GLY B  1 379 ? 41.062  26.451  50.340  1.00 33.02 ? 396  GLY B N   1 
ATOM   7444  C  CA  . GLY B  1 379 ? 41.134  25.882  51.676  1.00 32.23 ? 396  GLY B CA  1 
ATOM   7445  C  C   . GLY B  1 379 ? 40.418  26.730  52.725  1.00 32.02 ? 396  GLY B C   1 
ATOM   7446  O  O   . GLY B  1 379 ? 39.586  27.579  52.399  1.00 29.89 ? 396  GLY B O   1 
ATOM   7447  N  N   . ARG B  1 380 ? 40.793  26.497  53.991  1.00 31.15 ? 397  ARG B N   1 
ATOM   7448  C  CA  . ARG B  1 380 ? 40.023  26.916  55.152  1.00 30.67 ? 397  ARG B CA  1 
ATOM   7449  C  C   . ARG B  1 380 ? 40.295  28.379  55.491  1.00 30.94 ? 397  ARG B C   1 
ATOM   7450  O  O   . ARG B  1 380 ? 40.840  28.689  56.549  1.00 31.34 ? 397  ARG B O   1 
ATOM   7451  C  CB  . ARG B  1 380 ? 40.398  26.009  56.331  1.00 31.86 ? 397  ARG B CB  1 
ATOM   7452  C  CG  . ARG B  1 380 ? 39.997  24.549  56.183  1.00 32.87 ? 397  ARG B CG  1 
ATOM   7453  C  CD  . ARG B  1 380 ? 38.543  24.326  56.571  1.00 35.32 ? 397  ARG B CD  1 
ATOM   7454  N  NE  . ARG B  1 380 ? 38.200  22.901  56.637  1.00 36.78 ? 397  ARG B NE  1 
ATOM   7455  C  CZ  . ARG B  1 380 ? 37.931  22.094  55.616  1.00 38.07 ? 397  ARG B CZ  1 
ATOM   7456  N  NH1 . ARG B  1 380 ? 37.820  22.570  54.385  1.00 39.55 ? 397  ARG B NH1 1 
ATOM   7457  N  NH2 . ARG B  1 380 ? 37.738  20.805  55.838  1.00 37.54 ? 397  ARG B NH2 1 
ATOM   7458  N  N   . LEU B  1 381 ? 39.863  29.285  54.610  1.00 29.73 ? 398  LEU B N   1 
ATOM   7459  C  CA  . LEU B  1 381 ? 40.196  30.694  54.741  1.00 28.87 ? 398  LEU B CA  1 
ATOM   7460  C  C   . LEU B  1 381 ? 39.129  31.434  55.546  1.00 27.62 ? 398  LEU B C   1 
ATOM   7461  O  O   . LEU B  1 381 ? 39.326  32.601  55.881  1.00 27.71 ? 398  LEU B O   1 
ATOM   7462  C  CB  . LEU B  1 381 ? 40.396  31.295  53.350  1.00 30.81 ? 398  LEU B CB  1 
ATOM   7463  C  CG  . LEU B  1 381 ? 41.552  30.714  52.524  1.00 32.57 ? 398  LEU B CG  1 
ATOM   7464  C  CD1 . LEU B  1 381 ? 41.472  31.177  51.078  1.00 33.15 ? 398  LEU B CD1 1 
ATOM   7465  C  CD2 . LEU B  1 381 ? 42.909  31.075  53.105  1.00 33.50 ? 398  LEU B CD2 1 
ATOM   7466  N  N   . PHE B  1 382 ? 37.999  30.773  55.844  1.00 27.07 ? 399  PHE B N   1 
ATOM   7467  C  CA  . PHE B  1 382 ? 37.082  31.276  56.859  1.00 26.27 ? 399  PHE B CA  1 
ATOM   7468  C  C   . PHE B  1 382 ? 37.567  30.742  58.207  1.00 27.58 ? 399  PHE B C   1 
ATOM   7469  O  O   . PHE B  1 382 ? 37.056  29.744  58.716  1.00 26.71 ? 399  PHE B O   1 
ATOM   7470  C  CB  . PHE B  1 382 ? 35.601  30.934  56.656  1.00 24.66 ? 399  PHE B CB  1 
ATOM   7471  C  CG  . PHE B  1 382 ? 34.914  31.564  55.449  1.00 23.57 ? 399  PHE B CG  1 
ATOM   7472  C  CD1 . PHE B  1 382 ? 35.525  32.566  54.699  1.00 22.32 ? 399  PHE B CD1 1 
ATOM   7473  C  CD2 . PHE B  1 382 ? 33.637  31.156  55.075  1.00 23.03 ? 399  PHE B CD2 1 
ATOM   7474  C  CE1 . PHE B  1 382 ? 34.882  33.124  53.605  1.00 22.96 ? 399  PHE B CE1 1 
ATOM   7475  C  CE2 . PHE B  1 382 ? 33.001  31.717  53.978  1.00 22.19 ? 399  PHE B CE2 1 
ATOM   7476  C  CZ  . PHE B  1 382 ? 33.620  32.699  53.246  1.00 22.17 ? 399  PHE B CZ  1 
ATOM   7477  N  N   . THR B  1 383 ? 38.562  31.440  58.765  1.00 28.26 ? 400  THR B N   1 
ATOM   7478  C  CA  . THR B  1 383 ? 39.232  31.021  59.985  1.00 27.70 ? 400  THR B CA  1 
ATOM   7479  C  C   . THR B  1 383 ? 38.311  31.241  61.182  1.00 27.94 ? 400  THR B C   1 
ATOM   7480  O  O   . THR B  1 383 ? 37.356  32.022  61.110  1.00 26.84 ? 400  THR B O   1 
ATOM   7481  C  CB  . THR B  1 383 ? 40.533  31.802  60.146  1.00 27.91 ? 400  THR B CB  1 
ATOM   7482  O  OG1 . THR B  1 383 ? 40.124  33.154  60.340  1.00 29.41 ? 400  THR B OG1 1 
ATOM   7483  C  CG2 . THR B  1 383 ? 41.468  31.649  58.959  1.00 27.78 ? 400  THR B CG2 1 
ATOM   7484  N  N   . PRO B  1 384 ? 38.590  30.587  62.335  1.00 28.48 ? 401  PRO B N   1 
ATOM   7485  C  CA  . PRO B  1 384 ? 37.847  30.862  63.565  1.00 27.72 ? 401  PRO B CA  1 
ATOM   7486  C  C   . PRO B  1 384 ? 37.686  32.354  63.846  1.00 28.12 ? 401  PRO B C   1 
ATOM   7487  O  O   . PRO B  1 384 ? 36.623  32.790  64.283  1.00 27.65 ? 401  PRO B O   1 
ATOM   7488  C  CB  . PRO B  1 384 ? 38.676  30.138  64.634  1.00 28.45 ? 401  PRO B CB  1 
ATOM   7489  C  CG  . PRO B  1 384 ? 39.309  28.985  63.890  1.00 28.70 ? 401  PRO B CG  1 
ATOM   7490  C  CD  . PRO B  1 384 ? 39.597  29.524  62.499  1.00 28.53 ? 401  PRO B CD  1 
ATOM   7491  N  N   . ASP B  1 385 ? 38.737  33.138  63.574  1.00 28.00 ? 402  ASP B N   1 
ATOM   7492  C  CA  . ASP B  1 385 ? 38.682  34.579  63.774  1.00 29.03 ? 402  ASP B CA  1 
ATOM   7493  C  C   . ASP B  1 385 ? 37.693  35.227  62.803  1.00 26.59 ? 402  ASP B C   1 
ATOM   7494  O  O   . ASP B  1 385 ? 36.996  36.175  63.171  1.00 24.88 ? 402  ASP B O   1 
ATOM   7495  C  CB  . ASP B  1 385 ? 40.061  35.216  63.677  1.00 31.79 ? 402  ASP B CB  1 
ATOM   7496  C  CG  . ASP B  1 385 ? 40.989  34.938  64.854  1.00 36.15 ? 402  ASP B CG  1 
ATOM   7497  O  OD1 . ASP B  1 385 ? 40.496  34.947  66.004  1.00 37.91 ? 402  ASP B OD1 1 
ATOM   7498  O  OD2 . ASP B  1 385 ? 42.200  34.739  64.615  1.00 38.32 ? 402  ASP B OD2 1 
ATOM   7499  N  N   . VAL B  1 386 ? 37.651  34.734  61.558  1.00 25.45 ? 403  VAL B N   1 
ATOM   7500  C  CA  . VAL B  1 386 ? 36.702  35.237  60.572  1.00 25.99 ? 403  VAL B CA  1 
ATOM   7501  C  C   . VAL B  1 386 ? 35.271  34.972  61.051  1.00 24.86 ? 403  VAL B C   1 
ATOM   7502  O  O   . VAL B  1 386 ? 34.420  35.860  60.994  1.00 23.47 ? 403  VAL B O   1 
ATOM   7503  C  CB  . VAL B  1 386 ? 36.956  34.636  59.172  1.00 26.18 ? 403  VAL B CB  1 
ATOM   7504  C  CG1 . VAL B  1 386 ? 35.776  34.847  58.226  1.00 25.83 ? 403  VAL B CG1 1 
ATOM   7505  C  CG2 . VAL B  1 386 ? 38.233  35.199  58.552  1.00 25.81 ? 403  VAL B CG2 1 
ATOM   7506  N  N   . ILE B  1 387 ? 35.013  33.749  61.524  1.00 25.40 ? 404  ILE B N   1 
ATOM   7507  C  CA  . ILE B  1 387 ? 33.664  33.348  61.902  1.00 28.20 ? 404  ILE B CA  1 
ATOM   7508  C  C   . ILE B  1 387 ? 33.224  34.108  63.155  1.00 28.24 ? 404  ILE B C   1 
ATOM   7509  O  O   . ILE B  1 387 ? 32.115  34.639  63.201  1.00 27.28 ? 404  ILE B O   1 
ATOM   7510  C  CB  . ILE B  1 387 ? 33.577  31.822  62.078  1.00 29.26 ? 404  ILE B CB  1 
ATOM   7511  C  CG1 . ILE B  1 387 ? 33.887  31.099  60.764  1.00 29.65 ? 404  ILE B CG1 1 
ATOM   7512  C  CG2 . ILE B  1 387 ? 32.209  31.411  62.633  1.00 29.91 ? 404  ILE B CG2 1 
ATOM   7513  C  CD1 . ILE B  1 387 ? 34.104  29.606  60.905  1.00 30.21 ? 404  ILE B CD1 1 
ATOM   7514  N  N   . ARG B  1 388 ? 34.110  34.182  64.157  1.00 28.65 ? 405  ARG B N   1 
ATOM   7515  C  CA  . ARG B  1 388 ? 33.820  34.930  65.372  1.00 29.69 ? 405  ARG B CA  1 
ATOM   7516  C  C   . ARG B  1 388 ? 33.499  36.387  65.034  1.00 28.56 ? 405  ARG B C   1 
ATOM   7517  O  O   . ARG B  1 388 ? 32.553  36.948  65.582  1.00 28.80 ? 405  ARG B O   1 
ATOM   7518  C  CB  . ARG B  1 388 ? 34.948  34.774  66.401  1.00 30.94 ? 405  ARG B CB  1 
ATOM   7519  C  CG  . ARG B  1 388 ? 34.906  33.451  67.154  1.00 31.18 ? 405  ARG B CG  1 
ATOM   7520  C  CD  . ARG B  1 388 ? 35.860  33.427  68.338  1.00 31.59 ? 405  ARG B CD  1 
ATOM   7521  N  NE  . ARG B  1 388 ? 37.260  33.351  67.910  1.00 31.92 ? 405  ARG B NE  1 
ATOM   7522  C  CZ  . ARG B  1 388 ? 38.019  32.258  67.909  1.00 33.81 ? 405  ARG B CZ  1 
ATOM   7523  N  NH1 . ARG B  1 388 ? 37.562  31.107  68.380  1.00 33.99 ? 405  ARG B NH1 1 
ATOM   7524  N  NH2 . ARG B  1 388 ? 39.249  32.318  67.426  1.00 35.13 ? 405  ARG B NH2 1 
ATOM   7525  N  N   . ALA B  1 389 ? 34.260  36.990  64.111  1.00 28.18 ? 406  ALA B N   1 
ATOM   7526  C  CA  . ALA B  1 389 ? 34.008  38.365  63.705  1.00 27.75 ? 406  ALA B CA  1 
ATOM   7527  C  C   . ALA B  1 389 ? 32.590  38.515  63.150  1.00 28.44 ? 406  ALA B C   1 
ATOM   7528  O  O   . ALA B  1 389 ? 31.881  39.452  63.515  1.00 28.25 ? 406  ALA B O   1 
ATOM   7529  C  CB  . ALA B  1 389 ? 35.046  38.813  62.699  1.00 28.00 ? 406  ALA B CB  1 
ATOM   7530  N  N   . MET B  1 390 ? 32.182  37.595  62.261  1.00 27.52 ? 407  MET B N   1 
ATOM   7531  C  CA  . MET B  1 390 ? 30.849  37.630  61.679  1.00 28.02 ? 407  MET B CA  1 
ATOM   7532  C  C   . MET B  1 390 ? 29.777  37.544  62.769  1.00 28.45 ? 407  MET B C   1 
ATOM   7533  O  O   . MET B  1 390 ? 28.761  38.233  62.686  1.00 29.33 ? 407  MET B O   1 
ATOM   7534  C  CB  . MET B  1 390 ? 30.660  36.495  60.662  1.00 28.12 ? 407  MET B CB  1 
ATOM   7535  C  CG  . MET B  1 390 ? 31.361  36.734  59.334  1.00 27.78 ? 407  MET B CG  1 
ATOM   7536  S  SD  . MET B  1 390 ? 30.712  38.154  58.435  1.00 28.40 ? 407  MET B SD  1 
ATOM   7537  C  CE  . MET B  1 390 ? 29.071  37.557  58.002  1.00 29.57 ? 407  MET B CE  1 
ATOM   7538  N  N   . ALA B  1 391 ? 30.014  36.711  63.790  1.00 29.85 ? 408  ALA B N   1 
ATOM   7539  C  CA  . ALA B  1 391 ? 29.054  36.505  64.869  1.00 31.45 ? 408  ALA B CA  1 
ATOM   7540  C  C   . ALA B  1 391 ? 29.028  37.697  65.827  1.00 34.20 ? 408  ALA B C   1 
ATOM   7541  O  O   . ALA B  1 391 ? 28.020  37.930  66.489  1.00 33.98 ? 408  ALA B O   1 
ATOM   7542  C  CB  . ALA B  1 391 ? 29.373  35.225  65.610  1.00 30.81 ? 408  ALA B CB  1 
ATOM   7543  N  N   . SER B  1 392 ? 30.139  38.441  65.903  1.00 35.15 ? 409  SER B N   1 
ATOM   7544  C  CA  . SER B  1 392 ? 30.210  39.655  66.702  1.00 35.71 ? 409  SER B CA  1 
ATOM   7545  C  C   . SER B  1 392 ? 29.474  40.795  65.999  1.00 35.21 ? 409  SER B C   1 
ATOM   7546  O  O   . SER B  1 392 ? 28.763  41.566  66.643  1.00 34.52 ? 409  SER B O   1 
ATOM   7547  C  CB  . SER B  1 392 ? 31.657  40.011  67.005  1.00 38.05 ? 409  SER B CB  1 
ATOM   7548  O  OG  . SER B  1 392 ? 31.785  41.338  67.495  1.00 39.19 ? 409  SER B OG  1 
ATOM   7549  N  N   . ILE B  1 393 ? 29.637  40.879  64.671  1.00 33.38 ? 410  ILE B N   1 
ATOM   7550  C  CA  . ILE B  1 393 ? 29.090  41.964  63.868  1.00 33.52 ? 410  ILE B CA  1 
ATOM   7551  C  C   . ILE B  1 393 ? 27.588  41.776  63.651  1.00 33.41 ? 410  ILE B C   1 
ATOM   7552  O  O   . ILE B  1 393 ? 26.850  42.758  63.626  1.00 33.73 ? 410  ILE B O   1 
ATOM   7553  C  CB  . ILE B  1 393 ? 29.848  42.070  62.527  1.00 34.72 ? 410  ILE B CB  1 
ATOM   7554  C  CG1 . ILE B  1 393 ? 31.304  42.511  62.742  1.00 35.38 ? 410  ILE B CG1 1 
ATOM   7555  C  CG2 . ILE B  1 393 ? 29.128  42.995  61.543  1.00 34.63 ? 410  ILE B CG2 1 
ATOM   7556  C  CD1 . ILE B  1 393 ? 32.207  42.286  61.540  1.00 35.93 ? 410  ILE B CD1 1 
ATOM   7557  N  N   . ASN B  1 394 ? 27.145  40.524  63.458  1.00 32.25 ? 411  ASN B N   1 
ATOM   7558  C  CA  . ASN B  1 394 ? 25.769  40.237  63.078  1.00 32.08 ? 411  ASN B CA  1 
ATOM   7559  C  C   . ASN B  1 394 ? 25.106  39.343  64.123  1.00 32.55 ? 411  ASN B C   1 
ATOM   7560  O  O   . ASN B  1 394 ? 25.732  38.421  64.636  1.00 31.34 ? 411  ASN B O   1 
ATOM   7561  C  CB  . ASN B  1 394 ? 25.688  39.532  61.724  1.00 30.96 ? 411  ASN B CB  1 
ATOM   7562  C  CG  . ASN B  1 394 ? 26.415  40.285  60.635  1.00 28.40 ? 411  ASN B CG  1 
ATOM   7563  O  OD1 . ASN B  1 394 ? 25.898  41.272  60.109  1.00 26.83 ? 411  ASN B OD1 1 
ATOM   7564  N  ND2 . ASN B  1 394 ? 27.612  39.840  60.282  1.00 27.90 ? 411  ASN B ND2 1 
ATOM   7565  N  N   . GLU B  1 395 ? 23.815  39.582  64.384  1.00 34.78 ? 412  GLU B N   1 
ATOM   7566  C  CA  . GLU B  1 395 ? 23.044  38.700  65.248  1.00 36.97 ? 412  GLU B CA  1 
ATOM   7567  C  C   . GLU B  1 395 ? 22.874  37.340  64.568  1.00 34.36 ? 412  GLU B C   1 
ATOM   7568  O  O   . GLU B  1 395 ? 23.039  36.303  65.209  1.00 30.69 ? 412  GLU B O   1 
ATOM   7569  C  CB  . GLU B  1 395 ? 21.701  39.336  65.611  1.00 41.00 ? 412  GLU B CB  1 
ATOM   7570  C  CG  . GLU B  1 395 ? 20.946  38.594  66.713  1.00 46.18 ? 412  GLU B CG  1 
ATOM   7571  C  CD  . GLU B  1 395 ? 21.672  38.498  68.048  1.00 51.17 ? 412  GLU B CD  1 
ATOM   7572  O  OE1 . GLU B  1 395 ? 22.157  39.543  68.540  1.00 54.03 ? 412  GLU B OE1 1 
ATOM   7573  O  OE2 . GLU B  1 395 ? 21.747  37.378  68.602  1.00 52.98 ? 412  GLU B OE2 1 
ATOM   7574  N  N   . ARG B  1 396 ? 22.546  37.354  63.266  1.00 33.36 ? 413  ARG B N   1 
ATOM   7575  C  CA  . ARG B  1 396 ? 22.383  36.133  62.490  1.00 32.44 ? 413  ARG B CA  1 
ATOM   7576  C  C   . ARG B  1 396 ? 23.268  36.204  61.245  1.00 31.66 ? 413  ARG B C   1 
ATOM   7577  O  O   . ARG B  1 396 ? 22.791  36.558  60.169  1.00 32.16 ? 413  ARG B O   1 
ATOM   7578  C  CB  . ARG B  1 396 ? 20.917  35.941  62.081  1.00 33.88 ? 413  ARG B CB  1 
ATOM   7579  C  CG  . ARG B  1 396 ? 19.903  35.936  63.220  1.00 34.94 ? 413  ARG B CG  1 
ATOM   7580  C  CD  . ARG B  1 396 ? 20.173  34.855  64.250  1.00 35.18 ? 413  ARG B CD  1 
ATOM   7581  N  NE  . ARG B  1 396 ? 20.136  33.492  63.707  1.00 35.88 ? 413  ARG B NE  1 
ATOM   7582  C  CZ  . ARG B  1 396 ? 19.036  32.791  63.418  1.00 37.69 ? 413  ARG B CZ  1 
ATOM   7583  N  NH1 . ARG B  1 396 ? 17.835  33.333  63.529  1.00 38.04 ? 413  ARG B NH1 1 
ATOM   7584  N  NH2 . ARG B  1 396 ? 19.142  31.536  63.012  1.00 37.61 ? 413  ARG B NH2 1 
ATOM   7585  N  N   . PRO B  1 397 ? 24.579  35.874  61.337  1.00 29.58 ? 414  PRO B N   1 
ATOM   7586  C  CA  . PRO B  1 397 ? 25.465  35.942  60.173  1.00 28.38 ? 414  PRO B CA  1 
ATOM   7587  C  C   . PRO B  1 397 ? 25.160  34.832  59.169  1.00 26.32 ? 414  PRO B C   1 
ATOM   7588  O  O   . PRO B  1 397 ? 24.899  33.698  59.560  1.00 26.51 ? 414  PRO B O   1 
ATOM   7589  C  CB  . PRO B  1 397 ? 26.856  35.790  60.800  1.00 28.51 ? 414  PRO B CB  1 
ATOM   7590  C  CG  . PRO B  1 397 ? 26.609  34.912  62.007  1.00 27.92 ? 414  PRO B CG  1 
ATOM   7591  C  CD  . PRO B  1 397 ? 25.271  35.394  62.544  1.00 28.74 ? 414  PRO B CD  1 
ATOM   7592  N  N   . VAL B  1 398 ? 25.200  35.173  57.875  1.00 26.10 ? 415  VAL B N   1 
ATOM   7593  C  CA  . VAL B  1 398 ? 25.050  34.190  56.811  1.00 24.46 ? 415  VAL B CA  1 
ATOM   7594  C  C   . VAL B  1 398 ? 26.437  33.836  56.280  1.00 23.14 ? 415  VAL B C   1 
ATOM   7595  O  O   . VAL B  1 398 ? 27.163  34.709  55.810  1.00 23.46 ? 415  VAL B O   1 
ATOM   7596  C  CB  . VAL B  1 398 ? 24.135  34.732  55.700  1.00 24.92 ? 415  VAL B CB  1 
ATOM   7597  C  CG1 . VAL B  1 398 ? 23.985  33.737  54.553  1.00 25.04 ? 415  VAL B CG1 1 
ATOM   7598  C  CG2 . VAL B  1 398 ? 22.770  35.135  56.248  1.00 25.27 ? 415  VAL B CG2 1 
ATOM   7599  N  N   . ILE B  1 399 ? 26.789  32.551  56.374  1.00 23.06 ? 416  ILE B N   1 
ATOM   7600  C  CA  . ILE B  1 399 ? 28.109  32.053  56.024  1.00 22.61 ? 416  ILE B CA  1 
ATOM   7601  C  C   . ILE B  1 399 ? 27.940  30.908  55.026  1.00 23.45 ? 416  ILE B C   1 
ATOM   7602  O  O   . ILE B  1 399 ? 27.499  29.826  55.410  1.00 24.12 ? 416  ILE B O   1 
ATOM   7603  C  CB  . ILE B  1 399 ? 28.867  31.591  57.287  1.00 22.62 ? 416  ILE B CB  1 
ATOM   7604  C  CG1 . ILE B  1 399 ? 29.031  32.725  58.309  1.00 22.72 ? 416  ILE B CG1 1 
ATOM   7605  C  CG2 . ILE B  1 399 ? 30.214  30.964  56.920  1.00 23.05 ? 416  ILE B CG2 1 
ATOM   7606  C  CD1 . ILE B  1 399 ? 29.594  32.283  59.648  1.00 23.93 ? 416  ILE B CD1 1 
ATOM   7607  N  N   . PHE B  1 400 ? 28.301  31.152  53.755  1.00 23.02 ? 417  PHE B N   1 
ATOM   7608  C  CA  . PHE B  1 400 ? 28.283  30.130  52.714  1.00 22.45 ? 417  PHE B CA  1 
ATOM   7609  C  C   . PHE B  1 400 ? 29.718  29.771  52.320  1.00 22.31 ? 417  PHE B C   1 
ATOM   7610  O  O   . PHE B  1 400 ? 30.457  30.620  51.820  1.00 21.75 ? 417  PHE B O   1 
ATOM   7611  C  CB  . PHE B  1 400 ? 27.504  30.616  51.485  1.00 23.47 ? 417  PHE B CB  1 
ATOM   7612  C  CG  . PHE B  1 400 ? 25.979  30.584  51.559  1.00 23.80 ? 417  PHE B CG  1 
ATOM   7613  C  CD1 . PHE B  1 400 ? 25.300  30.696  52.771  1.00 24.79 ? 417  PHE B CD1 1 
ATOM   7614  C  CD2 . PHE B  1 400 ? 25.220  30.445  50.399  1.00 24.86 ? 417  PHE B CD2 1 
ATOM   7615  C  CE1 . PHE B  1 400 ? 23.911  30.669  52.820  1.00 24.85 ? 417  PHE B CE1 1 
ATOM   7616  C  CE2 . PHE B  1 400 ? 23.830  30.419  50.454  1.00 24.42 ? 417  PHE B CE2 1 
ATOM   7617  C  CZ  . PHE B  1 400 ? 23.180  30.525  51.664  1.00 25.12 ? 417  PHE B CZ  1 
ATOM   7618  N  N   . ALA B  1 401 ? 30.094  28.504  52.531  1.00 22.38 ? 418  ALA B N   1 
ATOM   7619  C  CA  . ALA B  1 401 ? 31.395  27.979  52.136  1.00 24.46 ? 418  ALA B CA  1 
ATOM   7620  C  C   . ALA B  1 401 ? 31.238  27.002  50.969  1.00 25.41 ? 418  ALA B C   1 
ATOM   7621  O  O   . ALA B  1 401 ? 31.011  25.813  51.180  1.00 25.58 ? 418  ALA B O   1 
ATOM   7622  C  CB  . ALA B  1 401 ? 32.044  27.310  53.329  1.00 24.50 ? 418  ALA B CB  1 
ATOM   7623  N  N   . LEU B  1 402 ? 31.413  27.495  49.733  1.00 26.38 ? 419  LEU B N   1 
ATOM   7624  C  CA  . LEU B  1 402 ? 30.969  26.775  48.548  1.00 25.71 ? 419  LEU B CA  1 
ATOM   7625  C  C   . LEU B  1 402 ? 32.118  26.089  47.812  1.00 27.87 ? 419  LEU B C   1 
ATOM   7626  O  O   . LEU B  1 402 ? 31.871  25.425  46.811  1.00 31.45 ? 419  LEU B O   1 
ATOM   7627  C  CB  . LEU B  1 402 ? 30.240  27.735  47.607  1.00 25.30 ? 419  LEU B CB  1 
ATOM   7628  C  CG  . LEU B  1 402 ? 29.004  28.444  48.167  1.00 25.36 ? 419  LEU B CG  1 
ATOM   7629  C  CD1 . LEU B  1 402 ? 28.324  29.283  47.091  1.00 25.55 ? 419  LEU B CD1 1 
ATOM   7630  C  CD2 . LEU B  1 402 ? 28.008  27.470  48.762  1.00 26.96 ? 419  LEU B CD2 1 
ATOM   7631  N  N   . SER B  1 403 ? 33.363  26.238  48.273  1.00 29.03 ? 420  SER B N   1 
ATOM   7632  C  CA  . SER B  1 403 ? 34.497  25.714  47.523  1.00 30.31 ? 420  SER B CA  1 
ATOM   7633  C  C   . SER B  1 403 ? 34.531  24.183  47.582  1.00 32.42 ? 420  SER B C   1 
ATOM   7634  O  O   . SER B  1 403 ? 34.083  23.590  48.558  1.00 31.28 ? 420  SER B O   1 
ATOM   7635  C  CB  . SER B  1 403 ? 35.789  26.322  47.990  1.00 30.03 ? 420  SER B CB  1 
ATOM   7636  O  OG  . SER B  1 403 ? 35.889  27.669  47.548  1.00 27.38 ? 420  SER B OG  1 
ATOM   7637  N  N   . ASN B  1 404 ? 35.060  23.565  46.514  1.00 36.70 ? 421  ASN B N   1 
ATOM   7638  C  CA  . ASN B  1 404 ? 35.145  22.118  46.360  1.00 40.99 ? 421  ASN B CA  1 
ATOM   7639  C  C   . ASN B  1 404 ? 36.568  21.711  45.977  1.00 41.08 ? 421  ASN B C   1 
ATOM   7640  O  O   . ASN B  1 404 ? 37.279  22.493  45.348  1.00 41.07 ? 421  ASN B O   1 
ATOM   7641  C  CB  . ASN B  1 404 ? 34.210  21.596  45.274  1.00 43.35 ? 421  ASN B CB  1 
ATOM   7642  C  CG  . ASN B  1 404 ? 32.767  21.965  45.514  1.00 46.61 ? 421  ASN B CG  1 
ATOM   7643  O  OD1 . ASN B  1 404 ? 32.175  22.693  44.710  1.00 53.36 ? 421  ASN B OD1 1 
ATOM   7644  N  ND2 . ASN B  1 404 ? 32.181  21.477  46.596  1.00 48.52 ? 421  ASN B ND2 1 
ATOM   7645  N  N   . PRO B  1 405 ? 37.035  20.482  46.312  1.00 42.20 ? 422  PRO B N   1 
ATOM   7646  C  CA  . PRO B  1 405 ? 36.290  19.534  47.148  1.00 41.97 ? 422  PRO B CA  1 
ATOM   7647  C  C   . PRO B  1 405 ? 36.365  19.898  48.632  1.00 40.39 ? 422  PRO B C   1 
ATOM   7648  O  O   . PRO B  1 405 ? 36.809  20.990  48.972  1.00 38.85 ? 422  PRO B O   1 
ATOM   7649  C  CB  . PRO B  1 405 ? 36.984  18.198  46.809  1.00 42.41 ? 422  PRO B CB  1 
ATOM   7650  C  CG  . PRO B  1 405 ? 38.422  18.589  46.567  1.00 42.43 ? 422  PRO B CG  1 
ATOM   7651  C  CD  . PRO B  1 405 ? 38.330  19.937  45.868  1.00 42.41 ? 422  PRO B CD  1 
ATOM   7652  N  N   . THR B  1 406 ? 35.935  18.979  49.509  1.00 41.52 ? 423  THR B N   1 
ATOM   7653  C  CA  . THR B  1 406 ? 35.727  19.273  50.923  1.00 41.03 ? 423  THR B CA  1 
ATOM   7654  C  C   . THR B  1 406 ? 36.974  19.907  51.543  1.00 40.30 ? 423  THR B C   1 
ATOM   7655  O  O   . THR B  1 406 ? 36.862  20.835  52.342  1.00 36.45 ? 423  THR B O   1 
ATOM   7656  C  CB  . THR B  1 406 ? 35.317  17.999  51.661  1.00 42.40 ? 423  THR B CB  1 
ATOM   7657  O  OG1 . THR B  1 406 ? 34.195  17.481  50.953  1.00 43.63 ? 423  THR B OG1 1 
ATOM   7658  C  CG2 . THR B  1 406 ? 34.915  18.258  53.101  1.00 43.51 ? 423  THR B CG2 1 
ATOM   7659  N  N   . ALA B  1 407 ? 38.158  19.416  51.157  1.00 41.30 ? 424  ALA B N   1 
ATOM   7660  C  CA  . ALA B  1 407 ? 39.420  19.914  51.685  1.00 43.33 ? 424  ALA B CA  1 
ATOM   7661  C  C   . ALA B  1 407 ? 39.639  21.390  51.343  1.00 42.31 ? 424  ALA B C   1 
ATOM   7662  O  O   . ALA B  1 407 ? 40.375  22.073  52.054  1.00 44.57 ? 424  ALA B O   1 
ATOM   7663  C  CB  . ALA B  1 407 ? 40.565  19.067  51.167  1.00 43.99 ? 424  ALA B CB  1 
ATOM   7664  N  N   . GLN B  1 408 ? 39.022  21.875  50.254  1.00 39.20 ? 425  GLN B N   1 
ATOM   7665  C  CA  . GLN B  1 408 ? 39.205  23.253  49.816  1.00 39.68 ? 425  GLN B CA  1 
ATOM   7666  C  C   . GLN B  1 408 ? 38.120  24.170  50.383  1.00 35.25 ? 425  GLN B C   1 
ATOM   7667  O  O   . GLN B  1 408 ? 38.144  25.371  50.126  1.00 33.65 ? 425  GLN B O   1 
ATOM   7668  C  CB  . GLN B  1 408 ? 39.222  23.375  48.289  1.00 42.78 ? 425  GLN B CB  1 
ATOM   7669  C  CG  . GLN B  1 408 ? 40.372  22.637  47.608  1.00 46.12 ? 425  GLN B CG  1 
ATOM   7670  C  CD  . GLN B  1 408 ? 41.732  22.988  48.174  1.00 50.13 ? 425  GLN B CD  1 
ATOM   7671  O  OE1 . GLN B  1 408 ? 42.125  24.159  48.239  1.00 53.86 ? 425  GLN B OE1 1 
ATOM   7672  N  NE2 . GLN B  1 408 ? 42.464  21.971  48.608  1.00 51.62 ? 425  GLN B NE2 1 
ATOM   7673  N  N   . ALA B  1 409 ? 37.180  23.614  51.158  1.00 33.50 ? 426  ALA B N   1 
ATOM   7674  C  CA  . ALA B  1 409 ? 36.067  24.385  51.693  1.00 31.44 ? 426  ALA B CA  1 
ATOM   7675  C  C   . ALA B  1 409 ? 36.575  25.397  52.721  1.00 29.61 ? 426  ALA B C   1 
ATOM   7676  O  O   . ALA B  1 409 ? 37.542  25.135  53.427  1.00 29.19 ? 426  ALA B O   1 
ATOM   7677  C  CB  . ALA B  1 409 ? 35.026  23.456  52.286  1.00 31.06 ? 426  ALA B CB  1 
ATOM   7678  N  N   . GLU B  1 410 ? 35.902  26.551  52.800  1.00 27.35 ? 427  GLU B N   1 
ATOM   7679  C  CA  . GLU B  1 410 ? 36.377  27.677  53.588  1.00 27.12 ? 427  GLU B CA  1 
ATOM   7680  C  C   . GLU B  1 410 ? 36.252  27.385  55.083  1.00 27.11 ? 427  GLU B C   1 
ATOM   7681  O  O   . GLU B  1 410 ? 37.049  27.891  55.872  1.00 25.79 ? 427  GLU B O   1 
ATOM   7682  C  CB  . GLU B  1 410 ? 35.651  28.970  53.207  1.00 26.13 ? 427  GLU B CB  1 
ATOM   7683  C  CG  . GLU B  1 410 ? 36.111  29.548  51.870  1.00 26.60 ? 427  GLU B CG  1 
ATOM   7684  C  CD  . GLU B  1 410 ? 35.623  28.851  50.606  1.00 26.49 ? 427  GLU B CD  1 
ATOM   7685  O  OE1 . GLU B  1 410 ? 34.709  27.992  50.672  1.00 25.94 ? 427  GLU B OE1 1 
ATOM   7686  O  OE2 . GLU B  1 410 ? 36.180  29.182  49.538  1.00 23.47 ? 427  GLU B OE2 1 
ATOM   7687  N  N   . CYS B  1 411 ? 35.240  26.591  55.461  1.00 27.87 ? 428  CYS B N   1 
ATOM   7688  C  CA  . CYS B  1 411 ? 35.093  26.103  56.825  1.00 28.07 ? 428  CYS B CA  1 
ATOM   7689  C  C   . CYS B  1 411 ? 34.113  24.931  56.837  1.00 28.63 ? 428  CYS B C   1 
ATOM   7690  O  O   . CYS B  1 411 ? 33.474  24.655  55.824  1.00 27.91 ? 428  CYS B O   1 
ATOM   7691  C  CB  . CYS B  1 411 ? 34.644  27.205  57.782  1.00 28.30 ? 428  CYS B CB  1 
ATOM   7692  S  SG  . CYS B  1 411 ? 32.962  27.820  57.504  1.00 29.32 ? 428  CYS B SG  1 
ATOM   7693  N  N   . THR B  1 412 ? 34.022  24.230  57.977  1.00 29.27 ? 429  THR B N   1 
ATOM   7694  C  CA  . THR B  1 412 ? 33.074  23.134  58.127  1.00 29.98 ? 429  THR B CA  1 
ATOM   7695  C  C   . THR B  1 412 ? 31.816  23.664  58.814  1.00 30.17 ? 429  THR B C   1 
ATOM   7696  O  O   . THR B  1 412 ? 31.832  24.745  59.396  1.00 31.23 ? 429  THR B O   1 
ATOM   7697  C  CB  . THR B  1 412 ? 33.698  21.976  58.910  1.00 30.13 ? 429  THR B CB  1 
ATOM   7698  O  OG1 . THR B  1 412 ? 33.941  22.461  60.225  1.00 30.57 ? 429  THR B OG1 1 
ATOM   7699  C  CG2 . THR B  1 412 ? 34.993  21.469  58.302  1.00 31.00 ? 429  THR B CG2 1 
ATOM   7700  N  N   . ALA B  1 413 ? 30.732  22.882  58.759  1.00 31.83 ? 430  ALA B N   1 
ATOM   7701  C  CA  . ALA B  1 413 ? 29.501  23.234  59.452  1.00 33.18 ? 430  ALA B CA  1 
ATOM   7702  C  C   . ALA B  1 413 ? 29.727  23.276  60.964  1.00 34.33 ? 430  ALA B C   1 
ATOM   7703  O  O   . ALA B  1 413 ? 29.205  24.155  61.645  1.00 33.40 ? 430  ALA B O   1 
ATOM   7704  C  CB  . ALA B  1 413 ? 28.399  22.261  59.097  1.00 33.96 ? 430  ALA B CB  1 
ATOM   7705  N  N   . GLU B  1 414 ? 30.503  22.319  61.485  1.00 37.21 ? 431  GLU B N   1 
ATOM   7706  C  CA  . GLU B  1 414 ? 30.760  22.237  62.916  1.00 40.62 ? 431  GLU B CA  1 
ATOM   7707  C  C   . GLU B  1 414 ? 31.398  23.540  63.399  1.00 38.93 ? 431  GLU B C   1 
ATOM   7708  O  O   . GLU B  1 414 ? 30.955  24.115  64.394  1.00 38.26 ? 431  GLU B O   1 
ATOM   7709  C  CB  . GLU B  1 414 ? 31.629  21.016  63.217  1.00 45.32 ? 431  GLU B CB  1 
ATOM   7710  C  CG  . GLU B  1 414 ? 31.801  20.743  64.709  1.00 51.40 ? 431  GLU B CG  1 
ATOM   7711  C  CD  . GLU B  1 414 ? 32.570  19.472  65.022  1.00 56.67 ? 431  GLU B CD  1 
ATOM   7712  O  OE1 . GLU B  1 414 ? 32.943  19.292  66.202  1.00 60.65 ? 431  GLU B OE1 1 
ATOM   7713  O  OE2 . GLU B  1 414 ? 32.788  18.657  64.098  1.00 59.36 ? 431  GLU B OE2 1 
ATOM   7714  N  N   . GLU B  1 415 ? 32.422  24.002  62.668  1.00 37.10 ? 432  GLU B N   1 
ATOM   7715  C  CA  . GLU B  1 415 ? 33.102  25.253  62.966  1.00 35.81 ? 432  GLU B CA  1 
ATOM   7716  C  C   . GLU B  1 415 ? 32.103  26.406  62.968  1.00 33.83 ? 432  GLU B C   1 
ATOM   7717  O  O   . GLU B  1 415 ? 32.057  27.184  63.916  1.00 33.46 ? 432  GLU B O   1 
ATOM   7718  C  CB  . GLU B  1 415 ? 34.216  25.531  61.954  1.00 37.14 ? 432  GLU B CB  1 
ATOM   7719  C  CG  . GLU B  1 415 ? 35.433  24.629  62.135  1.00 39.49 ? 432  GLU B CG  1 
ATOM   7720  C  CD  . GLU B  1 415 ? 36.473  24.665  61.024  1.00 40.79 ? 432  GLU B CD  1 
ATOM   7721  O  OE1 . GLU B  1 415 ? 37.536  24.049  61.243  1.00 43.45 ? 432  GLU B OE1 1 
ATOM   7722  O  OE2 . GLU B  1 415 ? 36.237  25.263  59.951  1.00 37.06 ? 432  GLU B OE2 1 
ATOM   7723  N  N   . ALA B  1 416 ? 31.309  26.517  61.897  1.00 32.45 ? 433  ALA B N   1 
ATOM   7724  C  CA  . ALA B  1 416 ? 30.425  27.659  61.726  1.00 32.46 ? 433  ALA B CA  1 
ATOM   7725  C  C   . ALA B  1 416 ? 29.423  27.753  62.876  1.00 30.68 ? 433  ALA B C   1 
ATOM   7726  O  O   . ALA B  1 416 ? 29.237  28.829  63.440  1.00 30.79 ? 433  ALA B O   1 
ATOM   7727  C  CB  . ALA B  1 416 ? 29.724  27.577  60.384  1.00 32.98 ? 433  ALA B CB  1 
ATOM   7728  N  N   . TYR B  1 417 ? 28.772  26.631  63.212  1.00 30.43 ? 434  TYR B N   1 
ATOM   7729  C  CA  . TYR B  1 417 ? 27.705  26.635  64.205  1.00 31.48 ? 434  TYR B CA  1 
ATOM   7730  C  C   . TYR B  1 417 ? 28.292  26.823  65.607  1.00 31.52 ? 434  TYR B C   1 
ATOM   7731  O  O   . TYR B  1 417 ? 27.739  27.571  66.413  1.00 29.80 ? 434  TYR B O   1 
ATOM   7732  C  CB  . TYR B  1 417 ? 26.866  25.354  64.110  1.00 32.54 ? 434  TYR B CB  1 
ATOM   7733  C  CG  . TYR B  1 417 ? 25.957  25.283  62.889  1.00 33.04 ? 434  TYR B CG  1 
ATOM   7734  C  CD1 . TYR B  1 417 ? 25.027  26.282  62.624  1.00 33.19 ? 434  TYR B CD1 1 
ATOM   7735  C  CD2 . TYR B  1 417 ? 26.057  24.233  61.982  1.00 33.87 ? 434  TYR B CD2 1 
ATOM   7736  C  CE1 . TYR B  1 417 ? 24.207  26.228  61.508  1.00 34.78 ? 434  TYR B CE1 1 
ATOM   7737  C  CE2 . TYR B  1 417 ? 25.248  24.170  60.859  1.00 33.77 ? 434  TYR B CE2 1 
ATOM   7738  C  CZ  . TYR B  1 417 ? 24.324  25.172  60.620  1.00 34.94 ? 434  TYR B CZ  1 
ATOM   7739  O  OH  . TYR B  1 417 ? 23.525  25.114  59.517  1.00 36.00 ? 434  TYR B OH  1 
ATOM   7740  N  N   . THR B  1 418 ? 29.413  26.149  65.890  1.00 33.61 ? 435  THR B N   1 
ATOM   7741  C  CA  . THR B  1 418 ? 30.019  26.221  67.211  1.00 34.73 ? 435  THR B CA  1 
ATOM   7742  C  C   . THR B  1 418 ? 30.511  27.645  67.463  1.00 34.51 ? 435  THR B C   1 
ATOM   7743  O  O   . THR B  1 418 ? 30.194  28.235  68.491  1.00 32.91 ? 435  THR B O   1 
ATOM   7744  C  CB  . THR B  1 418 ? 31.142  25.190  67.334  1.00 36.89 ? 435  THR B CB  1 
ATOM   7745  O  OG1 . THR B  1 418 ? 30.566  23.917  67.059  1.00 38.14 ? 435  THR B OG1 1 
ATOM   7746  C  CG2 . THR B  1 418 ? 31.744  25.147  68.726  1.00 39.43 ? 435  THR B CG2 1 
ATOM   7747  N  N   . LEU B  1 419 ? 31.251  28.214  66.502  1.00 33.25 ? 436  LEU B N   1 
ATOM   7748  C  CA  . LEU B  1 419 ? 31.948  29.472  66.729  1.00 33.19 ? 436  LEU B CA  1 
ATOM   7749  C  C   . LEU B  1 419 ? 31.010  30.678  66.613  1.00 34.15 ? 436  LEU B C   1 
ATOM   7750  O  O   . LEU B  1 419 ? 31.418  31.795  66.931  1.00 34.33 ? 436  LEU B O   1 
ATOM   7751  C  CB  . LEU B  1 419 ? 33.139  29.563  65.773  1.00 34.80 ? 436  LEU B CB  1 
ATOM   7752  C  CG  . LEU B  1 419 ? 34.230  28.500  65.956  1.00 35.36 ? 436  LEU B CG  1 
ATOM   7753  C  CD1 . LEU B  1 419 ? 35.278  28.575  64.861  1.00 36.51 ? 436  LEU B CD1 1 
ATOM   7754  C  CD2 . LEU B  1 419 ? 34.903  28.623  67.313  1.00 35.85 ? 436  LEU B CD2 1 
ATOM   7755  N  N   . THR B  1 420 ? 29.755  30.474  66.183  1.00 32.75 ? 437  THR B N   1 
ATOM   7756  C  CA  . THR B  1 420 ? 28.774  31.553  66.194  1.00 33.23 ? 437  THR B CA  1 
ATOM   7757  C  C   . THR B  1 420 ? 27.703  31.304  67.261  1.00 33.53 ? 437  THR B C   1 
ATOM   7758  O  O   . THR B  1 420 ? 26.729  32.046  67.330  1.00 31.45 ? 437  THR B O   1 
ATOM   7759  C  CB  . THR B  1 420 ? 28.152  31.728  64.805  1.00 33.81 ? 437  THR B CB  1 
ATOM   7760  O  OG1 . THR B  1 420 ? 27.407  30.548  64.515  1.00 33.30 ? 437  THR B OG1 1 
ATOM   7761  C  CG2 . THR B  1 420 ? 29.198  31.968  63.731  1.00 32.97 ? 437  THR B CG2 1 
ATOM   7762  N  N   . GLU B  1 421 ? 27.894  30.271  68.093  1.00 35.58 ? 438  GLU B N   1 
ATOM   7763  C  CA  . GLU B  1 421 ? 26.964  29.924  69.162  1.00 39.45 ? 438  GLU B CA  1 
ATOM   7764  C  C   . GLU B  1 421 ? 25.586  29.601  68.576  1.00 37.78 ? 438  GLU B C   1 
ATOM   7765  O  O   . GLU B  1 421 ? 24.559  29.959  69.154  1.00 37.58 ? 438  GLU B O   1 
ATOM   7766  C  CB  . GLU B  1 421 ? 26.905  31.035  70.215  1.00 42.46 ? 438  GLU B CB  1 
ATOM   7767  C  CG  . GLU B  1 421 ? 28.271  31.434  70.770  1.00 46.13 ? 438  GLU B CG  1 
ATOM   7768  C  CD  . GLU B  1 421 ? 28.268  32.727  71.574  1.00 51.77 ? 438  GLU B CD  1 
ATOM   7769  O  OE1 . GLU B  1 421 ? 27.882  32.694  72.766  1.00 51.66 ? 438  GLU B OE1 1 
ATOM   7770  O  OE2 . GLU B  1 421 ? 28.619  33.782  70.991  1.00 53.22 ? 438  GLU B OE2 1 
ATOM   7771  N  N   . GLY B  1 422 ? 25.579  28.925  67.419  1.00 36.87 ? 439  GLY B N   1 
ATOM   7772  C  CA  . GLY B  1 422 ? 24.357  28.431  66.803  1.00 34.81 ? 439  GLY B CA  1 
ATOM   7773  C  C   . GLY B  1 422 ? 23.505  29.540  66.186  1.00 34.52 ? 439  GLY B C   1 
ATOM   7774  O  O   . GLY B  1 422 ? 22.321  29.328  65.938  1.00 33.76 ? 439  GLY B O   1 
ATOM   7775  N  N   . ARG B  1 423 ? 24.112  30.701  65.903  1.00 33.86 ? 440  ARG B N   1 
ATOM   7776  C  CA  . ARG B  1 423 ? 23.380  31.857  65.404  1.00 33.09 ? 440  ARG B CA  1 
ATOM   7777  C  C   . ARG B  1 423 ? 23.520  32.013  63.887  1.00 31.35 ? 440  ARG B C   1 
ATOM   7778  O  O   . ARG B  1 423 ? 22.785  32.793  63.284  1.00 31.93 ? 440  ARG B O   1 
ATOM   7779  C  CB  . ARG B  1 423 ? 23.840  33.130  66.126  1.00 34.35 ? 440  ARG B CB  1 
ATOM   7780  C  CG  . ARG B  1 423 ? 23.269  33.273  67.530  1.00 35.02 ? 440  ARG B CG  1 
ATOM   7781  C  CD  . ARG B  1 423 ? 23.540  34.639  68.133  1.00 35.73 ? 440  ARG B CD  1 
ATOM   7782  N  NE  . ARG B  1 423 ? 24.965  34.806  68.436  1.00 36.86 ? 440  ARG B NE  1 
ATOM   7783  C  CZ  . ARG B  1 423 ? 25.793  35.737  67.963  1.00 38.40 ? 440  ARG B CZ  1 
ATOM   7784  N  NH1 . ARG B  1 423 ? 25.415  36.587  67.021  1.00 37.72 ? 440  ARG B NH1 1 
ATOM   7785  N  NH2 . ARG B  1 423 ? 27.030  35.799  68.429  1.00 39.06 ? 440  ARG B NH2 1 
ATOM   7786  N  N   . CYS B  1 424 ? 24.456  31.289  63.264  1.00 29.89 ? 441  CYS B N   1 
ATOM   7787  C  CA  . CYS B  1 424 ? 24.707  31.463  61.841  1.00 31.09 ? 441  CYS B CA  1 
ATOM   7788  C  C   . CYS B  1 424 ? 23.707  30.659  61.011  1.00 30.58 ? 441  CYS B C   1 
ATOM   7789  O  O   . CYS B  1 424 ? 23.201  29.633  61.458  1.00 30.47 ? 441  CYS B O   1 
ATOM   7790  C  CB  . CYS B  1 424 ? 26.126  31.062  61.458  1.00 31.07 ? 441  CYS B CB  1 
ATOM   7791  S  SG  . CYS B  1 424 ? 26.454  29.288  61.596  1.00 33.71 ? 441  CYS B SG  1 
ATOM   7792  N  N   . LEU B  1 425 ? 23.435  31.156  59.798  1.00 30.70 ? 442  LEU B N   1 
ATOM   7793  C  CA  . LEU B  1 425 ? 22.831  30.364  58.738  1.00 30.49 ? 442  LEU B CA  1 
ATOM   7794  C  C   . LEU B  1 425 ? 23.936  29.926  57.781  1.00 28.60 ? 442  LEU B C   1 
ATOM   7795  O  O   . LEU B  1 425 ? 24.582  30.763  57.156  1.00 28.05 ? 442  LEU B O   1 
ATOM   7796  C  CB  . LEU B  1 425 ? 21.754  31.188  58.037  1.00 31.51 ? 442  LEU B CB  1 
ATOM   7797  C  CG  . LEU B  1 425 ? 20.522  31.518  58.887  1.00 33.58 ? 442  LEU B CG  1 
ATOM   7798  C  CD1 . LEU B  1 425 ? 19.539  32.364  58.111  1.00 34.23 ? 442  LEU B CD1 1 
ATOM   7799  C  CD2 . LEU B  1 425 ? 19.849  30.249  59.379  1.00 35.25 ? 442  LEU B CD2 1 
ATOM   7800  N  N   . PHE B  1 426 ? 24.159  28.612  57.698  1.00 27.02 ? 443  PHE B N   1 
ATOM   7801  C  CA  . PHE B  1 426 ? 25.308  28.070  56.998  1.00 27.15 ? 443  PHE B CA  1 
ATOM   7802  C  C   . PHE B  1 426 ? 24.877  27.157  55.852  1.00 26.87 ? 443  PHE B C   1 
ATOM   7803  O  O   . PHE B  1 426 ? 23.961  26.349  56.001  1.00 26.08 ? 443  PHE B O   1 
ATOM   7804  C  CB  . PHE B  1 426 ? 26.178  27.295  57.988  1.00 26.54 ? 443  PHE B CB  1 
ATOM   7805  C  CG  . PHE B  1 426 ? 27.346  26.574  57.334  1.00 27.31 ? 443  PHE B CG  1 
ATOM   7806  C  CD1 . PHE B  1 426 ? 28.517  27.257  57.014  1.00 27.28 ? 443  PHE B CD1 1 
ATOM   7807  C  CD2 . PHE B  1 426 ? 27.264  25.219  57.024  1.00 27.67 ? 443  PHE B CD2 1 
ATOM   7808  C  CE1 . PHE B  1 426 ? 29.577  26.596  56.412  1.00 27.13 ? 443  PHE B CE1 1 
ATOM   7809  C  CE2 . PHE B  1 426 ? 28.328  24.563  56.424  1.00 27.28 ? 443  PHE B CE2 1 
ATOM   7810  C  CZ  . PHE B  1 426 ? 29.481  25.251  56.120  1.00 27.06 ? 443  PHE B CZ  1 
ATOM   7811  N  N   . ALA B  1 427 ? 25.596  27.263  54.730  1.00 25.74 ? 444  ALA B N   1 
ATOM   7812  C  CA  . ALA B  1 427 ? 25.476  26.316  53.635  1.00 26.32 ? 444  ALA B CA  1 
ATOM   7813  C  C   . ALA B  1 427 ? 26.852  26.062  53.033  1.00 27.34 ? 444  ALA B C   1 
ATOM   7814  O  O   . ALA B  1 427 ? 27.723  26.932  53.080  1.00 27.52 ? 444  ALA B O   1 
ATOM   7815  C  CB  . ALA B  1 427 ? 24.512  26.839  52.593  1.00 25.68 ? 444  ALA B CB  1 
ATOM   7816  N  N   . SER B  1 428 ? 27.034  24.860  52.478  1.00 27.91 ? 445  SER B N   1 
ATOM   7817  C  CA  . SER B  1 428 ? 28.238  24.528  51.737  1.00 31.00 ? 445  SER B CA  1 
ATOM   7818  C  C   . SER B  1 428 ? 27.872  23.717  50.498  1.00 32.91 ? 445  SER B C   1 
ATOM   7819  O  O   . SER B  1 428 ? 26.725  23.307  50.329  1.00 33.94 ? 445  SER B O   1 
ATOM   7820  C  CB  . SER B  1 428 ? 29.237  23.789  52.600  1.00 32.79 ? 445  SER B CB  1 
ATOM   7821  O  OG  . SER B  1 428 ? 28.924  22.406  52.689  1.00 36.50 ? 445  SER B OG  1 
ATOM   7822  N  N   . GLY B  1 429 ? 28.864  23.515  49.626  1.00 33.92 ? 446  GLY B N   1 
ATOM   7823  C  CA  . GLY B  1 429 ? 28.729  22.616  48.494  1.00 36.62 ? 446  GLY B CA  1 
ATOM   7824  C  C   . GLY B  1 429 ? 29.181  21.201  48.845  1.00 38.84 ? 446  GLY B C   1 
ATOM   7825  O  O   . GLY B  1 429 ? 29.043  20.299  48.024  1.00 42.21 ? 446  GLY B O   1 
ATOM   7826  N  N   . SER B  1 430 ? 29.722  21.028  50.061  1.00 40.38 ? 447  SER B N   1 
ATOM   7827  C  CA  . SER B  1 430 ? 30.197  19.743  50.551  1.00 43.29 ? 447  SER B CA  1 
ATOM   7828  C  C   . SER B  1 430 ? 29.103  19.054  51.368  1.00 47.88 ? 447  SER B C   1 
ATOM   7829  O  O   . SER B  1 430 ? 28.260  19.719  51.967  1.00 47.51 ? 447  SER B O   1 
ATOM   7830  C  CB  . SER B  1 430 ? 31.450  19.913  51.382  1.00 43.69 ? 447  SER B CB  1 
ATOM   7831  O  OG  . SER B  1 430 ? 32.426  20.693  50.706  1.00 44.84 ? 447  SER B OG  1 
ATOM   7832  N  N   . PRO B  1 431 ? 29.101  17.703  51.454  1.00 54.17 ? 448  PRO B N   1 
ATOM   7833  C  CA  . PRO B  1 431 ? 28.085  16.983  52.224  1.00 56.11 ? 448  PRO B CA  1 
ATOM   7834  C  C   . PRO B  1 431 ? 28.448  16.888  53.704  1.00 55.28 ? 448  PRO B C   1 
ATOM   7835  O  O   . PRO B  1 431 ? 29.071  15.921  54.135  1.00 57.84 ? 448  PRO B O   1 
ATOM   7836  C  CB  . PRO B  1 431 ? 28.087  15.618  51.514  1.00 56.43 ? 448  PRO B CB  1 
ATOM   7837  C  CG  . PRO B  1 431 ? 29.541  15.405  51.146  1.00 57.30 ? 448  PRO B CG  1 
ATOM   7838  C  CD  . PRO B  1 431 ? 30.083  16.797  50.835  1.00 55.79 ? 448  PRO B CD  1 
ATOM   7839  N  N   . PHE B  1 432 ? 28.065  17.915  54.469  1.00 53.71 ? 449  PHE B N   1 
ATOM   7840  C  CA  . PHE B  1 432 ? 28.259  17.923  55.910  1.00 51.43 ? 449  PHE B CA  1 
ATOM   7841  C  C   . PHE B  1 432 ? 27.011  17.341  56.564  1.00 50.07 ? 449  PHE B C   1 
ATOM   7842  O  O   . PHE B  1 432 ? 25.894  17.680  56.181  1.00 50.25 ? 449  PHE B O   1 
ATOM   7843  C  CB  . PHE B  1 432 ? 28.556  19.338  56.424  1.00 49.31 ? 449  PHE B CB  1 
ATOM   7844  C  CG  . PHE B  1 432 ? 29.908  19.902  56.004  1.00 47.79 ? 449  PHE B CG  1 
ATOM   7845  C  CD1 . PHE B  1 432 ? 31.088  19.213  56.273  1.00 45.01 ? 449  PHE B CD1 1 
ATOM   7846  C  CD2 . PHE B  1 432 ? 29.992  21.104  55.310  1.00 44.84 ? 449  PHE B CD2 1 
ATOM   7847  C  CE1 . PHE B  1 432 ? 32.313  19.725  55.876  1.00 45.13 ? 449  PHE B CE1 1 
ATOM   7848  C  CE2 . PHE B  1 432 ? 31.220  21.609  54.911  1.00 43.58 ? 449  PHE B CE2 1 
ATOM   7849  C  CZ  . PHE B  1 432 ? 32.376  20.919  55.193  1.00 45.13 ? 449  PHE B CZ  1 
ATOM   7850  N  N   . GLY B  1 433 ? 27.222  16.460  57.549  1.00 53.61 ? 450  GLY B N   1 
ATOM   7851  C  CA  . GLY B  1 433 ? 26.133  15.865  58.307  1.00 53.52 ? 450  GLY B CA  1 
ATOM   7852  C  C   . GLY B  1 433 ? 25.649  16.814  59.399  1.00 54.36 ? 450  GLY B C   1 
ATOM   7853  O  O   . GLY B  1 433 ? 26.304  17.817  59.685  1.00 53.47 ? 450  GLY B O   1 
ATOM   7854  N  N   . PRO B  1 434 ? 24.499  16.521  60.052  1.00 54.52 ? 451  PRO B N   1 
ATOM   7855  C  CA  . PRO B  1 434 ? 23.949  17.409  61.077  1.00 51.58 ? 451  PRO B CA  1 
ATOM   7856  C  C   . PRO B  1 434 ? 24.960  17.679  62.189  1.00 49.43 ? 451  PRO B C   1 
ATOM   7857  O  O   . PRO B  1 434 ? 25.837  16.859  62.459  1.00 48.06 ? 451  PRO B O   1 
ATOM   7858  C  CB  . PRO B  1 434 ? 22.695  16.670  61.589  1.00 53.50 ? 451  PRO B CB  1 
ATOM   7859  C  CG  . PRO B  1 434 ? 22.346  15.697  60.482  1.00 54.04 ? 451  PRO B CG  1 
ATOM   7860  C  CD  . PRO B  1 434 ? 23.677  15.316  59.850  1.00 55.59 ? 451  PRO B CD  1 
ATOM   7861  N  N   . VAL B  1 435 ? 24.831  18.854  62.810  1.00 49.18 ? 452  VAL B N   1 
ATOM   7862  C  CA  . VAL B  1 435 ? 25.721  19.279  63.875  1.00 48.34 ? 452  VAL B CA  1 
ATOM   7863  C  C   . VAL B  1 435 ? 24.886  19.427  65.143  1.00 49.12 ? 452  VAL B C   1 
ATOM   7864  O  O   . VAL B  1 435 ? 23.836  20.068  65.125  1.00 45.93 ? 452  VAL B O   1 
ATOM   7865  C  CB  . VAL B  1 435 ? 26.452  20.589  63.516  1.00 47.89 ? 452  VAL B CB  1 
ATOM   7866  C  CG1 . VAL B  1 435 ? 27.333  21.092  64.656  1.00 47.64 ? 452  VAL B CG1 1 
ATOM   7867  C  CG2 . VAL B  1 435 ? 27.273  20.442  62.240  1.00 47.72 ? 452  VAL B CG2 1 
ATOM   7868  N  N   . LYS B  1 436 ? 25.365  18.813  66.232  1.00 51.03 ? 453  LYS B N   1 
ATOM   7869  C  CA  . LYS B  1 436 ? 24.693  18.881  67.518  1.00 52.42 ? 453  LYS B CA  1 
ATOM   7870  C  C   . LYS B  1 436 ? 25.594  19.614  68.508  1.00 48.21 ? 453  LYS B C   1 
ATOM   7871  O  O   . LYS B  1 436 ? 26.661  19.118  68.858  1.00 47.03 ? 453  LYS B O   1 
ATOM   7872  C  CB  . LYS B  1 436 ? 24.338  17.473  68.011  1.00 55.60 ? 453  LYS B CB  1 
ATOM   7873  C  CG  . LYS B  1 436 ? 23.621  17.443  69.353  1.00 58.76 ? 453  LYS B CG  1 
ATOM   7874  C  CD  . LYS B  1 436 ? 22.810  16.177  69.599  1.00 61.57 ? 453  LYS B CD  1 
ATOM   7875  C  CE  . LYS B  1 436 ? 21.964  16.287  70.828  1.00 64.20 ? 453  LYS B CE  1 
ATOM   7876  N  NZ  . LYS B  1 436 ? 20.945  15.237  70.866  1.00 65.56 ? 453  LYS B NZ  1 
ATOM   7877  N  N   . LEU B  1 437 ? 25.148  20.799  68.941  1.00 47.53 ? 454  LEU B N   1 
ATOM   7878  C  CA  . LEU B  1 437 ? 25.871  21.583  69.927  1.00 49.24 ? 454  LEU B CA  1 
ATOM   7879  C  C   . LEU B  1 437 ? 25.650  20.962  71.304  1.00 54.44 ? 454  LEU B C   1 
ATOM   7880  O  O   . LEU B  1 437 ? 24.728  20.170  71.499  1.00 55.99 ? 454  LEU B O   1 
ATOM   7881  C  CB  . LEU B  1 437 ? 25.433  23.049  69.894  1.00 46.38 ? 454  LEU B CB  1 
ATOM   7882  C  CG  . LEU B  1 437 ? 25.617  23.792  68.565  1.00 44.62 ? 454  LEU B CG  1 
ATOM   7883  C  CD1 . LEU B  1 437 ? 25.223  25.250  68.728  1.00 44.52 ? 454  LEU B CD1 1 
ATOM   7884  C  CD2 . LEU B  1 437 ? 27.036  23.691  68.024  1.00 44.31 ? 454  LEU B CD2 1 
ATOM   7885  N  N   . THR B  1 438 ? 26.502  21.355  72.257  1.00 57.02 ? 455  THR B N   1 
ATOM   7886  C  CA  . THR B  1 438 ? 26.549  20.743  73.575  1.00 59.54 ? 455  THR B CA  1 
ATOM   7887  C  C   . THR B  1 438 ? 25.282  21.079  74.365  1.00 61.38 ? 455  THR B C   1 
ATOM   7888  O  O   . THR B  1 438 ? 24.874  20.306  75.230  1.00 63.09 ? 455  THR B O   1 
ATOM   7889  C  CB  . THR B  1 438 ? 27.816  21.206  74.293  1.00 59.50 ? 455  THR B CB  1 
ATOM   7890  O  OG1 . THR B  1 438 ? 27.752  22.628  74.336  1.00 59.29 ? 455  THR B OG1 1 
ATOM   7891  C  CG2 . THR B  1 438 ? 29.084  20.768  73.580  1.00 59.63 ? 455  THR B CG2 1 
ATOM   7892  N  N   . ASP B  1 439 ? 24.655  22.221  74.049  1.00 62.74 ? 456  ASP B N   1 
ATOM   7893  C  CA  . ASP B  1 439 ? 23.435  22.647  74.719  1.00 60.66 ? 456  ASP B CA  1 
ATOM   7894  C  C   . ASP B  1 439 ? 22.219  21.896  74.172  1.00 60.18 ? 456  ASP B C   1 
ATOM   7895  O  O   . ASP B  1 439 ? 21.101  22.148  74.615  1.00 60.02 ? 456  ASP B O   1 
ATOM   7896  C  CB  . ASP B  1 439 ? 23.256  24.158  74.649  1.00 62.41 ? 456  ASP B CB  1 
ATOM   7897  C  CG  . ASP B  1 439 ? 22.950  24.749  73.277  1.00 65.17 ? 456  ASP B CG  1 
ATOM   7898  O  OD1 . ASP B  1 439 ? 22.978  23.994  72.279  1.00 64.39 ? 456  ASP B OD1 1 
ATOM   7899  O  OD2 . ASP B  1 439 ? 22.671  25.965  73.220  1.00 66.58 ? 456  ASP B OD2 1 
ATOM   7900  N  N   . GLY B  1 440 ? 22.434  21.008  73.189  1.00 60.89 ? 457  GLY B N   1 
ATOM   7901  C  CA  . GLY B  1 440 ? 21.412  20.070  72.748  1.00 60.08 ? 457  GLY B CA  1 
ATOM   7902  C  C   . GLY B  1 440 ? 20.869  20.390  71.355  1.00 58.82 ? 457  GLY B C   1 
ATOM   7903  O  O   . GLY B  1 440 ? 20.340  19.506  70.684  1.00 57.46 ? 457  GLY B O   1 
ATOM   7904  N  N   . ARG B  1 441 ? 20.994  21.653  70.924  1.00 55.94 ? 458  ARG B N   1 
ATOM   7905  C  CA  . ARG B  1 441 ? 20.401  22.093  69.671  1.00 53.27 ? 458  ARG B CA  1 
ATOM   7906  C  C   . ARG B  1 441 ? 21.047  21.362  68.496  1.00 51.45 ? 458  ARG B C   1 
ATOM   7907  O  O   . ARG B  1 441 ? 22.253  21.117  68.497  1.00 50.21 ? 458  ARG B O   1 
ATOM   7908  C  CB  . ARG B  1 441 ? 20.523  23.612  69.519  1.00 52.21 ? 458  ARG B CB  1 
ATOM   7909  C  CG  . ARG B  1 441 ? 19.615  24.405  70.449  1.00 51.22 ? 458  ARG B CG  1 
ATOM   7910  C  CD  . ARG B  1 441 ? 19.765  25.899  70.211  1.00 52.03 ? 458  ARG B CD  1 
ATOM   7911  N  NE  . ARG B  1 441 ? 21.138  26.350  70.472  1.00 52.89 ? 458  ARG B NE  1 
ATOM   7912  C  CZ  . ARG B  1 441 ? 21.659  27.528  70.137  1.00 54.55 ? 458  ARG B CZ  1 
ATOM   7913  N  NH1 . ARG B  1 441 ? 20.936  28.431  69.495  1.00 56.58 ? 458  ARG B NH1 1 
ATOM   7914  N  NH2 . ARG B  1 441 ? 22.917  27.796  70.439  1.00 54.43 ? 458  ARG B NH2 1 
ATOM   7915  N  N   . VAL B  1 442 ? 20.217  21.006  67.505  1.00 48.37 ? 459  VAL B N   1 
ATOM   7916  C  CA  . VAL B  1 442 ? 20.669  20.293  66.321  1.00 48.39 ? 459  VAL B CA  1 
ATOM   7917  C  C   . VAL B  1 442 ? 20.465  21.197  65.108  1.00 46.90 ? 459  VAL B C   1 
ATOM   7918  O  O   . VAL B  1 442 ? 19.397  21.785  64.945  1.00 46.17 ? 459  VAL B O   1 
ATOM   7919  C  CB  . VAL B  1 442 ? 19.937  18.947  66.146  1.00 49.93 ? 459  VAL B CB  1 
ATOM   7920  C  CG1 . VAL B  1 442 ? 20.317  18.248  64.845  1.00 50.22 ? 459  VAL B CG1 1 
ATOM   7921  C  CG2 . VAL B  1 442 ? 20.172  18.018  67.332  1.00 52.01 ? 459  VAL B CG2 1 
ATOM   7922  N  N   . PHE B  1 443 ? 21.503  21.291  64.266  1.00 45.73 ? 460  PHE B N   1 
ATOM   7923  C  CA  . PHE B  1 443 ? 21.458  22.099  63.058  1.00 43.26 ? 460  PHE B CA  1 
ATOM   7924  C  C   . PHE B  1 443 ? 21.675  21.203  61.845  1.00 41.88 ? 460  PHE B C   1 
ATOM   7925  O  O   . PHE B  1 443 ? 22.494  20.287  61.881  1.00 43.88 ? 460  PHE B O   1 
ATOM   7926  C  CB  . PHE B  1 443 ? 22.510  23.211  63.115  1.00 41.99 ? 460  PHE B CB  1 
ATOM   7927  C  CG  . PHE B  1 443 ? 22.245  24.233  64.208  1.00 40.55 ? 460  PHE B CG  1 
ATOM   7928  C  CD1 . PHE B  1 443 ? 22.725  24.033  65.499  1.00 41.81 ? 460  PHE B CD1 1 
ATOM   7929  C  CD2 . PHE B  1 443 ? 21.498  25.375  63.949  1.00 40.03 ? 460  PHE B CD2 1 
ATOM   7930  C  CE1 . PHE B  1 443 ? 22.468  24.957  66.500  1.00 41.18 ? 460  PHE B CE1 1 
ATOM   7931  C  CE2 . PHE B  1 443 ? 21.246  26.298  64.951  1.00 40.99 ? 460  PHE B CE2 1 
ATOM   7932  C  CZ  . PHE B  1 443 ? 21.729  26.087  66.225  1.00 41.88 ? 460  PHE B CZ  1 
ATOM   7933  N  N   . THR B  1 444 ? 20.927  21.489  60.776  1.00 43.30 ? 461  THR B N   1 
ATOM   7934  C  CA  . THR B  1 444 ? 21.083  20.793  59.512  1.00 42.74 ? 461  THR B CA  1 
ATOM   7935  C  C   . THR B  1 444 ? 21.633  21.786  58.490  1.00 38.04 ? 461  THR B C   1 
ATOM   7936  O  O   . THR B  1 444 ? 20.920  22.683  58.046  1.00 37.08 ? 461  THR B O   1 
ATOM   7937  C  CB  . THR B  1 444 ? 19.737  20.198  59.102  1.00 46.38 ? 461  THR B CB  1 
ATOM   7938  O  OG1 . THR B  1 444 ? 19.400  19.328  60.178  1.00 48.36 ? 461  THR B OG1 1 
ATOM   7939  C  CG2 . THR B  1 444 ? 19.803  19.393  57.816  1.00 47.31 ? 461  THR B CG2 1 
ATOM   7940  N  N   . PRO B  1 445 ? 22.926  21.682  58.109  1.00 36.27 ? 462  PRO B N   1 
ATOM   7941  C  CA  . PRO B  1 445 ? 23.522  22.636  57.173  1.00 35.86 ? 462  PRO B CA  1 
ATOM   7942  C  C   . PRO B  1 445 ? 22.911  22.494  55.782  1.00 34.96 ? 462  PRO B C   1 
ATOM   7943  O  O   . PRO B  1 445 ? 22.641  21.385  55.330  1.00 35.14 ? 462  PRO B O   1 
ATOM   7944  C  CB  . PRO B  1 445 ? 25.021  22.283  57.207  1.00 35.78 ? 462  PRO B CB  1 
ATOM   7945  C  CG  . PRO B  1 445 ? 25.053  20.821  57.596  1.00 36.59 ? 462  PRO B CG  1 
ATOM   7946  C  CD  . PRO B  1 445 ? 23.877  20.645  58.544  1.00 36.48 ? 462  PRO B CD  1 
ATOM   7947  N  N   . GLY B  1 446 ? 22.681  23.632  55.119  1.00 34.21 ? 463  GLY B N   1 
ATOM   7948  C  CA  . GLY B  1 446 ? 22.252  23.627  53.732  1.00 34.62 ? 463  GLY B CA  1 
ATOM   7949  C  C   . GLY B  1 446 ? 23.329  23.019  52.837  1.00 33.69 ? 463  GLY B C   1 
ATOM   7950  O  O   . GLY B  1 446 ? 24.520  23.171  53.104  1.00 31.64 ? 463  GLY B O   1 
ATOM   7951  N  N   . GLN B  1 447 ? 22.896  22.306  51.796  1.00 34.39 ? 464  GLN B N   1 
ATOM   7952  C  CA  . GLN B  1 447 ? 23.801  21.822  50.767  1.00 37.80 ? 464  GLN B CA  1 
ATOM   7953  C  C   . GLN B  1 447 ? 23.416  22.486  49.447  1.00 37.02 ? 464  GLN B C   1 
ATOM   7954  O  O   . GLN B  1 447 ? 22.309  22.281  48.954  1.00 35.39 ? 464  GLN B O   1 
ATOM   7955  C  CB  . GLN B  1 447 ? 23.743  20.295  50.696  1.00 41.36 ? 464  GLN B CB  1 
ATOM   7956  C  CG  . GLN B  1 447 ? 24.932  19.659  49.982  1.00 45.29 ? 464  GLN B CG  1 
ATOM   7957  C  CD  . GLN B  1 447 ? 24.670  18.229  49.557  1.00 49.70 ? 464  GLN B CD  1 
ATOM   7958  O  OE1 . GLN B  1 447 ? 24.865  17.861  48.393  1.00 50.99 ? 464  GLN B OE1 1 
ATOM   7959  N  NE2 . GLN B  1 447 ? 24.224  17.406  50.498  1.00 51.17 ? 464  GLN B NE2 1 
ATOM   7960  N  N   . GLY B  1 448 ? 24.325  23.305  48.900  1.00 35.09 ? 465  GLY B N   1 
ATOM   7961  C  CA  . GLY B  1 448 ? 24.069  24.056  47.678  1.00 33.95 ? 465  GLY B CA  1 
ATOM   7962  C  C   . GLY B  1 448 ? 24.383  23.225  46.435  1.00 32.55 ? 465  GLY B C   1 
ATOM   7963  O  O   . GLY B  1 448 ? 25.317  23.537  45.692  1.00 33.65 ? 465  GLY B O   1 
ATOM   7964  N  N   . ASN B  1 449 ? 23.569  22.182  46.226  1.00 28.18 ? 466  ASN B N   1 
ATOM   7965  C  CA  . ASN B  1 449 ? 23.776  21.176  45.197  1.00 27.60 ? 466  ASN B CA  1 
ATOM   7966  C  C   . ASN B  1 449 ? 23.059  21.604  43.917  1.00 26.32 ? 466  ASN B C   1 
ATOM   7967  O  O   . ASN B  1 449 ? 21.857  21.863  43.947  1.00 22.87 ? 466  ASN B O   1 
ATOM   7968  C  CB  . ASN B  1 449 ? 23.237  19.838  45.694  1.00 28.34 ? 466  ASN B CB  1 
ATOM   7969  C  CG  . ASN B  1 449 ? 23.657  18.662  44.848  1.00 29.48 ? 466  ASN B CG  1 
ATOM   7970  O  OD1 . ASN B  1 449 ? 23.662  18.742  43.616  1.00 28.48 ? 466  ASN B OD1 1 
ATOM   7971  N  ND2 . ASN B  1 449 ? 24.003  17.558  45.491  1.00 30.91 ? 466  ASN B ND2 1 
ATOM   7972  N  N   . ASN B  1 450 ? 23.782  21.612  42.785  1.00 25.64 ? 467  ASN B N   1 
ATOM   7973  C  CA  . ASN B  1 450 ? 23.236  22.091  41.520  1.00 25.69 ? 467  ASN B CA  1 
ATOM   7974  C  C   . ASN B  1 450 ? 22.030  21.262  41.060  1.00 23.13 ? 467  ASN B C   1 
ATOM   7975  O  O   . ASN B  1 450 ? 21.205  21.757  40.290  1.00 21.86 ? 467  ASN B O   1 
ATOM   7976  C  CB  . ASN B  1 450 ? 24.311  22.176  40.437  1.00 26.80 ? 467  ASN B CB  1 
ATOM   7977  C  CG  . ASN B  1 450 ? 25.198  23.392  40.602  1.00 28.55 ? 467  ASN B CG  1 
ATOM   7978  O  OD1 . ASN B  1 450 ? 25.163  24.062  41.641  1.00 30.60 ? 467  ASN B OD1 1 
ATOM   7979  N  ND2 . ASN B  1 450 ? 26.007  23.695  39.600  1.00 27.94 ? 467  ASN B ND2 1 
ATOM   7980  N  N   . VAL B  1 451 ? 21.896  20.024  41.552  1.00 21.65 ? 468  VAL B N   1 
ATOM   7981  C  CA  . VAL B  1 451 ? 20.813  19.144  41.130  1.00 22.26 ? 468  VAL B CA  1 
ATOM   7982  C  C   . VAL B  1 451 ? 19.444  19.711  41.526  1.00 21.59 ? 468  VAL B C   1 
ATOM   7983  O  O   . VAL B  1 451 ? 18.432  19.266  40.997  1.00 21.20 ? 468  VAL B O   1 
ATOM   7984  C  CB  . VAL B  1 451 ? 20.999  17.704  41.655  1.00 23.29 ? 468  VAL B CB  1 
ATOM   7985  C  CG1 . VAL B  1 451 ? 20.721  17.575  43.153  1.00 24.00 ? 468  VAL B CG1 1 
ATOM   7986  C  CG2 . VAL B  1 451 ? 20.144  16.706  40.882  1.00 23.97 ? 468  VAL B CG2 1 
ATOM   7987  N  N   . TYR B  1 452 ? 19.398  20.684  42.447  1.00 21.17 ? 469  TYR B N   1 
ATOM   7988  C  CA  . TYR B  1 452 ? 18.154  21.367  42.790  1.00 21.50 ? 469  TYR B CA  1 
ATOM   7989  C  C   . TYR B  1 452 ? 17.579  22.155  41.606  1.00 21.03 ? 469  TYR B C   1 
ATOM   7990  O  O   . TYR B  1 452 ? 16.367  22.363  41.539  1.00 21.60 ? 469  TYR B O   1 
ATOM   7991  C  CB  . TYR B  1 452 ? 18.399  22.311  43.974  1.00 22.80 ? 469  TYR B CB  1 
ATOM   7992  C  CG  . TYR B  1 452 ? 18.419  21.693  45.369  1.00 23.96 ? 469  TYR B CG  1 
ATOM   7993  C  CD1 . TYR B  1 452 ? 17.368  20.905  45.832  1.00 25.23 ? 469  TYR B CD1 1 
ATOM   7994  C  CD2 . TYR B  1 452 ? 19.483  21.918  46.238  1.00 25.05 ? 469  TYR B CD2 1 
ATOM   7995  C  CE1 . TYR B  1 452 ? 17.380  20.357  47.106  1.00 25.51 ? 469  TYR B CE1 1 
ATOM   7996  C  CE2 . TYR B  1 452 ? 19.504  21.379  47.515  1.00 25.68 ? 469  TYR B CE2 1 
ATOM   7997  C  CZ  . TYR B  1 452 ? 18.451  20.593  47.952  1.00 26.24 ? 469  TYR B CZ  1 
ATOM   7998  O  OH  . TYR B  1 452 ? 18.476  20.060  49.215  1.00 25.51 ? 469  TYR B OH  1 
ATOM   7999  N  N   . ILE B  1 453 ? 18.434  22.594  40.670  1.00 20.69 ? 470  ILE B N   1 
ATOM   8000  C  CA  . ILE B  1 453 ? 18.056  23.562  39.648  1.00 20.59 ? 470  ILE B CA  1 
ATOM   8001  C  C   . ILE B  1 453 ? 18.017  22.934  38.249  1.00 20.41 ? 470  ILE B C   1 
ATOM   8002  O  O   . ILE B  1 453 ? 17.023  23.103  37.544  1.00 19.69 ? 470  ILE B O   1 
ATOM   8003  C  CB  . ILE B  1 453 ? 19.006  24.778  39.689  1.00 20.44 ? 470  ILE B CB  1 
ATOM   8004  C  CG1 . ILE B  1 453 ? 18.927  25.538  41.026  1.00 20.43 ? 470  ILE B CG1 1 
ATOM   8005  C  CG2 . ILE B  1 453 ? 18.772  25.705  38.497  1.00 20.85 ? 470  ILE B CG2 1 
ATOM   8006  C  CD1 . ILE B  1 453 ? 17.600  26.226  41.295  1.00 21.28 ? 470  ILE B CD1 1 
ATOM   8007  N  N   . PHE B  1 454 ? 19.097  22.262  37.808  1.00 19.77 ? 471  PHE B N   1 
ATOM   8008  C  CA  . PHE B  1 454 ? 19.254  21.953  36.388  1.00 19.80 ? 471  PHE B CA  1 
ATOM   8009  C  C   . PHE B  1 454 ? 18.177  20.983  35.886  1.00 19.93 ? 471  PHE B C   1 
ATOM   8010  O  O   . PHE B  1 454 ? 17.699  21.147  34.766  1.00 20.10 ? 471  PHE B O   1 
ATOM   8011  C  CB  . PHE B  1 454 ? 20.660  21.489  35.972  1.00 19.94 ? 471  PHE B CB  1 
ATOM   8012  C  CG  . PHE B  1 454 ? 21.194  20.188  36.553  1.00 20.34 ? 471  PHE B CG  1 
ATOM   8013  C  CD1 . PHE B  1 454 ? 20.822  18.956  36.020  1.00 21.10 ? 471  PHE B CD1 1 
ATOM   8014  C  CD2 . PHE B  1 454 ? 22.090  20.201  37.613  1.00 20.92 ? 471  PHE B CD2 1 
ATOM   8015  C  CE1 . PHE B  1 454 ? 21.318  17.776  36.552  1.00 21.56 ? 471  PHE B CE1 1 
ATOM   8016  C  CE2 . PHE B  1 454 ? 22.588  19.018  38.141  1.00 21.22 ? 471  PHE B CE2 1 
ATOM   8017  C  CZ  . PHE B  1 454 ? 22.196  17.809  37.613  1.00 22.26 ? 471  PHE B CZ  1 
ATOM   8018  N  N   . PRO B  1 455 ? 17.742  19.936  36.627  1.00 19.97 ? 472  PRO B N   1 
ATOM   8019  C  CA  . PRO B  1 455 ? 16.731  19.021  36.090  1.00 20.25 ? 472  PRO B CA  1 
ATOM   8020  C  C   . PRO B  1 455 ? 15.427  19.722  35.714  1.00 19.67 ? 472  PRO B C   1 
ATOM   8021  O  O   . PRO B  1 455 ? 14.926  19.552  34.603  1.00 19.09 ? 472  PRO B O   1 
ATOM   8022  C  CB  . PRO B  1 455 ? 16.550  18.003  37.231  1.00 20.00 ? 472  PRO B CB  1 
ATOM   8023  C  CG  . PRO B  1 455 ? 17.862  18.053  37.971  1.00 19.80 ? 472  PRO B CG  1 
ATOM   8024  C  CD  . PRO B  1 455 ? 18.198  19.535  37.969  1.00 19.87 ? 472  PRO B CD  1 
ATOM   8025  N  N   . GLY B  1 456 ? 14.909  20.534  36.641  1.00 19.86 ? 473  GLY B N   1 
ATOM   8026  C  CA  . GLY B  1 456 ? 13.634  21.215  36.463  1.00 19.95 ? 473  GLY B CA  1 
ATOM   8027  C  C   . GLY B  1 456 ? 13.691  22.296  35.386  1.00 20.00 ? 473  GLY B C   1 
ATOM   8028  O  O   . GLY B  1 456 ? 12.720  22.487  34.655  1.00 20.41 ? 473  GLY B O   1 
ATOM   8029  N  N   . VAL B  1 457 ? 14.819  23.019  35.306  1.00 19.40 ? 474  VAL B N   1 
ATOM   8030  C  CA  . VAL B  1 457 ? 15.008  24.024  34.271  1.00 18.58 ? 474  VAL B CA  1 
ATOM   8031  C  C   . VAL B  1 457 ? 15.052  23.343  32.902  1.00 18.35 ? 474  VAL B C   1 
ATOM   8032  O  O   . VAL B  1 457 ? 14.401  23.798  31.969  1.00 18.29 ? 474  VAL B O   1 
ATOM   8033  C  CB  . VAL B  1 457 ? 16.266  24.881  34.507  1.00 19.17 ? 474  VAL B CB  1 
ATOM   8034  C  CG1 . VAL B  1 457 ? 16.637  25.711  33.279  1.00 19.69 ? 474  VAL B CG1 1 
ATOM   8035  C  CG2 . VAL B  1 457 ? 16.096  25.780  35.726  1.00 19.86 ? 474  VAL B CG2 1 
ATOM   8036  N  N   . ALA B  1 458 ? 15.827  22.257  32.783  1.00 17.57 ? 475  ALA B N   1 
ATOM   8037  C  CA  . ALA B  1 458 ? 15.948  21.536  31.524  1.00 17.56 ? 475  ALA B CA  1 
ATOM   8038  C  C   . ALA B  1 458 ? 14.585  21.021  31.055  1.00 17.67 ? 475  ALA B C   1 
ATOM   8039  O  O   . ALA B  1 458 ? 14.244  21.158  29.882  1.00 16.35 ? 475  ALA B O   1 
ATOM   8040  C  CB  . ALA B  1 458 ? 16.949  20.413  31.665  1.00 17.26 ? 475  ALA B CB  1 
ATOM   8041  N  N   . LEU B  1 459 ? 13.801  20.440  31.974  1.00 18.10 ? 476  LEU B N   1 
ATOM   8042  C  CA  . LEU B  1 459 ? 12.511  19.871  31.616  1.00 18.41 ? 476  LEU B CA  1 
ATOM   8043  C  C   . LEU B  1 459 ? 11.601  20.961  31.050  1.00 17.81 ? 476  LEU B C   1 
ATOM   8044  O  O   . LEU B  1 459 ? 10.976  20.772  30.010  1.00 18.09 ? 476  LEU B O   1 
ATOM   8045  C  CB  . LEU B  1 459 ? 11.879  19.182  32.826  1.00 18.61 ? 476  LEU B CB  1 
ATOM   8046  C  CG  . LEU B  1 459 ? 10.496  18.564  32.602  1.00 19.21 ? 476  LEU B CG  1 
ATOM   8047  C  CD1 . LEU B  1 459 ? 10.519  17.482  31.538  1.00 19.79 ? 476  LEU B CD1 1 
ATOM   8048  C  CD2 . LEU B  1 459 ? 9.943   18.014  33.900  1.00 19.95 ? 476  LEU B CD2 1 
ATOM   8049  N  N   . ALA B  1 460 ? 11.545  22.108  31.735  1.00 18.14 ? 477  ALA B N   1 
ATOM   8050  C  CA  . ALA B  1 460 ? 10.670  23.200  31.334  1.00 18.17 ? 477  ALA B CA  1 
ATOM   8051  C  C   . ALA B  1 460 ? 11.064  23.726  29.954  1.00 18.29 ? 477  ALA B C   1 
ATOM   8052  O  O   . ALA B  1 460 ? 10.207  23.930  29.093  1.00 18.60 ? 477  ALA B O   1 
ATOM   8053  C  CB  . ALA B  1 460 ? 10.706  24.286  32.377  1.00 18.06 ? 477  ALA B CB  1 
ATOM   8054  N  N   . VAL B  1 461 ? 12.369  23.928  29.734  1.00 17.77 ? 478  VAL B N   1 
ATOM   8055  C  CA  . VAL B  1 461 ? 12.848  24.431  28.457  1.00 17.47 ? 478  VAL B CA  1 
ATOM   8056  C  C   . VAL B  1 461 ? 12.457  23.473  27.327  1.00 17.41 ? 478  VAL B C   1 
ATOM   8057  O  O   . VAL B  1 461 ? 11.983  23.903  26.269  1.00 17.61 ? 478  VAL B O   1 
ATOM   8058  C  CB  . VAL B  1 461 ? 14.369  24.674  28.516  1.00 17.69 ? 478  VAL B CB  1 
ATOM   8059  C  CG1 . VAL B  1 461 ? 14.983  24.886  27.135  1.00 17.63 ? 478  VAL B CG1 1 
ATOM   8060  C  CG2 . VAL B  1 461 ? 14.709  25.847  29.431  1.00 17.97 ? 478  VAL B CG2 1 
ATOM   8061  N  N   . ILE B  1 462 ? 12.679  22.171  27.545  1.00 17.38 ? 479  ILE B N   1 
ATOM   8062  C  CA  . ILE B  1 462 ? 12.389  21.158  26.543  1.00 17.99 ? 479  ILE B CA  1 
ATOM   8063  C  C   . ILE B  1 462 ? 10.881  21.098  26.259  1.00 18.64 ? 479  ILE B C   1 
ATOM   8064  O  O   . ILE B  1 462 ? 10.471  21.120  25.094  1.00 18.72 ? 479  ILE B O   1 
ATOM   8065  C  CB  . ILE B  1 462 ? 12.972  19.802  26.987  1.00 18.30 ? 479  ILE B CB  1 
ATOM   8066  C  CG1 . ILE B  1 462 ? 14.507  19.835  26.959  1.00 17.90 ? 479  ILE B CG1 1 
ATOM   8067  C  CG2 . ILE B  1 462 ? 12.440  18.650  26.133  1.00 18.28 ? 479  ILE B CG2 1 
ATOM   8068  C  CD1 . ILE B  1 462 ? 15.149  18.676  27.693  1.00 18.30 ? 479  ILE B CD1 1 
ATOM   8069  N  N   . LEU B  1 463 ? 10.059  21.026  27.316  1.00 18.84 ? 480  LEU B N   1 
ATOM   8070  C  CA  . LEU B  1 463 ? 8.616   20.863  27.167  1.00 19.08 ? 480  LEU B CA  1 
ATOM   8071  C  C   . LEU B  1 463 ? 7.981   22.067  26.463  1.00 19.54 ? 480  LEU B C   1 
ATOM   8072  O  O   . LEU B  1 463 ? 6.949   21.904  25.810  1.00 19.77 ? 480  LEU B O   1 
ATOM   8073  C  CB  . LEU B  1 463 ? 7.934   20.610  28.512  1.00 19.54 ? 480  LEU B CB  1 
ATOM   8074  C  CG  . LEU B  1 463 ? 8.199   19.263  29.190  1.00 20.54 ? 480  LEU B CG  1 
ATOM   8075  C  CD1 . LEU B  1 463 ? 7.320   19.109  30.423  1.00 20.46 ? 480  LEU B CD1 1 
ATOM   8076  C  CD2 . LEU B  1 463 ? 8.014   18.077  28.257  1.00 20.78 ? 480  LEU B CD2 1 
ATOM   8077  N  N   . CYS B  1 464 ? 8.593   23.260  26.584  1.00 19.64 ? 481  CYS B N   1 
ATOM   8078  C  CA  . CYS B  1 464 ? 8.052   24.492  26.025  1.00 19.58 ? 481  CYS B CA  1 
ATOM   8079  C  C   . CYS B  1 464 ? 8.619   24.795  24.637  1.00 20.15 ? 481  CYS B C   1 
ATOM   8080  O  O   . CYS B  1 464 ? 8.237   25.798  24.032  1.00 19.20 ? 481  CYS B O   1 
ATOM   8081  C  CB  . CYS B  1 464 ? 8.347   25.689  26.928  1.00 20.24 ? 481  CYS B CB  1 
ATOM   8082  S  SG  . CYS B  1 464 ? 7.475   25.664  28.517  1.00 21.36 ? 481  CYS B SG  1 
ATOM   8083  N  N   . ASN B  1 465 ? 9.519   23.933  24.134  1.00 19.93 ? 482  ASN B N   1 
ATOM   8084  C  CA  . ASN B  1 465 ? 10.205  24.140  22.865  1.00 20.36 ? 482  ASN B CA  1 
ATOM   8085  C  C   . ASN B  1 465 ? 10.921  25.495  22.861  1.00 19.79 ? 482  ASN B C   1 
ATOM   8086  O  O   . ASN B  1 465 ? 10.959  26.187  21.846  1.00 19.91 ? 482  ASN B O   1 
ATOM   8087  C  CB  . ASN B  1 465 ? 9.261   23.997  21.672  1.00 21.31 ? 482  ASN B CB  1 
ATOM   8088  C  CG  . ASN B  1 465 ? 8.765   22.584  21.452  1.00 22.11 ? 482  ASN B CG  1 
ATOM   8089  O  OD1 . ASN B  1 465 ? 9.398   21.610  21.876  1.00 23.90 ? 482  ASN B OD1 1 
ATOM   8090  N  ND2 . ASN B  1 465 ? 7.646   22.447  20.758  1.00 22.25 ? 482  ASN B ND2 1 
ATOM   8091  N  N   . THR B  1 466 ? 11.501  25.859  24.006  1.00 19.55 ? 483  THR B N   1 
ATOM   8092  C  CA  . THR B  1 466 ? 12.203  27.121  24.171  1.00 19.73 ? 483  THR B CA  1 
ATOM   8093  C  C   . THR B  1 466 ? 13.501  27.077  23.362  1.00 19.77 ? 483  THR B C   1 
ATOM   8094  O  O   . THR B  1 466 ? 14.109  26.017  23.218  1.00 19.53 ? 483  THR B O   1 
ATOM   8095  C  CB  . THR B  1 466 ? 12.432  27.332  25.670  1.00 19.94 ? 483  THR B CB  1 
ATOM   8096  O  OG1 . THR B  1 466 ? 11.159  27.675  26.204  1.00 19.77 ? 483  THR B OG1 1 
ATOM   8097  C  CG2 . THR B  1 466 ? 13.398  28.456  25.995  1.00 20.05 ? 483  THR B CG2 1 
ATOM   8098  N  N   . ARG B  1 467 ? 13.918  28.240  22.846  1.00 21.06 ? 484  ARG B N   1 
ATOM   8099  C  CA  . ARG B  1 467 ? 15.042  28.330  21.924  1.00 21.55 ? 484  ARG B CA  1 
ATOM   8100  C  C   . ARG B  1 467 ? 16.242  29.052  22.536  1.00 21.57 ? 484  ARG B C   1 
ATOM   8101  O  O   . ARG B  1 467 ? 17.367  28.837  22.084  1.00 19.81 ? 484  ARG B O   1 
ATOM   8102  C  CB  . ARG B  1 467 ? 14.601  29.040  20.643  1.00 23.01 ? 484  ARG B CB  1 
ATOM   8103  C  CG  . ARG B  1 467 ? 13.445  28.333  19.952  1.00 24.82 ? 484  ARG B CG  1 
ATOM   8104  C  CD  . ARG B  1 467 ? 12.865  29.162  18.836  1.00 26.65 ? 484  ARG B CD  1 
ATOM   8105  N  NE  . ARG B  1 467 ? 13.694  29.111  17.629  1.00 28.10 ? 484  ARG B NE  1 
ATOM   8106  C  CZ  . ARG B  1 467 ? 13.744  28.111  16.759  1.00 28.24 ? 484  ARG B CZ  1 
ATOM   8107  N  NH1 . ARG B  1 467 ? 13.026  27.017  16.951  1.00 28.12 ? 484  ARG B NH1 1 
ATOM   8108  N  NH2 . ARG B  1 467 ? 14.523  28.213  15.693  1.00 29.11 ? 484  ARG B NH2 1 
ATOM   8109  N  N   . HIS B  1 468 ? 16.003  29.932  23.522  1.00 22.21 ? 485  HIS B N   1 
ATOM   8110  C  CA  . HIS B  1 468 ? 17.076  30.606  24.240  1.00 22.18 ? 485  HIS B CA  1 
ATOM   8111  C  C   . HIS B  1 468 ? 16.714  30.710  25.719  1.00 22.07 ? 485  HIS B C   1 
ATOM   8112  O  O   . HIS B  1 468 ? 15.546  30.878  26.062  1.00 22.15 ? 485  HIS B O   1 
ATOM   8113  C  CB  . HIS B  1 468 ? 17.366  31.984  23.630  1.00 23.62 ? 485  HIS B CB  1 
ATOM   8114  C  CG  . HIS B  1 468 ? 17.512  31.936  22.147  1.00 24.65 ? 485  HIS B CG  1 
ATOM   8115  N  ND1 . HIS B  1 468 ? 18.591  31.343  21.521  1.00 24.87 ? 485  HIS B ND1 1 
ATOM   8116  C  CD2 . HIS B  1 468 ? 16.679  32.327  21.174  1.00 24.86 ? 485  HIS B CD2 1 
ATOM   8117  C  CE1 . HIS B  1 468 ? 18.416  31.408  20.207  1.00 25.31 ? 485  HIS B CE1 1 
ATOM   8118  N  NE2 . HIS B  1 468 ? 17.262  32.005  19.974  1.00 25.34 ? 485  HIS B NE2 1 
ATOM   8119  N  N   . ILE B  1 469 ? 17.735  30.609  26.583  1.00 21.55 ? 486  ILE B N   1 
ATOM   8120  C  CA  . ILE B  1 469 ? 17.560  30.638  28.027  1.00 21.78 ? 486  ILE B CA  1 
ATOM   8121  C  C   . ILE B  1 469 ? 18.181  31.922  28.584  1.00 22.45 ? 486  ILE B C   1 
ATOM   8122  O  O   . ILE B  1 469 ? 19.402  32.072  28.619  1.00 21.90 ? 486  ILE B O   1 
ATOM   8123  C  CB  . ILE B  1 469 ? 18.167  29.382  28.681  1.00 21.61 ? 486  ILE B CB  1 
ATOM   8124  C  CG1 . ILE B  1 469 ? 17.761  28.094  27.947  1.00 21.77 ? 486  ILE B CG1 1 
ATOM   8125  C  CG2 . ILE B  1 469 ? 17.801  29.322  30.162  1.00 22.05 ? 486  ILE B CG2 1 
ATOM   8126  C  CD1 . ILE B  1 469 ? 18.491  26.847  28.419  1.00 22.04 ? 486  ILE B CD1 1 
ATOM   8127  N  N   . SER B  1 470 ? 17.321  32.846  29.030  1.00 23.22 ? 487  SER B N   1 
ATOM   8128  C  CA  . SER B  1 470 ? 17.758  34.087  29.648  1.00 23.19 ? 487  SER B CA  1 
ATOM   8129  C  C   . SER B  1 470 ? 18.208  33.822  31.083  1.00 23.05 ? 487  SER B C   1 
ATOM   8130  O  O   . SER B  1 470 ? 17.864  32.800  31.669  1.00 22.06 ? 487  SER B O   1 
ATOM   8131  C  CB  . SER B  1 470 ? 16.658  35.118  29.615  1.00 23.93 ? 487  SER B CB  1 
ATOM   8132  O  OG  . SER B  1 470 ? 15.586  34.727  30.463  1.00 24.43 ? 487  SER B OG  1 
ATOM   8133  N  N   . ASP B  1 471 ? 18.938  34.780  31.665  1.00 24.32 ? 488  ASP B N   1 
ATOM   8134  C  CA  . ASP B  1 471 ? 19.346  34.682  33.059  1.00 24.86 ? 488  ASP B CA  1 
ATOM   8135  C  C   . ASP B  1 471 ? 18.117  34.712  33.975  1.00 23.54 ? 488  ASP B C   1 
ATOM   8136  O  O   . ASP B  1 471 ? 18.143  34.139  35.062  1.00 21.51 ? 488  ASP B O   1 
ATOM   8137  C  CB  . ASP B  1 471 ? 20.384  35.738  33.406  1.00 28.11 ? 488  ASP B CB  1 
ATOM   8138  C  CG  . ASP B  1 471 ? 21.836  35.406  33.071  1.00 30.91 ? 488  ASP B CG  1 
ATOM   8139  O  OD1 . ASP B  1 471 ? 22.128  34.244  32.697  1.00 31.10 ? 488  ASP B OD1 1 
ATOM   8140  O  OD2 . ASP B  1 471 ? 22.680  36.314  33.211  1.00 34.82 ? 488  ASP B OD2 1 
ATOM   8141  N  N   . SER B  1 472 ? 17.026  35.350  33.527  1.00 22.40 ? 489  SER B N   1 
ATOM   8142  C  CA  . SER B  1 472 ? 15.833  35.473  34.351  1.00 23.06 ? 489  SER B CA  1 
ATOM   8143  C  C   . SER B  1 472 ? 15.174  34.113  34.595  1.00 22.13 ? 489  SER B C   1 
ATOM   8144  O  O   . SER B  1 472 ? 14.450  33.960  35.577  1.00 22.13 ? 489  SER B O   1 
ATOM   8145  C  CB  . SER B  1 472 ? 14.863  36.472  33.768  1.00 24.79 ? 489  SER B CB  1 
ATOM   8146  O  OG  . SER B  1 472 ? 14.450  36.082  32.468  1.00 26.72 ? 489  SER B OG  1 
ATOM   8147  N  N   . VAL B  1 473 ? 15.436  33.127  33.722  1.00 20.17 ? 490  VAL B N   1 
ATOM   8148  C  CA  . VAL B  1 473 ? 14.972  31.763  33.939  1.00 19.87 ? 490  VAL B CA  1 
ATOM   8149  C  C   . VAL B  1 473 ? 15.585  31.207  35.227  1.00 19.43 ? 490  VAL B C   1 
ATOM   8150  O  O   . VAL B  1 473 ? 14.895  30.566  36.016  1.00 19.51 ? 490  VAL B O   1 
ATOM   8151  C  CB  . VAL B  1 473 ? 15.285  30.858  32.728  1.00 20.71 ? 490  VAL B CB  1 
ATOM   8152  C  CG1 . VAL B  1 473 ? 15.066  29.378  33.029  1.00 20.92 ? 490  VAL B CG1 1 
ATOM   8153  C  CG2 . VAL B  1 473 ? 14.496  31.271  31.493  1.00 20.74 ? 490  VAL B CG2 1 
ATOM   8154  N  N   . PHE B  1 474 ? 16.886  31.450  35.434  1.00 19.55 ? 491  PHE B N   1 
ATOM   8155  C  CA  . PHE B  1 474 ? 17.582  30.961  36.615  1.00 19.79 ? 491  PHE B CA  1 
ATOM   8156  C  C   . PHE B  1 474 ? 17.112  31.722  37.854  1.00 20.18 ? 491  PHE B C   1 
ATOM   8157  O  O   . PHE B  1 474 ? 17.033  31.146  38.931  1.00 20.03 ? 491  PHE B O   1 
ATOM   8158  C  CB  . PHE B  1 474 ? 19.094  31.033  36.374  1.00 19.72 ? 491  PHE B CB  1 
ATOM   8159  C  CG  . PHE B  1 474 ? 19.511  30.014  35.329  1.00 20.09 ? 491  PHE B CG  1 
ATOM   8160  C  CD1 . PHE B  1 474 ? 19.656  28.673  35.673  1.00 20.14 ? 491  PHE B CD1 1 
ATOM   8161  C  CD2 . PHE B  1 474 ? 19.678  30.381  33.996  1.00 20.42 ? 491  PHE B CD2 1 
ATOM   8162  C  CE1 . PHE B  1 474 ? 19.982  27.727  34.714  1.00 19.77 ? 491  PHE B CE1 1 
ATOM   8163  C  CE2 . PHE B  1 474 ? 20.013  29.432  33.045  1.00 20.36 ? 491  PHE B CE2 1 
ATOM   8164  C  CZ  . PHE B  1 474 ? 20.158  28.109  33.406  1.00 20.15 ? 491  PHE B CZ  1 
ATOM   8165  N  N   . LEU B  1 475 ? 16.791  33.012  37.710  1.00 20.87 ? 492  LEU B N   1 
ATOM   8166  C  CA  . LEU B  1 475 ? 16.232  33.764  38.826  1.00 21.63 ? 492  LEU B CA  1 
ATOM   8167  C  C   . LEU B  1 475 ? 14.893  33.146  39.244  1.00 21.71 ? 492  LEU B C   1 
ATOM   8168  O  O   . LEU B  1 475 ? 14.649  32.943  40.431  1.00 21.63 ? 492  LEU B O   1 
ATOM   8169  C  CB  . LEU B  1 475 ? 16.083  35.241  38.471  1.00 22.71 ? 492  LEU B CB  1 
ATOM   8170  C  CG  . LEU B  1 475 ? 15.419  36.126  39.532  1.00 23.31 ? 492  LEU B CG  1 
ATOM   8171  C  CD1 . LEU B  1 475 ? 16.161  36.065  40.848  1.00 23.63 ? 492  LEU B CD1 1 
ATOM   8172  C  CD2 . LEU B  1 475 ? 15.315  37.556  39.052  1.00 24.32 ? 492  LEU B CD2 1 
ATOM   8173  N  N   A GLU B  1 476 ? 14.046  32.838  38.253  0.50 22.10 ? 493  GLU B N   1 
ATOM   8174  N  N   B GLU B  1 476 ? 14.041  32.837  38.260  0.50 21.90 ? 493  GLU B N   1 
ATOM   8175  C  CA  A GLU B  1 476 ? 12.740  32.239  38.493  0.50 22.63 ? 493  GLU B CA  1 
ATOM   8176  C  CA  B GLU B  1 476 ? 12.739  32.239  38.524  0.50 22.25 ? 493  GLU B CA  1 
ATOM   8177  C  C   A GLU B  1 476 ? 12.897  30.876  39.164  0.50 21.69 ? 493  GLU B C   1 
ATOM   8178  C  C   B GLU B  1 476 ? 12.898  30.869  39.176  0.50 21.50 ? 493  GLU B C   1 
ATOM   8179  O  O   A GLU B  1 476 ? 12.115  30.530  40.046  0.50 22.01 ? 493  GLU B O   1 
ATOM   8180  O  O   B GLU B  1 476 ? 12.118  30.510  40.054  0.50 21.83 ? 493  GLU B O   1 
ATOM   8181  C  CB  A GLU B  1 476 ? 11.957  32.081  37.190  0.50 23.75 ? 493  GLU B CB  1 
ATOM   8182  C  CB  B GLU B  1 476 ? 11.912  32.106  37.248  0.50 23.03 ? 493  GLU B CB  1 
ATOM   8183  C  CG  A GLU B  1 476 ? 10.526  31.596  37.404  0.50 24.81 ? 493  GLU B CG  1 
ATOM   8184  C  CG  B GLU B  1 476 ? 11.344  33.438  36.770  0.50 23.71 ? 493  GLU B CG  1 
ATOM   8185  C  CD  A GLU B  1 476 ? 9.550   32.656  37.886  0.50 25.94 ? 493  GLU B CD  1 
ATOM   8186  C  CD  B GLU B  1 476 ? 10.680  34.250  37.867  0.50 24.49 ? 493  GLU B CD  1 
ATOM   8187  O  OE1 A GLU B  1 476 ? 9.804   33.861  37.683  0.50 26.91 ? 493  GLU B OE1 1 
ATOM   8188  O  OE1 B GLU B  1 476 ? 9.886   33.660  38.636  0.50 25.00 ? 493  GLU B OE1 1 
ATOM   8189  O  OE2 A GLU B  1 476 ? 8.526   32.265  38.482  0.50 28.07 ? 493  GLU B OE2 1 
ATOM   8190  O  OE2 B GLU B  1 476 ? 10.950  35.468  37.945  0.50 24.17 ? 493  GLU B OE2 1 
ATOM   8191  N  N   . ALA B  1 477 ? 13.914  30.113  38.745  1.00 21.35 ? 494  ALA B N   1 
ATOM   8192  C  CA  . ALA B  1 477 ? 14.189  28.802  39.314  1.00 21.30 ? 494  ALA B CA  1 
ATOM   8193  C  C   . ALA B  1 477 ? 14.582  28.917  40.786  1.00 20.97 ? 494  ALA B C   1 
ATOM   8194  O  O   . ALA B  1 477 ? 14.126  28.118  41.601  1.00 21.61 ? 494  ALA B O   1 
ATOM   8195  C  CB  . ALA B  1 477 ? 15.262  28.097  38.515  1.00 21.51 ? 494  ALA B CB  1 
ATOM   8196  N  N   . ALA B  1 478 ? 15.423  29.907  41.116  1.00 20.40 ? 495  ALA B N   1 
ATOM   8197  C  CA  . ALA B  1 478 ? 15.876  30.116  42.486  1.00 19.96 ? 495  ALA B CA  1 
ATOM   8198  C  C   . ALA B  1 478 ? 14.690  30.408  43.405  1.00 20.44 ? 495  ALA B C   1 
ATOM   8199  O  O   . ALA B  1 478 ? 14.572  29.817  44.476  1.00 20.58 ? 495  ALA B O   1 
ATOM   8200  C  CB  . ALA B  1 478 ? 16.887  31.239  42.532  1.00 19.95 ? 495  ALA B CB  1 
ATOM   8201  N  N   . LYS B  1 479 ? 13.824  31.332  42.973  1.00 21.29 ? 496  LYS B N   1 
ATOM   8202  C  CA  . LYS B  1 479 ? 12.623  31.689  43.713  1.00 22.72 ? 496  LYS B CA  1 
ATOM   8203  C  C   . LYS B  1 479 ? 11.713  30.476  43.873  1.00 22.99 ? 496  LYS B C   1 
ATOM   8204  O  O   . LYS B  1 479 ? 11.111  30.305  44.930  1.00 22.85 ? 496  LYS B O   1 
ATOM   8205  C  CB  . LYS B  1 479 ? 11.868  32.839  43.036  1.00 23.74 ? 496  LYS B CB  1 
ATOM   8206  C  CG  . LYS B  1 479 ? 12.622  34.152  43.053  1.00 25.75 ? 496  LYS B CG  1 
ATOM   8207  C  CD  . LYS B  1 479 ? 11.870  35.354  42.497  1.00 28.02 ? 496  LYS B CD  1 
ATOM   8208  C  CE  . LYS B  1 479 ? 11.626  35.262  41.030  1.00 29.77 ? 496  LYS B CE  1 
ATOM   8209  N  NZ  . LYS B  1 479 ? 11.213  36.552  40.473  1.00 30.31 ? 496  LYS B NZ  1 
ATOM   8210  N  N   . ALA B  1 480 ? 11.610  29.649  42.821  1.00 23.27 ? 497  ALA B N   1 
ATOM   8211  C  CA  . ALA B  1 480 ? 10.742  28.480  42.836  1.00 24.20 ? 497  ALA B CA  1 
ATOM   8212  C  C   . ALA B  1 480 ? 11.286  27.406  43.776  1.00 24.25 ? 497  ALA B C   1 
ATOM   8213  O  O   . ALA B  1 480 ? 10.511  26.647  44.347  1.00 24.74 ? 497  ALA B O   1 
ATOM   8214  C  CB  . ALA B  1 480 ? 10.558  27.935  41.432  1.00 24.35 ? 497  ALA B CB  1 
ATOM   8215  N  N   . LEU B  1 481 ? 12.614  27.334  43.926  1.00 23.01 ? 498  LEU B N   1 
ATOM   8216  C  CA  . LEU B  1 481 ? 13.224  26.404  44.863  1.00 23.20 ? 498  LEU B CA  1 
ATOM   8217  C  C   . LEU B  1 481 ? 12.910  26.822  46.302  1.00 23.15 ? 498  LEU B C   1 
ATOM   8218  O  O   . LEU B  1 481 ? 12.449  26.007  47.095  1.00 24.69 ? 498  LEU B O   1 
ATOM   8219  C  CB  . LEU B  1 481 ? 14.732  26.316  44.617  1.00 22.13 ? 498  LEU B CB  1 
ATOM   8220  C  CG  . LEU B  1 481 ? 15.518  25.403  45.564  1.00 22.15 ? 498  LEU B CG  1 
ATOM   8221  C  CD1 . LEU B  1 481 ? 15.015  23.976  45.541  1.00 22.65 ? 498  LEU B CD1 1 
ATOM   8222  C  CD2 . LEU B  1 481 ? 17.005  25.431  45.240  1.00 22.19 ? 498  LEU B CD2 1 
ATOM   8223  N  N   . THR B  1 482 ? 13.158  28.092  46.634  1.00 23.94 ? 499  THR B N   1 
ATOM   8224  C  CA  . THR B  1 482 ? 13.023  28.578  48.001  1.00 25.26 ? 499  THR B CA  1 
ATOM   8225  C  C   . THR B  1 482 ? 11.560  28.538  48.457  1.00 26.05 ? 499  THR B C   1 
ATOM   8226  O  O   . THR B  1 482 ? 11.290  28.359  49.643  1.00 24.78 ? 499  THR B O   1 
ATOM   8227  C  CB  . THR B  1 482 ? 13.611  29.984  48.093  1.00 25.59 ? 499  THR B CB  1 
ATOM   8228  O  OG1 . THR B  1 482 ? 15.008  29.756  47.930  1.00 28.04 ? 499  THR B OG1 1 
ATOM   8229  C  CG2 . THR B  1 482 ? 13.352  30.653  49.431  1.00 25.77 ? 499  THR B CG2 1 
ATOM   8230  N  N   . SER B  1 483 ? 10.617  28.656  47.515  1.00 26.82 ? 500  SER B N   1 
ATOM   8231  C  CA  . SER B  1 483 ? 9.200   28.685  47.854  1.00 28.88 ? 500  SER B CA  1 
ATOM   8232  C  C   . SER B  1 483 ? 8.669   27.322  48.316  1.00 29.22 ? 500  SER B C   1 
ATOM   8233  O  O   . SER B  1 483 ? 7.543   27.253  48.803  1.00 29.67 ? 500  SER B O   1 
ATOM   8234  C  CB  . SER B  1 483 ? 8.378   29.213  46.700  1.00 29.03 ? 500  SER B CB  1 
ATOM   8235  O  OG  . SER B  1 483 ? 8.239   28.213  45.702  1.00 30.93 ? 500  SER B OG  1 
ATOM   8236  N  N   A GLN B  1 484 ? 9.469   26.257  48.197  0.63 28.37 ? 501  GLN B N   1 
ATOM   8237  N  N   B GLN B  1 484 ? 9.468   26.255  48.140  0.37 29.55 ? 501  GLN B N   1 
ATOM   8238  C  CA  A GLN B  1 484 ? 9.014   24.930  48.578  0.63 28.35 ? 501  GLN B CA  1 
ATOM   8239  C  CA  B GLN B  1 484 ? 9.091   24.905  48.539  0.37 30.13 ? 501  GLN B CA  1 
ATOM   8240  C  C   A GLN B  1 484 ? 9.408   24.603  50.016  0.63 28.73 ? 501  GLN B C   1 
ATOM   8241  C  C   B GLN B  1 484 ? 9.287   24.684  50.039  0.37 29.97 ? 501  GLN B C   1 
ATOM   8242  O  O   A GLN B  1 484 ? 9.119   23.509  50.495  0.63 27.54 ? 501  GLN B O   1 
ATOM   8243  O  O   B GLN B  1 484 ? 8.734   23.735  50.590  0.37 30.01 ? 501  GLN B O   1 
ATOM   8244  C  CB  A GLN B  1 484 ? 9.572   23.895  47.607  0.63 27.71 ? 501  GLN B CB  1 
ATOM   8245  C  CB  B GLN B  1 484 ? 9.909   23.823  47.828  0.37 30.66 ? 501  GLN B CB  1 
ATOM   8246  C  CG  A GLN B  1 484 ? 9.121   24.119  46.169  0.63 26.89 ? 501  GLN B CG  1 
ATOM   8247  C  CG  B GLN B  1 484 ? 9.260   23.257  46.568  0.37 31.15 ? 501  GLN B CG  1 
ATOM   8248  C  CD  A GLN B  1 484 ? 9.472   22.960  45.270  0.63 25.62 ? 501  GLN B CD  1 
ATOM   8249  C  CD  B GLN B  1 484 ? 9.093   24.283  45.472  0.37 31.19 ? 501  GLN B CD  1 
ATOM   8250  O  OE1 A GLN B  1 484 ? 8.942   21.857  45.422  0.63 25.17 ? 501  GLN B OE1 1 
ATOM   8251  O  OE1 B GLN B  1 484 ? 8.334   25.250  45.605  0.37 32.00 ? 501  GLN B OE1 1 
ATOM   8252  N  NE2 A GLN B  1 484 ? 10.368  23.199  44.325  0.63 26.09 ? 501  GLN B NE2 1 
ATOM   8253  N  NE2 B GLN B  1 484 ? 9.806   24.081  44.375  0.37 31.42 ? 501  GLN B NE2 1 
ATOM   8254  N  N   . LEU B  1 485 ? 10.088  25.539  50.690  1.00 29.47 ? 502  LEU B N   1 
ATOM   8255  C  CA  . LEU B  1 485 ? 10.369  25.404  52.113  1.00 29.16 ? 502  LEU B CA  1 
ATOM   8256  C  C   . LEU B  1 485 ? 9.094   25.678  52.905  1.00 30.30 ? 502  LEU B C   1 
ATOM   8257  O  O   . LEU B  1 485 ? 8.464   26.709  52.710  1.00 28.98 ? 502  LEU B O   1 
ATOM   8258  C  CB  . LEU B  1 485 ? 11.486  26.363  52.523  1.00 29.84 ? 502  LEU B CB  1 
ATOM   8259  C  CG  . LEU B  1 485 ? 12.901  25.954  52.108  1.00 29.81 ? 502  LEU B CG  1 
ATOM   8260  C  CD1 . LEU B  1 485 ? 13.873  27.111  52.252  1.00 30.40 ? 502  LEU B CD1 1 
ATOM   8261  C  CD2 . LEU B  1 485 ? 13.368  24.768  52.927  1.00 29.95 ? 502  LEU B CD2 1 
ATOM   8262  N  N   . THR B  1 486 ? 8.720   24.749  53.793  1.00 35.04 ? 503  THR B N   1 
ATOM   8263  C  CA  . THR B  1 486 ? 7.557   24.936  54.650  1.00 38.92 ? 503  THR B CA  1 
ATOM   8264  C  C   . THR B  1 486 ? 7.941   25.851  55.813  1.00 40.95 ? 503  THR B C   1 
ATOM   8265  O  O   . THR B  1 486 ? 9.118   25.976  56.154  1.00 37.02 ? 503  THR B O   1 
ATOM   8266  C  CB  . THR B  1 486 ? 7.033   23.585  55.143  1.00 40.10 ? 503  THR B CB  1 
ATOM   8267  O  OG1 . THR B  1 486 ? 8.063   23.018  55.946  1.00 40.95 ? 503  THR B OG1 1 
ATOM   8268  C  CG2 . THR B  1 486 ? 6.689   22.627  54.015  1.00 39.42 ? 503  THR B CG2 1 
ATOM   8269  N  N   . ASP B  1 487 ? 6.930   26.490  56.414  1.00 44.91 ? 504  ASP B N   1 
ATOM   8270  C  CA  . ASP B  1 487 ? 7.121   27.348  57.575  1.00 48.54 ? 504  ASP B CA  1 
ATOM   8271  C  C   . ASP B  1 487 ? 7.884   26.602  58.669  1.00 47.56 ? 504  ASP B C   1 
ATOM   8272  O  O   . ASP B  1 487 ? 8.775   27.168  59.295  1.00 49.07 ? 504  ASP B O   1 
ATOM   8273  C  CB  . ASP B  1 487 ? 5.792   27.887  58.084  1.00 50.75 ? 504  ASP B CB  1 
ATOM   8274  C  CG  . ASP B  1 487 ? 5.163   28.986  57.240  1.00 53.44 ? 504  ASP B CG  1 
ATOM   8275  O  OD1 . ASP B  1 487 ? 5.835   29.474  56.305  1.00 52.69 ? 504  ASP B OD1 1 
ATOM   8276  O  OD2 . ASP B  1 487 ? 4.002   29.344  57.524  1.00 56.84 ? 504  ASP B OD2 1 
ATOM   8277  N  N   . GLU B  1 488 ? 7.536   25.327  58.878  1.00 47.61 ? 505  GLU B N   1 
ATOM   8278  C  CA  . GLU B  1 488 ? 8.193   24.492  59.871  1.00 48.22 ? 505  GLU B CA  1 
ATOM   8279  C  C   . GLU B  1 488 ? 9.683   24.360  59.555  1.00 45.78 ? 505  GLU B C   1 
ATOM   8280  O  O   . GLU B  1 488 ? 10.515  24.434  60.455  1.00 43.84 ? 505  GLU B O   1 
ATOM   8281  C  CB  . GLU B  1 488 ? 7.533   23.113  59.914  1.00 51.47 ? 505  GLU B CB  1 
ATOM   8282  C  CG  . GLU B  1 488 ? 7.962   22.253  61.100  1.00 55.85 ? 505  GLU B CG  1 
ATOM   8283  C  CD  . GLU B  1 488 ? 7.486   20.812  61.011  1.00 60.35 ? 505  GLU B CD  1 
ATOM   8284  O  OE1 . GLU B  1 488 ? 8.123   20.019  60.281  1.00 63.67 ? 505  GLU B OE1 1 
ATOM   8285  O  OE2 . GLU B  1 488 ? 6.461   20.486  61.648  1.00 62.29 ? 505  GLU B OE2 1 
ATOM   8286  N  N   . GLU B  1 489 ? 10.012  24.147  58.276  1.00 44.58 ? 506  GLU B N   1 
ATOM   8287  C  CA  . GLU B  1 489 ? 11.394  23.965  57.852  1.00 42.81 ? 506  GLU B CA  1 
ATOM   8288  C  C   . GLU B  1 489 ? 12.194  25.250  58.066  1.00 40.82 ? 506  GLU B C   1 
ATOM   8289  O  O   . GLU B  1 489 ? 13.347  25.197  58.488  1.00 41.60 ? 506  GLU B O   1 
ATOM   8290  C  CB  . GLU B  1 489 ? 11.464  23.520  56.391  1.00 43.23 ? 506  GLU B CB  1 
ATOM   8291  C  CG  . GLU B  1 489 ? 11.148  22.040  56.203  1.00 44.06 ? 506  GLU B CG  1 
ATOM   8292  C  CD  . GLU B  1 489 ? 10.943  21.608  54.764  1.00 44.82 ? 506  GLU B CD  1 
ATOM   8293  O  OE1 . GLU B  1 489 ? 11.108  20.399  54.510  1.00 46.97 ? 506  GLU B OE1 1 
ATOM   8294  O  OE2 . GLU B  1 489 ? 10.596  22.453  53.912  1.00 44.58 ? 506  GLU B OE2 1 
ATOM   8295  N  N   . LEU B  1 490 ? 11.578  26.397  57.764  1.00 41.79 ? 507  LEU B N   1 
ATOM   8296  C  CA  . LEU B  1 490 ? 12.217  27.691  57.953  1.00 42.75 ? 507  LEU B CA  1 
ATOM   8297  C  C   . LEU B  1 490 ? 12.447  27.954  59.443  1.00 45.86 ? 507  LEU B C   1 
ATOM   8298  O  O   . LEU B  1 490 ? 13.443  28.573  59.811  1.00 45.27 ? 507  LEU B O   1 
ATOM   8299  C  CB  . LEU B  1 490 ? 11.362  28.777  57.302  1.00 41.84 ? 507  LEU B CB  1 
ATOM   8300  C  CG  . LEU B  1 490 ? 11.322  28.764  55.769  1.00 41.68 ? 507  LEU B CG  1 
ATOM   8301  C  CD1 . LEU B  1 490 ? 10.136  29.542  55.240  1.00 41.02 ? 507  LEU B CD1 1 
ATOM   8302  C  CD2 . LEU B  1 490 ? 12.613  29.317  55.180  1.00 41.98 ? 507  LEU B CD2 1 
ATOM   8303  N  N   . ALA B  1 491 ? 11.536  27.461  60.295  1.00 47.20 ? 508  ALA B N   1 
ATOM   8304  C  CA  . ALA B  1 491 ? 11.662  27.615  61.738  1.00 46.67 ? 508  ALA B CA  1 
ATOM   8305  C  C   . ALA B  1 491 ? 12.774  26.721  62.290  1.00 46.87 ? 508  ALA B C   1 
ATOM   8306  O  O   . ALA B  1 491 ? 13.345  27.030  63.333  1.00 49.69 ? 508  ALA B O   1 
ATOM   8307  C  CB  . ALA B  1 491 ? 10.333  27.328  62.405  1.00 46.94 ? 508  ALA B CB  1 
ATOM   8308  N  N   . GLN B  1 492 ? 13.075  25.617  61.591  1.00 46.88 ? 509  GLN B N   1 
ATOM   8309  C  CA  . GLN B  1 492 ? 14.206  24.762  61.927  1.00 48.39 ? 509  GLN B CA  1 
ATOM   8310  C  C   . GLN B  1 492 ? 15.506  25.295  61.317  1.00 46.65 ? 509  GLN B C   1 
ATOM   8311  O  O   . GLN B  1 492 ? 16.578  24.753  61.579  1.00 48.42 ? 509  GLN B O   1 
ATOM   8312  C  CB  . GLN B  1 492 ? 13.991  23.335  61.421  1.00 52.58 ? 509  GLN B CB  1 
ATOM   8313  C  CG  . GLN B  1 492 ? 12.841  22.586  62.085  1.00 56.38 ? 509  GLN B CG  1 
ATOM   8314  C  CD  . GLN B  1 492 ? 12.643  21.200  61.507  1.00 61.51 ? 509  GLN B CD  1 
ATOM   8315  O  OE1 . GLN B  1 492 ? 13.477  20.303  61.680  1.00 64.07 ? 509  GLN B OE1 1 
ATOM   8316  N  NE2 . GLN B  1 492 ? 11.535  21.010  60.805  1.00 63.71 ? 509  GLN B NE2 1 
ATOM   8317  N  N   . GLY B  1 493 ? 15.407  26.329  60.472  1.00 44.58 ? 510  GLY B N   1 
ATOM   8318  C  CA  . GLY B  1 493 ? 16.574  26.964  59.878  1.00 44.64 ? 510  GLY B CA  1 
ATOM   8319  C  C   . GLY B  1 493 ? 17.140  26.177  58.693  1.00 42.14 ? 510  GLY B C   1 
ATOM   8320  O  O   . GLY B  1 493 ? 18.349  26.184  58.466  1.00 41.55 ? 510  GLY B O   1 
ATOM   8321  N  N   . ARG B  1 494 ? 16.265  25.508  57.931  1.00 39.64 ? 511  ARG B N   1 
ATOM   8322  C  CA  . ARG B  1 494 ? 16.671  24.853  56.696  1.00 38.91 ? 511  ARG B CA  1 
ATOM   8323  C  C   . ARG B  1 494 ? 16.720  25.890  55.577  1.00 31.89 ? 511  ARG B C   1 
ATOM   8324  O  O   . ARG B  1 494 ? 15.864  26.771  55.516  1.00 30.30 ? 511  ARG B O   1 
ATOM   8325  C  CB  . ARG B  1 494 ? 15.713  23.722  56.304  1.00 43.77 ? 511  ARG B CB  1 
ATOM   8326  C  CG  . ARG B  1 494 ? 15.604  22.596  57.322  1.00 48.60 ? 511  ARG B CG  1 
ATOM   8327  C  CD  . ARG B  1 494 ? 15.072  21.325  56.673  1.00 54.97 ? 511  ARG B CD  1 
ATOM   8328  N  NE  . ARG B  1 494 ? 14.534  20.340  57.621  1.00 60.20 ? 511  ARG B NE  1 
ATOM   8329  C  CZ  . ARG B  1 494 ? 15.207  19.713  58.582  1.00 61.24 ? 511  ARG B CZ  1 
ATOM   8330  N  NH1 . ARG B  1 494 ? 16.484  19.977  58.795  1.00 63.07 ? 511  ARG B NH1 1 
ATOM   8331  N  NH2 . ARG B  1 494 ? 14.593  18.818  59.337  1.00 62.94 ? 511  ARG B NH2 1 
ATOM   8332  N  N   . LEU B  1 495 ? 17.731  25.780  54.705  1.00 28.12 ? 512  LEU B N   1 
ATOM   8333  C  CA  . LEU B  1 495 ? 17.940  26.743  53.634  1.00 26.64 ? 512  LEU B CA  1 
ATOM   8334  C  C   . LEU B  1 495 ? 17.547  26.161  52.277  1.00 26.26 ? 512  LEU B C   1 
ATOM   8335  O  O   . LEU B  1 495 ? 17.421  26.913  51.311  1.00 24.98 ? 512  LEU B O   1 
ATOM   8336  C  CB  . LEU B  1 495 ? 19.398  27.196  53.653  1.00 27.28 ? 512  LEU B CB  1 
ATOM   8337  C  CG  . LEU B  1 495 ? 19.818  28.008  54.883  1.00 26.64 ? 512  LEU B CG  1 
ATOM   8338  C  CD1 . LEU B  1 495 ? 21.308  28.300  54.860  1.00 27.10 ? 512  LEU B CD1 1 
ATOM   8339  C  CD2 . LEU B  1 495 ? 19.022  29.295  54.960  1.00 25.53 ? 512  LEU B CD2 1 
ATOM   8340  N  N   . TYR B  1 496 ? 17.344  24.836  52.227  1.00 25.55 ? 513  TYR B N   1 
ATOM   8341  C  CA  . TYR B  1 496 ? 17.002  24.123  51.004  1.00 25.91 ? 513  TYR B CA  1 
ATOM   8342  C  C   . TYR B  1 496 ? 16.063  22.966  51.336  1.00 26.86 ? 513  TYR B C   1 
ATOM   8343  O  O   . TYR B  1 496 ? 16.179  22.362  52.403  1.00 26.09 ? 513  TYR B O   1 
ATOM   8344  C  CB  . TYR B  1 496 ? 18.212  23.504  50.301  1.00 25.69 ? 513  TYR B CB  1 
ATOM   8345  C  CG  . TYR B  1 496 ? 19.244  24.517  49.833  1.00 25.40 ? 513  TYR B CG  1 
ATOM   8346  C  CD1 . TYR B  1 496 ? 19.039  25.262  48.678  1.00 24.78 ? 513  TYR B CD1 1 
ATOM   8347  C  CD2 . TYR B  1 496 ? 20.418  24.729  50.546  1.00 25.32 ? 513  TYR B CD2 1 
ATOM   8348  C  CE1 . TYR B  1 496 ? 19.972  26.189  48.250  1.00 25.05 ? 513  TYR B CE1 1 
ATOM   8349  C  CE2 . TYR B  1 496 ? 21.355  25.661  50.131  1.00 25.62 ? 513  TYR B CE2 1 
ATOM   8350  C  CZ  . TYR B  1 496 ? 21.136  26.383  48.973  1.00 25.02 ? 513  TYR B CZ  1 
ATOM   8351  O  OH  . TYR B  1 496 ? 22.048  27.307  48.553  1.00 25.81 ? 513  TYR B OH  1 
ATOM   8352  N  N   . PRO B  1 497 ? 15.123  22.604  50.431  1.00 27.81 ? 514  PRO B N   1 
ATOM   8353  C  CA  . PRO B  1 497 ? 14.262  21.443  50.653  1.00 27.27 ? 514  PRO B CA  1 
ATOM   8354  C  C   . PRO B  1 497 ? 15.103  20.175  50.758  1.00 28.33 ? 514  PRO B C   1 
ATOM   8355  O  O   . PRO B  1 497 ? 16.241  20.147  50.292  1.00 27.97 ? 514  PRO B O   1 
ATOM   8356  C  CB  . PRO B  1 497 ? 13.312  21.421  49.448  1.00 27.87 ? 514  PRO B CB  1 
ATOM   8357  C  CG  . PRO B  1 497 ? 13.406  22.816  48.866  1.00 28.40 ? 514  PRO B CG  1 
ATOM   8358  C  CD  . PRO B  1 497 ? 14.813  23.307  49.176  1.00 27.56 ? 514  PRO B CD  1 
ATOM   8359  N  N   . PRO B  1 498 ? 14.576  19.095  51.378  1.00 28.18 ? 515  PRO B N   1 
ATOM   8360  C  CA  . PRO B  1 498 ? 15.324  17.843  51.501  1.00 28.45 ? 515  PRO B CA  1 
ATOM   8361  C  C   . PRO B  1 498 ? 15.680  17.271  50.130  1.00 29.08 ? 515  PRO B C   1 
ATOM   8362  O  O   . PRO B  1 498 ? 14.833  17.243  49.240  1.00 28.00 ? 515  PRO B O   1 
ATOM   8363  C  CB  . PRO B  1 498 ? 14.396  16.896  52.293  1.00 29.09 ? 515  PRO B CB  1 
ATOM   8364  C  CG  . PRO B  1 498 ? 13.293  17.778  52.841  1.00 29.53 ? 515  PRO B CG  1 
ATOM   8365  C  CD  . PRO B  1 498 ? 13.231  19.025  51.973  1.00 28.66 ? 515  PRO B CD  1 
ATOM   8366  N  N   . LEU B  1 499 ? 16.922  16.786  49.979  1.00 29.71 ? 516  LEU B N   1 
ATOM   8367  C  CA  . LEU B  1 499 ? 17.362  16.156  48.740  1.00 30.36 ? 516  LEU B CA  1 
ATOM   8368  C  C   . LEU B  1 499 ? 16.544  14.896  48.463  1.00 29.30 ? 516  LEU B C   1 
ATOM   8369  O  O   . LEU B  1 499 ? 16.389  14.509  47.308  1.00 28.83 ? 516  LEU B O   1 
ATOM   8370  C  CB  . LEU B  1 499 ? 18.855  15.822  48.761  1.00 32.17 ? 516  LEU B CB  1 
ATOM   8371  C  CG  . LEU B  1 499 ? 19.821  16.955  48.404  1.00 35.27 ? 516  LEU B CG  1 
ATOM   8372  C  CD1 . LEU B  1 499 ? 21.252  16.524  48.680  1.00 36.46 ? 516  LEU B CD1 1 
ATOM   8373  C  CD2 . LEU B  1 499 ? 19.684  17.393  46.957  1.00 35.39 ? 516  LEU B CD2 1 
ATOM   8374  N  N   . ALA B  1 500 ? 16.043  14.243  49.521  1.00 28.91 ? 517  ALA B N   1 
ATOM   8375  C  CA  . ALA B  1 500 ? 15.213  13.054  49.365  1.00 28.59 ? 517  ALA B CA  1 
ATOM   8376  C  C   . ALA B  1 500 ? 13.982  13.342  48.505  1.00 26.83 ? 517  ALA B C   1 
ATOM   8377  O  O   . ALA B  1 500 ? 13.458  12.434  47.859  1.00 26.39 ? 517  ALA B O   1 
ATOM   8378  C  CB  . ALA B  1 500 ? 14.814  12.510  50.723  1.00 28.95 ? 517  ALA B CB  1 
ATOM   8379  N  N   . ASN B  1 501 ? 13.530  14.602  48.491  1.00 26.04 ? 518  ASN B N   1 
ATOM   8380  C  CA  . ASN B  1 501 ? 12.332  14.994  47.764  1.00 27.35 ? 518  ASN B CA  1 
ATOM   8381  C  C   . ASN B  1 501 ? 12.670  15.604  46.404  1.00 24.92 ? 518  ASN B C   1 
ATOM   8382  O  O   . ASN B  1 501 ? 11.853  16.333  45.851  1.00 24.16 ? 518  ASN B O   1 
ATOM   8383  C  CB  . ASN B  1 501 ? 11.523  16.034  48.535  1.00 29.08 ? 518  ASN B CB  1 
ATOM   8384  C  CG  . ASN B  1 501 ? 11.124  15.571  49.915  1.00 31.94 ? 518  ASN B CG  1 
ATOM   8385  O  OD1 . ASN B  1 501 ? 11.213  14.380  50.229  1.00 33.84 ? 518  ASN B OD1 1 
ATOM   8386  N  ND2 . ASN B  1 501 ? 10.662  16.496  50.743  1.00 33.68 ? 518  ASN B ND2 1 
ATOM   8387  N  N   . ILE B  1 502 ? 13.855  15.302  45.859  1.00 23.94 ? 519  ILE B N   1 
ATOM   8388  C  CA  . ILE B  1 502 ? 14.361  16.024  44.697  1.00 23.87 ? 519  ILE B CA  1 
ATOM   8389  C  C   . ILE B  1 502 ? 13.410  15.879  43.508  1.00 23.61 ? 519  ILE B C   1 
ATOM   8390  O  O   . ILE B  1 502 ? 13.297  16.805  42.706  1.00 23.66 ? 519  ILE B O   1 
ATOM   8391  C  CB  . ILE B  1 502 ? 15.806  15.602  44.347  1.00 22.85 ? 519  ILE B CB  1 
ATOM   8392  C  CG1 . ILE B  1 502 ? 16.401  16.471  43.244  1.00 22.38 ? 519  ILE B CG1 1 
ATOM   8393  C  CG2 . ILE B  1 502 ? 15.905  14.118  43.993  1.00 23.47 ? 519  ILE B CG2 1 
ATOM   8394  C  CD1 . ILE B  1 502 ? 16.480  17.947  43.586  1.00 22.37 ? 519  ILE B CD1 1 
ATOM   8395  N  N   . GLN B  1 503 ? 12.728  14.731  43.377  1.00 25.14 ? 520  GLN B N   1 
ATOM   8396  C  CA  . GLN B  1 503 ? 11.827  14.527  42.249  1.00 26.26 ? 520  GLN B CA  1 
ATOM   8397  C  C   . GLN B  1 503 ? 10.698  15.556  42.290  1.00 25.47 ? 520  GLN B C   1 
ATOM   8398  O  O   . GLN B  1 503 ? 10.458  16.255  41.310  1.00 24.63 ? 520  GLN B O   1 
ATOM   8399  C  CB  . GLN B  1 503 ? 11.227  13.123  42.161  1.00 28.05 ? 520  GLN B CB  1 
ATOM   8400  C  CG  . GLN B  1 503 ? 12.223  12.043  41.755  1.00 29.50 ? 520  GLN B CG  1 
ATOM   8401  C  CD  . GLN B  1 503 ? 11.557  10.769  41.275  1.00 32.90 ? 520  GLN B CD  1 
ATOM   8402  O  OE1 . GLN B  1 503 ? 10.849  10.752  40.260  1.00 35.05 ? 520  GLN B OE1 1 
ATOM   8403  N  NE2 . GLN B  1 503 ? 11.790  9.679   41.991  1.00 33.44 ? 520  GLN B NE2 1 
ATOM   8404  N  N   . GLU B  1 504 ? 10.002  15.643  43.427  1.00 26.26 ? 521  GLU B N   1 
ATOM   8405  C  CA  . GLU B  1 504 ? 8.891   16.571  43.574  1.00 27.18 ? 521  GLU B CA  1 
ATOM   8406  C  C   . GLU B  1 504 ? 9.380   18.014  43.425  1.00 25.96 ? 521  GLU B C   1 
ATOM   8407  O  O   . GLU B  1 504 ? 8.693   18.841  42.826  1.00 23.79 ? 521  GLU B O   1 
ATOM   8408  C  CB  . GLU B  1 504 ? 8.209   16.348  44.924  1.00 30.06 ? 521  GLU B CB  1 
ATOM   8409  C  CG  . GLU B  1 504 ? 7.093   17.343  45.236  1.00 32.64 ? 521  GLU B CG  1 
ATOM   8410  C  CD  . GLU B  1 504 ? 6.505   17.204  46.635  1.00 36.83 ? 521  GLU B CD  1 
ATOM   8411  O  OE1 . GLU B  1 504 ? 6.975   16.347  47.413  1.00 41.00 ? 521  GLU B OE1 1 
ATOM   8412  O  OE2 . GLU B  1 504 ? 5.572   17.966  46.953  1.00 38.80 ? 521  GLU B OE2 1 
ATOM   8413  N  N   . VAL B  1 505 ? 10.565  18.307  43.982  1.00 24.35 ? 522  VAL B N   1 
ATOM   8414  C  CA  . VAL B  1 505 ? 11.146  19.642  43.931  1.00 23.38 ? 522  VAL B CA  1 
ATOM   8415  C  C   . VAL B  1 505 ? 11.398  20.037  42.471  1.00 22.49 ? 522  VAL B C   1 
ATOM   8416  O  O   . VAL B  1 505 ? 11.077  21.152  42.059  1.00 20.74 ? 522  VAL B O   1 
ATOM   8417  C  CB  . VAL B  1 505 ? 12.431  19.724  44.787  1.00 23.29 ? 522  VAL B CB  1 
ATOM   8418  C  CG1 . VAL B  1 505 ? 13.231  20.995  44.530  1.00 23.03 ? 522  VAL B CG1 1 
ATOM   8419  C  CG2 . VAL B  1 505 ? 12.138  19.599  46.279  1.00 24.11 ? 522  VAL B CG2 1 
ATOM   8420  N  N   . SER B  1 506 ? 11.962  19.112  41.687  1.00 22.40 ? 523  SER B N   1 
ATOM   8421  C  CA  . SER B  1 506 ? 12.325  19.395  40.303  1.00 21.82 ? 523  SER B CA  1 
ATOM   8422  C  C   . SER B  1 506 ? 11.083  19.655  39.450  1.00 21.29 ? 523  SER B C   1 
ATOM   8423  O  O   . SER B  1 506 ? 11.082  20.560  38.619  1.00 19.86 ? 523  SER B O   1 
ATOM   8424  C  CB  . SER B  1 506 ? 13.152  18.286  39.718  1.00 21.23 ? 523  SER B CB  1 
ATOM   8425  O  OG  . SER B  1 506 ? 14.387  18.145  40.406  1.00 21.32 ? 523  SER B OG  1 
ATOM   8426  N  N   . ILE B  1 507 ? 10.027  18.859  39.654  1.00 22.21 ? 524  ILE B N   1 
ATOM   8427  C  CA  . ILE B  1 507 ? 8.805   19.016  38.880  1.00 23.09 ? 524  ILE B CA  1 
ATOM   8428  C  C   . ILE B  1 507 ? 8.143   20.351  39.212  1.00 22.54 ? 524  ILE B C   1 
ATOM   8429  O  O   . ILE B  1 507 ? 7.678   21.044  38.307  1.00 21.85 ? 524  ILE B O   1 
ATOM   8430  C  CB  . ILE B  1 507 ? 7.841   17.832  39.084  1.00 24.72 ? 524  ILE B CB  1 
ATOM   8431  C  CG1 . ILE B  1 507 ? 8.468   16.505  38.647  1.00 26.69 ? 524  ILE B CG1 1 
ATOM   8432  C  CG2 . ILE B  1 507 ? 6.511   18.085  38.376  1.00 25.04 ? 524  ILE B CG2 1 
ATOM   8433  C  CD1 . ILE B  1 507 ? 9.147   16.543  37.294  1.00 27.65 ? 524  ILE B CD1 1 
ATOM   8434  N  N   . ASN B  1 508 ? 8.090   20.705  40.502  1.00 22.20 ? 525  ASN B N   1 
ATOM   8435  C  CA  . ASN B  1 508 ? 7.528   21.983  40.917  1.00 22.71 ? 525  ASN B CA  1 
ATOM   8436  C  C   . ASN B  1 508 ? 8.300   23.142  40.286  1.00 21.97 ? 525  ASN B C   1 
ATOM   8437  O  O   . ASN B  1 508 ? 7.703   24.144  39.886  1.00 21.43 ? 525  ASN B O   1 
ATOM   8438  C  CB  . ASN B  1 508 ? 7.464   22.099  42.437  1.00 24.85 ? 525  ASN B CB  1 
ATOM   8439  C  CG  . ASN B  1 508 ? 6.368   21.239  43.028  1.00 25.98 ? 525  ASN B CG  1 
ATOM   8440  O  OD1 . ASN B  1 508 ? 5.499   20.746  42.299  1.00 27.86 ? 525  ASN B OD1 1 
ATOM   8441  N  ND2 . ASN B  1 508 ? 6.390   21.041  44.337  1.00 26.56 ? 525  ASN B ND2 1 
ATOM   8442  N  N   . ILE B  1 509 ? 9.628   23.007  40.201  1.00 21.11 ? 526  ILE B N   1 
ATOM   8443  C  CA  . ILE B  1 509 ? 10.447  24.025  39.561  1.00 21.08 ? 526  ILE B CA  1 
ATOM   8444  C  C   . ILE B  1 509 ? 10.096  24.097  38.079  1.00 20.42 ? 526  ILE B C   1 
ATOM   8445  O  O   . ILE B  1 509 ? 9.923   25.189  37.546  1.00 20.34 ? 526  ILE B O   1 
ATOM   8446  C  CB  . ILE B  1 509 ? 11.946  23.766  39.797  1.00 21.36 ? 526  ILE B CB  1 
ATOM   8447  C  CG1 . ILE B  1 509 ? 12.322  24.105  41.240  1.00 22.72 ? 526  ILE B CG1 1 
ATOM   8448  C  CG2 . ILE B  1 509 ? 12.802  24.541  38.791  1.00 21.67 ? 526  ILE B CG2 1 
ATOM   8449  C  CD1 . ILE B  1 509 ? 13.732  23.705  41.625  1.00 23.83 ? 526  ILE B CD1 1 
ATOM   8450  N  N   . ALA B  1 510 ? 9.979   22.930  37.430  1.00 20.35 ? 527  ALA B N   1 
ATOM   8451  C  CA  . ALA B  1 510 ? 9.662   22.872  36.012  1.00 20.52 ? 527  ALA B CA  1 
ATOM   8452  C  C   . ALA B  1 510 ? 8.329   23.567  35.730  1.00 19.96 ? 527  ALA B C   1 
ATOM   8453  O  O   . ALA B  1 510 ? 8.196   24.271  34.728  1.00 19.15 ? 527  ALA B O   1 
ATOM   8454  C  CB  . ALA B  1 510 ? 9.658   21.439  35.546  1.00 20.73 ? 527  ALA B CB  1 
ATOM   8455  N  N   . ILE B  1 511 ? 7.356   23.396  36.634  1.00 20.34 ? 528  ILE B N   1 
ATOM   8456  C  CA  . ILE B  1 511 ? 6.037   23.985  36.455  1.00 20.99 ? 528  ILE B CA  1 
ATOM   8457  C  C   . ILE B  1 511 ? 6.130   25.509  36.496  1.00 21.40 ? 528  ILE B C   1 
ATOM   8458  O  O   . ILE B  1 511 ? 5.590   26.186  35.624  1.00 21.87 ? 528  ILE B O   1 
ATOM   8459  C  CB  . ILE B  1 511 ? 5.041   23.428  37.489  1.00 21.89 ? 528  ILE B CB  1 
ATOM   8460  C  CG1 . ILE B  1 511 ? 4.796   21.941  37.261  1.00 22.29 ? 528  ILE B CG1 1 
ATOM   8461  C  CG2 . ILE B  1 511 ? 3.732   24.221  37.471  1.00 22.68 ? 528  ILE B CG2 1 
ATOM   8462  C  CD1 . ILE B  1 511 ? 4.135   21.215  38.421  1.00 22.06 ? 528  ILE B CD1 1 
ATOM   8463  N  N   . LYS B  1 512 ? 6.815   26.050  37.510  1.00 23.41 ? 529  LYS B N   1 
ATOM   8464  C  CA  . LYS B  1 512 ? 6.950   27.491  37.662  1.00 23.81 ? 529  LYS B CA  1 
ATOM   8465  C  C   . LYS B  1 512 ? 7.725   28.084  36.490  1.00 22.16 ? 529  LYS B C   1 
ATOM   8466  O  O   . LYS B  1 512 ? 7.393   29.171  36.021  1.00 21.74 ? 529  LYS B O   1 
ATOM   8467  C  CB  . LYS B  1 512 ? 7.620   27.875  38.986  1.00 26.38 ? 529  LYS B CB  1 
ATOM   8468  C  CG  . LYS B  1 512 ? 6.809   27.502  40.215  1.00 30.83 ? 529  LYS B CG  1 
ATOM   8469  C  CD  . LYS B  1 512 ? 5.569   28.361  40.433  1.00 34.34 ? 529  LYS B CD  1 
ATOM   8470  C  CE  . LYS B  1 512 ? 5.858   29.597  41.222  1.00 38.43 ? 529  LYS B CE  1 
ATOM   8471  N  NZ  . LYS B  1 512 ? 6.154   29.291  42.628  1.00 40.26 ? 529  LYS B NZ  1 
ATOM   8472  N  N   . VAL B  1 513 ? 8.756   27.372  36.018  1.00 20.84 ? 530  VAL B N   1 
ATOM   8473  C  CA  . VAL B  1 513 ? 9.550   27.858  34.901  1.00 20.03 ? 530  VAL B CA  1 
ATOM   8474  C  C   . VAL B  1 513 ? 8.713   27.822  33.620  1.00 19.58 ? 530  VAL B C   1 
ATOM   8475  O  O   . VAL B  1 513 ? 8.778   28.754  32.826  1.00 18.79 ? 530  VAL B O   1 
ATOM   8476  C  CB  . VAL B  1 513 ? 10.876  27.089  34.752  1.00 20.20 ? 530  VAL B CB  1 
ATOM   8477  C  CG1 . VAL B  1 513 ? 11.618  27.476  33.480  1.00 20.17 ? 530  VAL B CG1 1 
ATOM   8478  C  CG2 . VAL B  1 513 ? 11.774  27.302  35.966  1.00 21.21 ? 530  VAL B CG2 1 
ATOM   8479  N  N   . THR B  1 514 ? 7.917   26.758  33.433  1.00 20.74 ? 531  THR B N   1 
ATOM   8480  C  CA  . THR B  1 514 ? 7.024   26.641  32.288  1.00 20.99 ? 531  THR B CA  1 
ATOM   8481  C  C   . THR B  1 514 ? 6.066   27.836  32.259  1.00 21.83 ? 531  THR B C   1 
ATOM   8482  O  O   . THR B  1 514 ? 5.856   28.432  31.205  1.00 21.37 ? 531  THR B O   1 
ATOM   8483  C  CB  . THR B  1 514 ? 6.276   25.305  32.343  1.00 21.34 ? 531  THR B CB  1 
ATOM   8484  O  OG1 . THR B  1 514 ? 7.235   24.260  32.183  1.00 21.26 ? 531  THR B OG1 1 
ATOM   8485  C  CG2 . THR B  1 514 ? 5.221   25.172  31.259  1.00 21.44 ? 531  THR B CG2 1 
ATOM   8486  N  N   . GLU B  1 515 ? 5.500   28.191  33.421  1.00 22.60 ? 532  GLU B N   1 
ATOM   8487  C  CA  . GLU B  1 515 ? 4.558   29.300  33.511  1.00 24.61 ? 532  GLU B CA  1 
ATOM   8488  C  C   . GLU B  1 515 ? 5.246   30.592  33.088  1.00 24.59 ? 532  GLU B C   1 
ATOM   8489  O  O   . GLU B  1 515 ? 4.666   31.400  32.367  1.00 24.91 ? 532  GLU B O   1 
ATOM   8490  C  CB  . GLU B  1 515 ? 3.997   29.447  34.924  1.00 26.90 ? 532  GLU B CB  1 
ATOM   8491  C  CG  . GLU B  1 515 ? 2.984   28.364  35.280  1.00 30.08 ? 532  GLU B CG  1 
ATOM   8492  C  CD  . GLU B  1 515 ? 2.584   28.307  36.744  1.00 33.81 ? 532  GLU B CD  1 
ATOM   8493  O  OE1 . GLU B  1 515 ? 3.296   28.861  37.606  1.00 37.09 ? 532  GLU B OE1 1 
ATOM   8494  O  OE2 . GLU B  1 515 ? 1.529   27.700  37.018  1.00 40.19 ? 532  GLU B OE2 1 
ATOM   8495  N  N   . TYR B  1 516 ? 6.499   30.754  33.527  1.00 24.42 ? 533  TYR B N   1 
ATOM   8496  C  CA  . TYR B  1 516 ? 7.294   31.925  33.204  1.00 24.15 ? 533  TYR B CA  1 
ATOM   8497  C  C   . TYR B  1 516 ? 7.591   32.003  31.706  1.00 22.74 ? 533  TYR B C   1 
ATOM   8498  O  O   . TYR B  1 516 ? 7.551   33.085  31.122  1.00 23.28 ? 533  TYR B O   1 
ATOM   8499  C  CB  . TYR B  1 516 ? 8.584   31.900  34.033  1.00 25.71 ? 533  TYR B CB  1 
ATOM   8500  C  CG  . TYR B  1 516 ? 9.519   33.042  33.679  1.00 27.25 ? 533  TYR B CG  1 
ATOM   8501  C  CD1 . TYR B  1 516 ? 9.364   34.293  34.267  1.00 29.26 ? 533  TYR B CD1 1 
ATOM   8502  C  CD2 . TYR B  1 516 ? 10.531  32.879  32.742  1.00 27.99 ? 533  TYR B CD2 1 
ATOM   8503  C  CE1 . TYR B  1 516 ? 10.201  35.346  33.939  1.00 30.51 ? 533  TYR B CE1 1 
ATOM   8504  C  CE2 . TYR B  1 516 ? 11.371  33.927  32.400  1.00 29.14 ? 533  TYR B CE2 1 
ATOM   8505  C  CZ  . TYR B  1 516 ? 11.203  35.162  33.000  1.00 30.78 ? 533  TYR B CZ  1 
ATOM   8506  O  OH  . TYR B  1 516 ? 12.022  36.205  32.675  1.00 34.50 ? 533  TYR B OH  1 
ATOM   8507  N  N   . LEU B  1 517 ? 7.938   30.871  31.085  1.00 21.72 ? 534  LEU B N   1 
ATOM   8508  C  CA  . LEU B  1 517 ? 8.353   30.881  29.686  1.00 20.66 ? 534  LEU B CA  1 
ATOM   8509  C  C   . LEU B  1 517 ? 7.175   31.291  28.801  1.00 20.46 ? 534  LEU B C   1 
ATOM   8510  O  O   . LEU B  1 517 ? 7.327   32.085  27.873  1.00 20.18 ? 534  LEU B O   1 
ATOM   8511  C  CB  . LEU B  1 517 ? 8.931   29.523  29.285  1.00 19.51 ? 534  LEU B CB  1 
ATOM   8512  C  CG  . LEU B  1 517 ? 10.257  29.130  29.946  1.00 19.28 ? 534  LEU B CG  1 
ATOM   8513  C  CD1 . LEU B  1 517 ? 10.556  27.652  29.722  1.00 18.87 ? 534  LEU B CD1 1 
ATOM   8514  C  CD2 . LEU B  1 517 ? 11.411  29.984  29.434  1.00 19.15 ? 534  LEU B CD2 1 
ATOM   8515  N  N   . TYR B  1 518 ? 5.989   30.758  29.099  1.00 21.68 ? 535  TYR B N   1 
ATOM   8516  C  CA  . TYR B  1 518 ? 4.803   31.079  28.319  1.00 22.23 ? 535  TYR B CA  1 
ATOM   8517  C  C   . TYR B  1 518 ? 4.413   32.537  28.537  1.00 23.40 ? 535  TYR B C   1 
ATOM   8518  O  O   . TYR B  1 518 ? 4.040   33.214  27.580  1.00 25.01 ? 535  TYR B O   1 
ATOM   8519  C  CB  . TYR B  1 518 ? 3.616   30.170  28.646  1.00 21.51 ? 535  TYR B CB  1 
ATOM   8520  C  CG  . TYR B  1 518 ? 3.599   28.862  27.872  1.00 21.14 ? 535  TYR B CG  1 
ATOM   8521  C  CD1 . TYR B  1 518 ? 3.263   28.837  26.524  1.00 21.28 ? 535  TYR B CD1 1 
ATOM   8522  C  CD2 . TYR B  1 518 ? 3.898   27.655  28.492  1.00 21.40 ? 535  TYR B CD2 1 
ATOM   8523  C  CE1 . TYR B  1 518 ? 3.247   27.651  25.808  1.00 20.88 ? 535  TYR B CE1 1 
ATOM   8524  C  CE2 . TYR B  1 518 ? 3.875   26.462  27.789  1.00 21.34 ? 535  TYR B CE2 1 
ATOM   8525  C  CZ  . TYR B  1 518 ? 3.550   26.462  26.444  1.00 20.75 ? 535  TYR B CZ  1 
ATOM   8526  O  OH  . TYR B  1 518 ? 3.517   25.286  25.758  1.00 21.48 ? 535  TYR B OH  1 
ATOM   8527  N  N   . ALA B  1 519 ? 4.502   33.006  29.789  1.00 23.98 ? 536  ALA B N   1 
ATOM   8528  C  CA  . ALA B  1 519 ? 4.090   34.359  30.134  1.00 26.50 ? 536  ALA B CA  1 
ATOM   8529  C  C   . ALA B  1 519 ? 4.983   35.401  29.463  1.00 27.21 ? 536  ALA B C   1 
ATOM   8530  O  O   . ALA B  1 519 ? 4.528   36.511  29.205  1.00 27.41 ? 536  ALA B O   1 
ATOM   8531  C  CB  . ALA B  1 519 ? 4.068   34.545  31.637  1.00 27.09 ? 536  ALA B CB  1 
ATOM   8532  N  N   . ASN B  1 520 ? 6.244   35.043  29.176  1.00 26.67 ? 537  ASN B N   1 
ATOM   8533  C  CA  . ASN B  1 520 ? 7.217   35.993  28.661  1.00 27.39 ? 537  ASN B CA  1 
ATOM   8534  C  C   . ASN B  1 520 ? 7.539   35.721  27.192  1.00 28.18 ? 537  ASN B C   1 
ATOM   8535  O  O   . ASN B  1 520 ? 8.544   36.212  26.686  1.00 29.50 ? 537  ASN B O   1 
ATOM   8536  C  CB  . ASN B  1 520 ? 8.460   35.995  29.543  1.00 29.23 ? 537  ASN B CB  1 
ATOM   8537  C  CG  . ASN B  1 520 ? 8.221   36.757  30.822  1.00 29.96 ? 537  ASN B CG  1 
ATOM   8538  O  OD1 . ASN B  1 520 ? 8.364   37.983  30.833  1.00 31.76 ? 537  ASN B OD1 1 
ATOM   8539  N  ND2 . ASN B  1 520 ? 7.849   36.067  31.890  1.00 29.79 ? 537  ASN B ND2 1 
ATOM   8540  N  N   . LYS B  1 521 ? 6.678   34.947  26.517  1.00 28.79 ? 538  LYS B N   1 
ATOM   8541  C  CA  . LYS B  1 521 ? 6.765   34.705  25.083  1.00 30.86 ? 538  LYS B CA  1 
ATOM   8542  C  C   . LYS B  1 521 ? 8.096   34.054  24.711  1.00 28.46 ? 538  LYS B C   1 
ATOM   8543  O  O   . LYS B  1 521 ? 8.668   34.368  23.667  1.00 28.06 ? 538  LYS B O   1 
ATOM   8544  C  CB  . LYS B  1 521 ? 6.539   36.003  24.296  1.00 36.64 ? 538  LYS B CB  1 
ATOM   8545  C  CG  . LYS B  1 521 ? 5.284   36.777  24.694  1.00 40.73 ? 538  LYS B CG  1 
ATOM   8546  C  CD  . LYS B  1 521 ? 4.036   35.926  24.917  1.00 45.05 ? 538  LYS B CD  1 
ATOM   8547  C  CE  . LYS B  1 521 ? 3.631   35.068  23.749  1.00 49.05 ? 538  LYS B CE  1 
ATOM   8548  N  NZ  . LYS B  1 521 ? 3.173   35.855  22.600  1.00 52.81 ? 538  LYS B NZ  1 
ATOM   8549  N  N   . MET B  1 522 ? 8.580   33.144  25.565  1.00 25.79 ? 539  MET B N   1 
ATOM   8550  C  CA  . MET B  1 522 ? 9.799   32.400  25.286  1.00 25.41 ? 539  MET B CA  1 
ATOM   8551  C  C   . MET B  1 522 ? 9.487   30.944  24.935  1.00 24.24 ? 539  MET B C   1 
ATOM   8552  O  O   . MET B  1 522 ? 10.411  30.187  24.642  1.00 23.66 ? 539  MET B O   1 
ATOM   8553  C  CB  . MET B  1 522 ? 10.741  32.432  26.494  1.00 26.06 ? 539  MET B CB  1 
ATOM   8554  C  CG  . MET B  1 522 ? 11.246  33.821  26.847  1.00 27.72 ? 539  MET B CG  1 
ATOM   8555  S  SD  . MET B  1 522 ? 11.853  33.884  28.543  1.00 29.86 ? 539  MET B SD  1 
ATOM   8556  C  CE  . MET B  1 522 ? 12.381  35.600  28.672  1.00 31.18 ? 539  MET B CE  1 
ATOM   8557  N  N   . ALA B  1 523 ? 8.200   30.555  24.966  1.00 23.48 ? 540  ALA B N   1 
ATOM   8558  C  CA  . ALA B  1 523 ? 7.784   29.210  24.584  1.00 23.59 ? 540  ALA B CA  1 
ATOM   8559  C  C   . ALA B  1 523 ? 7.307   29.211  23.135  1.00 23.03 ? 540  ALA B C   1 
ATOM   8560  O  O   . ALA B  1 523 ? 6.801   30.224  22.655  1.00 22.41 ? 540  ALA B O   1 
ATOM   8561  C  CB  . ALA B  1 523 ? 6.695   28.718  25.512  1.00 24.52 ? 540  ALA B CB  1 
ATOM   8562  N  N   . PHE B  1 524 ? 7.472   28.068  22.455  1.00 21.90 ? 541  PHE B N   1 
ATOM   8563  C  CA  . PHE B  1 524 ? 7.019   27.910  21.081  1.00 22.58 ? 541  PHE B CA  1 
ATOM   8564  C  C   . PHE B  1 524 ? 6.142   26.667  20.908  1.00 23.34 ? 541  PHE B C   1 
ATOM   8565  O  O   . PHE B  1 524 ? 5.737   26.367  19.791  1.00 25.81 ? 541  PHE B O   1 
ATOM   8566  C  CB  . PHE B  1 524 ? 8.242   27.889  20.157  1.00 22.55 ? 541  PHE B CB  1 
ATOM   8567  C  CG  . PHE B  1 524 ? 8.931   29.242  20.067  1.00 23.33 ? 541  PHE B CG  1 
ATOM   8568  C  CD1 . PHE B  1 524 ? 9.940   29.592  20.960  1.00 23.85 ? 541  PHE B CD1 1 
ATOM   8569  C  CD2 . PHE B  1 524 ? 8.529   30.184  19.127  1.00 23.43 ? 541  PHE B CD2 1 
ATOM   8570  C  CE1 . PHE B  1 524 ? 10.546  30.839  20.893  1.00 24.29 ? 541  PHE B CE1 1 
ATOM   8571  C  CE2 . PHE B  1 524 ? 9.147   31.424  19.057  1.00 24.73 ? 541  PHE B CE2 1 
ATOM   8572  C  CZ  . PHE B  1 524 ? 10.150  31.753  19.945  1.00 24.72 ? 541  PHE B CZ  1 
ATOM   8573  N  N   . ARG B  1 525 ? 5.824   25.955  21.992  1.00 22.78 ? 542  ARG B N   1 
ATOM   8574  C  CA  . ARG B  1 525 ? 4.927   24.815  21.908  1.00 23.00 ? 542  ARG B CA  1 
ATOM   8575  C  C   . ARG B  1 525 ? 3.490   25.317  22.036  1.00 23.50 ? 542  ARG B C   1 
ATOM   8576  O  O   . ARG B  1 525 ? 3.094   25.784  23.099  1.00 22.12 ? 542  ARG B O   1 
ATOM   8577  C  CB  . ARG B  1 525 ? 5.273   23.781  22.984  1.00 22.90 ? 542  ARG B CB  1 
ATOM   8578  C  CG  . ARG B  1 525 ? 4.605   22.428  22.793  1.00 23.72 ? 542  ARG B CG  1 
ATOM   8579  C  CD  . ARG B  1 525 ? 3.134   22.413  23.175  1.00 24.57 ? 542  ARG B CD  1 
ATOM   8580  N  NE  . ARG B  1 525 ? 2.636   21.034  23.170  1.00 26.22 ? 542  ARG B NE  1 
ATOM   8581  C  CZ  . ARG B  1 525 ? 1.366   20.650  23.194  1.00 26.90 ? 542  ARG B CZ  1 
ATOM   8582  N  NH1 . ARG B  1 525 ? 0.380   21.523  23.076  1.00 27.17 ? 542  ARG B NH1 1 
ATOM   8583  N  NH2 . ARG B  1 525 ? 1.097   19.366  23.309  1.00 27.55 ? 542  ARG B NH2 1 
ATOM   8584  N  N   . TYR B  1 526 ? 2.736   25.243  20.932  1.00 24.47 ? 543  TYR B N   1 
ATOM   8585  C  CA  . TYR B  1 526 ? 1.332   25.634  20.919  1.00 26.72 ? 543  TYR B CA  1 
ATOM   8586  C  C   . TYR B  1 526 ? 0.496   24.495  20.340  1.00 27.64 ? 543  TYR B C   1 
ATOM   8587  O  O   . TYR B  1 526 ? 0.975   23.757  19.478  1.00 26.52 ? 543  TYR B O   1 
ATOM   8588  C  CB  . TYR B  1 526 ? 1.148   26.935  20.131  1.00 27.46 ? 543  TYR B CB  1 
ATOM   8589  C  CG  . TYR B  1 526 ? 1.754   28.138  20.838  1.00 28.77 ? 543  TYR B CG  1 
ATOM   8590  C  CD1 . TYR B  1 526 ? 1.080   28.780  21.870  1.00 30.22 ? 543  TYR B CD1 1 
ATOM   8591  C  CD2 . TYR B  1 526 ? 3.015   28.609  20.493  1.00 30.63 ? 543  TYR B CD2 1 
ATOM   8592  C  CE1 . TYR B  1 526 ? 1.635   29.865  22.530  1.00 32.27 ? 543  TYR B CE1 1 
ATOM   8593  C  CE2 . TYR B  1 526 ? 3.587   29.687  21.150  1.00 32.19 ? 543  TYR B CE2 1 
ATOM   8594  C  CZ  . TYR B  1 526 ? 2.894   30.318  22.167  1.00 34.10 ? 543  TYR B CZ  1 
ATOM   8595  O  OH  . TYR B  1 526 ? 3.458   31.388  22.800  1.00 41.28 ? 543  TYR B OH  1 
ATOM   8596  N  N   . PRO B  1 527 ? -0.783  24.322  20.756  1.00 29.36 ? 544  PRO B N   1 
ATOM   8597  C  CA  . PRO B  1 527 ? -1.442  25.216  21.711  1.00 28.88 ? 544  PRO B CA  1 
ATOM   8598  C  C   . PRO B  1 527 ? -0.856  25.239  23.122  1.00 27.30 ? 544  PRO B C   1 
ATOM   8599  O  O   . PRO B  1 527 ? -0.278  24.259  23.592  1.00 25.92 ? 544  PRO B O   1 
ATOM   8600  C  CB  . PRO B  1 527 ? -2.910  24.736  21.724  1.00 30.56 ? 544  PRO B CB  1 
ATOM   8601  C  CG  . PRO B  1 527 ? -2.856  23.316  21.223  1.00 31.56 ? 544  PRO B CG  1 
ATOM   8602  C  CD  . PRO B  1 527 ? -1.680  23.265  20.262  1.00 30.62 ? 544  PRO B CD  1 
ATOM   8603  N  N   . GLU B  1 528 ? -1.013  26.395  23.771  1.00 25.78 ? 545  GLU B N   1 
ATOM   8604  C  CA  . GLU B  1 528 ? -0.534  26.610  25.124  1.00 27.88 ? 545  GLU B CA  1 
ATOM   8605  C  C   . GLU B  1 528 ? -1.450  25.886  26.106  1.00 28.04 ? 545  GLU B C   1 
ATOM   8606  O  O   . GLU B  1 528 ? -2.665  26.071  26.062  1.00 26.76 ? 545  GLU B O   1 
ATOM   8607  C  CB  . GLU B  1 528 ? -0.506  28.109  25.417  1.00 27.74 ? 545  GLU B CB  1 
ATOM   8608  C  CG  . GLU B  1 528 ? -0.241  28.435  26.885  1.00 28.28 ? 545  GLU B CG  1 
ATOM   8609  C  CD  . GLU B  1 528 ? -0.031  29.910  27.160  1.00 29.33 ? 545  GLU B CD  1 
ATOM   8610  O  OE1 . GLU B  1 528 ? 0.069   30.675  26.179  1.00 30.53 ? 545  GLU B OE1 1 
ATOM   8611  O  OE2 . GLU B  1 528 ? 0.042   30.293  28.348  1.00 30.28 ? 545  GLU B OE2 1 
ATOM   8612  N  N   . PRO B  1 529 ? -0.912  25.057  27.030  1.00 28.81 ? 546  PRO B N   1 
ATOM   8613  C  CA  . PRO B  1 529 ? -1.747  24.387  28.025  1.00 30.40 ? 546  PRO B CA  1 
ATOM   8614  C  C   . PRO B  1 529 ? -2.351  25.399  28.992  1.00 32.09 ? 546  PRO B C   1 
ATOM   8615  O  O   . PRO B  1 529 ? -1.695  26.364  29.377  1.00 31.89 ? 546  PRO B O   1 
ATOM   8616  C  CB  . PRO B  1 529 ? -0.773  23.425  28.718  1.00 30.13 ? 546  PRO B CB  1 
ATOM   8617  C  CG  . PRO B  1 529 ? 0.566   24.102  28.554  1.00 29.35 ? 546  PRO B CG  1 
ATOM   8618  C  CD  . PRO B  1 529 ? 0.514   24.721  27.174  1.00 29.20 ? 546  PRO B CD  1 
ATOM   8619  N  N   . GLU B  1 530 ? -3.606  25.161  29.381  1.00 33.69 ? 547  GLU B N   1 
ATOM   8620  C  CA  . GLU B  1 530 ? -4.284  26.029  30.327  1.00 36.47 ? 547  GLU B CA  1 
ATOM   8621  C  C   . GLU B  1 530 ? -3.758  25.741  31.732  1.00 32.19 ? 547  GLU B C   1 
ATOM   8622  O  O   . GLU B  1 530 ? -3.605  26.655  32.528  1.00 31.66 ? 547  GLU B O   1 
ATOM   8623  C  CB  . GLU B  1 530 ? -5.798  25.849  30.194  1.00 42.07 ? 547  GLU B CB  1 
ATOM   8624  C  CG  . GLU B  1 530 ? -6.592  27.075  30.638  1.00 48.35 ? 547  GLU B CG  1 
ATOM   8625  C  CD  . GLU B  1 530 ? -8.003  27.164  30.075  1.00 54.85 ? 547  GLU B CD  1 
ATOM   8626  O  OE1 . GLU B  1 530 ? -8.636  28.227  30.259  1.00 59.28 ? 547  GLU B OE1 1 
ATOM   8627  O  OE2 . GLU B  1 530 ? -8.475  26.186  29.457  1.00 58.77 ? 547  GLU B OE2 1 
ATOM   8628  N  N   . ASP B  1 531 ? -3.475  24.463  32.011  1.00 30.96 ? 548  ASP B N   1 
ATOM   8629  C  CA  . ASP B  1 531 ? -3.000  24.010  33.308  1.00 30.22 ? 548  ASP B CA  1 
ATOM   8630  C  C   . ASP B  1 531 ? -1.568  23.495  33.156  1.00 28.06 ? 548  ASP B C   1 
ATOM   8631  O  O   . ASP B  1 531 ? -1.354  22.374  32.703  1.00 27.44 ? 548  ASP B O   1 
ATOM   8632  C  CB  . ASP B  1 531 ? -3.956  22.969  33.870  1.00 31.42 ? 548  ASP B CB  1 
ATOM   8633  C  CG  . ASP B  1 531 ? -3.602  22.361  35.218  1.00 34.53 ? 548  ASP B CG  1 
ATOM   8634  O  OD1 . ASP B  1 531 ? -2.444  22.510  35.658  1.00 37.32 ? 548  ASP B OD1 1 
ATOM   8635  O  OD2 . ASP B  1 531 ? -4.497  21.740  35.823  1.00 36.93 ? 548  ASP B OD2 1 
ATOM   8636  N  N   . LYS B  1 532 ? -0.594  24.315  33.559  1.00 27.09 ? 549  LYS B N   1 
ATOM   8637  C  CA  . LYS B  1 532 ? 0.810   24.004  33.339  1.00 27.70 ? 549  LYS B CA  1 
ATOM   8638  C  C   . LYS B  1 532 ? 1.260   22.833  34.211  1.00 27.67 ? 549  LYS B C   1 
ATOM   8639  O  O   . LYS B  1 532 ? 2.151   22.085  33.816  1.00 27.84 ? 549  LYS B O   1 
ATOM   8640  C  CB  . LYS B  1 532 ? 1.691   25.234  33.582  1.00 27.96 ? 549  LYS B CB  1 
ATOM   8641  C  CG  . LYS B  1 532 ? 1.840   26.160  32.388  1.00 28.72 ? 549  LYS B CG  1 
ATOM   8642  C  CD  . LYS B  1 532 ? 0.566   26.873  31.963  1.00 28.99 ? 549  LYS B CD  1 
ATOM   8643  C  CE  . LYS B  1 532 ? 0.835   27.952  30.966  1.00 28.83 ? 549  LYS B CE  1 
ATOM   8644  N  NZ  . LYS B  1 532 ? -0.404  28.636  30.583  1.00 29.92 ? 549  LYS B NZ  1 
ATOM   8645  N  N   . ALA B  1 533 ? 0.658   22.683  35.398  1.00 27.75 ? 550  ALA B N   1 
ATOM   8646  C  CA  . ALA B  1 533 ? 1.031   21.613  36.307  1.00 28.02 ? 550  ALA B CA  1 
ATOM   8647  C  C   . ALA B  1 533 ? 0.698   20.264  35.678  1.00 27.84 ? 550  ALA B C   1 
ATOM   8648  O  O   . ALA B  1 533 ? 1.521   19.352  35.683  1.00 26.61 ? 550  ALA B O   1 
ATOM   8649  C  CB  . ALA B  1 533 ? 0.344   21.794  37.646  1.00 28.26 ? 550  ALA B CB  1 
ATOM   8650  N  N   . LYS B  1 534 ? -0.523  20.160  35.141  1.00 28.61 ? 551  LYS B N   1 
ATOM   8651  C  CA  . LYS B  1 534 ? -0.997  18.961  34.467  1.00 28.55 ? 551  LYS B CA  1 
ATOM   8652  C  C   . LYS B  1 534 ? -0.127  18.670  33.247  1.00 25.13 ? 551  LYS B C   1 
ATOM   8653  O  O   . LYS B  1 534 ? 0.241   17.523  33.010  1.00 24.91 ? 551  LYS B O   1 
ATOM   8654  C  CB  . LYS B  1 534 ? -2.468  19.160  34.080  1.00 32.11 ? 551  LYS B CB  1 
ATOM   8655  C  CG  . LYS B  1 534 ? -3.155  18.002  33.364  1.00 37.16 ? 551  LYS B CG  1 
ATOM   8656  C  CD  . LYS B  1 534 ? -4.587  18.332  32.951  1.00 41.47 ? 551  LYS B CD  1 
ATOM   8657  C  CE  . LYS B  1 534 ? -5.317  17.200  32.291  1.00 44.57 ? 551  LYS B CE  1 
ATOM   8658  N  NZ  . LYS B  1 534 ? -4.783  16.880  30.964  1.00 47.00 ? 551  LYS B NZ  1 
ATOM   8659  N  N   . TYR B  1 535 ? 0.191   19.721  32.484  1.00 23.58 ? 552  TYR B N   1 
ATOM   8660  C  CA  . TYR B  1 535 ? 0.962   19.597  31.257  1.00 23.60 ? 552  TYR B CA  1 
ATOM   8661  C  C   . TYR B  1 535 ? 2.307   18.929  31.547  1.00 23.21 ? 552  TYR B C   1 
ATOM   8662  O  O   . TYR B  1 535 ? 2.690   17.990  30.855  1.00 22.34 ? 552  TYR B O   1 
ATOM   8663  C  CB  . TYR B  1 535 ? 1.131   20.987  30.640  1.00 23.60 ? 552  TYR B CB  1 
ATOM   8664  C  CG  . TYR B  1 535 ? 2.021   21.039  29.406  1.00 23.71 ? 552  TYR B CG  1 
ATOM   8665  C  CD1 . TYR B  1 535 ? 1.536   20.650  28.164  1.00 23.18 ? 552  TYR B CD1 1 
ATOM   8666  C  CD2 . TYR B  1 535 ? 3.335   21.495  29.477  1.00 22.56 ? 552  TYR B CD2 1 
ATOM   8667  C  CE1 . TYR B  1 535 ? 2.332   20.692  27.032  1.00 23.09 ? 552  TYR B CE1 1 
ATOM   8668  C  CE2 . TYR B  1 535 ? 4.137   21.549  28.347  1.00 22.95 ? 552  TYR B CE2 1 
ATOM   8669  C  CZ  . TYR B  1 535 ? 3.638   21.137  27.123  1.00 22.81 ? 552  TYR B CZ  1 
ATOM   8670  O  OH  . TYR B  1 535 ? 4.392   21.173  25.985  1.00 22.93 ? 552  TYR B OH  1 
ATOM   8671  N  N   . VAL B  1 536 ? 3.004   19.415  32.580  1.00 23.66 ? 553  VAL B N   1 
ATOM   8672  C  CA  . VAL B  1 536 ? 4.324   18.909  32.924  1.00 24.30 ? 553  VAL B CA  1 
ATOM   8673  C  C   . VAL B  1 536 ? 4.213   17.488  33.478  1.00 24.77 ? 553  VAL B C   1 
ATOM   8674  O  O   . VAL B  1 536 ? 4.948   16.594  33.055  1.00 23.08 ? 553  VAL B O   1 
ATOM   8675  C  CB  . VAL B  1 536 ? 5.032   19.853  33.918  1.00 24.08 ? 553  VAL B CB  1 
ATOM   8676  C  CG1 . VAL B  1 536 ? 6.286   19.219  34.509  1.00 23.60 ? 553  VAL B CG1 1 
ATOM   8677  C  CG2 . VAL B  1 536 ? 5.358   21.195  33.276  1.00 23.40 ? 553  VAL B CG2 1 
ATOM   8678  N  N   . LYS B  1 537 ? 3.282   17.276  34.413  1.00 25.05 ? 554  LYS B N   1 
ATOM   8679  C  CA  . LYS B  1 537 ? 3.201   16.009  35.126  1.00 27.06 ? 554  LYS B CA  1 
ATOM   8680  C  C   . LYS B  1 537 ? 2.838   14.860  34.184  1.00 27.11 ? 554  LYS B C   1 
ATOM   8681  O  O   . LYS B  1 537 ? 3.283   13.735  34.395  1.00 27.29 ? 554  LYS B O   1 
ATOM   8682  C  CB  . LYS B  1 537 ? 2.245   16.102  36.317  1.00 27.88 ? 554  LYS B CB  1 
ATOM   8683  C  CG  . LYS B  1 537 ? 2.790   16.901  37.484  1.00 29.39 ? 554  LYS B CG  1 
ATOM   8684  C  CD  . LYS B  1 537 ? 1.865   16.962  38.693  1.00 31.42 ? 554  LYS B CD  1 
ATOM   8685  C  CE  . LYS B  1 537 ? 2.499   17.747  39.792  1.00 34.39 ? 554  LYS B CE  1 
ATOM   8686  N  NZ  . LYS B  1 537 ? 1.707   17.733  41.024  1.00 36.66 ? 554  LYS B NZ  1 
ATOM   8687  N  N   . GLU B  1 538 ? 2.065   15.144  33.130  1.00 27.47 ? 555  GLU B N   1 
ATOM   8688  C  CA  . GLU B  1 538 ? 1.659   14.110  32.188  1.00 29.03 ? 555  GLU B CA  1 
ATOM   8689  C  C   . GLU B  1 538 ? 2.784   13.747  31.219  1.00 26.01 ? 555  GLU B C   1 
ATOM   8690  O  O   . GLU B  1 538 ? 2.675   12.744  30.521  1.00 25.43 ? 555  GLU B O   1 
ATOM   8691  C  CB  . GLU B  1 538 ? 0.406   14.516  31.407  1.00 31.18 ? 555  GLU B CB  1 
ATOM   8692  C  CG  . GLU B  1 538 ? -0.862  14.414  32.249  1.00 34.73 ? 555  GLU B CG  1 
ATOM   8693  C  CD  . GLU B  1 538 ? -2.126  14.933  31.590  1.00 38.76 ? 555  GLU B CD  1 
ATOM   8694  O  OE1 . GLU B  1 538 ? -2.066  15.439  30.444  1.00 39.22 ? 555  GLU B OE1 1 
ATOM   8695  O  OE2 . GLU B  1 538 ? -3.184  14.832  32.251  1.00 44.02 ? 555  GLU B OE2 1 
ATOM   8696  N  N   . ARG B  1 539 ? 3.866   14.536  31.170  1.00 25.63 ? 556  ARG B N   1 
ATOM   8697  C  CA  . ARG B  1 539 ? 4.902   14.318  30.169  1.00 23.66 ? 556  ARG B CA  1 
ATOM   8698  C  C   . ARG B  1 539 ? 6.186   13.735  30.763  1.00 23.34 ? 556  ARG B C   1 
ATOM   8699  O  O   . ARG B  1 539 ? 7.076   13.362  30.003  1.00 22.84 ? 556  ARG B O   1 
ATOM   8700  C  CB  . ARG B  1 539 ? 5.144   15.617  29.396  1.00 24.11 ? 556  ARG B CB  1 
ATOM   8701  C  CG  . ARG B  1 539 ? 4.031   15.852  28.384  1.00 25.06 ? 556  ARG B CG  1 
ATOM   8702  C  CD  . ARG B  1 539 ? 4.032   17.246  27.772  1.00 25.72 ? 556  ARG B CD  1 
ATOM   8703  N  NE  . ARG B  1 539 ? 2.916   17.391  26.830  1.00 26.92 ? 556  ARG B NE  1 
ATOM   8704  C  CZ  . ARG B  1 539 ? 1.622   17.397  27.157  1.00 26.44 ? 556  ARG B CZ  1 
ATOM   8705  N  NH1 . ARG B  1 539 ? 1.245   17.380  28.423  1.00 25.20 ? 556  ARG B NH1 1 
ATOM   8706  N  NH2 . ARG B  1 539 ? 0.700   17.446  26.210  1.00 27.25 ? 556  ARG B NH2 1 
ATOM   8707  N  N   . THR B  1 540 ? 6.287   13.645  32.096  1.00 22.54 ? 557  THR B N   1 
ATOM   8708  C  CA  . THR B  1 540 ? 7.485   13.097  32.719  1.00 23.07 ? 557  THR B CA  1 
ATOM   8709  C  C   . THR B  1 540 ? 7.557   11.597  32.429  1.00 23.37 ? 557  THR B C   1 
ATOM   8710  O  O   . THR B  1 540 ? 6.544   10.900  32.463  1.00 22.65 ? 557  THR B O   1 
ATOM   8711  C  CB  . THR B  1 540 ? 7.521   13.383  34.221  1.00 23.72 ? 557  THR B CB  1 
ATOM   8712  O  OG1 . THR B  1 540 ? 6.357   12.825  34.821  1.00 23.02 ? 557  THR B OG1 1 
ATOM   8713  C  CG2 . THR B  1 540 ? 7.584   14.866  34.532  1.00 24.15 ? 557  THR B CG2 1 
ATOM   8714  N  N   . TRP B  1 541 ? 8.771   11.125  32.124  1.00 22.32 ? 558  TRP B N   1 
ATOM   8715  C  CA  . TRP B  1 541 ? 9.028   9.722   31.843  1.00 22.65 ? 558  TRP B CA  1 
ATOM   8716  C  C   . TRP B  1 541 ? 8.917   8.912   33.128  1.00 23.85 ? 558  TRP B C   1 
ATOM   8717  O  O   . TRP B  1 541 ? 9.409   9.348   34.165  1.00 22.94 ? 558  TRP B O   1 
ATOM   8718  C  CB  . TRP B  1 541 ? 10.422  9.568   31.220  1.00 22.17 ? 558  TRP B CB  1 
ATOM   8719  C  CG  . TRP B  1 541 ? 10.831  8.149   30.931  1.00 21.71 ? 558  TRP B CG  1 
ATOM   8720  C  CD1 . TRP B  1 541 ? 10.539  7.420   29.817  1.00 22.48 ? 558  TRP B CD1 1 
ATOM   8721  C  CD2 . TRP B  1 541 ? 11.644  7.298   31.766  1.00 21.84 ? 558  TRP B CD2 1 
ATOM   8722  N  NE1 . TRP B  1 541 ? 11.102  6.175   29.905  1.00 22.45 ? 558  TRP B NE1 1 
ATOM   8723  C  CE2 . TRP B  1 541 ? 11.785  6.069   31.086  1.00 22.07 ? 558  TRP B CE2 1 
ATOM   8724  C  CE3 . TRP B  1 541 ? 12.257  7.453   33.013  1.00 21.71 ? 558  TRP B CE3 1 
ATOM   8725  C  CZ2 . TRP B  1 541 ? 12.519  5.007   31.610  1.00 21.78 ? 558  TRP B CZ2 1 
ATOM   8726  C  CZ3 . TRP B  1 541 ? 12.977  6.400   33.536  1.00 21.65 ? 558  TRP B CZ3 1 
ATOM   8727  C  CH2 . TRP B  1 541 ? 13.102  5.195   32.842  1.00 21.36 ? 558  TRP B CH2 1 
ATOM   8728  N  N   . ARG B  1 542 ? 8.297   7.729   33.022  1.00 25.80 ? 559  ARG B N   1 
ATOM   8729  C  CA  . ARG B  1 542 ? 8.047   6.847   34.153  1.00 28.19 ? 559  ARG B CA  1 
ATOM   8730  C  C   . ARG B  1 542 ? 8.908   5.590   34.048  1.00 25.70 ? 559  ARG B C   1 
ATOM   8731  O  O   . ARG B  1 542 ? 9.062   5.033   32.968  1.00 25.01 ? 559  ARG B O   1 
ATOM   8732  C  CB  . ARG B  1 542 ? 6.575   6.417   34.195  1.00 31.21 ? 559  ARG B CB  1 
ATOM   8733  C  CG  . ARG B  1 542 ? 5.671   7.332   35.009  1.00 36.63 ? 559  ARG B CG  1 
ATOM   8734  C  CD  . ARG B  1 542 ? 5.319   8.623   34.309  1.00 41.53 ? 559  ARG B CD  1 
ATOM   8735  N  NE  . ARG B  1 542 ? 4.565   9.523   35.192  1.00 47.71 ? 559  ARG B NE  1 
ATOM   8736  C  CZ  . ARG B  1 542 ? 3.989   10.673  34.836  1.00 51.01 ? 559  ARG B CZ  1 
ATOM   8737  N  NH1 . ARG B  1 542 ? 4.011   11.086  33.577  1.00 48.17 ? 559  ARG B NH1 1 
ATOM   8738  N  NH2 . ARG B  1 542 ? 3.382   11.408  35.755  1.00 54.69 ? 559  ARG B NH2 1 
ATOM   8739  N  N   . SER B  1 543 ? 9.405   5.128   35.198  1.00 25.77 ? 560  SER B N   1 
ATOM   8740  C  CA  . SER B  1 543 ? 10.307  3.988   35.278  1.00 25.94 ? 560  SER B CA  1 
ATOM   8741  C  C   . SER B  1 543 ? 9.555   2.669   35.473  1.00 24.85 ? 560  SER B C   1 
ATOM   8742  O  O   . SER B  1 543 ? 10.174  1.605   35.454  1.00 24.89 ? 560  SER B O   1 
ATOM   8743  C  CB  . SER B  1 543 ? 11.298  4.201   36.390  1.00 26.94 ? 560  SER B CB  1 
ATOM   8744  O  OG  . SER B  1 543 ? 10.615  4.340   37.626  1.00 27.60 ? 560  SER B OG  1 
ATOM   8745  N  N   . GLU B  1 544 ? 8.230   2.721   35.676  1.00 24.75 ? 561  GLU B N   1 
ATOM   8746  C  CA  . GLU B  1 544 ? 7.448   1.498   35.786  1.00 26.18 ? 561  GLU B CA  1 
ATOM   8747  C  C   . GLU B  1 544 ? 7.491   0.750   34.457  1.00 24.43 ? 561  GLU B C   1 
ATOM   8748  O  O   . GLU B  1 544 ? 7.436   1.358   33.391  1.00 23.50 ? 561  GLU B O   1 
ATOM   8749  C  CB  . GLU B  1 544 ? 5.973   1.695   36.143  1.00 28.85 ? 561  GLU B CB  1 
ATOM   8750  C  CG  . GLU B  1 544 ? 5.747   2.189   37.570  1.00 31.87 ? 561  GLU B CG  1 
ATOM   8751  C  CD  . GLU B  1 544 ? 5.864   3.691   37.762  1.00 34.40 ? 561  GLU B CD  1 
ATOM   8752  O  OE1 . GLU B  1 544 ? 6.036   4.413   36.756  1.00 35.89 ? 561  GLU B OE1 1 
ATOM   8753  O  OE2 . GLU B  1 544 ? 5.787   4.139   38.925  1.00 36.23 ? 561  GLU B OE2 1 
ATOM   8754  N  N   . TYR B  1 545 ? 7.559   -0.581  34.544  1.00 24.14 ? 562  TYR B N   1 
ATOM   8755  C  CA  . TYR B  1 545 ? 7.527   -1.441  33.375  1.00 24.92 ? 562  TYR B CA  1 
ATOM   8756  C  C   . TYR B  1 545 ? 6.170   -1.329  32.686  1.00 26.58 ? 562  TYR B C   1 
ATOM   8757  O  O   . TYR B  1 545 ? 5.142   -1.182  33.347  1.00 26.46 ? 562  TYR B O   1 
ATOM   8758  C  CB  . TYR B  1 545 ? 7.732   -2.908  33.764  1.00 24.39 ? 562  TYR B CB  1 
ATOM   8759  C  CG  . TYR B  1 545 ? 9.116   -3.306  34.260  1.00 23.59 ? 562  TYR B CG  1 
ATOM   8760  C  CD1 . TYR B  1 545 ? 10.273  -2.873  33.620  1.00 23.08 ? 562  TYR B CD1 1 
ATOM   8761  C  CD2 . TYR B  1 545 ? 9.262   -4.148  35.357  1.00 23.16 ? 562  TYR B CD2 1 
ATOM   8762  C  CE1 . TYR B  1 545 ? 11.529  -3.261  34.060  1.00 22.32 ? 562  TYR B CE1 1 
ATOM   8763  C  CE2 . TYR B  1 545 ? 10.512  -4.542  35.808  1.00 22.28 ? 562  TYR B CE2 1 
ATOM   8764  C  CZ  . TYR B  1 545 ? 11.649  -4.097  35.157  1.00 22.24 ? 562  TYR B CZ  1 
ATOM   8765  O  OH  . TYR B  1 545 ? 12.884  -4.477  35.600  1.00 20.94 ? 562  TYR B OH  1 
ATOM   8766  N  N   . ASP B  1 546 ? 6.189   -1.424  31.355  1.00 28.63 ? 563  ASP B N   1 
ATOM   8767  C  CA  . ASP B  1 546 ? 4.971   -1.580  30.576  1.00 31.52 ? 563  ASP B CA  1 
ATOM   8768  C  C   . ASP B  1 546 ? 4.723   -3.065  30.326  1.00 29.90 ? 563  ASP B C   1 
ATOM   8769  O  O   . ASP B  1 546 ? 5.637   -3.884  30.424  1.00 27.60 ? 563  ASP B O   1 
ATOM   8770  C  CB  . ASP B  1 546 ? 5.046   -0.832  29.253  1.00 34.90 ? 563  ASP B CB  1 
ATOM   8771  C  CG  . ASP B  1 546 ? 5.294   0.665   29.361  1.00 38.66 ? 563  ASP B CG  1 
ATOM   8772  O  OD1 . ASP B  1 546 ? 4.637   1.311   30.212  1.00 41.74 ? 563  ASP B OD1 1 
ATOM   8773  O  OD2 . ASP B  1 546 ? 6.136   1.174   28.589  1.00 41.21 ? 563  ASP B OD2 1 
ATOM   8774  N  N   . SER B  1 547 ? 3.469   -3.396  30.006  1.00 27.97 ? 564  SER B N   1 
ATOM   8775  C  CA  . SER B  1 547 ? 3.132   -4.705  29.475  1.00 29.27 ? 564  SER B CA  1 
ATOM   8776  C  C   . SER B  1 547 ? 3.665   -4.814  28.046  1.00 28.84 ? 564  SER B C   1 
ATOM   8777  O  O   . SER B  1 547 ? 3.550   -3.873  27.262  1.00 28.59 ? 564  SER B O   1 
ATOM   8778  C  CB  . SER B  1 547 ? 1.639   -4.947  29.539  1.00 30.04 ? 564  SER B CB  1 
ATOM   8779  O  OG  . SER B  1 547 ? 1.285   -6.195  28.957  1.00 29.26 ? 564  SER B OG  1 
ATOM   8780  N  N   . LEU B  1 548 ? 4.293   -5.952  27.730  1.00 27.85 ? 565  LEU B N   1 
ATOM   8781  C  CA  . LEU B  1 548 ? 4.758   -6.231  26.380  1.00 28.47 ? 565  LEU B CA  1 
ATOM   8782  C  C   . LEU B  1 548 ? 4.013   -7.441  25.823  1.00 28.17 ? 565  LEU B C   1 
ATOM   8783  O  O   . LEU B  1 548 ? 4.459   -8.054  24.854  1.00 27.68 ? 565  LEU B O   1 
ATOM   8784  C  CB  . LEU B  1 548 ? 6.272   -6.446  26.380  1.00 30.53 ? 565  LEU B CB  1 
ATOM   8785  C  CG  . LEU B  1 548 ? 7.116   -5.233  26.786  1.00 31.74 ? 565  LEU B CG  1 
ATOM   8786  C  CD1 . LEU B  1 548 ? 8.579   -5.627  26.930  1.00 32.98 ? 565  LEU B CD1 1 
ATOM   8787  C  CD2 . LEU B  1 548 ? 6.971   -4.103  25.784  1.00 31.66 ? 565  LEU B CD2 1 
ATOM   8788  N  N   . LEU B  1 549 ? 2.854   -7.751  26.420  1.00 27.25 ? 566  LEU B N   1 
ATOM   8789  C  CA  . LEU B  1 549 ? 2.062   -8.902  26.026  1.00 27.08 ? 566  LEU B CA  1 
ATOM   8790  C  C   . LEU B  1 549 ? 1.323   -8.599  24.722  1.00 26.30 ? 566  LEU B C   1 
ATOM   8791  O  O   . LEU B  1 549 ? 0.548   -7.647  24.660  1.00 25.63 ? 566  LEU B O   1 
ATOM   8792  C  CB  . LEU B  1 549 ? 1.085   -9.218  27.159  1.00 28.85 ? 566  LEU B CB  1 
ATOM   8793  C  CG  . LEU B  1 549 ? 0.254   -10.493 26.993  1.00 30.80 ? 566  LEU B CG  1 
ATOM   8794  C  CD1 . LEU B  1 549 ? 1.131   -11.730 27.128  1.00 31.75 ? 566  LEU B CD1 1 
ATOM   8795  C  CD2 . LEU B  1 549 ? -0.894  -10.529 27.989  1.00 31.82 ? 566  LEU B CD2 1 
ATOM   8796  N  N   . PRO B  1 550 ? 1.507   -9.403  23.649  1.00 25.35 ? 567  PRO B N   1 
ATOM   8797  C  CA  . PRO B  1 550 ? 0.670   -9.282  22.452  1.00 25.80 ? 567  PRO B CA  1 
ATOM   8798  C  C   . PRO B  1 550 ? -0.818  -9.377  22.794  1.00 25.55 ? 567  PRO B C   1 
ATOM   8799  O  O   . PRO B  1 550 ? -1.191  -10.053 23.751  1.00 25.36 ? 567  PRO B O   1 
ATOM   8800  C  CB  . PRO B  1 550 ? 1.145   -10.451 21.571  1.00 25.27 ? 567  PRO B CB  1 
ATOM   8801  C  CG  . PRO B  1 550 ? 2.571   -10.701 22.017  1.00 25.47 ? 567  PRO B CG  1 
ATOM   8802  C  CD  . PRO B  1 550 ? 2.537   -10.449 23.517  1.00 25.60 ? 567  PRO B CD  1 
ATOM   8803  N  N   . ASP B  1 551 ? -1.656  -8.689  22.010  1.00 24.35 ? 568  ASP B N   1 
ATOM   8804  C  CA  . ASP B  1 551 ? -3.089  -8.648  22.264  1.00 25.60 ? 568  ASP B CA  1 
ATOM   8805  C  C   . ASP B  1 551 ? -3.766  -9.820  21.550  1.00 25.18 ? 568  ASP B C   1 
ATOM   8806  O  O   . ASP B  1 551 ? -3.916  -9.812  20.328  1.00 24.35 ? 568  ASP B O   1 
ATOM   8807  C  CB  . ASP B  1 551 ? -3.670  -7.302  21.853  1.00 26.76 ? 568  ASP B CB  1 
ATOM   8808  C  CG  . ASP B  1 551 ? -5.096  -7.030  22.313  1.00 28.34 ? 568  ASP B CG  1 
ATOM   8809  O  OD1 . ASP B  1 551 ? -5.607  -7.809  23.151  1.00 28.26 ? 568  ASP B OD1 1 
ATOM   8810  O  OD2 . ASP B  1 551 ? -5.682  -6.037  21.834  1.00 29.47 ? 568  ASP B OD2 1 
ATOM   8811  N  N   . VAL B  1 552 ? -4.181  -10.829 22.328  1.00 25.35 ? 569  VAL B N   1 
ATOM   8812  C  CA  . VAL B  1 552 ? -4.788  -12.033 21.787  1.00 25.31 ? 569  VAL B CA  1 
ATOM   8813  C  C   . VAL B  1 552 ? -6.261  -12.072 22.195  1.00 26.00 ? 569  VAL B C   1 
ATOM   8814  O  O   . VAL B  1 552 ? -6.598  -11.815 23.349  1.00 26.81 ? 569  VAL B O   1 
ATOM   8815  C  CB  . VAL B  1 552 ? -4.027  -13.282 22.276  1.00 25.47 ? 569  VAL B CB  1 
ATOM   8816  C  CG1 . VAL B  1 552 ? -4.647  -14.575 21.759  1.00 25.58 ? 569  VAL B CG1 1 
ATOM   8817  C  CG2 . VAL B  1 552 ? -2.548  -13.211 21.907  1.00 25.16 ? 569  VAL B CG2 1 
ATOM   8818  N  N   . TYR B  1 553 ? -7.130  -12.400 21.234  1.00 26.17 ? 570  TYR B N   1 
ATOM   8819  C  CA  . TYR B  1 553 ? -8.569  -12.369 21.443  1.00 27.26 ? 570  TYR B CA  1 
ATOM   8820  C  C   . TYR B  1 553 ? -9.262  -13.124 20.315  1.00 29.14 ? 570  TYR B C   1 
ATOM   8821  O  O   . TYR B  1 553 ? -8.735  -13.219 19.206  1.00 28.19 ? 570  TYR B O   1 
ATOM   8822  C  CB  . TYR B  1 553 ? -9.076  -10.926 21.521  1.00 28.41 ? 570  TYR B CB  1 
ATOM   8823  C  CG  . TYR B  1 553 ? -8.716  -10.066 20.315  1.00 26.45 ? 570  TYR B CG  1 
ATOM   8824  C  CD1 . TYR B  1 553 ? -7.511  -9.375  20.267  1.00 25.65 ? 570  TYR B CD1 1 
ATOM   8825  C  CD2 . TYR B  1 553 ? -9.577  -9.943  19.231  1.00 25.95 ? 570  TYR B CD2 1 
ATOM   8826  C  CE1 . TYR B  1 553 ? -7.177  -8.585  19.178  1.00 25.86 ? 570  TYR B CE1 1 
ATOM   8827  C  CE2 . TYR B  1 553 ? -9.251  -9.163  18.132  1.00 25.70 ? 570  TYR B CE2 1 
ATOM   8828  C  CZ  . TYR B  1 553 ? -8.038  -8.495  18.099  1.00 25.32 ? 570  TYR B CZ  1 
ATOM   8829  O  OH  . TYR B  1 553 ? -7.705  -7.714  17.030  1.00 24.93 ? 570  TYR B OH  1 
ATOM   8830  N  N   . GLU B  1 554 ? -10.452 -13.659 20.620  1.00 32.96 ? 571  GLU B N   1 
ATOM   8831  C  CA  . GLU B  1 554 ? -11.220 -14.429 19.656  1.00 35.93 ? 571  GLU B CA  1 
ATOM   8832  C  C   . GLU B  1 554 ? -11.995 -13.480 18.747  1.00 33.12 ? 571  GLU B C   1 
ATOM   8833  O  O   . GLU B  1 554 ? -12.437 -12.419 19.179  1.00 32.67 ? 571  GLU B O   1 
ATOM   8834  C  CB  . GLU B  1 554 ? -12.187 -15.386 20.353  1.00 41.40 ? 571  GLU B CB  1 
ATOM   8835  C  CG  . GLU B  1 554 ? -11.479 -16.470 21.160  1.00 46.78 ? 571  GLU B CG  1 
ATOM   8836  C  CD  . GLU B  1 554 ? -12.417 -17.530 21.708  1.00 51.69 ? 571  GLU B CD  1 
ATOM   8837  O  OE1 . GLU B  1 554 ? -13.314 -17.174 22.504  1.00 55.22 ? 571  GLU B OE1 1 
ATOM   8838  O  OE2 . GLU B  1 554 ? -12.249 -18.709 21.330  1.00 55.38 ? 571  GLU B OE2 1 
ATOM   8839  N  N   . TRP B  1 555 ? -12.129 -13.872 17.480  1.00 32.94 ? 572  TRP B N   1 
ATOM   8840  C  CA  . TRP B  1 555 ? -13.031 -13.207 16.558  1.00 35.30 ? 572  TRP B CA  1 
ATOM   8841  C  C   . TRP B  1 555 ? -14.430 -13.799 16.706  1.00 40.47 ? 572  TRP B C   1 
ATOM   8842  O  O   . TRP B  1 555 ? -14.568 -14.975 17.036  1.00 40.52 ? 572  TRP B O   1 
ATOM   8843  C  CB  . TRP B  1 555 ? -12.546 -13.362 15.112  1.00 33.00 ? 572  TRP B CB  1 
ATOM   8844  C  CG  . TRP B  1 555 ? -11.596 -12.298 14.632  1.00 30.93 ? 572  TRP B CG  1 
ATOM   8845  C  CD1 . TRP B  1 555 ? -11.193 -11.162 15.272  1.00 29.97 ? 572  TRP B CD1 1 
ATOM   8846  C  CD2 . TRP B  1 555 ? -10.963 -12.274 13.338  1.00 30.23 ? 572  TRP B CD2 1 
ATOM   8847  N  NE1 . TRP B  1 555 ? -10.341 -10.445 14.475  1.00 28.87 ? 572  TRP B NE1 1 
ATOM   8848  C  CE2 . TRP B  1 555 ? -10.183 -11.099 13.284  1.00 30.13 ? 572  TRP B CE2 1 
ATOM   8849  C  CE3 . TRP B  1 555 ? -10.974 -13.131 12.232  1.00 31.69 ? 572  TRP B CE3 1 
ATOM   8850  C  CZ2 . TRP B  1 555 ? -9.424  -10.766 12.167  1.00 31.41 ? 572  TRP B CZ2 1 
ATOM   8851  C  CZ3 . TRP B  1 555 ? -10.219 -12.801 11.128  1.00 32.48 ? 572  TRP B CZ3 1 
ATOM   8852  C  CH2 . TRP B  1 555 ? -9.460  -11.632 11.098  1.00 32.54 ? 572  TRP B CH2 1 
ATOM   8853  N  N   . PRO B  1 556 ? -15.507 -13.013 16.472  1.00 46.14 ? 573  PRO B N   1 
ATOM   8854  C  CA  . PRO B  1 556 ? -16.844 -13.581 16.291  1.00 48.65 ? 573  PRO B CA  1 
ATOM   8855  C  C   . PRO B  1 556 ? -16.884 -14.460 15.041  1.00 52.09 ? 573  PRO B C   1 
ATOM   8856  O  O   . PRO B  1 556 ? -16.382 -14.066 13.990  1.00 52.71 ? 573  PRO B O   1 
ATOM   8857  C  CB  . PRO B  1 556 ? -17.763 -12.346 16.172  1.00 47.56 ? 573  PRO B CB  1 
ATOM   8858  C  CG  . PRO B  1 556 ? -16.949 -11.208 16.756  1.00 48.15 ? 573  PRO B CG  1 
ATOM   8859  C  CD  . PRO B  1 556 ? -15.505 -11.542 16.419  1.00 47.27 ? 573  PRO B CD  1 
ATOM   8860  N  N   . GLU B  1 557 ? -17.475 -15.655 15.167  1.00 55.59 ? 574  GLU B N   1 
ATOM   8861  C  CA  . GLU B  1 557 ? -17.577 -16.587 14.052  1.00 58.55 ? 574  GLU B CA  1 
ATOM   8862  C  C   . GLU B  1 557 ? -18.821 -16.251 13.210  1.00 59.54 ? 574  GLU B C   1 
ATOM   8863  O  O   . GLU B  1 557 ? -19.772 -15.683 13.792  1.00 63.88 ? 574  GLU B O   1 
ATOM   8864  C  CB  . GLU B  1 557 ? -17.636 -18.033 14.547  1.00 58.79 ? 574  GLU B CB  1 
ATOM   8865  N  N   . LYS C  1 5   ? 15.532  -11.363 10.396  1.00 68.24 ? 22   LYS C N   1 
ATOM   8866  C  CA  . LYS C  1 5   ? 15.393  -12.729 9.819   1.00 67.76 ? 22   LYS C CA  1 
ATOM   8867  C  C   . LYS C  1 5   ? 15.812  -12.722 8.350   1.00 64.50 ? 22   LYS C C   1 
ATOM   8868  O  O   . LYS C  1 5   ? 16.662  -13.522 7.962   1.00 64.05 ? 22   LYS C O   1 
ATOM   8869  C  CB  . LYS C  1 5   ? 13.974  -13.293 9.961   1.00 70.21 ? 22   LYS C CB  1 
ATOM   8870  C  CG  . LYS C  1 5   ? 13.525  -13.579 11.388  1.00 73.55 ? 22   LYS C CG  1 
ATOM   8871  C  CD  . LYS C  1 5   ? 14.314  -14.669 12.104  1.00 76.33 ? 22   LYS C CD  1 
ATOM   8872  C  CE  . LYS C  1 5   ? 13.763  -14.935 13.468  1.00 80.38 ? 22   LYS C CE  1 
ATOM   8873  N  NZ  . LYS C  1 5   ? 14.562  -15.923 14.197  1.00 83.13 ? 22   LYS C NZ  1 
ATOM   8874  N  N   . GLU C  1 6   ? 15.212  -11.832 7.540   1.00 59.29 ? 23   GLU C N   1 
ATOM   8875  C  CA  . GLU C  1 6   ? 15.512  -11.796 6.115   1.00 56.06 ? 23   GLU C CA  1 
ATOM   8876  C  C   . GLU C  1 6   ? 17.014  -11.579 5.953   1.00 56.10 ? 23   GLU C C   1 
ATOM   8877  O  O   . GLU C  1 6   ? 17.527  -10.498 6.237   1.00 54.06 ? 23   GLU C O   1 
ATOM   8878  C  CB  . GLU C  1 6   ? 14.720  -10.761 5.308   1.00 53.53 ? 23   GLU C CB  1 
ATOM   8879  C  CG  . GLU C  1 6   ? 14.846  -10.970 3.798   1.00 51.58 ? 23   GLU C CG  1 
ATOM   8880  C  CD  . GLU C  1 6   ? 14.056  -10.039 2.887   1.00 50.00 ? 23   GLU C CD  1 
ATOM   8881  O  OE1 . GLU C  1 6   ? 13.531  -9.007  3.350   1.00 50.22 ? 23   GLU C OE1 1 
ATOM   8882  O  OE2 . GLU C  1 6   ? 13.956  -10.365 1.685   1.00 47.01 ? 23   GLU C OE2 1 
ATOM   8883  N  N   . LYS C  1 7   ? 17.707  -12.636 5.514   1.00 55.09 ? 24   LYS C N   1 
ATOM   8884  C  CA  . LYS C  1 7   ? 19.157  -12.632 5.430   1.00 54.71 ? 24   LYS C CA  1 
ATOM   8885  C  C   . LYS C  1 7   ? 19.592  -11.796 4.229   1.00 50.62 ? 24   LYS C C   1 
ATOM   8886  O  O   . LYS C  1 7   ? 19.047  -11.942 3.136   1.00 49.70 ? 24   LYS C O   1 
ATOM   8887  C  CB  . LYS C  1 7   ? 19.681  -14.069 5.347   1.00 56.70 ? 24   LYS C CB  1 
ATOM   8888  C  CG  . LYS C  1 7   ? 19.261  -14.959 6.512   1.00 58.68 ? 24   LYS C CG  1 
ATOM   8889  C  CD  . LYS C  1 7   ? 20.124  -16.202 6.692   1.00 60.75 ? 24   LYS C CD  1 
ATOM   8890  C  CE  . LYS C  1 7   ? 21.504  -15.872 7.171   1.00 62.48 ? 24   LYS C CE  1 
ATOM   8891  N  NZ  . LYS C  1 7   ? 22.367  -17.055 7.185   1.00 64.33 ? 24   LYS C NZ  1 
ATOM   8892  N  N   . GLY C  1 8   ? 20.581  -10.924 4.456   1.00 46.96 ? 25   GLY C N   1 
ATOM   8893  C  CA  . GLY C  1 8   ? 21.052  -9.991  3.447   1.00 45.06 ? 25   GLY C CA  1 
ATOM   8894  C  C   . GLY C  1 8   ? 21.396  -8.643  4.071   1.00 44.78 ? 25   GLY C C   1 
ATOM   8895  O  O   . GLY C  1 8   ? 21.263  -8.466  5.283   1.00 43.83 ? 25   GLY C O   1 
ATOM   8896  N  N   . LYS C  1 9   ? 21.834  -7.701  3.225   1.00 42.88 ? 26   LYS C N   1 
ATOM   8897  C  CA  . LYS C  1 9   ? 22.224  -6.373  3.671   1.00 42.27 ? 26   LYS C CA  1 
ATOM   8898  C  C   . LYS C  1 9   ? 20.980  -5.487  3.727   1.00 41.26 ? 26   LYS C C   1 
ATOM   8899  O  O   . LYS C  1 9   ? 20.382  -5.202  2.693   1.00 37.07 ? 26   LYS C O   1 
ATOM   8900  C  CB  . LYS C  1 9   ? 23.298  -5.797  2.742   1.00 42.91 ? 26   LYS C CB  1 
ATOM   8901  N  N   . PRO C  1 10  ? 20.549  -5.035  4.930   1.00 40.49 ? 27   PRO C N   1 
ATOM   8902  C  CA  . PRO C  1 10  ? 19.323  -4.240  5.070   1.00 39.62 ? 27   PRO C CA  1 
ATOM   8903  C  C   . PRO C  1 10  ? 19.126  -3.100  4.069   1.00 38.77 ? 27   PRO C C   1 
ATOM   8904  O  O   . PRO C  1 10  ? 17.997  -2.812  3.676   1.00 37.27 ? 27   PRO C O   1 
ATOM   8905  C  CB  . PRO C  1 10  ? 19.436  -3.705  6.515   1.00 40.10 ? 27   PRO C CB  1 
ATOM   8906  C  CG  . PRO C  1 10  ? 20.221  -4.767  7.243   1.00 40.38 ? 27   PRO C CG  1 
ATOM   8907  C  CD  . PRO C  1 10  ? 21.214  -5.281  6.221   1.00 39.79 ? 27   PRO C CD  1 
ATOM   8908  N  N   . LEU C  1 11  ? 20.221  -2.446  3.660   1.00 36.32 ? 28   LEU C N   1 
ATOM   8909  C  CA  . LEU C  1 11  ? 20.114  -1.264  2.819   1.00 35.26 ? 28   LEU C CA  1 
ATOM   8910  C  C   . LEU C  1 11  ? 19.613  -1.626  1.418   1.00 33.26 ? 28   LEU C C   1 
ATOM   8911  O  O   . LEU C  1 11  ? 18.961  -0.790  0.797   1.00 32.74 ? 28   LEU C O   1 
ATOM   8912  C  CB  . LEU C  1 11  ? 21.428  -0.481  2.777   1.00 35.55 ? 28   LEU C CB  1 
ATOM   8913  C  CG  . LEU C  1 11  ? 21.778  0.310   4.043   1.00 36.47 ? 28   LEU C CG  1 
ATOM   8914  C  CD1 . LEU C  1 11  ? 23.169  0.903   3.935   1.00 37.51 ? 28   LEU C CD1 1 
ATOM   8915  C  CD2 . LEU C  1 11  ? 20.769  1.409   4.344   1.00 37.09 ? 28   LEU C CD2 1 
ATOM   8916  N  N   . MET C  1 12  ? 19.879  -2.847  0.919   1.00 30.61 ? 29   MET C N   1 
ATOM   8917  C  CA  . MET C  1 12  ? 19.358  -3.226  -0.391  1.00 31.03 ? 29   MET C CA  1 
ATOM   8918  C  C   . MET C  1 12  ? 18.001  -3.920  -0.261  1.00 29.27 ? 29   MET C C   1 
ATOM   8919  O  O   . MET C  1 12  ? 17.214  -3.880  -1.201  1.00 29.93 ? 29   MET C O   1 
ATOM   8920  C  CB  . MET C  1 12  ? 20.358  -4.035  -1.239  1.00 32.91 ? 29   MET C CB  1 
ATOM   8921  C  CG  . MET C  1 12  ? 20.428  -5.531  -0.999  1.00 35.30 ? 29   MET C CG  1 
ATOM   8922  S  SD  . MET C  1 12  ? 21.756  -6.318  -1.947  1.00 35.51 ? 29   MET C SD  1 
ATOM   8923  C  CE  . MET C  1 12  ? 21.246  -6.141  -3.659  1.00 32.42 ? 29   MET C CE  1 
ATOM   8924  N  N   . LEU C  1 13  ? 17.705  -4.515  0.901   1.00 27.68 ? 30   LEU C N   1 
ATOM   8925  C  CA  . LEU C  1 13  ? 16.448  -5.224  1.095   1.00 27.20 ? 30   LEU C CA  1 
ATOM   8926  C  C   . LEU C  1 13  ? 15.301  -4.247  1.362   1.00 26.55 ? 30   LEU C C   1 
ATOM   8927  O  O   . LEU C  1 13  ? 14.156  -4.546  1.040   1.00 26.02 ? 30   LEU C O   1 
ATOM   8928  C  CB  . LEU C  1 13  ? 16.596  -6.221  2.244   1.00 27.80 ? 30   LEU C CB  1 
ATOM   8929  C  CG  . LEU C  1 13  ? 17.603  -7.357  2.030   1.00 28.98 ? 30   LEU C CG  1 
ATOM   8930  C  CD1 . LEU C  1 13  ? 17.654  -8.232  3.270   1.00 29.88 ? 30   LEU C CD1 1 
ATOM   8931  C  CD2 . LEU C  1 13  ? 17.272  -8.190  0.809   1.00 29.63 ? 30   LEU C CD2 1 
ATOM   8932  N  N   . ASN C  1 14  ? 15.608  -3.114  2.005   1.00 26.63 ? 31   ASN C N   1 
ATOM   8933  C  CA  . ASN C  1 14  ? 14.609  -2.133  2.401   1.00 26.61 ? 31   ASN C CA  1 
ATOM   8934  C  C   . ASN C  1 14  ? 14.292  -1.238  1.204   1.00 25.38 ? 31   ASN C C   1 
ATOM   8935  O  O   . ASN C  1 14  ? 15.150  -0.466  0.789   1.00 24.09 ? 31   ASN C O   1 
ATOM   8936  C  CB  . ASN C  1 14  ? 15.113  -1.318  3.590   1.00 27.90 ? 31   ASN C CB  1 
ATOM   8937  C  CG  . ASN C  1 14  ? 14.157  -0.244  4.061   1.00 28.59 ? 31   ASN C CG  1 
ATOM   8938  O  OD1 . ASN C  1 14  ? 13.061  -0.079  3.514   1.00 28.59 ? 31   ASN C OD1 1 
ATOM   8939  N  ND2 . ASN C  1 14  ? 14.548  0.488   5.094   1.00 30.23 ? 31   ASN C ND2 1 
ATOM   8940  N  N   . PRO C  1 15  ? 13.057  -1.257  0.647   1.00 25.46 ? 32   PRO C N   1 
ATOM   8941  C  CA  . PRO C  1 15  ? 12.739  -0.438  -0.525  1.00 25.81 ? 32   PRO C CA  1 
ATOM   8942  C  C   . PRO C  1 15  ? 12.929  1.059   -0.293  1.00 25.42 ? 32   PRO C C   1 
ATOM   8943  O  O   . PRO C  1 15  ? 13.108  1.816   -1.243  1.00 24.50 ? 32   PRO C O   1 
ATOM   8944  C  CB  . PRO C  1 15  ? 11.283  -0.790  -0.862  1.00 26.07 ? 32   PRO C CB  1 
ATOM   8945  C  CG  . PRO C  1 15  ? 10.735  -1.398  0.402   1.00 27.30 ? 32   PRO C CG  1 
ATOM   8946  C  CD  . PRO C  1 15  ? 11.908  -2.054  1.103   1.00 26.30 ? 32   PRO C CD  1 
ATOM   8947  N  N   . ARG C  1 16  ? 12.913  1.469   0.978   1.00 26.23 ? 33   ARG C N   1 
ATOM   8948  C  CA  . ARG C  1 16  ? 13.046  2.867   1.341   1.00 28.04 ? 33   ARG C CA  1 
ATOM   8949  C  C   . ARG C  1 16  ? 14.462  3.371   1.054   1.00 26.60 ? 33   ARG C C   1 
ATOM   8950  O  O   . ARG C  1 16  ? 14.631  4.527   0.678   1.00 26.68 ? 33   ARG C O   1 
ATOM   8951  C  CB  . ARG C  1 16  ? 12.614  2.997   2.805   1.00 32.15 ? 33   ARG C CB  1 
ATOM   8952  C  CG  . ARG C  1 16  ? 12.317  4.412   3.278   1.00 36.07 ? 33   ARG C CG  1 
ATOM   8953  C  CD  . ARG C  1 16  ? 11.084  4.400   4.175   1.00 38.46 ? 33   ARG C CD  1 
ATOM   8954  N  NE  . ARG C  1 16  ? 9.870   4.163   3.384   1.00 40.47 ? 33   ARG C NE  1 
ATOM   8955  C  CZ  . ARG C  1 16  ? 8.668   3.821   3.842   1.00 42.10 ? 33   ARG C CZ  1 
ATOM   8956  N  NH1 . ARG C  1 16  ? 8.491   3.523   5.119   1.00 43.32 ? 33   ARG C NH1 1 
ATOM   8957  N  NH2 . ARG C  1 16  ? 7.643   3.751   3.008   1.00 40.67 ? 33   ARG C NH2 1 
ATOM   8958  N  N   . THR C  1 17  ? 15.474  2.509   1.228   1.00 25.09 ? 34   THR C N   1 
ATOM   8959  C  CA  . THR C  1 17  ? 16.861  2.912   1.032   1.00 24.43 ? 34   THR C CA  1 
ATOM   8960  C  C   . THR C  1 17  ? 17.449  2.311   -0.249  1.00 23.40 ? 34   THR C C   1 
ATOM   8961  O  O   . THR C  1 17  ? 18.428  2.840   -0.771  1.00 23.46 ? 34   THR C O   1 
ATOM   8962  C  CB  . THR C  1 17  ? 17.697  2.543   2.261   1.00 24.86 ? 34   THR C CB  1 
ATOM   8963  O  OG1 . THR C  1 17  ? 17.566  1.148   2.508   1.00 24.53 ? 34   THR C OG1 1 
ATOM   8964  C  CG2 . THR C  1 17  ? 17.257  3.290   3.507   1.00 26.16 ? 34   THR C CG2 1 
ATOM   8965  N  N   . ASN C  1 18  ? 16.858  1.223   -0.758  1.00 22.33 ? 35   ASN C N   1 
ATOM   8966  C  CA  . ASN C  1 18  ? 17.417  0.472   -1.874  1.00 21.63 ? 35   ASN C CA  1 
ATOM   8967  C  C   . ASN C  1 18  ? 17.533  1.347   -3.122  1.00 21.19 ? 35   ASN C C   1 
ATOM   8968  O  O   . ASN C  1 18  ? 16.582  2.025   -3.511  1.00 20.61 ? 35   ASN C O   1 
ATOM   8969  C  CB  . ASN C  1 18  ? 16.600  -0.784  -2.156  1.00 21.61 ? 35   ASN C CB  1 
ATOM   8970  C  CG  . ASN C  1 18  ? 17.119  -1.581  -3.332  1.00 21.76 ? 35   ASN C CG  1 
ATOM   8971  O  OD1 . ASN C  1 18  ? 18.336  -1.770  -3.482  1.00 21.26 ? 35   ASN C OD1 1 
ATOM   8972  N  ND2 . ASN C  1 18  ? 16.217  -2.060  -4.176  1.00 21.25 ? 35   ASN C ND2 1 
ATOM   8973  N  N   . LYS C  1 19  ? 18.716  1.293   -3.749  1.00 21.50 ? 36   LYS C N   1 
ATOM   8974  C  CA  . LYS C  1 19  ? 19.017  2.007   -4.981  1.00 21.81 ? 36   LYS C CA  1 
ATOM   8975  C  C   . LYS C  1 19  ? 19.233  1.031   -6.139  1.00 21.28 ? 36   LYS C C   1 
ATOM   8976  O  O   . LYS C  1 19  ? 19.346  1.457   -7.284  1.00 20.97 ? 36   LYS C O   1 
ATOM   8977  C  CB  . LYS C  1 19  ? 20.264  2.875   -4.780  1.00 23.36 ? 36   LYS C CB  1 
ATOM   8978  C  CG  . LYS C  1 19  ? 20.117  3.941   -3.690  1.00 25.61 ? 36   LYS C CG  1 
ATOM   8979  C  CD  . LYS C  1 19  ? 21.409  4.588   -3.203  1.00 27.35 ? 36   LYS C CD  1 
ATOM   8980  C  CE  . LYS C  1 19  ? 22.191  5.274   -4.262  1.00 28.63 ? 36   LYS C CE  1 
ATOM   8981  N  NZ  . LYS C  1 19  ? 23.233  6.139   -3.699  1.00 28.83 ? 36   LYS C NZ  1 
ATOM   8982  N  N   . GLY C  1 20  ? 19.301  -0.274  -5.848  1.00 21.19 ? 37   GLY C N   1 
ATOM   8983  C  CA  . GLY C  1 20  ? 19.483  -1.276  -6.886  1.00 20.51 ? 37   GLY C CA  1 
ATOM   8984  C  C   . GLY C  1 20  ? 20.787  -1.029  -7.640  1.00 20.96 ? 37   GLY C C   1 
ATOM   8985  O  O   . GLY C  1 20  ? 21.822  -0.798  -7.022  1.00 20.25 ? 37   GLY C O   1 
ATOM   8986  N  N   . MET C  1 21  ? 20.715  -0.995  -8.974  1.00 21.56 ? 38   MET C N   1 
ATOM   8987  C  CA  . MET C  1 21  ? 21.908  -0.860  -9.795  1.00 23.58 ? 38   MET C CA  1 
ATOM   8988  C  C   . MET C  1 21  ? 22.493  0.554   -9.727  1.00 23.33 ? 38   MET C C   1 
ATOM   8989  O  O   . MET C  1 21  ? 23.580  0.775   -10.257 1.00 23.06 ? 38   MET C O   1 
ATOM   8990  C  CB  . MET C  1 21  ? 21.618  -1.270  -11.242 1.00 26.56 ? 38   MET C CB  1 
ATOM   8991  C  CG  . MET C  1 21  ? 21.548  -2.780  -11.400 1.00 29.95 ? 38   MET C CG  1 
ATOM   8992  S  SD  . MET C  1 21  ? 21.480  -3.321  -13.114 1.00 38.15 ? 38   MET C SD  1 
ATOM   8993  C  CE  . MET C  1 21  ? 23.117  -2.826  -13.662 1.00 38.72 ? 38   MET C CE  1 
ATOM   8994  N  N   . ALA C  1 22  ? 21.812  1.485   -9.040  1.00 22.23 ? 39   ALA C N   1 
ATOM   8995  C  CA  . ALA C  1 22  ? 22.342  2.827   -8.830  1.00 21.77 ? 39   ALA C CA  1 
ATOM   8996  C  C   . ALA C  1 22  ? 23.274  2.910   -7.620  1.00 20.62 ? 39   ALA C C   1 
ATOM   8997  O  O   . ALA C  1 22  ? 23.871  3.958   -7.392  1.00 20.47 ? 39   ALA C O   1 
ATOM   8998  C  CB  . ALA C  1 22  ? 21.214  3.830   -8.704  1.00 21.42 ? 39   ALA C CB  1 
ATOM   8999  N  N   . PHE C  1 23  ? 23.409  1.836   -6.832  1.00 19.66 ? 40   PHE C N   1 
ATOM   9000  C  CA  . PHE C  1 23  ? 24.453  1.802   -5.823  1.00 20.14 ? 40   PHE C CA  1 
ATOM   9001  C  C   . PHE C  1 23  ? 25.794  1.955   -6.542  1.00 19.80 ? 40   PHE C C   1 
ATOM   9002  O  O   . PHE C  1 23  ? 26.027  1.281   -7.541  1.00 19.31 ? 40   PHE C O   1 
ATOM   9003  C  CB  . PHE C  1 23  ? 24.480  0.525   -4.973  1.00 20.69 ? 40   PHE C CB  1 
ATOM   9004  C  CG  . PHE C  1 23  ? 23.460  0.429   -3.843  1.00 20.82 ? 40   PHE C CG  1 
ATOM   9005  C  CD1 . PHE C  1 23  ? 23.585  1.212   -2.699  1.00 21.91 ? 40   PHE C CD1 1 
ATOM   9006  C  CD2 . PHE C  1 23  ? 22.421  -0.494  -3.894  1.00 20.98 ? 40   PHE C CD2 1 
ATOM   9007  C  CE1 . PHE C  1 23  ? 22.677  1.102   -1.654  1.00 21.47 ? 40   PHE C CE1 1 
ATOM   9008  C  CE2 . PHE C  1 23  ? 21.516  -0.602  -2.847  1.00 20.86 ? 40   PHE C CE2 1 
ATOM   9009  C  CZ  . PHE C  1 23  ? 21.649  0.190   -1.727  1.00 20.79 ? 40   PHE C CZ  1 
ATOM   9010  N  N   . THR C  1 24  ? 26.660  2.843   -6.032  1.00 19.84 ? 41   THR C N   1 
ATOM   9011  C  CA  . THR C  1 24  ? 27.946  3.115   -6.663  1.00 20.92 ? 41   THR C CA  1 
ATOM   9012  C  C   . THR C  1 24  ? 28.904  1.971   -6.339  1.00 21.11 ? 41   THR C C   1 
ATOM   9013  O  O   . THR C  1 24  ? 28.670  1.200   -5.413  1.00 20.15 ? 41   THR C O   1 
ATOM   9014  C  CB  . THR C  1 24  ? 28.533  4.460   -6.227  1.00 21.93 ? 41   THR C CB  1 
ATOM   9015  O  OG1 . THR C  1 24  ? 28.939  4.344   -4.867  1.00 22.74 ? 41   THR C OG1 1 
ATOM   9016  C  CG2 . THR C  1 24  ? 27.577  5.625   -6.417  1.00 23.00 ? 41   THR C CG2 1 
ATOM   9017  N  N   . LEU C  1 25  ? 30.009  1.886   -7.086  1.00 22.39 ? 42   LEU C N   1 
ATOM   9018  C  CA  . LEU C  1 25  ? 30.998  0.850   -6.840  1.00 23.14 ? 42   LEU C CA  1 
ATOM   9019  C  C   . LEU C  1 25  ? 31.472  0.910   -5.386  1.00 23.50 ? 42   LEU C C   1 
ATOM   9020  O  O   . LEU C  1 25  ? 31.521  -0.115  -4.705  1.00 23.21 ? 42   LEU C O   1 
ATOM   9021  C  CB  . LEU C  1 25  ? 32.166  0.952   -7.818  1.00 24.31 ? 42   LEU C CB  1 
ATOM   9022  C  CG  . LEU C  1 25  ? 33.241  -0.134  -7.680  1.00 26.12 ? 42   LEU C CG  1 
ATOM   9023  C  CD1 . LEU C  1 25  ? 32.667  -1.529  -7.892  1.00 26.39 ? 42   LEU C CD1 1 
ATOM   9024  C  CD2 . LEU C  1 25  ? 34.399  0.103   -8.641  1.00 27.38 ? 42   LEU C CD2 1 
ATOM   9025  N  N   . GLN C  1 26  ? 31.821  2.110   -4.911  1.00 24.97 ? 43   GLN C N   1 
ATOM   9026  C  CA  . GLN C  1 26  ? 32.334  2.279   -3.561  1.00 25.77 ? 43   GLN C CA  1 
ATOM   9027  C  C   . GLN C  1 26  ? 31.255  1.975   -2.523  1.00 23.47 ? 43   GLN C C   1 
ATOM   9028  O  O   . GLN C  1 26  ? 31.557  1.411   -1.475  1.00 22.89 ? 43   GLN C O   1 
ATOM   9029  C  CB  . GLN C  1 26  ? 32.898  3.678   -3.305  1.00 30.30 ? 43   GLN C CB  1 
ATOM   9030  C  CG  . GLN C  1 26  ? 34.258  3.931   -3.944  1.00 34.91 ? 43   GLN C CG  1 
ATOM   9031  C  CD  . GLN C  1 26  ? 35.176  4.761   -3.069  1.00 40.10 ? 43   GLN C CD  1 
ATOM   9032  O  OE1 . GLN C  1 26  ? 34.796  5.823   -2.561  1.00 41.40 ? 43   GLN C OE1 1 
ATOM   9033  N  NE2 . GLN C  1 26  ? 36.393  4.273   -2.866  1.00 41.97 ? 43   GLN C NE2 1 
ATOM   9034  N  N   . GLU C  1 27  ? 30.004  2.365   -2.795  1.00 22.40 ? 44   GLU C N   1 
ATOM   9035  C  CA  . GLU C  1 27  ? 28.912  2.027   -1.898  1.00 21.59 ? 44   GLU C CA  1 
ATOM   9036  C  C   . GLU C  1 27  ? 28.815  0.509   -1.777  1.00 21.46 ? 44   GLU C C   1 
ATOM   9037  O  O   . GLU C  1 27  ? 28.735  -0.018  -0.674  1.00 21.43 ? 44   GLU C O   1 
ATOM   9038  C  CB  . GLU C  1 27  ? 27.588  2.619   -2.374  1.00 22.62 ? 44   GLU C CB  1 
ATOM   9039  C  CG  . GLU C  1 27  ? 27.472  4.122   -2.119  1.00 23.39 ? 44   GLU C CG  1 
ATOM   9040  C  CD  . GLU C  1 27  ? 26.220  4.757   -2.696  1.00 23.89 ? 44   GLU C CD  1 
ATOM   9041  O  OE1 . GLU C  1 27  ? 25.557  4.150   -3.568  1.00 23.52 ? 44   GLU C OE1 1 
ATOM   9042  O  OE2 . GLU C  1 27  ? 25.889  5.873   -2.251  1.00 25.23 ? 44   GLU C OE2 1 
ATOM   9043  N  N   . ARG C  1 28  ? 28.836  -0.183  -2.922  1.00 21.88 ? 45   ARG C N   1 
ATOM   9044  C  CA  . ARG C  1 28  ? 28.697  -1.629  -2.949  1.00 22.22 ? 45   ARG C CA  1 
ATOM   9045  C  C   . ARG C  1 28  ? 29.798  -2.290  -2.123  1.00 22.38 ? 45   ARG C C   1 
ATOM   9046  O  O   . ARG C  1 28  ? 29.522  -3.180  -1.319  1.00 23.16 ? 45   ARG C O   1 
ATOM   9047  C  CB  . ARG C  1 28  ? 28.725  -2.146  -4.393  1.00 22.21 ? 45   ARG C CB  1 
ATOM   9048  C  CG  . ARG C  1 28  ? 27.510  -1.742  -5.212  1.00 22.32 ? 45   ARG C CG  1 
ATOM   9049  C  CD  . ARG C  1 28  ? 27.646  -2.212  -6.643  1.00 22.77 ? 45   ARG C CD  1 
ATOM   9050  N  NE  . ARG C  1 28  ? 26.660  -1.594  -7.534  1.00 22.86 ? 45   ARG C NE  1 
ATOM   9051  C  CZ  . ARG C  1 28  ? 26.353  -2.031  -8.749  1.00 22.76 ? 45   ARG C CZ  1 
ATOM   9052  N  NH1 . ARG C  1 28  ? 26.934  -3.106  -9.238  1.00 22.81 ? 45   ARG C NH1 1 
ATOM   9053  N  NH2 . ARG C  1 28  ? 25.446  -1.396  -9.467  1.00 23.34 ? 45   ARG C NH2 1 
ATOM   9054  N  N   . GLN C  1 29  ? 31.047  -1.863  -2.331  1.00 21.51 ? 46   GLN C N   1 
ATOM   9055  C  CA  . GLN C  1 29  ? 32.175  -2.478  -1.648  1.00 23.33 ? 46   GLN C CA  1 
ATOM   9056  C  C   . GLN C  1 29  ? 32.089  -2.235  -0.140  1.00 23.58 ? 46   GLN C C   1 
ATOM   9057  O  O   . GLN C  1 29  ? 32.228  -3.170  0.648   1.00 23.28 ? 46   GLN C O   1 
ATOM   9058  C  CB  . GLN C  1 29  ? 33.475  -1.994  -2.289  1.00 23.87 ? 46   GLN C CB  1 
ATOM   9059  C  CG  . GLN C  1 29  ? 33.666  -2.508  -3.713  1.00 24.48 ? 46   GLN C CG  1 
ATOM   9060  C  CD  . GLN C  1 29  ? 34.930  -1.997  -4.371  1.00 26.58 ? 46   GLN C CD  1 
ATOM   9061  O  OE1 . GLN C  1 29  ? 35.537  -1.013  -3.930  1.00 27.92 ? 46   GLN C OE1 1 
ATOM   9062  N  NE2 . GLN C  1 29  ? 35.341  -2.657  -5.444  1.00 25.83 ? 46   GLN C NE2 1 
ATOM   9063  N  N   . MET C  1 30  ? 31.811  -0.990  0.260   1.00 23.66 ? 47   MET C N   1 
ATOM   9064  C  CA  . MET C  1 30  ? 31.839  -0.622  1.667   1.00 24.61 ? 47   MET C CA  1 
ATOM   9065  C  C   . MET C  1 30  ? 30.643  -1.212  2.414   1.00 24.65 ? 47   MET C C   1 
ATOM   9066  O  O   . MET C  1 30  ? 30.769  -1.548  3.589   1.00 26.22 ? 47   MET C O   1 
ATOM   9067  C  CB  . MET C  1 30  ? 31.868  0.901   1.854   1.00 25.18 ? 47   MET C CB  1 
ATOM   9068  C  CG  . MET C  1 30  ? 33.188  1.547   1.482   1.00 26.59 ? 47   MET C CG  1 
ATOM   9069  S  SD  . MET C  1 30  ? 33.342  3.217   2.155   1.00 29.10 ? 47   MET C SD  1 
ATOM   9070  C  CE  . MET C  1 30  ? 34.777  3.766   1.218   1.00 28.33 ? 47   MET C CE  1 
ATOM   9071  N  N   . LEU C  1 31  ? 29.496  -1.351  1.737   1.00 24.18 ? 48   LEU C N   1 
ATOM   9072  C  CA  . LEU C  1 31  ? 28.275  -1.806  2.384   1.00 24.95 ? 48   LEU C CA  1 
ATOM   9073  C  C   . LEU C  1 31  ? 28.073  -3.317  2.241   1.00 24.15 ? 48   LEU C C   1 
ATOM   9074  O  O   . LEU C  1 31  ? 27.049  -3.832  2.676   1.00 24.30 ? 48   LEU C O   1 
ATOM   9075  C  CB  . LEU C  1 31  ? 27.085  -1.029  1.824   1.00 25.83 ? 48   LEU C CB  1 
ATOM   9076  C  CG  . LEU C  1 31  ? 27.132  0.491   2.008   1.00 26.53 ? 48   LEU C CG  1 
ATOM   9077  C  CD1 . LEU C  1 31  ? 25.971  1.139   1.288   1.00 26.68 ? 48   LEU C CD1 1 
ATOM   9078  C  CD2 . LEU C  1 31  ? 27.124  0.878   3.480   1.00 28.46 ? 48   LEU C CD2 1 
ATOM   9079  N  N   . GLY C  1 32  ? 29.044  -4.033  1.664   1.00 24.25 ? 49   GLY C N   1 
ATOM   9080  C  CA  . GLY C  1 32  ? 28.966  -5.485  1.551   1.00 23.77 ? 49   GLY C CA  1 
ATOM   9081  C  C   . GLY C  1 32  ? 27.988  -5.951  0.470   1.00 23.16 ? 49   GLY C C   1 
ATOM   9082  O  O   . GLY C  1 32  ? 27.436  -7.041  0.580   1.00 24.99 ? 49   GLY C O   1 
ATOM   9083  N  N   . LEU C  1 33  ? 27.809  -5.152  -0.589  1.00 21.90 ? 50   LEU C N   1 
ATOM   9084  C  CA  . LEU C  1 33  ? 26.882  -5.477  -1.667  1.00 21.86 ? 50   LEU C CA  1 
ATOM   9085  C  C   . LEU C  1 33  ? 27.617  -5.989  -2.908  1.00 21.22 ? 50   LEU C C   1 
ATOM   9086  O  O   . LEU C  1 33  ? 26.977  -6.444  -3.853  1.00 22.37 ? 50   LEU C O   1 
ATOM   9087  C  CB  . LEU C  1 33  ? 26.041  -4.249  -2.016  1.00 22.01 ? 50   LEU C CB  1 
ATOM   9088  C  CG  . LEU C  1 33  ? 25.378  -3.519  -0.844  1.00 22.55 ? 50   LEU C CG  1 
ATOM   9089  C  CD1 . LEU C  1 33  ? 24.506  -2.387  -1.362  1.00 22.76 ? 50   LEU C CD1 1 
ATOM   9090  C  CD2 . LEU C  1 33  ? 24.561  -4.453  0.029   1.00 23.12 ? 50   LEU C CD2 1 
ATOM   9091  N  N   . GLN C  1 34  ? 28.951  -5.910  -2.923  1.00 21.88 ? 51   GLN C N   1 
ATOM   9092  C  CA  . GLN C  1 34  ? 29.714  -6.235  -4.117  1.00 22.50 ? 51   GLN C CA  1 
ATOM   9093  C  C   . GLN C  1 34  ? 29.459  -7.698  -4.473  1.00 22.38 ? 51   GLN C C   1 
ATOM   9094  O  O   . GLN C  1 34  ? 29.578  -8.577  -3.622  1.00 22.52 ? 51   GLN C O   1 
ATOM   9095  C  CB  . GLN C  1 34  ? 31.196  -5.928  -3.893  1.00 23.49 ? 51   GLN C CB  1 
ATOM   9096  C  CG  . GLN C  1 34  ? 32.078  -6.106  -5.125  1.00 24.51 ? 51   GLN C CG  1 
ATOM   9097  C  CD  . GLN C  1 34  ? 31.865  -5.046  -6.184  1.00 25.73 ? 51   GLN C CD  1 
ATOM   9098  O  OE1 . GLN C  1 34  ? 30.976  -4.197  -6.082  1.00 24.78 ? 51   GLN C OE1 1 
ATOM   9099  N  NE2 . GLN C  1 34  ? 32.697  -5.076  -7.215  1.00 27.51 ? 51   GLN C NE2 1 
ATOM   9100  N  N   . GLY C  1 35  ? 29.053  -7.936  -5.724  1.00 22.65 ? 52   GLY C N   1 
ATOM   9101  C  CA  . GLY C  1 35  ? 28.729  -9.275  -6.188  1.00 22.81 ? 52   GLY C CA  1 
ATOM   9102  C  C   . GLY C  1 35  ? 27.237  -9.602  -6.103  1.00 22.65 ? 52   GLY C C   1 
ATOM   9103  O  O   . GLY C  1 35  ? 26.791  -10.568 -6.725  1.00 23.04 ? 52   GLY C O   1 
ATOM   9104  N  N   . LEU C  1 36  ? 26.468  -8.807  -5.344  1.00 21.44 ? 53   LEU C N   1 
ATOM   9105  C  CA  . LEU C  1 36  ? 25.045  -9.058  -5.161  1.00 21.34 ? 53   LEU C CA  1 
ATOM   9106  C  C   . LEU C  1 36  ? 24.246  -8.290  -6.211  1.00 20.99 ? 53   LEU C C   1 
ATOM   9107  O  O   . LEU C  1 36  ? 23.025  -8.408  -6.269  1.00 21.74 ? 53   LEU C O   1 
ATOM   9108  C  CB  . LEU C  1 36  ? 24.617  -8.682  -3.740  1.00 21.44 ? 53   LEU C CB  1 
ATOM   9109  C  CG  . LEU C  1 36  ? 25.305  -9.447  -2.603  1.00 21.41 ? 53   LEU C CG  1 
ATOM   9110  C  CD1 . LEU C  1 36  ? 24.790  -9.034  -1.229  1.00 21.91 ? 53   LEU C CD1 1 
ATOM   9111  C  CD2 . LEU C  1 36  ? 25.149  -10.943 -2.783  1.00 21.93 ? 53   LEU C CD2 1 
ATOM   9112  N  N   . LEU C  1 37  ? 24.950  -7.491  -7.022  1.00 21.01 ? 54   LEU C N   1 
ATOM   9113  C  CA  . LEU C  1 37  ? 24.361  -6.772  -8.140  1.00 21.70 ? 54   LEU C CA  1 
ATOM   9114  C  C   . LEU C  1 37  ? 25.221  -7.010  -9.379  1.00 21.47 ? 54   LEU C C   1 
ATOM   9115  O  O   . LEU C  1 37  ? 26.406  -7.297  -9.259  1.00 21.37 ? 54   LEU C O   1 
ATOM   9116  C  CB  . LEU C  1 37  ? 24.280  -5.284  -7.802  1.00 21.03 ? 54   LEU C CB  1 
ATOM   9117  C  CG  . LEU C  1 37  ? 23.281  -4.901  -6.708  1.00 21.06 ? 54   LEU C CG  1 
ATOM   9118  C  CD1 . LEU C  1 37  ? 23.701  -3.600  -6.040  1.00 21.17 ? 54   LEU C CD1 1 
ATOM   9119  C  CD2 . LEU C  1 37  ? 21.875  -4.802  -7.276  1.00 20.87 ? 54   LEU C CD2 1 
ATOM   9120  N  N   . PRO C  1 38  ? 24.656  -6.920  -10.603 1.00 23.65 ? 55   PRO C N   1 
ATOM   9121  C  CA  . PRO C  1 38  ? 25.448  -7.083  -11.821 1.00 23.88 ? 55   PRO C CA  1 
ATOM   9122  C  C   . PRO C  1 38  ? 26.493  -5.980  -11.971 1.00 24.78 ? 55   PRO C C   1 
ATOM   9123  O  O   . PRO C  1 38  ? 26.340  -4.901  -11.407 1.00 24.66 ? 55   PRO C O   1 
ATOM   9124  C  CB  . PRO C  1 38  ? 24.419  -7.084  -12.956 1.00 24.26 ? 55   PRO C CB  1 
ATOM   9125  C  CG  . PRO C  1 38  ? 23.182  -6.459  -12.368 1.00 24.90 ? 55   PRO C CG  1 
ATOM   9126  C  CD  . PRO C  1 38  ? 23.229  -6.696  -10.873 1.00 23.81 ? 55   PRO C CD  1 
ATOM   9127  N  N   . PRO C  1 39  ? 27.586  -6.214  -12.733 1.00 26.30 ? 56   PRO C N   1 
ATOM   9128  C  CA  . PRO C  1 39  ? 28.753  -5.330  -12.723 1.00 28.75 ? 56   PRO C CA  1 
ATOM   9129  C  C   . PRO C  1 39  ? 28.607  -4.081  -13.592 1.00 31.35 ? 56   PRO C C   1 
ATOM   9130  O  O   . PRO C  1 39  ? 29.475  -3.794  -14.415 1.00 37.71 ? 56   PRO C O   1 
ATOM   9131  C  CB  . PRO C  1 39  ? 29.887  -6.256  -13.234 1.00 28.93 ? 56   PRO C CB  1 
ATOM   9132  C  CG  . PRO C  1 39  ? 29.242  -7.610  -13.457 1.00 27.91 ? 56   PRO C CG  1 
ATOM   9133  C  CD  . PRO C  1 39  ? 27.767  -7.355  -13.640 1.00 27.47 ? 56   PRO C CD  1 
ATOM   9134  N  N   . LYS C  1 40  ? 27.499  -3.363  -13.390 1.00 30.32 ? 57   LYS C N   1 
ATOM   9135  C  CA  . LYS C  1 40  ? 27.130  -2.166  -14.132 1.00 29.35 ? 57   LYS C CA  1 
ATOM   9136  C  C   . LYS C  1 40  ? 26.566  -1.175  -13.118 1.00 28.95 ? 57   LYS C C   1 
ATOM   9137  O  O   . LYS C  1 40  ? 25.687  -1.538  -12.341 1.00 27.22 ? 57   LYS C O   1 
ATOM   9138  C  CB  . LYS C  1 40  ? 26.087  -2.553  -15.187 1.00 31.02 ? 57   LYS C CB  1 
ATOM   9139  C  CG  . LYS C  1 40  ? 25.220  -1.443  -15.806 1.00 32.38 ? 57   LYS C CG  1 
ATOM   9140  C  CD  . LYS C  1 40  ? 25.853  -0.696  -16.974 1.00 32.56 ? 57   LYS C CD  1 
ATOM   9141  C  CE  . LYS C  1 40  ? 24.995  0.407   -17.538 1.00 31.81 ? 57   LYS C CE  1 
ATOM   9142  N  NZ  . LYS C  1 40  ? 23.699  -0.049  -18.048 1.00 31.40 ? 57   LYS C NZ  1 
ATOM   9143  N  N   . ILE C  1 41  ? 27.115  0.046   -13.100 1.00 28.35 ? 58   ILE C N   1 
ATOM   9144  C  CA  . ILE C  1 41  ? 26.645  1.109   -12.228 1.00 26.97 ? 58   ILE C CA  1 
ATOM   9145  C  C   . ILE C  1 41  ? 25.720  1.996   -13.052 1.00 26.76 ? 58   ILE C C   1 
ATOM   9146  O  O   . ILE C  1 41  ? 26.153  2.560   -14.052 1.00 24.95 ? 58   ILE C O   1 
ATOM   9147  C  CB  . ILE C  1 41  ? 27.821  1.928   -11.662 1.00 28.22 ? 58   ILE C CB  1 
ATOM   9148  C  CG1 . ILE C  1 41  ? 28.955  1.046   -11.119 1.00 28.29 ? 58   ILE C CG1 1 
ATOM   9149  C  CG2 . ILE C  1 41  ? 27.329  2.938   -10.621 1.00 29.05 ? 58   ILE C CG2 1 
ATOM   9150  C  CD1 . ILE C  1 41  ? 28.527  0.074   -10.039 1.00 28.76 ? 58   ILE C CD1 1 
ATOM   9151  N  N   . GLU C  1 42  ? 24.463  2.136   -12.617 1.00 25.36 ? 59   GLU C N   1 
ATOM   9152  C  CA  . GLU C  1 42  ? 23.503  2.939   -13.355 1.00 26.01 ? 59   GLU C CA  1 
ATOM   9153  C  C   . GLU C  1 42  ? 23.139  4.192   -12.566 1.00 25.65 ? 59   GLU C C   1 
ATOM   9154  O  O   . GLU C  1 42  ? 23.484  4.328   -11.394 1.00 26.34 ? 59   GLU C O   1 
ATOM   9155  C  CB  . GLU C  1 42  ? 22.266  2.111   -13.695 1.00 26.81 ? 59   GLU C CB  1 
ATOM   9156  C  CG  . GLU C  1 42  ? 22.571  1.014   -14.709 1.00 28.67 ? 59   GLU C CG  1 
ATOM   9157  C  CD  . GLU C  1 42  ? 21.373  0.257   -15.247 1.00 29.32 ? 59   GLU C CD  1 
ATOM   9158  O  OE1 . GLU C  1 42  ? 20.271  0.343   -14.651 1.00 29.23 ? 59   GLU C OE1 1 
ATOM   9159  O  OE2 . GLU C  1 42  ? 21.558  -0.400  -16.301 1.00 28.60 ? 59   GLU C OE2 1 
ATOM   9160  N  N   . THR C  1 43  ? 22.473  5.115   -13.261 1.00 25.02 ? 60   THR C N   1 
ATOM   9161  C  CA  . THR C  1 43  ? 21.854  6.275   -12.649 1.00 24.14 ? 60   THR C CA  1 
ATOM   9162  C  C   . THR C  1 43  ? 20.353  6.019   -12.597 1.00 22.36 ? 60   THR C C   1 
ATOM   9163  O  O   . THR C  1 43  ? 19.844  5.158   -13.309 1.00 21.63 ? 60   THR C O   1 
ATOM   9164  C  CB  . THR C  1 43  ? 22.181  7.528   -13.459 1.00 25.37 ? 60   THR C CB  1 
ATOM   9165  O  OG1 . THR C  1 43  ? 21.607  7.285   -14.739 1.00 25.18 ? 60   THR C OG1 1 
ATOM   9166  C  CG2 . THR C  1 43  ? 23.675  7.781   -13.563 1.00 27.48 ? 60   THR C CG2 1 
ATOM   9167  N  N   . GLN C  1 44  ? 19.649  6.808   -11.786 1.00 22.28 ? 61   GLN C N   1 
ATOM   9168  C  CA  . GLN C  1 44  ? 18.201  6.712   -11.710 1.00 22.67 ? 61   GLN C CA  1 
ATOM   9169  C  C   . GLN C  1 44  ? 17.585  6.945   -13.093 1.00 23.38 ? 61   GLN C C   1 
ATOM   9170  O  O   . GLN C  1 44  ? 16.577  6.331   -13.427 1.00 22.63 ? 61   GLN C O   1 
ATOM   9171  C  CB  . GLN C  1 44  ? 17.680  7.694   -10.664 1.00 22.21 ? 61   GLN C CB  1 
ATOM   9172  C  CG  . GLN C  1 44  ? 16.274  7.372   -10.173 1.00 22.26 ? 61   GLN C CG  1 
ATOM   9173  C  CD  . GLN C  1 44  ? 15.747  8.433   -9.238  1.00 22.49 ? 61   GLN C CD  1 
ATOM   9174  O  OE1 . GLN C  1 44  ? 15.389  9.537   -9.664  1.00 24.82 ? 61   GLN C OE1 1 
ATOM   9175  N  NE2 . GLN C  1 44  ? 15.683  8.111   -7.958  1.00 22.16 ? 61   GLN C NE2 1 
ATOM   9176  N  N   . ASP C  1 45  ? 18.209  7.818   -13.897 1.00 25.23 ? 62   ASP C N   1 
ATOM   9177  C  CA  . ASP C  1 45  ? 17.738  8.141   -15.239 1.00 26.63 ? 62   ASP C CA  1 
ATOM   9178  C  C   . ASP C  1 45  ? 17.605  6.881   -16.093 1.00 24.99 ? 62   ASP C C   1 
ATOM   9179  O  O   . ASP C  1 45  ? 16.576  6.669   -16.728 1.00 25.30 ? 62   ASP C O   1 
ATOM   9180  C  CB  . ASP C  1 45  ? 18.654  9.148   -15.919 1.00 29.44 ? 62   ASP C CB  1 
ATOM   9181  C  CG  . ASP C  1 45  ? 18.542  10.594  -15.451 1.00 32.98 ? 62   ASP C CG  1 
ATOM   9182  O  OD1 . ASP C  1 45  ? 17.587  10.911  -14.705 1.00 33.93 ? 62   ASP C OD1 1 
ATOM   9183  O  OD2 . ASP C  1 45  ? 19.416  11.401  -15.841 1.00 35.19 ? 62   ASP C OD2 1 
ATOM   9184  N  N   . ILE C  1 46  ? 18.650  6.047   -16.102 1.00 24.64 ? 63   ILE C N   1 
ATOM   9185  C  CA  . ILE C  1 46  ? 18.661  4.838   -16.907 1.00 24.45 ? 63   ILE C CA  1 
ATOM   9186  C  C   . ILE C  1 46  ? 17.623  3.843   -16.391 1.00 23.13 ? 63   ILE C C   1 
ATOM   9187  O  O   . ILE C  1 46  ? 16.943  3.200   -17.189 1.00 23.19 ? 63   ILE C O   1 
ATOM   9188  C  CB  . ILE C  1 46  ? 20.069  4.217   -16.937 1.00 26.00 ? 63   ILE C CB  1 
ATOM   9189  C  CG1 . ILE C  1 46  ? 21.047  5.087   -17.728 1.00 27.84 ? 63   ILE C CG1 1 
ATOM   9190  C  CG2 . ILE C  1 46  ? 20.027  2.786   -17.473 1.00 26.61 ? 63   ILE C CG2 1 
ATOM   9191  C  CD1 . ILE C  1 46  ? 20.741  5.182   -19.214 1.00 28.75 ? 63   ILE C CD1 1 
ATOM   9192  N  N   . GLN C  1 47  ? 17.541  3.679   -15.066 1.00 22.06 ? 64   GLN C N   1 
ATOM   9193  C  CA  . GLN C  1 47  ? 16.571  2.775   -14.466 1.00 21.98 ? 64   GLN C CA  1 
ATOM   9194  C  C   . GLN C  1 47  ? 15.157  3.191   -14.873 1.00 22.58 ? 64   GLN C C   1 
ATOM   9195  O  O   . GLN C  1 47  ? 14.316  2.343   -15.172 1.00 23.11 ? 64   GLN C O   1 
ATOM   9196  C  CB  . GLN C  1 47  ? 16.675  2.775   -12.939 1.00 22.40 ? 64   GLN C CB  1 
ATOM   9197  C  CG  . GLN C  1 47  ? 17.974  2.199   -12.382 1.00 21.33 ? 64   GLN C CG  1 
ATOM   9198  C  CD  . GLN C  1 47  ? 18.108  2.423   -10.891 1.00 21.82 ? 64   GLN C CD  1 
ATOM   9199  O  OE1 . GLN C  1 47  ? 18.100  3.566   -10.420 1.00 22.63 ? 64   GLN C OE1 1 
ATOM   9200  N  NE2 . GLN C  1 47  ? 18.206  1.345   -10.125 1.00 21.55 ? 64   GLN C NE2 1 
ATOM   9201  N  N   . ALA C  1 48  ? 14.900  4.505   -14.879 1.00 23.53 ? 65   ALA C N   1 
ATOM   9202  C  CA  . ALA C  1 48  ? 13.583  5.026   -15.224 1.00 25.12 ? 65   ALA C CA  1 
ATOM   9203  C  C   . ALA C  1 48  ? 13.256  4.733   -16.690 1.00 24.50 ? 65   ALA C C   1 
ATOM   9204  O  O   . ALA C  1 48  ? 12.150  4.303   -16.999 1.00 24.33 ? 65   ALA C O   1 
ATOM   9205  C  CB  . ALA C  1 48  ? 13.506  6.503   -14.914 1.00 25.49 ? 65   ALA C CB  1 
ATOM   9206  N  N   . LEU C  1 49  ? 14.232  4.927   -17.585 1.00 25.17 ? 66   LEU C N   1 
ATOM   9207  C  CA  . LEU C  1 49  ? 14.024  4.719   -19.013 1.00 24.38 ? 66   LEU C CA  1 
ATOM   9208  C  C   . LEU C  1 49  ? 13.751  3.246   -19.313 1.00 23.14 ? 66   LEU C C   1 
ATOM   9209  O  O   . LEU C  1 49  ? 12.916  2.932   -20.159 1.00 22.76 ? 66   LEU C O   1 
ATOM   9210  C  CB  . LEU C  1 49  ? 15.221  5.232   -19.813 1.00 25.55 ? 66   LEU C CB  1 
ATOM   9211  C  CG  . LEU C  1 49  ? 15.365  6.752   -19.918 1.00 27.90 ? 66   LEU C CG  1 
ATOM   9212  C  CD1 . LEU C  1 49  ? 16.689  7.100   -20.582 1.00 29.07 ? 66   LEU C CD1 1 
ATOM   9213  C  CD2 . LEU C  1 49  ? 14.207  7.382   -20.680 1.00 29.11 ? 66   LEU C CD2 1 
ATOM   9214  N  N   . ARG C  1 50  ? 14.458  2.342   -18.623 1.00 22.42 ? 67   ARG C N   1 
ATOM   9215  C  CA  . ARG C  1 50  ? 14.207  0.915   -18.764 1.00 23.08 ? 67   ARG C CA  1 
ATOM   9216  C  C   . ARG C  1 50  ? 12.749  0.636   -18.407 1.00 23.87 ? 67   ARG C C   1 
ATOM   9217  O  O   . ARG C  1 50  ? 12.049  -0.075  -19.130 1.00 23.92 ? 67   ARG C O   1 
ATOM   9218  C  CB  . ARG C  1 50  ? 15.156  0.084   -17.885 1.00 22.95 ? 67   ARG C CB  1 
ATOM   9219  C  CG  . ARG C  1 50  ? 14.869  -1.410  -17.905 1.00 23.36 ? 67   ARG C CG  1 
ATOM   9220  C  CD  . ARG C  1 50  ? 15.729  -2.219  -16.951 1.00 23.67 ? 67   ARG C CD  1 
ATOM   9221  N  NE  . ARG C  1 50  ? 17.140  -2.185  -17.351 1.00 24.89 ? 67   ARG C NE  1 
ATOM   9222  C  CZ  . ARG C  1 50  ? 18.135  -1.538  -16.748 1.00 25.68 ? 67   ARG C CZ  1 
ATOM   9223  N  NH1 . ARG C  1 50  ? 17.938  -0.858  -15.631 1.00 26.37 ? 67   ARG C NH1 1 
ATOM   9224  N  NH2 . ARG C  1 50  ? 19.344  -1.568  -17.280 1.00 25.83 ? 67   ARG C NH2 1 
ATOM   9225  N  N   . PHE C  1 51  ? 12.285  1.226   -17.301 1.00 25.30 ? 68   PHE C N   1 
ATOM   9226  C  CA  . PHE C  1 51  ? 10.921  0.999   -16.845 1.00 26.82 ? 68   PHE C CA  1 
ATOM   9227  C  C   . PHE C  1 51  ? 9.915   1.451   -17.906 1.00 27.09 ? 68   PHE C C   1 
ATOM   9228  O  O   . PHE C  1 51  ? 8.993   0.704   -18.226 1.00 28.34 ? 68   PHE C O   1 
ATOM   9229  C  CB  . PHE C  1 51  ? 10.601  1.689   -15.516 1.00 27.74 ? 68   PHE C CB  1 
ATOM   9230  C  CG  . PHE C  1 51  ? 9.100   1.780   -15.284 1.00 29.23 ? 68   PHE C CG  1 
ATOM   9231  C  CD1 . PHE C  1 51  ? 8.403   0.728   -14.709 1.00 31.13 ? 68   PHE C CD1 1 
ATOM   9232  C  CD2 . PHE C  1 51  ? 8.388   2.899   -15.695 1.00 30.11 ? 68   PHE C CD2 1 
ATOM   9233  C  CE1 . PHE C  1 51  ? 7.031   0.806   -14.525 1.00 31.80 ? 68   PHE C CE1 1 
ATOM   9234  C  CE2 . PHE C  1 51  ? 7.016   2.967   -15.520 1.00 32.14 ? 68   PHE C CE2 1 
ATOM   9235  C  CZ  . PHE C  1 51  ? 6.345   1.923   -14.932 1.00 32.15 ? 68   PHE C CZ  1 
ATOM   9236  N  N   . HIS C  1 52  ? 10.074  2.679   -18.418 1.00 27.51 ? 69   HIS C N   1 
ATOM   9237  C  CA  . HIS C  1 52  ? 9.110   3.266   -19.340 1.00 29.42 ? 69   HIS C CA  1 
ATOM   9238  C  C   . HIS C  1 52  ? 9.030   2.433   -20.620 1.00 29.64 ? 69   HIS C C   1 
ATOM   9239  O  O   . HIS C  1 52  ? 7.955   2.268   -21.189 1.00 30.14 ? 69   HIS C O   1 
ATOM   9240  C  CB  . HIS C  1 52  ? 9.466   4.726   -19.654 1.00 30.21 ? 69   HIS C CB  1 
ATOM   9241  C  CG  . HIS C  1 52  ? 9.333   5.663   -18.497 1.00 31.21 ? 69   HIS C CG  1 
ATOM   9242  N  ND1 . HIS C  1 52  ? 8.189   5.780   -17.734 1.00 32.78 ? 69   HIS C ND1 1 
ATOM   9243  C  CD2 . HIS C  1 52  ? 10.199  6.553   -17.999 1.00 31.04 ? 69   HIS C CD2 1 
ATOM   9244  C  CE1 . HIS C  1 52  ? 8.383   6.700   -16.797 1.00 32.08 ? 69   HIS C CE1 1 
ATOM   9245  N  NE2 . HIS C  1 52  ? 9.598   7.182   -16.941 1.00 30.64 ? 69   HIS C NE2 1 
ATOM   9246  N  N   . ARG C  1 53  ? 10.180  1.909   -21.057 1.00 30.02 ? 70   ARG C N   1 
ATOM   9247  C  CA  . ARG C  1 53  ? 10.260  1.057   -22.234 1.00 32.46 ? 70   ARG C CA  1 
ATOM   9248  C  C   . ARG C  1 53  ? 9.469   -0.229  -22.003 1.00 31.92 ? 70   ARG C C   1 
ATOM   9249  O  O   . ARG C  1 53  ? 8.684   -0.641  -22.857 1.00 32.13 ? 70   ARG C O   1 
ATOM   9250  C  CB  . ARG C  1 53  ? 11.726  0.733   -22.541 1.00 35.05 ? 70   ARG C CB  1 
ATOM   9251  C  CG  . ARG C  1 53  ? 11.936  -0.040  -23.835 1.00 38.97 ? 70   ARG C CG  1 
ATOM   9252  C  CD  . ARG C  1 53  ? 13.250  -0.794  -23.817 1.00 42.08 ? 70   ARG C CD  1 
ATOM   9253  N  NE  . ARG C  1 53  ? 13.251  -1.868  -22.816 1.00 44.41 ? 70   ARG C NE  1 
ATOM   9254  C  CZ  . ARG C  1 53  ? 14.310  -2.606  -22.499 1.00 45.57 ? 70   ARG C CZ  1 
ATOM   9255  N  NH1 . ARG C  1 53  ? 15.466  -2.407  -23.117 1.00 44.61 ? 70   ARG C NH1 1 
ATOM   9256  N  NH2 . ARG C  1 53  ? 14.207  -3.537  -21.562 1.00 44.42 ? 70   ARG C NH2 1 
ATOM   9257  N  N   . ASN C  1 54  ? 9.683   -0.855  -20.841 1.00 30.71 ? 71   ASN C N   1 
ATOM   9258  C  CA  . ASN C  1 54  ? 9.014   -2.098  -20.493 1.00 31.80 ? 71   ASN C CA  1 
ATOM   9259  C  C   . ASN C  1 54  ? 7.501   -1.895  -20.396 1.00 34.24 ? 71   ASN C C   1 
ATOM   9260  O  O   . ASN C  1 54  ? 6.744   -2.757  -20.840 1.00 34.54 ? 71   ASN C O   1 
ATOM   9261  C  CB  . ASN C  1 54  ? 9.564   -2.688  -19.200 1.00 32.25 ? 71   ASN C CB  1 
ATOM   9262  C  CG  . ASN C  1 54  ? 10.963  -3.236  -19.360 1.00 33.93 ? 71   ASN C CG  1 
ATOM   9263  O  OD1 . ASN C  1 54  ? 11.454  -3.385  -20.485 1.00 35.32 ? 71   ASN C OD1 1 
ATOM   9264  N  ND2 . ASN C  1 54  ? 11.609  -3.565  -18.253 1.00 33.34 ? 71   ASN C ND2 1 
ATOM   9265  N  N   . LEU C  1 55  ? 7.062   -0.766  -19.821 1.00 34.31 ? 72   LEU C N   1 
ATOM   9266  C  CA  . LEU C  1 55  ? 5.645   -0.544  -19.563 1.00 37.51 ? 72   LEU C CA  1 
ATOM   9267  C  C   . LEU C  1 55  ? 4.872   -0.508  -20.883 1.00 40.26 ? 72   LEU C C   1 
ATOM   9268  O  O   . LEU C  1 55  ? 3.730   -0.960  -20.942 1.00 40.42 ? 72   LEU C O   1 
ATOM   9269  C  CB  . LEU C  1 55  ? 5.410   0.735   -18.758 1.00 37.18 ? 72   LEU C CB  1 
ATOM   9270  C  CG  . LEU C  1 55  ? 3.997   0.907   -18.185 1.00 38.46 ? 72   LEU C CG  1 
ATOM   9271  C  CD1 . LEU C  1 55  ? 3.753   -0.078  -17.056 1.00 38.93 ? 72   LEU C CD1 1 
ATOM   9272  C  CD2 . LEU C  1 55  ? 3.722   2.322   -17.709 1.00 38.14 ? 72   LEU C CD2 1 
ATOM   9273  N  N   . LYS C  1 56  ? 5.513   0.024   -21.933 1.00 44.27 ? 73   LYS C N   1 
ATOM   9274  C  CA  . LYS C  1 56  ? 4.908   0.183   -23.248 1.00 48.41 ? 73   LYS C CA  1 
ATOM   9275  C  C   . LYS C  1 56  ? 4.616   -1.171  -23.897 1.00 49.73 ? 73   LYS C C   1 
ATOM   9276  O  O   . LYS C  1 56  ? 3.786   -1.246  -24.801 1.00 51.46 ? 73   LYS C O   1 
ATOM   9277  C  CB  . LYS C  1 56  ? 5.839   1.038   -24.116 1.00 51.87 ? 73   LYS C CB  1 
ATOM   9278  C  CG  . LYS C  1 56  ? 5.276   1.497   -25.454 1.00 56.44 ? 73   LYS C CG  1 
ATOM   9279  C  CD  . LYS C  1 56  ? 6.049   2.664   -26.060 1.00 60.27 ? 73   LYS C CD  1 
ATOM   9280  C  CE  . LYS C  1 56  ? 5.557   3.095   -27.415 1.00 62.53 ? 73   LYS C CE  1 
ATOM   9281  N  NZ  . LYS C  1 56  ? 5.963   2.180   -28.487 1.00 62.31 ? 73   LYS C NZ  1 
ATOM   9282  N  N   . LYS C  1 57  ? 5.286   -2.235  -23.435 1.00 49.17 ? 74   LYS C N   1 
ATOM   9283  C  CA  . LYS C  1 57  ? 5.118   -3.568  -23.995 1.00 51.94 ? 74   LYS C CA  1 
ATOM   9284  C  C   . LYS C  1 57  ? 3.943   -4.309  -23.357 1.00 51.93 ? 74   LYS C C   1 
ATOM   9285  O  O   . LYS C  1 57  ? 3.595   -5.401  -23.803 1.00 50.64 ? 74   LYS C O   1 
ATOM   9286  C  CB  . LYS C  1 57  ? 6.382   -4.414  -23.801 1.00 53.31 ? 74   LYS C CB  1 
ATOM   9287  C  CG  . LYS C  1 57  ? 7.606   -3.959  -24.583 1.00 54.83 ? 74   LYS C CG  1 
ATOM   9288  C  CD  . LYS C  1 57  ? 7.369   -3.765  -26.077 1.00 56.02 ? 74   LYS C CD  1 
ATOM   9289  C  CE  . LYS C  1 57  ? 8.644   -3.725  -26.865 1.00 56.87 ? 74   LYS C CE  1 
ATOM   9290  N  NZ  . LYS C  1 57  ? 9.593   -2.739  -26.342 1.00 56.84 ? 74   LYS C NZ  1 
ATOM   9291  N  N   . MET C  1 58  ? 3.345   -3.740  -22.305 1.00 50.50 ? 75   MET C N   1 
ATOM   9292  C  CA  . MET C  1 58  ? 2.219   -4.381  -21.646 1.00 50.73 ? 75   MET C CA  1 
ATOM   9293  C  C   . MET C  1 58  ? 0.917   -3.860  -22.245 1.00 49.34 ? 75   MET C C   1 
ATOM   9294  O  O   . MET C  1 58  ? 0.861   -2.745  -22.762 1.00 53.82 ? 75   MET C O   1 
ATOM   9295  C  CB  . MET C  1 58  ? 2.280   -4.164  -20.132 1.00 51.63 ? 75   MET C CB  1 
ATOM   9296  C  CG  . MET C  1 58  ? 3.385   -4.969  -19.490 1.00 53.74 ? 75   MET C CG  1 
ATOM   9297  S  SD  . MET C  1 58  ? 3.938   -4.277  -17.923 1.00 56.06 ? 75   MET C SD  1 
ATOM   9298  C  CE  . MET C  1 58  ? 5.490   -5.176  -17.788 1.00 56.55 ? 75   MET C CE  1 
ATOM   9299  N  N   . THR C  1 59  ? -0.121  -4.699  -22.187 1.00 45.11 ? 76   THR C N   1 
ATOM   9300  C  CA  . THR C  1 59  ? -1.353  -4.441  -22.913 1.00 42.93 ? 76   THR C CA  1 
ATOM   9301  C  C   . THR C  1 59  ? -2.332  -3.693  -22.010 1.00 40.02 ? 76   THR C C   1 
ATOM   9302  O  O   . THR C  1 59  ? -2.562  -2.502  -22.201 1.00 40.65 ? 76   THR C O   1 
ATOM   9303  C  CB  . THR C  1 59  ? -1.907  -5.768  -23.434 1.00 41.55 ? 76   THR C CB  1 
ATOM   9304  O  OG1 . THR C  1 59  ? -0.904  -6.247  -24.325 1.00 40.57 ? 76   THR C OG1 1 
ATOM   9305  C  CG2 . THR C  1 59  ? -3.219  -5.615  -24.181 1.00 43.16 ? 76   THR C CG2 1 
ATOM   9306  N  N   . SER C  1 60  ? -2.890  -4.393  -21.019 1.00 40.35 ? 77   SER C N   1 
ATOM   9307  C  CA  . SER C  1 60  ? -4.029  -3.884  -20.270 1.00 41.83 ? 77   SER C CA  1 
ATOM   9308  C  C   . SER C  1 60  ? -3.562  -2.947  -19.158 1.00 41.27 ? 77   SER C C   1 
ATOM   9309  O  O   . SER C  1 60  ? -2.488  -3.144  -18.592 1.00 41.47 ? 77   SER C O   1 
ATOM   9310  C  CB  . SER C  1 60  ? -4.855  -5.008  -19.704 1.00 42.96 ? 77   SER C CB  1 
ATOM   9311  O  OG  . SER C  1 60  ? -4.120  -5.754  -18.743 1.00 43.02 ? 77   SER C OG  1 
ATOM   9312  N  N   . PRO C  1 61  ? -4.363  -1.916  -18.798 1.00 40.97 ? 78   PRO C N   1 
ATOM   9313  C  CA  . PRO C  1 61  ? -4.069  -1.086  -17.626 1.00 41.47 ? 78   PRO C CA  1 
ATOM   9314  C  C   . PRO C  1 61  ? -3.770  -1.881  -16.354 1.00 40.44 ? 78   PRO C C   1 
ATOM   9315  O  O   . PRO C  1 61  ? -2.988  -1.439  -15.519 1.00 38.97 ? 78   PRO C O   1 
ATOM   9316  C  CB  . PRO C  1 61  ? -5.347  -0.236  -17.496 1.00 40.99 ? 78   PRO C CB  1 
ATOM   9317  C  CG  . PRO C  1 61  ? -5.856  -0.117  -18.914 1.00 40.93 ? 78   PRO C CG  1 
ATOM   9318  C  CD  . PRO C  1 61  ? -5.572  -1.477  -19.517 1.00 40.95 ? 78   PRO C CD  1 
ATOM   9319  N  N   . LEU C  1 62  ? -4.392  -3.059  -16.221 1.00 41.39 ? 79   LEU C N   1 
ATOM   9320  C  CA  . LEU C  1 62  ? -4.232  -3.894  -15.042 1.00 42.34 ? 79   LEU C CA  1 
ATOM   9321  C  C   . LEU C  1 62  ? -2.827  -4.494  -14.979 1.00 41.79 ? 79   LEU C C   1 
ATOM   9322  O  O   . LEU C  1 62  ? -2.242  -4.562  -13.897 1.00 37.02 ? 79   LEU C O   1 
ATOM   9323  C  CB  . LEU C  1 62  ? -5.313  -4.972  -15.027 1.00 46.04 ? 79   LEU C CB  1 
ATOM   9324  C  CG  . LEU C  1 62  ? -6.717  -4.499  -14.634 1.00 50.07 ? 79   LEU C CG  1 
ATOM   9325  C  CD1 . LEU C  1 62  ? -7.762  -5.570  -14.891 1.00 51.93 ? 79   LEU C CD1 1 
ATOM   9326  C  CD2 . LEU C  1 62  ? -6.732  -4.084  -13.170 1.00 52.80 ? 79   LEU C CD2 1 
ATOM   9327  N  N   . GLU C  1 63  ? -2.302  -4.938  -16.130 1.00 40.19 ? 80   GLU C N   1 
ATOM   9328  C  CA  . GLU C  1 63  ? -0.937  -5.442  -16.220 1.00 40.31 ? 80   GLU C CA  1 
ATOM   9329  C  C   . GLU C  1 63  ? 0.057   -4.339  -15.853 1.00 34.31 ? 80   GLU C C   1 
ATOM   9330  O  O   . GLU C  1 63  ? 1.050   -4.593  -15.174 1.00 32.07 ? 80   GLU C O   1 
ATOM   9331  C  CB  . GLU C  1 63  ? -0.614  -5.943  -17.630 1.00 45.34 ? 80   GLU C CB  1 
ATOM   9332  C  CG  . GLU C  1 63  ? -1.314  -7.244  -18.013 1.00 51.52 ? 80   GLU C CG  1 
ATOM   9333  C  CD  . GLU C  1 63  ? -1.179  -7.591  -19.489 1.00 58.39 ? 80   GLU C CD  1 
ATOM   9334  O  OE1 . GLU C  1 63  ? -0.047  -7.509  -20.017 1.00 62.71 ? 80   GLU C OE1 1 
ATOM   9335  O  OE2 . GLU C  1 63  ? -2.201  -7.945  -20.116 1.00 61.69 ? 80   GLU C OE2 1 
ATOM   9336  N  N   . LYS C  1 64  ? -0.211  -3.121  -16.334 1.00 32.10 ? 81   LYS C N   1 
ATOM   9337  C  CA  . LYS C  1 64  ? 0.607   -1.959  -16.029 1.00 31.78 ? 81   LYS C CA  1 
ATOM   9338  C  C   . LYS C  1 64  ? 0.572   -1.680  -14.526 1.00 31.10 ? 81   LYS C C   1 
ATOM   9339  O  O   . LYS C  1 64  ? 1.615   -1.463  -13.916 1.00 30.52 ? 81   LYS C O   1 
ATOM   9340  C  CB  . LYS C  1 64  ? 0.121   -0.733  -16.812 1.00 32.51 ? 81   LYS C CB  1 
ATOM   9341  C  CG  . LYS C  1 64  ? 0.241   -0.829  -18.327 1.00 34.81 ? 81   LYS C CG  1 
ATOM   9342  C  CD  . LYS C  1 64  ? -0.243  0.426   -19.046 1.00 35.67 ? 81   LYS C CD  1 
ATOM   9343  C  CE  . LYS C  1 64  ? -0.412  0.243   -20.522 1.00 36.87 ? 81   LYS C CE  1 
ATOM   9344  N  NZ  . LYS C  1 64  ? 0.841   -0.160  -21.163 1.00 37.72 ? 81   LYS C NZ  1 
ATOM   9345  N  N   . TYR C  1 65  ? -0.632  -1.705  -13.940 1.00 29.77 ? 82   TYR C N   1 
ATOM   9346  C  CA  . TYR C  1 65  ? -0.821  -1.442  -12.521 1.00 30.31 ? 82   TYR C CA  1 
ATOM   9347  C  C   . TYR C  1 65  ? 0.021   -2.397  -11.678 1.00 30.58 ? 82   TYR C C   1 
ATOM   9348  O  O   . TYR C  1 65  ? 0.652   -1.974  -10.709 1.00 30.45 ? 82   TYR C O   1 
ATOM   9349  C  CB  . TYR C  1 65  ? -2.303  -1.558  -12.146 1.00 30.71 ? 82   TYR C CB  1 
ATOM   9350  C  CG  . TYR C  1 65  ? -2.563  -1.503  -10.646 1.00 28.72 ? 82   TYR C CG  1 
ATOM   9351  C  CD1 . TYR C  1 65  ? -2.548  -2.657  -9.872  1.00 28.21 ? 82   TYR C CD1 1 
ATOM   9352  C  CD2 . TYR C  1 65  ? -2.811  -0.294  -10.007 1.00 28.44 ? 82   TYR C CD2 1 
ATOM   9353  C  CE1 . TYR C  1 65  ? -2.767  -2.609  -8.502  1.00 28.97 ? 82   TYR C CE1 1 
ATOM   9354  C  CE2 . TYR C  1 65  ? -3.038  -0.232  -8.640  1.00 28.06 ? 82   TYR C CE2 1 
ATOM   9355  C  CZ  . TYR C  1 65  ? -3.021  -1.394  -7.888  1.00 28.35 ? 82   TYR C CZ  1 
ATOM   9356  O  OH  . TYR C  1 65  ? -3.239  -1.336  -6.542  1.00 29.05 ? 82   TYR C OH  1 
ATOM   9357  N  N   . ILE C  1 66  ? 0.012   -3.685  -12.043 1.00 30.70 ? 83   ILE C N   1 
ATOM   9358  C  CA  . ILE C  1 66  ? 0.709   -4.717  -11.291 1.00 32.26 ? 83   ILE C CA  1 
ATOM   9359  C  C   . ILE C  1 66  ? 2.215   -4.485  -11.379 1.00 32.17 ? 83   ILE C C   1 
ATOM   9360  O  O   . ILE C  1 66  ? 2.936   -4.698  -10.404 1.00 31.50 ? 83   ILE C O   1 
ATOM   9361  C  CB  . ILE C  1 66  ? 0.314   -6.121  -11.794 1.00 34.14 ? 83   ILE C CB  1 
ATOM   9362  C  CG1 . ILE C  1 66  ? -1.146  -6.442  -11.470 1.00 36.09 ? 83   ILE C CG1 1 
ATOM   9363  C  CG2 . ILE C  1 66  ? 1.249   -7.202  -11.251 1.00 35.00 ? 83   ILE C CG2 1 
ATOM   9364  C  CD1 . ILE C  1 66  ? -1.475  -6.472  -9.986  1.00 37.42 ? 83   ILE C CD1 1 
ATOM   9365  N  N   . TYR C  1 67  ? 2.676   -4.039  -12.550 1.00 31.81 ? 84   TYR C N   1 
ATOM   9366  C  CA  . TYR C  1 67  ? 4.096   -3.824  -12.778 1.00 31.63 ? 84   TYR C CA  1 
ATOM   9367  C  C   . TYR C  1 67  ? 4.601   -2.635  -11.957 1.00 28.11 ? 84   TYR C C   1 
ATOM   9368  O  O   . TYR C  1 67  ? 5.611   -2.753  -11.268 1.00 27.16 ? 84   TYR C O   1 
ATOM   9369  C  CB  . TYR C  1 67  ? 4.366   -3.609  -14.269 1.00 34.25 ? 84   TYR C CB  1 
ATOM   9370  C  CG  . TYR C  1 67  ? 5.843   -3.574  -14.638 1.00 38.49 ? 84   TYR C CG  1 
ATOM   9371  C  CD1 . TYR C  1 67  ? 6.717   -4.553  -14.182 1.00 40.63 ? 84   TYR C CD1 1 
ATOM   9372  C  CD2 . TYR C  1 67  ? 6.364   -2.558  -15.433 1.00 41.41 ? 84   TYR C CD2 1 
ATOM   9373  C  CE1 . TYR C  1 67  ? 8.060   -4.534  -14.517 1.00 44.48 ? 84   TYR C CE1 1 
ATOM   9374  C  CE2 . TYR C  1 67  ? 7.708   -2.523  -15.767 1.00 43.86 ? 84   TYR C CE2 1 
ATOM   9375  C  CZ  . TYR C  1 67  ? 8.559   -3.513  -15.306 1.00 46.59 ? 84   TYR C CZ  1 
ATOM   9376  O  OH  . TYR C  1 67  ? 9.886   -3.503  -15.625 1.00 50.57 ? 84   TYR C OH  1 
ATOM   9377  N  N   A ILE C  1 68  ? 3.898   -1.498  -12.028 0.50 26.59 ? 85   ILE C N   1 
ATOM   9378  N  N   B ILE C  1 68  ? 3.899   -1.498  -12.058 0.50 27.11 ? 85   ILE C N   1 
ATOM   9379  C  CA  A ILE C  1 68  ? 4.390   -0.274  -11.412 0.50 26.06 ? 85   ILE C CA  1 
ATOM   9380  C  CA  B ILE C  1 68  ? 4.320   -0.260  -11.417 0.50 26.96 ? 85   ILE C CA  1 
ATOM   9381  C  C   A ILE C  1 68  ? 4.296   -0.376  -9.886  0.50 25.11 ? 85   ILE C C   1 
ATOM   9382  C  C   B ILE C  1 68  ? 4.314   -0.433  -9.898  0.50 25.52 ? 85   ILE C C   1 
ATOM   9383  O  O   A ILE C  1 68  ? 5.218   0.047   -9.192  0.50 23.92 ? 85   ILE C O   1 
ATOM   9384  O  O   B ILE C  1 68  ? 5.294   -0.109  -9.231  0.50 24.15 ? 85   ILE C O   1 
ATOM   9385  C  CB  A ILE C  1 68  ? 3.676   0.973   -11.969 0.50 26.47 ? 85   ILE C CB  1 
ATOM   9386  C  CB  B ILE C  1 68  ? 3.430   0.923   -11.843 0.50 28.25 ? 85   ILE C CB  1 
ATOM   9387  C  CG1 A ILE C  1 68  ? 4.510   2.238   -11.736 0.50 27.14 ? 85   ILE C CG1 1 
ATOM   9388  C  CG1 B ILE C  1 68  ? 3.280   1.003   -13.356 0.50 28.67 ? 85   ILE C CG1 1 
ATOM   9389  C  CG2 A ILE C  1 68  ? 2.260   1.113   -11.410 0.50 25.89 ? 85   ILE C CG2 1 
ATOM   9390  C  CG2 B ILE C  1 68  ? 3.962   2.234   -11.266 0.50 28.99 ? 85   ILE C CG2 1 
ATOM   9391  C  CD1 A ILE C  1 68  ? 3.817   3.527   -12.143 0.50 27.39 ? 85   ILE C CD1 1 
ATOM   9392  C  CD1 B ILE C  1 68  ? 2.367   2.117   -13.834 0.50 28.48 ? 85   ILE C CD1 1 
ATOM   9393  N  N   . MET C  1 69  ? 3.206   -0.949  -9.356  1.00 24.60 ? 86   MET C N   1 
ATOM   9394  C  CA  . MET C  1 69  ? 3.054   -1.072  -7.910  1.00 25.43 ? 86   MET C CA  1 
ATOM   9395  C  C   . MET C  1 69  ? 4.089   -2.043  -7.337  1.00 26.04 ? 86   MET C C   1 
ATOM   9396  O  O   . MET C  1 69  ? 4.522   -1.889  -6.197  1.00 25.85 ? 86   MET C O   1 
ATOM   9397  C  CB  . MET C  1 69  ? 1.636   -1.498  -7.511  1.00 25.47 ? 86   MET C CB  1 
ATOM   9398  C  CG  . MET C  1 69  ? 0.557   -0.486  -7.874  1.00 26.05 ? 86   MET C CG  1 
ATOM   9399  S  SD  . MET C  1 69  ? 0.917   1.223   -7.418  1.00 25.74 ? 86   MET C SD  1 
ATOM   9400  C  CE  . MET C  1 69  ? 0.982   1.034   -5.631  1.00 26.56 ? 86   MET C CE  1 
ATOM   9401  N  N   . GLY C  1 70  ? 4.507   -3.027  -8.139  1.00 27.17 ? 87   GLY C N   1 
ATOM   9402  C  CA  . GLY C  1 70  ? 5.581   -3.926  -7.750  1.00 27.50 ? 87   GLY C CA  1 
ATOM   9403  C  C   . GLY C  1 70  ? 6.856   -3.163  -7.393  1.00 28.55 ? 87   GLY C C   1 
ATOM   9404  O  O   . GLY C  1 70  ? 7.587   -3.570  -6.492  1.00 30.17 ? 87   GLY C O   1 
ATOM   9405  N  N   . ILE C  1 71  ? 7.103   -2.046  -8.090  1.00 27.76 ? 88   ILE C N   1 
ATOM   9406  C  CA  . ILE C  1 71  ? 8.319   -1.270  -7.902  1.00 27.83 ? 88   ILE C CA  1 
ATOM   9407  C  C   . ILE C  1 71  ? 8.284   -0.563  -6.548  1.00 26.94 ? 88   ILE C C   1 
ATOM   9408  O  O   . ILE C  1 71  ? 9.319   -0.447  -5.899  1.00 25.17 ? 88   ILE C O   1 
ATOM   9409  C  CB  . ILE C  1 71  ? 8.538   -0.299  -9.076  1.00 28.58 ? 88   ILE C CB  1 
ATOM   9410  C  CG1 . ILE C  1 71  ? 8.583   -1.060  -10.398 1.00 30.13 ? 88   ILE C CG1 1 
ATOM   9411  C  CG2 . ILE C  1 71  ? 9.795   0.547   -8.874  1.00 28.48 ? 88   ILE C CG2 1 
ATOM   9412  C  CD1 . ILE C  1 71  ? 8.652   -0.176  -11.623 1.00 31.39 ? 88   ILE C CD1 1 
ATOM   9413  N  N   . GLN C  1 72  ? 7.093   -0.147  -6.095  1.00 27.44 ? 89   GLN C N   1 
ATOM   9414  C  CA  . GLN C  1 72  ? 6.953   0.502   -4.799  1.00 28.98 ? 89   GLN C CA  1 
ATOM   9415  C  C   . GLN C  1 72  ? 7.509   -0.395  -3.690  1.00 28.28 ? 89   GLN C C   1 
ATOM   9416  O  O   . GLN C  1 72  ? 8.024   0.113   -2.697  1.00 28.84 ? 89   GLN C O   1 
ATOM   9417  C  CB  . GLN C  1 72  ? 5.504   0.907   -4.510  1.00 30.81 ? 89   GLN C CB  1 
ATOM   9418  C  CG  . GLN C  1 72  ? 5.303   1.600   -3.163  1.00 33.12 ? 89   GLN C CG  1 
ATOM   9419  C  CD  . GLN C  1 72  ? 3.848   1.733   -2.762  1.00 35.72 ? 89   GLN C CD  1 
ATOM   9420  O  OE1 . GLN C  1 72  ? 3.090   0.757   -2.756  1.00 38.11 ? 89   GLN C OE1 1 
ATOM   9421  N  NE2 . GLN C  1 72  ? 3.441   2.942   -2.401  1.00 37.62 ? 89   GLN C NE2 1 
ATOM   9422  N  N   . GLU C  1 73  ? 7.419   -1.721  -3.866  1.00 28.93 ? 90   GLU C N   1 
ATOM   9423  C  CA  . GLU C  1 73  ? 7.891   -2.675  -2.870  1.00 30.69 ? 90   GLU C CA  1 
ATOM   9424  C  C   . GLU C  1 73  ? 9.367   -3.038  -3.064  1.00 28.37 ? 90   GLU C C   1 
ATOM   9425  O  O   . GLU C  1 73  ? 9.907   -3.806  -2.270  1.00 29.17 ? 90   GLU C O   1 
ATOM   9426  C  CB  . GLU C  1 73  ? 7.043   -3.951  -2.880  1.00 35.22 ? 90   GLU C CB  1 
ATOM   9427  C  CG  . GLU C  1 73  ? 5.846   -3.892  -1.932  1.00 39.92 ? 90   GLU C CG  1 
ATOM   9428  C  CD  . GLU C  1 73  ? 5.069   -5.190  -1.746  1.00 43.38 ? 90   GLU C CD  1 
ATOM   9429  O  OE1 . GLU C  1 73  ? 3.878   -5.170  -2.131  1.00 45.47 ? 90   GLU C OE1 1 
ATOM   9430  O  OE2 . GLU C  1 73  ? 5.617   -6.196  -1.211  1.00 41.67 ? 90   GLU C OE2 1 
ATOM   9431  N  N   . ARG C  1 74  ? 10.028  -2.493  -4.094  1.00 25.50 ? 91   ARG C N   1 
ATOM   9432  C  CA  . ARG C  1 74  ? 11.420  -2.836  -4.369  1.00 26.11 ? 91   ARG C CA  1 
ATOM   9433  C  C   . ARG C  1 74  ? 12.336  -1.628  -4.178  1.00 23.47 ? 91   ARG C C   1 
ATOM   9434  O  O   . ARG C  1 74  ? 13.395  -1.750  -3.559  1.00 22.91 ? 91   ARG C O   1 
ATOM   9435  C  CB  . ARG C  1 74  ? 11.616  -3.396  -5.783  1.00 28.34 ? 91   ARG C CB  1 
ATOM   9436  C  CG  . ARG C  1 74  ? 10.974  -4.754  -6.030  1.00 32.26 ? 91   ARG C CG  1 
ATOM   9437  C  CD  . ARG C  1 74  ? 11.311  -5.292  -7.418  1.00 35.79 ? 91   ARG C CD  1 
ATOM   9438  N  NE  . ARG C  1 74  ? 10.602  -6.546  -7.708  1.00 39.50 ? 91   ARG C NE  1 
ATOM   9439  C  CZ  . ARG C  1 74  ? 11.134  -7.742  -7.951  1.00 42.69 ? 91   ARG C CZ  1 
ATOM   9440  N  NH1 . ARG C  1 74  ? 12.448  -7.918  -7.990  1.00 44.32 ? 91   ARG C NH1 1 
ATOM   9441  N  NH2 . ARG C  1 74  ? 10.333  -8.778  -8.159  1.00 44.09 ? 91   ARG C NH2 1 
ATOM   9442  N  N   . ASN C  1 75  ? 11.930  -0.478  -4.734  1.00 21.39 ? 92   ASN C N   1 
ATOM   9443  C  CA  . ASN C  1 75  ? 12.760  0.715   -4.780  1.00 20.80 ? 92   ASN C CA  1 
ATOM   9444  C  C   . ASN C  1 75  ? 11.842  1.937   -4.766  1.00 21.23 ? 92   ASN C C   1 
ATOM   9445  O  O   . ASN C  1 75  ? 11.277  2.299   -5.792  1.00 21.59 ? 92   ASN C O   1 
ATOM   9446  C  CB  . ASN C  1 75  ? 13.676  0.657   -5.999  1.00 20.14 ? 92   ASN C CB  1 
ATOM   9447  C  CG  . ASN C  1 75  ? 14.610  1.837   -6.106  1.00 19.68 ? 92   ASN C CG  1 
ATOM   9448  O  OD1 . ASN C  1 75  ? 14.331  2.917   -5.574  1.00 19.15 ? 92   ASN C OD1 1 
ATOM   9449  N  ND2 . ASN C  1 75  ? 15.717  1.651   -6.815  1.00 20.53 ? 92   ASN C ND2 1 
ATOM   9450  N  N   . GLU C  1 76  ? 11.693  2.555   -3.591  1.00 22.07 ? 93   GLU C N   1 
ATOM   9451  C  CA  . GLU C  1 76  ? 10.656  3.551   -3.360  1.00 24.17 ? 93   GLU C CA  1 
ATOM   9452  C  C   . GLU C  1 76  ? 10.941  4.804   -4.181  1.00 22.48 ? 93   GLU C C   1 
ATOM   9453  O  O   . GLU C  1 76  ? 10.034  5.379   -4.783  1.00 20.69 ? 93   GLU C O   1 
ATOM   9454  C  CB  . GLU C  1 76  ? 10.606  3.854   -1.863  1.00 26.41 ? 93   GLU C CB  1 
ATOM   9455  C  CG  . GLU C  1 76  ? 9.491   4.808   -1.455  1.00 29.22 ? 93   GLU C CG  1 
ATOM   9456  C  CD  . GLU C  1 76  ? 9.362   4.922   0.052   1.00 31.45 ? 93   GLU C CD  1 
ATOM   9457  O  OE1 . GLU C  1 76  ? 10.250  5.527   0.701   1.00 33.64 ? 93   GLU C OE1 1 
ATOM   9458  O  OE2 . GLU C  1 76  ? 8.373   4.372   0.576   1.00 35.02 ? 93   GLU C OE2 1 
ATOM   9459  N  N   . LYS C  1 77  ? 12.216  5.204   -4.215  1.00 21.69 ? 94   LYS C N   1 
ATOM   9460  C  CA  . LYS C  1 77  ? 12.604  6.420   -4.908  1.00 22.05 ? 94   LYS C CA  1 
ATOM   9461  C  C   . LYS C  1 77  ? 12.449  6.240   -6.417  1.00 21.17 ? 94   LYS C C   1 
ATOM   9462  O  O   . LYS C  1 77  ? 12.027  7.175   -7.094  1.00 20.48 ? 94   LYS C O   1 
ATOM   9463  C  CB  . LYS C  1 77  ? 13.998  6.887   -4.479  1.00 23.05 ? 94   LYS C CB  1 
ATOM   9464  C  CG  . LYS C  1 77  ? 14.019  7.502   -3.090  1.00 25.19 ? 94   LYS C CG  1 
ATOM   9465  C  CD  . LYS C  1 77  ? 15.287  8.274   -2.755  1.00 26.85 ? 94   LYS C CD  1 
ATOM   9466  C  CE  . LYS C  1 77  ? 15.131  9.053   -1.491  1.00 28.63 ? 94   LYS C CE  1 
ATOM   9467  N  NZ  . LYS C  1 77  ? 16.395  9.654   -1.055  1.00 30.81 ? 94   LYS C NZ  1 
ATOM   9468  N  N   . LEU C  1 78  ? 12.775  5.049   -6.937  1.00 20.57 ? 95   LEU C N   1 
ATOM   9469  C  CA  . LEU C  1 78  ? 12.568  4.754   -8.353  1.00 21.10 ? 95   LEU C CA  1 
ATOM   9470  C  C   . LEU C  1 78  ? 11.076  4.803   -8.680  1.00 20.44 ? 95   LEU C C   1 
ATOM   9471  O  O   . LEU C  1 78  ? 10.689  5.346   -9.712  1.00 20.22 ? 95   LEU C O   1 
ATOM   9472  C  CB  . LEU C  1 78  ? 13.175  3.413   -8.758  1.00 21.23 ? 95   LEU C CB  1 
ATOM   9473  C  CG  . LEU C  1 78  ? 13.088  3.040   -10.241 1.00 22.23 ? 95   LEU C CG  1 
ATOM   9474  C  CD1 . LEU C  1 78  ? 13.725  4.092   -11.142 1.00 22.76 ? 95   LEU C CD1 1 
ATOM   9475  C  CD2 . LEU C  1 78  ? 13.740  1.684   -10.467 1.00 22.88 ? 95   LEU C CD2 1 
ATOM   9476  N  N   . PHE C  1 79  ? 10.249  4.244   -7.789  1.00 19.97 ? 96   PHE C N   1 
ATOM   9477  C  CA  . PHE C  1 79  ? 8.809   4.222   -7.983  1.00 19.81 ? 96   PHE C CA  1 
ATOM   9478  C  C   . PHE C  1 79  ? 8.273   5.643   -8.157  1.00 19.79 ? 96   PHE C C   1 
ATOM   9479  O  O   . PHE C  1 79  ? 7.531   5.906   -9.104  1.00 20.89 ? 96   PHE C O   1 
ATOM   9480  C  CB  . PHE C  1 79  ? 8.136   3.473   -6.827  1.00 21.28 ? 96   PHE C CB  1 
ATOM   9481  C  CG  . PHE C  1 79  ? 6.619   3.607   -6.800  1.00 22.47 ? 96   PHE C CG  1 
ATOM   9482  C  CD1 . PHE C  1 79  ? 5.821   2.850   -7.652  1.00 23.34 ? 96   PHE C CD1 1 
ATOM   9483  C  CD2 . PHE C  1 79  ? 5.996   4.487   -5.922  1.00 23.51 ? 96   PHE C CD2 1 
ATOM   9484  C  CE1 . PHE C  1 79  ? 4.439   2.980   -7.627  1.00 25.13 ? 96   PHE C CE1 1 
ATOM   9485  C  CE2 . PHE C  1 79  ? 4.615   4.616   -5.903  1.00 24.45 ? 96   PHE C CE2 1 
ATOM   9486  C  CZ  . PHE C  1 79  ? 3.839   3.860   -6.752  1.00 24.47 ? 96   PHE C CZ  1 
ATOM   9487  N  N   . TYR C  1 80  ? 8.646   6.557   -7.254  1.00 19.66 ? 97   TYR C N   1 
ATOM   9488  C  CA  . TYR C  1 80  ? 8.093   7.905   -7.264  1.00 20.60 ? 97   TYR C CA  1 
ATOM   9489  C  C   . TYR C  1 80  ? 8.647   8.693   -8.449  1.00 21.25 ? 97   TYR C C   1 
ATOM   9490  O  O   . TYR C  1 80  ? 7.919   9.484   -9.042  1.00 21.17 ? 97   TYR C O   1 
ATOM   9491  C  CB  . TYR C  1 80  ? 8.279   8.583   -5.903  1.00 20.01 ? 97   TYR C CB  1 
ATOM   9492  C  CG  . TYR C  1 80  ? 7.271   8.046   -4.899  1.00 21.14 ? 97   TYR C CG  1 
ATOM   9493  C  CD1 . TYR C  1 80  ? 5.923   8.345   -5.037  1.00 21.64 ? 97   TYR C CD1 1 
ATOM   9494  C  CD2 . TYR C  1 80  ? 7.646   7.212   -3.851  1.00 21.48 ? 97   TYR C CD2 1 
ATOM   9495  C  CE1 . TYR C  1 80  ? 4.979   7.840   -4.162  1.00 22.53 ? 97   TYR C CE1 1 
ATOM   9496  C  CE2 . TYR C  1 80  ? 6.711   6.708   -2.961  1.00 22.28 ? 97   TYR C CE2 1 
ATOM   9497  C  CZ  . TYR C  1 80  ? 5.373   7.021   -3.123  1.00 23.34 ? 97   TYR C CZ  1 
ATOM   9498  O  OH  . TYR C  1 80  ? 4.416   6.545   -2.274  1.00 27.53 ? 97   TYR C OH  1 
ATOM   9499  N  N   . ARG C  1 81  ? 9.916   8.446   -8.801  1.00 21.57 ? 98   ARG C N   1 
ATOM   9500  C  CA  . ARG C  1 81  ? 10.534  9.023   -9.988  1.00 22.76 ? 98   ARG C CA  1 
ATOM   9501  C  C   . ARG C  1 81  ? 9.730   8.697   -11.246 1.00 22.62 ? 98   ARG C C   1 
ATOM   9502  O  O   . ARG C  1 81  ? 9.408   9.596   -12.023 1.00 25.05 ? 98   ARG C O   1 
ATOM   9503  C  CB  . ARG C  1 81  ? 11.976  8.521   -10.144 1.00 23.00 ? 98   ARG C CB  1 
ATOM   9504  C  CG  . ARG C  1 81  ? 12.638  8.863   -11.472 1.00 24.20 ? 98   ARG C CG  1 
ATOM   9505  C  CD  . ARG C  1 81  ? 12.761  10.365  -11.680 1.00 24.89 ? 98   ARG C CD  1 
ATOM   9506  N  NE  . ARG C  1 81  ? 13.320  10.703  -12.993 1.00 26.58 ? 98   ARG C NE  1 
ATOM   9507  C  CZ  . ARG C  1 81  ? 14.597  10.650  -13.365 1.00 28.80 ? 98   ARG C CZ  1 
ATOM   9508  N  NH1 . ARG C  1 81  ? 15.556  10.389  -12.491 1.00 29.89 ? 98   ARG C NH1 1 
ATOM   9509  N  NH2 . ARG C  1 81  ? 14.916  10.900  -14.624 1.00 29.81 ? 98   ARG C NH2 1 
ATOM   9510  N  N   . ILE C  1 82  ? 9.433   7.409   -11.454 1.00 22.81 ? 99   ILE C N   1 
ATOM   9511  C  CA  A ILE C  1 82  ? 8.719   6.907   -12.617 0.61 23.79 ? 99   ILE C CA  1 
ATOM   9512  C  CA  B ILE C  1 82  ? 8.763   6.995   -12.678 0.39 23.28 ? 99   ILE C CA  1 
ATOM   9513  C  C   . ILE C  1 82  ? 7.347   7.576   -12.712 1.00 24.67 ? 99   ILE C C   1 
ATOM   9514  O  O   . ILE C  1 82  ? 6.897   8.000   -13.778 1.00 24.92 ? 99   ILE C O   1 
ATOM   9515  C  CB  A ILE C  1 82  ? 8.608   5.375   -12.493 0.61 25.03 ? 99   ILE C CB  1 
ATOM   9516  C  CB  B ILE C  1 82  ? 8.810   5.470   -12.895 0.39 23.18 ? 99   ILE C CB  1 
ATOM   9517  C  CG1 A ILE C  1 82  ? 9.913   4.675   -12.900 0.61 25.51 ? 99   ILE C CG1 1 
ATOM   9518  C  CG1 B ILE C  1 82  ? 8.087   4.687   -11.801 0.39 22.97 ? 99   ILE C CG1 1 
ATOM   9519  C  CG2 A ILE C  1 82  ? 7.405   4.839   -13.265 0.61 25.36 ? 99   ILE C CG2 1 
ATOM   9520  C  CG2 B ILE C  1 82  ? 10.256  4.997   -13.067 0.39 22.89 ? 99   ILE C CG2 1 
ATOM   9521  C  CD1 A ILE C  1 82  ? 10.018  3.236   -12.424 0.61 25.70 ? 99   ILE C CD1 1 
ATOM   9522  C  CD1 B ILE C  1 82  ? 8.290   3.188   -11.884 0.39 23.34 ? 99   ILE C CD1 1 
ATOM   9523  N  N   . LEU C  1 83  ? 6.671   7.644   -11.561 1.00 25.18 ? 100  LEU C N   1 
ATOM   9524  C  CA  . LEU C  1 83  ? 5.350   8.244   -11.461 1.00 27.62 ? 100  LEU C CA  1 
ATOM   9525  C  C   . LEU C  1 83  ? 5.413   9.730   -11.820 1.00 28.30 ? 100  LEU C C   1 
ATOM   9526  O  O   . LEU C  1 83  ? 4.583   10.225  -12.577 1.00 28.00 ? 100  LEU C O   1 
ATOM   9527  C  CB  . LEU C  1 83  ? 4.869   7.993   -10.032 1.00 29.30 ? 100  LEU C CB  1 
ATOM   9528  C  CG  . LEU C  1 83  ? 3.452   8.445   -9.668  1.00 32.49 ? 100  LEU C CG  1 
ATOM   9529  C  CD1 . LEU C  1 83  ? 2.408   8.181   -10.747 1.00 33.15 ? 100  LEU C CD1 1 
ATOM   9530  C  CD2 . LEU C  1 83  ? 3.082   7.720   -8.376  1.00 33.16 ? 100  LEU C CD2 1 
ATOM   9531  N  N   . GLN C  1 84  ? 6.429   10.428  -11.305 1.00 29.95 ? 101  GLN C N   1 
ATOM   9532  C  CA  . GLN C  1 84  ? 6.583   11.857  -11.535 1.00 29.72 ? 101  GLN C CA  1 
ATOM   9533  C  C   . GLN C  1 84  ? 6.944   12.145  -12.991 1.00 30.90 ? 101  GLN C C   1 
ATOM   9534  O  O   . GLN C  1 84  ? 6.528   13.168  -13.532 1.00 31.89 ? 101  GLN C O   1 
ATOM   9535  C  CB  . GLN C  1 84  ? 7.632   12.425  -10.582 1.00 29.85 ? 101  GLN C CB  1 
ATOM   9536  C  CG  . GLN C  1 84  ? 7.157   12.489  -9.135  1.00 30.32 ? 101  GLN C CG  1 
ATOM   9537  C  CD  . GLN C  1 84  ? 8.250   12.841  -8.149  1.00 31.18 ? 101  GLN C CD  1 
ATOM   9538  O  OE1 . GLN C  1 84  ? 9.450   12.666  -8.400  1.00 31.25 ? 101  GLN C OE1 1 
ATOM   9539  N  NE2 . GLN C  1 84  ? 7.829   13.341  -6.998  1.00 31.74 ? 101  GLN C NE2 1 
ATOM   9540  N  N   . ASP C  1 85  ? 7.721   11.249  -13.612 1.00 30.39 ? 102  ASP C N   1 
ATOM   9541  C  CA  . ASP C  1 85  ? 8.117   11.383  -15.008 1.00 30.32 ? 102  ASP C CA  1 
ATOM   9542  C  C   . ASP C  1 85  ? 6.900   11.462  -15.925 1.00 31.98 ? 102  ASP C C   1 
ATOM   9543  O  O   . ASP C  1 85  ? 6.913   12.222  -16.886 1.00 31.94 ? 102  ASP C O   1 
ATOM   9544  C  CB  . ASP C  1 85  ? 8.956   10.205  -15.486 1.00 29.64 ? 102  ASP C CB  1 
ATOM   9545  C  CG  . ASP C  1 85  ? 10.436  10.219  -15.126 1.00 29.20 ? 102  ASP C CG  1 
ATOM   9546  O  OD1 . ASP C  1 85  ? 10.924  11.267  -14.660 1.00 29.88 ? 102  ASP C OD1 1 
ATOM   9547  O  OD2 . ASP C  1 85  ? 11.087  9.169   -15.306 1.00 29.25 ? 102  ASP C OD2 1 
ATOM   9548  N  N   . ASP C  1 86  ? 5.874   10.650  -15.639 1.00 33.34 ? 103  ASP C N   1 
ATOM   9549  C  CA  . ASP C  1 86  ? 4.790   10.389  -16.574 1.00 35.00 ? 103  ASP C CA  1 
ATOM   9550  C  C   . ASP C  1 86  ? 3.461   10.530  -15.833 1.00 32.28 ? 103  ASP C C   1 
ATOM   9551  O  O   . ASP C  1 86  ? 2.572   9.694   -15.966 1.00 30.06 ? 103  ASP C O   1 
ATOM   9552  C  CB  . ASP C  1 86  ? 4.971   9.010   -17.194 1.00 37.89 ? 103  ASP C CB  1 
ATOM   9553  C  CG  . ASP C  1 86  ? 4.187   8.716   -18.466 1.00 41.70 ? 103  ASP C CG  1 
ATOM   9554  O  OD1 . ASP C  1 86  ? 3.797   9.683   -19.161 1.00 45.74 ? 103  ASP C OD1 1 
ATOM   9555  O  OD2 . ASP C  1 86  ? 3.948   7.518   -18.738 1.00 42.55 ? 103  ASP C OD2 1 
ATOM   9556  N  N   . ILE C  1 87  ? 3.341   11.612  -15.058 1.00 32.66 ? 104  ILE C N   1 
ATOM   9557  C  CA  . ILE C  1 87  ? 2.317   11.719  -14.029 1.00 33.43 ? 104  ILE C CA  1 
ATOM   9558  C  C   . ILE C  1 87  ? 0.925   11.732  -14.663 1.00 31.78 ? 104  ILE C C   1 
ATOM   9559  O  O   . ILE C  1 87  ? 0.012   11.086  -14.156 1.00 30.36 ? 104  ILE C O   1 
ATOM   9560  C  CB  . ILE C  1 87  ? 2.571   12.945  -13.127 1.00 35.81 ? 104  ILE C CB  1 
ATOM   9561  C  CG1 . ILE C  1 87  ? 1.693   12.919  -11.875 1.00 35.84 ? 104  ILE C CG1 1 
ATOM   9562  C  CG2 . ILE C  1 87  ? 2.425   14.264  -13.893 1.00 36.28 ? 104  ILE C CG2 1 
ATOM   9563  C  CD1 . ILE C  1 87  ? 2.126   11.904  -10.834 1.00 37.62 ? 104  ILE C CD1 1 
ATOM   9564  N  N   . GLU C  1 88  ? 0.768   12.443  -15.783 1.00 31.97 ? 105  GLU C N   1 
ATOM   9565  C  CA  . GLU C  1 88  ? -0.538  12.579  -16.409 1.00 33.24 ? 105  GLU C CA  1 
ATOM   9566  C  C   . GLU C  1 88  ? -1.046  11.214  -16.877 1.00 30.68 ? 105  GLU C C   1 
ATOM   9567  O  O   . GLU C  1 88  ? -2.221  10.897  -16.695 1.00 28.48 ? 105  GLU C O   1 
ATOM   9568  C  CB  . GLU C  1 88  ? -0.505  13.601  -17.547 1.00 34.71 ? 105  GLU C CB  1 
ATOM   9569  C  CG  . GLU C  1 88  ? -1.888  13.837  -18.146 1.00 36.94 ? 105  GLU C CG  1 
ATOM   9570  C  CD  . GLU C  1 88  ? -2.016  15.017  -19.091 1.00 37.99 ? 105  GLU C CD  1 
ATOM   9571  O  OE1 . GLU C  1 88  ? -1.020  15.746  -19.310 1.00 38.38 ? 105  GLU C OE1 1 
ATOM   9572  O  OE2 . GLU C  1 88  ? -3.142  15.192  -19.603 1.00 36.47 ? 105  GLU C OE2 1 
ATOM   9573  N  N   . SER C  1 89  ? -0.151  10.401  -17.449 1.00 30.72 ? 106  SER C N   1 
ATOM   9574  C  CA  . SER C  1 89  ? -0.517  9.096   -17.985 1.00 31.98 ? 106  SER C CA  1 
ATOM   9575  C  C   . SER C  1 89  ? -0.722  8.048   -16.890 1.00 30.22 ? 106  SER C C   1 
ATOM   9576  O  O   . SER C  1 89  ? -1.527  7.139   -17.071 1.00 30.44 ? 106  SER C O   1 
ATOM   9577  C  CB  . SER C  1 89  ? 0.503   8.598   -18.981 1.00 32.48 ? 106  SER C CB  1 
ATOM   9578  O  OG  . SER C  1 89  ? 0.514   9.409   -20.145 1.00 35.97 ? 106  SER C OG  1 
ATOM   9579  N  N   . LEU C  1 90  ? 0.025   8.142   -15.781 1.00 30.56 ? 107  LEU C N   1 
ATOM   9580  C  CA  . LEU C  1 90  ? 0.086   7.053   -14.813 1.00 30.61 ? 107  LEU C CA  1 
ATOM   9581  C  C   . LEU C  1 90  ? -0.878  7.266   -13.641 1.00 32.60 ? 107  LEU C C   1 
ATOM   9582  O  O   . LEU C  1 90  ? -1.197  6.312   -12.934 1.00 31.05 ? 107  LEU C O   1 
ATOM   9583  C  CB  . LEU C  1 90  ? 1.519   6.870   -14.319 1.00 31.08 ? 107  LEU C CB  1 
ATOM   9584  C  CG  . LEU C  1 90  ? 2.547   6.422   -15.364 1.00 31.13 ? 107  LEU C CG  1 
ATOM   9585  C  CD1 . LEU C  1 90  ? 3.917   6.307   -14.726 1.00 31.59 ? 107  LEU C CD1 1 
ATOM   9586  C  CD2 . LEU C  1 90  ? 2.174   5.110   -16.028 1.00 31.45 ? 107  LEU C CD2 1 
ATOM   9587  N  N   . MET C  1 91  ? -1.344  8.502   -13.427 1.00 35.42 ? 108  MET C N   1 
ATOM   9588  C  CA  . MET C  1 91  ? -2.281  8.783   -12.347 1.00 37.23 ? 108  MET C CA  1 
ATOM   9589  C  C   . MET C  1 91  ? -3.540  7.921   -12.482 1.00 36.41 ? 108  MET C C   1 
ATOM   9590  O  O   . MET C  1 91  ? -3.987  7.346   -11.489 1.00 36.45 ? 108  MET C O   1 
ATOM   9591  C  CB  . MET C  1 91  ? -2.609  10.280  -12.258 1.00 39.81 ? 108  MET C CB  1 
ATOM   9592  C  CG  . MET C  1 91  ? -1.538  11.077  -11.522 1.00 43.03 ? 108  MET C CG  1 
ATOM   9593  S  SD  . MET C  1 91  ? -1.953  12.792  -11.129 1.00 50.66 ? 108  MET C SD  1 
ATOM   9594  C  CE  . MET C  1 91  ? -2.056  13.566  -12.749 1.00 49.65 ? 108  MET C CE  1 
ATOM   9595  N  N   . PRO C  1 92  ? -4.150  7.778   -13.686 1.00 35.95 ? 109  PRO C N   1 
ATOM   9596  C  CA  . PRO C  1 92  ? -5.280  6.858   -13.867 1.00 35.61 ? 109  PRO C CA  1 
ATOM   9597  C  C   . PRO C  1 92  ? -4.969  5.361   -13.940 1.00 35.05 ? 109  PRO C C   1 
ATOM   9598  O  O   . PRO C  1 92  ? -5.882  4.557   -14.114 1.00 36.10 ? 109  PRO C O   1 
ATOM   9599  C  CB  . PRO C  1 92  ? -5.909  7.371   -15.175 1.00 36.69 ? 109  PRO C CB  1 
ATOM   9600  C  CG  . PRO C  1 92  ? -4.749  7.934   -15.954 1.00 36.23 ? 109  PRO C CG  1 
ATOM   9601  C  CD  . PRO C  1 92  ? -3.840  8.541   -14.905 1.00 37.05 ? 109  PRO C CD  1 
ATOM   9602  N  N   . ILE C  1 93  ? -3.683  4.998   -13.826 1.00 33.81 ? 110  ILE C N   1 
ATOM   9603  C  CA  . ILE C  1 93  ? -3.262  3.619   -13.637 1.00 33.21 ? 110  ILE C CA  1 
ATOM   9604  C  C   . ILE C  1 93  ? -3.153  3.327   -12.139 1.00 31.74 ? 110  ILE C C   1 
ATOM   9605  O  O   . ILE C  1 93  ? -3.669  2.314   -11.680 1.00 31.63 ? 110  ILE C O   1 
ATOM   9606  C  CB  . ILE C  1 93  ? -1.932  3.331   -14.367 1.00 34.64 ? 110  ILE C CB  1 
ATOM   9607  C  CG1 . ILE C  1 93  ? -2.029  3.586   -15.874 1.00 36.39 ? 110  ILE C CG1 1 
ATOM   9608  C  CG2 . ILE C  1 93  ? -1.434  1.913   -14.077 1.00 33.99 ? 110  ILE C CG2 1 
ATOM   9609  C  CD1 . ILE C  1 93  ? -3.114  2.790   -16.578 1.00 38.02 ? 110  ILE C CD1 1 
ATOM   9610  N  N   . VAL C  1 94  ? -2.468  4.198   -11.383 1.00 31.23 ? 111  VAL C N   1 
ATOM   9611  C  CA  . VAL C  1 94  ? -2.213  3.934   -9.970  1.00 31.81 ? 111  VAL C CA  1 
ATOM   9612  C  C   . VAL C  1 94  ? -3.447  4.282   -9.137  1.00 31.92 ? 111  VAL C C   1 
ATOM   9613  O  O   . VAL C  1 94  ? -3.619  3.729   -8.050  1.00 30.54 ? 111  VAL C O   1 
ATOM   9614  C  CB  . VAL C  1 94  ? -0.962  4.627   -9.396  1.00 32.33 ? 111  VAL C CB  1 
ATOM   9615  C  CG1 . VAL C  1 94  ? 0.312   4.166   -10.098 1.00 32.28 ? 111  VAL C CG1 1 
ATOM   9616  C  CG2 . VAL C  1 94  ? -1.073  6.148   -9.415  1.00 32.79 ? 111  VAL C CG2 1 
ATOM   9617  N  N   . TYR C  1 95  ? -4.291  5.199   -9.633  1.00 33.08 ? 112  TYR C N   1 
ATOM   9618  C  CA  . TYR C  1 95  ? -5.501  5.579   -8.918  1.00 35.04 ? 112  TYR C CA  1 
ATOM   9619  C  C   . TYR C  1 95  ? -6.715  5.317   -9.813  1.00 35.97 ? 112  TYR C C   1 
ATOM   9620  O  O   . TYR C  1 95  ? -6.702  4.395   -10.621 1.00 34.42 ? 112  TYR C O   1 
ATOM   9621  C  CB  . TYR C  1 95  ? -5.372  7.025   -8.419  1.00 35.32 ? 112  TYR C CB  1 
ATOM   9622  C  CG  . TYR C  1 95  ? -6.389  7.379   -7.343  1.00 36.73 ? 112  TYR C CG  1 
ATOM   9623  C  CD1 . TYR C  1 95  ? -6.567  6.559   -6.235  1.00 36.72 ? 112  TYR C CD1 1 
ATOM   9624  C  CD2 . TYR C  1 95  ? -7.210  8.494   -7.462  1.00 38.81 ? 112  TYR C CD2 1 
ATOM   9625  C  CE1 . TYR C  1 95  ? -7.511  6.849   -5.267  1.00 39.04 ? 112  TYR C CE1 1 
ATOM   9626  C  CE2 . TYR C  1 95  ? -8.157  8.797   -6.496  1.00 40.08 ? 112  TYR C CE2 1 
ATOM   9627  C  CZ  . TYR C  1 95  ? -8.310  7.970   -5.400  1.00 40.96 ? 112  TYR C CZ  1 
ATOM   9628  O  OH  . TYR C  1 95  ? -9.234  8.256   -4.441  1.00 49.88 ? 112  TYR C OH  1 
ATOM   9629  N  N   . THR C  1 96  ? -7.784  6.101   -9.625  1.00 37.40 ? 113  THR C N   1 
ATOM   9630  C  CA  . THR C  1 96  ? -9.018  5.942   -10.382 1.00 38.63 ? 113  THR C CA  1 
ATOM   9631  C  C   . THR C  1 96  ? -8.724  6.258   -11.848 1.00 38.74 ? 113  THR C C   1 
ATOM   9632  O  O   . THR C  1 96  ? -8.033  7.238   -12.124 1.00 38.15 ? 113  THR C O   1 
ATOM   9633  C  CB  . THR C  1 96  ? -10.106 6.867   -9.823  1.00 39.23 ? 113  THR C CB  1 
ATOM   9634  O  OG1 . THR C  1 96  ? -10.322 6.541   -8.454  1.00 40.48 ? 113  THR C OG1 1 
ATOM   9635  C  CG2 . THR C  1 96  ? -11.436 6.727   -10.541 1.00 40.34 ? 113  THR C CG2 1 
ATOM   9636  N  N   . PRO C  1 97  ? -9.254  5.487   -12.831 1.00 38.87 ? 114  PRO C N   1 
ATOM   9637  C  CA  . PRO C  1 97  ? -10.155 4.354   -12.573 1.00 38.51 ? 114  PRO C CA  1 
ATOM   9638  C  C   . PRO C  1 97  ? -9.638  2.914   -12.513 1.00 37.09 ? 114  PRO C C   1 
ATOM   9639  O  O   . PRO C  1 97  ? -10.434 1.995   -12.328 1.00 37.76 ? 114  PRO C O   1 
ATOM   9640  C  CB  . PRO C  1 97  ? -11.084 4.557   -13.787 1.00 39.96 ? 114  PRO C CB  1 
ATOM   9641  C  CG  . PRO C  1 97  ? -10.136 4.879   -14.922 1.00 39.94 ? 114  PRO C CG  1 
ATOM   9642  C  CD  . PRO C  1 97  ? -9.074  5.745   -14.270 1.00 39.77 ? 114  PRO C CD  1 
ATOM   9643  N  N   . THR C  1 98  ? -8.322  2.703   -12.652 1.00 36.14 ? 115  THR C N   1 
ATOM   9644  C  CA  . THR C  1 98  ? -7.781  1.354   -12.783 1.00 33.86 ? 115  THR C CA  1 
ATOM   9645  C  C   . THR C  1 98  ? -7.728  0.655   -11.424 1.00 33.07 ? 115  THR C C   1 
ATOM   9646  O  O   . THR C  1 98  ? -8.009  -0.538  -11.332 1.00 30.97 ? 115  THR C O   1 
ATOM   9647  C  CB  . THR C  1 98  ? -6.390  1.399   -13.418 1.00 35.37 ? 115  THR C CB  1 
ATOM   9648  O  OG1 . THR C  1 98  ? -6.522  2.078   -14.662 1.00 34.69 ? 115  THR C OG1 1 
ATOM   9649  C  CG2 . THR C  1 98  ? -5.806  0.019   -13.666 1.00 34.72 ? 115  THR C CG2 1 
ATOM   9650  N  N   . VAL C  1 99  ? -7.349  1.399   -10.376 1.00 31.56 ? 116  VAL C N   1 
ATOM   9651  C  CA  . VAL C  1 99  ? -6.973  0.809   -9.098  1.00 32.35 ? 116  VAL C CA  1 
ATOM   9652  C  C   . VAL C  1 99  ? -8.069  -0.129  -8.589  1.00 32.97 ? 116  VAL C C   1 
ATOM   9653  O  O   . VAL C  1 99  ? -7.765  -1.213  -8.095  1.00 32.06 ? 116  VAL C O   1 
ATOM   9654  C  CB  . VAL C  1 99  ? -6.622  1.882   -8.048  1.00 33.04 ? 116  VAL C CB  1 
ATOM   9655  C  CG1 . VAL C  1 99  ? -7.782  2.835   -7.775  1.00 34.64 ? 116  VAL C CG1 1 
ATOM   9656  C  CG2 . VAL C  1 99  ? -6.135  1.253   -6.750  1.00 33.50 ? 116  VAL C CG2 1 
ATOM   9657  N  N   . GLY C  1 100 ? -9.336  0.279   -8.726  1.00 34.32 ? 117  GLY C N   1 
ATOM   9658  C  CA  . GLY C  1 100 ? -10.457 -0.470  -8.175  1.00 35.86 ? 117  GLY C CA  1 
ATOM   9659  C  C   . GLY C  1 100 ? -10.651 -1.836  -8.838  1.00 37.55 ? 117  GLY C C   1 
ATOM   9660  O  O   . GLY C  1 100 ? -11.181 -2.756  -8.217  1.00 40.77 ? 117  GLY C O   1 
ATOM   9661  N  N   . LEU C  1 101 ? -10.230 -1.962  -10.101 1.00 36.62 ? 118  LEU C N   1 
ATOM   9662  C  CA  . LEU C  1 101 ? -10.360 -3.210  -10.835 1.00 38.71 ? 118  LEU C CA  1 
ATOM   9663  C  C   . LEU C  1 101 ? -9.351  -4.249  -10.339 1.00 41.02 ? 118  LEU C C   1 
ATOM   9664  O  O   . LEU C  1 101 ? -9.655  -5.440  -10.327 1.00 39.23 ? 118  LEU C O   1 
ATOM   9665  C  CB  . LEU C  1 101 ? -10.192 -2.929  -12.328 1.00 40.28 ? 118  LEU C CB  1 
ATOM   9666  C  CG  . LEU C  1 101 ? -11.292 -2.089  -12.987 1.00 41.27 ? 118  LEU C CG  1 
ATOM   9667  C  CD1 . LEU C  1 101 ? -10.885 -1.696  -14.397 1.00 42.65 ? 118  LEU C CD1 1 
ATOM   9668  C  CD2 . LEU C  1 101 ? -12.622 -2.824  -13.007 1.00 42.31 ? 118  LEU C CD2 1 
ATOM   9669  N  N   . ALA C  1 102 ? -8.168  -3.799  -9.900  1.00 42.23 ? 119  ALA C N   1 
ATOM   9670  C  CA  . ALA C  1 102 ? -7.022  -4.678  -9.703  1.00 44.20 ? 119  ALA C CA  1 
ATOM   9671  C  C   . ALA C  1 102 ? -7.293  -5.768  -8.665  1.00 47.36 ? 119  ALA C C   1 
ATOM   9672  O  O   . ALA C  1 102 ? -6.995  -6.933  -8.923  1.00 46.74 ? 119  ALA C O   1 
ATOM   9673  C  CB  . ALA C  1 102 ? -5.804  -3.863  -9.332  1.00 46.05 ? 119  ALA C CB  1 
HETATM 9674  N  N   . CSX C  1 103 ? -7.840  -5.395  -7.498  1.00 49.52 ? 120  CSX C N   1 
HETATM 9675  C  CA  . CSX C  1 103 ? -8.082  -6.345  -6.418  1.00 51.43 ? 120  CSX C CA  1 
HETATM 9676  C  CB  . CSX C  1 103 ? -8.611  -5.668  -5.149  1.00 56.99 ? 120  CSX C CB  1 
HETATM 9677  S  SG  . CSX C  1 103 ? -7.306  -4.954  -4.120  1.00 59.05 ? 120  CSX C SG  1 
HETATM 9678  C  C   . CSX C  1 103 ? -9.076  -7.426  -6.843  1.00 52.67 ? 120  CSX C C   1 
HETATM 9679  O  O   . CSX C  1 103 ? -8.842  -8.611  -6.608  1.00 53.58 ? 120  CSX C O   1 
HETATM 9680  O  OD  . CSX C  1 103 ? -6.362  -6.077  -3.781  1.00 57.14 ? 120  CSX C OD  1 
ATOM   9681  N  N   A SER C  1 104 ? -10.184 -7.002  -7.462  0.50 51.66 ? 121  SER C N   1 
ATOM   9682  N  N   B SER C  1 104 ? -10.187 -7.004  -7.460  0.50 51.01 ? 121  SER C N   1 
ATOM   9683  C  CA  A SER C  1 104 ? -11.236 -7.912  -7.885  0.50 50.59 ? 121  SER C CA  1 
ATOM   9684  C  CA  B SER C  1 104 ? -11.233 -7.921  -7.886  0.50 49.50 ? 121  SER C CA  1 
ATOM   9685  C  C   A SER C  1 104 ? -10.712 -8.897  -8.930  0.50 49.39 ? 121  SER C C   1 
ATOM   9686  C  C   B SER C  1 104 ? -10.689 -8.909  -8.915  0.50 48.84 ? 121  SER C C   1 
ATOM   9687  O  O   A SER C  1 104 ? -11.065 -10.075 -8.899  0.50 49.32 ? 121  SER C O   1 
ATOM   9688  O  O   B SER C  1 104 ? -11.007 -10.097 -8.863  0.50 48.92 ? 121  SER C O   1 
ATOM   9689  C  CB  A SER C  1 104 ? -12.436 -7.143  -8.391  0.50 50.53 ? 121  SER C CB  1 
ATOM   9690  C  CB  B SER C  1 104 ? -12.429 -7.174  -8.430  0.50 48.74 ? 121  SER C CB  1 
ATOM   9691  O  OG  A SER C  1 104 ? -12.037 -5.997  -9.132  0.50 49.59 ? 121  SER C OG  1 
ATOM   9692  O  OG  B SER C  1 104 ? -13.024 -6.357  -7.431  0.50 46.48 ? 121  SER C OG  1 
ATOM   9693  N  N   . GLN C  1 105 ? -9.868  -8.406  -9.846  1.00 46.27 ? 122  GLN C N   1 
ATOM   9694  C  CA  . GLN C  1 105 ? -9.333  -9.228  -10.921 1.00 45.81 ? 122  GLN C CA  1 
ATOM   9695  C  C   . GLN C  1 105 ? -8.250  -10.168 -10.388 1.00 42.59 ? 122  GLN C C   1 
ATOM   9696  O  O   . GLN C  1 105 ? -8.282  -11.360 -10.683 1.00 41.13 ? 122  GLN C O   1 
ATOM   9697  C  CB  . GLN C  1 105 ? -8.751  -8.424  -12.086 1.00 45.90 ? 122  GLN C CB  1 
ATOM   9698  C  CG  . GLN C  1 105 ? -9.676  -7.374  -12.697 1.00 48.52 ? 122  GLN C CG  1 
ATOM   9699  C  CD  . GLN C  1 105 ? -11.152 -7.679  -12.563 1.00 51.88 ? 122  GLN C CD  1 
ATOM   9700  O  OE1 . GLN C  1 105 ? -11.890 -6.965  -11.874 1.00 54.98 ? 122  GLN C OE1 1 
ATOM   9701  N  NE2 . GLN C  1 105 ? -11.596 -8.738  -13.227 1.00 53.35 ? 122  GLN C NE2 1 
ATOM   9702  N  N   . TYR C  1 106 ? -7.294  -9.624  -9.620  1.00 41.74 ? 123  TYR C N   1 
ATOM   9703  C  CA  . TYR C  1 106 ? -6.062  -10.332 -9.294  1.00 42.69 ? 123  TYR C CA  1 
ATOM   9704  C  C   . TYR C  1 106 ? -5.981  -10.702 -7.814  1.00 41.07 ? 123  TYR C C   1 
ATOM   9705  O  O   . TYR C  1 106 ? -5.396  -11.725 -7.472  1.00 40.24 ? 123  TYR C O   1 
ATOM   9706  C  CB  . TYR C  1 106 ? -4.830  -9.490  -9.643  1.00 45.30 ? 123  TYR C CB  1 
ATOM   9707  C  CG  . TYR C  1 106 ? -4.524  -9.365  -11.129 1.00 48.51 ? 123  TYR C CG  1 
ATOM   9708  C  CD1 . TYR C  1 106 ? -5.094  -8.356  -11.896 1.00 51.10 ? 123  TYR C CD1 1 
ATOM   9709  C  CD2 . TYR C  1 106 ? -3.651  -10.243 -11.763 1.00 50.42 ? 123  TYR C CD2 1 
ATOM   9710  C  CE1 . TYR C  1 106 ? -4.815  -8.229  -13.247 1.00 53.10 ? 123  TYR C CE1 1 
ATOM   9711  C  CE2 . TYR C  1 106 ? -3.365  -10.129 -13.115 1.00 52.46 ? 123  TYR C CE2 1 
ATOM   9712  C  CZ  . TYR C  1 106 ? -3.949  -9.118  -13.859 1.00 52.58 ? 123  TYR C CZ  1 
ATOM   9713  O  OH  . TYR C  1 106 ? -3.681  -8.985  -15.191 1.00 54.62 ? 123  TYR C OH  1 
ATOM   9714  N  N   . GLY C  1 107 ? -6.524  -9.861  -6.930  1.00 40.57 ? 124  GLY C N   1 
ATOM   9715  C  CA  . GLY C  1 107 ? -6.203  -9.957  -5.513  1.00 40.28 ? 124  GLY C CA  1 
ATOM   9716  C  C   . GLY C  1 107 ? -4.768  -9.488  -5.269  1.00 37.77 ? 124  GLY C C   1 
ATOM   9717  O  O   . GLY C  1 107 ? -4.302  -8.573  -5.944  1.00 37.68 ? 124  GLY C O   1 
ATOM   9718  N  N   . HIS C  1 108 ? -4.067  -10.121 -4.319  1.00 34.64 ? 125  HIS C N   1 
ATOM   9719  C  CA  . HIS C  1 108 ? -2.711  -9.714  -3.976  1.00 33.33 ? 125  HIS C CA  1 
ATOM   9720  C  C   . HIS C  1 108 ? -1.986  -10.865 -3.280  1.00 31.22 ? 125  HIS C C   1 
ATOM   9721  O  O   . HIS C  1 108 ? -2.621  -11.683 -2.620  1.00 32.78 ? 125  HIS C O   1 
ATOM   9722  C  CB  . HIS C  1 108 ? -2.743  -8.447  -3.111  1.00 32.72 ? 125  HIS C CB  1 
ATOM   9723  C  CG  . HIS C  1 108 ? -1.401  -7.872  -2.793  1.00 32.40 ? 125  HIS C CG  1 
ATOM   9724  N  ND1 . HIS C  1 108 ? -0.664  -7.155  -3.709  1.00 32.04 ? 125  HIS C ND1 1 
ATOM   9725  C  CD2 . HIS C  1 108 ? -0.665  -7.904  -1.674  1.00 32.19 ? 125  HIS C CD2 1 
ATOM   9726  C  CE1 . HIS C  1 108 ? 0.478   -6.773  -3.153  1.00 32.31 ? 125  HIS C CE1 1 
ATOM   9727  N  NE2 . HIS C  1 108 ? 0.496   -7.217  -1.916  1.00 32.29 ? 125  HIS C NE2 1 
ATOM   9728  N  N   . ILE C  1 109 ? -0.659  -10.926 -3.461  1.00 30.24 ? 126  ILE C N   1 
ATOM   9729  C  CA  . ILE C  1 109 ? 0.198   -11.816 -2.691  1.00 29.91 ? 126  ILE C CA  1 
ATOM   9730  C  C   . ILE C  1 109 ? 1.080   -10.957 -1.785  1.00 28.31 ? 126  ILE C C   1 
ATOM   9731  O  O   . ILE C  1 109 ? 1.912   -10.194 -2.271  1.00 29.12 ? 126  ILE C O   1 
ATOM   9732  C  CB  . ILE C  1 109 ? 1.033   -12.725 -3.611  1.00 31.64 ? 126  ILE C CB  1 
ATOM   9733  C  CG1 . ILE C  1 109 ? 0.133   -13.633 -4.448  1.00 34.37 ? 126  ILE C CG1 1 
ATOM   9734  C  CG2 . ILE C  1 109 ? 2.058   -13.529 -2.806  1.00 30.93 ? 126  ILE C CG2 1 
ATOM   9735  C  CD1 . ILE C  1 109 ? 0.874   -14.470 -5.476  1.00 36.86 ? 126  ILE C CD1 1 
ATOM   9736  N  N   . PHE C  1 110 ? 0.904   -11.117 -0.469  1.00 26.06 ? 127  PHE C N   1 
ATOM   9737  C  CA  . PHE C  1 110 ? 1.490   -10.211 0.505   1.00 26.41 ? 127  PHE C CA  1 
ATOM   9738  C  C   . PHE C  1 110 ? 2.928   -10.597 0.823   1.00 26.67 ? 127  PHE C C   1 
ATOM   9739  O  O   . PHE C  1 110 ? 3.256   -11.777 0.961   1.00 26.57 ? 127  PHE C O   1 
ATOM   9740  C  CB  . PHE C  1 110 ? 0.675   -10.193 1.800   1.00 25.88 ? 127  PHE C CB  1 
ATOM   9741  C  CG  . PHE C  1 110 ? -0.586  -9.358  1.662   1.00 26.16 ? 127  PHE C CG  1 
ATOM   9742  C  CD1 . PHE C  1 110 ? -1.747  -9.906  1.129   1.00 25.96 ? 127  PHE C CD1 1 
ATOM   9743  C  CD2 . PHE C  1 110 ? -0.591  -8.016  2.029   1.00 26.55 ? 127  PHE C CD2 1 
ATOM   9744  C  CE1 . PHE C  1 110 ? -2.888  -9.131  0.977   1.00 25.98 ? 127  PHE C CE1 1 
ATOM   9745  C  CE2 . PHE C  1 110 ? -1.736  -7.249  1.882   1.00 26.02 ? 127  PHE C CE2 1 
ATOM   9746  C  CZ  . PHE C  1 110 ? -2.878  -7.807  1.355   1.00 25.81 ? 127  PHE C CZ  1 
ATOM   9747  N  N   . ARG C  1 111 ? 3.766   -9.565  0.939   1.00 27.03 ? 128  ARG C N   1 
ATOM   9748  C  CA  . ARG C  1 111 ? 4.998   -9.644  1.704   1.00 27.40 ? 128  ARG C CA  1 
ATOM   9749  C  C   . ARG C  1 111 ? 4.985   -8.470  2.677   1.00 27.31 ? 128  ARG C C   1 
ATOM   9750  O  O   . ARG C  1 111 ? 4.641   -8.629  3.845   1.00 27.29 ? 128  ARG C O   1 
ATOM   9751  C  CB  . ARG C  1 111 ? 6.234   -9.683  0.794   1.00 27.60 ? 128  ARG C CB  1 
ATOM   9752  C  CG  . ARG C  1 111 ? 7.536   -9.867  1.563   1.00 28.78 ? 128  ARG C CG  1 
ATOM   9753  C  CD  . ARG C  1 111 ? 8.770   -9.722  0.673   1.00 29.64 ? 128  ARG C CD  1 
ATOM   9754  N  NE  . ARG C  1 111 ? 9.100   -8.323  0.377   1.00 30.84 ? 128  ARG C NE  1 
ATOM   9755  C  CZ  . ARG C  1 111 ? 9.751   -7.473  1.172   1.00 30.21 ? 128  ARG C CZ  1 
ATOM   9756  N  NH1 . ARG C  1 111 ? 10.252  -7.864  2.330   1.00 31.06 ? 128  ARG C NH1 1 
ATOM   9757  N  NH2 . ARG C  1 111 ? 9.933   -6.225  0.782   1.00 31.17 ? 128  ARG C NH2 1 
ATOM   9758  N  N   . ARG C  1 112 ? 5.329   -7.286  2.167   1.00 28.58 ? 129  ARG C N   1 
ATOM   9759  C  CA  . ARG C  1 112 ? 5.293   -6.063  2.950   1.00 30.93 ? 129  ARG C CA  1 
ATOM   9760  C  C   . ARG C  1 112 ? 3.834   -5.645  3.136   1.00 29.32 ? 129  ARG C C   1 
ATOM   9761  O  O   . ARG C  1 112 ? 3.020   -5.832  2.234   1.00 29.33 ? 129  ARG C O   1 
ATOM   9762  C  CB  . ARG C  1 112 ? 6.140   -5.046  2.175   1.00 35.84 ? 129  ARG C CB  1 
ATOM   9763  C  CG  . ARG C  1 112 ? 6.404   -3.695  2.819   1.00 41.06 ? 129  ARG C CG  1 
ATOM   9764  C  CD  . ARG C  1 112 ? 7.246   -2.847  1.874   1.00 43.09 ? 129  ARG C CD  1 
ATOM   9765  N  NE  . ARG C  1 112 ? 7.576   -1.524  2.417   1.00 46.86 ? 129  ARG C NE  1 
ATOM   9766  C  CZ  . ARG C  1 112 ? 8.412   -1.286  3.427   1.00 49.53 ? 129  ARG C CZ  1 
ATOM   9767  N  NH1 . ARG C  1 112 ? 9.027   -2.279  4.050   1.00 47.21 ? 129  ARG C NH1 1 
ATOM   9768  N  NH2 . ARG C  1 112 ? 8.640   -0.038  3.806   1.00 53.06 ? 129  ARG C NH2 1 
ATOM   9769  N  N   . PRO C  1 113 ? 3.446   -5.105  4.313   1.00 28.81 ? 130  PRO C N   1 
ATOM   9770  C  CA  . PRO C  1 113 ? 2.113   -4.522  4.495   1.00 30.23 ? 130  PRO C CA  1 
ATOM   9771  C  C   . PRO C  1 113 ? 1.821   -3.421  3.475   1.00 31.20 ? 130  PRO C C   1 
ATOM   9772  O  O   . PRO C  1 113 ? 2.731   -2.706  3.075   1.00 30.86 ? 130  PRO C O   1 
ATOM   9773  C  CB  . PRO C  1 113 ? 2.131   -3.959  5.929   1.00 29.57 ? 130  PRO C CB  1 
ATOM   9774  C  CG  . PRO C  1 113 ? 3.280   -4.661  6.619   1.00 29.38 ? 130  PRO C CG  1 
ATOM   9775  C  CD  . PRO C  1 113 ? 4.261   -5.059  5.534   1.00 28.24 ? 130  PRO C CD  1 
ATOM   9776  N  N   . LYS C  1 114 ? 0.548   -3.298  3.076   1.00 34.35 ? 131  LYS C N   1 
ATOM   9777  C  CA  A LYS C  1 114 ? 0.070   -2.253  2.183   0.50 35.20 ? 131  LYS C CA  1 
ATOM   9778  C  CA  B LYS C  1 114 ? 0.137   -2.220  2.188   0.50 35.78 ? 131  LYS C CA  1 
ATOM   9779  C  C   . LYS C  1 114 ? -0.490  -1.090  3.002   1.00 34.30 ? 131  LYS C C   1 
ATOM   9780  O  O   . LYS C  1 114 ? -0.624  0.025   2.502   1.00 34.95 ? 131  LYS C O   1 
ATOM   9781  C  CB  A LYS C  1 114 ? -1.074  -2.788  1.311   0.50 36.66 ? 131  LYS C CB  1 
ATOM   9782  C  CB  B LYS C  1 114 ? -0.791  -2.705  1.068   0.50 38.16 ? 131  LYS C CB  1 
ATOM   9783  C  CG  A LYS C  1 114 ? -0.804  -4.073  0.537   0.50 37.70 ? 131  LYS C CG  1 
ATOM   9784  C  CG  B LYS C  1 114 ? -0.077  -3.487  -0.026  0.50 39.89 ? 131  LYS C CG  1 
ATOM   9785  C  CD  A LYS C  1 114 ? 0.130   -3.908  -0.655  0.50 38.28 ? 131  LYS C CD  1 
ATOM   9786  C  CD  B LYS C  1 114 ? 1.276   -2.898  -0.414  0.50 40.96 ? 131  LYS C CD  1 
ATOM   9787  C  CE  A LYS C  1 114 ? -0.475  -3.113  -1.764  0.50 38.17 ? 131  LYS C CE  1 
ATOM   9788  C  CE  B LYS C  1 114 ? 1.180   -1.594  -1.142  0.50 41.65 ? 131  LYS C CE  1 
ATOM   9789  N  NZ  A LYS C  1 114 ? 0.428   -3.069  -2.916  0.50 38.54 ? 131  LYS C NZ  1 
ATOM   9790  N  NZ  B LYS C  1 114 ? 0.613   -1.770  -2.481  0.50 42.55 ? 131  LYS C NZ  1 
ATOM   9791  N  N   . GLY C  1 115 ? -0.838  -1.382  4.260   1.00 30.96 ? 132  GLY C N   1 
ATOM   9792  C  CA  . GLY C  1 115 ? -1.554  -0.463  5.131   1.00 28.68 ? 132  GLY C CA  1 
ATOM   9793  C  C   . GLY C  1 115 ? -2.283  -1.257  6.212   1.00 26.38 ? 132  GLY C C   1 
ATOM   9794  O  O   . GLY C  1 115 ? -2.088  -2.462  6.311   1.00 25.80 ? 132  GLY C O   1 
ATOM   9795  N  N   . LEU C  1 116 ? -3.115  -0.580  7.008   1.00 23.18 ? 133  LEU C N   1 
ATOM   9796  C  CA  . LEU C  1 116 ? -3.802  -1.218  8.116   1.00 22.77 ? 133  LEU C CA  1 
ATOM   9797  C  C   . LEU C  1 116 ? -5.186  -1.666  7.668   1.00 21.48 ? 133  LEU C C   1 
ATOM   9798  O  O   . LEU C  1 116 ? -5.907  -0.898  7.026   1.00 20.82 ? 133  LEU C O   1 
ATOM   9799  C  CB  . LEU C  1 116 ? -3.928  -0.285  9.317   1.00 23.10 ? 133  LEU C CB  1 
ATOM   9800  C  CG  . LEU C  1 116 ? -2.684  -0.079  10.181  1.00 23.16 ? 133  LEU C CG  1 
ATOM   9801  C  CD1 . LEU C  1 116 ? -3.078  0.837   11.327  1.00 23.69 ? 133  LEU C CD1 1 
ATOM   9802  C  CD2 . LEU C  1 116 ? -2.078  -1.359  10.705  1.00 22.59 ? 133  LEU C CD2 1 
ATOM   9803  N  N   . PHE C  1 117 ? -5.534  -2.901  8.046   1.00 20.69 ? 134  PHE C N   1 
ATOM   9804  C  CA  . PHE C  1 117 ? -6.889  -3.423  7.969   1.00 20.79 ? 134  PHE C CA  1 
ATOM   9805  C  C   . PHE C  1 117 ? -7.483  -3.495  9.373   1.00 21.61 ? 134  PHE C C   1 
ATOM   9806  O  O   . PHE C  1 117 ? -6.961  -4.198  10.239  1.00 21.79 ? 134  PHE C O   1 
ATOM   9807  C  CB  . PHE C  1 117 ? -6.896  -4.816  7.333   1.00 21.40 ? 134  PHE C CB  1 
ATOM   9808  C  CG  . PHE C  1 117 ? -6.456  -4.830  5.880   1.00 22.14 ? 134  PHE C CG  1 
ATOM   9809  C  CD1 . PHE C  1 117 ? -7.382  -4.661  4.860   1.00 22.30 ? 134  PHE C CD1 1 
ATOM   9810  C  CD2 . PHE C  1 117 ? -5.116  -4.991  5.542   1.00 23.16 ? 134  PHE C CD2 1 
ATOM   9811  C  CE1 . PHE C  1 117 ? -6.981  -4.664  3.538   1.00 23.67 ? 134  PHE C CE1 1 
ATOM   9812  C  CE2 . PHE C  1 117 ? -4.724  -5.001  4.213   1.00 23.89 ? 134  PHE C CE2 1 
ATOM   9813  C  CZ  . PHE C  1 117 ? -5.654  -4.827  3.216   1.00 23.48 ? 134  PHE C CZ  1 
ATOM   9814  N  N   . ILE C  1 118 ? -8.583  -2.761  9.587   1.00 20.80 ? 135  ILE C N   1 
ATOM   9815  C  CA  . ILE C  1 118 ? -9.285  -2.748  10.856  1.00 21.82 ? 135  ILE C CA  1 
ATOM   9816  C  C   . ILE C  1 118 ? -10.700 -3.272  10.621  1.00 22.14 ? 135  ILE C C   1 
ATOM   9817  O  O   . ILE C  1 118 ? -11.489 -2.612  9.949   1.00 22.83 ? 135  ILE C O   1 
ATOM   9818  C  CB  . ILE C  1 118 ? -9.294  -1.326  11.449  1.00 23.21 ? 135  ILE C CB  1 
ATOM   9819  C  CG1 . ILE C  1 118 ? -7.875  -0.827  11.745  1.00 23.01 ? 135  ILE C CG1 1 
ATOM   9820  C  CG2 . ILE C  1 118 ? -10.197 -1.241  12.685  1.00 22.77 ? 135  ILE C CG2 1 
ATOM   9821  C  CD1 . ILE C  1 118 ? -7.780  0.673   11.975  1.00 23.47 ? 135  ILE C CD1 1 
ATOM   9822  N  N   . SER C  1 119 ? -11.022 -4.433  11.204  1.00 22.29 ? 136  SER C N   1 
ATOM   9823  C  CA  . SER C  1 119 ? -12.318 -5.061  10.980  1.00 22.68 ? 136  SER C CA  1 
ATOM   9824  C  C   . SER C  1 119 ? -13.232 -4.874  12.190  1.00 22.20 ? 136  SER C C   1 
ATOM   9825  O  O   . SER C  1 119 ? -12.780 -4.595  13.299  1.00 22.40 ? 136  SER C O   1 
ATOM   9826  C  CB  . SER C  1 119 ? -12.178 -6.523  10.648  1.00 23.39 ? 136  SER C CB  1 
ATOM   9827  O  OG  . SER C  1 119 ? -12.055 -7.303  11.831  1.00 23.95 ? 136  SER C OG  1 
ATOM   9828  N  N   . ILE C  1 120 ? -14.535 -5.061  11.956  1.00 23.77 ? 137  ILE C N   1 
ATOM   9829  C  CA  . ILE C  1 120 ? -15.543 -4.965  13.001  1.00 24.18 ? 137  ILE C CA  1 
ATOM   9830  C  C   . ILE C  1 120 ? -15.289 -6.055  14.042  1.00 23.33 ? 137  ILE C C   1 
ATOM   9831  O  O   . ILE C  1 120 ? -15.606 -5.879  15.214  1.00 21.12 ? 137  ILE C O   1 
ATOM   9832  C  CB  . ILE C  1 120 ? -16.965 -5.019  12.394  1.00 25.76 ? 137  ILE C CB  1 
ATOM   9833  C  CG1 . ILE C  1 120 ? -18.063 -4.776  13.439  1.00 27.80 ? 137  ILE C CG1 1 
ATOM   9834  C  CG2 . ILE C  1 120 ? -17.208 -6.323  11.634  1.00 25.85 ? 137  ILE C CG2 1 
ATOM   9835  C  CD1 . ILE C  1 120 ? -18.083 -3.375  14.016  1.00 28.24 ? 137  ILE C CD1 1 
ATOM   9836  N  N   . SER C  1 121 ? -14.662 -7.158  13.614  1.00 24.47 ? 138  SER C N   1 
ATOM   9837  C  CA  . SER C  1 121 ? -14.304 -8.243  14.513  1.00 25.84 ? 138  SER C CA  1 
ATOM   9838  C  C   . SER C  1 121 ? -13.188 -7.826  15.471  1.00 25.65 ? 138  SER C C   1 
ATOM   9839  O  O   . SER C  1 121 ? -12.952 -8.514  16.462  1.00 26.43 ? 138  SER C O   1 
ATOM   9840  C  CB  . SER C  1 121 ? -13.929 -9.475  13.727  1.00 26.59 ? 138  SER C CB  1 
ATOM   9841  O  OG  . SER C  1 121 ? -15.036 -9.940  12.964  1.00 27.19 ? 138  SER C OG  1 
ATOM   9842  N  N   . ASP C  1 122 ? -12.511 -6.705  15.174  1.00 24.35 ? 139  ASP C N   1 
ATOM   9843  C  CA  . ASP C  1 122 ? -11.422 -6.197  15.995  1.00 24.27 ? 139  ASP C CA  1 
ATOM   9844  C  C   . ASP C  1 122 ? -11.897 -5.130  16.982  1.00 23.99 ? 139  ASP C C   1 
ATOM   9845  O  O   . ASP C  1 122 ? -11.080 -4.538  17.685  1.00 22.36 ? 139  ASP C O   1 
ATOM   9846  C  CB  . ASP C  1 122 ? -10.284 -5.674  15.129  1.00 24.78 ? 139  ASP C CB  1 
ATOM   9847  C  CG  . ASP C  1 122 ? -9.674  -6.704  14.193  1.00 24.86 ? 139  ASP C CG  1 
ATOM   9848  O  OD1 . ASP C  1 122 ? -9.184  -7.736  14.709  1.00 24.45 ? 139  ASP C OD1 1 
ATOM   9849  O  OD2 . ASP C  1 122 ? -9.719  -6.481  12.959  1.00 24.57 ? 139  ASP C OD2 1 
ATOM   9850  N  N   . ARG C  1 123 ? -13.214 -4.889  17.070  1.00 24.60 ? 140  ARG C N   1 
ATOM   9851  C  CA  . ARG C  1 123 ? -13.713 -3.854  17.959  1.00 25.70 ? 140  ARG C CA  1 
ATOM   9852  C  C   . ARG C  1 123 ? -13.209 -4.103  19.379  1.00 24.43 ? 140  ARG C C   1 
ATOM   9853  O  O   . ARG C  1 123 ? -13.183 -5.237  19.849  1.00 25.09 ? 140  ARG C O   1 
ATOM   9854  C  CB  . ARG C  1 123 ? -15.240 -3.727  17.932  1.00 29.40 ? 140  ARG C CB  1 
ATOM   9855  C  CG  . ARG C  1 123 ? -16.007 -4.940  18.434  1.00 32.79 ? 140  ARG C CG  1 
ATOM   9856  C  CD  . ARG C  1 123 ? -17.494 -4.725  18.182  1.00 37.90 ? 140  ARG C CD  1 
ATOM   9857  N  NE  . ARG C  1 123 ? -18.306 -5.890  18.551  1.00 41.52 ? 140  ARG C NE  1 
ATOM   9858  C  CZ  . ARG C  1 123 ? -18.365 -7.046  17.885  1.00 45.34 ? 140  ARG C CZ  1 
ATOM   9859  N  NH1 . ARG C  1 123 ? -17.669 -7.232  16.773  1.00 43.18 ? 140  ARG C NH1 1 
ATOM   9860  N  NH2 . ARG C  1 123 ? -19.135 -8.021  18.342  1.00 47.26 ? 140  ARG C NH2 1 
ATOM   9861  N  N   . GLY C  1 124 ? -12.799 -3.018  20.041  1.00 23.27 ? 141  GLY C N   1 
ATOM   9862  C  CA  . GLY C  1 124 ? -12.212 -3.070  21.368  1.00 23.98 ? 141  GLY C CA  1 
ATOM   9863  C  C   . GLY C  1 124 ? -10.695 -3.265  21.336  1.00 23.52 ? 141  GLY C C   1 
ATOM   9864  O  O   . GLY C  1 124 ? -10.051 -3.107  22.367  1.00 24.32 ? 141  GLY C O   1 
ATOM   9865  N  N   . HIS C  1 125 ? -10.126 -3.581  20.163  1.00 23.58 ? 142  HIS C N   1 
ATOM   9866  C  CA  . HIS C  1 125 ? -8.711  -3.916  20.065  1.00 23.77 ? 142  HIS C CA  1 
ATOM   9867  C  C   . HIS C  1 125 ? -8.025  -3.122  18.950  1.00 23.25 ? 142  HIS C C   1 
ATOM   9868  O  O   . HIS C  1 125 ? -6.960  -3.508  18.478  1.00 22.13 ? 142  HIS C O   1 
ATOM   9869  C  CB  . HIS C  1 125 ? -8.539  -5.424  19.850  1.00 24.56 ? 142  HIS C CB  1 
ATOM   9870  C  CG  . HIS C  1 125 ? -9.131  -6.277  20.927  1.00 25.47 ? 142  HIS C CG  1 
ATOM   9871  N  ND1 . HIS C  1 125 ? -8.491  -6.530  22.122  1.00 26.61 ? 142  HIS C ND1 1 
ATOM   9872  C  CD2 . HIS C  1 125 ? -10.308 -6.923  20.994  1.00 26.46 ? 142  HIS C CD2 1 
ATOM   9873  C  CE1 . HIS C  1 125 ? -9.262  -7.303  22.879  1.00 27.09 ? 142  HIS C CE1 1 
ATOM   9874  N  NE2 . HIS C  1 125 ? -10.372 -7.556  22.210  1.00 26.87 ? 142  HIS C NE2 1 
ATOM   9875  N  N   . VAL C  1 126 ? -8.600  -1.979  18.563  1.00 22.96 ? 143  VAL C N   1 
ATOM   9876  C  CA  . VAL C  1 126 ? -8.092  -1.221  17.428  1.00 23.30 ? 143  VAL C CA  1 
ATOM   9877  C  C   . VAL C  1 126 ? -6.716  -0.634  17.747  1.00 23.18 ? 143  VAL C C   1 
ATOM   9878  O  O   . VAL C  1 126 ? -5.860  -0.598  16.868  1.00 22.40 ? 143  VAL C O   1 
ATOM   9879  C  CB  . VAL C  1 126 ? -9.097  -0.136  16.999  1.00 23.53 ? 143  VAL C CB  1 
ATOM   9880  C  CG1 . VAL C  1 126 ? -8.517  0.819   15.962  1.00 23.23 ? 143  VAL C CG1 1 
ATOM   9881  C  CG2 . VAL C  1 126 ? -10.385 -0.765  16.479  1.00 24.35 ? 143  VAL C CG2 1 
ATOM   9882  N  N   . ARG C  1 127 ? -6.494  -0.184  18.991  1.00 23.28 ? 144  ARG C N   1 
ATOM   9883  C  CA  . ARG C  1 127 ? -5.219  0.426   19.348  1.00 25.26 ? 144  ARG C CA  1 
ATOM   9884  C  C   . ARG C  1 127 ? -4.074  -0.566  19.129  1.00 24.00 ? 144  ARG C C   1 
ATOM   9885  O  O   . ARG C  1 127 ? -2.992  -0.171  18.695  1.00 21.50 ? 144  ARG C O   1 
ATOM   9886  C  CB  . ARG C  1 127 ? -5.189  0.972   20.783  1.00 27.51 ? 144  ARG C CB  1 
ATOM   9887  C  CG  . ARG C  1 127 ? -3.879  1.648   21.178  1.00 29.24 ? 144  ARG C CG  1 
ATOM   9888  C  CD  . ARG C  1 127 ? -3.518  2.825   20.267  1.00 32.08 ? 144  ARG C CD  1 
ATOM   9889  N  NE  . ARG C  1 127 ? -2.164  3.352   20.479  1.00 34.05 ? 144  ARG C NE  1 
ATOM   9890  C  CZ  . ARG C  1 127 ? -1.749  4.082   21.512  1.00 35.58 ? 144  ARG C CZ  1 
ATOM   9891  N  NH1 . ARG C  1 127 ? -2.582  4.424   22.479  1.00 37.31 ? 144  ARG C NH1 1 
ATOM   9892  N  NH2 . ARG C  1 127 ? -0.489  4.480   21.564  1.00 37.19 ? 144  ARG C NH2 1 
ATOM   9893  N  N   . SER C  1 128 ? -4.319  -1.849  19.427  1.00 23.94 ? 145  SER C N   1 
ATOM   9894  C  CA  . SER C  1 128 ? -3.324  -2.894  19.241  1.00 25.93 ? 145  SER C CA  1 
ATOM   9895  C  C   . SER C  1 128 ? -2.940  -3.032  17.769  1.00 24.26 ? 145  SER C C   1 
ATOM   9896  O  O   . SER C  1 128 ? -1.779  -3.293  17.458  1.00 22.99 ? 145  SER C O   1 
ATOM   9897  C  CB  . SER C  1 128 ? -3.810  -4.208  19.793  1.00 29.18 ? 145  SER C CB  1 
ATOM   9898  O  OG  . SER C  1 128 ? -4.017  -4.090  21.190  1.00 32.86 ? 145  SER C OG  1 
ATOM   9899  N  N   . ILE C  1 129 ? -3.913  -2.838  16.868  1.00 22.62 ? 146  ILE C N   1 
ATOM   9900  C  CA  . ILE C  1 129 ? -3.652  -2.905  15.439  1.00 22.62 ? 146  ILE C CA  1 
ATOM   9901  C  C   . ILE C  1 129 ? -2.829  -1.693  15.004  1.00 22.55 ? 146  ILE C C   1 
ATOM   9902  O  O   . ILE C  1 129 ? -1.867  -1.833  14.252  1.00 22.46 ? 146  ILE C O   1 
ATOM   9903  C  CB  . ILE C  1 129 ? -4.962  -3.051  14.641  1.00 22.42 ? 146  ILE C CB  1 
ATOM   9904  C  CG1 . ILE C  1 129 ? -5.538  -4.464  14.812  1.00 23.02 ? 146  ILE C CG1 1 
ATOM   9905  C  CG2 . ILE C  1 129 ? -4.753  -2.699  13.168  1.00 22.51 ? 146  ILE C CG2 1 
ATOM   9906  C  CD1 . ILE C  1 129 ? -6.929  -4.657  14.241  1.00 23.46 ? 146  ILE C CD1 1 
ATOM   9907  N  N   . VAL C  1 130 ? -3.203  -0.501  15.479  1.00 22.78 ? 147  VAL C N   1 
ATOM   9908  C  CA  . VAL C  1 130 ? -2.479  0.712   15.130  1.00 22.48 ? 147  VAL C CA  1 
ATOM   9909  C  C   . VAL C  1 130 ? -1.022  0.608   15.596  1.00 23.06 ? 147  VAL C C   1 
ATOM   9910  O  O   . VAL C  1 130 ? -0.113  1.060   14.901  1.00 21.77 ? 147  VAL C O   1 
ATOM   9911  C  CB  . VAL C  1 130 ? -3.201  1.941   15.714  1.00 22.44 ? 147  VAL C CB  1 
ATOM   9912  C  CG1 . VAL C  1 130 ? -2.355  3.208   15.627  1.00 22.35 ? 147  VAL C CG1 1 
ATOM   9913  C  CG2 . VAL C  1 130 ? -4.553  2.148   15.036  1.00 21.79 ? 147  VAL C CG2 1 
ATOM   9914  N  N   . ASP C  1 131 ? -0.811  -0.001  16.769  1.00 24.08 ? 148  ASP C N   1 
ATOM   9915  C  CA  . ASP C  1 131 ? 0.516   -0.160  17.349  1.00 24.28 ? 148  ASP C CA  1 
ATOM   9916  C  C   . ASP C  1 131 ? 1.366   -1.165  16.568  1.00 23.87 ? 148  ASP C C   1 
ATOM   9917  O  O   . ASP C  1 131 ? 2.583   -1.189  16.753  1.00 24.34 ? 148  ASP C O   1 
ATOM   9918  C  CB  . ASP C  1 131 ? 0.435   -0.554  18.816  1.00 25.29 ? 148  ASP C CB  1 
ATOM   9919  C  CG  . ASP C  1 131 ? 0.072   0.555   19.793  1.00 26.60 ? 148  ASP C CG  1 
ATOM   9920  O  OD1 . ASP C  1 131 ? 0.054   1.741   19.395  1.00 27.52 ? 148  ASP C OD1 1 
ATOM   9921  O  OD2 . ASP C  1 131 ? -0.198  0.217   20.952  1.00 29.59 ? 148  ASP C OD2 1 
ATOM   9922  N  N   . ASN C  1 132 ? 0.743   -1.982  15.704  1.00 22.18 ? 149  ASN C N   1 
ATOM   9923  C  CA  . ASN C  1 132 ? 1.478   -2.900  14.847  1.00 21.74 ? 149  ASN C CA  1 
ATOM   9924  C  C   . ASN C  1 132 ? 2.037   -2.222  13.596  1.00 21.65 ? 149  ASN C C   1 
ATOM   9925  O  O   . ASN C  1 132 ? 2.859   -2.820  12.907  1.00 21.64 ? 149  ASN C O   1 
ATOM   9926  C  CB  . ASN C  1 132 ? 0.630   -4.095  14.431  1.00 21.47 ? 149  ASN C CB  1 
ATOM   9927  C  CG  . ASN C  1 132 ? 0.476   -5.101  15.546  1.00 21.34 ? 149  ASN C CG  1 
ATOM   9928  O  OD1 . ASN C  1 132 ? 1.223   -5.067  16.530  1.00 21.76 ? 149  ASN C OD1 1 
ATOM   9929  N  ND2 . ASN C  1 132 ? -0.473  -6.011  15.400  1.00 21.53 ? 149  ASN C ND2 1 
ATOM   9930  N  N   . TRP C  1 133 ? 1.594   -1.003  13.273  1.00 21.04 ? 150  TRP C N   1 
ATOM   9931  C  CA  . TRP C  1 133 ? 2.150   -0.311  12.122  1.00 21.14 ? 150  TRP C CA  1 
ATOM   9932  C  C   . TRP C  1 133 ? 3.619   0.029   12.388  1.00 21.96 ? 150  TRP C C   1 
ATOM   9933  O  O   . TRP C  1 133 ? 3.948   0.610   13.419  1.00 21.03 ? 150  TRP C O   1 
ATOM   9934  C  CB  . TRP C  1 133 ? 1.339   0.945   11.769  1.00 20.94 ? 150  TRP C CB  1 
ATOM   9935  C  CG  . TRP C  1 133 ? 1.749   1.555   10.455  1.00 20.79 ? 150  TRP C CG  1 
ATOM   9936  C  CD1 . TRP C  1 133 ? 2.352   2.760   10.251  1.00 21.27 ? 150  TRP C CD1 1 
ATOM   9937  C  CD2 . TRP C  1 133 ? 1.622   0.948   9.152   1.00 21.58 ? 150  TRP C CD2 1 
ATOM   9938  N  NE1 . TRP C  1 133 ? 2.591   2.957   8.918   1.00 21.32 ? 150  TRP C NE1 1 
ATOM   9939  C  CE2 . TRP C  1 133 ? 2.155   1.863   8.220   1.00 22.07 ? 150  TRP C CE2 1 
ATOM   9940  C  CE3 . TRP C  1 133 ? 1.100   -0.261  8.685   1.00 22.57 ? 150  TRP C CE3 1 
ATOM   9941  C  CZ2 . TRP C  1 133 ? 2.188   1.598   6.856   1.00 22.79 ? 150  TRP C CZ2 1 
ATOM   9942  C  CZ3 . TRP C  1 133 ? 1.125   -0.519  7.334   1.00 23.18 ? 150  TRP C CZ3 1 
ATOM   9943  C  CH2 . TRP C  1 133 ? 1.668   0.397   6.433   1.00 23.70 ? 150  TRP C CH2 1 
ATOM   9944  N  N   . PRO C  1 134 ? 4.558   -0.326  11.484  1.00 23.71 ? 151  PRO C N   1 
ATOM   9945  C  CA  . PRO C  1 134 ? 5.991   -0.166  11.762  1.00 25.43 ? 151  PRO C CA  1 
ATOM   9946  C  C   . PRO C  1 134 ? 6.521   1.265   11.883  1.00 26.93 ? 151  PRO C C   1 
ATOM   9947  O  O   . PRO C  1 134 ? 7.518   1.482   12.564  1.00 28.99 ? 151  PRO C O   1 
ATOM   9948  C  CB  . PRO C  1 134 ? 6.668   -0.917  10.592  1.00 25.71 ? 151  PRO C CB  1 
ATOM   9949  C  CG  . PRO C  1 134 ? 5.581   -1.758  9.990   1.00 26.33 ? 151  PRO C CG  1 
ATOM   9950  C  CD  . PRO C  1 134 ? 4.306   -0.961  10.185  1.00 24.80 ? 151  PRO C CD  1 
ATOM   9951  N  N   . GLU C  1 135 ? 5.851   2.237   11.248  1.00 27.04 ? 152  GLU C N   1 
ATOM   9952  C  CA  . GLU C  1 135 ? 6.325   3.616   11.217  1.00 27.97 ? 152  GLU C CA  1 
ATOM   9953  C  C   . GLU C  1 135 ? 5.782   4.399   12.408  1.00 27.50 ? 152  GLU C C   1 
ATOM   9954  O  O   . GLU C  1 135 ? 4.611   4.254   12.768  1.00 25.77 ? 152  GLU C O   1 
ATOM   9955  C  CB  . GLU C  1 135 ? 5.897   4.306   9.922   1.00 29.40 ? 152  GLU C CB  1 
ATOM   9956  C  CG  . GLU C  1 135 ? 6.308   3.545   8.664   1.00 33.19 ? 152  GLU C CG  1 
ATOM   9957  C  CD  . GLU C  1 135 ? 7.800   3.341   8.481   1.00 36.05 ? 152  GLU C CD  1 
ATOM   9958  O  OE1 . GLU C  1 135 ? 8.597   4.102   9.069   1.00 38.55 ? 152  GLU C OE1 1 
ATOM   9959  O  OE2 . GLU C  1 135 ? 8.160   2.392   7.756   1.00 40.42 ? 152  GLU C OE2 1 
ATOM   9960  N  N   . ASN C  1 136 ? 6.623   5.285   12.967  1.00 26.85 ? 153  ASN C N   1 
ATOM   9961  C  CA  . ASN C  1 136 ? 6.316   5.949   14.225  1.00 29.12 ? 153  ASN C CA  1 
ATOM   9962  C  C   . ASN C  1 136 ? 5.838   7.391   14.048  1.00 27.00 ? 153  ASN C C   1 
ATOM   9963  O  O   . ASN C  1 136 ? 5.397   7.982   15.033  1.00 25.77 ? 153  ASN C O   1 
ATOM   9964  C  CB  . ASN C  1 136 ? 7.513   5.976   15.170  1.00 31.95 ? 153  ASN C CB  1 
ATOM   9965  C  CG  . ASN C  1 136 ? 7.931   4.594   15.608  1.00 36.91 ? 153  ASN C CG  1 
ATOM   9966  O  OD1 . ASN C  1 136 ? 7.121   3.858   16.184  1.00 38.51 ? 153  ASN C OD1 1 
ATOM   9967  N  ND2 . ASN C  1 136 ? 9.183   4.232   15.363  1.00 39.32 ? 153  ASN C ND2 1 
ATOM   9968  N  N   . HIS C  1 137 ? 5.915   7.951   12.831  1.00 25.87 ? 154  HIS C N   1 
ATOM   9969  C  CA  . HIS C  1 137 ? 5.692   9.381   12.638  1.00 26.89 ? 154  HIS C CA  1 
ATOM   9970  C  C   . HIS C  1 137 ? 4.692   9.672   11.523  1.00 25.77 ? 154  HIS C C   1 
ATOM   9971  O  O   . HIS C  1 137 ? 4.910   10.554  10.686  1.00 28.80 ? 154  HIS C O   1 
ATOM   9972  C  CB  . HIS C  1 137 ? 7.010   10.111  12.352  1.00 28.81 ? 154  HIS C CB  1 
ATOM   9973  C  CG  . HIS C  1 137 ? 7.995   9.963   13.454  1.00 31.36 ? 154  HIS C CG  1 
ATOM   9974  N  ND1 . HIS C  1 137 ? 7.810   10.513  14.704  1.00 32.51 ? 154  HIS C ND1 1 
ATOM   9975  C  CD2 . HIS C  1 137 ? 9.154   9.296   13.502  1.00 32.51 ? 154  HIS C CD2 1 
ATOM   9976  C  CE1 . HIS C  1 137 ? 8.843   10.196  15.473  1.00 32.92 ? 154  HIS C CE1 1 
ATOM   9977  N  NE2 . HIS C  1 137 ? 9.673   9.467   14.758  1.00 32.69 ? 154  HIS C NE2 1 
ATOM   9978  N  N   . VAL C  1 138 ? 3.544   8.997   11.576  1.00 22.33 ? 155  VAL C N   1 
ATOM   9979  C  CA  . VAL C  1 138 ? 2.523   9.166   10.561  1.00 20.19 ? 155  VAL C CA  1 
ATOM   9980  C  C   . VAL C  1 138 ? 1.960   10.585  10.619  1.00 20.21 ? 155  VAL C C   1 
ATOM   9981  O  O   . VAL C  1 138 ? 1.667   11.087  11.703  1.00 20.82 ? 155  VAL C O   1 
ATOM   9982  C  CB  . VAL C  1 138 ? 1.438   8.096   10.762  1.00 19.14 ? 155  VAL C CB  1 
ATOM   9983  C  CG1 . VAL C  1 138 ? 0.188   8.394   9.946   1.00 18.65 ? 155  VAL C CG1 1 
ATOM   9984  C  CG2 . VAL C  1 138 ? 1.990   6.711   10.449  1.00 18.74 ? 155  VAL C CG2 1 
ATOM   9985  N  N   . LYS C  1 139 ? 1.811   11.203  9.439   1.00 19.59 ? 156  LYS C N   1 
ATOM   9986  C  CA  . LYS C  1 139 ? 1.275   12.548  9.308   1.00 20.14 ? 156  LYS C CA  1 
ATOM   9987  C  C   . LYS C  1 139 ? 0.005   12.565  8.455   1.00 20.03 ? 156  LYS C C   1 
ATOM   9988  O  O   . LYS C  1 139 ? -0.821  13.466  8.624   1.00 20.16 ? 156  LYS C O   1 
ATOM   9989  C  CB  . LYS C  1 139 ? 2.314   13.503  8.705   1.00 21.01 ? 156  LYS C CB  1 
ATOM   9990  C  CG  . LYS C  1 139 ? 3.566   13.761  9.543   1.00 22.13 ? 156  LYS C CG  1 
ATOM   9991  C  CD  . LYS C  1 139 ? 3.332   14.252  10.966  1.00 23.74 ? 156  LYS C CD  1 
ATOM   9992  C  CE  . LYS C  1 139 ? 2.463   15.465  11.019  1.00 25.53 ? 156  LYS C CE  1 
ATOM   9993  N  NZ  . LYS C  1 139 ? 2.194   15.887  12.397  1.00 26.46 ? 156  LYS C NZ  1 
ATOM   9994  N  N   . ALA C  1 140 ? -0.132  11.605  7.522   1.00 19.57 ? 157  ALA C N   1 
ATOM   9995  C  CA  . ALA C  1 140 ? -1.261  11.569  6.601   1.00 19.93 ? 157  ALA C CA  1 
ATOM   9996  C  C   . ALA C  1 140 ? -1.892  10.180  6.591   1.00 19.30 ? 157  ALA C C   1 
ATOM   9997  O  O   . ALA C  1 140 ? -1.231  9.198   6.251   1.00 18.77 ? 157  ALA C O   1 
ATOM   9998  C  CB  . ALA C  1 140 ? -0.824  11.960  5.208   1.00 19.71 ? 157  ALA C CB  1 
ATOM   9999  N  N   . VAL C  1 141 ? -3.178  10.124  6.959   1.00 18.68 ? 158  VAL C N   1 
ATOM   10000 C  CA  . VAL C  1 141 ? -3.979  8.909   6.891   1.00 18.67 ? 158  VAL C CA  1 
ATOM   10001 C  C   . VAL C  1 141 ? -5.073  9.090   5.841   1.00 18.25 ? 158  VAL C C   1 
ATOM   10002 O  O   . VAL C  1 141 ? -5.782  10.101  5.853   1.00 18.18 ? 158  VAL C O   1 
ATOM   10003 C  CB  . VAL C  1 141 ? -4.616  8.579   8.253   1.00 18.90 ? 158  VAL C CB  1 
ATOM   10004 C  CG1 . VAL C  1 141 ? -5.487  7.330   8.168   1.00 19.16 ? 158  VAL C CG1 1 
ATOM   10005 C  CG2 . VAL C  1 141 ? -3.584  8.453   9.363   1.00 19.30 ? 158  VAL C CG2 1 
ATOM   10006 N  N   . VAL C  1 142 ? -5.211  8.107   4.939   1.00 18.14 ? 159  VAL C N   1 
ATOM   10007 C  CA  . VAL C  1 142 ? -6.379  8.014   4.072   1.00 18.44 ? 159  VAL C CA  1 
ATOM   10008 C  C   . VAL C  1 142 ? -7.129  6.730   4.422   1.00 18.51 ? 159  VAL C C   1 
ATOM   10009 O  O   . VAL C  1 142 ? -6.529  5.661   4.476   1.00 18.08 ? 159  VAL C O   1 
ATOM   10010 C  CB  . VAL C  1 142 ? -6.025  8.070   2.574   1.00 18.92 ? 159  VAL C CB  1 
ATOM   10011 C  CG1 . VAL C  1 142 ? -7.244  7.850   1.684   1.00 19.88 ? 159  VAL C CG1 1 
ATOM   10012 C  CG2 . VAL C  1 142 ? -5.336  9.380   2.220   1.00 19.55 ? 159  VAL C CG2 1 
ATOM   10013 N  N   . VAL C  1 143 ? -8.442  6.854   4.673   1.00 18.13 ? 160  VAL C N   1 
ATOM   10014 C  CA  . VAL C  1 143 ? -9.253  5.743   5.145   1.00 18.45 ? 160  VAL C CA  1 
ATOM   10015 C  C   . VAL C  1 143 ? -10.493 5.592   4.264   1.00 19.19 ? 160  VAL C C   1 
ATOM   10016 O  O   . VAL C  1 143 ? -11.112 6.590   3.874   1.00 19.56 ? 160  VAL C O   1 
ATOM   10017 C  CB  . VAL C  1 143 ? -9.645  5.904   6.627   1.00 18.62 ? 160  VAL C CB  1 
ATOM   10018 C  CG1 . VAL C  1 143 ? -10.376 7.215   6.906   1.00 18.61 ? 160  VAL C CG1 1 
ATOM   10019 C  CG2 . VAL C  1 143 ? -10.464 4.718   7.125   1.00 18.66 ? 160  VAL C CG2 1 
ATOM   10020 N  N   . THR C  1 144 ? -10.841 4.325   3.993   1.00 19.65 ? 161  THR C N   1 
ATOM   10021 C  CA  . THR C  1 144 ? -12.072 3.940   3.311   1.00 20.59 ? 161  THR C CA  1 
ATOM   10022 C  C   . THR C  1 144 ? -12.693 2.737   4.019   1.00 20.88 ? 161  THR C C   1 
ATOM   10023 O  O   . THR C  1 144 ? -11.998 1.977   4.690   1.00 20.02 ? 161  THR C O   1 
ATOM   10024 C  CB  . THR C  1 144 ? -11.774 3.610   1.847   1.00 21.69 ? 161  THR C CB  1 
ATOM   10025 O  OG1 . THR C  1 144 ? -13.027 3.522   1.171   1.00 21.66 ? 161  THR C OG1 1 
ATOM   10026 C  CG2 . THR C  1 144 ? -10.996 2.316   1.683   1.00 22.26 ? 161  THR C CG2 1 
ATOM   10027 N  N   . ASP C  1 145 ? -14.009 2.561   3.830   1.00 21.02 ? 162  ASP C N   1 
ATOM   10028 C  CA  . ASP C  1 145 ? -14.692 1.325   4.190   1.00 21.12 ? 162  ASP C CA  1 
ATOM   10029 C  C   . ASP C  1 145 ? -15.122 0.565   2.934   1.00 21.02 ? 162  ASP C C   1 
ATOM   10030 O  O   . ASP C  1 145 ? -15.773 -0.475  3.035   1.00 21.28 ? 162  ASP C O   1 
ATOM   10031 C  CB  . ASP C  1 145 ? -15.863 1.585   5.124   1.00 21.30 ? 162  ASP C CB  1 
ATOM   10032 C  CG  . ASP C  1 145 ? -17.031 2.355   4.525   1.00 21.54 ? 162  ASP C CG  1 
ATOM   10033 O  OD1 . ASP C  1 145 ? -16.914 2.787   3.358   1.00 21.98 ? 162  ASP C OD1 1 
ATOM   10034 O  OD2 . ASP C  1 145 ? -18.052 2.514   5.232   1.00 22.83 ? 162  ASP C OD2 1 
ATOM   10035 N  N   . GLY C  1 146 ? -14.780 1.104   1.757   1.00 21.01 ? 163  GLY C N   1 
ATOM   10036 C  CA  . GLY C  1 146 ? -14.967 0.415   0.487   1.00 21.84 ? 163  GLY C CA  1 
ATOM   10037 C  C   . GLY C  1 146 ? -16.429 0.349   0.031   1.00 22.96 ? 163  GLY C C   1 
ATOM   10038 O  O   . GLY C  1 146 ? -16.753 -0.429  -0.867  1.00 22.78 ? 163  GLY C O   1 
ATOM   10039 N  N   . GLU C  1 147 ? -17.308 1.163   0.627   1.00 22.75 ? 164  GLU C N   1 
ATOM   10040 C  CA  . GLU C  1 147 ? -18.735 1.042   0.361   1.00 24.75 ? 164  GLU C CA  1 
ATOM   10041 C  C   . GLU C  1 147 ? -19.086 1.707   -0.972  1.00 25.80 ? 164  GLU C C   1 
ATOM   10042 O  O   . GLU C  1 147 ? -19.991 1.253   -1.670  1.00 25.56 ? 164  GLU C O   1 
ATOM   10043 C  CB  . GLU C  1 147 ? -19.603 1.612   1.485   1.00 25.88 ? 164  GLU C CB  1 
ATOM   10044 C  CG  . GLU C  1 147 ? -21.096 1.564   1.165   1.00 27.09 ? 164  GLU C CG  1 
ATOM   10045 C  CD  . GLU C  1 147 ? -22.041 1.523   2.351   1.00 29.18 ? 164  GLU C CD  1 
ATOM   10046 O  OE1 . GLU C  1 147 ? -21.748 2.158   3.388   1.00 28.97 ? 164  GLU C OE1 1 
ATOM   10047 O  OE2 . GLU C  1 147 ? -23.102 0.869   2.217   1.00 33.81 ? 164  GLU C OE2 1 
ATOM   10048 N  N   . ARG C  1 148 ? -18.385 2.793   -1.313  1.00 25.58 ? 165  ARG C N   1 
ATOM   10049 C  CA  . ARG C  1 148 ? -18.705 3.540   -2.516  1.00 28.00 ? 165  ARG C CA  1 
ATOM   10050 C  C   . ARG C  1 148 ? -17.422 3.863   -3.271  1.00 27.72 ? 165  ARG C C   1 
ATOM   10051 O  O   . ARG C  1 148 ? -17.030 5.023   -3.370  1.00 25.27 ? 165  ARG C O   1 
ATOM   10052 C  CB  . ARG C  1 148 ? -19.471 4.819   -2.158  1.00 29.53 ? 165  ARG C CB  1 
ATOM   10053 C  CG  . ARG C  1 148 ? -20.190 5.450   -3.341  1.00 32.80 ? 165  ARG C CG  1 
ATOM   10054 C  CD  . ARG C  1 148 ? -20.004 6.956   -3.368  1.00 35.85 ? 165  ARG C CD  1 
ATOM   10055 N  NE  . ARG C  1 148 ? -18.624 7.264   -3.762  1.00 41.44 ? 165  ARG C NE  1 
ATOM   10056 C  CZ  . ARG C  1 148 ? -17.992 8.433   -3.662  1.00 44.61 ? 165  ARG C CZ  1 
ATOM   10057 N  NH1 . ARG C  1 148 ? -18.578 9.479   -3.098  1.00 45.65 ? 165  ARG C NH1 1 
ATOM   10058 N  NH2 . ARG C  1 148 ? -16.754 8.537   -4.121  1.00 44.11 ? 165  ARG C NH2 1 
ATOM   10059 N  N   . ILE C  1 149 ? -16.781 2.818   -3.804  1.00 30.30 ? 166  ILE C N   1 
ATOM   10060 C  CA  . ILE C  1 149 ? -15.616 2.993   -4.653  1.00 31.78 ? 166  ILE C CA  1 
ATOM   10061 C  C   . ILE C  1 149 ? -16.075 3.663   -5.942  1.00 33.73 ? 166  ILE C C   1 
ATOM   10062 O  O   . ILE C  1 149 ? -16.946 3.149   -6.644  1.00 33.41 ? 166  ILE C O   1 
ATOM   10063 C  CB  . ILE C  1 149 ? -14.893 1.662   -4.931  1.00 31.55 ? 166  ILE C CB  1 
ATOM   10064 C  CG1 . ILE C  1 149 ? -14.438 0.965   -3.643  1.00 31.71 ? 166  ILE C CG1 1 
ATOM   10065 C  CG2 . ILE C  1 149 ? -13.731 1.870   -5.902  1.00 30.97 ? 166  ILE C CG2 1 
ATOM   10066 C  CD1 . ILE C  1 149 ? -13.511 1.787   -2.768  1.00 32.00 ? 166  ILE C CD1 1 
ATOM   10067 N  N   . LEU C  1 150 ? -15.464 4.815   -6.235  1.00 37.23 ? 167  LEU C N   1 
ATOM   10068 C  CA  . LEU C  1 150 ? -15.899 5.680   -7.318  1.00 42.13 ? 167  LEU C CA  1 
ATOM   10069 C  C   . LEU C  1 150 ? -15.967 4.882   -8.618  1.00 40.97 ? 167  LEU C C   1 
ATOM   10070 O  O   . LEU C  1 150 ? -14.942 4.437   -9.127  1.00 43.31 ? 167  LEU C O   1 
ATOM   10071 C  CB  . LEU C  1 150 ? -14.917 6.848   -7.404  1.00 46.15 ? 167  LEU C CB  1 
ATOM   10072 C  CG  . LEU C  1 150 ? -15.293 8.006   -8.335  1.00 48.56 ? 167  LEU C CG  1 
ATOM   10073 C  CD1 . LEU C  1 150 ? -16.638 8.637   -7.997  1.00 49.11 ? 167  LEU C CD1 1 
ATOM   10074 C  CD2 . LEU C  1 150 ? -14.179 9.042   -8.270  1.00 49.74 ? 167  LEU C CD2 1 
ATOM   10075 N  N   . GLY C  1 151 ? -17.194 4.664   -9.108  1.00 41.41 ? 168  GLY C N   1 
ATOM   10076 C  CA  . GLY C  1 151 ? -17.425 4.022   -10.391 1.00 40.06 ? 168  GLY C CA  1 
ATOM   10077 C  C   . GLY C  1 151 ? -17.727 2.527   -10.282 1.00 40.40 ? 168  GLY C C   1 
ATOM   10078 O  O   . GLY C  1 151 ? -18.002 1.895   -11.300 1.00 41.65 ? 168  GLY C O   1 
ATOM   10079 N  N   . LEU C  1 152 ? -17.673 1.959   -9.067  1.00 39.71 ? 169  LEU C N   1 
ATOM   10080 C  CA  . LEU C  1 152 ? -17.766 0.513   -8.896  1.00 38.44 ? 169  LEU C CA  1 
ATOM   10081 C  C   . LEU C  1 152 ? -18.717 0.117   -7.764  1.00 35.47 ? 169  LEU C C   1 
ATOM   10082 O  O   . LEU C  1 152 ? -19.190 -1.014  -7.736  1.00 36.46 ? 169  LEU C O   1 
ATOM   10083 C  CB  . LEU C  1 152 ? -16.363 -0.051  -8.668  1.00 39.75 ? 169  LEU C CB  1 
ATOM   10084 C  CG  . LEU C  1 152 ? -15.385 0.078   -9.843  1.00 41.42 ? 169  LEU C CG  1 
ATOM   10085 C  CD1 . LEU C  1 152 ? -13.977 -0.334  -9.445  1.00 41.49 ? 169  LEU C CD1 1 
ATOM   10086 C  CD2 . LEU C  1 152 ? -15.849 -0.744  -11.036 1.00 42.41 ? 169  LEU C CD2 1 
ATOM   10087 N  N   . GLY C  1 153 ? -18.993 1.028   -6.828  1.00 32.78 ? 170  GLY C N   1 
ATOM   10088 C  CA  . GLY C  1 153 ? -19.860 0.725   -5.703  1.00 31.56 ? 170  GLY C CA  1 
ATOM   10089 C  C   . GLY C  1 153 ? -19.112 -0.048  -4.619  1.00 29.74 ? 170  GLY C C   1 
ATOM   10090 O  O   . GLY C  1 153 ? -17.955 0.241   -4.339  1.00 27.89 ? 170  GLY C O   1 
ATOM   10091 N  N   . ASP C  1 154 ? -19.792 -1.037  -4.026  1.00 28.34 ? 171  ASP C N   1 
ATOM   10092 C  CA  . ASP C  1 154 ? -19.328 -1.696  -2.817  1.00 27.43 ? 171  ASP C CA  1 
ATOM   10093 C  C   . ASP C  1 154 ? -18.361 -2.819  -3.190  1.00 27.42 ? 171  ASP C C   1 
ATOM   10094 O  O   . ASP C  1 154 ? -18.776 -3.841  -3.730  1.00 28.68 ? 171  ASP C O   1 
ATOM   10095 C  CB  . ASP C  1 154 ? -20.524 -2.146  -1.991  1.00 27.83 ? 171  ASP C CB  1 
ATOM   10096 C  CG  . ASP C  1 154 ? -20.226 -2.783  -0.642  1.00 27.25 ? 171  ASP C CG  1 
ATOM   10097 O  OD1 . ASP C  1 154 ? -19.042 -3.088  -0.374  1.00 26.37 ? 171  ASP C OD1 1 
ATOM   10098 O  OD2 . ASP C  1 154 ? -21.183 -2.960  0.137   1.00 26.68 ? 171  ASP C OD2 1 
ATOM   10099 N  N   . LEU C  1 155 ? -17.069 -2.627  -2.888  1.00 26.10 ? 172  LEU C N   1 
ATOM   10100 C  CA  . LEU C  1 155 ? -16.063 -3.646  -3.152  1.00 26.08 ? 172  LEU C CA  1 
ATOM   10101 C  C   . LEU C  1 155 ? -15.495 -4.210  -1.850  1.00 26.49 ? 172  LEU C C   1 
ATOM   10102 O  O   . LEU C  1 155 ? -14.559 -5.004  -1.894  1.00 26.83 ? 172  LEU C O   1 
ATOM   10103 C  CB  . LEU C  1 155 ? -14.933 -3.076  -4.007  1.00 27.25 ? 172  LEU C CB  1 
ATOM   10104 C  CG  . LEU C  1 155 ? -15.283 -2.675  -5.442  1.00 29.40 ? 172  LEU C CG  1 
ATOM   10105 C  CD1 . LEU C  1 155 ? -14.025 -2.156  -6.112  1.00 30.47 ? 172  LEU C CD1 1 
ATOM   10106 C  CD2 . LEU C  1 155 ? -15.893 -3.806  -6.258  1.00 30.05 ? 172  LEU C CD2 1 
ATOM   10107 N  N   . GLY C  1 156 ? -16.022 -3.782  -0.698  1.00 25.04 ? 173  GLY C N   1 
ATOM   10108 C  CA  . GLY C  1 156 ? -15.479 -4.216  0.579   1.00 24.67 ? 173  GLY C CA  1 
ATOM   10109 C  C   . GLY C  1 156 ? -13.967 -4.001  0.644   1.00 23.31 ? 173  GLY C C   1 
ATOM   10110 O  O   . GLY C  1 156 ? -13.477 -2.938  0.280   1.00 20.31 ? 173  GLY C O   1 
ATOM   10111 N  N   . VAL C  1 157 ? -13.232 -5.036  1.070   1.00 23.87 ? 174  VAL C N   1 
ATOM   10112 C  CA  . VAL C  1 157 ? -11.805 -4.909  1.321   1.00 26.63 ? 174  VAL C CA  1 
ATOM   10113 C  C   . VAL C  1 157 ? -11.039 -4.859  0.000   1.00 29.16 ? 174  VAL C C   1 
ATOM   10114 O  O   . VAL C  1 157 ? -9.861  -4.519  -0.002  1.00 31.89 ? 174  VAL C O   1 
ATOM   10115 C  CB  . VAL C  1 157 ? -11.233 -6.018  2.224   1.00 27.57 ? 174  VAL C CB  1 
ATOM   10116 C  CG1 . VAL C  1 157 ? -11.931 -6.061  3.576   1.00 28.17 ? 174  VAL C CG1 1 
ATOM   10117 C  CG2 . VAL C  1 157 ? -11.262 -7.382  1.554   1.00 28.68 ? 174  VAL C CG2 1 
ATOM   10118 N  N   . TYR C  1 158 ? -11.711 -5.134  -1.125  1.00 31.60 ? 175  TYR C N   1 
ATOM   10119 C  CA  . TYR C  1 158 ? -11.097 -4.972  -2.435  1.00 34.59 ? 175  TYR C CA  1 
ATOM   10120 C  C   . TYR C  1 158 ? -10.880 -3.501  -2.810  1.00 34.75 ? 175  TYR C C   1 
ATOM   10121 O  O   . TYR C  1 158 ? -10.391 -3.234  -3.907  1.00 38.64 ? 175  TYR C O   1 
ATOM   10122 C  CB  . TYR C  1 158 ? -11.902 -5.654  -3.549  1.00 36.63 ? 175  TYR C CB  1 
ATOM   10123 C  CG  . TYR C  1 158 ? -11.786 -7.169  -3.687  1.00 39.50 ? 175  TYR C CG  1 
ATOM   10124 C  CD1 . TYR C  1 158 ? -10.744 -7.895  -3.111  1.00 41.44 ? 175  TYR C CD1 1 
ATOM   10125 C  CD2 . TYR C  1 158 ? -12.708 -7.870  -4.452  1.00 40.22 ? 175  TYR C CD2 1 
ATOM   10126 C  CE1 . TYR C  1 158 ? -10.650 -9.270  -3.264  1.00 41.17 ? 175  TYR C CE1 1 
ATOM   10127 C  CE2 . TYR C  1 158 ? -12.621 -9.241  -4.617  1.00 43.26 ? 175  TYR C CE2 1 
ATOM   10128 C  CZ  . TYR C  1 158 ? -11.588 -9.944  -4.024  1.00 43.43 ? 175  TYR C CZ  1 
ATOM   10129 O  OH  . TYR C  1 158 ? -11.518 -11.296 -4.203  1.00 45.92 ? 175  TYR C OH  1 
ATOM   10130 N  N   A GLY C  1 159 ? -11.251 -2.576  -1.911  0.25 33.61 ? 176  GLY C N   1 
ATOM   10131 N  N   B GLY C  1 159 ? -11.231 -2.576  -1.904  0.25 33.17 ? 176  GLY C N   1 
ATOM   10132 N  N   C GLY C  1 159 ? -11.274 -2.573  -1.925  0.25 34.20 ? 176  GLY C N   1 
ATOM   10133 N  N   D GLY C  1 159 ? -11.234 -2.579  -1.902  0.25 33.35 ? 176  GLY C N   1 
ATOM   10134 C  CA  A GLY C  1 159 ? -10.993 -1.155  -2.088  0.25 33.28 ? 176  GLY C CA  1 
ATOM   10135 C  CA  B GLY C  1 159 ? -11.040 -1.153  -2.126  0.25 32.53 ? 176  GLY C CA  1 
ATOM   10136 C  CA  C GLY C  1 159 ? -11.035 -1.153  -2.121  0.25 34.31 ? 176  GLY C CA  1 
ATOM   10137 C  CA  D GLY C  1 159 ? -10.946 -1.163  -2.062  0.25 32.83 ? 176  GLY C CA  1 
ATOM   10138 C  C   A GLY C  1 159 ? -9.774  -0.693  -1.290  0.25 32.43 ? 176  GLY C C   1 
ATOM   10139 C  C   B GLY C  1 159 ? -9.900  -0.581  -1.284  0.25 31.30 ? 176  GLY C C   1 
ATOM   10140 C  C   C GLY C  1 159 ? -9.931  -0.646  -1.196  0.25 33.87 ? 176  GLY C C   1 
ATOM   10141 C  C   D GLY C  1 159 ? -9.710  -0.738  -1.270  0.25 31.77 ? 176  GLY C C   1 
ATOM   10142 O  O   A GLY C  1 159 ? -9.509  0.503   -1.196  0.25 31.58 ? 176  GLY C O   1 
ATOM   10143 O  O   B GLY C  1 159 ? -9.778  0.634   -1.159  0.25 30.64 ? 176  GLY C O   1 
ATOM   10144 O  O   C GLY C  1 159 ? -9.517  0.508   -1.286  0.25 32.84 ? 176  GLY C O   1 
ATOM   10145 O  O   D GLY C  1 159 ? -9.416  0.452   -1.174  0.25 30.88 ? 176  GLY C O   1 
ATOM   10146 N  N   A MET C  1 160 ? -9.035  -1.654  -0.721  0.25 31.84 ? 177  MET C N   1 
ATOM   10147 N  N   B MET C  1 160 ? -9.058  -1.454  -0.714  0.50 30.51 ? 177  MET C N   1 
ATOM   10148 N  N   D MET C  1 160 ? -8.986  -1.717  -0.711  0.25 30.83 ? 177  MET C N   1 
ATOM   10149 C  CA  A MET C  1 160 ? -7.786  -1.379  -0.026  0.25 31.01 ? 177  MET C CA  1 
ATOM   10150 C  CA  B MET C  1 160 ? -7.891  -0.992  0.023   0.50 28.70 ? 177  MET C CA  1 
ATOM   10151 C  CA  D MET C  1 160 ? -7.728  -1.453  -0.027  0.25 29.85 ? 177  MET C CA  1 
ATOM   10152 C  C   A MET C  1 160 ? -6.852  -0.570  -0.926  0.25 29.60 ? 177  MET C C   1 
ATOM   10153 C  C   B MET C  1 160 ? -6.821  -0.491  -0.943  0.50 28.62 ? 177  MET C C   1 
ATOM   10154 C  C   D MET C  1 160 ? -6.824  -0.606  -0.922  0.25 28.98 ? 177  MET C C   1 
ATOM   10155 O  O   A MET C  1 160 ? -6.078  0.251   -0.441  0.25 29.54 ? 177  MET C O   1 
ATOM   10156 O  O   B MET C  1 160 ? -5.902  0.200   -0.512  0.50 29.14 ? 177  MET C O   1 
ATOM   10157 O  O   D MET C  1 160 ? -6.053  0.215   -0.431  0.25 29.00 ? 177  MET C O   1 
ATOM   10158 C  CB  A MET C  1 160 ? -7.091  -2.689  0.370   0.25 31.36 ? 177  MET C CB  1 
ATOM   10159 C  CB  B MET C  1 160 ? -7.273  -2.083  0.905   0.50 27.66 ? 177  MET C CB  1 
ATOM   10160 C  CB  D MET C  1 160 ? -7.008  -2.757  0.348   0.25 29.47 ? 177  MET C CB  1 
ATOM   10161 C  CG  A MET C  1 160 ? -6.883  -3.638  -0.802  0.25 31.91 ? 177  MET C CG  1 
ATOM   10162 C  CG  B MET C  1 160 ? -5.883  -1.747  1.453   0.50 26.54 ? 177  MET C CG  1 
ATOM   10163 C  CG  D MET C  1 160 ? -6.719  -3.685  -0.828  0.25 29.46 ? 177  MET C CG  1 
ATOM   10164 S  SD  A MET C  1 160 ? -6.497  -5.350  -0.374  0.25 33.26 ? 177  MET C SD  1 
ATOM   10165 S  SD  B MET C  1 160 ? -5.715  -0.211  2.391   0.50 23.91 ? 177  MET C SD  1 
ATOM   10166 S  SD  D MET C  1 160 ? -5.785  -5.177  -0.419  0.25 29.55 ? 177  MET C SD  1 
ATOM   10167 C  CE  A MET C  1 160 ? -4.738  -5.421  -0.742  0.25 32.64 ? 177  MET C CE  1 
ATOM   10168 C  CE  B MET C  1 160 ? -4.680  -0.825  3.724   0.50 24.03 ? 177  MET C CE  1 
ATOM   10169 C  CE  D MET C  1 160 ? -7.080  -6.203  0.291   0.25 29.10 ? 177  MET C CE  1 
ATOM   10170 N  N   . GLY C  1 161 ? -6.931  -0.830  -2.237  1.00 28.00 ? 178  GLY C N   1 
ATOM   10171 C  CA  . GLY C  1 161 ? -6.108  -0.169  -3.238  1.00 26.87 ? 178  GLY C CA  1 
ATOM   10172 C  C   . GLY C  1 161 ? -6.325  1.343   -3.315  1.00 25.16 ? 178  GLY C C   1 
ATOM   10173 O  O   . GLY C  1 161 ? -5.410  2.050   -3.725  1.00 22.62 ? 178  GLY C O   1 
ATOM   10174 N  N   . ILE C  1 162 ? -7.522  1.836   -2.946  1.00 24.46 ? 179  ILE C N   1 
ATOM   10175 C  CA  . ILE C  1 162 ? -7.868  3.237   -3.138  1.00 23.92 ? 179  ILE C CA  1 
ATOM   10176 C  C   . ILE C  1 162 ? -7.022  4.123   -2.218  1.00 23.07 ? 179  ILE C C   1 
ATOM   10177 O  O   . ILE C  1 162 ? -6.381  5.049   -2.712  1.00 22.92 ? 179  ILE C O   1 
ATOM   10178 C  CB  . ILE C  1 162 ? -9.389  3.485   -3.003  1.00 25.48 ? 179  ILE C CB  1 
ATOM   10179 C  CG1 . ILE C  1 162 ? -10.128 3.190   -4.316  1.00 26.20 ? 179  ILE C CG1 1 
ATOM   10180 C  CG2 . ILE C  1 162 ? -9.693  4.909   -2.536  1.00 26.03 ? 179  ILE C CG2 1 
ATOM   10181 C  CD1 . ILE C  1 162 ? -10.070 1.740   -4.764  1.00 26.62 ? 179  ILE C CD1 1 
ATOM   10182 N  N   . PRO C  1 163 ? -6.984  3.922   -0.876  1.00 22.89 ? 180  PRO C N   1 
ATOM   10183 C  CA  . PRO C  1 163 ? -6.092  4.712   -0.025  1.00 22.41 ? 180  PRO C CA  1 
ATOM   10184 C  C   . PRO C  1 163 ? -4.610  4.620   -0.392  1.00 21.23 ? 180  PRO C C   1 
ATOM   10185 O  O   . PRO C  1 163 ? -3.894  5.612   -0.276  1.00 20.34 ? 180  PRO C O   1 
ATOM   10186 C  CB  . PRO C  1 163 ? -6.373  4.186   1.395   1.00 23.08 ? 180  PRO C CB  1 
ATOM   10187 C  CG  . PRO C  1 163 ? -7.762  3.613   1.310   1.00 24.25 ? 180  PRO C CG  1 
ATOM   10188 C  CD  . PRO C  1 163 ? -7.852  3.029   -0.090  1.00 24.11 ? 180  PRO C CD  1 
ATOM   10189 N  N   . VAL C  1 164 ? -4.167  3.434   -0.836  1.00 21.02 ? 181  VAL C N   1 
ATOM   10190 C  CA  . VAL C  1 164 ? -2.792  3.218   -1.264  1.00 21.44 ? 181  VAL C CA  1 
ATOM   10191 C  C   . VAL C  1 164 ? -2.493  4.133   -2.450  1.00 21.54 ? 181  VAL C C   1 
ATOM   10192 O  O   . VAL C  1 164 ? -1.485  4.841   -2.461  1.00 20.24 ? 181  VAL C O   1 
ATOM   10193 C  CB  . VAL C  1 164 ? -2.509  1.744   -1.623  1.00 21.89 ? 181  VAL C CB  1 
ATOM   10194 C  CG1 . VAL C  1 164 ? -1.130  1.557   -2.252  1.00 22.49 ? 181  VAL C CG1 1 
ATOM   10195 C  CG2 . VAL C  1 164 ? -2.656  0.825   -0.419  1.00 22.10 ? 181  VAL C CG2 1 
ATOM   10196 N  N   . GLY C  1 165 ? -3.372  4.098   -3.458  1.00 22.01 ? 182  GLY C N   1 
ATOM   10197 C  CA  . GLY C  1 165 ? -3.196  4.907   -4.655  1.00 21.80 ? 182  GLY C CA  1 
ATOM   10198 C  C   . GLY C  1 165 ? -3.279  6.400   -4.351  1.00 22.27 ? 182  GLY C C   1 
ATOM   10199 O  O   . GLY C  1 165 ? -2.505  7.192   -4.888  1.00 22.95 ? 182  GLY C O   1 
ATOM   10200 N  N   . LYS C  1 166 ? -4.224  6.781   -3.487  1.00 22.01 ? 183  LYS C N   1 
ATOM   10201 C  CA  . LYS C  1 166 ? -4.391  8.177   -3.114  1.00 23.07 ? 183  LYS C CA  1 
ATOM   10202 C  C   . LYS C  1 166 ? -3.086  8.710   -2.521  1.00 22.47 ? 183  LYS C C   1 
ATOM   10203 O  O   . LYS C  1 166 ? -2.621  9.791   -2.891  1.00 21.37 ? 183  LYS C O   1 
ATOM   10204 C  CB  . LYS C  1 166 ? -5.568  8.321   -2.142  1.00 24.00 ? 183  LYS C CB  1 
ATOM   10205 C  CG  . LYS C  1 166 ? -6.069  9.743   -1.896  1.00 25.19 ? 183  LYS C CG  1 
ATOM   10206 C  CD  . LYS C  1 166 ? -6.861  10.322  -3.059  1.00 26.37 ? 183  LYS C CD  1 
ATOM   10207 C  CE  . LYS C  1 166 ? -7.702  11.496  -2.672  1.00 26.60 ? 183  LYS C CE  1 
ATOM   10208 N  NZ  . LYS C  1 166 ? -8.764  11.721  -3.651  1.00 26.56 ? 183  LYS C NZ  1 
ATOM   10209 N  N   . LEU C  1 167 ? -2.480  7.937   -1.613  1.00 21.90 ? 184  LEU C N   1 
ATOM   10210 C  CA  . LEU C  1 167 ? -1.302  8.402   -0.897  1.00 21.85 ? 184  LEU C CA  1 
ATOM   10211 C  C   . LEU C  1 167 ? -0.076  8.419   -1.812  1.00 21.59 ? 184  LEU C C   1 
ATOM   10212 O  O   . LEU C  1 167 ? 0.834   9.216   -1.590  1.00 21.52 ? 184  LEU C O   1 
ATOM   10213 C  CB  . LEU C  1 167 ? -1.088  7.584   0.376   1.00 21.37 ? 184  LEU C CB  1 
ATOM   10214 C  CG  . LEU C  1 167 ? -2.052  7.920   1.521   1.00 21.18 ? 184  LEU C CG  1 
ATOM   10215 C  CD1 . LEU C  1 167 ? -2.074  6.824   2.557   1.00 21.74 ? 184  LEU C CD1 1 
ATOM   10216 C  CD2 . LEU C  1 167 ? -1.699  9.252   2.166   1.00 21.43 ? 184  LEU C CD2 1 
ATOM   10217 N  N   . CYS C  1 168 ? -0.071  7.582   -2.856  1.00 21.94 ? 185  CYS C N   1 
ATOM   10218 C  CA  . CYS C  1 168 ? 0.940   7.661   -3.902  1.00 23.13 ? 185  CYS C CA  1 
ATOM   10219 C  C   . CYS C  1 168 ? 0.931   9.049   -4.551  1.00 22.70 ? 185  CYS C C   1 
ATOM   10220 O  O   . CYS C  1 168 ? 1.982   9.572   -4.926  1.00 23.33 ? 185  CYS C O   1 
ATOM   10221 C  CB  . CYS C  1 168 ? 0.761   6.556   -4.941  1.00 24.90 ? 185  CYS C CB  1 
ATOM   10222 S  SG  . CYS C  1 168 ? 1.243   4.916   -4.334  1.00 27.84 ? 185  CYS C SG  1 
ATOM   10223 N  N   . LEU C  1 169 ? -0.255  9.649   -4.674  1.00 22.03 ? 186  LEU C N   1 
ATOM   10224 C  CA  . LEU C  1 169 ? -0.379  10.973  -5.268  1.00 22.83 ? 186  LEU C CA  1 
ATOM   10225 C  C   . LEU C  1 169 ? -0.028  12.065  -4.257  1.00 22.02 ? 186  LEU C C   1 
ATOM   10226 O  O   . LEU C  1 169 ? 0.511   13.097  -4.650  1.00 22.85 ? 186  LEU C O   1 
ATOM   10227 C  CB  . LEU C  1 169 ? -1.780  11.152  -5.851  1.00 23.49 ? 186  LEU C CB  1 
ATOM   10228 C  CG  . LEU C  1 169 ? -2.188  10.125  -6.910  1.00 25.25 ? 186  LEU C CG  1 
ATOM   10229 C  CD1 . LEU C  1 169 ? -3.562  10.437  -7.469  1.00 26.55 ? 186  LEU C CD1 1 
ATOM   10230 C  CD2 . LEU C  1 169 ? -1.161  10.057  -8.025  1.00 25.93 ? 186  LEU C CD2 1 
ATOM   10231 N  N   . TYR C  1 170 ? -0.321  11.852  -2.962  1.00 21.51 ? 187  TYR C N   1 
ATOM   10232 C  CA  . TYR C  1 170 ? 0.144   12.764  -1.922  1.00 20.02 ? 187  TYR C CA  1 
ATOM   10233 C  C   . TYR C  1 170 ? 1.654   12.973  -2.071  1.00 19.75 ? 187  TYR C C   1 
ATOM   10234 O  O   . TYR C  1 170 ? 2.145   14.104  -2.044  1.00 19.82 ? 187  TYR C O   1 
ATOM   10235 C  CB  . TYR C  1 170 ? -0.127  12.267  -0.497  1.00 20.54 ? 187  TYR C CB  1 
ATOM   10236 C  CG  . TYR C  1 170 ? -1.502  12.524  0.115   1.00 21.82 ? 187  TYR C CG  1 
ATOM   10237 C  CD1 . TYR C  1 170 ? -2.678  12.296  -0.584  1.00 22.24 ? 187  TYR C CD1 1 
ATOM   10238 C  CD2 . TYR C  1 170 ? -1.613  12.956  1.434   1.00 22.77 ? 187  TYR C CD2 1 
ATOM   10239 C  CE1 . TYR C  1 170 ? -3.919  12.518  -0.004  1.00 23.22 ? 187  TYR C CE1 1 
ATOM   10240 C  CE2 . TYR C  1 170 ? -2.845  13.177  2.029   1.00 23.51 ? 187  TYR C CE2 1 
ATOM   10241 C  CZ  . TYR C  1 170 ? -4.004  12.964  1.306   1.00 24.39 ? 187  TYR C CZ  1 
ATOM   10242 O  OH  . TYR C  1 170 ? -5.210  13.201  1.908   1.00 25.82 ? 187  TYR C OH  1 
ATOM   10243 N  N   . THR C  1 171 ? 2.394   11.864  -2.195  1.00 19.09 ? 188  THR C N   1 
ATOM   10244 C  CA  . THR C  1 171 ? 3.847   11.905  -2.255  1.00 19.92 ? 188  THR C CA  1 
ATOM   10245 C  C   . THR C  1 171 ? 4.309   12.432  -3.614  1.00 20.32 ? 188  THR C C   1 
ATOM   10246 O  O   . THR C  1 171 ? 5.132   13.343  -3.675  1.00 20.89 ? 188  THR C O   1 
ATOM   10247 C  CB  . THR C  1 171 ? 4.423   10.515  -1.971  1.00 19.93 ? 188  THR C CB  1 
ATOM   10248 O  OG1 . THR C  1 171 ? 4.096   10.203  -0.621  1.00 20.54 ? 188  THR C OG1 1 
ATOM   10249 C  CG2 . THR C  1 171 ? 5.934   10.456  -2.119  1.00 19.99 ? 188  THR C CG2 1 
ATOM   10250 N  N   . ALA C  1 172 ? 3.810   11.842  -4.704  1.00 21.00 ? 189  ALA C N   1 
ATOM   10251 C  CA  . ALA C  1 172 ? 4.312   12.176  -6.031  1.00 21.94 ? 189  ALA C CA  1 
ATOM   10252 C  C   . ALA C  1 172 ? 4.023   13.637  -6.388  1.00 23.62 ? 189  ALA C C   1 
ATOM   10253 O  O   . ALA C  1 172 ? 4.848   14.277  -7.036  1.00 23.29 ? 189  ALA C O   1 
ATOM   10254 C  CB  . ALA C  1 172 ? 3.735   11.233  -7.061  1.00 21.48 ? 189  ALA C CB  1 
ATOM   10255 N  N   . CYS C  1 173 ? 2.866   14.168  -5.959  1.00 24.04 ? 190  CYS C N   1 
ATOM   10256 C  CA  . CYS C  1 173 ? 2.421   15.489  -6.390  1.00 24.31 ? 190  CYS C CA  1 
ATOM   10257 C  C   . CYS C  1 173 ? 2.917   16.590  -5.450  1.00 25.62 ? 190  CYS C C   1 
ATOM   10258 O  O   . CYS C  1 173 ? 3.278   17.670  -5.919  1.00 26.50 ? 190  CYS C O   1 
ATOM   10259 C  CB  . CYS C  1 173 ? 0.902   15.560  -6.527  1.00 25.39 ? 190  CYS C CB  1 
ATOM   10260 S  SG  . CYS C  1 173 ? 0.231   14.434  -7.781  1.00 27.13 ? 190  CYS C SG  1 
ATOM   10261 N  N   . ALA C  1 174 ? 2.928   16.330  -4.132  1.00 24.21 ? 191  ALA C N   1 
ATOM   10262 C  CA  . ALA C  1 174 ? 3.212   17.376  -3.162  1.00 23.72 ? 191  ALA C CA  1 
ATOM   10263 C  C   . ALA C  1 174 ? 4.426   17.060  -2.288  1.00 23.41 ? 191  ALA C C   1 
ATOM   10264 O  O   . ALA C  1 174 ? 4.764   17.861  -1.420  1.00 24.47 ? 191  ALA C O   1 
ATOM   10265 C  CB  . ALA C  1 174 ? 1.988   17.615  -2.307  1.00 24.09 ? 191  ALA C CB  1 
ATOM   10266 N  N   . GLY C  1 175 ? 5.067   15.901  -2.492  1.00 22.85 ? 192  GLY C N   1 
ATOM   10267 C  CA  . GLY C  1 175 ? 6.244   15.521  -1.723  1.00 22.56 ? 192  GLY C CA  1 
ATOM   10268 C  C   . GLY C  1 175 ? 5.963   15.344  -0.228  1.00 22.20 ? 192  GLY C C   1 
ATOM   10269 O  O   . GLY C  1 175 ? 6.805   15.667  0.612   1.00 21.22 ? 192  GLY C O   1 
ATOM   10270 N  N   . ILE C  1 176 ? 4.782   14.818  0.113   1.00 22.15 ? 193  ILE C N   1 
ATOM   10271 C  CA  . ILE C  1 176 ? 4.539   14.339  1.462   1.00 21.64 ? 193  ILE C CA  1 
ATOM   10272 C  C   . ILE C  1 176 ? 5.348   13.055  1.622   1.00 22.19 ? 193  ILE C C   1 
ATOM   10273 O  O   . ILE C  1 176 ? 5.320   12.199  0.743   1.00 22.06 ? 193  ILE C O   1 
ATOM   10274 C  CB  . ILE C  1 176 ? 3.030   14.147  1.711   1.00 22.02 ? 193  ILE C CB  1 
ATOM   10275 C  CG1 . ILE C  1 176 ? 2.305   15.503  1.632   1.00 22.83 ? 193  ILE C CG1 1 
ATOM   10276 C  CG2 . ILE C  1 176 ? 2.773   13.439  3.043   1.00 21.59 ? 193  ILE C CG2 1 
ATOM   10277 C  CD1 . ILE C  1 176 ? 0.800   15.420  1.522   1.00 23.55 ? 193  ILE C CD1 1 
ATOM   10278 N  N   . ARG C  1 177 ? 6.095   12.944  2.726   1.00 23.00 ? 194  ARG C N   1 
ATOM   10279 C  CA  . ARG C  1 177 ? 7.018   11.833  2.915   1.00 24.23 ? 194  ARG C CA  1 
ATOM   10280 C  C   . ARG C  1 177 ? 6.271   10.502  2.906   1.00 23.34 ? 194  ARG C C   1 
ATOM   10281 O  O   . ARG C  1 177 ? 5.347   10.303  3.697   1.00 20.89 ? 194  ARG C O   1 
ATOM   10282 C  CB  . ARG C  1 177 ? 7.786   11.926  4.233   1.00 26.14 ? 194  ARG C CB  1 
ATOM   10283 C  CG  . ARG C  1 177 ? 8.888   12.971  4.227   1.00 29.21 ? 194  ARG C CG  1 
ATOM   10284 C  CD  . ARG C  1 177 ? 9.588   13.060  5.567   1.00 31.86 ? 194  ARG C CD  1 
ATOM   10285 N  NE  . ARG C  1 177 ? 10.249  11.797  5.910   1.00 35.17 ? 194  ARG C NE  1 
ATOM   10286 C  CZ  . ARG C  1 177 ? 11.141  11.644  6.881   1.00 41.49 ? 194  ARG C CZ  1 
ATOM   10287 N  NH1 . ARG C  1 177 ? 11.491  12.670  7.642   1.00 43.24 ? 194  ARG C NH1 1 
ATOM   10288 N  NH2 . ARG C  1 177 ? 11.690  10.460  7.081   1.00 43.75 ? 194  ARG C NH2 1 
ATOM   10289 N  N   . PRO C  1 178 ? 6.675   9.538   2.043   1.00 23.34 ? 195  PRO C N   1 
ATOM   10290 C  CA  . PRO C  1 178 ? 5.976   8.257   1.957   1.00 23.49 ? 195  PRO C CA  1 
ATOM   10291 C  C   . PRO C  1 178 ? 5.980   7.475   3.271   1.00 23.55 ? 195  PRO C C   1 
ATOM   10292 O  O   . PRO C  1 178 ? 5.005   6.790   3.572   1.00 23.45 ? 195  PRO C O   1 
ATOM   10293 C  CB  . PRO C  1 178 ? 6.656   7.491   0.802   1.00 24.07 ? 195  PRO C CB  1 
ATOM   10294 C  CG  . PRO C  1 178 ? 7.934   8.260   0.496   1.00 24.00 ? 195  PRO C CG  1 
ATOM   10295 C  CD  . PRO C  1 178 ? 7.789   9.652   1.083   1.00 23.43 ? 195  PRO C CD  1 
ATOM   10296 N  N   . ASP C  1 179 ? 7.045   7.612   4.072   1.00 23.35 ? 196  ASP C N   1 
ATOM   10297 C  CA  . ASP C  1 179 ? 7.127   6.903   5.341   1.00 24.87 ? 196  ASP C CA  1 
ATOM   10298 C  C   . ASP C  1 179 ? 6.170   7.495   6.381   1.00 23.62 ? 196  ASP C C   1 
ATOM   10299 O  O   . ASP C  1 179 ? 5.960   6.880   7.425   1.00 23.59 ? 196  ASP C O   1 
ATOM   10300 C  CB  . ASP C  1 179 ? 8.562   6.751   5.831   1.00 27.02 ? 196  ASP C CB  1 
ATOM   10301 C  CG  . ASP C  1 179 ? 9.303   8.020   6.235   1.00 29.39 ? 196  ASP C CG  1 
ATOM   10302 O  OD1 . ASP C  1 179 ? 8.826   9.128   5.916   1.00 30.82 ? 196  ASP C OD1 1 
ATOM   10303 O  OD2 . ASP C  1 179 ? 10.362  7.889   6.876   1.00 32.38 ? 196  ASP C OD2 1 
ATOM   10304 N  N   . ARG C  1 180 ? 5.564   8.657   6.093   1.00 21.98 ? 197  ARG C N   1 
ATOM   10305 C  CA  . ARG C  1 180 ? 4.609   9.271   7.008   1.00 22.26 ? 197  ARG C CA  1 
ATOM   10306 C  C   . ARG C  1 180 ? 3.174   9.152   6.492   1.00 20.44 ? 197  ARG C C   1 
ATOM   10307 O  O   . ARG C  1 180 ? 2.278   9.817   7.013   1.00 19.84 ? 197  ARG C O   1 
ATOM   10308 C  CB  . ARG C  1 180 ? 5.023   10.725  7.253   1.00 23.65 ? 197  ARG C CB  1 
ATOM   10309 C  CG  . ARG C  1 180 ? 6.416   10.776  7.859   1.00 26.01 ? 197  ARG C CG  1 
ATOM   10310 C  CD  . ARG C  1 180 ? 6.771   12.127  8.420   1.00 29.05 ? 197  ARG C CD  1 
ATOM   10311 N  NE  . ARG C  1 180 ? 8.085   12.086  9.071   1.00 31.60 ? 197  ARG C NE  1 
ATOM   10312 C  CZ  . ARG C  1 180 ? 8.765   13.169  9.441   1.00 35.62 ? 197  ARG C CZ  1 
ATOM   10313 N  NH1 . ARG C  1 180 ? 8.282   14.381  9.198   1.00 34.10 ? 197  ARG C NH1 1 
ATOM   10314 N  NH2 . ARG C  1 180 ? 9.939   13.035  10.035  1.00 35.18 ? 197  ARG C NH2 1 
ATOM   10315 N  N   . CYS C  1 181 ? 2.958   8.266   5.511   1.00 19.75 ? 198  CYS C N   1 
ATOM   10316 C  CA  . CYS C  1 181 ? 1.643   8.023   4.932   1.00 20.26 ? 198  CYS C CA  1 
ATOM   10317 C  C   . CYS C  1 181 ? 1.113   6.669   5.403   1.00 19.86 ? 198  CYS C C   1 
ATOM   10318 O  O   . CYS C  1 181 ? 1.864   5.693   5.456   1.00 20.46 ? 198  CYS C O   1 
ATOM   10319 C  CB  . CYS C  1 181 ? 1.709   8.052   3.409   1.00 20.87 ? 198  CYS C CB  1 
ATOM   10320 S  SG  . CYS C  1 181 ? 2.074   9.691   2.730   1.00 22.22 ? 198  CYS C SG  1 
ATOM   10321 N  N   . LEU C  1 182 ? -0.185  6.618   5.736   1.00 18.29 ? 199  LEU C N   1 
ATOM   10322 C  CA  . LEU C  1 182 ? -0.789  5.421   6.296   1.00 18.32 ? 199  LEU C CA  1 
ATOM   10323 C  C   . LEU C  1 182 ? -2.140  5.169   5.627   1.00 18.63 ? 199  LEU C C   1 
ATOM   10324 O  O   . LEU C  1 182 ? -3.126  5.840   5.930   1.00 18.59 ? 199  LEU C O   1 
ATOM   10325 C  CB  . LEU C  1 182 ? -0.928  5.541   7.814   1.00 19.08 ? 199  LEU C CB  1 
ATOM   10326 C  CG  . LEU C  1 182 ? -1.705  4.418   8.510   1.00 19.03 ? 199  LEU C CG  1 
ATOM   10327 C  CD1 . LEU C  1 182 ? -1.142  3.059   8.149   1.00 19.96 ? 199  LEU C CD1 1 
ATOM   10328 C  CD2 . LEU C  1 182 ? -1.689  4.622   10.011  1.00 19.82 ? 199  LEU C CD2 1 
ATOM   10329 N  N   . PRO C  1 183 ? -2.221  4.191   4.695   1.00 18.00 ? 200  PRO C N   1 
ATOM   10330 C  CA  . PRO C  1 183 ? -3.498  3.767   4.122   1.00 17.96 ? 200  PRO C CA  1 
ATOM   10331 C  C   . PRO C  1 183 ? -4.232  2.851   5.099   1.00 18.21 ? 200  PRO C C   1 
ATOM   10332 O  O   . PRO C  1 183 ? -3.609  2.008   5.747   1.00 17.99 ? 200  PRO C O   1 
ATOM   10333 C  CB  . PRO C  1 183 ? -3.123  3.041   2.813   1.00 18.40 ? 200  PRO C CB  1 
ATOM   10334 C  CG  . PRO C  1 183 ? -1.604  3.129   2.723   1.00 18.45 ? 200  PRO C CG  1 
ATOM   10335 C  CD  . PRO C  1 183 ? -1.081  3.476   4.104   1.00 18.23 ? 200  PRO C CD  1 
ATOM   10336 N  N   . VAL C  1 184 ? -5.559  3.020   5.188   1.00 18.13 ? 201  VAL C N   1 
ATOM   10337 C  CA  . VAL C  1 184 ? -6.367  2.269   6.135   1.00 18.57 ? 201  VAL C CA  1 
ATOM   10338 C  C   . VAL C  1 184 ? -7.638  1.810   5.427   1.00 20.15 ? 201  VAL C C   1 
ATOM   10339 O  O   . VAL C  1 184 ? -8.300  2.598   4.750   1.00 19.21 ? 201  VAL C O   1 
ATOM   10340 C  CB  . VAL C  1 184 ? -6.710  3.080   7.403   1.00 18.65 ? 201  VAL C CB  1 
ATOM   10341 C  CG1 . VAL C  1 184 ? -7.579  2.284   8.369   1.00 18.31 ? 201  VAL C CG1 1 
ATOM   10342 C  CG2 . VAL C  1 184 ? -5.464  3.587   8.122   1.00 18.90 ? 201  VAL C CG2 1 
ATOM   10343 N  N   . CYS C  1 185 ? -7.957  0.524   5.607   1.00 21.27 ? 202  CYS C N   1 
ATOM   10344 C  CA  . CYS C  1 185 ? -9.194  -0.062  5.130   1.00 23.51 ? 202  CYS C CA  1 
ATOM   10345 C  C   . CYS C  1 185 ? -9.990  -0.576  6.328   1.00 22.80 ? 202  CYS C C   1 
ATOM   10346 O  O   . CYS C  1 185 ? -9.491  -1.386  7.112   1.00 21.89 ? 202  CYS C O   1 
ATOM   10347 C  CB  . CYS C  1 185 ? -8.891  -1.156  4.115   1.00 27.20 ? 202  CYS C CB  1 
ATOM   10348 S  SG  . CYS C  1 185 ? -10.373 -1.954  3.448   1.00 32.55 ? 202  CYS C SG  1 
ATOM   10349 N  N   . ILE C  1 186 ? -11.210 -0.053  6.483   1.00 22.53 ? 203  ILE C N   1 
ATOM   10350 C  CA  . ILE C  1 186 ? -12.131 -0.486  7.519   1.00 24.24 ? 203  ILE C CA  1 
ATOM   10351 C  C   . ILE C  1 186 ? -13.018 -1.575  6.921   1.00 25.01 ? 203  ILE C C   1 
ATOM   10352 O  O   . ILE C  1 186 ? -13.687 -1.318  5.922   1.00 25.56 ? 203  ILE C O   1 
ATOM   10353 C  CB  . ILE C  1 186 ? -12.991 0.690   8.020   1.00 25.54 ? 203  ILE C CB  1 
ATOM   10354 C  CG1 . ILE C  1 186 ? -12.160 1.876   8.511   1.00 26.67 ? 203  ILE C CG1 1 
ATOM   10355 C  CG2 . ILE C  1 186 ? -13.984 0.223   9.089   1.00 26.01 ? 203  ILE C CG2 1 
ATOM   10356 C  CD1 . ILE C  1 186 ? -11.451 1.649   9.829   1.00 27.24 ? 203  ILE C CD1 1 
ATOM   10357 N  N   . ASP C  1 187 ? -13.045 -2.762  7.542   1.00 24.83 ? 204  ASP C N   1 
ATOM   10358 C  CA  . ASP C  1 187 ? -13.850 -3.872  7.050   1.00 25.82 ? 204  ASP C CA  1 
ATOM   10359 C  C   . ASP C  1 187 ? -14.978 -4.185  8.032   1.00 24.30 ? 204  ASP C C   1 
ATOM   10360 O  O   . ASP C  1 187 ? -14.755 -4.813  9.063   1.00 22.14 ? 204  ASP C O   1 
ATOM   10361 C  CB  . ASP C  1 187 ? -13.022 -5.122  6.803   1.00 27.24 ? 204  ASP C CB  1 
ATOM   10362 C  CG  . ASP C  1 187 ? -13.795 -6.301  6.221   1.00 30.10 ? 204  ASP C CG  1 
ATOM   10363 O  OD1 . ASP C  1 187 ? -14.988 -6.113  5.857   1.00 31.03 ? 204  ASP C OD1 1 
ATOM   10364 O  OD2 . ASP C  1 187 ? -13.202 -7.400  6.131   1.00 29.82 ? 204  ASP C OD2 1 
ATOM   10365 N  N   . VAL C  1 188 ? -16.202 -3.779  7.678   1.00 24.41 ? 205  VAL C N   1 
ATOM   10366 C  CA  . VAL C  1 188 ? -17.373 -4.089  8.483   1.00 24.54 ? 205  VAL C CA  1 
ATOM   10367 C  C   . VAL C  1 188 ? -18.312 -5.025  7.718   1.00 24.88 ? 205  VAL C C   1 
ATOM   10368 O  O   . VAL C  1 188 ? -19.482 -5.154  8.077   1.00 24.89 ? 205  VAL C O   1 
ATOM   10369 C  CB  . VAL C  1 188 ? -18.086 -2.790  8.905   1.00 24.89 ? 205  VAL C CB  1 
ATOM   10370 C  CG1 . VAL C  1 188 ? -17.187 -1.928  9.783   1.00 24.95 ? 205  VAL C CG1 1 
ATOM   10371 C  CG2 . VAL C  1 188 ? -18.605 -1.998  7.709   1.00 24.52 ? 205  VAL C CG2 1 
ATOM   10372 N  N   . GLY C  1 189 ? -17.785 -5.680  6.676   1.00 24.34 ? 206  GLY C N   1 
ATOM   10373 C  CA  . GLY C  1 189 ? -18.573 -6.523  5.791   1.00 25.48 ? 206  GLY C CA  1 
ATOM   10374 C  C   . GLY C  1 189 ? -18.806 -5.853  4.440   1.00 25.19 ? 206  GLY C C   1 
ATOM   10375 O  O   . GLY C  1 189 ? -18.285 -4.770  4.179   1.00 24.99 ? 206  GLY C O   1 
ATOM   10376 N  N   . THR C  1 190 ? -19.609 -6.511  3.593   1.00 26.13 ? 207  THR C N   1 
ATOM   10377 C  CA  . THR C  1 190 ? -19.959 -5.995  2.281   1.00 25.74 ? 207  THR C CA  1 
ATOM   10378 C  C   . THR C  1 190 ? -21.354 -6.493  1.902   1.00 28.91 ? 207  THR C C   1 
ATOM   10379 O  O   . THR C  1 190 ? -21.729 -7.617  2.235   1.00 28.49 ? 207  THR C O   1 
ATOM   10380 C  CB  . THR C  1 190 ? -18.899 -6.418  1.264   1.00 25.50 ? 207  THR C CB  1 
ATOM   10381 O  OG1 . THR C  1 190 ? -19.281 -5.880  0.002   1.00 24.56 ? 207  THR C OG1 1 
ATOM   10382 C  CG2 . THR C  1 190 ? -18.741 -7.925  1.155   1.00 25.17 ? 207  THR C CG2 1 
ATOM   10383 N  N   . ASP C  1 191 ? -22.100 -5.644  1.184   1.00 29.47 ? 208  ASP C N   1 
ATOM   10384 C  CA  . ASP C  1 191 ? -23.419 -5.990  0.678   1.00 31.70 ? 208  ASP C CA  1 
ATOM   10385 C  C   . ASP C  1 191 ? -23.324 -6.502  -0.761  1.00 32.51 ? 208  ASP C C   1 
ATOM   10386 O  O   . ASP C  1 191 ? -24.343 -6.798  -1.381  1.00 33.62 ? 208  ASP C O   1 
ATOM   10387 C  CB  . ASP C  1 191 ? -24.370 -4.809  0.800   1.00 32.18 ? 208  ASP C CB  1 
ATOM   10388 C  CG  . ASP C  1 191 ? -24.801 -4.449  2.215   1.00 34.11 ? 208  ASP C CG  1 
ATOM   10389 O  OD1 . ASP C  1 191 ? -24.349 -5.123  3.167   1.00 31.80 ? 208  ASP C OD1 1 
ATOM   10390 O  OD2 . ASP C  1 191 ? -25.600 -3.494  2.353   1.00 36.41 ? 208  ASP C OD2 1 
ATOM   10391 N  N   . ASN C  1 192 ? -22.098 -6.610  -1.290  1.00 31.69 ? 209  ASN C N   1 
ATOM   10392 C  CA  . ASN C  1 192 ? -21.866 -7.116  -2.633  1.00 30.93 ? 209  ASN C CA  1 
ATOM   10393 C  C   . ASN C  1 192 ? -21.994 -8.640  -2.616  1.00 31.62 ? 209  ASN C C   1 
ATOM   10394 O  O   . ASN C  1 192 ? -21.111 -9.337  -2.115  1.00 28.79 ? 209  ASN C O   1 
ATOM   10395 C  CB  . ASN C  1 192 ? -20.524 -6.608  -3.153  1.00 30.46 ? 209  ASN C CB  1 
ATOM   10396 C  CG  . ASN C  1 192 ? -20.231 -7.041  -4.569  1.00 31.01 ? 209  ASN C CG  1 
ATOM   10397 O  OD1 . ASN C  1 192 ? -20.733 -8.073  -5.029  1.00 31.85 ? 209  ASN C OD1 1 
ATOM   10398 N  ND2 . ASN C  1 192 ? -19.386 -6.293  -5.261  1.00 30.07 ? 209  ASN C ND2 1 
ATOM   10399 N  N   . ILE C  1 193 ? -23.100 -9.154  -3.176  1.00 32.98 ? 210  ILE C N   1 
ATOM   10400 C  CA  . ILE C  1 193 ? -23.426 -10.573 -3.090  1.00 34.67 ? 210  ILE C CA  1 
ATOM   10401 C  C   . ILE C  1 193 ? -22.353 -11.411 -3.784  1.00 32.29 ? 210  ILE C C   1 
ATOM   10402 O  O   . ILE C  1 193 ? -22.054 -12.516 -3.332  1.00 32.78 ? 210  ILE C O   1 
ATOM   10403 C  CB  . ILE C  1 193 ? -24.822 -10.866 -3.676  1.00 37.30 ? 210  ILE C CB  1 
ATOM   10404 C  CG1 . ILE C  1 193 ? -25.932 -10.111 -2.931  1.00 39.72 ? 210  ILE C CG1 1 
ATOM   10405 C  CG2 . ILE C  1 193 ? -25.096 -12.371 -3.716  1.00 38.12 ? 210  ILE C CG2 1 
ATOM   10406 C  CD1 . ILE C  1 193 ? -25.970 -10.346 -1.430  1.00 40.71 ? 210  ILE C CD1 1 
ATOM   10407 N  N   . ALA C  1 194 ? -21.793 -10.886 -4.879  1.00 30.57 ? 211  ALA C N   1 
ATOM   10408 C  CA  . ALA C  1 194 ? -20.806 -11.605 -5.667  1.00 31.82 ? 211  ALA C CA  1 
ATOM   10409 C  C   . ALA C  1 194 ? -19.540 -11.869 -4.848  1.00 32.40 ? 211  ALA C C   1 
ATOM   10410 O  O   . ALA C  1 194 ? -18.914 -12.917 -4.996  1.00 32.30 ? 211  ALA C O   1 
ATOM   10411 C  CB  . ALA C  1 194 ? -20.503 -10.833 -6.929  1.00 32.07 ? 211  ALA C CB  1 
ATOM   10412 N  N   . LEU C  1 195 ? -19.181 -10.923 -3.971  1.00 31.34 ? 212  LEU C N   1 
ATOM   10413 C  CA  . LEU C  1 195 ? -18.004 -11.063 -3.131  1.00 30.57 ? 212  LEU C CA  1 
ATOM   10414 C  C   . LEU C  1 195 ? -18.275 -12.055 -2.002  1.00 29.61 ? 212  LEU C C   1 
ATOM   10415 O  O   . LEU C  1 195 ? -17.394 -12.839 -1.649  1.00 29.19 ? 212  LEU C O   1 
ATOM   10416 C  CB  . LEU C  1 195 ? -17.577 -9.694  -2.599  1.00 29.98 ? 212  LEU C CB  1 
ATOM   10417 C  CG  . LEU C  1 195 ? -17.118 -8.683  -3.656  1.00 30.38 ? 212  LEU C CG  1 
ATOM   10418 C  CD1 . LEU C  1 195 ? -16.687 -7.378  -3.004  1.00 30.35 ? 212  LEU C CD1 1 
ATOM   10419 C  CD2 . LEU C  1 195 ? -16.000 -9.235  -4.515  1.00 31.39 ? 212  LEU C CD2 1 
ATOM   10420 N  N   . LEU C  1 196 ? -19.493 -12.032 -1.446  1.00 28.70 ? 213  LEU C N   1 
ATOM   10421 C  CA  . LEU C  1 196 ? -19.843 -12.910 -0.337  1.00 30.31 ? 213  LEU C CA  1 
ATOM   10422 C  C   . LEU C  1 196 ? -19.834 -14.378 -0.768  1.00 30.33 ? 213  LEU C C   1 
ATOM   10423 O  O   . LEU C  1 196 ? -19.735 -15.259 0.087   1.00 31.18 ? 213  LEU C O   1 
ATOM   10424 C  CB  . LEU C  1 196 ? -21.203 -12.521 0.246   1.00 31.44 ? 213  LEU C CB  1 
ATOM   10425 C  CG  . LEU C  1 196 ? -21.272 -11.173 0.971   1.00 32.51 ? 213  LEU C CG  1 
ATOM   10426 C  CD1 . LEU C  1 196 ? -22.688 -10.896 1.449   1.00 33.42 ? 213  LEU C CD1 1 
ATOM   10427 C  CD2 . LEU C  1 196 ? -20.305 -11.113 2.138   1.00 32.97 ? 213  LEU C CD2 1 
ATOM   10428 N  N   . LYS C  1 197 ? -19.942 -14.638 -2.079  1.00 30.60 ? 214  LYS C N   1 
ATOM   10429 C  CA  . LYS C  1 197 ? -19.918 -15.993 -2.609  1.00 33.85 ? 214  LYS C CA  1 
ATOM   10430 C  C   . LYS C  1 197 ? -18.542 -16.341 -3.179  1.00 33.05 ? 214  LYS C C   1 
ATOM   10431 O  O   . LYS C  1 197 ? -18.364 -17.427 -3.727  1.00 32.15 ? 214  LYS C O   1 
ATOM   10432 C  CB  . LYS C  1 197 ? -20.922 -16.155 -3.756  1.00 37.54 ? 214  LYS C CB  1 
ATOM   10433 C  CG  . LYS C  1 197 ? -22.388 -15.900 -3.423  1.00 42.62 ? 214  LYS C CG  1 
ATOM   10434 C  CD  . LYS C  1 197 ? -23.327 -16.103 -4.609  1.00 46.97 ? 214  LYS C CD  1 
ATOM   10435 C  CE  . LYS C  1 197 ? -22.856 -15.415 -5.859  1.00 51.29 ? 214  LYS C CE  1 
ATOM   10436 N  NZ  . LYS C  1 197 ? -23.884 -15.382 -6.901  1.00 55.13 ? 214  LYS C NZ  1 
ATOM   10437 N  N   . ASP C  1 198 ? -17.578 -15.419 -3.075  1.00 32.42 ? 215  ASP C N   1 
ATOM   10438 C  CA  . ASP C  1 198 ? -16.296 -15.578 -3.747  1.00 31.37 ? 215  ASP C CA  1 
ATOM   10439 C  C   . ASP C  1 198 ? -15.309 -16.227 -2.778  1.00 29.95 ? 215  ASP C C   1 
ATOM   10440 O  O   . ASP C  1 198 ? -14.946 -15.630 -1.769  1.00 27.82 ? 215  ASP C O   1 
ATOM   10441 C  CB  . ASP C  1 198 ? -15.822 -14.248 -4.311  1.00 33.00 ? 215  ASP C CB  1 
ATOM   10442 C  CG  . ASP C  1 198 ? -14.493 -14.254 -5.052  1.00 34.32 ? 215  ASP C CG  1 
ATOM   10443 O  OD1 . ASP C  1 198 ? -13.902 -15.342 -5.207  1.00 35.66 ? 215  ASP C OD1 1 
ATOM   10444 O  OD2 . ASP C  1 198 ? -14.054 -13.157 -5.461  1.00 36.45 ? 215  ASP C OD2 1 
ATOM   10445 N  N   . PRO C  1 199 ? -14.823 -17.460 -3.051  1.00 29.81 ? 216  PRO C N   1 
ATOM   10446 C  CA  . PRO C  1 199 ? -13.869 -18.110 -2.150  1.00 29.88 ? 216  PRO C CA  1 
ATOM   10447 C  C   . PRO C  1 199 ? -12.528 -17.382 -2.039  1.00 29.35 ? 216  PRO C C   1 
ATOM   10448 O  O   . PRO C  1 199 ? -11.758 -17.667 -1.128  1.00 28.85 ? 216  PRO C O   1 
ATOM   10449 C  CB  . PRO C  1 199 ? -13.722 -19.521 -2.743  1.00 31.29 ? 216  PRO C CB  1 
ATOM   10450 C  CG  . PRO C  1 199 ? -14.068 -19.349 -4.206  1.00 32.06 ? 216  PRO C CG  1 
ATOM   10451 C  CD  . PRO C  1 199 ? -15.152 -18.281 -4.228  1.00 31.43 ? 216  PRO C CD  1 
ATOM   10452 N  N   . PHE C  1 200 ? -12.279 -16.432 -2.954  1.00 29.58 ? 217  PHE C N   1 
ATOM   10453 C  CA  . PHE C  1 200 ? -11.028 -15.694 -3.020  1.00 29.65 ? 217  PHE C CA  1 
ATOM   10454 C  C   . PHE C  1 200 ? -11.176 -14.279 -2.466  1.00 28.51 ? 217  PHE C C   1 
ATOM   10455 O  O   . PHE C  1 200 ? -10.202 -13.528 -2.478  1.00 27.12 ? 217  PHE C O   1 
ATOM   10456 C  CB  . PHE C  1 200 ? -10.577 -15.660 -4.483  1.00 31.87 ? 217  PHE C CB  1 
ATOM   10457 C  CG  . PHE C  1 200 ? -10.289 -17.035 -5.069  1.00 33.01 ? 217  PHE C CG  1 
ATOM   10458 C  CD1 . PHE C  1 200 ? -9.433  -17.922 -4.423  1.00 32.75 ? 217  PHE C CD1 1 
ATOM   10459 C  CD2 . PHE C  1 200 ? -10.902 -17.449 -6.247  1.00 34.92 ? 217  PHE C CD2 1 
ATOM   10460 C  CE1 . PHE C  1 200 ? -9.181  -19.176 -4.955  1.00 34.67 ? 217  PHE C CE1 1 
ATOM   10461 C  CE2 . PHE C  1 200 ? -10.654 -18.711 -6.768  1.00 35.58 ? 217  PHE C CE2 1 
ATOM   10462 C  CZ  . PHE C  1 200 ? -9.796  -19.569 -6.124  1.00 34.19 ? 217  PHE C CZ  1 
ATOM   10463 N  N   . TYR C  1 201 ? -12.381 -13.917 -1.990  1.00 27.19 ? 218  TYR C N   1 
ATOM   10464 C  CA  . TYR C  1 201 ? -12.600 -12.634 -1.335  1.00 27.10 ? 218  TYR C CA  1 
ATOM   10465 C  C   . TYR C  1 201 ? -11.725 -12.571 -0.080  1.00 27.21 ? 218  TYR C C   1 
ATOM   10466 O  O   . TYR C  1 201 ? -11.590 -13.561 0.640   1.00 27.06 ? 218  TYR C O   1 
ATOM   10467 C  CB  . TYR C  1 201 ? -14.081 -12.411 -1.000  1.00 26.17 ? 218  TYR C CB  1 
ATOM   10468 C  CG  . TYR C  1 201 ? -14.371 -11.085 -0.305  1.00 25.07 ? 218  TYR C CG  1 
ATOM   10469 C  CD1 . TYR C  1 201 ? -13.996 -9.873  -0.873  1.00 25.00 ? 218  TYR C CD1 1 
ATOM   10470 C  CD2 . TYR C  1 201 ? -14.958 -11.050 0.953   1.00 24.72 ? 218  TYR C CD2 1 
ATOM   10471 C  CE1 . TYR C  1 201 ? -14.233 -8.668  -0.230  1.00 25.66 ? 218  TYR C CE1 1 
ATOM   10472 C  CE2 . TYR C  1 201 ? -15.201 -9.854  1.607   1.00 25.26 ? 218  TYR C CE2 1 
ATOM   10473 C  CZ  . TYR C  1 201 ? -14.833 -8.658  1.018   1.00 25.30 ? 218  TYR C CZ  1 
ATOM   10474 O  OH  . TYR C  1 201 ? -15.071 -7.494  1.686   1.00 24.35 ? 218  TYR C OH  1 
ATOM   10475 N  N   . MET C  1 202 ? -11.144 -11.395 0.186   1.00 27.18 ? 219  MET C N   1 
ATOM   10476 C  CA  . MET C  1 202 ? -10.114 -11.267 1.207   1.00 28.49 ? 219  MET C CA  1 
ATOM   10477 C  C   . MET C  1 202 ? -10.650 -10.584 2.465   1.00 27.81 ? 219  MET C C   1 
ATOM   10478 O  O   . MET C  1 202 ? -9.869  -10.254 3.353   1.00 27.57 ? 219  MET C O   1 
ATOM   10479 C  CB  . MET C  1 202 ? -8.913  -10.493 0.647   1.00 29.88 ? 219  MET C CB  1 
ATOM   10480 C  CG  . MET C  1 202 ? -8.271  -11.182 -0.540  1.00 32.69 ? 219  MET C CG  1 
ATOM   10481 S  SD  . MET C  1 202 ? -6.727  -10.426 -1.084  1.00 36.66 ? 219  MET C SD  1 
ATOM   10482 C  CE  . MET C  1 202 ? -7.295  -8.866  -1.772  1.00 39.03 ? 219  MET C CE  1 
ATOM   10483 N  N   . GLY C  1 203 ? -11.975 -10.389 2.552   1.00 26.32 ? 220  GLY C N   1 
ATOM   10484 C  CA  . GLY C  1 203 ? -12.579 -9.689  3.674   1.00 26.19 ? 220  GLY C CA  1 
ATOM   10485 C  C   . GLY C  1 203 ? -13.488 -10.596 4.501   1.00 26.88 ? 220  GLY C C   1 
ATOM   10486 O  O   . GLY C  1 203 ? -13.539 -11.804 4.280   1.00 27.27 ? 220  GLY C O   1 
ATOM   10487 N  N   . LEU C  1 204 ? -14.193 -9.992  5.466   1.00 26.49 ? 221  LEU C N   1 
ATOM   10488 C  CA  . LEU C  1 204 ? -15.158 -10.700 6.294   1.00 26.77 ? 221  LEU C CA  1 
ATOM   10489 C  C   . LEU C  1 204 ? -16.343 -11.122 5.430   1.00 26.32 ? 221  LEU C C   1 
ATOM   10490 O  O   . LEU C  1 204 ? -16.842 -10.326 4.634   1.00 24.99 ? 221  LEU C O   1 
ATOM   10491 C  CB  . LEU C  1 204 ? -15.639 -9.822  7.449   1.00 27.80 ? 221  LEU C CB  1 
ATOM   10492 C  CG  . LEU C  1 204 ? -14.619 -9.480  8.540   1.00 29.35 ? 221  LEU C CG  1 
ATOM   10493 C  CD1 . LEU C  1 204 ? -15.275 -8.524  9.528   1.00 29.53 ? 221  LEU C CD1 1 
ATOM   10494 C  CD2 . LEU C  1 204 ? -14.084 -10.714 9.252   1.00 29.17 ? 221  LEU C CD2 1 
ATOM   10495 N  N   . TYR C  1 205 ? -16.795 -12.370 5.620   1.00 26.30 ? 222  TYR C N   1 
ATOM   10496 C  CA  . TYR C  1 205 ? -17.968 -12.887 4.933   1.00 26.21 ? 222  TYR C CA  1 
ATOM   10497 C  C   . TYR C  1 205 ? -19.216 -12.548 5.746   1.00 27.19 ? 222  TYR C C   1 
ATOM   10498 O  O   . TYR C  1 205 ? -19.776 -13.399 6.438   1.00 28.10 ? 222  TYR C O   1 
ATOM   10499 C  CB  . TYR C  1 205 ? -17.836 -14.393 4.687   1.00 26.28 ? 222  TYR C CB  1 
ATOM   10500 C  CG  . TYR C  1 205 ? -16.808 -14.775 3.633   1.00 25.82 ? 222  TYR C CG  1 
ATOM   10501 C  CD1 . TYR C  1 205 ? -17.030 -14.524 2.285   1.00 25.74 ? 222  TYR C CD1 1 
ATOM   10502 C  CD2 . TYR C  1 205 ? -15.620 -15.403 3.988   1.00 26.46 ? 222  TYR C CD2 1 
ATOM   10503 C  CE1 . TYR C  1 205 ? -16.100 -14.881 1.320   1.00 26.43 ? 222  TYR C CE1 1 
ATOM   10504 C  CE2 . TYR C  1 205 ? -14.681 -15.762 3.034   1.00 27.11 ? 222  TYR C CE2 1 
ATOM   10505 C  CZ  . TYR C  1 205 ? -14.919 -15.500 1.698   1.00 26.54 ? 222  TYR C CZ  1 
ATOM   10506 O  OH  . TYR C  1 205 ? -13.978 -15.863 0.778   1.00 26.07 ? 222  TYR C OH  1 
ATOM   10507 N  N   . GLN C  1 206 ? -19.624 -11.278 5.678   1.00 27.04 ? 223  GLN C N   1 
ATOM   10508 C  CA  . GLN C  1 206 ? -20.862 -10.824 6.290   1.00 27.01 ? 223  GLN C CA  1 
ATOM   10509 C  C   . GLN C  1 206 ? -21.341 -9.579  5.549   1.00 27.24 ? 223  GLN C C   1 
ATOM   10510 O  O   . GLN C  1 206 ? -20.559 -8.894  4.886   1.00 25.60 ? 223  GLN C O   1 
ATOM   10511 C  CB  . GLN C  1 206 ? -20.690 -10.522 7.782   1.00 27.89 ? 223  GLN C CB  1 
ATOM   10512 C  CG  . GLN C  1 206 ? -19.769 -9.340  8.072   1.00 28.63 ? 223  GLN C CG  1 
ATOM   10513 C  CD  . GLN C  1 206 ? -19.744 -8.913  9.522   1.00 29.18 ? 223  GLN C CD  1 
ATOM   10514 O  OE1 . GLN C  1 206 ? -20.214 -7.826  9.882   1.00 31.00 ? 223  GLN C OE1 1 
ATOM   10515 N  NE2 . GLN C  1 206 ? -19.163 -9.750  10.368  1.00 28.66 ? 223  GLN C NE2 1 
ATOM   10516 N  N   . LYS C  1 207 ? -22.639 -9.292  5.682   1.00 27.60 ? 224  LYS C N   1 
ATOM   10517 C  CA  . LYS C  1 207 ? -23.203 -8.031  5.230   1.00 29.02 ? 224  LYS C CA  1 
ATOM   10518 C  C   . LYS C  1 207 ? -22.659 -6.915  6.121   1.00 26.61 ? 224  LYS C C   1 
ATOM   10519 O  O   . LYS C  1 207 ? -22.209 -7.175  7.235   1.00 25.45 ? 224  LYS C O   1 
ATOM   10520 C  CB  . LYS C  1 207 ? -24.736 -8.058  5.312   1.00 31.80 ? 224  LYS C CB  1 
ATOM   10521 C  CG  . LYS C  1 207 ? -25.431 -9.204  4.581   1.00 34.91 ? 224  LYS C CG  1 
ATOM   10522 C  CD  . LYS C  1 207 ? -25.506 -9.077  3.066   1.00 39.00 ? 224  LYS C CD  1 
ATOM   10523 C  CE  . LYS C  1 207 ? -26.378 -7.953  2.600   1.00 42.86 ? 224  LYS C CE  1 
ATOM   10524 N  NZ  . LYS C  1 207 ? -27.729 -7.996  3.169   1.00 45.17 ? 224  LYS C NZ  1 
ATOM   10525 N  N   . ARG C  1 208 ? -22.751 -5.671  5.637   1.00 26.28 ? 225  ARG C N   1 
ATOM   10526 C  CA  . ARG C  1 208 ? -22.262 -4.511  6.369   1.00 25.85 ? 225  ARG C CA  1 
ATOM   10527 C  C   . ARG C  1 208 ? -23.001 -4.338  7.694   1.00 27.04 ? 225  ARG C C   1 
ATOM   10528 O  O   . ARG C  1 208 ? -24.231 -4.335  7.732   1.00 27.88 ? 225  ARG C O   1 
ATOM   10529 C  CB  . ARG C  1 208 ? -22.400 -3.241  5.524   1.00 25.41 ? 225  ARG C CB  1 
ATOM   10530 C  CG  . ARG C  1 208 ? -21.368 -3.168  4.409   1.00 24.87 ? 225  ARG C CG  1 
ATOM   10531 C  CD  . ARG C  1 208 ? -21.406 -1.860  3.630   1.00 24.86 ? 225  ARG C CD  1 
ATOM   10532 N  NE  . ARG C  1 208 ? -20.288 -1.787  2.677   1.00 24.02 ? 225  ARG C NE  1 
ATOM   10533 C  CZ  . ARG C  1 208 ? -19.010 -1.616  2.999   1.00 23.73 ? 225  ARG C CZ  1 
ATOM   10534 N  NH1 . ARG C  1 208 ? -18.671 -1.167  4.194   1.00 23.85 ? 225  ARG C NH1 1 
ATOM   10535 N  NH2 . ARG C  1 208 ? -18.069 -1.837  2.099   1.00 24.15 ? 225  ARG C NH2 1 
ATOM   10536 N  N   . ASP C  1 209 ? -22.235 -4.179  8.778   1.00 27.46 ? 226  ASP C N   1 
ATOM   10537 C  CA  . ASP C  1 209 ? -22.786 -3.793  10.065  1.00 29.24 ? 226  ASP C CA  1 
ATOM   10538 C  C   . ASP C  1 209 ? -23.213 -2.330  9.977   1.00 30.39 ? 226  ASP C C   1 
ATOM   10539 O  O   . ASP C  1 209 ? -22.392 -1.469  9.658   1.00 29.15 ? 226  ASP C O   1 
ATOM   10540 C  CB  . ASP C  1 209 ? -21.778 -4.000  11.184  1.00 28.80 ? 226  ASP C CB  1 
ATOM   10541 C  CG  . ASP C  1 209 ? -22.324 -3.932  12.604  1.00 30.20 ? 226  ASP C CG  1 
ATOM   10542 O  OD1 . ASP C  1 209 ? -23.211 -3.084  12.866  1.00 30.66 ? 226  ASP C OD1 1 
ATOM   10543 O  OD2 . ASP C  1 209 ? -21.828 -4.704  13.453  1.00 29.89 ? 226  ASP C OD2 1 
ATOM   10544 N  N   . ARG C  1 210 ? -24.499 -2.066  10.247  1.00 31.68 ? 227  ARG C N   1 
ATOM   10545 C  CA  . ARG C  1 210 ? -25.047 -0.717  10.198  1.00 32.27 ? 227  ARG C CA  1 
ATOM   10546 C  C   . ARG C  1 210 ? -25.589 -0.318  11.567  1.00 30.99 ? 227  ARG C C   1 
ATOM   10547 O  O   . ARG C  1 210 ? -26.371 0.624   11.673  1.00 32.76 ? 227  ARG C O   1 
ATOM   10548 C  CB  . ARG C  1 210 ? -26.135 -0.643  9.122   1.00 34.21 ? 227  ARG C CB  1 
ATOM   10549 C  CG  . ARG C  1 210 ? -25.574 -0.835  7.720   1.00 35.86 ? 227  ARG C CG  1 
ATOM   10550 C  CD  . ARG C  1 210 ? -26.666 -0.998  6.688   1.00 37.53 ? 227  ARG C CD  1 
ATOM   10551 N  NE  . ARG C  1 210 ? -26.122 -1.275  5.354   1.00 38.14 ? 227  ARG C NE  1 
ATOM   10552 C  CZ  . ARG C  1 210 ? -25.403 -0.435  4.616   1.00 37.91 ? 227  ARG C CZ  1 
ATOM   10553 N  NH1 . ARG C  1 210 ? -25.139 0.783   5.048   1.00 39.50 ? 227  ARG C NH1 1 
ATOM   10554 N  NH2 . ARG C  1 210 ? -24.967 -0.813  3.430   1.00 37.51 ? 227  ARG C NH2 1 
ATOM   10555 N  N   . THR C  1 211 ? -25.155 -1.031  12.610  1.00 29.16 ? 228  THR C N   1 
ATOM   10556 C  CA  . THR C  1 211 ? -25.584 -0.762  13.970  1.00 28.51 ? 228  THR C CA  1 
ATOM   10557 C  C   . THR C  1 211 ? -24.680 0.315   14.562  1.00 27.24 ? 228  THR C C   1 
ATOM   10558 O  O   . THR C  1 211 ? -23.796 0.840   13.886  1.00 26.40 ? 228  THR C O   1 
ATOM   10559 C  CB  . THR C  1 211 ? -25.544 -2.053  14.790  1.00 30.24 ? 228  THR C CB  1 
ATOM   10560 O  OG1 . THR C  1 211 ? -24.175 -2.422  14.942  1.00 29.80 ? 228  THR C OG1 1 
ATOM   10561 C  CG2 . THR C  1 211 ? -26.296 -3.196  14.131  1.00 31.45 ? 228  THR C CG2 1 
ATOM   10562 N  N   . GLN C  1 212 ? -24.903 0.619   15.844  1.00 26.49 ? 229  GLN C N   1 
ATOM   10563 C  CA  . GLN C  1 212 ? -24.029 1.505   16.592  1.00 27.59 ? 229  GLN C CA  1 
ATOM   10564 C  C   . GLN C  1 212 ? -22.588 0.984   16.583  1.00 27.04 ? 229  GLN C C   1 
ATOM   10565 O  O   . GLN C  1 212 ? -21.657 1.769   16.743  1.00 24.98 ? 229  GLN C O   1 
ATOM   10566 C  CB  . GLN C  1 212 ? -24.555 1.640   18.021  1.00 29.74 ? 229  GLN C CB  1 
ATOM   10567 C  CG  . GLN C  1 212 ? -23.789 2.629   18.894  1.00 30.82 ? 229  GLN C CG  1 
ATOM   10568 C  CD  . GLN C  1 212 ? -23.702 4.017   18.297  1.00 33.10 ? 229  GLN C CD  1 
ATOM   10569 O  OE1 . GLN C  1 212 ? -24.691 4.568   17.802  1.00 35.63 ? 229  GLN C OE1 1 
ATOM   10570 N  NE2 . GLN C  1 212 ? -22.517 4.608   18.347  1.00 35.30 ? 229  GLN C NE2 1 
ATOM   10571 N  N   . GLN C  1 213 ? -22.404 -0.334  16.411  1.00 25.63 ? 230  GLN C N   1 
ATOM   10572 C  CA  . GLN C  1 213 ? -21.070 -0.926  16.393  1.00 26.69 ? 230  GLN C CA  1 
ATOM   10573 C  C   . GLN C  1 213 ? -20.217 -0.320  15.277  1.00 25.04 ? 230  GLN C C   1 
ATOM   10574 O  O   . GLN C  1 213 ? -19.007 -0.181  15.441  1.00 25.31 ? 230  GLN C O   1 
ATOM   10575 C  CB  . GLN C  1 213 ? -21.156 -2.447  16.261  1.00 28.36 ? 230  GLN C CB  1 
ATOM   10576 C  CG  . GLN C  1 213 ? -21.798 -3.128  17.466  1.00 31.04 ? 230  GLN C CG  1 
ATOM   10577 C  CD  . GLN C  1 213 ? -21.835 -4.636  17.357  1.00 35.09 ? 230  GLN C CD  1 
ATOM   10578 O  OE1 . GLN C  1 213 ? -21.530 -5.218  16.310  1.00 37.63 ? 230  GLN C OE1 1 
ATOM   10579 N  NE2 . GLN C  1 213 ? -22.219 -5.285  18.447  1.00 36.81 ? 230  GLN C NE2 1 
ATOM   10580 N  N   . TYR C  1 214 ? -20.846 0.045   14.152  1.00 23.66 ? 231  TYR C N   1 
ATOM   10581 C  CA  . TYR C  1 214 ? -20.142 0.668   13.041  1.00 23.77 ? 231  TYR C CA  1 
ATOM   10582 C  C   . TYR C  1 214 ? -19.570 2.016   13.481  1.00 24.52 ? 231  TYR C C   1 
ATOM   10583 O  O   . TYR C  1 214 ? -18.365 2.253   13.361  1.00 22.85 ? 231  TYR C O   1 
ATOM   10584 C  CB  . TYR C  1 214 ? -21.063 0.810   11.823  1.00 24.22 ? 231  TYR C CB  1 
ATOM   10585 C  CG  . TYR C  1 214 ? -20.475 1.610   10.668  1.00 24.11 ? 231  TYR C CG  1 
ATOM   10586 C  CD1 . TYR C  1 214 ? -19.515 1.060   9.828   1.00 25.10 ? 231  TYR C CD1 1 
ATOM   10587 C  CD2 . TYR C  1 214 ? -20.864 2.923   10.428  1.00 24.38 ? 231  TYR C CD2 1 
ATOM   10588 C  CE1 . TYR C  1 214 ? -18.964 1.783   8.782   1.00 24.14 ? 231  TYR C CE1 1 
ATOM   10589 C  CE2 . TYR C  1 214 ? -20.327 3.656   9.382   1.00 24.48 ? 231  TYR C CE2 1 
ATOM   10590 C  CZ  . TYR C  1 214 ? -19.371 3.086   8.559   1.00 24.34 ? 231  TYR C CZ  1 
ATOM   10591 O  OH  . TYR C  1 214 ? -18.835 3.802   7.531   1.00 23.57 ? 231  TYR C OH  1 
ATOM   10592 N  N   . ASP C  1 215 ? -20.451 2.899   13.965  1.00 23.71 ? 232  ASP C N   1 
ATOM   10593 C  CA  . ASP C  1 215 ? -20.052 4.202   14.477  1.00 25.26 ? 232  ASP C CA  1 
ATOM   10594 C  C   . ASP C  1 215 ? -18.996 4.065   15.568  1.00 23.78 ? 232  ASP C C   1 
ATOM   10595 O  O   . ASP C  1 215 ? -18.040 4.843   15.593  1.00 24.00 ? 232  ASP C O   1 
ATOM   10596 C  CB  . ASP C  1 215 ? -21.238 4.987   15.015  1.00 26.45 ? 232  ASP C CB  1 
ATOM   10597 C  CG  . ASP C  1 215 ? -22.215 5.479   13.963  1.00 28.96 ? 232  ASP C CG  1 
ATOM   10598 O  OD1 . ASP C  1 215 ? -22.446 4.740   12.983  1.00 31.43 ? 232  ASP C OD1 1 
ATOM   10599 O  OD2 . ASP C  1 215 ? -22.764 6.581   14.145  1.00 31.85 ? 232  ASP C OD2 1 
ATOM   10600 N  N   . ASP C  1 216 ? -19.176 3.097   16.475  1.00 22.82 ? 233  ASP C N   1 
ATOM   10601 C  CA  . ASP C  1 216 ? -18.248 2.912   17.580  1.00 24.32 ? 233  ASP C CA  1 
ATOM   10602 C  C   . ASP C  1 216 ? -16.860 2.529   17.058  1.00 23.17 ? 233  ASP C C   1 
ATOM   10603 O  O   . ASP C  1 216 ? -15.856 2.925   17.647  1.00 23.68 ? 233  ASP C O   1 
ATOM   10604 C  CB  . ASP C  1 216 ? -18.738 1.879   18.584  1.00 26.38 ? 233  ASP C CB  1 
ATOM   10605 C  CG  . ASP C  1 216 ? -19.920 2.276   19.461  1.00 28.45 ? 233  ASP C CG  1 
ATOM   10606 O  OD1 . ASP C  1 216 ? -20.289 3.472   19.482  1.00 30.78 ? 233  ASP C OD1 1 
ATOM   10607 O  OD2 . ASP C  1 216 ? -20.485 1.368   20.096  1.00 32.43 ? 233  ASP C OD2 1 
ATOM   10608 N  N   . LEU C  1 217 ? -16.809 1.754   15.967  1.00 21.70 ? 234  LEU C N   1 
ATOM   10609 C  CA  . LEU C  1 217 ? -15.546 1.303   15.401  1.00 21.68 ? 234  LEU C CA  1 
ATOM   10610 C  C   . LEU C  1 217 ? -14.810 2.479   14.762  1.00 21.21 ? 234  LEU C C   1 
ATOM   10611 O  O   . LEU C  1 217 ? -13.590 2.590   14.895  1.00 21.16 ? 234  LEU C O   1 
ATOM   10612 C  CB  . LEU C  1 217 ? -15.778 0.183   14.389  1.00 21.44 ? 234  LEU C CB  1 
ATOM   10613 C  CG  . LEU C  1 217 ? -14.514 -0.459  13.804  1.00 20.48 ? 234  LEU C CG  1 
ATOM   10614 C  CD1 . LEU C  1 217 ? -13.790 -1.294  14.834  1.00 20.50 ? 234  LEU C CD1 1 
ATOM   10615 C  CD2 . LEU C  1 217 ? -14.842 -1.280  12.581  1.00 20.63 ? 234  LEU C CD2 1 
ATOM   10616 N  N   . ILE C  1 218 ? -15.553 3.354   14.070  1.00 21.04 ? 235  ILE C N   1 
ATOM   10617 C  CA  . ILE C  1 218 ? -14.958 4.522   13.434  1.00 21.35 ? 235  ILE C CA  1 
ATOM   10618 C  C   . ILE C  1 218 ? -14.411 5.449   14.525  1.00 22.56 ? 235  ILE C C   1 
ATOM   10619 O  O   . ILE C  1 218 ? -13.301 5.969   14.399  1.00 23.57 ? 235  ILE C O   1 
ATOM   10620 C  CB  . ILE C  1 218 ? -15.956 5.230   12.494  1.00 21.09 ? 235  ILE C CB  1 
ATOM   10621 C  CG1 . ILE C  1 218 ? -16.492 4.304   11.382  1.00 22.24 ? 235  ILE C CG1 1 
ATOM   10622 C  CG2 . ILE C  1 218 ? -15.351 6.506   11.905  1.00 20.78 ? 235  ILE C CG2 1 
ATOM   10623 C  CD1 . ILE C  1 218 ? -15.438 3.758   10.433  1.00 22.39 ? 235  ILE C CD1 1 
ATOM   10624 N  N   . ASP C  1 219 ? -15.175 5.627   15.611  1.00 23.18 ? 236  ASP C N   1 
ATOM   10625 C  CA  . ASP C  1 219 ? -14.735 6.415   16.758  1.00 24.34 ? 236  ASP C CA  1 
ATOM   10626 C  C   . ASP C  1 219 ? -13.439 5.864   17.354  1.00 22.86 ? 236  ASP C C   1 
ATOM   10627 O  O   . ASP C  1 219 ? -12.547 6.632   17.703  1.00 22.00 ? 236  ASP C O   1 
ATOM   10628 C  CB  . ASP C  1 219 ? -15.779 6.445   17.864  1.00 26.85 ? 236  ASP C CB  1 
ATOM   10629 C  CG  . ASP C  1 219 ? -16.901 7.459   17.708  1.00 30.13 ? 236  ASP C CG  1 
ATOM   10630 O  OD1 . ASP C  1 219 ? -16.780 8.373   16.861  1.00 33.86 ? 236  ASP C OD1 1 
ATOM   10631 O  OD2 . ASP C  1 219 ? -17.902 7.308   18.428  1.00 35.55 ? 236  ASP C OD2 1 
ATOM   10632 N  N   . GLU C  1 220 ? -13.371 4.537   17.507  1.00 21.42 ? 237  GLU C N   1 
ATOM   10633 C  CA  . GLU C  1 220 ? -12.226 3.867   18.105  1.00 22.09 ? 237  GLU C CA  1 
ATOM   10634 C  C   . GLU C  1 220 ? -10.976 4.081   17.246  1.00 21.52 ? 237  GLU C C   1 
ATOM   10635 O  O   . GLU C  1 220 ? -9.891  4.316   17.778  1.00 21.02 ? 237  GLU C O   1 
ATOM   10636 C  CB  . GLU C  1 220 ? -12.555 2.385   18.275  1.00 22.83 ? 237  GLU C CB  1 
ATOM   10637 C  CG  . GLU C  1 220 ? -11.584 1.653   19.197  1.00 24.11 ? 237  GLU C CG  1 
ATOM   10638 C  CD  . GLU C  1 220 ? -11.830 0.161   19.330  1.00 24.79 ? 237  GLU C CD  1 
ATOM   10639 O  OE1 . GLU C  1 220 ? -12.902 -0.335  18.907  1.00 25.52 ? 237  GLU C OE1 1 
ATOM   10640 O  OE2 . GLU C  1 220 ? -10.923 -0.514  19.855  1.00 24.30 ? 237  GLU C OE2 1 
ATOM   10641 N  N   . PHE C  1 221 ? -11.147 3.996   15.921  1.00 21.36 ? 238  PHE C N   1 
ATOM   10642 C  CA  . PHE C  1 221 ? -10.082 4.241   14.958  1.00 20.86 ? 238  PHE C CA  1 
ATOM   10643 C  C   . PHE C  1 221 ? -9.543  5.667   15.087  1.00 20.87 ? 238  PHE C C   1 
ATOM   10644 O  O   . PHE C  1 221 ? -8.332  5.862   15.193  1.00 20.90 ? 238  PHE C O   1 
ATOM   10645 C  CB  . PHE C  1 221 ? -10.625 3.922   13.560  1.00 20.71 ? 238  PHE C CB  1 
ATOM   10646 C  CG  . PHE C  1 221 ? -9.899  4.620   12.420  1.00 21.01 ? 238  PHE C CG  1 
ATOM   10647 C  CD1 . PHE C  1 221 ? -8.602  4.265   12.074  1.00 21.82 ? 238  PHE C CD1 1 
ATOM   10648 C  CD2 . PHE C  1 221 ? -10.529 5.620   11.685  1.00 22.58 ? 238  PHE C CD2 1 
ATOM   10649 C  CE1 . PHE C  1 221 ? -7.952  4.903   11.028  1.00 21.94 ? 238  PHE C CE1 1 
ATOM   10650 C  CE2 . PHE C  1 221 ? -9.874  6.252   10.638  1.00 22.94 ? 238  PHE C CE2 1 
ATOM   10651 C  CZ  . PHE C  1 221 ? -8.586  5.891   10.316  1.00 22.61 ? 238  PHE C CZ  1 
ATOM   10652 N  N   . MET C  1 222 ? -10.439 6.663   15.072  1.00 20.10 ? 239  MET C N   1 
ATOM   10653 C  CA  . MET C  1 222 ? -10.041 8.061   15.177  1.00 20.68 ? 239  MET C CA  1 
ATOM   10654 C  C   . MET C  1 222 ? -9.252  8.299   16.466  1.00 21.52 ? 239  MET C C   1 
ATOM   10655 O  O   . MET C  1 222 ? -8.229  8.988   16.448  1.00 21.21 ? 239  MET C O   1 
ATOM   10656 C  CB  . MET C  1 222 ? -11.259 8.994   15.137  1.00 20.72 ? 239  MET C CB  1 
ATOM   10657 C  CG  . MET C  1 222 ? -12.047 8.925   13.844  1.00 21.32 ? 239  MET C CG  1 
ATOM   10658 S  SD  . MET C  1 222 ? -11.169 9.484   12.371  1.00 21.79 ? 239  MET C SD  1 
ATOM   10659 C  CE  . MET C  1 222 ? -11.217 11.268  12.578  1.00 21.98 ? 239  MET C CE  1 
ATOM   10660 N  N   . LYS C  1 223 ? -9.715  7.714   17.579  1.00 21.42 ? 240  LYS C N   1 
ATOM   10661 C  CA  . LYS C  1 223 ? -9.052  7.877   18.864  1.00 23.23 ? 240  LYS C CA  1 
ATOM   10662 C  C   . LYS C  1 223 ? -7.687  7.182   18.873  1.00 22.49 ? 240  LYS C C   1 
ATOM   10663 O  O   . LYS C  1 223 ? -6.724  7.736   19.401  1.00 21.84 ? 240  LYS C O   1 
ATOM   10664 C  CB  . LYS C  1 223 ? -9.948  7.352   19.991  1.00 25.65 ? 240  LYS C CB  1 
ATOM   10665 C  CG  . LYS C  1 223 ? -9.362  7.437   21.387  1.00 27.98 ? 240  LYS C CG  1 
ATOM   10666 C  CD  . LYS C  1 223 ? -10.315 6.969   22.482  1.00 30.81 ? 240  LYS C CD  1 
ATOM   10667 C  CE  . LYS C  1 223 ? -9.781  7.253   23.853  1.00 33.42 ? 240  LYS C CE  1 
ATOM   10668 N  NZ  . LYS C  1 223 ? -8.474  6.625   24.074  1.00 33.87 ? 240  LYS C NZ  1 
ATOM   10669 N  N   . ALA C  1 224 ? -7.617  5.965   18.316  1.00 21.45 ? 241  ALA C N   1 
ATOM   10670 C  CA  . ALA C  1 224 ? -6.389  5.182   18.315  1.00 21.50 ? 241  ALA C CA  1 
ATOM   10671 C  C   . ALA C  1 224 ? -5.303  5.863   17.479  1.00 21.11 ? 241  ALA C C   1 
ATOM   10672 O  O   . ALA C  1 224 ? -4.148  5.902   17.896  1.00 20.37 ? 241  ALA C O   1 
ATOM   10673 C  CB  . ALA C  1 224 ? -6.661  3.783   17.806  1.00 22.40 ? 241  ALA C CB  1 
ATOM   10674 N  N   . ILE C  1 225 ? -5.674  6.377   16.296  1.00 21.01 ? 242  ILE C N   1 
ATOM   10675 C  CA  . ILE C  1 225 ? -4.724  7.027   15.406  1.00 21.39 ? 242  ILE C CA  1 
ATOM   10676 C  C   . ILE C  1 225 ? -4.125  8.250   16.100  1.00 21.68 ? 242  ILE C C   1 
ATOM   10677 O  O   . ILE C  1 225 ? -2.909  8.439   16.070  1.00 21.17 ? 242  ILE C O   1 
ATOM   10678 C  CB  . ILE C  1 225 ? -5.371  7.408   14.060  1.00 22.21 ? 242  ILE C CB  1 
ATOM   10679 C  CG1 . ILE C  1 225 ? -5.694  6.185   13.203  1.00 23.17 ? 242  ILE C CG1 1 
ATOM   10680 C  CG2 . ILE C  1 225 ? -4.500  8.404   13.289  1.00 22.10 ? 242  ILE C CG2 1 
ATOM   10681 C  CD1 . ILE C  1 225 ? -4.476  5.423   12.709  1.00 23.03 ? 242  ILE C CD1 1 
ATOM   10682 N  N   . THR C  1 226 ? -4.983  9.084   16.705  1.00 21.35 ? 243  THR C N   1 
ATOM   10683 C  CA  . THR C  1 226 ? -4.544  10.342  17.291  1.00 21.80 ? 243  THR C CA  1 
ATOM   10684 C  C   . THR C  1 226 ? -3.851  10.115  18.638  1.00 22.89 ? 243  THR C C   1 
ATOM   10685 O  O   . THR C  1 226 ? -2.959  10.888  18.999  1.00 22.36 ? 243  THR C O   1 
ATOM   10686 C  CB  . THR C  1 226 ? -5.711  11.323  17.398  1.00 22.27 ? 243  THR C CB  1 
ATOM   10687 O  OG1 . THR C  1 226 ? -6.768  10.697  18.121  1.00 22.03 ? 243  THR C OG1 1 
ATOM   10688 C  CG2 . THR C  1 226 ? -6.200  11.760  16.030  1.00 22.68 ? 243  THR C CG2 1 
ATOM   10689 N  N   . ASP C  1 227 ? -4.240  9.065   19.373  1.00 22.35 ? 244  ASP C N   1 
ATOM   10690 C  CA  . ASP C  1 227 ? -3.515  8.682   20.578  1.00 23.42 ? 244  ASP C CA  1 
ATOM   10691 C  C   . ASP C  1 227 ? -2.065  8.328   20.238  1.00 22.64 ? 244  ASP C C   1 
ATOM   10692 O  O   . ASP C  1 227 ? -1.152  8.731   20.957  1.00 22.16 ? 244  ASP C O   1 
ATOM   10693 C  CB  . ASP C  1 227 ? -4.173  7.530   21.324  1.00 24.04 ? 244  ASP C CB  1 
ATOM   10694 C  CG  . ASP C  1 227 ? -5.414  7.870   22.142  1.00 26.13 ? 244  ASP C CG  1 
ATOM   10695 O  OD1 . ASP C  1 227 ? -5.733  9.073   22.271  1.00 25.26 ? 244  ASP C OD1 1 
ATOM   10696 O  OD2 . ASP C  1 227 ? -6.060  6.919   22.635  1.00 26.84 ? 244  ASP C OD2 1 
ATOM   10697 N  N   . ARG C  1 228 ? -1.849  7.566   19.157  1.00 21.13 ? 245  ARG C N   1 
ATOM   10698 C  CA  . ARG C  1 228 ? -0.500  7.148   18.793  1.00 21.35 ? 245  ARG C CA  1 
ATOM   10699 C  C   . ARG C  1 228 ? 0.272   8.303   18.154  1.00 21.23 ? 245  ARG C C   1 
ATOM   10700 O  O   . ARG C  1 228 ? 1.422   8.549   18.517  1.00 20.90 ? 245  ARG C O   1 
ATOM   10701 C  CB  . ARG C  1 228 ? -0.443  5.925   17.867  1.00 21.99 ? 245  ARG C CB  1 
ATOM   10702 C  CG  . ARG C  1 228 ? 1.003   5.529   17.583  1.00 22.29 ? 245  ARG C CG  1 
ATOM   10703 C  CD  . ARG C  1 228 ? 1.218   4.191   16.898  1.00 22.57 ? 245  ARG C CD  1 
ATOM   10704 N  NE  . ARG C  1 228 ? 2.657   3.980   16.682  1.00 22.02 ? 245  ARG C NE  1 
ATOM   10705 C  CZ  . ARG C  1 228 ? 3.211   2.997   15.996  1.00 21.90 ? 245  ARG C CZ  1 
ATOM   10706 N  NH1 . ARG C  1 228 ? 2.465   2.070   15.428  1.00 22.17 ? 245  ARG C NH1 1 
ATOM   10707 N  NH2 . ARG C  1 228 ? 4.528   2.940   15.875  1.00 22.24 ? 245  ARG C NH2 1 
ATOM   10708 N  N   . TYR C  1 229 ? -0.344  9.009   17.196  1.00 19.99 ? 246  TYR C N   1 
ATOM   10709 C  CA  . TYR C  1 229 ? 0.415   9.870   16.300  1.00 20.08 ? 246  TYR C CA  1 
ATOM   10710 C  C   . TYR C  1 229 ? 0.202   11.358  16.583  1.00 20.73 ? 246  TYR C C   1 
ATOM   10711 O  O   . TYR C  1 229 ? 0.971   12.191  16.096  1.00 19.18 ? 246  TYR C O   1 
ATOM   10712 C  CB  . TYR C  1 229 ? 0.028   9.476   14.873  1.00 19.64 ? 246  TYR C CB  1 
ATOM   10713 C  CG  . TYR C  1 229 ? 0.536   8.109   14.434  1.00 18.75 ? 246  TYR C CG  1 
ATOM   10714 C  CD1 . TYR C  1 229 ? 1.884   7.775   14.540  1.00 18.74 ? 246  TYR C CD1 1 
ATOM   10715 C  CD2 . TYR C  1 229 ? -0.334  7.147   13.933  1.00 18.19 ? 246  TYR C CD2 1 
ATOM   10716 C  CE1 . TYR C  1 229 ? 2.349   6.532   14.143  1.00 18.66 ? 246  TYR C CE1 1 
ATOM   10717 C  CE2 . TYR C  1 229 ? 0.119   5.904   13.524  1.00 18.05 ? 246  TYR C CE2 1 
ATOM   10718 C  CZ  . TYR C  1 229 ? 1.465   5.598   13.633  1.00 18.61 ? 246  TYR C CZ  1 
ATOM   10719 O  OH  . TYR C  1 229 ? 1.929   4.388   13.224  1.00 19.31 ? 246  TYR C OH  1 
ATOM   10720 N  N   . GLY C  1 230 ? -0.846  11.695  17.348  1.00 20.22 ? 247  GLY C N   1 
ATOM   10721 C  CA  . GLY C  1 230 ? -1.090  13.067  17.752  1.00 21.26 ? 247  GLY C CA  1 
ATOM   10722 C  C   . GLY C  1 230 ? -2.406  13.588  17.183  1.00 23.06 ? 247  GLY C C   1 
ATOM   10723 O  O   . GLY C  1 230 ? -2.862  13.138  16.132  1.00 21.17 ? 247  GLY C O   1 
ATOM   10724 N  N   . ARG C  1 231 ? -2.984  14.574  17.874  1.00 24.60 ? 248  ARG C N   1 
ATOM   10725 C  CA  . ARG C  1 231 ? -4.291  15.099  17.505  1.00 27.76 ? 248  ARG C CA  1 
ATOM   10726 C  C   . ARG C  1 231 ? -4.246  15.867  16.184  1.00 24.29 ? 248  ARG C C   1 
ATOM   10727 O  O   . ARG C  1 231 ? -5.287  16.066  15.576  1.00 24.54 ? 248  ARG C O   1 
ATOM   10728 C  CB  . ARG C  1 231 ? -4.875  15.979  18.617  1.00 32.26 ? 248  ARG C CB  1 
ATOM   10729 C  CG  . ARG C  1 231 ? -5.411  15.175  19.794  1.00 37.75 ? 248  ARG C CG  1 
ATOM   10730 C  CD  . ARG C  1 231 ? -6.381  15.972  20.661  1.00 43.08 ? 248  ARG C CD  1 
ATOM   10731 N  NE  . ARG C  1 231 ? -7.735  16.058  20.095  1.00 48.24 ? 248  ARG C NE  1 
ATOM   10732 C  CZ  . ARG C  1 231 ? -8.823  15.444  20.572  1.00 52.34 ? 248  ARG C CZ  1 
ATOM   10733 N  NH1 . ARG C  1 231 ? -8.726  14.550  21.544  1.00 53.81 ? 248  ARG C NH1 1 
ATOM   10734 N  NH2 . ARG C  1 231 ? -10.014 15.705  20.054  1.00 53.27 ? 248  ARG C NH2 1 
ATOM   10735 N  N   . ASN C  1 232 ? -3.066  16.312  15.735  1.00 22.69 ? 249  ASN C N   1 
ATOM   10736 C  CA  . ASN C  1 232 ? -2.998  17.060  14.488  1.00 22.76 ? 249  ASN C CA  1 
ATOM   10737 C  C   . ASN C  1 232 ? -2.817  16.128  13.286  1.00 21.65 ? 249  ASN C C   1 
ATOM   10738 O  O   . ASN C  1 232 ? -2.695  16.614  12.165  1.00 21.65 ? 249  ASN C O   1 
ATOM   10739 C  CB  . ASN C  1 232 ? -1.961  18.180  14.542  1.00 24.14 ? 249  ASN C CB  1 
ATOM   10740 C  CG  . ASN C  1 232 ? -0.531  17.702  14.617  1.00 25.87 ? 249  ASN C CG  1 
ATOM   10741 O  OD1 . ASN C  1 232 ? -0.208  16.601  14.163  1.00 26.66 ? 249  ASN C OD1 1 
ATOM   10742 N  ND2 . ASN C  1 232 ? 0.353   18.535  15.151  1.00 27.68 ? 249  ASN C ND2 1 
ATOM   10743 N  N   . THR C  1 233 ? -2.825  14.803  13.501  1.00 20.06 ? 250  THR C N   1 
ATOM   10744 C  CA  . THR C  1 233 ? -2.659  13.856  12.408  1.00 19.17 ? 250  THR C CA  1 
ATOM   10745 C  C   . THR C  1 233 ? -3.786  14.063  11.397  1.00 18.84 ? 250  THR C C   1 
ATOM   10746 O  O   . THR C  1 233 ? -4.960  14.005  11.765  1.00 18.89 ? 250  THR C O   1 
ATOM   10747 C  CB  . THR C  1 233 ? -2.657  12.421  12.933  1.00 18.93 ? 250  THR C CB  1 
ATOM   10748 O  OG1 . THR C  1 233 ? -1.652  12.316  13.936  1.00 18.88 ? 250  THR C OG1 1 
ATOM   10749 C  CG2 . THR C  1 233 ? -2.397  11.416  11.825  1.00 18.90 ? 250  THR C CG2 1 
ATOM   10750 N  N   . LEU C  1 234 ? -3.419  14.265  10.123  1.00 18.47 ? 251  LEU C N   1 
ATOM   10751 C  CA  . LEU C  1 234 ? -4.389  14.460  9.055   1.00 19.22 ? 251  LEU C CA  1 
ATOM   10752 C  C   . LEU C  1 234 ? -5.073  13.130  8.730   1.00 19.42 ? 251  LEU C C   1 
ATOM   10753 O  O   . LEU C  1 234 ? -4.395  12.142  8.439   1.00 18.26 ? 251  LEU C O   1 
ATOM   10754 C  CB  . LEU C  1 234 ? -3.707  15.052  7.822   1.00 20.13 ? 251  LEU C CB  1 
ATOM   10755 C  CG  . LEU C  1 234 ? -4.592  15.216  6.579   1.00 21.18 ? 251  LEU C CG  1 
ATOM   10756 C  CD1 . LEU C  1 234 ? -5.802  16.078  6.859   1.00 21.68 ? 251  LEU C CD1 1 
ATOM   10757 C  CD2 . LEU C  1 234 ? -3.809  15.807  5.425   1.00 22.56 ? 251  LEU C CD2 1 
ATOM   10758 N  N   . ILE C  1 235 ? -6.416  13.108  8.802   1.00 18.64 ? 252  ILE C N   1 
ATOM   10759 C  CA  . ILE C  1 235 ? -7.187  11.912  8.492   1.00 18.73 ? 252  ILE C CA  1 
ATOM   10760 C  C   . ILE C  1 235 ? -8.205  12.253  7.406   1.00 19.14 ? 252  ILE C C   1 
ATOM   10761 O  O   . ILE C  1 235 ? -9.153  13.002  7.648   1.00 20.07 ? 252  ILE C O   1 
ATOM   10762 C  CB  . ILE C  1 235 ? -7.866  11.337  9.749   1.00 19.34 ? 252  ILE C CB  1 
ATOM   10763 C  CG1 . ILE C  1 235 ? -6.865  11.040  10.873  1.00 20.40 ? 252  ILE C CG1 1 
ATOM   10764 C  CG2 . ILE C  1 235 ? -8.693  10.099  9.400   1.00 19.28 ? 252  ILE C CG2 1 
ATOM   10765 C  CD1 . ILE C  1 235 ? -7.508  10.868  12.239  1.00 20.96 ? 252  ILE C CD1 1 
ATOM   10766 N  N   . GLN C  1 236 ? -8.015  11.678  6.213   1.00 19.53 ? 253  GLN C N   1 
ATOM   10767 C  CA  . GLN C  1 236 ? -8.863  11.973  5.071   1.00 19.00 ? 253  GLN C CA  1 
ATOM   10768 C  C   . GLN C  1 236 ? -9.749  10.767  4.766   1.00 19.16 ? 253  GLN C C   1 
ATOM   10769 O  O   . GLN C  1 236 ? -9.238  9.667   4.546   1.00 18.06 ? 253  GLN C O   1 
ATOM   10770 C  CB  . GLN C  1 236 ? -8.036  12.312  3.835   1.00 20.11 ? 253  GLN C CB  1 
ATOM   10771 C  CG  . GLN C  1 236 ? -8.882  12.838  2.679   1.00 21.33 ? 253  GLN C CG  1 
ATOM   10772 C  CD  . GLN C  1 236 ? -8.607  12.151  1.360   1.00 22.16 ? 253  GLN C CD  1 
ATOM   10773 O  OE1 . GLN C  1 236 ? -7.501  12.203  0.816   1.00 22.07 ? 253  GLN C OE1 1 
ATOM   10774 N  NE2 . GLN C  1 236 ? -9.628  11.500  0.823   1.00 24.96 ? 253  GLN C NE2 1 
ATOM   10775 N  N   . PHE C  1 237 ? -11.070 11.002  4.732   1.00 18.41 ? 254  PHE C N   1 
ATOM   10776 C  CA  . PHE C  1 237 ? -12.059 9.981   4.426   1.00 19.04 ? 254  PHE C CA  1 
ATOM   10777 C  C   . PHE C  1 237 ? -12.255 9.911   2.912   1.00 20.49 ? 254  PHE C C   1 
ATOM   10778 O  O   . PHE C  1 237 ? -12.304 10.940  2.237   1.00 20.74 ? 254  PHE C O   1 
ATOM   10779 C  CB  . PHE C  1 237 ? -13.387 10.278  5.135   1.00 19.94 ? 254  PHE C CB  1 
ATOM   10780 C  CG  . PHE C  1 237 ? -13.449 9.939   6.620   1.00 21.10 ? 254  PHE C CG  1 
ATOM   10781 C  CD1 . PHE C  1 237 ? -12.507 10.436  7.521   1.00 22.47 ? 254  PHE C CD1 1 
ATOM   10782 C  CD2 . PHE C  1 237 ? -14.445 9.103   7.114   1.00 21.06 ? 254  PHE C CD2 1 
ATOM   10783 C  CE1 . PHE C  1 237 ? -12.571 10.116  8.872   1.00 22.27 ? 254  PHE C CE1 1 
ATOM   10784 C  CE2 . PHE C  1 237 ? -14.501 8.782   8.466   1.00 21.89 ? 254  PHE C CE2 1 
ATOM   10785 C  CZ  . PHE C  1 237 ? -13.569 9.291   9.343   1.00 21.60 ? 254  PHE C CZ  1 
ATOM   10786 N  N   . GLU C  1 238 ? -12.397 8.670   2.445   1.00 21.76 ? 255  GLU C N   1 
ATOM   10787 C  CA  . GLU C  1 238 ? -12.506 8.443   0.990   1.00 23.05 ? 255  GLU C CA  1 
ATOM   10788 C  C   . GLU C  1 238 ? -13.420 7.262   0.658   1.00 21.58 ? 255  GLU C C   1 
ATOM   10789 O  O   . GLU C  1 238 ? -13.290 6.219   1.299   1.00 20.78 ? 255  GLU C O   1 
ATOM   10790 C  CB  . GLU C  1 238 ? -11.132 8.152   0.388   1.00 25.24 ? 255  GLU C CB  1 
ATOM   10791 C  CG  . GLU C  1 238 ? -11.143 8.042   -1.133  1.00 27.95 ? 255  GLU C CG  1 
ATOM   10792 C  CD  . GLU C  1 238 ? -10.853 9.337   -1.868  1.00 30.61 ? 255  GLU C CD  1 
ATOM   10793 O  OE1 . GLU C  1 238 ? -10.613 10.368  -1.212  1.00 31.69 ? 255  GLU C OE1 1 
ATOM   10794 O  OE2 . GLU C  1 238 ? -10.867 9.309   -3.111  1.00 34.22 ? 255  GLU C OE2 1 
ATOM   10795 N  N   . ASP C  1 239 ? -14.359 7.475   -0.246  1.00 22.55 ? 256  ASP C N   1 
ATOM   10796 C  CA  . ASP C  1 239 ? -15.198 6.429   -0.823  1.00 23.17 ? 256  ASP C CA  1 
ATOM   10797 C  C   . ASP C  1 239 ? -16.083 5.762   0.233   1.00 22.39 ? 256  ASP C C   1 
ATOM   10798 O  O   . ASP C  1 239 ? -16.390 4.580   0.116   1.00 21.52 ? 256  ASP C O   1 
ATOM   10799 C  CB  . ASP C  1 239 ? -14.379 5.440   -1.644  1.00 24.60 ? 256  ASP C CB  1 
ATOM   10800 C  CG  . ASP C  1 239 ? -13.926 5.920   -3.020  1.00 26.59 ? 256  ASP C CG  1 
ATOM   10801 O  OD1 . ASP C  1 239 ? -14.338 7.022   -3.432  1.00 27.70 ? 256  ASP C OD1 1 
ATOM   10802 O  OD2 . ASP C  1 239 ? -13.162 5.181   -3.679  1.00 29.51 ? 256  ASP C OD2 1 
ATOM   10803 N  N   . PHE C  1 240 ? -16.496 6.531   1.248   1.00 22.60 ? 257  PHE C N   1 
ATOM   10804 C  CA  . PHE C  1 240 ? -17.596 6.153   2.126   1.00 22.61 ? 257  PHE C CA  1 
ATOM   10805 C  C   . PHE C  1 240 ? -18.915 6.414   1.404   1.00 22.66 ? 257  PHE C C   1 
ATOM   10806 O  O   . PHE C  1 240 ? -18.953 7.195   0.461   1.00 22.58 ? 257  PHE C O   1 
ATOM   10807 C  CB  . PHE C  1 240 ? -17.552 6.964   3.426   1.00 22.08 ? 257  PHE C CB  1 
ATOM   10808 C  CG  . PHE C  1 240 ? -16.555 6.448   4.448   1.00 22.35 ? 257  PHE C CG  1 
ATOM   10809 C  CD1 . PHE C  1 240 ? -15.189 6.649   4.277   1.00 23.35 ? 257  PHE C CD1 1 
ATOM   10810 C  CD2 . PHE C  1 240 ? -16.986 5.769   5.581   1.00 21.59 ? 257  PHE C CD2 1 
ATOM   10811 C  CE1 . PHE C  1 240 ? -14.281 6.165   5.204   1.00 23.19 ? 257  PHE C CE1 1 
ATOM   10812 C  CE2 . PHE C  1 240 ? -16.073 5.293   6.508   1.00 22.60 ? 257  PHE C CE2 1 
ATOM   10813 C  CZ  . PHE C  1 240 ? -14.724 5.486   6.318   1.00 22.84 ? 257  PHE C CZ  1 
ATOM   10814 N  N   . GLY C  1 241 ? -19.992 5.765   1.867   1.00 23.06 ? 258  GLY C N   1 
ATOM   10815 C  CA  . GLY C  1 241 ? -21.333 6.077   1.402   1.00 23.55 ? 258  GLY C CA  1 
ATOM   10816 C  C   . GLY C  1 241 ? -21.705 7.514   1.754   1.00 23.91 ? 258  GLY C C   1 
ATOM   10817 O  O   . GLY C  1 241 ? -21.162 8.071   2.700   1.00 23.78 ? 258  GLY C O   1 
ATOM   10818 N  N   . ASN C  1 242 ? -22.651 8.090   1.001   1.00 26.53 ? 259  ASN C N   1 
ATOM   10819 C  CA  . ASN C  1 242 ? -22.978 9.508   1.088   1.00 27.60 ? 259  ASN C CA  1 
ATOM   10820 C  C   . ASN C  1 242 ? -23.383 9.914   2.505   1.00 26.43 ? 259  ASN C C   1 
ATOM   10821 O  O   . ASN C  1 242 ? -22.869 10.900  3.034   1.00 25.82 ? 259  ASN C O   1 
ATOM   10822 C  CB  . ASN C  1 242 ? -24.065 9.904   0.093   1.00 30.42 ? 259  ASN C CB  1 
ATOM   10823 C  CG  . ASN C  1 242 ? -23.528 10.098  -1.306  1.00 33.23 ? 259  ASN C CG  1 
ATOM   10824 O  OD1 . ASN C  1 242 ? -22.361 9.793   -1.584  1.00 37.40 ? 259  ASN C OD1 1 
ATOM   10825 N  ND2 . ASN C  1 242 ? -24.360 10.614  -2.198  1.00 34.10 ? 259  ASN C ND2 1 
ATOM   10826 N  N   . HIS C  1 243 ? -24.313 9.172   3.109   1.00 25.40 ? 260  HIS C N   1 
ATOM   10827 C  CA  . HIS C  1 243 ? -24.776 9.490   4.450   1.00 26.77 ? 260  HIS C CA  1 
ATOM   10828 C  C   . HIS C  1 243 ? -23.600 9.497   5.426   1.00 24.89 ? 260  HIS C C   1 
ATOM   10829 O  O   . HIS C  1 243 ? -23.432 10.441  6.193   1.00 24.37 ? 260  HIS C O   1 
ATOM   10830 C  CB  . HIS C  1 243 ? -25.853 8.505   4.918   1.00 29.24 ? 260  HIS C CB  1 
ATOM   10831 C  CG  . HIS C  1 243 ? -26.320 8.769   6.318   1.00 32.15 ? 260  HIS C CG  1 
ATOM   10832 N  ND1 . HIS C  1 243 ? -26.709 10.024  6.738   1.00 31.76 ? 260  HIS C ND1 1 
ATOM   10833 C  CD2 . HIS C  1 243 ? -26.465 7.959   7.381   1.00 33.47 ? 260  HIS C CD2 1 
ATOM   10834 C  CE1 . HIS C  1 243 ? -27.072 9.965   8.012   1.00 32.89 ? 260  HIS C CE1 1 
ATOM   10835 N  NE2 . HIS C  1 243 ? -26.932 8.721   8.425   1.00 33.86 ? 260  HIS C NE2 1 
ATOM   10836 N  N   . ASN C  1 244 ? -22.787 8.436   5.390   1.00 23.44 ? 261  ASN C N   1 
ATOM   10837 C  CA  . ASN C  1 244 ? -21.649 8.310   6.285   1.00 23.27 ? 261  ASN C CA  1 
ATOM   10838 C  C   . ASN C  1 244 ? -20.631 9.424   6.018   1.00 22.42 ? 261  ASN C C   1 
ATOM   10839 O  O   . ASN C  1 244 ? -20.110 10.016  6.961   1.00 21.88 ? 261  ASN C O   1 
ATOM   10840 C  CB  . ASN C  1 244 ? -21.043 6.912   6.206   1.00 23.34 ? 261  ASN C CB  1 
ATOM   10841 C  CG  . ASN C  1 244 ? -21.924 5.867   6.853   1.00 24.37 ? 261  ASN C CG  1 
ATOM   10842 O  OD1 . ASN C  1 244 ? -22.742 6.182   7.723   1.00 25.00 ? 261  ASN C OD1 1 
ATOM   10843 N  ND2 . ASN C  1 244 ? -21.760 4.613   6.468   1.00 25.23 ? 261  ASN C ND2 1 
ATOM   10844 N  N   . ALA C  1 245 ? -20.370 9.728   4.741   1.00 22.08 ? 262  ALA C N   1 
ATOM   10845 C  CA  . ALA C  1 245 ? -19.366 10.728  4.389   1.00 22.50 ? 262  ALA C CA  1 
ATOM   10846 C  C   . ALA C  1 245 ? -19.696 12.076  5.030   1.00 22.40 ? 262  ALA C C   1 
ATOM   10847 O  O   . ALA C  1 245 ? -18.851 12.668  5.702   1.00 20.69 ? 262  ALA C O   1 
ATOM   10848 C  CB  . ALA C  1 245 ? -19.234 10.842  2.885   1.00 21.98 ? 262  ALA C CB  1 
ATOM   10849 N  N   . PHE C  1 246 ? -20.941 12.535  4.845   1.00 23.55 ? 263  PHE C N   1 
ATOM   10850 C  CA  . PHE C  1 246 ? -21.371 13.829  5.357   1.00 24.40 ? 263  PHE C CA  1 
ATOM   10851 C  C   . PHE C  1 246 ? -21.407 13.835  6.887   1.00 22.98 ? 263  PHE C C   1 
ATOM   10852 O  O   . PHE C  1 246 ? -20.934 14.783  7.509   1.00 21.18 ? 263  PHE C O   1 
ATOM   10853 C  CB  . PHE C  1 246 ? -22.734 14.231  4.782   1.00 26.96 ? 263  PHE C CB  1 
ATOM   10854 C  CG  . PHE C  1 246 ? -22.669 14.919  3.425   1.00 30.37 ? 263  PHE C CG  1 
ATOM   10855 C  CD1 . PHE C  1 246 ? -22.363 16.276  3.329   1.00 32.31 ? 263  PHE C CD1 1 
ATOM   10856 C  CD2 . PHE C  1 246 ? -22.933 14.218  2.249   1.00 32.36 ? 263  PHE C CD2 1 
ATOM   10857 C  CE1 . PHE C  1 246 ? -22.300 16.904  2.090   1.00 32.36 ? 263  PHE C CE1 1 
ATOM   10858 C  CE2 . PHE C  1 246 ? -22.881 14.855  1.015   1.00 32.42 ? 263  PHE C CE2 1 
ATOM   10859 C  CZ  . PHE C  1 246 ? -22.561 16.195  0.938   1.00 32.10 ? 263  PHE C CZ  1 
ATOM   10860 N  N   . ARG C  1 247 ? -21.973 12.794  7.504   1.00 22.37 ? 264  ARG C N   1 
ATOM   10861 C  CA  . ARG C  1 247 ? -22.179 12.826  8.944   1.00 23.51 ? 264  ARG C CA  1 
ATOM   10862 C  C   . ARG C  1 247 ? -20.848 12.708  9.686   1.00 22.06 ? 264  ARG C C   1 
ATOM   10863 O  O   . ARG C  1 247 ? -20.687 13.319  10.734  1.00 21.68 ? 264  ARG C O   1 
ATOM   10864 C  CB  . ARG C  1 247 ? -23.198 11.793  9.432   1.00 24.44 ? 264  ARG C CB  1 
ATOM   10865 C  CG  . ARG C  1 247 ? -22.701 10.361  9.506   1.00 26.13 ? 264  ARG C CG  1 
ATOM   10866 C  CD  . ARG C  1 247 ? -23.882 9.411   9.664   1.00 27.70 ? 264  ARG C CD  1 
ATOM   10867 N  NE  . ARG C  1 247 ? -23.417 8.022   9.678   1.00 28.60 ? 264  ARG C NE  1 
ATOM   10868 C  CZ  . ARG C  1 247 ? -23.254 7.285   10.759  1.00 30.01 ? 264  ARG C CZ  1 
ATOM   10869 N  NH1 . ARG C  1 247 ? -23.385 7.824   11.955  1.00 32.01 ? 264  ARG C NH1 1 
ATOM   10870 N  NH2 . ARG C  1 247 ? -22.945 6.006   10.639  1.00 32.02 ? 264  ARG C NH2 1 
ATOM   10871 N  N   . PHE C  1 248 ? -19.895 11.937  9.144   1.00 22.00 ? 265  PHE C N   1 
ATOM   10872 C  CA  . PHE C  1 248 ? -18.589 11.802  9.775   1.00 21.63 ? 265  PHE C CA  1 
ATOM   10873 C  C   . PHE C  1 248 ? -17.796 13.099  9.629   1.00 20.94 ? 265  PHE C C   1 
ATOM   10874 O  O   . PHE C  1 248 ? -17.097 13.493  10.556  1.00 21.22 ? 265  PHE C O   1 
ATOM   10875 C  CB  . PHE C  1 248 ? -17.819 10.589  9.238   1.00 21.23 ? 265  PHE C CB  1 
ATOM   10876 C  CG  . PHE C  1 248 ? -18.332 9.243   9.730   1.00 21.18 ? 265  PHE C CG  1 
ATOM   10877 C  CD1 . PHE C  1 248 ? -18.870 9.096   11.006  1.00 22.57 ? 265  PHE C CD1 1 
ATOM   10878 C  CD2 . PHE C  1 248 ? -18.276 8.120   8.911   1.00 21.38 ? 265  PHE C CD2 1 
ATOM   10879 C  CE1 . PHE C  1 248 ? -19.335 7.863   11.444  1.00 22.82 ? 265  PHE C CE1 1 
ATOM   10880 C  CE2 . PHE C  1 248 ? -18.741 6.891   9.352   1.00 21.54 ? 265  PHE C CE2 1 
ATOM   10881 C  CZ  . PHE C  1 248 ? -19.269 6.764   10.614  1.00 22.42 ? 265  PHE C CZ  1 
ATOM   10882 N  N   . LEU C  1 249 ? -17.920 13.777  8.485   1.00 22.10 ? 266  LEU C N   1 
ATOM   10883 C  CA  . LEU C  1 249 ? -17.297 15.082  8.325   1.00 22.85 ? 266  LEU C CA  1 
ATOM   10884 C  C   . LEU C  1 249 ? -17.835 16.033  9.395   1.00 23.76 ? 266  LEU C C   1 
ATOM   10885 O  O   . LEU C  1 249 ? -17.064 16.716  10.062  1.00 22.39 ? 266  LEU C O   1 
ATOM   10886 C  CB  . LEU C  1 249 ? -17.512 15.629  6.915   1.00 23.30 ? 266  LEU C CB  1 
ATOM   10887 C  CG  . LEU C  1 249 ? -16.925 17.017  6.631   1.00 23.28 ? 266  LEU C CG  1 
ATOM   10888 C  CD1 . LEU C  1 249 ? -15.414 17.043  6.828   1.00 23.19 ? 266  LEU C CD1 1 
ATOM   10889 C  CD2 . LEU C  1 249 ? -17.288 17.475  5.234   1.00 23.48 ? 266  LEU C CD2 1 
ATOM   10890 N  N   . ARG C  1 250 ? -19.162 16.054  9.582   1.00 25.19 ? 267  ARG C N   1 
ATOM   10891 C  CA  . ARG C  1 250 ? -19.777 16.926  10.574  1.00 26.99 ? 267  ARG C CA  1 
ATOM   10892 C  C   . ARG C  1 250 ? -19.374 16.504  11.987  1.00 24.67 ? 267  ARG C C   1 
ATOM   10893 O  O   . ARG C  1 250 ? -19.144 17.355  12.838  1.00 23.49 ? 267  ARG C O   1 
ATOM   10894 C  CB  . ARG C  1 250 ? -21.303 16.956  10.414  1.00 29.63 ? 267  ARG C CB  1 
ATOM   10895 C  CG  . ARG C  1 250 ? -22.046 17.626  11.561  1.00 34.91 ? 267  ARG C CG  1 
ATOM   10896 C  CD  . ARG C  1 250 ? -23.524 17.835  11.242  1.00 39.60 ? 267  ARG C CD  1 
ATOM   10897 N  NE  . ARG C  1 250 ? -23.735 18.946  10.307  1.00 44.29 ? 267  ARG C NE  1 
ATOM   10898 C  CZ  . ARG C  1 250 ? -24.902 19.293  9.770   1.00 47.96 ? 267  ARG C CZ  1 
ATOM   10899 N  NH1 . ARG C  1 250 ? -25.984 18.558  9.976   1.00 48.93 ? 267  ARG C NH1 1 
ATOM   10900 N  NH2 . ARG C  1 250 ? -24.973 20.369  9.006   1.00 49.56 ? 267  ARG C NH2 1 
ATOM   10901 N  N   . LYS C  1 251 ? -19.286 15.193  12.236  1.00 24.19 ? 268  LYS C N   1 
ATOM   10902 C  CA  . LYS C  1 251 ? -19.024 14.687  13.578  1.00 25.33 ? 268  LYS C CA  1 
ATOM   10903 C  C   . LYS C  1 251 ? -17.595 14.998  14.033  1.00 25.76 ? 268  LYS C C   1 
ATOM   10904 O  O   . LYS C  1 251 ? -17.371 15.205  15.226  1.00 26.02 ? 268  LYS C O   1 
ATOM   10905 C  CB  . LYS C  1 251 ? -19.293 13.179  13.635  1.00 25.63 ? 268  LYS C CB  1 
ATOM   10906 C  CG  . LYS C  1 251 ? -19.148 12.509  14.994  1.00 26.85 ? 268  LYS C CG  1 
ATOM   10907 C  CD  . LYS C  1 251 ? -19.523 11.032  14.965  1.00 27.67 ? 268  LYS C CD  1 
ATOM   10908 C  CE  . LYS C  1 251 ? -19.480 10.409  16.318  1.00 29.16 ? 268  LYS C CE  1 
ATOM   10909 N  NZ  . LYS C  1 251 ? -19.990 9.037   16.281  1.00 30.01 ? 268  LYS C NZ  1 
ATOM   10910 N  N   . TYR C  1 252 ? -16.631 15.036  13.101  1.00 24.25 ? 269  TYR C N   1 
ATOM   10911 C  CA  . TYR C  1 252 ? -15.223 14.982  13.476  1.00 24.01 ? 269  TYR C CA  1 
ATOM   10912 C  C   . TYR C  1 252 ? -14.459 16.265  13.146  1.00 24.91 ? 269  TYR C C   1 
ATOM   10913 O  O   . TYR C  1 252 ? -13.360 16.453  13.664  1.00 25.51 ? 269  TYR C O   1 
ATOM   10914 C  CB  . TYR C  1 252 ? -14.536 13.797  12.789  1.00 24.07 ? 269  TYR C CB  1 
ATOM   10915 C  CG  . TYR C  1 252 ? -14.982 12.425  13.272  1.00 23.63 ? 269  TYR C CG  1 
ATOM   10916 C  CD1 . TYR C  1 252 ? -15.078 12.134  14.626  1.00 23.97 ? 269  TYR C CD1 1 
ATOM   10917 C  CD2 . TYR C  1 252 ? -15.336 11.429  12.366  1.00 24.02 ? 269  TYR C CD2 1 
ATOM   10918 C  CE1 . TYR C  1 252 ? -15.500 10.890  15.068  1.00 24.96 ? 269  TYR C CE1 1 
ATOM   10919 C  CE2 . TYR C  1 252 ? -15.746 10.178  12.795  1.00 24.20 ? 269  TYR C CE2 1 
ATOM   10920 C  CZ  . TYR C  1 252 ? -15.831 9.910   14.149  1.00 25.22 ? 269  TYR C CZ  1 
ATOM   10921 O  OH  . TYR C  1 252 ? -16.244 8.683   14.576  1.00 27.68 ? 269  TYR C OH  1 
ATOM   10922 N  N   . ARG C  1 253 ? -15.006 17.146  12.301  1.00 26.15 ? 270  ARG C N   1 
ATOM   10923 C  CA  . ARG C  1 253 ? -14.192 18.196  11.702  1.00 26.89 ? 270  ARG C CA  1 
ATOM   10924 C  C   . ARG C  1 253 ? -13.678 19.195  12.740  1.00 27.71 ? 270  ARG C C   1 
ATOM   10925 O  O   . ARG C  1 253 ? -12.623 19.787  12.524  1.00 26.36 ? 270  ARG C O   1 
ATOM   10926 C  CB  . ARG C  1 253 ? -14.888 18.951  10.567  1.00 27.78 ? 270  ARG C CB  1 
ATOM   10927 C  CG  . ARG C  1 253 ? -16.180 19.670  10.924  1.00 28.63 ? 270  ARG C CG  1 
ATOM   10928 C  CD  . ARG C  1 253 ? -16.817 20.239  9.669   1.00 30.13 ? 270  ARG C CD  1 
ATOM   10929 N  NE  . ARG C  1 253 ? -15.880 21.117  8.959   1.00 30.80 ? 270  ARG C NE  1 
ATOM   10930 C  CZ  . ARG C  1 253 ? -16.003 21.522  7.702   1.00 31.58 ? 270  ARG C CZ  1 
ATOM   10931 N  NH1 . ARG C  1 253 ? -17.099 21.245  7.016   1.00 32.53 ? 270  ARG C NH1 1 
ATOM   10932 N  NH2 . ARG C  1 253 ? -15.022 22.209  7.139   1.00 31.48 ? 270  ARG C NH2 1 
ATOM   10933 N  N   . GLU C  1 254 ? -14.408 19.383  13.851  1.00 28.34 ? 271  GLU C N   1 
ATOM   10934 C  CA  . GLU C  1 254 ? -13.988 20.308  14.896  1.00 30.74 ? 271  GLU C CA  1 
ATOM   10935 C  C   . GLU C  1 254 ? -13.326 19.570  16.059  1.00 29.36 ? 271  GLU C C   1 
ATOM   10936 O  O   . GLU C  1 254 ? -12.877 20.205  17.011  1.00 28.58 ? 271  GLU C O   1 
ATOM   10937 C  CB  . GLU C  1 254 ? -15.169 21.164  15.356  1.00 34.28 ? 271  GLU C CB  1 
ATOM   10938 C  CG  . GLU C  1 254 ? -15.519 22.261  14.356  1.00 38.16 ? 271  GLU C CG  1 
ATOM   10939 C  CD  . GLU C  1 254 ? -16.810 23.014  14.630  1.00 44.63 ? 271  GLU C CD  1 
ATOM   10940 O  OE1 . GLU C  1 254 ? -16.967 24.095  14.021  1.00 48.74 ? 271  GLU C OE1 1 
ATOM   10941 O  OE2 . GLU C  1 254 ? -17.662 22.532  15.415  1.00 46.93 ? 271  GLU C OE2 1 
ATOM   10942 N  N   . LYS C  1 255 ? -13.243 18.237  15.972  1.00 29.18 ? 272  LYS C N   1 
ATOM   10943 C  CA  . LYS C  1 255 ? -12.621 17.426  17.008  1.00 30.10 ? 272  LYS C CA  1 
ATOM   10944 C  C   . LYS C  1 255 ? -11.270 16.879  16.541  1.00 27.22 ? 272  LYS C C   1 
ATOM   10945 O  O   . LYS C  1 255 ? -10.367 16.693  17.358  1.00 25.90 ? 272  LYS C O   1 
ATOM   10946 C  CB  . LYS C  1 255 ? -13.583 16.300  17.405  1.00 34.05 ? 272  LYS C CB  1 
ATOM   10947 C  CG  . LYS C  1 255 ? -13.146 15.500  18.620  1.00 39.12 ? 272  LYS C CG  1 
ATOM   10948 C  CD  . LYS C  1 255 ? -14.156 14.468  19.110  1.00 43.31 ? 272  LYS C CD  1 
ATOM   10949 C  CE  . LYS C  1 255 ? -13.619 13.700  20.278  1.00 46.52 ? 272  LYS C CE  1 
ATOM   10950 N  NZ  . LYS C  1 255 ? -14.522 12.620  20.682  1.00 48.82 ? 272  LYS C NZ  1 
ATOM   10951 N  N   . TYR C  1 256 ? -11.144 16.598  15.236  1.00 25.02 ? 273  TYR C N   1 
ATOM   10952 C  CA  . TYR C  1 256 ? -9.927  16.043  14.665  1.00 24.05 ? 273  TYR C CA  1 
ATOM   10953 C  C   . TYR C  1 256 ? -9.506  16.864  13.449  1.00 22.34 ? 273  TYR C C   1 
ATOM   10954 O  O   . TYR C  1 256 ? -10.227 17.766  13.024  1.00 21.23 ? 273  TYR C O   1 
ATOM   10955 C  CB  . TYR C  1 256 ? -10.182 14.579  14.292  1.00 23.81 ? 273  TYR C CB  1 
ATOM   10956 C  CG  . TYR C  1 256 ? -10.468 13.674  15.479  1.00 24.80 ? 273  TYR C CG  1 
ATOM   10957 C  CD1 . TYR C  1 256 ? -9.459  13.330  16.371  1.00 25.73 ? 273  TYR C CD1 1 
ATOM   10958 C  CD2 . TYR C  1 256 ? -11.737 13.155  15.707  1.00 24.77 ? 273  TYR C CD2 1 
ATOM   10959 C  CE1 . TYR C  1 256 ? -9.706  12.506  17.456  1.00 26.98 ? 273  TYR C CE1 1 
ATOM   10960 C  CE2 . TYR C  1 256 ? -11.997 12.328  16.787  1.00 24.77 ? 273  TYR C CE2 1 
ATOM   10961 C  CZ  . TYR C  1 256 ? -10.977 11.997  17.661  1.00 25.88 ? 273  TYR C CZ  1 
ATOM   10962 O  OH  . TYR C  1 256 ? -11.212 11.193  18.734  1.00 24.97 ? 273  TYR C OH  1 
ATOM   10963 N  N   . CYS C  1 257 ? -8.330  16.534  12.896  1.00 21.16 ? 274  CYS C N   1 
ATOM   10964 C  CA  . CYS C  1 257 ? -7.842  17.156  11.674  1.00 21.27 ? 274  CYS C CA  1 
ATOM   10965 C  C   . CYS C  1 257 ? -8.260  16.296  10.484  1.00 22.04 ? 274  CYS C C   1 
ATOM   10966 O  O   . CYS C  1 257 ? -7.562  15.346  10.116  1.00 21.59 ? 274  CYS C O   1 
ATOM   10967 C  CB  . CYS C  1 257 ? -6.327  17.331  11.701  1.00 21.35 ? 274  CYS C CB  1 
ATOM   10968 S  SG  . CYS C  1 257 ? -5.684  18.228  10.263  1.00 22.64 ? 274  CYS C SG  1 
ATOM   10969 N  N   . THR C  1 258 ? -9.408  16.629  9.887   1.00 20.71 ? 275  THR C N   1 
ATOM   10970 C  CA  . THR C  1 258 ? -10.034 15.719  8.947   1.00 20.61 ? 275  THR C CA  1 
ATOM   10971 C  C   . THR C  1 258 ? -10.737 16.499  7.842   1.00 21.28 ? 275  THR C C   1 
ATOM   10972 O  O   . THR C  1 258 ? -11.224 17.614  8.049   1.00 21.34 ? 275  THR C O   1 
ATOM   10973 C  CB  . THR C  1 258 ? -10.983 14.797  9.718   1.00 20.85 ? 275  THR C CB  1 
ATOM   10974 O  OG1 . THR C  1 258 ? -11.422 13.849  8.752   1.00 21.88 ? 275  THR C OG1 1 
ATOM   10975 C  CG2 . THR C  1 258 ? -12.172 15.519  10.325  1.00 21.51 ? 275  THR C CG2 1 
ATOM   10976 N  N   . PHE C  1 259 ? -10.764 15.887  6.657   1.00 21.73 ? 276  PHE C N   1 
ATOM   10977 C  CA  . PHE C  1 259 ? -11.566 16.367  5.548   1.00 21.70 ? 276  PHE C CA  1 
ATOM   10978 C  C   . PHE C  1 259 ? -11.995 15.154  4.738   1.00 21.08 ? 276  PHE C C   1 
ATOM   10979 O  O   . PHE C  1 259 ? -11.494 14.050  4.940   1.00 20.54 ? 276  PHE C O   1 
ATOM   10980 C  CB  . PHE C  1 259 ? -10.847 17.409  4.681   1.00 22.02 ? 276  PHE C CB  1 
ATOM   10981 C  CG  . PHE C  1 259 ? -9.763  16.933  3.721   1.00 23.02 ? 276  PHE C CG  1 
ATOM   10982 C  CD1 . PHE C  1 259 ? -8.468  16.694  4.168   1.00 24.29 ? 276  PHE C CD1 1 
ATOM   10983 C  CD2 . PHE C  1 259 ? -10.020 16.806  2.358   1.00 23.75 ? 276  PHE C CD2 1 
ATOM   10984 C  CE1 . PHE C  1 259 ? -7.474  16.290  3.286   1.00 24.81 ? 276  PHE C CE1 1 
ATOM   10985 C  CE2 . PHE C  1 259 ? -9.022  16.409  1.476   1.00 24.04 ? 276  PHE C CE2 1 
ATOM   10986 C  CZ  . PHE C  1 259 ? -7.752  16.152  1.941   1.00 24.18 ? 276  PHE C CZ  1 
ATOM   10987 N  N   . ASN C  1 260 ? -12.940 15.393  3.834   1.00 20.28 ? 277  ASN C N   1 
ATOM   10988 C  CA  . ASN C  1 260 ? -13.422 14.381  2.915   1.00 21.01 ? 277  ASN C CA  1 
ATOM   10989 C  C   . ASN C  1 260 ? -13.227 14.924  1.505   1.00 21.52 ? 277  ASN C C   1 
ATOM   10990 O  O   . ASN C  1 260 ? -13.826 15.934  1.143   1.00 20.93 ? 277  ASN C O   1 
ATOM   10991 C  CB  . ASN C  1 260 ? -14.872 14.027  3.223   1.00 21.17 ? 277  ASN C CB  1 
ATOM   10992 C  CG  . ASN C  1 260 ? -15.394 12.933  2.326   1.00 21.75 ? 277  ASN C CG  1 
ATOM   10993 O  OD1 . ASN C  1 260 ? -15.407 13.090  1.098   1.00 23.01 ? 277  ASN C OD1 1 
ATOM   10994 N  ND2 . ASN C  1 260 ? -15.830 11.829  2.916   1.00 22.56 ? 277  ASN C ND2 1 
ATOM   10995 N  N   . ASP C  1 261 ? -12.368 14.261  0.724   1.00 22.36 ? 278  ASP C N   1 
ATOM   10996 C  CA  . ASP C  1 261 ? -11.991 14.764  -0.587  1.00 23.76 ? 278  ASP C CA  1 
ATOM   10997 C  C   . ASP C  1 261 ? -13.154 14.678  -1.575  1.00 22.99 ? 278  ASP C C   1 
ATOM   10998 O  O   . ASP C  1 261 ? -13.261 15.508  -2.473  1.00 22.10 ? 278  ASP C O   1 
ATOM   10999 C  CB  . ASP C  1 261 ? -10.798 14.028  -1.170  1.00 24.83 ? 278  ASP C CB  1 
ATOM   11000 C  CG  . ASP C  1 261 ? -10.282 14.661  -2.450  1.00 26.81 ? 278  ASP C CG  1 
ATOM   11001 O  OD1 . ASP C  1 261 ? -9.912  15.850  -2.387  1.00 28.01 ? 278  ASP C OD1 1 
ATOM   11002 O  OD2 . ASP C  1 261 ? -10.308 13.980  -3.500  1.00 28.32 ? 278  ASP C OD2 1 
ATOM   11003 N  N   . ASP C  1 262 ? -14.010 13.663  -1.417  1.00 23.44 ? 279  ASP C N   1 
ATOM   11004 C  CA  . ASP C  1 262 ? -15.145 13.478  -2.307  1.00 24.32 ? 279  ASP C CA  1 
ATOM   11005 C  C   . ASP C  1 262 ? -16.087 14.677  -2.224  1.00 23.82 ? 279  ASP C C   1 
ATOM   11006 O  O   . ASP C  1 262 ? -16.667 15.069  -3.233  1.00 24.16 ? 279  ASP C O   1 
ATOM   11007 C  CB  . ASP C  1 262 ? -15.854 12.157  -2.054  1.00 25.04 ? 279  ASP C CB  1 
ATOM   11008 C  CG  . ASP C  1 262 ? -14.956 10.941  -2.225  1.00 26.99 ? 279  ASP C CG  1 
ATOM   11009 O  OD1 . ASP C  1 262 ? -14.355 10.812  -3.317  1.00 30.79 ? 279  ASP C OD1 1 
ATOM   11010 O  OD2 . ASP C  1 262 ? -14.841 10.158  -1.262  1.00 26.83 ? 279  ASP C OD2 1 
ATOM   11011 N  N   . ILE C  1 263 ? -16.230 15.246  -1.023  1.00 23.55 ? 280  ILE C N   1 
ATOM   11012 C  CA  . ILE C  1 263 ? -17.102 16.389  -0.803  1.00 23.08 ? 280  ILE C CA  1 
ATOM   11013 C  C   . ILE C  1 263 ? -16.323 17.685  -1.033  1.00 23.03 ? 280  ILE C C   1 
ATOM   11014 O  O   . ILE C  1 263 ? -16.702 18.494  -1.880  1.00 22.92 ? 280  ILE C O   1 
ATOM   11015 C  CB  . ILE C  1 263 ? -17.717 16.335  0.607   1.00 22.40 ? 280  ILE C CB  1 
ATOM   11016 C  CG1 . ILE C  1 263 ? -18.525 15.050  0.805   1.00 22.81 ? 280  ILE C CG1 1 
ATOM   11017 C  CG2 . ILE C  1 263 ? -18.549 17.586  0.896   1.00 22.32 ? 280  ILE C CG2 1 
ATOM   11018 C  CD1 . ILE C  1 263 ? -18.952 14.788  2.235   1.00 22.98 ? 280  ILE C CD1 1 
ATOM   11019 N  N   . GLN C  1 264 ? -15.247 17.885  -0.258  1.00 21.34 ? 281  GLN C N   1 
ATOM   11020 C  CA  . GLN C  1 264 ? -14.614 19.192  -0.147  1.00 21.29 ? 281  GLN C CA  1 
ATOM   11021 C  C   . GLN C  1 264 ? -13.624 19.455  -1.280  1.00 21.59 ? 281  GLN C C   1 
ATOM   11022 O  O   . GLN C  1 264 ? -13.537 20.583  -1.771  1.00 20.07 ? 281  GLN C O   1 
ATOM   11023 C  CB  . GLN C  1 264 ? -13.954 19.336  1.224   1.00 21.61 ? 281  GLN C CB  1 
ATOM   11024 C  CG  . GLN C  1 264 ? -14.965 19.415  2.360   1.00 22.07 ? 281  GLN C CG  1 
ATOM   11025 C  CD  . GLN C  1 264 ? -14.354 19.166  3.720   1.00 21.86 ? 281  GLN C CD  1 
ATOM   11026 O  OE1 . GLN C  1 264 ? -13.819 18.084  3.997   1.00 20.62 ? 281  GLN C OE1 1 
ATOM   11027 N  NE2 . GLN C  1 264 ? -14.423 20.177  4.575   1.00 20.57 ? 281  GLN C NE2 1 
ATOM   11028 N  N   . GLY C  1 265 ? -12.862 18.430  -1.672  1.00 21.45 ? 282  GLY C N   1 
ATOM   11029 C  CA  . GLY C  1 265 ? -11.943 18.558  -2.793  1.00 22.23 ? 282  GLY C CA  1 
ATOM   11030 C  C   . GLY C  1 265 ? -12.688 18.787  -4.109  1.00 22.84 ? 282  GLY C C   1 
ATOM   11031 O  O   . GLY C  1 265 ? -12.277 19.621  -4.913  1.00 22.77 ? 282  GLY C O   1 
ATOM   11032 N  N   . THR C  1 266 ? -13.775 18.028  -4.302  1.00 22.63 ? 283  THR C N   1 
ATOM   11033 C  CA  . THR C  1 266 ? -14.680 18.180  -5.434  1.00 23.16 ? 283  THR C CA  1 
ATOM   11034 C  C   . THR C  1 266 ? -15.168 19.624  -5.524  1.00 23.13 ? 283  THR C C   1 
ATOM   11035 O  O   . THR C  1 266 ? -15.092 20.238  -6.585  1.00 23.78 ? 283  THR C O   1 
ATOM   11036 C  CB  . THR C  1 266 ? -15.859 17.216  -5.281  1.00 23.34 ? 283  THR C CB  1 
ATOM   11037 O  OG1 . THR C  1 266 ? -15.331 15.892  -5.352  1.00 23.53 ? 283  THR C OG1 1 
ATOM   11038 C  CG2 . THR C  1 266 ? -16.909 17.401  -6.362  1.00 23.65 ? 283  THR C CG2 1 
ATOM   11039 N  N   . ALA C  1 267 ? -15.682 20.146  -4.404  1.00 23.10 ? 284  ALA C N   1 
ATOM   11040 C  CA  . ALA C  1 267 ? -16.213 21.500  -4.348  1.00 23.10 ? 284  ALA C CA  1 
ATOM   11041 C  C   . ALA C  1 267 ? -15.168 22.516  -4.806  1.00 22.88 ? 284  ALA C C   1 
ATOM   11042 O  O   . ALA C  1 267 ? -15.498 23.426  -5.562  1.00 22.75 ? 284  ALA C O   1 
ATOM   11043 C  CB  . ALA C  1 267 ? -16.703 21.812  -2.951  1.00 22.83 ? 284  ALA C CB  1 
ATOM   11044 N  N   . ALA C  1 268 ? -13.915 22.353  -4.352  1.00 23.36 ? 285  ALA C N   1 
ATOM   11045 C  CA  . ALA C  1 268 ? -12.867 23.332  -4.610  1.00 22.84 ? 285  ALA C CA  1 
ATOM   11046 C  C   . ALA C  1 268 ? -12.426 23.306  -6.076  1.00 22.70 ? 285  ALA C C   1 
ATOM   11047 O  O   . ALA C  1 268 ? -12.212 24.360  -6.668  1.00 22.02 ? 285  ALA C O   1 
ATOM   11048 C  CB  . ALA C  1 268 ? -11.693 23.104  -3.683  1.00 22.81 ? 285  ALA C CB  1 
ATOM   11049 N  N   . VAL C  1 269 ? -12.275 22.112  -6.661  1.00 22.87 ? 286  VAL C N   1 
ATOM   11050 C  CA  . VAL C  1 269 ? -11.797 22.017  -8.033  1.00 23.39 ? 286  VAL C CA  1 
ATOM   11051 C  C   . VAL C  1 269 ? -12.874 22.552  -8.983  1.00 22.99 ? 286  VAL C C   1 
ATOM   11052 O  O   . VAL C  1 269 ? -12.554 23.226  -9.958  1.00 22.02 ? 286  VAL C O   1 
ATOM   11053 C  CB  . VAL C  1 269 ? -11.320 20.606  -8.430  1.00 25.06 ? 286  VAL C CB  1 
ATOM   11054 C  CG1 . VAL C  1 269 ? -12.449 19.584  -8.468  1.00 25.63 ? 286  VAL C CG1 1 
ATOM   11055 C  CG2 . VAL C  1 269 ? -10.579 20.625  -9.765  1.00 26.76 ? 286  VAL C CG2 1 
ATOM   11056 N  N   . ALA C  1 270 ? -14.146 22.272  -8.679  1.00 22.73 ? 287  ALA C N   1 
ATOM   11057 C  CA  . ALA C  1 270 ? -15.265 22.785  -9.454  1.00 23.83 ? 287  ALA C CA  1 
ATOM   11058 C  C   . ALA C  1 270 ? -15.307 24.311  -9.387  1.00 24.24 ? 287  ALA C C   1 
ATOM   11059 O  O   . ALA C  1 270 ? -15.387 24.979  -10.419 1.00 25.03 ? 287  ALA C O   1 
ATOM   11060 C  CB  . ALA C  1 270 ? -16.560 22.178  -8.954  1.00 23.80 ? 287  ALA C CB  1 
ATOM   11061 N  N   . LEU C  1 271 ? -15.255 24.853  -8.163  1.00 22.98 ? 288  LEU C N   1 
ATOM   11062 C  CA  . LEU C  1 271 ? -15.257 26.293  -7.954  1.00 22.54 ? 288  LEU C CA  1 
ATOM   11063 C  C   . LEU C  1 271 ? -14.120 26.940  -8.745  1.00 22.60 ? 288  LEU C C   1 
ATOM   11064 O  O   . LEU C  1 271 ? -14.336 27.942  -9.425  1.00 22.75 ? 288  LEU C O   1 
ATOM   11065 C  CB  . LEU C  1 271 ? -15.170 26.636  -6.466  1.00 22.67 ? 288  LEU C CB  1 
ATOM   11066 C  CG  . LEU C  1 271 ? -15.141 28.129  -6.120  1.00 23.31 ? 288  LEU C CG  1 
ATOM   11067 C  CD1 . LEU C  1 271 ? -16.377 28.864  -6.647  1.00 23.15 ? 288  LEU C CD1 1 
ATOM   11068 C  CD2 . LEU C  1 271 ? -15.006 28.326  -4.623  1.00 23.62 ? 288  LEU C CD2 1 
ATOM   11069 N  N   . ALA C  1 272 ? -12.910 26.368  -8.658  1.00 21.54 ? 289  ALA C N   1 
ATOM   11070 C  CA  . ALA C  1 272 ? -11.753 26.926  -9.341  1.00 21.98 ? 289  ALA C CA  1 
ATOM   11071 C  C   . ALA C  1 272 ? -12.031 27.112  -10.835 1.00 22.15 ? 289  ALA C C   1 
ATOM   11072 O  O   . ALA C  1 272 ? -11.666 28.137  -11.407 1.00 23.64 ? 289  ALA C O   1 
ATOM   11073 C  CB  . ALA C  1 272 ? -10.532 26.057  -9.114  1.00 22.31 ? 289  ALA C CB  1 
ATOM   11074 N  N   . GLY C  1 273 ? -12.663 26.116  -11.465 1.00 22.88 ? 290  GLY C N   1 
ATOM   11075 C  CA  . GLY C  1 273 ? -13.050 26.199  -12.864 1.00 22.81 ? 290  GLY C CA  1 
ATOM   11076 C  C   . GLY C  1 273 ? -14.024 27.349  -13.129 1.00 23.32 ? 290  GLY C C   1 
ATOM   11077 O  O   . GLY C  1 273 ? -13.906 28.044  -14.135 1.00 23.97 ? 290  GLY C O   1 
ATOM   11078 N  N   . LEU C  1 274 ? -14.992 27.529  -12.227 1.00 23.50 ? 291  LEU C N   1 
ATOM   11079 C  CA  . LEU C  1 274 ? -15.976 28.592  -12.343 1.00 24.13 ? 291  LEU C CA  1 
ATOM   11080 C  C   . LEU C  1 274 ? -15.317 29.962  -12.179 1.00 25.45 ? 291  LEU C C   1 
ATOM   11081 O  O   . LEU C  1 274 ? -15.717 30.917  -12.841 1.00 25.66 ? 291  LEU C O   1 
ATOM   11082 C  CB  . LEU C  1 274 ? -17.078 28.374  -11.311 1.00 23.94 ? 291  LEU C CB  1 
ATOM   11083 C  CG  . LEU C  1 274 ? -17.910 27.100  -11.481 1.00 24.77 ? 291  LEU C CG  1 
ATOM   11084 C  CD1 . LEU C  1 274 ? -18.911 26.992  -10.350 1.00 25.43 ? 291  LEU C CD1 1 
ATOM   11085 C  CD2 . LEU C  1 274 ? -18.622 27.052  -12.828 1.00 25.48 ? 291  LEU C CD2 1 
ATOM   11086 N  N   . LEU C  1 275 ? -14.324 30.066  -11.283 1.00 25.40 ? 292  LEU C N   1 
ATOM   11087 C  CA  . LEU C  1 275 ? -13.606 31.315  -11.077 1.00 25.82 ? 292  LEU C CA  1 
ATOM   11088 C  C   . LEU C  1 275 ? -12.764 31.650  -12.309 1.00 27.17 ? 292  LEU C C   1 
ATOM   11089 O  O   . LEU C  1 275 ? -12.585 32.822  -12.646 1.00 27.52 ? 292  LEU C O   1 
ATOM   11090 C  CB  . LEU C  1 275 ? -12.743 31.242  -9.817  1.00 26.28 ? 292  LEU C CB  1 
ATOM   11091 C  CG  . LEU C  1 275 ? -13.493 31.181  -8.483  1.00 27.04 ? 292  LEU C CG  1 
ATOM   11092 C  CD1 . LEU C  1 275 ? -12.500 30.885  -7.372  1.00 27.43 ? 292  LEU C CD1 1 
ATOM   11093 C  CD2 . LEU C  1 275 ? -14.260 32.463  -8.176  1.00 27.74 ? 292  LEU C CD2 1 
ATOM   11094 N  N   . ALA C  1 276 ? -12.224 30.619  -12.965 1.00 26.99 ? 293  ALA C N   1 
ATOM   11095 C  CA  . ALA C  1 276 ? -11.495 30.807  -14.210 1.00 27.13 ? 293  ALA C CA  1 
ATOM   11096 C  C   . ALA C  1 276 ? -12.429 31.349  -15.293 1.00 28.29 ? 293  ALA C C   1 
ATOM   11097 O  O   . ALA C  1 276 ? -12.056 32.250  -16.042 1.00 28.47 ? 293  ALA C O   1 
ATOM   11098 C  CB  . ALA C  1 276 ? -10.846 29.512  -14.631 1.00 26.12 ? 293  ALA C CB  1 
ATOM   11099 N  N   . ALA C  1 277 ? -13.643 30.794  -15.364 1.00 28.81 ? 294  ALA C N   1 
ATOM   11100 C  CA  . ALA C  1 277 ? -14.637 31.219  -16.338 1.00 30.73 ? 294  ALA C CA  1 
ATOM   11101 C  C   . ALA C  1 277 ? -14.984 32.697  -16.159 1.00 32.49 ? 294  ALA C C   1 
ATOM   11102 O  O   . ALA C  1 277 ? -15.195 33.401  -17.149 1.00 31.79 ? 294  ALA C O   1 
ATOM   11103 C  CB  . ALA C  1 277 ? -15.873 30.349  -16.237 1.00 30.09 ? 294  ALA C CB  1 
ATOM   11104 N  N   A GLN C  1 278 ? -15.043 33.144  -14.896 0.50 33.02 ? 295  GLN C N   1 
ATOM   11105 N  N   B GLN C  1 278 ? -15.025 33.149  -14.898 0.50 32.79 ? 295  GLN C N   1 
ATOM   11106 C  CA  A GLN C  1 278 ? -15.370 34.520  -14.552 0.50 34.06 ? 295  GLN C CA  1 
ATOM   11107 C  CA  B GLN C  1 278 ? -15.376 34.518  -14.555 0.50 33.65 ? 295  GLN C CA  1 
ATOM   11108 C  C   A GLN C  1 278 ? -14.320 35.493  -15.087 0.50 34.31 ? 295  GLN C C   1 
ATOM   11109 C  C   B GLN C  1 278 ? -14.308 35.501  -15.042 0.50 34.04 ? 295  GLN C C   1 
ATOM   11110 O  O   A GLN C  1 278 ? -14.610 36.676  -15.252 0.50 33.68 ? 295  GLN C O   1 
ATOM   11111 O  O   B GLN C  1 278 ? -14.575 36.697  -15.132 0.50 33.21 ? 295  GLN C O   1 
ATOM   11112 C  CB  A GLN C  1 278 ? -15.468 34.716  -13.039 0.50 34.52 ? 295  GLN C CB  1 
ATOM   11113 C  CB  B GLN C  1 278 ? -15.579 34.640  -13.043 0.50 33.80 ? 295  GLN C CB  1 
ATOM   11114 C  CG  A GLN C  1 278 ? -16.796 34.284  -12.430 0.50 35.19 ? 295  GLN C CG  1 
ATOM   11115 C  CG  B GLN C  1 278 ? -15.843 36.064  -12.565 0.50 34.14 ? 295  GLN C CG  1 
ATOM   11116 C  CD  A GLN C  1 278 ? -16.872 34.570  -10.946 0.50 35.98 ? 295  GLN C CD  1 
ATOM   11117 C  CD  B GLN C  1 278 ? -17.192 36.597  -12.993 0.50 35.60 ? 295  GLN C CD  1 
ATOM   11118 O  OE1 A GLN C  1 278 ? -16.549 35.670  -10.489 0.50 38.21 ? 295  GLN C OE1 1 
ATOM   11119 O  OE1 B GLN C  1 278 ? -18.063 35.854  -13.458 0.50 38.30 ? 295  GLN C OE1 1 
ATOM   11120 N  NE2 A GLN C  1 278 ? -17.276 33.574  -10.173 0.50 35.90 ? 295  GLN C NE2 1 
ATOM   11121 N  NE2 B GLN C  1 278 ? -17.387 37.897  -12.832 0.50 35.79 ? 295  GLN C NE2 1 
ATOM   11122 N  N   . LYS C  1 279 ? -13.098 35.004  -15.335 1.00 34.95 ? 296  LYS C N   1 
ATOM   11123 C  CA  . LYS C  1 279 ? -12.053 35.823  -15.940 1.00 38.68 ? 296  LYS C CA  1 
ATOM   11124 C  C   . LYS C  1 279 ? -12.460 36.244  -17.357 1.00 40.75 ? 296  LYS C C   1 
ATOM   11125 O  O   . LYS C  1 279 ? -12.020 37.283  -17.843 1.00 41.90 ? 296  LYS C O   1 
ATOM   11126 C  CB  . LYS C  1 279 ? -10.688 35.122  -15.936 1.00 40.77 ? 296  LYS C CB  1 
ATOM   11127 C  CG  . LYS C  1 279 ? -10.106 34.859  -14.549 1.00 42.80 ? 296  LYS C CG  1 
ATOM   11128 C  CD  . LYS C  1 279 ? -8.928  33.890  -14.518 1.00 46.46 ? 296  LYS C CD  1 
ATOM   11129 C  CE  . LYS C  1 279 ? -7.641  34.454  -15.038 1.00 48.87 ? 296  LYS C CE  1 
ATOM   11130 N  NZ  . LYS C  1 279 ? -6.978  35.325  -14.062 1.00 49.52 ? 296  LYS C NZ  1 
ATOM   11131 N  N   . VAL C  1 280 ? -13.314 35.443  -18.006 1.00 42.69 ? 297  VAL C N   1 
ATOM   11132 C  CA  . VAL C  1 280 ? -13.857 35.761  -19.319 1.00 42.86 ? 297  VAL C CA  1 
ATOM   11133 C  C   . VAL C  1 280 ? -15.170 36.527  -19.161 1.00 46.26 ? 297  VAL C C   1 
ATOM   11134 O  O   . VAL C  1 280 ? -15.338 37.601  -19.735 1.00 48.67 ? 297  VAL C O   1 
ATOM   11135 C  CB  . VAL C  1 280 ? -14.048 34.460  -20.124 1.00 43.77 ? 297  VAL C CB  1 
ATOM   11136 C  CG1 . VAL C  1 280 ? -14.605 34.720  -21.519 1.00 44.75 ? 297  VAL C CG1 1 
ATOM   11137 C  CG2 . VAL C  1 280 ? -12.757 33.649  -20.205 1.00 41.00 ? 297  VAL C CG2 1 
ATOM   11138 N  N   . ILE C  1 281 ? -16.097 35.957  -18.384 1.00 48.35 ? 298  ILE C N   1 
ATOM   11139 C  CA  . ILE C  1 281 ? -17.406 36.547  -18.147 1.00 51.31 ? 298  ILE C CA  1 
ATOM   11140 C  C   . ILE C  1 281 ? -17.354 37.368  -16.859 1.00 50.58 ? 298  ILE C C   1 
ATOM   11141 O  O   . ILE C  1 281 ? -17.712 36.880  -15.791 1.00 52.23 ? 298  ILE C O   1 
ATOM   11142 C  CB  . ILE C  1 281 ? -18.486 35.451  -18.077 1.00 52.96 ? 298  ILE C CB  1 
ATOM   11143 C  CG1 . ILE C  1 281 ? -18.414 34.511  -19.275 1.00 53.79 ? 298  ILE C CG1 1 
ATOM   11144 C  CG2 . ILE C  1 281 ? -19.883 36.056  -17.922 1.00 54.48 ? 298  ILE C CG2 1 
ATOM   11145 C  CD1 . ILE C  1 281 ? -19.120 33.188  -19.048 1.00 55.52 ? 298  ILE C CD1 1 
ATOM   11146 N  N   . SER C  1 282 ? -16.951 38.634  -16.980 1.00 47.13 ? 299  SER C N   1 
ATOM   11147 C  CA  . SER C  1 282 ? -16.613 39.456  -15.831 1.00 46.43 ? 299  SER C CA  1 
ATOM   11148 C  C   . SER C  1 282 ? -17.821 40.230  -15.295 1.00 44.47 ? 299  SER C C   1 
ATOM   11149 O  O   . SER C  1 282 ? -17.645 41.148  -14.496 1.00 43.10 ? 299  SER C O   1 
ATOM   11150 C  CB  . SER C  1 282 ? -15.483 40.387  -16.191 1.00 46.67 ? 299  SER C CB  1 
ATOM   11151 O  OG  . SER C  1 282 ? -15.777 41.081  -17.395 1.00 48.08 ? 299  SER C OG  1 
ATOM   11152 N  N   . LYS C  1 283 ? -19.045 39.850  -15.690 1.00 44.23 ? 300  LYS C N   1 
ATOM   11153 C  CA  . LYS C  1 283 ? -20.234 40.545  -15.212 1.00 45.42 ? 300  LYS C CA  1 
ATOM   11154 C  C   . LYS C  1 283 ? -20.399 40.304  -13.712 1.00 43.57 ? 300  LYS C C   1 
ATOM   11155 O  O   . LYS C  1 283 ? -19.926 39.291  -13.196 1.00 42.11 ? 300  LYS C O   1 
ATOM   11156 C  CB  . LYS C  1 283 ? -21.514 40.104  -15.932 1.00 47.22 ? 300  LYS C CB  1 
ATOM   11157 C  CG  . LYS C  1 283 ? -21.983 38.684  -15.635 1.00 47.71 ? 300  LYS C CG  1 
ATOM   11158 C  CD  . LYS C  1 283 ? -23.172 38.258  -16.483 1.00 49.52 ? 300  LYS C CD  1 
ATOM   11159 C  CE  . LYS C  1 283 ? -23.647 36.878  -16.169 1.00 49.77 ? 300  LYS C CE  1 
ATOM   11160 N  NZ  . LYS C  1 283 ? -24.672 36.470  -17.131 1.00 50.85 ? 300  LYS C NZ  1 
ATOM   11161 N  N   . PRO C  1 284 ? -21.088 41.212  -12.976 1.00 42.36 ? 301  PRO C N   1 
ATOM   11162 C  CA  . PRO C  1 284 ? -21.255 41.070  -11.528 1.00 41.59 ? 301  PRO C CA  1 
ATOM   11163 C  C   . PRO C  1 284 ? -21.852 39.725  -11.123 1.00 39.32 ? 301  PRO C C   1 
ATOM   11164 O  O   . PRO C  1 284 ? -22.721 39.197  -11.815 1.00 34.47 ? 301  PRO C O   1 
ATOM   11165 C  CB  . PRO C  1 284 ? -22.181 42.240  -11.141 1.00 42.61 ? 301  PRO C CB  1 
ATOM   11166 C  CG  . PRO C  1 284 ? -22.003 43.252  -12.256 1.00 43.52 ? 301  PRO C CG  1 
ATOM   11167 C  CD  . PRO C  1 284 ? -21.724 42.432  -13.501 1.00 42.57 ? 301  PRO C CD  1 
ATOM   11168 N  N   . ILE C  1 285 ? -21.385 39.204  -9.979  1.00 38.17 ? 302  ILE C N   1 
ATOM   11169 C  CA  . ILE C  1 285 ? -21.858 37.946  -9.420  1.00 40.18 ? 302  ILE C CA  1 
ATOM   11170 C  C   . ILE C  1 285 ? -23.370 37.985  -9.203  1.00 37.67 ? 302  ILE C C   1 
ATOM   11171 O  O   . ILE C  1 285 ? -24.031 36.957  -9.331  1.00 37.21 ? 302  ILE C O   1 
ATOM   11172 C  CB  . ILE C  1 285 ? -21.092 37.600  -8.126  1.00 45.17 ? 302  ILE C CB  1 
ATOM   11173 C  CG1 . ILE C  1 285 ? -19.837 36.784  -8.428  1.00 46.73 ? 302  ILE C CG1 1 
ATOM   11174 C  CG2 . ILE C  1 285 ? -21.977 36.868  -7.115  1.00 46.98 ? 302  ILE C CG2 1 
ATOM   11175 C  CD1 . ILE C  1 285 ? -18.841 37.469  -9.344  1.00 48.31 ? 302  ILE C CD1 1 
ATOM   11176 N  N   . SER C  1 286 ? -23.919 39.168  -8.899  1.00 37.20 ? 303  SER C N   1 
ATOM   11177 C  CA  . SER C  1 286 ? -25.349 39.313  -8.667  1.00 37.72 ? 303  SER C CA  1 
ATOM   11178 C  C   . SER C  1 286 ? -26.182 38.863  -9.873  1.00 36.01 ? 303  SER C C   1 
ATOM   11179 O  O   . SER C  1 286 ? -27.372 38.593  -9.719  1.00 38.47 ? 303  SER C O   1 
ATOM   11180 C  CB  . SER C  1 286 ? -25.695 40.731  -8.261  1.00 39.46 ? 303  SER C CB  1 
ATOM   11181 O  OG  . SER C  1 286 ? -25.205 41.677  -9.203  1.00 42.75 ? 303  SER C OG  1 
ATOM   11182 N  N   . GLU C  1 287 ? -25.562 38.764  -11.059 1.00 34.25 ? 304  GLU C N   1 
ATOM   11183 C  CA  . GLU C  1 287 ? -26.271 38.435  -12.290 1.00 35.44 ? 304  GLU C CA  1 
ATOM   11184 C  C   . GLU C  1 287 ? -26.108 36.965  -12.687 1.00 33.60 ? 304  GLU C C   1 
ATOM   11185 O  O   . GLU C  1 287 ? -26.715 36.519  -13.662 1.00 33.32 ? 304  GLU C O   1 
ATOM   11186 C  CB  . GLU C  1 287 ? -25.758 39.308  -13.436 1.00 37.71 ? 304  GLU C CB  1 
ATOM   11187 C  CG  . GLU C  1 287 ? -26.179 40.771  -13.326 1.00 40.90 ? 304  GLU C CG  1 
ATOM   11188 C  CD  . GLU C  1 287 ? -25.543 41.659  -14.382 1.00 43.31 ? 304  GLU C CD  1 
ATOM   11189 O  OE1 . GLU C  1 287 ? -25.515 41.255  -15.560 1.00 42.96 ? 304  GLU C OE1 1 
ATOM   11190 O  OE2 . GLU C  1 287 ? -25.084 42.763  -14.027 1.00 46.43 ? 304  GLU C OE2 1 
ATOM   11191 N  N   . HIS C  1 288 ? -25.279 36.213  -11.956 1.00 32.64 ? 305  HIS C N   1 
ATOM   11192 C  CA  . HIS C  1 288 ? -25.077 34.806  -12.263 1.00 33.06 ? 305  HIS C CA  1 
ATOM   11193 C  C   . HIS C  1 288 ? -26.254 33.999  -11.725 1.00 30.27 ? 305  HIS C C   1 
ATOM   11194 O  O   . HIS C  1 288 ? -26.898 34.395  -10.757 1.00 29.61 ? 305  HIS C O   1 
ATOM   11195 C  CB  . HIS C  1 288 ? -23.723 34.308  -11.744 1.00 35.63 ? 305  HIS C CB  1 
ATOM   11196 C  CG  . HIS C  1 288 ? -22.582 34.716  -12.616 1.00 40.29 ? 305  HIS C CG  1 
ATOM   11197 N  ND1 . HIS C  1 288 ? -22.339 34.106  -13.828 1.00 44.44 ? 305  HIS C ND1 1 
ATOM   11198 C  CD2 . HIS C  1 288 ? -21.656 35.676  -12.491 1.00 42.00 ? 305  HIS C CD2 1 
ATOM   11199 C  CE1 . HIS C  1 288 ? -21.284 34.675  -14.399 1.00 47.04 ? 305  HIS C CE1 1 
ATOM   11200 N  NE2 . HIS C  1 288 ? -20.852 35.631  -13.601 1.00 45.67 ? 305  HIS C NE2 1 
ATOM   11201 N  N   . LYS C  1 289 ? -26.534 32.877  -12.393 1.00 29.34 ? 306  LYS C N   1 
ATOM   11202 C  CA  . LYS C  1 289 ? -27.517 31.916  -11.926 1.00 29.29 ? 306  LYS C CA  1 
ATOM   11203 C  C   . LYS C  1 289 ? -27.012 30.525  -12.295 1.00 27.77 ? 306  LYS C C   1 
ATOM   11204 O  O   . LYS C  1 289 ? -26.671 30.277  -13.450 1.00 26.17 ? 306  LYS C O   1 
ATOM   11205 C  CB  . LYS C  1 289 ? -28.907 32.208  -12.503 1.00 31.33 ? 306  LYS C CB  1 
ATOM   11206 C  CG  . LYS C  1 289 ? -30.021 31.400  -11.851 1.00 34.37 ? 306  LYS C CG  1 
ATOM   11207 C  CD  . LYS C  1 289 ? -31.412 31.606  -12.436 1.00 38.04 ? 306  LYS C CD  1 
ATOM   11208 C  CE  . LYS C  1 289 ? -31.939 33.003  -12.296 1.00 39.38 ? 306  LYS C CE  1 
ATOM   11209 N  NZ  . LYS C  1 289 ? -33.296 33.071  -12.845 1.00 40.02 ? 306  LYS C NZ  1 
ATOM   11210 N  N   . ILE C  1 290 ? -26.925 29.651  -11.285 1.00 26.45 ? 307  ILE C N   1 
ATOM   11211 C  CA  . ILE C  1 290 ? -26.340 28.328  -11.434 1.00 26.49 ? 307  ILE C CA  1 
ATOM   11212 C  C   . ILE C  1 290 ? -27.467 27.300  -11.379 1.00 25.77 ? 307  ILE C C   1 
ATOM   11213 O  O   . ILE C  1 290 ? -28.243 27.294  -10.424 1.00 26.00 ? 307  ILE C O   1 
ATOM   11214 C  CB  . ILE C  1 290 ? -25.297 28.054  -10.331 1.00 27.33 ? 307  ILE C CB  1 
ATOM   11215 C  CG1 . ILE C  1 290 ? -24.375 29.253  -10.068 1.00 29.64 ? 307  ILE C CG1 1 
ATOM   11216 C  CG2 . ILE C  1 290 ? -24.499 26.783  -10.628 1.00 27.15 ? 307  ILE C CG2 1 
ATOM   11217 C  CD1 . ILE C  1 290 ? -23.586 29.715  -11.277 1.00 31.12 ? 307  ILE C CD1 1 
ATOM   11218 N  N   . LEU C  1 291 ? -27.534 26.425  -12.391 1.00 25.63 ? 308  LEU C N   1 
ATOM   11219 C  CA  . LEU C  1 291 ? -28.491 25.328  -12.396 1.00 25.86 ? 308  LEU C CA  1 
ATOM   11220 C  C   . LEU C  1 291 ? -27.729 24.003  -12.402 1.00 25.14 ? 308  LEU C C   1 
ATOM   11221 O  O   . LEU C  1 291 ? -26.989 23.714  -13.339 1.00 23.19 ? 308  LEU C O   1 
ATOM   11222 C  CB  . LEU C  1 291 ? -29.430 25.440  -13.597 1.00 25.92 ? 308  LEU C CB  1 
ATOM   11223 C  CG  . LEU C  1 291 ? -30.452 24.307  -13.770 1.00 26.93 ? 308  LEU C CG  1 
ATOM   11224 C  CD1 . LEU C  1 291 ? -31.331 24.109  -12.547 1.00 26.62 ? 308  LEU C CD1 1 
ATOM   11225 C  CD2 . LEU C  1 291 ? -31.317 24.569  -14.995 1.00 27.61 ? 308  LEU C CD2 1 
ATOM   11226 N  N   . PHE C  1 292 ? -27.938 23.206  -11.351 1.00 25.30 ? 309  PHE C N   1 
ATOM   11227 C  CA  . PHE C  1 292 ? -27.321 21.895  -11.228 1.00 25.47 ? 309  PHE C CA  1 
ATOM   11228 C  C   . PHE C  1 292 ? -28.245 20.832  -11.814 1.00 25.88 ? 309  PHE C C   1 
ATOM   11229 O  O   . PHE C  1 292 ? -29.457 20.861  -11.586 1.00 25.04 ? 309  PHE C O   1 
ATOM   11230 C  CB  . PHE C  1 292 ? -27.046 21.516  -9.770  1.00 24.63 ? 309  PHE C CB  1 
ATOM   11231 C  CG  . PHE C  1 292 ? -25.863 22.219  -9.119  1.00 24.16 ? 309  PHE C CG  1 
ATOM   11232 C  CD1 . PHE C  1 292 ? -26.013 23.462  -8.519  1.00 23.61 ? 309  PHE C CD1 1 
ATOM   11233 C  CD2 . PHE C  1 292 ? -24.609 21.618  -9.091  1.00 24.06 ? 309  PHE C CD2 1 
ATOM   11234 C  CE1 . PHE C  1 292 ? -24.934 24.094  -7.921  1.00 23.89 ? 309  PHE C CE1 1 
ATOM   11235 C  CE2 . PHE C  1 292 ? -23.533 22.255  -8.500  1.00 24.00 ? 309  PHE C CE2 1 
ATOM   11236 C  CZ  . PHE C  1 292 ? -23.699 23.489  -7.910  1.00 24.06 ? 309  PHE C CZ  1 
ATOM   11237 N  N   . LEU C  1 293 ? -27.642 19.903  -12.568 1.00 26.65 ? 310  LEU C N   1 
ATOM   11238 C  CA  . LEU C  1 293 ? -28.258 18.619  -12.861 1.00 27.85 ? 310  LEU C CA  1 
ATOM   11239 C  C   . LEU C  1 293 ? -27.752 17.615  -11.827 1.00 27.27 ? 310  LEU C C   1 
ATOM   11240 O  O   . LEU C  1 293 ? -26.603 17.197  -11.879 1.00 28.75 ? 310  LEU C O   1 
ATOM   11241 C  CB  . LEU C  1 293 ? -27.958 18.137  -14.278 1.00 28.52 ? 310  LEU C CB  1 
ATOM   11242 C  CG  . LEU C  1 293 ? -28.622 16.814  -14.677 1.00 30.37 ? 310  LEU C CG  1 
ATOM   11243 C  CD1 . LEU C  1 293 ? -30.055 17.038  -15.114 1.00 31.41 ? 310  LEU C CD1 1 
ATOM   11244 C  CD2 . LEU C  1 293 ? -27.836 16.085  -15.751 1.00 31.68 ? 310  LEU C CD2 1 
ATOM   11245 N  N   . GLY C  1 294 ? -28.639 17.232  -10.911 1.00 28.64 ? 311  GLY C N   1 
ATOM   11246 C  CA  . GLY C  1 294 ? -28.285 16.442  -9.747  1.00 29.49 ? 311  GLY C CA  1 
ATOM   11247 C  C   . GLY C  1 294 ? -28.377 17.301  -8.493  1.00 29.83 ? 311  GLY C C   1 
ATOM   11248 O  O   . GLY C  1 294 ? -28.250 18.526  -8.567  1.00 29.41 ? 311  GLY C O   1 
ATOM   11249 N  N   . ALA C  1 295 ? -28.628 16.639  -7.360  1.00 28.70 ? 312  ALA C N   1 
ATOM   11250 C  CA  . ALA C  1 295 ? -28.696 17.298  -6.067  1.00 28.91 ? 312  ALA C CA  1 
ATOM   11251 C  C   . ALA C  1 295 ? -28.076 16.385  -5.011  1.00 29.02 ? 312  ALA C C   1 
ATOM   11252 O  O   . ALA C  1 295 ? -28.560 16.307  -3.890  1.00 28.53 ? 312  ALA C O   1 
ATOM   11253 C  CB  . ALA C  1 295 ? -30.132 17.652  -5.743  1.00 28.73 ? 312  ALA C CB  1 
ATOM   11254 N  N   . GLY C  1 296 ? -26.985 15.712  -5.394  1.00 31.48 ? 313  GLY C N   1 
ATOM   11255 C  CA  . GLY C  1 296 ? -26.345 14.716  -4.552  1.00 30.98 ? 313  GLY C CA  1 
ATOM   11256 C  C   . GLY C  1 296 ? -25.138 15.299  -3.827  1.00 31.45 ? 313  GLY C C   1 
ATOM   11257 O  O   . GLY C  1 296 ? -25.106 16.488  -3.508  1.00 29.49 ? 313  GLY C O   1 
ATOM   11258 N  N   . GLU C  1 297 ? -24.149 14.433  -3.586  1.00 31.60 ? 314  GLU C N   1 
ATOM   11259 C  CA  . GLU C  1 297 ? -22.985 14.774  -2.790  1.00 30.49 ? 314  GLU C CA  1 
ATOM   11260 C  C   . GLU C  1 297 ? -22.201 15.889  -3.475  1.00 29.36 ? 314  GLU C C   1 
ATOM   11261 O  O   . GLU C  1 297 ? -21.819 16.864  -2.830  1.00 28.96 ? 314  GLU C O   1 
ATOM   11262 C  CB  . GLU C  1 297 ? -22.148 13.512  -2.574  1.00 31.23 ? 314  GLU C CB  1 
ATOM   11263 C  CG  . GLU C  1 297 ? -20.768 13.775  -1.978  1.00 32.00 ? 314  GLU C CG  1 
ATOM   11264 C  CD  . GLU C  1 297 ? -20.012 12.514  -1.606  1.00 31.99 ? 314  GLU C CD  1 
ATOM   11265 O  OE1 . GLU C  1 297 ? -20.311 11.933  -0.539  1.00 30.56 ? 314  GLU C OE1 1 
ATOM   11266 O  OE2 . GLU C  1 297 ? -19.135 12.109  -2.397  1.00 32.95 ? 314  GLU C OE2 1 
ATOM   11267 N  N   . ALA C  1 298 ? -21.957 15.724  -4.778  1.00 28.39 ? 315  ALA C N   1 
ATOM   11268 C  CA  . ALA C  1 298 ? -21.176 16.684  -5.541  1.00 29.23 ? 315  ALA C CA  1 
ATOM   11269 C  C   . ALA C  1 298 ? -21.907 18.025  -5.608  1.00 27.80 ? 315  ALA C C   1 
ATOM   11270 O  O   . ALA C  1 298 ? -21.304 19.055  -5.343  1.00 27.41 ? 315  ALA C O   1 
ATOM   11271 C  CB  . ALA C  1 298 ? -20.869 16.135  -6.918  1.00 30.13 ? 315  ALA C CB  1 
ATOM   11272 N  N   . ALA C  1 299 ? -23.208 18.002  -5.923  1.00 28.39 ? 316  ALA C N   1 
ATOM   11273 C  CA  . ALA C  1 299 ? -23.992 19.223  -6.058  1.00 28.60 ? 316  ALA C CA  1 
ATOM   11274 C  C   . ALA C  1 299 ? -23.945 20.045  -4.773  1.00 28.52 ? 316  ALA C C   1 
ATOM   11275 O  O   . ALA C  1 299 ? -23.740 21.256  -4.817  1.00 27.53 ? 316  ALA C O   1 
ATOM   11276 C  CB  . ALA C  1 299 ? -25.417 18.890  -6.422  1.00 29.05 ? 316  ALA C CB  1 
ATOM   11277 N  N   . LEU C  1 300 ? -24.156 19.375  -3.635  1.00 28.69 ? 317  LEU C N   1 
ATOM   11278 C  CA  . LEU C  1 300 ? -24.266 20.042  -2.347  1.00 28.69 ? 317  LEU C CA  1 
ATOM   11279 C  C   . LEU C  1 300 ? -22.907 20.590  -1.924  1.00 26.00 ? 317  LEU C C   1 
ATOM   11280 O  O   . LEU C  1 300 ? -22.806 21.738  -1.505  1.00 27.71 ? 317  LEU C O   1 
ATOM   11281 C  CB  . LEU C  1 300 ? -24.835 19.056  -1.331  1.00 30.25 ? 317  LEU C CB  1 
ATOM   11282 C  CG  . LEU C  1 300 ? -26.277 18.611  -1.588  1.00 30.61 ? 317  LEU C CG  1 
ATOM   11283 C  CD1 . LEU C  1 300 ? -26.632 17.417  -0.715  1.00 32.12 ? 317  LEU C CD1 1 
ATOM   11284 C  CD2 . LEU C  1 300 ? -27.238 19.761  -1.362  1.00 29.77 ? 317  LEU C CD2 1 
ATOM   11285 N  N   . GLY C  1 301 ? -21.861 19.773  -2.068  1.00 24.95 ? 318  GLY C N   1 
ATOM   11286 C  CA  . GLY C  1 301 ? -20.505 20.225  -1.818  1.00 23.80 ? 318  GLY C CA  1 
ATOM   11287 C  C   . GLY C  1 301 ? -20.186 21.488  -2.615  1.00 22.71 ? 318  GLY C C   1 
ATOM   11288 O  O   . GLY C  1 301 ? -19.759 22.490  -2.047  1.00 21.33 ? 318  GLY C O   1 
ATOM   11289 N  N   . ILE C  1 302 ? -20.423 21.430  -3.931  1.00 21.17 ? 319  ILE C N   1 
ATOM   11290 C  CA  . ILE C  1 302 ? -20.053 22.512  -4.833  1.00 21.71 ? 319  ILE C CA  1 
ATOM   11291 C  C   . ILE C  1 302 ? -20.865 23.760  -4.496  1.00 21.31 ? 319  ILE C C   1 
ATOM   11292 O  O   . ILE C  1 302 ? -20.301 24.849  -4.407  1.00 22.10 ? 319  ILE C O   1 
ATOM   11293 C  CB  . ILE C  1 302 ? -20.228 22.104  -6.310  1.00 21.49 ? 319  ILE C CB  1 
ATOM   11294 C  CG1 . ILE C  1 302 ? -19.315 20.942  -6.688  1.00 21.67 ? 319  ILE C CG1 1 
ATOM   11295 C  CG2 . ILE C  1 302 ? -20.000 23.299  -7.239  1.00 21.85 ? 319  ILE C CG2 1 
ATOM   11296 C  CD1 . ILE C  1 302 ? -19.718 20.241  -7.977  1.00 22.51 ? 319  ILE C CD1 1 
ATOM   11297 N  N   . ALA C  1 303 ? -22.180 23.590  -4.315  1.00 21.16 ? 320  ALA C N   1 
ATOM   11298 C  CA  . ALA C  1 303 ? -23.074 24.717  -4.098  1.00 21.99 ? 320  ALA C CA  1 
ATOM   11299 C  C   . ALA C  1 303 ? -22.703 25.451  -2.811  1.00 23.46 ? 320  ALA C C   1 
ATOM   11300 O  O   . ALA C  1 303 ? -22.681 26.676  -2.778  1.00 23.32 ? 320  ALA C O   1 
ATOM   11301 C  CB  . ALA C  1 303 ? -24.507 24.247  -4.070  1.00 22.67 ? 320  ALA C CB  1 
ATOM   11302 N  N   . ASN C  1 304 ? -22.376 24.704  -1.752  1.00 24.86 ? 321  ASN C N   1 
ATOM   11303 C  CA  . ASN C  1 304 ? -22.059 25.335  -0.480  1.00 26.24 ? 321  ASN C CA  1 
ATOM   11304 C  C   . ASN C  1 304 ? -20.785 26.170  -0.606  1.00 24.45 ? 321  ASN C C   1 
ATOM   11305 O  O   . ASN C  1 304 ? -20.680 27.222  0.025   1.00 24.69 ? 321  ASN C O   1 
ATOM   11306 C  CB  . ASN C  1 304 ? -22.060 24.332  0.670   1.00 30.50 ? 321  ASN C CB  1 
ATOM   11307 C  CG  . ASN C  1 304 ? -23.468 23.990  1.111   1.00 34.33 ? 321  ASN C CG  1 
ATOM   11308 O  OD1 . ASN C  1 304 ? -24.247 24.881  1.478   1.00 37.60 ? 321  ASN C OD1 1 
ATOM   11309 N  ND2 . ASN C  1 304 ? -23.822 22.712  1.086   1.00 37.29 ? 321  ASN C ND2 1 
ATOM   11310 N  N   . LEU C  1 305 ? -19.831 25.745  -1.445  1.00 23.10 ? 322  LEU C N   1 
ATOM   11311 C  CA  . LEU C  1 305 ? -18.606 26.513  -1.602  1.00 22.93 ? 322  LEU C CA  1 
ATOM   11312 C  C   . LEU C  1 305 ? -18.838 27.714  -2.525  1.00 22.33 ? 322  LEU C C   1 
ATOM   11313 O  O   . LEU C  1 305 ? -18.234 28.762  -2.311  1.00 22.12 ? 322  LEU C O   1 
ATOM   11314 C  CB  . LEU C  1 305 ? -17.441 25.641  -2.064  1.00 23.33 ? 322  LEU C CB  1 
ATOM   11315 C  CG  . LEU C  1 305 ? -16.043 26.187  -1.756  1.00 23.52 ? 322  LEU C CG  1 
ATOM   11316 C  CD1 . LEU C  1 305 ? -15.736 26.219  -0.260  1.00 23.85 ? 322  LEU C CD1 1 
ATOM   11317 C  CD2 . LEU C  1 305 ? -14.991 25.378  -2.487  1.00 23.00 ? 322  LEU C CD2 1 
ATOM   11318 N  N   . ILE C  1 306 ? -19.692 27.577  -3.550  1.00 23.02 ? 323  ILE C N   1 
ATOM   11319 C  CA  . ILE C  1 306 ? -20.063 28.712  -4.393  1.00 22.71 ? 323  ILE C CA  1 
ATOM   11320 C  C   . ILE C  1 306 ? -20.659 29.820  -3.521  1.00 22.94 ? 323  ILE C C   1 
ATOM   11321 O  O   . ILE C  1 306 ? -20.327 30.989  -3.694  1.00 22.78 ? 323  ILE C O   1 
ATOM   11322 C  CB  . ILE C  1 306 ? -21.028 28.306  -5.526  1.00 22.98 ? 323  ILE C CB  1 
ATOM   11323 C  CG1 . ILE C  1 306 ? -20.340 27.401  -6.563  1.00 23.48 ? 323  ILE C CG1 1 
ATOM   11324 C  CG2 . ILE C  1 306 ? -21.651 29.543  -6.189  1.00 22.61 ? 323  ILE C CG2 1 
ATOM   11325 C  CD1 . ILE C  1 306 ? -21.285 26.788  -7.583  1.00 23.84 ? 323  ILE C CD1 1 
ATOM   11326 N  N   . VAL C  1 307 ? -21.543 29.450  -2.589  1.00 23.22 ? 324  VAL C N   1 
ATOM   11327 C  CA  . VAL C  1 307 ? -22.178 30.410  -1.697  1.00 24.53 ? 324  VAL C CA  1 
ATOM   11328 C  C   . VAL C  1 307 ? -21.129 31.163  -0.875  1.00 25.10 ? 324  VAL C C   1 
ATOM   11329 O  O   . VAL C  1 307 ? -21.210 32.383  -0.731  1.00 24.49 ? 324  VAL C O   1 
ATOM   11330 C  CB  . VAL C  1 307 ? -23.213 29.693  -0.809  1.00 25.41 ? 324  VAL C CB  1 
ATOM   11331 C  CG1 . VAL C  1 307 ? -23.675 30.548  0.364   1.00 27.13 ? 324  VAL C CG1 1 
ATOM   11332 C  CG2 . VAL C  1 307 ? -24.409 29.225  -1.626  1.00 25.73 ? 324  VAL C CG2 1 
ATOM   11333 N  N   . MET C  1 308 ? -20.129 30.451  -0.343  1.00 24.61 ? 325  MET C N   1 
ATOM   11334 C  CA  . MET C  1 308 ? -19.082 31.093  0.439   1.00 25.46 ? 325  MET C CA  1 
ATOM   11335 C  C   . MET C  1 308 ? -18.284 32.070  -0.426  1.00 25.66 ? 325  MET C C   1 
ATOM   11336 O  O   . MET C  1 308 ? -17.909 33.144  0.045   1.00 25.39 ? 325  MET C O   1 
ATOM   11337 C  CB  . MET C  1 308 ? -18.143 30.058  1.065   1.00 26.47 ? 325  MET C CB  1 
ATOM   11338 C  CG  . MET C  1 308 ? -18.787 29.273  2.184   1.00 27.83 ? 325  MET C CG  1 
ATOM   11339 S  SD  . MET C  1 308 ? -17.699 27.979  2.811   1.00 31.08 ? 325  MET C SD  1 
ATOM   11340 C  CE  . MET C  1 308 ? -16.405 28.968  3.573   1.00 30.40 ? 325  MET C CE  1 
ATOM   11341 N  N   . SER C  1 309 ? -18.043 31.700  -1.690  1.00 23.84 ? 326  SER C N   1 
ATOM   11342 C  CA  . SER C  1 309 ? -17.365 32.572  -2.635  1.00 25.96 ? 326  SER C CA  1 
ATOM   11343 C  C   . SER C  1 309 ? -18.200 33.828  -2.894  1.00 26.20 ? 326  SER C C   1 
ATOM   11344 O  O   . SER C  1 309 ? -17.659 34.930  -2.923  1.00 26.20 ? 326  SER C O   1 
ATOM   11345 C  CB  . SER C  1 309 ? -17.057 31.838  -3.926  1.00 26.24 ? 326  SER C CB  1 
ATOM   11346 O  OG  . SER C  1 309 ? -16.422 32.681  -4.878  1.00 25.74 ? 326  SER C OG  1 
ATOM   11347 N  N   . MET C  1 310 ? -19.518 33.652  -3.074  1.00 26.51 ? 327  MET C N   1 
ATOM   11348 C  CA  . MET C  1 310 ? -20.412 34.759  -3.397  1.00 27.80 ? 327  MET C CA  1 
ATOM   11349 C  C   . MET C  1 310 ? -20.537 35.724  -2.216  1.00 29.32 ? 327  MET C C   1 
ATOM   11350 O  O   . MET C  1 310 ? -20.604 36.939  -2.423  1.00 30.23 ? 327  MET C O   1 
ATOM   11351 C  CB  . MET C  1 310 ? -21.808 34.254  -3.774  1.00 27.73 ? 327  MET C CB  1 
ATOM   11352 C  CG  . MET C  1 310 ? -21.899 33.635  -5.155  1.00 28.54 ? 327  MET C CG  1 
ATOM   11353 S  SD  . MET C  1 310 ? -23.549 32.981  -5.477  1.00 29.90 ? 327  MET C SD  1 
ATOM   11354 C  CE  . MET C  1 310 ? -23.396 32.565  -7.220  1.00 30.00 ? 327  MET C CE  1 
ATOM   11355 N  N   . VAL C  1 311 ? -20.606 35.170  -0.995  1.00 29.14 ? 328  VAL C N   1 
ATOM   11356 C  CA  . VAL C  1 311 ? -20.707 35.946  0.235   1.00 30.29 ? 328  VAL C CA  1 
ATOM   11357 C  C   . VAL C  1 311 ? -19.462 36.816  0.405   1.00 32.86 ? 328  VAL C C   1 
ATOM   11358 O  O   . VAL C  1 311 ? -19.547 37.940  0.890   1.00 32.78 ? 328  VAL C O   1 
ATOM   11359 C  CB  . VAL C  1 311 ? -20.929 35.034  1.462   1.00 31.82 ? 328  VAL C CB  1 
ATOM   11360 C  CG1 . VAL C  1 311 ? -20.562 35.711  2.782   1.00 32.35 ? 328  VAL C CG1 1 
ATOM   11361 C  CG2 . VAL C  1 311 ? -22.358 34.506  1.519   1.00 31.96 ? 328  VAL C CG2 1 
ATOM   11362 N  N   . GLU C  1 312 ? -18.303 36.281  0.013   1.00 34.97 ? 329  GLU C N   1 
ATOM   11363 C  CA  . GLU C  1 312 ? -17.050 37.015  0.062   1.00 37.80 ? 329  GLU C CA  1 
ATOM   11364 C  C   . GLU C  1 312 ? -17.075 38.189  -0.918  1.00 38.46 ? 329  GLU C C   1 
ATOM   11365 O  O   . GLU C  1 312 ? -16.350 39.162  -0.729  1.00 38.16 ? 329  GLU C O   1 
ATOM   11366 C  CB  . GLU C  1 312 ? -15.932 36.017  -0.234  1.00 41.48 ? 329  GLU C CB  1 
ATOM   11367 C  CG  . GLU C  1 312 ? -14.525 36.556  -0.011  1.00 44.94 ? 329  GLU C CG  1 
ATOM   11368 C  CD  . GLU C  1 312 ? -13.490 35.445  0.027   1.00 46.07 ? 329  GLU C CD  1 
ATOM   11369 O  OE1 . GLU C  1 312 ? -13.045 35.113  1.146   1.00 46.82 ? 329  GLU C OE1 1 
ATOM   11370 O  OE2 . GLU C  1 312 ? -13.135 34.913  -1.048  1.00 46.10 ? 329  GLU C OE2 1 
ATOM   11371 N  N   . ASN C  1 313 ? -17.915 38.096  -1.958  1.00 38.13 ? 330  ASN C N   1 
ATOM   11372 C  CA  . ASN C  1 313 ? -17.983 39.102  -3.007  1.00 38.98 ? 330  ASN C CA  1 
ATOM   11373 C  C   . ASN C  1 313 ? -19.250 39.954  -2.888  1.00 37.25 ? 330  ASN C C   1 
ATOM   11374 O  O   . ASN C  1 313 ? -19.694 40.525  -3.880  1.00 38.04 ? 330  ASN C O   1 
ATOM   11375 C  CB  . ASN C  1 313 ? -17.877 38.446  -4.381  1.00 39.33 ? 330  ASN C CB  1 
ATOM   11376 C  CG  . ASN C  1 313 ? -16.484 37.931  -4.646  1.00 41.01 ? 330  ASN C CG  1 
ATOM   11377 O  OD1 . ASN C  1 313 ? -15.581 38.719  -4.939  1.00 42.38 ? 330  ASN C OD1 1 
ATOM   11378 N  ND2 . ASN C  1 313 ? -16.285 36.625  -4.552  1.00 43.61 ? 330  ASN C ND2 1 
ATOM   11379 N  N   . GLY C  1 314 ? -19.837 40.040  -1.687  1.00 36.55 ? 331  GLY C N   1 
ATOM   11380 C  CA  . GLY C  1 314 ? -20.782 41.105  -1.385  1.00 37.69 ? 331  GLY C CA  1 
ATOM   11381 C  C   . GLY C  1 314 ? -22.228 40.640  -1.208  1.00 37.15 ? 331  GLY C C   1 
ATOM   11382 O  O   . GLY C  1 314 ? -23.047 41.403  -0.698  1.00 39.14 ? 331  GLY C O   1 
ATOM   11383 N  N   . LEU C  1 315 ? -22.560 39.412  -1.630  1.00 35.56 ? 332  LEU C N   1 
ATOM   11384 C  CA  . LEU C  1 315 ? -23.913 38.902  -1.461  1.00 34.93 ? 332  LEU C CA  1 
ATOM   11385 C  C   . LEU C  1 315 ? -24.100 38.402  -0.032  1.00 33.57 ? 332  LEU C C   1 
ATOM   11386 O  O   . LEU C  1 315 ? -23.152 37.940  0.591   1.00 33.89 ? 332  LEU C O   1 
ATOM   11387 C  CB  . LEU C  1 315 ? -24.213 37.788  -2.463  1.00 35.19 ? 332  LEU C CB  1 
ATOM   11388 C  CG  . LEU C  1 315 ? -24.341 38.210  -3.929  1.00 36.91 ? 332  LEU C CG  1 
ATOM   11389 C  CD1 . LEU C  1 315 ? -24.611 36.992  -4.785  1.00 38.13 ? 332  LEU C CD1 1 
ATOM   11390 C  CD2 . LEU C  1 315 ? -25.439 39.250  -4.124  1.00 37.72 ? 332  LEU C CD2 1 
ATOM   11391 N  N   . SER C  1 316 ? -25.339 38.474  0.469   1.00 33.84 ? 333  SER C N   1 
ATOM   11392 C  CA  . SER C  1 316 ? -25.690 37.792  1.705   1.00 35.43 ? 333  SER C CA  1 
ATOM   11393 C  C   . SER C  1 316 ? -25.818 36.296  1.424   1.00 35.68 ? 333  SER C C   1 
ATOM   11394 O  O   . SER C  1 316 ? -25.987 35.884  0.276   1.00 33.92 ? 333  SER C O   1 
ATOM   11395 C  CB  . SER C  1 316 ? -26.956 38.340  2.324   1.00 35.27 ? 333  SER C CB  1 
ATOM   11396 O  OG  . SER C  1 316 ? -28.111 37.907  1.619   1.00 35.09 ? 333  SER C OG  1 
ATOM   11397 N  N   . GLU C  1 317 ? -25.740 35.494  2.489   1.00 35.26 ? 334  GLU C N   1 
ATOM   11398 C  CA  . GLU C  1 317 ? -25.839 34.053  2.365   1.00 37.21 ? 334  GLU C CA  1 
ATOM   11399 C  C   . GLU C  1 317 ? -27.155 33.693  1.678   1.00 37.45 ? 334  GLU C C   1 
ATOM   11400 O  O   . GLU C  1 317 ? -27.168 32.893  0.743   1.00 33.44 ? 334  GLU C O   1 
ATOM   11401 C  CB  . GLU C  1 317 ? -25.731 33.393  3.738   1.00 38.16 ? 334  GLU C CB  1 
ATOM   11402 C  CG  . GLU C  1 317 ? -25.595 31.877  3.664   1.00 40.46 ? 334  GLU C CG  1 
ATOM   11403 C  CD  . GLU C  1 317 ? -25.374 31.219  5.011   1.00 41.83 ? 334  GLU C CD  1 
ATOM   11404 O  OE1 . GLU C  1 317 ? -26.330 31.201  5.808   1.00 42.87 ? 334  GLU C OE1 1 
ATOM   11405 O  OE2 . GLU C  1 317 ? -24.247 30.746  5.266   1.00 44.75 ? 334  GLU C OE2 1 
ATOM   11406 N  N   . GLN C  1 318 ? -28.251 34.307  2.145   1.00 38.27 ? 335  GLN C N   1 
ATOM   11407 C  CA  . GLN C  1 318 ? -29.586 33.980  1.666   1.00 40.60 ? 335  GLN C CA  1 
ATOM   11408 C  C   . GLN C  1 318 ? -29.731 34.351  0.187   1.00 38.10 ? 335  GLN C C   1 
ATOM   11409 O  O   . GLN C  1 318 ? -30.353 33.609  -0.575  1.00 36.70 ? 335  GLN C O   1 
ATOM   11410 C  CB  . GLN C  1 318 ? -30.677 34.602  2.545   1.00 44.40 ? 335  GLN C CB  1 
ATOM   11411 C  CG  . GLN C  1 318 ? -30.570 36.111  2.748   1.00 47.94 ? 335  GLN C CG  1 
ATOM   11412 C  CD  . GLN C  1 318 ? -29.854 36.527  4.021   1.00 51.97 ? 335  GLN C CD  1 
ATOM   11413 O  OE1 . GLN C  1 318 ? -28.775 36.023  4.365   1.00 51.04 ? 335  GLN C OE1 1 
ATOM   11414 N  NE2 . GLN C  1 318 ? -30.454 37.469  4.737   1.00 52.14 ? 335  GLN C NE2 1 
ATOM   11415 N  N   . GLU C  1 319 ? -29.150 35.488  -0.218  1.00 35.82 ? 336  GLU C N   1 
ATOM   11416 C  CA  . GLU C  1 319 ? -29.240 35.954  -1.595  1.00 35.86 ? 336  GLU C CA  1 
ATOM   11417 C  C   . GLU C  1 319 ? -28.393 35.080  -2.517  1.00 33.09 ? 336  GLU C C   1 
ATOM   11418 O  O   . GLU C  1 319 ? -28.782 34.824  -3.655  1.00 31.15 ? 336  GLU C O   1 
ATOM   11419 C  CB  . GLU C  1 319 ? -28.828 37.423  -1.700  1.00 39.63 ? 336  GLU C CB  1 
ATOM   11420 C  CG  . GLU C  1 319 ? -29.963 38.379  -1.341  1.00 44.25 ? 336  GLU C CG  1 
ATOM   11421 C  CD  . GLU C  1 319 ? -31.054 38.436  -2.398  1.00 49.31 ? 336  GLU C CD  1 
ATOM   11422 O  OE1 . GLU C  1 319 ? -30.804 39.055  -3.456  1.00 55.68 ? 336  GLU C OE1 1 
ATOM   11423 O  OE2 . GLU C  1 319 ? -32.136 37.843  -2.184  1.00 51.31 ? 336  GLU C OE2 1 
ATOM   11424 N  N   . ALA C  1 320 ? -27.227 34.643  -2.021  1.00 29.67 ? 337  ALA C N   1 
ATOM   11425 C  CA  . ALA C  1 320 ? -26.351 33.762  -2.775  1.00 27.91 ? 337  ALA C CA  1 
ATOM   11426 C  C   . ALA C  1 320 ? -27.042 32.425  -3.038  1.00 26.94 ? 337  ALA C C   1 
ATOM   11427 O  O   . ALA C  1 320 ? -26.988 31.910  -4.152  1.00 26.35 ? 337  ALA C O   1 
ATOM   11428 C  CB  . ALA C  1 320 ? -25.045 33.582  -2.033  1.00 27.04 ? 337  ALA C CB  1 
ATOM   11429 N  N   . GLN C  1 321 ? -27.702 31.884  -2.006  1.00 27.46 ? 338  GLN C N   1 
ATOM   11430 C  CA  . GLN C  1 321 ? -28.421 30.621  -2.097  1.00 28.76 ? 338  GLN C CA  1 
ATOM   11431 C  C   . GLN C  1 321 ? -29.536 30.694  -3.142  1.00 30.48 ? 338  GLN C C   1 
ATOM   11432 O  O   . GLN C  1 321 ? -29.787 29.712  -3.835  1.00 29.29 ? 338  GLN C O   1 
ATOM   11433 C  CB  . GLN C  1 321 ? -28.975 30.229  -0.725  1.00 28.78 ? 338  GLN C CB  1 
ATOM   11434 C  CG  . GLN C  1 321 ? -27.907 29.705  0.231   1.00 30.01 ? 338  GLN C CG  1 
ATOM   11435 C  CD  . GLN C  1 321 ? -28.348 29.670  1.678   1.00 30.17 ? 338  GLN C CD  1 
ATOM   11436 O  OE1 . GLN C  1 321 ? -29.387 30.222  2.053   1.00 30.94 ? 338  GLN C OE1 1 
ATOM   11437 N  NE2 . GLN C  1 321 ? -27.544 29.024  2.509   1.00 29.93 ? 338  GLN C NE2 1 
ATOM   11438 N  N   . LYS C  1 322 ? -30.186 31.860  -3.260  1.00 32.29 ? 339  LYS C N   1 
ATOM   11439 C  CA  . LYS C  1 322 ? -31.288 32.048  -4.195  1.00 34.57 ? 339  LYS C CA  1 
ATOM   11440 C  C   . LYS C  1 322 ? -30.808 32.093  -5.649  1.00 32.32 ? 339  LYS C C   1 
ATOM   11441 O  O   . LYS C  1 322 ? -31.630 32.041  -6.559  1.00 32.92 ? 339  LYS C O   1 
ATOM   11442 C  CB  . LYS C  1 322 ? -32.115 33.290  -3.829  1.00 38.40 ? 339  LYS C CB  1 
ATOM   11443 C  CG  . LYS C  1 322 ? -33.187 33.037  -2.768  1.00 42.36 ? 339  LYS C CG  1 
ATOM   11444 C  CD  . LYS C  1 322 ? -33.904 34.277  -2.246  1.00 45.21 ? 339  LYS C CD  1 
ATOM   11445 C  CE  . LYS C  1 322 ? -33.098 35.007  -1.216  1.00 47.76 ? 339  LYS C CE  1 
ATOM   11446 N  NZ  . LYS C  1 322 ? -33.766 36.212  -0.710  1.00 50.05 ? 339  LYS C NZ  1 
ATOM   11447 N  N   . LYS C  1 323 ? -29.493 32.158  -5.885  1.00 30.98 ? 340  LYS C N   1 
ATOM   11448 C  CA  . LYS C  1 323 ? -28.974 32.137  -7.243  1.00 30.60 ? 340  LYS C CA  1 
ATOM   11449 C  C   . LYS C  1 323 ? -28.638 30.715  -7.692  1.00 29.74 ? 340  LYS C C   1 
ATOM   11450 O  O   . LYS C  1 323 ? -28.164 30.532  -8.809  1.00 27.74 ? 340  LYS C O   1 
ATOM   11451 C  CB  . LYS C  1 323 ? -27.769 33.074  -7.358  1.00 32.71 ? 340  LYS C CB  1 
ATOM   11452 C  CG  . LYS C  1 323 ? -28.180 34.535  -7.217  1.00 35.55 ? 340  LYS C CG  1 
ATOM   11453 C  CD  . LYS C  1 323 ? -27.079 35.560  -7.442  1.00 38.16 ? 340  LYS C CD  1 
ATOM   11454 C  CE  . LYS C  1 323 ? -27.500 36.898  -6.912  1.00 40.31 ? 340  LYS C CE  1 
ATOM   11455 N  NZ  . LYS C  1 323 ? -28.705 37.426  -7.558  1.00 41.26 ? 340  LYS C NZ  1 
ATOM   11456 N  N   . ILE C  1 324 ? -28.908 29.715  -6.841  1.00 28.73 ? 341  ILE C N   1 
ATOM   11457 C  CA  . ILE C  1 324 ? -28.551 28.337  -7.139  1.00 27.96 ? 341  ILE C CA  1 
ATOM   11458 C  C   . ILE C  1 324 ? -29.818 27.486  -7.154  1.00 27.34 ? 341  ILE C C   1 
ATOM   11459 O  O   . ILE C  1 324 ? -30.563 27.457  -6.177  1.00 27.02 ? 341  ILE C O   1 
ATOM   11460 C  CB  . ILE C  1 324 ? -27.506 27.809  -6.139  1.00 27.79 ? 341  ILE C CB  1 
ATOM   11461 C  CG1 . ILE C  1 324 ? -26.187 28.577  -6.268  1.00 28.40 ? 341  ILE C CG1 1 
ATOM   11462 C  CG2 . ILE C  1 324 ? -27.304 26.302  -6.318  1.00 27.05 ? 341  ILE C CG2 1 
ATOM   11463 C  CD1 . ILE C  1 324 ? -25.184 28.299  -5.164  1.00 28.93 ? 341  ILE C CD1 1 
ATOM   11464 N  N   . TRP C  1 325 ? -30.051 26.808  -8.285  1.00 27.15 ? 342  TRP C N   1 
ATOM   11465 C  CA  . TRP C  1 325 ? -31.165 25.886  -8.425  1.00 28.04 ? 342  TRP C CA  1 
ATOM   11466 C  C   . TRP C  1 325 ? -30.616 24.483  -8.657  1.00 27.64 ? 342  TRP C C   1 
ATOM   11467 O  O   . TRP C  1 325 ? -29.489 24.324  -9.124  1.00 25.07 ? 342  TRP C O   1 
ATOM   11468 C  CB  . TRP C  1 325 ? -32.081 26.322  -9.579  1.00 30.04 ? 342  TRP C CB  1 
ATOM   11469 C  CG  . TRP C  1 325 ? -32.796 27.629  -9.354  1.00 31.75 ? 342  TRP C CG  1 
ATOM   11470 C  CD1 . TRP C  1 325 ? -32.280 28.884  -9.495  1.00 32.41 ? 342  TRP C CD1 1 
ATOM   11471 C  CD2 . TRP C  1 325 ? -34.177 27.807  -8.970  1.00 33.24 ? 342  TRP C CD2 1 
ATOM   11472 N  NE1 . TRP C  1 325 ? -33.235 29.826  -9.219  1.00 32.83 ? 342  TRP C NE1 1 
ATOM   11473 C  CE2 . TRP C  1 325 ? -34.407 29.198  -8.892  1.00 33.45 ? 342  TRP C CE2 1 
ATOM   11474 C  CE3 . TRP C  1 325 ? -35.231 26.933  -8.681  1.00 35.16 ? 342  TRP C CE3 1 
ATOM   11475 C  CZ2 . TRP C  1 325 ? -35.645 29.730  -8.542  1.00 34.19 ? 342  TRP C CZ2 1 
ATOM   11476 C  CZ3 . TRP C  1 325 ? -36.457 27.459  -8.338  1.00 35.70 ? 342  TRP C CZ3 1 
ATOM   11477 C  CH2 . TRP C  1 325 ? -36.659 28.838  -8.272  1.00 36.11 ? 342  TRP C CH2 1 
ATOM   11478 N  N   . MET C  1 326 ? -31.419 23.470  -8.319  1.00 28.80 ? 343  MET C N   1 
ATOM   11479 C  CA  . MET C  1 326 ? -31.029 22.090  -8.543  1.00 30.07 ? 343  MET C CA  1 
ATOM   11480 C  C   . MET C  1 326 ? -32.195 21.318  -9.154  1.00 31.17 ? 343  MET C C   1 
ATOM   11481 O  O   . MET C  1 326 ? -33.352 21.559  -8.810  1.00 31.29 ? 343  MET C O   1 
ATOM   11482 C  CB  . MET C  1 326 ? -30.590 21.424  -7.235  1.00 31.30 ? 343  MET C CB  1 
ATOM   11483 C  CG  . MET C  1 326 ? -29.446 22.137  -6.533  1.00 31.46 ? 343  MET C CG  1 
ATOM   11484 S  SD  . MET C  1 326 ? -28.827 21.218  -5.108  1.00 32.68 ? 343  MET C SD  1 
ATOM   11485 C  CE  . MET C  1 326 ? -27.446 22.293  -4.692  1.00 32.87 ? 343  MET C CE  1 
ATOM   11486 N  N   . PHE C  1 327 ? -31.851 20.391  -10.057 1.00 32.25 ? 344  PHE C N   1 
ATOM   11487 C  CA  . PHE C  1 327 ? -32.804 19.541  -10.754 1.00 33.65 ? 344  PHE C CA  1 
ATOM   11488 C  C   . PHE C  1 327 ? -32.300 18.101  -10.684 1.00 33.00 ? 344  PHE C C   1 
ATOM   11489 O  O   . PHE C  1 327 ? -31.307 17.765  -11.325 1.00 33.36 ? 344  PHE C O   1 
ATOM   11490 C  CB  . PHE C  1 327 ? -32.923 20.070  -12.188 1.00 34.62 ? 344  PHE C CB  1 
ATOM   11491 C  CG  . PHE C  1 327 ? -34.013 19.441  -13.047 1.00 36.61 ? 344  PHE C CG  1 
ATOM   11492 C  CD1 . PHE C  1 327 ? -33.821 18.203  -13.653 1.00 38.31 ? 344  PHE C CD1 1 
ATOM   11493 C  CD2 . PHE C  1 327 ? -35.212 20.108  -13.277 1.00 38.95 ? 344  PHE C CD2 1 
ATOM   11494 C  CE1 . PHE C  1 327 ? -34.813 17.639  -14.445 1.00 39.27 ? 344  PHE C CE1 1 
ATOM   11495 C  CE2 . PHE C  1 327 ? -36.199 19.540  -14.071 1.00 39.18 ? 344  PHE C CE2 1 
ATOM   11496 C  CZ  . PHE C  1 327 ? -35.997 18.308  -14.651 1.00 38.92 ? 344  PHE C CZ  1 
ATOM   11497 N  N   . ASP C  1 328 ? -32.977 17.257  -9.894  1.00 34.21 ? 345  ASP C N   1 
ATOM   11498 C  CA  . ASP C  1 328 ? -32.539 15.882  -9.698  1.00 35.23 ? 345  ASP C CA  1 
ATOM   11499 C  C   . ASP C  1 328 ? -33.408 14.936  -10.533 1.00 37.45 ? 345  ASP C C   1 
ATOM   11500 O  O   . ASP C  1 328 ? -34.146 15.379  -11.413 1.00 36.24 ? 345  ASP C O   1 
ATOM   11501 C  CB  . ASP C  1 328 ? -32.480 15.541  -8.217  1.00 35.17 ? 345  ASP C CB  1 
ATOM   11502 C  CG  . ASP C  1 328 ? -33.820 15.353  -7.519  1.00 36.38 ? 345  ASP C CG  1 
ATOM   11503 O  OD1 . ASP C  1 328 ? -34.868 15.599  -8.163  1.00 36.16 ? 345  ASP C OD1 1 
ATOM   11504 O  OD2 . ASP C  1 328 ? -33.803 14.963  -6.330  1.00 37.05 ? 345  ASP C OD2 1 
ATOM   11505 N  N   . LYS C  1 329 ? -33.306 13.628  -10.240 1.00 37.18 ? 346  LYS C N   1 
ATOM   11506 C  CA  . LYS C  1 329 ? -34.007 12.582  -10.970 1.00 38.50 ? 346  LYS C CA  1 
ATOM   11507 C  C   . LYS C  1 329 ? -35.523 12.791  -10.933 1.00 39.38 ? 346  LYS C C   1 
ATOM   11508 O  O   . LYS C  1 329 ? -36.223 12.310  -11.821 1.00 40.62 ? 346  LYS C O   1 
ATOM   11509 C  CB  . LYS C  1 329 ? -33.643 11.201  -10.406 1.00 38.46 ? 346  LYS C CB  1 
ATOM   11510 N  N   . TYR C  1 330 ? -36.023 13.511  -9.921  1.00 40.29 ? 347  TYR C N   1 
ATOM   11511 C  CA  . TYR C  1 330 ? -37.452 13.731  -9.747  1.00 42.46 ? 347  TYR C CA  1 
ATOM   11512 C  C   . TYR C  1 330 ? -37.888 15.090  -10.301 1.00 41.27 ? 347  TYR C C   1 
ATOM   11513 O  O   . TYR C  1 330 ? -39.082 15.374  -10.338 1.00 41.17 ? 347  TYR C O   1 
ATOM   11514 C  CB  . TYR C  1 330 ? -37.777 13.599  -8.256  1.00 47.90 ? 347  TYR C CB  1 
ATOM   11515 C  CG  . TYR C  1 330 ? -37.402 12.247  -7.664  1.00 54.48 ? 347  TYR C CG  1 
ATOM   11516 C  CD1 . TYR C  1 330 ? -36.094 11.967  -7.284  1.00 57.94 ? 347  TYR C CD1 1 
ATOM   11517 C  CD2 . TYR C  1 330 ? -38.353 11.247  -7.494  1.00 59.39 ? 347  TYR C CD2 1 
ATOM   11518 C  CE1 . TYR C  1 330 ? -35.744 10.736  -6.753  1.00 61.98 ? 347  TYR C CE1 1 
ATOM   11519 C  CE2 . TYR C  1 330 ? -38.017 10.013  -6.961  1.00 61.41 ? 347  TYR C CE2 1 
ATOM   11520 C  CZ  . TYR C  1 330 ? -36.708 9.756   -6.589  1.00 63.68 ? 347  TYR C CZ  1 
ATOM   11521 O  OH  . TYR C  1 330 ? -36.368 8.542   -6.062  1.00 66.28 ? 347  TYR C OH  1 
ATOM   11522 N  N   . GLY C  1 331 ? -36.931 15.929  -10.723 1.00 39.02 ? 348  GLY C N   1 
ATOM   11523 C  CA  . GLY C  1 331 ? -37.243 17.229  -11.301 1.00 38.01 ? 348  GLY C CA  1 
ATOM   11524 C  C   . GLY C  1 331 ? -36.653 18.374  -10.481 1.00 38.55 ? 348  GLY C C   1 
ATOM   11525 O  O   . GLY C  1 331 ? -35.704 18.179  -9.723  1.00 37.82 ? 348  GLY C O   1 
ATOM   11526 N  N   . LEU C  1 332 ? -37.232 19.570  -10.646 1.00 39.06 ? 349  LEU C N   1 
ATOM   11527 C  CA  . LEU C  1 332 ? -36.716 20.780  -10.026 1.00 39.17 ? 349  LEU C CA  1 
ATOM   11528 C  C   . LEU C  1 332 ? -37.016 20.749  -8.528  1.00 40.56 ? 349  LEU C C   1 
ATOM   11529 O  O   . LEU C  1 332 ? -38.146 20.475  -8.125  1.00 41.34 ? 349  LEU C O   1 
ATOM   11530 C  CB  . LEU C  1 332 ? -37.331 22.008  -10.695 1.00 36.21 ? 349  LEU C CB  1 
ATOM   11531 C  CG  . LEU C  1 332 ? -36.697 23.359  -10.344 1.00 36.14 ? 349  LEU C CG  1 
ATOM   11532 C  CD1 . LEU C  1 332 ? -35.287 23.490  -10.910 1.00 33.79 ? 349  LEU C CD1 1 
ATOM   11533 C  CD2 . LEU C  1 332 ? -37.571 24.500  -10.836 1.00 36.39 ? 349  LEU C CD2 1 
ATOM   11534 N  N   . LEU C  1 333 ? -35.992 21.032  -7.713  1.00 39.86 ? 350  LEU C N   1 
ATOM   11535 C  CA  . LEU C  1 333 ? -36.162 21.113  -6.270  1.00 39.82 ? 350  LEU C CA  1 
ATOM   11536 C  C   . LEU C  1 333 ? -36.883 22.415  -5.933  1.00 39.90 ? 350  LEU C C   1 
ATOM   11537 O  O   . LEU C  1 333 ? -36.268 23.478  -5.912  1.00 39.69 ? 350  LEU C O   1 
ATOM   11538 C  CB  . LEU C  1 333 ? -34.821 21.000  -5.543  1.00 38.17 ? 350  LEU C CB  1 
ATOM   11539 C  CG  . LEU C  1 333 ? -34.278 19.582  -5.338  1.00 38.01 ? 350  LEU C CG  1 
ATOM   11540 C  CD1 . LEU C  1 333 ? -33.806 18.932  -6.633  1.00 38.13 ? 350  LEU C CD1 1 
ATOM   11541 C  CD2 . LEU C  1 333 ? -33.158 19.591  -4.303  1.00 37.27 ? 350  LEU C CD2 1 
ATOM   11542 N  N   . VAL C  1 334 ? -38.197 22.310  -5.686  1.00 41.88 ? 351  VAL C N   1 
ATOM   11543 C  CA  . VAL C  1 334 ? -39.021 23.445  -5.305  1.00 44.74 ? 351  VAL C CA  1 
ATOM   11544 C  C   . VAL C  1 334 ? -39.770 23.096  -4.021  1.00 46.50 ? 351  VAL C C   1 
ATOM   11545 O  O   . VAL C  1 334 ? -39.958 21.922  -3.708  1.00 45.10 ? 351  VAL C O   1 
ATOM   11546 C  CB  . VAL C  1 334 ? -40.003 23.859  -6.420  1.00 47.54 ? 351  VAL C CB  1 
ATOM   11547 C  CG1 . VAL C  1 334 ? -39.271 24.352  -7.664  1.00 47.45 ? 351  VAL C CG1 1 
ATOM   11548 C  CG2 . VAL C  1 334 ? -40.976 22.739  -6.780  1.00 47.85 ? 351  VAL C CG2 1 
ATOM   11549 N  N   . LYS C  1 335 ? -40.198 24.133  -3.292  1.00 48.90 ? 352  LYS C N   1 
ATOM   11550 C  CA  . LYS C  1 335 ? -40.911 23.958  -2.036  1.00 54.72 ? 352  LYS C CA  1 
ATOM   11551 C  C   . LYS C  1 335 ? -42.264 23.303  -2.307  1.00 56.01 ? 352  LYS C C   1 
ATOM   11552 O  O   . LYS C  1 335 ? -43.046 23.804  -3.110  1.00 56.00 ? 352  LYS C O   1 
ATOM   11553 C  CB  . LYS C  1 335 ? -41.097 25.300  -1.316  1.00 56.42 ? 352  LYS C CB  1 
ATOM   11554 C  CG  . LYS C  1 335 ? -39.822 25.911  -0.745  1.00 59.75 ? 352  LYS C CG  1 
ATOM   11555 C  CD  . LYS C  1 335 ? -40.007 27.291  -0.120  1.00 61.75 ? 352  LYS C CD  1 
ATOM   11556 C  CE  . LYS C  1 335 ? -38.730 27.865  0.411   1.00 62.91 ? 352  LYS C CE  1 
ATOM   11557 N  NZ  . LYS C  1 335 ? -38.888 29.265  0.818   1.00 63.48 ? 352  LYS C NZ  1 
ATOM   11558 N  N   . GLY C  1 336 ? -42.508 22.164  -1.645  1.00 58.17 ? 353  GLY C N   1 
ATOM   11559 C  CA  . GLY C  1 336 ? -43.802 21.500  -1.678  1.00 59.41 ? 353  GLY C CA  1 
ATOM   11560 C  C   . GLY C  1 336 ? -43.913 20.460  -2.793  1.00 59.45 ? 353  GLY C C   1 
ATOM   11561 O  O   . GLY C  1 336 ? -45.018 20.039  -3.126  1.00 61.79 ? 353  GLY C O   1 
ATOM   11562 N  N   . ARG C  1 337 ? -42.775 20.035  -3.359  1.00 58.28 ? 354  ARG C N   1 
ATOM   11563 C  CA  . ARG C  1 337 ? -42.777 18.986  -4.368  1.00 57.73 ? 354  ARG C CA  1 
ATOM   11564 C  C   . ARG C  1 337 ? -43.014 17.639  -3.683  1.00 59.70 ? 354  ARG C C   1 
ATOM   11565 O  O   . ARG C  1 337 ? -42.862 17.521  -2.468  1.00 60.02 ? 354  ARG C O   1 
ATOM   11566 C  CB  . ARG C  1 337 ? -41.483 18.985  -5.195  1.00 53.62 ? 354  ARG C CB  1 
ATOM   11567 C  CG  . ARG C  1 337 ? -40.236 18.451  -4.504  1.00 51.22 ? 354  ARG C CG  1 
ATOM   11568 C  CD  . ARG C  1 337 ? -39.116 18.167  -5.493  1.00 48.77 ? 354  ARG C CD  1 
ATOM   11569 N  NE  . ARG C  1 337 ? -38.072 17.322  -4.904  1.00 46.25 ? 354  ARG C NE  1 
ATOM   11570 C  CZ  . ARG C  1 337 ? -37.060 16.768  -5.566  1.00 45.92 ? 354  ARG C CZ  1 
ATOM   11571 N  NH1 . ARG C  1 337 ? -36.906 16.977  -6.863  1.00 45.55 ? 354  ARG C NH1 1 
ATOM   11572 N  NH2 . ARG C  1 337 ? -36.201 15.996  -4.921  1.00 46.63 ? 354  ARG C NH2 1 
ATOM   11573 N  N   . LYS C  1 338 ? -43.379 16.624  -4.476  1.00 61.04 ? 355  LYS C N   1 
ATOM   11574 C  CA  . LYS C  1 338 ? -43.681 15.304  -3.944  1.00 62.61 ? 355  LYS C CA  1 
ATOM   11575 C  C   . LYS C  1 338 ? -42.402 14.624  -3.455  1.00 59.46 ? 355  LYS C C   1 
ATOM   11576 O  O   . LYS C  1 338 ? -42.383 14.065  -2.362  1.00 59.81 ? 355  LYS C O   1 
ATOM   11577 C  CB  . LYS C  1 338 ? -44.403 14.416  -4.965  1.00 66.01 ? 355  LYS C CB  1 
ATOM   11578 C  CG  . LYS C  1 338 ? -45.800 14.877  -5.370  1.00 68.15 ? 355  LYS C CG  1 
ATOM   11579 C  CD  . LYS C  1 338 ? -46.770 13.750  -5.717  1.00 70.85 ? 355  LYS C CD  1 
ATOM   11580 C  CE  . LYS C  1 338 ? -46.265 12.753  -6.721  1.00 72.41 ? 355  LYS C CE  1 
ATOM   11581 N  NZ  . LYS C  1 338 ? -45.994 13.345  -8.034  1.00 73.04 ? 355  LYS C NZ  1 
ATOM   11582 N  N   . ALA C  1 339 ? -41.335 14.688  -4.262  1.00 57.01 ? 356  ALA C N   1 
ATOM   11583 C  CA  . ALA C  1 339 ? -40.099 13.975  -3.972  1.00 55.61 ? 356  ALA C CA  1 
ATOM   11584 C  C   . ALA C  1 339 ? -39.403 14.566  -2.744  1.00 53.00 ? 356  ALA C C   1 
ATOM   11585 O  O   . ALA C  1 339 ? -39.670 15.702  -2.356  1.00 51.55 ? 356  ALA C O   1 
ATOM   11586 C  CB  . ALA C  1 339 ? -39.203 13.993  -5.192  1.00 56.47 ? 356  ALA C CB  1 
ATOM   11587 N  N   . LYS C  1 340 ? -38.494 13.776  -2.154  1.00 52.30 ? 357  LYS C N   1 
ATOM   11588 C  CA  . LYS C  1 340 ? -37.908 14.072  -0.853  1.00 52.22 ? 357  LYS C CA  1 
ATOM   11589 C  C   . LYS C  1 340 ? -36.852 15.172  -0.969  1.00 52.01 ? 357  LYS C C   1 
ATOM   11590 O  O   . LYS C  1 340 ? -36.101 15.223  -1.942  1.00 52.01 ? 357  LYS C O   1 
ATOM   11591 C  CB  . LYS C  1 340 ? -37.301 12.805  -0.235  1.00 49.61 ? 357  LYS C CB  1 
ATOM   11592 N  N   . ILE C  1 341 ? -36.816 16.040  0.054   1.00 50.74 ? 358  ILE C N   1 
ATOM   11593 C  CA  . ILE C  1 341 ? -35.860 17.131  0.179   1.00 48.90 ? 358  ILE C CA  1 
ATOM   11594 C  C   . ILE C  1 341 ? -35.170 16.995  1.534   1.00 47.74 ? 358  ILE C C   1 
ATOM   11595 O  O   . ILE C  1 341 ? -35.800 17.226  2.562   1.00 50.83 ? 358  ILE C O   1 
ATOM   11596 C  CB  . ILE C  1 341 ? -36.571 18.495  0.067   1.00 47.92 ? 358  ILE C CB  1 
ATOM   11597 C  CG1 . ILE C  1 341 ? -37.271 18.683  -1.282  1.00 48.44 ? 358  ILE C CG1 1 
ATOM   11598 C  CG2 . ILE C  1 341 ? -35.609 19.647  0.362   1.00 48.56 ? 358  ILE C CG2 1 
ATOM   11599 C  CD1 . ILE C  1 341 ? -36.331 18.862  -2.462  1.00 48.00 ? 358  ILE C CD1 1 
ATOM   11600 N  N   . ASP C  1 342 ? -33.883 16.632  1.543   1.00 46.90 ? 359  ASP C N   1 
ATOM   11601 C  CA  . ASP C  1 342 ? -33.155 16.485  2.795   1.00 46.09 ? 359  ASP C CA  1 
ATOM   11602 C  C   . ASP C  1 342 ? -32.745 17.867  3.305   1.00 47.53 ? 359  ASP C C   1 
ATOM   11603 O  O   . ASP C  1 342 ? -33.007 18.878  2.656   1.00 49.89 ? 359  ASP C O   1 
ATOM   11604 C  CB  . ASP C  1 342 ? -32.008 15.494  2.669   1.00 46.89 ? 359  ASP C CB  1 
ATOM   11605 C  CG  . ASP C  1 342 ? -30.812 15.949  1.845   1.00 46.99 ? 359  ASP C CG  1 
ATOM   11606 O  OD1 . ASP C  1 342 ? -30.447 17.139  1.946   1.00 43.50 ? 359  ASP C OD1 1 
ATOM   11607 O  OD2 . ASP C  1 342 ? -30.230 15.097  1.141   1.00 49.84 ? 359  ASP C OD2 1 
ATOM   11608 N  N   . SER C  1 343 ? -32.102 17.900  4.479   1.00 47.38 ? 360  SER C N   1 
ATOM   11609 C  CA  . SER C  1 343 ? -31.788 19.149  5.154   1.00 45.03 ? 360  SER C CA  1 
ATOM   11610 C  C   . SER C  1 343 ? -30.658 19.886  4.432   1.00 43.43 ? 360  SER C C   1 
ATOM   11611 O  O   . SER C  1 343 ? -30.628 21.113  4.434   1.00 44.35 ? 360  SER C O   1 
ATOM   11612 C  CB  . SER C  1 343 ? -31.462 18.916  6.618   1.00 44.05 ? 360  SER C CB  1 
ATOM   11613 O  OG  . SER C  1 343 ? -30.304 18.105  6.773   1.00 42.26 ? 360  SER C OG  1 
ATOM   11614 N  N   . TYR C  1 344 ? -29.734 19.136  3.819   1.00 42.20 ? 361  TYR C N   1 
ATOM   11615 C  CA  . TYR C  1 344 ? -28.646 19.725  3.052   1.00 41.52 ? 361  TYR C CA  1 
ATOM   11616 C  C   . TYR C  1 344 ? -29.192 20.412  1.796   1.00 39.70 ? 361  TYR C C   1 
ATOM   11617 O  O   . TYR C  1 344 ? -28.641 21.419  1.359   1.00 36.19 ? 361  TYR C O   1 
ATOM   11618 C  CB  . TYR C  1 344 ? -27.591 18.676  2.678   1.00 42.34 ? 361  TYR C CB  1 
ATOM   11619 C  CG  . TYR C  1 344 ? -26.620 18.288  3.787   1.00 44.19 ? 361  TYR C CG  1 
ATOM   11620 C  CD1 . TYR C  1 344 ? -26.891 17.231  4.653   1.00 44.97 ? 361  TYR C CD1 1 
ATOM   11621 C  CD2 . TYR C  1 344 ? -25.422 18.972  3.958   1.00 43.49 ? 361  TYR C CD2 1 
ATOM   11622 C  CE1 . TYR C  1 344 ? -26.003 16.874  5.658   1.00 44.60 ? 361  TYR C CE1 1 
ATOM   11623 C  CE2 . TYR C  1 344 ? -24.527 18.626  4.960   1.00 44.40 ? 361  TYR C CE2 1 
ATOM   11624 C  CZ  . TYR C  1 344 ? -24.820 17.577  5.814   1.00 43.11 ? 361  TYR C CZ  1 
ATOM   11625 O  OH  . TYR C  1 344 ? -23.933 17.241  6.795   1.00 41.13 ? 361  TYR C OH  1 
ATOM   11626 N  N   . GLN C  1 345 ? -30.268 19.857  1.218   1.00 39.23 ? 362  GLN C N   1 
ATOM   11627 C  CA  . GLN C  1 345 ? -30.833 20.355  -0.030  1.00 39.76 ? 362  GLN C CA  1 
ATOM   11628 C  C   . GLN C  1 345 ? -31.777 21.532  0.219   1.00 40.01 ? 362  GLN C C   1 
ATOM   11629 O  O   . GLN C  1 345 ? -32.094 22.272  -0.711  1.00 38.50 ? 362  GLN C O   1 
ATOM   11630 C  CB  . GLN C  1 345 ? -31.605 19.253  -0.757  1.00 37.61 ? 362  GLN C CB  1 
ATOM   11631 C  CG  . GLN C  1 345 ? -30.752 18.067  -1.197  1.00 37.52 ? 362  GLN C CG  1 
ATOM   11632 C  CD  . GLN C  1 345 ? -31.573 16.911  -1.730  1.00 37.49 ? 362  GLN C CD  1 
ATOM   11633 O  OE1 . GLN C  1 345 ? -32.621 16.558  -1.178  1.00 36.19 ? 362  GLN C OE1 1 
ATOM   11634 N  NE2 . GLN C  1 345 ? -31.112 16.311  -2.819  1.00 37.12 ? 362  GLN C NE2 1 
ATOM   11635 N  N   . GLU C  1 346 ? -32.212 21.701  1.474   1.00 42.10 ? 363  GLU C N   1 
ATOM   11636 C  CA  . GLU C  1 346 ? -33.282 22.627  1.824   1.00 44.71 ? 363  GLU C CA  1 
ATOM   11637 C  C   . GLU C  1 346 ? -32.933 24.071  1.453   1.00 40.46 ? 363  GLU C C   1 
ATOM   11638 O  O   . GLU C  1 346 ? -33.795 24.806  0.977   1.00 38.00 ? 363  GLU C O   1 
ATOM   11639 C  CB  . GLU C  1 346 ? -33.590 22.471  3.316   1.00 49.59 ? 363  GLU C CB  1 
ATOM   11640 C  CG  . GLU C  1 346 ? -34.768 23.308  3.807   1.00 54.13 ? 363  GLU C CG  1 
ATOM   11641 C  CD  . GLU C  1 346 ? -35.044 23.169  5.297   1.00 60.56 ? 363  GLU C CD  1 
ATOM   11642 O  OE1 . GLU C  1 346 ? -34.299 22.436  5.989   1.00 64.19 ? 363  GLU C OE1 1 
ATOM   11643 O  OE2 . GLU C  1 346 ? -36.011 23.803  5.773   1.00 65.48 ? 363  GLU C OE2 1 
ATOM   11644 N  N   . PRO C  1 347 ? -31.687 24.557  1.674   1.00 38.27 ? 364  PRO C N   1 
ATOM   11645 C  CA  . PRO C  1 347 ? -31.339 25.938  1.326   1.00 36.67 ? 364  PRO C CA  1 
ATOM   11646 C  C   . PRO C  1 347 ? -31.375 26.279  -0.166  1.00 35.32 ? 364  PRO C C   1 
ATOM   11647 O  O   . PRO C  1 347 ? -31.422 27.454  -0.522  1.00 33.41 ? 364  PRO C O   1 
ATOM   11648 C  CB  . PRO C  1 347 ? -29.921 26.108  1.905   1.00 37.56 ? 364  PRO C CB  1 
ATOM   11649 C  CG  . PRO C  1 347 ? -29.758 24.968  2.889   1.00 38.22 ? 364  PRO C CG  1 
ATOM   11650 C  CD  . PRO C  1 347 ? -30.568 23.834  2.298   1.00 38.64 ? 364  PRO C CD  1 
ATOM   11651 N  N   . PHE C  1 348 ? -31.336 25.257  -1.033  1.00 33.91 ? 365  PHE C N   1 
ATOM   11652 C  CA  . PHE C  1 348 ? -31.373 25.466  -2.473  1.00 34.56 ? 365  PHE C CA  1 
ATOM   11653 C  C   . PHE C  1 348 ? -32.733 25.070  -3.043  1.00 36.22 ? 365  PHE C C   1 
ATOM   11654 O  O   . PHE C  1 348 ? -32.889 24.997  -4.262  1.00 36.72 ? 365  PHE C O   1 
ATOM   11655 C  CB  . PHE C  1 348 ? -30.231 24.679  -3.119  1.00 33.56 ? 365  PHE C CB  1 
ATOM   11656 C  CG  . PHE C  1 348 ? -28.884 24.967  -2.472  1.00 32.81 ? 365  PHE C CG  1 
ATOM   11657 C  CD1 . PHE C  1 348 ? -28.229 26.174  -2.699  1.00 31.68 ? 365  PHE C CD1 1 
ATOM   11658 C  CD2 . PHE C  1 348 ? -28.284 24.036  -1.631  1.00 32.50 ? 365  PHE C CD2 1 
ATOM   11659 C  CE1 . PHE C  1 348 ? -27.009 26.440  -2.100  1.00 31.72 ? 365  PHE C CE1 1 
ATOM   11660 C  CE2 . PHE C  1 348 ? -27.061 24.308  -1.037  1.00 32.83 ? 365  PHE C CE2 1 
ATOM   11661 C  CZ  . PHE C  1 348 ? -26.425 25.509  -1.275  1.00 31.37 ? 365  PHE C CZ  1 
ATOM   11662 N  N   . THR C  1 349 ? -33.701 24.811  -2.155  1.00 36.75 ? 366  THR C N   1 
ATOM   11663 C  CA  . THR C  1 349 ? -35.057 24.477  -2.553  1.00 38.21 ? 366  THR C CA  1 
ATOM   11664 C  C   . THR C  1 349 ? -35.900 25.741  -2.417  1.00 39.57 ? 366  THR C C   1 
ATOM   11665 O  O   . THR C  1 349 ? -36.183 26.188  -1.305  1.00 41.64 ? 366  THR C O   1 
ATOM   11666 C  CB  . THR C  1 349 ? -35.576 23.325  -1.694  1.00 37.98 ? 366  THR C CB  1 
ATOM   11667 O  OG1 . THR C  1 349 ? -34.661 22.250  -1.889  1.00 39.21 ? 366  THR C OG1 1 
ATOM   11668 C  CG2 . THR C  1 349 ? -36.965 22.866  -2.097  1.00 38.85 ? 366  THR C CG2 1 
ATOM   11669 N  N   . HIS C  1 350 ? -36.275 26.308  -3.569  1.00 39.46 ? 367  HIS C N   1 
ATOM   11670 C  CA  . HIS C  1 350 ? -36.882 27.626  -3.640  1.00 40.90 ? 367  HIS C CA  1 
ATOM   11671 C  C   . HIS C  1 350 ? -38.361 27.500  -3.994  1.00 42.73 ? 367  HIS C C   1 
ATOM   11672 O  O   . HIS C  1 350 ? -38.816 26.443  -4.428  1.00 38.36 ? 367  HIS C O   1 
ATOM   11673 C  CB  . HIS C  1 350 ? -36.145 28.475  -4.680  1.00 40.82 ? 367  HIS C CB  1 
ATOM   11674 C  CG  . HIS C  1 350 ? -34.673 28.540  -4.440  1.00 41.68 ? 367  HIS C CG  1 
ATOM   11675 N  ND1 . HIS C  1 350 ? -34.138 28.870  -3.213  1.00 41.40 ? 367  HIS C ND1 1 
ATOM   11676 C  CD2 . HIS C  1 350 ? -33.630 28.331  -5.257  1.00 41.54 ? 367  HIS C CD2 1 
ATOM   11677 C  CE1 . HIS C  1 350 ? -32.814 28.846  -3.294  1.00 41.36 ? 367  HIS C CE1 1 
ATOM   11678 N  NE2 . HIS C  1 350 ? -32.485 28.525  -4.527  1.00 40.79 ? 367  HIS C NE2 1 
ATOM   11679 N  N   . SER C  1 351 ? -39.095 28.603  -3.811  1.00 45.12 ? 368  SER C N   1 
ATOM   11680 C  CA  . SER C  1 351 ? -40.483 28.690  -4.236  1.00 48.46 ? 368  SER C CA  1 
ATOM   11681 C  C   . SER C  1 351 ? -40.561 28.474  -5.744  1.00 50.95 ? 368  SER C C   1 
ATOM   11682 O  O   . SER C  1 351 ? -39.749 29.019  -6.490  1.00 51.10 ? 368  SER C O   1 
ATOM   11683 C  CB  . SER C  1 351 ? -41.097 30.012  -3.843  1.00 47.41 ? 368  SER C CB  1 
ATOM   11684 O  OG  . SER C  1 351 ? -41.126 30.156  -2.430  1.00 48.29 ? 368  SER C OG  1 
ATOM   11685 N  N   . ALA C  1 352 ? -41.536 27.666  -6.177  1.00 52.04 ? 369  ALA C N   1 
ATOM   11686 C  CA  . ALA C  1 352 ? -41.679 27.325  -7.582  1.00 53.09 ? 369  ALA C CA  1 
ATOM   11687 C  C   . ALA C  1 352 ? -41.875 28.594  -8.409  1.00 54.16 ? 369  ALA C C   1 
ATOM   11688 O  O   . ALA C  1 352 ? -42.574 29.513  -7.984  1.00 54.59 ? 369  ALA C O   1 
ATOM   11689 C  CB  . ALA C  1 352 ? -42.835 26.363  -7.771  1.00 52.19 ? 369  ALA C CB  1 
ATOM   11690 N  N   . PRO C  1 353 ? -41.254 28.692  -9.607  1.00 55.90 ? 370  PRO C N   1 
ATOM   11691 C  CA  . PRO C  1 353 ? -41.573 29.769  -10.543 1.00 57.45 ? 370  PRO C CA  1 
ATOM   11692 C  C   . PRO C  1 353 ? -42.950 29.508  -11.150 1.00 60.43 ? 370  PRO C C   1 
ATOM   11693 O  O   . PRO C  1 353 ? -43.491 28.411  -11.010 1.00 58.99 ? 370  PRO C O   1 
ATOM   11694 C  CB  . PRO C  1 353 ? -40.432 29.721  -11.572 1.00 56.96 ? 370  PRO C CB  1 
ATOM   11695 C  CG  . PRO C  1 353 ? -39.928 28.290  -11.520 1.00 56.11 ? 370  PRO C CG  1 
ATOM   11696 C  CD  . PRO C  1 353 ? -40.224 27.774  -10.120 1.00 55.77 ? 370  PRO C CD  1 
ATOM   11697 N  N   . GLU C  1 354 ? -43.498 30.523  -11.830 1.00 64.24 ? 371  GLU C N   1 
ATOM   11698 C  CA  . GLU C  1 354 ? -44.867 30.494  -12.325 1.00 67.56 ? 371  GLU C CA  1 
ATOM   11699 C  C   . GLU C  1 354 ? -45.118 29.201  -13.099 1.00 66.25 ? 371  GLU C C   1 
ATOM   11700 O  O   . GLU C  1 354 ? -46.115 28.522  -12.861 1.00 67.00 ? 371  GLU C O   1 
ATOM   11701 C  CB  . GLU C  1 354 ? -45.146 31.735  -13.175 1.00 71.26 ? 371  GLU C CB  1 
ATOM   11702 C  CG  . GLU C  1 354 ? -46.634 32.019  -13.366 1.00 75.47 ? 371  GLU C CG  1 
ATOM   11703 C  CD  . GLU C  1 354 ? -46.924 33.284  -14.155 1.00 77.36 ? 371  GLU C CD  1 
ATOM   11704 O  OE1 . GLU C  1 354 ? -46.602 33.308  -15.363 1.00 76.85 ? 371  GLU C OE1 1 
ATOM   11705 O  OE2 . GLU C  1 354 ? -47.460 34.246  -13.562 1.00 78.19 ? 371  GLU C OE2 1 
ATOM   11706 N  N   . SER C  1 355 ? -44.203 28.874  -14.021 1.00 65.61 ? 372  SER C N   1 
ATOM   11707 C  CA  . SER C  1 355 ? -44.222 27.610  -14.743 1.00 66.31 ? 372  SER C CA  1 
ATOM   11708 C  C   . SER C  1 355 ? -43.206 26.649  -14.125 1.00 66.08 ? 372  SER C C   1 
ATOM   11709 O  O   . SER C  1 355 ? -42.072 27.042  -13.862 1.00 68.74 ? 372  SER C O   1 
ATOM   11710 C  CB  . SER C  1 355 ? -43.941 27.835  -16.209 1.00 68.02 ? 372  SER C CB  1 
ATOM   11711 O  OG  . SER C  1 355 ? -43.774 26.603  -16.897 1.00 69.35 ? 372  SER C OG  1 
ATOM   11712 N  N   . ILE C  1 356 ? -43.615 25.391  -13.903 1.00 63.90 ? 373  ILE C N   1 
ATOM   11713 C  CA  . ILE C  1 356 ? -42.744 24.387  -13.309 1.00 62.38 ? 373  ILE C CA  1 
ATOM   11714 C  C   . ILE C  1 356 ? -42.202 23.482  -14.416 1.00 60.45 ? 373  ILE C C   1 
ATOM   11715 O  O   . ILE C  1 356 ? -42.973 22.827  -15.112 1.00 60.64 ? 373  ILE C O   1 
ATOM   11716 C  CB  . ILE C  1 356 ? -43.478 23.589  -12.213 1.00 64.24 ? 373  ILE C CB  1 
ATOM   11717 C  CG1 . ILE C  1 356 ? -43.979 24.516  -11.096 1.00 65.35 ? 373  ILE C CG1 1 
ATOM   11718 C  CG2 . ILE C  1 356 ? -42.593 22.466  -11.665 1.00 63.28 ? 373  ILE C CG2 1 
ATOM   11719 C  CD1 . ILE C  1 356 ? -44.744 23.817  -9.984  1.00 66.19 ? 373  ILE C CD1 1 
ATOM   11720 N  N   . PRO C  1 357 ? -40.862 23.406  -14.609 1.00 57.99 ? 374  PRO C N   1 
ATOM   11721 C  CA  . PRO C  1 357 ? -40.280 22.592  -15.678 1.00 55.29 ? 374  PRO C CA  1 
ATOM   11722 C  C   . PRO C  1 357 ? -40.553 21.100  -15.512 1.00 54.26 ? 374  PRO C C   1 
ATOM   11723 O  O   . PRO C  1 357 ? -40.654 20.609  -14.391 1.00 57.19 ? 374  PRO C O   1 
ATOM   11724 C  CB  . PRO C  1 357 ? -38.766 22.885  -15.612 1.00 57.14 ? 374  PRO C CB  1 
ATOM   11725 C  CG  . PRO C  1 357 ? -38.635 24.116  -14.738 1.00 58.04 ? 374  PRO C CG  1 
ATOM   11726 C  CD  . PRO C  1 357 ? -39.838 24.106  -13.816 1.00 58.65 ? 374  PRO C CD  1 
ATOM   11727 N  N   . ASP C  1 358 ? -40.657 20.393  -16.643 1.00 53.17 ? 375  ASP C N   1 
ATOM   11728 C  CA  . ASP C  1 358 ? -40.734 18.941  -16.656 1.00 52.96 ? 375  ASP C CA  1 
ATOM   11729 C  C   . ASP C  1 358 ? -39.345 18.364  -16.916 1.00 48.22 ? 375  ASP C C   1 
ATOM   11730 O  O   . ASP C  1 358 ? -38.937 17.420  -16.246 1.00 48.65 ? 375  ASP C O   1 
ATOM   11731 C  CB  . ASP C  1 358 ? -41.732 18.432  -17.687 1.00 56.45 ? 375  ASP C CB  1 
ATOM   11732 C  CG  . ASP C  1 358 ? -43.194 18.450  -17.261 1.00 61.24 ? 375  ASP C CG  1 
ATOM   11733 O  OD1 . ASP C  1 358 ? -43.532 17.723  -16.299 1.00 63.63 ? 375  ASP C OD1 1 
ATOM   11734 O  OD2 . ASP C  1 358 ? -43.984 19.181  -17.900 1.00 63.24 ? 375  ASP C OD2 1 
ATOM   11735 N  N   . THR C  1 359 ? -38.643 18.936  -17.903 1.00 43.62 ? 376  THR C N   1 
ATOM   11736 C  CA  . THR C  1 359 ? -37.348 18.444  -18.344 1.00 41.78 ? 376  THR C CA  1 
ATOM   11737 C  C   . THR C  1 359 ? -36.272 19.464  -17.971 1.00 37.89 ? 376  THR C C   1 
ATOM   11738 O  O   . THR C  1 359 ? -36.579 20.610  -17.650 1.00 35.71 ? 376  THR C O   1 
ATOM   11739 C  CB  . THR C  1 359 ? -37.379 18.202  -19.854 1.00 43.51 ? 376  THR C CB  1 
ATOM   11740 O  OG1 . THR C  1 359 ? -37.459 19.491  -20.452 1.00 42.63 ? 376  THR C OG1 1 
ATOM   11741 C  CG2 . THR C  1 359 ? -38.563 17.363  -20.305 1.00 44.31 ? 376  THR C CG2 1 
ATOM   11742 N  N   . PHE C  1 360 ? -35.005 19.041  -18.053 1.00 36.00 ? 377  PHE C N   1 
ATOM   11743 C  CA  . PHE C  1 360 ? -33.887 19.927  -17.774 1.00 35.50 ? 377  PHE C CA  1 
ATOM   11744 C  C   . PHE C  1 360 ? -33.872 21.063  -18.798 1.00 35.18 ? 377  PHE C C   1 
ATOM   11745 O  O   . PHE C  1 360 ? -33.568 22.200  -18.455 1.00 34.71 ? 377  PHE C O   1 
ATOM   11746 C  CB  . PHE C  1 360 ? -32.561 19.160  -17.747 1.00 34.97 ? 377  PHE C CB  1 
ATOM   11747 C  CG  . PHE C  1 360 ? -31.397 19.981  -17.206 1.00 33.54 ? 377  PHE C CG  1 
ATOM   11748 C  CD1 . PHE C  1 360 ? -31.287 20.242  -15.843 1.00 33.43 ? 377  PHE C CD1 1 
ATOM   11749 C  CD2 . PHE C  1 360 ? -30.417 20.485  -18.056 1.00 33.36 ? 377  PHE C CD2 1 
ATOM   11750 C  CE1 . PHE C  1 360 ? -30.234 20.992  -15.348 1.00 32.10 ? 377  PHE C CE1 1 
ATOM   11751 C  CE2 . PHE C  1 360 ? -29.363 21.235  -17.555 1.00 32.57 ? 377  PHE C CE2 1 
ATOM   11752 C  CZ  . PHE C  1 360 ? -29.272 21.484  -16.203 1.00 32.15 ? 377  PHE C CZ  1 
ATOM   11753 N  N   . GLU C  1 361 ? -34.217 20.755  -20.055 1.00 34.90 ? 378  GLU C N   1 
ATOM   11754 C  CA  . GLU C  1 361 ? -34.288 21.770  -21.094 1.00 35.00 ? 378  GLU C CA  1 
ATOM   11755 C  C   . GLU C  1 361 ? -35.306 22.841  -20.709 1.00 34.26 ? 378  GLU C C   1 
ATOM   11756 O  O   . GLU C  1 361 ? -35.037 24.033  -20.847 1.00 35.36 ? 378  GLU C O   1 
ATOM   11757 C  CB  . GLU C  1 361 ? -34.641 21.141  -22.442 1.00 36.38 ? 378  GLU C CB  1 
ATOM   11758 C  CG  . GLU C  1 361 ? -34.702 22.147  -23.587 1.00 37.91 ? 378  GLU C CG  1 
ATOM   11759 C  CD  . GLU C  1 361 ? -35.253 21.561  -24.874 1.00 41.19 ? 378  GLU C CD  1 
ATOM   11760 O  OE1 . GLU C  1 361 ? -35.401 22.316  -25.859 1.00 42.33 ? 378  GLU C OE1 1 
ATOM   11761 O  OE2 . GLU C  1 361 ? -35.533 20.345  -24.887 1.00 41.79 ? 378  GLU C OE2 1 
ATOM   11762 N  N   . ASP C  1 362 ? -36.479 22.417  -20.229 1.00 34.85 ? 379  ASP C N   1 
ATOM   11763 C  CA  . ASP C  1 362 ? -37.504 23.357  -19.805 1.00 37.01 ? 379  ASP C CA  1 
ATOM   11764 C  C   . ASP C  1 362 ? -36.965 24.229  -18.671 1.00 35.97 ? 379  ASP C C   1 
ATOM   11765 O  O   . ASP C  1 362 ? -37.254 25.422  -18.615 1.00 36.98 ? 379  ASP C O   1 
ATOM   11766 C  CB  . ASP C  1 362 ? -38.794 22.657  -19.405 1.00 40.27 ? 379  ASP C CB  1 
ATOM   11767 C  CG  . ASP C  1 362 ? -39.437 21.787  -20.480 1.00 44.23 ? 379  ASP C CG  1 
ATOM   11768 O  OD1 . ASP C  1 362 ? -39.496 22.238  -21.648 1.00 44.76 ? 379  ASP C OD1 1 
ATOM   11769 O  OD2 . ASP C  1 362 ? -39.879 20.666  -20.137 1.00 46.96 ? 379  ASP C OD2 1 
ATOM   11770 N  N   . ALA C  1 363 ? -36.180 23.625  -17.770 1.00 35.32 ? 380  ALA C N   1 
ATOM   11771 C  CA  . ALA C  1 363 ? -35.636 24.338  -16.624 1.00 34.47 ? 380  ALA C CA  1 
ATOM   11772 C  C   . ALA C  1 363 ? -34.653 25.414  -17.080 1.00 32.98 ? 380  ALA C C   1 
ATOM   11773 O  O   . ALA C  1 363 ? -34.636 26.508  -16.522 1.00 33.96 ? 380  ALA C O   1 
ATOM   11774 C  CB  . ALA C  1 363 ? -34.989 23.362  -15.660 1.00 34.52 ? 380  ALA C CB  1 
ATOM   11775 N  N   . VAL C  1 364 ? -33.840 25.095  -18.092 1.00 32.65 ? 381  VAL C N   1 
ATOM   11776 C  CA  . VAL C  1 364 ? -32.889 26.044  -18.650 1.00 32.94 ? 381  VAL C CA  1 
ATOM   11777 C  C   . VAL C  1 364 ? -33.650 27.232  -19.238 1.00 33.70 ? 381  VAL C C   1 
ATOM   11778 O  O   . VAL C  1 364 ? -33.293 28.383  -18.990 1.00 33.71 ? 381  VAL C O   1 
ATOM   11779 C  CB  . VAL C  1 364 ? -31.967 25.366  -19.684 1.00 32.97 ? 381  VAL C CB  1 
ATOM   11780 C  CG1 . VAL C  1 364 ? -31.204 26.362  -20.552 1.00 33.10 ? 381  VAL C CG1 1 
ATOM   11781 C  CG2 . VAL C  1 364 ? -30.987 24.412  -19.008 1.00 33.69 ? 381  VAL C CG2 1 
ATOM   11782 N  N   . ASN C  1 365 ? -34.718 26.952  -19.993 1.00 34.40 ? 382  ASN C N   1 
ATOM   11783 C  CA  . ASN C  1 365 ? -35.440 27.999  -20.701 1.00 35.55 ? 382  ASN C CA  1 
ATOM   11784 C  C   . ASN C  1 365 ? -36.227 28.876  -19.726 1.00 35.76 ? 382  ASN C C   1 
ATOM   11785 O  O   . ASN C  1 365 ? -36.337 30.078  -19.947 1.00 36.28 ? 382  ASN C O   1 
ATOM   11786 C  CB  . ASN C  1 365 ? -36.290 27.422  -21.829 1.00 35.35 ? 382  ASN C CB  1 
ATOM   11787 C  CG  . ASN C  1 365 ? -35.447 27.065  -23.031 1.00 35.39 ? 382  ASN C CG  1 
ATOM   11788 O  OD1 . ASN C  1 365 ? -34.627 27.877  -23.472 1.00 36.55 ? 382  ASN C OD1 1 
ATOM   11789 N  ND2 . ASN C  1 365 ? -35.612 25.866  -23.572 1.00 36.65 ? 382  ASN C ND2 1 
ATOM   11790 N  N   . ILE C  1 366 ? -36.755 28.295  -18.642 1.00 37.19 ? 383  ILE C N   1 
ATOM   11791 C  CA  . ILE C  1 366 ? -37.521 29.071  -17.676 1.00 37.43 ? 383  ILE C CA  1 
ATOM   11792 C  C   . ILE C  1 366 ? -36.585 29.859  -16.756 1.00 36.39 ? 383  ILE C C   1 
ATOM   11793 O  O   . ILE C  1 366 ? -36.818 31.043  -16.527 1.00 35.10 ? 383  ILE C O   1 
ATOM   11794 C  CB  . ILE C  1 366 ? -38.501 28.180  -16.890 1.00 39.93 ? 383  ILE C CB  1 
ATOM   11795 C  CG1 . ILE C  1 366 ? -39.651 27.704  -17.786 1.00 41.83 ? 383  ILE C CG1 1 
ATOM   11796 C  CG2 . ILE C  1 366 ? -39.024 28.903  -15.647 1.00 40.95 ? 383  ILE C CG2 1 
ATOM   11797 C  CD1 . ILE C  1 366 ? -40.533 26.635  -17.163 1.00 43.83 ? 383  ILE C CD1 1 
ATOM   11798 N  N   . LEU C  1 367 ? -35.543 29.208  -16.217 1.00 34.36 ? 384  LEU C N   1 
ATOM   11799 C  CA  . LEU C  1 367 ? -34.691 29.820  -15.204 1.00 34.11 ? 384  LEU C CA  1 
ATOM   11800 C  C   . LEU C  1 367 ? -33.620 30.709  -15.840 1.00 32.28 ? 384  LEU C C   1 
ATOM   11801 O  O   . LEU C  1 367 ? -33.136 31.634  -15.192 1.00 31.24 ? 384  LEU C O   1 
ATOM   11802 C  CB  . LEU C  1 367 ? -34.045 28.753  -14.318 1.00 34.43 ? 384  LEU C CB  1 
ATOM   11803 C  CG  . LEU C  1 367 ? -34.979 27.971  -13.386 1.00 35.38 ? 384  LEU C CG  1 
ATOM   11804 C  CD1 . LEU C  1 367 ? -34.221 26.806  -12.773 1.00 35.88 ? 384  LEU C CD1 1 
ATOM   11805 C  CD2 . LEU C  1 367 ? -35.574 28.843  -12.290 1.00 36.37 ? 384  LEU C CD2 1 
ATOM   11806 N  N   . LYS C  1 368 ? -33.215 30.390  -17.076 1.00 31.86 ? 385  LYS C N   1 
ATOM   11807 C  CA  . LYS C  1 368 ? -32.197 31.138  -17.803 1.00 31.87 ? 385  LYS C CA  1 
ATOM   11808 C  C   . LYS C  1 368 ? -30.897 31.219  -17.004 1.00 30.08 ? 385  LYS C C   1 
ATOM   11809 O  O   . LYS C  1 368 ? -30.407 32.308  -16.715 1.00 30.67 ? 385  LYS C O   1 
ATOM   11810 C  CB  . LYS C  1 368 ? -32.698 32.536  -18.192 1.00 35.45 ? 385  LYS C CB  1 
ATOM   11811 C  CG  . LYS C  1 368 ? -33.828 32.531  -19.208 1.00 37.89 ? 385  LYS C CG  1 
ATOM   11812 C  CD  . LYS C  1 368 ? -34.129 33.894  -19.821 1.00 39.70 ? 385  LYS C CD  1 
ATOM   11813 C  CE  . LYS C  1 368 ? -34.960 33.768  -21.057 1.00 41.48 ? 385  LYS C CE  1 
ATOM   11814 N  NZ  . LYS C  1 368 ? -36.236 33.106  -20.779 1.00 44.32 ? 385  LYS C NZ  1 
ATOM   11815 N  N   . PRO C  1 369 ? -30.273 30.075  -16.643 1.00 27.88 ? 386  PRO C N   1 
ATOM   11816 C  CA  . PRO C  1 369 ? -28.970 30.098  -15.975 1.00 26.91 ? 386  PRO C CA  1 
ATOM   11817 C  C   . PRO C  1 369 ? -27.829 30.541  -16.889 1.00 25.90 ? 386  PRO C C   1 
ATOM   11818 O  O   . PRO C  1 369 ? -27.902 30.397  -18.106 1.00 25.73 ? 386  PRO C O   1 
ATOM   11819 C  CB  . PRO C  1 369 ? -28.809 28.639  -15.509 1.00 27.29 ? 386  PRO C CB  1 
ATOM   11820 C  CG  . PRO C  1 369 ? -29.582 27.843  -16.542 1.00 27.32 ? 386  PRO C CG  1 
ATOM   11821 C  CD  . PRO C  1 369 ? -30.786 28.712  -16.850 1.00 27.67 ? 386  PRO C CD  1 
ATOM   11822 N  N   . SER C  1 370 ? -26.775 31.085  -16.272 1.00 24.78 ? 387  SER C N   1 
ATOM   11823 C  CA  . SER C  1 370 ? -25.531 31.388  -16.953 1.00 25.17 ? 387  SER C CA  1 
ATOM   11824 C  C   . SER C  1 370 ? -24.605 30.173  -16.935 1.00 25.00 ? 387  SER C C   1 
ATOM   11825 O  O   . SER C  1 370 ? -23.656 30.111  -17.714 1.00 25.79 ? 387  SER C O   1 
ATOM   11826 C  CB  . SER C  1 370 ? -24.865 32.575  -16.315 1.00 26.14 ? 387  SER C CB  1 
ATOM   11827 O  OG  . SER C  1 370 ? -24.628 32.323  -14.939 1.00 28.53 ? 387  SER C OG  1 
ATOM   11828 N  N   . THR C  1 371 ? -24.890 29.218  -16.039 1.00 24.10 ? 388  THR C N   1 
ATOM   11829 C  CA  . THR C  1 371 ? -24.002 28.094  -15.775 1.00 24.00 ? 388  THR C CA  1 
ATOM   11830 C  C   . THR C  1 371 ? -24.847 26.855  -15.513 1.00 22.71 ? 388  THR C C   1 
ATOM   11831 O  O   . THR C  1 371 ? -25.788 26.919  -14.726 1.00 22.41 ? 388  THR C O   1 
ATOM   11832 C  CB  . THR C  1 371 ? -23.123 28.386  -14.559 1.00 24.71 ? 388  THR C CB  1 
ATOM   11833 O  OG1 . THR C  1 371 ? -22.377 29.569  -14.827 1.00 23.90 ? 388  THR C OG1 1 
ATOM   11834 C  CG2 . THR C  1 371 ? -22.155 27.254  -14.259 1.00 25.64 ? 388  THR C CG2 1 
ATOM   11835 N  N   . ILE C  1 372 ? -24.489 25.733  -16.154 1.00 22.92 ? 389  ILE C N   1 
ATOM   11836 C  CA  . ILE C  1 372 ? -25.065 24.446  -15.801 1.00 22.92 ? 389  ILE C CA  1 
ATOM   11837 C  C   . ILE C  1 372 ? -23.938 23.513  -15.367 1.00 22.41 ? 389  ILE C C   1 
ATOM   11838 O  O   . ILE C  1 372 ? -22.848 23.530  -15.938 1.00 21.55 ? 389  ILE C O   1 
ATOM   11839 C  CB  . ILE C  1 372 ? -25.929 23.855  -16.933 1.00 24.08 ? 389  ILE C CB  1 
ATOM   11840 C  CG1 . ILE C  1 372 ? -25.155 23.707  -18.244 1.00 24.71 ? 389  ILE C CG1 1 
ATOM   11841 C  CG2 . ILE C  1 372 ? -27.202 24.686  -17.101 1.00 24.80 ? 389  ILE C CG2 1 
ATOM   11842 C  CD1 . ILE C  1 372 ? -25.897 22.932  -19.321 1.00 25.28 ? 389  ILE C CD1 1 
ATOM   11843 N  N   . ILE C  1 373 ? -24.205 22.745  -14.307 1.00 22.76 ? 390  ILE C N   1 
ATOM   11844 C  CA  . ILE C  1 373 ? -23.215 21.835  -13.755 1.00 23.48 ? 390  ILE C CA  1 
ATOM   11845 C  C   . ILE C  1 373 ? -23.837 20.446  -13.701 1.00 23.58 ? 390  ILE C C   1 
ATOM   11846 O  O   . ILE C  1 373 ? -24.863 20.253  -13.052 1.00 22.82 ? 390  ILE C O   1 
ATOM   11847 C  CB  . ILE C  1 373 ? -22.725 22.299  -12.370 1.00 23.66 ? 390  ILE C CB  1 
ATOM   11848 C  CG1 . ILE C  1 373 ? -22.084 23.693  -12.436 1.00 23.77 ? 390  ILE C CG1 1 
ATOM   11849 C  CG2 . ILE C  1 373 ? -21.763 21.270  -11.763 1.00 23.18 ? 390  ILE C CG2 1 
ATOM   11850 C  CD1 . ILE C  1 373 ? -21.759 24.291  -11.077 1.00 24.28 ? 390  ILE C CD1 1 
ATOM   11851 N  N   . GLY C  1 374 ? -23.190 19.503  -14.396 1.00 24.88 ? 391  GLY C N   1 
ATOM   11852 C  CA  . GLY C  1 374 ? -23.684 18.143  -14.533 1.00 25.67 ? 391  GLY C CA  1 
ATOM   11853 C  C   . GLY C  1 374 ? -22.990 17.206  -13.545 1.00 25.49 ? 391  GLY C C   1 
ATOM   11854 O  O   . GLY C  1 374 ? -21.812 16.897  -13.704 1.00 25.61 ? 391  GLY C O   1 
ATOM   11855 N  N   . VAL C  1 375 ? -23.742 16.776  -12.529 1.00 26.26 ? 392  VAL C N   1 
ATOM   11856 C  CA  . VAL C  1 375 ? -23.244 15.870  -11.506 1.00 29.30 ? 392  VAL C CA  1 
ATOM   11857 C  C   . VAL C  1 375 ? -24.361 14.887  -11.155 1.00 29.64 ? 392  VAL C C   1 
ATOM   11858 O  O   . VAL C  1 375 ? -24.704 14.725  -9.988  1.00 28.57 ? 392  VAL C O   1 
ATOM   11859 C  CB  . VAL C  1 375 ? -22.742 16.645  -10.267 1.00 29.58 ? 392  VAL C CB  1 
ATOM   11860 C  CG1 . VAL C  1 375 ? -21.346 17.217  -10.477 1.00 30.74 ? 392  VAL C CG1 1 
ATOM   11861 C  CG2 . VAL C  1 375 ? -23.712 17.748  -9.850  1.00 30.74 ? 392  VAL C CG2 1 
ATOM   11862 N  N   . ALA C  1 376 ? -24.923 14.241  -12.189 1.00 31.47 ? 393  ALA C N   1 
ATOM   11863 C  CA  . ALA C  1 376 ? -26.019 13.295  -12.024 1.00 33.23 ? 393  ALA C CA  1 
ATOM   11864 C  C   . ALA C  1 376 ? -25.553 11.852  -12.228 1.00 33.95 ? 393  ALA C C   1 
ATOM   11865 O  O   . ALA C  1 376 ? -26.208 10.931  -11.751 1.00 34.25 ? 393  ALA C O   1 
ATOM   11866 C  CB  . ALA C  1 376 ? -27.145 13.635  -12.978 1.00 34.16 ? 393  ALA C CB  1 
ATOM   11867 N  N   . GLY C  1 377 ? -24.448 11.659  -12.962 1.00 36.39 ? 394  GLY C N   1 
ATOM   11868 C  CA  . GLY C  1 377 ? -23.902 10.335  -13.224 1.00 38.81 ? 394  GLY C CA  1 
ATOM   11869 C  C   . GLY C  1 377 ? -24.876 9.435   -13.987 1.00 41.12 ? 394  GLY C C   1 
ATOM   11870 O  O   . GLY C  1 377 ? -24.963 8.242   -13.701 1.00 41.19 ? 394  GLY C O   1 
ATOM   11871 N  N   . ALA C  1 378 ? -25.590 10.004  -14.970 1.00 41.81 ? 395  ALA C N   1 
ATOM   11872 C  CA  . ALA C  1 378 ? -26.675 9.295   -15.633 1.00 42.06 ? 395  ALA C CA  1 
ATOM   11873 C  C   . ALA C  1 378 ? -26.633 9.479   -17.150 1.00 41.00 ? 395  ALA C C   1 
ATOM   11874 O  O   . ALA C  1 378 ? -27.663 9.373   -17.810 1.00 43.79 ? 395  ALA C O   1 
ATOM   11875 C  CB  . ALA C  1 378 ? -27.998 9.756   -15.057 1.00 42.41 ? 395  ALA C CB  1 
ATOM   11876 N  N   . GLY C  1 379 ? -25.442 9.722   -17.707 1.00 41.62 ? 396  GLY C N   1 
ATOM   11877 C  CA  . GLY C  1 379 ? -25.271 9.777   -19.151 1.00 43.27 ? 396  GLY C CA  1 
ATOM   11878 C  C   . GLY C  1 379 ? -25.572 11.161  -19.726 1.00 43.98 ? 396  GLY C C   1 
ATOM   11879 O  O   . GLY C  1 379 ? -25.486 12.169  -19.026 1.00 43.83 ? 396  GLY C O   1 
ATOM   11880 N  N   . ARG C  1 380 ? -25.958 11.179  -21.008 1.00 43.13 ? 397  ARG C N   1 
ATOM   11881 C  CA  . ARG C  1 380 ? -25.899 12.370  -21.842 1.00 42.52 ? 397  ARG C CA  1 
ATOM   11882 C  C   . ARG C  1 380 ? -27.171 13.204  -21.699 1.00 41.26 ? 397  ARG C C   1 
ATOM   11883 O  O   . ARG C  1 380 ? -27.945 13.328  -22.647 1.00 41.81 ? 397  ARG C O   1 
ATOM   11884 C  CB  . ARG C  1 380 ? -25.688 11.919  -23.293 1.00 43.99 ? 397  ARG C CB  1 
ATOM   11885 C  CG  . ARG C  1 380 ? -24.383 11.183  -23.567 1.00 43.71 ? 397  ARG C CG  1 
ATOM   11886 C  CD  . ARG C  1 380 ? -23.206 12.131  -23.688 1.00 45.48 ? 397  ARG C CD  1 
ATOM   11887 N  NE  . ARG C  1 380 ? -22.000 11.494  -24.235 1.00 47.39 ? 397  ARG C NE  1 
ATOM   11888 C  CZ  . ARG C  1 380 ? -21.184 10.657  -23.596 1.00 49.45 ? 397  ARG C CZ  1 
ATOM   11889 N  NH1 . ARG C  1 380 ? -21.383 10.354  -22.321 1.00 49.65 ? 397  ARG C NH1 1 
ATOM   11890 N  NH2 . ARG C  1 380 ? -20.150 10.135  -24.237 1.00 49.26 ? 397  ARG C NH2 1 
ATOM   11891 N  N   . LEU C  1 381 ? -27.352 13.829  -20.529 1.00 38.32 ? 398  LEU C N   1 
ATOM   11892 C  CA  . LEU C  1 381 ? -28.574 14.560  -20.231 1.00 37.34 ? 398  LEU C CA  1 
ATOM   11893 C  C   . LEU C  1 381 ? -28.441 16.044  -20.577 1.00 33.05 ? 398  LEU C C   1 
ATOM   11894 O  O   . LEU C  1 381 ? -29.434 16.764  -20.560 1.00 33.99 ? 398  LEU C O   1 
ATOM   11895 C  CB  . LEU C  1 381 ? -28.942 14.347  -18.765 1.00 39.28 ? 398  LEU C CB  1 
ATOM   11896 C  CG  . LEU C  1 381 ? -29.330 12.914  -18.391 1.00 42.74 ? 398  LEU C CG  1 
ATOM   11897 C  CD1 . LEU C  1 381 ? -29.371 12.738  -16.886 1.00 43.53 ? 398  LEU C CD1 1 
ATOM   11898 C  CD2 . LEU C  1 381 ? -30.668 12.533  -19.004 1.00 44.63 ? 398  LEU C CD2 1 
ATOM   11899 N  N   . PHE C  1 382 ? -27.222 16.507  -20.868 1.00 31.46 ? 399  PHE C N   1 
ATOM   11900 C  CA  . PHE C  1 382 ? -27.038 17.793  -21.524 1.00 30.27 ? 399  PHE C CA  1 
ATOM   11901 C  C   . PHE C  1 382 ? -27.215 17.556  -23.021 1.00 30.09 ? 399  PHE C C   1 
ATOM   11902 O  O   . PHE C  1 382 ? -26.237 17.428  -23.754 1.00 26.83 ? 399  PHE C O   1 
ATOM   11903 C  CB  . PHE C  1 382 ? -25.679 18.415  -21.186 1.00 29.24 ? 399  PHE C CB  1 
ATOM   11904 C  CG  . PHE C  1 382 ? -25.524 18.992  -19.782 1.00 28.32 ? 399  PHE C CG  1 
ATOM   11905 C  CD1 . PHE C  1 382 ? -26.554 18.925  -18.846 1.00 28.32 ? 399  PHE C CD1 1 
ATOM   11906 C  CD2 . PHE C  1 382 ? -24.318 19.558  -19.387 1.00 28.59 ? 399  PHE C CD2 1 
ATOM   11907 C  CE1 . PHE C  1 382 ? -26.393 19.455  -17.575 1.00 28.70 ? 399  PHE C CE1 1 
ATOM   11908 C  CE2 . PHE C  1 382 ? -24.157 20.067  -18.105 1.00 28.44 ? 399  PHE C CE2 1 
ATOM   11909 C  CZ  . PHE C  1 382 ? -25.196 20.019  -17.208 1.00 27.91 ? 399  PHE C CZ  1 
ATOM   11910 N  N   . THR C  1 383 ? -28.483 17.472  -23.439 1.00 33.27 ? 400  THR C N   1 
ATOM   11911 C  CA  . THR C  1 383 ? -28.837 17.112  -24.804 1.00 34.77 ? 400  THR C CA  1 
ATOM   11912 C  C   . THR C  1 383 ? -28.459 18.261  -25.735 1.00 36.04 ? 400  THR C C   1 
ATOM   11913 O  O   . THR C  1 383 ? -28.249 19.389  -25.284 1.00 34.76 ? 400  THR C O   1 
ATOM   11914 C  CB  . THR C  1 383 ? -30.330 16.799  -24.898 1.00 35.06 ? 400  THR C CB  1 
ATOM   11915 O  OG1 . THR C  1 383 ? -30.993 18.031  -24.628 1.00 35.92 ? 400  THR C OG1 1 
ATOM   11916 C  CG2 . THR C  1 383 ? -30.773 15.715  -23.930 1.00 35.64 ? 400  THR C CG2 1 
ATOM   11917 N  N   . PRO C  1 384 ? -28.354 18.012  -27.059 1.00 34.77 ? 401  PRO C N   1 
ATOM   11918 C  CA  . PRO C  1 384 ? -28.176 19.095  -28.029 1.00 34.58 ? 401  PRO C CA  1 
ATOM   11919 C  C   . PRO C  1 384 ? -29.089 20.303  -27.828 1.00 33.48 ? 401  PRO C C   1 
ATOM   11920 O  O   . PRO C  1 384 ? -28.650 21.433  -28.020 1.00 33.68 ? 401  PRO C O   1 
ATOM   11921 C  CB  . PRO C  1 384 ? -28.439 18.370  -29.364 1.00 34.75 ? 401  PRO C CB  1 
ATOM   11922 C  CG  . PRO C  1 384 ? -27.880 16.986  -29.115 1.00 34.98 ? 401  PRO C CG  1 
ATOM   11923 C  CD  . PRO C  1 384 ? -28.320 16.678  -27.685 1.00 35.26 ? 401  PRO C CD  1 
ATOM   11924 N  N   . ASP C  1 385 ? -30.345 20.061  -27.429 1.00 33.31 ? 402  ASP C N   1 
ATOM   11925 C  CA  . ASP C  1 385 ? -31.305 21.137  -27.230 1.00 35.18 ? 402  ASP C CA  1 
ATOM   11926 C  C   . ASP C  1 385 ? -30.989 21.926  -25.957 1.00 33.48 ? 402  ASP C C   1 
ATOM   11927 O  O   . ASP C  1 385 ? -31.201 23.135  -25.919 1.00 34.33 ? 402  ASP C O   1 
ATOM   11928 C  CB  . ASP C  1 385 ? -32.734 20.619  -27.258 1.00 37.31 ? 402  ASP C CB  1 
ATOM   11929 C  CG  . ASP C  1 385 ? -33.239 20.192  -28.631 1.00 41.74 ? 402  ASP C CG  1 
ATOM   11930 O  OD1 . ASP C  1 385 ? -32.595 20.568  -29.641 1.00 42.74 ? 402  ASP C OD1 1 
ATOM   11931 O  OD2 . ASP C  1 385 ? -34.256 19.471  -28.676 1.00 43.16 ? 402  ASP C OD2 1 
ATOM   11932 N  N   . VAL C  1 386 ? -30.509 21.240  -24.913 1.00 32.15 ? 403  VAL C N   1 
ATOM   11933 C  CA  . VAL C  1 386 ? -30.067 21.903  -23.693 1.00 30.54 ? 403  VAL C CA  1 
ATOM   11934 C  C   . VAL C  1 386 ? -28.895 22.825  -24.025 1.00 28.84 ? 403  VAL C C   1 
ATOM   11935 O  O   . VAL C  1 386 ? -28.897 23.985  -23.626 1.00 28.23 ? 403  VAL C O   1 
ATOM   11936 C  CB  . VAL C  1 386 ? -29.698 20.895  -22.585 1.00 30.51 ? 403  VAL C CB  1 
ATOM   11937 C  CG1 . VAL C  1 386 ? -28.902 21.535  -21.450 1.00 30.77 ? 403  VAL C CG1 1 
ATOM   11938 C  CG2 . VAL C  1 386 ? -30.937 20.206  -22.038 1.00 30.94 ? 403  VAL C CG2 1 
ATOM   11939 N  N   . ILE C  1 387 ? -27.917 22.295  -24.769 1.00 28.38 ? 404  ILE C N   1 
ATOM   11940 C  CA  . ILE C  1 387 ? -26.700 23.016  -25.106 1.00 29.74 ? 404  ILE C CA  1 
ATOM   11941 C  C   . ILE C  1 387 ? -27.035 24.229  -25.974 1.00 30.92 ? 404  ILE C C   1 
ATOM   11942 O  O   . ILE C  1 387 ? -26.483 25.306  -25.769 1.00 31.08 ? 404  ILE C O   1 
ATOM   11943 C  CB  . ILE C  1 387 ? -25.685 22.077  -25.787 1.00 29.52 ? 404  ILE C CB  1 
ATOM   11944 C  CG1 . ILE C  1 387 ? -25.238 20.960  -24.841 1.00 30.61 ? 404  ILE C CG1 1 
ATOM   11945 C  CG2 . ILE C  1 387 ? -24.488 22.857  -26.327 1.00 30.02 ? 404  ILE C CG2 1 
ATOM   11946 C  CD1 . ILE C  1 387 ? -24.329 19.923  -25.476 1.00 30.83 ? 404  ILE C CD1 1 
ATOM   11947 N  N   . ARG C  1 388 ? -27.930 24.040  -26.951 1.00 32.39 ? 405  ARG C N   1 
ATOM   11948 C  CA  . ARG C  1 388 ? -28.346 25.114  -27.839 1.00 32.50 ? 405  ARG C CA  1 
ATOM   11949 C  C   . ARG C  1 388 ? -29.082 26.193  -27.050 1.00 30.34 ? 405  ARG C C   1 
ATOM   11950 O  O   . ARG C  1 388 ? -28.860 27.382  -27.270 1.00 29.93 ? 405  ARG C O   1 
ATOM   11951 C  CB  . ARG C  1 388 ? -29.216 24.574  -28.981 1.00 35.20 ? 405  ARG C CB  1 
ATOM   11952 C  CG  . ARG C  1 388 ? -28.436 23.911  -30.105 1.00 36.95 ? 405  ARG C CG  1 
ATOM   11953 C  CD  . ARG C  1 388 ? -29.344 23.107  -31.029 1.00 39.76 ? 405  ARG C CD  1 
ATOM   11954 N  NE  . ARG C  1 388 ? -30.431 23.888  -31.634 1.00 41.44 ? 405  ARG C NE  1 
ATOM   11955 C  CZ  . ARG C  1 388 ? -30.321 24.765  -32.632 1.00 42.51 ? 405  ARG C CZ  1 
ATOM   11956 N  NH1 . ARG C  1 388 ? -29.142 25.050  -33.163 1.00 42.32 ? 405  ARG C NH1 1 
ATOM   11957 N  NH2 . ARG C  1 388 ? -31.407 25.356  -33.103 1.00 42.33 ? 405  ARG C NH2 1 
ATOM   11958 N  N   . ALA C  1 389 ? -29.950 25.777  -26.123 1.00 30.64 ? 406  ALA C N   1 
ATOM   11959 C  CA  . ALA C  1 389 ? -30.676 26.725  -25.292 1.00 31.27 ? 406  ALA C CA  1 
ATOM   11960 C  C   . ALA C  1 389 ? -29.703 27.603  -24.502 1.00 31.40 ? 406  ALA C C   1 
ATOM   11961 O  O   . ALA C  1 389 ? -29.904 28.814  -24.395 1.00 29.48 ? 406  ALA C O   1 
ATOM   11962 C  CB  . ALA C  1 389 ? -31.630 25.991  -24.381 1.00 32.02 ? 406  ALA C CB  1 
ATOM   11963 N  N   . MET C  1 390 ? -28.648 26.988  -23.951 1.00 29.73 ? 407  MET C N   1 
ATOM   11964 C  CA  . MET C  1 390 ? -27.663 27.712  -23.161 1.00 29.09 ? 407  MET C CA  1 
ATOM   11965 C  C   . MET C  1 390 ? -26.965 28.774  -24.015 1.00 29.24 ? 407  MET C C   1 
ATOM   11966 O  O   . MET C  1 390 ? -26.725 29.885  -23.543 1.00 28.48 ? 407  MET C O   1 
ATOM   11967 C  CB  . MET C  1 390 ? -26.623 26.756  -22.558 1.00 28.49 ? 407  MET C CB  1 
ATOM   11968 C  CG  . MET C  1 390 ? -27.108 26.008  -21.332 1.00 28.20 ? 407  MET C CG  1 
ATOM   11969 S  SD  . MET C  1 390 ? -27.484 27.105  -19.950 1.00 28.62 ? 407  MET C SD  1 
ATOM   11970 C  CE  . MET C  1 390 ? -25.840 27.669  -19.490 1.00 28.50 ? 407  MET C CE  1 
ATOM   11971 N  N   . ALA C  1 391 ? -26.647 28.427  -25.268 1.00 30.78 ? 408  ALA C N   1 
ATOM   11972 C  CA  . ALA C  1 391 ? -25.965 29.334  -26.182 1.00 32.47 ? 408  ALA C CA  1 
ATOM   11973 C  C   . ALA C  1 391 ? -26.902 30.435  -26.682 1.00 32.23 ? 408  ALA C C   1 
ATOM   11974 O  O   . ALA C  1 391 ? -26.441 31.496  -27.096 1.00 32.54 ? 408  ALA C O   1 
ATOM   11975 C  CB  . ALA C  1 391 ? -25.381 28.551  -27.337 1.00 32.71 ? 408  ALA C CB  1 
ATOM   11976 N  N   . SER C  1 392 ? -28.211 30.167  -26.667 1.00 33.99 ? 409  SER C N   1 
ATOM   11977 C  CA  . SER C  1 392 ? -29.216 31.147  -27.049 1.00 34.49 ? 409  SER C CA  1 
ATOM   11978 C  C   . SER C  1 392 ? -29.417 32.168  -25.931 1.00 35.08 ? 409  SER C C   1 
ATOM   11979 O  O   . SER C  1 392 ? -29.725 33.330  -26.195 1.00 34.01 ? 409  SER C O   1 
ATOM   11980 C  CB  . SER C  1 392 ? -30.516 30.466  -27.402 1.00 36.71 ? 409  SER C CB  1 
ATOM   11981 O  OG  . SER C  1 392 ? -31.558 31.416  -27.565 1.00 39.00 ? 409  SER C OG  1 
ATOM   11982 N  N   . ILE C  1 393 ? -29.245 31.719  -24.682 1.00 32.15 ? 410  ILE C N   1 
ATOM   11983 C  CA  . ILE C  1 393 ? -29.532 32.531  -23.513 1.00 32.54 ? 410  ILE C CA  1 
ATOM   11984 C  C   . ILE C  1 393 ? -28.308 33.370  -23.149 1.00 30.82 ? 410  ILE C C   1 
ATOM   11985 O  O   . ILE C  1 393 ? -28.457 34.516  -22.729 1.00 32.17 ? 410  ILE C O   1 
ATOM   11986 C  CB  . ILE C  1 393 ? -30.002 31.634  -22.351 1.00 33.73 ? 410  ILE C CB  1 
ATOM   11987 C  CG1 . ILE C  1 393 ? -31.357 30.995  -22.669 1.00 34.56 ? 410  ILE C CG1 1 
ATOM   11988 C  CG2 . ILE C  1 393 ? -30.047 32.399  -21.026 1.00 34.34 ? 410  ILE C CG2 1 
ATOM   11989 C  CD1 . ILE C  1 393 ? -31.692 29.785  -21.813 1.00 34.99 ? 410  ILE C CD1 1 
ATOM   11990 N  N   . ASN C  1 394 ? -27.111 32.791  -23.313 1.00 28.30 ? 411  ASN C N   1 
ATOM   11991 C  CA  . ASN C  1 394 ? -25.869 33.396  -22.861 1.00 28.18 ? 411  ASN C CA  1 
ATOM   11992 C  C   . ASN C  1 394 ? -24.909 33.501  -24.035 1.00 27.87 ? 411  ASN C C   1 
ATOM   11993 O  O   . ASN C  1 394 ? -24.853 32.598  -24.866 1.00 29.41 ? 411  ASN C O   1 
ATOM   11994 C  CB  . ASN C  1 394 ? -25.186 32.570  -21.774 1.00 26.96 ? 411  ASN C CB  1 
ATOM   11995 C  CG  . ASN C  1 394 ? -26.128 32.234  -20.646 1.00 26.36 ? 411  ASN C CG  1 
ATOM   11996 O  OD1 . ASN C  1 394 ? -26.388 33.079  -19.783 1.00 27.28 ? 411  ASN C OD1 1 
ATOM   11997 N  ND2 . ASN C  1 394 ? -26.645 31.016  -20.630 1.00 25.88 ? 411  ASN C ND2 1 
ATOM   11998 N  N   . GLU C  1 395 ? -24.140 34.591  -24.071 1.00 27.71 ? 412  GLU C N   1 
ATOM   11999 C  CA  . GLU C  1 395 ? -23.102 34.751  -25.072 1.00 28.34 ? 412  GLU C CA  1 
ATOM   12000 C  C   . GLU C  1 395 ? -22.011 33.701  -24.865 1.00 28.32 ? 412  GLU C C   1 
ATOM   12001 O  O   . GLU C  1 395 ? -21.521 33.136  -25.840 1.00 29.70 ? 412  GLU C O   1 
ATOM   12002 C  CB  . GLU C  1 395 ? -22.507 36.157  -25.046 1.00 29.79 ? 412  GLU C CB  1 
ATOM   12003 C  CG  . GLU C  1 395 ? -21.375 36.344  -26.053 1.00 32.25 ? 412  GLU C CG  1 
ATOM   12004 C  CD  . GLU C  1 395 ? -21.751 36.150  -27.515 1.00 35.22 ? 412  GLU C CD  1 
ATOM   12005 O  OE1 . GLU C  1 395 ? -20.819 35.866  -28.301 1.00 37.62 ? 412  GLU C OE1 1 
ATOM   12006 O  OE2 . GLU C  1 395 ? -22.944 36.299  -27.878 1.00 37.03 ? 412  GLU C OE2 1 
ATOM   12007 N  N   . ARG C  1 396 ? -21.628 33.456  -23.604 1.00 27.34 ? 413  ARG C N   1 
ATOM   12008 C  CA  . ARG C  1 396 ? -20.582 32.492  -23.288 1.00 27.84 ? 413  ARG C CA  1 
ATOM   12009 C  C   . ARG C  1 396 ? -21.098 31.539  -22.215 1.00 27.06 ? 413  ARG C C   1 
ATOM   12010 O  O   . ARG C  1 396 ? -20.823 31.726  -21.033 1.00 26.52 ? 413  ARG C O   1 
ATOM   12011 C  CB  . ARG C  1 396 ? -19.299 33.198  -22.831 1.00 28.74 ? 413  ARG C CB  1 
ATOM   12012 C  CG  . ARG C  1 396 ? -18.735 34.224  -23.806 1.00 29.52 ? 413  ARG C CG  1 
ATOM   12013 C  CD  . ARG C  1 396 ? -18.310 33.631  -25.144 1.00 30.13 ? 413  ARG C CD  1 
ATOM   12014 N  NE  . ARG C  1 396 ? -17.166 32.716  -25.051 1.00 30.80 ? 413  ARG C NE  1 
ATOM   12015 C  CZ  . ARG C  1 396 ? -15.885 33.052  -24.932 1.00 32.11 ? 413  ARG C CZ  1 
ATOM   12016 N  NH1 . ARG C  1 396 ? -15.513 34.320  -24.852 1.00 32.61 ? 413  ARG C NH1 1 
ATOM   12017 N  NH2 . ARG C  1 396 ? -14.966 32.103  -24.896 1.00 31.75 ? 413  ARG C NH2 1 
ATOM   12018 N  N   . PRO C  1 397 ? -21.889 30.502  -22.576 1.00 26.50 ? 414  PRO C N   1 
ATOM   12019 C  CA  . PRO C  1 397 ? -22.467 29.608  -21.575 1.00 27.11 ? 414  PRO C CA  1 
ATOM   12020 C  C   . PRO C  1 397 ? -21.382 28.776  -20.892 1.00 25.56 ? 414  PRO C C   1 
ATOM   12021 O  O   . PRO C  1 397 ? -20.455 28.302  -21.543 1.00 26.57 ? 414  PRO C O   1 
ATOM   12022 C  CB  . PRO C  1 397 ? -23.448 28.755  -22.391 1.00 27.10 ? 414  PRO C CB  1 
ATOM   12023 C  CG  . PRO C  1 397 ? -22.851 28.739  -23.774 1.00 27.27 ? 414  PRO C CG  1 
ATOM   12024 C  CD  . PRO C  1 397 ? -22.272 30.134  -23.949 1.00 27.17 ? 414  PRO C CD  1 
ATOM   12025 N  N   . VAL C  1 398 ? -21.492 28.647  -19.568 1.00 25.52 ? 415  VAL C N   1 
ATOM   12026 C  CA  . VAL C  1 398 ? -20.582 27.819  -18.793 1.00 23.51 ? 415  VAL C CA  1 
ATOM   12027 C  C   . VAL C  1 398 ? -21.240 26.453  -18.649 1.00 22.48 ? 415  VAL C C   1 
ATOM   12028 O  O   . VAL C  1 398 ? -22.332 26.348  -18.097 1.00 22.96 ? 415  VAL C O   1 
ATOM   12029 C  CB  . VAL C  1 398 ? -20.259 28.423  -17.410 1.00 23.60 ? 415  VAL C CB  1 
ATOM   12030 C  CG1 . VAL C  1 398 ? -19.261 27.566  -16.642 1.00 23.14 ? 415  VAL C CG1 1 
ATOM   12031 C  CG2 . VAL C  1 398 ? -19.743 29.856  -17.507 1.00 24.03 ? 415  VAL C CG2 1 
ATOM   12032 N  N   . ILE C  1 399 ? -20.567 25.415  -19.151 1.00 22.63 ? 416  ILE C N   1 
ATOM   12033 C  CA  . ILE C  1 399 ? -21.108 24.066  -19.176 1.00 22.28 ? 416  ILE C CA  1 
ATOM   12034 C  C   . ILE C  1 399 ? -20.064 23.132  -18.572 1.00 23.19 ? 416  ILE C C   1 
ATOM   12035 O  O   . ILE C  1 399 ? -19.012 22.917  -19.173 1.00 24.58 ? 416  ILE C O   1 
ATOM   12036 C  CB  . ILE C  1 399 ? -21.474 23.647  -20.614 1.00 23.30 ? 416  ILE C CB  1 
ATOM   12037 C  CG1 . ILE C  1 399 ? -22.445 24.641  -21.271 1.00 24.42 ? 416  ILE C CG1 1 
ATOM   12038 C  CG2 . ILE C  1 399 ? -22.022 22.219  -20.641 1.00 23.43 ? 416  ILE C CG2 1 
ATOM   12039 C  CD1 . ILE C  1 399 ? -22.782 24.332  -22.719 1.00 25.56 ? 416  ILE C CD1 1 
ATOM   12040 N  N   . PHE C  1 400 ? -20.352 22.620  -17.370 1.00 23.19 ? 417  PHE C N   1 
ATOM   12041 C  CA  . PHE C  1 400 ? -19.474 21.672  -16.700 1.00 24.26 ? 417  PHE C CA  1 
ATOM   12042 C  C   . PHE C  1 400 ? -20.153 20.309  -16.698 1.00 24.73 ? 417  PHE C C   1 
ATOM   12043 O  O   . PHE C  1 400 ? -21.222 20.152  -16.111 1.00 25.45 ? 417  PHE C O   1 
ATOM   12044 C  CB  . PHE C  1 400 ? -19.150 22.106  -15.267 1.00 25.71 ? 417  PHE C CB  1 
ATOM   12045 C  CG  . PHE C  1 400 ? -18.069 23.168  -15.124 1.00 26.62 ? 417  PHE C CG  1 
ATOM   12046 C  CD1 . PHE C  1 400 ? -17.793 24.069  -16.148 1.00 27.03 ? 417  PHE C CD1 1 
ATOM   12047 C  CD2 . PHE C  1 400 ? -17.333 23.273  -13.947 1.00 27.70 ? 417  PHE C CD2 1 
ATOM   12048 C  CE1 . PHE C  1 400 ? -16.817 25.041  -16.001 1.00 27.44 ? 417  PHE C CE1 1 
ATOM   12049 C  CE2 . PHE C  1 400 ? -16.349 24.241  -13.813 1.00 27.93 ? 417  PHE C CE2 1 
ATOM   12050 C  CZ  . PHE C  1 400 ? -16.100 25.127  -14.837 1.00 27.80 ? 417  PHE C CZ  1 
ATOM   12051 N  N   . ALA C  1 401 ? -19.535 19.352  -17.398 1.00 26.13 ? 418  ALA C N   1 
ATOM   12052 C  CA  . ALA C  1 401 ? -20.024 17.984  -17.472 1.00 26.76 ? 418  ALA C CA  1 
ATOM   12053 C  C   . ALA C  1 401 ? -19.084 17.096  -16.663 1.00 27.77 ? 418  ALA C C   1 
ATOM   12054 O  O   . ALA C  1 401 ? -18.115 16.568  -17.209 1.00 28.20 ? 418  ALA C O   1 
ATOM   12055 C  CB  . ALA C  1 401 ? -20.106 17.548  -18.921 1.00 26.25 ? 418  ALA C CB  1 
ATOM   12056 N  N   . LEU C  1 402 ? -19.375 16.968  -15.361 1.00 28.72 ? 419  LEU C N   1 
ATOM   12057 C  CA  . LEU C  1 402 ? -18.410 16.465  -14.392 1.00 31.67 ? 419  LEU C CA  1 
ATOM   12058 C  C   . LEU C  1 402 ? -18.570 14.963  -14.148 1.00 34.78 ? 419  LEU C C   1 
ATOM   12059 O  O   . LEU C  1 402 ? -17.671 14.346  -13.577 1.00 35.74 ? 419  LEU C O   1 
ATOM   12060 C  CB  . LEU C  1 402 ? -18.527 17.240  -13.078 1.00 30.75 ? 419  LEU C CB  1 
ATOM   12061 C  CG  . LEU C  1 402 ? -18.208 18.738  -13.131 1.00 29.93 ? 419  LEU C CG  1 
ATOM   12062 C  CD1 . LEU C  1 402 ? -18.214 19.324  -11.728 1.00 29.44 ? 419  LEU C CD1 1 
ATOM   12063 C  CD2 . LEU C  1 402 ? -16.883 19.028  -13.818 1.00 30.63 ? 419  LEU C CD2 1 
ATOM   12064 N  N   . SER C  1 403 ? -19.699 14.376  -14.561 1.00 36.94 ? 420  SER C N   1 
ATOM   12065 C  CA  . SER C  1 403 ? -19.962 12.972  -14.281 1.00 37.82 ? 420  SER C CA  1 
ATOM   12066 C  C   . SER C  1 403 ? -18.917 12.079  -14.954 1.00 38.39 ? 420  SER C C   1 
ATOM   12067 O  O   . SER C  1 403 ? -18.510 12.327  -16.088 1.00 38.72 ? 420  SER C O   1 
ATOM   12068 C  CB  . SER C  1 403 ? -21.361 12.602  -14.672 1.00 37.26 ? 420  SER C CB  1 
ATOM   12069 O  OG  . SER C  1 403 ? -22.299 13.262  -13.834 1.00 35.94 ? 420  SER C OG  1 
ATOM   12070 N  N   . ASN C  1 404 ? -18.468 11.055  -14.215 1.00 40.95 ? 421  ASN C N   1 
ATOM   12071 C  CA  . ASN C  1 404 ? -17.454 10.101  -14.647 1.00 41.89 ? 421  ASN C CA  1 
ATOM   12072 C  C   . ASN C  1 404 ? -18.018 8.683   -14.539 1.00 43.03 ? 421  ASN C C   1 
ATOM   12073 O  O   . ASN C  1 404 ? -18.905 8.446   -13.720 1.00 40.84 ? 421  ASN C O   1 
ATOM   12074 C  CB  . ASN C  1 404 ? -16.188 10.191  -13.798 1.00 42.97 ? 421  ASN C CB  1 
ATOM   12075 C  CG  . ASN C  1 404 ? -15.575 11.573  -13.798 1.00 44.41 ? 421  ASN C CG  1 
ATOM   12076 O  OD1 . ASN C  1 404 ? -15.194 12.088  -14.855 1.00 42.81 ? 421  ASN C OD1 1 
ATOM   12077 N  ND2 . ASN C  1 404 ? -15.451 12.183  -12.628 1.00 45.48 ? 421  ASN C ND2 1 
ATOM   12078 N  N   . PRO C  1 405 ? -17.542 7.689   -15.336 1.00 44.33 ? 422  PRO C N   1 
ATOM   12079 C  CA  . PRO C  1 405 ? -16.548 7.903   -16.395 1.00 44.07 ? 422  PRO C CA  1 
ATOM   12080 C  C   . PRO C  1 405 ? -17.162 8.447   -17.684 1.00 42.56 ? 422  PRO C C   1 
ATOM   12081 O  O   . PRO C  1 405 ? -18.350 8.755   -17.711 1.00 42.28 ? 422  PRO C O   1 
ATOM   12082 C  CB  . PRO C  1 405 ? -15.969 6.486   -16.567 1.00 45.62 ? 422  PRO C CB  1 
ATOM   12083 C  CG  . PRO C  1 405 ? -17.160 5.584   -16.331 1.00 45.87 ? 422  PRO C CG  1 
ATOM   12084 C  CD  . PRO C  1 405 ? -17.943 6.275   -15.225 1.00 45.16 ? 422  PRO C CD  1 
ATOM   12085 N  N   . THR C  1 406 ? -16.349 8.535   -18.748 1.00 43.57 ? 423  THR C N   1 
ATOM   12086 C  CA  . THR C  1 406 ? -16.721 9.219   -19.981 1.00 44.84 ? 423  THR C CA  1 
ATOM   12087 C  C   . THR C  1 406 ? -18.142 8.856   -20.410 1.00 45.35 ? 423  THR C C   1 
ATOM   12088 O  O   . THR C  1 406 ? -18.866 9.718   -20.904 1.00 43.01 ? 423  THR C O   1 
ATOM   12089 C  CB  . THR C  1 406 ? -15.726 8.899   -21.096 1.00 47.91 ? 423  THR C CB  1 
ATOM   12090 O  OG1 . THR C  1 406 ? -14.428 9.193   -20.591 1.00 50.16 ? 423  THR C OG1 1 
ATOM   12091 C  CG2 . THR C  1 406 ? -15.973 9.722   -22.349 1.00 48.49 ? 423  THR C CG2 1 
ATOM   12092 N  N   . ALA C  1 407 ? -18.534 7.588   -20.224 1.00 46.24 ? 424  ALA C N   1 
ATOM   12093 C  CA  . ALA C  1 407 ? -19.829 7.101   -20.683 1.00 47.56 ? 424  ALA C CA  1 
ATOM   12094 C  C   . ALA C  1 407 ? -20.982 7.753   -19.916 1.00 46.26 ? 424  ALA C C   1 
ATOM   12095 O  O   . ALA C  1 407 ? -22.102 7.814   -20.423 1.00 48.97 ? 424  ALA C O   1 
ATOM   12096 C  CB  . ALA C  1 407 ? -19.882 5.590   -20.571 1.00 47.87 ? 424  ALA C CB  1 
ATOM   12097 N  N   . GLN C  1 408 ? -20.715 8.237   -18.697 1.00 43.01 ? 425  GLN C N   1 
ATOM   12098 C  CA  . GLN C  1 408 ? -21.756 8.800   -17.851 1.00 41.57 ? 425  GLN C CA  1 
ATOM   12099 C  C   . GLN C  1 408 ? -21.811 10.326  -17.967 1.00 36.49 ? 425  GLN C C   1 
ATOM   12100 O  O   . GLN C  1 408 ? -22.684 10.946  -17.370 1.00 32.32 ? 425  GLN C O   1 
ATOM   12101 C  CB  . GLN C  1 408 ? -21.519 8.371   -16.403 1.00 45.00 ? 425  GLN C CB  1 
ATOM   12102 C  CG  . GLN C  1 408 ? -21.530 6.861   -16.192 1.00 48.11 ? 425  GLN C CG  1 
ATOM   12103 C  CD  . GLN C  1 408 ? -22.836 6.213   -16.594 1.00 50.14 ? 425  GLN C CD  1 
ATOM   12104 O  OE1 . GLN C  1 408 ? -23.917 6.603   -16.137 1.00 53.42 ? 425  GLN C OE1 1 
ATOM   12105 N  NE2 . GLN C  1 408 ? -22.754 5.220   -17.468 1.00 51.38 ? 425  GLN C NE2 1 
ATOM   12106 N  N   . ALA C  1 409 ? -20.897 10.927  -18.743 1.00 36.40 ? 426  ALA C N   1 
ATOM   12107 C  CA  . ALA C  1 409 ? -20.810 12.377  -18.851 1.00 35.57 ? 426  ALA C CA  1 
ATOM   12108 C  C   . ALA C  1 409 ? -22.075 12.951  -19.490 1.00 35.61 ? 426  ALA C C   1 
ATOM   12109 O  O   . ALA C  1 409 ? -22.721 12.301  -20.311 1.00 35.75 ? 426  ALA C O   1 
ATOM   12110 C  CB  . ALA C  1 409 ? -19.578 12.768  -19.637 1.00 36.33 ? 426  ALA C CB  1 
ATOM   12111 N  N   . GLU C  1 410 ? -22.408 14.191  -19.108 1.00 32.91 ? 427  GLU C N   1 
ATOM   12112 C  CA  . GLU C  1 410 ? -23.621 14.848  -19.568 1.00 31.81 ? 427  GLU C CA  1 
ATOM   12113 C  C   . GLU C  1 410 ? -23.514 15.189  -21.053 1.00 31.73 ? 427  GLU C C   1 
ATOM   12114 O  O   . GLU C  1 410 ? -24.527 15.264  -21.742 1.00 32.96 ? 427  GLU C O   1 
ATOM   12115 C  CB  . GLU C  1 410 ? -23.925 16.094  -18.735 1.00 30.86 ? 427  GLU C CB  1 
ATOM   12116 C  CG  . GLU C  1 410 ? -24.455 15.783  -17.338 1.00 30.28 ? 427  GLU C CG  1 
ATOM   12117 C  CD  . GLU C  1 410 ? -23.461 15.267  -16.300 1.00 29.43 ? 427  GLU C CD  1 
ATOM   12118 O  OE1 . GLU C  1 410 ? -22.232 15.285  -16.539 1.00 28.53 ? 427  GLU C OE1 1 
ATOM   12119 O  OE2 . GLU C  1 410 ? -23.948 14.842  -15.227 1.00 28.66 ? 427  GLU C OE2 1 
ATOM   12120 N  N   . CYS C  1 411 ? -22.284 15.412  -21.526 1.00 31.70 ? 428  CYS C N   1 
ATOM   12121 C  CA  . CYS C  1 411 ? -22.012 15.633  -22.936 1.00 32.96 ? 428  CYS C CA  1 
ATOM   12122 C  C   . CYS C  1 411 ? -20.507 15.538  -23.141 1.00 33.61 ? 428  CYS C C   1 
ATOM   12123 O  O   . CYS C  1 411 ? -19.764 15.433  -22.169 1.00 35.26 ? 428  CYS C O   1 
ATOM   12124 C  CB  . CYS C  1 411 ? -22.551 16.977  -23.425 1.00 33.05 ? 428  CYS C CB  1 
ATOM   12125 S  SG  . CYS C  1 411 ? -21.795 18.418  -22.623 1.00 32.69 ? 428  CYS C SG  1 
ATOM   12126 N  N   . THR C  1 412 ? -20.078 15.576  -24.405 1.00 34.77 ? 429  THR C N   1 
ATOM   12127 C  CA  . THR C  1 412 ? -18.666 15.573  -24.748 1.00 36.83 ? 429  THR C CA  1 
ATOM   12128 C  C   . THR C  1 412 ? -18.226 17.004  -25.027 1.00 36.52 ? 429  THR C C   1 
ATOM   12129 O  O   . THR C  1 412 ? -19.059 17.885  -25.225 1.00 39.05 ? 429  THR C O   1 
ATOM   12130 C  CB  . THR C  1 412 ? -18.424 14.675  -25.962 1.00 38.98 ? 429  THR C CB  1 
ATOM   12131 O  OG1 . THR C  1 412 ? -19.138 15.258  -27.049 1.00 39.72 ? 429  THR C OG1 1 
ATOM   12132 C  CG2 . THR C  1 412 ? -18.906 13.253  -25.740 1.00 39.45 ? 429  THR C CG2 1 
ATOM   12133 N  N   . ALA C  1 413 ? -16.909 17.212  -25.040 1.00 36.20 ? 430  ALA C N   1 
ATOM   12134 C  CA  . ALA C  1 413 ? -16.329 18.473  -25.465 1.00 38.58 ? 430  ALA C CA  1 
ATOM   12135 C  C   . ALA C  1 413 ? -16.779 18.788  -26.891 1.00 40.56 ? 430  ALA C C   1 
ATOM   12136 O  O   . ALA C  1 413 ? -17.146 19.923  -27.188 1.00 38.84 ? 430  ALA C O   1 
ATOM   12137 C  CB  . ALA C  1 413 ? -14.823 18.405  -25.355 1.00 37.87 ? 430  ALA C CB  1 
ATOM   12138 N  N   . GLU C  1 414 ? -16.764 17.756  -27.748 1.00 43.14 ? 431  GLU C N   1 
ATOM   12139 C  CA  . GLU C  1 414 ? -17.155 17.869  -29.144 1.00 43.90 ? 431  GLU C CA  1 
ATOM   12140 C  C   . GLU C  1 414 ? -18.552 18.477  -29.246 1.00 40.47 ? 431  GLU C C   1 
ATOM   12141 O  O   . GLU C  1 414 ? -18.742 19.485  -29.922 1.00 39.60 ? 431  GLU C O   1 
ATOM   12142 C  CB  . GLU C  1 414 ? -17.105 16.483  -29.793 1.00 48.97 ? 431  GLU C CB  1 
ATOM   12143 C  CG  . GLU C  1 414 ? -17.137 16.498  -31.320 1.00 54.25 ? 431  GLU C CG  1 
ATOM   12144 C  CD  . GLU C  1 414 ? -15.842 16.946  -31.978 1.00 60.10 ? 431  GLU C CD  1 
ATOM   12145 O  OE1 . GLU C  1 414 ? -14.765 16.454  -31.572 1.00 64.06 ? 431  GLU C OE1 1 
ATOM   12146 O  OE2 . GLU C  1 414 ? -15.911 17.770  -32.916 1.00 65.21 ? 431  GLU C OE2 1 
ATOM   12147 N  N   . GLU C  1 415 ? -19.520 17.864  -28.556 1.00 39.42 ? 432  GLU C N   1 
ATOM   12148 C  CA  . GLU C  1 415 ? -20.895 18.339  -28.567 1.00 40.97 ? 432  GLU C CA  1 
ATOM   12149 C  C   . GLU C  1 415 ? -20.970 19.781  -28.064 1.00 39.02 ? 432  GLU C C   1 
ATOM   12150 O  O   . GLU C  1 415 ? -21.699 20.593  -28.634 1.00 38.68 ? 432  GLU C O   1 
ATOM   12151 C  CB  . GLU C  1 415 ? -21.787 17.428  -27.724 1.00 43.05 ? 432  GLU C CB  1 
ATOM   12152 C  CG  . GLU C  1 415 ? -22.052 16.072  -28.374 1.00 45.60 ? 432  GLU C CG  1 
ATOM   12153 C  CD  . GLU C  1 415 ? -22.722 15.049  -27.472 1.00 46.98 ? 432  GLU C CD  1 
ATOM   12154 O  OE1 . GLU C  1 415 ? -22.742 15.246  -26.239 1.00 46.88 ? 432  GLU C OE1 1 
ATOM   12155 O  OE2 . GLU C  1 415 ? -23.239 14.050  -28.013 1.00 48.96 ? 432  GLU C OE2 1 
ATOM   12156 N  N   . ALA C  1 416 ? -20.217 20.088  -27.000 1.00 35.98 ? 433  ALA C N   1 
ATOM   12157 C  CA  . ALA C  1 416 ? -20.311 21.374  -26.325 1.00 34.71 ? 433  ALA C CA  1 
ATOM   12158 C  C   . ALA C  1 416 ? -19.821 22.497  -27.237 1.00 32.51 ? 433  ALA C C   1 
ATOM   12159 O  O   . ALA C  1 416 ? -20.526 23.483  -27.442 1.00 32.71 ? 433  ALA C O   1 
ATOM   12160 C  CB  . ALA C  1 416 ? -19.532 21.339  -25.024 1.00 34.29 ? 433  ALA C CB  1 
ATOM   12161 N  N   . TYR C  1 417 ? -18.615 22.330  -27.786 1.00 32.27 ? 434  TYR C N   1 
ATOM   12162 C  CA  . TYR C  1 417 ? -17.998 23.352  -28.617 1.00 35.19 ? 434  TYR C CA  1 
ATOM   12163 C  C   . TYR C  1 417 ? -18.760 23.509  -29.937 1.00 35.96 ? 434  TYR C C   1 
ATOM   12164 O  O   . TYR C  1 417 ? -18.967 24.637  -30.381 1.00 36.45 ? 434  TYR C O   1 
ATOM   12165 C  CB  . TYR C  1 417 ? -16.509 23.037  -28.814 1.00 34.74 ? 434  TYR C CB  1 
ATOM   12166 C  CG  . TYR C  1 417 ? -15.641 23.279  -27.586 1.00 35.21 ? 434  TYR C CG  1 
ATOM   12167 C  CD1 . TYR C  1 417 ? -15.628 24.513  -26.940 1.00 36.62 ? 434  TYR C CD1 1 
ATOM   12168 C  CD2 . TYR C  1 417 ? -14.861 22.262  -27.046 1.00 35.02 ? 434  TYR C CD2 1 
ATOM   12169 C  CE1 . TYR C  1 417 ? -14.850 24.732  -25.812 1.00 35.70 ? 434  TYR C CE1 1 
ATOM   12170 C  CE2 . TYR C  1 417 ? -14.089 22.467  -25.914 1.00 35.65 ? 434  TYR C CE2 1 
ATOM   12171 C  CZ  . TYR C  1 417 ? -14.082 23.704  -25.293 1.00 36.26 ? 434  TYR C CZ  1 
ATOM   12172 O  OH  . TYR C  1 417 ? -13.313 23.906  -24.179 1.00 34.54 ? 434  TYR C OH  1 
ATOM   12173 N  N   . THR C  1 418 ? -19.186 22.397  -30.557 1.00 37.51 ? 435  THR C N   1 
ATOM   12174 C  CA  . THR C  1 418 ? -19.768 22.457  -31.894 1.00 36.65 ? 435  THR C CA  1 
ATOM   12175 C  C   . THR C  1 418 ? -21.162 23.075  -31.835 1.00 36.19 ? 435  THR C C   1 
ATOM   12176 O  O   . THR C  1 418 ? -21.487 23.916  -32.669 1.00 36.23 ? 435  THR C O   1 
ATOM   12177 C  CB  . THR C  1 418 ? -19.800 21.088  -32.574 1.00 37.95 ? 435  THR C CB  1 
ATOM   12178 O  OG1 . THR C  1 418 ? -20.534 20.196  -31.739 1.00 40.35 ? 435  THR C OG1 1 
ATOM   12179 C  CG2 . THR C  1 418 ? -18.409 20.543  -32.843 1.00 38.17 ? 435  THR C CG2 1 
ATOM   12180 N  N   . LEU C  1 419 ? -21.971 22.676  -30.843 1.00 35.00 ? 436  LEU C N   1 
ATOM   12181 C  CA  . LEU C  1 419 ? -23.361 23.104  -30.775 1.00 36.19 ? 436  LEU C CA  1 
ATOM   12182 C  C   . LEU C  1 419 ? -23.498 24.524  -30.211 1.00 36.24 ? 436  LEU C C   1 
ATOM   12183 O  O   . LEU C  1 419 ? -24.566 25.118  -30.341 1.00 36.00 ? 436  LEU C O   1 
ATOM   12184 C  CB  . LEU C  1 419 ? -24.185 22.089  -29.982 1.00 35.65 ? 436  LEU C CB  1 
ATOM   12185 C  CG  . LEU C  1 419 ? -24.401 20.734  -30.667 1.00 37.17 ? 436  LEU C CG  1 
ATOM   12186 C  CD1 . LEU C  1 419 ? -24.853 19.672  -29.692 1.00 36.70 ? 436  LEU C CD1 1 
ATOM   12187 C  CD2 . LEU C  1 419 ? -25.409 20.850  -31.797 1.00 39.24 ? 436  LEU C CD2 1 
ATOM   12188 N  N   . THR C  1 420 ? -22.442 25.070  -29.589 1.00 35.56 ? 437  THR C N   1 
ATOM   12189 C  CA  . THR C  1 420 ? -22.452 26.461  -29.144 1.00 34.88 ? 437  THR C CA  1 
ATOM   12190 C  C   . THR C  1 420 ? -21.565 27.314  -30.048 1.00 36.35 ? 437  THR C C   1 
ATOM   12191 O  O   . THR C  1 420 ? -21.404 28.506  -29.794 1.00 37.48 ? 437  THR C O   1 
ATOM   12192 C  CB  . THR C  1 420 ? -22.000 26.584  -27.687 1.00 32.95 ? 437  THR C CB  1 
ATOM   12193 O  OG1 . THR C  1 420 ? -20.620 26.226  -27.678 1.00 32.06 ? 437  THR C OG1 1 
ATOM   12194 C  CG2 . THR C  1 420 ? -22.822 25.724  -26.746 1.00 32.44 ? 437  THR C CG2 1 
ATOM   12195 N  N   . GLU C  1 421 ? -20.980 26.693  -31.081 1.00 39.41 ? 438  GLU C N   1 
ATOM   12196 C  CA  . GLU C  1 421 ? -20.212 27.392  -32.100 1.00 41.78 ? 438  GLU C CA  1 
ATOM   12197 C  C   . GLU C  1 421 ? -18.955 28.007  -31.485 1.00 39.18 ? 438  GLU C C   1 
ATOM   12198 O  O   . GLU C  1 421 ? -18.515 29.078  -31.899 1.00 38.79 ? 438  GLU C O   1 
ATOM   12199 C  CB  . GLU C  1 421 ? -21.100 28.415  -32.812 1.00 46.47 ? 438  GLU C CB  1 
ATOM   12200 C  CG  . GLU C  1 421 ? -22.365 27.798  -33.401 1.00 50.95 ? 438  GLU C CG  1 
ATOM   12201 C  CD  . GLU C  1 421 ? -23.417 28.812  -33.805 1.00 57.58 ? 438  GLU C CD  1 
ATOM   12202 O  OE1 . GLU C  1 421 ? -23.893 29.552  -32.913 1.00 64.37 ? 438  GLU C OE1 1 
ATOM   12203 O  OE2 . GLU C  1 421 ? -23.760 28.857  -35.006 1.00 59.93 ? 438  GLU C OE2 1 
ATOM   12204 N  N   . GLY C  1 422 ? -18.377 27.305  -30.503 1.00 38.31 ? 439  GLY C N   1 
ATOM   12205 C  CA  . GLY C  1 422 ? -17.099 27.675  -29.914 1.00 35.70 ? 439  GLY C CA  1 
ATOM   12206 C  C   . GLY C  1 422 ? -17.234 28.744  -28.831 1.00 33.97 ? 439  GLY C C   1 
ATOM   12207 O  O   . GLY C  1 422 ? -16.234 29.334  -28.424 1.00 34.90 ? 439  GLY C O   1 
ATOM   12208 N  N   . ARG C  1 423 ? -18.466 28.985  -28.365 1.00 32.01 ? 440  ARG C N   1 
ATOM   12209 C  CA  . ARG C  1 423 ? -18.738 30.064  -27.429 1.00 31.34 ? 440  ARG C CA  1 
ATOM   12210 C  C   . ARG C  1 423 ? -18.767 29.558  -25.986 1.00 31.04 ? 440  ARG C C   1 
ATOM   12211 O  O   . ARG C  1 423 ? -18.596 30.350  -25.061 1.00 29.05 ? 440  ARG C O   1 
ATOM   12212 C  CB  . ARG C  1 423 ? -20.038 30.784  -27.807 1.00 32.32 ? 440  ARG C CB  1 
ATOM   12213 C  CG  . ARG C  1 423 ? -19.916 31.606  -29.083 1.00 32.68 ? 440  ARG C CG  1 
ATOM   12214 C  CD  . ARG C  1 423 ? -21.073 32.576  -29.274 1.00 33.52 ? 440  ARG C CD  1 
ATOM   12215 N  NE  . ARG C  1 423 ? -22.329 31.917  -29.651 1.00 34.54 ? 440  ARG C NE  1 
ATOM   12216 C  CZ  . ARG C  1 423 ? -23.436 31.834  -28.915 1.00 37.36 ? 440  ARG C CZ  1 
ATOM   12217 N  NH1 . ARG C  1 423 ? -23.452 32.256  -27.661 1.00 36.91 ? 440  ARG C NH1 1 
ATOM   12218 N  NH2 . ARG C  1 423 ? -24.532 31.305  -29.433 1.00 37.65 ? 440  ARG C NH2 1 
ATOM   12219 N  N   . CYS C  1 424 ? -18.965 28.250  -25.780 1.00 30.42 ? 441  CYS C N   1 
ATOM   12220 C  CA  . CYS C  1 424 ? -19.110 27.729  -24.428 1.00 31.98 ? 441  CYS C CA  1 
ATOM   12221 C  C   . CYS C  1 424 ? -17.766 27.742  -23.700 1.00 32.18 ? 441  CYS C C   1 
ATOM   12222 O  O   . CYS C  1 424 ? -16.714 27.619  -24.326 1.00 32.08 ? 441  CYS C O   1 
ATOM   12223 C  CB  . CYS C  1 424 ? -19.715 26.331  -24.429 1.00 33.14 ? 441  CYS C CB  1 
ATOM   12224 S  SG  . CYS C  1 424 ? -18.637 25.081  -25.170 1.00 35.76 ? 441  CYS C SG  1 
ATOM   12225 N  N   . LEU C  1 425 ? -17.820 27.949  -22.376 1.00 32.53 ? 442  LEU C N   1 
ATOM   12226 C  CA  . LEU C  1 425 ? -16.701 27.684  -21.486 1.00 31.75 ? 442  LEU C CA  1 
ATOM   12227 C  C   . LEU C  1 425 ? -16.960 26.336  -20.822 1.00 29.71 ? 442  LEU C C   1 
ATOM   12228 O  O   . LEU C  1 425 ? -17.915 26.188  -20.060 1.00 25.98 ? 442  LEU C O   1 
ATOM   12229 C  CB  . LEU C  1 425 ? -16.536 28.803  -20.458 1.00 34.99 ? 442  LEU C CB  1 
ATOM   12230 C  CG  . LEU C  1 425 ? -16.216 30.189  -21.030 1.00 36.96 ? 442  LEU C CG  1 
ATOM   12231 C  CD1 . LEU C  1 425 ? -16.430 31.276  -19.988 1.00 38.35 ? 442  LEU C CD1 1 
ATOM   12232 C  CD2 . LEU C  1 425 ? -14.797 30.244  -21.567 1.00 37.55 ? 442  LEU C CD2 1 
ATOM   12233 N  N   . PHE C  1 426 ? -16.121 25.350  -21.160 1.00 29.22 ? 443  PHE C N   1 
ATOM   12234 C  CA  . PHE C  1 426 ? -16.425 23.954  -20.896 1.00 28.85 ? 443  PHE C CA  1 
ATOM   12235 C  C   . PHE C  1 426 ? -15.343 23.336  -20.014 1.00 28.74 ? 443  PHE C C   1 
ATOM   12236 O  O   . PHE C  1 426 ? -14.163 23.666  -20.130 1.00 29.51 ? 443  PHE C O   1 
ATOM   12237 C  CB  . PHE C  1 426 ? -16.565 23.178  -22.212 1.00 29.14 ? 443  PHE C CB  1 
ATOM   12238 C  CG  . PHE C  1 426 ? -16.854 21.694  -22.028 1.00 28.73 ? 443  PHE C CG  1 
ATOM   12239 C  CD1 . PHE C  1 426 ? -18.152 21.243  -21.820 1.00 28.55 ? 443  PHE C CD1 1 
ATOM   12240 C  CD2 . PHE C  1 426 ? -15.824 20.758  -22.039 1.00 29.45 ? 443  PHE C CD2 1 
ATOM   12241 C  CE1 . PHE C  1 426 ? -18.414 19.894  -21.643 1.00 29.45 ? 443  PHE C CE1 1 
ATOM   12242 C  CE2 . PHE C  1 426 ? -16.091 19.410  -21.854 1.00 28.96 ? 443  PHE C CE2 1 
ATOM   12243 C  CZ  . PHE C  1 426 ? -17.383 18.979  -21.656 1.00 28.97 ? 443  PHE C CZ  1 
ATOM   12244 N  N   . ALA C  1 427 ? -15.784 22.441  -19.125 1.00 28.21 ? 444  ALA C N   1 
ATOM   12245 C  CA  . ALA C  1 427 ? -14.892 21.584  -18.364 1.00 28.93 ? 444  ALA C CA  1 
ATOM   12246 C  C   . ALA C  1 427 ? -15.595 20.257  -18.102 1.00 27.93 ? 444  ALA C C   1 
ATOM   12247 O  O   . ALA C  1 427 ? -16.821 20.193  -18.084 1.00 26.02 ? 444  ALA C O   1 
ATOM   12248 C  CB  . ALA C  1 427 ? -14.478 22.256  -17.072 1.00 29.66 ? 444  ALA C CB  1 
ATOM   12249 N  N   . SER C  1 428 ? -14.794 19.207  -17.887 1.00 29.09 ? 445  SER C N   1 
ATOM   12250 C  CA  . SER C  1 428 ? -15.308 17.862  -17.721 1.00 29.69 ? 445  SER C CA  1 
ATOM   12251 C  C   . SER C  1 428 ? -14.604 17.179  -16.555 1.00 30.15 ? 445  SER C C   1 
ATOM   12252 O  O   . SER C  1 428 ? -13.548 17.624  -16.114 1.00 30.07 ? 445  SER C O   1 
ATOM   12253 C  CB  . SER C  1 428 ? -15.132 17.059  -18.992 1.00 30.54 ? 445  SER C CB  1 
ATOM   12254 O  OG  . SER C  1 428 ? -13.762 17.013  -19.377 1.00 30.76 ? 445  SER C OG  1 
ATOM   12255 N  N   . GLY C  1 429 ? -15.209 16.091  -16.075 1.00 32.30 ? 446  GLY C N   1 
ATOM   12256 C  CA  . GLY C  1 429 ? -14.574 15.222  -15.101 1.00 34.60 ? 446  GLY C CA  1 
ATOM   12257 C  C   . GLY C  1 429 ? -13.671 14.200  -15.788 1.00 37.52 ? 446  GLY C C   1 
ATOM   12258 O  O   . GLY C  1 429 ? -12.625 13.843  -15.255 1.00 39.63 ? 446  GLY C O   1 
ATOM   12259 N  N   . SER C  1 430 ? -14.102 13.729  -16.967 1.00 38.59 ? 447  SER C N   1 
ATOM   12260 C  CA  . SER C  1 430 ? -13.377 12.717  -17.719 1.00 43.26 ? 447  SER C CA  1 
ATOM   12261 C  C   . SER C  1 430 ? -12.537 13.371  -18.814 1.00 43.63 ? 447  SER C C   1 
ATOM   12262 O  O   . SER C  1 430 ? -12.906 14.416  -19.347 1.00 43.61 ? 447  SER C O   1 
ATOM   12263 C  CB  . SER C  1 430 ? -14.326 11.693  -18.287 1.00 45.26 ? 447  SER C CB  1 
ATOM   12264 O  OG  . SER C  1 430 ? -15.327 12.308  -19.087 1.00 48.30 ? 447  SER C OG  1 
ATOM   12265 N  N   . PRO C  1 431 ? -11.384 12.771  -19.193 1.00 45.43 ? 448  PRO C N   1 
ATOM   12266 C  CA  . PRO C  1 431 ? -10.442 13.425  -20.103 1.00 47.21 ? 448  PRO C CA  1 
ATOM   12267 C  C   . PRO C  1 431 ? -10.941 13.481  -21.545 1.00 44.71 ? 448  PRO C C   1 
ATOM   12268 O  O   . PRO C  1 431 ? -11.362 12.470  -22.101 1.00 44.54 ? 448  PRO C O   1 
ATOM   12269 C  CB  . PRO C  1 431 ? -9.174  12.560  -19.951 1.00 48.15 ? 448  PRO C CB  1 
ATOM   12270 C  CG  . PRO C  1 431 ? -9.705  11.180  -19.625 1.00 47.80 ? 448  PRO C CG  1 
ATOM   12271 C  CD  . PRO C  1 431 ? -10.938 11.431  -18.773 1.00 47.03 ? 448  PRO C CD  1 
ATOM   12272 N  N   . PHE C  1 432 ? -10.909 14.684  -22.130 1.00 43.32 ? 449  PHE C N   1 
ATOM   12273 C  CA  . PHE C  1 432 ? -11.220 14.867  -23.538 1.00 42.01 ? 449  PHE C CA  1 
ATOM   12274 C  C   . PHE C  1 432 ? -10.035 15.547  -24.215 1.00 43.27 ? 449  PHE C C   1 
ATOM   12275 O  O   . PHE C  1 432 ? -9.402  16.430  -23.636 1.00 44.00 ? 449  PHE C O   1 
ATOM   12276 C  CB  . PHE C  1 432 ? -12.504 15.677  -23.735 1.00 42.45 ? 449  PHE C CB  1 
ATOM   12277 C  CG  . PHE C  1 432 ? -13.776 14.970  -23.289 1.00 40.90 ? 449  PHE C CG  1 
ATOM   12278 C  CD1 . PHE C  1 432 ? -14.315 13.930  -24.039 1.00 40.14 ? 449  PHE C CD1 1 
ATOM   12279 C  CD2 . PHE C  1 432 ? -14.447 15.366  -22.135 1.00 40.40 ? 449  PHE C CD2 1 
ATOM   12280 C  CE1 . PHE C  1 432 ? -15.479 13.293  -23.633 1.00 39.44 ? 449  PHE C CE1 1 
ATOM   12281 C  CE2 . PHE C  1 432 ? -15.613 14.729  -21.738 1.00 38.17 ? 449  PHE C CE2 1 
ATOM   12282 C  CZ  . PHE C  1 432 ? -16.126 13.695  -22.486 1.00 39.02 ? 449  PHE C CZ  1 
ATOM   12283 N  N   . GLY C  1 433 ? -9.747  15.114  -25.448 1.00 45.41 ? 450  GLY C N   1 
ATOM   12284 C  CA  . GLY C  1 433 ? -8.670  15.681  -26.242 1.00 43.70 ? 450  GLY C CA  1 
ATOM   12285 C  C   . GLY C  1 433 ? -9.136  16.931  -26.983 1.00 44.29 ? 450  GLY C C   1 
ATOM   12286 O  O   . GLY C  1 433 ? -10.323 17.258  -26.971 1.00 41.84 ? 450  GLY C O   1 
ATOM   12287 N  N   . PRO C  1 434 ? -8.218  17.661  -27.654 1.00 45.14 ? 451  PRO C N   1 
ATOM   12288 C  CA  . PRO C  1 434 ? -8.583  18.886  -28.371 1.00 46.86 ? 451  PRO C CA  1 
ATOM   12289 C  C   . PRO C  1 434 ? -9.765  18.724  -29.329 1.00 46.79 ? 451  PRO C C   1 
ATOM   12290 O  O   . PRO C  1 434 ? -10.027 17.630  -29.829 1.00 46.83 ? 451  PRO C O   1 
ATOM   12291 C  CB  . PRO C  1 434 ? -7.278  19.249  -29.111 1.00 47.32 ? 451  PRO C CB  1 
ATOM   12292 C  CG  . PRO C  1 434 ? -6.184  18.640  -28.260 1.00 46.18 ? 451  PRO C CG  1 
ATOM   12293 C  CD  . PRO C  1 434 ? -6.783  17.346  -27.746 1.00 44.83 ? 451  PRO C CD  1 
ATOM   12294 N  N   . VAL C  1 435 ? -10.489 19.828  -29.552 1.00 45.47 ? 452  VAL C N   1 
ATOM   12295 C  CA  . VAL C  1 435 ? -11.599 19.858  -30.491 1.00 47.03 ? 452  VAL C CA  1 
ATOM   12296 C  C   . VAL C  1 435 ? -11.278 20.893  -31.567 1.00 48.36 ? 452  VAL C C   1 
ATOM   12297 O  O   . VAL C  1 435 ? -11.081 22.070  -31.263 1.00 46.49 ? 452  VAL C O   1 
ATOM   12298 C  CB  . VAL C  1 435 ? -12.940 20.162  -29.793 1.00 47.01 ? 452  VAL C CB  1 
ATOM   12299 C  CG1 . VAL C  1 435 ? -14.088 20.322  -30.786 1.00 47.38 ? 452  VAL C CG1 1 
ATOM   12300 C  CG2 . VAL C  1 435 ? -13.289 19.104  -28.753 1.00 46.20 ? 452  VAL C CG2 1 
ATOM   12301 N  N   . LYS C  1 436 ? -11.201 20.429  -32.820 1.00 50.71 ? 453  LYS C N   1 
ATOM   12302 C  CA  . LYS C  1 436 ? -11.004 21.301  -33.965 1.00 53.62 ? 453  LYS C CA  1 
ATOM   12303 C  C   . LYS C  1 436 ? -12.353 21.520  -34.641 1.00 51.89 ? 453  LYS C C   1 
ATOM   12304 O  O   . LYS C  1 436 ? -13.007 20.563  -35.049 1.00 52.42 ? 453  LYS C O   1 
ATOM   12305 C  CB  . LYS C  1 436 ? -10.003 20.715  -34.968 1.00 57.05 ? 453  LYS C CB  1 
ATOM   12306 C  CG  . LYS C  1 436 ? -9.587  21.669  -36.085 1.00 59.71 ? 453  LYS C CG  1 
ATOM   12307 C  CD  . LYS C  1 436 ? -8.361  21.211  -36.867 1.00 62.47 ? 453  LYS C CD  1 
ATOM   12308 C  CE  . LYS C  1 436 ? -7.801  22.287  -37.746 1.00 65.55 ? 453  LYS C CE  1 
ATOM   12309 N  NZ  . LYS C  1 436 ? -6.533  21.882  -38.362 1.00 66.71 ? 453  LYS C NZ  1 
ATOM   12310 N  N   . LEU C  1 437 ? -12.771 22.785  -34.720 1.00 50.32 ? 454  LEU C N   1 
ATOM   12311 C  CA  . LEU C  1 437 ? -13.956 23.146  -35.476 1.00 51.96 ? 454  LEU C CA  1 
ATOM   12312 C  C   . LEU C  1 437 ? -13.548 23.307  -36.938 1.00 52.49 ? 454  LEU C C   1 
ATOM   12313 O  O   . LEU C  1 437 ? -12.371 23.502  -37.244 1.00 50.07 ? 454  LEU C O   1 
ATOM   12314 C  CB  . LEU C  1 437 ? -14.585 24.417  -34.907 1.00 51.58 ? 454  LEU C CB  1 
ATOM   12315 C  CG  . LEU C  1 437 ? -15.035 24.361  -33.442 1.00 50.72 ? 454  LEU C CG  1 
ATOM   12316 C  CD1 . LEU C  1 437 ? -15.619 25.705  -33.041 1.00 50.04 ? 454  LEU C CD1 1 
ATOM   12317 C  CD2 . LEU C  1 437 ? -16.037 23.246  -33.163 1.00 48.85 ? 454  LEU C CD2 1 
ATOM   12318 N  N   . THR C  1 438 ? -14.537 23.229  -37.832 1.00 53.19 ? 455  THR C N   1 
ATOM   12319 C  CA  . THR C  1 438 ? -14.289 23.262  -39.264 1.00 54.92 ? 455  THR C CA  1 
ATOM   12320 C  C   . THR C  1 438 ? -13.755 24.634  -39.679 1.00 54.90 ? 455  THR C C   1 
ATOM   12321 O  O   . THR C  1 438 ? -13.079 24.742  -40.699 1.00 56.49 ? 455  THR C O   1 
ATOM   12322 C  CB  . THR C  1 438 ? -15.570 22.884  -40.009 1.00 53.98 ? 455  THR C CB  1 
ATOM   12323 O  OG1 . THR C  1 438 ? -16.580 23.769  -39.534 1.00 55.36 ? 455  THR C OG1 1 
ATOM   12324 C  CG2 . THR C  1 438 ? -15.981 21.446  -39.750 1.00 53.41 ? 455  THR C CG2 1 
ATOM   12325 N  N   . ASP C  1 439 ? -14.029 25.670  -38.871 1.00 54.27 ? 456  ASP C N   1 
ATOM   12326 C  CA  . ASP C  1 439 ? -13.543 27.013  -39.154 1.00 55.38 ? 456  ASP C CA  1 
ATOM   12327 C  C   . ASP C  1 439 ? -12.068 27.169  -38.781 1.00 53.14 ? 456  ASP C C   1 
ATOM   12328 O  O   . ASP C  1 439 ? -11.512 28.248  -38.964 1.00 54.64 ? 456  ASP C O   1 
ATOM   12329 C  CB  . ASP C  1 439 ? -14.397 28.085  -38.488 1.00 56.86 ? 456  ASP C CB  1 
ATOM   12330 C  CG  . ASP C  1 439 ? -14.322 28.182  -36.969 1.00 58.63 ? 456  ASP C CG  1 
ATOM   12331 O  OD1 . ASP C  1 439 ? -13.748 27.269  -36.338 1.00 56.50 ? 456  ASP C OD1 1 
ATOM   12332 O  OD2 . ASP C  1 439 ? -14.824 29.189  -36.426 1.00 59.62 ? 456  ASP C OD2 1 
ATOM   12333 N  N   . GLY C  1 440 ? -11.447 26.118  -38.227 1.00 54.35 ? 457  GLY C N   1 
ATOM   12334 C  CA  . GLY C  1 440 ? -10.011 26.106  -37.981 1.00 55.03 ? 457  GLY C CA  1 
ATOM   12335 C  C   . GLY C  1 440 ? -9.652  26.175  -36.495 1.00 55.86 ? 457  GLY C C   1 
ATOM   12336 O  O   . GLY C  1 440 ? -8.572  25.732  -36.107 1.00 55.93 ? 457  GLY C O   1 
ATOM   12337 N  N   . ARG C  1 441 ? -10.546 26.731  -35.666 1.00 55.32 ? 458  ARG C N   1 
ATOM   12338 C  CA  . ARG C  1 441 ? -10.245 26.989  -34.263 1.00 54.60 ? 458  ARG C CA  1 
ATOM   12339 C  C   . ARG C  1 441 ? -10.071 25.679  -33.496 1.00 51.59 ? 458  ARG C C   1 
ATOM   12340 O  O   . ARG C  1 441 ? -10.818 24.727  -33.712 1.00 48.94 ? 458  ARG C O   1 
ATOM   12341 C  CB  . ARG C  1 441 ? -11.350 27.812  -33.590 1.00 53.63 ? 458  ARG C CB  1 
ATOM   12342 C  CG  . ARG C  1 441 ? -11.440 29.260  -34.051 1.00 54.07 ? 458  ARG C CG  1 
ATOM   12343 C  CD  . ARG C  1 441 ? -12.596 29.986  -33.381 1.00 52.94 ? 458  ARG C CD  1 
ATOM   12344 N  NE  . ARG C  1 441 ? -13.887 29.386  -33.740 1.00 53.59 ? 458  ARG C NE  1 
ATOM   12345 C  CZ  . ARG C  1 441 ? -15.065 29.685  -33.200 1.00 53.72 ? 458  ARG C CZ  1 
ATOM   12346 N  NH1 . ARG C  1 441 ? -15.151 30.562  -32.212 1.00 55.54 ? 458  ARG C NH1 1 
ATOM   12347 N  NH2 . ARG C  1 441 ? -16.158 29.088  -33.646 1.00 53.46 ? 458  ARG C NH2 1 
ATOM   12348 N  N   . VAL C  1 442 ? -9.086  25.661  -32.586 1.00 50.81 ? 459  VAL C N   1 
ATOM   12349 C  CA  . VAL C  1 442 ? -8.805  24.506  -31.746 1.00 49.86 ? 459  VAL C CA  1 
ATOM   12350 C  C   . VAL C  1 442 ? -9.077  24.879  -30.288 1.00 46.28 ? 459  VAL C C   1 
ATOM   12351 O  O   . VAL C  1 442 ? -8.582  25.897  -29.808 1.00 46.52 ? 459  VAL C O   1 
ATOM   12352 C  CB  . VAL C  1 442 ? -7.356  24.009  -31.929 1.00 50.83 ? 459  VAL C CB  1 
ATOM   12353 C  CG1 . VAL C  1 442 ? -7.094  22.724  -31.149 1.00 50.73 ? 459  VAL C CG1 1 
ATOM   12354 C  CG2 . VAL C  1 442 ? -6.998  23.811  -33.397 1.00 52.36 ? 459  VAL C CG2 1 
ATOM   12355 N  N   . PHE C  1 443 ? -9.853  24.035  -29.594 1.00 43.91 ? 460  PHE C N   1 
ATOM   12356 C  CA  . PHE C  1 443 ? -10.192 24.235  -28.191 1.00 42.48 ? 460  PHE C CA  1 
ATOM   12357 C  C   . PHE C  1 443 ? -9.609  23.094  -27.360 1.00 43.25 ? 460  PHE C C   1 
ATOM   12358 O  O   . PHE C  1 443 ? -9.842  21.927  -27.664 1.00 44.21 ? 460  PHE C O   1 
ATOM   12359 C  CB  . PHE C  1 443 ? -11.712 24.300  -28.007 1.00 41.31 ? 460  PHE C CB  1 
ATOM   12360 C  CG  . PHE C  1 443 ? -12.360 25.561  -28.563 1.00 41.57 ? 460  PHE C CG  1 
ATOM   12361 C  CD1 . PHE C  1 443 ? -12.498 26.697  -27.772 1.00 40.15 ? 460  PHE C CD1 1 
ATOM   12362 C  CD2 . PHE C  1 443 ? -12.822 25.612  -29.876 1.00 41.25 ? 460  PHE C CD2 1 
ATOM   12363 C  CE1 . PHE C  1 443 ? -13.081 27.849  -28.280 1.00 40.69 ? 460  PHE C CE1 1 
ATOM   12364 C  CE2 . PHE C  1 443 ? -13.406 26.768  -30.377 1.00 41.05 ? 460  PHE C CE2 1 
ATOM   12365 C  CZ  . PHE C  1 443 ? -13.532 27.883  -29.581 1.00 40.50 ? 460  PHE C CZ  1 
ATOM   12366 N  N   . THR C  1 444 ? -8.864  23.445  -26.303 1.00 42.20 ? 461  THR C N   1 
ATOM   12367 C  CA  . THR C  1 444 ? -8.294  22.466  -25.390 1.00 41.07 ? 461  THR C CA  1 
ATOM   12368 C  C   . THR C  1 444 ? -9.053  22.531  -24.064 1.00 39.68 ? 461  THR C C   1 
ATOM   12369 O  O   . THR C  1 444 ? -8.783  23.405  -23.242 1.00 37.95 ? 461  THR C O   1 
ATOM   12370 C  CB  . THR C  1 444 ? -6.801  22.744  -25.219 1.00 40.93 ? 461  THR C CB  1 
ATOM   12371 O  OG1 . THR C  1 444 ? -6.263  22.813  -26.538 1.00 43.33 ? 461  THR C OG1 1 
ATOM   12372 C  CG2 . THR C  1 444 ? -6.086  21.656  -24.436 1.00 40.05 ? 461  THR C CG2 1 
ATOM   12373 N  N   . PRO C  1 445 ? -10.037 21.629  -23.825 1.00 37.73 ? 462  PRO C N   1 
ATOM   12374 C  CA  . PRO C  1 445 ? -10.833 21.651  -22.595 1.00 37.01 ? 462  PRO C CA  1 
ATOM   12375 C  C   . PRO C  1 445 ? -10.110 21.065  -21.386 1.00 37.45 ? 462  PRO C C   1 
ATOM   12376 O  O   . PRO C  1 445 ? -9.381  20.084  -21.511 1.00 37.41 ? 462  PRO C O   1 
ATOM   12377 C  CB  . PRO C  1 445 ? -12.056 20.812  -22.984 1.00 36.70 ? 462  PRO C CB  1 
ATOM   12378 C  CG  . PRO C  1 445 ? -11.505 19.789  -23.949 1.00 36.84 ? 462  PRO C CG  1 
ATOM   12379 C  CD  . PRO C  1 445 ? -10.457 20.555  -24.741 1.00 37.90 ? 462  PRO C CD  1 
ATOM   12380 N  N   . GLY C  1 446 ? -10.335 21.676  -20.217 1.00 37.15 ? 463  GLY C N   1 
ATOM   12381 C  CA  . GLY C  1 446 ? -9.725  21.227  -18.977 1.00 36.72 ? 463  GLY C CA  1 
ATOM   12382 C  C   . GLY C  1 446 ? -10.548 20.131  -18.302 1.00 33.64 ? 463  GLY C C   1 
ATOM   12383 O  O   . GLY C  1 446 ? -11.755 20.025  -18.513 1.00 33.31 ? 463  GLY C O   1 
ATOM   12384 N  N   . GLN C  1 447 ? -9.861  19.328  -17.485 1.00 34.18 ? 464  GLN C N   1 
ATOM   12385 C  CA  . GLN C  1 447 ? -10.483 18.325  -16.638 1.00 34.14 ? 464  GLN C CA  1 
ATOM   12386 C  C   . GLN C  1 447 ? -10.425 18.809  -15.190 1.00 31.19 ? 464  GLN C C   1 
ATOM   12387 O  O   . GLN C  1 447 ? -9.353  19.153  -14.709 1.00 32.28 ? 464  GLN C O   1 
ATOM   12388 C  CB  . GLN C  1 447 ? -9.709  17.016  -16.802 1.00 36.79 ? 464  GLN C CB  1 
ATOM   12389 C  CG  . GLN C  1 447 ? -10.365 15.813  -16.131 1.00 38.52 ? 464  GLN C CG  1 
ATOM   12390 C  CD  . GLN C  1 447 ? -9.400  14.685  -15.827 1.00 39.74 ? 464  GLN C CD  1 
ATOM   12391 O  OE1 . GLN C  1 447 ? -8.176  14.829  -15.928 1.00 38.75 ? 464  GLN C OE1 1 
ATOM   12392 N  NE2 . GLN C  1 447 ? -9.947  13.550  -15.415 1.00 40.93 ? 464  GLN C NE2 1 
ATOM   12393 N  N   . GLY C  1 448 ? -11.572 18.839  -14.502 1.00 29.70 ? 465  GLY C N   1 
ATOM   12394 C  CA  . GLY C  1 448 ? -11.630 19.242  -13.103 1.00 29.06 ? 465  GLY C CA  1 
ATOM   12395 C  C   . GLY C  1 448 ? -11.302 18.078  -12.169 1.00 27.80 ? 465  GLY C C   1 
ATOM   12396 O  O   . GLY C  1 448 ? -12.173 17.584  -11.460 1.00 29.70 ? 465  GLY C O   1 
ATOM   12397 N  N   . ASN C  1 449 ? -10.028 17.670  -12.179 1.00 26.54 ? 466  ASN C N   1 
ATOM   12398 C  CA  . ASN C  1 449 ? -9.524  16.512  -11.458 1.00 25.98 ? 466  ASN C CA  1 
ATOM   12399 C  C   . ASN C  1 449 ? -9.249  16.892  -10.002 1.00 24.83 ? 466  ASN C C   1 
ATOM   12400 O  O   . ASN C  1 449 ? -8.610  17.903  -9.726  1.00 23.57 ? 466  ASN C O   1 
ATOM   12401 C  CB  . ASN C  1 449 ? -8.271  16.002  -12.165 1.00 27.18 ? 466  ASN C CB  1 
ATOM   12402 C  CG  . ASN C  1 449 ? -7.794  14.655  -11.675 1.00 29.07 ? 466  ASN C CG  1 
ATOM   12403 O  OD1 . ASN C  1 449 ? -7.699  14.415  -10.465 1.00 28.42 ? 466  ASN C OD1 1 
ATOM   12404 N  ND2 . ASN C  1 449 ? -7.462  13.769  -12.600 1.00 30.98 ? 466  ASN C ND2 1 
ATOM   12405 N  N   . ASN C  1 450 ? -9.707  16.057  -9.063  1.00 24.94 ? 467  ASN C N   1 
ATOM   12406 C  CA  . ASN C  1 450 ? -9.531  16.335  -7.645  1.00 24.19 ? 467  ASN C CA  1 
ATOM   12407 C  C   . ASN C  1 450 ? -8.053  16.441  -7.267  1.00 23.30 ? 467  ASN C C   1 
ATOM   12408 O  O   . ASN C  1 450 ? -7.727  17.057  -6.251  1.00 22.47 ? 467  ASN C O   1 
ATOM   12409 C  CB  . ASN C  1 450 ? -10.245 15.313  -6.769  1.00 25.80 ? 467  ASN C CB  1 
ATOM   12410 C  CG  . ASN C  1 450 ? -11.703 15.652  -6.581  1.00 26.44 ? 467  ASN C CG  1 
ATOM   12411 O  OD1 . ASN C  1 450 ? -12.305 16.318  -7.430  1.00 29.60 ? 467  ASN C OD1 1 
ATOM   12412 N  ND2 . ASN C  1 450 ? -12.287 15.207  -5.481  1.00 26.45 ? 467  ASN C ND2 1 
ATOM   12413 N  N   . VAL C  1 451 ? -7.150  15.887  -8.089  1.00 22.84 ? 468  VAL C N   1 
ATOM   12414 C  CA  . VAL C  1 451 ? -5.732  15.881  -7.754  1.00 23.06 ? 468  VAL C CA  1 
ATOM   12415 C  C   . VAL C  1 451 ? -5.155  17.301  -7.760  1.00 22.44 ? 468  VAL C C   1 
ATOM   12416 O  O   . VAL C  1 451 ? -4.085  17.528  -7.211  1.00 22.08 ? 468  VAL C O   1 
ATOM   12417 C  CB  . VAL C  1 451 ? -4.917  14.944  -8.667  1.00 23.51 ? 468  VAL C CB  1 
ATOM   12418 C  CG1 . VAL C  1 451 ? -4.687  15.544  -10.050 1.00 24.28 ? 468  VAL C CG1 1 
ATOM   12419 C  CG2 . VAL C  1 451 ? -3.588  14.556  -8.027  1.00 23.91 ? 468  VAL C CG2 1 
ATOM   12420 N  N   . TYR C  1 452 ? -5.851  18.271  -8.363  1.00 22.49 ? 469  TYR C N   1 
ATOM   12421 C  CA  . TYR C  1 452 ? -5.394  19.654  -8.340  1.00 22.56 ? 469  TYR C CA  1 
ATOM   12422 C  C   . TYR C  1 452 ? -5.377  20.220  -6.916  1.00 21.63 ? 469  TYR C C   1 
ATOM   12423 O  O   . TYR C  1 452 ? -4.633  21.155  -6.640  1.00 22.48 ? 469  TYR C O   1 
ATOM   12424 C  CB  . TYR C  1 452 ? -6.292  20.526  -9.223  1.00 23.92 ? 469  TYR C CB  1 
ATOM   12425 C  CG  . TYR C  1 452 ? -6.039  20.453  -10.723 1.00 24.86 ? 469  TYR C CG  1 
ATOM   12426 C  CD1 . TYR C  1 452 ? -4.789  20.743  -11.265 1.00 25.61 ? 469  TYR C CD1 1 
ATOM   12427 C  CD2 . TYR C  1 452 ? -7.055  20.090  -11.599 1.00 25.64 ? 469  TYR C CD2 1 
ATOM   12428 C  CE1 . TYR C  1 452 ? -4.565  20.685  -12.633 1.00 26.40 ? 469  TYR C CE1 1 
ATOM   12429 C  CE2 . TYR C  1 452 ? -6.841  20.023  -12.965 1.00 26.86 ? 469  TYR C CE2 1 
ATOM   12430 C  CZ  . TYR C  1 452 ? -5.594  20.325  -13.485 1.00 27.25 ? 469  TYR C CZ  1 
ATOM   12431 O  OH  . TYR C  1 452 ? -5.409  20.253  -14.835 1.00 28.93 ? 469  TYR C OH  1 
ATOM   12432 N  N   . ILE C  1 453 ? -6.204  19.671  -6.014  1.00 21.03 ? 470  ILE C N   1 
ATOM   12433 C  CA  . ILE C  1 453 ? -6.470  20.311  -4.736  1.00 20.95 ? 470  ILE C CA  1 
ATOM   12434 C  C   . ILE C  1 453 ? -5.844  19.537  -3.571  1.00 20.61 ? 470  ILE C C   1 
ATOM   12435 O  O   . ILE C  1 453 ? -5.114  20.137  -2.794  1.00 21.24 ? 470  ILE C O   1 
ATOM   12436 C  CB  . ILE C  1 453 ? -7.987  20.532  -4.565  1.00 20.75 ? 470  ILE C CB  1 
ATOM   12437 C  CG1 . ILE C  1 453 ? -8.515  21.565  -5.569  1.00 20.94 ? 470  ILE C CG1 1 
ATOM   12438 C  CG2 . ILE C  1 453 ? -8.349  20.920  -3.133  1.00 20.72 ? 470  ILE C CG2 1 
ATOM   12439 C  CD1 . ILE C  1 453 ? -8.046  22.989  -5.323  1.00 21.15 ? 470  ILE C CD1 1 
ATOM   12440 N  N   . PHE C  1 454 ? -6.117  18.230  -3.432  1.00 20.29 ? 471  PHE C N   1 
ATOM   12441 C  CA  . PHE C  1 454 ? -5.879  17.549  -2.164  1.00 20.99 ? 471  PHE C CA  1 
ATOM   12442 C  C   . PHE C  1 454 ? -4.388  17.467  -1.822  1.00 20.66 ? 471  PHE C C   1 
ATOM   12443 O  O   . PHE C  1 454 ? -4.048  17.626  -0.652  1.00 19.97 ? 471  PHE C O   1 
ATOM   12444 C  CB  . PHE C  1 454 ? -6.556  16.178  -2.034  1.00 21.17 ? 471  PHE C CB  1 
ATOM   12445 C  CG  . PHE C  1 454 ? -6.125  15.092  -3.009  1.00 21.40 ? 471  PHE C CG  1 
ATOM   12446 C  CD1 . PHE C  1 454 ? -4.964  14.356  -2.794  1.00 21.31 ? 471  PHE C CD1 1 
ATOM   12447 C  CD2 . PHE C  1 454 ? -6.899  14.789  -4.121  1.00 21.23 ? 471  PHE C CD2 1 
ATOM   12448 C  CE1 . PHE C  1 454 ? -4.578  13.371  -3.686  1.00 21.25 ? 471  PHE C CE1 1 
ATOM   12449 C  CE2 . PHE C  1 454 ? -6.509  13.796  -5.007  1.00 21.51 ? 471  PHE C CE2 1 
ATOM   12450 C  CZ  . PHE C  1 454 ? -5.347  13.095  -4.791  1.00 21.04 ? 471  PHE C CZ  1 
ATOM   12451 N  N   . PRO C  1 455 ? -3.437  17.244  -2.763  1.00 21.09 ? 472  PRO C N   1 
ATOM   12452 C  CA  . PRO C  1 455 ? -2.018  17.197  -2.390  1.00 21.76 ? 472  PRO C CA  1 
ATOM   12453 C  C   . PRO C  1 455 ? -1.524  18.473  -1.698  1.00 22.42 ? 472  PRO C C   1 
ATOM   12454 O  O   . PRO C  1 455 ? -0.956  18.412  -0.606  1.00 22.15 ? 472  PRO C O   1 
ATOM   12455 C  CB  . PRO C  1 455 ? -1.299  16.941  -3.728  1.00 21.59 ? 472  PRO C CB  1 
ATOM   12456 C  CG  . PRO C  1 455 ? -2.357  16.324  -4.614  1.00 21.71 ? 472  PRO C CG  1 
ATOM   12457 C  CD  . PRO C  1 455 ? -3.642  17.032  -4.206  1.00 21.49 ? 472  PRO C CD  1 
ATOM   12458 N  N   . GLY C  1 456 ? -1.776  19.625  -2.335  1.00 21.74 ? 473  GLY C N   1 
ATOM   12459 C  CA  . GLY C  1 456 ? -1.331  20.925  -1.850  1.00 21.18 ? 473  GLY C CA  1 
ATOM   12460 C  C   . GLY C  1 456 ? -1.954  21.295  -0.505  1.00 21.21 ? 473  GLY C C   1 
ATOM   12461 O  O   . GLY C  1 456 ? -1.262  21.795  0.383   1.00 21.15 ? 473  GLY C O   1 
ATOM   12462 N  N   . VAL C  1 457 ? -3.263  21.050  -0.359  1.00 20.82 ? 474  VAL C N   1 
ATOM   12463 C  CA  . VAL C  1 457 ? -3.947  21.328  0.892   1.00 20.66 ? 474  VAL C CA  1 
ATOM   12464 C  C   . VAL C  1 457 ? -3.347  20.446  1.990   1.00 20.04 ? 474  VAL C C   1 
ATOM   12465 O  O   . VAL C  1 457 ? -3.008  20.939  3.060   1.00 18.81 ? 474  VAL C O   1 
ATOM   12466 C  CB  . VAL C  1 457 ? -5.471  21.149  0.750   1.00 21.71 ? 474  VAL C CB  1 
ATOM   12467 C  CG1 . VAL C  1 457 ? -6.192  21.133  2.094   1.00 22.75 ? 474  VAL C CG1 1 
ATOM   12468 C  CG2 . VAL C  1 457 ? -6.060  22.224  -0.152  1.00 22.55 ? 474  VAL C CG2 1 
ATOM   12469 N  N   . ALA C  1 458 ? -3.188  19.148  1.718   1.00 19.45 ? 475  ALA C N   1 
ATOM   12470 C  CA  . ALA C  1 458 ? -2.669  18.241  2.733   1.00 19.71 ? 475  ALA C CA  1 
ATOM   12471 C  C   . ALA C  1 458 ? -1.289  18.702  3.197   1.00 19.17 ? 475  ALA C C   1 
ATOM   12472 O  O   . ALA C  1 458 ? -1.015  18.709  4.395   1.00 18.80 ? 475  ALA C O   1 
ATOM   12473 C  CB  . ALA C  1 458 ? -2.629  16.824  2.209   1.00 19.96 ? 475  ALA C CB  1 
ATOM   12474 N  N   . LEU C  1 459 ? -0.426  19.091  2.249   1.00 19.27 ? 476  LEU C N   1 
ATOM   12475 C  CA  . LEU C  1 459 ? 0.939   19.477  2.578   1.00 19.85 ? 476  LEU C CA  1 
ATOM   12476 C  C   . LEU C  1 459 ? 0.923   20.691  3.506   1.00 19.75 ? 476  LEU C C   1 
ATOM   12477 O  O   . LEU C  1 459 ? 1.618   20.704  4.514   1.00 19.67 ? 476  LEU C O   1 
ATOM   12478 C  CB  . LEU C  1 459 ? 1.771   19.759  1.326   1.00 20.29 ? 476  LEU C CB  1 
ATOM   12479 C  CG  . LEU C  1 459 ? 3.223   20.184  1.583   1.00 20.66 ? 476  LEU C CG  1 
ATOM   12480 C  CD1 . LEU C  1 459 ? 3.983   19.066  2.279   1.00 20.73 ? 476  LEU C CD1 1 
ATOM   12481 C  CD2 . LEU C  1 459 ? 3.948   20.601  0.317   1.00 20.22 ? 476  LEU C CD2 1 
ATOM   12482 N  N   . ALA C  1 460 ? 0.129   21.713  3.157   1.00 20.26 ? 477  ALA C N   1 
ATOM   12483 C  CA  . ALA C  1 460 ? 0.049   22.939  3.939   1.00 19.68 ? 477  ALA C CA  1 
ATOM   12484 C  C   . ALA C  1 460 ? -0.421  22.645  5.364   1.00 19.64 ? 477  ALA C C   1 
ATOM   12485 O  O   . ALA C  1 460 ? 0.169   23.128  6.323   1.00 18.51 ? 477  ALA C O   1 
ATOM   12486 C  CB  . ALA C  1 460 ? -0.875  23.924  3.256   1.00 20.15 ? 477  ALA C CB  1 
ATOM   12487 N  N   . VAL C  1 461 ? -1.498  21.860  5.491   1.00 19.78 ? 478  VAL C N   1 
ATOM   12488 C  CA  . VAL C  1 461 ? -2.055  21.521  6.790   1.00 19.93 ? 478  VAL C CA  1 
ATOM   12489 C  C   . VAL C  1 461 ? -0.993  20.835  7.654   1.00 19.29 ? 478  VAL C C   1 
ATOM   12490 O  O   . VAL C  1 461 ? -0.812  21.192  8.814   1.00 18.95 ? 478  VAL C O   1 
ATOM   12491 C  CB  . VAL C  1 461 ? -3.307  20.642  6.600   1.00 20.01 ? 478  VAL C CB  1 
ATOM   12492 C  CG1 . VAL C  1 461 ? -3.712  19.912  7.874   1.00 20.68 ? 478  VAL C CG1 1 
ATOM   12493 C  CG2 . VAL C  1 461 ? -4.473  21.456  6.059   1.00 20.14 ? 478  VAL C CG2 1 
ATOM   12494 N  N   . ILE C  1 462 ? -0.288  19.858  7.076   1.00 19.45 ? 479  ILE C N   1 
ATOM   12495 C  CA  . ILE C  1 462 ? 0.714   19.092  7.802   1.00 19.55 ? 479  ILE C CA  1 
ATOM   12496 C  C   . ILE C  1 462 ? 1.858   20.005  8.247   1.00 20.02 ? 479  ILE C C   1 
ATOM   12497 O  O   . ILE C  1 462 ? 2.230   19.990  9.423   1.00 19.40 ? 479  ILE C O   1 
ATOM   12498 C  CB  . ILE C  1 462 ? 1.200   17.895  6.965   1.00 20.05 ? 479  ILE C CB  1 
ATOM   12499 C  CG1 . ILE C  1 462 ? 0.103   16.837  6.841   1.00 20.35 ? 479  ILE C CG1 1 
ATOM   12500 C  CG2 . ILE C  1 462 ? 2.487   17.291  7.536   1.00 19.99 ? 479  ILE C CG2 1 
ATOM   12501 C  CD1 . ILE C  1 462 ? 0.311   15.841  5.718   1.00 21.30 ? 479  ILE C CD1 1 
ATOM   12502 N  N   . LEU C  1 463 ? 2.396   20.802  7.310   1.00 19.81 ? 480  LEU C N   1 
ATOM   12503 C  CA  . LEU C  1 463 ? 3.567   21.628  7.568   1.00 21.32 ? 480  LEU C CA  1 
ATOM   12504 C  C   . LEU C  1 463 ? 3.260   22.706  8.611   1.00 21.52 ? 480  LEU C C   1 
ATOM   12505 O  O   . LEU C  1 463 ? 4.161   23.129  9.334   1.00 20.51 ? 480  LEU C O   1 
ATOM   12506 C  CB  . LEU C  1 463 ? 4.097   22.239  6.269   1.00 21.71 ? 480  LEU C CB  1 
ATOM   12507 C  CG  . LEU C  1 463 ? 4.706   21.279  5.240   1.00 21.71 ? 480  LEU C CG  1 
ATOM   12508 C  CD1 . LEU C  1 463 ? 5.323   22.083  4.108   1.00 21.94 ? 480  LEU C CD1 1 
ATOM   12509 C  CD2 . LEU C  1 463 ? 5.742   20.323  5.802   1.00 21.83 ? 480  LEU C CD2 1 
ATOM   12510 N  N   . CYS C  1 464 ? 1.989   23.129  8.709   1.00 21.63 ? 481  CYS C N   1 
ATOM   12511 C  CA  . CYS C  1 464 ? 1.588   24.180  9.630   1.00 21.21 ? 481  CYS C CA  1 
ATOM   12512 C  C   . CYS C  1 464 ? 1.137   23.639  10.985  1.00 21.26 ? 481  CYS C C   1 
ATOM   12513 O  O   . CYS C  1 464 ? 0.760   24.429  11.848  1.00 21.89 ? 481  CYS C O   1 
ATOM   12514 C  CB  . CYS C  1 464 ? 0.447   25.005  9.045   1.00 21.87 ? 481  CYS C CB  1 
ATOM   12515 S  SG  . CYS C  1 464 ? 0.958   26.026  7.639   1.00 22.54 ? 481  CYS C SG  1 
ATOM   12516 N  N   . ASN C  1 465 ? 1.169   22.311  11.175  1.00 21.20 ? 482  ASN C N   1 
ATOM   12517 C  CA  . ASN C  1 465 ? 0.646   21.682  12.381  1.00 22.03 ? 482  ASN C CA  1 
ATOM   12518 C  C   . ASN C  1 465 ? -0.794  22.143  12.640  1.00 21.36 ? 482  ASN C C   1 
ATOM   12519 O  O   . ASN C  1 465 ? -1.184  22.357  13.788  1.00 21.48 ? 482  ASN C O   1 
ATOM   12520 C  CB  . ASN C  1 465 ? 1.546   21.920  13.594  1.00 22.57 ? 482  ASN C CB  1 
ATOM   12521 C  CG  . ASN C  1 465 ? 2.896   21.245  13.486  1.00 24.50 ? 482  ASN C CG  1 
ATOM   12522 O  OD1 . ASN C  1 465 ? 3.073   20.282  12.729  1.00 26.42 ? 482  ASN C OD1 1 
ATOM   12523 N  ND2 . ASN C  1 465 ? 3.866   21.722  14.250  1.00 25.28 ? 482  ASN C ND2 1 
ATOM   12524 N  N   . THR C  1 466 ? -1.579  22.267  11.561  1.00 20.53 ? 483  THR C N   1 
ATOM   12525 C  CA  . THR C  1 466 ? -2.979  22.662  11.628  1.00 20.58 ? 483  THR C CA  1 
ATOM   12526 C  C   . THR C  1 466 ? -3.788  21.524  12.248  1.00 20.87 ? 483  THR C C   1 
ATOM   12527 O  O   . THR C  1 466 ? -3.474  20.349  12.053  1.00 21.55 ? 483  THR C O   1 
ATOM   12528 C  CB  . THR C  1 466 ? -3.441  23.024  10.215  1.00 20.56 ? 483  THR C CB  1 
ATOM   12529 O  OG1 . THR C  1 466 ? -2.836  24.285  9.965   1.00 20.84 ? 483  THR C OG1 1 
ATOM   12530 C  CG2 . THR C  1 466 ? -4.943  23.195  10.076  1.00 20.31 ? 483  THR C CG2 1 
ATOM   12531 N  N   . ARG C  1 467 ? -4.839  21.884  12.990  1.00 21.32 ? 484  ARG C N   1 
ATOM   12532 C  CA  . ARG C  1 467 ? -5.577  20.930  13.803  1.00 21.58 ? 484  ARG C CA  1 
ATOM   12533 C  C   . ARG C  1 467 ? -7.004  20.719  13.299  1.00 21.74 ? 484  ARG C C   1 
ATOM   12534 O  O   . ARG C  1 467 ? -7.593  19.678  13.587  1.00 20.87 ? 484  ARG C O   1 
ATOM   12535 C  CB  . ARG C  1 467 ? -5.606  21.422  15.254  1.00 23.38 ? 484  ARG C CB  1 
ATOM   12536 C  CG  . ARG C  1 467 ? -4.217  21.537  15.861  1.00 25.06 ? 484  ARG C CG  1 
ATOM   12537 C  CD  . ARG C  1 467 ? -4.256  22.159  17.245  1.00 26.79 ? 484  ARG C CD  1 
ATOM   12538 N  NE  . ARG C  1 467 ? -4.708  21.211  18.267  1.00 27.43 ? 484  ARG C NE  1 
ATOM   12539 C  CZ  . ARG C  1 467 ? -3.948  20.279  18.834  1.00 28.55 ? 484  ARG C CZ  1 
ATOM   12540 N  NH1 . ARG C  1 467 ? -2.706  20.081  18.433  1.00 28.70 ? 484  ARG C NH1 1 
ATOM   12541 N  NH2 . ARG C  1 467 ? -4.438  19.538  19.808  1.00 29.07 ? 484  ARG C NH2 1 
ATOM   12542 N  N   . HIS C  1 468 ? -7.569  21.725  12.614  1.00 21.32 ? 485  HIS C N   1 
ATOM   12543 C  CA  . HIS C  1 468 ? -8.895  21.623  12.023  1.00 22.46 ? 485  HIS C CA  1 
ATOM   12544 C  C   . HIS C  1 468 ? -8.899  22.352  10.681  1.00 22.20 ? 485  HIS C C   1 
ATOM   12545 O  O   . HIS C  1 468 ? -8.204  23.357  10.514  1.00 22.06 ? 485  HIS C O   1 
ATOM   12546 C  CB  . HIS C  1 468 ? -9.973  22.153  12.979  1.00 23.29 ? 485  HIS C CB  1 
ATOM   12547 C  CG  . HIS C  1 468 ? -9.894  21.584  14.358  1.00 23.89 ? 485  HIS C CG  1 
ATOM   12548 N  ND1 . HIS C  1 468 ? -10.140 20.255  14.641  1.00 23.14 ? 485  HIS C ND1 1 
ATOM   12549 C  CD2 . HIS C  1 468 ? -9.534  22.155  15.525  1.00 23.88 ? 485  HIS C CD2 1 
ATOM   12550 C  CE1 . HIS C  1 468 ? -9.957  20.050  15.942  1.00 24.13 ? 485  HIS C CE1 1 
ATOM   12551 N  NE2 . HIS C  1 468 ? -9.584  21.188  16.497  1.00 23.09 ? 485  HIS C NE2 1 
ATOM   12552 N  N   . ILE C  1 469 ? -9.674  21.813  9.730   1.00 21.45 ? 486  ILE C N   1 
ATOM   12553 C  CA  . ILE C  1 469 ? -9.718  22.316  8.368   1.00 21.18 ? 486  ILE C CA  1 
ATOM   12554 C  C   . ILE C  1 469 ? -11.110 22.889  8.100   1.00 21.78 ? 486  ILE C C   1 
ATOM   12555 O  O   . ILE C  1 469 ? -12.073 22.146  7.930   1.00 21.47 ? 486  ILE C O   1 
ATOM   12556 C  CB  . ILE C  1 469 ? -9.336  21.212  7.367   1.00 21.37 ? 486  ILE C CB  1 
ATOM   12557 C  CG1 . ILE C  1 469 ? -8.026  20.506  7.778   1.00 21.32 ? 486  ILE C CG1 1 
ATOM   12558 C  CG2 . ILE C  1 469 ? -9.256  21.778  5.951   1.00 21.31 ? 486  ILE C CG2 1 
ATOM   12559 C  CD1 . ILE C  1 469 ? -7.718  19.252  6.982   1.00 22.07 ? 486  ILE C CD1 1 
ATOM   12560 N  N   . SER C  1 470 ? -11.199 24.223  8.075   1.00 22.26 ? 487  SER C N   1 
ATOM   12561 C  CA  . SER C  1 470 ? -12.437 24.919  7.770   1.00 23.35 ? 487  SER C CA  1 
ATOM   12562 C  C   . SER C  1 470 ? -12.711 24.843  6.270   1.00 23.40 ? 487  SER C C   1 
ATOM   12563 O  O   . SER C  1 470 ? -11.796 24.635  5.478   1.00 21.21 ? 487  SER C O   1 
ATOM   12564 C  CB  . SER C  1 470 ? -12.365 26.350  8.215   1.00 24.83 ? 487  SER C CB  1 
ATOM   12565 O  OG  . SER C  1 470 ? -11.378 27.041  7.458   1.00 27.06 ? 487  SER C OG  1 
ATOM   12566 N  N   . ASP C  1 471 ? -13.975 25.055  5.885   1.00 24.31 ? 488  ASP C N   1 
ATOM   12567 C  CA  . ASP C  1 471 ? -14.335 25.110  4.477   1.00 25.55 ? 488  ASP C CA  1 
ATOM   12568 C  C   . ASP C  1 471 ? -13.604 26.265  3.790   1.00 24.51 ? 488  ASP C C   1 
ATOM   12569 O  O   . ASP C  1 471 ? -13.363 26.211  2.587   1.00 24.47 ? 488  ASP C O   1 
ATOM   12570 C  CB  . ASP C  1 471 ? -15.843 25.174  4.285   1.00 28.03 ? 488  ASP C CB  1 
ATOM   12571 C  CG  . ASP C  1 471 ? -16.586 23.848  4.416   1.00 29.92 ? 488  ASP C CG  1 
ATOM   12572 O  OD1 . ASP C  1 471 ? -15.924 22.783  4.444   1.00 30.63 ? 488  ASP C OD1 1 
ATOM   12573 O  OD2 . ASP C  1 471 ? -17.829 23.885  4.491   1.00 33.46 ? 488  ASP C OD2 1 
ATOM   12574 N  N   . SER C  1 472 ? -13.252 27.310  4.551   1.00 23.27 ? 489  SER C N   1 
ATOM   12575 C  CA  . SER C  1 472 ? -12.584 28.471  3.985   1.00 23.23 ? 489  SER C CA  1 
ATOM   12576 C  C   . SER C  1 472 ? -11.192 28.111  3.461   1.00 22.06 ? 489  SER C C   1 
ATOM   12577 O  O   . SER C  1 472 ? -10.677 28.790  2.578   1.00 21.23 ? 489  SER C O   1 
ATOM   12578 C  CB  . SER C  1 472 ? -12.542 29.620  4.970   1.00 24.46 ? 489  SER C CB  1 
ATOM   12579 O  OG  . SER C  1 472 ? -11.779 29.301  6.124   1.00 26.18 ? 489  SER C OG  1 
ATOM   12580 N  N   . VAL C  1 473 ? -10.594 27.026  3.971   1.00 20.95 ? 490  VAL C N   1 
ATOM   12581 C  CA  . VAL C  1 473 ? -9.319  26.550  3.452   1.00 21.07 ? 490  VAL C CA  1 
ATOM   12582 C  C   . VAL C  1 473 ? -9.496  26.099  2.003   1.00 21.73 ? 490  VAL C C   1 
ATOM   12583 O  O   . VAL C  1 473 ? -8.623  26.347  1.176   1.00 22.83 ? 490  VAL C O   1 
ATOM   12584 C  CB  . VAL C  1 473 ? -8.743  25.421  4.332   1.00 22.30 ? 490  VAL C CB  1 
ATOM   12585 C  CG1 . VAL C  1 473 ? -7.572  24.700  3.673   1.00 22.35 ? 490  VAL C CG1 1 
ATOM   12586 C  CG2 . VAL C  1 473 ? -8.343  25.943  5.706   1.00 22.50 ? 490  VAL C CG2 1 
ATOM   12587 N  N   . PHE C  1 474 ? -10.627 25.439  1.708   1.00 21.12 ? 491  PHE C N   1 
ATOM   12588 C  CA  . PHE C  1 474 ? -10.902 24.927  0.373   1.00 21.85 ? 491  PHE C CA  1 
ATOM   12589 C  C   . PHE C  1 474 ? -11.250 26.069  -0.579  1.00 22.29 ? 491  PHE C C   1 
ATOM   12590 O  O   . PHE C  1 474 ? -10.972 25.970  -1.769  1.00 22.93 ? 491  PHE C O   1 
ATOM   12591 C  CB  . PHE C  1 474 ? -11.996 23.855  0.405   1.00 21.47 ? 491  PHE C CB  1 
ATOM   12592 C  CG  . PHE C  1 474 ? -11.480 22.572  1.029   1.00 21.51 ? 491  PHE C CG  1 
ATOM   12593 C  CD1 . PHE C  1 474 ? -10.702 21.688  0.288   1.00 21.57 ? 491  PHE C CD1 1 
ATOM   12594 C  CD2 . PHE C  1 474 ? -11.723 22.285  2.370   1.00 21.32 ? 491  PHE C CD2 1 
ATOM   12595 C  CE1 . PHE C  1 474 ? -10.199 20.535  0.869   1.00 21.48 ? 491  PHE C CE1 1 
ATOM   12596 C  CE2 . PHE C  1 474 ? -11.219 21.130  2.944   1.00 21.57 ? 491  PHE C CE2 1 
ATOM   12597 C  CZ  . PHE C  1 474 ? -10.462 20.259  2.193   1.00 21.55 ? 491  PHE C CZ  1 
ATOM   12598 N  N   . LEU C  1 475 ? -11.847 27.146  -0.058  1.00 23.54 ? 492  LEU C N   1 
ATOM   12599 C  CA  . LEU C  1 475 ? -12.104 28.330  -0.866  1.00 24.13 ? 492  LEU C CA  1 
ATOM   12600 C  C   . LEU C  1 475 ? -10.774 28.961  -1.287  1.00 24.50 ? 492  LEU C C   1 
ATOM   12601 O  O   . LEU C  1 475 ? -10.589 29.330  -2.447  1.00 22.20 ? 492  LEU C O   1 
ATOM   12602 C  CB  . LEU C  1 475 ? -12.990 29.294  -0.074  1.00 25.09 ? 492  LEU C CB  1 
ATOM   12603 C  CG  . LEU C  1 475 ? -13.283 30.651  -0.720  1.00 25.66 ? 492  LEU C CG  1 
ATOM   12604 C  CD1 . LEU C  1 475 ? -13.861 30.511  -2.117  1.00 26.53 ? 492  LEU C CD1 1 
ATOM   12605 C  CD2 . LEU C  1 475 ? -14.228 31.448  0.160   1.00 26.99 ? 492  LEU C CD2 1 
ATOM   12606 N  N   . GLU C  1 476 ? -9.831  29.057  -0.342  1.00 24.86 ? 493  GLU C N   1 
ATOM   12607 C  CA  . GLU C  1 476 ? -8.508  29.602  -0.620  1.00 25.75 ? 493  GLU C CA  1 
ATOM   12608 C  C   . GLU C  1 476 ? -7.767  28.738  -1.643  1.00 24.43 ? 493  GLU C C   1 
ATOM   12609 O  O   . GLU C  1 476 ? -7.078  29.262  -2.517  1.00 25.41 ? 493  GLU C O   1 
ATOM   12610 C  CB  . GLU C  1 476 ? -7.684  29.729  0.664   1.00 28.56 ? 493  GLU C CB  1 
ATOM   12611 C  CG  . GLU C  1 476 ? -6.262  30.236  0.432   1.00 30.44 ? 493  GLU C CG  1 
ATOM   12612 C  CD  . GLU C  1 476 ? -6.168  31.613  -0.210  1.00 33.90 ? 493  GLU C CD  1 
ATOM   12613 O  OE1 . GLU C  1 476 ? -5.087  31.919  -0.757  1.00 36.88 ? 493  GLU C OE1 1 
ATOM   12614 O  OE2 . GLU C  1 476 ? -7.152  32.386  -0.151  1.00 34.61 ? 493  GLU C OE2 1 
ATOM   12615 N  N   . ALA C  1 477 ? -7.890  27.413  -1.521  1.00 23.17 ? 494  ALA C N   1 
ATOM   12616 C  CA  . ALA C  1 477 ? -7.232  26.492  -2.438  1.00 22.96 ? 494  ALA C CA  1 
ATOM   12617 C  C   . ALA C  1 477 ? -7.770  26.670  -3.859  1.00 22.10 ? 494  ALA C C   1 
ATOM   12618 O  O   . ALA C  1 477 ? -7.009  26.640  -4.826  1.00 20.77 ? 494  ALA C O   1 
ATOM   12619 C  CB  . ALA C  1 477 ? -7.413  25.067  -1.957  1.00 22.42 ? 494  ALA C CB  1 
ATOM   12620 N  N   . ALA C  1 478 ? -9.090  26.828  -3.979  1.00 21.98 ? 495  ALA C N   1 
ATOM   12621 C  CA  . ALA C  1 478 ? -9.725  27.062  -5.270  1.00 22.74 ? 495  ALA C CA  1 
ATOM   12622 C  C   . ALA C  1 478 ? -9.169  28.326  -5.930  1.00 23.59 ? 495  ALA C C   1 
ATOM   12623 O  O   . ALA C  1 478 ? -8.876  28.323  -7.124  1.00 24.17 ? 495  ALA C O   1 
ATOM   12624 C  CB  . ALA C  1 478 ? -11.226 27.140  -5.102  1.00 22.62 ? 495  ALA C CB  1 
ATOM   12625 N  N   . LYS C  1 479 ? -9.017  29.402  -5.148  1.00 25.10 ? 496  LYS C N   1 
ATOM   12626 C  CA  . LYS C  1 479 ? -8.511  30.664  -5.672  1.00 25.91 ? 496  LYS C CA  1 
ATOM   12627 C  C   . LYS C  1 479 ? -7.048  30.503  -6.077  1.00 26.16 ? 496  LYS C C   1 
ATOM   12628 O  O   . LYS C  1 479 ? -6.637  31.011  -7.117  1.00 26.78 ? 496  LYS C O   1 
ATOM   12629 C  CB  . LYS C  1 479 ? -8.723  31.810  -4.671  1.00 26.93 ? 496  LYS C CB  1 
ATOM   12630 C  CG  . LYS C  1 479 ? -10.188 32.172  -4.452  1.00 27.80 ? 496  LYS C CG  1 
ATOM   12631 C  CD  . LYS C  1 479 ? -10.467 33.393  -3.582  1.00 30.45 ? 496  LYS C CD  1 
ATOM   12632 C  CE  . LYS C  1 479 ? -10.065 33.211  -2.154  1.00 31.28 ? 496  LYS C CE  1 
ATOM   12633 N  NZ  . LYS C  1 479 ? -10.454 34.358  -1.328  1.00 31.46 ? 496  LYS C NZ  1 
ATOM   12634 N  N   . ALA C  1 480 ? -6.271  29.781  -5.260  1.00 25.47 ? 497  ALA C N   1 
ATOM   12635 C  CA  . ALA C  1 480 ? -4.856  29.576  -5.534  1.00 25.12 ? 497  ALA C CA  1 
ATOM   12636 C  C   . ALA C  1 480 ? -4.656  28.753  -6.805  1.00 24.63 ? 497  ALA C C   1 
ATOM   12637 O  O   . ALA C  1 480 ? -3.675  28.947  -7.514  1.00 26.54 ? 497  ALA C O   1 
ATOM   12638 C  CB  . ALA C  1 480 ? -4.193  28.910  -4.352  1.00 25.68 ? 497  ALA C CB  1 
ATOM   12639 N  N   . LEU C  1 481 ? -5.566  27.811  -7.073  1.00 24.32 ? 498  LEU C N   1 
ATOM   12640 C  CA  . LEU C  1 481 ? -5.500  27.009  -8.285  1.00 24.71 ? 498  LEU C CA  1 
ATOM   12641 C  C   . LEU C  1 481 ? -5.709  27.906  -9.506  1.00 24.25 ? 498  LEU C C   1 
ATOM   12642 O  O   . LEU C  1 481 ? -4.893  27.903  -10.423 1.00 23.40 ? 498  LEU C O   1 
ATOM   12643 C  CB  . LEU C  1 481 ? -6.525  25.873  -8.228  1.00 24.55 ? 498  LEU C CB  1 
ATOM   12644 C  CG  . LEU C  1 481 ? -6.627  24.973  -9.466  1.00 24.40 ? 498  LEU C CG  1 
ATOM   12645 C  CD1 . LEU C  1 481 ? -5.296  24.343  -9.833  1.00 25.25 ? 498  LEU C CD1 1 
ATOM   12646 C  CD2 . LEU C  1 481 ? -7.673  23.897  -9.259  1.00 24.35 ? 498  LEU C CD2 1 
ATOM   12647 N  N   . THR C  1 482 ? -6.798  28.682  -9.503  1.00 25.94 ? 499  THR C N   1 
ATOM   12648 C  CA  . THR C  1 482 ? -7.150  29.530  -10.636 1.00 27.99 ? 499  THR C CA  1 
ATOM   12649 C  C   . THR C  1 482 ? -6.080  30.599  -10.880 1.00 29.45 ? 499  THR C C   1 
ATOM   12650 O  O   . THR C  1 482 ? -5.842  30.988  -12.022 1.00 29.48 ? 499  THR C O   1 
ATOM   12651 C  CB  . THR C  1 482 ? -8.525  30.148  -10.387 1.00 29.38 ? 499  THR C CB  1 
ATOM   12652 O  OG1 . THR C  1 482 ? -9.416  29.039  -10.356 1.00 30.58 ? 499  THR C OG1 1 
ATOM   12653 C  CG2 . THR C  1 482 ? -8.958  31.106  -11.483 1.00 30.41 ? 499  THR C CG2 1 
ATOM   12654 N  N   . SER C  1 483 ? -5.419  31.068  -9.815  1.00 30.38 ? 500  SER C N   1 
ATOM   12655 C  CA  . SER C  1 483 ? -4.446  32.146  -9.932  1.00 31.88 ? 500  SER C CA  1 
ATOM   12656 C  C   . SER C  1 483 ? -3.218  31.721  -10.742 1.00 31.76 ? 500  SER C C   1 
ATOM   12657 O  O   . SER C  1 483 ? -2.407  32.566  -11.103 1.00 34.23 ? 500  SER C O   1 
ATOM   12658 C  CB  . SER C  1 483 ? -4.038  32.655  -8.569  1.00 33.45 ? 500  SER C CB  1 
ATOM   12659 O  OG  . SER C  1 483 ? -3.172  31.735  -7.916  1.00 34.53 ? 500  SER C OG  1 
ATOM   12660 N  N   . GLN C  1 484 ? -3.077  30.421  -11.027 1.00 30.83 ? 501  GLN C N   1 
ATOM   12661 C  CA  . GLN C  1 484 ? -1.912  29.913  -11.735 1.00 31.77 ? 501  GLN C CA  1 
ATOM   12662 C  C   . GLN C  1 484 ? -2.164  29.784  -13.236 1.00 31.91 ? 501  GLN C C   1 
ATOM   12663 O  O   . GLN C  1 484 ? -1.242  29.472  -13.984 1.00 32.04 ? 501  GLN C O   1 
ATOM   12664 C  CB  . GLN C  1 484 ? -1.529  28.554  -11.158 1.00 31.48 ? 501  GLN C CB  1 
ATOM   12665 C  CG  . GLN C  1 484 ? -1.036  28.638  -9.721  1.00 31.90 ? 501  GLN C CG  1 
ATOM   12666 C  CD  . GLN C  1 484 ? -0.437  27.338  -9.247  1.00 33.84 ? 501  GLN C CD  1 
ATOM   12667 O  OE1 . GLN C  1 484 ? 0.586   26.885  -9.772  1.00 35.35 ? 501  GLN C OE1 1 
ATOM   12668 N  NE2 . GLN C  1 484 ? -1.061  26.729  -8.247  1.00 35.00 ? 501  GLN C NE2 1 
ATOM   12669 N  N   . LEU C  1 485 ? -3.416  29.985  -13.659 1.00 33.50 ? 502  LEU C N   1 
ATOM   12670 C  CA  . LEU C  1 485 ? -3.794  29.886  -15.060 1.00 35.33 ? 502  LEU C CA  1 
ATOM   12671 C  C   . LEU C  1 485 ? -3.293  31.120  -15.805 1.00 35.75 ? 502  LEU C C   1 
ATOM   12672 O  O   . LEU C  1 485 ? -3.584  32.238  -15.393 1.00 35.70 ? 502  LEU C O   1 
ATOM   12673 C  CB  . LEU C  1 485 ? -5.316  29.772  -15.117 1.00 36.73 ? 502  LEU C CB  1 
ATOM   12674 C  CG  . LEU C  1 485 ? -5.918  29.348  -16.458 1.00 38.19 ? 502  LEU C CG  1 
ATOM   12675 C  CD1 . LEU C  1 485 ? -5.568  27.908  -16.770 1.00 37.54 ? 502  LEU C CD1 1 
ATOM   12676 C  CD2 . LEU C  1 485 ? -7.421  29.559  -16.432 1.00 39.55 ? 502  LEU C CD2 1 
ATOM   12677 N  N   . THR C  1 486 ? -2.532  30.912  -16.888 1.00 38.50 ? 503  THR C N   1 
ATOM   12678 C  CA  . THR C  1 486 ? -1.978  32.019  -17.654 1.00 40.87 ? 503  THR C CA  1 
ATOM   12679 C  C   . THR C  1 486 ? -3.023  32.515  -18.652 1.00 40.93 ? 503  THR C C   1 
ATOM   12680 O  O   . THR C  1 486 ? -4.044  31.867  -18.872 1.00 40.86 ? 503  THR C O   1 
ATOM   12681 C  CB  . THR C  1 486 ? -0.685  31.605  -18.359 1.00 41.18 ? 503  THR C CB  1 
ATOM   12682 O  OG1 . THR C  1 486 ? -1.052  30.646  -19.345 1.00 43.15 ? 503  THR C OG1 1 
ATOM   12683 C  CG2 . THR C  1 486 ? 0.353   31.039  -17.405 1.00 41.44 ? 503  THR C CG2 1 
ATOM   12684 N  N   . ASP C  1 487 ? -2.741  33.673  -19.258 1.00 45.45 ? 504  ASP C N   1 
ATOM   12685 C  CA  . ASP C  1 487 ? -3.608  34.265  -20.268 1.00 47.39 ? 504  ASP C CA  1 
ATOM   12686 C  C   . ASP C  1 487 ? -3.669  33.370  -21.505 1.00 46.46 ? 504  ASP C C   1 
ATOM   12687 O  O   . ASP C  1 487 ? -4.750  33.142  -22.049 1.00 45.91 ? 504  ASP C O   1 
ATOM   12688 C  CB  . ASP C  1 487 ? -3.151  35.672  -20.619 1.00 50.51 ? 504  ASP C CB  1 
ATOM   12689 C  CG  . ASP C  1 487 ? -3.278  36.700  -19.504 1.00 53.20 ? 504  ASP C CG  1 
ATOM   12690 O  OD1 . ASP C  1 487 ? -3.979  36.413  -18.508 1.00 56.26 ? 504  ASP C OD1 1 
ATOM   12691 O  OD2 . ASP C  1 487 ? -2.664  37.779  -19.634 1.00 56.45 ? 504  ASP C OD2 1 
ATOM   12692 N  N   . GLU C  1 488 ? -2.502  32.867  -21.936 1.00 43.55 ? 505  GLU C N   1 
ATOM   12693 C  CA  . GLU C  1 488 ? -2.405  32.017  -23.113 1.00 43.12 ? 505  GLU C CA  1 
ATOM   12694 C  C   . GLU C  1 488 ? -3.226  30.741  -22.921 1.00 41.59 ? 505  GLU C C   1 
ATOM   12695 O  O   . GLU C  1 488 ? -3.838  30.258  -23.869 1.00 40.70 ? 505  GLU C O   1 
ATOM   12696 C  CB  . GLU C  1 488 ? -0.948  31.667  -23.423 1.00 44.32 ? 505  GLU C CB  1 
ATOM   12697 N  N   . GLU C  1 489 ? -3.229  30.199  -21.696 1.00 39.35 ? 506  GLU C N   1 
ATOM   12698 C  CA  . GLU C  1 489 ? -3.972  28.985  -21.392 1.00 38.67 ? 506  GLU C CA  1 
ATOM   12699 C  C   . GLU C  1 489 ? -5.471  29.270  -21.457 1.00 37.15 ? 506  GLU C C   1 
ATOM   12700 O  O   . GLU C  1 489 ? -6.215  28.508  -22.065 1.00 38.12 ? 506  GLU C O   1 
ATOM   12701 C  CB  . GLU C  1 489 ? -3.551  28.405  -20.039 1.00 38.25 ? 506  GLU C CB  1 
ATOM   12702 C  CG  . GLU C  1 489 ? -2.217  27.666  -20.095 1.00 38.13 ? 506  GLU C CG  1 
ATOM   12703 C  CD  . GLU C  1 489 ? -1.524  27.453  -18.758 1.00 38.03 ? 506  GLU C CD  1 
ATOM   12704 O  OE1 . GLU C  1 489 ? -2.025  27.931  -17.720 1.00 36.95 ? 506  GLU C OE1 1 
ATOM   12705 O  OE2 . GLU C  1 489 ? -0.458  26.803  -18.762 1.00 38.81 ? 506  GLU C OE2 1 
ATOM   12706 N  N   . LEU C  1 490 ? -5.908  30.374  -20.844 1.00 37.63 ? 507  LEU C N   1 
ATOM   12707 C  CA  . LEU C  1 490 ? -7.318  30.737  -20.848 1.00 40.56 ? 507  LEU C CA  1 
ATOM   12708 C  C   . LEU C  1 490 ? -7.809  30.954  -22.283 1.00 41.48 ? 507  LEU C C   1 
ATOM   12709 O  O   . LEU C  1 490 ? -8.934  30.581  -22.612 1.00 41.03 ? 507  LEU C O   1 
ATOM   12710 C  CB  . LEU C  1 490 ? -7.540  31.972  -19.976 1.00 42.06 ? 507  LEU C CB  1 
ATOM   12711 C  CG  . LEU C  1 490 ? -8.990  32.449  -19.829 1.00 44.60 ? 507  LEU C CG  1 
ATOM   12712 C  CD1 . LEU C  1 490 ? -9.914  31.357  -19.311 1.00 45.06 ? 507  LEU C CD1 1 
ATOM   12713 C  CD2 . LEU C  1 490 ? -9.045  33.660  -18.912 1.00 45.91 ? 507  LEU C CD2 1 
ATOM   12714 N  N   . ALA C  1 491 ? -6.957  31.539  -23.137 1.00 43.03 ? 508  ALA C N   1 
ATOM   12715 C  CA  . ALA C  1 491 ? -7.308  31.808  -24.525 1.00 43.69 ? 508  ALA C CA  1 
ATOM   12716 C  C   . ALA C  1 491 ? -7.528  30.507  -25.295 1.00 45.18 ? 508  ALA C C   1 
ATOM   12717 O  O   . ALA C  1 491 ? -8.382  30.460  -26.178 1.00 48.54 ? 508  ALA C O   1 
ATOM   12718 C  CB  . ALA C  1 491 ? -6.237  32.654  -25.175 1.00 44.09 ? 508  ALA C CB  1 
ATOM   12719 N  N   . GLN C  1 492 ? -6.761  29.459  -24.953 1.00 43.63 ? 509  GLN C N   1 
ATOM   12720 C  CA  . GLN C  1 492 ? -6.921  28.135  -25.540 1.00 45.08 ? 509  GLN C CA  1 
ATOM   12721 C  C   . GLN C  1 492 ? -8.247  27.492  -25.127 1.00 43.63 ? 509  GLN C C   1 
ATOM   12722 O  O   . GLN C  1 492 ? -8.669  26.517  -25.747 1.00 44.54 ? 509  GLN C O   1 
ATOM   12723 C  CB  . GLN C  1 492 ? -5.820  27.168  -25.100 1.00 49.26 ? 509  GLN C CB  1 
ATOM   12724 C  CG  . GLN C  1 492 ? -4.438  27.463  -25.671 1.00 52.90 ? 509  GLN C CG  1 
ATOM   12725 C  CD  . GLN C  1 492 ? -3.353  26.590  -25.073 1.00 57.11 ? 509  GLN C CD  1 
ATOM   12726 O  OE1 . GLN C  1 492 ? -3.594  25.777  -24.171 1.00 57.00 ? 509  GLN C OE1 1 
ATOM   12727 N  NE2 . GLN C  1 492 ? -2.135  26.756  -25.570 1.00 59.20 ? 509  GLN C NE2 1 
ATOM   12728 N  N   . GLY C  1 493 ? -8.878  28.010  -24.065 1.00 41.65 ? 510  GLY C N   1 
ATOM   12729 C  CA  . GLY C  1 493 ? -10.133 27.470  -23.566 1.00 40.18 ? 510  GLY C CA  1 
ATOM   12730 C  C   . GLY C  1 493 ? -9.943  26.621  -22.309 1.00 37.86 ? 510  GLY C C   1 
ATOM   12731 O  O   . GLY C  1 493 ? -10.880 25.952  -21.878 1.00 35.63 ? 510  GLY C O   1 
ATOM   12732 N  N   . ARG C  1 494 ? -8.732  26.653  -21.728 1.00 37.40 ? 511  ARG C N   1 
ATOM   12733 C  CA  . ARG C  1 494 ? -8.433  25.927  -20.501 1.00 37.08 ? 511  ARG C CA  1 
ATOM   12734 C  C   . ARG C  1 494 ? -8.951  26.705  -19.296 1.00 32.51 ? 511  ARG C C   1 
ATOM   12735 O  O   . ARG C  1 494 ? -8.694  27.898  -19.183 1.00 35.26 ? 511  ARG C O   1 
ATOM   12736 C  CB  . ARG C  1 494 ? -6.926  25.737  -20.291 1.00 38.39 ? 511  ARG C CB  1 
ATOM   12737 C  CG  . ARG C  1 494 ? -6.260  24.687  -21.169 1.00 41.10 ? 511  ARG C CG  1 
ATOM   12738 C  CD  . ARG C  1 494 ? -4.767  24.617  -20.889 1.00 42.77 ? 511  ARG C CD  1 
ATOM   12739 N  NE  . ARG C  1 494 ? -4.072  23.556  -21.627 1.00 43.70 ? 511  ARG C NE  1 
ATOM   12740 C  CZ  . ARG C  1 494 ? -4.029  22.263  -21.305 1.00 45.80 ? 511  ARG C CZ  1 
ATOM   12741 N  NH1 . ARG C  1 494 ? -4.674  21.800  -20.248 1.00 45.63 ? 511  ARG C NH1 1 
ATOM   12742 N  NH2 . ARG C  1 494 ? -3.322  21.428  -22.048 1.00 47.55 ? 511  ARG C NH2 1 
ATOM   12743 N  N   . LEU C  1 495 ? -9.657  26.011  -18.394 1.00 30.20 ? 512  LEU C N   1 
ATOM   12744 C  CA  . LEU C  1 495 ? -10.106 26.580  -17.133 1.00 28.80 ? 512  LEU C CA  1 
ATOM   12745 C  C   . LEU C  1 495 ? -9.292  26.029  -15.960 1.00 29.48 ? 512  LEU C C   1 
ATOM   12746 O  O   . LEU C  1 495 ? -9.572  26.351  -14.804 1.00 27.53 ? 512  LEU C O   1 
ATOM   12747 C  CB  . LEU C  1 495 ? -11.595 26.273  -16.986 1.00 28.99 ? 512  LEU C CB  1 
ATOM   12748 C  CG  . LEU C  1 495 ? -12.502 26.877  -18.063 1.00 29.17 ? 512  LEU C CG  1 
ATOM   12749 C  CD1 . LEU C  1 495 ? -13.953 26.526  -17.793 1.00 30.45 ? 512  LEU C CD1 1 
ATOM   12750 C  CD2 . LEU C  1 495 ? -12.322 28.382  -18.148 1.00 29.11 ? 512  LEU C CD2 1 
ATOM   12751 N  N   . TYR C  1 496 ? -8.286  25.203  -16.277 1.00 28.64 ? 513  TYR C N   1 
ATOM   12752 C  CA  . TYR C  1 496 ? -7.396  24.609  -15.294 1.00 27.84 ? 513  TYR C CA  1 
ATOM   12753 C  C   . TYR C  1 496 ? -5.979  24.596  -15.856 1.00 28.78 ? 513  TYR C C   1 
ATOM   12754 O  O   . TYR C  1 496 ? -5.791  24.376  -17.049 1.00 29.44 ? 513  TYR C O   1 
ATOM   12755 C  CB  . TYR C  1 496 ? -7.800  23.167  -14.970 1.00 26.35 ? 513  TYR C CB  1 
ATOM   12756 C  CG  . TYR C  1 496 ? -9.176  23.039  -14.336 1.00 24.93 ? 513  TYR C CG  1 
ATOM   12757 C  CD1 . TYR C  1 496 ? -9.362  23.343  -12.995 1.00 24.38 ? 513  TYR C CD1 1 
ATOM   12758 C  CD2 . TYR C  1 496 ? -10.278 22.610  -15.067 1.00 24.03 ? 513  TYR C CD2 1 
ATOM   12759 C  CE1 . TYR C  1 496 ? -10.604 23.229  -12.398 1.00 23.61 ? 513  TYR C CE1 1 
ATOM   12760 C  CE2 . TYR C  1 496 ? -11.531 22.506  -14.482 1.00 23.73 ? 513  TYR C CE2 1 
ATOM   12761 C  CZ  . TYR C  1 496 ? -11.692 22.816  -13.143 1.00 23.08 ? 513  TYR C CZ  1 
ATOM   12762 O  OH  . TYR C  1 496 ? -12.912 22.720  -12.543 1.00 22.57 ? 513  TYR C OH  1 
ATOM   12763 N  N   . PRO C  1 497 ? -4.938  24.800  -15.021 1.00 29.78 ? 514  PRO C N   1 
ATOM   12764 C  CA  . PRO C  1 497 ? -3.557  24.657  -15.483 1.00 29.86 ? 514  PRO C CA  1 
ATOM   12765 C  C   . PRO C  1 497 ? -3.304  23.227  -15.959 1.00 30.87 ? 514  PRO C C   1 
ATOM   12766 O  O   . PRO C  1 497 ? -4.001  22.301  -15.541 1.00 30.64 ? 514  PRO C O   1 
ATOM   12767 C  CB  . PRO C  1 497 ? -2.686  25.045  -14.277 1.00 29.50 ? 514  PRO C CB  1 
ATOM   12768 C  CG  . PRO C  1 497 ? -3.616  24.978  -13.084 1.00 29.93 ? 514  PRO C CG  1 
ATOM   12769 C  CD  . PRO C  1 497 ? -5.037  25.159  -13.598 1.00 29.73 ? 514  PRO C CD  1 
ATOM   12770 N  N   . PRO C  1 498 ? -2.312  22.998  -16.850 1.00 32.53 ? 515  PRO C N   1 
ATOM   12771 C  CA  . PRO C  1 498 ? -2.057  21.664  -17.398 1.00 32.56 ? 515  PRO C CA  1 
ATOM   12772 C  C   . PRO C  1 498 ? -1.780  20.636  -16.304 1.00 30.83 ? 515  PRO C C   1 
ATOM   12773 O  O   . PRO C  1 498 ? -1.105  20.950  -15.328 1.00 30.59 ? 515  PRO C O   1 
ATOM   12774 C  CB  . PRO C  1 498 ? -0.834  21.873  -18.314 1.00 33.44 ? 515  PRO C CB  1 
ATOM   12775 C  CG  . PRO C  1 498 ? -0.850  23.351  -18.635 1.00 33.89 ? 515  PRO C CG  1 
ATOM   12776 C  CD  . PRO C  1 498 ? -1.381  24.011  -17.375 1.00 34.46 ? 515  PRO C CD  1 
ATOM   12777 N  N   . LEU C  1 499 ? -2.303  19.415  -16.484 1.00 31.45 ? 516  LEU C N   1 
ATOM   12778 C  CA  . LEU C  1 499 ? -2.097  18.318  -15.544 1.00 31.35 ? 516  LEU C CA  1 
ATOM   12779 C  C   . LEU C  1 499 ? -0.627  17.908  -15.495 1.00 31.11 ? 516  LEU C C   1 
ATOM   12780 O  O   . LEU C  1 499 ? -0.158  17.422  -14.468 1.00 31.93 ? 516  LEU C O   1 
ATOM   12781 C  CB  . LEU C  1 499 ? -2.962  17.105  -15.881 1.00 32.02 ? 516  LEU C CB  1 
ATOM   12782 C  CG  . LEU C  1 499 ? -4.265  16.945  -15.097 1.00 34.30 ? 516  LEU C CG  1 
ATOM   12783 C  CD1 . LEU C  1 499 ? -4.950  15.675  -15.580 1.00 35.93 ? 516  LEU C CD1 1 
ATOM   12784 C  CD2 . LEU C  1 499 ? -4.047  16.902  -13.588 1.00 34.12 ? 516  LEU C CD2 1 
ATOM   12785 N  N   . ALA C  1 500 ? 0.088   18.079  -16.611 1.00 30.50 ? 517  ALA C N   1 
ATOM   12786 C  CA  . ALA C  1 500 ? 1.514   17.795  -16.669 1.00 30.69 ? 517  ALA C CA  1 
ATOM   12787 C  C   . ALA C  1 500 ? 2.288   18.596  -15.622 1.00 30.28 ? 517  ALA C C   1 
ATOM   12788 O  O   . ALA C  1 500 ? 3.357   18.168  -15.193 1.00 30.34 ? 517  ALA C O   1 
ATOM   12789 C  CB  . ALA C  1 500 ? 2.039   18.079  -18.060 1.00 31.52 ? 517  ALA C CB  1 
ATOM   12790 N  N   . ASN C  1 501 ? 1.749   19.752  -15.208 1.00 30.01 ? 518  ASN C N   1 
ATOM   12791 C  CA  . ASN C  1 501 ? 2.435   20.633  -14.279 1.00 29.43 ? 518  ASN C CA  1 
ATOM   12792 C  C   . ASN C  1 501 ? 1.945   20.425  -12.842 1.00 28.01 ? 518  ASN C C   1 
ATOM   12793 O  O   . ASN C  1 501 ? 2.118   21.307  -12.006 1.00 26.73 ? 518  ASN C O   1 
ATOM   12794 C  CB  . ASN C  1 501 ? 2.257   22.091  -14.697 1.00 33.40 ? 518  ASN C CB  1 
ATOM   12795 C  CG  . ASN C  1 501 ? 2.837   22.391  -16.061 1.00 36.66 ? 518  ASN C CG  1 
ATOM   12796 O  OD1 . ASN C  1 501 ? 3.673   21.636  -16.572 1.00 39.44 ? 518  ASN C OD1 1 
ATOM   12797 N  ND2 . ASN C  1 501 ? 2.430   23.503  -16.656 1.00 38.63 ? 518  ASN C ND2 1 
ATOM   12798 N  N   . ILE C  1 502 ? 1.378   19.252  -12.529 1.00 28.16 ? 519  ILE C N   1 
ATOM   12799 C  CA  . ILE C  1 502 ? 0.688   19.057  -11.258 1.00 27.08 ? 519  ILE C CA  1 
ATOM   12800 C  C   . ILE C  1 502 ? 1.633   19.260  -10.071 1.00 26.35 ? 519  ILE C C   1 
ATOM   12801 O  O   . ILE C  1 502 ? 1.202   19.765  -9.040  1.00 26.19 ? 519  ILE C O   1 
ATOM   12802 C  CB  . ILE C  1 502 ? -0.028  17.692  -11.193 1.00 26.06 ? 519  ILE C CB  1 
ATOM   12803 C  CG1 . ILE C  1 502 ? -0.868  17.541  -9.914  1.00 25.61 ? 519  ILE C CG1 1 
ATOM   12804 C  CG2 . ILE C  1 502 ? 0.952   16.529  -11.350 1.00 26.31 ? 519  ILE C CG2 1 
ATOM   12805 C  CD1 . ILE C  1 502 ? -1.946  18.593  -9.733  1.00 25.39 ? 519  ILE C CD1 1 
ATOM   12806 N  N   . GLN C  1 503 ? 2.914   18.882  -10.203 1.00 27.40 ? 520  GLN C N   1 
ATOM   12807 C  CA  . GLN C  1 503 ? 3.858   19.024  -9.102  1.00 27.58 ? 520  GLN C CA  1 
ATOM   12808 C  C   . GLN C  1 503 ? 4.016   20.493  -8.707  1.00 27.62 ? 520  GLN C C   1 
ATOM   12809 O  O   . GLN C  1 503 ? 3.885   20.845  -7.534  1.00 26.41 ? 520  GLN C O   1 
ATOM   12810 C  CB  . GLN C  1 503 ? 5.242   18.456  -9.419  1.00 28.46 ? 520  GLN C CB  1 
ATOM   12811 C  CG  . GLN C  1 503 ? 5.332   16.937  -9.374  1.00 30.05 ? 520  GLN C CG  1 
ATOM   12812 C  CD  . GLN C  1 503 ? 6.766   16.449  -9.387  1.00 31.56 ? 520  GLN C CD  1 
ATOM   12813 O  OE1 . GLN C  1 503 ? 7.259   15.916  -10.385 1.00 33.27 ? 520  GLN C OE1 1 
ATOM   12814 N  NE2 . GLN C  1 503 ? 7.466   16.671  -8.285  1.00 33.44 ? 520  GLN C NE2 1 
ATOM   12815 N  N   . GLU C  1 504 ? 4.324   21.339  -9.694  1.00 28.05 ? 521  GLU C N   1 
ATOM   12816 C  CA  . GLU C  1 504 ? 4.492   22.769  -9.484  1.00 28.90 ? 521  GLU C CA  1 
ATOM   12817 C  C   . GLU C  1 504 ? 3.192   23.396  -8.975  1.00 26.38 ? 521  GLU C C   1 
ATOM   12818 O  O   . GLU C  1 504 ? 3.218   24.246  -8.079  1.00 26.10 ? 521  GLU C O   1 
ATOM   12819 C  CB  . GLU C  1 504 ? 4.940   23.397  -10.805 1.00 33.20 ? 521  GLU C CB  1 
ATOM   12820 C  CG  . GLU C  1 504 ? 5.161   24.906  -10.739 1.00 38.13 ? 521  GLU C CG  1 
ATOM   12821 C  CD  . GLU C  1 504 ? 5.320   25.559  -12.104 1.00 43.09 ? 521  GLU C CD  1 
ATOM   12822 O  OE1 . GLU C  1 504 ? 5.418   24.831  -13.114 1.00 48.79 ? 521  GLU C OE1 1 
ATOM   12823 O  OE2 . GLU C  1 504 ? 5.326   26.805  -12.159 1.00 48.40 ? 521  GLU C OE2 1 
ATOM   12824 N  N   . VAL C  1 505 ? 2.062   22.987  -9.561  1.00 24.90 ? 522  VAL C N   1 
ATOM   12825 C  CA  . VAL C  1 505 ? 0.761   23.517  -9.179  1.00 24.77 ? 522  VAL C CA  1 
ATOM   12826 C  C   . VAL C  1 505 ? 0.491   23.217  -7.704  1.00 24.45 ? 522  VAL C C   1 
ATOM   12827 O  O   . VAL C  1 505 ? 0.039   24.099  -6.974  1.00 24.57 ? 522  VAL C O   1 
ATOM   12828 C  CB  . VAL C  1 505 ? -0.368  22.981  -10.084 1.00 25.45 ? 522  VAL C CB  1 
ATOM   12829 C  CG1 . VAL C  1 505 ? -1.757  23.255  -9.518  1.00 25.63 ? 522  VAL C CG1 1 
ATOM   12830 C  CG2 . VAL C  1 505 ? -0.264  23.544  -11.495 1.00 25.90 ? 522  VAL C CG2 1 
ATOM   12831 N  N   . SER C  1 506 ? 0.782   21.983  -7.270  1.00 23.52 ? 523  SER C N   1 
ATOM   12832 C  CA  . SER C  1 506 ? 0.480   21.555  -5.910  1.00 23.57 ? 523  SER C CA  1 
ATOM   12833 C  C   . SER C  1 506 ? 1.315   22.329  -4.891  1.00 22.90 ? 523  SER C C   1 
ATOM   12834 O  O   . SER C  1 506 ? 0.803   22.729  -3.845  1.00 21.89 ? 523  SER C O   1 
ATOM   12835 C  CB  . SER C  1 506 ? 0.667   20.063  -5.748  1.00 24.02 ? 523  SER C CB  1 
ATOM   12836 O  OG  . SER C  1 506 ? -0.265  19.337  -6.541  1.00 23.13 ? 523  SER C OG  1 
ATOM   12837 N  N   . ILE C  1 507 ? 2.602   22.529  -5.200  1.00 22.93 ? 524  ILE C N   1 
ATOM   12838 C  CA  . ILE C  1 507 ? 3.501   23.262  -4.325  1.00 24.28 ? 524  ILE C CA  1 
ATOM   12839 C  C   . ILE C  1 507 ? 3.010   24.701  -4.174  1.00 23.75 ? 524  ILE C C   1 
ATOM   12840 O  O   . ILE C  1 507 ? 3.021   25.241  -3.070  1.00 22.99 ? 524  ILE C O   1 
ATOM   12841 C  CB  . ILE C  1 507 ? 4.956   23.185  -4.836  1.00 26.21 ? 524  ILE C CB  1 
ATOM   12842 C  CG1 . ILE C  1 507 ? 5.496   21.750  -4.814  1.00 27.88 ? 524  ILE C CG1 1 
ATOM   12843 C  CG2 . ILE C  1 507 ? 5.870   24.130  -4.056  1.00 27.53 ? 524  ILE C CG2 1 
ATOM   12844 C  CD1 . ILE C  1 507 ? 5.322   21.026  -3.490  1.00 28.05 ? 524  ILE C CD1 1 
ATOM   12845 N  N   . ASN C  1 508 ? 2.570   25.312  -5.279  1.00 23.61 ? 525  ASN C N   1 
ATOM   12846 C  CA  . ASN C  1 508 ? 2.106   26.692  -5.267  1.00 24.69 ? 525  ASN C CA  1 
ATOM   12847 C  C   . ASN C  1 508 ? 0.833   26.835  -4.434  1.00 24.33 ? 525  ASN C C   1 
ATOM   12848 O  O   . ASN C  1 508 ? 0.663   27.836  -3.745  1.00 25.23 ? 525  ASN C O   1 
ATOM   12849 C  CB  . ASN C  1 508 ? 1.942   27.227  -6.686  1.00 25.61 ? 525  ASN C CB  1 
ATOM   12850 C  CG  . ASN C  1 508 ? 3.279   27.508  -7.334  1.00 27.65 ? 525  ASN C CG  1 
ATOM   12851 O  OD1 . ASN C  1 508 ? 4.288   27.640  -6.632  1.00 28.47 ? 525  ASN C OD1 1 
ATOM   12852 N  ND2 . ASN C  1 508 ? 3.312   27.604  -8.656  1.00 27.96 ? 525  ASN C ND2 1 
ATOM   12853 N  N   . ILE C  1 509 ? -0.052  25.833  -4.489  1.00 23.80 ? 526  ILE C N   1 
ATOM   12854 C  CA  . ILE C  1 509 ? -1.259  25.835  -3.679  1.00 23.35 ? 526  ILE C CA  1 
ATOM   12855 C  C   . ILE C  1 509 ? -0.878  25.710  -2.204  1.00 23.10 ? 526  ILE C C   1 
ATOM   12856 O  O   . ILE C  1 509 ? -1.434  26.415  -1.371  1.00 21.96 ? 526  ILE C O   1 
ATOM   12857 C  CB  . ILE C  1 509 ? -2.231  24.730  -4.135  1.00 24.35 ? 526  ILE C CB  1 
ATOM   12858 C  CG1 . ILE C  1 509 ? -2.838  25.076  -5.494  1.00 24.40 ? 526  ILE C CG1 1 
ATOM   12859 C  CG2 . ILE C  1 509 ? -3.317  24.473  -3.087  1.00 23.84 ? 526  ILE C CG2 1 
ATOM   12860 C  CD1 . ILE C  1 509 ? -3.582  23.934  -6.151  1.00 25.39 ? 526  ILE C CD1 1 
ATOM   12861 N  N   . ALA C  1 510 ? 0.078   24.823  -1.893  1.00 23.03 ? 527  ALA C N   1 
ATOM   12862 C  CA  . ALA C  1 510 ? 0.530   24.609  -0.525  1.00 23.76 ? 527  ALA C CA  1 
ATOM   12863 C  C   . ALA C  1 510 ? 1.065   25.904  0.081   1.00 23.44 ? 527  ALA C C   1 
ATOM   12864 O  O   . ALA C  1 510 ? 0.813   26.197  1.248   1.00 23.78 ? 527  ALA C O   1 
ATOM   12865 C  CB  . ALA C  1 510 ? 1.580   23.514  -0.488  1.00 24.45 ? 527  ALA C CB  1 
ATOM   12866 N  N   . ILE C  1 511 ? 1.800   26.682  -0.721  1.00 23.55 ? 528  ILE C N   1 
ATOM   12867 C  CA  . ILE C  1 511 ? 2.378   27.931  -0.247  1.00 23.37 ? 528  ILE C CA  1 
ATOM   12868 C  C   . ILE C  1 511 ? 1.255   28.916  0.089   1.00 23.47 ? 528  ILE C C   1 
ATOM   12869 O  O   . ILE C  1 511 ? 1.271   29.536  1.151   1.00 22.46 ? 528  ILE C O   1 
ATOM   12870 C  CB  . ILE C  1 511 ? 3.383   28.478  -1.281  1.00 23.20 ? 528  ILE C CB  1 
ATOM   12871 C  CG1 . ILE C  1 511 ? 4.585   27.531  -1.419  1.00 23.59 ? 528  ILE C CG1 1 
ATOM   12872 C  CG2 . ILE C  1 511 ? 3.820   29.901  -0.931  1.00 23.05 ? 528  ILE C CG2 1 
ATOM   12873 C  CD1 . ILE C  1 511 ? 5.482   27.800  -2.616  1.00 24.29 ? 528  ILE C CD1 1 
ATOM   12874 N  N   . LYS C  1 512 ? 0.269   29.042  -0.805  1.00 24.71 ? 529  LYS C N   1 
ATOM   12875 C  CA  . LYS C  1 512 ? -0.834  29.973  -0.607  1.00 24.86 ? 529  LYS C CA  1 
ATOM   12876 C  C   . LYS C  1 512 ? -1.681  29.570  0.597   1.00 23.50 ? 529  LYS C C   1 
ATOM   12877 O  O   . LYS C  1 512 ? -2.134  30.426  1.352   1.00 23.62 ? 529  LYS C O   1 
ATOM   12878 C  CB  . LYS C  1 512 ? -1.736  30.032  -1.841  1.00 27.54 ? 529  LYS C CB  1 
ATOM   12879 C  CG  . LYS C  1 512 ? -1.149  30.724  -3.064  1.00 31.53 ? 529  LYS C CG  1 
ATOM   12880 C  CD  . LYS C  1 512 ? -0.951  32.226  -2.912  1.00 35.23 ? 529  LYS C CD  1 
ATOM   12881 C  CE  . LYS C  1 512 ? -1.053  32.956  -4.228  1.00 39.88 ? 529  LYS C CE  1 
ATOM   12882 N  NZ  . LYS C  1 512 ? -0.214  32.369  -5.280  1.00 41.90 ? 529  LYS C NZ  1 
ATOM   12883 N  N   . VAL C  1 513 ? -1.916  28.266  0.763   1.00 22.61 ? 530  VAL C N   1 
ATOM   12884 C  CA  . VAL C  1 513 ? -2.733  27.782  1.864   1.00 21.18 ? 530  VAL C CA  1 
ATOM   12885 C  C   . VAL C  1 513 ? -1.964  27.958  3.177   1.00 21.36 ? 530  VAL C C   1 
ATOM   12886 O  O   . VAL C  1 513 ? -2.565  28.278  4.195   1.00 20.82 ? 530  VAL C O   1 
ATOM   12887 C  CB  . VAL C  1 513 ? -3.179  26.331  1.596   1.00 21.11 ? 530  VAL C CB  1 
ATOM   12888 C  CG1 . VAL C  1 513 ? -3.916  25.709  2.773   1.00 20.91 ? 530  VAL C CG1 1 
ATOM   12889 C  CG2 . VAL C  1 513 ? -4.052  26.240  0.350   1.00 21.78 ? 530  VAL C CG2 1 
ATOM   12890 N  N   . THR C  1 514 ? -0.631  27.797  3.139   1.00 21.95 ? 531  THR C N   1 
ATOM   12891 C  CA  . THR C  1 514 ? 0.213   27.985  4.312   1.00 23.05 ? 531  THR C CA  1 
ATOM   12892 C  C   . THR C  1 514 ? 0.127   29.443  4.769   1.00 23.88 ? 531  THR C C   1 
ATOM   12893 O  O   . THR C  1 514 ? -0.004  29.726  5.957   1.00 22.46 ? 531  THR C O   1 
ATOM   12894 C  CB  . THR C  1 514 ? 1.658   27.587  3.995   1.00 23.11 ? 531  THR C CB  1 
ATOM   12895 O  OG1 . THR C  1 514 ? 1.715   26.175  3.819   1.00 22.70 ? 531  THR C OG1 1 
ATOM   12896 C  CG2 . THR C  1 514 ? 2.624   27.949  5.109   1.00 23.10 ? 531  THR C CG2 1 
ATOM   12897 N  N   . GLU C  1 515 ? 0.216   30.371  3.811   1.00 25.45 ? 532  GLU C N   1 
ATOM   12898 C  CA  . GLU C  1 515 ? 0.060   31.788  4.106   1.00 26.75 ? 532  GLU C CA  1 
ATOM   12899 C  C   . GLU C  1 515 ? -1.292  32.032  4.775   1.00 25.77 ? 532  GLU C C   1 
ATOM   12900 O  O   . GLU C  1 515 ? -1.381  32.762  5.762   1.00 26.26 ? 532  GLU C O   1 
ATOM   12901 C  CB  . GLU C  1 515 ? 0.260   32.604  2.828   1.00 28.76 ? 532  GLU C CB  1 
ATOM   12902 C  CG  . GLU C  1 515 ? 1.726   32.659  2.408   1.00 31.77 ? 532  GLU C CG  1 
ATOM   12903 C  CD  . GLU C  1 515 ? 2.039   33.173  1.015   1.00 35.53 ? 532  GLU C CD  1 
ATOM   12904 O  OE1 . GLU C  1 515 ? 1.137   33.297  0.156   1.00 39.60 ? 532  GLU C OE1 1 
ATOM   12905 O  OE2 . GLU C  1 515 ? 3.235   33.447  0.798   1.00 39.23 ? 532  GLU C OE2 1 
ATOM   12906 N  N   . TYR C  1 516 ? -2.339  31.398  4.243   1.00 25.08 ? 533  TYR C N   1 
ATOM   12907 C  CA  . TYR C  1 516 ? -3.688  31.587  4.752   1.00 24.11 ? 533  TYR C CA  1 
ATOM   12908 C  C   . TYR C  1 516 ? -3.810  31.057  6.181   1.00 23.38 ? 533  TYR C C   1 
ATOM   12909 O  O   . TYR C  1 516 ? -4.437  31.696  7.026   1.00 22.23 ? 533  TYR C O   1 
ATOM   12910 C  CB  . TYR C  1 516 ? -4.693  30.915  3.811   1.00 25.05 ? 533  TYR C CB  1 
ATOM   12911 C  CG  . TYR C  1 516 ? -6.122  30.976  4.325   1.00 25.55 ? 533  TYR C CG  1 
ATOM   12912 C  CD1 . TYR C  1 516 ? -6.950  32.056  4.031   1.00 26.26 ? 533  TYR C CD1 1 
ATOM   12913 C  CD2 . TYR C  1 516 ? -6.629  29.965  5.129   1.00 26.51 ? 533  TYR C CD2 1 
ATOM   12914 C  CE1 . TYR C  1 516 ? -8.247  32.117  4.513   1.00 26.43 ? 533  TYR C CE1 1 
ATOM   12915 C  CE2 . TYR C  1 516 ? -7.920  30.018  5.622   1.00 27.08 ? 533  TYR C CE2 1 
ATOM   12916 C  CZ  . TYR C  1 516 ? -8.727  31.102  5.320   1.00 27.50 ? 533  TYR C CZ  1 
ATOM   12917 O  OH  . TYR C  1 516 ? -10.000 31.136  5.809   1.00 29.52 ? 533  TYR C OH  1 
ATOM   12918 N  N   . LEU C  1 517 ? -3.227  29.884  6.457   1.00 22.81 ? 534  LEU C N   1 
ATOM   12919 C  CA  . LEU C  1 517 ? -3.383  29.267  7.766   1.00 22.71 ? 534  LEU C CA  1 
ATOM   12920 C  C   . LEU C  1 517 ? -2.708  30.134  8.831   1.00 21.74 ? 534  LEU C C   1 
ATOM   12921 O  O   . LEU C  1 517 ? -3.258  30.342  9.905   1.00 22.24 ? 534  LEU C O   1 
ATOM   12922 C  CB  . LEU C  1 517 ? -2.833  27.841  7.757   1.00 22.61 ? 534  LEU C CB  1 
ATOM   12923 C  CG  . LEU C  1 517 ? -3.598  26.824  6.904   1.00 22.35 ? 534  LEU C CG  1 
ATOM   12924 C  CD1 . LEU C  1 517 ? -2.755  25.572  6.708   1.00 22.29 ? 534  LEU C CD1 1 
ATOM   12925 C  CD2 . LEU C  1 517 ? -4.949  26.477  7.514   1.00 21.93 ? 534  LEU C CD2 1 
ATOM   12926 N  N   . TYR C  1 518 ? -1.516  30.648  8.527   1.00 22.75 ? 535  TYR C N   1 
ATOM   12927 C  CA  . TYR C  1 518 ? -0.798  31.504  9.458   1.00 23.67 ? 535  TYR C CA  1 
ATOM   12928 C  C   . TYR C  1 518 ? -1.552  32.816  9.664   1.00 25.40 ? 535  TYR C C   1 
ATOM   12929 O  O   . TYR C  1 518 ? -1.639  33.297  10.791  1.00 26.39 ? 535  TYR C O   1 
ATOM   12930 C  CB  . TYR C  1 518 ? 0.645   31.753  9.008   1.00 22.85 ? 535  TYR C CB  1 
ATOM   12931 C  CG  . TYR C  1 518 ? 1.624   30.669  9.437   1.00 22.49 ? 535  TYR C CG  1 
ATOM   12932 C  CD1 . TYR C  1 518 ? 1.951   30.491  10.777  1.00 22.53 ? 535  TYR C CD1 1 
ATOM   12933 C  CD2 . TYR C  1 518 ? 2.237   29.837  8.507   1.00 23.28 ? 535  TYR C CD2 1 
ATOM   12934 C  CE1 . TYR C  1 518 ? 2.850   29.516  11.176  1.00 22.64 ? 535  TYR C CE1 1 
ATOM   12935 C  CE2 . TYR C  1 518 ? 3.150   28.867  8.894   1.00 22.91 ? 535  TYR C CE2 1 
ATOM   12936 C  CZ  . TYR C  1 518 ? 3.453   28.701  10.233  1.00 22.77 ? 535  TYR C CZ  1 
ATOM   12937 O  OH  . TYR C  1 518 ? 4.344   27.741  10.625  1.00 23.27 ? 535  TYR C OH  1 
ATOM   12938 N  N   . ALA C  1 519 ? -2.109  33.375  8.582   1.00 26.95 ? 536  ALA C N   1 
ATOM   12939 C  CA  . ALA C  1 519 ? -2.779  34.666  8.641   1.00 27.89 ? 536  ALA C CA  1 
ATOM   12940 C  C   . ALA C  1 519 ? -4.101  34.584  9.409   1.00 29.07 ? 536  ALA C C   1 
ATOM   12941 O  O   . ALA C  1 519 ? -4.567  35.602  9.912   1.00 29.68 ? 536  ALA C O   1 
ATOM   12942 C  CB  . ALA C  1 519 ? -2.989  35.203  7.239   1.00 28.34 ? 536  ALA C CB  1 
ATOM   12943 N  N   . ASN C  1 520 ? -4.708  33.392  9.510   1.00 28.56 ? 537  ASN C N   1 
ATOM   12944 C  CA  . ASN C  1 520 ? -6.022  33.260  10.125  1.00 29.20 ? 537  ASN C CA  1 
ATOM   12945 C  C   . ASN C  1 520 ? -5.957  32.438  11.415  1.00 30.41 ? 537  ASN C C   1 
ATOM   12946 O  O   . ASN C  1 520 ? -6.981  31.949  11.891  1.00 31.32 ? 537  ASN C O   1 
ATOM   12947 C  CB  . ASN C  1 520 ? -7.032  32.717  9.121   1.00 29.45 ? 537  ASN C CB  1 
ATOM   12948 C  CG  . ASN C  1 520 ? -7.267  33.687  7.987   1.00 30.04 ? 537  ASN C CG  1 
ATOM   12949 O  OD1 . ASN C  1 520 ? -8.218  34.474  8.031   1.00 31.45 ? 537  ASN C OD1 1 
ATOM   12950 N  ND2 . ASN C  1 520 ? -6.404  33.678  6.984   1.00 29.71 ? 537  ASN C ND2 1 
ATOM   12951 N  N   . LYS C  1 521 ? -4.757  32.315  11.991  1.00 30.85 ? 538  LYS C N   1 
ATOM   12952 C  CA  . LYS C  1 521 ? -4.564  31.728  13.310  1.00 33.11 ? 538  LYS C CA  1 
ATOM   12953 C  C   . LYS C  1 521 ? -4.945  30.248  13.323  1.00 29.85 ? 538  LYS C C   1 
ATOM   12954 O  O   . LYS C  1 521 ? -5.431  29.749  14.336  1.00 29.05 ? 538  LYS C O   1 
ATOM   12955 C  CB  . LYS C  1 521 ? -5.372  32.461  14.391  1.00 38.23 ? 538  LYS C CB  1 
ATOM   12956 C  CG  . LYS C  1 521 ? -5.259  33.980  14.418  1.00 42.90 ? 538  LYS C CG  1 
ATOM   12957 C  CD  . LYS C  1 521 ? -3.866  34.532  14.704  1.00 46.61 ? 538  LYS C CD  1 
ATOM   12958 C  CE  . LYS C  1 521 ? -2.989  34.642  13.495  1.00 48.10 ? 538  LYS C CE  1 
ATOM   12959 N  NZ  . LYS C  1 521 ? -1.881  35.565  13.757  1.00 50.06 ? 538  LYS C NZ  1 
ATOM   12960 N  N   . MET C  1 522 ? -4.708  29.542  12.211  1.00 26.45 ? 539  MET C N   1 
ATOM   12961 C  CA  . MET C  1 522 ? -5.050  28.130  12.127  1.00 24.89 ? 539  MET C CA  1 
ATOM   12962 C  C   . MET C  1 522 ? -3.795  27.256  12.163  1.00 23.64 ? 539  MET C C   1 
ATOM   12963 O  O   . MET C  1 522 ? -3.915  26.031  12.176  1.00 23.07 ? 539  MET C O   1 
ATOM   12964 C  CB  . MET C  1 522 ? -5.837  27.842  10.844  1.00 24.34 ? 539  MET C CB  1 
ATOM   12965 C  CG  . MET C  1 522 ? -7.213  28.488  10.811  1.00 24.45 ? 539  MET C CG  1 
ATOM   12966 S  SD  . MET C  1 522 ? -7.850  28.582  9.127   1.00 25.31 ? 539  MET C SD  1 
ATOM   12967 C  CE  . MET C  1 522 ? -9.431  29.401  9.386   1.00 25.71 ? 539  MET C CE  1 
ATOM   12968 N  N   . ALA C  1 523 ? -2.611  27.884  12.172  1.00 22.67 ? 540  ALA C N   1 
ATOM   12969 C  CA  . ALA C  1 523 ? -1.340  27.177  12.247  1.00 22.16 ? 540  ALA C CA  1 
ATOM   12970 C  C   . ALA C  1 523 ? -0.838  27.136  13.690  1.00 23.01 ? 540  ALA C C   1 
ATOM   12971 O  O   . ALA C  1 523 ? -1.089  28.062  14.462  1.00 23.88 ? 540  ALA C O   1 
ATOM   12972 C  CB  . ALA C  1 523 ? -0.331  27.851  11.345  1.00 22.04 ? 540  ALA C CB  1 
ATOM   12973 N  N   . PHE C  1 524 ? -0.108  26.068  14.040  1.00 22.83 ? 541  PHE C N   1 
ATOM   12974 C  CA  . PHE C  1 524 ? 0.465   25.929  15.374  1.00 22.92 ? 541  PHE C CA  1 
ATOM   12975 C  C   . PHE C  1 524 ? 1.969   25.664  15.312  1.00 22.95 ? 541  PHE C C   1 
ATOM   12976 O  O   . PHE C  1 524 ? 2.588   25.445  16.354  1.00 23.27 ? 541  PHE C O   1 
ATOM   12977 C  CB  . PHE C  1 524 ? -0.276  24.836  16.150  1.00 22.95 ? 541  PHE C CB  1 
ATOM   12978 C  CG  . PHE C  1 524 ? -1.698  25.254  16.496  1.00 24.24 ? 541  PHE C CG  1 
ATOM   12979 C  CD1 . PHE C  1 524 ? -1.960  26.012  17.631  1.00 25.05 ? 541  PHE C CD1 1 
ATOM   12980 C  CD2 . PHE C  1 524 ? -2.759  24.941  15.653  1.00 24.87 ? 541  PHE C CD2 1 
ATOM   12981 C  CE1 . PHE C  1 524 ? -3.254  26.409  17.936  1.00 25.79 ? 541  PHE C CE1 1 
ATOM   12982 C  CE2 . PHE C  1 524 ? -4.050  25.340  15.964  1.00 25.53 ? 541  PHE C CE2 1 
ATOM   12983 C  CZ  . PHE C  1 524 ? -4.294  26.077  17.101  1.00 26.67 ? 541  PHE C CZ  1 
ATOM   12984 N  N   . ARG C  1 525 ? 2.563   25.728  14.115  1.00 22.27 ? 542  ARG C N   1 
ATOM   12985 C  CA  . ARG C  1 525 ? 4.000   25.534  13.973  1.00 23.16 ? 542  ARG C CA  1 
ATOM   12986 C  C   . ARG C  1 525 ? 4.697   26.883  14.139  1.00 24.11 ? 542  ARG C C   1 
ATOM   12987 O  O   . ARG C  1 525 ? 4.619   27.737  13.256  1.00 23.50 ? 542  ARG C O   1 
ATOM   12988 C  CB  . ARG C  1 525 ? 4.339   24.866  12.638  1.00 23.24 ? 542  ARG C CB  1 
ATOM   12989 C  CG  . ARG C  1 525 ? 5.760   24.329  12.523  1.00 24.34 ? 542  ARG C CG  1 
ATOM   12990 C  CD  . ARG C  1 525 ? 6.810   25.417  12.354  1.00 25.34 ? 542  ARG C CD  1 
ATOM   12991 N  NE  . ARG C  1 525 ? 8.107   24.827  12.010  1.00 26.05 ? 542  ARG C NE  1 
ATOM   12992 C  CZ  . ARG C  1 525 ? 9.294   25.410  12.133  1.00 27.59 ? 542  ARG C CZ  1 
ATOM   12993 N  NH1 . ARG C  1 525 ? 9.410   26.661  12.561  1.00 27.17 ? 542  ARG C NH1 1 
ATOM   12994 N  NH2 . ARG C  1 525 ? 10.373  24.716  11.824  1.00 27.62 ? 542  ARG C NH2 1 
ATOM   12995 N  N   . TYR C  1 526 ? 5.360   27.061  15.290  1.00 24.28 ? 543  TYR C N   1 
ATOM   12996 C  CA  . TYR C  1 526 ? 6.092   28.283  15.590  1.00 25.56 ? 543  TYR C CA  1 
ATOM   12997 C  C   . TYR C  1 526 ? 7.521   27.918  15.988  1.00 25.73 ? 543  TYR C C   1 
ATOM   12998 O  O   . TYR C  1 526 ? 7.730   26.881  16.615  1.00 25.35 ? 543  TYR C O   1 
ATOM   12999 C  CB  . TYR C  1 526 ? 5.362   29.075  16.677  1.00 26.75 ? 543  TYR C CB  1 
ATOM   13000 C  CG  . TYR C  1 526 ? 4.046   29.668  16.199  1.00 28.89 ? 543  TYR C CG  1 
ATOM   13001 C  CD1 . TYR C  1 526 ? 4.019   30.828  15.434  1.00 31.26 ? 543  TYR C CD1 1 
ATOM   13002 C  CD2 . TYR C  1 526 ? 2.833   29.059  16.496  1.00 30.31 ? 543  TYR C CD2 1 
ATOM   13003 C  CE1 . TYR C  1 526 ? 2.826   31.367  14.977  1.00 32.12 ? 543  TYR C CE1 1 
ATOM   13004 C  CE2 . TYR C  1 526 ? 1.634   29.591  16.051  1.00 31.37 ? 543  TYR C CE2 1 
ATOM   13005 C  CZ  . TYR C  1 526 ? 1.631   30.745  15.289  1.00 32.13 ? 543  TYR C CZ  1 
ATOM   13006 O  OH  . TYR C  1 526 ? 0.452   31.268  14.848  1.00 36.68 ? 543  TYR C OH  1 
ATOM   13007 N  N   . PRO C  1 527 ? 8.553   28.733  15.661  1.00 27.37 ? 544  PRO C N   1 
ATOM   13008 C  CA  . PRO C  1 527 ? 8.390   30.024  14.982  1.00 27.92 ? 544  PRO C CA  1 
ATOM   13009 C  C   . PRO C  1 527 ? 7.759   29.975  13.592  1.00 27.21 ? 544  PRO C C   1 
ATOM   13010 O  O   . PRO C  1 527 ? 7.987   29.030  12.837  1.00 26.25 ? 544  PRO C O   1 
ATOM   13011 C  CB  . PRO C  1 527 ? 9.834   30.568  14.884  1.00 28.61 ? 544  PRO C CB  1 
ATOM   13012 C  CG  . PRO C  1 527 ? 10.610  29.797  15.923  1.00 29.08 ? 544  PRO C CG  1 
ATOM   13013 C  CD  . PRO C  1 527 ? 9.958   28.435  15.970  1.00 28.18 ? 544  PRO C CD  1 
ATOM   13014 N  N   . GLU C  1 528 ? 7.003   31.032  13.266  1.00 28.03 ? 545  GLU C N   1 
ATOM   13015 C  CA  . GLU C  1 528 ? 6.402   31.215  11.952  1.00 27.85 ? 545  GLU C CA  1 
ATOM   13016 C  C   . GLU C  1 528 ? 7.475   31.625  10.948  1.00 29.07 ? 545  GLU C C   1 
ATOM   13017 O  O   . GLU C  1 528 ? 8.233   32.554  11.208  1.00 29.83 ? 545  GLU C O   1 
ATOM   13018 C  CB  . GLU C  1 528 ? 5.319   32.293  12.039  1.00 28.35 ? 545  GLU C CB  1 
ATOM   13019 C  CG  . GLU C  1 528 ? 4.760   32.736  10.688  1.00 28.97 ? 545  GLU C CG  1 
ATOM   13020 C  CD  . GLU C  1 528 ? 3.588   33.706  10.766  1.00 29.34 ? 545  GLU C CD  1 
ATOM   13021 O  OE1 . GLU C  1 528 ? 3.136   34.025  11.887  1.00 28.99 ? 545  GLU C OE1 1 
ATOM   13022 O  OE2 . GLU C  1 528 ? 3.132   34.150  9.689   1.00 28.45 ? 545  GLU C OE2 1 
ATOM   13023 N  N   . PRO C  1 529 ? 7.563   30.976  9.765   1.00 28.62 ? 546  PRO C N   1 
ATOM   13024 C  CA  . PRO C  1 529 ? 8.547   31.361  8.752   1.00 30.06 ? 546  PRO C CA  1 
ATOM   13025 C  C   . PRO C  1 529 ? 8.204   32.699  8.103   1.00 31.04 ? 546  PRO C C   1 
ATOM   13026 O  O   . PRO C  1 529 ? 7.038   32.988  7.854   1.00 29.13 ? 546  PRO C O   1 
ATOM   13027 C  CB  . PRO C  1 529 ? 8.479   30.200  7.753   1.00 29.90 ? 546  PRO C CB  1 
ATOM   13028 C  CG  . PRO C  1 529 ? 7.049   29.719  7.867   1.00 29.15 ? 546  PRO C CG  1 
ATOM   13029 C  CD  . PRO C  1 529 ? 6.723   29.844  9.339   1.00 28.63 ? 546  PRO C CD  1 
ATOM   13030 N  N   . GLU C  1 530 ? 9.233   33.508  7.832   1.00 32.88 ? 547  GLU C N   1 
ATOM   13031 C  CA  . GLU C  1 530 ? 9.042   34.798  7.191   1.00 35.36 ? 547  GLU C CA  1 
ATOM   13032 C  C   . GLU C  1 530 ? 8.709   34.585  5.715   1.00 33.49 ? 547  GLU C C   1 
ATOM   13033 O  O   . GLU C  1 530 ? 7.861   35.287  5.174   1.00 33.72 ? 547  GLU C O   1 
ATOM   13034 C  CB  . GLU C  1 530 ? 10.274  35.679  7.418   1.00 40.61 ? 547  GLU C CB  1 
ATOM   13035 C  CG  . GLU C  1 530 ? 10.524  35.971  8.897   1.00 46.16 ? 547  GLU C CG  1 
ATOM   13036 C  CD  . GLU C  1 530 ? 11.696  36.890  9.211   1.00 52.13 ? 547  GLU C CD  1 
ATOM   13037 O  OE1 . GLU C  1 530 ? 12.661  36.422  9.861   1.00 54.67 ? 547  GLU C OE1 1 
ATOM   13038 O  OE2 . GLU C  1 530 ? 11.636  38.077  8.819   1.00 56.38 ? 547  GLU C OE2 1 
ATOM   13039 N  N   . ASP C  1 531 ? 9.371   33.605  5.081   1.00 31.11 ? 548  ASP C N   1 
ATOM   13040 C  CA  . ASP C  1 531 ? 9.185   33.298  3.669   1.00 31.44 ? 548  ASP C CA  1 
ATOM   13041 C  C   . ASP C  1 531 ? 8.483   31.946  3.533   1.00 30.49 ? 548  ASP C C   1 
ATOM   13042 O  O   . ASP C  1 531 ? 9.111   30.901  3.689   1.00 28.87 ? 548  ASP C O   1 
ATOM   13043 C  CB  . ASP C  1 531 ? 10.521  33.311  2.942   1.00 32.48 ? 548  ASP C CB  1 
ATOM   13044 C  CG  . ASP C  1 531 ? 10.502  32.967  1.459   1.00 35.30 ? 548  ASP C CG  1 
ATOM   13045 O  OD1 . ASP C  1 531 ? 9.416   32.649  0.929   1.00 37.18 ? 548  ASP C OD1 1 
ATOM   13046 O  OD2 . ASP C  1 531 ? 11.583  33.029  0.836   1.00 37.84 ? 548  ASP C OD2 1 
ATOM   13047 N  N   . LYS C  1 532 ? 7.182   31.969  3.221   1.00 30.14 ? 549  LYS C N   1 
ATOM   13048 C  CA  . LYS C  1 532 ? 6.397   30.741  3.186   1.00 30.37 ? 549  LYS C CA  1 
ATOM   13049 C  C   . LYS C  1 532 ? 6.829   29.841  2.027   1.00 30.20 ? 549  LYS C C   1 
ATOM   13050 O  O   . LYS C  1 532 ? 6.833   28.623  2.175   1.00 31.09 ? 549  LYS C O   1 
ATOM   13051 C  CB  . LYS C  1 532 ? 4.889   31.015  3.172   1.00 29.27 ? 549  LYS C CB  1 
ATOM   13052 C  CG  . LYS C  1 532 ? 4.289   31.255  4.549   1.00 29.83 ? 549  LYS C CG  1 
ATOM   13053 C  CD  . LYS C  1 532 ? 4.789   32.513  5.249   1.00 29.58 ? 549  LYS C CD  1 
ATOM   13054 C  CE  . LYS C  1 532 ? 4.060   32.803  6.521   1.00 29.38 ? 549  LYS C CE  1 
ATOM   13055 N  NZ  . LYS C  1 532 ? 4.552   34.013  7.185   1.00 29.91 ? 549  LYS C NZ  1 
ATOM   13056 N  N   . ALA C  1 533 ? 7.213   30.426  0.887   1.00 29.96 ? 550  ALA C N   1 
ATOM   13057 C  CA  . ALA C  1 533 ? 7.607   29.635  -0.270  1.00 30.22 ? 550  ALA C CA  1 
ATOM   13058 C  C   . ALA C  1 533 ? 8.847   28.802  0.049   1.00 29.45 ? 550  ALA C C   1 
ATOM   13059 O  O   . ALA C  1 533 ? 8.909   27.616  -0.274  1.00 27.27 ? 550  ALA C O   1 
ATOM   13060 C  CB  . ALA C  1 533 ? 7.831   30.529  -1.472  1.00 30.79 ? 550  ALA C CB  1 
ATOM   13061 N  N   . LYS C  1 534 ? 9.831   29.433  0.695   1.00 29.08 ? 551  LYS C N   1 
ATOM   13062 C  CA  . LYS C  1 534 ? 11.062  28.766  1.084   1.00 29.87 ? 551  LYS C CA  1 
ATOM   13063 C  C   . LYS C  1 534 ? 10.764  27.651  2.084   1.00 27.67 ? 551  LYS C C   1 
ATOM   13064 O  O   . LYS C  1 534 ? 11.354  26.576  2.012   1.00 25.85 ? 551  LYS C O   1 
ATOM   13065 C  CB  . LYS C  1 534 ? 12.009  29.805  1.698   1.00 33.62 ? 551  LYS C CB  1 
ATOM   13066 C  CG  . LYS C  1 534 ? 13.352  29.284  2.191   1.00 36.73 ? 551  LYS C CG  1 
ATOM   13067 C  CD  . LYS C  1 534 ? 14.224  30.397  2.765   1.00 40.19 ? 551  LYS C CD  1 
ATOM   13068 C  CE  . LYS C  1 534 ? 15.666  30.023  2.893   1.00 43.09 ? 551  LYS C CE  1 
ATOM   13069 N  NZ  . LYS C  1 534 ? 15.913  29.164  4.052   1.00 45.84 ? 551  LYS C NZ  1 
ATOM   13070 N  N   . TYR C  1 535 ? 9.848   27.933  3.019   1.00 27.12 ? 552  TYR C N   1 
ATOM   13071 C  CA  . TYR C  1 535 ? 9.485   27.004  4.077   1.00 26.05 ? 552  TYR C CA  1 
ATOM   13072 C  C   . TYR C  1 535 ? 8.945   25.717  3.457   1.00 25.64 ? 552  TYR C C   1 
ATOM   13073 O  O   . TYR C  1 535 ? 9.399   24.630  3.803   1.00 25.91 ? 552  TYR C O   1 
ATOM   13074 C  CB  . TYR C  1 535 ? 8.482   27.688  5.012   1.00 25.68 ? 552  TYR C CB  1 
ATOM   13075 C  CG  . TYR C  1 535 ? 7.946   26.817  6.141   1.00 24.98 ? 552  TYR C CG  1 
ATOM   13076 C  CD1 . TYR C  1 535 ? 8.720   26.548  7.261   1.00 25.22 ? 552  TYR C CD1 1 
ATOM   13077 C  CD2 . TYR C  1 535 ? 6.664   26.280  6.096   1.00 24.55 ? 552  TYR C CD2 1 
ATOM   13078 C  CE1 . TYR C  1 535 ? 8.244   25.758  8.296   1.00 25.87 ? 552  TYR C CE1 1 
ATOM   13079 C  CE2 . TYR C  1 535 ? 6.173   25.493  7.127   1.00 24.37 ? 552  TYR C CE2 1 
ATOM   13080 C  CZ  . TYR C  1 535 ? 6.965   25.231  8.232   1.00 24.73 ? 552  TYR C CZ  1 
ATOM   13081 O  OH  . TYR C  1 535 ? 6.518   24.454  9.261   1.00 23.00 ? 552  TYR C OH  1 
ATOM   13082 N  N   . VAL C  1 536 ? 7.982   25.854  2.539   1.00 26.32 ? 553  VAL C N   1 
ATOM   13083 C  CA  . VAL C  1 536 ? 7.342   24.705  1.917   1.00 26.54 ? 553  VAL C CA  1 
ATOM   13084 C  C   . VAL C  1 536 ? 8.360   23.954  1.055   1.00 27.49 ? 553  VAL C C   1 
ATOM   13085 O  O   . VAL C  1 536 ? 8.523   22.746  1.211   1.00 26.76 ? 553  VAL C O   1 
ATOM   13086 C  CB  . VAL C  1 536 ? 6.096   25.114  1.108   1.00 26.89 ? 553  VAL C CB  1 
ATOM   13087 C  CG1 . VAL C  1 536 ? 5.539   23.956  0.286   1.00 27.08 ? 553  VAL C CG1 1 
ATOM   13088 C  CG2 . VAL C  1 536 ? 5.009   25.700  2.002   1.00 27.13 ? 553  VAL C CG2 1 
ATOM   13089 N  N   . LYS C  1 537 ? 9.069   24.671  0.174   1.00 27.60 ? 554  LYS C N   1 
ATOM   13090 C  CA  . LYS C  1 537 ? 9.938   24.030  -0.804  1.00 29.43 ? 554  LYS C CA  1 
ATOM   13091 C  C   . LYS C  1 537 ? 11.080  23.268  -0.130  1.00 29.12 ? 554  LYS C C   1 
ATOM   13092 O  O   . LYS C  1 537 ? 11.508  22.247  -0.656  1.00 30.77 ? 554  LYS C O   1 
ATOM   13093 C  CB  . LYS C  1 537 ? 10.471  25.016  -1.852  1.00 30.99 ? 554  LYS C CB  1 
ATOM   13094 C  CG  . LYS C  1 537 ? 9.401   25.551  -2.792  1.00 32.88 ? 554  LYS C CG  1 
ATOM   13095 C  CD  . LYS C  1 537 ? 9.893   26.492  -3.888  1.00 34.52 ? 554  LYS C CD  1 
ATOM   13096 C  CE  . LYS C  1 537 ? 8.747   26.994  -4.712  1.00 36.57 ? 554  LYS C CE  1 
ATOM   13097 N  NZ  . LYS C  1 537 ? 9.181   27.620  -5.962  1.00 38.23 ? 554  LYS C NZ  1 
ATOM   13098 N  N   . GLU C  1 538 ? 11.569  23.750  1.020   1.00 30.25 ? 555  GLU C N   1 
ATOM   13099 C  CA  . GLU C  1 538 ? 12.658  23.093  1.732   1.00 31.73 ? 555  GLU C CA  1 
ATOM   13100 C  C   . GLU C  1 538 ? 12.192  21.819  2.440   1.00 29.68 ? 555  GLU C C   1 
ATOM   13101 O  O   . GLU C  1 538 ? 13.023  21.005  2.840   1.00 29.46 ? 555  GLU C O   1 
ATOM   13102 C  CB  . GLU C  1 538 ? 13.294  24.016  2.773   1.00 36.10 ? 555  GLU C CB  1 
ATOM   13103 C  CG  . GLU C  1 538 ? 14.182  25.089  2.151   1.00 40.83 ? 555  GLU C CG  1 
ATOM   13104 C  CD  . GLU C  1 538 ? 14.822  26.048  3.138   1.00 44.03 ? 555  GLU C CD  1 
ATOM   13105 O  OE1 . GLU C  1 538 ? 14.473  26.047  4.339   1.00 45.41 ? 555  GLU C OE1 1 
ATOM   13106 O  OE2 . GLU C  1 538 ? 15.705  26.798  2.676   1.00 51.31 ? 555  GLU C OE2 1 
ATOM   13107 N  N   . ARG C  1 539 ? 10.875  21.637  2.600   1.00 27.28 ? 556  ARG C N   1 
ATOM   13108 C  CA  . ARG C  1 539 ? 10.357  20.513  3.364   1.00 24.90 ? 556  ARG C CA  1 
ATOM   13109 C  C   . ARG C  1 539 ? 9.781   19.413  2.469   1.00 24.41 ? 556  ARG C C   1 
ATOM   13110 O  O   . ARG C  1 539 ? 9.550   18.316  2.970   1.00 25.57 ? 556  ARG C O   1 
ATOM   13111 C  CB  . ARG C  1 539 ? 9.366   21.055  4.398   1.00 24.91 ? 556  ARG C CB  1 
ATOM   13112 C  CG  . ARG C  1 539 ? 10.107  21.706  5.557   1.00 25.86 ? 556  ARG C CG  1 
ATOM   13113 C  CD  . ARG C  1 539 ? 9.214   22.474  6.515   1.00 27.11 ? 556  ARG C CD  1 
ATOM   13114 N  NE  . ARG C  1 539 ? 10.005  23.082  7.593   1.00 28.61 ? 556  ARG C NE  1 
ATOM   13115 C  CZ  . ARG C  1 539 ? 10.906  24.058  7.451   1.00 29.41 ? 556  ARG C CZ  1 
ATOM   13116 N  NH1 . ARG C  1 539 ? 11.125  24.620  6.276   1.00 28.83 ? 556  ARG C NH1 1 
ATOM   13117 N  NH2 . ARG C  1 539 ? 11.589  24.478  8.498   1.00 30.46 ? 556  ARG C NH2 1 
ATOM   13118 N  N   . THR C  1 540 ? 9.586   19.683  1.167   1.00 23.01 ? 557  THR C N   1 
ATOM   13119 C  CA  A THR C  1 540 ? 9.021   18.691  0.263   0.66 23.52 ? 557  THR C CA  1 
ATOM   13120 C  CA  B THR C  1 540 ? 9.037   18.710  0.236   0.34 23.76 ? 557  THR C CA  1 
ATOM   13121 C  C   . THR C  1 540 ? 10.017  17.547  0.089   1.00 23.72 ? 557  THR C C   1 
ATOM   13122 O  O   . THR C  1 540 ? 11.218  17.762  -0.032  1.00 23.86 ? 557  THR C O   1 
ATOM   13123 C  CB  A THR C  1 540 ? 8.633   19.289  -1.090  0.66 23.69 ? 557  THR C CB  1 
ATOM   13124 C  CB  B THR C  1 540 ? 8.780   19.400  -1.105  0.34 24.14 ? 557  THR C CB  1 
ATOM   13125 O  OG1 A THR C  1 540 ? 9.761   19.994  -1.598  0.66 23.28 ? 557  THR C OG1 1 
ATOM   13126 O  OG1 B THR C  1 540 ? 8.013   20.570  -0.843  0.34 24.58 ? 557  THR C OG1 1 
ATOM   13127 C  CG2 A THR C  1 540 ? 7.463   20.248  -0.996  0.66 24.00 ? 557  THR C CG2 1 
ATOM   13128 C  CG2 B THR C  1 540 ? 8.010   18.529  -2.079  0.34 24.18 ? 557  THR C CG2 1 
ATOM   13129 N  N   . TRP C  1 541 ? 9.496   16.317  0.078   1.00 24.11 ? 558  TRP C N   1 
ATOM   13130 C  CA  . TRP C  1 541 ? 10.323  15.128  -0.070  1.00 23.98 ? 558  TRP C CA  1 
ATOM   13131 C  C   . TRP C  1 541 ? 10.756  14.982  -1.527  1.00 26.08 ? 558  TRP C C   1 
ATOM   13132 O  O   . TRP C  1 541 ? 9.952   15.193  -2.428  1.00 26.87 ? 558  TRP C O   1 
ATOM   13133 C  CB  . TRP C  1 541 ? 9.531   13.903  0.405   1.00 23.60 ? 558  TRP C CB  1 
ATOM   13134 C  CG  . TRP C  1 541 ? 10.240  12.583  0.252   1.00 22.95 ? 558  TRP C CG  1 
ATOM   13135 C  CD1 . TRP C  1 541 ? 11.066  11.981  1.154   1.00 22.80 ? 558  TRP C CD1 1 
ATOM   13136 C  CD2 . TRP C  1 541 ? 10.138  11.676  -0.867  1.00 21.88 ? 558  TRP C CD2 1 
ATOM   13137 N  NE1 . TRP C  1 541 ? 11.497  10.775  0.671   1.00 22.45 ? 558  TRP C NE1 1 
ATOM   13138 C  CE2 . TRP C  1 541 ? 10.941  10.557  -0.561  1.00 22.20 ? 558  TRP C CE2 1 
ATOM   13139 C  CE3 . TRP C  1 541 ? 9.450   11.702  -2.084  1.00 22.48 ? 558  TRP C CE3 1 
ATOM   13140 C  CZ2 . TRP C  1 541 ? 11.078  9.480   -1.435  1.00 22.99 ? 558  TRP C CZ2 1 
ATOM   13141 C  CZ3 . TRP C  1 541 ? 9.588   10.638  -2.950  1.00 23.11 ? 558  TRP C CZ3 1 
ATOM   13142 C  CH2 . TRP C  1 541 ? 10.387  9.538   -2.624  1.00 22.54 ? 558  TRP C CH2 1 
ATOM   13143 N  N   . ARG C  1 542 ? 12.020  14.597  -1.737  1.00 28.42 ? 559  ARG C N   1 
ATOM   13144 C  CA  . ARG C  1 542 ? 12.629  14.532  -3.058  1.00 30.75 ? 559  ARG C CA  1 
ATOM   13145 C  C   . ARG C  1 542 ? 12.907  13.075  -3.432  1.00 28.16 ? 559  ARG C C   1 
ATOM   13146 O  O   . ARG C  1 542 ? 13.371  12.299  -2.601  1.00 28.23 ? 559  ARG C O   1 
ATOM   13147 C  CB  . ARG C  1 542 ? 13.936  15.339  -3.052  1.00 35.81 ? 559  ARG C CB  1 
ATOM   13148 C  CG  . ARG C  1 542 ? 13.845  16.823  -2.708  1.00 40.34 ? 559  ARG C CG  1 
ATOM   13149 C  CD  . ARG C  1 542 ? 12.779  17.542  -3.523  1.00 45.48 ? 559  ARG C CD  1 
ATOM   13150 N  NE  . ARG C  1 542 ? 12.963  18.995  -3.651  1.00 51.77 ? 559  ARG C NE  1 
ATOM   13151 C  CZ  . ARG C  1 542 ? 12.933  19.910  -2.679  1.00 53.60 ? 559  ARG C CZ  1 
ATOM   13152 N  NH1 . ARG C  1 542 ? 12.832  19.561  -1.405  1.00 54.14 ? 559  ARG C NH1 1 
ATOM   13153 N  NH2 . ARG C  1 542 ? 13.017  21.192  -2.992  1.00 55.85 ? 559  ARG C NH2 1 
ATOM   13154 N  N   . SER C  1 543 ? 12.671  12.729  -4.703  1.00 26.72 ? 560  SER C N   1 
ATOM   13155 C  CA  . SER C  1 543 ? 12.797  11.356  -5.171  1.00 27.40 ? 560  SER C CA  1 
ATOM   13156 C  C   . SER C  1 543 ? 14.221  11.035  -5.635  1.00 25.56 ? 560  SER C C   1 
ATOM   13157 O  O   . SER C  1 543 ? 14.495  9.894   -5.997  1.00 24.58 ? 560  SER C O   1 
ATOM   13158 C  CB  . SER C  1 543 ? 11.808  11.068  -6.268  1.00 27.17 ? 560  SER C CB  1 
ATOM   13159 O  OG  . SER C  1 543 ? 12.080  11.868  -7.406  1.00 27.68 ? 560  SER C OG  1 
ATOM   13160 N  N   . GLU C  1 544 ? 15.121  12.026  -5.640  1.00 25.00 ? 561  GLU C N   1 
ATOM   13161 C  CA  . GLU C  1 544 ? 16.504  11.779  -6.019  1.00 25.58 ? 561  GLU C CA  1 
ATOM   13162 C  C   . GLU C  1 544 ? 17.175  10.912  -4.956  1.00 24.11 ? 561  GLU C C   1 
ATOM   13163 O  O   . GLU C  1 544 ? 16.911  11.060  -3.764  1.00 22.47 ? 561  GLU C O   1 
ATOM   13164 C  CB  . GLU C  1 544 ? 17.319  13.065  -6.174  1.00 28.82 ? 561  GLU C CB  1 
ATOM   13165 C  CG  . GLU C  1 544 ? 16.930  13.914  -7.384  1.00 32.06 ? 561  GLU C CG  1 
ATOM   13166 C  CD  . GLU C  1 544 ? 15.774  14.878  -7.164  1.00 36.54 ? 561  GLU C CD  1 
ATOM   13167 O  OE1 . GLU C  1 544 ? 15.260  14.956  -6.028  1.00 37.84 ? 561  GLU C OE1 1 
ATOM   13168 O  OE2 . GLU C  1 544 ? 15.381  15.557  -8.140  1.00 40.27 ? 561  GLU C OE2 1 
ATOM   13169 N  N   . TYR C  1 545 ? 18.064  10.025  -5.407  1.00 23.75 ? 562  TYR C N   1 
ATOM   13170 C  CA  . TYR C  1 545 ? 18.839  9.179   -4.519  1.00 24.92 ? 562  TYR C CA  1 
ATOM   13171 C  C   . TYR C  1 545 ? 19.772  10.034  -3.662  1.00 26.56 ? 562  TYR C C   1 
ATOM   13172 O  O   . TYR C  1 545 ? 20.315  11.036  -4.129  1.00 26.40 ? 562  TYR C O   1 
ATOM   13173 C  CB  . TYR C  1 545 ? 19.683  8.182   -5.318  1.00 23.68 ? 562  TYR C CB  1 
ATOM   13174 C  CG  . TYR C  1 545 ? 18.925  7.076   -6.037  1.00 22.94 ? 562  TYR C CG  1 
ATOM   13175 C  CD1 . TYR C  1 545 ? 17.886  6.387   -5.416  1.00 22.14 ? 562  TYR C CD1 1 
ATOM   13176 C  CD2 . TYR C  1 545 ? 19.264  6.712   -7.337  1.00 21.13 ? 562  TYR C CD2 1 
ATOM   13177 C  CE1 . TYR C  1 545 ? 17.210  5.365   -6.066  1.00 21.29 ? 562  TYR C CE1 1 
ATOM   13178 C  CE2 . TYR C  1 545 ? 18.593  5.697   -7.998  1.00 21.50 ? 562  TYR C CE2 1 
ATOM   13179 C  CZ  . TYR C  1 545 ? 17.562  5.024   -7.362  1.00 20.80 ? 562  TYR C CZ  1 
ATOM   13180 O  OH  . TYR C  1 545 ? 16.903  4.027   -8.011  1.00 19.51 ? 562  TYR C OH  1 
ATOM   13181 N  N   . ASP C  1 546 ? 19.950  9.607   -2.410  1.00 27.18 ? 563  ASP C N   1 
ATOM   13182 C  CA  . ASP C  1 546 ? 20.982  10.140  -1.537  1.00 29.82 ? 563  ASP C CA  1 
ATOM   13183 C  C   . ASP C  1 546 ? 22.225  9.262   -1.648  1.00 28.27 ? 563  ASP C C   1 
ATOM   13184 O  O   . ASP C  1 546 ? 22.154  8.130   -2.130  1.00 26.31 ? 563  ASP C O   1 
ATOM   13185 C  CB  . ASP C  1 546 ? 20.508  10.214  -0.091  1.00 32.17 ? 563  ASP C CB  1 
ATOM   13186 C  CG  . ASP C  1 546 ? 19.281  11.086  0.146   1.00 35.41 ? 563  ASP C CG  1 
ATOM   13187 O  OD1 . ASP C  1 546 ? 19.243  12.209  -0.404  1.00 37.22 ? 563  ASP C OD1 1 
ATOM   13188 O  OD2 . ASP C  1 546 ? 18.374  10.639  0.878   1.00 38.52 ? 563  ASP C OD2 1 
ATOM   13189 N  N   . SER C  1 547 ? 23.360  9.817   -1.212  1.00 27.06 ? 564  SER C N   1 
ATOM   13190 C  CA  . SER C  1 547 ? 24.577  9.048   -1.010  1.00 27.25 ? 564  SER C CA  1 
ATOM   13191 C  C   . SER C  1 547 ? 24.438  8.214   0.260   1.00 27.01 ? 564  SER C C   1 
ATOM   13192 O  O   . SER C  1 547 ? 23.983  8.722   1.284   1.00 27.21 ? 564  SER C O   1 
ATOM   13193 C  CB  . SER C  1 547 ? 25.783  9.953   -0.930  1.00 28.10 ? 564  SER C CB  1 
ATOM   13194 O  OG  . SER C  1 547 ? 26.941  9.234   -0.535  1.00 28.42 ? 564  SER C OG  1 
ATOM   13195 N  N   . LEU C  1 548 ? 24.843  6.940   0.185   1.00 25.85 ? 565  LEU C N   1 
ATOM   13196 C  CA  . LEU C  1 548 ? 24.859  6.062   1.345   1.00 26.65 ? 565  LEU C CA  1 
ATOM   13197 C  C   . LEU C  1 548 ? 26.293  5.638   1.666   1.00 25.96 ? 565  LEU C C   1 
ATOM   13198 O  O   . LEU C  1 548 ? 26.503  4.694   2.424   1.00 25.85 ? 565  LEU C O   1 
ATOM   13199 C  CB  . LEU C  1 548 ? 23.942  4.867   1.078   1.00 27.67 ? 565  LEU C CB  1 
ATOM   13200 C  CG  . LEU C  1 548 ? 22.449  5.186   0.933   1.00 28.81 ? 565  LEU C CG  1 
ATOM   13201 C  CD1 . LEU C  1 548 ? 21.677  3.974   0.436   1.00 30.09 ? 565  LEU C CD1 1 
ATOM   13202 C  CD2 . LEU C  1 548 ? 21.846  5.675   2.241   1.00 30.13 ? 565  LEU C CD2 1 
ATOM   13203 N  N   . LEU C  1 549 ? 27.271  6.376   1.120   1.00 24.24 ? 566  LEU C N   1 
ATOM   13204 C  CA  . LEU C  1 549 ? 28.683  6.080   1.311   1.00 24.68 ? 566  LEU C CA  1 
ATOM   13205 C  C   . LEU C  1 549 ? 29.120  6.491   2.718   1.00 23.76 ? 566  LEU C C   1 
ATOM   13206 O  O   . LEU C  1 549 ? 28.956  7.646   3.103   1.00 23.94 ? 566  LEU C O   1 
ATOM   13207 C  CB  . LEU C  1 549 ? 29.467  6.837   0.240   1.00 25.55 ? 566  LEU C CB  1 
ATOM   13208 C  CG  . LEU C  1 549 ? 30.971  6.555   0.172   1.00 27.74 ? 566  LEU C CG  1 
ATOM   13209 C  CD1 . LEU C  1 549 ? 31.232  5.152   -0.354  1.00 28.93 ? 566  LEU C CD1 1 
ATOM   13210 C  CD2 . LEU C  1 549 ? 31.676  7.596   -0.681  1.00 28.84 ? 566  LEU C CD2 1 
ATOM   13211 N  N   . PRO C  1 550 ? 29.700  5.575   3.528   1.00 23.70 ? 567  PRO C N   1 
ATOM   13212 C  CA  . PRO C  1 550 ? 30.325  5.952   4.798   1.00 23.83 ? 567  PRO C CA  1 
ATOM   13213 C  C   . PRO C  1 550 ? 31.384  7.035   4.601   1.00 24.65 ? 567  PRO C C   1 
ATOM   13214 O  O   . PRO C  1 550 ? 32.012  7.096   3.544   1.00 24.25 ? 567  PRO C O   1 
ATOM   13215 C  CB  . PRO C  1 550 ? 30.945  4.640   5.303   1.00 23.44 ? 567  PRO C CB  1 
ATOM   13216 C  CG  . PRO C  1 550 ? 30.142  3.559   4.629   1.00 24.00 ? 567  PRO C CG  1 
ATOM   13217 C  CD  . PRO C  1 550 ? 29.788  4.130   3.268   1.00 24.50 ? 567  PRO C CD  1 
ATOM   13218 N  N   . ASP C  1 551 ? 31.573  7.869   5.631   1.00 23.44 ? 568  ASP C N   1 
ATOM   13219 C  CA  . ASP C  1 551 ? 32.541  8.954   5.589   1.00 24.60 ? 568  ASP C CA  1 
ATOM   13220 C  C   . ASP C  1 551 ? 33.905  8.428   6.038   1.00 23.74 ? 568  ASP C C   1 
ATOM   13221 O  O   . ASP C  1 551 ? 34.138  8.235   7.232   1.00 22.25 ? 568  ASP C O   1 
ATOM   13222 C  CB  . ASP C  1 551 ? 32.066  10.139  6.417   1.00 26.04 ? 568  ASP C CB  1 
ATOM   13223 C  CG  . ASP C  1 551 ? 32.860  11.428  6.243   1.00 28.76 ? 568  ASP C CG  1 
ATOM   13224 O  OD1 . ASP C  1 551 ? 33.729  11.465  5.348   1.00 29.54 ? 568  ASP C OD1 1 
ATOM   13225 O  OD2 . ASP C  1 551 ? 32.605  12.390  7.008   1.00 30.93 ? 568  ASP C OD2 1 
ATOM   13226 N  N   . VAL C  1 552 ? 34.798  8.205   5.062   1.00 23.63 ? 569  VAL C N   1 
ATOM   13227 C  CA  . VAL C  1 552 ? 36.123  7.656   5.308   1.00 23.63 ? 569  VAL C CA  1 
ATOM   13228 C  C   . VAL C  1 552 ? 37.160  8.754   5.063   1.00 24.00 ? 569  VAL C C   1 
ATOM   13229 O  O   . VAL C  1 552 ? 37.161  9.395   4.011   1.00 23.65 ? 569  VAL C O   1 
ATOM   13230 C  CB  . VAL C  1 552 ? 36.384  6.422   4.419   1.00 24.45 ? 569  VAL C CB  1 
ATOM   13231 C  CG1 . VAL C  1 552 ? 37.775  5.832   4.637   1.00 25.37 ? 569  VAL C CG1 1 
ATOM   13232 C  CG2 . VAL C  1 552 ? 35.325  5.350   4.628   1.00 24.84 ? 569  VAL C CG2 1 
ATOM   13233 N  N   . TYR C  1 553 ? 38.039  8.962   6.051   1.00 23.92 ? 570  TYR C N   1 
ATOM   13234 C  CA  . TYR C  1 553 ? 38.991  10.060  6.024   1.00 24.81 ? 570  TYR C CA  1 
ATOM   13235 C  C   . TYR C  1 553 ? 40.168  9.744   6.938   1.00 26.44 ? 570  TYR C C   1 
ATOM   13236 O  O   . TYR C  1 553 ? 40.032  9.023   7.928   1.00 26.65 ? 570  TYR C O   1 
ATOM   13237 C  CB  . TYR C  1 553 ? 38.334  11.375  6.456   1.00 24.45 ? 570  TYR C CB  1 
ATOM   13238 C  CG  . TYR C  1 553 ? 37.658  11.357  7.824   1.00 24.24 ? 570  TYR C CG  1 
ATOM   13239 C  CD1 . TYR C  1 553 ? 36.339  10.942  7.967   1.00 24.16 ? 570  TYR C CD1 1 
ATOM   13240 C  CD2 . TYR C  1 553 ? 38.328  11.776  8.969   1.00 24.71 ? 570  TYR C CD2 1 
ATOM   13241 C  CE1 . TYR C  1 553 ? 35.709  10.929  9.202   1.00 24.08 ? 570  TYR C CE1 1 
ATOM   13242 C  CE2 . TYR C  1 553 ? 37.709  11.770  10.210  1.00 24.95 ? 570  TYR C CE2 1 
ATOM   13243 C  CZ  . TYR C  1 553 ? 36.395  11.345  10.329  1.00 25.07 ? 570  TYR C CZ  1 
ATOM   13244 O  OH  . TYR C  1 553 ? 35.792  11.331  11.556  1.00 26.14 ? 570  TYR C OH  1 
ATOM   13245 N  N   . GLU C  1 554 ? 41.320  10.330  6.599   1.00 28.95 ? 571  GLU C N   1 
ATOM   13246 C  CA  . GLU C  1 554 ? 42.527  10.168  7.387   1.00 30.88 ? 571  GLU C CA  1 
ATOM   13247 C  C   . GLU C  1 554 ? 42.450  11.079  8.607   1.00 28.96 ? 571  GLU C C   1 
ATOM   13248 O  O   . GLU C  1 554 ? 42.015  12.223  8.517   1.00 27.73 ? 571  GLU C O   1 
ATOM   13249 C  CB  . GLU C  1 554 ? 43.765  10.500  6.548   1.00 34.43 ? 571  GLU C CB  1 
ATOM   13250 C  CG  . GLU C  1 554 ? 44.002  9.520   5.401   1.00 37.79 ? 571  GLU C CG  1 
ATOM   13251 C  CD  . GLU C  1 554 ? 44.416  8.117   5.823   1.00 43.38 ? 571  GLU C CD  1 
ATOM   13252 O  OE1 . GLU C  1 554 ? 44.265  7.182   5.003   1.00 46.68 ? 571  GLU C OE1 1 
ATOM   13253 O  OE2 . GLU C  1 554 ? 44.910  7.953   6.961   1.00 46.99 ? 571  GLU C OE2 1 
ATOM   13254 N  N   . TRP C  1 555 ? 42.871  10.551  9.755   1.00 28.78 ? 572  TRP C N   1 
ATOM   13255 C  CA  . TRP C  1 555 ? 43.233  11.392  10.880  1.00 29.82 ? 572  TRP C CA  1 
ATOM   13256 C  C   . TRP C  1 555 ? 44.636  11.933  10.632  1.00 33.13 ? 572  TRP C C   1 
ATOM   13257 O  O   . TRP C  1 555 ? 45.474  11.207  10.114  1.00 33.73 ? 572  TRP C O   1 
ATOM   13258 C  CB  . TRP C  1 555 ? 43.196  10.598  12.191  1.00 28.27 ? 572  TRP C CB  1 
ATOM   13259 C  CG  . TRP C  1 555 ? 41.844  10.490  12.844  1.00 27.42 ? 572  TRP C CG  1 
ATOM   13260 C  CD1 . TRP C  1 555 ? 40.670  11.083  12.486  1.00 26.67 ? 572  TRP C CD1 1 
ATOM   13261 C  CD2 . TRP C  1 555 ? 41.570  9.750   14.050  1.00 27.18 ? 572  TRP C CD2 1 
ATOM   13262 N  NE1 . TRP C  1 555 ? 39.681  10.751  13.377  1.00 27.56 ? 572  TRP C NE1 1 
ATOM   13263 C  CE2 . TRP C  1 555 ? 40.206  9.940   14.349  1.00 27.39 ? 572  TRP C CE2 1 
ATOM   13264 C  CE3 . TRP C  1 555 ? 42.346  8.949   14.896  1.00 29.35 ? 572  TRP C CE3 1 
ATOM   13265 C  CZ2 . TRP C  1 555 ? 39.605  9.352   15.460  1.00 29.09 ? 572  TRP C CZ2 1 
ATOM   13266 C  CZ3 . TRP C  1 555 ? 41.748  8.368   15.993  1.00 30.91 ? 572  TRP C CZ3 1 
ATOM   13267 C  CH2 . TRP C  1 555 ? 40.397  8.572   16.270  1.00 29.09 ? 572  TRP C CH2 1 
ATOM   13268 N  N   . PRO C  1 556 ? 44.949  13.198  10.982  1.00 38.43 ? 573  PRO C N   1 
ATOM   13269 C  CA  . PRO C  1 556 ? 46.340  13.663  10.968  1.00 43.06 ? 573  PRO C CA  1 
ATOM   13270 C  C   . PRO C  1 556 ? 47.338  12.623  11.486  1.00 47.18 ? 573  PRO C C   1 
ATOM   13271 O  O   . PRO C  1 556 ? 48.316  12.324  10.803  1.00 51.29 ? 573  PRO C O   1 
ATOM   13272 C  CB  . PRO C  1 556 ? 46.271  14.912  11.850  1.00 42.26 ? 573  PRO C CB  1 
ATOM   13273 C  CG  . PRO C  1 556 ? 44.894  15.475  11.548  1.00 43.40 ? 573  PRO C CG  1 
ATOM   13274 C  CD  . PRO C  1 556 ? 43.998  14.249  11.377  1.00 41.01 ? 573  PRO C CD  1 
ATOM   13275 N  N   . GLU C  1 557 ? 47.063  12.061  12.676  1.00 48.63 ? 574  GLU C N   1 
ATOM   13276 C  CA  . GLU C  1 557 ? 47.865  10.999  13.274  1.00 47.75 ? 574  GLU C CA  1 
ATOM   13277 C  C   . GLU C  1 557 ? 49.328  11.433  13.395  1.00 47.99 ? 574  GLU C C   1 
ATOM   13278 O  O   . GLU C  1 557 ? 50.245  10.634  13.194  1.00 44.67 ? 574  GLU C O   1 
ATOM   13279 C  CB  . GLU C  1 557 ? 47.742  9.684   12.496  1.00 50.00 ? 574  GLU C CB  1 
ATOM   13280 C  CG  . GLU C  1 557 ? 46.456  8.914   12.781  1.00 52.12 ? 574  GLU C CG  1 
ATOM   13281 C  CD  . GLU C  1 557 ? 46.336  7.577   12.067  1.00 56.75 ? 574  GLU C CD  1 
ATOM   13282 O  OE1 . GLU C  1 557 ? 47.214  7.255   11.234  1.00 60.54 ? 574  GLU C OE1 1 
ATOM   13283 O  OE2 . GLU C  1 557 ? 45.362  6.845   12.354  1.00 57.62 ? 574  GLU C OE2 1 
ATOM   13284 N  N   . SER C  1 558 ? 49.531  12.704  13.756  1.00 48.87 ? 575  SER C N   1 
ATOM   13285 C  CA  . SER C  1 558 ? 50.862  13.281  13.868  1.00 48.83 ? 575  SER C CA  1 
ATOM   13286 C  C   . SER C  1 558 ? 51.049  13.859  15.279  1.00 47.45 ? 575  SER C C   1 
ATOM   13287 O  O   . SER C  1 558 ? 52.202  14.203  15.608  1.00 46.71 ? 575  SER C O   1 
ATOM   13288 C  CB  . SER C  1 558 ? 51.082  14.325  12.801  1.00 47.66 ? 575  SER C CB  1 
ATOM   13289 O  OG  . SER C  1 558 ? 49.977  15.218  12.738  1.00 50.90 ? 575  SER C OG  1 
ATOM   13290 N  N   . SER C  1 560 ? 52.071  12.887  19.174  1.00 54.97 ? 577  SER C N   1 
ATOM   13291 C  CA  . SER C  1 560 ? 53.003  11.942  19.847  1.00 54.92 ? 577  SER C CA  1 
ATOM   13292 C  C   . SER C  1 560 ? 52.341  10.573  19.959  1.00 54.25 ? 577  SER C C   1 
ATOM   13293 O  O   . SER C  1 560 ? 51.126  10.484  20.121  1.00 53.89 ? 577  SER C O   1 
ATOM   13294 C  CB  . SER C  1 560 ? 53.426  12.444  21.210  1.00 55.09 ? 577  SER C CB  1 
ATOM   13295 O  OG  . SER C  1 560 ? 54.027  13.729  21.124  1.00 57.33 ? 577  SER C OG  1 
ATOM   13296 N  N   . SER C  1 561 ? 53.156  9.516   19.874  1.00 51.05 ? 578  SER C N   1 
ATOM   13297 C  CA  . SER C  1 561 ? 52.670  8.163   20.080  1.00 50.06 ? 578  SER C CA  1 
ATOM   13298 C  C   . SER C  1 561 ? 52.328  7.971   21.553  1.00 48.47 ? 578  SER C C   1 
ATOM   13299 O  O   . SER C  1 561 ? 52.772  8.744   22.400  1.00 45.74 ? 578  SER C O   1 
ATOM   13300 C  CB  . SER C  1 561 ? 53.678  7.130   19.627  1.00 49.80 ? 578  SER C CB  1 
ATOM   13301 O  OG  . SER C  1 561 ? 53.832  7.137   18.215  1.00 48.51 ? 578  SER C OG  1 
ATOM   13302 N  N   . PRO C  1 562 ? 51.530  6.938   21.901  1.00 51.80 ? 579  PRO C N   1 
ATOM   13303 C  CA  . PRO C  1 562 ? 51.375  6.524   23.294  1.00 53.33 ? 579  PRO C CA  1 
ATOM   13304 C  C   . PRO C  1 562 ? 52.721  6.117   23.892  1.00 51.15 ? 579  PRO C C   1 
ATOM   13305 O  O   . PRO C  1 562 ? 53.657  5.784   23.167  1.00 49.17 ? 579  PRO C O   1 
ATOM   13306 C  CB  . PRO C  1 562 ? 50.387  5.334   23.234  1.00 53.81 ? 579  PRO C CB  1 
ATOM   13307 C  CG  . PRO C  1 562 ? 49.711  5.456   21.880  1.00 53.37 ? 579  PRO C CG  1 
ATOM   13308 C  CD  . PRO C  1 562 ? 50.731  6.122   20.976  1.00 53.20 ? 579  PRO C CD  1 
ATOM   13309 N  N   . PRO C  1 563 ? 52.857  6.134   25.234  1.00 51.60 ? 580  PRO C N   1 
ATOM   13310 C  CA  . PRO C  1 563 ? 54.032  5.567   25.898  1.00 51.88 ? 580  PRO C CA  1 
ATOM   13311 C  C   . PRO C  1 563 ? 54.006  4.042   25.852  1.00 51.49 ? 580  PRO C C   1 
ATOM   13312 O  O   . PRO C  1 563 ? 55.037  3.457   25.469  1.00 53.01 ? 580  PRO C O   1 
ATOM   13313 C  CB  . PRO C  1 563 ? 53.885  6.112   27.322  1.00 52.14 ? 580  PRO C CB  1 
ATOM   13314 C  CG  . PRO C  1 563 ? 52.388  6.179   27.510  1.00 53.09 ? 580  PRO C CG  1 
ATOM   13315 C  CD  . PRO C  1 563 ? 51.875  6.689   26.180  1.00 52.68 ? 580  PRO C CD  1 
ATOM   13316 N  N   . GLU D  1 6   ? 14.874  -2.739  7.056   1.00 49.00 ? 23   GLU D N   1 
ATOM   13317 C  CA  . GLU D  1 6   ? 13.449  -2.699  6.624   1.00 48.04 ? 23   GLU D CA  1 
ATOM   13318 C  C   . GLU D  1 6   ? 12.551  -2.799  7.855   1.00 48.90 ? 23   GLU D C   1 
ATOM   13319 O  O   . GLU D  1 6   ? 12.595  -3.795  8.573   1.00 48.98 ? 23   GLU D O   1 
ATOM   13320 C  CB  . GLU D  1 6   ? 13.151  -3.816  5.621   1.00 46.16 ? 23   GLU D CB  1 
ATOM   13321 C  CG  . GLU D  1 6   ? 11.807  -3.665  4.911   1.00 44.85 ? 23   GLU D CG  1 
ATOM   13322 C  CD  . GLU D  1 6   ? 11.543  -4.714  3.843   1.00 44.19 ? 23   GLU D CD  1 
ATOM   13323 O  OE1 . GLU D  1 6   ? 12.353  -5.661  3.723   1.00 45.28 ? 23   GLU D OE1 1 
ATOM   13324 O  OE2 . GLU D  1 6   ? 10.532  -4.581  3.121   1.00 39.86 ? 23   GLU D OE2 1 
ATOM   13325 N  N   . LYS D  1 7   ? 11.749  -1.753  8.092   1.00 48.88 ? 24   LYS D N   1 
ATOM   13326 C  CA  . LYS D  1 7   ? 10.867  -1.697  9.247   1.00 49.33 ? 24   LYS D CA  1 
ATOM   13327 C  C   . LYS D  1 7   ? 9.672   -2.622  9.023   1.00 46.18 ? 24   LYS D C   1 
ATOM   13328 O  O   . LYS D  1 7   ? 9.030   -2.581  7.973   1.00 41.23 ? 24   LYS D O   1 
ATOM   13329 C  CB  . LYS D  1 7   ? 10.421  -0.259  9.540   1.00 51.60 ? 24   LYS D CB  1 
ATOM   13330 C  CG  . LYS D  1 7   ? 11.466  0.592   10.253  1.00 55.00 ? 24   LYS D CG  1 
ATOM   13331 C  CD  . LYS D  1 7   ? 11.044  2.032   10.526  1.00 56.55 ? 24   LYS D CD  1 
ATOM   13332 C  CE  . LYS D  1 7   ? 11.833  2.672   11.627  1.00 58.87 ? 24   LYS D CE  1 
ATOM   13333 N  NZ  . LYS D  1 7   ? 13.282  2.569   11.429  1.00 60.94 ? 24   LYS D NZ  1 
ATOM   13334 N  N   . GLY D  1 8   ? 9.388   -3.445  10.040  1.00 43.76 ? 25   GLY D N   1 
ATOM   13335 C  CA  . GLY D  1 8   ? 8.295   -4.403  10.006  1.00 43.56 ? 25   GLY D CA  1 
ATOM   13336 C  C   . GLY D  1 8   ? 8.679   -5.680  10.745  1.00 43.17 ? 25   GLY D C   1 
ATOM   13337 O  O   . GLY D  1 8   ? 9.768   -5.766  11.308  1.00 44.11 ? 25   GLY D O   1 
ATOM   13338 N  N   . LYS D  1 9   ? 7.779   -6.670  10.728  1.00 42.13 ? 26   LYS D N   1 
ATOM   13339 C  CA  . LYS D  1 9   ? 8.010   -7.925  11.424  1.00 41.85 ? 26   LYS D CA  1 
ATOM   13340 C  C   . LYS D  1 9   ? 8.815   -8.859  10.520  1.00 41.23 ? 26   LYS D C   1 
ATOM   13341 O  O   . LYS D  1 9   ? 8.389   -9.173  9.412   1.00 38.91 ? 26   LYS D O   1 
ATOM   13342 C  CB  . LYS D  1 9   ? 6.668   -8.503  11.884  1.00 43.18 ? 26   LYS D CB  1 
ATOM   13343 C  CG  . LYS D  1 9   ? 5.907   -7.629  12.878  1.00 44.68 ? 26   LYS D CG  1 
ATOM   13344 C  CD  . LYS D  1 9   ? 6.689   -7.293  14.144  1.00 46.91 ? 26   LYS D CD  1 
ATOM   13345 C  CE  . LYS D  1 9   ? 5.819   -6.848  15.280  1.00 48.82 ? 26   LYS D CE  1 
ATOM   13346 N  NZ  . LYS D  1 9   ? 4.947   -5.717  14.939  1.00 49.66 ? 26   LYS D NZ  1 
ATOM   13347 N  N   . PRO D  1 10  ? 10.016  -9.307  10.958  1.00 41.51 ? 27   PRO D N   1 
ATOM   13348 C  CA  . PRO D  1 10  ? 10.860  -10.199 10.153  1.00 42.83 ? 27   PRO D CA  1 
ATOM   13349 C  C   . PRO D  1 10  ? 10.189  -11.402 9.482   1.00 40.01 ? 27   PRO D C   1 
ATOM   13350 O  O   . PRO D  1 10  ? 10.486  -11.715 8.331   1.00 35.92 ? 27   PRO D O   1 
ATOM   13351 C  CB  . PRO D  1 10  ? 11.905  -10.664 11.187  1.00 43.77 ? 27   PRO D CB  1 
ATOM   13352 C  CG  . PRO D  1 10  ? 12.032  -9.513  12.155  1.00 44.03 ? 27   PRO D CG  1 
ATOM   13353 C  CD  . PRO D  1 10  ? 10.641  -8.927  12.237  1.00 43.45 ? 27   PRO D CD  1 
ATOM   13354 N  N   . LEU D  1 11  ? 9.295   -12.080 10.215  1.00 38.64 ? 28   LEU D N   1 
ATOM   13355 C  CA  . LEU D  1 11  ? 8.690   -13.319 9.742   1.00 36.99 ? 28   LEU D CA  1 
ATOM   13356 C  C   . LEU D  1 11  ? 7.837   -13.056 8.503   1.00 34.88 ? 28   LEU D C   1 
ATOM   13357 O  O   . LEU D  1 11  ? 7.699   -13.929 7.652   1.00 32.48 ? 28   LEU D O   1 
ATOM   13358 C  CB  . LEU D  1 11  ? 7.875   -13.970 10.857  1.00 37.88 ? 28   LEU D CB  1 
ATOM   13359 C  CG  . LEU D  1 11  ? 8.679   -14.622 11.987  1.00 39.15 ? 28   LEU D CG  1 
ATOM   13360 C  CD1 . LEU D  1 11  ? 7.744   -15.123 13.073  1.00 38.86 ? 28   LEU D CD1 1 
ATOM   13361 C  CD2 . LEU D  1 11  ? 9.559   -15.760 11.481  1.00 39.93 ? 28   LEU D CD2 1 
ATOM   13362 N  N   . MET D  1 12  ? 7.289   -11.841 8.413   1.00 33.14 ? 29   MET D N   1 
ATOM   13363 C  CA  . MET D  1 12  ? 6.421   -11.423 7.326   1.00 32.29 ? 29   MET D CA  1 
ATOM   13364 C  C   . MET D  1 12  ? 7.255   -10.947 6.136   1.00 29.48 ? 29   MET D C   1 
ATOM   13365 O  O   . MET D  1 12  ? 6.919   -11.214 4.985   1.00 27.55 ? 29   MET D O   1 
ATOM   13366 C  CB  . MET D  1 12  ? 5.534   -10.282 7.839   1.00 35.39 ? 29   MET D CB  1 
ATOM   13367 C  CG  . MET D  1 12  ? 4.308   -9.988  7.022   1.00 37.61 ? 29   MET D CG  1 
ATOM   13368 S  SD  . MET D  1 12  ? 3.380   -8.629  7.767   1.00 36.70 ? 29   MET D SD  1 
ATOM   13369 C  CE  . MET D  1 12  ? 2.199   -8.452  6.425   1.00 35.28 ? 29   MET D CE  1 
ATOM   13370 N  N   . LEU D  1 13  ? 8.341   -10.220 6.420   1.00 28.42 ? 30   LEU D N   1 
ATOM   13371 C  CA  . LEU D  1 13  ? 9.151   -9.606  5.377   1.00 28.58 ? 30   LEU D CA  1 
ATOM   13372 C  C   . LEU D  1 13  ? 10.084  -10.623 4.714   1.00 27.29 ? 30   LEU D C   1 
ATOM   13373 O  O   . LEU D  1 13  ? 10.487  -10.431 3.569   1.00 25.81 ? 30   LEU D O   1 
ATOM   13374 C  CB  . LEU D  1 13  ? 9.939   -8.458  6.007   1.00 28.87 ? 30   LEU D CB  1 
ATOM   13375 C  CG  . LEU D  1 13  ? 9.103   -7.311  6.582   1.00 29.57 ? 30   LEU D CG  1 
ATOM   13376 C  CD1 . LEU D  1 13  ? 10.013  -6.339  7.307   1.00 30.60 ? 30   LEU D CD1 1 
ATOM   13377 C  CD2 . LEU D  1 13  ? 8.296   -6.600  5.500   1.00 29.93 ? 30   LEU D CD2 1 
ATOM   13378 N  N   . ASN D  1 14  ? 10.442  -11.685 5.442   1.00 27.13 ? 31   ASN D N   1 
ATOM   13379 C  CA  . ASN D  1 14  ? 11.361  -12.698 4.940   1.00 26.12 ? 31   ASN D CA  1 
ATOM   13380 C  C   . ASN D  1 14  ? 10.591  -13.705 4.087   1.00 25.30 ? 31   ASN D C   1 
ATOM   13381 O  O   . ASN D  1 14  ? 9.786   -14.470 4.613   1.00 24.15 ? 31   ASN D O   1 
ATOM   13382 C  CB  . ASN D  1 14  ? 12.083  -13.394 6.086   1.00 26.79 ? 31   ASN D CB  1 
ATOM   13383 C  CG  . ASN D  1 14  ? 13.079  -14.431 5.618   1.00 28.35 ? 31   ASN D CG  1 
ATOM   13384 O  OD1 . ASN D  1 14  ? 13.249  -14.655 4.414   1.00 28.20 ? 31   ASN D OD1 1 
ATOM   13385 N  ND2 . ASN D  1 14  ? 13.752  -15.073 6.560   1.00 32.22 ? 31   ASN D ND2 1 
ATOM   13386 N  N   . PRO D  1 15  ? 10.817  -13.765 2.756   1.00 24.88 ? 32   PRO D N   1 
ATOM   13387 C  CA  . PRO D  1 15  ? 10.099  -14.717 1.908   1.00 25.74 ? 32   PRO D CA  1 
ATOM   13388 C  C   . PRO D  1 15  ? 10.262  -16.181 2.310   1.00 25.85 ? 32   PRO D C   1 
ATOM   13389 O  O   . PRO D  1 15  ? 9.424   -17.011 1.969   1.00 26.08 ? 32   PRO D O   1 
ATOM   13390 C  CB  . PRO D  1 15  ? 10.645  -14.443 0.499   1.00 26.46 ? 32   PRO D CB  1 
ATOM   13391 C  CG  . PRO D  1 15  ? 11.955  -13.741 0.738   1.00 27.26 ? 32   PRO D CG  1 
ATOM   13392 C  CD  . PRO D  1 15  ? 11.753  -12.927 1.994   1.00 26.43 ? 32   PRO D CD  1 
ATOM   13393 N  N   . ARG D  1 16  ? 11.331  -16.495 3.050   1.00 27.10 ? 33   ARG D N   1 
ATOM   13394 C  CA  . ARG D  1 16  ? 11.588  -17.861 3.473   1.00 28.84 ? 33   ARG D CA  1 
ATOM   13395 C  C   . ARG D  1 16  ? 10.577  -18.318 4.527   1.00 27.58 ? 33   ARG D C   1 
ATOM   13396 O  O   . ARG D  1 16  ? 10.256  -19.504 4.583   1.00 28.47 ? 33   ARG D O   1 
ATOM   13397 C  CB  . ARG D  1 16  ? 13.044  -17.965 3.935   1.00 31.09 ? 33   ARG D CB  1 
ATOM   13398 C  CG  . ARG D  1 16  ? 13.535  -19.388 4.142   1.00 34.33 ? 33   ARG D CG  1 
ATOM   13399 C  CD  . ARG D  1 16  ? 15.013  -19.502 3.792   1.00 36.64 ? 33   ARG D CD  1 
ATOM   13400 N  NE  . ARG D  1 16  ? 15.215  -19.413 2.340   1.00 38.29 ? 33   ARG D NE  1 
ATOM   13401 C  CZ  . ARG D  1 16  ? 16.169  -18.756 1.681   1.00 38.73 ? 33   ARG D CZ  1 
ATOM   13402 N  NH1 . ARG D  1 16  ? 17.106  -18.092 2.331   1.00 41.70 ? 33   ARG D NH1 1 
ATOM   13403 N  NH2 . ARG D  1 16  ? 16.202  -18.801 0.359   1.00 38.92 ? 33   ARG D NH2 1 
ATOM   13404 N  N   . THR D  1 17  ? 10.074  -17.387 5.352   1.00 26.43 ? 34   THR D N   1 
ATOM   13405 C  CA  . THR D  1 17  ? 9.174   -17.727 6.447   1.00 25.15 ? 34   THR D CA  1 
ATOM   13406 C  C   . THR D  1 17  ? 7.765   -17.171 6.208   1.00 23.83 ? 34   THR D C   1 
ATOM   13407 O  O   . THR D  1 17  ? 6.820   -17.625 6.851   1.00 23.76 ? 34   THR D O   1 
ATOM   13408 C  CB  . THR D  1 17  ? 9.736   -17.219 7.777   1.00 25.56 ? 34   THR D CB  1 
ATOM   13409 O  OG1 . THR D  1 17  ? 9.966   -15.819 7.654   1.00 24.38 ? 34   THR D OG1 1 
ATOM   13410 C  CG2 . THR D  1 17  ? 11.034  -17.899 8.181   1.00 26.74 ? 34   THR D CG2 1 
ATOM   13411 N  N   . ASN D  1 18  ? 7.627   -16.186 5.313   1.00 22.29 ? 35   ASN D N   1 
ATOM   13412 C  CA  . ASN D  1 18  ? 6.363   -15.494 5.087   1.00 22.23 ? 35   ASN D CA  1 
ATOM   13413 C  C   . ASN D  1 18  ? 5.302   -16.465 4.565   1.00 23.15 ? 35   ASN D C   1 
ATOM   13414 O  O   . ASN D  1 18  ? 5.546   -17.211 3.617   1.00 23.30 ? 35   ASN D O   1 
ATOM   13415 C  CB  . ASN D  1 18  ? 6.553   -14.315 4.137   1.00 22.01 ? 35   ASN D CB  1 
ATOM   13416 C  CG  . ASN D  1 18  ? 5.259   -13.604 3.806   1.00 21.42 ? 35   ASN D CG  1 
ATOM   13417 O  OD1 . ASN D  1 18  ? 4.445   -13.358 4.702   1.00 20.82 ? 35   ASN D OD1 1 
ATOM   13418 N  ND2 . ASN D  1 18  ? 5.051   -13.274 2.538   1.00 20.91 ? 35   ASN D ND2 1 
ATOM   13419 N  N   . LYS D  1 19  ? 4.118   -16.422 5.197   1.00 23.08 ? 36   LYS D N   1 
ATOM   13420 C  CA  . LYS D  1 19  ? 2.971   -17.233 4.821   1.00 22.90 ? 36   LYS D CA  1 
ATOM   13421 C  C   . LYS D  1 19  ? 1.851   -16.368 4.233   1.00 21.62 ? 36   LYS D C   1 
ATOM   13422 O  O   . LYS D  1 19  ? 0.872   -16.902 3.716   1.00 20.92 ? 36   LYS D O   1 
ATOM   13423 C  CB  . LYS D  1 19  ? 2.453   -17.977 6.059   1.00 23.91 ? 36   LYS D CB  1 
ATOM   13424 C  CG  . LYS D  1 19  ? 3.408   -19.013 6.639   1.00 25.25 ? 36   LYS D CG  1 
ATOM   13425 C  CD  . LYS D  1 19  ? 3.068   -19.500 8.044   1.00 26.68 ? 36   LYS D CD  1 
ATOM   13426 C  CE  . LYS D  1 19  ? 1.731   -20.139 8.167   1.00 28.83 ? 36   LYS D CE  1 
ATOM   13427 N  NZ  . LYS D  1 19  ? 1.587   -20.825 9.456   1.00 29.13 ? 36   LYS D NZ  1 
ATOM   13428 N  N   . GLY D  1 20  ? 1.990   -15.039 4.322   1.00 20.88 ? 37   GLY D N   1 
ATOM   13429 C  CA  . GLY D  1 20  ? 0.973   -14.114 3.841   1.00 20.81 ? 37   GLY D CA  1 
ATOM   13430 C  C   . GLY D  1 20  ? -0.363  -14.343 4.544   1.00 20.68 ? 37   GLY D C   1 
ATOM   13431 O  O   . GLY D  1 20  ? -0.426  -14.444 5.763   1.00 20.49 ? 37   GLY D O   1 
ATOM   13432 N  N   . MET D  1 21  ? -1.431  -14.486 3.760   1.00 22.49 ? 38   MET D N   1 
ATOM   13433 C  CA  . MET D  1 21  ? -2.763  -14.626 4.327   1.00 23.54 ? 38   MET D CA  1 
ATOM   13434 C  C   . MET D  1 21  ? -2.985  -16.002 4.952   1.00 22.81 ? 38   MET D C   1 
ATOM   13435 O  O   . MET D  1 21  ? -4.033  -16.233 5.550   1.00 22.53 ? 38   MET D O   1 
ATOM   13436 C  CB  . MET D  1 21  ? -3.824  -14.342 3.267   1.00 25.77 ? 38   MET D CB  1 
ATOM   13437 C  CG  . MET D  1 21  ? -3.993  -12.861 3.048   1.00 27.95 ? 38   MET D CG  1 
ATOM   13438 S  SD  . MET D  1 21  ? -5.481  -12.524 2.108   1.00 34.23 ? 38   MET D SD  1 
ATOM   13439 C  CE  . MET D  1 21  ? -5.014  -13.176 0.498   1.00 34.97 ? 38   MET D CE  1 
ATOM   13440 N  N   . ALA D  1 22  ? -1.998  -16.903 4.848   1.00 21.48 ? 39   ALA D N   1 
ATOM   13441 C  CA  . ALA D  1 22  ? -2.102  -18.196 5.502   1.00 21.68 ? 39   ALA D CA  1 
ATOM   13442 C  C   . ALA D  1 22  ? -1.576  -18.154 6.938   1.00 21.25 ? 39   ALA D C   1 
ATOM   13443 O  O   . ALA D  1 22  ? -1.669  -19.159 7.642   1.00 21.65 ? 39   ALA D O   1 
ATOM   13444 C  CB  . ALA D  1 22  ? -1.404  -19.250 4.673   1.00 21.95 ? 39   ALA D CB  1 
ATOM   13445 N  N   . PHE D  1 23  ? -1.044  -17.007 7.389   1.00 20.29 ? 40   PHE D N   1 
ATOM   13446 C  CA  . PHE D  1 23  ? -0.823  -16.800 8.815   1.00 20.63 ? 40   PHE D CA  1 
ATOM   13447 C  C   . PHE D  1 23  ? -2.171  -16.938 9.521   1.00 21.82 ? 40   PHE D C   1 
ATOM   13448 O  O   . PHE D  1 23  ? -3.149  -16.320 9.099   1.00 21.36 ? 40   PHE D O   1 
ATOM   13449 C  CB  . PHE D  1 23  ? -0.209  -15.447 9.207   1.00 20.68 ? 40   PHE D CB  1 
ATOM   13450 C  CG  . PHE D  1 23  ? 1.295   -15.292 8.997   1.00 20.64 ? 40   PHE D CG  1 
ATOM   13451 C  CD1 . PHE D  1 23  ? 2.202   -15.972 9.806   1.00 21.41 ? 40   PHE D CD1 1 
ATOM   13452 C  CD2 . PHE D  1 23  ? 1.803   -14.432 8.028   1.00 20.64 ? 40   PHE D CD2 1 
ATOM   13453 C  CE1 . PHE D  1 23  ? 3.571   -15.822 9.623   1.00 21.75 ? 40   PHE D CE1 1 
ATOM   13454 C  CE2 . PHE D  1 23  ? 3.174   -14.281 7.856   1.00 20.93 ? 40   PHE D CE2 1 
ATOM   13455 C  CZ  . PHE D  1 23  ? 4.054   -14.980 8.649   1.00 20.78 ? 40   PHE D CZ  1 
ATOM   13456 N  N   . THR D  1 24  ? -2.216  -17.739 10.598  1.00 22.28 ? 41   THR D N   1 
ATOM   13457 C  CA  . THR D  1 24  ? -3.464  -17.983 11.313  1.00 22.49 ? 41   THR D CA  1 
ATOM   13458 C  C   . THR D  1 24  ? -3.782  -16.764 12.173  1.00 23.42 ? 41   THR D C   1 
ATOM   13459 O  O   . THR D  1 24  ? -2.933  -15.898 12.363  1.00 21.30 ? 41   THR D O   1 
ATOM   13460 C  CB  . THR D  1 24  ? -3.395  -19.246 12.174  1.00 22.84 ? 41   THR D CB  1 
ATOM   13461 O  OG1 . THR D  1 24  ? -2.554  -18.966 13.288  1.00 22.55 ? 41   THR D OG1 1 
ATOM   13462 C  CG2 . THR D  1 24  ? -2.914  -20.468 11.413  1.00 23.78 ? 41   THR D CG2 1 
ATOM   13463 N  N   . LEU D  1 25  ? -5.013  -16.719 12.702  1.00 23.61 ? 42   LEU D N   1 
ATOM   13464 C  CA  . LEU D  1 25  ? -5.450  -15.615 13.540  1.00 23.96 ? 42   LEU D CA  1 
ATOM   13465 C  C   . LEU D  1 25  ? -4.541  -15.492 14.758  1.00 24.23 ? 42   LEU D C   1 
ATOM   13466 O  O   . LEU D  1 25  ? -4.105  -14.392 15.104  1.00 23.61 ? 42   LEU D O   1 
ATOM   13467 C  CB  . LEU D  1 25  ? -6.908  -15.780 13.970  1.00 24.36 ? 42   LEU D CB  1 
ATOM   13468 C  CG  . LEU D  1 25  ? -7.467  -14.665 14.858  1.00 24.70 ? 42   LEU D CG  1 
ATOM   13469 C  CD1 . LEU D  1 25  ? -7.420  -13.323 14.132  1.00 25.03 ? 42   LEU D CD1 1 
ATOM   13470 C  CD2 . LEU D  1 25  ? -8.885  -14.976 15.311  1.00 24.91 ? 42   LEU D CD2 1 
ATOM   13471 N  N   . GLN D  1 26  ? -4.300  -16.626 15.423  1.00 24.28 ? 43   GLN D N   1 
ATOM   13472 C  CA  . GLN D  1 26  ? -3.461  -16.666 16.605  1.00 25.06 ? 43   GLN D CA  1 
ATOM   13473 C  C   . GLN D  1 26  ? -2.025  -16.266 16.265  1.00 22.99 ? 43   GLN D C   1 
ATOM   13474 O  O   . GLN D  1 26  ? -1.407  -15.533 17.031  1.00 22.54 ? 43   GLN D O   1 
ATOM   13475 C  CB  . GLN D  1 26  ? -3.494  -18.046 17.264  1.00 28.72 ? 43   GLN D CB  1 
ATOM   13476 C  CG  . GLN D  1 26  ? -4.615  -18.233 18.281  1.00 32.16 ? 43   GLN D CG  1 
ATOM   13477 C  CD  . GLN D  1 26  ? -4.289  -19.295 19.313  1.00 35.49 ? 43   GLN D CD  1 
ATOM   13478 O  OE1 . GLN D  1 26  ? -3.936  -18.989 20.455  1.00 39.23 ? 43   GLN D OE1 1 
ATOM   13479 N  NE2 . GLN D  1 26  ? -4.356  -20.556 18.911  1.00 38.81 ? 43   GLN D NE2 1 
ATOM   13480 N  N   . GLU D  1 27  ? -1.493  -16.755 15.136  1.00 22.79 ? 44   GLU D N   1 
ATOM   13481 C  CA  . GLU D  1 27  ? -0.143  -16.396 14.713  1.00 22.95 ? 44   GLU D CA  1 
ATOM   13482 C  C   . GLU D  1 27  ? -0.047  -14.877 14.558  1.00 22.69 ? 44   GLU D C   1 
ATOM   13483 O  O   . GLU D  1 27  ? 0.863   -14.248 15.097  1.00 23.10 ? 44   GLU D O   1 
ATOM   13484 C  CB  . GLU D  1 27  ? 0.266   -17.081 13.408  1.00 23.07 ? 44   GLU D CB  1 
ATOM   13485 C  CG  . GLU D  1 27  ? 0.665   -18.545 13.579  1.00 24.23 ? 44   GLU D CG  1 
ATOM   13486 C  CD  . GLU D  1 27  ? 0.844   -19.327 12.287  1.00 25.64 ? 44   GLU D CD  1 
ATOM   13487 O  OE1 . GLU D  1 27  ? 0.437   -18.839 11.206  1.00 24.94 ? 44   GLU D OE1 1 
ATOM   13488 O  OE2 . GLU D  1 27  ? 1.405   -20.443 12.356  1.00 26.49 ? 44   GLU D OE2 1 
ATOM   13489 N  N   . ARG D  1 28  ? -1.011  -14.294 13.840  1.00 22.02 ? 45   ARG D N   1 
ATOM   13490 C  CA  . ARG D  1 28  ? -1.010  -12.866 13.568  1.00 21.59 ? 45   ARG D CA  1 
ATOM   13491 C  C   . ARG D  1 28  ? -1.002  -12.057 14.863  1.00 21.29 ? 45   ARG D C   1 
ATOM   13492 O  O   . ARG D  1 28  ? -0.261  -11.087 14.987  1.00 21.73 ? 45   ARG D O   1 
ATOM   13493 C  CB  . ARG D  1 28  ? -2.230  -12.483 12.730  1.00 21.11 ? 45   ARG D CB  1 
ATOM   13494 C  CG  . ARG D  1 28  ? -2.209  -13.047 11.320  1.00 21.76 ? 45   ARG D CG  1 
ATOM   13495 C  CD  . ARG D  1 28  ? -3.508  -12.720 10.600  1.00 20.98 ? 45   ARG D CD  1 
ATOM   13496 N  NE  . ARG D  1 28  ? -3.595  -13.404 9.306   1.00 21.04 ? 45   ARG D NE  1 
ATOM   13497 C  CZ  . ARG D  1 28  ? -4.436  -13.093 8.327   1.00 21.40 ? 45   ARG D CZ  1 
ATOM   13498 N  NH1 . ARG D  1 28  ? -5.219  -12.032 8.424   1.00 20.69 ? 45   ARG D NH1 1 
ATOM   13499 N  NH2 . ARG D  1 28  ? -4.475  -13.838 7.238   1.00 22.88 ? 45   ARG D NH2 1 
ATOM   13500 N  N   . GLN D  1 29  ? -1.845  -12.444 15.820  1.00 21.21 ? 46   GLN D N   1 
ATOM   13501 C  CA  . GLN D  1 29  ? -1.984  -11.691 17.055  1.00 21.40 ? 46   GLN D CA  1 
ATOM   13502 C  C   . GLN D  1 29  ? -0.700  -11.762 17.881  1.00 22.53 ? 46   GLN D C   1 
ATOM   13503 O  O   . GLN D  1 29  ? -0.181  -10.730 18.308  1.00 21.84 ? 46   GLN D O   1 
ATOM   13504 C  CB  . GLN D  1 29  ? -3.212  -12.184 17.818  1.00 21.82 ? 46   GLN D CB  1 
ATOM   13505 C  CG  . GLN D  1 29  ? -4.524  -11.728 17.192  1.00 22.41 ? 46   GLN D CG  1 
ATOM   13506 C  CD  . GLN D  1 29  ? -5.749  -12.270 17.896  1.00 23.70 ? 46   GLN D CD  1 
ATOM   13507 O  OE1 . GLN D  1 29  ? -5.659  -13.162 18.748  1.00 23.02 ? 46   GLN D OE1 1 
ATOM   13508 N  NE2 . GLN D  1 29  ? -6.911  -11.750 17.526  1.00 24.34 ? 46   GLN D NE2 1 
ATOM   13509 N  N   . MET D  1 30  ? -0.187  -12.979 18.098  1.00 23.04 ? 47   MET D N   1 
ATOM   13510 C  CA  . MET D  1 30  ? 0.980   -13.170 18.945  1.00 24.25 ? 47   MET D CA  1 
ATOM   13511 C  C   . MET D  1 30  ? 2.251   -12.612 18.303  1.00 24.06 ? 47   MET D C   1 
ATOM   13512 O  O   . MET D  1 30  ? 3.143   -12.172 19.025  1.00 24.38 ? 47   MET D O   1 
ATOM   13513 C  CB  . MET D  1 30  ? 1.193   -14.651 19.268  1.00 25.63 ? 47   MET D CB  1 
ATOM   13514 C  CG  . MET D  1 30  ? 0.136   -15.220 20.182  1.00 27.37 ? 47   MET D CG  1 
ATOM   13515 S  SD  . MET D  1 30  ? 0.571   -16.872 20.753  1.00 31.35 ? 47   MET D SD  1 
ATOM   13516 C  CE  . MET D  1 30  ? -0.972  -17.356 21.537  1.00 30.95 ? 47   MET D CE  1 
ATOM   13517 N  N   . LEU D  1 31  ? 2.338   -12.629 16.966  1.00 23.52 ? 48   LEU D N   1 
ATOM   13518 C  CA  . LEU D  1 31  ? 3.549   -12.208 16.270  1.00 24.69 ? 48   LEU D CA  1 
ATOM   13519 C  C   . LEU D  1 31  ? 3.495   -10.732 15.870  1.00 24.31 ? 48   LEU D C   1 
ATOM   13520 O  O   . LEU D  1 31  ? 4.443   -10.225 15.270  1.00 24.19 ? 48   LEU D O   1 
ATOM   13521 C  CB  . LEU D  1 31  ? 3.782   -13.090 15.047  1.00 26.10 ? 48   LEU D CB  1 
ATOM   13522 C  CG  . LEU D  1 31  ? 4.018   -14.577 15.326  1.00 27.86 ? 48   LEU D CG  1 
ATOM   13523 C  CD1 . LEU D  1 31  ? 4.047   -15.336 14.011  1.00 28.87 ? 48   LEU D CD1 1 
ATOM   13524 C  CD2 . LEU D  1 31  ? 5.294   -14.805 16.117  1.00 28.58 ? 48   LEU D CD2 1 
ATOM   13525 N  N   . GLY D  1 32  ? 2.399   -10.043 16.199  1.00 23.87 ? 49   GLY D N   1 
ATOM   13526 C  CA  . GLY D  1 32  ? 2.284   -8.616  15.937  1.00 23.74 ? 49   GLY D CA  1 
ATOM   13527 C  C   . GLY D  1 32  ? 1.988   -8.302  14.472  1.00 22.92 ? 49   GLY D C   1 
ATOM   13528 O  O   . GLY D  1 32  ? 2.398   -7.250  13.978  1.00 23.84 ? 49   GLY D O   1 
ATOM   13529 N  N   . LEU D  1 33  ? 1.256   -9.203  13.797  1.00 21.43 ? 50   LEU D N   1 
ATOM   13530 C  CA  . LEU D  1 33  ? 0.882   -9.037  12.399  1.00 21.73 ? 50   LEU D CA  1 
ATOM   13531 C  C   . LEU D  1 33  ? -0.583  -8.627  12.254  1.00 20.74 ? 50   LEU D C   1 
ATOM   13532 O  O   . LEU D  1 33  ? -1.026  -8.353  11.139  1.00 20.92 ? 50   LEU D O   1 
ATOM   13533 C  CB  . LEU D  1 33  ? 1.109   -10.334 11.629  1.00 22.49 ? 50   LEU D CB  1 
ATOM   13534 C  CG  . LEU D  1 33  ? 2.468   -11.011 11.824  1.00 23.09 ? 50   LEU D CG  1 
ATOM   13535 C  CD1 . LEU D  1 33  ? 2.512   -12.255 10.958  1.00 23.27 ? 50   LEU D CD1 1 
ATOM   13536 C  CD2 . LEU D  1 33  ? 3.610   -10.063 11.498  1.00 23.70 ? 50   LEU D CD2 1 
ATOM   13537 N  N   . GLN D  1 34  ? -1.345  -8.634  13.352  1.00 20.84 ? 51   GLN D N   1 
ATOM   13538 C  CA  . GLN D  1 34  ? -2.771  -8.347  13.275  1.00 21.63 ? 51   GLN D CA  1 
ATOM   13539 C  C   . GLN D  1 34  ? -2.971  -6.948  12.694  1.00 21.83 ? 51   GLN D C   1 
ATOM   13540 O  O   . GLN D  1 34  ? -2.394  -5.979  13.186  1.00 23.25 ? 51   GLN D O   1 
ATOM   13541 C  CB  . GLN D  1 34  ? -3.407  -8.493  14.658  1.00 22.45 ? 51   GLN D CB  1 
ATOM   13542 C  CG  . GLN D  1 34  ? -4.932  -8.422  14.668  1.00 23.77 ? 51   GLN D CG  1 
ATOM   13543 C  CD  . GLN D  1 34  ? -5.606  -9.610  14.014  1.00 24.75 ? 51   GLN D CD  1 
ATOM   13544 O  OE1 . GLN D  1 34  ? -4.960  -10.527 13.489  1.00 24.39 ? 51   GLN D OE1 1 
ATOM   13545 N  NE2 . GLN D  1 34  ? -6.931  -9.602  14.037  1.00 24.80 ? 51   GLN D NE2 1 
ATOM   13546 N  N   . GLY D  1 35  ? -3.761  -6.865  11.618  1.00 22.10 ? 52   GLY D N   1 
ATOM   13547 C  CA  . GLY D  1 35  ? -4.051  -5.600  10.961  1.00 21.84 ? 52   GLY D CA  1 
ATOM   13548 C  C   . GLY D  1 35  ? -3.123  -5.313  9.778   1.00 21.51 ? 52   GLY D C   1 
ATOM   13549 O  O   . GLY D  1 35  ? -3.410  -4.415  8.986   1.00 21.97 ? 52   GLY D O   1 
ATOM   13550 N  N   . LEU D  1 36  ? -2.023  -6.071  9.649   1.00 20.34 ? 53   LEU D N   1 
ATOM   13551 C  CA  . LEU D  1 36  ? -1.079  -5.883  8.553   1.00 21.02 ? 53   LEU D CA  1 
ATOM   13552 C  C   . LEU D  1 36  ? -1.471  -6.770  7.372   1.00 21.25 ? 53   LEU D C   1 
ATOM   13553 O  O   . LEU D  1 36  ? -0.871  -6.698  6.298   1.00 21.56 ? 53   LEU D O   1 
ATOM   13554 C  CB  . LEU D  1 36  ? 0.346   -6.178  9.021   1.00 20.93 ? 53   LEU D CB  1 
ATOM   13555 C  CG  . LEU D  1 36  ? 0.841   -5.389  10.236  1.00 21.42 ? 53   LEU D CG  1 
ATOM   13556 C  CD1 . LEU D  1 36  ? 2.312   -5.716  10.506  1.00 21.65 ? 53   LEU D CD1 1 
ATOM   13557 C  CD2 . LEU D  1 36  ? 0.658   -3.897  10.051  1.00 21.81 ? 53   LEU D CD2 1 
ATOM   13558 N  N   . LEU D  1 37  ? -2.479  -7.619  7.590   1.00 20.85 ? 54   LEU D N   1 
ATOM   13559 C  CA  . LEU D  1 37  ? -3.037  -8.469  6.555   1.00 21.46 ? 54   LEU D CA  1 
ATOM   13560 C  C   . LEU D  1 37  ? -4.549  -8.282  6.569   1.00 21.78 ? 54   LEU D C   1 
ATOM   13561 O  O   . LEU D  1 37  ? -5.113  -7.918  7.598   1.00 21.74 ? 54   LEU D O   1 
ATOM   13562 C  CB  . LEU D  1 37  ? -2.657  -9.922  6.840   1.00 21.52 ? 54   LEU D CB  1 
ATOM   13563 C  CG  . LEU D  1 37  ? -1.174  -10.267 6.684   1.00 22.47 ? 54   LEU D CG  1 
ATOM   13564 C  CD1 . LEU D  1 37  ? -0.824  -11.517 7.463   1.00 23.22 ? 54   LEU D CD1 1 
ATOM   13565 C  CD2 . LEU D  1 37  ? -0.826  -10.440 5.221   1.00 22.79 ? 54   LEU D CD2 1 
ATOM   13566 N  N   . PRO D  1 38  ? -5.250  -8.534  5.444   1.00 22.96 ? 55   PRO D N   1 
ATOM   13567 C  CA  . PRO D  1 38  ? -6.707  -8.422  5.417   1.00 23.91 ? 55   PRO D CA  1 
ATOM   13568 C  C   . PRO D  1 38  ? -7.358  -9.468  6.318   1.00 25.11 ? 55   PRO D C   1 
ATOM   13569 O  O   . PRO D  1 38  ? -6.759  -10.503 6.602   1.00 25.31 ? 55   PRO D O   1 
ATOM   13570 C  CB  . PRO D  1 38  ? -7.071  -8.581  3.938   1.00 23.98 ? 55   PRO D CB  1 
ATOM   13571 C  CG  . PRO D  1 38  ? -5.899  -9.287  3.327   1.00 24.21 ? 55   PRO D CG  1 
ATOM   13572 C  CD  . PRO D  1 38  ? -4.678  -8.903  4.142   1.00 23.63 ? 55   PRO D CD  1 
ATOM   13573 N  N   . PRO D  1 39  ? -8.586  -9.205  6.823   1.00 25.96 ? 56   PRO D N   1 
ATOM   13574 C  CA  . PRO D  1 39  ? -9.221  -10.062 7.826   1.00 27.62 ? 56   PRO D CA  1 
ATOM   13575 C  C   . PRO D  1 39  ? -9.862  -11.322 7.249   1.00 30.48 ? 56   PRO D C   1 
ATOM   13576 O  O   . PRO D  1 39  ? -11.077 -11.508 7.317   1.00 34.30 ? 56   PRO D O   1 
ATOM   13577 C  CB  . PRO D  1 39  ? -10.249 -9.102  8.452   1.00 28.13 ? 56   PRO D CB  1 
ATOM   13578 C  CG  . PRO D  1 39  ? -10.657 -8.220  7.310   1.00 27.48 ? 56   PRO D CG  1 
ATOM   13579 C  CD  . PRO D  1 39  ? -9.397  -8.021  6.494   1.00 27.33 ? 56   PRO D CD  1 
ATOM   13580 N  N   . LYS D  1 40  ? -9.003  -12.167 6.677   1.00 29.68 ? 57   LYS D N   1 
ATOM   13581 C  CA  . LYS D  1 40  ? -9.359  -13.427 6.051   1.00 29.73 ? 57   LYS D CA  1 
ATOM   13582 C  C   . LYS D  1 40  ? -8.181  -14.371 6.279   1.00 28.28 ? 57   LYS D C   1 
ATOM   13583 O  O   . LYS D  1 40  ? -7.047  -14.003 5.974   1.00 25.65 ? 57   LYS D O   1 
ATOM   13584 C  CB  . LYS D  1 40  ? -9.598  -13.191 4.555   1.00 30.95 ? 57   LYS D CB  1 
ATOM   13585 C  CG  . LYS D  1 40  ? -9.631  -14.422 3.637   1.00 32.61 ? 57   LYS D CG  1 
ATOM   13586 C  CD  . LYS D  1 40  ? -10.941 -15.205 3.622   1.00 32.44 ? 57   LYS D CD  1 
ATOM   13587 C  CE  . LYS D  1 40  ? -10.925 -16.402 2.700   1.00 32.05 ? 57   LYS D CE  1 
ATOM   13588 N  NZ  . LYS D  1 40  ? -10.714 -16.067 1.286   1.00 31.49 ? 57   LYS D NZ  1 
ATOM   13589 N  N   . ILE D  1 41  ? -8.457  -15.553 6.844   1.00 26.76 ? 58   ILE D N   1 
ATOM   13590 C  CA  . ILE D  1 41  ? -7.443  -16.579 7.032   1.00 27.42 ? 58   ILE D CA  1 
ATOM   13591 C  C   . ILE D  1 41  ? -7.562  -17.578 5.883   1.00 27.70 ? 58   ILE D C   1 
ATOM   13592 O  O   . ILE D  1 41  ? -8.620  -18.170 5.690   1.00 26.34 ? 58   ILE D O   1 
ATOM   13593 C  CB  . ILE D  1 41  ? -7.602  -17.281 8.395   1.00 27.31 ? 58   ILE D CB  1 
ATOM   13594 C  CG1 . ILE D  1 41  ? -7.831  -16.289 9.547   1.00 28.01 ? 58   ILE D CG1 1 
ATOM   13595 C  CG2 . ILE D  1 41  ? -6.415  -18.207 8.668   1.00 27.70 ? 58   ILE D CG2 1 
ATOM   13596 C  CD1 . ILE D  1 41  ? -6.744  -15.241 9.703   1.00 28.03 ? 58   ILE D CD1 1 
ATOM   13597 N  N   . GLU D  1 42  ? -6.471  -17.766 5.132   1.00 26.91 ? 59   GLU D N   1 
ATOM   13598 C  CA  . GLU D  1 42  ? -6.471  -18.679 4.000   1.00 27.96 ? 59   GLU D CA  1 
ATOM   13599 C  C   . GLU D  1 42  ? -5.536  -19.852 4.283   1.00 28.13 ? 59   GLU D C   1 
ATOM   13600 O  O   . GLU D  1 42  ? -4.860  -19.888 5.307   1.00 28.12 ? 59   GLU D O   1 
ATOM   13601 C  CB  . GLU D  1 42  ? -6.080  -17.934 2.725   1.00 28.92 ? 59   GLU D CB  1 
ATOM   13602 C  CG  . GLU D  1 42  ? -7.128  -16.912 2.299   1.00 30.89 ? 59   GLU D CG  1 
ATOM   13603 C  CD  . GLU D  1 42  ? -6.954  -16.332 0.911   1.00 32.46 ? 59   GLU D CD  1 
ATOM   13604 O  OE1 . GLU D  1 42  ? -5.852  -16.464 0.339   1.00 33.99 ? 59   GLU D OE1 1 
ATOM   13605 O  OE2 . GLU D  1 42  ? -7.942  -15.761 0.391   1.00 33.34 ? 59   GLU D OE2 1 
ATOM   13606 N  N   . THR D  1 43  ? -5.559  -20.837 3.381   1.00 28.38 ? 60   THR D N   1 
ATOM   13607 C  CA  . THR D  1 43  ? -4.600  -21.929 3.387   1.00 27.85 ? 60   THR D CA  1 
ATOM   13608 C  C   . THR D  1 43  ? -3.703  -21.771 2.163   1.00 25.52 ? 60   THR D C   1 
ATOM   13609 O  O   . THR D  1 43  ? -4.008  -20.985 1.267   1.00 23.90 ? 60   THR D O   1 
ATOM   13610 C  CB  . THR D  1 43  ? -5.344  -23.265 3.376   1.00 29.68 ? 60   THR D CB  1 
ATOM   13611 O  OG1 . THR D  1 43  ? -6.142  -23.253 2.196   1.00 29.37 ? 60   THR D OG1 1 
ATOM   13612 C  CG2 . THR D  1 43  ? -6.230  -23.461 4.594   1.00 31.14 ? 60   THR D CG2 1 
ATOM   13613 N  N   . GLN D  1 44  ? -2.610  -22.541 2.120   1.00 25.39 ? 61   GLN D N   1 
ATOM   13614 C  CA  . GLN D  1 44  ? -1.748  -22.573 0.948   1.00 24.51 ? 61   GLN D CA  1 
ATOM   13615 C  C   . GLN D  1 44  ? -2.551  -23.016 -0.279  1.00 25.11 ? 61   GLN D C   1 
ATOM   13616 O  O   . GLN D  1 44  ? -2.320  -22.522 -1.382  1.00 22.87 ? 61   GLN D O   1 
ATOM   13617 C  CB  . GLN D  1 44  ? -0.540  -23.485 1.172   1.00 23.59 ? 61   GLN D CB  1 
ATOM   13618 C  CG  . GLN D  1 44  ? 0.651   -23.154 0.277   1.00 23.85 ? 61   GLN D CG  1 
ATOM   13619 C  CD  . GLN D  1 44  ? 1.778   -24.149 0.436   1.00 24.42 ? 61   GLN D CD  1 
ATOM   13620 O  OE1 . GLN D  1 44  ? 1.725   -25.273 -0.075  1.00 25.49 ? 61   GLN D OE1 1 
ATOM   13621 N  NE2 . GLN D  1 44  ? 2.809   -23.750 1.160   1.00 24.14 ? 61   GLN D NE2 1 
ATOM   13622 N  N   . ASP D  1 45  ? -3.502  -23.939 -0.079  1.00 26.71 ? 62   ASP D N   1 
ATOM   13623 C  CA  . ASP D  1 45  ? -4.341  -24.443 -1.158  1.00 28.41 ? 62   ASP D CA  1 
ATOM   13624 C  C   . ASP D  1 45  ? -5.077  -23.299 -1.856  1.00 28.62 ? 62   ASP D C   1 
ATOM   13625 O  O   . ASP D  1 45  ? -5.125  -23.260 -3.089  1.00 27.71 ? 62   ASP D O   1 
ATOM   13626 C  CB  . ASP D  1 45  ? -5.317  -25.496 -0.651  1.00 31.32 ? 62   ASP D CB  1 
ATOM   13627 C  CG  . ASP D  1 45  ? -4.741  -26.872 -0.336  1.00 33.85 ? 62   ASP D CG  1 
ATOM   13628 O  OD1 . ASP D  1 45  ? -3.555  -27.118 -0.659  1.00 35.92 ? 62   ASP D OD1 1 
ATOM   13629 O  OD2 . ASP D  1 45  ? -5.483  -27.696 0.239   1.00 35.42 ? 62   ASP D OD2 1 
ATOM   13630 N  N   . ILE D  1 46  ? -5.632  -22.365 -1.065  1.00 28.13 ? 63   ILE D N   1 
ATOM   13631 C  CA  . ILE D  1 46  ? -6.402  -21.244 -1.594  1.00 28.52 ? 63   ILE D CA  1 
ATOM   13632 C  C   . ILE D  1 46  ? -5.482  -20.256 -2.311  1.00 27.52 ? 63   ILE D C   1 
ATOM   13633 O  O   . ILE D  1 46  ? -5.841  -19.744 -3.374  1.00 27.57 ? 63   ILE D O   1 
ATOM   13634 C  CB  . ILE D  1 46  ? -7.208  -20.544 -0.480  1.00 30.69 ? 63   ILE D CB  1 
ATOM   13635 C  CG1 . ILE D  1 46  ? -8.266  -21.470 0.134   1.00 32.74 ? 63   ILE D CG1 1 
ATOM   13636 C  CG2 . ILE D  1 46  ? -7.832  -19.239 -0.980  1.00 30.74 ? 63   ILE D CG2 1 
ATOM   13637 C  CD1 . ILE D  1 46  ? -9.301  -21.980 -0.852  1.00 34.80 ? 63   ILE D CD1 1 
ATOM   13638 N  N   . GLN D  1 47  ? -4.325  -19.954 -1.704  1.00 25.44 ? 64   GLN D N   1 
ATOM   13639 C  CA  . GLN D  1 47  ? -3.356  -19.051 -2.312  1.00 25.52 ? 64   GLN D CA  1 
ATOM   13640 C  C   . GLN D  1 47  ? -2.929  -19.585 -3.680  1.00 25.89 ? 64   GLN D C   1 
ATOM   13641 O  O   . GLN D  1 47  ? -2.767  -18.815 -4.626  1.00 26.94 ? 64   GLN D O   1 
ATOM   13642 C  CB  . GLN D  1 47  ? -2.133  -18.855 -1.412  1.00 24.86 ? 64   GLN D CB  1 
ATOM   13643 C  CG  . GLN D  1 47  ? -2.415  -18.103 -0.115  1.00 23.71 ? 64   GLN D CG  1 
ATOM   13644 C  CD  . GLN D  1 47  ? -1.270  -18.177 0.874   1.00 24.43 ? 64   GLN D CD  1 
ATOM   13645 O  OE1 . GLN D  1 47  ? -0.827  -19.267 1.251   1.00 24.17 ? 64   GLN D OE1 1 
ATOM   13646 N  NE2 . GLN D  1 47  ? -0.767  -17.025 1.301   1.00 24.12 ? 64   GLN D NE2 1 
ATOM   13647 N  N   . ALA D  1 48  ? -2.727  -20.907 -3.761  1.00 26.45 ? 65   ALA D N   1 
ATOM   13648 C  CA  . ALA D  1 48  ? -2.263  -21.549 -4.980  1.00 28.04 ? 65   ALA D CA  1 
ATOM   13649 C  C   . ALA D  1 48  ? -3.336  -21.447 -6.063  1.00 27.86 ? 65   ALA D C   1 
ATOM   13650 O  O   . ALA D  1 48  ? -3.038  -21.080 -7.193  1.00 26.57 ? 65   ALA D O   1 
ATOM   13651 C  CB  . ALA D  1 48  ? -1.891  -22.987 -4.702  1.00 28.28 ? 65   ALA D CB  1 
ATOM   13652 N  N   . LEU D  1 49  ? -4.586  -21.755 -5.702  1.00 30.43 ? 66   LEU D N   1 
ATOM   13653 C  CA  . LEU D  1 49  ? -5.697  -21.648 -6.639  1.00 31.39 ? 66   LEU D CA  1 
ATOM   13654 C  C   . LEU D  1 49  ? -5.800  -20.226 -7.192  1.00 31.34 ? 66   LEU D C   1 
ATOM   13655 O  O   . LEU D  1 49  ? -6.050  -20.054 -8.384  1.00 32.18 ? 66   LEU D O   1 
ATOM   13656 C  CB  . LEU D  1 49  ? -7.003  -22.098 -5.987  1.00 33.66 ? 66   LEU D CB  1 
ATOM   13657 C  CG  . LEU D  1 49  ? -7.180  -23.611 -5.821  1.00 36.31 ? 66   LEU D CG  1 
ATOM   13658 C  CD1 . LEU D  1 49  ? -8.435  -23.910 -5.020  1.00 37.69 ? 66   LEU D CD1 1 
ATOM   13659 C  CD2 . LEU D  1 49  ? -7.227  -24.325 -7.165  1.00 37.85 ? 66   LEU D CD2 1 
ATOM   13660 N  N   . ARG D  1 50  ? -5.593  -19.211 -6.338  1.00 30.19 ? 67   ARG D N   1 
ATOM   13661 C  CA  . ARG D  1 50  ? -5.666  -17.821 -6.774  1.00 29.49 ? 67   ARG D CA  1 
ATOM   13662 C  C   . ARG D  1 50  ? -4.609  -17.562 -7.846  1.00 30.32 ? 67   ARG D C   1 
ATOM   13663 O  O   . ARG D  1 50  ? -4.894  -16.946 -8.874  1.00 30.36 ? 67   ARG D O   1 
ATOM   13664 C  CB  . ARG D  1 50  ? -5.474  -16.822 -5.625  1.00 28.11 ? 67   ARG D CB  1 
ATOM   13665 C  CG  . ARG D  1 50  ? -5.431  -15.365 -6.069  1.00 28.54 ? 67   ARG D CG  1 
ATOM   13666 C  CD  . ARG D  1 50  ? -5.147  -14.402 -4.924  1.00 29.17 ? 67   ARG D CD  1 
ATOM   13667 N  NE  . ARG D  1 50  ? -6.284  -14.303 -4.003  1.00 29.00 ? 67   ARG D NE  1 
ATOM   13668 C  CZ  . ARG D  1 50  ? -6.387  -14.829 -2.788  1.00 27.67 ? 67   ARG D CZ  1 
ATOM   13669 N  NH1 . ARG D  1 50  ? -5.385  -15.495 -2.241  1.00 27.11 ? 67   ARG D NH1 1 
ATOM   13670 N  NH2 . ARG D  1 50  ? -7.515  -14.682 -2.118  1.00 27.92 ? 67   ARG D NH2 1 
ATOM   13671 N  N   . PHE D  1 51  ? -3.383  -18.032 -7.587  1.00 30.04 ? 68   PHE D N   1 
ATOM   13672 C  CA  . PHE D  1 51  ? -2.278  -17.817 -8.500  1.00 32.02 ? 68   PHE D CA  1 
ATOM   13673 C  C   . PHE D  1 51  ? -2.562  -18.494 -9.842  1.00 33.30 ? 68   PHE D C   1 
ATOM   13674 O  O   . PHE D  1 51  ? -2.309  -17.909 -10.891 1.00 33.91 ? 68   PHE D O   1 
ATOM   13675 C  CB  . PHE D  1 51  ? -0.953  -18.332 -7.930  1.00 34.15 ? 68   PHE D CB  1 
ATOM   13676 C  CG  . PHE D  1 51  ? 0.075   -18.466 -9.040  1.00 35.63 ? 68   PHE D CG  1 
ATOM   13677 C  CD1 . PHE D  1 51  ? 0.159   -19.641 -9.779  1.00 37.91 ? 68   PHE D CD1 1 
ATOM   13678 C  CD2 . PHE D  1 51  ? 0.892   -17.399 -9.389  1.00 35.43 ? 68   PHE D CD2 1 
ATOM   13679 C  CE1 . PHE D  1 51  ? 1.058   -19.751 -10.826 1.00 38.28 ? 68   PHE D CE1 1 
ATOM   13680 C  CE2 . PHE D  1 51  ? 1.798   -17.521 -10.429 1.00 36.64 ? 68   PHE D CE2 1 
ATOM   13681 C  CZ  . PHE D  1 51  ? 1.876   -18.696 -11.141 1.00 37.42 ? 68   PHE D CZ  1 
ATOM   13682 N  N   . HIS D  1 52  ? -3.057  -19.736 -9.797  1.00 35.56 ? 69   HIS D N   1 
ATOM   13683 C  CA  . HIS D  1 52  ? -3.308  -20.509 -11.003 1.00 38.93 ? 69   HIS D CA  1 
ATOM   13684 C  C   . HIS D  1 52  ? -4.341  -19.782 -11.864 1.00 43.21 ? 69   HIS D C   1 
ATOM   13685 O  O   . HIS D  1 52  ? -4.174  -19.680 -13.077 1.00 44.90 ? 69   HIS D O   1 
ATOM   13686 C  CB  . HIS D  1 52  ? -3.695  -21.949 -10.645 1.00 37.29 ? 69   HIS D CB  1 
ATOM   13687 C  CG  . HIS D  1 52  ? -2.562  -22.741 -10.075 1.00 36.45 ? 69   HIS D CG  1 
ATOM   13688 N  ND1 . HIS D  1 52  ? -1.320  -22.805 -10.670 1.00 34.86 ? 69   HIS D ND1 1 
ATOM   13689 C  CD2 . HIS D  1 52  ? -2.484  -23.504 -8.977  1.00 35.54 ? 69   HIS D CD2 1 
ATOM   13690 C  CE1 . HIS D  1 52  ? -0.526  -23.577 -9.943  1.00 35.35 ? 69   HIS D CE1 1 
ATOM   13691 N  NE2 . HIS D  1 52  ? -1.211  -24.008 -8.907  1.00 35.17 ? 69   HIS D NE2 1 
ATOM   13692 N  N   . ARG D  1 53  ? -5.385  -19.250 -11.217 1.00 44.69 ? 70   ARG D N   1 
ATOM   13693 C  CA  . ARG D  1 53  ? -6.410  -18.475 -11.901 1.00 45.61 ? 70   ARG D CA  1 
ATOM   13694 C  C   . ARG D  1 53  ? -5.804  -17.230 -12.550 1.00 44.78 ? 70   ARG D C   1 
ATOM   13695 O  O   . ARG D  1 53  ? -6.108  -16.932 -13.703 1.00 47.02 ? 70   ARG D O   1 
ATOM   13696 C  CB  . ARG D  1 53  ? -7.518  -18.067 -10.926 1.00 47.60 ? 70   ARG D CB  1 
ATOM   13697 C  CG  . ARG D  1 53  ? -8.661  -17.297 -11.573 1.00 50.48 ? 70   ARG D CG  1 
ATOM   13698 C  CD  . ARG D  1 53  ? -9.421  -16.469 -10.558 1.00 51.86 ? 70   ARG D CD  1 
ATOM   13699 N  NE  . ARG D  1 53  ? -8.599  -15.386 -10.005 1.00 53.34 ? 70   ARG D NE  1 
ATOM   13700 C  CZ  . ARG D  1 53  ? -8.990  -14.538 -9.056  1.00 53.78 ? 70   ARG D CZ  1 
ATOM   13701 N  NH1 . ARG D  1 53  ? -10.201 -14.640 -8.530  1.00 53.33 ? 70   ARG D NH1 1 
ATOM   13702 N  NH2 . ARG D  1 53  ? -8.166  -13.590 -8.636  1.00 51.71 ? 70   ARG D NH2 1 
ATOM   13703 N  N   . ASN D  1 54  ? -4.962  -16.503 -11.804 1.00 42.56 ? 71   ASN D N   1 
ATOM   13704 C  CA  . ASN D  1 54  ? -4.366  -15.265 -12.287 1.00 43.27 ? 71   ASN D CA  1 
ATOM   13705 C  C   . ASN D  1 54  ? -3.392  -15.535 -13.434 1.00 47.68 ? 71   ASN D C   1 
ATOM   13706 O  O   . ASN D  1 54  ? -3.139  -14.648 -14.249 1.00 47.09 ? 71   ASN D O   1 
ATOM   13707 C  CB  . ASN D  1 54  ? -3.645  -14.508 -11.177 1.00 41.87 ? 71   ASN D CB  1 
ATOM   13708 C  CG  . ASN D  1 54  ? -4.596  -13.889 -10.181 1.00 41.54 ? 71   ASN D CG  1 
ATOM   13709 O  OD1 . ASN D  1 54  ? -5.796  -13.771 -10.452 1.00 42.92 ? 71   ASN D OD1 1 
ATOM   13710 N  ND2 . ASN D  1 54  ? -4.077  -13.461 -9.039  1.00 40.33 ? 71   ASN D ND2 1 
ATOM   13711 N  N   . LEU D  1 55  ? -2.827  -16.749 -13.473 1.00 51.23 ? 72   LEU D N   1 
ATOM   13712 C  CA  . LEU D  1 55  ? -1.882  -17.122 -14.513 1.00 53.29 ? 72   LEU D CA  1 
ATOM   13713 C  C   . LEU D  1 55  ? -2.642  -17.521 -15.778 1.00 54.92 ? 72   LEU D C   1 
ATOM   13714 O  O   . LEU D  1 55  ? -2.293  -17.072 -16.867 1.00 55.66 ? 72   LEU D O   1 
ATOM   13715 C  CB  . LEU D  1 55  ? -0.971  -18.247 -14.024 1.00 52.01 ? 72   LEU D CB  1 
ATOM   13716 C  CG  . LEU D  1 55  ? 0.271   -18.512 -14.880 1.00 50.53 ? 72   LEU D CG  1 
ATOM   13717 C  CD1 . LEU D  1 55  ? 1.314   -17.428 -14.690 1.00 49.96 ? 72   LEU D CD1 1 
ATOM   13718 C  CD2 . LEU D  1 55  ? 0.853   -19.876 -14.584 1.00 50.89 ? 72   LEU D CD2 1 
ATOM   13719 N  N   . LYS D  1 56  ? -3.680  -18.356 -15.622 1.00 56.95 ? 73   LYS D N   1 
ATOM   13720 C  CA  . LYS D  1 56  ? -4.524  -18.775 -16.734 1.00 58.82 ? 73   LYS D CA  1 
ATOM   13721 C  C   . LYS D  1 56  ? -5.163  -17.561 -17.407 1.00 62.90 ? 73   LYS D C   1 
ATOM   13722 O  O   . LYS D  1 56  ? -5.517  -17.634 -18.580 1.00 67.02 ? 73   LYS D O   1 
ATOM   13723 C  CB  . LYS D  1 56  ? -5.617  -19.751 -16.286 1.00 57.88 ? 73   LYS D CB  1 
ATOM   13724 N  N   . LYS D  1 57  ? -5.308  -16.455 -16.659 1.00 66.97 ? 74   LYS D N   1 
ATOM   13725 C  CA  . LYS D  1 57  ? -5.758  -15.182 -17.204 1.00 68.38 ? 74   LYS D CA  1 
ATOM   13726 C  C   . LYS D  1 57  ? -4.561  -14.329 -17.628 1.00 69.68 ? 74   LYS D C   1 
ATOM   13727 O  O   . LYS D  1 57  ? -4.584  -13.107 -17.479 1.00 70.95 ? 74   LYS D O   1 
ATOM   13728 C  CB  . LYS D  1 57  ? -6.616  -14.438 -16.171 1.00 67.87 ? 74   LYS D CB  1 
ATOM   13729 N  N   . MET D  1 58  ? -3.518  -14.982 -18.156 1.00 69.83 ? 75   MET D N   1 
ATOM   13730 C  CA  . MET D  1 58  ? -2.374  -14.302 -18.747 1.00 71.15 ? 75   MET D CA  1 
ATOM   13731 C  C   . MET D  1 58  ? -1.933  -15.104 -19.971 1.00 71.22 ? 75   MET D C   1 
ATOM   13732 O  O   . MET D  1 58  ? -2.180  -16.308 -20.042 1.00 69.88 ? 75   MET D O   1 
ATOM   13733 C  CB  . MET D  1 58  ? -1.231  -14.157 -17.734 1.00 70.35 ? 75   MET D CB  1 
ATOM   13734 N  N   . THR D  1 59  ? -1.287  -14.429 -20.932 1.00 69.32 ? 76   THR D N   1 
ATOM   13735 C  CA  . THR D  1 59  ? -1.125  -14.982 -22.270 1.00 66.90 ? 76   THR D CA  1 
ATOM   13736 C  C   . THR D  1 59  ? 0.354   -15.104 -22.646 1.00 60.97 ? 76   THR D C   1 
ATOM   13737 O  O   . THR D  1 59  ? 0.774   -16.154 -23.129 1.00 59.08 ? 76   THR D O   1 
ATOM   13738 C  CB  . THR D  1 59  ? -1.929  -14.142 -23.268 1.00 69.33 ? 76   THR D CB  1 
ATOM   13739 O  OG1 . THR D  1 59  ? -1.735  -14.762 -24.536 1.00 70.15 ? 76   THR D OG1 1 
ATOM   13740 C  CG2 . THR D  1 59  ? -1.517  -12.680 -23.313 1.00 69.84 ? 76   THR D CG2 1 
ATOM   13741 N  N   . SER D  1 60  ? 1.135   -14.040 -22.422 1.00 56.99 ? 77   SER D N   1 
ATOM   13742 C  CA  . SER D  1 60  ? 2.532   -13.998 -22.831 1.00 55.33 ? 77   SER D CA  1 
ATOM   13743 C  C   . SER D  1 60  ? 3.388   -14.867 -21.909 1.00 52.62 ? 77   SER D C   1 
ATOM   13744 O  O   . SER D  1 60  ? 3.359   -14.675 -20.696 1.00 48.87 ? 77   SER D O   1 
ATOM   13745 C  CB  . SER D  1 60  ? 3.037   -12.578 -22.839 1.00 55.46 ? 77   SER D CB  1 
ATOM   13746 O  OG  . SER D  1 60  ? 4.442   -12.537 -23.048 1.00 57.97 ? 77   SER D OG  1 
ATOM   13747 N  N   . PRO D  1 61  ? 4.170   -15.841 -22.439 1.00 49.51 ? 78   PRO D N   1 
ATOM   13748 C  CA  . PRO D  1 61  ? 5.148   -16.574 -21.628 1.00 47.67 ? 78   PRO D CA  1 
ATOM   13749 C  C   . PRO D  1 61  ? 6.080   -15.679 -20.812 1.00 45.59 ? 78   PRO D C   1 
ATOM   13750 O  O   . PRO D  1 61  ? 6.419   -16.021 -19.682 1.00 41.99 ? 78   PRO D O   1 
ATOM   13751 C  CB  . PRO D  1 61  ? 5.916   -17.406 -22.673 1.00 48.38 ? 78   PRO D CB  1 
ATOM   13752 C  CG  . PRO D  1 61  ? 4.909   -17.623 -23.782 1.00 47.54 ? 78   PRO D CG  1 
ATOM   13753 C  CD  . PRO D  1 61  ? 4.122   -16.326 -23.829 1.00 48.94 ? 78   PRO D CD  1 
ATOM   13754 N  N   . LEU D  1 62  ? 6.479   -14.535 -21.388 1.00 44.91 ? 79   LEU D N   1 
ATOM   13755 C  CA  . LEU D  1 62  ? 7.354   -13.589 -20.709 1.00 47.49 ? 79   LEU D CA  1 
ATOM   13756 C  C   . LEU D  1 62  ? 6.638   -12.985 -19.503 1.00 46.31 ? 79   LEU D C   1 
ATOM   13757 O  O   . LEU D  1 62  ? 7.232   -12.866 -18.435 1.00 45.35 ? 79   LEU D O   1 
ATOM   13758 C  CB  . LEU D  1 62  ? 7.855   -12.489 -21.645 1.00 49.24 ? 79   LEU D CB  1 
ATOM   13759 C  CG  . LEU D  1 62  ? 9.021   -12.847 -22.575 1.00 53.23 ? 79   LEU D CG  1 
ATOM   13760 C  CD1 . LEU D  1 62  ? 10.229  -13.302 -21.773 1.00 55.74 ? 79   LEU D CD1 1 
ATOM   13761 C  CD2 . LEU D  1 62  ? 8.644   -13.896 -23.609 1.00 55.30 ? 79   LEU D CD2 1 
ATOM   13762 N  N   . GLU D  1 63  ? 5.370   -12.599 -19.686 1.00 45.67 ? 80   GLU D N   1 
ATOM   13763 C  CA  . GLU D  1 63  ? 4.587   -11.989 -18.623 1.00 43.80 ? 80   GLU D CA  1 
ATOM   13764 C  C   . GLU D  1 63  ? 4.282   -13.015 -17.532 1.00 41.03 ? 80   GLU D C   1 
ATOM   13765 O  O   . GLU D  1 63  ? 4.147   -12.654 -16.367 1.00 42.29 ? 80   GLU D O   1 
ATOM   13766 C  CB  . GLU D  1 63  ? 3.296   -11.384 -19.179 1.00 44.77 ? 80   GLU D CB  1 
ATOM   13767 N  N   . LYS D  1 64  ? 4.145   -14.290 -17.918 1.00 39.68 ? 81   LYS D N   1 
ATOM   13768 C  CA  . LYS D  1 64  ? 4.006   -15.367 -16.952 1.00 39.17 ? 81   LYS D CA  1 
ATOM   13769 C  C   . LYS D  1 64  ? 5.293   -15.488 -16.133 1.00 36.61 ? 81   LYS D C   1 
ATOM   13770 O  O   . LYS D  1 64  ? 5.242   -15.571 -14.908 1.00 34.65 ? 81   LYS D O   1 
ATOM   13771 C  CB  . LYS D  1 64  ? 3.637   -16.675 -17.661 1.00 40.70 ? 81   LYS D CB  1 
ATOM   13772 C  CG  . LYS D  1 64  ? 2.212   -16.729 -18.197 1.00 42.75 ? 81   LYS D CG  1 
ATOM   13773 C  CD  . LYS D  1 64  ? 1.839   -18.053 -18.849 1.00 44.90 ? 81   LYS D CD  1 
ATOM   13774 C  CE  . LYS D  1 64  ? 0.442   -18.041 -19.392 1.00 47.04 ? 81   LYS D CE  1 
ATOM   13775 N  NZ  . LYS D  1 64  ? 0.072   -19.344 -19.950 1.00 48.49 ? 81   LYS D NZ  1 
ATOM   13776 N  N   . TYR D  1 65  ? 6.445   -15.483 -16.817 1.00 34.34 ? 82   TYR D N   1 
ATOM   13777 C  CA  . TYR D  1 65  ? 7.741   -15.587 -16.160 1.00 33.41 ? 82   TYR D CA  1 
ATOM   13778 C  C   . TYR D  1 65  ? 7.884   -14.497 -15.099 1.00 33.53 ? 82   TYR D C   1 
ATOM   13779 O  O   . TYR D  1 65  ? 8.209   -14.787 -13.948 1.00 33.56 ? 82   TYR D O   1 
ATOM   13780 C  CB  . TYR D  1 65  ? 8.869   -15.494 -17.193 1.00 33.18 ? 82   TYR D CB  1 
ATOM   13781 C  CG  . TYR D  1 65  ? 10.260  -15.383 -16.589 1.00 31.25 ? 82   TYR D CG  1 
ATOM   13782 C  CD1 . TYR D  1 65  ? 10.992  -16.519 -16.263 1.00 31.47 ? 82   TYR D CD1 1 
ATOM   13783 C  CD2 . TYR D  1 65  ? 10.835  -14.146 -16.335 1.00 31.12 ? 82   TYR D CD2 1 
ATOM   13784 C  CE1 . TYR D  1 65  ? 12.255  -16.427 -15.704 1.00 31.39 ? 82   TYR D CE1 1 
ATOM   13785 C  CE2 . TYR D  1 65  ? 12.099  -14.040 -15.779 1.00 32.42 ? 82   TYR D CE2 1 
ATOM   13786 C  CZ  . TYR D  1 65  ? 12.812  -15.184 -15.467 1.00 31.23 ? 82   TYR D CZ  1 
ATOM   13787 O  OH  . TYR D  1 65  ? 14.056  -15.086 -14.922 1.00 31.30 ? 82   TYR D OH  1 
ATOM   13788 N  N   . ILE D  1 66  ? 7.640   -13.246 -15.502 1.00 33.39 ? 83   ILE D N   1 
ATOM   13789 C  CA  . ILE D  1 66  ? 7.771   -12.095 -14.620 1.00 35.79 ? 83   ILE D CA  1 
ATOM   13790 C  C   . ILE D  1 66  ? 6.907   -12.292 -13.374 1.00 34.67 ? 83   ILE D C   1 
ATOM   13791 O  O   . ILE D  1 66  ? 7.365   -12.043 -12.258 1.00 32.54 ? 83   ILE D O   1 
ATOM   13792 C  CB  . ILE D  1 66  ? 7.403   -10.792 -15.356 1.00 39.02 ? 83   ILE D CB  1 
ATOM   13793 C  CG1 . ILE D  1 66  ? 8.343   -10.507 -16.537 1.00 42.50 ? 83   ILE D CG1 1 
ATOM   13794 C  CG2 . ILE D  1 66  ? 7.353   -9.610  -14.387 1.00 38.82 ? 83   ILE D CG2 1 
ATOM   13795 C  CD1 . ILE D  1 66  ? 9.776   -10.188 -16.142 1.00 44.42 ? 83   ILE D CD1 1 
ATOM   13796 N  N   . TYR D  1 67  ? 5.659   -12.732 -13.573 1.00 34.21 ? 84   TYR D N   1 
ATOM   13797 C  CA  . TYR D  1 67  ? 4.707   -12.844 -12.478 1.00 36.58 ? 84   TYR D CA  1 
ATOM   13798 C  C   . TYR D  1 67  ? 5.110   -13.983 -11.538 1.00 33.75 ? 84   TYR D C   1 
ATOM   13799 O  O   . TYR D  1 67  ? 5.105   -13.814 -10.322 1.00 32.40 ? 84   TYR D O   1 
ATOM   13800 C  CB  . TYR D  1 67  ? 3.287   -13.011 -13.027 1.00 39.28 ? 84   TYR D CB  1 
ATOM   13801 C  CG  . TYR D  1 67  ? 2.212   -12.947 -11.952 1.00 43.12 ? 84   TYR D CG  1 
ATOM   13802 C  CD1 . TYR D  1 67  ? 1.912   -11.749 -11.312 1.00 45.24 ? 84   TYR D CD1 1 
ATOM   13803 C  CD2 . TYR D  1 67  ? 1.491   -14.078 -11.583 1.00 45.31 ? 84   TYR D CD2 1 
ATOM   13804 C  CE1 . TYR D  1 67  ? 0.940   -11.680 -10.326 1.00 46.27 ? 84   TYR D CE1 1 
ATOM   13805 C  CE2 . TYR D  1 67  ? 0.520   -14.023 -10.595 1.00 45.76 ? 84   TYR D CE2 1 
ATOM   13806 C  CZ  . TYR D  1 67  ? 0.243   -12.821 -9.967  1.00 47.10 ? 84   TYR D CZ  1 
ATOM   13807 O  OH  . TYR D  1 67  ? -0.720  -12.762 -8.999  1.00 50.62 ? 84   TYR D OH  1 
ATOM   13808 N  N   . ILE D  1 68  ? 5.459   -15.141 -12.101 1.00 32.80 ? 85   ILE D N   1 
ATOM   13809 C  CA  . ILE D  1 68  ? 5.810   -16.307 -11.302 1.00 33.13 ? 85   ILE D CA  1 
ATOM   13810 C  C   . ILE D  1 68  ? 7.055   -16.003 -10.467 1.00 30.55 ? 85   ILE D C   1 
ATOM   13811 O  O   . ILE D  1 68  ? 7.079   -16.281 -9.271  1.00 29.78 ? 85   ILE D O   1 
ATOM   13812 C  CB  . ILE D  1 68  ? 6.009   -17.548 -12.192 1.00 35.64 ? 85   ILE D CB  1 
ATOM   13813 C  CG1 . ILE D  1 68  ? 4.708   -17.965 -12.864 1.00 39.22 ? 85   ILE D CG1 1 
ATOM   13814 C  CG2 . ILE D  1 68  ? 6.602   -18.711 -11.395 1.00 38.30 ? 85   ILE D CG2 1 
ATOM   13815 C  CD1 . ILE D  1 68  ? 4.883   -18.869 -14.073 1.00 40.45 ? 85   ILE D CD1 1 
ATOM   13816 N  N   . MET D  1 69  ? 8.092   -15.446 -11.102 1.00 30.47 ? 86   MET D N   1 
ATOM   13817 C  CA  . MET D  1 69  ? 9.364   -15.219 -10.429 1.00 30.37 ? 86   MET D CA  1 
ATOM   13818 C  C   . MET D  1 69  ? 9.218   -14.150 -9.344  1.00 29.44 ? 86   MET D C   1 
ATOM   13819 O  O   . MET D  1 69  ? 9.981   -14.143 -8.384  1.00 28.21 ? 86   MET D O   1 
ATOM   13820 C  CB  . MET D  1 69  ? 10.463  -14.819 -11.421 1.00 30.21 ? 86   MET D CB  1 
ATOM   13821 C  CG  . MET D  1 69  ? 10.853  -15.913 -12.407 1.00 30.63 ? 86   MET D CG  1 
ATOM   13822 S  SD  . MET D  1 69  ? 11.240  -17.516 -11.670 1.00 29.17 ? 86   MET D SD  1 
ATOM   13823 C  CE  . MET D  1 69  ? 12.617  -17.068 -10.603 1.00 29.46 ? 86   MET D CE  1 
ATOM   13824 N  N   . GLY D  1 70  ? 8.234   -13.254 -9.492  1.00 28.81 ? 87   GLY D N   1 
ATOM   13825 C  CA  . GLY D  1 70  ? 7.913   -12.286 -8.456  1.00 29.88 ? 87   GLY D CA  1 
ATOM   13826 C  C   . GLY D  1 70  ? 7.513   -12.956 -7.141  1.00 30.98 ? 87   GLY D C   1 
ATOM   13827 O  O   . GLY D  1 70  ? 7.771   -12.414 -6.068  1.00 31.68 ? 87   GLY D O   1 
ATOM   13828 N  N   . ILE D  1 71  ? 6.892   -14.140 -7.229  1.00 31.29 ? 88   ILE D N   1 
ATOM   13829 C  CA  . ILE D  1 71  ? 6.423   -14.858 -6.053  1.00 31.09 ? 88   ILE D CA  1 
ATOM   13830 C  C   . ILE D  1 71  ? 7.630   -15.329 -5.241  1.00 30.30 ? 88   ILE D C   1 
ATOM   13831 O  O   . ILE D  1 71  ? 7.582   -15.333 -4.010  1.00 29.06 ? 88   ILE D O   1 
ATOM   13832 C  CB  . ILE D  1 71  ? 5.501   -16.036 -6.428  1.00 32.45 ? 88   ILE D CB  1 
ATOM   13833 C  CG1 . ILE D  1 71  ? 4.486   -15.678 -7.514  1.00 33.69 ? 88   ILE D CG1 1 
ATOM   13834 C  CG2 . ILE D  1 71  ? 4.809   -16.604 -5.188  1.00 32.12 ? 88   ILE D CG2 1 
ATOM   13835 C  CD1 . ILE D  1 71  ? 3.728   -14.393 -7.253  1.00 35.08 ? 88   ILE D CD1 1 
ATOM   13836 N  N   . GLN D  1 72  ? 8.718   -15.697 -5.938  1.00 29.42 ? 89   GLN D N   1 
ATOM   13837 C  CA  . GLN D  1 72  ? 9.913   -16.224 -5.294  1.00 29.86 ? 89   GLN D CA  1 
ATOM   13838 C  C   . GLN D  1 72  ? 10.467  -15.215 -4.287  1.00 29.73 ? 89   GLN D C   1 
ATOM   13839 O  O   . GLN D  1 72  ? 10.982  -15.616 -3.246  1.00 29.27 ? 89   GLN D O   1 
ATOM   13840 C  CB  . GLN D  1 72  ? 10.982  -16.622 -6.317  1.00 30.57 ? 89   GLN D CB  1 
ATOM   13841 C  CG  . GLN D  1 72  ? 12.251  -17.198 -5.693  1.00 32.48 ? 89   GLN D CG  1 
ATOM   13842 C  CD  . GLN D  1 72  ? 13.359  -17.460 -6.691  1.00 34.51 ? 89   GLN D CD  1 
ATOM   13843 O  OE1 . GLN D  1 72  ? 13.690  -16.613 -7.529  1.00 36.10 ? 89   GLN D OE1 1 
ATOM   13844 N  NE2 . GLN D  1 72  ? 13.955  -18.642 -6.612  1.00 35.60 ? 89   GLN D NE2 1 
ATOM   13845 N  N   . GLU D  1 73  ? 10.343  -13.914 -4.594  1.00 29.38 ? 90   GLU D N   1 
ATOM   13846 C  CA  . GLU D  1 73  ? 10.843  -12.850 -3.732  1.00 31.57 ? 90   GLU D CA  1 
ATOM   13847 C  C   . GLU D  1 73  ? 9.846   -12.459 -2.638  1.00 30.25 ? 90   GLU D C   1 
ATOM   13848 O  O   . GLU D  1 73  ? 10.159  -11.581 -1.838  1.00 31.06 ? 90   GLU D O   1 
ATOM   13849 C  CB  . GLU D  1 73  ? 11.192  -11.593 -4.537  1.00 35.66 ? 90   GLU D CB  1 
ATOM   13850 C  CG  . GLU D  1 73  ? 12.552  -11.666 -5.226  1.00 39.30 ? 90   GLU D CG  1 
ATOM   13851 C  CD  . GLU D  1 73  ? 13.101  -10.342 -5.749  1.00 42.24 ? 90   GLU D CD  1 
ATOM   13852 O  OE1 . GLU D  1 73  ? 13.405  -10.320 -6.966  1.00 46.66 ? 90   GLU D OE1 1 
ATOM   13853 O  OE2 . GLU D  1 73  ? 13.241  -9.355  -4.971  1.00 37.12 ? 90   GLU D OE2 1 
ATOM   13854 N  N   . ARG D  1 74  ? 8.663   -13.093 -2.586  1.00 28.25 ? 91   ARG D N   1 
ATOM   13855 C  CA  . ARG D  1 74  ? 7.643   -12.731 -1.607  1.00 27.79 ? 91   ARG D CA  1 
ATOM   13856 C  C   . ARG D  1 74  ? 7.353   -13.867 -0.625  1.00 24.59 ? 91   ARG D C   1 
ATOM   13857 O  O   . ARG D  1 74  ? 7.254   -13.635 0.576   1.00 23.37 ? 91   ARG D O   1 
ATOM   13858 C  CB  . ARG D  1 74  ? 6.333   -12.329 -2.289  1.00 29.40 ? 91   ARG D CB  1 
ATOM   13859 C  CG  . ARG D  1 74  ? 6.463   -11.085 -3.153  1.00 32.24 ? 91   ARG D CG  1 
ATOM   13860 C  CD  . ARG D  1 74  ? 5.142   -10.731 -3.825  1.00 35.62 ? 91   ARG D CD  1 
ATOM   13861 N  NE  . ARG D  1 74  ? 5.273   -9.476  -4.574  1.00 38.62 ? 91   ARG D NE  1 
ATOM   13862 C  CZ  . ARG D  1 74  ? 4.717   -8.304  -4.281  1.00 42.58 ? 91   ARG D CZ  1 
ATOM   13863 N  NH1 . ARG D  1 74  ? 3.886   -8.178  -3.256  1.00 43.58 ? 91   ARG D NH1 1 
ATOM   13864 N  NH2 . ARG D  1 74  ? 5.000   -7.248  -5.030  1.00 44.30 ? 91   ARG D NH2 1 
ATOM   13865 N  N   . ASN D  1 75  ? 7.184   -15.079 -1.154  1.00 23.02 ? 92   ASN D N   1 
ATOM   13866 C  CA  . ASN D  1 75  ? 6.710   -16.221 -0.388  1.00 22.49 ? 92   ASN D CA  1 
ATOM   13867 C  C   . ASN D  1 75  ? 7.286   -17.479 -1.034  1.00 22.86 ? 92   ASN D C   1 
ATOM   13868 O  O   . ASN D  1 75  ? 6.764   -17.961 -2.039  1.00 22.13 ? 92   ASN D O   1 
ATOM   13869 C  CB  . ASN D  1 75  ? 5.185   -16.207 -0.317  1.00 21.10 ? 92   ASN D CB  1 
ATOM   13870 C  CG  . ASN D  1 75  ? 4.601   -17.315 0.523   1.00 21.00 ? 92   ASN D CG  1 
ATOM   13871 O  OD1 . ASN D  1 75  ? 5.245   -18.348 0.752   1.00 20.15 ? 92   ASN D OD1 1 
ATOM   13872 N  ND2 . ASN D  1 75  ? 3.371   -17.124 0.979   1.00 20.79 ? 92   ASN D ND2 1 
ATOM   13873 N  N   . GLU D  1 76  ? 8.386   -17.980 -0.460  1.00 23.99 ? 93   GLU D N   1 
ATOM   13874 C  CA  . GLU D  1 76  ? 9.173   -19.037 -1.075  1.00 25.01 ? 93   GLU D CA  1 
ATOM   13875 C  C   . GLU D  1 76  ? 8.364   -20.327 -1.186  1.00 23.70 ? 93   GLU D C   1 
ATOM   13876 O  O   . GLU D  1 76  ? 8.384   -20.989 -2.225  1.00 23.40 ? 93   GLU D O   1 
ATOM   13877 C  CB  . GLU D  1 76  ? 10.446  -19.258 -0.259  1.00 26.81 ? 93   GLU D CB  1 
ATOM   13878 C  CG  . GLU D  1 76  ? 11.417  -20.230 -0.915  1.00 28.58 ? 93   GLU D CG  1 
ATOM   13879 C  CD  . GLU D  1 76  ? 12.802  -20.125 -0.314  1.00 30.27 ? 93   GLU D CD  1 
ATOM   13880 O  OE1 . GLU D  1 76  ? 12.982  -20.611 0.821   1.00 31.85 ? 93   GLU D OE1 1 
ATOM   13881 O  OE2 . GLU D  1 76  ? 13.675  -19.512 -0.966  1.00 34.59 ? 93   GLU D OE2 1 
ATOM   13882 N  N   . LYS D  1 77  ? 7.668   -20.683 -0.105  1.00 22.57 ? 94   LYS D N   1 
ATOM   13883 C  CA  . LYS D  1 77  ? 6.912   -21.925 -0.058  1.00 22.61 ? 94   LYS D CA  1 
ATOM   13884 C  C   . LYS D  1 77  ? 5.787   -21.895 -1.086  1.00 22.42 ? 94   LYS D C   1 
ATOM   13885 O  O   . LYS D  1 77  ? 5.574   -22.889 -1.778  1.00 22.04 ? 94   LYS D O   1 
ATOM   13886 C  CB  . LYS D  1 77  ? 6.451   -22.223 1.372   1.00 23.18 ? 94   LYS D CB  1 
ATOM   13887 C  CG  . LYS D  1 77  ? 7.588   -22.778 2.215   1.00 23.58 ? 94   LYS D CG  1 
ATOM   13888 C  CD  . LYS D  1 77  ? 7.201   -23.310 3.584   1.00 25.07 ? 94   LYS D CD  1 
ATOM   13889 C  CE  . LYS D  1 77  ? 8.370   -24.005 4.212   1.00 26.86 ? 94   LYS D CE  1 
ATOM   13890 N  NZ  . LYS D  1 77  ? 8.100   -24.313 5.614   1.00 28.97 ? 94   LYS D NZ  1 
ATOM   13891 N  N   . LEU D  1 78  ? 5.102   -20.749 -1.216  1.00 21.71 ? 95   LEU D N   1 
ATOM   13892 C  CA  . LEU D  1 78  ? 4.033   -20.622 -2.192  1.00 22.31 ? 95   LEU D CA  1 
ATOM   13893 C  C   . LEU D  1 78  ? 4.592   -20.766 -3.609  1.00 21.63 ? 95   LEU D C   1 
ATOM   13894 O  O   . LEU D  1 78  ? 3.997   -21.450 -4.437  1.00 21.81 ? 95   LEU D O   1 
ATOM   13895 C  CB  . LEU D  1 78  ? 3.285   -19.304 -2.003  1.00 22.78 ? 95   LEU D CB  1 
ATOM   13896 C  CG  . LEU D  1 78  ? 2.079   -19.073 -2.919  1.00 23.81 ? 95   LEU D CG  1 
ATOM   13897 C  CD1 . LEU D  1 78  ? 1.023   -20.156 -2.737  1.00 23.93 ? 95   LEU D CD1 1 
ATOM   13898 C  CD2 . LEU D  1 78  ? 1.489   -17.686 -2.684  1.00 23.68 ? 95   LEU D CD2 1 
ATOM   13899 N  N   . PHE D  1 79  ? 5.742   -20.132 -3.875  1.00 22.84 ? 96   PHE D N   1 
ATOM   13900 C  CA  . PHE D  1 79  ? 6.382   -20.192 -5.180  1.00 22.65 ? 96   PHE D CA  1 
ATOM   13901 C  C   . PHE D  1 79  ? 6.606   -21.648 -5.591  1.00 22.36 ? 96   PHE D C   1 
ATOM   13902 O  O   . PHE D  1 79  ? 6.260   -22.024 -6.709  1.00 22.19 ? 96   PHE D O   1 
ATOM   13903 C  CB  . PHE D  1 79  ? 7.681   -19.376 -5.156  1.00 23.98 ? 96   PHE D CB  1 
ATOM   13904 C  CG  . PHE D  1 79  ? 8.570   -19.523 -6.385  1.00 24.57 ? 96   PHE D CG  1 
ATOM   13905 C  CD1 . PHE D  1 79  ? 8.256   -18.883 -7.580  1.00 25.63 ? 96   PHE D CD1 1 
ATOM   13906 C  CD2 . PHE D  1 79  ? 9.725   -20.299 -6.341  1.00 26.18 ? 96   PHE D CD2 1 
ATOM   13907 C  CE1 . PHE D  1 79  ? 9.071   -19.018 -8.696  1.00 26.35 ? 96   PHE D CE1 1 
ATOM   13908 C  CE2 . PHE D  1 79  ? 10.540  -20.431 -7.458  1.00 27.00 ? 96   PHE D CE2 1 
ATOM   13909 C  CZ  . PHE D  1 79  ? 10.215  -19.790 -8.633  1.00 26.97 ? 96   PHE D CZ  1 
ATOM   13910 N  N   . TYR D  1 80  ? 7.176   -22.461 -4.690  1.00 22.29 ? 97   TYR D N   1 
ATOM   13911 C  CA  . TYR D  1 80  ? 7.560   -23.827 -5.022  1.00 22.73 ? 97   TYR D CA  1 
ATOM   13912 C  C   . TYR D  1 80  ? 6.324   -24.722 -5.092  1.00 23.27 ? 97   TYR D C   1 
ATOM   13913 O  O   . TYR D  1 80  ? 6.261   -25.606 -5.945  1.00 25.89 ? 97   TYR D O   1 
ATOM   13914 C  CB  . TYR D  1 80  ? 8.654   -24.354 -4.080  1.00 22.42 ? 97   TYR D CB  1 
ATOM   13915 C  CG  . TYR D  1 80  ? 10.012  -23.765 -4.434  1.00 22.34 ? 97   TYR D CG  1 
ATOM   13916 C  CD1 . TYR D  1 80  ? 10.624  -24.083 -5.642  1.00 23.35 ? 97   TYR D CD1 1 
ATOM   13917 C  CD2 . TYR D  1 80  ? 10.662  -22.863 -3.601  1.00 21.72 ? 97   TYR D CD2 1 
ATOM   13918 C  CE1 . TYR D  1 80  ? 11.840  -23.530 -6.006  1.00 22.29 ? 97   TYR D CE1 1 
ATOM   13919 C  CE2 . TYR D  1 80  ? 11.883  -22.307 -3.953  1.00 22.74 ? 97   TYR D CE2 1 
ATOM   13920 C  CZ  . TYR D  1 80  ? 12.472  -22.641 -5.160  1.00 23.02 ? 97   TYR D CZ  1 
ATOM   13921 O  OH  . TYR D  1 80  ? 13.677  -22.110 -5.541  1.00 27.26 ? 97   TYR D OH  1 
ATOM   13922 N  N   . ARG D  1 81  ? 5.336   -24.474 -4.226  1.00 23.64 ? 98   ARG D N   1 
ATOM   13923 C  CA  . ARG D  1 81  ? 4.047   -25.148 -4.301  1.00 24.68 ? 98   ARG D CA  1 
ATOM   13924 C  C   . ARG D  1 81  ? 3.465   -25.006 -5.707  1.00 24.79 ? 98   ARG D C   1 
ATOM   13925 O  O   . ARG D  1 81  ? 3.019   -25.985 -6.304  1.00 23.82 ? 98   ARG D O   1 
ATOM   13926 C  CB  . ARG D  1 81  ? 3.085   -24.596 -3.242  1.00 25.25 ? 98   ARG D CB  1 
ATOM   13927 C  CG  . ARG D  1 81  ? 1.632   -25.040 -3.370  1.00 26.30 ? 98   ARG D CG  1 
ATOM   13928 C  CD  . ARG D  1 81  ? 1.463   -26.554 -3.341  1.00 27.08 ? 98   ARG D CD  1 
ATOM   13929 N  NE  . ARG D  1 81  ? 0.070   -26.973 -3.534  1.00 29.05 ? 98   ARG D NE  1 
ATOM   13930 C  CZ  . ARG D  1 81  ? -0.917  -26.934 -2.637  1.00 31.12 ? 98   ARG D CZ  1 
ATOM   13931 N  NH1 . ARG D  1 81  ? -0.703  -26.543 -1.392  1.00 32.48 ? 98   ARG D NH1 1 
ATOM   13932 N  NH2 . ARG D  1 81  ? -2.131  -27.320 -2.988  1.00 33.12 ? 98   ARG D NH2 1 
ATOM   13933 N  N   . ILE D  1 82  ? 3.484   -23.774 -6.224  1.00 26.43 ? 99   ILE D N   1 
ATOM   13934 C  CA  . ILE D  1 82  ? 2.890   -23.437 -7.509  1.00 29.50 ? 99   ILE D CA  1 
ATOM   13935 C  C   . ILE D  1 82  ? 3.640   -24.129 -8.650  1.00 29.83 ? 99   ILE D C   1 
ATOM   13936 O  O   . ILE D  1 82  ? 3.017   -24.599 -9.600  1.00 31.19 ? 99   ILE D O   1 
ATOM   13937 C  CB  . ILE D  1 82  ? 2.856   -21.905 -7.659  1.00 32.00 ? 99   ILE D CB  1 
ATOM   13938 C  CG1 . ILE D  1 82  ? 1.648   -21.317 -6.931  1.00 33.64 ? 99   ILE D CG1 1 
ATOM   13939 C  CG2 . ILE D  1 82  ? 2.904   -21.474 -9.124  1.00 34.91 ? 99   ILE D CG2 1 
ATOM   13940 C  CD1 . ILE D  1 82  ? 1.810   -19.851 -6.570  1.00 35.64 ? 99   ILE D CD1 1 
ATOM   13941 N  N   . LEU D  1 83  ? 4.975   -24.159 -8.563  1.00 29.31 ? 100  LEU D N   1 
ATOM   13942 C  CA  . LEU D  1 83  ? 5.808   -24.851 -9.535  1.00 29.66 ? 100  LEU D CA  1 
ATOM   13943 C  C   . LEU D  1 83  ? 5.465   -26.337 -9.567  1.00 28.74 ? 100  LEU D C   1 
ATOM   13944 O  O   . LEU D  1 83  ? 5.293   -26.911 -10.638 1.00 27.42 ? 100  LEU D O   1 
ATOM   13945 C  CB  . LEU D  1 83  ? 7.293   -24.663 -9.230  1.00 30.36 ? 100  LEU D CB  1 
ATOM   13946 C  CG  . LEU D  1 83  ? 8.069   -23.736 -10.165 1.00 33.41 ? 100  LEU D CG  1 
ATOM   13947 C  CD1 . LEU D  1 83  ? 9.503   -23.579 -9.662  1.00 32.42 ? 100  LEU D CD1 1 
ATOM   13948 C  CD2 . LEU D  1 83  ? 8.053   -24.269 -11.596 1.00 34.27 ? 100  LEU D CD2 1 
ATOM   13949 N  N   . GLN D  1 84  ? 5.401   -26.945 -8.381  1.00 28.79 ? 101  GLN D N   1 
ATOM   13950 C  CA  . GLN D  1 84  ? 5.174   -28.373 -8.243  1.00 30.71 ? 101  GLN D CA  1 
ATOM   13951 C  C   . GLN D  1 84  ? 3.785   -28.743 -8.762  1.00 31.66 ? 101  GLN D C   1 
ATOM   13952 O  O   . GLN D  1 84  ? 3.637   -29.758 -9.437  1.00 32.23 ? 101  GLN D O   1 
ATOM   13953 C  CB  . GLN D  1 84  ? 5.384   -28.754 -6.779  1.00 31.04 ? 101  GLN D CB  1 
ATOM   13954 C  CG  . GLN D  1 84  ? 6.834   -28.626 -6.319  1.00 30.78 ? 101  GLN D CG  1 
ATOM   13955 C  CD  . GLN D  1 84  ? 6.994   -28.625 -4.813  1.00 31.78 ? 101  GLN D CD  1 
ATOM   13956 O  OE1 . GLN D  1 84  ? 6.023   -28.555 -4.050  1.00 31.36 ? 101  GLN D OE1 1 
ATOM   13957 N  NE2 . GLN D  1 84  ? 8.240   -28.683 -4.368  1.00 32.58 ? 101  GLN D NE2 1 
ATOM   13958 N  N   . ASP D  1 85  ? 2.786   -27.897 -8.463  1.00 31.91 ? 102  ASP D N   1 
ATOM   13959 C  CA  . ASP D  1 85  ? 1.410   -28.112 -8.887  1.00 32.70 ? 102  ASP D CA  1 
ATOM   13960 C  C   . ASP D  1 85  ? 1.305   -28.268 -10.403 1.00 32.30 ? 102  ASP D C   1 
ATOM   13961 O  O   . ASP D  1 85  ? 0.484   -29.052 -10.869 1.00 32.90 ? 102  ASP D O   1 
ATOM   13962 C  CB  . ASP D  1 85  ? 0.500   -26.940 -8.548  1.00 32.99 ? 102  ASP D CB  1 
ATOM   13963 C  CG  . ASP D  1 85  ? -0.003  -26.826 -7.116  1.00 34.03 ? 102  ASP D CG  1 
ATOM   13964 O  OD1 . ASP D  1 85  ? 0.144   -27.805 -6.348  1.00 33.45 ? 102  ASP D OD1 1 
ATOM   13965 O  OD2 . ASP D  1 85  ? -0.550  -25.747 -6.788  1.00 33.13 ? 102  ASP D OD2 1 
ATOM   13966 N  N   . ASP D  1 86  ? 2.090   -27.482 -11.155 1.00 31.14 ? 103  ASP D N   1 
ATOM   13967 C  CA  . ASP D  1 86  ? 1.906   -27.347 -12.595 1.00 32.28 ? 103  ASP D CA  1 
ATOM   13968 C  C   . ASP D  1 86  ? 3.259   -27.478 -13.295 1.00 30.43 ? 103  ASP D C   1 
ATOM   13969 O  O   . ASP D  1 86  ? 3.587   -26.703 -14.189 1.00 30.00 ? 103  ASP D O   1 
ATOM   13970 C  CB  . ASP D  1 86  ? 1.176   -26.047 -12.903 1.00 33.32 ? 103  ASP D CB  1 
ATOM   13971 C  CG  . ASP D  1 86  ? 0.622   -25.902 -14.315 1.00 36.58 ? 103  ASP D CG  1 
ATOM   13972 O  OD1 . ASP D  1 86  ? 0.159   -26.924 -14.869 1.00 35.85 ? 103  ASP D OD1 1 
ATOM   13973 O  OD2 . ASP D  1 86  ? 0.627   -24.761 -14.836 1.00 37.71 ? 103  ASP D OD2 1 
ATOM   13974 N  N   . ILE D  1 87  ? 4.025   -28.501 -12.911 1.00 30.39 ? 104  ILE D N   1 
ATOM   13975 C  CA  . ILE D  1 87  ? 5.454   -28.533 -13.195 1.00 31.89 ? 104  ILE D CA  1 
ATOM   13976 C  C   . ILE D  1 87  ? 5.720   -28.705 -14.694 1.00 31.19 ? 104  ILE D C   1 
ATOM   13977 O  O   . ILE D  1 87  ? 6.621   -28.065 -15.226 1.00 31.11 ? 104  ILE D O   1 
ATOM   13978 C  CB  . ILE D  1 87  ? 6.162   -29.588 -12.318 1.00 32.64 ? 104  ILE D CB  1 
ATOM   13979 C  CG1 . ILE D  1 87  ? 7.681   -29.493 -12.443 1.00 33.11 ? 104  ILE D CG1 1 
ATOM   13980 C  CG2 . ILE D  1 87  ? 5.656   -31.006 -12.591 1.00 33.64 ? 104  ILE D CG2 1 
ATOM   13981 C  CD1 . ILE D  1 87  ? 8.277   -28.251 -11.804 1.00 34.68 ? 104  ILE D CD1 1 
ATOM   13982 N  N   . GLU D  1 88  ? 4.930   -29.532 -15.391 1.00 33.93 ? 105  GLU D N   1 
ATOM   13983 C  CA  . GLU D  1 88  ? 5.151   -29.775 -16.813 1.00 33.18 ? 105  GLU D CA  1 
ATOM   13984 C  C   . GLU D  1 88  ? 4.958   -28.490 -17.621 1.00 31.64 ? 105  GLU D C   1 
ATOM   13985 O  O   . GLU D  1 88  ? 5.734   -28.212 -18.530 1.00 30.44 ? 105  GLU D O   1 
ATOM   13986 C  CB  . GLU D  1 88  ? 4.254   -30.892 -17.353 1.00 35.19 ? 105  GLU D CB  1 
ATOM   13987 C  CG  . GLU D  1 88  ? 4.540   -31.225 -18.816 1.00 36.92 ? 105  GLU D CG  1 
ATOM   13988 C  CD  . GLU D  1 88  ? 3.854   -32.458 -19.380 1.00 38.57 ? 105  GLU D CD  1 
ATOM   13989 O  OE1 . GLU D  1 88  ? 3.118   -33.148 -18.646 1.00 38.60 ? 105  GLU D OE1 1 
ATOM   13990 O  OE2 . GLU D  1 88  ? 4.071   -32.724 -20.582 1.00 41.91 ? 105  GLU D OE2 1 
ATOM   13991 N  N   . SER D  1 89  ? 3.929   -27.700 -17.294 1.00 32.02 ? 106  SER D N   1 
ATOM   13992 C  CA  . SER D  1 89  ? 3.645   -26.481 -18.037 1.00 32.81 ? 106  SER D CA  1 
ATOM   13993 C  C   . SER D  1 89  ? 4.585   -25.342 -17.642 1.00 32.56 ? 106  SER D C   1 
ATOM   13994 O  O   . SER D  1 89  ? 4.878   -24.489 -18.474 1.00 31.50 ? 106  SER D O   1 
ATOM   13995 C  CB  . SER D  1 89  ? 2.202   -26.064 -17.874 1.00 34.09 ? 106  SER D CB  1 
ATOM   13996 O  OG  . SER D  1 89  ? 1.344   -27.006 -18.502 1.00 35.32 ? 106  SER D OG  1 
ATOM   13997 N  N   . LEU D  1 90  ? 5.060   -25.321 -16.387 1.00 32.90 ? 107  LEU D N   1 
ATOM   13998 C  CA  . LEU D  1 90  ? 5.790   -24.168 -15.879 1.00 31.68 ? 107  LEU D CA  1 
ATOM   13999 C  C   . LEU D  1 90  ? 7.301   -24.323 -16.055 1.00 32.22 ? 107  LEU D C   1 
ATOM   14000 O  O   . LEU D  1 90  ? 8.004   -23.318 -16.094 1.00 30.81 ? 107  LEU D O   1 
ATOM   14001 C  CB  . LEU D  1 90  ? 5.413   -23.881 -14.427 1.00 31.65 ? 107  LEU D CB  1 
ATOM   14002 C  CG  . LEU D  1 90  ? 3.973   -23.407 -14.195 1.00 32.31 ? 107  LEU D CG  1 
ATOM   14003 C  CD1 . LEU D  1 90  ? 3.736   -23.081 -12.735 1.00 32.20 ? 107  LEU D CD1 1 
ATOM   14004 C  CD2 . LEU D  1 90  ? 3.632   -22.210 -15.057 1.00 32.33 ? 107  LEU D CD2 1 
ATOM   14005 N  N   . MET D  1 91  ? 7.811   -25.552 -16.195 1.00 34.70 ? 108  MET D N   1 
ATOM   14006 C  CA  . MET D  1 91  ? 9.243   -25.736 -16.395 1.00 37.70 ? 108  MET D CA  1 
ATOM   14007 C  C   . MET D  1 91  ? 9.722   -24.939 -17.613 1.00 38.52 ? 108  MET D C   1 
ATOM   14008 O  O   . MET D  1 91  ? 10.746  -24.259 -17.529 1.00 40.45 ? 108  MET D O   1 
ATOM   14009 C  CB  . MET D  1 91  ? 9.623   -27.218 -16.509 1.00 40.48 ? 108  MET D CB  1 
ATOM   14010 C  CG  . MET D  1 91  ? 9.638   -27.944 -15.169 1.00 43.82 ? 108  MET D CG  1 
ATOM   14011 S  SD  . MET D  1 91  ? 10.399  -29.583 -15.188 1.00 49.93 ? 108  MET D SD  1 
ATOM   14012 C  CE  . MET D  1 91  ? 9.513   -30.342 -16.557 1.00 47.90 ? 108  MET D CE  1 
ATOM   14013 N  N   . PRO D  1 92  ? 9.014   -24.965 -18.771 1.00 37.61 ? 109  PRO D N   1 
ATOM   14014 C  CA  . PRO D  1 92  ? 9.390   -24.141 -19.927 1.00 37.15 ? 109  PRO D CA  1 
ATOM   14015 C  C   . PRO D  1 92  ? 9.278   -22.625 -19.759 1.00 35.42 ? 109  PRO D C   1 
ATOM   14016 O  O   . PRO D  1 92  ? 9.771   -21.880 -20.608 1.00 34.11 ? 109  PRO D O   1 
ATOM   14017 C  CB  . PRO D  1 92  ? 8.448   -24.631 -21.052 1.00 37.97 ? 109  PRO D CB  1 
ATOM   14018 C  CG  . PRO D  1 92  ? 7.933   -25.965 -20.570 1.00 38.12 ? 109  PRO D CG  1 
ATOM   14019 C  CD  . PRO D  1 92  ? 7.858   -25.827 -19.061 1.00 38.46 ? 109  PRO D CD  1 
ATOM   14020 N  N   . ILE D  1 93  ? 8.593   -22.179 -18.696 1.00 34.49 ? 110  ILE D N   1 
ATOM   14021 C  CA  . ILE D  1 93  ? 8.465   -20.763 -18.386 1.00 35.06 ? 110  ILE D CA  1 
ATOM   14022 C  C   . ILE D  1 93  ? 9.628   -20.321 -17.501 1.00 34.50 ? 110  ILE D C   1 
ATOM   14023 O  O   . ILE D  1 93  ? 10.258  -19.306 -17.788 1.00 33.20 ? 110  ILE D O   1 
ATOM   14024 C  CB  . ILE D  1 93  ? 7.111   -20.447 -17.718 1.00 36.69 ? 110  ILE D CB  1 
ATOM   14025 C  CG1 . ILE D  1 93  ? 5.919   -20.807 -18.616 1.00 38.22 ? 110  ILE D CG1 1 
ATOM   14026 C  CG2 . ILE D  1 93  ? 7.052   -18.986 -17.271 1.00 35.97 ? 110  ILE D CG2 1 
ATOM   14027 C  CD1 . ILE D  1 93  ? 5.811   -19.984 -19.888 1.00 38.90 ? 110  ILE D CD1 1 
ATOM   14028 N  N   . VAL D  1 94  ? 9.891   -21.068 -16.417 1.00 33.23 ? 111  VAL D N   1 
ATOM   14029 C  CA  . VAL D  1 94  ? 10.891  -20.657 -15.441 1.00 33.26 ? 111  VAL D CA  1 
ATOM   14030 C  C   . VAL D  1 94  ? 12.291  -20.997 -15.958 1.00 32.10 ? 111  VAL D C   1 
ATOM   14031 O  O   . VAL D  1 94  ? 13.259  -20.362 -15.544 1.00 31.26 ? 111  VAL D O   1 
ATOM   14032 C  CB  . VAL D  1 94  ? 10.672  -21.232 -14.027 1.00 34.97 ? 111  VAL D CB  1 
ATOM   14033 C  CG1 . VAL D  1 94  ? 9.309   -20.841 -13.458 1.00 35.12 ? 111  VAL D CG1 1 
ATOM   14034 C  CG2 . VAL D  1 94  ? 10.869  -22.743 -13.977 1.00 34.99 ? 111  VAL D CG2 1 
ATOM   14035 N  N   . TYR D  1 95  ? 12.397  -21.984 -16.860 1.00 32.30 ? 112  TYR D N   1 
ATOM   14036 C  CA  . TYR D  1 95  ? 13.677  -22.324 -17.464 1.00 34.47 ? 112  TYR D CA  1 
ATOM   14037 C  C   . TYR D  1 95  ? 13.567  -22.213 -18.989 1.00 36.64 ? 112  TYR D C   1 
ATOM   14038 O  O   . TYR D  1 95  ? 12.763  -21.436 -19.502 1.00 35.82 ? 112  TYR D O   1 
ATOM   14039 C  CB  . TYR D  1 95  ? 14.130  -23.694 -16.941 1.00 34.47 ? 112  TYR D CB  1 
ATOM   14040 C  CG  . TYR D  1 95  ? 15.598  -23.986 -17.217 1.00 35.46 ? 112  TYR D CG  1 
ATOM   14041 C  CD1 . TYR D  1 95  ? 16.585  -23.076 -16.862 1.00 35.20 ? 112  TYR D CD1 1 
ATOM   14042 C  CD2 . TYR D  1 95  ? 15.991  -25.144 -17.879 1.00 38.09 ? 112  TYR D CD2 1 
ATOM   14043 C  CE1 . TYR D  1 95  ? 17.920  -23.315 -17.135 1.00 37.81 ? 112  TYR D CE1 1 
ATOM   14044 C  CE2 . TYR D  1 95  ? 17.325  -25.395 -18.156 1.00 40.62 ? 112  TYR D CE2 1 
ATOM   14045 C  CZ  . TYR D  1 95  ? 18.289  -24.474 -17.790 1.00 41.02 ? 112  TYR D CZ  1 
ATOM   14046 O  OH  . TYR D  1 95  ? 19.605  -24.709 -18.055 1.00 48.46 ? 112  TYR D OH  1 
ATOM   14047 N  N   . THR D  1 96  ? 14.414  -22.963 -19.710 1.00 38.70 ? 113  THR D N   1 
ATOM   14048 C  CA  . THR D  1 96  ? 14.496  -22.880 -21.162 1.00 40.70 ? 113  THR D CA  1 
ATOM   14049 C  C   . THR D  1 96  ? 13.166  -23.332 -21.767 1.00 39.44 ? 113  THR D C   1 
ATOM   14050 O  O   . THR D  1 96  ? 12.582  -24.300 -21.284 1.00 38.07 ? 113  THR D O   1 
ATOM   14051 C  CB  . THR D  1 96  ? 15.671  -23.728 -21.660 1.00 43.07 ? 113  THR D CB  1 
ATOM   14052 O  OG1 . THR D  1 96  ? 15.796  -23.481 -23.057 1.00 45.37 ? 113  THR D OG1 1 
ATOM   14053 C  CG2 . THR D  1 96  ? 15.470  -25.219 -21.453 1.00 43.39 ? 113  THR D CG2 1 
ATOM   14054 N  N   . PRO D  1 97  ? 12.639  -22.678 -22.834 1.00 38.00 ? 114  PRO D N   1 
ATOM   14055 C  CA  . PRO D  1 97  ? 13.293  -21.541 -23.495 1.00 37.50 ? 114  PRO D CA  1 
ATOM   14056 C  C   . PRO D  1 97  ? 12.934  -20.097 -23.131 1.00 36.23 ? 114  PRO D C   1 
ATOM   14057 O  O   . PRO D  1 97  ? 13.464  -19.170 -23.744 1.00 37.05 ? 114  PRO D O   1 
ATOM   14058 C  CB  . PRO D  1 97  ? 12.857  -21.856 -24.942 1.00 37.94 ? 114  PRO D CB  1 
ATOM   14059 C  CG  . PRO D  1 97  ? 11.413  -22.279 -24.805 1.00 37.95 ? 114  PRO D CG  1 
ATOM   14060 C  CD  . PRO D  1 97  ? 11.391  -23.074 -23.511 1.00 39.22 ? 114  PRO D CD  1 
ATOM   14061 N  N   . THR D  1 98  ? 12.049  -19.900 -22.146 1.00 34.92 ? 115  THR D N   1 
ATOM   14062 C  CA  . THR D  1 98  ? 11.517  -18.575 -21.847 1.00 34.91 ? 115  THR D CA  1 
ATOM   14063 C  C   . THR D  1 98  ? 12.552  -17.708 -21.129 1.00 35.27 ? 115  THR D C   1 
ATOM   14064 O  O   . THR D  1 98  ? 12.642  -16.509 -21.388 1.00 35.50 ? 115  THR D O   1 
ATOM   14065 C  CB  . THR D  1 98  ? 10.246  -18.712 -21.011 1.00 34.79 ? 115  THR D CB  1 
ATOM   14066 O  OG1 . THR D  1 98  ? 9.352   -19.481 -21.807 1.00 35.05 ? 115  THR D OG1 1 
ATOM   14067 C  CG2 . THR D  1 98  ? 9.605   -17.377 -20.676 1.00 35.01 ? 115  THR D CG2 1 
ATOM   14068 N  N   . VAL D  1 99  ? 13.314  -18.314 -20.210 1.00 35.32 ? 116  VAL D N   1 
ATOM   14069 C  CA  . VAL D  1 99  ? 14.110  -17.569 -19.247 1.00 36.01 ? 116  VAL D CA  1 
ATOM   14070 C  C   . VAL D  1 99  ? 15.153  -16.709 -19.964 1.00 36.29 ? 116  VAL D C   1 
ATOM   14071 O  O   . VAL D  1 99  ? 15.397  -15.573 -19.565 1.00 36.30 ? 116  VAL D O   1 
ATOM   14072 C  CB  . VAL D  1 99  ? 14.760  -18.515 -18.215 1.00 36.67 ? 116  VAL D CB  1 
ATOM   14073 C  CG1 . VAL D  1 99  ? 15.735  -19.502 -18.849 1.00 37.78 ? 116  VAL D CG1 1 
ATOM   14074 C  CG2 . VAL D  1 99  ? 15.446  -17.746 -17.098 1.00 36.67 ? 116  VAL D CG2 1 
ATOM   14075 N  N   . GLY D  1 100 ? 15.754  -17.249 -21.028 1.00 36.79 ? 117  GLY D N   1 
ATOM   14076 C  CA  . GLY D  1 100 ? 16.767  -16.536 -21.790 1.00 37.45 ? 117  GLY D CA  1 
ATOM   14077 C  C   . GLY D  1 100 ? 16.239  -15.237 -22.398 1.00 38.80 ? 117  GLY D C   1 
ATOM   14078 O  O   . GLY D  1 100 ? 16.993  -14.278 -22.545 1.00 42.50 ? 117  GLY D O   1 
ATOM   14079 N  N   . LEU D  1 101 ? 14.942  -15.209 -22.736 1.00 39.74 ? 118  LEU D N   1 
ATOM   14080 C  CA  . LEU D  1 101 ? 14.326  -14.057 -23.379 1.00 40.44 ? 118  LEU D CA  1 
ATOM   14081 C  C   . LEU D  1 101 ? 14.066  -12.928 -22.380 1.00 40.57 ? 118  LEU D C   1 
ATOM   14082 O  O   . LEU D  1 101 ? 14.103  -11.758 -22.757 1.00 38.16 ? 118  LEU D O   1 
ATOM   14083 C  CB  . LEU D  1 101 ? 13.027  -14.494 -24.055 1.00 42.63 ? 118  LEU D CB  1 
ATOM   14084 C  CG  . LEU D  1 101 ? 13.159  -15.521 -25.186 1.00 43.82 ? 118  LEU D CG  1 
ATOM   14085 C  CD1 . LEU D  1 101 ? 11.783  -16.009 -25.598 1.00 44.45 ? 118  LEU D CD1 1 
ATOM   14086 C  CD2 . LEU D  1 101 ? 13.909  -14.958 -26.385 1.00 44.87 ? 118  LEU D CD2 1 
ATOM   14087 N  N   . ALA D  1 102 ? 13.801  -13.283 -21.115 1.00 42.06 ? 119  ALA D N   1 
ATOM   14088 C  CA  . ALA D  1 102 ? 13.290  -12.351 -20.116 1.00 42.31 ? 119  ALA D CA  1 
ATOM   14089 C  C   . ALA D  1 102 ? 14.250  -11.190 -19.853 1.00 41.72 ? 119  ALA D C   1 
ATOM   14090 O  O   . ALA D  1 102 ? 13.829  -10.036 -19.884 1.00 39.06 ? 119  ALA D O   1 
ATOM   14091 C  CB  . ALA D  1 102 ? 12.986  -13.097 -18.837 1.00 44.30 ? 119  ALA D CB  1 
HETATM 14092 N  N   . CSX D  1 103 ? 15.527  -11.496 -19.579 1.00 44.21 ? 120  CSX D N   1 
HETATM 14093 C  CA  . CSX D  1 103 ? 16.523  -10.478 -19.265 1.00 45.83 ? 120  CSX D CA  1 
HETATM 14094 C  CB  . CSX D  1 103 ? 17.899  -11.075 -18.964 1.00 48.87 ? 120  CSX D CB  1 
HETATM 14095 S  SG  . CSX D  1 103 ? 18.044  -11.684 -17.272 1.00 50.48 ? 120  CSX D SG  1 
HETATM 14096 C  C   . CSX D  1 103 ? 16.704  -9.501  -20.423 1.00 48.41 ? 120  CSX D C   1 
HETATM 14097 O  O   . CSX D  1 103 ? 16.627  -8.289  -20.228 1.00 50.05 ? 120  CSX D O   1 
HETATM 14098 O  OD  . CSX D  1 103 ? 17.623  -10.552 -16.366 1.00 47.58 ? 120  CSX D OD  1 
ATOM   14099 N  N   . SER D  1 104 ? 16.962  -10.043 -21.620 1.00 46.28 ? 121  SER D N   1 
ATOM   14100 C  CA  . SER D  1 104 ? 17.261  -9.234  -22.791 1.00 47.59 ? 121  SER D CA  1 
ATOM   14101 C  C   . SER D  1 104 ? 16.128  -8.254  -23.088 1.00 48.76 ? 121  SER D C   1 
ATOM   14102 O  O   . SER D  1 104 ? 16.383  -7.158  -23.582 1.00 51.36 ? 121  SER D O   1 
ATOM   14103 C  CB  . SER D  1 104 ? 17.581  -10.099 -23.997 1.00 48.42 ? 121  SER D CB  1 
ATOM   14104 O  OG  . SER D  1 104 ? 16.922  -11.357 -23.932 1.00 47.98 ? 121  SER D OG  1 
ATOM   14105 N  N   . GLN D  1 105 ? 14.889  -8.644  -22.764 1.00 48.07 ? 122  GLN D N   1 
ATOM   14106 C  CA  . GLN D  1 105 ? 13.722  -7.877  -23.166 1.00 49.11 ? 122  GLN D CA  1 
ATOM   14107 C  C   . GLN D  1 105 ? 13.250  -6.944  -22.048 1.00 45.86 ? 122  GLN D C   1 
ATOM   14108 O  O   . GLN D  1 105 ? 12.803  -5.835  -22.337 1.00 44.49 ? 122  GLN D O   1 
ATOM   14109 C  CB  . GLN D  1 105 ? 12.687  -8.863  -23.709 1.00 50.53 ? 122  GLN D CB  1 
ATOM   14110 C  CG  . GLN D  1 105 ? 13.174  -9.583  -24.964 1.00 53.57 ? 122  GLN D CG  1 
ATOM   14111 C  CD  . GLN D  1 105 ? 12.075  -10.286 -25.731 1.00 56.84 ? 122  GLN D CD  1 
ATOM   14112 O  OE1 . GLN D  1 105 ? 11.010  -9.716  -25.992 1.00 59.81 ? 122  GLN D OE1 1 
ATOM   14113 N  NE2 . GLN D  1 105 ? 12.325  -11.532 -26.108 1.00 58.44 ? 122  GLN D NE2 1 
ATOM   14114 N  N   . TYR D  1 106 ? 13.350  -7.382  -20.784 1.00 43.86 ? 123  TYR D N   1 
ATOM   14115 C  CA  . TYR D  1 106 ? 12.819  -6.620  -19.661 1.00 43.07 ? 123  TYR D CA  1 
ATOM   14116 C  C   . TYR D  1 106 ? 13.929  -6.126  -18.733 1.00 40.22 ? 123  TYR D C   1 
ATOM   14117 O  O   . TYR D  1 106 ? 13.778  -5.088  -18.100 1.00 38.24 ? 123  TYR D O   1 
ATOM   14118 C  CB  . TYR D  1 106 ? 11.813  -7.450  -18.857 1.00 46.39 ? 123  TYR D CB  1 
ATOM   14119 C  CG  . TYR D  1 106 ? 10.462  -7.631  -19.534 1.00 51.70 ? 123  TYR D CG  1 
ATOM   14120 C  CD1 . TYR D  1 106 ? 9.472   -6.658  -19.427 1.00 55.34 ? 123  TYR D CD1 1 
ATOM   14121 C  CD2 . TYR D  1 106 ? 10.172  -8.771  -20.274 1.00 54.55 ? 123  TYR D CD2 1 
ATOM   14122 C  CE1 . TYR D  1 106 ? 8.239   -6.811  -20.041 1.00 57.32 ? 123  TYR D CE1 1 
ATOM   14123 C  CE2 . TYR D  1 106 ? 8.941   -8.937  -20.890 1.00 57.94 ? 123  TYR D CE2 1 
ATOM   14124 C  CZ  . TYR D  1 106 ? 7.972   -7.954  -20.773 1.00 58.94 ? 123  TYR D CZ  1 
ATOM   14125 O  OH  . TYR D  1 106 ? 6.755   -8.106  -21.374 1.00 62.45 ? 123  TYR D OH  1 
ATOM   14126 N  N   . GLY D  1 107 ? 15.032  -6.872  -18.631 1.00 39.35 ? 124  GLY D N   1 
ATOM   14127 C  CA  . GLY D  1 107 ? 16.020  -6.619  -17.596 1.00 37.88 ? 124  GLY D CA  1 
ATOM   14128 C  C   . GLY D  1 107 ? 15.466  -7.053  -16.241 1.00 35.56 ? 124  GLY D C   1 
ATOM   14129 O  O   . GLY D  1 107 ? 14.689  -8.001  -16.180 1.00 34.98 ? 124  GLY D O   1 
ATOM   14130 N  N   . HIS D  1 108 ? 15.857  -6.346  -15.174 1.00 33.29 ? 125  HIS D N   1 
ATOM   14131 C  CA  . HIS D  1 108 ? 15.410  -6.666  -13.824 1.00 32.00 ? 125  HIS D CA  1 
ATOM   14132 C  C   . HIS D  1 108 ? 15.506  -5.413  -12.958 1.00 30.19 ? 125  HIS D C   1 
ATOM   14133 O  O   . HIS D  1 108 ? 16.390  -4.588  -13.180 1.00 29.64 ? 125  HIS D O   1 
ATOM   14134 C  CB  . HIS D  1 108 ? 16.240  -7.822  -13.249 1.00 31.00 ? 125  HIS D CB  1 
ATOM   14135 C  CG  . HIS D  1 108 ? 15.785  -8.323  -11.915 1.00 31.33 ? 125  HIS D CG  1 
ATOM   14136 N  ND1 . HIS D  1 108 ? 14.604  -9.013  -11.734 1.00 31.45 ? 125  HIS D ND1 1 
ATOM   14137 C  CD2 . HIS D  1 108 ? 16.340  -8.224  -10.701 1.00 31.00 ? 125  HIS D CD2 1 
ATOM   14138 C  CE1 . HIS D  1 108 ? 14.471  -9.328  -10.452 1.00 30.78 ? 125  HIS D CE1 1 
ATOM   14139 N  NE2 . HIS D  1 108 ? 15.516  -8.863  -9.807  1.00 30.77 ? 125  HIS D NE2 1 
ATOM   14140 N  N   . ILE D  1 109 ? 14.558  -5.266  -12.019 1.00 27.50 ? 126  ILE D N   1 
ATOM   14141 C  CA  . ILE D  1 109 ? 14.620  -4.252  -10.976 1.00 27.51 ? 126  ILE D CA  1 
ATOM   14142 C  C   . ILE D  1 109 ? 14.959  -4.956  -9.667  1.00 26.50 ? 126  ILE D C   1 
ATOM   14143 O  O   . ILE D  1 109 ? 14.162  -5.751  -9.178  1.00 26.32 ? 126  ILE D O   1 
ATOM   14144 C  CB  . ILE D  1 109 ? 13.297  -3.476  -10.836 1.00 28.53 ? 126  ILE D CB  1 
ATOM   14145 C  CG1 . ILE D  1 109 ? 12.917  -2.749  -12.113 1.00 30.49 ? 126  ILE D CG1 1 
ATOM   14146 C  CG2 . ILE D  1 109 ? 13.355  -2.511  -9.650  1.00 27.32 ? 126  ILE D CG2 1 
ATOM   14147 C  CD1 . ILE D  1 109 ? 11.532  -2.128  -12.069 1.00 32.23 ? 126  ILE D CD1 1 
ATOM   14148 N  N   . PHE D  1 110 ? 16.125  -4.628  -9.102  1.00 25.51 ? 127  PHE D N   1 
ATOM   14149 C  CA  . PHE D  1 110 ? 16.693  -5.396  -8.006  1.00 25.97 ? 127  PHE D CA  1 
ATOM   14150 C  C   . PHE D  1 110 ? 16.116  -4.944  -6.670  1.00 26.36 ? 127  PHE D C   1 
ATOM   14151 O  O   . PHE D  1 110 ? 15.895  -3.751  -6.451  1.00 25.16 ? 127  PHE D O   1 
ATOM   14152 C  CB  . PHE D  1 110 ? 18.219  -5.270  -7.995  1.00 25.94 ? 127  PHE D CB  1 
ATOM   14153 C  CG  . PHE D  1 110 ? 18.876  -6.180  -9.018  1.00 25.28 ? 127  PHE D CG  1 
ATOM   14154 C  CD1 . PHE D  1 110 ? 19.058  -5.758  -10.329 1.00 24.87 ? 127  PHE D CD1 1 
ATOM   14155 C  CD2 . PHE D  1 110 ? 19.271  -7.468  -8.670  1.00 25.49 ? 127  PHE D CD2 1 
ATOM   14156 C  CE1 . PHE D  1 110 ? 19.639  -6.598  -11.267 1.00 26.22 ? 127  PHE D CE1 1 
ATOM   14157 C  CE2 . PHE D  1 110 ? 19.850  -8.306  -9.612  1.00 26.06 ? 127  PHE D CE2 1 
ATOM   14158 C  CZ  . PHE D  1 110 ? 20.030  -7.871  -10.909 1.00 26.83 ? 127  PHE D CZ  1 
ATOM   14159 N  N   . ARG D  1 111 ? 15.861  -5.939  -5.807  1.00 25.95 ? 128  ARG D N   1 
ATOM   14160 C  CA  . ARG D  1 111 ? 15.774  -5.746  -4.368  1.00 26.32 ? 128  ARG D CA  1 
ATOM   14161 C  C   . ARG D  1 111 ? 16.644  -6.823  -3.723  1.00 25.86 ? 128  ARG D C   1 
ATOM   14162 O  O   . ARG D  1 111 ? 17.800  -6.563  -3.396  1.00 24.94 ? 128  ARG D O   1 
ATOM   14163 C  CB  . ARG D  1 111 ? 14.327  -5.735  -3.857  1.00 26.96 ? 128  ARG D CB  1 
ATOM   14164 C  CG  . ARG D  1 111 ? 14.210  -5.502  -2.354  1.00 28.55 ? 128  ARG D CG  1 
ATOM   14165 C  CD  . ARG D  1 111 ? 12.785  -5.664  -1.830  1.00 28.74 ? 128  ARG D CD  1 
ATOM   14166 N  NE  . ARG D  1 111 ? 12.401  -7.063  -1.612  1.00 29.31 ? 128  ARG D NE  1 
ATOM   14167 C  CZ  . ARG D  1 111 ? 12.701  -7.816  -0.552  1.00 28.95 ? 128  ARG D CZ  1 
ATOM   14168 N  NH1 . ARG D  1 111 ? 13.406  -7.330  0.456   1.00 27.50 ? 128  ARG D NH1 1 
ATOM   14169 N  NH2 . ARG D  1 111 ? 12.274  -9.068  -0.502  1.00 29.94 ? 128  ARG D NH2 1 
ATOM   14170 N  N   . ARG D  1 112 ? 16.102  -8.042  -3.600  1.00 26.48 ? 129  ARG D N   1 
ATOM   14171 C  CA  . ARG D  1 112 ? 16.870  -9.170  -3.098  1.00 29.14 ? 129  ARG D CA  1 
ATOM   14172 C  C   . ARG D  1 112 ? 17.895  -9.598  -4.143  1.00 28.29 ? 129  ARG D C   1 
ATOM   14173 O  O   . ARG D  1 112 ? 17.626  -9.524  -5.342  1.00 27.96 ? 129  ARG D O   1 
ATOM   14174 C  CB  . ARG D  1 112 ? 15.992  -10.393 -2.815  1.00 33.45 ? 129  ARG D CB  1 
ATOM   14175 C  CG  . ARG D  1 112 ? 15.233  -10.353 -1.498  1.00 38.39 ? 129  ARG D CG  1 
ATOM   14176 C  CD  . ARG D  1 112 ? 14.261  -11.522 -1.413  1.00 41.42 ? 129  ARG D CD  1 
ATOM   14177 N  NE  . ARG D  1 112 ? 14.937  -12.824 -1.451  1.00 43.30 ? 129  ARG D NE  1 
ATOM   14178 C  CZ  . ARG D  1 112 ? 15.576  -13.403 -0.438  1.00 46.25 ? 129  ARG D CZ  1 
ATOM   14179 N  NH1 . ARG D  1 112 ? 15.668  -12.810 0.745   1.00 46.67 ? 129  ARG D NH1 1 
ATOM   14180 N  NH2 . ARG D  1 112 ? 16.111  -14.597 -0.614  1.00 49.24 ? 129  ARG D NH2 1 
ATOM   14181 N  N   . PRO D  1 113 ? 19.084  -10.094 -3.731  1.00 29.72 ? 130  PRO D N   1 
ATOM   14182 C  CA  . PRO D  1 113 ? 20.037  -10.674 -4.679  1.00 30.40 ? 130  PRO D CA  1 
ATOM   14183 C  C   . PRO D  1 113 ? 19.434  -11.902 -5.360  1.00 32.49 ? 130  PRO D C   1 
ATOM   14184 O  O   . PRO D  1 113 ? 18.723  -12.673 -4.722  1.00 34.25 ? 130  PRO D O   1 
ATOM   14185 C  CB  . PRO D  1 113 ? 21.266  -11.038 -3.827  1.00 30.47 ? 130  PRO D CB  1 
ATOM   14186 C  CG  . PRO D  1 113 ? 21.069  -10.301 -2.519  1.00 30.38 ? 130  PRO D CG  1 
ATOM   14187 C  CD  . PRO D  1 113 ? 19.569  -10.136 -2.343  1.00 29.97 ? 130  PRO D CD  1 
ATOM   14188 N  N   . LYS D  1 114 ? 19.735  -12.064 -6.654  1.00 34.29 ? 131  LYS D N   1 
ATOM   14189 C  CA  . LYS D  1 114 ? 19.328  -13.228 -7.432  1.00 36.43 ? 131  LYS D CA  1 
ATOM   14190 C  C   . LYS D  1 114 ? 20.422  -14.297 -7.396  1.00 33.22 ? 131  LYS D C   1 
ATOM   14191 O  O   . LYS D  1 114 ? 20.178  -15.462 -7.693  1.00 34.97 ? 131  LYS D O   1 
ATOM   14192 C  CB  . LYS D  1 114 ? 19.049  -12.791 -8.876  1.00 38.48 ? 131  LYS D CB  1 
ATOM   14193 C  CG  . LYS D  1 114 ? 17.779  -11.968 -9.087  1.00 43.30 ? 131  LYS D CG  1 
ATOM   14194 C  CD  . LYS D  1 114 ? 16.524  -12.781 -9.394  1.00 46.49 ? 131  LYS D CD  1 
ATOM   14195 C  CE  . LYS D  1 114 ? 16.122  -13.737 -8.307  1.00 49.53 ? 131  LYS D CE  1 
ATOM   14196 N  NZ  . LYS D  1 114 ? 14.902  -14.475 -8.644  1.00 51.52 ? 131  LYS D NZ  1 
ATOM   14197 N  N   . GLY D  1 115 ? 21.631  -13.885 -7.018  1.00 30.24 ? 132  GLY D N   1 
ATOM   14198 C  CA  . GLY D  1 115 ? 22.794  -14.753 -7.012  1.00 27.26 ? 132  GLY D CA  1 
ATOM   14199 C  C   . GLY D  1 115 ? 24.050  -13.897 -7.075  1.00 25.51 ? 132  GLY D C   1 
ATOM   14200 O  O   . GLY D  1 115 ? 23.965  -12.676 -6.951  1.00 26.13 ? 132  GLY D O   1 
ATOM   14201 N  N   . LEU D  1 116 ? 25.200  -14.545 -7.268  1.00 23.41 ? 133  LEU D N   1 
ATOM   14202 C  CA  . LEU D  1 116 ? 26.469  -13.843 -7.287  1.00 23.54 ? 133  LEU D CA  1 
ATOM   14203 C  C   . LEU D  1 116 ? 26.845  -13.473 -8.718  1.00 22.97 ? 133  LEU D C   1 
ATOM   14204 O  O   . LEU D  1 116 ? 26.709  -14.284 -9.633  1.00 23.23 ? 133  LEU D O   1 
ATOM   14205 C  CB  . LEU D  1 116 ? 27.573  -14.678 -6.638  1.00 23.83 ? 133  LEU D CB  1 
ATOM   14206 C  CG  . LEU D  1 116 ? 27.534  -14.794 -5.112  1.00 24.47 ? 133  LEU D CG  1 
ATOM   14207 C  CD1 . LEU D  1 116 ? 28.685  -15.686 -4.666  1.00 24.45 ? 133  LEU D CD1 1 
ATOM   14208 C  CD2 . LEU D  1 116 ? 27.593  -13.457 -4.401  1.00 24.57 ? 133  LEU D CD2 1 
ATOM   14209 N  N   . PHE D  1 117 ? 27.353  -12.243 -8.865  1.00 22.09 ? 134  PHE D N   1 
ATOM   14210 C  CA  . PHE D  1 117 ? 27.988  -11.763 -10.078 1.00 21.92 ? 134  PHE D CA  1 
ATOM   14211 C  C   . PHE D  1 117 ? 29.478  -11.586 -9.807  1.00 21.36 ? 134  PHE D C   1 
ATOM   14212 O  O   . PHE D  1 117 ? 29.863  -10.826 -8.917  1.00 21.80 ? 134  PHE D O   1 
ATOM   14213 C  CB  . PHE D  1 117 ? 27.352  -10.447 -10.534 1.00 22.32 ? 134  PHE D CB  1 
ATOM   14214 C  CG  . PHE D  1 117 ? 25.918  -10.579 -11.027 1.00 23.37 ? 134  PHE D CG  1 
ATOM   14215 C  CD1 . PHE D  1 117 ? 25.649  -10.892 -12.356 1.00 23.83 ? 134  PHE D CD1 1 
ATOM   14216 C  CD2 . PHE D  1 117 ? 24.845  -10.388 -10.164 1.00 24.19 ? 134  PHE D CD2 1 
ATOM   14217 C  CE1 . PHE D  1 117 ? 24.346  -11.008 -12.806 1.00 24.72 ? 134  PHE D CE1 1 
ATOM   14218 C  CE2 . PHE D  1 117 ? 23.542  -10.505 -10.620 1.00 25.27 ? 134  PHE D CE2 1 
ATOM   14219 C  CZ  . PHE D  1 117 ? 23.294  -10.815 -11.937 1.00 25.28 ? 134  PHE D CZ  1 
ATOM   14220 N  N   . ILE D  1 118 ? 30.300  -12.322 -10.560 1.00 21.35 ? 135  ILE D N   1 
ATOM   14221 C  CA  . ILE D  1 118 ? 31.749  -12.267 -10.439 1.00 22.44 ? 135  ILE D CA  1 
ATOM   14222 C  C   . ILE D  1 118 ? 32.310  -11.828 -11.786 1.00 23.13 ? 135  ILE D C   1 
ATOM   14223 O  O   . ILE D  1 118 ? 32.177  -12.547 -12.776 1.00 24.62 ? 135  ILE D O   1 
ATOM   14224 C  CB  . ILE D  1 118 ? 32.324  -13.628 -10.002 1.00 23.21 ? 135  ILE D CB  1 
ATOM   14225 C  CG1 . ILE D  1 118 ? 31.701  -14.093 -8.686  1.00 23.70 ? 135  ILE D CG1 1 
ATOM   14226 C  CG2 . ILE D  1 118 ? 33.854  -13.583 -9.926  1.00 22.39 ? 135  ILE D CG2 1 
ATOM   14227 C  CD1 . ILE D  1 118 ? 32.104  -15.489 -8.262  1.00 24.47 ? 135  ILE D CD1 1 
ATOM   14228 N  N   . SER D  1 119 ? 32.938  -10.651 -11.819 1.00 23.44 ? 136  SER D N   1 
ATOM   14229 C  CA  . SER D  1 119 ? 33.428  -10.108 -13.074 1.00 23.20 ? 136  SER D CA  1 
ATOM   14230 C  C   . SER D  1 119 ? 34.949  -10.206 -13.122 1.00 23.60 ? 136  SER D C   1 
ATOM   14231 O  O   . SER D  1 119 ? 35.598  -10.365 -12.089 1.00 23.22 ? 136  SER D O   1 
ATOM   14232 C  CB  . SER D  1 119 ? 32.955  -8.701  -13.284 1.00 23.80 ? 136  SER D CB  1 
ATOM   14233 O  OG  . SER D  1 119 ? 33.787  -7.764  -12.616 1.00 24.49 ? 136  SER D OG  1 
ATOM   14234 N  N   . ILE D  1 120 ? 35.503  -10.084 -14.335 1.00 23.87 ? 137  ILE D N   1 
ATOM   14235 C  CA  . ILE D  1 120 ? 36.946  -10.077 -14.542 1.00 24.86 ? 137  ILE D CA  1 
ATOM   14236 C  C   . ILE D  1 120 ? 37.566  -8.868  -13.835 1.00 24.99 ? 137  ILE D C   1 
ATOM   14237 O  O   . ILE D  1 120 ? 38.728  -8.907  -13.436 1.00 24.63 ? 137  ILE D O   1 
ATOM   14238 C  CB  . ILE D  1 120 ? 37.270  -10.120 -16.052 1.00 25.75 ? 137  ILE D CB  1 
ATOM   14239 C  CG1 . ILE D  1 120 ? 38.747  -10.420 -16.327 1.00 26.64 ? 137  ILE D CG1 1 
ATOM   14240 C  CG2 . ILE D  1 120 ? 36.818  -8.844  -16.760 1.00 25.75 ? 137  ILE D CG2 1 
ATOM   14241 C  CD1 . ILE D  1 120 ? 39.162  -11.837 -15.983 1.00 27.11 ? 137  ILE D CD1 1 
ATOM   14242 N  N   . SER D  1 121 ? 36.776  -7.802  -13.641 1.00 24.71 ? 138  SER D N   1 
ATOM   14243 C  CA  . SER D  1 121 ? 37.250  -6.621  -12.932 1.00 25.35 ? 138  SER D CA  1 
ATOM   14244 C  C   . SER D  1 121 ? 37.431  -6.894  -11.435 1.00 25.68 ? 138  SER D C   1 
ATOM   14245 O  O   . SER D  1 121 ? 38.053  -6.093  -10.737 1.00 26.07 ? 138  SER D O   1 
ATOM   14246 C  CB  . SER D  1 121 ? 36.320  -5.461  -13.163 1.00 26.34 ? 138  SER D CB  1 
ATOM   14247 O  OG  . SER D  1 121 ? 36.320  -5.073  -14.529 1.00 25.36 ? 138  SER D OG  1 
ATOM   14248 N  N   . ASP D  1 122 ? 36.894  -8.025  -10.952 1.00 25.02 ? 139  ASP D N   1 
ATOM   14249 C  CA  . ASP D  1 122 ? 36.980  -8.409  -9.549  1.00 24.58 ? 139  ASP D CA  1 
ATOM   14250 C  C   . ASP D  1 122 ? 38.093  -9.430  -9.318  1.00 25.31 ? 139  ASP D C   1 
ATOM   14251 O  O   . ASP D  1 122 ? 38.204  -9.980  -8.222  1.00 24.46 ? 139  ASP D O   1 
ATOM   14252 C  CB  . ASP D  1 122 ? 35.652  -8.969  -9.062  1.00 24.43 ? 139  ASP D CB  1 
ATOM   14253 C  CG  . ASP D  1 122 ? 34.479  -8.004  -9.152  1.00 24.81 ? 139  ASP D CG  1 
ATOM   14254 O  OD1 . ASP D  1 122 ? 34.582  -6.911  -8.559  1.00 26.07 ? 139  ASP D OD1 1 
ATOM   14255 O  OD2 . ASP D  1 122 ? 33.479  -8.348  -9.816  1.00 24.64 ? 139  ASP D OD2 1 
ATOM   14256 N  N   . ARG D  1 123 ? 38.921  -9.687  -10.340 1.00 25.57 ? 140  ARG D N   1 
ATOM   14257 C  CA  A ARG D  1 123 ? 40.019  -10.631 -10.206 0.52 26.21 ? 140  ARG D CA  1 
ATOM   14258 C  CA  B ARG D  1 123 ? 40.013  -10.636 -10.202 0.48 26.28 ? 140  ARG D CA  1 
ATOM   14259 C  C   . ARG D  1 123 ? 40.873  -10.238 -9.002  1.00 25.93 ? 140  ARG D C   1 
ATOM   14260 O  O   . ARG D  1 123 ? 41.187  -9.063  -8.808  1.00 24.82 ? 140  ARG D O   1 
ATOM   14261 C  CB  A ARG D  1 123 ? 40.845  -10.710 -11.496 0.52 27.62 ? 140  ARG D CB  1 
ATOM   14262 C  CB  B ARG D  1 123 ? 40.807  -10.768 -11.507 0.48 27.75 ? 140  ARG D CB  1 
ATOM   14263 C  CG  A ARG D  1 123 ? 41.688  -9.485  -11.823 0.52 28.60 ? 140  ARG D CG  1 
ATOM   14264 C  CG  B ARG D  1 123 ? 41.517  -9.526  -12.030 0.48 28.89 ? 140  ARG D CG  1 
ATOM   14265 C  CD  A ARG D  1 123 ? 42.408  -9.618  -13.160 0.52 29.92 ? 140  ARG D CD  1 
ATOM   14266 C  CD  B ARG D  1 123 ? 42.120  -9.810  -13.404 0.48 30.12 ? 140  ARG D CD  1 
ATOM   14267 N  NE  A ARG D  1 123 ? 43.225  -10.836 -13.230 0.52 30.17 ? 140  ARG D NE  1 
ATOM   14268 N  NE  B ARG D  1 123 ? 42.873  -8.692  -13.985 0.48 30.91 ? 140  ARG D NE  1 
ATOM   14269 C  CZ  A ARG D  1 123 ? 44.548  -10.917 -13.087 0.52 30.83 ? 140  ARG D CZ  1 
ATOM   14270 C  CZ  B ARG D  1 123 ? 42.336  -7.603  -14.520 0.48 31.73 ? 140  ARG D CZ  1 
ATOM   14271 N  NH1 A ARG D  1 123 ? 45.268  -9.842  -12.813 0.52 30.56 ? 140  ARG D NH1 1 
ATOM   14272 N  NH1 B ARG D  1 123 ? 41.024  -7.452  -14.546 0.48 31.62 ? 140  ARG D NH1 1 
ATOM   14273 N  NH2 A ARG D  1 123 ? 45.150  -12.089 -13.203 0.52 31.11 ? 140  ARG D NH2 1 
ATOM   14274 N  NH2 B ARG D  1 123 ? 43.118  -6.670  -15.032 0.48 32.49 ? 140  ARG D NH2 1 
ATOM   14275 N  N   . GLY D  1 124 ? 41.230  -11.236 -8.187  1.00 25.33 ? 141  GLY D N   1 
ATOM   14276 C  CA  . GLY D  1 124 ? 41.987  -11.019 -6.966  1.00 25.94 ? 141  GLY D CA  1 
ATOM   14277 C  C   . GLY D  1 124 ? 41.093  -10.807 -5.743  1.00 25.79 ? 141  GLY D C   1 
ATOM   14278 O  O   . GLY D  1 124 ? 41.579  -10.862 -4.619  1.00 25.67 ? 141  GLY D O   1 
ATOM   14279 N  N   . HIS D  1 125 ? 39.786  -10.599 -5.953  1.00 25.69 ? 142  HIS D N   1 
ATOM   14280 C  CA  . HIS D  1 125 ? 38.884  -10.218 -4.876  1.00 25.03 ? 142  HIS D CA  1 
ATOM   14281 C  C   . HIS D  1 125 ? 37.637  -11.104 -4.869  1.00 24.39 ? 142  HIS D C   1 
ATOM   14282 O  O   . HIS D  1 125 ? 36.607  -10.725 -4.313  1.00 24.17 ? 142  HIS D O   1 
ATOM   14283 C  CB  . HIS D  1 125 ? 38.532  -8.730  -5.003  1.00 25.69 ? 142  HIS D CB  1 
ATOM   14284 C  CG  . HIS D  1 125 ? 39.724  -7.834  -4.912  1.00 26.80 ? 142  HIS D CG  1 
ATOM   14285 N  ND1 . HIS D  1 125 ? 40.264  -7.439  -3.706  1.00 27.04 ? 142  HIS D ND1 1 
ATOM   14286 C  CD2 . HIS D  1 125 ? 40.494  -7.282  -5.862  1.00 27.20 ? 142  HIS D CD2 1 
ATOM   14287 C  CE1 . HIS D  1 125 ? 41.324  -6.675  -3.931  1.00 26.66 ? 142  HIS D CE1 1 
ATOM   14288 N  NE2 . HIS D  1 125 ? 41.477  -6.560  -5.231  1.00 26.84 ? 142  HIS D NE2 1 
ATOM   14289 N  N   . VAL D  1 126 ? 37.738  -12.302 -5.454  1.00 24.02 ? 143  VAL D N   1 
ATOM   14290 C  CA  . VAL D  1 126 ? 36.573  -13.154 -5.645  1.00 24.34 ? 143  VAL D CA  1 
ATOM   14291 C  C   . VAL D  1 126 ? 36.072  -13.649 -4.291  1.00 23.99 ? 143  VAL D C   1 
ATOM   14292 O  O   . VAL D  1 126 ? 34.865  -13.746 -4.083  1.00 23.33 ? 143  VAL D O   1 
ATOM   14293 C  CB  . VAL D  1 126 ? 36.856  -14.322 -6.611  1.00 23.50 ? 143  VAL D CB  1 
ATOM   14294 C  CG1 . VAL D  1 126 ? 35.713  -15.329 -6.647  1.00 23.95 ? 143  VAL D CG1 1 
ATOM   14295 C  CG2 . VAL D  1 126 ? 37.158  -13.826 -8.019  1.00 23.79 ? 143  VAL D CG2 1 
ATOM   14296 N  N   . ARG D  1 127 ? 36.994  -13.955 -3.369  1.00 24.87 ? 144  ARG D N   1 
ATOM   14297 C  CA  . ARG D  1 127 ? 36.604  -14.471 -2.065  1.00 26.12 ? 144  ARG D CA  1 
ATOM   14298 C  C   . ARG D  1 127 ? 35.733  -13.459 -1.313  1.00 25.23 ? 144  ARG D C   1 
ATOM   14299 O  O   . ARG D  1 127 ? 34.805  -13.862 -0.613  1.00 22.39 ? 144  ARG D O   1 
ATOM   14300 C  CB  . ARG D  1 127 ? 37.814  -14.934 -1.241  1.00 28.59 ? 144  ARG D CB  1 
ATOM   14301 C  CG  . ARG D  1 127 ? 37.474  -15.544 0.115   1.00 31.05 ? 144  ARG D CG  1 
ATOM   14302 C  CD  . ARG D  1 127 ? 36.508  -16.731 0.037   1.00 33.55 ? 144  ARG D CD  1 
ATOM   14303 N  NE  . ARG D  1 127 ? 35.951  -17.136 1.337   1.00 35.18 ? 144  ARG D NE  1 
ATOM   14304 C  CZ  . ARG D  1 127 ? 36.561  -17.858 2.274   1.00 35.85 ? 144  ARG D CZ  1 
ATOM   14305 N  NH1 . ARG D  1 127 ? 37.796  -18.297 2.101   1.00 36.03 ? 144  ARG D NH1 1 
ATOM   14306 N  NH2 . ARG D  1 127 ? 35.924  -18.143 3.395   1.00 37.05 ? 144  ARG D NH2 1 
ATOM   14307 N  N   . SER D  1 128 ? 36.012  -12.154 -1.464  1.00 24.80 ? 145  SER D N   1 
ATOM   14308 C  CA  A SER D  1 128 ? 35.248  -11.110 -0.796  0.44 25.16 ? 145  SER D CA  1 
ATOM   14309 C  CA  B SER D  1 128 ? 35.238  -11.141 -0.762  0.56 25.17 ? 145  SER D CA  1 
ATOM   14310 C  C   . SER D  1 128 ? 33.808  -11.094 -1.301  1.00 24.64 ? 145  SER D C   1 
ATOM   14311 O  O   . SER D  1 128 ? 32.881  -10.793 -0.551  1.00 25.04 ? 145  SER D O   1 
ATOM   14312 C  CB  A SER D  1 128 ? 35.889  -9.759  -0.987  0.44 25.75 ? 145  SER D CB  1 
ATOM   14313 C  CB  B SER D  1 128 ? 35.906  -9.781  -0.793  0.56 25.82 ? 145  SER D CB  1 
ATOM   14314 O  OG  A SER D  1 128 ? 37.206  -9.740  -0.458  0.44 26.33 ? 145  SER D OG  1 
ATOM   14315 O  OG  B SER D  1 128 ? 36.112  -9.312  -2.117  0.56 26.36 ? 145  SER D OG  1 
ATOM   14316 N  N   . ILE D  1 129 ? 33.629  -11.410 -2.591  1.00 23.71 ? 146  ILE D N   1 
ATOM   14317 C  CA  . ILE D  1 129 ? 32.304  -11.477 -3.190  1.00 23.23 ? 146  ILE D CA  1 
ATOM   14318 C  C   . ILE D  1 129 ? 31.555  -12.703 -2.663  1.00 22.28 ? 146  ILE D C   1 
ATOM   14319 O  O   . ILE D  1 129 ? 30.395  -12.603 -2.272  1.00 21.98 ? 146  ILE D O   1 
ATOM   14320 C  CB  . ILE D  1 129 ? 32.394  -11.447 -4.729  1.00 23.63 ? 146  ILE D CB  1 
ATOM   14321 C  CG1 . ILE D  1 129 ? 32.732  -10.033 -5.218  1.00 23.74 ? 146  ILE D CG1 1 
ATOM   14322 C  CG2 . ILE D  1 129 ? 31.114  -11.982 -5.374  1.00 24.18 ? 146  ILE D CG2 1 
ATOM   14323 C  CD1 . ILE D  1 129 ? 33.094  -9.941  -6.688  1.00 24.35 ? 146  ILE D CD1 1 
ATOM   14324 N  N   . VAL D  1 130 ? 32.218  -13.861 -2.638  1.00 21.38 ? 147  VAL D N   1 
ATOM   14325 C  CA  . VAL D  1 130 ? 31.601  -15.072 -2.120  1.00 21.31 ? 147  VAL D CA  1 
ATOM   14326 C  C   . VAL D  1 130 ? 31.162  -14.857 -0.670  1.00 22.42 ? 147  VAL D C   1 
ATOM   14327 O  O   . VAL D  1 130 ? 30.105  -15.350 -0.266  1.00 22.37 ? 147  VAL D O   1 
ATOM   14328 C  CB  . VAL D  1 130 ? 32.562  -16.266 -2.275  1.00 21.67 ? 147  VAL D CB  1 
ATOM   14329 C  CG1 . VAL D  1 130 ? 32.153  -17.470 -1.430  1.00 21.99 ? 147  VAL D CG1 1 
ATOM   14330 C  CG2 . VAL D  1 130 ? 32.713  -16.656 -3.740  1.00 21.67 ? 147  VAL D CG2 1 
ATOM   14331 N  N   . ASP D  1 131 ? 31.950  -14.087 0.096   1.00 23.13 ? 148  ASP D N   1 
ATOM   14332 C  CA  . ASP D  1 131 ? 31.660  -13.854 1.505   1.00 24.48 ? 148  ASP D CA  1 
ATOM   14333 C  C   . ASP D  1 131 ? 30.472  -12.908 1.690   1.00 23.77 ? 148  ASP D C   1 
ATOM   14334 O  O   . ASP D  1 131 ? 29.942  -12.824 2.792   1.00 23.76 ? 148  ASP D O   1 
ATOM   14335 C  CB  . ASP D  1 131 ? 32.888  -13.369 2.259   1.00 25.96 ? 148  ASP D CB  1 
ATOM   14336 C  CG  . ASP D  1 131 ? 33.946  -14.428 2.542   1.00 27.60 ? 148  ASP D CG  1 
ATOM   14337 O  OD1 . ASP D  1 131 ? 33.659  -15.627 2.346   1.00 27.76 ? 148  ASP D OD1 1 
ATOM   14338 O  OD2 . ASP D  1 131 ? 35.061  -14.040 2.927   1.00 30.44 ? 148  ASP D OD2 1 
ATOM   14339 N  N   . ASN D  1 132 ? 30.053  -12.202 0.630   1.00 22.98 ? 149  ASN D N   1 
ATOM   14340 C  CA  . ASN D  1 132 ? 28.884  -11.335 0.691   1.00 22.75 ? 149  ASN D CA  1 
ATOM   14341 C  C   . ASN D  1 132 ? 27.580  -12.110 0.502   1.00 23.01 ? 149  ASN D C   1 
ATOM   14342 O  O   . ASN D  1 132 ? 26.508  -11.564 0.753   1.00 23.89 ? 149  ASN D O   1 
ATOM   14343 C  CB  . ASN D  1 132 ? 28.972  -10.195 -0.319  1.00 22.80 ? 149  ASN D CB  1 
ATOM   14344 C  CG  . ASN D  1 132 ? 29.937  -9.116  0.116   1.00 22.72 ? 149  ASN D CG  1 
ATOM   14345 O  OD1 . ASN D  1 132 ? 30.238  -8.989  1.309   1.00 22.21 ? 149  ASN D OD1 1 
ATOM   14346 N  ND2 . ASN D  1 132 ? 30.415  -8.318  -0.826  1.00 22.79 ? 149  ASN D ND2 1 
ATOM   14347 N  N   . TRP D  1 133 ? 27.644  -13.361 0.036   1.00 22.52 ? 150  TRP D N   1 
ATOM   14348 C  CA  . TRP D  1 133 ? 26.435  -14.160 -0.062  1.00 22.53 ? 150  TRP D CA  1 
ATOM   14349 C  C   . TRP D  1 133 ? 25.913  -14.445 1.347   1.00 23.60 ? 150  TRP D C   1 
ATOM   14350 O  O   . TRP D  1 133 ? 26.657  -14.925 2.196   1.00 23.13 ? 150  TRP D O   1 
ATOM   14351 C  CB  . TRP D  1 133 ? 26.672  -15.455 -0.851  1.00 22.36 ? 150  TRP D CB  1 
ATOM   14352 C  CG  . TRP D  1 133 ? 25.391  -16.174 -1.180  1.00 22.23 ? 150  TRP D CG  1 
ATOM   14353 C  CD1 . TRP D  1 133 ? 24.965  -17.372 -0.691  1.00 22.94 ? 150  TRP D CD1 1 
ATOM   14354 C  CD2 . TRP D  1 133 ? 24.339  -15.701 -2.049  1.00 22.44 ? 150  TRP D CD2 1 
ATOM   14355 N  NE1 . TRP D  1 133 ? 23.732  -17.681 -1.199  1.00 23.40 ? 150  TRP D NE1 1 
ATOM   14356 C  CE2 . TRP D  1 133 ? 23.319  -16.677 -2.031  1.00 22.83 ? 150  TRP D CE2 1 
ATOM   14357 C  CE3 . TRP D  1 133 ? 24.161  -14.557 -2.835  1.00 23.10 ? 150  TRP D CE3 1 
ATOM   14358 C  CZ2 . TRP D  1 133 ? 22.146  -16.544 -2.771  1.00 23.33 ? 150  TRP D CZ2 1 
ATOM   14359 C  CZ3 . TRP D  1 133 ? 23.000  -14.424 -3.565  1.00 22.97 ? 150  TRP D CZ3 1 
ATOM   14360 C  CH2 . TRP D  1 133 ? 22.006  -15.405 -3.532  1.00 23.12 ? 150  TRP D CH2 1 
ATOM   14361 N  N   . PRO D  1 134 ? 24.642  -14.103 1.661   1.00 26.09 ? 151  PRO D N   1 
ATOM   14362 C  CA  . PRO D  1 134 ? 24.144  -14.215 3.035   1.00 27.82 ? 151  PRO D CA  1 
ATOM   14363 C  C   . PRO D  1 134 ? 23.904  -15.603 3.631   1.00 28.48 ? 151  PRO D C   1 
ATOM   14364 O  O   . PRO D  1 134 ? 23.772  -15.717 4.845   1.00 32.01 ? 151  PRO D O   1 
ATOM   14365 C  CB  . PRO D  1 134 ? 22.847  -13.377 2.995   1.00 27.97 ? 151  PRO D CB  1 
ATOM   14366 C  CG  . PRO D  1 134 ? 22.412  -13.396 1.558   1.00 28.47 ? 151  PRO D CG  1 
ATOM   14367 C  CD  . PRO D  1 134 ? 23.679  -13.480 0.742   1.00 26.52 ? 151  PRO D CD  1 
ATOM   14368 N  N   . GLU D  1 135 ? 23.855  -16.650 2.797   1.00 28.68 ? 152  GLU D N   1 
ATOM   14369 C  CA  . GLU D  1 135 ? 23.577  -18.000 3.267   1.00 28.03 ? 152  GLU D CA  1 
ATOM   14370 C  C   . GLU D  1 135 ? 24.890  -18.719 3.573   1.00 26.95 ? 152  GLU D C   1 
ATOM   14371 O  O   . GLU D  1 135 ? 25.847  -18.625 2.808   1.00 24.44 ? 152  GLU D O   1 
ATOM   14372 C  CB  . GLU D  1 135 ? 22.766  -18.764 2.216   1.00 30.22 ? 152  GLU D CB  1 
ATOM   14373 C  CG  . GLU D  1 135 ? 21.527  -18.017 1.726   1.00 33.17 ? 152  GLU D CG  1 
ATOM   14374 C  CD  . GLU D  1 135 ? 20.447  -17.769 2.760   1.00 35.73 ? 152  GLU D CD  1 
ATOM   14375 O  OE1 . GLU D  1 135 ? 20.488  -18.366 3.860   1.00 37.52 ? 152  GLU D OE1 1 
ATOM   14376 O  OE2 . GLU D  1 135 ? 19.560  -16.947 2.446   1.00 41.72 ? 152  GLU D OE2 1 
ATOM   14377 N  N   . ASN D  1 136 ? 24.917  -19.481 4.673   1.00 27.78 ? 153  ASN D N   1 
ATOM   14378 C  CA  . ASN D  1 136 ? 26.164  -20.028 5.189   1.00 29.72 ? 153  ASN D CA  1 
ATOM   14379 C  C   . ASN D  1 136 ? 26.398  -21.490 4.803   1.00 27.20 ? 153  ASN D C   1 
ATOM   14380 O  O   . ASN D  1 136 ? 27.494  -21.990 5.046   1.00 25.87 ? 153  ASN D O   1 
ATOM   14381 C  CB  . ASN D  1 136 ? 26.235  -19.940 6.711   1.00 33.73 ? 153  ASN D CB  1 
ATOM   14382 C  CG  . ASN D  1 136 ? 25.975  -18.544 7.223   1.00 38.97 ? 153  ASN D CG  1 
ATOM   14383 O  OD1 . ASN D  1 136 ? 24.933  -18.291 7.841   1.00 45.33 ? 153  ASN D OD1 1 
ATOM   14384 N  ND2 . ASN D  1 136 ? 26.896  -17.627 6.970   1.00 40.16 ? 153  ASN D ND2 1 
ATOM   14385 N  N   . HIS D  1 137 ? 25.400  -22.180 4.229   1.00 26.78 ? 154  HIS D N   1 
ATOM   14386 C  CA  . HIS D  1 137 ? 25.494  -23.624 4.033   1.00 27.55 ? 154  HIS D CA  1 
ATOM   14387 C  C   . HIS D  1 137 ? 25.127  -24.042 2.606   1.00 26.07 ? 154  HIS D C   1 
ATOM   14388 O  O   . HIS D  1 137 ? 24.348  -24.977 2.415   1.00 27.03 ? 154  HIS D O   1 
ATOM   14389 C  CB  . HIS D  1 137 ? 24.593  -24.373 5.025   1.00 29.98 ? 154  HIS D CB  1 
ATOM   14390 C  CG  . HIS D  1 137 ? 24.750  -23.941 6.442   1.00 35.45 ? 154  HIS D CG  1 
ATOM   14391 N  ND1 . HIS D  1 137 ? 25.872  -24.228 7.187   1.00 38.17 ? 154  HIS D ND1 1 
ATOM   14392 C  CD2 . HIS D  1 137 ? 23.946  -23.215 7.236   1.00 36.28 ? 154  HIS D CD2 1 
ATOM   14393 C  CE1 . HIS D  1 137 ? 25.737  -23.703 8.396   1.00 39.39 ? 154  HIS D CE1 1 
ATOM   14394 N  NE2 . HIS D  1 137 ? 24.570  -23.089 8.449   1.00 39.60 ? 154  HIS D NE2 1 
ATOM   14395 N  N   . VAL D  1 138 ? 25.746  -23.405 1.605   1.00 23.20 ? 155  VAL D N   1 
ATOM   14396 C  CA  . VAL D  1 138 ? 25.481  -23.719 0.208   1.00 21.67 ? 155  VAL D CA  1 
ATOM   14397 C  C   . VAL D  1 138 ? 25.970  -25.134 -0.109  1.00 21.78 ? 155  VAL D C   1 
ATOM   14398 O  O   . VAL D  1 138 ? 27.073  -25.520 0.289   1.00 21.68 ? 155  VAL D O   1 
ATOM   14399 C  CB  . VAL D  1 138 ? 26.121  -22.669 -0.718  1.00 21.31 ? 155  VAL D CB  1 
ATOM   14400 C  CG1 . VAL D  1 138 ? 26.093  -23.083 -2.187  1.00 21.53 ? 155  VAL D CG1 1 
ATOM   14401 C  CG2 . VAL D  1 138 ? 25.468  -21.302 -0.529  1.00 21.59 ? 155  VAL D CG2 1 
ATOM   14402 N  N   . LYS D  1 139 ? 25.123  -25.879 -0.837  1.00 21.92 ? 156  LYS D N   1 
ATOM   14403 C  CA  . LYS D  1 139 ? 25.401  -27.239 -1.276  1.00 21.77 ? 156  LYS D CA  1 
ATOM   14404 C  C   . LYS D  1 139 ? 25.401  -27.360 -2.805  1.00 21.15 ? 156  LYS D C   1 
ATOM   14405 O  O   . LYS D  1 139 ? 26.065  -28.249 -3.343  1.00 20.96 ? 156  LYS D O   1 
ATOM   14406 C  CB  . LYS D  1 139 ? 24.343  -28.178 -0.688  1.00 22.14 ? 156  LYS D CB  1 
ATOM   14407 C  CG  . LYS D  1 139 ? 24.340  -28.292 0.824   1.00 24.00 ? 156  LYS D CG  1 
ATOM   14408 C  CD  . LYS D  1 139 ? 25.658  -28.712 1.460   1.00 25.70 ? 156  LYS D CD  1 
ATOM   14409 C  CE  . LYS D  1 139 ? 26.126  -30.063 1.040   1.00 27.78 ? 156  LYS D CE  1 
ATOM   14410 N  NZ  . LYS D  1 139 ? 27.481  -30.324 1.536   1.00 29.28 ? 156  LYS D NZ  1 
ATOM   14411 N  N   . ALA D  1 140 ? 24.674  -26.477 -3.509  1.00 19.63 ? 157  ALA D N   1 
ATOM   14412 C  CA  . ALA D  1 140 ? 24.517  -26.586 -4.958  1.00 19.82 ? 157  ALA D CA  1 
ATOM   14413 C  C   . ALA D  1 140 ? 24.756  -25.233 -5.629  1.00 20.05 ? 157  ALA D C   1 
ATOM   14414 O  O   . ALA D  1 140 ? 24.026  -24.279 -5.365  1.00 20.90 ? 157  ALA D O   1 
ATOM   14415 C  CB  . ALA D  1 140 ? 23.139  -27.112 -5.285  1.00 19.77 ? 157  ALA D CB  1 
ATOM   14416 N  N   . VAL D  1 141 ? 25.794  -25.168 -6.473  1.00 19.21 ? 158  VAL D N   1 
ATOM   14417 C  CA  . VAL D  1 141 ? 26.130  -23.989 -7.258  1.00 19.67 ? 158  VAL D CA  1 
ATOM   14418 C  C   . VAL D  1 141 ? 25.886  -24.307 -8.734  1.00 19.55 ? 158  VAL D C   1 
ATOM   14419 O  O   . VAL D  1 141 ? 26.333  -25.349 -9.212  1.00 19.83 ? 158  VAL D O   1 
ATOM   14420 C  CB  . VAL D  1 141 ? 27.606  -23.600 -7.018  1.00 20.25 ? 158  VAL D CB  1 
ATOM   14421 C  CG1 . VAL D  1 141 ? 28.064  -22.459 -7.920  1.00 21.09 ? 158  VAL D CG1 1 
ATOM   14422 C  CG2 . VAL D  1 141 ? 27.885  -23.262 -5.558  1.00 20.37 ? 158  VAL D CG2 1 
ATOM   14423 N  N   . VAL D  1 142 ? 25.178  -23.415 -9.449  1.00 18.56 ? 159  VAL D N   1 
ATOM   14424 C  CA  . VAL D  1 142 ? 25.106  -23.467 -10.906 1.00 18.21 ? 159  VAL D CA  1 
ATOM   14425 C  C   . VAL D  1 142 ? 25.737  -22.179 -11.447 1.00 19.22 ? 159  VAL D C   1 
ATOM   14426 O  O   . VAL D  1 142 ? 25.343  -21.078 -11.051 1.00 18.08 ? 159  VAL D O   1 
ATOM   14427 C  CB  . VAL D  1 142 ? 23.675  -23.672 -11.444 1.00 18.11 ? 159  VAL D CB  1 
ATOM   14428 C  CG1 . VAL D  1 142 ? 23.620  -23.631 -12.968 1.00 18.07 ? 159  VAL D CG1 1 
ATOM   14429 C  CG2 . VAL D  1 142 ? 23.036  -24.959 -10.922 1.00 17.80 ? 159  VAL D CG2 1 
ATOM   14430 N  N   . VAL D  1 143 ? 26.734  -22.327 -12.336 1.00 18.62 ? 160  VAL D N   1 
ATOM   14431 C  CA  . VAL D  1 143 ? 27.533  -21.208 -12.817 1.00 19.26 ? 160  VAL D CA  1 
ATOM   14432 C  C   . VAL D  1 143 ? 27.513  -21.181 -14.351 1.00 20.94 ? 160  VAL D C   1 
ATOM   14433 O  O   . VAL D  1 143 ? 27.617  -22.231 -14.989 1.00 20.78 ? 160  VAL D O   1 
ATOM   14434 C  CB  . VAL D  1 143 ? 28.971  -21.281 -12.269 1.00 19.39 ? 160  VAL D CB  1 
ATOM   14435 C  CG1 . VAL D  1 143 ? 29.634  -22.627 -12.543 1.00 18.93 ? 160  VAL D CG1 1 
ATOM   14436 C  CG2 . VAL D  1 143 ? 29.850  -20.143 -12.784 1.00 19.87 ? 160  VAL D CG2 1 
ATOM   14437 N  N   . THR D  1 144 ? 27.373  -19.970 -14.922 1.00 21.16 ? 161  THR D N   1 
ATOM   14438 C  CA  . THR D  1 144 ? 27.472  -19.729 -16.358 1.00 22.13 ? 161  THR D CA  1 
ATOM   14439 C  C   . THR D  1 144 ? 28.364  -18.509 -16.599 1.00 22.28 ? 161  THR D C   1 
ATOM   14440 O  O   . THR D  1 144 ? 28.553  -17.691 -15.700 1.00 22.22 ? 161  THR D O   1 
ATOM   14441 C  CB  . THR D  1 144 ? 26.084  -19.521 -16.972 1.00 22.70 ? 161  THR D CB  1 
ATOM   14442 O  OG1 . THR D  1 144 ? 26.275  -19.448 -18.386 1.00 23.22 ? 161  THR D OG1 1 
ATOM   14443 C  CG2 . THR D  1 144 ? 25.396  -18.251 -16.502 1.00 23.29 ? 161  THR D CG2 1 
ATOM   14444 N  N   . ASP D  1 145 ? 28.903  -18.399 -17.820 1.00 22.93 ? 162  ASP D N   1 
ATOM   14445 C  CA  . ASP D  1 145 ? 29.539  -17.172 -18.286 1.00 23.17 ? 162  ASP D CA  1 
ATOM   14446 C  C   . ASP D  1 145 ? 28.715  -16.523 -19.403 1.00 24.41 ? 162  ASP D C   1 
ATOM   14447 O  O   . ASP D  1 145 ? 29.131  -15.517 -19.982 1.00 25.13 ? 162  ASP D O   1 
ATOM   14448 C  CB  . ASP D  1 145 ? 30.990  -17.401 -18.687 1.00 23.55 ? 162  ASP D CB  1 
ATOM   14449 C  CG  . ASP D  1 145 ? 31.229  -18.213 -19.955 1.00 23.70 ? 162  ASP D CG  1 
ATOM   14450 O  OD1 . ASP D  1 145 ? 30.238  -18.698 -20.530 1.00 22.06 ? 162  ASP D OD1 1 
ATOM   14451 O  OD2 . ASP D  1 145 ? 32.415  -18.346 -20.352 1.00 23.89 ? 162  ASP D OD2 1 
ATOM   14452 N  N   . GLY D  1 146 ? 27.550  -17.104 -19.710 1.00 24.38 ? 163  GLY D N   1 
ATOM   14453 C  CA  . GLY D  1 146 ? 26.607  -16.514 -20.646 1.00 24.41 ? 163  GLY D CA  1 
ATOM   14454 C  C   . GLY D  1 146 ? 27.045  -16.626 -22.109 1.00 25.20 ? 163  GLY D C   1 
ATOM   14455 O  O   . GLY D  1 146 ? 26.430  -16.008 -22.975 1.00 24.64 ? 163  GLY D O   1 
ATOM   14456 N  N   . GLU D  1 147 ? 28.079  -17.427 -22.400 1.00 26.10 ? 164  GLU D N   1 
ATOM   14457 C  CA  . GLU D  1 147 ? 28.653  -17.426 -23.740 1.00 26.96 ? 164  GLU D CA  1 
ATOM   14458 C  C   . GLU D  1 147 ? 27.769  -18.206 -24.713 1.00 27.39 ? 164  GLU D C   1 
ATOM   14459 O  O   . GLU D  1 147 ? 27.654  -17.820 -25.873 1.00 25.97 ? 164  GLU D O   1 
ATOM   14460 C  CB  . GLU D  1 147 ? 30.090  -17.944 -23.820 1.00 27.37 ? 164  GLU D CB  1 
ATOM   14461 C  CG  . GLU D  1 147 ? 30.696  -17.719 -25.205 1.00 28.60 ? 164  GLU D CG  1 
ATOM   14462 C  CD  . GLU D  1 147 ? 32.206  -17.801 -25.349 1.00 31.15 ? 164  GLU D CD  1 
ATOM   14463 O  OE1 . GLU D  1 147 ? 32.926  -18.129 -24.381 1.00 29.59 ? 164  GLU D OE1 1 
ATOM   14464 O  OE2 . GLU D  1 147 ? 32.663  -17.498 -26.475 1.00 33.90 ? 164  GLU D OE2 1 
ATOM   14465 N  N   . ARG D  1 148 ? 27.160  -19.306 -24.251 1.00 27.81 ? 165  ARG D N   1 
ATOM   14466 C  CA  . ARG D  1 148 ? 26.425  -20.186 -25.143 1.00 29.94 ? 165  ARG D CA  1 
ATOM   14467 C  C   . ARG D  1 148 ? 25.078  -20.549 -24.526 1.00 29.10 ? 165  ARG D C   1 
ATOM   14468 O  O   . ARG D  1 148 ? 24.848  -21.693 -24.136 1.00 27.83 ? 165  ARG D O   1 
ATOM   14469 C  CB  . ARG D  1 148 ? 27.260  -21.436 -25.442 1.00 34.15 ? 165  ARG D CB  1 
ATOM   14470 C  CG  . ARG D  1 148 ? 26.776  -22.228 -26.650 1.00 38.15 ? 165  ARG D CG  1 
ATOM   14471 C  CD  . ARG D  1 148 ? 26.691  -23.715 -26.343 1.00 42.97 ? 165  ARG D CD  1 
ATOM   14472 N  NE  . ARG D  1 148 ? 25.620  -23.957 -25.366 1.00 47.65 ? 165  ARG D NE  1 
ATOM   14473 C  CZ  . ARG D  1 148 ? 25.282  -25.116 -24.808 1.00 50.09 ? 165  ARG D CZ  1 
ATOM   14474 N  NH1 . ARG D  1 148 ? 25.939  -26.225 -25.104 1.00 52.85 ? 165  ARG D NH1 1 
ATOM   14475 N  NH2 . ARG D  1 148 ? 24.274  -25.153 -23.949 1.00 48.75 ? 165  ARG D NH2 1 
ATOM   14476 N  N   . ILE D  1 149 ? 24.179  -19.566 -24.459 1.00 30.32 ? 166  ILE D N   1 
ATOM   14477 C  CA  . ILE D  1 149 ? 22.850  -19.799 -23.923 1.00 31.73 ? 166  ILE D CA  1 
ATOM   14478 C  C   . ILE D  1 149 ? 22.089  -20.644 -24.938 1.00 35.11 ? 166  ILE D C   1 
ATOM   14479 O  O   . ILE D  1 149 ? 21.935  -20.241 -26.094 1.00 34.32 ? 166  ILE D O   1 
ATOM   14480 C  CB  . ILE D  1 149 ? 22.125  -18.476 -23.601 1.00 31.09 ? 166  ILE D CB  1 
ATOM   14481 C  CG1 . ILE D  1 149 ? 22.905  -17.625 -22.595 1.00 31.48 ? 166  ILE D CG1 1 
ATOM   14482 C  CG2 . ILE D  1 149 ? 20.691  -18.728 -23.133 1.00 30.86 ? 166  ILE D CG2 1 
ATOM   14483 C  CD1 . ILE D  1 149 ? 23.142  -18.283 -21.248 1.00 32.15 ? 166  ILE D CD1 1 
ATOM   14484 N  N   . LEU D  1 150 ? 21.626  -21.816 -24.485 1.00 37.35 ? 167  LEU D N   1 
ATOM   14485 C  CA  . LEU D  1 150 ? 20.957  -22.778 -25.344 1.00 39.16 ? 167  LEU D CA  1 
ATOM   14486 C  C   . LEU D  1 150 ? 19.851  -22.078 -26.128 1.00 39.01 ? 167  LEU D C   1 
ATOM   14487 O  O   . LEU D  1 150 ? 18.810  -21.731 -25.569 1.00 38.63 ? 167  LEU D O   1 
ATOM   14488 C  CB  . LEU D  1 150 ? 20.401  -23.926 -24.499 1.00 41.95 ? 167  LEU D CB  1 
ATOM   14489 C  CG  . LEU D  1 150 ? 19.705  -25.051 -25.274 1.00 44.04 ? 167  LEU D CG  1 
ATOM   14490 C  CD1 . LEU D  1 150 ? 20.717  -25.840 -26.089 1.00 44.31 ? 167  LEU D CD1 1 
ATOM   14491 C  CD2 . LEU D  1 150 ? 18.920  -25.970 -24.348 1.00 45.17 ? 167  LEU D CD2 1 
ATOM   14492 N  N   . GLY D  1 151 ? 20.108  -21.847 -27.420 1.00 38.96 ? 168  GLY D N   1 
ATOM   14493 C  CA  . GLY D  1 151 ? 19.098  -21.327 -28.325 1.00 38.31 ? 168  GLY D CA  1 
ATOM   14494 C  C   . GLY D  1 151 ? 19.308  -19.856 -28.686 1.00 39.01 ? 168  GLY D C   1 
ATOM   14495 O  O   . GLY D  1 151 ? 18.693  -19.385 -29.639 1.00 39.95 ? 168  GLY D O   1 
ATOM   14496 N  N   . LEU D  1 152 ? 20.157  -19.130 -27.939 1.00 36.32 ? 169  LEU D N   1 
ATOM   14497 C  CA  . LEU D  1 152 ? 20.255  -17.682 -28.104 1.00 35.45 ? 169  LEU D CA  1 
ATOM   14498 C  C   . LEU D  1 152 ? 21.697  -17.198 -28.291 1.00 33.63 ? 169  LEU D C   1 
ATOM   14499 O  O   . LEU D  1 152 ? 21.906  -16.073 -28.738 1.00 33.03 ? 169  LEU D O   1 
ATOM   14500 C  CB  . LEU D  1 152 ? 19.588  -16.999 -26.910 1.00 36.87 ? 169  LEU D CB  1 
ATOM   14501 C  CG  . LEU D  1 152 ? 18.090  -17.275 -26.720 1.00 38.12 ? 169  LEU D CG  1 
ATOM   14502 C  CD1 . LEU D  1 152 ? 17.597  -16.748 -25.382 1.00 37.69 ? 169  LEU D CD1 1 
ATOM   14503 C  CD2 . LEU D  1 152 ? 17.261  -16.682 -27.850 1.00 39.61 ? 169  LEU D CD2 1 
ATOM   14504 N  N   . GLY D  1 153 ? 22.692  -18.026 -27.952 1.00 32.16 ? 170  GLY D N   1 
ATOM   14505 C  CA  . GLY D  1 153 ? 24.087  -17.660 -28.131 1.00 30.30 ? 170  GLY D CA  1 
ATOM   14506 C  C   . GLY D  1 153 ? 24.605  -16.812 -26.971 1.00 29.52 ? 170  GLY D C   1 
ATOM   14507 O  O   . GLY D  1 153 ? 24.284  -17.078 -25.813 1.00 28.93 ? 170  GLY D O   1 
ATOM   14508 N  N   . ASP D  1 154 ? 25.403  -15.787 -27.302 1.00 27.76 ? 171  ASP D N   1 
ATOM   14509 C  CA  . ASP D  1 154 ? 26.152  -15.023 -26.314 1.00 28.38 ? 171  ASP D CA  1 
ATOM   14510 C  C   . ASP D  1 154 ? 25.298  -13.869 -25.782 1.00 28.37 ? 171  ASP D C   1 
ATOM   14511 O  O   . ASP D  1 154 ? 25.117  -12.867 -26.470 1.00 28.03 ? 171  ASP D O   1 
ATOM   14512 C  CB  . ASP D  1 154 ? 27.477  -14.569 -26.908 1.00 28.02 ? 171  ASP D CB  1 
ATOM   14513 C  CG  . ASP D  1 154 ? 28.412  -13.818 -25.972 1.00 27.75 ? 171  ASP D CG  1 
ATOM   14514 O  OD1 . ASP D  1 154 ? 27.963  -13.436 -24.870 1.00 27.41 ? 171  ASP D OD1 1 
ATOM   14515 O  OD2 . ASP D  1 154 ? 29.592  -13.631 -26.346 1.00 27.53 ? 171  ASP D OD2 1 
ATOM   14516 N  N   . LEU D  1 155 ? 24.792  -14.012 -24.548 1.00 26.82 ? 172  LEU D N   1 
ATOM   14517 C  CA  . LEU D  1 155 ? 23.951  -12.998 -23.925 1.00 27.57 ? 172  LEU D CA  1 
ATOM   14518 C  C   . LEU D  1 155 ? 24.654  -12.347 -22.730 1.00 26.29 ? 172  LEU D C   1 
ATOM   14519 O  O   . LEU D  1 155 ? 24.048  -11.553 -22.016 1.00 25.96 ? 172  LEU D O   1 
ATOM   14520 C  CB  . LEU D  1 155 ? 22.621  -13.621 -23.499 1.00 28.62 ? 172  LEU D CB  1 
ATOM   14521 C  CG  . LEU D  1 155 ? 21.721  -14.160 -24.616 1.00 30.84 ? 172  LEU D CG  1 
ATOM   14522 C  CD1 . LEU D  1 155 ? 20.448  -14.738 -24.017 1.00 31.72 ? 172  LEU D CD1 1 
ATOM   14523 C  CD2 . LEU D  1 155 ? 21.374  -13.102 -25.653 1.00 31.25 ? 172  LEU D CD2 1 
ATOM   14524 N  N   . GLY D  1 156 ? 25.925  -12.685 -22.499 1.00 25.92 ? 173  GLY D N   1 
ATOM   14525 C  CA  . GLY D  1 156 ? 26.663  -12.147 -21.370 1.00 25.48 ? 173  GLY D CA  1 
ATOM   14526 C  C   . GLY D  1 156 ? 25.869  -12.269 -20.071 1.00 25.72 ? 173  GLY D C   1 
ATOM   14527 O  O   . GLY D  1 156 ? 25.306  -13.321 -19.778 1.00 25.90 ? 173  GLY D O   1 
ATOM   14528 N  N   . VAL D  1 157 ? 25.794  -11.158 -19.329 1.00 25.40 ? 174  VAL D N   1 
ATOM   14529 C  CA  . VAL D  1 157 ? 25.142  -11.112 -18.031 1.00 28.35 ? 174  VAL D CA  1 
ATOM   14530 C  C   . VAL D  1 157 ? 23.630  -11.300 -18.164 1.00 28.75 ? 174  VAL D C   1 
ATOM   14531 O  O   . VAL D  1 157 ? 22.976  -11.669 -17.193 1.00 30.37 ? 174  VAL D O   1 
ATOM   14532 C  CB  . VAL D  1 157 ? 25.505  -9.782  -17.339 1.00 29.75 ? 174  VAL D CB  1 
ATOM   14533 C  CG1 . VAL D  1 157 ? 24.598  -9.460  -16.163 1.00 31.35 ? 174  VAL D CG1 1 
ATOM   14534 C  CG2 . VAL D  1 157 ? 26.963  -9.777  -16.903 1.00 30.07 ? 174  VAL D CG2 1 
ATOM   14535 N  N   . TYR D  1 158 ? 23.078  -11.108 -19.368 1.00 29.47 ? 175  TYR D N   1 
ATOM   14536 C  CA  . TYR D  1 158 ? 21.653  -11.307 -19.592 1.00 32.15 ? 175  TYR D CA  1 
ATOM   14537 C  C   . TYR D  1 158 ? 21.274  -12.790 -19.504 1.00 33.39 ? 175  TYR D C   1 
ATOM   14538 O  O   . TYR D  1 158 ? 20.111  -13.116 -19.732 1.00 35.12 ? 175  TYR D O   1 
ATOM   14539 C  CB  . TYR D  1 158 ? 21.173  -10.741 -20.937 1.00 32.67 ? 175  TYR D CB  1 
ATOM   14540 C  CG  . TYR D  1 158 ? 20.883  -9.247  -21.057 1.00 34.03 ? 175  TYR D CG  1 
ATOM   14541 C  CD1 . TYR D  1 158 ? 20.719  -8.411  -19.951 1.00 36.04 ? 175  TYR D CD1 1 
ATOM   14542 C  CD2 . TYR D  1 158 ? 20.706  -8.684  -22.312 1.00 35.52 ? 175  TYR D CD2 1 
ATOM   14543 C  CE1 . TYR D  1 158 ? 20.433  -7.060  -20.102 1.00 35.53 ? 175  TYR D CE1 1 
ATOM   14544 C  CE2 . TYR D  1 158 ? 20.411  -7.340  -22.476 1.00 37.95 ? 175  TYR D CE2 1 
ATOM   14545 C  CZ  . TYR D  1 158 ? 20.273  -6.524  -21.369 1.00 37.60 ? 175  TYR D CZ  1 
ATOM   14546 O  OH  . TYR D  1 158 ? 19.977  -5.208  -21.587 1.00 38.52 ? 175  TYR D OH  1 
ATOM   14547 N  N   A GLY D  1 159 ? 22.228  -13.661 -19.130 0.54 31.74 ? 176  GLY D N   1 
ATOM   14548 N  N   B GLY D  1 159 ? 22.251  -13.669 -19.238 0.46 32.02 ? 176  GLY D N   1 
ATOM   14549 C  CA  A GLY D  1 159 ? 21.969  -15.081 -18.950 0.54 31.96 ? 176  GLY D CA  1 
ATOM   14550 C  CA  B GLY D  1 159 ? 21.984  -15.074 -18.980 0.46 32.40 ? 176  GLY D CA  1 
ATOM   14551 C  C   A GLY D  1 159 ? 22.181  -15.573 -17.513 0.54 30.71 ? 176  GLY D C   1 
ATOM   14552 C  C   B GLY D  1 159 ? 21.875  -15.361 -17.483 0.46 31.76 ? 176  GLY D C   1 
ATOM   14553 O  O   A GLY D  1 159 ? 22.378  -16.766 -17.305 0.54 30.11 ? 176  GLY D O   1 
ATOM   14554 O  O   B GLY D  1 159 ? 21.762  -16.517 -17.081 0.46 29.92 ? 176  GLY D O   1 
ATOM   14555 N  N   A MET D  1 160 ? 22.115  -14.671 -16.521 0.54 29.29 ? 177  MET D N   1 
ATOM   14556 N  N   B MET D  1 160 ? 21.908  -14.297 -16.669 0.46 30.71 ? 177  MET D N   1 
ATOM   14557 C  CA  A MET D  1 160 ? 22.104  -15.066 -15.117 0.54 27.14 ? 177  MET D CA  1 
ATOM   14558 C  CA  B MET D  1 160 ? 21.855  -14.425 -15.222 0.46 29.20 ? 177  MET D CA  1 
ATOM   14559 C  C   A MET D  1 160 ? 20.768  -15.736 -14.792 0.54 26.44 ? 177  MET D C   1 
ATOM   14560 C  C   B MET D  1 160 ? 20.665  -15.297 -14.832 0.46 28.33 ? 177  MET D C   1 
ATOM   14561 O  O   A MET D  1 160 ? 20.689  -16.554 -13.879 0.54 26.17 ? 177  MET D O   1 
ATOM   14562 O  O   B MET D  1 160 ? 20.648  -15.879 -13.751 0.46 28.55 ? 177  MET D O   1 
ATOM   14563 C  CB  A MET D  1 160 ? 22.355  -13.858 -14.202 0.54 26.51 ? 177  MET D CB  1 
ATOM   14564 C  CB  B MET D  1 160 ? 21.735  -13.055 -14.538 0.46 28.72 ? 177  MET D CB  1 
ATOM   14565 C  CG  A MET D  1 160 ? 22.081  -14.064 -12.707 0.54 25.52 ? 177  MET D CG  1 
ATOM   14566 C  CG  B MET D  1 160 ? 20.475  -12.275 -14.895 0.46 28.39 ? 177  MET D CG  1 
ATOM   14567 S  SD  A MET D  1 160 ? 22.949  -15.419 -11.888 0.54 23.52 ? 177  MET D SD  1 
ATOM   14568 S  SD  B MET D  1 160 ? 20.205  -10.777 -13.920 0.46 28.41 ? 177  MET D SD  1 
ATOM   14569 C  CE  A MET D  1 160 ? 23.520  -14.565 -10.414 0.54 23.26 ? 177  MET D CE  1 
ATOM   14570 C  CE  B MET D  1 160 ? 21.382  -9.649  -14.674 0.46 27.08 ? 177  MET D CE  1 
ATOM   14571 N  N   A GLY D  1 161 ? 19.724  -15.404 -15.562 0.54 25.77 ? 178  GLY D N   1 
ATOM   14572 N  N   B GLY D  1 161 ? 19.677  -15.379 -15.728 0.46 27.03 ? 178  GLY D N   1 
ATOM   14573 C  CA  A GLY D  1 161 ? 18.429  -16.052 -15.428 0.54 25.60 ? 178  GLY D CA  1 
ATOM   14574 C  CA  B GLY D  1 161 ? 18.422  -16.053 -15.439 0.46 26.46 ? 178  GLY D CA  1 
ATOM   14575 C  C   A GLY D  1 161 ? 18.528  -17.574 -15.529 0.54 25.01 ? 178  GLY D C   1 
ATOM   14576 C  C   B GLY D  1 161 ? 18.539  -17.574 -15.517 0.46 25.51 ? 178  GLY D C   1 
ATOM   14577 O  O   A GLY D  1 161 ? 17.716  -18.285 -14.938 0.54 23.67 ? 178  GLY D O   1 
ATOM   14578 O  O   B GLY D  1 161 ? 17.742  -18.284 -14.906 0.46 24.31 ? 178  GLY D O   1 
ATOM   14579 N  N   . ILE D  1 162 ? 19.524  -18.065 -16.281 1.00 24.68 ? 179  ILE D N   1 
ATOM   14580 C  CA  . ILE D  1 162 ? 19.672  -19.492 -16.533 1.00 25.64 ? 179  ILE D CA  1 
ATOM   14581 C  C   . ILE D  1 162 ? 20.031  -20.227 -15.236 1.00 24.46 ? 179  ILE D C   1 
ATOM   14582 O  O   . ILE D  1 162 ? 19.328  -21.166 -14.870 1.00 23.70 ? 179  ILE D O   1 
ATOM   14583 C  CB  . ILE D  1 162 ? 20.648  -19.765 -17.697 1.00 25.94 ? 179  ILE D CB  1 
ATOM   14584 C  CG1 . ILE D  1 162 ? 19.942  -19.613 -19.053 1.00 27.36 ? 179  ILE D CG1 1 
ATOM   14585 C  CG2 . ILE D  1 162 ? 21.295  -21.145 -17.585 1.00 26.38 ? 179  ILE D CG2 1 
ATOM   14586 C  CD1 . ILE D  1 162 ? 19.338  -18.242 -19.303 1.00 27.62 ? 179  ILE D CD1 1 
ATOM   14587 N  N   . PRO D  1 163 ? 21.117  -19.882 -14.504 1.00 23.81 ? 180  PRO D N   1 
ATOM   14588 C  CA  . PRO D  1 163 ? 21.369  -20.512 -13.205 1.00 23.00 ? 180  PRO D CA  1 
ATOM   14589 C  C   . PRO D  1 163 ? 20.199  -20.426 -12.223 1.00 22.31 ? 180  PRO D C   1 
ATOM   14590 O  O   . PRO D  1 163 ? 19.918  -21.395 -11.519 1.00 20.35 ? 180  PRO D O   1 
ATOM   14591 C  CB  . PRO D  1 163 ? 22.612  -19.781 -12.701 1.00 24.49 ? 180  PRO D CB  1 
ATOM   14592 C  CG  . PRO D  1 163 ? 23.339  -19.391 -13.970 1.00 24.84 ? 180  PRO D CG  1 
ATOM   14593 C  CD  . PRO D  1 163 ? 22.217  -18.998 -14.921 1.00 24.75 ? 180  PRO D CD  1 
ATOM   14594 N  N   . VAL D  1 164 ? 19.518  -19.271 -12.195 1.00 21.52 ? 181  VAL D N   1 
ATOM   14595 C  CA  . VAL D  1 164 ? 18.373  -19.056 -11.320 1.00 22.00 ? 181  VAL D CA  1 
ATOM   14596 C  C   . VAL D  1 164 ? 17.302  -20.103 -11.618 1.00 20.92 ? 181  VAL D C   1 
ATOM   14597 O  O   . VAL D  1 164 ? 16.837  -20.791 -10.712 1.00 20.39 ? 181  VAL D O   1 
ATOM   14598 C  CB  . VAL D  1 164 ? 17.798  -17.629 -11.439 1.00 22.67 ? 181  VAL D CB  1 
ATOM   14599 C  CG1 . VAL D  1 164 ? 16.505  -17.459 -10.651 1.00 23.69 ? 181  VAL D CG1 1 
ATOM   14600 C  CG2 . VAL D  1 164 ? 18.808  -16.578 -11.007 1.00 23.05 ? 181  VAL D CG2 1 
ATOM   14601 N  N   . GLY D  1 165 ? 16.910  -20.209 -12.892 1.00 21.13 ? 182  GLY D N   1 
ATOM   14602 C  CA  . GLY D  1 165 ? 15.855  -21.123 -13.298 1.00 20.95 ? 182  GLY D CA  1 
ATOM   14603 C  C   . GLY D  1 165 ? 16.255  -22.585 -13.106 1.00 21.64 ? 182  GLY D C   1 
ATOM   14604 O  O   . GLY D  1 165 ? 15.431  -23.407 -12.717 1.00 20.90 ? 182  GLY D O   1 
ATOM   14605 N  N   . LYS D  1 166 ? 17.522  -22.901 -13.398 1.00 21.17 ? 183  LYS D N   1 
ATOM   14606 C  CA  . LYS D  1 166 ? 18.038  -24.244 -13.197 1.00 21.85 ? 183  LYS D CA  1 
ATOM   14607 C  C   . LYS D  1 166 ? 17.854  -24.648 -11.734 1.00 20.55 ? 183  LYS D C   1 
ATOM   14608 O  O   . LYS D  1 166 ? 17.352  -25.730 -11.442 1.00 20.38 ? 183  LYS D O   1 
ATOM   14609 C  CB  . LYS D  1 166 ? 19.516  -24.298 -13.595 1.00 22.96 ? 183  LYS D CB  1 
ATOM   14610 C  CG  . LYS D  1 166 ? 20.106  -25.688 -13.740 1.00 25.33 ? 183  LYS D CG  1 
ATOM   14611 C  CD  . LYS D  1 166 ? 19.871  -26.262 -15.126 1.00 27.26 ? 183  LYS D CD  1 
ATOM   14612 C  CE  . LYS D  1 166 ? 20.549  -27.567 -15.349 1.00 27.62 ? 183  LYS D CE  1 
ATOM   14613 N  NZ  . LYS D  1 166 ? 20.303  -28.003 -16.723 1.00 27.85 ? 183  LYS D NZ  1 
ATOM   14614 N  N   . LEU D  1 167 ? 18.250  -23.769 -10.811 1.00 19.62 ? 184  LEU D N   1 
ATOM   14615 C  CA  . LEU D  1 167 ? 18.196  -24.096 -9.396  1.00 20.60 ? 184  LEU D CA  1 
ATOM   14616 C  C   . LEU D  1 167 ? 16.753  -24.146 -8.888  1.00 20.93 ? 184  LEU D C   1 
ATOM   14617 O  O   . LEU D  1 167 ? 16.467  -24.907 -7.968  1.00 21.22 ? 184  LEU D O   1 
ATOM   14618 C  CB  . LEU D  1 167 ? 19.078  -23.141 -8.594  1.00 20.09 ? 184  LEU D CB  1 
ATOM   14619 C  CG  . LEU D  1 167 ? 20.582  -23.408 -8.712  1.00 19.80 ? 184  LEU D CG  1 
ATOM   14620 C  CD1 . LEU D  1 167 ? 21.385  -22.236 -8.211  1.00 20.12 ? 184  LEU D CD1 1 
ATOM   14621 C  CD2 . LEU D  1 167 ? 20.979  -24.675 -7.970  1.00 19.71 ? 184  LEU D CD2 1 
ATOM   14622 N  N   . CYS D  1 168 ? 15.836  -23.386 -9.500  1.00 20.84 ? 185  CYS D N   1 
ATOM   14623 C  CA  . CYS D  1 168 ? 14.418  -23.555 -9.209  1.00 23.22 ? 185  CYS D CA  1 
ATOM   14624 C  C   . CYS D  1 168 ? 13.981  -25.004 -9.454  1.00 22.79 ? 185  CYS D C   1 
ATOM   14625 O  O   . CYS D  1 168 ? 13.158  -25.523 -8.705  1.00 23.94 ? 185  CYS D O   1 
ATOM   14626 C  CB  . CYS D  1 168 ? 13.546  -22.595 -10.013 1.00 25.25 ? 185  CYS D CB  1 
ATOM   14627 S  SG  . CYS D  1 168 ? 13.684  -20.875 -9.461  1.00 30.42 ? 185  CYS D SG  1 
ATOM   14628 N  N   . LEU D  1 169 ? 14.558  -25.658 -10.476 1.00 22.58 ? 186  LEU D N   1 
ATOM   14629 C  CA  . LEU D  1 169 ? 14.205  -27.030 -10.823 1.00 23.37 ? 186  LEU D CA  1 
ATOM   14630 C  C   . LEU D  1 169 ? 14.920  -28.033 -9.916  1.00 22.09 ? 186  LEU D C   1 
ATOM   14631 O  O   . LEU D  1 169 ? 14.393  -29.119 -9.665  1.00 21.62 ? 186  LEU D O   1 
ATOM   14632 C  CB  . LEU D  1 169 ? 14.477  -27.316 -12.303 1.00 23.78 ? 186  LEU D CB  1 
ATOM   14633 C  CG  . LEU D  1 169 ? 13.709  -26.444 -13.305 1.00 24.84 ? 186  LEU D CG  1 
ATOM   14634 C  CD1 . LEU D  1 169 ? 14.037  -26.810 -14.748 1.00 25.17 ? 186  LEU D CD1 1 
ATOM   14635 C  CD2 . LEU D  1 169 ? 12.210  -26.515 -13.089 1.00 26.50 ? 186  LEU D CD2 1 
ATOM   14636 N  N   . TYR D  1 170 ? 16.111  -27.682 -9.417  1.00 21.32 ? 187  TYR D N   1 
ATOM   14637 C  CA  . TYR D  1 170 ? 16.754  -28.481 -8.381  1.00 21.21 ? 187  TYR D CA  1 
ATOM   14638 C  C   . TYR D  1 170 ? 15.786  -28.657 -7.208  1.00 21.26 ? 187  TYR D C   1 
ATOM   14639 O  O   . TYR D  1 170 ? 15.611  -29.763 -6.686  1.00 20.66 ? 187  TYR D O   1 
ATOM   14640 C  CB  . TYR D  1 170 ? 18.055  -27.869 -7.851  1.00 20.73 ? 187  TYR D CB  1 
ATOM   14641 C  CG  . TYR D  1 170 ? 19.339  -28.113 -8.636  1.00 21.31 ? 187  TYR D CG  1 
ATOM   14642 C  CD1 . TYR D  1 170 ? 19.407  -27.971 -10.017 1.00 20.85 ? 187  TYR D CD1 1 
ATOM   14643 C  CD2 . TYR D  1 170 ? 20.510  -28.458 -7.968  1.00 21.95 ? 187  TYR D CD2 1 
ATOM   14644 C  CE1 . TYR D  1 170 ? 20.598  -28.167 -10.706 1.00 21.34 ? 187  TYR D CE1 1 
ATOM   14645 C  CE2 . TYR D  1 170 ? 21.700  -28.674 -8.644  1.00 22.25 ? 187  TYR D CE2 1 
ATOM   14646 C  CZ  . TYR D  1 170 ? 21.742  -28.541 -10.020 1.00 22.28 ? 187  TYR D CZ  1 
ATOM   14647 O  OH  . TYR D  1 170 ? 22.934  -28.747 -10.654 1.00 23.50 ? 187  TYR D OH  1 
ATOM   14648 N  N   . THR D  1 171 ? 15.156  -27.551 -6.792  1.00 20.89 ? 188  THR D N   1 
ATOM   14649 C  CA  . THR D  1 171 ? 14.286  -27.564 -5.629  1.00 21.01 ? 188  THR D CA  1 
ATOM   14650 C  C   . THR D  1 171 ? 12.961  -28.238 -5.979  1.00 21.73 ? 188  THR D C   1 
ATOM   14651 O  O   . THR D  1 171 ? 12.527  -29.148 -5.277  1.00 21.73 ? 188  THR D O   1 
ATOM   14652 C  CB  . THR D  1 171 ? 14.078  -26.146 -5.100  1.00 21.04 ? 188  THR D CB  1 
ATOM   14653 O  OG1 . THR D  1 171 ? 15.362  -25.663 -4.725  1.00 20.31 ? 188  THR D OG1 1 
ATOM   14654 C  CG2 . THR D  1 171 ? 13.173  -26.098 -3.882  1.00 20.87 ? 188  THR D CG2 1 
ATOM   14655 N  N   . ALA D  1 172 ? 12.304  -27.771 -7.045  1.00 23.04 ? 189  ALA D N   1 
ATOM   14656 C  CA  . ALA D  1 172 ? 10.955  -28.223 -7.355  1.00 23.53 ? 189  ALA D CA  1 
ATOM   14657 C  C   . ALA D  1 172 ? 10.943  -29.709 -7.705  1.00 23.42 ? 189  ALA D C   1 
ATOM   14658 O  O   . ALA D  1 172 ? 9.987   -30.403 -7.376  1.00 23.80 ? 189  ALA D O   1 
ATOM   14659 C  CB  . ALA D  1 172 ? 10.363  -27.394 -8.475  1.00 23.85 ? 189  ALA D CB  1 
ATOM   14660 N  N   . CYS D  1 173 ? 12.006  -30.203 -8.354  1.00 23.12 ? 190  CYS D N   1 
ATOM   14661 C  CA  . CYS D  1 173 ? 12.002  -31.563 -8.872  1.00 24.07 ? 190  CYS D CA  1 
ATOM   14662 C  C   . CYS D  1 173 ? 12.573  -32.561 -7.860  1.00 24.62 ? 190  CYS D C   1 
ATOM   14663 O  O   . CYS D  1 173 ? 12.096  -33.690 -7.796  1.00 25.73 ? 190  CYS D O   1 
ATOM   14664 C  CB  . CYS D  1 173 ? 12.729  -31.669 -10.208 1.00 24.48 ? 190  CYS D CB  1 
ATOM   14665 S  SG  . CYS D  1 173 ? 11.958  -30.706 -11.538 1.00 26.44 ? 190  CYS D SG  1 
ATOM   14666 N  N   . ALA D  1 174 ? 13.593  -32.167 -7.086  1.00 23.26 ? 191  ALA D N   1 
ATOM   14667 C  CA  . ALA D  1 174 ? 14.312  -33.124 -6.254  1.00 23.29 ? 191  ALA D CA  1 
ATOM   14668 C  C   . ALA D  1 174 ? 14.316  -32.728 -4.777  1.00 23.56 ? 191  ALA D C   1 
ATOM   14669 O  O   . ALA D  1 174 ? 14.847  -33.464 -3.952  1.00 24.96 ? 191  ALA D O   1 
ATOM   14670 C  CB  . ALA D  1 174 ? 15.723  -33.296 -6.783  1.00 22.73 ? 191  ALA D CB  1 
ATOM   14671 N  N   . GLY D  1 175 ? 13.712  -31.587 -4.427  1.00 23.45 ? 192  GLY D N   1 
ATOM   14672 C  CA  . GLY D  1 175 ? 13.612  -31.182 -3.034  1.00 22.80 ? 192  GLY D CA  1 
ATOM   14673 C  C   . GLY D  1 175 ? 14.965  -30.787 -2.442  1.00 22.01 ? 192  GLY D C   1 
ATOM   14674 O  O   . GLY D  1 175 ? 15.194  -30.958 -1.246  1.00 20.82 ? 192  GLY D O   1 
ATOM   14675 N  N   . ILE D  1 176 ? 15.855  -30.237 -3.276  1.00 21.97 ? 193  ILE D N   1 
ATOM   14676 C  CA  . ILE D  1 176 ? 17.073  -29.623 -2.775  1.00 22.49 ? 193  ILE D CA  1 
ATOM   14677 C  C   . ILE D  1 176 ? 16.685  -28.295 -2.121  1.00 22.85 ? 193  ILE D C   1 
ATOM   14678 O  O   . ILE D  1 176 ? 15.941  -27.511 -2.706  1.00 22.40 ? 193  ILE D O   1 
ATOM   14679 C  CB  . ILE D  1 176 ? 18.111  -29.475 -3.905  1.00 23.19 ? 193  ILE D CB  1 
ATOM   14680 C  CG1 . ILE D  1 176 ? 18.566  -30.858 -4.405  1.00 23.90 ? 193  ILE D CG1 1 
ATOM   14681 C  CG2 . ILE D  1 176 ? 19.299  -28.615 -3.472  1.00 23.53 ? 193  ILE D CG2 1 
ATOM   14682 C  CD1 . ILE D  1 176 ? 19.418  -30.825 -5.658  1.00 23.92 ? 193  ILE D CD1 1 
ATOM   14683 N  N   . ARG D  1 177 ? 17.169  -28.071 -0.891  1.00 21.90 ? 194  ARG D N   1 
ATOM   14684 C  CA  . ARG D  1 177 ? 16.758  -26.921 -0.101  1.00 23.05 ? 194  ARG D CA  1 
ATOM   14685 C  C   . ARG D  1 177 ? 17.122  -25.627 -0.821  1.00 21.41 ? 194  ARG D C   1 
ATOM   14686 O  O   . ARG D  1 177 ? 18.282  -25.413 -1.163  1.00 20.32 ? 194  ARG D O   1 
ATOM   14687 C  CB  . ARG D  1 177 ? 17.403  -26.911 1.289   1.00 24.64 ? 194  ARG D CB  1 
ATOM   14688 C  CG  . ARG D  1 177 ? 16.786  -27.913 2.254   1.00 27.74 ? 194  ARG D CG  1 
ATOM   14689 C  CD  . ARG D  1 177 ? 17.453  -27.922 3.616   1.00 31.19 ? 194  ARG D CD  1 
ATOM   14690 N  NE  . ARG D  1 177 ? 17.405  -26.607 4.265   1.00 34.93 ? 194  ARG D NE  1 
ATOM   14691 C  CZ  . ARG D  1 177 ? 17.674  -26.385 5.547   1.00 41.73 ? 194  ARG D CZ  1 
ATOM   14692 N  NH1 . ARG D  1 177 ? 17.930  -27.396 6.362   1.00 42.66 ? 194  ARG D NH1 1 
ATOM   14693 N  NH2 . ARG D  1 177 ? 17.660  -25.150 6.017   1.00 44.20 ? 194  ARG D NH2 1 
ATOM   14694 N  N   . PRO D  1 178 ? 16.149  -24.717 -1.057  1.00 21.96 ? 195  PRO D N   1 
ATOM   14695 C  CA  . PRO D  1 178 ? 16.420  -23.481 -1.798  1.00 22.62 ? 195  PRO D CA  1 
ATOM   14696 C  C   . PRO D  1 178 ? 17.451  -22.571 -1.133  1.00 22.52 ? 195  PRO D C   1 
ATOM   14697 O  O   . PRO D  1 178 ? 18.224  -21.916 -1.829  1.00 22.33 ? 195  PRO D O   1 
ATOM   14698 C  CB  . PRO D  1 178 ? 15.047  -22.794 -1.963  1.00 22.30 ? 195  PRO D CB  1 
ATOM   14699 C  CG  . PRO D  1 178 ? 14.138  -23.482 -0.974  1.00 22.13 ? 195  PRO D CG  1 
ATOM   14700 C  CD  . PRO D  1 178 ? 14.743  -24.844 -0.656  1.00 21.95 ? 195  PRO D CD  1 
ATOM   14701 N  N   . ASP D  1 179 ? 17.514  -22.575 0.207   1.00 23.63 ? 196  ASP D N   1 
ATOM   14702 C  CA  . ASP D  1 179 ? 18.477  -21.740 0.914   1.00 24.67 ? 196  ASP D CA  1 
ATOM   14703 C  C   . ASP D  1 179 ? 19.905  -22.261 0.726   1.00 23.68 ? 196  ASP D C   1 
ATOM   14704 O  O   . ASP D  1 179 ? 20.858  -21.560 1.061   1.00 23.29 ? 196  ASP D O   1 
ATOM   14705 C  CB  . ASP D  1 179 ? 18.116  -21.562 2.381   1.00 27.21 ? 196  ASP D CB  1 
ATOM   14706 C  CG  . ASP D  1 179 ? 18.116  -22.820 3.239   1.00 30.11 ? 196  ASP D CG  1 
ATOM   14707 O  OD1 . ASP D  1 179 ? 18.223  -23.924 2.672   1.00 32.85 ? 196  ASP D OD1 1 
ATOM   14708 O  OD2 . ASP D  1 179 ? 18.003  -22.686 4.473   1.00 32.68 ? 196  ASP D OD2 1 
ATOM   14709 N  N   . ARG D  1 180 ? 20.058  -23.480 0.184   1.00 22.68 ? 197  ARG D N   1 
ATOM   14710 C  CA  . ARG D  1 180 ? 21.377  -24.061 -0.047  1.00 22.79 ? 197  ARG D CA  1 
ATOM   14711 C  C   . ARG D  1 180 ? 21.771  -24.026 -1.525  1.00 21.82 ? 197  ARG D C   1 
ATOM   14712 O  O   . ARG D  1 180 ? 22.745  -24.671 -1.910  1.00 21.56 ? 197  ARG D O   1 
ATOM   14713 C  CB  . ARG D  1 180 ? 21.374  -25.478 0.535   1.00 24.45 ? 197  ARG D CB  1 
ATOM   14714 C  CG  . ARG D  1 180 ? 21.140  -25.418 2.037   1.00 27.05 ? 197  ARG D CG  1 
ATOM   14715 C  CD  . ARG D  1 180 ? 21.466  -26.704 2.747   1.00 30.15 ? 197  ARG D CD  1 
ATOM   14716 N  NE  . ARG D  1 180 ? 21.213  -26.581 4.187   1.00 32.66 ? 197  ARG D NE  1 
ATOM   14717 C  CZ  . ARG D  1 180 ? 21.113  -27.621 5.017   1.00 36.61 ? 197  ARG D CZ  1 
ATOM   14718 N  NH1 . ARG D  1 180 ? 21.223  -28.859 4.555   1.00 34.44 ? 197  ARG D NH1 1 
ATOM   14719 N  NH2 . ARG D  1 180 ? 20.881  -27.419 6.307   1.00 38.51 ? 197  ARG D NH2 1 
ATOM   14720 N  N   . CYS D  1 181 ? 21.037  -23.248 -2.333  1.00 21.20 ? 198  CYS D N   1 
ATOM   14721 C  CA  . CYS D  1 181 ? 21.293  -23.109 -3.759  1.00 21.51 ? 198  CYS D CA  1 
ATOM   14722 C  C   . CYS D  1 181 ? 21.891  -21.734 -4.051  1.00 20.93 ? 198  CYS D C   1 
ATOM   14723 O  O   . CYS D  1 181 ? 21.432  -20.733 -3.495  1.00 20.84 ? 198  CYS D O   1 
ATOM   14724 C  CB  . CYS D  1 181 ? 20.011  -23.283 -4.564  1.00 22.17 ? 198  CYS D CB  1 
ATOM   14725 S  SG  . CYS D  1 181 ? 19.313  -24.954 -4.467  1.00 24.20 ? 198  CYS D SG  1 
ATOM   14726 N  N   . LEU D  1 182 ? 22.905  -21.696 -4.930  1.00 20.07 ? 199  LEU D N   1 
ATOM   14727 C  CA  . LEU D  1 182 ? 23.627  -20.465 -5.227  1.00 20.15 ? 199  LEU D CA  1 
ATOM   14728 C  C   . LEU D  1 182 ? 23.822  -20.313 -6.738  1.00 19.43 ? 199  LEU D C   1 
ATOM   14729 O  O   . LEU D  1 182 ? 24.697  -20.951 -7.321  1.00 18.35 ? 199  LEU D O   1 
ATOM   14730 C  CB  . LEU D  1 182 ? 24.959  -20.455 -4.482  1.00 21.04 ? 199  LEU D CB  1 
ATOM   14731 C  CG  . LEU D  1 182 ? 25.939  -19.335 -4.847  1.00 22.23 ? 199  LEU D CG  1 
ATOM   14732 C  CD1 . LEU D  1 182 ? 25.288  -17.981 -4.651  1.00 22.29 ? 199  LEU D CD1 1 
ATOM   14733 C  CD2 . LEU D  1 182 ? 27.226  -19.438 -4.047  1.00 22.12 ? 199  LEU D CD2 1 
ATOM   14734 N  N   . PRO D  1 183 ? 23.028  -19.450 -7.414  1.00 19.06 ? 200  PRO D N   1 
ATOM   14735 C  CA  . PRO D  1 183 ? 23.266  -19.113 -8.821  1.00 18.88 ? 200  PRO D CA  1 
ATOM   14736 C  C   . PRO D  1 183 ? 24.446  -18.151 -8.967  1.00 19.51 ? 200  PRO D C   1 
ATOM   14737 O  O   . PRO D  1 183 ? 24.624  -17.245 -8.148  1.00 18.45 ? 200  PRO D O   1 
ATOM   14738 C  CB  . PRO D  1 183 ? 21.925  -18.480 -9.287  1.00 19.18 ? 200  PRO D CB  1 
ATOM   14739 C  CG  . PRO D  1 183 ? 20.974  -18.645 -8.120  1.00 19.67 ? 200  PRO D CG  1 
ATOM   14740 C  CD  . PRO D  1 183 ? 21.831  -18.778 -6.877  1.00 19.14 ? 200  PRO D CD  1 
ATOM   14741 N  N   . VAL D  1 184 ? 25.270  -18.367 -10.003 1.00 19.68 ? 201  VAL D N   1 
ATOM   14742 C  CA  . VAL D  1 184 ? 26.477  -17.581 -10.211 1.00 20.31 ? 201  VAL D CA  1 
ATOM   14743 C  C   . VAL D  1 184 ? 26.579  -17.240 -11.693 1.00 22.16 ? 201  VAL D C   1 
ATOM   14744 O  O   . VAL D  1 184 ? 26.472  -18.117 -12.547 1.00 20.88 ? 201  VAL D O   1 
ATOM   14745 C  CB  . VAL D  1 184 ? 27.769  -18.279 -9.742  1.00 20.54 ? 201  VAL D CB  1 
ATOM   14746 C  CG1 . VAL D  1 184 ? 29.005  -17.442 -10.050 1.00 20.98 ? 201  VAL D CG1 1 
ATOM   14747 C  CG2 . VAL D  1 184 ? 27.732  -18.621 -8.259  1.00 20.71 ? 201  VAL D CG2 1 
ATOM   14748 N  N   . CYS D  1 185 ? 26.786  -15.948 -11.974 1.00 23.96 ? 202  CYS D N   1 
ATOM   14749 C  CA  . CYS D  1 185 ? 27.087  -15.469 -13.309 1.00 24.20 ? 202  CYS D CA  1 
ATOM   14750 C  C   . CYS D  1 185 ? 28.493  -14.875 -13.310 1.00 23.90 ? 202  CYS D C   1 
ATOM   14751 O  O   . CYS D  1 185 ? 28.789  -13.994 -12.507 1.00 23.02 ? 202  CYS D O   1 
ATOM   14752 C  CB  . CYS D  1 185 ? 26.057  -14.436 -13.748 1.00 28.56 ? 202  CYS D CB  1 
ATOM   14753 S  SG  . CYS D  1 185 ? 26.340  -13.824 -15.430 1.00 34.07 ? 202  CYS D SG  1 
ATOM   14754 N  N   . ILE D  1 186 ? 29.357  -15.386 -14.195 1.00 23.30 ? 203  ILE D N   1 
ATOM   14755 C  CA  . ILE D  1 186 ? 30.702  -14.866 -14.365 1.00 24.48 ? 203  ILE D CA  1 
ATOM   14756 C  C   . ILE D  1 186 ? 30.718  -13.976 -15.607 1.00 24.04 ? 203  ILE D C   1 
ATOM   14757 O  O   . ILE D  1 186 ? 30.338  -14.410 -16.689 1.00 24.85 ? 203  ILE D O   1 
ATOM   14758 C  CB  . ILE D  1 186 ? 31.724  -16.013 -14.436 1.00 27.33 ? 203  ILE D CB  1 
ATOM   14759 C  CG1 . ILE D  1 186 ? 31.735  -16.794 -13.118 1.00 28.67 ? 203  ILE D CG1 1 
ATOM   14760 C  CG2 . ILE D  1 186 ? 33.112  -15.483 -14.803 1.00 28.08 ? 203  ILE D CG2 1 
ATOM   14761 C  CD1 . ILE D  1 186 ? 32.612  -18.027 -13.109 1.00 31.53 ? 203  ILE D CD1 1 
ATOM   14762 N  N   . ASP D  1 187 ? 31.126  -12.718 -15.423 1.00 23.59 ? 204  ASP D N   1 
ATOM   14763 C  CA  . ASP D  1 187 ? 31.113  -11.727 -16.484 1.00 23.96 ? 204  ASP D CA  1 
ATOM   14764 C  C   . ASP D  1 187 ? 32.545  -11.359 -16.850 1.00 23.80 ? 204  ASP D C   1 
ATOM   14765 O  O   . ASP D  1 187 ? 33.220  -10.670 -16.091 1.00 24.42 ? 204  ASP D O   1 
ATOM   14766 C  CB  . ASP D  1 187 ? 30.368  -10.469 -16.077 1.00 25.82 ? 204  ASP D CB  1 
ATOM   14767 C  CG  . ASP D  1 187 ? 30.285  -9.390  -17.152 1.00 27.05 ? 204  ASP D CG  1 
ATOM   14768 O  OD1 . ASP D  1 187 ? 30.599  -9.690  -18.330 1.00 28.13 ? 204  ASP D OD1 1 
ATOM   14769 O  OD2 . ASP D  1 187 ? 29.894  -8.260  -16.809 1.00 28.04 ? 204  ASP D OD2 1 
ATOM   14770 N  N   . VAL D  1 188 ? 32.982  -11.814 -18.028 1.00 23.45 ? 205  VAL D N   1 
ATOM   14771 C  CA  . VAL D  1 188 ? 34.288  -11.466 -18.563 1.00 23.58 ? 205  VAL D CA  1 
ATOM   14772 C  C   . VAL D  1 188 ? 34.109  -10.647 -19.841 1.00 24.20 ? 205  VAL D C   1 
ATOM   14773 O  O   . VAL D  1 188 ? 35.051  -10.500 -20.619 1.00 23.94 ? 205  VAL D O   1 
ATOM   14774 C  CB  . VAL D  1 188 ? 35.114  -12.741 -18.808 1.00 24.22 ? 205  VAL D CB  1 
ATOM   14775 C  CG1 . VAL D  1 188 ? 35.323  -13.520 -17.512 1.00 23.85 ? 205  VAL D CG1 1 
ATOM   14776 C  CG2 . VAL D  1 188 ? 34.486  -13.627 -19.880 1.00 24.52 ? 205  VAL D CG2 1 
ATOM   14777 N  N   . GLY D  1 189 ? 32.903  -10.092 -20.027 1.00 23.43 ? 206  GLY D N   1 
ATOM   14778 C  CA  . GLY D  1 189 ? 32.549  -9.391  -21.251 1.00 24.16 ? 206  GLY D CA  1 
ATOM   14779 C  C   . GLY D  1 189 ? 31.615  -10.225 -22.122 1.00 24.30 ? 206  GLY D C   1 
ATOM   14780 O  O   . GLY D  1 189 ? 31.243  -11.341 -21.769 1.00 23.55 ? 206  GLY D O   1 
ATOM   14781 N  N   . THR D  1 190 ? 31.233  -9.647  -23.264 1.00 25.42 ? 207  THR D N   1 
ATOM   14782 C  CA  . THR D  1 190 ? 30.397  -10.314 -24.245 1.00 25.22 ? 207  THR D CA  1 
ATOM   14783 C  C   . THR D  1 190 ? 30.897  -9.927  -25.631 1.00 26.78 ? 207  THR D C   1 
ATOM   14784 O  O   . THR D  1 190 ? 31.415  -8.827  -25.815 1.00 27.35 ? 207  THR D O   1 
ATOM   14785 C  CB  . THR D  1 190 ? 28.931  -9.925  -24.045 1.00 24.08 ? 207  THR D CB  1 
ATOM   14786 O  OG1 . THR D  1 190 ? 28.212  -10.611 -25.066 1.00 22.86 ? 207  THR D OG1 1 
ATOM   14787 C  CG2 . THR D  1 190 ? 28.688  -8.431  -24.151 1.00 24.31 ? 207  THR D CG2 1 
ATOM   14788 N  N   . ASP D  1 191 ? 30.718  -10.837 -26.594 1.00 28.41 ? 208  ASP D N   1 
ATOM   14789 C  CA  . ASP D  1 191 ? 31.055  -10.577 -27.985 1.00 30.64 ? 208  ASP D CA  1 
ATOM   14790 C  C   . ASP D  1 191 ? 29.791  -10.237 -28.773 1.00 32.11 ? 208  ASP D C   1 
ATOM   14791 O  O   . ASP D  1 191 ? 29.837  -10.122 -29.995 1.00 35.14 ? 208  ASP D O   1 
ATOM   14792 C  CB  . ASP D  1 191 ? 31.810  -11.748 -28.593 1.00 31.28 ? 208  ASP D CB  1 
ATOM   14793 C  CG  . ASP D  1 191 ? 33.233  -11.948 -28.091 1.00 31.77 ? 208  ASP D CG  1 
ATOM   14794 O  OD1 . ASP D  1 191 ? 33.773  -11.030 -27.430 1.00 31.39 ? 208  ASP D OD1 1 
ATOM   14795 O  OD2 . ASP D  1 191 ? 33.790  -13.029 -28.352 1.00 33.84 ? 208  ASP D OD2 1 
ATOM   14796 N  N   . ASN D  1 192 ? 28.665  -10.076 -28.064 1.00 30.78 ? 209  ASN D N   1 
ATOM   14797 C  CA  . ASN D  1 192 ? 27.409  -9.667  -28.667 1.00 30.87 ? 209  ASN D CA  1 
ATOM   14798 C  C   . ASN D  1 192 ? 27.430  -8.151  -28.881 1.00 32.04 ? 209  ASN D C   1 
ATOM   14799 O  O   . ASN D  1 192 ? 27.304  -7.381  -27.927 1.00 29.43 ? 209  ASN D O   1 
ATOM   14800 C  CB  . ASN D  1 192 ? 26.242  -10.119 -27.798 1.00 31.04 ? 209  ASN D CB  1 
ATOM   14801 C  CG  . ASN D  1 192 ? 24.905  -9.938  -28.474 1.00 30.82 ? 209  ASN D CG  1 
ATOM   14802 O  OD1 . ASN D  1 192 ? 24.710  -8.970  -29.215 1.00 31.89 ? 209  ASN D OD1 1 
ATOM   14803 N  ND2 . ASN D  1 192 ? 23.977  -10.855 -28.242 1.00 29.65 ? 209  ASN D ND2 1 
ATOM   14804 N  N   . ILE D  1 193 ? 27.579  -7.736  -30.146 1.00 32.41 ? 210  ILE D N   1 
ATOM   14805 C  CA  . ILE D  1 193 ? 27.742  -6.331  -30.503 1.00 33.49 ? 210  ILE D CA  1 
ATOM   14806 C  C   . ILE D  1 193 ? 26.497  -5.531  -30.112 1.00 30.52 ? 210  ILE D C   1 
ATOM   14807 O  O   . ILE D  1 193 ? 26.612  -4.370  -29.722 1.00 30.28 ? 210  ILE D O   1 
ATOM   14808 C  CB  . ILE D  1 193 ? 28.079  -6.173  -32.003 1.00 36.23 ? 210  ILE D CB  1 
ATOM   14809 C  CG1 . ILE D  1 193 ? 28.556  -4.755  -32.344 1.00 39.41 ? 210  ILE D CG1 1 
ATOM   14810 C  CG2 . ILE D  1 193 ? 26.902  -6.583  -32.892 1.00 36.97 ? 210  ILE D CG2 1 
ATOM   14811 C  CD1 . ILE D  1 193 ? 29.916  -4.384  -31.776 1.00 41.14 ? 210  ILE D CD1 1 
ATOM   14812 N  N   . ALA D  1 194 ? 25.311  -6.143  -30.212 1.00 29.70 ? 211  ALA D N   1 
ATOM   14813 C  CA  . ALA D  1 194 ? 24.078  -5.460  -29.847 1.00 30.24 ? 211  ALA D CA  1 
ATOM   14814 C  C   . ALA D  1 194 ? 24.098  -5.075  -28.369 1.00 30.08 ? 211  ALA D C   1 
ATOM   14815 O  O   . ALA D  1 194 ? 23.628  -3.998  -28.005 1.00 29.73 ? 211  ALA D O   1 
ATOM   14816 C  CB  . ALA D  1 194 ? 22.873  -6.315  -30.182 1.00 30.27 ? 211  ALA D CB  1 
ATOM   14817 N  N   . LEU D  1 195 ? 24.662  -5.946  -27.521 1.00 28.98 ? 212  LEU D N   1 
ATOM   14818 C  CA  . LEU D  1 195 ? 24.708  -5.693  -26.089 1.00 28.51 ? 212  LEU D CA  1 
ATOM   14819 C  C   . LEU D  1 195 ? 25.751  -4.621  -25.790 1.00 27.41 ? 212  LEU D C   1 
ATOM   14820 O  O   . LEU D  1 195 ? 25.526  -3.750  -24.950 1.00 26.49 ? 212  LEU D O   1 
ATOM   14821 C  CB  . LEU D  1 195 ? 24.979  -6.988  -25.318 1.00 29.39 ? 212  LEU D CB  1 
ATOM   14822 C  CG  . LEU D  1 195 ? 23.933  -8.098  -25.488 1.00 30.32 ? 212  LEU D CG  1 
ATOM   14823 C  CD1 . LEU D  1 195 ? 24.264  -9.342  -24.663 1.00 30.08 ? 212  LEU D CD1 1 
ATOM   14824 C  CD2 . LEU D  1 195 ? 22.541  -7.601  -25.143 1.00 31.28 ? 212  LEU D CD2 1 
ATOM   14825 N  N   . LEU D  1 196 ? 26.884  -4.667  -26.500 1.00 26.74 ? 213  LEU D N   1 
ATOM   14826 C  CA  . LEU D  1 196 ? 27.958  -3.719  -26.260 1.00 28.37 ? 213  LEU D CA  1 
ATOM   14827 C  C   . LEU D  1 196 ? 27.520  -2.291  -26.595 1.00 29.30 ? 213  LEU D C   1 
ATOM   14828 O  O   . LEU D  1 196 ? 28.128  -1.345  -26.108 1.00 30.71 ? 213  LEU D O   1 
ATOM   14829 C  CB  . LEU D  1 196 ? 29.201  -4.133  -27.048 1.00 29.10 ? 213  LEU D CB  1 
ATOM   14830 C  CG  . LEU D  1 196 ? 29.908  -5.403  -26.562 1.00 29.89 ? 213  LEU D CG  1 
ATOM   14831 C  CD1 . LEU D  1 196 ? 30.992  -5.808  -27.546 1.00 30.89 ? 213  LEU D CD1 1 
ATOM   14832 C  CD2 . LEU D  1 196 ? 30.495  -5.216  -25.169 1.00 30.32 ? 213  LEU D CD2 1 
ATOM   14833 N  N   . LYS D  1 197 ? 26.474  -2.132  -27.415 1.00 31.26 ? 214  LYS D N   1 
ATOM   14834 C  CA  . LYS D  1 197 ? 25.997  -0.813  -27.809 1.00 33.86 ? 214  LYS D CA  1 
ATOM   14835 C  C   . LYS D  1 197 ? 24.695  -0.454  -27.090 1.00 33.72 ? 214  LYS D C   1 
ATOM   14836 O  O   . LYS D  1 197 ? 24.107  0.585   -27.379 1.00 34.31 ? 214  LYS D O   1 
ATOM   14837 C  CB  . LYS D  1 197 ? 25.782  -0.769  -29.327 1.00 35.87 ? 214  LYS D CB  1 
ATOM   14838 C  CG  . LYS D  1 197 ? 27.017  -1.046  -30.181 1.00 37.48 ? 214  LYS D CG  1 
ATOM   14839 C  CD  . LYS D  1 197 ? 28.250  -0.224  -29.828 1.00 40.48 ? 214  LYS D CD  1 
ATOM   14840 C  CE  . LYS D  1 197 ? 27.997  1.252   -29.829 1.00 44.88 ? 214  LYS D CE  1 
ATOM   14841 N  NZ  . LYS D  1 197 ? 29.222  1.995   -29.524 1.00 47.83 ? 214  LYS D NZ  1 
ATOM   14842 N  N   . ASP D  1 198 ? 24.261  -1.304  -26.149 1.00 32.86 ? 215  ASP D N   1 
ATOM   14843 C  CA  . ASP D  1 198 ? 22.965  -1.158  -25.502 1.00 32.40 ? 215  ASP D CA  1 
ATOM   14844 C  C   . ASP D  1 198 ? 23.144  -0.423  -24.176 1.00 31.24 ? 215  ASP D C   1 
ATOM   14845 O  O   . ASP D  1 198 ? 23.767  -0.951  -23.258 1.00 29.65 ? 215  ASP D O   1 
ATOM   14846 C  CB  . ASP D  1 198 ? 22.298  -2.513  -25.311 1.00 33.94 ? 215  ASP D CB  1 
ATOM   14847 C  CG  . ASP D  1 198 ? 20.921  -2.498  -24.664 1.00 36.60 ? 215  ASP D CG  1 
ATOM   14848 O  OD1 . ASP D  1 198 ? 20.410  -1.392  -24.388 1.00 37.70 ? 215  ASP D OD1 1 
ATOM   14849 O  OD2 . ASP D  1 198 ? 20.373  -3.598  -24.431 1.00 39.68 ? 215  ASP D OD2 1 
ATOM   14850 N  N   . PRO D  1 199 ? 22.580  0.797   -24.005 1.00 31.32 ? 216  PRO D N   1 
ATOM   14851 C  CA  . PRO D  1 199 ? 22.704  1.516   -22.734 1.00 30.37 ? 216  PRO D CA  1 
ATOM   14852 C  C   . PRO D  1 199 ? 22.009  0.840   -21.551 1.00 28.51 ? 216  PRO D C   1 
ATOM   14853 O  O   . PRO D  1 199 ? 22.259  1.213   -20.409 1.00 29.21 ? 216  PRO D O   1 
ATOM   14854 C  CB  . PRO D  1 199 ? 22.097  2.892   -23.057 1.00 31.38 ? 216  PRO D CB  1 
ATOM   14855 C  CG  . PRO D  1 199 ? 21.115  2.610   -24.168 1.00 32.07 ? 216  PRO D CG  1 
ATOM   14856 C  CD  . PRO D  1 199 ? 21.788  1.536   -25.004 1.00 31.88 ? 216  PRO D CD  1 
ATOM   14857 N  N   . PHE D  1 200 ? 21.162  -0.164  -21.825 1.00 26.97 ? 217  PHE D N   1 
ATOM   14858 C  CA  . PHE D  1 200 ? 20.430  -0.875  -20.787 1.00 28.08 ? 217  PHE D CA  1 
ATOM   14859 C  C   . PHE D  1 200 ? 21.078  -2.223  -20.459 1.00 27.87 ? 217  PHE D C   1 
ATOM   14860 O  O   . PHE D  1 200 ? 20.571  -2.952  -19.606 1.00 27.52 ? 217  PHE D O   1 
ATOM   14861 C  CB  . PHE D  1 200 ? 18.980  -1.032  -21.254 1.00 29.30 ? 217  PHE D CB  1 
ATOM   14862 C  CG  . PHE D  1 200 ? 18.260  0.294   -21.462 1.00 31.55 ? 217  PHE D CG  1 
ATOM   14863 C  CD1 . PHE D  1 200 ? 18.198  1.241   -20.444 1.00 32.77 ? 217  PHE D CD1 1 
ATOM   14864 C  CD2 . PHE D  1 200 ? 17.690  0.613   -22.692 1.00 34.68 ? 217  PHE D CD2 1 
ATOM   14865 C  CE1 . PHE D  1 200 ? 17.559  2.459   -20.641 1.00 33.94 ? 217  PHE D CE1 1 
ATOM   14866 C  CE2 . PHE D  1 200 ? 17.049  1.833   -22.884 1.00 35.67 ? 217  PHE D CE2 1 
ATOM   14867 C  CZ  . PHE D  1 200 ? 16.988  2.753   -21.860 1.00 34.45 ? 217  PHE D CZ  1 
ATOM   14868 N  N   . TYR D  1 201 ? 22.190  -2.560  -21.125 1.00 26.65 ? 218  TYR D N   1 
ATOM   14869 C  CA  . TYR D  1 201 ? 22.914  -3.788  -20.822 1.00 25.89 ? 218  TYR D CA  1 
ATOM   14870 C  C   . TYR D  1 201 ? 23.443  -3.715  -19.389 1.00 25.52 ? 218  TYR D C   1 
ATOM   14871 O  O   . TYR D  1 201 ? 23.840  -2.651  -18.933 1.00 25.95 ? 218  TYR D O   1 
ATOM   14872 C  CB  . TYR D  1 201 ? 24.048  -4.014  -21.828 1.00 24.84 ? 218  TYR D CB  1 
ATOM   14873 C  CG  . TYR D  1 201 ? 24.877  -5.260  -21.546 1.00 23.42 ? 218  TYR D CG  1 
ATOM   14874 C  CD1 . TYR D  1 201 ? 24.276  -6.508  -21.417 1.00 23.78 ? 218  TYR D CD1 1 
ATOM   14875 C  CD2 . TYR D  1 201 ? 26.256  -5.183  -21.373 1.00 23.98 ? 218  TYR D CD2 1 
ATOM   14876 C  CE1 . TYR D  1 201 ? 25.023  -7.644  -21.150 1.00 23.43 ? 218  TYR D CE1 1 
ATOM   14877 C  CE2 . TYR D  1 201 ? 27.012  -6.310  -21.087 1.00 23.89 ? 218  TYR D CE2 1 
ATOM   14878 C  CZ  . TYR D  1 201 ? 26.393  -7.544  -20.978 1.00 24.13 ? 218  TYR D CZ  1 
ATOM   14879 O  OH  . TYR D  1 201 ? 27.139  -8.657  -20.703 1.00 24.32 ? 218  TYR D OH  1 
ATOM   14880 N  N   . MET D  1 202 ? 23.462  -4.852  -18.684 1.00 26.40 ? 219  MET D N   1 
ATOM   14881 C  CA  . MET D  1 202 ? 23.709  -4.856  -17.251 1.00 27.05 ? 219  MET D CA  1 
ATOM   14882 C  C   . MET D  1 202 ? 25.080  -5.454  -16.920 1.00 27.16 ? 219  MET D C   1 
ATOM   14883 O  O   . MET D  1 202 ? 25.365  -5.724  -15.756 1.00 26.04 ? 219  MET D O   1 
ATOM   14884 C  CB  . MET D  1 202 ? 22.583  -5.611  -16.531 1.00 29.69 ? 219  MET D CB  1 
ATOM   14885 C  CG  . MET D  1 202 ? 21.218  -4.948  -16.684 1.00 31.50 ? 219  MET D CG  1 
ATOM   14886 S  SD  . MET D  1 202 ? 19.899  -5.705  -15.708 1.00 35.84 ? 219  MET D SD  1 
ATOM   14887 C  CE  . MET D  1 202 ? 19.590  -7.229  -16.613 1.00 37.99 ? 219  MET D CE  1 
ATOM   14888 N  N   . GLY D  1 203 ? 25.951  -5.605  -17.927 1.00 25.42 ? 220  GLY D N   1 
ATOM   14889 C  CA  . GLY D  1 203 ? 27.266  -6.198  -17.722 1.00 26.15 ? 220  GLY D CA  1 
ATOM   14890 C  C   . GLY D  1 203 ? 28.394  -5.247  -18.115 1.00 27.01 ? 220  GLY D C   1 
ATOM   14891 O  O   . GLY D  1 203 ? 28.155  -4.072  -18.395 1.00 27.84 ? 220  GLY D O   1 
ATOM   14892 N  N   . LEU D  1 204 ? 29.628  -5.774  -18.119 1.00 26.64 ? 221  LEU D N   1 
ATOM   14893 C  CA  . LEU D  1 204 ? 30.807  -5.009  -18.499 1.00 26.33 ? 221  LEU D CA  1 
ATOM   14894 C  C   . LEU D  1 204 ? 30.781  -4.733  -20.002 1.00 26.02 ? 221  LEU D C   1 
ATOM   14895 O  O   . LEU D  1 204 ? 30.453  -5.610  -20.804 1.00 25.99 ? 221  LEU D O   1 
ATOM   14896 C  CB  . LEU D  1 204 ? 32.081  -5.759  -18.109 1.00 27.63 ? 221  LEU D CB  1 
ATOM   14897 C  CG  . LEU D  1 204 ? 32.375  -5.927  -16.613 1.00 29.22 ? 221  LEU D CG  1 
ATOM   14898 C  CD1 . LEU D  1 204 ? 33.636  -6.767  -16.460 1.00 30.27 ? 221  LEU D CD1 1 
ATOM   14899 C  CD2 . LEU D  1 204 ? 32.541  -4.610  -15.867 1.00 29.25 ? 221  LEU D CD2 1 
ATOM   14900 N  N   . TYR D  1 205 ? 31.140  -3.502  -20.384 1.00 26.30 ? 222  TYR D N   1 
ATOM   14901 C  CA  . TYR D  1 205 ? 31.165  -3.120  -21.787 1.00 26.71 ? 222  TYR D CA  1 
ATOM   14902 C  C   . TYR D  1 205 ? 32.553  -3.415  -22.352 1.00 28.14 ? 222  TYR D C   1 
ATOM   14903 O  O   . TYR D  1 205 ? 33.359  -2.511  -22.562 1.00 28.05 ? 222  TYR D O   1 
ATOM   14904 C  CB  . TYR D  1 205 ? 30.775  -1.648  -21.951 1.00 26.66 ? 222  TYR D CB  1 
ATOM   14905 C  CG  . TYR D  1 205 ? 29.306  -1.330  -21.698 1.00 26.79 ? 222  TYR D CG  1 
ATOM   14906 C  CD1 . TYR D  1 205 ? 28.321  -1.713  -22.602 1.00 25.55 ? 222  TYR D CD1 1 
ATOM   14907 C  CD2 . TYR D  1 205 ? 28.911  -0.606  -20.576 1.00 27.22 ? 222  TYR D CD2 1 
ATOM   14908 C  CE1 . TYR D  1 205 ? 26.987  -1.407  -22.385 1.00 26.06 ? 222  TYR D CE1 1 
ATOM   14909 C  CE2 . TYR D  1 205 ? 27.580  -0.285  -20.356 1.00 27.58 ? 222  TYR D CE2 1 
ATOM   14910 C  CZ  . TYR D  1 205 ? 26.615  -0.689  -21.261 1.00 26.54 ? 222  TYR D CZ  1 
ATOM   14911 O  OH  . TYR D  1 205 ? 25.303  -0.368  -21.042 1.00 26.69 ? 222  TYR D OH  1 
ATOM   14912 N  N   . GLN D  1 206 ? 32.822  -4.702  -22.576 1.00 27.84 ? 223  GLN D N   1 
ATOM   14913 C  CA  . GLN D  1 206 ? 34.056  -5.142  -23.202 1.00 29.82 ? 223  GLN D CA  1 
ATOM   14914 C  C   . GLN D  1 206 ? 33.796  -6.483  -23.883 1.00 29.75 ? 223  GLN D C   1 
ATOM   14915 O  O   . GLN D  1 206 ? 32.890  -7.220  -23.498 1.00 27.58 ? 223  GLN D O   1 
ATOM   14916 C  CB  . GLN D  1 206 ? 35.206  -5.259  -22.198 1.00 29.90 ? 223  GLN D CB  1 
ATOM   14917 C  CG  . GLN D  1 206 ? 34.962  -6.290  -21.101 1.00 31.45 ? 223  GLN D CG  1 
ATOM   14918 C  CD  . GLN D  1 206 ? 36.170  -6.553  -20.231 1.00 32.24 ? 223  GLN D CD  1 
ATOM   14919 O  OE1 . GLN D  1 206 ? 36.640  -5.678  -19.492 1.00 33.09 ? 223  GLN D OE1 1 
ATOM   14920 N  NE2 . GLN D  1 206 ? 36.671  -7.779  -20.285 1.00 31.81 ? 223  GLN D NE2 1 
ATOM   14921 N  N   . LYS D  1 207 ? 34.598  -6.769  -24.912 1.00 29.47 ? 224  LYS D N   1 
ATOM   14922 C  CA  . LYS D  1 207 ? 34.643  -8.081  -25.533 1.00 29.75 ? 224  LYS D CA  1 
ATOM   14923 C  C   . LYS D  1 207 ? 35.114  -9.096  -24.491 1.00 26.71 ? 224  LYS D C   1 
ATOM   14924 O  O   . LYS D  1 207 ? 35.713  -8.720  -23.488 1.00 25.51 ? 224  LYS D O   1 
ATOM   14925 C  CB  . LYS D  1 207 ? 35.575  -7.973  -26.745 1.00 32.26 ? 224  LYS D CB  1 
ATOM   14926 C  CG  . LYS D  1 207 ? 35.038  -7.124  -27.896 1.00 35.77 ? 224  LYS D CG  1 
ATOM   14927 C  CD  . LYS D  1 207 ? 34.524  -7.926  -29.084 1.00 38.93 ? 224  LYS D CD  1 
ATOM   14928 C  CE  . LYS D  1 207 ? 35.655  -8.500  -29.887 1.00 41.69 ? 224  LYS D CE  1 
ATOM   14929 N  NZ  . LYS D  1 207 ? 35.210  -9.467  -30.896 1.00 43.21 ? 224  LYS D NZ  1 
ATOM   14930 N  N   . ARG D  1 208 ? 34.833  -10.377 -24.735 1.00 26.37 ? 225  ARG D N   1 
ATOM   14931 C  CA  . ARG D  1 208 ? 35.205  -11.429 -23.801 1.00 27.37 ? 225  ARG D CA  1 
ATOM   14932 C  C   . ARG D  1 208 ? 36.723  -11.496 -23.674 1.00 28.03 ? 225  ARG D C   1 
ATOM   14933 O  O   . ARG D  1 208 ? 37.432  -11.539 -24.679 1.00 28.99 ? 225  ARG D O   1 
ATOM   14934 C  CB  . ARG D  1 208 ? 34.659  -12.797 -24.228 1.00 26.10 ? 225  ARG D CB  1 
ATOM   14935 C  CG  . ARG D  1 208 ? 33.161  -12.934 -24.010 1.00 25.52 ? 225  ARG D CG  1 
ATOM   14936 C  CD  . ARG D  1 208 ? 32.597  -14.290 -24.427 1.00 24.27 ? 225  ARG D CD  1 
ATOM   14937 N  NE  . ARG D  1 208 ? 31.187  -14.390 -24.029 1.00 23.51 ? 225  ARG D NE  1 
ATOM   14938 C  CZ  . ARG D  1 208 ? 30.732  -14.485 -22.777 1.00 23.44 ? 225  ARG D CZ  1 
ATOM   14939 N  NH1 . ARG D  1 208 ? 31.551  -14.756 -21.775 1.00 23.07 ? 225  ARG D NH1 1 
ATOM   14940 N  NH2 . ARG D  1 208 ? 29.440  -14.342 -22.530 1.00 23.34 ? 225  ARG D NH2 1 
ATOM   14941 N  N   . ASP D  1 209 ? 37.202  -11.493 -22.424 1.00 29.29 ? 226  ASP D N   1 
ATOM   14942 C  CA  . ASP D  1 209 ? 38.599  -11.744 -22.117 1.00 30.38 ? 226  ASP D CA  1 
ATOM   14943 C  C   . ASP D  1 209 ? 38.885  -13.221 -22.367 1.00 32.36 ? 226  ASP D C   1 
ATOM   14944 O  O   . ASP D  1 209 ? 38.258  -14.073 -21.743 1.00 32.51 ? 226  ASP D O   1 
ATOM   14945 C  CB  . ASP D  1 209 ? 38.923  -11.376 -20.679 1.00 30.09 ? 226  ASP D CB  1 
ATOM   14946 C  CG  . ASP D  1 209 ? 40.399  -11.386 -20.310 1.00 29.99 ? 226  ASP D CG  1 
ATOM   14947 O  OD1 . ASP D  1 209 ? 41.104  -12.322 -20.734 1.00 31.06 ? 226  ASP D OD1 1 
ATOM   14948 O  OD2 . ASP D  1 209 ? 40.825  -10.475 -19.572 1.00 30.15 ? 226  ASP D OD2 1 
ATOM   14949 N  N   . ARG D  1 210 ? 39.828  -13.500 -23.278 1.00 33.45 ? 227  ARG D N   1 
ATOM   14950 C  CA  . ARG D  1 210 ? 40.187  -14.863 -23.639 1.00 35.91 ? 227  ARG D CA  1 
ATOM   14951 C  C   . ARG D  1 210 ? 41.667  -15.112 -23.339 1.00 36.22 ? 227  ARG D C   1 
ATOM   14952 O  O   . ARG D  1 210 ? 42.250  -16.062 -23.857 1.00 37.59 ? 227  ARG D O   1 
ATOM   14953 C  CB  . ARG D  1 210 ? 39.857  -15.128 -25.114 1.00 36.87 ? 227  ARG D CB  1 
ATOM   14954 C  CG  . ARG D  1 210 ? 38.372  -15.109 -25.446 1.00 39.27 ? 227  ARG D CG  1 
ATOM   14955 C  CD  . ARG D  1 210 ? 38.129  -15.287 -26.933 1.00 40.97 ? 227  ARG D CD  1 
ATOM   14956 N  NE  . ARG D  1 210 ? 36.745  -15.011 -27.335 1.00 41.27 ? 227  ARG D NE  1 
ATOM   14957 C  CZ  . ARG D  1 210 ? 35.680  -15.752 -27.037 1.00 42.45 ? 227  ARG D CZ  1 
ATOM   14958 N  NH1 . ARG D  1 210 ? 35.806  -16.843 -26.303 1.00 45.40 ? 227  ARG D NH1 1 
ATOM   14959 N  NH2 . ARG D  1 210 ? 34.484  -15.398 -27.477 1.00 40.62 ? 227  ARG D NH2 1 
ATOM   14960 N  N   . THR D  1 211 ? 42.258  -14.268 -22.484 1.00 34.12 ? 228  THR D N   1 
ATOM   14961 C  CA  . THR D  1 211 ? 43.646  -14.417 -22.084 1.00 33.96 ? 228  THR D CA  1 
ATOM   14962 C  C   . THR D  1 211 ? 43.706  -15.417 -20.934 1.00 33.61 ? 228  THR D C   1 
ATOM   14963 O  O   . THR D  1 211 ? 42.692  -16.003 -20.559 1.00 33.24 ? 228  THR D O   1 
ATOM   14964 C  CB  . THR D  1 211 ? 44.248  -13.063 -21.691 1.00 34.54 ? 228  THR D CB  1 
ATOM   14965 O  OG1 . THR D  1 211 ? 43.638  -12.645 -20.470 1.00 32.54 ? 228  THR D OG1 1 
ATOM   14966 C  CG2 . THR D  1 211 ? 44.069  -12.007 -22.770 1.00 34.37 ? 228  THR D CG2 1 
ATOM   14967 N  N   . GLN D  1 212 ? 44.909  -15.587 -20.381 1.00 31.44 ? 229  GLN D N   1 
ATOM   14968 C  CA  . GLN D  1 212 ? 45.123  -16.405 -19.200 1.00 32.35 ? 229  GLN D CA  1 
ATOM   14969 C  C   . GLN D  1 212 ? 44.290  -15.886 -18.024 1.00 30.83 ? 229  GLN D C   1 
ATOM   14970 O  O   . GLN D  1 212 ? 43.971  -16.648 -17.117 1.00 30.09 ? 229  GLN D O   1 
ATOM   14971 C  CB  . GLN D  1 212 ? 46.626  -16.399 -18.913 1.00 34.09 ? 229  GLN D CB  1 
ATOM   14972 C  CG  . GLN D  1 212 ? 47.060  -17.247 -17.722 1.00 36.10 ? 229  GLN D CG  1 
ATOM   14973 C  CD  . GLN D  1 212 ? 46.672  -18.703 -17.853 1.00 38.45 ? 229  GLN D CD  1 
ATOM   14974 O  OE1 . GLN D  1 212 ? 46.735  -19.289 -18.940 1.00 41.07 ? 229  GLN D OE1 1 
ATOM   14975 N  NE2 . GLN D  1 212 ? 46.256  -19.299 -16.743 1.00 38.22 ? 229  GLN D NE2 1 
ATOM   14976 N  N   . GLN D  1 213 ? 43.944  -14.593 -18.036 1.00 29.55 ? 230  GLN D N   1 
ATOM   14977 C  CA  . GLN D  1 213 ? 43.153  -13.996 -16.970 1.00 30.10 ? 230  GLN D CA  1 
ATOM   14978 C  C   . GLN D  1 213 ? 41.801  -14.693 -16.817 1.00 28.41 ? 230  GLN D C   1 
ATOM   14979 O  O   . GLN D  1 213 ? 41.265  -14.744 -15.709 1.00 25.94 ? 230  GLN D O   1 
ATOM   14980 C  CB  . GLN D  1 213 ? 42.949  -12.499 -17.201 1.00 31.76 ? 230  GLN D CB  1 
ATOM   14981 C  CG  . GLN D  1 213 ? 44.207  -11.666 -16.983 1.00 34.03 ? 230  GLN D CG  1 
ATOM   14982 C  CD  . GLN D  1 213 ? 43.947  -10.175 -16.996 1.00 36.28 ? 230  GLN D CD  1 
ATOM   14983 O  OE1 . GLN D  1 213 ? 42.886  -9.700  -17.417 1.00 39.16 ? 230  GLN D OE1 1 
ATOM   14984 N  NE2 . GLN D  1 213 ? 44.928  -9.416  -16.534 1.00 37.78 ? 230  GLN D NE2 1 
ATOM   14985 N  N   . TYR D  1 214 ? 41.249  -15.209 -17.926 1.00 26.43 ? 231  TYR D N   1 
ATOM   14986 C  CA  . TYR D  1 214 ? 39.976  -15.913 -17.898 1.00 26.33 ? 231  TYR D CA  1 
ATOM   14987 C  C   . TYR D  1 214 ? 40.117  -17.198 -17.079 1.00 26.89 ? 231  TYR D C   1 
ATOM   14988 O  O   . TYR D  1 214 ? 39.365  -17.418 -16.131 1.00 23.67 ? 231  TYR D O   1 
ATOM   14989 C  CB  . TYR D  1 214 ? 39.500  -16.174 -19.331 1.00 25.89 ? 231  TYR D CB  1 
ATOM   14990 C  CG  . TYR D  1 214 ? 38.240  -17.020 -19.419 1.00 25.62 ? 231  TYR D CG  1 
ATOM   14991 C  CD1 . TYR D  1 214 ? 36.989  -16.466 -19.190 1.00 24.97 ? 231  TYR D CD1 1 
ATOM   14992 C  CD2 . TYR D  1 214 ? 38.302  -18.377 -19.718 1.00 25.97 ? 231  TYR D CD2 1 
ATOM   14993 C  CE1 . TYR D  1 214 ? 35.838  -17.234 -19.243 1.00 25.13 ? 231  TYR D CE1 1 
ATOM   14994 C  CE2 . TYR D  1 214 ? 37.156  -19.154 -19.783 1.00 25.99 ? 231  TYR D CE2 1 
ATOM   14995 C  CZ  . TYR D  1 214 ? 35.921  -18.581 -19.546 1.00 25.23 ? 231  TYR D CZ  1 
ATOM   14996 O  OH  . TYR D  1 214 ? 34.792  -19.342 -19.605 1.00 25.54 ? 231  TYR D OH  1 
ATOM   14997 N  N   . ASP D  1 215 ? 41.099  -18.032 -17.452 1.00 28.29 ? 232  ASP D N   1 
ATOM   14998 C  CA  . ASP D  1 215 ? 41.384  -19.283 -16.760 1.00 29.02 ? 232  ASP D CA  1 
ATOM   14999 C  C   . ASP D  1 215 ? 41.638  -19.036 -15.276 1.00 29.24 ? 232  ASP D C   1 
ATOM   15000 O  O   . ASP D  1 215 ? 41.167  -19.801 -14.432 1.00 27.89 ? 232  ASP D O   1 
ATOM   15001 C  CB  . ASP D  1 215 ? 42.568  -20.000 -17.395 1.00 31.40 ? 232  ASP D CB  1 
ATOM   15002 C  CG  . ASP D  1 215 ? 42.307  -20.591 -18.775 1.00 33.49 ? 232  ASP D CG  1 
ATOM   15003 O  OD1 . ASP D  1 215 ? 41.548  -19.970 -19.545 1.00 35.24 ? 232  ASP D OD1 1 
ATOM   15004 O  OD2 . ASP D  1 215 ? 42.885  -21.654 -19.081 1.00 34.78 ? 232  ASP D OD2 1 
ATOM   15005 N  N   . ASP D  1 216 ? 42.404  -17.979 -14.969 1.00 28.14 ? 233  ASP D N   1 
ATOM   15006 C  CA  . ASP D  1 216 ? 42.755  -17.650 -13.596 1.00 28.47 ? 233  ASP D CA  1 
ATOM   15007 C  C   . ASP D  1 216 ? 41.507  -17.292 -12.788 1.00 26.24 ? 233  ASP D C   1 
ATOM   15008 O  O   . ASP D  1 216 ? 41.410  -17.669 -11.624 1.00 25.41 ? 233  ASP D O   1 
ATOM   15009 C  CB  . ASP D  1 216 ? 43.800  -16.546 -13.535 1.00 30.99 ? 233  ASP D CB  1 
ATOM   15010 C  CG  . ASP D  1 216 ? 45.189  -16.923 -14.038 1.00 33.96 ? 233  ASP D CG  1 
ATOM   15011 O  OD1 . ASP D  1 216 ? 45.388  -18.102 -14.396 1.00 34.30 ? 233  ASP D OD1 1 
ATOM   15012 O  OD2 . ASP D  1 216 ? 46.064  -16.034 -14.065 1.00 38.15 ? 233  ASP D OD2 1 
ATOM   15013 N  N   . LEU D  1 217 ? 40.570  -16.550 -13.393 1.00 25.30 ? 234  LEU D N   1 
ATOM   15014 C  CA  . LEU D  1 217 ? 39.357  -16.131 -12.700 1.00 24.40 ? 234  LEU D CA  1 
ATOM   15015 C  C   . LEU D  1 217 ? 38.489  -17.340 -12.355 1.00 24.76 ? 234  LEU D C   1 
ATOM   15016 O  O   . LEU D  1 217 ? 37.910  -17.399 -11.271 1.00 23.92 ? 234  LEU D O   1 
ATOM   15017 C  CB  . LEU D  1 217 ? 38.559  -15.143 -13.543 1.00 23.86 ? 234  LEU D CB  1 
ATOM   15018 C  CG  . LEU D  1 217 ? 37.331  -14.535 -12.854 1.00 22.76 ? 234  LEU D CG  1 
ATOM   15019 C  CD1 . LEU D  1 217 ? 37.754  -13.482 -11.838 1.00 22.67 ? 234  LEU D CD1 1 
ATOM   15020 C  CD2 . LEU D  1 217 ? 36.384  -13.963 -13.885 1.00 22.72 ? 234  LEU D CD2 1 
ATOM   15021 N  N   . ILE D  1 218 ? 38.367  -18.286 -13.295 1.00 25.08 ? 235  ILE D N   1 
ATOM   15022 C  CA  . ILE D  1 218 ? 37.558  -19.472 -13.060 1.00 26.04 ? 235  ILE D CA  1 
ATOM   15023 C  C   . ILE D  1 218 ? 38.190  -20.284 -11.927 1.00 25.14 ? 235  ILE D C   1 
ATOM   15024 O  O   . ILE D  1 218 ? 37.480  -20.767 -11.051 1.00 25.64 ? 235  ILE D O   1 
ATOM   15025 C  CB  . ILE D  1 218 ? 37.369  -20.314 -14.341 1.00 26.20 ? 235  ILE D CB  1 
ATOM   15026 C  CG1 . ILE D  1 218 ? 36.794  -19.505 -15.517 1.00 27.89 ? 235  ILE D CG1 1 
ATOM   15027 C  CG2 . ILE D  1 218 ? 36.514  -21.549 -14.054 1.00 26.50 ? 235  ILE D CG2 1 
ATOM   15028 C  CD1 . ILE D  1 218 ? 35.384  -18.977 -15.310 1.00 28.54 ? 235  ILE D CD1 1 
ATOM   15029 N  N   . ASP D  1 219 ? 39.523  -20.436 -11.950 1.00 25.04 ? 236  ASP D N   1 
ATOM   15030 C  CA  . ASP D  1 219 ? 40.257  -21.109 -10.883 1.00 25.18 ? 236  ASP D CA  1 
ATOM   15031 C  C   . ASP D  1 219 ? 40.001  -20.440 -9.530  1.00 24.00 ? 236  ASP D C   1 
ATOM   15032 O  O   . ASP D  1 219 ? 39.772  -21.115 -8.525  1.00 22.22 ? 236  ASP D O   1 
ATOM   15033 C  CB  . ASP D  1 219 ? 41.758  -21.094 -11.136 1.00 27.75 ? 236  ASP D CB  1 
ATOM   15034 C  CG  . ASP D  1 219 ? 42.316  -22.171 -12.057 1.00 31.19 ? 236  ASP D CG  1 
ATOM   15035 O  OD1 . ASP D  1 219 ? 41.554  -23.084 -12.439 1.00 33.70 ? 236  ASP D OD1 1 
ATOM   15036 O  OD2 . ASP D  1 219 ? 43.520  -22.082 -12.394 1.00 33.26 ? 236  ASP D OD2 1 
ATOM   15037 N  N   . GLU D  1 220 ? 40.075  -19.105 -9.509  1.00 23.32 ? 237  GLU D N   1 
ATOM   15038 C  CA  . GLU D  1 220 ? 39.870  -18.338 -8.290  1.00 24.15 ? 237  GLU D CA  1 
ATOM   15039 C  C   . GLU D  1 220 ? 38.454  -18.570 -7.755  1.00 23.61 ? 237  GLU D C   1 
ATOM   15040 O  O   . GLU D  1 220 ? 38.262  -18.700 -6.548  1.00 23.38 ? 237  GLU D O   1 
ATOM   15041 C  CB  . GLU D  1 220 ? 40.109  -16.851 -8.553  1.00 24.97 ? 237  GLU D CB  1 
ATOM   15042 C  CG  . GLU D  1 220 ? 40.262  -16.032 -7.274  1.00 25.70 ? 237  GLU D CG  1 
ATOM   15043 C  CD  . GLU D  1 220 ? 40.357  -14.528 -7.460  1.00 26.06 ? 237  GLU D CD  1 
ATOM   15044 O  OE1 . GLU D  1 220 ? 40.499  -14.044 -8.603  1.00 26.17 ? 237  GLU D OE1 1 
ATOM   15045 O  OE2 . GLU D  1 220 ? 40.269  -13.832 -6.429  1.00 26.21 ? 237  GLU D OE2 1 
ATOM   15046 N  N   . PHE D  1 221 ? 37.479  -18.642 -8.668  1.00 23.35 ? 238  PHE D N   1 
ATOM   15047 C  CA  . PHE D  1 221 ? 36.087  -18.898 -8.319  1.00 23.21 ? 238  PHE D CA  1 
ATOM   15048 C  C   . PHE D  1 221 ? 35.920  -20.269 -7.659  1.00 24.08 ? 238  PHE D C   1 
ATOM   15049 O  O   . PHE D  1 221 ? 35.221  -20.388 -6.650  1.00 23.70 ? 238  PHE D O   1 
ATOM   15050 C  CB  . PHE D  1 221 ? 35.231  -18.760 -9.580  1.00 23.44 ? 238  PHE D CB  1 
ATOM   15051 C  CG  . PHE D  1 221 ? 33.892  -19.478 -9.502  1.00 23.96 ? 238  PHE D CG  1 
ATOM   15052 C  CD1 . PHE D  1 221 ? 32.856  -18.970 -8.730  1.00 24.79 ? 238  PHE D CD1 1 
ATOM   15053 C  CD2 . PHE D  1 221 ? 33.674  -20.654 -10.212 1.00 24.48 ? 238  PHE D CD2 1 
ATOM   15054 C  CE1 . PHE D  1 221 ? 31.637  -19.628 -8.666  1.00 24.79 ? 238  PHE D CE1 1 
ATOM   15055 C  CE2 . PHE D  1 221 ? 32.454  -21.307 -10.141 1.00 25.12 ? 238  PHE D CE2 1 
ATOM   15056 C  CZ  . PHE D  1 221 ? 31.443  -20.797 -9.364  1.00 24.95 ? 238  PHE D CZ  1 
ATOM   15057 N  N   . MET D  1 222 ? 36.523  -21.306 -8.255  1.00 23.42 ? 239  MET D N   1 
ATOM   15058 C  CA  . MET D  1 222 ? 36.371  -22.670 -7.764  1.00 23.85 ? 239  MET D CA  1 
ATOM   15059 C  C   . MET D  1 222 ? 36.947  -22.764 -6.350  1.00 23.41 ? 239  MET D C   1 
ATOM   15060 O  O   . MET D  1 222 ? 36.332  -23.350 -5.463  1.00 22.93 ? 239  MET D O   1 
ATOM   15061 C  CB  . MET D  1 222 ? 37.050  -23.683 -8.697  1.00 24.01 ? 239  MET D CB  1 
ATOM   15062 C  CG  . MET D  1 222 ? 36.455  -23.747 -10.101 1.00 24.55 ? 239  MET D CG  1 
ATOM   15063 S  SD  . MET D  1 222 ? 34.754  -24.347 -10.169 1.00 24.11 ? 239  MET D SD  1 
ATOM   15064 C  CE  . MET D  1 222 ? 34.933  -26.116 -9.907  1.00 24.82 ? 239  MET D CE  1 
ATOM   15065 N  N   . LYS D  1 223 ? 38.101  -22.127 -6.143  1.00 24.02 ? 240  LYS D N   1 
ATOM   15066 C  CA  . LYS D  1 223 ? 38.781  -22.119 -4.860  1.00 25.10 ? 240  LYS D CA  1 
ATOM   15067 C  C   . LYS D  1 223 ? 37.967  -21.347 -3.818  1.00 24.31 ? 240  LYS D C   1 
ATOM   15068 O  O   . LYS D  1 223 ? 37.801  -21.829 -2.699  1.00 23.06 ? 240  LYS D O   1 
ATOM   15069 C  CB  . LYS D  1 223 ? 40.193  -21.557 -5.049  1.00 28.29 ? 240  LYS D CB  1 
ATOM   15070 C  CG  . LYS D  1 223 ? 41.035  -21.457 -3.782  1.00 30.58 ? 240  LYS D CG  1 
ATOM   15071 C  CD  . LYS D  1 223 ? 42.464  -20.985 -4.030  1.00 32.37 ? 240  LYS D CD  1 
ATOM   15072 C  CE  . LYS D  1 223 ? 43.046  -20.278 -2.845  1.00 34.27 ? 240  LYS D CE  1 
ATOM   15073 N  NZ  . LYS D  1 223 ? 43.017  -21.105 -1.638  1.00 35.51 ? 240  LYS D NZ  1 
ATOM   15074 N  N   . ALA D  1 224 ? 37.447  -20.167 -4.190  1.00 23.09 ? 241  ALA D N   1 
ATOM   15075 C  CA  . ALA D  1 224 ? 36.705  -19.325 -3.261  1.00 21.85 ? 241  ALA D CA  1 
ATOM   15076 C  C   . ALA D  1 224 ? 35.438  -20.027 -2.778  1.00 21.29 ? 241  ALA D C   1 
ATOM   15077 O  O   . ALA D  1 224 ? 35.127  -19.980 -1.593  1.00 20.85 ? 241  ALA D O   1 
ATOM   15078 C  CB  . ALA D  1 224 ? 36.378  -17.990 -3.896  1.00 22.52 ? 241  ALA D CB  1 
ATOM   15079 N  N   . ILE D  1 225 ? 34.707  -20.661 -3.701  1.00 21.43 ? 242  ILE D N   1 
ATOM   15080 C  CA  . ILE D  1 225 ? 33.474  -21.358 -3.361  1.00 22.15 ? 242  ILE D CA  1 
ATOM   15081 C  C   . ILE D  1 225 ? 33.759  -22.490 -2.375  1.00 22.00 ? 242  ILE D C   1 
ATOM   15082 O  O   . ILE D  1 225 ? 33.028  -22.650 -1.401  1.00 20.31 ? 242  ILE D O   1 
ATOM   15083 C  CB  . ILE D  1 225 ? 32.769  -21.891 -4.624  1.00 22.52 ? 242  ILE D CB  1 
ATOM   15084 C  CG1 . ILE D  1 225 ? 32.116  -20.766 -5.421  1.00 23.05 ? 242  ILE D CG1 1 
ATOM   15085 C  CG2 . ILE D  1 225 ? 31.754  -22.983 -4.274  1.00 22.93 ? 242  ILE D CG2 1 
ATOM   15086 C  CD1 . ILE D  1 225 ? 30.901  -20.143 -4.753  1.00 23.20 ? 242  ILE D CD1 1 
ATOM   15087 N  N   . THR D  1 226 ? 34.784  -23.304 -2.663  1.00 22.10 ? 243  THR D N   1 
ATOM   15088 C  CA  . THR D  1 226 ? 35.058  -24.481 -1.852  1.00 22.38 ? 243  THR D CA  1 
ATOM   15089 C  C   . THR D  1 226 ? 35.757  -24.090 -0.546  1.00 23.12 ? 243  THR D C   1 
ATOM   15090 O  O   . THR D  1 226 ? 35.579  -24.768 0.462   1.00 23.21 ? 243  THR D O   1 
ATOM   15091 C  CB  . THR D  1 226 ? 35.841  -25.529 -2.646  1.00 22.92 ? 243  THR D CB  1 
ATOM   15092 O  OG1 . THR D  1 226 ? 36.992  -24.938 -3.242  1.00 22.77 ? 243  THR D OG1 1 
ATOM   15093 C  CG2 . THR D  1 226 ? 35.001  -26.142 -3.750  1.00 23.40 ? 243  THR D CG2 1 
ATOM   15094 N  N   . ASP D  1 227 ? 36.529  -22.997 -0.549  1.00 24.09 ? 244  ASP D N   1 
ATOM   15095 C  CA  . ASP D  1 227 ? 37.106  -22.464 0.680   1.00 24.49 ? 244  ASP D CA  1 
ATOM   15096 C  C   . ASP D  1 227 ? 35.997  -22.130 1.678   1.00 24.94 ? 244  ASP D C   1 
ATOM   15097 O  O   . ASP D  1 227 ? 36.084  -22.493 2.851   1.00 23.83 ? 244  ASP D O   1 
ATOM   15098 C  CB  . ASP D  1 227 ? 38.014  -21.272 0.409   1.00 25.03 ? 244  ASP D CB  1 
ATOM   15099 C  CG  . ASP D  1 227 ? 39.418  -21.601 -0.078  1.00 26.67 ? 244  ASP D CG  1 
ATOM   15100 O  OD1 . ASP D  1 227 ? 39.802  -22.791 -0.018  1.00 27.02 ? 244  ASP D OD1 1 
ATOM   15101 O  OD2 . ASP D  1 227 ? 40.119  -20.667 -0.524  1.00 30.02 ? 244  ASP D OD2 1 
ATOM   15102 N  N   . ARG D  1 228 ? 34.940  -21.451 1.216   1.00 23.22 ? 245  ARG D N   1 
ATOM   15103 C  CA  . ARG D  1 228 ? 33.889  -21.024 2.126   1.00 23.15 ? 245  ARG D CA  1 
ATOM   15104 C  C   . ARG D  1 228 ? 32.987  -22.204 2.490   1.00 22.41 ? 245  ARG D C   1 
ATOM   15105 O  O   . ARG D  1 228 ? 32.670  -22.395 3.661   1.00 21.81 ? 245  ARG D O   1 
ATOM   15106 C  CB  . ARG D  1 228 ? 33.062  -19.848 1.589   1.00 23.28 ? 245  ARG D CB  1 
ATOM   15107 C  CG  . ARG D  1 228 ? 31.969  -19.440 2.568   1.00 22.88 ? 245  ARG D CG  1 
ATOM   15108 C  CD  . ARG D  1 228 ? 31.168  -18.196 2.205   1.00 23.01 ? 245  ARG D CD  1 
ATOM   15109 N  NE  . ARG D  1 228 ? 30.175  -17.938 3.259   1.00 22.66 ? 245  ARG D NE  1 
ATOM   15110 C  CZ  . ARG D  1 228 ? 29.206  -17.027 3.239   1.00 23.08 ? 245  ARG D CZ  1 
ATOM   15111 N  NH1 . ARG D  1 228 ? 29.086  -16.192 2.224   1.00 23.17 ? 245  ARG D NH1 1 
ATOM   15112 N  NH2 . ARG D  1 228 ? 28.346  -16.962 4.245   1.00 23.44 ? 245  ARG D NH2 1 
ATOM   15113 N  N   . TYR D  1 229 ? 32.558  -22.986 1.495   1.00 21.08 ? 246  TYR D N   1 
ATOM   15114 C  CA  . TYR D  1 229 ? 31.448  -23.907 1.697   1.00 21.31 ? 246  TYR D CA  1 
ATOM   15115 C  C   . TYR D  1 229 ? 31.897  -25.364 1.817   1.00 21.21 ? 246  TYR D C   1 
ATOM   15116 O  O   . TYR D  1 229 ? 31.109  -26.198 2.250   1.00 21.67 ? 246  TYR D O   1 
ATOM   15117 C  CB  . TYR D  1 229 ? 30.456  -23.684 0.555   1.00 20.54 ? 246  TYR D CB  1 
ATOM   15118 C  CG  . TYR D  1 229 ? 29.722  -22.352 0.611   1.00 20.34 ? 246  TYR D CG  1 
ATOM   15119 C  CD1 . TYR D  1 229 ? 28.970  -21.990 1.721   1.00 20.44 ? 246  TYR D CD1 1 
ATOM   15120 C  CD2 . TYR D  1 229 ? 29.785  -21.452 -0.450  1.00 20.95 ? 246  TYR D CD2 1 
ATOM   15121 C  CE1 . TYR D  1 229 ? 28.295  -20.779 1.773   1.00 20.13 ? 246  TYR D CE1 1 
ATOM   15122 C  CE2 . TYR D  1 229 ? 29.115  -20.239 -0.410  1.00 20.47 ? 246  TYR D CE2 1 
ATOM   15123 C  CZ  . TYR D  1 229 ? 28.374  -19.901 0.708   1.00 20.23 ? 246  TYR D CZ  1 
ATOM   15124 O  OH  . TYR D  1 229 ? 27.699  -18.716 0.751   1.00 20.74 ? 246  TYR D OH  1 
ATOM   15125 N  N   . GLY D  1 230 ? 33.150  -25.674 1.459   1.00 22.45 ? 247  GLY D N   1 
ATOM   15126 C  CA  . GLY D  1 230 ? 33.663  -27.032 1.572   1.00 22.99 ? 247  GLY D CA  1 
ATOM   15127 C  C   . GLY D  1 230 ? 34.000  -27.635 0.208   1.00 24.20 ? 247  GLY D C   1 
ATOM   15128 O  O   . GLY D  1 230 ? 33.402  -27.276 -0.804  1.00 22.29 ? 247  GLY D O   1 
ATOM   15129 N  N   . ARG D  1 231 ? 34.946  -28.585 0.202   1.00 25.24 ? 248  ARG D N   1 
ATOM   15130 C  CA  . ARG D  1 231 ? 35.424  -29.204 -1.028  1.00 28.20 ? 248  ARG D CA  1 
ATOM   15131 C  C   . ARG D  1 231 ? 34.351  -30.053 -1.710  1.00 26.19 ? 248  ARG D C   1 
ATOM   15132 O  O   . ARG D  1 231 ? 34.461  -30.317 -2.906  1.00 26.86 ? 248  ARG D O   1 
ATOM   15133 C  CB  . ARG D  1 231 ? 36.651  -30.093 -0.786  1.00 33.46 ? 248  ARG D CB  1 
ATOM   15134 C  CG  . ARG D  1 231 ? 37.918  -29.356 -0.379  1.00 38.40 ? 248  ARG D CG  1 
ATOM   15135 C  CD  . ARG D  1 231 ? 38.501  -28.491 -1.480  1.00 43.76 ? 248  ARG D CD  1 
ATOM   15136 N  NE  . ARG D  1 231 ? 39.188  -29.279 -2.512  1.00 48.54 ? 248  ARG D NE  1 
ATOM   15137 C  CZ  . ARG D  1 231 ? 40.379  -29.011 -3.053  1.00 51.05 ? 248  ARG D CZ  1 
ATOM   15138 N  NH1 . ARG D  1 231 ? 41.107  -27.987 -2.634  1.00 52.05 ? 248  ARG D NH1 1 
ATOM   15139 N  NH2 . ARG D  1 231 ? 40.846  -29.777 -4.027  1.00 52.98 ? 248  ARG D NH2 1 
ATOM   15140 N  N   . ASN D  1 232 ? 33.313  -30.476 -0.976  1.00 24.57 ? 249  ASN D N   1 
ATOM   15141 C  CA  . ASN D  1 232 ? 32.292  -31.335 -1.555  1.00 24.82 ? 249  ASN D CA  1 
ATOM   15142 C  C   . ASN D  1 232 ? 31.137  -30.522 -2.152  1.00 22.88 ? 249  ASN D C   1 
ATOM   15143 O  O   . ASN D  1 232 ? 30.165  -31.111 -2.620  1.00 23.23 ? 249  ASN D O   1 
ATOM   15144 C  CB  . ASN D  1 232 ? 31.821  -32.398 -0.565  1.00 25.94 ? 249  ASN D CB  1 
ATOM   15145 C  CG  . ASN D  1 232 ? 31.025  -31.859 0.600   1.00 28.57 ? 249  ASN D CG  1 
ATOM   15146 O  OD1 . ASN D  1 232 ? 30.493  -30.746 0.546   1.00 31.17 ? 249  ASN D OD1 1 
ATOM   15147 N  ND2 . ASN D  1 232 ? 30.902  -32.651 1.657   1.00 29.13 ? 249  ASN D ND2 1 
ATOM   15148 N  N   . THR D  1 233 ? 31.239  -29.185 -2.158  1.00 21.02 ? 250  THR D N   1 
ATOM   15149 C  CA  . THR D  1 233 ? 30.184  -28.355 -2.718  1.00 20.12 ? 250  THR D CA  1 
ATOM   15150 C  C   . THR D  1 233 ? 30.018  -28.687 -4.200  1.00 19.62 ? 250  THR D C   1 
ATOM   15151 O  O   . THR D  1 233 ? 30.977  -28.627 -4.970  1.00 19.24 ? 250  THR D O   1 
ATOM   15152 C  CB  . THR D  1 233 ? 30.479  -26.866 -2.541  1.00 19.86 ? 250  THR D CB  1 
ATOM   15153 O  OG1 . THR D  1 233 ? 30.754  -26.626 -1.163  1.00 21.08 ? 250  THR D OG1 1 
ATOM   15154 C  CG2 . THR D  1 233 ? 29.302  -26.008 -2.976  1.00 19.31 ? 250  THR D CG2 1 
ATOM   15155 N  N   . LEU D  1 234 ? 28.784  -29.011 -4.588  1.00 20.03 ? 251  LEU D N   1 
ATOM   15156 C  CA  . LEU D  1 234 ? 28.476  -29.365 -5.963  1.00 20.43 ? 251  LEU D CA  1 
ATOM   15157 C  C   . LEU D  1 234 ? 28.500  -28.099 -6.817  1.00 20.71 ? 251  LEU D C   1 
ATOM   15158 O  O   . LEU D  1 234 ? 27.772  -27.147 -6.526  1.00 20.37 ? 251  LEU D O   1 
ATOM   15159 C  CB  . LEU D  1 234 ? 27.111  -30.049 -6.029  1.00 21.09 ? 251  LEU D CB  1 
ATOM   15160 C  CG  . LEU D  1 234 ? 26.583  -30.359 -7.435  1.00 22.66 ? 251  LEU D CG  1 
ATOM   15161 C  CD1 . LEU D  1 234 ? 27.492  -31.353 -8.127  1.00 23.06 ? 251  LEU D CD1 1 
ATOM   15162 C  CD2 . LEU D  1 234 ? 25.164  -30.899 -7.393  1.00 23.66 ? 251  LEU D CD2 1 
ATOM   15163 N  N   . ILE D  1 235 ? 29.335  -28.113 -7.866  1.00 19.85 ? 252  ILE D N   1 
ATOM   15164 C  CA  . ILE D  1 235 ? 29.458  -26.989 -8.781  1.00 20.97 ? 252  ILE D CA  1 
ATOM   15165 C  C   . ILE D  1 235 ? 29.154  -27.474 -10.197 1.00 20.70 ? 252  ILE D C   1 
ATOM   15166 O  O   . ILE D  1 235 ? 29.937  -28.218 -10.786 1.00 21.36 ? 252  ILE D O   1 
ATOM   15167 C  CB  . ILE D  1 235 ? 30.851  -26.338 -8.700  1.00 21.10 ? 252  ILE D CB  1 
ATOM   15168 C  CG1 . ILE D  1 235 ? 31.191  -25.882 -7.273  1.00 22.03 ? 252  ILE D CG1 1 
ATOM   15169 C  CG2 . ILE D  1 235 ? 30.954  -25.188 -9.708  1.00 21.34 ? 252  ILE D CG2 1 
ATOM   15170 C  CD1 . ILE D  1 235 ? 32.641  -25.469 -7.077  1.00 22.56 ? 252  ILE D CD1 1 
ATOM   15171 N  N   . GLN D  1 236 ? 28.034  -27.000 -10.749 1.00 20.29 ? 253  GLN D N   1 
ATOM   15172 C  CA  . GLN D  1 236 ? 27.579  -27.428 -12.058 1.00 20.78 ? 253  GLN D CA  1 
ATOM   15173 C  C   . GLN D  1 236 ? 27.740  -26.296 -13.076 1.00 21.78 ? 253  GLN D C   1 
ATOM   15174 O  O   . GLN D  1 236 ? 27.204  -25.205 -12.879 1.00 20.89 ? 253  GLN D O   1 
ATOM   15175 C  CB  . GLN D  1 236 ? 26.119  -27.858 -11.982 1.00 21.09 ? 253  GLN D CB  1 
ATOM   15176 C  CG  . GLN D  1 236 ? 25.639  -28.504 -13.276 1.00 22.33 ? 253  GLN D CG  1 
ATOM   15177 C  CD  . GLN D  1 236 ? 24.367  -27.880 -13.793 1.00 22.71 ? 253  GLN D CD  1 
ATOM   15178 O  OE1 . GLN D  1 236 ? 23.297  -28.019 -13.198 1.00 22.08 ? 253  GLN D OE1 1 
ATOM   15179 N  NE2 . GLN D  1 236 ? 24.480  -27.182 -14.913 1.00 25.91 ? 253  GLN D NE2 1 
ATOM   15180 N  N   . PHE D  1 237 ? 28.455  -26.595 -14.172 1.00 21.61 ? 254  PHE D N   1 
ATOM   15181 C  CA  . PHE D  1 237 ? 28.722  -25.658 -15.255 1.00 22.11 ? 254  PHE D CA  1 
ATOM   15182 C  C   . PHE D  1 237 ? 27.597  -25.733 -16.282 1.00 22.57 ? 254  PHE D C   1 
ATOM   15183 O  O   . PHE D  1 237 ? 27.152  -26.823 -16.630 1.00 23.01 ? 254  PHE D O   1 
ATOM   15184 C  CB  . PHE D  1 237 ? 30.067  -25.980 -15.918 1.00 22.81 ? 254  PHE D CB  1 
ATOM   15185 C  CG  . PHE D  1 237 ? 31.302  -25.473 -15.185 1.00 24.62 ? 254  PHE D CG  1 
ATOM   15186 C  CD1 . PHE D  1 237 ? 31.603  -25.912 -13.901 1.00 25.77 ? 254  PHE D CD1 1 
ATOM   15187 C  CD2 . PHE D  1 237 ? 32.188  -24.595 -15.804 1.00 25.15 ? 254  PHE D CD2 1 
ATOM   15188 C  CE1 . PHE D  1 237 ? 32.733  -25.455 -13.242 1.00 26.75 ? 254  PHE D CE1 1 
ATOM   15189 C  CE2 . PHE D  1 237 ? 33.321  -24.150 -15.145 1.00 26.08 ? 254  PHE D CE2 1 
ATOM   15190 C  CZ  . PHE D  1 237 ? 33.588  -24.574 -13.863 1.00 27.18 ? 254  PHE D CZ  1 
ATOM   15191 N  N   . GLU D  1 238 ? 27.177  -24.543 -16.719 1.00 23.35 ? 255  GLU D N   1 
ATOM   15192 C  CA  . GLU D  1 238 ? 26.047  -24.456 -17.664 1.00 25.73 ? 255  GLU D CA  1 
ATOM   15193 C  C   . GLU D  1 238 ? 26.242  -23.339 -18.694 1.00 24.61 ? 255  GLU D C   1 
ATOM   15194 O  O   . GLU D  1 238 ? 26.624  -22.234 -18.292 1.00 23.20 ? 255  GLU D O   1 
ATOM   15195 C  CB  . GLU D  1 238 ? 24.753  -24.144 -16.915 1.00 28.38 ? 255  GLU D CB  1 
ATOM   15196 C  CG  . GLU D  1 238 ? 23.514  -24.174 -17.801 1.00 31.59 ? 255  GLU D CG  1 
ATOM   15197 C  CD  . GLU D  1 238 ? 22.765  -25.493 -17.770 1.00 34.86 ? 255  GLU D CD  1 
ATOM   15198 O  OE1 . GLU D  1 238 ? 23.202  -26.418 -17.061 1.00 35.37 ? 255  GLU D OE1 1 
ATOM   15199 O  OE2 . GLU D  1 238 ? 21.737  -25.589 -18.463 1.00 38.71 ? 255  GLU D OE2 1 
ATOM   15200 N  N   . ASP D  1 239 ? 26.065  -23.651 -19.969 1.00 24.63 ? 256  ASP D N   1 
ATOM   15201 C  CA  . ASP D  1 239 ? 26.013  -22.683 -21.063 1.00 25.02 ? 256  ASP D CA  1 
ATOM   15202 C  C   . ASP D  1 239 ? 27.345  -21.955 -21.254 1.00 24.40 ? 256  ASP D C   1 
ATOM   15203 O  O   . ASP D  1 239 ? 27.363  -20.790 -21.649 1.00 24.71 ? 256  ASP D O   1 
ATOM   15204 C  CB  . ASP D  1 239 ? 24.825  -21.737 -20.936 1.00 26.09 ? 256  ASP D CB  1 
ATOM   15205 C  CG  . ASP D  1 239 ? 23.454  -22.336 -21.237 1.00 29.11 ? 256  ASP D CG  1 
ATOM   15206 O  OD1 . ASP D  1 239 ? 23.396  -23.510 -21.667 1.00 30.82 ? 256  ASP D OD1 1 
ATOM   15207 O  OD2 . ASP D  1 239 ? 22.440  -21.619 -21.045 1.00 31.60 ? 256  ASP D OD2 1 
ATOM   15208 N  N   . PHE D  1 240 ? 28.454  -22.666 -21.018 1.00 23.80 ? 257  PHE D N   1 
ATOM   15209 C  CA  . PHE D  1 240 ? 29.767  -22.257 -21.489 1.00 24.16 ? 257  PHE D CA  1 
ATOM   15210 C  C   . PHE D  1 240 ? 29.904  -22.627 -22.967 1.00 24.56 ? 257  PHE D C   1 
ATOM   15211 O  O   . PHE D  1 240 ? 29.209  -23.513 -23.457 1.00 24.57 ? 257  PHE D O   1 
ATOM   15212 C  CB  . PHE D  1 240 ? 30.857  -22.939 -20.653 1.00 24.81 ? 257  PHE D CB  1 
ATOM   15213 C  CG  . PHE D  1 240 ? 31.130  -22.306 -19.293 1.00 24.75 ? 257  PHE D CG  1 
ATOM   15214 C  CD1 . PHE D  1 240 ? 30.253  -22.492 -18.229 1.00 25.00 ? 257  PHE D CD1 1 
ATOM   15215 C  CD2 . PHE D  1 240 ? 32.271  -21.539 -19.081 1.00 25.56 ? 257  PHE D CD2 1 
ATOM   15216 C  CE1 . PHE D  1 240 ? 30.504  -21.906 -16.994 1.00 25.47 ? 257  PHE D CE1 1 
ATOM   15217 C  CE2 . PHE D  1 240 ? 32.522  -20.964 -17.841 1.00 25.85 ? 257  PHE D CE2 1 
ATOM   15218 C  CZ  . PHE D  1 240 ? 31.640  -21.154 -16.800 1.00 25.74 ? 257  PHE D CZ  1 
ATOM   15219 N  N   . GLY D  1 241 ? 30.798  -21.935 -23.676 1.00 26.17 ? 258  GLY D N   1 
ATOM   15220 C  CA  . GLY D  1 241 ? 31.154  -22.304 -25.037 1.00 27.77 ? 258  GLY D CA  1 
ATOM   15221 C  C   . GLY D  1 241 ? 31.838  -23.669 -25.045 1.00 28.18 ? 258  GLY D C   1 
ATOM   15222 O  O   . GLY D  1 241 ? 32.448  -24.052 -24.053 1.00 26.66 ? 258  GLY D O   1 
ATOM   15223 N  N   . ASN D  1 242 ? 31.741  -24.382 -26.174 1.00 31.51 ? 259  ASN D N   1 
ATOM   15224 C  CA  . ASN D  1 242 ? 32.105  -25.791 -26.250 1.00 34.13 ? 259  ASN D CA  1 
ATOM   15225 C  C   . ASN D  1 242 ? 33.543  -26.039 -25.800 1.00 34.81 ? 259  ASN D C   1 
ATOM   15226 O  O   . ASN D  1 242 ? 33.790  -26.956 -25.017 1.00 36.32 ? 259  ASN D O   1 
ATOM   15227 C  CB  . ASN D  1 242 ? 31.911  -26.359 -27.653 1.00 37.83 ? 259  ASN D CB  1 
ATOM   15228 C  CG  . ASN D  1 242 ? 30.470  -26.686 -27.969 1.00 42.11 ? 259  ASN D CG  1 
ATOM   15229 O  OD1 . ASN D  1 242 ? 29.574  -26.497 -27.135 1.00 45.60 ? 259  ASN D OD1 1 
ATOM   15230 N  ND2 . ASN D  1 242 ? 30.229  -27.205 -29.164 1.00 43.63 ? 259  ASN D ND2 1 
ATOM   15231 N  N   . HIS D  1 243 ? 34.494  -25.251 -26.315 1.00 35.29 ? 260  HIS D N   1 
ATOM   15232 C  CA  . HIS D  1 243 ? 35.894  -25.451 -25.967 1.00 37.05 ? 260  HIS D CA  1 
ATOM   15233 C  C   . HIS D  1 243 ? 36.060  -25.384 -24.447 1.00 35.74 ? 260  HIS D C   1 
ATOM   15234 O  O   . HIS D  1 243 ? 36.640  -26.290 -23.845 1.00 37.28 ? 260  HIS D O   1 
ATOM   15235 C  CB  . HIS D  1 243 ? 36.801  -24.468 -26.717 1.00 39.65 ? 260  HIS D CB  1 
ATOM   15236 C  CG  . HIS D  1 243 ? 38.254  -24.623 -26.383 1.00 43.86 ? 260  HIS D CG  1 
ATOM   15237 N  ND1 . HIS D  1 243 ? 38.973  -25.765 -26.673 1.00 45.17 ? 260  HIS D ND1 1 
ATOM   15238 C  CD2 . HIS D  1 243 ? 39.106  -23.804 -25.749 1.00 45.58 ? 260  HIS D CD2 1 
ATOM   15239 C  CE1 . HIS D  1 243 ? 40.220  -25.618 -26.249 1.00 45.99 ? 260  HIS D CE1 1 
ATOM   15240 N  NE2 . HIS D  1 243 ? 40.325  -24.433 -25.687 1.00 46.58 ? 260  HIS D NE2 1 
ATOM   15241 N  N   . ASN D  1 244 ? 35.503  -24.331 -23.831 1.00 30.29 ? 261  ASN D N   1 
ATOM   15242 C  CA  . ASN D  1 244 ? 35.637  -24.113 -22.400 1.00 28.85 ? 261  ASN D CA  1 
ATOM   15243 C  C   . ASN D  1 244 ? 34.908  -25.200 -21.606 1.00 27.41 ? 261  ASN D C   1 
ATOM   15244 O  O   . ASN D  1 244 ? 35.381  -25.605 -20.546 1.00 27.15 ? 261  ASN D O   1 
ATOM   15245 C  CB  . ASN D  1 244 ? 35.162  -22.719 -22.006 1.00 27.96 ? 261  ASN D CB  1 
ATOM   15246 C  CG  . ASN D  1 244 ? 36.108  -21.630 -22.459 1.00 28.62 ? 261  ASN D CG  1 
ATOM   15247 O  OD1 . ASN D  1 244 ? 37.306  -21.876 -22.651 1.00 26.43 ? 261  ASN D OD1 1 
ATOM   15248 N  ND2 . ASN D  1 244 ? 35.597  -20.413 -22.597 1.00 28.11 ? 261  ASN D ND2 1 
ATOM   15249 N  N   . ALA D  1 245 ? 33.763  -25.670 -22.115 1.00 27.19 ? 262  ALA D N   1 
ATOM   15250 C  CA  . ALA D  1 245 ? 32.935  -26.618 -21.383 1.00 27.10 ? 262  ALA D CA  1 
ATOM   15251 C  C   . ALA D  1 245 ? 33.694  -27.921 -21.148 1.00 28.07 ? 262  ALA D C   1 
ATOM   15252 O  O   . ALA D  1 245 ? 33.836  -28.361 -20.005 1.00 25.75 ? 262  ALA D O   1 
ATOM   15253 C  CB  . ALA D  1 245 ? 31.644  -26.865 -22.119 1.00 26.73 ? 262  ALA D CB  1 
ATOM   15254 N  N   . PHE D  1 246 ? 34.185  -28.523 -22.238 1.00 28.87 ? 263  PHE D N   1 
ATOM   15255 C  CA  . PHE D  1 246 ? 34.901  -29.791 -22.161 1.00 31.35 ? 263  PHE D CA  1 
ATOM   15256 C  C   . PHE D  1 246 ? 36.199  -29.635 -21.375 1.00 29.30 ? 263  PHE D C   1 
ATOM   15257 O  O   . PHE D  1 246 ? 36.515  -30.480 -20.537 1.00 29.26 ? 263  PHE D O   1 
ATOM   15258 C  CB  . PHE D  1 246 ? 35.254  -30.378 -23.531 1.00 34.48 ? 263  PHE D CB  1 
ATOM   15259 C  CG  . PHE D  1 246 ? 34.141  -31.182 -24.186 1.00 38.53 ? 263  PHE D CG  1 
ATOM   15260 C  CD1 . PHE D  1 246 ? 33.977  -32.533 -23.903 1.00 39.86 ? 263  PHE D CD1 1 
ATOM   15261 C  CD2 . PHE D  1 246 ? 33.268  -30.584 -25.092 1.00 41.15 ? 263  PHE D CD2 1 
ATOM   15262 C  CE1 . PHE D  1 246 ? 32.965  -33.266 -24.511 1.00 41.05 ? 263  PHE D CE1 1 
ATOM   15263 C  CE2 . PHE D  1 246 ? 32.262  -31.321 -25.697 1.00 41.43 ? 263  PHE D CE2 1 
ATOM   15264 C  CZ  . PHE D  1 246 ? 32.110  -32.659 -25.404 1.00 42.33 ? 263  PHE D CZ  1 
ATOM   15265 N  N   . ARG D  1 247 ? 36.956  -28.567 -21.643 1.00 28.34 ? 264  ARG D N   1 
ATOM   15266 C  CA  . ARG D  1 247 ? 38.286  -28.450 -21.065 1.00 29.26 ? 264  ARG D CA  1 
ATOM   15267 C  C   . ARG D  1 247 ? 38.189  -28.174 -19.561 1.00 28.04 ? 264  ARG D C   1 
ATOM   15268 O  O   . ARG D  1 247 ? 39.053  -28.618 -18.807 1.00 26.78 ? 264  ARG D O   1 
ATOM   15269 C  CB  . ARG D  1 247 ? 39.171  -27.466 -21.843 1.00 29.92 ? 264  ARG D CB  1 
ATOM   15270 C  CG  . ARG D  1 247 ? 39.074  -26.000 -21.454 1.00 31.89 ? 264  ARG D CG  1 
ATOM   15271 C  CD  . ARG D  1 247 ? 39.786  -25.125 -22.472 1.00 31.59 ? 264  ARG D CD  1 
ATOM   15272 N  NE  . ARG D  1 247 ? 39.575  -23.698 -22.207 1.00 32.26 ? 264  ARG D NE  1 
ATOM   15273 C  CZ  . ARG D  1 247 ? 40.233  -22.960 -21.322 1.00 31.82 ? 264  ARG D CZ  1 
ATOM   15274 N  NH1 . ARG D  1 247 ? 41.220  -23.478 -20.610 1.00 31.77 ? 264  ARG D NH1 1 
ATOM   15275 N  NH2 . ARG D  1 247 ? 39.922  -21.685 -21.179 1.00 31.49 ? 264  ARG D NH2 1 
ATOM   15276 N  N   . PHE D  1 248 ? 37.128  -27.479 -19.117 1.00 26.73 ? 265  PHE D N   1 
ATOM   15277 C  CA  . PHE D  1 248 ? 36.935  -27.215 -17.696 1.00 25.66 ? 265  PHE D CA  1 
ATOM   15278 C  C   . PHE D  1 248 ? 36.440  -28.475 -16.989 1.00 25.04 ? 265  PHE D C   1 
ATOM   15279 O  O   . PHE D  1 248 ? 36.811  -28.711 -15.843 1.00 24.34 ? 265  PHE D O   1 
ATOM   15280 C  CB  . PHE D  1 248 ? 35.989  -26.041 -17.407 1.00 25.42 ? 265  PHE D CB  1 
ATOM   15281 C  CG  . PHE D  1 248 ? 36.586  -24.662 -17.653 1.00 25.42 ? 265  PHE D CG  1 
ATOM   15282 C  CD1 . PHE D  1 248 ? 37.953  -24.435 -17.519 1.00 26.03 ? 265  PHE D CD1 1 
ATOM   15283 C  CD2 . PHE D  1 248 ? 35.775  -23.592 -18.024 1.00 25.48 ? 265  PHE D CD2 1 
ATOM   15284 C  CE1 . PHE D  1 248 ? 38.490  -23.180 -17.750 1.00 26.45 ? 265  PHE D CE1 1 
ATOM   15285 C  CE2 . PHE D  1 248 ? 36.318  -22.339 -18.252 1.00 25.67 ? 265  PHE D CE2 1 
ATOM   15286 C  CZ  . PHE D  1 248 ? 37.671  -22.134 -18.112 1.00 26.26 ? 265  PHE D CZ  1 
ATOM   15287 N  N   . LEU D  1 249 ? 35.608  -29.279 -17.660 1.00 25.34 ? 266  LEU D N   1 
ATOM   15288 C  CA  . LEU D  1 249 ? 35.166  -30.540 -17.086 1.00 26.72 ? 266  LEU D CA  1 
ATOM   15289 C  C   . LEU D  1 249 ? 36.387  -31.436 -16.853 1.00 28.26 ? 266  LEU D C   1 
ATOM   15290 O  O   . LEU D  1 249 ? 36.514  -32.055 -15.800 1.00 27.28 ? 266  LEU D O   1 
ATOM   15291 C  CB  . LEU D  1 249 ? 34.118  -31.227 -17.962 1.00 26.19 ? 266  LEU D CB  1 
ATOM   15292 C  CG  . LEU D  1 249 ? 33.658  -32.617 -17.501 1.00 26.35 ? 266  LEU D CG  1 
ATOM   15293 C  CD1 . LEU D  1 249 ? 33.031  -32.601 -16.113 1.00 26.42 ? 266  LEU D CD1 1 
ATOM   15294 C  CD2 . LEU D  1 249 ? 32.688  -33.220 -18.491 1.00 26.39 ? 266  LEU D CD2 1 
ATOM   15295 N  N   . ARG D  1 250 ? 37.290  -31.488 -17.839 1.00 28.85 ? 267  ARG D N   1 
ATOM   15296 C  CA  . ARG D  1 250 ? 38.500  -32.291 -17.734 1.00 30.18 ? 267  ARG D CA  1 
ATOM   15297 C  C   . ARG D  1 250 ? 39.401  -31.753 -16.625 1.00 27.53 ? 267  ARG D C   1 
ATOM   15298 O  O   . ARG D  1 250 ? 39.964  -32.528 -15.860 1.00 26.94 ? 267  ARG D O   1 
ATOM   15299 C  CB  . ARG D  1 250 ? 39.257  -32.341 -19.066 1.00 34.09 ? 267  ARG D CB  1 
ATOM   15300 C  CG  . ARG D  1 250 ? 40.597  -33.058 -18.964 1.00 39.86 ? 267  ARG D CG  1 
ATOM   15301 C  CD  . ARG D  1 250 ? 41.196  -33.406 -20.323 1.00 45.40 ? 267  ARG D CD  1 
ATOM   15302 N  NE  . ARG D  1 250 ? 40.382  -34.355 -21.094 1.00 50.66 ? 267  ARG D NE  1 
ATOM   15303 C  CZ  . ARG D  1 250 ? 40.103  -35.617 -20.753 1.00 57.04 ? 267  ARG D CZ  1 
ATOM   15304 N  NH1 . ARG D  1 250 ? 40.545  -36.128 -19.616 1.00 60.48 ? 267  ARG D NH1 1 
ATOM   15305 N  NH2 . ARG D  1 250 ? 39.373  -36.376 -21.554 1.00 59.54 ? 267  ARG D NH2 1 
ATOM   15306 N  N   . LYS D  1 251 ? 39.521  -30.426 -16.538 1.00 27.78 ? 268  LYS D N   1 
ATOM   15307 C  CA  . LYS D  1 251 ? 40.430  -29.789 -15.600 1.00 28.24 ? 268  LYS D CA  1 
ATOM   15308 C  C   . LYS D  1 251 ? 39.998  -30.014 -14.150 1.00 27.54 ? 268  LYS D C   1 
ATOM   15309 O  O   . LYS D  1 251 ? 40.850  -30.227 -13.296 1.00 26.17 ? 268  LYS D O   1 
ATOM   15310 C  CB  . LYS D  1 251 ? 40.525  -28.286 -15.883 1.00 29.94 ? 268  LYS D CB  1 
ATOM   15311 C  CG  . LYS D  1 251 ? 41.563  -27.546 -15.061 1.00 30.89 ? 268  LYS D CG  1 
ATOM   15312 C  CD  . LYS D  1 251 ? 41.755  -26.100 -15.493 1.00 32.06 ? 268  LYS D CD  1 
ATOM   15313 C  CE  . LYS D  1 251 ? 42.831  -25.437 -14.697 1.00 32.62 ? 268  LYS D CE  1 
ATOM   15314 N  NZ  . LYS D  1 251 ? 43.041  -24.054 -15.132 1.00 33.67 ? 268  LYS D NZ  1 
ATOM   15315 N  N   . TYR D  1 252 ? 38.687  -29.979 -13.870 1.00 26.54 ? 269  TYR D N   1 
ATOM   15316 C  CA  . TYR D  1 252 ? 38.217  -29.842 -12.499 1.00 25.52 ? 269  TYR D CA  1 
ATOM   15317 C  C   . TYR D  1 252 ? 37.568  -31.104 -11.934 1.00 24.93 ? 269  TYR D C   1 
ATOM   15318 O  O   . TYR D  1 252 ? 37.335  -31.164 -10.731 1.00 24.29 ? 269  TYR D O   1 
ATOM   15319 C  CB  . TYR D  1 252 ? 37.182  -28.717 -12.438 1.00 24.66 ? 269  TYR D CB  1 
ATOM   15320 C  CG  . TYR D  1 252 ? 37.755  -27.328 -12.660 1.00 24.70 ? 269  TYR D CG  1 
ATOM   15321 C  CD1 . TYR D  1 252 ? 38.903  -26.902 -12.000 1.00 24.93 ? 269  TYR D CD1 1 
ATOM   15322 C  CD2 . TYR D  1 252 ? 37.150  -26.450 -13.552 1.00 25.66 ? 269  TYR D CD2 1 
ATOM   15323 C  CE1 . TYR D  1 252 ? 39.421  -25.635 -12.202 1.00 26.32 ? 269  TYR D CE1 1 
ATOM   15324 C  CE2 . TYR D  1 252 ? 37.659  -25.180 -13.760 1.00 26.48 ? 269  TYR D CE2 1 
ATOM   15325 C  CZ  . TYR D  1 252 ? 38.794  -24.772 -13.084 1.00 26.52 ? 269  TYR D CZ  1 
ATOM   15326 O  OH  . TYR D  1 252 ? 39.283  -23.522 -13.311 1.00 29.00 ? 269  TYR D OH  1 
ATOM   15327 N  N   . ARG D  1 253 ? 37.251  -32.097 -12.768 1.00 25.50 ? 270  ARG D N   1 
ATOM   15328 C  CA  . ARG D  1 253 ? 36.350  -33.155 -12.334 1.00 26.49 ? 270  ARG D CA  1 
ATOM   15329 C  C   . ARG D  1 253 ? 36.975  -34.027 -11.241 1.00 26.67 ? 270  ARG D C   1 
ATOM   15330 O  O   . ARG D  1 253 ? 36.247  -34.587 -10.429 1.00 25.08 ? 270  ARG D O   1 
ATOM   15331 C  CB  . ARG D  1 253 ? 35.855  -34.001 -13.508 1.00 28.22 ? 270  ARG D CB  1 
ATOM   15332 C  CG  . ARG D  1 253 ? 36.909  -34.784 -14.272 1.00 29.18 ? 270  ARG D CG  1 
ATOM   15333 C  CD  . ARG D  1 253 ? 36.266  -35.505 -15.445 1.00 30.77 ? 270  ARG D CD  1 
ATOM   15334 N  NE  . ARG D  1 253 ? 35.218  -36.421 -14.986 1.00 30.88 ? 270  ARG D NE  1 
ATOM   15335 C  CZ  . ARG D  1 253 ? 34.285  -36.965 -15.748 1.00 31.99 ? 270  ARG D CZ  1 
ATOM   15336 N  NH1 . ARG D  1 253 ? 34.322  -36.802 -17.063 1.00 32.74 ? 270  ARG D NH1 1 
ATOM   15337 N  NH2 . ARG D  1 253 ? 33.320  -37.676 -15.186 1.00 32.05 ? 270  ARG D NH2 1 
ATOM   15338 N  N   . GLU D  1 254 ? 38.310  -34.154 -11.223 1.00 28.43 ? 271  GLU D N   1 
ATOM   15339 C  CA  . GLU D  1 254 ? 38.985  -34.959 -10.214 1.00 30.51 ? 271  GLU D CA  1 
ATOM   15340 C  C   . GLU D  1 254 ? 39.492  -34.097 -9.058  1.00 29.40 ? 271  GLU D C   1 
ATOM   15341 O  O   . GLU D  1 254 ? 40.003  -34.635 -8.079  1.00 28.30 ? 271  GLU D O   1 
ATOM   15342 C  CB  . GLU D  1 254 ? 40.145  -35.738 -10.839 1.00 35.87 ? 271  GLU D CB  1 
ATOM   15343 C  CG  . GLU D  1 254 ? 39.689  -36.785 -11.851 1.00 40.80 ? 271  GLU D CG  1 
ATOM   15344 C  CD  . GLU D  1 254 ? 40.821  -37.535 -12.528 1.00 48.49 ? 271  GLU D CD  1 
ATOM   15345 O  OE1 . GLU D  1 254 ? 40.518  -38.335 -13.437 1.00 56.11 ? 271  GLU D OE1 1 
ATOM   15346 O  OE2 . GLU D  1 254 ? 41.998  -37.333 -12.154 1.00 52.66 ? 271  GLU D OE2 1 
ATOM   15347 N  N   . LYS D  1 255 ? 39.364  -32.770 -9.182  1.00 28.24 ? 272  LYS D N   1 
ATOM   15348 C  CA  . LYS D  1 255 ? 39.834  -31.832 -8.172  1.00 29.55 ? 272  LYS D CA  1 
ATOM   15349 C  C   . LYS D  1 255 ? 38.662  -31.311 -7.337  1.00 26.49 ? 272  LYS D C   1 
ATOM   15350 O  O   . LYS D  1 255 ? 38.833  -31.025 -6.156  1.00 26.13 ? 272  LYS D O   1 
ATOM   15351 C  CB  . LYS D  1 255 ? 40.596  -30.702 -8.877  1.00 33.53 ? 272  LYS D CB  1 
ATOM   15352 C  CG  . LYS D  1 255 ? 41.290  -29.677 -7.986  1.00 38.41 ? 272  LYS D CG  1 
ATOM   15353 C  CD  . LYS D  1 255 ? 42.235  -28.755 -8.752  1.00 41.98 ? 272  LYS D CD  1 
ATOM   15354 C  CE  . LYS D  1 255 ? 42.659  -27.533 -7.993  1.00 45.24 ? 272  LYS D CE  1 
ATOM   15355 N  NZ  . LYS D  1 255 ? 43.377  -27.850 -6.756  1.00 48.17 ? 272  LYS D NZ  1 
ATOM   15356 N  N   . TYR D  1 256 ? 37.480  -31.183 -7.954  1.00 24.88 ? 273  TYR D N   1 
ATOM   15357 C  CA  . TYR D  1 256 ? 36.300  -30.638 -7.296  1.00 24.35 ? 273  TYR D CA  1 
ATOM   15358 C  C   . TYR D  1 256 ? 35.094  -31.532 -7.567  1.00 22.76 ? 273  TYR D C   1 
ATOM   15359 O  O   . TYR D  1 256 ? 35.176  -32.465 -8.359  1.00 22.56 ? 273  TYR D O   1 
ATOM   15360 C  CB  . TYR D  1 256 ? 36.018  -29.220 -7.809  1.00 24.49 ? 273  TYR D CB  1 
ATOM   15361 C  CG  . TYR D  1 256 ? 37.112  -28.211 -7.499  1.00 24.61 ? 273  TYR D CG  1 
ATOM   15362 C  CD1 . TYR D  1 256 ? 37.249  -27.694 -6.221  1.00 25.36 ? 273  TYR D CD1 1 
ATOM   15363 C  CD2 . TYR D  1 256 ? 37.999  -27.769 -8.474  1.00 24.77 ? 273  TYR D CD2 1 
ATOM   15364 C  CE1 . TYR D  1 256 ? 38.241  -26.781 -5.913  1.00 25.79 ? 273  TYR D CE1 1 
ATOM   15365 C  CE2 . TYR D  1 256 ? 38.998  -26.855 -8.180  1.00 25.70 ? 273  TYR D CE2 1 
ATOM   15366 C  CZ  . TYR D  1 256 ? 39.114  -26.355 -6.894  1.00 26.56 ? 273  TYR D CZ  1 
ATOM   15367 O  OH  . TYR D  1 256 ? 40.075  -25.445 -6.565  1.00 27.73 ? 273  TYR D OH  1 
ATOM   15368 N  N   . CYS D  1 257 ? 33.974  -31.228 -6.898  1.00 21.06 ? 274  CYS D N   1 
ATOM   15369 C  CA  . CYS D  1 257 ? 32.718  -31.916 -7.128  1.00 21.03 ? 274  CYS D CA  1 
ATOM   15370 C  C   . CYS D  1 257 ? 31.938  -31.158 -8.200  1.00 21.47 ? 274  CYS D C   1 
ATOM   15371 O  O   . CYS D  1 257 ? 31.221  -30.206 -7.895  1.00 20.90 ? 274  CYS D O   1 
ATOM   15372 C  CB  . CYS D  1 257 ? 31.931  -32.044 -5.830  1.00 20.84 ? 274  CYS D CB  1 
ATOM   15373 S  SG  . CYS D  1 257 ? 30.443  -33.063 -5.985  1.00 22.67 ? 274  CYS D SG  1 
ATOM   15374 N  N   . THR D  1 258 ? 32.103  -31.574 -9.463  1.00 21.08 ? 275  THR D N   1 
ATOM   15375 C  CA  . THR D  1 258 ? 31.626  -30.775 -10.580 1.00 21.20 ? 275  THR D CA  1 
ATOM   15376 C  C   . THR D  1 258 ? 31.159  -31.668 -11.728 1.00 21.56 ? 275  THR D C   1 
ATOM   15377 O  O   . THR D  1 258 ? 31.684  -32.758 -11.949 1.00 21.24 ? 275  THR D O   1 
ATOM   15378 C  CB  . THR D  1 258 ? 32.724  -29.797 -11.003 1.00 21.21 ? 275  THR D CB  1 
ATOM   15379 O  OG1 . THR D  1 258 ? 32.152  -28.962 -12.006 1.00 21.94 ? 275  THR D OG1 1 
ATOM   15380 C  CG2 . THR D  1 258 ? 33.970  -30.479 -11.538 1.00 21.61 ? 275  THR D CG2 1 
ATOM   15381 N  N   . PHE D  1 259 ? 30.139  -31.184 -12.444 1.00 21.41 ? 276  PHE D N   1 
ATOM   15382 C  CA  . PHE D  1 259 ? 29.705  -31.789 -13.692 1.00 21.82 ? 276  PHE D CA  1 
ATOM   15383 C  C   . PHE D  1 259 ? 29.226  -30.675 -14.616 1.00 21.90 ? 276  PHE D C   1 
ATOM   15384 O  O   . PHE D  1 259 ? 29.073  -29.536 -14.179 1.00 21.53 ? 276  PHE D O   1 
ATOM   15385 C  CB  . PHE D  1 259 ? 28.652  -32.869 -13.431 1.00 22.12 ? 276  PHE D CB  1 
ATOM   15386 C  CG  . PHE D  1 259 ? 27.220  -32.446 -13.131 1.00 23.50 ? 276  PHE D CG  1 
ATOM   15387 C  CD1 . PHE D  1 259 ? 26.819  -32.137 -11.836 1.00 25.10 ? 276  PHE D CD1 1 
ATOM   15388 C  CD2 . PHE D  1 259 ? 26.258  -32.438 -14.135 1.00 23.80 ? 276  PHE D CD2 1 
ATOM   15389 C  CE1 . PHE D  1 259 ? 25.500  -31.793 -11.567 1.00 25.23 ? 276  PHE D CE1 1 
ATOM   15390 C  CE2 . PHE D  1 259 ? 24.941  -32.107 -13.856 1.00 24.52 ? 276  PHE D CE2 1 
ATOM   15391 C  CZ  . PHE D  1 259 ? 24.567  -31.783 -12.576 1.00 24.45 ? 276  PHE D CZ  1 
ATOM   15392 N  N   . ASN D  1 260 ? 29.045  -31.024 -15.893 1.00 21.63 ? 277  ASN D N   1 
ATOM   15393 C  CA  . ASN D  1 260 ? 28.540  -30.114 -16.906 1.00 22.25 ? 277  ASN D CA  1 
ATOM   15394 C  C   . ASN D  1 260 ? 27.284  -30.748 -17.483 1.00 22.90 ? 277  ASN D C   1 
ATOM   15395 O  O   . ASN D  1 260 ? 27.350  -31.810 -18.106 1.00 21.36 ? 277  ASN D O   1 
ATOM   15396 C  CB  . ASN D  1 260 ? 29.587  -29.814 -17.974 1.00 23.25 ? 277  ASN D CB  1 
ATOM   15397 C  CG  . ASN D  1 260 ? 29.092  -28.817 -19.001 1.00 24.68 ? 277  ASN D CG  1 
ATOM   15398 O  OD1 . ASN D  1 260 ? 28.106  -29.079 -19.701 1.00 26.56 ? 277  ASN D OD1 1 
ATOM   15399 N  ND2 . ASN D  1 260 ? 29.755  -27.675 -19.114 1.00 24.70 ? 277  ASN D ND2 1 
ATOM   15400 N  N   . ASP D  1 261 ? 26.133  -30.120 -17.223 1.00 22.45 ? 278  ASP D N   1 
ATOM   15401 C  CA  . ASP D  1 261 ? 24.869  -30.729 -17.583 1.00 23.43 ? 278  ASP D CA  1 
ATOM   15402 C  C   . ASP D  1 261 ? 24.718  -30.814 -19.100 1.00 23.69 ? 278  ASP D C   1 
ATOM   15403 O  O   . ASP D  1 261 ? 24.105  -31.754 -19.600 1.00 22.02 ? 278  ASP D O   1 
ATOM   15404 C  CB  . ASP D  1 261 ? 23.680  -30.001 -16.989 1.00 24.41 ? 278  ASP D CB  1 
ATOM   15405 C  CG  . ASP D  1 261 ? 22.372  -30.745 -17.192 1.00 25.44 ? 278  ASP D CG  1 
ATOM   15406 O  OD1 . ASP D  1 261 ? 22.304  -31.913 -16.758 1.00 27.24 ? 278  ASP D OD1 1 
ATOM   15407 O  OD2 . ASP D  1 261 ? 21.452  -30.170 -17.809 1.00 28.18 ? 278  ASP D OD2 1 
ATOM   15408 N  N   . ASP D  1 262 ? 25.279  -29.834 -19.818 1.00 24.85 ? 279  ASP D N   1 
ATOM   15409 C  CA  . ASP D  1 262 ? 25.142  -29.759 -21.265 1.00 26.39 ? 279  ASP D CA  1 
ATOM   15410 C  C   . ASP D  1 262 ? 25.806  -30.964 -21.935 1.00 26.08 ? 279  ASP D C   1 
ATOM   15411 O  O   . ASP D  1 262 ? 25.335  -31.426 -22.975 1.00 26.42 ? 279  ASP D O   1 
ATOM   15412 C  CB  . ASP D  1 262 ? 25.674  -28.442 -21.812 1.00 28.28 ? 279  ASP D CB  1 
ATOM   15413 C  CG  . ASP D  1 262 ? 24.978  -27.192 -21.285 1.00 32.07 ? 279  ASP D CG  1 
ATOM   15414 O  OD1 . ASP D  1 262 ? 23.733  -27.152 -21.336 1.00 35.41 ? 279  ASP D OD1 1 
ATOM   15415 O  OD2 . ASP D  1 262 ? 25.688  -26.273 -20.822 1.00 33.93 ? 279  ASP D OD2 1 
ATOM   15416 N  N   . ILE D  1 263 ? 26.900  -31.456 -21.339 1.00 25.49 ? 280  ILE D N   1 
ATOM   15417 C  CA  . ILE D  1 263 ? 27.636  -32.597 -21.860 1.00 24.19 ? 280  ILE D CA  1 
ATOM   15418 C  C   . ILE D  1 263 ? 27.075  -33.881 -21.254 1.00 23.75 ? 280  ILE D C   1 
ATOM   15419 O  O   . ILE D  1 263 ? 26.636  -34.773 -21.974 1.00 23.02 ? 280  ILE D O   1 
ATOM   15420 C  CB  . ILE D  1 263 ? 29.142  -32.447 -21.576 1.00 25.19 ? 280  ILE D CB  1 
ATOM   15421 C  CG1 . ILE D  1 263 ? 29.722  -31.225 -22.297 1.00 25.76 ? 280  ILE D CG1 1 
ATOM   15422 C  CG2 . ILE D  1 263 ? 29.895  -33.732 -21.928 1.00 24.96 ? 280  ILE D CG2 1 
ATOM   15423 C  CD1 . ILE D  1 263 ? 31.136  -30.857 -21.875 1.00 26.14 ? 280  ILE D CD1 1 
ATOM   15424 N  N   . GLN D  1 264 ? 27.087  -33.961 -19.917 1.00 23.37 ? 281  GLN D N   1 
ATOM   15425 C  CA  . GLN D  1 264 ? 26.899  -35.225 -19.223 1.00 22.73 ? 281  GLN D CA  1 
ATOM   15426 C  C   . GLN D  1 264 ? 25.422  -35.525 -19.006 1.00 22.54 ? 281  GLN D C   1 
ATOM   15427 O  O   . GLN D  1 264 ? 25.010  -36.681 -19.080 1.00 22.74 ? 281  GLN D O   1 
ATOM   15428 C  CB  . GLN D  1 264 ? 27.656  -35.198 -17.898 1.00 23.00 ? 281  GLN D CB  1 
ATOM   15429 C  CG  . GLN D  1 264 ? 29.167  -35.189 -18.087 1.00 23.54 ? 281  GLN D CG  1 
ATOM   15430 C  CD  . GLN D  1 264 ? 29.906  -34.834 -16.819 1.00 23.28 ? 281  GLN D CD  1 
ATOM   15431 O  OE1 . GLN D  1 264 ? 29.755  -33.730 -16.279 1.00 23.68 ? 281  GLN D OE1 1 
ATOM   15432 N  NE2 . GLN D  1 264 ? 30.716  -35.765 -16.337 1.00 22.51 ? 281  GLN D NE2 1 
ATOM   15433 N  N   . GLY D  1 265 ? 24.635  -34.487 -18.711 1.00 21.78 ? 282  GLY D N   1 
ATOM   15434 C  CA  . GLY D  1 265 ? 23.198  -34.646 -18.578 1.00 21.56 ? 282  GLY D CA  1 
ATOM   15435 C  C   . GLY D  1 265 ? 22.569  -35.046 -19.911 1.00 21.98 ? 282  GLY D C   1 
ATOM   15436 O  O   . GLY D  1 265 ? 21.744  -35.958 -19.961 1.00 21.61 ? 282  GLY D O   1 
ATOM   15437 N  N   . THR D  1 266 ? 22.968  -34.344 -20.978 1.00 22.32 ? 283  THR D N   1 
ATOM   15438 C  CA  . THR D  1 266 ? 22.512  -34.634 -22.329 1.00 23.28 ? 283  THR D CA  1 
ATOM   15439 C  C   . THR D  1 266 ? 22.805  -36.094 -22.668 1.00 24.08 ? 283  THR D C   1 
ATOM   15440 O  O   . THR D  1 266 ? 21.925  -36.817 -23.134 1.00 24.93 ? 283  THR D O   1 
ATOM   15441 C  CB  . THR D  1 266 ? 23.206  -33.689 -23.305 1.00 24.82 ? 283  THR D CB  1 
ATOM   15442 O  OG1 . THR D  1 266 ? 22.821  -32.372 -22.918 1.00 25.49 ? 283  THR D OG1 1 
ATOM   15443 C  CG2 . THR D  1 266 ? 22.820  -33.953 -24.749 1.00 25.88 ? 283  THR D CG2 1 
ATOM   15444 N  N   . ALA D  1 267 ? 24.054  -36.507 -22.431 1.00 23.96 ? 284  ALA D N   1 
ATOM   15445 C  CA  . ALA D  1 267 ? 24.494  -37.863 -22.719 1.00 23.83 ? 284  ALA D CA  1 
ATOM   15446 C  C   . ALA D  1 267 ? 23.599  -38.883 -22.021 1.00 23.73 ? 284  ALA D C   1 
ATOM   15447 O  O   . ALA D  1 267 ? 23.151  -39.836 -22.654 1.00 23.39 ? 284  ALA D O   1 
ATOM   15448 C  CB  . ALA D  1 267 ? 25.943  -38.031 -22.324 1.00 23.16 ? 284  ALA D CB  1 
ATOM   15449 N  N   . ALA D  1 268 ? 23.339  -38.673 -20.721 1.00 23.46 ? 285  ALA D N   1 
ATOM   15450 C  CA  . ALA D  1 268 ? 22.575  -39.618 -19.918 1.00 23.67 ? 285  ALA D CA  1 
ATOM   15451 C  C   . ALA D  1 268 ? 21.130  -39.735 -20.396 1.00 23.44 ? 285  ALA D C   1 
ATOM   15452 O  O   . ALA D  1 268 ? 20.561  -40.827 -20.398 1.00 22.60 ? 285  ALA D O   1 
ATOM   15453 C  CB  . ALA D  1 268 ? 22.619  -39.225 -18.457 1.00 23.10 ? 285  ALA D CB  1 
ATOM   15454 N  N   . VAL D  1 269 ? 20.501  -38.605 -20.725 1.00 23.30 ? 286  VAL D N   1 
ATOM   15455 C  CA  . VAL D  1 269 ? 19.093  -38.647 -21.076 1.00 24.33 ? 286  VAL D CA  1 
ATOM   15456 C  C   . VAL D  1 269 ? 18.937  -39.283 -22.465 1.00 23.30 ? 286  VAL D C   1 
ATOM   15457 O  O   . VAL D  1 269 ? 18.004  -40.048 -22.690 1.00 23.03 ? 286  VAL D O   1 
ATOM   15458 C  CB  . VAL D  1 269 ? 18.417  -37.265 -20.949 1.00 26.51 ? 286  VAL D CB  1 
ATOM   15459 C  CG1 . VAL D  1 269 ? 18.938  -36.258 -21.962 1.00 28.01 ? 286  VAL D CG1 1 
ATOM   15460 C  CG2 . VAL D  1 269 ? 16.900  -37.375 -21.032 1.00 28.18 ? 286  VAL D CG2 1 
ATOM   15461 N  N   . ALA D  1 270 ? 19.879  -39.025 -23.379 1.00 23.60 ? 287  ALA D N   1 
ATOM   15462 C  CA  . ALA D  1 270 ? 19.856  -39.651 -24.696 1.00 24.17 ? 287  ALA D CA  1 
ATOM   15463 C  C   . ALA D  1 270 ? 20.075  -41.161 -24.587 1.00 24.92 ? 287  ALA D C   1 
ATOM   15464 O  O   . ALA D  1 270 ? 19.385  -41.933 -25.254 1.00 24.84 ? 287  ALA D O   1 
ATOM   15465 C  CB  . ALA D  1 270 ? 20.894  -39.024 -25.597 1.00 23.81 ? 287  ALA D CB  1 
ATOM   15466 N  N   . LEU D  1 271 ? 21.047  -41.582 -23.763 1.00 23.61 ? 288  LEU D N   1 
ATOM   15467 C  CA  . LEU D  1 271 ? 21.312  -43.000 -23.569 1.00 23.71 ? 288  LEU D CA  1 
ATOM   15468 C  C   . LEU D  1 271 ? 20.063  -43.682 -23.013 1.00 23.83 ? 288  LEU D C   1 
ATOM   15469 O  O   . LEU D  1 271 ? 19.704  -44.765 -23.460 1.00 24.90 ? 288  LEU D O   1 
ATOM   15470 C  CB  . LEU D  1 271 ? 22.521  -43.266 -22.671 1.00 24.12 ? 288  LEU D CB  1 
ATOM   15471 C  CG  . LEU D  1 271 ? 22.811  -44.740 -22.368 1.00 24.58 ? 288  LEU D CG  1 
ATOM   15472 C  CD1 . LEU D  1 271 ? 23.106  -45.517 -23.650 1.00 25.00 ? 288  LEU D CD1 1 
ATOM   15473 C  CD2 . LEU D  1 271 ? 23.951  -44.904 -21.386 1.00 25.83 ? 288  LEU D CD2 1 
ATOM   15474 N  N   . ALA D  1 272 ? 19.394  -43.041 -22.049 1.00 23.91 ? 289  ALA D N   1 
ATOM   15475 C  CA  . ALA D  1 272 ? 18.217  -43.627 -21.421 1.00 23.93 ? 289  ALA D CA  1 
ATOM   15476 C  C   . ALA D  1 272 ? 17.165  -43.980 -22.473 1.00 24.49 ? 289  ALA D C   1 
ATOM   15477 O  O   . ALA D  1 272 ? 16.541  -45.040 -22.401 1.00 22.30 ? 289  ALA D O   1 
ATOM   15478 C  CB  . ALA D  1 272 ? 17.656  -42.681 -20.379 1.00 24.05 ? 289  ALA D CB  1 
ATOM   15479 N  N   . GLY D  1 273 ? 16.960  -43.061 -23.427 1.00 24.45 ? 290  GLY D N   1 
ATOM   15480 C  CA  . GLY D  1 273 ? 16.041  -43.280 -24.533 1.00 25.31 ? 290  GLY D CA  1 
ATOM   15481 C  C   . GLY D  1 273 ? 16.450  -44.477 -25.390 1.00 24.42 ? 290  GLY D C   1 
ATOM   15482 O  O   . GLY D  1 273 ? 15.614  -45.316 -25.714 1.00 25.78 ? 290  GLY D O   1 
ATOM   15483 N  N   . LEU D  1 274 ? 17.737  -44.539 -25.750 1.00 24.68 ? 291  LEU D N   1 
ATOM   15484 C  CA  . LEU D  1 274 ? 18.276  -45.629 -26.549 1.00 25.20 ? 291  LEU D CA  1 
ATOM   15485 C  C   . LEU D  1 274 ? 18.096  -46.966 -25.829 1.00 25.50 ? 291  LEU D C   1 
ATOM   15486 O  O   . LEU D  1 274 ? 17.824  -47.972 -26.474 1.00 25.19 ? 291  LEU D O   1 
ATOM   15487 C  CB  . LEU D  1 274 ? 19.745  -45.373 -26.881 1.00 26.04 ? 291  LEU D CB  1 
ATOM   15488 C  CG  . LEU D  1 274 ? 20.053  -44.132 -27.727 1.00 27.44 ? 291  LEU D CG  1 
ATOM   15489 C  CD1 . LEU D  1 274 ? 21.555  -43.962 -27.859 1.00 27.49 ? 291  LEU D CD1 1 
ATOM   15490 C  CD2 . LEU D  1 274 ? 19.411  -44.163 -29.109 1.00 28.13 ? 291  LEU D CD2 1 
ATOM   15491 N  N   . LEU D  1 275 ? 18.264  -46.982 -24.500 1.00 26.18 ? 292  LEU D N   1 
ATOM   15492 C  CA  . LEU D  1 275 ? 18.118  -48.198 -23.715 1.00 27.60 ? 292  LEU D CA  1 
ATOM   15493 C  C   . LEU D  1 275 ? 16.657  -48.641 -23.689 1.00 27.70 ? 292  LEU D C   1 
ATOM   15494 O  O   . LEU D  1 275 ? 16.373  -49.836 -23.704 1.00 26.83 ? 292  LEU D O   1 
ATOM   15495 C  CB  . LEU D  1 275 ? 18.664  -47.999 -22.301 1.00 28.52 ? 292  LEU D CB  1 
ATOM   15496 C  CG  . LEU D  1 275 ? 20.185  -47.900 -22.178 1.00 29.02 ? 292  LEU D CG  1 
ATOM   15497 C  CD1 . LEU D  1 275 ? 20.562  -47.499 -20.763 1.00 29.37 ? 292  LEU D CD1 1 
ATOM   15498 C  CD2 . LEU D  1 275 ? 20.887  -49.195 -22.567 1.00 30.28 ? 292  LEU D CD2 1 
ATOM   15499 N  N   . ALA D  1 276 ? 15.737  -47.673 -23.650 1.00 28.56 ? 293  ALA D N   1 
ATOM   15500 C  CA  . ALA D  1 276 ? 14.314  -47.967 -23.694 1.00 29.55 ? 293  ALA D CA  1 
ATOM   15501 C  C   . ALA D  1 276 ? 13.943  -48.585 -25.046 1.00 30.78 ? 293  ALA D C   1 
ATOM   15502 O  O   . ALA D  1 276 ? 13.152  -49.525 -25.105 1.00 30.81 ? 293  ALA D O   1 
ATOM   15503 C  CB  . ALA D  1 276 ? 13.524  -46.711 -23.420 1.00 30.06 ? 293  ALA D CB  1 
ATOM   15504 N  N   . ALA D  1 277 ? 14.527  -48.057 -26.129 1.00 32.41 ? 294  ALA D N   1 
ATOM   15505 C  CA  . ALA D  1 277 ? 14.300  -48.595 -27.464 1.00 32.27 ? 294  ALA D CA  1 
ATOM   15506 C  C   . ALA D  1 277 ? 14.806  -50.035 -27.546 1.00 33.35 ? 294  ALA D C   1 
ATOM   15507 O  O   . ALA D  1 277 ? 14.123  -50.892 -28.101 1.00 35.64 ? 294  ALA D O   1 
ATOM   15508 C  CB  . ALA D  1 277 ? 14.964  -47.723 -28.507 1.00 31.87 ? 294  ALA D CB  1 
ATOM   15509 N  N   . GLN D  1 278 ? 15.998  -50.286 -26.991 1.00 33.16 ? 295  GLN D N   1 
ATOM   15510 C  CA  . GLN D  1 278 ? 16.607  -51.608 -27.006 1.00 36.16 ? 295  GLN D CA  1 
ATOM   15511 C  C   . GLN D  1 278 ? 15.738  -52.621 -26.259 1.00 38.67 ? 295  GLN D C   1 
ATOM   15512 O  O   . GLN D  1 278 ? 15.740  -53.798 -26.612 1.00 39.29 ? 295  GLN D O   1 
ATOM   15513 C  CB  . GLN D  1 278 ? 18.031  -51.579 -26.445 1.00 36.59 ? 295  GLN D CB  1 
ATOM   15514 C  CG  . GLN D  1 278 ? 18.655  -52.951 -26.191 1.00 38.23 ? 295  GLN D CG  1 
ATOM   15515 C  CD  . GLN D  1 278 ? 18.832  -53.800 -27.436 1.00 40.63 ? 295  GLN D CD  1 
ATOM   15516 O  OE1 . GLN D  1 278 ? 18.475  -53.412 -28.555 1.00 38.88 ? 295  GLN D OE1 1 
ATOM   15517 N  NE2 . GLN D  1 278 ? 19.402  -54.983 -27.250 1.00 41.11 ? 295  GLN D NE2 1 
ATOM   15518 N  N   . LYS D  1 279 ? 15.007  -52.175 -25.229 1.00 39.27 ? 296  LYS D N   1 
ATOM   15519 C  CA  . LYS D  1 279 ? 14.115  -53.066 -24.501 1.00 41.39 ? 296  LYS D CA  1 
ATOM   15520 C  C   . LYS D  1 279 ? 13.007  -53.565 -25.426 1.00 44.59 ? 296  LYS D C   1 
ATOM   15521 O  O   . LYS D  1 279 ? 12.622  -54.730 -25.355 1.00 47.26 ? 296  LYS D O   1 
ATOM   15522 C  CB  . LYS D  1 279 ? 13.496  -52.420 -23.256 1.00 42.32 ? 296  LYS D CB  1 
ATOM   15523 C  CG  . LYS D  1 279 ? 14.365  -52.467 -22.009 1.00 43.86 ? 296  LYS D CG  1 
ATOM   15524 C  CD  . LYS D  1 279 ? 13.648  -52.068 -20.724 1.00 45.21 ? 296  LYS D CD  1 
ATOM   15525 C  CE  . LYS D  1 279 ? 12.605  -53.060 -20.306 1.00 46.91 ? 296  LYS D CE  1 
ATOM   15526 N  NZ  . LYS D  1 279 ? 12.043  -52.735 -18.992 1.00 48.76 ? 296  LYS D NZ  1 
ATOM   15527 N  N   . VAL D  1 280 ? 12.502  -52.674 -26.289 1.00 45.01 ? 297  VAL D N   1 
ATOM   15528 C  CA  . VAL D  1 280 ? 11.437  -53.011 -27.222 1.00 44.75 ? 297  VAL D CA  1 
ATOM   15529 C  C   . VAL D  1 280 ? 11.998  -53.853 -28.370 1.00 43.90 ? 297  VAL D C   1 
ATOM   15530 O  O   . VAL D  1 280 ? 11.378  -54.834 -28.766 1.00 46.15 ? 297  VAL D O   1 
ATOM   15531 C  CB  . VAL D  1 280 ? 10.739  -51.742 -27.748 1.00 45.28 ? 297  VAL D CB  1 
ATOM   15532 C  CG1 . VAL D  1 280 ? 9.671   -52.065 -28.788 1.00 46.81 ? 297  VAL D CG1 1 
ATOM   15533 C  CG2 . VAL D  1 280 ? 10.142  -50.907 -26.620 1.00 44.24 ? 297  VAL D CG2 1 
ATOM   15534 N  N   . ILE D  1 281 ? 13.167  -53.472 -28.897 1.00 43.62 ? 298  ILE D N   1 
ATOM   15535 C  CA  . ILE D  1 281 ? 13.693  -54.055 -30.124 1.00 45.16 ? 298  ILE D CA  1 
ATOM   15536 C  C   . ILE D  1 281 ? 14.407  -55.374 -29.827 1.00 47.22 ? 298  ILE D C   1 
ATOM   15537 O  O   . ILE D  1 281 ? 14.254  -56.340 -30.576 1.00 45.40 ? 298  ILE D O   1 
ATOM   15538 C  CB  . ILE D  1 281 ? 14.624  -53.060 -30.846 1.00 45.50 ? 298  ILE D CB  1 
ATOM   15539 C  CG1 . ILE D  1 281 ? 13.870  -51.814 -31.312 1.00 45.89 ? 298  ILE D CG1 1 
ATOM   15540 C  CG2 . ILE D  1 281 ? 15.353  -53.733 -32.009 1.00 46.31 ? 298  ILE D CG2 1 
ATOM   15541 C  CD1 . ILE D  1 281 ? 14.773  -50.686 -31.781 1.00 46.64 ? 298  ILE D CD1 1 
ATOM   15542 N  N   . SER D  1 282 ? 15.224  -55.391 -28.766 1.00 48.07 ? 299  SER D N   1 
ATOM   15543 C  CA  . SER D  1 282 ? 15.995  -56.566 -28.384 1.00 50.06 ? 299  SER D CA  1 
ATOM   15544 C  C   . SER D  1 282 ? 16.914  -56.989 -29.529 1.00 51.55 ? 299  SER D C   1 
ATOM   15545 O  O   . SER D  1 282 ? 16.965  -58.164 -29.885 1.00 50.92 ? 299  SER D O   1 
ATOM   15546 C  CB  . SER D  1 282 ? 15.101  -57.716 -27.961 1.00 50.84 ? 299  SER D CB  1 
ATOM   15547 O  OG  . SER D  1 282 ? 14.184  -57.323 -26.950 1.00 52.24 ? 299  SER D OG  1 
ATOM   15548 N  N   . LYS D  1 283 ? 17.630  -56.014 -30.100 1.00 52.60 ? 300  LYS D N   1 
ATOM   15549 C  CA  . LYS D  1 283 ? 18.600  -56.270 -31.153 1.00 54.29 ? 300  LYS D CA  1 
ATOM   15550 C  C   . LYS D  1 283 ? 19.952  -56.554 -30.505 1.00 52.76 ? 300  LYS D C   1 
ATOM   15551 O  O   . LYS D  1 283 ? 20.398  -55.777 -29.666 1.00 50.19 ? 300  LYS D O   1 
ATOM   15552 C  CB  . LYS D  1 283 ? 18.654  -55.052 -32.084 1.00 56.95 ? 300  LYS D CB  1 
ATOM   15553 C  CG  . LYS D  1 283 ? 19.499  -55.186 -33.342 1.00 59.27 ? 300  LYS D CG  1 
ATOM   15554 C  CD  . LYS D  1 283 ? 19.261  -54.041 -34.321 1.00 61.34 ? 300  LYS D CD  1 
ATOM   15555 C  CE  . LYS D  1 283 ? 19.745  -54.331 -35.703 1.00 63.64 ? 300  LYS D CE  1 
ATOM   15556 N  NZ  . LYS D  1 283 ? 21.203  -54.457 -35.744 1.00 66.27 ? 300  LYS D NZ  1 
ATOM   15557 N  N   . PRO D  1 284 ? 20.644  -57.666 -30.850 1.00 53.17 ? 301  PRO D N   1 
ATOM   15558 C  CA  . PRO D  1 284 ? 21.944  -57.969 -30.250 1.00 53.13 ? 301  PRO D CA  1 
ATOM   15559 C  C   . PRO D  1 284 ? 22.880  -56.765 -30.333 1.00 52.81 ? 301  PRO D C   1 
ATOM   15560 O  O   . PRO D  1 284 ? 23.071  -56.199 -31.407 1.00 51.91 ? 301  PRO D O   1 
ATOM   15561 C  CB  . PRO D  1 284 ? 22.453  -59.176 -31.061 1.00 53.37 ? 301  PRO D CB  1 
ATOM   15562 C  CG  . PRO D  1 284 ? 21.191  -59.830 -31.582 1.00 53.29 ? 301  PRO D CG  1 
ATOM   15563 C  CD  . PRO D  1 284 ? 20.217  -58.687 -31.823 1.00 53.88 ? 301  PRO D CD  1 
ATOM   15564 N  N   . ILE D  1 285 ? 23.467  -56.399 -29.187 1.00 52.43 ? 302  ILE D N   1 
ATOM   15565 C  CA  . ILE D  1 285 ? 24.252  -55.182 -29.054 1.00 54.64 ? 302  ILE D CA  1 
ATOM   15566 C  C   . ILE D  1 285 ? 25.381  -55.162 -30.085 1.00 54.74 ? 302  ILE D C   1 
ATOM   15567 O  O   . ILE D  1 285 ? 25.730  -54.097 -30.587 1.00 56.08 ? 302  ILE D O   1 
ATOM   15568 C  CB  . ILE D  1 285 ? 24.766  -55.032 -27.607 1.00 56.30 ? 302  ILE D CB  1 
ATOM   15569 C  CG1 . ILE D  1 285 ? 23.610  -54.693 -26.652 1.00 57.56 ? 302  ILE D CG1 1 
ATOM   15570 C  CG2 . ILE D  1 285 ? 25.896  -54.004 -27.512 1.00 55.94 ? 302  ILE D CG2 1 
ATOM   15571 C  CD1 . ILE D  1 285 ? 23.940  -54.837 -25.176 1.00 58.54 ? 302  ILE D CD1 1 
ATOM   15572 N  N   . SER D  1 286 ? 25.933  -56.338 -30.413 1.00 56.68 ? 303  SER D N   1 
ATOM   15573 C  CA  . SER D  1 286 ? 27.043  -56.435 -31.351 1.00 57.74 ? 303  SER D CA  1 
ATOM   15574 C  C   . SER D  1 286 ? 26.601  -56.190 -32.798 1.00 56.57 ? 303  SER D C   1 
ATOM   15575 O  O   . SER D  1 286 ? 27.449  -56.053 -33.678 1.00 58.37 ? 303  SER D O   1 
ATOM   15576 C  CB  . SER D  1 286 ? 27.760  -57.762 -31.212 1.00 59.27 ? 303  SER D CB  1 
ATOM   15577 O  OG  . SER D  1 286 ? 26.849  -58.853 -31.185 1.00 61.07 ? 303  SER D OG  1 
ATOM   15578 N  N   . GLU D  1 287 ? 25.286  -56.121 -33.049 1.00 53.24 ? 304  GLU D N   1 
ATOM   15579 C  CA  . GLU D  1 287 ? 24.772  -55.861 -34.387 1.00 53.29 ? 304  GLU D CA  1 
ATOM   15580 C  C   . GLU D  1 287 ? 24.297  -54.412 -34.528 1.00 51.38 ? 304  GLU D C   1 
ATOM   15581 O  O   . GLU D  1 287 ? 23.736  -54.046 -35.561 1.00 50.10 ? 304  GLU D O   1 
ATOM   15582 C  CB  . GLU D  1 287 ? 23.622  -56.817 -34.706 1.00 56.55 ? 304  GLU D CB  1 
ATOM   15583 C  CG  . GLU D  1 287 ? 24.016  -58.292 -34.666 1.00 59.35 ? 304  GLU D CG  1 
ATOM   15584 C  CD  . GLU D  1 287 ? 22.877  -59.259 -34.948 1.00 61.72 ? 304  GLU D CD  1 
ATOM   15585 O  OE1 . GLU D  1 287 ? 23.152  -60.476 -34.986 1.00 65.59 ? 304  GLU D OE1 1 
ATOM   15586 O  OE2 . GLU D  1 287 ? 21.721  -58.811 -35.122 1.00 62.65 ? 304  GLU D OE2 1 
ATOM   15587 N  N   . HIS D  1 288 ? 24.515  -53.588 -33.494 1.00 46.27 ? 305  HIS D N   1 
ATOM   15588 C  CA  . HIS D  1 288 ? 24.112  -52.191 -33.532 1.00 44.05 ? 305  HIS D CA  1 
ATOM   15589 C  C   . HIS D  1 288 ? 25.146  -51.378 -34.299 1.00 40.30 ? 305  HIS D C   1 
ATOM   15590 O  O   . HIS D  1 288 ? 26.337  -51.674 -34.251 1.00 38.98 ? 305  HIS D O   1 
ATOM   15591 C  CB  . HIS D  1 288 ? 23.975  -51.601 -32.124 1.00 46.15 ? 305  HIS D CB  1 
ATOM   15592 C  CG  . HIS D  1 288 ? 22.747  -52.031 -31.404 1.00 47.74 ? 305  HIS D CG  1 
ATOM   15593 N  ND1 . HIS D  1 288 ? 22.083  -51.214 -30.516 1.00 51.09 ? 305  HIS D ND1 1 
ATOM   15594 C  CD2 . HIS D  1 288 ? 22.062  -53.177 -31.442 1.00 48.34 ? 305  HIS D CD2 1 
ATOM   15595 C  CE1 . HIS D  1 288 ? 21.029  -51.864 -30.038 1.00 51.95 ? 305  HIS D CE1 1 
ATOM   15596 N  NE2 . HIS D  1 288 ? 21.000  -53.058 -30.588 1.00 49.04 ? 305  HIS D NE2 1 
ATOM   15597 N  N   . LYS D  1 289 ? 24.674  -50.341 -34.995 1.00 39.87 ? 306  LYS D N   1 
ATOM   15598 C  CA  . LYS D  1 289 ? 25.569  -49.379 -35.615 1.00 41.44 ? 306  LYS D CA  1 
ATOM   15599 C  C   . LYS D  1 289 ? 24.908  -48.006 -35.569 1.00 38.23 ? 306  LYS D C   1 
ATOM   15600 O  O   . LYS D  1 289 ? 23.789  -47.839 -36.052 1.00 36.75 ? 306  LYS D O   1 
ATOM   15601 C  CB  . LYS D  1 289 ? 25.960  -49.840 -37.025 1.00 45.57 ? 306  LYS D CB  1 
ATOM   15602 C  CG  . LYS D  1 289 ? 26.949  -48.926 -37.738 1.00 49.54 ? 306  LYS D CG  1 
ATOM   15603 C  CD  . LYS D  1 289 ? 27.924  -49.629 -38.676 1.00 52.07 ? 306  LYS D CD  1 
ATOM   15604 C  CE  . LYS D  1 289 ? 27.271  -50.590 -39.614 1.00 55.29 ? 306  LYS D CE  1 
ATOM   15605 N  NZ  . LYS D  1 289 ? 28.204  -51.019 -40.659 1.00 57.38 ? 306  LYS D NZ  1 
ATOM   15606 N  N   . ILE D  1 290 ? 25.611  -47.044 -34.955 1.00 37.33 ? 307  ILE D N   1 
ATOM   15607 C  CA  . ILE D  1 290 ? 25.063  -45.731 -34.650 1.00 35.53 ? 307  ILE D CA  1 
ATOM   15608 C  C   . ILE D  1 290 ? 25.683  -44.714 -35.605 1.00 33.70 ? 307  ILE D C   1 
ATOM   15609 O  O   . ILE D  1 290 ? 26.906  -44.636 -35.709 1.00 36.10 ? 307  ILE D O   1 
ATOM   15610 C  CB  . ILE D  1 290 ? 25.347  -45.330 -33.187 1.00 35.05 ? 307  ILE D CB  1 
ATOM   15611 C  CG1 . ILE D  1 290 ? 25.167  -46.493 -32.201 1.00 35.10 ? 307  ILE D CG1 1 
ATOM   15612 C  CG2 . ILE D  1 290 ? 24.519  -44.105 -32.790 1.00 34.91 ? 307  ILE D CG2 1 
ATOM   15613 C  CD1 . ILE D  1 290 ? 23.753  -47.022 -32.101 1.00 35.27 ? 307  ILE D CD1 1 
ATOM   15614 N  N   . LEU D  1 291 ? 24.834  -43.916 -36.262 1.00 34.05 ? 308  LEU D N   1 
ATOM   15615 C  CA  . LEU D  1 291 ? 25.301  -42.846 -37.132 1.00 34.95 ? 308  LEU D CA  1 
ATOM   15616 C  C   . LEU D  1 291 ? 24.807  -41.509 -36.584 1.00 32.99 ? 308  LEU D C   1 
ATOM   15617 O  O   . LEU D  1 291 ? 23.605  -41.293 -36.455 1.00 33.08 ? 308  LEU D O   1 
ATOM   15618 C  CB  . LEU D  1 291 ? 24.833  -43.090 -38.570 1.00 36.40 ? 308  LEU D CB  1 
ATOM   15619 C  CG  . LEU D  1 291 ? 25.078  -41.954 -39.572 1.00 37.78 ? 308  LEU D CG  1 
ATOM   15620 C  CD1 . LEU D  1 291 ? 26.537  -41.534 -39.635 1.00 37.51 ? 308  LEU D CD1 1 
ATOM   15621 C  CD2 . LEU D  1 291 ? 24.592  -42.345 -40.960 1.00 39.61 ? 308  LEU D CD2 1 
ATOM   15622 N  N   . PHE D  1 292 ? 25.747  -40.616 -36.257 1.00 34.44 ? 309  PHE D N   1 
ATOM   15623 C  CA  . PHE D  1 292 ? 25.399  -39.293 -35.760 1.00 35.75 ? 309  PHE D CA  1 
ATOM   15624 C  C   . PHE D  1 292 ? 25.364  -38.297 -36.918 1.00 35.42 ? 309  PHE D C   1 
ATOM   15625 O  O   . PHE D  1 292 ? 26.300  -38.239 -37.713 1.00 35.05 ? 309  PHE D O   1 
ATOM   15626 C  CB  . PHE D  1 292 ? 26.402  -38.789 -34.718 1.00 36.31 ? 309  PHE D CB  1 
ATOM   15627 C  CG  . PHE D  1 292 ? 26.280  -39.424 -33.338 1.00 36.67 ? 309  PHE D CG  1 
ATOM   15628 C  CD1 . PHE D  1 292 ? 26.957  -40.599 -33.029 1.00 36.54 ? 309  PHE D CD1 1 
ATOM   15629 C  CD2 . PHE D  1 292 ? 25.504  -38.829 -32.346 1.00 36.55 ? 309  PHE D CD2 1 
ATOM   15630 C  CE1 . PHE D  1 292 ? 26.845  -41.170 -31.768 1.00 36.53 ? 309  PHE D CE1 1 
ATOM   15631 C  CE2 . PHE D  1 292 ? 25.398  -39.403 -31.087 1.00 35.65 ? 309  PHE D CE2 1 
ATOM   15632 C  CZ  . PHE D  1 292 ? 26.067  -40.572 -30.802 1.00 35.58 ? 309  PHE D CZ  1 
ATOM   15633 N  N   . LEU D  1 293 ? 24.283  -37.509 -36.975 1.00 36.10 ? 310  LEU D N   1 
ATOM   15634 C  CA  . LEU D  1 293 ? 24.275  -36.250 -37.702 1.00 38.49 ? 310  LEU D CA  1 
ATOM   15635 C  C   . LEU D  1 293 ? 24.823  -35.169 -36.773 1.00 38.38 ? 310  LEU D C   1 
ATOM   15636 O  O   . LEU D  1 293 ? 24.111  -34.690 -35.895 1.00 38.58 ? 310  LEU D O   1 
ATOM   15637 C  CB  . LEU D  1 293 ? 22.873  -35.890 -38.191 1.00 37.67 ? 310  LEU D CB  1 
ATOM   15638 C  CG  . LEU D  1 293 ? 22.774  -34.623 -39.051 1.00 39.36 ? 310  LEU D CG  1 
ATOM   15639 C  CD1 . LEU D  1 293 ? 23.328  -34.853 -40.447 1.00 39.88 ? 310  LEU D CD1 1 
ATOM   15640 C  CD2 . LEU D  1 293 ? 21.345  -34.117 -39.117 1.00 39.81 ? 310  LEU D CD2 1 
ATOM   15641 N  N   . GLY D  1 294 ? 26.085  -34.789 -36.996 1.00 41.16 ? 311  GLY D N   1 
ATOM   15642 C  CA  . GLY D  1 294 ? 26.803  -33.883 -36.115 1.00 42.44 ? 311  GLY D CA  1 
ATOM   15643 C  C   . GLY D  1 294 ? 27.962  -34.606 -35.435 1.00 43.98 ? 311  GLY D C   1 
ATOM   15644 O  O   . GLY D  1 294 ? 27.949  -35.832 -35.314 1.00 43.91 ? 311  GLY D O   1 
ATOM   15645 N  N   . ALA D  1 295 ? 28.969  -33.832 -35.013 1.00 43.45 ? 312  ALA D N   1 
ATOM   15646 C  CA  . ALA D  1 295 ? 30.112  -34.372 -34.294 1.00 43.05 ? 312  ALA D CA  1 
ATOM   15647 C  C   . ALA D  1 295 ? 30.634  -33.351 -33.282 1.00 42.83 ? 312  ALA D C   1 
ATOM   15648 O  O   . ALA D  1 295 ? 31.832  -33.297 -33.014 1.00 45.32 ? 312  ALA D O   1 
ATOM   15649 C  CB  . ALA D  1 295 ? 31.185  -34.783 -35.278 1.00 41.89 ? 312  ALA D CB  1 
ATOM   15650 N  N   . GLY D  1 296 ? 29.715  -32.566 -32.707 1.00 44.11 ? 313  GLY D N   1 
ATOM   15651 C  CA  . GLY D  1 296 ? 30.064  -31.531 -31.748 1.00 45.47 ? 313  GLY D CA  1 
ATOM   15652 C  C   . GLY D  1 296 ? 29.912  -32.029 -30.313 1.00 45.77 ? 313  GLY D C   1 
ATOM   15653 O  O   . GLY D  1 296 ? 30.189  -33.190 -30.026 1.00 43.66 ? 313  GLY D O   1 
ATOM   15654 N  N   . GLU D  1 297 ? 29.449  -31.134 -29.433 1.00 47.48 ? 314  GLU D N   1 
ATOM   15655 C  CA  . GLU D  1 297 ? 29.401  -31.384 -28.000 1.00 46.09 ? 314  GLU D CA  1 
ATOM   15656 C  C   . GLU D  1 297 ? 28.459  -32.547 -27.696 1.00 42.82 ? 314  GLU D C   1 
ATOM   15657 O  O   . GLU D  1 297 ? 28.862  -33.517 -27.056 1.00 40.72 ? 314  GLU D O   1 
ATOM   15658 C  CB  . GLU D  1 297 ? 28.984  -30.103 -27.272 1.00 46.62 ? 314  GLU D CB  1 
ATOM   15659 C  CG  . GLU D  1 297 ? 28.774  -30.273 -25.768 1.00 46.81 ? 314  GLU D CG  1 
ATOM   15660 C  CD  . GLU D  1 297 ? 28.568  -28.969 -25.021 1.00 45.52 ? 314  GLU D CD  1 
ATOM   15661 O  OE1 . GLU D  1 297 ? 29.565  -28.250 -24.816 1.00 47.44 ? 314  GLU D OE1 1 
ATOM   15662 O  OE2 . GLU D  1 297 ? 27.414  -28.659 -24.664 1.00 45.14 ? 314  GLU D OE2 1 
ATOM   15663 N  N   . ALA D  1 298 ? 27.205  -32.429 -28.149 1.00 40.03 ? 315  ALA D N   1 
ATOM   15664 C  CA  . ALA D  1 298 ? 26.183  -33.417 -27.855 1.00 38.36 ? 315  ALA D CA  1 
ATOM   15665 C  C   . ALA D  1 298 ? 26.597  -34.789 -28.387 1.00 38.58 ? 315  ALA D C   1 
ATOM   15666 O  O   . ALA D  1 298 ? 26.500  -35.779 -27.670 1.00 37.34 ? 315  ALA D O   1 
ATOM   15667 C  CB  . ALA D  1 298 ? 24.854  -32.971 -28.417 1.00 38.76 ? 315  ALA D CB  1 
ATOM   15668 N  N   . ALA D  1 299 ? 27.086  -34.832 -29.634 1.00 39.91 ? 316  ALA D N   1 
ATOM   15669 C  CA  . ALA D  1 299 ? 27.472  -36.078 -30.281 1.00 39.15 ? 316  ALA D CA  1 
ATOM   15670 C  C   . ALA D  1 299 ? 28.568  -36.793 -29.490 1.00 38.80 ? 316  ALA D C   1 
ATOM   15671 O  O   . ALA D  1 299 ? 28.457  -37.989 -29.230 1.00 36.68 ? 316  ALA D O   1 
ATOM   15672 C  CB  . ALA D  1 299 ? 27.919  -35.809 -31.699 1.00 39.85 ? 316  ALA D CB  1 
ATOM   15673 N  N   . LEU D  1 300 ? 29.633  -36.061 -29.132 1.00 36.71 ? 317  LEU D N   1 
ATOM   15674 C  CA  . LEU D  1 300 ? 30.778  -36.648 -28.451 1.00 37.13 ? 317  LEU D CA  1 
ATOM   15675 C  C   . LEU D  1 300 ? 30.370  -37.133 -27.061 1.00 33.93 ? 317  LEU D C   1 
ATOM   15676 O  O   . LEU D  1 300 ? 30.797  -38.204 -26.631 1.00 30.90 ? 317  LEU D O   1 
ATOM   15677 C  CB  . LEU D  1 300 ? 31.929  -35.645 -28.376 1.00 40.24 ? 317  LEU D CB  1 
ATOM   15678 C  CG  . LEU D  1 300 ? 32.615  -35.326 -29.709 1.00 43.17 ? 317  LEU D CG  1 
ATOM   15679 C  CD1 . LEU D  1 300 ? 33.546  -34.127 -29.590 1.00 43.12 ? 317  LEU D CD1 1 
ATOM   15680 C  CD2 . LEU D  1 300 ? 33.375  -36.540 -30.221 1.00 43.27 ? 317  LEU D CD2 1 
ATOM   15681 N  N   . GLY D  1 301 ? 29.534  -36.336 -26.382 1.00 31.59 ? 318  GLY D N   1 
ATOM   15682 C  CA  . GLY D  1 301 ? 29.023  -36.678 -25.067 1.00 30.56 ? 318  GLY D CA  1 
ATOM   15683 C  C   . GLY D  1 301 ? 28.241  -37.987 -25.093 1.00 28.82 ? 318  GLY D C   1 
ATOM   15684 O  O   . GLY D  1 301 ? 28.539  -38.900 -24.329 1.00 26.29 ? 318  GLY D O   1 
ATOM   15685 N  N   . ILE D  1 302 ? 27.243  -38.052 -25.982 1.00 28.09 ? 319  ILE D N   1 
ATOM   15686 C  CA  . ILE D  1 302 ? 26.363  -39.203 -26.112 1.00 28.29 ? 319  ILE D CA  1 
ATOM   15687 C  C   . ILE D  1 302 ? 27.176  -40.437 -26.511 1.00 29.38 ? 319  ILE D C   1 
ATOM   15688 O  O   . ILE D  1 302 ? 27.015  -41.497 -25.909 1.00 27.23 ? 319  ILE D O   1 
ATOM   15689 C  CB  . ILE D  1 302 ? 25.230  -38.895 -27.109 1.00 27.82 ? 319  ILE D CB  1 
ATOM   15690 C  CG1 . ILE D  1 302 ? 24.329  -37.762 -26.601 1.00 27.69 ? 319  ILE D CG1 1 
ATOM   15691 C  CG2 . ILE D  1 302 ? 24.411  -40.144 -27.432 1.00 27.91 ? 319  ILE D CG2 1 
ATOM   15692 C  CD1 . ILE D  1 302 ? 23.486  -37.102 -27.675 1.00 27.51 ? 319  ILE D CD1 1 
ATOM   15693 N  N   . ALA D  1 303 ? 28.057  -40.286 -27.510 1.00 29.24 ? 320  ALA D N   1 
ATOM   15694 C  CA  . ALA D  1 303 ? 28.836  -41.396 -28.039 1.00 29.88 ? 320  ALA D CA  1 
ATOM   15695 C  C   . ALA D  1 303 ? 29.695  -42.031 -26.944 1.00 31.09 ? 320  ALA D C   1 
ATOM   15696 O  O   . ALA D  1 303 ? 29.770  -43.254 -26.835 1.00 29.31 ? 320  ALA D O   1 
ATOM   15697 C  CB  . ALA D  1 303 ? 29.687  -40.918 -29.198 1.00 30.54 ? 320  ALA D CB  1 
ATOM   15698 N  N   . ASN D  1 304 ? 30.331  -41.186 -26.123 1.00 31.73 ? 321  ASN D N   1 
ATOM   15699 C  CA  . ASN D  1 304 ? 31.212  -41.657 -25.067 1.00 31.35 ? 321  ASN D CA  1 
ATOM   15700 C  C   . ASN D  1 304 ? 30.426  -42.491 -24.055 1.00 28.54 ? 321  ASN D C   1 
ATOM   15701 O  O   . ASN D  1 304 ? 30.945  -43.487 -23.552 1.00 27.12 ? 321  ASN D O   1 
ATOM   15702 C  CB  . ASN D  1 304 ? 31.996  -40.510 -24.435 1.00 34.68 ? 321  ASN D CB  1 
ATOM   15703 C  CG  . ASN D  1 304 ? 33.128  -40.033 -25.323 1.00 40.24 ? 321  ASN D CG  1 
ATOM   15704 O  OD1 . ASN D  1 304 ? 33.898  -40.848 -25.848 1.00 42.86 ? 321  ASN D OD1 1 
ATOM   15705 N  ND2 . ASN D  1 304 ? 33.259  -38.725 -25.502 1.00 42.33 ? 321  ASN D ND2 1 
ATOM   15706 N  N   . LEU D  1 305 ? 29.171  -42.113 -23.780 1.00 25.33 ? 322  LEU D N   1 
ATOM   15707 C  CA  . LEU D  1 305 ? 28.373  -42.830 -22.796 1.00 25.73 ? 322  LEU D CA  1 
ATOM   15708 C  C   . LEU D  1 305 ? 27.836  -44.130 -23.404 1.00 25.99 ? 322  LEU D C   1 
ATOM   15709 O  O   . LEU D  1 305 ? 27.724  -45.138 -22.707 1.00 25.49 ? 322  LEU D O   1 
ATOM   15710 C  CB  . LEU D  1 305 ? 27.260  -41.935 -22.249 1.00 25.71 ? 322  LEU D CB  1 
ATOM   15711 C  CG  . LEU D  1 305 ? 26.708  -42.302 -20.865 1.00 26.05 ? 322  LEU D CG  1 
ATOM   15712 C  CD1 . LEU D  1 305 ? 27.771  -42.205 -19.786 1.00 27.05 ? 322  LEU D CD1 1 
ATOM   15713 C  CD2 . LEU D  1 305 ? 25.516  -41.438 -20.480 1.00 25.44 ? 322  LEU D CD2 1 
ATOM   15714 N  N   . ILE D  1 306 ? 27.520  -44.119 -24.708 1.00 25.25 ? 323  ILE D N   1 
ATOM   15715 C  CA  . ILE D  1 306 ? 27.111  -45.332 -25.399 1.00 25.07 ? 323  ILE D CA  1 
ATOM   15716 C  C   . ILE D  1 306 ? 28.232  -46.365 -25.304 1.00 24.52 ? 323  ILE D C   1 
ATOM   15717 O  O   . ILE D  1 306 ? 27.965  -47.538 -25.069 1.00 25.86 ? 323  ILE D O   1 
ATOM   15718 C  CB  . ILE D  1 306 ? 26.729  -45.062 -26.867 1.00 25.44 ? 323  ILE D CB  1 
ATOM   15719 C  CG1 . ILE D  1 306 ? 25.468  -44.208 -26.979 1.00 24.97 ? 323  ILE D CG1 1 
ATOM   15720 C  CG2 . ILE D  1 306 ? 26.568  -46.379 -27.632 1.00 25.69 ? 323  ILE D CG2 1 
ATOM   15721 C  CD1 . ILE D  1 306 ? 25.169  -43.722 -28.386 1.00 25.54 ? 323  ILE D CD1 1 
ATOM   15722 N  N   . VAL D  1 307 ? 29.475  -45.917 -25.502 1.00 24.64 ? 324  VAL D N   1 
ATOM   15723 C  CA  . VAL D  1 307 ? 30.625  -46.805 -25.472 1.00 26.29 ? 324  VAL D CA  1 
ATOM   15724 C  C   . VAL D  1 307 ? 30.752  -47.433 -24.085 1.00 27.09 ? 324  VAL D C   1 
ATOM   15725 O  O   . VAL D  1 307 ? 30.993  -48.633 -23.977 1.00 26.68 ? 324  VAL D O   1 
ATOM   15726 C  CB  . VAL D  1 307 ? 31.911  -46.068 -25.887 1.00 27.10 ? 324  VAL D CB  1 
ATOM   15727 C  CG1 . VAL D  1 307 ? 33.158  -46.910 -25.639 1.00 29.24 ? 324  VAL D CG1 1 
ATOM   15728 C  CG2 . VAL D  1 307 ? 31.855  -45.633 -27.346 1.00 28.67 ? 324  VAL D CG2 1 
ATOM   15729 N  N   . MET D  1 308 ? 30.573  -46.626 -23.029 1.00 26.39 ? 325  MET D N   1 
ATOM   15730 C  CA  . MET D  1 308 ? 30.641  -47.131 -21.665 1.00 26.83 ? 325  MET D CA  1 
ATOM   15731 C  C   . MET D  1 308 ? 29.549  -48.174 -21.423 1.00 25.79 ? 325  MET D C   1 
ATOM   15732 O  O   . MET D  1 308 ? 29.797  -49.189 -20.776 1.00 25.39 ? 325  MET D O   1 
ATOM   15733 C  CB  . MET D  1 308 ? 30.527  -45.992 -20.647 1.00 27.67 ? 325  MET D CB  1 
ATOM   15734 C  CG  . MET D  1 308 ? 31.738  -45.084 -20.620 1.00 28.82 ? 325  MET D CG  1 
ATOM   15735 S  SD  . MET D  1 308 ? 31.596  -43.741 -19.421 1.00 31.86 ? 325  MET D SD  1 
ATOM   15736 C  CE  . MET D  1 308 ? 31.439  -44.711 -17.915 1.00 32.32 ? 325  MET D CE  1 
ATOM   15737 N  N   . SER D  1 309 ? 28.349  -47.934 -21.963 1.00 25.20 ? 326  SER D N   1 
ATOM   15738 C  CA  . SER D  1 309 ? 27.242  -48.866 -21.819 1.00 27.29 ? 326  SER D CA  1 
ATOM   15739 C  C   . SER D  1 309 ? 27.562  -50.193 -22.516 1.00 28.38 ? 326  SER D C   1 
ATOM   15740 O  O   . SER D  1 309 ? 27.287  -51.266 -21.979 1.00 27.88 ? 326  SER D O   1 
ATOM   15741 C  CB  . SER D  1 309 ? 25.968  -48.262 -22.341 1.00 26.82 ? 326  SER D CB  1 
ATOM   15742 O  OG  . SER D  1 309 ? 24.890  -49.188 -22.319 1.00 28.36 ? 326  SER D OG  1 
ATOM   15743 N  N   . MET D  1 310 ? 28.152  -50.111 -23.714 1.00 28.14 ? 327  MET D N   1 
ATOM   15744 C  CA  . MET D  1 310 ? 28.510  -51.298 -24.478 1.00 29.86 ? 327  MET D CA  1 
ATOM   15745 C  C   . MET D  1 310 ? 29.591  -52.093 -23.744 1.00 30.73 ? 327  MET D C   1 
ATOM   15746 O  O   . MET D  1 310 ? 29.513  -53.319 -23.674 1.00 31.13 ? 327  MET D O   1 
ATOM   15747 C  CB  . MET D  1 310 ? 28.983  -50.922 -25.888 1.00 30.47 ? 327  MET D CB  1 
ATOM   15748 C  CG  . MET D  1 310 ? 27.855  -50.481 -26.807 1.00 32.12 ? 327  MET D CG  1 
ATOM   15749 S  SD  . MET D  1 310 ? 28.421  -49.977 -28.446 1.00 33.64 ? 327  MET D SD  1 
ATOM   15750 C  CE  . MET D  1 310 ? 26.856  -49.648 -29.264 1.00 35.05 ? 327  MET D CE  1 
ATOM   15751 N  N   . VAL D  1 311 ? 30.585  -51.385 -23.187 1.00 31.22 ? 328  VAL D N   1 
ATOM   15752 C  CA  . VAL D  1 311 ? 31.718  -52.023 -22.530 1.00 31.29 ? 328  VAL D CA  1 
ATOM   15753 C  C   . VAL D  1 311 ? 31.250  -52.808 -21.302 1.00 31.97 ? 328  VAL D C   1 
ATOM   15754 O  O   . VAL D  1 311 ? 31.762  -53.899 -21.046 1.00 29.88 ? 328  VAL D O   1 
ATOM   15755 C  CB  . VAL D  1 311 ? 32.815  -51.000 -22.173 1.00 32.26 ? 328  VAL D CB  1 
ATOM   15756 C  CG1 . VAL D  1 311 ? 33.814  -51.542 -21.153 1.00 31.84 ? 328  VAL D CG1 1 
ATOM   15757 C  CG2 . VAL D  1 311 ? 33.548  -50.513 -23.419 1.00 32.20 ? 328  VAL D CG2 1 
ATOM   15758 N  N   . GLU D  1 312 ? 30.267  -52.276 -20.559 1.00 31.72 ? 329  GLU D N   1 
ATOM   15759 C  CA  . GLU D  1 312 ? 29.837  -52.914 -19.323 1.00 34.16 ? 329  GLU D CA  1 
ATOM   15760 C  C   . GLU D  1 312 ? 29.054  -54.186 -19.654 1.00 33.95 ? 329  GLU D C   1 
ATOM   15761 O  O   . GLU D  1 312 ? 28.958  -55.075 -18.812 1.00 35.18 ? 329  GLU D O   1 
ATOM   15762 C  CB  . GLU D  1 312 ? 29.121  -51.955 -18.361 1.00 35.57 ? 329  GLU D CB  1 
ATOM   15763 C  CG  . GLU D  1 312 ? 27.650  -51.678 -18.663 1.00 37.90 ? 329  GLU D CG  1 
ATOM   15764 C  CD  . GLU D  1 312 ? 26.889  -50.929 -17.571 1.00 39.91 ? 329  GLU D CD  1 
ATOM   15765 O  OE1 . GLU D  1 312 ? 27.456  -50.640 -16.491 1.00 36.91 ? 329  GLU D OE1 1 
ATOM   15766 O  OE2 . GLU D  1 312 ? 25.697  -50.619 -17.807 1.00 42.55 ? 329  GLU D OE2 1 
ATOM   15767 N  N   . ASN D  1 313 ? 28.529  -54.270 -20.886 1.00 34.40 ? 330  ASN D N   1 
ATOM   15768 C  CA  . ASN D  1 313 ? 27.794  -55.433 -21.363 1.00 34.44 ? 330  ASN D CA  1 
ATOM   15769 C  C   . ASN D  1 313 ? 28.724  -56.481 -21.974 1.00 34.55 ? 330  ASN D C   1 
ATOM   15770 O  O   . ASN D  1 313 ? 28.270  -57.582 -22.281 1.00 34.64 ? 330  ASN D O   1 
ATOM   15771 C  CB  . ASN D  1 313 ? 26.714  -55.039 -22.364 1.00 34.65 ? 330  ASN D CB  1 
ATOM   15772 C  CG  . ASN D  1 313 ? 25.465  -54.555 -21.670 1.00 37.51 ? 330  ASN D CG  1 
ATOM   15773 O  OD1 . ASN D  1 313 ? 24.693  -55.367 -21.147 1.00 38.88 ? 330  ASN D OD1 1 
ATOM   15774 N  ND2 . ASN D  1 313 ? 25.243  -53.250 -21.662 1.00 38.53 ? 330  ASN D ND2 1 
ATOM   15775 N  N   . GLY D  1 314 ? 30.002  -56.133 -22.173 1.00 34.52 ? 331  GLY D N   1 
ATOM   15776 C  CA  . GLY D  1 314 ? 31.034  -57.118 -22.458 1.00 36.36 ? 331  GLY D CA  1 
ATOM   15777 C  C   . GLY D  1 314 ? 31.767  -56.899 -23.785 1.00 37.83 ? 331  GLY D C   1 
ATOM   15778 O  O   . GLY D  1 314 ? 32.538  -57.763 -24.194 1.00 38.92 ? 331  GLY D O   1 
ATOM   15779 N  N   . LEU D  1 315 ? 31.539  -55.760 -24.454 1.00 38.57 ? 332  LEU D N   1 
ATOM   15780 C  CA  . LEU D  1 315 ? 32.338  -55.378 -25.610 1.00 39.52 ? 332  LEU D CA  1 
ATOM   15781 C  C   . LEU D  1 315 ? 33.615  -54.714 -25.111 1.00 41.17 ? 332  LEU D C   1 
ATOM   15782 O  O   . LEU D  1 315 ? 33.628  -54.142 -24.024 1.00 42.71 ? 332  LEU D O   1 
ATOM   15783 C  CB  . LEU D  1 315 ? 31.596  -54.421 -26.543 1.00 38.90 ? 332  LEU D CB  1 
ATOM   15784 C  CG  . LEU D  1 315 ? 30.451  -55.001 -27.376 1.00 39.89 ? 332  LEU D CG  1 
ATOM   15785 C  CD1 . LEU D  1 315 ? 29.227  -55.301 -26.530 1.00 41.51 ? 332  LEU D CD1 1 
ATOM   15786 C  CD2 . LEU D  1 315 ? 30.097  -54.034 -28.495 1.00 39.45 ? 332  LEU D CD2 1 
ATOM   15787 N  N   . SER D  1 316 ? 34.679  -54.773 -25.920 1.00 42.04 ? 333  SER D N   1 
ATOM   15788 C  CA  . SER D  1 316 ? 35.857  -53.956 -25.679 1.00 42.27 ? 333  SER D CA  1 
ATOM   15789 C  C   . SER D  1 316 ? 35.571  -52.521 -26.114 1.00 40.64 ? 333  SER D C   1 
ATOM   15790 O  O   . SER D  1 316 ? 34.683  -52.272 -26.928 1.00 40.04 ? 333  SER D O   1 
ATOM   15791 C  CB  . SER D  1 316 ? 37.085  -54.504 -26.376 1.00 43.38 ? 333  SER D CB  1 
ATOM   15792 O  OG  . SER D  1 316 ? 37.079  -54.190 -27.761 1.00 44.78 ? 333  SER D OG  1 
ATOM   15793 N  N   . GLU D  1 317 ? 36.346  -51.585 -25.564 1.00 42.32 ? 334  GLU D N   1 
ATOM   15794 C  CA  . GLU D  1 317 ? 36.218  -50.173 -25.884 1.00 44.26 ? 334  GLU D CA  1 
ATOM   15795 C  C   . GLU D  1 317 ? 36.384  -49.967 -27.389 1.00 44.84 ? 334  GLU D C   1 
ATOM   15796 O  O   . GLU D  1 317 ? 35.591  -49.265 -28.012 1.00 41.86 ? 334  GLU D O   1 
ATOM   15797 C  CB  . GLU D  1 317 ? 37.265  -49.392 -25.089 1.00 45.07 ? 334  GLU D CB  1 
ATOM   15798 C  CG  . GLU D  1 317 ? 37.097  -47.877 -25.167 1.00 46.98 ? 334  GLU D CG  1 
ATOM   15799 C  CD  . GLU D  1 317 ? 38.008  -47.120 -24.218 1.00 49.01 ? 334  GLU D CD  1 
ATOM   15800 O  OE1 . GLU D  1 317 ? 39.236  -47.113 -24.446 1.00 51.39 ? 334  GLU D OE1 1 
ATOM   15801 O  OE2 . GLU D  1 317 ? 37.488  -46.550 -23.238 1.00 50.08 ? 334  GLU D OE2 1 
ATOM   15802 N  N   . GLN D  1 318 ? 37.413  -50.602 -27.962 1.00 47.76 ? 335  GLN D N   1 
ATOM   15803 C  CA  . GLN D  1 318 ? 37.776  -50.401 -29.357 1.00 52.35 ? 335  GLN D CA  1 
ATOM   15804 C  C   . GLN D  1 318 ? 36.644  -50.852 -30.281 1.00 49.18 ? 335  GLN D C   1 
ATOM   15805 O  O   . GLN D  1 318 ? 36.309  -50.148 -31.231 1.00 47.96 ? 335  GLN D O   1 
ATOM   15806 C  CB  . GLN D  1 318 ? 39.084  -51.128 -29.675 1.00 57.78 ? 335  GLN D CB  1 
ATOM   15807 C  CG  . GLN D  1 318 ? 39.687  -50.763 -31.027 1.00 62.35 ? 335  GLN D CG  1 
ATOM   15808 C  CD  . GLN D  1 318 ? 41.013  -51.444 -31.298 1.00 67.40 ? 335  GLN D CD  1 
ATOM   15809 O  OE1 . GLN D  1 318 ? 41.575  -52.140 -30.443 1.00 68.51 ? 335  GLN D OE1 1 
ATOM   15810 N  NE2 . GLN D  1 318 ? 41.532  -51.242 -32.502 1.00 68.91 ? 335  GLN D NE2 1 
ATOM   15811 N  N   . GLU D  1 319 ? 36.049  -52.018 -30.002 1.00 49.08 ? 336  GLU D N   1 
ATOM   15812 C  CA  . GLU D  1 319 ? 35.020  -52.557 -30.878 1.00 49.99 ? 336  GLU D CA  1 
ATOM   15813 C  C   . GLU D  1 319 ? 33.708  -51.793 -30.688 1.00 46.94 ? 336  GLU D C   1 
ATOM   15814 O  O   . GLU D  1 319 ? 32.922  -51.688 -31.628 1.00 45.44 ? 336  GLU D O   1 
ATOM   15815 C  CB  . GLU D  1 319 ? 34.884  -54.074 -30.736 1.00 54.16 ? 336  GLU D CB  1 
ATOM   15816 C  CG  . GLU D  1 319 ? 34.288  -54.552 -29.416 1.00 59.14 ? 336  GLU D CG  1 
ATOM   15817 C  CD  . GLU D  1 319 ? 34.497  -56.040 -29.185 1.00 64.86 ? 336  GLU D CD  1 
ATOM   15818 O  OE1 . GLU D  1 319 ? 33.501  -56.795 -29.135 1.00 68.43 ? 336  GLU D OE1 1 
ATOM   15819 O  OE2 . GLU D  1 319 ? 35.673  -56.443 -29.051 1.00 69.35 ? 336  GLU D OE2 1 
ATOM   15820 N  N   . ALA D  1 320 ? 33.478  -51.241 -29.488 1.00 43.02 ? 337  ALA D N   1 
ATOM   15821 C  CA  . ALA D  1 320 ? 32.300  -50.419 -29.244 1.00 40.75 ? 337  ALA D CA  1 
ATOM   15822 C  C   . ALA D  1 320 ? 32.369  -49.136 -30.074 1.00 38.06 ? 337  ALA D C   1 
ATOM   15823 O  O   . ALA D  1 320 ? 31.380  -48.730 -30.679 1.00 36.79 ? 337  ALA D O   1 
ATOM   15824 C  CB  . ALA D  1 320 ? 32.167  -50.123 -27.764 1.00 40.60 ? 337  ALA D CB  1 
ATOM   15825 N  N   . GLN D  1 321 ? 33.550  -48.511 -30.104 1.00 39.06 ? 338  GLN D N   1 
ATOM   15826 C  CA  . GLN D  1 321 ? 33.757  -47.262 -30.822 1.00 41.11 ? 338  GLN D CA  1 
ATOM   15827 C  C   . GLN D  1 321 ? 33.578  -47.464 -32.327 1.00 42.83 ? 338  GLN D C   1 
ATOM   15828 O  O   . GLN D  1 321 ? 33.056  -46.583 -33.012 1.00 43.29 ? 338  GLN D O   1 
ATOM   15829 C  CB  . GLN D  1 321 ? 35.151  -46.721 -30.510 1.00 42.70 ? 338  GLN D CB  1 
ATOM   15830 C  CG  . GLN D  1 321 ? 35.302  -46.198 -29.086 1.00 42.79 ? 338  GLN D CG  1 
ATOM   15831 C  CD  . GLN D  1 321 ? 36.739  -45.936 -28.699 1.00 43.24 ? 338  GLN D CD  1 
ATOM   15832 O  OE1 . GLN D  1 321 ? 37.679  -46.356 -29.384 1.00 45.10 ? 338  GLN D OE1 1 
ATOM   15833 N  NE2 . GLN D  1 321 ? 36.925  -45.243 -27.586 1.00 43.06 ? 338  GLN D NE2 1 
ATOM   15834 N  N   . LYS D  1 322 ? 33.994  -48.637 -32.825 1.00 42.04 ? 339  LYS D N   1 
ATOM   15835 C  CA  . LYS D  1 322 ? 33.902  -48.965 -34.241 1.00 43.86 ? 339  LYS D CA  1 
ATOM   15836 C  C   . LYS D  1 322 ? 32.444  -49.031 -34.698 1.00 44.69 ? 339  LYS D C   1 
ATOM   15837 O  O   . LYS D  1 322 ? 32.182  -49.007 -35.898 1.00 47.67 ? 339  LYS D O   1 
ATOM   15838 C  CB  . LYS D  1 322 ? 34.612  -50.287 -34.556 1.00 44.26 ? 339  LYS D CB  1 
ATOM   15839 N  N   . LYS D  1 323 ? 31.498  -49.105 -33.752 1.00 43.36 ? 340  LYS D N   1 
ATOM   15840 C  CA  . LYS D  1 323 ? 30.085  -49.190 -34.092 1.00 42.56 ? 340  LYS D CA  1 
ATOM   15841 C  C   . LYS D  1 323 ? 29.450  -47.803 -34.177 1.00 40.15 ? 340  LYS D C   1 
ATOM   15842 O  O   . LYS D  1 323 ? 28.250  -47.693 -34.423 1.00 41.15 ? 340  LYS D O   1 
ATOM   15843 C  CB  . LYS D  1 323 ? 29.367  -50.088 -33.079 1.00 44.46 ? 340  LYS D CB  1 
ATOM   15844 C  CG  . LYS D  1 323 ? 29.884  -51.518 -33.095 1.00 46.58 ? 340  LYS D CG  1 
ATOM   15845 C  CD  . LYS D  1 323 ? 29.115  -52.504 -32.228 1.00 47.95 ? 340  LYS D CD  1 
ATOM   15846 C  CE  . LYS D  1 323 ? 29.811  -53.828 -32.161 1.00 49.20 ? 340  LYS D CE  1 
ATOM   15847 N  NZ  . LYS D  1 323 ? 29.854  -54.509 -33.458 1.00 50.94 ? 340  LYS D NZ  1 
ATOM   15848 N  N   . ILE D  1 324 ? 30.254  -46.746 -33.999 1.00 39.94 ? 341  ILE D N   1 
ATOM   15849 C  CA  . ILE D  1 324 ? 29.739  -45.387 -33.987 1.00 38.98 ? 341  ILE D CA  1 
ATOM   15850 C  C   . ILE D  1 324 ? 30.406  -44.583 -35.103 1.00 38.64 ? 341  ILE D C   1 
ATOM   15851 O  O   . ILE D  1 324 ? 31.631  -44.517 -35.172 1.00 37.10 ? 341  ILE D O   1 
ATOM   15852 C  CB  . ILE D  1 324 ? 29.938  -44.747 -32.599 1.00 37.95 ? 341  ILE D CB  1 
ATOM   15853 C  CG1 . ILE D  1 324 ? 29.056  -45.435 -31.548 1.00 39.38 ? 341  ILE D CG1 1 
ATOM   15854 C  CG2 . ILE D  1 324 ? 29.684  -43.240 -32.647 1.00 37.67 ? 341  ILE D CG2 1 
ATOM   15855 C  CD1 . ILE D  1 324 ? 29.402  -45.090 -30.111 1.00 40.18 ? 341  ILE D CD1 1 
ATOM   15856 N  N   . TRP D  1 325 ? 29.568  -43.974 -35.954 1.00 41.22 ? 342  TRP D N   1 
ATOM   15857 C  CA  . TRP D  1 325 ? 30.004  -43.110 -37.043 1.00 43.86 ? 342  TRP D CA  1 
ATOM   15858 C  C   . TRP D  1 325 ? 29.395  -41.722 -36.864 1.00 43.06 ? 342  TRP D C   1 
ATOM   15859 O  O   . TRP D  1 325 ? 28.300  -41.592 -36.316 1.00 40.71 ? 342  TRP D O   1 
ATOM   15860 C  CB  . TRP D  1 325 ? 29.586  -43.700 -38.401 1.00 46.50 ? 342  TRP D CB  1 
ATOM   15861 C  CG  . TRP D  1 325 ? 30.198  -45.039 -38.721 1.00 48.76 ? 342  TRP D CG  1 
ATOM   15862 C  CD1 . TRP D  1 325 ? 29.798  -46.259 -38.260 1.00 50.48 ? 342  TRP D CD1 1 
ATOM   15863 C  CD2 . TRP D  1 325 ? 31.314  -45.291 -39.602 1.00 51.48 ? 342  TRP D CD2 1 
ATOM   15864 N  NE1 . TRP D  1 325 ? 30.594  -47.248 -38.772 1.00 50.38 ? 342  TRP D NE1 1 
ATOM   15865 C  CE2 . TRP D  1 325 ? 31.531  -46.687 -39.600 1.00 51.80 ? 342  TRP D CE2 1 
ATOM   15866 C  CE3 . TRP D  1 325 ? 32.149  -44.480 -40.380 1.00 52.51 ? 342  TRP D CE3 1 
ATOM   15867 C  CZ2 . TRP D  1 325 ? 32.545  -47.282 -40.347 1.00 53.59 ? 342  TRP D CZ2 1 
ATOM   15868 C  CZ3 . TRP D  1 325 ? 33.149  -45.072 -41.122 1.00 52.85 ? 342  TRP D CZ3 1 
ATOM   15869 C  CH2 . TRP D  1 325 ? 33.344  -46.454 -41.103 1.00 53.61 ? 342  TRP D CH2 1 
ATOM   15870 N  N   . MET D  1 326 ? 30.095  -40.693 -37.364 1.00 43.76 ? 343  MET D N   1 
ATOM   15871 C  CA  . MET D  1 326 ? 29.618  -39.323 -37.255 1.00 45.52 ? 343  MET D CA  1 
ATOM   15872 C  C   . MET D  1 326 ? 29.712  -38.621 -38.610 1.00 47.44 ? 343  MET D C   1 
ATOM   15873 O  O   . MET D  1 326 ? 30.634  -38.867 -39.387 1.00 45.55 ? 343  MET D O   1 
ATOM   15874 C  CB  . MET D  1 326 ? 30.417  -38.547 -36.201 1.00 46.48 ? 343  MET D CB  1 
ATOM   15875 C  CG  . MET D  1 326 ? 30.370  -39.172 -34.817 1.00 45.93 ? 343  MET D CG  1 
ATOM   15876 S  SD  . MET D  1 326 ? 31.044  -38.110 -33.523 1.00 43.81 ? 343  MET D SD  1 
ATOM   15877 C  CE  . MET D  1 326 ? 30.765  -39.180 -32.104 1.00 44.06 ? 343  MET D CE  1 
ATOM   15878 N  N   . PHE D  1 327 ? 28.744  -37.730 -38.865 1.00 48.80 ? 344  PHE D N   1 
ATOM   15879 C  CA  . PHE D  1 327 ? 28.650  -37.002 -40.119 1.00 50.94 ? 344  PHE D CA  1 
ATOM   15880 C  C   . PHE D  1 327 ? 28.274  -35.552 -39.821 1.00 50.32 ? 344  PHE D C   1 
ATOM   15881 O  O   . PHE D  1 327 ? 27.120  -35.265 -39.502 1.00 49.15 ? 344  PHE D O   1 
ATOM   15882 C  CB  . PHE D  1 327 ? 27.622  -37.698 -41.019 1.00 52.71 ? 344  PHE D CB  1 
ATOM   15883 C  CG  . PHE D  1 327 ? 27.541  -37.160 -42.442 1.00 54.80 ? 344  PHE D CG  1 
ATOM   15884 C  CD1 . PHE D  1 327 ? 26.788  -36.027 -42.739 1.00 55.41 ? 344  PHE D CD1 1 
ATOM   15885 C  CD2 . PHE D  1 327 ? 28.209  -37.798 -43.484 1.00 54.16 ? 344  PHE D CD2 1 
ATOM   15886 C  CE1 . PHE D  1 327 ? 26.716  -35.543 -44.038 1.00 55.62 ? 344  PHE D CE1 1 
ATOM   15887 C  CE2 . PHE D  1 327 ? 28.135  -37.310 -44.780 1.00 54.01 ? 344  PHE D CE2 1 
ATOM   15888 C  CZ  . PHE D  1 327 ? 27.387  -36.187 -45.055 1.00 54.21 ? 344  PHE D CZ  1 
ATOM   15889 N  N   . ASP D  1 328 ? 29.257  -34.650 -39.946 1.00 53.53 ? 345  ASP D N   1 
ATOM   15890 C  CA  . ASP D  1 328 ? 29.096  -33.255 -39.563 1.00 57.34 ? 345  ASP D CA  1 
ATOM   15891 C  C   . ASP D  1 328 ? 28.711  -32.430 -40.793 1.00 61.68 ? 345  ASP D C   1 
ATOM   15892 O  O   . ASP D  1 328 ? 28.203  -32.974 -41.771 1.00 61.62 ? 345  ASP D O   1 
ATOM   15893 C  CB  . ASP D  1 328 ? 30.337  -32.765 -38.829 1.00 58.17 ? 345  ASP D CB  1 
ATOM   15894 C  CG  . ASP D  1 328 ? 31.603  -32.633 -39.664 1.00 59.47 ? 345  ASP D CG  1 
ATOM   15895 O  OD1 . ASP D  1 328 ? 31.548  -32.937 -40.875 1.00 59.16 ? 345  ASP D OD1 1 
ATOM   15896 O  OD2 . ASP D  1 328 ? 32.639  -32.226 -39.097 1.00 59.20 ? 345  ASP D OD2 1 
ATOM   15897 N  N   . LYS D  1 329 ? 28.940  -31.109 -40.724 1.00 64.13 ? 346  LYS D N   1 
ATOM   15898 C  CA  . LYS D  1 329 ? 28.624  -30.193 -41.811 1.00 65.40 ? 346  LYS D CA  1 
ATOM   15899 C  C   . LYS D  1 329 ? 29.604  -30.366 -42.972 1.00 65.84 ? 346  LYS D C   1 
ATOM   15900 O  O   . LYS D  1 329 ? 29.278  -30.021 -44.106 1.00 67.37 ? 346  LYS D O   1 
ATOM   15901 C  CB  . LYS D  1 329 ? 28.640  -28.745 -41.306 1.00 64.62 ? 346  LYS D CB  1 
ATOM   15902 N  N   . TYR D  1 330 ? 30.796  -30.905 -42.687 1.00 66.83 ? 347  TYR D N   1 
ATOM   15903 C  CA  . TYR D  1 330 ? 31.838  -31.067 -43.689 1.00 69.29 ? 347  TYR D CA  1 
ATOM   15904 C  C   . TYR D  1 330 ? 31.889  -32.513 -44.186 1.00 71.36 ? 347  TYR D C   1 
ATOM   15905 O  O   . TYR D  1 330 ? 32.946  -32.982 -44.604 1.00 73.25 ? 347  TYR D O   1 
ATOM   15906 C  CB  . TYR D  1 330 ? 33.176  -30.642 -43.075 1.00 72.75 ? 347  TYR D CB  1 
ATOM   15907 C  CG  . TYR D  1 330 ? 33.226  -29.219 -42.533 1.00 74.92 ? 347  TYR D CG  1 
ATOM   15908 C  CD1 . TYR D  1 330 ? 32.684  -28.901 -41.291 1.00 75.71 ? 347  TYR D CD1 1 
ATOM   15909 C  CD2 . TYR D  1 330 ? 33.843  -28.199 -43.249 1.00 75.38 ? 347  TYR D CD2 1 
ATOM   15910 C  CE1 . TYR D  1 330 ? 32.736  -27.611 -40.788 1.00 76.02 ? 347  TYR D CE1 1 
ATOM   15911 C  CE2 . TYR D  1 330 ? 33.903  -26.905 -42.756 1.00 76.14 ? 347  TYR D CE2 1 
ATOM   15912 C  CZ  . TYR D  1 330 ? 33.348  -26.610 -41.522 1.00 77.30 ? 347  TYR D CZ  1 
ATOM   15913 O  OH  . TYR D  1 330 ? 33.402  -25.338 -41.030 1.00 79.13 ? 347  TYR D OH  1 
ATOM   15914 N  N   . GLY D  1 331 ? 30.747  -33.213 -44.143 1.00 71.70 ? 348  GLY D N   1 
ATOM   15915 C  CA  . GLY D  1 331 ? 30.656  -34.577 -44.643 1.00 70.74 ? 348  GLY D CA  1 
ATOM   15916 C  C   . GLY D  1 331 ? 30.929  -35.610 -43.550 1.00 70.61 ? 348  GLY D C   1 
ATOM   15917 O  O   . GLY D  1 331 ? 30.793  -35.317 -42.362 1.00 70.07 ? 348  GLY D O   1 
ATOM   15918 N  N   . LEU D  1 332 ? 31.311  -36.823 -43.975 1.00 65.47 ? 349  LEU D N   1 
ATOM   15919 C  CA  . LEU D  1 332 ? 31.528  -37.938 -43.067 1.00 64.13 ? 349  LEU D CA  1 
ATOM   15920 C  C   . LEU D  1 332 ? 32.900  -37.792 -42.420 1.00 64.89 ? 349  LEU D C   1 
ATOM   15921 O  O   . LEU D  1 332 ? 33.855  -37.385 -43.077 1.00 65.65 ? 349  LEU D O   1 
ATOM   15922 C  CB  . LEU D  1 332 ? 31.418  -39.271 -43.808 1.00 62.15 ? 349  LEU D CB  1 
ATOM   15923 C  CG  . LEU D  1 332 ? 31.435  -40.533 -42.936 1.00 61.60 ? 349  LEU D CG  1 
ATOM   15924 C  CD1 . LEU D  1 332 ? 30.089  -40.744 -42.262 1.00 61.84 ? 349  LEU D CD1 1 
ATOM   15925 C  CD2 . LEU D  1 332 ? 31.832  -41.768 -43.729 1.00 60.07 ? 349  LEU D CD2 1 
ATOM   15926 N  N   . LEU D  1 333 ? 32.983  -38.141 -41.130 1.00 65.32 ? 350  LEU D N   1 
ATOM   15927 C  CA  . LEU D  1 333 ? 34.252  -38.183 -40.423 1.00 64.69 ? 350  LEU D CA  1 
ATOM   15928 C  C   . LEU D  1 333 ? 34.938  -39.514 -40.731 1.00 64.09 ? 350  LEU D C   1 
ATOM   15929 O  O   . LEU D  1 333 ? 34.537  -40.557 -40.217 1.00 64.34 ? 350  LEU D O   1 
ATOM   15930 C  CB  . LEU D  1 333 ? 34.047  -37.978 -38.921 1.00 64.78 ? 350  LEU D CB  1 
ATOM   15931 C  CG  . LEU D  1 333 ? 33.812  -36.538 -38.450 1.00 64.07 ? 350  LEU D CG  1 
ATOM   15932 C  CD1 . LEU D  1 333 ? 32.407  -36.037 -38.761 1.00 62.83 ? 350  LEU D CD1 1 
ATOM   15933 C  CD2 . LEU D  1 333 ? 34.098  -36.411 -36.962 1.00 64.77 ? 350  LEU D CD2 1 
ATOM   15934 N  N   . VAL D  1 334 ? 35.960  -39.461 -41.594 1.00 63.93 ? 351  VAL D N   1 
ATOM   15935 C  CA  . VAL D  1 334 ? 36.749  -40.629 -41.954 1.00 63.39 ? 351  VAL D CA  1 
ATOM   15936 C  C   . VAL D  1 334 ? 38.224  -40.242 -41.909 1.00 65.01 ? 351  VAL D C   1 
ATOM   15937 O  O   . VAL D  1 334 ? 38.557  -39.064 -42.023 1.00 65.46 ? 351  VAL D O   1 
ATOM   15938 C  CB  . VAL D  1 334 ? 36.355  -41.174 -43.340 1.00 61.54 ? 351  VAL D CB  1 
ATOM   15939 N  N   . LYS D  1 335 ? 39.098  -41.243 -41.742 1.00 68.11 ? 352  LYS D N   1 
ATOM   15940 C  CA  . LYS D  1 335 ? 40.526  -41.002 -41.598 1.00 70.59 ? 352  LYS D CA  1 
ATOM   15941 C  C   . LYS D  1 335 ? 41.084  -40.404 -42.889 1.00 74.71 ? 352  LYS D C   1 
ATOM   15942 O  O   . LYS D  1 335 ? 40.909  -40.968 -43.968 1.00 74.63 ? 352  LYS D O   1 
ATOM   15943 C  CB  . LYS D  1 335 ? 41.298  -42.271 -41.209 1.00 70.43 ? 352  LYS D CB  1 
ATOM   15944 C  CG  . LYS D  1 335 ? 41.363  -42.557 -39.712 1.00 71.44 ? 352  LYS D CG  1 
ATOM   15945 C  CD  . LYS D  1 335 ? 42.462  -43.532 -39.302 1.00 71.89 ? 352  LYS D CD  1 
ATOM   15946 C  CE  . LYS D  1 335 ? 42.140  -44.968 -39.572 1.00 73.40 ? 352  LYS D CE  1 
ATOM   15947 N  NZ  . LYS D  1 335 ? 41.230  -45.525 -38.568 1.00 73.60 ? 352  LYS D NZ  1 
ATOM   15948 N  N   . GLY D  1 336 ? 41.753  -39.252 -42.754 1.00 75.50 ? 353  GLY D N   1 
ATOM   15949 C  CA  . GLY D  1 336 ? 42.409  -38.588 -43.869 1.00 75.06 ? 353  GLY D CA  1 
ATOM   15950 C  C   . GLY D  1 336 ? 41.413  -37.833 -44.744 1.00 76.41 ? 353  GLY D C   1 
ATOM   15951 O  O   . GLY D  1 336 ? 41.447  -37.959 -45.965 1.00 79.72 ? 353  GLY D O   1 
ATOM   15952 N  N   . ARG D  1 337 ? 40.531  -37.051 -44.106 1.00 76.73 ? 354  ARG D N   1 
ATOM   15953 C  CA  . ARG D  1 337 ? 39.583  -36.207 -44.817 1.00 76.19 ? 354  ARG D CA  1 
ATOM   15954 C  C   . ARG D  1 337 ? 40.132  -34.781 -44.861 1.00 77.40 ? 354  ARG D C   1 
ATOM   15955 O  O   . ARG D  1 337 ? 41.232  -34.521 -44.380 1.00 78.95 ? 354  ARG D O   1 
ATOM   15956 C  CB  . ARG D  1 337 ? 38.186  -36.295 -44.184 1.00 73.86 ? 354  ARG D CB  1 
ATOM   15957 C  CG  . ARG D  1 337 ? 37.995  -35.600 -42.842 1.00 71.57 ? 354  ARG D CG  1 
ATOM   15958 C  CD  . ARG D  1 337 ? 36.518  -35.436 -42.508 1.00 69.68 ? 354  ARG D CD  1 
ATOM   15959 N  NE  . ARG D  1 337 ? 36.288  -34.494 -41.407 1.00 67.21 ? 354  ARG D NE  1 
ATOM   15960 C  CZ  . ARG D  1 337 ? 35.105  -34.018 -41.025 1.00 66.20 ? 354  ARG D CZ  1 
ATOM   15961 N  NH1 . ARG D  1 337 ? 33.995  -34.388 -41.642 1.00 65.26 ? 354  ARG D NH1 1 
ATOM   15962 N  NH2 . ARG D  1 337 ? 35.041  -33.156 -40.026 1.00 66.96 ? 354  ARG D NH2 1 
ATOM   15963 N  N   . LYS D  1 338 ? 39.354  -33.865 -45.450 1.00 78.15 ? 355  LYS D N   1 
ATOM   15964 C  CA  . LYS D  1 338 ? 39.776  -32.484 -45.624 1.00 78.58 ? 355  LYS D CA  1 
ATOM   15965 C  C   . LYS D  1 338 ? 39.615  -31.717 -44.314 1.00 78.92 ? 355  LYS D C   1 
ATOM   15966 O  O   . LYS D  1 338 ? 40.550  -31.060 -43.861 1.00 77.01 ? 355  LYS D O   1 
ATOM   15967 C  CB  . LYS D  1 338 ? 38.968  -31.813 -46.742 1.00 78.38 ? 355  LYS D CB  1 
ATOM   15968 N  N   . ALA D  1 339 ? 38.419  -31.810 -43.717 1.00 80.66 ? 356  ALA D N   1 
ATOM   15969 C  CA  . ALA D  1 339 ? 38.053  -30.990 -42.572 1.00 80.94 ? 356  ALA D CA  1 
ATOM   15970 C  C   . ALA D  1 339 ? 38.793  -31.450 -41.316 1.00 80.71 ? 356  ALA D C   1 
ATOM   15971 O  O   . ALA D  1 339 ? 39.391  -32.525 -41.296 1.00 79.35 ? 356  ALA D O   1 
ATOM   15972 C  CB  . ALA D  1 339 ? 36.552  -31.016 -42.381 1.00 79.90 ? 356  ALA D CB  1 
ATOM   15973 N  N   . LYS D  1 340 ? 38.734  -30.611 -40.272 1.00 80.53 ? 357  LYS D N   1 
ATOM   15974 C  CA  . LYS D  1 340 ? 39.522  -30.796 -39.062 1.00 79.92 ? 357  LYS D CA  1 
ATOM   15975 C  C   . LYS D  1 340 ? 38.946  -31.933 -38.220 1.00 78.58 ? 357  LYS D C   1 
ATOM   15976 O  O   . LYS D  1 340 ? 37.735  -32.011 -38.019 1.00 75.82 ? 357  LYS D O   1 
ATOM   15977 C  CB  . LYS D  1 340 ? 39.560  -29.499 -38.244 1.00 78.94 ? 357  LYS D CB  1 
ATOM   15978 N  N   . ILE D  1 341 ? 39.845  -32.796 -37.728 1.00 78.71 ? 358  ILE D N   1 
ATOM   15979 C  CA  . ILE D  1 341 ? 39.501  -33.899 -36.844 1.00 79.11 ? 358  ILE D CA  1 
ATOM   15980 C  C   . ILE D  1 341 ? 40.341  -33.774 -35.575 1.00 79.19 ? 358  ILE D C   1 
ATOM   15981 O  O   . ILE D  1 341 ? 41.537  -34.057 -35.598 1.00 80.78 ? 358  ILE D O   1 
ATOM   15982 C  CB  . ILE D  1 341 ? 39.736  -35.251 -37.547 1.00 78.60 ? 358  ILE D CB  1 
ATOM   15983 C  CG1 . ILE D  1 341 ? 38.791  -35.449 -38.738 1.00 77.97 ? 358  ILE D CG1 1 
ATOM   15984 C  CG2 . ILE D  1 341 ? 39.647  -36.416 -36.559 1.00 78.18 ? 358  ILE D CG2 1 
ATOM   15985 C  CD1 . ILE D  1 341 ? 37.320  -35.549 -38.370 1.00 77.66 ? 358  ILE D CD1 1 
ATOM   15986 N  N   . ASP D  1 342 ? 39.704  -33.359 -34.472 1.00 80.37 ? 359  ASP D N   1 
ATOM   15987 C  CA  . ASP D  1 342 ? 40.388  -33.233 -33.192 1.00 81.95 ? 359  ASP D CA  1 
ATOM   15988 C  C   . ASP D  1 342 ? 40.511  -34.616 -32.550 1.00 82.67 ? 359  ASP D C   1 
ATOM   15989 O  O   . ASP D  1 342 ? 40.032  -35.607 -33.100 1.00 84.02 ? 359  ASP D O   1 
ATOM   15990 C  CB  . ASP D  1 342 ? 39.742  -32.169 -32.313 1.00 80.72 ? 359  ASP D CB  1 
ATOM   15991 C  CG  . ASP D  1 342 ? 38.310  -32.432 -31.869 1.00 83.12 ? 359  ASP D CG  1 
ATOM   15992 O  OD1 . ASP D  1 342 ? 38.056  -33.524 -31.322 1.00 84.74 ? 359  ASP D OD1 1 
ATOM   15993 O  OD2 . ASP D  1 342 ? 37.465  -31.530 -32.053 1.00 83.25 ? 359  ASP D OD2 1 
ATOM   15994 N  N   . SER D  1 343 ? 41.171  -34.667 -31.386 1.00 82.03 ? 360  SER D N   1 
ATOM   15995 C  CA  . SER D  1 343 ? 41.487  -35.921 -30.716 1.00 79.60 ? 360  SER D CA  1 
ATOM   15996 C  C   . SER D  1 343 ? 40.269  -36.482 -29.982 1.00 73.38 ? 360  SER D C   1 
ATOM   15997 O  O   . SER D  1 343 ? 40.244  -37.666 -29.656 1.00 74.24 ? 360  SER D O   1 
ATOM   15998 C  CB  . SER D  1 343 ? 42.652  -35.747 -29.773 1.00 81.11 ? 360  SER D CB  1 
ATOM   15999 O  OG  . SER D  1 343 ? 42.349  -34.804 -28.754 1.00 82.92 ? 360  SER D OG  1 
ATOM   16000 N  N   . TYR D  1 344 ? 39.273  -35.628 -29.710 1.00 67.04 ? 361  TYR D N   1 
ATOM   16001 C  CA  . TYR D  1 344 ? 38.025  -36.064 -29.103 1.00 61.82 ? 361  TYR D CA  1 
ATOM   16002 C  C   . TYR D  1 344 ? 37.191  -36.829 -30.132 1.00 58.47 ? 361  TYR D C   1 
ATOM   16003 O  O   . TYR D  1 344 ? 36.429  -37.724 -29.771 1.00 54.26 ? 361  TYR D O   1 
ATOM   16004 C  CB  . TYR D  1 344 ? 37.265  -34.860 -28.538 1.00 61.22 ? 361  TYR D CB  1 
ATOM   16005 N  N   . GLN D  1 345 ? 37.342  -36.463 -31.412 1.00 56.45 ? 362  GLN D N   1 
ATOM   16006 C  CA  . GLN D  1 345 ? 36.604  -37.085 -32.500 1.00 53.06 ? 362  GLN D CA  1 
ATOM   16007 C  C   . GLN D  1 345 ? 37.345  -38.327 -32.995 1.00 50.83 ? 362  GLN D C   1 
ATOM   16008 O  O   . GLN D  1 345 ? 36.722  -39.220 -33.563 1.00 50.32 ? 362  GLN D O   1 
ATOM   16009 C  CB  . GLN D  1 345 ? 36.361  -36.069 -33.620 1.00 51.59 ? 362  GLN D CB  1 
ATOM   16010 C  CG  . GLN D  1 345 ? 35.457  -34.908 -33.215 1.00 50.56 ? 362  GLN D CG  1 
ATOM   16011 C  CD  . GLN D  1 345 ? 35.400  -33.789 -34.234 1.00 51.02 ? 362  GLN D CD  1 
ATOM   16012 O  OE1 . GLN D  1 345 ? 36.430  -33.311 -34.723 1.00 51.95 ? 362  GLN D OE1 1 
ATOM   16013 N  NE2 . GLN D  1 345 ? 34.194  -33.338 -34.553 1.00 50.28 ? 362  GLN D NE2 1 
ATOM   16014 N  N   . GLU D  1 346 ? 38.661  -38.392 -32.744 1.00 51.50 ? 363  GLU D N   1 
ATOM   16015 C  CA  . GLU D  1 346 ? 39.523  -39.430 -33.295 1.00 53.33 ? 363  GLU D CA  1 
ATOM   16016 C  C   . GLU D  1 346 ? 38.945  -40.830 -33.068 1.00 55.11 ? 363  GLU D C   1 
ATOM   16017 O  O   . GLU D  1 346 ? 38.912  -41.628 -34.002 1.00 57.18 ? 363  GLU D O   1 
ATOM   16018 C  CB  . GLU D  1 346 ? 40.946  -39.345 -32.738 1.00 53.30 ? 363  GLU D CB  1 
ATOM   16019 N  N   . PRO D  1 347 ? 38.497  -41.198 -31.842 1.00 54.87 ? 364  PRO D N   1 
ATOM   16020 C  CA  . PRO D  1 347 ? 37.911  -42.523 -31.602 1.00 52.43 ? 364  PRO D CA  1 
ATOM   16021 C  C   . PRO D  1 347 ? 36.761  -42.942 -32.518 1.00 50.70 ? 364  PRO D C   1 
ATOM   16022 O  O   . PRO D  1 347 ? 36.541  -44.136 -32.715 1.00 51.56 ? 364  PRO D O   1 
ATOM   16023 C  CB  . PRO D  1 347 ? 37.444  -42.439 -30.134 1.00 54.17 ? 364  PRO D CB  1 
ATOM   16024 C  CG  . PRO D  1 347 ? 38.355  -41.407 -29.510 1.00 55.23 ? 364  PRO D CG  1 
ATOM   16025 C  CD  . PRO D  1 347 ? 38.580  -40.389 -30.613 1.00 55.09 ? 364  PRO D CD  1 
ATOM   16026 N  N   . PHE D  1 348 ? 36.023  -41.965 -33.062 1.00 49.19 ? 365  PHE D N   1 
ATOM   16027 C  CA  . PHE D  1 348 ? 34.857  -42.249 -33.886 1.00 48.77 ? 365  PHE D CA  1 
ATOM   16028 C  C   . PHE D  1 348 ? 35.119  -41.889 -35.350 1.00 50.96 ? 365  PHE D C   1 
ATOM   16029 O  O   . PHE D  1 348 ? 34.177  -41.767 -36.132 1.00 48.44 ? 365  PHE D O   1 
ATOM   16030 C  CB  . PHE D  1 348 ? 33.657  -41.493 -33.308 1.00 47.48 ? 365  PHE D CB  1 
ATOM   16031 C  CG  . PHE D  1 348 ? 33.450  -41.725 -31.816 1.00 45.58 ? 365  PHE D CG  1 
ATOM   16032 C  CD1 . PHE D  1 348 ? 33.100  -42.983 -31.336 1.00 45.55 ? 365  PHE D CD1 1 
ATOM   16033 C  CD2 . PHE D  1 348 ? 33.593  -40.686 -30.903 1.00 44.40 ? 365  PHE D CD2 1 
ATOM   16034 C  CE1 . PHE D  1 348 ? 32.914  -43.196 -29.980 1.00 44.82 ? 365  PHE D CE1 1 
ATOM   16035 C  CE2 . PHE D  1 348 ? 33.407  -40.906 -29.548 1.00 45.08 ? 365  PHE D CE2 1 
ATOM   16036 C  CZ  . PHE D  1 348 ? 33.064  -42.158 -29.091 1.00 44.96 ? 365  PHE D CZ  1 
ATOM   16037 N  N   . THR D  1 349 ? 36.398  -41.722 -35.714 1.00 54.91 ? 366  THR D N   1 
ATOM   16038 C  CA  . THR D  1 349 ? 36.785  -41.475 -37.094 1.00 57.87 ? 366  THR D CA  1 
ATOM   16039 C  C   . THR D  1 349 ? 37.432  -42.745 -37.642 1.00 59.49 ? 366  THR D C   1 
ATOM   16040 O  O   . THR D  1 349 ? 38.496  -43.151 -37.179 1.00 61.05 ? 366  THR D O   1 
ATOM   16041 C  CB  . THR D  1 349 ? 37.726  -40.274 -37.188 1.00 57.40 ? 366  THR D CB  1 
ATOM   16042 O  OG1 . THR D  1 349 ? 38.875  -40.616 -36.419 1.00 61.23 ? 366  THR D OG1 1 
ATOM   16043 C  CG2 . THR D  1 349 ? 37.090  -38.993 -36.679 1.00 56.18 ? 366  THR D CG2 1 
ATOM   16044 N  N   . HIS D  1 350 ? 36.766  -43.364 -38.622 1.00 61.95 ? 367  HIS D N   1 
ATOM   16045 C  CA  . HIS D  1 350 ? 37.213  -44.621 -39.198 1.00 63.62 ? 367  HIS D CA  1 
ATOM   16046 C  C   . HIS D  1 350 ? 37.544  -44.400 -40.680 1.00 62.31 ? 367  HIS D C   1 
ATOM   16047 O  O   . HIS D  1 350 ? 38.573  -44.955 -41.125 1.00 62.68 ? 367  HIS D O   1 
ATOM   16048 C  CB  . HIS D  1 350 ? 36.146  -45.708 -39.015 1.00 62.65 ? 367  HIS D CB  1 
ATOM   16049 C  CG  . HIS D  1 350 ? 35.435  -45.660 -37.700 1.00 62.80 ? 367  HIS D CG  1 
ATOM   16050 N  ND1 . HIS D  1 350 ? 36.029  -46.007 -36.506 1.00 62.54 ? 367  HIS D ND1 1 
ATOM   16051 C  CD2 . HIS D  1 350 ? 34.186  -45.279 -37.393 1.00 61.14 ? 367  HIS D CD2 1 
ATOM   16052 C  CE1 . HIS D  1 350 ? 35.156  -45.847 -35.520 1.00 62.15 ? 367  HIS D CE1 1 
ATOM   16053 N  NE2 . HIS D  1 350 ? 34.029  -45.410 -36.038 1.00 61.72 ? 367  HIS D NE2 1 
ATOM   16054 N  N   . PRO D  1 357 ? 30.542  -41.200 -49.350 1.00 69.61 ? 374  PRO D N   1 
ATOM   16055 C  CA  . PRO D  1 357 ? 29.213  -40.678 -49.051 1.00 70.55 ? 374  PRO D CA  1 
ATOM   16056 C  C   . PRO D  1 357 ? 29.276  -39.160 -48.906 1.00 72.62 ? 374  PRO D C   1 
ATOM   16057 O  O   . PRO D  1 357 ? 30.031  -38.647 -48.084 1.00 78.47 ? 374  PRO D O   1 
ATOM   16058 C  CB  . PRO D  1 357 ? 28.777  -41.377 -47.750 1.00 69.91 ? 374  PRO D CB  1 
ATOM   16059 C  CG  . PRO D  1 357 ? 30.068  -41.886 -47.151 1.00 69.63 ? 374  PRO D CG  1 
ATOM   16060 C  CD  . PRO D  1 357 ? 30.976  -42.153 -48.340 1.00 70.29 ? 374  PRO D CD  1 
ATOM   16061 N  N   . ASP D  1 358 ? 28.476  -38.452 -49.712 1.00 72.47 ? 375  ASP D N   1 
ATOM   16062 C  CA  . ASP D  1 358 ? 28.557  -37.001 -49.797 1.00 72.38 ? 375  ASP D CA  1 
ATOM   16063 C  C   . ASP D  1 358 ? 27.346  -36.345 -49.135 1.00 69.09 ? 375  ASP D C   1 
ATOM   16064 O  O   . ASP D  1 358 ? 27.422  -35.177 -48.759 1.00 69.90 ? 375  ASP D O   1 
ATOM   16065 C  CB  . ASP D  1 358 ? 28.766  -36.531 -51.229 1.00 75.08 ? 375  ASP D CB  1 
ATOM   16066 C  CG  . ASP D  1 358 ? 27.821  -37.120 -52.267 1.00 78.12 ? 375  ASP D CG  1 
ATOM   16067 O  OD1 . ASP D  1 358 ? 26.591  -37.017 -52.066 1.00 81.67 ? 375  ASP D OD1 1 
ATOM   16068 O  OD2 . ASP D  1 358 ? 28.323  -37.673 -53.270 1.00 77.76 ? 375  ASP D OD2 1 
ATOM   16069 N  N   . THR D  1 359 ? 26.230  -37.078 -49.019 1.00 65.89 ? 376  THR D N   1 
ATOM   16070 C  CA  . THR D  1 359 ? 25.074  -36.599 -48.276 1.00 65.67 ? 376  THR D CA  1 
ATOM   16071 C  C   . THR D  1 359 ? 24.762  -37.593 -47.157 1.00 61.69 ? 376  THR D C   1 
ATOM   16072 O  O   . THR D  1 359 ? 25.366  -38.662 -47.082 1.00 60.22 ? 376  THR D O   1 
ATOM   16073 C  CB  . THR D  1 359 ? 23.892  -36.372 -49.224 1.00 67.08 ? 376  THR D CB  1 
ATOM   16074 O  OG1 . THR D  1 359 ? 22.950  -35.593 -48.494 1.00 69.82 ? 376  THR D OG1 1 
ATOM   16075 C  CG2 . THR D  1 359 ? 23.234  -37.655 -49.699 1.00 66.72 ? 376  THR D CG2 1 
ATOM   16076 N  N   . PHE D  1 360 ? 23.828  -37.220 -46.274 1.00 58.27 ? 377  PHE D N   1 
ATOM   16077 C  CA  . PHE D  1 360 ? 23.490  -38.044 -45.124 1.00 57.06 ? 377  PHE D CA  1 
ATOM   16078 C  C   . PHE D  1 360 ? 22.657  -39.237 -45.590 1.00 56.32 ? 377  PHE D C   1 
ATOM   16079 O  O   . PHE D  1 360 ? 22.787  -40.327 -45.039 1.00 53.25 ? 377  PHE D O   1 
ATOM   16080 C  CB  . PHE D  1 360 ? 22.773  -37.228 -44.043 1.00 55.24 ? 377  PHE D CB  1 
ATOM   16081 C  CG  . PHE D  1 360 ? 22.603  -37.974 -42.725 1.00 52.89 ? 377  PHE D CG  1 
ATOM   16082 C  CD1 . PHE D  1 360 ? 23.693  -38.190 -41.886 1.00 52.46 ? 377  PHE D CD1 1 
ATOM   16083 C  CD2 . PHE D  1 360 ? 21.360  -38.458 -42.329 1.00 51.32 ? 377  PHE D CD2 1 
ATOM   16084 C  CE1 . PHE D  1 360 ? 23.543  -38.876 -40.690 1.00 51.13 ? 377  PHE D CE1 1 
ATOM   16085 C  CE2 . PHE D  1 360 ? 21.214  -39.143 -41.133 1.00 51.39 ? 377  PHE D CE2 1 
ATOM   16086 C  CZ  . PHE D  1 360 ? 22.305  -39.349 -40.316 1.00 51.51 ? 377  PHE D CZ  1 
ATOM   16087 N  N   . GLU D  1 361 ? 21.811  -39.013 -46.606 1.00 58.05 ? 378  GLU D N   1 
ATOM   16088 C  CA  . GLU D  1 361 ? 21.026  -40.070 -47.230 1.00 58.85 ? 378  GLU D CA  1 
ATOM   16089 C  C   . GLU D  1 361 ? 21.947  -41.176 -47.743 1.00 56.83 ? 378  GLU D C   1 
ATOM   16090 O  O   . GLU D  1 361 ? 21.674  -42.354 -47.533 1.00 57.55 ? 378  GLU D O   1 
ATOM   16091 C  CB  . GLU D  1 361 ? 20.174  -39.513 -48.374 1.00 61.74 ? 378  GLU D CB  1 
ATOM   16092 C  CG  . GLU D  1 361 ? 19.173  -40.518 -48.940 1.00 64.06 ? 378  GLU D CG  1 
ATOM   16093 C  CD  . GLU D  1 361 ? 18.416  -40.068 -50.180 1.00 64.93 ? 378  GLU D CD  1 
ATOM   16094 O  OE1 . GLU D  1 361 ? 18.656  -38.943 -50.673 1.00 64.66 ? 378  GLU D OE1 1 
ATOM   16095 O  OE2 . GLU D  1 361 ? 17.572  -40.859 -50.656 1.00 63.67 ? 378  GLU D OE2 1 
ATOM   16096 N  N   . ASP D  1 362 ? 23.037  -40.785 -48.416 1.00 56.46 ? 379  ASP D N   1 
ATOM   16097 C  CA  . ASP D  1 362 ? 24.015  -41.728 -48.931 1.00 58.17 ? 379  ASP D CA  1 
ATOM   16098 C  C   . ASP D  1 362 ? 24.662  -42.469 -47.766 1.00 56.08 ? 379  ASP D C   1 
ATOM   16099 O  O   . ASP D  1 362 ? 24.783  -43.690 -47.805 1.00 57.42 ? 379  ASP D O   1 
ATOM   16100 C  CB  . ASP D  1 362 ? 25.086  -41.042 -49.765 1.00 61.43 ? 379  ASP D CB  1 
ATOM   16101 C  CG  . ASP D  1 362 ? 24.633  -40.467 -51.100 1.00 62.50 ? 379  ASP D CG  1 
ATOM   16102 O  OD1 . ASP D  1 362 ? 23.434  -40.600 -51.426 1.00 62.64 ? 379  ASP D OD1 1 
ATOM   16103 O  OD2 . ASP D  1 362 ? 25.485  -39.878 -51.797 1.00 66.25 ? 379  ASP D OD2 1 
ATOM   16104 N  N   . ALA D  1 363 ? 25.069  -41.703 -46.744 1.00 54.22 ? 380  ALA D N   1 
ATOM   16105 C  CA  . ALA D  1 363 ? 25.694  -42.239 -45.545 1.00 51.36 ? 380  ALA D CA  1 
ATOM   16106 C  C   . ALA D  1 363 ? 24.846  -43.356 -44.938 1.00 46.34 ? 380  ALA D C   1 
ATOM   16107 O  O   . ALA D  1 363 ? 25.385  -44.392 -44.557 1.00 47.57 ? 380  ALA D O   1 
ATOM   16108 C  CB  . ALA D  1 363 ? 25.929  -41.124 -44.546 1.00 53.00 ? 380  ALA D CB  1 
ATOM   16109 N  N   . VAL D  1 364 ? 23.527  -43.133 -44.850 1.00 44.52 ? 381  VAL D N   1 
ATOM   16110 C  CA  . VAL D  1 364 ? 22.602  -44.118 -44.308 1.00 45.23 ? 381  VAL D CA  1 
ATOM   16111 C  C   . VAL D  1 364 ? 22.622  -45.378 -45.174 1.00 49.70 ? 381  VAL D C   1 
ATOM   16112 O  O   . VAL D  1 364 ? 22.579  -46.486 -44.642 1.00 49.77 ? 381  VAL D O   1 
ATOM   16113 C  CB  . VAL D  1 364 ? 21.173  -43.555 -44.183 1.00 44.27 ? 381  VAL D CB  1 
ATOM   16114 C  CG1 . VAL D  1 364 ? 20.146  -44.636 -43.861 1.00 44.40 ? 381  VAL D CG1 1 
ATOM   16115 C  CG2 . VAL D  1 364 ? 21.092  -42.438 -43.150 1.00 44.97 ? 381  VAL D CG2 1 
ATOM   16116 N  N   . ASN D  1 365 ? 22.690  -45.199 -46.503 1.00 50.17 ? 382  ASN D N   1 
ATOM   16117 C  CA  . ASN D  1 365 ? 22.585  -46.309 -47.441 1.00 48.27 ? 382  ASN D CA  1 
ATOM   16118 C  C   . ASN D  1 365 ? 23.871  -47.129 -47.466 1.00 47.64 ? 382  ASN D C   1 
ATOM   16119 O  O   . ASN D  1 365 ? 23.807  -48.346 -47.616 1.00 48.36 ? 382  ASN D O   1 
ATOM   16120 C  CB  . ASN D  1 365 ? 22.202  -45.845 -48.845 1.00 47.48 ? 382  ASN D CB  1 
ATOM   16121 C  CG  . ASN D  1 365 ? 20.724  -45.556 -48.971 1.00 47.37 ? 382  ASN D CG  1 
ATOM   16122 O  OD1 . ASN D  1 365 ? 19.893  -46.381 -48.576 1.00 48.92 ? 382  ASN D OD1 1 
ATOM   16123 N  ND2 . ASN D  1 365 ? 20.371  -44.398 -49.506 1.00 48.60 ? 382  ASN D ND2 1 
ATOM   16124 N  N   . ILE D  1 366 ? 25.028  -46.468 -47.323 1.00 49.41 ? 383  ILE D N   1 
ATOM   16125 C  CA  . ILE D  1 366 ? 26.311  -47.147 -47.448 1.00 51.95 ? 383  ILE D CA  1 
ATOM   16126 C  C   . ILE D  1 366 ? 26.693  -47.810 -46.122 1.00 52.75 ? 383  ILE D C   1 
ATOM   16127 O  O   . ILE D  1 366 ? 27.299  -48.880 -46.129 1.00 52.50 ? 383  ILE D O   1 
ATOM   16128 C  CB  . ILE D  1 366 ? 27.415  -46.202 -47.971 1.00 55.46 ? 383  ILE D CB  1 
ATOM   16129 C  CG1 . ILE D  1 366 ? 28.746  -46.930 -48.192 1.00 57.87 ? 383  ILE D CG1 1 
ATOM   16130 C  CG2 . ILE D  1 366 ? 27.610  -44.989 -47.062 1.00 58.17 ? 383  ILE D CG2 1 
ATOM   16131 C  CD1 . ILE D  1 366 ? 28.692  -48.064 -49.202 1.00 60.62 ? 383  ILE D CD1 1 
ATOM   16132 N  N   . LEU D  1 367 ? 26.349  -47.173 -44.993 1.00 52.05 ? 384  LEU D N   1 
ATOM   16133 C  CA  . LEU D  1 367 ? 26.734  -47.675 -43.680 1.00 49.15 ? 384  LEU D CA  1 
ATOM   16134 C  C   . LEU D  1 367 ? 25.653  -48.600 -43.123 1.00 47.36 ? 384  LEU D C   1 
ATOM   16135 O  O   . LEU D  1 367 ? 25.968  -49.548 -42.407 1.00 49.73 ? 384  LEU D O   1 
ATOM   16136 C  CB  . LEU D  1 367 ? 27.020  -46.519 -42.722 1.00 47.69 ? 384  LEU D CB  1 
ATOM   16137 C  CG  . LEU D  1 367 ? 28.251  -45.663 -43.037 1.00 48.81 ? 384  LEU D CG  1 
ATOM   16138 C  CD1 . LEU D  1 367 ? 28.316  -44.463 -42.103 1.00 49.96 ? 384  LEU D CD1 1 
ATOM   16139 C  CD2 . LEU D  1 367 ? 29.540  -46.464 -42.957 1.00 48.34 ? 384  LEU D CD2 1 
ATOM   16140 N  N   . LYS D  1 368 ? 24.386  -48.304 -43.436 1.00 46.51 ? 385  LYS D N   1 
ATOM   16141 C  CA  . LYS D  1 368 ? 23.252  -49.076 -42.951 1.00 47.97 ? 385  LYS D CA  1 
ATOM   16142 C  C   . LYS D  1 368 ? 23.265  -49.111 -41.424 1.00 47.56 ? 385  LYS D C   1 
ATOM   16143 O  O   . LYS D  1 368 ? 23.489  -50.161 -40.824 1.00 48.15 ? 385  LYS D O   1 
ATOM   16144 C  CB  . LYS D  1 368 ? 23.212  -50.486 -43.554 1.00 51.94 ? 385  LYS D CB  1 
ATOM   16145 C  CG  . LYS D  1 368 ? 22.941  -50.538 -45.056 1.00 54.62 ? 385  LYS D CG  1 
ATOM   16146 C  CD  . LYS D  1 368 ? 22.547  -51.922 -45.564 1.00 57.54 ? 385  LYS D CD  1 
ATOM   16147 C  CE  . LYS D  1 368 ? 22.302  -51.970 -47.042 1.00 58.44 ? 385  LYS D CE  1 
ATOM   16148 N  NZ  . LYS D  1 368 ? 23.535  -51.786 -47.815 1.00 60.22 ? 385  LYS D NZ  1 
ATOM   16149 N  N   . PRO D  1 369 ? 23.017  -47.965 -40.749 1.00 44.26 ? 386  PRO D N   1 
ATOM   16150 C  CA  . PRO D  1 369 ? 22.915  -47.940 -39.290 1.00 41.95 ? 386  PRO D CA  1 
ATOM   16151 C  C   . PRO D  1 369 ? 21.550  -48.415 -38.806 1.00 37.62 ? 386  PRO D C   1 
ATOM   16152 O  O   . PRO D  1 369 ? 20.558  -48.297 -39.523 1.00 38.67 ? 386  PRO D O   1 
ATOM   16153 C  CB  . PRO D  1 369 ? 23.155  -46.455 -38.984 1.00 42.69 ? 386  PRO D CB  1 
ATOM   16154 C  CG  . PRO D  1 369 ? 22.515  -45.745 -40.154 1.00 43.64 ? 386  PRO D CG  1 
ATOM   16155 C  CD  . PRO D  1 369 ? 22.819  -46.636 -41.350 1.00 44.53 ? 386  PRO D CD  1 
ATOM   16156 N  N   . SER D  1 370 ? 21.524  -48.955 -37.581 1.00 35.34 ? 387  SER D N   1 
ATOM   16157 C  CA  . SER D  1 370 ? 20.287  -49.262 -36.878 1.00 33.33 ? 387  SER D CA  1 
ATOM   16158 C  C   . SER D  1 370 ? 19.737  -48.013 -36.184 1.00 31.88 ? 387  SER D C   1 
ATOM   16159 O  O   . SER D  1 370 ? 18.542  -47.929 -35.917 1.00 31.62 ? 387  SER D O   1 
ATOM   16160 C  CB  . SER D  1 370 ? 20.502  -50.390 -35.894 1.00 33.06 ? 387  SER D CB  1 
ATOM   16161 O  OG  . SER D  1 370 ? 21.675  -50.173 -35.121 1.00 33.85 ? 387  SER D OG  1 
ATOM   16162 N  N   . THR D  1 371 ? 20.617  -47.047 -35.888 1.00 31.97 ? 388  THR D N   1 
ATOM   16163 C  CA  . THR D  1 371 ? 20.237  -45.844 -35.163 1.00 31.66 ? 388  THR D CA  1 
ATOM   16164 C  C   . THR D  1 371 ? 20.851  -44.620 -35.840 1.00 29.91 ? 388  THR D C   1 
ATOM   16165 O  O   . THR D  1 371 ? 22.029  -44.630 -36.194 1.00 29.69 ? 388  THR D O   1 
ATOM   16166 C  CB  . THR D  1 371 ? 20.717  -45.953 -33.714 1.00 32.47 ? 388  THR D CB  1 
ATOM   16167 O  OG1 . THR D  1 371 ? 20.071  -47.084 -33.132 1.00 31.79 ? 388  THR D OG1 1 
ATOM   16168 C  CG2 . THR D  1 371 ? 20.420  -44.700 -32.907 1.00 31.66 ? 388  THR D CG2 1 
ATOM   16169 N  N   . ILE D  1 372 ? 20.046  -43.561 -35.979 1.00 29.85 ? 389  ILE D N   1 
ATOM   16170 C  CA  . ILE D  1 372 ? 20.554  -42.252 -36.365 1.00 31.81 ? 389  ILE D CA  1 
ATOM   16171 C  C   . ILE D  1 372 ? 20.191  -41.244 -35.276 1.00 30.31 ? 389  ILE D C   1 
ATOM   16172 O  O   . ILE D  1 372 ? 19.053  -41.206 -34.811 1.00 30.09 ? 389  ILE D O   1 
ATOM   16173 C  CB  . ILE D  1 372 ? 20.030  -41.811 -37.748 1.00 33.03 ? 389  ILE D CB  1 
ATOM   16174 C  CG1 . ILE D  1 372 ? 18.501  -41.836 -37.831 1.00 33.94 ? 389  ILE D CG1 1 
ATOM   16175 C  CG2 . ILE D  1 372 ? 20.676  -42.644 -38.854 1.00 33.37 ? 389  ILE D CG2 1 
ATOM   16176 C  CD1 . ILE D  1 372 ? 17.931  -41.088 -39.026 1.00 35.26 ? 389  ILE D CD1 1 
ATOM   16177 N  N   . ILE D  1 373 ? 21.171  -40.422 -34.886 1.00 31.19 ? 390  ILE D N   1 
ATOM   16178 C  CA  . ILE D  1 373 ? 20.971  -39.441 -33.830 1.00 31.34 ? 390  ILE D CA  1 
ATOM   16179 C  C   . ILE D  1 373 ? 21.225  -38.052 -34.407 1.00 29.82 ? 390  ILE D C   1 
ATOM   16180 O  O   . ILE D  1 373 ? 22.321  -37.776 -34.887 1.00 30.79 ? 390  ILE D O   1 
ATOM   16181 C  CB  . ILE D  1 373 ? 21.868  -39.747 -32.614 1.00 31.37 ? 390  ILE D CB  1 
ATOM   16182 C  CG1 . ILE D  1 373 ? 21.568  -41.145 -32.037 1.00 31.73 ? 390  ILE D CG1 1 
ATOM   16183 C  CG2 . ILE D  1 373 ? 21.734  -38.657 -31.547 1.00 31.20 ? 390  ILE D CG2 1 
ATOM   16184 C  CD1 . ILE D  1 373 ? 22.591  -41.648 -31.032 1.00 31.18 ? 390  ILE D CD1 1 
ATOM   16185 N  N   . GLY D  1 374 ? 20.195  -37.199 -34.347 1.00 30.15 ? 391  GLY D N   1 
ATOM   16186 C  CA  . GLY D  1 374 ? 20.253  -35.855 -34.899 1.00 31.44 ? 391  GLY D CA  1 
ATOM   16187 C  C   . GLY D  1 374 ? 20.593  -34.808 -33.838 1.00 30.90 ? 391  GLY D C   1 
ATOM   16188 O  O   . GLY D  1 374 ? 19.748  -34.452 -33.020 1.00 31.35 ? 391  GLY D O   1 
ATOM   16189 N  N   . VAL D  1 375 ? 21.833  -34.309 -33.890 1.00 33.22 ? 392  VAL D N   1 
ATOM   16190 C  CA  . VAL D  1 375 ? 22.305  -33.261 -32.999 1.00 36.88 ? 392  VAL D CA  1 
ATOM   16191 C  C   . VAL D  1 375 ? 23.101  -32.242 -33.816 1.00 38.48 ? 392  VAL D C   1 
ATOM   16192 O  O   . VAL D  1 375 ? 24.269  -31.982 -33.537 1.00 39.47 ? 392  VAL D O   1 
ATOM   16193 C  CB  . VAL D  1 375 ? 23.121  -33.858 -31.831 1.00 37.14 ? 392  VAL D CB  1 
ATOM   16194 C  CG1 . VAL D  1 375 ? 22.211  -34.519 -30.802 1.00 37.27 ? 392  VAL D CG1 1 
ATOM   16195 C  CG2 . VAL D  1 375 ? 24.196  -34.833 -32.303 1.00 37.10 ? 392  VAL D CG2 1 
ATOM   16196 N  N   . ALA D  1 376 ? 22.440  -31.663 -34.828 1.00 42.69 ? 393  ALA D N   1 
ATOM   16197 C  CA  . ALA D  1 376 ? 23.086  -30.771 -35.782 1.00 44.65 ? 393  ALA D CA  1 
ATOM   16198 C  C   . ALA D  1 376 ? 22.659  -29.321 -35.556 1.00 44.95 ? 393  ALA D C   1 
ATOM   16199 O  O   . ALA D  1 376 ? 23.443  -28.409 -35.805 1.00 44.23 ? 393  ALA D O   1 
ATOM   16200 C  CB  . ALA D  1 376 ? 22.771  -31.216 -37.194 1.00 46.42 ? 393  ALA D CB  1 
ATOM   16201 N  N   . GLY D  1 377 ? 21.410  -29.119 -35.115 1.00 46.99 ? 394  GLY D N   1 
ATOM   16202 C  CA  . GLY D  1 377 ? 20.882  -27.792 -34.838 1.00 49.08 ? 394  GLY D CA  1 
ATOM   16203 C  C   . GLY D  1 377 ? 20.623  -27.001 -36.120 1.00 51.69 ? 394  GLY D C   1 
ATOM   16204 O  O   . GLY D  1 377 ? 20.565  -25.773 -36.088 1.00 48.94 ? 394  GLY D O   1 
ATOM   16205 N  N   . ALA D  1 378 ? 20.429  -27.723 -37.233 1.00 54.89 ? 395  ALA D N   1 
ATOM   16206 C  CA  . ALA D  1 378 ? 20.473  -27.135 -38.562 1.00 54.59 ? 395  ALA D CA  1 
ATOM   16207 C  C   . ALA D  1 378 ? 19.219  -27.485 -39.360 1.00 54.89 ? 395  ALA D C   1 
ATOM   16208 O  O   . ALA D  1 378 ? 19.272  -27.550 -40.583 1.00 56.95 ? 395  ALA D O   1 
ATOM   16209 C  CB  . ALA D  1 378 ? 21.729  -27.600 -39.273 1.00 53.78 ? 395  ALA D CB  1 
ATOM   16210 N  N   . GLY D  1 379 ? 18.091  -27.689 -38.669 1.00 56.61 ? 396  GLY D N   1 
ATOM   16211 C  CA  . GLY D  1 379 ? 16.809  -27.873 -39.333 1.00 57.61 ? 396  GLY D CA  1 
ATOM   16212 C  C   . GLY D  1 379 ? 16.608  -29.302 -39.839 1.00 59.49 ? 396  GLY D C   1 
ATOM   16213 O  O   . GLY D  1 379 ? 17.283  -30.230 -39.395 1.00 58.66 ? 396  GLY D O   1 
ATOM   16214 N  N   . ARG D  1 380 ? 15.678  -29.450 -40.792 1.00 59.45 ? 397  ARG D N   1 
ATOM   16215 C  CA  . ARG D  1 380 ? 15.108  -30.737 -41.159 1.00 57.53 ? 397  ARG D CA  1 
ATOM   16216 C  C   . ARG D  1 380 ? 16.044  -31.500 -42.093 1.00 56.79 ? 397  ARG D C   1 
ATOM   16217 O  O   . ARG D  1 380 ? 15.790  -31.577 -43.293 1.00 58.51 ? 397  ARG D O   1 
ATOM   16218 C  CB  . ARG D  1 380 ? 13.755  -30.496 -41.838 1.00 57.66 ? 397  ARG D CB  1 
ATOM   16219 C  CG  . ARG D  1 380 ? 12.692  -29.861 -40.952 1.00 57.59 ? 397  ARG D CG  1 
ATOM   16220 C  CD  . ARG D  1 380 ? 12.026  -30.880 -40.045 1.00 57.90 ? 397  ARG D CD  1 
ATOM   16221 N  NE  . ARG D  1 380 ? 10.873  -30.329 -39.324 1.00 58.16 ? 397  ARG D NE  1 
ATOM   16222 C  CZ  . ARG D  1 380 ? 10.918  -29.435 -38.339 1.00 58.83 ? 397  ARG D CZ  1 
ATOM   16223 N  NH1 . ARG D  1 380 ? 12.074  -28.956 -37.910 1.00 58.85 ? 397  ARG D NH1 1 
ATOM   16224 N  NH2 . ARG D  1 380 ? 9.797   -29.031 -37.766 1.00 59.62 ? 397  ARG D NH2 1 
ATOM   16225 N  N   . LEU D  1 381 ? 17.106  -32.088 -41.526 1.00 54.42 ? 398  LEU D N   1 
ATOM   16226 C  CA  . LEU D  1 381 ? 18.087  -32.839 -42.297 1.00 51.51 ? 398  LEU D CA  1 
ATOM   16227 C  C   . LEU D  1 381 ? 17.734  -34.325 -42.330 1.00 49.00 ? 398  LEU D C   1 
ATOM   16228 O  O   . LEU D  1 381 ? 18.355  -35.077 -43.077 1.00 46.66 ? 398  LEU D O   1 
ATOM   16229 C  CB  . LEU D  1 381 ? 19.497  -32.630 -41.751 1.00 52.68 ? 398  LEU D CB  1 
ATOM   16230 C  CG  . LEU D  1 381 ? 20.203  -31.353 -42.210 1.00 55.00 ? 398  LEU D CG  1 
ATOM   16231 C  CD1 . LEU D  1 381 ? 19.558  -30.128 -41.603 1.00 55.47 ? 398  LEU D CD1 1 
ATOM   16232 C  CD2 . LEU D  1 381 ? 21.683  -31.395 -41.883 1.00 55.80 ? 398  LEU D CD2 1 
ATOM   16233 N  N   . PHE D  1 382 ? 16.775  -34.752 -41.497 1.00 47.31 ? 399  PHE D N   1 
ATOM   16234 C  CA  . PHE D  1 382 ? 16.200  -36.082 -41.626 1.00 47.15 ? 399  PHE D CA  1 
ATOM   16235 C  C   . PHE D  1 382 ? 15.011  -35.956 -42.575 1.00 47.76 ? 399  PHE D C   1 
ATOM   16236 O  O   . PHE D  1 382 ? 13.860  -35.890 -42.142 1.00 47.77 ? 399  PHE D O   1 
ATOM   16237 C  CB  . PHE D  1 382 ? 15.827  -36.724 -40.282 1.00 43.07 ? 399  PHE D CB  1 
ATOM   16238 C  CG  . PHE D  1 382 ? 16.982  -37.101 -39.359 1.00 41.33 ? 399  PHE D CG  1 
ATOM   16239 C  CD1 . PHE D  1 382 ? 18.308  -37.063 -39.789 1.00 39.03 ? 399  PHE D CD1 1 
ATOM   16240 C  CD2 . PHE D  1 382 ? 16.729  -37.525 -38.057 1.00 40.39 ? 399  PHE D CD2 1 
ATOM   16241 C  CE1 . PHE D  1 382 ? 19.342  -37.414 -38.933 1.00 39.52 ? 399  PHE D CE1 1 
ATOM   16242 C  CE2 . PHE D  1 382 ? 17.768  -37.876 -37.208 1.00 38.68 ? 399  PHE D CE2 1 
ATOM   16243 C  CZ  . PHE D  1 382 ? 19.070  -37.822 -37.646 1.00 38.28 ? 399  PHE D CZ  1 
ATOM   16244 N  N   . THR D  1 383 ? 15.326  -35.899 -43.875 1.00 51.35 ? 400  THR D N   1 
ATOM   16245 C  CA  . THR D  1 383 ? 14.336  -35.679 -44.919 1.00 53.20 ? 400  THR D CA  1 
ATOM   16246 C  C   . THR D  1 383 ? 13.478  -36.931 -45.060 1.00 53.59 ? 400  THR D C   1 
ATOM   16247 O  O   . THR D  1 383 ? 13.921  -38.023 -44.707 1.00 53.54 ? 400  THR D O   1 
ATOM   16248 C  CB  . THR D  1 383 ? 15.032  -35.359 -46.242 1.00 53.47 ? 400  THR D CB  1 
ATOM   16249 O  OG1 . THR D  1 383 ? 15.772  -36.537 -46.546 1.00 52.95 ? 400  THR D OG1 1 
ATOM   16250 C  CG2 . THR D  1 383 ? 15.940  -34.144 -46.162 1.00 54.49 ? 400  THR D CG2 1 
ATOM   16251 N  N   . PRO D  1 384 ? 12.245  -36.824 -45.604 1.00 54.12 ? 401  PRO D N   1 
ATOM   16252 C  CA  . PRO D  1 384 ? 11.431  -38.008 -45.886 1.00 54.37 ? 401  PRO D CA  1 
ATOM   16253 C  C   . PRO D  1 384 ? 12.236  -39.166 -46.479 1.00 53.94 ? 401  PRO D C   1 
ATOM   16254 O  O   . PRO D  1 384 ? 12.017  -40.319 -46.111 1.00 55.99 ? 401  PRO D O   1 
ATOM   16255 C  CB  . PRO D  1 384 ? 10.380  -37.448 -46.859 1.00 55.42 ? 401  PRO D CB  1 
ATOM   16256 C  CG  . PRO D  1 384 ? 10.184  -36.018 -46.397 1.00 54.64 ? 401  PRO D CG  1 
ATOM   16257 C  CD  . PRO D  1 384 ? 11.568  -35.565 -45.959 1.00 53.29 ? 401  PRO D CD  1 
ATOM   16258 N  N   . ASP D  1 385 ? 13.177  -38.845 -47.378 1.00 51.64 ? 402  ASP D N   1 
ATOM   16259 C  CA  . ASP D  1 385 ? 14.062  -39.831 -47.985 1.00 51.38 ? 402  ASP D CA  1 
ATOM   16260 C  C   . ASP D  1 385 ? 14.857  -40.589 -46.922 1.00 49.54 ? 402  ASP D C   1 
ATOM   16261 O  O   . ASP D  1 385 ? 14.929  -41.816 -46.962 1.00 46.58 ? 402  ASP D O   1 
ATOM   16262 C  CB  . ASP D  1 385 ? 15.027  -39.189 -48.971 1.00 53.57 ? 402  ASP D CB  1 
ATOM   16263 C  CG  . ASP D  1 385 ? 14.475  -38.877 -50.357 1.00 57.03 ? 402  ASP D CG  1 
ATOM   16264 O  OD1 . ASP D  1 385 ? 13.311  -39.246 -50.629 1.00 54.73 ? 402  ASP D OD1 1 
ATOM   16265 O  OD2 . ASP D  1 385 ? 15.222  -38.270 -51.156 1.00 57.36 ? 402  ASP D OD2 1 
ATOM   16266 N  N   . VAL D  1 386 ? 15.475  -39.849 -45.992 1.00 48.80 ? 403  VAL D N   1 
ATOM   16267 C  CA  . VAL D  1 386 ? 16.320  -40.440 -44.964 1.00 45.90 ? 403  VAL D CA  1 
ATOM   16268 C  C   . VAL D  1 386 ? 15.484  -41.378 -44.094 1.00 42.37 ? 403  VAL D C   1 
ATOM   16269 O  O   . VAL D  1 386 ? 15.939  -42.470 -43.767 1.00 43.44 ? 403  VAL D O   1 
ATOM   16270 C  CB  . VAL D  1 386 ? 17.040  -39.362 -44.125 1.00 46.53 ? 403  VAL D CB  1 
ATOM   16271 C  CG1 . VAL D  1 386 ? 17.723  -39.940 -42.887 1.00 46.90 ? 403  VAL D CG1 1 
ATOM   16272 C  CG2 . VAL D  1 386 ? 18.053  -38.587 -44.960 1.00 45.76 ? 403  VAL D CG2 1 
ATOM   16273 N  N   . ILE D  1 387 ? 14.261  -40.960 -43.744 1.00 43.48 ? 404  ILE D N   1 
ATOM   16274 C  CA  . ILE D  1 387 ? 13.389  -41.753 -42.891 1.00 44.71 ? 404  ILE D CA  1 
ATOM   16275 C  C   . ILE D  1 387 ? 13.050  -43.067 -43.595 1.00 47.32 ? 404  ILE D C   1 
ATOM   16276 O  O   . ILE D  1 387 ? 13.216  -44.141 -43.014 1.00 45.31 ? 404  ILE D O   1 
ATOM   16277 C  CB  . ILE D  1 387 ? 12.121  -40.972 -42.487 1.00 46.19 ? 404  ILE D CB  1 
ATOM   16278 C  CG1 . ILE D  1 387 ? 12.394  -39.930 -41.397 1.00 47.63 ? 404  ILE D CG1 1 
ATOM   16279 C  CG2 . ILE D  1 387 ? 11.018  -41.923 -42.028 1.00 47.64 ? 404  ILE D CG2 1 
ATOM   16280 C  CD1 . ILE D  1 387 ? 13.107  -38.681 -41.866 1.00 46.77 ? 404  ILE D CD1 1 
ATOM   16281 N  N   . ARG D  1 388 ? 12.567  -42.969 -44.845 1.00 46.81 ? 405  ARG D N   1 
ATOM   16282 C  CA  . ARG D  1 388 ? 12.161  -44.135 -45.618 1.00 45.58 ? 405  ARG D CA  1 
ATOM   16283 C  C   . ARG D  1 388 ? 13.329  -45.113 -45.743 1.00 42.67 ? 405  ARG D C   1 
ATOM   16284 O  O   . ARG D  1 388 ? 13.145  -46.318 -45.598 1.00 43.46 ? 405  ARG D O   1 
ATOM   16285 C  CB  . ARG D  1 388 ? 11.610  -43.738 -46.996 1.00 48.48 ? 405  ARG D CB  1 
ATOM   16286 C  CG  . ARG D  1 388 ? 10.202  -43.158 -46.971 1.00 49.68 ? 405  ARG D CG  1 
ATOM   16287 C  CD  . ARG D  1 388 ? 9.627   -42.906 -48.368 1.00 51.63 ? 405  ARG D CD  1 
ATOM   16288 N  NE  . ARG D  1 388 ? 10.346  -41.846 -49.089 1.00 51.17 ? 405  ARG D NE  1 
ATOM   16289 C  CZ  . ARG D  1 388 ? 9.896   -40.616 -49.362 1.00 50.45 ? 405  ARG D CZ  1 
ATOM   16290 N  NH1 . ARG D  1 388 ? 8.679   -40.231 -49.012 1.00 48.37 ? 405  ARG D NH1 1 
ATOM   16291 N  NH2 . ARG D  1 388 ? 10.683  -39.760 -49.991 1.00 50.48 ? 405  ARG D NH2 1 
ATOM   16292 N  N   . ALA D  1 389 ? 14.532  -44.583 -45.990 1.00 43.00 ? 406  ALA D N   1 
ATOM   16293 C  CA  . ALA D  1 389 ? 15.729  -45.397 -46.140 1.00 42.72 ? 406  ALA D CA  1 
ATOM   16294 C  C   . ALA D  1 389 ? 16.099  -46.105 -44.834 1.00 45.02 ? 406  ALA D C   1 
ATOM   16295 O  O   . ALA D  1 389 ? 16.704  -47.179 -44.867 1.00 43.44 ? 406  ALA D O   1 
ATOM   16296 C  CB  . ALA D  1 389 ? 16.868  -44.536 -46.637 1.00 42.99 ? 406  ALA D CB  1 
ATOM   16297 N  N   . MET D  1 390 ? 15.771  -45.490 -43.686 1.00 44.70 ? 407  MET D N   1 
ATOM   16298 C  CA  . MET D  1 390 ? 15.990  -46.127 -42.395 1.00 43.58 ? 407  MET D CA  1 
ATOM   16299 C  C   . MET D  1 390 ? 14.966  -47.244 -42.206 1.00 42.63 ? 407  MET D C   1 
ATOM   16300 O  O   . MET D  1 390 ? 15.320  -48.337 -41.768 1.00 41.23 ? 407  MET D O   1 
ATOM   16301 C  CB  . MET D  1 390 ? 15.914  -45.120 -41.237 1.00 42.03 ? 407  MET D CB  1 
ATOM   16302 C  CG  . MET D  1 390 ? 17.194  -44.328 -41.014 1.00 40.92 ? 407  MET D CG  1 
ATOM   16303 S  SD  . MET D  1 390 ? 18.619  -45.332 -40.543 1.00 43.09 ? 407  MET D SD  1 
ATOM   16304 C  CE  . MET D  1 390 ? 18.040  -45.945 -38.954 1.00 42.53 ? 407  MET D CE  1 
ATOM   16305 N  N   . ALA D  1 391 ? 13.707  -46.959 -42.561 1.00 43.39 ? 408  ALA D N   1 
ATOM   16306 C  CA  . ALA D  1 391 ? 12.626  -47.930 -42.479 1.00 46.46 ? 408  ALA D CA  1 
ATOM   16307 C  C   . ALA D  1 391 ? 12.840  -49.086 -43.458 1.00 49.70 ? 408  ALA D C   1 
ATOM   16308 O  O   . ALA D  1 391 ? 12.299  -50.171 -43.258 1.00 49.80 ? 408  ALA D O   1 
ATOM   16309 C  CB  . ALA D  1 391 ? 11.305  -47.242 -42.733 1.00 47.14 ? 408  ALA D CB  1 
ATOM   16310 N  N   . SER D  1 392 ? 13.610  -48.843 -44.526 1.00 53.61 ? 409  SER D N   1 
ATOM   16311 C  CA  . SER D  1 392 ? 13.955  -49.883 -45.481 1.00 54.90 ? 409  SER D CA  1 
ATOM   16312 C  C   . SER D  1 392 ? 14.993  -50.829 -44.883 1.00 54.78 ? 409  SER D C   1 
ATOM   16313 O  O   . SER D  1 392 ? 14.834  -52.046 -44.956 1.00 56.01 ? 409  SER D O   1 
ATOM   16314 C  CB  . SER D  1 392 ? 14.449  -49.290 -46.779 1.00 57.07 ? 409  SER D CB  1 
ATOM   16315 O  OG  . SER D  1 392 ? 15.007  -50.294 -47.617 1.00 58.30 ? 409  SER D OG  1 
ATOM   16316 N  N   . ILE D  1 393 ? 16.051  -50.254 -44.298 1.00 51.54 ? 410  ILE D N   1 
ATOM   16317 C  CA  . ILE D  1 393 ? 17.199  -51.017 -43.830 1.00 51.00 ? 410  ILE D CA  1 
ATOM   16318 C  C   . ILE D  1 393 ? 16.847  -51.789 -42.555 1.00 48.80 ? 410  ILE D C   1 
ATOM   16319 O  O   . ILE D  1 393 ? 17.364  -52.882 -42.343 1.00 49.56 ? 410  ILE D O   1 
ATOM   16320 C  CB  . ILE D  1 393 ? 18.414  -50.090 -43.628 1.00 51.00 ? 410  ILE D CB  1 
ATOM   16321 C  CG1 . ILE D  1 393 ? 18.840  -49.432 -44.946 1.00 53.26 ? 410  ILE D CG1 1 
ATOM   16322 C  CG2 . ILE D  1 393 ? 19.582  -50.831 -42.978 1.00 50.04 ? 410  ILE D CG2 1 
ATOM   16323 C  CD1 . ILE D  1 393 ? 19.709  -48.198 -44.778 1.00 52.71 ? 410  ILE D CD1 1 
ATOM   16324 N  N   . ASN D  1 394 ? 15.969  -51.226 -41.715 1.00 46.75 ? 411  ASN D N   1 
ATOM   16325 C  CA  . ASN D  1 394 ? 15.697  -51.776 -40.393 1.00 44.08 ? 411  ASN D CA  1 
ATOM   16326 C  C   . ASN D  1 394 ? 14.207  -52.062 -40.239 1.00 43.07 ? 411  ASN D C   1 
ATOM   16327 O  O   . ASN D  1 394 ? 13.371  -51.301 -40.718 1.00 42.29 ? 411  ASN D O   1 
ATOM   16328 C  CB  . ASN D  1 394 ? 16.139  -50.821 -39.286 1.00 41.31 ? 411  ASN D CB  1 
ATOM   16329 C  CG  . ASN D  1 394 ? 17.572  -50.378 -39.455 1.00 39.05 ? 411  ASN D CG  1 
ATOM   16330 O  OD1 . ASN D  1 394 ? 18.501  -51.153 -39.202 1.00 39.67 ? 411  ASN D OD1 1 
ATOM   16331 N  ND2 . ASN D  1 394 ? 17.776  -49.138 -39.873 1.00 38.54 ? 411  ASN D ND2 1 
ATOM   16332 N  N   . GLU D  1 395 ? 13.891  -53.153 -39.531 1.00 46.07 ? 412  GLU D N   1 
ATOM   16333 C  CA  . GLU D  1 395 ? 12.520  -53.474 -39.169 1.00 47.14 ? 412  GLU D CA  1 
ATOM   16334 C  C   . GLU D  1 395 ? 11.988  -52.417 -38.200 1.00 47.87 ? 412  GLU D C   1 
ATOM   16335 O  O   . GLU D  1 395 ? 10.857  -51.956 -38.348 1.00 45.33 ? 412  GLU D O   1 
ATOM   16336 C  CB  . GLU D  1 395 ? 12.465  -54.883 -38.575 1.00 50.67 ? 412  GLU D CB  1 
ATOM   16337 C  CG  . GLU D  1 395 ? 11.080  -55.310 -38.091 1.00 54.15 ? 412  GLU D CG  1 
ATOM   16338 C  CD  . GLU D  1 395 ? 10.013  -55.473 -39.162 1.00 59.77 ? 412  GLU D CD  1 
ATOM   16339 O  OE1 . GLU D  1 395 ? 8.850   -55.727 -38.775 1.00 62.85 ? 412  GLU D OE1 1 
ATOM   16340 O  OE2 . GLU D  1 395 ? 10.327  -55.367 -40.371 1.00 62.46 ? 412  GLU D OE2 1 
ATOM   16341 N  N   . ARG D  1 396 ? 12.812  -52.048 -37.208 1.00 48.13 ? 413  ARG D N   1 
ATOM   16342 C  CA  . ARG D  1 396 ? 12.452  -51.032 -36.231 1.00 48.10 ? 413  ARG D CA  1 
ATOM   16343 C  C   . ARG D  1 396 ? 13.580  -50.005 -36.161 1.00 46.43 ? 413  ARG D C   1 
ATOM   16344 O  O   . ARG D  1 396 ? 14.493  -50.139 -35.347 1.00 44.10 ? 413  ARG D O   1 
ATOM   16345 C  CB  . ARG D  1 396 ? 12.187  -51.659 -34.854 1.00 51.47 ? 413  ARG D CB  1 
ATOM   16346 C  CG  . ARG D  1 396 ? 11.136  -52.761 -34.803 1.00 52.05 ? 413  ARG D CG  1 
ATOM   16347 C  CD  . ARG D  1 396 ? 9.732   -52.287 -35.155 1.00 53.65 ? 413  ARG D CD  1 
ATOM   16348 N  NE  . ARG D  1 396 ? 9.126   -51.373 -34.178 1.00 54.39 ? 413  ARG D NE  1 
ATOM   16349 C  CZ  . ARG D  1 396 ? 8.607   -51.702 -32.994 1.00 54.95 ? 413  ARG D CZ  1 
ATOM   16350 N  NH1 . ARG D  1 396 ? 8.676   -52.941 -32.536 1.00 54.24 ? 413  ARG D NH1 1 
ATOM   16351 N  NH2 . ARG D  1 396 ? 8.015   -50.773 -32.262 1.00 56.42 ? 413  ARG D NH2 1 
ATOM   16352 N  N   . PRO D  1 397 ? 13.571  -48.957 -37.020 1.00 43.15 ? 414  PRO D N   1 
ATOM   16353 C  CA  . PRO D  1 397 ? 14.645  -47.963 -37.020 1.00 40.11 ? 414  PRO D CA  1 
ATOM   16354 C  C   . PRO D  1 397 ? 14.571  -47.077 -35.779 1.00 35.59 ? 414  PRO D C   1 
ATOM   16355 O  O   . PRO D  1 397 ? 13.482  -46.760 -35.304 1.00 34.11 ? 414  PRO D O   1 
ATOM   16356 C  CB  . PRO D  1 397 ? 14.388  -47.186 -38.323 1.00 41.10 ? 414  PRO D CB  1 
ATOM   16357 C  CG  . PRO D  1 397 ? 12.891  -47.265 -38.498 1.00 41.80 ? 414  PRO D CG  1 
ATOM   16358 C  CD  . PRO D  1 397 ? 12.533  -48.666 -38.022 1.00 43.06 ? 414  PRO D CD  1 
ATOM   16359 N  N   . VAL D  1 398 ? 15.740  -46.699 -35.252 1.00 35.37 ? 415  VAL D N   1 
ATOM   16360 C  CA  . VAL D  1 398 ? 15.807  -45.757 -34.144 1.00 34.05 ? 415  VAL D CA  1 
ATOM   16361 C  C   . VAL D  1 398 ? 16.201  -44.395 -34.709 1.00 31.47 ? 415  VAL D C   1 
ATOM   16362 O  O   . VAL D  1 398 ? 17.283  -44.243 -35.276 1.00 33.10 ? 415  VAL D O   1 
ATOM   16363 C  CB  . VAL D  1 398 ? 16.782  -46.212 -33.041 1.00 32.93 ? 415  VAL D CB  1 
ATOM   16364 C  CG1 . VAL D  1 398 ? 16.765  -45.267 -31.844 1.00 32.40 ? 415  VAL D CG1 1 
ATOM   16365 C  CG2 . VAL D  1 398 ? 16.499  -47.643 -32.602 1.00 33.49 ? 415  VAL D CG2 1 
ATOM   16366 N  N   . ILE D  1 399 ? 15.303  -43.419 -34.547 1.00 31.67 ? 416  ILE D N   1 
ATOM   16367 C  CA  . ILE D  1 399 ? 15.514  -42.072 -35.053 1.00 32.21 ? 416  ILE D CA  1 
ATOM   16368 C  C   . ILE D  1 399 ? 15.348  -41.091 -33.895 1.00 30.49 ? 416  ILE D C   1 
ATOM   16369 O  O   . ILE D  1 399 ? 14.243  -40.916 -33.382 1.00 30.43 ? 416  ILE D O   1 
ATOM   16370 C  CB  . ILE D  1 399 ? 14.542  -41.758 -36.207 1.00 33.61 ? 416  ILE D CB  1 
ATOM   16371 C  CG1 . ILE D  1 399 ? 14.608  -42.818 -37.316 1.00 34.71 ? 416  ILE D CG1 1 
ATOM   16372 C  CG2 . ILE D  1 399 ? 14.790  -40.348 -36.750 1.00 34.01 ? 416  ILE D CG2 1 
ATOM   16373 C  CD1 . ILE D  1 399 ? 13.530  -42.677 -38.380 1.00 35.42 ? 416  ILE D CD1 1 
ATOM   16374 N  N   . PHE D  1 400 ? 16.460  -40.471 -33.482 1.00 31.86 ? 417  PHE D N   1 
ATOM   16375 C  CA  . PHE D  1 400 ? 16.440  -39.451 -32.444 1.00 32.75 ? 417  PHE D CA  1 
ATOM   16376 C  C   . PHE D  1 400 ? 16.743  -38.099 -33.084 1.00 32.22 ? 417  PHE D C   1 
ATOM   16377 O  O   . PHE D  1 400 ? 17.833  -37.891 -33.609 1.00 31.48 ? 417  PHE D O   1 
ATOM   16378 C  CB  . PHE D  1 400 ? 17.419  -39.813 -31.319 1.00 32.48 ? 417  PHE D CB  1 
ATOM   16379 C  CG  . PHE D  1 400 ? 16.873  -40.774 -30.267 1.00 33.45 ? 417  PHE D CG  1 
ATOM   16380 C  CD1 . PHE D  1 400 ? 15.984  -41.793 -30.602 1.00 33.74 ? 417  PHE D CD1 1 
ATOM   16381 C  CD2 . PHE D  1 400 ? 17.252  -40.655 -28.931 1.00 34.31 ? 417  PHE D CD2 1 
ATOM   16382 C  CE1 . PHE D  1 400 ? 15.490  -42.659 -29.636 1.00 33.79 ? 417  PHE D CE1 1 
ATOM   16383 C  CE2 . PHE D  1 400 ? 16.750  -41.520 -27.967 1.00 34.03 ? 417  PHE D CE2 1 
ATOM   16384 C  CZ  . PHE D  1 400 ? 15.874  -42.523 -28.320 1.00 34.52 ? 417  PHE D CZ  1 
ATOM   16385 N  N   . ALA D  1 401 ? 15.756  -37.198 -33.038 1.00 34.16 ? 418  ALA D N   1 
ATOM   16386 C  CA  . ALA D  1 401 ? 15.917  -35.839 -33.532 1.00 36.57 ? 418  ALA D CA  1 
ATOM   16387 C  C   . ALA D  1 401 ? 15.955  -34.884 -32.342 1.00 36.61 ? 418  ALA D C   1 
ATOM   16388 O  O   . ALA D  1 401 ? 14.915  -34.433 -31.863 1.00 38.11 ? 418  ALA D O   1 
ATOM   16389 C  CB  . ALA D  1 401 ? 14.792  -35.506 -34.489 1.00 36.59 ? 418  ALA D CB  1 
ATOM   16390 N  N   . LEU D  1 402 ? 17.169  -34.584 -31.872 1.00 38.79 ? 419  LEU D N   1 
ATOM   16391 C  CA  . LEU D  1 402 ? 17.353  -33.976 -30.563 1.00 41.41 ? 419  LEU D CA  1 
ATOM   16392 C  C   . LEU D  1 402 ? 17.520  -32.460 -30.660 1.00 44.45 ? 419  LEU D C   1 
ATOM   16393 O  O   . LEU D  1 402 ? 17.365  -31.768 -29.656 1.00 44.68 ? 419  LEU D O   1 
ATOM   16394 C  CB  . LEU D  1 402 ? 18.547  -34.637 -29.874 1.00 40.30 ? 419  LEU D CB  1 
ATOM   16395 C  CG  . LEU D  1 402 ? 18.386  -36.119 -29.520 1.00 40.16 ? 419  LEU D CG  1 
ATOM   16396 C  CD1 . LEU D  1 402 ? 19.584  -36.603 -28.721 1.00 40.59 ? 419  LEU D CD1 1 
ATOM   16397 C  CD2 . LEU D  1 402 ? 17.101  -36.399 -28.753 1.00 40.91 ? 419  LEU D CD2 1 
ATOM   16398 N  N   . SER D  1 403 ? 17.819  -31.943 -31.859 1.00 46.74 ? 420  SER D N   1 
ATOM   16399 C  CA  . SER D  1 403 ? 18.040  -30.517 -32.040 1.00 47.93 ? 420  SER D CA  1 
ATOM   16400 C  C   . SER D  1 403 ? 16.808  -29.720 -31.608 1.00 49.31 ? 420  SER D C   1 
ATOM   16401 O  O   . SER D  1 403 ? 15.675  -30.129 -31.865 1.00 49.38 ? 420  SER D O   1 
ATOM   16402 C  CB  . SER D  1 403 ? 18.443  -30.210 -33.458 1.00 48.36 ? 420  SER D CB  1 
ATOM   16403 O  OG  . SER D  1 403 ? 19.744  -30.717 -33.729 1.00 46.93 ? 420  SER D OG  1 
ATOM   16404 N  N   . ASN D  1 404 ? 17.055  -28.601 -30.911 1.00 53.34 ? 421  ASN D N   1 
ATOM   16405 C  CA  . ASN D  1 404 ? 16.023  -27.689 -30.435 1.00 53.99 ? 421  ASN D CA  1 
ATOM   16406 C  C   . ASN D  1 404 ? 16.328  -26.285 -30.957 1.00 54.41 ? 421  ASN D C   1 
ATOM   16407 O  O   . ASN D  1 404 ? 17.473  -26.005 -31.314 1.00 52.32 ? 421  ASN D O   1 
ATOM   16408 C  CB  . ASN D  1 404 ? 15.931  -27.686 -28.911 1.00 56.11 ? 421  ASN D CB  1 
ATOM   16409 C  CG  . ASN D  1 404 ? 15.537  -29.032 -28.349 1.00 56.98 ? 421  ASN D CG  1 
ATOM   16410 O  OD1 . ASN D  1 404 ? 14.485  -29.571 -28.708 1.00 55.53 ? 421  ASN D OD1 1 
ATOM   16411 N  ND2 . ASN D  1 404 ? 16.358  -29.588 -27.469 1.00 57.44 ? 421  ASN D ND2 1 
ATOM   16412 N  N   . PRO D  1 405 ? 15.339  -25.357 -31.034 1.00 55.67 ? 422  PRO D N   1 
ATOM   16413 C  CA  . PRO D  1 405 ? 13.930  -25.650 -30.742 1.00 56.06 ? 422  PRO D CA  1 
ATOM   16414 C  C   . PRO D  1 405 ? 13.232  -26.377 -31.891 1.00 55.07 ? 422  PRO D C   1 
ATOM   16415 O  O   . PRO D  1 405 ? 13.873  -26.723 -32.879 1.00 52.99 ? 422  PRO D O   1 
ATOM   16416 C  CB  . PRO D  1 405 ? 13.341  -24.249 -30.477 1.00 55.53 ? 422  PRO D CB  1 
ATOM   16417 C  CG  . PRO D  1 405 ? 14.165  -23.329 -31.349 1.00 55.15 ? 422  PRO D CG  1 
ATOM   16418 C  CD  . PRO D  1 405 ? 15.555  -23.944 -31.390 1.00 55.08 ? 422  PRO D CD  1 
ATOM   16419 N  N   . THR D  1 406 ? 11.917  -26.593 -31.751 1.00 56.79 ? 423  THR D N   1 
ATOM   16420 C  CA  . THR D  1 406 ? 11.139  -27.407 -32.675 1.00 60.96 ? 423  THR D CA  1 
ATOM   16421 C  C   . THR D  1 406 ? 11.593  -27.190 -34.119 1.00 62.31 ? 423  THR D C   1 
ATOM   16422 O  O   . THR D  1 406 ? 11.762  -28.157 -34.859 1.00 64.03 ? 423  THR D O   1 
ATOM   16423 C  CB  . THR D  1 406 ? 9.651   -27.095 -32.508 1.00 63.35 ? 423  THR D CB  1 
ATOM   16424 O  OG1 . THR D  1 406 ? 9.322   -27.444 -31.168 1.00 63.23 ? 423  THR D OG1 1 
ATOM   16425 C  CG2 . THR D  1 406 ? 8.767   -27.893 -33.451 1.00 64.12 ? 423  THR D CG2 1 
ATOM   16426 N  N   . ALA D  1 407 ? 11.792  -25.922 -34.505 1.00 60.70 ? 424  ALA D N   1 
ATOM   16427 C  CA  . ALA D  1 407 ? 12.049  -25.553 -35.889 1.00 60.20 ? 424  ALA D CA  1 
ATOM   16428 C  C   . ALA D  1 407 ? 13.419  -26.038 -36.370 1.00 60.05 ? 424  ALA D C   1 
ATOM   16429 O  O   . ALA D  1 407 ? 13.645  -26.115 -37.577 1.00 60.20 ? 424  ALA D O   1 
ATOM   16430 C  CB  . ALA D  1 407 ? 11.918  -24.053 -36.046 1.00 59.92 ? 424  ALA D CB  1 
ATOM   16431 N  N   . GLN D  1 408 ? 14.331  -26.355 -35.440 1.00 58.03 ? 425  GLN D N   1 
ATOM   16432 C  CA  . GLN D  1 408 ? 15.675  -26.795 -35.793 1.00 57.45 ? 425  GLN D CA  1 
ATOM   16433 C  C   . GLN D  1 408 ? 15.798  -28.319 -35.734 1.00 51.48 ? 425  GLN D C   1 
ATOM   16434 O  O   . GLN D  1 408 ? 16.855  -28.862 -36.055 1.00 47.70 ? 425  GLN D O   1 
ATOM   16435 C  CB  . GLN D  1 408 ? 16.703  -26.118 -34.885 1.00 60.88 ? 425  GLN D CB  1 
ATOM   16436 C  CG  . GLN D  1 408 ? 16.834  -24.614 -35.107 1.00 64.67 ? 425  GLN D CG  1 
ATOM   16437 C  CD  . GLN D  1 408 ? 17.278  -24.253 -36.510 1.00 67.74 ? 425  GLN D CD  1 
ATOM   16438 O  OE1 . GLN D  1 408 ? 16.517  -24.375 -37.477 1.00 70.47 ? 425  GLN D OE1 1 
ATOM   16439 N  NE2 . GLN D  1 408 ? 18.514  -23.794 -36.642 1.00 68.62 ? 425  GLN D NE2 1 
ATOM   16440 N  N   . ALA D  1 409 ? 14.712  -29.001 -35.350 1.00 49.83 ? 426  ALA D N   1 
ATOM   16441 C  CA  . ALA D  1 409 ? 14.703  -30.452 -35.243 1.00 50.83 ? 426  ALA D CA  1 
ATOM   16442 C  C   . ALA D  1 409 ? 14.944  -31.092 -36.610 1.00 51.65 ? 426  ALA D C   1 
ATOM   16443 O  O   . ALA D  1 409 ? 14.631  -30.501 -37.643 1.00 53.12 ? 426  ALA D O   1 
ATOM   16444 C  CB  . ALA D  1 409 ? 13.390  -30.912 -34.647 1.00 50.68 ? 426  ALA D CB  1 
ATOM   16445 N  N   . GLU D  1 410 ? 15.493  -32.312 -36.599 1.00 48.93 ? 427  GLU D N   1 
ATOM   16446 C  CA  . GLU D  1 410 ? 15.828  -33.021 -37.824 1.00 47.64 ? 427  GLU D CA  1 
ATOM   16447 C  C   . GLU D  1 410 ? 14.563  -33.524 -38.522 1.00 48.35 ? 427  GLU D C   1 
ATOM   16448 O  O   . GLU D  1 410 ? 14.543  -33.642 -39.746 1.00 49.68 ? 427  GLU D O   1 
ATOM   16449 C  CB  . GLU D  1 410 ? 16.806  -34.165 -37.556 1.00 45.06 ? 427  GLU D CB  1 
ATOM   16450 C  CG  . GLU D  1 410 ? 18.244  -33.713 -37.322 1.00 42.40 ? 427  GLU D CG  1 
ATOM   16451 C  CD  . GLU D  1 410 ? 18.552  -33.115 -35.957 1.00 38.52 ? 427  GLU D CD  1 
ATOM   16452 O  OE1 . GLU D  1 410 ? 17.668  -33.077 -35.077 1.00 37.53 ? 427  GLU D OE1 1 
ATOM   16453 O  OE2 . GLU D  1 410 ? 19.704  -32.676 -35.786 1.00 36.00 ? 427  GLU D OE2 1 
ATOM   16454 N  N   . CYS D  1 411 ? 13.522  -33.845 -37.742 1.00 50.04 ? 428  CYS D N   1 
ATOM   16455 C  CA  . CYS D  1 411 ? 12.226  -34.211 -38.297 1.00 51.06 ? 428  CYS D CA  1 
ATOM   16456 C  C   . CYS D  1 411 ? 11.155  -34.108 -37.213 1.00 52.32 ? 428  CYS D C   1 
ATOM   16457 O  O   . CYS D  1 411 ? 11.464  -33.892 -36.043 1.00 53.04 ? 428  CYS D O   1 
ATOM   16458 C  CB  . CYS D  1 411 ? 12.250  -35.599 -38.933 1.00 52.16 ? 428  CYS D CB  1 
ATOM   16459 S  SG  . CYS D  1 411 ? 12.524  -36.963 -37.768 1.00 51.07 ? 428  CYS D SG  1 
ATOM   16460 N  N   . THR D  1 412 ? 9.894   -34.258 -37.630 1.00 51.39 ? 429  THR D N   1 
ATOM   16461 C  CA  . THR D  1 412 ? 8.753   -34.218 -36.730 1.00 52.25 ? 429  THR D CA  1 
ATOM   16462 C  C   . THR D  1 412 ? 8.429   -35.643 -36.293 1.00 52.11 ? 429  THR D C   1 
ATOM   16463 O  O   . THR D  1 412 ? 8.899   -36.601 -36.904 1.00 52.53 ? 429  THR D O   1 
ATOM   16464 C  CB  . THR D  1 412 ? 7.573   -33.569 -37.455 1.00 53.83 ? 429  THR D CB  1 
ATOM   16465 O  OG1 . THR D  1 412 ? 8.132   -32.441 -38.122 1.00 54.64 ? 429  THR D OG1 1 
ATOM   16466 C  CG2 . THR D  1 412 ? 6.452   -33.138 -36.525 1.00 54.26 ? 429  THR D CG2 1 
ATOM   16467 N  N   . ALA D  1 413 ? 7.624   -35.760 -35.231 1.00 54.04 ? 430  ALA D N   1 
ATOM   16468 C  CA  . ALA D  1 413 ? 7.113   -37.040 -34.769 1.00 55.76 ? 430  ALA D CA  1 
ATOM   16469 C  C   . ALA D  1 413 ? 6.157   -37.633 -35.802 1.00 59.28 ? 430  ALA D C   1 
ATOM   16470 O  O   . ALA D  1 413 ? 6.285   -38.801 -36.169 1.00 58.36 ? 430  ALA D O   1 
ATOM   16471 C  CB  . ALA D  1 413 ? 6.432   -36.866 -33.431 1.00 56.37 ? 430  ALA D CB  1 
ATOM   16472 N  N   . GLU D  1 414 ? 5.193   -36.818 -36.254 1.00 62.00 ? 431  GLU D N   1 
ATOM   16473 C  CA  . GLU D  1 414 ? 4.218   -37.250 -37.244 1.00 63.48 ? 431  GLU D CA  1 
ATOM   16474 C  C   . GLU D  1 414 ? 4.940   -37.785 -38.478 1.00 58.23 ? 431  GLU D C   1 
ATOM   16475 O  O   . GLU D  1 414 ? 4.610   -38.864 -38.963 1.00 57.96 ? 431  GLU D O   1 
ATOM   16476 C  CB  . GLU D  1 414 ? 3.250   -36.129 -37.625 1.00 68.51 ? 431  GLU D CB  1 
ATOM   16477 C  CG  . GLU D  1 414 ? 2.089   -36.617 -38.488 1.00 72.61 ? 431  GLU D CG  1 
ATOM   16478 C  CD  . GLU D  1 414 ? 1.063   -35.558 -38.846 1.00 77.05 ? 431  GLU D CD  1 
ATOM   16479 O  OE1 . GLU D  1 414 ? 1.240   -34.385 -38.450 1.00 80.09 ? 431  GLU D OE1 1 
ATOM   16480 O  OE2 . GLU D  1 414 ? 0.079   -35.918 -39.526 1.00 78.89 ? 431  GLU D OE2 1 
ATOM   16481 N  N   . GLU D  1 415 ? 5.929   -37.026 -38.966 1.00 55.10 ? 432  GLU D N   1 
ATOM   16482 C  CA  . GLU D  1 415 ? 6.752   -37.442 -40.091 1.00 55.42 ? 432  GLU D CA  1 
ATOM   16483 C  C   . GLU D  1 415 ? 7.389   -38.804 -39.822 1.00 56.35 ? 432  GLU D C   1 
ATOM   16484 O  O   . GLU D  1 415 ? 7.391   -39.671 -40.692 1.00 54.09 ? 432  GLU D O   1 
ATOM   16485 C  CB  . GLU D  1 415 ? 7.863   -36.428 -40.370 1.00 57.95 ? 432  GLU D CB  1 
ATOM   16486 C  CG  . GLU D  1 415 ? 7.356   -35.097 -40.919 1.00 61.39 ? 432  GLU D CG  1 
ATOM   16487 C  CD  . GLU D  1 415 ? 8.429   -34.037 -41.112 1.00 64.76 ? 432  GLU D CD  1 
ATOM   16488 O  OE1 . GLU D  1 415 ? 9.628   -34.320 -40.888 1.00 63.86 ? 432  GLU D OE1 1 
ATOM   16489 O  OE2 . GLU D  1 415 ? 8.050   -32.907 -41.487 1.00 69.16 ? 432  GLU D OE2 1 
ATOM   16490 N  N   . ALA D  1 416 ? 7.937   -38.980 -38.613 1.00 54.89 ? 433  ALA D N   1 
ATOM   16491 C  CA  . ALA D  1 416 ? 8.726   -40.158 -38.286 1.00 53.96 ? 433  ALA D CA  1 
ATOM   16492 C  C   . ALA D  1 416 ? 7.869   -41.421 -38.351 1.00 52.01 ? 433  ALA D C   1 
ATOM   16493 O  O   . ALA D  1 416 ? 8.252   -42.388 -39.004 1.00 51.05 ? 433  ALA D O   1 
ATOM   16494 C  CB  . ALA D  1 416 ? 9.366   -39.990 -36.922 1.00 54.68 ? 433  ALA D CB  1 
ATOM   16495 N  N   . TYR D  1 417 ? 6.718   -41.408 -37.667 1.00 52.70 ? 434  TYR D N   1 
ATOM   16496 C  CA  . TYR D  1 417 ? 5.866   -42.585 -37.587 1.00 57.34 ? 434  TYR D CA  1 
ATOM   16497 C  C   . TYR D  1 417 ? 5.213   -42.855 -38.943 1.00 59.34 ? 434  TYR D C   1 
ATOM   16498 O  O   . TYR D  1 417 ? 5.186   -44.000 -39.391 1.00 60.57 ? 434  TYR D O   1 
ATOM   16499 C  CB  . TYR D  1 417 ? 4.820   -42.442 -36.476 1.00 58.53 ? 434  TYR D CB  1 
ATOM   16500 C  CG  . TYR D  1 417 ? 5.407   -42.381 -35.071 1.00 59.38 ? 434  TYR D CG  1 
ATOM   16501 C  CD1 . TYR D  1 417 ? 6.056   -43.481 -34.519 1.00 60.52 ? 434  TYR D CD1 1 
ATOM   16502 C  CD2 . TYR D  1 417 ? 5.303   -41.234 -34.293 1.00 58.75 ? 434  TYR D CD2 1 
ATOM   16503 C  CE1 . TYR D  1 417 ? 6.596   -43.437 -33.243 1.00 60.15 ? 434  TYR D CE1 1 
ATOM   16504 C  CE2 . TYR D  1 417 ? 5.835   -41.179 -33.014 1.00 60.43 ? 434  TYR D CE2 1 
ATOM   16505 C  CZ  . TYR D  1 417 ? 6.484   -42.283 -32.487 1.00 60.48 ? 434  TYR D CZ  1 
ATOM   16506 O  OH  . TYR D  1 417 ? 7.012   -42.241 -31.227 1.00 59.70 ? 434  TYR D OH  1 
ATOM   16507 N  N   . THR D  1 418 ? 4.696   -41.799 -39.587 1.00 61.28 ? 435  THR D N   1 
ATOM   16508 C  CA  . THR D  1 418 ? 3.976   -41.923 -40.849 1.00 61.46 ? 435  THR D CA  1 
ATOM   16509 C  C   . THR D  1 418 ? 4.857   -42.618 -41.886 1.00 58.96 ? 435  THR D C   1 
ATOM   16510 O  O   . THR D  1 418 ? 4.428   -43.585 -42.507 1.00 61.34 ? 435  THR D O   1 
ATOM   16511 C  CB  . THR D  1 418 ? 3.525   -40.547 -41.342 1.00 62.12 ? 435  THR D CB  1 
ATOM   16512 O  OG1 . THR D  1 418 ? 2.665   -40.024 -40.334 1.00 63.76 ? 435  THR D OG1 1 
ATOM   16513 C  CG2 . THR D  1 418 ? 2.751   -40.610 -42.647 1.00 62.90 ? 435  THR D CG2 1 
ATOM   16514 N  N   . LEU D  1 419 ? 6.091   -42.126 -42.048 1.00 57.05 ? 436  LEU D N   1 
ATOM   16515 C  CA  . LEU D  1 419 ? 6.962   -42.541 -43.138 1.00 56.05 ? 436  LEU D CA  1 
ATOM   16516 C  C   . LEU D  1 419 ? 7.633   -43.888 -42.853 1.00 56.59 ? 436  LEU D C   1 
ATOM   16517 O  O   . LEU D  1 419 ? 8.267   -44.445 -43.749 1.00 57.45 ? 436  LEU D O   1 
ATOM   16518 C  CB  . LEU D  1 419 ? 8.001   -41.452 -43.410 1.00 57.24 ? 436  LEU D CB  1 
ATOM   16519 C  CG  . LEU D  1 419 ? 7.555   -40.261 -44.268 1.00 58.95 ? 436  LEU D CG  1 
ATOM   16520 C  CD1 . LEU D  1 419 ? 7.405   -40.687 -45.720 1.00 59.79 ? 436  LEU D CD1 1 
ATOM   16521 C  CD2 . LEU D  1 419 ? 6.267   -39.616 -43.781 1.00 59.78 ? 436  LEU D CD2 1 
ATOM   16522 N  N   . THR D  1 420 ? 7.520   -44.404 -41.618 1.00 53.12 ? 437  THR D N   1 
ATOM   16523 C  CA  . THR D  1 420 ? 8.064   -45.715 -41.285 1.00 51.26 ? 437  THR D CA  1 
ATOM   16524 C  C   . THR D  1 420 ? 6.931   -46.714 -41.052 1.00 51.56 ? 437  THR D C   1 
ATOM   16525 O  O   . THR D  1 420 ? 7.191   -47.848 -40.654 1.00 49.81 ? 437  THR D O   1 
ATOM   16526 C  CB  . THR D  1 420 ? 8.979   -45.620 -40.061 1.00 49.20 ? 437  THR D CB  1 
ATOM   16527 O  OG1 . THR D  1 420 ? 8.169   -45.235 -38.955 1.00 47.34 ? 437  THR D OG1 1 
ATOM   16528 C  CG2 . THR D  1 420 ? 10.104  -44.618 -40.250 1.00 49.35 ? 437  THR D CG2 1 
ATOM   16529 N  N   . GLU D  1 421 ? 5.687   -46.284 -41.312 1.00 53.42 ? 438  GLU D N   1 
ATOM   16530 C  CA  . GLU D  1 421 ? 4.493   -47.080 -41.064 1.00 56.07 ? 438  GLU D CA  1 
ATOM   16531 C  C   . GLU D  1 421 ? 4.419   -47.471 -39.587 1.00 55.51 ? 438  GLU D C   1 
ATOM   16532 O  O   . GLU D  1 421 ? 4.015   -48.585 -39.260 1.00 53.60 ? 438  GLU D O   1 
ATOM   16533 C  CB  . GLU D  1 421 ? 4.420   -48.319 -41.961 1.00 58.27 ? 438  GLU D CB  1 
ATOM   16534 C  CG  . GLU D  1 421 ? 4.553   -48.017 -43.451 1.00 59.32 ? 438  GLU D CG  1 
ATOM   16535 C  CD  . GLU D  1 421 ? 4.088   -49.152 -44.349 1.00 60.55 ? 438  GLU D CD  1 
ATOM   16536 O  OE1 . GLU D  1 421 ? 2.871   -49.434 -44.364 1.00 60.58 ? 438  GLU D OE1 1 
ATOM   16537 O  OE2 . GLU D  1 421 ? 4.940   -49.765 -45.025 1.00 60.43 ? 438  GLU D OE2 1 
ATOM   16538 N  N   . GLY D  1 422 ? 4.808   -46.539 -38.707 1.00 56.70 ? 439  GLY D N   1 
ATOM   16539 C  CA  . GLY D  1 422 ? 4.686   -46.716 -37.268 1.00 54.44 ? 439  GLY D CA  1 
ATOM   16540 C  C   . GLY D  1 422 ? 5.631   -47.784 -36.715 1.00 53.46 ? 439  GLY D C   1 
ATOM   16541 O  O   . GLY D  1 422 ? 5.350   -48.371 -35.671 1.00 54.02 ? 439  GLY D O   1 
ATOM   16542 N  N   . ARG D  1 423 ? 6.756   -48.015 -37.404 1.00 49.68 ? 440  ARG D N   1 
ATOM   16543 C  CA  . ARG D  1 423 ? 7.712   -49.032 -36.993 1.00 49.27 ? 440  ARG D CA  1 
ATOM   16544 C  C   . ARG D  1 423 ? 8.910   -48.410 -36.275 1.00 48.17 ? 440  ARG D C   1 
ATOM   16545 O  O   . ARG D  1 423 ? 9.717   -49.135 -35.696 1.00 47.46 ? 440  ARG D O   1 
ATOM   16546 C  CB  . ARG D  1 423 ? 8.186   -49.842 -38.203 1.00 49.30 ? 440  ARG D CB  1 
ATOM   16547 C  CG  . ARG D  1 423 ? 7.117   -50.755 -38.787 1.00 48.69 ? 440  ARG D CG  1 
ATOM   16548 C  CD  . ARG D  1 423 ? 7.678   -51.685 -39.852 1.00 49.41 ? 440  ARG D CD  1 
ATOM   16549 N  NE  . ARG D  1 423 ? 8.060   -50.975 -41.079 1.00 48.55 ? 440  ARG D NE  1 
ATOM   16550 C  CZ  . ARG D  1 423 ? 9.277   -50.884 -41.615 1.00 49.12 ? 440  ARG D CZ  1 
ATOM   16551 N  NH1 . ARG D  1 423 ? 10.333  -51.410 -41.017 1.00 49.89 ? 440  ARG D NH1 1 
ATOM   16552 N  NH2 . ARG D  1 423 ? 9.437   -50.248 -42.764 1.00 48.96 ? 440  ARG D NH2 1 
ATOM   16553 N  N   . CYS D  1 424 ? 9.028   -47.077 -36.311 1.00 47.28 ? 441  CYS D N   1 
ATOM   16554 C  CA  . CYS D  1 424 ? 10.211  -46.411 -35.791 1.00 47.20 ? 441  CYS D CA  1 
ATOM   16555 C  C   . CYS D  1 424 ? 10.089  -46.220 -34.281 1.00 47.13 ? 441  CYS D C   1 
ATOM   16556 O  O   . CYS D  1 424 ? 8.987   -46.056 -33.756 1.00 46.71 ? 441  CYS D O   1 
ATOM   16557 C  CB  . CYS D  1 424 ? 10.444  -45.065 -36.464 1.00 47.38 ? 441  CYS D CB  1 
ATOM   16558 S  SG  . CYS D  1 424 ? 9.239   -43.794 -36.003 1.00 48.37 ? 441  CYS D SG  1 
ATOM   16559 N  N   . LEU D  1 425 ? 11.241  -46.270 -33.600 1.00 45.87 ? 442  LEU D N   1 
ATOM   16560 C  CA  . LEU D  1 425 ? 11.357  -45.814 -32.223 1.00 43.28 ? 442  LEU D CA  1 
ATOM   16561 C  C   . LEU D  1 425 ? 11.890  -44.385 -32.261 1.00 38.31 ? 442  LEU D C   1 
ATOM   16562 O  O   . LEU D  1 425 ? 13.008  -44.157 -32.713 1.00 36.95 ? 442  LEU D O   1 
ATOM   16563 C  CB  . LEU D  1 425 ? 12.270  -46.735 -31.411 1.00 42.67 ? 442  LEU D CB  1 
ATOM   16564 C  CG  . LEU D  1 425 ? 11.683  -48.084 -30.976 1.00 43.30 ? 442  LEU D CG  1 
ATOM   16565 C  CD1 . LEU D  1 425 ? 10.416  -47.902 -30.147 1.00 43.04 ? 442  LEU D CD1 1 
ATOM   16566 C  CD2 . LEU D  1 425 ? 11.417  -48.995 -32.166 1.00 43.80 ? 442  LEU D CD2 1 
ATOM   16567 N  N   . PHE D  1 426 ? 11.072  -43.429 -31.809 1.00 37.51 ? 443  PHE D N   1 
ATOM   16568 C  CA  . PHE D  1 426 ? 11.356  -42.023 -32.046 1.00 37.36 ? 443  PHE D CA  1 
ATOM   16569 C  C   . PHE D  1 426 ? 11.388  -41.253 -30.728 1.00 37.23 ? 443  PHE D C   1 
ATOM   16570 O  O   . PHE D  1 426 ? 10.588  -41.506 -29.828 1.00 37.96 ? 443  PHE D O   1 
ATOM   16571 C  CB  . PHE D  1 426 ? 10.319  -41.417 -32.997 1.00 37.32 ? 443  PHE D CB  1 
ATOM   16572 C  CG  . PHE D  1 426 ? 10.585  -39.952 -33.307 1.00 35.58 ? 443  PHE D CG  1 
ATOM   16573 C  CD1 . PHE D  1 426 ? 11.547  -39.588 -34.243 1.00 36.31 ? 443  PHE D CD1 1 
ATOM   16574 C  CD2 . PHE D  1 426 ? 9.904   -38.944 -32.634 1.00 35.66 ? 443  PHE D CD2 1 
ATOM   16575 C  CE1 . PHE D  1 426 ? 11.807  -38.250 -34.504 1.00 36.20 ? 443  PHE D CE1 1 
ATOM   16576 C  CE2 . PHE D  1 426 ? 10.168  -37.610 -32.902 1.00 34.84 ? 443  PHE D CE2 1 
ATOM   16577 C  CZ  . PHE D  1 426 ? 11.116  -37.265 -33.834 1.00 35.87 ? 443  PHE D CZ  1 
ATOM   16578 N  N   . ALA D  1 427 ? 12.328  -40.304 -30.648 1.00 37.65 ? 444  ALA D N   1 
ATOM   16579 C  CA  . ALA D  1 427 ? 12.395  -39.349 -29.556 1.00 38.99 ? 444  ALA D CA  1 
ATOM   16580 C  C   . ALA D  1 427 ? 12.900  -38.016 -30.094 1.00 38.55 ? 444  ALA D C   1 
ATOM   16581 O  O   . ALA D  1 427 ? 13.629  -37.978 -31.084 1.00 38.60 ? 444  ALA D O   1 
ATOM   16582 C  CB  . ALA D  1 427 ? 13.289  -39.866 -28.449 1.00 38.36 ? 444  ALA D CB  1 
ATOM   16583 N  N   . SER D  1 428 ? 12.508  -36.933 -29.415 1.00 39.12 ? 445  SER D N   1 
ATOM   16584 C  CA  . SER D  1 428 ? 12.886  -35.587 -29.811 1.00 40.07 ? 445  SER D CA  1 
ATOM   16585 C  C   . SER D  1 428 ? 13.325  -34.784 -28.590 1.00 39.42 ? 445  SER D C   1 
ATOM   16586 O  O   . SER D  1 428 ? 13.042  -35.165 -27.456 1.00 38.00 ? 445  SER D O   1 
ATOM   16587 C  CB  . SER D  1 428 ? 11.744  -34.898 -30.523 1.00 40.51 ? 445  SER D CB  1 
ATOM   16588 O  OG  . SER D  1 428 ? 10.569  -34.910 -29.721 1.00 40.73 ? 445  SER D OG  1 
ATOM   16589 N  N   . GLY D  1 429 ? 14.018  -33.671 -28.854 1.00 39.93 ? 446  GLY D N   1 
ATOM   16590 C  CA  . GLY D  1 429 ? 14.351  -32.688 -27.837 1.00 43.65 ? 446  GLY D CA  1 
ATOM   16591 C  C   . GLY D  1 429 ? 13.186  -31.733 -27.571 1.00 47.58 ? 446  GLY D C   1 
ATOM   16592 O  O   . GLY D  1 429 ? 13.055  -31.209 -26.467 1.00 49.07 ? 446  GLY D O   1 
ATOM   16593 N  N   . SER D  1 430 ? 12.344  -31.509 -28.590 1.00 49.91 ? 447  SER D N   1 
ATOM   16594 C  CA  . SER D  1 430 ? 11.248  -30.557 -28.494 1.00 51.59 ? 447  SER D CA  1 
ATOM   16595 C  C   . SER D  1 430 ? 9.915   -31.292 -28.350 1.00 52.81 ? 447  SER D C   1 
ATOM   16596 O  O   . SER D  1 430 ? 9.804   -32.454 -28.736 1.00 49.73 ? 447  SER D O   1 
ATOM   16597 C  CB  . SER D  1 430 ? 11.250  -29.627 -29.680 1.00 53.13 ? 447  SER D CB  1 
ATOM   16598 O  OG  . SER D  1 430 ? 11.425  -30.343 -30.894 1.00 54.66 ? 447  SER D OG  1 
ATOM   16599 N  N   . PRO D  1 431 ? 8.859   -30.645 -27.797 1.00 57.30 ? 448  PRO D N   1 
ATOM   16600 C  CA  . PRO D  1 431 ? 7.612   -31.340 -27.469 1.00 59.72 ? 448  PRO D CA  1 
ATOM   16601 C  C   . PRO D  1 431 ? 6.754   -31.646 -28.697 1.00 60.73 ? 448  PRO D C   1 
ATOM   16602 O  O   . PRO D  1 431 ? 6.737   -30.878 -29.657 1.00 61.83 ? 448  PRO D O   1 
ATOM   16603 C  CB  . PRO D  1 431 ? 6.893   -30.383 -26.487 1.00 59.15 ? 448  PRO D CB  1 
ATOM   16604 C  CG  . PRO D  1 431 ? 7.862   -29.229 -26.263 1.00 59.26 ? 448  PRO D CG  1 
ATOM   16605 C  CD  . PRO D  1 431 ? 8.795   -29.213 -27.463 1.00 58.41 ? 448  PRO D CD  1 
ATOM   16606 N  N   . PHE D  1 432 ? 6.046   -32.781 -28.641 1.00 59.87 ? 449  PHE D N   1 
ATOM   16607 C  CA  . PHE D  1 432 ? 5.170   -33.232 -29.712 1.00 59.52 ? 449  PHE D CA  1 
ATOM   16608 C  C   . PHE D  1 432 ? 4.004   -33.998 -29.089 1.00 62.39 ? 449  PHE D C   1 
ATOM   16609 O  O   . PHE D  1 432 ? 4.201   -34.779 -28.158 1.00 61.53 ? 449  PHE D O   1 
ATOM   16610 C  CB  . PHE D  1 432 ? 5.929   -34.119 -30.708 1.00 57.70 ? 449  PHE D CB  1 
ATOM   16611 C  CG  . PHE D  1 432 ? 6.907   -33.418 -31.646 1.00 54.55 ? 449  PHE D CG  1 
ATOM   16612 C  CD1 . PHE D  1 432 ? 6.538   -32.280 -32.357 1.00 53.05 ? 449  PHE D CD1 1 
ATOM   16613 C  CD2 . PHE D  1 432 ? 8.198   -33.909 -31.825 1.00 53.04 ? 449  PHE D CD2 1 
ATOM   16614 C  CE1 . PHE D  1 432 ? 7.436   -31.652 -33.212 1.00 51.97 ? 449  PHE D CE1 1 
ATOM   16615 C  CE2 . PHE D  1 432 ? 9.091   -33.277 -32.680 1.00 51.78 ? 449  PHE D CE2 1 
ATOM   16616 C  CZ  . PHE D  1 432 ? 8.708   -32.151 -33.372 1.00 51.47 ? 449  PHE D CZ  1 
ATOM   16617 N  N   . GLY D  1 433 ? 2.794   -33.771 -29.619 1.00 62.47 ? 450  GLY D N   1 
ATOM   16618 C  CA  . GLY D  1 433 ? 1.587   -34.395 -29.100 1.00 61.48 ? 450  GLY D CA  1 
ATOM   16619 C  C   . GLY D  1 433 ? 1.404   -35.805 -29.657 1.00 61.65 ? 450  GLY D C   1 
ATOM   16620 O  O   . GLY D  1 433 ? 2.095   -36.192 -30.598 1.00 63.32 ? 450  GLY D O   1 
ATOM   16621 N  N   . PRO D  1 434 ? 0.473   -36.615 -29.100 1.00 63.15 ? 451  PRO D N   1 
ATOM   16622 C  CA  . PRO D  1 434 ? 0.218   -37.963 -29.615 1.00 65.61 ? 451  PRO D CA  1 
ATOM   16623 C  C   . PRO D  1 434 ? -0.115  -37.932 -31.106 1.00 66.63 ? 451  PRO D C   1 
ATOM   16624 O  O   . PRO D  1 434 ? -0.780  -37.009 -31.573 1.00 65.65 ? 451  PRO D O   1 
ATOM   16625 C  CB  . PRO D  1 434 ? -0.954  -38.475 -28.755 1.00 64.06 ? 451  PRO D CB  1 
ATOM   16626 C  CG  . PRO D  1 434 ? -0.878  -37.645 -27.490 1.00 63.81 ? 451  PRO D CG  1 
ATOM   16627 C  CD  . PRO D  1 434 ? -0.377  -36.283 -27.944 1.00 63.63 ? 451  PRO D CD  1 
ATOM   16628 N  N   . VAL D  1 435 ? 0.375   -38.940 -31.841 1.00 68.11 ? 452  VAL D N   1 
ATOM   16629 C  CA  . VAL D  1 435 ? 0.192   -39.032 -33.282 1.00 66.74 ? 452  VAL D CA  1 
ATOM   16630 C  C   . VAL D  1 435 ? -0.450  -40.387 -33.624 1.00 65.59 ? 452  VAL D C   1 
ATOM   16631 O  O   . VAL D  1 435 ? -0.593  -41.206 -32.693 1.00 63.32 ? 452  VAL D O   1 
ATOM   16632 C  CB  . VAL D  1 435 ? 1.529   -38.837 -34.025 1.00 66.25 ? 452  VAL D CB  1 
ATOM   16633 C  CG1 . VAL D  1 435 ? 1.472   -39.347 -35.460 1.00 65.99 ? 452  VAL D CG1 1 
ATOM   16634 C  CG2 . VAL D  1 435 ? 1.982   -37.382 -33.990 1.00 65.96 ? 452  VAL D CG2 1 
ATOM   16635 N  N   . ARG D  1 441 ? -4.324  -46.747 -34.225 1.00 68.12 ? 458  ARG D N   1 
ATOM   16636 C  CA  . ARG D  1 441 ? -2.933  -46.811 -33.696 1.00 68.83 ? 458  ARG D CA  1 
ATOM   16637 C  C   . ARG D  1 441 ? -2.453  -45.404 -33.346 1.00 67.67 ? 458  ARG D C   1 
ATOM   16638 O  O   . ARG D  1 441 ? -2.282  -44.564 -34.226 1.00 67.56 ? 458  ARG D O   1 
ATOM   16639 C  CB  . ARG D  1 441 ? -1.967  -47.482 -34.681 1.00 68.14 ? 458  ARG D CB  1 
ATOM   16640 C  CG  . ARG D  1 441 ? -1.642  -48.934 -34.362 1.00 67.71 ? 458  ARG D CG  1 
ATOM   16641 C  CD  . ARG D  1 441 ? -0.849  -49.662 -35.447 1.00 68.52 ? 458  ARG D CD  1 
ATOM   16642 N  NE  . ARG D  1 441 ? -0.109  -48.797 -36.377 1.00 70.14 ? 458  ARG D NE  1 
ATOM   16643 C  CZ  . ARG D  1 441 ? 0.938   -49.144 -37.127 1.00 72.80 ? 458  ARG D CZ  1 
ATOM   16644 N  NH1 . ARG D  1 441 ? 1.545   -50.308 -36.960 1.00 73.24 ? 458  ARG D NH1 1 
ATOM   16645 N  NH2 . ARG D  1 441 ? 1.406   -48.295 -38.028 1.00 73.55 ? 458  ARG D NH2 1 
ATOM   16646 N  N   . VAL D  1 442 ? -2.234  -45.170 -32.047 1.00 67.12 ? 459  VAL D N   1 
ATOM   16647 C  CA  . VAL D  1 442 ? -1.787  -43.880 -31.549 1.00 65.82 ? 459  VAL D CA  1 
ATOM   16648 C  C   . VAL D  1 442 ? -0.379  -44.044 -30.975 1.00 64.78 ? 459  VAL D C   1 
ATOM   16649 O  O   . VAL D  1 442 ? -0.126  -44.970 -30.208 1.00 64.07 ? 459  VAL D O   1 
ATOM   16650 C  CB  . VAL D  1 442 ? -2.779  -43.344 -30.499 1.00 66.13 ? 459  VAL D CB  1 
ATOM   16651 C  CG1 . VAL D  1 442 ? -2.514  -41.882 -30.155 1.00 65.82 ? 459  VAL D CG1 1 
ATOM   16652 C  CG2 . VAL D  1 442 ? -4.227  -43.524 -30.944 1.00 67.28 ? 459  VAL D CG2 1 
ATOM   16653 N  N   . PHE D  1 443 ? 0.535   -43.149 -31.373 1.00 66.20 ? 460  PHE D N   1 
ATOM   16654 C  CA  . PHE D  1 443 ? 1.904   -43.143 -30.879 1.00 68.22 ? 460  PHE D CA  1 
ATOM   16655 C  C   . PHE D  1 443 ? 2.137   -41.875 -30.058 1.00 66.87 ? 460  PHE D C   1 
ATOM   16656 O  O   . PHE D  1 443 ? 1.921   -40.771 -30.553 1.00 67.05 ? 460  PHE D O   1 
ATOM   16657 C  CB  . PHE D  1 443 ? 2.884   -43.246 -32.053 1.00 68.01 ? 460  PHE D CB  1 
ATOM   16658 C  CG  . PHE D  1 443 ? 2.867   -44.579 -32.790 1.00 68.87 ? 460  PHE D CG  1 
ATOM   16659 C  CD1 . PHE D  1 443 ? 3.701   -45.623 -32.399 1.00 68.95 ? 460  PHE D CD1 1 
ATOM   16660 C  CD2 . PHE D  1 443 ? 2.023   -44.785 -33.878 1.00 69.45 ? 460  PHE D CD2 1 
ATOM   16661 C  CE1 . PHE D  1 443 ? 3.687   -46.835 -33.074 1.00 68.39 ? 460  PHE D CE1 1 
ATOM   16662 C  CE2 . PHE D  1 443 ? 2.013   -46.001 -34.548 1.00 68.23 ? 460  PHE D CE2 1 
ATOM   16663 C  CZ  . PHE D  1 443 ? 2.844   -47.022 -34.146 1.00 67.68 ? 460  PHE D CZ  1 
ATOM   16664 N  N   . THR D  1 444 ? 2.580   -42.053 -28.804 1.00 65.26 ? 461  THR D N   1 
ATOM   16665 C  CA  . THR D  1 444 ? 2.862   -40.951 -27.894 1.00 61.26 ? 461  THR D CA  1 
ATOM   16666 C  C   . THR D  1 444 ? 4.377   -40.790 -27.762 1.00 57.49 ? 461  THR D C   1 
ATOM   16667 O  O   . THR D  1 444 ? 5.001   -41.459 -26.939 1.00 56.07 ? 461  THR D O   1 
ATOM   16668 C  CB  . THR D  1 444 ? 2.208   -41.232 -26.540 1.00 61.83 ? 461  THR D CB  1 
ATOM   16669 O  OG1 . THR D  1 444 ? 0.825   -41.453 -26.801 1.00 62.89 ? 461  THR D OG1 1 
ATOM   16670 C  CG2 . THR D  1 444 ? 2.360   -40.079 -25.564 1.00 61.92 ? 461  THR D CG2 1 
ATOM   16671 N  N   . PRO D  1 445 ? 5.023   -39.906 -28.559 1.00 53.33 ? 462  PRO D N   1 
ATOM   16672 C  CA  . PRO D  1 445 ? 6.480   -39.769 -28.523 1.00 52.95 ? 462  PRO D CA  1 
ATOM   16673 C  C   . PRO D  1 445 ? 6.969   -39.056 -27.263 1.00 51.54 ? 462  PRO D C   1 
ATOM   16674 O  O   . PRO D  1 445 ? 6.266   -38.215 -26.703 1.00 50.48 ? 462  PRO D O   1 
ATOM   16675 C  CB  . PRO D  1 445 ? 6.776   -38.975 -29.804 1.00 52.27 ? 462  PRO D CB  1 
ATOM   16676 C  CG  . PRO D  1 445 ? 5.548   -38.116 -29.986 1.00 52.54 ? 462  PRO D CG  1 
ATOM   16677 C  CD  . PRO D  1 445 ? 4.395   -38.988 -29.522 1.00 52.87 ? 462  PRO D CD  1 
ATOM   16678 N  N   . GLY D  1 446 ? 8.185   -39.411 -26.833 1.00 50.82 ? 463  GLY D N   1 
ATOM   16679 C  CA  . GLY D  1 446 ? 8.778   -38.866 -25.623 1.00 48.47 ? 463  GLY D CA  1 
ATOM   16680 C  C   . GLY D  1 446 ? 9.797   -37.777 -25.946 1.00 45.96 ? 463  GLY D C   1 
ATOM   16681 O  O   . GLY D  1 446 ? 10.419  -37.794 -27.009 1.00 42.61 ? 463  GLY D O   1 
ATOM   16682 N  N   . GLN D  1 447 ? 9.958   -36.843 -25.001 1.00 44.25 ? 464  GLN D N   1 
ATOM   16683 C  CA  . GLN D  1 447 ? 10.880  -35.727 -25.136 1.00 42.61 ? 464  GLN D CA  1 
ATOM   16684 C  C   . GLN D  1 447 ? 12.080  -35.969 -24.223 1.00 36.74 ? 464  GLN D C   1 
ATOM   16685 O  O   . GLN D  1 447 ? 11.906  -36.159 -23.024 1.00 35.59 ? 464  GLN D O   1 
ATOM   16686 C  CB  . GLN D  1 447 ? 10.162  -34.435 -24.742 1.00 46.13 ? 464  GLN D CB  1 
ATOM   16687 C  CG  . GLN D  1 447 ? 10.956  -33.166 -25.035 1.00 50.04 ? 464  GLN D CG  1 
ATOM   16688 C  CD  . GLN D  1 447 ? 10.606  -32.000 -24.130 1.00 54.72 ? 464  GLN D CD  1 
ATOM   16689 O  OE1 . GLN D  1 447 ? 9.746   -32.093 -23.245 1.00 56.48 ? 464  GLN D OE1 1 
ATOM   16690 N  NE2 . GLN D  1 447 ? 11.293  -30.885 -24.337 1.00 54.66 ? 464  GLN D NE2 1 
ATOM   16691 N  N   . GLY D  1 448 ? 13.291  -35.945 -24.793 1.00 33.57 ? 465  GLY D N   1 
ATOM   16692 C  CA  . GLY D  1 448 ? 14.509  -36.226 -24.047 1.00 34.11 ? 465  GLY D CA  1 
ATOM   16693 C  C   . GLY D  1 448 ? 15.011  -35.000 -23.284 1.00 32.18 ? 465  GLY D C   1 
ATOM   16694 O  O   . GLY D  1 448 ? 16.043  -34.425 -23.623 1.00 36.47 ? 465  GLY D O   1 
ATOM   16695 N  N   . ASN D  1 449 ? 14.281  -34.634 -22.232 1.00 28.57 ? 466  ASN D N   1 
ATOM   16696 C  CA  . ASN D  1 449 ? 14.535  -33.423 -21.467 1.00 27.81 ? 466  ASN D CA  1 
ATOM   16697 C  C   . ASN D  1 449 ? 15.616  -33.681 -20.417 1.00 26.14 ? 466  ASN D C   1 
ATOM   16698 O  O   . ASN D  1 449 ? 15.523  -34.647 -19.671 1.00 25.37 ? 466  ASN D O   1 
ATOM   16699 C  CB  . ASN D  1 449 ? 13.253  -32.961 -20.788 1.00 27.49 ? 466  ASN D CB  1 
ATOM   16700 C  CG  . ASN D  1 449 ? 13.297  -31.505 -20.400 1.00 28.83 ? 466  ASN D CG  1 
ATOM   16701 O  OD1 . ASN D  1 449 ? 14.247  -31.064 -19.746 1.00 24.91 ? 466  ASN D OD1 1 
ATOM   16702 N  ND2 . ASN D  1 449 ? 12.286  -30.746 -20.802 1.00 30.77 ? 466  ASN D ND2 1 
ATOM   16703 N  N   . ASN D  1 450 ? 16.604  -32.784 -20.326 1.00 25.82 ? 467  ASN D N   1 
ATOM   16704 C  CA  . ASN D  1 450 ? 17.676  -32.905 -19.344 1.00 27.57 ? 467  ASN D CA  1 
ATOM   16705 C  C   . ASN D  1 450 ? 17.161  -32.905 -17.901 1.00 25.53 ? 467  ASN D C   1 
ATOM   16706 O  O   . ASN D  1 450 ? 17.856  -33.407 -17.019 1.00 24.59 ? 467  ASN D O   1 
ATOM   16707 C  CB  . ASN D  1 450 ? 18.734  -31.822 -19.517 1.00 28.96 ? 467  ASN D CB  1 
ATOM   16708 C  CG  . ASN D  1 450 ? 19.699  -32.136 -20.635 1.00 31.34 ? 467  ASN D CG  1 
ATOM   16709 O  OD1 . ASN D  1 450 ? 19.379  -32.905 -21.550 1.00 33.91 ? 467  ASN D OD1 1 
ATOM   16710 N  ND2 . ASN D  1 450 ? 20.884  -31.551 -20.580 1.00 30.80 ? 467  ASN D ND2 1 
ATOM   16711 N  N   . VAL D  1 451 ? 15.961  -32.361 -17.646 1.00 23.25 ? 468  VAL D N   1 
ATOM   16712 C  CA  . VAL D  1 451 ? 15.431  -32.297 -16.287 1.00 23.86 ? 468  VAL D CA  1 
ATOM   16713 C  C   . VAL D  1 451 ? 15.235  -33.702 -15.704 1.00 22.60 ? 468  VAL D C   1 
ATOM   16714 O  O   . VAL D  1 451 ? 15.105  -33.856 -14.493 1.00 22.89 ? 468  VAL D O   1 
ATOM   16715 C  CB  . VAL D  1 451 ? 14.118  -31.489 -16.191 1.00 23.73 ? 468  VAL D CB  1 
ATOM   16716 C  CG1 . VAL D  1 451 ? 12.939  -32.204 -16.847 1.00 23.82 ? 468  VAL D CG1 1 
ATOM   16717 C  CG2 . VAL D  1 451 ? 13.781  -31.133 -14.745 1.00 23.86 ? 468  VAL D CG2 1 
ATOM   16718 N  N   . TYR D  1 452 ? 15.185  -34.726 -16.560 1.00 22.38 ? 469  TYR D N   1 
ATOM   16719 C  CA  . TYR D  1 452 ? 15.064  -36.103 -16.104 1.00 22.47 ? 469  TYR D CA  1 
ATOM   16720 C  C   . TYR D  1 452 ? 16.265  -36.547 -15.269 1.00 21.44 ? 469  TYR D C   1 
ATOM   16721 O  O   . TYR D  1 452 ? 16.114  -37.446 -14.449 1.00 21.60 ? 469  TYR D O   1 
ATOM   16722 C  CB  . TYR D  1 452 ? 14.916  -37.051 -17.299 1.00 23.17 ? 469  TYR D CB  1 
ATOM   16723 C  CG  . TYR D  1 452 ? 13.525  -37.088 -17.915 1.00 23.64 ? 469  TYR D CG  1 
ATOM   16724 C  CD1 . TYR D  1 452 ? 12.405  -37.391 -17.149 1.00 23.81 ? 469  TYR D CD1 1 
ATOM   16725 C  CD2 . TYR D  1 452 ? 13.332  -36.799 -19.262 1.00 24.39 ? 469  TYR D CD2 1 
ATOM   16726 C  CE1 . TYR D  1 452 ? 11.136  -37.423 -17.707 1.00 25.07 ? 469  TYR D CE1 1 
ATOM   16727 C  CE2 . TYR D  1 452 ? 12.069  -36.818 -19.828 1.00 25.09 ? 469  TYR D CE2 1 
ATOM   16728 C  CZ  . TYR D  1 452 ? 10.969  -37.138 -19.051 1.00 25.45 ? 469  TYR D CZ  1 
ATOM   16729 O  OH  . TYR D  1 452 ? 9.731   -37.164 -19.627 1.00 26.97 ? 469  TYR D OH  1 
ATOM   16730 N  N   . ILE D  1 453 ? 17.441  -35.940 -15.484 1.00 21.37 ? 470  ILE D N   1 
ATOM   16731 C  CA  . ILE D  1 453 ? 18.693  -36.459 -14.944 1.00 21.64 ? 470  ILE D CA  1 
ATOM   16732 C  C   . ILE D  1 453 ? 19.238  -35.564 -13.823 1.00 21.86 ? 470  ILE D C   1 
ATOM   16733 O  O   . ILE D  1 453 ? 19.505  -36.067 -12.734 1.00 22.66 ? 470  ILE D O   1 
ATOM   16734 C  CB  . ILE D  1 453 ? 19.729  -36.661 -16.069 1.00 21.70 ? 470  ILE D CB  1 
ATOM   16735 C  CG1 . ILE D  1 453 ? 19.287  -37.743 -17.076 1.00 22.45 ? 470  ILE D CG1 1 
ATOM   16736 C  CG2 . ILE D  1 453 ? 21.117  -36.965 -15.501 1.00 22.04 ? 470  ILE D CG2 1 
ATOM   16737 C  CD1 . ILE D  1 453 ? 19.131  -39.137 -16.491 1.00 22.62 ? 470  ILE D CD1 1 
ATOM   16738 N  N   . PHE D  1 454 ? 19.432  -34.260 -14.080 1.00 21.81 ? 471  PHE D N   1 
ATOM   16739 C  CA  . PHE D  1 454 ? 20.274  -33.438 -13.216 1.00 21.56 ? 471  PHE D CA  1 
ATOM   16740 C  C   . PHE D  1 454 ? 19.696  -33.342 -11.798 1.00 21.20 ? 471  PHE D C   1 
ATOM   16741 O  O   . PHE D  1 454 ? 20.459  -33.443 -10.838 1.00 20.50 ? 471  PHE D O   1 
ATOM   16742 C  CB  . PHE D  1 454 ? 20.651  -32.072 -13.814 1.00 21.77 ? 471  PHE D CB  1 
ATOM   16743 C  CG  . PHE D  1 454 ? 19.539  -31.062 -14.055 1.00 22.36 ? 471  PHE D CG  1 
ATOM   16744 C  CD1 . PHE D  1 454 ? 19.017  -30.312 -13.006 1.00 22.64 ? 471  PHE D CD1 1 
ATOM   16745 C  CD2 . PHE D  1 454 ? 19.030  -30.849 -15.333 1.00 22.53 ? 471  PHE D CD2 1 
ATOM   16746 C  CE1 . PHE D  1 454 ? 17.995  -29.403 -13.223 1.00 22.97 ? 471  PHE D CE1 1 
ATOM   16747 C  CE2 . PHE D  1 454 ? 18.016  -29.927 -15.549 1.00 22.71 ? 471  PHE D CE2 1 
ATOM   16748 C  CZ  . PHE D  1 454 ? 17.495  -29.211 -14.492 1.00 23.94 ? 471  PHE D CZ  1 
ATOM   16749 N  N   . PRO D  1 455 ? 18.371  -33.159 -11.563 1.00 20.99 ? 472  PRO D N   1 
ATOM   16750 C  CA  . PRO D  1 455 ? 17.869  -33.039 -10.190 1.00 20.70 ? 472  PRO D CA  1 
ATOM   16751 C  C   . PRO D  1 455 ? 18.201  -34.240 -9.305  1.00 20.44 ? 472  PRO D C   1 
ATOM   16752 O  O   . PRO D  1 455 ? 18.670  -34.066 -8.185  1.00 20.50 ? 472  PRO D O   1 
ATOM   16753 C  CB  . PRO D  1 455 ? 16.346  -32.835 -10.352 1.00 20.76 ? 472  PRO D CB  1 
ATOM   16754 C  CG  . PRO D  1 455 ? 16.194  -32.333 -11.781 1.00 20.85 ? 472  PRO D CG  1 
ATOM   16755 C  CD  . PRO D  1 455 ? 17.296  -33.045 -12.557 1.00 21.05 ? 472  PRO D CD  1 
ATOM   16756 N  N   . GLY D  1 456 ? 17.967  -35.452 -9.823  1.00 20.77 ? 473  GLY D N   1 
ATOM   16757 C  CA  . GLY D  1 456 ? 18.174  -36.677 -9.063  1.00 21.04 ? 473  GLY D CA  1 
ATOM   16758 C  C   . GLY D  1 456 ? 19.651  -36.948 -8.783  1.00 20.95 ? 473  GLY D C   1 
ATOM   16759 O  O   . GLY D  1 456 ? 20.006  -37.366 -7.681  1.00 21.98 ? 473  GLY D O   1 
ATOM   16760 N  N   . VAL D  1 457 ? 20.508  -36.718 -9.785  1.00 20.52 ? 474  VAL D N   1 
ATOM   16761 C  CA  . VAL D  1 457 ? 21.945  -36.890 -9.615  1.00 20.48 ? 474  VAL D CA  1 
ATOM   16762 C  C   . VAL D  1 457 ? 22.459  -35.908 -8.559  1.00 20.38 ? 474  VAL D C   1 
ATOM   16763 O  O   . VAL D  1 457 ? 23.204  -36.297 -7.650  1.00 18.71 ? 474  VAL D O   1 
ATOM   16764 C  CB  . VAL D  1 457 ? 22.688  -36.749 -10.955 1.00 21.40 ? 474  VAL D CB  1 
ATOM   16765 C  CG1 . VAL D  1 457 ? 24.204  -36.668 -10.792 1.00 22.20 ? 474  VAL D CG1 1 
ATOM   16766 C  CG2 . VAL D  1 457 ? 22.321  -37.893 -11.897 1.00 21.91 ? 474  VAL D CG2 1 
ATOM   16767 N  N   . ALA D  1 458 ? 22.038  -34.642 -8.663  1.00 19.62 ? 475  ALA D N   1 
ATOM   16768 C  CA  . ALA D  1 458 ? 22.523  -33.611 -7.755  1.00 19.67 ? 475  ALA D CA  1 
ATOM   16769 C  C   . ALA D  1 458 ? 22.122  -33.941 -6.319  1.00 19.62 ? 475  ALA D C   1 
ATOM   16770 O  O   . ALA D  1 458 ? 22.929  -33.788 -5.411  1.00 20.17 ? 475  ALA D O   1 
ATOM   16771 C  CB  . ALA D  1 458 ? 22.018  -32.253 -8.173  1.00 19.57 ? 475  ALA D CB  1 
ATOM   16772 N  N   . LEU D  1 459 ? 20.881  -34.399 -6.120  1.00 20.15 ? 476  LEU D N   1 
ATOM   16773 C  CA  . LEU D  1 459 ? 20.402  -34.718 -4.786  1.00 20.32 ? 476  LEU D CA  1 
ATOM   16774 C  C   . LEU D  1 459 ? 21.235  -35.854 -4.189  1.00 20.30 ? 476  LEU D C   1 
ATOM   16775 O  O   . LEU D  1 459 ? 21.698  -35.744 -3.061  1.00 20.69 ? 476  LEU D O   1 
ATOM   16776 C  CB  . LEU D  1 459 ? 18.915  -35.060 -4.809  1.00 20.77 ? 476  LEU D CB  1 
ATOM   16777 C  CG  . LEU D  1 459 ? 18.316  -35.482 -3.464  1.00 20.62 ? 476  LEU D CG  1 
ATOM   16778 C  CD1 . LEU D  1 459 ? 18.352  -34.344 -2.458  1.00 20.73 ? 476  LEU D CD1 1 
ATOM   16779 C  CD2 . LEU D  1 459 ? 16.906  -35.990 -3.638  1.00 20.79 ? 476  LEU D CD2 1 
ATOM   16780 N  N   . ALA D  1 460 ? 21.446  -36.934 -4.953  1.00 20.03 ? 477  ALA D N   1 
ATOM   16781 C  CA  . ALA D  1 460 ? 22.179  -38.085 -4.452  1.00 20.15 ? 477  ALA D CA  1 
ATOM   16782 C  C   . ALA D  1 460 ? 23.607  -37.696 -4.068  1.00 20.15 ? 477  ALA D C   1 
ATOM   16783 O  O   . ALA D  1 460 ? 24.109  -38.125 -3.032  1.00 20.84 ? 477  ALA D O   1 
ATOM   16784 C  CB  . ALA D  1 460 ? 22.175  -39.188 -5.486  1.00 20.58 ? 477  ALA D CB  1 
ATOM   16785 N  N   . VAL D  1 461 ? 24.261  -36.898 -4.920  1.00 19.81 ? 478  VAL D N   1 
ATOM   16786 C  CA  . VAL D  1 461 ? 25.627  -36.460 -4.684  1.00 19.42 ? 478  VAL D CA  1 
ATOM   16787 C  C   . VAL D  1 461 ? 25.699  -35.658 -3.382  1.00 19.59 ? 478  VAL D C   1 
ATOM   16788 O  O   . VAL D  1 461 ? 26.587  -35.883 -2.556  1.00 18.28 ? 478  VAL D O   1 
ATOM   16789 C  CB  . VAL D  1 461 ? 26.131  -35.663 -5.903  1.00 19.85 ? 478  VAL D CB  1 
ATOM   16790 C  CG1 . VAL D  1 461 ? 27.362  -34.826 -5.595  1.00 20.77 ? 478  VAL D CG1 1 
ATOM   16791 C  CG2 . VAL D  1 461 ? 26.397  -36.575 -7.095  1.00 20.12 ? 478  VAL D CG2 1 
ATOM   16792 N  N   . ILE D  1 462 ? 24.739  -34.745 -3.193  1.00 19.23 ? 479  ILE D N   1 
ATOM   16793 C  CA  . ILE D  1 462 ? 24.712  -33.877 -2.025  1.00 19.48 ? 479  ILE D CA  1 
ATOM   16794 C  C   . ILE D  1 462 ? 24.467  -34.693 -0.749  1.00 19.96 ? 479  ILE D C   1 
ATOM   16795 O  O   . ILE D  1 462 ? 25.194  -34.527 0.231   1.00 19.68 ? 479  ILE D O   1 
ATOM   16796 C  CB  . ILE D  1 462 ? 23.676  -32.752 -2.218  1.00 19.50 ? 479  ILE D CB  1 
ATOM   16797 C  CG1 . ILE D  1 462 ? 24.168  -31.724 -3.241  1.00 19.18 ? 479  ILE D CG1 1 
ATOM   16798 C  CG2 . ILE D  1 462 ? 23.321  -32.081 -0.888  1.00 19.78 ? 479  ILE D CG2 1 
ATOM   16799 C  CD1 . ILE D  1 462 ? 23.092  -30.757 -3.706  1.00 19.68 ? 479  ILE D CD1 1 
ATOM   16800 N  N   . LEU D  1 463 ? 23.450  -35.567 -0.752  1.00 20.43 ? 480  LEU D N   1 
ATOM   16801 C  CA  . LEU D  1 463 ? 23.073  -36.305 0.447   1.00 20.46 ? 480  LEU D CA  1 
ATOM   16802 C  C   . LEU D  1 463 ? 24.175  -37.289 0.852   1.00 20.93 ? 480  LEU D C   1 
ATOM   16803 O  O   . LEU D  1 463 ? 24.264  -37.656 2.024   1.00 21.40 ? 480  LEU D O   1 
ATOM   16804 C  CB  . LEU D  1 463 ? 21.734  -37.024 0.268   1.00 20.88 ? 480  LEU D CB  1 
ATOM   16805 C  CG  . LEU D  1 463 ? 20.490  -36.149 0.074   1.00 21.81 ? 480  LEU D CG  1 
ATOM   16806 C  CD1 . LEU D  1 463 ? 19.256  -37.018 -0.073  1.00 22.32 ? 480  LEU D CD1 1 
ATOM   16807 C  CD2 . LEU D  1 463 ? 20.283  -35.151 1.199   1.00 22.25 ? 480  LEU D CD2 1 
ATOM   16808 N  N   . CYS D  1 464 ? 25.015  -37.702 -0.110  1.00 20.66 ? 481  CYS D N   1 
ATOM   16809 C  CA  . CYS D  1 464 ? 26.059  -38.690 0.130   1.00 21.13 ? 481  CYS D CA  1 
ATOM   16810 C  C   . CYS D  1 464 ? 27.389  -38.042 0.514   1.00 21.47 ? 481  CYS D C   1 
ATOM   16811 O  O   . CYS D  1 464 ? 28.353  -38.750 0.814   1.00 19.74 ? 481  CYS D O   1 
ATOM   16812 C  CB  . CYS D  1 464 ? 26.282  -39.556 -1.105  1.00 21.42 ? 481  CYS D CB  1 
ATOM   16813 S  SG  . CYS D  1 464 ? 24.955  -40.751 -1.406  1.00 22.30 ? 481  CYS D SG  1 
ATOM   16814 N  N   . ASN D  1 465 ? 27.443  -36.702 0.492   1.00 21.57 ? 482  ASN D N   1 
ATOM   16815 C  CA  . ASN D  1 465 ? 28.686  -35.962 0.673   1.00 22.26 ? 482  ASN D CA  1 
ATOM   16816 C  C   . ASN D  1 465 ? 29.746  -36.453 -0.314  1.00 21.51 ? 482  ASN D C   1 
ATOM   16817 O  O   . ASN D  1 465 ? 30.920  -36.574 0.041   1.00 22.04 ? 482  ASN D O   1 
ATOM   16818 C  CB  . ASN D  1 465 ? 29.196  -36.040 2.110   1.00 23.38 ? 482  ASN D CB  1 
ATOM   16819 C  CG  . ASN D  1 465 ? 28.249  -35.425 3.112   1.00 24.43 ? 482  ASN D CG  1 
ATOM   16820 O  OD1 . ASN D  1 465 ? 27.464  -34.530 2.777   1.00 27.25 ? 482  ASN D OD1 1 
ATOM   16821 N  ND2 . ASN D  1 465 ? 28.348  -35.845 4.362   1.00 25.28 ? 482  ASN D ND2 1 
ATOM   16822 N  N   . THR D  1 466 ? 29.327  -36.728 -1.558  1.00 21.35 ? 483  THR D N   1 
ATOM   16823 C  CA  . THR D  1 466 ? 30.238  -37.172 -2.606  1.00 21.33 ? 483  THR D CA  1 
ATOM   16824 C  C   . THR D  1 466 ? 31.136  -36.003 -3.020  1.00 21.10 ? 483  THR D C   1 
ATOM   16825 O  O   . THR D  1 466 ? 30.731  -34.847 -2.958  1.00 20.52 ? 483  THR D O   1 
ATOM   16826 C  CB  . THR D  1 466 ? 29.413  -37.738 -3.767  1.00 22.29 ? 483  THR D CB  1 
ATOM   16827 O  OG1 . THR D  1 466 ? 28.970  -39.028 -3.355  1.00 22.45 ? 483  THR D OG1 1 
ATOM   16828 C  CG2 . THR D  1 466 ? 30.201  -37.897 -5.053  1.00 22.40 ? 483  THR D CG2 1 
ATOM   16829 N  N   . ARG D  1 467 ? 32.366  -36.316 -3.437  1.00 21.27 ? 484  ARG D N   1 
ATOM   16830 C  CA  . ARG D  1 467 ? 33.383  -35.308 -3.684  1.00 22.16 ? 484  ARG D CA  1 
ATOM   16831 C  C   . ARG D  1 467 ? 33.764  -35.227 -5.161  1.00 22.63 ? 484  ARG D C   1 
ATOM   16832 O  O   . ARG D  1 467 ? 34.286  -34.202 -5.590  1.00 23.38 ? 484  ARG D O   1 
ATOM   16833 C  CB  . ARG D  1 467 ? 34.642  -35.603 -2.864  1.00 23.81 ? 484  ARG D CB  1 
ATOM   16834 C  CG  . ARG D  1 467 ? 34.381  -35.765 -1.374  1.00 25.05 ? 484  ARG D CG  1 
ATOM   16835 C  CD  . ARG D  1 467 ? 35.627  -36.218 -0.643  1.00 27.07 ? 484  ARG D CD  1 
ATOM   16836 N  NE  . ARG D  1 467 ? 36.607  -35.146 -0.443  1.00 27.98 ? 484  ARG D NE  1 
ATOM   16837 C  CZ  . ARG D  1 467 ? 36.507  -34.164 0.448   1.00 28.73 ? 484  ARG D CZ  1 
ATOM   16838 N  NH1 . ARG D  1 467 ? 35.401  -34.000 1.157   1.00 28.06 ? 484  ARG D NH1 1 
ATOM   16839 N  NH2 . ARG D  1 467 ? 37.524  -33.337 0.618   1.00 28.06 ? 484  ARG D NH2 1 
ATOM   16840 N  N   . HIS D  1 468 ? 33.564  -36.313 -5.920  1.00 23.45 ? 485  HIS D N   1 
ATOM   16841 C  CA  . HIS D  1 468 ? 33.828  -36.308 -7.353  1.00 24.45 ? 485  HIS D CA  1 
ATOM   16842 C  C   . HIS D  1 468 ? 32.776  -37.161 -8.055  1.00 24.20 ? 485  HIS D C   1 
ATOM   16843 O  O   . HIS D  1 468 ? 32.291  -38.145 -7.496  1.00 22.51 ? 485  HIS D O   1 
ATOM   16844 C  CB  . HIS D  1 468 ? 35.245  -36.801 -7.677  1.00 26.06 ? 485  HIS D CB  1 
ATOM   16845 C  CG  . HIS D  1 468 ? 36.313  -36.144 -6.868  1.00 26.83 ? 485  HIS D CG  1 
ATOM   16846 N  ND1 . HIS D  1 468 ? 36.699  -34.829 -7.041  1.00 26.80 ? 485  HIS D ND1 1 
ATOM   16847 C  CD2 . HIS D  1 468 ? 37.035  -36.618 -5.838  1.00 27.03 ? 485  HIS D CD2 1 
ATOM   16848 C  CE1 . HIS D  1 468 ? 37.640  -34.536 -6.148  1.00 27.98 ? 485  HIS D CE1 1 
ATOM   16849 N  NE2 . HIS D  1 468 ? 37.862  -35.613 -5.411  1.00 27.62 ? 485  HIS D NE2 1 
ATOM   16850 N  N   . ILE D  1 469 ? 32.440  -36.765 -9.289  1.00 23.56 ? 486  ILE D N   1 
ATOM   16851 C  CA  . ILE D  1 469 ? 31.358  -37.377 -10.040 1.00 23.93 ? 486  ILE D CA  1 
ATOM   16852 C  C   . ILE D  1 469 ? 31.941  -38.039 -11.289 1.00 25.41 ? 486  ILE D C   1 
ATOM   16853 O  O   . ILE D  1 469 ? 32.351  -37.359 -12.229 1.00 25.83 ? 486  ILE D O   1 
ATOM   16854 C  CB  . ILE D  1 469 ? 30.282  -36.328 -10.377 1.00 23.24 ? 486  ILE D CB  1 
ATOM   16855 C  CG1 . ILE D  1 469 ? 29.818  -35.576 -9.122  1.00 23.14 ? 486  ILE D CG1 1 
ATOM   16856 C  CG2 . ILE D  1 469 ? 29.113  -36.979 -11.104 1.00 23.86 ? 486  ILE D CG2 1 
ATOM   16857 C  CD1 . ILE D  1 469 ? 28.924  -34.381 -9.396  1.00 23.70 ? 486  ILE D CD1 1 
ATOM   16858 N  N   . SER D  1 470 ? 31.990  -39.376 -11.274 1.00 26.35 ? 487  SER D N   1 
ATOM   16859 C  CA  . SER D  1 470 ? 32.509  -40.144 -12.394 1.00 26.42 ? 487  SER D CA  1 
ATOM   16860 C  C   . SER D  1 470 ? 31.467  -40.185 -13.508 1.00 25.50 ? 487  SER D C   1 
ATOM   16861 O  O   . SER D  1 470 ? 30.286  -39.956 -13.255 1.00 23.57 ? 487  SER D O   1 
ATOM   16862 C  CB  . SER D  1 470 ? 32.881  -41.533 -11.953 1.00 27.24 ? 487  SER D CB  1 
ATOM   16863 O  OG  . SER D  1 470 ? 31.715  -42.246 -11.571 1.00 28.67 ? 487  SER D OG  1 
ATOM   16864 N  N   . ASP D  1 471 ? 31.900  -40.533 -14.728 1.00 25.55 ? 488  ASP D N   1 
ATOM   16865 C  CA  . ASP D  1 471 ? 30.971  -40.711 -15.833 1.00 26.93 ? 488  ASP D CA  1 
ATOM   16866 C  C   . ASP D  1 471 ? 30.025  -41.879 -15.550 1.00 25.12 ? 488  ASP D C   1 
ATOM   16867 O  O   . ASP D  1 471 ? 28.888  -41.867 -16.012 1.00 24.39 ? 488  ASP D O   1 
ATOM   16868 C  CB  . ASP D  1 471 ? 31.689  -40.841 -17.169 1.00 30.52 ? 488  ASP D CB  1 
ATOM   16869 C  CG  . ASP D  1 471 ? 32.104  -39.531 -17.827 1.00 34.22 ? 488  ASP D CG  1 
ATOM   16870 O  OD1 . ASP D  1 471 ? 31.589  -38.460 -17.420 1.00 36.34 ? 488  ASP D OD1 1 
ATOM   16871 O  OD2 . ASP D  1 471 ? 32.959  -39.586 -18.733 1.00 40.64 ? 488  ASP D OD2 1 
ATOM   16872 N  N   . SER D  1 472 ? 30.474  -42.859 -14.752 1.00 24.09 ? 489  SER D N   1 
ATOM   16873 C  CA  A SER D  1 472 ? 29.654  -44.007 -14.400 0.46 24.05 ? 489  SER D CA  1 
ATOM   16874 C  CA  B SER D  1 472 ? 29.646  -44.007 -14.417 0.54 24.13 ? 489  SER D CA  1 
ATOM   16875 C  C   . SER D  1 472 ? 28.389  -43.583 -13.654 1.00 23.61 ? 489  SER D C   1 
ATOM   16876 O  O   . SER D  1 472 ? 27.381  -44.283 -13.697 1.00 24.80 ? 489  SER D O   1 
ATOM   16877 C  CB  A SER D  1 472 ? 30.437  -45.008 -13.592 0.46 24.86 ? 489  SER D CB  1 
ATOM   16878 C  CB  B SER D  1 472 ? 30.431  -45.059 -13.662 0.54 25.17 ? 489  SER D CB  1 
ATOM   16879 O  OG  A SER D  1 472 ? 31.500  -45.559 -14.355 0.46 24.93 ? 489  SER D OG  1 
ATOM   16880 O  OG  B SER D  1 472 ? 31.052  -44.531 -12.498 0.54 25.38 ? 489  SER D OG  1 
ATOM   16881 N  N   . VAL D  1 473 ? 28.437  -42.440 -12.954 1.00 22.45 ? 490  VAL D N   1 
ATOM   16882 C  CA  . VAL D  1 473 ? 27.258  -41.950 -12.249 1.00 22.58 ? 490  VAL D CA  1 
ATOM   16883 C  C   . VAL D  1 473 ? 26.156  -41.646 -13.270 1.00 21.65 ? 490  VAL D C   1 
ATOM   16884 O  O   . VAL D  1 473 ? 24.987  -41.942 -13.024 1.00 22.77 ? 490  VAL D O   1 
ATOM   16885 C  CB  . VAL D  1 473 ? 27.559  -40.728 -11.351 1.00 22.85 ? 490  VAL D CB  1 
ATOM   16886 C  CG1 . VAL D  1 473 ? 26.297  -40.011 -10.885 1.00 23.34 ? 490  VAL D CG1 1 
ATOM   16887 C  CG2 . VAL D  1 473 ? 28.418  -41.099 -10.150 1.00 23.02 ? 490  VAL D CG2 1 
ATOM   16888 N  N   . PHE D  1 474 ? 26.534  -41.058 -14.413 1.00 21.20 ? 491  PHE D N   1 
ATOM   16889 C  CA  . PHE D  1 474 ? 25.575  -40.668 -15.444 1.00 21.89 ? 491  PHE D CA  1 
ATOM   16890 C  C   . PHE D  1 474 ? 25.035  -41.898 -16.180 1.00 21.80 ? 491  PHE D C   1 
ATOM   16891 O  O   . PHE D  1 474 ? 23.880  -41.902 -16.597 1.00 21.13 ? 491  PHE D O   1 
ATOM   16892 C  CB  . PHE D  1 474 ? 26.211  -39.625 -16.369 1.00 21.77 ? 491  PHE D CB  1 
ATOM   16893 C  CG  . PHE D  1 474 ? 26.380  -38.281 -15.673 1.00 22.56 ? 491  PHE D CG  1 
ATOM   16894 C  CD1 . PHE D  1 474 ? 25.291  -37.433 -15.492 1.00 23.68 ? 491  PHE D CD1 1 
ATOM   16895 C  CD2 . PHE D  1 474 ? 27.609  -37.896 -15.149 1.00 22.87 ? 491  PHE D CD2 1 
ATOM   16896 C  CE1 . PHE D  1 474 ? 25.433  -36.226 -14.819 1.00 23.02 ? 491  PHE D CE1 1 
ATOM   16897 C  CE2 . PHE D  1 474 ? 27.750  -36.683 -14.485 1.00 23.31 ? 491  PHE D CE2 1 
ATOM   16898 C  CZ  . PHE D  1 474 ? 26.662  -35.854 -14.325 1.00 23.54 ? 491  PHE D CZ  1 
ATOM   16899 N  N   . LEU D  1 475 ? 25.865  -42.941 -16.321 1.00 22.28 ? 492  LEU D N   1 
ATOM   16900 C  CA  . LEU D  1 475 ? 25.424  -44.225 -16.848 1.00 22.65 ? 492  LEU D CA  1 
ATOM   16901 C  C   . LEU D  1 475 ? 24.367  -44.837 -15.928 1.00 22.93 ? 492  LEU D C   1 
ATOM   16902 O  O   . LEU D  1 475 ? 23.340  -45.334 -16.386 1.00 22.05 ? 492  LEU D O   1 
ATOM   16903 C  CB  . LEU D  1 475 ? 26.649  -45.127 -16.987 1.00 24.51 ? 492  LEU D CB  1 
ATOM   16904 C  CG  . LEU D  1 475 ? 26.409  -46.541 -17.527 1.00 26.13 ? 492  LEU D CG  1 
ATOM   16905 C  CD1 . LEU D  1 475 ? 25.734  -46.528 -18.885 1.00 27.11 ? 492  LEU D CD1 1 
ATOM   16906 C  CD2 . LEU D  1 475 ? 27.722  -47.302 -17.609 1.00 26.63 ? 492  LEU D CD2 1 
ATOM   16907 N  N   . GLU D  1 476 ? 24.617  -44.775 -14.615 1.00 23.54 ? 493  GLU D N   1 
ATOM   16908 C  CA  . GLU D  1 476 ? 23.708  -45.331 -13.626 1.00 24.83 ? 493  GLU D CA  1 
ATOM   16909 C  C   . GLU D  1 476 ? 22.391  -44.555 -13.628 1.00 22.76 ? 493  GLU D C   1 
ATOM   16910 O  O   . GLU D  1 476 ? 21.322  -45.144 -13.515 1.00 22.41 ? 493  GLU D O   1 
ATOM   16911 C  CB  . GLU D  1 476 ? 24.385  -45.296 -12.254 1.00 28.21 ? 493  GLU D CB  1 
ATOM   16912 C  CG  . GLU D  1 476 ? 23.994  -46.454 -11.345 1.00 32.19 ? 493  GLU D CG  1 
ATOM   16913 C  CD  . GLU D  1 476 ? 24.159  -47.830 -11.971 1.00 34.42 ? 493  GLU D CD  1 
ATOM   16914 O  OE1 . GLU D  1 476 ? 25.191  -48.148 -12.609 1.00 37.06 ? 493  GLU D OE1 1 
ATOM   16915 O  OE2 . GLU D  1 476 ? 23.200  -48.598 -11.807 1.00 39.63 ? 493  GLU D OE2 1 
ATOM   16916 N  N   . ALA D  1 477 ? 22.473  -43.228 -13.752 1.00 22.68 ? 494  ALA D N   1 
ATOM   16917 C  CA  . ALA D  1 477 ? 21.287  -42.387 -13.833 1.00 22.48 ? 494  ALA D CA  1 
ATOM   16918 C  C   . ALA D  1 477 ? 20.451  -42.728 -15.072 1.00 21.80 ? 494  ALA D C   1 
ATOM   16919 O  O   . ALA D  1 477 ? 19.223  -42.776 -14.997 1.00 21.36 ? 494  ALA D O   1 
ATOM   16920 C  CB  . ALA D  1 477 ? 21.696  -40.931 -13.822 1.00 22.90 ? 494  ALA D CB  1 
ATOM   16921 N  N   . ALA D  1 478 ? 21.113  -42.950 -16.213 1.00 21.48 ? 495  ALA D N   1 
ATOM   16922 C  CA  . ALA D  1 478 ? 20.417  -43.316 -17.444 1.00 22.27 ? 495  ALA D CA  1 
ATOM   16923 C  C   . ALA D  1 478 ? 19.635  -44.615 -17.252 1.00 23.20 ? 495  ALA D C   1 
ATOM   16924 O  O   . ALA D  1 478 ? 18.455  -44.686 -17.580 1.00 24.18 ? 495  ALA D O   1 
ATOM   16925 C  CB  . ALA D  1 478 ? 21.391  -43.429 -18.591 1.00 22.18 ? 495  ALA D CB  1 
ATOM   16926 N  N   . LYS D  1 479 ? 20.284  -45.635 -16.679 1.00 24.00 ? 496  LYS D N   1 
ATOM   16927 C  CA  . LYS D  1 479 ? 19.623  -46.909 -16.454 1.00 24.72 ? 496  LYS D CA  1 
ATOM   16928 C  C   . LYS D  1 479 ? 18.457  -46.733 -15.485 1.00 24.74 ? 496  LYS D C   1 
ATOM   16929 O  O   . LYS D  1 479 ? 17.423  -47.363 -15.668 1.00 24.16 ? 496  LYS D O   1 
ATOM   16930 C  CB  . LYS D  1 479 ? 20.605  -47.979 -15.965 1.00 25.70 ? 496  LYS D CB  1 
ATOM   16931 C  CG  . LYS D  1 479 ? 21.655  -48.356 -16.995 1.00 27.50 ? 496  LYS D CG  1 
ATOM   16932 C  CD  . LYS D  1 479 ? 22.648  -49.425 -16.555 1.00 29.04 ? 496  LYS D CD  1 
ATOM   16933 C  CE  . LYS D  1 479 ? 23.556  -48.950 -15.473 1.00 29.77 ? 496  LYS D CE  1 
ATOM   16934 N  NZ  . LYS D  1 479 ? 24.602  -49.939 -15.197 1.00 30.53 ? 496  LYS D NZ  1 
ATOM   16935 N  N   . ALA D  1 480 ? 18.624  -45.886 -14.457 1.00 24.50 ? 497  ALA D N   1 
ATOM   16936 C  CA  . ALA D  1 480 ? 17.594  -45.694 -13.447 1.00 25.19 ? 497  ALA D CA  1 
ATOM   16937 C  C   . ALA D  1 480 ? 16.378  -44.978 -14.034 1.00 26.21 ? 497  ALA D C   1 
ATOM   16938 O  O   . ALA D  1 480 ? 15.258  -45.193 -13.581 1.00 27.99 ? 497  ALA D O   1 
ATOM   16939 C  CB  . ALA D  1 480 ? 18.151  -44.931 -12.264 1.00 26.04 ? 497  ALA D CB  1 
ATOM   16940 N  N   . LEU D  1 481 ? 16.602  -44.114 -15.030 1.00 25.88 ? 498  LEU D N   1 
ATOM   16941 C  CA  . LEU D  1 481 ? 15.508  -43.432 -15.707 1.00 26.19 ? 498  LEU D CA  1 
ATOM   16942 C  C   . LEU D  1 481 ? 14.704  -44.433 -16.542 1.00 26.77 ? 498  LEU D C   1 
ATOM   16943 O  O   . LEU D  1 481 ? 13.480  -44.493 -16.433 1.00 26.22 ? 498  LEU D O   1 
ATOM   16944 C  CB  . LEU D  1 481 ? 16.051  -42.289 -16.561 1.00 25.37 ? 498  LEU D CB  1 
ATOM   16945 C  CG  . LEU D  1 481 ? 15.015  -41.539 -17.406 1.00 25.96 ? 498  LEU D CG  1 
ATOM   16946 C  CD1 . LEU D  1 481 ? 13.915  -40.920 -16.562 1.00 26.27 ? 498  LEU D CD1 1 
ATOM   16947 C  CD2 . LEU D  1 481 ? 15.700  -40.489 -18.241 1.00 26.18 ? 498  LEU D CD2 1 
ATOM   16948 N  N   . THR D  1 482 ? 15.404  -45.231 -17.357 1.00 27.84 ? 499  THR D N   1 
ATOM   16949 C  CA  . THR D  1 482 ? 14.767  -46.181 -18.260 1.00 29.72 ? 499  THR D CA  1 
ATOM   16950 C  C   . THR D  1 482 ? 13.958  -47.212 -17.472 1.00 29.96 ? 499  THR D C   1 
ATOM   16951 O  O   . THR D  1 482 ? 12.899  -47.635 -17.924 1.00 29.38 ? 499  THR D O   1 
ATOM   16952 C  CB  . THR D  1 482 ? 15.835  -46.849 -19.124 1.00 31.70 ? 499  THR D CB  1 
ATOM   16953 O  OG1 . THR D  1 482 ? 16.446  -45.802 -19.869 1.00 33.64 ? 499  THR D OG1 1 
ATOM   16954 C  CG2 . THR D  1 482 ? 15.262  -47.873 -20.087 1.00 32.53 ? 499  THR D CG2 1 
ATOM   16955 N  N   . SER D  1 483 ? 14.448  -47.600 -16.288 1.00 29.60 ? 500  SER D N   1 
ATOM   16956 C  CA  . SER D  1 483 ? 13.824  -48.658 -15.505 1.00 31.57 ? 500  SER D CA  1 
ATOM   16957 C  C   . SER D  1 483 ? 12.464  -48.243 -14.938 1.00 32.01 ? 500  SER D C   1 
ATOM   16958 O  O   . SER D  1 483 ? 11.746  -49.089 -14.414 1.00 34.24 ? 500  SER D O   1 
ATOM   16959 C  CB  . SER D  1 483 ? 14.734  -49.125 -14.397 1.00 32.30 ? 500  SER D CB  1 
ATOM   16960 O  OG  . SER D  1 483 ? 14.842  -48.131 -13.388 1.00 33.36 ? 500  SER D OG  1 
ATOM   16961 N  N   . GLN D  1 484 ? 12.089  -46.962 -15.035 1.00 31.87 ? 501  GLN D N   1 
ATOM   16962 C  CA  . GLN D  1 484 ? 10.816  -46.519 -14.484 1.00 32.78 ? 501  GLN D CA  1 
ATOM   16963 C  C   . GLN D  1 484 ? 9.693   -46.538 -15.522 1.00 32.73 ? 501  GLN D C   1 
ATOM   16964 O  O   . GLN D  1 484 ? 8.549   -46.251 -15.180 1.00 30.65 ? 501  GLN D O   1 
ATOM   16965 C  CB  . GLN D  1 484 ? 10.979  -45.133 -13.875 1.00 34.18 ? 501  GLN D CB  1 
ATOM   16966 C  CG  . GLN D  1 484 ? 11.961  -45.127 -12.712 1.00 35.07 ? 501  GLN D CG  1 
ATOM   16967 C  CD  . GLN D  1 484 ? 11.907  -43.839 -11.937 1.00 35.07 ? 501  GLN D CD  1 
ATOM   16968 O  OE1 . GLN D  1 484 ? 10.883  -43.510 -11.329 1.00 35.42 ? 501  GLN D OE1 1 
ATOM   16969 N  NE2 . GLN D  1 484 ? 13.004  -43.095 -11.969 1.00 35.24 ? 501  GLN D NE2 1 
ATOM   16970 N  N   . LEU D  1 485 ? 10.019  -46.860 -16.781 1.00 34.73 ? 502  LEU D N   1 
ATOM   16971 C  CA  . LEU D  1 485 ? 9.003   -47.084 -17.800 1.00 36.04 ? 502  LEU D CA  1 
ATOM   16972 C  C   . LEU D  1 485 ? 8.247   -48.372 -17.484 1.00 37.47 ? 502  LEU D C   1 
ATOM   16973 O  O   . LEU D  1 485 ? 8.858   -49.385 -17.153 1.00 35.86 ? 502  LEU D O   1 
ATOM   16974 C  CB  . LEU D  1 485 ? 9.642   -47.159 -19.186 1.00 37.27 ? 502  LEU D CB  1 
ATOM   16975 C  CG  . LEU D  1 485 ? 10.062  -45.828 -19.813 1.00 37.28 ? 502  LEU D CG  1 
ATOM   16976 C  CD1 . LEU D  1 485 ? 10.906  -46.071 -21.048 1.00 38.25 ? 502  LEU D CD1 1 
ATOM   16977 C  CD2 . LEU D  1 485 ? 8.848   -44.987 -20.163 1.00 37.79 ? 502  LEU D CD2 1 
ATOM   16978 N  N   . THR D  1 486 ? 6.914   -48.318 -17.589 1.00 40.09 ? 503  THR D N   1 
ATOM   16979 C  CA  . THR D  1 486 ? 6.083   -49.508 -17.479 1.00 44.48 ? 503  THR D CA  1 
ATOM   16980 C  C   . THR D  1 486 ? 6.050   -50.216 -18.834 1.00 45.07 ? 503  THR D C   1 
ATOM   16981 O  O   . THR D  1 486 ? 6.393   -49.627 -19.856 1.00 42.13 ? 503  THR D O   1 
ATOM   16982 C  CB  . THR D  1 486 ? 4.674   -49.131 -17.021 1.00 44.89 ? 503  THR D CB  1 
ATOM   16983 O  OG1 . THR D  1 486 ? 4.122   -48.381 -18.097 1.00 44.92 ? 503  THR D OG1 1 
ATOM   16984 C  CG2 . THR D  1 486 ? 4.665   -48.325 -15.733 1.00 45.80 ? 503  THR D CG2 1 
ATOM   16985 N  N   . ASP D  1 487 ? 5.612   -51.480 -18.825 1.00 48.65 ? 504  ASP D N   1 
ATOM   16986 C  CA  . ASP D  1 487 ? 5.442   -52.260 -20.042 1.00 50.02 ? 504  ASP D CA  1 
ATOM   16987 C  C   . ASP D  1 487 ? 4.429   -51.577 -20.960 1.00 50.91 ? 504  ASP D C   1 
ATOM   16988 O  O   . ASP D  1 487 ? 4.657   -51.474 -22.165 1.00 49.09 ? 504  ASP D O   1 
ATOM   16989 C  CB  . ASP D  1 487 ? 5.054   -53.696 -19.720 1.00 52.03 ? 504  ASP D CB  1 
ATOM   16990 C  CG  . ASP D  1 487 ? 6.161   -54.563 -19.136 1.00 52.78 ? 504  ASP D CG  1 
ATOM   16991 O  OD1 . ASP D  1 487 ? 7.330   -54.129 -19.169 1.00 52.78 ? 504  ASP D OD1 1 
ATOM   16992 O  OD2 . ASP D  1 487 ? 5.844   -55.670 -18.653 1.00 55.72 ? 504  ASP D OD2 1 
ATOM   16993 N  N   . GLU D  1 488 ? 3.321   -51.105 -20.372 1.00 51.35 ? 505  GLU D N   1 
ATOM   16994 C  CA  . GLU D  1 488 ? 2.282   -50.399 -21.107 1.00 51.56 ? 505  GLU D CA  1 
ATOM   16995 C  C   . GLU D  1 488 ? 2.889   -49.223 -21.870 1.00 52.67 ? 505  GLU D C   1 
ATOM   16996 O  O   . GLU D  1 488 ? 2.638   -49.063 -23.065 1.00 52.69 ? 505  GLU D O   1 
ATOM   16997 C  CB  . GLU D  1 488 ? 1.178   -49.925 -20.160 1.00 51.62 ? 505  GLU D CB  1 
ATOM   16998 N  N   . GLU D  1 489 ? 3.693   -48.410 -21.170 1.00 49.48 ? 506  GLU D N   1 
ATOM   16999 C  CA  . GLU D  1 489 ? 4.297   -47.223 -21.756 1.00 47.17 ? 506  GLU D CA  1 
ATOM   17000 C  C   . GLU D  1 489 ? 5.212   -47.609 -22.918 1.00 46.01 ? 506  GLU D C   1 
ATOM   17001 O  O   . GLU D  1 489 ? 5.222   -46.932 -23.945 1.00 45.28 ? 506  GLU D O   1 
ATOM   17002 C  CB  . GLU D  1 489 ? 5.043   -46.412 -20.695 1.00 47.06 ? 506  GLU D CB  1 
ATOM   17003 C  CG  . GLU D  1 489 ? 4.118   -45.577 -19.814 1.00 46.04 ? 506  GLU D CG  1 
ATOM   17004 C  CD  . GLU D  1 489 ? 4.745   -45.023 -18.544 1.00 46.52 ? 506  GLU D CD  1 
ATOM   17005 O  OE1 . GLU D  1 489 ? 5.851   -45.461 -18.154 1.00 43.68 ? 506  GLU D OE1 1 
ATOM   17006 O  OE2 . GLU D  1 489 ? 4.113   -44.129 -17.943 1.00 48.21 ? 506  GLU D OE2 1 
ATOM   17007 N  N   . LEU D  1 490 ? 5.970   -48.700 -22.753 1.00 46.57 ? 507  LEU D N   1 
ATOM   17008 C  CA  . LEU D  1 490 ? 6.881   -49.168 -23.788 1.00 50.34 ? 507  LEU D CA  1 
ATOM   17009 C  C   . LEU D  1 490 ? 6.100   -49.606 -25.031 1.00 52.70 ? 507  LEU D C   1 
ATOM   17010 O  O   . LEU D  1 490 ? 6.563   -49.402 -26.152 1.00 53.14 ? 507  LEU D O   1 
ATOM   17011 C  CB  . LEU D  1 490 ? 7.762   -50.295 -23.246 1.00 49.94 ? 507  LEU D CB  1 
ATOM   17012 C  CG  . LEU D  1 490 ? 8.830   -49.888 -22.223 1.00 50.04 ? 507  LEU D CG  1 
ATOM   17013 C  CD1 . LEU D  1 490 ? 9.439   -51.106 -21.551 1.00 50.15 ? 507  LEU D CD1 1 
ATOM   17014 C  CD2 . LEU D  1 490 ? 9.922   -49.047 -22.863 1.00 49.06 ? 507  LEU D CD2 1 
ATOM   17015 N  N   . ALA D  1 491 ? 4.908   -50.183 -24.829 1.00 56.26 ? 508  ALA D N   1 
ATOM   17016 C  CA  . ALA D  1 491 ? 4.079   -50.668 -25.926 1.00 57.47 ? 508  ALA D CA  1 
ATOM   17017 C  C   . ALA D  1 491 ? 3.492   -49.508 -26.733 1.00 56.99 ? 508  ALA D C   1 
ATOM   17018 O  O   . ALA D  1 491 ? 3.105   -49.696 -27.884 1.00 58.46 ? 508  ALA D O   1 
ATOM   17019 C  CB  . ALA D  1 491 ? 2.987   -51.568 -25.391 1.00 56.95 ? 508  ALA D CB  1 
ATOM   17020 N  N   . GLN D  1 492 ? 3.431   -48.316 -26.125 1.00 56.37 ? 509  GLN D N   1 
ATOM   17021 C  CA  . GLN D  1 492 ? 2.936   -47.120 -26.789 1.00 55.38 ? 509  GLN D CA  1 
ATOM   17022 C  C   . GLN D  1 492 ? 4.067   -46.376 -27.502 1.00 51.92 ? 509  GLN D C   1 
ATOM   17023 O  O   . GLN D  1 492 ? 3.821   -45.352 -28.135 1.00 51.06 ? 509  GLN D O   1 
ATOM   17024 C  CB  . GLN D  1 492 ? 2.280   -46.193 -25.765 1.00 60.16 ? 509  GLN D CB  1 
ATOM   17025 C  CG  . GLN D  1 492 ? 1.070   -46.797 -25.061 1.00 63.64 ? 509  GLN D CG  1 
ATOM   17026 C  CD  . GLN D  1 492 ? 0.560   -45.937 -23.925 1.00 67.01 ? 509  GLN D CD  1 
ATOM   17027 O  OE1 . GLN D  1 492 ? 0.469   -46.376 -22.773 1.00 69.02 ? 509  GLN D OE1 1 
ATOM   17028 N  NE2 . GLN D  1 492 ? 0.227   -44.694 -24.241 1.00 66.99 ? 509  GLN D NE2 1 
ATOM   17029 N  N   . GLY D  1 493 ? 5.302   -46.883 -27.389 1.00 49.10 ? 510  GLY D N   1 
ATOM   17030 C  CA  . GLY D  1 493 ? 6.457   -46.266 -28.023 1.00 47.64 ? 510  GLY D CA  1 
ATOM   17031 C  C   . GLY D  1 493 ? 7.020   -45.105 -27.201 1.00 45.65 ? 510  GLY D C   1 
ATOM   17032 O  O   . GLY D  1 493 ? 7.783   -44.293 -27.720 1.00 46.11 ? 510  GLY D O   1 
ATOM   17033 N  N   . ARG D  1 494 ? 6.654   -45.047 -25.915 1.00 44.93 ? 511  ARG D N   1 
ATOM   17034 C  CA  . ARG D  1 494 ? 7.103   -43.992 -25.019 1.00 43.27 ? 511  ARG D CA  1 
ATOM   17035 C  C   . ARG D  1 494 ? 8.472   -44.378 -24.462 1.00 38.37 ? 511  ARG D C   1 
ATOM   17036 O  O   . ARG D  1 494 ? 8.595   -45.418 -23.819 1.00 38.06 ? 511  ARG D O   1 
ATOM   17037 C  CB  . ARG D  1 494 ? 6.070   -43.833 -23.898 1.00 47.10 ? 511  ARG D CB  1 
ATOM   17038 C  CG  . ARG D  1 494 ? 5.978   -42.438 -23.300 1.00 50.57 ? 511  ARG D CG  1 
ATOM   17039 C  CD  . ARG D  1 494 ? 4.997   -42.383 -22.132 1.00 51.43 ? 511  ARG D CD  1 
ATOM   17040 N  NE  . ARG D  1 494 ? 4.329   -41.079 -22.038 1.00 52.08 ? 511  ARG D NE  1 
ATOM   17041 C  CZ  . ARG D  1 494 ? 4.930   -39.897 -21.907 1.00 54.14 ? 511  ARG D CZ  1 
ATOM   17042 N  NH1 . ARG D  1 494 ? 6.242   -39.818 -21.761 1.00 54.10 ? 511  ARG D NH1 1 
ATOM   17043 N  NH2 . ARG D  1 494 ? 4.211   -38.788 -21.919 1.00 56.54 ? 511  ARG D NH2 1 
ATOM   17044 N  N   . LEU D  1 495 ? 9.486   -43.538 -24.713 1.00 33.81 ? 512  LEU D N   1 
ATOM   17045 C  CA  . LEU D  1 495 ? 10.864  -43.858 -24.364 1.00 33.12 ? 512  LEU D CA  1 
ATOM   17046 C  C   . LEU D  1 495 ? 11.330  -43.084 -23.127 1.00 31.91 ? 512  LEU D C   1 
ATOM   17047 O  O   . LEU D  1 495 ? 12.484  -43.224 -22.720 1.00 29.64 ? 512  LEU D O   1 
ATOM   17048 C  CB  . LEU D  1 495 ? 11.753  -43.561 -25.569 1.00 33.25 ? 512  LEU D CB  1 
ATOM   17049 C  CG  . LEU D  1 495 ? 11.439  -44.345 -26.848 1.00 34.51 ? 512  LEU D CG  1 
ATOM   17050 C  CD1 . LEU D  1 495 ? 12.251  -43.794 -28.002 1.00 35.85 ? 512  LEU D CD1 1 
ATOM   17051 C  CD2 . LEU D  1 495 ? 11.693  -45.831 -26.678 1.00 35.01 ? 512  LEU D CD2 1 
ATOM   17052 N  N   . TYR D  1 496 ? 10.428  -42.286 -22.539 1.00 31.12 ? 513  TYR D N   1 
ATOM   17053 C  CA  . TYR D  1 496 ? 10.715  -41.481 -21.361 1.00 30.43 ? 513  TYR D CA  1 
ATOM   17054 C  C   . TYR D  1 496 ? 9.482   -41.457 -20.464 1.00 31.50 ? 513  TYR D C   1 
ATOM   17055 O  O   . TYR D  1 496 ? 8.363   -41.412 -20.968 1.00 32.49 ? 513  TYR D O   1 
ATOM   17056 C  CB  . TYR D  1 496 ? 11.093  -40.051 -21.756 1.00 28.88 ? 513  TYR D CB  1 
ATOM   17057 C  CG  . TYR D  1 496 ? 12.427  -39.978 -22.476 1.00 27.45 ? 513  TYR D CG  1 
ATOM   17058 C  CD1 . TYR D  1 496 ? 13.615  -40.132 -21.772 1.00 26.91 ? 513  TYR D CD1 1 
ATOM   17059 C  CD2 . TYR D  1 496 ? 12.505  -39.780 -23.851 1.00 26.38 ? 513  TYR D CD2 1 
ATOM   17060 C  CE1 . TYR D  1 496 ? 14.841  -40.084 -22.412 1.00 26.15 ? 513  TYR D CE1 1 
ATOM   17061 C  CE2 . TYR D  1 496 ? 13.726  -39.729 -24.502 1.00 25.14 ? 513  TYR D CE2 1 
ATOM   17062 C  CZ  . TYR D  1 496 ? 14.899  -39.886 -23.779 1.00 25.12 ? 513  TYR D CZ  1 
ATOM   17063 O  OH  . TYR D  1 496 ? 16.121  -39.835 -24.387 1.00 23.50 ? 513  TYR D OH  1 
ATOM   17064 N  N   . PRO D  1 497 ? 9.636   -41.480 -19.118 1.00 32.56 ? 514  PRO D N   1 
ATOM   17065 C  CA  . PRO D  1 497 ? 8.484   -41.414 -18.219 1.00 32.09 ? 514  PRO D CA  1 
ATOM   17066 C  C   . PRO D  1 497 ? 7.767   -40.082 -18.404 1.00 31.92 ? 514  PRO D C   1 
ATOM   17067 O  O   . PRO D  1 497 ? 8.369   -39.133 -18.902 1.00 32.56 ? 514  PRO D O   1 
ATOM   17068 C  CB  . PRO D  1 497 ? 9.067   -41.572 -16.799 1.00 32.15 ? 514  PRO D CB  1 
ATOM   17069 C  CG  . PRO D  1 497 ? 10.487  -42.055 -17.010 1.00 32.58 ? 514  PRO D CG  1 
ATOM   17070 C  CD  . PRO D  1 497 ? 10.911  -41.566 -18.388 1.00 32.68 ? 514  PRO D CD  1 
ATOM   17071 N  N   . PRO D  1 498 ? 6.469   -39.973 -18.029 1.00 31.31 ? 515  PRO D N   1 
ATOM   17072 C  CA  . PRO D  1 498 ? 5.736   -38.708 -18.135 1.00 32.03 ? 515  PRO D CA  1 
ATOM   17073 C  C   . PRO D  1 498 ? 6.387   -37.586 -17.329 1.00 32.67 ? 515  PRO D C   1 
ATOM   17074 O  O   . PRO D  1 498 ? 6.745   -37.789 -16.172 1.00 32.40 ? 515  PRO D O   1 
ATOM   17075 C  CB  . PRO D  1 498 ? 4.325   -39.034 -17.603 1.00 32.37 ? 515  PRO D CB  1 
ATOM   17076 C  CG  . PRO D  1 498 ? 4.221   -40.542 -17.676 1.00 33.38 ? 515  PRO D CG  1 
ATOM   17077 C  CD  . PRO D  1 498 ? 5.636   -41.071 -17.515 1.00 32.55 ? 515  PRO D CD  1 
ATOM   17078 N  N   . LEU D  1 499 ? 6.500   -36.402 -17.947 1.00 33.51 ? 516  LEU D N   1 
ATOM   17079 C  CA  . LEU D  1 499 ? 7.086   -35.229 -17.313 1.00 33.40 ? 516  LEU D CA  1 
ATOM   17080 C  C   . LEU D  1 499 ? 6.286   -34.837 -16.076 1.00 32.00 ? 516  LEU D C   1 
ATOM   17081 O  O   . LEU D  1 499 ? 6.848   -34.265 -15.145 1.00 32.19 ? 516  LEU D O   1 
ATOM   17082 C  CB  . LEU D  1 499 ? 7.170   -34.040 -18.269 1.00 34.82 ? 516  LEU D CB  1 
ATOM   17083 C  CG  . LEU D  1 499 ? 8.455   -33.887 -19.088 1.00 36.64 ? 516  LEU D CG  1 
ATOM   17084 C  CD1 . LEU D  1 499 ? 8.341   -32.627 -19.929 1.00 37.30 ? 516  LEU D CD1 1 
ATOM   17085 C  CD2 . LEU D  1 499 ? 9.712   -33.840 -18.241 1.00 36.89 ? 516  LEU D CD2 1 
ATOM   17086 N  N   . ALA D  1 500 ? 4.977   -35.116 -16.086 1.00 31.57 ? 517  ALA D N   1 
ATOM   17087 C  CA  . ALA D  1 500 ? 4.120   -34.815 -14.949 1.00 32.45 ? 517  ALA D CA  1 
ATOM   17088 C  C   . ALA D  1 500 ? 4.613   -35.514 -13.679 1.00 31.55 ? 517  ALA D C   1 
ATOM   17089 O  O   . ALA D  1 500 ? 4.330   -35.045 -12.579 1.00 31.81 ? 517  ALA D O   1 
ATOM   17090 C  CB  . ALA D  1 500 ? 2.687   -35.193 -15.263 1.00 33.14 ? 517  ALA D CB  1 
ATOM   17091 N  N   . ASN D  1 501 ? 5.350   -36.624 -13.833 1.00 30.10 ? 518  ASN D N   1 
ATOM   17092 C  CA  . ASN D  1 501 ? 5.814   -37.417 -12.703 1.00 30.63 ? 518  ASN D CA  1 
ATOM   17093 C  C   . ASN D  1 501 ? 7.266   -37.100 -12.329 1.00 27.75 ? 518  ASN D C   1 
ATOM   17094 O  O   . ASN D  1 501 ? 7.917   -37.913 -11.674 1.00 25.85 ? 518  ASN D O   1 
ATOM   17095 C  CB  . ASN D  1 501 ? 5.715   -38.910 -13.007 1.00 32.43 ? 518  ASN D CB  1 
ATOM   17096 C  CG  . ASN D  1 501 ? 4.303   -39.367 -13.294 1.00 34.72 ? 518  ASN D CG  1 
ATOM   17097 O  OD1 . ASN D  1 501 ? 3.343   -38.615 -13.096 1.00 35.06 ? 518  ASN D OD1 1 
ATOM   17098 N  ND2 . ASN D  1 501 ? 4.157   -40.607 -13.738 1.00 35.78 ? 518  ASN D ND2 1 
ATOM   17099 N  N   . ILE D  1 502 ? 7.774   -35.921 -12.716 1.00 27.08 ? 519  ILE D N   1 
ATOM   17100 C  CA  . ILE D  1 502 ? 9.203   -35.633 -12.623 1.00 27.00 ? 519  ILE D CA  1 
ATOM   17101 C  C   . ILE D  1 502 ? 9.690   -35.732 -11.173 1.00 26.85 ? 519  ILE D C   1 
ATOM   17102 O  O   . ILE D  1 502 ? 10.815  -36.168 -10.942 1.00 26.22 ? 519  ILE D O   1 
ATOM   17103 C  CB  . ILE D  1 502 ? 9.552   -34.273 -13.266 1.00 26.59 ? 519  ILE D CB  1 
ATOM   17104 C  CG1 . ILE D  1 502 ? 11.064  -34.048 -13.378 1.00 26.02 ? 519  ILE D CG1 1 
ATOM   17105 C  CG2 . ILE D  1 502 ? 8.882   -33.111 -12.532 1.00 27.56 ? 519  ILE D CG2 1 
ATOM   17106 C  CD1 . ILE D  1 502 ? 11.811  -35.111 -14.164 1.00 25.98 ? 519  ILE D CD1 1 
ATOM   17107 N  N   . GLN D  1 503 ? 8.851   -35.342 -10.203 1.00 27.80 ? 520  GLN D N   1 
ATOM   17108 C  CA  . GLN D  1 503 ? 9.232   -35.403 -8.798  1.00 29.73 ? 520  GLN D CA  1 
ATOM   17109 C  C   . GLN D  1 503 ? 9.541   -36.847 -8.406  1.00 29.45 ? 520  GLN D C   1 
ATOM   17110 O  O   . GLN D  1 503 ? 10.620  -37.136 -7.894  1.00 26.70 ? 520  GLN D O   1 
ATOM   17111 C  CB  . GLN D  1 503 ? 8.164   -34.846 -7.853  1.00 31.75 ? 520  GLN D CB  1 
ATOM   17112 C  CG  . GLN D  1 503 ? 7.968   -33.335 -7.928  1.00 34.17 ? 520  GLN D CG  1 
ATOM   17113 C  CD  . GLN D  1 503 ? 7.263   -32.767 -6.711  1.00 37.62 ? 520  GLN D CD  1 
ATOM   17114 O  OE1 . GLN D  1 503 ? 7.791   -32.782 -5.592  1.00 39.13 ? 520  GLN D OE1 1 
ATOM   17115 N  NE2 . GLN D  1 503 ? 6.064   -32.242 -6.914  1.00 39.83 ? 520  GLN D NE2 1 
ATOM   17116 N  N   . GLU D  1 504 ? 8.580   -37.746 -8.652  1.00 29.81 ? 521  GLU D N   1 
ATOM   17117 C  CA  . GLU D  1 504 ? 8.729   -39.156 -8.323  1.00 30.88 ? 521  GLU D CA  1 
ATOM   17118 C  C   . GLU D  1 504 ? 9.930   -39.751 -9.060  1.00 29.20 ? 521  GLU D C   1 
ATOM   17119 O  O   . GLU D  1 504 ? 10.701  -40.511 -8.475  1.00 27.97 ? 521  GLU D O   1 
ATOM   17120 C  CB  . GLU D  1 504 ? 7.427   -39.885 -8.662  1.00 34.10 ? 521  GLU D CB  1 
ATOM   17121 C  CG  . GLU D  1 504 ? 7.445   -41.385 -8.371  1.00 39.08 ? 521  GLU D CG  1 
ATOM   17122 C  CD  . GLU D  1 504 ? 6.167   -42.116 -8.765  1.00 43.06 ? 521  GLU D CD  1 
ATOM   17123 O  OE1 . GLU D  1 504 ? 5.174   -41.448 -9.121  1.00 45.22 ? 521  GLU D OE1 1 
ATOM   17124 O  OE2 . GLU D  1 504 ? 6.167   -43.364 -8.732  1.00 47.02 ? 521  GLU D OE2 1 
ATOM   17125 N  N   . VAL D  1 505 ? 10.073  -39.410 -10.348 1.00 26.25 ? 522  VAL D N   1 
ATOM   17126 C  CA  . VAL D  1 505 ? 11.153  -39.925 -11.175 1.00 25.80 ? 522  VAL D CA  1 
ATOM   17127 C  C   . VAL D  1 505 ? 12.502  -39.476 -10.611 1.00 25.13 ? 522  VAL D C   1 
ATOM   17128 O  O   . VAL D  1 505 ? 13.451  -40.261 -10.573 1.00 25.05 ? 522  VAL D O   1 
ATOM   17129 C  CB  . VAL D  1 505 ? 11.003  -39.497 -12.650 1.00 26.20 ? 522  VAL D CB  1 
ATOM   17130 C  CG1 . VAL D  1 505 ? 12.267  -39.759 -13.458 1.00 25.63 ? 522  VAL D CG1 1 
ATOM   17131 C  CG2 . VAL D  1 505 ? 9.810   -40.163 -13.323 1.00 27.83 ? 522  VAL D CG2 1 
ATOM   17132 N  N   . SER D  1 506 ? 12.583  -38.207 -10.191 1.00 24.94 ? 523  SER D N   1 
ATOM   17133 C  CA  . SER D  1 506 ? 13.835  -37.625 -9.727  1.00 24.50 ? 523  SER D CA  1 
ATOM   17134 C  C   . SER D  1 506 ? 14.295  -38.284 -8.425  1.00 23.27 ? 523  SER D C   1 
ATOM   17135 O  O   . SER D  1 506 ? 15.480  -38.561 -8.256  1.00 21.68 ? 523  SER D O   1 
ATOM   17136 C  CB  . SER D  1 506 ? 13.719  -36.124 -9.580  1.00 24.12 ? 523  SER D CB  1 
ATOM   17137 O  OG  . SER D  1 506 ? 13.615  -35.485 -10.849 1.00 23.68 ? 523  SER D OG  1 
ATOM   17138 N  N   . ILE D  1 507 ? 13.349  -38.531 -7.515  1.00 23.55 ? 524  ILE D N   1 
ATOM   17139 C  CA  . ILE D  1 507 ? 13.642  -39.162 -6.238  1.00 25.49 ? 524  ILE D CA  1 
ATOM   17140 C  C   . ILE D  1 507 ? 14.114  -40.596 -6.474  1.00 25.71 ? 524  ILE D C   1 
ATOM   17141 O  O   . ILE D  1 507 ? 15.068  -41.045 -5.839  1.00 25.40 ? 524  ILE D O   1 
ATOM   17142 C  CB  . ILE D  1 507 ? 12.422  -39.087 -5.296  1.00 27.78 ? 524  ILE D CB  1 
ATOM   17143 C  CG1 . ILE D  1 507 ? 12.028  -37.642 -4.976  1.00 29.64 ? 524  ILE D CG1 1 
ATOM   17144 C  CG2 . ILE D  1 507 ? 12.655  -39.891 -4.016  1.00 28.98 ? 524  ILE D CG2 1 
ATOM   17145 C  CD1 . ILE D  1 507 ? 13.177  -36.756 -4.530  1.00 29.71 ? 524  ILE D CD1 1 
ATOM   17146 N  N   . ASN D  1 508 ? 13.464  -41.308 -7.403  1.00 25.90 ? 525  ASN D N   1 
ATOM   17147 C  CA  . ASN D  1 508 ? 13.830  -42.685 -7.702  1.00 26.38 ? 525  ASN D CA  1 
ATOM   17148 C  C   . ASN D  1 508 ? 15.240  -42.747 -8.283  1.00 26.04 ? 525  ASN D C   1 
ATOM   17149 O  O   . ASN D  1 508 ? 15.998  -43.670 -7.975  1.00 25.92 ? 525  ASN D O   1 
ATOM   17150 C  CB  . ASN D  1 508 ? 12.820  -43.356 -8.626  1.00 28.67 ? 525  ASN D CB  1 
ATOM   17151 C  CG  . ASN D  1 508 ? 11.530  -43.699 -7.920  1.00 31.17 ? 525  ASN D CG  1 
ATOM   17152 O  OD1 . ASN D  1 508 ? 11.482  -43.715 -6.686  1.00 35.96 ? 525  ASN D OD1 1 
ATOM   17153 N  ND2 . ASN D  1 508 ? 10.478  -43.981 -8.676  1.00 31.76 ? 525  ASN D ND2 1 
ATOM   17154 N  N   . ILE D  1 509 ? 15.587  -41.772 -9.130  1.00 24.46 ? 526  ILE D N   1 
ATOM   17155 C  CA  . ILE D  1 509 ? 16.926  -41.713 -9.694  1.00 24.57 ? 526  ILE D CA  1 
ATOM   17156 C  C   . ILE D  1 509 ? 17.928  -41.448 -8.574  1.00 23.29 ? 526  ILE D C   1 
ATOM   17157 O  O   . ILE D  1 509 ? 18.977  -42.085 -8.536  1.00 23.29 ? 526  ILE D O   1 
ATOM   17158 C  CB  . ILE D  1 509 ? 17.018  -40.679 -10.831 1.00 24.87 ? 526  ILE D CB  1 
ATOM   17159 C  CG1 . ILE D  1 509 ? 16.295  -41.195 -12.083 1.00 25.75 ? 526  ILE D CG1 1 
ATOM   17160 C  CG2 . ILE D  1 509 ? 18.472  -40.315 -11.140 1.00 24.78 ? 526  ILE D CG2 1 
ATOM   17161 C  CD1 . ILE D  1 509 ? 16.093  -40.143 -13.153 1.00 26.53 ? 526  ILE D CD1 1 
ATOM   17162 N  N   . ALA D  1 510 ? 17.591  -40.519 -7.669  1.00 22.99 ? 527  ALA D N   1 
ATOM   17163 C  CA  . ALA D  1 510 ? 18.461  -40.187 -6.549  1.00 23.34 ? 527  ALA D CA  1 
ATOM   17164 C  C   . ALA D  1 510 ? 18.752  -41.416 -5.685  1.00 23.87 ? 527  ALA D C   1 
ATOM   17165 O  O   . ALA D  1 510 ? 19.890  -41.602 -5.249  1.00 24.70 ? 527  ALA D O   1 
ATOM   17166 C  CB  . ALA D  1 510 ? 17.851  -39.069 -5.733  1.00 22.50 ? 527  ALA D CB  1 
ATOM   17167 N  N   . ILE D  1 511 ? 17.728  -42.244 -5.439  1.00 24.28 ? 528  ILE D N   1 
ATOM   17168 C  CA  . ILE D  1 511 ? 17.876  -43.418 -4.591  1.00 25.06 ? 528  ILE D CA  1 
ATOM   17169 C  C   . ILE D  1 511 ? 18.858  -44.393 -5.243  1.00 25.32 ? 528  ILE D C   1 
ATOM   17170 O  O   . ILE D  1 511 ? 19.769  -44.884 -4.581  1.00 24.52 ? 528  ILE D O   1 
ATOM   17171 C  CB  . ILE D  1 511 ? 16.504  -44.057 -4.293  1.00 26.06 ? 528  ILE D CB  1 
ATOM   17172 C  CG1 . ILE D  1 511 ? 15.646  -43.134 -3.433  1.00 25.54 ? 528  ILE D CG1 1 
ATOM   17173 C  CG2 . ILE D  1 511 ? 16.656  -45.434 -3.637  1.00 27.03 ? 528  ILE D CG2 1 
ATOM   17174 C  CD1 . ILE D  1 511 ? 14.166  -43.464 -3.431  1.00 25.06 ? 528  ILE D CD1 1 
ATOM   17175 N  N   . LYS D  1 512 ? 18.683  -44.647 -6.550  1.00 26.20 ? 529  LYS D N   1 
ATOM   17176 C  CA  . LYS D  1 512 ? 19.541  -45.562 -7.287  1.00 26.40 ? 529  LYS D CA  1 
ATOM   17177 C  C   . LYS D  1 512 ? 20.979  -45.053 -7.340  1.00 24.61 ? 529  LYS D C   1 
ATOM   17178 O  O   . LYS D  1 512 ? 21.910  -45.838 -7.188  1.00 25.42 ? 529  LYS D O   1 
ATOM   17179 C  CB  . LYS D  1 512 ? 19.035  -45.809 -8.713  1.00 29.22 ? 529  LYS D CB  1 
ATOM   17180 C  CG  . LYS D  1 512 ? 17.858  -46.768 -8.812  1.00 31.96 ? 529  LYS D CG  1 
ATOM   17181 C  CD  . LYS D  1 512 ? 18.242  -48.233 -8.631  1.00 35.76 ? 529  LYS D CD  1 
ATOM   17182 C  CE  . LYS D  1 512 ? 17.179  -49.176 -9.120  1.00 40.74 ? 529  LYS D CE  1 
ATOM   17183 N  NZ  . LYS D  1 512 ? 16.907  -49.062 -10.562 1.00 42.95 ? 529  LYS D NZ  1 
ATOM   17184 N  N   . VAL D  1 513 ? 21.166  -43.748 -7.572  1.00 22.50 ? 530  VAL D N   1 
ATOM   17185 C  CA  . VAL D  1 513 ? 22.507  -43.184 -7.591  1.00 22.56 ? 530  VAL D CA  1 
ATOM   17186 C  C   . VAL D  1 513 ? 23.106  -43.247 -6.181  1.00 21.44 ? 530  VAL D C   1 
ATOM   17187 O  O   . VAL D  1 513 ? 24.290  -43.534 -6.037  1.00 20.73 ? 530  VAL D O   1 
ATOM   17188 C  CB  . VAL D  1 513 ? 22.549  -41.755 -8.163  1.00 22.19 ? 530  VAL D CB  1 
ATOM   17189 C  CG1 . VAL D  1 513 ? 23.949  -41.163 -8.097  1.00 22.31 ? 530  VAL D CG1 1 
ATOM   17190 C  CG2 . VAL D  1 513 ? 22.033  -41.718 -9.600  1.00 22.85 ? 530  VAL D CG2 1 
ATOM   17191 N  N   . THR D  1 514 ? 22.295  -42.994 -5.148  1.00 21.88 ? 531  THR D N   1 
ATOM   17192 C  CA  . THR D  1 514 ? 22.768  -43.058 -3.768  1.00 22.53 ? 531  THR D CA  1 
ATOM   17193 C  C   . THR D  1 514 ? 23.321  -44.459 -3.485  1.00 23.72 ? 531  THR D C   1 
ATOM   17194 O  O   . THR D  1 514 ? 24.434  -44.598 -2.984  1.00 23.72 ? 531  THR D O   1 
ATOM   17195 C  CB  . THR D  1 514 ? 21.645  -42.677 -2.801  1.00 22.86 ? 531  THR D CB  1 
ATOM   17196 O  OG1 . THR D  1 514 ? 21.354  -41.290 -2.975  1.00 22.27 ? 531  THR D OG1 1 
ATOM   17197 C  CG2 . THR D  1 514 ? 22.024  -42.881 -1.345  1.00 22.60 ? 531  THR D CG2 1 
ATOM   17198 N  N   . GLU D  1 515 ? 22.544  -45.493 -3.834  1.00 24.57 ? 532  GLU D N   1 
ATOM   17199 C  CA  . GLU D  1 515 ? 22.962  -46.876 -3.661  1.00 26.66 ? 532  GLU D CA  1 
ATOM   17200 C  C   . GLU D  1 515 ? 24.287  -47.114 -4.381  1.00 26.22 ? 532  GLU D C   1 
ATOM   17201 O  O   . GLU D  1 515 ? 25.197  -47.722 -3.828  1.00 26.14 ? 532  GLU D O   1 
ATOM   17202 C  CB  . GLU D  1 515 ? 21.864  -47.819 -4.152  1.00 29.21 ? 532  GLU D CB  1 
ATOM   17203 C  CG  . GLU D  1 515 ? 20.647  -47.842 -3.231  1.00 31.10 ? 532  GLU D CG  1 
ATOM   17204 C  CD  . GLU D  1 515 ? 19.417  -48.546 -3.780  1.00 35.08 ? 532  GLU D CD  1 
ATOM   17205 O  OE1 . GLU D  1 515 ? 19.410  -48.938 -4.971  1.00 36.02 ? 532  GLU D OE1 1 
ATOM   17206 O  OE2 . GLU D  1 515 ? 18.450  -48.701 -2.999  1.00 39.39 ? 532  GLU D OE2 1 
ATOM   17207 N  N   . TYR D  1 516 ? 24.397  -46.602 -5.610  1.00 26.02 ? 533  TYR D N   1 
ATOM   17208 C  CA  . TYR D  1 516 ? 25.607  -46.748 -6.401  1.00 26.39 ? 533  TYR D CA  1 
ATOM   17209 C  C   . TYR D  1 516 ? 26.802  -46.097 -5.704  1.00 25.58 ? 533  TYR D C   1 
ATOM   17210 O  O   . TYR D  1 516 ? 27.895  -46.662 -5.689  1.00 26.51 ? 533  TYR D O   1 
ATOM   17211 C  CB  . TYR D  1 516 ? 25.389  -46.154 -7.797  1.00 27.45 ? 533  TYR D CB  1 
ATOM   17212 C  CG  . TYR D  1 516 ? 26.649  -46.194 -8.645  1.00 28.84 ? 533  TYR D CG  1 
ATOM   17213 C  CD1 . TYR D  1 516 ? 27.001  -47.345 -9.341  1.00 30.85 ? 533  TYR D CD1 1 
ATOM   17214 C  CD2 . TYR D  1 516 ? 27.496  -45.097 -8.722  1.00 30.20 ? 533  TYR D CD2 1 
ATOM   17215 C  CE1 . TYR D  1 516 ? 28.159  -47.398 -10.098 1.00 32.43 ? 533  TYR D CE1 1 
ATOM   17216 C  CE2 . TYR D  1 516 ? 28.658  -45.138 -9.473  1.00 32.39 ? 533  TYR D CE2 1 
ATOM   17217 C  CZ  . TYR D  1 516 ? 28.986  -46.290 -10.164 1.00 32.91 ? 533  TYR D CZ  1 
ATOM   17218 O  OH  . TYR D  1 516 ? 30.126  -46.333 -10.907 1.00 37.79 ? 533  TYR D OH  1 
ATOM   17219 N  N   . LEU D  1 517 ? 26.608  -44.899 -5.143  1.00 24.21 ? 534  LEU D N   1 
ATOM   17220 C  CA  . LEU D  1 517 ? 27.718  -44.146 -4.578  1.00 23.62 ? 534  LEU D CA  1 
ATOM   17221 C  C   . LEU D  1 517 ? 28.279  -44.873 -3.351  1.00 22.86 ? 534  LEU D C   1 
ATOM   17222 O  O   . LEU D  1 517 ? 29.492  -45.006 -3.208  1.00 22.58 ? 534  LEU D O   1 
ATOM   17223 C  CB  . LEU D  1 517 ? 27.276  -42.715 -4.267  1.00 22.72 ? 534  LEU D CB  1 
ATOM   17224 C  CG  . LEU D  1 517 ? 26.946  -41.837 -5.482  1.00 21.95 ? 534  LEU D CG  1 
ATOM   17225 C  CD1 . LEU D  1 517 ? 26.219  -40.564 -5.073  1.00 21.77 ? 534  LEU D CD1 1 
ATOM   17226 C  CD2 . LEU D  1 517 ? 28.195  -41.504 -6.267  1.00 21.59 ? 534  LEU D CD2 1 
ATOM   17227 N  N   . TYR D  1 518 ? 27.396  -45.373 -2.485  1.00 23.75 ? 535  TYR D N   1 
ATOM   17228 C  CA  . TYR D  1 518 ? 27.823  -46.096 -1.293  1.00 25.39 ? 535  TYR D CA  1 
ATOM   17229 C  C   . TYR D  1 518 ? 28.545  -47.387 -1.678  1.00 27.58 ? 535  TYR D C   1 
ATOM   17230 O  O   . TYR D  1 518 ? 29.545  -47.737 -1.056  1.00 30.00 ? 535  TYR D O   1 
ATOM   17231 C  CB  . TYR D  1 518 ? 26.636  -46.383 -0.365  1.00 24.49 ? 535  TYR D CB  1 
ATOM   17232 C  CG  . TYR D  1 518 ? 26.311  -45.236 0.582   1.00 23.93 ? 535  TYR D CG  1 
ATOM   17233 C  CD1 . TYR D  1 518 ? 27.139  -44.957 1.666   1.00 23.69 ? 535  TYR D CD1 1 
ATOM   17234 C  CD2 . TYR D  1 518 ? 25.184  -44.439 0.403   1.00 23.73 ? 535  TYR D CD2 1 
ATOM   17235 C  CE1 . TYR D  1 518 ? 26.868  -43.913 2.532   1.00 23.32 ? 535  TYR D CE1 1 
ATOM   17236 C  CE2 . TYR D  1 518 ? 24.896  -43.397 1.272   1.00 23.09 ? 535  TYR D CE2 1 
ATOM   17237 C  CZ  . TYR D  1 518 ? 25.741  -43.132 2.338   1.00 23.70 ? 535  TYR D CZ  1 
ATOM   17238 O  OH  . TYR D  1 518 ? 25.467  -42.106 3.200   1.00 22.73 ? 535  TYR D OH  1 
ATOM   17239 N  N   . ALA D  1 519 ? 28.037  -48.083 -2.706  1.00 29.14 ? 536  ALA D N   1 
ATOM   17240 C  CA  . ALA D  1 519 ? 28.561  -49.384 -3.094  1.00 29.82 ? 536  ALA D CA  1 
ATOM   17241 C  C   . ALA D  1 519 ? 29.952  -49.254 -3.710  1.00 29.96 ? 536  ALA D C   1 
ATOM   17242 O  O   . ALA D  1 519 ? 30.743  -50.189 -3.630  1.00 33.01 ? 536  ALA D O   1 
ATOM   17243 C  CB  . ALA D  1 519 ? 27.600  -50.073 -4.033  1.00 30.13 ? 536  ALA D CB  1 
ATOM   17244 N  N   . ASN D  1 520 ? 30.264  -48.093 -4.296  1.00 28.62 ? 537  ASN D N   1 
ATOM   17245 C  CA  . ASN D  1 520 ? 31.529  -47.912 -4.993  1.00 29.84 ? 537  ASN D CA  1 
ATOM   17246 C  C   . ASN D  1 520 ? 32.465  -46.979 -4.224  1.00 29.91 ? 537  ASN D C   1 
ATOM   17247 O  O   . ASN D  1 520 ? 33.440  -46.489 -4.787  1.00 33.56 ? 537  ASN D O   1 
ATOM   17248 C  CB  . ASN D  1 520 ? 31.300  -47.444 -6.427  1.00 32.37 ? 537  ASN D CB  1 
ATOM   17249 C  CG  . ASN D  1 520 ? 30.607  -48.494 -7.263  1.00 32.47 ? 537  ASN D CG  1 
ATOM   17250 O  OD1 . ASN D  1 520 ? 31.276  -49.259 -7.965  1.00 36.79 ? 537  ASN D OD1 1 
ATOM   17251 N  ND2 . ASN D  1 520 ? 29.288  -48.577 -7.181  1.00 32.09 ? 537  ASN D ND2 1 
ATOM   17252 N  N   . LYS D  1 521 ? 32.190  -46.758 -2.935  1.00 30.15 ? 538  LYS D N   1 
ATOM   17253 C  CA  . LYS D  1 521 ? 33.093  -46.024 -2.061  1.00 31.17 ? 538  LYS D CA  1 
ATOM   17254 C  C   . LYS D  1 521 ? 33.292  -44.601 -2.575  1.00 28.81 ? 538  LYS D C   1 
ATOM   17255 O  O   . LYS D  1 521 ? 34.404  -44.091 -2.555  1.00 29.03 ? 538  LYS D O   1 
ATOM   17256 C  CB  . LYS D  1 521 ? 34.431  -46.762 -1.915  1.00 36.16 ? 538  LYS D CB  1 
ATOM   17257 C  CG  . LYS D  1 521 ? 34.300  -48.219 -1.473  1.00 39.49 ? 538  LYS D CG  1 
ATOM   17258 C  CD  . LYS D  1 521 ? 33.422  -48.435 -0.242  1.00 44.02 ? 538  LYS D CD  1 
ATOM   17259 C  CE  . LYS D  1 521 ? 33.860  -47.639 0.960   1.00 47.38 ? 538  LYS D CE  1 
ATOM   17260 N  NZ  . LYS D  1 521 ? 33.004  -47.874 2.128   1.00 49.10 ? 538  LYS D NZ  1 
ATOM   17261 N  N   . MET D  1 522 ? 32.201  -43.972 -3.029  1.00 26.86 ? 539  MET D N   1 
ATOM   17262 C  CA  . MET D  1 522 ? 32.229  -42.589 -3.474  1.00 26.39 ? 539  MET D CA  1 
ATOM   17263 C  C   . MET D  1 522 ? 31.400  -41.703 -2.542  1.00 24.36 ? 539  MET D C   1 
ATOM   17264 O  O   . MET D  1 522 ? 31.312  -40.501 -2.782  1.00 23.83 ? 539  MET D O   1 
ATOM   17265 C  CB  . MET D  1 522 ? 31.663  -42.466 -4.893  1.00 27.41 ? 539  MET D CB  1 
ATOM   17266 C  CG  . MET D  1 522 ? 32.436  -43.242 -5.942  1.00 29.04 ? 539  MET D CG  1 
ATOM   17267 S  SD  . MET D  1 522 ? 31.445  -43.480 -7.430  1.00 32.68 ? 539  MET D SD  1 
ATOM   17268 C  CE  . MET D  1 522 ? 32.721  -44.014 -8.581  1.00 34.77 ? 539  MET D CE  1 
ATOM   17269 N  N   . ALA D  1 523 ? 30.780  -42.297 -1.509  1.00 23.11 ? 540  ALA D N   1 
ATOM   17270 C  CA  . ALA D  1 523 ? 30.032  -41.553 -0.503  1.00 22.40 ? 540  ALA D CA  1 
ATOM   17271 C  C   . ALA D  1 523 ? 30.876  -41.380 0.761   1.00 22.45 ? 540  ALA D C   1 
ATOM   17272 O  O   . ALA D  1 523 ? 31.678  -42.255 1.103   1.00 21.94 ? 540  ALA D O   1 
ATOM   17273 C  CB  . ALA D  1 523 ? 28.734  -42.264 -0.188  1.00 22.13 ? 540  ALA D CB  1 
ATOM   17274 N  N   . PHE D  1 524 ? 30.675  -40.249 1.453   1.00 22.05 ? 541  PHE D N   1 
ATOM   17275 C  CA  . PHE D  1 524 ? 31.406  -39.938 2.673   1.00 22.14 ? 541  PHE D CA  1 
ATOM   17276 C  C   . PHE D  1 524 ? 30.472  -39.584 3.834   1.00 23.12 ? 541  PHE D C   1 
ATOM   17277 O  O   . PHE D  1 524 ? 30.947  -39.214 4.905   1.00 25.08 ? 541  PHE D O   1 
ATOM   17278 C  CB  . PHE D  1 524 ? 32.400  -38.813 2.372   1.00 21.93 ? 541  PHE D CB  1 
ATOM   17279 C  CG  . PHE D  1 524 ? 33.546  -39.269 1.483   1.00 22.84 ? 541  PHE D CG  1 
ATOM   17280 C  CD1 . PHE D  1 524 ? 34.684  -39.848 2.034   1.00 22.78 ? 541  PHE D CD1 1 
ATOM   17281 C  CD2 . PHE D  1 524 ? 33.455  -39.179 0.096   1.00 23.13 ? 541  PHE D CD2 1 
ATOM   17282 C  CE1 . PHE D  1 524 ? 35.720  -40.280 1.222   1.00 24.32 ? 541  PHE D CE1 1 
ATOM   17283 C  CE2 . PHE D  1 524 ? 34.494  -39.618 -0.712  1.00 23.61 ? 541  PHE D CE2 1 
ATOM   17284 C  CZ  . PHE D  1 524 ? 35.622  -40.170 -0.150  1.00 24.16 ? 541  PHE D CZ  1 
ATOM   17285 N  N   . ARG D  1 525 ? 29.155  -39.717 3.647   1.00 22.95 ? 542  ARG D N   1 
ATOM   17286 C  CA  . ARG D  1 525 ? 28.210  -39.518 4.735   1.00 23.29 ? 542  ARG D CA  1 
ATOM   17287 C  C   . ARG D  1 525 ? 28.050  -40.832 5.498   1.00 23.33 ? 542  ARG D C   1 
ATOM   17288 O  O   . ARG D  1 525 ? 27.499  -41.799 4.975   1.00 21.87 ? 542  ARG D O   1 
ATOM   17289 C  CB  . ARG D  1 525 ? 26.875  -38.986 4.205   1.00 23.18 ? 542  ARG D CB  1 
ATOM   17290 C  CG  . ARG D  1 525 ? 25.933  -38.432 5.262   1.00 23.75 ? 542  ARG D CG  1 
ATOM   17291 C  CD  . ARG D  1 525 ? 25.201  -39.504 6.059   1.00 24.72 ? 542  ARG D CD  1 
ATOM   17292 N  NE  . ARG D  1 525 ? 24.177  -38.891 6.912   1.00 26.03 ? 542  ARG D NE  1 
ATOM   17293 C  CZ  . ARG D  1 525 ? 23.682  -39.390 8.040   1.00 27.28 ? 542  ARG D CZ  1 
ATOM   17294 N  NH1 . ARG D  1 525 ? 24.073  -40.567 8.499   1.00 27.99 ? 542  ARG D NH1 1 
ATOM   17295 N  NH2 . ARG D  1 525 ? 22.787  -38.691 8.714   1.00 27.90 ? 542  ARG D NH2 1 
ATOM   17296 N  N   . TYR D  1 526 ? 28.553  -40.845 6.739   1.00 24.06 ? 543  TYR D N   1 
ATOM   17297 C  CA  . TYR D  1 526 ? 28.468  -42.003 7.616   1.00 25.96 ? 543  TYR D CA  1 
ATOM   17298 C  C   . TYR D  1 526 ? 27.878  -41.566 8.954   1.00 26.86 ? 543  TYR D C   1 
ATOM   17299 O  O   . TYR D  1 526 ? 28.095  -40.436 9.381   1.00 28.15 ? 543  TYR D O   1 
ATOM   17300 C  CB  . TYR D  1 526 ? 29.843  -42.661 7.763   1.00 26.72 ? 543  TYR D CB  1 
ATOM   17301 C  CG  . TYR D  1 526 ? 30.306  -43.328 6.479   1.00 28.16 ? 543  TYR D CG  1 
ATOM   17302 C  CD1 . TYR D  1 526 ? 29.827  -44.580 6.113   1.00 29.95 ? 543  TYR D CD1 1 
ATOM   17303 C  CD2 . TYR D  1 526 ? 31.197  -42.695 5.620   1.00 29.85 ? 543  TYR D CD2 1 
ATOM   17304 C  CE1 . TYR D  1 526 ? 30.221  -45.185 4.929   1.00 30.47 ? 543  TYR D CE1 1 
ATOM   17305 C  CE2 . TYR D  1 526 ? 31.597  -43.288 4.434   1.00 30.64 ? 543  TYR D CE2 1 
ATOM   17306 C  CZ  . TYR D  1 526 ? 31.109  -44.536 4.089   1.00 31.21 ? 543  TYR D CZ  1 
ATOM   17307 O  OH  . TYR D  1 526 ? 31.512  -45.128 2.931   1.00 34.49 ? 543  TYR D OH  1 
ATOM   17308 N  N   . PRO D  1 527 ? 27.115  -42.427 9.666   1.00 28.27 ? 544  PRO D N   1 
ATOM   17309 C  CA  . PRO D  1 527 ? 26.859  -43.801 9.234   1.00 28.62 ? 544  PRO D CA  1 
ATOM   17310 C  C   . PRO D  1 527 ? 26.051  -43.939 7.945   1.00 29.58 ? 544  PRO D C   1 
ATOM   17311 O  O   . PRO D  1 527 ? 25.257  -43.064 7.598   1.00 28.91 ? 544  PRO D O   1 
ATOM   17312 C  CB  . PRO D  1 527 ? 26.123  -44.415 10.435  1.00 29.93 ? 544  PRO D CB  1 
ATOM   17313 C  CG  . PRO D  1 527 ? 25.495  -43.240 11.137  1.00 30.11 ? 544  PRO D CG  1 
ATOM   17314 C  CD  . PRO D  1 527 ? 26.492  -42.112 10.961  1.00 29.64 ? 544  PRO D CD  1 
ATOM   17315 N  N   . GLU D  1 528 ? 26.291  -45.056 7.250   1.00 30.14 ? 545  GLU D N   1 
ATOM   17316 C  CA  . GLU D  1 528 ? 25.616  -45.382 6.003   1.00 31.23 ? 545  GLU D CA  1 
ATOM   17317 C  C   . GLU D  1 528 ? 24.205  -45.873 6.313   1.00 31.59 ? 545  GLU D C   1 
ATOM   17318 O  O   . GLU D  1 528 ? 24.039  -46.769 7.137   1.00 31.09 ? 545  GLU D O   1 
ATOM   17319 C  CB  . GLU D  1 528 ? 26.413  -46.463 5.268   1.00 31.88 ? 545  GLU D CB  1 
ATOM   17320 C  CG  . GLU D  1 528 ? 25.701  -47.040 4.047   1.00 31.60 ? 545  GLU D CG  1 
ATOM   17321 C  CD  . GLU D  1 528 ? 26.521  -47.983 3.180   1.00 32.83 ? 545  GLU D CD  1 
ATOM   17322 O  OE1 . GLU D  1 528 ? 27.744  -48.138 3.389   1.00 34.27 ? 545  GLU D OE1 1 
ATOM   17323 O  OE2 . GLU D  1 528 ? 25.906  -48.574 2.272   1.00 34.47 ? 545  GLU D OE2 1 
ATOM   17324 N  N   . PRO D  1 529 ? 23.148  -45.323 5.668   1.00 30.69 ? 546  PRO D N   1 
ATOM   17325 C  CA  . PRO D  1 529 ? 21.785  -45.800 5.901   1.00 31.44 ? 546  PRO D CA  1 
ATOM   17326 C  C   . PRO D  1 529 ? 21.601  -47.202 5.331   1.00 31.89 ? 546  PRO D C   1 
ATOM   17327 O  O   . PRO D  1 529 ? 22.112  -47.510 4.257   1.00 30.83 ? 546  PRO D O   1 
ATOM   17328 C  CB  . PRO D  1 529 ? 20.915  -44.759 5.177   1.00 31.66 ? 546  PRO D CB  1 
ATOM   17329 C  CG  . PRO D  1 529 ? 21.809  -44.258 4.063   1.00 30.92 ? 546  PRO D CG  1 
ATOM   17330 C  CD  . PRO D  1 529 ? 23.206  -44.249 4.662   1.00 31.08 ? 546  PRO D CD  1 
ATOM   17331 N  N   . GLU D  1 530 ? 20.877  -48.047 6.071   1.00 35.58 ? 547  GLU D N   1 
ATOM   17332 C  CA  . GLU D  1 530 ? 20.537  -49.380 5.603   1.00 38.78 ? 547  GLU D CA  1 
ATOM   17333 C  C   . GLU D  1 530 ? 19.508  -49.285 4.480   1.00 36.69 ? 547  GLU D C   1 
ATOM   17334 O  O   . GLU D  1 530 ? 19.573  -50.043 3.519   1.00 38.71 ? 547  GLU D O   1 
ATOM   17335 C  CB  . GLU D  1 530 ? 19.969  -50.231 6.739   1.00 43.90 ? 547  GLU D CB  1 
ATOM   17336 C  CG  . GLU D  1 530 ? 21.022  -50.673 7.750   1.00 49.59 ? 547  GLU D CG  1 
ATOM   17337 C  CD  . GLU D  1 530 ? 20.458  -51.540 8.863   1.00 53.66 ? 547  GLU D CD  1 
ATOM   17338 O  OE1 . GLU D  1 530 ? 20.628  -51.175 10.046  1.00 56.32 ? 547  GLU D OE1 1 
ATOM   17339 O  OE2 . GLU D  1 530 ? 19.834  -52.575 8.539   1.00 56.90 ? 547  GLU D OE2 1 
ATOM   17340 N  N   . ASP D  1 531 ? 18.553  -48.358 4.632   1.00 36.00 ? 548  ASP D N   1 
ATOM   17341 C  CA  . ASP D  1 531 ? 17.467  -48.168 3.685   1.00 34.52 ? 548  ASP D CA  1 
ATOM   17342 C  C   . ASP D  1 531 ? 17.657  -46.833 2.962   1.00 32.26 ? 548  ASP D C   1 
ATOM   17343 O  O   . ASP D  1 531 ? 17.309  -45.781 3.491   1.00 30.43 ? 548  ASP D O   1 
ATOM   17344 C  CB  . ASP D  1 531 ? 16.128  -48.262 4.400   1.00 34.47 ? 548  ASP D CB  1 
ATOM   17345 C  CG  . ASP D  1 531 ? 14.890  -48.105 3.530   1.00 35.86 ? 548  ASP D CG  1 
ATOM   17346 O  OD1 . ASP D  1 531 ? 15.040  -47.820 2.328   1.00 35.30 ? 548  ASP D OD1 1 
ATOM   17347 O  OD2 . ASP D  1 531 ? 13.778  -48.275 4.066   1.00 40.57 ? 548  ASP D OD2 1 
ATOM   17348 N  N   . LYS D  1 532 ? 18.186  -46.888 1.734   1.00 32.25 ? 549  LYS D N   1 
ATOM   17349 C  CA  . LYS D  1 532 ? 18.498  -45.683 0.978   1.00 31.51 ? 549  LYS D CA  1 
ATOM   17350 C  C   . LYS D  1 532 ? 17.221  -44.938 0.578   1.00 30.64 ? 549  LYS D C   1 
ATOM   17351 O  O   . LYS D  1 532 ? 17.225  -43.713 0.511   1.00 31.76 ? 549  LYS D O   1 
ATOM   17352 C  CB  . LYS D  1 532 ? 19.367  -45.999 -0.242  1.00 30.48 ? 549  LYS D CB  1 
ATOM   17353 C  CG  . LYS D  1 532 ? 20.859  -46.092 0.031   1.00 31.05 ? 549  LYS D CG  1 
ATOM   17354 C  CD  . LYS D  1 532 ? 21.270  -47.190 1.005   1.00 30.88 ? 549  LYS D CD  1 
ATOM   17355 C  CE  . LYS D  1 532 ? 22.745  -47.434 0.983   1.00 31.15 ? 549  LYS D CE  1 
ATOM   17356 N  NZ  . LYS D  1 532 ? 23.127  -48.520 1.892   1.00 32.02 ? 549  LYS D NZ  1 
ATOM   17357 N  N   . ALA D  1 533 ? 16.130  -45.667 0.313   1.00 31.22 ? 550  ALA D N   1 
ATOM   17358 C  CA  . ALA D  1 533 ? 14.890  -45.038 -0.120  1.00 30.81 ? 550  ALA D CA  1 
ATOM   17359 C  C   . ALA D  1 533 ? 14.371  -44.103 0.969   1.00 30.81 ? 550  ALA D C   1 
ATOM   17360 O  O   . ALA D  1 533 ? 14.023  -42.955 0.695   1.00 28.50 ? 550  ALA D O   1 
ATOM   17361 C  CB  . ALA D  1 533 ? 13.864  -46.088 -0.491  1.00 31.64 ? 550  ALA D CB  1 
ATOM   17362 N  N   . LYS D  1 534 ? 14.342  -44.612 2.205   1.00 30.68 ? 551  LYS D N   1 
ATOM   17363 C  CA  . LYS D  1 534 ? 13.917  -43.849 3.364   1.00 31.56 ? 551  LYS D CA  1 
ATOM   17364 C  C   . LYS D  1 534 ? 14.862  -42.668 3.584   1.00 28.63 ? 551  LYS D C   1 
ATOM   17365 O  O   . LYS D  1 534 ? 14.404  -41.560 3.836   1.00 28.29 ? 551  LYS D O   1 
ATOM   17366 C  CB  . LYS D  1 534 ? 13.868  -44.789 4.575   1.00 35.99 ? 551  LYS D CB  1 
ATOM   17367 C  CG  . LYS D  1 534 ? 13.563  -44.146 5.920   1.00 40.48 ? 551  LYS D CG  1 
ATOM   17368 C  CD  . LYS D  1 534 ? 13.823  -45.086 7.092   1.00 45.05 ? 551  LYS D CD  1 
ATOM   17369 C  CE  . LYS D  1 534 ? 13.667  -44.423 8.427   1.00 48.47 ? 551  LYS D CE  1 
ATOM   17370 N  NZ  . LYS D  1 534 ? 14.075  -45.324 9.510   1.00 51.56 ? 551  LYS D NZ  1 
ATOM   17371 N  N   . TYR D  1 535 ? 16.175  -42.918 3.478   1.00 25.86 ? 552  TYR D N   1 
ATOM   17372 C  CA  . TYR D  1 535 ? 17.193  -41.897 3.681   1.00 24.79 ? 552  TYR D CA  1 
ATOM   17373 C  C   . TYR D  1 535 ? 16.943  -40.693 2.773   1.00 23.94 ? 552  TYR D C   1 
ATOM   17374 O  O   . TYR D  1 535 ? 17.011  -39.552 3.225   1.00 22.40 ? 552  TYR D O   1 
ATOM   17375 C  CB  . TYR D  1 535 ? 18.578  -42.490 3.409   1.00 24.60 ? 552  TYR D CB  1 
ATOM   17376 C  CG  . TYR D  1 535 ? 19.730  -41.505 3.523   1.00 24.13 ? 552  TYR D CG  1 
ATOM   17377 C  CD1 . TYR D  1 535 ? 20.187  -41.089 4.767   1.00 23.88 ? 552  TYR D CD1 1 
ATOM   17378 C  CD2 . TYR D  1 535 ? 20.370  -41.001 2.393   1.00 24.00 ? 552  TYR D CD2 1 
ATOM   17379 C  CE1 . TYR D  1 535 ? 21.234  -40.191 4.888   1.00 23.98 ? 552  TYR D CE1 1 
ATOM   17380 C  CE2 . TYR D  1 535 ? 21.424  -40.106 2.503   1.00 23.67 ? 552  TYR D CE2 1 
ATOM   17381 C  CZ  . TYR D  1 535 ? 21.853  -39.696 3.755   1.00 24.05 ? 552  TYR D CZ  1 
ATOM   17382 O  OH  . TYR D  1 535 ? 22.886  -38.809 3.893   1.00 24.55 ? 552  TYR D OH  1 
ATOM   17383 N  N   . VAL D  1 536 ? 16.682  -40.956 1.487   1.00 24.73 ? 553  VAL D N   1 
ATOM   17384 C  CA  . VAL D  1 536 ? 16.502  -39.890 0.515   1.00 24.62 ? 553  VAL D CA  1 
ATOM   17385 C  C   . VAL D  1 536 ? 15.168  -39.188 0.776   1.00 25.63 ? 553  VAL D C   1 
ATOM   17386 O  O   . VAL D  1 536 ? 15.119  -37.960 0.830   1.00 26.02 ? 553  VAL D O   1 
ATOM   17387 C  CB  . VAL D  1 536 ? 16.631  -40.415 -0.928  1.00 24.38 ? 553  VAL D CB  1 
ATOM   17388 C  CG1 . VAL D  1 536 ? 16.232  -39.366 -1.960  1.00 24.57 ? 553  VAL D CG1 1 
ATOM   17389 C  CG2 . VAL D  1 536 ? 18.040  -40.921 -1.217  1.00 23.57 ? 553  VAL D CG2 1 
ATOM   17390 N  N   . LYS D  1 537 ? 14.097  -39.962 0.983   1.00 26.34 ? 554  LYS D N   1 
ATOM   17391 C  CA  . LYS D  1 537 ? 12.754  -39.401 1.080   1.00 28.30 ? 554  LYS D CA  1 
ATOM   17392 C  C   . LYS D  1 537 ? 12.572  -38.551 2.339   1.00 28.55 ? 554  LYS D C   1 
ATOM   17393 O  O   . LYS D  1 537 ? 11.786  -37.604 2.329   1.00 28.66 ? 554  LYS D O   1 
ATOM   17394 C  CB  . LYS D  1 537 ? 11.693  -40.504 1.009   1.00 30.00 ? 554  LYS D CB  1 
ATOM   17395 C  CG  . LYS D  1 537 ? 11.521  -41.083 -0.382  1.00 31.67 ? 554  LYS D CG  1 
ATOM   17396 C  CD  . LYS D  1 537 ? 10.557  -42.255 -0.494  1.00 33.34 ? 554  LYS D CD  1 
ATOM   17397 C  CE  . LYS D  1 537 ? 10.406  -42.669 -1.926  1.00 35.69 ? 554  LYS D CE  1 
ATOM   17398 N  NZ  . LYS D  1 537 ? 9.574   -43.863 -2.091  1.00 37.70 ? 554  LYS D NZ  1 
ATOM   17399 N  N   . GLU D  1 538 ? 13.293  -38.872 3.420   1.00 28.86 ? 555  GLU D N   1 
ATOM   17400 C  CA  . GLU D  1 538 ? 13.164  -38.111 4.656   1.00 30.22 ? 555  GLU D CA  1 
ATOM   17401 C  C   . GLU D  1 538 ? 13.931  -36.791 4.586   1.00 28.48 ? 555  GLU D C   1 
ATOM   17402 O  O   . GLU D  1 538 ? 13.713  -35.930 5.431   1.00 27.39 ? 555  GLU D O   1 
ATOM   17403 C  CB  . GLU D  1 538 ? 13.630  -38.910 5.872   1.00 33.00 ? 555  GLU D CB  1 
ATOM   17404 C  CG  . GLU D  1 538 ? 12.597  -39.938 6.318   1.00 36.29 ? 555  GLU D CG  1 
ATOM   17405 C  CD  . GLU D  1 538 ? 13.035  -40.875 7.427   1.00 39.99 ? 555  GLU D CD  1 
ATOM   17406 O  OE1 . GLU D  1 538 ? 14.205  -40.815 7.874   1.00 40.73 ? 555  GLU D OE1 1 
ATOM   17407 O  OE2 . GLU D  1 538 ? 12.167  -41.678 7.836   1.00 44.47 ? 555  GLU D OE2 1 
ATOM   17408 N  N   . ARG D  1 539 ? 14.823  -36.629 3.596   1.00 26.73 ? 556  ARG D N   1 
ATOM   17409 C  CA  . ARG D  1 539 ? 15.678  -35.452 3.533   1.00 25.91 ? 556  ARG D CA  1 
ATOM   17410 C  C   . ARG D  1 539 ? 15.228  -34.442 2.471   1.00 25.57 ? 556  ARG D C   1 
ATOM   17411 O  O   . ARG D  1 539 ? 15.799  -33.355 2.401   1.00 26.65 ? 556  ARG D O   1 
ATOM   17412 C  CB  . ARG D  1 539 ? 17.128  -35.913 3.351   1.00 25.12 ? 556  ARG D CB  1 
ATOM   17413 C  CG  . ARG D  1 539 ? 17.687  -36.451 4.661   1.00 26.10 ? 556  ARG D CG  1 
ATOM   17414 C  CD  . ARG D  1 539 ? 19.031  -37.154 4.541   1.00 27.35 ? 556  ARG D CD  1 
ATOM   17415 N  NE  . ARG D  1 539 ? 19.455  -37.623 5.866   1.00 29.24 ? 556  ARG D NE  1 
ATOM   17416 C  CZ  . ARG D  1 539 ? 18.845  -38.558 6.597   1.00 29.64 ? 556  ARG D CZ  1 
ATOM   17417 N  NH1 . ARG D  1 539 ? 17.852  -39.270 6.092   1.00 28.92 ? 556  ARG D NH1 1 
ATOM   17418 N  NH2 . ARG D  1 539 ? 19.262  -38.808 7.828   1.00 29.81 ? 556  ARG D NH2 1 
ATOM   17419 N  N   . THR D  1 540 ? 14.207  -34.763 1.662   1.00 25.98 ? 557  THR D N   1 
ATOM   17420 C  CA  . THR D  1 540 ? 13.758  -33.835 0.628   1.00 25.74 ? 557  THR D CA  1 
ATOM   17421 C  C   . THR D  1 540 ? 13.044  -32.659 1.296   1.00 24.99 ? 557  THR D C   1 
ATOM   17422 O  O   . THR D  1 540 ? 12.311  -32.845 2.262   1.00 23.97 ? 557  THR D O   1 
ATOM   17423 C  CB  . THR D  1 540 ? 12.860  -34.511 -0.413  1.00 26.77 ? 557  THR D CB  1 
ATOM   17424 O  OG1 . THR D  1 540 ? 11.797  -35.182 0.262   1.00 25.75 ? 557  THR D OG1 1 
ATOM   17425 C  CG2 . THR D  1 540 ? 13.610  -35.507 -1.277  1.00 27.43 ? 557  THR D CG2 1 
ATOM   17426 N  N   . TRP D  1 541 ? 13.282  -31.450 0.772   1.00 24.15 ? 558  TRP D N   1 
ATOM   17427 C  CA  . TRP D  1 541 ? 12.659  -30.233 1.270   1.00 24.89 ? 558  TRP D CA  1 
ATOM   17428 C  C   . TRP D  1 541 ? 11.165  -30.237 0.945   1.00 26.07 ? 558  TRP D C   1 
ATOM   17429 O  O   . TRP D  1 541 ? 10.760  -30.654 -0.140  1.00 26.38 ? 558  TRP D O   1 
ATOM   17430 C  CB  . TRP D  1 541 ? 13.348  -29.002 0.659   1.00 24.39 ? 558  TRP D CB  1 
ATOM   17431 C  CG  . TRP D  1 541 ? 12.775  -27.683 1.111   1.00 23.58 ? 558  TRP D CG  1 
ATOM   17432 C  CD1 . TRP D  1 541 ? 13.046  -27.026 2.277   1.00 24.38 ? 558  TRP D CD1 1 
ATOM   17433 C  CD2 . TRP D  1 541 ? 11.838  -26.851 0.394   1.00 22.80 ? 558  TRP D CD2 1 
ATOM   17434 N  NE1 . TRP D  1 541 ? 12.344  -25.849 2.337   1.00 23.27 ? 558  TRP D NE1 1 
ATOM   17435 C  CE2 . TRP D  1 541 ? 11.599  -25.713 1.196   1.00 23.71 ? 558  TRP D CE2 1 
ATOM   17436 C  CE3 . TRP D  1 541 ? 11.184  -26.953 -0.838  1.00 23.30 ? 558  TRP D CE3 1 
ATOM   17437 C  CZ2 . TRP D  1 541 ? 10.731  -24.693 0.802   1.00 23.96 ? 558  TRP D CZ2 1 
ATOM   17438 C  CZ3 . TRP D  1 541 ? 10.336  -25.938 -1.227  1.00 23.53 ? 558  TRP D CZ3 1 
ATOM   17439 C  CH2 . TRP D  1 541 ? 10.113  -24.827 -0.417  1.00 22.82 ? 558  TRP D CH2 1 
ATOM   17440 N  N   . ARG D  1 542 ? 10.360  -29.738 1.889   1.00 27.67 ? 559  ARG D N   1 
ATOM   17441 C  CA  . ARG D  1 542 ? 8.910   -29.742 1.764   1.00 29.27 ? 559  ARG D CA  1 
ATOM   17442 C  C   . ARG D  1 542 ? 8.394   -28.306 1.715   1.00 27.94 ? 559  ARG D C   1 
ATOM   17443 O  O   . ARG D  1 542 ? 8.856   -27.458 2.473   1.00 27.94 ? 559  ARG D O   1 
ATOM   17444 C  CB  . ARG D  1 542 ? 8.311   -30.495 2.957   1.00 32.01 ? 559  ARG D CB  1 
ATOM   17445 C  CG  . ARG D  1 542 ? 8.556   -31.997 2.939   1.00 35.07 ? 559  ARG D CG  1 
ATOM   17446 C  CD  . ARG D  1 542 ? 8.097   -32.652 4.235   1.00 39.57 ? 559  ARG D CD  1 
ATOM   17447 N  NE  . ARG D  1 542 ? 6.659   -32.511 4.503   1.00 42.70 ? 559  ARG D NE  1 
ATOM   17448 C  CZ  . ARG D  1 542 ? 5.669   -33.119 3.847   1.00 45.78 ? 559  ARG D CZ  1 
ATOM   17449 N  NH1 . ARG D  1 542 ? 5.932   -33.957 2.856   1.00 46.69 ? 559  ARG D NH1 1 
ATOM   17450 N  NH2 . ARG D  1 542 ? 4.411   -32.891 4.190   1.00 46.50 ? 559  ARG D NH2 1 
ATOM   17451 N  N   . SER D  1 543 ? 7.409   -28.060 0.845   1.00 27.15 ? 560  SER D N   1 
ATOM   17452 C  CA  . SER D  1 543 ? 6.892   -26.721 0.609   1.00 28.04 ? 560  SER D CA  1 
ATOM   17453 C  C   . SER D  1 543 ? 5.661   -26.443 1.472   1.00 27.62 ? 560  SER D C   1 
ATOM   17454 O  O   . SER D  1 543 ? 5.101   -25.351 1.400   1.00 27.66 ? 560  SER D O   1 
ATOM   17455 C  CB  . SER D  1 543 ? 6.594   -26.506 -0.866  1.00 28.38 ? 560  SER D CB  1 
ATOM   17456 O  OG  . SER D  1 543 ? 5.657   -27.457 -1.353  1.00 28.30 ? 560  SER D OG  1 
ATOM   17457 N  N   . GLU D  1 544 ? 5.241   -27.415 2.289   1.00 27.41 ? 561  GLU D N   1 
ATOM   17458 C  CA  . GLU D  1 544 ? 4.153   -27.188 3.228   1.00 28.50 ? 561  GLU D CA  1 
ATOM   17459 C  C   . GLU D  1 544 ? 4.592   -26.161 4.269   1.00 26.33 ? 561  GLU D C   1 
ATOM   17460 O  O   . GLU D  1 544 ? 5.718   -26.211 4.758   1.00 25.13 ? 561  GLU D O   1 
ATOM   17461 C  CB  . GLU D  1 544 ? 3.695   -28.436 3.989   1.00 30.00 ? 561  GLU D CB  1 
ATOM   17462 C  CG  . GLU D  1 544 ? 2.888   -29.427 3.154   1.00 31.64 ? 561  GLU D CG  1 
ATOM   17463 C  CD  . GLU D  1 544 ? 3.702   -30.421 2.344   1.00 35.29 ? 561  GLU D CD  1 
ATOM   17464 O  OE1 . GLU D  1 544 ? 3.063   -31.260 1.672   1.00 36.88 ? 561  GLU D OE1 1 
ATOM   17465 O  OE2 . GLU D  1 544 ? 4.954   -30.379 2.382   1.00 36.59 ? 561  GLU D OE2 1 
ATOM   17466 N  N   . TYR D  1 545 ? 3.684   -25.239 4.609   1.00 24.97 ? 562  TYR D N   1 
ATOM   17467 C  CA  . TYR D  1 545 ? 3.923   -24.264 5.659   1.00 25.73 ? 562  TYR D CA  1 
ATOM   17468 C  C   . TYR D  1 545 ? 4.076   -24.969 7.004   1.00 27.15 ? 562  TYR D C   1 
ATOM   17469 O  O   . TYR D  1 545 ? 3.429   -25.984 7.255   1.00 26.64 ? 562  TYR D O   1 
ATOM   17470 C  CB  . TYR D  1 545 ? 2.759   -23.281 5.809   1.00 25.39 ? 562  TYR D CB  1 
ATOM   17471 C  CG  . TYR D  1 545 ? 2.524   -22.304 4.665   1.00 24.43 ? 562  TYR D CG  1 
ATOM   17472 C  CD1 . TYR D  1 545 ? 3.574   -21.624 4.054   1.00 23.51 ? 562  TYR D CD1 1 
ATOM   17473 C  CD2 . TYR D  1 545 ? 1.234   -22.043 4.217   1.00 24.94 ? 562  TYR D CD2 1 
ATOM   17474 C  CE1 . TYR D  1 545 ? 3.347   -20.718 3.028   1.00 23.51 ? 562  TYR D CE1 1 
ATOM   17475 C  CE2 . TYR D  1 545 ? 0.994   -21.144 3.191   1.00 24.04 ? 562  TYR D CE2 1 
ATOM   17476 C  CZ  . TYR D  1 545 ? 2.051   -20.476 2.598   1.00 24.23 ? 562  TYR D CZ  1 
ATOM   17477 O  OH  . TYR D  1 545 ? 1.794   -19.591 1.591   1.00 23.18 ? 562  TYR D OH  1 
ATOM   17478 N  N   . ASP D  1 546 ? 4.911   -24.391 7.873   1.00 29.30 ? 563  ASP D N   1 
ATOM   17479 C  CA  . ASP D  1 546 ? 5.032   -24.835 9.250   1.00 31.57 ? 563  ASP D CA  1 
ATOM   17480 C  C   . ASP D  1 546 ? 4.214   -23.904 10.139  1.00 30.40 ? 563  ASP D C   1 
ATOM   17481 O  O   . ASP D  1 546 ? 3.835   -22.811 9.722   1.00 28.11 ? 563  ASP D O   1 
ATOM   17482 C  CB  . ASP D  1 546 ? 6.486   -24.890 9.686   1.00 34.76 ? 563  ASP D CB  1 
ATOM   17483 C  CG  . ASP D  1 546 ? 7.380   -25.756 8.811   1.00 37.26 ? 563  ASP D CG  1 
ATOM   17484 O  OD1 . ASP D  1 546 ? 7.011   -26.923 8.574   1.00 39.27 ? 563  ASP D OD1 1 
ATOM   17485 O  OD2 . ASP D  1 546 ? 8.437   -25.258 8.373   1.00 41.94 ? 563  ASP D OD2 1 
ATOM   17486 N  N   . SER D  1 547 ? 3.922   -24.378 11.353  1.00 29.47 ? 564  SER D N   1 
ATOM   17487 C  CA  . SER D  1 547 ? 3.321   -23.556 12.387  1.00 30.44 ? 564  SER D CA  1 
ATOM   17488 C  C   . SER D  1 547 ? 4.386   -22.608 12.930  1.00 30.73 ? 564  SER D C   1 
ATOM   17489 O  O   . SER D  1 547 ? 5.516   -23.026 13.178  1.00 30.98 ? 564  SER D O   1 
ATOM   17490 C  CB  . SER D  1 547 ? 2.724   -24.408 13.484  1.00 29.89 ? 564  SER D CB  1 
ATOM   17491 O  OG  . SER D  1 547 ? 2.230   -23.611 14.551  1.00 29.27 ? 564  SER D OG  1 
ATOM   17492 N  N   . LEU D  1 548 ? 4.023   -21.328 13.078  1.00 29.41 ? 565  LEU D N   1 
ATOM   17493 C  CA  . LEU D  1 548 ? 4.915   -20.337 13.660  1.00 30.05 ? 565  LEU D CA  1 
ATOM   17494 C  C   . LEU D  1 548 ? 4.324   -19.824 14.971  1.00 29.46 ? 565  LEU D C   1 
ATOM   17495 O  O   . LEU D  1 548 ? 4.754   -18.792 15.477  1.00 29.29 ? 565  LEU D O   1 
ATOM   17496 C  CB  . LEU D  1 548 ? 5.159   -19.204 12.662  1.00 30.42 ? 565  LEU D CB  1 
ATOM   17497 C  CG  . LEU D  1 548 ? 5.846   -19.606 11.353  1.00 32.29 ? 565  LEU D CG  1 
ATOM   17498 C  CD1 . LEU D  1 548 ? 5.962   -18.420 10.418  1.00 33.94 ? 565  LEU D CD1 1 
ATOM   17499 C  CD2 . LEU D  1 548 ? 7.217   -20.211 11.589  1.00 33.62 ? 565  LEU D CD2 1 
ATOM   17500 N  N   . LEU D  1 549 ? 3.366   -20.580 15.528  1.00 28.86 ? 566  LEU D N   1 
ATOM   17501 C  CA  . LEU D  1 549 ? 2.660   -20.188 16.735  1.00 28.04 ? 566  LEU D CA  1 
ATOM   17502 C  C   . LEU D  1 549 ? 3.546   -20.434 17.954  1.00 29.46 ? 566  LEU D C   1 
ATOM   17503 O  O   . LEU D  1 549 ? 3.931   -21.575 18.208  1.00 27.71 ? 566  LEU D O   1 
ATOM   17504 C  CB  . LEU D  1 549 ? 1.367   -20.997 16.833  1.00 28.80 ? 566  LEU D CB  1 
ATOM   17505 C  CG  . LEU D  1 549 ? 0.474   -20.687 18.039  1.00 29.44 ? 566  LEU D CG  1 
ATOM   17506 C  CD1 . LEU D  1 549 ? -0.134  -19.302 17.903  1.00 29.95 ? 566  LEU D CD1 1 
ATOM   17507 C  CD2 . LEU D  1 549 ? -0.612  -21.727 18.235  1.00 29.25 ? 566  LEU D CD2 1 
ATOM   17508 N  N   . PRO D  1 550 ? 3.878   -19.393 18.759  1.00 28.10 ? 567  PRO D N   1 
ATOM   17509 C  CA  . PRO D  1 550 ? 4.568   -19.599 20.034  1.00 27.97 ? 567  PRO D CA  1 
ATOM   17510 C  C   . PRO D  1 550 ? 3.817   -20.581 20.929  1.00 27.77 ? 567  PRO D C   1 
ATOM   17511 O  O   . PRO D  1 550 ? 2.592   -20.638 20.892  1.00 26.42 ? 567  PRO D O   1 
ATOM   17512 C  CB  . PRO D  1 550 ? 4.628   -18.203 20.670  1.00 27.41 ? 567  PRO D CB  1 
ATOM   17513 C  CG  . PRO D  1 550 ? 4.450   -17.244 19.521  1.00 27.86 ? 567  PRO D CG  1 
ATOM   17514 C  CD  . PRO D  1 550 ? 3.617   -17.973 18.481  1.00 28.18 ? 567  PRO D CD  1 
ATOM   17515 N  N   . ASP D  1 551 ? 4.571   -21.310 21.758  1.00 26.67 ? 568  ASP D N   1 
ATOM   17516 C  CA  . ASP D  1 551 ? 4.018   -22.349 22.611  1.00 26.63 ? 568  ASP D CA  1 
ATOM   17517 C  C   . ASP D  1 551 ? 3.598   -21.742 23.949  1.00 26.31 ? 568  ASP D C   1 
ATOM   17518 O  O   . ASP D  1 551 ? 4.447   -21.423 24.780  1.00 23.65 ? 568  ASP D O   1 
ATOM   17519 C  CB  . ASP D  1 551 ? 5.020   -23.479 22.792  1.00 27.58 ? 568  ASP D CB  1 
ATOM   17520 C  CG  . ASP D  1 551 ? 4.468   -24.727 23.467  1.00 29.35 ? 568  ASP D CG  1 
ATOM   17521 O  OD1 . ASP D  1 551 ? 3.239   -24.788 23.651  1.00 28.93 ? 568  ASP D OD1 1 
ATOM   17522 O  OD2 . ASP D  1 551 ? 5.274   -25.624 23.808  1.00 29.21 ? 568  ASP D OD2 1 
ATOM   17523 N  N   . VAL D  1 552 ? 2.277   -21.611 24.148  1.00 26.54 ? 569  VAL D N   1 
ATOM   17524 C  CA  . VAL D  1 552 ? 1.712   -20.970 25.323  1.00 26.66 ? 569  VAL D CA  1 
ATOM   17525 C  C   . VAL D  1 552 ? 0.972   -22.021 26.147  1.00 26.61 ? 569  VAL D C   1 
ATOM   17526 O  O   . VAL D  1 552 ? 0.174   -22.777 25.597  1.00 27.00 ? 569  VAL D O   1 
ATOM   17527 C  CB  . VAL D  1 552 ? 0.763   -19.821 24.922  1.00 27.31 ? 569  VAL D CB  1 
ATOM   17528 C  CG1 . VAL D  1 552 ? 0.180   -19.116 26.142  1.00 27.58 ? 569  VAL D CG1 1 
ATOM   17529 C  CG2 . VAL D  1 552 ? 1.441   -18.811 24.004  1.00 27.60 ? 569  VAL D CG2 1 
ATOM   17530 N  N   . TYR D  1 553 ? 1.228   -22.037 27.463  1.00 26.25 ? 570  TYR D N   1 
ATOM   17531 C  CA  . TYR D  1 553 ? 0.705   -23.064 28.351  1.00 26.84 ? 570  TYR D CA  1 
ATOM   17532 C  C   . TYR D  1 553 ? 0.810   -22.594 29.800  1.00 28.88 ? 570  TYR D C   1 
ATOM   17533 O  O   . TYR D  1 553 ? 1.668   -21.779 30.136  1.00 27.79 ? 570  TYR D O   1 
ATOM   17534 C  CB  . TYR D  1 553 ? 1.450   -24.386 28.129  1.00 26.09 ? 570  TYR D CB  1 
ATOM   17535 C  CG  . TYR D  1 553 ? 2.967   -24.305 28.284  1.00 24.75 ? 570  TYR D CG  1 
ATOM   17536 C  CD1 . TYR D  1 553 ? 3.781   -23.979 27.206  1.00 24.67 ? 570  TYR D CD1 1 
ATOM   17537 C  CD2 . TYR D  1 553 ? 3.582   -24.555 29.504  1.00 24.59 ? 570  TYR D CD2 1 
ATOM   17538 C  CE1 . TYR D  1 553 ? 5.160   -23.908 27.335  1.00 24.41 ? 570  TYR D CE1 1 
ATOM   17539 C  CE2 . TYR D  1 553 ? 4.959   -24.488 29.647  1.00 24.76 ? 570  TYR D CE2 1 
ATOM   17540 C  CZ  . TYR D  1 553 ? 5.751   -24.160 28.561  1.00 24.75 ? 570  TYR D CZ  1 
ATOM   17541 O  OH  . TYR D  1 553 ? 7.106   -24.082 28.708  1.00 24.89 ? 570  TYR D OH  1 
ATOM   17542 N  N   . GLU D  1 554 ? -0.081  -23.118 30.651  1.00 31.22 ? 571  GLU D N   1 
ATOM   17543 C  CA  . GLU D  1 554 ? -0.091  -22.790 32.068  1.00 35.04 ? 571  GLU D CA  1 
ATOM   17544 C  C   . GLU D  1 554 ? 0.943   -23.631 32.811  1.00 33.67 ? 571  GLU D C   1 
ATOM   17545 O  O   . GLU D  1 554 ? 1.172   -24.786 32.463  1.00 31.31 ? 571  GLU D O   1 
ATOM   17546 C  CB  . GLU D  1 554 ? -1.478  -23.016 32.672  1.00 39.16 ? 571  GLU D CB  1 
ATOM   17547 C  CG  . GLU D  1 554 ? -2.491  -21.962 32.234  1.00 43.39 ? 571  GLU D CG  1 
ATOM   17548 C  CD  . GLU D  1 554 ? -3.918  -22.215 32.689  1.00 48.84 ? 571  GLU D CD  1 
ATOM   17549 O  OE1 . GLU D  1 554 ? -4.228  -23.348 33.117  1.00 50.73 ? 571  GLU D OE1 1 
ATOM   17550 O  OE2 . GLU D  1 554 ? -4.719  -21.258 32.623  1.00 52.48 ? 571  GLU D OE2 1 
ATOM   17551 N  N   . TRP D  1 555 ? 1.565   -23.021 33.827  1.00 35.59 ? 572  TRP D N   1 
ATOM   17552 C  CA  . TRP D  1 555 ? 2.406   -23.731 34.776  1.00 37.17 ? 572  TRP D CA  1 
ATOM   17553 C  C   . TRP D  1 555 ? 1.542   -24.295 35.900  1.00 41.23 ? 572  TRP D C   1 
ATOM   17554 O  O   . TRP D  1 555 ? 0.483   -23.746 36.193  1.00 41.04 ? 572  TRP D O   1 
ATOM   17555 C  CB  . TRP D  1 555 ? 3.479   -22.801 35.359  1.00 36.49 ? 572  TRP D CB  1 
ATOM   17556 C  CG  . TRP D  1 555 ? 4.761   -22.715 34.574  1.00 34.37 ? 572  TRP D CG  1 
ATOM   17557 C  CD1 . TRP D  1 555 ? 5.132   -23.441 33.479  1.00 33.93 ? 572  TRP D CD1 1 
ATOM   17558 C  CD2 . TRP D  1 555 ? 5.882   -21.863 34.890  1.00 33.73 ? 572  TRP D CD2 1 
ATOM   17559 N  NE1 . TRP D  1 555 ? 6.396   -23.089 33.085  1.00 33.66 ? 572  TRP D NE1 1 
ATOM   17560 C  CE2 . TRP D  1 555 ? 6.882   -22.126 33.930  1.00 33.19 ? 572  TRP D CE2 1 
ATOM   17561 C  CE3 . TRP D  1 555 ? 6.133   -20.907 35.881  1.00 36.07 ? 572  TRP D CE3 1 
ATOM   17562 C  CZ2 . TRP D  1 555 ? 8.108   -21.463 33.935  1.00 35.01 ? 572  TRP D CZ2 1 
ATOM   17563 C  CZ3 . TRP D  1 555 ? 7.346   -20.252 35.885  1.00 36.98 ? 572  TRP D CZ3 1 
ATOM   17564 C  CH2 . TRP D  1 555 ? 8.322   -20.534 34.926  1.00 35.74 ? 572  TRP D CH2 1 
ATOM   17565 N  N   . PRO D  1 556 ? 1.959   -25.399 36.564  1.00 46.36 ? 573  PRO D N   1 
ATOM   17566 C  CA  . PRO D  1 556 ? 1.308   -25.846 37.798  1.00 49.95 ? 573  PRO D CA  1 
ATOM   17567 C  C   . PRO D  1 556 ? 1.496   -24.820 38.914  1.00 53.26 ? 573  PRO D C   1 
ATOM   17568 O  O   . PRO D  1 556 ? 2.545   -24.184 39.003  1.00 55.33 ? 573  PRO D O   1 
ATOM   17569 C  CB  . PRO D  1 556 ? 1.993   -27.190 38.116  1.00 49.74 ? 573  PRO D CB  1 
ATOM   17570 C  CG  . PRO D  1 556 ? 2.655   -27.598 36.818  1.00 48.71 ? 573  PRO D CG  1 
ATOM   17571 C  CD  . PRO D  1 556 ? 3.052   -26.293 36.155  1.00 47.67 ? 573  PRO D CD  1 
ATOM   17572 N  N   . GLU D  1 557 ? 0.472   -24.671 39.764  1.00 57.70 ? 574  GLU D N   1 
ATOM   17573 C  CA  . GLU D  1 557 ? 0.489   -23.692 40.842  1.00 60.27 ? 574  GLU D CA  1 
ATOM   17574 C  C   . GLU D  1 557 ? 1.403   -24.188 41.977  1.00 60.88 ? 574  GLU D C   1 
ATOM   17575 O  O   . GLU D  1 557 ? 1.943   -23.316 42.698  1.00 64.60 ? 574  GLU D O   1 
ATOM   17576 C  CB  . GLU D  1 557 ? -0.926  -23.432 41.362  1.00 59.17 ? 574  GLU D CB  1 
ATOM   17577 N  N   . PRO D  1 562 ? 5.616   -18.759 47.742  1.00 73.65 ? 579  PRO D N   1 
ATOM   17578 C  CA  . PRO D  1 562 ? 6.380   -17.575 47.365  1.00 73.72 ? 579  PRO D CA  1 
ATOM   17579 C  C   . PRO D  1 562 ? 6.649   -16.689 48.582  1.00 72.39 ? 579  PRO D C   1 
ATOM   17580 O  O   . PRO D  1 562 ? 5.812   -15.864 48.943  1.00 72.25 ? 579  PRO D O   1 
ATOM   17581 C  CB  . PRO D  1 562 ? 5.519   -16.874 46.295  1.00 74.12 ? 579  PRO D CB  1 
ATOM   17582 C  CG  . PRO D  1 562 ? 4.135   -17.437 46.512  1.00 74.76 ? 579  PRO D CG  1 
ATOM   17583 C  CD  . PRO D  1 562 ? 4.389   -18.863 46.966  1.00 74.40 ? 579  PRO D CD  1 
ATOM   17584 N  N   . PRO D  1 563 ? 7.816   -16.834 49.257  1.00 69.60 ? 580  PRO D N   1 
ATOM   17585 C  CA  . PRO D  1 563 ? 8.120   -16.046 50.454  1.00 68.10 ? 580  PRO D CA  1 
ATOM   17586 C  C   . PRO D  1 563 ? 8.333   -14.569 50.147  1.00 66.70 ? 580  PRO D C   1 
ATOM   17587 O  O   . PRO D  1 563 ? 7.916   -13.761 51.000  1.00 68.59 ? 580  PRO D O   1 
ATOM   17588 C  CB  . PRO D  1 563 ? 9.396   -16.719 50.989  1.00 66.15 ? 580  PRO D CB  1 
ATOM   17589 C  CG  . PRO D  1 563 ? 10.065  -17.255 49.746  1.00 66.44 ? 580  PRO D CG  1 
ATOM   17590 C  CD  . PRO D  1 563 ? 8.908   -17.755 48.900  1.00 68.51 ? 580  PRO D CD  1 
HETATM 17591 P  PA  A NAD E  2 .   ? 34.874  -30.492 9.783   0.30 30.93 ? 601  NAD A PA  1 
HETATM 17592 P  PA  B NAD E  2 .   ? 34.885  -30.452 9.850   0.70 35.23 ? 601  NAD A PA  1 
HETATM 17593 O  O1A A NAD E  2 .   ? 34.213  -31.661 9.134   0.30 32.03 ? 601  NAD A O1A 1 
HETATM 17594 O  O1A B NAD E  2 .   ? 34.116  -31.511 9.138   0.70 37.73 ? 601  NAD A O1A 1 
HETATM 17595 O  O2A A NAD E  2 .   ? 36.336  -30.304 9.560   0.30 32.16 ? 601  NAD A O2A 1 
HETATM 17596 O  O2A B NAD E  2 .   ? 36.335  -30.319 9.543   0.70 38.06 ? 601  NAD A O2A 1 
HETATM 17597 O  O5B A NAD E  2 .   ? 34.573  -30.518 11.359  0.30 28.42 ? 601  NAD A O5B 1 
HETATM 17598 O  O5B B NAD E  2 .   ? 34.684  -30.604 11.436  0.70 30.36 ? 601  NAD A O5B 1 
HETATM 17599 C  C5B A NAD E  2 .   ? 34.287  -31.800 11.972  0.30 26.41 ? 601  NAD A C5B 1 
HETATM 17600 C  C5B B NAD E  2 .   ? 34.269  -31.877 11.992  0.70 26.92 ? 601  NAD A C5B 1 
HETATM 17601 C  C4B A NAD E  2 .   ? 33.185  -31.645 12.993  0.30 25.40 ? 601  NAD A C4B 1 
HETATM 17602 C  C4B B NAD E  2 .   ? 33.189  -31.665 13.026  0.70 25.29 ? 601  NAD A C4B 1 
HETATM 17603 O  O4B A NAD E  2 .   ? 33.669  -30.866 14.115  0.30 24.24 ? 601  NAD A O4B 1 
HETATM 17604 O  O4B B NAD E  2 .   ? 33.692  -30.829 14.099  0.70 23.26 ? 601  NAD A O4B 1 
HETATM 17605 C  C3B A NAD E  2 .   ? 31.916  -30.923 12.525  0.30 25.03 ? 601  NAD A C3B 1 
HETATM 17606 C  C3B B NAD E  2 .   ? 31.905  -30.972 12.554  0.70 24.84 ? 601  NAD A C3B 1 
HETATM 17607 O  O3B A NAD E  2 .   ? 30.789  -31.485 13.186  0.30 25.51 ? 601  NAD A O3B 1 
HETATM 17608 O  O3B B NAD E  2 .   ? 30.818  -31.562 13.259  0.70 25.62 ? 601  NAD A O3B 1 
HETATM 17609 C  C2B A NAD E  2 .   ? 32.178  -29.473 12.944  0.30 24.50 ? 601  NAD A C2B 1 
HETATM 17610 C  C2B B NAD E  2 .   ? 32.145  -29.504 12.925  0.70 23.93 ? 601  NAD A C2B 1 
HETATM 17611 O  O2B A NAD E  2 .   ? 30.985  -28.746 13.142  0.30 24.37 ? 601  NAD A O2B 1 
HETATM 17612 O  O2B B NAD E  2 .   ? 30.943  -28.791 13.132  0.70 23.74 ? 601  NAD A O2B 1 
HETATM 17613 C  C1B A NAD E  2 .   ? 32.916  -29.682 14.262  0.30 24.03 ? 601  NAD A C1B 1 
HETATM 17614 C  C1B B NAD E  2 .   ? 32.901  -29.667 14.238  0.70 23.13 ? 601  NAD A C1B 1 
HETATM 17615 N  N9A A NAD E  2 .   ? 33.858  -28.635 14.633  0.30 23.35 ? 601  NAD A N9A 1 
HETATM 17616 N  N9A B NAD E  2 .   ? 33.828  -28.606 14.605  0.70 22.14 ? 601  NAD A N9A 1 
HETATM 17617 C  C8A A NAD E  2 .   ? 34.973  -28.254 13.930  0.30 23.29 ? 601  NAD A C8A 1 
HETATM 17618 C  C8A B NAD E  2 .   ? 34.963  -28.248 13.923  0.70 22.30 ? 601  NAD A C8A 1 
HETATM 17619 N  N7A A NAD E  2 .   ? 35.680  -27.334 14.534  0.30 23.04 ? 601  NAD A N7A 1 
HETATM 17620 N  N7A B NAD E  2 .   ? 35.679  -27.344 14.540  0.70 21.90 ? 601  NAD A N7A 1 
HETATM 17621 C  C5A A NAD E  2 .   ? 35.002  -27.109 15.722  0.30 23.14 ? 601  NAD A C5A 1 
HETATM 17622 C  C5A B NAD E  2 .   ? 34.995  -27.119 15.724  0.70 22.12 ? 601  NAD A C5A 1 
HETATM 17623 C  C6A A NAD E  2 .   ? 35.247  -26.249 16.809  0.30 23.10 ? 601  NAD A C6A 1 
HETATM 17624 C  C6A B NAD E  2 .   ? 35.246  -26.274 16.822  0.70 22.07 ? 601  NAD A C6A 1 
HETATM 17625 N  N6A A NAD E  2 .   ? 36.307  -25.445 16.810  0.30 23.39 ? 601  NAD A N6A 1 
HETATM 17626 N  N6A B NAD E  2 .   ? 36.323  -25.490 16.842  0.70 22.63 ? 601  NAD A N6A 1 
HETATM 17627 N  N1A A NAD E  2 .   ? 34.377  -26.258 17.844  0.30 22.86 ? 601  NAD A N1A 1 
HETATM 17628 N  N1A B NAD E  2 .   ? 34.362  -26.271 17.847  0.70 21.70 ? 601  NAD A N1A 1 
HETATM 17629 C  C2A A NAD E  2 .   ? 33.334  -27.095 17.778  0.30 23.02 ? 601  NAD A C2A 1 
HETATM 17630 C  C2A B NAD E  2 .   ? 33.303  -27.088 17.763  0.70 21.97 ? 601  NAD A C2A 1 
HETATM 17631 N  N3A A NAD E  2 .   ? 33.000  -27.951 16.815  0.30 22.92 ? 601  NAD A N3A 1 
HETATM 17632 N  N3A B NAD E  2 .   ? 32.962  -27.929 16.788  0.70 21.68 ? 601  NAD A N3A 1 
HETATM 17633 C  C4A A NAD E  2 .   ? 33.883  -27.913 15.802  0.30 23.13 ? 601  NAD A C4A 1 
HETATM 17634 C  C4A B NAD E  2 .   ? 33.857  -27.901 15.784  0.70 21.97 ? 601  NAD A C4A 1 
HETATM 17635 O  O3  A NAD E  2 .   ? 34.112  -29.153 9.351   0.30 36.29 ? 601  NAD A O3  1 
HETATM 17636 O  O3  B NAD E  2 .   ? 34.172  -29.041 9.613   0.70 48.16 ? 601  NAD A O3  1 
HETATM 17637 P  PN  A NAD E  2 .   ? 32.686  -28.928 8.658   0.30 40.43 ? 601  NAD A PN  1 
HETATM 17638 P  PN  B NAD E  2 .   ? 32.818  -28.662 8.850   0.70 58.26 ? 601  NAD A PN  1 
HETATM 17639 O  O1N A NAD E  2 .   ? 32.075  -27.678 9.203   0.30 40.19 ? 601  NAD A O1N 1 
HETATM 17640 O  O1N B NAD E  2 .   ? 31.966  -27.818 9.739   0.70 58.03 ? 601  NAD A O1N 1 
HETATM 17641 O  O2N A NAD E  2 .   ? 31.914  -30.202 8.748   0.30 39.75 ? 601  NAD A O2N 1 
HETATM 17642 O  O2N B NAD E  2 .   ? 32.225  -29.901 8.262   0.70 57.06 ? 601  NAD A O2N 1 
HETATM 17643 O  O5D A NAD E  2 .   ? 33.147  -28.680 7.140   0.30 39.82 ? 601  NAD A O5D 1 
HETATM 17644 O  O5D B NAD E  2 .   ? 33.437  -27.756 7.685   0.70 58.98 ? 601  NAD A O5D 1 
HETATM 17645 C  C5D A NAD E  2 .   ? 34.557  -28.415 6.908   0.30 39.77 ? 601  NAD A C5D 1 
HETATM 17646 C  C5D B NAD E  2 .   ? 34.340  -28.368 6.729   0.70 60.71 ? 601  NAD A C5D 1 
HETATM 17647 C  C4D A NAD E  2 .   ? 34.714  -27.396 5.805   0.30 39.64 ? 601  NAD A C4D 1 
HETATM 17648 C  C4D B NAD E  2 .   ? 34.443  -27.480 5.514   0.70 60.80 ? 601  NAD A C4D 1 
HETATM 17649 O  O4D A NAD E  2 .   ? 33.900  -26.244 6.083   0.30 39.40 ? 601  NAD A O4D 1 
HETATM 17650 O  O4D B NAD E  2 .   ? 33.116  -27.121 5.067   0.70 58.33 ? 601  NAD A O4D 1 
HETATM 17651 C  C3D A NAD E  2 .   ? 36.117  -26.805 5.632   0.30 39.18 ? 601  NAD A C3D 1 
HETATM 17652 C  C3D B NAD E  2 .   ? 35.175  -26.147 5.732   0.70 62.32 ? 601  NAD A C3D 1 
HETATM 17653 O  O3D A NAD E  2 .   ? 36.919  -27.645 4.814   0.30 39.03 ? 601  NAD A O3D 1 
HETATM 17654 O  O3D B NAD E  2 .   ? 35.824  -25.711 4.544   0.70 65.74 ? 601  NAD A O3D 1 
HETATM 17655 C  C2D A NAD E  2 .   ? 35.849  -25.448 4.965   0.30 39.83 ? 601  NAD A C2D 1 
HETATM 17656 C  C2D B NAD E  2 .   ? 34.031  -25.218 6.157   0.70 61.76 ? 601  NAD A C2D 1 
HETATM 17657 O  O2D A NAD E  2 .   ? 35.935  -25.499 3.549   0.30 39.31 ? 601  NAD A O2D 1 
HETATM 17658 O  O2D B NAD E  2 .   ? 34.327  -23.850 5.917   0.70 63.15 ? 601  NAD A O2D 1 
HETATM 17659 C  C1D A NAD E  2 .   ? 34.400  -25.122 5.359   0.30 39.71 ? 601  NAD A C1D 1 
HETATM 17660 C  C1D B NAD E  2 .   ? 32.914  -25.719 5.233   0.70 59.20 ? 601  NAD A C1D 1 
HETATM 17661 N  N1N A NAD E  2 .   ? 34.280  -23.926 6.216   0.30 39.62 ? 601  NAD A N1N 1 
HETATM 17662 N  N1N B NAD E  2 .   ? 31.539  -25.475 5.744   0.70 55.89 ? 601  NAD A N1N 1 
HETATM 17663 C  C2N A NAD E  2 .   ? 34.949  -22.806 5.873   0.30 39.25 ? 601  NAD A C2N 1 
HETATM 17664 C  C2N B NAD E  2 .   ? 30.811  -26.491 6.261   0.70 54.17 ? 601  NAD A C2N 1 
HETATM 17665 C  C3N A NAD E  2 .   ? 34.827  -21.673 6.669   0.30 38.98 ? 601  NAD A C3N 1 
HETATM 17666 C  C3N B NAD E  2 .   ? 29.525  -26.228 6.734   0.70 53.70 ? 601  NAD A C3N 1 
HETATM 17667 C  C7N A NAD E  2 .   ? 35.580  -20.438 6.284   0.30 38.92 ? 601  NAD A C7N 1 
HETATM 17668 C  C7N B NAD E  2 .   ? 28.680  -27.321 7.316   0.70 53.54 ? 601  NAD A C7N 1 
HETATM 17669 O  O7N A NAD E  2 .   ? 35.425  -19.393 6.935   0.30 38.89 ? 601  NAD A O7N 1 
HETATM 17670 O  O7N B NAD E  2 .   ? 27.555  -27.056 7.771   0.70 52.32 ? 601  NAD A O7N 1 
HETATM 17671 N  N7N A NAD E  2 .   ? 36.423  -20.515 5.264   0.30 38.62 ? 601  NAD A N7N 1 
HETATM 17672 N  N7N B NAD E  2 .   ? 29.163  -28.556 7.320   0.70 52.69 ? 601  NAD A N7N 1 
HETATM 17673 C  C4N A NAD E  2 .   ? 34.039  -21.707 7.811   0.30 39.67 ? 601  NAD A C4N 1 
HETATM 17674 C  C4N B NAD E  2 .   ? 29.008  -24.941 6.660   0.70 52.91 ? 601  NAD A C4N 1 
HETATM 17675 C  C5N A NAD E  2 .   ? 33.364  -22.867 8.141   0.30 39.85 ? 601  NAD A C5N 1 
HETATM 17676 C  C5N B NAD E  2 .   ? 29.772  -23.925 6.123   0.70 52.58 ? 601  NAD A C5N 1 
HETATM 17677 C  C6N A NAD E  2 .   ? 33.489  -23.978 7.337   0.30 39.65 ? 601  NAD A C6N 1 
HETATM 17678 C  C6N B NAD E  2 .   ? 31.039  -24.199 5.664   0.70 53.30 ? 601  NAD A C6N 1 
HETATM 17679 C  C1  . EDO F  3 .   ? 44.865  -19.646 21.451  1.00 56.00 ? 602  EDO A C1  1 
HETATM 17680 O  O1  . EDO F  3 .   ? 46.092  -18.947 21.293  1.00 59.13 ? 602  EDO A O1  1 
HETATM 17681 C  C2  . EDO F  3 .   ? 43.719  -18.926 20.840  1.00 54.81 ? 602  EDO A C2  1 
HETATM 17682 O  O2  . EDO F  3 .   ? 42.438  -19.390 21.251  1.00 52.44 ? 602  EDO A O2  1 
HETATM 17683 C  C1  . EDO G  3 .   ? 48.443  -48.688 39.346  1.00 47.56 ? 603  EDO A C1  1 
HETATM 17684 O  O1  . EDO G  3 .   ? 49.708  -49.270 39.638  1.00 48.97 ? 603  EDO A O1  1 
HETATM 17685 C  C2  . EDO G  3 .   ? 48.330  -48.165 37.957  1.00 46.58 ? 603  EDO A C2  1 
HETATM 17686 O  O2  . EDO G  3 .   ? 47.962  -49.149 37.002  1.00 46.88 ? 603  EDO A O2  1 
HETATM 17687 CL CL  . CL  H  4 .   ? 37.276  -1.810  24.864  1.00 25.27 ? 604  CL  A CL  1 
HETATM 17688 P  PA  . NAD I  2 .   ? 30.493  -40.953 48.511  1.00 26.09 ? 605  NAD A PA  1 
HETATM 17689 O  O1A . NAD I  2 .   ? 29.537  -40.398 49.511  1.00 25.83 ? 605  NAD A O1A 1 
HETATM 17690 O  O2A . NAD I  2 .   ? 29.929  -41.630 47.305  1.00 24.07 ? 605  NAD A O2A 1 
HETATM 17691 O  O5B . NAD I  2 .   ? 31.497  -41.976 49.232  1.00 24.79 ? 605  NAD A O5B 1 
HETATM 17692 C  C5B . NAD I  2 .   ? 32.160  -41.620 50.466  1.00 24.55 ? 605  NAD A C5B 1 
HETATM 17693 C  C4B . NAD I  2 .   ? 32.862  -42.845 50.995  1.00 23.65 ? 605  NAD A C4B 1 
HETATM 17694 O  O4B . NAD I  2 .   ? 33.705  -42.460 52.113  1.00 23.71 ? 605  NAD A O4B 1 
HETATM 17695 C  C3B . NAD I  2 .   ? 31.941  -43.957 51.526  1.00 23.85 ? 605  NAD A C3B 1 
HETATM 17696 O  O3B . NAD I  2 .   ? 32.426  -45.249 51.175  1.00 22.43 ? 605  NAD A O3B 1 
HETATM 17697 C  C2B . NAD I  2 .   ? 31.969  -43.697 53.035  1.00 24.17 ? 605  NAD A C2B 1 
HETATM 17698 O  O2B . NAD I  2 .   ? 31.648  -44.815 53.835  1.00 24.93 ? 605  NAD A O2B 1 
HETATM 17699 C  C1B . NAD I  2 .   ? 33.433  -43.311 53.196  1.00 23.89 ? 605  NAD A C1B 1 
HETATM 17700 N  N9A . NAD I  2 .   ? 33.730  -42.631 54.449  1.00 24.12 ? 605  NAD A N9A 1 
HETATM 17701 C  C8A . NAD I  2 .   ? 33.042  -41.596 55.032  1.00 24.48 ? 605  NAD A C8A 1 
HETATM 17702 N  N7A . NAD I  2 .   ? 33.546  -41.216 56.179  1.00 24.26 ? 605  NAD A N7A 1 
HETATM 17703 C  C5A . NAD I  2 .   ? 34.623  -42.068 56.373  1.00 24.73 ? 605  NAD A C5A 1 
HETATM 17704 C  C6A . NAD I  2 .   ? 35.554  -42.201 57.417  1.00 25.95 ? 605  NAD A C6A 1 
HETATM 17705 N  N6A . NAD I  2 .   ? 35.500  -41.398 58.476  1.00 27.14 ? 605  NAD A N6A 1 
HETATM 17706 N  N1A . NAD I  2 .   ? 36.512  -43.152 57.308  1.00 25.69 ? 605  NAD A N1A 1 
HETATM 17707 C  C2A . NAD I  2 .   ? 36.508  -43.925 56.213  1.00 24.93 ? 605  NAD A C2A 1 
HETATM 17708 N  N3A . NAD I  2 .   ? 35.674  -43.908 55.175  1.00 24.95 ? 605  NAD A N3A 1 
HETATM 17709 C  C4A . NAD I  2 .   ? 34.745  -42.948 55.316  1.00 24.60 ? 605  NAD A C4A 1 
HETATM 17710 O  O3  . NAD I  2 .   ? 31.476  -39.778 48.046  1.00 24.18 ? 605  NAD A O3  1 
HETATM 17711 P  PN  . NAD I  2 .   ? 32.243  -39.589 46.648  1.00 24.80 ? 605  NAD A PN  1 
HETATM 17712 O  O1N . NAD I  2 .   ? 32.984  -40.858 46.360  1.00 22.18 ? 605  NAD A O1N 1 
HETATM 17713 O  O2N . NAD I  2 .   ? 31.292  -39.070 45.622  1.00 23.62 ? 605  NAD A O2N 1 
HETATM 17714 O  O5D . NAD I  2 .   ? 33.273  -38.423 47.017  1.00 25.47 ? 605  NAD A O5D 1 
HETATM 17715 C  C5D . NAD I  2 .   ? 34.307  -38.668 47.996  1.00 26.99 ? 605  NAD A C5D 1 
HETATM 17716 C  C4D . NAD I  2 .   ? 35.206  -37.463 48.048  1.00 28.50 ? 605  NAD A C4D 1 
HETATM 17717 O  O4D . NAD I  2 .   ? 35.922  -37.349 46.794  1.00 29.56 ? 605  NAD A O4D 1 
HETATM 17718 C  C3D . NAD I  2 .   ? 34.480  -36.117 48.254  1.00 29.47 ? 605  NAD A C3D 1 
HETATM 17719 O  O3D . NAD I  2 .   ? 35.249  -35.255 49.082  1.00 29.55 ? 605  NAD A O3D 1 
HETATM 17720 C  C2D . NAD I  2 .   ? 34.362  -35.581 46.825  1.00 30.14 ? 605  NAD A C2D 1 
HETATM 17721 O  O2D . NAD I  2 .   ? 34.224  -34.172 46.738  1.00 31.52 ? 605  NAD A O2D 1 
HETATM 17722 C  C1D . NAD I  2 .   ? 35.732  -36.032 46.314  1.00 30.48 ? 605  NAD A C1D 1 
HETATM 17723 N  N1N . NAD I  2 .   ? 35.914  -36.014 44.845  1.00 33.46 ? 605  NAD A N1N 1 
HETATM 17724 C  C2N . NAD I  2 .   ? 34.863  -35.734 44.046  1.00 33.48 ? 605  NAD A C2N 1 
HETATM 17725 C  C3N . NAD I  2 .   ? 35.062  -35.643 42.673  1.00 32.93 ? 605  NAD A C3N 1 
HETATM 17726 C  C7N . NAD I  2 .   ? 33.880  -35.338 41.806  1.00 34.51 ? 605  NAD A C7N 1 
HETATM 17727 O  O7N . NAD I  2 .   ? 32.731  -35.499 42.250  1.00 35.33 ? 605  NAD A O7N 1 
HETATM 17728 N  N7N . NAD I  2 .   ? 34.107  -34.794 40.617  1.00 34.32 ? 605  NAD A N7N 1 
HETATM 17729 C  C4N . NAD I  2 .   ? 36.318  -35.885 42.134  1.00 33.65 ? 605  NAD A C4N 1 
HETATM 17730 C  C5N . NAD I  2 .   ? 37.380  -36.169 42.974  1.00 33.90 ? 605  NAD A C5N 1 
HETATM 17731 C  C6N . NAD I  2 .   ? 37.172  -36.225 44.334  1.00 34.02 ? 605  NAD A C6N 1 
HETATM 17732 MG MG  . MG  J  5 .   ? 24.006  -22.084 10.124  1.00 34.16 ? 606  MG  A MG  1 
HETATM 17733 O  O1  . TLA K  6 .   ? 21.967  -42.007 10.920  1.00 59.69 ? 607  TLA A O1  1 
HETATM 17734 O  O11 . TLA K  6 .   ? 23.603  -40.610 11.432  1.00 62.30 ? 607  TLA A O11 1 
HETATM 17735 C  C1  . TLA K  6 .   ? 22.433  -41.024 11.526  1.00 60.46 ? 607  TLA A C1  1 
HETATM 17736 C  C2  . TLA K  6 .   ? 21.485  -40.265 12.465  1.00 61.34 ? 607  TLA A C2  1 
HETATM 17737 O  O2  . TLA K  6 .   ? 20.179  -40.205 11.927  1.00 64.50 ? 607  TLA A O2  1 
HETATM 17738 C  C3  . TLA K  6 .   ? 22.015  -38.849 12.742  1.00 57.83 ? 607  TLA A C3  1 
HETATM 17739 O  O3  . TLA K  6 .   ? 22.348  -38.197 11.531  1.00 56.64 ? 607  TLA A O3  1 
HETATM 17740 C  C4  . TLA K  6 .   ? 20.981  -38.040 13.536  1.00 58.78 ? 607  TLA A C4  1 
HETATM 17741 O  O4  . TLA K  6 .   ? 19.886  -38.593 13.788  1.00 64.12 ? 607  TLA A O4  1 
HETATM 17742 O  O41 . TLA K  6 .   ? 21.303  -36.883 13.868  1.00 50.85 ? 607  TLA A O41 1 
HETATM 17743 CL CL  . CL  L  4 .   ? 16.679  -9.720  36.164  1.00 24.32 ? 601  CL  B CL  1 
HETATM 17744 P  PA  A NAD M  2 .   ? 38.378  30.698  39.776  0.50 27.69 ? 602  NAD B PA  1 
HETATM 17745 P  PA  B NAD M  2 .   ? 38.370  30.709  39.778  0.50 27.18 ? 602  NAD B PA  1 
HETATM 17746 O  O1A A NAD M  2 .   ? 39.768  30.186  39.568  0.50 27.77 ? 602  NAD B O1A 1 
HETATM 17747 O  O1A B NAD M  2 .   ? 39.777  30.237  39.592  0.50 27.29 ? 602  NAD B O1A 1 
HETATM 17748 O  O2A A NAD M  2 .   ? 37.624  31.216  38.597  0.50 26.47 ? 602  NAD B O2A 1 
HETATM 17749 O  O2A B NAD M  2 .   ? 37.634  31.245  38.597  0.50 25.93 ? 602  NAD B O2A 1 
HETATM 17750 O  O5B A NAD M  2 .   ? 38.402  31.845  40.893  0.50 27.33 ? 602  NAD B O5B 1 
HETATM 17751 O  O5B B NAD M  2 .   ? 38.332  31.816  40.933  0.50 26.86 ? 602  NAD B O5B 1 
HETATM 17752 C  C5B A NAD M  2 .   ? 39.030  31.649  42.180  0.50 26.10 ? 602  NAD B C5B 1 
HETATM 17753 C  C5B B NAD M  2 .   ? 39.050  31.650  42.176  0.50 25.53 ? 602  NAD B C5B 1 
HETATM 17754 C  C4B A NAD M  2 .   ? 39.084  32.983  42.882  0.50 24.95 ? 602  NAD B C4B 1 
HETATM 17755 C  C4B B NAD M  2 .   ? 39.094  32.985  42.876  0.50 24.34 ? 602  NAD B C4B 1 
HETATM 17756 O  O4B A NAD M  2 .   ? 39.609  32.795  44.222  0.50 24.93 ? 602  NAD B O4B 1 
HETATM 17757 O  O4B B NAD M  2 .   ? 39.612  32.801  44.219  0.50 24.28 ? 602  NAD B O4B 1 
HETATM 17758 C  C3B A NAD M  2 .   ? 39.985  34.042  42.225  0.50 24.62 ? 602  NAD B C3B 1 
HETATM 17759 C  C3B B NAD M  2 .   ? 39.992  34.048  42.223  0.50 23.99 ? 602  NAD B C3B 1 
HETATM 17760 O  O3B A NAD M  2 .   ? 39.413  35.344  42.290  0.50 23.38 ? 602  NAD B O3B 1 
HETATM 17761 O  O3B B NAD M  2 .   ? 39.418  35.349  42.292  0.50 22.74 ? 602  NAD B O3B 1 
HETATM 17762 C  C2B A NAD M  2 .   ? 41.258  33.950  43.068  0.50 24.27 ? 602  NAD B C2B 1 
HETATM 17763 C  C2B B NAD M  2 .   ? 41.264  33.956  43.068  0.50 23.62 ? 602  NAD B C2B 1 
HETATM 17764 O  O2B A NAD M  2 .   ? 42.045  35.120  43.047  0.50 24.24 ? 602  NAD B O2B 1 
HETATM 17765 O  O2B B NAD M  2 .   ? 42.050  35.127  43.051  0.50 23.59 ? 602  NAD B O2B 1 
HETATM 17766 C  C1B A NAD M  2 .   ? 40.638  33.728  44.440  0.50 24.39 ? 602  NAD B C1B 1 
HETATM 17767 C  C1B B NAD M  2 .   ? 40.641  33.733  44.439  0.50 23.73 ? 602  NAD B C1B 1 
HETATM 17768 N  N9A A NAD M  2 .   ? 41.574  33.218  45.432  0.50 24.38 ? 602  NAD B N9A 1 
HETATM 17769 N  N9A B NAD M  2 .   ? 41.576  33.221  45.431  0.50 23.68 ? 602  NAD B N9A 1 
HETATM 17770 C  C8A A NAD M  2 .   ? 42.470  32.187  45.291  0.50 24.88 ? 602  NAD B C8A 1 
HETATM 17771 C  C8A B NAD M  2 .   ? 42.473  32.191  45.290  0.50 24.16 ? 602  NAD B C8A 1 
HETATM 17772 N  N7A A NAD M  2 .   ? 43.203  31.986  46.359  0.50 24.70 ? 602  NAD B N7A 1 
HETATM 17773 N  N7A B NAD M  2 .   ? 43.205  31.989  46.358  0.50 23.97 ? 602  NAD B N7A 1 
HETATM 17774 C  C5A A NAD M  2 .   ? 42.774  32.955  47.254  0.50 24.87 ? 602  NAD B C5A 1 
HETATM 17775 C  C5A B NAD M  2 .   ? 42.776  32.957  47.254  0.50 24.14 ? 602  NAD B C5A 1 
HETATM 17776 C  C6A A NAD M  2 .   ? 43.157  33.280  48.568  0.50 25.36 ? 602  NAD B C6A 1 
HETATM 17777 C  C6A B NAD M  2 .   ? 43.158  33.281  48.568  0.50 24.61 ? 602  NAD B C6A 1 
HETATM 17778 N  N6A A NAD M  2 .   ? 44.111  32.589  49.187  0.50 26.04 ? 602  NAD B N6A 1 
HETATM 17779 N  N6A B NAD M  2 .   ? 44.111  32.589  49.188  0.50 25.26 ? 602  NAD B N6A 1 
HETATM 17780 N  N1A A NAD M  2 .   ? 42.531  34.307  49.186  0.50 25.16 ? 602  NAD B N1A 1 
HETATM 17781 N  N1A B NAD M  2 .   ? 42.530  34.306  49.186  0.50 24.41 ? 602  NAD B N1A 1 
HETATM 17782 C  C2A A NAD M  2 .   ? 41.578  34.959  48.507  0.50 25.42 ? 602  NAD B C2A 1 
HETATM 17783 C  C2A B NAD M  2 .   ? 41.578  34.959  48.507  0.50 24.66 ? 602  NAD B C2A 1 
HETATM 17784 N  N3A A NAD M  2 .   ? 41.128  34.746  47.273  0.50 24.57 ? 602  NAD B N3A 1 
HETATM 17785 N  N3A B NAD M  2 .   ? 41.129  34.747  47.273  0.50 23.84 ? 602  NAD B N3A 1 
HETATM 17786 C  C4A A NAD M  2 .   ? 41.771  33.721  46.693  0.50 24.78 ? 602  NAD B C4A 1 
HETATM 17787 C  C4A B NAD M  2 .   ? 41.773  33.722  46.693  0.50 24.05 ? 602  NAD B C4A 1 
HETATM 17788 O  O3  A NAD M  2 .   ? 37.508  29.558  40.494  0.50 28.18 ? 602  NAD B O3  1 
HETATM 17789 O  O3  B NAD M  2 .   ? 37.511  29.528  40.443  0.50 27.82 ? 602  NAD B O3  1 
HETATM 17790 P  PN  A NAD M  2 .   ? 35.947  29.197  40.370  0.50 28.43 ? 602  NAD B PN  1 
HETATM 17791 P  PN  B NAD M  2 .   ? 35.941  29.196  40.352  0.50 28.17 ? 602  NAD B PN  1 
HETATM 17792 O  O1N A NAD M  2 .   ? 35.160  30.439  40.644  0.50 26.63 ? 602  NAD B O1N 1 
HETATM 17793 O  O1N B NAD M  2 .   ? 35.179  30.448  40.647  0.50 26.35 ? 602  NAD B O1N 1 
HETATM 17794 O  O2N A NAD M  2 .   ? 35.706  28.484  39.079  0.50 29.09 ? 602  NAD B O2N 1 
HETATM 17795 O  O2N B NAD M  2 .   ? 35.663  28.493  39.063  0.50 28.79 ? 602  NAD B O2N 1 
HETATM 17796 O  O5D A NAD M  2 .   ? 35.764  28.161  41.576  0.50 28.94 ? 602  NAD B O5D 1 
HETATM 17797 O  O5D B NAD M  2 .   ? 35.768  28.157  41.557  0.50 28.81 ? 602  NAD B O5D 1 
HETATM 17798 C  C5D A NAD M  2 .   ? 35.948  28.618  42.934  0.50 30.64 ? 602  NAD B C5D 1 
HETATM 17799 C  C5D B NAD M  2 .   ? 35.862  28.623  42.921  0.50 30.66 ? 602  NAD B C5D 1 
HETATM 17800 C  C4D A NAD M  2 .   ? 35.668  27.475  43.877  0.50 31.72 ? 602  NAD B C4D 1 
HETATM 17801 C  C4D B NAD M  2 .   ? 35.621  27.460  43.849  0.50 31.81 ? 602  NAD B C4D 1 
HETATM 17802 O  O4D A NAD M  2 .   ? 34.242  27.247  43.944  0.50 32.99 ? 602  NAD B O4D 1 
HETATM 17803 O  O4D B NAD M  2 .   ? 34.203  27.183  43.917  0.50 33.20 ? 602  NAD B O4D 1 
HETATM 17804 C  C3D A NAD M  2 .   ? 36.292  26.124  43.488  0.50 31.97 ? 602  NAD B C3D 1 
HETATM 17805 C  C3D B NAD M  2 .   ? 36.290  26.136  43.438  0.50 32.10 ? 602  NAD B C3D 1 
HETATM 17806 O  O3D A NAD M  2 .   ? 36.679  25.380  44.636  0.50 31.88 ? 602  NAD B O3D 1 
HETATM 17807 O  O3D B NAD M  2 .   ? 36.719  25.398  44.574  0.50 31.98 ? 602  NAD B O3D 1 
HETATM 17808 C  C2D A NAD M  2 .   ? 35.152  25.424  42.740  0.50 33.27 ? 602  NAD B C2D 1 
HETATM 17809 C  C2D B NAD M  2 .   ? 35.168  25.401  42.696  0.50 33.46 ? 602  NAD B C2D 1 
HETATM 17810 O  O2D A NAD M  2 .   ? 35.236  24.009  42.775  0.50 32.70 ? 602  NAD B O2D 1 
HETATM 17811 O  O2D B NAD M  2 .   ? 35.311  23.990  42.708  0.50 32.76 ? 602  NAD B O2D 1 
HETATM 17812 C  C1D A NAD M  2 .   ? 33.969  25.899  43.585  0.50 34.31 ? 602  NAD B C1D 1 
HETATM 17813 C  C1D B NAD M  2 .   ? 33.984  25.823  43.567  0.50 34.62 ? 602  NAD B C1D 1 
HETATM 17814 N  N1N A NAD M  2 .   ? 32.673  25.849  42.882  0.50 36.66 ? 602  NAD B N1N 1 
HETATM 17815 N  N1N B NAD M  2 .   ? 32.671  25.707  42.902  0.50 37.26 ? 602  NAD B N1N 1 
HETATM 17816 C  C2N A NAD M  2 .   ? 31.584  25.425  43.557  0.50 38.67 ? 602  NAD B C2N 1 
HETATM 17817 C  C2N B NAD M  2 .   ? 32.605  25.168  41.668  0.50 38.76 ? 602  NAD B C2N 1 
HETATM 17818 C  C3N A NAD M  2 .   ? 30.361  25.358  42.900  0.50 40.21 ? 602  NAD B C3N 1 
HETATM 17819 C  C3N B NAD M  2 .   ? 31.362  25.029  41.058  0.50 39.16 ? 602  NAD B C3N 1 
HETATM 17820 C  C7N A NAD M  2 .   ? 29.152  24.892  43.654  0.50 40.40 ? 602  NAD B C7N 1 
HETATM 17821 C  C7N B NAD M  2 .   ? 31.279  24.446  39.682  0.50 38.99 ? 602  NAD B C7N 1 
HETATM 17822 O  O7N A NAD M  2 .   ? 28.068  24.769  43.063  0.50 40.81 ? 602  NAD B O7N 1 
HETATM 17823 O  O7N B NAD M  2 .   ? 30.170  24.176  39.196  0.50 38.55 ? 602  NAD B O7N 1 
HETATM 17824 N  N7N A NAD M  2 .   ? 29.282  24.645  44.951  0.50 40.98 ? 602  NAD B N7N 1 
HETATM 17825 N  N7N B NAD M  2 .   ? 32.409  24.261  39.014  0.50 39.14 ? 602  NAD B N7N 1 
HETATM 17826 C  C4N A NAD M  2 .   ? 30.271  25.736  41.567  0.50 39.60 ? 602  NAD B C4N 1 
HETATM 17827 C  C4N B NAD M  2 .   ? 30.216  25.463  41.709  0.50 40.05 ? 602  NAD B C4N 1 
HETATM 17828 C  C5N A NAD M  2 .   ? 31.400  26.170  40.899  0.50 38.61 ? 602  NAD B C5N 1 
HETATM 17829 C  C5N B NAD M  2 .   ? 30.312  26.010  42.973  0.50 39.93 ? 602  NAD B C5N 1 
HETATM 17830 C  C6N A NAD M  2 .   ? 32.604  26.225  41.565  0.50 37.15 ? 602  NAD B C6N 1 
HETATM 17831 C  C6N B NAD M  2 .   ? 31.547  26.126  43.569  0.50 39.01 ? 602  NAD B C6N 1 
HETATM 17832 O  O1  . TLA N  6 .   ? 15.255  23.789  13.572  1.00 50.92 ? 603  TLA B O1  1 
HETATM 17833 O  O11 . TLA N  6 .   ? 13.199  24.197  14.296  1.00 60.06 ? 603  TLA B O11 1 
HETATM 17834 C  C1  . TLA N  6 .   ? 14.220  24.484  13.643  1.00 56.97 ? 603  TLA B C1  1 
HETATM 17835 C  C2  . TLA N  6 .   ? 14.213  25.809  12.869  1.00 60.28 ? 603  TLA B C2  1 
HETATM 17836 O  O2  . TLA N  6 .   ? 15.244  26.665  13.317  1.00 61.42 ? 603  TLA B O2  1 
HETATM 17837 C  C3  . TLA N  6 .   ? 12.859  26.511  13.012  1.00 63.91 ? 603  TLA B C3  1 
HETATM 17838 O  O3  . TLA N  6 .   ? 12.550  26.702  14.380  1.00 66.07 ? 603  TLA B O3  1 
HETATM 17839 C  C4  . TLA N  6 .   ? 12.866  27.839  12.243  1.00 66.64 ? 603  TLA B C4  1 
HETATM 17840 O  O4  . TLA N  6 .   ? 12.107  27.930  11.259  1.00 72.50 ? 603  TLA B O4  1 
HETATM 17841 O  O41 . TLA N  6 .   ? 13.627  28.738  12.654  1.00 69.68 ? 603  TLA B O41 1 
HETATM 17842 C  C1  . EDO O  3 .   ? 20.518  38.775  48.713  1.00 46.91 ? 604  EDO B C1  1 
HETATM 17843 O  O1  . EDO O  3 .   ? 21.115  39.106  49.957  1.00 47.14 ? 604  EDO B O1  1 
HETATM 17844 C  C2  . EDO O  3 .   ? 19.389  37.812  48.823  1.00 45.60 ? 604  EDO B C2  1 
HETATM 17845 O  O2  . EDO O  3 .   ? 18.512  38.068  49.901  1.00 43.92 ? 604  EDO B O2  1 
HETATM 17846 P  PA  . NAD P  2 .   ? 4.487   17.430  23.376  1.00 33.55 ? 605  NAD B PA  1 
HETATM 17847 O  O1A . NAD P  2 .   ? 3.702   18.688  23.487  1.00 39.14 ? 605  NAD B O1A 1 
HETATM 17848 O  O2A . NAD P  2 .   ? 3.937   16.195  24.004  1.00 39.64 ? 605  NAD B O2A 1 
HETATM 17849 O  O5B . NAD P  2 .   ? 5.977   17.652  23.925  1.00 30.43 ? 605  NAD B O5B 1 
HETATM 17850 C  C5B . NAD P  2 .   ? 6.588   18.959  23.999  1.00 26.37 ? 605  NAD B C5B 1 
HETATM 17851 C  C4B . NAD P  2 .   ? 8.055   18.839  23.658  1.00 25.08 ? 605  NAD B C4B 1 
HETATM 17852 O  O4B . NAD P  2 .   ? 8.749   18.148  24.727  1.00 23.21 ? 605  NAD B O4B 1 
HETATM 17853 C  C3B . NAD P  2 .   ? 8.392   18.045  22.391  1.00 25.15 ? 605  NAD B C3B 1 
HETATM 17854 O  O3B . NAD P  2 .   ? 9.544   18.605  21.765  1.00 25.49 ? 605  NAD B O3B 1 
HETATM 17855 C  C2B . NAD P  2 .   ? 8.656   16.634  22.928  1.00 24.37 ? 605  NAD B C2B 1 
HETATM 17856 O  O2B . NAD P  2 .   ? 9.573   15.943  22.114  1.00 24.61 ? 605  NAD B O2B 1 
HETATM 17857 C  C1B . NAD P  2 .   ? 9.311   16.938  24.268  1.00 23.02 ? 605  NAD B C1B 1 
HETATM 17858 N  N9A . NAD P  2 .   ? 9.116   15.977  25.348  1.00 20.91 ? 605  NAD B N9A 1 
HETATM 17859 C  C8A . NAD P  2 .   ? 7.933   15.626  25.953  1.00 21.40 ? 605  NAD B C8A 1 
HETATM 17860 N  N7A . NAD P  2 .   ? 8.083   14.818  26.975  1.00 20.42 ? 605  NAD B N7A 1 
HETATM 17861 C  C5A . NAD P  2 .   ? 9.460   14.671  27.082  1.00 20.22 ? 605  NAD B C5A 1 
HETATM 17862 C  C6A . NAD P  2 .   ? 10.269  13.951  27.977  1.00 20.28 ? 605  NAD B C6A 1 
HETATM 17863 N  N6A . NAD P  2 .   ? 9.724   13.240  28.961  1.00 19.87 ? 605  NAD B N6A 1 
HETATM 17864 N  N1A . NAD P  2 .   ? 11.613  13.998  27.808  1.00 19.91 ? 605  NAD B N1A 1 
HETATM 17865 C  C2A . NAD P  2 .   ? 12.093  14.734  26.799  1.00 20.01 ? 605  NAD B C2A 1 
HETATM 17866 N  N3A . NAD P  2 .   ? 11.433  15.458  25.894  1.00 19.42 ? 605  NAD B N3A 1 
HETATM 17867 C  C4A . NAD P  2 .   ? 10.107  15.388  26.094  1.00 19.89 ? 605  NAD B C4A 1 
HETATM 17868 O  O3  . NAD P  2 .   ? 4.747   17.126  21.827  1.00 45.18 ? 605  NAD B O3  1 
HETATM 17869 P  PN  . NAD P  2 .   ? 5.066   15.716  21.131  1.00 57.97 ? 605  NAD B PN  1 
HETATM 17870 O  O1N . NAD P  2 .   ? 4.930   14.639  22.159  1.00 53.11 ? 605  NAD B O1N 1 
HETATM 17871 O  O2N . NAD P  2 .   ? 6.376   15.828  20.424  1.00 58.07 ? 605  NAD B O2N 1 
HETATM 17872 O  O5D . NAD P  2 .   ? 3.887   15.582  20.042  1.00 60.94 ? 605  NAD B O5D 1 
HETATM 17873 C  C5D . NAD P  2 .   ? 2.494   15.863  20.355  1.00 61.78 ? 605  NAD B C5D 1 
HETATM 17874 C  C4D . NAD P  2 .   ? 1.663   14.608  20.212  1.00 61.81 ? 605  NAD B C4D 1 
HETATM 17875 O  O4D . NAD P  2 .   ? 2.065   13.873  19.032  1.00 61.85 ? 605  NAD B O4D 1 
HETATM 17876 C  C3D . NAD P  2 .   ? 1.745   13.615  21.385  1.00 62.64 ? 605  NAD B C3D 1 
HETATM 17877 O  O3D . NAD P  2 .   ? 0.457   13.090  21.685  1.00 64.23 ? 605  NAD B O3D 1 
HETATM 17878 C  C2D . NAD P  2 .   ? 2.727   12.546  20.883  1.00 62.38 ? 605  NAD B C2D 1 
HETATM 17879 O  O2D . NAD P  2 .   ? 2.496   11.266  21.452  1.00 60.34 ? 605  NAD B O2D 1 
HETATM 17880 C  C1D . NAD P  2 .   ? 2.407   12.536  19.385  1.00 61.94 ? 605  NAD B C1D 1 
HETATM 17881 N  N1N . NAD P  2 .   ? 3.542   12.088  18.533  1.00 59.90 ? 605  NAD B N1N 1 
HETATM 17882 C  C2N . NAD P  2 .   ? 4.426   12.997  18.066  1.00 58.71 ? 605  NAD B C2N 1 
HETATM 17883 C  C3N . NAD P  2 .   ? 5.501   12.563  17.291  1.00 59.88 ? 605  NAD B C3N 1 
HETATM 17884 C  C7N . NAD P  2 .   ? 6.487   13.559  16.757  1.00 62.37 ? 605  NAD B C7N 1 
HETATM 17885 O  O7N . NAD P  2 .   ? 7.527   13.165  16.205  1.00 65.97 ? 605  NAD B O7N 1 
HETATM 17886 N  N7N . NAD P  2 .   ? 6.194   14.849  16.854  1.00 60.83 ? 605  NAD B N7N 1 
HETATM 17887 C  C4N . NAD P  2 .   ? 5.633   11.214  16.985  1.00 58.70 ? 605  NAD B C4N 1 
HETATM 17888 C  C5N . NAD P  2 .   ? 4.712   10.306  17.471  1.00 58.47 ? 605  NAD B C5N 1 
HETATM 17889 C  C6N . NAD P  2 .   ? 3.666   10.751  18.249  1.00 57.82 ? 605  NAD B C6N 1 
HETATM 17890 MG MG  . MG  Q  5 .   ? 11.354  8.480   15.293  1.00 30.23 ? 606  MG  B MG  1 
HETATM 17891 O  O1  . TLA R  6 .   ? -0.747  17.593  20.103  1.00 59.34 ? 601  TLA C O1  1 
HETATM 17892 O  O11 . TLA R  6 .   ? -1.660  15.615  20.535  1.00 49.76 ? 601  TLA C O11 1 
HETATM 17893 C  C1  . TLA R  6 .   ? -1.517  16.841  20.734  1.00 56.00 ? 601  TLA C C1  1 
HETATM 17894 C  C2  . TLA R  6 .   ? -2.375  17.470  21.840  1.00 58.89 ? 601  TLA C C2  1 
HETATM 17895 O  O2  . TLA R  6 .   ? -3.743  17.455  21.483  1.00 61.36 ? 601  TLA C O2  1 
HETATM 17896 C  C3  . TLA R  6 .   ? -1.926  18.908  22.134  1.00 60.43 ? 601  TLA C C3  1 
HETATM 17897 O  O3  . TLA R  6 .   ? -1.917  19.676  20.947  1.00 61.91 ? 601  TLA C O3  1 
HETATM 17898 C  C4  . TLA R  6 .   ? -2.829  19.547  23.198  1.00 61.70 ? 601  TLA C C4  1 
HETATM 17899 O  O4  . TLA R  6 .   ? -2.617  20.741  23.479  1.00 60.48 ? 601  TLA C O4  1 
HETATM 17900 O  O41 . TLA R  6 .   ? -3.714  18.831  23.708  1.00 68.65 ? 601  TLA C O41 1 
HETATM 17901 C  C1  . EDO S  3 .   ? -19.408 30.918  -9.004  1.00 49.53 ? 602  EDO C C1  1 
HETATM 17902 O  O1  . EDO S  3 .   ? -18.129 31.514  -9.013  1.00 51.14 ? 602  EDO C O1  1 
HETATM 17903 C  C2  . EDO S  3 .   ? -20.456 31.765  -9.622  1.00 49.87 ? 602  EDO C C2  1 
HETATM 17904 O  O2  . EDO S  3 .   ? -20.121 32.219  -10.917 1.00 51.04 ? 602  EDO C O2  1 
HETATM 17905 CL CL  . CL  T  4 .   ? 17.802  -1.873  -10.386 1.00 22.40 ? 603  CL  C CL  1 
HETATM 17906 P  PA  . NAD U  2 .   ? 9.256   21.234  10.784  1.00 36.28 ? 604  NAD C PA  1 
HETATM 17907 O  O1A . NAD U  2 .   ? 8.744   21.873  12.031  1.00 41.21 ? 604  NAD C O1A 1 
HETATM 17908 O  O2A . NAD U  2 .   ? 9.961   22.106  9.807   1.00 40.62 ? 604  NAD C O2A 1 
HETATM 17909 O  O5B . NAD U  2 .   ? 8.061   20.456  10.043  1.00 31.89 ? 604  NAD C O5B 1 
HETATM 17910 C  C5B . NAD U  2 .   ? 6.700   20.920  10.254  1.00 27.77 ? 604  NAD C C5B 1 
HETATM 17911 C  C4B . NAD U  2 .   ? 5.756   19.747  10.356  1.00 25.44 ? 604  NAD C C4B 1 
HETATM 17912 O  O4B . NAD U  2 .   ? 5.655   19.090  9.068   1.00 24.62 ? 604  NAD C O4B 1 
HETATM 17913 C  C3B . NAD U  2 .   ? 6.137   18.633  11.335  1.00 25.43 ? 604  NAD C C3B 1 
HETATM 17914 O  O3B . NAD U  2 .   ? 4.937   18.105  11.890  1.00 24.83 ? 604  NAD C O3B 1 
HETATM 17915 C  C2B . NAD U  2 .   ? 6.897   17.645  10.442  1.00 25.43 ? 604  NAD C C2B 1 
HETATM 17916 O  O2B . NAD U  2 .   ? 6.863   16.330  10.946  1.00 25.74 ? 604  NAD C O2B 1 
HETATM 17917 C  C1B . NAD U  2 .   ? 6.091   17.750  9.153   1.00 24.29 ? 604  NAD C C1B 1 
HETATM 17918 N  N9A . NAD U  2 .   ? 6.780   17.502  7.895   1.00 23.51 ? 604  NAD C N9A 1 
HETATM 17919 C  C8A . NAD U  2 .   ? 7.828   18.211  7.364   1.00 23.68 ? 604  NAD C C8A 1 
HETATM 17920 N  N7A . NAD U  2 .   ? 8.147   17.841  6.148   1.00 22.98 ? 604  NAD C N7A 1 
HETATM 17921 C  C5A . NAD U  2 .   ? 7.225   16.853  5.839   1.00 22.52 ? 604  NAD C C5A 1 
HETATM 17922 C  C6A . NAD U  2 .   ? 7.011   16.062  4.692   1.00 22.49 ? 604  NAD C C6A 1 
HETATM 17923 N  N6A . NAD U  2 .   ? 7.785   16.199  3.621   1.00 22.14 ? 604  NAD C N6A 1 
HETATM 17924 N  N1A . NAD U  2 .   ? 6.004   15.156  4.708   1.00 22.11 ? 604  NAD C N1A 1 
HETATM 17925 C  C2A . NAD U  2 .   ? 5.259   15.072  5.815   1.00 22.53 ? 604  NAD C C2A 1 
HETATM 17926 N  N3A . NAD U  2 .   ? 5.357   15.761  6.949   1.00 22.31 ? 604  NAD C N3A 1 
HETATM 17927 C  C4A . NAD U  2 .   ? 6.365   16.648  6.900   1.00 22.97 ? 604  NAD C C4A 1 
HETATM 17928 O  O3  . NAD U  2 .   ? 10.207  20.021  11.216  1.00 51.05 ? 604  NAD C O3  1 
HETATM 17929 P  PN  . NAD U  2 .   ? 10.072  19.132  12.544  1.00 61.29 ? 604  NAD C PN  1 
HETATM 17930 O  O1N . NAD U  2 .   ? 8.911   19.632  13.338  1.00 57.99 ? 604  NAD C O1N 1 
HETATM 17931 O  O2N . NAD U  2 .   ? 10.104  17.691  12.153  1.00 62.17 ? 604  NAD C O2N 1 
HETATM 17932 O  O5D . NAD U  2 .   ? 11.420  19.483  13.333  1.00 66.61 ? 604  NAD C O5D 1 
HETATM 17933 C  C5D . NAD U  2 .   ? 11.977  20.820  13.370  1.00 66.44 ? 604  NAD C C5D 1 
HETATM 17934 C  C4D . NAD U  2 .   ? 13.481  20.709  13.353  1.00 64.71 ? 604  NAD C C4D 1 
HETATM 17935 O  O4D . NAD U  2 .   ? 13.893  19.662  14.264  1.00 64.09 ? 604  NAD C O4D 1 
HETATM 17936 C  C3D . NAD U  2 .   ? 14.105  20.351  11.994  1.00 63.02 ? 604  NAD C C3D 1 
HETATM 17937 O  O3D . NAD U  2 .   ? 15.358  20.999  11.817  1.00 63.95 ? 604  NAD C O3D 1 
HETATM 17938 C  C2D . NAD U  2 .   ? 14.237  18.824  12.070  1.00 62.71 ? 604  NAD C C2D 1 
HETATM 17939 O  O2D . NAD U  2 .   ? 15.290  18.299  11.277  1.00 61.89 ? 604  NAD C O2D 1 
HETATM 17940 C  C1D . NAD U  2 .   ? 14.579  18.636  13.550  1.00 63.25 ? 604  NAD C C1D 1 
HETATM 17941 N  N1N . NAD U  2 .   ? 14.177  17.308  14.081  1.00 62.70 ? 604  NAD C N1N 1 
HETATM 17942 C  C2N . NAD U  2 .   ? 12.972  17.153  14.672  1.00 62.42 ? 604  NAD C C2N 1 
HETATM 17943 C  C3N . NAD U  2 .   ? 12.608  15.894  15.148  1.00 64.68 ? 604  NAD C C3N 1 
HETATM 17944 C  C7N . NAD U  2 .   ? 11.273  15.711  15.805  1.00 66.53 ? 604  NAD C C7N 1 
HETATM 17945 O  O7N . NAD U  2 .   ? 10.908  14.577  16.155  1.00 69.51 ? 604  NAD C O7N 1 
HETATM 17946 N  N7N . NAD U  2 .   ? 10.513  16.781  15.994  1.00 67.10 ? 604  NAD C N7N 1 
HETATM 17947 C  C4N . NAD U  2 .   ? 13.483  14.821  15.016  1.00 61.25 ? 604  NAD C C4N 1 
HETATM 17948 C  C5N . NAD U  2 .   ? 14.707  15.007  14.404  1.00 60.46 ? 604  NAD C C5N 1 
HETATM 17949 C  C6N . NAD U  2 .   ? 15.049  16.257  13.937  1.00 60.53 ? 604  NAD C C6N 1 
HETATM 17950 P  PA  . NAD V  2 .   ? -24.756 11.136  -6.026  1.00 34.90 ? 605  NAD C PA  1 
HETATM 17951 O  O1A . NAD V  2 .   ? -25.296 9.749   -6.141  1.00 36.02 ? 605  NAD C O1A 1 
HETATM 17952 O  O2A . NAD V  2 .   ? -24.340 11.645  -4.687  1.00 36.47 ? 605  NAD C O2A 1 
HETATM 17953 O  O5B . NAD V  2 .   ? -25.803 12.170  -6.670  1.00 35.27 ? 605  NAD C O5B 1 
HETATM 17954 C  C5B . NAD V  2 .   ? -26.497 11.848  -7.900  1.00 36.16 ? 605  NAD C C5B 1 
HETATM 17955 C  C4B . NAD V  2 .   ? -27.580 12.871  -8.133  1.00 36.28 ? 605  NAD C C4B 1 
HETATM 17956 O  O4B . NAD V  2 .   ? -28.003 12.803  -9.519  1.00 37.98 ? 605  NAD C O4B 1 
HETATM 17957 C  C3B . NAD V  2 .   ? -28.864 12.710  -7.305  1.00 35.82 ? 605  NAD C C3B 1 
HETATM 17958 O  O3B . NAD V  2 .   ? -29.352 13.979  -6.889  1.00 33.59 ? 605  NAD C O3B 1 
HETATM 17959 C  C2B . NAD V  2 .   ? -29.845 12.081  -8.300  1.00 37.56 ? 605  NAD C C2B 1 
HETATM 17960 O  O2B . NAD V  2 .   ? -31.195 12.346  -7.981  1.00 34.72 ? 605  NAD C O2B 1 
HETATM 17961 C  C1B . NAD V  2 .   ? -29.409 12.796  -9.572  1.00 37.80 ? 605  NAD C C1B 1 
HETATM 17962 N  N9A . NAD V  2 .   ? -29.830 12.159  -10.813 1.00 40.94 ? 605  NAD C N9A 1 
HETATM 17963 C  C8A . NAD V  2 .   ? -29.655 10.849  -11.188 1.00 41.29 ? 605  NAD C C8A 1 
HETATM 17964 N  N7A . NAD V  2 .   ? -30.143 10.578  -12.375 1.00 41.13 ? 605  NAD C N7A 1 
HETATM 17965 C  C5A . NAD V  2 .   ? -30.671 11.785  -12.811 1.00 41.42 ? 605  NAD C C5A 1 
HETATM 17966 C  C6A . NAD V  2 .   ? -31.331 12.170  -13.996 1.00 41.70 ? 605  NAD C C6A 1 
HETATM 17967 N  N6A . NAD V  2 .   ? -31.558 11.284  -14.964 1.00 41.85 ? 605  NAD C N6A 1 
HETATM 17968 N  N1A . NAD V  2 .   ? -31.731 13.457  -14.124 1.00 39.58 ? 605  NAD C N1A 1 
HETATM 17969 C  C2A . NAD V  2 .   ? -31.471 14.297  -13.115 1.00 40.22 ? 605  NAD C C2A 1 
HETATM 17970 N  N3A . NAD V  2 .   ? -30.857 14.056  -11.957 1.00 39.91 ? 605  NAD C N3A 1 
HETATM 17971 C  C4A . NAD V  2 .   ? -30.480 12.769  -11.861 1.00 40.77 ? 605  NAD C C4A 1 
HETATM 17972 O  O3  . NAD V  2 .   ? -23.470 11.250  -6.968  1.00 33.99 ? 605  NAD C O3  1 
HETATM 17973 P  PN  . NAD V  2 .   ? -22.211 12.218  -6.793  1.00 35.20 ? 605  NAD C PN  1 
HETATM 17974 O  O1N . NAD V  2 .   ? -22.770 13.590  -6.599  1.00 36.83 ? 605  NAD C O1N 1 
HETATM 17975 O  O2N . NAD V  2 .   ? -21.272 11.672  -5.764  1.00 36.05 ? 605  NAD C O2N 1 
HETATM 17976 O  O5D . NAD V  2 .   ? -21.512 12.089  -8.228  1.00 36.54 ? 605  NAD C O5D 1 
HETATM 17977 C  C5D . NAD V  2 .   ? -22.230 12.450  -9.424  1.00 35.64 ? 605  NAD C C5D 1 
HETATM 17978 C  C4D . NAD V  2 .   ? -21.260 12.425  -10.578 1.00 37.28 ? 605  NAD C C4D 1 
HETATM 17979 O  O4D . NAD V  2 .   ? -20.241 13.429  -10.360 1.00 37.64 ? 605  NAD C O4D 1 
HETATM 17980 C  C3D . NAD V  2 .   ? -20.516 11.090  -10.800 1.00 37.24 ? 605  NAD C C3D 1 
HETATM 17981 O  O3D . NAD V  2 .   ? -20.463 10.736  -12.179 1.00 36.90 ? 605  NAD C O3D 1 
HETATM 17982 C  C2D . NAD V  2 .   ? -19.110 11.357  -10.247 1.00 36.40 ? 605  NAD C C2D 1 
HETATM 17983 O  O2D . NAD V  2 .   ? -18.080 10.627  -10.897 1.00 37.25 ? 605  NAD C O2D 1 
HETATM 17984 C  C1D . NAD V  2 .   ? -18.972 12.840  -10.597 1.00 36.71 ? 605  NAD C C1D 1 
HETATM 17985 N  N1N . NAD V  2 .   ? -17.939 13.559  -9.816  1.00 35.98 ? 605  NAD C N1N 1 
HETATM 17986 C  C2N . NAD V  2 .   ? -16.939 14.184  -10.476 1.00 36.18 ? 605  NAD C C2N 1 
HETATM 17987 C  C3N . NAD V  2 .   ? -15.949 14.848  -9.753  1.00 37.23 ? 605  NAD C C3N 1 
HETATM 17988 C  C7N . NAD V  2 .   ? -14.835 15.545  -10.481 1.00 37.95 ? 605  NAD C C7N 1 
HETATM 17989 O  O7N . NAD V  2 .   ? -13.940 16.127  -9.843  1.00 37.08 ? 605  NAD C O7N 1 
HETATM 17990 N  N7N . NAD V  2 .   ? -14.833 15.508  -11.807 1.00 35.89 ? 605  NAD C N7N 1 
HETATM 17991 C  C4N . NAD V  2 .   ? -15.998 14.848  -8.364  1.00 37.53 ? 605  NAD C C4N 1 
HETATM 17992 C  C5N . NAD V  2 .   ? -17.029 14.195  -7.710  1.00 37.72 ? 605  NAD C C5N 1 
HETATM 17993 C  C6N . NAD V  2 .   ? -18.001 13.548  -8.444  1.00 37.66 ? 605  NAD C C6N 1 
HETATM 17994 O  O1  . TLA W  6 .   ? 38.975  -34.364 3.763   1.00 58.70 ? 601  TLA D O1  1 
HETATM 17995 O  O11 . TLA W  6 .   ? 39.946  -32.442 4.275   1.00 64.52 ? 601  TLA D O11 1 
HETATM 17996 C  C1  . TLA W  6 .   ? 38.953  -33.142 3.998   1.00 58.69 ? 601  TLA D C1  1 
HETATM 17997 C  C2  . TLA W  6 .   ? 37.587  -32.444 3.967   1.00 57.62 ? 601  TLA D C2  1 
HETATM 17998 O  O2  . TLA W  6 .   ? 36.613  -33.237 3.316   1.00 62.55 ? 601  TLA D O2  1 
HETATM 17999 C  C3  . TLA W  6 .   ? 37.700  -31.077 3.284   1.00 54.63 ? 601  TLA D C3  1 
HETATM 18000 O  O3  . TLA W  6 .   ? 38.282  -31.224 2.005   1.00 55.07 ? 601  TLA D O3  1 
HETATM 18001 C  C4  . TLA W  6 .   ? 36.322  -30.412 3.196   1.00 51.84 ? 601  TLA D C4  1 
HETATM 18002 O  O4  . TLA W  6 .   ? 36.285  -29.222 2.820   1.00 46.82 ? 601  TLA D O4  1 
HETATM 18003 O  O41 . TLA W  6 .   ? 35.334  -31.106 3.502   1.00 52.78 ? 601  TLA D O41 1 
HETATM 18004 CL CL  . CL  X  4 .   ? -0.952  -13.905 0.444   1.00 23.77 ? 602  CL  D CL  1 
HETATM 18005 P  PA  . NAD Y  2 .   ? 27.412  -28.139 -31.480 1.00 50.10 ? 603  NAD D PA  1 
HETATM 18006 O  O1A . NAD Y  2 .   ? 27.622  -26.765 -32.026 1.00 55.78 ? 603  NAD D O1A 1 
HETATM 18007 O  O2A . NAD Y  2 .   ? 28.203  -28.580 -30.296 1.00 50.45 ? 603  NAD D O2A 1 
HETATM 18008 O  O5B . NAD Y  2 .   ? 27.580  -29.216 -32.662 1.00 54.46 ? 603  NAD D O5B 1 
HETATM 18009 C  C5B . NAD Y  2 .   ? 26.914  -29.020 -33.938 1.00 54.30 ? 603  NAD D C5B 1 
HETATM 18010 C  C4B . NAD Y  2 .   ? 27.382  -30.073 -34.914 1.00 56.13 ? 603  NAD D C4B 1 
HETATM 18011 O  O4B . NAD Y  2 .   ? 26.458  -30.131 -36.033 1.00 58.22 ? 603  NAD D O4B 1 
HETATM 18012 C  C3B . NAD Y  2 .   ? 28.771  -29.849 -35.533 1.00 55.60 ? 603  NAD D C3B 1 
HETATM 18013 O  O3B . NAD Y  2 .   ? 29.496  -31.068 -35.635 1.00 51.98 ? 603  NAD D O3B 1 
HETATM 18014 C  C2B . NAD Y  2 .   ? 28.443  -29.293 -36.922 1.00 57.67 ? 603  NAD D C2B 1 
HETATM 18015 O  O2B . NAD Y  2 .   ? 29.458  -29.535 -37.872 1.00 55.43 ? 603  NAD D O2B 1 
HETATM 18016 C  C1B . NAD Y  2 .   ? 27.179  -30.081 -37.241 1.00 59.52 ? 603  NAD D C1B 1 
HETATM 18017 N  N9A . NAD Y  2 .   ? 26.338  -29.473 -38.266 1.00 64.35 ? 603  NAD D N9A 1 
HETATM 18018 C  C8A . NAD Y  2 .   ? 25.827  -28.200 -38.265 1.00 65.65 ? 603  NAD D C8A 1 
HETATM 18019 N  N7A . NAD Y  2 .   ? 25.098  -27.930 -39.320 1.00 64.96 ? 603  NAD D N7A 1 
HETATM 18020 C  C5A . NAD Y  2 .   ? 25.129  -29.100 -40.064 1.00 67.13 ? 603  NAD D C5A 1 
HETATM 18021 C  C6A . NAD Y  2 .   ? 24.552  -29.461 -41.297 1.00 66.78 ? 603  NAD D C6A 1 
HETATM 18022 N  N6A . NAD Y  2 .   ? 23.807  -28.592 -41.976 1.00 64.88 ? 603  NAD D N6A 1 
HETATM 18023 N  N1A . NAD Y  2 .   ? 24.772  -30.710 -41.772 1.00 66.17 ? 603  NAD D N1A 1 
HETATM 18024 C  C2A . NAD Y  2 .   ? 25.528  -31.536 -41.035 1.00 66.79 ? 603  NAD D C2A 1 
HETATM 18025 N  N3A . NAD Y  2 .   ? 26.125  -31.311 -39.865 1.00 66.57 ? 603  NAD D N3A 1 
HETATM 18026 C  C4A . NAD Y  2 .   ? 25.889  -30.061 -39.426 1.00 66.58 ? 603  NAD D C4A 1 
HETATM 18027 O  O3  . NAD Y  2 .   ? 25.874  -28.286 -31.071 1.00 48.24 ? 603  NAD D O3  1 
HETATM 18028 P  PN  . NAD Y  2 .   ? 25.330  -29.090 -29.800 1.00 49.02 ? 603  NAD D PN  1 
HETATM 18029 O  O1N . NAD Y  2 .   ? 25.719  -28.370 -28.549 1.00 50.67 ? 603  NAD D O1N 1 
HETATM 18030 O  O2N . NAD Y  2 .   ? 25.789  -30.500 -29.964 1.00 47.42 ? 603  NAD D O2N 1 
HETATM 18031 O  O5D . NAD Y  2 .   ? 23.741  -28.986 -29.992 1.00 47.68 ? 603  NAD D O5D 1 
HETATM 18032 C  C5D . NAD Y  2 .   ? 23.140  -29.502 -31.199 1.00 47.39 ? 603  NAD D C5D 1 
HETATM 18033 C  C4D . NAD Y  2 .   ? 21.651  -29.606 -30.986 1.00 49.12 ? 603  NAD D C4D 1 
HETATM 18034 O  O4D . NAD Y  2 .   ? 21.394  -30.513 -29.892 1.00 49.57 ? 603  NAD D O4D 1 
HETATM 18035 C  C3D . NAD Y  2 .   ? 20.926  -28.288 -30.646 1.00 49.90 ? 603  NAD D C3D 1 
HETATM 18036 O  O3D . NAD Y  2 .   ? 19.819  -28.063 -31.512 1.00 49.73 ? 603  NAD D O3D 1 
HETATM 18037 C  C2D . NAD Y  2 .   ? 20.459  -28.460 -29.192 1.00 50.19 ? 603  NAD D C2D 1 
HETATM 18038 O  O2D . NAD Y  2 .   ? 19.185  -27.893 -28.924 1.00 49.10 ? 603  NAD D O2D 1 
HETATM 18039 C  C1D . NAD Y  2 .   ? 20.345  -29.983 -29.102 1.00 50.53 ? 603  NAD D C1D 1 
HETATM 18040 N  N1N . NAD Y  2 .   ? 20.455  -30.514 -27.724 1.00 51.00 ? 603  NAD D N1N 1 
HETATM 18041 C  C2N . NAD Y  2 .   ? 19.411  -31.196 -27.204 1.00 51.57 ? 603  NAD D C2N 1 
HETATM 18042 C  C3N . NAD Y  2 .   ? 19.497  -31.693 -25.905 1.00 52.99 ? 603  NAD D C3N 1 
HETATM 18043 C  C7N . NAD Y  2 .   ? 18.337  -32.455 -25.332 1.00 54.57 ? 603  NAD D C7N 1 
HETATM 18044 O  O7N . NAD Y  2 .   ? 18.427  -32.971 -24.206 1.00 53.01 ? 603  NAD D O7N 1 
HETATM 18045 N  N7N . NAD Y  2 .   ? 17.229  -32.544 -26.056 1.00 52.52 ? 603  NAD D N7N 1 
HETATM 18046 C  C4N . NAD Y  2 .   ? 20.646  -31.466 -25.158 1.00 51.53 ? 603  NAD D C4N 1 
HETATM 18047 C  C5N . NAD Y  2 .   ? 21.700  -30.761 -25.712 1.00 49.66 ? 603  NAD D C5N 1 
HETATM 18048 C  C6N . NAD Y  2 .   ? 21.598  -30.281 -26.999 1.00 50.70 ? 603  NAD D C6N 1 
HETATM 18049 C  C1  A EDO Z  3 .   ? 20.798  -48.282 -29.840 0.50 30.39 ? 604  EDO D C1  1 
HETATM 18050 C  C1  B EDO Z  3 .   ? 22.272  -48.695 -28.334 0.50 35.83 ? 604  EDO D C1  1 
HETATM 18051 O  O1  A EDO Z  3 .   ? 20.433  -47.056 -30.425 0.50 29.46 ? 604  EDO D O1  1 
HETATM 18052 O  O1  B EDO Z  3 .   ? 23.520  -48.947 -28.944 0.50 35.77 ? 604  EDO D O1  1 
HETATM 18053 C  C2  A EDO Z  3 .   ? 19.818  -48.762 -28.834 0.50 30.38 ? 604  EDO D C2  1 
HETATM 18054 C  C2  B EDO Z  3 .   ? 22.335  -48.677 -26.854 0.50 35.69 ? 604  EDO D C2  1 
HETATM 18055 O  O2  A EDO Z  3 .   ? 18.474  -48.558 -29.216 0.50 30.91 ? 604  EDO D O2  1 
HETATM 18056 O  O2  B EDO Z  3 .   ? 21.155  -49.177 -26.265 0.50 35.98 ? 604  EDO D O2  1 
HETATM 18057 P  PA  . NAD AA 2 .   ? 22.217  -35.367 6.759   1.00 34.13 ? 605  NAD D PA  1 
HETATM 18058 O  O1A . NAD AA 2 .   ? 22.322  -36.855 6.757   1.00 36.74 ? 605  NAD D O1A 1 
HETATM 18059 O  O2A . NAD AA 2 .   ? 20.986  -34.758 7.346   1.00 38.58 ? 605  NAD D O2A 1 
HETATM 18060 O  O5B . NAD AA 2 .   ? 22.400  -34.818 5.257   1.00 29.95 ? 605  NAD D O5B 1 
HETATM 18061 C  C5B . NAD AA 2 .   ? 23.509  -35.279 4.452   1.00 27.17 ? 605  NAD D C5B 1 
HETATM 18062 C  C4B . NAD AA 2 .   ? 24.077  -34.130 3.652   1.00 25.62 ? 605  NAD D C4B 1 
HETATM 18063 O  O4B . NAD AA 2 .   ? 23.062  -33.607 2.761   1.00 24.30 ? 605  NAD D O4B 1 
HETATM 18064 C  C3B . NAD AA 2 .   ? 24.570  -32.915 4.444   1.00 24.99 ? 605  NAD D C3B 1 
HETATM 18065 O  O3B . NAD AA 2 .   ? 25.696  -32.367 3.771   1.00 25.95 ? 605  NAD D O3B 1 
HETATM 18066 C  C2B . NAD AA 2 .   ? 23.372  -31.961 4.422   1.00 24.93 ? 605  NAD D C2B 1 
HETATM 18067 O  O2B . NAD AA 2 .   ? 23.780  -30.611 4.484   1.00 25.25 ? 605  NAD D O2B 1 
HETATM 18068 C  C1B . NAD AA 2 .   ? 22.788  -32.251 3.044   1.00 24.58 ? 605  NAD D C1B 1 
HETATM 18069 N  N9A . NAD AA 2 .   ? 21.347  -32.105 2.880   1.00 23.18 ? 605  NAD D N9A 1 
HETATM 18070 C  C8A . NAD AA 2 .   ? 20.364  -32.851 3.479   1.00 23.66 ? 605  NAD D C8A 1 
HETATM 18071 N  N7A . NAD AA 2 .   ? 19.159  -32.575 3.042   1.00 23.10 ? 605  NAD D N7A 1 
HETATM 18072 C  C5A . NAD AA 2 .   ? 19.365  -31.622 2.058   1.00 22.57 ? 605  NAD D C5A 1 
HETATM 18073 C  C6A . NAD AA 2 .   ? 18.485  -30.925 1.212   1.00 23.08 ? 605  NAD D C6A 1 
HETATM 18074 N  N6A . NAD AA 2 .   ? 17.174  -31.158 1.259   1.00 23.32 ? 605  NAD D N6A 1 
HETATM 18075 N  N1A . NAD AA 2 .   ? 19.004  -30.025 0.344   1.00 22.39 ? 605  NAD D N1A 1 
HETATM 18076 C  C2A . NAD AA 2 .   ? 20.332  -29.849 0.346   1.00 22.53 ? 605  NAD D C2A 1 
HETATM 18077 N  N3A . NAD AA 2 .   ? 21.259  -30.438 1.101   1.00 21.92 ? 605  NAD D N3A 1 
HETATM 18078 C  C4A . NAD AA 2 .   ? 20.709  -31.332 1.939   1.00 22.77 ? 605  NAD D C4A 1 
HETATM 18079 O  O3  . NAD AA 2 .   ? 23.507  -34.753 7.468   1.00 42.78 ? 605  NAD D O3  1 
HETATM 18080 P  PN  . NAD AA 2 .   ? 23.736  -33.487 8.426   1.00 55.39 ? 605  NAD D PN  1 
HETATM 18081 O  O1N . NAD AA 2 .   ? 23.152  -32.267 7.794   1.00 52.74 ? 605  NAD D O1N 1 
HETATM 18082 O  O2N . NAD AA 2 .   ? 25.179  -33.483 8.810   1.00 53.81 ? 605  NAD D O2N 1 
HETATM 18083 O  O5D . NAD AA 2 .   ? 22.825  -33.894 9.681   1.00 57.11 ? 605  NAD D O5D 1 
HETATM 18084 C  C5D . NAD AA 2 .   ? 23.405  -34.399 10.910  1.00 59.09 ? 605  NAD D C5D 1 
HETATM 18085 C  C4D . NAD AA 2 .   ? 22.405  -34.252 12.034  1.00 59.76 ? 605  NAD D C4D 1 
HETATM 18086 O  O4D . NAD AA 2 .   ? 22.696  -33.050 12.785  1.00 61.32 ? 605  NAD D O4D 1 
HETATM 18087 C  C3D . NAD AA 2 .   ? 20.926  -34.132 11.626  1.00 59.25 ? 605  NAD D C3D 1 
HETATM 18088 O  O3D . NAD AA 2 .   ? 20.076  -34.742 12.590  1.00 59.59 ? 605  NAD D O3D 1 
HETATM 18089 C  C2D . NAD AA 2 .   ? 20.715  -32.615 11.551  1.00 59.58 ? 605  NAD D C2D 1 
HETATM 18090 O  O2D . NAD AA 2 .   ? 19.367  -32.225 11.765  1.00 58.76 ? 605  NAD D O2D 1 
HETATM 18091 C  C1D . NAD AA 2 .   ? 21.589  -32.153 12.721  1.00 60.56 ? 605  NAD D C1D 1 
HETATM 18092 N  N1N . NAD AA 2 .   ? 22.108  -30.771 12.582  1.00 60.04 ? 605  NAD D N1N 1 
HETATM 18093 C  C2N . NAD AA 2 .   ? 23.249  -30.556 11.893  1.00 60.20 ? 605  NAD D C2N 1 
HETATM 18094 C  C3N . NAD AA 2 .   ? 23.724  -29.253 11.756  1.00 61.51 ? 605  NAD D C3N 1 
HETATM 18095 C  C7N . NAD AA 2 .   ? 24.993  -29.008 10.996  1.00 61.57 ? 605  NAD D C7N 1 
HETATM 18096 O  O7N . NAD AA 2 .   ? 25.368  -27.845 10.779  1.00 64.88 ? 605  NAD D O7N 1 
HETATM 18097 N  N7N . NAD AA 2 .   ? 25.699  -30.057 10.597  1.00 59.62 ? 605  NAD D N7N 1 
HETATM 18098 C  C4N . NAD AA 2 .   ? 23.034  -28.198 12.344  1.00 59.22 ? 605  NAD D C4N 1 
HETATM 18099 C  C5N . NAD AA 2 .   ? 21.871  -28.447 13.047  1.00 58.35 ? 605  NAD D C5N 1 
HETATM 18100 C  C6N . NAD AA 2 .   ? 21.410  -29.740 13.161  1.00 58.06 ? 605  NAD D C6N 1 
HETATM 18101 O  O   . HOH BA 7 .   ? 43.788  -8.616  44.017  1.00 40.60 ? 701  HOH A O   1 
HETATM 18102 O  O   . HOH BA 7 .   ? 52.074  -46.931 62.455  1.00 31.72 ? 702  HOH A O   1 
HETATM 18103 O  O   . HOH BA 7 .   ? 44.205  -46.745 24.427  1.00 38.73 ? 703  HOH A O   1 
HETATM 18104 O  O   . HOH BA 7 .   ? 59.132  -40.882 57.402  1.00 45.36 ? 704  HOH A O   1 
HETATM 18105 O  O   . HOH BA 7 .   ? 48.722  -50.075 63.302  1.00 47.58 ? 705  HOH A O   1 
HETATM 18106 O  O   . HOH BA 7 .   ? 51.751  -24.412 36.221  1.00 28.82 ? 706  HOH A O   1 
HETATM 18107 O  O   . HOH BA 7 .   ? 45.530  4.086   33.838  1.00 39.88 ? 707  HOH A O   1 
HETATM 18108 O  O   . HOH BA 7 .   ? 48.031  -43.430 65.358  1.00 47.80 ? 708  HOH A O   1 
HETATM 18109 O  O   . HOH BA 7 .   ? 40.749  -49.959 23.159  1.00 35.51 ? 709  HOH A O   1 
HETATM 18110 O  O   . HOH BA 7 .   ? 39.864  -29.684 47.396  1.00 45.97 ? 710  HOH A O   1 
HETATM 18111 O  O   . HOH BA 7 .   ? 33.875  -14.591 19.194  1.00 26.84 ? 711  HOH A O   1 
HETATM 18112 O  O   . HOH BA 7 .   ? 54.522  -49.091 60.181  1.00 37.86 ? 712  HOH A O   1 
HETATM 18113 O  O   . HOH BA 7 .   ? 59.105  -38.608 29.696  1.00 49.27 ? 713  HOH A O   1 
HETATM 18114 O  O   . HOH BA 7 .   ? 17.668  -33.808 49.987  1.00 43.97 ? 714  HOH A O   1 
HETATM 18115 O  O   . HOH BA 7 .   ? 37.830  -53.141 59.675  1.00 31.55 ? 715  HOH A O   1 
HETATM 18116 O  O   . HOH BA 7 .   ? 50.971  -27.853 42.252  1.00 46.50 ? 716  HOH A O   1 
HETATM 18117 O  O   . HOH BA 7 .   ? 47.377  -41.394 8.643   1.00 51.91 ? 717  HOH A O   1 
HETATM 18118 O  O   . HOH BA 7 .   ? 28.053  -45.063 45.467  1.00 48.24 ? 718  HOH A O   1 
HETATM 18119 O  O   . HOH BA 7 .   ? 51.447  -32.040 11.230  1.00 53.50 ? 719  HOH A O   1 
HETATM 18120 O  O   . HOH BA 7 .   ? 31.442  -17.793 25.786  1.00 39.83 ? 720  HOH A O   1 
HETATM 18121 O  O   . HOH BA 7 .   ? 50.350  -39.441 18.038  1.00 60.68 ? 721  HOH A O   1 
HETATM 18122 O  O   . HOH BA 7 .   ? 42.633  -62.063 51.722  1.00 43.88 ? 722  HOH A O   1 
HETATM 18123 O  O   . HOH BA 7 .   ? 26.353  -54.497 40.847  1.00 39.91 ? 723  HOH A O   1 
HETATM 18124 O  O   . HOH BA 7 .   ? 29.740  -18.989 35.659  1.00 31.64 ? 724  HOH A O   1 
HETATM 18125 O  O   . HOH BA 7 .   ? 31.965  -30.837 39.405  1.00 37.17 ? 725  HOH A O   1 
HETATM 18126 O  O   . HOH BA 7 .   ? 36.291  -62.755 55.256  1.00 38.18 ? 726  HOH A O   1 
HETATM 18127 O  O   . HOH BA 7 .   ? 28.675  -41.319 51.716  1.00 39.46 ? 727  HOH A O   1 
HETATM 18128 O  O   . HOH BA 7 .   ? 35.840  -27.223 10.226  1.00 60.77 ? 728  HOH A O   1 
HETATM 18129 O  O   . HOH BA 7 .   ? 31.839  -38.635 53.135  1.00 31.77 ? 729  HOH A O   1 
HETATM 18130 O  O   . HOH BA 7 .   ? 26.680  -20.798 47.189  1.00 46.06 ? 730  HOH A O   1 
HETATM 18131 O  O   . HOH BA 7 .   ? 41.140  -4.067  -0.891  1.00 45.92 ? 731  HOH A O   1 
HETATM 18132 O  O   . HOH BA 7 .   ? 46.317  -30.629 58.510  1.00 36.05 ? 732  HOH A O   1 
HETATM 18133 O  O   . HOH BA 7 .   ? 48.139  -30.838 45.210  1.00 33.80 ? 733  HOH A O   1 
HETATM 18134 O  O   . HOH BA 7 .   ? 58.517  -31.988 42.534  1.00 49.58 ? 734  HOH A O   1 
HETATM 18135 O  O   . HOH BA 7 .   ? 44.128  -13.932 21.208  1.00 31.43 ? 735  HOH A O   1 
HETATM 18136 O  O   . HOH BA 7 .   ? 28.066  -49.302 27.434  1.00 53.93 ? 736  HOH A O   1 
HETATM 18137 O  O   . HOH BA 7 .   ? 63.811  -38.954 34.123  1.00 51.44 ? 737  HOH A O   1 
HETATM 18138 O  O   . HOH BA 7 .   ? 13.157  -39.903 39.847  1.00 34.46 ? 738  HOH A O   1 
HETATM 18139 O  O   . HOH BA 7 .   ? 48.274  -50.368 34.758  1.00 41.91 ? 739  HOH A O   1 
HETATM 18140 O  O   . HOH BA 7 .   ? 29.776  -28.644 10.815  1.00 52.36 ? 740  HOH A O   1 
HETATM 18141 O  O   . HOH BA 7 .   ? 31.294  -27.927 40.100  1.00 33.14 ? 741  HOH A O   1 
HETATM 18142 O  O   . HOH BA 7 .   ? 47.227  -15.867 25.990  1.00 33.92 ? 742  HOH A O   1 
HETATM 18143 O  O   . HOH BA 7 .   ? 24.988  -48.557 29.703  1.00 34.05 ? 743  HOH A O   1 
HETATM 18144 O  O   . HOH BA 7 .   ? 47.455  -23.937 40.565  1.00 50.28 ? 744  HOH A O   1 
HETATM 18145 O  O   . HOH BA 7 .   ? 16.888  -17.998 53.508  1.00 33.13 ? 745  HOH A O   1 
HETATM 18146 O  O   . HOH BA 7 .   ? 23.329  -12.098 49.350  1.00 51.51 ? 746  HOH A O   1 
HETATM 18147 O  O   . HOH BA 7 .   ? 9.784   -22.211 20.830  1.00 27.02 ? 747  HOH A O   1 
HETATM 18148 O  O   . HOH BA 7 .   ? 48.150  -42.535 18.794  1.00 36.55 ? 748  HOH A O   1 
HETATM 18149 O  O   . HOH BA 7 .   ? 8.116   -23.675 26.254  1.00 37.47 ? 749  HOH A O   1 
HETATM 18150 O  O   . HOH BA 7 .   ? 33.925  -32.893 37.266  1.00 33.56 ? 750  HOH A O   1 
HETATM 18151 O  O   . HOH BA 7 .   ? 9.328   -31.713 24.199  1.00 29.05 ? 751  HOH A O   1 
HETATM 18152 O  O   . HOH BA 7 .   ? 6.978   -31.338 40.649  1.00 29.37 ? 752  HOH A O   1 
HETATM 18153 O  O   . HOH BA 7 .   ? 52.012  -30.826 38.168  1.00 34.90 ? 753  HOH A O   1 
HETATM 18154 O  O   . HOH BA 7 .   ? 28.269  -30.858 13.124  1.00 33.96 ? 754  HOH A O   1 
HETATM 18155 O  O   . HOH BA 7 .   ? 27.610  -42.646 46.722  1.00 42.75 ? 755  HOH A O   1 
HETATM 18156 O  O   . HOH BA 7 .   ? 26.850  -18.524 29.008  1.00 38.85 ? 756  HOH A O   1 
HETATM 18157 O  O   . HOH BA 7 .   ? 49.447  -12.542 26.705  1.00 48.97 ? 757  HOH A O   1 
HETATM 18158 O  O   . HOH BA 7 .   ? 48.583  -5.581  33.096  1.00 42.12 ? 758  HOH A O   1 
HETATM 18159 O  O   . HOH BA 7 .   ? 50.376  -58.413 57.207  1.00 45.67 ? 759  HOH A O   1 
HETATM 18160 O  O   . HOH BA 7 .   ? 46.107  -57.635 47.183  1.00 36.74 ? 760  HOH A O   1 
HETATM 18161 O  O   . HOH BA 7 .   ? 55.361  -36.013 44.334  1.00 29.34 ? 761  HOH A O   1 
HETATM 18162 O  O   . HOH BA 7 .   ? 14.140  -24.772 42.553  1.00 22.87 ? 762  HOH A O   1 
HETATM 18163 O  O   . HOH BA 7 .   ? 37.739  -26.405 1.896   1.00 37.71 ? 763  HOH A O   1 
HETATM 18164 O  O   . HOH BA 7 .   ? 8.247   -31.292 45.042  1.00 37.07 ? 764  HOH A O   1 
HETATM 18165 O  O   . HOH BA 7 .   ? 32.600  -35.441 4.177   1.00 29.88 ? 765  HOH A O   1 
HETATM 18166 O  O   . HOH BA 7 .   ? 44.700  -59.514 30.423  1.00 35.84 ? 766  HOH A O   1 
HETATM 18167 O  O   . HOH BA 7 .   ? 33.754  -44.073 60.846  1.00 47.73 ? 767  HOH A O   1 
HETATM 18168 O  O   . HOH BA 7 .   ? 25.533  -15.714 37.997  1.00 58.82 ? 768  HOH A O   1 
HETATM 18169 O  O   . HOH BA 7 .   ? 21.864  -15.397 49.840  1.00 45.51 ? 769  HOH A O   1 
HETATM 18170 O  O   . HOH BA 7 .   ? 23.814  -32.771 47.337  1.00 30.85 ? 770  HOH A O   1 
HETATM 18171 O  O   . HOH BA 7 .   ? 16.089  -39.563 21.036  1.00 34.03 ? 771  HOH A O   1 
HETATM 18172 O  O   . HOH BA 7 .   ? 45.591  -46.595 64.463  1.00 45.35 ? 772  HOH A O   1 
HETATM 18173 O  O   . HOH BA 7 .   ? 58.200  -29.021 37.720  1.00 53.17 ? 773  HOH A O   1 
HETATM 18174 O  O   . HOH BA 7 .   ? 0.750   -28.246 28.989  1.00 44.62 ? 774  HOH A O   1 
HETATM 18175 O  O   . HOH BA 7 .   ? 47.972  -17.928 35.780  1.00 37.81 ? 775  HOH A O   1 
HETATM 18176 O  O   . HOH BA 7 .   ? 22.513  -11.685 31.266  1.00 32.53 ? 776  HOH A O   1 
HETATM 18177 O  O   . HOH BA 7 .   ? 44.150  8.593   18.435  1.00 53.93 ? 777  HOH A O   1 
HETATM 18178 O  O   . HOH BA 7 .   ? 40.413  -47.630 11.446  1.00 55.44 ? 778  HOH A O   1 
HETATM 18179 O  O   . HOH BA 7 .   ? 46.035  -42.740 20.212  1.00 29.40 ? 779  HOH A O   1 
HETATM 18180 O  O   . HOH BA 7 .   ? 43.148  -2.692  16.708  1.00 28.27 ? 780  HOH A O   1 
HETATM 18181 O  O   . HOH BA 7 .   ? 64.607  -42.567 47.747  1.00 45.71 ? 781  HOH A O   1 
HETATM 18182 O  O   . HOH BA 7 .   ? 47.338  -48.634 30.803  1.00 36.38 ? 782  HOH A O   1 
HETATM 18183 O  O   . HOH BA 7 .   ? 54.782  -31.777 30.258  1.00 40.79 ? 783  HOH A O   1 
HETATM 18184 O  O   . HOH BA 7 .   ? 35.782  -50.646 18.331  1.00 56.27 ? 784  HOH A O   1 
HETATM 18185 O  O   . HOH BA 7 .   ? 39.417  -2.348  2.075   1.00 29.52 ? 785  HOH A O   1 
HETATM 18186 O  O   . HOH BA 7 .   ? 30.072  -35.748 18.317  1.00 25.96 ? 786  HOH A O   1 
HETATM 18187 O  O   . HOH BA 7 .   ? 55.892  -39.236 30.169  1.00 36.94 ? 787  HOH A O   1 
HETATM 18188 O  O   . HOH BA 7 .   ? 39.305  -3.723  31.685  1.00 42.77 ? 788  HOH A O   1 
HETATM 18189 O  O   . HOH BA 7 .   ? 35.673  -62.950 45.356  1.00 60.31 ? 789  HOH A O   1 
HETATM 18190 O  O   . HOH BA 7 .   ? 12.108  -22.814 32.069  1.00 26.43 ? 790  HOH A O   1 
HETATM 18191 O  O   . HOH BA 7 .   ? 51.593  -35.445 12.399  1.00 61.57 ? 791  HOH A O   1 
HETATM 18192 O  O   . HOH BA 7 .   ? 35.763  -54.879 58.332  1.00 27.43 ? 792  HOH A O   1 
HETATM 18193 O  O   . HOH BA 7 .   ? 30.474  -33.917 16.253  1.00 24.38 ? 793  HOH A O   1 
HETATM 18194 O  O   . HOH BA 7 .   ? 27.335  -39.084 48.845  1.00 34.90 ? 794  HOH A O   1 
HETATM 18195 O  O   . HOH BA 7 .   ? 42.094  -32.778 47.729  1.00 31.89 ? 795  HOH A O   1 
HETATM 18196 O  O   . HOH BA 7 .   ? 23.737  -52.681 44.495  1.00 45.91 ? 796  HOH A O   1 
HETATM 18197 O  O   . HOH BA 7 .   ? 43.326  -18.338 41.713  1.00 43.38 ? 797  HOH A O   1 
HETATM 18198 O  O   . HOH BA 7 .   ? 26.300  -20.929 40.064  1.00 36.45 ? 798  HOH A O   1 
HETATM 18199 O  O   . HOH BA 7 .   ? 46.770  -46.191 22.228  1.00 58.85 ? 799  HOH A O   1 
HETATM 18200 O  O   . HOH BA 7 .   ? 41.872  -64.922 36.703  1.00 42.50 ? 800  HOH A O   1 
HETATM 18201 O  O   . HOH BA 7 .   ? 33.401  -26.181 11.269  1.00 56.12 ? 801  HOH A O   1 
HETATM 18202 O  O   . HOH BA 7 .   ? 26.576  -16.813 16.865  1.00 46.47 ? 802  HOH A O   1 
HETATM 18203 O  O   . HOH BA 7 .   ? 45.335  -16.386 24.098  1.00 33.63 ? 803  HOH A O   1 
HETATM 18204 O  O   . HOH BA 7 .   ? 10.481  -28.127 16.769  1.00 35.01 ? 804  HOH A O   1 
HETATM 18205 O  O   . HOH BA 7 .   ? 44.027  -25.268 40.186  1.00 48.07 ? 805  HOH A O   1 
HETATM 18206 O  O   . HOH BA 7 .   ? 33.760  -39.786 40.981  1.00 33.27 ? 806  HOH A O   1 
HETATM 18207 O  O   . HOH BA 7 .   ? 19.225  -32.217 47.853  1.00 29.35 ? 807  HOH A O   1 
HETATM 18208 O  O   . HOH BA 7 .   ? 38.619  -54.332 50.352  1.00 22.22 ? 808  HOH A O   1 
HETATM 18209 O  O   . HOH BA 7 .   ? 3.797   -28.554 31.546  1.00 34.42 ? 809  HOH A O   1 
HETATM 18210 O  O   . HOH BA 7 .   ? 3.026   -31.246 25.175  1.00 49.80 ? 810  HOH A O   1 
HETATM 18211 O  O   . HOH BA 7 .   ? 20.482  -35.191 41.059  1.00 21.59 ? 811  HOH A O   1 
HETATM 18212 O  O   . HOH BA 7 .   ? 28.458  -22.262 14.534  1.00 40.45 ? 812  HOH A O   1 
HETATM 18213 O  O   . HOH BA 7 .   ? 8.793   -21.674 49.883  1.00 53.13 ? 813  HOH A O   1 
HETATM 18214 O  O   . HOH BA 7 .   ? 15.366  -39.672 25.563  1.00 29.98 ? 814  HOH A O   1 
HETATM 18215 O  O   . HOH BA 7 .   ? 32.236  -34.431 52.457  1.00 43.96 ? 815  HOH A O   1 
HETATM 18216 O  O   . HOH BA 7 .   ? 29.572  -0.747  6.045   1.00 29.54 ? 816  HOH A O   1 
HETATM 18217 O  O   . HOH BA 7 .   ? 28.048  -48.476 45.096  1.00 32.23 ? 817  HOH A O   1 
HETATM 18218 O  O   . HOH BA 7 .   ? 31.880  -26.470 42.318  1.00 32.37 ? 818  HOH A O   1 
HETATM 18219 O  O   . HOH BA 7 .   ? 45.607  -13.652 38.762  1.00 54.88 ? 819  HOH A O   1 
HETATM 18220 O  O   . HOH BA 7 .   ? 24.891  -51.312 36.713  1.00 31.49 ? 820  HOH A O   1 
HETATM 18221 O  O   . HOH BA 7 .   ? 27.325  -52.704 27.151  1.00 55.01 ? 821  HOH A O   1 
HETATM 18222 O  O   . HOH BA 7 .   ? 59.383  -37.785 46.205  1.00 30.26 ? 822  HOH A O   1 
HETATM 18223 O  O   . HOH BA 7 .   ? 34.106  -5.874  -2.023  1.00 26.57 ? 823  HOH A O   1 
HETATM 18224 O  O   . HOH BA 7 .   ? 31.146  -38.256 7.420   1.00 38.72 ? 824  HOH A O   1 
HETATM 18225 O  O   . HOH BA 7 .   ? 5.766   -27.557 39.018  1.00 42.86 ? 825  HOH A O   1 
HETATM 18226 O  O   . HOH BA 7 .   ? 35.424  -37.344 59.793  1.00 47.87 ? 826  HOH A O   1 
HETATM 18227 O  O   . HOH BA 7 .   ? 33.021  -6.568  33.700  1.00 43.56 ? 827  HOH A O   1 
HETATM 18228 O  O   . HOH BA 7 .   ? 6.626   -25.051 41.794  1.00 50.46 ? 828  HOH A O   1 
HETATM 18229 O  O   . HOH BA 7 .   ? 64.775  -38.972 52.059  1.00 49.77 ? 829  HOH A O   1 
HETATM 18230 O  O   . HOH BA 7 .   ? 16.037  -42.769 26.449  1.00 50.02 ? 830  HOH A O   1 
HETATM 18231 O  O   . HOH BA 7 .   ? 11.915  -32.940 20.368  1.00 37.37 ? 831  HOH A O   1 
HETATM 18232 O  O   . HOH BA 7 .   ? 51.959  -26.376 50.158  1.00 44.22 ? 832  HOH A O   1 
HETATM 18233 O  O   . HOH BA 7 .   ? 45.037  -23.105 39.866  1.00 50.05 ? 833  HOH A O   1 
HETATM 18234 O  O   . HOH BA 7 .   ? 37.060  -59.453 42.422  1.00 35.16 ? 834  HOH A O   1 
HETATM 18235 O  O   . HOH BA 7 .   ? 16.497  -37.576 19.223  1.00 30.42 ? 835  HOH A O   1 
HETATM 18236 O  O   . HOH BA 7 .   ? 43.917  -53.201 64.513  1.00 53.49 ? 836  HOH A O   1 
HETATM 18237 O  O   . HOH BA 7 .   ? 42.806  -44.823 11.735  1.00 37.33 ? 837  HOH A O   1 
HETATM 18238 O  O   . HOH BA 7 .   ? 38.568  -27.835 37.175  1.00 34.45 ? 838  HOH A O   1 
HETATM 18239 O  O   . HOH BA 7 .   ? 9.518   -19.572 41.652  1.00 30.20 ? 839  HOH A O   1 
HETATM 18240 O  O   . HOH BA 7 .   ? 41.195  -6.973  5.909   1.00 49.01 ? 840  HOH A O   1 
HETATM 18241 O  O   . HOH BA 7 .   ? 56.648  -26.147 29.899  1.00 54.38 ? 841  HOH A O   1 
HETATM 18242 O  O   . HOH BA 7 .   ? 51.429  -42.851 29.060  1.00 31.88 ? 842  HOH A O   1 
HETATM 18243 O  O   . HOH BA 7 .   ? 34.574  -42.762 47.406  1.00 18.03 ? 843  HOH A O   1 
HETATM 18244 O  O   . HOH BA 7 .   ? 31.114  -43.360 17.896  1.00 21.47 ? 844  HOH A O   1 
HETATM 18245 O  O   . HOH BA 7 .   ? 25.791  -31.708 17.244  1.00 29.05 ? 845  HOH A O   1 
HETATM 18246 O  O   . HOH BA 7 .   ? 47.175  -35.245 58.238  1.00 34.38 ? 846  HOH A O   1 
HETATM 18247 O  O   . HOH BA 7 .   ? 39.873  -34.516 43.743  1.00 43.30 ? 847  HOH A O   1 
HETATM 18248 O  O   . HOH BA 7 .   ? 15.141  -35.356 41.727  1.00 25.36 ? 848  HOH A O   1 
HETATM 18249 O  O   . HOH BA 7 .   ? 28.151  -41.121 40.558  1.00 30.28 ? 849  HOH A O   1 
HETATM 18250 O  O   . HOH BA 7 .   ? 49.744  -17.971 37.920  1.00 47.44 ? 850  HOH A O   1 
HETATM 18251 O  O   . HOH BA 7 .   ? 39.253  -60.741 42.572  1.00 37.22 ? 851  HOH A O   1 
HETATM 18252 O  O   . HOH BA 7 .   ? 38.093  -44.032 59.315  1.00 31.02 ? 852  HOH A O   1 
HETATM 18253 O  O   . HOH BA 7 .   ? 44.763  -11.590 35.424  1.00 50.84 ? 853  HOH A O   1 
HETATM 18254 O  O   . HOH BA 7 .   ? 41.370  -21.961 22.965  1.00 50.85 ? 854  HOH A O   1 
HETATM 18255 O  O   . HOH BA 7 .   ? 21.772  -43.161 8.478   1.00 52.91 ? 855  HOH A O   1 
HETATM 18256 O  O   . HOH BA 7 .   ? 47.168  3.546   20.033  1.00 38.97 ? 856  HOH A O   1 
HETATM 18257 O  O   . HOH BA 7 .   ? 7.975   -34.903 33.227  1.00 27.61 ? 857  HOH A O   1 
HETATM 18258 O  O   . HOH BA 7 .   ? 49.976  -37.232 34.290  1.00 24.92 ? 858  HOH A O   1 
HETATM 18259 O  O   . HOH BA 7 .   ? 11.723  -41.922 32.078  1.00 43.68 ? 859  HOH A O   1 
HETATM 18260 O  O   . HOH BA 7 .   ? 31.587  -44.498 40.203  1.00 35.71 ? 860  HOH A O   1 
HETATM 18261 O  O   . HOH BA 7 .   ? 36.845  -53.735 37.732  1.00 29.98 ? 861  HOH A O   1 
HETATM 18262 O  O   . HOH BA 7 .   ? 29.026  -45.458 53.583  1.00 43.06 ? 862  HOH A O   1 
HETATM 18263 O  O   . HOH BA 7 .   ? 43.041  -23.180 14.436  1.00 43.19 ? 863  HOH A O   1 
HETATM 18264 O  O   . HOH BA 7 .   ? 14.489  -26.918 15.843  1.00 56.09 ? 864  HOH A O   1 
HETATM 18265 O  O   . HOH BA 7 .   ? 25.409  -47.676 20.861  1.00 37.46 ? 865  HOH A O   1 
HETATM 18266 O  O   . HOH BA 7 .   ? 48.199  -9.823  28.409  1.00 41.78 ? 866  HOH A O   1 
HETATM 18267 O  O   . HOH BA 7 .   ? 8.560   -34.844 30.640  1.00 29.16 ? 867  HOH A O   1 
HETATM 18268 O  O   . HOH BA 7 .   ? 35.493  7.638   17.531  1.00 46.30 ? 868  HOH A O   1 
HETATM 18269 O  O   . HOH BA 7 .   ? 30.836  -47.400 51.665  1.00 31.05 ? 869  HOH A O   1 
HETATM 18270 O  O   . HOH BA 7 .   ? 33.765  -44.673 21.996  1.00 22.95 ? 870  HOH A O   1 
HETATM 18271 O  O   . HOH BA 7 .   ? 12.594  -33.865 47.420  1.00 36.60 ? 871  HOH A O   1 
HETATM 18272 O  O   . HOH BA 7 .   ? 9.891   -38.141 28.512  1.00 26.29 ? 872  HOH A O   1 
HETATM 18273 O  O   . HOH BA 7 .   ? 19.582  -17.709 30.474  1.00 28.16 ? 873  HOH A O   1 
HETATM 18274 O  O   . HOH BA 7 .   ? 38.711  -26.221 48.081  1.00 53.79 ? 874  HOH A O   1 
HETATM 18275 O  O   . HOH BA 7 .   ? 46.616  -42.105 11.553  1.00 52.77 ? 875  HOH A O   1 
HETATM 18276 O  O   . HOH BA 7 .   ? 46.200  -42.659 62.767  1.00 35.46 ? 876  HOH A O   1 
HETATM 18277 O  O   . HOH BA 7 .   ? 32.092  -1.621  21.561  1.00 29.44 ? 877  HOH A O   1 
HETATM 18278 O  O   . HOH BA 7 .   ? 52.869  -31.040 26.749  1.00 38.50 ? 878  HOH A O   1 
HETATM 18279 O  O   . HOH BA 7 .   ? 31.122  -33.385 9.857   1.00 36.83 ? 879  HOH A O   1 
HETATM 18280 O  O   . HOH BA 7 .   ? 23.964  -37.276 21.793  1.00 21.43 ? 880  HOH A O   1 
HETATM 18281 O  O   . HOH BA 7 .   ? 24.710  -16.072 25.257  1.00 57.45 ? 881  HOH A O   1 
HETATM 18282 O  O   . HOH BA 7 .   ? 15.533  -19.580 18.108  1.00 50.41 ? 882  HOH A O   1 
HETATM 18283 O  O   . HOH BA 7 .   ? 37.476  6.620   16.510  1.00 40.37 ? 883  HOH A O   1 
HETATM 18284 O  O   . HOH BA 7 .   ? 41.368  -1.927  9.129   1.00 25.77 ? 884  HOH A O   1 
HETATM 18285 O  O   . HOH BA 7 .   ? 24.754  -40.699 19.612  1.00 19.81 ? 885  HOH A O   1 
HETATM 18286 O  O   . HOH BA 7 .   ? 52.015  -5.585  22.226  1.00 49.10 ? 886  HOH A O   1 
HETATM 18287 O  O   . HOH BA 7 .   ? 64.200  -41.077 54.121  1.00 54.09 ? 887  HOH A O   1 
HETATM 18288 O  O   . HOH BA 7 .   ? 52.110  -24.902 27.054  1.00 35.16 ? 888  HOH A O   1 
HETATM 18289 O  O   . HOH BA 7 .   ? 36.995  -46.680 8.790   1.00 62.12 ? 889  HOH A O   1 
HETATM 18290 O  O   . HOH BA 7 .   ? 16.003  -30.663 53.134  1.00 45.07 ? 890  HOH A O   1 
HETATM 18291 O  O   . HOH BA 7 .   ? 18.652  -47.051 28.212  1.00 48.02 ? 891  HOH A O   1 
HETATM 18292 O  O   . HOH BA 7 .   ? 28.751  -57.743 54.427  1.00 49.01 ? 892  HOH A O   1 
HETATM 18293 O  O   . HOH BA 7 .   ? 15.445  -40.492 32.593  1.00 26.63 ? 893  HOH A O   1 
HETATM 18294 O  O   . HOH BA 7 .   ? 54.968  -24.151 31.987  1.00 55.13 ? 894  HOH A O   1 
HETATM 18295 O  O   . HOH BA 7 .   ? 48.842  -28.297 43.864  1.00 54.84 ? 895  HOH A O   1 
HETATM 18296 O  O   . HOH BA 7 .   ? 22.762  -46.586 27.094  1.00 30.66 ? 896  HOH A O   1 
HETATM 18297 O  O   . HOH BA 7 .   ? 32.958  -25.424 45.623  1.00 45.94 ? 897  HOH A O   1 
HETATM 18298 O  O   . HOH BA 7 .   ? 52.368  -40.390 66.772  1.00 37.46 ? 898  HOH A O   1 
HETATM 18299 O  O   . HOH BA 7 .   ? 35.180  -41.666 39.545  1.00 33.98 ? 899  HOH A O   1 
HETATM 18300 O  O   . HOH BA 7 .   ? 41.316  -53.133 29.403  1.00 29.01 ? 900  HOH A O   1 
HETATM 18301 O  O   . HOH BA 7 .   ? 17.370  -33.737 41.430  1.00 22.59 ? 901  HOH A O   1 
HETATM 18302 O  O   . HOH BA 7 .   ? 40.256  -3.942  29.156  1.00 31.81 ? 902  HOH A O   1 
HETATM 18303 O  O   . HOH BA 7 .   ? 44.353  -10.301 15.261  1.00 39.22 ? 903  HOH A O   1 
HETATM 18304 O  O   . HOH BA 7 .   ? 53.503  -44.920 61.631  1.00 29.03 ? 904  HOH A O   1 
HETATM 18305 O  O   . HOH BA 7 .   ? 37.104  -52.427 35.064  1.00 30.56 ? 905  HOH A O   1 
HETATM 18306 O  O   . HOH BA 7 .   ? 42.734  -42.311 59.973  1.00 26.32 ? 906  HOH A O   1 
HETATM 18307 O  O   . HOH BA 7 .   ? 52.201  -55.649 50.085  1.00 39.66 ? 907  HOH A O   1 
HETATM 18308 O  O   . HOH BA 7 .   ? 20.565  -24.421 53.827  1.00 43.25 ? 908  HOH A O   1 
HETATM 18309 O  O   . HOH BA 7 .   ? 9.951   -12.958 45.956  1.00 39.76 ? 909  HOH A O   1 
HETATM 18310 O  O   . HOH BA 7 .   ? 25.486  -21.852 21.606  1.00 26.68 ? 910  HOH A O   1 
HETATM 18311 O  O   . HOH BA 7 .   ? 29.979  -37.281 9.877   1.00 40.82 ? 911  HOH A O   1 
HETATM 18312 O  O   . HOH BA 7 .   ? 26.660  -24.298 50.083  1.00 62.10 ? 912  HOH A O   1 
HETATM 18313 O  O   . HOH BA 7 .   ? 41.996  -13.632 10.876  1.00 53.13 ? 913  HOH A O   1 
HETATM 18314 O  O   . HOH BA 7 .   ? 61.031  -37.681 41.906  1.00 59.92 ? 914  HOH A O   1 
HETATM 18315 O  O   . HOH BA 7 .   ? 41.678  -59.240 63.711  1.00 60.71 ? 915  HOH A O   1 
HETATM 18316 O  O   . HOH BA 7 .   ? 32.070  -50.682 61.893  1.00 43.19 ? 916  HOH A O   1 
HETATM 18317 O  O   . HOH BA 7 .   ? 40.435  5.933   7.323   1.00 33.78 ? 917  HOH A O   1 
HETATM 18318 O  O   . HOH BA 7 .   ? 28.354  -42.080 25.163  1.00 20.86 ? 918  HOH A O   1 
HETATM 18319 O  O   . HOH BA 7 .   ? 32.036  -18.775 34.941  1.00 30.45 ? 919  HOH A O   1 
HETATM 18320 O  O   . HOH BA 7 .   ? 28.707  -57.947 42.222  1.00 44.80 ? 920  HOH A O   1 
HETATM 18321 O  O   . HOH BA 7 .   ? 23.869  1.455   20.410  1.00 37.94 ? 921  HOH A O   1 
HETATM 18322 O  O   . HOH BA 7 .   ? 50.323  -30.277 59.898  1.00 51.31 ? 922  HOH A O   1 
HETATM 18323 O  O   . HOH BA 7 .   ? 41.031  -4.737  10.059  1.00 28.76 ? 923  HOH A O   1 
HETATM 18324 O  O   . HOH BA 7 .   ? 42.332  -31.837 28.076  1.00 19.53 ? 924  HOH A O   1 
HETATM 18325 O  O   . HOH BA 7 .   ? 59.157  -42.875 29.053  1.00 55.84 ? 925  HOH A O   1 
HETATM 18326 O  O   . HOH BA 7 .   ? 16.738  -28.862 40.067  1.00 26.67 ? 926  HOH A O   1 
HETATM 18327 O  O   . HOH BA 7 .   ? 50.738  -20.342 35.803  1.00 46.40 ? 927  HOH A O   1 
HETATM 18328 O  O   . HOH BA 7 .   ? 42.123  -50.700 21.026  1.00 44.17 ? 928  HOH A O   1 
HETATM 18329 O  O   . HOH BA 7 .   ? 41.079  -11.417 9.621   1.00 40.85 ? 929  HOH A O   1 
HETATM 18330 O  O   . HOH BA 7 .   ? 32.053  -21.376 25.900  1.00 26.42 ? 930  HOH A O   1 
HETATM 18331 O  O   . HOH BA 7 .   ? 53.912  -52.005 58.663  1.00 52.72 ? 931  HOH A O   1 
HETATM 18332 O  O   . HOH BA 7 .   ? 47.952  -23.038 28.480  1.00 24.09 ? 932  HOH A O   1 
HETATM 18333 O  O   . HOH BA 7 .   ? 53.008  -37.588 24.027  1.00 42.42 ? 933  HOH A O   1 
HETATM 18334 O  O   . HOH BA 7 .   ? 57.371  -25.130 52.207  1.00 51.68 ? 934  HOH A O   1 
HETATM 18335 O  O   . HOH BA 7 .   ? 42.710  3.405   33.425  1.00 39.79 ? 935  HOH A O   1 
HETATM 18336 O  O   . HOH BA 7 .   ? 44.186  -43.467 13.733  1.00 27.51 ? 936  HOH A O   1 
HETATM 18337 O  O   . HOH BA 7 .   ? 27.306  -34.073 12.465  1.00 43.82 ? 937  HOH A O   1 
HETATM 18338 O  O   . HOH BA 7 .   ? 28.549  -13.342 32.036  1.00 55.52 ? 938  HOH A O   1 
HETATM 18339 O  O   . HOH BA 7 .   ? 50.197  -4.032  20.788  1.00 40.35 ? 939  HOH A O   1 
HETATM 18340 O  O   . HOH BA 7 .   ? 31.788  -51.426 40.700  1.00 28.14 ? 940  HOH A O   1 
HETATM 18341 O  O   . HOH BA 7 .   ? 27.397  -35.605 38.011  1.00 25.46 ? 941  HOH A O   1 
HETATM 18342 O  O   . HOH BA 7 .   ? 31.236  6.345   10.105  1.00 26.78 ? 942  HOH A O   1 
HETATM 18343 O  O   . HOH BA 7 .   ? 59.909  -46.907 34.585  1.00 55.26 ? 943  HOH A O   1 
HETATM 18344 O  O   . HOH BA 7 .   ? 29.022  -10.125 35.854  1.00 45.69 ? 944  HOH A O   1 
HETATM 18345 O  O   . HOH BA 7 .   ? 54.070  -52.177 49.382  1.00 30.45 ? 945  HOH A O   1 
HETATM 18346 O  O   . HOH BA 7 .   ? 10.378  -40.821 28.892  1.00 42.59 ? 946  HOH A O   1 
HETATM 18347 O  O   . HOH BA 7 .   ? 32.114  -56.819 60.719  1.00 37.24 ? 947  HOH A O   1 
HETATM 18348 O  O   . HOH BA 7 .   ? 38.937  -45.148 10.377  1.00 34.31 ? 948  HOH A O   1 
HETATM 18349 O  O   . HOH BA 7 .   ? 39.356  -6.173  3.738   1.00 46.85 ? 949  HOH A O   1 
HETATM 18350 O  O   . HOH BA 7 .   ? 53.236  -34.525 42.007  1.00 40.88 ? 950  HOH A O   1 
HETATM 18351 O  O   . HOH BA 7 .   ? 33.060  -45.479 11.202  1.00 40.86 ? 951  HOH A O   1 
HETATM 18352 O  O   . HOH BA 7 .   ? 30.352  -42.382 28.331  1.00 18.76 ? 952  HOH A O   1 
HETATM 18353 O  O   . HOH BA 7 .   ? 40.330  -30.096 58.270  1.00 46.17 ? 953  HOH A O   1 
HETATM 18354 O  O   . HOH BA 7 .   ? 46.003  -61.863 30.681  1.00 58.14 ? 954  HOH A O   1 
HETATM 18355 O  O   . HOH BA 7 .   ? 56.549  -28.467 24.649  1.00 56.42 ? 955  HOH A O   1 
HETATM 18356 O  O   . HOH BA 7 .   ? 54.859  -47.129 46.333  1.00 30.45 ? 956  HOH A O   1 
HETATM 18357 O  O   . HOH BA 7 .   ? 33.688  -53.123 58.601  1.00 42.22 ? 957  HOH A O   1 
HETATM 18358 O  O   . HOH BA 7 .   ? 50.144  -28.547 56.514  1.00 38.01 ? 958  HOH A O   1 
HETATM 18359 O  O   . HOH BA 7 .   ? 45.677  -35.679 60.451  1.00 40.36 ? 959  HOH A O   1 
HETATM 18360 O  O   . HOH BA 7 .   ? 43.306  -41.380 5.973   1.00 40.35 ? 960  HOH A O   1 
HETATM 18361 O  O   . HOH BA 7 .   ? 27.167  -45.678 35.128  1.00 29.92 ? 961  HOH A O   1 
HETATM 18362 O  O   . HOH BA 7 .   ? 35.576  -45.993 35.651  1.00 26.06 ? 962  HOH A O   1 
HETATM 18363 O  O   . HOH BA 7 .   ? 29.553  -13.999 24.703  1.00 46.59 ? 963  HOH A O   1 
HETATM 18364 O  O   . HOH BA 7 .   ? 31.433  -34.382 46.965  1.00 43.74 ? 964  HOH A O   1 
HETATM 18365 O  O   . HOH BA 7 .   ? 55.126  -31.228 58.768  1.00 53.70 ? 965  HOH A O   1 
HETATM 18366 O  O   . HOH BA 7 .   ? 46.674  -58.654 51.410  1.00 45.78 ? 966  HOH A O   1 
HETATM 18367 O  O   . HOH BA 7 .   ? 42.217  -47.359 25.698  1.00 35.96 ? 967  HOH A O   1 
HETATM 18368 O  O   . HOH BA 7 .   ? 51.533  -31.775 19.023  1.00 48.36 ? 968  HOH A O   1 
HETATM 18369 O  O   . HOH BA 7 .   ? 30.158  -59.662 52.903  1.00 46.05 ? 969  HOH A O   1 
HETATM 18370 O  O   . HOH BA 7 .   ? 41.819  -49.975 25.692  1.00 48.84 ? 970  HOH A O   1 
HETATM 18371 O  O   . HOH BA 7 .   ? 31.898  -23.602 43.078  1.00 36.86 ? 971  HOH A O   1 
HETATM 18372 O  O   . HOH BA 7 .   ? 28.060  -38.948 13.856  1.00 21.39 ? 972  HOH A O   1 
HETATM 18373 O  O   . HOH BA 7 .   ? 17.143  -13.474 51.544  1.00 44.34 ? 973  HOH A O   1 
HETATM 18374 O  O   . HOH BA 7 .   ? 50.618  -28.280 51.805  1.00 35.20 ? 974  HOH A O   1 
HETATM 18375 O  O   . HOH BA 7 .   ? 38.607  -37.781 54.199  1.00 24.77 ? 975  HOH A O   1 
HETATM 18376 O  O   . HOH BA 7 .   ? 27.403  -49.976 50.724  1.00 43.90 ? 976  HOH A O   1 
HETATM 18377 O  O   . HOH BA 7 .   ? 40.781  -15.501 14.553  1.00 46.79 ? 977  HOH A O   1 
HETATM 18378 O  O   . HOH BA 7 .   ? 36.395  -44.624 12.710  1.00 26.78 ? 978  HOH A O   1 
HETATM 18379 O  O   . HOH BA 7 .   ? 47.723  -60.250 44.451  1.00 54.08 ? 979  HOH A O   1 
HETATM 18380 O  O   . HOH BA 7 .   ? 19.998  1.389   14.855  1.00 58.83 ? 980  HOH A O   1 
HETATM 18381 O  O   . HOH BA 7 .   ? 26.815  -12.442 36.688  1.00 48.05 ? 981  HOH A O   1 
HETATM 18382 O  O   . HOH BA 7 .   ? 7.524   -21.753 42.510  1.00 40.45 ? 982  HOH A O   1 
HETATM 18383 O  O   . HOH BA 7 .   ? 55.361  -32.680 26.545  1.00 52.32 ? 983  HOH A O   1 
HETATM 18384 O  O   . HOH BA 7 .   ? 30.121  -36.572 46.278  1.00 32.36 ? 984  HOH A O   1 
HETATM 18385 O  O   . HOH BA 7 .   ? 22.791  -42.287 18.441  1.00 37.50 ? 985  HOH A O   1 
HETATM 18386 O  O   . HOH BA 7 .   ? 32.135  -39.310 57.737  1.00 43.46 ? 986  HOH A O   1 
HETATM 18387 O  O   . HOH BA 7 .   ? 19.737  -46.478 34.694  1.00 28.91 ? 987  HOH A O   1 
HETATM 18388 O  O   . HOH BA 7 .   ? 60.736  -30.257 31.159  1.00 56.81 ? 988  HOH A O   1 
HETATM 18389 O  O   . HOH BA 7 .   ? 30.570  -38.079 50.797  1.00 45.13 ? 989  HOH A O   1 
HETATM 18390 O  O   . HOH BA 7 .   ? 19.972  -17.877 50.419  1.00 48.26 ? 990  HOH A O   1 
HETATM 18391 O  O   . HOH BA 7 .   ? 19.273  -13.778 44.011  1.00 26.56 ? 991  HOH A O   1 
HETATM 18392 O  O   . HOH BA 7 .   ? 29.828  -63.410 58.703  1.00 57.91 ? 992  HOH A O   1 
HETATM 18393 O  O   . HOH BA 7 .   ? 34.110  -16.323 17.281  1.00 38.92 ? 993  HOH A O   1 
HETATM 18394 O  O   . HOH BA 7 .   ? 53.481  -30.461 22.133  1.00 48.05 ? 994  HOH A O   1 
HETATM 18395 O  O   . HOH BA 7 .   ? 25.555  -38.797 34.150  1.00 22.73 ? 995  HOH A O   1 
HETATM 18396 O  O   . HOH BA 7 .   ? 35.622  -9.777  17.807  1.00 24.57 ? 996  HOH A O   1 
HETATM 18397 O  O   . HOH BA 7 .   ? 38.828  -31.652 39.277  1.00 42.25 ? 997  HOH A O   1 
HETATM 18398 O  O   . HOH BA 7 .   ? 39.127  -35.023 40.365  1.00 44.39 ? 998  HOH A O   1 
HETATM 18399 O  O   . HOH BA 7 .   ? 34.748  -10.467 20.511  1.00 23.43 ? 999  HOH A O   1 
HETATM 18400 O  O   . HOH BA 7 .   ? 27.846  -36.652 40.531  1.00 31.39 ? 1000 HOH A O   1 
HETATM 18401 O  O   . HOH BA 7 .   ? 32.061  -38.345 42.962  1.00 34.97 ? 1001 HOH A O   1 
HETATM 18402 O  O   . HOH BA 7 .   ? 32.794  -48.657 27.943  1.00 28.62 ? 1002 HOH A O   1 
HETATM 18403 O  O   . HOH BA 7 .   ? 63.283  -46.103 40.041  1.00 35.78 ? 1003 HOH A O   1 
HETATM 18404 O  O   . HOH BA 7 .   ? 49.636  -36.398 13.586  1.00 49.12 ? 1004 HOH A O   1 
HETATM 18405 O  O   . HOH BA 7 .   ? 40.212  -60.888 32.375  1.00 42.46 ? 1005 HOH A O   1 
HETATM 18406 O  O   . HOH BA 7 .   ? 38.379  -61.477 46.289  1.00 49.99 ? 1006 HOH A O   1 
HETATM 18407 O  O   . HOH BA 7 .   ? 45.540  -27.190 56.427  1.00 58.94 ? 1007 HOH A O   1 
HETATM 18408 O  O   . HOH BA 7 .   ? 58.632  -43.345 58.305  1.00 38.80 ? 1008 HOH A O   1 
HETATM 18409 O  O   . HOH BA 7 .   ? 36.641  -25.135 12.947  1.00 40.66 ? 1009 HOH A O   1 
HETATM 18410 O  O   . HOH BA 7 .   ? 45.969  -62.722 35.993  1.00 40.39 ? 1010 HOH A O   1 
HETATM 18411 O  O   . HOH BA 7 .   ? 49.679  -29.026 21.057  1.00 49.52 ? 1011 HOH A O   1 
HETATM 18412 O  O   . HOH BA 7 .   ? 4.361   -29.607 23.114  1.00 58.65 ? 1012 HOH A O   1 
HETATM 18413 O  O   . HOH BA 7 .   ? 32.030  -45.901 33.950  1.00 50.34 ? 1013 HOH A O   1 
HETATM 18414 O  O   . HOH BA 7 .   ? 25.254  -37.193 45.862  1.00 28.38 ? 1014 HOH A O   1 
HETATM 18415 O  O   . HOH BA 7 .   ? 21.397  -38.994 43.164  1.00 27.16 ? 1015 HOH A O   1 
HETATM 18416 O  O   . HOH BA 7 .   ? 38.803  -41.694 4.417   1.00 35.81 ? 1016 HOH A O   1 
HETATM 18417 O  O   . HOH BA 7 .   ? 54.503  -43.071 63.668  1.00 39.96 ? 1017 HOH A O   1 
HETATM 18418 O  O   . HOH BA 7 .   ? 52.692  -22.636 27.984  1.00 56.40 ? 1018 HOH A O   1 
HETATM 18419 O  O   . HOH BA 7 .   ? 43.461  2.185   12.872  1.00 22.29 ? 1019 HOH A O   1 
HETATM 18420 O  O   . HOH BA 7 .   ? 57.311  -25.314 37.710  1.00 58.87 ? 1020 HOH A O   1 
HETATM 18421 O  O   . HOH BA 7 .   ? 41.855  -4.071  -8.464  1.00 52.50 ? 1021 HOH A O   1 
HETATM 18422 O  O   . HOH BA 7 .   ? 29.429  -47.343 47.119  1.00 29.16 ? 1022 HOH A O   1 
HETATM 18423 O  O   . HOH BA 7 .   ? 41.294  -25.111 38.378  1.00 58.94 ? 1023 HOH A O   1 
HETATM 18424 O  O   . HOH BA 7 .   ? 44.540  -36.089 4.783   1.00 33.78 ? 1024 HOH A O   1 
HETATM 18425 O  O   . HOH BA 7 .   ? 42.627  -0.796  -5.928  1.00 38.66 ? 1025 HOH A O   1 
HETATM 18426 O  O   . HOH BA 7 .   ? 33.800  -39.241 59.407  1.00 43.73 ? 1026 HOH A O   1 
HETATM 18427 O  O   . HOH BA 7 .   ? 18.319  -36.227 15.370  1.00 46.32 ? 1027 HOH A O   1 
HETATM 18428 O  O   . HOH BA 7 .   ? 5.001   -30.461 36.242  1.00 43.44 ? 1028 HOH A O   1 
HETATM 18429 O  O   . HOH BA 7 .   ? 25.962  0.900   18.253  1.00 48.47 ? 1029 HOH A O   1 
HETATM 18430 O  O   . HOH BA 7 .   ? 48.370  -38.563 12.439  1.00 36.60 ? 1030 HOH A O   1 
HETATM 18431 O  O   . HOH BA 7 .   ? 40.463  0.058   2.504   1.00 35.64 ? 1031 HOH A O   1 
HETATM 18432 O  O   . HOH BA 7 .   ? 24.382  -29.067 15.728  1.00 24.35 ? 1032 HOH A O   1 
HETATM 18433 O  O   . HOH BA 7 .   ? 38.637  -16.849 15.363  1.00 47.03 ? 1033 HOH A O   1 
HETATM 18434 O  O   . HOH BA 7 .   ? 39.000  -19.435 15.066  1.00 39.69 ? 1034 HOH A O   1 
HETATM 18435 O  O   . HOH BA 7 .   ? 49.760  -59.176 48.894  1.00 54.42 ? 1035 HOH A O   1 
HETATM 18436 O  O   . HOH BA 7 .   ? 28.771  -6.816  31.313  1.00 37.76 ? 1036 HOH A O   1 
HETATM 18437 O  O   . HOH BA 7 .   ? 17.703  -9.375  39.275  1.00 34.59 ? 1037 HOH A O   1 
HETATM 18438 O  O   . HOH BA 7 .   ? 38.435  -64.568 48.161  1.00 59.40 ? 1038 HOH A O   1 
HETATM 18439 O  O   . HOH BA 7 .   ? 26.615  -57.078 52.916  1.00 39.25 ? 1039 HOH A O   1 
HETATM 18440 O  O   . HOH BA 7 .   ? 45.682  -25.541 18.214  1.00 46.68 ? 1040 HOH A O   1 
HETATM 18441 O  O   . HOH BA 7 .   ? 17.039  -38.905 43.915  1.00 44.93 ? 1041 HOH A O   1 
HETATM 18442 O  O   . HOH BA 7 .   ? 54.180  -53.871 34.879  1.00 50.34 ? 1042 HOH A O   1 
HETATM 18443 O  O   . HOH BA 7 .   ? 17.462  -20.146 16.594  1.00 49.39 ? 1043 HOH A O   1 
HETATM 18444 O  O   . HOH BA 7 .   ? 17.088  -7.409  34.156  1.00 23.57 ? 1044 HOH A O   1 
HETATM 18445 O  O   . HOH BA 7 .   ? 39.746  -44.054 6.114   1.00 38.96 ? 1045 HOH A O   1 
HETATM 18446 O  O   . HOH BA 7 .   ? 36.985  -10.801 15.598  1.00 29.31 ? 1046 HOH A O   1 
HETATM 18447 O  O   . HOH BA 7 .   ? 44.058  -48.178 19.345  1.00 36.15 ? 1047 HOH A O   1 
HETATM 18448 O  O   . HOH BA 7 .   ? 39.868  -33.068 59.588  1.00 32.44 ? 1048 HOH A O   1 
HETATM 18449 O  O   . HOH BA 7 .   ? 35.754  -66.879 48.285  1.00 55.84 ? 1049 HOH A O   1 
HETATM 18450 O  O   . HOH BA 7 .   ? 23.684  -50.170 44.755  1.00 51.62 ? 1050 HOH A O   1 
HETATM 18451 O  O   . HOH BA 7 .   ? 48.946  -8.337  26.321  1.00 32.46 ? 1051 HOH A O   1 
HETATM 18452 O  O   . HOH BA 7 .   ? 43.200  -13.153 12.961  1.00 43.87 ? 1052 HOH A O   1 
HETATM 18453 O  O   . HOH BA 7 .   ? 25.961  -22.330 16.612  1.00 34.99 ? 1053 HOH A O   1 
HETATM 18454 O  O   . HOH BA 7 .   ? 24.335  -36.013 14.602  1.00 32.35 ? 1054 HOH A O   1 
HETATM 18455 O  O   . HOH BA 7 .   ? 26.651  -4.525  32.085  1.00 35.82 ? 1055 HOH A O   1 
HETATM 18456 O  O   . HOH BA 7 .   ? 33.915  -6.946  1.722   1.00 31.25 ? 1056 HOH A O   1 
HETATM 18457 O  O   . HOH BA 7 .   ? 12.738  -32.941 15.202  1.00 54.01 ? 1057 HOH A O   1 
HETATM 18458 O  O   . HOH BA 7 .   ? 29.998  -20.248 28.840  1.00 40.97 ? 1058 HOH A O   1 
HETATM 18459 O  O   . HOH BA 7 .   ? 35.869  -49.937 23.528  1.00 40.10 ? 1059 HOH A O   1 
HETATM 18460 O  O   . HOH BA 7 .   ? 49.516  -30.463 38.679  1.00 25.30 ? 1060 HOH A O   1 
HETATM 18461 O  O   . HOH BA 7 .   ? 61.443  -35.740 27.920  1.00 53.79 ? 1061 HOH A O   1 
HETATM 18462 O  O   . HOH BA 7 .   ? 33.497  -56.393 38.064  1.00 40.44 ? 1062 HOH A O   1 
HETATM 18463 O  O   . HOH BA 7 .   ? 56.579  -29.092 30.014  1.00 54.95 ? 1063 HOH A O   1 
HETATM 18464 O  O   . HOH BA 7 .   ? 37.228  2.048   -9.658  1.00 34.41 ? 1064 HOH A O   1 
HETATM 18465 O  O   . HOH BA 7 .   ? 45.105  5.682   18.281  1.00 35.13 ? 1065 HOH A O   1 
HETATM 18466 O  O   . HOH BA 7 .   ? 51.490  -48.825 32.155  1.00 47.16 ? 1066 HOH A O   1 
HETATM 18467 O  O   . HOH BA 7 .   ? 17.357  -45.477 36.385  1.00 46.29 ? 1067 HOH A O   1 
HETATM 18468 O  O   . HOH BA 7 .   ? 22.911  -39.970 45.335  1.00 35.73 ? 1068 HOH A O   1 
HETATM 18469 O  O   . HOH BA 7 .   ? 22.450  -9.597  40.626  1.00 45.90 ? 1069 HOH A O   1 
HETATM 18470 O  O   . HOH BA 7 .   ? 24.463  -44.758 17.001  1.00 46.55 ? 1070 HOH A O   1 
HETATM 18471 O  O   . HOH BA 7 .   ? 25.550  -20.844 10.244  1.00 42.40 ? 1071 HOH A O   1 
HETATM 18472 O  O   . HOH BA 7 .   ? 17.005  -28.964 13.186  1.00 49.98 ? 1072 HOH A O   1 
HETATM 18473 O  O   . HOH BA 7 .   ? 48.787  -19.744 33.907  1.00 32.36 ? 1073 HOH A O   1 
HETATM 18474 O  O   . HOH BA 7 .   ? 19.185  -25.321 14.738  1.00 46.76 ? 1074 HOH A O   1 
HETATM 18475 O  O   . HOH BA 7 .   ? 7.470   -28.859 48.073  1.00 36.86 ? 1075 HOH A O   1 
HETATM 18476 O  O   . HOH BA 7 .   ? 23.092  -29.393 50.438  1.00 42.69 ? 1076 HOH A O   1 
HETATM 18477 O  O   . HOH BA 7 .   ? 42.586  1.954   9.882   1.00 26.70 ? 1077 HOH A O   1 
HETATM 18478 O  O   . HOH BA 7 .   ? 22.640  -22.293 50.722  1.00 41.64 ? 1078 HOH A O   1 
HETATM 18479 O  O   . HOH BA 7 .   ? 53.708  -53.112 46.992  1.00 49.16 ? 1079 HOH A O   1 
HETATM 18480 O  O   . HOH BA 7 .   ? 49.645  -35.605 20.638  1.00 34.66 ? 1080 HOH A O   1 
HETATM 18481 O  O   . HOH BA 7 .   ? 38.978  -62.556 35.410  1.00 35.58 ? 1081 HOH A O   1 
HETATM 18482 O  O   . HOH BA 7 .   ? 24.381  -9.258  37.085  1.00 39.75 ? 1082 HOH A O   1 
HETATM 18483 O  O   . HOH BA 7 .   ? 44.667  -7.062  18.186  1.00 24.79 ? 1083 HOH A O   1 
HETATM 18484 O  O   . HOH BA 7 .   ? 31.339  -54.111 59.623  1.00 35.91 ? 1084 HOH A O   1 
HETATM 18485 O  O   . HOH BA 7 .   ? 53.812  -39.329 22.329  1.00 49.43 ? 1085 HOH A O   1 
HETATM 18486 O  O   . HOH BA 7 .   ? 9.123   -24.268 18.757  1.00 55.19 ? 1086 HOH A O   1 
HETATM 18487 O  O   . HOH BA 7 .   ? 23.686  -20.543 11.364  1.00 41.71 ? 1087 HOH A O   1 
HETATM 18488 O  O   . HOH BA 7 .   ? 30.151  -32.194 47.005  1.00 39.93 ? 1088 HOH A O   1 
HETATM 18489 O  O   . HOH BA 7 .   ? 18.452  -27.587 53.866  1.00 40.46 ? 1089 HOH A O   1 
HETATM 18490 O  O   . HOH BA 7 .   ? 52.231  -55.924 47.282  1.00 48.71 ? 1090 HOH A O   1 
HETATM 18491 O  O   . HOH BA 7 .   ? 23.964  -20.099 14.842  1.00 45.07 ? 1091 HOH A O   1 
HETATM 18492 O  O   . HOH BA 7 .   ? 47.747  -3.321  38.931  1.00 49.24 ? 1092 HOH A O   1 
HETATM 18493 O  O   . HOH BA 7 .   ? 59.880  -50.110 48.543  1.00 36.11 ? 1093 HOH A O   1 
HETATM 18494 O  O   . HOH BA 7 .   ? 6.053   -41.568 39.944  1.00 40.93 ? 1094 HOH A O   1 
HETATM 18495 O  O   . HOH BA 7 .   ? 49.689  -24.120 26.569  1.00 26.66 ? 1095 HOH A O   1 
HETATM 18496 O  O   . HOH BA 7 .   ? 29.527  -38.617 41.016  1.00 35.75 ? 1096 HOH A O   1 
HETATM 18497 O  O   . HOH BA 7 .   ? 45.713  -34.058 7.546   1.00 52.64 ? 1097 HOH A O   1 
HETATM 18498 O  O   . HOH BA 7 .   ? 37.102  -23.148 14.678  1.00 52.72 ? 1098 HOH A O   1 
HETATM 18499 O  O   . HOH BA 7 .   ? 24.880  -39.050 31.233  1.00 28.09 ? 1099 HOH A O   1 
HETATM 18500 O  O   . HOH BA 7 .   ? 64.708  -29.559 44.729  1.00 48.70 ? 1100 HOH A O   1 
HETATM 18501 O  O   . HOH BA 7 .   ? 26.830  -14.138 16.540  1.00 48.77 ? 1101 HOH A O   1 
HETATM 18502 O  O   . HOH BA 7 .   ? 16.018  -37.794 41.958  1.00 32.63 ? 1102 HOH A O   1 
HETATM 18503 O  O   . HOH BA 7 .   ? 50.869  -26.697 37.778  1.00 29.25 ? 1103 HOH A O   1 
HETATM 18504 O  O   . HOH BA 7 .   ? 44.340  -44.162 61.232  1.00 28.33 ? 1104 HOH A O   1 
HETATM 18505 O  O   . HOH BA 7 .   ? 37.631  -25.938 52.770  1.00 35.97 ? 1105 HOH A O   1 
HETATM 18506 O  O   . HOH BA 7 .   ? 61.501  -47.534 54.240  1.00 54.04 ? 1106 HOH A O   1 
HETATM 18507 O  O   . HOH BA 7 .   ? 25.388  -13.572 19.017  1.00 60.52 ? 1107 HOH A O   1 
HETATM 18508 O  O   . HOH BA 7 .   ? 50.007  -24.389 50.284  1.00 51.31 ? 1108 HOH A O   1 
HETATM 18509 O  O   . HOH BA 7 .   ? 42.570  0.088   -16.241 1.00 57.93 ? 1109 HOH A O   1 
HETATM 18510 O  O   . HOH BA 7 .   ? 35.842  -48.219 34.249  1.00 38.43 ? 1110 HOH A O   1 
HETATM 18511 O  O   . HOH BA 7 .   ? 27.983  -46.636 32.801  1.00 35.26 ? 1111 HOH A O   1 
HETATM 18512 O  O   . HOH BA 7 .   ? 62.487  -39.503 41.327  1.00 56.78 ? 1112 HOH A O   1 
HETATM 18513 O  O   . HOH BA 7 .   ? 7.432   -28.284 22.804  1.00 37.79 ? 1113 HOH A O   1 
HETATM 18514 O  O   . HOH BA 7 .   ? 48.460  1.579   35.216  1.00 42.31 ? 1114 HOH A O   1 
HETATM 18515 O  O   . HOH BA 7 .   ? 44.003  -9.876  18.056  1.00 27.58 ? 1115 HOH A O   1 
HETATM 18516 O  O   . HOH BA 7 .   ? 50.249  -46.879 41.776  1.00 48.73 ? 1116 HOH A O   1 
HETATM 18517 O  O   . HOH BA 7 .   ? 43.581  -24.261 22.780  1.00 45.07 ? 1117 HOH A O   1 
HETATM 18518 O  O   . HOH BA 7 .   ? 35.466  -49.583 27.152  1.00 32.42 ? 1118 HOH A O   1 
HETATM 18519 O  O   . HOH BA 7 .   ? 14.734  -23.221 16.451  1.00 49.87 ? 1119 HOH A O   1 
HETATM 18520 O  O   . HOH BA 7 .   ? 23.358  -54.192 46.727  1.00 37.47 ? 1120 HOH A O   1 
HETATM 18521 O  O   . HOH BA 7 .   ? 26.285  -18.925 22.241  1.00 51.76 ? 1121 HOH A O   1 
HETATM 18522 O  O   . HOH BA 7 .   ? 2.132   -31.098 29.973  1.00 53.54 ? 1122 HOH A O   1 
HETATM 18523 O  O   . HOH BA 7 .   ? 32.159  -6.598  8.270   1.00 44.48 ? 1123 HOH A O   1 
HETATM 18524 O  O   . HOH BA 7 .   ? 7.226   -31.159 22.872  1.00 57.79 ? 1124 HOH A O   1 
HETATM 18525 O  O   . HOH BA 7 .   ? 47.206  -7.661  19.874  1.00 31.10 ? 1125 HOH A O   1 
HETATM 18526 O  O   . HOH BA 7 .   ? 29.071  -46.244 25.704  1.00 46.61 ? 1126 HOH A O   1 
HETATM 18527 O  O   . HOH BA 7 .   ? 56.252  -40.623 26.801  1.00 51.45 ? 1127 HOH A O   1 
HETATM 18528 O  O   . HOH BA 7 .   ? 24.371  -58.280 45.500  1.00 59.01 ? 1128 HOH A O   1 
HETATM 18529 O  O   . HOH BA 7 .   ? 57.438  -47.703 34.105  1.00 49.49 ? 1129 HOH A O   1 
HETATM 18530 O  O   . HOH BA 7 .   ? 38.393  -54.474 33.184  1.00 50.85 ? 1130 HOH A O   1 
HETATM 18531 O  O   . HOH BA 7 .   ? 47.777  -0.442  20.259  1.00 35.08 ? 1131 HOH A O   1 
HETATM 18532 O  O   . HOH BA 7 .   ? 47.774  -57.602 63.775  1.00 53.95 ? 1132 HOH A O   1 
HETATM 18533 O  O   . HOH BA 7 .   ? 26.999  -18.130 39.332  1.00 59.17 ? 1133 HOH A O   1 
HETATM 18534 O  O   . HOH BA 7 .   ? 26.973  -8.791  14.781  1.00 55.05 ? 1134 HOH A O   1 
HETATM 18535 O  O   . HOH BA 7 .   ? 29.425  -54.973 40.030  1.00 39.90 ? 1135 HOH A O   1 
HETATM 18536 O  O   . HOH BA 7 .   ? 37.322  -41.848 61.103  1.00 40.15 ? 1136 HOH A O   1 
HETATM 18537 O  O   . HOH BA 7 .   ? 32.106  -18.297 18.512  1.00 51.10 ? 1137 HOH A O   1 
HETATM 18538 O  O   . HOH BA 7 .   ? 36.186  -16.432 15.162  1.00 51.50 ? 1138 HOH A O   1 
HETATM 18539 O  O   . HOH BA 7 .   ? 8.544   -35.523 44.820  1.00 34.18 ? 1139 HOH A O   1 
HETATM 18540 O  O   . HOH BA 7 .   ? 36.697  -32.861 40.369  1.00 34.04 ? 1140 HOH A O   1 
HETATM 18541 O  O   . HOH BA 7 .   ? 64.055  -41.695 41.465  1.00 51.29 ? 1141 HOH A O   1 
HETATM 18542 O  O   . HOH BA 7 .   ? 56.347  -49.290 46.218  1.00 38.01 ? 1142 HOH A O   1 
HETATM 18543 O  O   . HOH BA 7 .   ? 63.171  -41.029 26.803  1.00 59.86 ? 1143 HOH A O   1 
HETATM 18544 O  O   . HOH BA 7 .   ? 63.073  -51.153 36.580  1.00 39.60 ? 1144 HOH A O   1 
HETATM 18545 O  O   . HOH BA 7 .   ? 51.531  -35.591 23.020  1.00 42.72 ? 1145 HOH A O   1 
HETATM 18546 O  O   . HOH BA 7 .   ? 22.549  -19.933 49.421  1.00 54.27 ? 1146 HOH A O   1 
HETATM 18547 O  O   . HOH BA 7 .   ? 40.724  -44.204 60.078  1.00 31.05 ? 1147 HOH A O   1 
HETATM 18548 O  O   . HOH BA 7 .   ? 47.198  -13.231 20.562  1.00 52.72 ? 1148 HOH A O   1 
HETATM 18549 O  O   . HOH BA 7 .   ? 43.383  -8.227  13.771  1.00 56.83 ? 1149 HOH A O   1 
HETATM 18550 O  O   . HOH BA 7 .   ? 45.098  -64.983 36.563  1.00 55.39 ? 1150 HOH A O   1 
HETATM 18551 O  O   . HOH BA 7 .   ? 54.017  -42.742 29.268  1.00 49.10 ? 1151 HOH A O   1 
HETATM 18552 O  O   . HOH BA 7 .   ? 45.039  -42.395 7.752   1.00 45.41 ? 1152 HOH A O   1 
HETATM 18553 O  O   . HOH BA 7 .   ? 53.544  -29.800 29.210  1.00 39.85 ? 1153 HOH A O   1 
HETATM 18554 O  O   . HOH BA 7 .   ? 42.354  -37.657 62.272  1.00 55.07 ? 1154 HOH A O   1 
HETATM 18555 O  O   . HOH BA 7 .   ? 39.950  -62.849 48.147  1.00 48.07 ? 1155 HOH A O   1 
HETATM 18556 O  O   . HOH BA 7 .   ? 44.463  -44.868 8.263   1.00 50.51 ? 1156 HOH A O   1 
HETATM 18557 O  O   . HOH BA 7 .   ? 23.739  -47.239 46.985  1.00 50.67 ? 1157 HOH A O   1 
HETATM 18558 O  O   . HOH BA 7 .   ? 46.136  -10.926 19.550  1.00 39.57 ? 1158 HOH A O   1 
HETATM 18559 O  O   . HOH BA 7 .   ? 38.800  -25.219 37.896  1.00 48.56 ? 1159 HOH A O   1 
HETATM 18560 O  O   . HOH BA 7 .   ? 33.546  -49.635 18.382  1.00 55.67 ? 1160 HOH A O   1 
HETATM 18561 O  O   . HOH BA 7 .   ? 50.151  -13.886 28.917  1.00 60.22 ? 1161 HOH A O   1 
HETATM 18562 O  O   . HOH BA 7 .   ? 25.480  -41.332 47.390  1.00 47.67 ? 1162 HOH A O   1 
HETATM 18563 O  O   . HOH BA 7 .   ? 29.917  -20.207 25.672  1.00 47.04 ? 1163 HOH A O   1 
HETATM 18564 O  O   . HOH BA 7 .   ? 45.217  -45.163 18.537  1.00 42.36 ? 1164 HOH A O   1 
HETATM 18565 O  O   . HOH BA 7 .   ? 49.150  -19.728 24.777  1.00 54.94 ? 1165 HOH A O   1 
HETATM 18566 O  O   . HOH BA 7 .   ? 53.378  -54.627 30.864  1.00 56.48 ? 1166 HOH A O   1 
HETATM 18567 O  O   . HOH BA 7 .   ? 6.479   -33.651 23.891  1.00 57.07 ? 1167 HOH A O   1 
HETATM 18568 O  O   . HOH BA 7 .   ? 11.305  -33.331 22.863  1.00 42.04 ? 1168 HOH A O   1 
HETATM 18569 O  O   . HOH BA 7 .   ? 20.921  -40.729 47.007  1.00 50.55 ? 1169 HOH A O   1 
HETATM 18570 O  O   . HOH BA 7 .   ? 10.871  -37.873 25.724  1.00 42.42 ? 1170 HOH A O   1 
HETATM 18571 O  O   . HOH BA 7 .   ? 50.640  -30.270 13.016  1.00 41.19 ? 1171 HOH A O   1 
HETATM 18572 O  O   . HOH BA 7 .   ? 35.781  -2.000  33.455  1.00 56.95 ? 1172 HOH A O   1 
HETATM 18573 O  O   . HOH BA 7 .   ? 7.906   -24.727 49.456  1.00 51.51 ? 1173 HOH A O   1 
HETATM 18574 O  O   . HOH BA 7 .   ? 16.136  -15.298 53.306  1.00 42.83 ? 1174 HOH A O   1 
HETATM 18575 O  O   . HOH BA 7 .   ? 6.796   -35.130 26.114  1.00 55.69 ? 1175 HOH A O   1 
HETATM 18576 O  O   . HOH BA 7 .   ? 22.099  2.767   14.230  1.00 50.35 ? 1176 HOH A O   1 
HETATM 18577 O  O   . HOH BA 7 .   ? 27.671  -36.759 47.316  1.00 30.60 ? 1177 HOH A O   1 
HETATM 18578 O  O   . HOH BA 7 .   ? 47.929  1.823   21.766  1.00 40.69 ? 1178 HOH A O   1 
HETATM 18579 O  O   . HOH BA 7 .   ? 31.852  -46.852 21.898  1.00 32.13 ? 1179 HOH A O   1 
HETATM 18580 O  O   . HOH BA 7 .   ? 14.988  -20.436 15.736  1.00 57.53 ? 1180 HOH A O   1 
HETATM 18581 O  O   . HOH BA 7 .   ? 27.078  -45.791 16.500  1.00 50.92 ? 1181 HOH A O   1 
HETATM 18582 O  O   . HOH BA 7 .   ? 43.885  -32.245 7.845   1.00 46.97 ? 1182 HOH A O   1 
HETATM 18583 O  O   . HOH BA 7 .   ? 24.805  -9.411  39.804  1.00 47.26 ? 1183 HOH A O   1 
HETATM 18584 O  O   . HOH BA 7 .   ? 15.872  -39.667 46.375  1.00 45.66 ? 1184 HOH A O   1 
HETATM 18585 O  O   . HOH BA 7 .   ? 50.180  -1.354  20.334  1.00 37.00 ? 1185 HOH A O   1 
HETATM 18586 O  O   . HOH BA 7 .   ? 5.264   -30.263 38.879  1.00 50.96 ? 1186 HOH A O   1 
HETATM 18587 O  O   . HOH BA 7 .   ? 26.156  -47.860 17.800  1.00 53.12 ? 1187 HOH A O   1 
HETATM 18588 O  O   . HOH BA 7 .   ? 12.795  -40.169 24.878  1.00 44.44 ? 1188 HOH A O   1 
HETATM 18589 O  O   . HOH BA 7 .   ? 41.207  -4.337  2.164   1.00 49.30 ? 1189 HOH A O   1 
HETATM 18590 O  O   . HOH BA 7 .   ? 32.973  -46.997 36.591  1.00 43.93 ? 1190 HOH A O   1 
HETATM 18591 O  O   . HOH BA 7 .   ? 27.597  -47.143 48.752  1.00 47.52 ? 1191 HOH A O   1 
HETATM 18592 O  O   . HOH BA 7 .   ? 30.107  -52.334 61.189  1.00 53.38 ? 1192 HOH A O   1 
HETATM 18593 O  O   . HOH BA 7 .   ? 43.687  -60.867 65.161  1.00 58.16 ? 1193 HOH A O   1 
HETATM 18594 O  O   . HOH BA 7 .   ? 49.981  -47.861 30.549  1.00 36.46 ? 1194 HOH A O   1 
HETATM 18595 O  O   . HOH BA 7 .   ? 30.180  -47.170 23.865  1.00 35.93 ? 1195 HOH A O   1 
HETATM 18596 O  O   . HOH BA 7 .   ? 46.753  -60.039 48.899  1.00 62.14 ? 1196 HOH A O   1 
HETATM 18597 O  O   . HOH BA 7 .   ? 45.109  -48.360 22.143  1.00 52.55 ? 1197 HOH A O   1 
HETATM 18598 O  O   . HOH BA 7 .   ? 49.935  -10.615 30.208  1.00 52.10 ? 1198 HOH A O   1 
HETATM 18599 O  O   . HOH BA 7 .   ? 8.078   -18.835 19.821  1.00 48.26 ? 1199 HOH A O   1 
HETATM 18600 O  O   . HOH BA 7 .   ? 50.924  -34.269 18.178  1.00 58.71 ? 1200 HOH A O   1 
HETATM 18601 O  O   . HOH BA 7 .   ? 45.298  -1.456  15.572  1.00 36.60 ? 1201 HOH A O   1 
HETATM 18602 O  O   . HOH BA 7 .   ? 49.310  -13.625 22.000  1.00 50.91 ? 1202 HOH A O   1 
HETATM 18603 O  O   . HOH BA 7 .   ? 38.093  -25.722 9.512   1.00 61.75 ? 1203 HOH A O   1 
HETATM 18604 O  O   . HOH BA 7 .   ? 43.753  -5.448  16.252  1.00 50.28 ? 1204 HOH A O   1 
HETATM 18605 O  O   . HOH BA 7 .   ? 26.119  -32.603 48.621  1.00 38.55 ? 1205 HOH A O   1 
HETATM 18606 O  O   . HOH BA 7 .   ? 20.960  -48.416 25.427  1.00 44.94 ? 1206 HOH A O   1 
HETATM 18607 O  O   . HOH BA 7 .   ? 49.526  -27.856 39.739  1.00 35.86 ? 1207 HOH A O   1 
HETATM 18608 O  O   . HOH BA 7 .   ? 49.367  -22.505 24.269  1.00 52.00 ? 1208 HOH A O   1 
HETATM 18609 O  O   . HOH BA 7 .   ? 57.061  -61.207 44.045  1.00 55.15 ? 1209 HOH A O   1 
HETATM 18610 O  O   . HOH BA 7 .   ? 35.253  -30.969 39.067  1.00 53.46 ? 1210 HOH A O   1 
HETATM 18611 O  O   . HOH BA 7 .   ? 54.687  -21.240 32.154  1.00 57.85 ? 1211 HOH A O   1 
HETATM 18612 O  O   . HOH BA 7 .   ? 31.970  -6.089  4.332   1.00 56.82 ? 1212 HOH A O   1 
HETATM 18613 O  O   . HOH BA 7 .   ? 7.503   -37.300 28.485  1.00 46.68 ? 1213 HOH A O   1 
HETATM 18614 O  O   . HOH BA 7 .   ? 32.188  -20.864 10.325  1.00 52.94 ? 1214 HOH A O   1 
HETATM 18615 O  O   . HOH BA 7 .   ? 48.413  -58.075 45.978  1.00 56.99 ? 1215 HOH A O   1 
HETATM 18616 O  O   . HOH BA 7 .   ? 30.716  -52.973 39.080  1.00 39.86 ? 1216 HOH A O   1 
HETATM 18617 O  O   . HOH BA 7 .   ? 26.646  -38.431 51.991  1.00 53.38 ? 1217 HOH A O   1 
HETATM 18618 O  O   . HOH BA 7 .   ? 29.983  -40.542 53.776  1.00 39.15 ? 1218 HOH A O   1 
HETATM 18619 O  O   . HOH BA 7 .   ? 23.266  -35.394 46.628  1.00 37.24 ? 1219 HOH A O   1 
HETATM 18620 O  O   . HOH BA 7 .   ? 40.378  -51.201 27.702  1.00 40.12 ? 1220 HOH A O   1 
HETATM 18621 O  O   . HOH BA 7 .   ? 55.976  -54.003 50.261  1.00 38.88 ? 1221 HOH A O   1 
HETATM 18622 O  O   . HOH BA 7 .   ? 50.693  -3.609  32.410  1.00 55.20 ? 1222 HOH A O   1 
HETATM 18623 O  O   . HOH BA 7 .   ? 38.603  -56.887 29.726  1.00 52.28 ? 1223 HOH A O   1 
HETATM 18624 O  O   . HOH BA 7 .   ? 51.481  -8.017  26.186  1.00 39.34 ? 1224 HOH A O   1 
HETATM 18625 O  O   . HOH BA 7 .   ? 38.979  -54.279 30.518  1.00 35.84 ? 1225 HOH A O   1 
HETATM 18626 O  O   . HOH BA 7 .   ? 33.367  -1.174  -15.747 1.00 36.92 ? 1226 HOH A O   1 
HETATM 18627 O  O   . HOH BA 7 .   ? 40.264  -44.423 62.852  1.00 47.41 ? 1227 HOH A O   1 
HETATM 18628 O  O   . HOH BA 7 .   ? 27.169  -50.782 35.698  1.00 42.62 ? 1228 HOH A O   1 
HETATM 18629 O  O   . HOH BA 7 .   ? 41.943  -40.475 62.111  1.00 35.10 ? 1229 HOH A O   1 
HETATM 18630 O  O   . HOH BA 7 .   ? 61.190  -57.884 45.772  1.00 37.81 ? 1230 HOH A O   1 
HETATM 18631 O  O   . HOH BA 7 .   ? 48.085  -25.867 18.283  1.00 48.33 ? 1231 HOH A O   1 
HETATM 18632 O  O   . HOH BA 7 .   ? 37.634  -51.794 27.006  1.00 48.07 ? 1232 HOH A O   1 
HETATM 18633 O  O   . HOH BA 7 .   ? 49.708  -27.972 12.298  1.00 44.30 ? 1233 HOH A O   1 
HETATM 18634 O  O   . HOH BA 7 .   ? 37.264  -24.091 48.421  1.00 48.45 ? 1234 HOH A O   1 
HETATM 18635 O  O   . HOH BA 7 .   ? 48.637  -26.700 20.652  1.00 43.21 ? 1235 HOH A O   1 
HETATM 18636 O  O   . HOH BA 7 .   ? 29.862  -45.801 17.449  1.00 34.80 ? 1236 HOH A O   1 
HETATM 18637 O  O   . HOH BA 7 .   ? 44.571  -36.914 63.843  1.00 54.87 ? 1237 HOH A O   1 
HETATM 18638 O  O   . HOH BA 7 .   ? 7.131   -31.018 49.616  1.00 51.00 ? 1238 HOH A O   1 
HETATM 18639 O  O   . HOH BA 7 .   ? 49.467  -8.133  33.113  1.00 55.09 ? 1239 HOH A O   1 
HETATM 18640 O  O   . HOH BA 7 .   ? 51.530  -45.229 30.557  1.00 49.67 ? 1240 HOH A O   1 
HETATM 18641 O  O   . HOH BA 7 .   ? 8.537   -33.299 49.436  1.00 49.97 ? 1241 HOH A O   1 
HETATM 18642 O  O   . HOH BA 7 .   ? 36.529  -53.295 29.684  1.00 40.61 ? 1242 HOH A O   1 
HETATM 18643 O  O   . HOH BA 7 .   ? 40.086  -57.331 27.717  1.00 50.73 ? 1243 HOH A O   1 
HETATM 18644 O  O   . HOH BA 7 .   ? 39.550  -41.132 62.890  1.00 47.83 ? 1244 HOH A O   1 
HETATM 18645 O  O   . HOH CA 7 .   ? 32.978  10.692  11.005  1.00 37.03 ? 701  HOH B O   1 
HETATM 18646 O  O   . HOH CA 7 .   ? 38.645  36.021  67.133  1.00 38.95 ? 702  HOH B O   1 
HETATM 18647 O  O   . HOH CA 7 .   ? 29.467  15.654  58.046  1.00 51.56 ? 703  HOH B O   1 
HETATM 18648 O  O   . HOH CA 7 .   ? 10.449  21.644  51.344  1.00 31.30 ? 704  HOH B O   1 
HETATM 18649 O  O   . HOH CA 7 .   ? 12.137  37.101  36.569  1.00 47.26 ? 705  HOH B O   1 
HETATM 18650 O  O   . HOH CA 7 .   ? 28.285  48.367  50.290  1.00 29.98 ? 706  HOH B O   1 
HETATM 18651 O  O   . HOH CA 7 .   ? 30.433  20.151  37.180  1.00 38.00 ? 707  HOH B O   1 
HETATM 18652 O  O   . HOH CA 7 .   ? 9.476   2.431   38.688  1.00 28.08 ? 708  HOH B O   1 
HETATM 18653 O  O   . HOH CA 7 .   ? 30.670  14.906  8.014   1.00 32.78 ? 709  HOH B O   1 
HETATM 18654 O  O   . HOH CA 7 .   ? 11.475  4.799   43.801  1.00 40.07 ? 710  HOH B O   1 
HETATM 18655 O  O   . HOH CA 7 .   ? 22.037  26.946  58.774  1.00 32.25 ? 711  HOH B O   1 
HETATM 18656 O  O   . HOH CA 7 .   ? 33.322  27.240  38.409  1.00 39.84 ? 712  HOH B O   1 
HETATM 18657 O  O   . HOH CA 7 .   ? -6.473  -9.501  24.750  1.00 47.44 ? 713  HOH B O   1 
HETATM 18658 O  O   . HOH CA 7 .   ? 39.365  29.357  11.355  1.00 51.74 ? 714  HOH B O   1 
HETATM 18659 O  O   . HOH CA 7 .   ? 12.080  9.802   36.283  1.00 38.90 ? 715  HOH B O   1 
HETATM 18660 O  O   . HOH CA 7 .   ? 13.579  35.869  50.937  1.00 36.47 ? 716  HOH B O   1 
HETATM 18661 O  O   . HOH CA 7 .   ? 20.149  6.064   30.394  1.00 41.57 ? 717  HOH B O   1 
HETATM 18662 O  O   . HOH CA 7 .   ? 44.923  44.113  46.274  1.00 30.51 ? 718  HOH B O   1 
HETATM 18663 O  O   . HOH CA 7 .   ? 25.845  36.970  24.490  1.00 44.94 ? 719  HOH B O   1 
HETATM 18664 O  O   . HOH CA 7 .   ? 45.269  28.457  49.937  1.00 54.38 ? 720  HOH B O   1 
HETATM 18665 O  O   . HOH CA 7 .   ? 8.511   29.621  59.746  1.00 50.81 ? 721  HOH B O   1 
HETATM 18666 O  O   . HOH CA 7 .   ? 18.837  7.853   49.513  1.00 37.92 ? 722  HOH B O   1 
HETATM 18667 O  O   . HOH CA 7 .   ? 11.819  28.030  8.762   1.00 61.22 ? 723  HOH B O   1 
HETATM 18668 O  O   . HOH CA 7 .   ? 38.692  39.691  64.373  1.00 30.78 ? 724  HOH B O   1 
HETATM 18669 O  O   . HOH CA 7 .   ? 9.480   31.236  40.573  1.00 37.81 ? 725  HOH B O   1 
HETATM 18670 O  O   . HOH CA 7 .   ? -15.273 -12.658 12.219  1.00 38.15 ? 726  HOH B O   1 
HETATM 18671 O  O   . HOH CA 7 .   ? 25.763  19.699  9.931   1.00 33.54 ? 727  HOH B O   1 
HETATM 18672 O  O   . HOH CA 7 .   ? 6.605   -9.270  36.462  1.00 25.52 ? 728  HOH B O   1 
HETATM 18673 O  O   . HOH CA 7 .   ? 43.550  36.425  63.288  1.00 50.69 ? 729  HOH B O   1 
HETATM 18674 O  O   . HOH CA 7 .   ? 20.866  -13.945 22.785  1.00 44.96 ? 730  HOH B O   1 
HETATM 18675 O  O   . HOH CA 7 .   ? 27.646  42.407  35.507  1.00 48.55 ? 731  HOH B O   1 
HETATM 18676 O  O   . HOH CA 7 .   ? 13.286  2.445   29.088  1.00 29.35 ? 732  HOH B O   1 
HETATM 18677 O  O   . HOH CA 7 .   ? 22.947  18.875  55.644  1.00 57.88 ? 733  HOH B O   1 
HETATM 18678 O  O   . HOH CA 7 .   ? 44.411  21.875  31.383  1.00 34.12 ? 734  HOH B O   1 
HETATM 18679 O  O   . HOH CA 7 .   ? 38.601  22.507  59.513  1.00 47.97 ? 735  HOH B O   1 
HETATM 18680 O  O   . HOH CA 7 .   ? 4.249   31.122  38.307  1.00 39.24 ? 736  HOH B O   1 
HETATM 18681 O  O   . HOH CA 7 .   ? 34.511  31.036  32.966  1.00 34.12 ? 737  HOH B O   1 
HETATM 18682 O  O   . HOH CA 7 .   ? 33.073  15.902  39.429  1.00 35.18 ? 738  HOH B O   1 
HETATM 18683 O  O   . HOH CA 7 .   ? 23.658  14.017  7.098   1.00 46.30 ? 739  HOH B O   1 
HETATM 18684 O  O   . HOH CA 7 .   ? 16.966  14.580  52.456  1.00 33.75 ? 740  HOH B O   1 
HETATM 18685 O  O   . HOH CA 7 .   ? -3.669  20.270  37.759  1.00 52.99 ? 741  HOH B O   1 
HETATM 18686 O  O   . HOH CA 7 .   ? 2.291   8.731   21.815  1.00 54.62 ? 742  HOH B O   1 
HETATM 18687 O  O   . HOH CA 7 .   ? 18.548  0.715   23.307  1.00 49.07 ? 743  HOH B O   1 
HETATM 18688 O  O   . HOH CA 7 .   ? 12.479  18.819  56.006  1.00 52.51 ? 744  HOH B O   1 
HETATM 18689 O  O   . HOH CA 7 .   ? 7.796   34.887  39.503  1.00 44.43 ? 745  HOH B O   1 
HETATM 18690 O  O   . HOH CA 7 .   ? 22.559  3.468   50.120  1.00 41.83 ? 746  HOH B O   1 
HETATM 18691 O  O   . HOH CA 7 .   ? 11.735  38.785  42.856  1.00 55.28 ? 747  HOH B O   1 
HETATM 18692 O  O   . HOH CA 7 .   ? 32.588  -3.080  47.556  1.00 56.59 ? 748  HOH B O   1 
HETATM 18693 O  O   . HOH CA 7 .   ? 50.991  8.159   34.268  1.00 45.99 ? 749  HOH B O   1 
HETATM 18694 O  O   . HOH CA 7 .   ? 35.455  32.266  18.457  1.00 47.67 ? 750  HOH B O   1 
HETATM 18695 O  O   . HOH CA 7 .   ? 19.691  -14.336 48.614  1.00 48.40 ? 751  HOH B O   1 
HETATM 18696 O  O   . HOH CA 7 .   ? 16.607  27.037  11.154  1.00 62.39 ? 752  HOH B O   1 
HETATM 18697 O  O   . HOH CA 7 .   ? 6.925   21.990  49.972  1.00 44.56 ? 753  HOH B O   1 
HETATM 18698 O  O   . HOH CA 7 .   ? 25.177  6.898   28.332  1.00 35.72 ? 754  HOH B O   1 
HETATM 18699 O  O   . HOH CA 7 .   ? 30.989  51.165  43.188  1.00 43.21 ? 755  HOH B O   1 
HETATM 18700 O  O   . HOH CA 7 .   ? 1.602   -10.711 30.918  1.00 38.27 ? 756  HOH B O   1 
HETATM 18701 O  O   . HOH CA 7 .   ? 5.908   3.012   32.091  1.00 44.94 ? 757  HOH B O   1 
HETATM 18702 O  O   . HOH CA 7 .   ? 4.606   9.879   22.079  1.00 58.86 ? 758  HOH B O   1 
HETATM 18703 O  O   . HOH CA 7 .   ? 7.068   23.896  18.675  1.00 39.46 ? 759  HOH B O   1 
HETATM 18704 O  O   . HOH CA 7 .   ? 16.935  -4.967  49.826  1.00 47.43 ? 760  HOH B O   1 
HETATM 18705 O  O   . HOH CA 7 .   ? 39.136  47.860  35.591  1.00 52.75 ? 761  HOH B O   1 
HETATM 18706 O  O   . HOH CA 7 .   ? 46.926  47.476  54.237  1.00 51.98 ? 762  HOH B O   1 
HETATM 18707 O  O   . HOH CA 7 .   ? 43.323  13.737  25.004  1.00 21.37 ? 763  HOH B O   1 
HETATM 18708 O  O   . HOH CA 7 .   ? 34.786  15.751  42.408  1.00 48.80 ? 764  HOH B O   1 
HETATM 18709 O  O   . HOH CA 7 .   ? 23.054  38.450  58.393  1.00 33.05 ? 765  HOH B O   1 
HETATM 18710 O  O   . HOH CA 7 .   ? 33.731  28.464  19.062  1.00 36.60 ? 766  HOH B O   1 
HETATM 18711 O  O   . HOH CA 7 .   ? 34.830  44.696  45.970  1.00 21.82 ? 767  HOH B O   1 
HETATM 18712 O  O   . HOH CA 7 .   ? -1.254  -6.126  28.316  1.00 37.87 ? 768  HOH B O   1 
HETATM 18713 O  O   . HOH CA 7 .   ? 6.353   31.400  37.301  1.00 36.35 ? 769  HOH B O   1 
HETATM 18714 O  O   . HOH CA 7 .   ? 34.407  4.861   33.887  1.00 56.24 ? 770  HOH B O   1 
HETATM 18715 O  O   . HOH CA 7 .   ? 49.195  3.504   33.616  1.00 46.69 ? 771  HOH B O   1 
HETATM 18716 O  O   . HOH CA 7 .   ? 29.048  8.021   34.392  1.00 31.99 ? 772  HOH B O   1 
HETATM 18717 O  O   . HOH CA 7 .   ? 47.007  35.354  48.215  1.00 49.85 ? 773  HOH B O   1 
HETATM 18718 O  O   . HOH CA 7 .   ? 43.319  44.602  50.060  1.00 26.74 ? 774  HOH B O   1 
HETATM 18719 O  O   . HOH CA 7 .   ? 49.792  36.188  40.599  1.00 49.53 ? 775  HOH B O   1 
HETATM 18720 O  O   . HOH CA 7 .   ? 45.339  19.591  17.292  1.00 28.86 ? 776  HOH B O   1 
HETATM 18721 O  O   . HOH CA 7 .   ? 48.400  20.260  20.864  1.00 37.43 ? 777  HOH B O   1 
HETATM 18722 O  O   . HOH CA 7 .   ? 27.882  27.095  15.106  1.00 26.42 ? 778  HOH B O   1 
HETATM 18723 O  O   . HOH CA 7 .   ? 27.874  8.939   9.485   1.00 25.50 ? 779  HOH B O   1 
HETATM 18724 O  O   . HOH CA 7 .   ? 27.672  46.981  57.272  1.00 39.76 ? 780  HOH B O   1 
HETATM 18725 O  O   . HOH CA 7 .   ? 41.685  24.094  24.205  1.00 28.52 ? 781  HOH B O   1 
HETATM 18726 O  O   . HOH CA 7 .   ? 7.662   20.588  56.886  1.00 49.61 ? 782  HOH B O   1 
HETATM 18727 O  O   . HOH CA 7 .   ? 2.049   31.266  32.074  1.00 29.90 ? 783  HOH B O   1 
HETATM 18728 O  O   . HOH CA 7 .   ? 19.951  26.136  60.561  1.00 38.41 ? 784  HOH B O   1 
HETATM 18729 O  O   . HOH CA 7 .   ? 20.215  2.130   28.723  1.00 42.77 ? 785  HOH B O   1 
HETATM 18730 O  O   . HOH CA 7 .   ? 14.232  37.646  43.977  1.00 35.71 ? 786  HOH B O   1 
HETATM 18731 O  O   . HOH CA 7 .   ? 33.138  52.577  48.893  1.00 41.50 ? 787  HOH B O   1 
HETATM 18732 O  O   . HOH CA 7 .   ? 41.473  22.523  34.845  1.00 31.48 ? 788  HOH B O   1 
HETATM 18733 O  O   . HOH CA 7 .   ? 29.037  36.225  71.903  1.00 49.51 ? 789  HOH B O   1 
HETATM 18734 O  O   . HOH CA 7 .   ? 28.347  30.988  39.077  1.00 42.68 ? 790  HOH B O   1 
HETATM 18735 O  O   . HOH CA 7 .   ? 34.726  10.166  33.859  1.00 38.58 ? 791  HOH B O   1 
HETATM 18736 O  O   . HOH CA 7 .   ? 40.668  15.705  26.081  1.00 40.07 ? 792  HOH B O   1 
HETATM 18737 O  O   . HOH CA 7 .   ? 21.191  -7.143  41.530  1.00 38.09 ? 793  HOH B O   1 
HETATM 18738 O  O   . HOH CA 7 .   ? 30.061  -0.504  34.956  1.00 51.39 ? 794  HOH B O   1 
HETATM 18739 O  O   . HOH CA 7 .   ? 30.039  -4.806  54.302  1.00 56.20 ? 795  HOH B O   1 
HETATM 18740 O  O   . HOH CA 7 .   ? 25.433  42.950  37.850  1.00 28.55 ? 796  HOH B O   1 
HETATM 18741 O  O   . HOH CA 7 .   ? 11.715  38.435  31.268  1.00 55.74 ? 797  HOH B O   1 
HETATM 18742 O  O   . HOH CA 7 .   ? 41.236  24.895  43.745  1.00 45.79 ? 798  HOH B O   1 
HETATM 18743 O  O   . HOH CA 7 .   ? 43.057  35.555  40.627  1.00 36.98 ? 799  HOH B O   1 
HETATM 18744 O  O   . HOH CA 7 .   ? 55.059  6.379   30.424  1.00 50.13 ? 800  HOH B O   1 
HETATM 18745 O  O   . HOH CA 7 .   ? 30.546  5.883   23.313  1.00 26.30 ? 801  HOH B O   1 
HETATM 18746 O  O   . HOH CA 7 .   ? 10.975  18.024  19.597  1.00 38.35 ? 802  HOH B O   1 
HETATM 18747 O  O   . HOH CA 7 .   ? 32.392  46.597  33.292  1.00 49.57 ? 803  HOH B O   1 
HETATM 18748 O  O   . HOH CA 7 .   ? 35.116  20.726  61.868  1.00 41.20 ? 804  HOH B O   1 
HETATM 18749 O  O   . HOH CA 7 .   ? 45.305  8.452   21.048  1.00 37.75 ? 805  HOH B O   1 
HETATM 18750 O  O   . HOH CA 7 .   ? 8.394   20.385  47.576  1.00 41.90 ? 806  HOH B O   1 
HETATM 18751 O  O   . HOH CA 7 .   ? 30.458  18.689  10.159  1.00 24.84 ? 807  HOH B O   1 
HETATM 18752 O  O   . HOH CA 7 .   ? 13.008  -0.679  46.299  1.00 42.71 ? 808  HOH B O   1 
HETATM 18753 O  O   . HOH CA 7 .   ? 2.367   37.795  28.312  1.00 47.94 ? 809  HOH B O   1 
HETATM 18754 O  O   . HOH CA 7 .   ? 31.966  23.423  50.174  1.00 33.52 ? 810  HOH B O   1 
HETATM 18755 O  O   . HOH CA 7 .   ? 39.266  15.192  5.631   1.00 42.29 ? 811  HOH B O   1 
HETATM 18756 O  O   . HOH CA 7 .   ? -0.691  18.662  40.309  1.00 48.13 ? 812  HOH B O   1 
HETATM 18757 O  O   . HOH CA 7 .   ? 26.300  43.596  58.854  1.00 32.93 ? 813  HOH B O   1 
HETATM 18758 O  O   . HOH CA 7 .   ? 2.035   -8.013  30.766  1.00 30.97 ? 814  HOH B O   1 
HETATM 18759 O  O   . HOH CA 7 .   ? 24.859  34.344  21.304  1.00 44.22 ? 815  HOH B O   1 
HETATM 18760 O  O   . HOH CA 7 .   ? 41.310  26.669  28.266  1.00 57.42 ? 816  HOH B O   1 
HETATM 18761 O  O   . HOH CA 7 .   ? 16.871  35.686  64.364  1.00 45.74 ? 817  HOH B O   1 
HETATM 18762 O  O   . HOH CA 7 .   ? 18.384  21.300  53.488  1.00 46.11 ? 818  HOH B O   1 
HETATM 18763 O  O   . HOH CA 7 .   ? 5.491   18.082  42.030  1.00 47.44 ? 819  HOH B O   1 
HETATM 18764 O  O   . HOH CA 7 .   ? 19.821  9.490   22.963  1.00 28.88 ? 820  HOH B O   1 
HETATM 18765 O  O   . HOH CA 7 .   ? 41.339  40.027  37.298  1.00 43.92 ? 821  HOH B O   1 
HETATM 18766 O  O   . HOH CA 7 .   ? 6.584   -7.849  44.499  1.00 38.14 ? 822  HOH B O   1 
HETATM 18767 O  O   . HOH CA 7 .   ? 10.263  -11.832 20.342  1.00 46.85 ? 823  HOH B O   1 
HETATM 18768 O  O   . HOH CA 7 .   ? 14.034  23.167  23.793  1.00 23.51 ? 824  HOH B O   1 
HETATM 18769 O  O   . HOH CA 7 .   ? 30.231  40.769  35.494  1.00 31.22 ? 825  HOH B O   1 
HETATM 18770 O  O   . HOH CA 7 .   ? 20.518  25.154  57.064  1.00 43.13 ? 826  HOH B O   1 
HETATM 18771 O  O   . HOH CA 7 .   ? 10.770  5.213   41.218  1.00 37.66 ? 827  HOH B O   1 
HETATM 18772 O  O   . HOH CA 7 .   ? 37.995  24.283  28.259  1.00 25.66 ? 828  HOH B O   1 
HETATM 18773 O  O   . HOH CA 7 .   ? 41.606  34.032  55.778  1.00 25.39 ? 829  HOH B O   1 
HETATM 18774 O  O   . HOH CA 7 .   ? 14.527  32.404  28.035  1.00 21.92 ? 830  HOH B O   1 
HETATM 18775 O  O   . HOH CA 7 .   ? 20.206  24.854  20.376  1.00 19.29 ? 831  HOH B O   1 
HETATM 18776 O  O   . HOH CA 7 .   ? 40.560  28.314  41.338  1.00 45.00 ? 832  HOH B O   1 
HETATM 18777 O  O   . HOH CA 7 .   ? 0.790   32.490  29.719  1.00 36.15 ? 833  HOH B O   1 
HETATM 18778 O  O   . HOH CA 7 .   ? 15.746  18.881  19.959  1.00 26.08 ? 834  HOH B O   1 
HETATM 18779 O  O   . HOH CA 7 .   ? 46.399  42.556  59.093  1.00 46.25 ? 835  HOH B O   1 
HETATM 18780 O  O   . HOH CA 7 .   ? 39.299  53.926  45.466  1.00 29.32 ? 836  HOH B O   1 
HETATM 18781 O  O   . HOH CA 7 .   ? 8.179   31.063  42.831  1.00 41.05 ? 837  HOH B O   1 
HETATM 18782 O  O   . HOH CA 7 .   ? 39.899  15.695  10.047  1.00 36.84 ? 838  HOH B O   1 
HETATM 18783 O  O   . HOH CA 7 .   ? 43.266  45.969  47.503  1.00 30.91 ? 839  HOH B O   1 
HETATM 18784 O  O   . HOH CA 7 .   ? 43.897  39.107  60.108  1.00 34.13 ? 840  HOH B O   1 
HETATM 18785 O  O   . HOH CA 7 .   ? 27.603  21.886  37.579  1.00 30.33 ? 841  HOH B O   1 
HETATM 18786 O  O   . HOH CA 7 .   ? 10.047  -18.689 32.401  1.00 38.17 ? 842  HOH B O   1 
HETATM 18787 O  O   . HOH CA 7 .   ? 6.219   32.339  21.076  1.00 37.30 ? 843  HOH B O   1 
HETATM 18788 O  O   . HOH CA 7 .   ? 29.866  0.207   26.886  1.00 26.13 ? 844  HOH B O   1 
HETATM 18789 O  O   . HOH CA 7 .   ? 20.445  30.043  25.439  1.00 20.07 ? 845  HOH B O   1 
HETATM 18790 O  O   . HOH CA 7 .   ? 40.318  10.846  38.270  1.00 44.92 ? 846  HOH B O   1 
HETATM 18791 O  O   . HOH CA 7 .   ? 17.796  12.174  13.386  1.00 44.06 ? 847  HOH B O   1 
HETATM 18792 O  O   . HOH CA 7 .   ? 26.675  21.450  53.855  1.00 42.62 ? 848  HOH B O   1 
HETATM 18793 O  O   . HOH CA 7 .   ? 36.176  22.398  12.664  1.00 29.09 ? 849  HOH B O   1 
HETATM 18794 O  O   . HOH CA 7 .   ? 41.948  35.148  60.163  1.00 35.75 ? 850  HOH B O   1 
HETATM 18795 O  O   . HOH CA 7 .   ? 27.092  7.853   35.989  1.00 26.01 ? 851  HOH B O   1 
HETATM 18796 O  O   . HOH CA 7 .   ? 44.577  25.044  47.500  1.00 60.06 ? 852  HOH B O   1 
HETATM 18797 O  O   . HOH CA 7 .   ? 41.911  29.006  43.542  1.00 34.36 ? 853  HOH B O   1 
HETATM 18798 O  O   . HOH CA 7 .   ? 32.549  49.130  34.251  1.00 58.33 ? 854  HOH B O   1 
HETATM 18799 O  O   . HOH CA 7 .   ? 39.744  17.755  25.241  1.00 28.99 ? 855  HOH B O   1 
HETATM 18800 O  O   . HOH CA 7 .   ? 29.641  27.516  28.526  1.00 22.15 ? 856  HOH B O   1 
HETATM 18801 O  O   . HOH CA 7 .   ? 38.071  27.232  59.577  1.00 36.57 ? 857  HOH B O   1 
HETATM 18802 O  O   . HOH CA 7 .   ? 39.150  33.582  27.912  1.00 52.15 ? 858  HOH B O   1 
HETATM 18803 O  O   . HOH CA 7 .   ? 33.289  6.476   32.448  1.00 58.94 ? 859  HOH B O   1 
HETATM 18804 O  O   . HOH CA 7 .   ? 12.757  12.403  45.230  1.00 24.04 ? 860  HOH B O   1 
HETATM 18805 O  O   . HOH CA 7 .   ? 33.519  9.051   45.991  1.00 49.08 ? 861  HOH B O   1 
HETATM 18806 O  O   . HOH CA 7 .   ? 50.217  45.767  54.067  1.00 51.83 ? 862  HOH B O   1 
HETATM 18807 O  O   . HOH CA 7 .   ? 35.169  17.715  5.467   1.00 56.40 ? 863  HOH B O   1 
HETATM 18808 O  O   . HOH CA 7 .   ? -3.637  -8.221  18.136  1.00 22.85 ? 864  HOH B O   1 
HETATM 18809 O  O   . HOH CA 7 .   ? 35.673  50.050  31.643  1.00 49.96 ? 865  HOH B O   1 
HETATM 18810 O  O   . HOH CA 7 .   ? 26.353  -4.328  36.998  1.00 39.64 ? 866  HOH B O   1 
HETATM 18811 O  O   . HOH CA 7 .   ? 22.172  24.438  12.712  1.00 31.89 ? 867  HOH B O   1 
HETATM 18812 O  O   . HOH CA 7 .   ? 20.823  1.228   47.404  1.00 43.77 ? 868  HOH B O   1 
HETATM 18813 O  O   . HOH CA 7 .   ? 33.008  56.996  45.920  1.00 48.56 ? 869  HOH B O   1 
HETATM 18814 O  O   . HOH CA 7 .   ? 20.415  54.661  41.925  1.00 51.01 ? 870  HOH B O   1 
HETATM 18815 O  O   . HOH CA 7 .   ? 43.341  35.546  51.478  1.00 34.70 ? 871  HOH B O   1 
HETATM 18816 O  O   . HOH CA 7 .   ? 16.005  26.950  48.978  1.00 30.43 ? 872  HOH B O   1 
HETATM 18817 O  O   . HOH CA 7 .   ? 18.230  35.263  19.995  1.00 36.14 ? 873  HOH B O   1 
HETATM 18818 O  O   . HOH CA 7 .   ? 38.867  28.759  49.780  1.00 27.24 ? 874  HOH B O   1 
HETATM 18819 O  O   . HOH CA 7 .   ? 31.729  17.379  37.558  1.00 46.30 ? 875  HOH B O   1 
HETATM 18820 O  O   . HOH CA 7 .   ? 29.914  21.921  68.807  1.00 50.46 ? 876  HOH B O   1 
HETATM 18821 O  O   . HOH CA 7 .   ? 3.582   4.547   35.561  1.00 54.46 ? 877  HOH B O   1 
HETATM 18822 O  O   . HOH CA 7 .   ? 22.518  37.569  51.731  1.00 32.55 ? 878  HOH B O   1 
HETATM 18823 O  O   . HOH CA 7 .   ? 31.876  36.307  68.153  1.00 36.65 ? 879  HOH B O   1 
HETATM 18824 O  O   . HOH CA 7 .   ? -3.296  -11.140 25.118  1.00 25.64 ? 880  HOH B O   1 
HETATM 18825 O  O   . HOH CA 7 .   ? 40.177  22.659  26.179  1.00 24.26 ? 881  HOH B O   1 
HETATM 18826 O  O   . HOH CA 7 .   ? 50.249  42.590  56.860  1.00 46.27 ? 882  HOH B O   1 
HETATM 18827 O  O   . HOH CA 7 .   ? 7.462   12.578  23.709  1.00 48.76 ? 883  HOH B O   1 
HETATM 18828 O  O   . HOH CA 7 .   ? 23.102  14.447  51.214  1.00 47.01 ? 884  HOH B O   1 
HETATM 18829 O  O   . HOH CA 7 .   ? 21.772  30.748  28.982  1.00 19.48 ? 885  HOH B O   1 
HETATM 18830 O  O   . HOH CA 7 .   ? 10.834  32.339  46.744  1.00 34.08 ? 886  HOH B O   1 
HETATM 18831 O  O   . HOH CA 7 .   ? 19.545  29.469  67.374  1.00 53.40 ? 887  HOH B O   1 
HETATM 18832 O  O   . HOH CA 7 .   ? 35.871  10.578  17.512  1.00 27.49 ? 888  HOH B O   1 
HETATM 18833 O  O   . HOH CA 7 .   ? 1.248   21.727  17.657  1.00 29.70 ? 889  HOH B O   1 
HETATM 18834 O  O   . HOH CA 7 .   ? 23.876  26.668  13.021  1.00 34.40 ? 890  HOH B O   1 
HETATM 18835 O  O   . HOH CA 7 .   ? 17.860  28.073  19.496  1.00 21.35 ? 891  HOH B O   1 
HETATM 18836 O  O   . HOH CA 7 .   ? -1.935  -7.109  25.695  1.00 32.65 ? 892  HOH B O   1 
HETATM 18837 O  O   . HOH CA 7 .   ? 32.091  24.702  32.470  1.00 22.40 ? 893  HOH B O   1 
HETATM 18838 O  O   . HOH CA 7 .   ? 45.399  30.359  46.095  1.00 45.15 ? 894  HOH B O   1 
HETATM 18839 O  O   . HOH CA 7 .   ? 25.962  4.853   10.485  1.00 51.90 ? 895  HOH B O   1 
HETATM 18840 O  O   . HOH CA 7 .   ? 19.241  23.642  61.032  1.00 47.10 ? 896  HOH B O   1 
HETATM 18841 O  O   . HOH CA 7 .   ? 35.165  41.566  65.271  1.00 45.70 ? 897  HOH B O   1 
HETATM 18842 O  O   . HOH CA 7 .   ? 29.046  49.142  39.929  1.00 35.44 ? 898  HOH B O   1 
HETATM 18843 O  O   . HOH CA 7 .   ? 37.264  26.237  39.359  1.00 42.35 ? 899  HOH B O   1 
HETATM 18844 O  O   . HOH CA 7 .   ? 9.975   46.895  46.465  1.00 34.27 ? 900  HOH B O   1 
HETATM 18845 O  O   . HOH CA 7 .   ? 41.621  32.303  63.469  1.00 44.16 ? 901  HOH B O   1 
HETATM 18846 O  O   . HOH CA 7 .   ? 23.666  50.375  47.869  1.00 45.98 ? 902  HOH B O   1 
HETATM 18847 O  O   . HOH CA 7 .   ? 33.417  25.615  12.304  1.00 28.99 ? 903  HOH B O   1 
HETATM 18848 O  O   . HOH CA 7 .   ? 15.321  20.796  39.529  1.00 18.81 ? 904  HOH B O   1 
HETATM 18849 O  O   . HOH CA 7 .   ? 7.480   -17.259 39.747  1.00 33.77 ? 905  HOH B O   1 
HETATM 18850 O  O   . HOH CA 7 .   ? 2.751   20.643  42.111  1.00 53.90 ? 906  HOH B O   1 
HETATM 18851 O  O   . HOH CA 7 .   ? -6.801  -14.103 24.876  1.00 50.62 ? 907  HOH B O   1 
HETATM 18852 O  O   . HOH CA 7 .   ? 37.538  56.035  48.539  1.00 42.97 ? 908  HOH B O   1 
HETATM 18853 O  O   . HOH CA 7 .   ? 32.490  35.117  23.630  1.00 27.31 ? 909  HOH B O   1 
HETATM 18854 O  O   . HOH CA 7 .   ? -5.351  -6.397  17.612  1.00 30.87 ? 910  HOH B O   1 
HETATM 18855 O  O   . HOH CA 7 .   ? 25.750  4.191   13.829  1.00 44.45 ? 911  HOH B O   1 
HETATM 18856 O  O   . HOH CA 7 .   ? 33.840  13.245  40.034  1.00 36.14 ? 912  HOH B O   1 
HETATM 18857 O  O   . HOH CA 7 .   ? 0.815   -5.237  23.336  1.00 50.10 ? 913  HOH B O   1 
HETATM 18858 O  O   . HOH CA 7 .   ? 17.860  -13.571 23.274  1.00 47.10 ? 914  HOH B O   1 
HETATM 18859 O  O   . HOH CA 7 .   ? 2.220   32.303  25.582  1.00 35.35 ? 915  HOH B O   1 
HETATM 18860 O  O   . HOH CA 7 .   ? 41.904  21.824  54.343  1.00 46.12 ? 916  HOH B O   1 
HETATM 18861 O  O   . HOH CA 7 .   ? 1.599   -1.362  30.079  1.00 44.66 ? 917  HOH B O   1 
HETATM 18862 O  O   . HOH CA 7 .   ? 9.511   29.209  51.583  1.00 39.33 ? 918  HOH B O   1 
HETATM 18863 O  O   . HOH CA 7 .   ? 36.865  36.564  37.318  1.00 41.47 ? 919  HOH B O   1 
HETATM 18864 O  O   . HOH CA 7 .   ? 45.640  40.430  50.639  1.00 40.68 ? 920  HOH B O   1 
HETATM 18865 O  O   . HOH CA 7 .   ? 1.207   16.327  23.572  1.00 51.47 ? 921  HOH B O   1 
HETATM 18866 O  O   . HOH CA 7 .   ? 43.582  47.735  39.200  1.00 27.59 ? 922  HOH B O   1 
HETATM 18867 O  O   . HOH CA 7 .   ? 12.050  -19.955 31.747  1.00 46.82 ? 923  HOH B O   1 
HETATM 18868 O  O   . HOH CA 7 .   ? 46.649  7.516   34.751  1.00 42.18 ? 924  HOH B O   1 
HETATM 18869 O  O   . HOH CA 7 .   ? 47.710  23.227  25.700  1.00 33.08 ? 925  HOH B O   1 
HETATM 18870 O  O   . HOH CA 7 .   ? 57.798  9.738   34.425  1.00 60.52 ? 926  HOH B O   1 
HETATM 18871 O  O   . HOH CA 7 .   ? 44.618  51.430  54.691  1.00 52.39 ? 927  HOH B O   1 
HETATM 18872 O  O   . HOH CA 7 .   ? 40.795  28.695  21.242  1.00 47.55 ? 928  HOH B O   1 
HETATM 18873 O  O   . HOH CA 7 .   ? 6.235   20.176  20.015  1.00 36.18 ? 929  HOH B O   1 
HETATM 18874 O  O   . HOH CA 7 .   ? 17.604  21.890  67.819  1.00 54.62 ? 930  HOH B O   1 
HETATM 18875 O  O   . HOH CA 7 .   ? 12.888  30.836  23.568  1.00 22.25 ? 931  HOH B O   1 
HETATM 18876 O  O   . HOH CA 7 .   ? 0.769   -19.044 29.892  1.00 33.48 ? 932  HOH B O   1 
HETATM 18877 O  O   . HOH CA 7 .   ? 21.969  8.521   26.416  1.00 49.08 ? 933  HOH B O   1 
HETATM 18878 O  O   . HOH CA 7 .   ? 18.435  49.748  37.543  1.00 48.72 ? 934  HOH B O   1 
HETATM 18879 O  O   . HOH CA 7 .   ? 3.779   13.720  25.269  1.00 44.47 ? 935  HOH B O   1 
HETATM 18880 O  O   . HOH CA 7 .   ? 16.769  40.396  46.649  1.00 39.70 ? 936  HOH B O   1 
HETATM 18881 O  O   . HOH CA 7 .   ? 4.559   -1.705  36.020  1.00 38.61 ? 937  HOH B O   1 
HETATM 18882 O  O   . HOH CA 7 .   ? 35.189  32.654  42.350  1.00 21.09 ? 938  HOH B O   1 
HETATM 18883 O  O   . HOH CA 7 .   ? 21.146  29.628  63.350  1.00 29.69 ? 939  HOH B O   1 
HETATM 18884 O  O   . HOH CA 7 .   ? 42.004  33.282  15.135  1.00 58.25 ? 940  HOH B O   1 
HETATM 18885 O  O   . HOH CA 7 .   ? 44.392  15.935  14.875  1.00 51.09 ? 941  HOH B O   1 
HETATM 18886 O  O   . HOH CA 7 .   ? 17.955  22.909  12.494  1.00 53.77 ? 942  HOH B O   1 
HETATM 18887 O  O   . HOH CA 7 .   ? 37.401  37.693  65.477  1.00 31.93 ? 943  HOH B O   1 
HETATM 18888 O  O   . HOH CA 7 .   ? 11.355  38.474  34.160  1.00 42.96 ? 944  HOH B O   1 
HETATM 18889 O  O   . HOH CA 7 .   ? 44.292  24.067  49.999  1.00 55.37 ? 945  HOH B O   1 
HETATM 18890 O  O   . HOH CA 7 .   ? 5.411   -6.760  22.567  1.00 44.43 ? 946  HOH B O   1 
HETATM 18891 O  O   . HOH CA 7 .   ? 22.426  6.482   13.017  1.00 41.59 ? 947  HOH B O   1 
HETATM 18892 O  O   . HOH CA 7 .   ? 45.010  11.859  15.335  1.00 38.63 ? 948  HOH B O   1 
HETATM 18893 O  O   . HOH CA 7 .   ? 35.345  -4.243  24.365  1.00 23.38 ? 949  HOH B O   1 
HETATM 18894 O  O   . HOH CA 7 .   ? 33.859  28.415  12.810  1.00 48.24 ? 950  HOH B O   1 
HETATM 18895 O  O   . HOH CA 7 .   ? 12.205  21.285  22.899  1.00 23.64 ? 951  HOH B O   1 
HETATM 18896 O  O   . HOH CA 7 .   ? 11.670  4.268   27.930  1.00 32.47 ? 952  HOH B O   1 
HETATM 18897 O  O   . HOH CA 7 .   ? 19.887  6.864   13.571  1.00 53.32 ? 953  HOH B O   1 
HETATM 18898 O  O   . HOH CA 7 .   ? 11.605  38.256  55.316  1.00 51.16 ? 954  HOH B O   1 
HETATM 18899 O  O   . HOH CA 7 .   ? 51.230  20.159  30.333  1.00 58.22 ? 955  HOH B O   1 
HETATM 18900 O  O   . HOH CA 7 .   ? 19.826  36.875  30.008  1.00 32.45 ? 956  HOH B O   1 
HETATM 18901 O  O   . HOH CA 7 .   ? 14.019  9.754   48.512  1.00 49.87 ? 957  HOH B O   1 
HETATM 18902 O  O   . HOH CA 7 .   ? -2.463  28.365  22.378  1.00 41.25 ? 958  HOH B O   1 
HETATM 18903 O  O   . HOH CA 7 .   ? 20.147  36.647  52.732  1.00 37.37 ? 959  HOH B O   1 
HETATM 18904 O  O   . HOH CA 7 .   ? 7.568   37.320  34.397  1.00 48.13 ? 960  HOH B O   1 
HETATM 18905 O  O   . HOH CA 7 .   ? 5.421   31.873  24.762  1.00 29.24 ? 961  HOH B O   1 
HETATM 18906 O  O   . HOH CA 7 .   ? 12.487  9.342   21.322  1.00 41.50 ? 962  HOH B O   1 
HETATM 18907 O  O   . HOH CA 7 .   ? 7.814   6.458   37.540  1.00 53.96 ? 963  HOH B O   1 
HETATM 18908 O  O   . HOH CA 7 .   ? 15.308  16.094  18.077  1.00 20.29 ? 964  HOH B O   1 
HETATM 18909 O  O   . HOH CA 7 .   ? 37.649  21.891  40.490  1.00 42.84 ? 965  HOH B O   1 
HETATM 18910 O  O   . HOH CA 7 .   ? 22.172  -0.275  49.153  1.00 47.92 ? 966  HOH B O   1 
HETATM 18911 O  O   . HOH CA 7 .   ? 26.551  21.050  42.818  1.00 34.92 ? 967  HOH B O   1 
HETATM 18912 O  O   . HOH CA 7 .   ? 19.098  23.332  55.058  1.00 41.19 ? 968  HOH B O   1 
HETATM 18913 O  O   . HOH CA 7 .   ? 8.295   -19.570 24.060  1.00 22.96 ? 969  HOH B O   1 
HETATM 18914 O  O   . HOH CA 7 .   ? 55.721  46.142  40.594  1.00 28.93 ? 970  HOH B O   1 
HETATM 18915 O  O   . HOH CA 7 .   ? -1.536  24.780  37.085  1.00 53.79 ? 971  HOH B O   1 
HETATM 18916 O  O   . HOH CA 7 .   ? 10.510  12.845  38.379  1.00 55.29 ? 972  HOH B O   1 
HETATM 18917 O  O   . HOH CA 7 .   ? 16.207  42.004  37.483  1.00 26.10 ? 973  HOH B O   1 
HETATM 18918 O  O   . HOH CA 7 .   ? 24.699  14.841  45.055  1.00 40.38 ? 974  HOH B O   1 
HETATM 18919 O  O   . HOH CA 7 .   ? 46.968  38.197  53.595  1.00 51.42 ? 975  HOH B O   1 
HETATM 18920 O  O   . HOH CA 7 .   ? 25.276  17.129  41.926  1.00 38.38 ? 976  HOH B O   1 
HETATM 18921 O  O   . HOH CA 7 .   ? 11.106  -2.394  45.940  1.00 41.21 ? 977  HOH B O   1 
HETATM 18922 O  O   . HOH CA 7 .   ? 0.724   10.689  30.317  1.00 48.73 ? 978  HOH B O   1 
HETATM 18923 O  O   . HOH CA 7 .   ? 11.421  25.910  19.019  1.00 20.14 ? 979  HOH B O   1 
HETATM 18924 O  O   . HOH CA 7 .   ? 41.042  26.725  24.984  1.00 33.40 ? 980  HOH B O   1 
HETATM 18925 O  O   . HOH CA 7 .   ? 18.603  22.899  73.478  1.00 53.11 ? 981  HOH B O   1 
HETATM 18926 O  O   . HOH CA 7 .   ? 19.710  9.701   30.856  1.00 33.17 ? 982  HOH B O   1 
HETATM 18927 O  O   . HOH CA 7 .   ? 38.646  22.648  13.690  1.00 28.09 ? 983  HOH B O   1 
HETATM 18928 O  O   . HOH CA 7 .   ? 10.728  23.926  15.707  1.00 48.68 ? 984  HOH B O   1 
HETATM 18929 O  O   . HOH CA 7 .   ? 44.775  54.468  43.610  1.00 39.33 ? 985  HOH B O   1 
HETATM 18930 O  O   . HOH CA 7 .   ? 16.997  -10.414 30.045  1.00 30.46 ? 986  HOH B O   1 
HETATM 18931 O  O   . HOH CA 7 .   ? 18.582  -6.921  40.670  1.00 30.54 ? 987  HOH B O   1 
HETATM 18932 O  O   . HOH CA 7 .   ? 40.924  42.606  61.714  1.00 34.60 ? 988  HOH B O   1 
HETATM 18933 O  O   . HOH CA 7 .   ? 22.938  41.626  37.118  1.00 32.14 ? 989  HOH B O   1 
HETATM 18934 O  O   . HOH CA 7 .   ? 48.772  2.361   24.220  1.00 34.47 ? 990  HOH B O   1 
HETATM 18935 O  O   . HOH CA 7 .   ? 37.944  15.154  26.487  1.00 50.31 ? 991  HOH B O   1 
HETATM 18936 O  O   . HOH CA 7 .   ? 5.120   24.615  41.053  1.00 36.40 ? 992  HOH B O   1 
HETATM 18937 O  O   . HOH CA 7 .   ? -0.729  29.826  33.178  1.00 44.49 ? 993  HOH B O   1 
HETATM 18938 O  O   . HOH CA 7 .   ? 42.977  24.689  54.476  1.00 38.25 ? 994  HOH B O   1 
HETATM 18939 O  O   . HOH CA 7 .   ? 21.607  51.802  38.223  1.00 35.68 ? 995  HOH B O   1 
HETATM 18940 O  O   . HOH CA 7 .   ? 19.310  37.825  54.958  1.00 39.44 ? 996  HOH B O   1 
HETATM 18941 O  O   . HOH CA 7 .   ? 24.421  34.869  36.647  1.00 29.62 ? 997  HOH B O   1 
HETATM 18942 O  O   . HOH CA 7 .   ? 18.739  17.103  52.196  1.00 32.52 ? 998  HOH B O   1 
HETATM 18943 O  O   . HOH CA 7 .   ? 48.340  14.527  37.023  1.00 49.48 ? 999  HOH B O   1 
HETATM 18944 O  O   . HOH CA 7 .   ? 15.694  1.139   21.431  1.00 49.57 ? 1000 HOH B O   1 
HETATM 18945 O  O   . HOH CA 7 .   ? 42.188  31.836  39.610  1.00 42.93 ? 1001 HOH B O   1 
HETATM 18946 O  O   . HOH CA 7 .   ? 23.075  37.224  35.931  1.00 42.79 ? 1002 HOH B O   1 
HETATM 18947 O  O   . HOH CA 7 .   ? 52.358  10.738  24.717  1.00 50.78 ? 1003 HOH B O   1 
HETATM 18948 O  O   . HOH CA 7 .   ? -4.639  22.403  30.338  1.00 47.29 ? 1004 HOH B O   1 
HETATM 18949 O  O   . HOH CA 7 .   ? 14.023  -1.520  30.892  1.00 23.76 ? 1005 HOH B O   1 
HETATM 18950 O  O   . HOH CA 7 .   ? 40.838  6.564   40.553  1.00 58.80 ? 1006 HOH B O   1 
HETATM 18951 O  O   . HOH CA 7 .   ? 21.016  -13.961 45.964  1.00 40.86 ? 1007 HOH B O   1 
HETATM 18952 O  O   . HOH CA 7 .   ? 27.691  17.112  65.894  1.00 53.81 ? 1008 HOH B O   1 
HETATM 18953 O  O   . HOH CA 7 .   ? 7.576   4.415   30.553  1.00 45.33 ? 1009 HOH B O   1 
HETATM 18954 O  O   . HOH CA 7 .   ? 51.337  17.881  22.153  1.00 38.88 ? 1010 HOH B O   1 
HETATM 18955 O  O   . HOH CA 7 .   ? 15.348  6.975   17.478  1.00 42.96 ? 1011 HOH B O   1 
HETATM 18956 O  O   . HOH CA 7 .   ? 14.186  22.881  16.806  1.00 33.98 ? 1012 HOH B O   1 
HETATM 18957 O  O   . HOH CA 7 .   ? -5.154  26.015  24.559  1.00 51.71 ? 1013 HOH B O   1 
HETATM 18958 O  O   . HOH CA 7 .   ? 26.233  35.630  29.208  1.00 46.85 ? 1014 HOH B O   1 
HETATM 18959 O  O   . HOH CA 7 .   ? 30.696  34.038  68.640  1.00 42.03 ? 1015 HOH B O   1 
HETATM 18960 O  O   . HOH CA 7 .   ? 6.957   7.178   30.488  1.00 30.86 ? 1016 HOH B O   1 
HETATM 18961 O  O   . HOH CA 7 .   ? 12.362  8.831   13.620  1.00 38.63 ? 1017 HOH B O   1 
HETATM 18962 O  O   . HOH CA 7 .   ? 22.726  42.157  63.539  1.00 46.02 ? 1018 HOH B O   1 
HETATM 18963 O  O   . HOH CA 7 .   ? 17.933  29.533  17.265  1.00 40.54 ? 1019 HOH B O   1 
HETATM 18964 O  O   . HOH CA 7 .   ? 21.346  19.294  7.518   1.00 50.67 ? 1020 HOH B O   1 
HETATM 18965 O  O   . HOH CA 7 .   ? 38.216  50.652  34.389  1.00 48.55 ? 1021 HOH B O   1 
HETATM 18966 O  O   . HOH CA 7 .   ? -2.878  20.755  30.803  1.00 39.62 ? 1022 HOH B O   1 
HETATM 18967 O  O   . HOH CA 7 .   ? 30.958  19.936  59.851  1.00 34.14 ? 1023 HOH B O   1 
HETATM 18968 O  O   . HOH CA 7 .   ? 1.730   -14.610 32.800  1.00 30.13 ? 1024 HOH B O   1 
HETATM 18969 O  O   . HOH CA 7 .   ? 44.556  18.909  36.387  1.00 45.33 ? 1025 HOH B O   1 
HETATM 18970 O  O   . HOH CA 7 .   ? 40.767  37.682  40.445  1.00 35.58 ? 1026 HOH B O   1 
HETATM 18971 O  O   . HOH CA 7 .   ? 17.366  10.134  51.748  1.00 52.58 ? 1027 HOH B O   1 
HETATM 18972 O  O   . HOH CA 7 .   ? 42.003  3.080   30.987  1.00 31.03 ? 1028 HOH B O   1 
HETATM 18973 O  O   . HOH CA 7 .   ? 20.391  20.778  51.564  1.00 34.86 ? 1029 HOH B O   1 
HETATM 18974 O  O   . HOH CA 7 .   ? 13.630  20.005  17.330  1.00 30.90 ? 1030 HOH B O   1 
HETATM 18975 O  O   . HOH CA 7 .   ? 6.887   -4.788  38.132  1.00 23.20 ? 1031 HOH B O   1 
HETATM 18976 O  O   . HOH CA 7 .   ? 47.010  47.935  45.590  1.00 36.94 ? 1032 HOH B O   1 
HETATM 18977 O  O   . HOH CA 7 .   ? 23.614  31.914  71.150  1.00 49.01 ? 1033 HOH B O   1 
HETATM 18978 O  O   . HOH CA 7 .   ? 23.475  8.712   30.597  1.00 36.37 ? 1034 HOH B O   1 
HETATM 18979 O  O   . HOH CA 7 .   ? 11.244  -2.408  30.358  1.00 24.82 ? 1035 HOH B O   1 
HETATM 18980 O  O   . HOH CA 7 .   ? 10.871  20.723  18.401  1.00 42.57 ? 1036 HOH B O   1 
HETATM 18981 O  O   . HOH CA 7 .   ? 9.724   7.949   38.536  1.00 53.42 ? 1037 HOH B O   1 
HETATM 18982 O  O   . HOH CA 7 .   ? 30.139  50.055  47.460  1.00 53.67 ? 1038 HOH B O   1 
HETATM 18983 O  O   . HOH CA 7 .   ? -11.366 -13.204 23.404  1.00 42.99 ? 1039 HOH B O   1 
HETATM 18984 O  O   . HOH CA 7 .   ? 21.826  39.582  61.446  1.00 45.76 ? 1040 HOH B O   1 
HETATM 18985 O  O   . HOH CA 7 .   ? -3.444  -13.339 26.702  1.00 42.34 ? 1041 HOH B O   1 
HETATM 18986 O  O   . HOH CA 7 .   ? 25.495  33.728  71.320  1.00 46.57 ? 1042 HOH B O   1 
HETATM 18987 O  O   . HOH CA 7 .   ? 44.625  28.065  52.976  1.00 50.88 ? 1043 HOH B O   1 
HETATM 18988 O  O   . HOH CA 7 .   ? 47.018  10.062  19.904  1.00 41.81 ? 1044 HOH B O   1 
HETATM 18989 O  O   . HOH CA 7 .   ? 6.292   12.443  27.105  1.00 38.71 ? 1045 HOH B O   1 
HETATM 18990 O  O   . HOH CA 7 .   ? 46.765  45.313  44.565  1.00 27.42 ? 1046 HOH B O   1 
HETATM 18991 O  O   . HOH CA 7 .   ? 24.138  44.636  57.938  1.00 44.22 ? 1047 HOH B O   1 
HETATM 18992 O  O   . HOH CA 7 .   ? 19.099  16.706  8.601   1.00 57.31 ? 1048 HOH B O   1 
HETATM 18993 O  O   . HOH CA 7 .   ? 28.318  29.650  15.835  1.00 42.40 ? 1049 HOH B O   1 
HETATM 18994 O  O   . HOH CA 7 .   ? 32.784  43.495  30.191  1.00 51.23 ? 1050 HOH B O   1 
HETATM 18995 O  O   . HOH CA 7 .   ? 39.277  43.368  30.968  1.00 50.66 ? 1051 HOH B O   1 
HETATM 18996 O  O   . HOH CA 7 .   ? 39.164  -2.047  27.416  1.00 31.05 ? 1052 HOH B O   1 
HETATM 18997 O  O   . HOH CA 7 .   ? 47.695  24.678  20.623  1.00 38.08 ? 1053 HOH B O   1 
HETATM 18998 O  O   . HOH CA 7 .   ? -11.233 -16.729 17.218  1.00 37.42 ? 1054 HOH B O   1 
HETATM 18999 O  O   . HOH CA 7 .   ? 45.079  30.021  15.640  1.00 39.53 ? 1055 HOH B O   1 
HETATM 19000 O  O   . HOH CA 7 .   ? 5.703   25.670  50.580  1.00 48.55 ? 1056 HOH B O   1 
HETATM 19001 O  O   . HOH CA 7 .   ? 31.095  52.223  47.322  1.00 50.33 ? 1057 HOH B O   1 
HETATM 19002 O  O   . HOH CA 7 .   ? -0.366  -7.071  19.818  1.00 33.02 ? 1058 HOH B O   1 
HETATM 19003 O  O   . HOH CA 7 .   ? 8.556   3.617   28.330  1.00 57.34 ? 1059 HOH B O   1 
HETATM 19004 O  O   . HOH CA 7 .   ? 8.813   -1.550  29.869  1.00 27.88 ? 1060 HOH B O   1 
HETATM 19005 O  O   . HOH CA 7 .   ? -1.091  26.736  35.292  1.00 39.23 ? 1061 HOH B O   1 
HETATM 19006 O  O   . HOH CA 7 .   ? 2.965   0.887   33.657  1.00 45.65 ? 1062 HOH B O   1 
HETATM 19007 O  O   . HOH CA 7 .   ? 45.293  33.452  51.829  1.00 50.54 ? 1063 HOH B O   1 
HETATM 19008 O  O   . HOH CA 7 .   ? 17.089  37.841  31.820  1.00 33.44 ? 1064 HOH B O   1 
HETATM 19009 O  O   . HOH CA 7 .   ? 15.438  9.630   20.448  1.00 32.87 ? 1065 HOH B O   1 
HETATM 19010 O  O   . HOH CA 7 .   ? 42.020  19.121  47.691  1.00 54.85 ? 1066 HOH B O   1 
HETATM 19011 O  O   . HOH CA 7 .   ? 25.912  14.619  42.735  1.00 45.80 ? 1067 HOH B O   1 
HETATM 19012 O  O   . HOH CA 7 .   ? -3.962  28.620  27.059  1.00 50.77 ? 1068 HOH B O   1 
HETATM 19013 O  O   . HOH CA 7 .   ? 44.108  10.160  36.074  1.00 46.07 ? 1069 HOH B O   1 
HETATM 19014 O  O   . HOH CA 7 .   ? 31.957  52.520  44.868  1.00 40.47 ? 1070 HOH B O   1 
HETATM 19015 O  O   . HOH CA 7 .   ? 39.382  18.428  7.567   1.00 52.20 ? 1071 HOH B O   1 
HETATM 19016 O  O   . HOH CA 7 .   ? 16.171  6.385   50.179  1.00 51.91 ? 1072 HOH B O   1 
HETATM 19017 O  O   . HOH CA 7 .   ? 3.281   -14.527 35.150  1.00 29.66 ? 1073 HOH B O   1 
HETATM 19018 O  O   . HOH CA 7 .   ? 10.316  19.351  49.760  1.00 39.65 ? 1074 HOH B O   1 
HETATM 19019 O  O   . HOH CA 7 .   ? 45.475  12.424  36.755  1.00 44.97 ? 1075 HOH B O   1 
HETATM 19020 O  O   . HOH CA 7 .   ? 10.056  13.404  45.489  1.00 26.96 ? 1076 HOH B O   1 
HETATM 19021 O  O   . HOH CA 7 .   ? 13.507  45.737  52.165  1.00 59.56 ? 1077 HOH B O   1 
HETATM 19022 O  O   . HOH CA 7 .   ? 19.154  20.160  8.515   1.00 52.05 ? 1078 HOH B O   1 
HETATM 19023 O  O   . HOH CA 7 .   ? 33.461  -1.685  31.572  1.00 45.06 ? 1079 HOH B O   1 
HETATM 19024 O  O   . HOH CA 7 .   ? 12.054  -18.797 18.630  1.00 62.53 ? 1080 HOH B O   1 
HETATM 19025 O  O   . HOH CA 7 .   ? 4.695   -5.803  33.825  1.00 54.42 ? 1081 HOH B O   1 
HETATM 19026 O  O   . HOH CA 7 .   ? 9.612   3.268   44.473  1.00 58.76 ? 1082 HOH B O   1 
HETATM 19027 O  O   . HOH CA 7 .   ? 6.973   -3.720  40.996  1.00 36.52 ? 1083 HOH B O   1 
HETATM 19028 O  O   . HOH CA 7 .   ? 41.833  36.213  57.530  1.00 27.65 ? 1084 HOH B O   1 
HETATM 19029 O  O   . HOH CA 7 .   ? 35.196  34.317  22.271  1.00 41.83 ? 1085 HOH B O   1 
HETATM 19030 O  O   . HOH CA 7 .   ? 35.890  23.648  39.724  1.00 60.32 ? 1086 HOH B O   1 
HETATM 19031 O  O   . HOH CA 7 .   ? -2.297  16.837  26.140  1.00 57.65 ? 1087 HOH B O   1 
HETATM 19032 O  O   . HOH CA 7 .   ? 20.943  43.269  36.902  1.00 47.64 ? 1088 HOH B O   1 
HETATM 19033 O  O   . HOH CA 7 .   ? -5.380  23.152  27.899  1.00 38.28 ? 1089 HOH B O   1 
HETATM 19034 O  O   . HOH CA 7 .   ? 27.696  50.492  55.127  1.00 44.84 ? 1090 HOH B O   1 
HETATM 19035 O  O   . HOH CA 7 .   ? 12.027  -9.812  20.681  1.00 39.02 ? 1091 HOH B O   1 
HETATM 19036 O  O   . HOH CA 7 .   ? 34.244  44.904  63.526  1.00 49.20 ? 1092 HOH B O   1 
HETATM 19037 O  O   . HOH CA 7 .   ? -13.154 -10.013 20.956  1.00 50.08 ? 1093 HOH B O   1 
HETATM 19038 O  O   . HOH CA 7 .   ? -6.785  29.773  32.185  1.00 49.73 ? 1094 HOH B O   1 
HETATM 19039 O  O   . HOH CA 7 .   ? 9.116   14.160  47.822  1.00 48.62 ? 1095 HOH B O   1 
HETATM 19040 O  O   . HOH CA 7 .   ? 40.808  29.668  67.739  1.00 42.98 ? 1096 HOH B O   1 
HETATM 19041 O  O   . HOH CA 7 .   ? 13.843  6.047   26.838  1.00 45.09 ? 1097 HOH B O   1 
HETATM 19042 O  O   . HOH CA 7 .   ? 43.743  29.702  56.911  1.00 53.43 ? 1098 HOH B O   1 
HETATM 19043 O  O   . HOH CA 7 .   ? 40.669  22.043  10.175  1.00 52.69 ? 1099 HOH B O   1 
HETATM 19044 O  O   . HOH CA 7 .   ? 42.778  36.021  54.039  1.00 27.19 ? 1100 HOH B O   1 
HETATM 19045 O  O   . HOH CA 7 .   ? 38.828  16.816  49.611  1.00 45.62 ? 1101 HOH B O   1 
HETATM 19046 O  O   . HOH CA 7 .   ? 16.758  9.540   49.149  1.00 36.87 ? 1102 HOH B O   1 
HETATM 19047 O  O   . HOH CA 7 .   ? 10.829  7.368   16.849  0.50 31.55 ? 1103 HOH B O   1 
HETATM 19048 O  O   . HOH CA 7 .   ? 6.923   -1.892  37.289  1.00 24.70 ? 1104 HOH B O   1 
HETATM 19049 O  O   . HOH CA 7 .   ? 25.314  47.174  56.238  1.00 52.16 ? 1105 HOH B O   1 
HETATM 19050 O  O   . HOH CA 7 .   ? 49.815  18.142  34.359  1.00 43.43 ? 1106 HOH B O   1 
HETATM 19051 O  O   . HOH CA 7 .   ? 37.868  -1.476  32.039  1.00 41.38 ? 1107 HOH B O   1 
HETATM 19052 O  O   . HOH CA 7 .   ? 40.642  27.750  59.528  1.00 39.26 ? 1108 HOH B O   1 
HETATM 19053 O  O   . HOH CA 7 .   ? 5.110   13.674  37.564  1.00 50.35 ? 1109 HOH B O   1 
HETATM 19054 O  O   . HOH CA 7 .   ? 7.268   7.457   21.848  1.00 56.60 ? 1110 HOH B O   1 
HETATM 19055 O  O   . HOH CA 7 .   ? 49.803  16.971  17.802  1.00 54.55 ? 1111 HOH B O   1 
HETATM 19056 O  O   . HOH CA 7 .   ? 31.370  29.868  12.559  1.00 59.75 ? 1112 HOH B O   1 
HETATM 19057 O  O   . HOH CA 7 .   ? 43.195  46.709  35.809  1.00 45.81 ? 1113 HOH B O   1 
HETATM 19058 O  O   . HOH CA 7 .   ? 7.143   -0.815  40.106  1.00 41.72 ? 1114 HOH B O   1 
HETATM 19059 O  O   . HOH CA 7 .   ? 46.590  23.501  31.861  1.00 51.39 ? 1115 HOH B O   1 
HETATM 19060 O  O   . HOH CA 7 .   ? 37.531  51.592  57.444  1.00 61.93 ? 1116 HOH B O   1 
HETATM 19061 O  O   . HOH CA 7 .   ? 9.174   16.282  53.522  1.00 45.72 ? 1117 HOH B O   1 
HETATM 19062 O  O   . HOH CA 7 .   ? 6.227   29.946  49.807  1.00 46.16 ? 1118 HOH B O   1 
HETATM 19063 O  O   . HOH CA 7 .   ? 25.337  34.632  33.537  1.00 44.62 ? 1119 HOH B O   1 
HETATM 19064 O  O   . HOH CA 7 .   ? 5.741   24.898  43.828  1.00 40.51 ? 1120 HOH B O   1 
HETATM 19065 O  O   . HOH CA 7 .   ? 41.379  49.242  39.478  1.00 41.38 ? 1121 HOH B O   1 
HETATM 19066 O  O   . HOH CA 7 .   ? 32.478  1.216   33.699  1.00 50.46 ? 1122 HOH B O   1 
HETATM 19067 O  O   . HOH CA 7 .   ? 42.949  44.991  33.431  1.00 60.50 ? 1123 HOH B O   1 
HETATM 19068 O  O   . HOH CA 7 .   ? 27.397  27.510  26.390  1.00 41.57 ? 1124 HOH B O   1 
HETATM 19069 O  O   . HOH CA 7 .   ? 15.388  31.796  17.332  1.00 43.45 ? 1125 HOH B O   1 
HETATM 19070 O  O   . HOH CA 7 .   ? 20.311  51.352  49.295  1.00 54.41 ? 1126 HOH B O   1 
HETATM 19071 O  O   . HOH CA 7 .   ? 7.799   13.649  13.059  1.00 58.91 ? 1127 HOH B O   1 
HETATM 19072 O  O   . HOH CA 7 .   ? 29.262  0.153   32.464  1.00 50.85 ? 1128 HOH B O   1 
HETATM 19073 O  O   . HOH CA 7 .   ? 17.790  25.966  64.303  1.00 46.04 ? 1129 HOH B O   1 
HETATM 19074 O  O   . HOH CA 7 .   ? 4.987   23.499  58.095  1.00 50.75 ? 1130 HOH B O   1 
HETATM 19075 O  O   . HOH CA 7 .   ? 5.331   13.216  13.832  1.00 58.92 ? 1131 HOH B O   1 
HETATM 19076 O  O   . HOH CA 7 .   ? 1.244   34.819  27.963  1.00 52.32 ? 1132 HOH B O   1 
HETATM 19077 O  O   . HOH CA 7 .   ? 28.543  20.731  11.050  1.00 38.12 ? 1133 HOH B O   1 
HETATM 19078 O  O   . HOH CA 7 .   ? 43.060  39.419  39.086  1.00 67.34 ? 1134 HOH B O   1 
HETATM 19079 O  O   . HOH CA 7 .   ? 19.509  8.732   52.289  1.00 52.48 ? 1135 HOH B O   1 
HETATM 19080 O  O   . HOH CA 7 .   ? 30.163  31.063  14.757  1.00 48.42 ? 1136 HOH B O   1 
HETATM 19081 O  O   . HOH CA 7 .   ? 22.337  -6.169  52.830  1.00 47.37 ? 1137 HOH B O   1 
HETATM 19082 O  O   . HOH CA 7 .   ? 21.394  9.831   10.732  1.00 44.18 ? 1138 HOH B O   1 
HETATM 19083 O  O   . HOH CA 7 .   ? 44.019  27.496  44.722  1.00 54.75 ? 1139 HOH B O   1 
HETATM 19084 O  O   . HOH CA 7 .   ? 51.604  5.616   33.671  1.00 64.81 ? 1140 HOH B O   1 
HETATM 19085 O  O   . HOH CA 7 .   ? 25.169  50.506  50.038  1.00 44.79 ? 1141 HOH B O   1 
HETATM 19086 O  O   . HOH CA 7 .   ? -5.440  25.826  35.160  1.00 51.46 ? 1142 HOH B O   1 
HETATM 19087 O  O   . HOH CA 7 .   ? 21.656  54.428  39.295  1.00 49.88 ? 1143 HOH B O   1 
HETATM 19088 O  O   . HOH CA 7 .   ? 12.788  6.870   15.915  0.50 30.89 ? 1144 HOH B O   1 
HETATM 19089 O  O   . HOH CA 7 .   ? -1.594  18.546  37.847  1.00 47.88 ? 1145 HOH B O   1 
HETATM 19090 O  O   . HOH CA 7 .   ? -3.382  29.605  29.355  1.00 47.38 ? 1146 HOH B O   1 
HETATM 19091 O  O   . HOH CA 7 .   ? 39.718  21.686  39.042  1.00 49.11 ? 1147 HOH B O   1 
HETATM 19092 O  O   . HOH CA 7 .   ? 49.419  22.791  21.771  1.00 49.85 ? 1148 HOH B O   1 
HETATM 19093 O  O   . HOH CA 7 .   ? 21.259  18.165  52.110  1.00 44.01 ? 1149 HOH B O   1 
HETATM 19094 O  O   . HOH CA 7 .   ? 32.817  44.089  65.621  1.00 54.17 ? 1150 HOH B O   1 
HETATM 19095 O  O   . HOH CA 7 .   ? 5.296   33.347  35.556  1.00 40.62 ? 1151 HOH B O   1 
HETATM 19096 O  O   . HOH CA 7 .   ? 20.805  8.475   28.970  1.00 53.47 ? 1152 HOH B O   1 
HETATM 19097 O  O   . HOH CA 7 .   ? 44.944  37.818  50.218  1.00 51.22 ? 1153 HOH B O   1 
HETATM 19098 O  O   . HOH CA 7 .   ? 41.606  20.616  40.543  1.00 58.11 ? 1154 HOH B O   1 
HETATM 19099 O  O   . HOH CA 7 .   ? 19.053  -11.521 51.531  1.00 50.28 ? 1155 HOH B O   1 
HETATM 19100 O  O   . HOH CA 7 .   ? 35.461  39.229  66.680  1.00 40.81 ? 1156 HOH B O   1 
HETATM 19101 O  O   . HOH CA 7 .   ? 30.445  38.430  34.163  1.00 37.25 ? 1157 HOH B O   1 
HETATM 19102 O  O   . HOH CA 7 .   ? 39.943  23.914  11.668  1.00 44.86 ? 1158 HOH B O   1 
HETATM 19103 O  O   . HOH CA 7 .   ? 7.567   10.195  28.237  1.00 45.72 ? 1159 HOH B O   1 
HETATM 19104 O  O   . HOH CA 7 .   ? 12.515  38.603  47.502  1.00 45.61 ? 1160 HOH B O   1 
HETATM 19105 O  O   . HOH CA 7 .   ? 16.974  19.437  54.470  1.00 57.15 ? 1161 HOH B O   1 
HETATM 19106 O  O   . HOH CA 7 .   ? 35.297  24.417  11.005  1.00 45.52 ? 1162 HOH B O   1 
HETATM 19107 O  O   . HOH CA 7 .   ? 27.870  20.471  39.719  1.00 48.38 ? 1163 HOH B O   1 
HETATM 19108 O  O   . HOH CA 7 .   ? -1.818  19.399  29.080  1.00 45.72 ? 1164 HOH B O   1 
HETATM 19109 O  O   . HOH CA 7 .   ? 0.348   -12.276 32.610  1.00 49.30 ? 1165 HOH B O   1 
HETATM 19110 O  O   . HOH CA 7 .   ? -4.054  -9.098  26.343  1.00 45.44 ? 1166 HOH B O   1 
HETATM 19111 O  O   . HOH CA 7 .   ? 29.061  -4.613  35.739  1.00 49.31 ? 1167 HOH B O   1 
HETATM 19112 O  O   . HOH CA 7 .   ? 19.142  27.771  62.388  1.00 40.51 ? 1168 HOH B O   1 
HETATM 19113 O  O   . HOH CA 7 .   ? 39.177  26.211  41.382  1.00 47.18 ? 1169 HOH B O   1 
HETATM 19114 O  O   . HOH CA 7 .   ? 43.229  30.919  42.188  1.00 42.80 ? 1170 HOH B O   1 
HETATM 19115 O  O   . HOH CA 7 .   ? 43.704  32.472  61.642  1.00 48.96 ? 1171 HOH B O   1 
HETATM 19116 O  O   . HOH CA 7 .   ? 1.508   13.176  26.845  1.00 40.19 ? 1172 HOH B O   1 
HETATM 19117 O  O   . HOH CA 7 .   ? 28.897  27.432  12.429  1.00 40.40 ? 1173 HOH B O   1 
HETATM 19118 O  O   . HOH CA 7 .   ? 48.141  23.340  17.885  1.00 41.18 ? 1174 HOH B O   1 
HETATM 19119 O  O   . HOH CA 7 .   ? 2.579   -6.929  32.810  1.00 47.80 ? 1175 HOH B O   1 
HETATM 19120 O  O   . HOH CA 7 .   ? 33.108  18.545  60.010  1.00 45.13 ? 1176 HOH B O   1 
HETATM 19121 O  O   . HOH CA 7 .   ? 47.147  18.510  34.923  1.00 57.58 ? 1177 HOH B O   1 
HETATM 19122 O  O   . HOH CA 7 .   ? 12.525  32.449  14.039  1.00 53.52 ? 1178 HOH B O   1 
HETATM 19123 O  O   . HOH CA 7 .   ? 35.328  57.399  48.196  1.00 44.67 ? 1179 HOH B O   1 
HETATM 19124 O  O   . HOH CA 7 .   ? 32.144  6.442   30.065  1.00 62.07 ? 1180 HOH B O   1 
HETATM 19125 O  O   . HOH CA 7 .   ? 23.387  1.203   50.779  1.00 45.90 ? 1181 HOH B O   1 
HETATM 19126 O  O   . HOH CA 7 .   ? 35.538  11.235  46.302  1.00 47.61 ? 1182 HOH B O   1 
HETATM 19127 O  O   . HOH CA 7 .   ? 21.315  38.960  56.402  1.00 40.56 ? 1183 HOH B O   1 
HETATM 19128 O  O   . HOH CA 7 .   ? 4.208   -10.169 37.186  1.00 39.56 ? 1184 HOH B O   1 
HETATM 19129 O  O   . HOH CA 7 .   ? 24.822  14.336  53.850  1.00 51.96 ? 1185 HOH B O   1 
HETATM 19130 O  O   . HOH CA 7 .   ? -14.152 -14.167 10.378  1.00 38.87 ? 1186 HOH B O   1 
HETATM 19131 O  O   . HOH CA 7 .   ? 8.297   11.816  44.133  1.00 43.44 ? 1187 HOH B O   1 
HETATM 19132 O  O   . HOH CA 7 .   ? -6.995  22.122  31.582  1.00 55.16 ? 1188 HOH B O   1 
HETATM 19133 O  O   . HOH CA 7 .   ? -8.711  -17.342 18.160  1.00 46.56 ? 1189 HOH B O   1 
HETATM 19134 O  O   . HOH CA 7 .   ? 18.933  39.671  62.545  1.00 52.06 ? 1190 HOH B O   1 
HETATM 19135 O  O   . HOH CA 7 .   ? 14.070  38.175  49.772  1.00 42.66 ? 1191 HOH B O   1 
HETATM 19136 O  O   . HOH CA 7 .   ? 0.105   -16.507 33.254  1.00 45.28 ? 1192 HOH B O   1 
HETATM 19137 O  O   . HOH CA 7 .   ? 5.998   15.441  41.451  1.00 46.94 ? 1193 HOH B O   1 
HETATM 19138 O  O   . HOH CA 7 .   ? 30.056  22.587  9.790   1.00 52.27 ? 1194 HOH B O   1 
HETATM 19139 O  O   . HOH CA 7 .   ? 23.806  53.409  46.344  1.00 51.81 ? 1195 HOH B O   1 
HETATM 19140 O  O   . HOH CA 7 .   ? 47.610  49.121  52.349  1.00 42.48 ? 1196 HOH B O   1 
HETATM 19141 O  O   . HOH CA 7 .   ? 4.869   -4.738  39.853  1.00 55.69 ? 1197 HOH B O   1 
HETATM 19142 O  O   . HOH CA 7 .   ? 51.156  1.379   24.171  1.00 62.09 ? 1198 HOH B O   1 
HETATM 19143 O  O   . HOH CA 7 .   ? -1.722  16.028  36.892  1.00 44.70 ? 1199 HOH B O   1 
HETATM 19144 O  O   . HOH CA 7 .   ? 13.086  33.213  22.131  1.00 34.51 ? 1200 HOH B O   1 
HETATM 19145 O  O   . HOH CA 7 .   ? 43.909  32.494  56.462  1.00 33.26 ? 1201 HOH B O   1 
HETATM 19146 O  O   . HOH CA 7 .   ? 15.299  -6.215  51.417  1.00 47.67 ? 1202 HOH B O   1 
HETATM 19147 O  O   . HOH CA 7 .   ? 18.408  43.013  35.975  1.00 37.48 ? 1203 HOH B O   1 
HETATM 19148 O  O   . HOH CA 7 .   ? 45.521  36.006  54.674  1.00 42.82 ? 1204 HOH B O   1 
HETATM 19149 O  O   . HOH CA 7 .   ? 43.267  26.960  39.864  1.00 53.87 ? 1205 HOH B O   1 
HETATM 19150 O  O   . HOH CA 7 .   ? 5.767   32.286  18.449  1.00 49.57 ? 1206 HOH B O   1 
HETATM 19151 O  O   . HOH CA 7 .   ? 43.582  29.679  60.818  1.00 59.36 ? 1207 HOH B O   1 
HETATM 19152 O  O   . HOH CA 7 .   ? -1.527  29.021  19.462  1.00 47.89 ? 1208 HOH B O   1 
HETATM 19153 O  O   . HOH CA 7 .   ? 44.857  33.183  58.876  1.00 46.28 ? 1209 HOH B O   1 
HETATM 19154 O  O   . HOH CA 7 .   ? 3.129   -12.428 36.653  1.00 41.25 ? 1210 HOH B O   1 
HETATM 19155 O  O   . HOH CA 7 .   ? 11.908  34.818  47.027  1.00 46.97 ? 1211 HOH B O   1 
HETATM 19156 O  O   . HOH CA 7 .   ? 2.929   -16.705 37.071  1.00 46.87 ? 1212 HOH B O   1 
HETATM 19157 O  O   . HOH CA 7 .   ? 45.588  32.926  54.521  1.00 47.06 ? 1213 HOH B O   1 
HETATM 19158 O  O   . HOH CA 7 .   ? 1.866   -8.719  35.752  1.00 50.17 ? 1214 HOH B O   1 
HETATM 19159 O  O   . HOH CA 7 .   ? 13.585  -4.792  52.774  1.00 46.09 ? 1215 HOH B O   1 
HETATM 19160 O  O   . HOH DA 7 .   ? 13.616  -7.391  5.049   1.00 42.49 ? 701  HOH C O   1 
HETATM 19161 O  O   . HOH DA 7 .   ? -20.993 7.936   -12.686 1.00 52.26 ? 702  HOH C O   1 
HETATM 19162 O  O   . HOH DA 7 .   ? -5.077  13.864  -19.169 1.00 44.31 ? 703  HOH C O   1 
HETATM 19163 O  O   . HOH DA 7 .   ? -31.225 13.986  -5.345  1.00 40.99 ? 704  HOH C O   1 
HETATM 19164 O  O   . HOH DA 7 .   ? -43.116 26.013  -4.158  1.00 52.33 ? 705  HOH C O   1 
HETATM 19165 O  O   . HOH DA 7 .   ? 4.191   -0.835  3.677   1.00 52.16 ? 706  HOH C O   1 
HETATM 19166 O  O   . HOH DA 7 .   ? -30.586 35.753  -22.503 1.00 49.45 ? 707  HOH C O   1 
HETATM 19167 O  O   . HOH DA 7 .   ? -12.062 34.740  -11.164 1.00 37.56 ? 708  HOH C O   1 
HETATM 19168 O  O   . HOH DA 7 .   ? -0.648  27.574  -15.479 1.00 37.36 ? 709  HOH C O   1 
HETATM 19169 O  O   . HOH DA 7 .   ? -26.751 35.557  -16.103 1.00 42.13 ? 710  HOH C O   1 
HETATM 19170 O  O   . HOH DA 7 .   ? 44.214  7.806   9.354   1.00 35.84 ? 711  HOH C O   1 
HETATM 19171 O  O   . HOH DA 7 .   ? 8.207   16.438  13.202  1.00 46.32 ? 712  HOH C O   1 
HETATM 19172 O  O   . HOH DA 7 .   ? -1.120  -1.986  -4.575  1.00 58.50 ? 713  HOH C O   1 
HETATM 19173 O  O   . HOH DA 7 .   ? 5.476   28.330  -10.161 1.00 46.19 ? 714  HOH C O   1 
HETATM 19174 O  O   . HOH DA 7 .   ? -26.819 11.267  -4.439  1.00 49.53 ? 715  HOH C O   1 
HETATM 19175 O  O   . HOH DA 7 .   ? 5.850   3.654   -21.142 1.00 33.95 ? 716  HOH C O   1 
HETATM 19176 O  O   . HOH DA 7 .   ? -11.803 5.907   -5.676  1.00 40.29 ? 717  HOH C O   1 
HETATM 19177 O  O   . HOH DA 7 .   ? 12.668  9.051   -17.272 1.00 38.92 ? 718  HOH C O   1 
HETATM 19178 O  O   . HOH DA 7 .   ? -6.883  10.817  20.847  1.00 31.57 ? 719  HOH C O   1 
HETATM 19179 O  O   . HOH DA 7 .   ? -12.819 8.907   -4.671  1.00 37.22 ? 720  HOH C O   1 
HETATM 19180 O  O   . HOH DA 7 .   ? -22.176 2.037   -2.692  1.00 32.23 ? 721  HOH C O   1 
HETATM 19181 O  O   . HOH DA 7 .   ? -16.101 43.596  -17.290 1.00 42.11 ? 722  HOH C O   1 
HETATM 19182 O  O   . HOH DA 7 .   ? -11.387 33.246  5.545   1.00 44.65 ? 723  HOH C O   1 
HETATM 19183 O  O   . HOH DA 7 .   ? -26.485 8.680   -10.610 1.00 42.79 ? 724  HOH C O   1 
HETATM 19184 O  O   . HOH DA 7 .   ? 3.571   22.418  16.682  1.00 43.49 ? 725  HOH C O   1 
HETATM 19185 O  O   . HOH DA 7 .   ? 2.713   -6.986  -0.019  1.00 24.73 ? 726  HOH C O   1 
HETATM 19186 O  O   . HOH DA 7 .   ? -39.754 19.619  -12.218 1.00 43.44 ? 727  HOH C O   1 
HETATM 19187 O  O   . HOH DA 7 .   ? 9.012   34.276  -0.997  1.00 55.94 ? 728  HOH C O   1 
HETATM 19188 O  O   . HOH DA 7 .   ? -8.164  18.657  -23.810 1.00 49.40 ? 729  HOH C O   1 
HETATM 19189 O  O   . HOH DA 7 .   ? -17.967 42.020  -5.026  1.00 64.11 ? 730  HOH C O   1 
HETATM 19190 O  O   . HOH DA 7 .   ? -6.629  22.421  -18.719 1.00 40.57 ? 731  HOH C O   1 
HETATM 19191 O  O   . HOH DA 7 .   ? 14.269  11.958  -8.729  1.00 28.24 ? 732  HOH C O   1 
HETATM 19192 O  O   . HOH DA 7 .   ? -20.606 30.325  -12.575 1.00 43.15 ? 733  HOH C O   1 
HETATM 19193 O  O   . HOH DA 7 .   ? -8.499  -1.770  -4.829  1.00 51.67 ? 734  HOH C O   1 
HETATM 19194 O  O   . HOH DA 7 .   ? -24.854 41.942  -17.941 1.00 37.87 ? 735  HOH C O   1 
HETATM 19195 O  O   . HOH DA 7 .   ? -18.968 -14.601 -6.931  1.00 41.31 ? 736  HOH C O   1 
HETATM 19196 O  O   . HOH DA 7 .   ? 0.994   35.384  8.976   1.00 42.29 ? 737  HOH C O   1 
HETATM 19197 O  O   . HOH DA 7 .   ? 30.788  -1.707  -15.156 1.00 46.86 ? 738  HOH C O   1 
HETATM 19198 O  O   . HOH DA 7 .   ? -35.793 18.467  -26.865 1.00 49.72 ? 739  HOH C O   1 
HETATM 19199 O  O   . HOH DA 7 .   ? -3.304  0.813   -5.114  1.00 36.24 ? 740  HOH C O   1 
HETATM 19200 O  O   . HOH DA 7 .   ? -3.005  32.806  0.854   1.00 29.33 ? 741  HOH C O   1 
HETATM 19201 O  O   . HOH DA 7 .   ? -9.429  34.643  10.312  1.00 53.31 ? 742  HOH C O   1 
HETATM 19202 O  O   . HOH DA 7 .   ? -14.307 35.766  -9.198  1.00 55.44 ? 743  HOH C O   1 
HETATM 19203 O  O   . HOH DA 7 .   ? 9.142   25.034  17.754  1.00 31.37 ? 744  HOH C O   1 
HETATM 19204 O  O   . HOH DA 7 .   ? 1.349   14.952  -19.996 1.00 44.57 ? 745  HOH C O   1 
HETATM 19205 O  O   . HOH DA 7 .   ? -12.249 22.708  17.247  1.00 34.27 ? 746  HOH C O   1 
HETATM 19206 O  O   . HOH DA 7 .   ? -0.918  1.395   23.147  1.00 47.33 ? 747  HOH C O   1 
HETATM 19207 O  O   . HOH DA 7 .   ? 4.123   24.722  18.316  1.00 38.69 ? 748  HOH C O   1 
HETATM 19208 O  O   . HOH DA 7 .   ? 35.521  11.302  3.376   1.00 38.12 ? 749  HOH C O   1 
HETATM 19209 O  O   . HOH DA 7 .   ? 6.717   37.267  6.412   1.00 50.45 ? 750  HOH C O   1 
HETATM 19210 O  O   . HOH DA 7 .   ? -27.658 14.714  1.228   1.00 50.92 ? 751  HOH C O   1 
HETATM 19211 O  O   . HOH DA 7 .   ? -11.369 17.880  -33.338 1.00 46.59 ? 752  HOH C O   1 
HETATM 19212 O  O   . HOH DA 7 .   ? -1.190  18.341  -19.506 1.00 29.29 ? 753  HOH C O   1 
HETATM 19213 O  O   . HOH DA 7 .   ? -35.191 18.512  -30.915 1.00 30.49 ? 754  HOH C O   1 
HETATM 19214 O  O   . HOH DA 7 .   ? 12.614  6.498   0.172   1.00 32.41 ? 755  HOH C O   1 
HETATM 19215 O  O   . HOH DA 7 .   ? -20.018 3.992   4.065   1.00 23.43 ? 756  HOH C O   1 
HETATM 19216 O  O   . HOH DA 7 .   ? -13.654 26.037  -22.707 1.00 30.13 ? 757  HOH C O   1 
HETATM 19217 O  O   . HOH DA 7 .   ? 22.496  -19.491 6.250   1.00 43.49 ? 758  HOH C O   1 
HETATM 19218 O  O   . HOH DA 7 .   ? -18.681 7.219   14.715  1.00 31.03 ? 759  HOH C O   1 
HETATM 19219 O  O   . HOH DA 7 .   ? -18.842 9.772   -0.461  1.00 39.48 ? 760  HOH C O   1 
HETATM 19220 O  O   . HOH DA 7 .   ? -14.013 33.598  -4.421  1.00 36.12 ? 761  HOH C O   1 
HETATM 19221 O  O   . HOH DA 7 .   ? -14.036 -16.594 -7.505  1.00 38.38 ? 762  HOH C O   1 
HETATM 19222 O  O   . HOH DA 7 .   ? 5.346   22.371  -14.017 1.00 42.32 ? 763  HOH C O   1 
HETATM 19223 O  O   . HOH DA 7 .   ? -21.619 39.517  2.023   1.00 41.96 ? 764  HOH C O   1 
HETATM 19224 O  O   . HOH DA 7 .   ? -18.538 9.689   19.341  1.00 42.53 ? 765  HOH C O   1 
HETATM 19225 O  O   . HOH DA 7 .   ? 8.870   -0.282  -25.456 1.00 42.18 ? 766  HOH C O   1 
HETATM 19226 O  O   . HOH DA 7 .   ? 12.081  4.461   -22.130 1.00 40.59 ? 767  HOH C O   1 
HETATM 19227 O  O   . HOH DA 7 .   ? -13.228 -13.767 6.004   1.00 34.13 ? 768  HOH C O   1 
HETATM 19228 O  O   . HOH DA 7 .   ? -16.167 -7.663  4.085   1.00 24.00 ? 769  HOH C O   1 
HETATM 19229 O  O   . HOH DA 7 .   ? -1.538  18.564  10.823  1.00 21.79 ? 770  HOH C O   1 
HETATM 19230 O  O   . HOH DA 7 .   ? -38.618 31.390  -6.269  1.00 47.10 ? 771  HOH C O   1 
HETATM 19231 O  O   . HOH DA 7 .   ? -1.228  34.457  0.041   1.00 43.91 ? 772  HOH C O   1 
HETATM 19232 O  O   . HOH DA 7 .   ? 28.843  10.773  0.448   1.00 39.28 ? 773  HOH C O   1 
HETATM 19233 O  O   . HOH DA 7 .   ? -3.041  6.495   -19.133 1.00 47.25 ? 774  HOH C O   1 
HETATM 19234 O  O   . HOH DA 7 .   ? 14.006  17.809  -8.185  1.00 59.62 ? 775  HOH C O   1 
HETATM 19235 O  O   . HOH DA 7 .   ? -11.898 -19.688 0.565   1.00 46.62 ? 776  HOH C O   1 
HETATM 19236 O  O   . HOH DA 7 .   ? 36.357  1.325   -4.844  1.00 30.23 ? 777  HOH C O   1 
HETATM 19237 O  O   . HOH DA 7 .   ? 57.598  3.801   24.921  1.00 57.92 ? 778  HOH C O   1 
HETATM 19238 O  O   . HOH DA 7 .   ? 1.835   3.611   20.654  1.00 53.31 ? 779  HOH C O   1 
HETATM 19239 O  O   . HOH DA 7 .   ? -12.976 1.332   -12.623 1.00 47.88 ? 780  HOH C O   1 
HETATM 19240 O  O   . HOH DA 7 .   ? 9.104   -0.442  13.452  1.00 51.00 ? 781  HOH C O   1 
HETATM 19241 O  O   . HOH DA 7 .   ? -35.001 24.912  -26.189 1.00 36.20 ? 782  HOH C O   1 
HETATM 19242 O  O   . HOH DA 7 .   ? -15.519 -0.053  18.597  1.00 27.42 ? 783  HOH C O   1 
HETATM 19243 O  O   . HOH DA 7 .   ? -30.300 36.492  -5.052  1.00 37.11 ? 784  HOH C O   1 
HETATM 19244 O  O   . HOH DA 7 .   ? 28.928  -6.765  -8.627  1.00 44.36 ? 785  HOH C O   1 
HETATM 19245 O  O   . HOH DA 7 .   ? 10.429  13.522  -13.351 1.00 39.53 ? 786  HOH C O   1 
HETATM 19246 O  O   . HOH DA 7 .   ? 7.065   -4.873  -10.606 1.00 38.65 ? 787  HOH C O   1 
HETATM 19247 O  O   . HOH DA 7 .   ? 11.497  32.401  -1.743  1.00 49.87 ? 788  HOH C O   1 
HETATM 19248 O  O   . HOH DA 7 .   ? -17.675 -11.934 10.102  1.00 40.41 ? 789  HOH C O   1 
HETATM 19249 O  O   . HOH DA 7 .   ? -26.128 -2.059  0.180   1.00 53.44 ? 790  HOH C O   1 
HETATM 19250 O  O   . HOH DA 7 .   ? -12.479 15.869  -27.668 1.00 41.89 ? 791  HOH C O   1 
HETATM 19251 O  O   . HOH DA 7 .   ? 0.043   -4.464  18.999  1.00 29.52 ? 792  HOH C O   1 
HETATM 19252 O  O   . HOH DA 7 .   ? -12.222 -9.177  23.218  1.00 42.09 ? 793  HOH C O   1 
HETATM 19253 O  O   . HOH DA 7 .   ? 24.578  5.648   -9.322  1.00 25.70 ? 794  HOH C O   1 
HETATM 19254 O  O   . HOH DA 7 .   ? -21.509 9.501   -4.241  1.00 43.09 ? 795  HOH C O   1 
HETATM 19255 O  O   . HOH DA 7 .   ? -25.250 15.187  -25.341 1.00 46.37 ? 796  HOH C O   1 
HETATM 19256 O  O   . HOH DA 7 .   ? 19.743  -11.230 0.664   1.00 44.20 ? 797  HOH C O   1 
HETATM 19257 O  O   . HOH DA 7 .   ? -15.705 -4.251  3.756   1.00 35.47 ? 798  HOH C O   1 
HETATM 19258 O  O   . HOH DA 7 .   ? -0.564  32.285  -7.974  1.00 52.93 ? 799  HOH C O   1 
HETATM 19259 O  O   . HOH DA 7 .   ? -32.901 24.489  -27.464 1.00 32.93 ? 800  HOH C O   1 
HETATM 19260 O  O   . HOH DA 7 .   ? 34.124  8.037   2.210   1.00 29.54 ? 801  HOH C O   1 
HETATM 19261 O  O   . HOH DA 7 .   ? -9.736  11.271  20.958  1.00 39.87 ? 802  HOH C O   1 
HETATM 19262 O  O   . HOH DA 7 .   ? 20.913  11.688  -6.652  1.00 46.83 ? 803  HOH C O   1 
HETATM 19263 O  O   . HOH DA 7 .   ? -6.668  14.540  13.752  1.00 19.45 ? 804  HOH C O   1 
HETATM 19264 O  O   . HOH DA 7 .   ? -38.416 34.344  -21.712 1.00 59.61 ? 805  HOH C O   1 
HETATM 19265 O  O   . HOH DA 7 .   ? -13.336 -7.973  19.055  1.00 32.25 ? 806  HOH C O   1 
HETATM 19266 O  O   . HOH DA 7 .   ? -25.428 36.526  -26.907 1.00 44.83 ? 807  HOH C O   1 
HETATM 19267 O  O   . HOH DA 7 .   ? -0.842  -2.267  21.714  1.00 48.40 ? 808  HOH C O   1 
HETATM 19268 O  O   . HOH DA 7 .   ? -17.835 15.391  17.856  1.00 52.73 ? 809  HOH C O   1 
HETATM 19269 O  O   . HOH DA 7 .   ? -21.126 -7.461  20.042  1.00 53.21 ? 810  HOH C O   1 
HETATM 19270 O  O   . HOH DA 7 .   ? -6.182  4.374   21.810  1.00 40.39 ? 811  HOH C O   1 
HETATM 19271 O  O   . HOH DA 7 .   ? -12.127 4.592   -8.111  1.00 38.20 ? 812  HOH C O   1 
HETATM 19272 O  O   . HOH DA 7 .   ? -37.783 19.401  -23.110 1.00 52.29 ? 813  HOH C O   1 
HETATM 19273 O  O   . HOH DA 7 .   ? -11.486 24.124  -20.014 1.00 30.69 ? 814  HOH C O   1 
HETATM 19274 O  O   . HOH DA 7 .   ? -18.844 20.491  14.142  1.00 59.07 ? 815  HOH C O   1 
HETATM 19275 O  O   . HOH DA 7 .   ? 1.381   29.722  -13.493 1.00 53.57 ? 816  HOH C O   1 
HETATM 19276 O  O   . HOH DA 7 .   ? -18.305 34.987  -28.610 1.00 45.78 ? 817  HOH C O   1 
HETATM 19277 O  O   . HOH DA 7 .   ? 51.548  15.142  20.527  1.00 49.72 ? 818  HOH C O   1 
HETATM 19278 O  O   . HOH DA 7 .   ? -34.020 28.391  -26.034 1.00 38.49 ? 819  HOH C O   1 
HETATM 19279 O  O   . HOH DA 7 .   ? -8.678  0.534   20.886  1.00 26.33 ? 820  HOH C O   1 
HETATM 19280 O  O   . HOH DA 7 .   ? -41.441 15.546  -6.803  1.00 47.74 ? 821  HOH C O   1 
HETATM 19281 O  O   . HOH DA 7 .   ? -12.145 12.174  -4.261  1.00 34.80 ? 822  HOH C O   1 
HETATM 19282 O  O   . HOH DA 7 .   ? 6.465   0.665   6.588   1.00 61.06 ? 823  HOH C O   1 
HETATM 19283 O  O   . HOH DA 7 .   ? -16.419 9.674   0.859   1.00 24.72 ? 824  HOH C O   1 
HETATM 19284 O  O   . HOH DA 7 .   ? -17.695 -9.545  12.996  1.00 47.28 ? 825  HOH C O   1 
HETATM 19285 O  O   . HOH DA 7 .   ? -33.551 24.287  -6.899  1.00 30.69 ? 826  HOH C O   1 
HETATM 19286 O  O   . HOH DA 7 .   ? -13.251 9.081   18.567  1.00 26.49 ? 827  HOH C O   1 
HETATM 19287 O  O   . HOH DA 7 .   ? 9.333   9.768   9.636   1.00 34.43 ? 828  HOH C O   1 
HETATM 19288 O  O   . HOH DA 7 .   ? 10.560  17.293  9.529   1.00 50.99 ? 829  HOH C O   1 
HETATM 19289 O  O   . HOH DA 7 .   ? -19.854 -19.637 -3.341  1.00 48.04 ? 830  HOH C O   1 
HETATM 19290 O  O   . HOH DA 7 .   ? 4.242   17.837  -12.671 1.00 26.37 ? 831  HOH C O   1 
HETATM 19291 O  O   . HOH DA 7 .   ? 0.600   13.618  13.237  1.00 27.21 ? 832  HOH C O   1 
HETATM 19292 O  O   . HOH DA 7 .   ? -30.435 39.141  2.198   1.00 60.23 ? 833  HOH C O   1 
HETATM 19293 O  O   . HOH DA 7 .   ? -12.091 14.630  -12.734 1.00 42.84 ? 834  HOH C O   1 
HETATM 19294 O  O   . HOH DA 7 .   ? -7.112  18.040  15.772  1.00 20.76 ? 835  HOH C O   1 
HETATM 19295 O  O   . HOH DA 7 .   ? -26.328 22.515  2.205   1.00 34.89 ? 836  HOH C O   1 
HETATM 19296 O  O   . HOH DA 7 .   ? -23.790 -7.559  9.386   1.00 46.01 ? 837  HOH C O   1 
HETATM 19297 O  O   . HOH DA 7 .   ? 23.479  6.923   -6.268  1.00 49.79 ? 838  HOH C O   1 
HETATM 19298 O  O   . HOH DA 7 .   ? -6.107  -2.474  21.737  1.00 32.46 ? 839  HOH C O   1 
HETATM 19299 O  O   . HOH DA 7 .   ? -38.837 32.356  -17.743 1.00 46.37 ? 840  HOH C O   1 
HETATM 19300 O  O   . HOH DA 7 .   ? 26.587  -8.801  2.445   1.00 47.41 ? 841  HOH C O   1 
HETATM 19301 O  O   . HOH DA 7 .   ? 6.440   29.274  -6.520  1.00 45.33 ? 842  HOH C O   1 
HETATM 19302 O  O   . HOH DA 7 .   ? -16.959 14.126  -17.381 1.00 39.27 ? 843  HOH C O   1 
HETATM 19303 O  O   . HOH DA 7 .   ? -31.880 29.674  1.158   1.00 35.47 ? 844  HOH C O   1 
HETATM 19304 O  O   . HOH DA 7 .   ? -20.941 -7.172  12.790  1.00 25.25 ? 845  HOH C O   1 
HETATM 19305 O  O   . HOH DA 7 .   ? 11.799  20.249  9.039   1.00 70.82 ? 846  HOH C O   1 
HETATM 19306 O  O   . HOH DA 7 .   ? -15.708 3.672   20.245  1.00 29.37 ? 847  HOH C O   1 
HETATM 19307 O  O   . HOH DA 7 .   ? -7.452  28.160  15.185  1.00 49.12 ? 848  HOH C O   1 
HETATM 19308 O  O   . HOH DA 7 .   ? -18.011 34.215  -6.444  1.00 36.57 ? 849  HOH C O   1 
HETATM 19309 O  O   . HOH DA 7 .   ? -10.001 35.396  6.214   1.00 59.15 ? 850  HOH C O   1 
HETATM 19310 O  O   . HOH DA 7 .   ? -3.396  -2.139  22.962  1.00 53.06 ? 851  HOH C O   1 
HETATM 19311 O  O   . HOH DA 7 .   ? 10.994  13.504  -10.461 1.00 34.72 ? 852  HOH C O   1 
HETATM 19312 O  O   . HOH DA 7 .   ? -31.283 15.657  6.152   1.00 48.81 ? 853  HOH C O   1 
HETATM 19313 O  O   . HOH DA 7 .   ? -25.876 27.431  -30.862 1.00 49.73 ? 854  HOH C O   1 
HETATM 19314 O  O   . HOH DA 7 .   ? 0.661   33.392  12.788  1.00 33.36 ? 855  HOH C O   1 
HETATM 19315 O  O   . HOH DA 7 .   ? -8.911  25.687  9.322   1.00 23.95 ? 856  HOH C O   1 
HETATM 19316 O  O   . HOH DA 7 .   ? 17.460  13.425  -2.050  1.00 47.33 ? 857  HOH C O   1 
HETATM 19317 O  O   . HOH DA 7 .   ? -32.495 32.583  -9.074  1.00 46.13 ? 858  HOH C O   1 
HETATM 19318 O  O   . HOH DA 7 .   ? -8.540  26.773  -12.329 1.00 39.02 ? 859  HOH C O   1 
HETATM 19319 O  O   . HOH DA 7 .   ? 1.092   18.389  11.298  1.00 21.30 ? 860  HOH C O   1 
HETATM 19320 O  O   . HOH DA 7 .   ? -28.494 -5.651  2.033   1.00 57.31 ? 861  HOH C O   1 
HETATM 19321 O  O   . HOH DA 7 .   ? -4.314  12.190  -15.545 1.00 45.24 ? 862  HOH C O   1 
HETATM 19322 O  O   . HOH DA 7 .   ? -26.706 34.173  -27.474 1.00 46.65 ? 863  HOH C O   1 
HETATM 19323 O  O   . HOH DA 7 .   ? -7.939  -6.754  10.923  1.00 26.05 ? 864  HOH C O   1 
HETATM 19324 O  O   . HOH DA 7 .   ? -15.002 31.713  -28.887 1.00 53.04 ? 865  HOH C O   1 
HETATM 19325 O  O   . HOH DA 7 .   ? -29.888 30.814  4.660   1.00 50.70 ? 866  HOH C O   1 
HETATM 19326 O  O   . HOH DA 7 .   ? 4.857   16.260  -16.429 1.00 40.20 ? 867  HOH C O   1 
HETATM 19327 O  O   . HOH DA 7 .   ? -6.879  20.108  -17.124 1.00 34.45 ? 868  HOH C O   1 
HETATM 19328 O  O   . HOH DA 7 .   ? -5.233  33.260  -13.480 1.00 35.97 ? 869  HOH C O   1 
HETATM 19329 O  O   . HOH DA 7 .   ? 5.339   4.406   -0.861  1.00 46.93 ? 870  HOH C O   1 
HETATM 19330 O  O   . HOH DA 7 .   ? -40.388 19.700  -9.466  1.00 42.70 ? 871  HOH C O   1 
HETATM 19331 O  O   . HOH DA 7 .   ? -15.310 29.450  -25.863 1.00 32.47 ? 872  HOH C O   1 
HETATM 19332 O  O   . HOH DA 7 .   ? -22.527 32.367  -19.001 1.00 30.21 ? 873  HOH C O   1 
HETATM 19333 O  O   . HOH DA 7 .   ? 1.557   -7.271  -15.030 1.00 46.40 ? 874  HOH C O   1 
HETATM 19334 O  O   . HOH DA 7 .   ? 29.950  6.617   -3.744  1.00 30.14 ? 875  HOH C O   1 
HETATM 19335 O  O   . HOH DA 7 .   ? -24.138 -11.214 6.911   1.00 38.56 ? 876  HOH C O   1 
HETATM 19336 O  O   . HOH DA 7 .   ? -22.170 28.046  2.159   1.00 32.41 ? 877  HOH C O   1 
HETATM 19337 O  O   . HOH DA 7 .   ? -28.345 33.773  -18.010 1.00 28.56 ? 878  HOH C O   1 
HETATM 19338 O  O   . HOH DA 7 .   ? -1.684  2.511   -6.557  1.00 28.96 ? 879  HOH C O   1 
HETATM 19339 O  O   . HOH DA 7 .   ? 12.156  -2.017  -15.308 1.00 37.89 ? 880  HOH C O   1 
HETATM 19340 O  O   . HOH DA 7 .   ? -17.572 -1.359  17.445  1.00 28.65 ? 881  HOH C O   1 
HETATM 19341 O  O   . HOH DA 7 .   ? 32.022  -5.717  -0.323  1.00 24.64 ? 882  HOH C O   1 
HETATM 19342 O  O   . HOH DA 7 .   ? -23.302 -1.235  0.053   1.00 33.35 ? 883  HOH C O   1 
HETATM 19343 O  O   . HOH DA 7 .   ? 3.755   35.932  5.408   1.00 41.94 ? 884  HOH C O   1 
HETATM 19344 O  O   . HOH DA 7 .   ? -21.206 17.422  6.698   1.00 30.52 ? 885  HOH C O   1 
HETATM 19345 O  O   . HOH DA 7 .   ? 0.713   34.430  6.326   1.00 28.60 ? 886  HOH C O   1 
HETATM 19346 O  O   . HOH DA 7 .   ? -20.487 -15.930 2.631   1.00 55.60 ? 887  HOH C O   1 
HETATM 19347 O  O   . HOH DA 7 .   ? -25.035 27.498  1.620   1.00 37.11 ? 888  HOH C O   1 
HETATM 19348 O  O   . HOH DA 7 .   ? -6.645  35.117  -22.051 1.00 48.42 ? 889  HOH C O   1 
HETATM 19349 O  O   . HOH DA 7 .   ? -22.178 0.289   7.571   1.00 26.93 ? 890  HOH C O   1 
HETATM 19350 O  O   . HOH DA 7 .   ? 2.922   17.593  15.057  1.00 45.95 ? 891  HOH C O   1 
HETATM 19351 O  O   . HOH DA 7 .   ? -6.295  25.232  -27.820 1.00 40.93 ? 892  HOH C O   1 
HETATM 19352 O  O   . HOH DA 7 .   ? 23.460  12.471  -0.546  1.00 40.26 ? 893  HOH C O   1 
HETATM 19353 O  O   . HOH DA 7 .   ? -25.473 6.982   1.943   1.00 32.41 ? 894  HOH C O   1 
HETATM 19354 O  O   . HOH DA 7 .   ? 2.906   -2.191  -3.924  1.00 61.32 ? 895  HOH C O   1 
HETATM 19355 O  O   . HOH DA 7 .   ? 3.837   5.044   7.250   1.00 22.82 ? 896  HOH C O   1 
HETATM 19356 O  O   . HOH DA 7 .   ? 13.880  34.045  1.943   1.00 62.63 ? 897  HOH C O   1 
HETATM 19357 O  O   . HOH DA 7 .   ? 6.278   20.474  14.653  1.00 38.68 ? 898  HOH C O   1 
HETATM 19358 O  O   . HOH DA 7 .   ? -16.168 12.097  5.825   1.00 20.34 ? 899  HOH C O   1 
HETATM 19359 O  O   . HOH DA 7 .   ? -22.218 11.542  -26.972 1.00 51.58 ? 900  HOH C O   1 
HETATM 19360 O  O   . HOH DA 7 .   ? -13.431 38.917  -13.987 1.00 48.17 ? 901  HOH C O   1 
HETATM 19361 O  O   . HOH DA 7 .   ? -1.478  30.702  12.976  1.00 27.68 ? 902  HOH C O   1 
HETATM 19362 O  O   . HOH DA 7 .   ? -26.581 24.151  -32.730 1.00 49.24 ? 903  HOH C O   1 
HETATM 19363 O  O   . HOH DA 7 .   ? -43.650 17.251  -7.139  1.00 52.33 ? 904  HOH C O   1 
HETATM 19364 O  O   . HOH DA 7 .   ? -16.813 18.429  14.785  1.00 37.24 ? 905  HOH C O   1 
HETATM 19365 O  O   . HOH DA 7 .   ? -10.905 19.339  10.422  1.00 21.20 ? 906  HOH C O   1 
HETATM 19366 O  O   . HOH DA 7 .   ? -12.165 15.942  -30.222 1.00 53.20 ? 907  HOH C O   1 
HETATM 19367 O  O   . HOH DA 7 .   ? -5.988  24.516  13.175  1.00 21.97 ? 908  HOH C O   1 
HETATM 19368 O  O   . HOH DA 7 .   ? -32.707 23.287  -30.105 1.00 33.69 ? 909  HOH C O   1 
HETATM 19369 O  O   . HOH DA 7 .   ? -2.525  20.222  -5.120  1.00 22.55 ? 910  HOH C O   1 
HETATM 19370 O  O   . HOH DA 7 .   ? -7.725  33.380  -8.031  1.00 34.52 ? 911  HOH C O   1 
HETATM 19371 O  O   . HOH DA 7 .   ? -5.657  11.679  -12.526 1.00 54.58 ? 912  HOH C O   1 
HETATM 19372 O  O   . HOH DA 7 .   ? 21.309  -8.497  0.632   1.00 47.45 ? 913  HOH C O   1 
HETATM 19373 O  O   . HOH DA 7 .   ? 3.444   25.023  -18.731 1.00 47.30 ? 914  HOH C O   1 
HETATM 19374 O  O   . HOH DA 7 .   ? 2.739   7.397   -0.247  1.00 25.65 ? 915  HOH C O   1 
HETATM 19375 O  O   . HOH DA 7 .   ? -14.467 39.466  -21.584 1.00 44.45 ? 916  HOH C O   1 
HETATM 19376 O  O   . HOH DA 7 .   ? 2.253   -5.693  -7.914  1.00 44.12 ? 917  HOH C O   1 
HETATM 19377 O  O   . HOH DA 7 .   ? 40.796  14.579  7.724   1.00 36.22 ? 918  HOH C O   1 
HETATM 19378 O  O   . HOH DA 7 .   ? -33.425 14.013  -1.916  1.00 51.31 ? 919  HOH C O   1 
HETATM 19379 O  O   . HOH DA 7 .   ? -16.789 25.982  -37.878 1.00 57.13 ? 920  HOH C O   1 
HETATM 19380 O  O   . HOH DA 7 .   ? 6.892   33.596  0.271   1.00 47.14 ? 921  HOH C O   1 
HETATM 19381 O  O   . HOH DA 7 .   ? -25.728 12.586  6.313   1.00 47.70 ? 922  HOH C O   1 
HETATM 19382 O  O   . HOH DA 7 .   ? -13.403 3.584   -11.275 1.00 45.54 ? 923  HOH C O   1 
HETATM 19383 O  O   . HOH DA 7 .   ? 1.064   -0.342  -24.139 1.00 39.01 ? 924  HOH C O   1 
HETATM 19384 O  O   . HOH DA 7 .   ? -16.347 -2.465  5.234   1.00 25.59 ? 925  HOH C O   1 
HETATM 19385 O  O   . HOH DA 7 .   ? -22.048 -7.752  -7.456  1.00 43.89 ? 926  HOH C O   1 
HETATM 19386 O  O   . HOH DA 7 .   ? -23.419 6.698   -11.980 1.00 55.52 ? 927  HOH C O   1 
HETATM 19387 O  O   . HOH DA 7 .   ? -12.969 19.626  7.166   1.00 23.95 ? 928  HOH C O   1 
HETATM 19388 O  O   . HOH DA 7 .   ? -0.930  21.127  16.270  1.00 23.24 ? 929  HOH C O   1 
HETATM 19389 O  O   . HOH DA 7 .   ? -32.118 16.172  -20.130 1.00 31.48 ? 930  HOH C O   1 
HETATM 19390 O  O   . HOH DA 7 .   ? 25.707  4.690   5.090   1.00 48.01 ? 931  HOH C O   1 
HETATM 19391 O  O   . HOH DA 7 .   ? -6.609  34.917  -1.172  1.00 46.56 ? 932  HOH C O   1 
HETATM 19392 O  O   . HOH DA 7 .   ? -20.269 0.864   5.568   1.00 22.04 ? 933  HOH C O   1 
HETATM 19393 O  O   . HOH DA 7 .   ? -16.169 36.074  -7.279  1.00 54.12 ? 934  HOH C O   1 
HETATM 19394 O  O   . HOH DA 7 .   ? 25.383  -2.963  4.732   1.00 38.59 ? 935  HOH C O   1 
HETATM 19395 O  O   . HOH DA 7 .   ? -24.673 15.534  -7.203  1.00 28.43 ? 936  HOH C O   1 
HETATM 19396 O  O   . HOH DA 7 .   ? -15.951 25.404  7.821   1.00 32.61 ? 937  HOH C O   1 
HETATM 19397 O  O   . HOH DA 7 .   ? 14.678  3.907   -2.727  1.00 21.39 ? 938  HOH C O   1 
HETATM 19398 O  O   . HOH DA 7 .   ? -10.922 2.548   -9.636  1.00 39.69 ? 939  HOH C O   1 
HETATM 19399 O  O   . HOH DA 7 .   ? -25.826 -4.235  5.365   1.00 36.10 ? 940  HOH C O   1 
HETATM 19400 O  O   . HOH DA 7 .   ? -2.974  12.470  21.301  1.00 43.72 ? 941  HOH C O   1 
HETATM 19401 O  O   . HOH DA 7 .   ? 32.992  8.335   9.778   1.00 24.72 ? 942  HOH C O   1 
HETATM 19402 O  O   . HOH DA 7 .   ? -2.421  29.533  16.432  1.00 49.55 ? 943  HOH C O   1 
HETATM 19403 O  O   . HOH DA 7 .   ? 17.101  16.355  10.399  1.00 51.03 ? 944  HOH C O   1 
HETATM 19404 O  O   . HOH DA 7 .   ? -30.246 7.800   -12.699 1.00 50.83 ? 945  HOH C O   1 
HETATM 19405 O  O   . HOH DA 7 .   ? -18.746 21.277  4.042   1.00 40.64 ? 946  HOH C O   1 
HETATM 19406 O  O   . HOH DA 7 .   ? 29.302  0.610   -14.758 1.00 37.11 ? 947  HOH C O   1 
HETATM 19407 O  O   . HOH DA 7 .   ? -7.218  11.850  -9.441  1.00 47.88 ? 948  HOH C O   1 
HETATM 19408 O  O   . HOH DA 7 .   ? 17.250  5.009   -2.101  1.00 26.67 ? 949  HOH C O   1 
HETATM 19409 O  O   . HOH DA 7 .   ? 22.363  8.634   -17.078 1.00 46.21 ? 950  HOH C O   1 
HETATM 19410 O  O   . HOH DA 7 .   ? -36.548 24.998  1.475   1.00 55.06 ? 951  HOH C O   1 
HETATM 19411 O  O   . HOH DA 7 .   ? 10.898  17.615  5.649   1.00 33.05 ? 952  HOH C O   1 
HETATM 19412 O  O   . HOH DA 7 .   ? -1.431  -1.114  -24.366 1.00 54.82 ? 953  HOH C O   1 
HETATM 19413 O  O   . HOH DA 7 .   ? -27.896 13.660  -25.437 1.00 43.35 ? 954  HOH C O   1 
HETATM 19414 O  O   . HOH DA 7 .   ? 29.549  -4.015  -8.753  1.00 35.54 ? 955  HOH C O   1 
HETATM 19415 O  O   . HOH DA 7 .   ? 11.005  32.556  11.693  1.00 50.91 ? 956  HOH C O   1 
HETATM 19416 O  O   . HOH DA 7 .   ? 5.538   5.201   -18.582 1.00 38.70 ? 957  HOH C O   1 
HETATM 19417 O  O   . HOH DA 7 .   ? 6.032   18.250  -5.856  1.00 46.22 ? 958  HOH C O   1 
HETATM 19418 O  O   . HOH DA 7 .   ? -9.265  28.509  -28.990 1.00 59.24 ? 959  HOH C O   1 
HETATM 19419 O  O   . HOH DA 7 .   ? -25.515 12.631  -16.019 1.00 33.62 ? 960  HOH C O   1 
HETATM 19420 O  O   . HOH DA 7 .   ? -27.244 6.808   -12.842 1.00 59.37 ? 961  HOH C O   1 
HETATM 19421 O  O   . HOH DA 7 .   ? 4.236   34.454  14.458  1.00 41.15 ? 962  HOH C O   1 
HETATM 19422 O  O   . HOH DA 7 .   ? -36.394 32.746  -14.307 1.00 54.11 ? 963  HOH C O   1 
HETATM 19423 O  O   . HOH DA 7 .   ? 5.801   34.298  2.398   1.00 35.41 ? 964  HOH C O   1 
HETATM 19424 O  O   . HOH DA 7 .   ? 0.874   -9.687  -5.492  1.00 46.00 ? 965  HOH C O   1 
HETATM 19425 O  O   . HOH DA 7 .   ? -31.329 34.635  -15.391 1.00 35.05 ? 966  HOH C O   1 
HETATM 19426 O  O   . HOH DA 7 .   ? -38.511 15.486  2.257   1.00 45.70 ? 967  HOH C O   1 
HETATM 19427 O  O   . HOH DA 7 .   ? -15.335 11.532  -9.871  1.00 51.00 ? 968  HOH C O   1 
HETATM 19428 O  O   . HOH DA 7 .   ? -7.843  18.348  18.426  1.00 33.01 ? 969  HOH C O   1 
HETATM 19429 O  O   . HOH DA 7 .   ? 7.607   18.116  15.349  1.00 49.48 ? 970  HOH C O   1 
HETATM 19430 O  O   . HOH DA 7 .   ? -10.473 -12.860 -11.683 1.00 53.03 ? 971  HOH C O   1 
HETATM 19431 O  O   . HOH DA 7 .   ? 30.429  9.962   2.384   1.00 36.36 ? 972  HOH C O   1 
HETATM 19432 O  O   . HOH DA 7 .   ? -18.788 13.127  -5.025  1.00 43.76 ? 973  HOH C O   1 
HETATM 19433 O  O   . HOH DA 7 .   ? 1.158   29.612  -20.807 1.00 50.90 ? 974  HOH C O   1 
HETATM 19434 O  O   . HOH DA 7 .   ? 1.646   36.433  11.612  1.00 63.95 ? 975  HOH C O   1 
HETATM 19435 O  O   . HOH DA 7 .   ? -7.503  15.280  -21.856 1.00 50.85 ? 976  HOH C O   1 
HETATM 19436 O  O   . HOH DA 7 .   ? 3.056   3.904   3.587   1.00 52.87 ? 977  HOH C O   1 
HETATM 19437 O  O   . HOH DA 7 .   ? -29.167 36.098  -11.019 1.00 46.97 ? 978  HOH C O   1 
HETATM 19438 O  O   . HOH DA 7 .   ? -25.677 35.839  -19.834 1.00 52.17 ? 979  HOH C O   1 
HETATM 19439 O  O   . HOH DA 7 .   ? -2.520  -14.497 -2.174  1.00 33.40 ? 980  HOH C O   1 
HETATM 19440 O  O   . HOH DA 7 .   ? 1.007   19.501  18.913  1.00 50.02 ? 981  HOH C O   1 
HETATM 19441 O  O   . HOH DA 7 .   ? -38.384 24.453  -23.060 1.00 45.57 ? 982  HOH C O   1 
HETATM 19442 O  O   . HOH DA 7 .   ? -23.613 6.118   3.940   1.00 27.76 ? 983  HOH C O   1 
HETATM 19443 O  O   . HOH DA 7 .   ? 12.844  8.485   1.720   1.00 39.04 ? 984  HOH C O   1 
HETATM 19444 O  O   . HOH DA 7 .   ? -24.756 -7.332  -4.627  1.00 39.33 ? 985  HOH C O   1 
HETATM 19445 O  O   . HOH DA 7 .   ? -27.952 27.780  5.050   1.00 53.02 ? 986  HOH C O   1 
HETATM 19446 O  O   . HOH DA 7 .   ? -19.241 13.772  -29.490 1.00 50.16 ? 987  HOH C O   1 
HETATM 19447 O  O   . HOH DA 7 .   ? -26.047 8.585   -22.210 1.00 40.64 ? 988  HOH C O   1 
HETATM 19448 O  O   . HOH DA 7 .   ? 13.310  -9.706  7.760   1.00 52.75 ? 989  HOH C O   1 
HETATM 19449 O  O   . HOH DA 7 .   ? -8.470  -12.362 -4.436  1.00 30.77 ? 990  HOH C O   1 
HETATM 19450 O  O   . HOH DA 7 .   ? -19.135 40.579  -8.863  1.00 47.01 ? 991  HOH C O   1 
HETATM 19451 O  O   . HOH DA 7 .   ? 18.991  -4.212  -4.826  1.00 24.30 ? 992  HOH C O   1 
HETATM 19452 O  O   . HOH DA 7 .   ? 41.513  12.084  4.343   1.00 32.42 ? 993  HOH C O   1 
HETATM 19453 O  O   . HOH DA 7 .   ? 1.241   1.347   0.774   1.00 46.92 ? 994  HOH C O   1 
HETATM 19454 O  O   . HOH DA 7 .   ? -33.773 14.313  -15.946 1.00 41.44 ? 995  HOH C O   1 
HETATM 19455 O  O   . HOH DA 7 .   ? 11.633  32.262  6.225   1.00 41.13 ? 996  HOH C O   1 
HETATM 19456 O  O   . HOH DA 7 .   ? 1.719   14.959  15.913  1.00 35.25 ? 997  HOH C O   1 
HETATM 19457 O  O   . HOH DA 7 .   ? 7.746   -6.437  -6.367  1.00 38.77 ? 998  HOH C O   1 
HETATM 19458 O  O   . HOH DA 7 .   ? -15.430 -11.622 -7.465  1.00 54.91 ? 999  HOH C O   1 
HETATM 19459 O  O   . HOH DA 7 .   ? -11.726 30.766  -40.336 1.00 52.80 ? 1000 HOH C O   1 
HETATM 19460 O  O   . HOH DA 7 .   ? 27.734  7.888   -3.155  1.00 32.67 ? 1001 HOH C O   1 
HETATM 19461 O  O   . HOH DA 7 .   ? 3.065   11.377  14.294  1.00 22.15 ? 1002 HOH C O   1 
HETATM 19462 O  O   . HOH DA 7 .   ? -6.482  35.534  4.783   1.00 40.22 ? 1003 HOH C O   1 
HETATM 19463 O  O   . HOH DA 7 .   ? 4.706   15.922  13.807  1.00 42.84 ? 1004 HOH C O   1 
HETATM 19464 O  O   . HOH DA 7 .   ? 3.847   8.734   -21.881 1.00 60.50 ? 1005 HOH C O   1 
HETATM 19465 O  O   . HOH DA 7 .   ? 4.651   5.996   17.196  1.00 37.46 ? 1006 HOH C O   1 
HETATM 19466 O  O   . HOH DA 7 .   ? -12.655 33.084  3.155   1.00 43.99 ? 1007 HOH C O   1 
HETATM 19467 O  O   . HOH DA 7 .   ? -11.644 13.330  -26.691 1.00 49.84 ? 1008 HOH C O   1 
HETATM 19468 O  O   . HOH DA 7 .   ? -22.474 -1.753  -4.835  1.00 41.89 ? 1009 HOH C O   1 
HETATM 19469 O  O   . HOH DA 7 .   ? 18.351  7.438   -1.361  1.00 30.28 ? 1010 HOH C O   1 
HETATM 19470 O  O   . HOH DA 7 .   ? 16.391  -1.530  -13.277 1.00 33.18 ? 1011 HOH C O   1 
HETATM 19471 O  O   . HOH DA 7 .   ? 9.367   5.309   12.038  1.00 44.01 ? 1012 HOH C O   1 
HETATM 19472 O  O   . HOH DA 7 .   ? -23.922 6.659   -1.174  1.00 35.37 ? 1013 HOH C O   1 
HETATM 19473 O  O   . HOH DA 7 .   ? -15.760 -14.057 7.737   1.00 36.81 ? 1014 HOH C O   1 
HETATM 19474 O  O   . HOH DA 7 .   ? -21.956 3.236   21.846  1.00 38.33 ? 1015 HOH C O   1 
HETATM 19475 O  O   . HOH DA 7 .   ? 13.948  -0.359  -14.171 1.00 31.69 ? 1016 HOH C O   1 
HETATM 19476 O  O   . HOH DA 7 .   ? -27.203 -6.876  -0.876  1.00 52.80 ? 1017 HOH C O   1 
HETATM 19477 O  O   . HOH DA 7 .   ? 5.292   -1.365  15.708  1.00 40.02 ? 1018 HOH C O   1 
HETATM 19478 O  O   . HOH DA 7 .   ? -23.389 34.823  -19.157 1.00 37.57 ? 1019 HOH C O   1 
HETATM 19479 O  O   . HOH DA 7 .   ? -19.147 24.881  2.091   1.00 41.37 ? 1020 HOH C O   1 
HETATM 19480 O  O   . HOH DA 7 .   ? 15.211  9.184   -17.297 1.00 38.64 ? 1021 HOH C O   1 
HETATM 19481 O  O   . HOH DA 7 .   ? 11.552  15.457  6.780   1.00 54.99 ? 1022 HOH C O   1 
HETATM 19482 O  O   . HOH DA 7 .   ? -24.409 42.735  -2.911  1.00 46.75 ? 1023 HOH C O   1 
HETATM 19483 O  O   . HOH DA 7 .   ? 10.957  4.167   7.345   1.00 42.76 ? 1024 HOH C O   1 
HETATM 19484 O  O   . HOH DA 7 .   ? 7.161   27.301  -8.051  1.00 51.20 ? 1025 HOH C O   1 
HETATM 19485 O  O   . HOH DA 7 .   ? -20.762 17.355  -32.394 1.00 50.74 ? 1026 HOH C O   1 
HETATM 19486 O  O   . HOH DA 7 .   ? -22.673 0.339   21.742  1.00 52.37 ? 1027 HOH C O   1 
HETATM 19487 O  O   . HOH DA 7 .   ? -28.025 28.430  -29.870 1.00 37.93 ? 1028 HOH C O   1 
HETATM 19488 O  O   . HOH DA 7 .   ? 7.410   35.329  10.768  1.00 40.82 ? 1029 HOH C O   1 
HETATM 19489 O  O   . HOH DA 7 .   ? -6.219  -7.497  -17.664 1.00 66.54 ? 1030 HOH C O   1 
HETATM 19490 O  O   . HOH DA 7 .   ? 5.470   3.181   4.906   1.00 53.71 ? 1031 HOH C O   1 
HETATM 19491 O  O   . HOH DA 7 .   ? -8.753  36.436  -2.531  1.00 59.21 ? 1032 HOH C O   1 
HETATM 19492 O  O   . HOH DA 7 .   ? -28.816 38.241  -14.795 1.00 55.32 ? 1033 HOH C O   1 
HETATM 19493 O  O   . HOH DA 7 .   ? -26.572 -4.119  10.649  1.00 35.36 ? 1034 HOH C O   1 
HETATM 19494 O  O   . HOH DA 7 .   ? 1.399   6.546   22.492  1.00 52.61 ? 1035 HOH C O   1 
HETATM 19495 O  O   . HOH DA 7 .   ? -11.278 13.717  -9.939  1.00 35.31 ? 1036 HOH C O   1 
HETATM 19496 O  O   . HOH DA 7 .   ? -14.582 12.231  -5.895  1.00 45.68 ? 1037 HOH C O   1 
HETATM 19497 O  O   . HOH DA 7 .   ? 6.749   33.184  15.270  1.00 33.94 ? 1038 HOH C O   1 
HETATM 19498 O  O   . HOH DA 7 .   ? -4.039  19.143  -18.856 1.00 32.27 ? 1039 HOH C O   1 
HETATM 19499 O  O   . HOH DA 7 .   ? -16.383 -8.853  19.015  1.00 59.87 ? 1040 HOH C O   1 
HETATM 19500 O  O   . HOH DA 7 .   ? -0.611  16.396  17.405  1.00 34.47 ? 1041 HOH C O   1 
HETATM 19501 O  O   . HOH DA 7 .   ? -18.222 22.555  0.479   1.00 29.94 ? 1042 HOH C O   1 
HETATM 19502 O  O   . HOH DA 7 .   ? 30.637  3.936   -9.126  1.00 28.17 ? 1043 HOH C O   1 
HETATM 19503 O  O   . HOH DA 7 .   ? -26.775 36.363  6.522   1.00 59.31 ? 1044 HOH C O   1 
HETATM 19504 O  O   . HOH DA 7 .   ? -17.993 4.989   20.579  1.00 51.66 ? 1045 HOH C O   1 
HETATM 19505 O  O   . HOH DA 7 .   ? 27.238  2.879   -16.793 1.00 55.70 ? 1046 HOH C O   1 
HETATM 19506 O  O   . HOH DA 7 .   ? 1.091   30.554  -7.230  1.00 42.78 ? 1047 HOH C O   1 
HETATM 19507 O  O   . HOH DA 7 .   ? -23.445 2.476   7.651   1.00 30.85 ? 1048 HOH C O   1 
HETATM 19508 O  O   . HOH DA 7 .   ? -37.987 30.857  -2.230  1.00 63.80 ? 1049 HOH C O   1 
HETATM 19509 O  O   . HOH DA 7 .   ? -28.356 14.571  -1.491  1.00 45.85 ? 1050 HOH C O   1 
HETATM 19510 O  O   . HOH DA 7 .   ? 26.452  9.242   3.095   1.00 54.11 ? 1051 HOH C O   1 
HETATM 19511 O  O   . HOH DA 7 .   ? 20.674  13.902  -3.436  1.00 42.84 ? 1052 HOH C O   1 
HETATM 19512 O  O   . HOH DA 7 .   ? -22.724 41.506  -7.506  1.00 54.52 ? 1053 HOH C O   1 
HETATM 19513 O  O   . HOH DA 7 .   ? -0.544  35.219  -17.981 1.00 56.32 ? 1054 HOH C O   1 
HETATM 19514 O  O   . HOH DA 7 .   ? -8.860  11.879  -6.620  1.00 39.17 ? 1055 HOH C O   1 
HETATM 19515 O  O   . HOH DA 7 .   ? 0.847   4.018   -0.793  1.00 41.58 ? 1056 HOH C O   1 
HETATM 19516 O  O   . HOH DA 7 .   ? -13.151 29.826  8.727   1.00 53.09 ? 1057 HOH C O   1 
HETATM 19517 O  O   . HOH DA 7 .   ? -19.630 19.886  7.853   1.00 37.50 ? 1058 HOH C O   1 
HETATM 19518 O  O   . HOH DA 7 .   ? -24.830 -6.734  18.675  1.00 55.07 ? 1059 HOH C O   1 
HETATM 19519 O  O   . HOH DA 7 .   ? -24.757 36.782  5.008   1.00 45.63 ? 1060 HOH C O   1 
HETATM 19520 O  O   . HOH DA 7 .   ? -27.444 -0.068  17.277  1.00 31.29 ? 1061 HOH C O   1 
HETATM 19521 O  O   . HOH DA 7 .   ? -14.967 15.411  -27.243 1.00 35.89 ? 1062 HOH C O   1 
HETATM 19522 O  O   . HOH DA 7 .   ? -33.982 16.227  -18.212 1.00 43.11 ? 1063 HOH C O   1 
HETATM 19523 O  O   . HOH DA 7 .   ? -19.409 -8.600  14.746  1.00 41.57 ? 1064 HOH C O   1 
HETATM 19524 O  O   . HOH DA 7 .   ? 2.568   14.005  -17.614 1.00 37.89 ? 1065 HOH C O   1 
HETATM 19525 O  O   . HOH DA 7 .   ? -18.651 -3.933  20.809  1.00 52.12 ? 1066 HOH C O   1 
HETATM 19526 O  O   . HOH DA 7 .   ? -19.512 9.874   -27.165 1.00 47.41 ? 1067 HOH C O   1 
HETATM 19527 O  O   . HOH DA 7 .   ? -19.524 31.838  -32.576 1.00 57.58 ? 1068 HOH C O   1 
HETATM 19528 O  O   . HOH DA 7 .   ? 16.900  -4.896  -21.492 1.00 42.08 ? 1069 HOH C O   1 
HETATM 19529 O  O   . HOH DA 7 .   ? -29.939 40.178  -7.412  1.00 56.70 ? 1070 HOH C O   1 
HETATM 19530 O  O   . HOH DA 7 .   ? 1.762   26.765  -12.551 1.00 53.19 ? 1071 HOH C O   1 
HETATM 19531 O  O   . HOH DA 7 .   ? -6.363  -2.859  -5.986  1.00 50.99 ? 1072 HOH C O   1 
HETATM 19532 O  O   . HOH DA 7 .   ? 5.487   20.337  -12.299 1.00 30.80 ? 1073 HOH C O   1 
HETATM 19533 O  O   . HOH DA 7 .   ? -35.533 29.928  -0.747  1.00 41.49 ? 1074 HOH C O   1 
HETATM 19534 O  O   . HOH DA 7 .   ? 7.334   7.536   10.040  1.00 31.90 ? 1075 HOH C O   1 
HETATM 19535 O  O   . HOH DA 7 .   ? 22.951  -2.641  4.951   1.00 40.23 ? 1076 HOH C O   1 
HETATM 19536 O  O   . HOH DA 7 .   ? -27.458 19.105  7.039   1.00 57.30 ? 1077 HOH C O   1 
HETATM 19537 O  O   . HOH DA 7 .   ? 1.730   34.658  -5.688  1.00 62.59 ? 1078 HOH C O   1 
HETATM 19538 O  O   . HOH DA 7 .   ? 32.187  4.517   -6.735  1.00 31.85 ? 1079 HOH C O   1 
HETATM 19539 O  O   . HOH DA 7 .   ? 29.728  7.650   8.041   1.00 30.76 ? 1080 HOH C O   1 
HETATM 19540 O  O   . HOH DA 7 .   ? -18.087 -6.973  -7.928  1.00 40.20 ? 1081 HOH C O   1 
HETATM 19541 O  O   . HOH DA 7 .   ? 11.953  32.797  8.998   1.00 44.44 ? 1082 HOH C O   1 
HETATM 19542 O  O   . HOH DA 7 .   ? -2.498  -11.700 -6.541  1.00 40.23 ? 1083 HOH C O   1 
HETATM 19543 O  O   . HOH DA 7 .   ? -13.860 -6.416  22.573  1.00 56.37 ? 1084 HOH C O   1 
HETATM 19544 O  O   . HOH DA 7 .   ? 50.533  10.706  16.228  1.00 52.48 ? 1085 HOH C O   1 
HETATM 19545 O  O   . HOH DA 7 .   ? 41.306  6.457   4.892   1.00 50.19 ? 1086 HOH C O   1 
HETATM 19546 O  O   . HOH DA 7 .   ? 13.717  14.503  0.800   1.00 37.02 ? 1087 HOH C O   1 
HETATM 19547 O  O   . HOH DA 7 .   ? 4.780   21.238  -19.391 1.00 56.52 ? 1088 HOH C O   1 
HETATM 19548 O  O   . HOH DA 7 .   ? 0.146   33.992  -20.904 1.00 56.83 ? 1089 HOH C O   1 
HETATM 19549 O  O   . HOH DA 7 .   ? 14.054  26.280  8.677   1.00 50.21 ? 1090 HOH C O   1 
HETATM 19550 O  O   . HOH DA 7 .   ? -17.944 2.708   -14.252 1.00 59.92 ? 1091 HOH C O   1 
HETATM 19551 O  O   . HOH DA 7 .   ? -1.980  15.668  -22.399 1.00 47.98 ? 1092 HOH C O   1 
HETATM 19552 O  O   . HOH DA 7 .   ? 19.070  10.215  -8.296  1.00 20.76 ? 1093 HOH C O   1 
HETATM 19553 O  O   . HOH DA 7 .   ? -11.557 31.836  8.358   1.00 54.80 ? 1094 HOH C O   1 
HETATM 19554 O  O   . HOH DA 7 .   ? 12.638  2.105   6.870   1.00 48.53 ? 1095 HOH C O   1 
HETATM 19555 O  O   . HOH DA 7 .   ? 21.108  8.749   -9.902  1.00 23.27 ? 1096 HOH C O   1 
HETATM 19556 O  O   . HOH DA 7 .   ? -15.123 28.295  6.783   1.00 37.63 ? 1097 HOH C O   1 
HETATM 19557 O  O   . HOH DA 7 .   ? -33.974 17.875  -21.107 1.00 32.24 ? 1098 HOH C O   1 
HETATM 19558 O  O   . HOH DA 7 .   ? -7.549  22.049  19.110  1.00 50.73 ? 1099 HOH C O   1 
HETATM 19559 O  O   . HOH DA 7 .   ? 7.955   1.353   0.131   1.00 56.40 ? 1100 HOH C O   1 
HETATM 19560 O  O   . HOH DA 7 .   ? 48.948  14.380  8.595   1.00 44.14 ? 1101 HOH C O   1 
HETATM 19561 O  O   . HOH DA 7 .   ? -10.652 31.794  1.887   1.00 36.71 ? 1102 HOH C O   1 
HETATM 19562 O  O   . HOH DA 7 .   ? 5.384   -0.672  0.418   1.00 62.20 ? 1103 HOH C O   1 
HETATM 19563 O  O   . HOH DA 7 .   ? 9.969   7.998   3.159   1.00 41.98 ? 1104 HOH C O   1 
HETATM 19564 O  O   . HOH DA 7 .   ? -40.337 16.565  -13.626 1.00 57.33 ? 1105 HOH C O   1 
HETATM 19565 O  O   . HOH DA 7 .   ? -8.488  0.796   -16.680 1.00 52.03 ? 1106 HOH C O   1 
HETATM 19566 O  O   . HOH DA 7 .   ? 6.179   25.253  -7.249  1.00 50.87 ? 1107 HOH C O   1 
HETATM 19567 O  O   . HOH DA 7 .   ? -24.599 3.515   9.785   1.00 52.40 ? 1108 HOH C O   1 
HETATM 19568 O  O   . HOH DA 7 .   ? -6.779  19.113  21.822  1.00 55.06 ? 1109 HOH C O   1 
HETATM 19569 O  O   . HOH DA 7 .   ? -3.097  -9.633  -22.585 1.00 52.53 ? 1110 HOH C O   1 
HETATM 19570 O  O   . HOH DA 7 .   ? -2.039  19.444  26.278  1.00 55.34 ? 1111 HOH C O   1 
HETATM 19571 O  O   . HOH DA 7 .   ? -17.052 11.378  -5.402  1.00 35.07 ? 1112 HOH C O   1 
HETATM 19572 O  O   . HOH DA 7 .   ? 15.040  11.724  0.865   1.00 54.78 ? 1113 HOH C O   1 
HETATM 19573 O  O   . HOH DA 7 .   ? 0.884   25.488  -14.775 1.00 44.58 ? 1114 HOH C O   1 
HETATM 19574 O  O   . HOH DA 7 .   ? -7.948  -0.829  22.902  1.00 54.86 ? 1115 HOH C O   1 
HETATM 19575 O  O   . HOH DA 7 .   ? -29.811 36.013  -13.941 1.00 48.59 ? 1116 HOH C O   1 
HETATM 19576 O  O   . HOH DA 7 .   ? 30.103  -4.311  4.950   1.00 40.44 ? 1117 HOH C O   1 
HETATM 19577 O  O   . HOH DA 7 .   ? 2.359   30.368  -4.551  1.00 41.95 ? 1118 HOH C O   1 
HETATM 19578 O  O   . HOH DA 7 .   ? -19.520 5.876   -7.359  1.00 44.03 ? 1119 HOH C O   1 
HETATM 19579 O  O   . HOH DA 7 .   ? 19.929  10.036  -12.454 1.00 33.56 ? 1120 HOH C O   1 
HETATM 19580 O  O   . HOH DA 7 .   ? 11.267  6.779   14.249  1.00 39.98 ? 1121 HOH C O   1 
HETATM 19581 O  O   . HOH DA 7 .   ? 5.730   36.358  8.963   1.00 41.43 ? 1122 HOH C O   1 
HETATM 19582 O  O   . HOH DA 7 .   ? -15.937 41.415  -6.577  1.00 53.06 ? 1123 HOH C O   1 
HETATM 19583 O  O   . HOH DA 7 .   ? -23.605 7.579   -4.552  1.00 43.94 ? 1124 HOH C O   1 
HETATM 19584 O  O   . HOH DA 7 .   ? -8.736  10.608  -15.265 1.00 51.04 ? 1125 HOH C O   1 
HETATM 19585 O  O   . HOH DA 7 .   ? -18.896 31.400  -13.747 1.00 50.46 ? 1126 HOH C O   1 
HETATM 19586 O  O   . HOH DA 7 .   ? -33.724 11.824  -17.303 1.00 50.90 ? 1127 HOH C O   1 
HETATM 19587 O  O   . HOH DA 7 .   ? 0.688   32.028  -10.299 1.00 58.03 ? 1128 HOH C O   1 
HETATM 19588 O  O   . HOH DA 7 .   ? -1.069  35.158  -6.709  1.00 55.26 ? 1129 HOH C O   1 
HETATM 19589 O  O   . HOH DA 7 .   ? -6.459  9.846   -10.983 1.00 49.29 ? 1130 HOH C O   1 
HETATM 19590 O  O   . HOH DA 7 .   ? 35.640  7.230   0.257   1.00 40.10 ? 1131 HOH C O   1 
HETATM 19591 O  O   . HOH DA 7 .   ? -27.217 40.245  -1.526  1.00 48.42 ? 1132 HOH C O   1 
HETATM 19592 O  O   . HOH DA 7 .   ? -8.627  3.618   20.709  1.00 35.41 ? 1133 HOH C O   1 
HETATM 19593 O  O   . HOH DA 7 .   ? 17.639  -0.308  5.806   1.00 48.04 ? 1134 HOH C O   1 
HETATM 19594 O  O   . HOH DA 7 .   ? 42.959  5.584   8.108   1.00 52.06 ? 1135 HOH C O   1 
HETATM 19595 O  O   . HOH DA 7 .   ? -21.674 30.912  3.209   1.00 47.21 ? 1136 HOH C O   1 
HETATM 19596 O  O   . HOH DA 7 .   ? -31.450 27.508  -35.624 1.00 49.62 ? 1137 HOH C O   1 
HETATM 19597 O  O   . HOH DA 7 .   ? -14.528 12.884  8.097   1.00 36.59 ? 1138 HOH C O   1 
HETATM 19598 O  O   . HOH DA 7 .   ? 11.412  -6.397  -14.966 1.00 40.65 ? 1139 HOH C O   1 
HETATM 19599 O  O   . HOH DA 7 .   ? 2.761   30.864  -9.255  1.00 57.68 ? 1140 HOH C O   1 
HETATM 19600 O  O   . HOH DA 7 .   ? -29.213 -0.056  13.354  1.00 41.81 ? 1141 HOH C O   1 
HETATM 19601 O  O   . HOH DA 7 .   ? -27.800 31.387  -30.262 1.00 42.14 ? 1142 HOH C O   1 
HETATM 19602 O  O   . HOH DA 7 .   ? -3.027  38.575  9.362   1.00 53.88 ? 1143 HOH C O   1 
HETATM 19603 O  O   . HOH DA 7 .   ? -19.262 -1.774  19.701  1.00 36.92 ? 1144 HOH C O   1 
HETATM 19604 O  O   . HOH DA 7 .   ? 3.374   37.530  9.376   1.00 54.76 ? 1145 HOH C O   1 
HETATM 19605 O  O   . HOH DA 7 .   ? -3.424  34.522  2.972   1.00 34.87 ? 1146 HOH C O   1 
HETATM 19606 O  O   . HOH DA 7 .   ? -5.652  12.908  22.183  1.00 52.12 ? 1147 HOH C O   1 
HETATM 19607 O  O   . HOH DA 7 .   ? 8.987   15.753  -13.764 1.00 49.73 ? 1148 HOH C O   1 
HETATM 19608 O  O   . HOH DA 7 .   ? -13.460 5.038   21.108  1.00 36.59 ? 1149 HOH C O   1 
HETATM 19609 O  O   . HOH DA 7 .   ? 11.469  29.909  -2.548  1.00 42.03 ? 1150 HOH C O   1 
HETATM 19610 O  O   . HOH DA 7 .   ? 13.631  13.766  -10.996 1.00 42.30 ? 1151 HOH C O   1 
HETATM 19611 O  O   . HOH DA 7 .   ? -12.359 -5.737  24.715  1.00 47.39 ? 1152 HOH C O   1 
HETATM 19612 O  O   . HOH DA 7 .   ? -23.708 -4.180  -3.931  1.00 51.28 ? 1153 HOH C O   1 
HETATM 19613 O  O   . HOH DA 7 .   ? -6.974  34.682  -10.402 1.00 43.69 ? 1154 HOH C O   1 
HETATM 19614 O  O   . HOH DA 7 .   ? 11.562  15.283  3.722   1.00 49.31 ? 1155 HOH C O   1 
HETATM 19615 O  O   . HOH DA 7 .   ? 25.762  7.553   5.056   1.00 61.35 ? 1156 HOH C O   1 
HETATM 19616 O  O   . HOH DA 7 .   ? -26.814 37.366  -24.624 1.00 45.20 ? 1157 HOH C O   1 
HETATM 19617 O  O   . HOH DA 7 .   ? -20.623 21.122  2.456   1.00 44.17 ? 1158 HOH C O   1 
HETATM 19618 O  O   . HOH DA 7 .   ? -13.272 12.645  -8.242  1.00 47.16 ? 1159 HOH C O   1 
HETATM 19619 O  O   . HOH DA 7 .   ? -7.730  24.365  17.823  1.00 43.09 ? 1160 HOH C O   1 
HETATM 19620 O  O   . HOH DA 7 .   ? -10.651 26.267  11.578  1.00 39.72 ? 1161 HOH C O   1 
HETATM 19621 O  O   . HOH DA 7 .   ? -12.630 24.428  11.755  1.00 37.52 ? 1162 HOH C O   1 
HETATM 19622 O  O   . HOH DA 7 .   ? 12.782  29.009  -5.073  1.00 56.14 ? 1163 HOH C O   1 
HETATM 19623 O  O   . HOH DA 7 .   ? 17.520  15.827  -2.893  1.00 47.79 ? 1164 HOH C O   1 
HETATM 19624 O  O   . HOH DA 7 .   ? -16.109 12.766  -27.807 1.00 53.89 ? 1165 HOH C O   1 
HETATM 19625 O  O   . HOH DA 7 .   ? -6.100  17.751  -18.641 1.00 39.16 ? 1166 HOH C O   1 
HETATM 19626 O  O   . HOH DA 7 .   ? -12.801 35.140  -6.040  1.00 47.99 ? 1167 HOH C O   1 
HETATM 19627 O  O   . HOH DA 7 .   ? -14.380 -19.354 2.831   1.00 68.17 ? 1168 HOH C O   1 
HETATM 19628 O  O   . HOH DA 7 .   ? -14.559 5.279   -13.091 1.00 50.08 ? 1169 HOH C O   1 
HETATM 19629 O  O   . HOH DA 7 .   ? -23.848 0.032   -2.303  1.00 42.73 ? 1170 HOH C O   1 
HETATM 19630 O  O   . HOH DA 7 .   ? -23.154 8.089   -9.623  1.00 48.74 ? 1171 HOH C O   1 
HETATM 19631 O  O   . HOH DA 7 .   ? -30.048 35.924  -19.175 1.00 45.84 ? 1172 HOH C O   1 
HETATM 19632 O  O   . HOH DA 7 .   ? -16.959 10.431  -26.917 1.00 52.29 ? 1173 HOH C O   1 
HETATM 19633 O  O   . HOH DA 7 .   ? -30.286 6.961   -10.238 1.00 52.56 ? 1174 HOH C O   1 
HETATM 19634 O  O   . HOH DA 7 .   ? 5.183   -1.463  6.273   1.00 50.93 ? 1175 HOH C O   1 
HETATM 19635 O  O   . HOH DA 7 .   ? -20.894 14.883  -31.457 1.00 55.83 ? 1176 HOH C O   1 
HETATM 19636 O  O   . HOH DA 7 .   ? 2.640   -7.517  19.707  1.00 44.22 ? 1177 HOH C O   1 
HETATM 19637 O  O   . HOH DA 7 .   ? -24.425 43.058  -5.236  1.00 44.04 ? 1178 HOH C O   1 
HETATM 19638 O  O   . HOH DA 7 .   ? 8.148   20.009  -11.326 1.00 53.71 ? 1179 HOH C O   1 
HETATM 19639 O  O   . HOH DA 7 .   ? 0.495   19.639  -21.177 1.00 45.45 ? 1180 HOH C O   1 
HETATM 19640 O  O   . HOH DA 7 .   ? -15.098 32.300  3.696   1.00 40.12 ? 1181 HOH C O   1 
HETATM 19641 O  O   . HOH DA 7 .   ? 26.846  6.782   -10.113 1.00 32.80 ? 1182 HOH C O   1 
HETATM 19642 O  O   . HOH DA 7 .   ? 9.800   2.470   -25.738 1.00 51.65 ? 1183 HOH C O   1 
HETATM 19643 O  O   . HOH DA 7 .   ? -12.780 28.328  11.428  1.00 49.62 ? 1184 HOH C O   1 
HETATM 19644 O  O   . HOH DA 7 .   ? -6.491  2.662   23.967  1.00 47.28 ? 1185 HOH C O   1 
HETATM 19645 O  O   . HOH DA 7 .   ? -8.790  35.586  2.762   1.00 42.05 ? 1186 HOH C O   1 
HETATM 19646 O  O   . HOH DA 7 .   ? 32.481  3.072   -10.787 1.00 48.83 ? 1187 HOH C O   1 
HETATM 19647 O  O   . HOH DA 7 .   ? 34.811  4.427   -7.568  1.00 41.71 ? 1188 HOH C O   1 
HETATM 19648 O  O   . HOH DA 7 .   ? -11.755 35.830  10.735  1.00 51.92 ? 1189 HOH C O   1 
HETATM 19649 O  O   . HOH DA 7 .   ? 45.756  9.798   16.573  1.00 39.96 ? 1190 HOH C O   1 
HETATM 19650 O  O   . HOH DA 7 .   ? 29.222  1.202   -17.375 1.00 47.10 ? 1191 HOH C O   1 
HETATM 19651 O  O   . HOH DA 7 .   ? -7.586  25.677  15.438  1.00 33.88 ? 1192 HOH C O   1 
HETATM 19652 O  O   . HOH DA 7 .   ? -10.334 33.964  -8.162  1.00 46.26 ? 1193 HOH C O   1 
HETATM 19653 O  O   . HOH DA 7 .   ? 10.776  6.698   -22.377 1.00 53.28 ? 1194 HOH C O   1 
HETATM 19654 O  O   . HOH DA 7 .   ? -8.765  8.946   -16.989 1.00 46.20 ? 1195 HOH C O   1 
HETATM 19655 O  O   . HOH DA 7 .   ? 29.403  6.091   -9.946  1.00 36.49 ? 1196 HOH C O   1 
HETATM 19656 O  O   . HOH EA 7 .   ? 34.812  -7.864  -3.456  1.00 37.91 ? 701  HOH D O   1 
HETATM 19657 O  O   . HOH EA 7 .   ? 17.691  -36.600 -47.924 1.00 58.16 ? 702  HOH D O   1 
HETATM 19658 O  O   . HOH EA 7 .   ? 20.733  -49.618 -32.951 1.00 51.07 ? 703  HOH D O   1 
HETATM 19659 O  O   . HOH EA 7 .   ? 23.089  -51.037 -11.685 1.00 45.57 ? 704  HOH D O   1 
HETATM 19660 O  O   . HOH EA 7 .   ? 10.031  -44.359 -4.825  1.00 55.79 ? 705  HOH D O   1 
HETATM 19661 O  O   . HOH EA 7 .   ? 3.726   -44.036 -15.521 1.00 50.69 ? 706  HOH D O   1 
HETATM 19662 O  O   . HOH EA 7 .   ? 21.629  -30.336 7.578   1.00 50.52 ? 707  HOH D O   1 
HETATM 19663 O  O   . HOH EA 7 .   ? 33.171  -43.783 -14.766 1.00 40.46 ? 708  HOH D O   1 
HETATM 19664 O  O   . HOH EA 7 .   ? 19.762  -30.296 5.946   1.00 46.73 ? 709  HOH D O   1 
HETATM 19665 O  O   . HOH EA 7 .   ? 22.405  -13.669 -29.119 1.00 54.48 ? 710  HOH D O   1 
HETATM 19666 O  O   . HOH EA 7 .   ? 27.429  -48.197 -13.701 1.00 56.80 ? 711  HOH D O   1 
HETATM 19667 O  O   . HOH EA 7 .   ? 37.359  -14.884 3.453   1.00 45.30 ? 712  HOH D O   1 
HETATM 19668 O  O   . HOH EA 7 .   ? 44.853  -22.717 -17.926 1.00 49.45 ? 713  HOH D O   1 
HETATM 19669 O  O   . HOH EA 7 .   ? 29.648  -47.575 1.839   1.00 34.34 ? 714  HOH D O   1 
HETATM 19670 O  O   . HOH EA 7 .   ? -12.088 -13.436 -7.361  1.00 43.09 ? 715  HOH D O   1 
HETATM 19671 O  O   . HOH EA 7 .   ? 1.640   -29.811 -6.003  1.00 37.23 ? 716  HOH D O   1 
HETATM 19672 O  O   . HOH EA 7 .   ? 20.863  -50.215 -6.600  1.00 54.11 ? 717  HOH D O   1 
HETATM 19673 O  O   . HOH EA 7 .   ? 12.871  -16.815 -2.066  1.00 47.68 ? 718  HOH D O   1 
HETATM 19674 O  O   . HOH EA 7 .   ? 42.225  -18.540 -21.522 1.00 56.27 ? 719  HOH D O   1 
HETATM 19675 O  O   . HOH EA 7 .   ? 2.384   -33.533 -11.994 1.00 46.08 ? 720  HOH D O   1 
HETATM 19676 O  O   . HOH EA 7 .   ? 24.768  -30.498 6.963   1.00 48.38 ? 721  HOH D O   1 
HETATM 19677 O  O   . HOH EA 7 .   ? 29.654  -8.370  -20.280 1.00 21.44 ? 722  HOH D O   1 
HETATM 19678 O  O   . HOH EA 7 .   ? 27.147  -26.330 -27.871 1.00 48.33 ? 723  HOH D O   1 
HETATM 19679 O  O   . HOH EA 7 .   ? 21.593  -25.470 -21.004 1.00 36.25 ? 724  HOH D O   1 
HETATM 19680 O  O   . HOH EA 7 .   ? 39.442  -18.257 -1.015  1.00 37.97 ? 725  HOH D O   1 
HETATM 19681 O  O   . HOH EA 7 .   ? 22.879  -55.133 -19.366 1.00 46.92 ? 726  HOH D O   1 
HETATM 19682 O  O   . HOH EA 7 .   ? 2.009   -43.101 -18.960 1.00 55.01 ? 727  HOH D O   1 
HETATM 19683 O  O   . HOH EA 7 .   ? 36.422  -41.106 -26.146 1.00 58.96 ? 728  HOH D O   1 
HETATM 19684 O  O   . HOH EA 7 .   ? 27.268  -30.132 -2.083  1.00 43.03 ? 729  HOH D O   1 
HETATM 19685 O  O   . HOH EA 7 .   ? 38.339  -45.873 -32.129 1.00 53.42 ? 730  HOH D O   1 
HETATM 19686 O  O   . HOH EA 7 .   ? 17.839  -3.685  -24.016 1.00 41.57 ? 731  HOH D O   1 
HETATM 19687 O  O   . HOH EA 7 .   ? 22.069  -2.340  -29.244 1.00 45.71 ? 732  HOH D O   1 
HETATM 19688 O  O   . HOH EA 7 .   ? 14.462  -19.976 -4.297  1.00 41.91 ? 733  HOH D O   1 
HETATM 19689 O  O   . HOH EA 7 .   ? 15.401  -17.088 -13.967 1.00 32.90 ? 734  HOH D O   1 
HETATM 19690 O  O   . HOH EA 7 .   ? 22.501  -50.731 0.683   1.00 46.24 ? 735  HOH D O   1 
HETATM 19691 O  O   . HOH EA 7 .   ? 18.867  -33.254 7.261   1.00 51.42 ? 736  HOH D O   1 
HETATM 19692 O  O   . HOH EA 7 .   ? 20.882  -47.467 -12.136 1.00 40.73 ? 737  HOH D O   1 
HETATM 19693 O  O   . HOH EA 7 .   ? 28.389  -18.747 -28.190 1.00 42.42 ? 738  HOH D O   1 
HETATM 19694 O  O   . HOH EA 7 .   ? -1.256  -30.512 -9.600  1.00 55.81 ? 739  HOH D O   1 
HETATM 19695 O  O   . HOH EA 7 .   ? 38.937  -11.298 -1.629  1.00 34.82 ? 740  HOH D O   1 
HETATM 19696 O  O   . HOH EA 7 .   ? 5.608   -12.862 19.535  1.00 30.19 ? 741  HOH D O   1 
HETATM 19697 O  O   . HOH EA 7 .   ? 14.992  -53.214 -36.370 1.00 50.64 ? 742  HOH D O   1 
HETATM 19698 O  O   . HOH EA 7 .   ? 4.940   -52.541 -16.533 1.00 57.66 ? 743  HOH D O   1 
HETATM 19699 O  O   . HOH EA 7 .   ? 41.526  -29.089 -19.512 1.00 29.50 ? 744  HOH D O   1 
HETATM 19700 O  O   . HOH EA 7 .   ? 9.425   -51.819 -17.932 1.00 50.07 ? 745  HOH D O   1 
HETATM 19701 O  O   . HOH EA 7 .   ? 3.107   -27.493 -0.195  1.00 27.44 ? 746  HOH D O   1 
HETATM 19702 O  O   . HOH EA 7 .   ? 11.853  -47.848 2.340   1.00 56.50 ? 747  HOH D O   1 
HETATM 19703 O  O   . HOH EA 7 .   ? 40.776  -22.230 -15.335 1.00 36.32 ? 748  HOH D O   1 
HETATM 19704 O  O   . HOH EA 7 .   ? 40.449  -6.663  -9.563  1.00 32.76 ? 749  HOH D O   1 
HETATM 19705 O  O   . HOH EA 7 .   ? 18.209  -18.602 5.139   1.00 40.96 ? 750  HOH D O   1 
HETATM 19706 O  O   . HOH EA 7 .   ? 37.852  -5.488  -16.620 1.00 39.33 ? 751  HOH D O   1 
HETATM 19707 O  O   . HOH EA 7 .   ? -1.406  -4.637  4.762   1.00 29.23 ? 752  HOH D O   1 
HETATM 19708 O  O   . HOH EA 7 .   ? 39.762  -14.568 -3.959  1.00 27.74 ? 753  HOH D O   1 
HETATM 19709 O  O   . HOH EA 7 .   ? 24.136  -49.999 -19.937 1.00 40.25 ? 754  HOH D O   1 
HETATM 19710 O  O   . HOH EA 7 .   ? 14.482  -41.633 10.355  1.00 51.03 ? 755  HOH D O   1 
HETATM 19711 O  O   . HOH EA 7 .   ? 33.316  -30.336 2.006   1.00 36.67 ? 756  HOH D O   1 
HETATM 19712 O  O   . HOH EA 7 .   ? 42.339  -38.297 -40.375 1.00 53.93 ? 757  HOH D O   1 
HETATM 19713 O  O   . HOH EA 7 .   ? 12.203  -51.679 -14.353 1.00 50.30 ? 758  HOH D O   1 
HETATM 19714 O  O   . HOH EA 7 .   ? 6.441   -30.647 6.347   1.00 38.90 ? 759  HOH D O   1 
HETATM 19715 O  O   . HOH EA 7 .   ? 22.072  -48.343 -7.977  1.00 42.02 ? 760  HOH D O   1 
HETATM 19716 O  O   . HOH EA 7 .   ? 33.168  -9.632  1.798   1.00 28.98 ? 761  HOH D O   1 
HETATM 19717 O  O   . HOH EA 7 .   ? 1.485   -47.309 -43.644 1.00 55.28 ? 762  HOH D O   1 
HETATM 19718 O  O   . HOH EA 7 .   ? -2.216  -20.958 14.984  1.00 30.50 ? 763  HOH D O   1 
HETATM 19719 O  O   . HOH EA 7 .   ? 24.656  -49.243 -1.741  1.00 34.41 ? 764  HOH D O   1 
HETATM 19720 O  O   . HOH EA 7 .   ? 30.850  -8.320  -9.594  1.00 26.43 ? 765  HOH D O   1 
HETATM 19721 O  O   . HOH EA 7 .   ? 18.006  -51.667 -22.731 1.00 36.37 ? 766  HOH D O   1 
HETATM 19722 O  O   . HOH EA 7 .   ? 7.253   -48.042 -33.627 1.00 48.83 ? 767  HOH D O   1 
HETATM 19723 O  O   . HOH EA 7 .   ? 9.157   -42.044 -27.570 1.00 38.78 ? 768  HOH D O   1 
HETATM 19724 O  O   . HOH EA 7 .   ? 6.895   -44.348 -15.963 1.00 41.91 ? 769  HOH D O   1 
HETATM 19725 O  O   . HOH EA 7 .   ? 14.858  -14.247 -3.675  1.00 44.99 ? 770  HOH D O   1 
HETATM 19726 O  O   . HOH EA 7 .   ? 24.960  2.803   -28.539 1.00 48.36 ? 771  HOH D O   1 
HETATM 19727 O  O   . HOH EA 7 .   ? 28.282  -25.784 -20.991 1.00 27.71 ? 772  HOH D O   1 
HETATM 19728 O  O   . HOH EA 7 .   ? 38.158  -7.744  -23.750 1.00 38.60 ? 773  HOH D O   1 
HETATM 19729 O  O   . HOH EA 7 .   ? -3.575  -20.973 7.350   1.00 31.31 ? 774  HOH D O   1 
HETATM 19730 O  O   . HOH EA 7 .   ? -3.153  -25.920 -6.335  1.00 38.34 ? 775  HOH D O   1 
HETATM 19731 O  O   . HOH EA 7 .   ? 4.039   -32.269 -5.208  1.00 48.34 ? 776  HOH D O   1 
HETATM 19732 O  O   . HOH EA 7 .   ? 15.665  -8.769  -6.955  1.00 24.10 ? 777  HOH D O   1 
HETATM 19733 O  O   . HOH EA 7 .   ? 0.387   -21.666 21.943  1.00 27.12 ? 778  HOH D O   1 
HETATM 19734 O  O   . HOH EA 7 .   ? 1.036   -21.261 -18.393 1.00 58.81 ? 779  HOH D O   1 
HETATM 19735 O  O   . HOH EA 7 .   ? 17.820  -51.019 -29.954 1.00 34.43 ? 780  HOH D O   1 
HETATM 19736 O  O   . HOH EA 7 .   ? 36.099  -38.591 -27.287 1.00 40.17 ? 781  HOH D O   1 
HETATM 19737 O  O   . HOH EA 7 .   ? 16.614  -5.486  -25.628 1.00 54.05 ? 782  HOH D O   1 
HETATM 19738 O  O   . HOH EA 7 .   ? 1.838   -25.149 16.677  1.00 38.25 ? 783  HOH D O   1 
HETATM 19739 O  O   . HOH EA 7 .   ? 2.153   -33.962 -21.934 1.00 53.49 ? 784  HOH D O   1 
HETATM 19740 O  O   . HOH EA 7 .   ? 6.937   -11.116 15.107  1.00 43.13 ? 785  HOH D O   1 
HETATM 19741 O  O   . HOH EA 7 .   ? 34.114  -23.076 -27.794 1.00 52.12 ? 786  HOH D O   1 
HETATM 19742 O  O   . HOH EA 7 .   ? 26.965  -30.148 4.503   1.00 41.64 ? 787  HOH D O   1 
HETATM 19743 O  O   . HOH EA 7 .   ? 1.643   -28.899 -15.853 1.00 33.57 ? 788  HOH D O   1 
HETATM 19744 O  O   . HOH EA 7 .   ? 0.615   -24.949 24.127  1.00 41.15 ? 789  HOH D O   1 
HETATM 19745 O  O   . HOH EA 7 .   ? 14.454  -28.638 -18.673 1.00 39.06 ? 790  HOH D O   1 
HETATM 19746 O  O   . HOH EA 7 .   ? 6.704   -3.557  7.126   1.00 37.95 ? 791  HOH D O   1 
HETATM 19747 O  O   . HOH EA 7 .   ? 40.250  -6.573  -16.938 1.00 47.63 ? 792  HOH D O   1 
HETATM 19748 O  O   . HOH EA 7 .   ? 24.857  -33.297 14.324  1.00 42.27 ? 793  HOH D O   1 
HETATM 19749 O  O   . HOH EA 7 .   ? 48.433  -17.237 -14.291 1.00 53.93 ? 794  HOH D O   1 
HETATM 19750 O  O   . HOH EA 7 .   ? 32.772  -19.998 -22.483 1.00 25.76 ? 795  HOH D O   1 
HETATM 19751 O  O   . HOH EA 7 .   ? 40.322  -37.221 -7.499  1.00 41.66 ? 796  HOH D O   1 
HETATM 19752 O  O   . HOH EA 7 .   ? 16.183  -23.015 -5.705  1.00 32.86 ? 797  HOH D O   1 
HETATM 19753 O  O   . HOH EA 7 .   ? 30.901  -15.323 -27.945 1.00 34.92 ? 798  HOH D O   1 
HETATM 19754 O  O   . HOH EA 7 .   ? 3.513   -35.789 -18.583 1.00 36.46 ? 799  HOH D O   1 
HETATM 19755 O  O   . HOH EA 7 .   ? 8.537   -29.950 -22.192 1.00 52.05 ? 800  HOH D O   1 
HETATM 19756 O  O   . HOH EA 7 .   ? 3.548   -29.553 -3.837  1.00 31.98 ? 801  HOH D O   1 
HETATM 19757 O  O   . HOH EA 7 .   ? 22.189  -10.729 -7.424  1.00 28.91 ? 802  HOH D O   1 
HETATM 19758 O  O   . HOH EA 7 .   ? 18.691  -49.253 -12.551 1.00 50.54 ? 803  HOH D O   1 
HETATM 19759 O  O   . HOH EA 7 .   ? 7.194   -28.164 5.849   1.00 38.59 ? 804  HOH D O   1 
HETATM 19760 O  O   . HOH EA 7 .   ? 39.460  -8.182  -19.315 1.00 25.61 ? 805  HOH D O   1 
HETATM 19761 O  O   . HOH EA 7 .   ? 29.541  -8.886  3.896   1.00 57.02 ? 806  HOH D O   1 
HETATM 19762 O  O   . HOH EA 7 .   ? 43.264  -9.554  -20.203 1.00 39.08 ? 807  HOH D O   1 
HETATM 19763 O  O   . HOH EA 7 .   ? 43.238  -4.989  -6.508  1.00 41.96 ? 808  HOH D O   1 
HETATM 19764 O  O   . HOH EA 7 .   ? 26.569  -59.476 -21.432 1.00 36.11 ? 809  HOH D O   1 
HETATM 19765 O  O   . HOH EA 7 .   ? 7.954   -44.818 -7.353  1.00 52.75 ? 810  HOH D O   1 
HETATM 19766 O  O   . HOH EA 7 .   ? 2.986   -23.833 19.312  1.00 37.63 ? 811  HOH D O   1 
HETATM 19767 O  O   . HOH EA 7 .   ? 29.383  -1.862  -17.489 1.00 35.59 ? 812  HOH D O   1 
HETATM 19768 O  O   . HOH EA 7 .   ? 32.718  -46.906 -11.325 1.00 60.08 ? 813  HOH D O   1 
HETATM 19769 O  O   . HOH EA 7 .   ? 19.921  -22.556 -20.974 1.00 37.90 ? 814  HOH D O   1 
HETATM 19770 O  O   . HOH EA 7 .   ? 2.313   -51.578 -17.924 1.00 57.14 ? 815  HOH D O   1 
HETATM 19771 O  O   . HOH EA 7 .   ? 21.817  -28.471 -19.985 1.00 31.03 ? 816  HOH D O   1 
HETATM 19772 O  O   . HOH EA 7 .   ? 35.576  -2.592  -15.265 1.00 36.56 ? 817  HOH D O   1 
HETATM 19773 O  O   . HOH EA 7 .   ? 11.318  -48.079 -46.502 1.00 55.17 ? 818  HOH D O   1 
HETATM 19774 O  O   . HOH EA 7 .   ? 43.538  -18.100 -10.028 1.00 32.51 ? 819  HOH D O   1 
HETATM 19775 O  O   . HOH EA 7 .   ? 4.403   -5.136  17.514  1.00 57.22 ? 820  HOH D O   1 
HETATM 19776 O  O   . HOH EA 7 .   ? 28.852  -27.789 0.353   1.00 27.85 ? 821  HOH D O   1 
HETATM 19777 O  O   . HOH EA 7 .   ? 7.352   -18.230 15.936  1.00 50.30 ? 822  HOH D O   1 
HETATM 19778 O  O   . HOH EA 7 .   ? 0.008   -22.374 13.624  1.00 31.67 ? 823  HOH D O   1 
HETATM 19779 O  O   . HOH EA 7 .   ? 15.073  -31.683 -24.678 1.00 44.72 ? 824  HOH D O   1 
HETATM 19780 O  O   . HOH EA 7 .   ? 40.919  -34.111 6.163   1.00 49.59 ? 825  HOH D O   1 
HETATM 19781 O  O   . HOH EA 7 .   ? 40.944  -25.261 -4.011  1.00 41.89 ? 826  HOH D O   1 
HETATM 19782 O  O   . HOH EA 7 .   ? 17.863  -16.710 -7.064  1.00 34.03 ? 827  HOH D O   1 
HETATM 19783 O  O   . HOH EA 7 .   ? 12.639  -23.483 3.614   1.00 39.56 ? 828  HOH D O   1 
HETATM 19784 O  O   . HOH EA 7 .   ? 9.466   -10.619 -11.319 1.00 47.66 ? 829  HOH D O   1 
HETATM 19785 O  O   . HOH EA 7 .   ? 35.483  -30.658 -38.678 1.00 54.23 ? 830  HOH D O   1 
HETATM 19786 O  O   . HOH EA 7 .   ? 8.189   -43.452 -11.628 1.00 46.06 ? 831  HOH D O   1 
HETATM 19787 O  O   . HOH EA 7 .   ? 19.095  -30.313 -37.380 1.00 45.47 ? 832  HOH D O   1 
HETATM 19788 O  O   . HOH EA 7 .   ? 30.079  -31.801 4.097   1.00 52.56 ? 833  HOH D O   1 
HETATM 19789 O  O   . HOH EA 7 .   ? 14.631  -18.949 -26.184 1.00 47.40 ? 834  HOH D O   1 
HETATM 19790 O  O   . HOH EA 7 .   ? 22.291  -33.022 -47.924 1.00 52.46 ? 835  HOH D O   1 
HETATM 19791 O  O   . HOH EA 7 .   ? 7.103   -21.420 25.344  1.00 26.40 ? 836  HOH D O   1 
HETATM 19792 O  O   . HOH EA 7 .   ? 28.461  -33.199 -2.282  1.00 26.09 ? 837  HOH D O   1 
HETATM 19793 O  O   . HOH EA 7 .   ? 33.560  -34.226 -10.251 1.00 22.62 ? 838  HOH D O   1 
HETATM 19794 O  O   . HOH EA 7 .   ? 35.795  -32.382 -4.065  1.00 22.65 ? 839  HOH D O   1 
HETATM 19795 O  O   . HOH EA 7 .   ? 4.165   -39.039 -9.874  1.00 45.22 ? 840  HOH D O   1 
HETATM 19796 O  O   . HOH EA 7 .   ? 33.680  -28.993 -5.149  1.00 19.62 ? 841  HOH D O   1 
HETATM 19797 O  O   . HOH EA 7 .   ? 33.738  -33.054 4.530   1.00 47.74 ? 842  HOH D O   1 
HETATM 19798 O  O   . HOH EA 7 .   ? 28.109  -13.305 -17.789 1.00 41.45 ? 843  HOH D O   1 
HETATM 19799 O  O   . HOH EA 7 .   ? 13.641  -18.625 -13.480 1.00 31.78 ? 844  HOH D O   1 
HETATM 19800 O  O   . HOH EA 7 .   ? -0.463  -22.438 -13.233 1.00 47.00 ? 845  HOH D O   1 
HETATM 19801 O  O   . HOH EA 7 .   ? 26.984  -34.789 6.475   1.00 43.76 ? 846  HOH D O   1 
HETATM 19802 O  O   . HOH EA 7 .   ? 36.537  -11.670 -27.255 1.00 34.80 ? 847  HOH D O   1 
HETATM 19803 O  O   . HOH EA 7 .   ? 21.741  -19.892 -0.916  1.00 26.87 ? 848  HOH D O   1 
HETATM 19804 O  O   . HOH EA 7 .   ? 11.495  -49.976 -17.996 1.00 44.15 ? 849  HOH D O   1 
HETATM 19805 O  O   . HOH EA 7 .   ? 31.918  -35.091 -13.692 1.00 24.43 ? 850  HOH D O   1 
HETATM 19806 O  O   . HOH EA 7 .   ? 13.979  -43.533 -20.452 1.00 29.66 ? 851  HOH D O   1 
HETATM 19807 O  O   . HOH EA 7 .   ? 39.302  -24.861 -1.733  1.00 28.34 ? 852  HOH D O   1 
HETATM 19808 O  O   . HOH EA 7 .   ? -0.930  -8.305  17.289  1.00 22.30 ? 853  HOH D O   1 
HETATM 19809 O  O   . HOH EA 7 .   ? 47.272  -10.417 -15.542 1.00 61.09 ? 854  HOH D O   1 
HETATM 19810 O  O   . HOH EA 7 .   ? -2.693  -29.703 -0.424  1.00 42.96 ? 855  HOH D O   1 
HETATM 19811 O  O   . HOH EA 7 .   ? 8.998   -18.886 -24.453 1.00 41.96 ? 856  HOH D O   1 
HETATM 19812 O  O   . HOH EA 7 .   ? 42.108  -13.323 -13.454 1.00 30.75 ? 857  HOH D O   1 
HETATM 19813 O  O   . HOH EA 7 .   ? 8.582   -44.371 -30.527 1.00 42.15 ? 858  HOH D O   1 
HETATM 19814 O  O   . HOH EA 7 .   ? 13.131  -4.631  -15.480 1.00 37.37 ? 859  HOH D O   1 
HETATM 19815 O  O   . HOH EA 7 .   ? -1.154  -10.193 -8.160  1.00 39.99 ? 860  HOH D O   1 
HETATM 19816 O  O   . HOH EA 7 .   ? -5.888  -8.366  10.186  1.00 45.17 ? 861  HOH D O   1 
HETATM 19817 O  O   . HOH EA 7 .   ? 27.344  -32.757 0.285   1.00 23.70 ? 862  HOH D O   1 
HETATM 19818 O  O   . HOH EA 7 .   ? 38.772  -55.759 -29.238 1.00 61.40 ? 863  HOH D O   1 
HETATM 19819 O  O   . HOH EA 7 .   ? 6.017   -34.471 -10.497 1.00 27.35 ? 864  HOH D O   1 
HETATM 19820 O  O   . HOH EA 7 .   ? 31.140  -13.372 -19.332 1.00 29.46 ? 865  HOH D O   1 
HETATM 19821 O  O   . HOH EA 7 .   ? 10.339  -30.430 -4.096  1.00 41.05 ? 866  HOH D O   1 
HETATM 19822 O  O   . HOH EA 7 .   ? 31.720  -40.577 -8.633  1.00 25.72 ? 867  HOH D O   1 
HETATM 19823 O  O   . HOH EA 7 .   ? 41.026  -23.553 -8.360  1.00 30.42 ? 868  HOH D O   1 
HETATM 19824 O  O   . HOH EA 7 .   ? 23.970  3.264   -19.757 1.00 43.39 ? 869  HOH D O   1 
HETATM 19825 O  O   . HOH EA 7 .   ? 33.792  -16.716 -22.086 1.00 22.48 ? 870  HOH D O   1 
HETATM 19826 O  O   . HOH EA 7 .   ? 23.211  -9.661  -31.416 1.00 42.62 ? 871  HOH D O   1 
HETATM 19827 O  O   . HOH EA 7 .   ? 32.904  -35.089 1.543   1.00 21.53 ? 872  HOH D O   1 
HETATM 19828 O  O   . HOH EA 7 .   ? 15.983  -14.835 4.148   1.00 46.83 ? 873  HOH D O   1 
HETATM 19829 O  O   . HOH EA 7 .   ? -7.311  -22.028 -9.835  1.00 44.16 ? 874  HOH D O   1 
HETATM 19830 O  O   . HOH EA 7 .   ? 19.256  -19.062 -3.780  1.00 42.56 ? 875  HOH D O   1 
HETATM 19831 O  O   . HOH EA 7 .   ? 25.979  -15.277 -29.951 1.00 41.63 ? 876  HOH D O   1 
HETATM 19832 O  O   . HOH EA 7 .   ? 2.911   -11.093 4.336   1.00 24.56 ? 877  HOH D O   1 
HETATM 19833 O  O   . HOH EA 7 .   ? 10.905  -35.041 3.167   1.00 39.14 ? 878  HOH D O   1 
HETATM 19834 O  O   . HOH EA 7 .   ? 35.480  -3.213  -19.043 1.00 42.20 ? 879  HOH D O   1 
HETATM 19835 O  O   . HOH EA 7 .   ? 13.720  -32.030 -31.201 1.00 41.96 ? 880  HOH D O   1 
HETATM 19836 O  O   . HOH EA 7 .   ? -8.425  -24.774 1.846   1.00 51.78 ? 881  HOH D O   1 
HETATM 19837 O  O   . HOH EA 7 .   ? 28.143  -38.377 11.233  1.00 31.00 ? 882  HOH D O   1 
HETATM 19838 O  O   . HOH EA 7 .   ? 16.160  -36.404 -11.877 1.00 21.18 ? 883  HOH D O   1 
HETATM 19839 O  O   . HOH EA 7 .   ? 1.251   -32.235 -16.803 1.00 44.34 ? 884  HOH D O   1 
HETATM 19840 O  O   . HOH EA 7 .   ? 29.674  -38.808 -21.794 1.00 35.70 ? 885  HOH D O   1 
HETATM 19841 O  O   . HOH EA 7 .   ? 33.086  -0.167  -24.031 1.00 56.96 ? 886  HOH D O   1 
HETATM 19842 O  O   . HOH EA 7 .   ? -12.237 -13.758 8.475   1.00 43.99 ? 887  HOH D O   1 
HETATM 19843 O  O   . HOH EA 7 .   ? 0.572   -32.210 2.473   1.00 41.11 ? 888  HOH D O   1 
HETATM 19844 O  O   . HOH EA 7 .   ? 33.638  -44.197 -23.387 1.00 33.57 ? 889  HOH D O   1 
HETATM 19845 O  O   . HOH EA 7 .   ? 36.074  -33.231 -20.695 1.00 36.05 ? 890  HOH D O   1 
HETATM 19846 O  O   . HOH EA 7 .   ? -11.030 -16.120 7.767   1.00 32.86 ? 891  HOH D O   1 
HETATM 19847 O  O   . HOH EA 7 .   ? 9.658   -41.857 -5.677  1.00 48.24 ? 892  HOH D O   1 
HETATM 19848 O  O   . HOH EA 7 .   ? 5.325   -23.919 38.963  1.00 43.86 ? 893  HOH D O   1 
HETATM 19849 O  O   . HOH EA 7 .   ? -11.236 -18.667 4.846   1.00 51.44 ? 894  HOH D O   1 
HETATM 19850 O  O   . HOH EA 7 .   ? 0.131   -23.525 -17.292 1.00 54.80 ? 895  HOH D O   1 
HETATM 19851 O  O   . HOH EA 7 .   ? -6.059  -10.846 10.937  1.00 37.22 ? 896  HOH D O   1 
HETATM 19852 O  O   . HOH EA 7 .   ? 21.290  -10.253 -28.760 1.00 47.01 ? 897  HOH D O   1 
HETATM 19853 O  O   . HOH EA 7 .   ? 33.324  -38.993 -4.019  1.00 24.33 ? 898  HOH D O   1 
HETATM 19854 O  O   . HOH EA 7 .   ? 4.314   -27.109 11.849  1.00 50.22 ? 899  HOH D O   1 
HETATM 19855 O  O   . HOH EA 7 .   ? -2.660  -21.196 -14.885 1.00 53.73 ? 900  HOH D O   1 
HETATM 19856 O  O   . HOH EA 7 .   ? 1.099   -27.193 6.265   1.00 38.69 ? 901  HOH D O   1 
HETATM 19857 O  O   . HOH EA 7 .   ? 34.961  -36.343 -45.436 1.00 56.54 ? 902  HOH D O   1 
HETATM 19858 O  O   . HOH EA 7 .   ? 36.342  -15.926 -22.621 1.00 27.58 ? 903  HOH D O   1 
HETATM 19859 O  O   . HOH EA 7 .   ? 17.112  -32.341 4.949   1.00 40.45 ? 904  HOH D O   1 
HETATM 19860 O  O   . HOH EA 7 .   ? 16.095  -1.298  -7.808  1.00 25.13 ? 905  HOH D O   1 
HETATM 19861 O  O   . HOH EA 7 .   ? 34.651  -40.859 -15.217 1.00 41.01 ? 906  HOH D O   1 
HETATM 19862 O  O   . HOH EA 7 .   ? 8.573   -29.746 -1.659  1.00 31.71 ? 907  HOH D O   1 
HETATM 19863 O  O   . HOH EA 7 .   ? -1.904  -16.139 -4.730  1.00 37.10 ? 908  HOH D O   1 
HETATM 19864 O  O   . HOH EA 7 .   ? 31.827  -1.632  -18.390 1.00 43.59 ? 909  HOH D O   1 
HETATM 19865 O  O   . HOH EA 7 .   ? 32.303  -27.717 -17.724 1.00 20.87 ? 910  HOH D O   1 
HETATM 19866 O  O   . HOH EA 7 .   ? 30.556  -48.769 -12.269 1.00 41.71 ? 911  HOH D O   1 
HETATM 19867 O  O   . HOH EA 7 .   ? 7.383   -19.093 2.586   1.00 23.73 ? 912  HOH D O   1 
HETATM 19868 O  O   . HOH EA 7 .   ? 17.362  -49.841 -17.029 1.00 37.30 ? 913  HOH D O   1 
HETATM 19869 O  O   . HOH EA 7 .   ? -4.643  -25.833 -4.164  1.00 38.65 ? 914  HOH D O   1 
HETATM 19870 O  O   . HOH EA 7 .   ? 20.528  -55.182 -24.655 1.00 44.90 ? 915  HOH D O   1 
HETATM 19871 O  O   . HOH EA 7 .   ? 40.406  -33.011 -12.760 1.00 41.06 ? 916  HOH D O   1 
HETATM 19872 O  O   . HOH EA 7 .   ? 28.260  -25.578 2.872   1.00 27.02 ? 917  HOH D O   1 
HETATM 19873 O  O   . HOH EA 7 .   ? 23.462  -20.334 9.163   1.00 43.64 ? 918  HOH D O   1 
HETATM 19874 O  O   . HOH EA 7 .   ? -6.907  -18.801 12.287  1.00 27.54 ? 919  HOH D O   1 
HETATM 19875 O  O   . HOH EA 7 .   ? 26.554  -32.505 -31.833 1.00 44.70 ? 920  HOH D O   1 
HETATM 19876 O  O   . HOH EA 7 .   ? 44.391  -10.422 -4.475  1.00 51.41 ? 921  HOH D O   1 
HETATM 19877 O  O   . HOH EA 7 .   ? 30.279  -23.308 -28.372 1.00 48.53 ? 922  HOH D O   1 
HETATM 19878 O  O   . HOH EA 7 .   ? 29.307  -48.581 5.731   1.00 52.85 ? 923  HOH D O   1 
HETATM 19879 O  O   . HOH EA 7 .   ? 21.257  -51.649 -39.846 1.00 45.62 ? 924  HOH D O   1 
HETATM 19880 O  O   . HOH EA 7 .   ? 9.741   -27.448 5.188   1.00 43.83 ? 925  HOH D O   1 
HETATM 19881 O  O   . HOH EA 7 .   ? 24.943  -29.626 -25.726 1.00 47.17 ? 926  HOH D O   1 
HETATM 19882 O  O   . HOH EA 7 .   ? 16.143  -19.769 -22.325 1.00 41.04 ? 927  HOH D O   1 
HETATM 19883 O  O   . HOH EA 7 .   ? 30.871  -0.671  -25.635 1.00 45.13 ? 928  HOH D O   1 
HETATM 19884 O  O   . HOH EA 7 .   ? 31.872  -49.064 -18.805 1.00 32.81 ? 929  HOH D O   1 
HETATM 19885 O  O   . HOH EA 7 .   ? 29.668  -20.179 5.509   1.00 45.65 ? 930  HOH D O   1 
HETATM 19886 O  O   . HOH EA 7 .   ? 33.739  -31.479 -31.883 1.00 49.13 ? 931  HOH D O   1 
HETATM 19887 O  O   . HOH EA 7 .   ? -1.844  -14.610 -7.107  1.00 46.29 ? 932  HOH D O   1 
HETATM 19888 O  O   . HOH EA 7 .   ? 20.752  -24.015 5.396   1.00 40.57 ? 933  HOH D O   1 
HETATM 19889 O  O   . HOH EA 7 .   ? 2.169   -14.547 0.559   1.00 23.36 ? 934  HOH D O   1 
HETATM 19890 O  O   . HOH EA 7 .   ? 39.204  -20.198 3.740   1.00 58.06 ? 935  HOH D O   1 
HETATM 19891 O  O   . HOH EA 7 .   ? -6.956  -15.701 19.143  1.00 30.54 ? 936  HOH D O   1 
HETATM 19892 O  O   . HOH EA 7 .   ? 10.626  -34.137 -5.362  1.00 49.83 ? 937  HOH D O   1 
HETATM 19893 O  O   . HOH EA 7 .   ? 37.270  -18.262 -23.553 1.00 33.56 ? 938  HOH D O   1 
HETATM 19894 O  O   . HOH EA 7 .   ? 11.018  -21.666 2.826   1.00 34.68 ? 939  HOH D O   1 
HETATM 19895 O  O   . HOH EA 7 .   ? 42.239  -33.504 -23.137 1.00 56.75 ? 940  HOH D O   1 
HETATM 19896 O  O   . HOH EA 7 .   ? 10.559  -4.358  -23.416 1.00 57.28 ? 941  HOH D O   1 
HETATM 19897 O  O   . HOH EA 7 .   ? 18.009  -4.270  -19.275 1.00 31.28 ? 942  HOH D O   1 
HETATM 19898 O  O   . HOH EA 7 .   ? 24.370  -49.572 6.469   1.00 45.42 ? 943  HOH D O   1 
HETATM 19899 O  O   . HOH EA 7 .   ? 36.533  -4.825  -25.864 1.00 34.49 ? 944  HOH D O   1 
HETATM 19900 O  O   . HOH EA 7 .   ? 20.264  -34.246 -45.101 1.00 47.22 ? 945  HOH D O   1 
HETATM 19901 O  O   . HOH EA 7 .   ? 34.197  -43.645 1.499   1.00 34.50 ? 946  HOH D O   1 
HETATM 19902 O  O   . HOH EA 7 .   ? 6.623   -22.208 7.009   1.00 32.08 ? 947  HOH D O   1 
HETATM 19903 O  O   . HOH EA 7 .   ? 23.878  -57.940 -22.226 1.00 36.59 ? 948  HOH D O   1 
HETATM 19904 O  O   . HOH EA 7 .   ? 30.826  -29.018 2.903   1.00 37.30 ? 949  HOH D O   1 
HETATM 19905 O  O   . HOH EA 7 .   ? 15.995  -48.668 -0.291  1.00 51.70 ? 950  HOH D O   1 
HETATM 19906 O  O   . HOH EA 7 .   ? 17.865  -46.302 6.580   1.00 46.81 ? 951  HOH D O   1 
HETATM 19907 O  O   . HOH EA 7 .   ? 22.571  -22.935 -28.536 1.00 49.00 ? 952  HOH D O   1 
HETATM 19908 O  O   . HOH EA 7 .   ? 26.685  -50.187 -0.028  1.00 41.51 ? 953  HOH D O   1 
HETATM 19909 O  O   . HOH EA 7 .   ? 16.684  -19.881 -7.946  1.00 33.01 ? 954  HOH D O   1 
HETATM 19910 O  O   . HOH EA 7 .   ? 34.761  -43.822 -26.243 1.00 41.14 ? 955  HOH D O   1 
HETATM 19911 O  O   . HOH EA 7 .   ? 6.069   -30.914 -0.261  1.00 35.81 ? 956  HOH D O   1 
HETATM 19912 O  O   . HOH EA 7 .   ? 42.153  -14.428 -10.978 1.00 33.50 ? 957  HOH D O   1 
HETATM 19913 O  O   . HOH EA 7 .   ? 14.792  -46.190 -7.103  1.00 41.38 ? 958  HOH D O   1 
HETATM 19914 O  O   . HOH EA 7 .   ? 18.246  -49.385 0.207   1.00 37.62 ? 959  HOH D O   1 
HETATM 19915 O  O   . HOH EA 7 .   ? 4.547   -11.434 -8.706  1.00 41.63 ? 960  HOH D O   1 
HETATM 19916 O  O   . HOH EA 7 .   ? 47.280  -14.857 -21.942 1.00 39.22 ? 961  HOH D O   1 
HETATM 19917 O  O   . HOH EA 7 .   ? 18.201  -21.443 -22.716 1.00 35.74 ? 962  HOH D O   1 
HETATM 19918 O  O   . HOH EA 7 .   ? 27.629  -12.157 4.465   1.00 45.11 ? 963  HOH D O   1 
HETATM 19919 O  O   . HOH EA 7 .   ? 43.839  -7.854  -8.486  1.00 47.19 ? 964  HOH D O   1 
HETATM 19920 O  O   . HOH EA 7 .   ? 35.259  -37.637 -11.935 1.00 53.62 ? 965  HOH D O   1 
HETATM 19921 O  O   . HOH EA 7 .   ? 5.786   -5.938  8.699   1.00 43.79 ? 966  HOH D O   1 
HETATM 19922 O  O   . HOH EA 7 .   ? 24.298  -50.837 -24.677 1.00 43.98 ? 967  HOH D O   1 
HETATM 19923 O  O   . HOH EA 7 .   ? 0.347   -20.421 34.462  1.00 33.87 ? 968  HOH D O   1 
HETATM 19924 O  O   . HOH EA 7 .   ? 17.163  -50.423 -6.161  1.00 51.24 ? 969  HOH D O   1 
HETATM 19925 O  O   . HOH EA 7 .   ? -9.580  -12.016 -6.587  1.00 41.04 ? 970  HOH D O   1 
HETATM 19926 O  O   . HOH EA 7 .   ? -1.996  -24.993 29.423  1.00 43.54 ? 971  HOH D O   1 
HETATM 19927 O  O   . HOH EA 7 .   ? 34.433  -21.999 -25.290 1.00 38.53 ? 972  HOH D O   1 
HETATM 19928 O  O   . HOH EA 7 .   ? 7.487   -20.872 21.534  1.00 28.98 ? 973  HOH D O   1 
HETATM 19929 O  O   . HOH EA 7 .   ? -5.838  -19.103 14.925  1.00 30.22 ? 974  HOH D O   1 
HETATM 19930 O  O   . HOH EA 7 .   ? 14.275  -26.966 -41.605 1.00 50.24 ? 975  HOH D O   1 
HETATM 19931 O  O   . HOH EA 7 .   ? 5.535   -51.767 -42.438 1.00 48.42 ? 976  HOH D O   1 
HETATM 19932 O  O   . HOH EA 7 .   ? 12.009  -6.800  -11.955 1.00 48.37 ? 977  HOH D O   1 
HETATM 19933 O  O   . HOH EA 7 .   ? 28.335  -46.811 8.516   1.00 37.52 ? 978  HOH D O   1 
HETATM 19934 O  O   . HOH EA 7 .   ? 45.240  -19.785 -11.597 1.00 44.38 ? 979  HOH D O   1 
HETATM 19935 O  O   . HOH EA 7 .   ? 39.599  -52.190 -26.696 1.00 54.20 ? 980  HOH D O   1 
HETATM 19936 O  O   . HOH EA 7 .   ? -1.777  -24.240 4.453   1.00 26.20 ? 981  HOH D O   1 
HETATM 19937 O  O   . HOH EA 7 .   ? 35.667  -11.095 2.949   1.00 54.40 ? 982  HOH D O   1 
HETATM 19938 O  O   . HOH EA 7 .   ? 30.960  -44.946 -0.031  1.00 31.17 ? 983  HOH D O   1 
HETATM 19939 O  O   . HOH EA 7 .   ? 31.874  -10.629 -32.149 1.00 53.49 ? 984  HOH D O   1 
HETATM 19940 O  O   . HOH EA 7 .   ? 27.432  -9.734  -32.391 1.00 38.37 ? 985  HOH D O   1 
HETATM 19941 O  O   . HOH EA 7 .   ? 16.781  -30.570 -22.357 1.00 36.87 ? 986  HOH D O   1 
HETATM 19942 O  O   . HOH EA 7 .   ? 8.503   -37.350 -22.376 1.00 50.33 ? 987  HOH D O   1 
HETATM 19943 O  O   . HOH EA 7 .   ? 36.097  -12.277 -31.551 1.00 63.20 ? 988  HOH D O   1 
HETATM 19944 O  O   . HOH EA 7 .   ? 16.170  -16.853 6.242   1.00 45.69 ? 989  HOH D O   1 
HETATM 19945 O  O   . HOH EA 7 .   ? 1.452   -48.147 -29.885 1.00 61.97 ? 990  HOH D O   1 
HETATM 19946 O  O   . HOH EA 7 .   ? 6.542   -20.131 5.183   1.00 27.32 ? 991  HOH D O   1 
HETATM 19947 O  O   . HOH EA 7 .   ? -2.131  -20.785 22.089  1.00 36.85 ? 992  HOH D O   1 
HETATM 19948 O  O   . HOH EA 7 .   ? 10.297  -46.280 -0.410  1.00 50.94 ? 993  HOH D O   1 
HETATM 19949 O  O   . HOH EA 7 .   ? 8.542   -11.280 13.048  1.00 39.06 ? 994  HOH D O   1 
HETATM 19950 O  O   . HOH EA 7 .   ? 5.711   -36.887 -9.168  1.00 27.63 ? 995  HOH D O   1 
HETATM 19951 O  O   . HOH EA 7 .   ? 2.463   -31.120 -14.580 1.00 34.75 ? 996  HOH D O   1 
HETATM 19952 O  O   . HOH EA 7 .   ? 20.295  -47.181 8.933   1.00 36.68 ? 997  HOH D O   1 
HETATM 19953 O  O   . HOH EA 7 .   ? 10.491  -2.647  12.772  1.00 54.81 ? 998  HOH D O   1 
HETATM 19954 O  O   . HOH EA 7 .   ? 12.796  -26.598 -19.282 1.00 57.11 ? 999  HOH D O   1 
HETATM 19955 O  O   . HOH EA 7 .   ? 0.226   -23.553 9.246   1.00 56.49 ? 1000 HOH D O   1 
HETATM 19956 O  O   . HOH EA 7 .   ? 8.470   -35.093 1.577   1.00 49.22 ? 1001 HOH D O   1 
HETATM 19957 O  O   . HOH EA 7 .   ? 12.846  -10.071 -14.009 1.00 56.36 ? 1002 HOH D O   1 
HETATM 19958 O  O   . HOH EA 7 .   ? 38.949  -35.562 -2.384  1.00 43.54 ? 1003 HOH D O   1 
HETATM 19959 O  O   . HOH EA 7 .   ? 32.538  -36.949 -20.250 1.00 43.32 ? 1004 HOH D O   1 
HETATM 19960 O  O   . HOH EA 7 .   ? 39.601  -35.578 -15.924 1.00 46.98 ? 1005 HOH D O   1 
HETATM 19961 O  O   . HOH EA 7 .   ? 22.376  -21.888 3.772   1.00 28.98 ? 1006 HOH D O   1 
HETATM 19962 O  O   . HOH EA 7 .   ? 6.730   -42.231 -14.193 1.00 44.63 ? 1007 HOH D O   1 
HETATM 19963 O  O   . HOH EA 7 .   ? 11.418  -29.388 4.759   1.00 33.29 ? 1008 HOH D O   1 
HETATM 19964 O  O   . HOH EA 7 .   ? 2.677   -27.648 22.643  1.00 59.50 ? 1009 HOH D O   1 
HETATM 19965 O  O   . HOH EA 7 .   ? 31.068  -47.852 -16.375 1.00 45.16 ? 1010 HOH D O   1 
HETATM 19966 O  O   . HOH EA 7 .   ? 5.604   -36.154 -20.890 1.00 45.54 ? 1011 HOH D O   1 
HETATM 19967 O  O   . HOH EA 7 .   ? 22.025  -22.294 10.009  1.00 42.62 ? 1012 HOH D O   1 
HETATM 19968 O  O   . HOH EA 7 .   ? -2.798  -29.138 -5.398  1.00 50.14 ? 1013 HOH D O   1 
HETATM 19969 O  O   . HOH EA 7 .   ? 14.224  -50.397 -9.801  1.00 55.52 ? 1014 HOH D O   1 
HETATM 19970 O  O   . HOH EA 7 .   ? 41.133  -11.190 -24.870 1.00 47.90 ? 1015 HOH D O   1 
HETATM 19971 O  O   . HOH EA 7 .   ? -12.513 -16.338 -9.697  1.00 50.67 ? 1016 HOH D O   1 
HETATM 19972 O  O   . HOH EA 7 .   ? 37.743  -52.307 -22.895 1.00 46.39 ? 1017 HOH D O   1 
HETATM 19973 O  O   . HOH EA 7 .   ? 21.291  0.701   -28.681 1.00 56.34 ? 1018 HOH D O   1 
HETATM 19974 O  O   . HOH EA 7 .   ? 4.555   -9.407  19.048  1.00 47.10 ? 1019 HOH D O   1 
HETATM 19975 O  O   . HOH EA 7 .   ? 0.745   -25.773 3.748   1.00 25.11 ? 1020 HOH D O   1 
HETATM 19976 O  O   . HOH EA 7 .   ? 4.421   -33.162 -0.382  1.00 45.83 ? 1021 HOH D O   1 
HETATM 19977 O  O   . HOH EA 7 .   ? 4.396   -24.029 -21.516 1.00 47.79 ? 1022 HOH D O   1 
HETATM 19978 O  O   . HOH EA 7 .   ? 19.652  -5.464  -26.824 1.00 55.37 ? 1023 HOH D O   1 
HETATM 19979 O  O   . HOH EA 7 .   ? -3.160  -25.975 2.271   1.00 36.11 ? 1024 HOH D O   1 
HETATM 19980 O  O   . HOH EA 7 .   ? 22.635  -34.390 -45.587 1.00 51.24 ? 1025 HOH D O   1 
HETATM 19981 O  O   . HOH EA 7 .   ? 44.352  -18.282 -23.074 1.00 57.72 ? 1026 HOH D O   1 
HETATM 19982 O  O   . HOH EA 7 .   ? 28.314  -32.796 -46.882 1.00 57.86 ? 1027 HOH D O   1 
HETATM 19983 O  O   . HOH EA 7 .   ? 17.965  -28.390 -18.816 1.00 43.33 ? 1028 HOH D O   1 
HETATM 19984 O  O   . HOH EA 7 .   ? 36.369  -35.367 -19.012 1.00 37.93 ? 1029 HOH D O   1 
HETATM 19985 O  O   . HOH EA 7 .   ? 42.621  -26.275 -20.030 1.00 53.65 ? 1030 HOH D O   1 
HETATM 19986 O  O   . HOH EA 7 .   ? 39.990  -17.577 -4.098  1.00 43.43 ? 1031 HOH D O   1 
HETATM 19987 O  O   . HOH EA 7 .   ? 28.221  -26.804 11.804  1.00 57.07 ? 1032 HOH D O   1 
HETATM 19988 O  O   . HOH EA 7 .   ? -1.056  -20.874 -22.542 1.00 54.60 ? 1033 HOH D O   1 
HETATM 19989 O  O   . HOH EA 7 .   ? 39.455  -9.172  -25.519 1.00 45.89 ? 1034 HOH D O   1 
HETATM 19990 O  O   . HOH EA 7 .   ? 6.514   -23.029 16.937  1.00 58.49 ? 1035 HOH D O   1 
HETATM 19991 O  O   . HOH EA 7 .   ? 0.398   -30.047 -17.975 1.00 49.03 ? 1036 HOH D O   1 
HETATM 19992 O  O   . HOH EA 7 .   ? 42.025  -48.368 -39.884 1.00 56.88 ? 1037 HOH D O   1 
HETATM 19993 O  O   . HOH EA 7 .   ? 23.264  -28.191 -24.407 1.00 50.07 ? 1038 HOH D O   1 
HETATM 19994 O  O   . HOH EA 7 .   ? 7.266   -49.713 -29.297 1.00 47.45 ? 1039 HOH D O   1 
HETATM 19995 O  O   . HOH EA 7 .   ? 15.877  -43.478 -49.749 1.00 45.43 ? 1040 HOH D O   1 
HETATM 19996 O  O   . HOH EA 7 .   ? 28.163  -31.914 5.847   1.00 54.31 ? 1041 HOH D O   1 
HETATM 19997 O  O   . HOH EA 7 .   ? 29.994  -50.734 -10.575 1.00 54.19 ? 1042 HOH D O   1 
HETATM 19998 O  O   . HOH EA 7 .   ? 1.371   -27.799 31.219  1.00 38.34 ? 1043 HOH D O   1 
HETATM 19999 O  O   . HOH EA 7 .   ? -0.340  -27.265 1.788   1.00 43.14 ? 1044 HOH D O   1 
HETATM 20000 O  O   . HOH EA 7 .   ? 31.139  -40.894 -21.178 1.00 46.26 ? 1045 HOH D O   1 
HETATM 20001 O  O   . HOH EA 7 .   ? 29.756  -50.760 0.310   1.00 52.39 ? 1046 HOH D O   1 
HETATM 20002 O  O   . HOH EA 7 .   ? 38.281  -32.559 -3.243  1.00 35.59 ? 1047 HOH D O   1 
HETATM 20003 O  O   . HOH EA 7 .   ? 3.917   -28.549 9.351   1.00 55.51 ? 1048 HOH D O   1 
HETATM 20004 O  O   . HOH EA 7 .   ? 33.306  -28.299 -15.096 1.00 35.01 ? 1049 HOH D O   1 
HETATM 20005 O  O   . HOH EA 7 .   ? 14.967  -22.944 2.380   1.00 46.66 ? 1050 HOH D O   1 
HETATM 20006 O  O   . HOH EA 7 .   ? 2.623   -4.849  -5.351  1.00 51.73 ? 1051 HOH D O   1 
HETATM 20007 O  O   . HOH EA 7 .   ? 21.898  -52.828 -22.087 1.00 52.04 ? 1052 HOH D O   1 
HETATM 20008 O  O   . HOH EA 7 .   ? 31.689  -10.257 4.235   1.00 47.33 ? 1053 HOH D O   1 
HETATM 20009 O  O   . HOH EA 7 .   ? 36.344  -43.997 0.278   1.00 47.37 ? 1054 HOH D O   1 
HETATM 20010 O  O   . HOH EA 7 .   ? 10.965  -45.168 1.736   1.00 47.10 ? 1055 HOH D O   1 
HETATM 20011 O  O   . HOH EA 7 .   ? 37.854  -49.554 -21.443 1.00 60.05 ? 1056 HOH D O   1 
HETATM 20012 O  O   . HOH EA 7 .   ? 42.918  -19.297 -7.392  1.00 35.26 ? 1057 HOH D O   1 
HETATM 20013 O  O   . HOH EA 7 .   ? 38.994  -37.775 -0.527  1.00 57.73 ? 1058 HOH D O   1 
HETATM 20014 O  O   . HOH EA 7 .   ? 43.486  -6.966  -19.607 1.00 49.80 ? 1059 HOH D O   1 
HETATM 20015 O  O   . HOH EA 7 .   ? -0.317  -30.507 -3.966  1.00 49.35 ? 1060 HOH D O   1 
HETATM 20016 O  O   . HOH EA 7 .   ? 14.727  -46.132 -49.221 1.00 51.17 ? 1061 HOH D O   1 
HETATM 20017 O  O   . HOH EA 7 .   ? 24.288  -49.965 -6.917  1.00 41.25 ? 1062 HOH D O   1 
HETATM 20018 O  O   . HOH EA 7 .   ? 0.852   -24.253 20.977  1.00 41.67 ? 1063 HOH D O   1 
HETATM 20019 O  O   . HOH EA 7 .   ? 28.553  -23.823 -30.087 1.00 43.73 ? 1064 HOH D O   1 
HETATM 20020 O  O   . HOH EA 7 .   ? -4.787  -21.487 15.374  1.00 46.63 ? 1065 HOH D O   1 
HETATM 20021 O  O   . HOH EA 7 .   ? 39.898  -6.881  -21.868 1.00 47.37 ? 1066 HOH D O   1 
HETATM 20022 O  O   . HOH EA 7 .   ? 47.261  -13.412 -16.422 1.00 58.21 ? 1067 HOH D O   1 
HETATM 20023 O  O   . HOH EA 7 .   ? -2.518  -26.707 -11.116 1.00 64.03 ? 1068 HOH D O   1 
HETATM 20024 O  O   . HOH EA 7 .   ? 10.529  -33.154 -3.092  1.00 52.91 ? 1069 HOH D O   1 
HETATM 20025 O  O   . HOH EA 7 .   ? 8.953   -21.567 8.197   1.00 49.91 ? 1070 HOH D O   1 
HETATM 20026 O  O   . HOH EA 7 .   ? 10.282  -47.320 -10.410 1.00 52.16 ? 1071 HOH D O   1 
HETATM 20027 O  O   . HOH EA 7 .   ? 32.788  -2.297  -26.294 1.00 47.72 ? 1072 HOH D O   1 
HETATM 20028 O  O   . HOH EA 7 .   ? 42.094  -9.074  -22.859 1.00 51.86 ? 1073 HOH D O   1 
HETATM 20029 O  O   . HOH EA 7 .   ? 12.131  -28.736 -17.579 1.00 54.44 ? 1074 HOH D O   1 
HETATM 20030 O  O   . HOH EA 7 .   ? -3.914  -26.694 -8.849  1.00 52.75 ? 1075 HOH D O   1 
HETATM 20031 O  O   . HOH EA 7 .   ? 34.629  -40.970 -8.762  1.00 41.34 ? 1076 HOH D O   1 
HETATM 20032 O  O   . HOH EA 7 .   ? -0.365  -30.418 -1.308  1.00 47.04 ? 1077 HOH D O   1 
HETATM 20033 O  O   . HOH EA 7 .   ? 43.310  -22.372 -7.283  1.00 44.47 ? 1078 HOH D O   1 
HETATM 20034 O  O   . HOH EA 7 .   ? 19.404  -29.173 -23.502 1.00 57.92 ? 1079 HOH D O   1 
HETATM 20035 O  O   . HOH EA 7 .   ? 21.844  -52.119 -5.086  1.00 41.90 ? 1080 HOH D O   1 
HETATM 20036 O  O   . HOH EA 7 .   ? 44.115  -15.548 -9.546  1.00 54.93 ? 1081 HOH D O   1 
HETATM 20037 O  O   . HOH EA 7 .   ? 6.988   -35.019 -22.906 1.00 50.12 ? 1082 HOH D O   1 
HETATM 20038 O  O   . HOH EA 7 .   ? 13.400  -46.769 -9.363  1.00 45.72 ? 1083 HOH D O   1 
HETATM 20039 O  O   . HOH EA 7 .   ? 2.746   -22.116 -21.390 1.00 61.14 ? 1084 HOH D O   1 
HETATM 20040 O  O   . HOH EA 7 .   ? 43.468  -30.153 -17.718 1.00 48.96 ? 1085 HOH D O   1 
HETATM 20041 O  O   . HOH EA 7 .   ? 4.188   -32.002 -2.687  1.00 45.82 ? 1086 HOH D O   1 
HETATM 20042 O  O   . HOH EA 7 .   ? 17.750  -20.809 -5.818  1.00 44.46 ? 1087 HOH D O   1 
HETATM 20043 O  O   . HOH EA 7 .   ? 12.902  -26.956 6.320   1.00 56.59 ? 1088 HOH D O   1 
HETATM 20044 O  O   . HOH EA 7 .   ? -0.372  -18.793 32.252  1.00 38.49 ? 1089 HOH D O   1 
HETATM 20045 O  O   . HOH EA 7 .   ? -1.007  -23.793 11.600  1.00 44.50 ? 1090 HOH D O   1 
HETATM 20046 O  O   . HOH EA 7 .   ? 14.226  -55.528 -35.098 1.00 49.22 ? 1091 HOH D O   1 
HETATM 20047 O  O   . HOH EA 7 .   ? 5.946   -21.598 39.647  1.00 40.56 ? 1092 HOH D O   1 
HETATM 20048 O  O   . HOH EA 7 .   ? 25.512  -11.864 5.904   1.00 47.85 ? 1093 HOH D O   1 
HETATM 20049 O  O   . HOH EA 7 .   ? 41.701  -30.163 -22.090 1.00 40.81 ? 1094 HOH D O   1 
HETATM 20050 O  O   . HOH EA 7 .   ? 35.674  -39.950 -4.234  1.00 34.24 ? 1095 HOH D O   1 
HETATM 20051 O  O   . HOH EA 7 .   ? -11.150 -20.466 8.746   1.00 53.61 ? 1096 HOH D O   1 
HETATM 20052 O  O   . HOH EA 7 .   ? -0.766  -34.000 -16.355 1.00 47.67 ? 1097 HOH D O   1 
HETATM 20053 O  O   . HOH EA 7 .   ? -13.047 -16.960 5.762   1.00 43.73 ? 1098 HOH D O   1 
HETATM 20054 O  O   . HOH EA 7 .   ? 9.976   -43.009 3.357   1.00 47.34 ? 1099 HOH D O   1 
HETATM 20055 O  O   . HOH EA 7 .   ? 19.315  -50.873 -18.252 1.00 49.41 ? 1100 HOH D O   1 
HETATM 20056 O  O   . HOH EA 7 .   ? -11.329 -18.044 10.046  1.00 52.00 ? 1101 HOH D O   1 
HETATM 20057 O  O   . HOH EA 7 .   ? -9.810  -18.104 12.528  1.00 39.46 ? 1102 HOH D O   1 
HETATM 20058 O  O   . HOH EA 7 .   ? 14.500  -20.289 7.285   1.00 59.68 ? 1103 HOH D O   1 
HETATM 20059 O  O   . HOH EA 7 .   ? -6.737  -21.225 10.682  1.00 36.85 ? 1104 HOH D O   1 
HETATM 20060 O  O   . HOH EA 7 .   ? 46.118  -4.602  -6.736  1.00 47.39 ? 1105 HOH D O   1 
# 
